data_9FPR
# 
_entry.id   9FPR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9FPR         pdb_00009fpr 10.2210/pdb9fpr/pdb 
WWPDB D_1292139180 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FPR 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-13 
_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              alexeyus1@gmail.com 
_pdbx_contact_author.name_first         Alexey 
_pdbx_contact_author.name_last          Smirnov 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5080-9367 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'    1 0000-0001-5080-9367 
'Manakova, E.N.' 2 0000-0002-6027-2265 
'Grazulis, S.'   3 0000-0002-7928-5218 
'Paketuryte, V.' 4 0000-0003-0919-7826 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of carbonic anhydrase II with methyl 4-(2-phenylethylsulfanyl)-3-sulfamoyl-benzoate' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnov, A.'    1 0000-0001-5080-9367 
primary 'Manakova, E.N.' 2 0000-0002-6027-2265 
primary 'Grazulis, S.'   3 0000-0002-7928-5218 
primary 'Paketuryte, V.' 4 0000-0003-0919-7826 
# 
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 'methyl 4-(2-phenylethylsulfanyl)-3-sulfamoyl-benzoate' 351.440   1   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                    78.133    1   ?       ? ? ? 
5 water       nat water                                                   18.015    348 ?       ? ? ? 
# 
_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 'methyl 4-(2-phenylethylsulfanyl)-3-sulfamoyl-benzoate' A1IEN 
4 'DIMETHYL SULFOXIDE'                                    DMS   
5 water                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IEN non-polymer         . 'methyl 4-(2-phenylethylsulfanyl)-3-sulfamoyl-benzoate' ? 'C16 H17 N O4 S2' 351.440 
ALA   'L-peptide linking' y ALANINE                                                 ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                              ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                         ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                ? 'C3 H7 N O2 S'    121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                    ? 'C2 H6 O S'       78.133  
GLN   'L-peptide linking' y GLUTAMINE                                               ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                         ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                 ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                               ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                   ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                              ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                 ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                  ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                              ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                           ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                 ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                  ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                               ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                              ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                  ? 'C5 H11 N O2'     117.146 
ZN    non-polymer         . 'ZINC ION'                                              ? 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IEN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IEN 
_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 1   ZN    ZN  A . 
C 3 A1IEN 1   302 1   A1IEN JA4 A . 
D 4 DMS   1   303 1   DMS   DMS A . 
E 5 HOH   1   401 303 HOH   HOH A . 
E 5 HOH   2   402 331 HOH   HOH A . 
E 5 HOH   3   403 159 HOH   HOH A . 
E 5 HOH   4   404 102 HOH   HOH A . 
E 5 HOH   5   405 315 HOH   HOH A . 
E 5 HOH   6   406 213 HOH   HOH A . 
E 5 HOH   7   407 302 HOH   HOH A . 
E 5 HOH   8   408 271 HOH   HOH A . 
E 5 HOH   9   409 107 HOH   HOH A . 
E 5 HOH   10  410 311 HOH   HOH A . 
E 5 HOH   11  411 267 HOH   HOH A . 
E 5 HOH   12  412 216 HOH   HOH A . 
E 5 HOH   13  413 122 HOH   HOH A . 
E 5 HOH   14  414 318 HOH   HOH A . 
E 5 HOH   15  415 97  HOH   HOH A . 
E 5 HOH   16  416 232 HOH   HOH A . 
E 5 HOH   17  417 156 HOH   HOH A . 
E 5 HOH   18  418 273 HOH   HOH A . 
E 5 HOH   19  419 14  HOH   HOH A . 
E 5 HOH   20  420 127 HOH   HOH A . 
E 5 HOH   21  421 297 HOH   HOH A . 
E 5 HOH   22  422 38  HOH   HOH A . 
E 5 HOH   23  423 3   HOH   HOH A . 
E 5 HOH   24  424 282 HOH   HOH A . 
E 5 HOH   25  425 229 HOH   HOH A . 
E 5 HOH   26  426 74  HOH   HOH A . 
E 5 HOH   27  427 181 HOH   HOH A . 
E 5 HOH   28  428 141 HOH   HOH A . 
E 5 HOH   29  429 1   HOH   HOH A . 
E 5 HOH   30  430 109 HOH   HOH A . 
E 5 HOH   31  431 131 HOH   HOH A . 
E 5 HOH   32  432 115 HOH   HOH A . 
E 5 HOH   33  433 317 HOH   HOH A . 
E 5 HOH   34  434 15  HOH   HOH A . 
E 5 HOH   35  435 130 HOH   HOH A . 
E 5 HOH   36  436 6   HOH   HOH A . 
E 5 HOH   37  437 46  HOH   HOH A . 
E 5 HOH   38  438 300 HOH   HOH A . 
E 5 HOH   39  439 230 HOH   HOH A . 
E 5 HOH   40  440 255 HOH   HOH A . 
E 5 HOH   41  441 253 HOH   HOH A . 
E 5 HOH   42  442 344 HOH   HOH A . 
E 5 HOH   43  443 263 HOH   HOH A . 
E 5 HOH   44  444 22  HOH   HOH A . 
E 5 HOH   45  445 144 HOH   HOH A . 
E 5 HOH   46  446 192 HOH   HOH A . 
E 5 HOH   47  447 103 HOH   HOH A . 
E 5 HOH   48  448 47  HOH   HOH A . 
E 5 HOH   49  449 118 HOH   HOH A . 
E 5 HOH   50  450 55  HOH   HOH A . 
E 5 HOH   51  451 337 HOH   HOH A . 
E 5 HOH   52  452 160 HOH   HOH A . 
E 5 HOH   53  453 85  HOH   HOH A . 
E 5 HOH   54  454 111 HOH   HOH A . 
E 5 HOH   55  455 132 HOH   HOH A . 
E 5 HOH   56  456 209 HOH   HOH A . 
E 5 HOH   57  457 10  HOH   HOH A . 
E 5 HOH   58  458 16  HOH   HOH A . 
E 5 HOH   59  459 305 HOH   HOH A . 
E 5 HOH   60  460 183 HOH   HOH A . 
E 5 HOH   61  461 41  HOH   HOH A . 
E 5 HOH   62  462 194 HOH   HOH A . 
E 5 HOH   63  463 179 HOH   HOH A . 
E 5 HOH   64  464 5   HOH   HOH A . 
E 5 HOH   65  465 90  HOH   HOH A . 
E 5 HOH   66  466 32  HOH   HOH A . 
E 5 HOH   67  467 153 HOH   HOH A . 
E 5 HOH   68  468 92  HOH   HOH A . 
E 5 HOH   69  469 162 HOH   HOH A . 
E 5 HOH   70  470 347 HOH   HOH A . 
E 5 HOH   71  471 199 HOH   HOH A . 
E 5 HOH   72  472 186 HOH   HOH A . 
E 5 HOH   73  473 283 HOH   HOH A . 
E 5 HOH   74  474 4   HOH   HOH A . 
E 5 HOH   75  475 64  HOH   HOH A . 
E 5 HOH   76  476 108 HOH   HOH A . 
E 5 HOH   77  477 178 HOH   HOH A . 
E 5 HOH   78  478 231 HOH   HOH A . 
E 5 HOH   79  479 214 HOH   HOH A . 
E 5 HOH   80  480 133 HOH   HOH A . 
E 5 HOH   81  481 52  HOH   HOH A . 
E 5 HOH   82  482 129 HOH   HOH A . 
E 5 HOH   83  483 234 HOH   HOH A . 
E 5 HOH   84  484 180 HOH   HOH A . 
E 5 HOH   85  485 99  HOH   HOH A . 
E 5 HOH   86  486 58  HOH   HOH A . 
E 5 HOH   87  487 13  HOH   HOH A . 
E 5 HOH   88  488 9   HOH   HOH A . 
E 5 HOH   89  489 152 HOH   HOH A . 
E 5 HOH   90  490 339 HOH   HOH A . 
E 5 HOH   91  491 338 HOH   HOH A . 
E 5 HOH   92  492 248 HOH   HOH A . 
E 5 HOH   93  493 7   HOH   HOH A . 
E 5 HOH   94  494 137 HOH   HOH A . 
E 5 HOH   95  495 27  HOH   HOH A . 
E 5 HOH   96  496 91  HOH   HOH A . 
E 5 HOH   97  497 42  HOH   HOH A . 
E 5 HOH   98  498 62  HOH   HOH A . 
E 5 HOH   99  499 197 HOH   HOH A . 
E 5 HOH   100 500 96  HOH   HOH A . 
E 5 HOH   101 501 31  HOH   HOH A . 
E 5 HOH   102 502 319 HOH   HOH A . 
E 5 HOH   103 503 2   HOH   HOH A . 
E 5 HOH   104 504 94  HOH   HOH A . 
E 5 HOH   105 505 145 HOH   HOH A . 
E 5 HOH   106 506 84  HOH   HOH A . 
E 5 HOH   107 507 30  HOH   HOH A . 
E 5 HOH   108 508 82  HOH   HOH A . 
E 5 HOH   109 509 125 HOH   HOH A . 
E 5 HOH   110 510 308 HOH   HOH A . 
E 5 HOH   111 511 134 HOH   HOH A . 
E 5 HOH   112 512 328 HOH   HOH A . 
E 5 HOH   113 513 98  HOH   HOH A . 
E 5 HOH   114 514 8   HOH   HOH A . 
E 5 HOH   115 515 28  HOH   HOH A . 
E 5 HOH   116 516 138 HOH   HOH A . 
E 5 HOH   117 517 101 HOH   HOH A . 
E 5 HOH   118 518 68  HOH   HOH A . 
E 5 HOH   119 519 110 HOH   HOH A . 
E 5 HOH   120 520 333 HOH   HOH A . 
E 5 HOH   121 521 301 HOH   HOH A . 
E 5 HOH   122 522 37  HOH   HOH A . 
E 5 HOH   123 523 56  HOH   HOH A . 
E 5 HOH   124 524 12  HOH   HOH A . 
E 5 HOH   125 525 165 HOH   HOH A . 
E 5 HOH   126 526 69  HOH   HOH A . 
E 5 HOH   127 527 11  HOH   HOH A . 
E 5 HOH   128 528 242 HOH   HOH A . 
E 5 HOH   129 529 330 HOH   HOH A . 
E 5 HOH   130 530 40  HOH   HOH A . 
E 5 HOH   131 531 70  HOH   HOH A . 
E 5 HOH   132 532 60  HOH   HOH A . 
E 5 HOH   133 533 54  HOH   HOH A . 
E 5 HOH   134 534 75  HOH   HOH A . 
E 5 HOH   135 535 313 HOH   HOH A . 
E 5 HOH   136 536 93  HOH   HOH A . 
E 5 HOH   137 537 279 HOH   HOH A . 
E 5 HOH   138 538 17  HOH   HOH A . 
E 5 HOH   139 539 80  HOH   HOH A . 
E 5 HOH   140 540 48  HOH   HOH A . 
E 5 HOH   141 541 106 HOH   HOH A . 
E 5 HOH   142 542 20  HOH   HOH A . 
E 5 HOH   143 543 50  HOH   HOH A . 
E 5 HOH   144 544 136 HOH   HOH A . 
E 5 HOH   145 545 158 HOH   HOH A . 
E 5 HOH   146 546 25  HOH   HOH A . 
E 5 HOH   147 547 139 HOH   HOH A . 
E 5 HOH   148 548 327 HOH   HOH A . 
E 5 HOH   149 549 221 HOH   HOH A . 
E 5 HOH   150 550 195 HOH   HOH A . 
E 5 HOH   151 551 33  HOH   HOH A . 
E 5 HOH   152 552 29  HOH   HOH A . 
E 5 HOH   153 553 67  HOH   HOH A . 
E 5 HOH   154 554 87  HOH   HOH A . 
E 5 HOH   155 555 51  HOH   HOH A . 
E 5 HOH   156 556 119 HOH   HOH A . 
E 5 HOH   157 557 45  HOH   HOH A . 
E 5 HOH   158 558 66  HOH   HOH A . 
E 5 HOH   159 559 35  HOH   HOH A . 
E 5 HOH   160 560 73  HOH   HOH A . 
E 5 HOH   161 561 342 HOH   HOH A . 
E 5 HOH   162 562 147 HOH   HOH A . 
E 5 HOH   163 563 201 HOH   HOH A . 
E 5 HOH   164 564 117 HOH   HOH A . 
E 5 HOH   165 565 24  HOH   HOH A . 
E 5 HOH   166 566 142 HOH   HOH A . 
E 5 HOH   167 567 21  HOH   HOH A . 
E 5 HOH   168 568 49  HOH   HOH A . 
E 5 HOH   169 569 225 HOH   HOH A . 
E 5 HOH   170 570 298 HOH   HOH A . 
E 5 HOH   171 571 95  HOH   HOH A . 
E 5 HOH   172 572 19  HOH   HOH A . 
E 5 HOH   173 573 177 HOH   HOH A . 
E 5 HOH   174 574 100 HOH   HOH A . 
E 5 HOH   175 575 172 HOH   HOH A . 
E 5 HOH   176 576 257 HOH   HOH A . 
E 5 HOH   177 577 171 HOH   HOH A . 
E 5 HOH   178 578 78  HOH   HOH A . 
E 5 HOH   179 579 113 HOH   HOH A . 
E 5 HOH   180 580 314 HOH   HOH A . 
E 5 HOH   181 581 77  HOH   HOH A . 
E 5 HOH   182 582 306 HOH   HOH A . 
E 5 HOH   183 583 86  HOH   HOH A . 
E 5 HOH   184 584 105 HOH   HOH A . 
E 5 HOH   185 585 123 HOH   HOH A . 
E 5 HOH   186 586 65  HOH   HOH A . 
E 5 HOH   187 587 88  HOH   HOH A . 
E 5 HOH   188 588 114 HOH   HOH A . 
E 5 HOH   189 589 222 HOH   HOH A . 
E 5 HOH   190 590 296 HOH   HOH A . 
E 5 HOH   191 591 63  HOH   HOH A . 
E 5 HOH   192 592 244 HOH   HOH A . 
E 5 HOH   193 593 274 HOH   HOH A . 
E 5 HOH   194 594 143 HOH   HOH A . 
E 5 HOH   195 595 299 HOH   HOH A . 
E 5 HOH   196 596 187 HOH   HOH A . 
E 5 HOH   197 597 278 HOH   HOH A . 
E 5 HOH   198 598 23  HOH   HOH A . 
E 5 HOH   199 599 155 HOH   HOH A . 
E 5 HOH   200 600 61  HOH   HOH A . 
E 5 HOH   201 601 264 HOH   HOH A . 
E 5 HOH   202 602 173 HOH   HOH A . 
E 5 HOH   203 603 293 HOH   HOH A . 
E 5 HOH   204 604 176 HOH   HOH A . 
E 5 HOH   205 605 329 HOH   HOH A . 
E 5 HOH   206 606 76  HOH   HOH A . 
E 5 HOH   207 607 116 HOH   HOH A . 
E 5 HOH   208 608 26  HOH   HOH A . 
E 5 HOH   209 609 18  HOH   HOH A . 
E 5 HOH   210 610 189 HOH   HOH A . 
E 5 HOH   211 611 166 HOH   HOH A . 
E 5 HOH   212 612 170 HOH   HOH A . 
E 5 HOH   213 613 120 HOH   HOH A . 
E 5 HOH   214 614 210 HOH   HOH A . 
E 5 HOH   215 615 121 HOH   HOH A . 
E 5 HOH   216 616 236 HOH   HOH A . 
E 5 HOH   217 617 83  HOH   HOH A . 
E 5 HOH   218 618 59  HOH   HOH A . 
E 5 HOH   219 619 198 HOH   HOH A . 
E 5 HOH   220 620 36  HOH   HOH A . 
E 5 HOH   221 621 157 HOH   HOH A . 
E 5 HOH   222 622 228 HOH   HOH A . 
E 5 HOH   223 623 334 HOH   HOH A . 
E 5 HOH   224 624 215 HOH   HOH A . 
E 5 HOH   225 625 104 HOH   HOH A . 
E 5 HOH   226 626 39  HOH   HOH A . 
E 5 HOH   227 627 124 HOH   HOH A . 
E 5 HOH   228 628 44  HOH   HOH A . 
E 5 HOH   229 629 161 HOH   HOH A . 
E 5 HOH   230 630 184 HOH   HOH A . 
E 5 HOH   231 631 57  HOH   HOH A . 
E 5 HOH   232 632 250 HOH   HOH A . 
E 5 HOH   233 633 164 HOH   HOH A . 
E 5 HOH   234 634 71  HOH   HOH A . 
E 5 HOH   235 635 224 HOH   HOH A . 
E 5 HOH   236 636 220 HOH   HOH A . 
E 5 HOH   237 637 332 HOH   HOH A . 
E 5 HOH   238 638 240 HOH   HOH A . 
E 5 HOH   239 639 259 HOH   HOH A . 
E 5 HOH   240 640 254 HOH   HOH A . 
E 5 HOH   241 641 335 HOH   HOH A . 
E 5 HOH   242 642 291 HOH   HOH A . 
E 5 HOH   243 643 79  HOH   HOH A . 
E 5 HOH   244 644 290 HOH   HOH A . 
E 5 HOH   245 645 304 HOH   HOH A . 
E 5 HOH   246 646 217 HOH   HOH A . 
E 5 HOH   247 647 202 HOH   HOH A . 
E 5 HOH   248 648 128 HOH   HOH A . 
E 5 HOH   249 649 266 HOH   HOH A . 
E 5 HOH   250 650 316 HOH   HOH A . 
E 5 HOH   251 651 226 HOH   HOH A . 
E 5 HOH   252 652 146 HOH   HOH A . 
E 5 HOH   253 653 320 HOH   HOH A . 
E 5 HOH   254 654 275 HOH   HOH A . 
E 5 HOH   255 655 185 HOH   HOH A . 
E 5 HOH   256 656 346 HOH   HOH A . 
E 5 HOH   257 657 252 HOH   HOH A . 
E 5 HOH   258 658 277 HOH   HOH A . 
E 5 HOH   259 659 276 HOH   HOH A . 
E 5 HOH   260 660 191 HOH   HOH A . 
E 5 HOH   261 661 43  HOH   HOH A . 
E 5 HOH   262 662 324 HOH   HOH A . 
E 5 HOH   263 663 288 HOH   HOH A . 
E 5 HOH   264 664 256 HOH   HOH A . 
E 5 HOH   265 665 309 HOH   HOH A . 
E 5 HOH   266 666 249 HOH   HOH A . 
E 5 HOH   267 667 289 HOH   HOH A . 
E 5 HOH   268 668 261 HOH   HOH A . 
E 5 HOH   269 669 207 HOH   HOH A . 
E 5 HOH   270 670 260 HOH   HOH A . 
E 5 HOH   271 671 154 HOH   HOH A . 
E 5 HOH   272 672 167 HOH   HOH A . 
E 5 HOH   273 673 196 HOH   HOH A . 
E 5 HOH   274 674 265 HOH   HOH A . 
E 5 HOH   275 675 336 HOH   HOH A . 
E 5 HOH   276 676 235 HOH   HOH A . 
E 5 HOH   277 677 227 HOH   HOH A . 
E 5 HOH   278 678 243 HOH   HOH A . 
E 5 HOH   279 679 321 HOH   HOH A . 
E 5 HOH   280 680 150 HOH   HOH A . 
E 5 HOH   281 681 72  HOH   HOH A . 
E 5 HOH   282 682 175 HOH   HOH A . 
E 5 HOH   283 683 262 HOH   HOH A . 
E 5 HOH   284 684 206 HOH   HOH A . 
E 5 HOH   285 685 237 HOH   HOH A . 
E 5 HOH   286 686 292 HOH   HOH A . 
E 5 HOH   287 687 341 HOH   HOH A . 
E 5 HOH   288 688 53  HOH   HOH A . 
E 5 HOH   289 689 286 HOH   HOH A . 
E 5 HOH   290 690 211 HOH   HOH A . 
E 5 HOH   291 691 126 HOH   HOH A . 
E 5 HOH   292 692 287 HOH   HOH A . 
E 5 HOH   293 693 190 HOH   HOH A . 
E 5 HOH   294 694 112 HOH   HOH A . 
E 5 HOH   295 695 322 HOH   HOH A . 
E 5 HOH   296 696 168 HOH   HOH A . 
E 5 HOH   297 697 340 HOH   HOH A . 
E 5 HOH   298 698 345 HOH   HOH A . 
E 5 HOH   299 699 89  HOH   HOH A . 
E 5 HOH   300 700 272 HOH   HOH A . 
E 5 HOH   301 701 281 HOH   HOH A . 
E 5 HOH   302 702 212 HOH   HOH A . 
E 5 HOH   303 703 268 HOH   HOH A . 
E 5 HOH   304 704 169 HOH   HOH A . 
E 5 HOH   305 705 348 HOH   HOH A . 
E 5 HOH   306 706 188 HOH   HOH A . 
E 5 HOH   307 707 270 HOH   HOH A . 
E 5 HOH   308 708 258 HOH   HOH A . 
E 5 HOH   309 709 219 HOH   HOH A . 
E 5 HOH   310 710 326 HOH   HOH A . 
E 5 HOH   311 711 193 HOH   HOH A . 
E 5 HOH   312 712 174 HOH   HOH A . 
E 5 HOH   313 713 182 HOH   HOH A . 
E 5 HOH   314 714 280 HOH   HOH A . 
E 5 HOH   315 715 204 HOH   HOH A . 
E 5 HOH   316 716 285 HOH   HOH A . 
E 5 HOH   317 717 238 HOH   HOH A . 
E 5 HOH   318 718 34  HOH   HOH A . 
E 5 HOH   319 719 223 HOH   HOH A . 
E 5 HOH   320 720 343 HOH   HOH A . 
E 5 HOH   321 721 149 HOH   HOH A . 
E 5 HOH   322 722 81  HOH   HOH A . 
E 5 HOH   323 723 307 HOH   HOH A . 
E 5 HOH   324 724 269 HOH   HOH A . 
E 5 HOH   325 725 239 HOH   HOH A . 
E 5 HOH   326 726 245 HOH   HOH A . 
E 5 HOH   327 727 203 HOH   HOH A . 
E 5 HOH   328 728 241 HOH   HOH A . 
E 5 HOH   329 729 325 HOH   HOH A . 
E 5 HOH   330 730 295 HOH   HOH A . 
E 5 HOH   331 731 218 HOH   HOH A . 
E 5 HOH   332 732 247 HOH   HOH A . 
E 5 HOH   333 733 200 HOH   HOH A . 
E 5 HOH   334 734 163 HOH   HOH A . 
E 5 HOH   335 735 205 HOH   HOH A . 
E 5 HOH   336 736 251 HOH   HOH A . 
E 5 HOH   337 737 233 HOH   HOH A . 
E 5 HOH   338 738 312 HOH   HOH A . 
E 5 HOH   339 739 140 HOH   HOH A . 
E 5 HOH   340 740 294 HOH   HOH A . 
E 5 HOH   341 741 135 HOH   HOH A . 
E 5 HOH   342 742 246 HOH   HOH A . 
E 5 HOH   343 743 148 HOH   HOH A . 
E 5 HOH   344 744 284 HOH   HOH A . 
E 5 HOH   345 745 310 HOH   HOH A . 
E 5 HOH   346 746 323 HOH   HOH A . 
E 5 HOH   347 747 151 HOH   HOH A . 
E 5 HOH   348 748 208 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 45  ? CE ? A LYS 45  CE 
2  1 Y 1 A LYS 45  ? NZ ? A LYS 45  NZ 
3  1 Y 1 A LYS 80  ? CE ? A LYS 80  CE 
4  1 Y 1 A LYS 80  ? NZ ? A LYS 80  NZ 
5  1 Y 1 A LYS 159 ? CD ? A LYS 158 CD 
6  1 Y 1 A LYS 159 ? CE ? A LYS 158 CE 
7  1 Y 1 A LYS 159 ? NZ ? A LYS 158 NZ 
8  1 Y 1 A LYS 261 ? CD ? A LYS 260 CD 
9  1 Y 1 A LYS 261 ? CE ? A LYS 260 CE 
10 1 Y 1 A LYS 261 ? NZ ? A LYS 260 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.22   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        4 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        5 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.510 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FPR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.332 
_cell.length_a_esd                 ? 
_cell.length_b                     41.317 
_cell.length_b_esd                 ? 
_cell.length_c                     72.050 
_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                         9FPR 
_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                   9FPR 
_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             2.03 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.1 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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         2021-12-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976200 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976200 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FPR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.460 
_reflns.d_resolution_low                               40.981 
_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                                     41447 
_reflns.number_obs                                     41447 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.700 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.000 
_reflns.pdbx_netI_over_av_sigmaI                       9.300 
_reflns.pdbx_netI_over_sigmaI                          19.600 
_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                                0.056 
_reflns.pdbx_Rpim_I_all                                0.021 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       288108 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.047 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_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 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_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 
1.460 1.540  ? 1.700  41329 ? ? ? 5955 ? ? ? ? ? ? ? ? ? ? ? 6.900 ? ? 4.600  0.449 0.167 ? 1  1 ? ? ? 97.700 ? 0.389 0.389 ? ? ? 
? ? ? ? ? 
1.540 1.630  ? 2.800  39145 ? ? ? 5648 ? ? ? ? ? ? ? ? ? ? ? 6.900 ? ? 6.900  0.271 0.101 ? 2  1 ? ? ? 98.000 ? 0.235 0.235 ? ? ? 
? ? ? ? ? 
1.630 1.750  ? 4.100  37361 ? ? ? 5353 ? ? ? ? ? ? ? ? ? ? ? 7.000 ? ? 9.700  0.182 0.068 ? 3  1 ? ? ? 98.900 ? 0.156 0.156 ? ? ? 
? ? ? ? ? 
1.750 1.880  ? 6.500  34809 ? ? ? 4992 ? ? ? ? ? ? ? ? ? ? ? 7.000 ? ? 13.800 0.118 0.044 ? 4  1 ? ? ? 98.800 ? 0.100 0.100 ? ? ? 
? ? ? ? ? 
1.880 2.060  ? 9.700  31793 ? ? ? 4583 ? ? ? ? ? ? ? ? ? ? ? 6.900 ? ? 19.800 0.079 0.030 ? 5  1 ? ? ? 98.400 ? 0.066 0.066 ? ? ? 
? ? ? ? ? 
2.060 2.310  ? 13.200 28290 ? ? ? 4165 ? ? ? ? ? ? ? ? ? ? ? 6.800 ? ? 26.000 0.060 0.023 ? 6  1 ? ? ? 98.500 ? 0.048 0.048 ? ? ? 
? ? ? ? ? 
2.310 2.670  ? 15.600 26514 ? ? ? 3744 ? ? ? ? ? ? ? ? ? ? ? 7.100 ? ? 30.900 0.049 0.018 ? 7  1 ? ? ? 99.900 ? 0.040 0.040 ? ? ? 
? ? ? ? ? 
2.670 3.260  ? 16.100 22295 ? ? ? 3167 ? ? ? ? ? ? ? ? ? ? ? 7.000 ? ? 39.000 0.045 0.017 ? 8  1 ? ? ? 99.600 ? 0.036 0.036 ? ? ? 
? ? ? ? ? 
3.260 4.620  ? 17.700 16994 ? ? ? 2453 ? ? ? ? ? ? ? ? ? ? ? 6.900 ? ? 49.500 0.037 0.014 ? 9  1 ? ? ? 99.100 ? 0.031 0.031 ? ? ? 
? ? ? ? ? 
4.620 40.981 ? 17.400 9578  ? ? ? 1387 ? ? ? ? ? ? ? ? ? ? ? 6.900 ? ? 46.900 0.037 0.014 ? 10 1 ? ? ? 99.400 ? 0.031 0.031 ? ? ? 
? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.0800 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.2000 
_refine.aniso_B[2][2]                            0.2100 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            -0.3500 
_refine.B_iso_max                                90.070 
_refine.B_iso_mean                               20.0980 
_refine.B_iso_min                                9.730 
_refine.correlation_coeff_Fo_to_Fc               0.9780 
_refine.correlation_coeff_Fo_to_Fc_free          0.9530 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9FPR 
_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                            1.4600 
_refine.ls_d_res_low                             39.9800 
_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                     37425 
_refine.ls_number_reflns_R_free                  4008 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.3700 
_refine.ls_percent_reflns_R_free                 9.7000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1470 
_refine.ls_R_factor_R_free                       0.2091 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1406 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_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                       0.0850 
_refine.pdbx_overall_ESU_R_Free                  0.0810 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.4600 
_refine_hist.d_res_low                        39.9800 
_refine_hist.number_atoms_solvent             348 
_refine_hist.number_atoms_total               2415 
_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       257 
_refine_hist.pdbx_B_iso_mean_ligand           17.21 
_refine_hist.pdbx_B_iso_mean_solvent          32.31 
_refine_hist.pdbx_number_atoms_protein        2039 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_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' ? 0.014  0.012  2168 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.037  1.649  2952 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.047  5.000  265  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 34.774 23.774 106  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.858 15.000 349  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 22.209 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.155  0.200  262  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.015  0.020  1702 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 4.776  3.000  2168 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 27.204 5.000  205  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 15.313 5.000  2246 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.4600 
_refine_ls_shell.d_res_low                        1.4980 
_refine_ls_shell.number_reflns_all                2988 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             298 
_refine_ls_shell.number_reflns_R_work             2690 
_refine_ls_shell.percent_reflns_obs               97.7400 
_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            0.0000 
_refine_ls_shell.R_factor_R_work                  0.3000 
_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                  0.3480 
# 
_struct.entry_id                     9FPR 
_struct.title                        
'Crystal structure of carbonic anhydrase II with methyl 4-(2-phenylethylsulfanyl)-3-sulfamoyl-benzoate' 
_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        9FPR 
_struct_keywords.text            'DRUG DESIGN, CARBONIC ANHYDRASE, BENZENESULFONAMIDE, LYASE-LYASE INHIBITOR COMPLEX, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9FPR 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 230   ? 
1 MORE         2     ? 
1 'SSA (A^2)'  11420 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 219 ? ARG A 226 ? SER A 220 ARG A 227 1 ? 8 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN    . ZN  ? ? A HIS 94  A ZN    301 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN    . ZN  ? ? A HIS 96  A ZN    301 1_555 ? ? ? ? ? ? ? 2.000 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN    . ZN  ? ? A HIS 119 A ZN    301 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C A1IEN . N10 ? ? A ZN  301 A A1IEN 302 1_555 ? ? ? ? ? ? ? 1.900 ? ? 
# 
_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_555 105.8 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 109.7 ? 
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 97.6  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C A1IEN .   ? A A1IEN 302 ? 1_555 111.8 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C A1IEN .   ? A A1IEN 302 ? 1_555 111.7 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? C A1IEN .   ? A A1IEN 302 ? 1_555 118.7 ? 
# 
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 0.52 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 5.47 
# 
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 ? GLY A 150 ? LEU A 141 GLY A 151 
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  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? GLY A 150 ? LEU A 141 GLY A 151 
AA3 6  ILE A 215 ? SER A 218 ? ILE A 216 SER A 219 
# 
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 ILE A 209 ? O ILE A 210 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 GLY A 150 ? N GLY A 151 O VAL A 217 ? O VAL A 218 
# 
_pdbx_entry_details.entry_id                   9FPR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -141.85 52.62   
2 1 LYS A 76  ? ? -111.16 -73.32  
3 1 LYS A 111 ? ? 73.49   -6.09   
4 1 PHE A 176 ? ? -150.92 69.18   
5 1 ASN A 244 ? ? -98.33  47.43   
6 1 LYS A 252 ? ? 57.71   -136.97 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       748 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.87 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1IEN C13  C  N N 1   
A1IEN C20  C  N N 2   
A1IEN C12  C  N N 3   
A1IEN C16  C  Y N 4   
A1IEN O22  O  N N 5   
A1IEN C23  C  N N 6   
A1IEN O21  O  N N 7   
A1IEN C2   C  Y N 8   
A1IEN C3   C  Y N 9   
A1IEN C4   C  Y N 10  
A1IEN C5   C  Y N 11  
A1IEN C6   C  Y N 12  
A1IEN S7   S  N N 13  
A1IEN O9   O  N N 14  
A1IEN N10  N  N N 15  
A1IEN O8   O  N N 16  
A1IEN C1   C  Y N 17  
A1IEN S11  S  N N 18  
A1IEN C14  C  Y N 19  
A1IEN C18  C  Y N 20  
A1IEN C19  C  Y N 21  
A1IEN C17  C  Y N 22  
A1IEN C15  C  Y N 23  
A1IEN H1   H  N N 24  
A1IEN H2   H  N N 25  
A1IEN H3   H  N N 26  
A1IEN H4   H  N N 27  
A1IEN H5   H  N N 28  
A1IEN H6   H  N N 29  
A1IEN H7   H  N N 30  
A1IEN H8   H  N N 31  
A1IEN H9   H  N N 32  
A1IEN H10  H  N N 33  
A1IEN H11  H  N N 34  
A1IEN H12  H  N N 35  
A1IEN H13  H  N N 36  
A1IEN H14  H  N N 37  
A1IEN H15  H  N N 38  
A1IEN H16  H  N N 39  
A1IEN H17  H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
DMS   S    S  N N 128 
DMS   O    O  N N 129 
DMS   C1   C  N N 130 
DMS   C2   C  N N 131 
DMS   H11  H  N N 132 
DMS   H12  H  N N 133 
DMS   H13  H  N N 134 
DMS   H21  H  N N 135 
DMS   H22  H  N N 136 
DMS   H23  H  N N 137 
GLN   N    N  N N 138 
GLN   CA   C  N S 139 
GLN   C    C  N N 140 
GLN   O    O  N N 141 
GLN   CB   C  N N 142 
GLN   CG   C  N N 143 
GLN   CD   C  N N 144 
GLN   OE1  O  N N 145 
GLN   NE2  N  N N 146 
GLN   OXT  O  N N 147 
GLN   H    H  N N 148 
GLN   H2   H  N N 149 
GLN   HA   H  N N 150 
GLN   HB2  H  N N 151 
GLN   HB3  H  N N 152 
GLN   HG2  H  N N 153 
GLN   HG3  H  N N 154 
GLN   HE21 H  N N 155 
GLN   HE22 H  N N 156 
GLN   HXT  H  N N 157 
GLU   N    N  N N 158 
GLU   CA   C  N S 159 
GLU   C    C  N N 160 
GLU   O    O  N N 161 
GLU   CB   C  N N 162 
GLU   CG   C  N N 163 
GLU   CD   C  N N 164 
GLU   OE1  O  N N 165 
GLU   OE2  O  N N 166 
GLU   OXT  O  N N 167 
GLU   H    H  N N 168 
GLU   H2   H  N N 169 
GLU   HA   H  N N 170 
GLU   HB2  H  N N 171 
GLU   HB3  H  N N 172 
GLU   HG2  H  N N 173 
GLU   HG3  H  N N 174 
GLU   HE2  H  N N 175 
GLU   HXT  H  N N 176 
GLY   N    N  N N 177 
GLY   CA   C  N N 178 
GLY   C    C  N N 179 
GLY   O    O  N N 180 
GLY   OXT  O  N N 181 
GLY   H    H  N N 182 
GLY   H2   H  N N 183 
GLY   HA2  H  N N 184 
GLY   HA3  H  N N 185 
GLY   HXT  H  N N 186 
HIS   N    N  N N 187 
HIS   CA   C  N S 188 
HIS   C    C  N N 189 
HIS   O    O  N N 190 
HIS   CB   C  N N 191 
HIS   CG   C  Y N 192 
HIS   ND1  N  Y N 193 
HIS   CD2  C  Y N 194 
HIS   CE1  C  Y N 195 
HIS   NE2  N  Y N 196 
HIS   OXT  O  N N 197 
HIS   H    H  N N 198 
HIS   H2   H  N N 199 
HIS   HA   H  N N 200 
HIS   HB2  H  N N 201 
HIS   HB3  H  N N 202 
HIS   HD1  H  N N 203 
HIS   HD2  H  N N 204 
HIS   HE1  H  N N 205 
HIS   HE2  H  N N 206 
HIS   HXT  H  N N 207 
HOH   O    O  N N 208 
HOH   H1   H  N N 209 
HOH   H2   H  N N 210 
ILE   N    N  N N 211 
ILE   CA   C  N S 212 
ILE   C    C  N N 213 
ILE   O    O  N N 214 
ILE   CB   C  N S 215 
ILE   CG1  C  N N 216 
ILE   CG2  C  N N 217 
ILE   CD1  C  N N 218 
ILE   OXT  O  N N 219 
ILE   H    H  N N 220 
ILE   H2   H  N N 221 
ILE   HA   H  N N 222 
ILE   HB   H  N N 223 
ILE   HG12 H  N N 224 
ILE   HG13 H  N N 225 
ILE   HG21 H  N N 226 
ILE   HG22 H  N N 227 
ILE   HG23 H  N N 228 
ILE   HD11 H  N N 229 
ILE   HD12 H  N N 230 
ILE   HD13 H  N N 231 
ILE   HXT  H  N N 232 
LEU   N    N  N N 233 
LEU   CA   C  N S 234 
LEU   C    C  N N 235 
LEU   O    O  N N 236 
LEU   CB   C  N N 237 
LEU   CG   C  N N 238 
LEU   CD1  C  N N 239 
LEU   CD2  C  N N 240 
LEU   OXT  O  N N 241 
LEU   H    H  N N 242 
LEU   H2   H  N N 243 
LEU   HA   H  N N 244 
LEU   HB2  H  N N 245 
LEU   HB3  H  N N 246 
LEU   HG   H  N N 247 
LEU   HD11 H  N N 248 
LEU   HD12 H  N N 249 
LEU   HD13 H  N N 250 
LEU   HD21 H  N N 251 
LEU   HD22 H  N N 252 
LEU   HD23 H  N N 253 
LEU   HXT  H  N N 254 
LYS   N    N  N N 255 
LYS   CA   C  N S 256 
LYS   C    C  N N 257 
LYS   O    O  N N 258 
LYS   CB   C  N N 259 
LYS   CG   C  N N 260 
LYS   CD   C  N N 261 
LYS   CE   C  N N 262 
LYS   NZ   N  N N 263 
LYS   OXT  O  N N 264 
LYS   H    H  N N 265 
LYS   H2   H  N N 266 
LYS   HA   H  N N 267 
LYS   HB2  H  N N 268 
LYS   HB3  H  N N 269 
LYS   HG2  H  N N 270 
LYS   HG3  H  N N 271 
LYS   HD2  H  N N 272 
LYS   HD3  H  N N 273 
LYS   HE2  H  N N 274 
LYS   HE3  H  N N 275 
LYS   HZ1  H  N N 276 
LYS   HZ2  H  N N 277 
LYS   HZ3  H  N N 278 
LYS   HXT  H  N N 279 
MET   N    N  N N 280 
MET   CA   C  N S 281 
MET   C    C  N N 282 
MET   O    O  N N 283 
MET   CB   C  N N 284 
MET   CG   C  N N 285 
MET   SD   S  N N 286 
MET   CE   C  N N 287 
MET   OXT  O  N N 288 
MET   H    H  N N 289 
MET   H2   H  N N 290 
MET   HA   H  N N 291 
MET   HB2  H  N N 292 
MET   HB3  H  N N 293 
MET   HG2  H  N N 294 
MET   HG3  H  N N 295 
MET   HE1  H  N N 296 
MET   HE2  H  N N 297 
MET   HE3  H  N N 298 
MET   HXT  H  N N 299 
PHE   N    N  N N 300 
PHE   CA   C  N S 301 
PHE   C    C  N N 302 
PHE   O    O  N N 303 
PHE   CB   C  N N 304 
PHE   CG   C  Y N 305 
PHE   CD1  C  Y N 306 
PHE   CD2  C  Y N 307 
PHE   CE1  C  Y N 308 
PHE   CE2  C  Y N 309 
PHE   CZ   C  Y N 310 
PHE   OXT  O  N N 311 
PHE   H    H  N N 312 
PHE   H2   H  N N 313 
PHE   HA   H  N N 314 
PHE   HB2  H  N N 315 
PHE   HB3  H  N N 316 
PHE   HD1  H  N N 317 
PHE   HD2  H  N N 318 
PHE   HE1  H  N N 319 
PHE   HE2  H  N N 320 
PHE   HZ   H  N N 321 
PHE   HXT  H  N N 322 
PRO   N    N  N N 323 
PRO   CA   C  N S 324 
PRO   C    C  N N 325 
PRO   O    O  N N 326 
PRO   CB   C  N N 327 
PRO   CG   C  N N 328 
PRO   CD   C  N N 329 
PRO   OXT  O  N N 330 
PRO   H    H  N N 331 
PRO   HA   H  N N 332 
PRO   HB2  H  N N 333 
PRO   HB3  H  N N 334 
PRO   HG2  H  N N 335 
PRO   HG3  H  N N 336 
PRO   HD2  H  N N 337 
PRO   HD3  H  N N 338 
PRO   HXT  H  N N 339 
SER   N    N  N N 340 
SER   CA   C  N S 341 
SER   C    C  N N 342 
SER   O    O  N N 343 
SER   CB   C  N N 344 
SER   OG   O  N N 345 
SER   OXT  O  N N 346 
SER   H    H  N N 347 
SER   H2   H  N N 348 
SER   HA   H  N N 349 
SER   HB2  H  N N 350 
SER   HB3  H  N N 351 
SER   HG   H  N N 352 
SER   HXT  H  N N 353 
THR   N    N  N N 354 
THR   CA   C  N S 355 
THR   C    C  N N 356 
THR   O    O  N N 357 
THR   CB   C  N R 358 
THR   OG1  O  N N 359 
THR   CG2  C  N N 360 
THR   OXT  O  N N 361 
THR   H    H  N N 362 
THR   H2   H  N N 363 
THR   HA   H  N N 364 
THR   HB   H  N N 365 
THR   HG1  H  N N 366 
THR   HG21 H  N N 367 
THR   HG22 H  N N 368 
THR   HG23 H  N N 369 
THR   HXT  H  N N 370 
TRP   N    N  N N 371 
TRP   CA   C  N S 372 
TRP   C    C  N N 373 
TRP   O    O  N N 374 
TRP   CB   C  N N 375 
TRP   CG   C  Y N 376 
TRP   CD1  C  Y N 377 
TRP   CD2  C  Y N 378 
TRP   NE1  N  Y N 379 
TRP   CE2  C  Y N 380 
TRP   CE3  C  Y N 381 
TRP   CZ2  C  Y N 382 
TRP   CZ3  C  Y N 383 
TRP   CH2  C  Y N 384 
TRP   OXT  O  N N 385 
TRP   H    H  N N 386 
TRP   H2   H  N N 387 
TRP   HA   H  N N 388 
TRP   HB2  H  N N 389 
TRP   HB3  H  N N 390 
TRP   HD1  H  N N 391 
TRP   HE1  H  N N 392 
TRP   HE3  H  N N 393 
TRP   HZ2  H  N N 394 
TRP   HZ3  H  N N 395 
TRP   HH2  H  N N 396 
TRP   HXT  H  N N 397 
TYR   N    N  N N 398 
TYR   CA   C  N S 399 
TYR   C    C  N N 400 
TYR   O    O  N N 401 
TYR   CB   C  N N 402 
TYR   CG   C  Y N 403 
TYR   CD1  C  Y N 404 
TYR   CD2  C  Y N 405 
TYR   CE1  C  Y N 406 
TYR   CE2  C  Y N 407 
TYR   CZ   C  Y N 408 
TYR   OH   O  N N 409 
TYR   OXT  O  N N 410 
TYR   H    H  N N 411 
TYR   H2   H  N N 412 
TYR   HA   H  N N 413 
TYR   HB2  H  N N 414 
TYR   HB3  H  N N 415 
TYR   HD1  H  N N 416 
TYR   HD2  H  N N 417 
TYR   HE1  H  N N 418 
TYR   HE2  H  N N 419 
TYR   HH   H  N N 420 
TYR   HXT  H  N N 421 
VAL   N    N  N N 422 
VAL   CA   C  N S 423 
VAL   C    C  N N 424 
VAL   O    O  N N 425 
VAL   CB   C  N N 426 
VAL   CG1  C  N N 427 
VAL   CG2  C  N N 428 
VAL   OXT  O  N N 429 
VAL   H    H  N N 430 
VAL   H2   H  N N 431 
VAL   HA   H  N N 432 
VAL   HB   H  N N 433 
VAL   HG11 H  N N 434 
VAL   HG12 H  N N 435 
VAL   HG13 H  N N 436 
VAL   HG21 H  N N 437 
VAL   HG22 H  N N 438 
VAL   HG23 H  N N 439 
VAL   HXT  H  N N 440 
ZN    ZN   ZN N N 441 
# 
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 
A1IEN O21 C20  doub N N 1   
A1IEN C20 O22  sing N N 2   
A1IEN C20 C2   sing N N 3   
A1IEN C23 O22  sing N N 4   
A1IEN C3  C2   doub Y N 5   
A1IEN C3  C4   sing Y N 6   
A1IEN C2  C1   sing Y N 7   
A1IEN C4  C5   doub Y N 8   
A1IEN C19 C18  doub Y N 9   
A1IEN C19 C17  sing Y N 10  
A1IEN C18 C14  sing Y N 11  
A1IEN C17 C16  doub Y N 12  
A1IEN C1  C6   doub Y N 13  
A1IEN C5  C6   sing Y N 14  
A1IEN C5  S11  sing N N 15  
A1IEN C14 C13  sing N N 16  
A1IEN C14 C15  doub Y N 17  
A1IEN C12 C13  sing N N 18  
A1IEN C12 S11  sing N N 19  
A1IEN C6  S7   sing N N 20  
A1IEN C16 C15  sing Y N 21  
A1IEN S7  N10  sing N N 22  
A1IEN S7  O9   doub N N 23  
A1IEN S7  O8   doub N N 24  
A1IEN C13 H1   sing N N 25  
A1IEN C13 H2   sing N N 26  
A1IEN C12 H3   sing N N 27  
A1IEN C12 H4   sing N N 28  
A1IEN C16 H5   sing N N 29  
A1IEN C23 H6   sing N N 30  
A1IEN C23 H7   sing N N 31  
A1IEN C23 H8   sing N N 32  
A1IEN C3  H9   sing N N 33  
A1IEN C4  H10  sing N N 34  
A1IEN N10 H11  sing N N 35  
A1IEN N10 H12  sing N N 36  
A1IEN C1  H13  sing N N 37  
A1IEN C18 H14  sing N N 38  
A1IEN C19 H15  sing N N 39  
A1IEN C17 H16  sing N N 40  
A1IEN C15 H17  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TRP   N   CA   sing N N 356 
TRP   N   H    sing N N 357 
TRP   N   H2   sing N N 358 
TRP   CA  C    sing N N 359 
TRP   CA  CB   sing N N 360 
TRP   CA  HA   sing N N 361 
TRP   C   O    doub N N 362 
TRP   C   OXT  sing N N 363 
TRP   CB  CG   sing N N 364 
TRP   CB  HB2  sing N N 365 
TRP   CB  HB3  sing N N 366 
TRP   CG  CD1  doub Y N 367 
TRP   CG  CD2  sing Y N 368 
TRP   CD1 NE1  sing Y N 369 
TRP   CD1 HD1  sing N N 370 
TRP   CD2 CE2  doub Y N 371 
TRP   CD2 CE3  sing Y N 372 
TRP   NE1 CE2  sing Y N 373 
TRP   NE1 HE1  sing N N 374 
TRP   CE2 CZ2  sing Y N 375 
TRP   CE3 CZ3  doub Y N 376 
TRP   CE3 HE3  sing N N 377 
TRP   CZ2 CH2  doub Y N 378 
TRP   CZ2 HZ2  sing N N 379 
TRP   CZ3 CH2  sing Y N 380 
TRP   CZ3 HZ3  sing N N 381 
TRP   CH2 HH2  sing N N 382 
TRP   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4HT0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FPR 
_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]   0.023623 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006115 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024203 
_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]   0.014337 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS   A 1 4   ? 30.036  2.433   7.625   1.00 31.64 ? 4   HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 4   ? 31.016  1.628   8.428   1.00 32.42 ? 4   HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 4   ? 30.296  0.592   9.302   1.00 25.80 ? 4   HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 4   ? 30.486  -0.605  9.132   1.00 27.27 ? 4   HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 4   ? 31.833  2.537   9.330   1.00 39.39 ? 4   HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 4   ? 32.859  1.816   10.151  1.00 40.64 ? 4   HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 4   ? 32.794  1.761   11.557  1.00 42.46 ? 4   HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 4   ? 33.966  1.107   9.789   1.00 48.38 ? 4   HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 4   ? 33.819  1.079   12.026  1.00 43.42 ? 4   HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 4   ? 34.562  0.654   10.958  1.00 59.76 ? 4   HIS   A NE2 1 
ATOM   11   N  N   . TRP   A 1 5   ? 29.507  1.073   10.278  1.00 24.35 ? 5   TRP   A N   1 
ATOM   12   C  CA  . TRP   A 1 5   ? 28.805  0.190   11.206  1.00 17.44 ? 5   TRP   A CA  1 
ATOM   13   C  C   . TRP   A 1 5   ? 27.715  -0.563  10.478  1.00 17.44 ? 5   TRP   A C   1 
ATOM   14   O  O   . TRP   A 1 5   ? 27.207  -0.122  9.452   1.00 20.39 ? 5   TRP   A O   1 
ATOM   15   C  CB  . TRP   A 1 5   ? 28.206  0.937   12.396  1.00 18.88 ? 5   TRP   A CB  1 
ATOM   16   C  CG  . TRP   A 1 5   ? 27.044  1.817   12.044  1.00 18.70 ? 5   TRP   A CG  1 
ATOM   17   C  CD1 . TRP   A 1 5   ? 27.080  3.143   11.726  1.00 19.20 ? 5   TRP   A CD1 1 
ATOM   18   C  CD2 . TRP   A 1 5   ? 25.669  1.446   12.018  1.00 19.21 ? 5   TRP   A CD2 1 
ATOM   19   N  NE1 . TRP   A 1 5   ? 25.816  3.613   11.471  1.00 20.52 ? 5   TRP   A NE1 1 
ATOM   20   C  CE2 . TRP   A 1 5   ? 24.930  2.593   11.635  1.00 18.46 ? 5   TRP   A CE2 1 
ATOM   21   C  CE3 . TRP   A 1 5   ? 24.987  0.234   12.210  1.00 17.38 ? 5   TRP   A CE3 1 
ATOM   22   C  CZ2 . TRP   A 1 5   ? 23.542  2.591   11.509  1.00 19.12 ? 5   TRP   A CZ2 1 
ATOM   23   C  CZ3 . TRP   A 1 5   ? 23.613  0.231   12.049  1.00 20.03 ? 5   TRP   A CZ3 1 
ATOM   24   C  CH2 . TRP   A 1 5   ? 22.902  1.385   11.689  1.00 19.30 ? 5   TRP   A CH2 1 
ATOM   25   N  N   . GLY   A 1 6   ? 27.483  -1.768  10.963  1.00 16.00 ? 6   GLY   A N   1 
ATOM   26   C  CA  . GLY   A 1 6   ? 26.398  -2.544  10.383  1.00 17.20 ? 6   GLY   A CA  1 
ATOM   27   C  C   . GLY   A 1 6   ? 26.082  -3.747  11.273  1.00 14.34 ? 6   GLY   A C   1 
ATOM   28   O  O   . GLY   A 1 6   ? 26.083  -3.615  12.490  1.00 15.34 ? 6   GLY   A O   1 
ATOM   29   N  N   . TYR   A 1 7   ? 25.790  -4.891  10.628  1.00 20.43 ? 7   TYR   A N   1 
ATOM   30   C  CA  . TYR   A 1 7   ? 25.370  -6.092  11.325  1.00 19.29 ? 7   TYR   A CA  1 
ATOM   31   C  C   . TYR   A 1 7   ? 26.080  -7.262  10.655  1.00 27.71 ? 7   TYR   A C   1 
ATOM   32   O  O   . TYR   A 1 7   ? 25.545  -8.397  10.620  1.00 32.21 ? 7   TYR   A O   1 
ATOM   33   C  CB  . TYR   A 1 7   ? 23.850  -6.349  11.239  1.00 19.07 ? 7   TYR   A CB  1 
ATOM   34   C  CG  . TYR   A 1 7   ? 22.987  -5.245  11.808  1.00 14.47 ? 7   TYR   A CG  1 
ATOM   35   C  CD1 . TYR   A 1 7   ? 22.616  -4.182  10.992  1.00 14.90 ? 7   TYR   A CD1 1 
ATOM   36   C  CD2 . TYR   A 1 7   ? 22.626  -5.224  13.138  1.00 15.84 ? 7   TYR   A CD2 1 
ATOM   37   C  CE1 . TYR   A 1 7   ? 21.821  -3.150  11.469  1.00 14.84 ? 7   TYR   A CE1 1 
ATOM   38   C  CE2 . TYR   A 1 7   ? 21.877  -4.159  13.643  1.00 14.75 ? 7   TYR   A CE2 1 
ATOM   39   C  CZ  . TYR   A 1 7   ? 21.476  -3.133  12.808  1.00 13.99 ? 7   TYR   A CZ  1 
ATOM   40   O  OH  . TYR   A 1 7   ? 20.696  -2.136  13.289  1.00 14.29 ? 7   TYR   A OH  1 
ATOM   41   N  N   . GLY   A 1 8   ? 27.233  -6.965  10.052  1.00 23.52 ? 8   GLY   A N   1 
ATOM   42   C  CA  . GLY   A 1 8   ? 27.975  -7.992  9.325   1.00 25.66 ? 8   GLY   A CA  1 
ATOM   43   C  C   . GLY   A 1 8   ? 28.890  -8.762  10.266  1.00 24.07 ? 8   GLY   A C   1 
ATOM   44   O  O   . GLY   A 1 8   ? 28.781  -8.619  11.487  1.00 26.11 ? 8   GLY   A O   1 
ATOM   45   N  N   . LYS   A 1 9   ? 29.875  -9.492  9.686   1.00 26.05 ? 9   LYS   A N   1 
ATOM   46   C  CA  . LYS   A 1 9   ? 30.732  -10.321 10.523  1.00 27.82 ? 9   LYS   A CA  1 
ATOM   47   C  C   . LYS   A 1 9   ? 31.770  -9.514  11.309  1.00 23.90 ? 9   LYS   A C   1 
ATOM   48   O  O   . LYS   A 1 9   ? 32.326  -10.086 12.227  1.00 29.46 ? 9   LYS   A O   1 
ATOM   49   C  CB  . LYS   A 1 9   ? 31.337  -11.501 9.740   1.00 33.93 ? 9   LYS   A CB  1 
ATOM   50   C  CG  . LYS   A 1 9   ? 30.354  -12.634 9.442   1.00 42.23 ? 9   LYS   A CG  1 
ATOM   51   C  CD  . LYS   A 1 9   ? 30.961  -13.837 8.719   1.00 46.63 ? 9   LYS   A CD  1 
ATOM   52   C  CE  . LYS   A 1 9   ? 29.934  -14.741 8.058   1.00 45.86 ? 9   LYS   A CE  1 
ATOM   53   N  NZ  . LYS   A 1 9   ? 29.440  -14.174 6.781   1.00 46.18 ? 9   LYS   A NZ  1 
ATOM   54   N  N   . HIS   A 1 10  ? 32.039  -8.228  10.925  1.00 21.05 ? 10  HIS   A N   1 
ATOM   55   C  CA  . HIS   A 1 10  ? 33.159  -7.417  11.390  1.00 19.39 ? 10  HIS   A CA  1 
ATOM   56   C  C   . HIS   A 1 10  ? 32.770  -5.998  11.829  1.00 19.58 ? 10  HIS   A C   1 
ATOM   57   O  O   . HIS   A 1 10  ? 33.652  -5.237  12.261  1.00 24.80 ? 10  HIS   A O   1 
ATOM   58   C  CB  . HIS   A 1 10  ? 34.236  -7.233  10.273  1.00 23.21 ? 10  HIS   A CB  1 
ATOM   59   C  CG  . HIS   A 1 10  ? 34.780  -8.549  9.818   1.00 26.55 ? 10  HIS   A CG  1 
ATOM   60   N  ND1 . HIS   A 1 10  ? 35.780  -9.208  10.535  1.00 30.64 ? 10  HIS   A ND1 1 
ATOM   61   C  CD2 . HIS   A 1 10  ? 34.449  -9.352  8.764   1.00 30.13 ? 10  HIS   A CD2 1 
ATOM   62   C  CE1 . HIS   A 1 10  ? 36.046  -10.369 9.946   1.00 26.29 ? 10  HIS   A CE1 1 
ATOM   63   N  NE2 . HIS   A 1 10  ? 35.235  -10.487 8.837   1.00 30.49 ? 10  HIS   A NE2 1 
ATOM   64   N  N   . ASN   A 1 11  ? 31.484  -5.635  11.689  1.00 18.53 ? 11  ASN   A N   1 
ATOM   65   C  CA  . ASN   A 1 11  ? 31.107  -4.260  11.978  1.00 18.73 ? 11  ASN   A CA  1 
ATOM   66   C  C   . ASN   A 1 11  ? 29.822  -4.228  12.801  1.00 17.72 ? 11  ASN   A C   1 
ATOM   67   O  O   . ASN   A 1 11  ? 29.138  -3.183  12.853  1.00 19.74 ? 11  ASN   A O   1 
ATOM   68   C  CB  . ASN   A 1 11  ? 30.979  -3.480  10.672  1.00 17.71 ? 11  ASN   A CB  1 
ATOM   69   C  CG  . ASN   A 1 11  ? 29.828  -4.020  9.855   1.00 19.94 ? 11  ASN   A CG  1 
ATOM   70   O  OD1 . ASN   A 1 11  ? 29.305  -5.067  10.213  1.00 20.88 ? 11  ASN   A OD1 1 
ATOM   71   N  ND2 . ASN   A 1 11  ? 29.500  -3.361  8.739   1.00 21.32 ? 11  ASN   A ND2 1 
ATOM   72   N  N   . GLY   A 1 12  ? 29.508  -5.374  13.453  1.00 19.16 ? 12  GLY   A N   1 
ATOM   73   C  CA  . GLY   A 1 12  ? 28.225  -5.509  14.105  1.00 17.27 ? 12  GLY   A CA  1 
ATOM   74   C  C   . GLY   A 1 12  ? 28.159  -4.838  15.467  1.00 18.65 ? 12  GLY   A C   1 
ATOM   75   O  O   . GLY   A 1 12  ? 29.098  -4.144  15.903  1.00 16.34 ? 12  GLY   A O   1 
ATOM   76   N  N   . PRO   A 1 13  ? 27.064  -5.076  16.210  1.00 14.30 ? 13  PRO   A N   1 
ATOM   77   C  CA  . PRO   A 1 13  ? 26.834  -4.389  17.485  1.00 17.37 ? 13  PRO   A CA  1 
ATOM   78   C  C   . PRO   A 1 13  ? 27.983  -4.362  18.481  1.00 15.59 ? 13  PRO   A C   1 
ATOM   79   O  O   . PRO   A 1 13  ? 28.124  -3.382  19.205  1.00 17.59 ? 13  PRO   A O   1 
ATOM   80   C  CB  . PRO   A 1 13  ? 25.530  -5.052  18.009  1.00 17.65 ? 13  PRO   A CB  1 
ATOM   81   C  CG  . PRO   A 1 13  ? 24.817  -5.426  16.736  1.00 17.49 ? 13  PRO   A CG  1 
ATOM   82   C  CD  . PRO   A 1 13  ? 25.897  -5.882  15.779  1.00 16.45 ? 13  PRO   A CD  1 
ATOM   83   N  N   . GLU   A 1 14  ? 28.763  -5.461  18.560  1.00 16.42 ? 14  GLU   A N   1 
ATOM   84   C  CA  . GLU   A 1 14  ? 29.850  -5.514  19.527  1.00 17.13 ? 14  GLU   A CA  1 
ATOM   85   C  C   . GLU   A 1 14  ? 30.988  -4.550  19.171  1.00 14.62 ? 14  GLU   A C   1 
ATOM   86   O  O   . GLU   A 1 14  ? 31.882  -4.348  20.006  1.00 17.65 ? 14  GLU   A O   1 
ATOM   87   C  CB  . GLU   A 1 14  ? 30.368  -6.950  19.647  1.00 21.06 ? 14  GLU   A CB  1 
ATOM   88   C  CG  . GLU   A 1 14  ? 30.954  -7.497  18.337  1.00 22.73 ? 14  GLU   A CG  1 
ATOM   89   C  CD  . GLU   A 1 14  ? 30.162  -8.084  17.150  1.00 24.17 ? 14  GLU   A CD  1 
ATOM   90   O  OE1 . GLU   A 1 14  ? 28.988  -7.702  16.978  1.00 21.02 ? 14  GLU   A OE1 1 
ATOM   91   O  OE2 . GLU   A 1 14  ? 30.731  -8.915  16.415  1.00 23.12 ? 14  GLU   A OE2 1 
ATOM   92   N  N   . HIS   A 1 15  ? 30.980  -3.964  17.966  1.00 15.90 ? 15  HIS   A N   1 
ATOM   93   C  CA  . HIS   A 1 15  ? 32.018  -3.016  17.543  1.00 15.05 ? 15  HIS   A CA  1 
ATOM   94   C  C   . HIS   A 1 15  ? 31.595  -1.553  17.711  1.00 17.13 ? 15  HIS   A C   1 
ATOM   95   O  O   . HIS   A 1 15  ? 32.452  -0.655  17.594  1.00 16.79 ? 15  HIS   A O   1 
ATOM   96   C  CB  . HIS   A 1 15  ? 32.428  -3.258  16.062  1.00 14.94 ? 15  HIS   A CB  1 
ATOM   97   C  CG  . HIS   A 1 15  ? 33.054  -4.606  15.860  1.00 16.41 ? 15  HIS   A CG  1 
ATOM   98   N  ND1 . HIS   A 1 15  ? 34.392  -4.807  16.030  1.00 20.77 ? 15  HIS   A ND1 1 
ATOM   99   C  CD2 . HIS   A 1 15  ? 32.538  -5.798  15.458  1.00 17.75 ? 15  HIS   A CD2 1 
ATOM   100  C  CE1 . HIS   A 1 15  ? 34.663  -6.112  15.841  1.00 23.83 ? 15  HIS   A CE1 1 
ATOM   101  N  NE2 . HIS   A 1 15  ? 33.546  -6.731  15.459  1.00 21.73 ? 15  HIS   A NE2 1 
ATOM   102  N  N   . TRP   A 1 16  ? 30.298  -1.308  17.934  1.00 13.96 ? 16  TRP   A N   1 
ATOM   103  C  CA  . TRP   A 1 16  ? 29.747  0.026   17.755  1.00 14.44 ? 16  TRP   A CA  1 
ATOM   104  C  C   . TRP   A 1 16  ? 30.374  1.007   18.755  1.00 14.27 ? 16  TRP   A C   1 
ATOM   105  O  O   . TRP   A 1 16  ? 30.536  2.209   18.453  1.00 15.78 ? 16  TRP   A O   1 
ATOM   106  C  CB  . TRP   A 1 16  ? 28.220  -0.001  17.879  1.00 13.52 ? 16  TRP   A CB  1 
ATOM   107  C  CG  . TRP   A 1 16  ? 27.568  -0.734  16.756  1.00 14.04 ? 16  TRP   A CG  1 
ATOM   108  C  CD1 . TRP   A 1 16  ? 28.077  -1.149  15.555  1.00 13.59 ? 16  TRP   A CD1 1 
ATOM   109  C  CD2 . TRP   A 1 16  ? 26.145  -0.993  16.676  1.00 13.98 ? 16  TRP   A CD2 1 
ATOM   110  N  NE1 . TRP   A 1 16  ? 27.099  -1.789  14.795  1.00 13.98 ? 16  TRP   A NE1 1 
ATOM   111  C  CE2 . TRP   A 1 16  ? 25.900  -1.648  15.441  1.00 14.40 ? 16  TRP   A CE2 1 
ATOM   112  C  CE3 . TRP   A 1 16  ? 25.089  -0.725  17.554  1.00 13.27 ? 16  TRP   A CE3 1 
ATOM   113  C  CZ2 . TRP   A 1 16  ? 24.605  -2.064  15.072  1.00 13.13 ? 16  TRP   A CZ2 1 
ATOM   114  C  CZ3 . TRP   A 1 16  ? 23.829  -1.150  17.216  1.00 15.75 ? 16  TRP   A CZ3 1 
ATOM   115  C  CH2 . TRP   A 1 16  ? 23.595  -1.743  15.967  1.00 13.94 ? 16  TRP   A CH2 1 
ATOM   116  N  N   . HIS   A 1 17  ? 30.713  0.499   19.948  1.00 15.79 ? 17  HIS   A N   1 
ATOM   117  C  CA  . HIS   A 1 17  ? 31.214  1.315   21.030  1.00 15.85 ? 17  HIS   A CA  1 
ATOM   118  C  C   . HIS   A 1 17  ? 32.472  2.099   20.614  1.00 16.89 ? 17  HIS   A C   1 
ATOM   119  O  O   . HIS   A 1 17  ? 32.708  3.176   21.148  1.00 16.40 ? 17  HIS   A O   1 
ATOM   120  C  CB  . HIS   A 1 17  ? 31.449  0.524   22.322  1.00 16.23 ? 17  HIS   A CB  1 
ATOM   121  C  CG  . HIS   A 1 17  ? 32.631  -0.370  22.170  1.00 14.52 ? 17  HIS   A CG  1 
ATOM   122  N  ND1 . HIS   A 1 17  ? 33.886  -0.020  22.675  1.00 18.94 ? 17  HIS   A ND1 1 
ATOM   123  C  CD2 . HIS   A 1 17  ? 32.805  -1.552  21.521  1.00 17.73 ? 17  HIS   A CD2 1 
ATOM   124  C  CE1 . HIS   A 1 17  ? 34.757  -0.974  22.369  1.00 21.26 ? 17  HIS   A CE1 1 
ATOM   125  N  NE2 . HIS   A 1 17  ? 34.136  -1.911  21.670  1.00 20.71 ? 17  HIS   A NE2 1 
ATOM   126  N  N   . LYS   A 1 18  ? 33.221  1.567   19.662  1.00 15.45 ? 18  LYS   A N   1 
ATOM   127  C  CA  . LYS   A 1 18  ? 34.443  2.239   19.221  1.00 18.15 ? 18  LYS   A CA  1 
ATOM   128  C  C   . LYS   A 1 18  ? 34.168  3.584   18.526  1.00 18.52 ? 18  LYS   A C   1 
ATOM   129  O  O   . LYS   A 1 18  ? 34.918  4.542   18.761  1.00 23.21 ? 18  LYS   A O   1 
ATOM   130  C  CB  . LYS   A 1 18  ? 35.325  1.339   18.346  1.00 17.86 ? 18  LYS   A CB  1 
ATOM   131  C  CG  . LYS   A 1 18  ? 35.922  0.134   19.063  1.00 19.62 ? 18  LYS   A CG  1 
ATOM   132  C  CD  . LYS   A 1 18  ? 36.636  -0.819  18.103  1.00 19.64 ? 18  LYS   A CD  1 
ATOM   133  C  CE  . LYS   A 1 18  ? 35.663  -1.832  17.548  1.00 16.72 ? 18  LYS   A CE  1 
ATOM   134  N  NZ  . LYS   A 1 18  ? 36.295  -2.658  16.494  1.00 19.08 ? 18  LYS   A NZ  1 
ATOM   135  N  N   . ASP   A 1 19  ? 33.094  3.694   17.732  1.00 20.04 ? 19  ASP   A N   1 
ATOM   136  C  CA  . ASP   A 1 19  ? 32.745  5.004   17.182  1.00 18.68 ? 19  ASP   A CA  1 
ATOM   137  C  C   . ASP   A 1 19  ? 31.682  5.747   18.000  1.00 17.61 ? 19  ASP   A C   1 
ATOM   138  O  O   . ASP   A 1 19  ? 31.585  6.970   17.893  1.00 19.55 ? 19  ASP   A O   1 
ATOM   139  C  CB  . ASP   A 1 19  ? 32.218  4.878   15.763  1.00 22.50 ? 19  ASP   A CB  1 
ATOM   140  C  CG  . ASP   A 1 19  ? 33.341  4.594   14.797  1.00 30.42 ? 19  ASP   A CG  1 
ATOM   141  O  OD1 . ASP   A 1 19  ? 34.280  5.428   14.738  1.00 34.88 ? 19  ASP   A OD1 1 
ATOM   142  O  OD2 . ASP   A 1 19  ? 33.344  3.477   14.228  1.00 49.59 ? 19  ASP   A OD2 1 
ATOM   143  N  N   . PHE   A 1 20  ? 30.880  5.000   18.774  1.00 17.22 ? 20  PHE   A N   1 
ATOM   144  C  CA  . PHE   A 1 20  ? 29.806  5.582   19.561  1.00 15.07 ? 20  PHE   A CA  1 
ATOM   145  C  C   . PHE   A 1 20  ? 29.908  5.101   21.025  1.00 14.28 ? 20  PHE   A C   1 
ATOM   146  O  O   . PHE   A 1 20  ? 29.266  4.125   21.436  1.00 15.11 ? 20  PHE   A O   1 
ATOM   147  C  CB  . PHE   A 1 20  ? 28.472  5.166   18.941  1.00 15.19 ? 20  PHE   A CB  1 
ATOM   148  C  CG  . PHE   A 1 20  ? 28.407  5.542   17.489  1.00 16.22 ? 20  PHE   A CG  1 
ATOM   149  C  CD1 . PHE   A 1 20  ? 28.000  6.823   17.074  1.00 18.13 ? 20  PHE   A CD1 1 
ATOM   150  C  CD2 . PHE   A 1 20  ? 28.793  4.614   16.537  1.00 19.05 ? 20  PHE   A CD2 1 
ATOM   151  C  CE1 . PHE   A 1 20  ? 27.968  7.120   15.714  1.00 18.40 ? 20  PHE   A CE1 1 
ATOM   152  C  CE2 . PHE   A 1 20  ? 28.799  4.909   15.188  1.00 18.84 ? 20  PHE   A CE2 1 
ATOM   153  C  CZ  . PHE   A 1 20  ? 28.396  6.172   14.776  1.00 18.97 ? 20  PHE   A CZ  1 
ATOM   154  N  N   A PRO   A 1 21  ? 30.798  5.715   21.841  0.50 15.73 ? 21  PRO   A N   1 
ATOM   155  N  N   B PRO   A 1 21  ? 30.770  5.697   21.870  0.50 15.96 ? 21  PRO   A N   1 
ATOM   156  C  CA  A PRO   A 1 21  ? 31.024  5.304   23.239  0.50 16.46 ? 21  PRO   A CA  1 
ATOM   157  C  CA  B PRO   A 1 21  ? 30.999  5.121   23.197  0.50 17.15 ? 21  PRO   A CA  1 
ATOM   158  C  C   A PRO   A 1 21  ? 29.804  5.191   24.161  0.50 16.38 ? 21  PRO   A C   1 
ATOM   159  C  C   B PRO   A 1 21  ? 29.725  4.985   24.025  0.50 15.50 ? 21  PRO   A C   1 
ATOM   160  O  O   A PRO   A 1 21  ? 29.837  4.546   25.207  0.50 14.17 ? 21  PRO   A O   1 
ATOM   161  O  O   B PRO   A 1 21  ? 29.662  4.085   24.854  0.50 15.11 ? 21  PRO   A O   1 
ATOM   162  C  CB  A PRO   A 1 21  ? 32.023  6.366   23.742  0.50 16.77 ? 21  PRO   A CB  1 
ATOM   163  C  CB  B PRO   A 1 21  ? 32.076  6.026   23.806  0.50 16.45 ? 21  PRO   A CB  1 
ATOM   164  C  CG  A PRO   A 1 21  ? 31.926  7.470   22.708  0.50 15.29 ? 21  PRO   A CG  1 
ATOM   165  C  CG  B PRO   A 1 21  ? 32.759  6.553   22.581  0.50 16.79 ? 21  PRO   A CG  1 
ATOM   166  C  CD  A PRO   A 1 21  ? 31.757  6.744   21.396  0.50 16.16 ? 21  PRO   A CD  1 
ATOM   167  C  CD  B PRO   A 1 21  ? 31.675  6.817   21.560  0.50 17.52 ? 21  PRO   A CD  1 
ATOM   168  N  N   . ILE   A 1 22  ? 28.709  5.848   23.763  1.00 14.45 ? 22  ILE   A N   1 
ATOM   169  C  CA  . ILE   A 1 22  ? 27.420  5.757   24.452  1.00 15.75 ? 22  ILE   A CA  1 
ATOM   170  C  C   . ILE   A 1 22  ? 26.828  4.359   24.311  1.00 15.80 ? 22  ILE   A C   1 
ATOM   171  O  O   . ILE   A 1 22  ? 25.969  4.039   25.123  1.00 14.35 ? 22  ILE   A O   1 
ATOM   172  C  CB  . ILE   A 1 22  ? 26.439  6.843   23.981  1.00 15.70 ? 22  ILE   A CB  1 
ATOM   173  C  CG1 . ILE   A 1 22  ? 25.412  7.182   25.065  1.00 14.76 ? 22  ILE   A CG1 1 
ATOM   174  C  CG2 . ILE   A 1 22  ? 25.871  6.478   22.605  1.00 16.09 ? 22  ILE   A CG2 1 
ATOM   175  C  CD1 . ILE   A 1 22  ? 24.471  8.300   24.712  1.00 18.47 ? 22  ILE   A CD1 1 
ATOM   176  N  N   . ALA   A 1 23  ? 27.348  3.542   23.380  1.00 14.45 ? 23  ALA   A N   1 
ATOM   177  C  CA  . ALA   A 1 23  ? 26.891  2.155   23.285  1.00 15.42 ? 23  ALA   A CA  1 
ATOM   178  C  C   . ALA   A 1 23  ? 26.994  1.442   24.648  1.00 15.95 ? 23  ALA   A C   1 
ATOM   179  O  O   . ALA   A 1 23  ? 26.311  0.432   24.866  1.00 14.80 ? 23  ALA   A O   1 
ATOM   180  C  CB  . ALA   A 1 23  ? 27.714  1.421   22.228  1.00 14.61 ? 23  ALA   A CB  1 
ATOM   181  N  N   . LYS   A 1 24  ? 27.921  1.854   25.523  1.00 16.48 ? 24  LYS   A N   1 
ATOM   182  C  CA  . LYS   A 1 24  ? 28.060  1.246   26.853  1.00 16.38 ? 24  LYS   A CA  1 
ATOM   183  C  C   . LYS   A 1 24  ? 27.474  2.138   27.945  1.00 17.27 ? 24  LYS   A C   1 
ATOM   184  O  O   . LYS   A 1 24  ? 27.856  2.036   29.125  1.00 18.49 ? 24  LYS   A O   1 
ATOM   185  C  CB  . LYS   A 1 24  ? 29.547  1.000   27.132  1.00 18.26 ? 24  LYS   A CB  1 
ATOM   186  C  CG  . LYS   A 1 24  ? 30.217  -0.047  26.233  1.00 20.60 ? 24  LYS   A CG  1 
ATOM   187  C  CD  . LYS   A 1 24  ? 31.683  -0.230  26.594  1.00 24.51 ? 24  LYS   A CD  1 
ATOM   188  C  CE  . LYS   A 1 24  ? 32.459  -1.076  25.625  1.00 29.25 ? 24  LYS   A CE  1 
ATOM   189  N  NZ  . LYS   A 1 24  ? 32.193  -2.495  25.911  1.00 33.86 ? 24  LYS   A NZ  1 
ATOM   190  N  N   . GLY   A 1 25  ? 26.475  2.955   27.557  1.00 15.41 ? 25  GLY   A N   1 
ATOM   191  C  CA  . GLY   A 1 25  ? 25.902  3.900   28.501  1.00 15.86 ? 25  GLY   A CA  1 
ATOM   192  C  C   . GLY   A 1 25  ? 24.931  3.295   29.514  1.00 13.84 ? 25  GLY   A C   1 
ATOM   193  O  O   . GLY   A 1 25  ? 24.752  2.055   29.587  1.00 16.19 ? 25  GLY   A O   1 
ATOM   194  N  N   . GLU   A 1 26  ? 24.270  4.189   30.244  1.00 17.44 ? 26  GLU   A N   1 
ATOM   195  C  CA  . GLU   A 1 26  ? 23.411  3.830   31.366  1.00 16.71 ? 26  GLU   A CA  1 
ATOM   196  C  C   . GLU   A 1 26  ? 21.981  3.514   30.975  1.00 15.99 ? 26  GLU   A C   1 
ATOM   197  O  O   . GLU   A 1 26  ? 21.259  2.936   31.812  1.00 17.33 ? 26  GLU   A O   1 
ATOM   198  C  CB  . GLU   A 1 26  ? 23.405  4.935   32.419  1.00 20.45 ? 26  GLU   A CB  1 
ATOM   199  C  CG  . GLU   A 1 26  ? 24.794  5.084   33.004  1.00 25.15 ? 26  GLU   A CG  1 
ATOM   200  C  CD  . GLU   A 1 26  ? 25.402  3.826   33.645  1.00 28.89 ? 26  GLU   A CD  1 
ATOM   201  O  OE1 . GLU   A 1 26  ? 24.752  3.214   34.568  1.00 39.91 ? 26  GLU   A OE1 1 
ATOM   202  O  OE2 . GLU   A 1 26  ? 26.514  3.434   33.224  1.00 34.75 ? 26  GLU   A OE2 1 
ATOM   203  N  N   . ARG   A 1 27  ? 21.588  3.858   29.739  1.00 13.01 ? 27  ARG   A N   1 
ATOM   204  C  CA  . ARG   A 1 27  ? 20.166  3.666   29.404  1.00 14.48 ? 27  ARG   A CA  1 
ATOM   205  C  C   . ARG   A 1 27  ? 20.054  3.176   27.950  1.00 12.57 ? 27  ARG   A C   1 
ATOM   206  O  O   . ARG   A 1 27  ? 19.356  3.758   27.099  1.00 13.27 ? 27  ARG   A O   1 
ATOM   207  C  CB  . ARG   A 1 27  ? 19.267  4.856   29.777  1.00 18.49 ? 27  ARG   A CB  1 
ATOM   208  C  CG  . ARG   A 1 27  ? 19.607  6.166   29.090  1.00 21.70 ? 27  ARG   A CG  1 
ATOM   209  C  CD  . ARG   A 1 27  ? 18.547  7.252   29.285  1.00 24.14 ? 27  ARG   A CD  1 
ATOM   210  N  NE  . ARG   A 1 27  ? 17.367  7.188   28.376  1.00 20.02 ? 27  ARG   A NE  1 
ATOM   211  C  CZ  . ARG   A 1 27  ? 16.453  8.136   28.354  1.00 19.14 ? 27  ARG   A CZ  1 
ATOM   212  N  NH1 . ARG   A 1 27  ? 16.538  9.172   29.188  1.00 21.49 ? 27  ARG   A NH1 1 
ATOM   213  N  NH2 . ARG   A 1 27  ? 15.444  8.046   27.525  1.00 23.13 ? 27  ARG   A NH2 1 
ATOM   214  N  N   . GLN   A 1 28  ? 20.801  2.092   27.639  1.00 13.38 ? 28  GLN   A N   1 
ATOM   215  C  CA  . GLN   A 1 28  ? 20.830  1.529   26.287  1.00 11.92 ? 28  GLN   A CA  1 
ATOM   216  C  C   . GLN   A 1 28  ? 19.655  0.586   26.001  1.00 10.51 ? 28  GLN   A C   1 
ATOM   217  O  O   . GLN   A 1 28  ? 19.169  -0.080  26.909  1.00 12.86 ? 28  GLN   A O   1 
ATOM   218  C  CB  . GLN   A 1 28  ? 22.194  0.894   25.989  1.00 11.56 ? 28  GLN   A CB  1 
ATOM   219  C  CG  . GLN   A 1 28  ? 23.274  1.991   25.926  1.00 12.54 ? 28  GLN   A CG  1 
ATOM   220  C  CD  . GLN   A 1 28  ? 23.123  2.737   24.610  1.00 11.07 ? 28  GLN   A CD  1 
ATOM   221  O  OE1 . GLN   A 1 28  ? 23.377  2.220   23.510  1.00 13.46 ? 28  GLN   A OE1 1 
ATOM   222  N  NE2 . GLN   A 1 28  ? 22.817  4.075   24.693  1.00 10.32 ? 28  GLN   A NE2 1 
ATOM   223  N  N   . SER   A 1 29  ? 19.311  0.550   24.707  1.00 10.58 ? 29  SER   A N   1 
ATOM   224  C  CA  . SER   A 1 29  ? 18.238  -0.328  24.257  1.00 10.56 ? 29  SER   A CA  1 
ATOM   225  C  C   . SER   A 1 29  ? 18.736  -1.226  23.143  1.00 13.85 ? 29  SER   A C   1 
ATOM   226  O  O   . SER   A 1 29  ? 19.660  -0.895  22.384  1.00 12.36 ? 29  SER   A O   1 
ATOM   227  C  CB  . SER   A 1 29  ? 17.069  0.534   23.707  1.00 11.48 ? 29  SER   A CB  1 
ATOM   228  O  OG  . SER   A 1 29  ? 16.430  1.219   24.810  1.00 12.19 ? 29  SER   A OG  1 
ATOM   229  N  N   . PRO   A 1 30  ? 18.092  -2.387  22.884  1.00 13.06 ? 30  PRO   A N   1 
ATOM   230  C  CA  . PRO   A 1 30  ? 16.905  -2.894  23.585  1.00 12.18 ? 30  PRO   A CA  1 
