data_9GFW
# 
_entry.id   9GFW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   9GFW         pdb_00009gfw 10.2210/pdb9gfw/pdb 
WWPDB D_1292140924 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-11-13 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GFW 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              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 0000-0002-0162-1656 
'De Simone, G.' 2 0000-0001-9783-5431 
'Esposito, D.'  3 0000-0002-0759-5778 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            282 
_citation.language                  ? 
_citation.page_first                136873 
_citation.page_last                 136873 
_citation.title                     'Exploring the binding mode of phenyl and vinyl boronic acids to human carbonic anhydrases.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2024.136873 
_citation.pdbx_database_id_PubMed   39454912 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Esposito, D.'  1 ? 
primary 'Monti, S.M.'   2 ? 
primary 'Supuran, C.T.' 3 ? 
primary 'Winum, J.Y.'   4 ? 
primary 'De Simone, G.' 5 ? 
primary 'Alterio, V.'   6 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                 29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                             65.409    1   ?       ? ? ? 
3 non-polymer syn '(4-methylphenyl)-tris(oxidanyl)boron' 152.963   1   ?       ? ? ? 
4 non-polymer syn GLYCEROL                               92.094    1   ?       ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                   78.133    1   ?       ? ? ? 
6 non-polymer syn 'MERCURIBENZOIC ACID'                  321.703   1   ?       ? ? ? 
7 water       nat water                                  18.015    209 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                             ZN    
3 '(4-methylphenyl)-tris(oxidanyl)boron' A1IKU 
4 GLYCEROL                               GOL   
5 'DIMETHYL SULFOXIDE'                   DMS   
6 'MERCURIBENZOIC ACID'                  MBO   
7 water                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ERYTHROCYTES 
_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 
A1IKU non-polymer         . '(4-methylphenyl)-tris(oxidanyl)boron' ?                               'C7 H10 B O3'    152.963 
ALA   'L-peptide linking' y ALANINE                                ?                               'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                               ?                               'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                             ?                               'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                        ?                               'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                               ?                               'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                   ?                               'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                              ?                               'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                        ?                               'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                ?                               'C2 H5 N O2'     75.067  
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 
MBO   non-polymer         . 'MERCURIBENZOIC ACID'                  ?                               'C7 H5 Hg O2'    321.703 
MET   'L-peptide linking' y METHIONINE                             ?                               'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                          ?                               'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                ?                               'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                 ?                               'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                              ?                               'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                             ?                               'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                               ?                               'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                 ?                               'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                             ?                               'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IKU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IKU 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN    1   301 262  ZN    ZN  A . 
C 3 A1IKU 1   302 300  A1IKU JY5 A . 
D 4 GOL   1   303 311  GOL   GOL A . 
E 5 DMS   1   304 400  DMS   DMS A . 
F 6 MBO   1   305 1206 MBO   MBO A . 
G 7 HOH   1   401 203  HOH   HOH A . 
G 7 HOH   2   402 140  HOH   HOH A . 
G 7 HOH   3   403 137  HOH   HOH A . 
G 7 HOH   4   404 184  HOH   HOH A . 
G 7 HOH   5   405 51   HOH   HOH A . 
G 7 HOH   6   406 58   HOH   HOH A . 
G 7 HOH   7   407 189  HOH   HOH A . 
G 7 HOH   8   408 204  HOH   HOH A . 
G 7 HOH   9   409 16   HOH   HOH A . 
G 7 HOH   10  410 135  HOH   HOH A . 
G 7 HOH   11  411 24   HOH   HOH A . 
G 7 HOH   12  412 74   HOH   HOH A . 
G 7 HOH   13  413 153  HOH   HOH A . 
G 7 HOH   14  414 2    HOH   HOH A . 
G 7 HOH   15  415 38   HOH   HOH A . 
G 7 HOH   16  416 41   HOH   HOH A . 
G 7 HOH   17  417 111  HOH   HOH A . 
G 7 HOH   18  418 179  HOH   HOH A . 
G 7 HOH   19  419 26   HOH   HOH A . 
G 7 HOH   20  420 104  HOH   HOH A . 
G 7 HOH   21  421 123  HOH   HOH A . 
G 7 HOH   22  422 103  HOH   HOH A . 
G 7 HOH   23  423 13   HOH   HOH A . 
G 7 HOH   24  424 169  HOH   HOH A . 
G 7 HOH   25  425 18   HOH   HOH A . 
G 7 HOH   26  426 30   HOH   HOH A . 
G 7 HOH   27  427 173  HOH   HOH A . 
G 7 HOH   28  428 66   HOH   HOH A . 
G 7 HOH   29  429 158  HOH   HOH A . 
G 7 HOH   30  430 166  HOH   HOH A . 
G 7 HOH   31  431 152  HOH   HOH A . 
G 7 HOH   32  432 102  HOH   HOH A . 
G 7 HOH   33  433 59   HOH   HOH A . 
G 7 HOH   34  434 39   HOH   HOH A . 
G 7 HOH   35  435 160  HOH   HOH A . 
G 7 HOH   36  436 139  HOH   HOH A . 
G 7 HOH   37  437 77   HOH   HOH A . 
G 7 HOH   38  438 142  HOH   HOH A . 
G 7 HOH   39  439 98   HOH   HOH A . 
G 7 HOH   40  440 127  HOH   HOH A . 
G 7 HOH   41  441 147  HOH   HOH A . 
G 7 HOH   42  442 23   HOH   HOH A . 
G 7 HOH   43  443 63   HOH   HOH A . 
G 7 HOH   44  444 134  HOH   HOH A . 
G 7 HOH   45  445 6    HOH   HOH A . 
G 7 HOH   46  446 116  HOH   HOH A . 
G 7 HOH   47  447 10   HOH   HOH A . 
G 7 HOH   48  448 126  HOH   HOH A . 
G 7 HOH   49  449 188  HOH   HOH A . 
G 7 HOH   50  450 105  HOH   HOH A . 
G 7 HOH   51  451 149  HOH   HOH A . 
G 7 HOH   52  452 9    HOH   HOH A . 
G 7 HOH   53  453 72   HOH   HOH A . 
G 7 HOH   54  454 144  HOH   HOH A . 
G 7 HOH   55  455 36   HOH   HOH A . 
G 7 HOH   56  456 42   HOH   HOH A . 
G 7 HOH   57  457 22   HOH   HOH A . 
G 7 HOH   58  458 52   HOH   HOH A . 
G 7 HOH   59  459 5    HOH   HOH A . 
G 7 HOH   60  460 155  HOH   HOH A . 
G 7 HOH   61  461 122  HOH   HOH A . 
G 7 HOH   62  462 97   HOH   HOH A . 
G 7 HOH   63  463 186  HOH   HOH A . 
G 7 HOH   64  464 96   HOH   HOH A . 
G 7 HOH   65  465 4    HOH   HOH A . 
G 7 HOH   66  466 143  HOH   HOH A . 
G 7 HOH   67  467 121  HOH   HOH A . 
G 7 HOH   68  468 172  HOH   HOH A . 
G 7 HOH   69  469 94   HOH   HOH A . 
G 7 HOH   70  470 3    HOH   HOH A . 
G 7 HOH   71  471 118  HOH   HOH A . 
G 7 HOH   72  472 37   HOH   HOH A . 
G 7 HOH   73  473 1    HOH   HOH A . 
G 7 HOH   74  474 174  HOH   HOH A . 
G 7 HOH   75  475 84   HOH   HOH A . 
G 7 HOH   76  476 35   HOH   HOH A . 
G 7 HOH   77  477 78   HOH   HOH A . 
G 7 HOH   78  478 205  HOH   HOH A . 
G 7 HOH   79  479 112  HOH   HOH A . 
G 7 HOH   80  480 136  HOH   HOH A . 
G 7 HOH   81  481 207  HOH   HOH A . 
G 7 HOH   82  482 70   HOH   HOH A . 
G 7 HOH   83  483 50   HOH   HOH A . 
G 7 HOH   84  484 56   HOH   HOH A . 
G 7 HOH   85  485 11   HOH   HOH A . 
G 7 HOH   86  486 14   HOH   HOH A . 
G 7 HOH   87  487 27   HOH   HOH A . 
G 7 HOH   88  488 19   HOH   HOH A . 
G 7 HOH   89  489 120  HOH   HOH A . 
G 7 HOH   90  490 187  HOH   HOH A . 
G 7 HOH   91  491 21   HOH   HOH A . 
G 7 HOH   92  492 65   HOH   HOH A . 
G 7 HOH   93  493 43   HOH   HOH A . 
G 7 HOH   94  494 17   HOH   HOH A . 
G 7 HOH   95  495 201  HOH   HOH A . 
G 7 HOH   96  496 86   HOH   HOH A . 
G 7 HOH   97  497 181  HOH   HOH A . 
G 7 HOH   98  498 190  HOH   HOH A . 
G 7 HOH   99  499 145  HOH   HOH A . 
G 7 HOH   100 500 115  HOH   HOH A . 
G 7 HOH   101 501 48   HOH   HOH A . 
G 7 HOH   102 502 46   HOH   HOH A . 
G 7 HOH   103 503 130  HOH   HOH A . 
G 7 HOH   104 504 28   HOH   HOH A . 
G 7 HOH   105 505 107  HOH   HOH A . 
G 7 HOH   106 506 198  HOH   HOH A . 
G 7 HOH   107 507 161  HOH   HOH A . 
G 7 HOH   108 508 150  HOH   HOH A . 
G 7 HOH   109 509 15   HOH   HOH A . 
G 7 HOH   110 510 125  HOH   HOH A . 
G 7 HOH   111 511 114  HOH   HOH A . 
G 7 HOH   112 512 20   HOH   HOH A . 
G 7 HOH   113 513 40   HOH   HOH A . 
G 7 HOH   114 514 44   HOH   HOH A . 
G 7 HOH   115 515 32   HOH   HOH A . 
G 7 HOH   116 516 209  HOH   HOH A . 
G 7 HOH   117 517 79   HOH   HOH A . 
G 7 HOH   118 518 81   HOH   HOH A . 
G 7 HOH   119 519 71   HOH   HOH A . 
G 7 HOH   120 520 106  HOH   HOH A . 
G 7 HOH   121 521 128  HOH   HOH A . 
G 7 HOH   122 522 138  HOH   HOH A . 
G 7 HOH   123 523 55   HOH   HOH A . 
G 7 HOH   124 524 146  HOH   HOH A . 
G 7 HOH   125 525 80   HOH   HOH A . 
G 7 HOH   126 526 175  HOH   HOH A . 
G 7 HOH   127 527 151  HOH   HOH A . 
G 7 HOH   128 528 7    HOH   HOH A . 
G 7 HOH   129 529 85   HOH   HOH A . 
G 7 HOH   130 530 133  HOH   HOH A . 
G 7 HOH   131 531 82   HOH   HOH A . 
G 7 HOH   132 532 33   HOH   HOH A . 
G 7 HOH   133 533 76   HOH   HOH A . 
G 7 HOH   134 534 61   HOH   HOH A . 
G 7 HOH   135 535 69   HOH   HOH A . 
G 7 HOH   136 536 49   HOH   HOH A . 
G 7 HOH   137 537 47   HOH   HOH A . 
G 7 HOH   138 538 199  HOH   HOH A . 
G 7 HOH   139 539 25   HOH   HOH A . 
G 7 HOH   140 540 117  HOH   HOH A . 
G 7 HOH   141 541 148  HOH   HOH A . 
G 7 HOH   142 542 34   HOH   HOH A . 
G 7 HOH   143 543 196  HOH   HOH A . 
G 7 HOH   144 544 54   HOH   HOH A . 
G 7 HOH   145 545 75   HOH   HOH A . 
G 7 HOH   146 546 141  HOH   HOH A . 
G 7 HOH   147 547 171  HOH   HOH A . 
G 7 HOH   148 548 182  HOH   HOH A . 
G 7 HOH   149 549 113  HOH   HOH A . 
G 7 HOH   150 550 192  HOH   HOH A . 
G 7 HOH   151 551 90   HOH   HOH A . 
G 7 HOH   152 552 29   HOH   HOH A . 
G 7 HOH   153 553 176  HOH   HOH A . 
G 7 HOH   154 554 101  HOH   HOH A . 
G 7 HOH   155 555 8    HOH   HOH A . 
G 7 HOH   156 556 132  HOH   HOH A . 
G 7 HOH   157 557 87   HOH   HOH A . 
G 7 HOH   158 558 57   HOH   HOH A . 
G 7 HOH   159 559 53   HOH   HOH A . 
G 7 HOH   160 560 185  HOH   HOH A . 
G 7 HOH   161 561 62   HOH   HOH A . 
G 7 HOH   162 562 124  HOH   HOH A . 
G 7 HOH   163 563 12   HOH   HOH A . 
G 7 HOH   164 564 157  HOH   HOH A . 
G 7 HOH   165 565 180  HOH   HOH A . 
G 7 HOH   166 566 100  HOH   HOH A . 
G 7 HOH   167 567 95   HOH   HOH A . 
G 7 HOH   168 568 109  HOH   HOH A . 
G 7 HOH   169 569 91   HOH   HOH A . 
G 7 HOH   170 570 168  HOH   HOH A . 
G 7 HOH   171 571 119  HOH   HOH A . 
G 7 HOH   172 572 99   HOH   HOH A . 
G 7 HOH   173 573 108  HOH   HOH A . 
G 7 HOH   174 574 31   HOH   HOH A . 
G 7 HOH   175 575 129  HOH   HOH A . 
G 7 HOH   176 576 131  HOH   HOH A . 
G 7 HOH   177 577 202  HOH   HOH A . 
G 7 HOH   178 578 183  HOH   HOH A . 
G 7 HOH   179 579 164  HOH   HOH A . 
G 7 HOH   180 580 92   HOH   HOH A . 
G 7 HOH   181 581 162  HOH   HOH A . 
G 7 HOH   182 582 154  HOH   HOH A . 
G 7 HOH   183 583 167  HOH   HOH A . 
G 7 HOH   184 584 67   HOH   HOH A . 
G 7 HOH   185 585 170  HOH   HOH A . 
G 7 HOH   186 586 83   HOH   HOH A . 
G 7 HOH   187 587 89   HOH   HOH A . 
G 7 HOH   188 588 73   HOH   HOH A . 
G 7 HOH   189 589 200  HOH   HOH A . 
G 7 HOH   190 590 156  HOH   HOH A . 
G 7 HOH   191 591 88   HOH   HOH A . 
G 7 HOH   192 592 159  HOH   HOH A . 
G 7 HOH   193 593 163  HOH   HOH A . 
G 7 HOH   194 594 68   HOH   HOH A . 
G 7 HOH   195 595 110  HOH   HOH A . 
G 7 HOH   196 596 177  HOH   HOH A . 
G 7 HOH   197 597 178  HOH   HOH A . 
G 7 HOH   198 598 195  HOH   HOH A . 
G 7 HOH   199 599 60   HOH   HOH A . 
G 7 HOH   200 600 208  HOH   HOH A . 
G 7 HOH   201 601 45   HOH   HOH A . 
G 7 HOH   202 602 165  HOH   HOH A . 
G 7 HOH   203 603 93   HOH   HOH A . 
G 7 HOH   204 604 193  HOH   HOH A . 
G 7 HOH   205 605 206  HOH   HOH A . 
G 7 HOH   206 606 194  HOH   HOH A . 
G 7 HOH   207 607 191  HOH   HOH A . 
G 7 HOH   208 608 197  HOH   HOH A . 
G 7 HOH   209 609 64   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 reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000  ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .        3 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? O         ? ? ? .        4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? 5.8.0425 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.43 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GFW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.195 
_cell.length_a_esd                 ? 
_cell.length_b                     41.443 
_cell.length_b_esd                 ? 
_cell.length_c                     72.084 
_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                         9GFW 
_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                   9GFW 
_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             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.98 
_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              7.4 
_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    'AMMONIUM SULPHATE 2.8 M, TRIS-HCL 50 MM, 4-HYDROXYMERCURYBENZOATE' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-29 
_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 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GFW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.07 
_reflns.d_resolution_low                               50 
_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                                     103340 
_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                           97.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.081 
_reflns.pdbx_Rpim_I_all                                0.032 
_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                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.074 
_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                                    1.07 
_reflns_shell.d_res_low                                     1.09 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4889 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.6 
_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                               0.422 
_reflns_shell.pdbx_Rpim_I_all                               0.199 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.916 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          92.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.371 
_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]                            0.37 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.42 
_refine.aniso_B[2][2]                            -0.02 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.12 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               10.348 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.972 
_refine.correlation_coeff_Fo_to_Fc_free          0.964 
_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                                 9GFW 
_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                            1.07 
_refine.ls_d_res_low                             40.90 
_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                     101155 
_refine.ls_number_reflns_R_free                  2125 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.05 
_refine.ls_percent_reflns_R_free                 2.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14187 
_refine.ls_R_factor_R_free                       0.16216 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.14145 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.026 
_refine.pdbx_overall_ESU_R_Free                  0.027 
_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                             0.712 
_refine.overall_SU_ML                            0.017 
_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                       1.07 
_refine_hist.d_res_low                        40.90 
_refine_hist.number_atoms_solvent             209 
_refine_hist.number_atoms_total               2299 
_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        2058 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_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' ? 0.042  0.012  2208 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  2021 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.882  1.828  2998 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.676  1.781  4686 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.982  5.000  269  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 6.142  5.000  7    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 10.559 10.000 359  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.101  0.200  311  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  2591 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  495  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.249  0.935  1061 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.224  0.934  1061 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.746  1.686  1335 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.753  1.688  1336 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.813  1.147  1147 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.811  1.148  1146 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.899  1.989  1664 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.839  11.20  2395 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.505  10.53  2356 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 4.324  3.000  4229 ? 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                       1.070 
_refine_ls_shell.d_res_low                        1.098 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             143 
_refine_ls_shell.number_reflns_R_work             7130 
_refine_ls_shell.percent_reflns_obs               92.63 
_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                  0.179 
_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                  0.197 
# 
_struct.entry_id                     9GFW 
_struct.title                        'HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH 4-methylphenyl-boronic acid at pH 7.4' 
_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        9GFW 
_struct_keywords.text            'CARBONIC ANHYDRASE II, PROTEIN-INHIBITOR COMPLEX, INHIBITOR, BORONIC ACID, 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 ? 
F N N 6 ? 
G N N 7 ? 
# 
_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              9GFW 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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)' 760   ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  11820 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 HIS A 15  ? ASP A 19  ? HIS A 15  ASP A 19  5 ? 5 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? ILE A 166 ? ASP A 165 ILE A 167 5 ? 3 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN    . ZN ? ? A HIS 94  A ZN    301 1_555 ? ? ? ? ? ? ? 1.989 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN    . ZN ? ? A HIS 96  A ZN    301 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN    . ZN ? ? A HIS 119 A ZN    301 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc4 metalc ? ? A GLN 136 O   ? ? ? 1_555 F MBO   . HG ? ? A GLN 137 A MBO   305 1_555 ? ? ? ? ? ? ? 2.890 ? ? 
metalc5 metalc ? ? A GLU 204 O   ? ? ? 1_555 F MBO   . HG ? ? A GLU 205 A MBO   305 1_555 ? ? ? ? ? ? ? 2.949 ? ? 
metalc6 metalc ? ? A CYS 205 SG  B ? ? 1_555 F MBO   . HG ? ? A CYS 206 A MBO   305 1_555 ? ? ? ? ? ? ? 2.357 ? ? 
metalc7 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C A1IKU . O1 ? ? A ZN  301 A A1IKU 302 1_555 ? ? ? ? ? ? ? 1.906 ? ? 
metalc8 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C A1IKU . O3 ? ? A ZN  301 A A1IKU 302 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc9 metalc ? ? F MBO .   HG  ? ? ? 1_555 G HOH   . O  ? ? A MBO 305 A HOH   466 1_555 ? ? ? ? ? ? ? 2.988 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS   94  ? A HIS   94  ? 1_555 ZN ? B ZN  . ? A ZN  301 ? 1_555 NE2 ? A HIS   96  ? A HIS   96  ? 1_555 104.3 ? 
2  NE2 ? A HIS   94  ? A HIS   94  ? 1_555 ZN ? B ZN  . ? A ZN  301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 114.3 ? 
3  NE2 ? A HIS   96  ? A HIS   96  ? 1_555 ZN ? B ZN  . ? A ZN  301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 97.1  ? 
4  NE2 ? A HIS   94  ? A HIS   94  ? 1_555 ZN ? B ZN  . ? A ZN  301 ? 1_555 O1  ? C A1IKU .   ? A A1IKU 302 ? 1_555 111.1 ? 
5  NE2 ? A HIS   96  ? A HIS   96  ? 1_555 ZN ? B ZN  . ? A ZN  301 ? 1_555 O1  ? C A1IKU .   ? A A1IKU 302 ? 1_555 107.0 ? 
6  ND1 ? A HIS   119 ? A HIS   119 ? 1_555 ZN ? B ZN  . ? A ZN  301 ? 1_555 O1  ? C A1IKU .   ? A A1IKU 302 ? 1_555 120.4 ? 
7  NE2 ? A HIS   94  ? A HIS   94  ? 1_555 ZN ? B ZN  . ? A ZN  301 ? 1_555 O3  ? C A1IKU .   ? A A1IKU 302 ? 1_555 85.8  ? 
8  NE2 ? A HIS   96  ? A HIS   96  ? 1_555 ZN ? B ZN  . ? A ZN  301 ? 1_555 O3  ? C A1IKU .   ? A A1IKU 302 ? 1_555 168.1 ? 
9  ND1 ? A HIS   119 ? A HIS   119 ? 1_555 ZN ? B ZN  . ? A ZN  301 ? 1_555 O3  ? C A1IKU .   ? A A1IKU 302 ? 1_555 84.2  ? 
10 O1  ? C A1IKU .   ? A A1IKU 302 ? 1_555 ZN ? B ZN  . ? A ZN  301 ? 1_555 O3  ? C A1IKU .   ? A A1IKU 302 ? 1_555 62.7  ? 
11 O   ? A GLN   136 ? A GLN   137 ? 1_555 HG ? F MBO . ? A MBO 305 ? 1_555 CE1 ? F MBO   .   ? A MBO   305 ? 1_555 99.8  ? 
12 O   ? A GLN   136 ? A GLN   137 ? 1_555 HG ? F MBO . ? A MBO 305 ? 1_555 O   ? A GLU   204 ? A GLU   205 ? 1_555 94.8  ? 
13 CE1 ? F MBO   .   ? A MBO   305 ? 1_555 HG ? F MBO . ? A MBO 305 ? 1_555 O   ? A GLU   204 ? A GLU   205 ? 1_555 85.9  ? 
14 O   ? A GLN   136 ? A GLN   137 ? 1_555 HG ? F MBO . ? A MBO 305 ? 1_555 SG  B A CYS   205 ? A CYS   206 ? 1_555 81.5  ? 
15 CE1 ? F MBO   .   ? A MBO   305 ? 1_555 HG ? F MBO . ? A MBO 305 ? 1_555 SG  B A CYS   205 ? A CYS   206 ? 1_555 178.2 ? 
16 O   ? A GLU   204 ? A GLU   205 ? 1_555 HG ? F MBO . ? A MBO 305 ? 1_555 SG  B A CYS   205 ? A CYS   206 ? 1_555 92.7  ? 
17 O   ? A GLN   136 ? A GLN   137 ? 1_555 HG ? F MBO . ? A MBO 305 ? 1_555 O   ? G HOH   .   ? A HOH   466 ? 1_555 132.0 ? 
18 CE1 ? F MBO   .   ? A MBO   305 ? 1_555 HG ? F MBO . ? A MBO 305 ? 1_555 O   ? G HOH   .   ? A HOH   466 ? 1_555 99.7  ? 
19 O   ? A GLU   204 ? A GLU   205 ? 1_555 HG ? F MBO . ? A MBO 305 ? 1_555 O   ? G HOH   .   ? A HOH   466 ? 1_555 130.1 ? 
20 SG  B A CYS   205 ? A CYS   206 ? 1_555 HG ? F MBO . ? A MBO 305 ? 1_555 O   ? G HOH   .   ? A HOH   466 ? 1_555 80.4  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -3.07 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 10.02 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LYS A 45  ? SER A 50  ? LYS A 45  SER A 50  
AA3 2  VAL A 78  ? GLY A 82  ? VAL A 78  GLY A 82  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
_pdbx_entry_details.entry_id                   9GFW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            CYS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             206 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            A 
_pdbx_validate_rmsd_bond.auth_atom_id_2            SG 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            CYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             206 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            A 
_pdbx_validate_rmsd_bond.bond_value                1.961 
_pdbx_validate_rmsd_bond.bond_target_value         1.818 
_pdbx_validate_rmsd_bond.bond_deviation            0.143 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.017 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG A ARG 27 ? ? CD A ARG 27 ? ? NE  A ARG 27 ? ? 129.51 111.80 17.71 2.10 N 
2 1 NE A ARG 27 ? ? CZ A ARG 27 ? ? NH1 A ARG 27 ? ? 126.31 120.30 6.01  0.50 N 
3 1 NE A ARG 27 ? ? CZ A ARG 27 ? ? NH2 A ARG 27 ? ? 115.18 120.30 -5.12 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -144.50 53.42   
2 1 LYS A 76  ? ? -136.09 -39.30  
3 1 GLU A 106 ? ? -94.29  -61.46  
4 1 LYS A 111 ? ? 73.96   -5.03   
5 1 PHE A 176 ? ? -150.83 67.65   
6 1 ASN A 244 ? ? -94.36  46.59   
7 1 LYS A 252 ? ? 56.01   -138.82 
8 1 ASN A 253 ? ? -93.16  58.65   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 607 ? 6.02 . 
2 1 O ? A HOH 608 ? 6.58 . 
3 1 O ? A HOH 609 ? 7.53 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1IKU C2   C  Y N 1   
A1IKU C4   C  Y N 2   
A1IKU C5   C  Y N 3   
A1IKU C6   C  Y N 4   
A1IKU C1   C  Y N 5   
A1IKU C3   C  Y N 6   
A1IKU C7   C  N N 7   
A1IKU B1   B  N N 8   
A1IKU O1   O  N N 9   
A1IKU O2   O  N N 10  
A1IKU O3   O  N N 11  
A1IKU H1   H  N N 12  
A1IKU H2   H  N N 13  
A1IKU H3   H  N N 14  
A1IKU H4   H  N N 15  
A1IKU H5   H  N N 16  
A1IKU H6   H  N N 17  
A1IKU H7   H  N N 18  
A1IKU H8   H  N N 19  
A1IKU H9   H  N N 20  
A1IKU H10  H  N N 21  
ALA   N    N  N N 22  
ALA   CA   C  N S 23  
ALA   C    C  N N 24  
ALA   O    O  N N 25  
ALA   CB   C  N N 26  
ALA   OXT  O  N N 27  
ALA   H    H  N N 28  
ALA   H2   H  N N 29  
ALA   HA   H  N N 30  
ALA   HB1  H  N N 31  
ALA   HB2  H  N N 32  
ALA   HB3  H  N N 33  
ALA   HXT  H  N N 34  
ARG   N    N  N N 35  
ARG   CA   C  N S 36  
ARG   C    C  N N 37  
ARG   O    O  N N 38  
ARG   CB   C  N N 39  
ARG   CG   C  N N 40  
ARG   CD   C  N N 41  
ARG   NE   N  N N 42  
ARG   CZ   C  N N 43  
ARG   NH1  N  N N 44  
ARG   NH2  N  N N 45  
ARG   OXT  O  N N 46  
ARG   H    H  N N 47  
ARG   H2   H  N N 48  
ARG   HA   H  N N 49  
ARG   HB2  H  N N 50  
ARG   HB3  H  N N 51  
ARG   HG2  H  N N 52  
ARG   HG3  H  N N 53  
ARG   HD2  H  N N 54  
ARG   HD3  H  N N 55  
ARG   HE   H  N N 56  
ARG   HH11 H  N N 57  
ARG   HH12 H  N N 58  
ARG   HH21 H  N N 59  
ARG   HH22 H  N N 60  
ARG   HXT  H  N N 61  
ASN   N    N  N N 62  
ASN   CA   C  N S 63  
ASN   C    C  N N 64  
ASN   O    O  N N 65  
ASN   CB   C  N N 66  
ASN   CG   C  N N 67  
ASN   OD1  O  N N 68  
ASN   ND2  N  N N 69  
ASN   OXT  O  N N 70  
ASN   H    H  N N 71  
ASN   H2   H  N N 72  
ASN   HA   H  N N 73  
ASN   HB2  H  N N 74  
ASN   HB3  H  N N 75  
ASN   HD21 H  N N 76  
ASN   HD22 H  N N 77  
ASN   HXT  H  N N 78  
ASP   N    N  N N 79  
ASP   CA   C  N S 80  
ASP   C    C  N N 81  
ASP   O    O  N N 82  
ASP   CB   C  N N 83  
ASP   CG   C  N N 84  
ASP   OD1  O  N N 85  
ASP   OD2  O  N N 86  
ASP   OXT  O  N N 87  
ASP   H    H  N N 88  
ASP   H2   H  N N 89  
ASP   HA   H  N N 90  
ASP   HB2  H  N N 91  
ASP   HB3  H  N N 92  
ASP   HD2  H  N N 93  
ASP   HXT  H  N N 94  
CYS   N    N  N N 95  
CYS   CA   C  N R 96  
CYS   C    C  N N 97  
CYS   O    O  N N 98  
CYS   CB   C  N N 99  
CYS   SG   S  N N 100 
CYS   OXT  O  N N 101 
CYS   H    H  N N 102 
CYS   H2   H  N N 103 
CYS   HA   H  N N 104 
CYS   HB2  H  N N 105 
CYS   HB3  H  N N 106 
CYS   HG   H  N N 107 
CYS   HXT  H  N N 108 
DMS   S    S  N N 109 
DMS   O    O  N N 110 
DMS   C1   C  N N 111 
DMS   C2   C  N N 112 
DMS   H11  H  N N 113 
DMS   H12  H  N N 114 
DMS   H13  H  N N 115 
DMS   H21  H  N N 116 
DMS   H22  H  N N 117 
DMS   H23  H  N N 118 
GLN   N    N  N N 119 
GLN   CA   C  N S 120 
GLN   C    C  N N 121 
GLN   O    O  N N 122 
GLN   CB   C  N N 123 
GLN   CG   C  N N 124 
GLN   CD   C  N N 125 
GLN   OE1  O  N N 126 
GLN   NE2  N  N N 127 
GLN   OXT  O  N N 128 
GLN   H    H  N N 129 
GLN   H2   H  N N 130 
GLN   HA   H  N N 131 
GLN   HB2  H  N N 132 
GLN   HB3  H  N N 133 
GLN   HG2  H  N N 134 
GLN   HG3  H  N N 135 
GLN   HE21 H  N N 136 
GLN   HE22 H  N N 137 
GLN   HXT  H  N N 138 
GLU   N    N  N N 139 
GLU   CA   C  N S 140 
GLU   C    C  N N 141 
GLU   O    O  N N 142 
GLU   CB   C  N N 143 
GLU   CG   C  N N 144 
GLU   CD   C  N N 145 
GLU   OE1  O  N N 146 
GLU   OE2  O  N N 147 
GLU   OXT  O  N N 148 
GLU   H    H  N N 149 
GLU   H2   H  N N 150 
GLU   HA   H  N N 151 
GLU   HB2  H  N N 152 
GLU   HB3  H  N N 153 
GLU   HG2  H  N N 154 
GLU   HG3  H  N N 155 
GLU   HE2  H  N N 156 
GLU   HXT  H  N N 157 
GLY   N    N  N N 158 
GLY   CA   C  N N 159 
GLY   C    C  N N 160 
GLY   O    O  N N 161 
GLY   OXT  O  N N 162 
GLY   H    H  N N 163 
GLY   H2   H  N N 164 
GLY   HA2  H  N N 165 
GLY   HA3  H  N N 166 
GLY   HXT  H  N N 167 
GOL   C1   C  N N 168 
GOL   O1   O  N N 169 
GOL   C2   C  N N 170 
GOL   O2   O  N N 171 
GOL   C3   C  N N 172 
GOL   O3   O  N N 173 
GOL   H11  H  N N 174 
GOL   H12  H  N N 175 
GOL   HO1  H  N N 176 
GOL   H2   H  N N 177 
GOL   HO2  H  N N 178 
GOL   H31  H  N N 179 
GOL   H32  H  N N 180 
GOL   HO3  H  N N 181 
HIS   N    N  N N 182 
HIS   CA   C  N S 183 
HIS   C    C  N N 184 
HIS   O    O  N N 185 
HIS   CB   C  N N 186 
HIS   CG   C  Y N 187 
HIS   ND1  N  Y N 188 
HIS   CD2  C  Y N 189 
HIS   CE1  C  Y N 190 
HIS   NE2  N  Y N 191 
HIS   OXT  O  N N 192 
HIS   H    H  N N 193 
HIS   H2   H  N N 194 
HIS   HA   H  N N 195 
HIS   HB2  H  N N 196 
HIS   HB3  H  N N 197 
HIS   HD1  H  N N 198 
HIS   HD2  H  N N 199 
HIS   HE1  H  N N 200 
HIS   HE2  H  N N 201 
HIS   HXT  H  N N 202 
HOH   O    O  N N 203 
HOH   H1   H  N N 204 
HOH   H2   H  N N 205 
ILE   N    N  N N 206 
ILE   CA   C  N S 207 
ILE   C    C  N N 208 
ILE   O    O  N N 209 
ILE   CB   C  N S 210 
ILE   CG1  C  N N 211 
ILE   CG2  C  N N 212 
ILE   CD1  C  N N 213 
ILE   OXT  O  N N 214 
ILE   H    H  N N 215 
ILE   H2   H  N N 216 
ILE   HA   H  N N 217 
ILE   HB   H  N N 218 
ILE   HG12 H  N N 219 
ILE   HG13 H  N N 220 
ILE   HG21 H  N N 221 
ILE   HG22 H  N N 222 
ILE   HG23 H  N N 223 
ILE   HD11 H  N N 224 
ILE   HD12 H  N N 225 
ILE   HD13 H  N N 226 
ILE   HXT  H  N N 227 
LEU   N    N  N N 228 
LEU   CA   C  N S 229 
LEU   C    C  N N 230 
LEU   O    O  N N 231 
LEU   CB   C  N N 232 
LEU   CG   C  N N 233 
LEU   CD1  C  N N 234 
LEU   CD2  C  N N 235 
LEU   OXT  O  N N 236 
LEU   H    H  N N 237 
LEU   H2   H  N N 238 
LEU   HA   H  N N 239 
LEU   HB2  H  N N 240 
LEU   HB3  H  N N 241 
LEU   HG   H  N N 242 
LEU   HD11 H  N N 243 
LEU   HD12 H  N N 244 
LEU   HD13 H  N N 245 
LEU   HD21 H  N N 246 
LEU   HD22 H  N N 247 
LEU   HD23 H  N N 248 
LEU   HXT  H  N N 249 
LYS   N    N  N N 250 
LYS   CA   C  N S 251 
LYS   C    C  N N 252 
LYS   O    O  N N 253 
LYS   CB   C  N N 254 
LYS   CG   C  N N 255 
LYS   CD   C  N N 256 
LYS   CE   C  N N 257 
LYS   NZ   N  N N 258 
LYS   OXT  O  N N 259 
LYS   H    H  N N 260 
LYS   H2   H  N N 261 
LYS   HA   H  N N 262 
LYS   HB2  H  N N 263 
LYS   HB3  H  N N 264 
LYS   HG2  H  N N 265 
LYS   HG3  H  N N 266 
LYS   HD2  H  N N 267 
LYS   HD3  H  N N 268 
LYS   HE2  H  N N 269 
LYS   HE3  H  N N 270 
LYS   HZ1  H  N N 271 
LYS   HZ2  H  N N 272 
LYS   HZ3  H  N N 273 
LYS   HXT  H  N N 274 
MBO   HG   HG N N 275 
MBO   CE1  C  Y N 276 
MBO   CE2  C  Y N 277 
MBO   CE3  C  Y N 278 
MBO   CE4  C  Y N 279 
MBO   CE5  C  Y N 280 
MBO   CE6  C  Y N 281 
MBO   CZ   C  N N 282 
MBO   OZ1  O  N N 283 
MBO   OZ2  O  N N 284 
MBO   HE2  H  N N 285 
MBO   HE3  H  N N 286 
MBO   HE5  H  N N 287 
MBO   HE6  H  N N 288 
MBO   HZ2  H  N N 289 
MET   N    N  N N 290 
MET   CA   C  N S 291 
MET   C    C  N N 292 
MET   O    O  N N 293 
MET   CB   C  N N 294 
MET   CG   C  N N 295 
MET   SD   S  N N 296 
MET   CE   C  N N 297 
MET   OXT  O  N N 298 
MET   H    H  N N 299 
MET   H2   H  N N 300 
MET   HA   H  N N 301 
MET   HB2  H  N N 302 
MET   HB3  H  N N 303 
MET   HG2  H  N N 304 
MET   HG3  H  N N 305 
MET   HE1  H  N N 306 
MET   HE2  H  N N 307 
MET   HE3  H  N N 308 
MET   HXT  H  N N 309 
PHE   N    N  N N 310 
PHE   CA   C  N S 311 
PHE   C    C  N N 312 
PHE   O    O  N N 313 
PHE   CB   C  N N 314 
PHE   CG   C  Y N 315 
PHE   CD1  C  Y N 316 
PHE   CD2  C  Y N 317 
PHE   CE1  C  Y N 318 
PHE   CE2  C  Y N 319 
PHE   CZ   C  Y N 320 
PHE   OXT  O  N N 321 
PHE   H    H  N N 322 
PHE   H2   H  N N 323 
PHE   HA   H  N N 324 
PHE   HB2  H  N N 325 
PHE   HB3  H  N N 326 
PHE   HD1  H  N N 327 
PHE   HD2  H  N N 328 
PHE   HE1  H  N N 329 
PHE   HE2  H  N N 330 
PHE   HZ   H  N N 331 
PHE   HXT  H  N N 332 
PRO   N    N  N N 333 
PRO   CA   C  N S 334 
PRO   C    C  N N 335 
PRO   O    O  N N 336 
PRO   CB   C  N N 337 
PRO   CG   C  N N 338 
PRO   CD   C  N N 339 
PRO   OXT  O  N N 340 
PRO   H    H  N N 341 
PRO   HA   H  N N 342 
PRO   HB2  H  N N 343 
PRO   HB3  H  N N 344 
PRO   HG2  H  N N 345 
PRO   HG3  H  N N 346 
PRO   HD2  H  N N 347 
PRO   HD3  H  N N 348 
PRO   HXT  H  N N 349 
SER   N    N  N N 350 
SER   CA   C  N S 351 
SER   C    C  N N 352 
SER   O    O  N N 353 
SER   CB   C  N N 354 
SER   OG   O  N N 355 
SER   OXT  O  N N 356 
SER   H    H  N N 357 
SER   H2   H  N N 358 
SER   HA   H  N N 359 
SER   HB2  H  N N 360 
SER   HB3  H  N N 361 
SER   HG   H  N N 362 
SER   HXT  H  N N 363 
THR   N    N  N N 364 
THR   CA   C  N S 365 
THR   C    C  N N 366 
THR   O    O  N N 367 
THR   CB   C  N R 368 
THR   OG1  O  N N 369 
THR   CG2  C  N N 370 
THR   OXT  O  N N 371 
THR   H    H  N N 372 
THR   H2   H  N N 373 
THR   HA   H  N N 374 
THR   HB   H  N N 375 
THR   HG1  H  N N 376 
THR   HG21 H  N N 377 
THR   HG22 H  N N 378 
THR   HG23 H  N N 379 
THR   HXT  H  N N 380 
TRP   N    N  N N 381 
TRP   CA   C  N S 382 
TRP   C    C  N N 383 
TRP   O    O  N N 384 
TRP   CB   C  N N 385 
TRP   CG   C  Y N 386 
TRP   CD1  C  Y N 387 
TRP   CD2  C  Y N 388 
TRP   NE1  N  Y N 389 
TRP   CE2  C  Y N 390 
TRP   CE3  C  Y N 391 
TRP   CZ2  C  Y N 392 
TRP   CZ3  C  Y N 393 
TRP   CH2  C  Y N 394 
TRP   OXT  O  N N 395 
TRP   H    H  N N 396 
TRP   H2   H  N N 397 
TRP   HA   H  N N 398 
TRP   HB2  H  N N 399 
TRP   HB3  H  N N 400 
TRP   HD1  H  N N 401 
TRP   HE1  H  N N 402 
TRP   HE3  H  N N 403 
TRP   HZ2  H  N N 404 
TRP   HZ3  H  N N 405 
TRP   HH2  H  N N 406 
TRP   HXT  H  N N 407 
TYR   N    N  N N 408 
TYR   CA   C  N S 409 
TYR   C    C  N N 410 
TYR   O    O  N N 411 
TYR   CB   C  N N 412 
TYR   CG   C  Y N 413 
TYR   CD1  C  Y N 414 
TYR   CD2  C  Y N 415 
TYR   CE1  C  Y N 416 
TYR   CE2  C  Y N 417 
TYR   CZ   C  Y N 418 
TYR   OH   O  N N 419 
TYR   OXT  O  N N 420 
TYR   H    H  N N 421 
TYR   H2   H  N N 422 
TYR   HA   H  N N 423 
TYR   HB2  H  N N 424 
TYR   HB3  H  N N 425 
TYR   HD1  H  N N 426 
TYR   HD2  H  N N 427 
TYR   HE1  H  N N 428 
TYR   HE2  H  N N 429 
TYR   HH   H  N N 430 
TYR   HXT  H  N N 431 
VAL   N    N  N N 432 
VAL   CA   C  N S 433 
VAL   C    C  N N 434 
VAL   O    O  N N 435 
VAL   CB   C  N N 436 
VAL   CG1  C  N N 437 
VAL   CG2  C  N N 438 
VAL   OXT  O  N N 439 
VAL   H    H  N N 440 
VAL   H2   H  N N 441 
VAL   HA   H  N N 442 
VAL   HB   H  N N 443 
VAL   HG11 H  N N 444 
VAL   HG12 H  N N 445 
VAL   HG13 H  N N 446 
VAL   HG21 H  N N 447 
VAL   HG22 H  N N 448 
VAL   HG23 H  N N 449 
VAL   HXT  H  N N 450 
ZN    ZN   ZN N N 451 
# 
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 
A1IKU C7  C4   sing N N 1   
A1IKU C4  C5   doub Y N 2   
A1IKU C4  C3   sing Y N 3   
A1IKU C5  C6   sing Y N 4   
A1IKU C3  C2   doub Y N 5   
A1IKU C6  C1   doub Y N 6   
A1IKU C2  C1   sing Y N 7   
A1IKU C1  B1   sing N N 8   
A1IKU O1  B1   sing N N 9   
A1IKU O3  B1   sing N N 10  
A1IKU B1  O2   sing N N 11  
A1IKU C2  H1   sing N N 12  
A1IKU C5  H2   sing N N 13  
A1IKU C6  H3   sing N N 14  
A1IKU C3  H4   sing N N 15  
A1IKU C7  H5   sing N N 16  
A1IKU C7  H6   sing N N 17  
A1IKU C7  H7   sing N N 18  
A1IKU O1  H8   sing N N 19  
A1IKU O2  H9   sing N N 20  
A1IKU O3  H10  sing N N 21  
ALA   N   CA   sing N N 22  
ALA   N   H    sing N N 23  
ALA   N   H2   sing N N 24  
ALA   CA  C    sing N N 25  
ALA   CA  CB   sing N N 26  
ALA   CA  HA   sing N N 27  
ALA   C   O    doub N N 28  
ALA   C   OXT  sing N N 29  
ALA   CB  HB1  sing N N 30  
ALA   CB  HB2  sing N N 31  
ALA   CB  HB3  sing N N 32  
ALA   OXT HXT  sing N N 33  
ARG   N   CA   sing N N 34  
ARG   N   H    sing N N 35  
ARG   N   H2   sing N N 36  
ARG   CA  C    sing N N 37  
ARG   CA  CB   sing N N 38  
ARG   CA  HA   sing N N 39  
ARG   C   O    doub N N 40  
ARG   C   OXT  sing N N 41  
ARG   CB  CG   sing N N 42  
ARG   CB  HB2  sing N N 43  
ARG   CB  HB3  sing N N 44  
ARG   CG  CD   sing N N 45  
ARG   CG  HG2  sing N N 46  
ARG   CG  HG3  sing N N 47  
ARG   CD  NE   sing N N 48  
ARG   CD  HD2  sing N N 49  
ARG   CD  HD3  sing N N 50  
ARG   NE  CZ   sing N N 51  
ARG   NE  HE   sing N N 52  
ARG   CZ  NH1  sing N N 53  
ARG   CZ  NH2  doub N N 54  
ARG   NH1 HH11 sing N N 55  
ARG   NH1 HH12 sing N N 56  
ARG   NH2 HH21 sing N N 57  
ARG   NH2 HH22 sing N N 58  
ARG   OXT HXT  sing N N 59  
ASN   N   CA   sing N N 60  
ASN   N   H    sing N N 61  
ASN   N   H2   sing N N 62  
ASN   CA  C    sing N N 63  
ASN   CA  CB   sing N N 64  
ASN   CA  HA   sing N N 65  
ASN   C   O    doub N N 66  
ASN   C   OXT  sing N N 67  
ASN   CB  CG   sing N N 68  
ASN   CB  HB2  sing N N 69  
ASN   CB  HB3  sing N N 70  
ASN   CG  OD1  doub N N 71  
ASN   CG  ND2  sing N N 72  
ASN   ND2 HD21 sing N N 73  
ASN   ND2 HD22 sing N N 74  
ASN   OXT HXT  sing N N 75  
ASP   N   CA   sing N N 76  
ASP   N   H    sing N N 77  
ASP   N   H2   sing N N 78  
ASP   CA  C    sing N N 79  
ASP   CA  CB   sing N N 80  
ASP   CA  HA   sing N N 81  
ASP   C   O    doub N N 82  
ASP   C   OXT  sing N N 83  
ASP   CB  CG   sing N N 84  
ASP   CB  HB2  sing N N 85  
ASP   CB  HB3  sing N N 86  
ASP   CG  OD1  doub N N 87  
ASP   CG  OD2  sing N N 88  
ASP   OD2 HD2  sing N N 89  
ASP   OXT HXT  sing N N 90  
CYS   N   CA   sing N N 91  
CYS   N   H    sing N N 92  
CYS   N   H2   sing N N 93  
CYS   CA  C    sing N N 94  
CYS   CA  CB   sing N N 95  
CYS   CA  HA   sing N N 96  
CYS   C   O    doub N N 97  
CYS   C   OXT  sing N N 98  
CYS   CB  SG   sing N N 99  
CYS   CB  HB2  sing N N 100 
CYS   CB  HB3  sing N N 101 
CYS   SG  HG   sing N N 102 
CYS   OXT HXT  sing N N 103 
DMS   S   O    doub N N 104 
DMS   S   C1   sing N N 105 
DMS   S   C2   sing N N 106 
DMS   C1  H11  sing N N 107 
DMS   C1  H12  sing N N 108 
DMS   C1  H13  sing N N 109 
DMS   C2  H21  sing N N 110 
DMS   C2  H22  sing N N 111 
DMS   C2  H23  sing N N 112 
GLN   N   CA   sing N N 113 
GLN   N   H    sing N N 114 
GLN   N   H2   sing N N 115 
GLN   CA  C    sing N N 116 
GLN   CA  CB   sing N N 117 
GLN   CA  HA   sing N N 118 
GLN   C   O    doub N N 119 
GLN   C   OXT  sing N N 120 
GLN   CB  CG   sing N N 121 
GLN   CB  HB2  sing N N 122 
GLN   CB  HB3  sing N N 123 
GLN   CG  CD   sing N N 124 
GLN   CG  HG2  sing N N 125 
GLN   CG  HG3  sing N N 126 
GLN   CD  OE1  doub N N 127 
GLN   CD  NE2  sing N N 128 
GLN   NE2 HE21 sing N N 129 
GLN   NE2 HE22 sing N N 130 
GLN   OXT HXT  sing N N 131 
GLU   N   CA   sing N N 132 
GLU   N   H    sing N N 133 
GLU   N   H2   sing N N 134 
GLU   CA  C    sing N N 135 
GLU   CA  CB   sing N N 136 
GLU   CA  HA   sing N N 137 
GLU   C   O    doub N N 138 
GLU   C   OXT  sing N N 139 
GLU   CB  CG   sing N N 140 
GLU   CB  HB2  sing N N 141 
GLU   CB  HB3  sing N N 142 
GLU   CG  CD   sing N N 143 
GLU   CG  HG2  sing N N 144 
GLU   CG  HG3  sing N N 145 
GLU   CD  OE1  doub N N 146 
GLU   CD  OE2  sing N N 147 
GLU   OE2 HE2  sing N N 148 
GLU   OXT HXT  sing N N 149 
GLY   N   CA   sing N N 150 
GLY   N   H    sing N N 151 
GLY   N   H2   sing N N 152 
GLY   CA  C    sing N N 153 
GLY   CA  HA2  sing N N 154 
GLY   CA  HA3  sing N N 155 
GLY   C   O    doub N N 156 
GLY   C   OXT  sing N N 157 
GLY   OXT HXT  sing N N 158 
GOL   C1  O1   sing N N 159 
GOL   C1  C2   sing N N 160 
GOL   C1  H11  sing N N 161 
GOL   C1  H12  sing N N 162 
GOL   O1  HO1  sing N N 163 
GOL   C2  O2   sing N N 164 
GOL   C2  C3   sing N N 165 
GOL   C2  H2   sing N N 166 
GOL   O2  HO2  sing N N 167 
GOL   C3  O3   sing N N 168 
GOL   C3  H31  sing N N 169 
GOL   C3  H32  sing N N 170 
GOL   O3  HO3  sing N N 171 
HIS   N   CA   sing N N 172 
HIS   N   H    sing N N 173 
HIS   N   H2   sing N N 174 
HIS   CA  C    sing N N 175 
HIS   CA  CB   sing N N 176 
HIS   CA  HA   sing N N 177 
HIS   C   O    doub N N 178 
HIS   C   OXT  sing N N 179 
HIS   CB  CG   sing N N 180 
HIS   CB  HB2  sing N N 181 
HIS   CB  HB3  sing N N 182 
HIS   CG  ND1  sing Y N 183 
HIS   CG  CD2  doub Y N 184 
HIS   ND1 CE1  doub Y N 185 
HIS   ND1 HD1  sing N N 186 
HIS   CD2 NE2  sing Y N 187 
HIS   CD2 HD2  sing N N 188 
HIS   CE1 NE2  sing Y N 189 
HIS   CE1 HE1  sing N N 190 
HIS   NE2 HE2  sing N N 191 
HIS   OXT HXT  sing N N 192 
HOH   O   H1   sing N N 193 
HOH   O   H2   sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MBO   HG  CE1  sing N N 261 
MBO   CE1 CE2  sing Y N 262 
MBO   CE1 CE6  doub Y N 263 
MBO   CE2 CE3  doub Y N 264 
MBO   CE2 HE2  sing N N 265 
MBO   CE3 CE4  sing Y N 266 
MBO   CE3 HE3  sing N N 267 
MBO   CE4 CE5  doub Y N 268 
MBO   CE4 CZ   sing N N 269 
MBO   CE5 CE6  sing Y N 270 
MBO   CE5 HE5  sing N N 271 
MBO   CE6 HE6  sing N N 272 
MBO   CZ  OZ1  doub N N 273 
MBO   CZ  OZ2  sing N N 274 
MBO   OZ2 HZ2  sing N N 275 
MET   N   CA   sing N N 276 
MET   N   H    sing N N 277 
MET   N   H2   sing N N 278 
MET   CA  C    sing N N 279 
MET   CA  CB   sing N N 280 
MET   CA  HA   sing N N 281 
MET   C   O    doub N N 282 
MET   C   OXT  sing N N 283 
MET   CB  CG   sing N N 284 
MET   CB  HB2  sing N N 285 
MET   CB  HB3  sing N N 286 
MET   CG  SD   sing N N 287 
MET   CG  HG2  sing N N 288 
MET   CG  HG3  sing N N 289 
MET   SD  CE   sing N N 290 
MET   CE  HE1  sing N N 291 
MET   CE  HE2  sing N N 292 
MET   CE  HE3  sing N N 293 
MET   OXT HXT  sing N N 294 
PHE   N   CA   sing N N 295 
PHE   N   H    sing N N 296 
PHE   N   H2   sing N N 297 
PHE   CA  C    sing N N 298 
PHE   CA  CB   sing N N 299 
PHE   CA  HA   sing N N 300 
PHE   C   O    doub N N 301 
PHE   C   OXT  sing N N 302 
PHE   CB  CG   sing N N 303 
PHE   CB  HB2  sing N N 304 
PHE   CB  HB3  sing N N 305 
PHE   CG  CD1  doub Y N 306 
PHE   CG  CD2  sing Y N 307 
PHE   CD1 CE1  sing Y N 308 
PHE   CD1 HD1  sing N N 309 
PHE   CD2 CE2  doub Y N 310 
PHE   CD2 HD2  sing N N 311 
PHE   CE1 CZ   doub Y N 312 
PHE   CE1 HE1  sing N N 313 
PHE   CE2 CZ   sing Y N 314 
PHE   CE2 HE2  sing N N 315 
PHE   CZ  HZ   sing N N 316 
PHE   OXT HXT  sing N N 317 
PRO   N   CA   sing N N 318 
PRO   N   CD   sing N N 319 
PRO   N   H    sing N N 320 
PRO   CA  C    sing N N 321 
PRO   CA  CB   sing N N 322 
PRO   CA  HA   sing N N 323 
PRO   C   O    doub N N 324 
PRO   C   OXT  sing N N 325 
PRO   CB  CG   sing N N 326 
PRO   CB  HB2  sing N N 327 
PRO   CB  HB3  sing N N 328 
PRO   CG  CD   sing N N 329 
PRO   CG  HG2  sing N N 330 
PRO   CG  HG3  sing N N 331 
PRO   CD  HD2  sing N N 332 
PRO   CD  HD3  sing N N 333 
PRO   OXT HXT  sing N N 334 
SER   N   CA   sing N N 335 
SER   N   H    sing N N 336 
SER   N   H2   sing N N 337 
SER   CA  C    sing N N 338 
SER   CA  CB   sing N N 339 
SER   CA  HA   sing N N 340 
SER   C   O    doub N N 341 
SER   C   OXT  sing N N 342 
SER   CB  OG   sing N N 343 
SER   CB  HB2  sing N N 344 
SER   CB  HB3  sing N N 345 
SER   OG  HG   sing N N 346 
SER   OXT HXT  sing N N 347 
THR   N   CA   sing N N 348 
THR   N   H    sing N N 349 
THR   N   H2   sing N N 350 
THR   CA  C    sing N N 351 
THR   CA  CB   sing N N 352 
THR   CA  HA   sing N N 353 
THR   C   O    doub N N 354 
THR   C   OXT  sing N N 355 
THR   CB  OG1  sing N N 356 
THR   CB  CG2  sing N N 357 
THR   CB  HB   sing N N 358 
THR   OG1 HG1  sing N N 359 
THR   CG2 HG21 sing N N 360 
THR   CG2 HG22 sing N N 361 
THR   CG2 HG23 sing N N 362 
THR   OXT HXT  sing N N 363 
TRP   N   CA   sing N N 364 
TRP   N   H    sing N N 365 
TRP   N   H2   sing N N 366 
TRP   CA  C    sing N N 367 
TRP   CA  CB   sing N N 368 
TRP   CA  HA   sing N N 369 
TRP   C   O    doub N N 370 
TRP   C   OXT  sing N N 371 
TRP   CB  CG   sing N N 372 
TRP   CB  HB2  sing N N 373 
TRP   CB  HB3  sing N N 374 
TRP   CG  CD1  doub Y N 375 
TRP   CG  CD2  sing Y N 376 
TRP   CD1 NE1  sing Y N 377 
TRP   CD1 HD1  sing N N 378 
TRP   CD2 CE2  doub Y N 379 
TRP   CD2 CE3  sing Y N 380 
TRP   NE1 CE2  sing Y N 381 
TRP   NE1 HE1  sing N N 382 
TRP   CE2 CZ2  sing Y N 383 
TRP   CE3 CZ3  doub Y N 384 
TRP   CE3 HE3  sing N N 385 
TRP   CZ2 CH2  doub Y N 386 
TRP   CZ2 HZ2  sing N N 387 
TRP   CZ3 CH2  sing Y N 388 
TRP   CZ3 HZ3  sing N N 389 
TRP   CH2 HH2  sing N N 390 
TRP   OXT HXT  sing N N 391 
TYR   N   CA   sing N N 392 
TYR   N   H    sing N N 393 
TYR   N   H2   sing N N 394 
TYR   CA  C    sing N N 395 
TYR   CA  CB   sing N N 396 
TYR   CA  HA   sing N N 397 
TYR   C   O    doub N N 398 
TYR   C   OXT  sing N N 399 
TYR   CB  CG   sing N N 400 
TYR   CB  HB2  sing N N 401 
TYR   CB  HB3  sing N N 402 
TYR   CG  CD1  doub Y N 403 
TYR   CG  CD2  sing Y N 404 
TYR   CD1 CE1  sing Y N 405 
TYR   CD1 HD1  sing N N 406 
TYR   CD2 CE2  doub Y N 407 
TYR   CD2 HD2  sing N N 408 
TYR   CE1 CZ   doub Y N 409 
TYR   CE1 HE1  sing N N 410 
TYR   CE2 CZ   sing Y N 411 
TYR   CE2 HE2  sing N N 412 
TYR   CZ  OH   sing N N 413 
TYR   OH  HH   sing N N 414 
TYR   OXT HXT  sing N N 415 
VAL   N   CA   sing N N 416 
VAL   N   H    sing N N 417 
VAL   N   H2   sing N N 418 
VAL   CA  C    sing N N 419 
VAL   CA  CB   sing N N 420 
VAL   CA  HA   sing N N 421 
VAL   C   O    doub N N 422 
VAL   C   OXT  sing N N 423 
VAL   CB  CG1  sing N N 424 
VAL   CB  CG2  sing N N 425 
VAL   CB  HB   sing N N 426 
VAL   CG1 HG11 sing N N 427 
VAL   CG1 HG12 sing N N 428 
VAL   CG1 HG13 sing N N 429 
VAL   CG2 HG21 sing N N 430 
VAL   CG2 HG22 sing N N 431 
VAL   CG2 HG23 sing N N 432 
VAL   OXT HXT  sing N N 433 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Italian National Research Council (CNR)'   Italy 'Joint Bilateral Agreements CNR/CINVESTAV' 1 
'Ministero dell Universita e della Ricerca' Italy P2022EPH87                                 2 
# 
_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   1CA2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GFW 
_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]   0.023699 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006097 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024130 
_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]   0.014324 
_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 
B  
C  
HG 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS   A 1 3   ? 9.751   5.727   9.044   1.00 21.33 ? 3   HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 3   ? 9.645   4.482   9.847   1.00 20.26 ? 3   HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 3   ? 9.204   3.335   8.929   1.00 20.76 ? 3   HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 3   ? 8.433   3.596   7.985   1.00 23.17 ? 3   HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 3   ? 8.652   4.684   10.989  1.00 18.98 ? 3   HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 3   ? 9.042   5.792   11.921  1.00 20.69 ? 3   HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 3   ? 10.059  5.713   12.848  1.00 22.02 ? 3   HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 3   ? 8.518   7.023   12.056  1.00 21.81 ? 3   HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 3   ? 10.124  6.849   13.531  1.00 23.56 ? 3   HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 3   ? 9.210   7.654   13.062  1.00 25.37 ? 3   HIS   A NE2 1 
ATOM   11   N  N   . HIS   A 1 4   ? 9.696   2.130   9.176   1.00 18.45 ? 4   HIS   A N   1 
ATOM   12   C  CA  . HIS   A 1 4   ? 9.438   0.924   8.355   1.00 16.95 ? 4   HIS   A CA  1 
ATOM   13   C  C   . HIS   A 1 4   ? 8.989   -0.215  9.268   1.00 16.00 ? 4   HIS   A C   1 
ATOM   14   O  O   . HIS   A 1 4   ? 9.504   -1.340  9.256   1.00 20.49 ? 4   HIS   A O   1 
ATOM   15   C  CB  . HIS   A 1 4   ? 10.707  0.530   7.598   1.00 20.53 ? 4   HIS   A CB  1 
ATOM   16   C  CG  . HIS   A 1 4   ? 11.242  1.671   6.810   1.00 24.54 ? 4   HIS   A CG  1 
ATOM   17   N  ND1 . HIS   A 1 4   ? 10.718  2.066   5.598   1.00 30.42 ? 4   HIS   A ND1 1 
ATOM   18   C  CD2 . HIS   A 1 4   ? 12.229  2.525   7.090   1.00 28.16 ? 4   HIS   A CD2 1 
ATOM   19   C  CE1 . HIS   A 1 4   ? 11.399  3.117   5.154   1.00 33.23 ? 4   HIS   A CE1 1 
ATOM   20   N  NE2 . HIS   A 1 4   ? 12.319  3.418   6.054   1.00 32.26 ? 4   HIS   A NE2 1 
ATOM   21   N  N   . TRP   A 1 5   ? 7.990   0.036   10.071  1.00 14.95 ? 5   TRP   A N   1 
ATOM   22   C  CA  . TRP   A 1 5   ? 7.494   -0.988  10.997  1.00 12.25 ? 5   TRP   A CA  1 
ATOM   23   C  C   . TRP   A 1 5   ? 6.511   -1.869  10.257  1.00 11.14 ? 5   TRP   A C   1 
ATOM   24   O  O   . TRP   A 1 5   ? 5.905   -1.439  9.262   1.00 12.91 ? 5   TRP   A O   1 
ATOM   25   C  CB  . TRP   A 1 5   ? 6.863   -0.308  12.216  1.00 11.77 ? 5   TRP   A CB  1 
ATOM   26   C  CG  . TRP   A 1 5   ? 5.645   0.520   11.889  1.00 10.80 ? 5   TRP   A CG  1 
ATOM   27   C  CD1 . TRP   A 1 5   ? 5.553   1.852   11.604  1.00 12.50 ? 5   TRP   A CD1 1 
ATOM   28   C  CD2 . TRP   A 1 5   ? 4.289   0.011   11.890  1.00 9.64  ? 5   TRP   A CD2 1 
ATOM   29   N  NE1 . TRP   A 1 5   ? 4.258   2.207   11.382  1.00 12.34 ? 5   TRP   A NE1 1 
ATOM   30   C  CE2 . TRP   A 1 5   ? 3.457   1.098   11.545  1.00 10.31 ? 5   TRP   A CE2 1 
ATOM   31   C  CE3 . TRP   A 1 5   ? 3.698   -1.239  12.133  1.00 9.25  ? 5   TRP   A CE3 1 
ATOM   32   C  CZ2 . TRP   A 1 5   ? 2.079   0.969   11.465  1.00 10.75 ? 5   TRP   A CZ2 1 
ATOM   33   C  CZ3 . TRP   A 1 5   ? 2.335   -1.370  12.042  1.00 10.32 ? 5   TRP   A CZ3 1 
ATOM   34   C  CH2 . TRP   A 1 5   ? 1.558   -0.264  11.738  1.00 10.82 ? 5   TRP   A CH2 1 
ATOM   35   N  N   . GLY   A 1 6   ? 6.287   -3.051  10.797  1.00 9.94  ? 6   GLY   A N   1 
ATOM   36   C  CA  . GLY   A 1 6   ? 5.297   -3.968  10.227  1.00 10.23 ? 6   GLY   A CA  1 
ATOM   37   C  C   . GLY   A 1 6   ? 4.983   -5.052  11.237  1.00 8.93  ? 6   GLY   A C   1 
ATOM   38   O  O   . GLY   A 1 6   ? 4.997   -4.824  12.453  1.00 9.00  ? 6   GLY   A O   1 
ATOM   39   N  N   . TYR   A 1 7   ? 4.667   -6.241  10.705  1.00 9.86  ? 7   TYR   A N   1 
ATOM   40   C  CA  . TYR   A 1 7   ? 4.285   -7.382  11.522  1.00 10.81 ? 7   TYR   A CA  1 
ATOM   41   C  C   . TYR   A 1 7   ? 5.186   -8.598  11.352  1.00 13.56 ? 7   TYR   A C   1 
ATOM   42   O  O   . TYR   A 1 7   ? 4.910   -9.653  11.926  1.00 17.44 ? 7   TYR   A O   1 
ATOM   43   C  CB  . TYR   A 1 7   ? 2.807   -7.716  11.295  1.00 10.02 ? 7   TYR   A CB  1 
ATOM   44   C  CG  . TYR   A 1 7   ? 1.897   -6.614  11.776  1.00 7.95  ? 7   TYR   A CG  1 
ATOM   45   C  CD1 . TYR   A 1 7   ? 1.526   -6.576  13.111  1.00 7.26  ? 7   TYR   A CD1 1 
ATOM   46   C  CD2 . TYR   A 1 7   ? 1.423   -5.628  10.961  1.00 8.53  ? 7   TYR   A CD2 1 
ATOM   47   C  CE1 . TYR   A 1 7   ? 0.676   -5.589  13.590  1.00 6.95  ? 7   TYR   A CE1 1 
ATOM   48   C  CE2 . TYR   A 1 7   ? 0.597   -4.630  11.417  1.00 7.71  ? 7   TYR   A CE2 1 
ATOM   49   C  CZ  . TYR   A 1 7   ? 0.198   -4.620  12.752  1.00 6.92  ? 7   TYR   A CZ  1 
ATOM   50   O  OH  . TYR   A 1 7   ? -0.624  -3.630  13.181  1.00 7.27  ? 7   TYR   A OH  1 
ATOM   51   N  N   . GLY   A 1 8   ? 6.292   -8.445  10.620  1.00 14.14 ? 8   GLY   A N   1 
ATOM   52   C  CA  . GLY   A 1 8   ? 7.195   -9.557  10.363  1.00 15.62 ? 8   GLY   A CA  1 
ATOM   53   C  C   . GLY   A 1 8   ? 8.148   -9.798  11.529  1.00 13.92 ? 8   GLY   A C   1 
ATOM   54   O  O   . GLY   A 1 8   ? 8.293   -9.017  12.479  1.00 14.59 ? 8   GLY   A O   1 
ATOM   55   N  N   . LYS   A 1 9   ? 9.014   -10.791 11.345  1.00 16.72 ? 9   LYS   A N   1 
ATOM   56   C  CA  . LYS   A 1 9   ? 10.016  -11.127 12.344  1.00 18.40 ? 9   LYS   A CA  1 
ATOM   57   C  C   . LYS   A 1 9   ? 11.011  -9.980  12.507  1.00 17.53 ? 9   LYS   A C   1 
ATOM   58   O  O   . LYS   A 1 9   ? 11.531  -9.782  13.599  1.00 17.30 ? 9   LYS   A O   1 
ATOM   59   C  CB  . LYS   A 1 9   ? 10.842  -12.361 11.944  1.00 22.89 ? 9   LYS   A CB  1 
ATOM   60   C  CG  . LYS   A 1 9   ? 10.046  -13.663 11.886  1.00 30.33 ? 9   LYS   A CG  1 
ATOM   61   C  CD  . LYS   A 1 9   ? 10.817  -14.866 11.360  1.00 35.17 ? 9   LYS   A CD  1 
ATOM   62   C  CE  . LYS   A 1 9   ? 9.915   -16.055 11.177  1.00 39.26 ? 9   LYS   A CE  1 
ATOM   63   N  NZ  . LYS   A 1 9   ? 10.614  -17.196 10.575  1.00 41.68 ? 9   LYS   A NZ  1 
ATOM   64   N  N   . HIS   A 1 10  ? 11.300  -9.278  11.407  1.00 16.83 ? 10  HIS   A N   1 
ATOM   65   C  CA  . HIS   A 1 10  ? 12.334  -8.285  11.489  1.00 16.80 ? 10  HIS   A CA  1 
ATOM   66   C  C   . HIS   A 1 10  ? 11.820  -6.897  11.763  1.00 13.58 ? 10  HIS   A C   1 
ATOM   67   O  O   . HIS   A 1 10  ? 12.621  -6.046  12.093  1.00 15.84 ? 10  HIS   A O   1 
ATOM   68   C  CB  . HIS   A 1 10  ? 13.262  -8.314  10.283  1.00 19.72 ? 10  HIS   A CB  1 
ATOM   69   C  CG  . HIS   A 1 10  ? 14.070  -9.569  10.334  1.00 25.32 ? 10  HIS   A CG  1 
ATOM   70   N  ND1 . HIS   A 1 10  ? 13.746  -10.676 9.599   1.00 27.91 ? 10  HIS   A ND1 1 
ATOM   71   C  CD2 . HIS   A 1 10  ? 15.156  -9.913  11.063  1.00 27.16 ? 10  HIS   A CD2 1 
ATOM   72   C  CE1 . HIS   A 1 10  ? 14.627  -11.652 9.834   1.00 24.01 ? 10  HIS   A CE1 1 
ATOM   73   N  NE2 . HIS   A 1 10  ? 15.474  -11.204 10.757  1.00 30.62 ? 10  HIS   A NE2 1 
ATOM   74   N  N   . ASN   A 1 11  ? 10.509  -6.674  11.700  1.00 12.19 ? 11  ASN   A N   1 
ATOM   75   C  CA  . ASN   A 1 11  ? 9.991   -5.325  11.911  1.00 11.53 ? 11  ASN   A CA  1 
ATOM   76   C  C   . ASN   A 1 11  ? 8.709   -5.285  12.742  1.00 9.99  ? 11  ASN   A C   1 
ATOM   77   O  O   . ASN   A 1 11  ? 8.077   -4.229  12.833  1.00 9.95  ? 11  ASN   A O   1 
ATOM   78   C  CB  . ASN   A 1 11  ? 9.795   -4.594  10.581  1.00 12.30 ? 11  ASN   A CB  1 
ATOM   79   C  CG  . ASN   A 1 11  ? 8.718   -5.241  9.728   1.00 13.00 ? 11  ASN   A CG  1 
ATOM   80   O  OD1 . ASN   A 1 11  ? 8.084   -6.215  10.130  1.00 13.97 ? 11  ASN   A OD1 1 
ATOM   81   N  ND2 . ASN   A 1 11  ? 8.421   -4.694  8.561   1.00 16.69 ? 11  ASN   A ND2 1 
ATOM   82   N  N   . GLY   A 1 12  ? 8.407   -6.395  13.404  1.00 10.19 ? 12  GLY   A N   1 
ATOM   83   C  CA  . GLY   A 1 12  ? 7.137   -6.580  14.082  1.00 9.52  ? 12  GLY   A CA  1 
ATOM   84   C  C   . GLY   A 1 12  ? 7.113   -6.006  15.488  1.00 8.69  ? 12  GLY   A C   1 
ATOM   85   O  O   . GLY   A 1 12  ? 8.031   -5.319  15.926  1.00 8.87  ? 12  GLY   A O   1 
ATOM   86   N  N   . PRO   A 1 13  ? 6.041   -6.330  16.219  1.00 8.43  ? 13  PRO   A N   1 
ATOM   87   C  CA  . PRO   A 1 13  ? 5.807   -5.752  17.538  1.00 8.35  ? 13  PRO   A CA  1 
ATOM   88   C  C   . PRO   A 1 13  ? 6.964   -5.782  18.520  1.00 8.57  ? 13  PRO   A C   1 
ATOM   89   O  O   . PRO   A 1 13  ? 7.052   -4.874  19.326  1.00 9.33  ? 13  PRO   A O   1 
ATOM   90   C  CB  . PRO   A 1 13  ? 4.621   -6.603  18.047  1.00 8.69  ? 13  PRO   A CB  1 
ATOM   91   C  CG  . PRO   A 1 13  ? 3.803   -6.838  16.798  1.00 9.25  ? 13  PRO   A CG  1 
ATOM   92   C  CD  . PRO   A 1 13  ? 4.861   -7.068  15.720  1.00 9.05  ? 13  PRO   A CD  1 
ATOM   93   N  N   . GLU   A 1 14  ? 7.835   -6.809  18.469  1.00 9.56  ? 14  GLU   A N   1 
ATOM   94   C  CA  . GLU   A 1 14  ? 8.940   -6.859  19.423  1.00 11.31 ? 14  GLU   A CA  1 
ATOM   95   C  C   . GLU   A 1 14  ? 10.038  -5.863  19.091  1.00 9.68  ? 14  GLU   A C   1 
ATOM   96   O  O   . GLU   A 1 14  ? 10.934  -5.653  19.921  1.00 11.21 ? 14  GLU   A O   1 
ATOM   97   C  CB  . GLU   A 1 14  ? 9.441   -8.294  19.512  1.00 14.40 ? 14  GLU   A CB  1 
ATOM   98   C  CG  . GLU   A 1 14  ? 8.298   -9.262  19.846  1.00 18.26 ? 14  GLU   A CG  1 
ATOM   99   C  CD  . GLU   A 1 14  ? 7.293   -8.885  20.958  1.00 20.70 ? 14  GLU   A CD  1 
ATOM   100  O  OE1 . GLU   A 1 14  ? 7.811   -8.538  22.033  1.00 23.76 ? 14  GLU   A OE1 1 
ATOM   101  O  OE2 . GLU   A 1 14  ? 6.011   -8.999  20.849  1.00 22.21 ? 14  GLU   A OE2 1 
ATOM   102  N  N   . HIS   A 1 15  ? 9.999   -5.277  17.900  1.00 9.17  ? 15  HIS   A N   1 
ATOM   103  C  CA  . HIS   A 1 15  ? 10.974  -4.289  17.476  1.00 9.16  ? 15  HIS   A CA  1 
ATOM   104  C  C   . HIS   A 1 15  ? 10.494  -2.857  17.638  1.00 8.55  ? 15  HIS   A C   1 
ATOM   105  O  O   . HIS   A 1 15  ? 11.311  -1.928  17.586  1.00 9.16  ? 15  HIS   A O   1 
ATOM   106  C  CB  . HIS   A 1 15  ? 11.347  -4.493  16.003  1.00 9.79  ? 15  HIS   A CB  1 
ATOM   107  C  CG  . HIS   A 1 15  ? 12.104  -5.741  15.754  1.00 10.97 ? 15  HIS   A CG  1 
ATOM   108  N  ND1 . HIS   A 1 15  ? 13.475  -5.772  15.907  1.00 12.82 ? 15  HIS   A ND1 1 
ATOM   109  C  CD2 . HIS   A 1 15  ? 11.709  -6.930  15.309  1.00 13.05 ? 15  HIS   A CD2 1 
ATOM   110  C  CE1 . HIS   A 1 15  ? 13.884  -6.982  15.579  1.00 14.55 ? 15  HIS   A CE1 1 
ATOM   111  N  NE2 . HIS   A 1 15  ? 12.843  -7.712  15.223  1.00 14.18 ? 15  HIS   A NE2 1 
ATOM   112  N  N   . TRP   A 1 16  ? 9.178   -2.641  17.800  1.00 7.72  ? 16  TRP   A N   1 
ATOM   113  C  CA  . TRP   A 1 16  ? 8.618   -1.298  17.713  1.00 7.60  ? 16  TRP   A CA  1 
ATOM   114  C  C   . TRP   A 1 16  ? 9.207   -0.342  18.742  1.00 7.82  ? 16  TRP   A C   1 
ATOM   115  O  O   . TRP   A 1 16  ? 9.308   0.850   18.464  1.00 8.58  ? 16  TRP   A O   1 
ATOM   116  C  CB  . TRP   A 1 16  ? 7.099   -1.353  17.855  1.00 6.96  ? 16  TRP   A CB  1 
ATOM   117  C  CG  . TRP   A 1 16  ? 6.404   -2.044  16.723  1.00 6.60  ? 16  TRP   A CG  1 
ATOM   118  C  CD1 . TRP   A 1 16  ? 6.909   -2.490  15.532  1.00 7.24  ? 16  TRP   A CD1 1 
ATOM   119  C  CD2 . TRP   A 1 16  ? 5.000   -2.369  16.697  1.00 6.44  ? 16  TRP   A CD2 1 
ATOM   120  N  NE1 . TRP   A 1 16  ? 5.932   -3.050  14.764  1.00 7.22  ? 16  TRP   A NE1 1 
ATOM   121  C  CE2 . TRP   A 1 16  ? 4.751   -2.984  15.450  1.00 6.71  ? 16  TRP   A CE2 1 
ATOM   122  C  CE3 . TRP   A 1 16  ? 3.959   -2.219  17.608  1.00 6.37  ? 16  TRP   A CE3 1 
ATOM   123  C  CZ2 . TRP   A 1 16  ? 3.485   -3.441  15.086  1.00 6.87  ? 16  TRP   A CZ2 1 
ATOM   124  C  CZ3 . TRP   A 1 16  ? 2.704   -2.659  17.239  1.00 6.38  ? 16  TRP   A CZ3 1 
ATOM   125  C  CH2 . TRP   A 1 16  ? 2.466   -3.264  15.995  1.00 6.47  ? 16  TRP   A CH2 1 
ATOM   126  N  N   . HIS   A 1 17  ? 9.575   -0.856  19.914  1.00 8.11  ? 17  HIS   A N   1 
ATOM   127  C  CA  . HIS   A 1 17  ? 10.067  0.010   20.970  1.00 8.43  ? 17  HIS   A CA  1 
ATOM   128  C  C   . HIS   A 1 17  ? 11.315  0.812   20.617  1.00 9.25  ? 17  HIS   A C   1 
ATOM   129  O  O   . HIS   A 1 17  ? 11.561  1.847   21.231  1.00 10.09 ? 17  HIS   A O   1 
ATOM   130  C  CB  . HIS   A 1 17  ? 10.334  -0.770  22.244  1.00 9.10  ? 17  HIS   A CB  1 
ATOM   131  C  CG  . HIS   A 1 17  ? 11.538  -1.637  22.168  1.00 10.07 ? 17  HIS   A CG  1 
ATOM   132  N  ND1 . HIS   A 1 17  ? 12.725  -1.246  22.738  1.00 11.88 ? 17  HIS   A ND1 1 
ATOM   133  C  CD2 . HIS   A 1 17  ? 11.711  -2.815  21.592  1.00 10.62 ? 17  HIS   A CD2 1 
ATOM   134  C  CE1 . HIS   A 1 17  ? 13.584  -2.204  22.518  1.00 12.78 ? 17  HIS   A CE1 1 
ATOM   135  N  NE2 . HIS   A 1 17  ? 13.026  -3.169  21.819  1.00 11.81 ? 17  HIS   A NE2 1 