ATOM   231  C  C   . PRO   A 1 30  ? 17.307  -3.561  24.894  1.00 10.72 ? 30  PRO   A C   1 
ATOM   232  O  O   . PRO   A 1 30  ? 18.516  -3.568  25.232  1.00 12.35 ? 30  PRO   A O   1 
ATOM   233  C  CB  . PRO   A 1 30  ? 16.420  -3.938  22.552  1.00 12.02 ? 30  PRO   A CB  1 
ATOM   234  C  CG  . PRO   A 1 30  ? 17.755  -4.559  22.062  1.00 10.62 ? 30  PRO   A CG  1 
ATOM   235  C  CD  . PRO   A 1 30  ? 18.632  -3.320  21.917  1.00 11.75 ? 30  PRO   A CD  1 
ATOM   236  N  N   . VAL   A 1 31  ? 16.347  -4.136  25.606  1.00 12.59 ? 31  VAL   A N   1 
ATOM   237  C  CA  . VAL   A 1 31  ? 16.554  -4.848  26.859  1.00 12.47 ? 31  VAL   A CA  1 
ATOM   238  C  C   . VAL   A 1 31  ? 15.646  -6.072  26.868  1.00 13.04 ? 31  VAL   A C   1 
ATOM   239  O  O   . VAL   A 1 31  ? 14.709  -6.156  26.090  1.00 13.69 ? 31  VAL   A O   1 
ATOM   240  C  CB  . VAL   A 1 31  ? 16.255  -4.016  28.123  1.00 12.02 ? 31  VAL   A CB  1 
ATOM   241  C  CG1 . VAL   A 1 31  ? 17.165  -2.789  28.154  1.00 13.54 ? 31  VAL   A CG1 1 
ATOM   242  C  CG2 . VAL   A 1 31  ? 14.768  -3.596  28.162  1.00 13.43 ? 31  VAL   A CG2 1 
ATOM   243  N  N   . ASP   A 1 32  ? 16.014  -7.057  27.674  1.00 13.03 ? 32  ASP   A N   1 
ATOM   244  C  CA  . ASP   A 1 32  ? 15.084  -8.141  27.928  1.00 11.72 ? 32  ASP   A CA  1 
ATOM   245  C  C   . ASP   A 1 32  ? 14.034  -7.610  28.905  1.00 12.92 ? 32  ASP   A C   1 
ATOM   246  O  O   . ASP   A 1 32  ? 14.351  -6.955  29.897  1.00 13.90 ? 32  ASP   A O   1 
ATOM   247  C  CB  . ASP   A 1 32  ? 15.827  -9.304  28.567  1.00 12.20 ? 32  ASP   A CB  1 
ATOM   248  C  CG  . ASP   A 1 32  ? 14.916  -10.510 28.875  1.00 12.58 ? 32  ASP   A CG  1 
ATOM   249  O  OD1 . ASP   A 1 32  ? 14.191  -10.966 27.935  1.00 14.59 ? 32  ASP   A OD1 1 
ATOM   250  O  OD2 . ASP   A 1 32  ? 14.888  -10.907 30.095  1.00 17.09 ? 32  ASP   A OD2 1 
ATOM   251  N  N   . ILE   A 1 33  ? 12.767  -7.968  28.665  1.00 12.31 ? 33  ILE   A N   1 
ATOM   252  C  CA  . ILE   A 1 33  ? 11.668  -7.627  29.546  1.00 14.10 ? 33  ILE   A CA  1 
ATOM   253  C  C   . ILE   A 1 33  ? 11.401  -8.880  30.382  1.00 13.46 ? 33  ILE   A C   1 
ATOM   254  O  O   . ILE   A 1 33  ? 10.847  -9.879  29.878  1.00 16.72 ? 33  ILE   A O   1 
ATOM   255  C  CB  . ILE   A 1 33  ? 10.448  -7.179  28.710  1.00 13.39 ? 33  ILE   A CB  1 
ATOM   256  C  CG1 . ILE   A 1 33  ? 10.794  -5.919  27.897  1.00 15.39 ? 33  ILE   A CG1 1 
ATOM   257  C  CG2 . ILE   A 1 33  ? 9.189   -6.885  29.605  1.00 14.99 ? 33  ILE   A CG2 1 
ATOM   258  C  CD1 . ILE   A 1 33  ? 9.730   -5.608  26.780  1.00 15.38 ? 33  ILE   A CD1 1 
ATOM   259  N  N   . ASP   A 1 34  ? 11.739  -8.771  31.660  1.00 15.06 ? 34  ASP   A N   1 
ATOM   260  C  CA  . ASP   A 1 34  ? 11.501  -9.836  32.631  1.00 15.73 ? 34  ASP   A CA  1 
ATOM   261  C  C   . ASP   A 1 34  ? 10.079  -9.580  33.121  1.00 17.56 ? 34  ASP   A C   1 
ATOM   262  O  O   . ASP   A 1 34  ? 9.820   -8.615  33.873  1.00 19.26 ? 34  ASP   A O   1 
ATOM   263  C  CB  . ASP   A 1 34  ? 12.508  -9.763  33.785  1.00 19.66 ? 34  ASP   A CB  1 
ATOM   264  C  CG  . ASP   A 1 34  ? 12.209  -10.790 34.886  1.00 22.73 ? 34  ASP   A CG  1 
ATOM   265  O  OD1 . ASP   A 1 34  ? 11.078  -11.122 35.133  1.00 26.06 ? 34  ASP   A OD1 1 
ATOM   266  O  OD2 . ASP   A 1 34  ? 13.100  -11.250 35.495  1.00 34.54 ? 34  ASP   A OD2 1 
ATOM   267  N  N   . THR   A 1 35  ? 9.151   -10.386 32.623  1.00 15.67 ? 35  THR   A N   1 
ATOM   268  C  CA  . THR   A 1 35  ? 7.743   -10.090 32.853  1.00 18.52 ? 35  THR   A CA  1 
ATOM   269  C  C   . THR   A 1 35  ? 7.371   -10.226 34.323  1.00 20.99 ? 35  THR   A C   1 
ATOM   270  O  O   . THR   A 1 35  ? 6.402   -9.599  34.780  1.00 23.23 ? 35  THR   A O   1 
ATOM   271  C  CB  . THR   A 1 35  ? 6.831   -11.022 32.046  1.00 20.74 ? 35  THR   A CB  1 
ATOM   272  O  OG1 . THR   A 1 35  ? 6.988   -12.346 32.550  1.00 19.96 ? 35  THR   A OG1 1 
ATOM   273  C  CG2 . THR   A 1 35  ? 7.075   -10.950 30.551  1.00 20.67 ? 35  THR   A CG2 1 
ATOM   274  N  N   . HIS   A 1 36  ? 8.093   -11.080 35.055  1.00 19.65 ? 36  HIS   A N   1 
ATOM   275  C  CA  . HIS   A 1 36  ? 7.866   -11.266 36.478  1.00 23.04 ? 36  HIS   A CA  1 
ATOM   276  C  C   . HIS   A 1 36  ? 8.266   -10.048 37.316  1.00 25.71 ? 36  HIS   A C   1 
ATOM   277  O  O   . HIS   A 1 36  ? 7.534   -9.726  38.266  1.00 29.79 ? 36  HIS   A O   1 
ATOM   278  C  CB  . HIS   A 1 36  ? 8.444   -12.620 36.916  1.00 25.29 ? 36  HIS   A CB  1 
ATOM   279  C  CG  . HIS   A 1 36  ? 7.604   -13.718 36.351  1.00 31.15 ? 36  HIS   A CG  1 
ATOM   280  N  ND1 . HIS   A 1 36  ? 8.015   -14.509 35.289  1.00 32.72 ? 36  HIS   A ND1 1 
ATOM   281  C  CD2 . HIS   A 1 36  ? 6.328   -14.079 36.620  1.00 32.05 ? 36  HIS   A CD2 1 
ATOM   282  C  CE1 . HIS   A 1 36  ? 7.051   -15.358 34.975  1.00 34.67 ? 36  HIS   A CE1 1 
ATOM   283  N  NE2 . HIS   A 1 36  ? 6.008   -15.125 35.784  1.00 43.43 ? 36  HIS   A NE2 1 
ATOM   284  N  N   . THR   A 1 37  ? 9.319   -9.323  36.878  1.00 20.68 ? 37  THR   A N   1 
ATOM   285  C  CA  . THR   A 1 37  ? 9.791   -8.166  37.632  1.00 23.00 ? 37  THR   A CA  1 
ATOM   286  C  C   . THR   A 1 37  ? 9.264   -6.811  37.176  1.00 20.63 ? 37  THR   A C   1 
ATOM   287  O  O   . THR   A 1 37  ? 9.425   -5.840  37.921  1.00 26.03 ? 37  THR   A O   1 
ATOM   288  C  CB  . THR   A 1 37  ? 11.284  -8.197  37.872  1.00 30.97 ? 37  THR   A CB  1 
ATOM   289  O  OG1 . THR   A 1 37  ? 11.946  -8.026  36.639  1.00 39.65 ? 37  THR   A OG1 1 
ATOM   290  C  CG2 . THR   A 1 37  ? 11.683  -9.594  38.225  1.00 27.66 ? 37  THR   A CG2 1 
ATOM   291  N  N   . ALA   A 1 38  ? 8.719   -6.737  35.961  1.00 20.79 ? 38  ALA   A N   1 
ATOM   292  C  CA  . ALA   A 1 38  ? 8.052   -5.521  35.526  1.00 18.72 ? 38  ALA   A CA  1 
ATOM   293  C  C   . ALA   A 1 38  ? 6.895   -5.253  36.462  1.00 22.40 ? 38  ALA   A C   1 
ATOM   294  O  O   . ALA   A 1 38  ? 6.058   -6.126  36.707  1.00 27.99 ? 38  ALA   A O   1 
ATOM   295  C  CB  . ALA   A 1 38  ? 7.570   -5.701  34.114  1.00 18.70 ? 38  ALA   A CB  1 
ATOM   296  N  N   . LYS   A 1 39  ? 6.827   -4.038  36.978  1.00 23.23 ? 39  LYS   A N   1 
ATOM   297  C  CA  . LYS   A 1 39  ? 5.750   -3.762  37.913  1.00 25.10 ? 39  LYS   A CA  1 
ATOM   298  C  C   . LYS   A 1 39  ? 4.571   -3.050  37.260  1.00 20.44 ? 39  LYS   A C   1 
ATOM   299  O  O   . LYS   A 1 39  ? 4.732   -2.038  36.570  1.00 20.67 ? 39  LYS   A O   1 
ATOM   300  C  CB  . LYS   A 1 39  ? 6.220   -2.938  39.097  1.00 30.35 ? 39  LYS   A CB  1 
ATOM   301  C  CG  . LYS   A 1 39  ? 5.298   -3.019  40.314  1.00 33.44 ? 39  LYS   A CG  1 
ATOM   302  C  CD  . LYS   A 1 39  ? 5.843   -2.250  41.473  1.00 33.79 ? 39  LYS   A CD  1 
ATOM   303  C  CE  . LYS   A 1 39  ? 4.787   -1.447  42.199  1.00 39.72 ? 39  LYS   A CE  1 
ATOM   304  N  NZ  . LYS   A 1 39  ? 4.613   -1.948  43.568  1.00 44.75 ? 39  LYS   A NZ  1 
ATOM   305  N  N   . TYR   A 1 40  ? 3.395   -3.550  37.600  1.00 21.90 ? 40  TYR   A N   1 
ATOM   306  C  CA  . TYR   A 1 40  ? 2.195   -2.868  37.201  1.00 19.63 ? 40  TYR   A CA  1 
ATOM   307  C  C   . TYR   A 1 40  ? 2.201   -1.493  37.843  1.00 18.35 ? 40  TYR   A C   1 
ATOM   308  O  O   . TYR   A 1 40  ? 2.400   -1.346  39.064  1.00 22.17 ? 40  TYR   A O   1 
ATOM   309  C  CB  . TYR   A 1 40  ? 0.969   -3.679  37.633  1.00 24.43 ? 40  TYR   A CB  1 
ATOM   310  C  CG  . TYR   A 1 40  ? -0.310  -2.920  37.476  1.00 25.54 ? 40  TYR   A CG  1 
ATOM   311  C  CD1 . TYR   A 1 40  ? -0.681  -2.440  36.233  1.00 24.85 ? 40  TYR   A CD1 1 
ATOM   312  C  CD2 . TYR   A 1 40  ? -1.135  -2.669  38.557  1.00 29.68 ? 40  TYR   A CD2 1 
ATOM   313  C  CE1 . TYR   A 1 40  ? -1.867  -1.757  36.032  1.00 26.56 ? 40  TYR   A CE1 1 
ATOM   314  C  CE2 . TYR   A 1 40  ? -2.331  -1.989  38.385  1.00 29.45 ? 40  TYR   A CE2 1 
ATOM   315  C  CZ  . TYR   A 1 40  ? -2.691  -1.520  37.123  1.00 30.86 ? 40  TYR   A CZ  1 
ATOM   316  O  OH  . TYR   A 1 40  ? -3.854  -0.835  36.954  1.00 35.91 ? 40  TYR   A OH  1 
ATOM   317  N  N   . ASP   A 1 41  ? 1.897   -0.488  37.009  1.00 16.40 ? 41  ASP   A N   1 
ATOM   318  C  CA  . ASP   A 1 41  ? 1.878   0.909   37.449  1.00 17.20 ? 41  ASP   A CA  1 
ATOM   319  C  C   . ASP   A 1 41  ? 0.488   1.487   37.227  1.00 22.42 ? 41  ASP   A C   1 
ATOM   320  O  O   . ASP   A 1 41  ? 0.181   1.908   36.105  1.00 23.36 ? 41  ASP   A O   1 
ATOM   321  C  CB  . ASP   A 1 41  ? 2.910   1.756   36.696  1.00 21.03 ? 41  ASP   A CB  1 
ATOM   322  C  CG  . ASP   A 1 41  ? 2.974   3.157   37.259  1.00 24.55 ? 41  ASP   A CG  1 
ATOM   323  O  OD1 . ASP   A 1 41  ? 2.097   3.488   38.066  1.00 24.51 ? 41  ASP   A OD1 1 
ATOM   324  O  OD2 . ASP   A 1 41  ? 3.905   3.876   36.900  1.00 28.07 ? 41  ASP   A OD2 1 
ATOM   325  N  N   . PRO   A 1 42  ? -0.344  1.558   38.305  1.00 23.95 ? 42  PRO   A N   1 
ATOM   326  C  CA  . PRO   A 1 42  ? -1.715  2.035   38.152  1.00 24.70 ? 42  PRO   A CA  1 
ATOM   327  C  C   . PRO   A 1 42  ? -1.797  3.486   37.688  1.00 24.39 ? 42  PRO   A C   1 
ATOM   328  O  O   . PRO   A 1 42  ? -2.868  3.933   37.261  1.00 33.05 ? 42  PRO   A O   1 
ATOM   329  C  CB  . PRO   A 1 42  ? -2.369  1.777   39.537  1.00 30.88 ? 42  PRO   A CB  1 
ATOM   330  C  CG  . PRO   A 1 42  ? -1.220  1.709   40.495  1.00 36.29 ? 42  PRO   A CG  1 
ATOM   331  C  CD  . PRO   A 1 42  ? -0.041  1.148   39.696  1.00 29.81 ? 42  PRO   A CD  1 
ATOM   332  N  N   . SER   A 1 43  ? -0.684  4.217   37.790  1.00 26.17 ? 43  SER   A N   1 
ATOM   333  C  CA  . SER   A 1 43  ? -0.678  5.610   37.346  1.00 27.80 ? 43  SER   A CA  1 
ATOM   334  C  C   . SER   A 1 43  ? -0.397  5.754   35.845  1.00 27.34 ? 43  SER   A C   1 
ATOM   335  O  O   . SER   A 1 43  ? -0.495  6.873   35.317  1.00 34.10 ? 43  SER   A O   1 
ATOM   336  C  CB  . SER   A 1 43  ? 0.283   6.445   38.159  1.00 28.46 ? 43  SER   A CB  1 
ATOM   337  O  OG  . SER   A 1 43  ? 1.622   6.135   37.823  1.00 33.49 ? 43  SER   A OG  1 
ATOM   338  N  N   . LEU   A 1 44  ? -0.061  4.656   35.143  1.00 27.04 ? 44  LEU   A N   1 
ATOM   339  C  CA  . LEU   A 1 44  ? 0.079   4.740   33.687  1.00 23.30 ? 44  LEU   A CA  1 
ATOM   340  C  C   . LEU   A 1 44  ? -1.283  4.909   33.046  1.00 28.14 ? 44  LEU   A C   1 
ATOM   341  O  O   . LEU   A 1 44  ? -2.244  4.268   33.467  1.00 34.48 ? 44  LEU   A O   1 
ATOM   342  C  CB  . LEU   A 1 44  ? 0.742   3.487   33.114  1.00 21.63 ? 44  LEU   A CB  1 
ATOM   343  C  CG  . LEU   A 1 44  ? 2.219   3.386   33.412  1.00 19.20 ? 44  LEU   A CG  1 
ATOM   344  C  CD1 . LEU   A 1 44  ? 2.686   2.010   32.973  1.00 18.58 ? 44  LEU   A CD1 1 
ATOM   345  C  CD2 . LEU   A 1 44  ? 2.953   4.508   32.706  1.00 20.02 ? 44  LEU   A CD2 1 
ATOM   346  N  N   . LYS   A 1 45  ? -1.328  5.726   31.985  1.00 27.37 ? 45  LYS   A N   1 
ATOM   347  C  CA  . LYS   A 1 45  ? -2.577  5.882   31.259  1.00 26.57 ? 45  LYS   A CA  1 
ATOM   348  C  C   . LYS   A 1 45  ? -2.674  4.943   30.071  1.00 23.87 ? 45  LYS   A C   1 
ATOM   349  O  O   . LYS   A 1 45  ? -1.701  4.305   29.647  1.00 27.85 ? 45  LYS   A O   1 
ATOM   350  C  CB  . LYS   A 1 45  ? -2.794  7.321   30.807  1.00 25.71 ? 45  LYS   A CB  1 
ATOM   351  C  CG  . LYS   A 1 45  ? -2.517  8.349   31.884  1.00 29.55 ? 45  LYS   A CG  1 
ATOM   352  C  CD  . LYS   A 1 45  ? -2.531  9.756   31.377  1.00 40.30 ? 45  LYS   A CD  1 
ATOM   353  N  N   . PRO   A 1 46  ? -3.900  4.733   29.539  1.00 25.80 ? 46  PRO   A N   1 
ATOM   354  C  CA  . PRO   A 1 46  ? -4.000  4.005   28.280  1.00 24.92 ? 46  PRO   A CA  1 
ATOM   355  C  C   . PRO   A 1 46  ? -3.208  4.818   27.259  1.00 18.70 ? 46  PRO   A C   1 
ATOM   356  O  O   . PRO   A 1 46  ? -3.218  6.049   27.265  1.00 20.35 ? 46  PRO   A O   1 
ATOM   357  C  CB  . PRO   A 1 46  ? -5.510  4.130   27.977  1.00 24.64 ? 46  PRO   A CB  1 
ATOM   358  C  CG  . PRO   A 1 46  ? -6.159  4.207   29.351  1.00 29.22 ? 46  PRO   A CG  1 
ATOM   359  C  CD  . PRO   A 1 46  ? -5.216  5.109   30.121  1.00 26.34 ? 46  PRO   A CD  1 
ATOM   360  N  N   . LEU   A 1 47  ? -2.598  4.121   26.310  1.00 22.91 ? 47  LEU   A N   1 
ATOM   361  C  CA  . LEU   A 1 47  ? -1.909  4.786   25.227  1.00 20.04 ? 47  LEU   A CA  1 
ATOM   362  C  C   . LEU   A 1 47  ? -2.950  5.372   24.262  1.00 20.91 ? 47  LEU   A C   1 
ATOM   363  O  O   . LEU   A 1 47  ? -4.026  4.778   24.023  1.00 24.87 ? 47  LEU   A O   1 
ATOM   364  C  CB  . LEU   A 1 47  ? -1.108  3.670   24.565  1.00 25.69 ? 47  LEU   A CB  1 
ATOM   365  C  CG  . LEU   A 1 47  ? -0.081  4.072   23.543  1.00 24.74 ? 47  LEU   A CG  1 
ATOM   366  C  CD1 . LEU   A 1 47  ? 0.964   4.971   24.213  1.00 24.01 ? 47  LEU   A CD1 1 
ATOM   367  C  CD2 . LEU   A 1 47  ? 0.564   2.806   23.001  1.00 25.54 ? 47  LEU   A CD2 1 
ATOM   368  N  N   . SER   A 1 48  ? -2.673  6.574   23.744  1.00 16.77 ? 48  SER   A N   1 
ATOM   369  C  CA  . SER   A 1 48  ? -3.518  7.147   22.703  1.00 18.19 ? 48  SER   A CA  1 
ATOM   370  C  C   . SER   A 1 48  ? -2.747  7.162   21.384  1.00 17.65 ? 48  SER   A C   1 
ATOM   371  O  O   . SER   A 1 48  ? -1.748  7.880   21.225  1.00 18.18 ? 48  SER   A O   1 
ATOM   372  C  CB  . SER   A 1 48  ? -3.903  8.546   23.125  1.00 18.84 ? 48  SER   A CB  1 
ATOM   373  O  OG  . SER   A 1 48  ? -4.518  9.170   22.053  1.00 21.03 ? 48  SER   A OG  1 
ATOM   374  N  N   . VAL   A 1 49  ? -3.145  6.342   20.426  1.00 19.59 ? 49  VAL   A N   1 
ATOM   375  C  CA  . VAL   A 1 49  ? -2.494  6.237   19.126  1.00 18.55 ? 49  VAL   A CA  1 
ATOM   376  C  C   . VAL   A 1 49  ? -3.461  6.853   18.132  1.00 19.54 ? 49  VAL   A C   1 
ATOM   377  O  O   . VAL   A 1 49  ? -4.566  6.312   17.951  1.00 23.60 ? 49  VAL   A O   1 
ATOM   378  C  CB  . VAL   A 1 49  ? -2.227  4.756   18.757  1.00 20.87 ? 49  VAL   A CB  1 
ATOM   379  C  CG1 . VAL   A 1 49  ? -1.547  4.596   17.402  1.00 29.35 ? 49  VAL   A CG1 1 
ATOM   380  C  CG2 . VAL   A 1 49  ? -1.508  4.047   19.883  1.00 20.94 ? 49  VAL   A CG2 1 
ATOM   381  N  N   . SER   A 1 50  ? -3.126  8.021   17.585  1.00 20.00 ? 50  SER   A N   1 
ATOM   382  C  CA  . SER   A 1 50  ? -4.072  8.713   16.705  1.00 19.52 ? 50  SER   A CA  1 
ATOM   383  C  C   . SER   A 1 50  ? -3.498  8.771   15.302  1.00 20.35 ? 50  SER   A C   1 
ATOM   384  O  O   . SER   A 1 50  ? -2.773  9.678   14.986  1.00 20.86 ? 50  SER   A O   1 
ATOM   385  C  CB  . SER   A 1 50  ? -4.314  10.102  17.164  1.00 24.63 ? 50  SER   A CB  1 
ATOM   386  O  OG  . SER   A 1 50  ? -5.025  10.054  18.366  1.00 35.78 ? 50  SER   A OG  1 
ATOM   387  N  N   . TYR   A 1 51  ? -3.771  7.770   14.494  1.00 19.82 ? 51  TYR   A N   1 
ATOM   388  C  CA  . TYR   A 1 51  ? -3.179  7.618   13.178  1.00 16.77 ? 51  TYR   A CA  1 
ATOM   389  C  C   . TYR   A 1 51  ? -4.179  7.854   12.035  1.00 19.51 ? 51  TYR   A C   1 
ATOM   390  O  O   . TYR   A 1 51  ? -3.790  7.641   10.892  1.00 22.12 ? 51  TYR   A O   1 
ATOM   391  C  CB  . TYR   A 1 51  ? -2.518  6.235   13.047  1.00 18.07 ? 51  TYR   A CB  1 
ATOM   392  C  CG  . TYR   A 1 51  ? -1.228  5.984   13.810  1.00 15.73 ? 51  TYR   A CG  1 
ATOM   393  C  CD1 . TYR   A 1 51  ? -0.509  6.995   14.439  1.00 17.54 ? 51  TYR   A CD1 1 
ATOM   394  C  CD2 . TYR   A 1 51  ? -0.697  4.699   13.866  1.00 17.84 ? 51  TYR   A CD2 1 
ATOM   395  C  CE1 . TYR   A 1 51  ? 0.673   6.709   15.126  1.00 14.99 ? 51  TYR   A CE1 1 
ATOM   396  C  CE2 . TYR   A 1 51  ? 0.450   4.367   14.570  1.00 16.00 ? 51  TYR   A CE2 1 
ATOM   397  C  CZ  . TYR   A 1 51  ? 1.143   5.394   15.194  1.00 14.96 ? 51  TYR   A CZ  1 
ATOM   398  O  OH  . TYR   A 1 51  ? 2.305   5.112   15.857  1.00 14.43 ? 51  TYR   A OH  1 
ATOM   399  N  N   A ASP   A 1 52  ? -5.403  8.341   12.343  0.50 23.47 ? 52  ASP   A N   1 
ATOM   400  N  N   B ASP   A 1 52  ? -5.431  8.227   12.346  0.50 21.92 ? 52  ASP   A N   1 
ATOM   401  C  CA  A ASP   A 1 52  ? -6.488  8.559   11.379  0.50 24.15 ? 52  ASP   A CA  1 
ATOM   402  C  CA  B ASP   A 1 52  ? -6.424  8.494   11.310  0.50 23.07 ? 52  ASP   A CA  1 
ATOM   403  C  C   A ASP   A 1 52  ? -6.137  9.541   10.246  0.50 21.19 ? 52  ASP   A C   1 
ATOM   404  C  C   B ASP   A 1 52  ? -5.867  9.342   10.154  0.50 24.53 ? 52  ASP   A C   1 
ATOM   405  O  O   A ASP   A 1 52  ? -6.697  9.465   9.150   0.50 23.71 ? 52  ASP   A O   1 
ATOM   406  O  O   B ASP   A 1 52  ? -6.041  8.985   8.975   0.50 24.57 ? 52  ASP   A O   1 
ATOM   407  C  CB  A ASP   A 1 52  ? -7.775  8.995   12.090  0.50 27.25 ? 52  ASP   A CB  1 
ATOM   408  C  CB  B ASP   A 1 52  ? -7.669  9.137   11.919  0.50 24.23 ? 52  ASP   A CB  1 
ATOM   409  C  CG  A ASP   A 1 52  ? -7.561  10.087  13.128  0.50 32.85 ? 52  ASP   A CG  1 
ATOM   410  C  CG  B ASP   A 1 52  ? -8.765  9.300   10.894  0.50 26.47 ? 52  ASP   A CG  1 
ATOM   411  O  OD1 A ASP   A 1 52  ? -6.852  9.824   14.140  0.50 28.57 ? 52  ASP   A OD1 1 
ATOM   412  O  OD1 B ASP   A 1 52  ? -9.234  8.276   10.380  0.50 31.39 ? 52  ASP   A OD1 1 
ATOM   413  O  OD2 A ASP   A 1 52  ? -8.103  11.198  12.923  0.50 41.85 ? 52  ASP   A OD2 1 
ATOM   414  O  OD2 B ASP   A 1 52  ? -9.091  10.454  10.569  0.50 32.25 ? 52  ASP   A OD2 1 
ATOM   415  N  N   . GLN   A 1 53  ? -5.207  10.463  10.497  1.00 21.24 ? 53  GLN   A N   1 
ATOM   416  C  CA  . GLN   A 1 53  ? -4.753  11.448  9.513   1.00 24.21 ? 53  GLN   A CA  1 
ATOM   417  C  C   . GLN   A 1 53  ? -3.302  11.230  9.060   1.00 21.59 ? 53  GLN   A C   1 
ATOM   418  O  O   . GLN   A 1 53  ? -2.708  12.098  8.412   1.00 21.79 ? 53  GLN   A O   1 
ATOM   419  C  CB  . GLN   A 1 53  ? -4.870  12.879  10.082  1.00 27.87 ? 53  GLN   A CB  1 
ATOM   420  C  CG  . GLN   A 1 53  ? -6.281  13.276  10.499  1.00 41.95 ? 53  GLN   A CG  1 
ATOM   421  C  CD  . GLN   A 1 53  ? -6.983  13.640  9.217   1.00 42.92 ? 53  GLN   A CD  1 
ATOM   422  O  OE1 . GLN   A 1 53  ? -6.762  14.717  8.643   1.00 64.88 ? 53  GLN   A OE1 1 
ATOM   423  N  NE2 . GLN   A 1 53  ? -7.747  12.686  8.709   1.00 45.72 ? 53  GLN   A NE2 1 
ATOM   424  N  N   . ALA   A 1 54  ? -2.737  10.058  9.324   1.00 19.51 ? 54  ALA   A N   1 
ATOM   425  C  CA  . ALA   A 1 54  ? -1.346  9.848   8.951   1.00 17.32 ? 54  ALA   A CA  1 
ATOM   426  C  C   . ALA   A 1 54  ? -1.179  10.009  7.426   1.00 18.94 ? 54  ALA   A C   1 
ATOM   427  O  O   . ALA   A 1 54  ? -2.025  9.565   6.630   1.00 29.06 ? 54  ALA   A O   1 
ATOM   428  C  CB  . ALA   A 1 54  ? -0.931  8.452   9.399   1.00 17.83 ? 54  ALA   A CB  1 
ATOM   429  N  N   . THR   A 1 55  ? -0.038  10.583  7.005   1.00 16.62 ? 55  THR   A N   1 
ATOM   430  C  CA  . THR   A 1 55  ? 0.274   10.785  5.599   1.00 16.28 ? 55  THR   A CA  1 
ATOM   431  C  C   . THR   A 1 55  ? 1.618   10.151  5.262   1.00 14.35 ? 55  THR   A C   1 
ATOM   432  O  O   . THR   A 1 55  ? 2.658   10.752  5.512   1.00 15.57 ? 55  THR   A O   1 
ATOM   433  C  CB  . THR   A 1 55  ? 0.404   12.272  5.236   1.00 23.11 ? 55  THR   A CB  1 
ATOM   434  O  OG1 . THR   A 1 55  ? -0.827  12.931  5.490   1.00 30.82 ? 55  THR   A OG1 1 
ATOM   435  C  CG2 . THR   A 1 55  ? 0.717   12.402  3.765   1.00 27.84 ? 55  THR   A CG2 1 
ATOM   436  N  N   . SER   A 1 56  ? 1.601   8.912   4.784   1.00 15.63 ? 56  SER   A N   1 
ATOM   437  C  CA  . SER   A 1 56  ? 2.857   8.290   4.381   1.00 15.63 ? 56  SER   A CA  1 
ATOM   438  C  C   . SER   A 1 56  ? 3.350   8.946   3.085   1.00 16.68 ? 56  SER   A C   1 
ATOM   439  O  O   . SER   A 1 56  ? 2.536   9.433   2.268   1.00 19.29 ? 56  SER   A O   1 
ATOM   440  C  CB  . SER   A 1 56  ? 2.766   6.791   4.253   1.00 18.25 ? 56  SER   A CB  1 
ATOM   441  O  OG  . SER   A 1 56  ? 1.946   6.446   3.137   1.00 19.16 ? 56  SER   A OG  1 
ATOM   442  N  N   . LEU   A 1 57  ? 4.671   8.931   2.843   1.00 16.01 ? 57  LEU   A N   1 
ATOM   443  C  CA  . LEU   A 1 57  ? 5.175   9.568   1.633   1.00 18.39 ? 57  LEU   A CA  1 
ATOM   444  C  C   . LEU   A 1 57  ? 6.025   8.631   0.776   1.00 16.88 ? 57  LEU   A C   1 
ATOM   445  O  O   . LEU   A 1 57  ? 5.953   8.660   -0.446  1.00 16.94 ? 57  LEU   A O   1 
ATOM   446  C  CB  . LEU   A 1 57  ? 6.044   10.769  2.028   1.00 21.31 ? 57  LEU   A CB  1 
ATOM   447  C  CG  . LEU   A 1 57  ? 5.267   11.929  2.655   1.00 24.36 ? 57  LEU   A CG  1 
ATOM   448  C  CD1 . LEU   A 1 57  ? 6.212   13.039  3.098   1.00 31.66 ? 57  LEU   A CD1 1 
ATOM   449  C  CD2 . LEU   A 1 57  ? 4.196   12.465  1.698   1.00 33.61 ? 57  LEU   A CD2 1 
ATOM   450  N  N   . ARG   A 1 58  ? 6.914   7.862   1.431   1.00 15.75 ? 58  ARG   A N   1 
ATOM   451  C  CA  . ARG   A 1 58  ? 8.006   7.269   0.678   1.00 14.41 ? 58  ARG   A CA  1 
ATOM   452  C  C   . ARG   A 1 58  ? 8.520   6.093   1.504   1.00 13.59 ? 58  ARG   A C   1 
ATOM   453  O  O   . ARG   A 1 58  ? 8.402   6.096   2.726   1.00 14.31 ? 58  ARG   A O   1 
ATOM   454  C  CB  . ARG   A 1 58  ? 9.150   8.287   0.524   1.00 14.71 ? 58  ARG   A CB  1 
ATOM   455  C  CG  . ARG   A 1 58  ? 10.173  7.914   -0.545  1.00 15.84 ? 58  ARG   A CG  1 
ATOM   456  C  CD  . ARG   A 1 58  ? 11.220  9.025   -0.718  1.00 19.22 ? 58  ARG   A CD  1 
ATOM   457  N  NE  . ARG   A 1 58  ? 12.107  8.988   0.446   1.00 15.73 ? 58  ARG   A NE  1 
ATOM   458  C  CZ  . ARG   A 1 58  ? 13.419  9.188   0.399   1.00 16.57 ? 58  ARG   A CZ  1 
ATOM   459  N  NH1 . ARG   A 1 58  ? 14.009  9.441   -0.757  1.00 18.25 ? 58  ARG   A NH1 1 
ATOM   460  N  NH2 . ARG   A 1 58  ? 14.137  9.134   1.506   1.00 15.98 ? 58  ARG   A NH2 1 
ATOM   461  N  N   . ILE   A 1 59  ? 9.116   5.133   0.803   1.00 14.50 ? 59  ILE   A N   1 
ATOM   462  C  CA  . ILE   A 1 59  ? 9.803   4.056   1.493   1.00 13.31 ? 59  ILE   A CA  1 
ATOM   463  C  C   . ILE   A 1 59  ? 11.244  4.017   0.989   1.00 11.97 ? 59  ILE   A C   1 
ATOM   464  O  O   . ILE   A 1 59  ? 11.479  4.158   -0.214  1.00 14.17 ? 59  ILE   A O   1 
ATOM   465  C  CB  . ILE   A 1 59  ? 9.042   2.713   1.304   1.00 12.15 ? 59  ILE   A CB  1 
ATOM   466  C  CG1 . ILE   A 1 59  ? 9.628   1.581   2.160   1.00 12.92 ? 59  ILE   A CG1 1 
ATOM   467  C  CG2 . ILE   A 1 59  ? 8.962   2.331   -0.163  1.00 13.66 ? 59  ILE   A CG2 1 
ATOM   468  C  CD1 . ILE   A 1 59  ? 8.832   0.261   2.080   1.00 16.26 ? 59  ILE   A CD1 1 
ATOM   469  N  N   . LEU   A 1 60  ? 12.188  3.862   1.938   1.00 12.40 ? 60  LEU   A N   1 
ATOM   470  C  CA  . LEU   A 1 60  ? 13.625  3.994   1.650   1.00 12.48 ? 60  LEU   A CA  1 
ATOM   471  C  C   . LEU   A 1 60  ? 14.347  2.751   2.211   1.00 11.60 ? 60  LEU   A C   1 
ATOM   472  O  O   . LEU   A 1 60  ? 14.192  2.432   3.391   1.00 13.94 ? 60  LEU   A O   1 
ATOM   473  C  CB  . LEU   A 1 60  ? 14.157  5.275   2.346   1.00 12.54 ? 60  LEU   A CB  1 
ATOM   474  C  CG  . LEU   A 1 60  ? 15.703  5.394   2.365   1.00 11.90 ? 60  LEU   A CG  1 
ATOM   475  C  CD1 . LEU   A 1 60  ? 16.172  5.654   0.929   1.00 13.90 ? 60  LEU   A CD1 1 
ATOM   476  C  CD2 . LEU   A 1 60  ? 16.130  6.497   3.346   1.00 14.21 ? 60  LEU   A CD2 1 
ATOM   477  N  N   . ASN   A 1 61  ? 15.209  2.141   1.382   1.00 12.81 ? 61  ASN   A N   1 
ATOM   478  C  CA  . ASN   A 1 61  ? 16.166  1.163   1.882   1.00 14.84 ? 61  ASN   A CA  1 
ATOM   479  C  C   . ASN   A 1 61  ? 17.344  1.982   2.420   1.00 14.18 ? 61  ASN   A C   1 
ATOM   480  O  O   . ASN   A 1 61  ? 18.088  2.612   1.638   1.00 14.53 ? 61  ASN   A O   1 
ATOM   481  C  CB  . ASN   A 1 61  ? 16.572  0.203   0.752   1.00 16.02 ? 61  ASN   A CB  1 
ATOM   482  C  CG  . ASN   A 1 61  ? 17.617  -0.794  1.205   1.00 15.23 ? 61  ASN   A CG  1 
ATOM   483  O  OD1 . ASN   A 1 61  ? 18.398  -0.520  2.126   1.00 15.57 ? 61  ASN   A OD1 1 
ATOM   484  N  ND2 . ASN   A 1 61  ? 17.565  -1.981  0.634   1.00 14.60 ? 61  ASN   A ND2 1 
ATOM   485  N  N   . ASN   A 1 62  ? 17.480  1.998   3.751   1.00 13.29 ? 62  ASN   A N   1 
ATOM   486  C  CA  . ASN   A 1 62  ? 18.414  2.941   4.388   1.00 15.37 ? 62  ASN   A CA  1 
ATOM   487  C  C   . ASN   A 1 62  ? 19.792  2.290   4.508   1.00 17.11 ? 62  ASN   A C   1 
ATOM   488  O  O   . ASN   A 1 62  ? 20.723  2.907   5.061   1.00 18.94 ? 62  ASN   A O   1 
ATOM   489  C  CB  . ASN   A 1 62  ? 17.826  3.438   5.737   1.00 17.81 ? 62  ASN   A CB  1 
ATOM   490  C  CG  . ASN   A 1 62  ? 17.799  2.398   6.843   1.00 16.82 ? 62  ASN   A CG  1 
ATOM   491  O  OD1 . ASN   A 1 62  ? 18.658  1.536   6.883   1.00 16.90 ? 62  ASN   A OD1 1 
ATOM   492  N  ND2 . ASN   A 1 62  ? 16.795  2.388   7.713   1.00 19.55 ? 62  ASN   A ND2 1 
ATOM   493  N  N   . GLY   A 1 63  ? 19.927  1.033   4.016   1.00 14.03 ? 63  GLY   A N   1 
ATOM   494  C  CA  . GLY   A 1 63  ? 21.176  0.291   4.043   1.00 14.94 ? 63  GLY   A CA  1 
ATOM   495  C  C   . GLY   A 1 63  ? 21.168  -0.711  5.201   1.00 12.10 ? 63  GLY   A C   1 
ATOM   496  O  O   . GLY   A 1 63  ? 22.018  -1.605  5.215   1.00 15.77 ? 63  GLY   A O   1 
ATOM   497  N  N   . HIS   A 1 64  ? 20.287  -0.543  6.195   1.00 12.91 ? 64  HIS   A N   1 
ATOM   498  C  CA  . HIS   A 1 64  ? 20.240  -1.372  7.396   1.00 13.76 ? 64  HIS   A CA  1 
ATOM   499  C  C   . HIS   A 1 64  ? 18.863  -2.016  7.533   1.00 13.93 ? 64  HIS   A C   1 
ATOM   500  O  O   . HIS   A 1 64  ? 18.743  -3.136  7.996   1.00 13.68 ? 64  HIS   A O   1 
ATOM   501  C  CB  . HIS   A 1 64  ? 20.614  -0.633  8.699   1.00 17.22 ? 64  HIS   A CB  1 
ATOM   502  C  CG  . HIS   A 1 64  ? 21.975  -0.068  8.600   1.00 23.03 ? 64  HIS   A CG  1 
ATOM   503  N  ND1 . HIS   A 1 64  ? 22.191  1.274   8.402   1.00 25.68 ? 64  HIS   A ND1 1 
ATOM   504  C  CD2 . HIS   A 1 64  ? 23.169  -0.664  8.701   1.00 23.04 ? 64  HIS   A CD2 1 
ATOM   505  C  CE1 . HIS   A 1 64  ? 23.482  1.499   8.353   1.00 22.34 ? 64  HIS   A CE1 1 
ATOM   506  N  NE2 . HIS   A 1 64  ? 24.112  0.313   8.514   1.00 24.54 ? 64  HIS   A NE2 1 
ATOM   507  N  N   . ALA   A 1 65  ? 17.819  -1.251  7.244   1.00 13.14 ? 65  ALA   A N   1 
ATOM   508  C  CA  . ALA   A 1 65  ? 16.420  -1.678  7.198   1.00 13.56 ? 65  ALA   A CA  1 
ATOM   509  C  C   . ALA   A 1 65  ? 15.752  -0.825  6.112   1.00 12.48 ? 65  ALA   A C   1 
ATOM   510  O  O   . ALA   A 1 65  ? 16.429  -0.160  5.308   1.00 14.67 ? 65  ALA   A O   1 
ATOM   511  C  CB  . ALA   A 1 65  ? 15.760  -1.575  8.573   1.00 11.71 ? 65  ALA   A CB  1 
ATOM   512  N  N   . PHE   A 1 66  ? 14.419  -0.805  6.150   1.00 12.46 ? 66  PHE   A N   1 
ATOM   513  C  CA  . PHE   A 1 66  ? 13.726  0.164   5.304   1.00 14.10 ? 66  PHE   A CA  1 
ATOM   514  C  C   . PHE   A 1 66  ? 12.842  1.034   6.188   1.00 13.47 ? 66  PHE   A C   1 
ATOM   515  O  O   . PHE   A 1 66  ? 12.235  0.591   7.151   1.00 12.51 ? 66  PHE   A O   1 
ATOM   516  C  CB  . PHE   A 1 66  ? 12.878  -0.489  4.209   1.00 14.24 ? 66  PHE   A CB  1 
ATOM   517  C  CG  . PHE   A 1 66  ? 11.813  -1.431  4.717   1.00 13.71 ? 66  PHE   A CG  1 
ATOM   518  C  CD1 . PHE   A 1 66  ? 10.548  -0.984  5.065   1.00 15.69 ? 66  PHE   A CD1 1 
ATOM   519  C  CD2 . PHE   A 1 66  ? 12.075  -2.829  4.812   1.00 14.35 ? 66  PHE   A CD2 1 
ATOM   520  C  CE1 . PHE   A 1 66  ? 9.595   -1.885  5.534   1.00 14.82 ? 66  PHE   A CE1 1 
ATOM   521  C  CE2 . PHE   A 1 66  ? 11.122  -3.718  5.321   1.00 14.81 ? 66  PHE   A CE2 1 
ATOM   522  C  CZ  . PHE   A 1 66  ? 9.856   -3.256  5.645   1.00 15.15 ? 66  PHE   A CZ  1 
ATOM   523  N  N   . ASN   A 1 67  ? 12.834  2.337   5.853   1.00 12.44 ? 67  ASN   A N   1 
ATOM   524  C  CA  . ASN   A 1 67  ? 11.978  3.300   6.551   1.00 12.52 ? 67  ASN   A CA  1 
ATOM   525  C  C   . ASN   A 1 67  ? 10.772  3.659   5.681   1.00 12.24 ? 67  ASN   A C   1 
ATOM   526  O  O   . ASN   A 1 67  ? 10.920  3.990   4.504   1.00 13.19 ? 67  ASN   A O   1 
ATOM   527  C  CB  . ASN   A 1 67  ? 12.733  4.609   6.781   1.00 11.72 ? 67  ASN   A CB  1 
ATOM   528  C  CG  . ASN   A 1 67  ? 14.031  4.433   7.541   1.00 12.18 ? 67  ASN   A CG  1 
ATOM   529  O  OD1 . ASN   A 1 67  ? 14.160  3.501   8.311   1.00 14.59 ? 67  ASN   A OD1 1 
ATOM   530  N  ND2 . ASN   A 1 67  ? 14.928  5.421   7.479   1.00 17.42 ? 67  ASN   A ND2 1 
ATOM   531  N  N   . VAL   A 1 68  ? 9.573   3.512   6.297   1.00 11.65 ? 68  VAL   A N   1 
ATOM   532  C  CA  . VAL   A 1 68  ? 8.373   4.121   5.698   1.00 13.05 ? 68  VAL   A CA  1 
ATOM   533  C  C   . VAL   A 1 68  ? 8.195   5.490   6.353   1.00 12.26 ? 68  VAL   A C   1 
ATOM   534  O  O   . VAL   A 1 68  ? 8.055   5.558   7.595   1.00 11.59 ? 68  VAL   A O   1 
ATOM   535  C  CB  . VAL   A 1 68  ? 7.133   3.225   5.907   1.00 13.90 ? 68  VAL   A CB  1 
ATOM   536  C  CG1 . VAL   A 1 68  ? 5.868   3.974   5.460   1.00 14.06 ? 68  VAL   A CG1 1 
ATOM   537  C  CG2 . VAL   A 1 68  ? 7.239   1.861   5.220   1.00 15.23 ? 68  VAL   A CG2 1 
ATOM   538  N  N   . GLU   A 1 69  ? 8.273   6.530   5.516   1.00 13.36 ? 69  GLU   A N   1 
ATOM   539  C  CA  . GLU   A 1 69  ? 8.382   7.898   6.026   1.00 14.48 ? 69  GLU   A CA  1 
ATOM   540  C  C   . GLU   A 1 69  ? 7.019   8.562   5.940   1.00 13.95 ? 69  GLU   A C   1 
ATOM   541  O  O   . GLU   A 1 69  ? 6.245   8.287   5.000   1.00 15.68 ? 69  GLU   A O   1 
ATOM   542  C  CB  . GLU   A 1 69  ? 9.298   8.686   5.096   1.00 14.34 ? 69  GLU   A CB  1 
ATOM   543  C  CG  . GLU   A 1 69  ? 10.705  8.099   5.093   1.00 13.55 ? 69  GLU   A CG  1 
ATOM   544  C  CD  . GLU   A 1 69  ? 11.544  8.548   3.904   1.00 13.59 ? 69  GLU   A CD  1 
ATOM   545  O  OE1 . GLU   A 1 69  ? 11.013  9.192   2.948   1.00 16.33 ? 69  GLU   A OE1 1 
ATOM   546  O  OE2 . GLU   A 1 69  ? 12.729  8.171   3.824   1.00 14.88 ? 69  GLU   A OE2 1 
ATOM   547  N  N   . PHE   A 1 70  ? 6.770   9.420   6.930   1.00 14.16 ? 70  PHE   A N   1 
ATOM   548  C  CA  . PHE   A 1 70  ? 5.517   10.155  7.048   1.00 12.23 ? 70  PHE   A CA  1 
ATOM   549  C  C   . PHE   A 1 70  ? 5.771   11.655  6.977   1.00 14.16 ? 70  PHE   A C   1 
ATOM   550  O  O   . PHE   A 1 70  ? 6.831   12.160  7.386   1.00 16.26 ? 70  PHE   A O   1 
ATOM   551  C  CB  . PHE   A 1 70  ? 4.823   9.812   8.377   1.00 14.19 ? 70  PHE   A CB  1 
ATOM   552  C  CG  . PHE   A 1 70  ? 4.268   8.402   8.356   1.00 13.65 ? 70  PHE   A CG  1 
ATOM   553  C  CD1 . PHE   A 1 70  ? 5.097   7.299   8.547   1.00 16.62 ? 70  PHE   A CD1 1 
ATOM   554  C  CD2 . PHE   A 1 70  ? 2.934   8.200   8.008   1.00 15.37 ? 70  PHE   A CD2 1 
ATOM   555  C  CE1 . PHE   A 1 70  ? 4.578   6.021   8.447   1.00 15.66 ? 70  PHE   A CE1 1 
ATOM   556  C  CE2 . PHE   A 1 70  ? 2.416   6.916   7.897   1.00 14.55 ? 70  PHE   A CE2 1 
ATOM   557  C  CZ  . PHE   A 1 70  ? 3.244   5.819   8.122   1.00 15.94 ? 70  PHE   A CZ  1 
ATOM   558  N  N   . ASP   A 1 71  ? 4.759   12.370  6.503   1.00 16.90 ? 71  ASP   A N   1 
ATOM   559  C  CA  . ASP   A 1 71  ? 4.800   13.823  6.582   1.00 16.98 ? 71  ASP   A CA  1 
ATOM   560  C  C   . ASP   A 1 71  ? 4.564   14.247  8.035   1.00 18.04 ? 71  ASP   A C   1 
ATOM   561  O  O   . ASP   A 1 71  ? 3.465   14.083  8.551   1.00 23.29 ? 71  ASP   A O   1 
ATOM   562  C  CB  . ASP   A 1 71  ? 3.704   14.396  5.687   1.00 21.09 ? 71  ASP   A CB  1 
ATOM   563  C  CG  . ASP   A 1 71  ? 3.584   15.899  5.818   1.00 22.14 ? 71  ASP   A CG  1 
ATOM   564  O  OD1 . ASP   A 1 71  ? 4.441   16.508  6.437   1.00 25.27 ? 71  ASP   A OD1 1 
ATOM   565  O  OD2 . ASP   A 1 71  ? 2.609   16.451  5.302   1.00 34.10 ? 71  ASP   A OD2 1 
ATOM   566  N  N   . ASP   A 1 72  ? 5.570   14.824  8.705   1.00 17.66 ? 72  ASP   A N   1 
ATOM   567  C  CA  . ASP   A 1 72  ? 5.461   15.194  10.114  1.00 17.01 ? 72  ASP   A CA  1 
ATOM   568  C  C   . ASP   A 1 72  ? 5.568   16.721  10.214  1.00 23.04 ? 72  ASP   A C   1 
ATOM   569  O  O   . ASP   A 1 72  ? 6.093   17.206  11.230  1.00 26.81 ? 72  ASP   A O   1 
ATOM   570  C  CB  . ASP   A 1 72  ? 6.606   14.565  10.931  1.00 21.25 ? 72  ASP   A CB  1 
ATOM   571  C  CG  . ASP   A 1 72  ? 8.012   15.005  10.532  1.00 23.62 ? 72  ASP   A CG  1 
ATOM   572  O  OD1 . ASP   A 1 72  ? 8.174   15.596  9.421   1.00 28.81 ? 72  ASP   A OD1 1 
ATOM   573  O  OD2 . ASP   A 1 72  ? 8.950   14.700  11.292  1.00 24.32 ? 72  ASP   A OD2 1 
ATOM   574  N  N   . SER   A 1 73  ? 5.118   17.458  9.167   1.00 20.37 ? 73  SER   A N   1 
ATOM   575  C  CA  . SER   A 1 73  ? 5.157   18.923  9.115   1.00 24.86 ? 73  SER   A CA  1 
ATOM   576  C  C   . SER   A 1 73  ? 3.905   19.527  9.770   1.00 30.11 ? 73  SER   A C   1 
ATOM   577  O  O   . SER   A 1 73  ? 3.783   20.740  9.900   1.00 29.75 ? 73  SER   A O   1 
ATOM   578  C  CB  . SER   A 1 73  ? 5.293   19.401  7.672   1.00 27.03 ? 73  SER   A CB  1 
ATOM   579  O  OG  . SER   A 1 73  ? 4.104   19.118  6.920   1.00 24.59 ? 73  SER   A OG  1 
ATOM   580  N  N   . GLN   A 1 74  ? 2.939   18.696  10.141  1.00 31.18 ? 74  GLN   A N   1 
ATOM   581  C  CA  . GLN   A 1 74  ? 1.720   19.135  10.817  1.00 34.46 ? 74  GLN   A CA  1 
ATOM   582  C  C   . GLN   A 1 74  ? 1.368   18.068  11.841  1.00 27.75 ? 74  GLN   A C   1 
ATOM   583  O  O   . GLN   A 1 74  ? 1.887   16.967  11.701  1.00 23.31 ? 74  GLN   A O   1 
ATOM   584  C  CB  . GLN   A 1 74  ? 0.548   19.160  9.834   1.00 34.84 ? 74  GLN   A CB  1 
ATOM   585  C  CG  . GLN   A 1 74  ? 0.522   20.385  8.934   1.00 38.74 ? 74  GLN   A CG  1 
ATOM   586  C  CD  . GLN   A 1 74  ? 0.125   19.973  7.536   1.00 55.51 ? 74  GLN   A CD  1 
ATOM   587  O  OE1 . GLN   A 1 74  ? -1.055  19.937  7.222   1.00 50.57 ? 74  GLN   A OE1 1 
ATOM   588  N  NE2 . GLN   A 1 74  ? 1.108   19.616  6.707   1.00 60.68 ? 74  GLN   A NE2 1 
ATOM   589  N  N   . ASP   A 1 75  ? 0.507   18.390  12.826  1.00 35.09 ? 75  ASP   A N   1 
ATOM   590  C  CA  . ASP   A 1 75  ? 0.067   17.397  13.799  1.00 31.64 ? 75  ASP   A CA  1 
ATOM   591  C  C   . ASP   A 1 75  ? -0.949  16.472  13.148  1.00 32.35 ? 75  ASP   A C   1 
ATOM   592  O  O   . ASP   A 1 75  ? -2.163  16.736  13.141  1.00 50.36 ? 75  ASP   A O   1 
ATOM   593  C  CB  . ASP   A 1 75  ? -0.481  17.983  15.101  1.00 51.09 ? 75  ASP   A CB  1 
ATOM   594  C  CG  . ASP   A 1 75  ? 0.519   17.983  16.253  1.00 54.39 ? 75  ASP   A CG  1 
ATOM   595  O  OD1 . ASP   A 1 75  ? 1.482   17.147  16.268  1.00 45.49 ? 75  ASP   A OD1 1 
ATOM   596  O  OD2 . ASP   A 1 75  ? 0.350   18.847  17.138  1.00 60.06 ? 75  ASP   A OD2 1 
ATOM   597  N  N   . LYS   A 1 76  ? -0.436  15.385  12.604  1.00 27.50 ? 76  LYS   A N   1 
ATOM   598  C  CA  . LYS   A 1 76  ? -1.271  14.447  11.869  1.00 27.09 ? 76  LYS   A CA  1 
ATOM   599  C  C   . LYS   A 1 76  ? -1.376  13.141  12.667  1.00 31.22 ? 76  LYS   A C   1 
ATOM   600  O  O   . LYS   A 1 76  ? -2.387  12.835  13.300  1.00 53.52 ? 76  LYS   A O   1 
ATOM   601  C  CB  . LYS   A 1 76  ? -0.689  14.226  10.460  1.00 32.21 ? 76  LYS   A CB  1 
ATOM   602  C  CG  . LYS   A 1 76  ? -1.139  15.231  9.389   1.00 40.32 ? 76  LYS   A CG  1 
ATOM   603  C  CD  . LYS   A 1 76  ? -0.230  15.212  8.139   1.00 41.58 ? 76  LYS   A CD  1 
ATOM   604  C  CE  . LYS   A 1 76  ? -0.422  16.354  7.148   1.00 48.84 ? 76  LYS   A CE  1 
ATOM   605  N  NZ  . LYS   A 1 76  ? -1.542  16.072  6.226   1.00 53.77 ? 76  LYS   A NZ  1 
ATOM   606  N  N   . ALA   A 1 77  ? -0.298  12.386  12.674  1.00 27.91 ? 77  ALA   A N   1 
ATOM   607  C  CA  . ALA   A 1 77  ? -0.264  11.064  13.278  1.00 21.20 ? 77  ALA   A CA  1 
ATOM   608  C  C   . ALA   A 1 77  ? 0.485   11.184  14.608  1.00 18.04 ? 77  ALA   A C   1 
ATOM   609  O  O   . ALA   A 1 77  ? 1.699   11.468  14.596  1.00 25.12 ? 77  ALA   A O   1 
ATOM   610  C  CB  . ALA   A 1 77  ? 0.479   10.236  12.282  1.00 22.27 ? 77  ALA   A CB  1 
ATOM   611  N  N   . VAL   A 1 78  ? -0.208  11.114  15.742  1.00 18.39 ? 78  VAL   A N   1 
ATOM   612  C  CA  . VAL   A 1 78  ? 0.440   11.363  17.034  1.00 19.70 ? 78  VAL   A CA  1 
ATOM   613  C  C   . VAL   A 1 78  ? 0.182   10.252  18.051  1.00 21.43 ? 78  VAL   A C   1 
ATOM   614  O  O   . VAL   A 1 78  ? -0.837  9.551   18.086  1.00 18.85 ? 78  VAL   A O   1 
ATOM   615  C  CB  . VAL   A 1 78  ? 0.090   12.729  17.645  1.00 23.37 ? 78  VAL   A CB  1 
ATOM   616  C  CG1 . VAL   A 1 78  ? 0.238   13.915  16.691  1.00 30.51 ? 78  VAL   A CG1 1 
ATOM   617  C  CG2 . VAL   A 1 78  ? -1.310  12.630  18.131  1.00 22.88 ? 78  VAL   A CG2 1 
ATOM   618  N  N   . LEU   A 1 79  ? 1.189   10.087  18.901  1.00 15.76 ? 79  LEU   A N   1 
ATOM   619  C  CA  . LEU   A 1 79  ? 1.153   9.230   20.056  1.00 15.88 ? 79  LEU   A CA  1 
ATOM   620  C  C   . LEU   A 1 79  ? 1.159   10.122  21.285  1.00 16.06 ? 79  LEU   A C   1 
ATOM   621  O  O   . LEU   A 1 79  ? 1.987   11.024  21.371  1.00 16.43 ? 79  LEU   A O   1 
ATOM   622  C  CB  . LEU   A 1 79  ? 2.441   8.395   19.995  1.00 17.45 ? 79  LEU   A CB  1 
ATOM   623  C  CG  . LEU   A 1 79  ? 2.545   7.313   21.045  1.00 17.62 ? 79  LEU   A CG  1 
ATOM   624  C  CD1 . LEU   A 1 79  ? 1.460   6.260   20.861  1.00 19.86 ? 79  LEU   A CD1 1 
ATOM   625  C  CD2 . LEU   A 1 79  ? 3.936   6.711   20.980  1.00 16.99 ? 79  LEU   A CD2 1 
ATOM   626  N  N   . LYS   A 1 80  ? 0.271   9.869   22.230  1.00 16.32 ? 80  LYS   A N   1 
ATOM   627  C  CA  . LYS   A 1 80  ? 0.223   10.569  23.505  1.00 17.63 ? 80  LYS   A CA  1 
ATOM   628  C  C   . LYS   A 1 80  ? -0.335  9.614   24.554  1.00 16.64 ? 80  LYS   A C   1 
ATOM   629  O  O   . LYS   A 1 80  ? -0.604  8.423   24.267  1.00 15.74 ? 80  LYS   A O   1 
ATOM   630  C  CB  . LYS   A 1 80  ? -0.590  11.849  23.418  1.00 23.87 ? 80  LYS   A CB  1 
ATOM   631  C  CG  . LYS   A 1 80  ? -2.064  11.714  23.130  1.00 24.98 ? 80  LYS   A CG  1 
ATOM   632  C  CD  . LYS   A 1 80  ? -2.611  13.145  22.916  1.00 29.80 ? 80  LYS   A CD  1 
ATOM   633  N  N   . GLY   A 1 81  ? -0.405  10.085  25.792  1.00 18.64 ? 81  GLY   A N   1 
ATOM   634  C  CA  . GLY   A 1 81  ? -0.942  9.255   26.850  1.00 19.46 ? 81  GLY   A CA  1 
ATOM   635  C  C   . GLY   A 1 81  ? 0.087   8.203   27.185  1.00 18.36 ? 81  GLY   A C   1 
ATOM   636  O  O   . GLY   A 1 81  ? 1.292   8.417   27.005  1.00 18.09 ? 81  GLY   A O   1 
ATOM   637  N  N   . GLY   A 1 82  ? -0.398  7.099   27.737  1.00 21.57 ? 82  GLY   A N   1 
ATOM   638  C  CA  . GLY   A 1 82  ? 0.508   6.089   28.274  1.00 23.39 ? 82  GLY   A CA  1 
ATOM   639  C  C   . GLY   A 1 82  ? 1.448   6.708   29.304  1.00 18.59 ? 82  GLY   A C   1 
ATOM   640  O  O   . GLY   A 1 82  ? 0.980   7.413   30.207  1.00 25.73 ? 82  GLY   A O   1 
ATOM   641  N  N   . PRO   A 1 83  ? 2.795   6.538   29.181  1.00 20.58 ? 83  PRO   A N   1 
ATOM   642  C  CA  . PRO   A 1 83  ? 3.708   7.150   30.142  1.00 18.32 ? 83  PRO   A CA  1 
ATOM   643  C  C   . PRO   A 1 83  ? 4.127   8.567   29.731  1.00 19.06 ? 83  PRO   A C   1 
ATOM   644  O  O   . PRO   A 1 83  ? 4.918   9.170   30.440  1.00 23.77 ? 83  PRO   A O   1 
ATOM   645  C  CB  . PRO   A 1 83  ? 4.963   6.262   29.968  1.00 19.86 ? 83  PRO   A CB  1 
ATOM   646  C  CG  . PRO   A 1 83  ? 4.952   5.921   28.463  1.00 15.26 ? 83  PRO   A CG  1 
ATOM   647  C  CD  . PRO   A 1 83  ? 3.477   5.688   28.182  1.00 16.17 ? 83  PRO   A CD  1 
ATOM   648  N  N   . LEU   A 1 84  ? 3.632   9.055   28.577  1.00 19.23 ? 84  LEU   A N   1 
ATOM   649  C  CA  . LEU   A 1 84  ? 4.142   10.284  27.977  1.00 15.74 ? 84  LEU   A CA  1 
ATOM   650  C  C   . LEU   A 1 84  ? 3.444   11.529  28.506  1.00 17.13 ? 84  LEU   A C   1 
ATOM   651  O  O   . LEU   A 1 84  ? 2.241   11.520  28.781  1.00 22.51 ? 84  LEU   A O   1 
ATOM   652  C  CB  . LEU   A 1 84  ? 3.929   10.234  26.467  1.00 14.66 ? 84  LEU   A CB  1 
ATOM   653  C  CG  . LEU   A 1 84  ? 4.466   8.986   25.748  1.00 12.86 ? 84  LEU   A CG  1 
ATOM   654  C  CD1 . LEU   A 1 84  ? 3.996   8.909   24.302  1.00 15.24 ? 84  LEU   A CD1 1 
ATOM   655  C  CD2 . LEU   A 1 84  ? 6.000   8.975   25.826  1.00 16.62 ? 84  LEU   A CD2 1 
ATOM   656  N  N   . ASP   A 1 85  ? 4.203   12.630  28.500  1.00 20.00 ? 85  ASP   A N   1 
ATOM   657  C  CA  . ASP   A 1 85  ? 3.708   13.990  28.690  1.00 22.95 ? 85  ASP   A CA  1 
ATOM   658  C  C   . ASP   A 1 85  ? 3.764   14.650  27.326  1.00 23.50 ? 85  ASP   A C   1 
ATOM   659  O  O   . ASP   A 1 85  ? 4.793   14.601  26.658  1.00 35.98 ? 85  ASP   A O   1 
ATOM   660  C  CB  . ASP   A 1 85  ? 4.692   14.810  29.528  1.00 35.65 ? 85  ASP   A CB  1 
ATOM   661  C  CG  . ASP   A 1 85  ? 4.708   14.354  30.962  1.00 45.79 ? 85  ASP   A CG  1 
ATOM   662  O  OD1 . ASP   A 1 85  ? 3.681   13.756  31.399  1.00 49.58 ? 85  ASP   A OD1 1 
ATOM   663  O  OD2 . ASP   A 1 85  ? 5.748   14.584  31.625  1.00 52.03 ? 85  ASP   A OD2 1 
ATOM   664  N  N   . GLY   A 1 86  ? 2.711   15.358  26.943  1.00 29.39 ? 86  GLY   A N   1 
ATOM   665  C  CA  . GLY   A 1 86  ? 2.687   15.986  25.637  1.00 29.01 ? 86  GLY   A CA  1 
ATOM   666  C  C   . GLY   A 1 86  ? 2.497   14.995  24.476  1.00 26.83 ? 86  GLY   A C   1 
ATOM   667  O  O   . GLY   A 1 86  ? 2.055   13.833  24.602  1.00 27.81 ? 86  GLY   A O   1 
ATOM   668  N  N   . THR   A 1 87  ? 2.892   15.488  23.314  1.00 19.68 ? 87  THR   A N   1 
ATOM   669  C  CA  . THR   A 1 87  ? 2.439   14.975  22.043  1.00 21.52 ? 87  THR   A CA  1 
ATOM   670  C  C   . THR   A 1 87  ? 3.662   14.604  21.225  1.00 16.87 ? 87  THR   A C   1 
ATOM   671  O  O   . THR   A 1 87  ? 4.611   15.397  21.143  1.00 16.49 ? 87  THR   A O   1 
ATOM   672  C  CB  . THR   A 1 87  ? 1.700   16.102  21.316  1.00 27.42 ? 87  THR   A CB  1 
ATOM   673  O  OG1 . THR   A 1 87  ? 0.454   16.094  22.002  1.00 35.61 ? 87  THR   A OG1 1 
ATOM   674  C  CG2 . THR   A 1 87  ? 1.475   15.774  19.853  1.00 27.00 ? 87  THR   A CG2 1 
ATOM   675  N  N   . TYR   A 1 88  ? 3.650   13.395  20.669  1.00 16.92 ? 88  TYR   A N   1 
ATOM   676  C  CA  . TYR   A 1 88  ? 4.770   12.888  19.879  1.00 13.56 ? 88  TYR   A CA  1 
ATOM   677  C  C   . TYR   A 1 88  ? 4.296   12.595  18.461  1.00 14.06 ? 88  TYR   A C   1 
ATOM   678  O  O   . TYR   A 1 88  ? 3.358   11.823  18.290  1.00 17.22 ? 88  TYR   A O   1 
ATOM   679  C  CB  . TYR   A 1 88  ? 5.490   11.670  20.470  1.00 13.18 ? 88  TYR   A CB  1 
ATOM   680  C  CG  . TYR   A 1 88  ? 6.176   11.905  21.797  1.00 13.11 ? 88  TYR   A CG  1 
ATOM   681  C  CD1 . TYR   A 1 88  ? 5.506   12.287  22.960  1.00 13.38 ? 88  TYR   A CD1 1 
ATOM   682  C  CD2 . TYR   A 1 88  ? 7.567   11.771  21.866  1.00 12.46 ? 88  TYR   A CD2 1 
ATOM   683  C  CE1 . TYR   A 1 88  ? 6.188   12.509  24.178  1.00 13.40 ? 88  TYR   A CE1 1 
ATOM   684  C  CE2 . TYR   A 1 88  ? 8.225   11.933  23.078  1.00 13.10 ? 88  TYR   A CE2 1 
ATOM   685  C  CZ  . TYR   A 1 88  ? 7.558   12.245  24.242  1.00 12.23 ? 88  TYR   A CZ  1 
ATOM   686  O  OH  . TYR   A 1 88  ? 8.223   12.376  25.435  1.00 15.58 ? 88  TYR   A OH  1 
ATOM   687  N  N   . ARG   A 1 89  ? 4.966   13.107  17.455  1.00 13.21 ? 89  ARG   A N   1 
ATOM   688  C  CA  . ARG   A 1 89  ? 4.558   13.053  16.064  1.00 13.50 ? 89  ARG   A CA  1 
ATOM   689  C  C   . ARG   A 1 89  ? 5.262   11.892  15.355  1.00 12.73 ? 89  ARG   A C   1 
ATOM   690  O  O   . ARG   A 1 89  ? 6.492   11.759  15.443  1.00 12.28 ? 89  ARG   A O   1 
ATOM   691  C  CB  . ARG   A 1 89  ? 4.883   14.360  15.337  1.00 18.35 ? 89  ARG   A CB  1 
ATOM   692  C  CG  . ARG   A 1 89  ? 4.044   14.615  14.116  1.00 24.09 ? 89  ARG   A CG  1 
ATOM   693  C  CD  . ARG   A 1 89  ? 4.402   16.074  13.774  1.00 23.92 ? 89  ARG   A CD  1 
ATOM   694  N  NE  . ARG   A 1 89  ? 3.637   17.071  14.495  1.00 22.69 ? 89  ARG   A NE  1 
ATOM   695  C  CZ  . ARG   A 1 89  ? 3.776   18.397  14.322  1.00 23.93 ? 89  ARG   A CZ  1 
ATOM   696  N  NH1 . ARG   A 1 89  ? 4.614   18.838  13.396  1.00 29.54 ? 89  ARG   A NH1 1 
ATOM   697  N  NH2 . ARG   A 1 89  ? 3.043   19.277  15.022  1.00 29.77 ? 89  ARG   A NH2 1 
ATOM   698  N  N   . LEU   A 1 90  ? 4.504   11.076  14.617  1.00 14.37 ? 90  LEU   A N   1 
ATOM   699  C  CA  . LEU   A 1 90  ? 5.145   9.969   13.920  1.00 13.19 ? 90  LEU   A CA  1 
ATOM   700  C  C   . LEU   A 1 90  ? 5.977   10.533  12.766  1.00 12.36 ? 90  LEU   A C   1 
ATOM   701  O  O   . LEU   A 1 90  ? 5.480   11.264  11.898  1.00 16.55 ? 90  LEU   A O   1 
ATOM   702  C  CB  . LEU   A 1 90  ? 4.022   9.119   13.318  1.00 14.31 ? 90  LEU   A CB  1 
ATOM   703  C  CG  . LEU   A 1 90  ? 4.472   7.908   12.459  1.00 13.73 ? 90  LEU   A CG  1 
ATOM   704  C  CD1 . LEU   A 1 90  ? 5.191   6.815   13.272  1.00 15.85 ? 90  LEU   A CD1 1 
ATOM   705  C  CD2 . LEU   A 1 90  ? 3.236   7.284   11.830  1.00 14.80 ? 90  LEU   A CD2 1 
ATOM   706  N  N   . ILE   A 1 91  ? 7.229   10.075  12.675  1.00 12.24 ? 91  ILE   A N   1 
ATOM   707  C  CA  . ILE   A 1 91  ? 8.142   10.431  11.594  1.00 13.97 ? 91  ILE   A CA  1 
ATOM   708  C  C   . ILE   A 1 91  ? 8.416   9.276   10.628  1.00 14.87 ? 91  ILE   A C   1 
ATOM   709  O  O   . ILE   A 1 91  ? 8.459   9.458   9.422   1.00 13.78 ? 91  ILE   A O   1 
ATOM   710  C  CB  . ILE   A 1 91  ? 9.454   11.096  12.069  1.00 15.50 ? 91  ILE   A CB  1 
ATOM   711  C  CG1 . ILE   A 1 91  ? 10.357  11.454  10.883  1.00 14.88 ? 91  ILE   A CG1 1 
ATOM   712  C  CG2 . ILE   A 1 91  ? 10.193  10.223  13.096  1.00 15.49 ? 91  ILE   A CG2 1 
ATOM   713  C  CD1 . ILE   A 1 91  ? 11.488  12.352  11.317  1.00 18.25 ? 91  ILE   A CD1 1 
ATOM   714  N  N   . GLN   A 1 92  ? 8.549   8.049   11.155  1.00 12.47 ? 92  GLN   A N   1 
ATOM   715  C  CA  . GLN   A 1 92  ? 8.807   6.932   10.263  1.00 13.62 ? 92  GLN   A CA  1 
ATOM   716  C  C   . GLN   A 1 92  ? 8.574   5.646   11.043  1.00 11.33 ? 92  GLN   A C   1 
ATOM   717  O  O   . GLN   A 1 92  ? 8.532   5.680   12.267  1.00 12.73 ? 92  GLN   A O   1 
ATOM   718  C  CB  . GLN   A 1 92  ? 10.261  6.942   9.763   1.00 14.62 ? 92  GLN   A CB  1 
ATOM   719  C  CG  . GLN   A 1 92  ? 11.314  6.899   10.888  1.00 15.40 ? 92  GLN   A CG  1 
ATOM   720  C  CD  . GLN   A 1 92  ? 12.046  5.573   10.925  1.00 12.66 ? 92  GLN   A CD  1 
ATOM   721  O  OE1 . GLN   A 1 92  ? 11.473  4.527   11.217  1.00 12.92 ? 92  GLN   A OE1 1 
ATOM   722  N  NE2 . GLN   A 1 92  ? 13.339  5.575   10.617  1.00 17.98 ? 92  GLN   A NE2 1 
ATOM   723  N  N   . PHE   A 1 93  ? 8.366   4.521   10.323  1.00 11.70 ? 93  PHE   A N   1 
ATOM   724  C  CA  . PHE   A 1 93  ? 8.519   3.259   11.011  1.00 13.45 ? 93  PHE   A CA  1 
ATOM   725  C  C   . PHE   A 1 93  ? 9.481   2.389   10.215  1.00 11.23 ? 93  PHE   A C   1 
ATOM   726  O  O   . PHE   A 1 93  ? 9.718   2.569   9.032   1.00 11.16 ? 93  PHE   A O   1 
ATOM   727  C  CB  . PHE   A 1 93  ? 7.171   2.537   11.236  1.00 11.93 ? 93  PHE   A CB  1 
ATOM   728  C  CG  . PHE   A 1 93  ? 6.401   2.045   10.035  1.00 11.81 ? 93  PHE   A CG  1 
ATOM   729  C  CD1 . PHE   A 1 93  ? 6.825   0.903   9.322   1.00 12.09 ? 93  PHE   A CD1 1 
ATOM   730  C  CD2 . PHE   A 1 93  ? 5.236   2.728   9.607   1.00 13.44 ? 93  PHE   A CD2 1 
ATOM   731  C  CE1 . PHE   A 1 93  ? 6.105   0.443   8.217   1.00 12.71 ? 93  PHE   A CE1 1 
ATOM   732  C  CE2 . PHE   A 1 93  ? 4.509   2.255   8.507   1.00 13.90 ? 93  PHE   A CE2 1 
ATOM   733  C  CZ  . PHE   A 1 93  ? 4.921   1.099   7.849   1.00 12.36 ? 93  PHE   A CZ  1 
ATOM   734  N  N   . HIS   A 1 94  ? 9.979   1.354   10.914  1.00 11.86 ? 94  HIS   A N   1 
ATOM   735  C  CA  . HIS   A 1 94  ? 10.874  0.395   10.248  1.00 11.43 ? 94  HIS   A CA  1 
ATOM   736  C  C   . HIS   A 1 94  ? 10.723  -0.899  11.052  1.00 10.39 ? 94  HIS   A C   1 
ATOM   737  O  O   . HIS   A 1 94  ? 10.144  -0.895  12.140  1.00 12.89 ? 94  HIS   A O   1 
ATOM   738  C  CB  . HIS   A 1 94  ? 12.365  0.870   10.219  1.00 10.78 ? 94  HIS   A CB  1 
ATOM   739  C  CG  . HIS   A 1 94  ? 12.834  1.116   11.597  1.00 10.87 ? 94  HIS   A CG  1 
ATOM   740  N  ND1 . HIS   A 1 94  ? 12.642  2.327   12.256  1.00 11.65 ? 94  HIS   A ND1 1 
ATOM   741  C  CD2 . HIS   A 1 94  ? 13.472  0.312   12.495  1.00 11.19 ? 94  HIS   A CD2 1 
ATOM   742  C  CE1 . HIS   A 1 94  ? 13.043  2.221   13.512  1.00 10.86 ? 94  HIS   A CE1 1 
ATOM   743  N  NE2 . HIS   A 1 94  ? 13.540  0.946   13.689  1.00 11.89 ? 94  HIS   A NE2 1 
ATOM   744  N  N   . PHE   A 1 95  ? 11.418  -1.945  10.592  1.00 11.97 ? 95  PHE   A N   1 
ATOM   745  C  CA  . PHE   A 1 95  ? 11.440  -3.207  11.327  1.00 11.08 ? 95  PHE   A CA  1 
ATOM   746  C  C   . PHE   A 1 95  ? 12.889  -3.674  11.535  1.00 11.55 ? 95  PHE   A C   1 
ATOM   747  O  O   . PHE   A 1 95  ? 13.794  -3.264  10.814  1.00 13.15 ? 95  PHE   A O   1 
ATOM   748  C  CB  . PHE   A 1 95  ? 10.753  -4.289  10.475  1.00 11.40 ? 95  PHE   A CB  1 
ATOM   749  C  CG  . PHE   A 1 95  ? 9.274   -4.024  10.143  1.00 11.00 ? 95  PHE   A CG  1 
ATOM   750  C  CD1 . PHE   A 1 95  ? 8.901   -3.187  9.089   1.00 12.95 ? 95  PHE   A CD1 1 
ATOM   751  C  CD2 . PHE   A 1 95  ? 8.262   -4.702  10.845  1.00 11.69 ? 95  PHE   A CD2 1 
ATOM   752  C  CE1 . PHE   A 1 95  ? 7.563   -2.953  8.763   1.00 11.81 ? 95  PHE   A CE1 1 
ATOM   753  C  CE2 . PHE   A 1 95  ? 6.934   -4.474  10.524  1.00 12.90 ? 95  PHE   A CE2 1 
ATOM   754  C  CZ  . PHE   A 1 95  ? 6.592   -3.666  9.451   1.00 13.53 ? 95  PHE   A CZ  1 
ATOM   755  N  N   . HIS   A 1 96  ? 12.993  -4.649  12.457  1.00 11.21 ? 96  HIS   A N   1 
ATOM   756  C  CA  . HIS   A 1 96  ? 14.207  -5.459  12.575  1.00 11.37 ? 96  HIS   A CA  1 
ATOM   757  C  C   . HIS   A 1 96  ? 13.791  -6.927  12.440  1.00 13.24 ? 96  HIS   A C   1 
ATOM   758  O  O   . HIS   A 1 96  ? 12.683  -7.286  12.889  1.00 12.56 ? 96  HIS   A O   1 
ATOM   759  C  CB  . HIS   A 1 96  ? 14.833  -5.288  13.949  1.00 12.74 ? 96  HIS   A CB  1 
ATOM   760  C  CG  . HIS   A 1 96  ? 15.113  -3.852  14.262  1.00 11.44 ? 96  HIS   A CG  1 
ATOM   761  N  ND1 . HIS   A 1 96  ? 16.382  -3.296  14.097  1.00 11.60 ? 96  HIS   A ND1 1 
ATOM   762  C  CD2 . HIS   A 1 96  ? 14.302  -2.853  14.673  1.00 11.47 ? 96  HIS   A CD2 1 
ATOM   763  C  CE1 . HIS   A 1 96  ? 16.359  -2.010  14.457  1.00 11.82 ? 96  HIS   A CE1 1 
ATOM   764  N  NE2 . HIS   A 1 96  ? 15.065  -1.660  14.807  1.00 10.61 ? 96  HIS   A NE2 1 
ATOM   765  N  N   . TRP   A 1 97  ? 14.623  -7.746  11.761  1.00 12.67 ? 97  TRP   A N   1 
ATOM   766  C  CA  . TRP   A 1 97  ? 14.174  -9.124  11.564  1.00 11.53 ? 97  TRP   A CA  1 
ATOM   767  C  C   . TRP   A 1 97  ? 15.377  -10.038 11.489  1.00 10.90 ? 97  TRP   A C   1 
ATOM   768  O  O   . TRP   A 1 97  ? 16.530  -9.583  11.340  1.00 12.56 ? 97  TRP   A O   1 
ATOM   769  C  CB  . TRP   A 1 97  ? 13.251  -9.268  10.344  1.00 12.73 ? 97  TRP   A CB  1 
ATOM   770  C  CG  . TRP   A 1 97  ? 13.865  -8.874  9.039   1.00 12.69 ? 97  TRP   A CG  1 
ATOM   771  C  CD1 . TRP   A 1 97  ? 14.620  -9.651  8.203   1.00 16.17 ? 97  TRP   A CD1 1 
ATOM   772  C  CD2 . TRP   A 1 97  ? 13.971  -7.541  8.509   1.00 12.05 ? 97  TRP   A CD2 1 
ATOM   773  N  NE1 . TRP   A 1 97  ? 15.056  -8.970  7.086   1.00 13.14 ? 97  TRP   A NE1 1 
ATOM   774  C  CE2 . TRP   A 1 97  ? 14.658  -7.648  7.266   1.00 13.42 ? 97  TRP   A CE2 1 
ATOM   775  C  CE3 . TRP   A 1 97  ? 13.477  -6.268  8.931   1.00 11.00 ? 97  TRP   A CE3 1 
ATOM   776  C  CZ2 . TRP   A 1 97  ? 14.866  -6.550  6.425   1.00 13.69 ? 97  TRP   A CZ2 1 
ATOM   777  C  CZ3 . TRP   A 1 97  ? 13.724  -5.189  8.089   1.00 13.85 ? 97  TRP   A CZ3 1 
ATOM   778  C  CH2 . TRP   A 1 97  ? 14.314  -5.346  6.836   1.00 12.55 ? 97  TRP   A CH2 1 
ATOM   779  N  N   . GLY   A 1 98  ? 15.065  -11.345 11.499  1.00 11.84 ? 98  GLY   A N   1 
ATOM   780  C  CA  . GLY   A 1 98  ? 16.109  -12.361 11.535  1.00 14.23 ? 98  GLY   A CA  1 
ATOM   781  C  C   . GLY   A 1 98  ? 16.360  -13.047 10.207  1.00 12.91 ? 98  GLY   A C   1 
ATOM   782  O  O   . GLY   A 1 98  ? 15.633  -12.885 9.239   1.00 13.80 ? 98  GLY   A O   1 
ATOM   783  N  N   . SER   A 1 99  ? 17.360  -13.947 10.205  1.00 13.90 ? 99  SER   A N   1 
ATOM   784  C  CA  . SER   A 1 99  ? 17.602  -14.839 9.069   1.00 13.84 ? 99  SER   A CA  1 
ATOM   785  C  C   . SER   A 1 99  ? 16.703  -16.087 9.175   1.00 13.74 ? 99  SER   A C   1 
ATOM   786  O  O   . SER   A 1 99  ? 16.547  -16.778 8.169   1.00 18.85 ? 99  SER   A O   1 
ATOM   787  C  CB  . SER   A 1 99  ? 19.063  -15.287 9.044   1.00 16.84 ? 99  SER   A CB  1 
ATOM   788  O  OG  . SER   A 1 99  ? 19.465  -15.746 10.337  1.00 18.23 ? 99  SER   A OG  1 
ATOM   789  N  N   . LEU   A 1 100 ? 16.132  -16.316 10.363  1.00 13.78 ? 100 LEU   A N   1 
ATOM   790  C  CA  . LEU   A 1 100 ? 15.292  -17.470 10.650  1.00 14.93 ? 100 LEU   A CA  1 
ATOM   791  C  C   . LEU   A 1 100 ? 14.168  -16.965 11.560  1.00 15.19 ? 100 LEU   A C   1 
ATOM   792  O  O   . LEU   A 1 100 ? 14.337  -15.972 12.270  1.00 14.92 ? 100 LEU   A O   1 
ATOM   793  C  CB  . LEU   A 1 100 ? 16.092  -18.517 11.429  1.00 21.42 ? 100 LEU   A CB  1 
ATOM   794  C  CG  . LEU   A 1 100 ? 17.411  -18.939 10.805  1.00 25.52 ? 100 LEU   A CG  1 
ATOM   795  C  CD1 . LEU   A 1 100 ? 18.342  -19.476 11.896  1.00 35.20 ? 100 LEU   A CD1 1 
ATOM   796  C  CD2 . LEU   A 1 100 ? 17.092  -20.046 9.836   1.00 29.23 ? 100 LEU   A CD2 1 
ATOM   797  N  N   . ASP   A 1 101 ? 13.032  -17.672 11.600  1.00 14.80 ? 101 ASP   A N   1 
ATOM   798  C  CA  . ASP   A 1 101 ? 11.948  -17.188 12.449  1.00 15.28 ? 101 ASP   A CA  1 
ATOM   799  C  C   . ASP   A 1 101 ? 12.298  -17.132 13.938  1.00 16.59 ? 101 ASP   A C   1 
ATOM   800  O  O   . ASP   A 1 101 ? 11.660  -16.390 14.686  1.00 18.05 ? 101 ASP   A O   1 
ATOM   801  C  CB  . ASP   A 1 101 ? 10.715  -18.065 12.284  1.00 17.21 ? 101 ASP   A CB  1 
ATOM   802  C  CG  . ASP   A 1 101 ? 10.164  -18.132 10.857  1.00 21.57 ? 101 ASP   A CG  1 
ATOM   803  O  OD1 . ASP   A 1 101 ? 10.509  -17.306 9.967   1.00 17.64 ? 101 ASP   A OD1 1 
ATOM   804  O  OD2 . ASP   A 1 101 ? 9.325   -19.016 10.643  1.00 28.35 ? 101 ASP   A OD2 1 
ATOM   805  N  N   . GLY   A 1 102 ? 13.306  -17.910 14.406  1.00 15.44 ? 102 GLY   A N   1 
ATOM   806  C  CA  . GLY   A 1 102 ? 13.557  -17.928 15.835  1.00 14.35 ? 102 GLY   A CA  1 
ATOM   807  C  C   . GLY   A 1 102 ? 14.347  -16.728 16.356  1.00 15.35 ? 102 GLY   A C   1 
ATOM   808  O  O   . GLY   A 1 102 ? 14.688  -16.689 17.537  1.00 15.28 ? 102 GLY   A O   1 
ATOM   809  N  N   . GLN   A 1 103 ? 14.625  -15.714 15.509  1.00 14.06 ? 103 GLN   A N   1 
ATOM   810  C  CA  . GLN   A 1 103 ? 15.350  -14.577 16.024  1.00 13.30 ? 103 GLN   A CA  1 
ATOM   811  C  C   . GLN   A 1 103 ? 14.929  -13.382 15.161  1.00 12.22 ? 103 GLN   A C   1 
ATOM   812  O  O   . GLN   A 1 103 ? 14.415  -13.573 14.051  1.00 13.56 ? 103 GLN   A O   1 
ATOM   813  C  CB  . GLN   A 1 103 ? 16.866  -14.799 16.047  1.00 15.86 ? 103 GLN   A CB  1 
ATOM   814  C  CG  . GLN   A 1 103 ? 17.498  -15.025 14.674  1.00 15.45 ? 103 GLN   A CG  1 
ATOM   815  C  CD  . GLN   A 1 103 ? 18.940  -15.477 14.784  1.00 18.62 ? 103 GLN   A CD  1 
ATOM   816  O  OE1 . GLN   A 1 103 ? 19.258  -16.261 15.699  1.00 32.17 ? 103 GLN   A OE1 1 
ATOM   817  N  NE2 . GLN   A 1 103 ? 19.797  -15.070 13.862  1.00 19.59 ? 103 GLN   A NE2 1 
ATOM   818  N  N   . GLY   A 1 104 ? 15.240  -12.146 15.624  1.00 13.41 ? 104 GLY   A N   1 
ATOM   819  C  CA  . GLY   A 1 104 ? 14.923  -10.973 14.803  1.00 13.51 ? 104 GLY   A CA  1 
ATOM   820  C  C   . GLY   A 1 104 ? 14.448  -9.823  15.675  1.00 12.97 ? 104 GLY   A C   1 
ATOM   821  O  O   . GLY   A 1 104 ? 14.695  -8.658  15.286  1.00 15.14 ? 104 GLY   A O   1 
ATOM   822  N  N   . SER   A 1 105 ? 13.772  -10.101 16.813  1.00 12.68 ? 105 SER   A N   1 
ATOM   823  C  CA  . SER   A 1 105 ? 13.351  -8.957  17.615  1.00 12.22 ? 105 SER   A CA  1 
ATOM   824  C  C   . SER   A 1 105 ? 14.569  -8.378  18.335  1.00 11.74 ? 105 SER   A C   1 
ATOM   825  O  O   . SER   A 1 105 ? 15.586  -9.050  18.553  1.00 12.62 ? 105 SER   A O   1 
ATOM   826  C  CB  . SER   A 1 105 ? 12.261  -9.292  18.612  1.00 12.99 ? 105 SER   A CB  1 
ATOM   827  O  OG  . SER   A 1 105 ? 12.670  -10.252 19.593  1.00 12.41 ? 105 SER   A OG  1 
ATOM   828  N  N   . GLU   A 1 106 ? 14.445  -7.130  18.766  1.00 11.27 ? 106 GLU   A N   1 
ATOM   829  C  CA  . GLU   A 1 106 ? 15.465  -6.465  19.564  1.00 9.90  ? 106 GLU   A CA  1 
ATOM   830  C  C   . GLU   A 1 106 ? 15.122  -6.628  21.026  1.00 11.65 ? 106 GLU   A C   1 
ATOM   831  O  O   . GLU   A 1 106 ? 15.891  -7.180  21.812  1.00 12.96 ? 106 GLU   A O   1 
ATOM   832  C  CB  . GLU   A 1 106 ? 15.501  -4.986  19.180  1.00 13.05 ? 106 GLU   A CB  1 
ATOM   833  C  CG  . GLU   A 1 106 ? 15.977  -4.844  17.752  1.00 11.86 ? 106 GLU   A CG  1 
ATOM   834  C  CD  . GLU   A 1 106 ? 16.692  -3.551  17.464  1.00 11.31 ? 106 GLU   A CD  1 
ATOM   835  O  OE1 . GLU   A 1 106 ? 16.094  -2.483  17.716  1.00 11.63 ? 106 GLU   A OE1 1 
ATOM   836  O  OE2 . GLU   A 1 106 ? 17.793  -3.592  16.940  1.00 12.37 ? 106 GLU   A OE2 1 
ATOM   837  N  N   . HIS   A 1 107 ? 13.928  -6.179  21.454  1.00 12.16 ? 107 HIS   A N   1 
ATOM   838  C  CA  . HIS   A 1 107 ? 13.464  -6.530  22.789  1.00 10.18 ? 107 HIS   A CA  1 
ATOM   839  C  C   . HIS   A 1 107 ? 13.224  -8.042  22.821  1.00 9.98  ? 107 HIS   A C   1 
ATOM   840  O  O   . HIS   A 1 107 ? 12.844  -8.635  21.801  1.00 13.25 ? 107 HIS   A O   1 
ATOM   841  C  CB  . HIS   A 1 107 ? 12.195  -5.731  23.169  1.00 10.80 ? 107 HIS   A CB  1 
ATOM   842  C  CG  . HIS   A 1 107 ? 12.559  -4.284  23.318  1.00 11.60 ? 107 HIS   A CG  1 
ATOM   843  N  ND1 . HIS   A 1 107 ? 12.492  -3.403  22.258  1.00 11.06 ? 107 HIS   A ND1 1 
ATOM   844  C  CD2 . HIS   A 1 107 ? 13.041  -3.608  24.387  1.00 11.90 ? 107 HIS   A CD2 1 
ATOM   845  C  CE1 . HIS   A 1 107 ? 12.939  -2.183  22.659  1.00 11.01 ? 107 HIS   A CE1 1 
ATOM   846  N  NE2 . HIS   A 1 107 ? 13.285  -2.272  23.988  1.00 11.23 ? 107 HIS   A NE2 1 
ATOM   847  N  N   . THR   A 1 108 ? 13.376  -8.584  24.021  1.00 11.78 ? 108 THR   A N   1 
ATOM   848  C  CA  . THR   A 1 108 ? 13.006  -9.968  24.249  1.00 10.31 ? 108 THR   A CA  1 
ATOM   849  C  C   . THR   A 1 108 ? 12.050  -9.982  25.453  1.00 12.63 ? 108 THR   A C   1 
ATOM   850  O  O   . THR   A 1 108 ? 11.953  -9.032  26.253  1.00 13.69 ? 108 THR   A O   1 
ATOM   851  C  CB  . THR   A 1 108 ? 14.247  -10.851 24.414  1.00 12.08 ? 108 THR   A CB  1 
ATOM   852  O  OG1 . THR   A 1 108 ? 15.008  -10.321 25.503  1.00 13.16 ? 108 THR   A OG1 1 
ATOM   853  C  CG2 . THR   A 1 108 ? 15.016  -10.983 23.123  1.00 12.31 ? 108 THR   A CG2 1 
ATOM   854  N  N   . VAL   A 1 109 ? 11.290  -11.087 25.581  1.00 12.17 ? 109 VAL   A N   1 
ATOM   855  C  CA  . VAL   A 1 109 ? 10.320  -11.186 26.673  1.00 12.70 ? 109 VAL   A CA  1 
ATOM   856  C  C   . VAL   A 1 109 ? 10.658  -12.472 27.436  1.00 12.48 ? 109 VAL   A C   1 
ATOM   857  O  O   . VAL   A 1 109 ? 10.454  -13.558 26.854  1.00 13.85 ? 109 VAL   A O   1 
ATOM   858  C  CB  . VAL   A 1 109 ? 8.865   -11.180 26.140  1.00 14.78 ? 109 VAL   A CB  1 
ATOM   859  C  CG1 . VAL   A 1 109 ? 7.829   -11.337 27.267  1.00 16.37 ? 109 VAL   A CG1 1 