ATOM   136  N  N   . LYS   A 1 18  ? 12.104  0.354   19.641  1.00 8.86  ? 18  LYS   A N   1 
ATOM   137  C  CA  . LYS   A 1 18  ? 13.332  1.075   19.310  1.00 10.20 ? 18  LYS   A CA  1 
ATOM   138  C  C   . LYS   A 1 18  ? 13.026  2.443   18.707  1.00 10.51 ? 18  LYS   A C   1 
ATOM   139  O  O   . LYS   A 1 18  ? 13.649  3.440   19.073  1.00 13.68 ? 18  LYS   A O   1 
ATOM   140  C  CB  . LYS   A 1 18  ? 14.205  0.201   18.400  1.00 10.53 ? 18  LYS   A CB  1 
ATOM   141  C  CG  . LYS   A 1 18  ? 14.817  -0.970  19.160  1.00 10.82 ? 18  LYS   A CG  1 
ATOM   142  C  CD  . LYS   A 1 18  ? 15.552  -1.961  18.276  1.00 10.92 ? 18  LYS   A CD  1 
ATOM   143  C  CE  . LYS   A 1 18  ? 14.610  -2.926  17.615  1.00 10.68 ? 18  LYS   A CE  1 
ATOM   144  N  NZ  . LYS   A 1 18  ? 15.246  -3.745  16.585  1.00 10.75 ? 18  LYS   A NZ  1 
ATOM   145  N  N   . ASP   A 1 19  ? 12.069  2.510   17.787  1.00 10.26 ? 19  ASP   A N   1 
ATOM   146  C  CA  . ASP   A 1 19  ? 11.659  3.785   17.219  1.00 11.12 ? 19  ASP   A CA  1 
ATOM   147  C  C   . ASP   A 1 19  ? 10.560  4.471   18.037  1.00 10.58 ? 19  ASP   A C   1 
ATOM   148  O  O   . ASP   A 1 19  ? 10.392  5.693   17.954  1.00 12.21 ? 19  ASP   A O   1 
ATOM   149  C  CB  . ASP   A 1 19  ? 11.192  3.685   15.779  1.00 12.69 ? 19  ASP   A CB  1 
ATOM   150  C  CG  . ASP   A 1 19  ? 12.283  3.611   14.719  1.00 15.55 ? 19  ASP   A CG  1 
ATOM   151  O  OD1 . ASP   A 1 19  ? 13.433  3.515   15.085  1.00 21.24 ? 19  ASP   A OD1 1 
ATOM   152  O  OD2 . ASP   A 1 19  ? 11.971  3.602   13.517  1.00 20.15 ? 19  ASP   A OD2 1 
ATOM   153  N  N   . PHE   A 1 20  ? 9.789   3.686   18.783  1.00 9.48  ? 20  PHE   A N   1 
ATOM   154  C  CA  . PHE   A 1 20  ? 8.638   4.169   19.519  1.00 9.51  ? 20  PHE   A CA  1 
ATOM   155  C  C   . PHE   A 1 20  ? 8.727   3.692   20.958  1.00 9.59  ? 20  PHE   A C   1 
ATOM   156  O  O   . PHE   A 1 20  ? 8.094   2.700   21.358  1.00 9.06  ? 20  PHE   A O   1 
ATOM   157  C  CB  . PHE   A 1 20  ? 7.333   3.676   18.883  1.00 9.89  ? 20  PHE   A CB  1 
ATOM   158  C  CG  . PHE   A 1 20  ? 7.237   4.062   17.420  1.00 9.79  ? 20  PHE   A CG  1 
ATOM   159  C  CD1 . PHE   A 1 20  ? 6.829   5.329   17.035  1.00 11.54 ? 20  PHE   A CD1 1 
ATOM   160  C  CD2 . PHE   A 1 20  ? 7.613   3.154   16.446  1.00 11.03 ? 20  PHE   A CD2 1 
ATOM   161  C  CE1 . PHE   A 1 20  ? 6.792   5.658   15.681  1.00 12.44 ? 20  PHE   A CE1 1 
ATOM   162  C  CE2 . PHE   A 1 20  ? 7.599   3.495   15.106  1.00 12.41 ? 20  PHE   A CE2 1 
ATOM   163  C  CZ  . PHE   A 1 20  ? 7.179   4.743   14.738  1.00 13.18 ? 20  PHE   A CZ  1 
ATOM   164  N  N   . PRO   A 1 21  ? 9.564   4.332   21.801  1.00 10.18 ? 21  PRO   A N   1 
ATOM   165  C  CA  . PRO   A 1 21  ? 9.823   3.835   23.153  1.00 10.35 ? 21  PRO   A CA  1 
ATOM   166  C  C   . PRO   A 1 21  ? 8.578   3.727   24.036  1.00 9.46  ? 21  PRO   A C   1 
ATOM   167  O  O   . PRO   A 1 21  ? 8.576   2.946   24.981  1.00 9.62  ? 21  PRO   A O   1 
ATOM   168  C  CB  . PRO   A 1 21  ? 10.863  4.798   23.732  1.00 12.15 ? 21  PRO   A CB  1 
ATOM   169  C  CG  . PRO   A 1 21  ? 10.756  5.985   22.860  1.00 13.95 ? 21  PRO   A CG  1 
ATOM   170  C  CD  . PRO   A 1 21  ? 10.452  5.473   21.473  1.00 12.00 ? 21  PRO   A CD  1 
ATOM   171  N  N   A ILE   A 1 22  ? 7.531   4.472   23.646  0.50 8.80  ? 22  ILE   A N   1 
ATOM   172  N  N   B ILE   A 1 22  ? 7.487   4.453   23.751  0.50 9.61  ? 22  ILE   A N   1 
ATOM   173  C  CA  A ILE   A 1 22  ? 6.255   4.402   24.340  0.50 8.18  ? 22  ILE   A CA  1 
ATOM   174  C  CA  B ILE   A 1 22  ? 6.247   4.299   24.513  0.50 9.31  ? 22  ILE   A CA  1 
ATOM   175  C  C   A ILE   A 1 22  ? 5.640   3.002   24.245  0.50 8.03  ? 22  ILE   A C   1 
ATOM   176  C  C   B ILE   A 1 22  ? 5.680   2.881   24.371  0.50 8.60  ? 22  ILE   A C   1 
ATOM   177  O  O   A ILE   A 1 22  ? 4.697   2.735   24.974  0.50 7.90  ? 22  ILE   A O   1 
ATOM   178  O  O   B ILE   A 1 22  ? 4.810   2.472   25.145  0.50 8.43  ? 22  ILE   A O   1 
ATOM   179  C  CB  A ILE   A 1 22  ? 5.273   5.495   23.864  0.50 7.80  ? 22  ILE   A CB  1 
ATOM   180  C  CB  B ILE   A 1 22  ? 5.221   5.360   24.067  0.50 9.42  ? 22  ILE   A CB  1 
ATOM   181  C  CG1 A ILE   A 1 22  ? 4.178   5.723   24.896  0.50 7.96  ? 22  ILE   A CG1 1 
ATOM   182  C  CG1 B ILE   A 1 22  ? 4.166   5.717   25.121  0.50 10.45 ? 22  ILE   A CG1 1 
ATOM   183  C  CG2 A ILE   A 1 22  ? 4.702   5.160   22.497  0.50 7.51  ? 22  ILE   A CG2 1 
ATOM   184  C  CG2 B ILE   A 1 22  ? 4.568   4.914   22.771  0.50 9.20  ? 22  ILE   A CG2 1 
ATOM   185  C  CD1 A ILE   A 1 22  ? 3.247   6.875   24.632  0.50 8.87  ? 22  ILE   A CD1 1 
ATOM   186  C  CD1 B ILE   A 1 22  ? 4.748   6.248   26.417  0.50 11.45 ? 22  ILE   A CD1 1 
ATOM   187  N  N   . ALA   A 1 23  ? 6.181   2.113   23.390  1.00 8.23  ? 23  ALA   A N   1 
ATOM   188  C  CA  . ALA   A 1 23  ? 5.743   0.716   23.279  1.00 7.76  ? 23  ALA   A CA  1 
ATOM   189  C  C   . ALA   A 1 23  ? 5.872   0.004   24.626  1.00 8.53  ? 23  ALA   A C   1 
ATOM   190  O  O   . ALA   A 1 23  ? 5.169   -0.994  24.810  1.00 9.15  ? 23  ALA   A O   1 
ATOM   191  C  CB  . ALA   A 1 23  ? 6.591   -0.022  22.274  1.00 8.09  ? 23  ALA   A CB  1 
ATOM   192  N  N   . LYS   A 1 24  ? 6.787   0.458   25.499  1.00 8.89  ? 24  LYS   A N   1 
ATOM   193  C  CA  . LYS   A 1 24  ? 6.994   -0.141  26.809  1.00 10.10 ? 24  LYS   A CA  1 
ATOM   194  C  C   . LYS   A 1 24  ? 6.403   0.735   27.921  1.00 10.42 ? 24  LYS   A C   1 
ATOM   195  O  O   . LYS   A 1 24  ? 6.816   0.670   29.070  1.00 11.94 ? 24  LYS   A O   1 
ATOM   196  C  CB  . LYS   A 1 24  ? 8.488   -0.402  27.056  1.00 11.50 ? 24  LYS   A CB  1 
ATOM   197  C  CG  . LYS   A 1 24  ? 9.054   -1.493  26.158  1.00 12.75 ? 24  LYS   A CG  1 
ATOM   198  C  CD  . LYS   A 1 24  ? 10.524  -1.697  26.419  1.00 15.39 ? 24  LYS   A CD  1 
ATOM   199  C  CE  . LYS   A 1 24  ? 11.213  -2.715  25.596  1.00 17.45 ? 24  LYS   A CE  1 
ATOM   200  N  NZ  . LYS   A 1 24  ? 10.864  -4.054  26.053  1.00 19.48 ? 24  LYS   A NZ  1 
ATOM   201  N  N   . GLY   A 1 25  ? 5.393   1.539   27.563  1.00 10.02 ? 25  GLY   A N   1 
ATOM   202  C  CA  . GLY   A 1 25  ? 4.793   2.505   28.458  1.00 10.95 ? 25  GLY   A CA  1 
ATOM   203  C  C   . GLY   A 1 25  ? 3.792   1.891   29.439  1.00 9.85  ? 25  GLY   A C   1 
ATOM   204  O  O   . GLY   A 1 25  ? 3.617   0.681   29.551  1.00 11.07 ? 25  GLY   A O   1 
ATOM   205  N  N   . GLU   A 1 26  ? 3.167   2.800   30.174  1.00 9.86  ? 26  GLU   A N   1 
ATOM   206  C  CA  . GLU   A 1 26  ? 2.307   2.451   31.277  1.00 10.84 ? 26  GLU   A CA  1 
ATOM   207  C  C   . GLU   A 1 26  ? 0.860   2.223   30.882  1.00 9.23  ? 26  GLU   A C   1 
ATOM   208  O  O   . GLU   A 1 26  ? 0.093   1.733   31.719  1.00 9.89  ? 26  GLU   A O   1 
ATOM   209  C  CB  . GLU   A 1 26  ? 2.356   3.532   32.355  1.00 13.06 ? 26  GLU   A CB  1 
ATOM   210  C  CG  . GLU   A 1 26  ? 3.752   3.640   32.958  1.00 15.63 ? 26  GLU   A CG  1 
ATOM   211  C  CD  . GLU   A 1 26  ? 4.182   2.362   33.666  1.00 19.35 ? 26  GLU   A CD  1 
ATOM   212  O  OE1 . GLU   A 1 26  ? 3.460   1.882   34.563  1.00 24.58 ? 26  GLU   A OE1 1 
ATOM   213  O  OE2 . GLU   A 1 26  ? 5.218   1.795   33.278  1.00 24.83 ? 26  GLU   A OE2 1 
ATOM   214  N  N   . ARG   A 1 27  ? 0.483   2.512   29.646  1.00 7.33  ? 27  ARG   A N   1 
ATOM   215  C  CA  . ARG   A 1 27  ? -0.917  2.363   29.272  1.00 7.56  ? 27  ARG   A CA  1 
ATOM   216  C  C   . ARG   A 1 27  ? -1.011  1.885   27.837  1.00 6.36  ? 27  ARG   A C   1 
ATOM   217  O  O   . ARG   A 1 27  ? -1.750  2.408   27.016  1.00 7.01  ? 27  ARG   A O   1 
ATOM   218  C  CB  . ARG   A 1 27  ? -1.794  3.547   29.632  1.00 11.03 ? 27  ARG   A CB  1 
ATOM   219  C  CG  . ARG   A 1 27  ? -1.556  4.859   28.970  1.00 13.84 ? 27  ARG   A CG  1 
ATOM   220  C  CD  . ARG   A 1 27  ? -2.838  5.788   29.116  1.00 14.65 ? 27  ARG   A CD  1 
ATOM   221  N  NE  . ARG   A 1 27  ? -4.047  5.849   28.285  1.00 12.89 ? 27  ARG   A NE  1 
ATOM   222  C  CZ  . ARG   A 1 27  ? -4.767  6.925   28.277  1.00 10.87 ? 27  ARG   A CZ  1 
ATOM   223  N  NH1 . ARG   A 1 27  ? -4.576  8.021   29.043  1.00 11.25 ? 27  ARG   A NH1 1 
ATOM   224  N  NH2 . ARG   A 1 27  ? -5.757  6.912   27.465  1.00 13.99 ? 27  ARG   A NH2 1 
ATOM   225  N  N   . GLN   A 1 28  ? -0.309  0.777   27.553  1.00 5.92  ? 28  GLN   A N   1 
ATOM   226  C  CA  . GLN   A 1 28  ? -0.299  0.220   26.205  1.00 5.64  ? 28  GLN   A CA  1 
ATOM   227  C  C   . GLN   A 1 28  ? -1.447  -0.752  25.971  1.00 5.48  ? 28  GLN   A C   1 
ATOM   228  O  O   . GLN   A 1 28  ? -1.957  -1.419  26.885  1.00 6.28  ? 28  GLN   A O   1 
ATOM   229  C  CB  . GLN   A 1 28  ? 1.057   -0.436  25.952  1.00 5.92  ? 28  GLN   A CB  1 
ATOM   230  C  CG  . GLN   A 1 28  ? 2.179   0.586   25.829  1.00 6.58  ? 28  GLN   A CG  1 
ATOM   231  C  CD  . GLN   A 1 28  ? 2.061   1.378   24.535  1.00 6.31  ? 28  GLN   A CD  1 
ATOM   232  O  OE1 . GLN   A 1 28  ? 2.221   0.802   23.447  1.00 6.68  ? 28  GLN   A OE1 1 
ATOM   233  N  NE2 . GLN   A 1 28  ? 1.711   2.643   24.637  1.00 6.20  ? 28  GLN   A NE2 1 
ATOM   234  N  N   . SER   A 1 29  ? -1.831  -0.844  24.699  1.00 5.10  ? 29  SER   A N   1 
ATOM   235  C  CA  . SER   A 1 29  ? -2.876  -1.715  24.237  1.00 4.97  ? 29  SER   A CA  1 
ATOM   236  C  C   . SER   A 1 29  ? -2.363  -2.608  23.130  1.00 4.70  ? 29  SER   A C   1 
ATOM   237  O  O   . SER   A 1 29  ? -1.415  -2.254  22.423  1.00 5.65  ? 29  SER   A O   1 
ATOM   238  C  CB  . SER   A 1 29  ? -4.052  -0.880  23.727  1.00 4.98  ? 29  SER   A CB  1 
ATOM   239  O  OG  . SER   A 1 29  ? -4.651  -0.140  24.786  1.00 5.18  ? 29  SER   A OG  1 
ATOM   240  N  N   . PRO   A 1 30  ? -3.017  -3.755  22.881  1.00 4.85  ? 30  PRO   A N   1 
ATOM   241  C  CA  . PRO   A 1 30  ? -4.173  -4.297  23.616  1.00 4.88  ? 30  PRO   A CA  1 
ATOM   242  C  C   . PRO   A 1 30  ? -3.743  -4.913  24.926  1.00 5.20  ? 30  PRO   A C   1 
ATOM   243  O  O   . PRO   A 1 30  ? -2.569  -4.939  25.260  1.00 5.78  ? 30  PRO   A O   1 
ATOM   244  C  CB  . PRO   A 1 30  ? -4.693  -5.331  22.634  1.00 5.04  ? 30  PRO   A CB  1 
ATOM   245  C  CG  . PRO   A 1 30  ? -3.408  -5.915  22.047  1.00 5.06  ? 30  PRO   A CG  1 
ATOM   246  C  CD  . PRO   A 1 30  ? -2.535  -4.697  21.850  1.00 5.19  ? 30  PRO   A CD  1 
ATOM   247  N  N   . VAL   A 1 31  ? -4.737  -5.426  25.654  1.00 5.38  ? 31  VAL   A N   1 
ATOM   248  C  CA  . VAL   A 1 31  ? -4.558  -6.168  26.893  1.00 5.50  ? 31  VAL   A CA  1 
ATOM   249  C  C   . VAL   A 1 31  ? -5.437  -7.401  26.857  1.00 5.57  ? 31  VAL   A C   1 
ATOM   250  O  O   . VAL   A 1 31  ? -6.412  -7.467  26.100  1.00 6.13  ? 31  VAL   A O   1 
ATOM   251  C  CB  . VAL   A 1 31  ? -4.867  -5.318  28.133  1.00 6.10  ? 31  VAL   A CB  1 
ATOM   252  C  CG1 . VAL   A 1 31  ? -3.942  -4.111  28.234  1.00 7.11  ? 31  VAL   A CG1 1 
ATOM   253  C  CG2 . VAL   A 1 31  ? -6.343  -4.908  28.197  1.00 6.37  ? 31  VAL   A CG2 1 
ATOM   254  N  N   . ASP   A 1 32  ? -5.088  -8.363  27.709  1.00 5.83  ? 32  ASP   A N   1 
ATOM   255  C  CA  . ASP   A 1 32  ? -5.993  -9.439  28.017  1.00 6.05  ? 32  ASP   A CA  1 
ATOM   256  C  C   . ASP   A 1 32  ? -7.040  -8.922  29.010  1.00 6.28  ? 32  ASP   A C   1 
ATOM   257  O  O   . ASP   A 1 32  ? -6.744  -8.231  30.002  1.00 7.86  ? 32  ASP   A O   1 
ATOM   258  C  CB  . ASP   A 1 32  ? -5.266  -10.616 28.641  1.00 6.80  ? 32  ASP   A CB  1 
ATOM   259  C  CG  . ASP   A 1 32  ? -6.212  -11.765 28.967  1.00 7.23  ? 32  ASP   A CG  1 
ATOM   260  O  OD1 . ASP   A 1 32  ? -6.894  -12.244 28.032  1.00 7.52  ? 32  ASP   A OD1 1 
ATOM   261  O  OD2 . ASP   A 1 32  ? -6.217  -12.189 30.149  1.00 9.62  ? 32  ASP   A OD2 1 
ATOM   262  N  N   . ILE   A 1 33  ? -8.307  -9.237  28.728  1.00 5.94  ? 33  ILE   A N   1 
ATOM   263  C  CA  . ILE   A 1 33  ? -9.421  -8.880  29.590  1.00 6.05  ? 33  ILE   A CA  1 
ATOM   264  C  C   . ILE   A 1 33  ? -9.727  -10.122 30.420  1.00 6.48  ? 33  ILE   A C   1 
ATOM   265  O  O   . ILE   A 1 33  ? -10.290 -11.101 29.943  1.00 7.47  ? 33  ILE   A O   1 
ATOM   266  C  CB  . ILE   A 1 33  ? -10.632 -8.461  28.753  1.00 6.58  ? 33  ILE   A CB  1 
ATOM   267  C  CG1 . ILE   A 1 33  ? -10.312 -7.246  27.905  1.00 7.08  ? 33  ILE   A CG1 1 
ATOM   268  C  CG2 . ILE   A 1 33  ? -11.844 -8.206  29.655  1.00 7.54  ? 33  ILE   A CG2 1 
ATOM   269  C  CD1 . ILE   A 1 33  ? -11.306 -6.950  26.794  1.00 8.12  ? 33  ILE   A CD1 1 
ATOM   270  N  N   A ASP   A 1 34  ? -9.327  -10.071 31.681  0.50 7.18  ? 34  ASP   A N   1 
ATOM   271  N  N   B ASP   A 1 34  ? -9.320  -10.069 31.686  0.50 7.38  ? 34  ASP   A N   1 
ATOM   272  C  CA  A ASP   A 1 34  ? -9.611  -11.140 32.611  0.50 7.85  ? 34  ASP   A CA  1 
ATOM   273  C  CA  B ASP   A 1 34  ? -9.614  -11.106 32.654  0.50 8.30  ? 34  ASP   A CA  1 
ATOM   274  C  C   A ASP   A 1 34  ? -10.989 -10.837 33.174  0.50 8.17  ? 34  ASP   A C   1 
ATOM   275  C  C   B ASP   A 1 34  ? -11.011 -10.822 33.179  0.50 8.52  ? 34  ASP   A C   1 
ATOM   276  O  O   A ASP   A 1 34  ? -11.170 -9.875  33.930  0.50 9.35  ? 34  ASP   A O   1 
ATOM   277  O  O   B ASP   A 1 34  ? -11.238 -9.863  33.923  0.50 9.98  ? 34  ASP   A O   1 
ATOM   278  C  CB  A ASP   A 1 34  ? -8.539  -11.213 33.677  0.50 8.53  ? 34  ASP   A CB  1 
ATOM   279  C  CB  B ASP   A 1 34  ? -8.606  -11.107 33.788  0.50 9.34  ? 34  ASP   A CB  1 
ATOM   280  C  CG  A ASP   A 1 34  ? -8.635  -12.468 34.531  0.50 9.05  ? 34  ASP   A CG  1 
ATOM   281  C  CG  B ASP   A 1 34  ? -8.903  -12.118 34.889  0.50 10.42 ? 34  ASP   A CG  1 
ATOM   282  O  OD1 A ASP   A 1 34  ? -8.257  -13.547 34.057  0.50 10.34 ? 34  ASP   A OD1 1 
ATOM   283  O  OD1 B ASP   A 1 34  ? -10.068 -12.502 35.052  0.50 11.29 ? 34  ASP   A OD1 1 
ATOM   284  O  OD2 A ASP   A 1 34  ? -9.151  -12.351 35.655  0.50 10.17 ? 34  ASP   A OD2 1 
ATOM   285  O  OD2 B ASP   A 1 34  ? -7.954  -12.575 35.546  0.50 12.50 ? 34  ASP   A OD2 1 
ATOM   286  N  N   . THR   A 1 35  ? -11.968 -11.632 32.753  1.00 8.94  ? 35  THR   A N   1 
ATOM   287  C  CA  . THR   A 1 35  ? -13.361 -11.350 33.012  1.00 9.92  ? 35  THR   A CA  1 
ATOM   288  C  C   . THR   A 1 35  ? -13.688 -11.448 34.479  1.00 10.70 ? 35  THR   A C   1 
ATOM   289  O  O   . THR   A 1 35  ? -14.569 -10.731 34.946  1.00 13.10 ? 35  THR   A O   1 
ATOM   290  C  CB  . THR   A 1 35  ? -14.271 -12.259 32.200  1.00 11.03 ? 35  THR   A CB  1 
ATOM   291  O  OG1 . THR   A 1 35  ? -14.144 -13.613 32.644  1.00 11.85 ? 35  THR   A OG1 1 
ATOM   292  C  CG2 . THR   A 1 35  ? -14.021 -12.130 30.709  1.00 12.21 ? 35  THR   A CG2 1 
ATOM   293  N  N   . HIS   A 1 36  ? -12.938 -12.262 35.219  1.00 9.72  ? 36  HIS   A N   1 
ATOM   294  C  CA  . HIS   A 1 36  ? -13.183 -12.404 36.645  1.00 10.66 ? 36  HIS   A CA  1 
ATOM   295  C  C   . HIS   A 1 36  ? -12.657 -11.227 37.451  1.00 12.05 ? 36  HIS   A C   1 
ATOM   296  O  O   . HIS   A 1 36  ? -13.228 -10.932 38.515  1.00 17.19 ? 36  HIS   A O   1 
ATOM   297  C  CB  . HIS   A 1 36  ? -12.634 -13.746 37.130  1.00 11.61 ? 36  HIS   A CB  1 
ATOM   298  C  CG  . HIS   A 1 36  ? -13.433 -14.841 36.517  1.00 13.81 ? 36  HIS   A CG  1 
ATOM   299  N  ND1 . HIS   A 1 36  ? -13.000 -15.610 35.456  1.00 16.51 ? 36  HIS   A ND1 1 
ATOM   300  C  CD2 . HIS   A 1 36  ? -14.695 -15.247 36.820  1.00 16.83 ? 36  HIS   A CD2 1 
ATOM   301  C  CE1 . HIS   A 1 36  ? -13.960 -16.458 35.146  1.00 17.02 ? 36  HIS   A CE1 1 
ATOM   302  N  NE2 . HIS   A 1 36  ? -14.991 -16.280 35.963  1.00 18.37 ? 36  HIS   A NE2 1 
ATOM   303  N  N   . THR   A 1 37  ? -11.640 -10.508 36.933  1.00 10.50 ? 37  THR   A N   1 
ATOM   304  C  CA  . THR   A 1 37  ? -11.050 -9.373  37.617  1.00 11.17 ? 37  THR   A CA  1 
ATOM   305  C  C   . THR   A 1 37  ? -11.744 -8.067  37.254  1.00 10.81 ? 37  THR   A C   1 
ATOM   306  O  O   . THR   A 1 37  ? -11.690 -7.120  38.012  1.00 13.10 ? 37  THR   A O   1 
ATOM   307  C  CB  . THR   A 1 37  ? -9.538  -9.342  37.347  1.00 13.56 ? 37  THR   A CB  1 
ATOM   308  O  OG1 . THR   A 1 37  ? -8.990  -10.587 37.790  1.00 16.88 ? 37  THR   A OG1 1 
ATOM   309  C  CG2 . THR   A 1 37  ? -8.823  -8.214  38.076  1.00 14.24 ? 37  THR   A CG2 1 
ATOM   310  N  N   . ALA   A 1 38  ? -12.370 -7.984  36.105  1.00 10.26 ? 38  ALA   A N   1 
ATOM   311  C  CA  . ALA   A 1 38  ? -13.079 -6.772  35.681  1.00 9.51  ? 38  ALA   A CA  1 
ATOM   312  C  C   . ALA   A 1 38  ? -14.262 -6.606  36.616  1.00 10.65 ? 38  ALA   A C   1 
ATOM   313  O  O   . ALA   A 1 38  ? -14.860 -7.580  37.056  1.00 14.73 ? 38  ALA   A O   1 
ATOM   314  C  CB  . ALA   A 1 38  ? -13.563 -6.922  34.259  1.00 9.71  ? 38  ALA   A CB  1 
ATOM   315  N  N   . LYS   A 1 39  ? -14.534 -5.399  37.033  1.00 9.25  ? 39  LYS   A N   1 
ATOM   316  C  CA  . LYS   A 1 39  ? -15.615 -5.135  37.983  1.00 8.92  ? 39  LYS   A CA  1 
ATOM   317  C  C   . LYS   A 1 39  ? -16.711 -4.322  37.307  1.00 8.32  ? 39  LYS   A C   1 
ATOM   318  O  O   . LYS   A 1 39  ? -16.430 -3.331  36.615  1.00 8.05  ? 39  LYS   A O   1 
ATOM   319  C  CB  . LYS   A 1 39  ? -15.044 -4.353  39.165  1.00 10.23 ? 39  LYS   A CB  1 
ATOM   320  C  CG  . LYS   A 1 39  ? -16.006 -4.200  40.315  1.00 11.62 ? 39  LYS   A CG  1 
ATOM   321  C  CD  . LYS   A 1 39  ? -15.451 -3.378  41.473  1.00 12.96 ? 39  LYS   A CD  1 
ATOM   322  C  CE  . LYS   A 1 39  ? -16.401 -3.311  42.614  1.00 14.43 ? 39  LYS   A CE  1 
ATOM   323  N  NZ  . LYS   A 1 39  ? -15.933 -2.366  43.625  1.00 15.37 ? 39  LYS   A NZ  1 
ATOM   324  N  N   . TYR   A 1 40  ? -17.988 -4.678  37.571  1.00 8.69  ? 40  TYR   A N   1 
ATOM   325  C  CA  . TYR   A 1 40  ? -19.108 -3.875  37.147  1.00 9.29  ? 40  TYR   A CA  1 
ATOM   326  C  C   . TYR   A 1 40  ? -18.976 -2.477  37.748  1.00 9.82  ? 40  TYR   A C   1 
ATOM   327  O  O   . TYR   A 1 40  ? -18.706 -2.325  38.961  1.00 11.76 ? 40  TYR   A O   1 
ATOM   328  C  CB  . TYR   A 1 40  ? -20.423 -4.508  37.612  1.00 11.16 ? 40  TYR   A CB  1 
ATOM   329  C  CG  . TYR   A 1 40  ? -21.606 -3.572  37.432  1.00 12.42 ? 40  TYR   A CG  1 
ATOM   330  C  CD1 . TYR   A 1 40  ? -22.027 -3.175  36.169  1.00 12.52 ? 40  TYR   A CD1 1 
ATOM   331  C  CD2 . TYR   A 1 40  ? -22.323 -3.106  38.535  1.00 15.32 ? 40  TYR   A CD2 1 
ATOM   332  C  CE1 . TYR   A 1 40  ? -23.095 -2.309  36.011  1.00 14.54 ? 40  TYR   A CE1 1 
ATOM   333  C  CE2 . TYR   A 1 40  ? -23.417 -2.275  38.385  1.00 17.08 ? 40  TYR   A CE2 1 
ATOM   334  C  CZ  . TYR   A 1 40  ? -23.814 -1.891  37.118  1.00 16.24 ? 40  TYR   A CZ  1 
ATOM   335  O  OH  . TYR   A 1 40  ? -24.871 -1.028  36.948  1.00 20.19 ? 40  TYR   A OH  1 
ATOM   336  N  N   . ASP   A 1 41  ? -19.188 -1.461  36.934  1.00 9.91  ? 41  ASP   A N   1 
ATOM   337  C  CA  . ASP   A 1 41  ? -19.097 -0.083  37.383  1.00 11.62 ? 41  ASP   A CA  1 
ATOM   338  C  C   . ASP   A 1 41  ? -20.452 0.594   37.236  1.00 12.59 ? 41  ASP   A C   1 
ATOM   339  O  O   . ASP   A 1 41  ? -20.858 0.957   36.132  1.00 12.34 ? 41  ASP   A O   1 
ATOM   340  C  CB  . ASP   A 1 41  ? -18.017 0.659   36.605  1.00 12.37 ? 41  ASP   A CB  1 
ATOM   341  C  CG  . ASP   A 1 41  ? -17.774 2.083   37.051  1.00 16.31 ? 41  ASP   A CG  1 
ATOM   342  O  OD1 . ASP   A 1 41  ? -18.549 2.563   37.904  1.00 18.04 ? 41  ASP   A OD1 1 
ATOM   343  O  OD2 . ASP   A 1 41  ? -16.776 2.647   36.568  1.00 19.85 ? 41  ASP   A OD2 1 
ATOM   344  N  N   . PRO   A 1 42  ? -21.174 0.811   38.349  1.00 15.61 ? 42  PRO   A N   1 
ATOM   345  C  CA  . PRO   A 1 42  ? -22.459 1.497   38.261  1.00 17.44 ? 42  PRO   A CA  1 
ATOM   346  C  C   . PRO   A 1 42  ? -22.355 2.974   37.874  1.00 16.51 ? 42  PRO   A C   1 
ATOM   347  O  O   . PRO   A 1 42  ? -23.373 3.593   37.580  1.00 20.92 ? 42  PRO   A O   1 
ATOM   348  C  CB  . PRO   A 1 42  ? -23.093 1.298   39.651  1.00 18.87 ? 42  PRO   A CB  1 
ATOM   349  C  CG  . PRO   A 1 42  ? -22.001 0.848   40.514  1.00 18.84 ? 42  PRO   A CG  1 
ATOM   350  C  CD  . PRO   A 1 42  ? -20.813 0.406   39.715  1.00 16.93 ? 42  PRO   A CD  1 
ATOM   351  N  N   . SER   A 1 43  ? -21.156 3.585   37.876  1.00 18.43 ? 43  SER   A N   1 
ATOM   352  C  CA  . SER   A 1 43  ? -20.991 4.988   37.498  1.00 18.31 ? 43  SER   A CA  1 
ATOM   353  C  C   . SER   A 1 43  ? -21.015 5.200   35.986  1.00 17.36 ? 43  SER   A C   1 
ATOM   354  O  O   . SER   A 1 43  ? -21.168 6.319   35.516  1.00 19.96 ? 43  SER   A O   1 
ATOM   355  C  CB  . SER   A 1 43  ? -19.721 5.547   38.081  1.00 20.82 ? 43  SER   A CB  1 
ATOM   356  O  OG  . SER   A 1 43  ? -18.575 5.223   37.316  1.00 22.42 ? 43  SER   A OG  1 
ATOM   357  N  N   . LEU   A 1 44  ? -20.855 4.135   35.211  1.00 14.77 ? 44  LEU   A N   1 
ATOM   358  C  CA  . LEU   A 1 44  ? -20.894 4.246   33.767  1.00 13.11 ? 44  LEU   A CA  1 
ATOM   359  C  C   . LEU   A 1 44  ? -22.297 4.656   33.347  1.00 14.05 ? 44  LEU   A C   1 
ATOM   360  O  O   . LEU   A 1 44  ? -23.296 4.047   33.750  1.00 15.14 ? 44  LEU   A O   1 
ATOM   361  C  CB  . LEU   A 1 44  ? -20.481 2.915   33.134  1.00 11.40 ? 44  LEU   A CB  1 
ATOM   362  C  CG  . LEU   A 1 44  ? -19.019 2.516   33.367  1.00 10.10 ? 44  LEU   A CG  1 
ATOM   363  C  CD1 . LEU   A 1 44  ? -18.755 1.091   32.956  1.00 10.52 ? 44  LEU   A CD1 1 
ATOM   364  C  CD2 . LEU   A 1 44  ? -18.110 3.406   32.579  1.00 11.04 ? 44  LEU   A CD2 1 
ATOM   365  N  N   . LYS   A 1 45  ? -22.352 5.655   32.460  1.00 15.00 ? 45  LYS   A N   1 
ATOM   366  C  CA  . LYS   A 1 45  ? -23.609 6.112   31.893  1.00 15.30 ? 45  LYS   A CA  1 
ATOM   367  C  C   . LYS   A 1 45  ? -23.991 5.229   30.714  1.00 13.04 ? 45  LYS   A C   1 
ATOM   368  O  O   . LYS   A 1 45  ? -23.169 4.510   30.162  1.00 11.20 ? 45  LYS   A O   1 
ATOM   369  C  CB  . LYS   A 1 45  ? -23.495 7.567   31.435  1.00 17.60 ? 45  LYS   A CB  1 
ATOM   370  C  CG  . LYS   A 1 45  ? -23.059 8.586   32.474  1.00 20.51 ? 45  LYS   A CG  1 
ATOM   371  C  CD  . LYS   A 1 45  ? -23.855 8.604   33.765  1.00 26.20 ? 45  LYS   A CD  1 
ATOM   372  C  CE  . LYS   A 1 45  ? -23.102 9.348   34.832  1.00 30.73 ? 45  LYS   A CE  1 
ATOM   373  N  NZ  . LYS   A 1 45  ? -23.985 9.813   35.900  1.00 34.35 ? 45  LYS   A NZ  1 
ATOM   374  N  N   . PRO   A 1 46  ? -25.248 5.216   30.252  1.00 13.86 ? 46  PRO   A N   1 
ATOM   375  C  CA  . PRO   A 1 46  ? -25.552 4.436   29.052  1.00 13.99 ? 46  PRO   A CA  1 
ATOM   376  C  C   . PRO   A 1 46  ? -24.640 4.825   27.878  1.00 12.12 ? 46  PRO   A C   1 
ATOM   377  O  O   . PRO   A 1 46  ? -24.383 5.997   27.651  1.00 12.45 ? 46  PRO   A O   1 
ATOM   378  C  CB  . PRO   A 1 46  ? -27.009 4.779   28.782  1.00 15.89 ? 46  PRO   A CB  1 
ATOM   379  C  CG  . PRO   A 1 46  ? -27.526 5.129   30.153  1.00 16.95 ? 46  PRO   A CG  1 
ATOM   380  C  CD  . PRO   A 1 46  ? -26.427 5.897   30.806  1.00 15.56 ? 46  PRO   A CD  1 
ATOM   381  N  N   . LEU   A 1 47  ? -24.214 3.826   27.110  1.00 10.91 ? 47  LEU   A N   1 
ATOM   382  C  CA  . LEU   A 1 47  ? -23.427 4.084   25.898  1.00 10.18 ? 47  LEU   A CA  1 
ATOM   383  C  C   . LEU   A 1 47  ? -24.330 4.434   24.748  1.00 9.79  ? 47  LEU   A C   1 
ATOM   384  O  O   . LEU   A 1 47  ? -25.354 3.817   24.572  1.00 12.50 ? 47  LEU   A O   1 
ATOM   385  C  CB  . LEU   A 1 47  ? -22.661 2.834   25.493  1.00 10.92 ? 47  LEU   A CB  1 
ATOM   386  C  CG  . LEU   A 1 47  ? -21.594 2.995   24.405  1.00 10.60 ? 47  LEU   A CG  1 
ATOM   387  C  CD1 . LEU   A 1 47  ? -20.389 3.757   24.891  1.00 11.33 ? 47  LEU   A CD1 1 
ATOM   388  C  CD2 . LEU   A 1 47  ? -21.111 1.627   23.933  1.00 11.75 ? 47  LEU   A CD2 1 
ATOM   389  N  N   . SER   A 1 48  ? -23.930 5.422   23.951  1.00 9.04  ? 48  SER   A N   1 
ATOM   390  C  CA  . SER   A 1 48  ? -24.700 5.939   22.841  1.00 9.69  ? 48  SER   A CA  1 
ATOM   391  C  C   . SER   A 1 48  ? -23.854 5.888   21.581  1.00 9.52  ? 48  SER   A C   1 
ATOM   392  O  O   . SER   A 1 48  ? -22.890 6.631   21.450  1.00 10.61 ? 48  SER   A O   1 
ATOM   393  C  CB  . SER   A 1 48  ? -25.121 7.376   23.155  1.00 12.00 ? 48  SER   A CB  1 
ATOM   394  O  OG  . SER   A 1 48  ? -25.680 8.028   22.047  1.00 15.96 ? 48  SER   A OG  1 
ATOM   395  N  N   . VAL   A 1 49  ? -24.244 5.042   20.649  1.00 10.52 ? 49  VAL   A N   1 
ATOM   396  C  CA  . VAL   A 1 49  ? -23.611 4.936   19.355  1.00 11.35 ? 49  VAL   A CA  1 
ATOM   397  C  C   . VAL   A 1 49  ? -24.593 5.544   18.356  1.00 12.96 ? 49  VAL   A C   1 
ATOM   398  O  O   . VAL   A 1 49  ? -25.660 4.986   18.120  1.00 15.09 ? 49  VAL   A O   1 
ATOM   399  C  CB  . VAL   A 1 49  ? -23.254 3.468   19.025  1.00 13.47 ? 49  VAL   A CB  1 
ATOM   400  C  CG1 . VAL   A 1 49  ? -22.470 3.332   17.732  1.00 15.92 ? 49  VAL   A CG1 1 
ATOM   401  C  CG2 . VAL   A 1 49  ? -22.548 2.758   20.175  1.00 14.60 ? 49  VAL   A CG2 1 
ATOM   402  N  N   . SER   A 1 50  ? -24.295 6.728   17.808  1.00 12.45 ? 50  SER   A N   1 
ATOM   403  C  CA  . SER   A 1 50  ? -25.244 7.451   16.970  1.00 14.59 ? 50  SER   A CA  1 
ATOM   404  C  C   . SER   A 1 50  ? -24.643 7.600   15.584  1.00 12.69 ? 50  SER   A C   1 
ATOM   405  O  O   . SER   A 1 50  ? -23.977 8.567   15.293  1.00 13.49 ? 50  SER   A O   1 
ATOM   406  C  CB  . SER   A 1 50  ? -25.623 8.770   17.575  1.00 17.47 ? 50  SER   A CB  1 
ATOM   407  O  OG  . SER   A 1 50  ? -26.320 8.547   18.790  1.00 20.52 ? 50  SER   A OG  1 
ATOM   408  N  N   . TYR   A 1 51  ? -24.891 6.597   14.741  1.00 12.62 ? 51  TYR   A N   1 
ATOM   409  C  CA  . TYR   A 1 51  ? -24.290 6.552   13.426  1.00 12.50 ? 51  TYR   A CA  1 
ATOM   410  C  C   . TYR   A 1 51  ? -25.264 6.804   12.275  1.00 14.17 ? 51  TYR   A C   1 
ATOM   411  O  O   . TYR   A 1 51  ? -24.908 6.557   11.129  1.00 14.34 ? 51  TYR   A O   1 
ATOM   412  C  CB  . TYR   A 1 51  ? -23.656 5.165   13.231  1.00 12.17 ? 51  TYR   A CB  1 
ATOM   413  C  CG  . TYR   A 1 51  ? -22.395 4.839   14.021  1.00 11.08 ? 51  TYR   A CG  1 
ATOM   414  C  CD1 . TYR   A 1 51  ? -21.659 5.801   14.681  1.00 11.55 ? 51  TYR   A CD1 1 
ATOM   415  C  CD2 . TYR   A 1 51  ? -21.905 3.547   14.049  1.00 10.05 ? 51  TYR   A CD2 1 
ATOM   416  C  CE1 . TYR   A 1 51  ? -20.457 5.496   15.333  1.00 10.20 ? 51  TYR   A CE1 1 
ATOM   417  C  CE2 . TYR   A 1 51  ? -20.716 3.226   14.673  1.00 9.92  ? 51  TYR   A CE2 1 
ATOM   418  C  CZ  . TYR   A 1 51  ? -19.981 4.198   15.322  1.00 9.51  ? 51  TYR   A CZ  1 
ATOM   419  O  OH  . TYR   A 1 51  ? -18.818 3.828   15.930  1.00 9.41  ? 51  TYR   A OH  1 
ATOM   420  N  N   . ASP   A 1 52  ? -26.481 7.275   12.546  1.00 15.95 ? 52  ASP   A N   1 
ATOM   421  C  CA  . ASP   A 1 52  ? -27.465 7.466   11.487  1.00 18.05 ? 52  ASP   A CA  1 
ATOM   422  C  C   . ASP   A 1 52  ? -27.012 8.400   10.351  1.00 17.10 ? 52  ASP   A C   1 
ATOM   423  O  O   . ASP   A 1 52  ? -27.470 8.229   9.222   1.00 21.13 ? 52  ASP   A O   1 
ATOM   424  C  CB  . ASP   A 1 52  ? -28.788 7.952   12.061  1.00 21.06 ? 52  ASP   A CB  1 
ATOM   425  C  CG  . ASP   A 1 52  ? -28.631 9.106   13.043  1.00 26.28 ? 52  ASP   A CG  1 
ATOM   426  O  OD1 . ASP   A 1 52  ? -28.076 8.878   14.161  1.00 33.07 ? 52  ASP   A OD1 1 
ATOM   427  O  OD2 . ASP   A 1 52  ? -29.007 10.232  12.682  1.00 31.65 ? 52  ASP   A OD2 1 
ATOM   428  N  N   . GLN   A 1 53  ? -26.175 9.403   10.635  1.00 15.04 ? 53  GLN   A N   1 
ATOM   429  C  CA  . GLN   A 1 53  ? -25.718 10.323  9.602   1.00 15.58 ? 53  GLN   A CA  1 
ATOM   430  C  C   . GLN   A 1 53  ? -24.285 10.027  9.174   1.00 12.68 ? 53  GLN   A C   1 
ATOM   431  O  O   . GLN   A 1 53  ? -23.667 10.825  8.503   1.00 14.35 ? 53  GLN   A O   1 
ATOM   432  C  CB  . GLN   A 1 53  ? -25.890 11.763  10.082  1.00 18.38 ? 53  GLN   A CB  1 
ATOM   433  C  CG  . GLN   A 1 53  ? -27.332 12.080  10.451  1.00 21.93 ? 53  GLN   A CG  1 
ATOM   434  C  CD  . GLN   A 1 53  ? -28.223 12.084  9.236   1.00 24.19 ? 53  GLN   A CD  1 
ATOM   435  O  OE1 . GLN   A 1 53  ? -27.847 12.641  8.196   1.00 30.28 ? 53  GLN   A OE1 1 
ATOM   436  N  NE2 . GLN   A 1 53  ? -29.377 11.434  9.339   1.00 27.95 ? 53  GLN   A NE2 1 
ATOM   437  N  N   . ALA   A 1 54  ? -23.765 8.853   9.521   1.00 11.60 ? 54  ALA   A N   1 
ATOM   438  C  CA  . ALA   A 1 54  ? -22.409 8.508   9.124   1.00 12.12 ? 54  ALA   A CA  1 
ATOM   439  C  C   . ALA   A 1 54  ? -22.255 8.591   7.616   1.00 12.30 ? 54  ALA   A C   1 
ATOM   440  O  O   . ALA   A 1 54  ? -23.093 8.079   6.878   1.00 15.44 ? 54  ALA   A O   1 
ATOM   441  C  CB  . ALA   A 1 54  ? -22.012 7.130   9.602   1.00 13.24 ? 54  ALA   A CB  1 
ATOM   442  N  N   . THR   A 1 55  ? -21.169 9.214   7.170   1.00 11.18 ? 55  THR   A N   1 
ATOM   443  C  CA  . THR   A 1 55  ? -20.932 9.425   5.765   1.00 12.59 ? 55  THR   A CA  1 
ATOM   444  C  C   . THR   A 1 55  ? -19.551 8.901   5.425   1.00 10.60 ? 55  THR   A C   1 
ATOM   445  O  O   . THR   A 1 55  ? -18.541 9.547   5.650   1.00 10.65 ? 55  THR   A O   1 
ATOM   446  C  CB  . THR   A 1 55  ? -21.054 10.911  5.442   1.00 17.99 ? 55  THR   A CB  1 
ATOM   447  O  OG1 . THR   A 1 55  ? -22.247 11.498  6.000   1.00 22.61 ? 55  THR   A OG1 1 
ATOM   448  C  CG2 . THR   A 1 55  ? -20.939 10.997  3.932   1.00 19.85 ? 55  THR   A CG2 1 
ATOM   449  N  N   . SER   A 1 56  ? -19.529 7.669   4.930   1.00 10.51 ? 56  SER   A N   1 
ATOM   450  C  CA  . SER   A 1 56  ? -18.273 7.082   4.519   1.00 10.73 ? 56  SER   A CA  1 
ATOM   451  C  C   . SER   A 1 56  ? -17.836 7.732   3.222   1.00 10.66 ? 56  SER   A C   1 
ATOM   452  O  O   . SER   A 1 56  ? -18.646 8.172   2.409   1.00 12.75 ? 56  SER   A O   1 
ATOM   453  C  CB  . SER   A 1 56  ? -18.366 5.568   4.371   1.00 10.88 ? 56  SER   A CB  1 
ATOM   454  O  OG  . SER   A 1 56  ? -19.205 5.202   3.291   1.00 11.66 ? 56  SER   A OG  1 
ATOM   455  N  N   . LEU   A 1 57  ? -16.522 7.771   3.019   1.00 10.41 ? 57  LEU   A N   1 
ATOM   456  C  CA  . LEU   A 1 57  ? -15.996 8.347   1.794   1.00 11.86 ? 57  LEU   A CA  1 
ATOM   457  C  C   . LEU   A 1 57  ? -15.149 7.403   0.955   1.00 10.43 ? 57  LEU   A C   1 
ATOM   458  O  O   . LEU   A 1 57  ? -15.233 7.416   -0.268  1.00 11.43 ? 57  LEU   A O   1 
ATOM   459  C  CB  . LEU   A 1 57  ? -15.197 9.558   2.189   1.00 14.08 ? 57  LEU   A CB  1 
ATOM   460  C  CG  . LEU   A 1 57  ? -16.061 10.700  2.731   1.00 16.71 ? 57  LEU   A CG  1 
ATOM   461  C  CD1 . LEU   A 1 57  ? -15.112 11.782  3.166   1.00 18.24 ? 57  LEU   A CD1 1 
ATOM   462  C  CD2 . LEU   A 1 57  ? -17.132 11.217  1.769   1.00 18.65 ? 57  LEU   A CD2 1 
ATOM   463  N  N   . ARG   A 1 58  ? -14.279 6.628   1.580   1.00 9.98  ? 58  ARG   A N   1 
ATOM   464  C  CA  . ARG   A 1 58  ? -13.207 5.998   0.840   1.00 9.74  ? 58  ARG   A CA  1 
ATOM   465  C  C   . ARG   A 1 58  ? -12.705 4.816   1.654   1.00 8.83  ? 58  ARG   A C   1 
ATOM   466  O  O   . ARG   A 1 58  ? -12.813 4.805   2.869   1.00 9.14  ? 58  ARG   A O   1 
ATOM   467  C  CB  . ARG   A 1 58  ? -12.041 6.964   0.640   1.00 11.36 ? 58  ARG   A CB  1 
ATOM   468  C  CG  . ARG   A 1 58  ? -10.931 6.571   -0.317  1.00 12.65 ? 58  ARG   A CG  1 
ATOM   469  C  CD  . ARG   A 1 58  ? -9.924  7.669   -0.467  1.00 13.40 ? 58  ARG   A CD  1 
ATOM   470  N  NE  . ARG   A 1 58  ? -9.079  7.780   0.734   1.00 12.65 ? 58  ARG   A NE  1 
ATOM   471  C  CZ  . ARG   A 1 58  ? -7.748  7.943   0.689   1.00 12.52 ? 58  ARG   A CZ  1 
ATOM   472  N  NH1 . ARG   A 1 58  ? -7.163  8.231   -0.452  1.00 14.51 ? 58  ARG   A NH1 1 
ATOM   473  N  NH2 . ARG   A 1 58  ? -7.055  7.917   1.808   1.00 11.82 ? 58  ARG   A NH2 1 
ATOM   474  N  N   . ILE   A 1 59  ? -12.086 3.853   0.974   1.00 8.29  ? 59  ILE   A N   1 
ATOM   475  C  CA  . ILE   A 1 59  ? -11.412 2.732   1.604   1.00 8.11  ? 59  ILE   A CA  1 
ATOM   476  C  C   . ILE   A 1 59  ? -9.982  2.715   1.085   1.00 8.39  ? 59  ILE   A C   1 
ATOM   477  O  O   . ILE   A 1 59  ? -9.748  2.902   -0.123  1.00 9.61  ? 59  ILE   A O   1 
ATOM   478  C  CB  . ILE   A 1 59  ? -12.181 1.407   1.394   1.00 8.22  ? 59  ILE   A CB  1 
ATOM   479  C  CG1 . ILE   A 1 59  ? -11.628 0.306   2.276   1.00 8.81  ? 59  ILE   A CG1 1 
ATOM   480  C  CG2 . ILE   A 1 59  ? -12.250 1.028   -0.072  1.00 9.04  ? 59  ILE   A CG2 1 
ATOM   481  C  CD1 . ILE   A 1 59  ? -12.431 -0.967  2.216   1.00 8.90  ? 59  ILE   A CD1 1 
ATOM   482  N  N   . LEU   A 1 60  ? -9.031  2.555   2.001   1.00 8.07  ? 60  LEU   A N   1 
ATOM   483  C  CA  . LEU   A 1 60  ? -7.631  2.706   1.746   1.00 8.10  ? 60  LEU   A CA  1 
ATOM   484  C  C   . LEU   A 1 60  ? -6.841  1.491   2.267   1.00 8.03  ? 60  LEU   A C   1 
ATOM   485  O  O   . LEU   A 1 60  ? -6.938  1.171   3.427   1.00 8.51  ? 60  LEU   A O   1 
ATOM   486  C  CB  . LEU   A 1 60  ? -7.071  3.983   2.406   1.00 9.43  ? 60  LEU   A CB  1 
ATOM   487  C  CG  . LEU   A 1 60  ? -5.549  4.125   2.353   1.00 9.36  ? 60  LEU   A CG  1 
ATOM   488  C  CD1 . LEU   A 1 60  ? -5.023  4.398   0.960   1.00 10.65 ? 60  LEU   A CD1 1 
ATOM   489  C  CD2 . LEU   A 1 60  ? -5.118  5.196   3.357   1.00 10.11 ? 60  LEU   A CD2 1 
ATOM   490  N  N   . ASN   A 1 61  ? -5.962  0.861   1.452   1.00 8.11  ? 61  ASN   A N   1 
ATOM   491  C  CA  . ASN   A 1 61  ? -4.959  -0.095  1.919   1.00 8.14  ? 61  ASN   A CA  1 
ATOM   492  C  C   . ASN   A 1 61  ? -3.700  0.701   2.294   1.00 8.00  ? 61  ASN   A C   1 
ATOM   493  O  O   . ASN   A 1 61  ? -3.069  1.261   1.412   1.00 9.03  ? 61  ASN   A O   1 
ATOM   494  C  CB  . ASN   A 1 61  ? -4.661  -1.130  0.841   1.00 8.39  ? 61  ASN   A CB  1 
ATOM   495  C  CG  . ASN   A 1 61  ? -3.615  -2.133  1.266   1.00 8.07  ? 61  ASN   A CG  1 
ATOM   496  O  OD1 . ASN   A 1 61  ? -2.746  -1.858  2.122   1.00 8.95  ? 61  ASN   A OD1 1 
ATOM   497  N  ND2 . ASN   A 1 61  ? -3.645  -3.333  0.670   1.00 8.55  ? 61  ASN   A ND2 1 
ATOM   498  N  N   . ASN   A 1 62  ? -3.399  0.788   3.587   1.00 7.86  ? 62  ASN   A N   1 
ATOM   499  C  CA  . ASN   A 1 62  ? -2.296  1.609   4.044   1.00 9.16  ? 62  ASN   A CA  1 
ATOM   500  C  C   . ASN   A 1 62  ? -1.027  0.785   4.256   1.00 9.04  ? 62  ASN   A C   1 
ATOM   501  O  O   . ASN   A 1 62  ? -0.057  1.304   4.818   1.00 10.73 ? 62  ASN   A O   1 
ATOM   502  C  CB  . ASN   A 1 62  ? -2.632  2.435   5.273   1.00 9.48  ? 62  ASN   A CB  1 
ATOM   503  C  CG  . ASN   A 1 62  ? -3.001  1.584   6.448   1.00 9.57  ? 62  ASN   A CG  1 
ATOM   504  O  OD1 . ASN   A 1 62  ? -2.612  0.415   6.513   1.00 9.25  ? 62  ASN   A OD1 1 
ATOM   505  N  ND2 . ASN   A 1 62  ? -3.783  2.151   7.360   1.00 11.91 ? 62  ASN   A ND2 1 
ATOM   506  N  N   . GLY   A 1 63  ? -1.005  -0.473  3.821   1.00 9.40  ? 63  GLY   A N   1 
ATOM   507  C  CA  . GLY   A 1 63  ? 0.139   -1.330  4.006   1.00 9.67  ? 63  GLY   A CA  1 
ATOM   508  C  C   . GLY   A 1 63  ? 0.203   -2.040  5.365   1.00 9.44  ? 63  GLY   A C   1 
ATOM   509  O  O   . GLY   A 1 63  ? 1.078   -2.889  5.547   1.00 10.97 ? 63  GLY   A O   1 
ATOM   510  N  N   . HIS   A 1 64  ? -0.724  -1.742  6.262   1.00 9.28  ? 64  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 64  ? -0.825  -2.380  7.574   1.00 9.73  ? 64  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 64  ? -2.213  -2.982  7.801   1.00 9.03  ? 64  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 64  ? -2.321  -3.981  8.515   1.00 12.64 ? 64  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 64  ? -0.493  -1.371  8.676   1.00 10.50 ? 64  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 64  ? 0.756   -0.579  8.452   1.00 13.01 ? 64  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 64  ? 2.021   -1.132  8.523   1.00 14.68 ? 64  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 64  ? 0.953   0.713   8.210   1.00 14.32 ? 64  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 64  ? 2.932   -0.171  8.329   1.00 14.65 ? 64  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 64  ? 2.297   0.941   8.074   1.00 14.61 ? 64  HIS   A NE2 1 
ATOM   520  N  N   . ALA   A 1 65  ? -3.238  -2.332  7.279   1.00 8.27  ? 65  ALA   A N   1 
ATOM   521  C  CA  . ALA   A 1 65  ? -4.620  -2.800  7.294   1.00 7.74  ? 65  ALA   A CA  1 
ATOM   522  C  C   . ALA   A 1 65  ? -5.331  -2.060  6.165   1.00 7.43  ? 65  ALA   A C   1 
ATOM   523  O  O   . ALA   A 1 65  ? -4.660  -1.441  5.328   1.00 8.81  ? 65  ALA   A O   1 
ATOM   524  C  CB  . ALA   A 1 65  ? -5.238  -2.567  8.670   1.00 8.34  ? 65  ALA   A CB  1 
ATOM   525  N  N   . PHE   A 1 66  ? -6.646  -2.083  6.167   1.00 7.64  ? 66  PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 66  ? -7.408  -1.155  5.337   1.00 7.64  ? 66  PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 66  ? -8.324  -0.304  6.201   1.00 7.82  ? 66  PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 66  ? -8.936  -0.795  7.164   1.00 8.29  ? 66  PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 66  ? -8.180  -1.876  4.226   1.00 8.65  ? 66  PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 66  ? -9.250  -2.828  4.691   1.00 8.64  ? 66  PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 66  ? -10.527 -2.371  5.049   1.00 9.27  ? 66  PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 66  ? -8.953  -4.184  4.823   1.00 9.06  ? 66  PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 66  ? -11.483 -3.246  5.509   1.00 10.05 ? 66  PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 66  ? -9.937  -5.063  5.301   1.00 9.84  ? 66  PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 66  ? -11.200 -4.586  5.632   1.00 9.65  ? 66  PHE   A CZ  1 
ATOM   536  N  N   . ASN   A 1 67  ? -8.408  0.983   5.885   1.00 7.77  ? 67  ASN   A N   1 
ATOM   537  C  CA  . ASN   A 1 67  ? -9.285  1.898   6.618   1.00 7.68  ? 67  ASN   A CA  1 
ATOM   538  C  C   . ASN   A 1 67  ? -10.490 2.285   5.770   1.00 7.36  ? 67  ASN   A C   1 
ATOM   539  O  O   . ASN   A 1 67  ? -10.319 2.707   4.609   1.00 8.30  ? 67  ASN   A O   1 
ATOM   540  C  CB  . ASN   A 1 67  ? -8.561  3.190   6.992   1.00 8.50  ? 67  ASN   A CB  1 
ATOM   541  C  CG  . ASN   A 1 67  ? -7.484  3.026   8.013   1.00 10.14 ? 67  ASN   A CG  1 
ATOM   542  O  OD1 . ASN   A 1 67  ? -6.652  3.931   8.203   1.00 14.34 ? 67  ASN   A OD1 1 
ATOM   543  N  ND2 . ASN   A 1 67  ? -7.392  1.897   8.634   1.00 9.74  ? 67  ASN   A ND2 1 
ATOM   544  N  N   . VAL   A 1 68  ? -11.686 2.188   6.345   1.00 7.35  ? 68  VAL   A N   1 
ATOM   545  C  CA  . VAL   A 1 68  ? -12.883 2.831   5.815   1.00 7.22  ? 68  VAL   A CA  1 
ATOM   546  C  C   . VAL   A 1 68  ? -12.971 4.189   6.483   1.00 7.57  ? 68  VAL   A C   1 
ATOM   547  O  O   . VAL   A 1 68  ? -13.091 4.283   7.713   1.00 7.82  ? 68  VAL   A O   1 
ATOM   548  C  CB  . VAL   A 1 68  ? -14.141 1.998   6.001   1.00 8.34  ? 68  VAL   A CB  1 
ATOM   549  C  CG1 . VAL   A 1 68  ? -15.353 2.800   5.569   1.00 8.88  ? 68  VAL   A CG1 1 
ATOM   550  C  CG2 . VAL   A 1 68  ? -14.029 0.703   5.214   1.00 9.27  ? 68  VAL   A CG2 1 
ATOM   551  N  N   . GLU   A 1 69  ? -12.854 5.248   5.688   1.00 8.32  ? 69  GLU   A N   1 
ATOM   552  C  CA  . GLU   A 1 69  ? -12.762 6.604   6.175   1.00 8.52  ? 69  GLU   A CA  1 
ATOM   553  C  C   . GLU   A 1 69  ? -14.105 7.318   6.072   1.00 8.26  ? 69  GLU   A C   1 
ATOM   554  O  O   . GLU   A 1 69  ? -14.842 7.084   5.113   1.00 9.70  ? 69  GLU   A O   1 
ATOM   555  C  CB  . GLU   A 1 69  ? -11.760 7.353   5.299   1.00 9.83  ? 69  GLU   A CB  1 
ATOM   556  C  CG  . GLU   A 1 69  ? -10.378 6.740   5.343   1.00 10.30 ? 69  GLU   A CG  1 
ATOM   557  C  CD  . GLU   A 1 69  ? -9.524  7.249   4.201   1.00 12.01 ? 69  GLU   A CD  1 
ATOM   558  O  OE1 . GLU   A 1 69  ? -10.025 7.952   3.270   1.00 13.17 ? 69  GLU   A OE1 1 
ATOM   559  O  OE2 . GLU   A 1 69  ? -8.307  6.945   4.206   1.00 13.27 ? 69  GLU   A OE2 1 
ATOM   560  N  N   . PHE   A 1 70  ? -14.347 8.197   7.042   1.00 8.29  ? 70  PHE   A N   1 
ATOM   561  C  CA  . PHE   A 1 70  ? -15.599 8.933   7.130   1.00 8.71  ? 70  PHE   A CA  1 
ATOM   562  C  C   . PHE   A 1 70  ? -15.335 10.423  7.026   1.00 9.85  ? 70  PHE   A C   1 
ATOM   563  O  O   . PHE   A 1 70  ? -14.271 10.926  7.404   1.00 11.11 ? 70  PHE   A O   1 
ATOM   564  C  CB  . PHE   A 1 70  ? -16.270 8.626   8.467   1.00 8.91  ? 70  PHE   A CB  1 
ATOM   565  C  CG  . PHE   A 1 70  ? -16.836 7.216   8.463   1.00 8.65  ? 70  PHE   A CG  1 
ATOM   566  C  CD1 . PHE   A 1 70  ? -16.009 6.116   8.680   1.00 8.78  ? 70  PHE   A CD1 1 
ATOM   567  C  CD2 . PHE   A 1 70  ? -18.160 6.980   8.144   1.00 9.01  ? 70  PHE   A CD2 1 
ATOM   568  C  CE1 . PHE   A 1 70  ? -16.501 4.849   8.570   1.00 9.44  ? 70  PHE   A CE1 1 
ATOM   569  C  CE2 . PHE   A 1 70  ? -18.655 5.705   8.043   1.00 9.92  ? 70  PHE   A CE2 1 
ATOM   570  C  CZ  . PHE   A 1 70  ? -17.836 4.646   8.274   1.00 10.03 ? 70  PHE   A CZ  1 
ATOM   571  N  N   . ASP   A 1 71  ? -16.334 11.128  6.548   1.00 11.84 ? 71  ASP   A N   1 
ATOM   572  C  CA  . ASP   A 1 71  ? -16.351 12.577  6.601   1.00 13.56 ? 71  ASP   A CA  1 
ATOM   573  C  C   . ASP   A 1 71  ? -16.629 12.998  8.034   1.00 13.66 ? 71  ASP   A C   1 
ATOM   574  O  O   . ASP   A 1 71  ? -17.732 12.811  8.540   1.00 17.36 ? 71  ASP   A O   1 
ATOM   575  C  CB  . ASP   A 1 71  ? -17.445 13.117  5.716   1.00 17.28 ? 71  ASP   A CB  1 
ATOM   576  C  CG  . ASP   A 1 71  ? -17.627 14.623  5.775   1.00 20.64 ? 71  ASP   A CG  1 
ATOM   577  O  OD1 . ASP   A 1 71  ? -16.833 15.275  6.445   1.00 19.77 ? 71  ASP   A OD1 1 
ATOM   578  O  OD2 . ASP   A 1 71  ? -18.544 15.140  5.101   1.00 26.27 ? 71  ASP   A OD2 1 
ATOM   579  N  N   . ASP   A 1 72  ? -15.606 13.525  8.692   1.00 12.95 ? 72  ASP   A N   1 
ATOM   580  C  CA  . ASP   A 1 72  ? -15.687 13.950  10.084  1.00 12.81 ? 72  ASP   A CA  1 
ATOM   581  C  C   . ASP   A 1 72  ? -15.664 15.474  10.185  1.00 14.06 ? 72  ASP   A C   1 
ATOM   582  O  O   . ASP   A 1 72  ? -15.299 16.000  11.224  1.00 15.15 ? 72  ASP   A O   1 
ATOM   583  C  CB  . ASP   A 1 72  ? -14.596 13.287  10.916  1.00 12.93 ? 72  ASP   A CB  1 
ATOM   584  C  CG  . ASP   A 1 72  ? -13.207 13.801  10.600  1.00 13.64 ? 72  ASP   A CG  1 
ATOM   585  O  OD1 . ASP   A 1 72  ? -13.074 14.477  9.553   1.00 16.99 ? 72  ASP   A OD1 1 
ATOM   586  O  OD2 . ASP   A 1 72  ? -12.308 13.520  11.374  1.00 14.66 ? 72  ASP   A OD2 1 
ATOM   587  N  N   . SER   A 1 73  ? -16.103 16.188  9.141   1.00 15.58 ? 73  SER   A N   1 
ATOM   588  C  CA  . SER   A 1 73  ? -16.080 17.649  9.094   1.00 16.66 ? 73  SER   A CA  1 
ATOM   589  C  C   . SER   A 1 73  ? -17.319 18.271  9.737   1.00 17.62 ? 73  SER   A C   1 
ATOM   590  O  O   . SER   A 1 73  ? -17.359 19.491  9.955   1.00 18.16 ? 73  SER   A O   1 
ATOM   591  C  CB  . SER   A 1 73  ? -15.957 18.161  7.683   1.00 18.13 ? 73  SER   A CB  1 
ATOM   592  O  OG  . SER   A 1 73  ? -17.160 17.895  6.975   1.00 19.58 ? 73  SER   A OG  1 
ATOM   593  N  N   . GLN   A 1 74  ? -18.323 17.444  10.029  1.00 19.76 ? 74  GLN   A N   1 
ATOM   594  C  CA  . GLN   A 1 74  ? -19.548 17.902  10.658  1.00 20.12 ? 74  GLN   A CA  1 
ATOM   595  C  C   . GLN   A 1 74  ? -19.869 16.939  11.791  1.00 20.65 ? 74  GLN   A C   1 
ATOM   596  O  O   . GLN   A 1 74  ? -19.324 15.812  11.888  1.00 16.85 ? 74  GLN   A O   1 
ATOM   597  C  CB  . GLN   A 1 74  ? -20.714 17.922  9.666   1.00 21.35 ? 74  GLN   A CB  1 
ATOM   598  C  CG  . GLN   A 1 74  ? -20.698 19.062  8.654   1.00 26.24 ? 74  GLN   A CG  1 
ATOM   599  C  CD  . GLN   A 1 74  ? -21.808 18.898  7.642   1.00 30.27 ? 74  GLN   A CD  1 
ATOM   600  O  OE1 . GLN   A 1 74  ? -22.989 18.880  7.994   1.00 38.44 ? 74  GLN   A OE1 1 
ATOM   601  N  NE2 . GLN   A 1 74  ? -21.443 18.722  6.384   1.00 32.83 ? 74  GLN   A NE2 1 
ATOM   602  N  N   . ASP   A 1 75  ? -20.866 17.366  12.569  1.00 23.12 ? 75  ASP   A N   1 
ATOM   603  C  CA  . ASP   A 1 75  ? -21.305 16.615  13.725  1.00 22.44 ? 75  ASP   A CA  1 
ATOM   604  C  C   . ASP   A 1 75  ? -22.234 15.467  13.267  1.00 21.84 ? 75  ASP   A C   1 
ATOM   605  O  O   . ASP   A 1 75  ? -23.451 15.705  13.202  1.00 21.72 ? 75  ASP   A O   1 
ATOM   606  C  CB  . ASP   A 1 75  ? -21.922 17.623  14.688  1.00 25.30 ? 75  ASP   A CB  1 
ATOM   607  C  CG  . ASP   A 1 75  ? -22.542 17.032  15.940  1.00 27.42 ? 75  ASP   A CG  1 
ATOM   608  O  OD1 . ASP   A 1 75  ? -22.291 15.843  16.174  1.00 27.56 ? 75  ASP   A OD1 1 
ATOM   609  O  OD2 . ASP   A 1 75  ? -23.292 17.757  16.642  1.00 31.96 ? 75  ASP   A OD2 1 
ATOM   610  N  N   . LYS   A 1 76  ? -21.726 14.222  12.991  1.00 19.87 ? 76  LYS   A N   1 
ATOM   611  C  CA  . LYS   A 1 76  ? -22.521 13.211  12.234  1.00 20.44 ? 76  LYS   A CA  1 
ATOM   612  C  C   . LYS   A 1 76  ? -22.656 11.699  12.582  1.00 20.76 ? 76  LYS   A C   1 
ATOM   613  O  O   . LYS   A 1 76  ? -23.640 11.046  12.221  1.00 25.48 ? 76  LYS   A O   1 
ATOM   614  C  CB  . LYS   A 1 76  ? -21.991 13.084  10.807  1.00 19.18 ? 76  LYS   A CB  1 
ATOM   615  C  CG  . LYS   A 1 76  ? -22.216 14.313  9.951   1.00 23.28 ? 76  LYS   A CG  1 
ATOM   616  C  CD  . LYS   A 1 76  ? -21.828 14.047  8.497   1.00 28.53 ? 76  LYS   A CD  1 
ATOM   617  C  CE  . LYS   A 1 76  ? -22.052 15.136  7.491   1.00 32.63 ? 76  LYS   A CE  1 
ATOM   618  N  NZ  . LYS   A 1 76  ? -21.806 14.665  6.123   1.00 35.65 ? 76  LYS   A NZ  1 
ATOM   619  N  N   . ALA   A 1 77  ? -21.596 11.081  13.008  1.00 17.29 ? 77  ALA   A N   1 
ATOM   620  C  CA  . ALA   A 1 77  ? -21.479 9.740   13.567  1.00 11.30 ? 77  ALA   A CA  1 
ATOM   621  C  C   . ALA   A 1 77  ? -20.686 9.886   14.847  1.00 10.16 ? 77  ALA   A C   1 
ATOM   622  O  O   . ALA   A 1 77  ? -19.472 10.113  14.819  1.00 14.02 ? 77  ALA   A O   1 
ATOM   623  C  CB  . ALA   A 1 77  ? -20.753 8.913   12.547  1.00 13.38 ? 77  ALA   A CB  1 
ATOM   624  N  N   . VAL   A 1 78  ? -21.363 9.801   15.974  1.00 10.09 ? 78  VAL   A N   1 
ATOM   625  C  CA  . VAL   A 1 78  ? -20.676 10.055  17.196  1.00 10.97 ? 78  VAL   A CA  1 
ATOM   626  C  C   . VAL   A 1 78  ? -20.937 8.966   18.218  1.00 9.96  ? 78  VAL   A C   1 
ATOM   627  O  O   . VAL   A 1 78  ? -21.940 8.263   18.199  1.00 11.85 ? 78  VAL   A O   1 
ATOM   628  C  CB  . VAL   A 1 78  ? -20.989 11.423  17.780  1.00 13.84 ? 78  VAL   A CB  1 
ATOM   629  C  CG1 . VAL   A 1 78  ? -20.695 12.553  16.822  1.00 14.70 ? 78  VAL   A CG1 1 
ATOM   630  C  CG2 . VAL   A 1 78  ? -22.421 11.482  18.161  1.00 15.00 ? 78  VAL   A CG2 1 
ATOM   631  N  N   . LEU   A 1 79  ? -19.990 8.876   19.119  1.00 8.27  ? 79  LEU   A N   1 
ATOM   632  C  CA  . LEU   A 1 79  ? -20.003 7.996   20.253  1.00 8.72  ? 79  LEU   A CA  1 
ATOM   633  C  C   . LEU   A 1 79  ? -19.980 8.869   21.494  1.00 8.54  ? 79  LEU   A C   1 
ATOM   634  O  O   . LEU   A 1 79  ? -19.156 9.781   21.593  1.00 9.52  ? 79  LEU   A O   1 
ATOM   635  C  CB  . LEU   A 1 79  ? -18.744 7.116   20.176  1.00 9.98  ? 79  LEU   A CB  1 
ATOM   636  C  CG  . LEU   A 1 79  ? -18.592 6.010   21.223  1.00 10.34 ? 79  LEU   A CG  1 
ATOM   637  C  CD1 . LEU   A 1 79  ? -19.700 4.988   21.089  1.00 11.69 ? 79  LEU   A CD1 1 
ATOM   638  C  CD2 . LEU   A 1 79  ? -17.229 5.342   21.079  1.00 9.95  ? 79  LEU   A CD2 1 
ATOM   639  N  N   . LYS   A 1 80  ? -20.870 8.576   22.436  1.00 9.06  ? 80  LYS   A N   1 
ATOM   640  C  CA  . LYS   A 1 80  ? -20.954 9.298   23.682  1.00 10.08 ? 80  LYS   A CA  1 
ATOM   641  C  C   . LYS   A 1 80  ? -21.410 8.332   24.762  1.00 8.95  ? 80  LYS   A C   1 
ATOM   642  O  O   . LYS   A 1 80  ? -21.770 7.183   24.502  1.00 9.29  ? 80  LYS   A O   1 
ATOM   643  C  CB  . LYS   A 1 80  ? -21.998 10.425  23.568  1.00 13.37 ? 80  LYS   A CB  1 
ATOM   644  C  CG  . LYS   A 1 80  ? -21.919 11.385  22.426  1.00 16.97 ? 80  LYS   A CG  1 
ATOM   645  C  CD  . LYS   A 1 80  ? -23.093 12.345  22.351  1.00 21.94 ? 80  LYS   A CD  1 
ATOM   646  C  CE  . LYS   A 1 80  ? -23.348 13.101  23.617  1.00 26.01 ? 80  LYS   A CE  1 
ATOM   647  N  NZ  . LYS   A 1 80  ? -24.061 14.363  23.418  1.00 30.01 ? 80  LYS   A NZ  1 
ATOM   648  N  N   . GLY   A 1 81  ? -21.382 8.810   26.011  1.00 9.38  ? 81  GLY   A N   1 
ATOM   649  C  CA  . GLY   A 1 81  ? -21.868 8.036   27.131  1.00 10.00 ? 81  GLY   A CA  1 
ATOM   650  C  C   . GLY   A 1 81  ? -20.869 6.967   27.541  1.00 9.04  ? 81  GLY   A C   1 
ATOM   651  O  O   . GLY   A 1 81  ? -19.683 7.074   27.260  1.00 9.07  ? 81  GLY   A O   1 
ATOM   652  N  N   . GLY   A 1 82  ? -21.344 6.012   28.354  1.00 9.48  ? 82  GLY   A N   1 
ATOM   653  C  CA  . GLY   A 1 82  ? -20.436 5.014   28.895  1.00 9.66  ? 82  GLY   A CA  1 
ATOM   654  C  C   . GLY   A 1 82  ? -19.402 5.687   29.778  1.00 9.66  ? 82  GLY   A C   1 
ATOM   655  O  O   . GLY   A 1 82  ? -19.775 6.489   30.646  1.00 11.28 ? 82  GLY   A O   1 
ATOM   656  N  N   . PRO   A 1 83  ? -18.109 5.421   29.543  1.00 9.13  ? 83  PRO   A N   1 
ATOM   657  C  CA  . PRO   A 1 83  ? -17.070 6.072   30.314  1.00 10.05 ? 83  PRO   A CA  1 
ATOM   658  C  C   . PRO   A 1 83  ? -16.754 7.479   29.845  1.00 10.13 ? 83  PRO   A C   1 
ATOM   659  O  O   . PRO   A 1 83  ? -15.966 8.180   30.477  1.00 13.55 ? 83  PRO   A O   1 
ATOM   660  C  CB  . PRO   A 1 83  ? -15.906 5.132   30.094  1.00 10.42 ? 83  PRO   A CB  1 
ATOM   661  C  CG  . PRO   A 1 83  ? -16.068 4.640   28.675  1.00 9.78  ? 83  PRO   A CG  1 
ATOM   662  C  CD  . PRO   A 1 83  ? -17.576 4.507   28.516  1.00 9.34  ? 83  PRO   A CD  1 
ATOM   663  N  N   . LEU   A 1 84  ? -17.321 7.900   28.699  1.00 8.65  ? 84  LEU   A N   1 
ATOM   664  C  CA  . LEU   A 1 84  ? -16.841 9.079   27.993  1.00 8.69  ? 84  LEU   A CA  1 
ATOM   665  C  C   . LEU   A 1 84  ? -17.489 10.345  28.534  1.00 9.99  ? 84  LEU   A C   1 
ATOM   666  O  O   . LEU   A 1 84  ? -18.691 10.398  28.809  1.00 11.54 ? 84  LEU   A O   1 
ATOM   667  C  CB  . LEU   A 1 84  ? -17.179 8.947   26.513  1.00 7.65  ? 84  LEU   A CB  1 
ATOM   668  C  CG  . LEU   A 1 84  ? -16.633 7.700   25.820  1.00 7.50  ? 84  LEU   A CG  1 
ATOM   669  C  CD1 . LEU   A 1 84  ? -17.188 7.621   24.444  1.00 8.44  ? 84  LEU   A CD1 1 
ATOM   670  C  CD2 . LEU   A 1 84  ? -15.093 7.675   25.840  1.00 7.75  ? 84  LEU   A CD2 1 
ATOM   671  N  N   . ASP   A 1 85  ? -16.683 11.382  28.616  1.00 10.98 ? 85  ASP   A N   1 
ATOM   672  C  CA  . ASP   A 1 85  ? -17.151 12.731  28.849  1.00 13.27 ? 85  ASP   A CA  1 
ATOM   673  C  C   . ASP   A 1 85  ? -17.167 13.414  27.480  1.00 13.87 ? 85  ASP   A C   1 
ATOM   674  O  O   . ASP   A 1 85  ? -16.157 13.434  26.777  1.00 15.55 ? 85  ASP   A O   1 
ATOM   675  C  CB  . ASP   A 1 85  ? -16.253 13.416  29.876  1.00 16.51 ? 85  ASP   A CB  1 
ATOM   676  C  CG  . ASP   A 1 85  ? -16.380 12.886  31.303  1.00 20.85 ? 85  ASP   A CG  1 
ATOM   677  O  OD1 . ASP   A 1 85  ? -17.356 12.135  31.567  1.00 26.34 ? 85  ASP   A OD1 1 
ATOM   678  O  OD2 . ASP   A 1 85  ? -15.528 13.253  32.171  1.00 25.46 ? 85  ASP   A OD2 1 
ATOM   679  N  N   . GLY   A 1 86  ? -18.303 13.968  27.086  1.00 15.58 ? 86  GLY   A N   1 
ATOM   680  C  CA  . GLY   A 1 86  ? -18.384 14.710  25.844  1.00 15.45 ? 86  GLY   A CA  1 
ATOM   681  C  C   . GLY   A 1 86  ? -18.642 13.794  24.651  1.00 13.90 ? 86  GLY   A C   1 
ATOM   682  O  O   . GLY   A 1 86  ? -19.233 12.729  24.757  1.00 16.81 ? 86  GLY   A O   1 
ATOM   683  N  N   A THR   A 1 87  ? -18.197 14.237  23.477  0.50 11.55 ? 87  THR   A N   1 
ATOM   684  N  N   B THR   A 1 87  ? -18.256 14.298  23.470  0.50 11.09 ? 87  THR   A N   1 
ATOM   685  C  CA  A THR   A 1 87  ? -18.645 13.599  22.253  0.50 11.00 ? 87  THR   A CA  1 
ATOM   686  C  CA  B THR   A 1 87  ? -18.653 13.762  22.174  0.50 9.96  ? 87  THR   A CA  1 
ATOM   687  C  C   A THR   A 1 87  ? -17.441 13.322  21.358  0.50 9.06  ? 87  THR   A C   1 
ATOM   688  C  C   B THR   A 1 87  ? -17.388 13.294  21.466  0.50 8.32  ? 87  THR   A C   1 
ATOM   689  O  O   A THR   A 1 87  ? -16.585 14.174  21.088  0.50 9.21  ? 87  THR   A O   1 
ATOM   690  O  O   B THR   A 1 87  ? -16.412 14.059  21.449  0.50 8.78  ? 87  THR   A O   1 
ATOM   691  C  CB  A THR   A 1 87  ? -19.705 14.454  21.574  0.50 12.76 ? 87  THR   A CB  1 
ATOM   692  C  CB  B THR   A 1 87  ? -19.315 14.856  21.336  0.50 10.35 ? 87  THR   A CB  1 
ATOM   693  O  OG1 A THR   A 1 87  ? -19.134 15.745  21.472  0.50 14.39 ? 87  THR   A OG1 1 
ATOM   694  O  OG1 B THR   A 1 87  ? -20.437 15.286  22.094  0.50 12.34 ? 87  THR   A OG1 1 
ATOM   695  C  CG2 A THR   A 1 87  ? -20.942 14.667  22.417  0.50 13.07 ? 87  THR   A CG2 1 
ATOM   696  C  CG2 B THR   A 1 87  ? -19.769 14.319  19.995  0.50 10.32 ? 87  THR   A CG2 1 
ATOM   697  N  N   . TYR   A 1 88  ? -17.450 12.109  20.839  1.00 7.61  ? 88  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? -16.340 11.606  20.052  1.00 7.53  ? 88  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? -16.854 11.307  18.659  1.00 7.45  ? 88  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? -17.825 10.570  18.469  1.00 9.87  ? 88  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? -15.753 10.369  20.717  1.00 7.38  ? 88  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? -14.987 10.636  21.984  1.00 6.35  ? 88  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? -15.603 11.013  23.175  1.00 6.83  ? 88  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? -13.610 10.473  22.019  1.00 6.02  ? 88  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? -14.879 11.212  24.333  1.00 6.78  ? 88  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? -12.872 10.652  23.168  1.00 6.45  ? 88  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? -13.506 10.978  24.341  1.00 5.84  ? 88  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -12.808 11.093  25.498  1.00 6.53  ? 88  TYR   A OH  1 
ATOM   709  N  N   . ARG   A 1 89  ? -16.160 11.800  17.649  1.00 6.44  ? 89  ARG   A N   1 
ATOM   710  C  CA  . ARG   A 1 89  ? -16.633 11.716  16.272  1.00 6.75  ? 89  ARG   A CA  1 
ATOM   711  C  C   . ARG   A 1 89  ? -15.900 10.602  15.533  1.00 6.07  ? 89  ARG   A C   1 
ATOM   712  O  O   . ARG   A 1 89  ? -14.652 10.514  15.574  1.00 6.53  ? 89  ARG   A O   1 
ATOM   713  C  CB  . ARG   A 1 89  ? -16.343 13.051  15.599  1.00 8.53  ? 89  ARG   A CB  1 
ATOM   714  C  CG  . ARG   A 1 89  ? -17.017 13.228  14.256  1.00 10.44 ? 89  ARG   A CG  1 
ATOM   715  C  CD  . ARG   A 1 89  ? -16.801 14.624  13.694  1.00 12.04 ? 89  ARG   A CD  1 
ATOM   716  N  NE  . ARG   A 1 89  ? -17.429 15.643  14.536  1.00 14.29 ? 89  ARG   A NE  1 
ATOM   717  C  CZ  . ARG   A 1 89  ? -17.371 16.933  14.301  1.00 14.70 ? 89  ARG   A CZ  1 
ATOM   718  N  NH1 . ARG   A 1 89  ? -16.609 17.396  13.337  1.00 15.42 ? 89  ARG   A NH1 1 
ATOM   719  N  NH2 . ARG   A 1 89  ? -17.982 17.796  15.093  1.00 14.66 ? 89  ARG   A NH2 1 
ATOM   720  N  N   . LEU   A 1 90  ? -16.642 9.763   14.799  1.00 6.68  ? 90  LEU   A N   1 
ATOM   721  C  CA  . LEU   A 1 90  ? -16.051 8.690   14.009  1.00 6.72  ? 90  LEU   A CA  1 
ATOM   722  C  C   . LEU   A 1 90  ? -15.226 9.257   12.857  1.00 6.77  ? 90  LEU   A C   1 
ATOM   723  O  O   . LEU   A 1 90  ? -15.722 10.081  12.074  1.00 8.63  ? 90  LEU   A O   1 
ATOM   724  C  CB  . LEU   A 1 90  ? -17.180 7.830   13.455  1.00 7.22  ? 90  LEU   A CB  1 
ATOM   725  C  CG  . LEU   A 1 90  ? -16.775 6.640   12.585  1.00 7.97  ? 90  LEU   A CG  1 
ATOM   726  C  CD1 . LEU   A 1 90  ? -15.970 5.593   13.362  1.00 8.39  ? 90  LEU   A CD1 1 
ATOM   727  C  CD2 . LEU   A 1 90  ? -18.024 6.032   11.974  1.00 9.08  ? 90  LEU   A CD2 1 
ATOM   728  N  N   . ILE   A 1 91  ? -13.994 8.767   12.733  1.00 6.57  ? 91  ILE   A N   1 
ATOM   729  C  CA  . ILE   A 1 91  ? -13.100 9.136   11.644  1.00 6.83  ? 91  ILE   A CA  1 
ATOM   730  C  C   . ILE   A 1 91  ? -12.793 7.965   10.717  1.00 6.31  ? 91  ILE   A C   1 
ATOM   731  O  O   . ILE   A 1 91  ? -12.687 8.175   9.507   1.00 6.80  ? 91  ILE   A O   1 
ATOM   732  C  CB  . ILE   A 1 91  ? -11.828 9.835   12.168  1.00 7.16  ? 91  ILE   A CB  1 
ATOM   733  C  CG1 . ILE   A 1 91  ? -10.927 10.298  11.033  1.00 9.28  ? 91  ILE   A CG1 1 
ATOM   734  C  CG2 . ILE   A 1 91  ? -11.068 8.973   13.178  1.00 7.23  ? 91  ILE   A CG2 1 
ATOM   735  C  CD1 . ILE   A 1 91  ? -9.877  11.302  11.457  1.00 10.73 ? 91  ILE   A CD1 1 
ATOM   736  N  N   . GLN   A 1 92  ? -12.666 6.746   11.233  1.00 6.10  ? 92  GLN   A N   1 
ATOM   737  C  CA  . GLN   A 1 92  ? -12.359 5.606   10.380  1.00 6.09  ? 92  GLN   A CA  1 
ATOM   738  C  C   . GLN   A 1 92  ? -12.627 4.332   11.157  1.00 5.79  ? 92  GLN   A C   1 
ATOM   739  O  O   . GLN   A 1 92  ? -12.656 4.344   12.398  1.00 6.19  ? 92  GLN   A O   1 
ATOM   740  C  CB  . GLN   A 1 92  ? -10.919 5.605   9.897   1.00 7.16  ? 92  GLN   A CB  1 
ATOM   741  C  CG  . GLN   A 1 92  ? -9.877  5.720   10.995  1.00 7.57  ? 92  GLN   A CG  1 
ATOM   742  C  CD  . GLN   A 1 92  ? -9.086  4.449   11.211  1.00 7.57  ? 92  GLN   A CD  1 
ATOM   743  O  OE1 . GLN   A 1 92  ? -9.587  3.333   11.212  1.00 7.67  ? 92  GLN   A OE1 1 
ATOM   744  N  NE2 . GLN   A 1 92  ? -7.824  4.607   11.526  1.00 10.96 ? 92  GLN   A NE2 1 
ATOM   745  N  N   . PHE   A 1 93  ? -12.771 3.227   10.427  1.00 5.92  ? 93  PHE   A N   1 
ATOM   746  C  CA  . PHE   A 1 93  ? -12.645 1.928   11.053  1.00 5.64  ? 93  PHE   A CA  1 
ATOM   747  C  C   . PHE   A 1 93  ? -11.712 1.061   10.225  1.00 5.57  ? 93  PHE   A C   1 
ATOM   748  O  O   . PHE   A 1 93  ? -11.497 1.274   9.032   1.00 6.44  ? 93  PHE   A O   1 
ATOM   749  C  CB  . PHE   A 1 93  ? -13.989 1.211   11.282  1.00 6.16  ? 93  PHE   A CB  1 
ATOM   750  C  CG  . PHE   A 1 93  ? -14.758 0.737   10.066  1.00 6.43  ? 93  PHE   A CG  1 
ATOM   751  C  CD1 . PHE   A 1 93  ? -14.397 -0.419  9.393   1.00 6.88  ? 93  PHE   A CD1 1 
ATOM   752  C  CD2 . PHE   A 1 93  ? -15.908 1.419   9.647   1.00 7.01  ? 93  PHE   A CD2 1 
ATOM   753  C  CE1 . PHE   A 1 93  ? -15.125 -0.849  8.292   1.00 7.20  ? 93  PHE   A CE1 1 
ATOM   754  C  CE2 . PHE   A 1 93  ? -16.634 0.955   8.546   1.00 7.41  ? 93  PHE   A CE2 1 
ATOM   755  C  CZ  . PHE   A 1 93  ? -16.252 -0.185  7.896   1.00 7.67  ? 93  PHE   A CZ  1 
ATOM   756  N  N   . HIS   A 1 94  ? -11.173 0.036   10.904  1.00 5.28  ? 94  HIS   A N   1 
ATOM   757  C  CA  . HIS   A 1 94  ? -10.308 -0.949  10.292  1.00 5.44  ? 94  HIS   A CA  1 
ATOM   758  C  C   . HIS   A 1 94  ? -10.386 -2.217  11.125  1.00 4.96  ? 94  HIS   A C   1 
ATOM   759  O  O   . HIS   A 1 94  ? -10.996 -2.240  12.195  1.00 5.40  ? 94  HIS   A O   1 
ATOM   760  C  CB  . HIS   A 1 94  ? -8.871  -0.441  10.206  1.00 5.88  ? 94  HIS   A CB  1 
ATOM   761  C  CG  . HIS   A 1 94  ? -8.303  -0.162  11.571  1.00 5.47  ? 94  HIS   A CG  1 
ATOM   762  N  ND1 . HIS   A 1 94  ? -8.445  1.057   12.203  1.00 5.69  ? 94  HIS   A ND1 1 
ATOM   763  C  CD2 . HIS   A 1 94  ? -7.662  -0.981  12.460  1.00 5.29  ? 94  HIS   A CD2 1 
ATOM   764  C  CE1 . HIS   A 1 94  ? -7.906  0.939   13.434  1.00 5.31  ? 94  HIS   A CE1 1 
ATOM   765  N  NE2 . HIS   A 1 94  ? -7.424  -0.280  13.616  1.00 5.47  ? 94  HIS   A NE2 1 
ATOM   766  N  N   . PHE   A 1 95  ? -9.708  -3.265  10.656  1.00 4.91  ? 95  PHE   A N   1 
ATOM   767  C  CA  . PHE   A 1 95  ? -9.654  -4.559  11.319  1.00 4.94  ? 95  PHE   A CA  1 
ATOM   768  C  C   . PHE   A 1 95  ? -8.202  -4.979  11.523  1.00 4.87  ? 95  PHE   A C   1 
ATOM   769  O  O   . PHE   A 1 95  ? -7.287  -4.528  10.843  1.00 5.98  ? 95  PHE   A O   1 
ATOM   770  C  CB  . PHE   A 1 95  ? -10.369 -5.633  10.487  1.00 5.31  ? 95  PHE   A CB  1 
ATOM   771  C  CG  . PHE   A 1 95  ? -11.824 -5.353  10.157  1.00 5.29  ? 95  PHE   A CG  1 
ATOM   772  C  CD1 . PHE   A 1 95  ? -12.138 -4.513  9.089   1.00 6.04  ? 95  PHE   A CD1 1 
ATOM   773  C  CD2 . PHE   A 1 95  ? -12.863 -5.966  10.845  1.00 6.08  ? 95  PHE   A CD2 1 
ATOM   774  C  CE1 . PHE   A 1 95  ? -13.457 -4.304  8.739   1.00 6.89  ? 95  PHE   A CE1 1 
ATOM   775  C  CE2 . PHE   A 1 95  ? -14.161 -5.746  10.478  1.00 6.76  ? 95  PHE   A CE2 1 