ATOM   860  C  CG2 . VAL   A 1 109 ? 8.570   -9.902  25.321  1.00 15.41 ? 109 VAL   A CG2 1 
ATOM   861  N  N   . ASP   A 1 110 ? 11.116  -12.360 28.702  1.00 13.25 ? 110 ASP   A N   1 
ATOM   862  C  CA  . ASP   A 1 110 ? 11.656  -13.557 29.362  1.00 14.14 ? 110 ASP   A CA  1 
ATOM   863  C  C   . ASP   A 1 110 ? 12.617  -14.285 28.441  1.00 13.98 ? 110 ASP   A C   1 
ATOM   864  O  O   . ASP   A 1 110 ? 12.554  -15.520 28.378  1.00 15.82 ? 110 ASP   A O   1 
ATOM   865  C  CB  . ASP   A 1 110 ? 10.521  -14.402 29.910  1.00 16.14 ? 110 ASP   A CB  1 
ATOM   866  C  CG  . ASP   A 1 110 ? 9.671   -13.657 30.916  1.00 16.83 ? 110 ASP   A CG  1 
ATOM   867  O  OD1 . ASP   A 1 110 ? 10.190  -12.710 31.597  1.00 17.89 ? 110 ASP   A OD1 1 
ATOM   868  O  OD2 . ASP   A 1 110 ? 8.488   -13.999 31.000  1.00 19.82 ? 110 ASP   A OD2 1 
ATOM   869  N  N   . LYS   A 1 111 ? 13.501  -13.553 27.744  1.00 14.77 ? 111 LYS   A N   1 
ATOM   870  C  CA  . LYS   A 1 111 ? 14.508  -14.121 26.852  1.00 15.45 ? 111 LYS   A CA  1 
ATOM   871  C  C   . LYS   A 1 111 ? 13.940  -14.656 25.537  1.00 12.81 ? 111 LYS   A C   1 
ATOM   872  O  O   . LYS   A 1 111 ? 14.695  -14.991 24.646  1.00 15.39 ? 111 LYS   A O   1 
ATOM   873  C  CB  . LYS   A 1 111 ? 15.398  -15.133 27.580  1.00 16.69 ? 111 LYS   A CB  1 
ATOM   874  C  CG  . LYS   A 1 111 ? 16.142  -14.564 28.785  1.00 20.36 ? 111 LYS   A CG  1 
ATOM   875  C  CD  . LYS   A 1 111 ? 17.050  -13.369 28.420  1.00 21.87 ? 111 LYS   A CD  1 
ATOM   876  C  CE  . LYS   A 1 111 ? 17.791  -12.823 29.629  1.00 23.08 ? 111 LYS   A CE  1 
ATOM   877  N  NZ  . LYS   A 1 111 ? 18.946  -13.649 30.029  1.00 29.62 ? 111 LYS   A NZ  1 
ATOM   878  N  N   . LYS   A 1 112 ? 12.591  -14.677 25.370  1.00 12.28 ? 112 LYS   A N   1 
ATOM   879  C  CA  . LYS   A 1 112 ? 12.017  -15.079 24.085  1.00 15.05 ? 112 LYS   A CA  1 
ATOM   880  C  C   . LYS   A 1 112 ? 12.345  -14.035 23.012  1.00 13.55 ? 112 LYS   A C   1 
ATOM   881  O  O   . LYS   A 1 112 ? 12.051  -12.830 23.216  1.00 13.65 ? 112 LYS   A O   1 
ATOM   882  C  CB  . LYS   A 1 112 ? 10.495  -15.163 24.197  1.00 17.45 ? 112 LYS   A CB  1 
ATOM   883  C  CG  . LYS   A 1 112 ? 9.764   -15.513 22.898  1.00 18.43 ? 112 LYS   A CG  1 
ATOM   884  C  CD  . LYS   A 1 112 ? 8.212   -15.419 22.976  1.00 17.50 ? 112 LYS   A CD  1 
ATOM   885  C  CE  . LYS   A 1 112 ? 7.624   -15.678 21.610  1.00 19.49 ? 112 LYS   A CE  1 
ATOM   886  N  NZ  . LYS   A 1 112 ? 7.841   -17.072 21.184  1.00 20.01 ? 112 LYS   A NZ  1 
ATOM   887  N  N   A LYS   A 1 113 ? 12.939  -14.475 21.905  0.50 15.95 ? 113 LYS   A N   1 
ATOM   888  N  N   B LYS   A 1 113 ? 12.812  -14.515 21.855  0.50 16.10 ? 113 LYS   A N   1 
ATOM   889  C  CA  A LYS   A 1 113 ? 13.051  -13.660 20.695  0.50 14.69 ? 113 LYS   A CA  1 
ATOM   890  C  CA  B LYS   A 1 113 ? 13.081  -13.730 20.646  0.50 14.50 ? 113 LYS   A CA  1 
ATOM   891  C  C   A LYS   A 1 113 ? 11.871  -13.927 19.766  0.50 13.03 ? 113 LYS   A C   1 
ATOM   892  C  C   B LYS   A 1 113 ? 11.985  -13.930 19.597  0.50 13.06 ? 113 LYS   A C   1 
ATOM   893  O  O   A LYS   A 1 113 ? 11.419  -15.064 19.616  0.50 12.97 ? 113 LYS   A O   1 
ATOM   894  O  O   B LYS   A 1 113 ? 11.742  -15.049 19.130  0.50 13.87 ? 113 LYS   A O   1 
ATOM   895  C  CB  A LYS   A 1 113 ? 14.365  -13.939 19.973  0.50 17.01 ? 113 LYS   A CB  1 
ATOM   896  C  CB  B LYS   A 1 113 ? 14.359  -14.242 19.987  0.50 14.49 ? 113 LYS   A CB  1 
ATOM   897  C  CG  A LYS   A 1 113 ? 15.572  -13.596 20.822  0.50 16.01 ? 113 LYS   A CG  1 
ATOM   898  C  CG  B LYS   A 1 113 ? 15.631  -13.968 20.761  0.50 14.95 ? 113 LYS   A CG  1 
ATOM   899  C  CD  A LYS   A 1 113 ? 16.841  -14.228 20.263  0.50 17.57 ? 113 LYS   A CD  1 
ATOM   900  C  CD  B LYS   A 1 113 ? 16.810  -14.466 19.954  0.50 15.91 ? 113 LYS   A CD  1 
ATOM   901  C  CE  A LYS   A 1 113 ? 18.083  -13.667 20.915  0.50 18.34 ? 113 LYS   A CE  1 
ATOM   902  C  CE  B LYS   A 1 113 ? 18.132  -13.963 20.483  0.50 12.91 ? 113 LYS   A CE  1 
ATOM   903  N  NZ  A LYS   A 1 113 ? 19.247  -14.575 20.779  0.50 21.00 ? 113 LYS   A NZ  1 
ATOM   904  N  NZ  B LYS   A 1 113 ? 18.438  -14.539 21.813  0.50 15.39 ? 113 LYS   A NZ  1 
ATOM   905  N  N   . TYR   A 1 114 ? 11.290  -12.835 19.257  1.00 14.32 ? 114 TYR   A N   1 
ATOM   906  C  CA  . TYR   A 1 114 ? 10.339  -12.911 18.164  1.00 12.27 ? 114 TYR   A CA  1 
ATOM   907  C  C   . TYR   A 1 114 ? 10.997  -12.855 16.784  1.00 12.24 ? 114 TYR   A C   1 
ATOM   908  O  O   . TYR   A 1 114 ? 12.195  -12.521 16.634  1.00 14.41 ? 114 TYR   A O   1 
ATOM   909  C  CB  . TYR   A 1 114 ? 9.297   -11.801 18.264  1.00 13.05 ? 114 TYR   A CB  1 
ATOM   910  C  CG  . TYR   A 1 114 ? 8.306   -11.969 19.397  1.00 12.65 ? 114 TYR   A CG  1 
ATOM   911  C  CD1 . TYR   A 1 114 ? 8.612   -11.581 20.695  1.00 13.87 ? 114 TYR   A CD1 1 
ATOM   912  C  CD2 . TYR   A 1 114 ? 7.078   -12.636 19.221  1.00 15.08 ? 114 TYR   A CD2 1 
ATOM   913  C  CE1 . TYR   A 1 114 ? 7.735   -11.737 21.767  1.00 15.06 ? 114 TYR   A CE1 1 
ATOM   914  C  CE2 . TYR   A 1 114 ? 6.190   -12.784 20.280  1.00 15.87 ? 114 TYR   A CE2 1 
ATOM   915  C  CZ  . TYR   A 1 114 ? 6.510   -12.365 21.564  1.00 16.48 ? 114 TYR   A CZ  1 
ATOM   916  O  OH  . TYR   A 1 114 ? 5.613   -12.462 22.618  1.00 20.31 ? 114 TYR   A OH  1 
ATOM   917  N  N   . ALA   A 1 115 ? 10.223  -13.170 15.736  1.00 11.65 ? 115 ALA   A N   1 
ATOM   918  C  CA  . ALA   A 1 115 ? 10.739  -13.200 14.375  1.00 12.40 ? 115 ALA   A CA  1 
ATOM   919  C  C   . ALA   A 1 115 ? 11.164  -11.798 13.906  1.00 11.26 ? 115 ALA   A C   1 
ATOM   920  O  O   . ALA   A 1 115 ? 11.942  -11.662 12.979  1.00 13.03 ? 115 ALA   A O   1 
ATOM   921  C  CB  . ALA   A 1 115 ? 9.679   -13.819 13.456  1.00 13.86 ? 115 ALA   A CB  1 
ATOM   922  N  N   . ALA   A 1 116 ? 10.481  -10.777 14.406  1.00 11.96 ? 116 ALA   A N   1 
ATOM   923  C  CA  . ALA   A 1 116 ? 10.802  -9.427  13.960  1.00 11.47 ? 116 ALA   A CA  1 
ATOM   924  C  C   . ALA   A 1 116 ? 10.150  -8.488  14.975  1.00 12.22 ? 116 ALA   A C   1 
ATOM   925  O  O   . ALA   A 1 116 ? 9.441   -8.877  15.905  1.00 12.14 ? 116 ALA   A O   1 
ATOM   926  C  CB  . ALA   A 1 116 ? 10.206  -9.163  12.565  1.00 12.07 ? 116 ALA   A CB  1 
ATOM   927  N  N   . GLU   A 1 117 ? 10.491  -7.211  14.802  1.00 11.69 ? 117 GLU   A N   1 
ATOM   928  C  CA  . GLU   A 1 117 ? 9.952   -6.143  15.663  1.00 11.51 ? 117 GLU   A CA  1 
ATOM   929  C  C   . GLU   A 1 117 ? 9.820   -4.838  14.860  1.00 11.33 ? 117 GLU   A C   1 
ATOM   930  O  O   . GLU   A 1 117 ? 10.725  -4.429  14.107  1.00 12.65 ? 117 GLU   A O   1 
ATOM   931  C  CB  . GLU   A 1 117 ? 10.866  -5.908  16.866  1.00 11.86 ? 117 GLU   A CB  1 
ATOM   932  C  CG  . GLU   A 1 117 ? 10.353  -4.939  17.921  1.00 10.90 ? 117 GLU   A CG  1 
ATOM   933  C  CD  . GLU   A 1 117 ? 11.286  -4.859  19.123  1.00 12.55 ? 117 GLU   A CD  1 
ATOM   934  O  OE1 . GLU   A 1 117 ? 11.971  -5.884  19.469  1.00 12.38 ? 117 GLU   A OE1 1 
ATOM   935  O  OE2 . GLU   A 1 117 ? 11.346  -3.816  19.790  1.00 13.02 ? 117 GLU   A OE2 1 
ATOM   936  N  N   . LEU   A 1 118 ? 8.588   -4.313  14.921  1.00 11.44 ? 118 LEU   A N   1 
ATOM   937  C  CA  . LEU   A 1 118 ? 8.246   -3.052  14.277  1.00 11.53 ? 118 LEU   A CA  1 
ATOM   938  C  C   . LEU   A 1 118 ? 8.451   -1.887  15.267  1.00 10.41 ? 118 LEU   A C   1 
ATOM   939  O  O   . LEU   A 1 118 ? 8.049   -1.978  16.432  1.00 10.97 ? 118 LEU   A O   1 
ATOM   940  C  CB  . LEU   A 1 118 ? 6.749   -3.133  13.887  1.00 10.80 ? 118 LEU   A CB  1 
ATOM   941  C  CG  . LEU   A 1 118 ? 6.057   -1.798  13.506  1.00 10.83 ? 118 LEU   A CG  1 
ATOM   942  C  CD1 . LEU   A 1 118 ? 6.589   -1.236  12.196  1.00 13.22 ? 118 LEU   A CD1 1 
ATOM   943  C  CD2 . LEU   A 1 118 ? 4.592   -2.136  13.289  1.00 13.51 ? 118 LEU   A CD2 1 
ATOM   944  N  N   . HIS   A 1 119 ? 9.139   -0.821  14.770  1.00 10.99 ? 119 HIS   A N   1 
ATOM   945  C  CA  . HIS   A 1 119 ? 9.321   0.389   15.556  1.00 10.46 ? 119 HIS   A CA  1 
ATOM   946  C  C   . HIS   A 1 119 ? 8.681   1.588   14.862  1.00 10.37 ? 119 HIS   A C   1 
ATOM   947  O  O   . HIS   A 1 119 ? 9.101   1.913   13.723  1.00 11.44 ? 119 HIS   A O   1 
ATOM   948  C  CB  . HIS   A 1 119 ? 10.819  0.650   15.640  1.00 9.99  ? 119 HIS   A CB  1 
ATOM   949  C  CG  . HIS   A 1 119 ? 11.467  -0.380  16.532  1.00 10.31 ? 119 HIS   A CG  1 
ATOM   950  N  ND1 . HIS   A 1 119 ? 12.853  -0.564  16.589  1.00 11.96 ? 119 HIS   A ND1 1 
ATOM   951  C  CD2 . HIS   A 1 119 ? 10.944  -1.161  17.513  1.00 10.82 ? 119 HIS   A CD2 1 
ATOM   952  C  CE1 . HIS   A 1 119 ? 13.156  -1.458  17.492  1.00 10.57 ? 119 HIS   A CE1 1 
ATOM   953  N  NE2 . HIS   A 1 119 ? 12.006  -1.925  18.065  1.00 10.16 ? 119 HIS   A NE2 1 
ATOM   954  N  N   . LEU   A 1 120 ? 7.657   2.166   15.539  1.00 10.71 ? 120 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 120 ? 7.080   3.419   15.071  1.00 12.49 ? 120 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 120 ? 7.735   4.541   15.849  1.00 9.73  ? 120 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 120 ? 7.555   4.603   17.075  1.00 9.97  ? 120 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 120 ? 5.568   3.354   15.242  1.00 11.67 ? 120 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 120 ? 4.913   2.275   14.370  1.00 13.28 ? 120 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 120 ? 4.058   1.281   15.201  1.00 15.05 ? 120 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 120 ? 3.990   2.921   13.324  1.00 14.86 ? 120 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 121 ? 8.502   5.376   15.105  1.00 12.03 ? 121 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 121 ? 9.302   6.409   15.775  1.00 11.73 ? 121 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 121 ? 8.569   7.762   15.783  1.00 12.01 ? 121 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 121 ? 8.154   8.190   14.695  1.00 12.99 ? 121 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 121 ? 10.663  6.511   15.050  1.00 12.24 ? 121 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 121 ? 11.571  7.602   15.695  1.00 11.34 ? 121 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 121 ? 11.426  5.171   14.959  1.00 13.67 ? 121 VAL   A CG2 1 
ATOM   969  N  N   . HIS   A 1 122 ? 8.454   8.350   16.990  1.00 11.67 ? 122 HIS   A N   1 
ATOM   970  C  CA  . HIS   A 1 122 ? 7.767   9.641   17.132  1.00 11.57 ? 122 HIS   A CA  1 
ATOM   971  C  C   . HIS   A 1 122 ? 8.661   10.611  17.889  1.00 13.00 ? 122 HIS   A C   1 
ATOM   972  O  O   . HIS   A 1 122 ? 9.359   10.224  18.826  1.00 12.94 ? 122 HIS   A O   1 
ATOM   973  C  CB  . HIS   A 1 122 ? 6.449   9.494   17.938  1.00 14.23 ? 122 HIS   A CB  1 
ATOM   974  C  CG  . HIS   A 1 122 ? 5.569   8.335   17.556  1.00 11.48 ? 122 HIS   A CG  1 
ATOM   975  N  ND1 . HIS   A 1 122 ? 5.939   6.971   17.770  1.00 11.00 ? 122 HIS   A ND1 1 
ATOM   976  C  CD2 . HIS   A 1 122 ? 4.366   8.287   16.908  1.00 12.87 ? 122 HIS   A CD2 1 
ATOM   977  C  CE1 . HIS   A 1 122 ? 4.937   6.189   17.350  1.00 13.90 ? 122 HIS   A CE1 1 
ATOM   978  N  NE2 . HIS   A 1 122 ? 3.965   6.974   16.856  1.00 13.91 ? 122 HIS   A NE2 1 
ATOM   979  N  N   . TRP   A 1 123 ? 8.530   11.912  17.554  1.00 12.15 ? 123 TRP   A N   1 
ATOM   980  C  CA  . TRP   A 1 123 ? 9.349   12.905  18.253  1.00 13.66 ? 123 TRP   A CA  1 
ATOM   981  C  C   . TRP   A 1 123 ? 8.450   13.912  18.991  1.00 12.33 ? 123 TRP   A C   1 
ATOM   982  O  O   . TRP   A 1 123 ? 7.320   14.254  18.562  1.00 14.56 ? 123 TRP   A O   1 
ATOM   983  C  CB  . TRP   A 1 123 ? 10.320  13.613  17.302  1.00 15.09 ? 123 TRP   A CB  1 
ATOM   984  C  CG  . TRP   A 1 123 ? 9.663   14.230  16.102  1.00 15.25 ? 123 TRP   A CG  1 
ATOM   985  C  CD1 . TRP   A 1 123 ? 9.463   13.645  14.878  1.00 15.15 ? 123 TRP   A CD1 1 
ATOM   986  C  CD2 . TRP   A 1 123 ? 9.205   15.600  15.980  1.00 16.97 ? 123 TRP   A CD2 1 
ATOM   987  N  NE1 . TRP   A 1 123 ? 8.909   14.535  14.000  1.00 16.30 ? 123 TRP   A NE1 1 
ATOM   988  C  CE2 . TRP   A 1 123 ? 8.742   15.754  14.646  1.00 17.01 ? 123 TRP   A CE2 1 
ATOM   989  C  CE3 . TRP   A 1 123 ? 9.237   16.719  16.822  1.00 18.44 ? 123 TRP   A CE3 1 
ATOM   990  C  CZ2 . TRP   A 1 123 ? 8.252   16.974  14.168  1.00 20.90 ? 123 TRP   A CZ2 1 
ATOM   991  C  CZ3 . TRP   A 1 123 ? 8.669   17.898  16.365  1.00 20.56 ? 123 TRP   A CZ3 1 
ATOM   992  C  CH2 . TRP   A 1 123 ? 8.253   18.043  15.043  1.00 23.53 ? 123 TRP   A CH2 1 
ATOM   993  N  N   . ASN   A 1 124 ? 8.943   14.363  20.138  1.00 13.34 ? 124 ASN   A N   1 
ATOM   994  C  CA  . ASN   A 1 124 ? 8.218   15.248  21.026  1.00 14.13 ? 124 ASN   A CA  1 
ATOM   995  C  C   . ASN   A 1 124 ? 8.098   16.644  20.395  1.00 14.78 ? 124 ASN   A C   1 
ATOM   996  O  O   . ASN   A 1 124 ? 9.071   17.324  20.163  1.00 13.59 ? 124 ASN   A O   1 
ATOM   997  C  CB  . ASN   A 1 124 ? 8.983   15.304  22.354  1.00 13.63 ? 124 ASN   A CB  1 
ATOM   998  C  CG  . ASN   A 1 124 ? 8.188   15.935  23.463  1.00 14.12 ? 124 ASN   A CG  1 
ATOM   999  O  OD1 . ASN   A 1 124 ? 7.347   16.810  23.176  1.00 15.61 ? 124 ASN   A OD1 1 
ATOM   1000 N  ND2 . ASN   A 1 124 ? 8.387   15.479  24.695  1.00 15.49 ? 124 ASN   A ND2 1 
ATOM   1001 N  N   . THR   A 1 125 ? 6.866   17.106  20.139  1.00 14.78 ? 125 THR   A N   1 
ATOM   1002 C  CA  . THR   A 1 125 ? 6.636   18.363  19.415  1.00 17.21 ? 125 THR   A CA  1 
ATOM   1003 C  C   . THR   A 1 125 ? 7.199   19.551  20.203  1.00 17.26 ? 125 THR   A C   1 
ATOM   1004 O  O   . THR   A 1 125 ? 7.319   20.639  19.573  1.00 18.72 ? 125 THR   A O   1 
ATOM   1005 C  CB  . THR   A 1 125 ? 5.169   18.498  18.976  1.00 18.84 ? 125 THR   A CB  1 
ATOM   1006 O  OG1 . THR   A 1 125 ? 4.349   18.505  20.149  1.00 22.32 ? 125 THR   A OG1 1 
ATOM   1007 C  CG2 . THR   A 1 125 ? 4.790   17.364  18.039  1.00 23.52 ? 125 THR   A CG2 1 
ATOM   1008 N  N   . LYS   A 1 126 ? 7.384   19.336  21.605  1.00 15.31 ? 127 LYS   A N   1 
ATOM   1009 C  CA  . LYS   A 1 126 ? 7.900   20.530  22.330  1.00 13.81 ? 127 LYS   A CA  1 
ATOM   1010 C  C   . LYS   A 1 126 ? 9.299   20.942  21.839  1.00 13.72 ? 127 LYS   A C   1 
ATOM   1011 O  O   . LYS   A 1 126 ? 9.749   22.030  22.223  1.00 16.80 ? 127 LYS   A O   1 
ATOM   1012 C  CB  . LYS   A 1 126 ? 7.855   20.290  23.847  1.00 16.78 ? 127 LYS   A CB  1 
ATOM   1013 C  CG  . LYS   A 1 126 ? 8.870   19.298  24.408  1.00 18.63 ? 127 LYS   A CG  1 
ATOM   1014 C  CD  . LYS   A 1 126 ? 8.701   19.000  25.917  1.00 24.50 ? 127 LYS   A CD  1 
ATOM   1015 C  CE  . LYS   A 1 126 ? 8.968   20.202  26.804  1.00 32.07 ? 127 LYS   A CE  1 
ATOM   1016 N  NZ  . LYS   A 1 126 ? 8.950   19.880  28.262  1.00 40.90 ? 127 LYS   A NZ  1 
ATOM   1017 N  N   . TYR   A 1 127 ? 10.027  20.067  21.125  1.00 14.24 ? 128 TYR   A N   1 
ATOM   1018 C  CA  . TYR   A 1 127 ? 11.372  20.345  20.621  1.00 13.32 ? 128 TYR   A CA  1 
ATOM   1019 C  C   . TYR   A 1 127 ? 11.390  20.767  19.152  1.00 13.87 ? 128 TYR   A C   1 
ATOM   1020 O  O   . TYR   A 1 127 ? 12.460  21.081  18.629  1.00 17.21 ? 128 TYR   A O   1 
ATOM   1021 C  CB  . TYR   A 1 127 ? 12.349  19.198  20.918  1.00 13.87 ? 128 TYR   A CB  1 
ATOM   1022 C  CG  . TYR   A 1 127 ? 12.399  18.880  22.383  1.00 15.20 ? 128 TYR   A CG  1 
ATOM   1023 C  CD1 . TYR   A 1 127 ? 12.799  19.846  23.317  1.00 18.13 ? 128 TYR   A CD1 1 
ATOM   1024 C  CD2 . TYR   A 1 127 ? 12.060  17.598  22.869  1.00 14.93 ? 128 TYR   A CD2 1 
ATOM   1025 C  CE1 . TYR   A 1 127 ? 12.827  19.555  24.675  1.00 16.98 ? 128 TYR   A CE1 1 
ATOM   1026 C  CE2 . TYR   A 1 127 ? 12.087  17.294  24.218  1.00 14.41 ? 128 TYR   A CE2 1 
ATOM   1027 C  CZ  . TYR   A 1 127 ? 12.493  18.282  25.127  1.00 15.40 ? 128 TYR   A CZ  1 
ATOM   1028 O  OH  . TYR   A 1 127 ? 12.511  18.039  26.463  1.00 19.37 ? 128 TYR   A OH  1 
ATOM   1029 N  N   . GLY   A 1 128 ? 10.205  20.919  18.499  1.00 15.22 ? 129 GLY   A N   1 
ATOM   1030 C  CA  . GLY   A 1 128 ? 10.162  21.591  17.215  1.00 16.15 ? 129 GLY   A CA  1 
ATOM   1031 C  C   . GLY   A 1 128 ? 10.572  20.744  16.020  1.00 19.35 ? 129 GLY   A C   1 
ATOM   1032 O  O   . GLY   A 1 128 ? 9.910   20.848  14.971  1.00 20.34 ? 129 GLY   A O   1 
ATOM   1033 N  N   . ASP   A 1 129 ? 11.676  19.955  16.132  1.00 18.21 ? 130 ASP   A N   1 
ATOM   1034 C  CA  . ASP   A 1 129 ? 11.951  19.023  15.043  1.00 18.79 ? 130 ASP   A CA  1 
ATOM   1035 C  C   . ASP   A 1 129 ? 12.667  17.802  15.597  1.00 20.06 ? 130 ASP   A C   1 
ATOM   1036 O  O   . ASP   A 1 129 ? 13.074  17.792  16.769  1.00 17.79 ? 130 ASP   A O   1 
ATOM   1037 C  CB  . ASP   A 1 129 ? 12.717  19.636  13.859  1.00 20.52 ? 130 ASP   A CB  1 
ATOM   1038 C  CG  . ASP   A 1 129 ? 14.116  20.146  14.143  1.00 22.84 ? 130 ASP   A CG  1 
ATOM   1039 O  OD1 . ASP   A 1 129 ? 14.835  19.559  14.934  1.00 29.29 ? 130 ASP   A OD1 1 
ATOM   1040 O  OD2 . ASP   A 1 129 ? 14.534  21.089  13.528  1.00 33.54 ? 130 ASP   A OD2 1 
ATOM   1041 N  N   . PHE   A 1 130 ? 12.796  16.785  14.732  1.00 17.97 ? 131 PHE   A N   1 
ATOM   1042 C  CA  . PHE   A 1 130 ? 13.386  15.515  15.130  1.00 15.81 ? 131 PHE   A CA  1 
ATOM   1043 C  C   . PHE   A 1 130 ? 14.852  15.704  15.544  1.00 16.19 ? 131 PHE   A C   1 
ATOM   1044 O  O   . PHE   A 1 130 ? 15.263  15.132  16.554  1.00 14.36 ? 131 PHE   A O   1 
ATOM   1045 C  CB  . PHE   A 1 130 ? 13.321  14.568  13.949  1.00 14.93 ? 131 PHE   A CB  1 
ATOM   1046 C  CG  . PHE   A 1 130 ? 13.964  13.238  14.233  1.00 15.09 ? 131 PHE   A CG  1 
ATOM   1047 C  CD1 . PHE   A 1 130 ? 13.253  12.191  14.831  1.00 15.49 ? 131 PHE   A CD1 1 
ATOM   1048 C  CD2 . PHE   A 1 130 ? 15.293  13.050  13.936  1.00 16.17 ? 131 PHE   A CD2 1 
ATOM   1049 C  CE1 . PHE   A 1 130 ? 13.866  10.988  15.131  1.00 15.83 ? 131 PHE   A CE1 1 
ATOM   1050 C  CE2 . PHE   A 1 130 ? 15.892  11.828  14.181  1.00 17.51 ? 131 PHE   A CE2 1 
ATOM   1051 C  CZ  . PHE   A 1 130 ? 15.167  10.796  14.759  1.00 19.13 ? 131 PHE   A CZ  1 
ATOM   1052 N  N   . GLY   A 1 131 ? 15.609  16.530  14.788  1.00 17.80 ? 132 GLY   A N   1 
ATOM   1053 C  CA  . GLY   A 1 131 ? 17.033  16.678  15.093  1.00 17.48 ? 132 GLY   A CA  1 
ATOM   1054 C  C   . GLY   A 1 131 ? 17.273  17.278  16.487  1.00 17.54 ? 132 GLY   A C   1 
ATOM   1055 O  O   . GLY   A 1 131 ? 18.259  16.978  17.160  1.00 19.34 ? 132 GLY   A O   1 
ATOM   1056 N  N   . LYS   A 1 132 ? 16.421  18.230  16.886  1.00 15.41 ? 133 LYS   A N   1 
ATOM   1057 C  CA  . LYS   A 1 132 ? 16.502  18.760  18.243  1.00 15.07 ? 133 LYS   A CA  1 
ATOM   1058 C  C   . LYS   A 1 132 ? 15.999  17.748  19.270  1.00 16.01 ? 133 LYS   A C   1 
ATOM   1059 O  O   . LYS   A 1 132 ? 16.542  17.665  20.387  1.00 15.49 ? 133 LYS   A O   1 
ATOM   1060 C  CB  . LYS   A 1 132 ? 15.714  20.064  18.352  1.00 14.80 ? 133 LYS   A CB  1 
ATOM   1061 C  CG  . LYS   A 1 132 ? 16.408  21.284  17.748  1.00 19.98 ? 133 LYS   A CG  1 
ATOM   1062 C  CD  . LYS   A 1 132 ? 17.652  21.666  18.577  1.00 23.26 ? 133 LYS   A CD  1 
ATOM   1063 C  CE  . LYS   A 1 132 ? 18.116  23.066  18.207  1.00 28.76 ? 133 LYS   A CE  1 
ATOM   1064 N  NZ  . LYS   A 1 132 ? 18.735  22.949  16.879  1.00 32.71 ? 133 LYS   A NZ  1 
ATOM   1065 N  N   . ALA   A 1 133 ? 14.912  17.037  18.915  1.00 14.72 ? 134 ALA   A N   1 
ATOM   1066 C  CA  . ALA   A 1 133 ? 14.354  16.082  19.873  1.00 15.14 ? 134 ALA   A CA  1 
ATOM   1067 C  C   . ALA   A 1 133 ? 15.341  14.957  20.290  1.00 13.29 ? 134 ALA   A C   1 
ATOM   1068 O  O   . ALA   A 1 133 ? 15.364  14.613  21.472  1.00 14.91 ? 134 ALA   A O   1 
ATOM   1069 C  CB  . ALA   A 1 133 ? 13.135  15.423  19.215  1.00 15.43 ? 134 ALA   A CB  1 
ATOM   1070 N  N   . VAL   A 1 134 ? 16.178  14.452  19.379  1.00 13.30 ? 135 VAL   A N   1 
ATOM   1071 C  CA  . VAL   A 1 134 ? 17.066  13.327  19.729  1.00 13.50 ? 135 VAL   A CA  1 
ATOM   1072 C  C   . VAL   A 1 134 ? 18.154  13.802  20.694  1.00 14.28 ? 135 VAL   A C   1 
ATOM   1073 O  O   . VAL   A 1 134 ? 18.872  12.968  21.247  1.00 16.41 ? 135 VAL   A O   1 
ATOM   1074 C  CB  . VAL   A 1 134 ? 17.723  12.697  18.486  1.00 16.35 ? 135 VAL   A CB  1 
ATOM   1075 C  CG1 . VAL   A 1 134 ? 16.686  12.012  17.612  1.00 17.85 ? 135 VAL   A CG1 1 
ATOM   1076 C  CG2 . VAL   A 1 134 ? 18.661  13.615  17.704  1.00 16.52 ? 135 VAL   A CG2 1 
ATOM   1077 N  N   . GLN   A 1 135 ? 18.271  15.126  20.894  1.00 15.06 ? 136 GLN   A N   1 
ATOM   1078 C  CA  . GLN   A 1 135 ? 19.250  15.647  21.848  1.00 15.00 ? 136 GLN   A CA  1 
ATOM   1079 C  C   . GLN   A 1 135 ? 18.690  15.723  23.267  1.00 15.18 ? 136 GLN   A C   1 
ATOM   1080 O  O   . GLN   A 1 135 ? 19.342  16.252  24.192  1.00 18.59 ? 136 GLN   A O   1 
ATOM   1081 C  CB  . GLN   A 1 135 ? 19.802  17.017  21.398  1.00 15.10 ? 136 GLN   A CB  1 
ATOM   1082 C  CG  . GLN   A 1 135 ? 20.464  16.961  20.028  1.00 18.68 ? 136 GLN   A CG  1 
ATOM   1083 C  CD  . GLN   A 1 135 ? 20.967  18.311  19.548  1.00 19.99 ? 136 GLN   A CD  1 
ATOM   1084 O  OE1 . GLN   A 1 135 ? 21.831  18.937  20.183  1.00 28.61 ? 136 GLN   A OE1 1 
ATOM   1085 N  NE2 . GLN   A 1 135 ? 20.442  18.764  18.409  1.00 28.51 ? 136 GLN   A NE2 1 
ATOM   1086 N  N   . GLN   A 1 136 ? 17.448  15.237  23.453  1.00 13.74 ? 137 GLN   A N   1 
ATOM   1087 C  CA  . GLN   A 1 136 ? 16.761  15.416  24.723  1.00 14.73 ? 137 GLN   A CA  1 
ATOM   1088 C  C   . GLN   A 1 136 ? 16.389  14.074  25.324  1.00 14.20 ? 137 GLN   A C   1 
ATOM   1089 O  O   . GLN   A 1 136 ? 16.012  13.167  24.579  1.00 14.07 ? 137 GLN   A O   1 
ATOM   1090 C  CB  . GLN   A 1 136 ? 15.469  16.216  24.569  1.00 17.42 ? 137 GLN   A CB  1 
ATOM   1091 C  CG  . GLN   A 1 136 ? 15.700  17.512  23.784  1.00 18.27 ? 137 GLN   A CG  1 
ATOM   1092 C  CD  . GLN   A 1 136 ? 16.606  18.483  24.510  1.00 21.86 ? 137 GLN   A CD  1 
ATOM   1093 O  OE1 . GLN   A 1 136 ? 16.711  18.490  25.728  1.00 24.45 ? 137 GLN   A OE1 1 
ATOM   1094 N  NE2 . GLN   A 1 136 ? 17.296  19.302  23.752  1.00 32.65 ? 137 GLN   A NE2 1 
ATOM   1095 N  N   . PRO   A 1 137 ? 16.404  13.961  26.667  1.00 14.72 ? 138 PRO   A N   1 
ATOM   1096 C  CA  . PRO   A 1 137 ? 16.147  12.656  27.291  1.00 15.19 ? 138 PRO   A CA  1 
ATOM   1097 C  C   . PRO   A 1 137 ? 14.714  12.174  27.056  1.00 15.19 ? 138 PRO   A C   1 
ATOM   1098 O  O   . PRO   A 1 137 ? 14.435  10.973  27.084  1.00 16.90 ? 138 PRO   A O   1 
ATOM   1099 C  CB  . PRO   A 1 137 ? 16.414  12.867  28.781  1.00 16.23 ? 138 PRO   A CB  1 
ATOM   1100 C  CG  . PRO   A 1 137 ? 16.710  14.361  28.944  1.00 21.67 ? 138 PRO   A CG  1 
ATOM   1101 C  CD  . PRO   A 1 137 ? 16.883  15.002  27.590  1.00 18.23 ? 138 PRO   A CD  1 
ATOM   1102 N  N   . ASP   A 1 138 ? 13.810  13.132  26.809  1.00 13.83 ? 139 ASP   A N   1 
ATOM   1103 C  CA  . ASP   A 1 138 ? 12.408  12.803  26.541  1.00 15.23 ? 139 ASP   A CA  1 
ATOM   1104 C  C   . ASP   A 1 138 ? 12.073  13.204  25.090  1.00 12.19 ? 139 ASP   A C   1 
ATOM   1105 O  O   . ASP   A 1 138 ? 10.934  13.630  24.824  1.00 13.09 ? 139 ASP   A O   1 
ATOM   1106 C  CB  . ASP   A 1 138 ? 11.453  13.443  27.566  1.00 14.84 ? 139 ASP   A CB  1 
ATOM   1107 C  CG  . ASP   A 1 138 ? 11.520  14.958  27.598  1.00 16.12 ? 139 ASP   A CG  1 
ATOM   1108 O  OD1 . ASP   A 1 138 ? 12.452  15.481  26.927  1.00 18.77 ? 139 ASP   A OD1 1 
ATOM   1109 O  OD2 . ASP   A 1 138 ? 10.673  15.561  28.280  1.00 20.13 ? 139 ASP   A OD2 1 
ATOM   1110 N  N   . GLY   A 1 139 ? 13.006  13.094  24.140  1.00 12.79 ? 140 GLY   A N   1 
ATOM   1111 C  CA  . GLY   A 1 139 ? 12.815  13.599  22.799  1.00 12.98 ? 140 GLY   A CA  1 
ATOM   1112 C  C   . GLY   A 1 139 ? 11.946  12.690  21.942  1.00 11.40 ? 140 GLY   A C   1 
ATOM   1113 O  O   . GLY   A 1 139 ? 11.260  13.187  21.046  1.00 14.03 ? 140 GLY   A O   1 
ATOM   1114 N  N   . LEU   A 1 140 ? 12.089  11.350  22.117  1.00 12.98 ? 141 LEU   A N   1 
ATOM   1115 C  CA  . LEU   A 1 140 ? 11.428  10.399  21.210  1.00 12.71 ? 141 LEU   A CA  1 
ATOM   1116 C  C   . LEU   A 1 140 ? 10.588  9.434   22.027  1.00 13.48 ? 141 LEU   A C   1 
ATOM   1117 O  O   . LEU   A 1 140 ? 10.832  9.191   23.202  1.00 11.93 ? 141 LEU   A O   1 
ATOM   1118 C  CB  . LEU   A 1 140 ? 12.461  9.557   20.490  1.00 13.17 ? 141 LEU   A CB  1 
ATOM   1119 C  CG  . LEU   A 1 140 ? 13.345  10.269  19.479  1.00 15.57 ? 141 LEU   A CG  1 
ATOM   1120 C  CD1 . LEU   A 1 140 ? 14.096  9.273   18.609  1.00 14.34 ? 141 LEU   A CD1 1 
ATOM   1121 C  CD2 . LEU   A 1 140 ? 12.711  11.334  18.596  1.00 17.86 ? 141 LEU   A CD2 1 
ATOM   1122 N  N   . ALA   A 1 141 ? 9.525   8.953   21.361  1.00 12.11 ? 142 ALA   A N   1 
ATOM   1123 C  CA  . ALA   A 1 141 ? 8.774   7.814   21.897  1.00 11.61 ? 142 ALA   A CA  1 
ATOM   1124 C  C   . ALA   A 1 141 ? 8.716   6.816   20.747  1.00 12.64 ? 142 ALA   A C   1 
ATOM   1125 O  O   . ALA   A 1 141 ? 8.359   7.137   19.610  1.00 12.96 ? 142 ALA   A O   1 
ATOM   1126 C  CB  . ALA   A 1 141 ? 7.380   8.266   22.242  1.00 11.95 ? 142 ALA   A CB  1 
ATOM   1127 N  N   . VAL   A 1 142 ? 9.216   5.590   21.018  1.00 12.25 ? 143 VAL   A N   1 
ATOM   1128 C  CA  . VAL   A 1 142 ? 9.146   4.530   20.009  1.00 11.99 ? 143 VAL   A CA  1 
ATOM   1129 C  C   . VAL   A 1 142 ? 8.199   3.458   20.491  1.00 11.00 ? 143 VAL   A C   1 
ATOM   1130 O  O   . VAL   A 1 142 ? 8.323   3.002   21.627  1.00 12.11 ? 143 VAL   A O   1 
ATOM   1131 C  CB  . VAL   A 1 142 ? 10.547  3.973   19.655  1.00 10.43 ? 143 VAL   A CB  1 
ATOM   1132 C  CG1 . VAL   A 1 142 ? 10.453  2.923   18.552  1.00 13.89 ? 143 VAL   A CG1 1 
ATOM   1133 C  CG2 . VAL   A 1 142 ? 11.506  5.091   19.279  1.00 14.52 ? 143 VAL   A CG2 1 
ATOM   1134 N  N   . LEU   A 1 143 ? 7.201   3.211   19.632  1.00 10.72 ? 144 LEU   A N   1 
ATOM   1135 C  CA  . LEU   A 1 143 ? 6.239   2.155   19.924  1.00 10.66 ? 144 LEU   A CA  1 
ATOM   1136 C  C   . LEU   A 1 143 ? 6.745   0.898   19.217  1.00 10.42 ? 144 LEU   A C   1 
ATOM   1137 O  O   . LEU   A 1 143 ? 6.961   0.872   17.998  1.00 11.26 ? 144 LEU   A O   1 
ATOM   1138 C  CB  . LEU   A 1 143 ? 4.888   2.626   19.354  1.00 11.41 ? 144 LEU   A CB  1 
ATOM   1139 C  CG  . LEU   A 1 143 ? 3.731   1.617   19.413  1.00 10.75 ? 144 LEU   A CG  1 
ATOM   1140 C  CD1 . LEU   A 1 143 ? 3.512   1.260   20.860  1.00 14.14 ? 144 LEU   A CD1 1 
ATOM   1141 C  CD2 . LEU   A 1 143 ? 2.475   2.273   18.778  1.00 13.25 ? 144 LEU   A CD2 1 
ATOM   1142 N  N   . GLY   A 1 144 ? 7.017   -0.129  20.032  1.00 11.71 ? 145 GLY   A N   1 
ATOM   1143 C  CA  . GLY   A 1 144 ? 7.591   -1.382  19.550  1.00 11.42 ? 145 GLY   A CA  1 
ATOM   1144 C  C   . GLY   A 1 144 ? 6.517   -2.476  19.513  1.00 10.29 ? 145 GLY   A C   1 
ATOM   1145 O  O   . GLY   A 1 144 ? 5.763   -2.557  20.478  1.00 11.16 ? 145 GLY   A O   1 
ATOM   1146 N  N   . ILE   A 1 145 ? 6.460   -3.204  18.405  1.00 10.76 ? 146 ILE   A N   1 
ATOM   1147 C  CA  . ILE   A 1 145 ? 5.415   -4.218  18.292  1.00 10.81 ? 146 ILE   A CA  1 
ATOM   1148 C  C   . ILE   A 1 145 ? 6.159   -5.467  17.806  1.00 11.70 ? 146 ILE   A C   1 
ATOM   1149 O  O   . ILE   A 1 145 ? 6.797   -5.441  16.744  1.00 12.27 ? 146 ILE   A O   1 
ATOM   1150 C  CB  . ILE   A 1 145 ? 4.307   -3.736  17.322  1.00 12.61 ? 146 ILE   A CB  1 
ATOM   1151 C  CG1 . ILE   A 1 145 ? 3.692   -2.400  17.820  1.00 14.84 ? 146 ILE   A CG1 1 
ATOM   1152 C  CG2 . ILE   A 1 145 ? 3.240   -4.838  17.073  1.00 14.00 ? 146 ILE   A CG2 1 
ATOM   1153 C  CD1 . ILE   A 1 145 ? 2.558   -1.872  16.932  1.00 15.08 ? 146 ILE   A CD1 1 
ATOM   1154 N  N   . PHE   A 1 146 ? 5.894   -6.586  18.469  1.00 12.35 ? 147 PHE   A N   1 
ATOM   1155 C  CA  . PHE   A 1 146 ? 6.545   -7.836  18.075  1.00 12.53 ? 147 PHE   A CA  1 
ATOM   1156 C  C   . PHE   A 1 146 ? 5.815   -8.466  16.890  1.00 13.63 ? 147 PHE   A C   1 
ATOM   1157 O  O   . PHE   A 1 146 ? 4.592   -8.350  16.831  1.00 13.76 ? 147 PHE   A O   1 
ATOM   1158 C  CB  . PHE   A 1 146 ? 6.529   -8.803  19.264  1.00 12.69 ? 147 PHE   A CB  1 
ATOM   1159 C  CG  . PHE   A 1 146 ? 7.385   -8.356  20.411  1.00 10.51 ? 147 PHE   A CG  1 
ATOM   1160 C  CD1 . PHE   A 1 146 ? 8.761   -8.203  20.210  1.00 12.36 ? 147 PHE   A CD1 1 
ATOM   1161 C  CD2 . PHE   A 1 146 ? 6.890   -8.064  21.671  1.00 12.23 ? 147 PHE   A CD2 1 
ATOM   1162 C  CE1 . PHE   A 1 146 ? 9.569   -7.759  21.252  1.00 13.48 ? 147 PHE   A CE1 1 
ATOM   1163 C  CE2 . PHE   A 1 146 ? 7.691   -7.697  22.747  1.00 12.44 ? 147 PHE   A CE2 1 
ATOM   1164 C  CZ  . PHE   A 1 146 ? 9.058   -7.572  22.528  1.00 12.56 ? 147 PHE   A CZ  1 
ATOM   1165 N  N   . LEU   A 1 147 ? 6.541   -9.195  16.055  1.00 12.81 ? 148 LEU   A N   1 
ATOM   1166 C  CA  . LEU   A 1 147 ? 5.962   -10.002 14.983  1.00 12.72 ? 148 LEU   A CA  1 
ATOM   1167 C  C   . LEU   A 1 147 ? 6.283   -11.468 15.235  1.00 12.42 ? 148 LEU   A C   1 
ATOM   1168 O  O   . LEU   A 1 147 ? 7.447   -11.792 15.482  1.00 13.77 ? 148 LEU   A O   1 
ATOM   1169 C  CB  . LEU   A 1 147 ? 6.503   -9.630  13.600  1.00 13.46 ? 148 LEU   A CB  1 
ATOM   1170 C  CG  . LEU   A 1 147 ? 5.990   -8.341  12.959  1.00 13.49 ? 148 LEU   A CG  1 
ATOM   1171 C  CD1 . LEU   A 1 147 ? 6.196   -7.061  13.804  1.00 15.77 ? 148 LEU   A CD1 1 
ATOM   1172 C  CD2 . LEU   A 1 147 ? 6.560   -8.203  11.563  1.00 13.69 ? 148 LEU   A CD2 1 
ATOM   1173 N  N   . LYS   A 1 148 ? 5.242   -12.326 15.157  1.00 13.12 ? 149 LYS   A N   1 
ATOM   1174 C  CA  . LYS   A 1 148 ? 5.415   -13.761 15.102  1.00 12.51 ? 149 LYS   A CA  1 
ATOM   1175 C  C   . LYS   A 1 148 ? 4.924   -14.252 13.749  1.00 15.09 ? 149 LYS   A C   1 
ATOM   1176 O  O   . LYS   A 1 148 ? 4.075   -13.624 13.122  1.00 15.14 ? 149 LYS   A O   1 
ATOM   1177 C  CB  . LYS   A 1 148 ? 4.657   -14.359 16.289  1.00 14.35 ? 149 LYS   A CB  1 
ATOM   1178 C  CG  . LYS   A 1 148 ? 3.137   -14.345 16.212  1.00 16.79 ? 149 LYS   A CG  1 
ATOM   1179 C  CD  . LYS   A 1 148 ? 2.582   -15.049 17.445  1.00 24.71 ? 149 LYS   A CD  1 
ATOM   1180 C  CE  . LYS   A 1 148 ? 1.169   -15.541 17.285  1.00 32.78 ? 149 LYS   A CE  1 
ATOM   1181 N  NZ  . LYS   A 1 148 ? 0.890   -16.665 18.212  1.00 44.04 ? 149 LYS   A NZ  1 
ATOM   1182 N  N   . VAL   A 1 149 ? 5.417   -15.426 13.354  1.00 15.92 ? 150 VAL   A N   1 
ATOM   1183 C  CA  . VAL   A 1 149 ? 5.058   -15.998 12.071  1.00 15.34 ? 150 VAL   A CA  1 
ATOM   1184 C  C   . VAL   A 1 149 ? 3.860   -16.931 12.267  1.00 16.36 ? 150 VAL   A C   1 
ATOM   1185 O  O   . VAL   A 1 149 ? 3.900   -17.906 13.044  1.00 19.59 ? 150 VAL   A O   1 
ATOM   1186 C  CB  . VAL   A 1 149 ? 6.262   -16.751 11.452  1.00 15.00 ? 150 VAL   A CB  1 
ATOM   1187 C  CG1 . VAL   A 1 149 ? 5.847   -17.484 10.183  1.00 18.90 ? 150 VAL   A CG1 1 
ATOM   1188 C  CG2 . VAL   A 1 149 ? 7.388   -15.761 11.119  1.00 18.31 ? 150 VAL   A CG2 1 
ATOM   1189 N  N   . GLY   A 1 150 ? 2.786   -16.655 11.522  1.00 14.64 ? 151 GLY   A N   1 
ATOM   1190 C  CA  . GLY   A 1 150 ? 1.600   -17.502 11.583  1.00 17.36 ? 151 GLY   A CA  1 
ATOM   1191 C  C   . GLY   A 1 150 ? 0.709   -17.068 10.434  1.00 14.30 ? 151 GLY   A C   1 
ATOM   1192 O  O   . GLY   A 1 150 ? 1.148   -17.180 9.271   1.00 16.51 ? 151 GLY   A O   1 
ATOM   1193 N  N   A SER   A 1 151 ? -0.498  -16.564 10.753  0.50 17.03 ? 152 SER   A N   1 
ATOM   1194 N  N   B SER   A 1 151 ? -0.468  -16.513 10.778  0.50 16.52 ? 152 SER   A N   1 
ATOM   1195 C  CA  A SER   A 1 151 ? -1.379  -16.043 9.713   0.50 19.29 ? 152 SER   A CA  1 
ATOM   1196 C  CA  B SER   A 1 151 ? -1.372  -15.948 9.784   0.50 17.95 ? 152 SER   A CA  1 
ATOM   1197 C  C   A SER   A 1 151 ? -0.837  -14.725 9.166   0.50 16.48 ? 152 SER   A C   1 
ATOM   1198 C  C   B SER   A 1 151 ? -0.784  -14.689 9.157   0.50 15.45 ? 152 SER   A C   1 
ATOM   1199 O  O   A SER   A 1 151 ? -0.138  -13.998 9.886   0.50 18.57 ? 152 SER   A O   1 
ATOM   1200 O  O   B SER   A 1 151 ? -0.023  -13.962 9.814   0.50 17.27 ? 152 SER   A O   1 
ATOM   1201 C  CB  A SER   A 1 151 ? -2.781  -15.872 10.221  0.50 25.42 ? 152 SER   A CB  1 
ATOM   1202 C  CB  B SER   A 1 151 ? -2.696  -15.635 10.399  0.50 18.61 ? 152 SER   A CB  1 
ATOM   1203 O  OG  A SER   A 1 151 ? -2.822  -14.868 11.225  0.50 27.99 ? 152 SER   A OG  1 
ATOM   1204 O  OG  B SER   A 1 151 ? -3.258  -16.806 10.936  0.50 21.90 ? 152 SER   A OG  1 
ATOM   1205 N  N   . ALA   A 1 152 ? -1.134  -14.455 7.884   1.00 16.16 ? 153 ALA   A N   1 
ATOM   1206 C  CA  . ALA   A 1 152 ? -0.707  -13.236 7.232   1.00 16.89 ? 153 ALA   A CA  1 
ATOM   1207 C  C   . ALA   A 1 152 ? -1.342  -12.007 7.926   1.00 15.20 ? 153 ALA   A C   1 
ATOM   1208 O  O   . ALA   A 1 152 ? -2.455  -12.068 8.475   1.00 18.73 ? 153 ALA   A O   1 
ATOM   1209 C  CB  . ALA   A 1 152 ? -1.091  -13.243 5.763   1.00 19.52 ? 153 ALA   A CB  1 
ATOM   1210 N  N   . LYS   A 1 153 ? -0.602  -10.884 7.923   1.00 16.13 ? 154 LYS   A N   1 
ATOM   1211 C  CA  . LYS   A 1 153 ? -1.132  -9.585  8.341   1.00 17.08 ? 154 LYS   A CA  1 
ATOM   1212 C  C   . LYS   A 1 153 ? -1.545  -8.799  7.111   1.00 17.00 ? 154 LYS   A C   1 
ATOM   1213 O  O   . LYS   A 1 153 ? -0.714  -8.369  6.326   1.00 16.28 ? 154 LYS   A O   1 
ATOM   1214 C  CB  . LYS   A 1 153 ? -0.077  -8.823  9.156   1.00 16.84 ? 154 LYS   A CB  1 
ATOM   1215 C  CG  . LYS   A 1 153 ? -0.594  -7.570  9.878   1.00 20.46 ? 154 LYS   A CG  1 
ATOM   1216 C  CD  . LYS   A 1 153 ? -1.397  -7.912  11.122  1.00 23.12 ? 154 LYS   A CD  1 
ATOM   1217 C  CE  . LYS   A 1 153 ? -1.633  -6.732  12.049  1.00 23.75 ? 154 LYS   A CE  1 
ATOM   1218 N  NZ  . LYS   A 1 153 ? -2.618  -7.069  13.091  1.00 29.23 ? 154 LYS   A NZ  1 
ATOM   1219 N  N   . PRO   A 1 154 ? -2.864  -8.688  6.806   1.00 17.86 ? 155 PRO   A N   1 
ATOM   1220 C  CA  . PRO   A 1 154 ? -3.266  -8.076  5.535   1.00 17.71 ? 155 PRO   A CA  1 
ATOM   1221 C  C   . PRO   A 1 154 ? -2.723  -6.646  5.351   1.00 16.20 ? 155 PRO   A C   1 
ATOM   1222 O  O   . PRO   A 1 154 ? -2.299  -6.266  4.270   1.00 19.46 ? 155 PRO   A O   1 
ATOM   1223 C  CB  . PRO   A 1 154 ? -4.825  -8.107  5.634   1.00 19.25 ? 155 PRO   A CB  1 
ATOM   1224 C  CG  . PRO   A 1 154 ? -5.111  -9.244  6.607   1.00 26.55 ? 155 PRO   A CG  1 
ATOM   1225 C  CD  . PRO   A 1 154 ? -3.976  -9.240  7.604   1.00 20.95 ? 155 PRO   A CD  1 
ATOM   1226 N  N   . GLY   A 1 155 ? -2.661  -5.915  6.457   1.00 16.69 ? 156 GLY   A N   1 
ATOM   1227 C  CA  . GLY   A 1 155 ? -2.276  -4.511  6.445   1.00 15.83 ? 156 GLY   A CA  1 
ATOM   1228 C  C   . GLY   A 1 155 ? -0.769  -4.334  6.245   1.00 16.48 ? 156 GLY   A C   1 
ATOM   1229 O  O   . GLY   A 1 155 ? -0.331  -3.231  6.049   1.00 20.06 ? 156 GLY   A O   1 
ATOM   1230 N  N   . LEU   A 1 156 ? 0.007   -5.420  6.278   1.00 18.61 ? 157 LEU   A N   1 
ATOM   1231 C  CA  . LEU   A 1 156 ? 1.425   -5.375  5.953   1.00 17.05 ? 157 LEU   A CA  1 
ATOM   1232 C  C   . LEU   A 1 156 ? 1.704   -5.600  4.474   1.00 16.44 ? 157 LEU   A C   1 
ATOM   1233 O  O   . LEU   A 1 156 ? 2.796   -5.287  4.005   1.00 15.66 ? 157 LEU   A O   1 
ATOM   1234 C  CB  . LEU   A 1 156 ? 2.172   -6.419  6.797   1.00 15.15 ? 157 LEU   A CB  1 
ATOM   1235 C  CG  . LEU   A 1 156 ? 3.702   -6.513  6.585   1.00 15.08 ? 157 LEU   A CG  1 
ATOM   1236 C  CD1 . LEU   A 1 156 ? 4.382   -5.213  7.005   1.00 17.58 ? 157 LEU   A CD1 1 
ATOM   1237 C  CD2 . LEU   A 1 156 ? 4.278   -7.706  7.384   1.00 17.42 ? 157 LEU   A CD2 1 
ATOM   1238 N  N   . GLN   A 1 157 ? 0.752   -6.219  3.728   1.00 16.46 ? 158 GLN   A N   1 
ATOM   1239 C  CA  . GLN   A 1 157 ? 1.021   -6.629  2.355   1.00 15.87 ? 158 GLN   A CA  1 
ATOM   1240 C  C   . GLN   A 1 157 ? 1.472   -5.483  1.453   1.00 14.89 ? 158 GLN   A C   1 
ATOM   1241 O  O   . GLN   A 1 157 ? 2.308   -5.691  0.582   1.00 17.30 ? 158 GLN   A O   1 
ATOM   1242 C  CB  . GLN   A 1 157 ? -0.110  -7.503  1.776   1.00 18.22 ? 158 GLN   A CB  1 
ATOM   1243 C  CG  . GLN   A 1 157 ? 0.310   -8.285  0.501   1.00 20.83 ? 158 GLN   A CG  1 
ATOM   1244 C  CD  . GLN   A 1 157 ? 1.435   -9.275  0.786   1.00 17.29 ? 158 GLN   A CD  1 
ATOM   1245 O  OE1 . GLN   A 1 157 ? 1.488   -9.849  1.900   1.00 19.03 ? 158 GLN   A OE1 1 
ATOM   1246 N  NE2 . GLN   A 1 157 ? 2.330   -9.459  -0.196  1.00 18.06 ? 158 GLN   A NE2 1 
ATOM   1247 N  N   . LYS   A 1 158 ? 0.890   -4.280  1.607   1.00 16.85 ? 159 LYS   A N   1 
ATOM   1248 C  CA  . LYS   A 1 158 ? 1.335   -3.179  0.736   1.00 18.03 ? 159 LYS   A CA  1 
ATOM   1249 C  C   . LYS   A 1 158 ? 2.838   -2.851  0.919   1.00 15.69 ? 159 LYS   A C   1 
ATOM   1250 O  O   . LYS   A 1 158 ? 3.526   -2.576  -0.054  1.00 19.42 ? 159 LYS   A O   1 
ATOM   1251 C  CB  . LYS   A 1 158 ? 0.419   -1.950  0.879   1.00 22.88 ? 159 LYS   A CB  1 
ATOM   1252 C  CG  . LYS   A 1 158 ? -0.958  -2.055  0.199   1.00 29.17 ? 159 LYS   A CG  1 
ATOM   1253 N  N   . VAL   A 1 159 ? 3.332   -3.004  2.151   1.00 16.02 ? 160 VAL   A N   1 
ATOM   1254 C  CA  . VAL   A 1 159 ? 4.763   -2.856  2.426   1.00 14.36 ? 160 VAL   A CA  1 
ATOM   1255 C  C   . VAL   A 1 159 ? 5.544   -3.992  1.751   1.00 16.32 ? 160 VAL   A C   1 
ATOM   1256 O  O   . VAL   A 1 159 ? 6.506   -3.769  1.010   1.00 15.62 ? 160 VAL   A O   1 
ATOM   1257 C  CB  . VAL   A 1 159 ? 4.984   -2.865  3.944   1.00 13.97 ? 160 VAL   A CB  1 
ATOM   1258 C  CG1 . VAL   A 1 159 ? 6.482   -2.869  4.235   1.00 14.73 ? 160 VAL   A CG1 1 
ATOM   1259 C  CG2 . VAL   A 1 159 ? 4.264   -1.696  4.614   1.00 17.54 ? 160 VAL   A CG2 1 
ATOM   1260 N  N   . VAL   A 1 160 ? 5.114   -5.246  1.960   1.00 16.64 ? 161 VAL   A N   1 
ATOM   1261 C  CA  . VAL   A 1 160 ? 5.853   -6.384  1.412   1.00 17.15 ? 161 VAL   A CA  1 
ATOM   1262 C  C   . VAL   A 1 160 ? 5.976   -6.255  -0.108  1.00 16.79 ? 161 VAL   A C   1 
ATOM   1263 O  O   . VAL   A 1 160 ? 7.017   -6.497  -0.727  1.00 18.64 ? 161 VAL   A O   1 
ATOM   1264 C  CB  . VAL   A 1 160 ? 5.126   -7.694  1.817   1.00 20.92 ? 161 VAL   A CB  1 
ATOM   1265 C  CG1 . VAL   A 1 160 ? 5.520   -8.885  0.956   1.00 23.24 ? 161 VAL   A CG1 1 
ATOM   1266 C  CG2 . VAL   A 1 160 ? 5.435   -7.965  3.292   1.00 23.91 ? 161 VAL   A CG2 1 
ATOM   1267 N  N   . ASP   A 1 161 ? 4.876   -5.845  -0.737  1.00 17.10 ? 162 ASP   A N   1 
ATOM   1268 C  CA  . ASP   A 1 161 ? 4.865   -5.854  -2.188  1.00 18.88 ? 162 ASP   A CA  1 
ATOM   1269 C  C   . ASP   A 1 161 ? 5.757   -4.775  -2.819  1.00 18.54 ? 162 ASP   A C   1 
ATOM   1270 O  O   . ASP   A 1 161 ? 6.140   -4.950  -3.972  1.00 24.87 ? 162 ASP   A O   1 
ATOM   1271 C  CB  . ASP   A 1 161 ? 3.444   -5.819  -2.697  1.00 21.65 ? 162 ASP   A CB  1 
ATOM   1272 C  CG  . ASP   A 1 161 ? 2.793   -7.196  -2.644  1.00 24.46 ? 162 ASP   A CG  1 
ATOM   1273 O  OD1 . ASP   A 1 161 ? 3.520   -8.260  -2.755  1.00 30.01 ? 162 ASP   A OD1 1 
ATOM   1274 O  OD2 . ASP   A 1 161 ? 1.611   -7.202  -2.455  1.00 31.12 ? 162 ASP   A OD2 1 
ATOM   1275 N  N   . VAL   A 1 162 ? 6.087   -3.677  -2.107  1.00 17.23 ? 163 VAL   A N   1 
ATOM   1276 C  CA  . VAL   A 1 162 ? 6.931   -2.647  -2.712  1.00 17.58 ? 163 VAL   A CA  1 
ATOM   1277 C  C   . VAL   A 1 162 ? 8.417   -2.953  -2.519  1.00 16.26 ? 163 VAL   A C   1 
ATOM   1278 O  O   . VAL   A 1 162 ? 9.228   -2.272  -3.146  1.00 17.30 ? 163 VAL   A O   1 
ATOM   1279 C  CB  . VAL   A 1 162 ? 6.563   -1.258  -2.162  1.00 19.66 ? 163 VAL   A CB  1 
ATOM   1280 C  CG1 . VAL   A 1 162 ? 7.054   -1.016  -0.769  1.00 22.49 ? 163 VAL   A CG1 1 
ATOM   1281 C  CG2 . VAL   A 1 162 ? 6.935   -0.122  -3.090  1.00 23.65 ? 163 VAL   A CG2 1 
ATOM   1282 N  N   . LEU   A 1 163 ? 8.764   -3.960  -1.664  1.00 18.38 ? 164 LEU   A N   1 
ATOM   1283 C  CA  . LEU   A 1 163 ? 10.151  -4.236  -1.346  1.00 16.02 ? 164 LEU   A CA  1 
ATOM   1284 C  C   . LEU   A 1 163 ? 10.996  -4.565  -2.576  1.00 16.59 ? 164 LEU   A C   1 
ATOM   1285 O  O   . LEU   A 1 163 ? 12.184  -4.209  -2.579  1.00 17.75 ? 164 LEU   A O   1 
ATOM   1286 C  CB  . LEU   A 1 163 ? 10.284  -5.294  -0.244  1.00 16.56 ? 164 LEU   A CB  1 
ATOM   1287 C  CG  . LEU   A 1 163 ? 9.613   -4.948  1.100   1.00 15.85 ? 164 LEU   A CG  1 
ATOM   1288 C  CD1 . LEU   A 1 163 ? 9.846   -6.036  2.140   1.00 19.08 ? 164 LEU   A CD1 1 
ATOM   1289 C  CD2 . LEU   A 1 163 ? 10.096  -3.633  1.672   1.00 15.39 ? 164 LEU   A CD2 1 
ATOM   1290 N  N   . ASP   A 1 164 ? 10.466  -5.338  -3.544  1.00 20.27 ? 165 ASP   A N   1 
ATOM   1291 C  CA  . ASP   A 1 164 ? 11.269  -5.613  -4.744  1.00 22.66 ? 165 ASP   A CA  1 
ATOM   1292 C  C   . ASP   A 1 164 ? 11.692  -4.312  -5.464  1.00 22.48 ? 165 ASP   A C   1 
ATOM   1293 O  O   . ASP   A 1 164 ? 12.637  -4.305  -6.256  1.00 26.62 ? 165 ASP   A O   1 
ATOM   1294 C  CB  . ASP   A 1 164 ? 10.656  -6.693  -5.654  1.00 35.14 ? 165 ASP   A CB  1 
ATOM   1295 C  CG  . ASP   A 1 164 ? 9.203   -6.457  -6.000  1.00 70.06 ? 165 ASP   A CG  1 
ATOM   1296 O  OD1 . ASP   A 1 164 ? 8.902   -5.303  -6.365  1.00 71.49 ? 165 ASP   A OD1 1 
ATOM   1297 O  OD2 . ASP   A 1 164 ? 8.386   -7.432  -5.901  1.00 90.07 ? 165 ASP   A OD2 1 
ATOM   1298 N  N   . SER   A 1 165 ? 11.026  -3.183  -5.205  1.00 21.10 ? 166 SER   A N   1 
ATOM   1299 C  CA  . SER   A 1 165 ? 11.426  -1.962  -5.914  1.00 19.40 ? 166 SER   A CA  1 
ATOM   1300 C  C   . SER   A 1 165 ? 12.504  -1.168  -5.155  1.00 16.69 ? 166 SER   A C   1 
ATOM   1301 O  O   . SER   A 1 165 ? 13.051  -0.161  -5.690  1.00 18.70 ? 166 SER   A O   1 
ATOM   1302 C  CB  . SER   A 1 165 ? 10.245  -1.093  -6.207  1.00 23.81 ? 166 SER   A CB  1 
ATOM   1303 O  OG  . SER   A 1 165 ? 9.756   -0.480  -5.016  1.00 22.74 ? 166 SER   A OG  1 
ATOM   1304 N  N   . ILE   A 1 166 ? 12.770  -1.575  -3.904  1.00 14.86 ? 167 ILE   A N   1 
ATOM   1305 C  CA  . ILE   A 1 166 ? 13.831  -0.934  -3.124  1.00 14.99 ? 167 ILE   A CA  1 
ATOM   1306 C  C   . ILE   A 1 166 ? 14.838  -1.956  -2.596  1.00 14.94 ? 167 ILE   A C   1 
ATOM   1307 O  O   . ILE   A 1 166 ? 15.254  -1.885  -1.440  1.00 13.80 ? 167 ILE   A O   1 
ATOM   1308 C  CB  . ILE   A 1 166 ? 13.249  -0.072  -1.981  1.00 14.94 ? 167 ILE   A CB  1 
ATOM   1309 C  CG1 . ILE   A 1 166 ? 12.409  -0.885  -0.993  1.00 14.62 ? 167 ILE   A CG1 1 
ATOM   1310 C  CG2 . ILE   A 1 166 ? 12.458  1.111   -2.563  1.00 16.99 ? 167 ILE   A CG2 1 
ATOM   1311 C  CD1 . ILE   A 1 166 ? 12.386  -0.358  0.409   1.00 17.62 ? 167 ILE   A CD1 1 
ATOM   1312 N  N   . LYS   A 1 167 ? 15.248  -2.875  -3.466  1.00 16.47 ? 168 LYS   A N   1 
ATOM   1313 C  CA  . LYS   A 1 167 ? 16.023  -4.026  -2.997  1.00 15.19 ? 168 LYS   A CA  1 
ATOM   1314 C  C   . LYS   A 1 167 ? 17.336  -3.578  -2.340  1.00 17.13 ? 168 LYS   A C   1 
ATOM   1315 O  O   . LYS   A 1 167 ? 17.698  -4.179  -1.348  1.00 15.79 ? 168 LYS   A O   1 
ATOM   1316 C  CB  . LYS   A 1 167 ? 16.279  -4.990  -4.158  1.00 16.37 ? 168 LYS   A CB  1 
ATOM   1317 C  CG  . LYS   A 1 167 ? 17.013  -6.268  -3.782  1.00 17.16 ? 168 LYS   A CG  1 
ATOM   1318 C  CD  . LYS   A 1 167 ? 17.294  -7.085  -5.075  1.00 27.71 ? 168 LYS   A CD  1 
ATOM   1319 C  CE  . LYS   A 1 167 ? 18.017  -8.383  -4.815  1.00 29.20 ? 168 LYS   A CE  1 
ATOM   1320 N  NZ  . LYS   A 1 167 ? 18.248  -9.154  -6.056  1.00 39.98 ? 168 LYS   A NZ  1 
ATOM   1321 N  N   . THR   A 1 168 ? 18.034  -2.579  -2.920  1.00 15.24 ? 169 THR   A N   1 
ATOM   1322 C  CA  . THR   A 1 168 ? 19.386  -2.256  -2.507  1.00 15.36 ? 169 THR   A CA  1 
ATOM   1323 C  C   . THR   A 1 168 ? 19.445  -0.909  -1.812  1.00 13.74 ? 169 THR   A C   1 
ATOM   1324 O  O   . THR   A 1 168 ? 18.592  -0.062  -1.965  1.00 14.91 ? 169 THR   A O   1 
ATOM   1325 C  CB  . THR   A 1 168 ? 20.303  -2.275  -3.733  1.00 16.19 ? 169 THR   A CB  1 
ATOM   1326 O  OG1 . THR   A 1 168 ? 19.678  -1.550  -4.786  1.00 17.52 ? 169 THR   A OG1 1 
ATOM   1327 C  CG2 . THR   A 1 168 ? 20.488  -3.704  -4.190  1.00 15.91 ? 169 THR   A CG2 1 
ATOM   1328 N  N   . LYS   A 1 169 ? 20.535  -0.726  -1.082  1.00 16.19 ? 170 LYS   A N   1 
ATOM   1329 C  CA  . LYS   A 1 169 ? 20.772  0.433   -0.273  1.00 15.39 ? 170 LYS   A CA  1 
ATOM   1330 C  C   . LYS   A 1 169 ? 20.646  1.698   -1.118  1.00 13.80 ? 170 LYS   A C   1 
ATOM   1331 O  O   . LYS   A 1 169 ? 21.209  1.779   -2.217  1.00 16.55 ? 170 LYS   A O   1 
ATOM   1332 C  CB  . LYS   A 1 169 ? 22.192  0.321   0.301   1.00 14.83 ? 170 LYS   A CB  1 
ATOM   1333 C  CG  . LYS   A 1 169 ? 22.671  1.570   1.036   1.00 18.10 ? 170 LYS   A CG  1 
ATOM   1334 C  CD  . LYS   A 1 169 ? 23.986  1.261   1.760   1.00 20.63 ? 170 LYS   A CD  1 
ATOM   1335 C  CE  . LYS   A 1 169 ? 25.074  0.828   0.783   1.00 28.40 ? 170 LYS   A CE  1 
ATOM   1336 N  NZ  . LYS   A 1 169 ? 26.397  0.612   1.424   1.00 35.01 ? 170 LYS   A NZ  1 
ATOM   1337 N  N   . GLY   A 1 170 ? 19.839  2.636   -0.585  1.00 14.81 ? 171 GLY   A N   1 
ATOM   1338 C  CA  . GLY   A 1 170 ? 19.706  3.979   -1.161  1.00 14.65 ? 171 GLY   A CA  1 
ATOM   1339 C  C   . GLY   A 1 170 ? 18.568  4.062   -2.193  1.00 15.65 ? 171 GLY   A C   1 
ATOM   1340 O  O   . GLY   A 1 170 ? 18.195  5.161   -2.640  1.00 19.54 ? 171 GLY   A O   1 
ATOM   1341 N  N   . LYS   A 1 171 ? 17.932  2.932   -2.536  1.00 13.50 ? 172 LYS   A N   1 
ATOM   1342 C  CA  . LYS   A 1 171 ? 16.720  2.985   -3.344  1.00 15.06 ? 172 LYS   A CA  1 
ATOM   1343 C  C   . LYS   A 1 171 ? 15.511  3.430   -2.522  1.00 15.43 ? 172 LYS   A C   1 
ATOM   1344 O  O   . LYS   A 1 171 ? 15.346  3.100   -1.363  1.00 16.03 ? 172 LYS   A O   1 
ATOM   1345 C  CB  . LYS   A 1 171 ? 16.452  1.639   -4.027  1.00 16.65 ? 172 LYS   A CB  1 
ATOM   1346 C  CG  . LYS   A 1 171 ? 17.471  1.289   -5.091  1.00 19.10 ? 172 LYS   A CG  1 
ATOM   1347 C  CD  . LYS   A 1 171 ? 17.053  0.168   -6.093  1.00 26.70 ? 172 LYS   A CD  1 
ATOM   1348 C  CE  . LYS   A 1 171 ? 15.858  0.499   -7.002  1.00 28.19 ? 172 LYS   A CE  1 
ATOM   1349 N  NZ  . LYS   A 1 171 ? 15.397  -0.633  -7.869  1.00 28.66 ? 172 LYS   A NZ  1 
ATOM   1350 N  N   . SER   A 1 172 ? 14.661  4.219   -3.170  1.00 15.99 ? 173 SER   A N   1 
ATOM   1351 C  CA  . SER   A 1 172 ? 13.416  4.635   -2.557  1.00 15.88 ? 173 SER   A CA  1 
ATOM   1352 C  C   . SER   A 1 172 ? 12.269  4.458   -3.563  1.00 15.52 ? 173 SER   A C   1 
ATOM   1353 O  O   . SER   A 1 172 ? 12.465  4.420   -4.791  1.00 17.16 ? 173 SER   A O   1 
ATOM   1354 C  CB  . SER   A 1 172 ? 13.521  6.102   -2.109  1.00 17.10 ? 173 SER   A CB  1 
ATOM   1355 O  OG  . SER   A 1 172 ? 13.712  6.980   -3.211  1.00 20.60 ? 173 SER   A OG  1 
ATOM   1356 N  N   . ALA   A 1 173 ? 11.043  4.494   -3.025  1.00 16.98 ? 174 ALA   A N   1 
ATOM   1357 C  CA  . ALA   A 1 173 ? 9.858   4.427   -3.876  1.00 18.18 ? 174 ALA   A CA  1 
ATOM   1358 C  C   . ALA   A 1 173 ? 8.735   5.250   -3.226  1.00 16.57 ? 174 ALA   A C   1 
ATOM   1359 O  O   . ALA   A 1 173 ? 8.601   5.322   -2.001  1.00 14.95 ? 174 ALA   A O   1 
ATOM   1360 C  CB  . ALA   A 1 173 ? 9.447   2.983   -4.114  1.00 18.19 ? 174 ALA   A CB  1 
ATOM   1361 N  N   . ASP   A 1 174 ? 7.883   5.830   -4.092  1.00 17.54 ? 175 ASP   A N   1 
ATOM   1362 C  CA  . ASP   A 1 174 ? 6.702   6.531   -3.607  1.00 19.24 ? 175 ASP   A CA  1 
ATOM   1363 C  C   . ASP   A 1 174 ? 5.887   5.543   -2.760  1.00 16.58 ? 175 ASP   A C   1 
ATOM   1364 O  O   . ASP   A 1 174 ? 5.770   4.355   -3.082  1.00 21.11 ? 175 ASP   A O   1 
ATOM   1365 C  CB  . ASP   A 1 174 ? 5.885   7.144   -4.773  1.00 24.38 ? 175 ASP   A CB  1 
ATOM   1366 C  CG  . ASP   A 1 174 ? 6.658   8.258   -5.498  1.00 29.70 ? 175 ASP   A CG  1 
ATOM   1367 O  OD1 . ASP   A 1 174 ? 7.236   9.118   -4.818  1.00 45.66 ? 175 ASP   A OD1 1 
ATOM   1368 O  OD2 . ASP   A 1 174 ? 6.700   8.260   -6.757  1.00 42.09 ? 175 ASP   A OD2 1 
ATOM   1369 N  N   . PHE   A 1 175 ? 5.363   6.019   -1.631  1.00 16.04 ? 176 PHE   A N   1 
ATOM   1370 C  CA  . PHE   A 1 175 ? 4.615   5.120   -0.756  1.00 16.99 ? 176 PHE   A CA  1 
ATOM   1371 C  C   . PHE   A 1 175 ? 3.571   5.925   -0.006  1.00 14.34 ? 176 PHE   A C   1 
ATOM   1372 O  O   . PHE   A 1 175 ? 3.626   6.067   1.201   1.00 19.45 ? 176 PHE   A O   1 
ATOM   1373 C  CB  . PHE   A 1 175 ? 5.543   4.375   0.199   1.00 16.43 ? 176 PHE   A CB  1 
ATOM   1374 C  CG  . PHE   A 1 175 ? 4.970   3.072   0.733   1.00 15.29 ? 176 PHE   A CG  1 
ATOM   1375 C  CD1 . PHE   A 1 175 ? 4.655   2.035   -0.132  1.00 18.50 ? 176 PHE   A CD1 1 
ATOM   1376 C  CD2 . PHE   A 1 175 ? 4.612   2.932   2.069   1.00 14.98 ? 176 PHE   A CD2 1 
ATOM   1377 C  CE1 . PHE   A 1 175 ? 4.079   0.865   0.361   1.00 18.57 ? 176 PHE   A CE1 1 
ATOM   1378 C  CE2 . PHE   A 1 175 ? 4.030   1.766   2.584   1.00 16.65 ? 176 PHE   A CE2 1 
ATOM   1379 C  CZ  . PHE   A 1 175 ? 3.802   0.718   1.709   1.00 19.35 ? 176 PHE   A CZ  1 
ATOM   1380 N  N   . THR   A 1 176 ? 2.565   6.396   -0.755  1.00 19.25 ? 177 THR   A N   1 
ATOM   1381 C  CA  . THR   A 1 176 ? 1.545   7.262   -0.189  1.00 17.24 ? 177 THR   A CA  1 
ATOM   1382 C  C   . THR   A 1 176 ? 0.345   6.429   0.238   1.00 14.81 ? 177 THR   A C   1 
ATOM   1383 O  O   . THR   A 1 176 ? 0.170   5.307   -0.264  1.00 16.74 ? 177 THR   A O   1 
ATOM   1384 C  CB  . THR   A 1 176 ? 1.104   8.348   -1.189  1.00 18.83 ? 177 THR   A CB  1 
ATOM   1385 O  OG1 . THR   A 1 176 ? 0.594   7.768   -2.374  1.00 22.29 ? 177 THR   A OG1 1 
ATOM   1386 C  CG2 . THR   A 1 176 ? 2.148   9.387   -1.500  1.00 24.20 ? 177 THR   A CG2 1 
ATOM   1387 N  N   . ASN   A 1 177 ? -0.466  7.023   1.110   1.00 15.36 ? 178 ASN   A N   1 
ATOM   1388 C  CA  . ASN   A 1 177 ? -1.762  6.488   1.530   1.00 16.44 ? 178 ASN   A CA  1 
ATOM   1389 C  C   . ASN   A 1 177 ? -1.629  5.160   2.252   1.00 15.15 ? 178 ASN   A C   1 
ATOM   1390 O  O   . ASN   A 1 177 ? -2.565  4.371   2.250   1.00 19.19 ? 178 ASN   A O   1 
ATOM   1391 C  CB  . ASN   A 1 177 ? -2.730  6.382   0.353   1.00 17.00 ? 178 ASN   A CB  1 
ATOM   1392 C  CG  . ASN   A 1 177 ? -2.929  7.759   -0.257  1.00 16.63 ? 178 ASN   A CG  1 
ATOM   1393 O  OD1 . ASN   A 1 177 ? -3.655  8.584   0.317   1.00 19.52 ? 178 ASN   A OD1 1 
ATOM   1394 N  ND2 . ASN   A 1 177 ? -2.297  8.021   -1.398  1.00 18.94 ? 178 ASN   A ND2 1 
ATOM   1395 N  N   . PHE   A 1 178 ? -0.500  4.902   2.903   1.00 15.09 ? 179 PHE   A N   1 
ATOM   1396 C  CA  . PHE   A 1 178 ? -0.401  3.659   3.668   1.00 15.20 ? 179 PHE   A CA  1 
ATOM   1397 C  C   . PHE   A 1 178 ? -0.917  3.931   5.086   1.00 14.09 ? 179 PHE   A C   1 
ATOM   1398 O  O   . PHE   A 1 178 ? -0.505  4.913   5.718   1.00 19.17 ? 179 PHE   A O   1 
ATOM   1399 C  CB  . PHE   A 1 178 ? 1.059   3.207   3.760   1.00 15.78 ? 179 PHE   A CB  1 
ATOM   1400 C  CG  . PHE   A 1 178 ? 1.226   1.951   4.586   1.00 14.39 ? 179 PHE   A CG  1 
ATOM   1401 C  CD1 . PHE   A 1 178 ? 0.774   0.723   4.084   1.00 15.77 ? 179 PHE   A CD1 1 
ATOM   1402 C  CD2 . PHE   A 1 178 ? 1.562   2.019   5.939   1.00 14.01 ? 179 PHE   A CD2 1 
ATOM   1403 C  CE1 . PHE   A 1 178 ? 0.818   -0.421  4.876   1.00 19.26 ? 179 PHE   A CE1 1 
ATOM   1404 C  CE2 . PHE   A 1 178 ? 1.628   0.857   6.739   1.00 14.66 ? 179 PHE   A CE2 1 
ATOM   1405 C  CZ  . PHE   A 1 178 ? 1.215   -0.346  6.214   1.00 15.15 ? 179 PHE   A CZ  1 
ATOM   1406 N  N   . ASP   A 1 179 ? -1.762  3.040   5.627   1.00 17.05 ? 180 ASP   A N   1 
ATOM   1407 C  CA  . ASP   A 1 179 ? -2.401  3.292   6.906   1.00 13.57 ? 180 ASP   A CA  1 
ATOM   1408 C  C   . ASP   A 1 179 ? -1.740  2.446   7.990   1.00 14.67 ? 180 ASP   A C   1 
ATOM   1409 O  O   . ASP   A 1 179 ? -1.930  1.206   8.030   1.00 15.44 ? 180 ASP   A O   1 
ATOM   1410 C  CB  . ASP   A 1 179 ? -3.891  2.964   6.808   1.00 16.50 ? 180 ASP   A CB  1 
ATOM   1411 C  CG  . ASP   A 1 179 ? -4.655  3.335   8.075   1.00 18.91 ? 180 ASP   A CG  1 
ATOM   1412 O  OD1 . ASP   A 1 179 ? -4.045  3.624   9.121   1.00 18.83 ? 180 ASP   A OD1 1 
ATOM   1413 O  OD2 . ASP   A 1 179 ? -5.878  3.300   8.013   1.00 29.06 ? 180 ASP   A OD2 1 
ATOM   1414 N  N   . PRO   A 1 180 ? -0.930  3.043   8.910   1.00 13.14 ? 181 PRO   A N   1 
ATOM   1415 C  CA  . PRO   A 1 180 ? -0.186  2.245   9.882   1.00 14.86 ? 181 PRO   A CA  1 
ATOM   1416 C  C   . PRO   A 1 180 ? -1.085  1.591   10.930  1.00 14.53 ? 181 PRO   A C   1 
ATOM   1417 O  O   . PRO   A 1 180 ? -0.661  0.738   11.714  1.00 14.81 ? 181 PRO   A O   1 
ATOM   1418 C  CB  . PRO   A 1 180 ? 0.835   3.211   10.519  1.00 15.48 ? 181 PRO   A CB  1 
ATOM   1419 C  CG  . PRO   A 1 180 ? 0.154   4.559   10.333  1.00 14.64 ? 181 PRO   A CG  1 
ATOM   1420 C  CD  . PRO   A 1 180 ? -0.578  4.461   9.012   1.00 14.23 ? 181 PRO   A CD  1 
ATOM   1421 N  N   . ARG   A 1 181 ? -2.358  2.003   10.979  1.00 13.43 ? 182 ARG   A N   1 
ATOM   1422 C  CA  . ARG   A 1 181 ? -3.302  1.354   11.919  1.00 14.30 ? 182 ARG   A CA  1 
ATOM   1423 C  C   . ARG   A 1 181 ? -3.412  -0.131  11.599  1.00 15.72 ? 182 ARG   A C   1 
ATOM   1424 O  O   . ARG   A 1 181 ? -3.755  -0.891  12.513  1.00 18.10 ? 182 ARG   A O   1 
ATOM   1425 C  CB  . ARG   A 1 181 ? -4.700  1.979   11.867  1.00 16.88 ? 182 ARG   A CB  1 
ATOM   1426 C  CG  . ARG   A 1 181 ? -4.708  3.427   12.329  1.00 17.90 ? 182 ARG   A CG  1 
ATOM   1427 C  CD  . ARG   A 1 181 ? -6.081  4.065   12.323  1.00 18.63 ? 182 ARG   A CD  1 
ATOM   1428 N  NE  . ARG   A 1 181 ? -6.435  4.284   10.937  1.00 18.10 ? 182 ARG   A NE  1 
ATOM   1429 C  CZ  . ARG   A 1 181 ? -7.510  4.968   10.600  1.00 25.85 ? 182 ARG   A CZ  1 
ATOM   1430 N  NH1 . ARG   A 1 181 ? -8.247  5.514   11.559  1.00 28.12 ? 182 ARG   A NH1 1 
ATOM   1431 N  NH2 . ARG   A 1 181 ? -7.803  5.156   9.322   1.00 28.07 ? 182 ARG   A NH2 1 
ATOM   1432 N  N   . GLY   A 1 182 ? -3.164  -0.508  10.331  1.00 14.78 ? 183 GLY   A N   1 
ATOM   1433 C  CA  . GLY   A 1 182 ? -3.245  -1.925  9.965   1.00 16.69 ? 183 GLY   A CA  1 
ATOM   1434 C  C   . GLY   A 1 182 ? -2.120  -2.782  10.525  1.00 15.27 ? 183 GLY   A C   1 
ATOM   1435 O  O   . GLY   A 1 182 ? -2.169  -4.004  10.313  1.00 20.32 ? 183 GLY   A O   1 
ATOM   1436 N  N   . LEU   A 1 183 ? -1.150  -2.174  11.238  1.00 16.31 ? 184 LEU   A N   1 
ATOM   1437 C  CA  . LEU   A 1 183 ? -0.027  -2.937  11.801  1.00 14.67 ? 184 LEU   A CA  1 
ATOM   1438 C  C   . LEU   A 1 183 ? -0.161  -3.073  13.308  1.00 15.06 ? 184 LEU   A C   1 
ATOM   1439 O  O   . LEU   A 1 183 ? 0.725   -3.675  13.923  1.00 17.95 ? 184 LEU   A O   1 
ATOM   1440 C  CB  . LEU   A 1 183 ? 1.302   -2.275  11.484  1.00 14.23 ? 184 LEU   A CB  1 
ATOM   1441 C  CG  . LEU   A 1 183 ? 1.574   -2.107  9.993   1.00 15.30 ? 184 LEU   A CG  1 
ATOM   1442 C  CD1 . LEU   A 1 183 ? 2.799   -1.271  9.796   1.00 18.11 ? 184 LEU   A CD1 1 
ATOM   1443 C  CD2 . LEU   A 1 183 ? 1.701   -3.469  9.299   1.00 20.88 ? 184 LEU   A CD2 1 
ATOM   1444 N  N   . LEU   A 1 184 ? -1.296  -2.634  13.884  1.00 15.13 ? 185 LEU   A N   1 
ATOM   1445 C  CA  . LEU   A 1 184 ? -1.411  -2.647  15.331  1.00 14.04 ? 185 LEU   A CA  1 
ATOM   1446 C  C   . LEU   A 1 184 ? -2.087  -3.964  15.736  1.00 15.93 ? 185 LEU   A C   1 
ATOM   1447 O  O   . LEU   A 1 184 ? -2.947  -4.501  15.013  1.00 21.93 ? 185 LEU   A O   1 
ATOM   1448 C  CB  . LEU   A 1 184 ? -2.283  -1.480  15.851  1.00 14.70 ? 185 LEU   A CB  1 
ATOM   1449 C  CG  . LEU   A 1 184 ? -1.735  -0.110  15.484  1.00 15.57 ? 185 LEU   A CG  1 
ATOM   1450 C  CD1 . LEU   A 1 184 ? -2.685  0.999   15.910  1.00 18.93 ? 185 LEU   A CD1 1 
ATOM   1451 C  CD2 . LEU   A 1 184 ? -0.365  0.089   16.105  1.00 16.52 ? 185 LEU   A CD2 1 
ATOM   1452 N  N   . PRO   A 1 185 ? -1.796  -4.492  16.940  1.00 14.73 ? 186 PRO   A N   1 
ATOM   1453 C  CA  . PRO   A 1 185 ? -2.529  -5.640  17.463  1.00 14.61 ? 186 PRO   A CA  1 
ATOM   1454 C  C   . PRO   A 1 185 ? -3.836  -5.133  18.047  1.00 15.38 ? 186 PRO   A C   1 
ATOM   1455 O  O   . PRO   A 1 185 ? -4.089  -3.928  18.069  1.00 16.44 ? 186 PRO   A O   1 
ATOM   1456 C  CB  . PRO   A 1 185 ? -1.604  -6.173  18.554  1.00 16.60 ? 186 PRO   A CB  1 
ATOM   1457 C  CG  . PRO   A 1 185 ? -0.895  -4.905  19.076  1.00 14.64 ? 186 PRO   A CG  1 
ATOM   1458 C  CD  . PRO   A 1 185 ? -0.661  -4.076  17.807  1.00 15.17 ? 186 PRO   A CD  1 
ATOM   1459 N  N   . GLU   A 1 186 ? -4.660  -6.041  18.557  1.00 17.18 ? 187 GLU   A N   1 
ATOM   1460 C  CA  . GLU   A 1 186 ? -5.942  -5.665  19.130  1.00 16.31 ? 187 GLU   A CA  1 
ATOM   1461 C  C   . GLU   A 1 186 ? -5.763  -4.877  20.437  1.00 17.12 ? 187 GLU   A C   1 
ATOM   1462 O  O   . GLU   A 1 186 ? -6.388  -3.819  20.638  1.00 18.71 ? 187 GLU   A O   1 
ATOM   1463 C  CB  . GLU   A 1 186 ? -6.733  -6.967  19.283  1.00 20.23 ? 187 GLU   A CB  1 
ATOM   1464 C  CG  . GLU   A 1 186 ? -7.943  -6.794  20.139  1.00 22.57 ? 187 GLU   A CG  1 
ATOM   1465 C  CD  . GLU   A 1 186 ? -8.586  -8.154  20.482  1.00 20.72 ? 187 GLU   A CD  1 
ATOM   1466 O  OE1 . GLU   A 1 186 ? -9.333  -8.212  21.505  1.00 29.55 ? 187 GLU   A OE1 1 
ATOM   1467 O  OE2 . GLU   A 1 186 ? -8.389  -9.103  19.708  1.00 26.14 ? 187 GLU   A OE2 1 
ATOM   1468 N  N   . SER   A 1 187 ? -4.869  -5.337  21.318  1.00 14.75 ? 188 SER   A N   1 
ATOM   1469 C  CA  . SER   A 1 187 ? -4.665  -4.750  22.645  1.00 16.38 ? 188 SER   A CA  1 
ATOM   1470 C  C   . SER   A 1 187 ? -3.509  -3.750  22.613  1.00 16.35 ? 188 SER   A C   1 
ATOM   1471 O  O   . SER   A 1 187 ? -2.474  -4.034  22.030  1.00 17.16 ? 188 SER   A O   1 
ATOM   1472 C  CB  . SER   A 1 187 ? -4.285  -5.818  23.638  1.00 17.35 ? 188 SER   A CB  1 
ATOM   1473 O  OG  . SER   A 1 187 ? -4.049  -5.253  24.922  1.00 17.14 ? 188 SER   A OG  1 
ATOM   1474 N  N   . LEU   A 1 188 ? -3.672  -2.635  23.341  1.00 14.57 ? 189 LEU   A N   1 
ATOM   1475 C  CA  . LEU   A 1 188 ? -2.565  -1.690  23.505  1.00 14.17 ? 189 LEU   A CA  1 
ATOM   1476 C  C   . LEU   A 1 188 ? -1.924  -1.785  24.897  1.00 13.87 ? 189 LEU   A C   1 
ATOM   1477 O  O   . LEU   A 1 188 ? -1.229  -0.864  25.350  1.00 17.17 ? 189 LEU   A O   1 
ATOM   1478 C  CB  . LEU   A 1 188 ? -3.091  -0.245  23.300  1.00 15.77 ? 189 LEU   A CB  1 
ATOM   1479 C  CG  . LEU   A 1 188 ? -3.609  0.068   21.889  1.00 18.99 ? 189 LEU   A CG  1 
ATOM   1480 C  CD1 . LEU   A 1 188 ? -4.130  1.503   21.761  1.00 22.02 ? 189 LEU   A CD1 1 
ATOM   1481 C  CD2 . LEU   A 1 188 ? -2.571  -0.238  20.807  1.00 22.68 ? 189 LEU   A CD2 1 
ATOM   1482 N  N   . ASP   A 1 189 ? -2.104  -2.899  25.622  1.00 16.36 ? 190 ASP   A N   1 
ATOM   1483 C  CA  . ASP   A 1 189 ? -1.348  -3.122  26.843  1.00 15.37 ? 190 ASP   A CA  1 
ATOM   1484 C  C   . ASP   A 1 189 ? 0.156   -3.082  26.529  1.00 14.65 ? 190 ASP   A C   1 
ATOM   1485 O  O   . ASP   A 1 189 ? 0.568   -3.574  25.479  1.00 14.59 ? 190 ASP   A O   1 
ATOM   1486 C  CB  . ASP   A 1 189 ? -1.652  -4.501  27.405  1.00 17.08 ? 190 ASP   A CB  1 
ATOM   1487 C  CG  . ASP   A 1 189 ? -3.025  -4.621  28.029  1.00 22.66 ? 190 ASP   A CG  1 
ATOM   1488 O  OD1 . ASP   A 1 189 ? -3.696  -3.568  28.231  1.00 26.63 ? 190 ASP   A OD1 1 
ATOM   1489 O  OD2 . ASP   A 1 189 ? -3.398  -5.767  28.351  1.00 28.20 ? 190 ASP   A OD2 1 
ATOM   1490 N  N   . TYR   A 1 190 ? 0.953   -2.471  27.427  1.00 14.24 ? 191 TYR   A N   1 
ATOM   1491 C  CA  . TYR   A 1 190 ? 2.351   -2.260  27.080  1.00 12.70 ? 191 TYR   A CA  1 
ATOM   1492 C  C   . TYR   A 1 190 ? 3.243   -2.316  28.324  1.00 13.60 ? 191 TYR   A C   1 
ATOM   1493 O  O   . TYR   A 1 190 ? 2.810   -2.183  29.460  1.00 14.47 ? 191 TYR   A O   1 
ATOM   1494 C  CB  . TYR   A 1 190 ? 2.514   -0.888  26.419  1.00 13.58 ? 191 TYR   A CB  1 
ATOM   1495 C  CG  . TYR   A 1 190 ? 2.118   0.252   27.322  1.00 14.25 ? 191 TYR   A CG  1 
ATOM   1496 C  CD1 . TYR   A 1 190 ? 3.034   0.884   28.173  1.00 15.88 ? 191 TYR   A CD1 1 
ATOM   1497 C  CD2 . TYR   A 1 190 ? 0.842   0.788   27.270  1.00 15.89 ? 191 TYR   A CD2 1 
ATOM   1498 C  CE1 . TYR   A 1 190 ? 2.648   1.946   28.987  1.00 16.04 ? 191 TYR   A CE1 1 
ATOM   1499 C  CE2 . TYR   A 1 190 ? 0.468   1.889   28.036  1.00 14.95 ? 191 TYR   A CE2 1 
ATOM   1500 C  CZ  . TYR   A 1 190 ? 1.366   2.483   28.904  1.00 16.14 ? 191 TYR   A CZ  1 
ATOM   1501 O  OH  . TYR   A 1 190 ? 0.971   3.471   29.765  1.00 17.12 ? 191 TYR   A OH  1 
ATOM   1502 N  N   . TRP   A 1 191 ? 4.535   -2.451  28.018  1.00 13.10 ? 192 TRP   A N   1 
ATOM   1503 C  CA  . TRP   A 1 191 ? 5.615   -2.203  28.977  1.00 12.23 ? 192 TRP   A CA  1 
ATOM   1504 C  C   . TRP   A 1 191 ? 6.286   -0.902  28.565  1.00 12.39 ? 192 TRP   A C   1 
ATOM   1505 O  O   . TRP   A 1 191 ? 6.315   -0.569  27.382  1.00 14.39 ? 192 TRP   A O   1 
ATOM   1506 C  CB  . TRP   A 1 191 ? 6.629   -3.318  28.934  1.00 13.73 ? 192 TRP   A CB  1 
ATOM   1507 C  CG  . TRP   A 1 191 ? 6.120   -4.657  29.375  1.00 12.48 ? 192 TRP   A CG  1 
ATOM   1508 C  CD1 . TRP   A 1 191 ? 5.880   -5.027  30.653  1.00 12.04 ? 192 TRP   A CD1 1 
ATOM   1509 C  CD2 . TRP   A 1 191 ? 5.872   -5.807  28.548  1.00 12.93 ? 192 TRP   A CD2 1 
ATOM   1510 N  NE1 . TRP   A 1 191 ? 5.528   -6.364  30.685  1.00 13.69 ? 192 TRP   A NE1 1 
ATOM   1511 C  CE2 . TRP   A 1 191 ? 5.481   -6.846  29.405  1.00 15.00 ? 192 TRP   A CE2 1 
ATOM   1512 C  CE3 . TRP   A 1 191 ? 5.936   -6.027  27.163  1.00 13.23 ? 192 TRP   A CE3 1 
ATOM   1513 C  CZ2 . TRP   A 1 191 ? 5.198   -8.137  28.906  1.00 14.95 ? 192 TRP   A CZ2 1 
ATOM   1514 C  CZ3 . TRP   A 1 191 ? 5.656   -7.295  26.663  1.00 13.28 ? 192 TRP   A CZ3 1 
ATOM   1515 C  CH2 . TRP   A 1 191 ? 5.250   -8.302  27.549  1.00 14.27 ? 192 TRP   A CH2 1 
ATOM   1516 N  N   . THR   A 1 192 ? 6.871   -0.196  29.544  1.00 12.07 ? 193 THR   A N   1 
ATOM   1517 C  CA  . THR   A 1 192 ? 7.576   1.029   29.196  1.00 12.10 ? 193 THR   A CA  1 
ATOM   1518 C  C   . THR   A 1 192 ? 8.852   1.144   30.044  1.00 11.06 ? 193 THR   A C   1 
ATOM   1519 O  O   . THR   A 1 192 ? 8.866   0.800   31.223  1.00 12.32 ? 193 THR   A O   1 
ATOM   1520 C  CB  . THR   A 1 192 ? 6.651   2.245   29.292  1.00 10.78 ? 193 THR   A CB  1 
ATOM   1521 O  OG1 . THR   A 1 192 ? 7.348   3.444   28.901  1.00 13.32 ? 193 THR   A OG1 1 
ATOM   1522 C  CG2 . THR   A 1 192 ? 6.088   2.442   30.687  1.00 12.51 ? 193 THR   A CG2 1 
ATOM   1523 N  N   . TYR   A 1 193 ? 9.881   1.783   29.457  1.00 12.74 ? 194 TYR   A N   1 
ATOM   1524 C  CA  . TYR   A 1 193 ? 11.080  2.062   30.225  1.00 11.95 ? 194 TYR   A CA  1 
ATOM   1525 C  C   . TYR   A 1 193 ? 11.838  3.116   29.427  1.00 11.75 ? 194 TYR   A C   1 
ATOM   1526 O  O   . TYR   A 1 193 ? 11.659  3.249   28.218  1.00 11.42 ? 194 TYR   A O   1 
ATOM   1527 C  CB  . TYR   A 1 193 ? 11.957  0.779   30.388  1.00 10.75 ? 194 TYR   A CB  1 
ATOM   1528 C  CG  . TYR   A 1 193 ? 12.628  0.351   29.114  1.00 10.52 ? 194 TYR   A CG  1 
ATOM   1529 C  CD1 . TYR   A 1 193 ? 11.980  -0.402  28.117  1.00 11.58 ? 194 TYR   A CD1 1 
ATOM   1530 C  CD2 . TYR   A 1 193 ? 13.982  0.688   28.886  1.00 11.74 ? 194 TYR   A CD2 1 
ATOM   1531 C  CE1 . TYR   A 1 193 ? 12.582  -0.716  26.909  1.00 10.87 ? 194 TYR   A CE1 1 
ATOM   1532 C  CE2 . TYR   A 1 193 ? 14.613  0.346   27.688  1.00 12.21 ? 194 TYR   A CE2 1 
ATOM   1533 C  CZ  . TYR   A 1 193 ? 13.940  -0.387  26.709  1.00 10.07 ? 194 TYR   A CZ  1 
ATOM   1534 O  OH  . TYR   A 1 193 ? 14.558  -0.704  25.536  1.00 11.51 ? 194 TYR   A OH  1 
ATOM   1535 N  N   . PRO   A 1 194 ? 12.797  3.834   30.091  1.00 11.14 ? 195 PRO   A N   1 
ATOM   1536 C  CA  . PRO   A 1 194 ? 13.624  4.838   29.402  1.00 12.84 ? 195 PRO   A CA  1 
ATOM   1537 C  C   . PRO   A 1 194 ? 14.828  4.183   28.730  1.00 12.16 ? 195 PRO   A C   1 
ATOM   1538 O  O   . PRO   A 1 194 ? 15.525  3.402   29.392  1.00 13.46 ? 195 PRO   A O   1 
ATOM   1539 C  CB  . PRO   A 1 194 ? 14.165  5.717   30.563  1.00 15.62 ? 195 PRO   A CB  1 
ATOM   1540 C  CG  . PRO   A 1 194 ? 14.153  4.820   31.806  1.00 13.80 ? 195 PRO   A CG  1 
ATOM   1541 C  CD  . PRO   A 1 194 ? 13.034  3.809   31.540  1.00 12.87 ? 195 PRO   A CD  1 
ATOM   1542 N  N   . GLY   A 1 195 ? 15.077  4.514   27.446  1.00 11.07 ? 196 GLY   A N   1 
ATOM   1543 C  CA  . GLY   A 1 195 ? 16.202  3.873   26.775  1.00 13.15 ? 196 GLY   A CA  1 
ATOM   1544 C  C   . GLY   A 1 195 ? 16.762  4.729   25.667  1.00 10.66 ? 196 GLY   A C   1 
ATOM   1545 O  O   . GLY   A 1 195 ? 16.823  5.986   25.801  1.00 11.81 ? 196 GLY   A O   1 
ATOM   1546 N  N   . SER   A 1 196 ? 17.132  4.089   24.575  1.00 12.06 ? 197 SER   A N   1 
ATOM   1547 C  CA  . SER   A 1 196 ? 17.961  4.701   23.535  1.00 11.99 ? 197 SER   A CA  1 
ATOM   1548 C  C   . SER   A 1 196 ? 17.515  4.304   22.134  1.00 10.42 ? 197 SER   A C   1 
ATOM   1549 O  O   . SER   A 1 196 ? 16.720  3.352   21.973  1.00 11.43 ? 197 SER   A O   1 
ATOM   1550 C  CB  . SER   A 1 196 ? 19.450  4.335   23.681  1.00 13.14 ? 197 SER   A CB  1 
ATOM   1551 O  OG  . SER   A 1 196 ? 19.671  2.938   23.296  1.00 12.34 ? 197 SER   A OG  1 
ATOM   1552 N  N   . LEU   A 1 197 ? 18.010  4.992   21.120  1.00 11.40 ? 198 LEU   A N   1 
ATOM   1553 C  CA  . LEU   A 1 197 ? 18.013  4.445   19.772  1.00 11.05 ? 198 LEU   A CA  1 
ATOM   1554 C  C   . LEU   A 1 197 ? 18.801  3.129   19.820  1.00 13.18 ? 198 LEU   A C   1 
ATOM   1555 O  O   . LEU   A 1 197 ? 19.756  2.978   20.611  1.00 13.30 ? 198 LEU   A O   1 
ATOM   1556 C  CB  . LEU   A 1 197 ? 18.751  5.411   18.863  1.00 13.58 ? 198 LEU   A CB  1 
ATOM   1557 C  CG  . LEU   A 1 197 ? 18.109  6.793   18.770  1.00 12.26 ? 198 LEU   A CG  1 
ATOM   1558 C  CD1 . LEU   A 1 197 ? 18.999  7.725   17.941  1.00 17.06 ? 198 LEU   A CD1 1 
ATOM   1559 C  CD2 . LEU   A 1 197 ? 16.699  6.732   18.189  1.00 15.38 ? 198 LEU   A CD2 1 
ATOM   1560 N  N   . THR   A 1 198 ? 18.428  2.174   18.959  1.00 10.63 ? 199 THR   A N   1 
ATOM   1561 C  CA  . THR   A 1 198 ? 19.134  0.901   18.902  1.00 11.36 ? 199 THR   A CA  1 
ATOM   1562 C  C   . THR   A 1 198 ? 20.077  0.829   17.718  1.00 12.32 ? 199 THR   A C   1 
ATOM   1563 O  O   . THR   A 1 198 ? 20.750  -0.183  17.558  1.00 13.07 ? 199 THR   A O   1 
ATOM   1564 C  CB  . THR   A 1 198 ? 18.126  -0.265  18.856  1.00 11.27 ? 199 THR   A CB  1 
ATOM   1565 O  OG1 . THR   A 1 198 ? 17.537  -0.312  17.542  1.00 12.56 ? 199 THR   A OG1 1 
ATOM   1566 C  CG2 . THR   A 1 198 ? 17.180  -0.244  20.047  1.00 12.58 ? 199 THR   A CG2 1 
ATOM   1567 N  N   . THR   A 1 199 ? 20.285  1.928   16.982  1.00 12.63 ? 200 THR   A N   1 
ATOM   1568 C  CA  . THR   A 1 199 ? 21.334  1.975   15.986  1.00 14.21 ? 200 THR   A CA  1 
ATOM   1569 C  C   . THR   A 1 199 ? 22.135  3.222   16.295  1.00 12.63 ? 200 THR   A C   1 
ATOM   1570 O  O   . THR   A 1 199 ? 21.593  4.138   16.902  1.00 13.77 ? 200 THR   A O   1 
ATOM   1571 C  CB  . THR   A 1 199 ? 20.776  2.165   14.567  1.00 13.91 ? 200 THR   A CB  1 
ATOM   1572 O  OG1 . THR   A 1 199 ? 19.943  3.340   14.529  1.00 16.98 ? 200 THR   A OG1 1 
ATOM   1573 C  CG2 . THR   A 1 199 ? 19.929  0.988   14.153  1.00 15.85 ? 200 THR   A CG2 1 
ATOM   1574 N  N   . PRO   A 1 200 ? 23.421  3.306   15.869  1.00 13.88 ? 201 PRO   A N   1 
ATOM   1575 C  CA  . PRO   A 1 200 ? 24.150  4.577   15.977  1.00 12.87 ? 201 PRO   A CA  1 
ATOM   1576 C  C   . PRO   A 1 200 ? 23.233  5.673   15.431  1.00 14.16 ? 201 PRO   A C   1 
ATOM   1577 O  O   . PRO   A 1 200 ? 22.640  5.496   14.355  1.00 15.54 ? 201 PRO   A O   1 
ATOM   1578 C  CB  . PRO   A 1 200 ? 25.347  4.302   15.010  1.00 15.61 ? 201 PRO   A CB  1 
ATOM   1579 C  CG  . PRO   A 1 200 ? 25.619  2.832   15.256  1.00 15.28 ? 201 PRO   A CG  1 
ATOM   1580 C  CD  . PRO   A 1 200 ? 24.214  2.243   15.231  1.00 15.07 ? 201 PRO   A CD  1 
ATOM   1581 N  N   . PRO   A 1 201 ? 23.195  6.885   16.033  1.00 13.46 ? 202 PRO   A N   1 
ATOM   1582 C  CA  . PRO   A 1 201 ? 24.089  7.260   17.141  1.00 14.04 ? 202 PRO   A CA  1 
ATOM   1583 C  C   . PRO   A 1 201 ? 23.778  6.822   18.567  1.00 12.21 ? 202 PRO   A C   1 
ATOM   1584 O  O   . PRO   A 1 201 ? 24.431  7.257   19.527  1.00 15.11 ? 202 PRO   A O   1 
ATOM   1585 C  CB  . PRO   A 1 201 ? 24.035  8.818   17.046  1.00 14.15 ? 202 PRO   A CB  1 
ATOM   1586 C  CG  . PRO   A 1 201 ? 22.580  9.102   16.579  1.00 16.10 ? 202 PRO   A CG  1 
ATOM   1587 C  CD  . PRO   A 1 201 ? 22.301  7.993   15.581  1.00 15.82 ? 202 PRO   A CD  1 
ATOM   1588 N  N   . LEU   A 1 202 ? 22.786  5.903   18.730  1.00 11.96 ? 203 LEU   A N   1 
ATOM   1589 C  CA  . LEU   A 1 202 ? 22.547  5.300   20.036  1.00 11.39 ? 203 LEU   A CA  1 
ATOM   1590 C  C   . LEU   A 1 202 ? 22.203  6.277   21.158  1.00 11.90 ? 203 LEU   A C   1 
ATOM   1591 O  O   . LEU   A 1 202 ? 22.352  5.949   22.361  1.00 12.35 ? 203 LEU   A O   1 
ATOM   1592 C  CB  . LEU   A 1 202 ? 23.740  4.429   20.457  1.00 12.42 ? 203 LEU   A CB  1 
ATOM   1593 C  CG  . LEU   A 1 202 ? 24.046  3.250   19.495  1.00 11.89 ? 203 LEU   A CG  1 
ATOM   1594 C  CD1 . LEU   A 1 202 ? 25.409  2.619   19.803  1.00 14.90 ? 203 LEU   A CD1 1 
ATOM   1595 C  CD2 . LEU   A 1 202 ? 23.003  2.143   19.467  1.00 12.68 ? 203 LEU   A CD2 1 
ATOM   1596 N  N   . LEU   A 1 203 ? 21.607  7.415   20.732  1.00 14.05 ? 204 LEU   A N   1 
ATOM   1597 C  CA  . LEU   A 1 203 ? 21.276  8.465   21.691  1.00 12.81 ? 204 LEU   A CA  1 
ATOM   1598 C  C   . LEU   A 1 203 ? 20.226  8.060   22.731  1.00 11.40 ? 204 LEU   A C   1 
ATOM   1599 O  O   . LEU   A 1 203 ? 19.256  7.332   22.423  1.00 13.09 ? 204 LEU   A O   1 
ATOM   1600 C  CB  . LEU   A 1 203 ? 20.829  9.742   20.960  1.00 14.49 ? 204 LEU   A CB  1 
ATOM   1601 C  CG  . LEU   A 1 203 ? 21.890  10.304  20.001  1.00 15.33 ? 204 LEU   A CG  1 
ATOM   1602 C  CD1 . LEU   A 1 203 ? 21.324  11.462  19.154  1.00 18.26 ? 204 LEU   A CD1 1 
ATOM   1603 C  CD2 . LEU   A 1 203 ? 23.082  10.852  20.801  1.00 19.20 ? 204 LEU   A CD2 1 
ATOM   1604 N  N   . GLU   A 1 204 ? 20.437  8.510   23.953  1.00 13.54 ? 205 GLU   A N   1 
ATOM   1605 C  CA  . GLU   A 1 204 ? 19.642  8.138   25.087  1.00 13.11 ? 205 GLU   A CA  1 
ATOM   1606 C  C   . GLU   A 1 204 ? 18.449  9.066   25.214  1.00 12.58 ? 205 GLU   A C   1 
ATOM   1607 O  O   . GLU   A 1 204 ? 18.342  9.834   26.183  1.00 16.26 ? 205 GLU   A O   1 
ATOM   1608 C  CB  . GLU   A 1 204 ? 20.468  7.962   26.345  1.00 13.30 ? 205 GLU   A CB  1 
ATOM   1609 C  CG  . GLU   A 1 204 ? 21.326  6.724   26.182  1.00 13.36 ? 205 GLU   A CG  1 
ATOM   1610 C  CD  . GLU   A 1 204 ? 22.292  6.462   27.331  1.00 14.32 ? 205 GLU   A CD  1 
ATOM   1611 O  OE1 . GLU   A 1 204 ? 22.610  7.374   28.130  1.00 17.96 ? 205 GLU   A OE1 1 
ATOM   1612 O  OE2 . GLU   A 1 204 ? 22.729  5.305   27.441  1.00 13.11 ? 205 GLU   A OE2 1 
ATOM   1613 N  N   . CYS   A 1 205 ? 17.570  9.008   24.214  1.00 13.61 ? 206 CYS   A N   1 
ATOM   1614 C  CA  . CYS   A 1 205 ? 16.532  10.028  24.077  1.00 13.94 ? 206 CYS   A CA  1 
ATOM   1615 C  C   . CYS   A 1 205 ? 15.166  9.371   23.909  1.00 12.25 ? 206 CYS   A C   1 
ATOM   1616 O  O   . CYS   A 1 205 ? 14.245  10.055  23.511  1.00 13.74 ? 206 CYS   A O   1 
ATOM   1617 C  CB  . CYS   A 1 205 ? 16.798  10.860  22.821  1.00 15.42 ? 206 CYS   A CB  1 
ATOM   1618 S  SG  . CYS   A 1 205 ? 16.858  9.898   21.285  1.00 13.85 ? 206 CYS   A SG  1 
ATOM   1619 N  N   . VAL   A 1 206 ? 15.007  8.072   24.214  1.00 12.39 ? 207 VAL   A N   1 
ATOM   1620 C  CA  . VAL   A 1 206 ? 13.757  7.353   23.872  1.00 11.67 ? 207 VAL   A CA  1 
ATOM   1621 C  C   . VAL   A 1 206 ? 12.999  6.909   25.124  1.00 12.51 ? 207 VAL   A C   1 
ATOM   1622 O  O   . VAL   A 1 206 ? 13.545  6.251   26.012  1.00 14.24 ? 207 VAL   A O   1 
ATOM   1623 C  CB  . VAL   A 1 206 ? 14.049  6.113   23.013  1.00 11.18 ? 207 VAL   A CB  1 
ATOM   1624 C  CG1 . VAL   A 1 206 ? 12.735  5.440   22.669  1.00 12.02 ? 207 VAL   A CG1 1 
ATOM   1625 C  CG2 . VAL   A 1 206 ? 14.828  6.454   21.752  1.00 11.90 ? 207 VAL   A CG2 1 
ATOM   1626 N  N   . THR   A 1 207 ? 11.664  7.202   25.142  1.00 10.84 ? 208 THR   A N   1 
ATOM   1627 C  CA  . THR   A 1 207 ? 10.735  6.500   25.986  1.00 11.56 ? 208 THR   A CA  1 
ATOM   1628 C  C   . THR   A 1 207 ? 10.198  5.346   25.163  1.00 12.07 ? 208 THR   A C   1 
ATOM   1629 O  O   . THR   A 1 207 ? 9.575   5.567   24.122  1.00 12.43 ? 208 THR   A O   1 
ATOM   1630 C  CB  . THR   A 1 207 ? 9.567   7.383   26.433  1.00 12.98 ? 208 THR   A CB  1 
ATOM   1631 O  OG1 . THR   A 1 207 ? 10.078  8.513   27.153  1.00 13.45 ? 208 THR   A OG1 1 
ATOM   1632 C  CG2 . THR   A 1 207 ? 8.627   6.582   27.321  1.00 13.60 ? 208 THR   A CG2 1 
ATOM   1633 N  N   . TRP   A 1 208 ? 10.601  4.127   25.567  1.00 10.75 ? 209 TRP   A N   1 
ATOM   1634 C  CA  . TRP   A 1 208 ? 10.141  2.917   24.872  1.00 11.39 ? 209 TRP   A CA  1 
ATOM   1635 C  C   . TRP   A 1 208 ? 8.757   2.525   25.389  1.00 10.60 ? 209 TRP   A C   1 
ATOM   1636 O  O   . TRP   A 1 208 ? 8.543   2.456   26.602  1.00 10.83 ? 209 TRP   A O   1 
ATOM   1637 C  CB  . TRP   A 1 208 ? 11.151  1.750   25.131  1.00 12.96 ? 209 TRP   A CB  1 
ATOM   1638 C  CG  . TRP   A 1 208 ? 12.274  1.850   24.149  1.00 10.45 ? 209 TRP   A CG  1 
ATOM   1639 C  CD1 . TRP   A 1 208 ? 13.498  2.482   24.332  1.00 11.84 ? 209 TRP   A CD1 1 
ATOM   1640 C  CD2 . TRP   A 1 208 ? 12.208  1.496   22.750  1.00 10.87 ? 209 TRP   A CD2 1 
ATOM   1641 N  NE1 . TRP   A 1 208 ? 14.211  2.455   23.165  1.00 13.23 ? 209 TRP   A NE1 1 
ATOM   1642 C  CE2 . TRP   A 1 208 ? 13.468  1.811   22.188  1.00 12.63 ? 209 TRP   A CE2 1 
ATOM   1643 C  CE3 . TRP   A 1 208 ? 11.261  0.799   21.952  1.00 11.30 ? 209 TRP   A CE3 1 
ATOM   1644 C  CZ2 . TRP   A 1 208 ? 13.748  1.560   20.850  1.00 12.79 ? 209 TRP   A CZ2 1 
ATOM   1645 C  CZ3 . TRP   A 1 208 ? 11.546  0.561   20.634  1.00 12.08 ? 209 TRP   A CZ3 1 
ATOM   1646 C  CH2 . TRP   A 1 208 ? 12.780  0.913   20.084  1.00 11.41 ? 209 TRP   A CH2 1 
ATOM   1647 N  N   . ILE   A 1 209 ? 7.872   2.168   24.437  1.00 11.77 ? 210 ILE   A N   1 
ATOM   1648 C  CA  . ILE   A 1 209 ? 6.573   1.616   24.791  1.00 11.38 ? 210 ILE   A CA  1 
ATOM   1649 C  C   . ILE   A 1 209 ? 6.451   0.351   23.945  1.00 10.31 ? 210 ILE   A C   1 
ATOM   1650 O  O   . ILE   A 1 209 ? 6.400   0.455   22.706  1.00 11.53 ? 210 ILE   A O   1 
ATOM   1651 C  CB  . ILE   A 1 209 ? 5.493   2.661   24.397  1.00 12.74 ? 210 ILE   A CB  1 
ATOM   1652 C  CG1 . ILE   A 1 209 ? 5.700   3.951   25.215  1.00 13.44 ? 210 ILE   A CG1 1 
ATOM   1653 C  CG2 . ILE   A 1 209 ? 4.100   2.093   24.634  1.00 12.82 ? 210 ILE   A CG2 1 
ATOM   1654 C  CD1 . ILE   A 1 209 ? 4.795   5.110   24.767  1.00 14.15 ? 210 ILE   A CD1 1 
ATOM   1655 N  N   . VAL   A 1 210 ? 6.502   -0.818  24.612  1.00 13.83 ? 211 VAL   A N   1 
ATOM   1656 C  CA  . VAL   A 1 210 ? 6.518   -2.080  23.863  1.00 13.40 ? 211 VAL   A CA  1 
ATOM   1657 C  C   . VAL   A 1 210 ? 5.217   -2.824  24.125  1.00 11.19 ? 211 VAL   A C   1 
ATOM   1658 O  O   . VAL   A 1 210 ? 4.886   -3.045  25.284  1.00 11.92 ? 211 VAL   A O   1 
ATOM   1659 C  CB  . VAL   A 1 210 ? 7.736   -2.918  24.281  1.00 10.94 ? 211 VAL   A CB  1 
ATOM   1660 C  CG1 . VAL   A 1 210 ? 7.679   -4.291  23.576  1.00 10.73 ? 211 VAL   A CG1 1 
ATOM   1661 C  CG2 . VAL   A 1 210 ? 9.087   -2.185  24.033  1.00 11.91 ? 211 VAL   A CG2 1 
ATOM   1662 N  N   . LEU   A 1 211 ? 4.465   -3.087  23.053  1.00 13.13 ? 212 LEU   A N   1 
ATOM   1663 C  CA  . LEU   A 1 211 ? 3.154   -3.715  23.243  1.00 12.69 ? 212 LEU   A CA  1 
ATOM   1664 C  C   . LEU   A 1 211 ? 3.346   -5.183  23.578  1.00 13.08 ? 212 LEU   A C   1 
ATOM   1665 O  O   . LEU   A 1 211 ? 4.261   -5.864  23.051  1.00 13.60 ? 212 LEU   A O   1 
ATOM   1666 C  CB  . LEU   A 1 211 ? 2.320   -3.604  21.959  1.00 12.36 ? 212 LEU   A CB  1 
ATOM   1667 C  CG  . LEU   A 1 211 ? 1.950   -2.187  21.503  1.00 14.13 ? 212 LEU   A CG  1 
ATOM   1668 C  CD1 . LEU   A 1 211 ? 0.911   -2.224  20.347  1.00 16.07 ? 212 LEU   A CD1 1 
ATOM   1669 C  CD2 . LEU   A 1 211 ? 1.495   -1.317  22.678  1.00 16.78 ? 212 LEU   A CD2 1 
ATOM   1670 N  N   . LYS   A 1 212 ? 2.510   -5.645  24.507  1.00 11.89 ? 213 LYS   A N   1 
ATOM   1671 C  CA  . LYS   A 1 212 ? 2.578   -7.047  24.937  1.00 13.27 ? 213 LYS   A CA  1 
ATOM   1672 C  C   . LYS   A 1 212 ? 2.110   -7.983  23.829  1.00 14.18 ? 213 LYS   A C   1 
ATOM   1673 O  O   . LYS   A 1 212 ? 2.628   -9.085  23.694  1.00 15.13 ? 213 LYS   A O   1 
ATOM   1674 C  CB  . LYS   A 1 212 ? 1.785   -7.303  26.232  1.00 15.94 ? 213 LYS   A CB  1 
ATOM   1675 C  CG  . LYS   A 1 212 ? 1.603   -8.773  26.624  1.00 17.10 ? 213 LYS   A CG  1 
ATOM   1676 C  CD  . LYS   A 1 212 ? 0.934   -8.951  27.970  1.00 26.91 ? 213 LYS   A CD  1 
ATOM   1677 C  CE  . LYS   A 1 212 ? 0.755   -10.413 28.293  1.00 30.78 ? 213 LYS   A CE  1 
ATOM   1678 N  NZ  . LYS   A 1 212 ? -0.031  -10.566 29.541  1.00 49.55 ? 213 LYS   A NZ  1 
ATOM   1679 N  N   . GLU   A 1 213 ? 1.068   -7.609  23.102  1.00 12.83 ? 214 GLU   A N   1 
ATOM   1680 C  CA  . GLU   A 1 213 ? 0.466   -8.549  22.137  1.00 13.30 ? 214 GLU   A CA  1 
ATOM   1681 C  C   . GLU   A 1 213 ? 1.227   -8.418  20.807  1.00 13.61 ? 214 GLU   A C   1 
ATOM   1682 O  O   . GLU   A 1 213 ? 1.286   -7.346  20.182  1.00 13.51 ? 214 GLU   A O   1 
ATOM   1683 C  CB  . GLU   A 1 213 ? -0.999  -8.165  21.853  1.00 14.94 ? 214 GLU   A CB  1 
ATOM   1684 C  CG  . GLU   A 1 213 ? -1.659  -9.129  20.874  1.00 16.48 ? 214 GLU   A CG  1 
ATOM   1685 C  CD  . GLU   A 1 213 ? -3.147  -8.999  20.702  1.00 23.79 ? 214 GLU   A CD  1 
ATOM   1686 O  OE1 . GLU   A 1 213 ? -3.731  -8.079  21.260  1.00 17.89 ? 214 GLU   A OE1 1 
ATOM   1687 O  OE2 . GLU   A 1 213 ? -3.716  -9.912  20.065  1.00 33.68 ? 214 GLU   A OE2 1 
ATOM   1688 N  N   . PRO   A 1 214 ? 1.830   -9.494  20.291  1.00 12.64 ? 215 PRO   A N   1 
ATOM   1689 C  CA  . PRO   A 1 214 ? 2.471   -9.463  18.985  1.00 13.29 ? 215 PRO   A CA  1 
ATOM   1690 C  C   . PRO   A 1 214 ? 1.441   -9.491  17.878  1.00 14.80 ? 215 PRO   A C   1 
ATOM   1691 O  O   . PRO   A 1 214 ? 0.315   -9.939  18.113  1.00 17.55 ? 215 PRO   A O   1 
ATOM   1692 C  CB  . PRO   A 1 214 ? 3.238   -10.803 18.877  1.00 13.11 ? 215 PRO   A CB  1 
ATOM   1693 C  CG  . PRO   A 1 214 ? 2.571   -11.695 19.863  1.00 22.00 ? 215 PRO   A CG  1 
ATOM   1694 C  CD  . PRO   A 1 214 ? 1.822   -10.857 20.881  1.00 14.71 ? 215 PRO   A CD  1 
ATOM   1695 N  N   . ILE   A 1 215 ? 1.854   -9.050  16.687  1.00 14.49 ? 216 ILE   A N   1 
ATOM   1696 C  CA  . ILE   A 1 215 ? 1.036   -9.242  15.509  1.00 15.44 ? 216 ILE   A CA  1 
ATOM   1697 C  C   . ILE   A 1 215 ? 1.529   -10.513 14.821  1.00 13.23 ? 216 ILE   A C   1 
ATOM   1698 O  O   . ILE   A 1 215 ? 2.703   -10.866 14.926  1.00 14.25 ? 216 ILE   A O   1 
ATOM   1699 C  CB  . ILE   A 1 215 ? 1.011   -8.023  14.544  1.00 13.75 ? 216 ILE   A CB  1 
ATOM   1700 C  CG1 . ILE   A 1 215 ? 2.409   -7.643  14.084  1.00 13.01 ? 216 ILE   A CG1 1 
ATOM   1701 C  CG2 . ILE   A 1 215 ? 0.359   -6.788  15.186  1.00 15.69 ? 216 ILE   A CG2 1 
ATOM   1702 C  CD1 . ILE   A 1 215 ? 2.421   -6.672  12.846  1.00 15.82 ? 216 ILE   A CD1 1 
ATOM   1703 N  N   . SER   A 1 216 ? 0.633   -11.179 14.090  1.00 15.22 ? 217 SER   A N   1 
ATOM   1704 C  CA  . SER   A 1 216 ? 1.026   -12.317 13.278  1.00 16.55 ? 217 SER   A CA  1 
ATOM   1705 C  C   . SER   A 1 216 ? 1.244   -11.870 11.842  1.00 14.97 ? 217 SER   A C   1 
ATOM   1706 O  O   . SER   A 1 216 ? 0.407   -11.163 11.277  1.00 16.06 ? 217 SER   A O   1 
ATOM   1707 C  CB  . SER   A 1 216 ? -0.007  -13.438 13.262  1.00 16.56 ? 217 SER   A CB  1 
ATOM   1708 O  OG  . SER   A 1 216 ? -0.044  -14.057 14.509  1.00 19.36 ? 217 SER   A OG  1 
ATOM   1709 N  N   . VAL   A 1 217 ? 2.347   -12.322 11.252  1.00 14.31 ? 218 VAL   A N   1 
ATOM   1710 C  CA  . VAL   A 1 217 ? 2.622   -12.159 9.835   1.00 14.31 ? 218 VAL   A CA  1 
ATOM   1711 C  C   . VAL   A 1 217 ? 2.881   -13.533 9.238   1.00 16.19 ? 218 VAL   A C   1 
ATOM   1712 O  O   . VAL   A 1 217 ? 3.233   -14.471 9.989   1.00 15.46 ? 218 VAL   A O   1 
ATOM   1713 C  CB  . VAL   A 1 217 ? 3.777   -11.179 9.595   1.00 12.99 ? 218 VAL   A CB  1 
ATOM   1714 C  CG1 . VAL   A 1 217 ? 3.523   -9.830  10.290  1.00 15.40 ? 218 VAL   A CG1 1 
ATOM   1715 C  CG2 . VAL   A 1 217 ? 5.103   -11.769 10.070  1.00 16.34 ? 218 VAL   A CG2 1 
ATOM   1716 N  N   . SER   A 1 218 ? 2.739   -13.654 7.915   1.00 14.67 ? 219 SER   A N   1 
ATOM   1717 C  CA  . SER   A 1 218 ? 2.935   -15.000 7.365   1.00 14.37 ? 219 SER   A CA  1 
ATOM   1718 C  C   . SER   A 1 218 ? 4.415   -15.259 7.089   1.00 14.32 ? 219 SER   A C   1 
ATOM   1719 O  O   . SER   A 1 218 ? 5.255   -14.347 6.971   1.00 15.45 ? 219 SER   A O   1 
ATOM   1720 C  CB  . SER   A 1 218 ? 2.183   -15.223 6.086   1.00 17.10 ? 219 SER   A CB  1 
ATOM   1721 O  OG  . SER   A 1 218 ? 2.668   -14.380 5.062   1.00 16.54 ? 219 SER   A OG  1 
ATOM   1722 N  N   A SER   A 1 219 ? 4.742   -16.537 6.964   0.50 16.48 ? 220 SER   A N   1 
ATOM   1723 N  N   B SER   A 1 219 ? 4.741   -16.536 6.961   0.50 15.96 ? 220 SER   A N   1 
ATOM   1724 C  CA  A SER   A 1 219 ? 6.095   -16.906 6.597   0.50 17.30 ? 220 SER   A CA  1 
ATOM   1725 C  CA  B SER   A 1 219 ? 6.099   -16.901 6.610   0.50 16.38 ? 220 SER   A CA  1 
ATOM   1726 C  C   A SER   A 1 219 ? 6.497   -16.231 5.286   0.50 18.40 ? 220 SER   A C   1 
ATOM   1727 C  C   B SER   A 1 219 ? 6.503   -16.260 5.280   0.50 17.89 ? 220 SER   A C   1 
ATOM   1728 O  O   A SER   A 1 219 ? 7.622   -15.751 5.159   0.50 17.88 ? 220 SER   A O   1 
ATOM   1729 O  O   B SER   A 1 219 ? 7.635   -15.799 5.144   0.50 17.50 ? 220 SER   A O   1 
ATOM   1730 C  CB  A SER   A 1 219 ? 6.211   -18.408 6.552   0.50 19.01 ? 220 SER   A CB  1 
ATOM   1731 C  CB  B SER   A 1 219 ? 6.233   -18.408 6.654   0.50 15.92 ? 220 SER   A CB  1 
ATOM   1732 O  OG  A SER   A 1 219 ? 5.420   -18.948 5.500   0.50 19.60 ? 220 SER   A OG  1 
ATOM   1733 O  OG  B SER   A 1 219 ? 7.518   -18.846 6.226   0.50 16.38 ? 220 SER   A OG  1 
ATOM   1734 N  N   . GLU   A 1 220 ? 5.563   -16.159 4.325   1.00 16.98 ? 221 GLU   A N   1 
ATOM   1735 C  CA  . GLU   A 1 220 ? 5.829   -15.542 3.026   1.00 17.72 ? 221 GLU   A CA  1 
ATOM   1736 C  C   . GLU   A 1 220 ? 6.151   -14.056 3.178   1.00 18.25 ? 221 GLU   A C   1 
ATOM   1737 O  O   . GLU   A 1 220 ? 7.055   -13.574 2.480   1.00 17.68 ? 221 GLU   A O   1 
ATOM   1738 C  CB  . GLU   A 1 220 ? 4.707   -15.738 2.001   1.00 21.02 ? 221 GLU   A CB  1 
ATOM   1739 C  CG  . GLU   A 1 220 ? 4.499   -17.209 1.613   1.00 24.50 ? 221 GLU   A CG  1 
ATOM   1740 C  CD  . GLU   A 1 220 ? 3.659   -18.025 2.589   1.00 26.93 ? 221 GLU   A CD  1 
ATOM   1741 O  OE1 . GLU   A 1 220 ? 3.277   -17.527 3.657   1.00 27.49 ? 221 GLU   A OE1 1 
ATOM   1742 O  OE2 . GLU   A 1 220 ? 3.436   -19.210 2.317   1.00 34.11 ? 221 GLU   A OE2 1 
ATOM   1743 N  N   . GLN   A 1 221 ? 5.420   -13.379 4.080   1.00 14.70 ? 222 GLN   A N   1 
ATOM   1744 C  CA  . GLN   A 1 221 ? 5.670   -11.959 4.256   1.00 14.88 ? 222 GLN   A CA  1 
ATOM   1745 C  C   . GLN   A 1 221 ? 7.089   -11.737 4.797   1.00 14.62 ? 222 GLN   A C   1 
ATOM   1746 O  O   . GLN   A 1 221 ? 7.841   -10.906 4.243   1.00 16.85 ? 222 GLN   A O   1 
ATOM   1747 C  CB  . GLN   A 1 221 ? 4.611   -11.430 5.226   1.00 15.98 ? 222 GLN   A CB  1 
ATOM   1748 C  CG  . GLN   A 1 221 ? 3.290   -11.217 4.487   1.00 17.61 ? 222 GLN   A CG  1 
ATOM   1749 C  CD  . GLN   A 1 221 ? 2.150   -10.699 5.346   1.00 14.52 ? 222 GLN   A CD  1 
ATOM   1750 O  OE1 . GLN   A 1 221 ? 2.036   -11.032 6.496   1.00 15.05 ? 222 GLN   A OE1 1 
ATOM   1751 N  NE2 . GLN   A 1 221 ? 1.310   -9.810  4.796   1.00 15.80 ? 222 GLN   A NE2 1 
ATOM   1752 N  N   . VAL   A 1 222 ? 7.477   -12.487 5.845   1.00 14.47 ? 223 VAL   A N   1 
ATOM   1753 C  CA  . VAL   A 1 222 ? 8.801   -12.231 6.427   1.00 15.89 ? 223 VAL   A CA  1 
ATOM   1754 C  C   . VAL   A 1 222 ? 9.884   -12.754 5.458   1.00 18.15 ? 223 VAL   A C   1 
ATOM   1755 O  O   . VAL   A 1 222 ? 10.978  -12.168 5.368   1.00 16.38 ? 223 VAL   A O   1 
ATOM   1756 C  CB  . VAL   A 1 222 ? 8.954   -12.725 7.888   1.00 18.11 ? 223 VAL   A CB  1 
ATOM   1757 C  CG1 . VAL   A 1 222 ? 8.957   -14.252 7.960   1.00 18.13 ? 223 VAL   A CG1 1 
ATOM   1758 C  CG2 . VAL   A 1 222 ? 10.228  -12.210 8.540   1.00 19.66 ? 223 VAL   A CG2 1 
ATOM   1759 N  N   . LEU   A 1 223 ? 9.604   -13.808 4.665   1.00 19.07 ? 224 LEU   A N   1 
ATOM   1760 C  CA  . LEU   A 1 223 ? 10.556  -14.221 3.643   1.00 16.49 ? 224 LEU   A CA  1 
ATOM   1761 C  C   . LEU   A 1 223 ? 10.914  -13.101 2.667   1.00 16.55 ? 224 LEU   A C   1 
ATOM   1762 O  O   . LEU   A 1 223 ? 12.065  -12.983 2.266   1.00 16.94 ? 224 LEU   A O   1 
ATOM   1763 C  CB  . LEU   A 1 223 ? 10.073  -15.490 2.946   1.00 21.63 ? 224 LEU   A CB  1 
ATOM   1764 C  CG  . LEU   A 1 223 ? 10.308  -16.722 3.814   1.00 22.92 ? 224 LEU   A CG  1 
ATOM   1765 C  CD1 . LEU   A 1 223 ? 9.393   -17.887 3.378   1.00 30.06 ? 224 LEU   A CD1 1 
ATOM   1766 C  CD2 . LEU   A 1 223 ? 11.775  -17.082 3.824   1.00 25.95 ? 224 LEU   A CD2 1 
ATOM   1767 N  N   . LYS   A 1 224 ? 9.938   -12.243 2.348   1.00 16.71 ? 225 LYS   A N   1 
ATOM   1768 C  CA  . LYS   A 1 224 ? 10.158  -11.112 1.454   1.00 17.90 ? 225 LYS   A CA  1 
ATOM   1769 C  C   . LYS   A 1 224 ? 11.035  -10.047 2.126   1.00 15.59 ? 225 LYS   A C   1 
ATOM   1770 O  O   . LYS   A 1 224 ? 11.849  -9.426  1.419   1.00 17.04 ? 225 LYS   A O   1 
ATOM   1771 C  CB  . LYS   A 1 224 ? 8.843   -10.675 0.750   1.00 16.87 ? 225 LYS   A CB  1 
ATOM   1772 C  CG  . LYS   A 1 224 ? 8.345   -11.711 -0.287  1.00 19.37 ? 225 LYS   A CG  1 
ATOM   1773 C  CD  . LYS   A 1 224 ? 7.013   -11.412 -0.935  1.00 23.08 ? 225 LYS   A CD  1 
ATOM   1774 C  CE  . LYS   A 1 224 ? 6.497   -12.521 -1.843  1.00 30.49 ? 225 LYS   A CE  1 
ATOM   1775 N  NZ  . LYS   A 1 224 ? 5.174   -12.186 -2.465  1.00 27.47 ? 225 LYS   A NZ  1 
ATOM   1776 N  N   . PHE   A 1 225 ? 10.894  -9.830  3.445   1.00 14.22 ? 226 PHE   A N   1 
ATOM   1777 C  CA  . PHE   A 1 225 ? 11.858  -8.951  4.141   1.00 13.86 ? 226 PHE   A CA  1 
ATOM   1778 C  C   . PHE   A 1 225 ? 13.288  -9.409  3.918   1.00 14.54 ? 226 PHE   A C   1 
ATOM   1779 O  O   . PHE   A 1 225 ? 14.193  -8.629  3.672   1.00 14.72 ? 226 PHE   A O   1 
ATOM   1780 C  CB  . PHE   A 1 225 ? 11.645  -8.887  5.647   1.00 14.02 ? 226 PHE   A CB  1 
ATOM   1781 C  CG  . PHE   A 1 225 ? 10.458  -8.100  6.164   1.00 15.17 ? 226 PHE   A CG  1 
ATOM   1782 C  CD1 . PHE   A 1 225 ? 9.400   -7.688  5.362   1.00 18.54 ? 226 PHE   A CD1 1 
ATOM   1783 C  CD2 . PHE   A 1 225 ? 10.338  -7.869  7.528   1.00 18.25 ? 226 PHE   A CD2 1 
ATOM   1784 C  CE1 . PHE   A 1 225 ? 8.352   -6.939  5.893   1.00 20.22 ? 226 PHE   A CE1 1 
ATOM   1785 C  CE2 . PHE   A 1 225 ? 9.278   -7.155  8.072   1.00 20.73 ? 226 PHE   A CE2 1 
ATOM   1786 C  CZ  . PHE   A 1 225 ? 8.292   -6.673  7.238   1.00 16.89 ? 226 PHE   A CZ  1 
ATOM   1787 N  N   . ARG   A 1 226 ? 13.471  -10.741 3.967   1.00 12.95 ? 227 ARG   A N   1 
ATOM   1788 C  CA  . ARG   A 1 226 ? 14.797  -11.352 3.942   1.00 13.51 ? 227 ARG   A CA  1 
ATOM   1789 C  C   . ARG   A 1 226 ? 15.382  -11.360 2.531   1.00 14.86 ? 227 ARG   A C   1 
ATOM   1790 O  O   . ARG   A 1 226 ? 16.543  -11.765 2.381   1.00 15.98 ? 227 ARG   A O   1 
ATOM   1791 C  CB  . ARG   A 1 226 ? 14.650  -12.790 4.458   1.00 14.17 ? 227 ARG   A CB  1 
ATOM   1792 C  CG  . ARG   A 1 226 ? 14.336  -12.880 5.932   1.00 13.17 ? 227 ARG   A CG  1 
ATOM   1793 C  CD  . ARG   A 1 226 ? 14.324  -14.332 6.398   1.00 15.55 ? 227 ARG   A CD  1 
ATOM   1794 N  NE  . ARG   A 1 226 ? 13.764  -14.435 7.730   1.00 15.45 ? 227 ARG   A NE  1 
ATOM   1795 C  CZ  . ARG   A 1 226 ? 12.786  -15.294 8.083   1.00 16.09 ? 227 ARG   A CZ  1 
ATOM   1796 N  NH1 . ARG   A 1 226 ? 12.352  -16.215 7.220   1.00 20.00 ? 227 ARG   A NH1 1 
ATOM   1797 N  NH2 . ARG   A 1 226 ? 12.328  -15.259 9.310   1.00 17.90 ? 227 ARG   A NH2 1 
ATOM   1798 N  N   . LYS   A 1 227 ? 14.666  -10.872 1.495   1.00 13.76 ? 228 LYS   A N   1 
ATOM   1799 C  CA  . LYS   A 1 227 ? 15.203  -10.777 0.142   1.00 15.78 ? 228 LYS   A CA  1 
ATOM   1800 C  C   . LYS   A 1 227 ? 15.814  -9.400  -0.086  1.00 15.70 ? 228 LYS   A C   1 
ATOM   1801 O  O   . LYS   A 1 227 ? 16.438  -9.183  -1.139  1.00 16.88 ? 228 LYS   A O   1 
ATOM   1802 C  CB  . LYS   A 1 227 ? 14.098  -11.026 -0.892  1.00 16.83 ? 228 LYS   A CB  1 
ATOM   1803 C  CG  . LYS   A 1 227 ? 13.557  -12.448 -0.908  1.00 21.06 ? 228 LYS   A CG  1 
ATOM   1804 C  CD  . LYS   A 1 227 ? 12.584  -12.543 -2.059  1.00 24.70 ? 228 LYS   A CD  1 
ATOM   1805 C  CE  . LYS   A 1 227 ? 13.172  -13.103 -3.333  1.00 35.63 ? 228 LYS   A CE  1 
ATOM   1806 N  NZ  . LYS   A 1 227 ? 12.136  -13.132 -4.388  1.00 50.40 ? 228 LYS   A NZ  1 
ATOM   1807 N  N   . LEU   A 1 228 ? 15.614  -8.471  0.860   1.00 14.55 ? 229 LEU   A N   1 
ATOM   1808 C  CA  . LEU   A 1 228 ? 16.254  -7.173  0.713   1.00 13.75 ? 229 LEU   A CA  1 
ATOM   1809 C  C   . LEU   A 1 228 ? 17.766  -7.332  0.841   1.00 15.14 ? 229 LEU   A C   1 
ATOM   1810 O  O   . LEU   A 1 228 ? 18.272  -8.375  1.218   1.00 15.94 ? 229 LEU   A O   1 
ATOM   1811 C  CB  . LEU   A 1 228 ? 15.740  -6.244  1.831   1.00 13.89 ? 229 LEU   A CB  1 
ATOM   1812 C  CG  . LEU   A 1 228 ? 14.291  -5.732  1.636   1.00 15.71 ? 229 LEU   A CG  1 
ATOM   1813 C  CD1 . LEU   A 1 228 ? 13.715  -5.160  2.903   1.00 14.64 ? 229 LEU   A CD1 1 
ATOM   1814 C  CD2 . LEU   A 1 228 ? 14.161  -4.752  0.469   1.00 16.13 ? 229 LEU   A CD2 1 
ATOM   1815 N  N   . ASN   A 1 229 ? 18.479  -6.278  0.463   1.00 14.35 ? 230 ASN   A N   1 
ATOM   1816 C  CA  . ASN   A 1 229 ? 19.938  -6.297  0.459   1.00 13.94 ? 230 ASN   A CA  1 
ATOM   1817 C  C   . ASN   A 1 229 ? 20.487  -5.150  1.314   1.00 13.49 ? 230 ASN   A C   1 
ATOM   1818 O  O   . ASN   A 1 229 ? 20.029  -4.009  1.179   1.00 13.08 ? 230 ASN   A O   1 
ATOM   1819 C  CB  . ASN   A 1 229 ? 20.459  -6.062  -0.965  1.00 13.75 ? 230 ASN   A CB  1 
ATOM   1820 C  CG  . ASN   A 1 229 ? 20.421  -7.256  -1.893  1.00 15.00 ? 230 ASN   A CG  1 
ATOM   1821 O  OD1 . ASN   A 1 229 ? 20.933  -7.148  -3.012  1.00 18.45 ? 230 ASN   A OD1 1 
ATOM   1822 N  ND2 . ASN   A 1 229 ? 19.729  -8.338  -1.505  1.00 17.23 ? 230 ASN   A ND2 1 
ATOM   1823 N  N   . PHE   A 1 230 ? 21.534  -5.396  2.114   1.00 14.74 ? 231 PHE   A N   1 
ATOM   1824 C  CA  . PHE   A 1 230 ? 22.303  -4.303  2.715   1.00 12.33 ? 231 PHE   A CA  1 
ATOM   1825 C  C   . PHE   A 1 230 ? 23.183  -3.580  1.695   1.00 15.07 ? 231 PHE   A C   1 
ATOM   1826 O  O   . PHE   A 1 230 ? 23.511  -2.415  1.904   1.00 14.87 ? 231 PHE   A O   1 
ATOM   1827 C  CB  . PHE   A 1 230 ? 23.302  -4.894  3.711   1.00 14.50 ? 231 PHE   A CB  1 
ATOM   1828 C  CG  . PHE   A 1 230 ? 22.726  -5.496  4.977   1.00 12.18 ? 231 PHE   A CG  1 
ATOM   1829 C  CD1 . PHE   A 1 230 ? 21.891  -4.754  5.825   1.00 14.03 ? 231 PHE   A CD1 1 
ATOM   1830 C  CD2 . PHE   A 1 230 ? 23.000  -6.821  5.333   1.00 14.53 ? 231 PHE   A CD2 1 
ATOM   1831 C  CE1 . PHE   A 1 230 ? 21.448  -5.259  7.051   1.00 14.96 ? 231 PHE   A CE1 1 
ATOM   1832 C  CE2 . PHE   A 1 230 ? 22.589  -7.298  6.569   1.00 12.75 ? 231 PHE   A CE2 1 
ATOM   1833 C  CZ  . PHE   A 1 230 ? 21.752  -6.579  7.395   1.00 13.66 ? 231 PHE   A CZ  1 
ATOM   1834 N  N   . ASN   A 1 231 ? 23.637  -4.288  0.669   1.00 16.71 ? 232 ASN   A N   1 
ATOM   1835 C  CA  . ASN   A 1 231 ? 24.535  -3.715  -0.329  1.00 16.38 ? 232 ASN   A CA  1 
ATOM   1836 C  C   . ASN   A 1 231 ? 23.786  -2.775  -1.273  1.00 15.56 ? 232 ASN   A C   1 
ATOM   1837 O  O   . ASN   A 1 231 ? 22.556  -2.841  -1.426  1.00 15.26 ? 232 ASN   A O   1 
ATOM   1838 C  CB  . ASN   A 1 231 ? 25.132  -4.804  -1.213  1.00 16.64 ? 232 ASN   A CB  1 
ATOM   1839 C  CG  . ASN   A 1 231 ? 24.074  -5.725  -1.751  1.00 15.41 ? 232 ASN   A CG  1 
ATOM   1840 O  OD1 . ASN   A 1 231 ? 23.579  -6.542  -0.976  1.00 19.67 ? 232 ASN   A OD1 1 
ATOM   1841 N  ND2 . ASN   A 1 231 ? 23.710  -5.545  -3.027  1.00 16.23 ? 232 ASN   A ND2 1 
ATOM   1842 N  N   . GLY   A 1 232 ? 24.544  -1.907  -1.939  1.00 15.79 ? 233 GLY   A N   1 
ATOM   1843 C  CA  . GLY   A 1 232 ? 24.009  -1.121  -3.062  1.00 17.03 ? 233 GLY   A CA  1 
ATOM   1844 C  C   . GLY   A 1 232 ? 23.891  -1.922  -4.358  1.00 15.64 ? 233 GLY   A C   1 
ATOM   1845 O  O   . GLY   A 1 232 ? 24.417  -3.039  -4.503  1.00 17.34 ? 233 GLY   A O   1 
ATOM   1846 N  N   . GLU   A 1 233 ? 23.221  -1.335  -5.348  1.00 17.05 ? 234 GLU   A N   1 
ATOM   1847 C  CA  . GLU   A 1 233 ? 23.088  -1.894  -6.679  1.00 19.31 ? 234 GLU   A CA  1 
ATOM   1848 C  C   . GLU   A 1 233 ? 24.477  -2.147  -7.265  1.00 19.33 ? 234 GLU   A C   1 
ATOM   1849 O  O   . GLU   A 1 233 ? 25.378  -1.337  -7.137  1.00 21.92 ? 234 GLU   A O   1 
ATOM   1850 C  CB  . GLU   A 1 233 ? 22.278  -0.876  -7.499  1.00 18.18 ? 234 GLU   A CB  1 
ATOM   1851 C  CG  . GLU   A 1 233 ? 22.019  -1.376  -8.921  1.00 19.06 ? 234 GLU   A CG  1 
ATOM   1852 C  CD  . GLU   A 1 233 ? 21.238  -0.403  -9.774  1.00 22.90 ? 234 GLU   A CD  1 
ATOM   1853 O  OE1 . GLU   A 1 233 ? 21.014  0.775   -9.278  1.00 26.56 ? 234 GLU   A OE1 1 
ATOM   1854 O  OE2 . GLU   A 1 233 ? 20.985  -0.761  -10.964 1.00 25.40 ? 234 GLU   A OE2 1 
ATOM   1855 N  N   . GLY   A 1 234 ? 24.598  -3.269  -7.952  1.00 22.32 ? 235 GLY   A N   1 
ATOM   1856 C  CA  . GLY   A 1 234 ? 25.843  -3.646  -8.612  1.00 25.26 ? 235 GLY   A CA  1 
ATOM   1857 C  C   . GLY   A 1 234 ? 26.961  -4.102  -7.687  1.00 28.26 ? 235 GLY   A C   1 
ATOM   1858 O  O   . GLY   A 1 234 ? 28.086  -4.225  -8.164  1.00 30.26 ? 235 GLY   A O   1 
ATOM   1859 N  N   . GLU   A 1 235 ? 26.648  -4.282  -6.393  1.00 20.88 ? 236 GLU   A N   1 
ATOM   1860 C  CA  . GLU   A 1 235 ? 27.589  -4.839  -5.435  1.00 18.16 ? 236 GLU   A CA  1 
ATOM   1861 C  C   . GLU   A 1 235 ? 27.172  -6.260  -5.101  1.00 17.20 ? 236 GLU   A C   1 
ATOM   1862 O  O   . GLU   A 1 235 ? 26.013  -6.663  -5.260  1.00 21.44 ? 236 GLU   A O   1 
ATOM   1863 C  CB  . GLU   A 1 235 ? 27.606  -4.046  -4.140  1.00 17.64 ? 236 GLU   A CB  1 
ATOM   1864 C  CG  . GLU   A 1 235 ? 28.019  -2.611  -4.433  1.00 20.42 ? 236 GLU   A CG  1 
ATOM   1865 C  CD  . GLU   A 1 235 ? 27.968  -1.659  -3.244  1.00 30.09 ? 236 GLU   A CD  1 
ATOM   1866 O  OE1 . GLU   A 1 235 ? 27.423  -2.021  -2.167  1.00 22.15 ? 236 GLU   A OE1 1 
ATOM   1867 O  OE2 . GLU   A 1 235 ? 28.449  -0.520  -3.413  1.00 38.83 ? 236 GLU   A OE2 1 
ATOM   1868 N  N   . PRO   A 1 236 ? 28.125  -7.078  -4.627  1.00 18.21 ? 237 PRO   A N   1 
ATOM   1869 C  CA  . PRO   A 1 236 ? 27.798  -8.450  -4.241  1.00 16.85 ? 237 PRO   A CA  1 
ATOM   1870 C  C   . PRO   A 1 236 ? 26.720  -8.485  -3.168  1.00 17.28 ? 237 PRO   A C   1 
ATOM   1871 O  O   . PRO   A 1 236 ? 26.641  -7.657  -2.278  1.00 18.29 ? 237 PRO   A O   1 
ATOM   1872 C  CB  . PRO   A 1 236 ? 29.102  -9.003  -3.731  1.00 18.91 ? 237 PRO   A CB  1 
ATOM   1873 C  CG  . PRO   A 1 236 ? 30.167  -8.152  -4.446  1.00 20.95 ? 237 PRO   A CG  1 
ATOM   1874 C  CD  . PRO   A 1 236 ? 29.559  -6.767  -4.536  1.00 19.98 ? 237 PRO   A CD  1 
ATOM   1875 N  N   . GLU   A 1 237 ? 25.870  -9.508  -3.277  1.00 17.80 ? 238 GLU   A N   1 
ATOM   1876 C  CA  . GLU   A 1 237 ? 24.638  -9.536  -2.524  1.00 17.42 ? 238 GLU   A CA  1 
ATOM   1877 C  C   . GLU   A 1 237 ? 24.945  -9.855  -1.064  1.00 17.05 ? 238 GLU   A C   1 
ATOM   1878 O  O   . GLU   A 1 237 ? 25.602  -10.846 -0.759  1.00 17.43 ? 238 GLU   A O   1 
ATOM   1879 C  CB  . GLU   A 1 237 ? 23.679  -10.590 -3.070  1.00 20.48 ? 238 GLU   A CB  1 
ATOM   1880 C  CG  . GLU   A 1 237 ? 22.324  -10.508 -2.362  1.00 25.71 ? 238 GLU   A CG  1 
ATOM   1881 C  CD  . GLU   A 1 237 ? 21.172  -11.298 -2.974  1.00 26.71 ? 238 GLU   A CD  1 
ATOM   1882 O  OE1 . GLU   A 1 237 ? 21.331  -12.520 -3.166  1.00 30.63 ? 238 GLU   A OE1 1 
ATOM   1883 O  OE2 . GLU   A 1 237 ? 20.122  -10.687 -3.255  1.00 22.64 ? 238 GLU   A OE2 1 
ATOM   1884 N  N   . GLU   A 1 238 ? 24.456  -9.020  -0.158  1.00 15.39 ? 239 GLU   A N   1 
ATOM   1885 C  CA  . GLU   A 1 238 ? 24.455  -9.233  1.282   1.00 14.88 ? 239 GLU   A CA  1 
ATOM   1886 C  C   . GLU   A 1 238 ? 22.996  -9.211  1.693   1.00 13.95 ? 239 GLU   A C   1 
ATOM   1887 O  O   . GLU   A 1 238 ? 22.406  -8.136  1.801   1.00 14.48 ? 239 GLU   A O   1 
ATOM   1888 C  CB  . GLU   A 1 238 ? 25.219  -8.112  2.010   1.00 19.19 ? 239 GLU   A CB  1 
ATOM   1889 C  CG  . GLU   A 1 238 ? 26.668  -7.873  1.559   1.00 22.02 ? 239 GLU   A CG  1 
ATOM   1890 C  CD  . GLU   A 1 238 ? 27.246  -6.554  2.103   1.00 32.07 ? 239 GLU   A CD  1 
ATOM   1891 O  OE1 . GLU   A 1 238 ? 27.197  -6.354  3.320   1.00 30.81 ? 239 GLU   A OE1 1 
ATOM   1892 O  OE2 . GLU   A 1 238 ? 27.664  -5.671  1.302   1.00 29.91 ? 239 GLU   A OE2 1 
ATOM   1893 N  N   . LEU   A 1 239 ? 22.405  -10.381 1.943   1.00 14.57 ? 240 LEU   A N   1 
ATOM   1894 C  CA  . LEU   A 1 239 ? 20.997  -10.340 2.268   1.00 14.86 ? 240 LEU   A CA  1 
ATOM   1895 C  C   . LEU   A 1 239 ? 20.799  -9.533  3.545   1.00 13.69 ? 240 LEU   A C   1 
ATOM   1896 O  O   . LEU   A 1 239 ? 21.505  -9.664  4.523   1.00 15.19 ? 240 LEU   A O   1 
ATOM   1897 C  CB  . LEU   A 1 239 ? 20.463  -11.758 2.457   1.00 14.81 ? 240 LEU   A CB  1 
ATOM   1898 C  CG  . LEU   A 1 239 ? 20.413  -12.557 1.165   1.00 17.11 ? 240 LEU   A CG  1 
ATOM   1899 C  CD1 . LEU   A 1 239 ? 20.113  -14.001 1.474   1.00 20.36 ? 240 LEU   A CD1 1 
ATOM   1900 C  CD2 . LEU   A 1 239 ? 19.438  -11.976 0.130   1.00 17.75 ? 240 LEU   A CD2 1 
ATOM   1901 N  N   . MET   A 1 240 ? 19.749  -8.703  3.527   1.00 12.73 ? 241 MET   A N   1 
ATOM   1902 C  CA  . MET   A 1 240 ? 19.397  -7.907  4.684   1.00 14.84 ? 241 MET   A CA  1 
ATOM   1903 C  C   . MET   A 1 240 ? 18.626  -8.769  5.670   1.00 14.14 ? 241 MET   A C   1 
ATOM   1904 O  O   . MET   A 1 240 ? 17.404  -8.956  5.547   1.00 14.76 ? 241 MET   A O   1 
ATOM   1905 C  CB  . MET   A 1 240 ? 18.540  -6.717  4.254   1.00 15.16 ? 241 MET   A CB  1 
ATOM   1906 C  CG  . MET   A 1 240 ? 18.173  -5.779  5.424   1.00 14.75 ? 241 MET   A CG  1 
ATOM   1907 S  SD  . MET   A 1 240 ? 17.245  -4.324  4.847   1.00 15.08 ? 241 MET   A SD  1 
ATOM   1908 C  CE  . MET   A 1 240 ? 18.574  -3.290  4.201   1.00 16.13 ? 241 MET   A CE  1 
ATOM   1909 N  N   . VAL   A 1 241 ? 19.381  -9.330  6.627   1.00 13.80 ? 242 VAL   A N   1 
ATOM   1910 C  CA  . VAL   A 1 241 ? 18.839  -10.203 7.665   1.00 11.66 ? 242 VAL   A CA  1 
ATOM   1911 C  C   . VAL   A 1 241 ? 19.624  -9.964  8.963   1.00 11.89 ? 242 VAL   A C   1 
ATOM   1912 O  O   . VAL   A 1 241 ? 20.787  -9.506  8.909   1.00 14.05 ? 242 VAL   A O   1 
ATOM   1913 C  CB  . VAL   A 1 241 ? 18.930  -11.701 7.305   1.00 10.93 ? 242 VAL   A CB  1 
ATOM   1914 C  CG1 . VAL   A 1 241 ? 18.031  -12.051 6.113   1.00 14.37 ? 242 VAL   A CG1 1 
ATOM   1915 C  CG2 . VAL   A 1 241 ? 20.379  -12.136 7.110   1.00 14.94 ? 242 VAL   A CG2 1 
ATOM   1916 N  N   . ASP   A 1 242 ? 19.009  -10.269 10.110  1.00 12.89 ? 243 ASP   A N   1 
ATOM   1917 C  CA  . ASP   A 1 242 ? 19.673  -10.146 11.402  1.00 11.82 ? 243 ASP   A CA  1 
ATOM   1918 C  C   . ASP   A 1 242 ? 20.169  -8.705  11.606  1.00 13.81 ? 243 ASP   A C   1 
ATOM   1919 O  O   . ASP   A 1 242 ? 21.296  -8.462  12.074  1.00 13.94 ? 243 ASP   A O   1 
ATOM   1920 C  CB  . ASP   A 1 242 ? 20.754  -11.208 11.571  1.00 12.26 ? 243 ASP   A CB  1 
ATOM   1921 C  CG  . ASP   A 1 242 ? 20.183  -12.601 11.673  1.00 12.94 ? 243 ASP   A CG  1 
ATOM   1922 O  OD1 . ASP   A 1 242 ? 19.156  -12.740 12.355  1.00 14.80 ? 243 ASP   A OD1 1 
ATOM   1923 O  OD2 . ASP   A 1 242 ? 20.799  -13.483 11.049  1.00 15.04 ? 243 ASP   A OD2 1 
ATOM   1924 N  N   . ASN   A 1 243 ? 19.279  -7.742  11.356  1.00 12.07 ? 244 ASN   A N   1 
ATOM   1925 C  CA  . ASN   A 1 243 ? 19.594  -6.328  11.560  1.00 12.88 ? 244 ASN   A CA  1 
ATOM   1926 C  C   . ASN   A 1 243 ? 19.029  -5.900  12.913  1.00 12.42 ? 244 ASN   A C   1 
ATOM   1927 O  O   . ASN   A 1 243 ? 18.455  -4.796  12.999  1.00 11.77 ? 244 ASN   A O   1 
ATOM   1928 C  CB  . ASN   A 1 243 ? 19.038  -5.510  10.388  1.00 12.10 ? 244 ASN   A CB  1 
ATOM   1929 C  CG  . ASN   A 1 243 ? 17.550  -5.713  10.213  1.00 13.95 ? 244 ASN   A CG  1 
ATOM   1930 O  OD1 . ASN   A 1 243 ? 16.925  -6.489  10.958  1.00 14.45 ? 244 ASN   A OD1 1 
ATOM   1931 N  ND2 . ASN   A 1 243 ? 16.983  -4.980  9.261   1.00 13.60 ? 244 ASN   A ND2 1 
ATOM   1932 N  N   . TRP   A 1 244 ? 19.262  -6.680  13.974  1.00 13.07 ? 245 TRP   A N   1 
ATOM   1933 C  CA  . TRP   A 1 244 ? 18.823  -6.458  15.332  1.00 10.99 ? 245 TRP   A CA  1 
ATOM   1934 C  C   . TRP   A 1 244 ? 20.005  -6.308  16.260  1.00 13.88 ? 245 TRP   A C   1 
ATOM   1935 O  O   . TRP   A 1 244 ? 20.977  -7.033  16.116  1.00 13.34 ? 245 TRP   A O   1 
ATOM   1936 C  CB  . TRP   A 1 244 ? 17.834  -7.539  15.827  1.00 11.69 ? 245 TRP   A CB  1 
ATOM   1937 C  CG  . TRP   A 1 244 ? 18.329  -8.950  15.615  1.00 13.13 ? 245 TRP   A CG  1 
ATOM   1938 C  CD1 . TRP   A 1 244 ? 18.213  -9.685  14.462  1.00 11.63 ? 245 TRP   A CD1 1 
ATOM   1939 C  CD2 . TRP   A 1 244 ? 18.968  -9.793  16.606  1.00 12.77 ? 245 TRP   A CD2 1 
ATOM   1940 N  NE1 . TRP   A 1 244 ? 18.776  -10.934 14.640  1.00 10.78 ? 245 TRP   A NE1 1 
ATOM   1941 C  CE2 . TRP   A 1 244 ? 19.173  -11.046 15.967  1.00 11.51 ? 245 TRP   A CE2 1 
ATOM   1942 C  CE3 . TRP   A 1 244 ? 19.246  -9.671  17.987  1.00 12.13 ? 245 TRP   A CE3 1 
ATOM   1943 C  CZ2 . TRP   A 1 244 ? 19.804  -12.125 16.631  1.00 13.85 ? 245 TRP   A CZ2 1 
ATOM   1944 C  CZ3 . TRP   A 1 244 ? 19.886  -10.736 18.618  1.00 14.34 ? 245 TRP   A CZ3 1 
ATOM   1945 C  CH2 . TRP   A 1 244 ? 20.062  -11.964 17.969  1.00 15.03 ? 245 TRP   A CH2 1 
ATOM   1946 N  N   . ARG   A 1 245 ? 19.920  -5.355  17.186  1.00 11.26 ? 246 ARG   A N   1 
ATOM   1947 C  CA  . ARG   A 1 245 ? 20.878  -5.269  18.273  1.00 10.75 ? 246 ARG   A CA  1 
ATOM   1948 C  C   . ARG   A 1 245 ? 20.412  -6.182  19.407  1.00 12.60 ? 246 ARG   A C   1 
ATOM   1949 O  O   . ARG   A 1 245 ? 19.238  -6.212  19.767  1.00 14.27 ? 246 ARG   A O   1 
ATOM   1950 C  CB  . ARG   A 1 245 ? 20.941  -3.812  18.743  1.00 12.69 ? 246 ARG   A CB  1 
ATOM   1951 C  CG  . ARG   A 1 245 ? 22.051  -3.544  19.746  1.00 13.66 ? 246 ARG   A CG  1 
ATOM   1952 C  CD  . ARG   A 1 245 ? 21.959  -2.153  20.378  1.00 14.06 ? 246 ARG   A CD  1 
ATOM   1953 N  NE  . ARG   A 1 245 ? 23.230  -1.837  21.011  1.00 13.90 ? 246 ARG   A NE  1 
ATOM   1954 C  CZ  . ARG   A 1 245 ? 23.412  -0.874  21.905  1.00 13.46 ? 246 ARG   A CZ  1 
ATOM   1955 N  NH1 . ARG   A 1 245 ? 22.399  -0.092  22.279  1.00 12.99 ? 246 ARG   A NH1 1 
ATOM   1956 N  NH2 . ARG   A 1 245 ? 24.652  -0.612  22.311  1.00 14.43 ? 246 ARG   A NH2 1 
ATOM   1957 N  N   . PRO   A 1 246 ? 21.302  -6.978  20.023  1.00 12.46 ? 247 PRO   A N   1 
ATOM   1958 C  CA  . PRO   A 1 246 ? 20.945  -7.760  21.198  1.00 13.26 ? 247 PRO   A CA  1 
ATOM   1959 C  C   . PRO   A 1 246 ? 20.578  -6.944  22.437  1.00 13.98 ? 247 PRO   A C   1 
ATOM   1960 O  O   . PRO   A 1 246 ? 20.910  -5.746  22.526  1.00 13.73 ? 247 PRO   A O   1 
ATOM   1961 C  CB  . PRO   A 1 246 ? 22.184  -8.553  21.531  1.00 16.99 ? 247 PRO   A CB  1 
ATOM   1962 C  CG  . PRO   A 1 246 ? 23.082  -8.397  20.306  1.00 21.51 ? 247 PRO   A CG  1 
ATOM   1963 C  CD  . PRO   A 1 246 ? 22.749  -7.045  19.738  1.00 14.82 ? 247 PRO   A CD  1 
ATOM   1964 N  N   . ALA   A 1 247 ? 19.933  -7.610  23.381  1.00 15.37 ? 248 ALA   A N   1 
ATOM   1965 C  CA  . ALA   A 1 247 ? 19.584  -7.019  24.667  1.00 14.07 ? 248 ALA   A CA  1 
ATOM   1966 C  C   . ALA   A 1 247 ? 20.830  -6.463  25.353  1.00 13.73 ? 248 ALA   A C   1 
ATOM   1967 O  O   . ALA   A 1 247 ? 21.866  -7.102  25.413  1.00 15.87 ? 248 ALA   A O   1 
ATOM   1968 C  CB  . ALA   A 1 247 ? 18.791  -8.000  25.513  1.00 16.84 ? 248 ALA   A CB  1 
ATOM   1969 N  N   . GLN   A 1 248 ? 20.664  -5.290  25.960  1.00 13.65 ? 249 GLN   A N   1 
ATOM   1970 C  CA  . GLN   A 1 248 ? 21.722  -4.550  26.626  1.00 12.44 ? 249 GLN   A CA  1 
ATOM   1971 C  C   . GLN   A 1 248 ? 21.441  -4.539  28.124  1.00 14.18 ? 249 GLN   A C   1 
ATOM   1972 O  O   . GLN   A 1 248 ? 20.288  -4.749  28.592  1.00 16.04 ? 249 GLN   A O   1 
ATOM   1973 C  CB  . GLN   A 1 248 ? 21.723  -3.111  26.113  1.00 14.26 ? 249 GLN   A CB  1 
ATOM   1974 C  CG  . GLN   A 1 248 ? 22.063  -2.992  24.637  1.00 14.42 ? 249 GLN   A CG  1 
ATOM   1975 C  CD  . GLN   A 1 248 ? 23.391  -3.631  24.317  1.00 14.36 ? 249 GLN   A CD  1 
ATOM   1976 O  OE1 . GLN   A 1 248 ? 24.447  -3.294  24.891  1.00 18.68 ? 249 GLN   A OE1 1 
ATOM   1977 N  NE2 . GLN   A 1 248 ? 23.339  -4.555  23.378  1.00 16.10 ? 249 GLN   A NE2 1 
ATOM   1978 N  N   . PRO   A 1 249 ? 22.451  -4.224  28.971  1.00 14.00 ? 250 PRO   A N   1 
ATOM   1979 C  CA  . PRO   A 1 249 ? 22.233  -4.280  30.403  1.00 14.41 ? 250 PRO   A CA  1 
ATOM   1980 C  C   . PRO   A 1 249 ? 21.144  -3.323  30.887  1.00 15.31 ? 250 PRO   A C   1 
ATOM   1981 O  O   . PRO   A 1 249 ? 21.149  -2.159  30.512  1.00 15.45 ? 250 PRO   A O   1 
ATOM   1982 C  CB  . PRO   A 1 249 ? 23.616  -3.807  30.934  1.00 18.88 ? 250 PRO   A CB  1 
ATOM   1983 C  CG  . PRO   A 1 249 ? 24.584  -4.218  29.883  1.00 22.70 ? 250 PRO   A CG  1 
ATOM   1984 C  CD  . PRO   A 1 249 ? 23.847  -3.930  28.589  1.00 19.33 ? 250 PRO   A CD  1 
ATOM   1985 N  N   . LEU   A 1 250 ? 20.234  -3.785  31.750  1.00 16.02 ? 251 LEU   A N   1 
ATOM   1986 C  CA  . LEU   A 1 250 ? 19.144  -2.948  32.234  1.00 14.83 ? 251 LEU   A CA  1 
ATOM   1987 C  C   . LEU   A 1 250 ? 19.702  -1.863  33.164  1.00 13.06 ? 251 LEU   A C   1 
ATOM   1988 O  O   . LEU   A 1 250 ? 19.156  -0.723  33.233  1.00 13.76 ? 251 LEU   A O   1 
ATOM   1989 C  CB  . LEU   A 1 250 ? 18.113  -3.841  32.950  1.00 16.30 ? 251 LEU   A CB  1 
ATOM   1990 C  CG  . LEU   A 1 250 ? 16.829  -3.130  33.409  1.00 16.74 ? 251 LEU   A CG  1 
ATOM   1991 C  CD1 . LEU   A 1 250 ? 16.155  -2.487  32.186  1.00 18.02 ? 251 LEU   A CD1 1 
ATOM   1992 C  CD2 . LEU   A 1 250 ? 15.893  -4.120  34.103  1.00 20.22 ? 251 LEU   A CD2 1 
ATOM   1993 N  N   . LYS   A 1 251 ? 20.776  -2.139  33.922  1.00 16.86 ? 252 LYS   A N   1 
ATOM   1994 C  CA  . LYS   A 1 251 ? 21.348  -1.116  34.813  1.00 18.66 ? 252 LYS   A CA  1 
ATOM   1995 C  C   . LYS   A 1 251 ? 20.316  -0.602  35.813  1.00 17.68 ? 252 LYS   A C   1 
ATOM   1996 O  O   . LYS   A 1 251 ? 19.517  -1.382  36.367  1.00 22.36 ? 252 LYS   A O   1 
ATOM   1997 C  CB  . LYS   A 1 251 ? 22.165  -0.082  34.027  1.00 18.44 ? 252 LYS   A CB  1 
ATOM   1998 C  CG  . LYS   A 1 251 ? 23.367  -0.791  33.381  1.00 24.74 ? 252 LYS   A CG  1 
ATOM   1999 C  CD  . LYS   A 1 251 ? 24.438  0.093   32.909  1.00 34.45 ? 252 LYS   A CD  1 
ATOM   2000 C  CE  . LYS   A 1 251 ? 25.699  -0.647  32.532  1.00 34.36 ? 252 LYS   A CE  1 
ATOM   2001 N  NZ  . LYS   A 1 251 ? 26.516  0.319   31.767  1.00 43.28 ? 252 LYS   A NZ  1 
ATOM   2002 N  N   . ASN   A 1 252 ? 20.299  0.712   36.011  1.00 18.51 ? 253 ASN   A N   1 
ATOM   2003 C  CA  . ASN   A 1 252 ? 19.510  1.271   37.088  1.00 27.82 ? 253 ASN   A CA  1 
ATOM   2004 C  C   . ASN   A 1 252 ? 18.154  1.630   36.499  1.00 25.00 ? 253 ASN   A C   1 
ATOM   2005 O  O   . ASN   A 1 252 ? 17.868  2.861   36.509  1.00 31.54 ? 253 ASN   A O   1 
ATOM   2006 C  CB  . ASN   A 1 252 ? 20.112  2.581   37.622  1.00 38.96 ? 253 ASN   A CB  1 
ATOM   2007 C  CG  . ASN   A 1 252 ? 19.952  2.757   39.123  1.00 54.52 ? 253 ASN   A CG  1 
ATOM   2008 O  OD1 . ASN   A 1 252 ? 18.836  2.853   39.625  1.00 51.97 ? 253 ASN   A OD1 1 
ATOM   2009 N  ND2 . ASN   A 1 252 ? 21.071  2.781   39.847  1.00 69.40 ? 253 ASN   A ND2 1 
ATOM   2010 N  N   . ARG   A 1 253 ? 17.411  0.597   35.957  1.00 21.35 ? 254 ARG   A N   1 
ATOM   2011 C  CA  . ARG   A 1 253 ? 16.137  0.931   35.336  1.00 13.39 ? 254 ARG   A CA  1 
ATOM   2012 C  C   . ARG   A 1 253 ? 15.019  -0.019  35.716  1.00 17.40 ? 254 ARG   A C   1 
ATOM   2013 O  O   . ARG   A 1 253 ? 15.267  -1.221  35.859  1.00 25.26 ? 254 ARG   A O   1 
ATOM   2014 C  CB  . ARG   A 1 253 ? 16.210  1.024   33.798  1.00 12.29 ? 254 ARG   A CB  1 
ATOM   2015 C  CG  . ARG   A 1 253 ? 17.068  2.191   33.302  1.00 12.98 ? 254 ARG   A CG  1 
ATOM   2016 C  CD  . ARG   A 1 253 ? 17.232  2.176   31.797  1.00 13.25 ? 254 ARG   A CD  1 
ATOM   2017 N  NE  . ARG   A 1 253 ? 18.022  0.996   31.326  1.00 11.97 ? 254 ARG   A NE  1 
ATOM   2018 C  CZ  . ARG   A 1 253 ? 18.282  0.748   30.046  1.00 13.01 ? 254 ARG   A CZ  1 
ATOM   2019 N  NH1 . ARG   A 1 253 ? 17.655  1.420   29.061  1.00 13.75 ? 254 ARG   A NH1 1 
ATOM   2020 N  NH2 . ARG   A 1 253 ? 19.065  -0.280  29.709  1.00 11.91 ? 254 ARG   A NH2 1 
ATOM   2021 N  N   . GLN   A 1 254 ? 13.799  0.557   35.791  1.00 15.48 ? 255 GLN   A N   1 
ATOM   2022 C  CA  . GLN   A 1 254 ? 12.566  -0.169  36.042  1.00 16.83 ? 255 GLN   A CA  1 
ATOM   2023 C  C   . GLN   A 1 254 ? 11.748  -0.222  34.764  1.00 17.10 ? 255 GLN   A C   1 
ATOM   2024 O  O   . GLN   A 1 254 ? 11.457  0.810   34.122  1.00 20.53 ? 255 GLN   A O   1 
ATOM   2025 C  CB  . GLN   A 1 254 ? 11.789  0.480   37.188  1.00 27.09 ? 255 GLN   A CB  1 
ATOM   2026 C  CG  . GLN   A 1 254 ? 11.536  -0.520  38.310  1.00 41.95 ? 255 GLN   A CG  1 
ATOM   2027 C  CD  . GLN   A 1 254 ? 11.730  -0.050  39.743  1.00 43.95 ? 255 GLN   A CD  1 
ATOM   2028 O  OE1 . GLN   A 1 254 ? 11.703  1.142   40.066  1.00 74.33 ? 255 GLN   A OE1 1 
ATOM   2029 N  NE2 . GLN   A 1 254 ? 11.889  -1.028  40.637  1.00 47.48 ? 255 GLN   A NE2 1 
ATOM   2030 N  N   . ILE   A 1 255 ? 11.296  -1.425  34.444  1.00 15.13 ? 256 ILE   A N   1 
ATOM   2031 C  CA  . ILE   A 1 255 ? 10.311  -1.582  33.382  1.00 14.54 ? 256 ILE   A CA  1 
ATOM   2032 C  C   . ILE   A 1 255 ? 8.920   -1.651  34.022  1.00 14.71 ? 256 ILE   A C   1 
ATOM   2033 O  O   . ILE   A 1 255 ? 8.712   -2.382  34.998  1.00 16.02 ? 256 ILE   A O   1 
ATOM   2034 C  CB  . ILE   A 1 255 ? 10.603  -2.854  32.538  1.00 13.13 ? 256 ILE   A CB  1 
ATOM   2035 C  CG1 . ILE   A 1 255 ? 12.001  -2.834  31.915  1.00 16.15 ? 256 ILE   A CG1 1 
ATOM   2036 C  CG2 . ILE   A 1 255 ? 9.511   -3.040  31.482  1.00 15.83 ? 256 ILE   A CG2 1 
ATOM   2037 C  CD1 . ILE   A 1 255 ? 12.338  -4.094  31.162  1.00 15.96 ? 256 ILE   A CD1 1 
ATOM   2038 N  N   . LYS   A 1 256 ? 8.007   -0.789  33.557  1.00 14.27 ? 257 LYS   A N   1 
ATOM   2039 C  CA  . LYS   A 1 256 ? 6.678   -0.727  34.163  1.00 14.83 ? 257 LYS   A CA  1 
ATOM   2040 C  C   . LYS   A 1 256 ? 5.645   -1.289  33.185  1.00 11.93 ? 257 LYS   A C   1 
ATOM   2041 O  O   . LYS   A 1 256 ? 5.833   -1.129  31.974  1.00 14.19 ? 257 LYS   A O   1 
ATOM   2042 C  CB  . LYS   A 1 256 ? 6.375   0.747   34.430  1.00 14.41 ? 257 LYS   A CB  1 
ATOM   2043 C  CG  . LYS   A 1 256 ? 7.346   1.291   35.486  1.00 19.46 ? 257 LYS   A CG  1 
ATOM   2044 C  CD  . LYS   A 1 256 ? 7.032   2.647   35.932  1.00 26.47 ? 257 LYS   A CD  1 
ATOM   2045 C  CE  . LYS   A 1 256 ? 8.124   3.180   36.839  1.00 33.05 ? 257 LYS   A CE  1 
ATOM   2046 N  NZ  . LYS   A 1 256 ? 8.090   4.664   36.920  1.00 38.15 ? 257 LYS   A NZ  1 
ATOM   2047 N  N   . ALA   A 1 257 ? 4.605   -1.949  33.739  1.00 15.91 ? 258 ALA   A N   1 
ATOM   2048 C  CA  . ALA   A 1 257 ? 3.559   -2.567  32.937  1.00 14.99 ? 258 ALA   A CA  1 
ATOM   2049 C  C   . ALA   A 1 257 ? 2.310   -1.711  33.105  1.00 13.07 ? 258 ALA   A C   1 
ATOM   2050 O  O   . ALA   A 1 257 ? 1.986   -1.315  34.241  1.00 16.61 ? 258 ALA   A O   1 
ATOM   2051 C  CB  . ALA   A 1 257 ? 3.305   -4.018  33.326  1.00 17.59 ? 258 ALA   A CB  1 
ATOM   2052 N  N   . SER   A 1 258 ? 1.559   -1.561  31.986  1.00 15.06 ? 259 SER   A N   1 
ATOM   2053 C  CA  . SER   A 1 258 ? 0.323   -0.793  31.998  1.00 15.97 ? 259 SER   A CA  1 
ATOM   2054 C  C   . SER   A 1 258 ? -0.862  -1.657  32.430  1.00 15.00 ? 259 SER   A C   1 
ATOM   2055 O  O   . SER   A 1 258 ? -1.988  -1.156  32.505  1.00 21.55 ? 259 SER   A O   1 
ATOM   2056 C  CB  . SER   A 1 258 ? 0.066   -0.309  30.616  1.00 15.64 ? 259 SER   A CB  1 
ATOM   2057 O  OG  . SER   A 1 258 ? -0.439  -1.308  29.700  1.00 15.78 ? 259 SER   A OG  1 
ATOM   2058 N  N   . PHE   A 1 259 ? -0.606  -2.929  32.664  1.00 16.90 ? 260 PHE   A N   1 
ATOM   2059 C  CA  . PHE   A 1 259 ? -1.657  -3.914  32.841  1.00 19.42 ? 260 PHE   A CA  1 
ATOM   2060 C  C   . PHE   A 1 259 ? -1.331  -4.864  33.984  1.00 24.11 ? 260 PHE   A C   1 
ATOM   2061 O  O   . PHE   A 1 259 ? -0.163  -5.046  34.338  1.00 23.23 ? 260 PHE   A O   1 
ATOM   2062 C  CB  . PHE   A 1 259 ? -1.822  -4.716  31.545  1.00 19.13 ? 260 PHE   A CB  1 
ATOM   2063 C  CG  . PHE   A 1 259 ? -0.562  -5.489  31.194  1.00 16.93 ? 260 PHE   A CG  1 
ATOM   2064 C  CD1 . PHE   A 1 259 ? 0.418   -4.870  30.459  1.00 17.99 ? 260 PHE   A CD1 1 
ATOM   2065 C  CD2 . PHE   A 1 259 ? -0.281  -6.758  31.694  1.00 24.16 ? 260 PHE   A CD2 1 
ATOM   2066 C  CE1 . PHE   A 1 259 ? 1.604   -5.519  30.136  1.00 18.36 ? 260 PHE   A CE1 1 
ATOM   2067 C  CE2 . PHE   A 1 259 ? 0.901   -7.407  31.376  1.00 24.51 ? 260 PHE   A CE2 1 
ATOM   2068 C  CZ  . PHE   A 1 259 ? 1.857   -6.788  30.614  1.00 23.20 ? 260 PHE   A CZ  1 
ATOM   2069 N  N   . LYS   A 1 260 ? -2.421  -5.442  34.508  1.00 29.86 ? 261 LYS   A N   1 
ATOM   2070 C  CA  . LYS   A 1 260 ? -2.642  -6.712  35.200  1.00 43.56 ? 261 LYS   A CA  1 
ATOM   2071 C  C   . LYS   A 1 260 ? -2.513  -6.492  36.705  1.00 52.72 ? 261 LYS   A C   1 
ATOM   2072 O  O   . LYS   A 1 260 ? -1.523  -6.910  37.304  1.00 73.53 ? 261 LYS   A O   1 
ATOM   2073 C  CB  . LYS   A 1 260 ? -1.972  -7.952  34.577  1.00 47.06 ? 261 LYS   A CB  1 
ATOM   2074 C  CG  . LYS   A 1 260 ? -2.825  -8.707  33.549  1.00 61.22 ? 261 LYS   A CG  1 
ATOM   2075 O  OXT . LYS   A 1 260 ? -3.436  -5.880  37.279  1.00 65.08 ? 261 LYS   A OXT 1 
HETATM 2076 ZN ZN  . ZN    B 2 .   ? 14.347  0.120   15.368  1.00 11.84 ? 301 ZN    A ZN  1 
HETATM 2077 C  C13 . A1IEN C 3 .   ? 17.966  6.873   14.097  1.00 15.69 ? 302 A1IEN A C13 1 
HETATM 2078 C  C20 . A1IEN C 3 .   ? 17.405  0.958   11.371  1.00 13.48 ? 302 A1IEN A C20 1 
HETATM 2079 C  C12 . A1IEN C 3 .   ? 16.441  7.107   13.873  1.00 16.38 ? 302 A1IEN A C12 1 
HETATM 2080 C  C16 . A1IEN C 3 .   ? 19.534  10.416  14.381  1.00 19.23 ? 302 A1IEN A C16 1 
HETATM 2081 O  O22 . A1IEN C 3 .   ? 17.527  -0.148  12.081  1.00 12.86 ? 302 A1IEN A O22 1 
HETATM 2082 C  C23 . A1IEN C 3 .   ? 17.978  -1.352  11.422  1.00 14.98 ? 302 A1IEN A C23 1 
HETATM 2083 O  O21 . A1IEN C 3 .   ? 17.663  1.026   10.153  1.00 16.93 ? 302 A1IEN A O21 1 
HETATM 2084 C  C2  . A1IEN C 3 .   ? 16.904  2.073   12.164  1.00 12.40 ? 302 A1IEN A C2  1 
HETATM 2085 C  C3  . A1IEN C 3 .   ? 16.848  3.335   11.500  1.00 13.75 ? 302 A1IEN A C3  1 
HETATM 2086 C  C4  . A1IEN C 3 .   ? 16.393  4.380   12.334  1.00 11.48 ? 302 A1IEN A C4  1 
HETATM 2087 C  C5  . A1IEN C 3 .   ? 16.078  4.288   13.717  1.00 12.81 ? 302 A1IEN A C5  1 
HETATM 2088 C  C6  . A1IEN C 3 .   ? 16.193  3.007   14.329  1.00 11.74 ? 302 A1IEN A C6  1 
HETATM 2089 S  S7  . A1IEN C 3 .   ? 15.782  2.821   16.005  1.00 12.85 ? 302 A1IEN A S7  1 
HETATM 2090 O  O9  . A1IEN C 3 .   ? 14.486  3.437   16.177  1.00 13.31 ? 302 A1IEN A O9  1 
HETATM 2091 N  N10 . A1IEN C 3 .   ? 15.704  1.220   16.115  1.00 11.04 ? 302 A1IEN A N10 1 
HETATM 2092 O  O8  . A1IEN C 3 .   ? 16.889  3.347   16.857  1.00 15.03 ? 302 A1IEN A O8  1 
HETATM 2093 C  C1  . A1IEN C 3 .   ? 16.690  1.978   13.502  1.00 10.22 ? 302 A1IEN A C1  1 
HETATM 2094 S  S11 . A1IEN C 3 .   ? 15.479  5.751   14.604  1.00 15.42 ? 302 A1IEN A S11 1 
HETATM 2095 C  C14 . A1IEN C 3 .   ? 18.815  8.133   13.821  1.00 19.14 ? 302 A1IEN A C14 1 
HETATM 2096 C  C18 . A1IEN C 3 .   ? 19.584  8.161   12.673  1.00 22.75 ? 302 A1IEN A C18 1 
HETATM 2097 C  C19 . A1IEN C 3 .   ? 20.325  9.327   12.398  1.00 27.36 ? 302 A1IEN A C19 1 
HETATM 2098 C  C17 . A1IEN C 3 .   ? 20.283  10.486  13.217  1.00 26.48 ? 302 A1IEN A C17 1 
HETATM 2099 C  C15 . A1IEN C 3 .   ? 18.753  9.262   14.620  1.00 15.27 ? 302 A1IEN A C15 1 
HETATM 2100 S  S   . DMS   D 4 .   ? 22.414  -9.600  14.971  1.00 27.60 ? 303 DMS   A S   1 
HETATM 2101 O  O   . DMS   D 4 .   ? 22.905  -11.046 14.643  1.00 29.17 ? 303 DMS   A O   1 
HETATM 2102 C  C1  . DMS   D 4 .   ? 23.679  -8.582  14.292  1.00 29.08 ? 303 DMS   A C1  1 
HETATM 2103 C  C2  . DMS   D 4 .   ? 22.767  -9.385  16.641  1.00 23.48 ? 303 DMS   A C2  1 
HETATM 2104 O  O   . HOH   E 5 .   ? 2.005   19.584  18.431  1.00 43.89 ? 401 HOH   A O   1 
HETATM 2105 O  O   . HOH   E 5 .   ? 17.808  19.933  21.663  1.00 35.32 ? 402 HOH   A O   1 
HETATM 2106 O  O   . HOH   E 5 .   ? 0.304   -5.257  -2.024  1.00 33.14 ? 403 HOH   A O   1 
HETATM 2107 O  O   . HOH   E 5 .   ? -4.297  11.423  13.073  1.00 34.82 ? 404 HOH   A O   1 
HETATM 2108 O  O   . HOH   E 5 .   ? 4.047   19.918  22.048  1.00 39.46 ? 405 HOH   A O   1 
HETATM 2109 O  O   . HOH   E 5 .   ? 8.044   15.205  31.968  1.00 38.47 ? 406 HOH   A O   1 
HETATM 2110 O  O   . HOH   E 5 .   ? 23.861  -7.077  -6.336  1.00 34.69 ? 407 HOH   A O   1 
HETATM 2111 O  O   . HOH   E 5 .   ? 13.405  -2.896  40.023  1.00 37.40 ? 408 HOH   A O   1 
HETATM 2112 O  O   . HOH   E 5 .   ? 30.175  -8.030  13.458  1.00 26.10 ? 409 HOH   A O   1 
HETATM 2113 O  O   . HOH   E 5 .   ? 8.599   6.349   35.102  1.00 50.24 ? 410 HOH   A O   1 
HETATM 2114 O  O   . HOH   E 5 .   ? 4.745   -13.481 32.924  1.00 38.97 ? 411 HOH   A O   1 
HETATM 2115 O  O   . HOH   E 5 .   ? 10.009  -13.313 34.238  1.00 33.84 ? 412 HOH   A O   1 
HETATM 2116 O  O   . HOH   E 5 .   ? 22.790  -13.531 -1.327  1.00 33.33 ? 413 HOH   A O   1 
HETATM 2117 O  O   . HOH   E 5 .   ? -3.173  -12.372 19.633  1.00 40.38 ? 414 HOH   A O   1 