ATOM   776  C  CZ  . PHE   A 1 95  ? -14.470 -4.919  9.438   1.00 6.99  ? 95  PHE   A CZ  1 
ATOM   777  N  N   . HIS   A 1 96  ? -8.065  -5.957  12.416  1.00 4.84  ? 96  HIS   A N   1 
ATOM   778  C  CA  . HIS   A 1 96  ? -6.871  -6.765  12.591  1.00 4.76  ? 96  HIS   A CA  1 
ATOM   779  C  C   . HIS   A 1 96  ? -7.322  -8.218  12.485  1.00 4.96  ? 96  HIS   A C   1 
ATOM   780  O  O   . HIS   A 1 96  ? -8.378  -8.559  13.000  1.00 5.19  ? 96  HIS   A O   1 
ATOM   781  C  CB  . HIS   A 1 96  ? -6.216  -6.530  13.950  1.00 5.10  ? 96  HIS   A CB  1 
ATOM   782  C  CG  . HIS   A 1 96  ? -5.915  -5.092  14.217  1.00 5.25  ? 96  HIS   A CG  1 
ATOM   783  N  ND1 . HIS   A 1 96  ? -4.677  -4.516  14.010  1.00 6.38  ? 96  HIS   A ND1 1 
ATOM   784  C  CD2 . HIS   A 1 96  ? -6.697  -4.048  14.629  1.00 5.23  ? 96  HIS   A CD2 1 
ATOM   785  C  CE1 . HIS   A 1 96  ? -4.751  -3.214  14.306  1.00 5.49  ? 96  HIS   A CE1 1 
ATOM   786  N  NE2 . HIS   A 1 96  ? -5.976  -2.896  14.697  1.00 4.92  ? 96  HIS   A NE2 1 
ATOM   787  N  N   . TRP   A 1 97  ? -6.525  -9.059  11.823  1.00 4.98  ? 97  TRP   A N   1 
ATOM   788  C  CA  . TRP   A 1 97  ? -6.954  -10.428 11.610  1.00 5.42  ? 97  TRP   A CA  1 
ATOM   789  C  C   . TRP   A 1 97  ? -5.748  -11.355 11.493  1.00 5.31  ? 97  TRP   A C   1 
ATOM   790  O  O   . TRP   A 1 97  ? -4.580  -10.943 11.384  1.00 5.99  ? 97  TRP   A O   1 
ATOM   791  C  CB  . TRP   A 1 97  ? -7.862  -10.533 10.382  1.00 5.69  ? 97  TRP   A CB  1 
ATOM   792  C  CG  . TRP   A 1 97  ? -7.209  -10.152 9.090   1.00 5.72  ? 97  TRP   A CG  1 
ATOM   793  C  CD1 . TRP   A 1 97  ? -6.547  -10.980 8.226   1.00 6.25  ? 97  TRP   A CD1 1 
ATOM   794  C  CD2 . TRP   A 1 97  ? -7.156  -8.847  8.507   1.00 5.67  ? 97  TRP   A CD2 1 
ATOM   795  N  NE1 . TRP   A 1 97  ? -6.097  -10.272 7.131   1.00 6.76  ? 97  TRP   A NE1 1 
ATOM   796  C  CE2 . TRP   A 1 97  ? -6.453  -8.965  7.297   1.00 5.64  ? 97  TRP   A CE2 1 
ATOM   797  C  CE3 . TRP   A 1 97  ? -7.604  -7.588  8.901   1.00 5.48  ? 97  TRP   A CE3 1 
ATOM   798  C  CZ2 . TRP   A 1 97  ? -6.246  -7.861  6.447   1.00 6.22  ? 97  TRP   A CZ2 1 
ATOM   799  C  CZ3 . TRP   A 1 97  ? -7.390  -6.494  8.084   1.00 5.72  ? 97  TRP   A CZ3 1 
ATOM   800  C  CH2 . TRP   A 1 97  ? -6.709  -6.640  6.878   1.00 6.01  ? 97  TRP   A CH2 1 
ATOM   801  N  N   . GLY   A 1 98  ? -6.047  -12.648 11.506  1.00 5.97  ? 98  GLY   A N   1 
ATOM   802  C  CA  . GLY   A 1 98  ? -5.042  -13.684 11.537  1.00 6.42  ? 98  GLY   A CA  1 
ATOM   803  C  C   . GLY   A 1 98  ? -4.858  -14.388 10.206  1.00 7.08  ? 98  GLY   A C   1 
ATOM   804  O  O   . GLY   A 1 98  ? -5.585  -14.209 9.239   1.00 7.33  ? 98  GLY   A O   1 
ATOM   805  N  N   . SER   A 1 99  ? -3.843  -15.275 10.207  1.00 7.31  ? 99  SER   A N   1 
ATOM   806  C  CA  . SER   A 1 99  ? -3.630  -16.213 9.103   1.00 8.66  ? 99  SER   A CA  1 
ATOM   807  C  C   . SER   A 1 99  ? -4.513  -17.446 9.226   1.00 8.60  ? 99  SER   A C   1 
ATOM   808  O  O   . SER   A 1 99  ? -4.659  -18.185 8.253   1.00 10.66 ? 99  SER   A O   1 
ATOM   809  C  CB  . SER   A 1 99  ? -2.186  -16.615 9.017   1.00 9.46  ? 99  SER   A CB  1 
ATOM   810  O  OG  . SER   A 1 99  ? -1.713  -17.100 10.254  1.00 10.24 ? 99  SER   A OG  1 
ATOM   811  N  N   . LEU   A 1 100 ? -5.056  -17.677 10.430  1.00 8.44  ? 100 LEU   A N   1 
ATOM   812  C  CA  . LEU   A 1 100 ? -5.831  -18.853 10.790  1.00 9.58  ? 100 LEU   A CA  1 
ATOM   813  C  C   . LEU   A 1 100 ? -6.969  -18.381 11.678  1.00 8.18  ? 100 LEU   A C   1 
ATOM   814  O  O   . LEU   A 1 100 ? -6.823  -17.363 12.339  1.00 8.43  ? 100 LEU   A O   1 
ATOM   815  C  CB  . LEU   A 1 100 ? -5.028  -19.846 11.622  1.00 12.40 ? 100 LEU   A CB  1 
ATOM   816  C  CG  . LEU   A 1 100 ? -3.680  -20.265 11.079  1.00 14.47 ? 100 LEU   A CG  1 
ATOM   817  C  CD1 . LEU   A 1 100 ? -2.786  -20.960 12.107  1.00 16.83 ? 100 LEU   A CD1 1 
ATOM   818  C  CD2 . LEU   A 1 100 ? -4.028  -21.185 9.944   1.00 17.02 ? 100 LEU   A CD2 1 
ATOM   819  N  N   . ASP   A 1 101 ? -8.069  -19.127 11.732  1.00 8.89  ? 101 ASP   A N   1 
ATOM   820  C  CA  . ASP   A 1 101 ? -9.223  -18.649 12.470  1.00 9.18  ? 101 ASP   A CA  1 
ATOM   821  C  C   . ASP   A 1 101 ? -8.950  -18.556 13.970  1.00 9.56  ? 101 ASP   A C   1 
ATOM   822  O  O   . ASP   A 1 101 ? -9.630  -17.818 14.668  1.00 11.14 ? 101 ASP   A O   1 
ATOM   823  C  CB  . ASP   A 1 101 ? -10.415 -19.576 12.233  1.00 9.96  ? 101 ASP   A CB  1 
ATOM   824  C  CG  . ASP   A 1 101 ? -10.940 -19.654 10.818  1.00 10.82 ? 101 ASP   A CG  1 
ATOM   825  O  OD1 . ASP   A 1 101 ? -10.588 -18.797 10.008  1.00 10.67 ? 101 ASP   A OD1 1 
ATOM   826  O  OD2 . ASP   A 1 101 ? -11.740 -20.551 10.561  1.00 14.81 ? 101 ASP   A OD2 1 
ATOM   827  N  N   . GLY   A 1 102 ? -7.957  -19.289 14.487  1.00 9.56  ? 102 GLY   A N   1 
ATOM   828  C  CA  . GLY   A 1 102 ? -7.620  -19.330 15.903  1.00 10.48 ? 102 GLY   A CA  1 
ATOM   829  C  C   . GLY   A 1 102 ? -6.835  -18.138 16.431  1.00 8.78  ? 102 GLY   A C   1 
ATOM   830  O  O   . GLY   A 1 102 ? -6.477  -18.128 17.612  1.00 9.98  ? 102 GLY   A O   1 
ATOM   831  N  N   . GLN   A 1 103 ? -6.565  -17.126 15.593  1.00 8.11  ? 103 GLN   A N   1 
ATOM   832  C  CA  . GLN   A 1 103 ? -5.838  -15.950 16.038  1.00 7.32  ? 103 GLN   A CA  1 
ATOM   833  C  C   . GLN   A 1 103 ? -6.228  -14.795 15.145  1.00 6.53  ? 103 GLN   A C   1 
ATOM   834  O  O   . GLN   A 1 103 ? -6.779  -14.971 14.059  1.00 7.19  ? 103 GLN   A O   1 
ATOM   835  C  CB  . GLN   A 1 103 ? -4.333  -16.188 16.009  1.00 8.21  ? 103 GLN   A CB  1 
ATOM   836  C  CG  . GLN   A 1 103 ? -3.784  -16.415 14.587  1.00 9.49  ? 103 GLN   A CG  1 
ATOM   837  C  CD  . GLN   A 1 103 ? -2.454  -17.093 14.529  1.00 11.99 ? 103 GLN   A CD  1 
ATOM   838  O  OE1 . GLN   A 1 103 ? -2.299  -18.168 15.107  1.00 17.07 ? 103 GLN   A OE1 1 
ATOM   839  N  NE2 . GLN   A 1 103 ? -1.495  -16.531 13.821  1.00 11.59 ? 103 GLN   A NE2 1 
ATOM   840  N  N   . GLY   A 1 104 ? -5.917  -13.583 15.613  1.00 5.90  ? 104 GLY   A N   1 
ATOM   841  C  CA  . GLY   A 1 104 ? -6.186  -12.403 14.840  1.00 5.73  ? 104 GLY   A CA  1 
ATOM   842  C  C   . GLY   A 1 104 ? -6.619  -11.220 15.669  1.00 5.55  ? 104 GLY   A C   1 
ATOM   843  O  O   . GLY   A 1 104 ? -6.346  -10.078 15.289  1.00 6.05  ? 104 GLY   A O   1 
ATOM   844  N  N   . SER   A 1 105 ? -7.313  -11.459 16.797  1.00 5.17  ? 105 SER   A N   1 
ATOM   845  C  CA  . SER   A 1 105 ? -7.706  -10.347 17.629  1.00 5.05  ? 105 SER   A CA  1 
ATOM   846  C  C   . SER   A 1 105 ? -6.489  -9.787  18.374  1.00 4.96  ? 105 SER   A C   1 
ATOM   847  O  O   . SER   A 1 105 ? -5.492  -10.460 18.588  1.00 5.95  ? 105 SER   A O   1 
ATOM   848  C  CB  . SER   A 1 105 ? -8.844  -10.678 18.556  1.00 5.30  ? 105 SER   A CB  1 
ATOM   849  O  OG  . SER   A 1 105 ? -8.488  -11.611 19.568  1.00 5.76  ? 105 SER   A OG  1 
ATOM   850  N  N   . GLU   A 1 106 ? -6.643  -8.543  18.800  1.00 4.88  ? 106 GLU   A N   1 
ATOM   851  C  CA  . GLU   A 1 106 ? -5.637  -7.838  19.592  1.00 5.08  ? 106 GLU   A CA  1 
ATOM   852  C  C   . GLU   A 1 106 ? -5.970  -8.002  21.079  1.00 4.79  ? 106 GLU   A C   1 
ATOM   853  O  O   . GLU   A 1 106 ? -5.184  -8.572  21.842  1.00 5.46  ? 106 GLU   A O   1 
ATOM   854  C  CB  . GLU   A 1 106 ? -5.559  -6.388  19.145  1.00 5.12  ? 106 GLU   A CB  1 
ATOM   855  C  CG  . GLU   A 1 106 ? -5.090  -6.271  17.710  1.00 6.13  ? 106 GLU   A CG  1 
ATOM   856  C  CD  . GLU   A 1 106 ? -4.427  -4.993  17.392  1.00 5.22  ? 106 GLU   A CD  1 
ATOM   857  O  OE1 . GLU   A 1 106 ? -5.039  -3.927  17.652  1.00 5.53  ? 106 GLU   A OE1 1 
ATOM   858  O  OE2 . GLU   A 1 106 ? -3.288  -5.040  16.894  1.00 6.32  ? 106 GLU   A OE2 1 
ATOM   859  N  N   . HIS   A 1 107 ? -7.138  -7.509  21.492  1.00 4.72  ? 107 HIS   A N   1 
ATOM   860  C  CA  . HIS   A 1 107 ? -7.610  -7.891  22.815  1.00 4.85  ? 107 HIS   A CA  1 
ATOM   861  C  C   . HIS   A 1 107 ? -7.913  -9.385  22.835  1.00 4.87  ? 107 HIS   A C   1 
ATOM   862  O  O   . HIS   A 1 107 ? -8.257  -9.992  21.817  1.00 5.16  ? 107 HIS   A O   1 
ATOM   863  C  CB  . HIS   A 1 107 ? -8.857  -7.074  23.197  1.00 4.90  ? 107 HIS   A CB  1 
ATOM   864  C  CG  . HIS   A 1 107 ? -8.528  -5.629  23.333  1.00 4.73  ? 107 HIS   A CG  1 
ATOM   865  N  ND1 . HIS   A 1 107 ? -8.568  -4.746  22.285  1.00 4.78  ? 107 HIS   A ND1 1 
ATOM   866  C  CD2 . HIS   A 1 107 ? -8.070  -4.924  24.403  1.00 4.62  ? 107 HIS   A CD2 1 
ATOM   867  C  CE1 . HIS   A 1 107 ? -8.117  -3.560  22.738  1.00 4.87  ? 107 HIS   A CE1 1 
ATOM   868  N  NE2 . HIS   A 1 107 ? -7.800  -3.613  24.005  1.00 4.91  ? 107 HIS   A NE2 1 
ATOM   869  N  N   . THR   A 1 108 ? -7.777  -9.959  24.029  1.00 5.58  ? 108 THR   A N   1 
ATOM   870  C  CA  . THR   A 1 108 ? -8.157  -11.322 24.315  1.00 5.76  ? 108 THR   A CA  1 
ATOM   871  C  C   . THR   A 1 108 ? -9.098  -11.305 25.515  1.00 5.48  ? 108 THR   A C   1 
ATOM   872  O  O   . THR   A 1 108 ? -9.106  -10.339 26.282  1.00 5.90  ? 108 THR   A O   1 
ATOM   873  C  CB  . THR   A 1 108 ? -6.941  -12.226 24.524  1.00 6.47  ? 108 THR   A CB  1 
ATOM   874  O  OG1 . THR   A 1 108 ? -6.110  -11.718 25.552  1.00 6.94  ? 108 THR   A OG1 1 
ATOM   875  C  CG2 . THR   A 1 108 ? -6.128  -12.301 23.255  1.00 7.05  ? 108 THR   A CG2 1 
ATOM   876  N  N   . VAL   A 1 109 ? -9.878  -12.369 25.650  1.00 5.92  ? 109 VAL   A N   1 
ATOM   877  C  CA  . VAL   A 1 109 ? -10.863 -12.462 26.704  1.00 6.13  ? 109 VAL   A CA  1 
ATOM   878  C  C   . VAL   A 1 109 ? -10.575 -13.747 27.455  1.00 6.74  ? 109 VAL   A C   1 
ATOM   879  O  O   . VAL   A 1 109 ? -10.723 -14.838 26.892  1.00 7.48  ? 109 VAL   A O   1 
ATOM   880  C  CB  . VAL   A 1 109 ? -12.306 -12.452 26.176  1.00 6.88  ? 109 VAL   A CB  1 
ATOM   881  C  CG1 . VAL   A 1 109 ? -13.315 -12.600 27.332  1.00 7.83  ? 109 VAL   A CG1 1 
ATOM   882  C  CG2 . VAL   A 1 109 ? -12.576 -11.185 25.383  1.00 7.77  ? 109 VAL   A CG2 1 
ATOM   883  N  N   . ASP   A 1 110 ? -10.039 -13.637 28.671  1.00 7.13  ? 110 ASP   A N   1 
ATOM   884  C  CA  . ASP   A 1 110 ? -9.581  -14.826 29.380  1.00 8.21  ? 110 ASP   A CA  1 
ATOM   885  C  C   . ASP   A 1 110 ? -8.622  -15.655 28.515  1.00 9.04  ? 110 ASP   A C   1 
ATOM   886  O  O   . ASP   A 1 110 ? -8.683  -16.886 28.462  1.00 10.50 ? 110 ASP   A O   1 
ATOM   887  C  CB  . ASP   A 1 110 ? -10.735 -15.686 29.900  1.00 9.92  ? 110 ASP   A CB  1 
ATOM   888  C  CG  . ASP   A 1 110 ? -11.588 -14.966 30.927  1.00 9.84  ? 110 ASP   A CG  1 
ATOM   889  O  OD1 . ASP   A 1 110 ? -11.060 -14.062 31.612  1.00 10.15 ? 110 ASP   A OD1 1 
ATOM   890  O  OD2 . ASP   A 1 110 ? -12.797 -15.267 31.022  1.00 11.59 ? 110 ASP   A OD2 1 
ATOM   891  N  N   . LYS   A 1 111 ? -7.732  -14.899 27.843  1.00 7.98  ? 111 LYS   A N   1 
ATOM   892  C  CA  . LYS   A 1 111 ? -6.674  -15.402 26.962  1.00 8.77  ? 111 LYS   A CA  1 
ATOM   893  C  C   . LYS   A 1 111 ? -7.206  -15.910 25.621  1.00 8.53  ? 111 LYS   A C   1 
ATOM   894  O  O   . LYS   A 1 111 ? -6.406  -16.290 24.758  1.00 9.83  ? 111 LYS   A O   1 
ATOM   895  C  CB  . LYS   A 1 111 ? -5.787  -16.435 27.646  1.00 11.28 ? 111 LYS   A CB  1 
ATOM   896  C  CG  . LYS   A 1 111 ? -5.079  -15.890 28.881  1.00 13.74 ? 111 LYS   A CG  1 
ATOM   897  C  CD  . LYS   A 1 111 ? -4.142  -14.711 28.594  1.00 16.93 ? 111 LYS   A CD  1 
ATOM   898  C  CE  . LYS   A 1 111 ? -3.333  -14.107 29.747  1.00 19.87 ? 111 LYS   A CE  1 
ATOM   899  N  NZ  . LYS   A 1 111 ? -2.214  -14.927 30.163  1.00 22.56 ? 111 LYS   A NZ  1 
ATOM   900  N  N   . LYS   A 1 112 ? -8.530  -15.950 25.417  1.00 8.09  ? 112 LYS   A N   1 
ATOM   901  C  CA  . LYS   A 1 112 ? -9.081  -16.361 24.127  1.00 8.68  ? 112 LYS   A CA  1 
ATOM   902  C  C   . LYS   A 1 112 ? -8.802  -15.316 23.057  1.00 7.82  ? 112 LYS   A C   1 
ATOM   903  O  O   . LYS   A 1 112 ? -9.109  -14.143 23.235  1.00 7.52  ? 112 LYS   A O   1 
ATOM   904  C  CB  . LYS   A 1 112 ? -10.609 -16.562 24.227  1.00 10.20 ? 112 LYS   A CB  1 
ATOM   905  C  CG  . LYS   A 1 112 ? -11.304 -16.921 22.896  1.00 11.59 ? 112 LYS   A CG  1 
ATOM   906  C  CD  . LYS   A 1 112 ? -12.833 -16.837 22.921  1.00 13.52 ? 112 LYS   A CD  1 
ATOM   907  C  CE  . LYS   A 1 112 ? -13.429 -17.063 21.597  1.00 14.33 ? 112 LYS   A CE  1 
ATOM   908  N  NZ  . LYS   A 1 112 ? -13.230 -18.413 21.190  1.00 13.33 ? 112 LYS   A NZ  1 
ATOM   909  N  N   . LYS   A 1 113 ? -8.259  -15.793 21.933  1.00 8.02  ? 113 LYS   A N   1 
ATOM   910  C  CA  . LYS   A 1 113 ? -8.066  -14.994 20.735  1.00 7.70  ? 113 LYS   A CA  1 
ATOM   911  C  C   . LYS   A 1 113 ? -9.210  -15.262 19.774  1.00 7.35  ? 113 LYS   A C   1 
ATOM   912  O  O   . LYS   A 1 113 ? -9.557  -16.419 19.496  1.00 9.78  ? 113 LYS   A O   1 
ATOM   913  C  CB  . LYS   A 1 113 ? -6.768  -15.410 20.027  1.00 8.50  ? 113 LYS   A CB  1 
ATOM   914  C  CG  . LYS   A 1 113 ? -5.507  -15.069 20.811  1.00 8.39  ? 113 LYS   A CG  1 
ATOM   915  C  CD  . LYS   A 1 113 ? -4.253  -15.657 20.213  1.00 9.81  ? 113 LYS   A CD  1 
ATOM   916  C  CE  . LYS   A 1 113 ? -2.997  -15.059 20.750  1.00 12.64 ? 113 LYS   A CE  1 
ATOM   917  N  NZ  . LYS   A 1 113 ? -2.577  -15.851 21.887  1.00 15.59 ? 113 LYS   A NZ  1 
ATOM   918  N  N   . TYR   A 1 114 ? -9.814  -14.192 19.254  1.00 6.38  ? 114 TYR   A N   1 
ATOM   919  C  CA  . TYR   A 1 114 ? -10.806 -14.272 18.197  1.00 6.24  ? 114 TYR   A CA  1 
ATOM   920  C  C   . TYR   A 1 114 ? -10.133 -14.228 16.833  1.00 6.04  ? 114 TYR   A C   1 
ATOM   921  O  O   . TYR   A 1 114 ? -8.939  -13.938 16.707  1.00 6.52  ? 114 TYR   A O   1 
ATOM   922  C  CB  . TYR   A 1 114 ? -11.852 -13.152 18.355  1.00 6.36  ? 114 TYR   A CB  1 
ATOM   923  C  CG  . TYR   A 1 114 ? -12.785 -13.354 19.515  1.00 6.41  ? 114 TYR   A CG  1 
ATOM   924  C  CD1 . TYR   A 1 114 ? -12.496 -12.915 20.797  1.00 7.45  ? 114 TYR   A CD1 1 
ATOM   925  C  CD2 . TYR   A 1 114 ? -13.974 -14.006 19.317  1.00 7.53  ? 114 TYR   A CD2 1 
ATOM   926  C  CE1 . TYR   A 1 114 ? -13.411 -13.124 21.822  1.00 9.13  ? 114 TYR   A CE1 1 
ATOM   927  C  CE2 . TYR   A 1 114 ? -14.904 -14.205 20.329  1.00 9.62  ? 114 TYR   A CE2 1 
ATOM   928  C  CZ  . TYR   A 1 114 ? -14.614 -13.755 21.584  1.00 9.76  ? 114 TYR   A CZ  1 
ATOM   929  O  OH  . TYR   A 1 114 ? -15.513 -13.919 22.627  1.00 13.53 ? 114 TYR   A OH  1 
ATOM   930  N  N   . ALA   A 1 115 ? -10.907 -14.491 15.777  1.00 6.04  ? 115 ALA   A N   1 
ATOM   931  C  CA  . ALA   A 1 115 ? -10.377 -14.519 14.426  1.00 6.44  ? 115 ALA   A CA  1 
ATOM   932  C  C   . ALA   A 1 115 ? -9.990  -13.140 13.924  1.00 5.94  ? 115 ALA   A C   1 
ATOM   933  O  O   . ALA   A 1 115 ? -9.133  -13.003 13.044  1.00 6.73  ? 115 ALA   A O   1 
ATOM   934  C  CB  . ALA   A 1 115 ? -11.416 -15.123 13.490  1.00 7.00  ? 115 ALA   A CB  1 
ATOM   935  N  N   . ALA   A 1 116 ? -10.610 -12.097 14.425  1.00 5.58  ? 116 ALA   A N   1 
ATOM   936  C  CA  . ALA   A 1 116 ? -10.330 -10.757 13.982  1.00 5.06  ? 116 ALA   A CA  1 
ATOM   937  C  C   . ALA   A 1 116 ? -10.917 -9.792  15.006  1.00 4.71  ? 116 ALA   A C   1 
ATOM   938  O  O   . ALA   A 1 116 ? -11.658 -10.178 15.913  1.00 5.18  ? 116 ALA   A O   1 
ATOM   939  C  CB  . ALA   A 1 116 ? -10.845 -10.481 12.583  1.00 5.56  ? 116 ALA   A CB  1 
ATOM   940  N  N   . GLU   A 1 117 ? -10.607 -8.516  14.825  1.00 4.61  ? 117 GLU   A N   1 
ATOM   941  C  CA  . GLU   A 1 117 ? -11.092 -7.449  15.708  1.00 4.68  ? 117 GLU   A CA  1 
ATOM   942  C  C   . GLU   A 1 117 ? -11.279 -6.185  14.878  1.00 4.85  ? 117 GLU   A C   1 
ATOM   943  O  O   . GLU   A 1 117 ? -10.375 -5.793  14.141  1.00 5.65  ? 117 GLU   A O   1 
ATOM   944  C  CB  . GLU   A 1 117 ? -10.144 -7.260  16.885  1.00 4.65  ? 117 GLU   A CB  1 
ATOM   945  C  CG  . GLU   A 1 117 ? -10.607 -6.265  17.944  1.00 4.76  ? 117 GLU   A CG  1 
ATOM   946  C  CD  . GLU   A 1 117 ? -9.708  -6.213  19.156  1.00 4.69  ? 117 GLU   A CD  1 
ATOM   947  O  OE1 . GLU   A 1 117 ? -9.071  -7.241  19.472  1.00 5.45  ? 117 GLU   A OE1 1 
ATOM   948  O  OE2 . GLU   A 1 117 ? -9.608  -5.112  19.769  1.00 5.79  ? 117 GLU   A OE2 1 
ATOM   949  N  N   . LEU   A 1 118 ? -12.464 -5.605  14.994  1.00 4.42  ? 118 LEU   A N   1 
ATOM   950  C  CA  . LEU   A 1 118 ? -12.846 -4.354  14.356  1.00 4.36  ? 118 LEU   A CA  1 
ATOM   951  C  C   . LEU   A 1 118 ? -12.608 -3.212  15.336  1.00 4.18  ? 118 LEU   A C   1 
ATOM   952  O  O   . LEU   A 1 118 ? -13.018 -3.272  16.494  1.00 4.39  ? 118 LEU   A O   1 
ATOM   953  C  CB  . LEU   A 1 118 ? -14.347 -4.447  14.005  1.00 5.00  ? 118 LEU   A CB  1 
ATOM   954  C  CG  . LEU   A 1 118 ? -15.055 -3.145  13.615  1.00 5.47  ? 118 LEU   A CG  1 
ATOM   955  C  CD1 . LEU   A 1 118 ? -14.478 -2.514  12.387  1.00 5.83  ? 118 LEU   A CD1 1 
ATOM   956  C  CD2 . LEU   A 1 118 ? -16.530 -3.493  13.388  1.00 6.85  ? 118 LEU   A CD2 1 
ATOM   957  N  N   . HIS   A 1 119 ? -11.990 -2.137  14.857  1.00 4.11  ? 119 HIS   A N   1 
ATOM   958  C  CA  . HIS   A 1 119 ? -11.747 -0.920  15.609  1.00 4.34  ? 119 HIS   A CA  1 
ATOM   959  C  C   . HIS   A 1 119 ? -12.424 0.266   14.904  1.00 4.56  ? 119 HIS   A C   1 
ATOM   960  O  O   . HIS   A 1 119 ? -12.039 0.617   13.782  1.00 5.37  ? 119 HIS   A O   1 
ATOM   961  C  CB  . HIS   A 1 119 ? -10.243 -0.634  15.691  1.00 4.36  ? 119 HIS   A CB  1 
ATOM   962  C  CG  . HIS   A 1 119 ? -9.536  -1.608  16.555  1.00 4.33  ? 119 HIS   A CG  1 
ATOM   963  N  ND1 . HIS   A 1 119 ? -8.165  -1.821  16.536  1.00 4.34  ? 119 HIS   A ND1 1 
ATOM   964  C  CD2 . HIS   A 1 119 ? -10.055 -2.458  17.494  1.00 4.55  ? 119 HIS   A CD2 1 
ATOM   965  C  CE1 . HIS   A 1 119 ? -7.914  -2.759  17.439  1.00 4.56  ? 119 HIS   A CE1 1 
ATOM   966  N  NE2 . HIS   A 1 119 ? -9.021  -3.145  18.040  1.00 4.75  ? 119 HIS   A NE2 1 
ATOM   967  N  N   . LEU   A 1 120 ? -13.426 0.836   15.581  1.00 4.62  ? 120 LEU   A N   1 
ATOM   968  C  CA  . LEU   A 1 120 ? -14.080 2.063   15.132  1.00 4.91  ? 120 LEU   A CA  1 
ATOM   969  C  C   . LEU   A 1 120 ? -13.450 3.198   15.934  1.00 4.88  ? 120 LEU   A C   1 
ATOM   970  O  O   . LEU   A 1 120 ? -13.576 3.244   17.162  1.00 5.01  ? 120 LEU   A O   1 
ATOM   971  C  CB  . LEU   A 1 120 ? -15.583 1.991   15.340  1.00 5.56  ? 120 LEU   A CB  1 
ATOM   972  C  CG  . LEU   A 1 120 ? -16.271 0.929   14.470  1.00 6.33  ? 120 LEU   A CG  1 
ATOM   973  C  CD1 . LEU   A 1 120 ? -17.101 -0.013  15.318  1.00 8.65  ? 120 LEU   A CD1 1 
ATOM   974  C  CD2 . LEU   A 1 120 ? -17.116 1.552   13.409  1.00 7.70  ? 120 LEU   A CD2 1 
ATOM   975  N  N   . VAL   A 1 121 ? -12.732 4.086   15.238  1.00 5.11  ? 121 VAL   A N   1 
ATOM   976  C  CA  . VAL   A 1 121 ? -11.878 5.105   15.838  1.00 5.09  ? 121 VAL   A CA  1 
ATOM   977  C  C   . VAL   A 1 121 ? -12.599 6.447   15.856  1.00 5.05  ? 121 VAL   A C   1 
ATOM   978  O  O   . VAL   A 1 121 ? -13.070 6.895   14.819  1.00 5.97  ? 121 VAL   A O   1 
ATOM   979  C  CB  . VAL   A 1 121 ? -10.555 5.203   15.081  1.00 5.87  ? 121 VAL   A CB  1 
ATOM   980  C  CG1 . VAL   A 1 121 ? -9.644  6.238   15.711  1.00 6.62  ? 121 VAL   A CG1 1 
ATOM   981  C  CG2 . VAL   A 1 121 ? -9.892  3.846   14.959  1.00 6.82  ? 121 VAL   A CG2 1 
ATOM   982  N  N   . HIS   A 1 122 ? -12.621 7.080   17.027  1.00 5.23  ? 122 HIS   A N   1 
ATOM   983  C  CA  . HIS   A 1 122 ? -13.315 8.337   17.225  1.00 5.32  ? 122 HIS   A CA  1 
ATOM   984  C  C   . HIS   A 1 122 ? -12.413 9.307   17.958  1.00 5.40  ? 122 HIS   A C   1 
ATOM   985  O  O   . HIS   A 1 122 ? -11.649 8.911   18.827  1.00 6.09  ? 122 HIS   A O   1 
ATOM   986  C  CB  . HIS   A 1 122 ? -14.587 8.173   18.065  1.00 5.37  ? 122 HIS   A CB  1 
ATOM   987  C  CG  . HIS   A 1 122 ? -15.489 7.038   17.668  1.00 5.45  ? 122 HIS   A CG  1 
ATOM   988  N  ND1 . HIS   A 1 122 ? -15.161 5.733   17.927  1.00 5.78  ? 122 HIS   A ND1 1 
ATOM   989  C  CD2 . HIS   A 1 122 ? -16.703 6.997   17.100  1.00 5.86  ? 122 HIS   A CD2 1 
ATOM   990  C  CE1 . HIS   A 1 122 ? -16.172 4.958   17.480  1.00 6.03  ? 122 HIS   A CE1 1 
ATOM   991  N  NE2 . HIS   A 1 122 ? -17.143 5.711   16.986  1.00 6.50  ? 122 HIS   A NE2 1 
ATOM   992  N  N   . TRP   A 1 123 ? -12.558 10.608  17.662  1.00 5.73  ? 123 TRP   A N   1 
ATOM   993  C  CA  . TRP   A 1 123 ? -11.778 11.632  18.343  1.00 6.09  ? 123 TRP   A CA  1 
ATOM   994  C  C   . TRP   A 1 123 ? -12.676 12.614  19.089  1.00 6.08  ? 123 TRP   A C   1 
ATOM   995  O  O   . TRP   A 1 123 ? -13.800 12.915  18.699  1.00 6.62  ? 123 TRP   A O   1 
ATOM   996  C  CB  . TRP   A 1 123 ? -10.817 12.395  17.385  1.00 7.30  ? 123 TRP   A CB  1 
ATOM   997  C  CG  . TRP   A 1 123 ? -11.481 13.018  16.186  1.00 7.39  ? 123 TRP   A CG  1 
ATOM   998  C  CD1 . TRP   A 1 123 ? -11.739 12.430  14.996  1.00 7.81  ? 123 TRP   A CD1 1 
ATOM   999  C  CD2 . TRP   A 1 123 ? -11.969 14.371  16.069  1.00 8.27  ? 123 TRP   A CD2 1 
ATOM   1000 N  NE1 . TRP   A 1 123 ? -12.342 13.294  14.141  1.00 8.51  ? 123 TRP   A NE1 1 
ATOM   1001 C  CE2 . TRP   A 1 123 ? -12.499 14.498  14.766  1.00 8.55  ? 123 TRP   A CE2 1 
ATOM   1002 C  CE3 . TRP   A 1 123 ? -11.997 15.474  16.924  1.00 9.53  ? 123 TRP   A CE3 1 
ATOM   1003 C  CZ2 . TRP   A 1 123 ? -13.063 15.679  14.301  1.00 10.07 ? 123 TRP   A CZ2 1 
ATOM   1004 C  CZ3 . TRP   A 1 123 ? -12.557 16.653  16.466  1.00 10.81 ? 123 TRP   A CZ3 1 
ATOM   1005 C  CH2 . TRP   A 1 123 ? -13.075 16.743  15.173  1.00 10.97 ? 123 TRP   A CH2 1 
ATOM   1006 N  N   . ASN   A 1 124 ? -12.134 13.092  20.223  1.00 6.11  ? 124 ASN   A N   1 
ATOM   1007 C  CA  . ASN   A 1 124 ? -12.865 13.962  21.137  1.00 6.31  ? 124 ASN   A CA  1 
ATOM   1008 C  C   . ASN   A 1 124 ? -13.008 15.344  20.535  1.00 7.24  ? 124 ASN   A C   1 
ATOM   1009 O  O   . ASN   A 1 124 ? -12.006 16.028  20.309  1.00 7.47  ? 124 ASN   A O   1 
ATOM   1010 C  CB  . ASN   A 1 124 ? -12.109 14.003  22.430  1.00 6.42  ? 124 ASN   A CB  1 
ATOM   1011 C  CG  . ASN   A 1 124 ? -12.868 14.642  23.554  1.00 7.04  ? 124 ASN   A CG  1 
ATOM   1012 O  OD1 . ASN   A 1 124 ? -13.689 15.536  23.324  1.00 8.15  ? 124 ASN   A OD1 1 
ATOM   1013 N  ND2 . ASN   A 1 124 ? -12.543 14.239  24.770  1.00 7.66  ? 124 ASN   A ND2 1 
ATOM   1014 N  N   . THR   A 1 125 ? -14.256 15.773  20.298  1.00 7.54  ? 125 THR   A N   1 
ATOM   1015 C  CA  . THR   A 1 125 ? -14.489 17.015  19.571  1.00 8.68  ? 125 THR   A CA  1 
ATOM   1016 C  C   . THR   A 1 125 ? -13.987 18.232  20.324  1.00 9.02  ? 125 THR   A C   1 
ATOM   1017 O  O   . THR   A 1 125 ? -13.789 19.278  19.703  1.00 10.44 ? 125 THR   A O   1 
ATOM   1018 C  CB  . THR   A 1 125 ? -15.971 17.147  19.158  1.00 10.76 ? 125 THR   A CB  1 
ATOM   1019 O  OG1 . THR   A 1 125 ? -16.770 17.189  20.326  1.00 12.93 ? 125 THR   A OG1 1 
ATOM   1020 C  CG2 . THR   A 1 125 ? -16.408 16.015  18.239  1.00 11.78 ? 125 THR   A CG2 1 
ATOM   1021 N  N   . LYS   A 1 126 ? -13.750 18.123  21.628  1.00 9.36  ? 127 LYS   A N   1 
ATOM   1022 C  CA  . LYS   A 1 126 ? -13.261 19.292  22.357  1.00 9.95  ? 127 LYS   A CA  1 
ATOM   1023 C  C   . LYS   A 1 126 ? -11.866 19.704  21.879  1.00 9.14  ? 127 LYS   A C   1 
ATOM   1024 O  O   . LYS   A 1 126 ? -11.426 20.816  22.157  1.00 11.66 ? 127 LYS   A O   1 
ATOM   1025 C  CB  . LYS   A 1 126 ? -13.273 19.051  23.869  1.00 11.86 ? 127 LYS   A CB  1 
ATOM   1026 C  CG  . LYS   A 1 126 ? -12.201 18.171  24.424  1.00 12.95 ? 127 LYS   A CG  1 
ATOM   1027 C  CD  . LYS   A 1 126 ? -12.465 17.800  25.885  1.00 15.92 ? 127 LYS   A CD  1 
ATOM   1028 C  CE  . LYS   A 1 126 ? -12.141 18.888  26.805  1.00 17.64 ? 127 LYS   A CE  1 
ATOM   1029 N  NZ  . LYS   A 1 126 ? -12.376 18.425  28.174  1.00 19.92 ? 127 LYS   A NZ  1 
ATOM   1030 N  N   . TYR   A 1 127 ? -11.163 18.813  21.157  1.00 8.23  ? 128 TYR   A N   1 
ATOM   1031 C  CA  . TYR   A 1 127 ? -9.798  19.103  20.701  1.00 8.44  ? 128 TYR   A CA  1 
ATOM   1032 C  C   . TYR   A 1 127 ? -9.739  19.532  19.239  1.00 8.78  ? 128 TYR   A C   1 
ATOM   1033 O  O   . TYR   A 1 127 ? -8.644  19.776  18.720  1.00 9.63  ? 128 TYR   A O   1 
ATOM   1034 C  CB  . TYR   A 1 127 ? -8.844  17.946  20.959  1.00 8.65  ? 128 TYR   A CB  1 
ATOM   1035 C  CG  . TYR   A 1 127 ? -8.772  17.619  22.424  1.00 8.43  ? 128 TYR   A CG  1 
ATOM   1036 C  CD1 . TYR   A 1 127 ? -8.465  18.592  23.360  1.00 9.19  ? 128 TYR   A CD1 1 
ATOM   1037 C  CD2 . TYR   A 1 127 ? -9.139  16.362  22.890  1.00 7.96  ? 128 TYR   A CD2 1 
ATOM   1038 C  CE1 . TYR   A 1 127 ? -8.463  18.293  24.708  1.00 9.32  ? 128 TYR   A CE1 1 
ATOM   1039 C  CE2 . TYR   A 1 127 ? -9.134  16.048  24.227  1.00 8.39  ? 128 TYR   A CE2 1 
ATOM   1040 C  CZ  . TYR   A 1 127 ? -8.798  17.019  25.149  1.00 8.92  ? 128 TYR   A CZ  1 
ATOM   1041 O  OH  . TYR   A 1 127 ? -8.779  16.770  26.507  1.00 9.39  ? 128 TYR   A OH  1 
ATOM   1042 N  N   . GLY   A 1 128 ? -10.882 19.603  18.551  1.00 8.73  ? 129 GLY   A N   1 
ATOM   1043 C  CA  . GLY   A 1 128 ? -10.964 20.283  17.260  1.00 9.82  ? 129 GLY   A CA  1 
ATOM   1044 C  C   . GLY   A 1 128 ? -10.612 19.444  16.036  1.00 9.37  ? 129 GLY   A C   1 
ATOM   1045 O  O   . GLY   A 1 128 ? -11.249 19.567  14.997  1.00 10.72 ? 129 GLY   A O   1 
ATOM   1046 N  N   . ASP   A 1 129 ? -9.542  18.625  16.126  1.00 10.17 ? 130 ASP   A N   1 
ATOM   1047 C  CA  . ASP   A 1 129 ? -9.103  17.755  15.037  1.00 11.37 ? 130 ASP   A CA  1 
ATOM   1048 C  C   . ASP   A 1 129 ? -8.451  16.515  15.617  1.00 10.36 ? 130 ASP   A C   1 
ATOM   1049 O  O   . ASP   A 1 129 ? -8.055  16.489  16.782  1.00 9.79  ? 130 ASP   A O   1 
ATOM   1050 C  CB  . ASP   A 1 129 ? -8.181  18.477  14.000  1.00 12.43 ? 130 ASP   A CB  1 
ATOM   1051 C  CG  . ASP   A 1 129 ? -6.804  18.933  14.501  1.00 14.83 ? 130 ASP   A CG  1 
ATOM   1052 O  OD1 . ASP   A 1 129 ? -5.957  18.165  14.859  1.00 19.37 ? 130 ASP   A OD1 1 
ATOM   1053 O  OD2 . ASP   A 1 129 ? -6.443  20.115  14.338  1.00 20.64 ? 130 ASP   A OD2 1 
ATOM   1054 N  N   . PHE   A 1 130 ? -8.261  15.498  14.788  1.00 9.61  ? 131 PHE   A N   1 
ATOM   1055 C  CA  . PHE   A 1 130 ? -7.669  14.254  15.221  1.00 8.91  ? 131 PHE   A CA  1 
ATOM   1056 C  C   . PHE   A 1 130 ? -6.224  14.487  15.666  1.00 8.75  ? 131 PHE   A C   1 
ATOM   1057 O  O   . PHE   A 1 130 ? -5.766  13.915  16.645  1.00 8.16  ? 131 PHE   A O   1 
ATOM   1058 C  CB  . PHE   A 1 130 ? -7.749  13.253  14.064  1.00 8.84  ? 131 PHE   A CB  1 
ATOM   1059 C  CG  . PHE   A 1 130 ? -7.109  11.929  14.374  1.00 8.59  ? 131 PHE   A CG  1 
ATOM   1060 C  CD1 . PHE   A 1 130 ? -5.765  11.685  14.163  1.00 10.80 ? 131 PHE   A CD1 1 
ATOM   1061 C  CD2 . PHE   A 1 130 ? -7.859  10.900  14.874  1.00 8.66  ? 131 PHE   A CD2 1 
ATOM   1062 C  CE1 . PHE   A 1 130 ? -5.205  10.468  14.485  1.00 12.22 ? 131 PHE   A CE1 1 
ATOM   1063 C  CE2 . PHE   A 1 130 ? -7.292  9.671   15.175  1.00 10.06 ? 131 PHE   A CE2 1 
ATOM   1064 C  CZ  . PHE   A 1 130 ? -5.979  9.463   14.954  1.00 10.91 ? 131 PHE   A CZ  1 
ATOM   1065 N  N   . GLY   A 1 131 ? -5.467  15.305  14.911  1.00 10.27 ? 132 GLY   A N   1 
ATOM   1066 C  CA  . GLY   A 1 131 ? -4.072  15.542  15.238  1.00 10.70 ? 132 GLY   A CA  1 
ATOM   1067 C  C   . GLY   A 1 131 ? -3.851  16.156  16.624  1.00 10.27 ? 132 GLY   A C   1 
ATOM   1068 O  O   . GLY   A 1 131 ? -2.911  15.806  17.325  1.00 11.58 ? 132 GLY   A O   1 
ATOM   1069 N  N   . LYS   A 1 132 ? -4.714  17.090  16.998  1.00 9.49  ? 133 LYS   A N   1 
ATOM   1070 C  CA  . LYS   A 1 132 ? -4.640  17.637  18.343  1.00 9.21  ? 133 LYS   A CA  1 
ATOM   1071 C  C   . LYS   A 1 132 ? -5.146  16.649  19.390  1.00 8.23  ? 133 LYS   A C   1 
ATOM   1072 O  O   . LYS   A 1 132 ? -4.621  16.598  20.507  1.00 8.38  ? 133 LYS   A O   1 
ATOM   1073 C  CB  . LYS   A 1 132 ? -5.433  18.940  18.420  1.00 10.04 ? 133 LYS   A CB  1 
ATOM   1074 C  CG  . LYS   A 1 132 ? -4.714  20.050  17.729  1.00 14.11 ? 133 LYS   A CG  1 
ATOM   1075 C  CD  . LYS   A 1 132 ? -3.361  20.413  18.319  1.00 17.81 ? 133 LYS   A CD  1 
ATOM   1076 C  CE  . LYS   A 1 132 ? -3.597  21.457  19.320  1.00 20.35 ? 133 LYS   A CE  1 
ATOM   1077 N  NZ  . LYS   A 1 132 ? -2.295  21.915  19.770  1.00 24.69 ? 133 LYS   A NZ  1 
ATOM   1078 N  N   . ALA   A 1 133 ? -6.183  15.878  19.030  1.00 7.78  ? 134 ALA   A N   1 
ATOM   1079 C  CA  . ALA   A 1 133 ? -6.713  14.875  19.947  1.00 7.13  ? 134 ALA   A CA  1 
ATOM   1080 C  C   . ALA   A 1 133 ? -5.640  13.866  20.382  1.00 7.26  ? 134 ALA   A C   1 
ATOM   1081 O  O   . ALA   A 1 133 ? -5.634  13.453  21.537  1.00 7.76  ? 134 ALA   A O   1 
ATOM   1082 C  CB  . ALA   A 1 133 ? -7.893  14.188  19.326  1.00 7.11  ? 134 ALA   A CB  1 
ATOM   1083 N  N   . VAL   A 1 134 ? -4.733  13.479  19.484  1.00 8.21  ? 135 VAL   A N   1 
ATOM   1084 C  CA  . VAL   A 1 134 ? -3.707  12.502  19.821  1.00 9.18  ? 135 VAL   A CA  1 
ATOM   1085 C  C   . VAL   A 1 134 ? -2.523  13.104  20.573  1.00 9.24  ? 135 VAL   A C   1 
ATOM   1086 O  O   . VAL   A 1 134 ? -1.471  12.458  20.768  1.00 11.30 ? 135 VAL   A O   1 
ATOM   1087 C  CB  . VAL   A 1 134 ? -3.249  11.644  18.643  1.00 10.12 ? 135 VAL   A CB  1 
ATOM   1088 C  CG1 . VAL   A 1 134 ? -4.447  10.885  18.081  1.00 11.26 ? 135 VAL   A CG1 1 
ATOM   1089 C  CG2 . VAL   A 1 134 ? -2.544  12.446  17.562  1.00 10.56 ? 135 VAL   A CG2 1 
ATOM   1090 N  N   . GLN   A 1 135 ? -2.687  14.317  21.077  1.00 9.39  ? 136 GLN   A N   1 
ATOM   1091 C  CA  . GLN   A 1 135 ? -1.783  14.905  22.055  1.00 9.77  ? 136 GLN   A CA  1 
ATOM   1092 C  C   . GLN   A 1 135 ? -2.411  14.959  23.442  1.00 9.10  ? 136 GLN   A C   1 
ATOM   1093 O  O   . GLN   A 1 135 ? -1.888  15.613  24.350  1.00 10.23 ? 136 GLN   A O   1 
ATOM   1094 C  CB  . GLN   A 1 135 ? -1.380  16.310  21.600  1.00 11.98 ? 136 GLN   A CB  1 
ATOM   1095 C  CG  . GLN   A 1 135 ? -0.708  16.271  20.243  1.00 14.68 ? 136 GLN   A CG  1 
ATOM   1096 C  CD  . GLN   A 1 135 ? -0.234  17.628  19.792  1.00 18.29 ? 136 GLN   A CD  1 
ATOM   1097 O  OE1 . GLN   A 1 135 ? 0.664   18.230  20.382  1.00 26.33 ? 136 GLN   A OE1 1 
ATOM   1098 N  NE2 . GLN   A 1 135 ? -0.746  18.072  18.664  1.00 22.39 ? 136 GLN   A NE2 1 
ATOM   1099 N  N   . GLN   A 1 136 ? -3.534  14.253  23.617  1.00 8.25  ? 137 GLN   A N   1 
ATOM   1100 C  CA  . GLN   A 1 136 ? -4.323  14.365  24.837  1.00 7.91  ? 137 GLN   A CA  1 
ATOM   1101 C  C   . GLN   A 1 136 ? -4.574  12.981  25.436  1.00 7.19  ? 137 GLN   A C   1 
ATOM   1102 O  O   . GLN   A 1 136 ? -4.803  12.015  24.708  1.00 7.52  ? 137 GLN   A O   1 
ATOM   1103 C  CB  . GLN   A 1 136 ? -5.694  15.019  24.648  1.00 7.86  ? 137 GLN   A CB  1 
ATOM   1104 C  CG  . GLN   A 1 136 ? -5.667  16.215  23.694  1.00 9.57  ? 137 GLN   A CG  1 
ATOM   1105 C  CD  . GLN   A 1 136 ? -4.804  17.342  24.103  1.00 10.18 ? 137 GLN   A CD  1 
ATOM   1106 O  OE1 . GLN   A 1 136 ? -4.596  17.554  25.296  1.00 11.30 ? 137 GLN   A OE1 1 
ATOM   1107 N  NE2 . GLN   A 1 136 ? -4.272  18.067  23.121  1.00 11.93 ? 137 GLN   A NE2 1 
ATOM   1108 N  N   . PRO   A 1 137 ? -4.659  12.880  26.783  1.00 8.29  ? 138 PRO   A N   1 
ATOM   1109 C  CA  . PRO   A 1 137 ? -4.885  11.574  27.411  1.00 8.87  ? 138 PRO   A CA  1 
ATOM   1110 C  C   . PRO   A 1 137 ? -6.299  11.043  27.197  1.00 8.16  ? 138 PRO   A C   1 
ATOM   1111 O  O   . PRO   A 1 137 ? -6.501  9.843   27.349  1.00 11.26 ? 138 PRO   A O   1 
ATOM   1112 C  CB  . PRO   A 1 137 ? -4.589  11.802  28.876  1.00 11.17 ? 138 PRO   A CB  1 
ATOM   1113 C  CG  . PRO   A 1 137 ? -4.642  13.253  29.066  1.00 12.75 ? 138 PRO   A CG  1 
ATOM   1114 C  CD  . PRO   A 1 137 ? -4.267  13.928  27.754  1.00 9.96  ? 138 PRO   A CD  1 
ATOM   1115 N  N   . ASP   A 1 138 ? -7.249  11.931  26.844  1.00 6.97  ? 139 ASP   A N   1 
ATOM   1116 C  CA  . ASP   A 1 138 ? -8.623  11.574  26.540  1.00 6.92  ? 139 ASP   A CA  1 
ATOM   1117 C  C   . ASP   A 1 138 ? -8.982  11.993  25.125  1.00 6.10  ? 139 ASP   A C   1 
ATOM   1118 O  O   . ASP   A 1 138 ? -10.107 12.364  24.825  1.00 6.70  ? 139 ASP   A O   1 
ATOM   1119 C  CB  . ASP   A 1 138 ? -9.596  12.140  27.539  1.00 8.59  ? 139 ASP   A CB  1 
ATOM   1120 C  CG  . ASP   A 1 138 ? -9.596  13.637  27.606  1.00 9.15  ? 139 ASP   A CG  1 
ATOM   1121 O  OD1 . ASP   A 1 138 ? -8.681  14.238  26.984  1.00 9.24  ? 139 ASP   A OD1 1 
ATOM   1122 O  OD2 . ASP   A 1 138 ? -10.464 14.174  28.311  1.00 11.15 ? 139 ASP   A OD2 1 
ATOM   1123 N  N   . GLY   A 1 139 ? -8.012  11.892  24.221  1.00 5.75  ? 140 GLY   A N   1 
ATOM   1124 C  CA  . GLY   A 1 139 ? -8.242  12.333  22.866  1.00 5.74  ? 140 GLY   A CA  1 
ATOM   1125 C  C   . GLY   A 1 139 ? -9.084  11.416  22.004  1.00 5.08  ? 140 GLY   A C   1 
ATOM   1126 O  O   . GLY   A 1 139 ? -9.735  11.902  21.081  1.00 5.85  ? 140 GLY   A O   1 
ATOM   1127 N  N   . LEU   A 1 140 ? -9.006  10.090  22.237  1.00 5.04  ? 141 LEU   A N   1 
ATOM   1128 C  CA  . LEU   A 1 140 ? -9.620  9.133   21.336  1.00 5.37  ? 141 LEU   A CA  1 
ATOM   1129 C  C   . LEU   A 1 140 ? -10.521 8.180   22.115  1.00 4.78  ? 141 LEU   A C   1 
ATOM   1130 O  O   . LEU   A 1 140 ? -10.274 7.905   23.284  1.00 4.99  ? 141 LEU   A O   1 
ATOM   1131 C  CB  . LEU   A 1 140 ? -8.585  8.293   20.587  1.00 5.97  ? 141 LEU   A CB  1 
ATOM   1132 C  CG  . LEU   A 1 140 ? -7.607  9.064   19.689  1.00 6.82  ? 141 LEU   A CG  1 
ATOM   1133 C  CD1 . LEU   A 1 140 ? -6.685  8.043   19.037  1.00 8.10  ? 141 LEU   A CD1 1 
ATOM   1134 C  CD2 . LEU   A 1 140 ? -8.328  9.938   18.658  1.00 7.27  ? 141 LEU   A CD2 1 
ATOM   1135 N  N   . ALA   A 1 141 ? -11.504 7.631   21.407  1.00 5.20  ? 142 ALA   A N   1 
ATOM   1136 C  CA  . ALA   A 1 141 ? -12.290 6.508   21.906  1.00 5.61  ? 142 ALA   A CA  1 
ATOM   1137 C  C   . ALA   A 1 141 ? -12.357 5.497   20.793  1.00 5.29  ? 142 ALA   A C   1 
ATOM   1138 O  O   . ALA   A 1 141 ? -12.715 5.841   19.664  1.00 5.97  ? 142 ALA   A O   1 
ATOM   1139 C  CB  . ALA   A 1 141 ? -13.678 6.941   22.338  1.00 6.36  ? 142 ALA   A CB  1 
ATOM   1140 N  N   . VAL   A 1 142 ? -11.996 4.256   21.100  1.00 5.29  ? 143 VAL   A N   1 
ATOM   1141 C  CA  . VAL   A 1 142 ? -12.061 3.189   20.108  1.00 5.28  ? 143 VAL   A CA  1 
ATOM   1142 C  C   . VAL   A 1 142 ? -13.058 2.149   20.596  1.00 4.74  ? 143 VAL   A C   1 
ATOM   1143 O  O   . VAL   A 1 142 ? -12.936 1.644   21.712  1.00 5.12  ? 143 VAL   A O   1 
ATOM   1144 C  CB  . VAL   A 1 142 ? -10.683 2.579   19.779  1.00 5.71  ? 143 VAL   A CB  1 
ATOM   1145 C  CG1 . VAL   A 1 142 ? -10.828 1.519   18.707  1.00 6.33  ? 143 VAL   A CG1 1 
ATOM   1146 C  CG2 . VAL   A 1 142 ? -9.712  3.658   19.307  1.00 6.72  ? 143 VAL   A CG2 1 
ATOM   1147 N  N   . LEU   A 1 143 ? -14.036 1.884   19.742  1.00 4.77  ? 144 LEU   A N   1 
ATOM   1148 C  CA  . LEU   A 1 143 ? -14.985 0.793   19.952  1.00 5.07  ? 144 LEU   A CA  1 
ATOM   1149 C  C   . LEU   A 1 143 ? -14.419 -0.435  19.290  1.00 4.97  ? 144 LEU   A C   1 
ATOM   1150 O  O   . LEU   A 1 143 ? -14.207 -0.437  18.062  1.00 6.30  ? 144 LEU   A O   1 
ATOM   1151 C  CB  . LEU   A 1 143 ? -16.329 1.236   19.355  1.00 6.72  ? 144 LEU   A CB  1 
ATOM   1152 C  CG  . LEU   A 1 143 ? -17.510 0.292   19.522  1.00 7.91  ? 144 LEU   A CG  1 
ATOM   1153 C  CD1 . LEU   A 1 143 ? -17.792 0.024   20.974  1.00 9.43  ? 144 LEU   A CD1 1 
ATOM   1154 C  CD2 . LEU   A 1 143 ? -18.739 0.906   18.844  1.00 8.85  ? 144 LEU   A CD2 1 
ATOM   1155 N  N   . GLY   A 1 144 ? -14.125 -1.460  20.084  1.00 4.68  ? 145 GLY   A N   1 
ATOM   1156 C  CA  . GLY   A 1 144 ? -13.571 -2.704  19.610  1.00 4.79  ? 145 GLY   A CA  1 
ATOM   1157 C  C   . GLY   A 1 144 ? -14.605 -3.806  19.615  1.00 4.53  ? 145 GLY   A C   1 
ATOM   1158 O  O   . GLY   A 1 144 ? -15.352 -3.943  20.586  1.00 5.74  ? 145 GLY   A O   1 
ATOM   1159 N  N   . ILE   A 1 145 ? -14.658 -4.555  18.509  1.00 4.44  ? 146 ILE   A N   1 
ATOM   1160 C  CA  . ILE   A 1 145 ? -15.667 -5.589  18.301  1.00 4.53  ? 146 ILE   A CA  1 
ATOM   1161 C  C   . ILE   A 1 145 ? -14.957 -6.829  17.804  1.00 4.23  ? 146 ILE   A C   1 
ATOM   1162 O  O   . ILE   A 1 145 ? -14.231 -6.766  16.815  1.00 5.16  ? 146 ILE   A O   1 
ATOM   1163 C  CB  . ILE   A 1 145 ? -16.772 -5.119  17.342  1.00 5.36  ? 146 ILE   A CB  1 
ATOM   1164 C  CG1 . ILE   A 1 145 ? -17.427 -3.858  17.868  1.00 6.70  ? 146 ILE   A CG1 1 
ATOM   1165 C  CG2 . ILE   A 1 145 ? -17.787 -6.214  17.116  1.00 6.74  ? 146 ILE   A CG2 1 
ATOM   1166 C  CD1 . ILE   A 1 145 ? -18.456 -3.222  16.978  1.00 6.86  ? 146 ILE   A CD1 1 
ATOM   1167 N  N   . PHE   A 1 146 ? -15.135 -7.945  18.493  1.00 4.38  ? 147 PHE   A N   1 
ATOM   1168 C  CA  . PHE   A 1 146 ? -14.536 -9.194  18.079  1.00 4.85  ? 147 PHE   A CA  1 
ATOM   1169 C  C   . PHE   A 1 146 ? -15.311 -9.809  16.922  1.00 5.51  ? 147 PHE   A C   1 
ATOM   1170 O  O   . PHE   A 1 146 ? -16.534 -9.692  16.841  1.00 6.05  ? 147 PHE   A O   1 
ATOM   1171 C  CB  . PHE   A 1 146 ? -14.537 -10.165 19.252  1.00 5.03  ? 147 PHE   A CB  1 
ATOM   1172 C  CG  . PHE   A 1 146 ? -13.695 -9.704  20.420  1.00 5.18  ? 147 PHE   A CG  1 
ATOM   1173 C  CD1 . PHE   A 1 146 ? -12.330 -9.519  20.249  1.00 5.31  ? 147 PHE   A CD1 1 
ATOM   1174 C  CD2 . PHE   A 1 146 ? -14.235 -9.450  21.659  1.00 5.50  ? 147 PHE   A CD2 1 
ATOM   1175 C  CE1 . PHE   A 1 146 ? -11.517 -9.124  21.314  1.00 5.82  ? 147 PHE   A CE1 1 
ATOM   1176 C  CE2 . PHE   A 1 146 ? -13.447 -9.055  22.712  1.00 5.82  ? 147 PHE   A CE2 1 
ATOM   1177 C  CZ  . PHE   A 1 146 ? -12.084 -8.911  22.542  1.00 5.75  ? 147 PHE   A CZ  1 
ATOM   1178 N  N   . LEU   A 1 147 ? -14.577 -10.524 16.056  1.00 5.57  ? 148 LEU   A N   1 
ATOM   1179 C  CA  . LEU   A 1 147 ? -15.135 -11.317 14.986  1.00 5.87  ? 148 LEU   A CA  1 
ATOM   1180 C  C   . LEU   A 1 147 ? -14.802 -12.791 15.218  1.00 5.92  ? 148 LEU   A C   1 
ATOM   1181 O  O   . LEU   A 1 147 ? -13.653 -13.132 15.445  1.00 6.42  ? 148 LEU   A O   1 
ATOM   1182 C  CB  . LEU   A 1 147 ? -14.576 -10.934 13.617  1.00 6.16  ? 148 LEU   A CB  1 
ATOM   1183 C  CG  . LEU   A 1 147 ? -15.117 -9.670  12.962  1.00 6.53  ? 148 LEU   A CG  1 
ATOM   1184 C  CD1 . LEU   A 1 147 ? -14.894 -8.413  13.764  1.00 7.13  ? 148 LEU   A CD1 1 
ATOM   1185 C  CD2 . LEU   A 1 147 ? -14.513 -9.515  11.565  1.00 7.13  ? 148 LEU   A CD2 1 
ATOM   1186 N  N   . LYS   A 1 148 ? -15.822 -13.634 15.128  1.00 6.72  ? 149 LYS   A N   1 
ATOM   1187 C  CA  . LYS   A 1 148 ? -15.666 -15.080 15.067  1.00 7.67  ? 149 LYS   A CA  1 
ATOM   1188 C  C   . LYS   A 1 148 ? -16.135 -15.589 13.725  1.00 7.99  ? 149 LYS   A C   1 
ATOM   1189 O  O   . LYS   A 1 148 ? -16.933 -14.948 13.072  1.00 9.33  ? 149 LYS   A O   1 
ATOM   1190 C  CB  . LYS   A 1 148 ? -16.401 -15.755 16.212  1.00 9.18  ? 149 LYS   A CB  1 
ATOM   1191 C  CG  . LYS   A 1 148 ? -17.901 -15.631 16.170  1.00 10.93 ? 149 LYS   A CG  1 
ATOM   1192 C  CD  . LYS   A 1 148 ? -18.572 -16.253 17.391  1.00 14.14 ? 149 LYS   A CD  1 
ATOM   1193 C  CE  . LYS   A 1 148 ? -20.069 -16.325 17.344  1.00 19.41 ? 149 LYS   A CE  1 
ATOM   1194 N  NZ  . LYS   A 1 148 ? -20.680 -16.738 18.619  1.00 23.47 ? 149 LYS   A NZ  1 
ATOM   1195 N  N   . VAL   A 1 149 ? -15.655 -16.761 13.307  1.00 8.97  ? 150 VAL   A N   1 
ATOM   1196 C  CA  . VAL   A 1 149 ? -16.028 -17.363 12.042  1.00 9.54  ? 150 VAL   A CA  1 
ATOM   1197 C  C   . VAL   A 1 149 ? -17.223 -18.274 12.271  1.00 10.84 ? 150 VAL   A C   1 
ATOM   1198 O  O   . VAL   A 1 149 ? -17.170 -19.212 13.073  1.00 11.52 ? 150 VAL   A O   1 
ATOM   1199 C  CB  . VAL   A 1 149 ? -14.820 -18.117 11.443  1.00 10.48 ? 150 VAL   A CB  1 
ATOM   1200 C  CG1 . VAL   A 1 149 ? -15.194 -18.918 10.208  1.00 12.40 ? 150 VAL   A CG1 1 
ATOM   1201 C  CG2 . VAL   A 1 149 ? -13.690 -17.134 11.157  1.00 11.41 ? 150 VAL   A CG2 1 
ATOM   1202 N  N   . GLY   A 1 150 ? -18.285 -17.988 11.531  1.00 10.94 ? 151 GLY   A N   1 
ATOM   1203 C  CA  . GLY   A 1 150 ? -19.466 -18.833 11.550  1.00 11.93 ? 151 GLY   A CA  1 
ATOM   1204 C  C   . GLY   A 1 150 ? -20.373 -18.354 10.418  1.00 11.46 ? 151 GLY   A C   1 
ATOM   1205 O  O   . GLY   A 1 150 ? -20.018 -18.441 9.241   1.00 11.30 ? 151 GLY   A O   1 
ATOM   1206 N  N   . SER   A 1 151 ? -21.542 -17.858 10.774  1.00 12.09 ? 152 SER   A N   1 
ATOM   1207 C  CA  . SER   A 1 151 ? -22.454 -17.292 9.800   1.00 12.34 ? 152 SER   A CA  1 
ATOM   1208 C  C   . SER   A 1 151 ? -21.879 -16.015 9.173   1.00 11.01 ? 152 SER   A C   1 
ATOM   1209 O  O   . SER   A 1 151 ? -21.207 -15.249 9.828   1.00 11.30 ? 152 SER   A O   1 
ATOM   1210 C  CB  . SER   A 1 151 ? -23.782 -16.972 10.463  1.00 15.21 ? 152 SER   A CB  1 
ATOM   1211 O  OG  . SER   A 1 151 ? -24.367 -18.144 11.013  1.00 21.16 ? 152 SER   A OG  1 
ATOM   1212 N  N   . ALA   A 1 152 ? -22.234 -15.762 7.909   1.00 11.13 ? 153 ALA   A N   1 
ATOM   1213 C  CA  . ALA   A 1 152 ? -21.842 -14.537 7.246   1.00 11.28 ? 153 ALA   A CA  1 
ATOM   1214 C  C   . ALA   A 1 152 ? -22.495 -13.328 7.910   1.00 11.20 ? 153 ALA   A C   1 
ATOM   1215 O  O   . ALA   A 1 152 ? -23.618 -13.389 8.400   1.00 12.45 ? 153 ALA   A O   1 
ATOM   1216 C  CB  . ALA   A 1 152 ? -22.208 -14.584 5.765   1.00 12.88 ? 153 ALA   A CB  1 
ATOM   1217 N  N   . LYS   A 1 153 ? -21.789 -12.199 7.824   1.00 11.67 ? 154 LYS   A N   1 
ATOM   1218 C  CA  . LYS   A 1 153 ? -22.297 -10.914 8.263   1.00 11.75 ? 154 LYS   A CA  1 
ATOM   1219 C  C   . LYS   A 1 153 ? -22.697 -10.127 7.039   1.00 12.44 ? 154 LYS   A C   1 
ATOM   1220 O  O   . LYS   A 1 153 ? -21.844 -9.630  6.279   1.00 11.09 ? 154 LYS   A O   1 
ATOM   1221 C  CB  . LYS   A 1 153 ? -21.240 -10.130 9.041   1.00 11.94 ? 154 LYS   A CB  1 
ATOM   1222 C  CG  . LYS   A 1 153 ? -21.748 -8.877  9.793   1.00 13.95 ? 154 LYS   A CG  1 
ATOM   1223 C  CD  . LYS   A 1 153 ? -22.589 -9.255  11.015  1.00 16.63 ? 154 LYS   A CD  1 
ATOM   1224 C  CE  . LYS   A 1 153 ? -22.896 -8.074  11.881  1.00 18.97 ? 154 LYS   A CE  1 
ATOM   1225 N  NZ  . LYS   A 1 153 ? -23.980 -8.375  12.821  1.00 23.52 ? 154 LYS   A NZ  1 
ATOM   1226 N  N   . PRO   A 1 154 ? -23.997 -10.009 6.755   1.00 14.07 ? 155 PRO   A N   1 
ATOM   1227 C  CA  . PRO   A 1 154 ? -24.378 -9.353  5.509   1.00 14.45 ? 155 PRO   A CA  1 
ATOM   1228 C  C   . PRO   A 1 154 ? -23.864 -7.926  5.405   1.00 13.47 ? 155 PRO   A C   1 
ATOM   1229 O  O   . PRO   A 1 154 ? -23.479 -7.484  4.336   1.00 15.37 ? 155 PRO   A O   1 
ATOM   1230 C  CB  . PRO   A 1 154 ? -25.928 -9.410  5.523   1.00 17.25 ? 155 PRO   A CB  1 
ATOM   1231 C  CG  . PRO   A 1 154 ? -26.233 -10.589 6.407   1.00 19.48 ? 155 PRO   A CG  1 
ATOM   1232 C  CD  . PRO   A 1 154 ? -25.156 -10.584 7.473   1.00 16.97 ? 155 PRO   A CD  1 
ATOM   1233 N  N   . GLY   A 1 155 ? -23.852 -7.230  6.549   1.00 12.79 ? 156 GLY   A N   1 
ATOM   1234 C  CA  . GLY   A 1 155 ? -23.413 -5.841  6.604   1.00 13.92 ? 156 GLY   A CA  1 
ATOM   1235 C  C   . GLY   A 1 155 ? -21.916 -5.612  6.347   1.00 12.77 ? 156 GLY   A C   1 
ATOM   1236 O  O   . GLY   A 1 155 ? -21.492 -4.461  6.198   1.00 15.53 ? 156 GLY   A O   1 
ATOM   1237 N  N   . LEU   A 1 156 ? -21.127 -6.699  6.271   1.00 10.89 ? 157 LEU   A N   1 
ATOM   1238 C  CA  . LEU   A 1 156 ? -19.715 -6.638  5.941   1.00 9.73  ? 157 LEU   A CA  1 
ATOM   1239 C  C   . LEU   A 1 156 ? -19.487 -6.872  4.452   1.00 9.92  ? 157 LEU   A C   1 
ATOM   1240 O  O   . LEU   A 1 156 ? -18.396 -6.597  3.968   1.00 10.07 ? 157 LEU   A O   1 
ATOM   1241 C  CB  . LEU   A 1 156 ? -18.969 -7.706  6.754   1.00 9.63  ? 157 LEU   A CB  1 
ATOM   1242 C  CG  . LEU   A 1 156 ? -17.450 -7.792  6.634   1.00 10.18 ? 157 LEU   A CG  1 
ATOM   1243 C  CD1 . LEU   A 1 156 ? -16.772 -6.491  7.045   1.00 10.84 ? 157 LEU   A CD1 1 
ATOM   1244 C  CD2 . LEU   A 1 156 ? -16.935 -8.948  7.480   1.00 10.71 ? 157 LEU   A CD2 1 
ATOM   1245 N  N   . GLN   A 1 157 ? -20.438 -7.443  3.724   1.00 11.31 ? 158 GLN   A N   1 
ATOM   1246 C  CA  . GLN   A 1 157 ? -20.121 -7.949  2.391   1.00 11.79 ? 158 GLN   A CA  1 
ATOM   1247 C  C   . GLN   A 1 157 ? -19.682 -6.832  1.446   1.00 11.22 ? 158 GLN   A C   1 
ATOM   1248 O  O   . GLN   A 1 157 ? -18.825 -7.061  0.619   1.00 11.68 ? 158 GLN   A O   1 
ATOM   1249 C  CB  . GLN   A 1 157 ? -21.230 -8.816  1.813   1.00 13.28 ? 158 GLN   A CB  1 
ATOM   1250 C  CG  . GLN   A 1 157 ? -20.829 -9.555  0.540   1.00 14.37 ? 158 GLN   A CG  1 
ATOM   1251 C  CD  . GLN   A 1 157 ? -19.711 -10.552 0.755   1.00 13.84 ? 158 GLN   A CD  1 
ATOM   1252 O  OE1 . GLN   A 1 157 ? -19.559 -11.140 1.834   1.00 12.64 ? 158 GLN   A OE1 1 
ATOM   1253 N  NE2 . GLN   A 1 157 ? -18.921 -10.740 -0.294  1.00 15.10 ? 158 GLN   A NE2 1 
ATOM   1254 N  N   . LYS   A 1 158 ? -20.197 -5.611  1.576   1.00 12.05 ? 159 LYS   A N   1 
ATOM   1255 C  CA  . LYS   A 1 158 ? -19.773 -4.526  0.715   1.00 12.35 ? 159 LYS   A CA  1 
ATOM   1256 C  C   . LYS   A 1 158 ? -18.292 -4.205  0.908   1.00 11.38 ? 159 LYS   A C   1 
ATOM   1257 O  O   . LYS   A 1 158 ? -17.603 -3.835  -0.056  1.00 12.25 ? 159 LYS   A O   1 
ATOM   1258 C  CB  . LYS   A 1 158 ? -20.646 -3.297  0.953   1.00 14.78 ? 159 LYS   A CB  1 
ATOM   1259 C  CG  . LYS   A 1 158 ? -22.053 -3.457  0.350   1.00 19.11 ? 159 LYS   A CG  1 
ATOM   1260 C  CD  . LYS   A 1 158 ? -23.029 -2.314  0.606   1.00 25.01 ? 159 LYS   A CD  1 
ATOM   1261 C  CE  . LYS   A 1 158 ? -24.380 -2.527  -0.019  1.00 28.05 ? 159 LYS   A CE  1 
ATOM   1262 N  NZ  . LYS   A 1 158 ? -25.195 -1.307  -0.025  1.00 29.85 ? 159 LYS   A NZ  1 
ATOM   1263 N  N   . VAL   A 1 159 ? -17.790 -4.334  2.130   1.00 10.59 ? 160 VAL   A N   1 
ATOM   1264 C  CA  . VAL   A 1 159 ? -16.352 -4.213  2.376   1.00 10.09 ? 160 VAL   A CA  1 
ATOM   1265 C  C   . VAL   A 1 159 ? -15.594 -5.335  1.688   1.00 9.61  ? 160 VAL   A C   1 
ATOM   1266 O  O   . VAL   A 1 159 ? -14.648 -5.103  0.954   1.00 10.33 ? 160 VAL   A O   1 
ATOM   1267 C  CB  . VAL   A 1 159 ? -16.062 -4.214  3.883   1.00 10.24 ? 160 VAL   A CB  1 
ATOM   1268 C  CG1 . VAL   A 1 159 ? -14.569 -4.272  4.166   1.00 11.17 ? 160 VAL   A CG1 1 
ATOM   1269 C  CG2 . VAL   A 1 159 ? -16.678 -2.990  4.562   1.00 11.09 ? 160 VAL   A CG2 1 
ATOM   1270 N  N   . VAL   A 1 160 ? -16.025 -6.577  1.881   1.00 9.61  ? 161 VAL   A N   1 
ATOM   1271 C  CA  . VAL   A 1 160 ? -15.387 -7.723  1.254   1.00 10.18 ? 161 VAL   A CA  1 
ATOM   1272 C  C   . VAL   A 1 160 ? -15.309 -7.528  -0.258  1.00 11.23 ? 161 VAL   A C   1 
ATOM   1273 O  O   . VAL   A 1 160 ? -14.281 -7.828  -0.867  1.00 12.56 ? 161 VAL   A O   1 
ATOM   1274 C  CB  . VAL   A 1 160 ? -16.141 -9.012  1.632   1.00 10.84 ? 161 VAL   A CB  1 
ATOM   1275 C  CG1 . VAL   A 1 160 ? -15.687 -10.225 0.818   1.00 12.03 ? 161 VAL   A CG1 1 
ATOM   1276 C  CG2 . VAL   A 1 160 ? -15.989 -9.304  3.108   1.00 11.54 ? 161 VAL   A CG2 1 
ATOM   1277 N  N   . ASP   A 1 161 ? -16.402 -7.078  -0.859  1.00 11.68 ? 162 ASP   A N   1 
ATOM   1278 C  CA  . ASP   A 1 161 ? -16.479 -7.009  -2.304  1.00 13.66 ? 162 ASP   A CA  1 
ATOM   1279 C  C   . ASP   A 1 161 ? -15.535 -5.952  -2.887  1.00 13.59 ? 162 ASP   A C   1 
ATOM   1280 O  O   . ASP   A 1 161 ? -15.178 -6.051  -4.044  1.00 17.26 ? 162 ASP   A O   1 
ATOM   1281 C  CB  . ASP   A 1 161 ? -17.915 -6.797  -2.720  1.00 17.31 ? 162 ASP   A CB  1 
ATOM   1282 C  CG  . ASP   A 1 161 ? -18.760 -8.056  -2.628  1.00 21.14 ? 162 ASP   A CG  1 
ATOM   1283 O  OD1 . ASP   A 1 161 ? -18.166 -9.152  -2.576  1.00 25.86 ? 162 ASP   A OD1 1 
ATOM   1284 O  OD2 . ASP   A 1 161 ? -19.986 -7.911  -2.543  1.00 30.52 ? 162 ASP   A OD2 1 
ATOM   1285 N  N   . VAL   A 1 162 ? -15.151 -4.921  -2.147  1.00 12.39 ? 163 VAL   A N   1 
ATOM   1286 C  CA  . VAL   A 1 162 ? -14.330 -3.858  -2.692  1.00 12.45 ? 163 VAL   A CA  1 
ATOM   1287 C  C   . VAL   A 1 162 ? -12.836 -4.175  -2.512  1.00 11.54 ? 163 VAL   A C   1 
ATOM   1288 O  O   . VAL   A 1 162 ? -11.981 -3.485  -3.051  1.00 11.72 ? 163 VAL   A O   1 
ATOM   1289 C  CB  . VAL   A 1 162 ? -14.716 -2.497  -2.049  1.00 13.32 ? 163 VAL   A CB  1 
ATOM   1290 C  CG1 . VAL   A 1 162 ? -14.151 -2.309  -0.672  1.00 13.23 ? 163 VAL   A CG1 1 
ATOM   1291 C  CG2 . VAL   A 1 162 ? -14.332 -1.290  -2.909  1.00 14.77 ? 163 VAL   A CG2 1 
ATOM   1292 N  N   . LEU   A 1 163 ? -12.468 -5.195  -1.726  1.00 10.77 ? 164 LEU   A N   1 
ATOM   1293 C  CA  . LEU   A 1 163 ? -11.072 -5.459  -1.446  1.00 10.77 ? 164 LEU   A CA  1 
ATOM   1294 C  C   . LEU   A 1 163 ? -10.254 -5.744  -2.684  1.00 11.45 ? 164 LEU   A C   1 
ATOM   1295 O  O   . LEU   A 1 163 ? -9.063  -5.450  -2.703  1.00 11.84 ? 164 LEU   A O   1 
ATOM   1296 C  CB  . LEU   A 1 163 ? -10.969 -6.577  -0.420  1.00 10.78 ? 164 LEU   A CB  1 
ATOM   1297 C  CG  . LEU   A 1 163 ? -11.565 -6.262  0.963   1.00 11.00 ? 164 LEU   A CG  1 
ATOM   1298 C  CD1 . LEU   A 1 163 ? -11.321 -7.394  1.956   1.00 12.35 ? 164 LEU   A CD1 1 
ATOM   1299 C  CD2 . LEU   A 1 163 ? -11.066 -4.957  1.526   1.00 10.98 ? 164 LEU   A CD2 1 
ATOM   1300 N  N   . ASP   A 1 164 ? -10.877 -6.305  -3.729  1.00 13.85 ? 165 ASP   A N   1 
ATOM   1301 C  CA  . ASP   A 1 164 ? -10.165 -6.623  -4.947  1.00 16.51 ? 165 ASP   A CA  1 
ATOM   1302 C  C   . ASP   A 1 164 ? -9.591  -5.361  -5.565  1.00 16.29 ? 165 ASP   A C   1 
ATOM   1303 O  O   . ASP   A 1 164 ? -8.720  -5.481  -6.419  1.00 18.97 ? 165 ASP   A O   1 
ATOM   1304 C  CB  . ASP   A 1 164 ? -11.026 -7.280  -6.014  1.00 20.49 ? 165 ASP   A CB  1 
ATOM   1305 C  CG  . ASP   A 1 164 ? -11.908 -8.408  -5.526  1.00 26.58 ? 165 ASP   A CG  1 
ATOM   1306 O  OD1 . ASP   A 1 164 ? -12.608 -8.206  -4.509  1.00 32.03 ? 165 ASP   A OD1 1 
ATOM   1307 O  OD2 . ASP   A 1 164 ? -11.928 -9.437  -6.222  1.00 31.64 ? 165 ASP   A OD2 1 
ATOM   1308 N  N   . SER   A 1 165 ? -10.183 -4.200  -5.288  1.00 13.45 ? 166 SER   A N   1 
ATOM   1309 C  CA  . SER   A 1 165 ? -9.740  -2.944  -5.864  1.00 15.21 ? 166 SER   A CA  1 
ATOM   1310 C  C   . SER   A 1 165 ? -8.690  -2.228  -5.025  1.00 13.26 ? 166 SER   A C   1 
ATOM   1311 O  O   . SER   A 1 165 ? -8.162  -1.203  -5.464  1.00 14.34 ? 166 SER   A O   1 
ATOM   1312 C  CB  . SER   A 1 165 ? -10.901 -2.039  -6.137  1.00 17.61 ? 166 SER   A CB  1 
ATOM   1313 O  OG  . SER   A 1 165 ? -11.507 -1.580  -4.949  1.00 18.51 ? 166 SER   A OG  1 
ATOM   1314 N  N   . ILE   A 1 166 ? -8.364  -2.759  -3.835  1.00 10.54 ? 167 ILE   A N   1 
ATOM   1315 C  CA  . ILE   A 1 166 ? -7.368  -2.158  -2.987  1.00 10.47 ? 167 ILE   A CA  1 
ATOM   1316 C  C   . ILE   A 1 166 ? -6.366  -3.213  -2.507  1.00 9.62  ? 167 ILE   A C   1 
ATOM   1317 O  O   . ILE   A 1 166 ? -5.974  -3.241  -1.350  1.00 9.30  ? 167 ILE   A O   1 
ATOM   1318 C  CB  . ILE   A 1 166 ? -7.979  -1.363  -1.816  1.00 10.58 ? 167 ILE   A CB  1 
ATOM   1319 C  CG1 . ILE   A 1 166 ? -8.816  -2.218  -0.916  1.00 10.39 ? 167 ILE   A CG1 1 
ATOM   1320 C  CG2 . ILE   A 1 166 ? -8.756  -0.146  -2.325  1.00 11.94 ? 167 ILE   A CG2 1 
ATOM   1321 C  CD1 . ILE   A 1 166 ? -8.895  -1.707  0.510   1.00 10.80 ? 167 ILE   A CD1 1 
ATOM   1322 N  N   . LYS   A 1 167 ? -5.923  -4.063  -3.429  1.00 10.02 ? 168 LYS   A N   1 
ATOM   1323 C  CA  . LYS   A 1 167 ? -5.172  -5.232  -3.029  1.00 10.22 ? 168 LYS   A CA  1 
ATOM   1324 C  C   . LYS   A 1 167 ? -3.849  -4.888  -2.352  1.00 9.57  ? 168 LYS   A C   1 
ATOM   1325 O  O   . LYS   A 1 167 ? -3.387  -5.570  -1.441  1.00 9.97  ? 168 LYS   A O   1 
ATOM   1326 C  CB  . LYS   A 1 167 ? -4.859  -6.170  -4.190  1.00 12.05 ? 168 LYS   A CB  1 
ATOM   1327 C  CG  . LYS   A 1 167 ? -4.218  -7.499  -3.798  1.00 16.07 ? 168 LYS   A CG  1 
ATOM   1328 C  CD  . LYS   A 1 167 ? -4.156  -8.420  -5.015  1.00 20.02 ? 168 LYS   A CD  1 
ATOM   1329 C  CE  . LYS   A 1 167 ? -3.392  -9.685  -4.779  1.00 23.89 ? 168 LYS   A CE  1 
ATOM   1330 N  NZ  . LYS   A 1 167 ? -3.081  -10.397 -6.028  1.00 26.95 ? 168 LYS   A NZ  1 
ATOM   1331 N  N   . THR   A 1 168 ? -3.222  -3.819  -2.835  1.00 9.45  ? 169 THR   A N   1 
ATOM   1332 C  CA  . THR   A 1 168 ? -1.859  -3.472  -2.475  1.00 9.39  ? 169 THR   A CA  1 
ATOM   1333 C  C   . THR   A 1 168 ? -1.782  -2.094  -1.819  1.00 9.21  ? 169 THR   A C   1 
ATOM   1334 O  O   . THR   A 1 168 ? -2.643  -1.238  -1.943  1.00 9.77  ? 169 THR   A O   1 
ATOM   1335 C  CB  . THR   A 1 168 ? -0.941  -3.548  -3.706  1.00 10.61 ? 169 THR   A CB  1 
ATOM   1336 O  OG1 . THR   A 1 168 ? -1.520  -2.751  -4.748  1.00 11.34 ? 169 THR   A OG1 1 
ATOM   1337 C  CG2 . THR   A 1 168 ? -0.736  -4.982  -4.187  1.00 11.61 ? 169 THR   A CG2 1 
ATOM   1338 N  N   . LYS   A 1 169 ? -0.706  -1.957  -1.052  1.00 10.21 ? 170 LYS   A N   1 
ATOM   1339 C  CA  . LYS   A 1 169 ? -0.408  -0.778  -0.280  1.00 10.04 ? 170 LYS   A CA  1 
ATOM   1340 C  C   . LYS   A 1 169 ? -0.488  0.476   -1.142  1.00 10.93 ? 170 LYS   A C   1 
ATOM   1341 O  O   . LYS   A 1 169 ? 0.097   0.541   -2.252  1.00 11.78 ? 170 LYS   A O   1 
ATOM   1342 C  CB  . LYS   A 1 169 ? 1.027   -0.882  0.253   1.00 11.26 ? 170 LYS   A CB  1 
ATOM   1343 C  CG  . LYS   A 1 169 ? 1.474   0.301   1.102   1.00 12.86 ? 170 LYS   A CG  1 
ATOM   1344 C  CD  . LYS   A 1 169 ? 2.837   0.026   1.723   1.00 16.11 ? 170 LYS   A CD  1 
ATOM   1345 C  CE  . LYS   A 1 169 ? 3.897   -0.353  0.737   1.00 20.26 ? 170 LYS   A CE  1 
ATOM   1346 N  NZ  . LYS   A 1 169 ? 5.230   -0.495  1.314   1.00 24.15 ? 170 LYS   A NZ  1 
ATOM   1347 N  N   . GLY   A 1 170 ? -1.215  1.475   -0.661  1.00 11.13 ? 171 GLY   A N   1 
ATOM   1348 C  CA  . GLY   A 1 170 ? -1.364  2.743   -1.336  1.00 12.05 ? 171 GLY   A CA  1 
ATOM   1349 C  C   . GLY   A 1 170 ? -2.569  2.821   -2.269  1.00 11.82 ? 171 GLY   A C   1 
ATOM   1350 O  O   . GLY   A 1 170 ? -2.874  3.901   -2.767  1.00 14.90 ? 171 GLY   A O   1 
ATOM   1351 N  N   . LYS   A 1 171 ? -3.268  1.719   -2.544  1.00 10.51 ? 172 LYS   A N   1 
ATOM   1352 C  CA  . LYS   A 1 171 ? -4.489  1.793   -3.316  1.00 11.25 ? 172 LYS   A CA  1 
ATOM   1353 C  C   . LYS   A 1 171 ? -5.691  2.194   -2.467  1.00 10.83 ? 172 LYS   A C   1 
ATOM   1354 O  O   . LYS   A 1 171 ? -5.801  1.803   -1.314  1.00 9.96  ? 172 LYS   A O   1 
ATOM   1355 C  CB  . LYS   A 1 171 ? -4.783  0.431   -3.940  1.00 11.89 ? 172 LYS   A CB  1 
ATOM   1356 C  CG  . LYS   A 1 171 ? -3.782  -0.038  -4.989  1.00 13.60 ? 172 LYS   A CG  1 
ATOM   1357 C  CD  . LYS   A 1 171 ? -4.267  -1.057  -6.022  1.00 18.30 ? 172 LYS   A CD  1 
ATOM   1358 C  CE  . LYS   A 1 171 ? -3.487  -1.036  -7.295  1.00 22.76 ? 172 LYS   A CE  1 
ATOM   1359 N  NZ  . LYS   A 1 171 ? -3.807  0.078   -8.197  1.00 27.40 ? 172 LYS   A NZ  1 
ATOM   1360 N  N   . SER   A 1 172 ? -6.564  3.015   -3.060  1.00 11.82 ? 173 SER   A N   1 
ATOM   1361 C  CA  . SER   A 1 172 ? -7.819  3.429   -2.455  1.00 11.78 ? 173 SER   A CA  1 
ATOM   1362 C  C   . SER   A 1 172 ? -8.964  3.309   -3.452  1.00 11.58 ? 173 SER   A C   1 
ATOM   1363 O  O   . SER   A 1 172 ? -8.751  3.200   -4.688  1.00 12.81 ? 173 SER   A O   1 
ATOM   1364 C  CB  . SER   A 1 172 ? -7.724  4.817   -1.916  1.00 12.44 ? 173 SER   A CB  1 
ATOM   1365 O  OG  . SER   A 1 172 ? -7.606  5.783   -2.939  1.00 14.90 ? 173 SER   A OG  1 
ATOM   1366 N  N   . ALA   A 1 173 ? -10.198 3.280   -2.931  1.00 11.53 ? 174 ALA   A N   1 
ATOM   1367 C  CA  . ALA   A 1 173 ? -11.379 3.254   -3.768  1.00 11.83 ? 174 ALA   A CA  1 
ATOM   1368 C  C   . ALA   A 1 173 ? -12.479 4.073   -3.116  1.00 10.88 ? 174 ALA   A C   1 
ATOM   1369 O  O   . ALA   A 1 173 ? -12.547 4.169   -1.904  1.00 10.31 ? 174 ALA   A O   1 
ATOM   1370 C  CB  . ALA   A 1 173 ? -11.860 1.857   -3.993  1.00 12.72 ? 174 ALA   A CB  1 
ATOM   1371 N  N   . ASP   A 1 174 ? -13.318 4.680   -3.938  1.00 12.07 ? 175 ASP   A N   1 
ATOM   1372 C  CA  . ASP   A 1 174 ? -14.467 5.374   -3.410  1.00 13.01 ? 175 ASP   A CA  1 
ATOM   1373 C  C   . ASP   A 1 174 ? -15.285 4.347   -2.630  1.00 12.78 ? 175 ASP   A C   1 
ATOM   1374 O  O   . ASP   A 1 174 ? -15.420 3.167   -3.016  1.00 15.80 ? 175 ASP   A O   1 
ATOM   1375 C  CB  . ASP   A 1 174 ? -15.219 6.038   -4.563  1.00 15.88 ? 175 ASP   A CB  1 
ATOM   1376 C  CG  . ASP   A 1 174 ? -14.472 7.151   -5.325  1.00 18.15 ? 175 ASP   A CG  1 
ATOM   1377 O  OD1 . ASP   A 1 174 ? -13.766 7.965   -4.657  1.00 24.12 ? 175 ASP   A OD1 1 
ATOM   1378 O  OD2 . ASP   A 1 174 ? -14.620 7.290   -6.568  1.00 21.26 ? 175 ASP   A OD2 1 
ATOM   1379 N  N   . PHE   A 1 175 ? -15.826 4.799   -1.494  1.00 12.09 ? 176 PHE   A N   1 
ATOM   1380 C  CA  . PHE   A 1 175 ? -16.578 3.895   -0.645  1.00 11.97 ? 176 PHE   A CA  1 
ATOM   1381 C  C   . PHE   A 1 175 ? -17.634 4.685   0.108   1.00 11.38 ? 176 PHE   A C   1 
ATOM   1382 O  O   . PHE   A 1 175 ? -17.524 4.900   1.287   1.00 14.19 ? 176 PHE   A O   1 
ATOM   1383 C  CB  . PHE   A 1 175 ? -15.646 3.075   0.245   1.00 12.19 ? 176 PHE   A CB  1 
ATOM   1384 C  CG  . PHE   A 1 175 ? -16.289 1.809   0.799   1.00 12.36 ? 176 PHE   A CG  1 
ATOM   1385 C  CD1 . PHE   A 1 175 ? -16.532 0.741   -0.038  1.00 13.73 ? 176 PHE   A CD1 1 
ATOM   1386 C  CD2 . PHE   A 1 175 ? -16.605 1.673   2.141   1.00 12.13 ? 176 PHE   A CD2 1 
ATOM   1387 C  CE1 . PHE   A 1 175 ? -17.097 -0.425  0.440   1.00 14.22 ? 176 PHE   A CE1 1 
ATOM   1388 C  CE2 . PHE   A 1 175 ? -17.132 0.483   2.628   1.00 12.73 ? 176 PHE   A CE2 1 
ATOM   1389 C  CZ  . PHE   A 1 175 ? -17.387 -0.555  1.772   1.00 12.43 ? 176 PHE   A CZ  1 
ATOM   1390 N  N   . THR   A 1 176 ? -18.593 5.181   -0.617  1.00 11.65 ? 177 THR   A N   1 
ATOM   1391 C  CA  . THR   A 1 176 ? -19.644 6.015   -0.073  1.00 10.80 ? 177 THR   A CA  1 
ATOM   1392 C  C   . THR   A 1 176 ? -20.842 5.186   0.359   1.00 10.55 ? 177 THR   A C   1 
ATOM   1393 O  O   . THR   A 1 176 ? -21.045 4.059   -0.105  1.00 11.49 ? 177 THR   A O   1 
ATOM   1394 C  CB  . THR   A 1 176 ? -20.045 7.088   -1.090  1.00 12.61 ? 177 THR   A CB  1 
ATOM   1395 O  OG1 . THR   A 1 176 ? -20.409 6.448   -2.322  1.00 16.03 ? 177 THR   A OG1 1 
ATOM   1396 C  CG2 . THR   A 1 176 ? -18.937 8.092   -1.344  1.00 16.55 ? 177 THR   A CG2 1 
ATOM   1397 N  N   . ASN   A 1 177 ? -21.656 5.768   1.244   1.00 10.86 ? 178 ASN   A N   1 
ATOM   1398 C  CA  . ASN   A 1 177 ? -22.932 5.220   1.665   1.00 11.62 ? 178 ASN   A CA  1 
ATOM   1399 C  C   . ASN   A 1 177 ? -22.807 3.875   2.385   1.00 11.30 ? 178 ASN   A C   1 
ATOM   1400 O  O   . ASN   A 1 177 ? -23.772 3.135   2.373   1.00 14.87 ? 178 ASN   A O   1 
ATOM   1401 C  CB  . ASN   A 1 177 ? -23.893 5.166   0.500   1.00 12.52 ? 178 ASN   A CB  1 
ATOM   1402 C  CG  . ASN   A 1 177 ? -24.029 6.540   -0.113  1.00 13.13 ? 178 ASN   A CG  1 
ATOM   1403 O  OD1 . ASN   A 1 177 ? -24.619 7.411   0.520   1.00 14.91 ? 178 ASN   A OD1 1 
ATOM   1404 N  ND2 . ASN   A 1 177 ? -23.463 6.784   -1.280  1.00 13.44 ? 178 ASN   A ND2 1 
ATOM   1405 N  N   . PHE   A 1 178 ? -21.689 3.615   3.042   1.00 10.31 ? 179 PHE   A N   1 
ATOM   1406 C  CA  . PHE   A 1 178 ? -21.581 2.419   3.835   1.00 10.37 ? 179 PHE   A CA  1 
ATOM   1407 C  C   . PHE   A 1 178 ? -22.092 2.677   5.244   1.00 9.87  ? 179 PHE   A C   1 
ATOM   1408 O  O   . PHE   A 1 178 ? -21.735 3.674   5.860   1.00 11.30 ? 179 PHE   A O   1 
ATOM   1409 C  CB  . PHE   A 1 178 ? -20.121 1.945   3.900   1.00 11.07 ? 179 PHE   A CB  1 
ATOM   1410 C  CG  . PHE   A 1 178 ? -19.995 0.689   4.743   1.00 10.36 ? 179 PHE   A CG  1 
ATOM   1411 C  CD1 . PHE   A 1 178 ? -20.389 -0.533  4.230   1.00 11.22 ? 179 PHE   A CD1 1 
ATOM   1412 C  CD2 . PHE   A 1 178 ? -19.598 0.737   6.075   1.00 9.69  ? 179 PHE   A CD2 1 
ATOM   1413 C  CE1 . PHE   A 1 178 ? -20.312 -1.679  4.980   1.00 11.86 ? 179 PHE   A CE1 1 
ATOM   1414 C  CE2 . PHE   A 1 178 ? -19.560 -0.413  6.829   1.00 9.61  ? 179 PHE   A CE2 1 
ATOM   1415 C  CZ  . PHE   A 1 178 ? -19.925 -1.621  6.293   1.00 10.28 ? 179 PHE   A CZ  1 
ATOM   1416 N  N   . ASP   A 1 179 ? -22.919 1.767   5.756   1.00 10.10 ? 180 ASP   A N   1 