HETATM 2118 O  O   . HOH   E 5 .   ? 21.560  -8.096  -5.309  1.00 34.66 ? 415 HOH   A O   1 
HETATM 2119 O  O   . HOH   E 5 .   ? 15.817  4.153   37.345  1.00 30.44 ? 416 HOH   A O   1 
HETATM 2120 O  O   . HOH   E 5 .   ? 29.310  5.153   27.656  1.00 40.78 ? 417 HOH   A O   1 
HETATM 2121 O  O   . HOH   E 5 .   ? 23.246  9.869   27.942  1.00 40.37 ? 418 HOH   A O   1 
HETATM 2122 O  O   . HOH   E 5 .   ? 12.304  -1.911  7.846   1.00 14.70 ? 419 HOH   A O   1 
HETATM 2123 O  O   . HOH   E 5 .   ? 25.290  -1.496  26.567  1.00 23.08 ? 420 HOH   A O   1 
HETATM 2124 O  O   . HOH   E 5 .   ? 22.564  -2.318  -12.328 1.00 35.05 ? 421 HOH   A O   1 
HETATM 2125 O  O   . HOH   E 5 .   ? 6.826   -14.771 29.150  1.00 23.15 ? 422 HOH   A O   1 
HETATM 2126 O  O   . HOH   E 5 .   ? 24.562  6.961   29.806  1.00 19.49 ? 423 HOH   A O   1 
HETATM 2127 O  O   . HOH   E 5 .   ? 5.188   5.581   35.404  1.00 33.36 ? 424 HOH   A O   1 
HETATM 2128 O  O   . HOH   E 5 .   ? 25.747  -1.545  2.926   1.00 32.17 ? 425 HOH   A O   1 
HETATM 2129 O  O   . HOH   E 5 .   ? 16.171  -9.988  32.175  1.00 24.45 ? 426 HOH   A O   1 
HETATM 2130 O  O   . HOH   E 5 .   ? 6.777   16.248  27.072  1.00 28.65 ? 427 HOH   A O   1 
HETATM 2131 O  O   . HOH   E 5 .   ? 8.649   14.314  29.366  1.00 34.15 ? 428 HOH   A O   1 
HETATM 2132 O  O   . HOH   E 5 .   ? 19.772  -2.152  15.735  1.00 14.43 ? 429 HOH   A O   1 
HETATM 2133 O  O   . HOH   E 5 .   ? 23.608  -9.697  9.438   1.00 24.87 ? 430 HOH   A O   1 
HETATM 2134 O  O   . HOH   E 5 .   ? 11.806  7.840   29.000  1.00 23.16 ? 431 HOH   A O   1 
HETATM 2135 O  O   . HOH   E 5 .   ? 26.318  -8.370  13.122  1.00 30.61 ? 432 HOH   A O   1 
HETATM 2136 O  O   . HOH   E 5 .   ? 21.275  3.662   7.839   1.00 38.30 ? 433 HOH   A O   1 
HETATM 2137 O  O   . HOH   E 5 .   ? 14.859  -2.941  -6.513  1.00 25.52 ? 434 HOH   A O   1 
HETATM 2138 O  O   . HOH   E 5 .   ? -4.554  -8.820  17.834  1.00 29.93 ? 435 HOH   A O   1 
HETATM 2139 O  O   . HOH   E 5 .   ? 21.205  0.793   -4.649  1.00 17.18 ? 436 HOH   A O   1 
HETATM 2140 O  O   . HOH   E 5 .   ? -3.123  10.444  20.133  1.00 25.43 ? 437 HOH   A O   1 
HETATM 2141 O  O   . HOH   E 5 .   ? 10.145  -3.322  38.117  1.00 50.71 ? 438 HOH   A O   1 
HETATM 2142 O  O   . HOH   E 5 .   ? 14.787  -9.607  36.658  1.00 32.99 ? 439 HOH   A O   1 
HETATM 2143 O  O   . HOH   E 5 .   ? 24.230  -12.182 12.679  1.00 36.86 ? 440 HOH   A O   1 
HETATM 2144 O  O   . HOH   E 5 .   ? 15.116  19.422  27.603  1.00 37.84 ? 441 HOH   A O   1 
HETATM 2145 O  O   . HOH   E 5 .   ? 20.184  -15.582 18.068  1.00 32.16 ? 442 HOH   A O   1 
HETATM 2146 O  O   . HOH   E 5 .   ? 5.793   -9.268  -3.620  1.00 43.69 ? 443 HOH   A O   1 
HETATM 2147 O  O   . HOH   E 5 .   ? 28.584  -6.249  -1.100  1.00 25.86 ? 444 HOH   A O   1 
HETATM 2148 O  O   . HOH   E 5 .   ? 32.335  -5.161  22.473  1.00 31.92 ? 445 HOH   A O   1 
HETATM 2149 O  O   . HOH   E 5 .   ? 0.275   10.265  30.013  1.00 34.70 ? 446 HOH   A O   1 
HETATM 2150 O  O   . HOH   E 5 .   ? 12.366  2.447   -6.542  1.00 29.43 ? 447 HOH   A O   1 
HETATM 2151 O  O   . HOH   E 5 .   ? 10.583  -16.401 17.177  1.00 17.12 ? 448 HOH   A O   1 
HETATM 2152 O  O   . HOH   E 5 .   ? 19.633  11.131  28.090  1.00 29.56 ? 449 HOH   A O   1 
HETATM 2153 O  O   . HOH   E 5 .   ? 0.717   12.641  26.547  1.00 22.52 ? 450 HOH   A O   1 
HETATM 2154 O  O   . HOH   E 5 .   ? 23.333  3.195   4.745   1.00 47.36 ? 451 HOH   A O   1 
HETATM 2155 O  O   . HOH   E 5 .   ? 28.844  0.757   -5.696  1.00 33.02 ? 452 HOH   A O   1 
HETATM 2156 O  O   . HOH   E 5 .   ? 12.496  -13.506 36.741  1.00 29.14 ? 453 HOH   A O   1 
HETATM 2157 O  O   . HOH   E 5 .   ? 14.266  -13.006 31.585  1.00 27.48 ? 454 HOH   A O   1 
HETATM 2158 O  O   . HOH   E 5 .   ? 5.618   2.444   -4.910  1.00 29.95 ? 455 HOH   A O   1 
HETATM 2159 O  O   . HOH   E 5 .   ? 21.174  3.073   34.459  1.00 35.41 ? 456 HOH   A O   1 
HETATM 2160 O  O   . HOH   E 5 .   ? 13.006  -13.548 11.445  1.00 14.65 ? 457 HOH   A O   1 
HETATM 2161 O  O   . HOH   E 5 .   ? 10.332  10.601  25.524  1.00 14.04 ? 458 HOH   A O   1 
HETATM 2162 O  O   . HOH   E 5 .   ? 30.589  -3.447  -7.683  1.00 37.81 ? 459 HOH   A O   1 
HETATM 2163 O  O   . HOH   E 5 .   ? 24.566  -0.976  4.737   1.00 37.00 ? 460 HOH   A O   1 
HETATM 2164 O  O   . HOH   E 5 .   ? 6.109   22.100  17.692  1.00 20.75 ? 461 HOH   A O   1 
HETATM 2165 O  O   . HOH   E 5 .   ? -6.139  -10.947 20.526  1.00 39.95 ? 462 HOH   A O   1 
HETATM 2166 O  O   . HOH   E 5 .   ? 2.563   -10.651 -3.489  1.00 25.95 ? 463 HOH   A O   1 
HETATM 2167 O  O   . HOH   E 5 .   ? 14.139  7.897   6.086   1.00 16.52 ? 464 HOH   A O   1 
HETATM 2168 O  O   . HOH   E 5 .   ? 20.539  15.955  16.192  1.00 23.34 ? 465 HOH   A O   1 
HETATM 2169 O  O   . HOH   E 5 .   ? 3.112   12.387  11.335  1.00 22.13 ? 466 HOH   A O   1 
HETATM 2170 O  O   . HOH   E 5 .   ? -4.919  8.091   26.912  1.00 31.34 ? 467 HOH   A O   1 
HETATM 2171 O  O   . HOH   E 5 .   ? 8.021   -20.301 8.683   1.00 28.06 ? 468 HOH   A O   1 
HETATM 2172 O  O   . HOH   E 5 .   ? 27.458  -3.757  3.961   1.00 36.69 ? 469 HOH   A O   1 
HETATM 2173 O  O   . HOH   E 5 .   ? 16.960  22.849  14.863  1.00 31.80 ? 470 HOH   A O   1 
HETATM 2174 O  O   . HOH   E 5 .   ? -6.913  8.054   21.543  1.00 29.83 ? 471 HOH   A O   1 
HETATM 2175 O  O   . HOH   E 5 .   ? 25.620  0.790   -5.490  1.00 40.44 ? 472 HOH   A O   1 
HETATM 2176 O  O   . HOH   E 5 .   ? -6.320  -3.404  27.603  1.00 34.88 ? 473 HOH   A O   1 
HETATM 2177 O  O   . HOH   E 5 .   ? 3.942   -6.495  20.442  1.00 13.62 ? 474 HOH   A O   1 
HETATM 2178 O  O   . HOH   E 5 .   ? -1.737  -4.005  2.890   1.00 26.33 ? 475 HOH   A O   1 
HETATM 2179 O  O   . HOH   E 5 .   ? 5.651   21.325  13.127  1.00 26.64 ? 476 HOH   A O   1 
HETATM 2180 O  O   . HOH   E 5 .   ? 7.420   21.915  15.092  1.00 24.62 ? 477 HOH   A O   1 
HETATM 2181 O  O   . HOH   E 5 .   ? -4.854  -3.554  13.333  1.00 38.41 ? 478 HOH   A O   1 
HETATM 2182 O  O   . HOH   E 5 .   ? -4.775  -13.448 8.208   1.00 29.81 ? 479 HOH   A O   1 
HETATM 2183 O  O   . HOH   E 5 .   ? -0.865  -12.321 18.656  1.00 34.39 ? 480 HOH   A O   1 
HETATM 2184 O  O   . HOH   E 5 .   ? 20.515  12.739  23.400  1.00 19.42 ? 481 HOH   A O   1 
HETATM 2185 O  O   . HOH   E 5 .   ? -3.721  -5.904  9.142   1.00 23.78 ? 482 HOH   A O   1 
HETATM 2186 O  O   . HOH   E 5 .   ? 7.107   16.416  5.910   1.00 44.06 ? 483 HOH   A O   1 
HETATM 2187 O  O   . HOH   E 5 .   ? 22.805  -5.304  -8.150  1.00 37.50 ? 484 HOH   A O   1 
HETATM 2188 O  O   . HOH   E 5 .   ? 19.106  -2.857  -7.102  1.00 27.25 ? 485 HOH   A O   1 
HETATM 2189 O  O   . HOH   E 5 .   ? 17.360  -11.116 -2.820  1.00 21.48 ? 486 HOH   A O   1 
HETATM 2190 O  O   . HOH   E 5 .   ? 14.187  22.964  19.575  1.00 18.39 ? 487 HOH   A O   1 
HETATM 2191 O  O   . HOH   E 5 .   ? 7.076   12.217  27.903  1.00 20.78 ? 488 HOH   A O   1 
HETATM 2192 O  O   . HOH   E 5 .   ? 0.686   15.776  28.720  1.00 35.06 ? 489 HOH   A O   1 
HETATM 2193 O  O   . HOH   E 5 .   ? 27.629  -2.978  0.873   1.00 47.57 ? 490 HOH   A O   1 
HETATM 2194 O  O   . HOH   E 5 .   ? 26.772  3.294   1.758   1.00 38.65 ? 491 HOH   A O   1 
HETATM 2195 O  O   . HOH   E 5 .   ? 27.326  -9.386  15.618  1.00 33.86 ? 492 HOH   A O   1 
HETATM 2196 O  O   . HOH   E 5 .   ? 17.490  -9.197  20.904  1.00 13.86 ? 493 HOH   A O   1 
HETATM 2197 O  O   . HOH   E 5 .   ? -3.014  -0.749  28.987  1.00 37.52 ? 494 HOH   A O   1 
HETATM 2198 O  O   . HOH   E 5 .   ? -0.167  9.656   1.957   1.00 19.92 ? 495 HOH   A O   1 
HETATM 2199 O  O   . HOH   E 5 .   ? 1.191   -2.256  41.338  1.00 32.02 ? 496 HOH   A O   1 
HETATM 2200 O  O   . HOH   E 5 .   ? 4.823   17.731  23.690  1.00 21.79 ? 497 HOH   A O   1 
HETATM 2201 O  O   . HOH   E 5 .   ? -2.072  -1.264  6.813   1.00 23.82 ? 498 HOH   A O   1 
HETATM 2202 O  O   . HOH   E 5 .   ? 19.909  0.741   -12.982 1.00 43.72 ? 499 HOH   A O   1 
HETATM 2203 O  O   . HOH   E 5 .   ? 2.716   -1.932  -2.590  1.00 27.65 ? 500 HOH   A O   1 
HETATM 2204 O  O   . HOH   E 5 .   ? 26.456  9.029   20.046  1.00 20.77 ? 501 HOH   A O   1 
HETATM 2205 O  O   . HOH   E 5 .   ? -4.648  0.833   34.929  1.00 36.00 ? 502 HOH   A O   1 
HETATM 2206 O  O   . HOH   E 5 .   ? -0.865  7.469   4.795   1.00 19.18 ? 503 HOH   A O   1 
HETATM 2207 O  O   . HOH   E 5 .   ? 18.325  -16.091 31.115  1.00 30.54 ? 504 HOH   A O   1 
HETATM 2208 O  O   . HOH   E 5 .   ? 14.410  -3.330  37.392  1.00 21.65 ? 505 HOH   A O   1 
HETATM 2209 O  O   . HOH   E 5 .   ? 9.967   -17.762 7.314   1.00 27.48 ? 506 HOH   A O   1 
HETATM 2210 O  O   . HOH   E 5 .   ? 8.110   -14.979 26.688  1.00 18.53 ? 507 HOH   A O   1 
HETATM 2211 O  O   . HOH   E 5 .   ? 22.814  -14.005 9.257   1.00 25.26 ? 508 HOH   A O   1 
HETATM 2212 O  O   . HOH   E 5 .   ? 3.252   8.233   38.520  1.00 31.60 ? 509 HOH   A O   1 
HETATM 2213 O  O   . HOH   E 5 .   ? 9.226   11.266  2.697   1.00 42.33 ? 510 HOH   A O   1 
HETATM 2214 O  O   . HOH   E 5 .   ? 22.282  -14.451 -4.877  1.00 33.35 ? 511 HOH   A O   1 
HETATM 2215 O  O   . HOH   E 5 .   ? 27.874  -1.524  30.243  1.00 38.62 ? 512 HOH   A O   1 
HETATM 2216 O  O   . HOH   E 5 .   ? 23.553  -11.355 5.241   1.00 27.30 ? 513 HOH   A O   1 
HETATM 2217 O  O   . HOH   E 5 .   ? 17.238  -13.983 24.321  1.00 18.39 ? 514 HOH   A O   1 
HETATM 2218 O  O   . HOH   E 5 .   ? 10.364  10.403  7.670   1.00 19.35 ? 515 HOH   A O   1 
HETATM 2219 O  O   . HOH   E 5 .   ? 9.443   12.851  6.846   1.00 42.72 ? 516 HOH   A O   1 
HETATM 2220 O  O   . HOH   E 5 .   ? -2.160  1.723   34.523  1.00 37.17 ? 517 HOH   A O   1 
HETATM 2221 O  O   . HOH   E 5 .   ? 10.362  -17.581 20.024  1.00 21.17 ? 518 HOH   A O   1 
HETATM 2222 O  O   . HOH   E 5 .   ? 25.489  -0.527  28.937  1.00 26.85 ? 519 HOH   A O   1 
HETATM 2223 O  O   . HOH   E 5 .   ? 3.119   -18.655 8.015   1.00 23.08 ? 520 HOH   A O   1 
HETATM 2224 O  O   . HOH   E 5 .   ? 19.155  -14.082 -3.856  1.00 35.83 ? 521 HOH   A O   1 
HETATM 2225 O  O   . HOH   E 5 .   ? 29.582  -1.947  21.067  1.00 18.18 ? 522 HOH   A O   1 
HETATM 2226 O  O   . HOH   E 5 .   ? 4.903   -10.429 24.516  1.00 18.42 ? 523 HOH   A O   1 
HETATM 2227 O  O   . HOH   E 5 .   ? -0.608  -5.331  23.692  1.00 17.31 ? 524 HOH   A O   1 
HETATM 2228 O  O   . HOH   E 5 .   ? -0.649  21.429  17.256  1.00 45.70 ? 525 HOH   A O   1 
HETATM 2229 O  O   . HOH   E 5 .   ? 22.329  -9.819  25.117  1.00 27.84 ? 526 HOH   A O   1 
HETATM 2230 O  O   . HOH   E 5 .   ? 16.496  -11.626 18.068  1.00 13.44 ? 527 HOH   A O   1 
HETATM 2231 O  O   . HOH   E 5 .   ? 8.153   -7.286  -3.133  1.00 32.15 ? 528 HOH   A O   1 
HETATM 2232 O  O   . HOH   E 5 .   ? -5.311  4.620   20.674  1.00 24.54 ? 529 HOH   A O   1 
HETATM 2233 O  O   . HOH   E 5 .   ? 3.625   -14.322 22.048  1.00 24.86 ? 530 HOH   A O   1 
HETATM 2234 O  O   . HOH   E 5 .   ? -1.160  5.689   -2.964  1.00 25.05 ? 531 HOH   A O   1 
HETATM 2235 O  O   . HOH   E 5 .   ? -5.269  5.330   15.441  1.00 27.20 ? 532 HOH   A O   1 
HETATM 2236 O  O   . HOH   E 5 .   ? 20.353  4.622   12.084  1.00 27.40 ? 533 HOH   A O   1 
HETATM 2237 O  O   . HOH   E 5 .   ? 7.523   -16.688 14.683  1.00 20.92 ? 534 HOH   A O   1 
HETATM 2238 O  O   . HOH   E 5 .   ? -4.847  -7.165  11.412  1.00 34.94 ? 535 HOH   A O   1 
HETATM 2239 O  O   . HOH   E 5 .   ? 13.335  -17.100 30.544  1.00 32.94 ? 536 HOH   A O   1 
HETATM 2240 O  O   . HOH   E 5 .   ? -2.810  -16.211 6.497   1.00 38.28 ? 537 HOH   A O   1 
HETATM 2241 O  O   . HOH   E 5 .   ? 25.975  -2.922  20.934  1.00 17.23 ? 538 HOH   A O   1 
HETATM 2242 O  O   . HOH   E 5 .   ? 5.381   10.681  -2.295  1.00 30.23 ? 539 HOH   A O   1 
HETATM 2243 O  O   . HOH   E 5 .   ? 6.400   -16.731 18.807  1.00 18.76 ? 540 HOH   A O   1 
HETATM 2244 O  O   . HOH   E 5 .   ? 16.834  -6.584  31.164  1.00 21.60 ? 541 HOH   A O   1 
HETATM 2245 O  O   . HOH   E 5 .   ? 18.496  -6.848  29.137  1.00 16.24 ? 542 HOH   A O   1 
HETATM 2246 O  O   . HOH   E 5 .   ? 4.515   -14.377 -4.102  1.00 35.83 ? 543 HOH   A O   1 
HETATM 2247 O  O   . HOH   E 5 .   ? 22.530  -4.284  34.450  1.00 29.00 ? 544 HOH   A O   1 
HETATM 2248 O  O   . HOH   E 5 .   ? -5.398  -5.732  30.344  1.00 32.63 ? 545 HOH   A O   1 
HETATM 2249 O  O   . HOH   E 5 .   ? 17.626  -11.341 25.185  1.00 15.01 ? 546 HOH   A O   1 
HETATM 2250 O  O   . HOH   E 5 .   ? -5.859  -0.764  14.398  1.00 32.86 ? 547 HOH   A O   1 
HETATM 2251 O  O   . HOH   E 5 .   ? 34.931  3.776   22.790  1.00 35.91 ? 548 HOH   A O   1 
HETATM 2252 O  O   . HOH   E 5 .   ? 25.609  6.375   10.896  1.00 40.17 ? 549 HOH   A O   1 
HETATM 2253 O  O   . HOH   E 5 .   ? 21.269  -17.852 10.897  1.00 49.50 ? 550 HOH   A O   1 
HETATM 2254 O  O   . HOH   E 5 .   ? 1.750   11.850  8.874   1.00 16.63 ? 551 HOH   A O   1 
HETATM 2255 O  O   . HOH   E 5 .   ? 32.235  3.135   25.784  1.00 31.98 ? 552 HOH   A O   1 
HETATM 2256 O  O   . HOH   E 5 .   ? 23.816  2.914   -2.277  1.00 31.49 ? 553 HOH   A O   1 
HETATM 2257 O  O   . HOH   E 5 .   ? 13.637  -6.681  32.642  1.00 21.31 ? 554 HOH   A O   1 
HETATM 2258 O  O   . HOH   E 5 .   ? 13.877  -15.091 1.624   1.00 20.70 ? 555 HOH   A O   1 
HETATM 2259 O  O   . HOH   E 5 .   ? 7.635   -15.086 0.130   1.00 31.67 ? 556 HOH   A O   1 
HETATM 2260 O  O   . HOH   E 5 .   ? 8.912   4.653   30.960  1.00 19.69 ? 557 HOH   A O   1 
HETATM 2261 O  O   . HOH   E 5 .   ? 4.785   -8.101  32.960  1.00 20.84 ? 558 HOH   A O   1 
HETATM 2262 O  O   . HOH   E 5 .   ? 31.318  -6.995  8.447   1.00 28.35 ? 559 HOH   A O   1 
HETATM 2263 O  O   . HOH   E 5 .   ? 11.749  -8.220  -1.178  1.00 24.95 ? 560 HOH   A O   1 
HETATM 2264 O  O   . HOH   E 5 .   ? -3.630  13.847  6.338   1.00 31.95 ? 561 HOH   A O   1 
HETATM 2265 O  O   . HOH   E 5 .   ? -5.984  -2.110  24.953  1.00 23.63 ? 562 HOH   A O   1 
HETATM 2266 O  O   . HOH   E 5 .   ? -4.986  -4.509  33.629  1.00 43.05 ? 563 HOH   A O   1 
HETATM 2267 O  O   . HOH   E 5 .   ? 8.140   9.750   28.868  1.00 28.95 ? 564 HOH   A O   1 
HETATM 2268 O  O   . HOH   E 5 .   ? 34.135  -3.941  24.362  1.00 26.48 ? 565 HOH   A O   1 
HETATM 2269 O  O   . HOH   E 5 .   ? 7.507   0.855   -6.209  1.00 29.91 ? 566 HOH   A O   1 
HETATM 2270 O  O   . HOH   E 5 .   ? 22.202  10.730  24.428  1.00 19.48 ? 567 HOH   A O   1 
HETATM 2271 O  O   . HOH   E 5 .   ? -2.909  0.995   3.960   1.00 23.26 ? 568 HOH   A O   1 
HETATM 2272 O  O   . HOH   E 5 .   ? -2.978  1.701   1.255   1.00 35.16 ? 569 HOH   A O   1 
HETATM 2273 O  O   . HOH   E 5 .   ? -4.851  9.841   6.152   1.00 34.28 ? 570 HOH   A O   1 
HETATM 2274 O  O   . HOH   E 5 .   ? 12.766  -20.339 10.544  1.00 27.15 ? 571 HOH   A O   1 
HETATM 2275 O  O   . HOH   E 5 .   ? 22.274  0.392   29.446  1.00 17.96 ? 572 HOH   A O   1 
HETATM 2276 O  O   . HOH   E 5 .   ? 27.529  1.394   -1.455  1.00 37.96 ? 573 HOH   A O   1 
HETATM 2277 O  O   . HOH   E 5 .   ? -2.479  -11.327 11.331  1.00 22.88 ? 574 HOH   A O   1 
HETATM 2278 O  O   . HOH   E 5 .   ? 34.427  2.180   24.479  1.00 26.33 ? 575 HOH   A O   1 
HETATM 2279 O  O   . HOH   E 5 .   ? 29.840  -9.846  6.809   1.00 35.60 ? 576 HOH   A O   1 
HETATM 2280 O  O   . HOH   E 5 .   ? 13.940  -6.740  -7.139  1.00 35.79 ? 577 HOH   A O   1 
HETATM 2281 O  O   . HOH   E 5 .   ? 25.126  -4.850  7.803   1.00 26.17 ? 578 HOH   A O   1 
HETATM 2282 O  O   . HOH   E 5 .   ? 2.095   4.130   40.899  1.00 44.19 ? 579 HOH   A O   1 
HETATM 2283 O  O   . HOH   E 5 .   ? 4.372   16.427  33.400  1.00 31.79 ? 580 HOH   A O   1 
HETATM 2284 O  O   . HOH   E 5 .   ? -2.972  1.111   26.579  1.00 22.83 ? 581 HOH   A O   1 
HETATM 2285 O  O   . HOH   E 5 .   ? 12.513  -13.130 33.296  1.00 39.12 ? 582 HOH   A O   1 
HETATM 2286 O  O   . HOH   E 5 .   ? -3.902  6.533   8.205   1.00 33.53 ? 583 HOH   A O   1 
HETATM 2287 O  O   . HOH   E 5 .   ? 10.425  22.772  24.953  1.00 23.92 ? 584 HOH   A O   1 
HETATM 2288 O  O   . HOH   E 5 .   ? 9.836   3.168   33.576  1.00 27.80 ? 585 HOH   A O   1 
HETATM 2289 O  O   . HOH   E 5 .   ? -1.216  -16.573 13.614  1.00 24.35 ? 586 HOH   A O   1 
HETATM 2290 O  O   . HOH   E 5 .   ? 2.290   22.093  14.889  1.00 29.97 ? 587 HOH   A O   1 
HETATM 2291 O  O   . HOH   E 5 .   ? 20.208  4.602   1.903   1.00 26.72 ? 588 HOH   A O   1 
HETATM 2292 O  O   . HOH   E 5 .   ? 26.907  2.542   8.292   1.00 30.33 ? 589 HOH   A O   1 
HETATM 2293 O  O   . HOH   E 5 .   ? 6.109   7.833   32.750  1.00 36.56 ? 590 HOH   A O   1 
HETATM 2294 O  O   . HOH   E 5 .   ? 17.458  5.848   8.883   1.00 23.23 ? 591 HOH   A O   1 
HETATM 2295 O  O   . HOH   E 5 .   ? -2.357  -9.574  16.979  1.00 42.78 ? 592 HOH   A O   1 
HETATM 2296 O  O   . HOH   E 5 .   ? 30.634  3.709   11.873  1.00 53.85 ? 593 HOH   A O   1 
HETATM 2297 O  O   . HOH   E 5 .   ? 16.389  -14.216 0.782   1.00 26.56 ? 594 HOH   A O   1 
HETATM 2298 O  O   . HOH   E 5 .   ? 26.595  -11.093 11.138  1.00 44.89 ? 595 HOH   A O   1 
HETATM 2299 O  O   . HOH   E 5 .   ? 19.874  6.105   -4.866  1.00 34.34 ? 596 HOH   A O   1 
HETATM 2300 O  O   . HOH   E 5 .   ? 14.628  -17.548 5.882   1.00 29.09 ? 597 HOH   A O   1 
HETATM 2301 O  O   . HOH   E 5 .   ? -2.021  -9.869  14.194  1.00 21.63 ? 598 HOH   A O   1 
HETATM 2302 O  O   . HOH   E 5 .   ? 32.331  -2.264  7.515   1.00 38.37 ? 599 HOH   A O   1 
HETATM 2303 O  O   . HOH   E 5 .   ? 12.869  -17.478 21.778  1.00 20.87 ? 600 HOH   A O   1 
HETATM 2304 O  O   . HOH   E 5 .   ? -2.068  -12.803 16.276  1.00 42.64 ? 601 HOH   A O   1 
HETATM 2305 O  O   . HOH   E 5 .   ? 4.914   -8.079  38.629  1.00 38.55 ? 602 HOH   A O   1 
HETATM 2306 O  O   . HOH   E 5 .   ? 27.804  -5.834  -10.654 1.00 37.15 ? 603 HOH   A O   1 
HETATM 2307 O  O   . HOH   E 5 .   ? 15.268  17.327  11.938  1.00 31.60 ? 604 HOH   A O   1 
HETATM 2308 O  O   . HOH   E 5 .   ? -7.148  7.397   18.968  1.00 34.67 ? 605 HOH   A O   1 
HETATM 2309 O  O   . HOH   E 5 .   ? 11.882  -3.898  36.006  1.00 22.90 ? 606 HOH   A O   1 
HETATM 2310 O  O   . HOH   E 5 .   ? 23.923  -12.783 1.034   1.00 22.85 ? 607 HOH   A O   1 
HETATM 2311 O  O   . HOH   E 5 .   ? 18.928  -10.370 22.855  1.00 15.55 ? 608 HOH   A O   1 
HETATM 2312 O  O   . HOH   E 5 .   ? 25.920  -11.340 -5.634  1.00 20.44 ? 609 HOH   A O   1 
HETATM 2313 O  O   . HOH   E 5 .   ? 12.528  -17.980 26.683  1.00 28.70 ? 610 HOH   A O   1 
HETATM 2314 O  O   . HOH   E 5 .   ? 13.808  3.503   35.284  1.00 29.96 ? 611 HOH   A O   1 
HETATM 2315 O  O   . HOH   E 5 .   ? -2.803  1.613   31.715  1.00 36.26 ? 612 HOH   A O   1 
HETATM 2316 O  O   . HOH   E 5 .   ? 21.367  2.438   -6.808  1.00 27.69 ? 613 HOH   A O   1 
HETATM 2317 O  O   . HOH   E 5 .   ? 10.064  19.591  12.253  1.00 27.77 ? 614 HOH   A O   1 
HETATM 2318 O  O   . HOH   E 5 .   ? 20.760  -12.429 22.234  1.00 24.25 ? 615 HOH   A O   1 
HETATM 2319 O  O   . HOH   E 5 .   ? -4.381  -8.013  15.331  1.00 43.96 ? 616 HOH   A O   1 
HETATM 2320 O  O   . HOH   E 5 .   ? 14.597  -17.921 23.994  1.00 31.46 ? 617 HOH   A O   1 
HETATM 2321 O  O   . HOH   E 5 .   ? 20.445  -6.675  32.541  1.00 27.32 ? 618 HOH   A O   1 
HETATM 2322 O  O   . HOH   E 5 .   ? 8.339   5.216   -7.001  1.00 28.48 ? 619 HOH   A O   1 
HETATM 2323 O  O   . HOH   E 5 .   ? 11.437  -6.078  34.156  1.00 25.15 ? 620 HOH   A O   1 
HETATM 2324 O  O   . HOH   E 5 .   ? 15.614  5.278   -5.835  1.00 30.54 ? 621 HOH   A O   1 
HETATM 2325 O  O   . HOH   E 5 .   ? 23.822  -2.577  7.463   1.00 36.99 ? 622 HOH   A O   1 
HETATM 2326 O  O   . HOH   E 5 .   ? 2.345   -19.613 5.675   1.00 41.26 ? 623 HOH   A O   1 
HETATM 2327 O  O   . HOH   E 5 .   ? -3.747  -7.695  1.996   1.00 34.32 ? 624 HOH   A O   1 
HETATM 2328 O  O   . HOH   E 5 .   ? 26.196  -5.152  22.484  1.00 32.19 ? 625 HOH   A O   1 
HETATM 2329 O  O   . HOH   E 5 .   ? 11.256  16.920  12.099  1.00 28.26 ? 626 HOH   A O   1 
HETATM 2330 O  O   . HOH   E 5 .   ? 2.328   5.268   -3.597  1.00 31.66 ? 627 HOH   A O   1 
HETATM 2331 O  O   . HOH   E 5 .   ? 13.683  -6.876  -2.338  1.00 26.95 ? 628 HOH   A O   1 
HETATM 2332 O  O   . HOH   E 5 .   ? 3.954   1.078   40.128  1.00 38.97 ? 629 HOH   A O   1 
HETATM 2333 O  O   . HOH   E 5 .   ? 11.677  15.461  10.097  1.00 48.16 ? 630 HOH   A O   1 
HETATM 2334 O  O   . HOH   E 5 .   ? 28.623  8.004   21.573  1.00 17.83 ? 631 HOH   A O   1 
HETATM 2335 O  O   . HOH   E 5 .   ? 27.445  -4.282  6.638   1.00 35.32 ? 632 HOH   A O   1 
HETATM 2336 O  O   . HOH   E 5 .   ? 29.426  -6.986  -7.847  1.00 41.47 ? 633 HOH   A O   1 
HETATM 2337 O  O   . HOH   E 5 .   ? -6.773  6.217   23.841  1.00 32.91 ? 634 HOH   A O   1 
HETATM 2338 O  O   . HOH   E 5 .   ? -10.676 7.132   12.884  1.00 40.36 ? 635 HOH   A O   1 
HETATM 2339 O  O   . HOH   E 5 .   ? 31.329  1.120   14.461  1.00 42.69 ? 636 HOH   A O   1 
HETATM 2340 O  O   . HOH   E 5 .   ? 14.265  16.751  29.113  1.00 38.77 ? 637 HOH   A O   1 
HETATM 2341 O  O   . HOH   E 5 .   ? -4.355  12.932  19.346  1.00 35.70 ? 638 HOH   A O   1 
HETATM 2342 O  O   . HOH   E 5 .   ? 25.492  -9.092  -7.137  1.00 37.71 ? 639 HOH   A O   1 
HETATM 2343 O  O   . HOH   E 5 .   ? 11.066  7.861   -4.606  1.00 38.86 ? 640 HOH   A O   1 
HETATM 2344 O  O   . HOH   E 5 .   ? -0.276  -17.941 6.557   1.00 34.64 ? 641 HOH   A O   1 
HETATM 2345 O  O   . HOH   E 5 .   ? 27.811  -11.478 7.133   1.00 40.16 ? 642 HOH   A O   1 
HETATM 2346 O  O   . HOH   E 5 .   ? 19.433  13.306  25.841  1.00 32.23 ? 643 HOH   A O   1 
HETATM 2347 O  O   . HOH   E 5 .   ? 20.116  -1.374  39.527  1.00 48.72 ? 644 HOH   A O   1 
HETATM 2348 O  O   . HOH   E 5 .   ? 15.455  -10.609 -5.337  1.00 39.06 ? 645 HOH   A O   1 
HETATM 2349 O  O   . HOH   E 5 .   ? 31.712  -0.824  13.204  1.00 42.59 ? 646 HOH   A O   1 
HETATM 2350 O  O   . HOH   E 5 .   ? 8.161   -15.355 17.035  1.00 16.12 ? 647 HOH   A O   1 
HETATM 2351 O  O   . HOH   E 5 .   ? 29.713  -2.781  23.784  1.00 31.36 ? 648 HOH   A O   1 
HETATM 2352 O  O   . HOH   E 5 .   ? 4.643   -11.362 38.776  1.00 62.82 ? 649 HOH   A O   1 
HETATM 2353 O  O   . HOH   E 5 .   ? 18.198  19.900  14.480  1.00 41.97 ? 650 HOH   A O   1 
HETATM 2354 O  O   . HOH   E 5 .   ? 16.318  9.316   -3.307  1.00 39.37 ? 651 HOH   A O   1 
HETATM 2355 O  O   . HOH   E 5 .   ? 26.231  -8.704  18.802  1.00 35.10 ? 652 HOH   A O   1 
HETATM 2356 O  O   . HOH   E 5 .   ? 23.065  -0.679  37.545  1.00 46.85 ? 653 HOH   A O   1 
HETATM 2357 O  O   . HOH   E 5 .   ? -1.676  -7.723  25.400  1.00 23.79 ? 654 HOH   A O   1 
HETATM 2358 O  O   . HOH   E 5 .   ? 5.789   -14.410 25.524  1.00 33.89 ? 655 HOH   A O   1 
HETATM 2359 O  O   . HOH   E 5 .   ? 3.852   -2.513  -5.054  1.00 36.66 ? 656 HOH   A O   1 
HETATM 2360 O  O   . HOH   E 5 .   ? 3.142   -7.024  34.951  1.00 43.87 ? 657 HOH   A O   1 
HETATM 2361 O  O   . HOH   E 5 .   ? 29.052  -6.631  6.332   1.00 43.65 ? 658 HOH   A O   1 
HETATM 2362 O  O   . HOH   E 5 .   ? -0.849  -19.886 11.984  1.00 48.07 ? 659 HOH   A O   1 
HETATM 2363 O  O   . HOH   E 5 .   ? -2.773  -1.524  4.019   1.00 36.53 ? 660 HOH   A O   1 
HETATM 2364 O  O   . HOH   E 5 .   ? 3.273   21.917  17.522  1.00 30.39 ? 661 HOH   A O   1 
HETATM 2365 O  O   . HOH   E 5 .   ? 30.335  -7.974  0.227   1.00 42.55 ? 662 HOH   A O   1 
HETATM 2366 O  O   . HOH   E 5 .   ? -5.466  -5.865  2.406   1.00 47.95 ? 663 HOH   A O   1 
HETATM 2367 O  O   . HOH   E 5 .   ? 8.469   8.548   31.351  1.00 34.39 ? 664 HOH   A O   1 
HETATM 2368 O  O   . HOH   E 5 .   ? 16.732  -4.099  -8.074  1.00 44.90 ? 665 HOH   A O   1 
HETATM 2369 O  O   . HOH   E 5 .   ? -5.556  -4.418  4.626   1.00 39.47 ? 666 HOH   A O   1 
HETATM 2370 O  O   . HOH   E 5 .   ? -6.720  -1.211  9.318   1.00 46.91 ? 667 HOH   A O   1 
HETATM 2371 O  O   . HOH   E 5 .   ? 24.103  4.535   8.136   1.00 41.67 ? 668 HOH   A O   1 
HETATM 2372 O  O   . HOH   E 5 .   ? 13.799  18.865  10.547  1.00 32.86 ? 669 HOH   A O   1 
HETATM 2373 O  O   . HOH   E 5 .   ? 12.214  -2.320  -9.462  1.00 44.07 ? 670 HOH   A O   1 
HETATM 2374 O  O   . HOH   E 5 .   ? 4.055   -16.292 20.282  1.00 26.90 ? 671 HOH   A O   1 
HETATM 2375 O  O   . HOH   E 5 .   ? 3.077   -9.981  31.663  1.00 33.25 ? 672 HOH   A O   1 
HETATM 2376 O  O   . HOH   E 5 .   ? 32.899  -4.802  7.785   1.00 35.36 ? 673 HOH   A O   1 
HETATM 2377 O  O   . HOH   E 5 .   ? 25.608  1.696   5.286   1.00 38.97 ? 674 HOH   A O   1 
HETATM 2378 O  O   . HOH   E 5 .   ? 19.523  4.367   9.649   1.00 46.36 ? 675 HOH   A O   1 
HETATM 2379 O  O   . HOH   E 5 .   ? 10.976  -10.672 40.125  1.00 42.35 ? 676 HOH   A O   1 
HETATM 2380 O  O   . HOH   E 5 .   ? 26.689  -12.458 8.930   1.00 41.72 ? 677 HOH   A O   1 
HETATM 2381 O  O   . HOH   E 5 .   ? 6.934   5.559   33.311  1.00 30.90 ? 678 HOH   A O   1 
HETATM 2382 O  O   . HOH   E 5 .   ? 4.434   -15.839 24.186  1.00 35.76 ? 679 HOH   A O   1 
HETATM 2383 O  O   . HOH   E 5 .   ? 10.417  6.837   30.967  1.00 28.37 ? 680 HOH   A O   1 
HETATM 2384 O  O   . HOH   E 5 .   ? 19.687  -11.151 27.072  1.00 26.37 ? 681 HOH   A O   1 
HETATM 2385 O  O   . HOH   E 5 .   ? 4.915   18.623  26.663  1.00 41.37 ? 682 HOH   A O   1 
HETATM 2386 O  O   . HOH   E 5 .   ? -0.071  -18.605 14.897  1.00 41.94 ? 683 HOH   A O   1 
HETATM 2387 O  O   . HOH   E 5 .   ? 23.886  -11.864 8.190   1.00 29.10 ? 684 HOH   A O   1 
HETATM 2388 O  O   . HOH   E 5 .   ? 18.026  16.911  11.667  1.00 33.62 ? 685 HOH   A O   1 
HETATM 2389 O  O   . HOH   E 5 .   ? 15.530  8.914   10.399  1.00 25.98 ? 686 HOH   A O   1 
HETATM 2390 O  O   . HOH   E 5 .   ? 3.657   7.721   34.756  1.00 40.34 ? 687 HOH   A O   1 
HETATM 2391 O  O   . HOH   E 5 .   ? 19.142  -15.519 25.638  1.00 31.52 ? 688 HOH   A O   1 
HETATM 2392 O  O   . HOH   E 5 .   ? 27.818  -3.482  31.952  1.00 39.48 ? 689 HOH   A O   1 
HETATM 2393 O  O   . HOH   E 5 .   ? 19.532  -15.953 -2.059  1.00 38.78 ? 690 HOH   A O   1 
HETATM 2394 O  O   . HOH   E 5 .   ? 11.534  5.028   34.851  1.00 28.36 ? 691 HOH   A O   1 
HETATM 2395 O  O   . HOH   E 5 .   ? 27.586  -3.142  27.442  1.00 41.16 ? 692 HOH   A O   1 
HETATM 2396 O  O   . HOH   E 5 .   ? 10.083  -9.403  -2.788  1.00 40.29 ? 693 HOH   A O   1 
HETATM 2397 O  O   . HOH   E 5 .   ? -1.363  -10.393 24.861  1.00 35.57 ? 694 HOH   A O   1 
HETATM 2398 O  O   . HOH   E 5 .   ? 11.556  -20.253 7.307   1.00 45.73 ? 695 HOH   A O   1 
HETATM 2399 O  O   . HOH   E 5 .   ? 15.962  22.476  21.497  1.00 26.80 ? 696 HOH   A O   1 
HETATM 2400 O  O   . HOH   E 5 .   ? 17.839  1.655   -12.079 1.00 41.21 ? 697 HOH   A O   1 
HETATM 2401 O  O   . HOH   E 5 .   ? 5.939   23.178  23.344  1.00 31.78 ? 698 HOH   A O   1 
HETATM 2402 O  O   . HOH   E 5 .   ? 4.131   -11.964 26.466  1.00 24.21 ? 699 HOH   A O   1 
HETATM 2403 O  O   . HOH   E 5 .   ? 0.849   -0.279  42.942  1.00 37.83 ? 700 HOH   A O   1 
HETATM 2404 O  O   . HOH   E 5 .   ? 14.907  22.186  26.391  1.00 38.37 ? 701 HOH   A O   1 
HETATM 2405 O  O   . HOH   E 5 .   ? 22.744  14.326  22.697  1.00 28.35 ? 702 HOH   A O   1 
HETATM 2406 O  O   . HOH   E 5 .   ? -2.916  -5.416  0.208   1.00 39.68 ? 703 HOH   A O   1 
HETATM 2407 O  O   . HOH   E 5 .   ? 18.792  -9.776  31.719  1.00 30.59 ? 704 HOH   A O   1 
HETATM 2408 O  O   . HOH   E 5 .   ? 18.471  7.478   6.421   1.00 29.98 ? 705 HOH   A O   1 
HETATM 2409 O  O   . HOH   E 5 .   ? 22.824  -7.767  31.300  1.00 44.60 ? 706 HOH   A O   1 
HETATM 2410 O  O   . HOH   E 5 .   ? 36.475  0.664   26.030  1.00 33.66 ? 707 HOH   A O   1 
HETATM 2411 O  O   . HOH   E 5 .   ? 9.758   2.870   -7.786  1.00 41.34 ? 708 HOH   A O   1 
HETATM 2412 O  O   . HOH   E 5 .   ? 20.606  -4.987  -8.030  1.00 35.77 ? 709 HOH   A O   1 
HETATM 2413 O  O   . HOH   E 5 .   ? 29.603  -10.007 3.333   1.00 43.34 ? 710 HOH   A O   1 
HETATM 2414 O  O   . HOH   E 5 .   ? 15.953  -7.817  33.877  1.00 38.50 ? 711 HOH   A O   1 
HETATM 2415 O  O   . HOH   E 5 .   ? 13.741  -8.302  -4.492  1.00 33.88 ? 712 HOH   A O   1 
HETATM 2416 O  O   . HOH   E 5 .   ? 22.447  -15.842 7.093   1.00 38.27 ? 713 HOH   A O   1 
HETATM 2417 O  O   . HOH   E 5 .   ? 33.477  5.990   27.246  1.00 33.78 ? 714 HOH   A O   1 
HETATM 2418 O  O   . HOH   E 5 .   ? 8.111   23.655  26.122  1.00 27.58 ? 715 HOH   A O   1 
HETATM 2419 O  O   . HOH   E 5 .   ? 24.196  8.477   32.118  1.00 41.64 ? 716 HOH   A O   1 
HETATM 2420 O  O   . HOH   E 5 .   ? 0.728   -3.034  -3.679  1.00 43.00 ? 717 HOH   A O   1 
HETATM 2421 O  O   . HOH   E 5 .   ? 12.968  9.421   8.086   1.00 20.68 ? 718 HOH   A O   1 
HETATM 2422 O  O   . HOH   E 5 .   ? 24.706  4.439   -0.094  1.00 36.36 ? 719 HOH   A O   1 
HETATM 2423 O  O   . HOH   E 5 .   ? 4.630   -13.109 28.837  1.00 39.02 ? 720 HOH   A O   1 
HETATM 2424 O  O   . HOH   E 5 .   ? 23.044  -12.232 20.493  1.00 30.98 ? 721 HOH   A O   1 
HETATM 2425 O  O   . HOH   E 5 .   ? 19.846  -9.192  29.077  1.00 21.40 ? 722 HOH   A O   1 
HETATM 2426 O  O   . HOH   E 5 .   ? 23.852  9.766   12.642  1.00 45.88 ? 723 HOH   A O   1 
HETATM 2427 O  O   . HOH   E 5 .   ? 23.488  14.752  20.172  1.00 34.24 ? 724 HOH   A O   1 
HETATM 2428 O  O   . HOH   E 5 .   ? 22.914  5.090   -4.804  1.00 39.57 ? 725 HOH   A O   1 
HETATM 2429 O  O   . HOH   E 5 .   ? -7.380  7.392   26.009  1.00 39.01 ? 726 HOH   A O   1 
HETATM 2430 O  O   . HOH   E 5 .   ? 1.414   -13.166 26.084  1.00 34.31 ? 727 HOH   A O   1 
HETATM 2431 O  O   . HOH   E 5 .   ? -6.717  1.679   14.864  1.00 59.70 ? 728 HOH   A O   1 
HETATM 2432 O  O   . HOH   E 5 .   ? 4.633   9.338   36.543  1.00 28.87 ? 729 HOH   A O   1 
HETATM 2433 O  O   . HOH   E 5 .   ? 18.516  24.029  21.346  1.00 35.54 ? 730 HOH   A O   1 
HETATM 2434 O  O   . HOH   E 5 .   ? 33.984  -7.831  5.275   1.00 40.84 ? 731 HOH   A O   1 
HETATM 2435 O  O   . HOH   E 5 .   ? 23.882  3.169   -6.286  1.00 33.21 ? 732 HOH   A O   1 
HETATM 2436 O  O   . HOH   E 5 .   ? 27.470  7.378   28.621  1.00 40.13 ? 733 HOH   A O   1 
HETATM 2437 O  O   . HOH   E 5 .   ? 16.670  -13.745 -2.407  1.00 33.34 ? 734 HOH   A O   1 
HETATM 2438 O  O   . HOH   E 5 .   ? 25.205  -9.632  23.247  1.00 42.85 ? 735 HOH   A O   1 
HETATM 2439 O  O   . HOH   E 5 .   ? 18.511  -7.191  34.523  1.00 42.41 ? 736 HOH   A O   1 
HETATM 2440 O  O   . HOH   E 5 .   ? -8.219  -2.147  13.405  1.00 41.07 ? 737 HOH   A O   1 
HETATM 2441 O  O   . HOH   E 5 .   ? 27.619  10.465  18.135  1.00 41.53 ? 738 HOH   A O   1 
HETATM 2442 O  O   . HOH   E 5 .   ? 1.038   -13.679 22.653  1.00 31.31 ? 739 HOH   A O   1 
HETATM 2443 O  O   . HOH   E 5 .   ? 20.607  13.951  14.368  1.00 30.29 ? 740 HOH   A O   1 
HETATM 2444 O  O   . HOH   E 5 .   ? 15.382  -16.391 3.567   1.00 34.08 ? 741 HOH   A O   1 
HETATM 2445 O  O   . HOH   E 5 .   ? -7.410  -6.091  6.669   1.00 36.28 ? 742 HOH   A O   1 
HETATM 2446 O  O   . HOH   E 5 .   ? 26.449  11.062  21.837  1.00 29.14 ? 743 HOH   A O   1 
HETATM 2447 O  O   . HOH   E 5 .   ? 35.306  0.584   28.307  1.00 41.08 ? 744 HOH   A O   1 
HETATM 2448 O  O   . HOH   E 5 .   ? 33.051  -5.734  -5.070  1.00 33.69 ? 745 HOH   A O   1 
HETATM 2449 O  O   . HOH   E 5 .   ? 22.777  12.210  15.117  1.00 49.30 ? 746 HOH   A O   1 
HETATM 2450 O  O   . HOH   E 5 .   ? 24.798  11.740  23.889  1.00 31.40 ? 747 HOH   A O   1 
HETATM 2451 O  O   . HOH   E 5 .   ? 14.406  11.898  8.033   1.00 30.41 ? 748 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS   A 4   ? 0.3295 0.5133 0.3595 -0.0936 -0.0615 0.1833  4   HIS   A N   
2    C  CA  . HIS   A 4   ? 0.4444 0.3395 0.4479 -0.1060 -0.0556 0.1881  4   HIS   A CA  
3    C  C   . HIS   A 4   ? 0.2771 0.2951 0.4080 -0.0385 0.0908  0.0427  4   HIS   A C   
4    O  O   . HIS   A 4   ? 0.3422 0.3049 0.3889 0.0407  0.0330  -0.0114 4   HIS   A O   
5    C  CB  . HIS   A 4   ? 0.4189 0.5353 0.5425 -0.1758 -0.0549 0.2029  4   HIS   A CB  
6    C  CG  . HIS   A 4   ? 0.2977 0.8165 0.4301 -0.1840 -0.1569 0.0583  4   HIS   A CG  
7    N  ND1 . HIS   A 4   ? 0.4289 0.7683 0.4159 0.0332  -0.0868 0.0161  4   HIS   A ND1 
8    C  CD2 . HIS   A 4   ? 0.6136 0.6686 0.5562 -0.0550 0.0266  0.0342  4   HIS   A CD2 
9    C  CE1 . HIS   A 4   ? 0.1582 1.0362 0.4554 -0.0177 0.0047  0.1771  4   HIS   A CE1 
10   N  NE2 . HIS   A 4   ? 0.5782 1.0858 0.6066 0.0605  0.0258  0.0823  4   HIS   A NE2 
11   N  N   . TRP   A 5   ? 0.1956 0.3297 0.3998 -0.0380 0.0788  0.0425  5   TRP   A N   
12   C  CA  . TRP   A 5   ? 0.1039 0.2518 0.3068 -0.0390 0.0067  0.0066  5   TRP   A CA  
13   C  C   . TRP   A 5   ? 0.1536 0.1720 0.3368 -0.0021 -0.0221 -0.0050 5   TRP   A C   
14   O  O   . TRP   A 5   ? 0.2311 0.2020 0.3417 -0.0129 0.0000  0.0155  5   TRP   A O   
15   C  CB  . TRP   A 5   ? 0.2009 0.1975 0.3189 -0.0239 -0.0068 -0.0075 5   TRP   A CB  
16   C  CG  . TRP   A 5   ? 0.2206 0.1748 0.3151 -0.0208 0.0015  0.0100  5   TRP   A CG  
17   C  CD1 . TRP   A 5   ? 0.2676 0.1655 0.2966 0.0214  -0.0176 -0.0012 5   TRP   A CD1 
18   C  CD2 . TRP   A 5   ? 0.2363 0.1806 0.3128 -0.0465 -0.0232 -0.0187 5   TRP   A CD2 
19   N  NE1 . TRP   A 5   ? 0.3013 0.1668 0.3114 0.0062  -0.0100 0.0392  5   TRP   A NE1 
20   C  CE2 . TRP   A 5   ? 0.2023 0.2531 0.2460 -0.0173 -0.0248 0.0106  5   TRP   A CE2 
21   C  CE3 . TRP   A 5   ? 0.2042 0.1770 0.2789 -0.0473 0.0000  -0.0367 5   TRP   A CE3 
22   C  CZ2 . TRP   A 5   ? 0.1955 0.2365 0.2944 0.0093  -0.0044 -0.0251 5   TRP   A CZ2 
23   C  CZ3 . TRP   A 5   ? 0.2075 0.2588 0.2946 0.0255  -0.0031 -0.0132 5   TRP   A CZ3 
24   C  CH2 . TRP   A 5   ? 0.2045 0.2194 0.3096 -0.0008 -0.0653 -0.0607 5   TRP   A CH2 
25   N  N   . GLY   A 6   ? 0.1858 0.1389 0.2834 0.0066  -0.0107 -0.0210 6   GLY   A N   
26   C  CA  . GLY   A 6   ? 0.1472 0.1673 0.3392 0.0037  -0.0209 0.0116  6   GLY   A CA  
27   C  C   . GLY   A 6   ? 0.0869 0.1849 0.2732 0.0077  0.0065  0.0013  6   GLY   A C   
28   O  O   . GLY   A 6   ? 0.1205 0.1755 0.2868 0.0122  -0.0196 0.0241  6   GLY   A O   
29   N  N   . TYR   A 7   ? 0.2020 0.1791 0.3950 -0.0183 0.0097  -0.0223 7   TYR   A N   
30   C  CA  . TYR   A 7   ? 0.1206 0.1874 0.4248 0.0172  0.0342  0.0050  7   TYR   A CA  
31   C  C   . TYR   A 7   ? 0.2413 0.2073 0.6044 0.0158  0.1428  -0.0208 7   TYR   A C   
32   O  O   . TYR   A 7   ? 0.2599 0.2068 0.7572 0.0203  0.0523  -0.0255 7   TYR   A O   
33   C  CB  . TYR   A 7   ? 0.1253 0.1773 0.4218 0.0060  0.0350  -0.0649 7   TYR   A CB  
34   C  CG  . TYR   A 7   ? 0.0907 0.1723 0.2866 -0.0019 -0.0119 -0.0428 7   TYR   A CG  
35   C  CD1 . TYR   A 7   ? 0.1242 0.1694 0.2724 0.0029  -0.0002 -0.0425 7   TYR   A CD1 
36   C  CD2 . TYR   A 7   ? 0.0888 0.2262 0.2866 -0.0114 -0.0225 -0.0941 7   TYR   A CD2 
37   C  CE1 . TYR   A 7   ? 0.1298 0.1720 0.2621 -0.0087 0.0025  -0.0370 7   TYR   A CE1 
38   C  CE2 . TYR   A 7   ? 0.0968 0.1862 0.2776 -0.0170 -0.0488 -0.0325 7   TYR   A CE2 
39   C  CZ  . TYR   A 7   ? 0.0994 0.1880 0.2440 0.0084  -0.0239 -0.0530 7   TYR   A CZ  
40   O  OH  . TYR   A 7   ? 0.1062 0.1429 0.2938 -0.0036 -0.0117 -0.0240 7   TYR   A OH  
41   N  N   . GLY   A 8   ? 0.1144 0.2412 0.5382 0.0142  0.0203  -0.0596 8   GLY   A N   
42   C  CA  . GLY   A 8   ? 0.1597 0.2825 0.5327 0.0911  0.0092  0.0027  8   GLY   A CA  
43   C  C   . GLY   A 8   ? 0.1678 0.3325 0.4143 0.0272  -0.0038 0.0341  8   GLY   A C   
44   O  O   . GLY   A 8   ? 0.2809 0.2758 0.4355 0.0517  0.1181  -0.0172 8   GLY   A O   
45   N  N   . LYS   A 9   ? 0.2804 0.2887 0.4205 0.0883  -0.0423 -0.0048 9   LYS   A N   
46   C  CA  . LYS   A 9   ? 0.2558 0.3126 0.4885 0.0017  -0.1146 0.0406  9   LYS   A CA  
47   C  C   . LYS   A 9   ? 0.3583 0.1863 0.3633 -0.0049 -0.0686 0.0160  9   LYS   A C   
48   O  O   . LYS   A 9   ? 0.2965 0.4936 0.3294 0.0232  -0.0731 0.0642  9   LYS   A O   
49   C  CB  . LYS   A 9   ? 0.3514 0.4046 0.5333 0.0032  -0.0548 -0.0725 9   LYS   A CB  
50   C  CG  . LYS   A 9   ? 0.5790 0.5529 0.4727 -0.1443 -0.0653 -0.2304 9   LYS   A CG  
51   C  CD  . LYS   A 9   ? 0.5290 0.4896 0.7531 -0.0407 -0.2314 -0.2075 9   LYS   A CD  
52   C  CE  . LYS   A 9   ? 0.6741 0.4156 0.6529 0.0283  -0.3039 -0.2371 9   LYS   A CE  
53   N  NZ  . LYS   A 9   ? 0.7156 0.4468 0.5921 -0.1038 -0.1452 -0.1526 9   LYS   A NZ  
54   N  N   . HIS   A 10  ? 0.1817 0.1738 0.4441 0.0041  -0.0228 0.0229  10  HIS   A N   
55   C  CA  . HIS   A 10  ? 0.1231 0.2204 0.3934 0.0472  0.0096  -0.0274 10  HIS   A CA  
56   C  C   . HIS   A 10  ? 0.1571 0.1967 0.3899 0.0718  0.0309  0.0384  10  HIS   A C   
57   O  O   . HIS   A 10  ? 0.1464 0.3805 0.4152 0.0267  0.0190  -0.0193 10  HIS   A O   
58   C  CB  . HIS   A 10  ? 0.1831 0.3128 0.3858 0.0320  0.0582  -0.0824 10  HIS   A CB  
59   C  CG  . HIS   A 10  ? 0.2398 0.3334 0.4356 0.0370  0.1088  -0.0793 10  HIS   A CG  
60   N  ND1 . HIS   A 10  ? 0.3619 0.3402 0.4622 0.0583  0.0730  0.0281  10  HIS   A ND1 
61   C  CD2 . HIS   A 10  ? 0.3025 0.3262 0.5159 0.0128  0.0944  -0.1198 10  HIS   A CD2 
62   C  CE1 . HIS   A 10  ? 0.2564 0.2929 0.4496 -0.0387 0.0937  0.0329  10  HIS   A CE1 
63   N  NE2 . HIS   A 10  ? 0.3015 0.3656 0.4915 0.0250  0.0660  -0.0480 10  HIS   A NE2 
64   N  N   . ASN   A 11  ? 0.1427 0.2177 0.3437 0.0465  0.0384  0.0309  11  ASN   A N   
65   C  CA  . ASN   A 11  ? 0.1772 0.2230 0.3116 0.0295  0.0508  0.0091  11  ASN   A CA  
66   C  C   . ASN   A 11  ? 0.1833 0.2179 0.2719 0.0077  0.0401  -0.0199 11  ASN   A C   
67   O  O   . ASN   A 11  ? 0.1632 0.2579 0.3291 0.0347  0.0359  0.0389  11  ASN   A O   
68   C  CB  . ASN   A 11  ? 0.1680 0.2018 0.3029 0.0281  0.0027  0.0150  11  ASN   A CB  
69   C  CG  . ASN   A 11  ? 0.1188 0.2990 0.3399 0.0291  0.0072  0.0441  11  ASN   A CG  
70   O  OD1 . ASN   A 11  ? 0.1313 0.2780 0.3838 0.0111  -0.0241 0.0013  11  ASN   A OD1 
71   N  ND2 . ASN   A 11  ? 0.1964 0.2669 0.3468 0.0093  -0.0696 -0.0002 11  ASN   A ND2 
72   N  N   . GLY   A 12  ? 0.1456 0.2846 0.2977 -0.0237 0.0245  0.0136  12  GLY   A N   
73   C  CA  . GLY   A 12  ? 0.1004 0.2480 0.3079 -0.0300 -0.0082 -0.0133 12  GLY   A CA  
74   C  C   . GLY   A 12  ? 0.1285 0.2647 0.3154 0.0154  0.0021  -0.0139 12  GLY   A C   
75   O  O   . GLY   A 12  ? 0.1253 0.1858 0.3097 0.0151  0.0129  0.0276  12  GLY   A O   
76   N  N   . PRO   A 13  ? 0.0996 0.1781 0.2655 0.0192  -0.0383 0.0009  13  PRO   A N   
77   C  CA  . PRO   A 13  ? 0.1321 0.2337 0.2938 -0.0353 0.0152  -0.0043 13  PRO   A CA  
78   C  C   . PRO   A 13  ? 0.1585 0.1560 0.2779 -0.0109 0.0152  0.0152  13  PRO   A C   
79   O  O   . PRO   A 13  ? 0.1481 0.2296 0.2907 0.0245  -0.0013 0.0032  13  PRO   A O   
80   C  CB  . PRO   A 13  ? 0.1242 0.2447 0.3017 -0.0616 0.0059  -0.0250 13  PRO   A CB  
81   C  CG  . PRO   A 13  ? 0.2235 0.1632 0.2778 0.0204  -0.0151 -0.0354 13  PRO   A CG  
82   C  CD  . PRO   A 13  ? 0.1392 0.1964 0.2894 -0.0227 -0.0284 0.0091  13  PRO   A CD  
83   N  N   . GLU   A 14  ? 0.1891 0.1741 0.2605 0.0159  -0.0044 0.0362  14  GLU   A N   
84   C  CA  . GLU   A 14  ? 0.1920 0.1593 0.2996 0.0266  -0.0237 0.0356  14  GLU   A CA  
85   C  C   . GLU   A 14  ? 0.1648 0.1360 0.2547 0.0613  -0.0196 0.0162  14  GLU   A C   
86   O  O   . GLU   A 14  ? 0.1806 0.1842 0.3058 0.0719  -0.0569 0.0143  14  GLU   A O   
87   C  CB  . GLU   A 14  ? 0.2337 0.2152 0.3514 0.1028  -0.0498 0.0212  14  GLU   A CB  
88   C  CG  . GLU   A 14  ? 0.3147 0.2613 0.2876 0.0119  -0.0597 0.0274  14  GLU   A CG  
89   C  CD  . GLU   A 14  ? 0.2910 0.2575 0.3700 0.1065  -0.0670 -0.0592 14  GLU   A CD  
90   O  OE1 . GLU   A 14  ? 0.2479 0.1691 0.3814 0.0673  -0.0433 -0.0266 14  GLU   A OE1 
91   O  OE2 . GLU   A 14  ? 0.3353 0.1817 0.3615 0.0810  -0.0316 -0.0423 14  GLU   A OE2 
92   N  N   . HIS   A 15  ? 0.1348 0.1992 0.2703 -0.0015 -0.0170 0.0316  15  HIS   A N   
93   C  CA  . HIS   A 15  ? 0.1291 0.1658 0.2771 0.0129  -0.0086 0.0216  15  HIS   A CA  
94   C  C   . HIS   A 15  ? 0.1486 0.1833 0.3190 0.0239  -0.0079 -0.0025 15  HIS   A C   
95   O  O   . HIS   A 15  ? 0.0950 0.1953 0.3474 0.0447  -0.0429 -0.0108 15  HIS   A O   
96   C  CB  . HIS   A 15  ? 0.1270 0.1759 0.2647 0.0395  -0.0577 -0.0271 15  HIS   A CB  
97   C  CG  . HIS   A 15  ? 0.1341 0.1942 0.2952 0.0677  -0.0094 0.0209  15  HIS   A CG  
98   N  ND1 . HIS   A 15  ? 0.1643 0.3269 0.2981 0.1434  -0.0479 0.0111  15  HIS   A ND1 
99   C  CD2 . HIS   A 15  ? 0.1456 0.2136 0.3150 0.0528  -0.0394 0.0106  15  HIS   A CD2 
100  C  CE1 . HIS   A 15  ? 0.2255 0.2973 0.3825 0.0823  -0.0294 -0.0258 15  HIS   A CE1 
101  N  NE2 . HIS   A 15  ? 0.2396 0.2498 0.3364 0.1099  -0.0254 0.0173  15  HIS   A NE2 
102  N  N   . TRP   A 16  ? 0.1305 0.1495 0.2506 -0.0047 -0.0372 0.0116  16  TRP   A N   
103  C  CA  . TRP   A 16  ? 0.0849 0.1672 0.2963 0.0126  -0.0420 -0.0092 16  TRP   A CA  
104  C  C   . TRP   A 16  ? 0.1116 0.1770 0.2536 -0.0278 -0.0131 0.0000  16  TRP   A C   
105  O  O   . TRP   A 16  ? 0.1072 0.1687 0.3237 -0.0062 -0.0452 0.0116  16  TRP   A O   
106  C  CB  . TRP   A 16  ? 0.0815 0.1740 0.2581 0.0164  -0.0403 -0.0023 16  TRP   A CB  
107  C  CG  . TRP   A 16  ? 0.1174 0.1678 0.2484 0.0144  -0.0321 -0.0039 16  TRP   A CG  
108  C  CD1 . TRP   A 16  ? 0.1504 0.1298 0.2359 0.0310  -0.0569 -0.0142 16  TRP   A CD1 
109  C  CD2 . TRP   A 16  ? 0.1177 0.1411 0.2723 -0.0038 -0.0022 0.0116  16  TRP   A CD2 
110  N  NE1 . TRP   A 16  ? 0.1339 0.1450 0.2524 0.0039  -0.0497 -0.0010 16  TRP   A NE1 
111  C  CE2 . TRP   A 16  ? 0.1134 0.1540 0.2797 0.0025  -0.0314 -0.0006 16  TRP   A CE2 
112  C  CE3 . TRP   A 16  ? 0.1346 0.1327 0.2368 -0.0336 -0.0038 0.0093  16  TRP   A CE3 
113  C  CZ2 . TRP   A 16  ? 0.1203 0.0953 0.2830 -0.0282 0.0073  0.0203  16  TRP   A CZ2 
114  C  CZ3 . TRP   A 16  ? 0.1255 0.1626 0.3103 -0.0429 0.0053  0.0001  16  TRP   A CZ3 
115  C  CH2 . TRP   A 16  ? 0.1339 0.1452 0.2506 0.0209  0.0104  0.0324  16  TRP   A CH2 
116  N  N   . HIS   A 17  ? 0.1317 0.2057 0.2624 0.0230  -0.0018 -0.0153 17  HIS   A N   
117  C  CA  . HIS   A 17  ? 0.1334 0.2111 0.2578 -0.0218 -0.0115 0.0124  17  HIS   A CA  
118  C  C   . HIS   A 17  ? 0.1244 0.2426 0.2746 -0.0405 -0.0207 -0.0059 17  HIS   A C   
119  O  O   . HIS   A 17  ? 0.0770 0.2003 0.3456 0.0072  -0.0184 -0.0196 17  HIS   A O   
120  C  CB  . HIS   A 17  ? 0.1524 0.2194 0.2448 0.0540  0.0070  0.0114  17  HIS   A CB  
121  C  CG  . HIS   A 17  ? 0.1018 0.2084 0.2414 0.0199  -0.0225 -0.0162 17  HIS   A CG  
122  N  ND1 . HIS   A 17  ? 0.1240 0.2895 0.3061 -0.0074 -0.0434 0.0100  17  HIS   A ND1 
123  C  CD2 . HIS   A 17  ? 0.1755 0.2005 0.2975 0.0842  0.0154  -0.0047 17  HIS   A CD2 
124  C  CE1 . HIS   A 17  ? 0.1888 0.3279 0.2911 0.0516  -0.0419 0.0139  17  HIS   A CE1 
125  N  NE2 . HIS   A 17  ? 0.1759 0.2701 0.3410 0.0399  -0.0177 0.0418  17  HIS   A NE2 
126  N  N   . LYS   A 18  ? 0.1330 0.1952 0.2587 -0.0361 -0.0124 0.0242  18  LYS   A N   
127  C  CA  . LYS   A 18  ? 0.1253 0.2036 0.3606 -0.0008 0.0377  0.0316  18  LYS   A CA  
128  C  C   . LYS   A 18  ? 0.1576 0.2192 0.3267 -0.0429 -0.0157 0.0539  18  LYS   A C   
129  O  O   . LYS   A 18  ? 0.1490 0.2822 0.4506 -0.0639 -0.0879 0.0446  18  LYS   A O   
130  C  CB  . LYS   A 18  ? 0.0835 0.2377 0.3574 0.0299  0.0020  0.0208  18  LYS   A CB  
131  C  CG  . LYS   A 18  ? 0.1887 0.2354 0.3212 0.0609  -0.0175 0.0132  18  LYS   A CG  
132  C  CD  . LYS   A 18  ? 0.1684 0.2157 0.3623 0.0559  -0.0528 -0.0209 18  LYS   A CD  
133  C  CE  . LYS   A 18  ? 0.1490 0.1985 0.2877 0.0370  -0.0275 0.0252  18  LYS   A CE  
134  N  NZ  . LYS   A 18  ? 0.1210 0.3177 0.2859 0.0587  -0.0192 0.0059  18  LYS   A NZ  
135  N  N   . ASP   A 19  ? 0.2242 0.2701 0.2672 0.0064  -0.0293 0.0274  19  ASP   A N   
136  C  CA  . ASP   A 19  ? 0.1338 0.2558 0.3200 -0.0161 -0.0089 0.0342  19  ASP   A CA  
137  C  C   . ASP   A 19  ? 0.0847 0.2333 0.3512 -0.0278 -0.0348 0.0458  19  ASP   A C   
138  O  O   . ASP   A 19  ? 0.1738 0.1975 0.3712 -0.0460 0.0122  0.0272  19  ASP   A O   
139  C  CB  . ASP   A 19  ? 0.1687 0.3699 0.3164 0.0942  -0.0332 -0.0130 19  ASP   A CB  
140  C  CG  . ASP   A 19  ? 0.3149 0.4348 0.4062 0.1168  0.0905  0.0064  19  ASP   A CG  
141  O  OD1 . ASP   A 19  ? 0.4079 0.5325 0.3848 0.0308  0.0949  -0.0272 19  ASP   A OD1 
142  O  OD2 . ASP   A 19  ? 0.5506 0.7095 0.6241 0.0150  0.1301  -0.2707 19  ASP   A OD2 
143  N  N   . PHE   A 20  ? 0.1197 0.1856 0.3490 -0.0264 0.0019  0.0298  20  PHE   A N   
144  C  CA  . PHE   A 20  ? 0.0791 0.2397 0.2538 -0.0895 -0.0126 -0.0118 20  PHE   A CA  
145  C  C   . PHE   A 20  ? 0.1062 0.1709 0.2653 -0.0065 -0.0332 0.0085  20  PHE   A C   
146  O  O   . PHE   A 20  ? 0.1138 0.1551 0.3050 -0.0015 -0.0048 0.0023  20  PHE   A O   
147  C  CB  . PHE   A 20  ? 0.0955 0.2082 0.2736 -0.0487 -0.0615 -0.0085 20  PHE   A CB  
148  C  CG  . PHE   A 20  ? 0.1252 0.1993 0.2918 -0.0396 -0.0433 -0.0006 20  PHE   A CG  
149  C  CD1 . PHE   A 20  ? 0.1305 0.2164 0.3418 -0.0739 -0.0494 0.0606  20  PHE   A CD1 
150  C  CD2 . PHE   A 20  ? 0.1511 0.2940 0.2787 -0.0841 -0.0128 -0.0425 20  PHE   A CD2 
151  C  CE1 . PHE   A 20  ? 0.1461 0.2205 0.3325 -0.0290 -0.0579 0.0341  20  PHE   A CE1 
152  C  CE2 . PHE   A 20  ? 0.1059 0.2754 0.3346 0.0003  -0.0873 0.0581  20  PHE   A CE2 
153  C  CZ  . PHE   A 20  ? 0.0908 0.2689 0.3608 -0.0205 -0.0281 0.0815  20  PHE   A CZ  
154  N  N   A PRO   A 21  ? 0.0933 0.2253 0.2791 -0.0245 -0.0034 -0.0309 21  PRO   A N   
155  N  N   B PRO   A 21  ? 0.0996 0.2235 0.2832 -0.0140 -0.0198 -0.0218 21  PRO   A N   
156  C  CA  A PRO   A 21  ? 0.1046 0.2345 0.2863 -0.0648 -0.0334 -0.0154 21  PRO   A CA  
157  C  CA  B PRO   A 21  ? 0.1102 0.2530 0.2883 -0.0679 -0.0292 0.0065  21  PRO   A CA  
158  C  C   A PRO   A 21  ? 0.0881 0.2751 0.2591 -0.0252 -0.0647 0.0239  21  PRO   A C   
159  C  C   B PRO   A 21  ? 0.0806 0.2279 0.2805 -0.0198 -0.0544 0.0079  21  PRO   A C   
160  O  O   A PRO   A 21  ? 0.1446 0.1221 0.2716 -0.0516 -0.0520 0.0005  21  PRO   A O   
161  O  O   B PRO   A 21  ? 0.1152 0.2038 0.2550 -0.0574 -0.0551 -0.0122 21  PRO   A O   
162  C  CB  A PRO   A 21  ? 0.1009 0.2239 0.3121 -0.0589 -0.0348 -0.0221 21  PRO   A CB  
163  C  CB  B PRO   A 21  ? 0.1377 0.1969 0.2906 -0.0493 -0.0751 0.0392  21  PRO   A CB  
164  C  CG  A PRO   A 21  ? 0.0576 0.2153 0.3078 -0.0735 -0.0319 -0.0332 21  PRO   A CG  
165  C  CG  B PRO   A 21  ? 0.0671 0.2235 0.3471 -0.0469 -0.0414 0.0380  21  PRO   A CG  
166  C  CD  A PRO   A 21  ? 0.0921 0.2222 0.2997 -0.0394 -0.0229 -0.0304 21  PRO   A CD  
167  C  CD  B PRO   A 21  ? 0.0949 0.2319 0.3387 -0.0209 -0.0501 0.0113  21  PRO   A CD  
168  N  N   . ILE   A 22  ? 0.0908 0.1975 0.2606 -0.0027 -0.0432 -0.0384 22  ILE   A N   
169  C  CA  . ILE   A 22  ? 0.1338 0.1993 0.2652 -0.0061 -0.0179 0.0166  22  ILE   A CA  
170  C  C   . ILE   A 22  ? 0.1799 0.2032 0.2171 0.0076  -0.0165 -0.0162 22  ILE   A C   
171  O  O   . ILE   A 22  ? 0.1375 0.1357 0.2721 -0.0153 -0.0341 -0.0023 22  ILE   A O   
172  C  CB  . ILE   A 22  ? 0.1816 0.1729 0.2420 -0.0099 -0.0342 0.0187  22  ILE   A CB  
173  C  CG1 . ILE   A 22  ? 0.1544 0.1122 0.2940 -0.0267 -0.0233 0.0335  22  ILE   A CG1 
174  C  CG2 . ILE   A 22  ? 0.1529 0.1816 0.2768 0.0358  -0.0400 -0.0089 22  ILE   A CG2 
175  C  CD1 . ILE   A 22  ? 0.2262 0.1004 0.3751 -0.0039 -0.0370 0.0168  22  ILE   A CD1 
176  N  N   . ALA   A 23  ? 0.1428 0.1410 0.2653 -0.0238 -0.0035 -0.0233 23  ALA   A N   
177  C  CA  . ALA   A 23  ? 0.1669 0.1520 0.2670 -0.0469 0.0135  -0.0184 23  ALA   A CA  
178  C  C   . ALA   A 23  ? 0.1421 0.1720 0.2918 -0.0053 -0.0387 0.0068  23  ALA   A C   
179  O  O   . ALA   A 23  ? 0.0955 0.1866 0.2801 -0.0039 -0.0308 0.0332  23  ALA   A O   
180  C  CB  . ALA   A 23  ? 0.0971 0.1564 0.3018 -0.0181 -0.0013 -0.0131 23  ALA   A CB  
181  N  N   . LYS   A 24  ? 0.1465 0.2280 0.2517 0.0262  -0.0484 -0.0075 24  LYS   A N   
182  C  CA  . LYS   A 24  ? 0.0750 0.2851 0.2621 -0.0168 -0.0190 0.0058  24  LYS   A CA  
183  C  C   . LYS   A 24  ? 0.1564 0.2588 0.2409 -0.0055 -0.0226 0.0252  24  LYS   A C   
184  O  O   . LYS   A 24  ? 0.1497 0.2517 0.3012 0.0027  -0.0652 -0.0037 24  LYS   A O   
185  C  CB  . LYS   A 24  ? 0.0906 0.3043 0.2990 0.0318  -0.0188 0.0179  24  LYS   A CB  
186  C  CG  . LYS   A 24  ? 0.1411 0.2949 0.3467 0.1075  -0.0293 0.0359  24  LYS   A CG  
187  C  CD  . LYS   A 24  ? 0.1528 0.4274 0.3509 0.0848  -0.0621 0.0060  24  LYS   A CD  
188  C  CE  . LYS   A 24  ? 0.2764 0.4259 0.4090 0.0938  0.0586  0.0455  24  LYS   A CE  
189  N  NZ  . LYS   A 24  ? 0.4157 0.3896 0.4813 0.0400  0.0417  0.0006  24  LYS   A NZ  
190  N  N   . GLY   A 25  ? 0.1052 0.2086 0.2718 -0.0392 -0.0144 -0.0021 25  GLY   A N   
191  C  CA  . GLY   A 25  ? 0.1027 0.2685 0.2315 -0.0342 -0.0146 -0.0115 25  GLY   A CA  
192  C  C   . GLY   A 25  ? 0.1335 0.1946 0.1978 -0.0163 -0.0287 -0.0006 25  GLY   A C   
193  O  O   . GLY   A 25  ? 0.1299 0.1967 0.2883 -0.0216 -0.0326 0.0067  25  GLY   A O   
194  N  N   . GLU   A 26  ? 0.1281 0.2995 0.2350 0.0168  -0.0545 -0.0469 26  GLU   A N   
195  C  CA  . GLU   A 26  ? 0.0926 0.2912 0.2511 0.0150  -0.0489 -0.0469 26  GLU   A CA  
196  C  C   . GLU   A 26  ? 0.0806 0.2968 0.2301 0.0200  -0.0379 0.0001  26  GLU   A C   
197  O  O   . GLU   A 26  ? 0.1423 0.2532 0.2629 0.0206  -0.0314 0.0018  26  GLU   A O   
198  C  CB  . GLU   A 26  ? 0.1240 0.3310 0.3219 -0.0460 -0.0469 -0.0898 26  GLU   A CB  
199  C  CG  . GLU   A 26  ? 0.1012 0.5032 0.3511 -0.0547 -0.0333 -0.0273 26  GLU   A CG  
200  C  CD  . GLU   A 26  ? 0.2463 0.4908 0.3604 -0.0087 -0.1117 -0.0736 26  GLU   A CD  
201  O  OE1 . GLU   A 26  ? 0.4929 0.5804 0.4431 -0.0512 -0.1883 0.0895  26  GLU   A OE1 
202  O  OE2 . GLU   A 26  ? 0.2768 0.5337 0.5100 0.0211  -0.0473 -0.0309 26  GLU   A OE2 
203  N  N   . ARG   A 27  ? 0.1216 0.1414 0.2312 -0.0143 -0.0402 -0.0111 27  ARG   A N   
204  C  CA  . ARG   A 27  ? 0.1177 0.1934 0.2391 0.0044  -0.0552 -0.0352 27  ARG   A CA  
205  C  C   . ARG   A 27  ? 0.1403 0.1109 0.2262 -0.0290 -0.0348 -0.0189 27  ARG   A C   
206  O  O   . ARG   A 27  ? 0.1414 0.1373 0.2253 -0.0080 -0.0364 0.0000  27  ARG   A O   
207  C  CB  . ARG   A 27  ? 0.1700 0.2405 0.2921 0.0458  -0.0066 -0.0230 27  ARG   A CB  
208  C  CG  . ARG   A 27  ? 0.2371 0.2636 0.3238 0.0116  -0.0390 -0.0165 27  ARG   A CG  
209  C  CD  . ARG   A 27  ? 0.2559 0.3313 0.3300 0.0842  -0.0782 0.0406  27  ARG   A CD  
210  N  NE  . ARG   A 27  ? 0.2492 0.2085 0.3029 -0.0297 -0.0240 0.0005  27  ARG   A NE  
211  C  CZ  . ARG   A 27  ? 0.2169 0.2543 0.2562 -0.0262 -0.0395 0.0308  27  ARG   A CZ  
212  N  NH1 . ARG   A 27  ? 0.1977 0.3218 0.2970 -0.0181 -0.0466 -0.0447 27  ARG   A NH1 
213  N  NH2 . ARG   A 27  ? 0.2425 0.2989 0.3375 -0.0660 -0.0735 -0.0812 27  ARG   A NH2 
214  N  N   . GLN   A 28  ? 0.1350 0.1334 0.2400 0.0096  -0.0162 -0.0125 28  GLN   A N   
215  C  CA  . GLN   A 28  ? 0.0576 0.1581 0.2372 -0.0082 -0.0268 -0.0035 28  GLN   A CA  
216  C  C   . GLN   A 28  ? 0.0547 0.1386 0.2059 0.0087  -0.0242 -0.0049 28  GLN   A C   
217  O  O   . GLN   A 28  ? 0.1241 0.1747 0.1899 -0.0013 -0.0319 -0.0173 28  GLN   A O   
218  C  CB  . GLN   A 28  ? 0.0876 0.0962 0.2552 0.0071  -0.0162 0.0080  28  GLN   A CB  
219  C  CG  . GLN   A 28  ? 0.1486 0.0747 0.2533 -0.0223 -0.0501 -0.0030 28  GLN   A CG  
220  C  CD  . GLN   A 28  ? 0.1066 0.0879 0.2262 -0.0305 -0.0142 -0.0104 28  GLN   A CD  
221  O  OE1 . GLN   A 28  ? 0.1080 0.1441 0.2595 -0.0138 -0.0136 -0.0159 28  GLN   A OE1 
222  N  NE2 . GLN   A 28  ? 0.0731 0.0885 0.2305 -0.0060 -0.0326 0.0140  28  GLN   A NE2 
223  N  N   . SER   A 29  ? 0.0824 0.1080 0.2114 -0.0088 -0.0218 -0.0326 29  SER   A N   
224  C  CA  . SER   A 29  ? 0.0544 0.1122 0.2347 -0.0008 -0.0396 -0.0119 29  SER   A CA  
225  C  C   . SER   A 29  ? 0.1425 0.1705 0.2133 0.0133  -0.0326 -0.0006 29  SER   A C   
226  O  O   . SER   A 29  ? 0.1382 0.1036 0.2276 0.0105  -0.0220 -0.0072 29  SER   A O   
227  C  CB  . SER   A 29  ? 0.0983 0.1185 0.2194 0.0094  -0.0467 0.0150  29  SER   A CB  
228  O  OG  . SER   A 29  ? 0.0971 0.1265 0.2395 -0.0136 -0.0345 -0.0128 29  SER   A OG  
229  N  N   . PRO   A 30  ? 0.1251 0.1428 0.2285 0.0197  -0.0128 0.0179  30  PRO   A N   
230  C  CA  . PRO   A 30  ? 0.1310 0.1349 0.1970 0.0041  -0.0178 0.0013  30  PRO   A CA  
231  C  C   . PRO   A 30  ? 0.1138 0.1221 0.1715 -0.0183 -0.0185 -0.0149 30  PRO   A C   
232  O  O   . PRO   A 30  ? 0.1251 0.0955 0.2487 0.0172  -0.0483 0.0079  30  PRO   A O   
233  C  CB  . PRO   A 30  ? 0.0655 0.1529 0.2382 0.0355  -0.0541 -0.0223 30  PRO   A CB  
234  C  CG  . PRO   A 30  ? 0.0199 0.1147 0.2687 -0.0189 -0.0346 0.0011  30  PRO   A CG  
235  C  CD  . PRO   A 30  ? 0.1169 0.1097 0.2200 -0.0451 -0.0035 -0.0138 30  PRO   A CD  
236  N  N   . VAL   A 31  ? 0.1095 0.1603 0.2084 0.0183  0.0013  0.0226  31  VAL   A N   
237  C  CA  . VAL   A 31  ? 0.1346 0.1368 0.2021 -0.0217 0.0012  0.0187  31  VAL   A CA  
238  C  C   . VAL   A 31  ? 0.1720 0.1298 0.1935 -0.0258 -0.0523 0.0116  31  VAL   A C   
239  O  O   . VAL   A 31  ? 0.1370 0.1072 0.2758 0.0050  -0.0640 0.0075  31  VAL   A O   
240  C  CB  . VAL   A 31  ? 0.0651 0.1360 0.2556 -0.0116 -0.0315 -0.0231 31  VAL   A CB  
241  C  CG1 . VAL   A 31  ? 0.1249 0.1464 0.2430 -0.0467 -0.0491 -0.0035 31  VAL   A CG1 
242  C  CG2 . VAL   A 31  ? 0.0966 0.1479 0.2655 0.0390  0.0006  -0.0428 31  VAL   A CG2 
243  N  N   . ASP   A 32  ? 0.1363 0.1176 0.2409 -0.0020 -0.0257 0.0244  32  ASP   A N   
244  C  CA  . ASP   A 32  ? 0.1216 0.0849 0.2389 0.0346  -0.0113 0.0292  32  ASP   A CA  
245  C  C   . ASP   A 32  ? 0.1386 0.1384 0.2139 0.0178  -0.0134 -0.0026 32  ASP   A C   
246  O  O   . ASP   A 32  ? 0.1407 0.1633 0.2242 0.0241  -0.0381 -0.0105 32  ASP   A O   
247  C  CB  . ASP   A 32  ? 0.1158 0.0653 0.2825 0.0314  -0.0119 0.0276  32  ASP   A CB  
248  C  CG  . ASP   A 32  ? 0.1497 0.0750 0.2531 0.0102  -0.0362 0.0095  32  ASP   A CG  
249  O  OD1 . ASP   A 32  ? 0.1486 0.1781 0.2278 0.0214  -0.0381 -0.0006 32  ASP   A OD1 
250  O  OD2 . ASP   A 32  ? 0.2205 0.1758 0.2531 -0.0297 0.0113  0.0051  32  ASP   A OD2 
251  N  N   . ILE   A 33  ? 0.1285 0.1134 0.2255 -0.0054 0.0012  0.0070  33  ILE   A N   
252  C  CA  . ILE   A 33  ? 0.1600 0.1576 0.2182 0.0238  0.0053  0.0270  33  ILE   A CA  
253  C  C   . ILE   A 33  ? 0.1367 0.1483 0.2262 0.0621  0.0026  0.0266  33  ILE   A C   
254  O  O   . ILE   A 33  ? 0.1942 0.1679 0.2730 0.0019  -0.0131 0.0241  33  ILE   A O   
255  C  CB  . ILE   A 33  ? 0.1066 0.1273 0.2748 -0.0187 0.0015  0.0225  33  ILE   A CB  
256  C  CG1 . ILE   A 33  ? 0.1669 0.1299 0.2879 -0.0097 -0.0463 0.0479  33  ILE   A CG1 
257  C  CG2 . ILE   A 33  ? 0.0892 0.1881 0.2921 0.0785  -0.0212 0.0342  33  ILE   A CG2 
258  C  CD1 . ILE   A 33  ? 0.1526 0.1456 0.2858 -0.0168 -0.0460 0.0555  33  ILE   A CD1 
259  N  N   . ASP   A 34  ? 0.1896 0.1712 0.2114 0.0257  -0.0126 0.0422  34  ASP   A N   
260  C  CA  . ASP   A 34  ? 0.2430 0.1464 0.2082 0.0556  -0.0039 0.0301  34  ASP   A CA  
261  C  C   . ASP   A 34  ? 0.2161 0.1881 0.2629 -0.0109 0.0181  0.0089  34  ASP   A C   
262  O  O   . ASP   A 34  ? 0.2789 0.2003 0.2524 0.0751  -0.0055 0.0176  34  ASP   A O   
263  C  CB  . ASP   A 34  ? 0.3337 0.1705 0.2427 0.0488  -0.0649 0.0044  34  ASP   A CB  
264  C  CG  . ASP   A 34  ? 0.2995 0.2021 0.3618 0.0616  0.0223  0.0425  34  ASP   A CG  
265  O  OD1 . ASP   A 34  ? 0.3975 0.2289 0.3637 0.0229  0.0565  0.0526  34  ASP   A OD1 
266  O  OD2 . ASP   A 34  ? 0.3795 0.3774 0.5554 0.0308  -0.0440 0.2112  34  ASP   A OD2 
267  N  N   . THR   A 35  ? 0.1876 0.1452 0.2624 0.0431  -0.0049 0.0419  35  THR   A N   
268  C  CA  . THR   A 35  ? 0.1982 0.2469 0.2584 0.0952  -0.0021 0.0089  35  THR   A CA  
269  C  C   . THR   A 35  ? 0.2791 0.2674 0.2512 0.1108  0.0320  0.0483  35  THR   A C   
270  O  O   . THR   A 35  ? 0.2896 0.2916 0.3013 0.0952  0.0714  0.0497  35  THR   A O   
271  C  CB  . THR   A 35  ? 0.2594 0.2214 0.3071 0.0394  0.0070  0.0389  35  THR   A CB  
272  O  OG1 . THR   A 35  ? 0.2368 0.2164 0.3050 0.0258  0.0234  0.0399  35  THR   A OG1 
273  C  CG2 . THR   A 35  ? 0.2810 0.2384 0.2659 0.1072  -0.0375 0.0387  35  THR   A CG2 
274  N  N   . HIS   A 36  ? 0.3402 0.1743 0.2322 0.0356  0.0110  0.0675  36  HIS   A N   
275  C  CA  . HIS   A 36  ? 0.4220 0.2134 0.2401 0.0757  -0.0005 0.0324  36  HIS   A CA  
276  C  C   . HIS   A 36  ? 0.4014 0.3504 0.2251 -0.0364 0.0306  -0.0085 36  HIS   A C   
277  O  O   . HIS   A 36  ? 0.3800 0.4205 0.3315 -0.0027 0.0585  -0.0181 36  HIS   A O   
278  C  CB  . HIS   A 36  ? 0.4181 0.2091 0.3336 0.0606  0.0441  0.0793  36  HIS   A CB  
279  C  CG  . HIS   A 36  ? 0.5703 0.2907 0.3224 0.0266  -0.0259 0.0369  36  HIS   A CG  
280  N  ND1 . HIS   A 36  ? 0.7160 0.2537 0.2734 0.0604  -0.1043 0.0443  36  HIS   A ND1 
281  C  CD2 . HIS   A 36  ? 0.5866 0.3205 0.3107 -0.1459 -0.1632 0.0762  36  HIS   A CD2 
282  C  CE1 . HIS   A 36  ? 0.7576 0.2636 0.2960 0.1081  -0.1875 -0.0135 36  HIS   A CE1 
283  N  NE2 . HIS   A 36  ? 0.7663 0.4066 0.4772 -0.0267 -0.1474 -0.0617 36  HIS   A NE2 
284  N  N   . THR   A 37  ? 0.3210 0.1755 0.2891 0.0490  0.0205  0.0212  37  THR   A N   
285  C  CA  . THR   A 37  ? 0.4560 0.1526 0.2653 0.0774  -0.0153 0.0409  37  THR   A CA  
286  C  C   . THR   A 37  ? 0.2887 0.2045 0.2907 0.0888  -0.0527 0.0600  37  THR   A C   
287  O  O   . THR   A 37  ? 0.4065 0.2847 0.2979 0.0903  -0.0399 -0.0227 37  THR   A O   
288  C  CB  . THR   A 37  ? 0.4452 0.3371 0.3943 0.1725  -0.0687 0.0749  37  THR   A CB  
289  O  OG1 . THR   A 37  ? 0.6650 0.4454 0.3961 0.0824  -0.0810 -0.0048 37  THR   A OG1 
290  C  CG2 . THR   A 37  ? 0.2430 0.3189 0.4892 0.1702  -0.0950 0.0684  37  THR   A CG2 
291  N  N   . ALA   A 38  ? 0.3419 0.2043 0.2438 0.0708  -0.0225 0.0591  38  ALA   A N   
292  C  CA  . ALA   A 38  ? 0.2667 0.2086 0.2358 0.1293  0.0248  -0.0181 38  ALA   A CA  
293  C  C   . ALA   A 38  ? 0.1757 0.3347 0.3407 0.0328  0.0253  -0.0179 38  ALA   A C   
294  O  O   . ALA   A 38  ? 0.3015 0.3114 0.4507 0.0330  0.1430  -0.0151 38  ALA   A O   
295  C  CB  . ALA   A 38  ? 0.2889 0.1811 0.2404 0.0917  0.0055  0.0029  38  ALA   A CB  
296  N  N   . LYS   A 39  ? 0.2158 0.3500 0.3169 0.1013  -0.0099 -0.0505 39  LYS   A N   
297  C  CA  . LYS   A 39  ? 0.2220 0.4072 0.3243 0.1295  -0.0077 -0.0010 39  LYS   A CA  
298  C  C   . LYS   A 39  ? 0.1941 0.3366 0.2459 0.0776  -0.0162 -0.0361 39  LYS   A C   
299  O  O   . LYS   A 39  ? 0.1773 0.3168 0.2912 0.0346  -0.0375 -0.0262 39  LYS   A O   
300  C  CB  . LYS   A 39  ? 0.3262 0.4930 0.3341 0.2158  -0.0504 -0.0974 39  LYS   A CB  
301  C  CG  . LYS   A 39  ? 0.2714 0.6402 0.3591 0.2778  -0.1133 -0.0581 39  LYS   A CG  
302  C  CD  . LYS   A 39  ? 0.4193 0.5624 0.3023 0.1866  -0.1559 0.0474  39  LYS   A CD  
303  C  CE  . LYS   A 39  ? 0.3477 0.8920 0.2693 0.1269  -0.1181 -0.1104 39  LYS   A CE  
304  N  NZ  . LYS   A 39  ? 0.3547 0.8347 0.5109 0.1834  -0.1065 0.2268  39  LYS   A NZ  
305  N  N   . TYR   A 40  ? 0.2946 0.2626 0.2748 0.0316  0.0060  0.0322  40  TYR   A N   
306  C  CA  . TYR   A 40  ? 0.2118 0.2564 0.2777 -0.0514 -0.0010 -0.0066 40  TYR   A CA  
307  C  C   . TYR   A 40  ? 0.1978 0.2614 0.2382 0.0477  0.0092  -0.0003 40  TYR   A C   
308  O  O   . TYR   A 40  ? 0.2258 0.3542 0.2623 0.0290  -0.0346 -0.0044 40  TYR   A O   
309  C  CB  . TYR   A 40  ? 0.2312 0.3338 0.3632 -0.0737 0.0471  0.0237  40  TYR   A CB  
310  C  CG  . TYR   A 40  ? 0.2372 0.4613 0.2720 -0.0801 -0.0004 -0.0143 40  TYR   A CG  
311  C  CD1 . TYR   A 40  ? 0.1204 0.4704 0.3534 -0.0880 -0.1222 0.0245  40  TYR   A CD1 
312  C  CD2 . TYR   A 40  ? 0.1738 0.5761 0.3776 -0.0144 0.0322  -0.0113 40  TYR   A CD2 
313  C  CE1 . TYR   A 40  ? 0.1301 0.5999 0.2792 -0.0039 -0.0585 0.0200  40  TYR   A CE1 
314  C  CE2 . TYR   A 40  ? 0.2243 0.5671 0.3274 0.0305  0.0050  -0.0462 40  TYR   A CE2 
315  C  CZ  . TYR   A 40  ? 0.2006 0.6059 0.3660 -0.0657 0.0060  0.0243  40  TYR   A CZ  
316  O  OH  . TYR   A 40  ? 0.2555 0.6227 0.4864 0.0006  0.0011  -0.0758 40  TYR   A OH  
317  N  N   . ASP   A 41  ? 0.1752 0.2093 0.2384 0.0148  -0.0087 -0.0138 41  ASP   A N   
318  C  CA  . ASP   A 41  ? 0.2053 0.1964 0.2519 -0.0023 -0.0489 -0.0111 41  ASP   A CA  
319  C  C   . ASP   A 41  ? 0.2214 0.3182 0.3122 0.0276  -0.0070 -0.0298 41  ASP   A C   
320  O  O   . ASP   A 41  ? 0.2319 0.3585 0.2973 0.0053  0.0004  -0.0184 41  ASP   A O   
321  C  CB  . ASP   A 41  ? 0.2433 0.1923 0.3635 0.0159  -0.0291 -0.0039 41  ASP   A CB  
322  C  CG  . ASP   A 41  ? 0.3310 0.2841 0.3176 -0.0168 -0.0082 -0.1045 41  ASP   A CG  
323  O  OD1 . ASP   A 41  ? 0.3236 0.2961 0.3116 0.1017  -0.0386 -0.0416 41  ASP   A OD1 
324  O  OD2 . ASP   A 41  ? 0.3613 0.3491 0.3562 -0.0466 -0.0275 -0.0312 41  ASP   A OD2 
325  N  N   . PRO   A 42  ? 0.1626 0.4414 0.3058 0.0595  -0.0209 0.0023  42  PRO   A N   
326  C  CA  . PRO   A 42  ? 0.1899 0.3816 0.3670 0.0950  0.0460  0.0930  42  PRO   A CA  
327  C  C   . PRO   A 42  ? 0.1920 0.3538 0.3810 0.0859  0.0294  0.0628  42  PRO   A C   
328  O  O   . PRO   A 42  ? 0.2157 0.5871 0.4530 0.1351  -0.0146 0.0344  42  PRO   A O   
329  C  CB  . PRO   A 42  ? 0.2419 0.5264 0.4049 0.1322  0.0925  0.1358  42  PRO   A CB  
330  C  CG  . PRO   A 42  ? 0.3104 0.6963 0.3723 0.0587  0.0387  -0.0428 42  PRO   A CG  
331  C  CD  . PRO   A 42  ? 0.4210 0.4224 0.2893 0.0868  0.0696  -0.0055 42  PRO   A CD  
332  N  N   . SER   A 43  ? 0.3665 0.3243 0.3037 -0.0122 0.0423  -0.0053 43  SER   A N   
333  C  CA  . SER   A 43  ? 0.4497 0.2872 0.3193 0.0928  -0.0498 -0.0418 43  SER   A CA  
334  C  C   . SER   A 43  ? 0.4339 0.2911 0.3137 0.0948  -0.0460 -0.0156 43  SER   A C   
335  O  O   . SER   A 43  ? 0.5131 0.3543 0.4283 0.1483  -0.0652 0.0440  43  SER   A O   
336  C  CB  . SER   A 43  ? 0.3349 0.3167 0.4298 0.0761  -0.0454 -0.0655 43  SER   A CB  
337  O  OG  . SER   A 43  ? 0.4331 0.3656 0.4737 0.0946  -0.0089 -0.0317 43  SER   A OG  
338  N  N   . LEU   A 44  ? 0.3460 0.3828 0.2987 0.0920  -0.0443 -0.0589 44  LEU   A N   
339  C  CA  . LEU   A 44  ? 0.2685 0.2999 0.3167 0.1161  -0.0768 -0.0008 44  LEU   A CA  
340  C  C   . LEU   A 44  ? 0.2039 0.4519 0.4132 -0.0178 -0.0610 0.0542  44  LEU   A C   
341  O  O   . LEU   A 44  ? 0.1729 0.6074 0.5297 -0.0634 -0.0332 0.0533  44  LEU   A O   
342  C  CB  . LEU   A 44  ? 0.2527 0.2312 0.3381 0.0569  -0.0722 0.0182  44  LEU   A CB  
343  C  CG  . LEU   A 44  ? 0.2325 0.2077 0.2892 0.0304  -0.0256 0.0186  44  LEU   A CG  
344  C  CD1 . LEU   A 44  ? 0.1508 0.2394 0.3156 0.0057  -0.0473 -0.0445 44  LEU   A CD1 
345  C  CD2 . LEU   A 44  ? 0.2436 0.2352 0.2819 -0.0374 -0.0768 0.0003  44  LEU   A CD2 
346  N  N   . LYS   A 45  ? 0.2136 0.4507 0.3757 -0.0022 -0.0851 0.0311  45  LYS   A N   
347  C  CA  . LYS   A 45  ? 0.2554 0.2736 0.4804 0.0130  -0.1610 -0.0424 45  LYS   A CA  
348  C  C   . LYS   A 45  ? 0.2258 0.3280 0.3531 0.0465  -0.1142 0.0546  45  LYS   A C   
349  O  O   . LYS   A 45  ? 0.2088 0.5114 0.3378 -0.0686 -0.0068 -0.0902 45  LYS   A O   
350  C  CB  . LYS   A 45  ? 0.2159 0.3094 0.4514 0.0560  -0.0677 0.0176  45  LYS   A CB  
351  C  CG  . LYS   A 45  ? 0.3066 0.4270 0.3891 0.0293  -0.1317 -0.0124 45  LYS   A CG  
352  C  CD  . LYS   A 45  ? 0.4710 0.4152 0.6450 -0.1311 0.0370  0.0783  45  LYS   A CD  
353  N  N   . PRO   A 46  ? 0.2207 0.3899 0.3697 -0.0379 -0.0714 0.0297  46  PRO   A N   
354  C  CA  . PRO   A 46  ? 0.1806 0.4493 0.3170 -0.0963 -0.0546 0.0460  46  PRO   A CA  
355  C  C   . PRO   A 46  ? 0.1386 0.2684 0.3035 0.0198  -0.0299 0.0159  46  PRO   A C   
356  O  O   . PRO   A 46  ? 0.1482 0.2388 0.3861 -0.0572 -0.0794 0.0464  46  PRO   A O   
357  C  CB  . PRO   A 46  ? 0.1630 0.3867 0.3863 -0.0713 -0.0199 -0.0504 46  PRO   A CB  
358  C  CG  . PRO   A 46  ? 0.1985 0.5026 0.4092 -0.0640 0.0025  -0.0891 46  PRO   A CG  
359  C  CD  . PRO   A 46  ? 0.2879 0.3406 0.3723 -0.0005 -0.0463 -0.0857 46  PRO   A CD  
360  N  N   . LEU   A 47  ? 0.1819 0.3754 0.3131 0.0324  -0.0221 0.0130  47  LEU   A N   
361  C  CA  . LEU   A 47  ? 0.1513 0.3113 0.2989 0.0244  -0.0401 0.0465  47  LEU   A CA  
362  C  C   . LEU   A 47  ? 0.1589 0.2580 0.3775 -0.0299 -0.0908 0.0611  47  LEU   A C   
363  O  O   . LEU   A 47  ? 0.1186 0.3696 0.4567 -0.0403 -0.0851 0.0533  47  LEU   A O   
364  C  CB  . LEU   A 47  ? 0.2251 0.3370 0.4139 -0.0198 -0.0578 0.0132  47  LEU   A CB  
365  C  CG  . LEU   A 47  ? 0.1508 0.3259 0.4633 -0.0292 -0.0374 -0.1136 47  LEU   A CG  
366  C  CD1 . LEU   A 47  ? 0.1386 0.2171 0.5565 -0.0757 -0.0495 -0.0048 47  LEU   A CD1 
367  C  CD2 . LEU   A 47  ? 0.1274 0.2845 0.5586 0.0418  -0.0923 -0.0585 47  LEU   A CD2 
368  N  N   . SER   A 48  ? 0.1208 0.2133 0.3030 0.0168  -0.0364 0.0170  48  SER   A N   
369  C  CA  . SER   A 48  ? 0.2007 0.2229 0.2675 -0.0192 -0.0482 0.0207  48  SER   A CA  
370  C  C   . SER   A 48  ? 0.1896 0.1776 0.3035 -0.0289 -0.0033 0.0167  48  SER   A C   
371  O  O   . SER   A 48  ? 0.1737 0.1720 0.3450 -0.0435 -0.0320 -0.0623 48  SER   A O   
372  C  CB  . SER   A 48  ? 0.1641 0.2147 0.3369 -0.0131 -0.0502 0.0301  48  SER   A CB  
373  O  OG  . SER   A 48  ? 0.1939 0.2271 0.3780 0.0299  -0.0334 0.0597  48  SER   A OG  
374  N  N   . VAL   A 49  ? 0.2214 0.2339 0.2890 -0.0313 0.0099  -0.0122 49  VAL   A N   
375  C  CA  . VAL   A 49  ? 0.2634 0.1608 0.2806 -0.0612 -0.0041 -0.0310 49  VAL   A CA  
376  C  C   . VAL   A 49  ? 0.1781 0.2470 0.3172 -0.0784 -0.0298 -0.0545 49  VAL   A C   
377  O  O   . VAL   A 49  ? 0.2261 0.3362 0.3345 -0.1513 -0.0770 -0.0231 49  VAL   A O   
378  C  CB  . VAL   A 49  ? 0.3292 0.1525 0.3113 -0.0772 0.0066  -0.0245 49  VAL   A CB  
379  C  CG1 . VAL   A 49  ? 0.4561 0.3096 0.3493 -0.0957 0.0471  0.0141  49  VAL   A CG1 
380  C  CG2 . VAL   A 49  ? 0.2516 0.1747 0.3695 -0.0439 0.0219  -0.0179 49  VAL   A CG2 
381  N  N   . SER   A 50  ? 0.2291 0.2377 0.2932 -0.0184 -0.0494 0.0074  50  SER   A N   
382  C  CA  . SER   A 50  ? 0.2316 0.1510 0.3589 -0.0148 -0.0197 0.0325  50  SER   A CA  
383  C  C   . SER   A 50  ? 0.2156 0.2354 0.3223 -0.0142 -0.0517 0.0279  50  SER   A C   
384  O  O   . SER   A 50  ? 0.1791 0.2562 0.3571 -0.0476 -0.0761 0.0277  50  SER   A O   
385  C  CB  . SER   A 50  ? 0.3176 0.2108 0.4075 0.0787  0.0193  -0.0171 50  SER   A CB  
386  O  OG  . SER   A 50  ? 0.4440 0.4048 0.5108 0.0441  0.0598  -0.1058 50  SER   A OG  
387  N  N   . TYR   A 51  ? 0.1640 0.2707 0.3182 -0.0244 -0.0494 -0.0179 51  TYR   A N   
388  C  CA  . TYR   A 51  ? 0.1587 0.1824 0.2960 -0.0491 -0.0530 0.0474  51  TYR   A CA  
389  C  C   . TYR   A 51  ? 0.1691 0.2541 0.3181 0.0381  -0.0530 0.0407  51  TYR   A C   
390  O  O   . TYR   A 51  ? 0.1806 0.3272 0.3327 -0.0305 -0.0480 -0.0063 51  TYR   A O   
391  C  CB  . TYR   A 51  ? 0.1386 0.2186 0.3292 -0.0141 -0.0838 0.0201  51  TYR   A CB  
392  C  CG  . TYR   A 51  ? 0.1195 0.2142 0.2640 -0.0249 -0.0550 -0.0059 51  TYR   A CG  
393  C  CD1 . TYR   A 51  ? 0.1228 0.2154 0.3283 -0.0201 -0.0748 -0.0109 51  TYR   A CD1 
394  C  CD2 . TYR   A 51  ? 0.1432 0.2092 0.3256 -0.0003 -0.0197 -0.0495 51  TYR   A CD2 
395  C  CE1 . TYR   A 51  ? 0.0926 0.1737 0.3033 -0.0131 -0.0379 0.0203  51  TYR   A CE1 
396  C  CE2 . TYR   A 51  ? 0.1289 0.1709 0.3082 -0.0776 -0.0214 -0.0147 51  TYR   A CE2 
397  C  CZ  . TYR   A 51  ? 0.0915 0.1579 0.3190 -0.0312 -0.0463 -0.0210 51  TYR   A CZ  
398  O  OH  . TYR   A 51  ? 0.1145 0.1403 0.2933 -0.0130 -0.0455 -0.0091 51  TYR   A OH  
399  N  N   A ASP   A 52  ? 0.1547 0.3260 0.4111 0.0124  -0.0165 0.0385  52  ASP   A N   
400  N  N   B ASP   A 52  ? 0.1263 0.2900 0.4164 -0.0326 -0.0317 0.0528  52  ASP   A N   
401  C  CA  A ASP   A 52  ? 0.2100 0.3359 0.3714 0.0611  0.0000  0.0748  52  ASP   A CA  
402  C  CA  B ASP   A 52  ? 0.1668 0.3189 0.3910 0.0864  0.0042  0.0615  52  ASP   A CA  
403  C  C   A ASP   A 52  ? 0.1716 0.2769 0.3565 0.0244  -0.0491 0.0484  52  ASP   A C   
404  C  C   B ASP   A 52  ? 0.2073 0.3407 0.3840 0.0000  -0.0668 0.0714  52  ASP   A C   
405  O  O   A ASP   A 52  ? 0.2445 0.2956 0.3607 0.0527  -0.0761 0.1354  52  ASP   A O   
406  O  O   B ASP   A 52  ? 0.0862 0.4627 0.3848 0.0788  -0.0461 0.0767  52  ASP   A O   
407  C  CB  A ASP   A 52  ? 0.1709 0.3906 0.4738 0.0577  0.0054  0.0729  52  ASP   A CB  
408  C  CB  B ASP   A 52  ? 0.1277 0.3393 0.4535 0.0772  0.0220  0.0980  52  ASP   A CB  
409  C  CG  A ASP   A 52  ? 0.2384 0.4219 0.5877 0.0937  0.0480  -0.0104 52  ASP   A CG  
410  C  CG  B ASP   A 52  ? 0.1684 0.2450 0.5923 0.1250  -0.0461 0.0845  52  ASP   A CG  
411  O  OD1 A ASP   A 52  ? 0.3516 0.2351 0.4989 0.0469  0.1180  0.0532  52  ASP   A OD1 
412  O  OD1 B ASP   A 52  ? 0.3121 0.2943 0.5863 0.1249  -0.1242 0.0730  52  ASP   A OD1 
413  O  OD2 A ASP   A 52  ? 0.3501 0.5600 0.6799 0.1226  -0.0597 0.2425  52  ASP   A OD2 
414  O  OD2 B ASP   A 52  ? 0.3914 0.2646 0.5694 0.1895  0.1207  0.1295  52  ASP   A OD2 
415  N  N   . GLN   A 53  ? 0.1016 0.3468 0.3587 0.0203  -0.0538 0.0183  53  GLN   A N   
416  C  CA  . GLN   A 53  ? 0.1483 0.2884 0.4833 0.0500  0.0154  0.0361  53  GLN   A CA  
417  C  C   . GLN   A 53  ? 0.1431 0.2902 0.3869 0.0350  -0.0070 0.0315  53  GLN   A C   
418  O  O   . GLN   A 53  ? 0.2131 0.2928 0.3222 -0.0061 0.0068  -0.0057 53  GLN   A O   
419  C  CB  . GLN   A 53  ? 0.1921 0.3360 0.5308 0.0827  -0.0601 -0.0066 53  GLN   A CB  
420  C  CG  . GLN   A 53  ? 0.1860 0.6184 0.7896 0.0989  0.0210  0.1116  53  GLN   A CG  
421  C  CD  . GLN   A 53  ? 0.1711 0.5713 0.8885 -0.0092 -0.1291 0.0619  53  GLN   A CD  
422  O  OE1 . GLN   A 53  ? 0.4618 0.8219 1.1815 -0.1780 -0.0331 0.2931  53  GLN   A OE1 
423  N  NE2 . GLN   A 53  ? 0.3568 0.4026 0.9779 -0.0895 0.1237  0.1628  53  GLN   A NE2 
424  N  N   . ALA   A 54  ? 0.1646 0.2437 0.3328 0.0034  -0.0429 -0.0059 54  ALA   A N   
425  C  CA  . ALA   A 54  ? 0.1568 0.1532 0.3479 -0.0002 -0.0346 -0.0194 54  ALA   A CA  
426  C  C   . ALA   A 54  ? 0.1680 0.2226 0.3290 -0.0155 -0.0245 -0.0619 54  ALA   A C   
427  O  O   . ALA   A 54  ? 0.2187 0.5238 0.3614 0.0281  -0.0901 -0.1559 54  ALA   A O   
428  C  CB  . ALA   A 54  ? 0.1560 0.1766 0.3449 0.0257  -0.0350 -0.0118 54  ALA   A CB  
429  N  N   . THR   A 55  ? 0.1378 0.1747 0.3189 0.0497  -0.0521 0.0162  55  THR   A N   
430  C  CA  . THR   A 55  ? 0.1288 0.2000 0.2898 0.0533  -0.0648 0.0128  55  THR   A CA  
431  C  C   . THR   A 55  ? 0.1138 0.1791 0.2523 0.0164  -0.0375 0.0157  55  THR   A C   
432  O  O   . THR   A 55  ? 0.1310 0.1754 0.2850 0.0165  -0.0538 0.0225  55  THR   A O   
433  C  CB  . THR   A 55  ? 0.2867 0.2409 0.3503 0.0617  -0.0259 0.0959  55  THR   A CB  
434  O  OG1 . THR   A 55  ? 0.2736 0.2749 0.6224 0.0633  -0.1237 0.0476  55  THR   A OG1 
435  C  CG2 . THR   A 55  ? 0.4220 0.2791 0.3567 0.1119  -0.0193 0.0753  55  THR   A CG2 
436  N  N   . SER   A 56  ? 0.1492 0.1665 0.2782 0.0339  -0.0248 0.0373  56  SER   A N   
437  C  CA  . SER   A 56  ? 0.1569 0.1478 0.2893 0.0302  -0.0108 -0.0043 56  SER   A CA  
438  C  C   . SER   A 56  ? 0.1477 0.1970 0.2889 0.0472  -0.0069 0.0217  56  SER   A C   
439  O  O   . SER   A 56  ? 0.2213 0.1899 0.3216 0.0463  -0.0640 0.0262  56  SER   A O   
440  C  CB  . SER   A 56  ? 0.2644 0.1612 0.2677 0.0032  -0.0780 -0.0053 56  SER   A CB  
441  O  OG  . SER   A 56  ? 0.1877 0.2220 0.3183 -0.0545 -0.0974 0.0304  56  SER   A OG  
442  N  N   . LEU   A 57  ? 0.1442 0.1777 0.2864 0.0346  -0.0015 0.0228  57  LEU   A N   
443  C  CA  . LEU   A 57  ? 0.1932 0.1691 0.3365 -0.0082 0.0216  0.0418  57  LEU   A CA  
444  C  C   . LEU   A 57  ? 0.1659 0.2409 0.2346 -0.0222 -0.0150 0.0333  57  LEU   A C   
445  O  O   . LEU   A 57  ? 0.1884 0.2081 0.2472 -0.0046 -0.0443 0.0419  57  LEU   A O   
446  C  CB  . LEU   A 57  ? 0.2512 0.1321 0.4265 -0.0179 0.0057  0.0350  57  LEU   A CB  
447  C  CG  . LEU   A 57  ? 0.2971 0.2003 0.4279 -0.0256 0.0060  -0.0138 57  LEU   A CG  
448  C  CD1 . LEU   A 57  ? 0.3238 0.2495 0.6294 -0.1512 0.0211  0.0751  57  LEU   A CD1 
449  C  CD2 . LEU   A 57  ? 0.5028 0.1913 0.5831 0.1156  -0.0402 0.1028  57  LEU   A CD2 
450  N  N   . ARG   A 58  ? 0.1770 0.1553 0.2660 -0.0299 -0.0274 0.0196  58  ARG   A N   
451  C  CA  . ARG   A 58  ? 0.1490 0.1493 0.2490 -0.0251 -0.0076 0.0686  58  ARG   A CA  
452  C  C   . ARG   A 58  ? 0.1524 0.1281 0.2355 -0.0398 -0.0205 0.0369  58  ARG   A C   
453  O  O   . ARG   A 58  ? 0.1330 0.1615 0.2493 0.0179  -0.0047 0.0153  58  ARG   A O   
454  C  CB  . ARG   A 58  ? 0.0836 0.1798 0.2956 -0.0166 -0.0258 -0.0078 58  ARG   A CB  
455  C  CG  . ARG   A 58  ? 0.1680 0.1964 0.2372 -0.0199 -0.0163 0.0242  58  ARG   A CG  
456  C  CD  . ARG   A 58  ? 0.1468 0.2820 0.3016 -0.0583 -0.0214 0.0649  58  ARG   A CD  
457  N  NE  . ARG   A 58  ? 0.1352 0.1321 0.3304 0.0051  -0.0286 0.0397  58  ARG   A NE  
458  C  CZ  . ARG   A 58  ? 0.1506 0.2068 0.2721 -0.0348 -0.0326 -0.0018 58  ARG   A CZ  
459  N  NH1 . ARG   A 58  ? 0.1655 0.2071 0.3208 -0.0341 -0.0077 -0.0078 58  ARG   A NH1 
460  N  NH2 . ARG   A 58  ? 0.1571 0.1539 0.2963 -0.0145 -0.0331 0.0111  58  ARG   A NH2 
461  N  N   . ILE   A 59  ? 0.1287 0.1651 0.2570 -0.0008 -0.0570 0.0147  59  ILE   A N   
462  C  CA  . ILE   A 59  ? 0.1109 0.1380 0.2567 -0.0221 -0.0537 0.0106  59  ILE   A CA  
463  C  C   . ILE   A 59  ? 0.1405 0.1269 0.1874 -0.0044 -0.0188 -0.0190 59  ILE   A C   
464  O  O   . ILE   A 59  ? 0.1454 0.1870 0.2059 -0.0013 -0.0143 -0.0047 59  ILE   A O   
465  C  CB  . ILE   A 59  ? 0.1359 0.1251 0.2006 -0.0264 -0.0578 0.0259  59  ILE   A CB  
466  C  CG1 . ILE   A 59  ? 0.1450 0.1285 0.2172 -0.0317 -0.0811 0.0324  59  ILE   A CG1 
467  C  CG2 . ILE   A 59  ? 0.1542 0.1601 0.2046 0.0132  -0.0541 0.0192  59  ILE   A CG2 
468  C  CD1 . ILE   A 59  ? 0.2365 0.1456 0.2357 -0.0756 -0.0688 0.0109  59  ILE   A CD1 
469  N  N   . LEU   A 60  ? 0.1553 0.1125 0.2032 -0.0080 -0.0332 -0.0078 60  LEU   A N   
470  C  CA  . LEU   A 60  ? 0.1500 0.0524 0.2714 -0.0078 -0.0084 0.0212  60  LEU   A CA  
471  C  C   . LEU   A 60  ? 0.1465 0.0702 0.2238 -0.0111 -0.0412 -0.0032 60  LEU   A C   
472  O  O   . LEU   A 60  ? 0.1626 0.1375 0.2292 0.0237  -0.0087 0.0049  60  LEU   A O   
473  C  CB  . LEU   A 60  ? 0.1321 0.0953 0.2488 -0.0018 -0.0326 -0.0032 60  LEU   A CB  
474  C  CG  . LEU   A 60  ? 0.1344 0.1116 0.2062 0.0089  -0.0342 -0.0032 60  LEU   A CG  
475  C  CD1 . LEU   A 60  ? 0.1360 0.1798 0.2121 -0.0256 -0.0303 -0.0274 60  LEU   A CD1 
476  C  CD2 . LEU   A 60  ? 0.1521 0.1028 0.2852 -0.0047 -0.0471 -0.0216 60  LEU   A CD2 
477  N  N   . ASN   A 61  ? 0.1574 0.1122 0.2171 -0.0316 -0.0204 -0.0015 61  ASN   A N   
478  C  CA  . ASN   A 61  ? 0.1506 0.1822 0.2311 -0.0019 -0.0496 -0.0021 61  ASN   A CA  
479  C  C   . ASN   A 61  ? 0.1601 0.1533 0.2253 0.0037  -0.0337 -0.0032 61  ASN   A C   
480  O  O   . ASN   A 61  ? 0.1722 0.1298 0.2499 0.0044  -0.0324 0.0083  61  ASN   A O   
481  C  CB  . ASN   A 61  ? 0.1579 0.2100 0.2406 0.0307  -0.0226 0.0040  61  ASN   A CB  
482  C  CG  . ASN   A 61  ? 0.1964 0.1544 0.2279 0.0114  -0.0476 -0.0035 61  ASN   A CG  
483  O  OD1 . ASN   A 61  ? 0.2136 0.1363 0.2416 -0.0073 -0.0416 0.0093  61  ASN   A OD1 
484  N  ND2 . ASN   A 61  ? 0.1619 0.1373 0.2555 -0.0337 -0.0534 0.0105  61  ASN   A ND2 
485  N  N   . ASN   A 62  ? 0.2178 0.0598 0.2275 -0.0131 -0.0564 -0.0063 62  ASN   A N   
486  C  CA  . ASN   A 62  ? 0.2156 0.1319 0.2364 -0.0611 -0.0464 0.0021  62  ASN   A CA  
487  C  C   . ASN   A 62  ? 0.2052 0.2003 0.2444 -0.0479 -0.0263 -0.0218 62  ASN   A C   
488  O  O   . ASN   A 62  ? 0.2588 0.1690 0.2920 -0.0848 -0.0253 -0.0168 62  ASN   A O   
489  C  CB  . ASN   A 62  ? 0.2657 0.1538 0.2570 -0.0610 -0.0370 -0.0096 62  ASN   A CB  
490  C  CG  . ASN   A 62  ? 0.2142 0.1892 0.2355 0.0284  -0.0239 0.0072  62  ASN   A CG  
491  O  OD1 . ASN   A 62  ? 0.1727 0.1348 0.3348 0.0023  0.0175  -0.0029 62  ASN   A OD1 
492  N  ND2 . ASN   A 62  ? 0.2402 0.1896 0.3130 0.0072  -0.0183 -0.0156 62  ASN   A ND2 
493  N  N   . GLY   A 63  ? 0.1447 0.1827 0.2055 0.0153  0.0063  0.0038  63  GLY   A N   
494  C  CA  . GLY   A 63  ? 0.1364 0.1644 0.2669 -0.0047 0.0020  0.0398  63  GLY   A CA  
495  C  C   . GLY   A 63  ? 0.1005 0.1263 0.2328 -0.0168 -0.0145 0.0076  63  GLY   A C   
496  O  O   . GLY   A 63  ? 0.1446 0.1461 0.3085 0.0255  0.0223  0.0063  63  GLY   A O   
497  N  N   . HIS   A 64  ? 0.1427 0.1342 0.2136 -0.0331 0.0015  0.0010  64  HIS   A N   
498  C  CA  . HIS   A 64  ? 0.1167 0.1880 0.2181 0.0087  -0.0139 0.0153  64  HIS   A CA  
499  C  C   . HIS   A 64  ? 0.1496 0.1332 0.2463 -0.0184 -0.0146 0.0111  64  HIS   A C   
500  O  O   . HIS   A 64  ? 0.0930 0.1520 0.2749 -0.0080 -0.0392 0.0370  64  HIS   A O   
501  C  CB  . HIS   A 64  ? 0.1556 0.2499 0.2488 -0.0566 -0.0275 -0.0108 64  HIS   A CB  
502  C  CG  . HIS   A 64  ? 0.2150 0.3449 0.3152 -0.1181 0.0136  -0.0137 64  HIS   A CG  
503  N  ND1 . HIS   A 64  ? 0.2651 0.3777 0.3328 -0.0914 -0.0474 0.0378  64  HIS   A ND1 
504  C  CD2 . HIS   A 64  ? 0.2402 0.3601 0.2750 -0.0647 -0.0296 0.0097  64  HIS   A CD2 
505  C  CE1 . HIS   A 64  ? 0.2513 0.3340 0.2637 -0.0586 -0.0212 -0.0209 64  HIS   A CE1 
506  N  NE2 . HIS   A 64  ? 0.2594 0.3504 0.3227 -0.0873 -0.0379 -0.0016 64  HIS   A NE2 
507  N  N   . ALA   A 65  ? 0.1285 0.1005 0.2701 -0.0287 -0.0175 -0.0145 65  ALA   A N   
508  C  CA  . ALA   A 65  ? 0.1195 0.1867 0.2088 -0.0102 -0.0467 0.0146  65  ALA   A CA  
509  C  C   . ALA   A 65  ? 0.1281 0.1684 0.1775 0.0205  -0.0132 0.0067  65  ALA   A C   
510  O  O   . ALA   A 65  ? 0.1416 0.1801 0.2355 -0.0079 -0.0212 0.0237  65  ALA   A O   
511  C  CB  . ALA   A 65  ? 0.0794 0.1393 0.2262 0.0333  -0.0561 0.0051  65  ALA   A CB  
512  N  N   . PHE   A 66  ? 0.1221 0.1141 0.2372 0.0106  -0.0164 0.0248  66  PHE   A N   
513  C  CA  . PHE   A 66  ? 0.1701 0.1575 0.2080 0.0342  -0.0419 0.0038  66  PHE   A CA  
514  C  C   . PHE   A 66  ? 0.1549 0.1170 0.2398 0.0103  -0.0089 0.0132  66  PHE   A C   
515  O  O   . PHE   A 66  ? 0.1101 0.1533 0.2120 -0.0104 -0.0384 -0.0053 66  PHE   A O   
516  C  CB  . PHE   A 66  ? 0.1768 0.1371 0.2269 0.0107  -0.0613 0.0181  66  PHE   A CB  
517  C  CG  . PHE   A 66  ? 0.1860 0.1102 0.2244 0.0242  -0.0239 -0.0089 66  PHE   A CG  
518  C  CD1 . PHE   A 66  ? 0.1294 0.2480 0.2188 -0.0086 -0.0624 -0.0185 66  PHE   A CD1 
519  C  CD2 . PHE   A 66  ? 0.1899 0.1091 0.2461 0.0121  -0.0277 0.0164  66  PHE   A CD2 
520  C  CE1 . PHE   A 66  ? 0.1673 0.1564 0.2393 0.0280  -0.0639 0.0096  66  PHE   A CE1 
521  C  CE2 . PHE   A 66  ? 0.1732 0.1511 0.2384 -0.0149 -0.0466 -0.0150 66  PHE   A CE2 
522  C  CZ  . PHE   A 66  ? 0.2030 0.1407 0.2321 0.0052  -0.0519 -0.0277 66  PHE   A CZ  
523  N  N   . ASN   A 67  ? 0.1183 0.1104 0.2438 0.0079  -0.0337 0.0177  67  ASN   A N   
524  C  CA  . ASN   A 67  ? 0.1414 0.0912 0.2429 0.0070  -0.0510 -0.0037 67  ASN   A CA  
525  C  C   . ASN   A 67  ? 0.1485 0.0976 0.2187 0.0002  -0.0295 -0.0094 67  ASN   A C   
526  O  O   . ASN   A 67  ? 0.1131 0.1811 0.2068 0.0055  -0.0380 0.0163  67  ASN   A O   
527  C  CB  . ASN   A 67  ? 0.1524 0.0741 0.2187 0.0067  -0.0569 0.0167  67  ASN   A CB  
528  C  CG  . ASN   A 67  ? 0.1249 0.1162 0.2217 -0.0124 -0.0392 0.0019  67  ASN   A CG  
529  O  OD1 . ASN   A 67  ? 0.1781 0.1249 0.2515 -0.0257 -0.0337 0.0182  67  ASN   A OD1 
530  N  ND2 . ASN   A 67  ? 0.2018 0.1381 0.3219 -0.0665 -0.0309 -0.0183 67  ASN   A ND2 
531  N  N   . VAL   A 68  ? 0.1014 0.0684 0.2727 0.0046  -0.0335 0.0143  68  VAL   A N   
532  C  CA  . VAL   A 68  ? 0.1028 0.1587 0.2341 0.0245  -0.0401 0.0027  68  VAL   A CA  
533  C  C   . VAL   A 68  ? 0.1034 0.1664 0.1959 0.0030  -0.0286 0.0238  68  VAL   A C   
534  O  O   . VAL   A 68  ? 0.1465 0.0939 0.1998 0.0323  -0.0341 0.0184  68  VAL   A O   
535  C  CB  . VAL   A 68  ? 0.1228 0.1217 0.2837 0.0067  -0.0694 -0.0082 68  VAL   A CB  
536  C  CG1 . VAL   A 68  ? 0.0925 0.1892 0.2524 -0.0085 -0.0734 0.0083  68  VAL   A CG1 
537  C  CG2 . VAL   A 68  ? 0.1752 0.1407 0.2628 -0.0219 -0.0549 -0.0259 68  VAL   A CG2 
538  N  N   . GLU   A 69  ? 0.1536 0.1053 0.2488 0.0013  -0.0359 0.0234  69  GLU   A N   
539  C  CA  . GLU   A 69  ? 0.1386 0.1183 0.2933 0.0242  -0.0025 -0.0010 69  GLU   A CA  
540  C  C   . GLU   A 69  ? 0.1561 0.1141 0.2599 0.0308  -0.0505 0.0258  69  GLU   A C   
541  O  O   . GLU   A 69  ? 0.1906 0.1183 0.2868 0.0504  -0.0652 0.0158  69  GLU   A O   
542  C  CB  . GLU   A 69  ? 0.0835 0.1926 0.2687 0.0183  -0.0258 0.0041  69  GLU   A CB  
543  C  CG  . GLU   A 69  ? 0.1118 0.1524 0.2508 0.0441  -0.0046 0.0303  69  GLU   A CG  
544  C  CD  . GLU   A 69  ? 0.1644 0.1368 0.2152 -0.0212 -0.0110 -0.0050 69  GLU   A CD  
545  O  OE1 . GLU   A 69  ? 0.1830 0.1920 0.2452 -0.0174 -0.0163 0.0359  69  GLU   A OE1 
546  O  OE2 . GLU   A 69  ? 0.1456 0.1583 0.2614 -0.0228 -0.0294 0.0197  69  GLU   A OE2 
547  N  N   . PHE   A 70  ? 0.1043 0.1870 0.2466 0.0289  -0.0205 0.0041  70  PHE   A N   
548  C  CA  . PHE   A 70  ? 0.1276 0.0998 0.2371 0.0279  -0.0383 -0.0069 70  PHE   A CA  
549  C  C   . PHE   A 70  ? 0.1707 0.1106 0.2568 0.0011  -0.0517 -0.0050 70  PHE   A C   
550  O  O   . PHE   A 70  ? 0.1630 0.1447 0.3102 -0.0234 -0.0529 0.0550  70  PHE   A O   
551  C  CB  . PHE   A 70  ? 0.1912 0.1190 0.2287 0.0206  -0.0227 -0.0118 70  PHE   A CB  
552  C  CG  . PHE   A 70  ? 0.1508 0.1238 0.2441 0.0258  -0.0372 0.0024  70  PHE   A CG  
553  C  CD1 . PHE   A 70  ? 0.2401 0.1337 0.2575 0.0610  -0.0270 0.0110  70  PHE   A CD1 
554  C  CD2 . PHE   A 70  ? 0.1518 0.1506 0.2814 -0.0037 -0.0290 -0.0419 70  PHE   A CD2 
555  C  CE1 . PHE   A 70  ? 0.1788 0.1698 0.2463 0.0190  -0.0406 0.0047  70  PHE   A CE1 
556  C  CE2 . PHE   A 70  ? 0.1811 0.1362 0.2357 -0.0016 -0.0381 0.0005  70  PHE   A CE2 
557  C  CZ  . PHE   A 70  ? 0.1632 0.1682 0.2744 0.0080  -0.0093 0.0413  70  PHE   A CZ  
558  N  N   . ASP   A 71  ? 0.1752 0.1262 0.3407 0.0131  -0.0431 0.0120  71  ASP   A N   
559  C  CA  . ASP   A 71  ? 0.1870 0.1240 0.3343 0.0158  -0.0324 0.0256  71  ASP   A CA  
560  C  C   . ASP   A 71  ? 0.2125 0.1158 0.3571 0.0233  -0.0122 0.0083  71  ASP   A C   
561  O  O   . ASP   A 71  ? 0.2361 0.1738 0.4752 -0.0206 0.0623  -0.0027 71  ASP   A O   
562  C  CB  . ASP   A 71  ? 0.2822 0.1022 0.4170 0.0653  -0.1094 0.0060  71  ASP   A CB  
563  C  CG  . ASP   A 71  ? 0.2584 0.0944 0.4885 0.0398  -0.1637 0.0089  71  ASP   A CG  
564  O  OD1 . ASP   A 71  ? 0.2903 0.1738 0.4960 -0.0436 -0.1260 0.0291  71  ASP   A OD1 
565  O  OD2 . ASP   A 71  ? 0.2883 0.2203 0.7871 0.0427  -0.2329 0.1337  71  ASP   A OD2 
566  N  N   . ASP   A 72  ? 0.1985 0.1138 0.3585 0.0152  -0.0253 0.0361  72  ASP   A N   
567  C  CA  . ASP   A 72  ? 0.2079 0.0861 0.3524 -0.0190 -0.0524 0.0200  72  ASP   A CA  
568  C  C   . ASP   A 72  ? 0.3445 0.0950 0.4358 -0.0506 -0.0624 0.0098  72  ASP   A C   
569  O  O   . ASP   A 72  ? 0.4137 0.1283 0.4768 -0.0985 -0.0919 -0.0033 72  ASP   A O   
570  C  CB  . ASP   A 72  ? 0.2176 0.1801 0.4097 -0.0502 -0.0554 0.0729  72  ASP   A CB  
571  C  CG  . ASP   A 72  ? 0.2509 0.2190 0.4275 -0.0647 -0.0529 0.1289  72  ASP   A CG  
572  O  OD1 . ASP   A 72  ? 0.2451 0.4697 0.3798 -0.0240 -0.0910 0.1665  72  ASP   A OD1 
573  O  OD2 . ASP   A 72  ? 0.2463 0.3507 0.3270 -0.0179 -0.0530 0.0301  72  ASP   A OD2 
574  N  N   . SER   A 73  ? 0.2726 0.0903 0.4109 -0.0166 0.0064  0.0016  73  SER   A N   
575  C  CA  . SER   A 73  ? 0.3977 0.0928 0.4540 -0.0358 0.0003  -0.0218 73  SER   A CA  
576  C  C   . SER   A 73  ? 0.5033 0.1450 0.4957 -0.0339 0.1253  -0.0533 73  SER   A C   
577  O  O   . SER   A 73  ? 0.5280 0.1289 0.4734 -0.0149 -0.0225 -0.0255 73  SER   A O   
578  C  CB  . SER   A 73  ? 0.3565 0.2271 0.4434 -0.0526 0.0345  0.0017  73  SER   A CB  
579  O  OG  . SER   A 73  ? 0.3397 0.1339 0.4606 0.0765  -0.0104 0.0781  73  SER   A OG  
580  N  N   . GLN   A 74  ? 0.4133 0.1260 0.6452 -0.0108 0.0597  0.0178  74  GLN   A N   
581  C  CA  . GLN   A 74  ? 0.5042 0.2846 0.5204 0.0428  0.0859  -0.0318 74  GLN   A CA  
582  C  C   . GLN   A 74  ? 0.4089 0.2570 0.3883 -0.0178 -0.0557 -0.0675 74  GLN   A C   
583  O  O   . GLN   A 74  ? 0.3303 0.2096 0.3458 -0.0392 -0.0324 0.0237  74  GLN   A O   
584  C  CB  . GLN   A 74  ? 0.3955 0.3426 0.5856 0.2193  0.0818  0.1247  74  GLN   A CB  
585  C  CG  . GLN   A 74  ? 0.3609 0.4610 0.6501 0.0774  0.1930  0.1902  74  GLN   A CG  
586  C  CD  . GLN   A 74  ? 0.4334 0.7224 0.9533 -0.0812 -0.3296 0.2339  74  GLN   A CD  
587  O  OE1 . GLN   A 74  ? 0.3065 0.4558 1.1591 0.0663  -0.1742 0.2674  74  GLN   A OE1 
588  N  NE2 . GLN   A 74  ? 0.5201 0.7398 1.0455 -0.1114 -0.1889 0.2784  74  GLN   A NE2 
589  N  N   . ASP   A 75  ? 0.4720 0.3996 0.4616 -0.0571 0.0197  -0.0678 75  ASP   A N   
590  C  CA  . ASP   A 75  ? 0.2596 0.3782 0.5642 -0.1559 0.0084  -0.0675 75  ASP   A CA  
591  C  C   . ASP   A 75  ? 0.2402 0.3649 0.6240 -0.0501 -0.0851 -0.1071 75  ASP   A C   
592  O  O   . ASP   A 75  ? 0.2190 0.9055 0.7889 -0.0356 -0.0357 -0.0620 75  ASP   A O   
593  C  CB  . ASP   A 75  ? 0.6179 0.7076 0.6156 0.1392  -0.0177 -0.1664 75  ASP   A CB  
594  C  CG  . ASP   A 75  ? 1.1221 0.2215 0.7231 0.3859  -0.2071 0.1637  75  ASP   A CG  
595  O  OD1 . ASP   A 75  ? 0.4321 0.9394 0.3569 0.3717  -0.1324 -0.0143 75  ASP   A OD1 
596  O  OD2 . ASP   A 75  ? 0.6788 0.6778 0.9253 0.1601  0.0392  -0.1760 75  ASP   A OD2 
597  N  N   . LYS   A 76  ? 0.4071 0.2301 0.4077 0.0032  -0.1893 0.0161  76  LYS   A N   
598  C  CA  . LYS   A 76  ? 0.2461 0.1887 0.5946 -0.0489 -0.1312 0.0536  76  LYS   A CA  
599  C  C   . LYS   A 76  ? 0.2387 0.3213 0.6262 -0.0523 -0.0496 0.1434  76  LYS   A C   
600  O  O   . LYS   A 76  ? 0.5366 0.5874 0.9097 -0.2457 0.1401  0.1826  76  LYS   A O   
601  C  CB  . LYS   A 76  ? 0.4965 0.1632 0.5642 -0.0214 -0.2191 0.0857  76  LYS   A CB  
602  C  CG  . LYS   A 76  ? 0.8440 0.0822 0.6057 0.0196  -0.1702 0.0921  76  LYS   A CG  
603  C  CD  . LYS   A 76  ? 0.4397 0.3849 0.7554 -0.1939 -0.1732 0.0266  76  LYS   A CD  
604  C  CE  . LYS   A 76  ? 0.6788 0.4480 0.7289 0.1979  -0.2552 -0.0017 76  LYS   A CE  
605  N  NZ  . LYS   A 76  ? 1.0549 0.5332 0.4549 -0.0526 -0.3082 0.1694  76  LYS   A NZ  
606  N  N   . ALA   A 77  ? 0.3069 0.2811 0.4725 -0.0080 -0.0999 0.1376  77  ALA   A N   
607  C  CA  . ALA   A 77  ? 0.2566 0.2289 0.3199 -0.0599 -0.0960 0.0341  77  ALA   A CA  
608  C  C   . ALA   A 77  ? 0.1665 0.2000 0.3188 -0.0400 -0.0623 0.0209  77  ALA   A C   
609  O  O   . ALA   A 77  ? 0.1684 0.3133 0.4729 -0.0836 -0.0323 -0.0323 77  ALA   A O   
610  C  CB  . ALA   A 77  ? 0.2860 0.2066 0.3535 -0.0634 -0.0812 -0.0179 77  ALA   A CB  
611  N  N   . VAL   A 78  ? 0.2610 0.1603 0.2774 -0.0343 -0.0723 0.0405  78  VAL   A N   
612  C  CA  . VAL   A 78  ? 0.2670 0.2063 0.2751 0.0307  -0.0671 0.0001  78  VAL   A CA  
613  C  C   . VAL   A 78  ? 0.2323 0.2494 0.3324 -0.0033 -0.0529 0.0255  78  VAL   A C   
614  O  O   . VAL   A 78  ? 0.2260 0.1481 0.3421 0.0354  -0.1009 0.0374  78  VAL   A O   
615  C  CB  . VAL   A 78  ? 0.2831 0.2285 0.3764 0.0458  -0.0003 -0.0051 78  VAL   A CB  
616  C  CG1 . VAL   A 78  ? 0.4894 0.2258 0.4441 0.1227  -0.0917 0.0494  78  VAL   A CG1 
617  C  CG2 . VAL   A 78  ? 0.2436 0.2254 0.4005 0.0315  -0.0041 -0.0192 78  VAL   A CG2 
618  N  N   . LEU   A 79  ? 0.1822 0.1226 0.2939 0.0060  -0.0072 -0.0018 79  LEU   A N   
619  C  CA  . LEU   A 79  ? 0.0944 0.2272 0.2816 0.0098  -0.0409 0.0184  79  LEU   A CA  
620  C  C   . LEU   A 79  ? 0.1278 0.2097 0.2726 -0.0243 -0.0366 0.0089  79  LEU   A C   
621  O  O   . LEU   A 79  ? 0.1632 0.1650 0.2957 -0.0261 -0.0300 -0.0300 79  LEU   A O   
622  C  CB  . LEU   A 79  ? 0.0847 0.1770 0.4014 -0.0003 -0.0685 0.0546  79  LEU   A CB  
623  C  CG  . LEU   A 79  ? 0.1280 0.1696 0.3720 -0.0078 -0.0542 0.0175  79  LEU   A CG  
624  C  CD1 . LEU   A 79  ? 0.1319 0.1571 0.4654 -0.0068 -0.0229 0.0365  79  LEU   A CD1 
625  C  CD2 . LEU   A 79  ? 0.1568 0.1539 0.3347 0.0364  -0.0305 0.0375  79  LEU   A CD2 
626  N  N   . LYS   A 80  ? 0.1194 0.1981 0.3025 -0.0087 -0.0353 -0.0109 80  LYS   A N   
627  C  CA  . LYS   A 80  ? 0.1246 0.2409 0.3045 0.0032  -0.0124 0.0004  80  LYS   A CA  
628  C  C   . LYS   A 80  ? 0.1747 0.1653 0.2922 0.0044  -0.0162 -0.0243 80  LYS   A C   
629  O  O   . LYS   A 80  ? 0.1332 0.1373 0.3276 0.0048  -0.0494 0.0054  80  LYS   A O   
630  C  CB  . LYS   A 80  ? 0.2664 0.2468 0.3935 0.0544  0.0041  -0.0013 80  LYS   A CB  
631  C  CG  . LYS   A 80  ? 0.2812 0.2597 0.4081 0.0770  -0.0184 0.0245  80  LYS   A CG  
632  C  CD  . LYS   A 80  ? 0.2812 0.2776 0.5734 0.1238  -0.0510 0.0043  80  LYS   A CD  
633  N  N   . GLY   A 81  ? 0.1890 0.2298 0.2895 0.0372  0.0104  -0.0131 81  GLY   A N   
634  C  CA  . GLY   A 81  ? 0.1669 0.2323 0.3402 0.0806  -0.0248 0.0406  81  GLY   A CA  
635  C  C   . GLY   A 81  ? 0.1454 0.2319 0.3203 0.0721  0.0201  0.0788  81  GLY   A C   
636  O  O   . GLY   A 81  ? 0.1740 0.1661 0.3472 -0.0162 0.0312  0.0151  81  GLY   A O   
637  N  N   . GLY   A 82  ? 0.1510 0.1921 0.4766 0.0032  0.0043  0.0458  82  GLY   A N   
638  C  CA  . GLY   A 82  ? 0.2487 0.2528 0.3872 0.0356  -0.0542 0.0517  82  GLY   A CA  
639  C  C   . GLY   A 82  ? 0.1733 0.1898 0.3432 0.0399  0.0088  0.0337  82  GLY   A C   
640  O  O   . GLY   A 82  ? 0.2624 0.3139 0.4014 0.1437  0.0409  0.0155  82  GLY   A O   
641  N  N   . PRO   A 83  ? 0.1867 0.2412 0.3538 0.0605  0.0225  -0.0111 83  PRO   A N   
642  C  CA  . PRO   A 83  ? 0.2549 0.1043 0.3370 0.0730  0.0161  0.0189  83  PRO   A CA  
643  C  C   . PRO   A 83  ? 0.2812 0.1285 0.3146 0.0183  0.0026  0.0020  83  PRO   A C   
644  O  O   . PRO   A 83  ? 0.2588 0.3302 0.3139 0.0607  -0.0345 -0.0252 83  PRO   A O   
645  C  CB  . PRO   A 83  ? 0.1874 0.2684 0.2988 0.0840  -0.0050 0.0096  83  PRO   A CB  
646  C  CG  . PRO   A 83  ? 0.1547 0.1224 0.3025 0.0212  -0.0280 -0.0145 83  PRO   A CG  
647  C  CD  . PRO   A 83  ? 0.1281 0.1711 0.3152 0.0298  0.0024  0.0242  83  PRO   A CD  
648  N  N   . LEU   A 84  ? 0.2564 0.1903 0.2840 0.0737  0.0411  0.0163  84  LEU   A N   
649  C  CA  . LEU   A 84  ? 0.1910 0.1194 0.2877 0.0398  -0.0220 -0.0385 84  LEU   A CA  
650  C  C   . LEU   A 84  ? 0.1859 0.1353 0.3296 0.0211  0.0221  -0.0547 84  LEU   A C   
651  O  O   . LEU   A 84  ? 0.1806 0.2712 0.4036 0.0278  -0.0034 -0.1097 84  LEU   A O   
652  C  CB  . LEU   A 84  ? 0.1641 0.1192 0.2736 0.0555  -0.0044 -0.0399 84  LEU   A CB  
653  C  CG  . LEU   A 84  ? 0.0960 0.1159 0.2766 0.0422  -0.0168 -0.0372 84  LEU   A CG  
654  C  CD1 . LEU   A 84  ? 0.1931 0.0996 0.2864 0.0386  -0.0398 -0.0604 84  LEU   A CD1 
655  C  CD2 . LEU   A 84  ? 0.0937 0.2075 0.3304 0.0216  -0.0064 -0.0618 84  LEU   A CD2 
656  N  N   . ASP   A 85  ? 0.2240 0.1288 0.4070 0.0035  -0.0136 -0.0646 85  ASP   A N   
657  C  CA  . ASP   A 85  ? 0.3007 0.1271 0.4441 0.0009  0.0151  -0.0798 85  ASP   A CA  
658  C  C   . ASP   A 85  ? 0.2619 0.0838 0.5472 -0.0537 -0.0248 -0.0218 85  ASP   A C   
659  O  O   . ASP   A 85  ? 0.3810 0.3568 0.6294 0.0944  0.0621  -0.0611 85  ASP   A O   
660  C  CB  . ASP   A 85  ? 0.5309 0.2928 0.5309 -0.0060 -0.0522 -0.2399 85  ASP   A CB  
661  C  CG  . ASP   A 85  ? 0.5699 0.5945 0.5756 0.0269  -0.1590 -0.2276 85  ASP   A CG  
662  O  OD1 . ASP   A 85  ? 0.6218 0.5571 0.7050 0.0401  -0.1026 -0.2347 85  ASP   A OD1 
663  O  OD2 . ASP   A 85  ? 0.2863 0.8065 0.8841 0.0850  -0.0690 -0.2249 85  ASP   A OD2 
664  N  N   . GLY   A 86  ? 0.2933 0.2846 0.5386 -0.0478 -0.1564 -0.0320 86  GLY   A N   
665  C  CA  . GLY   A 86  ? 0.4013 0.3003 0.4006 -0.1219 -0.0087 -0.0784 86  GLY   A CA  
666  C  C   . GLY   A 86  ? 0.4358 0.2665 0.3170 -0.1111 -0.0516 0.0000  86  GLY   A C   
667  O  O   . GLY   A 86  ? 0.4357 0.2790 0.3419 -0.1393 -0.0321 -0.0094 86  GLY   A O   
668  N  N   . THR   A 87  ? 0.1898 0.2540 0.3039 0.0825  0.0077  0.0079  87  THR   A N   
669  C  CA  . THR   A 87  ? 0.2359 0.2725 0.3091 0.0981  -0.0048 0.0044  87  THR   A CA  
670  C  C   . THR   A 87  ? 0.1725 0.1604 0.3080 0.0152  -0.0128 -0.0006 87  THR   A C   
671  O  O   . THR   A 87  ? 0.1553 0.1106 0.3605 0.0194  -0.0147 -0.0271 87  THR   A O   
672  C  CB  . THR   A 87  ? 0.2283 0.4832 0.3303 0.2708  -0.0366 -0.0197 87  THR   A CB  
673  O  OG1 . THR   A 87  ? 0.2082 0.5648 0.5801 0.0949  -0.0381 -0.1489 87  THR   A OG1 
674  C  CG2 . THR   A 87  ? 0.3058 0.3353 0.3846 0.0530  -0.1164 0.0438  87  THR   A CG2 
675  N  N   . TYR   A 88  ? 0.1028 0.1847 0.3555 0.0401  -0.0232 -0.0389 88  TYR   A N   
676  C  CA  . TYR   A 88  ? 0.0951 0.1362 0.2839 0.0276  -0.0435 0.0010  88  TYR   A CA  
677  C  C   . TYR   A 88  ? 0.1323 0.1228 0.2793 0.0158  -0.0562 0.0078  88  TYR   A C   
678  O  O   . TYR   A 88  ? 0.1319 0.1822 0.3402 -0.0329 -0.0510 0.0172  88  TYR   A O   
679  C  CB  . TYR   A 88  ? 0.1075 0.1388 0.2545 0.0215  -0.0389 0.0102  88  TYR   A CB  
680  C  CG  . TYR   A 88  ? 0.1145 0.1288 0.2549 0.0150  -0.0406 0.0024  88  TYR   A CG  
681  C  CD1 . TYR   A 88  ? 0.1690 0.1134 0.2261 0.0290  -0.0419 0.0130  88  TYR   A CD1 
682  C  CD2 . TYR   A 88  ? 0.1093 0.0890 0.2749 0.0252  -0.0407 0.0135  88  TYR   A CD2 
683  C  CE1 . TYR   A 88  ? 0.1088 0.1417 0.2587 0.0261  -0.0214 0.0095  88  TYR   A CE1 
684  C  CE2 . TYR   A 88  ? 0.1640 0.0777 0.2561 -0.0155 -0.0198 -0.0122 88  TYR   A CE2 
685  C  CZ  . TYR   A 88  ? 0.1127 0.0824 0.2694 0.0113  -0.0312 -0.0305 88  TYR   A CZ  
686  O  OH  . TYR   A 88  ? 0.2304 0.1212 0.2405 -0.0277 -0.0249 0.0013  88  TYR   A OH  
687  N  N   . ARG   A 89  ? 0.1587 0.0912 0.2521 0.0489  -0.0221 -0.0377 89  ARG   A N   
688  C  CA  . ARG   A 89  ? 0.1550 0.0897 0.2681 0.0354  -0.0546 -0.0043 89  ARG   A CA  
689  C  C   . ARG   A 89  ? 0.1084 0.1230 0.2523 0.0316  -0.0232 -0.0111 89  ARG   A C   
690  O  O   . ARG   A 89  ? 0.0980 0.1136 0.2550 -0.0065 -0.0156 -0.0110 89  ARG   A O   
691  C  CB  . ARG   A 89  ? 0.2264 0.1409 0.3300 0.0048  -0.1017 0.0571  89  ARG   A CB  
692  C  CG  . ARG   A 89  ? 0.3793 0.2007 0.3352 0.0016  -0.1404 0.0819  89  ARG   A CG  
693  C  CD  . ARG   A 89  ? 0.3075 0.1132 0.4883 0.1220  -0.0652 0.0332  89  ARG   A CD  
694  N  NE  . ARG   A 89  ? 0.4118 0.1528 0.2976 0.1093  -0.0760 0.0375  89  ARG   A NE  
695  C  CZ  . ARG   A 89  ? 0.3802 0.1525 0.3764 0.0646  -0.0105 0.0641  89  ARG   A CZ  
696  N  NH1 . ARG   A 89  ? 0.3303 0.3054 0.4867 0.0269  -0.0120 0.1578  89  ARG   A NH1 
697  N  NH2 . ARG   A 89  ? 0.3333 0.3945 0.4032 0.1500  0.0088  0.0095  89  ARG   A NH2 
698  N  N   . LEU   A 90  ? 0.2118 0.0642 0.2699 0.0144  -0.0487 0.0029  90  LEU   A N   
699  C  CA  . LEU   A 90  ? 0.1124 0.1392 0.2494 -0.0238 -0.0201 -0.0163 90  LEU   A CA  
700  C  C   . LEU   A 90  ? 0.1450 0.1084 0.2161 0.0057  -0.0172 -0.0089 90  LEU   A C   
701  O  O   . LEU   A 90  ? 0.1806 0.1874 0.2610 0.0108  -0.0279 0.0446  90  LEU   A O   
702  C  CB  . LEU   A 90  ? 0.1594 0.1174 0.2667 -0.0425 -0.0410 -0.0223 90  LEU   A CB  
703  C  CG  . LEU   A 90  ? 0.1507 0.1251 0.2459 -0.0306 -0.0650 -0.0150 90  LEU   A CG  
704  C  CD1 . LEU   A 90  ? 0.1855 0.1162 0.3007 0.0042  -0.0319 0.0033  90  LEU   A CD1 
705  C  CD2 . LEU   A 90  ? 0.1295 0.1605 0.2724 -0.0116 -0.0807 -0.0076 90  LEU   A CD2 
706  N  N   . ILE   A 91  ? 0.1345 0.0734 0.2572 -0.0025 0.0046  -0.0043 91  ILE   A N   
707  C  CA  . ILE   A 91  ? 0.1551 0.1485 0.2272 0.0110  -0.0044 0.0132  91  ILE   A CA  
708  C  C   . ILE   A 91  ? 0.1946 0.1461 0.2240 0.0037  0.0077  0.0157  91  ILE   A C   
709  O  O   . ILE   A 91  ? 0.1673 0.1170 0.2389 0.0381  -0.0260 0.0002  91  ILE   A O   
710  C  CB  . ILE   A 91  ? 0.1985 0.1326 0.2576 -0.0414 -0.0107 0.0432  91  ILE   A CB  
711  C  CG1 . ILE   A 91  ? 0.2075 0.1154 0.2423 -0.0951 -0.0253 -0.0048 91  ILE   A CG1 
712  C  CG2 . ILE   A 91  ? 0.2114 0.1025 0.2746 -0.0095 0.0048  0.0480  91  ILE   A CG2 
713  C  CD1 . ILE   A 91  ? 0.2552 0.1975 0.2405 -0.1298 -0.0557 -0.0434 91  ILE   A CD1 
714  N  N   . GLN   A 92  ? 0.1037 0.1417 0.2284 -0.0062 -0.0317 0.0111  92  GLN   A N   
715  C  CA  . GLN   A 92  ? 0.1738 0.1314 0.2122 0.0076  -0.0010 0.0336  92  GLN   A CA  
716  C  C   . GLN   A 92  ? 0.1216 0.1101 0.1988 -0.0174 -0.0270 0.0083  92  GLN   A C   
717  O  O   . GLN   A 92  ? 0.1605 0.1109 0.2122 -0.0120 -0.0225 0.0130  92  GLN   A O   
718  C  CB  . GLN   A 92  ? 0.1497 0.1502 0.2555 -0.0414 -0.0286 0.0323  92  GLN   A CB  
719  C  CG  . GLN   A 92  ? 0.1781 0.1122 0.2949 0.0354  -0.0666 0.0108  92  GLN   A CG  
720  C  CD  . GLN   A 92  ? 0.1536 0.0892 0.2383 0.0000  -0.0125 0.0527  92  GLN   A CD  
721  O  OE1 . GLN   A 92  ? 0.1210 0.1119 0.2579 -0.0121 -0.0207 0.0334  92  GLN   A OE1 
722  N  NE2 . GLN   A 92  ? 0.1549 0.1969 0.3314 0.0430  0.0085  0.0081  92  GLN   A NE2 
723  N  N   . PHE   A 93  ? 0.1375 0.0966 0.2104 0.0178  -0.0593 0.0136  93  PHE   A N   
724  C  CA  . PHE   A 93  ? 0.1714 0.1027 0.2369 -0.0034 -0.0078 0.0412  93  PHE   A CA  
725  C  C   . PHE   A 93  ? 0.0973 0.1316 0.1978 -0.0489 -0.0458 0.0275  93  PHE   A C   
726  O  O   . PHE   A 93  ? 0.1192 0.1091 0.1956 0.0156  -0.0511 0.0223  93  PHE   A O   
727  C  CB  . PHE   A 93  ? 0.1244 0.1132 0.2156 -0.0005 -0.0522 -0.0020 93  PHE   A CB  
728  C  CG  . PHE   A 93  ? 0.1097 0.0939 0.2451 0.0077  -0.0433 -0.0196 93  PHE   A CG  
729  C  CD1 . PHE   A 93  ? 0.1273 0.1102 0.2219 -0.0044 -0.0445 -0.0266 93  PHE   A CD1 
730  C  CD2 . PHE   A 93  ? 0.1165 0.2064 0.1877 0.0171  -0.0545 0.0223  93  PHE   A CD2 
731  C  CE1 . PHE   A 93  ? 0.1389 0.1004 0.2437 -0.0108 -0.0797 -0.0044 93  PHE   A CE1 
732  C  CE2 . PHE   A 93  ? 0.1752 0.1306 0.2222 -0.0182 -0.0454 -0.0163 93  PHE   A CE2 
733  C  CZ  . PHE   A 93  ? 0.1073 0.1313 0.2311 -0.0057 -0.0339 -0.0010 93  PHE   A CZ  
734  N  N   . HIS   A 94  ? 0.1405 0.0824 0.2278 -0.0059 -0.0290 0.0097  94  HIS   A N   
735  C  CA  . HIS   A 94  ? 0.1140 0.0987 0.2215 -0.0443 -0.0022 -0.0024 94  HIS   A CA  
736  C  C   . HIS   A 94  ? 0.1039 0.1080 0.1829 -0.0333 -0.0429 -0.0052 94  HIS   A C   
737  O  O   . HIS   A 94  ? 0.1562 0.1210 0.2124 0.0288  -0.0311 0.0255  94  HIS   A O   
738  C  CB  . HIS   A 94  ? 0.0989 0.1399 0.1707 -0.0302 -0.0520 0.0135  94  HIS   A CB  
739  C  CG  . HIS   A 94  ? 0.1192 0.1292 0.1646 -0.0113 -0.0413 0.0089  94  HIS   A CG  
740  N  ND1 . HIS   A 94  ? 0.1389 0.1306 0.1729 0.0004  -0.0365 -0.0048 94  HIS   A ND1 
741  C  CD2 . HIS   A 94  ? 0.1145 0.1323 0.1784 -0.0096 -0.0560 0.0129  94  HIS   A CD2 
742  C  CE1 . HIS   A 94  ? 0.1493 0.0919 0.1712 -0.0248 -0.0301 0.0384  94  HIS   A CE1 
743  N  NE2 . HIS   A 94  ? 0.1301 0.0942 0.2274 -0.0198 -0.0730 -0.0155 94  HIS   A NE2 
744  N  N   . PHE   A 95  ? 0.1206 0.1285 0.2056 -0.0064 -0.0118 0.0008  95  PHE   A N   
745  C  CA  . PHE   A 95  ? 0.0838 0.1251 0.2122 -0.0163 -0.0390 0.0031  95  PHE   A CA  
746  C  C   . PHE   A 95  ? 0.1095 0.1129 0.2161 0.0231  -0.0350 0.0070  95  PHE   A C   
747  O  O   . PHE   A 95  ? 0.1759 0.1045 0.2190 -0.0021 -0.0305 0.0122  95  PHE   A O   
748  C  CB  . PHE   A 95  ? 0.1262 0.1169 0.1899 0.0024  -0.0331 -0.0110 95  PHE   A CB  
749  C  CG  . PHE   A 95  ? 0.1183 0.0969 0.2024 -0.0441 -0.0450 0.0076  95  PHE   A CG  
750  C  CD1 . PHE   A 95  ? 0.1025 0.1386 0.2508 0.0091  -0.0653 0.0215  95  PHE   A CD1 
751  C  CD2 . PHE   A 95  ? 0.1133 0.0851 0.2456 -0.0446 -0.0321 -0.0147 95  PHE   A CD2 
752  C  CE1 . PHE   A 95  ? 0.0935 0.1132 0.2419 -0.0087 -0.0541 0.0226  95  PHE   A CE1 
753  C  CE2 . PHE   A 95  ? 0.1360 0.1044 0.2497 -0.0439 -0.0480 0.0168  95  PHE   A CE2 
754  C  CZ  . PHE   A 95  ? 0.1495 0.1240 0.2406 -0.0116 -0.0173 0.0299  95  PHE   A CZ  
755  N  N   . HIS   A 96  ? 0.0980 0.1115 0.2163 0.0134  -0.0286 -0.0025 96  HIS   A N   
756  C  CA  . HIS   A 96  ? 0.1159 0.0998 0.2161 0.0252  -0.0301 0.0177  96  HIS   A CA  
757  C  C   . HIS   A 96  ? 0.1332 0.1296 0.2402 -0.0321 0.0085  0.0084  96  HIS   A C   
758  O  O   . HIS   A 96  ? 0.1016 0.1266 0.2488 0.0312  0.0074  0.0121  96  HIS   A O   
759  C  CB  . HIS   A 96  ? 0.1905 0.0973 0.1960 0.0058  -0.0121 -0.0088 96  HIS   A CB  
760  C  CG  . HIS   A 96  ? 0.1091 0.1032 0.2222 0.0030  -0.0205 -0.0106 96  HIS   A CG  
761  N  ND1 . HIS   A 96  ? 0.1168 0.0979 0.2260 -0.0036 -0.0366 -0.0008 96  HIS   A ND1 
762  C  CD2 . HIS   A 96  ? 0.1659 0.0379 0.2319 -0.0163 -0.0127 -0.0212 96  HIS   A CD2 
763  C  CE1 . HIS   A 96  ? 0.1447 0.0998 0.2043 0.0449  -0.0068 -0.0075 96  HIS   A CE1 
764  N  NE2 . HIS   A 96  ? 0.1096 0.0209 0.2727 0.0230  -0.0530 0.0355  96  HIS   A NE2 
765  N  N   . TRP   A 97  ? 0.1368 0.1041 0.2402 -0.0328 -0.0262 -0.0044 97  TRP   A N   
766  C  CA  . TRP   A 97  ? 0.1204 0.0844 0.2334 0.0108  -0.0701 0.0122  97  TRP   A CA  
767  C  C   . TRP   A 97  ? 0.1009 0.0782 0.2348 -0.0055 -0.0275 0.0159  97  TRP   A C   
768  O  O   . TRP   A 97  ? 0.1309 0.0864 0.2600 -0.0394 -0.0107 -0.0006 97  TRP   A O   
769  C  CB  . TRP   A 97  ? 0.1335 0.1497 0.2002 0.0161  -0.0480 -0.0040 97  TRP   A CB  
770  C  CG  . TRP   A 97  ? 0.1303 0.1284 0.2232 -0.0305 -0.0354 -0.0017 97  TRP   A CG  
771  C  CD1 . TRP   A 97  ? 0.1982 0.2068 0.2095 -0.0260 -0.0034 -0.0306 97  TRP   A CD1 
772  C  CD2 . TRP   A 97  ? 0.1438 0.1053 0.2086 -0.0103 -0.0232 -0.0113 97  TRP   A CD2 
773  N  NE1 . TRP   A 97  ? 0.1436 0.1346 0.2208 0.0111  -0.0078 -0.0219 97  TRP   A NE1 
774  C  CE2 . TRP   A 97  ? 0.1863 0.1187 0.2049 0.0089  -0.0160 -0.0280 97  TRP   A CE2 
775  C  CE3 . TRP   A 97  ? 0.0668 0.1111 0.2401 0.0017  -0.0003 0.0116  97  TRP   A CE3 
776  C  CZ2 . TRP   A 97  ? 0.1472 0.1393 0.2337 0.0158  -0.0405 -0.0055 97  TRP   A CZ2 
777  C  CZ3 . TRP   A 97  ? 0.1587 0.1734 0.1939 -0.0055 -0.0305 0.0248  97  TRP   A CZ3 
778  C  CH2 . TRP   A 97  ? 0.1271 0.1414 0.2082 0.0135  -0.0332 0.0131  97  TRP   A CH2 
779  N  N   . GLY   A 98  ? 0.1691 0.0635 0.2171 0.0105  -0.0245 -0.0206 98  GLY   A N   
780  C  CA  . GLY   A 98  ? 0.1953 0.1003 0.2451 0.0395  -0.0172 0.0084  98  GLY   A CA  
781  C  C   . GLY   A 98  ? 0.1921 0.0786 0.2199 0.0142  -0.0289 0.0200  98  GLY   A C   
782  O  O   . GLY   A 98  ? 0.2062 0.0643 0.2540 0.0026  -0.0369 0.0026  98  GLY   A O   
783  N  N   . SER   A 99  ? 0.1741 0.0890 0.2649 0.0212  -0.0119 -0.0034 99  SER   A N   
784  C  CA  . SER   A 99  ? 0.1643 0.0928 0.2685 0.0002  0.0153  -0.0034 99  SER   A CA  
785  C  C   . SER   A 99  ? 0.1896 0.0680 0.2644 0.0160  -0.0285 0.0237  99  SER   A C   
786  O  O   . SER   A 99  ? 0.2484 0.1808 0.2871 -0.0194 -0.0151 -0.0343 99  SER   A O   
787  C  CB  . SER   A 99  ? 0.1930 0.1414 0.3054 0.0434  0.0179  -0.0305 99  SER   A CB  
788  O  OG  . SER   A 99  ? 0.1890 0.1881 0.3156 -0.0283 -0.0170 -0.0215 99  SER   A OG  
789  N  N   . LEU   A 100 ? 0.1615 0.0818 0.2802 -0.0198 -0.0275 0.0164  100 LEU   A N   
790  C  CA  . LEU   A 100 ? 0.1615 0.0987 0.3069 -0.0316 0.0018  0.0011  100 LEU   A CA  
791  C  C   . LEU   A 100 ? 0.1804 0.1623 0.2345 -0.0092 -0.0184 -0.0114 100 LEU   A C   
792  O  O   . LEU   A 100 ? 0.1711 0.1363 0.2595 0.0124  -0.0222 -0.0151 100 LEU   A O   
793  C  CB  . LEU   A 100 ? 0.2387 0.1794 0.3956 0.0309  0.0118  0.0761  100 LEU   A CB  
794  C  CG  . LEU   A 100 ? 0.3739 0.1892 0.4066 0.0244  0.0715  -0.0394 100 LEU   A CG  
795  C  CD1 . LEU   A 100 ? 0.3814 0.4392 0.5168 0.1518  0.1037  0.0408  100 LEU   A CD1 
796  C  CD2 . LEU   A 100 ? 0.4098 0.2167 0.4840 -0.0948 0.1057  -0.1195 100 LEU   A CD2 
797  N  N   . ASP   A 101 ? 0.1436 0.1612 0.2573 0.0100  -0.0322 0.0369  101 ASP   A N   
798  C  CA  . ASP   A 101 ? 0.1917 0.1151 0.2736 -0.0505 -0.0036 -0.0051 101 ASP   A CA  
799  C  C   . ASP   A 101 ? 0.1967 0.1641 0.2696 0.0061  -0.0197 0.0021  101 ASP   A C   
800  O  O   . ASP   A 101 ? 0.2085 0.1357 0.3416 0.0165  0.0097  0.0438  101 ASP   A O   
801  C  CB  . ASP   A 101 ? 0.1646 0.1320 0.3573 -0.0438 -0.0469 0.0688  101 ASP   A CB  
802  C  CG  . ASP   A 101 ? 0.2045 0.2348 0.3802 -0.0566 -0.0757 0.0679  101 ASP   A CG  
803  O  OD1 . ASP   A 101 ? 0.1603 0.1791 0.3308 -0.0027 -0.0485 0.0277  101 ASP   A OD1 
804  O  OD2 . ASP   A 101 ? 0.3274 0.2461 0.5035 -0.1206 -0.1076 0.0403  101 ASP   A OD2 
805  N  N   . GLY   A 102 ? 0.2063 0.1363 0.2442 -0.0353 -0.0346 0.0549  102 GLY   A N   
806  C  CA  . GLY   A 102 ? 0.2111 0.0896 0.2445 -0.0134 -0.0002 -0.0106 102 GLY   A CA  
807  C  C   . GLY   A 102 ? 0.2380 0.0989 0.2463 -0.0089 -0.0165 -0.0145 102 GLY   A C   
808  O  O   . GLY   A 102 ? 0.1987 0.1162 0.2655 0.0271  -0.0253 0.0137  102 GLY   A O   
809  N  N   . GLN   A 103 ? 0.1402 0.1392 0.2549 -0.0008 -0.0313 0.0059  103 GLN   A N   
810  C  CA  . GLN   A 103 ? 0.1321 0.1007 0.2723 0.0275  -0.0557 0.0006  103 GLN   A CA  
811  C  C   . GLN   A 103 ? 0.1316 0.1115 0.2213 0.0127  -0.0410 0.0019  103 GLN   A C   
812  O  O   . GLN   A 103 ? 0.1589 0.1143 0.2419 0.0232  -0.0428 -0.0047 103 GLN   A O   
813  C  CB  . GLN   A 103 ? 0.1367 0.1428 0.3231 0.0212  0.0008  0.0083  103 GLN   A CB  
814  C  CG  . GLN   A 103 ? 0.1316 0.1319 0.3236 0.0398  0.0044  0.0275  103 GLN   A CG  
815  C  CD  . GLN   A 103 ? 0.1625 0.2377 0.3071 0.1203  0.0600  0.0364  103 GLN   A CD  
816  O  OE1 . GLN   A 103 ? 0.3514 0.3866 0.4845 0.1738  0.1260  0.2171  103 GLN   A OE1 
817  N  NE2 . GLN   A 103 ? 0.1791 0.2204 0.3449 0.0260  0.0512  0.0309  103 GLN   A NE2 
818  N  N   . GLY   A 104 ? 0.1514 0.0983 0.2598 0.0333  -0.0093 -0.0044 104 GLY   A N   
819  C  CA  . GLY   A 104 ? 0.1709 0.1229 0.2194 0.0192  -0.0148 -0.0004 104 GLY   A CA  
820  C  C   . GLY   A 104 ? 0.1270 0.1684 0.1974 -0.0153 -0.0250 -0.0200 104 GLY   A C   
821  O  O   . GLY   A 104 ? 0.1443 0.1531 0.2777 -0.0099 -0.0030 0.0122  104 GLY   A O   
822  N  N   . SER   A 105 ? 0.1224 0.1374 0.2218 0.0190  0.0078  -0.0232 105 SER   A N   
823  C  CA  . SER   A 105 ? 0.1332 0.1341 0.1971 -0.0179 -0.0188 -0.0386 105 SER   A CA  
824  C  C   . SER   A 105 ? 0.1213 0.1328 0.1920 0.0064  -0.0315 -0.0359 105 SER   A C   
825  O  O   . SER   A 105 ? 0.1231 0.1086 0.2476 -0.0075 -0.0406 -0.0206 105 SER   A O   
826  C  CB  . SER   A 105 ? 0.0836 0.2147 0.1952 0.0115  -0.0396 0.0047  105 SER   A CB  
827  O  OG  . SER   A 105 ? 0.1199 0.1091 0.2425 -0.0194 -0.0304 -0.0067 105 SER   A OG  
828  N  N   . GLU   A 106 ? 0.1219 0.1127 0.1935 -0.0373 -0.0325 -0.0252 106 GLU   A N   
829  C  CA  . GLU   A 106 ? 0.1016 0.0734 0.2010 -0.0168 -0.0286 -0.0217 106 GLU   A CA  
830  C  C   . GLU   A 106 ? 0.1247 0.1062 0.2116 0.0121  -0.0120 -0.0048 106 GLU   A C   
831  O  O   . GLU   A 106 ? 0.0976 0.1274 0.2672 -0.0064 -0.0496 0.0055  106 GLU   A O   
832  C  CB  . GLU   A 106 ? 0.1691 0.1080 0.2188 -0.0198 -0.0359 0.0484  106 GLU   A CB  
833  C  CG  . GLU   A 106 ? 0.1439 0.0846 0.2219 0.0006  -0.0395 0.0312  106 GLU   A CG  
834  C  CD  . GLU   A 106 ? 0.1237 0.0828 0.2231 -0.0006 -0.0082 -0.0089 106 GLU   A CD  
835  O  OE1 . GLU   A 106 ? 0.0800 0.1025 0.2591 0.0316  -0.0439 0.0110  106 GLU   A OE1 
836  O  OE2 . GLU   A 106 ? 0.0989 0.0903 0.2806 -0.0022 -0.0306 0.0156  106 GLU   A OE2 
837  N  N   . HIS   A 107 ? 0.1307 0.1375 0.1939 0.0250  -0.0042 -0.0412 107 HIS   A N   
838  C  CA  . HIS   A 107 ? 0.1181 0.0557 0.2129 0.0098  -0.0027 -0.0244 107 HIS   A CA  
839  C  C   . HIS   A 107 ? 0.1158 0.0630 0.2005 -0.0100 0.0236  -0.0215 107 HIS   A C   
840  O  O   . HIS   A 107 ? 0.1461 0.1205 0.2369 0.0373  -0.0310 -0.0230 107 HIS   A O   
841  C  CB  . HIS   A 107 ? 0.0846 0.0973 0.2282 0.0012  -0.0135 -0.0231 107 HIS   A CB  
842  C  CG  . HIS   A 107 ? 0.0845 0.1120 0.2442 -0.0243 -0.0084 0.0036  107 HIS   A CG  
843  N  ND1 . HIS   A 107 ? 0.0989 0.0940 0.2271 -0.0152 -0.0215 -0.0086 107 HIS   A ND1 
844  C  CD2 . HIS   A 107 ? 0.1113 0.0856 0.2552 0.0018  -0.0217 0.0017  107 HIS   A CD2 
845  C  CE1 . HIS   A 107 ? 0.1630 0.0491 0.2060 0.0148  -0.0077 -0.0039 107 HIS   A CE1 
846  N  NE2 . HIS   A 107 ? 0.1165 0.0949 0.2153 -0.0071 -0.0097 0.0158  107 HIS   A NE2 
847  N  N   . THR   A 108 ? 0.1242 0.0829 0.2405 -0.0403 -0.0035 -0.0020 108 THR   A N   
848  C  CA  . THR   A 108 ? 0.1244 0.0558 0.2113 0.0071  -0.0082 0.0022  108 THR   A CA  
849  C  C   . THR   A 108 ? 0.1334 0.1278 0.2188 -0.0286 0.0036  0.0103  108 THR   A C   
850  O  O   . THR   A 108 ? 0.1368 0.1032 0.2801 0.0088  -0.0234 0.0141  108 THR   A O   
851  C  CB  . THR   A 108 ? 0.1727 0.0800 0.2061 0.0397  -0.0469 -0.0078 108 THR   A CB  
852  O  OG1 . THR   A 108 ? 0.1648 0.1219 0.2134 -0.0030 -0.0312 -0.0061 108 THR   A OG1 
853  C  CG2 . THR   A 108 ? 0.1413 0.1205 0.2057 0.0021  -0.0391 0.0187  108 THR   A CG2 
854  N  N   . VAL   A 109 ? 0.1212 0.1050 0.2362 -0.0146 -0.0156 0.0409  109 VAL   A N   
855  C  CA  . VAL   A 109 ? 0.1280 0.1165 0.2379 -0.0032 -0.0166 0.0385  109 VAL   A CA  
856  C  C   . VAL   A 109 ? 0.1604 0.0883 0.2255 -0.0018 -0.0022 0.0114  109 VAL   A C   
857  O  O   . VAL   A 109 ? 0.1574 0.0840 0.2850 0.0061  -0.0199 -0.0149 109 VAL   A O   
858  C  CB  . VAL   A 109 ? 0.1335 0.1712 0.2567 0.0271  -0.0184 0.0145  109 VAL   A CB  
859  C  CG1 . VAL   A 109 ? 0.1273 0.1786 0.3159 -0.0089 -0.0013 0.0201  109 VAL   A CG1 
860  C  CG2 . VAL   A 109 ? 0.1597 0.1806 0.2449 -0.0259 -0.0073 0.0460  109 VAL   A CG2 
861  N  N   . ASP   A 110 ? 0.1808 0.0831 0.2394 0.0144  0.0031  0.0446  110 ASP   A N   
862  C  CA  . ASP   A 110 ? 0.1953 0.0933 0.2485 0.0359  0.0209  0.0440  110 ASP   A CA  
863  C  C   . ASP   A 110 ? 0.1944 0.0813 0.2555 -0.0158 -0.0049 -0.0256 110 ASP   A C   
864  O  O   . ASP   A 110 ? 0.2354 0.0662 0.2993 -0.0024 -0.0067 0.0323  110 ASP   A O   
865  C  CB  . ASP   A 110 ? 0.1732 0.1605 0.2794 0.0111  -0.0023 0.0323  110 ASP   A CB  
866  C  CG  . ASP   A 110 ? 0.2002 0.1726 0.2667 0.0092  0.0223  0.0195  110 ASP   A CG  
867  O  OD1 . ASP   A 110 ? 0.1942 0.1816 0.3037 0.0345  0.0500  0.0161  110 ASP   A OD1 
868  O  OD2 . ASP   A 110 ? 0.1878 0.2278 0.3373 0.0344  0.0157  0.0033  110 ASP   A OD2 
869  N  N   . LYS   A 111 ? 0.1526 0.1583 0.2502 -0.0161 -0.0236 0.0067  111 LYS   A N   
870  C  CA  . LYS   A 111 ? 0.1870 0.1556 0.2443 0.0467  -0.0378 0.0356  111 LYS   A CA  
871  C  C   . LYS   A 111 ? 0.1478 0.0827 0.2564 0.0058  0.0068  0.0079  111 LYS   A C   
872  O  O   . LYS   A 111 ? 0.1659 0.1543 0.2644 0.0223  -0.0021 0.0117  111 LYS   A O   
873  C  CB  . LYS   A 111 ? 0.2088 0.1514 0.2739 0.0479  -0.0447 0.0518  111 LYS   A CB  
874  C  CG  . LYS   A 111 ? 0.1982 0.2479 0.3274 0.0312  -0.0971 0.0545  111 LYS   A CG  
875  C  CD  . LYS   A 111 ? 0.1632 0.2982 0.3694 -0.0010 -0.0668 0.0185  111 LYS   A CD  
876  C  CE  . LYS   A 111 ? 0.2197 0.2685 0.3888 0.1119  -0.1256 -0.0245 111 LYS   A CE  
877  N  NZ  . LYS   A 111 ? 0.2705 0.3206 0.5344 0.1543  -0.0687 0.1084  111 LYS   A NZ  
878  N  N   . LYS   A 112 ? 0.1465 0.1040 0.2161 0.0129  -0.0289 0.0226  112 LYS   A N   
879  C  CA  . LYS   A 112 ? 0.2070 0.1513 0.2134 0.0126  -0.0407 0.0210  112 LYS   A CA  
880  C  C   . LYS   A 112 ? 0.1741 0.0944 0.2462 0.0359  -0.0493 0.0182  112 LYS   A C   
881  O  O   . LYS   A 112 ? 0.1594 0.1050 0.2541 0.0504  -0.0255 -0.0159 112 LYS   A O   
882  C  CB  . LYS   A 112 ? 0.2262 0.1597 0.2769 -0.0414 -0.0427 0.0037  112 LYS   A CB  
883  C  CG  . LYS   A 112 ? 0.2081 0.1867 0.3054 -0.0405 -0.0469 -0.0454 112 LYS   A CG  
884  C  CD  . LYS   A 112 ? 0.2147 0.1650 0.2854 -0.0458 -0.0537 -0.0315 112 LYS   A CD  
885  C  CE  . LYS   A 112 ? 0.3353 0.1284 0.2767 0.0129  -0.0604 0.0099  112 LYS   A CE  
886  N  NZ  . LYS   A 112 ? 0.3266 0.1036 0.3302 -0.0051 -0.0639 0.0155  112 LYS   A NZ  
887  N  N   A LYS   A 113 ? 0.1949 0.1704 0.2408 0.0271  -0.0498 0.0011  113 LYS   A N   
888  N  N   B LYS   A 113 ? 0.1755 0.1847 0.2516 0.0166  -0.0085 0.0293  113 LYS   A N   
889  C  CA  A LYS   A 113 ? 0.1608 0.1549 0.2424 0.0370  -0.0267 -0.0098 113 LYS   A CA  
890  C  CA  B LYS   A 113 ? 0.1643 0.1571 0.2293 0.0303  -0.0046 0.0032  113 LYS   A CA  
891  C  C   A LYS   A 113 ? 0.1203 0.0810 0.2938 0.0221  -0.0148 -0.0245 113 LYS   A C   
892  C  C   B LYS   A 113 ? 0.1028 0.1177 0.2759 0.0420  0.0060  -0.0215 113 LYS   A C   
893  O  O   A LYS   A 113 ? 0.1733 0.0872 0.2321 -0.0106 -0.0226 0.0023  113 LYS   A O   
894  O  O   B LYS   A 113 ? 0.1525 0.1226 0.2519 -0.0081 -0.0050 0.0004  113 LYS   A O   
895  C  CB  A LYS   A 113 ? 0.1374 0.1478 0.3611 0.0046  -0.0251 -0.0671 113 LYS   A CB  
896  C  CB  B LYS   A 113 ? 0.1378 0.1359 0.2766 0.0097  -0.0143 0.0052  113 LYS   A CB  
897  C  CG  A LYS   A 113 ? 0.1065 0.1837 0.3181 0.0295  -0.0102 -0.0433 113 LYS   A CG  
898  C  CG  B LYS   A 113 ? 0.1400 0.1234 0.3047 -0.0196 -0.0173 0.0150  113 LYS   A CG  
899  C  CD  A LYS   A 113 ? 0.1068 0.2060 0.3546 0.0516  -0.0008 -0.0190 113 LYS   A CD  
900  C  CD  B LYS   A 113 ? 0.1145 0.1738 0.3160 0.0074  -0.0367 -0.0240 113 LYS   A CD  
901  C  CE  A LYS   A 113 ? 0.1481 0.2346 0.3141 0.0227  -0.0186 -0.0043 113 LYS   A CE  
902  C  CE  B LYS   A 113 ? 0.1230 0.1533 0.2140 0.0119  -0.0219 -0.0465 113 LYS   A CE  
903  N  NZ  A LYS   A 113 ? 0.1773 0.2495 0.3711 0.0555  -0.0656 0.0258  113 LYS   A NZ  
904  N  NZ  B LYS   A 113 ? 0.1355 0.2345 0.2147 0.0597  -0.0071 -0.0328 113 LYS   A NZ  
905  N  N   . TYR   A 114 ? 0.1669 0.1145 0.2626 0.0389  -0.0173 -0.0042 114 TYR   A N   
906  C  CA  . TYR   A 114 ? 0.1199 0.0736 0.2727 0.0158  -0.0166 0.0009  114 TYR   A CA  
907  C  C   . TYR   A 114 ? 0.1611 0.0519 0.2522 0.0358  -0.0215 0.0044  114 TYR   A C   
908  O  O   . TYR   A 114 ? 0.1453 0.1127 0.2894 0.0100  -0.0143 0.0329  114 TYR   A O   
909  C  CB  . TYR   A 114 ? 0.1007 0.1280 0.2672 0.0411  -0.0257 -0.0051 114 TYR   A CB  
910  C  CG  . TYR   A 114 ? 0.1650 0.0531 0.2622 0.0389  -0.0072 0.0164  114 TYR   A CG  
911  C  CD1 . TYR   A 114 ? 0.1826 0.1048 0.2396 0.0590  -0.0328 0.0482  114 TYR   A CD1 
912  C  CD2 . TYR   A 114 ? 0.1684 0.1137 0.2907 0.0110  -0.0065 0.0242  114 TYR   A CD2 
913  C  CE1 . TYR   A 114 ? 0.2319 0.0955 0.2447 -0.0137 -0.0277 0.0164  114 TYR   A CE1 
914  C  CE2 . TYR   A 114 ? 0.2228 0.1277 0.2524 0.0247  0.0008  0.0507  114 TYR   A CE2 
915  C  CZ  . TYR   A 114 ? 0.2141 0.1398 0.2722 -0.0283 0.0135  0.0560  114 TYR   A CZ  
916  O  OH  . TYR   A 114 ? 0.2852 0.1597 0.3267 0.0003  0.0515  -0.0057 114 TYR   A OH  
917  N  N   . ALA   A 115 ? 0.1231 0.0740 0.2452 -0.0047 -0.0181 0.0057  115 ALA   A N   
918  C  CA  . ALA   A 115 ? 0.1460 0.0655 0.2595 -0.0756 -0.0077 -0.0022 115 ALA   A CA  
919  C  C   . ALA   A 115 ? 0.1615 0.0361 0.2301 -0.0094 -0.0189 0.0099  115 ALA   A C   
920  O  O   . ALA   A 115 ? 0.1471 0.0994 0.2483 -0.0098 -0.0261 0.0020  115 ALA   A O   
921  C  CB  . ALA   A 115 ? 0.1493 0.0670 0.3104 -0.0275 -0.0483 -0.0044 115 ALA   A CB  
922  N  N   . ALA   A 116 ? 0.1657 0.0445 0.2443 0.0043  -0.0320 -0.0002 116 ALA   A N   
923  C  CA  . ALA   A 116 ? 0.1741 0.0745 0.1872 -0.0134 -0.0067 0.0168  116 ALA   A CA  
924  C  C   . ALA   A 116 ? 0.1630 0.1145 0.1867 -0.0103 -0.0250 -0.0046 116 ALA   A C   
925  O  O   . ALA   A 116 ? 0.1431 0.0820 0.2359 0.0167  -0.0240 0.0145  116 ALA   A O   
926  C  CB  . ALA   A 116 ? 0.1849 0.0807 0.1928 -0.0190 -0.0392 -0.0092 116 ALA   A CB  
927  N  N   . GLU   A 117 ? 0.1301 0.0969 0.2169 -0.0117 -0.0343 -0.0053 117 GLU   A N   
928  C  CA  . GLU   A 117 ? 0.1517 0.0892 0.1964 0.0036  -0.0436 0.0010  117 GLU   A CA  
929  C  C   . GLU   A 117 ? 0.1109 0.1208 0.1987 0.0124  -0.0153 0.0260  117 GLU   A C   
930  O  O   . GLU   A 117 ? 0.1208 0.1065 0.2534 0.0023  0.0025  0.0229  117 GLU   A O   
931  C  CB  . GLU   A 117 ? 0.1381 0.1280 0.1847 0.0131  -0.0377 -0.0185 117 GLU   A CB  
932  C  CG  . GLU   A 117 ? 0.1400 0.0919 0.1822 -0.0076 -0.0356 -0.0155 117 GLU   A CG  
933  C  CD  . GLU   A 117 ? 0.1615 0.1262 0.1890 0.0201  -0.0390 -0.0103 117 GLU   A CD  
934  O  OE1 . GLU   A 117 ? 0.1163 0.1009 0.2529 -0.0105 -0.0435 -0.0017 117 GLU   A OE1 
935  O  OE2 . GLU   A 117 ? 0.1124 0.1356 0.2467 0.0145  -0.0705 -0.0230 117 GLU   A OE2 
936  N  N   . LEU   A 118 ? 0.0907 0.0993 0.2447 -0.0135 -0.0261 -0.0003 118 LEU   A N   
937  C  CA  . LEU   A 118 ? 0.0899 0.1080 0.2402 0.0117  -0.0159 -0.0055 118 LEU   A CA  
938  C  C   . LEU   A 118 ? 0.0537 0.1400 0.2018 0.0081  0.0070  -0.0087 118 LEU   A C   
939  O  O   . LEU   A 118 ? 0.0993 0.1109 0.2064 -0.0149 -0.0058 0.0057  118 LEU   A O   
940  C  CB  . LEU   A 118 ? 0.0994 0.0928 0.2179 0.0040  -0.0480 -0.0019 118 LEU   A CB  
941  C  CG  . LEU   A 118 ? 0.0820 0.0991 0.2305 -0.0010 -0.0263 0.0091  118 LEU   A CG  
942  C  CD1 . LEU   A 118 ? 0.1294 0.1482 0.2248 0.0066  -0.0190 0.0185  118 LEU   A CD1 
943  C  CD2 . LEU   A 118 ? 0.0770 0.1639 0.2722 -0.0126 -0.0238 0.0158  118 LEU   A CD2 
944  N  N   . HIS   A 119 ? 0.0824 0.1003 0.2348 0.0073  -0.0245 -0.0024 119 HIS   A N   
945  C  CA  . HIS   A 119 ? 0.0680 0.0966 0.2326 -0.0042 -0.0240 0.0098  119 HIS   A CA  
946  C  C   . HIS   A 119 ? 0.1260 0.0763 0.1916 -0.0103 -0.0237 -0.0076 119 HIS   A C   
947  O  O   . HIS   A 119 ? 0.0960 0.1288 0.2098 0.0170  -0.0130 -0.0116 119 HIS   A O   
948  C  CB  . HIS   A 119 ? 0.0515 0.1039 0.2240 0.0390  -0.0451 0.0164  119 HIS   A CB  
949  C  CG  . HIS   A 119 ? 0.0976 0.0903 0.2039 0.0351  -0.0328 0.0162  119 HIS   A CG  
950  N  ND1 . HIS   A 119 ? 0.0768 0.1357 0.2420 -0.0484 -0.0627 0.0336  119 HIS   A ND1 
951  C  CD2 . HIS   A 119 ? 0.1221 0.1154 0.1736 0.0064  -0.0295 0.0223  119 HIS   A CD2 
952  C  CE1 . HIS   A 119 ? 0.1086 0.0962 0.1966 -0.0140 0.0116  0.0219  119 HIS   A CE1 
953  N  NE2 . HIS   A 119 ? 0.0889 0.0901 0.2068 -0.0244 -0.0206 0.0195  119 HIS   A NE2 
954  N  N   . LEU   A 120 ? 0.0819 0.0858 0.2391 -0.0277 -0.0296 -0.0063 120 LEU   A N   
955  C  CA  . LEU   A 120 ? 0.1122 0.1113 0.2511 0.0061  -0.0314 -0.0127 120 LEU   A CA  
956  C  C   . LEU   A 120 ? 0.0892 0.0763 0.2041 0.0557  -0.0230 0.0006  120 LEU   A C   