ATOM   1417 C  CA  . ASP   A 1 179 ? -23.557 1.957   7.058   1.00 9.95  ? 180 ASP   A CA  1 
ATOM   1418 C  C   . ASP   A 1 179 ? -22.817 1.157   8.121   1.00 8.86  ? 180 ASP   A C   1 
ATOM   1419 O  O   . ASP   A 1 179 ? -22.930 -0.071  8.174   1.00 9.48  ? 180 ASP   A O   1 
ATOM   1420 C  CB  . ASP   A 1 179 ? -24.998 1.484   6.985   1.00 11.50 ? 180 ASP   A CB  1 
ATOM   1421 C  CG  . ASP   A 1 179 ? -25.799 1.741   8.247   1.00 12.77 ? 180 ASP   A CG  1 
ATOM   1422 O  OD1 . ASP   A 1 179 ? -25.202 2.209   9.219   1.00 11.46 ? 180 ASP   A OD1 1 
ATOM   1423 O  OD2 . ASP   A 1 179 ? -27.006 1.394   8.255   1.00 17.85 ? 180 ASP   A OD2 1 
ATOM   1424 N  N   . PRO   A 1 180 ? -22.033 1.802   9.008   1.00 8.56  ? 181 PRO   A N   1 
ATOM   1425 C  CA  . PRO   A 1 180 ? -21.291 1.034   10.008  1.00 8.67  ? 181 PRO   A CA  1 
ATOM   1426 C  C   . PRO   A 1 180 ? -22.188 0.403   11.064  1.00 8.34  ? 181 PRO   A C   1 
ATOM   1427 O  O   . PRO   A 1 180 ? -21.717 -0.469  11.787  1.00 8.70  ? 181 PRO   A O   1 
ATOM   1428 C  CB  . PRO   A 1 180 ? -20.347 2.088   10.588  1.00 9.43  ? 181 PRO   A CB  1 
ATOM   1429 C  CG  . PRO   A 1 180 ? -21.058 3.371   10.422  1.00 9.59  ? 181 PRO   A CG  1 
ATOM   1430 C  CD  . PRO   A 1 180 ? -21.787 3.252   9.095   1.00 9.36  ? 181 PRO   A CD  1 
ATOM   1431 N  N   . ARG   A 1 181 ? -23.474 0.774   11.112  1.00 8.76  ? 182 ARG   A N   1 
ATOM   1432 C  CA  . ARG   A 1 181 ? -24.381 0.095   12.048  1.00 9.13  ? 182 ARG   A CA  1 
ATOM   1433 C  C   . ARG   A 1 181 ? -24.507 -1.387  11.730  1.00 8.99  ? 182 ARG   A C   1 
ATOM   1434 O  O   . ARG   A 1 181 ? -24.848 -2.176  12.601  1.00 9.73  ? 182 ARG   A O   1 
ATOM   1435 C  CB  . ARG   A 1 181 ? -25.772 0.748   12.021  1.00 10.20 ? 182 ARG   A CB  1 
ATOM   1436 C  CG  . ARG   A 1 181 ? -25.702 2.163   12.579  1.00 11.61 ? 182 ARG   A CG  1 
ATOM   1437 C  CD  . ARG   A 1 181 ? -26.996 2.953   12.437  1.00 13.58 ? 182 ARG   A CD  1 
ATOM   1438 N  NE  . ARG   A 1 181 ? -27.216 3.188   11.018  1.00 16.12 ? 182 ARG   A NE  1 
ATOM   1439 C  CZ  . ARG   A 1 181 ? -28.202 3.939   10.538  1.00 19.02 ? 182 ARG   A CZ  1 
ATOM   1440 N  NH1 . ARG   A 1 181 ? -29.049 4.515   11.361  1.00 19.84 ? 182 ARG   A NH1 1 
ATOM   1441 N  NH2 . ARG   A 1 181 ? -28.320 4.171   9.244   1.00 22.00 ? 182 ARG   A NH2 1 
ATOM   1442 N  N   . GLY   A 1 182 ? -24.252 -1.766  10.473  1.00 9.19  ? 183 GLY   A N   1 
ATOM   1443 C  CA  . GLY   A 1 182 ? -24.325 -3.149  10.071  1.00 9.52  ? 183 GLY   A CA  1 
ATOM   1444 C  C   . GLY   A 1 182 ? -23.210 -4.025  10.603  1.00 9.03  ? 183 GLY   A C   1 
ATOM   1445 O  O   . GLY   A 1 182 ? -23.233 -5.218  10.369  1.00 11.50 ? 183 GLY   A O   1 
ATOM   1446 N  N   . LEU   A 1 183 ? -22.257 -3.441  11.347  1.00 8.44  ? 184 LEU   A N   1 
ATOM   1447 C  CA  . LEU   A 1 183 ? -21.154 -4.177  11.936  1.00 8.62  ? 184 LEU   A CA  1 
ATOM   1448 C  C   . LEU   A 1 183 ? -21.303 -4.327  13.444  1.00 8.20  ? 184 LEU   A C   1 
ATOM   1449 O  O   . LEU   A 1 183 ? -20.415 -4.897  14.074  1.00 9.82  ? 184 LEU   A O   1 
ATOM   1450 C  CB  . LEU   A 1 183 ? -19.843 -3.485  11.583  1.00 9.00  ? 184 LEU   A CB  1 
ATOM   1451 C  CG  . LEU   A 1 183 ? -19.538 -3.450  10.080  1.00 10.42 ? 184 LEU   A CG  1 
ATOM   1452 C  CD1 . LEU   A 1 183 ? -18.234 -2.710  9.847   1.00 11.80 ? 184 LEU   A CD1 1 
ATOM   1453 C  CD2 . LEU   A 1 183 ? -19.525 -4.814  9.424   1.00 12.78 ? 184 LEU   A CD2 1 
ATOM   1454 N  N   . LEU   A 1 184 ? -22.393 -3.853  14.033  1.00 8.26  ? 185 LEU   A N   1 
ATOM   1455 C  CA  . LEU   A 1 184 ? -22.556 -3.851  15.476  1.00 8.31  ? 185 LEU   A CA  1 
ATOM   1456 C  C   . LEU   A 1 184 ? -23.357 -5.078  15.933  1.00 9.17  ? 185 LEU   A C   1 
ATOM   1457 O  O   . LEU   A 1 184 ? -24.414 -5.382  15.388  1.00 11.51 ? 185 LEU   A O   1 
ATOM   1458 C  CB  . LEU   A 1 184 ? -23.310 -2.593  15.936  1.00 8.89  ? 185 LEU   A CB  1 
ATOM   1459 C  CG  . LEU   A 1 184 ? -22.720 -1.235  15.552  1.00 9.62  ? 185 LEU   A CG  1 
ATOM   1460 C  CD1 . LEU   A 1 184 ? -23.622 -0.091  15.988  1.00 10.56 ? 185 LEU   A CD1 1 
ATOM   1461 C  CD2 . LEU   A 1 184 ? -21.340 -1.095  16.115  1.00 11.23 ? 185 LEU   A CD2 1 
ATOM   1462 N  N   . PRO   A 1 185 ? -22.936 -5.744  17.014  1.00 8.24  ? 186 PRO   A N   1 
ATOM   1463 C  CA  . PRO   A 1 185 ? -23.717 -6.870  17.548  1.00 8.65  ? 186 PRO   A CA  1 
ATOM   1464 C  C   . PRO   A 1 185 ? -24.979 -6.335  18.215  1.00 8.73  ? 186 PRO   A C   1 
ATOM   1465 O  O   . PRO   A 1 185 ? -25.191 -5.132  18.350  1.00 9.46  ? 186 PRO   A O   1 
ATOM   1466 C  CB  . PRO   A 1 185 ? -22.772 -7.530  18.529  1.00 9.31  ? 186 PRO   A CB  1 
ATOM   1467 C  CG  . PRO   A 1 185 ? -22.018 -6.337  19.080  1.00 8.36  ? 186 PRO   A CG  1 
ATOM   1468 C  CD  . PRO   A 1 185 ? -21.767 -5.419  17.832  1.00 7.87  ? 186 PRO   A CD  1 
ATOM   1469 N  N   A GLU   A 1 186 ? -25.811 -7.297  18.602  0.50 9.43  ? 187 GLU   A N   1 
ATOM   1470 N  N   B GLU   A 1 186 ? -25.859 -7.243  18.658  0.50 9.40  ? 187 GLU   A N   1 
ATOM   1471 C  CA  A GLU   A 1 186 ? -27.073 -6.995  19.243  0.50 9.73  ? 187 GLU   A CA  1 
ATOM   1472 C  CA  B GLU   A 1 186 ? -27.111 -6.814  19.269  0.50 9.31  ? 187 GLU   A CA  1 
ATOM   1473 C  C   A GLU   A 1 186 ? -26.844 -6.172  20.515  0.50 9.38  ? 187 GLU   A C   1 
ATOM   1474 C  C   B GLU   A 1 186 ? -26.867 -6.111  20.598  0.50 9.42  ? 187 GLU   A C   1 
ATOM   1475 O  O   A GLU   A 1 186 ? -27.457 -5.111  20.664  0.50 10.78 ? 187 GLU   A O   1 
ATOM   1476 O  O   B GLU   A 1 186 ? -27.561 -5.154  20.942  0.50 11.05 ? 187 GLU   A O   1 
ATOM   1477 C  CB  A GLU   A 1 186 ? -27.749 -8.356  19.425  0.50 11.01 ? 187 GLU   A CB  1 
ATOM   1478 C  CB  B GLU   A 1 186 ? -28.051 -7.943  19.683  0.50 9.93  ? 187 GLU   A CB  1 
ATOM   1479 C  CG  A GLU   A 1 186 ? -28.971 -8.317  20.330  0.50 12.90 ? 187 GLU   A CG  1 
ATOM   1480 C  CG  B GLU   A 1 186 ? -28.685 -8.679  18.511  0.50 10.55 ? 187 GLU   A CG  1 
ATOM   1481 C  CD  A GLU   A 1 186 ? -29.699 -9.645  20.364  0.50 14.50 ? 187 GLU   A CD  1 
ATOM   1482 C  CD  B GLU   A 1 186 ? -29.458 -9.917  18.945  0.50 12.59 ? 187 GLU   A CD  1 
ATOM   1483 O  OE1 A GLU   A 1 186 ? -29.424 -10.527 19.518  0.50 15.33 ? 187 GLU   A OE1 1 
ATOM   1484 O  OE1 B GLU   A 1 186 ? -29.557 -10.253 20.162  0.50 13.81 ? 187 GLU   A OE1 1 
ATOM   1485 O  OE2 A GLU   A 1 186 ? -30.512 -9.798  21.278  0.50 17.84 ? 187 GLU   A OE2 1 
ATOM   1486 O  OE2 B GLU   A 1 186 ? -29.966 -10.584 18.045  0.50 14.05 ? 187 GLU   A OE2 1 
ATOM   1487 N  N   . SER   A 1 187 ? -25.969 -6.673  21.413  1.00 8.86  ? 188 SER   A N   1 
ATOM   1488 C  CA  . SER   A 1 187 ? -25.740 -6.096  22.729  1.00 9.31  ? 188 SER   A CA  1 
ATOM   1489 C  C   . SER   A 1 187 ? -24.604 -5.093  22.709  1.00 8.81  ? 188 SER   A C   1 
ATOM   1490 O  O   . SER   A 1 187 ? -23.562 -5.363  22.100  1.00 9.58  ? 188 SER   A O   1 
ATOM   1491 C  CB  . SER   A 1 187 ? -25.379 -7.171  23.729  1.00 10.32 ? 188 SER   A CB  1 
ATOM   1492 O  OG  . SER   A 1 187 ? -25.111 -6.643  25.025  1.00 10.66 ? 188 SER   A OG  1 
ATOM   1493 N  N   . LEU   A 1 188 ? -24.757 -4.001  23.464  1.00 8.37  ? 189 LEU   A N   1 
ATOM   1494 C  CA  . LEU   A 1 188 ? -23.683 -3.051  23.689  1.00 8.73  ? 189 LEU   A CA  1 
ATOM   1495 C  C   . LEU   A 1 188 ? -22.972 -3.291  25.018  1.00 8.48  ? 189 LEU   A C   1 
ATOM   1496 O  O   . LEU   A 1 188 ? -22.197 -2.443  25.432  1.00 9.77  ? 189 LEU   A O   1 
ATOM   1497 C  CB  . LEU   A 1 188 ? -24.159 -1.616  23.597  1.00 11.05 ? 189 LEU   A CB  1 
ATOM   1498 C  CG  . LEU   A 1 188 ? -24.685 -1.168  22.245  1.00 11.57 ? 189 LEU   A CG  1 
ATOM   1499 C  CD1 . LEU   A 1 188 ? -25.221 0.263   22.364  1.00 13.54 ? 189 LEU   A CD1 1 
ATOM   1500 C  CD2 . LEU   A 1 188 ? -23.634 -1.262  21.175  1.00 13.30 ? 189 LEU   A CD2 1 
ATOM   1501 N  N   . ASP   A 1 189 ? -23.152 -4.423  25.688  1.00 7.57  ? 190 ASP   A N   1 
ATOM   1502 C  CA  . ASP   A 1 189 ? -22.360 -4.695  26.881  1.00 7.73  ? 190 ASP   A CA  1 
ATOM   1503 C  C   . ASP   A 1 189 ? -20.877 -4.601  26.553  1.00 6.58  ? 190 ASP   A C   1 
ATOM   1504 O  O   . ASP   A 1 189 ? -20.458 -5.097  25.513  1.00 6.89  ? 190 ASP   A O   1 
ATOM   1505 C  CB  . ASP   A 1 189 ? -22.672 -6.073  27.450  1.00 9.93  ? 190 ASP   A CB  1 
ATOM   1506 C  CG  . ASP   A 1 189 ? -24.030 -6.285  28.106  1.00 12.69 ? 190 ASP   A CG  1 
ATOM   1507 O  OD1 . ASP   A 1 189 ? -24.684 -5.289  28.390  1.00 14.87 ? 190 ASP   A OD1 1 
ATOM   1508 O  OD2 . ASP   A 1 189 ? -24.386 -7.454  28.359  1.00 17.26 ? 190 ASP   A OD2 1 
ATOM   1509 N  N   . TYR   A 1 190 ? -20.101 -4.002  27.450  1.00 6.09  ? 191 TYR   A N   1 
ATOM   1510 C  CA  . TYR   A 1 190 ? -18.697 -3.747  27.142  1.00 5.63  ? 191 TYR   A CA  1 
ATOM   1511 C  C   . TYR   A 1 190 ? -17.832 -3.769  28.385  1.00 5.43  ? 191 TYR   A C   1 
ATOM   1512 O  O   . TYR   A 1 190 ? -18.292 -3.653  29.520  1.00 6.07  ? 191 TYR   A O   1 
ATOM   1513 C  CB  . TYR   A 1 190 ? -18.526 -2.400  26.395  1.00 6.00  ? 191 TYR   A CB  1 
ATOM   1514 C  CG  . TYR   A 1 190 ? -18.895 -1.200  27.246  1.00 6.30  ? 191 TYR   A CG  1 
ATOM   1515 C  CD1 . TYR   A 1 190 ? -17.978 -0.599  28.105  1.00 6.61  ? 191 TYR   A CD1 1 
ATOM   1516 C  CD2 . TYR   A 1 190 ? -20.175 -0.649  27.184  1.00 6.80  ? 191 TYR   A CD2 1 
ATOM   1517 C  CE1 . TYR   A 1 190 ? -18.321 0.490   28.886  1.00 6.99  ? 191 TYR   A CE1 1 
ATOM   1518 C  CE2 . TYR   A 1 190 ? -20.523 0.451   27.940  1.00 7.13  ? 191 TYR   A CE2 1 
ATOM   1519 C  CZ  . TYR   A 1 190 ? -19.604 0.997   28.825  1.00 7.11  ? 191 TYR   A CZ  1 
ATOM   1520 O  OH  . TYR   A 1 190 ? -19.941 2.037   29.648  1.00 8.19  ? 191 TYR   A OH  1 
ATOM   1521 N  N   . TRP   A 1 191 ? -16.536 -3.863  28.107  1.00 5.19  ? 192 TRP   A N   1 
ATOM   1522 C  CA  . TRP   A 1 191 ? -15.477 -3.575  29.054  1.00 5.14  ? 192 TRP   A CA  1 
ATOM   1523 C  C   . TRP   A 1 191 ? -14.760 -2.309  28.609  1.00 5.21  ? 192 TRP   A C   1 
ATOM   1524 O  O   . TRP   A 1 191 ? -14.642 -2.012  27.411  1.00 6.17  ? 192 TRP   A O   1 
ATOM   1525 C  CB  . TRP   A 1 191 ? -14.444 -4.713  29.096  1.00 5.88  ? 192 TRP   A CB  1 
ATOM   1526 C  CG  . TRP   A 1 191 ? -15.001 -6.034  29.540  1.00 6.12  ? 192 TRP   A CG  1 
ATOM   1527 C  CD1 . TRP   A 1 191 ? -15.238 -6.426  30.830  1.00 7.11  ? 192 TRP   A CD1 1 
ATOM   1528 C  CD2 . TRP   A 1 191 ? -15.279 -7.161  28.696  1.00 6.35  ? 192 TRP   A CD2 1 
ATOM   1529 N  NE1 . TRP   A 1 191 ? -15.671 -7.728  30.825  1.00 7.85  ? 192 TRP   A NE1 1 
ATOM   1530 C  CE2 . TRP   A 1 191 ? -15.709 -8.208  29.540  1.00 7.72  ? 192 TRP   A CE2 1 
ATOM   1531 C  CE3 . TRP   A 1 191 ? -15.185 -7.404  27.322  1.00 7.50  ? 192 TRP   A CE3 1 
ATOM   1532 C  CZ2 . TRP   A 1 191 ? -16.037 -9.472  29.024  1.00 9.23  ? 192 TRP   A CZ2 1 
ATOM   1533 C  CZ3 . TRP   A 1 191 ? -15.470 -8.654  26.848  1.00 8.95  ? 192 TRP   A CZ3 1 
ATOM   1534 C  CH2 . TRP   A 1 191 ? -15.875 -9.659  27.676  1.00 9.83  ? 192 TRP   A CH2 1 
ATOM   1535 N  N   . THR   A 1 192 ? -14.238 -1.557  29.575  1.00 5.01  ? 193 THR   A N   1 
ATOM   1536 C  CA  . THR   A 1 192 ? -13.530 -0.322  29.247  1.00 4.87  ? 193 THR   A CA  1 
ATOM   1537 C  C   . THR   A 1 192 ? -12.289 -0.158  30.108  1.00 5.06  ? 193 THR   A C   1 
ATOM   1538 O  O   . THR   A 1 192 ? -12.256 -0.528  31.277  1.00 5.71  ? 193 THR   A O   1 
ATOM   1539 C  CB  . THR   A 1 192 ? -14.458 0.897   29.367  1.00 5.23  ? 193 THR   A CB  1 
ATOM   1540 O  OG1 . THR   A 1 192 ? -13.796 2.094   28.971  1.00 5.84  ? 193 THR   A OG1 1 
ATOM   1541 C  CG2 . THR   A 1 192 ? -15.031 1.097   30.760  1.00 5.98  ? 193 THR   A CG2 1 
ATOM   1542 N  N   . TYR   A 1 193 ? -11.247 0.436   29.518  1.00 5.20  ? 194 TYR   A N   1 
ATOM   1543 C  CA  . TYR   A 1 193 ? -10.022 0.744   30.231  1.00 5.32  ? 194 TYR   A CA  1 
ATOM   1544 C  C   . TYR   A 1 193 ? -9.276  1.799   29.419  1.00 4.99  ? 194 TYR   A C   1 
ATOM   1545 O  O   . TYR   A 1 193 ? -9.501  1.965   28.212  1.00 5.03  ? 194 TYR   A O   1 
ATOM   1546 C  CB  . TYR   A 1 193 ? -9.173  -0.532  30.427  1.00 5.54  ? 194 TYR   A CB  1 
ATOM   1547 C  CG  . TYR   A 1 193 ? -8.477  -1.012  29.164  1.00 5.26  ? 194 TYR   A CG  1 
ATOM   1548 C  CD1 . TYR   A 1 193 ? -9.156  -1.708  28.175  1.00 5.03  ? 194 TYR   A CD1 1 
ATOM   1549 C  CD2 . TYR   A 1 193 ? -7.167  -0.676  28.942  1.00 5.29  ? 194 TYR   A CD2 1 
ATOM   1550 C  CE1 . TYR   A 1 193 ? -8.527  -2.047  26.987  1.00 5.05  ? 194 TYR   A CE1 1 
ATOM   1551 C  CE2 . TYR   A 1 193 ? -6.517  -1.018  27.767  1.00 5.24  ? 194 TYR   A CE2 1 
ATOM   1552 C  CZ  . TYR   A 1 193 ? -7.201  -1.681  26.774  1.00 5.15  ? 194 TYR   A CZ  1 
ATOM   1553 O  OH  . TYR   A 1 193 ? -6.533  -1.979  25.607  1.00 5.29  ? 194 TYR   A OH  1 
ATOM   1554 N  N   . PRO   A 1 194 ? -8.298  2.482   30.062  1.00 5.27  ? 195 PRO   A N   1 
ATOM   1555 C  CA  . PRO   A 1 194 ? -7.478  3.483   29.349  1.00 5.59  ? 195 PRO   A CA  1 
ATOM   1556 C  C   . PRO   A 1 194 ? -6.281  2.822   28.678  1.00 5.00  ? 195 PRO   A C   1 
ATOM   1557 O  O   . PRO   A 1 194 ? -5.553  2.048   29.344  1.00 5.61  ? 195 PRO   A O   1 
ATOM   1558 C  CB  . PRO   A 1 194 ? -7.007  4.420   30.474  1.00 6.64  ? 195 PRO   A CB  1 
ATOM   1559 C  CG  . PRO   A 1 194 ? -6.971  3.513   31.707  1.00 6.87  ? 195 PRO   A CG  1 
ATOM   1560 C  CD  . PRO   A 1 194 ? -8.103  2.550   31.506  1.00 5.99  ? 195 PRO   A CD  1 
ATOM   1561 N  N   . GLY   A 1 195 ? -6.054  3.108   27.411  1.00 5.00  ? 196 GLY   A N   1 
ATOM   1562 C  CA  . GLY   A 1 195 ? -4.937  2.493   26.695  1.00 5.18  ? 196 GLY   A CA  1 
ATOM   1563 C  C   . GLY   A 1 195 ? -4.416  3.385   25.580  1.00 4.83  ? 196 GLY   A C   1 
ATOM   1564 O  O   . GLY   A 1 195 ? -4.354  4.605   25.687  1.00 5.33  ? 196 GLY   A O   1 
ATOM   1565 N  N   . SER   A 1 196 ? -3.999  2.698   24.528  1.00 4.86  ? 197 SER   A N   1 
ATOM   1566 C  CA  . SER   A 1 196 ? -3.193  3.315   23.478  1.00 5.20  ? 197 SER   A CA  1 
ATOM   1567 C  C   . SER   A 1 196 ? -3.660  2.906   22.107  1.00 5.06  ? 197 SER   A C   1 
ATOM   1568 O  O   . SER   A 1 196 ? -4.426  1.933   21.954  1.00 5.38  ? 197 SER   A O   1 
ATOM   1569 C  CB  . SER   A 1 196 ? -1.722  2.936   23.610  1.00 5.45  ? 197 SER   A CB  1 
ATOM   1570 O  OG  . SER   A 1 196 ? -1.457  1.600   23.209  1.00 5.33  ? 197 SER   A OG  1 
ATOM   1571 N  N   . LEU   A 1 197 ? -3.104  3.574   21.079  1.00 5.79  ? 198 LEU   A N   1 
ATOM   1572 C  CA  . LEU   A 1 197 ? -3.104  3.012   19.742  1.00 6.01  ? 198 LEU   A CA  1 
ATOM   1573 C  C   . LEU   A 1 197 ? -2.370  1.682   19.752  1.00 5.34  ? 198 LEU   A C   1 
ATOM   1574 O  O   . LEU   A 1 197 ? -1.365  1.540   20.464  1.00 5.72  ? 198 LEU   A O   1 
ATOM   1575 C  CB  . LEU   A 1 197 ? -2.400  3.958   18.753  1.00 7.08  ? 198 LEU   A CB  1 
ATOM   1576 C  CG  . LEU   A 1 197 ? -2.956  5.372   18.641  1.00 8.97  ? 198 LEU   A CG  1 
ATOM   1577 C  CD1 . LEU   A 1 197 ? -2.090  6.151   17.646  1.00 9.78  ? 198 LEU   A CD1 1 
ATOM   1578 C  CD2 . LEU   A 1 197 ? -4.415  5.307   18.233  1.00 9.68  ? 198 LEU   A CD2 1 
ATOM   1579 N  N   . THR   A 1 198 ? -2.806  0.723   18.934  1.00 5.05  ? 199 THR   A N   1 
ATOM   1580 C  CA  . THR   A 1 198 ? -2.141  -0.572  18.898  1.00 5.11  ? 199 THR   A CA  1 
ATOM   1581 C  C   . THR   A 1 198 ? -1.132  -0.708  17.773  1.00 5.13  ? 199 THR   A C   1 
ATOM   1582 O  O   . THR   A 1 198 ? -0.529  -1.780  17.634  1.00 6.04  ? 199 THR   A O   1 
ATOM   1583 C  CB  . THR   A 1 198 ? -3.146  -1.714  18.814  1.00 5.05  ? 199 THR   A CB  1 
ATOM   1584 O  OG1 . THR   A 1 198 ? -3.768  -1.688  17.536  1.00 5.28  ? 199 THR   A OG1 1 
ATOM   1585 C  CG2 . THR   A 1 198 ? -4.158  -1.696  19.929  1.00 5.77  ? 199 THR   A CG2 1 
ATOM   1586 N  N   . THR   A 1 199 ? -0.936  0.357   16.994  1.00 5.68  ? 200 THR   A N   1 
ATOM   1587 C  CA  . THR   A 1 199 ? 0.119   0.427   16.017  1.00 6.22  ? 200 THR   A CA  1 
ATOM   1588 C  C   . THR   A 1 199 ? 0.960   1.630   16.312  1.00 6.64  ? 200 THR   A C   1 
ATOM   1589 O  O   . THR   A 1 199 ? 0.469   2.601   16.914  1.00 6.92  ? 200 THR   A O   1 
ATOM   1590 C  CB  . THR   A 1 199 ? -0.356  0.509   14.578  1.00 7.87  ? 200 THR   A CB  1 
ATOM   1591 O  OG1 . THR   A 1 199 ? -0.913  1.776   14.327  1.00 12.20 ? 200 THR   A OG1 1 
ATOM   1592 C  CG2 . THR   A 1 199 ? -1.391  -0.516  14.207  1.00 7.42  ? 200 THR   A CG2 1 
ATOM   1593 N  N   . PRO   A 1 200 ? 2.223   1.668   15.858  1.00 6.99  ? 201 PRO   A N   1 
ATOM   1594 C  CA  . PRO   A 1 200 ? 2.973   2.915   15.883  1.00 7.19  ? 201 PRO   A CA  1 
ATOM   1595 C  C   . PRO   A 1 200 ? 2.126   4.057   15.352  1.00 7.52  ? 201 PRO   A C   1 
ATOM   1596 O  O   . PRO   A 1 200 ? 1.457   3.868   14.330  1.00 8.46  ? 201 PRO   A O   1 
ATOM   1597 C  CB  . PRO   A 1 200 ? 4.167   2.579   15.029  1.00 8.20  ? 201 PRO   A CB  1 
ATOM   1598 C  CG  . PRO   A 1 200 ? 4.399   1.141   15.300  1.00 8.50  ? 201 PRO   A CG  1 
ATOM   1599 C  CD  . PRO   A 1 200 ? 2.981   0.553   15.263  1.00 7.63  ? 201 PRO   A CD  1 
ATOM   1600 N  N   . PRO   A 1 201 ? 2.130   5.245   15.993  1.00 7.80  ? 202 PRO   A N   1 
ATOM   1601 C  CA  . PRO   A 1 201 ? 3.041   5.654   17.077  1.00 8.04  ? 202 PRO   A CA  1 
ATOM   1602 C  C   . PRO   A 1 201 ? 2.648   5.262   18.503  1.00 6.99  ? 202 PRO   A C   1 
ATOM   1603 O  O   . PRO   A 1 201 ? 3.288   5.714   19.437  1.00 7.75  ? 202 PRO   A O   1 
ATOM   1604 C  CB  . PRO   A 1 201 ? 3.019   7.204   16.857  1.00 9.60  ? 202 PRO   A CB  1 
ATOM   1605 C  CG  . PRO   A 1 201 ? 1.645   7.473   16.354  1.00 10.01 ? 202 PRO   A CG  1 
ATOM   1606 C  CD  . PRO   A 1 201 ? 1.339   6.351   15.440  1.00 9.09  ? 202 PRO   A CD  1 
ATOM   1607 N  N   . LEU   A 1 202 ? 1.631   4.385   18.692  1.00 6.29  ? 203 LEU   A N   1 
ATOM   1608 C  CA  . LEU   A 1 202 ? 1.383   3.747   20.000  1.00 6.44  ? 203 LEU   A CA  1 
ATOM   1609 C  C   . LEU   A 1 202 ? 0.990   4.780   21.072  1.00 6.44  ? 203 LEU   A C   1 
ATOM   1610 O  O   . LEU   A 1 202 ? 1.184   4.567   22.265  1.00 6.81  ? 203 LEU   A O   1 
ATOM   1611 C  CB  . LEU   A 1 202 ? 2.555   2.866   20.458  1.00 6.46  ? 203 LEU   A CB  1 
ATOM   1612 C  CG  . LEU   A 1 202 ? 2.907   1.715   19.515  1.00 6.51  ? 203 LEU   A CG  1 
ATOM   1613 C  CD1 . LEU   A 1 202 ? 4.225   1.077   19.898  1.00 7.82  ? 203 LEU   A CD1 1 
ATOM   1614 C  CD2 . LEU   A 1 202 ? 1.827   0.668   19.486  1.00 6.68  ? 203 LEU   A CD2 1 
ATOM   1615 N  N   . LEU   A 1 203 ? 0.365   5.874   20.646  1.00 6.91  ? 204 LEU   A N   1 
ATOM   1616 C  CA  . LEU   A 1 203 ? 0.098   7.007   21.533  1.00 7.42  ? 204 LEU   A CA  1 
ATOM   1617 C  C   . LEU   A 1 203 ? -0.961  6.643   22.564  1.00 6.68  ? 204 LEU   A C   1 
ATOM   1618 O  O   . LEU   A 1 203 ? -1.955  5.978   22.257  1.00 6.26  ? 204 LEU   A O   1 
ATOM   1619 C  CB  . LEU   A 1 203 ? -0.305  8.216   20.699  1.00 8.85  ? 204 LEU   A CB  1 
ATOM   1620 C  CG  . LEU   A 1 203 ? 0.779   8.762   19.757  1.00 10.72 ? 204 LEU   A CG  1 
ATOM   1621 C  CD1 . LEU   A 1 203 ? 0.151   9.803   18.878  1.00 11.47 ? 204 LEU   A CD1 1 
ATOM   1622 C  CD2 . LEU   A 1 203 ? 1.979   9.296   20.464  1.00 12.95 ? 204 LEU   A CD2 1 
ATOM   1623 N  N   . GLU   A 1 204 ? -0.730  7.103   23.785  1.00 6.56  ? 205 GLU   A N   1 
ATOM   1624 C  CA  . GLU   A 1 204 ? -1.537  6.724   24.949  1.00 6.38  ? 205 GLU   A CA  1 
ATOM   1625 C  C   . GLU   A 1 204 ? -2.700  7.697   25.137  1.00 6.44  ? 205 GLU   A C   1 
ATOM   1626 O  O   . GLU   A 1 204 ? -2.746  8.499   26.077  1.00 7.91  ? 205 GLU   A O   1 
ATOM   1627 C  CB  . GLU   A 1 204 ? -0.647  6.586   26.177  1.00 6.84  ? 205 GLU   A CB  1 
ATOM   1628 C  CG  . GLU   A 1 204 ? 0.281   5.384   26.032  1.00 7.53  ? 205 GLU   A CG  1 
ATOM   1629 C  CD  . GLU   A 1 204 ? 1.188   5.122   27.202  1.00 7.92  ? 205 GLU   A CD  1 
ATOM   1630 O  OE1 . GLU   A 1 204 ? 1.498   6.051   27.983  1.00 9.24  ? 205 GLU   A OE1 1 
ATOM   1631 O  OE2 . GLU   A 1 204 ? 1.632   3.946   27.346  1.00 8.11  ? 205 GLU   A OE2 1 
ATOM   1632 N  N   A CYS   A 1 205 ? -3.636  7.629   24.195  0.50 6.09  ? 206 CYS   A N   1 
ATOM   1633 N  N   B CYS   A 1 205 ? -3.676  7.637   24.207  0.50 5.54  ? 206 CYS   A N   1 
ATOM   1634 C  CA  A CYS   A 1 205 ? -4.665  8.644   24.128  0.50 6.58  ? 206 CYS   A CA  1 
ATOM   1635 C  CA  B CYS   A 1 205 ? -4.746  8.631   24.086  0.50 5.61  ? 206 CYS   A CA  1 
ATOM   1636 C  C   A CYS   A 1 205 ? -6.057  8.027   24.040  0.50 5.62  ? 206 CYS   A C   1 
ATOM   1637 C  C   B CYS   A 1 205 ? -6.147  8.027   24.192  0.50 5.37  ? 206 CYS   A C   1 
ATOM   1638 O  O   A CYS   A 1 205 ? -6.985  8.773   23.723  0.50 5.78  ? 206 CYS   A O   1 
ATOM   1639 O  O   B CYS   A 1 205 ? -7.182  8.723   24.165  0.50 5.54  ? 206 CYS   A O   1 
ATOM   1640 C  CB  A CYS   A 1 205 ? -4.451  9.624   22.989  0.50 7.65  ? 206 CYS   A CB  1 
ATOM   1641 C  CB  B CYS   A 1 205 ? -4.713  9.353   22.752  0.50 5.77  ? 206 CYS   A CB  1 
ATOM   1642 S  SG  A CYS   A 1 205 ? -4.356  8.588   21.327  0.50 17.02 ? 206 CYS   A SG  1 
ATOM   1643 S  SG  B CYS   A 1 205 ? -2.942  10.068  22.556  0.50 7.37  ? 206 CYS   A SG  1 
ATOM   1644 N  N   . VAL   A 1 206 ? -6.224  6.703   24.277  1.00 5.52  ? 207 VAL   A N   1 
ATOM   1645 C  CA  . VAL   A 1 206 ? -7.448  5.999   23.929  1.00 5.26  ? 207 VAL   A CA  1 
ATOM   1646 C  C   . VAL   A 1 206 ? -8.217  5.578   25.165  1.00 5.24  ? 207 VAL   A C   1 
ATOM   1647 O  O   . VAL   A 1 206 ? -7.666  4.914   26.043  1.00 6.70  ? 207 VAL   A O   1 
ATOM   1648 C  CB  . VAL   A 1 206 ? -7.128  4.756   23.095  1.00 5.48  ? 207 VAL   A CB  1 
ATOM   1649 C  CG1 . VAL   A 1 206 ? -8.405  4.036   22.709  1.00 5.74  ? 207 VAL   A CG1 1 
ATOM   1650 C  CG2 . VAL   A 1 206 ? -6.379  5.116   21.808  1.00 6.06  ? 207 VAL   A CG2 1 
ATOM   1651 N  N   . THR   A 1 207 ? -9.520  5.877   25.186  1.00 5.00  ? 208 THR   A N   1 
ATOM   1652 C  CA  . THR   A 1 207 ? -10.468 5.154   26.029  1.00 5.15  ? 208 THR   A CA  1 
ATOM   1653 C  C   . THR   A 1 207 ? -11.015 3.999   25.212  1.00 4.54  ? 208 THR   A C   1 
ATOM   1654 O  O   . THR   A 1 207 ? -11.663 4.205   24.186  1.00 5.01  ? 208 THR   A O   1 
ATOM   1655 C  CB  . THR   A 1 207 ? -11.606 6.062   26.494  1.00 5.60  ? 208 THR   A CB  1 
ATOM   1656 O  OG1 . THR   A 1 207 ? -11.079 7.167   27.219  1.00 6.58  ? 208 THR   A OG1 1 
ATOM   1657 C  CG2 . THR   A 1 207 ? -12.539 5.266   27.388  1.00 6.57  ? 208 THR   A CG2 1 
ATOM   1658 N  N   . TRP   A 1 208 ? -10.651 2.777   25.630  1.00 4.57  ? 209 TRP   A N   1 
ATOM   1659 C  CA  . TRP   A 1 208 ? -11.101 1.588   24.935  1.00 4.49  ? 209 TRP   A CA  1 
ATOM   1660 C  C   . TRP   A 1 208 ? -12.470 1.167   25.444  1.00 4.59  ? 209 TRP   A C   1 
ATOM   1661 O  O   . TRP   A 1 208 ? -12.683 1.122   26.654  1.00 5.21  ? 209 TRP   A O   1 
ATOM   1662 C  CB  . TRP   A 1 208 ? -10.104 0.426   25.140  1.00 4.82  ? 209 TRP   A CB  1 
ATOM   1663 C  CG  . TRP   A 1 208 ? -8.948  0.526   24.208  1.00 4.67  ? 209 TRP   A CG  1 
ATOM   1664 C  CD1 . TRP   A 1 208 ? -7.715  1.083   24.408  1.00 5.36  ? 209 TRP   A CD1 1 
ATOM   1665 C  CD2 . TRP   A 1 208 ? -8.977  0.091   22.844  1.00 4.81  ? 209 TRP   A CD2 1 
ATOM   1666 N  NE1 . TRP   A 1 208 ? -6.997  1.020   23.260  1.00 5.80  ? 209 TRP   A NE1 1 
ATOM   1667 C  CE2 . TRP   A 1 208 ? -7.719  0.406   22.277  1.00 5.40  ? 209 TRP   A CE2 1 
ATOM   1668 C  CE3 . TRP   A 1 208 ? -9.930  -0.565  22.049  1.00 4.85  ? 209 TRP   A CE3 1 
ATOM   1669 C  CZ2 . TRP   A 1 208 ? -7.415  0.126   20.953  1.00 6.01  ? 209 TRP   A CZ2 1 
ATOM   1670 C  CZ3 . TRP   A 1 208 ? -9.612  -0.881  20.754  1.00 5.70  ? 209 TRP   A CZ3 1 
ATOM   1671 C  CH2 . TRP   A 1 208 ? -8.367  -0.534  20.218  1.00 6.09  ? 209 TRP   A CH2 1 
ATOM   1672 N  N   . ILE   A 1 209 ? -13.344 0.796   24.504  1.00 4.48  ? 210 ILE   A N   1 
ATOM   1673 C  CA  . ILE   A 1 209 ? -14.670 0.270   24.784  1.00 4.74  ? 210 ILE   A CA  1 
ATOM   1674 C  C   . ILE   A 1 209 ? -14.751 -1.001  23.955  1.00 4.43  ? 210 ILE   A C   1 
ATOM   1675 O  O   . ILE   A 1 209 ? -14.899 -0.911  22.743  1.00 5.28  ? 210 ILE   A O   1 
ATOM   1676 C  CB  . ILE   A 1 209 ? -15.744 1.296   24.437  1.00 5.49  ? 210 ILE   A CB  1 
ATOM   1677 C  CG1 . ILE   A 1 209 ? -15.583 2.564   25.284  1.00 6.52  ? 210 ILE   A CG1 1 
ATOM   1678 C  CG2 . ILE   A 1 209 ? -17.133 0.689   24.633  1.00 6.29  ? 210 ILE   A CG2 1 
ATOM   1679 C  CD1 . ILE   A 1 209 ? -16.410 3.748   24.857  1.00 7.87  ? 210 ILE   A CD1 1 
ATOM   1680 N  N   . VAL   A 1 210 ? -14.624 -2.164  24.604  1.00 4.24  ? 211 VAL   A N   1 
ATOM   1681 C  CA  . VAL   A 1 210 ? -14.540 -3.454  23.919  1.00 4.44  ? 211 VAL   A CA  1 
ATOM   1682 C  C   . VAL   A 1 210 ? -15.844 -4.196  24.170  1.00 4.52  ? 211 VAL   A C   1 
ATOM   1683 O  O   . VAL   A 1 210 ? -16.164 -4.500  25.315  1.00 5.07  ? 211 VAL   A O   1 
ATOM   1684 C  CB  . VAL   A 1 210 ? -13.318 -4.273  24.370  1.00 5.07  ? 211 VAL   A CB  1 
ATOM   1685 C  CG1 . VAL   A 1 210 ? -13.315 -5.615  23.671  1.00 5.72  ? 211 VAL   A CG1 1 
ATOM   1686 C  CG2 . VAL   A 1 210 ? -12.033 -3.483  24.111  1.00 6.00  ? 211 VAL   A CG2 1 
ATOM   1687 N  N   . LEU   A 1 211 ? -16.600 -4.441  23.118  1.00 5.12  ? 212 LEU   A N   1 
ATOM   1688 C  CA  . LEU   A 1 211 ? -17.899 -5.093  23.262  1.00 5.52  ? 212 LEU   A CA  1 
ATOM   1689 C  C   . LEU   A 1 211 ? -17.693 -6.570  23.620  1.00 5.99  ? 212 LEU   A C   1 
ATOM   1690 O  O   . LEU   A 1 211 ? -16.829 -7.257  23.078  1.00 6.55  ? 212 LEU   A O   1 
ATOM   1691 C  CB  . LEU   A 1 211 ? -18.729 -4.968  22.002  1.00 5.98  ? 212 LEU   A CB  1 
ATOM   1692 C  CG  . LEU   A 1 211 ? -19.124 -3.556  21.596  1.00 7.20  ? 212 LEU   A CG  1 
ATOM   1693 C  CD1 . LEU   A 1 211 ? -20.153 -3.587  20.478  1.00 8.13  ? 212 LEU   A CD1 1 
ATOM   1694 C  CD2 . LEU   A 1 211 ? -19.644 -2.739  22.744  1.00 7.70  ? 212 LEU   A CD2 1 
ATOM   1695 N  N   . LYS   A 1 212 ? -18.556 -7.071  24.518  1.00 6.34  ? 213 LYS   A N   1 
ATOM   1696 C  CA  . LYS   A 1 212 ? -18.482 -8.476  24.907  1.00 7.21  ? 213 LYS   A CA  1 
ATOM   1697 C  C   . LYS   A 1 212 ? -18.993 -9.414  23.819  1.00 6.95  ? 213 LYS   A C   1 
ATOM   1698 O  O   . LYS   A 1 212 ? -18.480 -10.526 23.681  1.00 8.52  ? 213 LYS   A O   1 
ATOM   1699 C  CB  . LYS   A 1 212 ? -19.246 -8.686  26.208  1.00 8.68  ? 213 LYS   A CB  1 
ATOM   1700 C  CG  . LYS   A 1 212 ? -19.395 -10.113 26.637  1.00 10.77 ? 213 LYS   A CG  1 
ATOM   1701 C  CD  . LYS   A 1 212 ? -19.915 -10.283 28.038  1.00 13.79 ? 213 LYS   A CD  1 
ATOM   1702 C  CE  . LYS   A 1 212 ? -20.192 -11.682 28.429  1.00 17.53 ? 213 LYS   A CE  1 
ATOM   1703 N  NZ  . LYS   A 1 212 ? -20.724 -11.821 29.780  1.00 22.46 ? 213 LYS   A NZ  1 
ATOM   1704 N  N   . GLU   A 1 213 ? -20.043 -9.032  23.090  1.00 6.66  ? 214 GLU   A N   1 
ATOM   1705 C  CA  . GLU   A 1 213 ? -20.647 -9.925  22.115  1.00 6.87  ? 214 GLU   A CA  1 
ATOM   1706 C  C   . GLU   A 1 213 ? -19.877 -9.813  20.810  1.00 6.72  ? 214 GLU   A C   1 
ATOM   1707 O  O   . GLU   A 1 213 ? -19.812 -8.727  20.225  1.00 6.82  ? 214 GLU   A O   1 
ATOM   1708 C  CB  . GLU   A 1 213 ? -22.095 -9.541  21.883  1.00 7.55  ? 214 GLU   A CB  1 
ATOM   1709 C  CG  . GLU   A 1 213 ? -22.781 -10.519 20.941  1.00 9.99  ? 214 GLU   A CG  1 
ATOM   1710 C  CD  . GLU   A 1 213 ? -24.273 -10.356 20.834  1.00 12.73 ? 214 GLU   A CD  1 
ATOM   1711 O  OE1 . GLU   A 1 213 ? -24.858 -9.351  21.277  1.00 12.36 ? 214 GLU   A OE1 1 
ATOM   1712 O  OE2 . GLU   A 1 213 ? -24.854 -11.348 20.284  1.00 19.57 ? 214 GLU   A OE2 1 
ATOM   1713 N  N   . PRO   A 1 214 ? -19.333 -10.934 20.283  1.00 6.95  ? 215 PRO   A N   1 
ATOM   1714 C  CA  . PRO   A 1 214 ? -18.689 -10.869 18.968  1.00 7.07  ? 215 PRO   A CA  1 
ATOM   1715 C  C   . PRO   A 1 214 ? -19.726 -10.804 17.885  1.00 7.63  ? 215 PRO   A C   1 
ATOM   1716 O  O   . PRO   A 1 214 ? -20.886 -11.184 18.074  1.00 9.31  ? 215 PRO   A O   1 
ATOM   1717 C  CB  . PRO   A 1 214 ? -17.932 -12.187 18.886  1.00 8.02  ? 215 PRO   A CB  1 
ATOM   1718 C  CG  . PRO   A 1 214 ? -18.792 -13.164 19.671  1.00 10.34 ? 215 PRO   A CG  1 
ATOM   1719 C  CD  . PRO   A 1 214 ? -19.307 -12.290 20.871  1.00 8.43  ? 215 PRO   A CD  1 
ATOM   1720 N  N   . ILE   A 1 215 ? -19.308 -10.367 16.697  1.00 7.02  ? 216 ILE   A N   1 
ATOM   1721 C  CA  . ILE   A 1 215 ? -20.076 -10.588 15.499  1.00 7.51  ? 216 ILE   A CA  1 
ATOM   1722 C  C   . ILE   A 1 215 ? -19.543 -11.829 14.822  1.00 7.97  ? 216 ILE   A C   1 
ATOM   1723 O  O   . ILE   A 1 215 ? -18.368 -12.166 14.951  1.00 8.93  ? 216 ILE   A O   1 
ATOM   1724 C  CB  . ILE   A 1 215 ? -20.087 -9.371  14.566  1.00 7.83  ? 216 ILE   A CB  1 
ATOM   1725 C  CG1 . ILE   A 1 215 ? -18.703 -8.986  14.061  1.00 8.10  ? 216 ILE   A CG1 1 
ATOM   1726 C  CG2 . ILE   A 1 215 ? -20.785 -8.201  15.246  1.00 8.55  ? 216 ILE   A CG2 1 
ATOM   1727 C  CD1 . ILE   A 1 215 ? -18.693 -7.987  12.910  1.00 9.71  ? 216 ILE   A CD1 1 
ATOM   1728 N  N   . SER   A 1 216 ? -20.398 -12.514 14.083  1.00 8.93  ? 217 SER   A N   1 
ATOM   1729 C  CA  . SER   A 1 216 ? -20.011 -13.655 13.264  1.00 9.51  ? 217 SER   A CA  1 
ATOM   1730 C  C   . SER   A 1 216 ? -19.821 -13.191 11.821  1.00 9.21  ? 217 SER   A C   1 
ATOM   1731 O  O   . SER   A 1 216 ? -20.648 -12.460 11.277  1.00 10.67 ? 217 SER   A O   1 
ATOM   1732 C  CB  . SER   A 1 216 ? -21.059 -14.731 13.307  1.00 12.11 ? 217 SER   A CB  1 
ATOM   1733 O  OG  . SER   A 1 216 ? -21.115 -15.343 14.569  1.00 15.29 ? 217 SER   A OG  1 
ATOM   1734 N  N   . VAL   A 1 217 ? -18.728 -13.656 11.201  1.00 8.72  ? 218 VAL   A N   1 
ATOM   1735 C  CA  . VAL   A 1 217 ? -18.488 -13.479 9.775   1.00 9.23  ? 218 VAL   A CA  1 
ATOM   1736 C  C   . VAL   A 1 217 ? -18.218 -14.847 9.180   1.00 8.87  ? 218 VAL   A C   1 
ATOM   1737 O  O   . VAL   A 1 217 ? -17.839 -15.778 9.889   1.00 9.72  ? 218 VAL   A O   1 
ATOM   1738 C  CB  . VAL   A 1 217 ? -17.292 -12.536 9.528   1.00 9.54  ? 218 VAL   A CB  1 
ATOM   1739 C  CG1 . VAL   A 1 217 ? -17.538 -11.201 10.190  1.00 10.34 ? 218 VAL   A CG1 1 
ATOM   1740 C  CG2 . VAL   A 1 217 ? -15.965 -13.137 9.945   1.00 10.22 ? 218 VAL   A CG2 1 
ATOM   1741 N  N   . SER   A 1 218 ? -18.396 -15.002 7.874   1.00 9.21  ? 219 SER   A N   1 
ATOM   1742 C  CA  . SER   A 1 218 ? -18.167 -16.336 7.308   1.00 9.48  ? 219 SER   A CA  1 
ATOM   1743 C  C   . SER   A 1 218 ? -16.687 -16.583 7.024   1.00 9.47  ? 219 SER   A C   1 
ATOM   1744 O  O   . SER   A 1 218 ? -15.883 -15.650 6.883   1.00 9.63  ? 219 SER   A O   1 
ATOM   1745 C  CB  . SER   A 1 218 ? -18.949 -16.557 6.055   1.00 9.80  ? 219 SER   A CB  1 
ATOM   1746 O  OG  . SER   A 1 218 ? -18.473 -15.684 5.037   1.00 10.68 ? 219 SER   A OG  1 
ATOM   1747 N  N   A SER   A 1 219 ? -16.367 -17.858 6.868   0.50 10.28 ? 220 SER   A N   1 
ATOM   1748 N  N   B SER   A 1 219 ? -16.335 -17.870 6.887   0.50 10.75 ? 220 SER   A N   1 
ATOM   1749 C  CA  A SER   A 1 219 ? -15.010 -18.214 6.537   0.50 10.67 ? 220 SER   A CA  1 
ATOM   1750 C  CA  B SER   A 1 219 ? -14.988 -18.250 6.490   0.50 11.53 ? 220 SER   A CA  1 
ATOM   1751 C  C   A SER   A 1 219 ? -14.617 -17.535 5.224   0.50 10.65 ? 220 SER   A C   1 
ATOM   1752 C  C   B SER   A 1 219 ? -14.610 -17.518 5.207   0.50 11.10 ? 220 SER   A C   1 
ATOM   1753 O  O   A SER   A 1 219 ? -13.485 -17.088 5.079   0.50 11.54 ? 220 SER   A O   1 
ATOM   1754 O  O   B SER   A 1 219 ? -13.482 -17.062 5.047   0.50 12.07 ? 220 SER   A O   1 
ATOM   1755 C  CB  A SER   A 1 219 ? -14.924 -19.714 6.513   0.50 11.74 ? 220 SER   A CB  1 
ATOM   1756 C  CB  B SER   A 1 219 ? -14.880 -19.771 6.334   0.50 13.69 ? 220 SER   A CB  1 
ATOM   1757 O  OG  A SER   A 1 219 ? -13.601 -20.114 6.232   0.50 11.88 ? 220 SER   A OG  1 
ATOM   1758 O  OG  B SER   A 1 219 ? -15.879 -20.311 5.476   0.50 15.31 ? 220 SER   A OG  1 
ATOM   1759 N  N   . GLU   A 1 220 ? -15.548 -17.442 4.264   1.00 10.44 ? 221 GLU   A N   1 
ATOM   1760 C  CA  . GLU   A 1 220 ? -15.231 -16.844 2.975   1.00 11.35 ? 221 GLU   A CA  1 
ATOM   1761 C  C   . GLU   A 1 220 ? -14.943 -15.344 3.120   1.00 11.22 ? 221 GLU   A C   1 
ATOM   1762 O  O   . GLU   A 1 220 ? -14.093 -14.791 2.406   1.00 12.17 ? 221 GLU   A O   1 
ATOM   1763 C  CB  . GLU   A 1 220 ? -16.368 -17.056 1.983   1.00 12.95 ? 221 GLU   A CB  1 
ATOM   1764 C  CG  . GLU   A 1 220 ? -16.580 -18.522 1.614   1.00 15.54 ? 221 GLU   A CG  1 
ATOM   1765 C  CD  . GLU   A 1 220 ? -17.501 -19.308 2.534   1.00 17.42 ? 221 GLU   A CD  1 
ATOM   1766 O  OE1 . GLU   A 1 220 ? -17.931 -18.857 3.608   1.00 18.90 ? 221 GLU   A OE1 1 
ATOM   1767 O  OE2 . GLU   A 1 220 ? -17.804 -20.444 2.152   1.00 23.49 ? 221 GLU   A OE2 1 
ATOM   1768 N  N   . GLN   A 1 221 ? -15.637 -14.656 4.032   1.00 9.40  ? 222 GLN   A N   1 
ATOM   1769 C  CA  . GLN   A 1 221 ? -15.392 -13.243 4.252   1.00 8.88  ? 222 GLN   A CA  1 
ATOM   1770 C  C   . GLN   A 1 221 ? -13.977 -13.041 4.775   1.00 9.08  ? 222 GLN   A C   1 
ATOM   1771 O  O   . GLN   A 1 221 ? -13.253 -12.185 4.280   1.00 9.85  ? 222 GLN   A O   1 
ATOM   1772 C  CB  . GLN   A 1 221 ? -16.477 -12.665 5.155   1.00 8.88  ? 222 GLN   A CB  1 
ATOM   1773 C  CG  . GLN   A 1 221 ? -17.822 -12.602 4.465   1.00 9.05  ? 222 GLN   A CG  1 
ATOM   1774 C  CD  . GLN   A 1 221 ? -18.934 -12.058 5.323   1.00 9.20  ? 222 GLN   A CD  1 
ATOM   1775 O  OE1 . GLN   A 1 221 ? -19.098 -12.411 6.515   1.00 9.50  ? 222 GLN   A OE1 1 
ATOM   1776 N  NE2 . GLN   A 1 221 ? -19.720 -11.173 4.746   1.00 10.26 ? 222 GLN   A NE2 1 
ATOM   1777 N  N   . VAL   A 1 222 ? -13.607 -13.760 5.824   1.00 9.25  ? 223 VAL   A N   1 
ATOM   1778 C  CA  . VAL   A 1 222 ? -12.278 -13.557 6.388   1.00 9.38  ? 223 VAL   A CA  1 
ATOM   1779 C  C   . VAL   A 1 222 ? -11.192 -14.025 5.416   1.00 10.14 ? 223 VAL   A C   1 
ATOM   1780 O  O   . VAL   A 1 222 ? -10.099 -13.455 5.357   1.00 10.12 ? 223 VAL   A O   1 
ATOM   1781 C  CB  . VAL   A 1 222 ? -12.116 -14.110 7.812   1.00 10.80 ? 223 VAL   A CB  1 
ATOM   1782 C  CG1 . VAL   A 1 222 ? -12.161 -15.607 7.881   1.00 11.76 ? 223 VAL   A CG1 1 
ATOM   1783 C  CG2 . VAL   A 1 222 ? -10.865 -13.545 8.506   1.00 11.50 ? 223 VAL   A CG2 1 
ATOM   1784 N  N   . LEU   A 1 223 ? -11.469 -15.074 4.635   1.00 10.51 ? 224 LEU   A N   1 
ATOM   1785 C  CA  . LEU   A 1 223 ? -10.490 -15.517 3.652   1.00 12.30 ? 224 LEU   A CA  1 
ATOM   1786 C  C   . LEU   A 1 223 ? -10.157 -14.404 2.658   1.00 10.91 ? 224 LEU   A C   1 
ATOM   1787 O  O   . LEU   A 1 223 ? -9.011  -14.289 2.225   1.00 11.52 ? 224 LEU   A O   1 
ATOM   1788 C  CB  . LEU   A 1 223 ? -11.009 -16.786 2.976   1.00 13.69 ? 224 LEU   A CB  1 
ATOM   1789 C  CG  . LEU   A 1 223 ? -10.759 -18.086 3.755   1.00 15.66 ? 224 LEU   A CG  1 
ATOM   1790 C  CD1 . LEU   A 1 223 ? -11.549 -19.252 3.228   1.00 17.15 ? 224 LEU   A CD1 1 
ATOM   1791 C  CD2 . LEU   A 1 223 ? -9.302  -18.468 3.787   1.00 17.05 ? 224 LEU   A CD2 1 
ATOM   1792 N  N   . LYS   A 1 224 ? -11.131 -13.559 2.321   1.00 10.28 ? 225 LYS   A N   1 
ATOM   1793 C  CA  . LYS   A 1 224 ? -10.860 -12.460 1.408   1.00 10.86 ? 225 LYS   A CA  1 
ATOM   1794 C  C   . LYS   A 1 224 ? -9.970  -11.398 2.051   1.00 9.45  ? 225 LYS   A C   1 
ATOM   1795 O  O   . LYS   A 1 224 ? -9.085  -10.872 1.380   1.00 10.41 ? 225 LYS   A O   1 
ATOM   1796 C  CB  . LYS   A 1 224 ? -12.156 -11.784 0.946   1.00 12.84 ? 225 LYS   A CB  1 
ATOM   1797 C  CG  . LYS   A 1 224 ? -11.975 -10.743 -0.134  1.00 17.10 ? 225 LYS   A CG  1 
ATOM   1798 C  CD  . LYS   A 1 224 ? -11.952 -11.397 -1.502  1.00 22.09 ? 225 LYS   A CD  1 
ATOM   1799 C  CE  . LYS   A 1 224 ? -13.324 -11.850 -1.948  1.00 25.91 ? 225 LYS   A CE  1 
ATOM   1800 N  NZ  . LYS   A 1 224 ? -13.355 -12.567 -3.233  1.00 28.83 ? 225 LYS   A NZ  1 
ATOM   1801 N  N   . PHE   A 1 225 ? -10.122 -11.148 3.335   1.00 8.53  ? 226 PHE   A N   1 
ATOM   1802 C  CA  . PHE   A 1 225 ? -9.219  -10.264 4.041   1.00 8.49  ? 226 PHE   A CA  1 
ATOM   1803 C  C   . PHE   A 1 225 ? -7.774  -10.746 3.883   1.00 8.25  ? 226 PHE   A C   1 
ATOM   1804 O  O   . PHE   A 1 225 ? -6.847  -9.962  3.682   1.00 8.42  ? 226 PHE   A O   1 
ATOM   1805 C  CB  . PHE   A 1 225 ? -9.491  -10.191 5.541   1.00 8.17  ? 226 PHE   A CB  1 
ATOM   1806 C  CG  . PHE   A 1 225 ? -10.687 -9.402  6.018   1.00 8.70  ? 226 PHE   A CG  1 
ATOM   1807 C  CD1 . PHE   A 1 225 ? -11.808 -9.121  5.241   1.00 10.62 ? 226 PHE   A CD1 1 
ATOM   1808 C  CD2 . PHE   A 1 225 ? -10.718 -9.019  7.354   1.00 12.51 ? 226 PHE   A CD2 1 
ATOM   1809 C  CE1 . PHE   A 1 225 ? -12.895 -8.433  5.757   1.00 11.58 ? 226 PHE   A CE1 1 
ATOM   1810 C  CE2 . PHE   A 1 225 ? -11.814 -8.350  7.872   1.00 13.42 ? 226 PHE   A CE2 1 
ATOM   1811 C  CZ  . PHE   A 1 225 ? -12.836 -7.987  7.040   1.00 12.13 ? 226 PHE   A CZ  1 
ATOM   1812 N  N   . ARG   A 1 226 ? -7.589  -12.069 3.974   1.00 8.20  ? 227 ARG   A N   1 
ATOM   1813 C  CA  . ARG   A 1 226 ? -6.275  -12.694 3.969   1.00 8.33  ? 227 ARG   A CA  1 
ATOM   1814 C  C   . ARG   A 1 226 ? -5.637  -12.728 2.582   1.00 8.98  ? 227 ARG   A C   1 
ATOM   1815 O  O   . ARG   A 1 226 ? -4.485  -13.128 2.460   1.00 10.34 ? 227 ARG   A O   1 
ATOM   1816 C  CB  . ARG   A 1 226 ? -6.356  -14.127 4.509   1.00 8.64  ? 227 ARG   A CB  1 
ATOM   1817 C  CG  . ARG   A 1 226 ? -6.859  -14.213 5.944   1.00 8.46  ? 227 ARG   A CG  1 
ATOM   1818 C  CD  . ARG   A 1 226 ? -6.886  -15.635 6.410   1.00 9.51  ? 227 ARG   A CD  1 
ATOM   1819 N  NE  . ARG   A 1 226 ? -7.409  -15.812 7.752   1.00 8.86  ? 227 ARG   A NE  1 
ATOM   1820 C  CZ  . ARG   A 1 226 ? -8.310  -16.707 8.100   1.00 9.65  ? 227 ARG   A CZ  1 
ATOM   1821 N  NH1 . ARG   A 1 226 ? -8.762  -17.587 7.264   1.00 11.57 ? 227 ARG   A NH1 1 
ATOM   1822 N  NH2 . ARG   A 1 226 ? -8.809  -16.652 9.308   1.00 10.18 ? 227 ARG   A NH2 1 
ATOM   1823 N  N   . LYS   A 1 227 ? -6.347  -12.297 1.543   1.00 8.42  ? 228 LYS   A N   1 
ATOM   1824 C  CA  . LYS   A 1 227 ? -5.815  -12.157 0.191   1.00 9.49  ? 228 LYS   A CA  1 
ATOM   1825 C  C   . LYS   A 1 227 ? -5.261  -10.771 -0.089  1.00 9.01  ? 228 LYS   A C   1 
ATOM   1826 O  O   . LYS   A 1 227 ? -4.632  -10.565 -1.134  1.00 10.29 ? 228 LYS   A O   1 
ATOM   1827 C  CB  . LYS   A 1 227 ? -6.868  -12.516 -0.848  1.00 12.06 ? 228 LYS   A CB  1 
ATOM   1828 C  CG  . LYS   A 1 227 ? -7.175  -13.998 -0.735  1.00 15.26 ? 228 LYS   A CG  1 
ATOM   1829 C  CD  . LYS   A 1 227 ? -8.096  -14.649 -1.724  1.00 18.89 ? 228 LYS   A CD  1 
ATOM   1830 C  CE  . LYS   A 1 227 ? -8.213  -16.142 -1.494  1.00 22.04 ? 228 LYS   A CE  1 
ATOM   1831 N  NZ  . LYS   A 1 227 ? -9.117  -16.731 -2.487  1.00 24.71 ? 228 LYS   A NZ  1 
ATOM   1832 N  N   . LEU   A 1 228 ? -5.504  -9.816  0.794   1.00 8.20  ? 229 LEU   A N   1 
ATOM   1833 C  CA  . LEU   A 1 228 ? -4.874  -8.519  0.693   1.00 8.72  ? 229 LEU   A CA  1 
ATOM   1834 C  C   . LEU   A 1 228 ? -3.365  -8.663  0.809   1.00 8.06  ? 229 LEU   A C   1 
ATOM   1835 O  O   . LEU   A 1 228 ? -2.849  -9.685  1.219   1.00 8.87  ? 229 LEU   A O   1 
ATOM   1836 C  CB  . LEU   A 1 228 ? -5.395  -7.577  1.765   1.00 8.40  ? 229 LEU   A CB  1 
ATOM   1837 C  CG  . LEU   A 1 228 ? -6.836  -7.105  1.568   1.00 8.87  ? 229 LEU   A CG  1 
ATOM   1838 C  CD1 . LEU   A 1 228 ? -7.367  -6.496  2.852   1.00 9.21  ? 229 LEU   A CD1 1 
ATOM   1839 C  CD2 . LEU   A 1 228 ? -6.926  -6.098  0.430   1.00 9.79  ? 229 LEU   A CD2 1 
ATOM   1840 N  N   . ASN   A 1 229 ? -2.665  -7.607  0.419   1.00 8.29  ? 230 ASN   A N   1 
ATOM   1841 C  CA  . ASN   A 1 229 ? -1.212  -7.564  0.421   1.00 8.93  ? 230 ASN   A CA  1 
ATOM   1842 C  C   . ASN   A 1 229 ? -0.694  -6.405  1.280   1.00 8.84  ? 230 ASN   A C   1 
ATOM   1843 O  O   . ASN   A 1 229 ? -1.180  -5.282  1.219   1.00 9.48  ? 230 ASN   A O   1 
ATOM   1844 C  CB  . ASN   A 1 229 ? -0.631  -7.355  -0.971  1.00 10.02 ? 230 ASN   A CB  1 
ATOM   1845 C  CG  . ASN   A 1 229 ? -0.713  -8.508  -1.940  1.00 11.30 ? 230 ASN   A CG  1 
ATOM   1846 O  OD1 . ASN   A 1 229 ? -0.240  -8.347  -3.072  1.00 13.76 ? 230 ASN   A OD1 1 
ATOM   1847 N  ND2 . ASN   A 1 229 ? -1.268  -9.636  -1.567  1.00 11.76 ? 230 ASN   A ND2 1 
ATOM   1848 N  N   . PHE   A 1 230 ? 0.347   -6.702  2.058   1.00 9.15  ? 231 PHE   A N   1 
ATOM   1849 C  CA  . PHE   A 1 230 ? 1.106   -5.659  2.738   1.00 9.38  ? 231 PHE   A CA  1 
ATOM   1850 C  C   . PHE   A 1 230 ? 1.948   -4.834  1.762   1.00 10.54 ? 231 PHE   A C   1 
ATOM   1851 O  O   . PHE   A 1 230 ? 2.203   -3.657  2.002   1.00 11.19 ? 231 PHE   A O   1 
ATOM   1852 C  CB  . PHE   A 1 230 ? 2.089   -6.246  3.739   1.00 9.78  ? 231 PHE   A CB  1 
ATOM   1853 C  CG  . PHE   A 1 230 ? 1.543   -6.846  5.017   1.00 9.23  ? 231 PHE   A CG  1 
ATOM   1854 C  CD1 . PHE   A 1 230 ? 0.760   -6.090  5.900   1.00 9.66  ? 231 PHE   A CD1 1 
ATOM   1855 C  CD2 . PHE   A 1 230 ? 1.866   -8.151  5.371   1.00 10.25 ? 231 PHE   A CD2 1 
ATOM   1856 C  CE1 . PHE   A 1 230 ? 0.376   -6.609  7.126   1.00 9.58  ? 231 PHE   A CE1 1 
ATOM   1857 C  CE2 . PHE   A 1 230 ? 1.468   -8.646  6.623   1.00 10.38 ? 231 PHE   A CE2 1 
ATOM   1858 C  CZ  . PHE   A 1 230 ? 0.723   -7.871  7.484   1.00 9.59  ? 231 PHE   A CZ  1 
ATOM   1859 N  N   . ASN   A 1 231 ? 2.443   -5.480  0.712   1.00 11.08 ? 232 ASN   A N   1 
ATOM   1860 C  CA  . ASN   A 1 231 ? 3.316   -4.866  -0.271  1.00 11.84 ? 232 ASN   A CA  1 
ATOM   1861 C  C   . ASN   A 1 231 ? 2.538   -3.980  -1.228  1.00 11.55 ? 232 ASN   A C   1 
ATOM   1862 O  O   . ASN   A 1 231 ? 1.326   -4.044  -1.393  1.00 12.04 ? 232 ASN   A O   1 
ATOM   1863 C  CB  . ASN   A 1 231 ? 4.022   -5.935  -1.091  1.00 12.93 ? 232 ASN   A CB  1 
ATOM   1864 C  CG  . ASN   A 1 231 ? 3.005   -6.878  -1.688  1.00 12.41 ? 232 ASN   A CG  1 
ATOM   1865 O  OD1 . ASN   A 1 231 ? 2.507   -7.764  -0.998  1.00 13.19 ? 232 ASN   A OD1 1 
ATOM   1866 N  ND2 . ASN   A 1 231 ? 2.679   -6.718  -2.962  1.00 14.15 ? 232 ASN   A ND2 1 
ATOM   1867 N  N   . GLY   A 1 232 ? 3.323   -3.128  -1.906  1.00 12.82 ? 233 GLY   A N   1 
ATOM   1868 C  CA  . GLY   A 1 232 ? 2.809   -2.331  -3.002  1.00 12.98 ? 233 GLY   A CA  1 
ATOM   1869 C  C   . GLY   A 1 232 ? 2.764   -3.100  -4.323  1.00 12.84 ? 233 GLY   A C   1 
ATOM   1870 O  O   . GLY   A 1 232 ? 3.361   -4.181  -4.443  1.00 13.82 ? 233 GLY   A O   1 
ATOM   1871 N  N   . GLU   A 1 233 ? 2.015   -2.546  -5.284  1.00 12.45 ? 234 GLU   A N   1 
ATOM   1872 C  CA  . GLU   A 1 233 ? 1.929   -3.126  -6.615  1.00 13.19 ? 234 GLU   A CA  1 
ATOM   1873 C  C   . GLU   A 1 233 ? 3.328   -3.275  -7.209  1.00 14.23 ? 234 GLU   A C   1 
ATOM   1874 O  O   . GLU   A 1 233 ? 4.167   -2.384  -7.097  1.00 15.57 ? 234 GLU   A O   1 
ATOM   1875 C  CB  . GLU   A 1 233 ? 1.050   -2.260  -7.510  1.00 13.22 ? 234 GLU   A CB  1 
ATOM   1876 C  CG  . GLU   A 1 233 ? 0.788   -2.812  -8.902  1.00 14.88 ? 234 GLU   A CG  1 
ATOM   1877 C  CD  . GLU   A 1 233 ? 0.036   -1.781  -9.718  1.00 18.30 ? 234 GLU   A CD  1 
ATOM   1878 O  OE1 . GLU   A 1 233 ? -0.236  -0.612  -9.261  1.00 19.32 ? 234 GLU   A OE1 1 
ATOM   1879 O  OE2 . GLU   A 1 233 ? -0.260  -2.148  -10.879 1.00 22.86 ? 234 GLU   A OE2 1 
ATOM   1880 N  N   . GLY   A 1 234 ? 3.580   -4.434  -7.826  1.00 16.18 ? 235 GLY   A N   1 
ATOM   1881 C  CA  . GLY   A 1 234 ? 4.822   -4.683  -8.534  1.00 18.06 ? 235 GLY   A CA  1 
ATOM   1882 C  C   . GLY   A 1 234 ? 5.959   -5.081  -7.602  1.00 18.57 ? 235 GLY   A C   1 
ATOM   1883 O  O   . GLY   A 1 234 ? 7.114   -5.157  -8.011  1.00 22.82 ? 235 GLY   A O   1 
ATOM   1884 N  N   . GLU   A 1 235 ? 5.628   -5.367  -6.340  1.00 17.16 ? 236 GLU   A N   1 
ATOM   1885 C  CA  . GLU   A 1 235 ? 6.600   -5.830  -5.361  1.00 17.27 ? 236 GLU   A CA  1 
ATOM   1886 C  C   . GLU   A 1 235 ? 6.273   -7.274  -4.991  1.00 18.14 ? 236 GLU   A C   1 
ATOM   1887 O  O   . GLU   A 1 235 ? 5.162   -7.744  -5.214  1.00 19.19 ? 236 GLU   A O   1 
ATOM   1888 C  CB  . GLU   A 1 235 ? 6.544   -5.030  -4.060  1.00 17.37 ? 236 GLU   A CB  1 
ATOM   1889 C  CG  . GLU   A 1 235 ? 6.906   -3.559  -4.261  1.00 19.58 ? 236 GLU   A CG  1 
ATOM   1890 C  CD  . GLU   A 1 235 ? 6.632   -2.674  -3.058  1.00 22.31 ? 236 GLU   A CD  1 
ATOM   1891 O  OE1 . GLU   A 1 235 ? 6.141   -3.152  -2.008  1.00 21.64 ? 236 GLU   A OE1 1 
ATOM   1892 O  OE2 . GLU   A 1 235 ? 6.937   -1.471  -3.185  1.00 27.15 ? 236 GLU   A OE2 1 
ATOM   1893 N  N   . PRO   A 1 236 ? 7.226   -8.010  -4.396  1.00 19.29 ? 237 PRO   A N   1 
ATOM   1894 C  CA  . PRO   A 1 236 ? 6.979   -9.404  -4.037  1.00 19.84 ? 237 PRO   A CA  1 
ATOM   1895 C  C   . PRO   A 1 236 ? 5.777   -9.498  -3.100  1.00 17.79 ? 237 PRO   A C   1 
ATOM   1896 O  O   . PRO   A 1 236 ? 5.674   -8.735  -2.155  1.00 18.29 ? 237 PRO   A O   1 
ATOM   1897 C  CB  . PRO   A 1 236 ? 8.266   -9.868  -3.362  1.00 21.24 ? 237 PRO   A CB  1 
ATOM   1898 C  CG  . PRO   A 1 236 ? 9.350   -8.922  -3.908  1.00 22.18 ? 237 PRO   A CG  1 
ATOM   1899 C  CD  . PRO   A 1 236 ? 8.613   -7.596  -4.107  1.00 20.72 ? 237 PRO   A CD  1 
ATOM   1900 N  N   . GLU   A 1 237 ? 4.945   -10.517 -3.296  1.00 16.92 ? 238 GLU   A N   1 
ATOM   1901 C  CA  . GLU   A 1 237 ? 3.690   -10.627 -2.582  1.00 15.80 ? 238 GLU   A CA  1 
ATOM   1902 C  C   . GLU   A 1 237 ? 3.902   -11.102 -1.146  1.00 14.47 ? 238 GLU   A C   1 
ATOM   1903 O  O   . GLU   A 1 237 ? 4.521   -12.124 -0.900  1.00 14.80 ? 238 GLU   A O   1 
ATOM   1904 C  CB  . GLU   A 1 237 ? 2.729   -11.595 -3.263  1.00 17.38 ? 238 GLU   A CB  1 
ATOM   1905 C  CG  . GLU   A 1 237 ? 1.320   -11.521 -2.696  1.00 18.03 ? 238 GLU   A CG  1 
ATOM   1906 C  CD  . GLU   A 1 237 ? 0.243   -12.333 -3.365  1.00 19.03 ? 238 GLU   A CD  1 
ATOM   1907 O  OE1 . GLU   A 1 237 ? 0.614   -13.363 -3.990  1.00 27.35 ? 238 GLU   A OE1 1 
ATOM   1908 O  OE2 . GLU   A 1 237 ? -0.951  -11.925 -3.332  1.00 16.73 ? 238 GLU   A OE2 1 
ATOM   1909 N  N   . GLU   A 1 238 ? 3.365   -10.332 -0.206  1.00 12.57 ? 239 GLU   A N   1 
ATOM   1910 C  CA  . GLU   A 1 238 ? 3.334   -10.616 1.210   1.00 12.99 ? 239 GLU   A CA  1 
ATOM   1911 C  C   . GLU   A 1 238 ? 1.883   -10.496 1.656   1.00 10.92 ? 239 GLU   A C   1 
ATOM   1912 O  O   . GLU   A 1 238 ? 1.340   -9.398  1.713   1.00 12.21 ? 239 GLU   A O   1 
ATOM   1913 C  CB  . GLU   A 1 238 ? 4.135   -9.565  1.986   1.00 16.36 ? 239 GLU   A CB  1 
ATOM   1914 C  CG  . GLU   A 1 238 ? 5.594   -9.341  1.616   1.00 19.56 ? 239 GLU   A CG  1 
ATOM   1915 C  CD  . GLU   A 1 238 ? 6.170   -8.203  2.441   1.00 25.07 ? 239 GLU   A CD  1 
ATOM   1916 O  OE1 . GLU   A 1 238 ? 6.542   -8.383  3.625   1.00 32.35 ? 239 GLU   A OE1 1 
ATOM   1917 O  OE2 . GLU   A 1 238 ? 6.172   -7.080  1.891   1.00 30.10 ? 239 GLU   A OE2 1 
ATOM   1918 N  N   . LEU   A 1 239 ? 1.259   -11.643 1.955   1.00 10.31 ? 240 LEU   A N   1 
ATOM   1919 C  CA  . LEU   A 1 239 ? -0.135  -11.595 2.310   1.00 9.47  ? 240 LEU   A CA  1 
ATOM   1920 C  C   . LEU   A 1 239 ? -0.326  -10.788 3.596   1.00 8.90  ? 240 LEU   A C   1 
ATOM   1921 O  O   . LEU   A 1 239 ? 0.420   -10.940 4.568   1.00 9.21  ? 240 LEU   A O   1 
ATOM   1922 C  CB  . LEU   A 1 239 ? -0.669  -13.010 2.492   1.00 10.01 ? 240 LEU   A CB  1 
ATOM   1923 C  CG  . LEU   A 1 239 ? -0.678  -13.877 1.234   1.00 11.67 ? 240 LEU   A CG  1 
ATOM   1924 C  CD1 . LEU   A 1 239 ? -1.185  -15.246 1.659   1.00 14.18 ? 240 LEU   A CD1 1 
ATOM   1925 C  CD2 . LEU   A 1 239 ? -1.541  -13.243 0.160   1.00 12.30 ? 240 LEU   A CD2 1 
ATOM   1926 N  N   . MET   A 1 240 ? -1.361  -9.963  3.596   1.00 8.58  ? 241 MET   A N   1 
ATOM   1927 C  CA  . MET   A 1 240 ? -1.759  -9.169  4.766   1.00 8.16  ? 241 MET   A CA  1 
ATOM   1928 C  C   . MET   A 1 240 ? -2.537  -10.082 5.697   1.00 7.60  ? 241 MET   A C   1 
ATOM   1929 O  O   . MET   A 1 240 ? -3.741  -10.207 5.588   1.00 8.08  ? 241 MET   A O   1 
ATOM   1930 C  CB  . MET   A 1 240 ? -2.589  -7.948  4.322   1.00 8.32  ? 241 MET   A CB  1 
ATOM   1931 C  CG  . MET   A 1 240 ? -2.925  -7.020  5.478   1.00 8.59  ? 241 MET   A CG  1 
ATOM   1932 S  SD  . MET   A 1 240 ? -3.880  -5.581  4.991   1.00 8.78  ? 241 MET   A SD  1 
ATOM   1933 C  CE  . MET   A 1 240 ? -2.583  -4.542  4.297   1.00 9.63  ? 241 MET   A CE  1 
ATOM   1934 N  N   . VAL   A 1 241 ? -1.790  -10.706 6.616   1.00 7.12  ? 242 VAL   A N   1 
ATOM   1935 C  CA  . VAL   A 1 241 ? -2.297  -11.585 7.653   1.00 6.86  ? 242 VAL   A CA  1 
ATOM   1936 C  C   . VAL   A 1 241 ? -1.492  -11.330 8.913   1.00 6.44  ? 242 VAL   A C   1 
ATOM   1937 O  O   . VAL   A 1 241 ? -0.324  -10.931 8.868   1.00 7.22  ? 242 VAL   A O   1 
ATOM   1938 C  CB  . VAL   A 1 241 ? -2.216  -13.088 7.255   1.00 8.20  ? 242 VAL   A CB  1 
ATOM   1939 C  CG1 . VAL   A 1 241 ? -3.119  -13.393 6.084   1.00 9.21  ? 242 VAL   A CG1 1 
ATOM   1940 C  CG2 . VAL   A 1 241 ? -0.794  -13.545 6.993   1.00 9.05  ? 242 VAL   A CG2 1 
ATOM   1941 N  N   . ASP   A 1 242 ? -2.106  -11.646 10.047  1.00 5.96  ? 243 ASP   A N   1 
ATOM   1942 C  CA  . ASP   A 1 242 ? -1.447  -11.534 11.332  1.00 6.38  ? 243 ASP   A CA  1 
ATOM   1943 C  C   . ASP   A 1 242 ? -0.944  -10.114 11.588  1.00 5.94  ? 243 ASP   A C   1 
ATOM   1944 O  O   . ASP   A 1 242 ? 0.137   -9.889  12.104  1.00 7.51  ? 243 ASP   A O   1 
ATOM   1945 C  CB  . ASP   A 1 242 ? -0.373  -12.593 11.530  1.00 7.08  ? 243 ASP   A CB  1 
ATOM   1946 C  CG  . ASP   A 1 242 ? -0.964  -13.993 11.631  1.00 7.25  ? 243 ASP   A CG  1 
ATOM   1947 O  OD1 . ASP   A 1 242 ? -1.994  -14.149 12.309  1.00 7.14  ? 243 ASP   A OD1 1 
ATOM   1948 O  OD2 . ASP   A 1 242 ? -0.384  -14.925 11.026  1.00 9.12  ? 243 ASP   A OD2 1 
ATOM   1949 N  N   . ASN   A 1 243 ? -1.828  -9.148  11.302  1.00 5.63  ? 244 ASN   A N   1 
ATOM   1950 C  CA  . ASN   A 1 243 ? -1.557  -7.727  11.521  1.00 5.68  ? 244 ASN   A CA  1 
ATOM   1951 C  C   . ASN   A 1 243 ? -2.100  -7.287  12.893  1.00 5.31  ? 244 ASN   A C   1 
ATOM   1952 O  O   . ASN   A 1 243 ? -2.754  -6.246  12.992  1.00 6.46  ? 244 ASN   A O   1 
ATOM   1953 C  CB  . ASN   A 1 243 ? -2.063  -6.880  10.370  1.00 5.67  ? 244 ASN   A CB  1 
ATOM   1954 C  CG  . ASN   A 1 243 ? -3.562  -7.008  10.173  1.00 6.34  ? 244 ASN   A CG  1 
ATOM   1955 O  OD1 . ASN   A 1 243 ? -4.210  -7.882  10.729  1.00 6.80  ? 244 ASN   A OD1 1 
ATOM   1956 N  ND2 . ASN   A 1 243 ? -4.111  -6.154  9.337   1.00 9.24  ? 244 ASN   A ND2 1 
ATOM   1957 N  N   . TRP   A 1 244 ? -1.819  -8.077  13.919  1.00 5.20  ? 245 TRP   A N   1 
ATOM   1958 C  CA  . TRP   A 1 244 ? -2.243  -7.837  15.301  1.00 5.23  ? 245 TRP   A CA  1 
ATOM   1959 C  C   . TRP   A 1 244 ? -1.038  -7.744  16.212  1.00 5.65  ? 245 TRP   A C   1 
ATOM   1960 O  O   . TRP   A 1 244 ? -0.057  -8.457  16.056  1.00 6.77  ? 245 TRP   A O   1 
ATOM   1961 C  CB  . TRP   A 1 244 ? -3.225  -8.924  15.783  1.00 5.66  ? 245 TRP   A CB  1 
ATOM   1962 C  CG  . TRP   A 1 244 ? -2.728  -10.330 15.604  1.00 5.59  ? 245 TRP   A CG  1 
ATOM   1963 C  CD1 . TRP   A 1 244 ? -2.874  -11.080 14.487  1.00 5.59  ? 245 TRP   A CD1 1 
ATOM   1964 C  CD2 . TRP   A 1 244 ? -2.161  -11.182 16.589  1.00 5.93  ? 245 TRP   A CD2 1 
ATOM   1965 N  NE1 . TRP   A 1 244 ? -2.346  -12.328 14.671  1.00 6.07  ? 245 TRP   A NE1 1 
ATOM   1966 C  CE2 . TRP   A 1 244 ? -1.908  -12.424 15.956  1.00 6.14  ? 245 TRP   A CE2 1 
ATOM   1967 C  CE3 . TRP   A 1 244 ? -1.834  -11.021 17.936  1.00 6.68  ? 245 TRP   A CE3 1 
ATOM   1968 C  CZ2 . TRP   A 1 244 ? -1.347  -13.481 16.645  1.00 7.40  ? 245 TRP   A CZ2 1 
ATOM   1969 C  CZ3 . TRP   A 1 244 ? -1.297  -12.099 18.618  1.00 7.82  ? 245 TRP   A CZ3 1 
ATOM   1970 C  CH2 . TRP   A 1 244 ? -1.083  -13.321 17.974  1.00 8.09  ? 245 TRP   A CH2 1 
ATOM   1971 N  N   . ARG   A 1 245 ? -1.164  -6.855  17.202  1.00 5.19  ? 246 ARG   A N   1 
ATOM   1972 C  CA  . ARG   A 1 245 ? -0.232  -6.728  18.291  1.00 5.48  ? 246 ARG   A CA  1 
ATOM   1973 C  C   . ARG   A 1 245 ? -0.719  -7.611  19.432  1.00 5.71  ? 246 ARG   A C   1 
ATOM   1974 O  O   . ARG   A 1 245 ? -1.913  -7.611  19.745  1.00 6.21  ? 246 ARG   A O   1 
ATOM   1975 C  CB  . ARG   A 1 245 ? -0.144  -5.279  18.771  1.00 5.51  ? 246 ARG   A CB  1 
ATOM   1976 C  CG  . ARG   A 1 245 ? 0.967   -5.014  19.751  1.00 5.53  ? 246 ARG   A CG  1 
ATOM   1977 C  CD  . ARG   A 1 245 ? 0.897   -3.641  20.367  1.00 5.63  ? 246 ARG   A CD  1 
ATOM   1978 N  NE  . ARG   A 1 245 ? 2.119   -3.338  21.088  1.00 6.20  ? 246 ARG   A NE  1 
ATOM   1979 C  CZ  . ARG   A 1 245 ? 2.336   -2.327  21.896  1.00 6.48  ? 246 ARG   A CZ  1 
ATOM   1980 N  NH1 . ARG   A 1 245 ? 1.333   -1.551  22.291  1.00 7.07  ? 246 ARG   A NH1 1 
ATOM   1981 N  NH2 . ARG   A 1 245 ? 3.572   -2.073  22.323  1.00 7.58  ? 246 ARG   A NH2 1 
ATOM   1982 N  N   . PRO   A 1 246 ? 0.171   -8.394  20.081  1.00 6.55  ? 247 PRO   A N   1 
ATOM   1983 C  CA  . PRO   A 1 246 ? -0.260  -9.193  21.206  1.00 7.06  ? 247 PRO   A CA  1 
ATOM   1984 C  C   . PRO   A 1 246 ? -0.563  -8.341  22.438  1.00 6.86  ? 247 PRO   A C   1 
ATOM   1985 O  O   . PRO   A 1 246 ? -0.223  -7.161  22.544  1.00 6.62  ? 247 PRO   A O   1 
ATOM   1986 C  CB  . PRO   A 1 246 ? 0.900   -10.135 21.462  1.00 8.75  ? 247 PRO   A CB  1 
ATOM   1987 C  CG  . PRO   A 1 246 ? 2.081   -9.347  20.998  1.00 10.69 ? 247 PRO   A CG  1 
ATOM   1988 C  CD  . PRO   A 1 246 ? 1.600   -8.578  19.795  1.00 7.96  ? 247 PRO   A CD  1 
ATOM   1989 N  N   . ALA   A 1 247 ? -1.197  -8.996  23.415  1.00 7.10  ? 248 ALA   A N   1 
ATOM   1990 C  CA  . ALA   A 1 247 ? -1.518  -8.345  24.675  1.00 7.28  ? 248 ALA   A CA  1 
ATOM   1991 C  C   . ALA   A 1 247 ? -0.277  -7.809  25.398  1.00 6.88  ? 248 ALA   A C   1 
ATOM   1992 O  O   . ALA   A 1 247 ? 0.773   -8.467  25.438  1.00 8.06  ? 248 ALA   A O   1 
ATOM   1993 C  CB  . ALA   A 1 247 ? -2.306  -9.285  25.567  1.00 8.35  ? 248 ALA   A CB  1 
ATOM   1994 N  N   . GLN   A 1 248 ? -0.439  -6.622  25.987  1.00 6.49  ? 249 GLN   A N   1 
ATOM   1995 C  CA  . GLN   A 1 248 ? 0.600   -5.885  26.676  1.00 7.12  ? 249 GLN   A CA  1 
ATOM   1996 C  C   . GLN   A 1 248 ? 0.322   -5.877  28.167  1.00 6.94  ? 249 GLN   A C   1 
ATOM   1997 O  O   . GLN   A 1 248 ? -0.803  -6.108  28.610  1.00 7.93  ? 249 GLN   A O   1 
ATOM   1998 C  CB  . GLN   A 1 248 ? 0.637   -4.455  26.138  1.00 7.60  ? 249 GLN   A CB  1 
ATOM   1999 C  CG  . GLN   A 1 248 ? 0.917   -4.420  24.637  1.00 7.58  ? 249 GLN   A CG  1 
ATOM   2000 C  CD  . GLN   A 1 248 ? 2.243   -5.058  24.285  1.00 8.41  ? 249 GLN   A CD  1 
ATOM   2001 O  OE1 . GLN   A 1 248 ? 3.272   -4.668  24.839  1.00 9.92  ? 249 GLN   A OE1 1 
ATOM   2002 N  NE2 . GLN   A 1 248 ? 2.223   -6.004  23.371  1.00 8.85  ? 249 GLN   A NE2 1 
ATOM   2003 N  N   . PRO   A 1 249 ? 1.321   -5.529  28.998  1.00 8.06  ? 250 PRO   A N   1 
ATOM   2004 C  CA  . PRO   A 1 249 ? 1.128   -5.537  30.438  1.00 8.85  ? 250 PRO   A CA  1 
ATOM   2005 C  C   . PRO   A 1 249 ? 0.040   -4.577  30.880  1.00 8.04  ? 250 PRO   A C   1 
ATOM   2006 O  O   . PRO   A 1 249 ? 0.039   -3.424  30.492  1.00 7.87  ? 250 PRO   A O   1 
ATOM   2007 C  CB  . PRO   A 1 249 ? 2.511   -5.152  30.998  1.00 10.45 ? 250 PRO   A CB  1 
ATOM   2008 C  CG  . PRO   A 1 249 ? 3.484   -5.608  29.905  1.00 10.79 ? 250 PRO   A CG  1 
ATOM   2009 C  CD  . PRO   A 1 249 ? 2.739   -5.277  28.637  1.00 9.29  ? 250 PRO   A CD  1 
ATOM   2010 N  N   . LEU   A 1 250 ? -0.810  -5.038  31.787  1.00 8.89  ? 251 LEU   A N   1 
ATOM   2011 C  CA  . LEU   A 1 250 ? -1.882  -4.199  32.287  1.00 8.89  ? 251 LEU   A CA  1 
ATOM   2012 C  C   . LEU   A 1 250 ? -1.394  -3.069  33.180  1.00 8.12  ? 251 LEU   A C   1 
ATOM   2013 O  O   . LEU   A 1 250 ? -1.998  -2.000  33.237  1.00 8.24  ? 251 LEU   A O   1 
ATOM   2014 C  CB  . LEU   A 1 250 ? -2.906  -5.053  33.043  1.00 10.31 ? 251 LEU   A CB  1 
ATOM   2015 C  CG  . LEU   A 1 250 ? -4.205  -4.361  33.464  1.00 11.21 ? 251 LEU   A CG  1 
ATOM   2016 C  CD1 . LEU   A 1 250 ? -4.966  -3.872  32.246  1.00 10.73 ? 251 LEU   A CD1 1 
ATOM   2017 C  CD2 . LEU   A 1 250 ? -5.079  -5.310  34.261  1.00 13.26 ? 251 LEU   A CD2 1 
ATOM   2018 N  N   . LYS   A 1 251 ? -0.286  -3.292  33.898  1.00 9.43  ? 252 LYS   A N   1 
ATOM   2019 C  CA  . LYS   A 1 251 ? 0.308   -2.268  34.756  1.00 11.11 ? 252 LYS   A CA  1 
ATOM   2020 C  C   . LYS   A 1 251 ? -0.744  -1.780  35.755  1.00 11.88 ? 252 LYS   A C   1 
ATOM   2021 O  O   . LYS   A 1 251 ? -1.501  -2.592  36.270  1.00 14.05 ? 252 LYS   A O   1 
ATOM   2022 C  CB  . LYS   A 1 251 ? 0.984   -1.151  33.948  1.00 12.87 ? 252 LYS   A CB  1 
ATOM   2023 C  CG  . LYS   A 1 251 ? 2.065   -1.737  33.054  1.00 15.70 ? 252 LYS   A CG  1 
ATOM   2024 C  CD  . LYS   A 1 251 ? 3.214   -0.885  32.581  1.00 19.39 ? 252 LYS   A CD  1 
ATOM   2025 C  CE  . LYS   A 1 251 ? 4.389   -1.732  32.248  1.00 20.37 ? 252 LYS   A CE  1 
ATOM   2026 N  NZ  . LYS   A 1 251 ? 5.202   -1.013  31.266  1.00 24.07 ? 252 LYS   A NZ  1 
ATOM   2027 N  N   . ASN   A 1 252 ? -0.790  -0.482  35.999  1.00 12.87 ? 253 ASN   A N   1 
ATOM   2028 C  CA  . ASN   A 1 252 ? -1.649  0.026   37.051  1.00 15.92 ? 253 ASN   A CA  1 
ATOM   2029 C  C   . ASN   A 1 252 ? -2.994  0.411   36.437  1.00 15.31 ? 253 ASN   A C   1 
ATOM   2030 O  O   . ASN   A 1 252 ? -3.310  1.633   36.462  1.00 19.36 ? 253 ASN   A O   1 
ATOM   2031 C  CB  . ASN   A 1 252 ? -0.973  1.215   37.719  1.00 19.24 ? 253 ASN   A CB  1 
ATOM   2032 C  CG  . ASN   A 1 252 ? -1.788  1.814   38.832  1.00 22.69 ? 253 ASN   A CG  1 
ATOM   2033 O  OD1 . ASN   A 1 252 ? -2.327  1.069   39.658  1.00 27.96 ? 253 ASN   A OD1 1 
ATOM   2034 N  ND2 . ASN   A 1 252 ? -1.864  3.140   38.891  1.00 25.19 ? 253 ASN   A ND2 1 
ATOM   2035 N  N   . ARG   A 1 253 ? -3.698  -0.578  35.785  1.00 10.95 ? 254 ARG   A N   1 
ATOM   2036 C  CA  . ARG   A 1 253 ? -5.018  -0.302  35.269  1.00 8.81  ? 254 ARG   A CA  1 
ATOM   2037 C  C   . ARG   A 1 253 ? -6.072  -1.256  35.765  1.00 9.53  ? 254 ARG   A C   1 
ATOM   2038 O  O   . ARG   A 1 253 ? -5.793  -2.363  36.127  1.00 12.97 ? 254 ARG   A O   1 
ATOM   2039 C  CB  . ARG   A 1 253 ? -4.936  -0.294  33.749  1.00 8.17  ? 254 ARG   A CB  1 
ATOM   2040 C  CG  . ARG   A 1 253 ? -4.063  0.838   33.239  1.00 8.04  ? 254 ARG   A CG  1 
ATOM   2041 C  CD  . ARG   A 1 253 ? -3.911  0.833   31.727  1.00 7.86  ? 254 ARG   A CD  1 
ATOM   2042 N  NE  . ARG   A 1 253 ? -3.108  -0.302  31.289  1.00 6.55  ? 254 ARG   A NE  1 
ATOM   2043 C  CZ  . ARG   A 1 253 ? -2.836  -0.569  30.019  1.00 5.89  ? 254 ARG   A CZ  1 
ATOM   2044 N  NH1 . ARG   A 1 253 ? -3.425  0.104   29.043  1.00 5.57  ? 254 ARG   A NH1 1 
ATOM   2045 N  NH2 . ARG   A 1 253 ? -2.002  -1.554  29.703  1.00 6.13  ? 254 ARG   A NH2 1 
ATOM   2046 N  N   . GLN   A 1 254 ? -7.300  -0.754  35.756  1.00 10.00 ? 255 GLN   A N   1 
ATOM   2047 C  CA  . GLN   A 1 254 ? -8.465  -1.556  36.069  1.00 11.02 ? 255 GLN   A CA  1 
ATOM   2048 C  C   . GLN   A 1 254 ? -9.370  -1.551  34.838  1.00 9.73  ? 255 GLN   A C   1 
ATOM   2049 O  O   . GLN   A 1 254 ? -9.548  -0.539  34.138  1.00 12.83 ? 255 GLN   A O   1 
ATOM   2050 C  CB  . GLN   A 1 254 ? -9.202  -1.188  37.347  1.00 13.01 ? 255 GLN   A CB  1 
ATOM   2051 C  CG  . GLN   A 1 254 ? -8.423  -1.488  38.624  1.00 14.61 ? 255 GLN   A CG  1 
ATOM   2052 C  CD  . GLN   A 1 254 ? -9.164  -1.057  39.872  1.00 14.26 ? 255 GLN   A CD  1 
ATOM   2053 O  OE1 . GLN   A 1 254 ? -9.824  -0.003  39.872  1.00 16.88 ? 255 GLN   A OE1 1 
ATOM   2054 N  NE2 . GLN   A 1 254 ? -9.080  -1.860  40.929  1.00 15.83 ? 255 GLN   A NE2 1 
ATOM   2055 N  N   . ILE   A 1 255 ? -9.884  -2.719  34.531  1.00 7.54  ? 256 ILE   A N   1 
ATOM   2056 C  CA  . ILE   A 1 255 ? -10.860 -2.867  33.493  1.00 6.99  ? 256 ILE   A CA  1 
ATOM   2057 C  C   . ILE   A 1 255 ? -12.246 -2.895  34.151  1.00 7.03  ? 256 ILE   A C   1 
ATOM   2058 O  O   . ILE   A 1 255 ? -12.467 -3.634  35.132  1.00 8.02  ? 256 ILE   A O   1 
ATOM   2059 C  CB  . ILE   A 1 255 ? -10.622 -4.135  32.678  1.00 7.61  ? 256 ILE   A CB  1 
ATOM   2060 C  CG1 . ILE   A 1 255 ? -9.177  -4.107  32.118  1.00 8.78  ? 256 ILE   A CG1 1 
ATOM   2061 C  CG2 . ILE   A 1 255 ? -11.655 -4.299  31.591  1.00 8.25  ? 256 ILE   A CG2 1 
ATOM   2062 C  CD1 . ILE   A 1 255 ? -8.783  -5.315  31.276  1.00 10.18 ? 256 ILE   A CD1 1 
ATOM   2063 N  N   . LYS   A 1 256 ? -13.150 -2.057  33.656  1.00 6.53  ? 257 LYS   A N   1 
ATOM   2064 C  CA  . LYS   A 1 256 ? -14.497 -1.992  34.195  1.00 7.17  ? 257 LYS   A CA  1 
ATOM   2065 C  C   . LYS   A 1 256 ? -15.475 -2.599  33.222  1.00 6.75  ? 257 LYS   A C   1 
ATOM   2066 O  O   . LYS   A 1 256 ? -15.316 -2.493  32.010  1.00 7.84  ? 257 LYS   A O   1 
ATOM   2067 C  CB  . LYS   A 1 256 ? -14.888 -0.531  34.433  1.00 8.46  ? 257 LYS   A CB  1 
ATOM   2068 C  CG  . LYS   A 1 256 ? -13.990 0.119   35.474  1.00 11.15 ? 257 LYS   A CG  1 
ATOM   2069 C  CD  . LYS   A 1 256 ? -14.011 -0.539  36.852  1.00 13.98 ? 257 LYS   A CD  1 
ATOM   2070 C  CE  . LYS   A 1 256 ? -13.399 0.251   37.972  1.00 16.16 ? 257 LYS   A CE  1 
ATOM   2071 N  NZ  . LYS   A 1 256 ? -13.596 -0.435  39.249  1.00 18.07 ? 257 LYS   A NZ  1 
ATOM   2072 N  N   . ALA   A 1 257 ? -16.507 -3.248  33.758  1.00 7.39  ? 258 ALA   A N   1 
ATOM   2073 C  CA  . ALA   A 1 257 ? -17.577 -3.835  32.969  1.00 7.09  ? 258 ALA   A CA  1 
ATOM   2074 C  C   . ALA   A 1 257 ? -18.832 -2.952  33.066  1.00 6.74  ? 258 ALA   A C   1 
ATOM   2075 O  O   . ALA   A 1 257 ? -19.173 -2.417  34.124  1.00 7.61  ? 258 ALA   A O   1 
ATOM   2076 C  CB  . ALA   A 1 257 ? -17.915 -5.218  33.491  1.00 8.04  ? 258 ALA   A CB  1 
ATOM   2077 N  N   . SER   A 1 258 ? -19.555 -2.882  31.959  1.00 6.86  ? 259 SER   A N   1 
ATOM   2078 C  CA  . SER   A 1 258 ? -20.799 -2.129  31.906  1.00 7.50  ? 259 SER   A CA  1 
ATOM   2079 C  C   . SER   A 1 258 ? -22.003 -2.917  32.410  1.00 8.52  ? 259 SER   A C   1 
ATOM   2080 O  O   . SER   A 1 258 ? -23.100 -2.359  32.467  1.00 10.20 ? 259 SER   A O   1 
ATOM   2081 C  CB  . SER   A 1 258 ? -21.089 -1.681  30.496  1.00 7.62  ? 259 SER   A CB  1 
ATOM   2082 O  OG  . SER   A 1 258 ? -21.520 -2.775  29.703  1.00 7.44  ? 259 SER   A OG  1 
ATOM   2083 N  N   . PHE   A 1 259 ? -21.798 -4.189  32.685  1.00 8.82  ? 260 PHE   A N   1 
ATOM   2084 C  CA  . PHE   A 1 259 ? -22.862 -5.165  32.887  1.00 10.94 ? 260 PHE   A CA  1 
ATOM   2085 C  C   . PHE   A 1 259 ? -22.550 -5.969  34.135  1.00 14.04 ? 260 PHE   A C   1 
ATOM   2086 O  O   . PHE   A 1 259 ? -21.402 -6.091  34.553  1.00 14.69 ? 260 PHE   A O   1 
ATOM   2087 C  CB  . PHE   A 1 259 ? -23.019 -6.102  31.678  1.00 12.19 ? 260 PHE   A CB  1 
ATOM   2088 C  CG  . PHE   A 1 259 ? -21.743 -6.853  31.352  1.00 12.15 ? 260 PHE   A CG  1 
ATOM   2089 C  CD1 . PHE   A 1 259 ? -20.750 -6.249  30.586  1.00 10.48 ? 260 PHE   A CD1 1 
ATOM   2090 C  CD2 . PHE   A 1 259 ? -21.493 -8.103  31.887  1.00 14.44 ? 260 PHE   A CD2 1 
ATOM   2091 C  CE1 . PHE   A 1 259 ? -19.555 -6.908  30.348  1.00 11.27 ? 260 PHE   A CE1 1 
ATOM   2092 C  CE2 . PHE   A 1 259 ? -20.306 -8.748  31.637  1.00 15.45 ? 260 PHE   A CE2 1 
ATOM   2093 C  CZ  . PHE   A 1 259 ? -19.338 -8.148  30.887  1.00 13.05 ? 260 PHE   A CZ  1 
ATOM   2094 N  N   . LYS   A 1 260 ? -23.645 -6.469  34.722  1.00 18.13 ? 261 LYS   A N   1 
ATOM   2095 C  CA  . LYS   A 1 260 ? -23.673 -7.585  35.665  1.00 23.45 ? 261 LYS   A CA  1 
ATOM   2096 C  C   . LYS   A 1 260 ? -22.671 -7.409  36.810  1.00 28.47 ? 261 LYS   A C   1 
ATOM   2097 O  O   . LYS   A 1 260 ? -22.663 -8.335  37.654  1.00 34.83 ? 261 LYS   A O   1 
ATOM   2098 C  CB  . LYS   A 1 260 ? -23.488 -8.976  35.030  1.00 24.82 ? 261 LYS   A CB  1 
ATOM   2099 C  CG  . LYS   A 1 260 ? -24.565 -9.304  33.993  1.00 32.63 ? 261 LYS   A CG  1 
ATOM   2100 C  CD  . LYS   A 1 260 ? -24.780 -10.783 33.670  1.00 37.42 ? 261 LYS   A CD  1 
ATOM   2101 C  CE  . LYS   A 1 260 ? -26.041 -11.041 32.874  1.00 41.75 ? 261 LYS   A CE  1 
ATOM   2102 N  NZ  . LYS   A 1 260 ? -26.172 -12.443 32.453  1.00 44.27 ? 261 LYS   A NZ  1 
HETATM 2103 ZN ZN  . ZN    B 2 .   ? -6.725  -1.096  15.290  1.00 5.16  ? 301 ZN    A ZN  1 
HETATM 2104 C  C2  . A1IKU C 3 .   ? -3.913  2.655   15.311  1.00 12.95 ? 302 A1IKU A C2  1 
HETATM 2105 C  C4  . A1IKU C 3 .   ? -4.211  4.878   14.335  1.00 13.86 ? 302 A1IKU A C4  1 
HETATM 2106 C  C5  . A1IKU C 3 .   ? -5.559  4.745   14.647  1.00 13.93 ? 302 A1IKU A C5  1 
HETATM 2107 C  C6  . A1IKU C 3 .   ? -6.070  3.607   15.291  1.00 12.96 ? 302 A1IKU A C6  1 
HETATM 2108 C  C1  . A1IKU C 3 .   ? -5.278  2.473   15.637  1.00 12.79 ? 302 A1IKU A C1  1 
HETATM 2109 C  C3  . A1IKU C 3 .   ? -3.410  3.798   14.686  1.00 13.63 ? 302 A1IKU A C3  1 
HETATM 2110 C  C7  . A1IKU C 3 .   ? -3.608  6.103   13.664  1.00 17.00 ? 302 A1IKU A C7  1 
HETATM 2111 B  B1  . A1IKU C 3 .   ? -5.813  1.130   16.406  1.00 9.91  ? 302 A1IKU A B1  1 
HETATM 2112 O  O1  . A1IKU C 3 .   ? -5.266  -0.086  15.987  1.00 8.10  ? 302 A1IKU A O1  1 
HETATM 2113 O  O2  . A1IKU C 3 .   ? -5.431  1.333   17.888  1.00 10.24 ? 302 A1IKU A O2  1 
HETATM 2114 O  O3  . A1IKU C 3 .   ? -7.242  1.032   16.331  1.00 10.85 ? 302 A1IKU A O3  1 
HETATM 2115 C  C1  . GOL   D 4 .   ? -4.370  2.610   11.186  1.00 14.49 ? 303 GOL   A C1  1 
HETATM 2116 O  O1  . GOL   D 4 .   ? -5.195  3.662   10.674  1.00 15.96 ? 303 GOL   A O1  1 
HETATM 2117 C  C2  . GOL   D 4 .   ? -5.040  1.260   11.005  1.00 13.69 ? 303 GOL   A C2  1 
HETATM 2118 O  O2  . GOL   D 4 .   ? -5.165  0.991   9.629   1.00 11.80 ? 303 GOL   A O2  1 
HETATM 2119 C  C3  . GOL   D 4 .   ? -4.321  0.073   11.639  1.00 13.69 ? 303 GOL   A C3  1 
HETATM 2120 O  O3  . GOL   D 4 .   ? -3.049  -0.107  11.028  1.00 13.68 ? 303 GOL   A O3  1 
HETATM 2121 S  S   . DMS   E 5 .   ? 1.213   -11.229 15.066  1.00 18.86 ? 304 DMS   A S   1 
HETATM 2122 O  O   . DMS   E 5 .   ? 1.460   -10.971 16.581  1.00 18.08 ? 304 DMS   A O   1 
HETATM 2123 C  C1  . DMS   E 5 .   ? 2.368   -10.177 14.320  1.00 19.45 ? 304 DMS   A C1  1 
HETATM 2124 C  C2  . DMS   E 5 .   ? 1.937   -12.759 14.656  1.00 21.24 ? 304 DMS   A C2  1 
HETATM 2125 HG HG  . MBO   F 6 .   ? -2.116  10.958  24.576  0.50 6.38  ? 305 MBO   A HG  1 
HETATM 2126 C  CE1 . MBO   F 6 .   ? -1.354  11.692  26.394  0.50 8.18  ? 305 MBO   A CE1 1 
HETATM 2127 C  CE2 . MBO   F 6 .   ? -1.273  10.820  27.479  0.50 8.03  ? 305 MBO   A CE2 1 
HETATM 2128 C  CE3 . MBO   F 6 .   ? -0.844  11.249  28.730  0.50 8.76  ? 305 MBO   A CE3 1 
HETATM 2129 C  CE4 . MBO   F 6 .   ? -0.377  12.530  28.885  0.50 9.62  ? 305 MBO   A CE4 1 
HETATM 2130 C  CE5 . MBO   F 6 .   ? -0.417  13.408  27.821  0.50 9.32  ? 305 MBO   A CE5 1 
HETATM 2131 C  CE6 . MBO   F 6 .   ? -0.848  12.978  26.569  0.50 9.28  ? 305 MBO   A CE6 1 
HETATM 2132 C  CZ  . MBO   F 6 .   ? 0.114   13.010  30.223  0.50 10.85 ? 305 MBO   A CZ  1 
HETATM 2133 O  OZ1 . MBO   F 6 .   ? 0.047   12.245  31.175  0.50 12.61 ? 305 MBO   A OZ1 1 
HETATM 2134 O  OZ2 . MBO   F 6 .   ? 0.609   14.117  30.261  0.50 10.35 ? 305 MBO   A OZ2 1 
HETATM 2135 O  O   . HOH   G 7 .   ? -24.208 12.675  6.164   1.00 27.42 ? 401 HOH   A O   1 
HETATM 2136 O  O   . HOH   G 7 .   ? -11.021 -14.583 34.229  1.00 18.17 ? 402 HOH   A O   1 
HETATM 2137 O  O   . HOH   G 7 .   ? 4.550   -1.990  29.093  1.00 18.35 ? 403 HOH   A O   1 
HETATM 2138 O  O   . HOH   G 7 .   ? -5.256  2.935   37.407  1.00 25.05 ? 404 HOH   A O   1 
HETATM 2139 O  O   . HOH   G 7 .   ? -12.533 13.135  29.319  1.00 20.68 ? 405 HOH   A O   1 
HETATM 2140 O  O   . HOH   G 7 .   ? -13.086 13.977  31.884  1.00 17.47 ? 406 HOH   A O   1 
HETATM 2141 O  O   . HOH   G 7 .   ? -6.201  -10.979 36.551  1.00 31.45 ? 407 HOH   A O   1 
HETATM 2142 O  O   . HOH   G 7 .   ? 4.624   -0.554  -5.337  1.00 26.74 ? 408 HOH   A O   1 
HETATM 2143 O  O   . HOH   G 7 .   ? -24.217 9.289   20.320  1.00 16.66 ? 409 HOH   A O   1 
HETATM 2144 O  O   . HOH   G 7 .   ? -10.593 16.520  29.424  1.00 17.37 ? 410 HOH   A O   1 
HETATM 2145 O  O   . HOH   G 7 .   ? -21.200 8.420   1.989   1.00 15.99 ? 411 HOH   A O   1 
HETATM 2146 O  O   . HOH   G 7 .   ? -9.307  6.499   29.020  1.00 13.62 ? 412 HOH   A O   1 
HETATM 2147 O  O   . HOH   G 7 .   ? -25.824 -4.819  13.259  1.00 26.87 ? 413 HOH   A O   1 
HETATM 2148 O  O   . HOH   G 7 .   ? -8.808  -3.297  7.941   1.00 6.45  ? 414 HOH   A O   1 
HETATM 2149 O  O   . HOH   G 7 .   ? -20.580 9.114   30.109  1.00 18.09 ? 415 HOH   A O   1 
HETATM 2150 O  O   . HOH   G 7 .   ? -6.983  6.474   6.429   1.00 15.80 ? 416 HOH   A O   1 
HETATM 2151 O  O   . HOH   G 7 .   ? -1.322  -3.666  15.718  1.00 7.29  ? 417 HOH   A O   1 
HETATM 2152 O  O   . HOH   G 7 .   ? -15.570 1.387   -4.952  1.00 24.55 ? 418 HOH   A O   1 
HETATM 2153 O  O   . HOH   G 7 .   ? -22.518 1.893   30.183  1.00 11.32 ? 419 HOH   A O   1 
HETATM 2154 O  O   . HOH   G 7 .   ? -11.249 -4.524  37.812  1.00 20.84 ? 420 HOH   A O   1 
HETATM 2155 O  O   . HOH   G 7 .   ? 4.252   -2.864  26.502  1.00 14.11 ? 421 HOH   A O   1 
HETATM 2156 O  O   . HOH   G 7 .   ? 9.908   2.219   12.612  1.00 26.03 ? 422 HOH   A O   1 
HETATM 2157 O  O   . HOH   G 7 .   ? -20.359 11.388  26.746  1.00 12.79 ? 423 HOH   A O   1 
HETATM 2158 O  O   . HOH   G 7 .   ? 6.964   -2.712  30.243  1.00 25.90 ? 424 HOH   A O   1 
HETATM 2159 O  O   . HOH   G 7 .   ? 3.469   5.602   29.705  1.00 14.10 ? 425 HOH   A O   1 
HETATM 2160 O  O   . HOH   G 7 .   ? -14.485 -15.957 29.090  1.00 17.14 ? 426 HOH   A O   1 
HETATM 2161 O  O   . HOH   G 7 .   ? -16.428 5.812   -7.837  1.00 23.85 ? 427 HOH   A O   1 
HETATM 2162 O  O   . HOH   G 7 .   ? -15.906 -9.957  37.628  1.00 19.58 ? 428 HOH   A O   1 
HETATM 2163 O  O   . HOH   G 7 .   ? -3.493  5.563   9.902   1.00 22.73 ? 429 HOH   A O   1 
HETATM 2164 O  O   . HOH   G 7 .   ? 5.710   -5.438  24.084  1.00 25.41 ? 430 HOH   A O   1 
HETATM 2165 O  O   . HOH   G 7 .   ? -24.173 -2.855  29.361  1.00 16.99 ? 431 HOH   A O   1 
HETATM 2166 O  O   . HOH   G 7 .   ? -22.848 -5.306  2.916   1.00 24.94 ? 432 HOH   A O   1 
HETATM 2167 O  O   . HOH   G 7 .   ? -13.945 14.843  27.308  1.00 18.77 ? 433 HOH   A O   1 
HETATM 2168 O  O   . HOH   G 7 .   ? -0.019  -0.516  -4.715  1.00 11.75 ? 434 HOH   A O   1 
HETATM 2169 O  O   . HOH   G 7 .   ? -27.557 -6.893  26.125  1.00 25.25 ? 435 HOH   A O   1 
HETATM 2170 O  O   . HOH   G 7 .   ? 1.790   -15.051 9.440   1.00 19.24 ? 436 HOH   A O   1 
HETATM 2171 O  O   . HOH   G 7 .   ? -0.485  15.063  16.403  1.00 23.87 ? 437 HOH   A O   1 
HETATM 2172 O  O   . HOH   G 7 .   ? 11.240  -6.349  22.512  1.00 19.42 ? 438 HOH   A O   1 
HETATM 2173 O  O   . HOH   G 7 .   ? -8.796  1.249   -6.557  1.00 23.43 ? 439 HOH   A O   1 
HETATM 2174 O  O   . HOH   G 7 .   ? -13.226 -21.770 8.660   1.00 22.15 ? 440 HOH   A O   1 
HETATM 2175 O  O   . HOH   G 7 .   ? -11.150 -19.169 7.390   1.00 20.23 ? 441 HOH   A O   1 
HETATM 2176 O  O   . HOH   G 7 .   ? -2.509  -2.733  11.379  1.00 11.06 ? 442 HOH   A O   1 
HETATM 2177 O  O   . HOH   G 7 .   ? -12.898 -22.191 12.373  1.00 24.09 ? 443 HOH   A O   1 
HETATM 2178 O  O   . HOH   G 7 .   ? -4.673  -11.459 32.248  1.00 16.31 ? 444 HOH   A O   1 
HETATM 2179 O  O   . HOH   G 7 .   ? -10.686 9.345   25.658  1.00 7.27  ? 445 HOH   A O   1 
HETATM 2180 O  O   . HOH   G 7 .   ? -2.588  -8.073  29.167  1.00 8.90  ? 446 HOH   A O   1 
HETATM 2181 O  O   . HOH   G 7 .   ? -18.059 -19.887 8.045   1.00 13.21 ? 447 HOH   A O   1 
HETATM 2182 O  O   . HOH   G 7 .   ? -7.155  -14.240 31.677  1.00 16.11 ? 448 HOH   A O   1 
HETATM 2183 O  O   . HOH   G 7 .   ? -17.725 3.561   40.290  1.00 28.65 ? 449 HOH   A O   1 
HETATM 2184 O  O   . HOH   G 7 .   ? -10.758 22.474  20.098  1.00 16.01 ? 450 HOH   A O   1 
HETATM 2185 O  O   . HOH   G 7 .   ? -1.513  24.079  18.307  1.00 27.45 ? 451 HOH   A O   1 
HETATM 2186 O  O   . HOH   G 7 .   ? -13.818 10.994  28.031  1.00 11.23 ? 452 HOH   A O   1 
HETATM 2187 O  O   . HOH   G 7 .   ? -16.210 16.545  23.611  1.00 15.66 ? 453 HOH   A O   1 
HETATM 2188 O  O   . HOH   G 7 .   ? 2.369   -12.734 5.245   1.00 19.65 ? 454 HOH   A O   1 
HETATM 2189 O  O   . HOH   G 7 .   ? 11.602  0.249   15.954  1.00 13.13 ? 455 HOH   A O   1 
HETATM 2190 O  O   . HOH   G 7 .   ? -3.589  -12.467 -2.847  1.00 19.27 ? 456 HOH   A O   1 
HETATM 2191 O  O   . HOH   G 7 .   ? -15.019 20.785  17.777  1.00 15.05 ? 457 HOH   A O   1 
HETATM 2192 O  O   . HOH   G 7 .   ? -18.064 11.324  11.383  1.00 14.96 ? 458 HOH   A O   1 
HETATM 2193 O  O   . HOH   G 7 .   ? -8.108  -14.989 11.454  1.00 8.15  ? 459 HOH   A O   1 
HETATM 2194 O  O   . HOH   G 7 .   ? -2.230  -3.986  -7.093  1.00 26.21 ? 460 HOH   A O   1 
HETATM 2195 O  O   . HOH   G 7 .   ? 8.530   -3.289  21.009  1.00 10.86 ? 461 HOH   A O   1 
HETATM 2196 O  O   . HOH   G 7 .   ? 13.721  2.692   22.706  1.00 18.07 ? 462 HOH   A O   1 
HETATM 2197 O  O   . HOH   G 7 .   ? 7.448   -7.290  -0.631  1.00 23.03 ? 463 HOH   A O   1 
HETATM 2198 O  O   . HOH   G 7 .   ? -12.237 11.316  5.595   1.00 20.69 ? 464 HOH   A O   1 
HETATM 2199 O  O   . HOH   G 7 .   ? -21.691 -6.726  23.667  1.00 9.41  ? 465 HOH   A O   1 
HETATM 2200 O  O   . HOH   G 7 .   ? 0.190   11.577  22.780  1.00 17.60 ? 466 HOH   A O   1 
HETATM 2201 O  O   . HOH   G 7 .   ? -10.532 -17.740 17.272  1.00 10.40 ? 467 HOH   A O   1 
HETATM 2202 O  O   . HOH   G 7 .   ? -12.000 -2.659  39.589  1.00 16.79 ? 468 HOH   A O   1 
HETATM 2203 O  O   . HOH   G 7 .   ? -6.290  17.266  27.588  1.00 16.45 ? 469 HOH   A O   1 
HETATM 2204 O  O   . HOH   G 7 .   ? -4.629  -13.040 18.120  1.00 7.00  ? 470 HOH   A O   1 
HETATM 2205 O  O   . HOH   G 7 .   ? -3.858  -15.260 24.495  1.00 10.35 ? 471 HOH   A O   1 
HETATM 2206 O  O   . HOH   G 7 .   ? 5.230   7.550   20.131  1.00 15.98 ? 472 HOH   A O   1 
HETATM 2207 O  O   . HOH   G 7 .   ? -17.155 -7.876  20.406  1.00 6.52  ? 473 HOH   A O   1 
HETATM 2208 O  O   . HOH   G 7 .   ? -19.967 -3.094  41.296  1.00 23.73 ? 474 HOH   A O   1 
HETATM 2209 O  O   . HOH   G 7 .   ? -15.580 9.454   -2.102  1.00 23.55 ? 475 HOH   A O   1 
HETATM 2210 O  O   . HOH   G 7 .   ? -16.150 -11.755 24.520  1.00 11.77 ? 476 HOH   A O   1 
HETATM 2211 O  O   . HOH   G 7 .   ? -18.454 -2.937  -2.531  1.00 24.64 ? 477 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 7 .   ? -16.835 -0.089  42.333  1.00 30.70 ? 478 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 7 .   ? -3.603  -10.674 20.966  1.00 7.35  ? 479 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 7 .   ? 1.172   -11.192 25.115  1.00 19.87 ? 480 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 7 .   ? -26.957 2.096   26.042  1.00 26.10 ? 481 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 7 .   ? -26.125 -5.634  33.788  1.00 29.75 ? 482 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 7 .   ? -13.777 20.708  15.165  1.00 15.41 ? 483 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 7 .   ? -26.328 4.118   15.564  1.00 21.47 ? 484 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 7 .   ? -19.337 10.585  8.993   1.00 11.67 ? 485 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 7 .   ? 13.142  0.883   24.479  1.00 16.47 ? 486 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 7 .   ? -23.341 -2.469  6.795   1.00 16.51 ? 487 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 7 .   ? -26.797 -1.874  14.566  1.00 17.08 ? 488 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 7 .   ? -7.431  -8.041  32.694  1.00 11.24 ? 489 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 7 .   ? -19.066 18.120  19.049  1.00 24.38 ? 490 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 7 .   ? -22.047 6.280   4.920   1.00 12.86 ? 491 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 7 .   ? 11.013  1.941   25.890  1.00 17.42 ? 492 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 7 .   ? -20.351 14.243  28.959  1.00 28.40 ? 493 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 7 .   ? -23.473 0.398   32.261  1.00 13.26 ? 494 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 7 .   ? -4.750  -15.628 1.249   1.00 29.37 ? 495 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 7 .   ? -12.002 9.921   3.198   1.00 17.14 ? 496 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 7 .   ? -10.553 9.000   7.908   1.00 19.00 ? 497 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 7 .   ? -22.299 -13.502 18.735  1.00 39.47 ? 498 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 7 .   ? 10.356  -10.305 16.082  1.00 17.41 ? 499 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 7 .   ? -3.490  -12.661 25.290  1.00 9.13  ? 500 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 7 .   ? -6.380  -3.946  -6.362  1.00 21.14 ? 501 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 7 .   ? -8.887  -14.885 36.823  1.00 14.88 ? 502 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 7 .   ? -4.274  -7.796  31.253  1.00 15.07 ? 503 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 7 .   ? -26.421 3.295   20.915  1.00 14.59 ? 504 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 7 .   ? -13.370 -15.652 -0.163  1.00 30.11 ? 505 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 7 .   ? -25.901 3.263   33.060  1.00 34.28 ? 506 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 7 .   ? -16.420 -15.236 32.898  1.00 24.00 ? 507 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 7 .   ? 2.411   -10.948 9.506   1.00 16.32 ? 508 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 7 .   ? -14.747 -18.122 18.842  1.00 13.07 ? 509 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 7 .   ? 4.805   -6.854  22.207  1.00 16.72 ? 510 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 7 .   ? 4.807   -4.423  20.960  1.00 10.16 ? 511 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 7 .   ? -13.150 -16.250 26.709  1.00 13.32 ? 512 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 7 .   ? -23.312 1.429   34.832  1.00 14.00 ? 513 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 7 .   ? -15.454 -21.451 13.209  1.00 14.30 ? 514 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 7 .   ? -8.134  -21.642 10.444  1.00 19.08 ? 515 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 7 .   ? -27.259 -10.324 22.418  1.00 29.59 ? 516 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 7 .   ? -23.450 -12.957 11.201  1.00 17.41 ? 517 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 7 .   ? -7.245  -16.479 1.827   1.00 19.50 ? 518 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 7 .   ? -25.256 -7.360  9.017   1.00 24.98 ? 519 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 7 .   ? -17.001 15.422  33.276  1.00 26.76 ? 520 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 7 .   ? 8.092   -8.740  16.395  1.00 17.01 ? 521 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 7 .   ? 1.402   -5.512  34.465  1.00 20.52 ? 522 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 7 .   ? -12.974 8.461   28.903  1.00 19.59 ? 523 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 7 .   ? 2.583   -3.839  7.841   1.00 18.69 ? 524 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 7 .   ? 1.112   13.266  19.882  1.00 32.26 ? 525 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 7 .   ? -22.125 -17.824 13.598  1.00 21.63 ? 526 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 7 .   ? -1.115  1.946   11.448  1.00 17.74 ? 527 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 7 .   ? -16.382 -9.376  33.209  1.00 14.97 ? 528 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 7 .   ? -1.347  5.171   -4.817  1.00 24.00 ? 529 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 7 .   ? 4.164   -6.338  7.897   1.00 19.82 ? 530 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 7 .   ? 14.071  6.248   19.397  1.00 28.13 ? 531 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 7 .   ? -12.097 3.264   30.953  1.00 12.31 ? 532 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 7 .   ? -6.907  21.829  19.697  1.00 13.71 ? 533 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 7 .   ? -25.557 -10.001 17.687  1.00 21.91 ? 534 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 7 .   ? -27.041 -3.412  25.094  1.00 15.75 ? 535 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 7 .   ? -9.210  -5.056  36.053  1.00 13.08 ? 536 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 7 .   ? -13.507 -18.038 14.722  1.00 13.41 ? 537 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 7 .   ? -13.675 -0.175  -6.208  1.00 26.80 ? 538 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 7 .   ? -23.916 -0.286  4.001   1.00 18.05 ? 539 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 7 .   ? 1.148   -0.956  29.365  1.00 9.78  ? 540 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 7 .   ? -0.561  -7.760  32.767  1.00 20.08 ? 541 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 7 .   ? 1.230   9.234   24.016  1.00 17.31 ? 542 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 7 .   ? -6.446  -18.784 5.962   1.00 26.74 ? 543 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 7 .   ? -12.809 4.177   -6.763  1.00 20.16 ? 544 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 7 .   ? -21.090 -19.371 6.689   1.00 27.67 ? 545 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 7 .   ? -16.509 -0.539  39.729  1.00 19.22 ? 546 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 7 .   ? 5.787   1.315   8.236   1.00 21.87 ? 547 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 7 .   ? -10.225 6.673   -3.958  1.00 25.07 ? 548 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 7 .   ? -2.167  -11.749 22.977  1.00 7.79  ? 549 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 7 .   ? -12.150 21.022  29.563  1.00 26.92 ? 550 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 7 .   ? -19.699 -13.109 24.443  1.00 27.59 ? 551 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 7 .   ? 7.458   6.582   21.571  1.00 13.09 ? 552 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 7 .   ? 2.833   -14.115 1.533   1.00 23.25 ? 553 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 7 .   ? -10.873 21.476  24.992  1.00 20.17 ? 554 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 7 .   ? -2.153  8.363   30.724  1.00 18.28 ? 555 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 7 .   ? -11.223 1.871   33.510  1.00 16.33 ? 556 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 7 .   ? -18.591 20.717  14.743  1.00 18.47 ? 557 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 7 .   ? -7.184  2.162   35.016  1.00 17.06 ? 558 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 7 .   ? -10.052 15.380  12.189  1.00 17.31 ? 559 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 7 .   ? -23.984 -0.962  27.398  1.00 28.97 ? 560 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 7 .   ? -9.607  -7.285  34.278  1.00 14.30 ? 561 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 7 .   ? -0.420  -13.732 22.247  1.00 15.77 ? 562 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 7 .   ? -23.141 -11.175 14.037  1.00 23.56 ? 563 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 7 .   ? -3.973  5.201   7.096   1.00 22.89 ? 564 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 7 .   ? -17.409 -7.951  35.341  1.00 26.51 ? 565 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 7 .   ? 14.081  0.455   14.787  1.00 20.23 ? 566 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 7 .   ? -18.612 20.421  5.644   1.00 29.38 ? 567 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 7 .   ? -24.701 -9.112  1.833   1.00 25.36 ? 568 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 7 .   ? -18.084 -11.474 31.602  1.00 24.49 ? 569 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 7 .   ? 8.904   -4.292  23.492  1.00 22.21 ? 570 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 7 .   ? -13.027 -16.697 17.014  1.00 9.87  ? 571 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 7 .   ? -22.727 -9.064  25.422  1.00 19.22 ? 572 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 7 .   ? -25.370 11.841  19.730  1.00 26.11 ? 573 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 7 .   ? -17.842 20.492  17.524  1.00 20.44 ? 574 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 7 .   ? -8.214  22.655  21.819  1.00 16.22 ? 575 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 7 .   ? -29.145 -5.346  24.409  1.00 18.40 ? 576 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 7 .   ? -7.074  -16.824 32.343  1.00 24.88 ? 577 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 7 .   ? 2.786   -13.115 8.049   1.00 24.76 ? 578 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 7 .   ? -1.905  -16.724 25.651  1.00 21.95 ? 579 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 7 .   ? 9.577   0.479   14.175  1.00 21.11 ? 580 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 7 .   ? -1.466  -12.383 27.162  1.00 20.52 ? 581 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 7 .   ? -16.996 -17.293 20.168  1.00 23.88 ? 582 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 7 .   ? 6.340   -4.602  27.475  1.00 29.05 ? 583 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 7 .   ? -17.068 -13.465 26.369  1.00 19.60 ? 584 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 7 .   ? -5.051  -9.094  33.635  1.00 22.07 ? 585 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 7 .   ? -10.864 5.608   31.011  1.00 16.91 ? 586 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 7 .   ? -25.970 -2.792  6.866   1.00 37.00 ? 587 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 7 .   ? -11.410 1.658   -7.705  1.00 30.36 ? 588 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 7 .   ? -1.007  4.359   10.243  1.00 29.76 ? 589 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 7 .   ? -8.345  8.151   8.318   1.00 25.17 ? 590 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 7 .   ? -11.606 11.248  0.810   1.00 23.52 ? 591 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 7 .   ? -9.433  3.757   34.795  1.00 16.75 ? 592 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 7 .   ? -1.285  -10.499 29.079  1.00 16.68 ? 593 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 7 .   ? -11.190 16.055  32.282  1.00 14.38 ? 594 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 7 .   ? -12.319 13.976  4.768   1.00 25.52 ? 595 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 7 .   ? 6.149   6.109   29.230  1.00 34.02 ? 596 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 7 .   ? -16.718 -14.241 28.811  1.00 26.59 ? 597 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 7 .   ? -5.810  -17.645 3.632   1.00 27.48 ? 598 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 7 .   ? -29.491 -2.892  13.168  1.00 25.53 ? 599 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 7 .   ? 4.053   9.006   22.776  1.00 26.78 ? 600 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 7 .   ? -12.985 -18.944 26.118  1.00 23.72 ? 601 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 7 .   ? 1.684   -13.610 20.604  1.00 21.34 ? 602 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 7 .   ? -27.212 -0.739  26.069  1.00 26.71 ? 603 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 7 .   ? -13.884 4.575   33.131  1.00 29.12 ? 604 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 7 .   ? 4.435   -5.095  34.136  1.00 33.69 ? 605 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 7 .   ? -7.361  -24.028 10.573  1.00 25.00 ? 606 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 7 .   ? -14.681 -20.040 27.879  1.00 28.16 ? 607 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 7 .   ? -12.081 14.037  1.833   1.00 30.69 ? 608 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 7 .   ? -32.302 -2.171  13.689  1.00 15.76 ? 609 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS   A 3   ? 0.2352 0.2285 0.3466 0.0583  0.0026  0.0765  3   HIS   A N   
2    C  CA  . HIS   A 3   ? 0.2275 0.2267 0.3155 0.0497  0.0030  0.0714  3   HIS   A CA  
3    C  C   . HIS   A 3   ? 0.2216 0.2662 0.3010 0.0358  -0.0145 0.0771  3   HIS   A C   
4    O  O   . HIS   A 3   ? 0.2367 0.3138 0.3297 0.0396  -0.0289 0.0902  3   HIS   A O   
5    C  CB  . HIS   A 3   ? 0.1589 0.2324 0.3297 0.0103  0.0158  0.0430  3   HIS   A CB  
6    C  CG  . HIS   A 3   ? 0.2104 0.2409 0.3346 0.0042  0.0325  0.0340  3   HIS   A CG  
7    N  ND1 . HIS   A 3   ? 0.2427 0.2746 0.3194 0.0046  0.0315  0.0345  3   HIS   A ND1 
8    C  CD2 . HIS   A 3   ? 0.2389 0.2460 0.3437 0.0174  0.0417  0.0293  3   HIS   A CD2 
9    C  CE1 . HIS   A 3   ? 0.2569 0.2777 0.3602 -0.0048 0.0255  0.0178  3   HIS   A CE1 
10   N  NE2 . HIS   A 3   ? 0.2976 0.2869 0.3793 -0.0098 0.0164  0.0268  3   HIS   A NE2 
11   N  N   . HIS   A 4   ? 0.1860 0.2421 0.2728 0.0074  0.0261  0.0737  4   HIS   A N   
12   C  CA  . HIS   A 4   ? 0.1494 0.2374 0.2568 -0.0027 0.0424  0.0898  4   HIS   A CA  
13   C  C   . HIS   A 4   ? 0.1454 0.2195 0.2428 -0.0066 0.0643  0.0696  4   HIS   A C   
14   O  O   . HIS   A 4   ? 0.2276 0.2524 0.2983 0.0170  0.0967  0.0593  4   HIS   A O   
15   C  CB  . HIS   A 4   ? 0.1883 0.3185 0.2730 -0.0081 0.0610  0.0925  4   HIS   A CB  
16   C  CG  . HIS   A 4   ? 0.2181 0.3739 0.3402 -0.0330 0.0414  0.1534  4   HIS   A CG  
17   N  ND1 . HIS   A 4   ? 0.3698 0.4184 0.3674 -0.0282 0.0125  0.2155  4   HIS   A ND1 
18   C  CD2 . HIS   A 4   ? 0.2697 0.4068 0.3931 -0.0598 0.0402  0.1712  4   HIS   A CD2 
19   C  CE1 . HIS   A 4   ? 0.3246 0.4965 0.4412 -0.0869 0.0210  0.1870  4   HIS   A CE1 
20   N  NE2 . HIS   A 4   ? 0.3582 0.4664 0.4010 -0.0768 0.0370  0.1918  4   HIS   A NE2 
21   N  N   . TRP   A 5   ? 0.1620 0.1759 0.2298 -0.0018 0.0730  0.0508  5   TRP   A N   
22   C  CA  . TRP   A 5   ? 0.1212 0.1541 0.1901 -0.0127 0.0491  0.0224  5   TRP   A CA  
23   C  C   . TRP   A 5   ? 0.1119 0.1657 0.1454 0.0050  0.0366  0.0182  5   TRP   A C   
24   O  O   . TRP   A 5   ? 0.1445 0.1984 0.1474 0.0160  0.0336  0.0293  5   TRP   A O   
25   C  CB  . TRP   A 5   ? 0.1256 0.1455 0.1760 -0.0173 0.0370  0.0208  5   TRP   A CB  
26   C  CG  . TRP   A 5   ? 0.1341 0.1469 0.1291 -0.0095 0.0370  0.0152  5   TRP   A CG  
27   C  CD1 . TRP   A 5   ? 0.1630 0.1617 0.1502 0.0021  0.0404  0.0223  5   TRP   A CD1 
28   C  CD2 . TRP   A 5   ? 0.1233 0.1453 0.0976 0.0086  0.0187  0.0041  5   TRP   A CD2 
29   N  NE1 . TRP   A 5   ? 0.1798 0.1569 0.1320 0.0130  0.0276  0.0197  5   TRP   A NE1 
30   C  CE2 . TRP   A 5   ? 0.1409 0.1557 0.0951 0.0227  0.0285  0.0015  5   TRP   A CE2 
31   C  CE3 . TRP   A 5   ? 0.1158 0.1482 0.0872 0.0097  0.0036  -0.0207 5   TRP   A CE3 
32   C  CZ2 . TRP   A 5   ? 0.1509 0.1876 0.0700 0.0292  0.0045  -0.0066 5   TRP   A CZ2 
33   C  CZ3 . TRP   A 5   ? 0.1271 0.1668 0.0978 0.0016  -0.0003 -0.0334 5   TRP   A CZ3 
34   C  CH2 . TRP   A 5   ? 0.1388 0.1867 0.0853 0.0084  -0.0157 -0.0324 5   TRP   A CH2 
35   N  N   . GLY   A 6   ? 0.1113 0.1471 0.1191 0.0108  0.0323  0.0058  6   GLY   A N   
36   C  CA  . GLY   A 6   ? 0.1066 0.1638 0.1180 0.0047  0.0229  -0.0047 6   GLY   A CA  
37   C  C   . GLY   A 6   ? 0.0878 0.1395 0.1119 0.0049  0.0182  -0.0136 6   GLY   A C   
38   O  O   . GLY   A 6   ? 0.0935 0.1377 0.1106 0.0006  0.0140  -0.0147 6   GLY   A O   
39   N  N   . TYR   A 7   ? 0.0918 0.1499 0.1329 -0.0030 0.0309  -0.0339 7   TYR   A N   
40   C  CA  . TYR   A 7   ? 0.1009 0.1417 0.1679 -0.0015 0.0318  -0.0259 7   TYR   A CA  
41   C  C   . TYR   A 7   ? 0.1283 0.1422 0.2448 -0.0018 0.0406  -0.0232 7   TYR   A C   
42   O  O   . TYR   A 7   ? 0.1409 0.1795 0.3422 0.0087  0.0611  0.0062  7   TYR   A O   
43   C  CB  . TYR   A 7   ? 0.0928 0.1375 0.1503 -0.0099 0.0260  -0.0342 7   TYR   A CB  
44   C  CG  . TYR   A 7   ? 0.0815 0.1141 0.1063 -0.0127 0.0079  -0.0320 7   TYR   A CG  
45   C  CD1 . TYR   A 7   ? 0.0714 0.1087 0.0956 -0.0135 -0.0010 -0.0180 7   TYR   A CD1 
46   C  CD2 . TYR   A 7   ? 0.0967 0.1317 0.0954 -0.0251 0.0077  -0.0243 7   TYR   A CD2 
47   C  CE1 . TYR   A 7   ? 0.0758 0.1024 0.0856 -0.0145 -0.0051 -0.0140 7   TYR   A CE1 
48   C  CE2 . TYR   A 7   ? 0.0910 0.1196 0.0823 -0.0194 0.0072  -0.0073 7   TYR   A CE2 
49   C  CZ  . TYR   A 7   ? 0.0896 0.0944 0.0786 -0.0170 -0.0036 -0.0168 7   TYR   A CZ  
50   O  OH  . TYR   A 7   ? 0.0977 0.0999 0.0784 -0.0067 0.0023  -0.0099 7   TYR   A OH  
51   N  N   . GLY   A 8   ? 0.1352 0.1546 0.2472 0.0013  0.0589  -0.0424 8   GLY   A N   
52   C  CA  . GLY   A 8   ? 0.1713 0.1536 0.2686 -0.0012 0.0455  -0.0426 8   GLY   A CA  
53   C  C   . GLY   A 8   ? 0.1496 0.1480 0.2313 0.0183  0.0478  -0.0479 8   GLY   A C   
54   O  O   . GLY   A 8   ? 0.1446 0.1790 0.2306 0.0047  0.0292  -0.0547 8   GLY   A O   
55   N  N   . LYS   A 9   ? 0.1713 0.1872 0.2764 0.0296  0.0336  -0.0475 9   LYS   A N   
56   C  CA  . LYS   A 9   ? 0.1979 0.2020 0.2989 0.0089  0.0178  -0.0280 9   LYS   A CA  
57   C  C   . LYS   A 9   ? 0.1887 0.1957 0.2816 0.0094  0.0441  -0.0455 9   LYS   A C   
58   O  O   . LYS   A 9   ? 0.1658 0.2009 0.2905 -0.0013 0.0270  -0.0312 9   LYS   A O   
59   C  CB  . LYS   A 9   ? 0.2667 0.2406 0.3622 0.0464  -0.0076 -0.0174 9   LYS   A CB  
60   C  CG  . LYS   A 9   ? 0.3851 0.3181 0.4489 0.0086  0.0062  -0.0121 9   LYS   A CG  
61   C  CD  . LYS   A 9   ? 0.4673 0.3668 0.5019 0.0451  0.0251  -0.0097 9   LYS   A CD  
62   C  CE  . LYS   A 9   ? 0.5384 0.4007 0.5525 0.0241  0.0195  -0.0361 9   LYS   A CE  
63   N  NZ  . LYS   A 9   ? 0.5861 0.4259 0.5716 0.0452  0.0328  -0.0170 9   LYS   A NZ  
64   N  N   . HIS   A 10  ? 0.1600 0.1623 0.3171 0.0312  0.0706  -0.0318 10  HIS   A N   
65   C  CA  . HIS   A 10  ? 0.1536 0.1813 0.3033 0.0293  0.0892  -0.0454 10  HIS   A CA  
66   C  C   . HIS   A 10  ? 0.1111 0.1646 0.2402 0.0064  0.0718  -0.0188 10  HIS   A C   
67   O  O   . HIS   A 10  ? 0.1066 0.2088 0.2863 0.0029  0.0340  -0.0484 10  HIS   A O   
68   C  CB  . HIS   A 10  ? 0.1777 0.2264 0.3449 0.0191  0.1292  -0.0543 10  HIS   A CB  
69   C  CG  . HIS   A 10  ? 0.2541 0.2756 0.4323 0.0359  0.1403  -0.0137 10  HIS   A CG  
70   N  ND1 . HIS   A 10  ? 0.2792 0.3021 0.4789 0.0344  0.1888  -0.0442 10  HIS   A ND1 
71   C  CD2 . HIS   A 10  ? 0.2752 0.3084 0.4483 0.0793  0.1607  -0.0295 10  HIS   A CD2 
72   C  CE1 . HIS   A 10  ? 0.2323 0.2113 0.4685 0.0362  0.1661  -0.0713 10  HIS   A CE1 
73   N  NE2 . HIS   A 10  ? 0.3776 0.3111 0.4745 0.0390  0.1347  -0.0383 10  HIS   A NE2 
74   N  N   . ASN   A 11  ? 0.1015 0.1513 0.2103 0.0061  0.0654  -0.0110 11  ASN   A N   
75   C  CA  . ASN   A 11  ? 0.1078 0.1533 0.1767 0.0048  0.0422  -0.0199 11  ASN   A CA  
76   C  C   . ASN   A 11  ? 0.0954 0.1455 0.1385 0.0079  0.0226  -0.0106 11  ASN   A C   
77   O  O   . ASN   A 11  ? 0.0939 0.1365 0.1474 0.0036  0.0366  -0.0055 11  ASN   A O   
78   C  CB  . ASN   A 11  ? 0.1254 0.1698 0.1719 0.0173  0.0577  -0.0158 11  ASN   A CB  
79   C  CG  . ASN   A 11  ? 0.1462 0.1953 0.1524 0.0154  0.0556  -0.0170 11  ASN   A CG  
80   O  OD1 . ASN   A 11  ? 0.1540 0.2042 0.1723 -0.0136 0.0346  -0.0074 11  ASN   A OD1 
81   N  ND2 . ASN   A 11  ? 0.1810 0.2739 0.1792 -0.0065 0.0510  0.0160  11  ASN   A ND2 
82   N  N   . GLY   A 12  ? 0.0847 0.1506 0.1519 0.0070  0.0171  -0.0080 12  GLY   A N   
83   C  CA  . GLY   A 12  ? 0.0786 0.1462 0.1367 0.0134  0.0119  -0.0090 12  GLY   A CA  
84   C  C   . GLY   A 12  ? 0.0752 0.1309 0.1241 0.0063  0.0016  -0.0046 12  GLY   A C   
85   O  O   . GLY   A 12  ? 0.0726 0.1353 0.1290 0.0045  -0.0063 0.0019  12  GLY   A O   
86   N  N   . PRO   A 13  ? 0.0768 0.1221 0.1212 -0.0021 0.0044  -0.0043 13  PRO   A N   
87   C  CA  . PRO   A 13  ? 0.0772 0.1149 0.1249 0.0004  0.0114  -0.0125 13  PRO   A CA  
88   C  C   . PRO   A 13  ? 0.0883 0.1210 0.1162 0.0018  0.0135  -0.0017 13  PRO   A C   
89   O  O   . PRO   A 13  ? 0.0785 0.1486 0.1273 -0.0052 0.0059  -0.0185 13  PRO   A O   
90   C  CB  . PRO   A 13  ? 0.0880 0.1165 0.1256 -0.0050 0.0163  -0.0073 13  PRO   A CB  
91   C  CG  . PRO   A 13  ? 0.0926 0.1282 0.1306 -0.0133 0.0153  -0.0075 13  PRO   A CG  
92   C  CD  . PRO   A 13  ? 0.0837 0.1299 0.1301 -0.0088 0.0090  -0.0144 13  PRO   A CD  
93   N  N   . GLU   A 14  ? 0.1115 0.1170 0.1347 0.0071  -0.0004 0.0015  14  GLU   A N   
94   C  CA  . GLU   A 14  ? 0.1473 0.1360 0.1463 0.0144  -0.0159 0.0012  14  GLU   A CA  
95   C  C   . GLU   A 14  ? 0.0961 0.1281 0.1435 0.0258  -0.0171 0.0052  14  GLU   A C   
96   O  O   . GLU   A 14  ? 0.1194 0.1542 0.1524 0.0303  -0.0317 0.0086  14  GLU   A O   
97   C  CB  . GLU   A 14  ? 0.1924 0.1663 0.1882 0.0269  -0.0512 0.0097  14  GLU   A CB  
98   C  CG  . GLU   A 14  ? 0.2584 0.2007 0.2344 -0.0023 -0.0336 0.0154  14  GLU   A CG  
99   C  CD  . GLU   A 14  ? 0.2612 0.2574 0.2677 0.0034  -0.0276 0.0073  14  GLU   A CD  
100  O  OE1 . GLU   A 14  ? 0.2977 0.3157 0.2891 -0.0289 -0.0324 0.0177  14  GLU   A OE1 
101  O  OE2 . GLU   A 14  ? 0.2534 0.3082 0.2822 0.0433  -0.0115 -0.0211 14  GLU   A OE2 
102  N  N   . HIS   A 15  ? 0.0788 0.1324 0.1372 0.0167  -0.0150 -0.0025 15  HIS   A N   
103  C  CA  . HIS   A 15  ? 0.0616 0.1333 0.1532 0.0176  -0.0072 0.0004  15  HIS   A CA  
104  C  C   . HIS   A 15  ? 0.0579 0.1358 0.1309 0.0065  -0.0026 -0.0107 15  HIS   A C   
105  O  O   . HIS   A 15  ? 0.0515 0.1421 0.1542 0.0067  0.0023  -0.0056 15  HIS   A O   
106  C  CB  . HIS   A 15  ? 0.0616 0.1463 0.1640 0.0228  -0.0047 -0.0076 15  HIS   A CB  
107  C  CG  . HIS   A 15  ? 0.0870 0.1587 0.1709 0.0357  -0.0126 -0.0147 15  HIS   A CG  
108  N  ND1 . HIS   A 15  ? 0.0933 0.1857 0.2079 0.0403  -0.0078 -0.0394 15  HIS   A ND1 
109  C  CD2 . HIS   A 15  ? 0.1131 0.1679 0.2145 0.0461  -0.0169 -0.0240 15  HIS   A CD2 
110  C  CE1 . HIS   A 15  ? 0.1322 0.1807 0.2399 0.0455  -0.0305 -0.0363 15  HIS   A CE1 
111  N  NE2 . HIS   A 15  ? 0.1341 0.1596 0.2449 0.0465  0.0014  -0.0315 15  HIS   A NE2 
112  N  N   . TRP   A 16  ? 0.0522 0.1136 0.1273 -0.0047 -0.0024 -0.0045 16  TRP   A N   
113  C  CA  . TRP   A 16  ? 0.0489 0.1191 0.1204 -0.0017 -0.0028 -0.0076 16  TRP   A CA  
114  C  C   . TRP   A 16  ? 0.0464 0.1246 0.1259 0.0072  -0.0090 -0.0059 16  TRP   A C   
115  O  O   . TRP   A 16  ? 0.0535 0.1268 0.1457 -0.0073 -0.0174 -0.0071 16  TRP   A O   
116  C  CB  . TRP   A 16  ? 0.0469 0.1143 0.1031 0.0055  -0.0052 -0.0115 16  TRP   A CB  
117  C  CG  . TRP   A 16  ? 0.0467 0.1065 0.0973 0.0000  -0.0048 -0.0097 16  TRP   A CG  
118  C  CD1 . TRP   A 16  ? 0.0549 0.1126 0.1076 0.0035  0.0033  -0.0108 16  TRP   A CD1 
119  C  CD2 . TRP   A 16  ? 0.0501 0.0995 0.0948 -0.0048 0.0015  -0.0111 16  TRP   A CD2 
120  N  NE1 . TRP   A 16  ? 0.0629 0.1100 0.1013 -0.0005 0.0096  -0.0208 16  TRP   A NE1 
121  C  CE2 . TRP   A 16  ? 0.0545 0.1019 0.0984 -0.0044 0.0016  -0.0110 16  TRP   A CE2 
122  C  CE3 . TRP   A 16  ? 0.0530 0.0978 0.0913 -0.0035 0.0022  -0.0062 16  TRP   A CE3 
123  C  CZ2 . TRP   A 16  ? 0.0654 0.1079 0.0875 -0.0119 -0.0031 -0.0116 16  TRP   A CZ2 
124  C  CZ3 . TRP   A 16  ? 0.0480 0.1001 0.0944 -0.0083 0.0069  -0.0045 16  TRP   A CZ3 
125  C  CH2 . TRP   A 16  ? 0.0506 0.1025 0.0925 -0.0123 0.0017  -0.0007 16  TRP   A CH2 
126  N  N   . HIS   A 17  ? 0.0469 0.1326 0.1285 0.0029  -0.0115 -0.0118 17  HIS   A N   
127  C  CA  . HIS   A 17  ? 0.0459 0.1472 0.1272 -0.0059 -0.0148 -0.0140 17  HIS   A CA  
128  C  C   . HIS   A 17  ? 0.0555 0.1555 0.1403 -0.0142 -0.0055 -0.0135 17  HIS   A C   
129  O  O   . HIS   A 17  ? 0.0602 0.1577 0.1652 -0.0185 -0.0113 -0.0288 17  HIS   A O   
130  C  CB  . HIS   A 17  ? 0.0591 0.1637 0.1227 0.0038  -0.0181 -0.0086 17  HIS   A CB  
131  C  CG  . HIS   A 17  ? 0.0618 0.1789 0.1416 0.0121  -0.0151 0.0035  17  HIS   A CG  
132  N  ND1 . HIS   A 17  ? 0.0740 0.2051 0.1720 0.0023  -0.0269 0.0125  17  HIS   A ND1 
133  C  CD2 . HIS   A 17  ? 0.0795 0.1764 0.1473 0.0174  -0.0174 0.0102  17  HIS   A CD2 
134  C  CE1 . HIS   A 17  ? 0.0872 0.2245 0.1735 0.0114  -0.0065 0.0131  17  HIS   A CE1 
135  N  NE2 . HIS   A 17  ? 0.0878 0.2011 0.1598 0.0269  -0.0046 0.0212  17  HIS   A NE2 
136  N  N   . LYS   A 18  ? 0.0449 0.1477 0.1441 -0.0055 -0.0051 -0.0125 18  LYS   A N   
137  C  CA  . LYS   A 18  ? 0.0478 0.1717 0.1679 -0.0132 -0.0180 0.0002  18  LYS   A CA  
138  C  C   . LYS   A 18  ? 0.0545 0.1787 0.1660 -0.0212 -0.0193 0.0010  18  LYS   A C   
139  O  O   . LYS   A 18  ? 0.0942 0.1921 0.2333 -0.0400 -0.0389 0.0071  18  LYS   A O   
140  C  CB  . LYS   A 18  ? 0.0510 0.1937 0.1554 0.0020  -0.0192 0.0044  18  LYS   A CB  
141  C  CG  . LYS   A 18  ? 0.0553 0.1996 0.1563 0.0106  -0.0182 0.0065  18  LYS   A CG  
142  C  CD  . LYS   A 18  ? 0.0630 0.1949 0.1567 0.0180  -0.0154 0.0163  18  LYS   A CD  
143  C  CE  . LYS   A 18  ? 0.0528 0.1930 0.1598 0.0216  -0.0075 0.0140  18  LYS   A CE  
144  N  NZ  . LYS   A 18  ? 0.0542 0.1977 0.1564 0.0415  -0.0087 0.0224  18  LYS   A NZ  
145  N  N   . ASP   A 19  ? 0.0524 0.1629 0.1743 -0.0111 -0.0134 -0.0019 19  ASP   A N   
146  C  CA  . ASP   A 19  ? 0.0660 0.1743 0.1819 -0.0074 -0.0092 0.0080  19  ASP   A CA  
147  C  C   . ASP   A 19  ? 0.0747 0.1472 0.1798 -0.0186 -0.0023 -0.0006 19  ASP   A C   
148  O  O   . ASP   A 19  ? 0.1072 0.1403 0.2161 -0.0284 0.0070  0.0057  19  ASP   A O   
149  C  CB  . ASP   A 19  ? 0.0931 0.1950 0.1939 0.0018  -0.0070 -0.0059 19  ASP   A CB  
150  C  CG  . ASP   A 19  ? 0.1262 0.2576 0.2069 0.0015  -0.0082 -0.0137 19  ASP   A CG  
151  O  OD1 . ASP   A 19  ? 0.1220 0.4125 0.2724 -0.0208 0.0123  -0.0104 19  ASP   A OD1 
152  O  OD2 . ASP   A 19  ? 0.2068 0.3153 0.2434 0.0218  -0.0083 -0.0177 19  ASP   A OD2 
153  N  N   . PHE   A 20  ? 0.0631 0.1371 0.1597 -0.0111 -0.0031 -0.0026 20  PHE   A N   
154  C  CA  . PHE   A 20  ? 0.0664 0.1339 0.1611 -0.0102 -0.0045 -0.0022 20  PHE   A CA  
155  C  C   . PHE   A 20  ? 0.0698 0.1337 0.1607 -0.0030 -0.0025 -0.0123 20  PHE   A C   
156  O  O   . PHE   A 20  ? 0.0753 0.1243 0.1445 -0.0106 -0.0024 -0.0163 20  PHE   A O   
157  C  CB  . PHE   A 20  ? 0.0747 0.1389 0.1621 -0.0238 -0.0063 0.0059  20  PHE   A CB  
158  C  CG  . PHE   A 20  ? 0.0612 0.1448 0.1657 -0.0259 -0.0079 0.0182  20  PHE   A CG  
159  C  CD1 . PHE   A 20  ? 0.0941 0.1638 0.1804 -0.0246 0.0003  0.0344  20  PHE   A CD1 
160  C  CD2 . PHE   A 20  ? 0.0765 0.1768 0.1658 -0.0164 -0.0124 0.0140  20  PHE   A CD2 
161  C  CE1 . PHE   A 20  ? 0.1109 0.1674 0.1940 -0.0168 -0.0027 0.0497  20  PHE   A CE1 
162  C  CE2 . PHE   A 20  ? 0.0805 0.2200 0.1708 -0.0104 -0.0069 0.0099  20  PHE   A CE2 
163  C  CZ  . PHE   A 20  ? 0.0961 0.2157 0.1890 -0.0228 0.0094  0.0275  20  PHE   A CZ  
164  N  N   . PRO   A 21  ? 0.0675 0.1488 0.1702 -0.0200 -0.0134 -0.0083 21  PRO   A N   
165  C  CA  . PRO   A 21  ? 0.0643 0.1677 0.1612 -0.0168 -0.0192 -0.0199 21  PRO   A CA  
166  C  C   . PRO   A 21  ? 0.0679 0.1434 0.1479 -0.0165 -0.0239 -0.0264 21  PRO   A C   
167  O  O   . PRO   A 21  ? 0.0730 0.1531 0.1394 -0.0066 -0.0291 -0.0175 21  PRO   A O   
168  C  CB  . PRO   A 21  ? 0.0762 0.1985 0.1867 -0.0296 -0.0273 -0.0207 21  PRO   A CB  
169  C  CG  . PRO   A 21  ? 0.1215 0.1941 0.2143 -0.0434 -0.0205 -0.0195 21  PRO   A CG  
170  C  CD  . PRO   A 21  ? 0.0890 0.1762 0.1907 -0.0386 -0.0244 0.0014  21  PRO   A CD  
171  N  N   A ILE   A 22  ? 0.0696 0.1300 0.1347 -0.0145 -0.0242 -0.0268 22  ILE   A N   
172  N  N   B ILE   A 22  ? 0.0748 0.1356 0.1545 -0.0090 -0.0248 -0.0291 22  ILE   A N   
173  C  CA  A ILE   A 22  ? 0.0746 0.1220 0.1139 -0.0116 -0.0204 -0.0226 22  ILE   A CA  
174  C  CA  B ILE   A 22  ? 0.0805 0.1271 0.1458 -0.0070 -0.0189 -0.0232 22  ILE   A CA  
175  C  C   A ILE   A 22  ? 0.0630 0.1254 0.1165 -0.0090 -0.0262 -0.0261 22  ILE   A C   
176  C  C   B ILE   A 22  ? 0.0656 0.1271 0.1338 -0.0064 -0.0247 -0.0250 22  ILE   A C   
177  O  O   A ILE   A 22  ? 0.0743 0.1196 0.1061 -0.0014 -0.0150 -0.0174 22  ILE   A O   
178  O  O   B ILE   A 22  ? 0.0607 0.1256 0.1338 -0.0016 -0.0236 -0.0117 22  ILE   A O   
179  C  CB  A ILE   A 22  ? 0.0716 0.1104 0.1143 -0.0182 -0.0161 -0.0163 22  ILE   A CB  
180  C  CB  B ILE   A 22  ? 0.0808 0.1257 0.1513 -0.0081 -0.0127 -0.0182 22  ILE   A CB  
181  C  CG1 A ILE   A 22  ? 0.0800 0.1059 0.1166 -0.0172 -0.0145 -0.0138 22  ILE   A CG1 
182  C  CG1 B ILE   A 22  ? 0.0943 0.1374 0.1654 -0.0123 -0.0018 -0.0207 22  ILE   A CG1 
183  C  CG2 A ILE   A 22  ? 0.0648 0.1084 0.1121 -0.0237 -0.0163 -0.0103 22  ILE   A CG2 
184  C  CG2 B ILE   A 22  ? 0.0784 0.1241 0.1470 -0.0007 -0.0169 -0.0101 22  ILE   A CG2 
185  C  CD1 A ILE   A 22  ? 0.0966 0.1074 0.1328 -0.0124 -0.0059 -0.0059 22  ILE   A CD1 
186  C  CD1 B ILE   A 22  ? 0.1134 0.1522 0.1693 -0.0161 0.0097  -0.0243 22  ILE   A CD1 
187  N  N   . ALA   A 23  ? 0.0584 0.1265 0.1277 -0.0033 -0.0193 -0.0206 23  ALA   A N   
188  C  CA  . ALA   A 23  ? 0.0549 0.1225 0.1172 -0.0042 -0.0204 -0.0177 23  ALA   A CA  
189  C  C   . ALA   A 23  ? 0.0623 0.1339 0.1276 0.0007  -0.0276 -0.0184 23  ALA   A C   
190  O  O   . ALA   A 23  ? 0.0800 0.1317 0.1360 0.0012  -0.0131 -0.0113 23  ALA   A O   
191  C  CB  . ALA   A 23  ? 0.0527 0.1333 0.1214 -0.0081 -0.0135 -0.0170 23  ALA   A CB  
192  N  N   . LYS   A 24  ? 0.0669 0.1492 0.1215 -0.0035 -0.0260 -0.0124 24  LYS   A N   
193  C  CA  . LYS   A 24  ? 0.0771 0.1883 0.1182 -0.0029 -0.0350 -0.0124 24  LYS   A CA  
194  C  C   . LYS   A 24  ? 0.0787 0.1974 0.1196 -0.0148 -0.0386 -0.0227 24  LYS   A C   
195  O  O   . LYS   A 24  ? 0.1026 0.2237 0.1272 -0.0071 -0.0422 -0.0191 24  LYS   A O   
196  C  CB  . LYS   A 24  ? 0.0880 0.2113 0.1376 0.0095  -0.0302 -0.0018 24  LYS   A CB  
197  C  CG  . LYS   A 24  ? 0.1023 0.2313 0.1508 0.0241  -0.0168 0.0108  24  LYS   A CG  
198  C  CD  . LYS   A 24  ? 0.1130 0.2669 0.2049 0.0362  -0.0098 0.0138  24  LYS   A CD  
199  C  CE  . LYS   A 24  ? 0.1553 0.2795 0.2283 0.0576  0.0040  0.0207  24  LYS   A CE  
200  N  NZ  . LYS   A 24  ? 0.1789 0.2898 0.2715 0.0570  0.0277  0.0244  24  LYS   A NZ  
201  N  N   . GLY   A 25  ? 0.0827 0.1774 0.1204 -0.0113 -0.0304 -0.0337 25  GLY   A N   
202  C  CA  . GLY   A 25  ? 0.0964 0.1838 0.1358 -0.0113 -0.0306 -0.0343 25  GLY   A CA  
203  C  C   . GLY   A 25  ? 0.0839 0.1783 0.1119 -0.0020 -0.0360 -0.0311 25  GLY   A C   
204  O  O   . GLY   A 25  ? 0.0928 0.1896 0.1379 -0.0129 -0.0300 -0.0104 25  GLY   A O   
205  N  N   . GLU   A 26  ? 0.0757 0.1970 0.1016 0.0015  -0.0370 -0.0293 26  GLU   A N   
206  C  CA  . GLU   A 26  ? 0.0998 0.2195 0.0925 0.0001  -0.0386 -0.0215 26  GLU   A CA  
207  C  C   . GLU   A 26  ? 0.0953 0.1657 0.0895 0.0000  -0.0371 -0.0139 26  GLU   A C   
208  O  O   . GLU   A 26  ? 0.1059 0.1868 0.0831 0.0035  -0.0204 -0.0056 26  GLU   A O   
209  C  CB  . GLU   A 26  ? 0.1285 0.2559 0.1118 -0.0088 -0.0442 -0.0521 26  GLU   A CB  
210  C  CG  . GLU   A 26  ? 0.1392 0.3195 0.1352 -0.0163 -0.0468 -0.0541 26  GLU   A CG  
211  C  CD  . GLU   A 26  ? 0.1616 0.3912 0.1823 -0.0036 -0.0635 -0.0314 26  GLU   A CD  
212  O  OE1 . GLU   A 26  ? 0.2540 0.4410 0.2388 -0.0252 -0.0466 0.0050  26  GLU   A OE1 
213  O  OE2 . GLU   A 26  ? 0.2519 0.4386 0.2529 0.0678  -0.0667 -0.0250 26  GLU   A OE2 
214  N  N   . ARG   A 27  ? 0.0745 0.1239 0.0801 -0.0054 -0.0340 -0.0152 27  ARG   A N   
215  C  CA  . ARG   A 27  ? 0.0859 0.1114 0.0898 0.0074  -0.0404 -0.0272 27  ARG   A CA  
216  C  C   . ARG   A 27  ? 0.0680 0.0995 0.0741 -0.0017 -0.0296 -0.0146 27  ARG   A C   
217  O  O   . ARG   A 27  ? 0.0725 0.1078 0.0857 0.0094  -0.0306 -0.0129 27  ARG   A O   
218  C  CB  . ARG   A 27  ? 0.1406 0.1615 0.1171 0.0339  -0.0575 -0.0493 27  ARG   A CB  
219  C  CG  . ARG   A 27  ? 0.1742 0.2122 0.1392 0.0043  -0.0382 -0.0349 27  ARG   A CG  
220  C  CD  . ARG   A 27  ? 0.2484 0.1745 0.1337 0.0357  0.0067  -0.0314 27  ARG   A CD  
221  N  NE  . ARG   A 27  ? 0.2627 0.1109 0.1161 -0.0152 0.0219  -0.0488 27  ARG   A NE  
222  C  CZ  . ARG   A 27  ? 0.1699 0.1572 0.0857 -0.0282 0.0318  -0.0156 27  ARG   A CZ  
223  N  NH1 . ARG   A 27  ? 0.1492 0.1740 0.1040 -0.0136 -0.0023 -0.0501 27  ARG   A NH1 
224  N  NH2 . ARG   A 27  ? 0.2015 0.2238 0.1059 -0.0722 0.0029  -0.0410 27  ARG   A NH2 
225  N  N   . GLN   A 28  ? 0.0545 0.1011 0.0693 -0.0025 -0.0261 -0.0143 28  GLN   A N   
226  C  CA  . GLN   A 28  ? 0.0546 0.0940 0.0656 0.0009  -0.0231 -0.0132 28  GLN   A CA  
227  C  C   . GLN   A 28  ? 0.0564 0.0913 0.0603 -0.0015 -0.0183 -0.0127 28  GLN   A C   
228  O  O   . GLN   A 28  ? 0.0718 0.1102 0.0564 -0.0046 -0.0189 -0.0039 28  GLN   A O   
229  C  CB  . GLN   A 28  ? 0.0504 0.1021 0.0722 -0.0002 -0.0231 -0.0097 28  GLN   A CB  
230  C  CG  . GLN   A 28  ? 0.0591 0.1072 0.0837 -0.0004 -0.0237 -0.0142 28  GLN   A CG  
231  C  CD  . GLN   A 28  ? 0.0536 0.1032 0.0826 -0.0061 -0.0212 -0.0150 28  GLN   A CD  
232  O  OE1 . GLN   A 28  ? 0.0573 0.1054 0.0910 -0.0098 -0.0127 -0.0141 28  GLN   A OE1 
233  N  NE2 . GLN   A 28  ? 0.0575 0.0978 0.0803 -0.0007 -0.0099 -0.0071 28  GLN   A NE2 
234  N  N   . SER   A 29  ? 0.0469 0.0896 0.0570 -0.0064 -0.0120 -0.0088 29  SER   A N   
235  C  CA  . SER   A 29  ? 0.0524 0.0789 0.0571 -0.0033 -0.0121 -0.0064 29  SER   A CA  
236  C  C   . SER   A 29  ? 0.0473 0.0789 0.0522 0.0029  -0.0116 -0.0047 29  SER   A C   
237  O  O   . SER   A 29  ? 0.0549 0.0917 0.0677 0.0015  -0.0068 -0.0106 29  SER   A O   
238  C  CB  . SER   A 29  ? 0.0541 0.0780 0.0572 0.0022  -0.0143 -0.0095 29  SER   A CB  
239  O  OG  . SER   A 29  ? 0.0550 0.0787 0.0631 0.0034  -0.0031 -0.0094 29  SER   A OG  
240  N  N   . PRO   A 30  ? 0.0533 0.0739 0.0570 0.0077  -0.0095 -0.0082 30  PRO   A N   
241  C  CA  . PRO   A 30  ? 0.0528 0.0759 0.0564 0.0074  -0.0131 -0.0014 30  PRO   A CA  
242  C  C   . PRO   A 30  ? 0.0562 0.0821 0.0592 0.0081  -0.0148 -0.0020 30  PRO   A C   
243  O  O   . PRO   A 30  ? 0.0579 0.0966 0.0650 0.0042  -0.0175 0.0065  30  PRO   A O   
244  C  CB  . PRO   A 30  ? 0.0619 0.0795 0.0499 0.0066  -0.0121 -0.0041 30  PRO   A CB  
245  C  CG  . PRO   A 30  ? 0.0609 0.0772 0.0542 0.0037  -0.0031 -0.0051 30  PRO   A CG  
246  C  CD  . PRO   A 30  ? 0.0649 0.0793 0.0528 0.0038  -0.0011 -0.0038 30  PRO   A CD  
247  N  N   . VAL   A 31  ? 0.0600 0.0872 0.0572 0.0091  -0.0106 0.0100  31  VAL   A N   
248  C  CA  . VAL   A 31  ? 0.0682 0.0827 0.0580 0.0115  -0.0136 0.0059  31  VAL   A CA  
249  C  C   . VAL   A 31  ? 0.0656 0.0855 0.0605 0.0159  -0.0117 0.0079  31  VAL   A C   
250  O  O   . VAL   A 31  ? 0.0789 0.0849 0.0689 0.0081  -0.0198 0.0148  31  VAL   A O   
251  C  CB  . VAL   A 31  ? 0.0771 0.0901 0.0646 0.0105  -0.0059 0.0046  31  VAL   A CB  
252  C  CG1 . VAL   A 31  ? 0.0956 0.1039 0.0704 0.0023  -0.0092 -0.0044 31  VAL   A CG1 
253  C  CG2 . VAL   A 31  ? 0.0826 0.0914 0.0681 0.0163  -0.0009 0.0054  31  VAL   A CG2 
254  N  N   . ASP   A 32  ? 0.0703 0.0912 0.0597 0.0152  -0.0115 0.0152  32  ASP   A N   
255  C  CA  . ASP   A 32  ? 0.0815 0.0849 0.0632 0.0115  -0.0110 0.0138  32  ASP   A CA  
256  C  C   . ASP   A 32  ? 0.0854 0.0951 0.0582 0.0077  -0.0110 0.0131  32  ASP   A C   
257  O  O   . ASP   A 32  ? 0.0987 0.1290 0.0709 -0.0044 -0.0077 -0.0083 32  ASP   A O   
258  C  CB  . ASP   A 32  ? 0.0986 0.0928 0.0666 0.0170  -0.0119 0.0155  32  ASP   A CB  
259  C  CG  . ASP   A 32  ? 0.1091 0.0949 0.0705 0.0163  -0.0053 0.0197  32  ASP   A CG  
260  O  OD1 . ASP   A 32  ? 0.1123 0.0907 0.0824 0.0086  -0.0084 0.0231  32  ASP   A OD1 
261  O  OD2 . ASP   A 32  ? 0.1603 0.1276 0.0776 -0.0040 -0.0156 0.0291  32  ASP   A OD2 
262  N  N   . ILE   A 33  ? 0.0818 0.0836 0.0603 0.0089  -0.0050 0.0090  33  ILE   A N   
263  C  CA  . ILE   A 33  ? 0.0882 0.0808 0.0607 0.0122  -0.0054 0.0121  33  ILE   A CA  
264  C  C   . ILE   A 33  ? 0.0987 0.0876 0.0599 0.0187  -0.0012 0.0112  33  ILE   A C   
265  O  O   . ILE   A 33  ? 0.1090 0.1008 0.0737 -0.0007 0.0057  0.0161  33  ILE   A O   
266  C  CB  . ILE   A 33  ? 0.0946 0.0839 0.0715 0.0157  -0.0091 0.0116  33  ILE   A CB  
267  C  CG1 . ILE   A 33  ? 0.0857 0.0931 0.0901 0.0108  -0.0080 0.0126  33  ILE   A CG1 
268  C  CG2 . ILE   A 33  ? 0.1007 0.0936 0.0920 0.0191  -0.0020 0.0107  33  ILE   A CG2 
269  C  CD1 . ILE   A 33  ? 0.0967 0.1107 0.1009 0.0089  -0.0095 0.0164  33  ILE   A CD1 
270  N  N   A ASP   A 34  ? 0.1133 0.0964 0.0629 0.0134  -0.0062 0.0166  34  ASP   A N   
271  N  N   B ASP   A 34  ? 0.1127 0.1019 0.0657 0.0145  -0.0102 0.0215  34  ASP   A N   
272  C  CA  A ASP   A 34  ? 0.1321 0.1012 0.0648 0.0221  0.0052  0.0178  34  ASP   A CA  
273  C  CA  B ASP   A 34  ? 0.1310 0.1133 0.0710 0.0250  -0.0026 0.0297  34  ASP   A CA  
274  C  C   A ASP   A 34  ? 0.1370 0.1123 0.0611 0.0265  0.0081  0.0239  34  ASP   A C   
275  C  C   B ASP   A 34  ? 0.1400 0.1192 0.0646 0.0277  0.0036  0.0305  34  ASP   A C   
276  O  O   A ASP   A 34  ? 0.1446 0.1306 0.0800 0.0340  0.0224  0.0150  34  ASP   A O   
277  O  O   B ASP   A 34  ? 0.1581 0.1398 0.0813 0.0401  0.0191  0.0238  34  ASP   A O   
278  C  CB  A ASP   A 34  ? 0.1449 0.1047 0.0745 0.0217  0.0056  0.0167  34  ASP   A CB  
279  C  CB  B ASP   A 34  ? 0.1395 0.1265 0.0886 0.0279  -0.0080 0.0367  34  ASP   A CB  
280  C  CG  A ASP   A 34  ? 0.1617 0.1092 0.0727 0.0151  0.0081  0.0132  34  ASP   A CG  
281  C  CG  B ASP   A 34  ? 0.1406 0.1538 0.1015 0.0271  -0.0113 0.0540  34  ASP   A CG  
282  O  OD1 A ASP   A 34  ? 0.1812 0.1085 0.1031 0.0224  0.0112  0.0224  34  ASP   A OD1 
283  O  OD1 B ASP   A 34  ? 0.1280 0.1851 0.1157 0.0322  -0.0002 0.0746  34  ASP   A OD1 
284  O  OD2 A ASP   A 34  ? 0.1849 0.1186 0.0828 0.0157  0.0283  0.0198  34  ASP   A OD2 
285  O  OD2 B ASP   A 34  ? 0.1709 0.1790 0.1247 0.0404  -0.0187 0.0833  34  ASP   A OD2 
286  N  N   . THR   A 35  ? 0.1298 0.1359 0.0738 0.0243  0.0075  0.0310  35  THR   A N   
287  C  CA  . THR   A 35  ? 0.1293 0.1545 0.0928 0.0289  0.0026  0.0384  35  THR   A CA  
288  C  C   . THR   A 35  ? 0.1437 0.1658 0.0970 0.0391  0.0171  0.0419  35  THR   A C   
289  O  O   . THR   A 35  ? 0.1860 0.1857 0.1259 0.0632  0.0246  0.0410  35  THR   A O   
290  C  CB  . THR   A 35  ? 0.1269 0.1805 0.1117 0.0214  -0.0029 0.0250  35  THR   A CB  
291  O  OG1 . THR   A 35  ? 0.1394 0.1865 0.1240 0.0030  0.0164  0.0274  35  THR   A OG1 
292  C  CG2 . THR   A 35  ? 0.1643 0.1923 0.1070 0.0197  -0.0253 0.0303  35  THR   A CG2 
293  N  N   . HIS   A 36  ? 0.1554 0.1380 0.0759 0.0307  0.0246  0.0391  36  HIS   A N   
294  C  CA  . HIS   A 36  ? 0.1875 0.1351 0.0822 0.0194  0.0217  0.0444  36  HIS   A CA  
295  C  C   . HIS   A 36  ? 0.2259 0.1568 0.0748 0.0074  0.0154  0.0323  36  HIS   A C   
296  O  O   . HIS   A 36  ? 0.3120 0.2298 0.1113 -0.0229 0.0500  0.0174  36  HIS   A O   
297  C  CB  . HIS   A 36  ? 0.2106 0.1365 0.0938 0.0136  0.0115  0.0490  36  HIS   A CB  
298  C  CG  . HIS   A 36  ? 0.2490 0.1488 0.1269 0.0314  -0.0234 0.0532  36  HIS   A CG  
299  N  ND1 . HIS   A 36  ? 0.2736 0.1865 0.1670 0.0726  -0.0394 0.0552  36  HIS   A ND1 
300  C  CD2 . HIS   A 36  ? 0.2762 0.1913 0.1719 -0.0032 -0.0262 0.0528  36  HIS   A CD2 
301  C  CE1 . HIS   A 36  ? 0.2954 0.1701 0.1812 0.0400  -0.0358 0.0552  36  HIS   A CE1 
302  N  NE2 . HIS   A 36  ? 0.2972 0.2054 0.1951 0.0145  -0.0239 0.0418  36  HIS   A NE2 
303  N  N   . THR   A 37  ? 0.1626 0.1419 0.0943 0.0323  0.0057  -0.0023 37  THR   A N   
304  C  CA  . THR   A 37  ? 0.1826 0.1450 0.0966 0.0517  -0.0176 0.0140  37  THR   A CA  
305  C  C   . THR   A 37  ? 0.1700 0.1370 0.1037 0.0469  -0.0259 0.0178  37  THR   A C   
306  O  O   . THR   A 37  ? 0.2185 0.1537 0.1255 0.0394  -0.0461 -0.0008 37  THR   A O   
307  C  CB  . THR   A 37  ? 0.1778 0.1566 0.1809 0.0539  -0.0489 0.0215  37  THR   A CB  
308  O  OG1 . THR   A 37  ? 0.2204 0.1570 0.2639 0.0654  -0.0660 0.0212  37  THR   A OG1 
309  C  CG2 . THR   A 37  ? 0.2015 0.1805 0.1589 0.0550  -0.0504 0.0165  37  THR   A CG2 
310  N  N   . ALA   A 38  ? 0.1683 0.1341 0.0871 0.0331  -0.0160 0.0329  38  ALA   A N   
311  C  CA  . ALA   A 38  ? 0.1451 0.1276 0.0883 0.0298  0.0011  0.0368  38  ALA   A CA  
312  C  C   . ALA   A 38  ? 0.1435 0.1265 0.1346 0.0141  0.0182  0.0243  38  ALA   A C   
313  O  O   . ALA   A 38  ? 0.2034 0.1484 0.2076 0.0028  0.0669  0.0271  38  ALA   A O   
314  C  CB  . ALA   A 38  ? 0.1398 0.1284 0.1004 0.0386  -0.0017 0.0288  38  ALA   A CB  
315  N  N   . LYS   A 39  ? 0.1024 0.1236 0.1253 0.0199  0.0088  0.0223  39  LYS   A N   
316  C  CA  . LYS   A 39  ? 0.1068 0.1317 0.1001 0.0334  -0.0099 0.0213  39  LYS   A CA  
317  C  C   . LYS   A 39  ? 0.1061 0.1362 0.0736 0.0285  -0.0169 0.0199  39  LYS   A C   
318  O  O   . LYS   A 39  ? 0.0973 0.1274 0.0811 0.0264  -0.0039 0.0054  39  LYS   A O   
319  C  CB  . LYS   A 39  ? 0.1326 0.1538 0.1022 0.0446  -0.0309 0.0154  39  LYS   A CB  
320  C  CG  . LYS   A 39  ? 0.1675 0.1703 0.1036 0.0534  -0.0280 0.0118  39  LYS   A CG  
321  C  CD  . LYS   A 39  ? 0.1961 0.2066 0.0895 0.0709  -0.0386 0.0114  39  LYS   A CD  
322  C  CE  . LYS   A 39  ? 0.2094 0.2456 0.0932 0.0719  -0.0354 0.0115  39  LYS   A CE  
323  N  NZ  . LYS   A 39  ? 0.2130 0.2402 0.1308 0.0914  -0.0439 0.0007  39  LYS   A NZ  
324  N  N   . TYR   A 40  ? 0.1047 0.1490 0.0765 0.0290  -0.0045 0.0361  40  TYR   A N   
325  C  CA  . TYR   A 40  ? 0.1040 0.1713 0.0775 0.0434  0.0017  0.0319  40  TYR   A CA  
326  C  C   . TYR   A 40  ? 0.1178 0.1770 0.0779 0.0536  -0.0104 0.0347  40  TYR   A C   
327  O  O   . TYR   A 40  ? 0.1798 0.1914 0.0756 0.0742  -0.0131 0.0233  40  TYR   A O   
328  C  CB  . TYR   A 40  ? 0.1120 0.2087 0.1033 0.0359  -0.0013 0.0478  40  TYR   A CB  
329  C  CG  . TYR   A 40  ? 0.1018 0.2607 0.1093 0.0503  0.0136  0.0588  40  TYR   A CG  
330  C  CD1 . TYR   A 40  ? 0.1070 0.2649 0.1035 0.0558  0.0148  0.0504  40  TYR   A CD1 
331  C  CD2 . TYR   A 40  ? 0.1517 0.3036 0.1265 0.0770  0.0220  0.0504  40  TYR   A CD2 
332  C  CE1 . TYR   A 40  ? 0.1124 0.3050 0.1350 0.0677  0.0054  0.0619  40  TYR   A CE1 
333  C  CE2 . TYR   A 40  ? 0.1457 0.3347 0.1684 0.0813  0.0233  0.0586  40  TYR   A CE2 
334  C  CZ  . TYR   A 40  ? 0.1135 0.3308 0.1728 0.0995  0.0112  0.0659  40  TYR   A CZ  
335  O  OH  . TYR   A 40  ? 0.1262 0.4035 0.2372 0.1333  0.0228  0.0731  40  TYR   A OH  
336  N  N   . ASP   A 41  ? 0.1336 0.1676 0.0752 0.0641  -0.0047 0.0253  41  ASP   A N   
337  C  CA  . ASP   A 41  ? 0.1765 0.1852 0.0796 0.0659  -0.0136 0.0146  41  ASP   A CA  
338  C  C   . ASP   A 41  ? 0.1904 0.2092 0.0787 0.0894  0.0108  0.0185  41  ASP   A C   
339  O  O   . ASP   A 41  ? 0.1705 0.2001 0.0981 0.0905  0.0004  0.0196  41  ASP   A O   
340  C  CB  . ASP   A 41  ? 0.1920 0.1694 0.1086 0.0558  -0.0348 0.0183  41  ASP   A CB  
341  C  CG  . ASP   A 41  ? 0.2544 0.2065 0.1588 0.0370  -0.0291 -0.0035 41  ASP   A CG  
342  O  OD1 . ASP   A 41  ? 0.3360 0.1907 0.1584 0.0743  -0.0352 -0.0229 41  ASP   A OD1 
343  O  OD2 . ASP   A 41  ? 0.3011 0.2450 0.2079 0.0172  -0.0252 -0.0571 41  ASP   A OD2 
344  N  N   . PRO   A 42  ? 0.2401 0.2474 0.1054 0.1354  0.0354  0.0131  42  PRO   A N   
345  C  CA  . PRO   A 42  ? 0.2475 0.2789 0.1361 0.1359  0.0474  0.0284  42  PRO   A CA  
346  C  C   . PRO   A 42  ? 0.2655 0.2441 0.1178 0.1555  0.0388  0.0189  42  PRO   A C   
347  O  O   . PRO   A 42  ? 0.3068 0.2978 0.1903 0.1900  0.0300  0.0260  42  PRO   A O   
348  C  CB  . PRO   A 42  ? 0.2686 0.2960 0.1522 0.1273  0.0667  0.0170  42  PRO   A CB  
349  C  CG  . PRO   A 42  ? 0.3048 0.3154 0.0956 0.1036  0.0421  0.0212  42  PRO   A CG  
350  C  CD  . PRO   A 42  ? 0.2692 0.2660 0.1077 0.1255  0.0205  0.0205  42  PRO   A CD  
351  N  N   . SER   A 43  ? 0.3264 0.2335 0.1400 0.1470  0.0229  -0.0063 43  SER   A N   
352  C  CA  . SER   A 43  ? 0.3239 0.2162 0.1555 0.1274  -0.0060 -0.0238 43  SER   A CA  
353  C  C   . SER   A 43  ? 0.3075 0.2062 0.1459 0.1205  -0.0156 -0.0169 43  SER   A C   
354  O  O   . SER   A 43  ? 0.3741 0.2156 0.1687 0.1002  -0.0441 -0.0069 43  SER   A O   