957  O  O   . LEU   A 120 ? 0.0980 0.0817 0.1991 -0.0029 -0.0269 -0.0118 120 LEU   A O   
958  C  CB  . LEU   A 120 ? 0.0983 0.0815 0.2633 0.0378  -0.0639 -0.0075 120 LEU   A CB  
959  C  CG  . LEU   A 120 ? 0.1265 0.1294 0.2485 -0.0275 -0.0824 0.0166  120 LEU   A CG  
960  C  CD1 . LEU   A 120 ? 0.2011 0.0876 0.2829 -0.0379 -0.0659 0.0301  120 LEU   A CD1 
961  C  CD2 . LEU   A 120 ? 0.1298 0.1683 0.2664 0.0105  -0.0947 0.0044  120 LEU   A CD2 
962  N  N   . VAL   A 121 ? 0.1039 0.1027 0.2505 0.0106  -0.0247 -0.0044 121 VAL   A N   
963  C  CA  . VAL   A 121 ? 0.1118 0.0851 0.2486 0.0208  -0.0294 -0.0126 121 VAL   A CA  
964  C  C   . VAL   A 121 ? 0.1454 0.0786 0.2323 0.0186  -0.0072 -0.0070 121 VAL   A C   
965  O  O   . VAL   A 121 ? 0.1684 0.0975 0.2276 -0.0253 -0.0434 -0.0069 121 VAL   A O   
966  C  CB  . VAL   A 121 ? 0.0933 0.0792 0.2925 0.0158  -0.0189 -0.0197 121 VAL   A CB  
967  C  CG1 . VAL   A 121 ? 0.1140 0.0425 0.2741 -0.0139 -0.0194 0.0353  121 VAL   A CG1 
968  C  CG2 . VAL   A 121 ? 0.1181 0.1134 0.2879 0.0532  0.0098  0.0261  121 VAL   A CG2 
969  N  N   . HIS   A 122 ? 0.1582 0.0727 0.2125 0.0055  -0.0240 0.0285  122 HIS   A N   
970  C  CA  . HIS   A 122 ? 0.1186 0.0675 0.2533 -0.0049 -0.0537 -0.0018 122 HIS   A CA  
971  C  C   . HIS   A 122 ? 0.1817 0.0776 0.2346 -0.0305 -0.0543 0.0052  122 HIS   A C   
972  O  O   . HIS   A 122 ? 0.1357 0.1047 0.2512 -0.0273 -0.0458 0.0156  122 HIS   A O   
973  C  CB  . HIS   A 122 ? 0.1586 0.1190 0.2632 -0.0094 -0.0341 0.0055  122 HIS   A CB  
974  C  CG  . HIS   A 122 ? 0.1597 0.0833 0.1932 0.0172  -0.0458 0.0013  122 HIS   A CG  
975  N  ND1 . HIS   A 122 ? 0.0890 0.0734 0.2554 0.0075  -0.0232 -0.0117 122 HIS   A ND1 
976  C  CD2 . HIS   A 122 ? 0.1240 0.1244 0.2405 -0.0070 -0.0350 0.0107  122 HIS   A CD2 
977  C  CE1 . HIS   A 122 ? 0.0853 0.1569 0.2858 -0.0066 -0.0506 -0.0199 122 HIS   A CE1 
978  N  NE2 . HIS   A 122 ? 0.1180 0.1291 0.2813 0.0018  -0.0212 0.0145  122 HIS   A NE2 
979  N  N   . TRP   A 123 ? 0.1101 0.0784 0.2732 -0.0039 -0.0260 0.0152  123 TRP   A N   
980  C  CA  . TRP   A 123 ? 0.1489 0.1109 0.2592 -0.0133 -0.0387 0.0032  123 TRP   A CA  
981  C  C   . TRP   A 123 ? 0.1540 0.1046 0.2098 -0.0130 -0.0288 0.0170  123 TRP   A C   
982  O  O   . TRP   A 123 ? 0.1490 0.1467 0.2576 -0.0140 -0.0628 -0.0038 123 TRP   A O   
983  C  CB  . TRP   A 123 ? 0.1702 0.1804 0.2229 -0.0315 -0.0445 0.0100  123 TRP   A CB  
984  C  CG  . TRP   A 123 ? 0.2346 0.1400 0.2046 -0.0289 -0.0074 0.0368  123 TRP   A CG  
985  C  CD1 . TRP   A 123 ? 0.1830 0.1720 0.2207 -0.0139 -0.0615 0.0281  123 TRP   A CD1 
986  C  CD2 . TRP   A 123 ? 0.2897 0.1292 0.2258 -0.0163 -0.0142 -0.0355 123 TRP   A CD2 
987  N  NE1 . TRP   A 123 ? 0.2552 0.1039 0.2604 -0.0189 -0.0948 -0.0072 123 TRP   A NE1 
988  C  CE2 . TRP   A 123 ? 0.2722 0.1332 0.2408 -0.0179 -0.0284 -0.0311 123 TRP   A CE2 
989  C  CE3 . TRP   A 123 ? 0.3350 0.0702 0.2956 -0.0681 -0.0507 -0.0171 123 TRP   A CE3 
990  C  CZ2 . TRP   A 123 ? 0.3888 0.1672 0.2380 -0.0186 -0.0450 0.0082  123 TRP   A CZ2 
991  C  CZ3 . TRP   A 123 ? 0.3859 0.0770 0.3181 -0.0545 -0.0809 -0.0320 123 TRP   A CZ3 
992  C  CH2 . TRP   A 123 ? 0.4308 0.1565 0.3067 -0.0637 -0.0515 -0.0053 123 TRP   A CH2 
993  N  N   . ASN   A 124 ? 0.1665 0.1061 0.2343 0.0114  -0.0334 -0.0392 124 ASN   A N   
994  C  CA  . ASN   A 124 ? 0.2225 0.0829 0.2315 0.0182  -0.0445 -0.0522 124 ASN   A CA  
995  C  C   . ASN   A 124 ? 0.1781 0.1269 0.2565 -0.0245 -0.0276 0.0001  124 ASN   A C   
996  O  O   . ASN   A 124 ? 0.1521 0.0912 0.2731 -0.0073 -0.0254 -0.0192 124 ASN   A O   
997  C  CB  . ASN   A 124 ? 0.1464 0.1270 0.2443 -0.0456 -0.0269 -0.0239 124 ASN   A CB  
998  C  CG  . ASN   A 124 ? 0.1382 0.1450 0.2530 -0.0214 -0.0296 -0.0104 124 ASN   A CG  
999  O  OD1 . ASN   A 124 ? 0.1748 0.1360 0.2820 0.0337  -0.0158 -0.0344 124 ASN   A OD1 
1000 N  ND2 . ASN   A 124 ? 0.1888 0.1301 0.2697 0.0052  -0.0422 -0.0076 124 ASN   A ND2 
1001 N  N   . THR   A 125 ? 0.1935 0.0955 0.2726 0.0161  -0.0403 -0.0166 125 THR   A N   
1002 C  CA  . THR   A 125 ? 0.2017 0.1180 0.3343 0.0035  -0.0820 0.0179  125 THR   A CA  
1003 C  C   . THR   A 125 ? 0.2011 0.1560 0.2985 0.0015  -0.0261 -0.0085 125 THR   A C   
1004 O  O   . THR   A 125 ? 0.2498 0.1371 0.3245 -0.0021 -0.0499 -0.0047 125 THR   A O   
1005 C  CB  . THR   A 125 ? 0.2027 0.1672 0.3460 -0.0032 -0.0801 -0.0072 125 THR   A CB  
1006 O  OG1 . THR   A 125 ? 0.2853 0.1262 0.4366 0.0666  -0.0520 0.0052  125 THR   A OG1 
1007 C  CG2 . THR   A 125 ? 0.3128 0.1973 0.3837 0.0013  -0.1444 -0.0219 125 THR   A CG2 
1008 N  N   . LYS   A 126 ? 0.2160 0.1360 0.2298 -0.0077 -0.0128 -0.0544 127 LYS   A N   
1009 C  CA  . LYS   A 126 ? 0.1152 0.1242 0.2852 -0.0057 -0.0174 -0.0446 127 LYS   A CA  
1010 C  C   . LYS   A 126 ? 0.1377 0.0637 0.3199 -0.0094 -0.0089 0.0004  127 LYS   A C   
1011 O  O   . LYS   A 126 ? 0.2111 0.0743 0.3529 -0.0218 -0.0332 -0.0279 127 LYS   A O   
1012 C  CB  . LYS   A 126 ? 0.2143 0.1278 0.2954 -0.0004 -0.0266 -0.0453 127 LYS   A CB  
1013 C  CG  . LYS   A 126 ? 0.2129 0.2328 0.2620 0.0031  -0.0741 0.0134  127 LYS   A CG  
1014 C  CD  . LYS   A 126 ? 0.4046 0.2643 0.2619 -0.1305 0.0384  -0.0430 127 LYS   A CD  
1015 C  CE  . LYS   A 126 ? 0.5485 0.3009 0.3690 -0.0599 -0.0635 -0.0942 127 LYS   A CE  
1016 N  NZ  . LYS   A 126 ? 0.5946 0.4602 0.4992 -0.1027 -0.1580 0.1925  127 LYS   A NZ  
1017 N  N   . TYR   A 127 ? 0.1808 0.1076 0.2524 0.0100  -0.0134 0.0049  128 TYR   A N   
1018 C  CA  . TYR   A 127 ? 0.1743 0.0896 0.2422 0.0177  -0.0218 -0.0011 128 TYR   A CA  
1019 C  C   . TYR   A 127 ? 0.1931 0.0797 0.2540 0.0058  -0.0278 -0.0010 128 TYR   A C   
1020 O  O   . TYR   A 127 ? 0.2082 0.1234 0.3221 0.0109  0.0074  0.0136  128 TYR   A O   
1021 C  CB  . TYR   A 127 ? 0.2190 0.0557 0.2523 0.0149  -0.0421 -0.0302 128 TYR   A CB  
1022 C  CG  . TYR   A 127 ? 0.2451 0.0958 0.2366 -0.0097 -0.0254 0.0001  128 TYR   A CG  
1023 C  CD1 . TYR   A 127 ? 0.2244 0.1896 0.2750 -0.0277 -0.0182 -0.0511 128 TYR   A CD1 
1024 C  CD2 . TYR   A 127 ? 0.2177 0.1183 0.2312 -0.0022 0.0239  0.0155  128 TYR   A CD2 
1025 C  CE1 . TYR   A 127 ? 0.2495 0.1270 0.2687 -0.0443 -0.0391 -0.0181 128 TYR   A CE1 
1026 C  CE2 . TYR   A 127 ? 0.1317 0.1939 0.2219 -0.0033 -0.0036 -0.0245 128 TYR   A CE2 
1027 C  CZ  . TYR   A 127 ? 0.2279 0.1116 0.2456 0.0159  -0.0204 -0.0132 128 TYR   A CZ  
1028 O  OH  . TYR   A 127 ? 0.3270 0.1486 0.2603 -0.0079 -0.0134 -0.0679 128 TYR   A OH  
1029 N  N   . GLY   A 128 ? 0.1891 0.1251 0.2640 0.0296  -0.0383 0.0226  129 GLY   A N   
1030 C  CA  . GLY   A 128 ? 0.2402 0.1059 0.2676 -0.0356 -0.0100 0.0220  129 GLY   A CA  
1031 C  C   . GLY   A 128 ? 0.2669 0.1916 0.2769 -0.0138 -0.0193 0.0122  129 GLY   A C   
1032 O  O   . GLY   A 128 ? 0.3364 0.1073 0.3292 0.0164  -0.0650 0.0277  129 GLY   A O   
1033 N  N   . ASP   A 129 ? 0.2722 0.1526 0.2672 0.0000  -0.0322 -0.0247 130 ASP   A N   
1034 C  CA  . ASP   A 129 ? 0.3088 0.1678 0.2373 0.0135  -0.0250 0.0064  130 ASP   A CA  
1035 C  C   . ASP   A 129 ? 0.3920 0.1483 0.2217 0.0130  -0.0356 0.0044  130 ASP   A C   
1036 O  O   . ASP   A 129 ? 0.2859 0.1538 0.2363 0.0501  -0.0521 -0.0273 130 ASP   A O   
1037 C  CB  . ASP   A 129 ? 0.3206 0.1989 0.2600 0.0971  -0.0068 0.0478  130 ASP   A CB  
1038 C  CG  . ASP   A 129 ? 0.3419 0.0961 0.4300 0.0903  0.0158  -0.0119 130 ASP   A CG  
1039 O  OD1 . ASP   A 129 ? 0.5953 0.1152 0.4022 -0.0981 -0.1435 0.0905  130 ASP   A OD1 
1040 O  OD2 . ASP   A 129 ? 0.4294 0.2951 0.5500 0.1711  0.1499  0.1816  130 ASP   A OD2 
1041 N  N   . PHE   A 130 ? 0.2664 0.1701 0.2463 0.0348  -0.0864 -0.0190 131 PHE   A N   
1042 C  CA  . PHE   A 130 ? 0.2150 0.1474 0.2383 -0.0039 -0.0422 -0.0042 131 PHE   A CA  
1043 C  C   . PHE   A 130 ? 0.2282 0.1425 0.2442 -0.0776 -0.0250 0.0229  131 PHE   A C   
1044 O  O   . PHE   A 130 ? 0.1734 0.1277 0.2445 -0.0230 -0.0285 0.0053  131 PHE   A O   
1045 C  CB  . PHE   A 130 ? 0.2314 0.0953 0.2402 0.0240  -0.0569 -0.0034 131 PHE   A CB  
1046 C  CG  . PHE   A 130 ? 0.1704 0.1050 0.2979 0.0027  -0.0238 0.0506  131 PHE   A CG  
1047 C  CD1 . PHE   A 130 ? 0.2102 0.1090 0.2692 -0.0117 0.0010  0.0300  131 PHE   A CD1 
1048 C  CD2 . PHE   A 130 ? 0.2032 0.1321 0.2790 0.0238  -0.0004 -0.0222 131 PHE   A CD2 
1049 C  CE1 . PHE   A 130 ? 0.2290 0.0939 0.2787 -0.0296 -0.0639 -0.0168 131 PHE   A CE1 
1050 C  CE2 . PHE   A 130 ? 0.2163 0.1425 0.3065 0.0129  -0.0345 0.0228  131 PHE   A CE2 
1051 C  CZ  . PHE   A 130 ? 0.2817 0.1324 0.3126 -0.0256 0.0173  -0.0494 131 PHE   A CZ  
1052 N  N   . GLY   A 131 ? 0.2741 0.1335 0.2687 -0.0734 0.0241  0.0116  132 GLY   A N   
1053 C  CA  . GLY   A 131 ? 0.2715 0.1337 0.2588 -0.0515 0.0167  0.0294  132 GLY   A CA  
1054 C  C   . GLY   A 131 ? 0.2330 0.1637 0.2699 -0.0342 0.0068  0.0087  132 GLY   A C   
1055 O  O   . GLY   A 131 ? 0.2474 0.0919 0.3952 -0.0284 -0.0132 0.0064  132 GLY   A O   
1056 N  N   . LYS   A 132 ? 0.2225 0.0939 0.2689 -0.0634 0.0212  -0.0018 133 LYS   A N   
1057 C  CA  . LYS   A 132 ? 0.2129 0.0910 0.2688 -0.0054 -0.0030 0.0102  133 LYS   A CA  
1058 C  C   . LYS   A 132 ? 0.2000 0.1392 0.2691 -0.0414 -0.0306 0.0149  133 LYS   A C   
1059 O  O   . LYS   A 132 ? 0.1906 0.1280 0.2698 -0.0330 -0.0434 -0.0016 133 LYS   A O   
1060 C  CB  . LYS   A 132 ? 0.1851 0.1113 0.2658 0.0100  -0.0218 -0.0100 133 LYS   A CB  
1061 C  CG  . LYS   A 132 ? 0.2303 0.1903 0.3385 -0.0368 -0.0151 0.0369  133 LYS   A CG  
1062 C  CD  . LYS   A 132 ? 0.2888 0.1951 0.3996 -0.0318 -0.0357 0.0754  133 LYS   A CD  
1063 C  CE  . LYS   A 132 ? 0.4757 0.1952 0.4218 -0.0274 0.0505  0.0889  133 LYS   A CE  
1064 N  NZ  . LYS   A 132 ? 0.5032 0.3060 0.4335 -0.0444 0.0293  0.0510  133 LYS   A NZ  
1065 N  N   . ALA   A 133 ? 0.1773 0.1274 0.2547 -0.0422 -0.0177 0.0270  134 ALA   A N   
1066 C  CA  . ALA   A 133 ? 0.1745 0.1107 0.2900 -0.0703 -0.0299 0.0289  134 ALA   A CA  
1067 C  C   . ALA   A 133 ? 0.1594 0.0960 0.2495 -0.0610 -0.0011 -0.0019 134 ALA   A C   
1068 O  O   . ALA   A 133 ? 0.1840 0.1310 0.2515 -0.0194 -0.0251 -0.0178 134 ALA   A O   
1069 C  CB  . ALA   A 133 ? 0.1964 0.1278 0.2618 -0.0463 -0.0623 -0.0201 134 ALA   A CB  
1070 N  N   . VAL   A 134 ? 0.1485 0.0847 0.2722 -0.0148 -0.0153 0.0170  135 VAL   A N   
1071 C  CA  . VAL   A 134 ? 0.1923 0.0657 0.2547 -0.0063 -0.0356 0.0074  135 VAL   A CA  
1072 C  C   . VAL   A 134 ? 0.1632 0.1551 0.2240 -0.0095 0.0020  -0.0185 135 VAL   A C   
1073 O  O   . VAL   A 134 ? 0.1547 0.1775 0.2913 -0.0155 -0.0190 0.0099  135 VAL   A O   
1074 C  CB  . VAL   A 134 ? 0.1852 0.1655 0.2703 -0.0836 0.0063  -0.0245 135 VAL   A CB  
1075 C  CG1 . VAL   A 134 ? 0.2322 0.1872 0.2588 -0.0517 -0.0366 -0.0208 135 VAL   A CG1 
1076 C  CG2 . VAL   A 134 ? 0.2014 0.1623 0.2638 -0.0427 0.0223  -0.0252 135 VAL   A CG2 
1077 N  N   . GLN   A 135 ? 0.1647 0.1546 0.2530 -0.0072 -0.0042 -0.0256 136 GLN   A N   
1078 C  CA  . GLN   A 135 ? 0.1587 0.1389 0.2722 -0.0419 -0.0174 0.0171  136 GLN   A CA  
1079 C  C   . GLN   A 135 ? 0.1556 0.1414 0.2795 -0.0289 -0.0204 0.0147  136 GLN   A C   
1080 O  O   . GLN   A 135 ? 0.1585 0.2518 0.2958 -0.0275 -0.0406 -0.0178 136 GLN   A O   
1081 C  CB  . GLN   A 135 ? 0.1420 0.1247 0.3072 -0.0306 -0.0039 0.0063  136 GLN   A CB  
1082 C  CG  . GLN   A 135 ? 0.2981 0.1298 0.2817 -0.0205 0.0088  0.0269  136 GLN   A CG  
1083 C  CD  . GLN   A 135 ? 0.2623 0.1472 0.3501 -0.0594 -0.0489 0.0146  136 GLN   A CD  
1084 O  OE1 . GLN   A 135 ? 0.2951 0.3618 0.4303 -0.1560 -0.0763 -0.0036 136 GLN   A OE1 
1085 N  NE2 . GLN   A 135 ? 0.3422 0.3800 0.3611 -0.0458 -0.0061 0.1215  136 GLN   A NE2 
1086 N  N   . GLN   A 136 ? 0.1485 0.0932 0.2804 -0.0250 -0.0025 -0.0147 137 GLN   A N   
1087 C  CA  . GLN   A 136 ? 0.1798 0.1490 0.2307 -0.0102 -0.0216 0.0312  137 GLN   A CA  
1088 C  C   . GLN   A 136 ? 0.1653 0.1560 0.2181 -0.0064 -0.0147 0.0198  137 GLN   A C   
1089 O  O   . GLN   A 136 ? 0.1041 0.1870 0.2433 -0.0031 -0.0281 -0.0029 137 GLN   A O   
1090 C  CB  . GLN   A 136 ? 0.1680 0.1801 0.3139 0.0032  -0.0074 0.0330  137 GLN   A CB  
1091 C  CG  . GLN   A 136 ? 0.2185 0.1884 0.2874 -0.0238 0.0015  0.0258  137 GLN   A CG  
1092 C  CD  . GLN   A 136 ? 0.2048 0.2078 0.4179 -0.0379 0.0017  0.0095  137 GLN   A CD  
1093 O  OE1 . GLN   A 136 ? 0.3011 0.2187 0.4093 0.0216  -0.0326 -0.1088 137 GLN   A OE1 
1094 N  NE2 . GLN   A 136 ? 0.2666 0.3181 0.6557 -0.0422 0.0804  0.1167  137 GLN   A NE2 
1095 N  N   . PRO   A 137 ? 0.1865 0.1701 0.2025 -0.0135 0.0075  -0.0034 138 PRO   A N   
1096 C  CA  . PRO   A 137 ? 0.1607 0.1927 0.2239 0.0017  -0.0067 0.0368  138 PRO   A CA  
1097 C  C   . PRO   A 137 ? 0.1917 0.1581 0.2271 -0.0248 -0.0265 0.0245  138 PRO   A C   
1098 O  O   . PRO   A 137 ? 0.1841 0.1375 0.3204 0.0000  -0.0347 0.0390  138 PRO   A O   
1099 C  CB  . PRO   A 137 ? 0.1863 0.2016 0.2287 0.0157  -0.0366 0.0200  138 PRO   A CB  
1100 C  CG  . PRO   A 137 ? 0.2957 0.2473 0.2805 -0.0414 -0.0328 -0.0128 138 PRO   A CG  
1101 C  CD  . PRO   A 137 ? 0.1644 0.3168 0.2116 -0.0281 -0.0355 -0.0573 138 PRO   A CD  
1102 N  N   . ASP   A 138 ? 0.1244 0.1924 0.2086 -0.0089 -0.0253 -0.0231 139 ASP   A N   
1103 C  CA  . ASP   A 138 ? 0.1231 0.2359 0.2195 -0.0324 0.0002  0.0083  139 ASP   A CA  
1104 C  C   . ASP   A 138 ? 0.1000 0.1269 0.2362 -0.0111 -0.0303 -0.0214 139 ASP   A C   
1105 O  O   . ASP   A 138 ? 0.0840 0.1407 0.2727 0.0050  -0.0120 -0.0006 139 ASP   A O   
1106 C  CB  . ASP   A 138 ? 0.1302 0.1691 0.2646 0.0026  -0.0357 -0.0109 139 ASP   A CB  
1107 C  CG  . ASP   A 138 ? 0.2194 0.1738 0.2190 0.0545  -0.0212 -0.0189 139 ASP   A CG  
1108 O  OD1 . ASP   A 138 ? 0.2501 0.1917 0.2713 0.0135  -0.0252 -0.0111 139 ASP   A OD1 
1109 O  OD2 . ASP   A 138 ? 0.1993 0.2381 0.3276 0.0559  0.0179  -0.0185 139 ASP   A OD2 
1110 N  N   . GLY   A 139 ? 0.1617 0.1339 0.1903 -0.0268 -0.0245 -0.0458 140 GLY   A N   
1111 C  CA  . GLY   A 139 ? 0.1643 0.1238 0.2050 -0.0374 -0.0422 -0.0406 140 GLY   A CA  
1112 C  C   . GLY   A 139 ? 0.1605 0.0646 0.2080 -0.0397 -0.0408 -0.0110 140 GLY   A C   
1113 O  O   . GLY   A 139 ? 0.1720 0.1118 0.2492 -0.0264 -0.0504 -0.0147 140 GLY   A O   
1114 N  N   . LEU   A 140 ? 0.1298 0.0661 0.2973 -0.0083 -0.0394 -0.0297 141 LEU   A N   
1115 C  CA  . LEU   A 140 ? 0.1188 0.1147 0.2494 -0.0206 -0.0059 -0.0386 141 LEU   A CA  
1116 C  C   . LEU   A 140 ? 0.1283 0.1653 0.2187 -0.0182 -0.0078 -0.0367 141 LEU   A C   
1117 O  O   . LEU   A 140 ? 0.1414 0.0892 0.2226 0.0025  -0.0219 -0.0229 141 LEU   A O   
1118 C  CB  . LEU   A 140 ? 0.1242 0.1332 0.2430 -0.0018 0.0142  -0.0095 141 LEU   A CB  
1119 C  CG  . LEU   A 140 ? 0.1301 0.1529 0.3085 0.0138  0.0444  0.0286  141 LEU   A CG  
1120 C  CD1 . LEU   A 140 ? 0.1057 0.1648 0.2745 0.0392  0.0027  0.0230  141 LEU   A CD1 
1121 C  CD2 . LEU   A 140 ? 0.1856 0.1460 0.3471 -0.0035 0.0251  0.0545  141 LEU   A CD2 
1122 N  N   . ALA   A 141 ? 0.1230 0.1156 0.2217 0.0031  -0.0446 -0.0001 142 ALA   A N   
1123 C  CA  . ALA   A 141 ? 0.0748 0.0897 0.2767 0.0093  -0.0201 -0.0104 142 ALA   A CA  
1124 C  C   . ALA   A 141 ? 0.1314 0.1277 0.2213 -0.0003 -0.0222 0.0160  142 ALA   A C   
1125 O  O   . ALA   A 141 ? 0.1587 0.0994 0.2341 -0.0329 -0.0300 0.0168  142 ALA   A O   
1126 C  CB  . ALA   A 141 ? 0.0820 0.0865 0.2855 0.0088  -0.0131 -0.0261 142 ALA   A CB  
1127 N  N   . VAL   A 142 ? 0.0840 0.1342 0.2469 0.0033  -0.0529 0.0008  143 VAL   A N   
1128 C  CA  . VAL   A 142 ? 0.0757 0.1172 0.2626 -0.0069 -0.0062 -0.0019 143 VAL   A CA  
1129 C  C   . VAL   A 142 ? 0.1086 0.1119 0.1974 -0.0137 -0.0275 0.0013  143 VAL   A C   
1130 O  O   . VAL   A 142 ? 0.1316 0.1102 0.2185 -0.0053 -0.0463 0.0125  143 VAL   A O   
1131 C  CB  . VAL   A 142 ? 0.0897 0.0810 0.2254 0.0136  -0.0279 -0.0194 143 VAL   A CB  
1132 C  CG1 . VAL   A 142 ? 0.1371 0.1472 0.2433 0.0855  -0.0494 -0.0622 143 VAL   A CG1 
1133 C  CG2 . VAL   A 142 ? 0.1316 0.1531 0.2671 -0.0298 -0.0317 0.0243  143 VAL   A CG2 
1134 N  N   . LEU   A 143 ? 0.1106 0.0748 0.2218 0.0055  -0.0496 -0.0024 144 LEU   A N   
1135 C  CA  . LEU   A 143 ? 0.1076 0.0831 0.2143 -0.0001 -0.0491 0.0017  144 LEU   A CA  
1136 C  C   . LEU   A 143 ? 0.1027 0.1156 0.1777 -0.0282 -0.0176 0.0098  144 LEU   A C   
1137 O  O   . LEU   A 143 ? 0.1682 0.0803 0.1794 -0.0077 -0.0300 -0.0039 144 LEU   A O   
1138 C  CB  . LEU   A 143 ? 0.0967 0.1037 0.2332 -0.0106 -0.0432 0.0159  144 LEU   A CB  
1139 C  CG  . LEU   A 143 ? 0.0978 0.0846 0.2261 -0.0038 -0.0617 0.0052  144 LEU   A CG  
1140 C  CD1 . LEU   A 143 ? 0.1075 0.1955 0.2344 -0.0199 -0.0572 -0.0033 144 LEU   A CD1 
1141 C  CD2 . LEU   A 143 ? 0.1007 0.1436 0.2592 0.0400  -0.0692 -0.0369 144 LEU   A CD2 
1142 N  N   . GLY   A 144 ? 0.1306 0.0795 0.2348 -0.0011 -0.0409 0.0096  145 GLY   A N   
1143 C  CA  . GLY   A 144 ? 0.1493 0.0628 0.2217 -0.0168 -0.0356 -0.0066 145 GLY   A CA  
1144 C  C   . GLY   A 144 ? 0.1047 0.0908 0.1953 -0.0021 -0.0296 0.0018  145 GLY   A C   
1145 O  O   . GLY   A 144 ? 0.1278 0.0777 0.2182 -0.0138 -0.0179 0.0073  145 GLY   A O   
1146 N  N   . ILE   A 145 ? 0.0906 0.1050 0.2134 -0.0089 -0.0399 0.0058  146 ILE   A N   
1147 C  CA  . ILE   A 145 ? 0.0727 0.1036 0.2344 -0.0006 -0.0303 -0.0133 146 ILE   A CA  
1148 C  C   . ILE   A 145 ? 0.1571 0.0763 0.2111 -0.0013 -0.0297 -0.0125 146 ILE   A C   
1149 O  O   . ILE   A 145 ? 0.1454 0.0804 0.2401 -0.0285 -0.0170 -0.0182 146 ILE   A O   
1150 C  CB  . ILE   A 145 ? 0.1267 0.1045 0.2481 -0.0259 -0.0534 0.0307  146 ILE   A CB  
1151 C  CG1 . ILE   A 145 ? 0.1518 0.1526 0.2594 0.0325  -0.0636 0.0094  146 ILE   A CG1 
1152 C  CG2 . ILE   A 145 ? 0.1140 0.1163 0.3014 -0.0299 -0.0067 0.0067  146 ILE   A CG2 
1153 C  CD1 . ILE   A 145 ? 0.1565 0.1546 0.2620 -0.0174 -0.0888 0.0271  146 ILE   A CD1 
1154 N  N   . PHE   A 146 ? 0.1165 0.0979 0.2547 -0.0125 -0.0128 0.0062  147 PHE   A N   
1155 C  CA  . PHE   A 146 ? 0.1065 0.1342 0.2353 0.0347  -0.0302 0.0026  147 PHE   A CA  
1156 C  C   . PHE   A 146 ? 0.1413 0.1436 0.2328 -0.0093 -0.0008 -0.0136 147 PHE   A C   
1157 O  O   . PHE   A 146 ? 0.1374 0.1317 0.2537 -0.0164 -0.0279 -0.0178 147 PHE   A O   
1158 C  CB  . PHE   A 146 ? 0.1477 0.1205 0.2138 0.0374  -0.0376 -0.0032 147 PHE   A CB  
1159 C  CG  . PHE   A 146 ? 0.1411 0.0406 0.2174 0.0037  -0.0228 0.0131  147 PHE   A CG  
1160 C  CD1 . PHE   A 146 ? 0.1168 0.0946 0.2581 0.0087  -0.0283 -0.0208 147 PHE   A CD1 
1161 C  CD2 . PHE   A 146 ? 0.1600 0.0881 0.2165 -0.0417 -0.0098 0.0044  147 PHE   A CD2 
1162 C  CE1 . PHE   A 146 ? 0.2176 0.1029 0.1917 0.0088  -0.0380 -0.0035 147 PHE   A CE1 
1163 C  CE2 . PHE   A 146 ? 0.1269 0.0967 0.2492 -0.0379 -0.0255 0.0151  147 PHE   A CE2 
1164 C  CZ  . PHE   A 146 ? 0.1346 0.1073 0.2355 -0.0113 -0.0127 -0.0001 147 PHE   A CZ  
1165 N  N   . LEU   A 147 ? 0.1529 0.1472 0.1865 0.0058  -0.0173 -0.0058 148 LEU   A N   
1166 C  CA  . LEU   A 147 ? 0.1425 0.1030 0.2376 0.0295  -0.0318 -0.0260 148 LEU   A CA  
1167 C  C   . LEU   A 147 ? 0.1104 0.0983 0.2632 -0.0234 -0.0333 0.0100  148 LEU   A C   
1168 O  O   . LEU   A 147 ? 0.1004 0.1274 0.2952 -0.0259 -0.0316 0.0009  148 LEU   A O   
1169 C  CB  . LEU   A 147 ? 0.1601 0.1109 0.2404 -0.0043 -0.0586 -0.0136 148 LEU   A CB  
1170 C  CG  . LEU   A 147 ? 0.1671 0.1181 0.2272 0.0044  -0.0389 -0.0025 148 LEU   A CG  
1171 C  CD1 . LEU   A 147 ? 0.2269 0.1091 0.2629 -0.0093 -0.0376 -0.0078 148 LEU   A CD1 
1172 C  CD2 . LEU   A 147 ? 0.1892 0.1138 0.2170 0.0137  -0.0347 -0.0080 148 LEU   A CD2 
1173 N  N   . LYS   A 148 ? 0.1842 0.0498 0.2644 -0.0496 -0.0297 -0.0153 149 LYS   A N   
1174 C  CA  . LYS   A 148 ? 0.1838 0.0678 0.2238 0.0151  -0.0433 -0.0111 149 LYS   A CA  
1175 C  C   . LYS   A 148 ? 0.1693 0.1488 0.2552 0.0026  -0.0469 -0.0270 149 LYS   A C   
1176 O  O   . LYS   A 148 ? 0.1565 0.1526 0.2658 0.0088  -0.0389 -0.0042 149 LYS   A O   
1177 C  CB  . LYS   A 148 ? 0.1547 0.1381 0.2524 0.0053  -0.0633 0.0215  149 LYS   A CB  
1178 C  CG  . LYS   A 148 ? 0.1529 0.1493 0.3356 -0.0450 0.0149  0.0013  149 LYS   A CG  
1179 C  CD  . LYS   A 148 ? 0.3368 0.2795 0.3225 -0.1002 -0.0057 0.0506  149 LYS   A CD  
1180 C  CE  . LYS   A 148 ? 0.3445 0.5672 0.3337 -0.1407 -0.0144 0.1090  149 LYS   A CE  
1181 N  NZ  . LYS   A 148 ? 0.5870 0.6307 0.4555 -0.4103 -0.0416 0.1200  149 LYS   A NZ  
1182 N  N   . VAL   A 149 ? 0.2195 0.1104 0.2748 0.0231  -0.0501 -0.0066 150 VAL   A N   
1183 C  CA  . VAL   A 149 ? 0.1744 0.1485 0.2601 0.0044  -0.0006 -0.0354 150 VAL   A CA  
1184 C  C   . VAL   A 149 ? 0.1927 0.1788 0.2501 -0.0261 -0.0469 -0.0120 150 VAL   A C   
1185 O  O   . VAL   A 149 ? 0.2623 0.1756 0.3065 -0.0550 -0.0721 -0.0027 150 VAL   A O   
1186 C  CB  . VAL   A 149 ? 0.1772 0.1280 0.2649 -0.0186 0.0134  -0.0258 150 VAL   A CB  
1187 C  CG1 . VAL   A 149 ? 0.1763 0.2730 0.2688 0.0095  -0.0207 -0.0682 150 VAL   A CG1 
1188 C  CG2 . VAL   A 149 ? 0.1441 0.2066 0.3450 -0.0364 -0.0363 0.0096  150 VAL   A CG2 
1189 N  N   . GLY   A 150 ? 0.1675 0.0986 0.2900 -0.0486 -0.0552 -0.0259 151 GLY   A N   
1190 C  CA  . GLY   A 150 ? 0.1770 0.1766 0.3060 -0.0745 -0.0666 0.0147  151 GLY   A CA  
1191 C  C   . GLY   A 150 ? 0.1583 0.1115 0.2734 -0.0633 -0.0582 -0.0241 151 GLY   A C   
1192 O  O   . GLY   A 150 ? 0.1860 0.1359 0.3053 -0.0617 -0.0346 -0.0252 151 GLY   A O   
1193 N  N   A SER   A 151 ? 0.1845 0.1370 0.3255 -0.0438 -0.0266 -0.0167 152 SER   A N   
1194 N  N   B SER   A 151 ? 0.1908 0.1022 0.3345 -0.0433 -0.0370 -0.0315 152 SER   A N   
1195 C  CA  A SER   A 151 ? 0.2519 0.1849 0.2961 -0.0263 -0.0430 -0.0152 152 SER   A CA  
1196 C  CA  B SER   A 151 ? 0.2506 0.1337 0.2979 -0.0407 -0.0517 -0.0223 152 SER   A CA  
1197 C  C   A SER   A 151 ? 0.2402 0.1542 0.2315 0.0031  -0.0785 -0.0166 152 SER   A C   
1198 C  C   B SER   A 151 ? 0.2508 0.1009 0.2354 -0.0006 -0.0820 -0.0168 152 SER   A C   
1199 O  O   A SER   A 151 ? 0.1939 0.2472 0.2643 0.0240  -0.0834 -0.0597 152 SER   A O   
1200 O  O   B SER   A 151 ? 0.1978 0.2009 0.2575 0.0109  -0.0858 -0.0472 152 SER   A O   
1201 C  CB  A SER   A 151 ? 0.2751 0.3151 0.3756 -0.0113 -0.0111 -0.0326 152 SER   A CB  
1202 C  CB  B SER   A 151 ? 0.2494 0.0553 0.4024 -0.0421 -0.0408 -0.0220 152 SER   A CB  
1203 O  OG  A SER   A 151 ? 0.2866 0.4426 0.3343 -0.0272 0.0010  -0.0797 152 SER   A OG  
1204 O  OG  B SER   A 151 ? 0.2359 0.1910 0.4052 -0.0972 -0.0509 0.0785  152 SER   A OG  
1205 N  N   . ALA   A 152 ? 0.2160 0.1643 0.2336 -0.0104 -0.0649 -0.0013 153 ALA   A N   
1206 C  CA  . ALA   A 152 ? 0.2206 0.1558 0.2651 0.0100  -0.0214 0.0000  153 ALA   A CA  
1207 C  C   . ALA   A 152 ? 0.1691 0.1406 0.2677 -0.0229 -0.0642 -0.0308 153 ALA   A C   
1208 O  O   . ALA   A 152 ? 0.2287 0.1434 0.3393 0.0158  -0.0055 -0.0057 153 ALA   A O   
1209 C  CB  . ALA   A 152 ? 0.2630 0.2125 0.2661 -0.0091 -0.0197 -0.0085 153 ALA   A CB  
1210 N  N   . LYS   A 153 ? 0.1912 0.1057 0.3158 -0.0130 -0.0646 -0.0384 154 LYS   A N   
1211 C  CA  . LYS   A 153 ? 0.2257 0.1654 0.2579 0.0247  -0.0263 -0.0502 154 LYS   A CA  
1212 C  C   . LYS   A 153 ? 0.1617 0.1648 0.3193 0.0145  -0.0217 -0.0252 154 LYS   A C   
1213 O  O   . LYS   A 153 ? 0.1585 0.1597 0.3005 0.0031  -0.0473 0.0072  154 LYS   A O   
1214 C  CB  . LYS   A 153 ? 0.2169 0.1558 0.2671 -0.0010 -0.0342 -0.0146 154 LYS   A CB  
1215 C  CG  . LYS   A 153 ? 0.2763 0.1672 0.3339 0.0036  -0.0361 -0.0571 154 LYS   A CG  
1216 C  CD  . LYS   A 153 ? 0.3146 0.2005 0.3635 0.0370  0.0293  -0.0395 154 LYS   A CD  
1217 C  CE  . LYS   A 153 ? 0.3216 0.3220 0.2588 0.0920  -0.0310 -0.0344 154 LYS   A CE  
1218 N  NZ  . LYS   A 153 ? 0.3074 0.5190 0.2841 0.0855  -0.0201 0.0296  154 LYS   A NZ  
1219 N  N   . PRO   A 154 ? 0.1544 0.1766 0.3474 -0.0266 -0.0432 0.0445  155 PRO   A N   
1220 C  CA  . PRO   A 154 ? 0.0961 0.2228 0.3539 -0.0598 -0.0511 0.0708  155 PRO   A CA  
1221 C  C   . PRO   A 154 ? 0.1770 0.1526 0.2859 0.0227  -0.0453 0.0139  155 PRO   A C   
1222 O  O   . PRO   A 154 ? 0.2124 0.2224 0.3046 0.0158  -0.0428 0.0535  155 PRO   A O   
1223 C  CB  . PRO   A 154 ? 0.1012 0.1489 0.4811 -0.0499 -0.0331 0.0359  155 PRO   A CB  
1224 C  CG  . PRO   A 154 ? 0.2125 0.3184 0.4780 0.0166  -0.0559 0.1544  155 PRO   A CG  
1225 C  CD  . PRO   A 154 ? 0.1726 0.2407 0.3828 -0.0088 -0.0082 0.0613  155 PRO   A CD  
1226 N  N   . GLY   A 155 ? 0.1587 0.1547 0.3206 0.0212  -0.0542 -0.0201 156 GLY   A N   
1227 C  CA  . GLY   A 155 ? 0.1289 0.1640 0.3085 0.0132  -0.0175 -0.0032 156 GLY   A CA  
1228 C  C   . GLY   A 155 ? 0.1296 0.1993 0.2970 -0.0282 -0.0230 0.0458  156 GLY   A C   
1229 O  O   . GLY   A 155 ? 0.2080 0.1903 0.3639 -0.0385 -0.0303 0.0429  156 GLY   A O   
1230 N  N   . LEU   A 156 ? 0.2197 0.1729 0.3144 -0.0142 0.0069  -0.0098 157 LEU   A N   
1231 C  CA  . LEU   A 156 ? 0.1891 0.1877 0.2712 -0.0026 -0.0591 0.0153  157 LEU   A CA  
1232 C  C   . LEU   A 156 ? 0.1967 0.1697 0.2581 -0.0381 -0.0663 0.0136  157 LEU   A C   
1233 O  O   . LEU   A 156 ? 0.1587 0.1526 0.2837 -0.0052 -0.0598 -0.0183 157 LEU   A O   
1234 C  CB  . LEU   A 156 ? 0.1280 0.1636 0.2838 -0.0159 -0.0606 0.0077  157 LEU   A CB  
1235 C  CG  . LEU   A 156 ? 0.1210 0.1626 0.2892 -0.0344 -0.0746 -0.0076 157 LEU   A CG  
1236 C  CD1 . LEU   A 156 ? 0.2262 0.1601 0.2816 -0.0523 -0.0888 -0.0262 157 LEU   A CD1 
1237 C  CD2 . LEU   A 156 ? 0.1565 0.2089 0.2962 -0.0013 -0.0685 0.0006  157 LEU   A CD2 
1238 N  N   . GLN   A 157 ? 0.1977 0.1881 0.2395 -0.0326 -0.0630 -0.0044 158 GLN   A N   
1239 C  CA  . GLN   A 157 ? 0.1867 0.1700 0.2463 -0.0637 -0.0620 0.0154  158 GLN   A CA  
1240 C  C   . GLN   A 157 ? 0.1824 0.1612 0.2221 -0.0302 -0.0502 0.0055  158 GLN   A C   
1241 O  O   . GLN   A 157 ? 0.2082 0.1409 0.3083 -0.0442 -0.0314 -0.0225 158 GLN   A O   
1242 C  CB  . GLN   A 157 ? 0.1556 0.2357 0.3008 -0.0901 -0.0403 0.0034  158 GLN   A CB  
1243 C  CG  . GLN   A 157 ? 0.1625 0.2370 0.3917 -0.0299 -0.0345 -0.0197 158 GLN   A CG  
1244 C  CD  . GLN   A 157 ? 0.1817 0.1734 0.3018 -0.0507 -0.0311 -0.0241 158 GLN   A CD  
1245 O  OE1 . GLN   A 157 ? 0.2292 0.2020 0.2916 -0.0591 -0.0312 -0.0168 158 GLN   A OE1 
1246 N  NE2 . GLN   A 157 ? 0.2093 0.1619 0.3149 -0.0468 -0.0389 -0.0044 158 GLN   A NE2 
1247 N  N   . LYS   A 158 ? 0.1554 0.1694 0.3151 -0.0027 -0.0700 -0.0099 159 LYS   A N   
1248 C  CA  . LYS   A 158 ? 0.1658 0.2527 0.2665 -0.0422 -0.0679 -0.0034 159 LYS   A CA  
1249 C  C   . LYS   A 158 ? 0.1765 0.1500 0.2697 -0.0518 -0.0528 -0.0245 159 LYS   A C   
1250 O  O   . LYS   A 158 ? 0.2086 0.2537 0.2754 -0.0675 -0.0734 0.0009  159 LYS   A O   
1251 C  CB  . LYS   A 158 ? 0.2310 0.2989 0.3396 0.0386  -0.0878 -0.0466 159 LYS   A CB  
1252 C  CG  . LYS   A 158 ? 0.3021 0.4186 0.3875 -0.0456 -0.1474 -0.0018 159 LYS   A CG  
1253 N  N   . VAL   A 159 ? 0.1346 0.1873 0.2865 -0.0208 -0.0668 0.0156  160 VAL   A N   
1254 C  CA  . VAL   A 159 ? 0.1190 0.1937 0.2330 -0.0105 -0.0286 -0.0085 160 VAL   A CA  
1255 C  C   . VAL   A 159 ? 0.1999 0.1679 0.2522 -0.0149 -0.0047 -0.0238 160 VAL   A C   
1256 O  O   . VAL   A 159 ? 0.1366 0.1696 0.2871 -0.0066 -0.0442 -0.0024 160 VAL   A O   
1257 C  CB  . VAL   A 159 ? 0.0838 0.1967 0.2504 0.0106  -0.0514 -0.0135 160 VAL   A CB  
1258 C  CG1 . VAL   A 159 ? 0.0767 0.1874 0.2957 -0.0241 -0.0476 -0.0131 160 VAL   A CG1 
1259 C  CG2 . VAL   A 159 ? 0.2039 0.1849 0.2776 0.0096  -0.0089 -0.0351 160 VAL   A CG2 
1260 N  N   . VAL   A 160 ? 0.2013 0.1533 0.2774 -0.0267 -0.0439 -0.0402 161 VAL   A N   
1261 C  CA  . VAL   A 160 ? 0.1720 0.1905 0.2892 -0.0286 0.0215  -0.0139 161 VAL   A CA  
1262 C  C   . VAL   A 160 ? 0.2080 0.1418 0.2883 -0.0383 -0.0083 0.0022  161 VAL   A C   
1263 O  O   . VAL   A 160 ? 0.2652 0.1790 0.2641 -0.0517 0.0099  -0.0613 161 VAL   A O   
1264 C  CB  . VAL   A 160 ? 0.3715 0.0978 0.3257 0.0240  0.0143  0.0392  161 VAL   A CB  
1265 C  CG1 . VAL   A 160 ? 0.2970 0.2002 0.3856 0.0093  -0.0871 -0.0528 161 VAL   A CG1 
1266 C  CG2 . VAL   A 160 ? 0.4480 0.1353 0.3251 0.0498  0.0004  0.0179  161 VAL   A CG2 
1267 N  N   . ASP   A 161 ? 0.2061 0.1689 0.2748 -0.0537 -0.0468 -0.0348 162 ASP   A N   
1268 C  CA  . ASP   A 161 ? 0.2370 0.1985 0.2819 -0.0212 -0.0262 0.0394  162 ASP   A CA  
1269 C  C   . ASP   A 161 ? 0.2641 0.2030 0.2375 -0.0737 -0.0422 -0.0225 162 ASP   A C   
1270 O  O   . ASP   A 161 ? 0.3790 0.2550 0.3109 -0.1104 0.0148  -0.0424 162 ASP   A O   
1271 C  CB  . ASP   A 161 ? 0.2480 0.2671 0.3076 -0.0759 -0.0348 -0.0121 162 ASP   A CB  
1272 C  CG  . ASP   A 161 ? 0.2781 0.3050 0.3463 -0.1212 -0.0462 -0.0487 162 ASP   A CG  
1273 O  OD1 . ASP   A 161 ? 0.3351 0.3500 0.4553 -0.0576 -0.0377 0.0389  162 ASP   A OD1 
1274 O  OD2 . ASP   A 161 ? 0.2976 0.4215 0.4632 -0.0127 0.0826  -0.0134 162 ASP   A OD2 
1275 N  N   . VAL   A 162 ? 0.2253 0.1790 0.2503 -0.0356 -0.0468 -0.0272 163 VAL   A N   
1276 C  CA  . VAL   A 162 ? 0.1773 0.2290 0.2615 -0.0219 -0.0834 0.0055  163 VAL   A CA  
1277 C  C   . VAL   A 162 ? 0.1795 0.2057 0.2323 -0.0145 -0.0289 0.0227  163 VAL   A C   
1278 O  O   . VAL   A 162 ? 0.2269 0.1565 0.2740 -0.0184 -0.0125 0.0335  163 VAL   A O   
1279 C  CB  . VAL   A 162 ? 0.2391 0.2286 0.2794 0.0070  -0.0427 0.0234  163 VAL   A CB  
1280 C  CG1 . VAL   A 162 ? 0.2643 0.2649 0.3252 0.0084  -0.0669 -0.0660 163 VAL   A CG1 
1281 C  CG2 . VAL   A 162 ? 0.2731 0.2260 0.3995 0.0165  0.0219  0.0343  163 VAL   A CG2 
1282 N  N   . LEU   A 163 ? 0.2095 0.1709 0.3177 -0.0480 -0.0793 0.0138  164 LEU   A N   
1283 C  CA  . LEU   A 163 ? 0.2091 0.1985 0.2009 -0.0239 -0.0491 -0.0069 164 LEU   A CA  
1284 C  C   . LEU   A 163 ? 0.2293 0.1712 0.2297 0.0062  -0.0277 -0.0053 164 LEU   A C   
1285 O  O   . LEU   A 163 ? 0.2268 0.1797 0.2678 0.0077  -0.0465 0.0035  164 LEU   A O   
1286 C  CB  . LEU   A 163 ? 0.2420 0.1743 0.2129 -0.0351 -0.0286 -0.0131 164 LEU   A CB  
1287 C  CG  . LEU   A 163 ? 0.2301 0.1287 0.2432 -0.0451 0.0059  -0.0127 164 LEU   A CG  
1288 C  CD1 . LEU   A 163 ? 0.2418 0.1502 0.3328 -0.0567 -0.0422 0.0414  164 LEU   A CD1 
1289 C  CD2 . LEU   A 163 ? 0.1740 0.1183 0.2924 -0.0178 -0.0182 -0.0284 164 LEU   A CD2 
1290 N  N   . ASP   A 164 ? 0.3765 0.1312 0.2624 -0.0188 -0.0073 -0.0462 165 ASP   A N   
1291 C  CA  . ASP   A 164 ? 0.3894 0.2132 0.2584 -0.0173 -0.0307 -0.0730 165 ASP   A CA  
1292 C  C   . ASP   A 164 ? 0.3200 0.3066 0.2276 -0.0325 -0.0326 -0.0223 165 ASP   A C   
1293 O  O   . ASP   A 164 ? 0.4528 0.2325 0.3261 0.0236  0.0825  0.0496  165 ASP   A O   
1294 C  CB  . ASP   A 164 ? 0.6998 0.3001 0.3352 -0.0753 -0.1479 -0.1083 165 ASP   A CB  
1295 C  CG  . ASP   A 164 ? 0.8468 1.1531 0.6619 -0.0381 -0.2953 -0.1766 165 ASP   A CG  
1296 O  OD1 . ASP   A 164 ? 1.1755 0.7343 0.8064 -0.7602 -0.3558 0.2210  165 ASP   A OD1 
1297 O  OD2 . ASP   A 164 ? 2.0005 0.6972 0.7245 -0.2491 -0.2730 0.1010  165 ASP   A OD2 
1298 N  N   . SER   A 165 ? 0.2764 0.2610 0.2642 -0.0480 -0.0449 -0.0322 166 SER   A N   
1299 C  CA  . SER   A 165 ? 0.2207 0.2596 0.2568 -0.0385 -0.0656 -0.0099 166 SER   A CA  
1300 C  C   . SER   A 165 ? 0.2032 0.2170 0.2139 -0.0058 -0.0414 -0.0135 166 SER   A C   
1301 O  O   . SER   A 165 ? 0.2334 0.2319 0.2451 0.0087  -0.0307 0.0220  166 SER   A O   
1302 C  CB  . SER   A 165 ? 0.3086 0.2931 0.3028 0.0403  -0.0272 0.0357  166 SER   A CB  
1303 O  OG  . SER   A 165 ? 0.2815 0.2262 0.3563 0.0566  -0.0658 0.0322  166 SER   A OG  
1304 N  N   . ILE   A 166 ? 0.1941 0.1791 0.1912 0.0190  -0.0607 -0.0358 167 ILE   A N   
1305 C  CA  . ILE   A 166 ? 0.1877 0.1429 0.2388 -0.0259 -0.0424 -0.0031 167 ILE   A CA  
1306 C  C   . ILE   A 166 ? 0.2064 0.1332 0.2280 -0.0217 -0.0111 0.0097  167 ILE   A C   
1307 O  O   . ILE   A 166 ? 0.1296 0.1414 0.2533 0.0097  -0.0321 -0.0066 167 ILE   A O   
1308 C  CB  . ILE   A 166 ? 0.1892 0.1474 0.2312 0.0271  -0.0293 0.0127  167 ILE   A CB  
1309 C  CG1 . ILE   A 166 ? 0.1590 0.1747 0.2215 -0.0228 -0.0568 -0.0002 167 ILE   A CG1 
1310 C  CG2 . ILE   A 166 ? 0.1830 0.1486 0.3139 0.0302  -0.0576 0.0248  167 ILE   A CG2 
1311 C  CD1 . ILE   A 166 ? 0.1842 0.2444 0.2407 -0.0467 -0.0160 -0.0126 167 ILE   A CD1 
1312 N  N   . LYS   A 167 ? 0.2160 0.1835 0.2262 0.0392  0.0075  0.0211  168 LYS   A N   
1313 C  CA  . LYS   A 167 ? 0.1827 0.1456 0.2488 0.0114  -0.0305 -0.0195 168 LYS   A CA  
1314 C  C   . LYS   A 167 ? 0.2634 0.1885 0.1991 -0.0580 -0.0412 -0.0142 168 LYS   A C   
1315 O  O   . LYS   A 167 ? 0.1935 0.1653 0.2409 0.0164  -0.0137 0.0022  168 LYS   A O   
1316 C  CB  . LYS   A 167 ? 0.2218 0.1515 0.2485 0.0228  -0.0157 -0.0263 168 LYS   A CB  
1317 C  CG  . LYS   A 167 ? 0.1291 0.2104 0.3123 0.0269  -0.0429 -0.0185 168 LYS   A CG  
1318 C  CD  . LYS   A 167 ? 0.3299 0.2790 0.4441 0.1034  -0.0851 -0.1579 168 LYS   A CD  
1319 C  CE  . LYS   A 167 ? 0.3871 0.2706 0.4518 0.0653  -0.0247 -0.0681 168 LYS   A CE  
1320 N  NZ  . LYS   A 167 ? 0.4521 0.5104 0.5565 -0.0192 0.0595  -0.2231 168 LYS   A NZ  
1321 N  N   . THR   A 168 ? 0.1757 0.1718 0.2316 -0.0033 -0.0009 0.0132  169 THR   A N   
1322 C  CA  . THR   A 168 ? 0.2129 0.1061 0.2644 0.0010  -0.0212 -0.0279 169 THR   A CA  
1323 C  C   . THR   A 168 ? 0.1658 0.0917 0.2645 0.0001  -0.0335 -0.0054 169 THR   A C   
1324 O  O   . THR   A 168 ? 0.1557 0.1353 0.2754 0.0219  -0.0252 0.0076  169 THR   A O   
1325 C  CB  . THR   A 168 ? 0.2488 0.1165 0.2495 0.0017  -0.0134 -0.0179 169 THR   A CB  
1326 O  OG1 . THR   A 168 ? 0.2161 0.1783 0.2713 -0.0051 -0.0080 0.0083  169 THR   A OG1 
1327 C  CG2 . THR   A 168 ? 0.2397 0.1223 0.2426 -0.0149 0.0346  -0.0310 169 THR   A CG2 
1328 N  N   . LYS   A 169 ? 0.1517 0.1934 0.2701 -0.0005 -0.0421 -0.0061 170 LYS   A N   
1329 C  CA  . LYS   A 169 ? 0.1831 0.1377 0.2637 0.0009  -0.0388 0.0286  170 LYS   A CA  
1330 C  C   . LYS   A 169 ? 0.1738 0.1439 0.2066 -0.0072 -0.0178 0.0140  170 LYS   A C   
1331 O  O   . LYS   A 169 ? 0.2427 0.1568 0.2294 0.0107  0.0155  0.0214  170 LYS   A O   
1332 C  CB  . LYS   A 169 ? 0.1784 0.1248 0.2602 -0.0144 -0.0482 0.0324  170 LYS   A CB  
1333 C  CG  . LYS   A 169 ? 0.2125 0.1636 0.3118 -0.0412 -0.0731 0.0135  170 LYS   A CG  
1334 C  CD  . LYS   A 169 ? 0.2253 0.2902 0.2685 -0.0314 -0.0710 0.0455  170 LYS   A CD  
1335 C  CE  . LYS   A 169 ? 0.3456 0.4171 0.3162 0.0174  -0.0065 0.0139  170 LYS   A CE  
1336 N  NZ  . LYS   A 169 ? 0.4216 0.5036 0.4051 -0.0135 -0.0665 0.1449  170 LYS   A NZ  
1337 N  N   . GLY   A 170 ? 0.1590 0.1391 0.2646 -0.0100 -0.0155 0.0025  171 GLY   A N   
1338 C  CA  . GLY   A 170 ? 0.1630 0.1434 0.2503 0.0049  -0.0134 0.0204  171 GLY   A CA  
1339 C  C   . GLY   A 170 ? 0.1744 0.1204 0.2998 0.0126  -0.0318 -0.0147 171 GLY   A C   
1340 O  O   . GLY   A 170 ? 0.2178 0.1626 0.3619 0.0231  -0.0341 0.0536  171 GLY   A O   
1341 N  N   . LYS   A 171 ? 0.1493 0.1370 0.2267 -0.0097 -0.0305 -0.0058 172 LYS   A N   
1342 C  CA  . LYS   A 171 ? 0.1465 0.1639 0.2617 0.0009  -0.0210 0.0078  172 LYS   A CA  
1343 C  C   . LYS   A 171 ? 0.1834 0.1691 0.2337 -0.0109 0.0005  0.0103  172 LYS   A C   
1344 O  O   . LYS   A 171 ? 0.1747 0.1788 0.2554 0.0172  -0.0407 0.0052  172 LYS   A O   
1345 C  CB  . LYS   A 171 ? 0.1655 0.1596 0.3076 -0.0184 0.0178  -0.0218 172 LYS   A CB  
1346 C  CG  . LYS   A 171 ? 0.1960 0.2237 0.3058 0.0381  0.0109  -0.0710 172 LYS   A CG  
1347 C  CD  . LYS   A 171 ? 0.3221 0.2679 0.4244 0.0044  -0.1033 -0.0886 172 LYS   A CD  
1348 C  CE  . LYS   A 171 ? 0.3101 0.3735 0.3876 -0.0178 -0.1059 -0.0761 172 LYS   A CE  
1349 N  NZ  . LYS   A 171 ? 0.4287 0.2465 0.4138 -0.0472 0.0321  -0.0483 172 LYS   A NZ  
1350 N  N   . SER   A 172 ? 0.1841 0.2096 0.2139 0.0107  -0.0157 0.0125  173 SER   A N   
1351 C  CA  . SER   A 172 ? 0.1772 0.1987 0.2273 -0.0116 -0.0227 -0.0333 173 SER   A CA  
1352 C  C   . SER   A 172 ? 0.1955 0.1964 0.1975 -0.0125 -0.0232 0.0037  173 SER   A C   
1353 O  O   . SER   A 172 ? 0.1920 0.2547 0.2054 0.0469  -0.0232 0.0138  173 SER   A O   
1354 C  CB  . SER   A 172 ? 0.2171 0.1944 0.2383 0.0250  -0.0251 -0.0385 173 SER   A CB  
1355 O  OG  . SER   A 172 ? 0.2133 0.2656 0.3037 0.0332  -0.0245 0.0138  173 SER   A OG  
1356 N  N   . ALA   A 173 ? 0.1734 0.2509 0.2208 -0.0203 -0.0491 0.0304  174 ALA   A N   
1357 C  CA  . ALA   A 173 ? 0.1938 0.2269 0.2699 0.0066  -0.0785 0.0071  174 ALA   A CA  
1358 C  C   . ALA   A 173 ? 0.2118 0.2031 0.2147 -0.0055 -0.0545 0.0146  174 ALA   A C   
1359 O  O   . ALA   A 173 ? 0.1673 0.1777 0.2228 0.0222  -0.0586 0.0217  174 ALA   A O   
1360 C  CB  . ALA   A 173 ? 0.2345 0.2006 0.2560 0.0400  -0.0731 -0.0440 174 ALA   A CB  
1361 N  N   . ASP   A 174 ? 0.1999 0.2470 0.2196 0.0433  -0.0402 0.0265  175 ASP   A N   
1362 C  CA  . ASP   A 174 ? 0.2073 0.2869 0.2366 0.0608  -0.0184 0.0653  175 ASP   A CA  
1363 C  C   . ASP   A 174 ? 0.2743 0.1781 0.1777 0.0351  -0.0753 0.0414  175 ASP   A C   
1364 O  O   . ASP   A 174 ? 0.2497 0.2268 0.3256 0.0286  -0.0312 -0.0479 175 ASP   A O   
1365 C  CB  . ASP   A 174 ? 0.2621 0.3537 0.3107 0.0289  -0.0908 0.1154  175 ASP   A CB  
1366 C  CG  . ASP   A 174 ? 0.4867 0.2391 0.4028 -0.0052 -0.0983 0.0644  175 ASP   A CG  
1367 O  OD1 . ASP   A 174 ? 0.7673 0.5138 0.4538 -0.1294 -0.2479 -0.0029 175 ASP   A OD1 
1368 O  OD2 . ASP   A 174 ? 0.6003 0.5796 0.4194 0.0363  -0.0763 0.0732  175 ASP   A OD2 
1369 N  N   . PHE   A 175 ? 0.1755 0.2233 0.2106 0.0096  -0.0406 0.0229  176 PHE   A N   
1370 C  CA  . PHE   A 175 ? 0.1949 0.2020 0.2485 0.0299  -0.0249 0.0413  176 PHE   A CA  
1371 C  C   . PHE   A 175 ? 0.1637 0.1479 0.2334 -0.0508 -0.0198 0.0159  176 PHE   A C   
1372 O  O   . PHE   A 175 ? 0.2268 0.2420 0.2702 0.0462  -0.0820 -0.0137 176 PHE   A O   
1373 C  CB  . PHE   A 175 ? 0.2444 0.1423 0.2375 -0.0089 -0.0543 0.0473  176 PHE   A CB  
1374 C  CG  . PHE   A 175 ? 0.1809 0.1305 0.2693 0.0139  -0.0479 0.0306  176 PHE   A CG  
1375 C  CD1 . PHE   A 175 ? 0.2760 0.1605 0.2666 0.0094  -0.0399 0.0133  176 PHE   A CD1 
1376 C  CD2 . PHE   A 175 ? 0.1375 0.1515 0.2799 0.0318  -0.0440 0.0157  176 PHE   A CD2 
1377 C  CE1 . PHE   A 175 ? 0.3033 0.1199 0.2822 0.0285  -0.0102 0.0055  176 PHE   A CE1 
1378 C  CE2 . PHE   A 175 ? 0.1342 0.1751 0.3233 0.0155  -0.0158 0.0127  176 PHE   A CE2 
1379 C  CZ  . PHE   A 175 ? 0.2670 0.1707 0.2976 0.0307  0.0151  -0.0016 176 PHE   A CZ  
1380 N  N   . THR   A 176 ? 0.2158 0.2430 0.2725 0.0295  -0.0505 0.0263  177 THR   A N   
1381 C  CA  . THR   A 176 ? 0.1973 0.1978 0.2597 0.0110  -0.0302 0.0659  177 THR   A CA  
1382 C  C   . THR   A 176 ? 0.1668 0.1880 0.2079 0.0125  -0.0333 0.0227  177 THR   A C   
1383 O  O   . THR   A 176 ? 0.1806 0.1881 0.2671 0.0194  -0.0306 0.0050  177 THR   A O   
1384 C  CB  . THR   A 176 ? 0.2070 0.2292 0.2794 -0.0480 -0.0944 0.0949  177 THR   A CB  
1385 O  OG1 . THR   A 176 ? 0.3137 0.2771 0.2560 0.0873  -0.0479 0.0332  177 THR   A OG1 
1386 C  CG2 . THR   A 176 ? 0.3228 0.2279 0.3689 -0.0864 -0.0368 0.1380  177 THR   A CG2 
1387 N  N   . ASN   A 177 ? 0.1680 0.1766 0.2390 0.0008  -0.0199 0.0178  178 ASN   A N   
1388 C  CA  . ASN   A 177 ? 0.1744 0.1661 0.2841 -0.0060 -0.0322 0.0240  178 ASN   A CA  
1389 C  C   . ASN   A 177 ? 0.1353 0.1762 0.2643 0.0009  -0.0379 0.0284  178 ASN   A C   
1390 O  O   . ASN   A 177 ? 0.1932 0.1654 0.3705 -0.0290 -0.0847 0.0815  178 ASN   A O   
1391 C  CB  . ASN   A 177 ? 0.2054 0.1585 0.2820 -0.0200 -0.0500 0.0880  178 ASN   A CB  
1392 C  CG  . ASN   A 177 ? 0.1766 0.1515 0.3037 0.0094  -0.0093 0.0653  178 ASN   A CG  
1393 O  OD1 . ASN   A 177 ? 0.1966 0.2170 0.3281 0.0243  0.0013  0.0027  178 ASN   A OD1 
1394 N  ND2 . ASN   A 177 ? 0.2103 0.2434 0.2660 -0.0443 -0.0216 0.0449  178 ASN   A ND2 
1395 N  N   . PHE   A 178 ? 0.1838 0.1761 0.2134 0.0006  -0.0697 0.0195  179 PHE   A N   
1396 C  CA  . PHE   A 178 ? 0.1411 0.1916 0.2449 -0.0091 -0.0389 0.0460  179 PHE   A CA  
1397 C  C   . PHE   A 178 ? 0.1389 0.1529 0.2434 0.0274  -0.0413 0.0159  179 PHE   A C   
1398 O  O   . PHE   A 178 ? 0.2045 0.2715 0.2525 -0.0142 -0.0576 -0.0398 179 PHE   A O   
1399 C  CB  . PHE   A 178 ? 0.1632 0.2072 0.2290 0.0178  -0.0402 0.0563  179 PHE   A CB  
1400 C  CG  . PHE   A 178 ? 0.1464 0.1759 0.2243 -0.0268 -0.0158 0.0446  179 PHE   A CG  
1401 C  CD1 . PHE   A 178 ? 0.1860 0.1553 0.2580 -0.0055 -0.0590 0.0381  179 PHE   A CD1 
1402 C  CD2 . PHE   A 178 ? 0.0743 0.2430 0.2150 0.0365  -0.0251 0.0578  179 PHE   A CD2 
1403 C  CE1 . PHE   A 178 ? 0.2623 0.2181 0.2514 -0.0032 -0.0622 0.0795  179 PHE   A CE1 
1404 C  CE2 . PHE   A 178 ? 0.1273 0.1935 0.2363 0.0161  -0.0505 0.0312  179 PHE   A CE2 
1405 C  CZ  . PHE   A 178 ? 0.1313 0.1989 0.2454 0.0230  -0.0533 0.0418  179 PHE   A CZ  
1406 N  N   . ASP   A 179 ? 0.1583 0.2419 0.2474 -0.0086 -0.0273 0.0345  180 ASP   A N   
1407 C  CA  . ASP   A 179 ? 0.1263 0.1662 0.2230 -0.0115 -0.0583 0.0405  180 ASP   A CA  
1408 C  C   . ASP   A 179 ? 0.1862 0.1726 0.1985 -0.0095 -0.0405 0.0425  180 ASP   A C   
1409 O  O   . ASP   A 179 ? 0.1152 0.1722 0.2993 -0.0240 -0.0296 -0.0100 180 ASP   A O   
1410 C  CB  . ASP   A 179 ? 0.1156 0.2492 0.2622 0.0067  -0.0128 0.0571  180 ASP   A CB  
1411 C  CG  . ASP   A 179 ? 0.1418 0.2647 0.3119 0.0013  0.0096  0.0055  180 ASP   A CG  
1412 O  OD1 . ASP   A 179 ? 0.2297 0.2267 0.2592 0.0373  0.0051  0.0218  180 ASP   A OD1 
1413 O  OD2 . ASP   A 179 ? 0.1511 0.5067 0.4463 -0.0907 -0.0792 -0.0326 180 ASP   A OD2 
1414 N  N   . PRO   A 180 ? 0.1467 0.1450 0.2074 -0.0099 -0.0155 0.0157  181 PRO   A N   
1415 C  CA  . PRO   A 180 ? 0.1639 0.1540 0.2467 -0.0125 -0.0377 0.0381  181 PRO   A CA  
1416 C  C   . PRO   A 180 ? 0.1244 0.2086 0.2192 -0.0008 -0.0346 0.0278  181 PRO   A C   
1417 O  O   . PRO   A 180 ? 0.2062 0.1263 0.2301 -0.0201 -0.0452 0.0167  181 PRO   A O   
1418 C  CB  . PRO   A 180 ? 0.1384 0.1758 0.2738 0.0044  -0.0680 0.0447  181 PRO   A CB  
1419 C  CG  . PRO   A 180 ? 0.1241 0.1680 0.2641 -0.0019 -0.0723 0.0424  181 PRO   A CG  
1420 C  CD  . PRO   A 180 ? 0.1787 0.1470 0.2147 -0.0243 -0.0270 0.0184  181 PRO   A CD  
1421 N  N   . ARG   A 181 ? 0.1150 0.1830 0.2122 -0.0142 -0.0089 0.0062  182 ARG   A N   
1422 C  CA  . ARG   A 181 ? 0.1090 0.1687 0.2657 -0.0074 0.0013  0.0089  182 ARG   A CA  
1423 C  C   . ARG   A 181 ? 0.1690 0.1944 0.2339 0.0057  -0.0633 -0.0035 182 ARG   A C   
1424 O  O   . ARG   A 181 ? 0.1569 0.2300 0.3009 -0.0215 -0.0531 0.0485  182 ARG   A O   
1425 C  CB  . ARG   A 181 ? 0.1229 0.2043 0.3140 0.0124  -0.0136 0.0075  182 ARG   A CB  
1426 C  CG  . ARG   A 181 ? 0.1874 0.1872 0.3054 -0.0002 -0.0029 0.0198  182 ARG   A CG  
1427 C  CD  . ARG   A 181 ? 0.2278 0.1806 0.2993 0.0355  0.0092  -0.0124 182 ARG   A CD  
1428 N  NE  . ARG   A 181 ? 0.1625 0.1892 0.3362 -0.0499 -0.0263 0.0276  182 ARG   A NE  
1429 C  CZ  . ARG   A 181 ? 0.2558 0.3569 0.3696 0.0974  -0.0012 -0.0298 182 ARG   A CZ  
1430 N  NH1 . ARG   A 181 ? 0.2598 0.3838 0.4246 0.1403  0.0634  0.0344  182 ARG   A NH1 
1431 N  NH2 . ARG   A 181 ? 0.2802 0.4121 0.3741 0.0946  0.0179  0.0196  182 ARG   A NH2 
1432 N  N   . GLY   A 182 ? 0.1289 0.1942 0.2382 0.0077  -0.0653 -0.0096 183 GLY   A N   
1433 C  CA  . GLY   A 182 ? 0.1507 0.1745 0.3087 0.0184  -0.0669 0.0042  183 GLY   A CA  
1434 C  C   . GLY   A 182 ? 0.1768 0.1362 0.2671 0.0190  -0.0571 -0.0034 183 GLY   A C   
1435 O  O   . GLY   A 182 ? 0.2432 0.1251 0.4036 0.0072  -0.0751 0.0212  183 GLY   A O   
1436 N  N   . LEU   A 183 ? 0.1775 0.1639 0.2782 -0.0223 -0.0664 0.0214  184 LEU   A N   
1437 C  CA  . LEU   A 183 ? 0.1579 0.1605 0.2391 -0.0134 -0.0250 0.0082  184 LEU   A CA  
1438 C  C   . LEU   A 183 ? 0.1740 0.1587 0.2393 -0.0358 -0.0252 0.0251  184 LEU   A C   
1439 O  O   . LEU   A 183 ? 0.2007 0.1910 0.2902 0.0222  -0.0286 0.0340  184 LEU   A O   
1440 C  CB  . LEU   A 183 ? 0.1637 0.1328 0.2440 -0.0092 -0.0337 0.0272  184 LEU   A CB  
1441 C  CG  . LEU   A 183 ? 0.1880 0.1567 0.2368 -0.0494 -0.0304 0.0124  184 LEU   A CG  
1442 C  CD1 . LEU   A 183 ? 0.1423 0.2727 0.2732 -0.0456 -0.0204 0.0517  184 LEU   A CD1 
1443 C  CD2 . LEU   A 183 ? 0.2669 0.2113 0.3152 0.0512  -0.0219 -0.0449 184 LEU   A CD2 
1444 N  N   . LEU   A 184 ? 0.1511 0.1661 0.2574 -0.0211 -0.0365 0.0064  185 LEU   A N   
1445 C  CA  . LEU   A 184 ? 0.1535 0.1298 0.2502 -0.0329 -0.0329 0.0287  185 LEU   A CA  
1446 C  C   . LEU   A 184 ? 0.1790 0.1567 0.2695 -0.0648 -0.0908 0.0558  185 LEU   A C   
1447 O  O   . LEU   A 184 ? 0.2473 0.2477 0.3383 -0.1215 -0.1394 0.0629  185 LEU   A O   
1448 C  CB  . LEU   A 184 ? 0.1258 0.1813 0.2512 -0.0222 -0.0416 -0.0103 185 LEU   A CB  
1449 C  CG  . LEU   A 184 ? 0.1156 0.2029 0.2732 -0.0239 -0.0466 -0.0032 185 LEU   A CG  
1450 C  CD1 . LEU   A 184 ? 0.1712 0.2544 0.2937 0.0189  -0.0312 -0.0454 185 LEU   A CD1 
1451 C  CD2 . LEU   A 184 ? 0.1416 0.1786 0.3073 -0.0546 -0.0783 0.0145  185 LEU   A CD2 
1452 N  N   . PRO   A 185 ? 0.1169 0.1669 0.2759 -0.0164 -0.0541 0.0776  186 PRO   A N   
1453 C  CA  . PRO   A 185 ? 0.1604 0.1396 0.2551 -0.0245 -0.0221 0.0458  186 PRO   A CA  
1454 C  C   . PRO   A 185 ? 0.1741 0.1335 0.2767 -0.0250 -0.0309 0.0236  186 PRO   A C   
1455 O  O   . PRO   A 185 ? 0.1216 0.1411 0.3619 -0.0017 -0.0797 0.0502  186 PRO   A O   
1456 C  CB  . PRO   A 185 ? 0.1417 0.2222 0.2669 -0.0615 -0.0536 0.0212  186 PRO   A CB  
1457 C  CG  . PRO   A 185 ? 0.1373 0.1576 0.2614 0.0214  -0.0484 -0.0048 186 PRO   A CG  
1458 C  CD  . PRO   A 185 ? 0.1321 0.2046 0.2395 0.0012  -0.0476 0.0080  186 PRO   A CD  
1459 N  N   . GLU   A 186 ? 0.1766 0.2116 0.2645 -0.0769 -0.0292 0.0095  187 GLU   A N   
1460 C  CA  . GLU   A 186 ? 0.2323 0.1048 0.2825 0.0084  -0.0233 0.0411  187 GLU   A CA  
1461 C  C   . GLU   A 186 ? 0.1409 0.2197 0.2898 -0.0195 -0.0473 0.0129  187 GLU   A C   
1462 O  O   . GLU   A 186 ? 0.1439 0.2197 0.3472 -0.0097 -0.0440 -0.0022 187 GLU   A O   
1463 C  CB  . GLU   A 186 ? 0.1676 0.1830 0.4181 -0.0337 -0.0185 0.0939  187 GLU   A CB  
1464 C  CG  . GLU   A 186 ? 0.1932 0.2205 0.4436 -0.0422 -0.0042 0.0560  187 GLU   A CG  
1465 C  CD  . GLU   A 186 ? 0.1407 0.2275 0.4190 -0.0210 -0.0260 0.0921  187 GLU   A CD  
1466 O  OE1 . GLU   A 186 ? 0.3193 0.3021 0.5013 0.0230  0.0588  0.1995  187 GLU   A OE1 
1467 O  OE2 . GLU   A 186 ? 0.1941 0.2146 0.5845 -0.0387 -0.0052 -0.0089 187 GLU   A OE2 
1468 N  N   . SER   A 187 ? 0.0996 0.1835 0.2772 -0.0195 -0.0373 0.0283  188 SER   A N   
1469 C  CA  . SER   A 187 ? 0.1504 0.2021 0.2697 -0.0100 -0.0580 0.0380  188 SER   A CA  
1470 C  C   . SER   A 187 ? 0.1788 0.1758 0.2666 -0.0091 0.0100  0.0245  188 SER   A C   
1471 O  O   . SER   A 187 ? 0.1414 0.2290 0.2816 -0.0237 -0.0252 -0.0181 188 SER   A O   
1472 C  CB  . SER   A 187 ? 0.2116 0.2041 0.2436 -0.0094 -0.0343 0.0466  188 SER   A CB  
1473 O  OG  . SER   A 187 ? 0.1575 0.1914 0.3025 -0.0400 -0.0286 0.0145  188 SER   A OG  
1474 N  N   . LEU   A 188 ? 0.0824 0.1723 0.2990 -0.0197 -0.0526 -0.0175 189 LEU   A N   
1475 C  CA  . LEU   A 188 ? 0.1224 0.1350 0.2809 -0.0306 -0.0610 0.0195  189 LEU   A CA  
1476 C  C   . LEU   A 188 ? 0.1138 0.1557 0.2575 0.0100  -0.0380 -0.0196 189 LEU   A C   
1477 O  O   . LEU   A 188 ? 0.1529 0.1867 0.3126 -0.0375 -0.0562 -0.0233 189 LEU   A O   
1478 C  CB  . LEU   A 188 ? 0.1554 0.1283 0.3155 -0.0341 -0.0572 0.0125  189 LEU   A CB  
1479 C  CG  . LEU   A 188 ? 0.1453 0.2402 0.3358 0.0535  -0.0604 0.0168  189 LEU   A CG  
1480 C  CD1 . LEU   A 188 ? 0.2307 0.2116 0.3944 0.0085  -0.0511 0.0406  189 LEU   A CD1 
1481 C  CD2 . LEU   A 188 ? 0.1142 0.4201 0.3276 -0.0275 -0.0599 0.0193  189 LEU   A CD2 
1482 N  N   . ASP   A 189 ? 0.1890 0.2075 0.2251 -0.0026 -0.0165 -0.0020 190 ASP   A N   
1483 C  CA  . ASP   A 189 ? 0.1252 0.1939 0.2646 -0.0179 -0.0265 0.0091  190 ASP   A CA  
1484 C  C   . ASP   A 189 ? 0.1219 0.1901 0.2448 0.0071  -0.0434 0.0039  190 ASP   A C   
1485 O  O   . ASP   A 189 ? 0.1346 0.1683 0.2515 -0.0008 -0.0507 -0.0004 190 ASP   A O   
1486 C  CB  . ASP   A 189 ? 0.1421 0.2375 0.2691 -0.0579 -0.0416 0.0543  190 ASP   A CB  
1487 C  CG  . ASP   A 189 ? 0.1641 0.3753 0.3213 -0.0564 -0.0290 0.0186  190 ASP   A CG  
1488 O  OD1 . ASP   A 189 ? 0.1391 0.4833 0.3896 -0.0200 0.0281  -0.0258 190 ASP   A OD1 
1489 O  OD2 . ASP   A 189 ? 0.2406 0.4232 0.4077 -0.1323 -0.0556 0.0793  190 ASP   A OD2 
1490 N  N   . TYR   A 190 ? 0.1174 0.1899 0.2336 -0.0091 -0.0352 0.0244  191 TYR   A N   
1491 C  CA  . TYR   A 190 ? 0.1249 0.1368 0.2210 0.0030  -0.0054 0.0030  191 TYR   A CA  
1492 C  C   . TYR   A 190 ? 0.1569 0.1540 0.2060 -0.0185 0.0020  0.0149  191 TYR   A C   
1493 O  O   . TYR   A 190 ? 0.1423 0.1709 0.2365 -0.0108 0.0005  -0.0044 191 TYR   A O   
1494 C  CB  . TYR   A 190 ? 0.1362 0.1331 0.2468 -0.0190 -0.0554 -0.0108 191 TYR   A CB  
1495 C  CG  . TYR   A 190 ? 0.1213 0.1711 0.2491 0.0087  -0.0194 -0.0165 191 TYR   A CG  
1496 C  CD1 . TYR   A 190 ? 0.1878 0.1414 0.2740 -0.0502 -0.0184 -0.0292 191 TYR   A CD1 
1497 C  CD2 . TYR   A 190 ? 0.1079 0.1971 0.2985 0.0021  -0.0063 -0.0166 191 TYR   A CD2 
1498 C  CE1 . TYR   A 190 ? 0.1711 0.1375 0.3010 0.0153  -0.0100 0.0081  191 TYR   A CE1 
1499 C  CE2 . TYR   A 190 ? 0.0978 0.1518 0.3184 -0.0500 -0.0392 -0.0222 191 TYR   A CE2 
1500 C  CZ  . TYR   A 190 ? 0.1296 0.1673 0.3163 -0.0507 -0.0315 -0.0535 191 TYR   A CZ  
1501 O  OH  . TYR   A 190 ? 0.2020 0.1585 0.2899 -0.0159 -0.0683 -0.0302 191 TYR   A OH  
1502 N  N   . TRP   A 191 ? 0.1235 0.1319 0.2423 -0.0142 -0.0458 -0.0006 192 TRP   A N   
1503 C  CA  . TRP   A 191 ? 0.1059 0.1141 0.2447 0.0044  -0.0438 0.0073  192 TRP   A CA  
1504 C  C   . TRP   A 191 ? 0.1066 0.1472 0.2170 -0.0029 -0.0088 0.0008  192 TRP   A C   
1505 O  O   . TRP   A 191 ? 0.1463 0.1562 0.2442 -0.0192 -0.0091 -0.0040 192 TRP   A O   
1506 C  CB  . TRP   A 191 ? 0.1386 0.0958 0.2871 0.0038  -0.0129 0.0217  192 TRP   A CB  
1507 C  CG  . TRP   A 191 ? 0.1619 0.1106 0.2014 0.0004  -0.0278 0.0197  192 TRP   A CG  
1508 C  CD1 . TRP   A 191 ? 0.1434 0.0782 0.2357 -0.0151 -0.0073 0.0408  192 TRP   A CD1 
1509 C  CD2 . TRP   A 191 ? 0.0930 0.1443 0.2539 0.0337  -0.0525 -0.0047 192 TRP   A CD2 
1510 N  NE1 . TRP   A 191 ? 0.1817 0.0709 0.2674 -0.0070 -0.0001 0.0182  192 TRP   A NE1 
1511 C  CE2 . TRP   A 191 ? 0.1919 0.1493 0.2285 0.0076  -0.0403 -0.0050 192 TRP   A CE2 
1512 C  CE3 . TRP   A 191 ? 0.1115 0.1375 0.2535 -0.0059 -0.0619 -0.0269 192 TRP   A CE3 
1513 C  CZ2 . TRP   A 191 ? 0.1417 0.1317 0.2944 0.0217  -0.0386 0.0060  192 TRP   A CZ2 
1514 C  CZ3 . TRP   A 191 ? 0.0844 0.1386 0.2814 -0.0134 -0.0516 -0.0383 192 TRP   A CZ3 
1515 C  CH2 . TRP   A 191 ? 0.0501 0.1932 0.2988 0.0058  -0.0675 -0.0002 192 TRP   A CH2 
1516 N  N   . THR   A 192 ? 0.1068 0.1474 0.2043 0.0042  -0.0157 0.0054  193 THR   A N   
1517 C  CA  . THR   A 192 ? 0.0882 0.1389 0.2326 0.0223  -0.0417 0.0270  193 THR   A CA  
1518 C  C   . THR   A 192 ? 0.0885 0.1331 0.1984 0.0075  -0.0275 0.0145  193 THR   A C   
1519 O  O   . THR   A 192 ? 0.1177 0.1213 0.2291 -0.0019 -0.0372 0.0128  193 THR   A O   
1520 C  CB  . THR   A 192 ? 0.0616 0.1436 0.2043 0.0170  -0.0270 0.0231  193 THR   A CB  
1521 O  OG1 . THR   A 192 ? 0.1371 0.1280 0.2411 -0.0029 -0.0121 0.0023  193 THR   A OG1 
1522 C  CG2 . THR   A 192 ? 0.1274 0.1294 0.2186 -0.0290 0.0067  0.0375  193 THR   A CG2 
1523 N  N   . TYR   A 193 ? 0.0779 0.1533 0.2527 -0.0110 -0.0458 0.0103  194 TYR   A N   
1524 C  CA  . TYR   A 193 ? 0.0671 0.1436 0.2432 0.0076  -0.0463 0.0285  194 TYR   A CA  
1525 C  C   . TYR   A 193 ? 0.1533 0.0901 0.2031 0.0067  -0.0250 -0.0168 194 TYR   A C   
1526 O  O   . TYR   A 193 ? 0.0976 0.1210 0.2154 -0.0044 -0.0136 -0.0074 194 TYR   A O   
1527 C  CB  . TYR   A 193 ? 0.1247 0.1021 0.1817 0.0050  -0.0162 -0.0071 194 TYR   A CB  
1528 C  CG  . TYR   A 193 ? 0.1012 0.1047 0.1938 -0.0025 -0.0091 -0.0136 194 TYR   A CG  
1529 C  CD1 . TYR   A 193 ? 0.1544 0.0996 0.1858 0.0043  -0.0251 -0.0162 194 TYR   A CD1 
1530 C  CD2 . TYR   A 193 ? 0.0960 0.0979 0.2522 0.0087  -0.0107 0.0184  194 TYR   A CD2 
1531 C  CE1 . TYR   A 193 ? 0.0883 0.1229 0.2018 0.0048  -0.0118 0.0021  194 TYR   A CE1 
1532 C  CE2 . TYR   A 193 ? 0.1684 0.1003 0.1952 0.0163  -0.0485 -0.0001 194 TYR   A CE2 
1533 C  CZ  . TYR   A 193 ? 0.0847 0.0955 0.2021 0.0080  -0.0187 -0.0096 194 TYR   A CZ  
1534 O  OH  . TYR   A 193 ? 0.1235 0.0917 0.2222 0.0110  -0.0212 0.0157  194 TYR   A OH  
1535 N  N   . PRO   A 194 ? 0.0958 0.1294 0.1978 0.0100  -0.0312 0.0011  195 PRO   A N   
1536 C  CA  . PRO   A 194 ? 0.1453 0.1410 0.2014 0.0032  0.0044  0.0033  195 PRO   A CA  
1537 C  C   . PRO   A 194 ? 0.1151 0.1353 0.2116 -0.0092 -0.0264 0.0096  195 PRO   A C   
1538 O  O   . PRO   A 194 ? 0.1109 0.1435 0.2568 0.0280  -0.0315 0.0219  195 PRO   A O   
1539 C  CB  . PRO   A 194 ? 0.1894 0.1761 0.2278 0.0130  -0.0201 -0.0186 195 PRO   A CB  
1540 C  CG  . PRO   A 194 ? 0.1500 0.1388 0.2355 -0.0584 -0.0358 -0.0182 195 PRO   A CG  
1541 C  CD  . PRO   A 194 ? 0.1389 0.1665 0.1835 -0.0682 -0.0211 -0.0113 195 PRO   A CD  
1542 N  N   . GLY   A 195 ? 0.0876 0.1341 0.1988 -0.0269 -0.0118 -0.0337 196 GLY   A N   
1543 C  CA  . GLY   A 195 ? 0.1265 0.1700 0.2030 0.0250  -0.0016 0.0082  196 GLY   A CA  
1544 C  C   . GLY   A 195 ? 0.0975 0.1043 0.2034 -0.0183 -0.0389 -0.0153 196 GLY   A C   
1545 O  O   . GLY   A 195 ? 0.1127 0.0820 0.2541 0.0236  -0.0259 -0.0083 196 GLY   A O   
1546 N  N   . SER   A 196 ? 0.1194 0.1317 0.2070 0.0012  -0.0462 -0.0173 197 SER   A N   
1547 C  CA  . SER   A 196 ? 0.0900 0.1779 0.1877 0.0359  -0.0460 -0.0012 197 SER   A CA  
1548 C  C   . SER   A 196 ? 0.0752 0.1251 0.1955 -0.0124 -0.0554 0.0116  197 SER   A C   
1549 O  O   . SER   A 196 ? 0.0904 0.1132 0.2307 -0.0229 -0.0571 -0.0154 197 SER   A O   
1550 C  CB  . SER   A 196 ? 0.0864 0.1353 0.2774 0.0311  -0.0644 -0.0187 197 SER   A CB  
1551 O  OG  . SER   A 196 ? 0.0888 0.1174 0.2627 -0.0243 -0.0458 -0.0106 197 SER   A OG  
1552 N  N   . LEU   A 197 ? 0.1005 0.1360 0.1966 0.0288  -0.0232 0.0201  198 LEU   A N   
1553 C  CA  . LEU   A 197 ? 0.1050 0.1172 0.1975 -0.0130 -0.0082 0.0055  198 LEU   A CA  
1554 C  C   . LEU   A 197 ? 0.1678 0.1140 0.2188 0.0034  -0.0372 -0.0040 198 LEU   A C   
1555 O  O   . LEU   A 197 ? 0.1647 0.0937 0.2469 -0.0355 -0.0436 0.0106  198 LEU   A O   
1556 C  CB  . LEU   A 197 ? 0.1561 0.1129 0.2470 0.0218  0.0105  0.0422  198 LEU   A CB  
1557 C  CG  . LEU   A 197 ? 0.1249 0.0933 0.2474 -0.0023 -0.0239 -0.0035 198 LEU   A CG  
1558 C  CD1 . LEU   A 197 ? 0.1892 0.1461 0.3129 -0.0750 -0.0449 0.0403  198 LEU   A CD1 
1559 C  CD2 . LEU   A 197 ? 0.1144 0.1299 0.3401 0.0534  -0.0505 0.0122  198 LEU   A CD2 
1560 N  N   . THR   A 198 ? 0.0698 0.1045 0.2294 0.0062  -0.0165 -0.0051 199 THR   A N   
1561 C  CA  . THR   A 198 ? 0.1129 0.0785 0.2401 0.0001  -0.0193 -0.0016 199 THR   A CA  
1562 C  C   . THR   A 198 ? 0.0991 0.1226 0.2463 -0.0049 -0.0328 -0.0117 199 THR   A C   
1563 O  O   . THR   A 198 ? 0.0985 0.1404 0.2578 0.0156  -0.0376 -0.0152 199 THR   A O   
1564 C  CB  . THR   A 198 ? 0.1669 0.0547 0.2066 -0.0095 -0.0125 -0.0026 199 THR   A CB  
1565 O  OG1 . THR   A 198 ? 0.1307 0.1210 0.2251 -0.0008 -0.0127 0.0042  199 THR   A OG1 
1566 C  CG2 . THR   A 198 ? 0.1116 0.1086 0.2577 -0.0061 -0.0027 0.0345  199 THR   A CG2 
1567 N  N   . THR   A 199 ? 0.1102 0.1542 0.2154 -0.0072 0.0002  -0.0013 200 THR   A N   
1568 C  CA  . THR   A 199 ? 0.1939 0.1489 0.1971 -0.0669 0.0281  -0.0210 200 THR   A CA  
1569 C  C   . THR   A 199 ? 0.1084 0.1389 0.2325 -0.0229 -0.0222 0.0049  200 THR   A C   
1570 O  O   . THR   A 199 ? 0.0982 0.1644 0.2606 -0.0177 0.0018  -0.0053 200 THR   A O   
1571 C  CB  . THR   A 199 ? 0.2050 0.0630 0.2603 -0.0010 -0.0418 -0.0105 200 THR   A CB  
1572 O  OG1 . THR   A 199 ? 0.2463 0.1252 0.2738 0.0529  -0.0761 -0.0176 200 THR   A OG1 
1573 C  CG2 . THR   A 199 ? 0.1574 0.1626 0.2823 -0.0316 -0.0671 -0.0432 200 THR   A CG2 
1574 N  N   . PRO   A 200 ? 0.1152 0.1405 0.2715 -0.0613 -0.0068 -0.0140 201 PRO   A N   
1575 C  CA  . PRO   A 200 ? 0.1233 0.1204 0.2452 -0.0545 -0.0071 0.0230  201 PRO   A CA  
1576 C  C   . PRO   A 200 ? 0.1840 0.1423 0.2118 -0.0126 -0.0016 -0.0047 201 PRO   A C   
1577 O  O   . PRO   A 200 ? 0.1734 0.1901 0.2269 -0.0324 -0.0120 0.0166  201 PRO   A O   
1578 C  CB  . PRO   A 200 ? 0.1287 0.1514 0.3129 -0.0343 0.0075  0.0037  201 PRO   A CB  
1579 C  CG  . PRO   A 200 ? 0.0842 0.1486 0.3476 -0.0168 -0.0140 -0.0314 201 PRO   A CG  
1580 C  CD  . PRO   A 200 ? 0.0757 0.2120 0.2850 -0.0145 -0.0356 -0.0031 201 PRO   A CD  
1581 N  N   . PRO   A 201 ? 0.1543 0.1334 0.2237 -0.0115 -0.0107 0.0041  202 PRO   A N   
1582 C  CA  . PRO   A 201 ? 0.1867 0.1158 0.2308 -0.0398 -0.0158 0.0081  202 PRO   A CA  
1583 C  C   . PRO   A 201 ? 0.1485 0.0836 0.2319 0.0025  -0.0034 0.0081  202 PRO   A C   
1584 O  O   . PRO   A 201 ? 0.1592 0.1435 0.2716 0.0011  -0.0215 -0.0128 202 PRO   A O   
1585 C  CB  . PRO   A 201 ? 0.1425 0.1151 0.2799 -0.0325 -0.0218 0.0148  202 PRO   A CB  
1586 C  CG  . PRO   A 201 ? 0.1576 0.1210 0.3331 -0.0384 -0.0502 -0.0083 202 PRO   A CG  
1587 C  CD  . PRO   A 201 ? 0.1698 0.1536 0.2774 0.0249  -0.0259 -0.0242 202 PRO   A CD  
1588 N  N   . LEU   A 202 ? 0.1068 0.1126 0.2350 0.0027  0.0024  0.0083  203 LEU   A N   
1589 C  CA  . LEU   A 202 ? 0.0912 0.1095 0.2318 0.0418  -0.0223 0.0019  203 LEU   A CA  
1590 C  C   . LEU   A 202 ? 0.0818 0.1368 0.2336 -0.0482 -0.0196 -0.0110 203 LEU   A C   
1591 O  O   . LEU   A 202 ? 0.0985 0.1321 0.2384 0.0027  -0.0370 -0.0036 203 LEU   A O   
1592 C  CB  . LEU   A 202 ? 0.0838 0.0906 0.2974 0.0377  -0.0585 -0.0425 203 LEU   A CB  
1593 C  CG  . LEU   A 202 ? 0.0628 0.0804 0.3085 -0.0184 -0.0294 -0.0502 203 LEU   A CG  
1594 C  CD1 . LEU   A 202 ? 0.0915 0.1539 0.3205 0.0221  -0.0406 -0.0284 203 LEU   A CD1 
1595 C  CD2 . LEU   A 202 ? 0.0703 0.0870 0.3244 -0.0259 -0.0109 -0.0578 203 LEU   A CD2 
1596 N  N   . LEU   A 203 ? 0.0831 0.1629 0.2877 -0.0003 -0.0170 0.0115  204 LEU   A N   
1597 C  CA  . LEU   A 203 ? 0.1066 0.1242 0.2557 0.0039  -0.0196 0.0359  204 LEU   A CA  
1598 C  C   . LEU   A 203 ? 0.1037 0.0983 0.2311 0.0047  -0.0179 -0.0120 204 LEU   A C   
1599 O  O   . LEU   A 203 ? 0.1119 0.1335 0.2519 -0.0143 -0.0457 -0.0339 204 LEU   A O   
1600 C  CB  . LEU   A 203 ? 0.1756 0.1174 0.2577 0.0016  -0.0058 0.0603  204 LEU   A CB  
1601 C  CG  . LEU   A 203 ? 0.1533 0.1508 0.2782 -0.0237 -0.0225 0.0571  204 LEU   A CG  
1602 C  CD1 . LEU   A 203 ? 0.1623 0.1542 0.3774 0.0333  -0.0588 0.0454  204 LEU   A CD1 
1603 C  CD2 . LEU   A 203 ? 0.1535 0.1826 0.3933 -0.0330 -0.0247 0.0030  204 LEU   A CD2 
1604 N  N   . GLU   A 204 ? 0.1170 0.1603 0.2371 -0.0008 -0.0318 -0.0185 205 GLU   A N   
1605 C  CA  . GLU   A 204 ? 0.1847 0.1068 0.2066 0.0131  -0.0280 -0.0479 205 GLU   A CA  
1606 C  C   . GLU   A 204 ? 0.1041 0.1288 0.2452 -0.0100 -0.0387 -0.0212 205 GLU   A C   