355  C  CB  . SER   A 43  ? 0.3430 0.2683 0.1795 0.1082  -0.0309 -0.0439 43  SER   A CB  
356  O  OG  . SER   A 43  ? 0.3346 0.2681 0.2489 0.0806  -0.0450 -0.0662 43  SER   A OG  
357  N  N   . LEU   A 44  ? 0.2627 0.1818 0.1163 0.0854  -0.0217 0.0050  44  LEU   A N   
358  C  CA  . LEU   A 44  ? 0.2086 0.1611 0.1284 0.0585  -0.0151 0.0172  44  LEU   A CA  
359  C  C   . LEU   A 44  ? 0.2056 0.1811 0.1469 0.0622  -0.0098 0.0237  44  LEU   A C   
360  O  O   . LEU   A 44  ? 0.2011 0.2067 0.1672 0.0839  0.0206  0.0379  44  LEU   A O   
361  C  CB  . LEU   A 44  ? 0.1645 0.1539 0.1145 0.0376  -0.0155 0.0160  44  LEU   A CB  
362  C  CG  . LEU   A 44  ? 0.1394 0.1452 0.0991 0.0243  -0.0085 0.0139  44  LEU   A CG  
363  C  CD1 . LEU   A 44  ? 0.1391 0.1597 0.1008 0.0135  -0.0046 0.0183  44  LEU   A CD1 
364  C  CD2 . LEU   A 44  ? 0.1460 0.1438 0.1297 0.0190  -0.0137 0.0207  44  LEU   A CD2 
365  N  N   . LYS   A 45  ? 0.2052 0.2000 0.1646 0.0578  -0.0219 0.0374  45  LYS   A N   
366  C  CA  . LYS   A 45  ? 0.1984 0.2007 0.1819 0.0682  -0.0093 0.0219  45  LYS   A CA  
367  C  C   . LYS   A 45  ? 0.1277 0.2002 0.1672 0.0569  -0.0049 0.0311  45  LYS   A C   
368  O  O   . LYS   A 45  ? 0.1229 0.1639 0.1386 0.0323  0.0084  0.0379  45  LYS   A O   
369  C  CB  . LYS   A 45  ? 0.2331 0.2065 0.2291 0.0648  -0.0247 0.0268  45  LYS   A CB  
370  C  CG  . LYS   A 45  ? 0.2778 0.2189 0.2824 0.0676  0.0037  0.0030  45  LYS   A CG  
371  C  CD  . LYS   A 45  ? 0.3333 0.3296 0.3325 0.0463  0.0165  -0.0063 45  LYS   A CD  
372  C  CE  . LYS   A 45  ? 0.3825 0.4044 0.3805 0.0443  0.0074  -0.0363 45  LYS   A CE  
373  N  NZ  . LYS   A 45  ? 0.4129 0.4879 0.4042 0.0584  0.0278  -0.0348 45  LYS   A NZ  
374  N  N   . PRO   A 46  ? 0.1148 0.2346 0.1771 0.0416  0.0147  0.0222  46  PRO   A N   
375  C  CA  . PRO   A 46  ? 0.1034 0.2381 0.1899 0.0031  0.0029  0.0356  46  PRO   A CA  
376  C  C   . PRO   A 46  ? 0.0923 0.1977 0.1702 0.0083  -0.0119 0.0354  46  PRO   A C   
377  O  O   . PRO   A 46  ? 0.1021 0.2082 0.1624 0.0165  0.0136  0.0356  46  PRO   A O   
378  C  CB  . PRO   A 46  ? 0.1135 0.2803 0.2099 0.0159  -0.0007 0.0404  46  PRO   A CB  
379  C  CG  . PRO   A 46  ? 0.1372 0.2831 0.2238 0.0323  0.0146  0.0247  46  PRO   A CG  
380  C  CD  . PRO   A 46  ? 0.1358 0.2605 0.1948 0.0509  0.0183  0.0190  46  PRO   A CD  
381  N  N   . LEU   A 47  ? 0.0863 0.1927 0.1355 -0.0140 -0.0114 0.0460  47  LEU   A N   
382  C  CA  . LEU   A 47  ? 0.0841 0.1681 0.1345 -0.0167 -0.0223 0.0481  47  LEU   A CA  
383  C  C   . LEU   A 47  ? 0.0798 0.1524 0.1396 -0.0143 -0.0285 0.0443  47  LEU   A C   
384  O  O   . LEU   A 47  ? 0.0823 0.2086 0.1838 -0.0396 -0.0334 0.0562  47  LEU   A O   
385  C  CB  . LEU   A 47  ? 0.1006 0.1691 0.1452 -0.0131 -0.0165 0.0439  47  LEU   A CB  
386  C  CG  . LEU   A 47  ? 0.1039 0.1616 0.1371 -0.0023 -0.0268 0.0382  47  LEU   A CG  
387  C  CD1 . LEU   A 47  ? 0.1037 0.1680 0.1587 -0.0154 -0.0121 0.0260  47  LEU   A CD1 
388  C  CD2 . LEU   A 47  ? 0.1097 0.1692 0.1673 -0.0077 -0.0240 0.0364  47  LEU   A CD2 
389  N  N   . SER   A 48  ? 0.0812 0.1370 0.1251 -0.0116 -0.0227 0.0328  48  SER   A N   
390  C  CA  . SER   A 48  ? 0.0944 0.1429 0.1306 -0.0041 -0.0174 0.0274  48  SER   A CA  
391  C  C   . SER   A 48  ? 0.1001 0.1436 0.1180 -0.0196 -0.0201 0.0213  48  SER   A C   
392  O  O   . SER   A 48  ? 0.1136 0.1568 0.1326 -0.0326 -0.0198 0.0012  48  SER   A O   
393  C  CB  . SER   A 48  ? 0.1269 0.1579 0.1708 0.0117  -0.0116 0.0239  48  SER   A CB  
394  O  OG  . SER   A 48  ? 0.1750 0.2072 0.2241 0.0430  -0.0029 0.0537  48  SER   A OG  
395  N  N   . VAL   A 49  ? 0.1148 0.1567 0.1279 -0.0421 -0.0052 0.0142  49  VAL   A N   
396  C  CA  . VAL   A 49  ? 0.1305 0.1641 0.1366 -0.0582 -0.0103 -0.0071 49  VAL   A CA  
397  C  C   . VAL   A 49  ? 0.1461 0.2042 0.1421 -0.0611 -0.0254 -0.0004 49  VAL   A C   
398  O  O   . VAL   A 49  ? 0.1541 0.2577 0.1616 -0.0914 -0.0445 0.0270  49  VAL   A O   
399  C  CB  . VAL   A 49  ? 0.1601 0.1885 0.1630 -0.0532 0.0097  -0.0051 49  VAL   A CB  
400  C  CG1 . VAL   A 49  ? 0.2267 0.2161 0.1619 -0.0539 0.0194  -0.0136 49  VAL   A CG1 
401  C  CG2 . VAL   A 49  ? 0.1874 0.1820 0.1852 -0.0548 0.0202  0.0026  49  VAL   A CG2 
402  N  N   . SER   A 50  ? 0.1237 0.1953 0.1537 -0.0516 -0.0083 0.0000  50  SER   A N   
403  C  CA  . SER   A 50  ? 0.1203 0.2333 0.2007 -0.0303 0.0097  0.0130  50  SER   A CA  
404  C  C   . SER   A 50  ? 0.1066 0.2037 0.1717 -0.0160 -0.0215 0.0164  50  SER   A C   
405  O  O   . SER   A 50  ? 0.1310 0.2136 0.1676 -0.0163 -0.0185 0.0110  50  SER   A O   
406  C  CB  . SER   A 50  ? 0.1763 0.2611 0.2261 -0.0293 0.0156  0.0014  50  SER   A CB  
407  O  OG  . SER   A 50  ? 0.2138 0.3033 0.2623 -0.0129 0.0348  -0.0121 50  SER   A OG  
408  N  N   . TYR   A 51  ? 0.1037 0.2151 0.1604 -0.0324 -0.0145 0.0102  51  TYR   A N   
409  C  CA  . TYR   A 51  ? 0.1043 0.2063 0.1643 -0.0234 -0.0301 0.0103  51  TYR   A CA  
410  C  C   . TYR   A 51  ? 0.1182 0.2407 0.1794 -0.0175 -0.0341 0.0224  51  TYR   A C   
411  O  O   . TYR   A 51  ? 0.1472 0.2176 0.1800 -0.0174 -0.0530 0.0171  51  TYR   A O   
412  C  CB  . TYR   A 51  ? 0.1176 0.1938 0.1507 -0.0363 -0.0503 0.0060  51  TYR   A CB  
413  C  CG  . TYR   A 51  ? 0.1231 0.1699 0.1277 -0.0359 -0.0435 0.0084  51  TYR   A CG  
414  C  CD1 . TYR   A 51  ? 0.1210 0.1616 0.1562 -0.0327 -0.0364 -0.0022 51  TYR   A CD1 
415  C  CD2 . TYR   A 51  ? 0.1220 0.1568 0.1027 -0.0443 -0.0344 0.0043  51  TYR   A CD2 
416  C  CE1 . TYR   A 51  ? 0.1018 0.1464 0.1392 -0.0430 -0.0315 -0.0037 51  TYR   A CE1 
417  C  CE2 . TYR   A 51  ? 0.1255 0.1379 0.1136 -0.0414 -0.0302 0.0015  51  TYR   A CE2 
418  C  CZ  . TYR   A 51  ? 0.0992 0.1471 0.1147 -0.0438 -0.0203 0.0043  51  TYR   A CZ  
419  O  OH  . TYR   A 51  ? 0.1094 0.1190 0.1290 -0.0363 -0.0208 -0.0094 51  TYR   A OH  
420  N  N   . ASP   A 52  ? 0.1051 0.2921 0.2088 -0.0059 -0.0422 0.0352  52  ASP   A N   
421  C  CA  . ASP   A 52  ? 0.1318 0.3306 0.2234 -0.0189 -0.0607 0.0381  52  ASP   A CA  
422  C  C   . ASP   A 52  ? 0.1140 0.3277 0.2078 -0.0107 -0.0693 0.0394  52  ASP   A C   
423  O  O   . ASP   A 52  ? 0.2068 0.3636 0.2322 -0.0658 -0.1065 0.0264  52  ASP   A O   
424  C  CB  . ASP   A 52  ? 0.1290 0.3968 0.2741 -0.0113 -0.0696 0.0331  52  ASP   A CB  
425  C  CG  . ASP   A 52  ? 0.2387 0.4293 0.3303 0.0180  -0.0237 0.0059  52  ASP   A CG  
426  O  OD1 . ASP   A 52  ? 0.3533 0.5035 0.3994 0.0267  0.0032  -0.0158 52  ASP   A OD1 
427  O  OD2 . ASP   A 52  ? 0.3484 0.4950 0.3589 0.0195  -0.0026 0.0529  52  ASP   A OD2 
428  N  N   . GLN   A 53  ? 0.1326 0.2547 0.1839 0.0259  -0.0341 0.0217  53  GLN   A N   
429  C  CA  . GLN   A 53  ? 0.1533 0.2340 0.2047 0.0358  -0.0278 0.0279  53  GLN   A CA  
430  C  C   . GLN   A 53  ? 0.1549 0.1694 0.1575 0.0316  -0.0301 0.0107  53  GLN   A C   
431  O  O   . GLN   A 53  ? 0.1714 0.1747 0.1988 0.0248  -0.0326 0.0164  53  GLN   A O   
432  C  CB  . GLN   A 53  ? 0.1796 0.2538 0.2648 0.0353  -0.0219 0.0107  53  GLN   A CB  
433  C  CG  . GLN   A 53  ? 0.1918 0.3209 0.3205 0.0312  0.0050  0.0148  53  GLN   A CG  
434  C  CD  . GLN   A 53  ? 0.2600 0.3494 0.3096 0.0461  -0.0033 0.0660  53  GLN   A CD  
435  O  OE1 . GLN   A 53  ? 0.3362 0.4601 0.3541 0.0349  -0.0232 0.1158  53  GLN   A OE1 
436  N  NE2 . GLN   A 53  ? 0.2963 0.3828 0.3827 0.0418  -0.0345 0.0777  53  GLN   A NE2 
437  N  N   . ALA   A 54  ? 0.1414 0.1483 0.1507 0.0138  -0.0318 0.0067  54  ALA   A N   
438  C  CA  . ALA   A 54  ? 0.1571 0.1562 0.1471 0.0187  -0.0364 -0.0054 54  ALA   A CA  
439  C  C   . ALA   A 54  ? 0.1605 0.1660 0.1405 0.0094  -0.0392 -0.0065 54  ALA   A C   
440  O  O   . ALA   A 54  ? 0.1715 0.2426 0.1726 -0.0073 -0.0516 -0.0388 54  ALA   A O   
441  C  CB  . ALA   A 54  ? 0.1720 0.1530 0.1778 0.0301  -0.0255 0.0010  54  ALA   A CB  
442  N  N   . THR   A 55  ? 0.1344 0.1503 0.1400 0.0307  -0.0526 0.0134  55  THR   A N   
443  C  CA  . THR   A 55  ? 0.1598 0.1631 0.1554 0.0472  -0.0546 0.0404  55  THR   A CA  
444  C  C   . THR   A 55  ? 0.1535 0.1327 0.1165 0.0134  -0.0478 0.0298  55  THR   A C   
445  O  O   . THR   A 55  ? 0.1433 0.1220 0.1391 0.0206  -0.0297 0.0207  55  THR   A O   
446  C  CB  . THR   A 55  ? 0.2159 0.2052 0.2623 0.0724  -0.0235 0.0637  55  THR   A CB  
447  O  OG1 . THR   A 55  ? 0.2646 0.2473 0.3468 0.0959  -0.0446 0.0408  55  THR   A OG1 
448  C  CG2 . THR   A 55  ? 0.2457 0.2307 0.2776 0.0705  -0.0117 0.1142  55  THR   A CG2 
449  N  N   . SER   A 56  ? 0.1460 0.1284 0.1246 0.0189  -0.0527 0.0243  56  SER   A N   
450  C  CA  . SER   A 56  ? 0.1605 0.1393 0.1078 0.0158  -0.0516 0.0177  56  SER   A CA  
451  C  C   . SER   A 56  ? 0.1841 0.1287 0.0923 0.0295  -0.0486 0.0193  56  SER   A C   
452  O  O   . SER   A 56  ? 0.2058 0.1564 0.1220 0.0439  -0.0651 0.0305  56  SER   A O   
453  C  CB  . SER   A 56  ? 0.1774 0.1409 0.0950 0.0143  -0.0557 0.0152  56  SER   A CB  
454  O  OG  . SER   A 56  ? 0.1906 0.1432 0.1091 -0.0027 -0.0648 0.0305  56  SER   A OG  
455  N  N   . LEU   A 57  ? 0.1856 0.1210 0.0887 0.0326  -0.0339 0.0243  57  LEU   A N   
456  C  CA  . LEU   A 57  ? 0.2021 0.1355 0.1130 0.0226  -0.0162 0.0247  57  LEU   A CA  
457  C  C   . LEU   A 57  ? 0.1913 0.1169 0.0878 0.0165  -0.0243 0.0300  57  LEU   A C   
458  O  O   . LEU   A 57  ? 0.2086 0.1423 0.0832 0.0289  -0.0373 0.0376  57  LEU   A O   
459  C  CB  . LEU   A 57  ? 0.2469 0.1364 0.1513 -0.0046 -0.0012 0.0404  57  LEU   A CB  
460  C  CG  . LEU   A 57  ? 0.2903 0.1519 0.1924 0.0099  -0.0062 0.0319  57  LEU   A CG  
461  C  CD1 . LEU   A 57  ? 0.2882 0.1884 0.2161 -0.0207 0.0105  0.0209  57  LEU   A CD1 
462  C  CD2 . LEU   A 57  ? 0.3083 0.1636 0.2367 0.0228  -0.0134 0.0509  57  LEU   A CD2 
463  N  N   . ARG   A 58  ? 0.1754 0.1196 0.0839 0.0094  -0.0182 0.0340  58  ARG   A N   
464  C  CA  . ARG   A 58  ? 0.1623 0.1251 0.0824 -0.0020 -0.0267 0.0305  58  ARG   A CA  
465  C  C   . ARG   A 58  ? 0.1577 0.1147 0.0631 0.0010  -0.0216 0.0187  58  ARG   A C   
466  O  O   . ARG   A 58  ? 0.1707 0.1090 0.0673 0.0115  -0.0222 0.0147  58  ARG   A O   
467  C  CB  . ARG   A 58  ? 0.1728 0.1481 0.1106 -0.0011 -0.0175 0.0371  58  ARG   A CB  
468  C  CG  . ARG   A 58  ? 0.1889 0.1604 0.1311 -0.0240 -0.0023 0.0452  58  ARG   A CG  
469  C  CD  . ARG   A 58  ? 0.1871 0.1688 0.1531 -0.0244 0.0067  0.0442  58  ARG   A CD  
470  N  NE  . ARG   A 58  ? 0.1725 0.1624 0.1455 -0.0234 0.0222  0.0357  58  ARG   A NE  
471  C  CZ  . ARG   A 58  ? 0.1695 0.1675 0.1386 -0.0268 0.0237  0.0378  58  ARG   A CZ  
472  N  NH1 . ARG   A 58  ? 0.2016 0.1816 0.1679 -0.0472 0.0378  0.0489  58  ARG   A NH1 
473  N  NH2 . ARG   A 58  ? 0.1663 0.1382 0.1444 -0.0215 0.0333  0.0222  58  ARG   A NH2 
474  N  N   . ILE   A 59  ? 0.1432 0.1119 0.0596 0.0070  -0.0218 0.0232  59  ILE   A N   
475  C  CA  . ILE   A 59  ? 0.1438 0.1115 0.0527 0.0011  -0.0106 0.0242  59  ILE   A CA  
476  C  C   . ILE   A 59  ? 0.1509 0.1103 0.0575 -0.0095 -0.0148 0.0243  59  ILE   A C   
477  O  O   . ILE   A 59  ? 0.1694 0.1470 0.0485 0.0028  -0.0171 0.0265  59  ILE   A O   
478  C  CB  . ILE   A 59  ? 0.1443 0.1020 0.0657 -0.0016 -0.0181 0.0158  59  ILE   A CB  
479  C  CG1 . ILE   A 59  ? 0.1553 0.1139 0.0654 -0.0029 -0.0164 0.0209  59  ILE   A CG1 
480  C  CG2 . ILE   A 59  ? 0.1546 0.1191 0.0697 -0.0036 -0.0290 0.0116  59  ILE   A CG2 
481  C  CD1 . ILE   A 59  ? 0.1581 0.1086 0.0712 0.0000  -0.0246 0.0090  59  ILE   A CD1 
482  N  N   . LEU   A 60  ? 0.1410 0.1099 0.0555 -0.0124 -0.0017 0.0248  60  LEU   A N   
483  C  CA  . LEU   A 60  ? 0.1435 0.1024 0.0616 -0.0078 -0.0157 0.0300  60  LEU   A CA  
484  C  C   . LEU   A 60  ? 0.1425 0.0992 0.0632 -0.0098 -0.0111 0.0221  60  LEU   A C   
485  O  O   . LEU   A 60  ? 0.1446 0.1144 0.0640 -0.0030 0.0017  0.0236  60  LEU   A O   
486  C  CB  . LEU   A 60  ? 0.1459 0.0984 0.1138 -0.0089 -0.0073 0.0194  60  LEU   A CB  
487  C  CG  . LEU   A 60  ? 0.1525 0.0971 0.1059 -0.0115 -0.0062 0.0263  60  LEU   A CG  
488  C  CD1 . LEU   A 60  ? 0.1662 0.1208 0.1174 -0.0184 0.0041  0.0194  60  LEU   A CD1 
489  C  CD2 . LEU   A 60  ? 0.1475 0.1170 0.1196 -0.0157 -0.0162 0.0164  60  LEU   A CD2 
490  N  N   . ASN   A 61  ? 0.1513 0.0950 0.0618 -0.0116 -0.0110 0.0209  61  ASN   A N   
491  C  CA  . ASN   A 61  ? 0.1495 0.1014 0.0584 -0.0227 0.0003  0.0102  61  ASN   A CA  
492  C  C   . ASN   A 61  ? 0.1434 0.0979 0.0625 -0.0182 -0.0026 0.0184  61  ASN   A C   
493  O  O   . ASN   A 61  ? 0.1630 0.1059 0.0742 -0.0250 0.0055  0.0230  61  ASN   A O   
494  C  CB  . ASN   A 61  ? 0.1480 0.1024 0.0681 -0.0242 0.0109  0.0069  61  ASN   A CB  
495  C  CG  . ASN   A 61  ? 0.1298 0.1069 0.0699 -0.0285 0.0063  -0.0007 61  ASN   A CG  
496  O  OD1 . ASN   A 61  ? 0.1342 0.1220 0.0839 -0.0180 -0.0037 0.0079  61  ASN   A OD1 
497  N  ND2 . ASN   A 61  ? 0.1390 0.1095 0.0761 -0.0179 0.0056  0.0015  61  ASN   A ND2 
498  N  N   . ASN   A 62  ? 0.1436 0.0897 0.0651 -0.0350 -0.0009 0.0139  62  ASN   A N   
499  C  CA  . ASN   A 62  ? 0.1565 0.1095 0.0821 -0.0360 -0.0055 0.0124  62  ASN   A CA  
500  C  C   . ASN   A 62  ? 0.1413 0.1251 0.0771 -0.0543 0.0043  0.0097  62  ASN   A C   
501  O  O   . ASN   A 62  ? 0.1469 0.1480 0.1126 -0.0544 -0.0019 0.0057  62  ASN   A O   
502  C  CB  . ASN   A 62  ? 0.1724 0.0985 0.0891 -0.0293 -0.0166 0.0049  62  ASN   A CB  
503  C  CG  . ASN   A 62  ? 0.1721 0.1032 0.0881 -0.0308 -0.0037 0.0036  62  ASN   A CG  
504  O  OD1 . ASN   A 62  ? 0.1480 0.1182 0.0853 -0.0230 0.0025  0.0119  62  ASN   A OD1 
505  N  ND2 . ASN   A 62  ? 0.2169 0.1164 0.1191 -0.0097 0.0232  0.0184  62  ASN   A ND2 
506  N  N   . GLY   A 63  ? 0.1430 0.1331 0.0811 -0.0330 0.0082  0.0119  63  GLY   A N   
507  C  CA  . GLY   A 63  ? 0.1421 0.1378 0.0875 -0.0342 0.0137  0.0127  63  GLY   A CA  
508  C  C   . GLY   A 63  ? 0.1340 0.1213 0.1033 -0.0286 -0.0002 0.0146  63  GLY   A C   
509  O  O   . GLY   A 63  ? 0.1598 0.1353 0.1216 -0.0158 0.0058  0.0143  63  GLY   A O   
510  N  N   . HIS   A 64  ? 0.1153 0.1436 0.0934 -0.0313 -0.0044 0.0279  64  HIS   A N   
511  C  CA  . HIS   A 64  ? 0.1293 0.1461 0.0940 -0.0389 -0.0115 0.0302  64  HIS   A CA  
512  C  C   . HIS   A 64  ? 0.1168 0.1130 0.1129 -0.0320 -0.0070 0.0348  64  HIS   A C   
513  O  O   . HIS   A 64  ? 0.1376 0.1531 0.1893 -0.0224 -0.0233 0.0849  64  HIS   A O   
514  C  CB  . HIS   A 64  ? 0.1308 0.1794 0.0887 -0.0515 -0.0065 0.0255  64  HIS   A CB  
515  C  CG  . HIS   A 64  ? 0.1710 0.2113 0.1119 -0.0587 -0.0058 0.0127  64  HIS   A CG  
516  N  ND1 . HIS   A 64  ? 0.1816 0.2465 0.1296 -0.0515 0.0164  -0.0075 64  HIS   A ND1 
517  C  CD2 . HIS   A 64  ? 0.1984 0.2203 0.1253 -0.0642 -0.0054 0.0143  64  HIS   A CD2 
518  C  CE1 . HIS   A 64  ? 0.1592 0.2446 0.1526 -0.0441 0.0247  0.0109  64  HIS   A CE1 
519  N  NE2 . HIS   A 64  ? 0.1866 0.2188 0.1495 -0.0677 0.0105  0.0205  64  HIS   A NE2 
520  N  N   . ALA   A 65  ? 0.1117 0.1058 0.0966 -0.0220 0.0016  0.0281  65  ALA   A N   
521  C  CA  . ALA   A 65  ? 0.1146 0.1066 0.0726 -0.0235 -0.0086 0.0192  65  ALA   A CA  
522  C  C   . ALA   A 65  ? 0.1261 0.0964 0.0597 -0.0152 -0.0028 0.0105  65  ALA   A C   
523  O  O   . ALA   A 65  ? 0.1464 0.1185 0.0697 -0.0253 -0.0054 0.0216  65  ALA   A O   
524  C  CB  . ALA   A 65  ? 0.1187 0.1195 0.0786 -0.0250 -0.0055 0.0175  65  ALA   A CB  
525  N  N   . PHE   A 66  ? 0.1186 0.1144 0.0572 -0.0049 0.0020  0.0219  66  PHE   A N   
526  C  CA  . PHE   A 66  ? 0.1336 0.1004 0.0561 0.0057  -0.0063 0.0173  66  PHE   A CA  
527  C  C   . PHE   A 66  ? 0.1436 0.0939 0.0596 -0.0012 -0.0019 0.0037  66  PHE   A C   
528  O  O   . PHE   A 66  ? 0.1632 0.0954 0.0562 0.0089  0.0147  0.0091  66  PHE   A O   
529  C  CB  . PHE   A 66  ? 0.1475 0.1310 0.0499 0.0097  -0.0151 0.0045  66  PHE   A CB  
530  C  CG  . PHE   A 66  ? 0.1543 0.1285 0.0453 0.0045  -0.0264 -0.0016 66  PHE   A CG  
531  C  CD1 . PHE   A 66  ? 0.1468 0.1442 0.0609 0.0057  -0.0331 -0.0077 66  PHE   A CD1 
532  C  CD2 . PHE   A 66  ? 0.1588 0.1297 0.0555 0.0111  -0.0262 -0.0179 66  PHE   A CD2 
533  C  CE1 . PHE   A 66  ? 0.1499 0.1500 0.0818 0.0005  -0.0392 -0.0027 66  PHE   A CE1 
534  C  CE2 . PHE   A 66  ? 0.1677 0.1348 0.0712 -0.0095 -0.0339 -0.0177 66  PHE   A CE2 
535  C  CZ  . PHE   A 66  ? 0.1510 0.1412 0.0742 -0.0175 -0.0400 -0.0136 66  PHE   A CZ  
536  N  N   . ASN   A 67  ? 0.1415 0.0906 0.0631 -0.0015 -0.0107 0.0107  67  ASN   A N   
537  C  CA  . ASN   A 67  ? 0.1477 0.0799 0.0642 0.0004  -0.0136 0.0106  67  ASN   A CA  
538  C  C   . ASN   A 67  ? 0.1427 0.0769 0.0599 0.0030  -0.0176 0.0165  67  ASN   A C   
539  O  O   . ASN   A 67  ? 0.1474 0.1083 0.0594 -0.0006 -0.0135 0.0302  67  ASN   A O   
540  C  CB  . ASN   A 67  ? 0.1582 0.0905 0.0740 -0.0131 -0.0155 0.0058  67  ASN   A CB  
541  C  CG  . ASN   A 67  ? 0.1575 0.1178 0.1098 -0.0255 -0.0207 0.0041  67  ASN   A CG  
542  O  OD1 . ASN   A 67  ? 0.1747 0.1593 0.2107 -0.0330 -0.0606 -0.0240 67  ASN   A OD1 
543  N  ND2 . ASN   A 67  ? 0.1529 0.1384 0.0787 -0.0254 -0.0331 0.0234  67  ASN   A ND2 
544  N  N   . VAL   A 68  ? 0.1372 0.0773 0.0645 0.0116  -0.0130 0.0167  68  VAL   A N   
545  C  CA  . VAL   A 68  ? 0.1388 0.0847 0.0508 0.0124  -0.0182 0.0167  68  VAL   A CA  
546  C  C   . VAL   A 68  ? 0.1427 0.0840 0.0606 0.0049  -0.0182 0.0143  68  VAL   A C   
547  O  O   . VAL   A 68  ? 0.1469 0.0914 0.0586 0.0137  -0.0125 0.0157  68  VAL   A O   
548  C  CB  . VAL   A 68  ? 0.1378 0.1032 0.0758 -0.0003 -0.0221 0.0122  68  VAL   A CB  
549  C  CG1 . VAL   A 68  ? 0.1313 0.1267 0.0791 0.0051  -0.0236 0.0075  68  VAL   A CG1 
550  C  CG2 . VAL   A 68  ? 0.1463 0.1166 0.0892 -0.0095 -0.0140 0.0028  68  VAL   A CG2 
551  N  N   . GLU   A 69  ? 0.1544 0.0933 0.0682 0.0094  -0.0132 0.0197  69  GLU   A N   
552  C  CA  . GLU   A 69  ? 0.1480 0.1023 0.0731 0.0045  -0.0114 0.0148  69  GLU   A CA  
553  C  C   . GLU   A 69  ? 0.1452 0.0970 0.0715 0.0102  -0.0233 0.0170  69  GLU   A C   
554  O  O   . GLU   A 69  ? 0.1596 0.1143 0.0947 0.0137  -0.0434 0.0074  69  GLU   A O   
555  C  CB  . GLU   A 69  ? 0.1495 0.1130 0.1108 -0.0015 0.0045  0.0230  69  GLU   A CB  
556  C  CG  . GLU   A 69  ? 0.1544 0.1095 0.1273 -0.0032 0.0176  0.0151  69  GLU   A CG  
557  C  CD  . GLU   A 69  ? 0.1783 0.1279 0.1499 0.0025  0.0173  0.0338  69  GLU   A CD  
558  O  OE1 . GLU   A 69  ? 0.1982 0.1401 0.1618 -0.0011 0.0043  0.0409  69  GLU   A OE1 
559  O  OE2 . GLU   A 69  ? 0.1677 0.1457 0.1905 -0.0062 0.0253  0.0252  69  GLU   A OE2 
560  N  N   . PHE   A 70  ? 0.1415 0.0991 0.0743 0.0104  -0.0233 0.0182  70  PHE   A N   
561  C  CA  . PHE   A 70  ? 0.1410 0.0912 0.0985 0.0155  -0.0233 0.0195  70  PHE   A CA  
562  C  C   . PHE   A 70  ? 0.1537 0.0952 0.1251 0.0147  -0.0286 0.0215  70  PHE   A C   
563  O  O   . PHE   A 70  ? 0.1768 0.0867 0.1587 0.0031  -0.0249 0.0229  70  PHE   A O   
564  C  CB  . PHE   A 70  ? 0.1402 0.1047 0.0933 0.0174  -0.0216 0.0114  70  PHE   A CB  
565  C  CG  . PHE   A 70  ? 0.1370 0.0954 0.0960 0.0264  -0.0202 0.0228  70  PHE   A CG  
566  C  CD1 . PHE   A 70  ? 0.1399 0.1010 0.0925 0.0243  -0.0033 0.0264  70  PHE   A CD1 
567  C  CD2 . PHE   A 70  ? 0.1367 0.1081 0.0974 0.0237  -0.0296 0.0259  70  PHE   A CD2 
568  C  CE1 . PHE   A 70  ? 0.1560 0.0909 0.1118 0.0233  0.0044  0.0310  70  PHE   A CE1 
569  C  CE2 . PHE   A 70  ? 0.1540 0.1156 0.1072 0.0152  -0.0164 0.0282  70  PHE   A CE2 
570  C  CZ  . PHE   A 70  ? 0.1625 0.0928 0.1257 0.0074  -0.0005 0.0203  70  PHE   A CZ  
571  N  N   . ASP   A 71  ? 0.1872 0.0941 0.1683 0.0255  -0.0476 0.0386  71  ASP   A N   
572  C  CA  . ASP   A 71  ? 0.2055 0.0883 0.2213 0.0220  -0.0478 0.0486  71  ASP   A CA  
573  C  C   . ASP   A 71  ? 0.1809 0.0799 0.2581 0.0193  -0.0239 0.0222  71  ASP   A C   
574  O  O   . ASP   A 71  ? 0.2047 0.1062 0.3487 -0.0027 0.0223  -0.0281 71  ASP   A O   
575  C  CB  . ASP   A 71  ? 0.2600 0.1352 0.2613 0.0284  -0.0891 0.0644  71  ASP   A CB  
576  C  CG  . ASP   A 71  ? 0.2999 0.1614 0.3227 0.0280  -0.1060 0.0577  71  ASP   A CG  
577  O  OD1 . ASP   A 71  ? 0.3157 0.1021 0.3331 0.0421  -0.0982 0.0459  71  ASP   A OD1 
578  O  OD2 . ASP   A 71  ? 0.3426 0.2042 0.4510 0.0621  -0.1234 0.0917  71  ASP   A OD2 
579  N  N   . ASP   A 72  ? 0.1769 0.1026 0.2125 0.0137  -0.0220 0.0308  72  ASP   A N   
580  C  CA  . ASP   A 72  ? 0.1783 0.0917 0.2163 -0.0076 -0.0032 0.0264  72  ASP   A CA  
581  C  C   . ASP   A 72  ? 0.2025 0.0980 0.2335 -0.0091 -0.0096 0.0228  72  ASP   A C   
582  O  O   . ASP   A 72  ? 0.2342 0.1077 0.2335 -0.0220 -0.0006 -0.0015 72  ASP   A O   
583  C  CB  . ASP   A 72  ? 0.2007 0.1044 0.1858 0.0030  0.0104  0.0353  72  ASP   A CB  
584  C  CG  . ASP   A 72  ? 0.2018 0.1657 0.1506 0.0101  -0.0122 0.0574  72  ASP   A CG  
585  O  OD1 . ASP   A 72  ? 0.2328 0.2321 0.1806 0.0008  -0.0291 0.0986  72  ASP   A OD1 
586  O  OD2 . ASP   A 72  ? 0.2258 0.2055 0.1257 -0.0020 -0.0173 0.0550  72  ASP   A OD2 
587  N  N   . SER   A 73  ? 0.2219 0.0954 0.2747 -0.0065 -0.0189 0.0411  73  SER   A N   
588  C  CA  . SER   A 73  ? 0.2306 0.1019 0.3006 -0.0159 -0.0040 0.0332  73  SER   A CA  
589  C  C   . SER   A 73  ? 0.2454 0.1016 0.3222 -0.0284 0.0091  0.0000  73  SER   A C   
590  O  O   . SER   A 73  ? 0.2711 0.1048 0.3141 -0.0061 -0.0135 -0.0051 73  SER   A O   
591  C  CB  . SER   A 73  ? 0.2668 0.1137 0.3083 -0.0224 -0.0098 0.0475  73  SER   A CB  
592  O  OG  . SER   A 73  ? 0.2908 0.1347 0.3183 0.0105  -0.0337 0.0341  73  SER   A OG  
593  N  N   . GLN   A 74  ? 0.2422 0.1352 0.3734 -0.0246 0.0313  -0.0075 74  GLN   A N   
594  C  CA  . GLN   A 74  ? 0.2480 0.1609 0.3556 -0.0260 0.0245  -0.0108 74  GLN   A CA  
595  C  C   . GLN   A 74  ? 0.2663 0.1907 0.3275 -0.0288 0.0096  -0.0100 74  GLN   A C   
596  O  O   . GLN   A 74  ? 0.2021 0.2009 0.2370 -0.0477 -0.0454 0.0368  74  GLN   A O   
597  C  CB  . GLN   A 74  ? 0.2595 0.1654 0.3860 -0.0207 0.0114  0.0200  74  GLN   A CB  
598  C  CG  . GLN   A 74  ? 0.3167 0.2638 0.4165 -0.0036 0.0277  0.0590  74  GLN   A CG  
599  C  CD  . GLN   A 74  ? 0.3548 0.3460 0.4492 0.0096  0.0100  0.0511  74  GLN   A CD  
600  O  OE1 . GLN   A 74  ? 0.4018 0.4962 0.5624 0.0365  0.0410  0.0479  74  GLN   A OE1 
601  N  NE2 . GLN   A 74  ? 0.4119 0.3885 0.4469 0.0261  -0.0031 0.0518  74  GLN   A NE2 
602  N  N   . ASP   A 75  ? 0.3274 0.2375 0.3134 -0.0087 0.0086  -0.0061 75  ASP   A N   
603  C  CA  . ASP   A 75  ? 0.3388 0.2034 0.3103 -0.0228 -0.0236 0.0049  75  ASP   A CA  
604  C  C   . ASP   A 75  ? 0.2654 0.2619 0.3023 -0.0261 -0.0640 0.0108  75  ASP   A C   
605  O  O   . ASP   A 75  ? 0.2718 0.1996 0.3538 0.0118  -0.0438 -0.0089 75  ASP   A O   
606  C  CB  . ASP   A 75  ? 0.3875 0.2137 0.3600 0.0017  0.0021  -0.0059 75  ASP   A CB  
607  C  CG  . ASP   A 75  ? 0.4200 0.2392 0.3825 0.0310  0.0170  0.0027  75  ASP   A CG  
608  O  OD1 . ASP   A 75  ? 0.3864 0.2322 0.4284 0.0570  -0.0230 0.0299  75  ASP   A OD1 
609  O  OD2 . ASP   A 75  ? 0.4832 0.2781 0.4530 0.0202  0.0755  -0.0314 75  ASP   A OD2 
610  N  N   . LYS   A 76  ? 0.2519 0.2434 0.2595 0.0031  -0.1154 0.0683  76  LYS   A N   
611  C  CA  . LYS   A 76  ? 0.2850 0.2075 0.2839 -0.0080 -0.0874 0.0478  76  LYS   A CA  
612  C  C   . LYS   A 76  ? 0.2522 0.2192 0.3172 -0.0107 -0.0999 0.0266  76  LYS   A C   
613  O  O   . LYS   A 76  ? 0.3131 0.3325 0.3222 -0.0552 -0.1221 0.0334  76  LYS   A O   
614  C  CB  . LYS   A 76  ? 0.3298 0.1561 0.2426 -0.0331 -0.1310 0.0294  76  LYS   A CB  
615  C  CG  . LYS   A 76  ? 0.4340 0.1827 0.2678 -0.0281 -0.1457 0.0463  76  LYS   A CG  
616  C  CD  . LYS   A 76  ? 0.5439 0.2491 0.2907 -0.0453 -0.1111 0.0410  76  LYS   A CD  
617  C  CE  . LYS   A 76  ? 0.6003 0.3348 0.3045 -0.0279 -0.1227 0.0577  76  LYS   A CE  
618  N  NZ  . LYS   A 76  ? 0.6489 0.3770 0.3286 -0.0400 -0.0956 0.0649  76  LYS   A NZ  
619  N  N   . ALA   A 77  ? 0.2315 0.2128 0.2124 0.0065  -0.0919 0.0279  77  ALA   A N   
620  C  CA  . ALA   A 77  ? 0.1403 0.1588 0.1303 0.0052  -0.0539 0.0182  77  ALA   A CA  
621  C  C   . ALA   A 77  ? 0.1033 0.1424 0.1399 0.0021  -0.0466 0.0159  77  ALA   A C   
622  O  O   . ALA   A 77  ? 0.1056 0.2384 0.1887 -0.0030 -0.0257 -0.0409 77  ALA   A O   
623  C  CB  . ALA   A 77  ? 0.1747 0.1989 0.1348 0.0196  -0.0475 0.0236  77  ALA   A CB  
624  N  N   . VAL   A 78  ? 0.1270 0.1382 0.1182 -0.0138 -0.0363 0.0211  78  VAL   A N   
625  C  CA  . VAL   A 78  ? 0.1569 0.1355 0.1240 -0.0226 -0.0459 0.0292  78  VAL   A CA  
626  C  C   . VAL   A 78  ? 0.1222 0.1334 0.1226 -0.0304 -0.0449 0.0265  78  VAL   A C   
627  O  O   . VAL   A 78  ? 0.1292 0.1628 0.1582 -0.0480 -0.0673 0.0396  78  VAL   A O   
628  C  CB  . VAL   A 78  ? 0.2113 0.1517 0.1629 0.0037  -0.0387 0.0239  78  VAL   A CB  
629  C  CG1 . VAL   A 78  ? 0.2217 0.1461 0.1904 0.0196  -0.0335 0.0321  78  VAL   A CG1 
630  C  CG2 . VAL   A 78  ? 0.2226 0.1642 0.1829 0.0103  -0.0161 0.0172  78  VAL   A CG2 
631  N  N   . LEU   A 79  ? 0.1064 0.1081 0.0996 -0.0263 -0.0261 0.0213  79  LEU   A N   
632  C  CA  . LEU   A 79  ? 0.1065 0.1187 0.1059 -0.0221 -0.0276 0.0206  79  LEU   A CA  
633  C  C   . LEU   A 79  ? 0.1117 0.1066 0.1059 -0.0143 -0.0255 0.0213  79  LEU   A C   
634  O  O   . LEU   A 79  ? 0.1276 0.1220 0.1122 -0.0251 -0.0140 0.0102  79  LEU   A O   
635  C  CB  . LEU   A 79  ? 0.1214 0.1356 0.1222 -0.0224 -0.0201 0.0170  79  LEU   A CB  
636  C  CG  . LEU   A 79  ? 0.1363 0.1366 0.1196 -0.0027 -0.0150 0.0090  79  LEU   A CG  
637  C  CD1 . LEU   A 79  ? 0.1458 0.1386 0.1594 -0.0005 0.0012  0.0271  79  LEU   A CD1 
638  C  CD2 . LEU   A 79  ? 0.1293 0.1343 0.1143 0.0056  -0.0160 -0.0068 79  LEU   A CD2 
639  N  N   . LYS   A 80  ? 0.1129 0.1135 0.1177 -0.0124 -0.0085 0.0130  80  LYS   A N   
640  C  CA  . LYS   A 80  ? 0.1342 0.1245 0.1240 -0.0018 -0.0079 0.0164  80  LYS   A CA  
641  C  C   . LYS   A 80  ? 0.0948 0.1157 0.1295 0.0077  -0.0085 0.0174  80  LYS   A C   
642  O  O   . LYS   A 80  ? 0.1061 0.1210 0.1258 -0.0043 -0.0067 0.0186  80  LYS   A O   
643  C  CB  . LYS   A 80  ? 0.2209 0.1382 0.1487 0.0215  0.0043  0.0150  80  LYS   A CB  
644  C  CG  . LYS   A 80  ? 0.2535 0.1804 0.2108 -0.0004 -0.0034 0.0372  80  LYS   A CG  
645  C  CD  . LYS   A 80  ? 0.2852 0.2580 0.2903 0.0368  -0.0226 0.0264  80  LYS   A CD  
646  C  CE  . LYS   A 80  ? 0.3582 0.2916 0.3384 0.0572  -0.0181 0.0205  80  LYS   A CE  
647  N  NZ  . LYS   A 80  ? 0.4089 0.3206 0.4106 0.0611  -0.0230 0.0397  80  LYS   A NZ  
648  N  N   . GLY   A 81  ? 0.1165 0.1140 0.1256 0.0084  -0.0044 0.0218  81  GLY   A N   
649  C  CA  . GLY   A 81  ? 0.1117 0.1346 0.1336 0.0149  0.0129  0.0380  81  GLY   A CA  
650  C  C   . GLY   A 81  ? 0.0909 0.1261 0.1264 0.0160  0.0142  0.0198  81  GLY   A C   
651  O  O   . GLY   A 81  ? 0.1010 0.1306 0.1130 0.0026  0.0114  0.0103  81  GLY   A O   
652  N  N   . GLY   A 82  ? 0.0929 0.1322 0.1350 0.0190  0.0146  0.0355  82  GLY   A N   
653  C  CA  . GLY   A 82  ? 0.1128 0.1253 0.1287 0.0201  0.0178  0.0265  82  GLY   A CA  
654  C  C   . GLY   A 82  ? 0.1128 0.1171 0.1371 0.0204  0.0158  0.0241  82  GLY   A C   
655  O  O   . GLY   A 82  ? 0.1223 0.1595 0.1467 0.0375  0.0237  -0.0016 82  GLY   A O   
656  N  N   . PRO   A 83  ? 0.1064 0.1191 0.1210 0.0230  0.0167  0.0146  83  PRO   A N   
657  C  CA  . PRO   A 83  ? 0.1209 0.1326 0.1284 0.0204  0.0007  0.0107  83  PRO   A CA  
658  C  C   . PRO   A 83  ? 0.1153 0.1373 0.1320 0.0046  -0.0068 0.0039  83  PRO   A C   
659  O  O   . PRO   A 83  ? 0.1644 0.1839 0.1663 -0.0232 -0.0384 0.0206  83  PRO   A O   
660  C  CB  . PRO   A 83  ? 0.1126 0.1343 0.1491 0.0221  0.0022  0.0261  83  PRO   A CB  
661  C  CG  . PRO   A 83  ? 0.1024 0.1239 0.1449 0.0261  0.0164  0.0250  83  PRO   A CG  
662  C  CD  . PRO   A 83  ? 0.0993 0.1172 0.1381 0.0211  0.0222  0.0190  83  PRO   A CD  
663  N  N   . LEU   A 84  ? 0.1052 0.1091 0.1142 0.0114  0.0029  -0.0019 84  LEU   A N   
664  C  CA  . LEU   A 84  ? 0.1068 0.0991 0.1244 0.0119  -0.0044 -0.0041 84  LEU   A CA  
665  C  C   . LEU   A 84  ? 0.1318 0.1092 0.1386 0.0170  0.0041  -0.0247 84  LEU   A C   
666  O  O   . LEU   A 84  ? 0.1239 0.1355 0.1790 0.0313  0.0203  -0.0287 84  LEU   A O   
667  C  CB  . LEU   A 84  ? 0.0917 0.0880 0.1109 0.0149  0.0130  0.0034  84  LEU   A CB  
668  C  CG  . LEU   A 84  ? 0.0938 0.0848 0.1060 0.0082  0.0130  0.0092  84  LEU   A CG  
669  C  CD1 . LEU   A 84  ? 0.1081 0.0928 0.1197 0.0119  0.0005  0.0032  84  LEU   A CD1 
670  C  CD2 . LEU   A 84  ? 0.1007 0.0871 0.1066 0.0108  0.0096  -0.0018 84  LEU   A CD2 
671  N  N   . ASP   A 85  ? 0.1577 0.1135 0.1458 0.0158  0.0070  -0.0332 85  ASP   A N   
672  C  CA  . ASP   A 85  ? 0.2104 0.1171 0.1767 0.0050  0.0313  -0.0446 85  ASP   A CA  
673  C  C   . ASP   A 85  ? 0.2136 0.1157 0.1973 0.0138  0.0500  -0.0149 85  ASP   A C   
674  O  O   . ASP   A 85  ? 0.2234 0.1522 0.2151 0.0332  0.0515  0.0062  85  ASP   A O   
675  C  CB  . ASP   A 85  ? 0.2608 0.1508 0.2157 -0.0121 0.0278  -0.0723 85  ASP   A CB  
676  C  CG  . ASP   A 85  ? 0.2731 0.2540 0.2651 -0.0292 0.0208  -0.0494 85  ASP   A CG  
677  O  OD1 . ASP   A 85  ? 0.3180 0.3288 0.3540 -0.0531 0.0370  -0.0406 85  ASP   A OD1 
678  O  OD2 . ASP   A 85  ? 0.2845 0.3562 0.3263 -0.0416 -0.0038 -0.0458 85  ASP   A OD2 
679  N  N   . GLY   A 86  ? 0.2381 0.1655 0.1883 -0.0045 0.0135  -0.0039 86  GLY   A N   
680  C  CA  . GLY   A 86  ? 0.2538 0.1368 0.1962 -0.0088 0.0063  -0.0134 86  GLY   A CA  
681  C  C   . GLY   A 86  ? 0.2233 0.1309 0.1740 -0.0166 -0.0053 -0.0070 86  GLY   A C   
682  O  O   . GLY   A 86  ? 0.2587 0.1802 0.1998 -0.0670 0.0019  0.0017  86  GLY   A O   
683  N  N   A THR   A 87  ? 0.1835 0.0931 0.1622 -0.0075 -0.0040 -0.0163 87  THR   A N   
684  N  N   B THR   A 87  ? 0.1684 0.0976 0.1550 0.0012  -0.0073 -0.0142 87  THR   A N   
685  C  CA  A THR   A 87  ? 0.1589 0.0942 0.1646 -0.0041 -0.0046 -0.0088 87  THR   A CA  
686  C  CA  B THR   A 87  ? 0.1259 0.0990 0.1533 0.0128  -0.0094 -0.0042 87  THR   A CA  
687  C  C   A THR   A 87  ? 0.1255 0.0805 0.1381 0.0003  -0.0176 0.0012  87  THR   A C   
688  C  C   B THR   A 87  ? 0.1042 0.0803 0.1316 0.0067  -0.0168 0.0032  87  THR   A C   
689  O  O   A THR   A 87  ? 0.1431 0.0690 0.1377 0.0060  -0.0231 0.0058  87  THR   A O   
690  O  O   B THR   A 87  ? 0.1186 0.0762 0.1385 0.0058  -0.0171 0.0065  87  THR   A O   
691  C  CB  A THR   A 87  ? 0.1678 0.1246 0.1924 0.0109  -0.0018 -0.0054 87  THR   A CB  
692  C  CB  B THR   A 87  ? 0.1117 0.1143 0.1673 0.0330  -0.0024 -0.0049 87  THR   A CB  
693  O  OG1 A THR   A 87  ? 0.1961 0.1448 0.2058 0.0077  -0.0009 0.0192  87  THR   A OG1 
694  O  OG1 B THR   A 87  ? 0.1117 0.1506 0.2065 0.0474  0.0118  -0.0162 87  THR   A OG1 
695  C  CG2 A THR   A 87  ? 0.1710 0.1154 0.2102 0.0202  0.0059  -0.0046 87  THR   A CG2 
696  C  CG2 B THR   A 87  ? 0.1152 0.1143 0.1623 0.0457  -0.0037 -0.0013 87  THR   A CG2 
697  N  N   . TYR   A 88  ? 0.0935 0.0749 0.1204 -0.0020 -0.0148 0.0039  88  TYR   A N   
698  C  CA  . TYR   A 88  ? 0.0972 0.0816 0.1072 -0.0036 -0.0160 0.0050  88  TYR   A CA  
699  C  C   . TYR   A 88  ? 0.1015 0.0768 0.1047 -0.0048 -0.0221 0.0090  88  TYR   A C   
700  O  O   . TYR   A 88  ? 0.1336 0.1258 0.1155 -0.0388 -0.0299 0.0201  88  TYR   A O   
701  C  CB  . TYR   A 88  ? 0.0930 0.0850 0.1022 0.0078  -0.0142 -0.0036 88  TYR   A CB  
702  C  CG  . TYR   A 88  ? 0.0884 0.0605 0.0922 0.0014  -0.0095 0.0050  88  TYR   A CG  
703  C  CD1 . TYR   A 88  ? 0.0781 0.0816 0.0996 0.0078  0.0002  0.0017  88  TYR   A CD1 
704  C  CD2 . TYR   A 88  ? 0.0946 0.0528 0.0811 0.0096  -0.0013 -0.0012 88  TYR   A CD2 
705  C  CE1 . TYR   A 88  ? 0.0866 0.0769 0.0937 0.0100  0.0037  -0.0087 88  TYR   A CE1 
706  C  CE2 . TYR   A 88  ? 0.0882 0.0677 0.0891 0.0039  -0.0036 0.0020  88  TYR   A CE2 
707  C  CZ  . TYR   A 88  ? 0.0810 0.0614 0.0793 -0.0046 -0.0006 -0.0067 88  TYR   A CZ  
708  O  OH  . TYR   A 88  ? 0.0832 0.0792 0.0857 -0.0004 -0.0067 -0.0093 88  TYR   A OH  
709  N  N   . ARG   A 89  ? 0.0901 0.0612 0.0931 0.0039  -0.0220 0.0001  89  ARG   A N   
710  C  CA  . ARG   A 89  ? 0.1063 0.0592 0.0908 0.0070  -0.0236 0.0125  89  ARG   A CA  
711  C  C   . ARG   A 89  ? 0.0944 0.0639 0.0721 0.0025  -0.0181 0.0146  89  ARG   A C   
712  O  O   . ARG   A 89  ? 0.0938 0.0702 0.0839 -0.0038 -0.0060 0.0135  89  ARG   A O   
713  C  CB  . ARG   A 89  ? 0.1376 0.0657 0.1207 0.0013  -0.0254 0.0223  89  ARG   A CB  
714  C  CG  . ARG   A 89  ? 0.1815 0.0860 0.1290 0.0010  -0.0270 0.0110  89  ARG   A CG  
715  C  CD  . ARG   A 89  ? 0.2091 0.1035 0.1447 0.0043  -0.0230 0.0210  89  ARG   A CD  
716  N  NE  . ARG   A 89  ? 0.2477 0.1311 0.1639 -0.0096 -0.0134 0.0313  89  ARG   A NE  
717  C  CZ  . ARG   A 89  ? 0.2549 0.1325 0.1711 -0.0030 -0.0151 0.0144  89  ARG   A CZ  
718  N  NH1 . ARG   A 89  ? 0.2691 0.1060 0.2107 0.0080  -0.0040 0.0383  89  ARG   A NH1 
719  N  NH2 . ARG   A 89  ? 0.2607 0.1352 0.1611 0.0042  -0.0207 0.0135  89  ARG   A NH2 
720  N  N   . LEU   A 90  ? 0.0985 0.0761 0.0791 0.0005  -0.0191 0.0111  90  LEU   A N   
721  C  CA  . LEU   A 90  ? 0.1089 0.0802 0.0662 -0.0023 -0.0261 0.0126  90  LEU   A CA  
722  C  C   . LEU   A 90  ? 0.1069 0.0879 0.0623 0.0016  -0.0237 0.0149  90  LEU   A C   
723  O  O   . LEU   A 90  ? 0.1169 0.1134 0.0973 0.0079  -0.0235 0.0417  90  LEU   A O   
724  C  CB  . LEU   A 90  ? 0.1113 0.0877 0.0750 -0.0061 -0.0211 0.0053  90  LEU   A CB  
725  C  CG  . LEU   A 90  ? 0.1297 0.0929 0.0801 -0.0125 -0.0193 -0.0007 90  LEU   A CG  
726  C  CD1 . LEU   A 90  ? 0.1458 0.0863 0.0864 -0.0117 -0.0143 -0.0051 90  LEU   A CD1 
727  C  CD2 . LEU   A 90  ? 0.1348 0.1187 0.0914 -0.0200 -0.0235 -0.0065 90  LEU   A CD2 
728  N  N   . ILE   A 91  ? 0.1181 0.0639 0.0673 0.0035  -0.0059 0.0089  91  ILE   A N   
729  C  CA  . ILE   A 91  ? 0.1248 0.0653 0.0695 0.0000  -0.0099 0.0113  91  ILE   A CA  
730  C  C   . ILE   A 91  ? 0.1215 0.0565 0.0614 0.0028  -0.0159 0.0126  91  ILE   A C   
731  O  O   . ILE   A 91  ? 0.1266 0.0677 0.0641 0.0000  -0.0091 0.0151  91  ILE   A O   
732  C  CB  . ILE   A 91  ? 0.1247 0.0797 0.0675 -0.0024 -0.0092 0.0042  91  ILE   A CB  
733  C  CG1 . ILE   A 91  ? 0.1546 0.1145 0.0834 -0.0225 -0.0032 0.0044  91  ILE   A CG1 
734  C  CG2 . ILE   A 91  ? 0.1147 0.0859 0.0740 -0.0052 -0.0164 -0.0058 91  ILE   A CG2 
735  C  CD1 . ILE   A 91  ? 0.1669 0.1312 0.1096 -0.0346 0.0001  0.0012  91  ILE   A CD1 
736  N  N   . GLN   A 92  ? 0.1179 0.0548 0.0590 -0.0004 -0.0130 0.0128  92  GLN   A N   
737  C  CA  . GLN   A 92  ? 0.1182 0.0587 0.0544 -0.0012 -0.0131 0.0171  92  GLN   A CA  
738  C  C   . GLN   A 92  ? 0.1117 0.0568 0.0512 0.0007  -0.0166 0.0140  92  GLN   A C   
739  O  O   . GLN   A 92  ? 0.1226 0.0592 0.0532 0.0000  -0.0103 0.0089  92  GLN   A O   
740  C  CB  . GLN   A 92  ? 0.1301 0.0635 0.0784 -0.0031 -0.0110 0.0184  92  GLN   A CB  
741  C  CG  . GLN   A 92  ? 0.1288 0.0695 0.0892 -0.0100 -0.0128 0.0093  92  GLN   A CG  
742  C  CD  . GLN   A 92  ? 0.1143 0.0779 0.0954 -0.0095 -0.0127 0.0105  92  GLN   A CD  
743  O  OE1 . GLN   A 92  ? 0.1223 0.0675 0.1016 -0.0014 -0.0143 0.0144  92  GLN   A OE1 
744  N  NE2 . GLN   A 92  ? 0.1247 0.1037 0.1878 -0.0063 -0.0145 0.0089  92  GLN   A NE2 
745  N  N   . PHE   A 93  ? 0.1157 0.0546 0.0546 0.0061  -0.0164 0.0090  93  PHE   A N   
746  C  CA  . PHE   A 93  ? 0.1070 0.0605 0.0467 0.0018  -0.0197 0.0070  93  PHE   A CA  
747  C  C   . PHE   A 93  ? 0.1035 0.0597 0.0480 -0.0040 -0.0188 0.0076  93  PHE   A C   
748  O  O   . PHE   A 93  ? 0.1244 0.0718 0.0485 0.0046  -0.0105 0.0098  93  PHE   A O   
749  C  CB  . PHE   A 93  ? 0.1051 0.0722 0.0566 0.0046  -0.0208 0.0070  93  PHE   A CB  
750  C  CG  . PHE   A 93  ? 0.1058 0.0766 0.0619 0.0034  -0.0277 0.0066  93  PHE   A CG  
751  C  CD1 . PHE   A 93  ? 0.1158 0.0818 0.0637 0.0048  -0.0276 0.0065  93  PHE   A CD1 
752  C  CD2 . PHE   A 93  ? 0.1102 0.0888 0.0674 0.0101  -0.0277 0.0087  93  PHE   A CD2 
753  C  CE1 . PHE   A 93  ? 0.1189 0.0836 0.0707 0.0066  -0.0296 0.0037  93  PHE   A CE1 
754  C  CE2 . PHE   A 93  ? 0.1124 0.0947 0.0743 0.0138  -0.0393 0.0102  93  PHE   A CE2 
755  C  CZ  . PHE   A 93  ? 0.1239 0.1063 0.0609 0.0091  -0.0406 0.0111  93  PHE   A CZ  
756  N  N   . HIS   A 94  ? 0.1015 0.0556 0.0434 0.0025  -0.0075 0.0062  94  HIS   A N   
757  C  CA  . HIS   A 94  ? 0.1007 0.0619 0.0439 0.0023  -0.0098 0.0026  94  HIS   A CA  
758  C  C   . HIS   A 94  ? 0.0846 0.0584 0.0454 -0.0020 -0.0089 -0.0002 94  HIS   A C   
759  O  O   . HIS   A 94  ? 0.0937 0.0611 0.0502 0.0042  0.0012  0.0044  94  HIS   A O   
760  C  CB  . HIS   A 94  ? 0.1026 0.0596 0.0608 0.0016  -0.0043 0.0021  94  HIS   A CB  
761  C  CG  . HIS   A 94  ? 0.0848 0.0604 0.0625 -0.0103 0.0021  0.0070  94  HIS   A CG  
762  N  ND1 . HIS   A 94  ? 0.0837 0.0584 0.0740 -0.0100 -0.0016 0.0046  94  HIS   A ND1 
763  C  CD2 . HIS   A 94  ? 0.0724 0.0610 0.0675 -0.0063 0.0012  0.0028  94  HIS   A CD2 
764  C  CE1 . HIS   A 94  ? 0.0795 0.0504 0.0717 -0.0149 -0.0027 -0.0045 94  HIS   A CE1 
765  N  NE2 . HIS   A 94  ? 0.0715 0.0616 0.0747 -0.0145 0.0015  -0.0072 94  HIS   A NE2 
766  N  N   . PHE   A 95  ? 0.0834 0.0596 0.0435 -0.0019 -0.0074 0.0036  95  PHE   A N   
767  C  CA  . PHE   A 95  ? 0.0848 0.0580 0.0449 -0.0023 -0.0129 -0.0002 95  PHE   A CA  
768  C  C   . PHE   A 95  ? 0.0807 0.0577 0.0464 -0.0025 -0.0075 -0.0073 95  PHE   A C   
769  O  O   . PHE   A 95  ? 0.0935 0.0715 0.0623 -0.0026 -0.0035 0.0024  95  PHE   A O   
770  C  CB  . PHE   A 95  ? 0.0862 0.0623 0.0531 -0.0049 -0.0141 -0.0016 95  PHE   A CB  
771  C  CG  . PHE   A 95  ? 0.0856 0.0601 0.0551 -0.0031 -0.0231 -0.0097 95  PHE   A CG  
772  C  CD1 . PHE   A 95  ? 0.0993 0.0707 0.0593 0.0002  -0.0256 -0.0045 95  PHE   A CD1 
773  C  CD2 . PHE   A 95  ? 0.0925 0.0687 0.0695 -0.0048 -0.0211 -0.0029 95  PHE   A CD2 
774  C  CE1 . PHE   A 95  ? 0.1054 0.0901 0.0662 0.0044  -0.0410 -0.0075 95  PHE   A CE1 
775  C  CE2 . PHE   A 95  ? 0.0949 0.0832 0.0786 -0.0088 -0.0285 -0.0156 95  PHE   A CE2 
776  C  CZ  . PHE   A 95  ? 0.0901 0.0969 0.0784 0.0005  -0.0348 -0.0137 95  PHE   A CZ  
777  N  N   . HIS   A 96  ? 0.0684 0.0653 0.0502 -0.0038 -0.0084 0.0017  96  HIS   A N   
778  C  CA  . HIS   A 96  ? 0.0664 0.0646 0.0496 -0.0034 -0.0052 0.0006  96  HIS   A CA  
779  C  C   . HIS   A 96  ? 0.0763 0.0607 0.0514 -0.0033 -0.0059 -0.0049 96  HIS   A C   
780  O  O   . HIS   A 96  ? 0.0705 0.0631 0.0636 -0.0013 0.0025  -0.0003 96  HIS   A O   
781  C  CB  . HIS   A 96  ? 0.0676 0.0668 0.0592 -0.0011 -0.0105 -0.0036 96  HIS   A CB  
782  C  CG  . HIS   A 96  ? 0.0663 0.0731 0.0599 -0.0030 -0.0109 -0.0040 96  HIS   A CG  
783  N  ND1 . HIS   A 96  ? 0.0694 0.0751 0.0976 -0.0001 -0.0045 -0.0085 96  HIS   A ND1 
784  C  CD2 . HIS   A 96  ? 0.0630 0.0747 0.0610 -0.0082 -0.0084 -0.0079 96  HIS   A CD2 
785  C  CE1 . HIS   A 96  ? 0.0641 0.0622 0.0822 -0.0069 -0.0013 -0.0081 96  HIS   A CE1 
786  N  NE2 . HIS   A 96  ? 0.0628 0.0662 0.0576 -0.0074 0.0005  -0.0103 96  HIS   A NE2 
787  N  N   . TRP   A 97  ? 0.0760 0.0582 0.0549 -0.0026 -0.0006 -0.0060 97  TRP   A N   
788  C  CA  . TRP   A 97  ? 0.0857 0.0640 0.0561 -0.0063 -0.0022 -0.0086 97  TRP   A CA  
789  C  C   . TRP   A 97  ? 0.0836 0.0660 0.0519 -0.0002 -0.0037 -0.0090 97  TRP   A C   
790  O  O   . TRP   A 97  ? 0.0877 0.0746 0.0650 -0.0003 0.0054  -0.0078 97  TRP   A O   
791  C  CB  . TRP   A 97  ? 0.0917 0.0641 0.0601 -0.0095 -0.0076 -0.0068 97  TRP   A CB  
792  C  CG  . TRP   A 97  ? 0.0946 0.0655 0.0571 -0.0080 -0.0074 -0.0127 97  TRP   A CG  
793  C  CD1 . TRP   A 97  ? 0.1006 0.0718 0.0650 -0.0118 -0.0051 -0.0137 97  TRP   A CD1 
794  C  CD2 . TRP   A 97  ? 0.0889 0.0710 0.0555 -0.0073 -0.0084 -0.0025 97  TRP   A CD2 
795  N  NE1 . TRP   A 97  ? 0.1166 0.0788 0.0612 -0.0015 0.0009  -0.0103 97  TRP   A NE1 
796  C  CE2 . TRP   A 97  ? 0.0916 0.0653 0.0572 -0.0143 -0.0007 -0.0090 97  TRP   A CE2 
797  C  CE3 . TRP   A 97  ? 0.0803 0.0730 0.0548 -0.0002 -0.0063 0.0000  97  TRP   A CE3 
798  C  CZ2 . TRP   A 97  ? 0.0990 0.0800 0.0573 -0.0069 0.0022  -0.0015 97  TRP   A CZ2 
799  C  CZ3 . TRP   A 97  ? 0.0856 0.0739 0.0577 -0.0074 -0.0041 0.0000  97  TRP   A CZ3 
800  C  CH2 . TRP   A 97  ? 0.0916 0.0719 0.0645 -0.0113 -0.0019 0.0064  97  TRP   A CH2 
801  N  N   . GLY   A 98  ? 0.0977 0.0631 0.0658 -0.0015 -0.0019 -0.0062 98  GLY   A N   
802  C  CA  . GLY   A 98  ? 0.1061 0.0692 0.0684 0.0023  0.0005  -0.0020 98  GLY   A CA  
803  C  C   . GLY   A 98  ? 0.1186 0.0751 0.0750 -0.0012 0.0002  -0.0058 98  GLY   A C   
804  O  O   . GLY   A 98  ? 0.1244 0.0777 0.0761 -0.0031 0.0019  -0.0141 98  GLY   A O   
805  N  N   . SER   A 99  ? 0.1272 0.0723 0.0782 0.0010  -0.0008 -0.0123 99  SER   A N   
806  C  CA  . SER   A 99  ? 0.1473 0.0856 0.0963 0.0039  0.0042  -0.0270 99  SER   A CA  
807  C  C   . SER   A 99  ? 0.1456 0.0721 0.1091 0.0087  0.0045  -0.0294 99  SER   A C   
808  O  O   . SER   A 99  ? 0.1859 0.1032 0.1159 -0.0041 0.0065  -0.0402 99  SER   A O   
809  C  CB  . SER   A 99  ? 0.1474 0.0955 0.1164 0.0009  0.0150  -0.0312 99  SER   A CB  
810  O  OG  . SER   A 99  ? 0.1379 0.0906 0.1603 0.0119  0.0046  -0.0233 99  SER   A OG  
811  N  N   . LEU   A 100 ? 0.1328 0.0690 0.1188 0.0087  0.0122  -0.0244 100 LEU   A N   
812  C  CA  . LEU   A 100 ? 0.1509 0.0699 0.1430 0.0095  0.0181  -0.0161 100 LEU   A CA  
813  C  C   . LEU   A 100 ? 0.1347 0.0644 0.1117 0.0023  0.0004  -0.0110 100 LEU   A C   
814  O  O   . LEU   A 100 ? 0.1415 0.0642 0.1143 -0.0043 0.0035  -0.0170 100 LEU   A O   
815  C  CB  . LEU   A 100 ? 0.1857 0.1025 0.1828 0.0241  0.0278  -0.0109 100 LEU   A CB  
816  C  CG  . LEU   A 100 ? 0.2052 0.1238 0.2205 0.0385  0.0303  -0.0225 100 LEU   A CG  
817  C  CD1 . LEU   A 100 ? 0.2036 0.1738 0.2621 0.0549  0.0145  -0.0206 100 LEU   A CD1 
818  C  CD2 . LEU   A 100 ? 0.2350 0.1720 0.2397 0.0172  0.0408  -0.0447 100 LEU   A CD2 
819  N  N   . ASP   A 101 ? 0.1335 0.0709 0.1332 -0.0032 -0.0073 -0.0106 101 ASP   A N   
820  C  CA  . ASP   A 101 ? 0.1476 0.0686 0.1325 -0.0035 0.0015  0.0122  101 ASP   A CA  
821  C  C   . ASP   A 101 ? 0.1528 0.0763 0.1340 -0.0043 0.0064  0.0077  101 ASP   A C   
822  O  O   . ASP   A 101 ? 0.1745 0.1119 0.1368 0.0076  0.0231  0.0138  101 ASP   A O   
823  C  CB  . ASP   A 101 ? 0.1505 0.0878 0.1401 -0.0189 0.0028  0.0196  101 ASP   A CB  
824  C  CG  . ASP   A 101 ? 0.1525 0.1009 0.1575 -0.0282 -0.0175 0.0154  101 ASP   A CG  
825  O  OD1 . ASP   A 101 ? 0.1575 0.1155 0.1323 -0.0229 -0.0131 0.0133  101 ASP   A OD1 
826  O  OD2 . ASP   A 101 ? 0.2151 0.1455 0.2019 -0.0719 -0.0272 0.0044  101 ASP   A OD2 
827  N  N   . GLY   A 102 ? 0.1581 0.0708 0.1343 -0.0143 -0.0075 0.0082  102 GLY   A N   
828  C  CA  . GLY   A 102 ? 0.1679 0.0909 0.1393 -0.0097 -0.0059 0.0199  102 GLY   A CA  
829  C  C   . GLY   A 102 ? 0.1356 0.0920 0.1059 -0.0021 -0.0029 0.0118  102 GLY   A C   
830  O  O   . GLY   A 102 ? 0.1615 0.1099 0.1078 -0.0096 0.0019  0.0256  102 GLY   A O   
831  N  N   . GLN   A 103 ? 0.1263 0.0920 0.0896 -0.0089 0.0022  0.0066  103 GLN   A N   
832  C  CA  . GLN   A 103 ? 0.1140 0.0802 0.0837 0.0024  0.0093  0.0000  103 GLN   A CA  
833  C  C   . GLN   A 103 ? 0.0953 0.0720 0.0805 -0.0048 0.0054  -0.0049 103 GLN   A C   
834  O  O   . GLN   A 103 ? 0.1102 0.0752 0.0877 -0.0090 0.0032  -0.0110 103 GLN   A O   
835  C  CB  . GLN   A 103 ? 0.1183 0.0816 0.1118 0.0149  0.0115  0.0044  103 GLN   A CB  
836  C  CG  . GLN   A 103 ? 0.1281 0.0993 0.1331 0.0224  0.0331  0.0086  103 GLN   A CG  
837  C  CD  . GLN   A 103 ? 0.1573 0.1254 0.1729 0.0510  0.0400  0.0339  103 GLN   A CD  
838  O  OE1 . GLN   A 103 ? 0.2167 0.1572 0.2746 0.0726  0.0549  0.0829  103 GLN   A OE1 
839  N  NE2 . GLN   A 103 ? 0.1662 0.1098 0.1642 0.0536  0.0432  0.0300  103 GLN   A NE2 
840  N  N   . GLY   A 104 ? 0.0827 0.0706 0.0707 0.0017  0.0035  -0.0132 104 GLY   A N   
841  C  CA  . GLY   A 104 ? 0.0815 0.0653 0.0708 -0.0104 0.0019  -0.0066 104 GLY   A CA  
842  C  C   . GLY   A 104 ? 0.0773 0.0651 0.0684 -0.0040 -0.0013 -0.0037 104 GLY   A C   
843  O  O   . GLY   A 104 ? 0.0778 0.0745 0.0776 -0.0055 0.0024  -0.0034 104 GLY   A O   
844  N  N   . SER   A 105 ? 0.0752 0.0564 0.0645 -0.0037 -0.0001 -0.0082 105 SER   A N   
845  C  CA  . SER   A 105 ? 0.0737 0.0532 0.0648 0.0011  -0.0051 -0.0065 105 SER   A CA  
846  C  C   . SER   A 105 ? 0.0698 0.0584 0.0600 -0.0018 -0.0023 -0.0019 105 SER   A C   
847  O  O   . SER   A 105 ? 0.0806 0.0673 0.0782 0.0056  -0.0108 -0.0072 105 SER   A O   
848  C  CB  . SER   A 105 ? 0.0742 0.0612 0.0657 0.0016  -0.0049 -0.0020 105 SER   A CB  
849  O  OG  . SER   A 105 ? 0.0833 0.0659 0.0695 0.0060  0.0011  0.0059  105 SER   A OG  
850  N  N   . GLU   A 106 ? 0.0693 0.0603 0.0556 -0.0005 -0.0078 -0.0026 106 GLU   A N   
851  C  CA  . GLU   A 106 ? 0.0706 0.0685 0.0539 0.0032  -0.0114 -0.0029 106 GLU   A CA  
852  C  C   . GLU   A 106 ? 0.0678 0.0624 0.0516 0.0001  -0.0148 0.0006  106 GLU   A C   
853  O  O   . GLU   A 106 ? 0.0787 0.0697 0.0588 0.0098  -0.0132 0.0020  106 GLU   A O   
854  C  CB  . GLU   A 106 ? 0.0698 0.0696 0.0551 -0.0038 -0.0070 0.0008  106 GLU   A CB  
855  C  CG  . GLU   A 106 ? 0.0932 0.0739 0.0655 -0.0043 0.0035  -0.0035 106 GLU   A CG  
856  C  CD  . GLU   A 106 ? 0.0643 0.0733 0.0605 -0.0010 0.0005  -0.0006 106 GLU   A CD  
857  O  OE1 . GLU   A 106 ? 0.0575 0.0714 0.0809 -0.0067 0.0027  -0.0061 106 GLU   A OE1 
858  O  OE2 . GLU   A 106 ? 0.0692 0.0804 0.0904 0.0028  0.0028  0.0021  106 GLU   A OE2 
859  N  N   . HIS   A 107 ? 0.0673 0.0649 0.0468 0.0043  -0.0083 0.0073  107 HIS   A N   
860  C  CA  . HIS   A 107 ? 0.0726 0.0611 0.0504 0.0030  -0.0126 0.0043  107 HIS   A CA  
861  C  C   . HIS   A 107 ? 0.0672 0.0642 0.0536 0.0090  -0.0072 0.0027  107 HIS   A C   
862  O  O   . HIS   A 107 ? 0.0755 0.0579 0.0626 -0.0033 -0.0079 0.0000  107 HIS   A O   
863  C  CB  . HIS   A 107 ? 0.0620 0.0691 0.0551 0.0019  -0.0118 0.0010  107 HIS   A CB  
864  C  CG  . HIS   A 107 ? 0.0589 0.0671 0.0536 0.0064  -0.0132 0.0010  107 HIS   A CG  
865  N  ND1 . HIS   A 107 ? 0.0633 0.0591 0.0589 0.0076  -0.0159 -0.0005 107 HIS   A ND1 
866  C  CD2 . HIS   A 107 ? 0.0571 0.0693 0.0491 0.0147  -0.0073 -0.0046 107 HIS   A CD2 
867  C  CE1 . HIS   A 107 ? 0.0676 0.0596 0.0577 0.0089  -0.0155 -0.0034 107 HIS   A CE1 
868  N  NE2 . HIS   A 107 ? 0.0685 0.0629 0.0549 0.0091  -0.0138 -0.0051 107 HIS   A NE2 
869  N  N   . THR   A 108 ? 0.0906 0.0639 0.0574 0.0050  -0.0057 0.0070  108 THR   A N   
870  C  CA  . THR   A 108 ? 0.0969 0.0598 0.0622 0.0061  -0.0084 0.0092  108 THR   A CA  
871  C  C   . THR   A 108 ? 0.0883 0.0625 0.0574 0.0104  -0.0171 0.0082  108 THR   A C   
872  O  O   . THR   A 108 ? 0.0869 0.0722 0.0649 0.0016  -0.0040 0.0048  108 THR   A O   
873  C  CB  . THR   A 108 ? 0.1043 0.0727 0.0686 0.0135  -0.0063 0.0064  108 THR   A CB  
874  O  OG1 . THR   A 108 ? 0.1032 0.0861 0.0743 0.0214  -0.0135 0.0145  108 THR   A OG1 
875  C  CG2 . THR   A 108 ? 0.1082 0.0794 0.0800 0.0181  -0.0023 0.0055  108 THR   A CG2 
876  N  N   . VAL   A 109 ? 0.0933 0.0645 0.0671 0.0059  -0.0001 0.0074  109 VAL   A N   
877  C  CA  . VAL   A 109 ? 0.0943 0.0731 0.0654 0.0056  -0.0015 0.0098  109 VAL   A CA  
878  C  C   . VAL   A 109 ? 0.1037 0.0851 0.0670 0.0015  0.0038  0.0160  109 VAL   A C   
879  O  O   . VAL   A 109 ? 0.1278 0.0757 0.0806 -0.0017 0.0071  0.0189  109 VAL   A O   
880  C  CB  . VAL   A 109 ? 0.0982 0.0825 0.0807 0.0026  -0.0081 0.0152  109 VAL   A CB  
881  C  CG1 . VAL   A 109 ? 0.1025 0.1069 0.0881 -0.0038 -0.0006 0.0159  109 VAL   A CG1 
882  C  CG2 . VAL   A 109 ? 0.1069 0.0967 0.0914 0.0044  -0.0136 0.0243  109 VAL   A CG2 
883  N  N   . ASP   A 110 ? 0.1220 0.0824 0.0662 0.0085  -0.0046 0.0274  110 ASP   A N   
884  C  CA  . ASP   A 110 ? 0.1347 0.0942 0.0831 0.0103  -0.0033 0.0376  110 ASP   A CA  
885  C  C   . ASP   A 110 ? 0.1538 0.0989 0.0907 0.0146  0.0076  0.0303  110 ASP   A C   
886  O  O   . ASP   A 110 ? 0.1787 0.0918 0.1284 0.0285  0.0146  0.0517  110 ASP   A O   
887  C  CB  . ASP   A 110 ? 0.1511 0.1125 0.1131 0.0053  0.0099  0.0451  110 ASP   A CB  
888  C  CG  . ASP   A 110 ? 0.1489 0.1232 0.1016 -0.0017 0.0060  0.0369  110 ASP   A CG  
889  O  OD1 . ASP   A 110 ? 0.1495 0.1162 0.1200 0.0042  0.0140  0.0340  110 ASP   A OD1 
890  O  OD2 . ASP   A 110 ? 0.1428 0.1772 0.1202 -0.0060 0.0100  0.0192  110 ASP   A OD2 
891  N  N   . LYS   A 111 ? 0.1294 0.0972 0.0764 0.0205  -0.0026 0.0306  111 LYS   A N   
892  C  CA  . LYS   A 111 ? 0.1466 0.0922 0.0943 0.0246  -0.0021 0.0296  111 LYS   A CA  
893  C  C   . LYS   A 111 ? 0.1539 0.0811 0.0888 0.0182  0.0177  0.0216  111 LYS   A C   
894  O  O   . LYS   A 111 ? 0.1437 0.1068 0.1229 0.0205  0.0291  0.0042  111 LYS   A O   
895  C  CB  . LYS   A 111 ? 0.1750 0.1347 0.1187 0.0548  0.0036  0.0362  111 LYS   A CB  
896  C  CG  . LYS   A 111 ? 0.1964 0.2013 0.1241 0.0819  -0.0226 0.0484  111 LYS   A CG  
897  C  CD  . LYS   A 111 ? 0.2091 0.2629 0.1709 0.0763  -0.0358 0.0118  111 LYS   A CD  
898  C  CE  . LYS   A 111 ? 0.2395 0.3317 0.1836 0.0711  -0.0497 0.0256  111 LYS   A CE  
899  N  NZ  . LYS   A 111 ? 0.2362 0.3671 0.2535 0.0710  -0.0359 0.0161  111 LYS   A NZ  
900  N  N   . LYS   A 112 ? 0.1476 0.0779 0.0817 0.0075  0.0109  0.0178  112 LYS   A N   
901  C  CA  . LYS   A 112 ? 0.1556 0.0793 0.0950 -0.0011 0.0108  0.0034  112 LYS   A CA  
902  C  C   . LYS   A 112 ? 0.1360 0.0644 0.0966 0.0051  -0.0025 0.0050  112 LYS   A C   
903  O  O   . LYS   A 112 ? 0.1206 0.0676 0.0972 0.0061  -0.0013 0.0035  112 LYS   A O   
904  C  CB  . LYS   A 112 ? 0.1607 0.1005 0.1264 -0.0202 0.0198  -0.0264 112 LYS   A CB  
905  C  CG  . LYS   A 112 ? 0.1725 0.1283 0.1393 -0.0337 0.0289  -0.0400 112 LYS   A CG  
906  C  CD  . LYS   A 112 ? 0.1901 0.1424 0.1812 -0.0113 0.0038  -0.0282 112 LYS   A CD  
907  C  CE  . LYS   A 112 ? 0.1974 0.1529 0.1939 -0.0168 -0.0012 -0.0158 112 LYS   A CE  
908  N  NZ  . LYS   A 112 ? 0.1877 0.1424 0.1763 -0.0247 -0.0093 0.0044  112 LYS   A NZ  
909  N  N   . LYS   A 113 ? 0.1394 0.0757 0.0895 0.0252  -0.0054 0.0009  113 LYS   A N   
910  C  CA  . LYS   A 113 ? 0.1271 0.0738 0.0915 0.0161  -0.0098 0.0066  113 LYS   A CA  
911  C  C   . LYS   A 113 ? 0.1248 0.0583 0.0959 0.0122  -0.0008 0.0073  113 LYS   A C   
912  O  O   . LYS   A 113 ? 0.1742 0.0565 0.1408 0.0107  -0.0312 0.0097  113 LYS   A O   
913  C  CB  . LYS   A 113 ? 0.1310 0.1013 0.0905 0.0188  -0.0097 0.0060  113 LYS   A CB  
914  C  CG  . LYS   A 113 ? 0.1187 0.1044 0.0955 0.0283  -0.0074 0.0070  113 LYS   A CG  
915  C  CD  . LYS   A 113 ? 0.1289 0.1243 0.1195 0.0317  -0.0061 0.0083  113 LYS   A CD  
916  C  CE  . LYS   A 113 ? 0.1315 0.1846 0.1641 0.0152  -0.0095 0.0146  113 LYS   A CE  
917  N  NZ  . LYS   A 113 ? 0.1760 0.2315 0.1847 0.0291  -0.0350 -0.0029 113 LYS   A NZ  
918  N  N   . TYR   A 114 ? 0.1004 0.0541 0.0876 0.0027  -0.0008 0.0045  114 TYR   A N   
919  C  CA  . TYR   A 114 ? 0.0900 0.0535 0.0934 -0.0037 -0.0004 0.0101  114 TYR   A CA  
920  C  C   . TYR   A 114 ? 0.0812 0.0564 0.0917 -0.0047 0.0000  0.0041  114 TYR   A C   
921  O  O   . TYR   A 114 ? 0.0867 0.0719 0.0889 0.0025  0.0041  -0.0049 114 TYR   A O   
922  C  CB  . TYR   A 114 ? 0.0909 0.0579 0.0927 -0.0006 0.0000  0.0090  114 TYR   A CB  
923  C  CG  . TYR   A 114 ? 0.1007 0.0568 0.0860 0.0073  -0.0038 0.0079  114 TYR   A CG  
924  C  CD1 . TYR   A 114 ? 0.1136 0.0736 0.0957 0.0158  -0.0065 0.0006  114 TYR   A CD1 
925  C  CD2 . TYR   A 114 ? 0.0995 0.0814 0.1049 -0.0040 0.0020  0.0080  114 TYR   A CD2 
926  C  CE1 . TYR   A 114 ? 0.1545 0.0991 0.0931 0.0259  0.0122  0.0036  114 TYR   A CE1 
927  C  CE2 . TYR   A 114 ? 0.1172 0.1139 0.1342 0.0015  0.0228  0.0110  114 TYR   A CE2 
928  C  CZ  . TYR   A 114 ? 0.1388 0.1068 0.1251 0.0155  0.0375  0.0209  114 TYR   A CZ  
929  O  OH  . TYR   A 114 ? 0.1896 0.1729 0.1512 0.0354  0.0836  0.0244  114 TYR   A OH  
930  N  N   . ALA   A 115 ? 0.0829 0.0568 0.0895 -0.0055 -0.0012 0.0013  115 ALA   A N   
931  C  CA  . ALA   A 115 ? 0.0913 0.0595 0.0935 -0.0041 -0.0018 -0.0058 115 ALA   A CA  
932  C  C   . ALA   A 115 ? 0.0867 0.0546 0.0841 -0.0039 -0.0002 -0.0121 115 ALA   A C   
933  O  O   . ALA   A 115 ? 0.1031 0.0542 0.0983 -0.0021 0.0081  -0.0151 115 ALA   A O   
934  C  CB  . ALA   A 115 ? 0.1087 0.0606 0.0963 -0.0095 -0.0028 -0.0063 115 ALA   A CB  
935  N  N   . ALA   A 116 ? 0.0809 0.0528 0.0783 -0.0067 0.0000  -0.0084 116 ALA   A N   
936  C  CA  . ALA   A 116 ? 0.0752 0.0472 0.0696 -0.0077 -0.0048 -0.0052 116 ALA   A CA  
937  C  C   . ALA   A 116 ? 0.0655 0.0503 0.0630 -0.0003 -0.0044 -0.0016 116 ALA   A C   
938  O  O   . ALA   A 116 ? 0.0696 0.0579 0.0691 -0.0026 0.0008  0.0024  116 ALA   A O   
939  C  CB  . ALA   A 116 ? 0.0817 0.0586 0.0707 -0.0089 -0.0063 -0.0041 116 ALA   A CB  
940  N  N   . GLU   A 117 ? 0.0696 0.0524 0.0529 -0.0029 -0.0023 -0.0006 117 GLU   A N   
941  C  CA  . GLU   A 117 ? 0.0625 0.0612 0.0541 -0.0012 -0.0049 0.0050  117 GLU   A CA  
942  C  C   . GLU   A 117 ? 0.0688 0.0660 0.0492 -0.0051 -0.0069 -0.0032 117 GLU   A C   
943  O  O   . GLU   A 117 ? 0.0741 0.0704 0.0699 0.0049  0.0035  0.0119  117 GLU   A O   
944  C  CB  . GLU   A 117 ? 0.0708 0.0573 0.0482 -0.0024 -0.0047 0.0051  117 GLU   A CB  
945  C  CG  . GLU   A 117 ? 0.0678 0.0653 0.0476 0.0014  -0.0064 0.0054  117 GLU   A CG  
946  C  CD  . GLU   A 117 ? 0.0731 0.0595 0.0454 -0.0022 -0.0084 0.0075  117 GLU   A CD  
947  O  OE1 . GLU   A 117 ? 0.0711 0.0760 0.0598 0.0073  -0.0135 0.0018  117 GLU   A OE1 
948  O  OE2 . GLU   A 117 ? 0.0993 0.0676 0.0530 -0.0028 -0.0240 0.0003  117 GLU   A OE2 
949  N  N   . LEU   A 118 ? 0.0623 0.0516 0.0540 -0.0038 -0.0125 0.0002  118 LEU   A N   
950  C  CA  . LEU   A 118 ? 0.0631 0.0553 0.0472 -0.0039 -0.0146 0.0024  118 LEU   A CA  
951  C  C   . LEU   A 118 ? 0.0603 0.0477 0.0505 -0.0005 -0.0123 0.0053  118 LEU   A C   
952  O  O   . LEU   A 118 ? 0.0654 0.0503 0.0510 -0.0037 -0.0052 0.0023  118 LEU   A O   
953  C  CB  . LEU   A 118 ? 0.0668 0.0651 0.0578 -0.0072 -0.0206 0.0072  118 LEU   A CB  
954  C  CG  . LEU   A 118 ? 0.0753 0.0744 0.0580 0.0026  -0.0269 0.0036  118 LEU   A CG  
955  C  CD1 . LEU   A 118 ? 0.0799 0.0789 0.0627 0.0013  -0.0332 0.0064  118 LEU   A CD1 
956  C  CD2 . LEU   A 118 ? 0.0847 0.0978 0.0776 0.0010  -0.0315 0.0051  118 LEU   A CD2 
957  N  N   . HIS   A 119 ? 0.0690 0.0465 0.0406 -0.0027 -0.0126 0.0008  119 HIS   A N   
958  C  CA  . HIS   A 119 ? 0.0711 0.0504 0.0433 -0.0047 -0.0152 0.0049  119 HIS   A CA  
959  C  C   . HIS   A 119 ? 0.0759 0.0526 0.0447 -0.0066 -0.0197 0.0068  119 HIS   A C   
960  O  O   . HIS   A 119 ? 0.0875 0.0641 0.0524 0.0034  -0.0130 0.0050  119 HIS   A O   
961  C  CB  . HIS   A 119 ? 0.0698 0.0507 0.0449 -0.0026 -0.0131 0.0016  119 HIS   A CB  
962  C  CG  . HIS   A 119 ? 0.0596 0.0543 0.0506 0.0050  -0.0104 -0.0086 119 HIS   A CG  
963  N  ND1 . HIS   A 119 ? 0.0546 0.0631 0.0471 -0.0014 -0.0035 -0.0022 119 HIS   A ND1 
964  C  CD2 . HIS   A 119 ? 0.0631 0.0581 0.0516 0.0022  -0.0183 0.0008  119 HIS   A CD2 
965  C  CE1 . HIS   A 119 ? 0.0576 0.0667 0.0490 0.0075  -0.0115 -0.0063 119 HIS   A CE1 
966  N  NE2 . HIS   A 119 ? 0.0569 0.0704 0.0531 -0.0014 -0.0166 0.0034  119 HIS   A NE2 
967  N  N   . LEU   A 120 ? 0.0803 0.0472 0.0478 -0.0024 -0.0128 0.0101  120 LEU   A N   
968  C  CA  . LEU   A 120 ? 0.0849 0.0537 0.0478 0.0048  -0.0189 0.0087  120 LEU   A CA  
969  C  C   . LEU   A 120 ? 0.0809 0.0529 0.0513 0.0059  -0.0201 0.0144  120 LEU   A C   
970  O  O   . LEU   A 120 ? 0.0782 0.0575 0.0545 0.0039  -0.0139 0.0089  120 LEU   A O   
971  C  CB  . LEU   A 120 ? 0.0832 0.0653 0.0626 0.0011  -0.0206 0.0045  120 LEU   A CB  
972  C  CG  . LEU   A 120 ? 0.0904 0.0818 0.0682 -0.0033 -0.0258 -0.0021 120 LEU   A CG  
973  C  CD1 . LEU   A 120 ? 0.1389 0.0966 0.0932 -0.0312 -0.0177 -0.0057 120 LEU   A CD1 
974  C  CD2 . LEU   A 120 ? 0.1030 0.1178 0.0715 0.0058  -0.0364 -0.0105 120 LEU   A CD2 
975  N  N   . VAL   A 121 ? 0.0904 0.0539 0.0496 -0.0007 -0.0168 0.0038  121 VAL   A N   
976  C  CA  . VAL   A 121 ? 0.0863 0.0569 0.0501 -0.0013 -0.0124 0.0052  121 VAL   A CA  
977  C  C   . VAL   A 121 ? 0.0804 0.0532 0.0580 -0.0045 -0.0126 0.0080  121 VAL   A C   
978  O  O   . VAL   A 121 ? 0.1078 0.0604 0.0583 0.0046  -0.0191 0.0082  121 VAL   A O   
979  C  CB  . VAL   A 121 ? 0.0939 0.0639 0.0652 -0.0004 -0.0049 0.0081  121 VAL   A CB  
980  C  CG1 . VAL   A 121 ? 0.0867 0.0742 0.0904 -0.0042 0.0008  0.0115  121 VAL   A CG1 
981  C  CG2 . VAL   A 121 ? 0.0998 0.0805 0.0787 0.0068  0.0001  0.0058  121 VAL   A CG2 
982  N  N   . HIS   A 122 ? 0.0853 0.0530 0.0602 -0.0013 -0.0162 0.0069  122 HIS   A N   
983  C  CA  . HIS   A 122 ? 0.0882 0.0501 0.0638 -0.0001 -0.0173 0.0064  122 HIS   A CA  
984  C  C   . HIS   A 122 ? 0.0848 0.0553 0.0648 -0.0036 -0.0147 0.0065  122 HIS   A C   
985  O  O   . HIS   A 122 ? 0.1008 0.0605 0.0700 -0.0106 -0.0221 0.0054  122 HIS   A O   
986  C  CB  . HIS   A 122 ? 0.0888 0.0452 0.0698 0.0048  -0.0126 0.0052  122 HIS   A CB  
987  C  CG  . HIS   A 122 ? 0.0844 0.0514 0.0713 0.0010  -0.0107 0.0026  122 HIS   A CG  
988  N  ND1 . HIS   A 122 ? 0.0904 0.0549 0.0739 -0.0037 -0.0099 0.0044  122 HIS   A ND1 
989  C  CD2 . HIS   A 122 ? 0.0809 0.0659 0.0756 0.0089  -0.0093 0.0079  122 HIS   A CD2 
990  C  CE1 . HIS   A 122 ? 0.0846 0.0664 0.0779 -0.0043 -0.0064 0.0006  122 HIS   A CE1 
991  N  NE2 . HIS   A 122 ? 0.0863 0.0779 0.0828 -0.0024 -0.0125 -0.0005 122 HIS   A NE2 
992  N  N   . TRP   A 123 ? 0.0951 0.0519 0.0707 -0.0025 -0.0176 -0.0011 123 TRP   A N   
993  C  CA  . TRP   A 123 ? 0.0986 0.0605 0.0722 -0.0079 -0.0151 -0.0013 123 TRP   A CA  
994  C  C   . TRP   A 123 ? 0.0967 0.0528 0.0812 -0.0052 -0.0181 0.0029  123 TRP   A C   
995  O  O   . TRP   A 123 ? 0.0964 0.0620 0.0929 0.0023  -0.0212 -0.0014 123 TRP   A O   
996  C  CB  . TRP   A 123 ? 0.1090 0.0840 0.0842 -0.0186 -0.0008 -0.0066 123 TRP   A CB  
997  C  CG  . TRP   A 123 ? 0.1226 0.0653 0.0929 -0.0262 0.0000  0.0004  123 TRP   A CG  
998  C  CD1 . TRP   A 123 ? 0.1294 0.0681 0.0989 -0.0126 -0.0047 0.0052  123 TRP   A CD1 
999  C  CD2 . TRP   A 123 ? 0.1544 0.0589 0.1007 -0.0298 0.0010  0.0016  123 TRP   A CD2 
1000 N  NE1 . TRP   A 123 ? 0.1497 0.0647 0.1088 -0.0114 -0.0177 0.0020  123 TRP   A NE1 
1001 C  CE2 . TRP   A 123 ? 0.1588 0.0557 0.1101 -0.0176 -0.0108 0.0076  123 TRP   A CE2 
1002 C  CE3 . TRP   A 123 ? 0.1941 0.0550 0.1127 -0.0281 0.0048  0.0012  123 TRP   A CE3 
1003 C  CZ2 . TRP   A 123 ? 0.1959 0.0542 0.1322 -0.0170 -0.0092 0.0275  123 TRP   A CZ2 
1004 C  CZ3 . TRP   A 123 ? 0.2167 0.0545 0.1394 -0.0208 0.0079  0.0038  123 TRP   A CZ3 
1005 C  CH2 . TRP   A 123 ? 0.2188 0.0554 0.1424 -0.0116 0.0007  0.0157  123 TRP   A CH2 
1006 N  N   . ASN   A 124 ? 0.0885 0.0556 0.0881 0.0004  -0.0141 -0.0014 124 ASN   A N   
1007 C  CA  . ASN   A 124 ? 0.1004 0.0511 0.0881 0.0045  -0.0117 -0.0036 124 ASN   A CA  
1008 C  C   . ASN   A 124 ? 0.1220 0.0563 0.0967 -0.0008 -0.0117 -0.0018 124 ASN   A C   
1009 O  O   . ASN   A 124 ? 0.1204 0.0591 0.1042 -0.0001 -0.0036 0.0016  124 ASN   A O   
1010 C  CB  . ASN   A 124 ? 0.1029 0.0524 0.0886 0.0000  -0.0131 -0.0003 124 ASN   A CB  
1011 C  CG  . ASN   A 124 ? 0.1149 0.0572 0.0954 -0.0031 -0.0074 -0.0021 124 ASN   A CG  
1012 O  OD1 . ASN   A 124 ? 0.1251 0.0709 0.1135 0.0163  0.0022  -0.0023 124 ASN   A OD1 
1013 N  ND2 . ASN   A 124 ? 0.1198 0.0728 0.0982 0.0108  -0.0024 -0.0047 124 ASN   A ND2 
1014 N  N   . THR   A 125 ? 0.1185 0.0509 0.1169 0.0056  -0.0231 0.0019  125 THR   A N   
1015 C  CA  . THR   A 125 ? 0.1410 0.0611 0.1277 0.0113  -0.0285 0.0101  125 THR   A CA  
1016 C  C   . THR   A 125 ? 0.1484 0.0544 0.1398 0.0210  -0.0152 0.0022  125 THR   A C   
1017 O  O   . THR   A 125 ? 0.1622 0.0688 0.1656 0.0082  -0.0204 0.0190  125 THR   A O   
1018 C  CB  . THR   A 125 ? 0.1538 0.0808 0.1741 0.0214  -0.0510 0.0207  125 THR   A CB  
1019 O  OG1 . THR   A 125 ? 0.1619 0.1125 0.2168 0.0473  -0.0086 0.0146  125 THR   A OG1 
1020 C  CG2 . THR   A 125 ? 0.1667 0.1046 0.1760 0.0035  -0.0667 0.0167  125 THR   A CG2 
1021 N  N   . LYS   A 126 ? 0.1608 0.0557 0.1391 0.0020  -0.0089 -0.0153 127 LYS   A N   
1022 C  CA  . LYS   A 126 ? 0.1715 0.0629 0.1434 0.0032  0.0038  -0.0256 127 LYS   A CA  
1023 C  C   . LYS   A 126 ? 0.1797 0.0487 0.1188 0.0017  0.0047  -0.0124 127 LYS   A C   
1024 O  O   . LYS   A 126 ? 0.2021 0.0592 0.1815 -0.0072 0.0192  -0.0306 127 LYS   A O   
1025 C  CB  . LYS   A 126 ? 0.2033 0.0962 0.1511 -0.0288 0.0087  -0.0290 127 LYS   A CB  
1026 C  CG  . LYS   A 126 ? 0.2229 0.1212 0.1478 -0.0246 0.0229  -0.0269 127 LYS   A CG  
1027 C  CD  . LYS   A 126 ? 0.2627 0.1724 0.1696 -0.0416 0.0305  -0.0117 127 LYS   A CD  
1028 C  CE  . LYS   A 126 ? 0.2981 0.2019 0.1702 0.0054  0.0252  -0.0202 127 LYS   A CE  
1029 N  NZ  . LYS   A 126 ? 0.3264 0.2654 0.1648 0.0154  0.0171  -0.0094 127 LYS   A NZ  
1030 N  N   . TYR   A 127 ? 0.1470 0.0567 0.1087 0.0018  -0.0017 -0.0129 128 TYR   A N   
1031 C  CA  . TYR   A 127 ? 0.1390 0.0706 0.1110 -0.0010 -0.0060 -0.0074 128 TYR   A CA  
1032 C  C   . TYR   A 127 ? 0.1451 0.0626 0.1257 -0.0015 -0.0041 -0.0002 128 TYR   A C   
1033 O  O   . TYR   A 127 ? 0.1615 0.0782 0.1260 -0.0029 0.0098  -0.0044 128 TYR   A O   
1034 C  CB  . TYR   A 127 ? 0.1446 0.0647 0.1192 -0.0034 -0.0020 -0.0133 128 TYR   A CB  
1035 C  CG  . TYR   A 127 ? 0.1342 0.0711 0.1148 0.0016  0.0003  -0.0185 128 TYR   A CG  
1036 C  CD1 . TYR   A 127 ? 0.1525 0.0715 0.1250 -0.0025 -0.0060 -0.0122 128 TYR   A CD1 
1037 C  CD2 . TYR   A 127 ? 0.1236 0.0754 0.1034 -0.0001 0.0045  -0.0227 128 TYR   A CD2 
1038 C  CE1 . TYR   A 127 ? 0.1599 0.0815 0.1125 0.0039  -0.0004 -0.0259 128 TYR   A CE1 
1039 C  CE2 . TYR   A 127 ? 0.1294 0.0769 0.1125 -0.0005 -0.0060 -0.0176 128 TYR   A CE2 
1040 C  CZ  . TYR   A 127 ? 0.1406 0.0888 0.1092 0.0080  0.0021  -0.0209 128 TYR   A CZ  
1041 O  OH  . TYR   A 127 ? 0.1587 0.0906 0.1074 0.0042  0.0009  -0.0266 128 TYR   A OH  
1042 N  N   . GLY   A 128 ? 0.1432 0.0652 0.1231 -0.0117 -0.0055 0.0064  129 GLY   A N   
1043 C  CA  . GLY   A 128 ? 0.1724 0.0676 0.1330 -0.0058 -0.0023 0.0066  129 GLY   A CA  
1044 C  C   . GLY   A 128 ? 0.1850 0.0679 0.1029 0.0000  -0.0112 0.0193  129 GLY   A C   
1045 O  O   . GLY   A 128 ? 0.2093 0.0829 0.1150 0.0086  -0.0122 0.0195  129 GLY   A O   
1046 N  N   . ASP   A 129 ? 0.2114 0.0792 0.0959 0.0136  -0.0074 0.0021  130 ASP   A N   
1047 C  CA  . ASP   A 129 ? 0.2490 0.1070 0.0760 0.0367  -0.0113 0.0025  130 ASP   A CA  
1048 C  C   . ASP   A 129 ? 0.2263 0.0903 0.0767 0.0162  -0.0102 0.0025  130 ASP   A C   
1049 O  O   . ASP   A 129 ? 0.2205 0.0764 0.0748 0.0223  -0.0063 0.0017  130 ASP   A O   
1050 C  CB  . ASP   A 129 ? 0.2826 0.1064 0.0831 0.0746  0.0073  0.0142  130 ASP   A CB  
1051 C  CG  . ASP   A 129 ? 0.2715 0.1032 0.1888 0.0687  0.0146  -0.0264 130 ASP   A CG  
1052 O  OD1 . ASP   A 129 ? 0.3397 0.1543 0.2419 0.0056  -0.0483 0.0409  130 ASP   A OD1 
1053 O  OD2 . ASP   A 129 ? 0.2830 0.1768 0.3244 0.0041  0.0016  0.0512  130 ASP   A OD2 
1054 N  N   . PHE   A 130 ? 0.2092 0.0824 0.0734 0.0123  -0.0049 0.0001  131 PHE   A N   
1055 C  CA  . PHE   A 130 ? 0.1779 0.0817 0.0788 0.0002  0.0048  -0.0020 131 PHE   A CA  
1056 C  C   . PHE   A 130 ? 0.1788 0.0737 0.0799 -0.0107 0.0179  -0.0070 131 PHE   A C   
1057 O  O   . PHE   A 130 ? 0.1444 0.0804 0.0852 -0.0200 0.0089  -0.0050 131 PHE   A O   
1058 C  CB  . PHE   A 130 ? 0.1628 0.0830 0.0897 -0.0085 0.0061  -0.0106 131 PHE   A CB  
1059 C  CG  . PHE   A 130 ? 0.1474 0.0814 0.0976 -0.0084 0.0102  -0.0237 131 PHE   A CG  
1060 C  CD1 . PHE   A 130 ? 0.1562 0.1060 0.1480 -0.0145 0.0172  -0.0334 131 PHE   A CD1 
1061 C  CD2 . PHE   A 130 ? 0.1402 0.0899 0.0990 -0.0160 0.0181  -0.0260 131 PHE   A CD2 
1062 C  CE1 . PHE   A 130 ? 0.1738 0.1313 0.1591 0.0001  0.0047  -0.0427 131 PHE   A CE1 
1063 C  CE2 . PHE   A 130 ? 0.1708 0.0987 0.1127 -0.0167 0.0019  -0.0246 131 PHE   A CE2 
1064 C  CZ  . PHE   A 130 ? 0.1839 0.0990 0.1313 -0.0014 -0.0126 -0.0348 131 PHE   A CZ  
1065 N  N   . GLY   A 131 ? 0.2025 0.0998 0.0879 -0.0290 0.0235  -0.0074 132 GLY   A N   
1066 C  CA  . GLY   A 131 ? 0.1900 0.1158 0.1005 -0.0245 0.0405  -0.0068 132 GLY   A CA  
1067 C  C   . GLY   A 131 ? 0.1716 0.1045 0.1138 -0.0320 0.0208  -0.0082 132 GLY   A C   
1068 O  O   . GLY   A 131 ? 0.1655 0.1206 0.1537 -0.0231 0.0359  -0.0318 132 GLY   A O   
1069 N  N   . LYS   A 132 ? 0.1569 0.0982 0.1054 -0.0297 0.0144  -0.0051 133 LYS   A N   
1070 C  CA  . LYS   A 132 ? 0.1534 0.0910 0.1053 -0.0451 0.0063  -0.0122 133 LYS   A CA  
1071 C  C   . LYS   A 132 ? 0.1266 0.0961 0.0898 -0.0332 0.0065  -0.0174 133 LYS   A C   
1072 O  O   . LYS   A 132 ? 0.1215 0.1057 0.0909 -0.0416 0.0000  -0.0205 133 LYS   A O   
1073 C  CB  . LYS   A 132 ? 0.1785 0.0946 0.1084 -0.0400 0.0088  -0.0214 133 LYS   A CB  
1074 C  CG  . LYS   A 132 ? 0.2169 0.1262 0.1930 -0.0352 -0.0070 0.0126  133 LYS   A CG  
1075 C  CD  . LYS   A 132 ? 0.2354 0.1768 0.2643 -0.0417 -0.0135 0.0444  133 LYS   A CD  
1076 C  CE  . LYS   A 132 ? 0.2712 0.2412 0.2607 -0.0216 -0.0054 0.0409  133 LYS   A CE  
1077 N  NZ  . LYS   A 132 ? 0.3078 0.3185 0.3118 -0.0183 -0.0224 0.0455  133 LYS   A NZ  
1078 N  N   . ALA   A 133 ? 0.1308 0.0885 0.0761 -0.0316 0.0070  -0.0136 134 ALA   A N   
1079 C  CA  . ALA   A 133 ? 0.1154 0.0843 0.0712 -0.0278 0.0042  -0.0106 134 ALA   A CA  
1080 C  C   . ALA   A 133 ? 0.1113 0.0884 0.0760 -0.0265 0.0099  -0.0053 134 ALA   A C   
1081 O  O   . ALA   A 133 ? 0.1049 0.1069 0.0831 -0.0221 0.0004  -0.0036 134 ALA   A O   
1082 C  CB  . ALA   A 133 ? 0.1176 0.0784 0.0740 -0.0269 -0.0055 -0.0036 134 ALA   A CB  
1083 N  N   . VAL   A 134 ? 0.1264 0.0979 0.0875 -0.0257 0.0179  -0.0126 135 VAL   A N   
1084 C  CA  . VAL   A 134 ? 0.1419 0.1061 0.1007 -0.0178 0.0160  -0.0117 135 VAL   A CA  
1085 C  C   . VAL   A 134 ? 0.1223 0.1237 0.1049 -0.0186 0.0222  -0.0048 135 VAL   A C   
1086 O  O   . VAL   A 134 ? 0.1400 0.1471 0.1421 -0.0111 0.0142  -0.0086 135 VAL   A O   
1087 C  CB  . VAL   A 134 ? 0.1658 0.1056 0.1131 -0.0157 0.0135  -0.0255 135 VAL   A CB  
1088 C  CG1 . VAL   A 134 ? 0.1788 0.1059 0.1430 -0.0187 0.0100  -0.0369 135 VAL   A CG1 
1089 C  CG2 . VAL   A 134 ? 0.1634 0.1235 0.1140 -0.0062 0.0230  -0.0165 135 VAL   A CG2 
1090 N  N   . GLN   A 135 ? 0.1074 0.1355 0.1139 -0.0280 0.0151  -0.0255 136 GLN   A N   
1091 C  CA  . GLN   A 135 ? 0.1052 0.1508 0.1151 -0.0301 0.0128  -0.0256 136 GLN   A CA  
1092 C  C   . GLN   A 135 ? 0.1048 0.1395 0.1014 -0.0376 -0.0003 -0.0180 136 GLN   A C   
1093 O  O   . GLN   A 135 ? 0.1132 0.1550 0.1205 -0.0422 -0.0127 -0.0198 136 GLN   A O   
1094 C  CB  . GLN   A 135 ? 0.1424 0.1714 0.1414 -0.0533 0.0104  -0.0087 136 GLN   A CB  
1095 C  CG  . GLN   A 135 ? 0.1729 0.2197 0.1650 -0.0624 0.0331  0.0207  136 GLN   A CG  
1096 C  CD  . GLN   A 135 ? 0.2382 0.2593 0.1972 -0.1027 0.0423  0.0551  136 GLN   A CD  
1097 O  OE1 . GLN   A 135 ? 0.3129 0.3354 0.3520 -0.1120 -0.0075 0.0164  136 GLN   A OE1 
1098 N  NE2 . GLN   A 135 ? 0.3308 0.2644 0.2553 -0.0997 0.0064  0.0708  136 GLN   A NE2 
1099 N  N   . GLN   A 136 ? 0.1042 0.1132 0.0960 -0.0290 0.0076  -0.0261 137 GLN   A N   
1100 C  CA  . GLN   A 136 ? 0.1010 0.1172 0.0823 -0.0240 -0.0012 -0.0296 137 GLN   A CA  
1101 C  C   . GLN   A 136 ? 0.0782 0.1175 0.0772 -0.0147 0.0001  -0.0248 137 GLN   A C   
1102 O  O   . GLN   A 136 ? 0.0865 0.1148 0.0845 -0.0139 -0.0049 -0.0213 137 GLN   A O   
1103 C  CB  . GLN   A 136 ? 0.1085 0.0962 0.0939 -0.0192 -0.0019 -0.0285 137 GLN   A CB  
1104 C  CG  . GLN   A 136 ? 0.1207 0.1255 0.1171 -0.0096 0.0003  -0.0186 137 GLN   A CG  
1105 C  CD  . GLN   A 136 ? 0.1353 0.1495 0.1020 -0.0285 -0.0061 -0.0277 137 GLN   A CD  
1106 O  OE1 . GLN   A 136 ? 0.1750 0.1618 0.0925 -0.0293 -0.0181 -0.0390 137 GLN   A OE1 
1107 N  NE2 . GLN   A 136 ? 0.1715 0.1666 0.1151 -0.0593 -0.0157 -0.0107 137 GLN   A NE2 
1108 N  N   . PRO   A 137 ? 0.0950 0.1405 0.0792 -0.0195 -0.0161 -0.0223 138 PRO   A N   
1109 C  CA  . PRO   A 137 ? 0.1088 0.1421 0.0860 -0.0101 -0.0254 -0.0049 138 PRO   A CA  
1110 C  C   . PRO   A 137 ? 0.1066 0.1194 0.0839 -0.0143 -0.0260 -0.0024 138 PRO   A C   
1111 O  O   . PRO   A 137 ? 0.1290 0.1321 0.1664 -0.0143 -0.0287 0.0120  138 PRO   A O   
1112 C  CB  . PRO   A 137 ? 0.1459 0.1868 0.0917 -0.0253 -0.0276 -0.0013 138 PRO   A CB  
1113 C  CG  . PRO   A 137 ? 0.1839 0.2049 0.0954 -0.0222 -0.0153 -0.0216 138 PRO   A CG  
1114 C  CD  . PRO   A 137 ? 0.1229 0.1677 0.0878 -0.0324 -0.0232 -0.0273 138 PRO   A CD  
1115 N  N   . ASP   A 138 ? 0.0906 0.1036 0.0706 -0.0127 -0.0148 -0.0069 139 ASP   A N   
1116 C  CA  . ASP   A 138 ? 0.0922 0.0964 0.0742 -0.0128 -0.0112 -0.0123 139 ASP   A CA  
1117 C  C   . ASP   A 138 ? 0.0830 0.0794 0.0693 -0.0070 -0.0057 -0.0132 139 ASP   A C   
1118 O  O   . ASP   A 138 ? 0.0811 0.0811 0.0920 0.0009  -0.0015 -0.0047 139 ASP   A O   
1119 C  CB  . ASP   A 138 ? 0.1161 0.1252 0.0849 -0.0111 0.0042  -0.0158 139 ASP   A CB  
1120 C  CG  . ASP   A 138 ? 0.1185 0.1292 0.0998 -0.0027 0.0110  -0.0239 139 ASP   A CG  
1121 O  OD1 . ASP   A 138 ? 0.1387 0.0991 0.1133 -0.0035 0.0120  -0.0282 139 ASP   A OD1 
1122 O  OD2 . ASP   A 138 ? 0.1448 0.1450 0.1339 0.0003  0.0409  -0.0447 139 ASP   A OD2 
1123 N  N   . GLY   A 139 ? 0.0741 0.0773 0.0668 -0.0009 -0.0134 -0.0136 140 GLY   A N   
1124 C  CA  . GLY   A 139 ? 0.0770 0.0735 0.0673 -0.0036 -0.0126 -0.0116 140 GLY   A CA  
1125 C  C   . GLY   A 139 ? 0.0695 0.0597 0.0638 -0.0046 -0.0087 -0.0061 140 GLY   A C   
1126 O  O   . GLY   A 139 ? 0.0847 0.0645 0.0730 -0.0006 -0.0091 -0.0011 140 GLY   A O   
1127 N  N   . LEU   A 140 ? 0.0719 0.0587 0.0606 -0.0004 -0.0068 -0.0029 141 LEU   A N   
1128 C  CA  . LEU   A 140 ? 0.0781 0.0587 0.0672 -0.0015 -0.0118 0.0022  141 LEU   A CA  
1129 C  C   . LEU   A 140 ? 0.0740 0.0505 0.0569 0.0028  -0.0147 0.0006  141 LEU   A C   
1130 O  O   . LEU   A 140 ? 0.0741 0.0575 0.0578 -0.0010 -0.0150 0.0014  141 LEU   A O   
1131 C  CB  . LEU   A 140 ? 0.0880 0.0592 0.0794 -0.0022 0.0014  0.0008  141 LEU   A CB  
1132 C  CG  . LEU   A 140 ? 0.0889 0.0758 0.0941 0.0037  0.0026  0.0065  141 LEU   A CG  
1133 C  CD1 . LEU   A 140 ? 0.1133 0.0810 0.1132 0.0127  0.0176  0.0059  141 LEU   A CD1 
1134 C  CD2 . LEU   A 140 ? 0.0969 0.0881 0.0912 0.0050  0.0004  0.0130  141 LEU   A CD2 
1135 N  N   . ALA   A 141 ? 0.0815 0.0601 0.0558 -0.0055 -0.0173 0.0029  142 ALA   A N   
1136 C  CA  . ALA   A 141 ? 0.0884 0.0591 0.0655 -0.0158 -0.0197 0.0053  142 ALA   A CA  
1137 C  C   . ALA   A 141 ? 0.0840 0.0552 0.0616 -0.0109 -0.0225 0.0111  142 ALA   A C   
1138 O  O   . ALA   A 141 ? 0.1030 0.0613 0.0626 -0.0074 -0.0285 0.0096  142 ALA   A O   
1139 C  CB  . ALA   A 141 ? 0.0957 0.0690 0.0766 -0.0150 -0.0144 0.0069  142 ALA   A CB  
1140 N  N   . VAL   A 142 ? 0.0894 0.0572 0.0541 -0.0094 -0.0221 0.0071  143 VAL   A N   
1141 C  CA  . VAL   A 142 ? 0.0898 0.0596 0.0512 -0.0068 -0.0191 0.0074  143 VAL   A CA  
1142 C  C   . VAL   A 142 ? 0.0874 0.0484 0.0442 0.0024  -0.0167 0.0024  143 VAL   A C   
1143 O  O   . VAL   A 142 ? 0.0855 0.0645 0.0444 -0.0038 -0.0187 0.0061  143 VAL   A O   
1144 C  CB  . VAL   A 142 ? 0.0840 0.0731 0.0598 -0.0059 -0.0207 0.0087  143 VAL   A CB  
1145 C  CG1 . VAL   A 142 ? 0.0899 0.0763 0.0742 0.0102  -0.0225 0.0013  143 VAL   A CG1 
1146 C  CG2 . VAL   A 142 ? 0.0886 0.0991 0.0676 -0.0118 -0.0139 0.0151  143 VAL   A CG2 
1147 N  N   . LEU   A 143 ? 0.0793 0.0551 0.0468 -0.0008 -0.0183 0.0085  144 LEU   A N   
1148 C  CA  . LEU   A 143 ? 0.0744 0.0661 0.0521 -0.0069 -0.0146 0.0063  144 LEU   A CA  
1149 C  C   . LEU   A 143 ? 0.0793 0.0582 0.0512 -0.0126 -0.0074 0.0054  144 LEU   A C   
1150 O  O   . LEU   A 143 ? 0.1154 0.0683 0.0555 -0.0074 -0.0006 0.0030  144 LEU   A O   
1151 C  CB  . LEU   A 143 ? 0.0912 0.0977 0.0664 -0.0054 -0.0138 0.0122  144 LEU   A CB  
1152 C  CG  . LEU   A 143 ? 0.0890 0.1000 0.1115 -0.0078 -0.0197 -0.0008 144 LEU   A CG  
1153 C  CD1 . LEU   A 143 ? 0.0991 0.1287 0.1301 -0.0058 -0.0179 0.0264  144 LEU   A CD1 
1154 C  CD2 . LEU   A 143 ? 0.0902 0.1395 0.1063 0.0069  -0.0261 0.0015  144 LEU   A CD2 
1155 N  N   . GLY   A 144 ? 0.0750 0.0548 0.0477 -0.0059 -0.0061 -0.0027 145 GLY   A N   
1156 C  CA  . GLY   A 144 ? 0.0676 0.0558 0.0584 -0.0030 -0.0016 0.0014  145 GLY   A CA  
1157 C  C   . GLY   A 144 ? 0.0612 0.0492 0.0618 -0.0043 -0.0071 -0.0008 145 GLY   A C   
1158 O  O   . GLY   A 144 ? 0.0786 0.0714 0.0680 -0.0145 0.0049  -0.0046 145 GLY   A O   
1159 N  N   . ILE   A 145 ? 0.0586 0.0518 0.0582 -0.0043 -0.0044 0.0006  146 ILE   A N   
1160 C  CA  . ILE   A 145 ? 0.0573 0.0553 0.0592 -0.0051 -0.0097 0.0007  146 ILE   A CA  
1161 C  C   . ILE   A 145 ? 0.0529 0.0488 0.0589 -0.0107 -0.0047 -0.0037 146 ILE   A C   
1162 O  O   . ILE   A 145 ? 0.0660 0.0533 0.0767 -0.0059 0.0038  0.0001  146 ILE   A O   
1163 C  CB  . ILE   A 145 ? 0.0646 0.0688 0.0700 -0.0026 -0.0210 -0.0001 146 ILE   A CB  
1164 C  CG1 . ILE   A 145 ? 0.0799 0.0806 0.0938 0.0078  -0.0231 0.0041  146 ILE   A CG1 
1165 C  CG2 . ILE   A 145 ? 0.0768 0.0771 0.1019 -0.0030 -0.0315 0.0024  146 ILE   A CG2 
1166 C  CD1 . ILE   A 145 ? 0.0797 0.0843 0.0966 0.0001  -0.0267 0.0128  146 ILE   A CD1 
1167 N  N   . PHE   A 146 ? 0.0605 0.0455 0.0602 -0.0062 -0.0020 0.0000  147 PHE   A N   
1168 C  CA  . PHE   A 146 ? 0.0633 0.0511 0.0699 -0.0075 -0.0041 0.0036  147 PHE   A CA  
1169 C  C   . PHE   A 146 ? 0.0748 0.0564 0.0779 -0.0066 -0.0043 -0.0051 147 PHE   A C   
1170 O  O   . PHE   A 146 ? 0.0689 0.0758 0.0849 -0.0079 -0.0109 -0.0147 147 PHE   A O   
1171 C  CB  . PHE   A 146 ? 0.0639 0.0507 0.0763 -0.0042 -0.0027 0.0057  147 PHE   A CB  
1172 C  CG  . PHE   A 146 ? 0.0674 0.0574 0.0719 0.0029  -0.0025 0.0094  147 PHE   A CG  
1173 C  CD1 . PHE   A 146 ? 0.0705 0.0594 0.0719 0.0025  -0.0044 0.0031  147 PHE   A CD1 
1174 C  CD2 . PHE   A 146 ? 0.0713 0.0650 0.0725 -0.0020 -0.0018 0.0105  147 PHE   A CD2 
1175 C  CE1 . PHE   A 146 ? 0.0709 0.0698 0.0802 -0.0020 -0.0111 0.0063  147 PHE   A CE1 
1176 C  CE2 . PHE   A 146 ? 0.0819 0.0759 0.0633 -0.0010 -0.0024 0.0121  147 PHE   A CE2 
1177 C  CZ  . PHE   A 146 ? 0.0832 0.0627 0.0723 -0.0077 -0.0074 0.0090  147 PHE   A CZ  
1178 N  N   . LEU   A 147 ? 0.0730 0.0636 0.0748 -0.0072 -0.0097 -0.0050 148 LEU   A N   
1179 C  CA  . LEU   A 147 ? 0.0806 0.0634 0.0789 -0.0129 -0.0134 -0.0057 148 LEU   A CA  
1180 C  C   . LEU   A 147 ? 0.0869 0.0598 0.0781 -0.0095 -0.0119 -0.0081 148 LEU   A C   
1181 O  O   . LEU   A 147 ? 0.0980 0.0545 0.0911 -0.0038 -0.0008 -0.0051 148 LEU   A O   
1182 C  CB  . LEU   A 147 ? 0.0902 0.0566 0.0872 -0.0172 -0.0140 -0.0078 148 LEU   A CB  
1183 C  CG  . LEU   A 147 ? 0.0985 0.0650 0.0845 -0.0127 -0.0189 -0.0043 148 LEU   A CG  
1184 C  CD1 . LEU   A 147 ? 0.1164 0.0699 0.0845 -0.0165 -0.0232 0.0005  148 LEU   A CD1 
1185 C  CD2 . LEU   A 147 ? 0.1025 0.0744 0.0939 -0.0161 -0.0219 -0.0043 148 LEU   A CD2 
1186 N  N   . LYS   A 148 ? 0.0956 0.0605 0.0989 -0.0127 -0.0174 -0.0032 149 LYS   A N   
1187 C  CA  . LYS   A 148 ? 0.1187 0.0584 0.1142 -0.0148 -0.0252 0.0024  149 LYS   A CA  
1188 C  C   . LYS   A 148 ? 0.1260 0.0552 0.1224 -0.0122 -0.0311 -0.0019 149 LYS   A C   
1189 O  O   . LYS   A 148 ? 0.1406 0.0889 0.1248 0.0064  -0.0324 -0.0086 149 LYS   A O   
1190 C  CB  . LYS   A 148 ? 0.1444 0.0920 0.1122 -0.0289 -0.0263 0.0061  149 LYS   A CB  
1191 C  CG  . LYS   A 148 ? 0.1552 0.1067 0.1533 -0.0368 -0.0094 0.0116  149 LYS   A CG  
1192 C  CD  . LYS   A 148 ? 0.1901 0.1391 0.2077 -0.0449 -0.0030 0.0223  149 LYS   A CD  
1193 C  CE  . LYS   A 148 ? 0.2350 0.2227 0.2798 -0.0261 0.0067  0.0228  149 LYS   A CE  
1194 N  NZ  . LYS   A 148 ? 0.2645 0.2906 0.3363 -0.0341 0.0202  0.0333  149 LYS   A NZ  
1195 N  N   . VAL   A 149 ? 0.1595 0.0622 0.1192 -0.0031 -0.0321 0.0008  150 VAL   A N   
1196 C  CA  . VAL   A 149 ? 0.1651 0.0802 0.1171 -0.0130 -0.0389 -0.0016 150 VAL   A CA  
1197 C  C   . VAL   A 149 ? 0.1873 0.0868 0.1378 -0.0249 -0.0303 -0.0020 150 VAL   A C   
1198 O  O   . VAL   A 149 ? 0.1859 0.1016 0.1502 -0.0282 -0.0194 0.0163  150 VAL   A O   
1199 C  CB  . VAL   A 149 ? 0.1729 0.0963 0.1290 -0.0100 -0.0361 -0.0026 150 VAL   A CB  
1200 C  CG1 . VAL   A 149 ? 0.2024 0.1411 0.1275 -0.0057 -0.0238 -0.0291 150 VAL   A CG1 
1201 C  CG2 . VAL   A 149 ? 0.1775 0.1062 0.1496 -0.0099 -0.0347 0.0015  150 VAL   A CG2 
1202 N  N   . GLY   A 150 ? 0.1811 0.0952 0.1391 -0.0379 -0.0273 -0.0018 151 GLY   A N   
1203 C  CA  . GLY   A 150 ? 0.1892 0.1135 0.1502 -0.0421 -0.0225 0.0019  151 GLY   A CA  
1204 C  C   . GLY   A 150 ? 0.1771 0.1148 0.1435 -0.0421 -0.0198 -0.0059 151 GLY   A C   
1205 O  O   . GLY   A 150 ? 0.1535 0.1281 0.1477 -0.0350 -0.0155 -0.0256 151 GLY   A O   
1206 N  N   . SER   A 151 ? 0.1681 0.1433 0.1478 -0.0428 -0.0226 -0.0156 152 SER   A N   
1207 C  CA  . SER   A 151 ? 0.1524 0.1401 0.1761 -0.0454 -0.0213 -0.0172 152 SER   A CA  
1208 C  C   . SER   A 151 ? 0.1435 0.1397 0.1350 -0.0372 -0.0276 -0.0263 152 SER   A C   
1209 O  O   . SER   A 151 ? 0.1600 0.1353 0.1340 -0.0402 -0.0262 -0.0290 152 SER   A O   
1210 C  CB  . SER   A 151 ? 0.1626 0.1946 0.2204 -0.0354 -0.0045 0.0059  152 SER   A CB  
1211 O  OG  . SER   A 151 ? 0.2365 0.2608 0.3065 -0.0463 0.0269  0.0353  152 SER   A OG  
1212 N  N   . ALA   A 152 ? 0.1548 0.1253 0.1425 -0.0311 -0.0475 -0.0193 153 ALA   A N   
1213 C  CA  . ALA   A 152 ? 0.1512 0.1423 0.1350 -0.0161 -0.0338 -0.0082 153 ALA   A CA  
1214 C  C   . ALA   A 152 ? 0.1439 0.1317 0.1497 -0.0210 -0.0314 -0.0126 153 ALA   A C   
1215 O  O   . ALA   A 152 ? 0.1408 0.1596 0.1723 -0.0247 -0.0216 -0.0053 153 ALA   A O   
1216 C  CB  . ALA   A 152 ? 0.1849 0.1571 0.1474 -0.0153 -0.0407 0.0033  153 ALA   A CB  
1217 N  N   . LYS   A 153 ? 0.1402 0.1309 0.1721 -0.0159 -0.0125 -0.0035 154 LYS   A N   
1218 C  CA  . LYS   A 153 ? 0.1323 0.1346 0.1795 -0.0086 -0.0201 0.0038  154 LYS   A CA  
1219 C  C   . LYS   A 153 ? 0.1210 0.1676 0.1839 -0.0134 -0.0306 -0.0119 154 LYS   A C   
1220 O  O   . LYS   A 153 ? 0.1261 0.1511 0.1439 -0.0076 -0.0429 -0.0156 154 LYS   A O   
1221 C  CB  . LYS   A 153 ? 0.1562 0.1290 0.1682 -0.0101 -0.0365 0.0166  154 LYS   A CB  
1222 C  CG  . LYS   A 153 ? 0.1971 0.1293 0.2035 -0.0111 -0.0318 0.0113  154 LYS   A CG  
1223 C  CD  . LYS   A 153 ? 0.2354 0.1675 0.2288 0.0012  -0.0085 0.0066  154 LYS   A CD  
1224 C  CE  . LYS   A 153 ? 0.2760 0.1984 0.2463 0.0125  0.0052  0.0042  154 LYS   A CE  
1225 N  NZ  . LYS   A 153 ? 0.2915 0.2790 0.3229 -0.0050 0.0247  0.0156  154 LYS   A NZ  
1226 N  N   . PRO   A 154 ? 0.1243 0.2021 0.2081 -0.0199 -0.0472 0.0044  155 PRO   A N   
1227 C  CA  . PRO   A 154 ? 0.1320 0.2034 0.2135 -0.0185 -0.0623 0.0136  155 PRO   A CA  
1228 C  C   . PRO   A 154 ? 0.1263 0.1971 0.1882 0.0039  -0.0451 0.0289  155 PRO   A C   
1229 O  O   . PRO   A 154 ? 0.1465 0.2452 0.1922 -0.0017 -0.0648 0.0408  155 PRO   A O   
1230 C  CB  . PRO   A 154 ? 0.1422 0.2583 0.2546 -0.0124 -0.0672 0.0159  155 PRO   A CB  
1231 C  CG  . PRO   A 154 ? 0.1606 0.2802 0.2993 -0.0262 -0.0405 0.0240  155 PRO   A CG  
1232 C  CD  . PRO   A 154 ? 0.1267 0.2485 0.2693 -0.0261 -0.0244 0.0219  155 PRO   A CD  
1233 N  N   . GLY   A 155 ? 0.1449 0.1594 0.1816 0.0070  -0.0292 0.0326  156 GLY   A N   
1234 C  CA  . GLY   A 155 ? 0.1509 0.1665 0.2112 0.0128  -0.0209 0.0275  156 GLY   A CA  
1235 C  C   . GLY   A 155 ? 0.1573 0.1333 0.1943 0.0056  -0.0320 0.0174  156 GLY   A C   
1236 O  O   . GLY   A 155 ? 0.1616 0.1474 0.2809 0.0014  -0.0277 0.0106  156 GLY   A O   
1237 N  N   . LEU   A 156 ? 0.1310 0.1414 0.1414 -0.0023 -0.0368 -0.0027 157 LEU   A N   
1238 C  CA  . LEU   A 156 ? 0.1282 0.1266 0.1145 -0.0182 -0.0334 -0.0115 157 LEU   A CA  
1239 C  C   . LEU   A 156 ? 0.1323 0.1376 0.1067 -0.0169 -0.0413 -0.0148 157 LEU   A C   
1240 O  O   . LEU   A 156 ? 0.1438 0.1321 0.1067 -0.0266 -0.0297 -0.0097 157 LEU   A O   
1241 C  CB  . LEU   A 156 ? 0.1234 0.1230 0.1192 -0.0146 -0.0380 -0.0166 157 LEU   A CB  
1242 C  CG  . LEU   A 156 ? 0.1304 0.1374 0.1189 -0.0135 -0.0343 -0.0172 157 LEU   A CG  
1243 C  CD1 . LEU   A 156 ? 0.1378 0.1534 0.1206 -0.0273 -0.0299 -0.0176 157 LEU   A CD1 
1244 C  CD2 . LEU   A 156 ? 0.1243 0.1335 0.1489 0.0008  -0.0288 -0.0130 157 LEU   A CD2 
1245 N  N   . GLN   A 157 ? 0.1505 0.1544 0.1245 -0.0395 -0.0474 -0.0093 158 GLN   A N   
1246 C  CA  . GLN   A 157 ? 0.1742 0.1444 0.1291 -0.0366 -0.0538 -0.0203 158 GLN   A CA  
1247 C  C   . GLN   A 157 ? 0.1576 0.1349 0.1336 -0.0398 -0.0590 -0.0184 158 GLN   A C   
1248 O  O   . GLN   A 157 ? 0.1601 0.1543 0.1290 -0.0317 -0.0457 -0.0138 158 GLN   A O   
1249 C  CB  . GLN   A 157 ? 0.1865 0.1597 0.1582 -0.0402 -0.0673 -0.0141 158 GLN   A CB  
1250 C  CG  . GLN   A 157 ? 0.2130 0.1664 0.1666 -0.0321 -0.0650 -0.0212 158 GLN   A CG  
1251 C  CD  . GLN   A 157 ? 0.2062 0.1560 0.1635 -0.0341 -0.0513 -0.0141 158 GLN   A CD  
1252 O  OE1 . GLN   A 157 ? 0.1989 0.1458 0.1356 -0.0164 -0.0490 -0.0179 158 GLN   A OE1 
1253 N  NE2 . GLN   A 157 ? 0.2228 0.1835 0.1671 -0.0350 -0.0547 -0.0312 158 GLN   A NE2 
1254 N  N   . LYS   A 158 ? 0.1655 0.1619 0.1303 -0.0193 -0.0569 -0.0016 159 LYS   A N   
1255 C  CA  . LYS   A 158 ? 0.1721 0.1501 0.1468 -0.0080 -0.0630 0.0023  159 LYS   A CA  
1256 C  C   . LYS   A 158 ? 0.1640 0.1556 0.1125 -0.0120 -0.0503 -0.0044 159 LYS   A C   
1257 O  O   . LYS   A 158 ? 0.1746 0.1692 0.1214 -0.0267 -0.0484 -0.0072 159 LYS   A O   
1258 C  CB  . LYS   A 158 ? 0.2279 0.1676 0.1658 0.0071  -0.0550 0.0257  159 LYS   A CB  
1259 C  CG  . LYS   A 158 ? 0.2490 0.2383 0.2388 0.0219  -0.0726 0.0364  159 LYS   A CG  
1260 C  CD  . LYS   A 158 ? 0.3060 0.3092 0.3348 0.0407  -0.0572 0.0193  159 LYS   A CD  
1261 C  CE  . LYS   A 158 ? 0.3216 0.3542 0.3900 0.0301  -0.0729 0.0190  159 LYS   A CE  
1262 N  NZ  . LYS   A 158 ? 0.3410 0.3802 0.4130 0.0284  -0.0769 -0.0011 159 LYS   A NZ  
1263 N  N   . VAL   A 159 ? 0.1645 0.1351 0.1024 -0.0175 -0.0448 -0.0121 160 VAL   A N   
1264 C  CA  . VAL   A 159 ? 0.1637 0.1202 0.0995 -0.0242 -0.0454 -0.0022 160 VAL   A CA  
1265 C  C   . VAL   A 159 ? 0.1515 0.1182 0.0953 -0.0273 -0.0356 -0.0075 160 VAL   A C   
1266 O  O   . VAL   A 159 ? 0.1599 0.1192 0.1131 -0.0268 -0.0309 -0.0087 160 VAL   A O   
1267 C  CB  . VAL   A 159 ? 0.1633 0.1254 0.1001 -0.0304 -0.0435 -0.0036 160 VAL   A CB  
1268 C  CG1 . VAL   A 159 ? 0.1694 0.1357 0.1189 -0.0309 -0.0425 0.0036  160 VAL   A CG1 
1269 C  CG2 . VAL   A 159 ? 0.1807 0.1345 0.1061 -0.0202 -0.0372 -0.0008 160 VAL   A CG2 
1270 N  N   . VAL   A 160 ? 0.1587 0.1028 0.1034 -0.0249 -0.0377 -0.0148 161 VAL   A N   
1271 C  CA  . VAL   A 160 ? 0.1612 0.1093 0.1161 -0.0263 -0.0344 -0.0210 161 VAL   A CA  
1272 C  C   . VAL   A 160 ? 0.1743 0.1192 0.1330 -0.0303 -0.0365 -0.0222 161 VAL   A C   
1273 O  O   . VAL   A 160 ? 0.2013 0.1441 0.1318 -0.0246 -0.0172 -0.0356 161 VAL   A O   
1274 C  CB  . VAL   A 160 ? 0.1602 0.1159 0.1357 -0.0281 -0.0338 -0.0272 161 VAL   A CB  
1275 C  CG1 . VAL   A 160 ? 0.1698 0.1282 0.1589 -0.0178 -0.0332 -0.0327 161 VAL   A CG1 
1276 C  CG2 . VAL   A 160 ? 0.1685 0.1248 0.1450 -0.0336 -0.0240 -0.0160 161 VAL   A CG2 
1277 N  N   . ASP   A 161 ? 0.1866 0.1485 0.1085 -0.0279 -0.0462 -0.0206 162 ASP   A N   
1278 C  CA  . ASP   A 161 ? 0.2211 0.1860 0.1117 -0.0358 -0.0581 -0.0245 162 ASP   A CA  
1279 C  C   . ASP   A 161 ? 0.2392 0.1849 0.0921 -0.0287 -0.0576 -0.0198 162 ASP   A C   
1280 O  O   . ASP   A 161 ? 0.3284 0.2125 0.1146 -0.0540 -0.0217 -0.0505 162 ASP   A O   
1281 C  CB  . ASP   A 161 ? 0.2600 0.2695 0.1280 -0.0310 -0.0668 -0.0236 162 ASP   A CB  
1282 C  CG  . ASP   A 161 ? 0.2885 0.3445 0.1701 -0.0695 -0.0722 -0.0395 162 ASP   A CG  
1283 O  OD1 . ASP   A 161 ? 0.3751 0.3239 0.2833 -0.1377 -0.0624 -0.0255 162 ASP   A OD1 
1284 O  OD2 . ASP   A 161 ? 0.3404 0.5186 0.3005 -0.0537 -0.0419 -0.0399 162 ASP   A OD2 
1285 N  N   . VAL   A 162 ? 0.2179 0.1676 0.0850 -0.0200 -0.0526 -0.0126 163 VAL   A N   
1286 C  CA  . VAL   A 162 ? 0.2166 0.1749 0.0814 -0.0092 -0.0415 0.0062  163 VAL   A CA  
1287 C  C   . VAL   A 162 ? 0.2070 0.1462 0.0849 -0.0167 -0.0254 -0.0007 163 VAL   A C   
1288 O  O   . VAL   A 162 ? 0.2033 0.1580 0.0839 -0.0088 -0.0165 0.0083  163 VAL   A O   
1289 C  CB  . VAL   A 162 ? 0.2177 0.1681 0.1201 0.0018  -0.0316 0.0109  163 VAL   A CB  
1290 C  CG1 . VAL   A 162 ? 0.2308 0.1527 0.1189 -0.0049 -0.0154 0.0051  163 VAL   A CG1 
1291 C  CG2 . VAL   A 162 ? 0.2392 0.1799 0.1418 0.0217  -0.0191 0.0210  163 VAL   A CG2 
1292 N  N   . LEU   A 163 ? 0.1850 0.1372 0.0869 -0.0196 -0.0244 -0.0029 164 LEU   A N   
1293 C  CA  . LEU   A 163 ? 0.1880 0.1347 0.0862 -0.0214 -0.0159 -0.0090 164 LEU   A CA  
1294 C  C   . LEU   A 163 ? 0.1982 0.1450 0.0916 -0.0251 -0.0106 -0.0201 164 LEU   A C   
1295 O  O   . LEU   A 163 ? 0.1924 0.1478 0.1094 -0.0199 -0.0047 -0.0013 164 LEU   A O   
1296 C  CB  . LEU   A 163 ? 0.1698 0.1239 0.1157 -0.0178 -0.0219 0.0020  164 LEU   A CB  
1297 C  CG  . LEU   A 163 ? 0.1785 0.1293 0.1099 -0.0157 -0.0278 0.0263  164 LEU   A CG  
1298 C  CD1 . LEU   A 163 ? 0.1807 0.1428 0.1456 -0.0103 -0.0332 0.0386  164 LEU   A CD1 
1299 C  CD2 . LEU   A 163 ? 0.1792 0.1403 0.0974 -0.0161 -0.0149 0.0253  164 LEU   A CD2 
1300 N  N   . ASP   A 164 ? 0.2280 0.1898 0.1082 -0.0288 -0.0180 -0.0395 165 ASP   A N   
1301 C  CA  . ASP   A 164 ? 0.2659 0.2291 0.1323 -0.0187 -0.0054 -0.0519 165 ASP   A CA  
1302 C  C   . ASP   A 164 ? 0.2656 0.2507 0.1024 -0.0173 0.0020  -0.0254 165 ASP   A C   
1303 O  O   . ASP   A 164 ? 0.2799 0.2877 0.1528 -0.0269 0.0452  -0.0386 165 ASP   A O   
1304 C  CB  . ASP   A 164 ? 0.3290 0.2800 0.1695 -0.0320 -0.0073 -0.0931 165 ASP   A CB  
1305 C  CG  . ASP   A 164 ? 0.3939 0.3242 0.2916 -0.0583 -0.0303 -0.0794 165 ASP   A CG  
1306 O  OD1 . ASP   A 164 ? 0.4151 0.4024 0.3992 -0.0676 -0.0218 -0.0574 165 ASP   A OD1 
1307 O  OD2 . ASP   A 164 ? 0.4920 0.3764 0.3335 -0.0390 -0.0272 -0.1407 165 ASP   A OD2 
1308 N  N   . SER   A 165 ? 0.2189 0.2202 0.0718 -0.0225 -0.0261 -0.0026 166 SER   A N   
1309 C  CA  . SER   A 165 ? 0.2480 0.2335 0.0964 -0.0149 -0.0257 0.0134  166 SER   A CA  
1310 C  C   . SER   A 165 ? 0.2198 0.2019 0.0819 -0.0061 -0.0207 0.0322  166 SER   A C   
1311 O  O   . SER   A 165 ? 0.2353 0.2112 0.0981 -0.0038 -0.0129 0.0435  166 SER   A O   
1312 C  CB  . SER   A 165 ? 0.2681 0.2502 0.1508 -0.0073 -0.0162 0.0293  166 SER   A CB  
1313 O  OG  . SER   A 165 ? 0.2827 0.2389 0.1815 0.0068  -0.0243 0.0203  166 SER   A OG  
1314 N  N   . ILE   A 166 ? 0.1902 0.1473 0.0628 -0.0158 -0.0063 0.0211  167 ILE   A N   
1315 C  CA  . ILE   A 166 ? 0.1803 0.1413 0.0759 -0.0071 -0.0050 0.0120  167 ILE   A CA  
1316 C  C   . ILE   A 166 ? 0.1741 0.1226 0.0686 -0.0242 -0.0038 0.0003  167 ILE   A C   
1317 O  O   . ILE   A 166 ? 0.1668 0.1169 0.0694 -0.0197 0.0033  -0.0007 167 ILE   A O   
1318 C  CB  . ILE   A 166 ? 0.1871 0.1293 0.0853 -0.0111 -0.0152 0.0043  167 ILE   A CB  
1319 C  CG1 . ILE   A 166 ? 0.1737 0.1453 0.0756 -0.0172 -0.0111 -0.0079 167 ILE   A CG1 
1320 C  CG2 . ILE   A 166 ? 0.1934 0.1422 0.1178 -0.0003 -0.0136 0.0114  167 ILE   A CG2 
1321 C  CD1 . ILE   A 166 ? 0.1831 0.1379 0.0893 -0.0290 -0.0039 -0.0232 167 ILE   A CD1 
1322 N  N   . LYS   A 167 ? 0.1764 0.1323 0.0718 -0.0104 -0.0045 -0.0027 168 LYS   A N   
1323 C  CA  . LYS   A 167 ? 0.1715 0.1347 0.0820 -0.0149 0.0023  -0.0149 168 LYS   A CA  
1324 C  C   . LYS   A 167 ? 0.1740 0.1098 0.0798 -0.0221 0.0118  0.0013  168 LYS   A C   
1325 O  O   . LYS   A 167 ? 0.1703 0.1118 0.0966 -0.0203 -0.0034 0.0037  168 LYS   A O   
1326 C  CB  . LYS   A 167 ? 0.2049 0.1545 0.0982 -0.0169 -0.0103 -0.0291 168 LYS   A CB  
1327 C  CG  . LYS   A 167 ? 0.2438 0.1910 0.1758 0.0012  -0.0031 -0.0212 168 LYS   A CG  
1328 C  CD  . LYS   A 167 ? 0.3085 0.2085 0.2437 0.0098  0.0046  -0.0425 168 LYS   A CD  
1329 C  CE  . LYS   A 167 ? 0.3603 0.2548 0.2924 0.0305  -0.0062 -0.0349 168 LYS   A CE  
1330 N  NZ  . LYS   A 167 ? 0.3932 0.2654 0.3654 0.0342  0.0086  -0.0646 168 LYS   A NZ  
1331 N  N   . THR   A 168 ? 0.1612 0.1177 0.0801 -0.0181 0.0179  0.0147  169 THR   A N   
1332 C  CA  . THR   A 168 ? 0.1541 0.1203 0.0821 -0.0160 0.0256  0.0105  169 THR   A CA  
1333 C  C   . THR   A 168 ? 0.1488 0.1269 0.0741 -0.0141 0.0189  0.0066  169 THR   A C   
1334 O  O   . THR   A 168 ? 0.1556 0.1202 0.0954 -0.0169 0.0257  0.0198  169 THR   A O   
1335 C  CB  . THR   A 168 ? 0.1632 0.1501 0.0898 -0.0076 0.0331  0.0128  169 THR   A CB  
1336 O  OG1 . THR   A 168 ? 0.1691 0.1672 0.0943 -0.0091 0.0338  0.0102  169 THR   A OG1 
1337 C  CG2 . THR   A 168 ? 0.1781 0.1532 0.1099 -0.0005 0.0337  0.0036  169 THR   A CG2 
1338 N  N   . LYS   A 169 ? 0.1541 0.1320 0.1017 -0.0080 0.0262  0.0051  170 LYS   A N   
1339 C  CA  . LYS   A 169 ? 0.1591 0.1257 0.0965 -0.0306 0.0231  0.0140  170 LYS   A CA  
1340 C  C   . LYS   A 169 ? 0.1704 0.1402 0.1043 -0.0334 0.0358  0.0296  170 LYS   A C   
1341 O  O   . LYS   A 169 ? 0.1874 0.1576 0.1024 -0.0381 0.0410  0.0174  170 LYS   A O   
1342 C  CB  . LYS   A 169 ? 0.1694 0.1416 0.1168 -0.0387 0.0217  0.0160  170 LYS   A CB  
1343 C  CG  . LYS   A 169 ? 0.1798 0.1743 0.1342 -0.0515 0.0206  0.0141  170 LYS   A CG  
1344 C  CD  . LYS   A 169 ? 0.2127 0.2132 0.1862 -0.0313 0.0103  0.0024  170 LYS   A CD  
1345 C  CE  . LYS   A 169 ? 0.2380 0.2915 0.2399 -0.0218 -0.0023 -0.0126 170 LYS   A CE  
1346 N  NZ  . LYS   A 169 ? 0.2812 0.3378 0.2985 0.0031  -0.0118 -0.0131 170 LYS   A NZ  
1347 N  N   . GLY   A 170 ? 0.1954 0.1150 0.1124 -0.0351 0.0310  0.0259  171 GLY   A N   
1348 C  CA  . GLY   A 170 ? 0.2068 0.1101 0.1409 -0.0326 0.0122  0.0288  171 GLY   A CA  
1349 C  C   . GLY   A 170 ? 0.2080 0.1129 0.1281 -0.0297 0.0109  0.0367  171 GLY   A C   
1350 O  O   . GLY   A 170 ? 0.2661 0.1247 0.1754 -0.0297 0.0062  0.0565  171 GLY   A O   
1351 N  N   . LYS   A 171 ? 0.1741 0.1101 0.1149 -0.0229 0.0157  0.0411  172 LYS   A N   
1352 C  CA  . LYS   A 171 ? 0.1857 0.1264 0.1154 -0.0164 0.0122  0.0460  172 LYS   A CA  
1353 C  C   . LYS   A 171 ? 0.1883 0.1441 0.0788 -0.0057 0.0108  0.0408  172 LYS   A C   
1354 O  O   . LYS   A 171 ? 0.1766 0.1332 0.0683 -0.0070 0.0076  0.0302  172 LYS   A O   
1355 C  CB  . LYS   A 171 ? 0.1946 0.1594 0.0975 -0.0195 0.0232  0.0176  172 LYS   A CB  
1356 C  CG  . LYS   A 171 ? 0.2036 0.2015 0.1117 -0.0103 0.0286  0.0028  172 LYS   A CG  
1357 C  CD  . LYS   A 171 ? 0.2694 0.2377 0.1879 -0.0125 0.0008  -0.0152 172 LYS   A CD  
1358 C  CE  . LYS   A 171 ? 0.3334 0.3117 0.2195 0.0102  0.0200  -0.0307 172 LYS   A CE  
1359 N  NZ  . LYS   A 171 ? 0.4007 0.3553 0.2850 0.0270  0.0082  -0.0233 172 LYS   A NZ  
1360 N  N   . SER   A 172 ? 0.2045 0.1661 0.0783 0.0114  0.0083  0.0539  173 SER   A N   
1361 C  CA  . SER   A 172 ? 0.1992 0.1748 0.0734 0.0211  0.0173  0.0325  173 SER   A CA  
1362 C  C   . SER   A 172 ? 0.1959 0.1741 0.0697 0.0208  -0.0059 0.0515  173 SER   A C   
1363 O  O   . SER   A 172 ? 0.2153 0.2030 0.0681 0.0231  -0.0001 0.0353  173 SER   A O   
1364 C  CB  . SER   A 172 ? 0.2075 0.1787 0.0862 0.0256  0.0085  0.0303  173 SER   A CB  
1365 O  OG  . SER   A 172 ? 0.2370 0.1948 0.1342 0.0163  0.0058  0.0496  173 SER   A OG  
1366 N  N   . ALA   A 173 ? 0.1891 0.1755 0.0734 0.0212  -0.0141 0.0311  174 ALA   A N   
1367 C  CA  . ALA   A 173 ? 0.1939 0.1822 0.0731 0.0134  -0.0227 0.0344  174 ALA   A CA  
1368 C  C   . ALA   A 173 ? 0.1834 0.1619 0.0678 0.0047  -0.0266 0.0246  174 ALA   A C   
1369 O  O   . ALA   A 173 ? 0.1828 0.1415 0.0674 0.0160  -0.0221 0.0273  174 ALA   A O   
1370 C  CB  . ALA   A 173 ? 0.2109 0.1853 0.0869 0.0153  -0.0237 0.0071  174 ALA   A CB  
1371 N  N   . ASP   A 174 ? 0.1983 0.1856 0.0747 0.0062  -0.0285 0.0356  175 ASP   A N   
1372 C  CA  . ASP   A 174 ? 0.2025 0.1858 0.1061 0.0176  -0.0437 0.0164  175 ASP   A CA  
1373 C  C   . ASP   A 174 ? 0.1972 0.1547 0.1334 0.0151  -0.0360 0.0022  175 ASP   A C   
1374 O  O   . ASP   A 174 ? 0.2263 0.2008 0.1730 -0.0069 -0.0247 -0.0374 175 ASP   A O   
1375 C  CB  . ASP   A 174 ? 0.2367 0.2188 0.1475 0.0195  -0.0597 0.0496  175 ASP   A CB  
1376 C  CG  . ASP   A 174 ? 0.2663 0.2494 0.1737 -0.0208 -0.0751 0.0703  175 ASP   A CG  
1377 O  OD1 . ASP   A 174 ? 0.3661 0.3030 0.2471 -0.0725 -0.0939 0.0713  175 ASP   A OD1 
1378 O  OD2 . ASP   A 174 ? 0.3196 0.2822 0.2059 -0.0265 -0.0412 0.0849  175 ASP   A OD2 
1379 N  N   . PHE   A 175 ? 0.1769 0.1510 0.1314 -0.0039 -0.0128 -0.0024 176 PHE   A N   
1380 C  CA  . PHE   A 175 ? 0.1680 0.1406 0.1459 0.0010  -0.0313 0.0089  176 PHE   A CA  
1381 C  C   . PHE   A 175 ? 0.1823 0.1429 0.1072 0.0021  -0.0421 0.0212  176 PHE   A C   
1382 O  O   . PHE   A 175 ? 0.2151 0.2101 0.1138 0.0564  -0.0718 -0.0058 176 PHE   A O   
1383 C  CB  . PHE   A 175 ? 0.1585 0.1374 0.1670 -0.0054 -0.0277 0.0039  176 PHE   A CB  
1384 C  CG  . PHE   A 175 ? 0.1810 0.1312 0.1572 -0.0024 -0.0156 0.0035  176 PHE   A CG  
1385 C  CD1 . PHE   A 175 ? 0.2170 0.1402 0.1644 -0.0070 0.0017  -0.0040 176 PHE   A CD1 
1386 C  CD2 . PHE   A 175 ? 0.1788 0.1396 0.1423 -0.0008 -0.0390 -0.0106 176 PHE   A CD2 
1387 C  CE1 . PHE   A 175 ? 0.2346 0.1317 0.1738 -0.0085 0.0035  -0.0061 176 PHE   A CE1 
1388 C  CE2 . PHE   A 175 ? 0.1969 0.1418 0.1450 -0.0013 -0.0229 -0.0024 176 PHE   A CE2 
1389 C  CZ  . PHE   A 175 ? 0.1972 0.1201 0.1548 -0.0153 -0.0094 0.0022  176 PHE   A CZ  
1390 N  N   . THR   A 176 ? 0.2016 0.1662 0.0747 0.0219  -0.0480 0.0351  177 THR   A N   
1391 C  CA  . THR   A 176 ? 0.1727 0.1616 0.0760 0.0241  -0.0444 0.0375  177 THR   A CA  
1392 C  C   . THR   A 176 ? 0.1830 0.1286 0.0892 0.0119  -0.0553 0.0470  177 THR   A C   
1393 O  O   . THR   A 176 ? 0.2119 0.1282 0.0964 0.0010  -0.0482 0.0323  177 THR   A O   
1394 C  CB  . THR   A 176 ? 0.2003 0.1818 0.0969 0.0218  -0.0395 0.0585  177 THR   A CB  
1395 O  OG1 . THR   A 176 ? 0.3086 0.2159 0.0845 0.0737  -0.0703 0.0624  177 THR   A OG1 
1396 C  CG2 . THR   A 176 ? 0.2248 0.2117 0.1922 0.0278  -0.0129 0.0773  177 THR   A CG2 
1397 N  N   . ASN   A 177 ? 0.1732 0.1371 0.1022 0.0138  -0.0483 0.0371  178 ASN   A N   
1398 C  CA  . ASN   A 177 ? 0.1663 0.1619 0.1133 0.0030  -0.0528 0.0482  178 ASN   A CA  
1399 C  C   . ASN   A 177 ? 0.1649 0.1554 0.1088 -0.0163 -0.0584 0.0546  178 ASN   A C   
1400 O  O   . ASN   A 177 ? 0.1868 0.1790 0.1991 -0.0423 -0.0610 0.0790  178 ASN   A O   
1401 C  CB  . ASN   A 177 ? 0.1788 0.1618 0.1348 0.0012  -0.0667 0.0516  178 ASN   A CB  
1402 C  CG  . ASN   A 177 ? 0.1888 0.1737 0.1361 0.0097  -0.0694 0.0447  178 ASN   A CG  
1403 O  OD1 . ASN   A 177 ? 0.1926 0.1861 0.1878 0.0309  -0.0327 0.0434  178 ASN   A OD1 
1404 N  ND2 . ASN   A 177 ? 0.2122 0.1560 0.1424 0.0115  -0.0756 0.0661  178 ASN   A ND2 
1405 N  N   . PHE   A 178 ? 0.1726 0.1276 0.0915 -0.0018 -0.0532 0.0373  179 PHE   A N   
1406 C  CA  . PHE   A 178 ? 0.1812 0.1318 0.0807 -0.0046 -0.0503 0.0323  179 PHE   A CA  
1407 C  C   . PHE   A 178 ? 0.1586 0.1328 0.0835 -0.0015 -0.0497 0.0154  179 PHE   A C   
1408 O  O   . PHE   A 178 ? 0.1930 0.1428 0.0935 -0.0139 -0.0412 0.0187  179 PHE   A O   
1409 C  CB  . PHE   A 178 ? 0.1895 0.1421 0.0890 -0.0035 -0.0279 0.0282  179 PHE   A CB  
1410 C  CG  . PHE   A 178 ? 0.1663 0.1398 0.0873 0.0101  -0.0353 0.0366  179 PHE   A CG  
1411 C  CD1 . PHE   A 178 ? 0.1807 0.1412 0.1041 0.0116  -0.0320 0.0237  179 PHE   A CD1 
1412 C  CD2 . PHE   A 178 ? 0.1369 0.1399 0.0911 0.0190  -0.0319 0.0349  179 PHE   A CD2 
1413 C  CE1 . PHE   A 178 ? 0.1904 0.1368 0.1232 0.0188  -0.0300 0.0296  179 PHE   A CE1 
1414 C  CE2 . PHE   A 178 ? 0.1357 0.1463 0.0830 0.0100  -0.0313 0.0384  179 PHE   A CE2 
1415 C  CZ  . PHE   A 178 ? 0.1509 0.1319 0.1076 0.0090  -0.0255 0.0439  179 PHE   A CZ  
1416 N  N   . ASP   A 179 ? 0.1487 0.1273 0.1078 0.0113  -0.0433 0.0221  180 ASP   A N   
1417 C  CA  . ASP   A 179 ? 0.1383 0.1305 0.1091 0.0160  -0.0413 0.0196  180 ASP   A CA  
1418 C  C   . ASP   A 179 ? 0.1158 0.1240 0.0967 0.0066  -0.0320 0.0186  180 ASP   A C   
1419 O  O   . ASP   A 179 ? 0.1299 0.1296 0.1006 -0.0001 -0.0360 0.0116  180 ASP   A O   
1420 C  CB  . ASP   A 179 ? 0.1307 0.1719 0.1342 0.0168  -0.0519 0.0215  180 ASP   A CB  
1421 C  CG  . ASP   A 179 ? 0.1463 0.1913 0.1473 0.0192  -0.0459 0.0129  180 ASP   A CG  
1422 O  OD1 . ASP   A 179 ? 0.1382 0.1641 0.1331 0.0341  -0.0310 0.0172  180 ASP   A OD1 
1423 O  OD2 . ASP   A 179 ? 0.1594 0.2868 0.2319 -0.0201 -0.0379 -0.0165 180 ASP   A OD2 
1424 N  N   . PRO   A 180 ? 0.1136 0.1193 0.0921 0.0089  -0.0346 0.0181  181 PRO   A N   
1425 C  CA  . PRO   A 180 ? 0.1102 0.1327 0.0861 0.0057  -0.0350 0.0208  181 PRO   A CA  
1426 C  C   . PRO   A 180 ? 0.1022 0.1343 0.0802 0.0134  -0.0325 0.0260  181 PRO   A C   
1427 O  O   . PRO   A 180 ? 0.1013 0.1324 0.0966 0.0084  -0.0364 0.0310  181 PRO   A O   
1428 C  CB  . PRO   A 180 ? 0.1223 0.1404 0.0954 -0.0002 -0.0287 0.0159  181 PRO   A CB  
1429 C  CG  . PRO   A 180 ? 0.1359 0.1374 0.0910 0.0011  -0.0315 0.0215  181 PRO   A CG  
1430 C  CD  . PRO   A 180 ? 0.1286 0.1276 0.0993 0.0039  -0.0359 0.0249  181 PRO   A CD  
1431 N  N   . ARG   A 181 ? 0.1004 0.1335 0.0987 0.0181  -0.0295 0.0255  182 ARG   A N   
1432 C  CA  . ARG   A 181 ? 0.1022 0.1323 0.1124 0.0136  -0.0261 0.0238  182 ARG   A CA  
1433 C  C   . ARG   A 181 ? 0.0954 0.1360 0.1101 0.0137  -0.0316 0.0156  182 ARG   A C   
1434 O  O   . ARG   A 181 ? 0.1034 0.1350 0.1311 0.0091  -0.0238 0.0333  182 ARG   A O   
1435 C  CB  . ARG   A 181 ? 0.1112 0.1348 0.1413 0.0122  -0.0150 0.0178  182 ARG   A CB  
1436 C  CG  . ARG   A 181 ? 0.1408 0.1451 0.1552 0.0244  0.0069  0.0114  182 ARG   A CG  
1437 C  CD  . ARG   A 181 ? 0.1563 0.1653 0.1942 0.0415  0.0241  0.0343  182 ARG   A CD  
1438 N  NE  . ARG   A 181 ? 0.1912 0.2034 0.2177 0.0781  0.0014  0.0421  182 ARG   A NE  
1439 C  CZ  . ARG   A 181 ? 0.2262 0.2587 0.2376 0.1142  -0.0063 0.0389  182 ARG   A CZ  
1440 N  NH1 . ARG   A 181 ? 0.2222 0.2690 0.2625 0.1201  0.0032  0.0477  182 ARG   A NH1 
1441 N  NH2 . ARG   A 181 ? 0.2870 0.2862 0.2627 0.1608  -0.0115 0.0426  182 ARG   A NH2 
1442 N  N   . GLY   A 182 ? 0.1065 0.1276 0.1151 0.0090  -0.0398 0.0189  183 GLY   A N   
1443 C  CA  . GLY   A 182 ? 0.1180 0.1267 0.1167 0.0016  -0.0493 0.0114  183 GLY   A CA  
1444 C  C   . GLY   A 182 ? 0.1050 0.1191 0.1189 0.0000  -0.0483 0.0123  183 GLY   A C   
1445 O  O   . GLY   A 182 ? 0.1409 0.1187 0.1771 0.0034  -0.0493 0.0019  183 GLY   A O   
1446 N  N   . LEU   A 183 ? 0.1003 0.1172 0.1032 0.0077  -0.0474 0.0136  184 LEU   A N   
1447 C  CA  . LEU   A 183 ? 0.0977 0.1195 0.1101 0.0065  -0.0399 0.0206  184 LEU   A CA  
1448 C  C   . LEU   A 183 ? 0.0950 0.1111 0.1053 -0.0034 -0.0379 0.0258  184 LEU   A C   
1449 O  O   . LEU   A 183 ? 0.1084 0.1452 0.1195 0.0103  -0.0294 0.0407  184 LEU   A O   
1450 C  CB  . LEU   A 183 ? 0.1100 0.1332 0.0986 0.0098  -0.0377 0.0246  184 LEU   A CB  
1451 C  CG  . LEU   A 183 ? 0.1362 0.1596 0.1000 0.0075  -0.0363 0.0268  184 LEU   A CG  
1452 C  CD1 . LEU   A 183 ? 0.1433 0.1936 0.1113 0.0106  -0.0387 0.0353  184 LEU   A CD1 
1453 C  CD2 . LEU   A 183 ? 0.1943 0.1810 0.1100 0.0082  -0.0192 -0.0013 184 LEU   A CD2 
1454 N  N   . LEU   A 184 ? 0.0955 0.1167 0.1016 0.0009  -0.0341 0.0205  185 LEU   A N   
1455 C  CA  . LEU   A 184 ? 0.0878 0.1254 0.1023 -0.0139 -0.0339 0.0210  185 LEU   A CA  
1456 C  C   . LEU   A 184 ? 0.1005 0.1405 0.1073 -0.0273 -0.0360 0.0266  185 LEU   A C   
1457 O  O   . LEU   A 184 ? 0.1304 0.1754 0.1312 -0.0452 -0.0586 0.0316  185 LEU   A O   
1458 C  CB  . LEU   A 184 ? 0.0994 0.1332 0.1050 -0.0095 -0.0313 0.0124  185 LEU   A CB  
1459 C  CG  . LEU   A 184 ? 0.1042 0.1327 0.1284 0.0060  -0.0373 0.0063  185 LEU   A CG  
1460 C  CD1 . LEU   A 184 ? 0.1269 0.1380 0.1364 0.0107  -0.0230 -0.0009 185 LEU   A CD1 
1461 C  CD2 . LEU   A 184 ? 0.1113 0.1449 0.1702 0.0055  -0.0507 0.0117  185 LEU   A CD2 
1462 N  N   . PRO   A 185 ? 0.0828 0.1260 0.1042 -0.0140 -0.0246 0.0231  186 PRO   A N   
1463 C  CA  . PRO   A 185 ? 0.1044 0.1100 0.1141 -0.0119 -0.0196 0.0213  186 PRO   A CA  
1464 C  C   . PRO   A 185 ? 0.0844 0.1184 0.1289 -0.0173 -0.0320 0.0208  186 PRO   A C   
1465 O  O   . PRO   A 185 ? 0.0718 0.1164 0.1710 -0.0111 -0.0274 0.0256  186 PRO   A O   
1466 C  CB  . PRO   A 185 ? 0.0973 0.1336 0.1228 -0.0018 -0.0094 0.0226  186 PRO   A CB  
1467 C  CG  . PRO   A 185 ? 0.0894 0.1263 0.1020 0.0122  -0.0160 0.0186  186 PRO   A CG  
1468 C  CD  . PRO   A 185 ? 0.0864 0.1135 0.0989 0.0056  -0.0247 0.0160  186 PRO   A CD  
1469 N  N   A GLU   A 186 ? 0.0859 0.1314 0.1408 -0.0231 -0.0208 0.0160  187 GLU   A N   
1470 N  N   B GLU   A 186 ? 0.0943 0.1252 0.1375 -0.0240 -0.0261 0.0183  187 GLU   A N   
1471 C  CA  A GLU   A 186 ? 0.0757 0.1427 0.1513 -0.0172 -0.0254 0.0130  187 GLU   A CA  
1472 C  CA  B GLU   A 186 ? 0.0825 0.1258 0.1452 -0.0207 -0.0324 0.0135  187 GLU   A CA  
1473 C  C   A GLU   A 186 ? 0.0657 0.1512 0.1394 -0.0019 -0.0215 0.0123  187 GLU   A C   
1474 C  C   B GLU   A 186 ? 0.0782 0.1433 0.1363 -0.0035 -0.0270 0.0146  187 GLU   A C   
1475 O  O   A GLU   A 186 ? 0.0804 0.1766 0.1523 0.0164  -0.0080 -0.0018 187 GLU   A O   
1476 O  O   B GLU   A 186 ? 0.0950 0.1756 0.1493 0.0178  -0.0158 0.0103  187 GLU   A O   
1477 C  CB  A GLU   A 186 ? 0.0852 0.1536 0.1794 -0.0240 -0.0219 0.0089  187 GLU   A CB  
1478 C  CB  B GLU   A 186 ? 0.0879 0.1216 0.1675 -0.0242 -0.0347 0.0045  187 GLU   A CB  
1479 C  CG  A GLU   A 186 ? 0.1100 0.1735 0.2064 -0.0154 -0.0027 0.0098  187 GLU   A CG  
1480 C  CG  B GLU   A 186 ? 0.1092 0.1133 0.1780 -0.0258 -0.0468 0.0020  187 GLU   A CG  
1481 C  CD  A GLU   A 186 ? 0.1373 0.1794 0.2339 -0.0151 0.0060  0.0019  187 GLU   A CD  
1482 C  CD  B GLU   A 186 ? 0.1464 0.1218 0.2098 -0.0315 -0.0392 0.0081  187 GLU   A CD  
1483 O  OE1 A GLU   A 186 ? 0.1646 0.1751 0.2425 -0.0106 0.0015  -0.0107 187 GLU   A OE1 
1484 O  OE1 B GLU   A 186 ? 0.1715 0.1386 0.2144 -0.0282 -0.0404 0.0038  187 GLU   A OE1 
1485 O  OE2 A GLU   A 186 ? 0.1920 0.2366 0.2491 -0.0053 0.0230  0.0546  187 GLU   A OE2 
1486 O  OE2 B GLU   A 186 ? 0.1733 0.1329 0.2277 -0.0233 -0.0458 0.0031  187 GLU   A OE2 
1487 N  N   . SER   A 187 ? 0.0603 0.1442 0.1319 -0.0083 -0.0248 0.0079  188 SER   A N   
1488 C  CA  . SER   A 187 ? 0.0703 0.1505 0.1329 -0.0118 -0.0201 0.0106  188 SER   A CA  
1489 C  C   . SER   A 187 ? 0.0537 0.1461 0.1349 -0.0103 -0.0134 0.0052  188 SER   A C   
1490 O  O   . SER   A 187 ? 0.0672 0.1554 0.1415 -0.0093 -0.0128 -0.0121 188 SER   A O   
1491 C  CB  . SER   A 187 ? 0.0884 0.1632 0.1403 -0.0106 -0.0219 0.0245  188 SER   A CB  
1492 O  OG  . SER   A 187 ? 0.0957 0.1658 0.1432 -0.0228 -0.0223 0.0238  188 SER   A OG  
1493 N  N   . LEU   A 188 ? 0.0559 0.1363 0.1255 -0.0140 -0.0185 0.0028  189 LEU   A N   
1494 C  CA  . LEU   A 188 ? 0.0580 0.1341 0.1396 -0.0124 -0.0201 0.0131  189 LEU   A CA  
1495 C  C   . LEU   A 188 ? 0.0694 0.1295 0.1231 -0.0072 -0.0224 -0.0028 189 LEU   A C   
1496 O  O   . LEU   A 188 ? 0.0998 0.1313 0.1399 -0.0128 -0.0316 -0.0018 189 LEU   A O   
1497 C  CB  . LEU   A 188 ? 0.0845 0.1493 0.1860 -0.0072 -0.0325 0.0300  189 LEU   A CB  
1498 C  CG  . LEU   A 188 ? 0.0777 0.1515 0.2103 0.0021  -0.0424 0.0337  189 LEU   A CG  
1499 C  CD1 . LEU   A 188 ? 0.1143 0.1519 0.2480 0.0099  -0.0444 0.0270  189 LEU   A CD1 
1500 C  CD2 . LEU   A 188 ? 0.1097 0.1802 0.2154 0.0102  -0.0428 0.0389  189 LEU   A CD2 
1501 N  N   . ASP   A 189 ? 0.0598 0.1268 0.1009 -0.0130 -0.0097 -0.0032 190 ASP   A N   
1502 C  CA  . ASP   A 189 ? 0.0644 0.1349 0.0943 -0.0078 -0.0029 -0.0046 190 ASP   A CA  
1503 C  C   . ASP   A 189 ? 0.0571 0.1113 0.0815 -0.0014 -0.0045 -0.0031 190 ASP   A C   
1504 O  O   . ASP   A 189 ? 0.0571 0.1201 0.0846 -0.0089 -0.0084 -0.0076 190 ASP   A O   
1505 C  CB  . ASP   A 189 ? 0.0936 0.1579 0.1257 -0.0360 -0.0041 0.0103  190 ASP   A CB  
1506 C  CG  . ASP   A 189 ? 0.1253 0.1976 0.1590 -0.0470 0.0108  0.0180  190 ASP   A CG  
1507 O  OD1 . ASP   A 189 ? 0.1075 0.2739 0.1833 -0.0234 0.0104  -0.0083 190 ASP   A OD1 
1508 O  OD2 . ASP   A 189 ? 0.1640 0.2525 0.2391 -0.0781 0.0237  0.0382  190 ASP   A OD2 
1509 N  N   . TYR   A 190 ? 0.0533 0.1059 0.0721 -0.0051 -0.0005 0.0054  191 TYR   A N   
1510 C  CA  . TYR   A 190 ? 0.0512 0.0978 0.0649 -0.0045 -0.0015 0.0119  191 TYR   A CA  
1511 C  C   . TYR   A 190 ? 0.0598 0.0812 0.0653 -0.0017 0.0000  0.0161  191 TYR   A C   
1512 O  O   . TYR   A 190 ? 0.0647 0.0993 0.0663 -0.0008 0.0070  0.0112  191 TYR   A O   
1513 C  CB  . TYR   A 190 ? 0.0559 0.1042 0.0679 -0.0008 -0.0048 0.0165  191 TYR   A CB  
1514 C  CG  . TYR   A 190 ? 0.0696 0.0947 0.0750 -0.0073 -0.0070 0.0148  191 TYR   A CG  
1515 C  CD1 . TYR   A 190 ? 0.0700 0.0941 0.0867 -0.0072 -0.0110 0.0112  191 TYR   A CD1 
1516 C  CD2 . TYR   A 190 ? 0.0719 0.1082 0.0780 -0.0019 -0.0108 0.0166  191 TYR   A CD2 
1517 C  CE1 . TYR   A 190 ? 0.0824 0.0914 0.0914 -0.0084 -0.0075 0.0082  191 TYR   A CE1 
1518 C  CE2 . TYR   A 190 ? 0.0781 0.0992 0.0935 0.0063  -0.0101 0.0147  191 TYR   A CE2 
1519 C  CZ  . TYR   A 190 ? 0.0878 0.0915 0.0908 0.0027  -0.0086 0.0125  191 TYR   A CZ  
1520 O  OH  . TYR   A 190 ? 0.1121 0.0964 0.1026 0.0082  -0.0091 -0.0030 191 TYR   A OH  
1521 N  N   . TRP   A 191 ? 0.0635 0.0835 0.0502 0.0002  -0.0057 0.0074  192 TRP   A N   
1522 C  CA  . TRP   A 191 ? 0.0574 0.0800 0.0578 0.0011  -0.0037 0.0069  192 TRP   A CA  
1523 C  C   . TRP   A 191 ? 0.0647 0.0819 0.0513 0.0040  -0.0070 0.0037  192 TRP   A C   
1524 O  O   . TRP   A 191 ? 0.0869 0.0940 0.0533 -0.0117 -0.0017 0.0058  192 TRP   A O   
1525 C  CB  . TRP   A 191 ? 0.0648 0.0832 0.0752 0.0043  -0.0075 0.0037  192 TRP   A CB  
1526 C  CG  . TRP   A 191 ? 0.0656 0.0862 0.0805 0.0095  -0.0098 0.0167  192 TRP   A CG  
1527 C  CD1 . TRP   A 191 ? 0.0919 0.0941 0.0841 0.0083  -0.0090 0.0132  192 TRP   A CD1 
1528 C  CD2 . TRP   A 191 ? 0.0640 0.0825 0.0946 0.0053  -0.0164 0.0098  192 TRP   A CD2 
1529 N  NE1 . TRP   A 191 ? 0.1028 0.0826 0.1127 0.0083  -0.0061 0.0280  192 TRP   A NE1 
1530 C  CE2 . TRP   A 191 ? 0.0838 0.0867 0.1228 0.0102  -0.0114 0.0169  192 TRP   A CE2 
1531 C  CE3 . TRP   A 191 ? 0.0772 0.1014 0.1061 0.0094  -0.0184 -0.0094 192 TRP   A CE3 
1532 C  CZ2 . TRP   A 191 ? 0.1042 0.0904 0.1561 0.0047  -0.0128 0.0091  192 TRP   A CZ2 
1533 C  CZ3 . TRP   A 191 ? 0.0879 0.1203 0.1317 0.0076  -0.0160 -0.0267 192 TRP   A CZ3 
1534 C  CH2 . TRP   A 191 ? 0.1036 0.1054 0.1645 -0.0054 -0.0191 -0.0207 192 TRP   A CH2 
1535 N  N   . THR   A 192 ? 0.0617 0.0850 0.0435 -0.0059 -0.0026 0.0065  193 THR   A N   
1536 C  CA  . THR   A 192 ? 0.0624 0.0775 0.0450 0.0020  -0.0038 0.0035  193 THR   A CA  
1537 C  C   . THR   A 192 ? 0.0625 0.0832 0.0464 0.0083  -0.0066 0.0010  193 THR   A C   
1538 O  O   . THR   A 192 ? 0.0683 0.0988 0.0496 0.0040  -0.0063 0.0013  193 THR   A O   
1539 C  CB  . THR   A 192 ? 0.0620 0.0751 0.0615 0.0055  -0.0022 -0.0014 193 THR   A CB  
1540 O  OG1 . THR   A 192 ? 0.0647 0.0783 0.0788 0.0033  -0.0063 -0.0012 193 THR   A OG1 
1541 C  CG2 . THR   A 192 ? 0.0642 0.0888 0.0741 0.0076  0.0020  -0.0024 193 THR   A CG2 
1542 N  N   . TYR   A 193 ? 0.0603 0.0893 0.0478 0.0082  -0.0133 0.0003  194 TYR   A N   
1543 C  CA  . TYR   A 193 ? 0.0677 0.0872 0.0471 0.0058  -0.0161 0.0021  194 TYR   A CA  
1544 C  C   . TYR   A 193 ? 0.0642 0.0745 0.0508 0.0107  -0.0204 -0.0036 194 TYR   A C   
1545 O  O   . TYR   A 193 ? 0.0607 0.0777 0.0525 0.0033  -0.0147 -0.0020 194 TYR   A O   
1546 C  CB  . TYR   A 193 ? 0.0670 0.0878 0.0557 0.0045  -0.0136 0.0071  194 TYR   A CB  
1547 C  CG  . TYR   A 193 ? 0.0643 0.0795 0.0560 0.0029  -0.0123 0.0036  194 TYR   A CG  
1548 C  CD1 . TYR   A 193 ? 0.0581 0.0728 0.0600 0.0037  -0.0128 0.0040  194 TYR   A CD1 
1549 C  CD2 . TYR   A 193 ? 0.0663 0.0783 0.0562 0.0043  -0.0158 -0.0025 194 TYR   A CD2 
1550 C  CE1 . TYR   A 193 ? 0.0551 0.0781 0.0585 0.0059  -0.0204 0.0043  194 TYR   A CE1 
1551 C  CE2 . TYR   A 193 ? 0.0594 0.0776 0.0620 -0.0012 -0.0132 0.0016  194 TYR   A CE2 
1552 C  CZ  . TYR   A 193 ? 0.0608 0.0785 0.0564 0.0051  -0.0111 0.0001  194 TYR   A CZ  
1553 O  OH  . TYR   A 193 ? 0.0611 0.0792 0.0607 0.0015  -0.0065 -0.0030 194 TYR   A OH  
1554 N  N   . PRO   A 194 ? 0.0661 0.0809 0.0532 -0.0011 -0.0149 -0.0097 195 PRO   A N   
1555 C  CA  . PRO   A 194 ? 0.0667 0.0849 0.0606 -0.0006 -0.0159 -0.0045 195 PRO   A CA  
1556 C  C   . PRO   A 194 ? 0.0602 0.0700 0.0595 -0.0038 -0.0148 0.0016  195 PRO   A C   
1557 O  O   . PRO   A 194 ? 0.0631 0.0883 0.0615 0.0092  -0.0087 -0.0033 195 PRO   A O   
1558 C  CB  . PRO   A 194 ? 0.0784 0.1012 0.0727 0.0006  -0.0102 -0.0169 195 PRO   A CB  
1559 C  CG  . PRO   A 194 ? 0.0852 0.1083 0.0672 -0.0029 -0.0070 -0.0223 195 PRO   A CG  
1560 C  CD  . PRO   A 194 ? 0.0809 0.0965 0.0498 -0.0023 -0.0111 -0.0095 195 PRO   A CD  
1561 N  N   . GLY   A 195 ? 0.0539 0.0791 0.0569 0.0096  -0.0093 -0.0061 196 GLY   A N   
1562 C  CA  . GLY   A 195 ? 0.0520 0.0845 0.0603 0.0033  -0.0089 -0.0054 196 GLY   A CA  
1563 C  C   . GLY   A 195 ? 0.0490 0.0755 0.0590 -0.0021 -0.0136 -0.0067 196 GLY   A C   
1564 O  O   . GLY   A 195 ? 0.0624 0.0732 0.0667 -0.0008 -0.0035 -0.0101 196 GLY   A O   
1565 N  N   . SER   A 196 ? 0.0519 0.0748 0.0579 -0.0095 -0.0144 -0.0072 197 SER   A N   
1566 C  CA  . SER   A 196 ? 0.0597 0.0767 0.0611 -0.0036 -0.0026 -0.0102 197 SER   A CA  
1567 C  C   . SER   A 196 ? 0.0522 0.0751 0.0647 0.0044  -0.0082 -0.0045 197 SER   A C   
1568 O  O   . SER   A 196 ? 0.0608 0.0786 0.0648 0.0011  -0.0093 -0.0104 197 SER   A O   
1569 C  CB  . SER   A 196 ? 0.0572 0.0813 0.0685 -0.0072 -0.0001 -0.0052 197 SER   A CB  
1570 O  OG  . SER   A 196 ? 0.0537 0.0795 0.0689 -0.0044 -0.0040 -0.0079 197 SER   A OG  
1571 N  N   . LEU   A 197 ? 0.0702 0.0851 0.0645 -0.0045 -0.0030 -0.0070 198 LEU   A N   
1572 C  CA  . LEU   A 197 ? 0.0797 0.0856 0.0629 -0.0038 0.0010  -0.0051 198 LEU   A CA  
1573 C  C   . LEU   A 197 ? 0.0569 0.0841 0.0618 -0.0042 -0.0028 -0.0075 198 LEU   A C   
1574 O  O   . LEU   A 197 ? 0.0575 0.0855 0.0740 -0.0013 -0.0062 -0.0158 198 LEU   A O   
1575 C  CB  . LEU   A 197 ? 0.0982 0.0956 0.0750 -0.0092 0.0021  0.0015  198 LEU   A CB  
1576 C  CG  . LEU   A 197 ? 0.1422 0.1075 0.0908 -0.0011 0.0029  0.0141  198 LEU   A CG  
1577 C  CD1 . LEU   A 197 ? 0.1504 0.1064 0.1146 -0.0157 -0.0028 0.0215  198 LEU   A CD1 
1578 C  CD2 . LEU   A 197 ? 0.1376 0.1229 0.1070 0.0223  0.0148  0.0090  198 LEU   A CD2 
1579 N  N   . THR   A 198 ? 0.0433 0.0829 0.0655 -0.0007 -0.0055 -0.0063 199 THR   A N   
1580 C  CA  . THR   A 198 ? 0.0505 0.0773 0.0660 -0.0009 -0.0089 -0.0101 199 THR   A CA  
1581 C  C   . THR   A 198 ? 0.0442 0.0774 0.0731 -0.0042 -0.0104 -0.0111 199 THR   A C   
1582 O  O   . THR   A 198 ? 0.0559 0.0870 0.0864 -0.0019 -0.0079 -0.0089 199 THR   A O   
1583 C  CB  . THR   A 198 ? 0.0551 0.0758 0.0607 -0.0029 -0.0075 -0.0052 199 THR   A CB  
1584 O  OG1 . THR   A 198 ? 0.0547 0.0855 0.0605 -0.0098 -0.0118 0.0000  199 THR   A OG1 
1585 C  CG2 . THR   A 198 ? 0.0642 0.0823 0.0727 0.0016  -0.0069 -0.0027 199 THR   A CG2 
1586 N  N   . THR   A 199 ? 0.0591 0.0810 0.0755 0.0056  0.0012  -0.0118 200 THR   A N   
1587 C  CA  . THR   A 199 ? 0.0712 0.0790 0.0861 -0.0008 0.0049  -0.0210 200 THR   A CA  
1588 C  C   . THR   A 199 ? 0.0708 0.0997 0.0817 -0.0088 0.0075  -0.0192 200 THR   A C   
1589 O  O   . THR   A 199 ? 0.0664 0.1014 0.0948 -0.0109 0.0104  -0.0161 200 THR   A O   
1590 C  CB  . THR   A 199 ? 0.1093 0.1016 0.0882 -0.0107 -0.0059 -0.0160 200 THR   A CB  
1591 O  OG1 . THR   A 199 ? 0.2310 0.1232 0.1092 0.0089  -0.0625 -0.0065 200 THR   A OG1 
1592 C  CG2 . THR   A 199 ? 0.1054 0.0924 0.0839 -0.0112 -0.0073 -0.0136 200 THR   A CG2 
1593 N  N   . PRO   A 200 ? 0.0690 0.1066 0.0899 -0.0045 0.0099  -0.0118 201 PRO   A N   
1594 C  CA  . PRO   A 200 ? 0.0684 0.1235 0.0813 -0.0143 -0.0017 -0.0059 201 PRO   A CA  
1595 C  C   . PRO   A 200 ? 0.0797 0.1218 0.0839 -0.0146 0.0028  -0.0055 201 PRO   A C   
1596 O  O   . PRO   A 200 ? 0.1049 0.1197 0.0968 -0.0071 -0.0119 -0.0057 201 PRO   A O   
1597 C  CB  . PRO   A 200 ? 0.0722 0.1353 0.1039 -0.0158 0.0095  -0.0122 201 PRO   A CB  
1598 C  CG  . PRO   A 200 ? 0.0809 0.1346 0.1074 -0.0005 0.0066  -0.0156 201 PRO   A CG  
1599 C  CD  . PRO   A 200 ? 0.0846 0.1152 0.0899 -0.0003 0.0084  -0.0169 201 PRO   A CD  
1600 N  N   . PRO   A 201 ? 0.0980 0.1111 0.0870 -0.0143 0.0063  0.0035  202 PRO   A N   
1601 C  CA  . PRO   A 201 ? 0.0935 0.1167 0.0953 -0.0233 0.0120  -0.0065 202 PRO   A CA  
1602 C  C   . PRO   A 201 ? 0.0612 0.1136 0.0906 -0.0191 0.0042  -0.0094 202 PRO   A C   
1603 O  O   . PRO   A 201 ? 0.0808 0.1064 0.1070 -0.0265 -0.0003 -0.0136 202 PRO   A O   
1604 C  CB  . PRO   A 201 ? 0.1376 0.1179 0.1092 -0.0369 0.0145  -0.0049 202 PRO   A CB  
1605 C  CG  . PRO   A 201 ? 0.1509 0.1073 0.1218 -0.0139 0.0135  0.0087  202 PRO   A CG  
1606 C  CD  . PRO   A 201 ? 0.1161 0.1235 0.1056 -0.0036 0.0038  0.0097  202 PRO   A CD  
1607 N  N   . LEU   A 202 ? 0.0563 0.1003 0.0824 -0.0119 0.0001  -0.0073 203 LEU   A N   
1608 C  CA  . LEU   A 202 ? 0.0617 0.0996 0.0830 -0.0060 -0.0034 -0.0081 203 LEU   A CA  
1609 C  C   . LEU   A 202 ? 0.0641 0.0958 0.0848 -0.0119 0.0038  -0.0047 203 LEU   A C   
1610 O  O   . LEU   A 202 ? 0.0716 0.0976 0.0895 -0.0065 -0.0055 -0.0135 203 LEU   A O   
1611 C  CB  . LEU   A 202 ? 0.0566 0.1083 0.0805 -0.0022 -0.0015 -0.0120 203 LEU   A CB  
1612 C  CG  . LEU   A 202 ? 0.0596 0.1006 0.0870 -0.0024 -0.0031 -0.0129 203 LEU   A CG  
1613 C  CD1 . LEU   A 202 ? 0.0676 0.1148 0.1147 -0.0007 -0.0057 -0.0149 203 LEU   A CD1 
1614 C  CD2 . LEU   A 202 ? 0.0587 0.0963 0.0987 -0.0021 -0.0004 -0.0118 203 LEU   A CD2 
1615 N  N   . LEU   A 203 ? 0.0801 0.0912 0.0910 -0.0057 0.0093  0.0000  204 LEU   A N   
1616 C  CA  . LEU   A 203 ? 0.0968 0.0733 0.1118 -0.0078 0.0099  -0.0099 204 LEU   A CA  
1617 C  C   . LEU   A 203 ? 0.0826 0.0792 0.0919 -0.0079 -0.0060 -0.0043 204 LEU   A C   
1618 O  O   . LEU   A 203 ? 0.0815 0.0806 0.0755 -0.0063 -0.0019 -0.0126 204 LEU   A O   
1619 C  CB  . LEU   A 203 ? 0.1213 0.0917 0.1233 0.0000  0.0231  -0.0023 204 LEU   A CB  
1620 C  CG  . LEU   A 203 ? 0.1499 0.1099 0.1474 0.0132  0.0402  0.0036  204 LEU   A CG  
1621 C  CD1 . LEU   A 203 ? 0.1787 0.1079 0.1492 -0.0015 0.0375  0.0151  204 LEU   A CD1 
1622 C  CD2 . LEU   A 203 ? 0.1551 0.1398 0.1970 -0.0138 0.0441  0.0184  204 LEU   A CD2 
1623 N  N   . GLU   A 204 ? 0.0677 0.0895 0.0920 -0.0154 -0.0062 -0.0139 205 GLU   A N   
1624 C  CA  . GLU   A 204 ? 0.0698 0.0938 0.0787 -0.0115 -0.0168 -0.0162 205 GLU   A CA  
1625 C  C   . GLU   A 204 ? 0.0812 0.0917 0.0717 -0.0128 -0.0171 -0.0113 205 GLU   A C   
1626 O  O   . GLU   A 204 ? 0.0933 0.1211 0.0860 -0.0005 -0.0127 -0.0291 205 GLU   A O   
1627 C  CB  . GLU   A 204 ? 0.0730 0.0998 0.0869 -0.0101 -0.0211 -0.0172 205 GLU   A CB  
1628 C  CG  . GLU   A 204 ? 0.0863 0.1023 0.0975 -0.0094 -0.0289 -0.0160 205 GLU   A CG  
1629 C  CD  . GLU   A 204 ? 0.0866 0.1168 0.0972 -0.0165 -0.0292 -0.0219 205 GLU   A CD  
1630 O  OE1 . GLU   A 204 ? 0.1002 0.1280 0.1228 -0.0052 -0.0429 -0.0368 205 GLU   A OE1 
1631 O  OE2 . GLU   A 204 ? 0.0919 0.1170 0.0990 -0.0061 -0.0303 -0.0091 205 GLU   A OE2 
1632 N  N   A CYS   A 205 ? 0.0706 0.0832 0.0776 -0.0134 -0.0172 -0.0129 206 CYS   A N   
1633 N  N   B CYS   A 205 ? 0.0714 0.0731 0.0658 -0.0119 -0.0118 -0.0166 206 CYS   A N   
1634 C  CA  A CYS   A 205 ? 0.0816 0.0925 0.0760 -0.0050 -0.0201 -0.0101 206 CYS   A CA  
1635 C  CA  B CYS   A 205 ? 0.0800 0.0757 0.0574 -0.0054 -0.0138 -0.0171 206 CYS   A CA  
1636 C  C   A CYS   A 205 ? 0.0708 0.0747 0.0678 -0.0015 -0.0144 -0.0044 206 CYS   A C   
1637 C  C   B CYS   A 205 ? 0.0715 0.0702 0.0622 -0.0033 -0.0136 -0.0128 206 CYS   A C   
1638 O  O   A CYS   A 205 ? 0.0754 0.0720 0.0720 -0.0020 -0.0181 0.0023  206 CYS   A O   
1639 O  O   B CYS   A 205 ? 0.0763 0.0701 0.0639 -0.0001 -0.0090 -0.0128 206 CYS   A O   
1640 C  CB  A CYS   A 205 ? 0.0713 0.1150 0.1042 -0.0154 -0.0051 0.0024  206 CYS   A CB  
1641 C  CB  B CYS   A 205 ? 0.0718 0.0821 0.0652 -0.0076 0.0041  -0.0119 206 CYS   A CB  
1642 S  SG  A CYS   A 205 ? 0.2075 0.2253 0.2138 -0.0304 -0.0313 -0.0218 206 CYS   A SG  
1643 S  SG  B CYS   A 205 ? 0.1007 0.0764 0.1026 -0.0492 -0.0343 -0.0431 206 CYS   A SG  
1644 N  N   . VAL   A 206 ? 0.0646 0.0723 0.0728 -0.0017 -0.0140 -0.0028 207 VAL   A N   
1645 C  CA  . VAL   A 206 ? 0.0622 0.0660 0.0713 -0.0020 -0.0175 -0.0027 207 VAL   A CA  
1646 C  C   . VAL   A 206 ? 0.0708 0.0701 0.0581 0.0045  -0.0163 -0.0018 207 VAL   A C   
1647 O  O   . VAL   A 206 ? 0.0783 0.1041 0.0718 0.0104  -0.0152 0.0126  207 VAL   A O   
1648 C  CB  . VAL   A 206 ? 0.0588 0.0763 0.0729 0.0052  -0.0090 -0.0031 207 VAL   A CB  
1649 C  CG1 . VAL   A 206 ? 0.0666 0.0768 0.0743 0.0027  -0.0173 -0.0115 207 VAL   A CG1 
1650 C  CG2 . VAL   A 206 ? 0.0751 0.0804 0.0746 0.0088  -0.0030 -0.0067 207 VAL   A CG2 
1651 N  N   . THR   A 207 ? 0.0634 0.0636 0.0628 -0.0009 -0.0153 0.0000  208 THR   A N   
1652 C  CA  . THR   A 207 ? 0.0690 0.0690 0.0573 -0.0004 -0.0173 0.0034  208 THR   A CA  
1653 C  C   . THR   A 207 ? 0.0648 0.0621 0.0456 -0.0006 -0.0113 0.0032  208 THR   A C   
1654 O  O   . THR   A 207 ? 0.0664 0.0673 0.0566 -0.0035 -0.0234 0.0004  208 THR   A O   
1655 C  CB  . THR   A 207 ? 0.0682 0.0745 0.0701 -0.0032 -0.0156 -0.0012 208 THR   A CB  
1656 O  OG1 . THR   A 207 ? 0.0963 0.0745 0.0792 -0.0008 -0.0068 -0.0148 208 THR   A OG1 
1657 C  CG2 . THR   A 207 ? 0.0802 0.0912 0.0779 -0.0055 -0.0058 0.0000  208 THR   A CG2 
1658 N  N   . TRP   A 208 ? 0.0672 0.0611 0.0450 0.0029  -0.0140 0.0040  209 TRP   A N   
1659 C  CA  . TRP   A 208 ? 0.0706 0.0543 0.0456 0.0039  -0.0140 0.0029  209 TRP   A CA  
1660 C  C   . TRP   A 208 ? 0.0694 0.0587 0.0461 0.0045  -0.0097 0.0000  209 TRP   A C   
1661 O  O   . TRP   A 208 ? 0.0742 0.0766 0.0470 -0.0080 -0.0084 0.0041  209 TRP   A O   
1662 C  CB  . TRP   A 208 ? 0.0786 0.0539 0.0506 0.0038  -0.0166 0.0031  209 TRP   A CB  
1663 C  CG  . TRP   A 208 ? 0.0613 0.0538 0.0623 0.0085  -0.0235 0.0013  209 TRP   A CG  
1664 C  CD1 . TRP   A 208 ? 0.0617 0.0697 0.0721 0.0046  -0.0181 -0.0015 209 TRP   A CD1 
1665 C  CD2 . TRP   A 208 ? 0.0644 0.0546 0.0638 0.0092  -0.0150 -0.0046 209 TRP   A CD2 
1666 N  NE1 . TRP   A 208 ? 0.0579 0.0817 0.0807 0.0049  -0.0162 -0.0079 209 TRP   A NE1 
1667 C  CE2 . TRP   A 208 ? 0.0610 0.0715 0.0724 0.0134  -0.0153 -0.0082 209 TRP   A CE2 
1668 C  CE3 . TRP   A 208 ? 0.0635 0.0630 0.0575 0.0060  -0.0166 -0.0103 209 TRP   A CE3 
1669 C  CZ2 . TRP   A 208 ? 0.0664 0.0773 0.0846 0.0199  -0.0028 -0.0090 209 TRP   A CZ2 
1670 C  CZ3 . TRP   A 208 ? 0.0774 0.0765 0.0624 0.0088  -0.0174 -0.0108 209 TRP   A CZ3 
1671 C  CH2 . TRP   A 208 ? 0.0893 0.0768 0.0652 0.0136  -0.0097 -0.0182 209 TRP   A CH2 
1672 N  N   . ILE   A 209 ? 0.0610 0.0650 0.0440 0.0000  -0.0055 0.0050  210 ILE   A N   
1673 C  CA  . ILE   A 209 ? 0.0617 0.0692 0.0492 0.0031  -0.0063 0.0060  210 ILE   A CA  
1674 C  C   . ILE   A 209 ? 0.0557 0.0627 0.0497 0.0000  -0.0076 0.0055  210 ILE   A C   
1675 O  O   . ILE   A 209 ? 0.0836 0.0655 0.0513 -0.0019 -0.0103 0.0016  210 ILE   A O   
1676 C  CB  . ILE   A 209 ? 0.0646 0.0707 0.0732 0.0048  -0.0031 0.0104  210 ILE   A CB  
1677 C  CG1 . ILE   A 209 ? 0.0740 0.0740 0.0995 0.0110  0.0000  0.0013  210 ILE   A CG1 
1678 C  CG2 . ILE   A 209 ? 0.0655 0.0884 0.0847 0.0132  -0.0002 0.0080  210 ILE   A CG2 
1679 C  CD1 . ILE   A 209 ? 0.0908 0.0811 0.1271 0.0190  -0.0050 0.0017  210 ILE   A CD1 
1680 N  N   . VAL   A 210 ? 0.0534 0.0615 0.0460 -0.0028 -0.0051 0.0051  211 VAL   A N   
1681 C  CA  . VAL   A 210 ? 0.0589 0.0602 0.0493 -0.0021 -0.0034 0.0093  211 VAL   A CA  
1682 C  C   . VAL   A 210 ? 0.0506 0.0675 0.0534 -0.0027 -0.0054 0.0095  211 VAL   A C   
1683 O  O   . VAL   A 210 ? 0.0623 0.0756 0.0545 -0.0081 -0.0002 0.0089  211 VAL   A O   
1684 C  CB  . VAL   A 210 ? 0.0622 0.0699 0.0605 -0.0015 -0.0100 0.0107  211 VAL   A CB  
1685 C  CG1 . VAL   A 210 ? 0.0672 0.0711 0.0791 -0.0007 -0.0043 0.0051  211 VAL   A CG1 
1686 C  CG2 . VAL   A 210 ? 0.0641 0.0764 0.0873 0.0020  -0.0068 0.0071  211 VAL   A CG2 
1687 N  N   . LEU   A 211 ? 0.0568 0.0833 0.0543 -0.0068 -0.0062 0.0053  212 LEU   A N   
1688 C  CA  . LEU   A 211 ? 0.0563 0.0868 0.0667 -0.0125 -0.0113 0.0019  212 LEU   A CA  
1689 C  C   . LEU   A 211 ? 0.0628 0.0944 0.0703 -0.0054 -0.0079 0.0011  212 LEU   A C   
1690 O  O   . LEU   A 211 ? 0.0732 0.0953 0.0803 -0.0072 -0.0098 0.0061  212 LEU   A O   
1691 C  CB  . LEU   A 211 ? 0.0552 0.0968 0.0751 -0.0115 -0.0122 0.0042  212 LEU   A CB  
1692 C  CG  . LEU   A 211 ? 0.0737 0.1033 0.0964 -0.0102 -0.0232 0.0112  212 LEU   A CG  
1693 C  CD1 . LEU   A 211 ? 0.0713 0.1301 0.1075 -0.0066 -0.0248 0.0105  212 LEU   A CD1 
1694 C  CD2 . LEU   A 211 ? 0.0971 0.1057 0.0896 -0.0032 -0.0191 0.0189  212 LEU   A CD2 
1695 N  N   . LYS   A 212 ? 0.0638 0.0965 0.0803 -0.0097 -0.0030 0.0060  213 LYS   A N   
1696 C  CA  . LYS   A 212 ? 0.0863 0.1011 0.0863 -0.0131 -0.0133 0.0165  213 LYS   A CA  
1697 C  C   . LYS   A 212 ? 0.0846 0.0840 0.0954 -0.0227 -0.0086 0.0153  213 LYS   A C   
1698 O  O   . LYS   A 212 ? 0.1063 0.0907 0.1267 -0.0097 -0.0291 0.0166  213 LYS   A O   
1699 C  CB  . LYS   A 212 ? 0.1079 0.1264 0.0952 -0.0226 -0.0022 0.0172  213 LYS   A CB  
1700 C  CG  . LYS   A 212 ? 0.1409 0.1401 0.1280 -0.0193 0.0031  0.0370  213 LYS   A CG  
1701 C  CD  . LYS   A 212 ? 0.1937 0.1859 0.1442 -0.0109 0.0145  0.0562  213 LYS   A CD  
1702 C  CE  . LYS   A 212 ? 0.2465 0.2214 0.1981 -0.0182 0.0222  0.0865  213 LYS   A CE  
1703 N  NZ  . LYS   A 212 ? 0.3026 0.3010 0.2496 -0.0288 0.0397  0.0803  213 LYS   A NZ  
1704 N  N   . GLU   A 213 ? 0.0751 0.0897 0.0882 -0.0100 -0.0154 0.0077  214 GLU   A N   
1705 C  CA  . GLU   A 213 ? 0.0693 0.0902 0.1013 -0.0210 -0.0093 0.0070  214 GLU   A CA  
1706 C  C   . GLU   A 213 ? 0.0739 0.0771 0.1042 -0.0184 -0.0116 0.0046  214 GLU   A C   
1707 O  O   . GLU   A 213 ? 0.0734 0.0881 0.0976 -0.0098 -0.0151 0.0109  214 GLU   A O   
1708 C  CB  . GLU   A 213 ? 0.0688 0.1114 0.1067 -0.0177 -0.0057 0.0039  214 GLU   A CB  
1709 C  CG  . GLU   A 213 ? 0.0994 0.1397 0.1404 -0.0317 -0.0213 0.0037  214 GLU   A CG  
1710 C  CD  . GLU   A 213 ? 0.1104 0.1828 0.1905 -0.0338 -0.0288 -0.0139 214 GLU   A CD  
1711 O  OE1 . GLU   A 213 ? 0.0982 0.1544 0.2167 -0.0149 -0.0308 0.0057  214 GLU   A OE1 
1712 O  OE2 . GLU   A 213 ? 0.1741 0.2277 0.3416 -0.0383 -0.0568 -0.0419 214 GLU   A OE2 
1713 N  N   . PRO   A 214 ? 0.0843 0.0831 0.0966 -0.0151 -0.0103 0.0050  215 PRO   A N   
1714 C  CA  . PRO   A 214 ? 0.0891 0.0860 0.0933 -0.0184 -0.0070 0.0008  215 PRO   A CA  
1715 C  C   . PRO   A 214 ? 0.0884 0.1042 0.0971 -0.0220 -0.0139 -0.0041 215 PRO   A C   
1716 O  O   . PRO   A 214 ? 0.0875 0.1472 0.1187 -0.0341 -0.0188 0.0012  215 PRO   A O   
1717 C  CB  . PRO   A 214 ? 0.1007 0.0903 0.1134 -0.0090 -0.0147 -0.0009 215 PRO   A CB  
1718 C  CG  . PRO   A 214 ? 0.1271 0.1183 0.1474 -0.0095 -0.0115 0.0012  215 PRO   A CG  
1719 C  CD  . PRO   A 214 ? 0.1061 0.0861 0.1277 -0.0052 -0.0105 0.0071  215 PRO   A CD  
1720 N  N   . ILE   A 215 ? 0.0762 0.0988 0.0916 -0.0160 -0.0187 -0.0150 216 ILE   A N   
1721 C  CA  . ILE   A 215 ? 0.0868 0.1012 0.0971 -0.0149 -0.0230 -0.0156 216 ILE   A CA  
1722 C  C   . ILE   A 215 ? 0.0956 0.0956 0.1114 -0.0139 -0.0244 -0.0165 216 ILE   A C   
1723 O  O   . ILE   A 215 ? 0.0986 0.0964 0.1443 -0.0180 -0.0157 -0.0271 216 ILE   A O   
1724 C  CB  . ILE   A 215 ? 0.0941 0.1049 0.0984 -0.0035 -0.0190 -0.0108 216 ILE   A CB  
1725 C  CG1 . ILE   A 215 ? 0.1051 0.1027 0.1000 0.0010  -0.0193 -0.0048 216 ILE   A CG1 
1726 C  CG2 . ILE   A 215 ? 0.0934 0.1149 0.1164 -0.0048 -0.0173 -0.0127 216 ILE   A CG2 
1727 C  CD1 . ILE   A 215 ? 0.1192 0.1279 0.1216 0.0019  -0.0165 0.0102  216 ILE   A CD1 
1728 N  N   . SER   A 216 ? 0.0999 0.1155 0.1239 -0.0127 -0.0315 -0.0259 217 SER   A N   
1729 C  CA  . SER   A 216 ? 0.1269 0.1075 0.1269 -0.0186 -0.0290 -0.0203 217 SER   A CA  
1730 C  C   . SER   A 216 ? 0.1272 0.1022 0.1204 -0.0101 -0.0377 -0.0125 217 SER   A C   
1731 O  O   . SER   A 216 ? 0.1408 0.1283 0.1361 0.0067  -0.0401 -0.0154 217 SER   A O   
1732 C  CB  . SER   A 216 ? 0.1805 0.1160 0.1636 -0.0276 -0.0184 -0.0194 217 SER   A CB  
1733 O  OG  . SER   A 216 ? 0.2194 0.1663 0.1952 -0.0369 -0.0191 0.0047  217 SER   A OG  
1734 N  N   . VAL   A 217 ? 0.1259 0.0854 0.1200 -0.0119 -0.0404 -0.0122 218 VAL   A N   
1735 C  CA  . VAL   A 217 ? 0.1510 0.0818 0.1177 -0.0221 -0.0368 -0.0139 218 VAL   A CA  
1736 C  C   . VAL   A 217 ? 0.1402 0.0821 0.1147 -0.0262 -0.0312 -0.0138 218 VAL   A C   
1737 O  O   . VAL   A 217 ? 0.1663 0.0743 0.1286 -0.0236 -0.0278 -0.0111 218 VAL   A O   
1738 C  CB  . VAL   A 217 ? 0.1468 0.0810 0.1344 -0.0168 -0.0379 -0.0118 218 VAL   A CB  
1739 C  CG1 . VAL   A 217 ? 0.1648 0.0859 0.1420 -0.0191 -0.0488 -0.0227 218 VAL   A CG1 
1740 C  CG2 . VAL   A 217 ? 0.1478 0.0841 0.1564 -0.0220 -0.0423 -0.0183 218 VAL   A CG2 
1741 N  N   . SER   A 218 ? 0.1463 0.0886 0.1147 -0.0243 -0.0296 -0.0160 219 SER   A N   
1742 C  CA  . SER   A 218 ? 0.1477 0.0841 0.1280 -0.0409 -0.0176 -0.0228 219 SER   A CA  
1743 C  C   . SER   A 218 ? 0.1613 0.0737 0.1247 -0.0322 -0.0149 -0.0176 219 SER   A C   
1744 O  O   . SER   A 218 ? 0.1533 0.0806 0.1317 -0.0291 -0.0201 -0.0113 219 SER   A O   
1745 C  CB  . SER   A 218 ? 0.1525 0.0889 0.1308 -0.0381 -0.0205 -0.0236 219 SER   A CB  
1746 O  OG  . SER   A 218 ? 0.1654 0.1080 0.1321 -0.0430 -0.0353 -0.0132 219 SER   A OG  
1747 N  N   A SER   A 219 ? 0.1616 0.0750 0.1539 -0.0344 -0.0130 -0.0133 220 SER   A N   
1748 N  N   B SER   A 219 ? 0.1737 0.0755 0.1592 -0.0328 -0.0147 -0.0131 220 SER   A N   
1749 C  CA  A SER   A 219 ? 0.1598 0.0876 0.1578 -0.0283 -0.0164 -0.0149 220 SER   A CA  
1750 C  CA  B SER   A 219 ? 0.1780 0.0907 0.1693 -0.0259 -0.0197 -0.0150 220 SER   A CA  
1751 C  C   A SER   A 219 ? 0.1556 0.0852 0.1638 -0.0257 -0.0222 -0.0156 220 SER   A C   
1752 C  C   B SER   A 219 ? 0.1643 0.0865 0.1707 -0.0243 -0.0260 -0.0158 220 SER   A C   
1753 O  O   A SER   A 219 ? 0.1557 0.1000 0.1826 -0.0225 -0.0116 -0.0075 220 SER   A O   
1754 O  O   B SER   A 219 ? 0.1648 0.1050 0.1887 -0.0214 -0.0149 -0.0047 220 SER   A O   
1755 C  CB  A SER   A 219 ? 0.1720 0.0974 0.1767 -0.0150 0.0013  -0.0123 220 SER   A CB  
1756 C  CB  B SER   A 219 ? 0.2125 0.1012 0.2064 -0.0098 -0.0039 -0.0162 220 SER   A CB  
1757 O  OG  A SER   A 219 ? 0.1654 0.1066 0.1791 -0.0131 0.0077  -0.0006 220 SER   A OG  
1758 O  OG  B SER   A 219 ? 0.2352 0.1212 0.2250 -0.0033 -0.0081 -0.0167 220 SER   A OG  
1759 N  N   . GLU   A 220 ? 0.1528 0.0889 0.1549 -0.0233 -0.0183 -0.0184 221 GLU   A N   
1760 C  CA  . GLU   A 220 ? 0.1662 0.1218 0.1432 -0.0192 -0.0186 -0.0328 221 GLU   A CA  
1761 C  C   . GLU   A 220 ? 0.1616 0.1268 0.1378 -0.0172 -0.0179 -0.0111 221 GLU   A C   
1762 O  O   . GLU   A 220 ? 0.1843 0.1351 0.1429 -0.0105 0.0022  -0.0173 221 GLU   A O   
1763 C  CB  . GLU   A 220 ? 0.1935 0.1522 0.1462 -0.0329 -0.0182 -0.0453 221 GLU   A CB  
1764 C  CG  . GLU   A 220 ? 0.2345 0.1716 0.1842 -0.0365 -0.0255 -0.0700 221 GLU   A CG  
1765 C  CD  . GLU   A 220 ? 0.2584 0.1778 0.2254 -0.0660 -0.0194 -0.0808 221 GLU   A CD  
1766 O  OE1 . GLU   A 220 ? 0.2802 0.1810 0.2569 -0.0836 0.0100  -0.0845 221 GLU   A OE1 
1767 O  OE2 . GLU   A 220 ? 0.3822 0.1966 0.3136 -0.0972 0.0284  -0.0967 221 GLU   A OE2 
1768 N  N   . GLN   A 221 ? 0.1296 0.1031 0.1245 -0.0229 -0.0244 -0.0086 222 GLN   A N   
1769 C  CA  . GLN   A 221 ? 0.1331 0.0966 0.1075 -0.0170 -0.0315 -0.0017 222 GLN   A CA  
1770 C  C   . GLN   A 221 ? 0.1334 0.0995 0.1119 -0.0214 -0.0294 0.0055  222 GLN   A C   
1771 O  O   . GLN   A 221 ? 0.1322 0.1200 0.1218 -0.0248 -0.0220 0.0027  222 GLN   A O   
1772 C  CB  . GLN   A 221 ? 0.1336 0.1006 0.1029 -0.0233 -0.0314 -0.0021 222 GLN   A CB  
1773 C  CG  . GLN   A 221 ? 0.1414 0.0890 0.1131 -0.0257 -0.0357 0.0012  222 GLN   A CG  
1774 C  CD  . GLN   A 221 ? 0.1382 0.0925 0.1189 -0.0254 -0.0338 -0.0107 222 GLN   A CD  
1775 O  OE1 . GLN   A 221 ? 0.1377 0.1050 0.1180 -0.0144 -0.0208 -0.0098 222 GLN   A OE1 
1776 N  NE2 . GLN   A 221 ? 0.1437 0.1201 0.1259 -0.0088 -0.0313 -0.0116 222 GLN   A NE2 
1777 N  N   . VAL   A 222 ? 0.1369 0.1016 0.1129 -0.0307 -0.0278 0.0159  223 VAL   A N   
1778 C  CA  . VAL   A 222 ? 0.1349 0.0952 0.1264 -0.0229 -0.0308 0.0157  223 VAL   A CA  
1779 C  C   . VAL   A 222 ? 0.1427 0.1083 0.1341 -0.0338 -0.0195 0.0168  223 VAL   A C   
1780 O  O   . VAL   A 222 ? 0.1444 0.1154 0.1247 -0.0277 -0.0172 0.0184  223 VAL   A O   
1781 C  CB  . VAL   A 222 ? 0.1446 0.1339 0.1315 -0.0195 -0.0306 0.0199  223 VAL   A CB  
1782 C  CG1 . VAL   A 222 ? 0.1441 0.1507 0.1517 -0.0232 -0.0315 0.0173  223 VAL   A CG1 
1783 C  CG2 . VAL   A 222 ? 0.1612 0.1442 0.1314 -0.0129 -0.0297 0.0147  223 VAL   A CG2 
1784 N  N   . LEU   A 223 ? 0.1510 0.0988 0.1492 -0.0297 -0.0059 0.0065  224 LEU   A N   
1785 C  CA  . LEU   A 223 ? 0.1679 0.1282 0.1711 -0.0214 -0.0020 0.0006  224 LEU   A CA  
1786 C  C   . LEU   A 223 ? 0.1437 0.1258 0.1448 -0.0184 -0.0072 -0.0207 224 LEU   A C   
1787 O  O   . LEU   A 223 ? 0.1505 0.1409 0.1460 -0.0217 0.0102  -0.0231 224 LEU   A O   
1788 C  CB  . LEU   A 223 ? 0.2040 0.1324 0.1835 -0.0146 0.0087  -0.0160 224 LEU   A CB  
1789 C  CG  . LEU   A 223 ? 0.2384 0.1505 0.2059 -0.0212 -0.0008 -0.0147 224 LEU   A CG  
1790 C  CD1 . LEU   A 223 ? 0.2354 0.1696 0.2463 -0.0256 -0.0160 -0.0128 224 LEU   A CD1 
1791 C  CD2 . LEU   A 223 ? 0.2539 0.1648 0.2288 -0.0113 -0.0191 -0.0288 224 LEU   A CD2 
1792 N  N   . LYS   A 224 ? 0.1444 0.1229 0.1233 -0.0256 -0.0128 -0.0116 225 LYS   A N   
1793 C  CA  . LYS   A 224 ? 0.1502 0.1449 0.1174 -0.0293 -0.0184 -0.0033 225 LYS   A CA  
1794 C  C   . LYS   A 224 ? 0.1521 0.1159 0.0909 -0.0241 -0.0149 -0.0003 225 LYS   A C   
1795 O  O   . LYS   A 224 ? 0.1744 0.1381 0.0829 -0.0302 -0.0175 0.0057  225 LYS   A O   
1796 C  CB  . LYS   A 224 ? 0.1627 0.1967 0.1283 -0.0321 -0.0475 0.0061  225 LYS   A CB  
1797 C  CG  . LYS   A 224 ? 0.2088 0.2525 0.1884 -0.0332 -0.0562 0.0239  225 LYS   A CG  
1798 C  CD  . LYS   A 224 ? 0.2943 0.3109 0.2338 -0.0322 -0.0458 0.0041  225 LYS   A CD  
1799 C  CE  . LYS   A 224 ? 0.3291 0.3641 0.2913 -0.0412 -0.0694 -0.0240 225 LYS   A CE  
1800 N  NZ  . LYS   A 224 ? 0.3612 0.4319 0.3022 -0.0310 -0.0907 -0.0294 225 LYS   A NZ  
1801 N  N   . PHE   A 225 ? 0.1317 0.0970 0.0954 -0.0144 -0.0002 -0.0005 226 PHE   A N   
1802 C  CA  . PHE   A 225 ? 0.1350 0.0986 0.0889 -0.0130 -0.0063 -0.0050 226 PHE   A CA  
1803 C  C   . PHE   A 225 ? 0.1398 0.0984 0.0750 -0.0196 0.0030  -0.0107 226 PHE   A C   
1804 O  O   . PHE   A 225 ? 0.1489 0.1067 0.0640 -0.0159 0.0019  -0.0116 226 PHE   A O   
1805 C  CB  . PHE   A 225 ? 0.1340 0.0829 0.0934 -0.0088 -0.0032 -0.0134 226 PHE   A CB  
1806 C  CG  . PHE   A 225 ? 0.1155 0.0870 0.1277 -0.0269 -0.0127 -0.0324 226 PHE   A CG  
1807 C  CD1 . PHE   A 225 ? 0.1366 0.1348 0.1320 -0.0058 -0.0118 -0.0230 226 PHE   A CD1 
1808 C  CD2 . PHE   A 225 ? 0.1400 0.1679 0.1675 -0.0027 -0.0246 -0.0663 226 PHE   A CD2 
1809 C  CE1 . PHE   A 225 ? 0.1292 0.1513 0.1594 -0.0104 -0.0189 -0.0235 226 PHE   A CE1 
1810 C  CE2 . PHE   A 225 ? 0.1358 0.1903 0.1837 -0.0016 -0.0216 -0.0784 226 PHE   A CE2 
1811 C  CZ  . PHE   A 225 ? 0.1218 0.1484 0.1904 -0.0174 -0.0215 -0.0657 226 PHE   A CZ  
1812 N  N   . ARG   A 226 ? 0.1273 0.1015 0.0827 -0.0072 -0.0006 -0.0100 227 ARG   A N   
1813 C  CA  . ARG   A 226 ? 0.1371 0.0986 0.0805 -0.0084 -0.0007 -0.0123 227 ARG   A CA  
1814 C  C   . ARG   A 226 ? 0.1443 0.1127 0.0843 -0.0119 0.0076  -0.0139 227 ARG   A C   
1815 O  O   . ARG   A 226 ? 0.1486 0.1423 0.1018 0.0033  0.0156  -0.0047 227 ARG   A O   
1816 C  CB  . ARG   A 226 ? 0.1503 0.1023 0.0754 -0.0039 -0.0060 -0.0093 227 ARG   A CB  
1817 C  CG  . ARG   A 226 ? 0.1474 0.0923 0.0815 -0.0069 -0.0067 -0.0063 227 ARG   A CG  
1818 C  CD  . ARG   A 226 ? 0.1682 0.0949 0.0981 -0.0077 -0.0074 -0.0039 227 ARG   A CD  
1819 N  NE  . ARG   A 226 ? 0.1608 0.0867 0.0890 -0.0199 -0.0156 -0.0147 227 ARG   A NE  
1820 C  CZ  . ARG   A 226 ? 0.1626 0.0971 0.1066 -0.0341 -0.0068 -0.0161 227 ARG   A CZ  
1821 N  NH1 . ARG   A 226 ? 0.1828 0.1128 0.1439 -0.0448 -0.0128 -0.0329 227 ARG   A NH1 
1822 N  NH2 . ARG   A 226 ? 0.1800 0.0896 0.1170 -0.0501 0.0060  -0.0078 227 ARG   A NH2 
1823 N  N   . LYS   A 227 ? 0.1357 0.1150 0.0693 -0.0095 0.0054  -0.0203 228 LYS   A N   
1824 C  CA  . LYS   A 227 ? 0.1652 0.1176 0.0775 -0.0186 0.0129  -0.0342 228 LYS   A CA  
1825 C  C   . LYS   A 227 ? 0.1633 0.1148 0.0642 -0.0172 0.0068  -0.0241 228 LYS   A C   
1826 O  O   . LYS   A 227 ? 0.1928 0.1266 0.0716 -0.0074 0.0222  -0.0225 228 LYS   A O   
1827 C  CB  . LYS   A 227 ? 0.2030 0.1670 0.0880 -0.0381 0.0090  -0.0367 228 LYS   A CB  
1828 C  CG  . LYS   A 227 ? 0.2570 0.1865 0.1363 -0.0484 0.0178  -0.0454 228 LYS   A CG  
1829 C  CD  . LYS   A 227 ? 0.2815 0.2422 0.1938 -0.0615 0.0042  -0.0718 228 LYS   A CD  
1830 C  CE  . LYS   A 227 ? 0.3277 0.2592 0.2504 -0.0620 -0.0036 -0.0604 228 LYS   A CE  
1831 N  NZ  . LYS   A 227 ? 0.3471 0.3062 0.2853 -0.0601 -0.0145 -0.0525 228 LYS   A NZ  
1832 N  N   . LEU   A 228 ? 0.1422 0.1000 0.0693 -0.0158 0.0157  -0.0197 229 LEU   A N   
1833 C  CA  . LEU   A 228 ? 0.1519 0.1028 0.0764 -0.0128 0.0102  -0.0135 229 LEU   A CA  
1834 C  C   . LEU   A 228 ? 0.1561 0.0880 0.0621 -0.0081 0.0214  -0.0094 229 LEU   A C   
1835 O  O   . LEU   A 228 ? 0.1521 0.0982 0.0866 0.0022  0.0122  -0.0073 229 LEU   A O   
1836 C  CB  . LEU   A 228 ? 0.1500 0.1059 0.0629 -0.0148 0.0052  -0.0078 229 LEU   A CB  
1837 C  CG  . LEU   A 228 ? 0.1457 0.1199 0.0714 -0.0133 -0.0067 -0.0102 229 LEU   A CG  
1838 C  CD1 . LEU   A 228 ? 0.1498 0.1243 0.0756 -0.0213 -0.0031 -0.0229 229 LEU   A CD1 
1839 C  CD2 . LEU   A 228 ? 0.1389 0.1296 0.1032 -0.0024 0.0037  0.0091  229 LEU   A CD2 
1840 N  N   . ASN   A 229 ? 0.1438 0.0914 0.0795 -0.0113 0.0073  -0.0047 230 ASN   A N   
1841 C  CA  . ASN   A 229 ? 0.1431 0.1104 0.0856 -0.0052 0.0158  -0.0030 230 ASN   A CA  
1842 C  C   . ASN   A 229 ? 0.1378 0.1217 0.0762 -0.0131 0.0124  0.0025  230 ASN   A C   
1843 O  O   . ASN   A 229 ? 0.1433 0.1211 0.0958 -0.0114 0.0141  -0.0030 230 ASN   A O   
1844 C  CB  . ASN   A 229 ? 0.1581 0.1328 0.0895 -0.0071 0.0266  -0.0077 230 ASN   A CB  
1845 C  CG  . ASN   A 229 ? 0.1936 0.1437 0.0920 -0.0056 0.0231  -0.0116 230 ASN   A CG  
1846 O  OD1 . ASN   A 229 ? 0.2509 0.1716 0.1002 0.0062  0.0447  -0.0141 230 ASN   A OD1 
1847 N  ND2 . ASN   A 229 ? 0.1944 0.1402 0.1120 -0.0198 0.0145  -0.0329 230 ASN   A ND2 
1848 N  N   . PHE   A 230 ? 0.1281 0.1209 0.0982 -0.0149 0.0184  0.0037  231 PHE   A N   
1849 C  CA  . PHE   A 230 ? 0.1378 0.1285 0.0900 -0.0235 0.0139  0.0021  231 PHE   A CA  
1850 C  C   . PHE   A 230 ? 0.1547 0.1446 0.1011 -0.0248 0.0202  0.0087  231 PHE   A C   
1851 O  O   . PHE   A 230 ? 0.1634 0.1570 0.1044 -0.0419 0.0202  0.0136  231 PHE   A O   
1852 C  CB  . PHE   A 230 ? 0.1367 0.1397 0.0950 -0.0247 0.0209  -0.0032 231 PHE   A CB  
1853 C  CG  . PHE   A 230 ? 0.1274 0.1336 0.0895 -0.0237 0.0180  -0.0046 231 PHE   A CG  
1854 C  CD1 . PHE   A 230 ? 0.1400 0.1408 0.0861 -0.0225 0.0156  -0.0036 231 PHE   A CD1 
1855 C  CD2 . PHE   A 230 ? 0.1473 0.1467 0.0953 -0.0112 0.0108  -0.0043 231 PHE   A CD2 
1856 C  CE1 . PHE   A 230 ? 0.1408 0.1443 0.0788 -0.0205 0.0051  -0.0035 231 PHE   A CE1 
1857 C  CE2 . PHE   A 230 ? 0.1547 0.1376 0.1021 -0.0198 0.0077  -0.0006 231 PHE   A CE2 
1858 C  CZ  . PHE   A 230 ? 0.1432 0.1420 0.0789 -0.0291 0.0013  0.0012  231 PHE   A CZ  
1859 N  N   . ASN   A 231 ? 0.1604 0.1564 0.1041 -0.0278 0.0310  0.0181  232 ASN   A N   
1860 C  CA  . ASN   A 231 ? 0.1417 0.1832 0.1246 -0.0169 0.0357  0.0171  232 ASN   A CA  
1861 C  C   . ASN   A 231 ? 0.1594 0.1810 0.0985 -0.0095 0.0428  0.0216  232 ASN   A C   
1862 O  O   . ASN   A 231 ? 0.1606 0.1781 0.1185 -0.0228 0.0385  0.0028  232 ASN   A O   
1863 C  CB  . ASN   A 231 ? 0.1635 0.1859 0.1416 -0.0057 0.0537  0.0150  232 ASN   A CB  
1864 C  CG  . ASN   A 231 ? 0.1643 0.1652 0.1420 0.0101  0.0376  0.0120  232 ASN   A CG  
1865 O  OD1 . ASN   A 231 ? 0.1970 0.1656 0.1387 -0.0043 0.0497  0.0042  232 ASN   A OD1 
1866 N  ND2 . ASN   A 231 ? 0.2190 0.1737 0.1447 0.0013  0.0361  0.0112  232 ASN   A ND2 
1867 N  N   . GLY   A 232 ? 0.1698 0.1780 0.1393 -0.0141 0.0432  0.0324  233 GLY   A N   
1868 C  CA  . GLY   A 232 ? 0.1919 0.1803 0.1210 -0.0116 0.0426  0.0389  233 GLY   A CA  
1869 C  C   . GLY   A 232 ? 0.1891 0.1687 0.1299 0.0085  0.0302  0.0309  233 GLY   A C   
1870 O  O   . GLY   A 232 ? 0.1929 0.2008 0.1313 0.0308  0.0612  0.0399  233 GLY   A O   
1871 N  N   . GLU   A 233 ? 0.1849 0.1684 0.1195 0.0070  0.0367  0.0294  234 GLU   A N   
1872 C  CA  . GLU   A 233 ? 0.1831 0.1869 0.1311 0.0053  0.0286  0.0241  234 GLU   A CA  
1873 C  C   . GLU   A 233 ? 0.2040 0.2064 0.1300 0.0264  0.0292  0.0173  234 GLU   A C   
1874 O  O   . GLU   A 233 ? 0.2001 0.2395 0.1517 0.0100  0.0515  0.0133  234 GLU   A O   
1875 C  CB  . GLU   A 233 ? 0.1829 0.1823 0.1369 0.0027  0.0296  0.0347  234 GLU   A CB  
1876 C  CG  . GLU   A 233 ? 0.2088 0.2187 0.1377 -0.0140 0.0525  0.0341  234 GLU   A CG  
1877 C  CD  . GLU   A 233 ? 0.2535 0.2716 0.1702 0.0207  0.0290  0.0212  234 GLU   A CD  
1878 O  OE1 . GLU   A 233 ? 0.2676 0.2633 0.2030 0.0201  0.0555  0.0510  234 GLU   A OE1 
1879 O  OE2 . GLU   A 233 ? 0.3554 0.3342 0.1787 -0.0006 -0.0069 0.0290  234 GLU   A OE2 
1880 N  N   . GLY   A 234 ? 0.2389 0.2213 0.1546 0.0401  0.0692  0.0106  235 GLY   A N   
1881 C  CA  . GLY   A 234 ? 0.2652 0.2704 0.1503 0.0527  0.0767  0.0193  235 GLY   A CA  
1882 C  C   . GLY   A 234 ? 0.2353 0.2860 0.1841 0.0515  0.0882  0.0244  235 GLY   A C   
1883 O  O   . GLY   A 234 ? 0.2582 0.4078 0.2010 0.0811  0.1087  0.0381  235 GLY   A O   
1884 N  N   . GLU   A 235 ? 0.1805 0.2682 0.2032 0.0631  0.0906  0.0553  236 GLU   A N   
1885 C  CA  . GLU   A 235 ? 0.2043 0.2279 0.2237 0.0708  0.0743  0.0603  236 GLU   A CA  
1886 C  C   . GLU   A 235 ? 0.2301 0.2407 0.2183 0.0517  0.0900  0.0765  236 GLU   A C   
1887 O  O   . GLU   A 235 ? 0.2834 0.2383 0.2074 0.0416  0.0865  0.0355  236 GLU   A O   
1888 C  CB  . GLU   A 235 ? 0.2115 0.2399 0.2084 0.0538  0.0798  0.0786  236 GLU   A CB  
1889 C  CG  . GLU   A 235 ? 0.2536 0.2519 0.2385 0.0169  0.0824  0.0840  236 GLU   A CG  
1890 C  CD  . GLU   A 235 ? 0.3046 0.2635 0.2793 -0.0209 0.0891  0.0758  236 GLU   A CD  
1891 O  OE1 . GLU   A 235 ? 0.2918 0.2592 0.2710 -0.0336 0.0633  0.0689  236 GLU   A OE1 
1892 O  OE2 . GLU   A 235 ? 0.3939 0.2774 0.3602 -0.0336 0.1052  0.0821  236 GLU   A OE2 
1893 N  N   . PRO   A 236 ? 0.1918 0.2843 0.2568 0.0580  0.1197  0.0846  237 PRO   A N   
1894 C  CA  . PRO   A 236 ? 0.2337 0.2741 0.2459 0.0704  0.1078  0.0775  237 PRO   A CA  
1895 C  C   . PRO   A 236 ? 0.2421 0.2528 0.1808 0.0427  0.0957  0.0353  237 PRO   A C   
1896 O  O   . PRO   A 236 ? 0.2333 0.2363 0.2251 0.0212  0.0793  0.0233  237 PRO   A O   
1897 C  CB  . PRO   A 236 ? 0.2336 0.2990 0.2741 0.0560  0.1184  0.0913  237 PRO   A CB  
1898 C  CG  . PRO   A 236 ? 0.2294 0.3097 0.3037 0.0546  0.1016  0.1118  237 PRO   A CG  
1899 C  CD  . PRO   A 236 ? 0.2158 0.2971 0.2740 0.0562  0.0966  0.1054  237 PRO   A CD  
1900 N  N   . GLU   A 237 ? 0.2260 0.2485 0.1682 0.0563  0.0815  -0.0073 238 GLU   A N   
1901 C  CA  . GLU   A 237 ? 0.2290 0.2183 0.1528 0.0287  0.0619  -0.0241 238 GLU   A CA  
1902 C  C   . GLU   A 237 ? 0.2110 0.1944 0.1442 0.0261  0.0688  -0.0133 238 GLU   A C   
1903 O  O   . GLU   A 237 ? 0.1907 0.2041 0.1676 0.0284  0.0526  -0.0052 238 GLU   A O   
1904 C  CB  . GLU   A 237 ? 0.2723 0.2239 0.1642 0.0409  0.0395  -0.0657 238 GLU   A CB  
1905 C  CG  . GLU   A 237 ? 0.2630 0.2332 0.1885 0.0357  0.0274  -0.0812 238 GLU   A CG  
1906 C  CD  . GLU   A 237 ? 0.2730 0.2427 0.2072 0.0248  0.0221  -0.1071 238 GLU   A CD  
1907 O  OE1 . GLU   A 237 ? 0.3775 0.2953 0.3662 0.0370  0.0134  -0.1620 238 GLU   A OE1 
1908 O  OE2 . GLU   A 237 ? 0.2433 0.1949 0.1973 0.0045  0.0204  -0.0746 238 GLU   A OE2 
1909 N  N   . GLU   A 238 ? 0.1799 0.1705 0.1270 0.0175  0.0461  -0.0037 239 GLU   A N   
1910 C  CA  . GLU   A 238 ? 0.1657 0.1869 0.1406 0.0129  0.0493  0.0025  239 GLU   A CA  
1911 C  C   . GLU   A 238 ? 0.1545 0.1434 0.1167 0.0136  0.0525  0.0015  239 GLU   A C   
1912 O  O   . GLU   A 238 ? 0.1795 0.1339 0.1503 -0.0048 0.0438  0.0065  239 GLU   A O   
1913 C  CB  . GLU   A 238 ? 0.2169 0.2385 0.1659 -0.0036 0.0300  0.0137  239 GLU   A CB  
1914 C  CG  . GLU   A 238 ? 0.2383 0.2668 0.2380 0.0277  0.0269  0.0001  239 GLU   A CG  
1915 C  CD  . GLU   A 238 ? 0.3272 0.3098 0.3154 -0.0076 0.0043  0.0036  239 GLU   A CD  
1916 O  OE1 . GLU   A 238 ? 0.4178 0.4080 0.4033 -0.0217 -0.0587 -0.0130 239 GLU   A OE1 
1917 O  OE2 . GLU   A 238 ? 0.4252 0.3168 0.4014 -0.0749 -0.0178 0.0232  239 GLU   A OE2 
1918 N  N   . LEU   A 239 ? 0.1581 0.1325 0.1009 0.0127  0.0408  -0.0077 240 LEU   A N   
1919 C  CA  . LEU   A 239 ? 0.1398 0.1327 0.0870 0.0074  0.0368  0.0034  240 LEU   A CA  
1920 C  C   . LEU   A 239 ? 0.1420 0.1266 0.0693 0.0036  0.0238  0.0082  240 LEU   A C   
1921 O  O   . LEU   A 239 ? 0.1286 0.1341 0.0871 0.0067  0.0246  0.0111  240 LEU   A O   
1922 C  CB  . LEU   A 239 ? 0.1418 0.1195 0.1187 0.0137  0.0318  0.0002  240 LEU   A CB  
1923 C  CG  . LEU   A 239 ? 0.1683 0.1215 0.1537 0.0202  0.0213  -0.0182 240 LEU   A CG  
1924 C  CD1 . LEU   A 239 ? 0.2161 0.1225 0.2001 0.0252  0.0124  -0.0137 240 LEU   A CD1 
1925 C  CD2 . LEU   A 239 ? 0.1988 0.1257 0.1425 0.0200  0.0237  -0.0304 240 LEU   A CD2 
1926 N  N   . MET   A 240 ? 0.1348 0.1206 0.0704 0.0058  0.0211  -0.0050 241 MET   A N   
1927 C  CA  . MET   A 240 ? 0.1280 0.1142 0.0677 -0.0064 0.0192  -0.0029 241 MET   A CA  
1928 C  C   . MET   A 240 ? 0.1226 0.1003 0.0655 -0.0055 0.0120  -0.0066 241 MET   A C   
1929 O  O   . MET   A 240 ? 0.1194 0.1175 0.0701 -0.0079 0.0109  -0.0032 241 MET   A O   
1930 C  CB  . MET   A 240 ? 0.1362 0.1077 0.0719 -0.0080 0.0142  0.0078  241 MET   A CB  
1931 C  CG  . MET   A 240 ? 0.1361 0.1129 0.0771 -0.0198 0.0135  -0.0133 241 MET   A CG  
1932 S  SD  . MET   A 240 ? 0.1384 0.0993 0.0958 -0.0103 0.0189  -0.0001 241 MET   A SD  
1933 C  CE  . MET   A 240 ? 0.1596 0.1087 0.0975 -0.0269 0.0201  0.0130  241 MET   A CE  
1934 N  N   . VAL   A 241 ? 0.1079 0.0956 0.0670 -0.0096 0.0137  -0.0060 242 VAL   A N   
1935 C  CA  . VAL   A 241 ? 0.1082 0.0968 0.0556 -0.0030 0.0091  -0.0064 242 VAL   A CA  
1936 C  C   . VAL   A 241 ? 0.0988 0.0778 0.0678 -0.0013 0.0068  -0.0093 242 VAL   A C   
1937 O  O   . VAL   A 241 ? 0.0910 0.1111 0.0722 -0.0081 0.0140  -0.0092 242 VAL   A O   
1938 C  CB  . VAL   A 241 ? 0.1241 0.1090 0.0782 -0.0060 0.0094  -0.0176 242 VAL   A CB  
1939 C  CG1 . VAL   A 241 ? 0.1501 0.1203 0.0795 -0.0117 0.0048  -0.0211 242 VAL   A CG1 
1940 C  CG2 . VAL   A 241 ? 0.1317 0.1180 0.0942 -0.0006 0.0052  -0.0134 242 VAL   A CG2 
1941 N  N   . ASP   A 242 ? 0.0852 0.0740 0.0671 -0.0048 0.0031  -0.0090 243 ASP   A N   
1942 C  CA  . ASP   A 242 ? 0.0946 0.0744 0.0735 0.0042  0.0054  -0.0122 243 ASP   A CA  
1943 C  C   . ASP   A 242 ? 0.0862 0.0752 0.0643 -0.0030 -0.0013 -0.0126 243 ASP   A C   
1944 O  O   . ASP   A 242 ? 0.0937 0.0878 0.1035 0.0011  -0.0170 -0.0196 243 ASP   A O   
1945 C  CB  . ASP   A 242 ? 0.0978 0.0853 0.0856 0.0087  0.0109  -0.0136 243 ASP   A CB  
1946 C  CG  . ASP   A 242 ? 0.0997 0.0820 0.0934 0.0106  0.0073  -0.0136 243 ASP   A CG  
1947 O  OD1 . ASP   A 242 ? 0.0987 0.0808 0.0915 0.0086  0.0098  -0.0101 243 ASP   A OD1 
1948 O  OD2 . ASP   A 242 ? 0.1272 0.0929 0.1262 0.0153  0.0239  -0.0217 243 ASP   A OD2 
1949 N  N   . ASN   A 243 ? 0.0752 0.0764 0.0622 -0.0050 0.0056  -0.0103 244 ASN   A N   
1950 C  CA  . ASN   A 243 ? 0.0766 0.0762 0.0630 -0.0058 0.0002  -0.0070 244 ASN   A CA  
1951 C  C   . ASN   A 243 ? 0.0644 0.0693 0.0681 -0.0051 -0.0008 -0.0042 244 ASN   A C   
1952 O  O   . ASN   A 243 ? 0.0929 0.0881 0.0644 0.0082  0.0026  -0.0009 244 ASN   A O   
1953 C  CB  . ASN   A 243 ? 0.0768 0.0824 0.0559 -0.0112 0.0071  0.0004  244 ASN   A CB  
1954 C  CG  . ASN   A 243 ? 0.0795 0.0899 0.0713 -0.0184 -0.0034 0.0105  244 ASN   A CG  
1955 O  OD1 . ASN   A 243 ? 0.0835 0.0873 0.0873 -0.0093 0.0021  0.0144  244 ASN   A OD1 
1956 N  ND2 . ASN   A 243 ? 0.0983 0.1298 0.1227 -0.0255 -0.0193 0.0454  244 ASN   A ND2 
1957 N  N   . TRP   A 244 ? 0.0645 0.0705 0.0625 0.0029  0.0038  -0.0078 245 TRP   A N   
1958 C  CA  . TRP   A 244 ? 0.0679 0.0718 0.0589 0.0000  -0.0032 -0.0121 245 TRP   A CA  
1959 C  C   . TRP   A 244 ? 0.0720 0.0847 0.0579 0.0004  -0.0031 -0.0102 245 TRP   A C   
1960 O  O   . TRP   A 244 ? 0.0785 0.1050 0.0737 0.0070  -0.0104 -0.0214 245 TRP   A O   
1961 C  CB  . TRP   A 244 ? 0.0709 0.0802 0.0636 -0.0042 0.0004  -0.0069 245 TRP   A CB  
1962 C  CG  . TRP   A 244 ? 0.0692 0.0794 0.0639 -0.0025 0.0018  -0.0032 245 TRP   A CG  
1963 C  CD1 . TRP   A 244 ? 0.0713 0.0691 0.0719 -0.0054 0.0033  -0.0040 245 TRP   A CD1 
1964 C  CD2 . TRP   A 244 ? 0.0791 0.0754 0.0708 0.0031  0.0023  0.0020  245 TRP   A CD2 
1965 N  NE1 . TRP   A 244 ? 0.0903 0.0686 0.0716 -0.0001 0.0013  -0.0091 245 TRP   A NE1 
1966 C  CE2 . TRP   A 244 ? 0.0809 0.0774 0.0749 0.0063  0.0051  0.0008  245 TRP   A CE2 
1967 C  CE3 . TRP   A 244 ? 0.0959 0.0820 0.0758 0.0001  -0.0046 0.0018  245 TRP   A CE3 
1968 C  CZ2 . TRP   A 244 ? 0.1034 0.0824 0.0953 0.0149  -0.0012 0.0029  245 TRP   A CZ2 
1969 C  CZ3 . TRP   A 244 ? 0.1177 0.0973 0.0820 0.0033  -0.0157 0.0045  245 TRP   A CZ3 
1970 C  CH2 . TRP   A 244 ? 0.1138 0.0891 0.1042 0.0114  -0.0108 0.0157  245 TRP   A CH2 
1971 N  N   . ARG   A 245 ? 0.0573 0.0835 0.0561 0.0023  -0.0084 -0.0142 246 ARG   A N   
1972 C  CA  . ARG   A 245 ? 0.0560 0.0899 0.0620 -0.0004 -0.0074 -0.0098 246 ARG   A CA  
1973 C  C   . ARG   A 245 ? 0.0671 0.0861 0.0638 0.0010  -0.0093 -0.0065 246 ARG   A C   
1974 O  O   . ARG   A 245 ? 0.0746 0.0839 0.0773 -0.0012 -0.0047 -0.0074 246 ARG   A O   
1975 C  CB  . ARG   A 245 ? 0.0605 0.0915 0.0570 -0.0013 -0.0046 -0.0083 246 ARG   A CB  
1976 C  CG  . ARG   A 245 ? 0.0532 0.0917 0.0653 -0.0055 -0.0013 -0.0093 246 ARG   A CG  
1977 C  CD  . ARG   A 245 ? 0.0517 0.0967 0.0654 -0.0073 -0.0061 -0.0145 246 ARG   A CD  
1978 N  NE  . ARG   A 245 ? 0.0556 0.1001 0.0797 -0.0079 -0.0150 -0.0159 246 ARG   A NE  
1979 C  CZ  . ARG   A 245 ? 0.0620 0.1064 0.0776 -0.0146 -0.0090 -0.0102 246 ARG   A CZ  
1980 N  NH1 . ARG   A 245 ? 0.0749 0.1043 0.0893 -0.0152 -0.0079 -0.0189 246 ARG   A NH1 
1981 N  NH2 . ARG   A 245 ? 0.0677 0.1177 0.1026 -0.0170 -0.0111 -0.0213 246 ARG   A NH2 
1982 N  N   . PRO   A 246 ? 0.0818 0.0965 0.0705 0.0073  -0.0080 0.0033  247 PRO   A N   
1983 C  CA  . PRO   A 246 ? 0.0936 0.1001 0.0742 0.0156  -0.0103 0.0044  247 PRO   A CA  
1984 C  C   . PRO   A 246 ? 0.0837 0.0991 0.0778 0.0151  -0.0105 0.0002  247 PRO   A C   
1985 O  O   . PRO   A 246 ? 0.0810 0.0991 0.0714 0.0115  -0.0101 -0.0054 247 PRO   A O   
1986 C  CB  . PRO   A 246 ? 0.1129 0.1274 0.0921 0.0329  0.0011  0.0132  247 PRO   A CB  
1987 C  CG  . PRO   A 246 ? 0.1159 0.1483 0.1416 0.0288  -0.0124 0.0124  247 PRO   A CG  
1988 C  CD  . PRO   A 246 ? 0.0866 0.1159 0.0998 0.0155  -0.0061 0.0047  247 PRO   A CD  
1989 N  N   . ALA   A 247 ? 0.0976 0.0960 0.0760 0.0121  -0.0060 -0.0035 248 ALA   A N   
1990 C  CA  . ALA   A 247 ? 0.0961 0.1042 0.0762 0.0173  -0.0079 -0.0003 248 ALA   A CA  
1991 C  C   . ALA   A 247 ? 0.0835 0.1044 0.0735 0.0191  -0.0095 0.0073  248 ALA   A C   
1992 O  O   . ALA   A 247 ? 0.0944 0.1150 0.0968 0.0311  -0.0216 0.0008  248 ALA   A O   
1993 C  CB  . ALA   A 247 ? 0.1012 0.1250 0.0909 0.0003  0.0007  -0.0057 248 ALA   A CB  
1994 N  N   . GLN   A 248 ? 0.0669 0.1035 0.0760 0.0187  -0.0124 0.0022  249 GLN   A N   
1995 C  CA  . GLN   A 248 ? 0.0743 0.1225 0.0736 0.0191  -0.0152 0.0003  249 GLN   A CA  
1996 C  C   . GLN   A 248 ? 0.0831 0.1140 0.0664 0.0280  -0.0173 0.0066  249 GLN   A C   
1997 O  O   . GLN   A 248 ? 0.0970 0.1222 0.0820 0.0150  -0.0037 0.0088  249 GLN   A O   
1998 C  CB  . GLN   A 248 ? 0.0863 0.1209 0.0812 0.0056  -0.0188 -0.0026 249 GLN   A CB  
1999 C  CG  . GLN   A 248 ? 0.0923 0.1125 0.0829 -0.0025 -0.0154 0.0004  249 GLN   A CG  
2000 C  CD  . GLN   A 248 ? 0.0850 0.1337 0.1006 -0.0112 -0.0157 -0.0112 249 GLN   A CD  
2001 O  OE1 . GLN   A 248 ? 0.0766 0.1707 0.1295 -0.0174 -0.0025 -0.0377 249 GLN   A OE1 
2002 N  NE2 . GLN   A 248 ? 0.0869 0.1506 0.0988 -0.0079 -0.0124 -0.0099 249 GLN   A NE2 
2003 N  N   . PRO   A 249 ? 0.0890 0.1389 0.0784 0.0299  -0.0230 -0.0038 250 PRO   A N   
2004 C  CA  . PRO   A 249 ? 0.1150 0.1433 0.0779 0.0370  -0.0283 -0.0006 250 PRO   A CA  
2005 C  C   . PRO   A 249 ? 0.1018 0.1247 0.0787 0.0295  -0.0244 -0.0011 250 PRO   A C   
2006 O  O   . PRO   A 249 ? 0.0920 0.1301 0.0766 0.0332  -0.0224 0.0092  250 PRO   A O   
2007 C  CB  . PRO   A 249 ? 0.1176 0.1730 0.1063 0.0418  -0.0457 -0.0113 250 PRO   A CB  
2008 C  CG  . PRO   A 249 ? 0.1052 0.1926 0.1120 0.0313  -0.0420 -0.0113 250 PRO   A CG  
2009 C  CD  . PRO   A 249 ? 0.0912 0.1632 0.0983 0.0242  -0.0283 -0.0139 250 PRO   A CD  
2010 N  N   . LEU   A 250 ? 0.1227 0.1259 0.0891 0.0294  -0.0155 0.0137  251 LEU   A N   
2011 C  CA  . LEU   A 250 ? 0.1203 0.1304 0.0867 0.0241  -0.0157 0.0098  251 LEU   A CA  
2012 C  C   . LEU   A 250 ? 0.1065 0.1321 0.0698 0.0263  -0.0203 0.0122  251 LEU   A C   
2013 O  O   . LEU   A 250 ? 0.0991 0.1316 0.0821 0.0242  -0.0293 0.0003  251 LEU   A O   
2014 C  CB  . LEU   A 250 ? 0.1490 0.1325 0.1103 0.0101  0.0005  0.0027  251 LEU   A CB  
2015 C  CG  . LEU   A 250 ? 0.1479 0.1558 0.1220 -0.0106 0.0215  -0.0119 251 LEU   A CG  
2016 C  CD1 . LEU   A 250 ? 0.1171 0.1613 0.1293 -0.0068 0.0153  -0.0260 251 LEU   A CD1 
2017 C  CD2 . LEU   A 250 ? 0.1713 0.1793 0.1532 -0.0253 0.0366  -0.0096 251 LEU   A CD2 
2018 N  N   . LYS   A 251 ? 0.1136 0.1622 0.0822 0.0441  -0.0357 -0.0029 252 LYS   A N   
2019 C  CA  . LYS   A 251 ? 0.1263 0.2097 0.0858 0.0396  -0.0457 -0.0187 252 LYS   A CA  
2020 C  C   . LYS   A 251 ? 0.1316 0.2142 0.1054 0.0365  -0.0445 -0.0190 252 LYS   A C   
2021 O  O   . LYS   A 251 ? 0.1804 0.2480 0.1054 0.0303  -0.0042 -0.0113 252 LYS   A O   
2022 C  CB  . LYS   A 251 ? 0.1346 0.2209 0.1332 0.0155  -0.0462 -0.0446 252 LYS   A CB  
2023 C  CG  . LYS   A 251 ? 0.1425 0.2889 0.1648 0.0209  -0.0356 -0.0586 252 LYS   A CG  
2024 C  CD  . LYS   A 251 ? 0.2247 0.2983 0.2137 0.0266  -0.0218 -0.0413 252 LYS   A CD  
2025 C  CE  . LYS   A 251 ? 0.1717 0.3435 0.2588 0.0270  -0.0248 -0.0287 252 LYS   A CE  
2026 N  NZ  . LYS   A 251 ? 0.2529 0.3599 0.3016 0.0284  -0.0239 -0.0041 252 LYS   A NZ  
2027 N  N   . ASN   A 252 ? 0.1452 0.2359 0.1077 0.0337  -0.0429 -0.0503 253 ASN   A N   
2028 C  CA  . ASN   A 252 ? 0.1996 0.2873 0.1179 0.0438  -0.0462 -0.0713 253 ASN   A CA  
2029 C  C   . ASN   A 252 ? 0.1724 0.2478 0.1613 0.0486  -0.0237 -0.0494 253 ASN   A C   
2030 O  O   . ASN   A 252 ? 0.2582 0.2615 0.2158 0.0377  -0.0199 -0.0612 253 ASN   A O   
2031 C  CB  . ASN   A 252 ? 0.2232 0.3357 0.1718 0.0297  -0.0536 -0.0925 253 ASN   A CB  
2032 C  CG  . ASN   A 252 ? 0.2871 0.3570 0.2179 0.0483  -0.0083 -0.0777 253 ASN   A CG  
2033 O  OD1 . ASN   A 252 ? 0.3736 0.4462 0.2427 0.0228  0.0306  -0.0522 253 ASN   A OD1 
2034 N  ND2 . ASN   A 252 ? 0.3078 0.3758 0.2733 0.0555  0.0114  -0.0980 253 ASN   A ND2 
2035 N  N   . ARG   A 253 ? 0.1089 0.2140 0.0928 0.0275  -0.0342 0.0114  254 ARG   A N   
2036 C  CA  . ARG   A 253 ? 0.1033 0.1544 0.0769 0.0159  -0.0233 -0.0089 254 ARG   A CA  
2037 C  C   . ARG   A 253 ? 0.1116 0.1471 0.1033 0.0179  0.0011  -0.0184 254 ARG   A C   
2038 O  O   . ARG   A 253 ? 0.1507 0.1622 0.1797 0.0272  0.0481  0.0094  254 ARG   A O   
2039 C  CB  . ARG   A 253 ? 0.0977 0.1374 0.0752 0.0148  -0.0262 -0.0120 254 ARG   A CB  
2040 C  CG  . ARG   A 253 ? 0.1126 0.1157 0.0770 0.0183  -0.0175 -0.0164 254 ARG   A CG  
2041 C  CD  . ARG   A 253 ? 0.1185 0.1062 0.0740 0.0191  -0.0192 -0.0139 254 ARG   A CD  
2042 N  NE  . ARG   A 253 ? 0.0886 0.0997 0.0602 0.0144  -0.0238 -0.0014 254 ARG   A NE  
2043 C  CZ  . ARG   A 253 ? 0.0774 0.0866 0.0597 0.0076  -0.0232 0.0002  254 ARG   A CZ  
2044 N  NH1 . ARG   A 253 ? 0.0609 0.0857 0.0648 0.0146  -0.0166 -0.0013 254 ARG   A NH1 
2045 N  NH2 . ARG   A 253 ? 0.0735 0.0995 0.0596 0.0115  -0.0273 -0.0004 254 ARG   A NH2 
2046 N  N   . GLN   A 254 ? 0.1080 0.1679 0.1039 0.0207  -0.0034 -0.0422 255 GLN   A N   
2047 C  CA  . GLN   A 254 ? 0.1350 0.1757 0.1077 0.0009  -0.0138 -0.0433 255 GLN   A CA  
2048 C  C   . GLN   A 254 ? 0.1111 0.1555 0.1028 0.0025  -0.0067 -0.0216 255 GLN   A C   
2049 O  O   . GLN   A 254 ? 0.1651 0.1422 0.1801 0.0007  -0.0492 -0.0334 255 GLN   A O   
2050 C  CB  . GLN   A 254 ? 0.1658 0.2036 0.1248 0.0063  0.0050  -0.0185 255 GLN   A CB  
2051 C  CG  . GLN   A 254 ? 0.1980 0.2156 0.1416 0.0212  0.0097  0.0064  255 GLN   A CG  
2052 C  CD  . GLN   A 254 ? 0.2125 0.1817 0.1474 0.0373  0.0100  0.0188  255 GLN   A CD  
2053 O  OE1 . GLN   A 254 ? 0.2624 0.1788 0.2001 0.0472  0.0236  0.0159  255 GLN   A OE1 
2054 N  NE2 . GLN   A 254 ? 0.2253 0.2212 0.1550 0.0463  0.0127  0.0382  255 GLN   A NE2 
2055 N  N   . ILE   A 255 ? 0.0899 0.1250 0.0715 0.0111  -0.0107 0.0012  256 ILE   A N   
2056 C  CA  . ILE   A 255 ? 0.0846 0.1100 0.0709 0.0063  -0.0112 0.0080  256 ILE   A CA  
2057 C  C   . ILE   A 255 ? 0.0842 0.1178 0.0650 0.0075  -0.0020 0.0139  256 ILE   A C   
2058 O  O   . ILE   A 255 ? 0.0970 0.1192 0.0883 0.0105  -0.0061 0.0321  256 ILE   A O   
2059 C  CB  . ILE   A 255 ? 0.0966 0.1104 0.0818 0.0090  -0.0151 0.0036  256 ILE   A CB  
2060 C  CG1 . ILE   A 255 ? 0.1121 0.1236 0.0976 0.0105  -0.0144 -0.0026 256 ILE   A CG1 
2061 C  CG2 . ILE   A 255 ? 0.1018 0.1212 0.0902 0.0156  -0.0187 -0.0104 256 ILE   A CG2 
2062 C  CD1 . ILE   A 255 ? 0.1449 0.1346 0.1069 0.0044  0.0042  -0.0118 256 ILE   A CD1 
2063 N  N   . LYS   A 256 ? 0.0836 0.1093 0.0551 0.0022  -0.0005 0.0160  257 LYS   A N   
2064 C  CA  . LYS   A 256 ? 0.0868 0.1274 0.0581 0.0058  0.0026  0.0144  257 LYS   A CA  
2065 C  C   . LYS   A 256 ? 0.0808 0.1217 0.0539 0.0062  -0.0083 0.0178  257 LYS   A C   
2066 O  O   . LYS   A 256 ? 0.0981 0.1415 0.0583 -0.0245 -0.0001 0.0058  257 LYS   A O   
2067 C  CB  . LYS   A 256 ? 0.1086 0.1352 0.0776 0.0152  0.0100  0.0051  257 LYS   A CB  
2068 C  CG  . LYS   A 256 ? 0.1512 0.1538 0.1186 0.0051  0.0074  -0.0146 257 LYS   A CG  
2069 C  CD  . LYS   A 256 ? 0.1900 0.1944 0.1465 0.0162  -0.0139 -0.0003 257 LYS   A CD  
2070 C  CE  . LYS   A 256 ? 0.2387 0.2307 0.1446 0.0204  -0.0047 -0.0169 257 LYS   A CE  
2071 N  NZ  . LYS   A 256 ? 0.2608 0.2507 0.1747 0.0286  -0.0337 0.0207  257 LYS   A NZ  
2072 N  N   . ALA   A 257 ? 0.0840 0.1413 0.0552 -0.0016 0.0072  0.0191  258 ALA   A N   
2073 C  CA  . ALA   A 257 ? 0.0693 0.1339 0.0661 0.0109  -0.0019 0.0150  258 ALA   A CA  
2074 C  C   . ALA   A 257 ? 0.0646 0.1231 0.0682 0.0049  0.0032  0.0196  258 ALA   A C   
2075 O  O   . ALA   A 257 ? 0.0863 0.1278 0.0748 0.0183  0.0078  0.0117  258 ALA   A O   
2076 C  CB  . ALA   A 257 ? 0.0817 0.1356 0.0881 0.0157  0.0112  0.0170  258 ALA   A CB  
2077 N  N   . SER   A 258 ? 0.0691 0.1252 0.0663 0.0084  -0.0016 0.0129  259 SER   A N   
2078 C  CA  . SER   A 258 ? 0.0775 0.1224 0.0848 0.0111  -0.0041 0.0148  259 SER   A CA  
2079 C  C   . SER   A 258 ? 0.0738 0.1403 0.1096 0.0043  0.0027  0.0208  259 SER   A C   
2080 O  O   . SER   A 258 ? 0.0756 0.1672 0.1445 0.0156  0.0185  0.0348  259 SER   A O   
2081 C  CB  . SER   A 258 ? 0.0827 0.1235 0.0833 0.0089  -0.0007 0.0143  259 SER   A CB  
2082 O  OG  . SER   A 258 ? 0.0650 0.1350 0.0824 0.0032  -0.0036 0.0064  259 SER   A OG  
2083 N  N   . PHE   A 259 ? 0.0761 0.1447 0.1141 0.0036  0.0150  0.0315  260 PHE   A N   
2084 C  CA  . PHE   A 259 ? 0.0926 0.1576 0.1655 0.0001  0.0165  0.0481  260 PHE   A CA  
2085 C  C   . PHE   A 259 ? 0.1367 0.2101 0.1864 -0.0142 0.0259  0.0721  260 PHE   A C   
2086 O  O   . PHE   A 259 ? 0.1703 0.2016 0.1862 0.0055  0.0124  0.0959  260 PHE   A O   
2087 C  CB  . PHE   A 259 ? 0.1123 0.1570 0.1935 -0.0109 0.0131  0.0356  260 PHE   A CB  
2088 C  CG  . PHE   A 259 ? 0.1195 0.1431 0.1990 -0.0093 -0.0001 0.0392  260 PHE   A CG  
2089 C  CD1 . PHE   A 259 ? 0.1292 0.1285 0.1402 -0.0096 -0.0116 0.0191  260 PHE   A CD1 
2090 C  CD2 . PHE   A 259 ? 0.1664 0.1495 0.2325 -0.0083 0.0318  0.0538  260 PHE   A CD2 
2091 C  CE1 . PHE   A 259 ? 0.1410 0.1309 0.1561 -0.0199 -0.0059 0.0090  260 PHE   A CE1 
2092 C  CE2 . PHE   A 259 ? 0.1827 0.1509 0.2532 0.0014  0.0360  0.0522  260 PHE   A CE2 
2093 C  CZ  . PHE   A 259 ? 0.1479 0.1363 0.2115 0.0057  0.0189  0.0163  260 PHE   A CZ  
2094 N  N   . LYS   A 260 ? 0.1720 0.2679 0.2491 -0.0346 0.0527  0.0956  261 LYS   A N   
2095 C  CA  . LYS   A 260 ? 0.2630 0.3216 0.3061 -0.0339 0.0656  0.1185  261 LYS   A CA  
2096 C  C   . LYS   A 260 ? 0.3280 0.3896 0.3639 -0.0320 0.0443  0.1069  261 LYS   A C   
2097 O  O   . LYS   A 260 ? 0.4394 0.4274 0.4562 -0.0400 0.0242  0.1581  261 LYS   A O   
2098 C  CB  . LYS   A 260 ? 0.3037 0.2619 0.3772 -0.0352 0.0449  0.1521  261 LYS   A CB  
2099 C  CG  . LYS   A 260 ? 0.3997 0.3741 0.4658 -0.0615 0.0068  0.1135  261 LYS   A CG  
2100 C  CD  . LYS   A 260 ? 0.4477 0.4216 0.5523 -0.0889 -0.0261 0.0897  261 LYS   A CD  
2101 C  CE  . LYS   A 260 ? 0.4977 0.4910 0.5974 -0.1010 -0.0505 0.0770  261 LYS   A CE  
2102 N  NZ  . LYS   A 260 ? 0.5218 0.5190 0.6412 -0.1092 -0.0672 0.0507  261 LYS   A NZ  
2103 ZN ZN  . ZN    B .   ? 0.0635 0.0710 0.0614 -0.0057 -0.0088 -0.0057 301 ZN    A ZN  
2104 C  C2  . A1IKU C .   ? 0.1978 0.1153 0.1786 0.0193  -0.0308 -0.0084 302 A1IKU A C2  
2105 C  C4  . A1IKU C .   ? 0.2381 0.1023 0.1860 0.0048  -0.0341 0.0069  302 A1IKU A C4  
2106 C  C5  . A1IKU C .   ? 0.2026 0.1229 0.2036 0.0172  -0.0700 -0.0027 302 A1IKU A C5  
2107 C  C6  . A1IKU C .   ? 0.1851 0.0946 0.2127 0.0050  -0.0630 -0.0117 302 A1IKU A C6  
2108 C  C1  . A1IKU C .   ? 0.1825 0.1182 0.1850 0.0108  -0.0575 0.0002  302 A1IKU A C1  
2109 C  C3  . A1IKU C .   ? 0.1977 0.1282 0.1917 0.0057  -0.0432 -0.0017 302 A1IKU A C3  
2110 C  C7  . A1IKU C .   ? 0.2878 0.1325 0.2255 0.0051  -0.0318 0.0304  302 A1IKU A C7  
2111 B  B1  . A1IKU C .   ? 0.1170 0.1166 0.1425 -0.0070 -0.0435 -0.0398 302 A1IKU A B1  
2112 O  O1  . A1IKU C .   ? 0.0844 0.0873 0.1359 -0.0132 -0.0275 -0.0091 302 A1IKU A O1  
2113 O  O2  . A1IKU C .   ? 0.1180 0.1274 0.1436 0.0078  -0.0464 -0.0431 302 A1IKU A O2  
2114 O  O3  . A1IKU C .   ? 0.1106 0.1392 0.1622 0.0026  -0.0639 0.0057  302 A1IKU A O3  
2115 C  C1  . GOL   D .   ? 0.1883 0.1951 0.1671 0.0078  -0.0296 0.0009  303 GOL   A C1  
2116 O  O1  . GOL   D .   ? 0.2269 0.1959 0.1835 0.0124  -0.0428 -0.0061 303 GOL   A O1  
2117 C  C2  . GOL   D .   ? 0.1785 0.1905 0.1512 0.0058  -0.0185 -0.0072 303 GOL   A C2  
2118 O  O2  . GOL   D .   ? 0.1635 0.1406 0.1443 0.0053  0.0003  0.0083  303 GOL   A O2  
2119 C  C3  . GOL   D .   ? 0.1549 0.2164 0.1486 0.0105  -0.0188 -0.0187 303 GOL   A C3  
2120 O  O3  . GOL   D .   ? 0.1681 0.1858 0.1656 0.0086  -0.0109 -0.0292 303 GOL   A O3  
2121 S  S   . DMS   E .   ? 0.2414 0.2371 0.2379 0.0066  0.0082  -0.0175 304 DMS   A S   
2122 O  O   . DMS   E .   ? 0.2076 0.2900 0.1893 0.0420  -0.0054 0.0075  304 DMS   A O   
2123 C  C1  . DMS   E .   ? 0.2186 0.2594 0.2609 -0.0037 -0.0270 0.0288  304 DMS   A C1  
2124 C  C2  . DMS   E .   ? 0.2601 0.2783 0.2684 0.0584  0.0175  -0.0011 304 DMS   A C2  
2125 HG HG  . MBO   F .   ? 0.0726 0.0798 0.0897 -0.0156 0.0046  -0.0223 305 MBO   A HG  
2126 C  CE1 . MBO   F .   ? 0.0709 0.1180 0.1219 -0.0165 -0.0065 -0.0485 305 MBO   A CE1 
2127 C  CE2 . MBO   F .   ? 0.0729 0.1176 0.1144 -0.0179 -0.0019 -0.0564 305 MBO   A CE2 
2128 C  CE3 . MBO   F .   ? 0.0955 0.1328 0.1042 -0.0113 0.0009  -0.0564 305 MBO   A CE3 
2129 C  CE4 . MBO   F .   ? 0.1075 0.1345 0.1235 -0.0075 0.0078  -0.0488 305 MBO   A CE4 
2130 C  CE5 . MBO   F .   ? 0.1102 0.1168 0.1271 -0.0142 0.0148  -0.0516 305 MBO   A CE5 
2131 C  CE6 . MBO   F .   ? 0.1150 0.1137 0.1238 -0.0142 0.0172  -0.0340 305 MBO   A CE6 
2132 C  CZ  . MBO   F .   ? 0.1188 0.1615 0.1317 -0.0129 0.0068  -0.0562 305 MBO   A CZ  
2133 O  OZ1 . MBO   F .   ? 0.1697 0.1782 0.1310 -0.0286 -0.0107 -0.0590 305 MBO   A OZ1 
2134 O  OZ2 . MBO   F .   ? 0.1175 0.1702 0.1054 -0.0268 0.0073  -0.0701 305 MBO   A OZ2 
2135 O  O   . HOH   G .   ? 0.4201 0.4008 0.2209 -0.0017 -0.0422 -0.0206 401 HOH   A O   
2136 O  O   . HOH   G .   ? 0.2754 0.2175 0.1974 0.0553  -0.0291 0.0226  402 HOH   A O   
2137 O  O   . HOH   G .   ? 0.2357 0.2618 0.1996 -0.0199 0.0047  -0.0470 403 HOH   A O   
2138 O  O   . HOH   G .   ? 0.2380 0.2055 0.5083 0.0329  -0.0276 -0.1233 404 HOH   A O   
2139 O  O   . HOH   G .   ? 0.2287 0.3428 0.2143 -0.1130 0.0841  -0.1441 405 HOH   A O   
2140 O  O   . HOH   G .   ? 0.2284 0.2474 0.1880 -0.0701 0.0482  -0.0918 406 HOH   A O   
2141 O  O   . HOH   G .   ? 0.5156 0.3772 0.3020 -0.0608 -0.0531 0.1099  407 HOH   A O   
2142 O  O   . HOH   G .   ? 0.4791 0.2243 0.3123 -0.0547 -0.0426 0.1225  408 HOH   A O   
2143 O  O   . HOH   G .   ? 0.1906 0.2153 0.2272 0.0254  -0.0198 0.0065  409 HOH   A O   
2144 O  O   . HOH   G .   ? 0.3078 0.1602 0.1920 -0.0411 0.0889  -0.0366 410 HOH   A O   
2145 O  O   . HOH   G .   ? 0.2539 0.1593 0.1941 0.0234  -0.1120 0.0268  411 HOH   A O   
2146 O  O   . HOH   G .   ? 0.1663 0.1734 0.1775 -0.0017 -0.0530 0.0013  412 HOH   A O   
2147 O  O   . HOH   G .   ? 0.2083 0.5099 0.3026 0.0822  -0.0153 0.1214  413 HOH   A O   
2148 O  O   . HOH   G .   ? 0.1160 0.0808 0.0481 -0.0092 -0.0102 0.0020  414 HOH   A O   
2149 O  O   . HOH   G .   ? 0.1978 0.2455 0.2441 0.0447  0.0692  -0.0006 415 HOH   A O   
2150 O  O   . HOH   G .   ? 0.2138 0.1443 0.2422 -0.0331 -0.0099 0.0167  416 HOH   A O   
2151 O  O   . HOH   G .   ? 0.0993 0.1011 0.0766 -0.0056 -0.0009 -0.0140 417 HOH   A O   
2152 O  O   . HOH   G .   ? 0.3391 0.3343 0.2594 0.0528  -0.0933 -0.1092 418 HOH   A O   
2153 O  O   . HOH   G .   ? 0.1124 0.1624 0.1552 0.0288  0.0142  0.0084  419 HOH   A O   
2154 O  O   . HOH   G .   ? 0.2688 0.2232 0.2997 -0.0112 0.0711  -0.0133 420 HOH   A O   
2155 O  O   . HOH   G .   ? 0.2259 0.1855 0.1244 -0.0549 -0.0275 -0.0073 421 HOH   A O   
2156 O  O   . HOH   G .   ? 0.2591 0.3290 0.4008 -0.0807 0.0874  -0.0779 422 HOH   A O   
2157 O  O   . HOH   G .   ? 0.1556 0.1288 0.2014 0.0000  0.0005  -0.0012 423 HOH   A O   
2158 O  O   . HOH   G .   ? 0.2420 0.4166 0.3252 0.0961  -0.0602 0.0271  424 HOH   A O   
2159 O  O   . HOH   G .   ? 0.1460 0.2041 0.1855 0.0105  -0.0890 -0.0501 425 HOH   A O   
2160 O  O   . HOH   G .   ? 0.2066 0.2501 0.1945 -0.0780 0.0331  0.0032  426 HOH   A O   
2161 O  O   . HOH   G .   ? 0.2395 0.3602 0.3062 0.1594  -0.1200 0.0279  427 HOH   A O   
2162 O  O   . HOH   G .   ? 0.3122 0.2348 0.1969 0.0234  0.0224  0.0592  428 HOH   A O   
2163 O  O   . HOH   G .   ? 0.3502 0.3131 0.2004 -0.0918 -0.0204 -0.0211 429 HOH   A O   
2164 O  O   . HOH   G .   ? 0.1810 0.2772 0.5072 -0.0464 0.0579  -0.0720 430 HOH   A O   
2165 O  O   . HOH   G .   ? 0.1064 0.3094 0.2295 0.0202  -0.0246 -0.0447 431 HOH   A O   
2166 O  O   . HOH   G .   ? 0.2601 0.3409 0.3465 0.0940  0.0278  0.1364  432 HOH   A O   
2167 O  O   . HOH   G .   ? 0.3353 0.1886 0.1891 -0.0355 0.1072  -0.0418 433 HOH   A O   
2168 O  O   . HOH   G .   ? 0.2005 0.1309 0.1148 -0.0075 0.0394  0.0260  434 HOH   A O   
2169 O  O   . HOH   G .   ? 0.1981 0.4284 0.3328 -0.0067 0.0028  -0.0042 435 HOH   A O   
2170 O  O   . HOH   G .   ? 0.1517 0.3433 0.2360 0.0359  0.0633  -0.0138 436 HOH   A O   
2171 O  O   . HOH   G .   ? 0.2665 0.2174 0.4231 -0.0138 0.1239  0.0052  437 HOH   A O   
2172 O  O   . HOH   G .   ? 0.2320 0.3004 0.2052 -0.0348 -0.0617 0.0621  438 HOH   A O   
2173 O  O   . HOH   G .   ? 0.4986 0.2802 0.1114 0.0102  -0.0185 0.0211  439 HOH   A O   
2174 O  O   . HOH   G .   ? 0.3297 0.2179 0.2939 -0.0610 -0.0945 0.0418  440 HOH   A O   
2175 O  O   . HOH   G .   ? 0.2554 0.2830 0.2302 -0.0770 -0.0219 -0.0693 441 HOH   A O   
2176 O  O   . HOH   G .   ? 0.1367 0.1740 0.1095 0.0094  -0.0232 -0.0199 442 HOH   A O   
2177 O  O   . HOH   G .   ? 0.3844 0.2544 0.2763 -0.0909 0.0425  0.0060  443 HOH   A O   
2178 O  O   . HOH   G .   ? 0.2315 0.2478 0.1403 -0.0173 -0.0256 0.0039  444 HOH   A O   
2179 O  O   . HOH   G .   ? 0.0972 0.0931 0.0858 -0.0013 -0.0017 -0.0110 445 HOH   A O   
2180 O  O   . HOH   G .   ? 0.1015 0.1362 0.1004 0.0007  -0.0264 0.0128  446 HOH   A O   
2181 O  O   . HOH   G .   ? 0.2033 0.0894 0.2091 -0.0320 0.0107  -0.0199 447 HOH   A O   
2182 O  O   . HOH   G .   ? 0.2864 0.1511 0.1743 0.0000  0.0431  0.0725  448 HOH   A O   
2183 O  O   . HOH   G .   ? 0.5248 0.3499 0.2136 0.0974  -0.0842 -0.0624 449 HOH   A O   
2184 O  O   . HOH   G .   ? 0.2665 0.1185 0.2231 0.0007  0.0251  0.0092  450 HOH   A O   
2185 O  O   . HOH   G .   ? 0.3216 0.3141 0.4071 0.1247  -0.1318 -0.0737 451 HOH   A O   
2186 O  O   . HOH   G .   ? 0.1444 0.1633 0.1188 -0.0075 0.0119  -0.0309 452 HOH   A O   
2187 O  O   . HOH   G .   ? 0.1683 0.1256 0.3010 -0.0030 0.0260  -0.0152 453 HOH   A O   
2188 O  O   . HOH   G .   ? 0.2448 0.2558 0.2458 0.1031  0.0214  -0.0044 454 HOH   A O   
2189 O  O   . HOH   G .   ? 0.1400 0.1744 0.1842 -0.0047 -0.0046 -0.0127 455 HOH   A O   
2190 O  O   . HOH   G .   ? 0.3276 0.2114 0.1932 0.0033  0.0680  -0.0734 456 HOH   A O   
2191 O  O   . HOH   G .   ? 0.2496 0.1543 0.1676 -0.0014 -0.0623 0.0030  457 HOH   A O   
2192 O  O   . HOH   G .   ? 0.1610 0.2316 0.1757 0.0251  -0.0520 -0.0008 458 HOH   A O   
2193 O  O   . HOH   G .   ? 0.1205 0.0798 0.1094 0.0007  0.0096  -0.0055 459 HOH   A O   
2194 O  O   . HOH   G .   ? 0.4114 0.3969 0.1873 -0.1419 -0.0613 -0.0127 460 HOH   A O   
2195 O  O   . HOH   G .   ? 0.0982 0.1609 0.1532 -0.0091 -0.0231 -0.0029 461 HOH   A O   
2196 O  O   . HOH   G .   ? 0.1168 0.3040 0.2657 -0.0442 -0.0230 -0.0638 462 HOH   A O   
2197 O  O   . HOH   G .   ? 0.2244 0.3012 0.3492 0.0324  0.0569  0.0061  463 HOH   A O   
2198 O  O   . HOH   G .   ? 0.2708 0.2721 0.2431 -0.0533 0.0546  -0.0291 464 HOH   A O   
2199 O  O   . HOH   G .   ? 0.0715 0.1461 0.1398 0.0008  -0.0170 -0.0317 465 HOH   A O   
2200 O  O   . HOH   G .   ? 0.2631 0.1905 0.2151 0.0319  -0.0011 -0.0547 466 HOH   A O   
2201 O  O   . HOH   G .   ? 0.1517 0.0897 0.1534 -0.0080 0.0124  0.0058  467 HOH   A O   
2202 O  O   . HOH   G .   ? 0.2189 0.2141 0.2047 0.0292  0.0018  0.0019  468 HOH   A O   
2203 O  O   . HOH   G .   ? 0.1963 0.2856 0.1431 0.0410  0.0000  -0.0393 469 HOH   A O   
2204 O  O   . HOH   G .   ? 0.0954 0.0897 0.0807 0.0184  -0.0127 -0.0035 470 HOH   A O   
2205 O  O   . HOH   G .   ? 0.1539 0.1037 0.1357 0.0331  0.0016  0.0173  471 HOH   A O   
2206 O  O   . HOH   G .   ? 0.1379 0.1617 0.3074 -0.0354 -0.0765 -0.0084 472 HOH   A O   
2207 O  O   . HOH   G .   ? 0.0746 0.0860 0.0869 -0.0167 0.0030  0.0072  473 HOH   A O   
2208 O  O   . HOH   G .   ? 0.3711 0.5005 0.0298 0.0511  0.0190  0.0577  474 HOH   A O   
2209 O  O   . HOH   G .   ? 0.3405 0.2702 0.2840 -0.0233 -0.0480 0.0700  475 HOH   A O   
2210 O  O   . HOH   G .   ? 0.1388 0.1479 0.1602 0.0211  -0.0265 0.0023  476 HOH   A O   
2211 O  O   . HOH   G .   ? 0.3384 0.3836 0.2142 -0.0109 -0.0888 0.0520  477 HOH   A O   
2212 O  O   . HOH   G .   ? 0.4362 0.4397 0.2902 -0.0569 0.0523  0.0337  478 HOH   A O   
2213 O  O   . HOH   G .   ? 0.0853 0.1054 0.0883 0.0244  -0.0090 -0.0056 479 HOH   A O   
2214 O  O   . HOH   G .   ? 0.3616 0.1449 0.2484 0.0797  -0.0769 -0.0163 480 HOH   A O   
2215 O  O   . HOH   G .   ? 0.2856 0.4428 0.2630 -0.1668 0.0037  0.0539  481 HOH   A O   
2216 O  O   . HOH   G .   ? 0.0460 0.6127 0.4714 -0.0187 0.0274  0.1445  482 HOH   A O   
2217 O  O   . HOH   G .   ? 0.2722 0.1016 0.2115 0.0091  -0.0727 -0.0088 483 HOH   A O   
2218 O  O   . HOH   G .   ? 0.2029 0.4121 0.2005 -0.0993 -0.0474 -0.0001 484 HOH   A O   
2219 O  O   . HOH   G .   ? 0.1519 0.1342 0.1573 0.0181  -0.0309 0.0120  485 HOH   A O   
2220 O  O   . HOH   G .   ? 0.1196 0.2948 0.2113 -0.0147 -0.0209 -0.0345 486 HOH   A O   
2221 O  O   . HOH   G .   ? 0.2071 0.1920 0.2280 -0.0248 -0.0207 -0.0416 487 HOH   A O   
2222 O  O   . HOH   G .   ? 0.2161 0.2500 0.1827 0.0961  0.0406  0.0805  488 HOH   A O   
2223 O  O   . HOH   G .   ? 0.1450 0.1750 0.1072 -0.0004 -0.0119 0.0021  489 HOH   A O   
2224 O  O   . HOH   G .   ? 0.2810 0.2415 0.4038 0.0347  -0.0991 0.0016  490 HOH   A O   
2225 O  O   . HOH   G .   ? 0.1971 0.1519 0.1394 0.0007  -0.0623 0.0170  491 HOH   A O   
2226 O  O   . HOH   G .   ? 0.1039 0.3101 0.2478 0.0236  -0.0284 0.0499  492 HOH   A O   
2227 O  O   . HOH   G .   ? 0.2926 0.4342 0.3521 0.0533  0.1386  -0.0021 493 HOH   A O   
2228 O  O   . HOH   G .   ? 0.1552 0.1758 0.1728 0.0473  0.0382  0.0497  494 HOH   A O   
2229 O  O   . HOH   G .   ? 0.2830 0.2147 0.6183 -0.0111 0.0942  -0.0764 495 HOH   A O   
2230 O  O   . HOH   G .   ? 0.2436 0.1715 0.2361 -0.0237 -0.0369 0.0672  496 HOH   A O   
2231 O  O   . HOH   G .   ? 0.3247 0.2073 0.1898 -0.0719 0.0337  -0.0400 497 HOH   A O   
2232 O  O   . HOH   G .   ? 0.5745 0.5588 0.3664 0.0230  0.0905  -0.0634 498 HOH   A O   
2233 O  O   . HOH   G .   ? 0.1706 0.1929 0.2978 0.0094  0.0055  0.0011  499 HOH   A O   
2234 O  O   . HOH   G .   ? 0.1156 0.1230 0.1082 0.0269  -0.0139 0.0282  500 HOH   A O   
2235 O  O   . HOH   G .   ? 0.3600 0.3544 0.0886 -0.0054 -0.0041 0.0116  501 HOH   A O   
2236 O  O   . HOH   G .   ? 0.1920 0.1759 0.1974 0.0091  -0.0061 0.0616  502 HOH   A O   
2237 O  O   . HOH   G .   ? 0.1612 0.2663 0.1450 -0.0048 -0.0152 -0.0332 503 HOH   A O   
2238 O  O   . HOH   G .   ? 0.1253 0.2296 0.1992 -0.0692 -0.0235 0.0383  504 HOH   A O   
2239 O  O   . HOH   G .   ? 0.3691 0.4587 0.3159 -0.0853 0.0756  -0.1560 505 HOH   A O   
2240 O  O   . HOH   G .   ? 0.3719 0.4840 0.4463 0.0520  -0.1209 0.0917  506 HOH   A O   
2241 O  O   . HOH   G .   ? 0.2305 0.4086 0.2728 -0.0355 0.0137  0.0739  507 HOH   A O   
2242 O  O   . HOH   G .   ? 0.1808 0.2072 0.2318 -0.0082 0.0105  0.0006  508 HOH   A O   
2243 O  O   . HOH   G .   ? 0.2048 0.1407 0.1509 -0.0143 -0.0046 0.0004  509 HOH   A O   
2244 O  O   . HOH   G .   ? 0.1488 0.2120 0.2743 0.0233  0.0714  -0.0103 510 HOH   A O   
2245 O  O   . HOH   G .   ? 0.0721 0.1762 0.1377 0.0072  -0.0091 -0.0451 511 HOH   A O   
2246 O  O   . HOH   G .   ? 0.1834 0.1311 0.1915 -0.0229 0.0153  -0.0120 512 HOH   A O   
2247 O  O   . HOH   G .   ? 0.1637 0.2193 0.1489 0.0809  0.0333  0.0371  513 HOH   A O   
2248 O  O   . HOH   G .   ? 0.2081 0.1032 0.2317 -0.0162 -0.0176 0.0309  514 HOH   A O   
2249 O  O   . HOH   G .   ? 0.3493 0.1535 0.2220 -0.0334 -0.0428 -0.0748 515 HOH   A O   
2250 O  O   . HOH   G .   ? 0.3303 0.3946 0.3992 -0.1477 0.0432  0.0867  516 HOH   A O   
2251 O  O   . HOH   G .   ? 0.1757 0.2857 0.1999 -0.0060 -0.0112 -0.0080 517 HOH   A O   
2252 O  O   . HOH   G .   ? 0.2752 0.2043 0.2612 0.0229  0.0140  -0.0678 518 HOH   A O   
2253 O  O   . HOH   G .   ? 0.3398 0.2905 0.3189 0.0967  0.0951  0.0771  519 HOH   A O   
2254 O  O   . HOH   G .   ? 0.4178 0.3491 0.2497 0.0079  0.0515  -0.0811 520 HOH   A O   
2255 O  O   . HOH   G .   ? 0.1796 0.2230 0.2436 0.0506  -0.0374 -0.0656 521 HOH   A O   
2256 O  O   . HOH   G .   ? 0.3219 0.2963 0.1615 0.1677  -0.0418 0.0180  522 HOH   A O   
2257 O  O   . HOH   G .   ? 0.2216 0.2172 0.3053 0.0281  0.0563  0.0433  523 HOH   A O   
2258 O  O   . HOH   G .   ? 0.2062 0.2937 0.2099 -0.0735 -0.0423 0.0277  524 HOH   A O   
2259 O  O   . HOH   G .   ? 0.3385 0.3289 0.5581 -0.0106 0.0967  -0.0573 525 HOH   A O   
2260 O  O   . HOH   G .   ? 0.4123 0.2121 0.1974 0.0178  0.0086  0.0398  526 HOH   A O   
2261 O  O   . HOH   G .   ? 0.1746 0.3029 0.1966 -0.0349 -0.0179 0.0109  527 HOH   A O   
2262 O  O   . HOH   G .   ? 0.1816 0.1958 0.1912 0.0255  0.0087  0.1109  528 HOH   A O   
2263 O  O   . HOH   G .   ? 0.3573 0.3160 0.2383 -0.0696 0.0932  0.0999  529 HOH   A O   
2264 O  O   . HOH   G .   ? 0.3284 0.2868 0.1378 -0.0295 0.0127  -0.0510 530 HOH   A O   
2265 O  O   . HOH   G .   ? 0.2363 0.2440 0.5885 -0.0399 0.0199  0.0678  531 HOH   A O   
2266 O  O   . HOH   G .   ? 0.1398 0.1394 0.1885 -0.0023 -0.0332 -0.0497 532 HOH   A O   
2267 O  O   . HOH   G .   ? 0.2305 0.1423 0.1479 -0.0121 0.0066  0.0006  533 HOH   A O   
2268 O  O   . HOH   G .   ? 0.2328 0.1982 0.4014 -0.0478 -0.0543 -0.0496 534 HOH   A O   
2269 O  O   . HOH   G .   ? 0.1219 0.2868 0.1897 0.0502  0.0025  0.0139  535 HOH   A O   
2270 O  O   . HOH   G .   ? 0.1780 0.1866 0.1324 0.0041  -0.0056 0.0370  536 HOH   A O   
2271 O  O   . HOH   G .   ? 0.2659 0.1094 0.1340 0.0185  -0.0314 0.0053  537 HOH   A O   
2272 O  O   . HOH   G .   ? 0.4344 0.2988 0.2851 0.0624  -0.0452 -0.0106 538 HOH   A O   
2273 O  O   . HOH   G .   ? 0.3248 0.1931 0.1680 -0.0477 -0.0572 -0.0204 539 HOH   A O   
2274 O  O   . HOH   G .   ? 0.0871 0.1701 0.1141 0.0083  -0.0384 0.0147  540 HOH   A O   
2275 O  O   . HOH   G .   ? 0.3529 0.1780 0.2319 0.0717  0.0361  0.0595  541 HOH   A O   
2276 O  O   . HOH   G .   ? 0.1478 0.1880 0.3219 -0.0751 -0.0272 -0.0234 542 HOH   A O   
2277 O  O   . HOH   G .   ? 0.3299 0.1832 0.5028 -0.0156 0.0638  -0.0619 543 HOH   A O   
2278 O  O   . HOH   G .   ? 0.2697 0.3779 0.1184 0.0687  -0.0463 0.0242  544 HOH   A O   
2279 O  O   . HOH   G .   ? 0.4405 0.3302 0.2806 -0.1275 -0.0007 -0.0705 545 HOH   A O   
2280 O  O   . HOH   G .   ? 0.2724 0.2519 0.2059 0.0406  -0.0721 0.0418  546 HOH   A O   
2281 O  O   . HOH   G .   ? 0.2341 0.3241 0.2724 -0.0383 -0.0067 0.0866  547 HOH   A O   
2282 O  O   . HOH   G .   ? 0.3367 0.3329 0.2827 0.0479  -0.0622 0.0463  548 HOH   A O   
2283 O  O   . HOH   G .   ? 0.0875 0.1023 0.1060 0.0241  -0.0151 0.0110  549 HOH   A O   
2284 O  O   . HOH   G .   ? 0.3986 0.2567 0.3672 0.0385  -0.0291 -0.0689 550 HOH   A O   
2285 O  O   . HOH   G .   ? 0.4731 0.2323 0.3426 -0.1118 0.0420  -0.0126 551 HOH   A O   
2286 O  O   . HOH   G .   ? 0.0937 0.1753 0.2281 -0.0140 0.0072  -0.0001 552 HOH   A O   
2287 O  O   . HOH   G .   ? 0.1873 0.1547 0.5413 0.0197  0.0254  -0.0111 553 HOH   A O   
2288 O  O   . HOH   G .   ? 0.3459 0.1751 0.2452 -0.0153 -0.0463 -0.0041 554 HOH   A O   
2289 O  O   . HOH   G .   ? 0.2714 0.2514 0.1715 -0.0111 -0.0463 -0.0647 555 HOH   A O   
2290 O  O   . HOH   G .   ? 0.2364 0.1880 0.1960 -0.0242 0.0312  -0.0158 556 HOH   A O   
2291 O  O   . HOH   G .   ? 0.2367 0.2219 0.2430 -0.0126 -0.0200 0.0683  557 HOH   A O   
2292 O  O   . HOH   G .   ? 0.2156 0.2570 0.1754 0.0646  0.0490  0.0571  558 HOH   A O   
2293 O  O   . HOH   G .   ? 0.2705 0.2368 0.1504 0.0286  -0.0191 0.0224  559 HOH   A O   
2294 O  O   . HOH   G .   ? 0.2808 0.4256 0.3943 0.0109  0.0325  -0.1597 560 HOH   A O   
2295 O  O   . HOH   G .   ? 0.1798 0.1600 0.2032 0.0168  0.0152  0.0213  561 HOH   A O   
2296 O  O   . HOH   G .   ? 0.1726 0.1715 0.2550 0.0782  -0.0194 -0.0042 562 HOH   A O   
2297 O  O   . HOH   G .   ? 0.1241 0.4723 0.2987 0.0003  -0.0729 0.0171  563 HOH   A O   
2298 O  O   . HOH   G .   ? 0.5023 0.1764 0.1908 -0.0242 0.0703  0.0017  564 HOH   A O   
2299 O  O   . HOH   G .   ? 0.3736 0.2738 0.3596 0.0784  -0.1614 0.0929  565 HOH   A O   
2300 O  O   . HOH   G .   ? 0.2613 0.2184 0.2887 0.0373  0.1015  0.0515  566 HOH   A O   
2301 O  O   . HOH   G .   ? 0.4068 0.3778 0.3314 -0.1925 -0.0321 -0.1057 567 HOH   A O   
2302 O  O   . HOH   G .   ? 0.3638 0.3773 0.2221 -0.1469 -0.0353 -0.0399 568 HOH   A O   
2303 O  O   . HOH   G .   ? 0.2287 0.2483 0.4534 0.0451  0.0799  0.1261  569 HOH   A O   
2304 O  O   . HOH   G .   ? 0.3207 0.3293 0.1938 -0.1092 -0.0675 0.0288  570 HOH   A O   
2305 O  O   . HOH   G .   ? 0.1562 0.0842 0.1346 -0.0178 -0.0260 -0.0037 571 HOH   A O   
2306 O  O   . HOH   G .   ? 0.2038 0.3028 0.2236 -0.0419 -0.0044 0.0138  572 HOH   A O   
2307 O  O   . HOH   G .   ? 0.3249 0.2942 0.3728 0.0447  0.0227  0.0400  573 HOH   A O   
2308 O  O   . HOH   G .   ? 0.2885 0.2488 0.2392 -0.0124 -0.0648 0.0187  574 HOH   A O   
2309 O  O   . HOH   G .   ? 0.3146 0.0974 0.2042 0.0324  0.0601  -0.0235 575 HOH   A O   
2310 O  O   . HOH   G .   ? 0.1816 0.2468 0.2705 0.0033  0.0138  0.0737  576 HOH   A O   
2311 O  O   . HOH   G .   ? 0.4314 0.2604 0.2534 -0.0274 0.0045  0.0268  577 HOH   A O   
2312 O  O   . HOH   G .   ? 0.3113 0.3678 0.2614 -0.1027 -0.0160 0.0590  578 HOH   A O   
2313 O  O   . HOH   G .   ? 0.2781 0.3004 0.2554 0.1216  -0.0478 0.0385  579 HOH   A O   
2314 O  O   . HOH   G .   ? 0.1789 0.1969 0.4261 0.0032  -0.1170 -0.0251 580 HOH   A O   
2315 O  O   . HOH   G .   ? 0.3283 0.1901 0.2613 0.0921  -0.2151 -0.0214 581 HOH   A O   
2316 O  O   . HOH   G .   ? 0.2520 0.3741 0.2812 -0.0046 -0.0115 -0.0483 582 HOH   A O   
2317 O  O   . HOH   G .   ? 0.2737 0.4742 0.3558 0.1040  -0.0410 0.0896  583 HOH   A O   
2318 O  O   . HOH   G .   ? 0.2833 0.2272 0.2340 -0.0105 -0.0196 0.0800  584 HOH   A O   
2319 O  O   . HOH   G .   ? 0.2968 0.3023 0.2392 0.0529  -0.0583 -0.0306 585 HOH   A O   
2320 O  O   . HOH   G .   ? 0.2631 0.1962 0.1829 -0.0780 -0.0371 -0.0139 586 HOH   A O   
2321 O  O   . HOH   G .   ? 0.5767 0.3531 0.4759 -0.0111 0.0359  -0.0560 587 HOH   A O   
2322 O  O   . HOH   G .   ? 0.4887 0.4213 0.2435 0.1445  -0.0161 0.0595  588 HOH   A O   
2323 O  O   . HOH   G .   ? 0.4240 0.2808 0.4258 -0.0662 -0.0532 0.0529  589 HOH   A O   
2324 O  O   . HOH   G .   ? 0.4279 0.3376 0.1908 -0.0573 0.1021  -0.0190 590 HOH   A O   
2325 O  O   . HOH   G .   ? 0.3828 0.2405 0.2702 -0.0387 -0.0284 0.0831  591 HOH   A O   
2326 O  O   . HOH   G .   ? 0.2729 0.2015 0.1617 0.0523  -0.0347 -0.0478 592 HOH   A O   
2327 O  O   . HOH   G .   ? 0.2057 0.2283 0.1995 0.0794  -0.0636 -0.0092 593 HOH   A O   
2328 O  O   . HOH   G .   ? 0.1813 0.1884 0.1764 -0.0102 0.0212  -0.0171 594 HOH   A O   
2329 O  O   . HOH   G .   ? 0.3760 0.2531 0.3403 -0.0703 0.0372  -0.0542 595 HOH   A O   
2330 O  O   . HOH   G .   ? 0.2131 0.4753 0.6041 -0.1038 -0.0724 -0.0090 596 HOH   A O   
2331 O  O   . HOH   G .   ? 0.2595 0.5135 0.2371 -0.0386 -0.0087 0.1545  597 HOH   A O   
2332 O  O   . HOH   G .   ? 0.4681 0.2500 0.3258 0.0093  0.0911  0.0017  598 HOH   A O   
2333 O  O   . HOH   G .   ? 0.2395 0.4303 0.3002 -0.0521 0.0889  -0.0250 599 HOH   A O   
2334 O  O   . HOH   G .   ? 0.2066 0.3302 0.4806 0.0064  0.0829  -0.1152 600 HOH   A O   
2335 O  O   . HOH   G .   ? 0.4368 0.1479 0.3162 -0.0124 0.1403  0.0040  601 HOH   A O   
2336 O  O   . HOH   G .   ? 0.2682 0.2511 0.2912 0.0864  0.0591  0.0444  602 HOH   A O   
2337 O  O   . HOH   G .   ? 0.3187 0.3611 0.3351 0.0669  0.0375  -0.0063 603 HOH   A O   
2338 O  O   . HOH   G .   ? 0.4207 0.4049 0.2806 0.0533  0.0832  -0.0646 604 HOH   A O   
2339 O  O   . HOH   G .   ? 0.3900 0.4970 0.3928 0.1075  -0.1239 0.0088  605 HOH   A O   
2340 O  O   . HOH   G .   ? 0.3960 0.3788 0.1751 0.0163  0.0674  -0.0296 606 HOH   A O   
2341 O  O   . HOH   G .   ? 0.4592 0.2568 0.3539 -0.0813 0.0881  -0.0274 607 HOH   A O   
2342 O  O   . HOH   G .   ? 0.4697 0.2949 0.4014 0.0213  0.0388  0.1193  608 HOH   A O   
2343 O  O   . HOH   G .   ? 0.1761 0.1897 0.2328 0.0064  0.0274  -0.0119 609 HOH   A O   
# 