1607 O  O   . GLU   A 204 ? 0.1618 0.2000 0.2560 0.0326  -0.0312 -0.0305 205 GLU   A O   
1608 C  CB  . GLU   A 204 ? 0.1220 0.1240 0.2594 0.0073  -0.0482 -0.0157 205 GLU   A CB  
1609 C  CG  . GLU   A 204 ? 0.1102 0.1454 0.2518 0.0201  -0.0174 -0.0022 205 GLU   A CG  
1610 C  CD  . GLU   A 204 ? 0.1648 0.1488 0.2305 0.0098  -0.0424 -0.0089 205 GLU   A CD  
1611 O  OE1 . GLU   A 204 ? 0.1657 0.2053 0.3114 -0.0190 -0.0678 -0.0460 205 GLU   A OE1 
1612 O  OE2 . GLU   A 204 ? 0.0862 0.1423 0.2697 -0.0277 -0.0612 -0.0129 205 GLU   A OE2 
1613 N  N   . CYS   A 205 ? 0.1736 0.1000 0.2434 -0.0087 -0.0508 -0.0032 206 CYS   A N   
1614 C  CA  . CYS   A 205 ? 0.1316 0.1711 0.2268 -0.0004 -0.0288 -0.0134 206 CYS   A CA  
1615 C  C   . CYS   A 205 ? 0.1298 0.1108 0.2247 0.0005  -0.0379 0.0201  206 CYS   A C   
1616 O  O   . CYS   A 205 ? 0.1127 0.1143 0.2949 -0.0037 -0.0724 0.0026  206 CYS   A O   
1617 C  CB  . CYS   A 205 ? 0.1531 0.1842 0.2485 -0.0433 -0.0124 -0.0023 206 CYS   A CB  
1618 S  SG  . CYS   A 205 ? 0.1479 0.1162 0.2622 0.0048  -0.0304 0.0066  206 CYS   A SG  
1619 N  N   . VAL   A 206 ? 0.1244 0.1071 0.2391 -0.0234 -0.0385 0.0083  207 VAL   A N   
1620 C  CA  . VAL   A 206 ? 0.0739 0.1355 0.2341 0.0124  -0.0241 -0.0133 207 VAL   A CA  
1621 C  C   . VAL   A 206 ? 0.0878 0.1364 0.2511 0.0188  -0.0096 -0.0205 207 VAL   A C   
1622 O  O   . VAL   A 206 ? 0.1377 0.1558 0.2474 -0.0168 -0.0124 -0.0025 207 VAL   A O   
1623 C  CB  . VAL   A 206 ? 0.0770 0.1331 0.2145 -0.0195 -0.0194 -0.0113 207 VAL   A CB  
1624 C  CG1 . VAL   A 206 ? 0.1048 0.1028 0.2492 -0.0286 -0.0640 -0.0096 207 VAL   A CG1 
1625 C  CG2 . VAL   A 206 ? 0.1068 0.1395 0.2057 0.0491  -0.0005 -0.0026 207 VAL   A CG2 
1626 N  N   . THR   A 207 ? 0.0806 0.1172 0.2141 0.0234  0.0018  -0.0113 208 THR   A N   
1627 C  CA  . THR   A 207 ? 0.0791 0.1224 0.2376 0.0084  -0.0135 -0.0193 208 THR   A CA  
1628 C  C   . THR   A 207 ? 0.1352 0.0846 0.2387 -0.0040 -0.0445 0.0155  208 THR   A C   
1629 O  O   . THR   A 207 ? 0.1763 0.0806 0.2152 -0.0220 -0.0491 -0.0031 208 THR   A O   
1630 C  CB  . THR   A 207 ? 0.0924 0.0969 0.3037 0.0082  -0.0066 -0.0361 208 THR   A CB  
1631 O  OG1 . THR   A 207 ? 0.1547 0.0862 0.2700 0.0070  0.0024  -0.0370 208 THR   A OG1 
1632 C  CG2 . THR   A 207 ? 0.0842 0.1581 0.2742 -0.0042 -0.0275 0.0048  208 THR   A CG2 
1633 N  N   . TRP   A 208 ? 0.0757 0.0807 0.2520 0.0000  -0.0245 0.0057  209 TRP   A N   
1634 C  CA  . TRP   A 208 ? 0.0776 0.0885 0.2666 -0.0013 -0.0223 -0.0064 209 TRP   A CA  
1635 C  C   . TRP   A 208 ? 0.0802 0.1188 0.2036 0.0373  -0.0129 0.0039  209 TRP   A C   
1636 O  O   . TRP   A 208 ? 0.0781 0.1093 0.2242 -0.0173 -0.0209 0.0127  209 TRP   A O   
1637 C  CB  . TRP   A 208 ? 0.1151 0.1307 0.2463 0.0296  -0.0161 0.0175  209 TRP   A CB  
1638 C  CG  . TRP   A 208 ? 0.1101 0.0779 0.2089 -0.0062 -0.0216 -0.0148 209 TRP   A CG  
1639 C  CD1 . TRP   A 208 ? 0.1332 0.0604 0.2560 -0.0152 -0.0342 0.0033  209 TRP   A CD1 
1640 C  CD2 . TRP   A 208 ? 0.1220 0.0813 0.2099 0.0054  -0.0174 -0.0129 209 TRP   A CD2 
1641 N  NE1 . TRP   A 208 ? 0.1690 0.1043 0.2293 0.0226  -0.0432 0.0053  209 TRP   A NE1 
1642 C  CE2 . TRP   A 208 ? 0.1190 0.1267 0.2339 0.0190  -0.0355 0.0278  209 TRP   A CE2 
1643 C  CE3 . TRP   A 208 ? 0.1418 0.0651 0.2222 0.0097  -0.0447 0.0092  209 TRP   A CE3 
1644 C  CZ2 . TRP   A 208 ? 0.1163 0.1259 0.2438 0.0341  -0.0653 -0.0001 209 TRP   A CZ2 
1645 C  CZ3 . TRP   A 208 ? 0.1456 0.0819 0.2315 0.0343  -0.0073 0.0306  209 TRP   A CZ3 
1646 C  CH2 . TRP   A 208 ? 0.0998 0.0949 0.2389 0.0438  -0.0324 -0.0137 209 TRP   A CH2 
1647 N  N   . ILE   A 209 ? 0.1277 0.0985 0.2208 -0.0064 -0.0316 0.0044  210 ILE   A N   
1648 C  CA  . ILE   A 209 ? 0.0937 0.1152 0.2233 -0.0100 -0.0601 -0.0164 210 ILE   A CA  
1649 C  C   . ILE   A 209 ? 0.0822 0.1113 0.1982 -0.0148 -0.0164 -0.0048 210 ILE   A C   
1650 O  O   . ILE   A 209 ? 0.1267 0.1188 0.1926 -0.0140 -0.0377 -0.0157 210 ILE   A O   
1651 C  CB  . ILE   A 209 ? 0.0511 0.1174 0.3154 -0.0183 -0.0350 -0.0050 210 ILE   A CB  
1652 C  CG1 . ILE   A 209 ? 0.1238 0.1113 0.2756 0.0179  -0.0469 0.0057  210 ILE   A CG1 
1653 C  CG2 . ILE   A 209 ? 0.0391 0.1690 0.2791 -0.0122 -0.0456 0.0127  210 ILE   A CG2 
1654 C  CD1 . ILE   A 209 ? 0.1185 0.1447 0.2745 0.0303  -0.0339 0.0299  210 ILE   A CD1 
1655 N  N   . VAL   A 210 ? 0.1159 0.1248 0.2847 0.0012  -0.0396 0.0176  211 VAL   A N   
1656 C  CA  . VAL   A 210 ? 0.0745 0.1694 0.2649 0.0083  -0.0490 -0.0237 211 VAL   A CA  
1657 C  C   . VAL   A 210 ? 0.1278 0.0942 0.2029 0.0184  -0.0040 -0.0184 211 VAL   A C   
1658 O  O   . VAL   A 210 ? 0.1075 0.1208 0.2247 -0.0351 -0.0121 -0.0011 211 VAL   A O   
1659 C  CB  . VAL   A 210 ? 0.0953 0.0707 0.2495 -0.0031 -0.0312 -0.0086 211 VAL   A CB  
1660 C  CG1 . VAL   A 210 ? 0.0925 0.0865 0.2287 0.0044  -0.0612 -0.0150 211 VAL   A CG1 
1661 C  CG2 . VAL   A 210 ? 0.0926 0.0912 0.2689 -0.0018 -0.0297 0.0013  211 VAL   A CG2 
1662 N  N   . LEU   A 211 ? 0.1131 0.1569 0.2287 -0.0317 -0.0185 -0.0141 212 LEU   A N   
1663 C  CA  . LEU   A 211 ? 0.1120 0.1328 0.2373 -0.0299 -0.0402 0.0092  212 LEU   A CA  
1664 C  C   . LEU   A 211 ? 0.1421 0.1528 0.2018 -0.0110 -0.0143 0.0418  212 LEU   A C   
1665 O  O   . LEU   A 211 ? 0.0939 0.1676 0.2554 -0.0500 -0.0296 -0.0018 212 LEU   A O   
1666 C  CB  . LEU   A 211 ? 0.1418 0.1134 0.2143 0.0020  -0.0406 0.0344  212 LEU   A CB  
1667 C  CG  . LEU   A 211 ? 0.1772 0.1073 0.2522 -0.0092 -0.0604 0.0398  212 LEU   A CG  
1668 C  CD1 . LEU   A 211 ? 0.1413 0.1931 0.2763 -0.0200 -0.0551 0.0294  212 LEU   A CD1 
1669 C  CD2 . LEU   A 211 ? 0.1621 0.2010 0.2743 0.0111  -0.0472 0.0249  212 LEU   A CD2 
1670 N  N   . LYS   A 212 ? 0.0961 0.1400 0.2156 -0.0126 -0.0337 0.0418  213 LYS   A N   
1671 C  CA  . LYS   A 212 ? 0.1400 0.1083 0.2559 -0.0096 -0.0386 0.0183  213 LYS   A CA  
1672 C  C   . LYS   A 212 ? 0.1576 0.1132 0.2678 -0.0144 -0.0439 0.0160  213 LYS   A C   
1673 O  O   . LYS   A 212 ? 0.1544 0.1120 0.3082 -0.0061 -0.0401 0.0177  213 LYS   A O   
1674 C  CB  . LYS   A 212 ? 0.2292 0.1109 0.2654 -0.0418 -0.0256 0.0249  213 LYS   A CB  
1675 C  CG  . LYS   A 212 ? 0.2737 0.1082 0.2677 0.0072  -0.0027 0.0318  213 LYS   A CG  
1676 C  CD  . LYS   A 212 ? 0.4162 0.2973 0.3090 -0.0741 0.0616  0.0429  213 LYS   A CD  
1677 C  CE  . LYS   A 212 ? 0.4294 0.3286 0.4115 -0.1277 0.0009  0.1216  213 LYS   A CE  
1678 N  NZ  . LYS   A 212 ? 0.8348 0.5466 0.5013 -0.1408 0.1419  0.1955  213 LYS   A NZ  
1679 N  N   . GLU   A 213 ? 0.1238 0.1138 0.2497 -0.0279 -0.0324 0.0052  214 GLU   A N   
1680 C  CA  . GLU   A 213 ? 0.1355 0.1373 0.2327 -0.0086 -0.0439 0.0043  214 GLU   A CA  
1681 C  C   . GLU   A 213 ? 0.1569 0.1489 0.2114 -0.0017 -0.0432 0.0121  214 GLU   A C   
1682 O  O   . GLU   A 213 ? 0.1086 0.1502 0.2546 -0.0189 -0.0357 0.0427  214 GLU   A O   
1683 C  CB  . GLU   A 213 ? 0.1350 0.1826 0.2501 -0.0067 -0.0475 -0.0107 214 GLU   A CB  
1684 C  CG  . GLU   A 213 ? 0.1740 0.1366 0.3156 -0.0505 -0.0297 -0.0127 214 GLU   A CG  
1685 C  CD  . GLU   A 213 ? 0.1830 0.3015 0.4195 -0.0427 0.0040  -0.1037 214 GLU   A CD  
1686 O  OE1 . GLU   A 213 ? 0.1635 0.1486 0.3678 -0.0173 -0.0524 0.0003  214 GLU   A OE1 
1687 O  OE2 . GLU   A 213 ? 0.2546 0.4755 0.5496 -0.1391 -0.0234 -0.1846 214 GLU   A OE2 
1688 N  N   . PRO   A 214 ? 0.1283 0.1000 0.2520 -0.0296 -0.0337 0.0177  215 PRO   A N   
1689 C  CA  . PRO   A 214 ? 0.1795 0.0901 0.2355 0.0239  -0.0223 -0.0099 215 PRO   A CA  
1690 C  C   . PRO   A 214 ? 0.1955 0.1134 0.2533 -0.0190 -0.0118 -0.0088 215 PRO   A C   
1691 O  O   . PRO   A 214 ? 0.1867 0.1687 0.3112 -0.0508 -0.0067 0.0267  215 PRO   A O   
1692 C  CB  . PRO   A 214 ? 0.1156 0.1346 0.2480 0.0452  -0.0223 0.0052  215 PRO   A CB  
1693 C  CG  . PRO   A 214 ? 0.2857 0.2099 0.3402 0.0871  0.0848  0.0497  215 PRO   A CG  
1694 C  CD  . PRO   A 214 ? 0.2103 0.0766 0.2721 -0.0077 0.0017  0.0009  215 PRO   A CD  
1695 N  N   . ILE   A 215 ? 0.1921 0.1375 0.2208 0.0225  -0.0159 -0.0122 216 ILE   A N   
1696 C  CA  . ILE   A 215 ? 0.2011 0.1445 0.2409 -0.0060 -0.0414 -0.0301 216 ILE   A CA  
1697 C  C   . ILE   A 215 ? 0.1292 0.1222 0.2512 -0.0074 -0.0306 -0.0043 216 ILE   A C   
1698 O  O   . ILE   A 215 ? 0.1353 0.1357 0.2706 -0.0027 0.0009  0.0053  216 ILE   A O   
1699 C  CB  . ILE   A 215 ? 0.0955 0.1495 0.2775 0.0143  -0.0239 -0.0122 216 ILE   A CB  
1700 C  CG1 . ILE   A 215 ? 0.1161 0.1283 0.2498 -0.0036 -0.0080 -0.0148 216 ILE   A CG1 
1701 C  CG2 . ILE   A 215 ? 0.1224 0.1679 0.3060 0.0710  -0.0620 -0.0083 216 ILE   A CG2 
1702 C  CD1 . ILE   A 215 ? 0.1949 0.1445 0.2616 0.0027  -0.0345 0.0052  216 ILE   A CD1 
1703 N  N   . SER   A 216 ? 0.1802 0.1210 0.2771 -0.0440 -0.0395 -0.0034 217 SER   A N   
1704 C  CA  . SER   A 216 ? 0.2011 0.1483 0.2794 -0.0375 -0.0337 -0.0261 217 SER   A CA  
1705 C  C   . SER   A 216 ? 0.1757 0.1161 0.2771 -0.0078 -0.0255 0.0039  217 SER   A C   
1706 O  O   . SER   A 216 ? 0.1485 0.1705 0.2912 -0.0124 -0.0583 -0.0039 217 SER   A O   
1707 C  CB  . SER   A 216 ? 0.2463 0.1212 0.2617 -0.0436 -0.0016 0.0286  217 SER   A CB  
1708 O  OG  . SER   A 216 ? 0.2113 0.2546 0.2697 -0.0384 -0.0150 0.0176  217 SER   A OG  
1709 N  N   . VAL   A 217 ? 0.1535 0.1198 0.2703 -0.0408 -0.0156 -0.0215 218 VAL   A N   
1710 C  CA  . VAL   A 217 ? 0.1467 0.1134 0.2837 -0.0086 -0.0259 0.0048  218 VAL   A CA  
1711 C  C   . VAL   A 217 ? 0.2429 0.1353 0.2368 -0.0047 -0.0394 -0.0174 218 VAL   A C   
1712 O  O   . VAL   A 217 ? 0.1571 0.1640 0.2661 -0.0542 -0.0538 0.0109  218 VAL   A O   
1713 C  CB  . VAL   A 217 ? 0.1224 0.0890 0.2822 0.0005  -0.0462 -0.0009 218 VAL   A CB  
1714 C  CG1 . VAL   A 217 ? 0.1780 0.1012 0.3057 -0.0436 -0.0199 -0.0309 218 VAL   A CG1 
1715 C  CG2 . VAL   A 217 ? 0.1234 0.1468 0.3504 -0.0184 -0.0886 -0.0096 218 VAL   A CG2 
1716 N  N   . SER   A 218 ? 0.2039 0.0948 0.2588 -0.0111 -0.0534 -0.0276 219 SER   A N   
1717 C  CA  . SER   A 218 ? 0.1571 0.1155 0.2735 0.0099  -0.0264 -0.0447 219 SER   A CA  
1718 C  C   . SER   A 218 ? 0.1396 0.1179 0.2864 -0.0075 -0.0361 -0.0021 219 SER   A C   
1719 O  O   . SER   A 218 ? 0.2057 0.1030 0.2782 -0.0432 -0.0529 -0.0098 219 SER   A O   
1720 C  CB  . SER   A 218 ? 0.2254 0.2164 0.2080 0.0132  -0.0033 -0.0215 219 SER   A CB  
1721 O  OG  . SER   A 218 ? 0.1928 0.1683 0.2672 0.0017  -0.0421 0.0086  219 SER   A OG  
1722 N  N   A SER   A 219 ? 0.1980 0.1321 0.2960 0.0080  -0.0374 -0.0270 220 SER   A N   
1723 N  N   B SER   A 219 ? 0.1945 0.1319 0.2800 0.0058  -0.0375 -0.0266 220 SER   A N   
1724 C  CA  A SER   A 219 ? 0.2135 0.0822 0.3617 -0.0018 -0.0117 -0.0072 220 SER   A CA  
1725 C  CA  B SER   A 219 ? 0.2089 0.0761 0.3373 -0.0019 -0.0176 -0.0044 220 SER   A CA  
1726 C  C   A SER   A 219 ? 0.2007 0.1813 0.3170 -0.0019 -0.0115 -0.0348 220 SER   A C   
1727 C  C   B SER   A 219 ? 0.1985 0.1759 0.3053 -0.0107 -0.0083 -0.0333 220 SER   A C   
1728 O  O   A SER   A 219 ? 0.1745 0.1604 0.3445 0.0130  -0.0165 -0.0197 220 SER   A O   
1729 O  O   B SER   A 219 ? 0.1659 0.1630 0.3360 0.0093  -0.0147 -0.0234 220 SER   A O   
1730 C  CB  A SER   A 219 ? 0.2538 0.0807 0.3877 0.0083  -0.0131 -0.0079 220 SER   A CB  
1731 C  CB  B SER   A 219 ? 0.2411 0.0710 0.2925 -0.0073 -0.0263 -0.0234 220 SER   A CB  
1732 O  OG  A SER   A 219 ? 0.2156 0.1152 0.4140 0.0015  0.0134  -0.0411 220 SER   A OG  
1733 O  OG  B SER   A 219 ? 0.2305 0.1292 0.2624 -0.0175 -0.0190 -0.0172 220 SER   A OG  
1734 N  N   . GLU   A 220 ? 0.2068 0.1242 0.3141 0.0276  -0.0099 -0.0291 221 GLU   A N   
1735 C  CA  . GLU   A 220 ? 0.2470 0.1230 0.3032 0.0058  -0.0309 -0.0363 221 GLU   A CA  
1736 C  C   . GLU   A 220 ? 0.2964 0.1174 0.2797 0.0004  0.0161  -0.0282 221 GLU   A C   
1737 O  O   . GLU   A 220 ? 0.2346 0.1813 0.2558 0.0226  -0.0116 -0.0122 221 GLU   A O   
1738 C  CB  . GLU   A 220 ? 0.3155 0.1605 0.3226 -0.0119 -0.0576 -0.0647 221 GLU   A CB  
1739 C  CG  . GLU   A 220 ? 0.4469 0.1449 0.3389 0.0055  -0.0754 -0.0678 221 GLU   A CG  
1740 C  CD  . GLU   A 220 ? 0.3554 0.2438 0.4240 -0.0819 -0.0631 -0.1571 221 GLU   A CD  
1741 O  OE1 . GLU   A 220 ? 0.3540 0.1895 0.5011 -0.0873 0.0179  -0.1301 221 GLU   A OE1 
1742 O  OE2 . GLU   A 220 ? 0.5836 0.2192 0.4933 -0.0856 -0.0109 -0.1213 221 GLU   A OE2 
1743 N  N   . GLN   A 221 ? 0.1870 0.1212 0.2502 -0.0226 -0.0140 -0.0089 222 GLN   A N   
1744 C  CA  . GLN   A 221 ? 0.1403 0.1152 0.3098 -0.0179 -0.0384 -0.0147 222 GLN   A CA  
1745 C  C   . GLN   A 221 ? 0.1330 0.1912 0.2312 0.0118  -0.0253 0.0190  222 GLN   A C   
1746 O  O   . GLN   A 221 ? 0.1838 0.1745 0.2816 -0.0041 -0.0186 0.0232  222 GLN   A O   
1747 C  CB  . GLN   A 221 ? 0.1725 0.1522 0.2823 -0.0284 -0.0256 -0.0171 222 GLN   A CB  
1748 C  CG  . GLN   A 221 ? 0.1878 0.2238 0.2576 -0.0279 -0.0413 -0.0192 222 GLN   A CG  
1749 C  CD  . GLN   A 221 ? 0.2036 0.1238 0.2242 -0.0301 -0.0439 -0.0054 222 GLN   A CD  
1750 O  OE1 . GLN   A 221 ? 0.1819 0.1654 0.2244 0.0055  -0.0216 -0.0032 222 GLN   A OE1 
1751 N  NE2 . GLN   A 221 ? 0.1916 0.1089 0.2997 -0.0174 -0.0479 0.0110  222 GLN   A NE2 
1752 N  N   . VAL   A 222 ? 0.1840 0.1080 0.2578 -0.0332 -0.0449 0.0243  223 VAL   A N   
1753 C  CA  . VAL   A 222 ? 0.1564 0.1768 0.2705 0.0042  -0.0305 -0.0036 223 VAL   A CA  
1754 C  C   . VAL   A 222 ? 0.2197 0.1906 0.2793 -0.0342 0.0186  0.0013  223 VAL   A C   
1755 O  O   . VAL   A 222 ? 0.1919 0.1370 0.2936 -0.0054 -0.0195 -0.0092 223 VAL   A O   
1756 C  CB  . VAL   A 222 ? 0.2347 0.1507 0.3028 0.0024  -0.0867 -0.0289 223 VAL   A CB  
1757 C  CG1 . VAL   A 222 ? 0.1874 0.1483 0.3529 -0.0003 -0.0290 -0.0068 223 VAL   A CG1 
1758 C  CG2 . VAL   A 222 ? 0.2328 0.2107 0.3034 -0.0473 -0.0682 -0.0097 223 VAL   A CG2 
1759 N  N   . LEU   A 223 ? 0.2892 0.1787 0.2567 0.0525  -0.0374 -0.0143 224 LEU   A N   
1760 C  CA  . LEU   A 223 ? 0.2267 0.1185 0.2815 -0.0153 -0.0314 -0.0201 224 LEU   A CA  
1761 C  C   . LEU   A 223 ? 0.1847 0.1858 0.2583 -0.0147 0.0016  -0.0215 224 LEU   A C   
1762 O  O   . LEU   A 223 ? 0.1572 0.1773 0.3088 0.0158  -0.0083 -0.0121 224 LEU   A O   
1763 C  CB  . LEU   A 223 ? 0.3398 0.1252 0.3569 -0.0285 -0.0300 -0.0485 224 LEU   A CB  
1764 C  CG  . LEU   A 223 ? 0.2038 0.2164 0.4505 -0.0075 0.0189  0.0280  224 LEU   A CG  
1765 C  CD1 . LEU   A 223 ? 0.3827 0.2694 0.4899 -0.0788 0.0334  -0.0281 224 LEU   A CD1 
1766 C  CD2 . LEU   A 223 ? 0.1932 0.2427 0.5500 -0.0139 0.0240  -0.0153 224 LEU   A CD2 
1767 N  N   . LYS   A 224 ? 0.2190 0.1636 0.2521 -0.0059 -0.0331 0.0002  225 LYS   A N   
1768 C  CA  . LYS   A 224 ? 0.1856 0.2043 0.2901 -0.0179 -0.0579 0.0251  225 LYS   A CA  
1769 C  C   . LYS   A 224 ? 0.1572 0.2018 0.2330 0.0297  -0.0302 0.0058  225 LYS   A C   
1770 O  O   . LYS   A 224 ? 0.1823 0.1923 0.2730 -0.0111 -0.0253 -0.0018 225 LYS   A O   
1771 C  CB  . LYS   A 224 ? 0.1763 0.1751 0.2895 -0.0388 -0.0635 0.0053  225 LYS   A CB  
1772 C  CG  . LYS   A 224 ? 0.1793 0.2355 0.3212 0.0008  -0.0769 -0.0632 225 LYS   A CG  
1773 C  CD  . LYS   A 224 ? 0.1306 0.2763 0.4699 -0.0412 -0.0539 0.0146  225 LYS   A CD  
1774 C  CE  . LYS   A 224 ? 0.2848 0.4272 0.4465 -0.1395 -0.1353 0.0132  225 LYS   A CE  
1775 N  NZ  . LYS   A 224 ? 0.2529 0.3326 0.4583 0.0399  0.0113  0.0078  225 LYS   A NZ  
1776 N  N   . PHE   A 225 ? 0.1658 0.1432 0.2312 0.0223  -0.0522 -0.0158 226 PHE   A N   
1777 C  CA  . PHE   A 225 ? 0.1793 0.0882 0.2592 -0.0027 -0.0043 -0.0251 226 PHE   A CA  
1778 C  C   . PHE   A 225 ? 0.2222 0.1001 0.2300 0.0258  0.0414  0.0000  226 PHE   A C   
1779 O  O   . PHE   A 225 ? 0.1278 0.1732 0.2583 0.0249  -0.0167 0.0001  226 PHE   A O   
1780 C  CB  . PHE   A 225 ? 0.1629 0.1077 0.2620 0.0055  -0.0358 0.0193  226 PHE   A CB  
1781 C  CG  . PHE   A 225 ? 0.1594 0.1615 0.2554 -0.0077 -0.0085 -0.0201 226 PHE   A CG  
1782 C  CD1 . PHE   A 225 ? 0.2343 0.2127 0.2576 0.0639  -0.0114 -0.0040 226 PHE   A CD1 
1783 C  CD2 . PHE   A 225 ? 0.1856 0.2201 0.2878 -0.0001 -0.0116 -0.0399 226 PHE   A CD2 
1784 C  CE1 . PHE   A 225 ? 0.2658 0.2146 0.2878 0.0455  0.0336  -0.0136 226 PHE   A CE1 
1785 C  CE2 . PHE   A 225 ? 0.1726 0.2878 0.3272 0.0271  -0.0458 -0.1134 226 PHE   A CE2 
1786 C  CZ  . PHE   A 225 ? 0.2477 0.0958 0.2979 -0.0024 -0.0372 -0.0442 226 PHE   A CZ  
1787 N  N   . ARG   A 226 ? 0.1504 0.0872 0.2545 -0.0072 -0.0006 0.0000  227 ARG   A N   
1788 C  CA  . ARG   A 226 ? 0.1431 0.1251 0.2452 -0.0168 -0.0299 0.0343  227 ARG   A CA  
1789 C  C   . ARG   A 226 ? 0.1285 0.1671 0.2691 -0.0290 -0.0111 0.0152  227 ARG   A C   
1790 O  O   . ARG   A 226 ? 0.1535 0.1371 0.3165 0.0240  -0.0376 -0.0041 227 ARG   A O   
1791 C  CB  . ARG   A 226 ? 0.1845 0.1129 0.2409 0.0466  0.0033  0.0405  227 ARG   A CB  
1792 C  CG  . ARG   A 226 ? 0.1456 0.1098 0.2449 0.0179  -0.0248 0.0403  227 ARG   A CG  
1793 C  CD  . ARG   A 226 ? 0.2373 0.1027 0.2509 0.0040  -0.0228 0.0322  227 ARG   A CD  
1794 N  NE  . ARG   A 226 ? 0.2061 0.1055 0.2755 -0.0025 -0.0186 0.0200  227 ARG   A NE  
1795 C  CZ  . ARG   A 226 ? 0.2213 0.1411 0.2490 -0.0300 -0.0197 0.0183  227 ARG   A CZ  
1796 N  NH1 . ARG   A 226 ? 0.2497 0.2133 0.2968 -0.0065 -0.0424 -0.0451 227 ARG   A NH1 
1797 N  NH2 . ARG   A 226 ? 0.2746 0.1337 0.2718 -0.0490 -0.0216 0.0047  227 ARG   A NH2 
1798 N  N   . LYS   A 227 ? 0.1773 0.1181 0.2273 -0.0166 -0.0471 -0.0240 228 LYS   A N   
1799 C  CA  . LYS   A 227 ? 0.2114 0.1384 0.2495 -0.0047 -0.0378 -0.0589 228 LYS   A CA  
1800 C  C   . LYS   A 227 ? 0.2122 0.1569 0.2274 0.0011  -0.0223 -0.0035 228 LYS   A C   
1801 O  O   . LYS   A 227 ? 0.2449 0.1156 0.2808 0.0140  -0.0002 -0.0264 228 LYS   A O   
1802 C  CB  . LYS   A 227 ? 0.2088 0.1707 0.2601 -0.0121 -0.0465 -0.0359 228 LYS   A CB  
1803 C  CG  . LYS   A 227 ? 0.2827 0.2084 0.3091 -0.0719 -0.0409 -0.0458 228 LYS   A CG  
1804 C  CD  . LYS   A 227 ? 0.3398 0.2584 0.3402 -0.1580 -0.0536 -0.0578 228 LYS   A CD  
1805 C  CE  . LYS   A 227 ? 0.5067 0.5347 0.3123 -0.1587 -0.0430 -0.0763 228 LYS   A CE  
1806 N  NZ  . LYS   A 227 ? 0.7428 0.6426 0.5294 -0.1332 -0.2528 -0.1055 228 LYS   A NZ  
1807 N  N   . LEU   A 228 ? 0.1503 0.1410 0.2615 -0.0167 -0.0342 -0.0094 229 LEU   A N   
1808 C  CA  . LEU   A 228 ? 0.1594 0.1162 0.2466 -0.0113 -0.0142 -0.0210 229 LEU   A CA  
1809 C  C   . LEU   A 228 ? 0.1896 0.1474 0.2380 0.0031  -0.0217 -0.0135 229 LEU   A C   
1810 O  O   . LEU   A 228 ? 0.2395 0.1109 0.2552 -0.0034 -0.0178 -0.0109 229 LEU   A O   
1811 C  CB  . LEU   A 228 ? 0.1503 0.1381 0.2393 0.0012  -0.0099 -0.0272 229 LEU   A CB  
1812 C  CG  . LEU   A 228 ? 0.1389 0.2188 0.2391 -0.0111 -0.0187 0.0210  229 LEU   A CG  
1813 C  CD1 . LEU   A 228 ? 0.1504 0.1594 0.2463 -0.0184 -0.0416 0.0026  229 LEU   A CD1 
1814 C  CD2 . LEU   A 228 ? 0.1799 0.1949 0.2377 -0.0320 0.0071  0.0185  229 LEU   A CD2 
1815 N  N   . ASN   A 229 ? 0.1328 0.1562 0.2562 -0.0114 0.0001  -0.0179 230 ASN   A N   
1816 C  CA  . ASN   A 229 ? 0.1270 0.1863 0.2164 0.0041  -0.0326 -0.0091 230 ASN   A CA  
1817 C  C   . ASN   A 229 ? 0.1697 0.1101 0.2329 0.0018  -0.0358 0.0305  230 ASN   A C   
1818 O  O   . ASN   A 229 ? 0.1210 0.1288 0.2469 0.0185  -0.0324 0.0232  230 ASN   A O   
1819 C  CB  . ASN   A 229 ? 0.1454 0.1418 0.2352 0.0142  -0.0117 -0.0190 230 ASN   A CB  
1820 C  CG  . ASN   A 229 ? 0.1623 0.1666 0.2408 -0.0343 -0.0242 -0.0296 230 ASN   A CG  
1821 O  OD1 . ASN   A 229 ? 0.2490 0.1747 0.2772 -0.0105 0.0096  -0.0005 230 ASN   A OD1 
1822 N  ND2 . ASN   A 229 ? 0.1532 0.1827 0.3188 -0.0501 0.0082  -0.0287 230 ASN   A ND2 
1823 N  N   . PHE   A 230 ? 0.1460 0.1658 0.2483 -0.0293 -0.0384 -0.0179 231 PHE   A N   
1824 C  CA  . PHE   A 230 ? 0.1036 0.1375 0.2275 -0.0089 -0.0277 0.0017  231 PHE   A CA  
1825 C  C   . PHE   A 230 ? 0.1982 0.1536 0.2207 0.0024  -0.0113 0.0003  231 PHE   A C   
1826 O  O   . PHE   A 230 ? 0.1569 0.1339 0.2741 -0.0135 -0.0078 0.0160  231 PHE   A O   
1827 C  CB  . PHE   A 230 ? 0.1926 0.1500 0.2082 0.0240  -0.0278 0.0167  231 PHE   A CB  
1828 C  CG  . PHE   A 230 ? 0.1520 0.1041 0.2064 0.0023  -0.0117 -0.0134 231 PHE   A CG  
1829 C  CD1 . PHE   A 230 ? 0.1432 0.1711 0.2187 0.0015  0.0050  -0.0307 231 PHE   A CD1 
1830 C  CD2 . PHE   A 230 ? 0.1951 0.0881 0.2688 -0.0258 -0.0097 -0.0083 231 PHE   A CD2 
1831 C  CE1 . PHE   A 230 ? 0.1538 0.1539 0.2606 -0.0501 -0.0432 0.0212  231 PHE   A CE1 
1832 C  CE2 . PHE   A 230 ? 0.1267 0.0991 0.2587 -0.0316 -0.0298 -0.0009 231 PHE   A CE2 
1833 C  CZ  . PHE   A 230 ? 0.1385 0.1373 0.2433 -0.0463 -0.0167 -0.0052 231 PHE   A CZ  
1834 N  N   . ASN   A 231 ? 0.2141 0.2131 0.2077 0.0682  0.0156  0.0100  232 ASN   A N   
1835 C  CA  . ASN   A 231 ? 0.2030 0.1693 0.2502 0.0477  0.0041  0.0044  232 ASN   A CA  
1836 C  C   . ASN   A 231 ? 0.1788 0.1874 0.2248 0.0063  -0.0099 0.0146  232 ASN   A C   
1837 O  O   . ASN   A 231 ? 0.1662 0.1220 0.2918 0.0421  -0.0244 0.0035  232 ASN   A O   
1838 C  CB  . ASN   A 231 ? 0.1909 0.1262 0.3152 0.0383  -0.0021 -0.0108 232 ASN   A CB  
1839 C  CG  . ASN   A 231 ? 0.1876 0.1400 0.2577 0.0591  0.0126  -0.0068 232 ASN   A CG  
1840 O  OD1 . ASN   A 231 ? 0.2407 0.2000 0.3065 0.0035  0.0369  -0.0156 232 ASN   A OD1 
1841 N  ND2 . ASN   A 231 ? 0.1368 0.2135 0.2665 0.0034  0.0024  -0.0021 232 ASN   A ND2 
1842 N  N   . GLY   A 232 ? 0.1867 0.1532 0.2602 0.0204  0.0160  0.0118  233 GLY   A N   
1843 C  CA  . GLY   A 232 ? 0.2100 0.1673 0.2695 -0.0111 -0.0016 0.0377  233 GLY   A CA  
1844 C  C   . GLY   A 232 ? 0.1872 0.1459 0.2611 0.0443  0.0308  0.0460  233 GLY   A C   
1845 O  O   . GLY   A 232 ? 0.2005 0.1561 0.3024 0.0652  0.0146  0.0036  233 GLY   A O   
1846 N  N   . GLU   A 233 ? 0.1208 0.2815 0.2456 -0.0215 -0.0016 0.0357  234 GLU   A N   
1847 C  CA  . GLU   A 233 ? 0.2199 0.2438 0.2700 0.1028  0.0022  0.0239  234 GLU   A CA  
1848 C  C   . GLU   A 233 ? 0.2294 0.2031 0.3019 0.0697  0.0273  0.0131  234 GLU   A C   
1849 O  O   . GLU   A 233 ? 0.2124 0.3134 0.3071 0.0093  0.0041  0.0046  234 GLU   A O   
1850 C  CB  . GLU   A 233 ? 0.2193 0.1597 0.3118 0.0690  0.0161  0.0488  234 GLU   A CB  
1851 C  CG  . GLU   A 233 ? 0.2237 0.1982 0.3021 -0.0368 0.0150  0.0646  234 GLU   A CG  
1852 C  CD  . GLU   A 233 ? 0.2835 0.2866 0.3000 0.0417  -0.0201 0.0211  234 GLU   A CD  
1853 O  OE1 . GLU   A 233 ? 0.3643 0.2463 0.3986 -0.0330 -0.0321 0.0011  234 GLU   A OE1 
1854 O  OE2 . GLU   A 233 ? 0.2494 0.3675 0.3481 0.0505  -0.0809 -0.0251 234 GLU   A OE2 
1855 N  N   . GLY   A 234 ? 0.2977 0.2448 0.3054 0.0724  0.0245  -0.0111 235 GLY   A N   
1856 C  CA  . GLY   A 234 ? 0.2568 0.2886 0.4142 0.0937  0.0212  0.0330  235 GLY   A CA  
1857 C  C   . GLY   A 234 ? 0.2969 0.4684 0.3086 0.0853  0.0250  0.0051  235 GLY   A C   
1858 O  O   . GLY   A 234 ? 0.3240 0.4908 0.3351 0.1638  0.0763  0.0414  235 GLY   A O   
1859 N  N   . GLU   A 235 ? 0.2603 0.1830 0.3499 -0.0023 -0.0082 0.0644  236 GLU   A N   
1860 C  CA  . GLU   A 235 ? 0.2519 0.1113 0.3267 -0.0100 -0.0160 0.0331  236 GLU   A CA  
1861 C  C   . GLU   A 235 ? 0.2086 0.0969 0.3480 0.0166  0.0304  0.0087  236 GLU   A C   
1862 O  O   . GLU   A 235 ? 0.2397 0.1786 0.3962 -0.0192 0.0313  -0.0029 236 GLU   A O   
1863 C  CB  . GLU   A 235 ? 0.1618 0.1820 0.3265 -0.0037 -0.0334 0.0302  236 GLU   A CB  
1864 C  CG  . GLU   A 235 ? 0.2825 0.1750 0.3185 -0.0373 0.0155  0.0350  236 GLU   A CG  
1865 C  CD  . GLU   A 235 ? 0.5079 0.2535 0.3820 -0.0873 0.0312  -0.0204 236 GLU   A CD  
1866 O  OE1 . GLU   A 235 ? 0.2337 0.2066 0.4012 -0.0149 -0.0063 -0.0334 236 GLU   A OE1 
1867 O  OE2 . GLU   A 235 ? 0.7127 0.1964 0.5662 -0.0619 0.0023  -0.0016 236 GLU   A OE2 
1868 N  N   . PRO   A 236 ? 0.2215 0.1542 0.3163 0.0372  0.0486  0.0454  237 PRO   A N   
1869 C  CA  . PRO   A 236 ? 0.1682 0.1592 0.3129 0.0365  0.0374  0.0450  237 PRO   A CA  
1870 C  C   . PRO   A 236 ? 0.2355 0.1621 0.2588 -0.0205 0.0452  0.0227  237 PRO   A C   
1871 O  O   . PRO   A 236 ? 0.2014 0.2036 0.2899 0.0003  0.0290  -0.0174 237 PRO   A O   
1872 C  CB  . PRO   A 236 ? 0.1468 0.1435 0.4282 0.0592  0.0410  0.0381  237 PRO   A CB  
1873 C  CG  . PRO   A 236 ? 0.2459 0.1274 0.4226 0.0547  0.0596  0.0657  237 PRO   A CG  
1874 C  CD  . PRO   A 236 ? 0.2003 0.1483 0.4104 0.0816  0.0974  0.0164  237 PRO   A CD  
1875 N  N   . GLU   A 237 ? 0.1946 0.1461 0.3355 0.0052  0.0232  0.0300  238 GLU   A N   
1876 C  CA  . GLU   A 237 ? 0.1765 0.2196 0.2657 -0.0016 0.0021  -0.0265 238 GLU   A CA  
1877 C  C   . GLU   A 237 ? 0.2267 0.1456 0.2756 0.0348  0.0264  0.0154  238 GLU   A C   
1878 O  O   . GLU   A 237 ? 0.2136 0.1400 0.3085 0.0241  -0.0220 0.0159  238 GLU   A O   
1879 C  CB  . GLU   A 237 ? 0.2168 0.2106 0.3508 -0.0274 -0.0040 -0.0397 238 GLU   A CB  
1880 C  CG  . GLU   A 237 ? 0.2860 0.3001 0.3909 -0.0486 0.0675  -0.1323 238 GLU   A CG  
1881 C  CD  . GLU   A 237 ? 0.3348 0.2370 0.4431 0.0212  -0.0596 -0.0559 238 GLU   A CD  
1882 O  OE1 . GLU   A 237 ? 0.3334 0.2409 0.5894 0.0558  0.0532  -0.0842 238 GLU   A OE1 
1883 O  OE2 . GLU   A 237 ? 0.3008 0.2077 0.3517 -0.0100 -0.0199 -0.0734 238 GLU   A OE2 
1884 N  N   . GLU   A 238 ? 0.1750 0.1513 0.2586 -0.0093 -0.0041 -0.0144 239 GLU   A N   
1885 C  CA  . GLU   A 238 ? 0.1445 0.1490 0.2720 0.0222  0.0138  -0.0186 239 GLU   A CA  
1886 C  C   . GLU   A 238 ? 0.1483 0.1313 0.2504 0.0334  0.0234  -0.0217 239 GLU   A C   
1887 O  O   . GLU   A 238 ? 0.1637 0.1201 0.2664 0.0307  -0.0074 -0.0143 239 GLU   A O   
1888 C  CB  . GLU   A 238 ? 0.2323 0.1763 0.3204 -0.0291 -0.0203 -0.0172 239 GLU   A CB  
1889 C  CG  . GLU   A 238 ? 0.2330 0.2084 0.3953 0.0379  -0.0055 -0.0463 239 GLU   A CG  
1890 C  CD  . GLU   A 238 ? 0.5444 0.2853 0.3890 -0.0878 -0.0489 -0.0541 239 GLU   A CD  
1891 O  OE1 . GLU   A 238 ? 0.3705 0.4004 0.3998 -0.1178 -0.0397 -0.1016 239 GLU   A OE1 
1892 O  OE2 . GLU   A 238 ? 0.2869 0.3725 0.4770 -0.0939 -0.0434 -0.0478 239 GLU   A OE2 
1893 N  N   . LEU   A 239 ? 0.1518 0.1569 0.2450 0.0298  0.0340  -0.0181 240 LEU   A N   
1894 C  CA  . LEU   A 239 ? 0.1398 0.1522 0.2728 0.0078  0.0144  0.0089  240 LEU   A CA  
1895 C  C   . LEU   A 239 ? 0.1142 0.1538 0.2521 0.0071  0.0044  0.0094  240 LEU   A C   
1896 O  O   . LEU   A 239 ? 0.1698 0.1421 0.2651 -0.0168 0.0048  -0.0203 240 LEU   A O   
1897 C  CB  . LEU   A 239 ? 0.1679 0.1431 0.2519 0.0166  -0.0139 0.0276  240 LEU   A CB  
1898 C  CG  . LEU   A 239 ? 0.2121 0.1414 0.2966 0.0608  -0.0359 -0.0200 240 LEU   A CG  
1899 C  CD1 . LEU   A 239 ? 0.2170 0.1169 0.4395 0.0846  -0.0982 -0.0366 240 LEU   A CD1 
1900 C  CD2 . LEU   A 239 ? 0.2000 0.1500 0.3246 -0.0030 -0.0681 -0.0212 240 LEU   A CD2 
1901 N  N   . MET   A 240 ? 0.1324 0.0912 0.2599 0.0020  -0.0114 -0.0020 241 MET   A N   
1902 C  CA  . MET   A 240 ? 0.1946 0.1411 0.2282 0.0219  -0.0122 0.0226  241 MET   A CA  
1903 C  C   . MET   A 240 ? 0.1908 0.1658 0.1808 -0.0251 -0.0304 -0.0167 241 MET   A C   
1904 O  O   . MET   A 240 ? 0.1722 0.1134 0.2751 0.0137  -0.0285 0.0015  241 MET   A O   
1905 C  CB  . MET   A 240 ? 0.2054 0.1053 0.2652 0.0070  -0.0315 0.0133  241 MET   A CB  
1906 C  CG  . MET   A 240 ? 0.1338 0.1339 0.2929 0.0449  0.0001  -0.0104 241 MET   A CG  
1907 S  SD  . MET   A 240 ? 0.1449 0.1269 0.3010 -0.0078 -0.0271 -0.0066 241 MET   A SD  
1908 C  CE  . MET   A 240 ? 0.1513 0.1294 0.3323 -0.0177 -0.0121 0.0242  241 MET   A CE  
1909 N  N   . VAL   A 241 ? 0.1808 0.1330 0.2104 0.0073  -0.0189 0.0107  242 VAL   A N   
1910 C  CA  . VAL   A 241 ? 0.1648 0.0785 0.1996 0.0221  -0.0171 -0.0104 242 VAL   A CA  
1911 C  C   . VAL   A 241 ? 0.1475 0.0968 0.2072 0.0370  -0.0130 -0.0084 242 VAL   A C   
1912 O  O   . VAL   A 241 ? 0.1678 0.1201 0.2459 -0.0227 -0.0137 0.0139  242 VAL   A O   
1913 C  CB  . VAL   A 241 ? 0.1047 0.0709 0.2396 -0.0093 -0.0457 -0.0145 242 VAL   A CB  
1914 C  CG1 . VAL   A 241 ? 0.1884 0.1098 0.2477 -0.0359 -0.0752 0.0106  242 VAL   A CG1 
1915 C  CG2 . VAL   A 241 ? 0.1402 0.1461 0.2813 0.0211  0.0029  -0.0228 242 VAL   A CG2 
1916 N  N   . ASP   A 242 ? 0.2043 0.0879 0.1974 0.0122  -0.0059 -0.0282 243 ASP   A N   
1917 C  CA  . ASP   A 242 ? 0.1416 0.1050 0.2024 0.0578  -0.0054 -0.0137 243 ASP   A CA  
1918 C  C   . ASP   A 242 ? 0.1511 0.1344 0.2391 0.0030  -0.0425 -0.0242 243 ASP   A C   
1919 O  O   . ASP   A 242 ? 0.1439 0.1091 0.2767 -0.0025 -0.0292 0.0086  243 ASP   A O   
1920 C  CB  . ASP   A 242 ? 0.1195 0.0872 0.2588 0.0383  -0.0264 -0.0128 243 ASP   A CB  
1921 C  CG  . ASP   A 242 ? 0.1720 0.1210 0.1985 0.0168  -0.0199 -0.0051 243 ASP   A CG  
1922 O  OD1 . ASP   A 242 ? 0.2023 0.1055 0.2545 -0.0021 -0.0098 -0.0096 243 ASP   A OD1 
1923 O  OD2 . ASP   A 242 ? 0.1750 0.1159 0.2805 0.0275  0.0109  -0.0121 243 ASP   A OD2 
1924 N  N   . ASN   A 243 ? 0.1269 0.1023 0.2292 -0.0272 -0.0096 -0.0274 244 ASN   A N   
1925 C  CA  . ASN   A 243 ? 0.1671 0.0971 0.2253 -0.0038 -0.0388 -0.0217 244 ASN   A CA  
1926 C  C   . ASN   A 243 ? 0.1722 0.0791 0.2207 0.0308  -0.0399 -0.0082 244 ASN   A C   
1927 O  O   . ASN   A 243 ? 0.1203 0.0693 0.2576 0.0147  -0.0082 0.0044  244 ASN   A O   
1928 C  CB  . ASN   A 243 ? 0.1339 0.1270 0.1985 0.0042  -0.0363 -0.0266 244 ASN   A CB  
1929 C  CG  . ASN   A 243 ? 0.1378 0.1619 0.2303 0.0132  -0.0330 0.0182  244 ASN   A CG  
1930 O  OD1 . ASN   A 243 ? 0.1769 0.1377 0.2346 0.0133  -0.0174 0.0021  244 ASN   A OD1 
1931 N  ND2 . ASN   A 243 ? 0.1438 0.1249 0.2479 -0.0034 -0.0806 -0.0002 244 ASN   A ND2 
1932 N  N   . TRP   A 244 ? 0.1457 0.1199 0.2308 -0.0400 -0.0168 0.0194  245 TRP   A N   
1933 C  CA  . TRP   A 244 ? 0.1064 0.0876 0.2236 -0.0425 -0.0310 -0.0159 245 TRP   A CA  
1934 C  C   . TRP   A 244 ? 0.0944 0.1804 0.2524 0.0118  -0.0337 -0.0273 245 TRP   A C   
1935 O  O   . TRP   A 244 ? 0.1156 0.1048 0.2864 0.0102  -0.0256 -0.0272 245 TRP   A O   
1936 C  CB  . TRP   A 244 ? 0.0883 0.0962 0.2598 -0.0177 -0.0041 0.0054  245 TRP   A CB  
1937 C  CG  . TRP   A 244 ? 0.1366 0.1248 0.2373 0.0208  -0.0100 -0.0027 245 TRP   A CG  
1938 C  CD1 . TRP   A 244 ? 0.1019 0.0766 0.2632 0.0445  0.0128  -0.0059 245 TRP   A CD1 
1939 C  CD2 . TRP   A 244 ? 0.1449 0.1165 0.2237 0.0155  0.0061  0.0086  245 TRP   A CD2 
1940 N  NE1 . TRP   A 244 ? 0.1172 0.0734 0.2187 0.0346  -0.0203 0.0118  245 TRP   A NE1 
1941 C  CE2 . TRP   A 244 ? 0.1012 0.1098 0.2262 0.0206  -0.0367 0.0089  245 TRP   A CE2 
1942 C  CE3 . TRP   A 244 ? 0.0894 0.1230 0.2485 0.0023  -0.0320 0.0126  245 TRP   A CE3 
1943 C  CZ2 . TRP   A 244 ? 0.1292 0.1587 0.2381 0.0444  -0.0348 0.0376  245 TRP   A CZ2 
1944 C  CZ3 . TRP   A 244 ? 0.1048 0.1429 0.2970 0.0256  -0.0215 0.0104  245 TRP   A CZ3 
1945 C  CH2 . TRP   A 244 ? 0.1368 0.1679 0.2663 0.0220  -0.0293 0.0103  245 TRP   A CH2 
1946 N  N   . ARG   A 245 ? 0.1047 0.1145 0.2086 0.0105  -0.0512 0.0070  246 ARG   A N   
1947 C  CA  . ARG   A 245 ? 0.1274 0.0815 0.1993 -0.0157 -0.0539 -0.0051 246 ARG   A CA  
1948 C  C   . ARG   A 245 ? 0.1421 0.1190 0.2175 0.0081  -0.0268 0.0104  246 ARG   A C   
1949 O  O   . ARG   A 245 ? 0.1666 0.1116 0.2639 -0.0071 -0.0017 0.0062  246 ARG   A O   
1950 C  CB  . ARG   A 245 ? 0.1547 0.1138 0.2135 -0.0282 -0.0461 -0.0496 246 ARG   A CB  
1951 C  CG  . ARG   A 245 ? 0.1296 0.1439 0.2452 -0.0080 -0.0644 -0.0359 246 ARG   A CG  
1952 C  CD  . ARG   A 245 ? 0.1155 0.1676 0.2513 -0.0261 -0.0476 -0.0510 246 ARG   A CD  
1953 N  NE  . ARG   A 245 ? 0.0885 0.1524 0.2874 -0.0232 -0.0290 -0.0436 246 ARG   A NE  
1954 C  CZ  . ARG   A 245 ? 0.0900 0.1802 0.2413 -0.0364 -0.0134 -0.0430 246 ARG   A CZ  
1955 N  NH1 . ARG   A 245 ? 0.1574 0.1174 0.2187 0.0012  -0.0189 0.0048  246 ARG   A NH1 
1956 N  NH2 . ARG   A 245 ? 0.0833 0.2016 0.2633 -0.0199 -0.0203 -0.0222 246 ARG   A NH2 
1957 N  N   . PRO   A 246 ? 0.1152 0.1046 0.2538 -0.0076 -0.0318 -0.0031 247 PRO   A N   
1958 C  CA  . PRO   A 246 ? 0.1000 0.1438 0.2601 0.0357  -0.0083 0.0081  247 PRO   A CA  
1959 C  C   . PRO   A 246 ? 0.1404 0.1629 0.2280 0.0334  -0.0247 0.0078  247 PRO   A C   
1960 O  O   . PRO   A 246 ? 0.1301 0.1368 0.2548 0.0147  -0.0190 0.0063  247 PRO   A O   
1961 C  CB  . PRO   A 246 ? 0.2396 0.1353 0.2707 0.1465  -0.0024 0.0323  247 PRO   A CB  
1962 C  CG  . PRO   A 246 ? 0.2520 0.2115 0.3538 0.0995  0.0321  0.1220  247 PRO   A CG  
1963 C  CD  . PRO   A 246 ? 0.1116 0.1273 0.3242 0.0192  0.0027  0.0493  247 PRO   A CD  
1964 N  N   . ALA   A 247 ? 0.1662 0.1795 0.2382 0.0108  -0.0137 0.0092  248 ALA   A N   
1965 C  CA  . ALA   A 247 ? 0.1147 0.1885 0.2314 -0.0157 -0.0096 0.0120  248 ALA   A CA  
1966 C  C   . ALA   A 247 ? 0.1242 0.1607 0.2368 0.0109  -0.0109 -0.0197 248 ALA   A C   
1967 O  O   . ALA   A 247 ? 0.1539 0.1665 0.2825 0.0302  -0.0234 0.0287  248 ALA   A O   
1968 C  CB  . ALA   A 247 ? 0.1999 0.1852 0.2547 -0.0075 0.0092  0.0357  248 ALA   A CB  
1969 N  N   . GLN   A 248 ? 0.1504 0.1252 0.2429 -0.0119 -0.0682 -0.0149 249 GLN   A N   
1970 C  CA  . GLN   A 248 ? 0.0930 0.1226 0.2569 -0.0145 -0.0452 0.0163  249 GLN   A CA  
1971 C  C   . GLN   A 248 ? 0.1511 0.1460 0.2414 0.0535  -0.0337 0.0212  249 GLN   A C   
1972 O  O   . GLN   A 248 ? 0.1959 0.1553 0.2580 0.0341  0.0027  0.0133  249 GLN   A O   
1973 C  CB  . GLN   A 248 ? 0.1637 0.1326 0.2452 -0.0139 -0.0337 0.0284  249 GLN   A CB  
1974 C  CG  . GLN   A 248 ? 0.1375 0.1680 0.2424 0.0223  -0.0284 -0.0097 249 GLN   A CG  
1975 C  CD  . GLN   A 248 ? 0.1406 0.1508 0.2541 0.0016  0.0027  0.0015  249 GLN   A CD  
1976 O  OE1 . GLN   A 248 ? 0.1612 0.2283 0.3202 -0.0414 -0.0219 -0.0020 249 GLN   A OE1 
1977 N  NE2 . GLN   A 248 ? 0.1734 0.1831 0.2552 0.0335  -0.0319 -0.0040 249 GLN   A NE2 
1978 N  N   . PRO   A 249 ? 0.1446 0.1594 0.2278 0.0080  -0.0105 0.0089  250 PRO   A N   
1979 C  CA  . PRO   A 249 ? 0.1162 0.2089 0.2226 0.0402  -0.0186 -0.0162 250 PRO   A CA  
1980 C  C   . PRO   A 249 ? 0.1704 0.1770 0.2341 0.0473  -0.0164 -0.0291 250 PRO   A C   
1981 O  O   . PRO   A 249 ? 0.1206 0.2193 0.2473 0.0096  -0.0434 0.0337  250 PRO   A O   
1982 C  CB  . PRO   A 249 ? 0.1156 0.3166 0.2850 0.0802  -0.0743 -0.0252 250 PRO   A CB  
1983 C  CG  . PRO   A 249 ? 0.2375 0.3856 0.2391 0.0566  -0.0550 -0.0265 250 PRO   A CG  
1984 C  CD  . PRO   A 249 ? 0.1134 0.3241 0.2969 0.0274  -0.0638 0.0197  250 PRO   A CD  
1985 N  N   . LEU   A 250 ? 0.1597 0.1679 0.2811 0.0296  -0.0275 -0.0006 251 LEU   A N   
1986 C  CA  . LEU   A 250 ? 0.1057 0.1854 0.2724 -0.0038 -0.0212 -0.0153 251 LEU   A CA  
1987 C  C   . LEU   A 250 ? 0.1220 0.1226 0.2518 0.0340  -0.0192 -0.0119 251 LEU   A C   
1988 O  O   . LEU   A 250 ? 0.1416 0.1037 0.2773 0.0258  -0.0424 -0.0211 251 LEU   A O   
1989 C  CB  . LEU   A 250 ? 0.1183 0.2072 0.2938 -0.0093 0.0117  -0.0175 251 LEU   A CB  
1990 C  CG  . LEU   A 250 ? 0.1381 0.2064 0.2916 -0.0172 0.0396  0.0094  251 LEU   A CG  
1991 C  CD1 . LEU   A 250 ? 0.1665 0.2099 0.3084 0.0006  -0.0308 -0.0258 251 LEU   A CD1 
1992 C  CD2 . LEU   A 250 ? 0.2014 0.2247 0.3421 -0.0680 0.0540  -0.0067 251 LEU   A CD2 
1993 N  N   . LYS   A 251 ? 0.1842 0.2175 0.2388 0.0403  -0.0555 -0.0111 252 LYS   A N   
1994 C  CA  . LYS   A 251 ? 0.1758 0.2319 0.3014 -0.0034 -0.0199 -0.0337 252 LYS   A CA  
1995 C  C   . LYS   A 251 ? 0.1935 0.2353 0.2427 0.0151  -0.0504 -0.0074 252 LYS   A C   
1996 O  O   . LYS   A 251 ? 0.2339 0.2965 0.3192 -0.0119 -0.0333 0.0494  252 LYS   A O   
1997 C  CB  . LYS   A 251 ? 0.2406 0.1804 0.2796 0.0055  -0.0561 -0.0257 252 LYS   A CB  
1998 C  CG  . LYS   A 251 ? 0.3195 0.2890 0.3315 -0.0556 0.0811  -0.0687 252 LYS   A CG  
1999 C  CD  . LYS   A 251 ? 0.3871 0.4154 0.5062 -0.1366 0.1067  -0.0884 252 LYS   A CD  
2000 C  CE  . LYS   A 251 ? 0.4003 0.3541 0.5513 -0.1645 0.0880  -0.2424 252 LYS   A CE  
2001 N  NZ  . LYS   A 251 ? 0.4860 0.3820 0.7764 0.1666  0.1196  0.0710  252 LYS   A NZ  
2002 N  N   . ASN   A 252 ? 0.1722 0.2561 0.2751 -0.0042 -0.0820 -0.0297 253 ASN   A N   
2003 C  CA  . ASN   A 252 ? 0.2014 0.5179 0.3377 0.0201  -0.0928 -0.1107 253 ASN   A CA  
2004 C  C   . ASN   A 252 ? 0.1586 0.3583 0.4330 0.0229  -0.0414 -0.0337 253 ASN   A C   
2005 O  O   . ASN   A 252 ? 0.3741 0.4049 0.4193 0.1353  -0.0030 0.0037  253 ASN   A O   
2006 C  CB  . ASN   A 252 ? 0.2873 0.6100 0.5829 -0.0307 -0.2116 -0.2063 253 ASN   A CB  
2007 C  CG  . ASN   A 252 ? 0.2614 1.1629 0.6473 -0.1153 -0.1591 -0.0972 253 ASN   A CG  
2008 O  OD1 . ASN   A 252 ? 0.3380 1.0908 0.5460 0.0136  -0.0966 0.0020  253 ASN   A OD1 
2009 N  ND2 . ASN   A 252 ? 0.3552 1.3250 0.9565 -0.0683 -0.3410 -0.0898 253 ASN   A ND2 
2010 N  N   . ARG   A 253 ? 0.0987 0.3365 0.3759 0.0333  -0.0343 0.0066  254 ARG   A N   
2011 C  CA  . ARG   A 253 ? 0.1208 0.1483 0.2396 0.0190  -0.0070 0.0263  254 ARG   A CA  
2012 C  C   . ARG   A 253 ? 0.1465 0.1766 0.3379 0.0150  0.0348  0.0265  254 ARG   A C   
2013 O  O   . ARG   A 253 ? 0.2891 0.1989 0.4718 0.0626  0.0694  0.0530  254 ARG   A O   
2014 C  CB  . ARG   A 253 ? 0.1360 0.1174 0.2136 -0.0095 -0.0451 0.0140  254 ARG   A CB  
2015 C  CG  . ARG   A 253 ? 0.1504 0.1210 0.2214 -0.0149 0.0073  -0.0195 254 ARG   A CG  
2016 C  CD  . ARG   A 253 ? 0.1622 0.1222 0.2190 0.0296  -0.0038 -0.0369 254 ARG   A CD  
2017 N  NE  . ARG   A 253 ? 0.1328 0.0840 0.2381 0.0077  -0.0232 -0.0263 254 ARG   A NE  
2018 C  CZ  . ARG   A 253 ? 0.1518 0.1283 0.2142 -0.0083 -0.0054 -0.0250 254 ARG   A CZ  
2019 N  NH1 . ARG   A 253 ? 0.1439 0.1386 0.2398 -0.0548 -0.0217 0.0109  254 ARG   A NH1 
2020 N  NH2 . ARG   A 253 ? 0.0953 0.1355 0.2218 0.0035  -0.0411 0.0024  254 ARG   A NH2 
2021 N  N   . GLN   A 254 ? 0.1144 0.1919 0.2820 -0.0046 -0.0413 -0.0442 255 GLN   A N   
2022 C  CA  . GLN   A 254 ? 0.1517 0.2400 0.2477 -0.0318 -0.0541 -0.0245 255 GLN   A CA  
2023 C  C   . GLN   A 254 ? 0.1761 0.2103 0.2635 0.0059  -0.0722 -0.0155 255 GLN   A C   
2024 O  O   . GLN   A 254 ? 0.2513 0.1993 0.3295 -0.0294 -0.0878 0.0025  255 GLN   A O   
2025 C  CB  . GLN   A 254 ? 0.3080 0.5085 0.2128 0.0696  -0.0514 -0.0582 255 GLN   A CB  
2026 C  CG  . GLN   A 254 ? 0.6499 0.5505 0.3934 0.1404  0.1407  -0.0234 255 GLN   A CG  
2027 C  CD  . GLN   A 254 ? 0.8088 0.2823 0.5787 -0.0534 -0.1449 -0.0847 255 GLN   A CD  
2028 O  OE1 . GLN   A 254 ? 1.1128 0.3268 1.3846 -0.0136 0.0778  -0.3010 255 GLN   A OE1 
2029 N  NE2 . GLN   A 254 ? 0.7992 0.2616 0.7431 0.0969  0.0030  -0.0302 255 GLN   A NE2 
2030 N  N   . ILE   A 255 ? 0.1303 0.1982 0.2463 0.0019  -0.0318 -0.0185 256 ILE   A N   
2031 C  CA  . ILE   A 255 ? 0.1565 0.1694 0.2265 -0.0068 -0.0153 -0.0351 256 ILE   A CA  
2032 C  C   . ILE   A 255 ? 0.1759 0.1429 0.2402 0.0516  0.0248  -0.0048 256 ILE   A C   
2033 O  O   . ILE   A 255 ? 0.1590 0.1852 0.2646 0.0042  -0.0039 0.0350  256 ILE   A O   
2034 C  CB  . ILE   A 255 ? 0.1255 0.1590 0.2143 0.0438  -0.0271 -0.0232 256 ILE   A CB  
2035 C  CG1 . ILE   A 255 ? 0.1496 0.1982 0.2657 0.1044  0.0136  -0.0256 256 ILE   A CG1 
2036 C  CG2 . ILE   A 255 ? 0.2142 0.1650 0.2222 0.0152  -0.0675 -0.0343 256 ILE   A CG2 
2037 C  CD1 . ILE   A 255 ? 0.1806 0.1738 0.2521 0.0138  -0.0376 -0.0546 256 ILE   A CD1 
2038 N  N   . LYS   A 256 ? 0.1432 0.1543 0.2445 -0.0067 -0.0285 0.0141  257 LYS   A N   
2039 C  CA  . LYS   A 256 ? 0.1525 0.1565 0.2542 -0.0119 -0.0200 -0.0250 257 LYS   A CA  
2040 C  C   . LYS   A 256 ? 0.1424 0.1169 0.1939 -0.0053 0.0008  0.0106  257 LYS   A C   
2041 O  O   . LYS   A 256 ? 0.1540 0.1870 0.1981 -0.0728 -0.0019 0.0084  257 LYS   A O   
2042 C  CB  . LYS   A 256 ? 0.1039 0.1389 0.3048 -0.0258 -0.0294 0.0003  257 LYS   A CB  
2043 C  CG  . LYS   A 256 ? 0.1793 0.1946 0.3656 -0.0649 -0.0303 -0.0983 257 LYS   A CG  
2044 C  CD  . LYS   A 256 ? 0.3751 0.2183 0.4123 -0.0605 0.0016  -0.1266 257 LYS   A CD  
2045 C  CE  . LYS   A 256 ? 0.4344 0.3115 0.5097 -0.1630 0.0244  -0.2014 257 LYS   A CE  
2046 N  NZ  . LYS   A 256 ? 0.3834 0.2845 0.7815 -0.0566 0.1499  -0.0845 257 LYS   A NZ  
2047 N  N   . ALA   A 257 ? 0.1647 0.1975 0.2422 -0.0639 0.0063  -0.0120 258 ALA   A N   
2048 C  CA  . ALA   A 257 ? 0.1320 0.1601 0.2773 -0.0111 -0.0297 0.0042  258 ALA   A CA  
2049 C  C   . ALA   A 257 ? 0.0925 0.1729 0.2312 -0.0578 -0.0089 -0.0192 258 ALA   A C   
2050 O  O   . ALA   A 257 ? 0.1835 0.2016 0.2460 -0.0089 -0.0059 -0.0538 258 ALA   A O   
2051 C  CB  . ALA   A 257 ? 0.2093 0.1560 0.3028 0.0054  -0.0248 0.0269  258 ALA   A CB  
2052 N  N   . SER   A 258 ? 0.1547 0.1732 0.2443 -0.0212 -0.0386 -0.0315 259 SER   A N   
2053 C  CA  . SER   A 258 ? 0.1179 0.2276 0.2614 -0.0253 0.0044  -0.0124 259 SER   A CA  
2054 C  C   . SER   A 258 ? 0.0958 0.2311 0.2430 -0.0190 -0.0259 -0.0108 259 SER   A C   
2055 O  O   . SER   A 258 ? 0.1055 0.3344 0.3788 0.0326  -0.0151 0.0016  259 SER   A O   
2056 C  CB  . SER   A 258 ? 0.1526 0.2024 0.2394 0.0032  -0.0313 -0.0182 259 SER   A CB  
2057 O  OG  . SER   A 258 ? 0.1396 0.2036 0.2563 -0.0234 -0.0001 -0.0106 259 SER   A OG  
2058 N  N   . PHE   A 259 ? 0.1630 0.2193 0.2596 -0.0604 -0.0280 -0.0117 260 PHE   A N   
2059 C  CA  . PHE   A 259 ? 0.1617 0.2495 0.3268 -0.0814 -0.0287 0.0000  260 PHE   A CA  
2060 C  C   . PHE   A 259 ? 0.2286 0.3607 0.3267 -0.1040 -0.0277 0.0398  260 PHE   A C   
2061 O  O   . PHE   A 259 ? 0.2804 0.2647 0.3376 -0.0659 -0.0753 0.0535  260 PHE   A O   
2062 C  CB  . PHE   A 259 ? 0.1320 0.2536 0.3413 -0.0182 -0.0104 -0.0312 260 PHE   A CB  
2063 C  CG  . PHE   A 259 ? 0.1174 0.2440 0.2817 -0.0219 -0.0425 -0.0109 260 PHE   A CG  
2064 C  CD1 . PHE   A 259 ? 0.1524 0.2348 0.2962 -0.0512 -0.0160 -0.0091 260 PHE   A CD1 
2065 C  CD2 . PHE   A 259 ? 0.2516 0.2623 0.4040 -0.0454 -0.0504 0.0347  260 PHE   A CD2 
2066 C  CE1 . PHE   A 259 ? 0.1576 0.2084 0.3314 -0.0535 -0.0447 -0.0073 260 PHE   A CE1 
2067 C  CE2 . PHE   A 259 ? 0.2962 0.2535 0.3817 -0.0460 -0.0554 0.0182  260 PHE   A CE2 
2068 C  CZ  . PHE   A 259 ? 0.2322 0.2492 0.4002 0.0323  -0.0438 0.0182  260 PHE   A CZ  
2069 N  N   . LYS   A 260 ? 0.2854 0.4592 0.3901 -0.1964 -0.0103 0.0256  261 LYS   A N   
2070 C  CA  . LYS   A 260 ? 0.5896 0.5139 0.5515 0.0936  0.0797  0.1958  261 LYS   A CA  
2071 C  C   . LYS   A 260 ? 0.7452 0.6384 0.6194 -0.0428 0.0625  0.0575  261 LYS   A C   
2072 O  O   . LYS   A 260 ? 0.4894 1.1752 1.1291 -0.0719 0.0049  -0.0392 261 LYS   A O   
2073 C  CB  . LYS   A 260 ? 0.7788 0.3156 0.6937 -0.1456 0.1297  0.0381  261 LYS   A CB  
2074 C  CG  . LYS   A 260 ? 0.8493 0.6287 0.8480 -0.4440 0.1254  0.1028  261 LYS   A CG  
2075 O  OXT . LYS   A 260 ? 0.6576 0.9181 0.8969 -0.0675 0.3512  0.1955  261 LYS   A OXT 
2076 ZN ZN  . ZN    B .   ? 0.1129 0.0967 0.2400 -0.0008 -0.0381 0.0016  301 ZN    A ZN  
2077 C  C13 . A1IEN C .   ? 0.1748 0.1353 0.2857 -0.0212 -0.0491 0.0153  302 A1IEN A C13 
2078 C  C20 . A1IEN C .   ? 0.1549 0.1508 0.2064 -0.0027 -0.0565 0.0105  302 A1IEN A C20 
2079 C  C12 . A1IEN C .   ? 0.1806 0.1101 0.3316 -0.0462 -0.0659 -0.0077 302 A1IEN A C12 
2080 C  C16 . A1IEN C .   ? 0.1601 0.1493 0.4213 -0.0133 -0.0044 -0.0035 302 A1IEN A C16 
2081 O  O22 . A1IEN C .   ? 0.1298 0.1147 0.2440 0.0039  -0.0348 -0.0088 302 A1IEN A O22 
2082 C  C23 . A1IEN C .   ? 0.1425 0.1637 0.2628 0.0315  -0.0218 -0.0455 302 A1IEN A C23 
2083 O  O21 . A1IEN C .   ? 0.2514 0.1345 0.2574 -0.0023 -0.0188 0.0176  302 A1IEN A O21 
2084 C  C2  . A1IEN C .   ? 0.1134 0.1407 0.2169 -0.0633 -0.0389 -0.0168 302 A1IEN A C2  
2085 C  C3  . A1IEN C .   ? 0.1763 0.1292 0.2169 -0.0108 -0.0042 -0.0277 302 A1IEN A C3  
2086 C  C4  . A1IEN C .   ? 0.1043 0.1158 0.2161 -0.0003 -0.0297 -0.0260 302 A1IEN A C4  
2087 C  C5  . A1IEN C .   ? 0.1450 0.1213 0.2204 0.0019  -0.0381 0.0118  302 A1IEN A C5  
2088 C  C6  . A1IEN C .   ? 0.1287 0.0854 0.2318 -0.0248 -0.0510 -0.0299 302 A1IEN A C6  
2089 S  S7  . A1IEN C .   ? 0.1483 0.0904 0.2495 -0.0018 -0.0451 -0.0163 302 A1IEN A S7  
2090 O  O9  . A1IEN C .   ? 0.1502 0.0971 0.2584 0.0281  -0.0210 -0.0128 302 A1IEN A O9  
2091 N  N10 . A1IEN C .   ? 0.0955 0.0840 0.2397 -0.0619 -0.0128 -0.0030 302 A1IEN A N10 
2092 O  O8  . A1IEN C .   ? 0.2075 0.0928 0.2706 -0.0334 -0.0718 -0.0473 302 A1IEN A O8  
2093 C  C1  . A1IEN C .   ? 0.0635 0.1181 0.2064 -0.0209 -0.0304 -0.0341 302 A1IEN A C1  
2094 S  S11 . A1IEN C .   ? 0.1709 0.1111 0.3037 0.0100  -0.0474 0.0134  302 A1IEN A S11 
2095 C  C14 . A1IEN C .   ? 0.1992 0.1977 0.3305 -0.0707 -0.0047 -0.0348 302 A1IEN A C14 
2096 C  C18 . A1IEN C .   ? 0.2595 0.2236 0.3813 -0.0383 0.0396  0.0484  302 A1IEN A C18 
2097 C  C19 . A1IEN C .   ? 0.2925 0.2827 0.4645 -0.1101 0.1078  -0.0336 302 A1IEN A C19 
2098 C  C17 . A1IEN C .   ? 0.3493 0.2063 0.4504 -0.0390 0.0525  0.0241  302 A1IEN A C17 
2099 C  C15 . A1IEN C .   ? 0.0978 0.1453 0.3370 -0.0140 -0.0643 -0.0145 302 A1IEN A C15 
2100 S  S   . DMS   D .   ? 0.3296 0.3116 0.4073 0.0047  -0.0036 -0.0111 303 DMS   A S   
2101 O  O   . DMS   D .   ? 0.3766 0.2968 0.4350 0.0084  0.0242  -0.0552 303 DMS   A O   
2102 C  C1  . DMS   D .   ? 0.4407 0.2365 0.4277 -0.0154 0.0300  0.0791  303 DMS   A C1  
2103 C  C2  . DMS   D .   ? 0.2754 0.2657 0.3511 0.0605  0.0021  -0.0310 303 DMS   A C2  
2104 O  O   . HOH   E .   ? 0.3909 0.2804 0.9962 -0.0925 0.1277  -0.2298 401 HOH   A O   
2105 O  O   . HOH   E .   ? 0.3688 0.4107 0.5624 -0.1654 0.0050  -0.1773 402 HOH   A O   
2106 O  O   . HOH   E .   ? 0.3693 0.3417 0.5480 -0.0920 -0.1307 -0.0772 403 HOH   A O   
2107 O  O   . HOH   E .   ? 0.5368 0.2871 0.4991 -0.0885 -0.1425 -0.0333 404 HOH   A O   
2108 O  O   . HOH   E .   ? 0.3730 0.7216 0.4046 0.0584  0.0222  0.0083  405 HOH   A O   
2109 O  O   . HOH   E .   ? 0.5421 0.3212 0.5982 -0.0572 0.2356  -0.0577 406 HOH   A O   
2110 O  O   . HOH   E .   ? 0.2674 0.5672 0.4835 -0.0253 -0.0567 0.0502  407 HOH   A O   
2111 O  O   . HOH   E .   ? 0.5553 0.3205 0.5453 0.0644  0.0988  0.0435  408 HOH   A O   
2112 O  O   . HOH   E .   ? 0.2897 0.2147 0.4873 -0.0570 0.1086  -0.0629 409 HOH   A O   
2113 O  O   . HOH   E .   ? 0.4279 1.0513 0.4297 0.1294  -0.1320 -0.1058 410 HOH   A O   
2114 O  O   . HOH   E .   ? 0.3302 0.5970 0.5535 0.0023  -0.0095 0.2644  411 HOH   A O   
2115 O  O   . HOH   E .   ? 0.5655 0.3123 0.4079 0.0203  0.0435  0.0816  412 HOH   A O   
2116 O  O   . HOH   E .   ? 0.3998 0.3721 0.4945 0.1137  0.1232  0.0695  413 HOH   A O   
2117 O  O   . HOH   E .   ? 0.4931 0.4264 0.6147 -0.2210 -0.0963 0.0095  414 HOH   A O   
2118 O  O   . HOH   E .   ? 0.3531 0.5825 0.3813 -0.1346 0.0082  -0.1371 415 HOH   A O   
2119 O  O   . HOH   E .   ? 0.2984 0.2554 0.6027 0.0147  0.0388  -0.1340 416 HOH   A O   
2120 O  O   . HOH   E .   ? 0.4380 0.8499 0.2617 0.0585  -0.0450 -0.0218 417 HOH   A O   
2121 O  O   . HOH   E .   ? 0.7072 0.1942 0.6325 0.0034  -0.0583 -0.0878 418 HOH   A O   
2122 O  O   . HOH   E .   ? 0.1582 0.1653 0.2348 -0.0272 -0.0362 0.0006  419 HOH   A O   
2123 O  O   . HOH   E .   ? 0.3371 0.2027 0.3370 -0.0671 -0.0422 0.0381  420 HOH   A O   
2124 O  O   . HOH   E .   ? 0.6882 0.2154 0.4280 0.0352  -0.0383 -0.0411 421 HOH   A O   
2125 O  O   . HOH   E .   ? 0.2260 0.3339 0.3198 -0.1176 0.0027  -0.0347 422 HOH   A O   
2126 O  O   . HOH   E .   ? 0.2185 0.1963 0.3258 0.0422  -0.0856 -0.0190 423 HOH   A O   
2127 O  O   . HOH   E .   ? 0.5098 0.3596 0.3981 -0.0392 -0.0122 -0.0044 424 HOH   A O   
2128 O  O   . HOH   E .   ? 0.3638 0.3022 0.5562 0.0369  -0.0837 -0.0217 425 HOH   A O   
2129 O  O   . HOH   E .   ? 0.3907 0.2251 0.3129 -0.0471 -0.1002 0.0277  426 HOH   A O   
2130 O  O   . HOH   E .   ? 0.3711 0.3303 0.3872 -0.1531 0.0917  -0.1005 427 HOH   A O   
2131 O  O   . HOH   E .   ? 0.2782 0.5080 0.5113 -0.1163 0.0622  -0.1590 428 HOH   A O   
2132 O  O   . HOH   E .   ? 0.1177 0.1603 0.2700 -0.0022 -0.0388 0.0206  429 HOH   A O   
2133 O  O   . HOH   E .   ? 0.1641 0.3191 0.4617 0.0708  -0.0399 0.0133  430 HOH   A O   
2134 O  O   . HOH   E .   ? 0.2190 0.1926 0.4683 -0.0124 -0.1231 0.0274  431 HOH   A O   
2135 O  O   . HOH   E .   ? 0.1835 0.3647 0.6149 -0.0023 -0.0610 -0.0910 432 HOH   A O   
2136 O  O   . HOH   E .   ? 0.1544 0.7804 0.5205 -0.0494 -0.0449 -0.0537 433 HOH   A O   
2137 O  O   . HOH   E .   ? 0.3865 0.3075 0.2755 0.0143  -0.0300 -0.0073 434 HOH   A O   
2138 O  O   . HOH   E .   ? 0.3166 0.3110 0.5095 0.0873  0.0355  0.0419  435 HOH   A O   
2139 O  O   . HOH   E .   ? 0.2611 0.1485 0.2433 0.0046  0.0137  0.0226  436 HOH   A O   
2140 O  O   . HOH   E .   ? 0.3375 0.2791 0.3497 0.0225  -0.0324 0.0122  437 HOH   A O   
2141 O  O   . HOH   E .   ? 0.6082 0.8626 0.4561 -0.2664 0.1760  -0.2212 438 HOH   A O   
2142 O  O   . HOH   E .   ? 0.4274 0.3636 0.4626 -0.0421 -0.0447 -0.0031 439 HOH   A O   
2143 O  O   . HOH   E .   ? 0.2390 0.6364 0.5252 0.0957  -0.0109 -0.1495 440 HOH   A O   
2144 O  O   . HOH   E .   ? 0.2096 0.7927 0.4356 0.0211  -0.0939 -0.0187 441 HOH   A O   
2145 O  O   . HOH   E .   ? 0.4453 0.2657 0.5109 0.1238  -0.0380 0.0863  442 HOH   A O   
2146 O  O   . HOH   E .   ? 0.4943 0.3873 0.7786 -0.1373 0.0579  -0.2752 443 HOH   A O   
2147 O  O   . HOH   E .   ? 0.2916 0.2038 0.4873 -0.0133 0.0089  -0.0024 444 HOH   A O   
2148 O  O   . HOH   E .   ? 0.4582 0.4075 0.3470 -0.0552 -0.0558 0.0838  445 HOH   A O   
2149 O  O   . HOH   E .   ? 0.4309 0.4862 0.4014 0.0841  0.0128  0.0055  446 HOH   A O   
2150 O  O   . HOH   E .   ? 0.5238 0.3249 0.2694 0.0089  -0.0184 -0.0058 447 HOH   A O   
2151 O  O   . HOH   E .   ? 0.2330 0.0969 0.3206 -0.0027 -0.0172 0.0467  448 HOH   A O   
2152 O  O   . HOH   E .   ? 0.2641 0.3882 0.4709 0.0041  -0.0724 -0.1412 449 HOH   A O   
2153 O  O   . HOH   E .   ? 0.2255 0.2294 0.4007 0.0026  -0.0106 -0.0430 450 HOH   A O   
2154 O  O   . HOH   E .   ? 0.2810 0.6355 0.8828 -0.2193 0.0447  -0.2972 451 HOH   A O   
2155 O  O   . HOH   E .   ? 0.4451 0.3125 0.4969 -0.0945 -0.0190 0.0644  452 HOH   A O   
2156 O  O   . HOH   E .   ? 0.2629 0.2604 0.5838 -0.0131 -0.0445 0.1522  453 HOH   A O   
2157 O  O   . HOH   E .   ? 0.4923 0.2084 0.3434 -0.1009 -0.0438 0.0567  454 HOH   A O   
2158 O  O   . HOH   E .   ? 0.3670 0.3023 0.4685 0.0443  -0.0571 -0.0892 455 HOH   A O   
2159 O  O   . HOH   E .   ? 0.7190 0.2758 0.3508 -0.0932 -0.0384 -0.0392 456 HOH   A O   
2160 O  O   . HOH   E .   ? 0.1341 0.1636 0.2588 -0.0172 -0.0498 -0.0095 457 HOH   A O   
2161 O  O   . HOH   E .   ? 0.1585 0.1028 0.2723 -0.0154 -0.0268 -0.0353 458 HOH   A O   
2162 O  O   . HOH   E .   ? 0.3533 0.2928 0.7906 -0.0456 0.0286  -0.1003 459 HOH   A O   
2163 O  O   . HOH   E .   ? 0.3231 0.5454 0.5371 0.0269  0.1527  0.1742  460 HOH   A O   
2164 O  O   . HOH   E .   ? 0.3339 0.1549 0.2996 0.0416  -0.0565 -0.0172 461 HOH   A O   
2165 O  O   . HOH   E .   ? 0.3389 0.5074 0.6716 -0.1527 -0.1722 0.0964  462 HOH   A O   
2166 O  O   . HOH   E .   ? 0.2772 0.2752 0.4337 -0.0655 -0.0709 -0.0326 463 HOH   A O   
2167 O  O   . HOH   E .   ? 0.1842 0.1705 0.2728 -0.0049 -0.0218 0.0414  464 HOH   A O   
2168 O  O   . HOH   E .   ? 0.2394 0.2709 0.3765 -0.0165 0.0686  0.0333  465 HOH   A O   
2169 O  O   . HOH   E .   ? 0.2467 0.2409 0.3533 -0.0102 -0.0577 -0.0277 466 HOH   A O   
2170 O  O   . HOH   E .   ? 0.2594 0.3850 0.5462 0.0879  -0.0369 0.0425  467 HOH   A O   
2171 O  O   . HOH   E .   ? 0.3565 0.2696 0.4400 -0.0877 -0.1036 0.0925  468 HOH   A O   
2172 O  O   . HOH   E .   ? 0.5190 0.3080 0.5672 -0.0948 0.1016  -0.0990 469 HOH   A O   
2173 O  O   . HOH   E .   ? 0.3526 0.3924 0.4631 -0.0033 -0.0704 -0.0548 470 HOH   A O   
2174 O  O   . HOH   E .   ? 0.1996 0.3362 0.5976 0.0208  -0.0790 0.0436  471 HOH   A O   
2175 O  O   . HOH   E .   ? 0.6541 0.3937 0.4888 -0.2882 0.0728  -0.1177 472 HOH   A O   
2176 O  O   . HOH   E .   ? 0.2347 0.5457 0.5447 -0.0422 -0.1210 0.0688  473 HOH   A O   
2177 O  O   . HOH   E .   ? 0.1030 0.1208 0.2937 0.0006  -0.0055 -0.0149 474 HOH   A O   
2178 O  O   . HOH   E .   ? 0.2528 0.3078 0.4398 0.0222  0.0397  0.0776  475 HOH   A O   
2179 O  O   . HOH   E .   ? 0.3238 0.2323 0.4560 -0.0359 -0.0372 0.0446  476 HOH   A O   
2180 O  O   . HOH   E .   ? 0.3535 0.1518 0.4301 0.0622  -0.1168 -0.0471 477 HOH   A O   
2181 O  O   . HOH   E .   ? 0.3966 0.5483 0.5146 -0.0691 -0.1235 0.1725  478 HOH   A O   
2182 O  O   . HOH   E .   ? 0.3051 0.3654 0.4621 -0.0912 -0.0966 0.0537  479 HOH   A O   
2183 O  O   . HOH   E .   ? 0.5209 0.1709 0.6150 -0.1069 -0.0208 0.1070  480 HOH   A O   
2184 O  O   . HOH   E .   ? 0.2011 0.1736 0.3631 -0.0150 -0.0842 0.0215  481 HOH   A O   
2185 O  O   . HOH   E .   ? 0.2947 0.1779 0.4310 0.0534  0.0211  0.0472  482 HOH   A O   
2186 O  O   . HOH   E .   ? 0.5066 0.3432 0.8241 -0.1566 0.1521  -0.1036 483 HOH   A O   
2187 O  O   . HOH   E .   ? 0.5890 0.2599 0.5761 -0.0513 -0.0889 -0.0133 484 HOH   A O   
2188 O  O   . HOH   E .   ? 0.3787 0.3126 0.3441 -0.0628 -0.0541 -0.0006 485 HOH   A O   
2189 O  O   . HOH   E .   ? 0.2929 0.1942 0.3289 -0.0011 0.0012  -0.0488 486 HOH   A O   
2190 O  O   . HOH   E .   ? 0.2172 0.1562 0.3252 0.0109  0.0127  -0.0035 487 HOH   A O   
2191 O  O   . HOH   E .   ? 0.2575 0.2323 0.2999 0.0290  0.0334  -0.0644 488 HOH   A O   
2192 O  O   . HOH   E .   ? 0.3057 0.4864 0.5400 0.1261  -0.0206 -0.0791 489 HOH   A O   
2193 O  O   . HOH   E .   ? 0.5015 0.4536 0.8523 -0.1331 -0.1079 -0.1655 490 HOH   A O   
2194 O  O   . HOH   E .   ? 0.3017 0.3880 0.7789 -0.1012 -0.0752 -0.0052 491 HOH   A O   
2195 O  O   . HOH   E .   ? 0.2859 0.3737 0.6269 -0.0772 -0.1860 0.0277  492 HOH   A O   
2196 O  O   . HOH   E .   ? 0.1102 0.1465 0.2696 0.0223  -0.0187 -0.0078 493 HOH   A O   
2197 O  O   . HOH   E .   ? 0.2186 0.7619 0.4449 0.0491  -0.0883 -0.2590 494 HOH   A O   
2198 O  O   . HOH   E .   ? 0.2545 0.1750 0.3273 0.0025  -0.0703 0.0252  495 HOH   A O   
2199 O  O   . HOH   E .   ? 0.3991 0.5297 0.2877 -0.0004 -0.0290 0.0655  496 HOH   A O   
2200 O  O   . HOH   E .   ? 0.1989 0.2043 0.4249 0.0316  -0.0087 -0.0193 497 HOH   A O   
2201 O  O   . HOH   E .   ? 0.2881 0.1942 0.4226 -0.0510 0.0269  0.0094  498 HOH   A O   
2202 O  O   . HOH   E .   ? 0.6269 0.4546 0.5796 0.0685  -0.1793 -0.0097 499 HOH   A O   
2203 O  O   . HOH   E .   ? 0.2741 0.4411 0.3352 -0.0292 -0.0809 0.1076  500 HOH   A O   
2204 O  O   . HOH   E .   ? 0.1885 0.1698 0.4307 -0.0138 -0.0355 0.0241  501 HOH   A O   
2205 O  O   . HOH   E .   ? 0.1716 0.6452 0.5511 0.0232  -0.0504 0.0498  502 HOH   A O   
2206 O  O   . HOH   E .   ? 0.1612 0.2920 0.2757 -0.0084 -0.0283 0.0100  503 HOH   A O   
2207 O  O   . HOH   E .   ? 0.4221 0.3740 0.3643 0.0763  -0.0379 -0.0044 504 HOH   A O   
2208 O  O   . HOH   E .   ? 0.2053 0.2133 0.4040 0.0047  -0.0181 -0.0078 505 HOH   A O   
2209 O  O   . HOH   E .   ? 0.2756 0.2492 0.5194 -0.0532 -0.0502 0.0000  506 HOH   A O   
2210 O  O   . HOH   E .   ? 0.2176 0.1360 0.3504 0.0335  -0.0276 -0.0111 507 HOH   A O   
2211 O  O   . HOH   E .   ? 0.2240 0.2445 0.4913 0.0566  0.0516  -0.0298 508 HOH   A O   
2212 O  O   . HOH   E .   ? 0.3374 0.3436 0.5198 -0.0707 -0.0859 -0.0500 509 HOH   A O   
2213 O  O   . HOH   E .   ? 0.6700 0.3229 0.6154 0.2302  -0.2532 0.0385  510 HOH   A O   
2214 O  O   . HOH   E .   ? 0.5419 0.1813 0.5441 0.0806  -0.0096 0.0247  511 HOH   A O   
2215 O  O   . HOH   E .   ? 0.4066 0.3182 0.7426 0.1239  -0.1280 0.0232  512 HOH   A O   
2216 O  O   . HOH   E .   ? 0.3206 0.3235 0.3933 0.1363  -0.0358 -0.0450 513 HOH   A O   
2217 O  O   . HOH   E .   ? 0.2406 0.1964 0.2618 0.0375  0.0025  -0.0270 514 HOH   A O   
2218 O  O   . HOH   E .   ? 0.2469 0.2118 0.2766 -0.0071 -0.0164 -0.0082 515 HOH   A O   
2219 O  O   . HOH   E .   ? 0.2764 0.5579 0.7889 0.1405  0.1743  0.0890  516 HOH   A O   
2220 O  O   . HOH   E .   ? 0.3646 0.5838 0.4637 0.1427  -0.0240 0.1097  517 HOH   A O   
2221 O  O   . HOH   E .   ? 0.2973 0.1700 0.3369 -0.0280 -0.0161 0.0107  518 HOH   A O   
2222 O  O   . HOH   E .   ? 0.3387 0.2335 0.4481 -0.1142 0.0405  -0.0546 519 HOH   A O   
2223 O  O   . HOH   E .   ? 0.3350 0.1244 0.4174 -0.0583 -0.0872 -0.0248 520 HOH   A O   
2224 O  O   . HOH   E .   ? 0.3609 0.2488 0.7516 0.0284  -0.1082 -0.0451 521 HOH   A O   
2225 O  O   . HOH   E .   ? 0.1464 0.1766 0.3677 0.0020  -0.0285 -0.0136 522 HOH   A O   
2226 O  O   . HOH   E .   ? 0.1632 0.2077 0.3289 0.0139  -0.0271 -0.0143 523 HOH   A O   
2227 O  O   . HOH   E .   ? 0.1170 0.2189 0.3218 -0.0170 -0.0274 -0.0381 524 HOH   A O   
2228 O  O   . HOH   E .   ? 0.4196 0.7390 0.5779 0.2645  0.0573  0.1857  525 HOH   A O   
2229 O  O   . HOH   E .   ? 0.3745 0.1878 0.4955 0.0982  -0.1323 0.0322  526 HOH   A O   
2230 O  O   . HOH   E .   ? 0.1192 0.1452 0.2460 -0.0047 -0.0435 -0.0173 527 HOH   A O   
2231 O  O   . HOH   E .   ? 0.4643 0.3303 0.4268 0.0182  0.0666  -0.1000 528 HOH   A O   
2232 O  O   . HOH   E .   ? 0.2628 0.2082 0.4613 -0.0662 -0.1043 0.0361  529 HOH   A O   
2233 O  O   . HOH   E .   ? 0.3064 0.2587 0.3794 -0.0055 0.0058  0.0291  530 HOH   A O   
2234 O  O   . HOH   E .   ? 0.2247 0.4023 0.3247 0.0754  -0.0610 -0.0187 531 HOH   A O   
2235 O  O   . HOH   E .   ? 0.1723 0.4426 0.4184 -0.0760 -0.0569 -0.0061 532 HOH   A O   
2236 O  O   . HOH   E .   ? 0.2355 0.3180 0.4874 -0.0198 0.0403  0.0409  533 HOH   A O   
2237 O  O   . HOH   E .   ? 0.2716 0.2027 0.3204 0.0587  -0.0568 -0.0214 534 HOH   A O   
2238 O  O   . HOH   E .   ? 0.4103 0.5044 0.4130 0.1106  -0.0414 -0.0220 535 HOH   A O   
2239 O  O   . HOH   E .   ? 0.6334 0.2501 0.3679 0.0815  -0.0057 0.0252  536 HOH   A O   
2240 O  O   . HOH   E .   ? 0.5520 0.3595 0.5431 -0.2098 -0.1857 -0.0278 537 HOH   A O   
2241 O  O   . HOH   E .   ? 0.1289 0.2424 0.2832 0.0357  -0.0242 0.0133  538 HOH   A O   
2242 O  O   . HOH   E .   ? 0.3571 0.3353 0.4560 -0.1227 -0.0653 0.1200  539 HOH   A O   
2243 O  O   . HOH   E .   ? 0.2243 0.2143 0.2742 -0.0456 -0.0086 0.0157  540 HOH   A O   
2244 O  O   . HOH   E .   ? 0.2278 0.2537 0.3393 -0.0223 -0.0414 -0.0380 541 HOH   A O   
2245 O  O   . HOH   E .   ? 0.1192 0.2111 0.2868 0.0006  -0.0541 0.0194  542 HOH   A O   
2246 O  O   . HOH   E .   ? 0.3977 0.5307 0.4328 -0.0947 0.0712  -0.1449 543 HOH   A O   
2247 O  O   . HOH   E .   ? 0.3785 0.3164 0.4070 0.1917  -0.0477 0.0476  544 HOH   A O   
2248 O  O   . HOH   E .   ? 0.2463 0.5315 0.4619 0.0031  0.0138  0.0399  545 HOH   A O   
2249 O  O   . HOH   E .   ? 0.1317 0.1524 0.2861 0.0144  -0.0546 0.0301  546 HOH   A O   
2250 O  O   . HOH   E .   ? 0.2014 0.6590 0.3882 0.0849  0.0551  0.1919  547 HOH   A O   
2251 O  O   . HOH   E .   ? 0.3630 0.4746 0.5270 0.1645  -0.0435 -0.0160 548 HOH   A O   
2252 O  O   . HOH   E .   ? 0.5977 0.4004 0.5280 0.2633  0.1095  0.1975  549 HOH   A O   
2253 O  O   . HOH   E .   ? 0.7562 0.2804 0.8440 0.2086  -0.4381 -0.1081 550 HOH   A O   
2254 O  O   . HOH   E .   ? 0.1838 0.1504 0.2976 0.0053  -0.0230 0.0058  551 HOH   A O   
2255 O  O   . HOH   E .   ? 0.2187 0.4495 0.5468 -0.0389 -0.1182 0.0908  552 HOH   A O   
2256 O  O   . HOH   E .   ? 0.4209 0.3323 0.4432 -0.1186 0.1342  -0.0421 553 HOH   A O   
2257 O  O   . HOH   E .   ? 0.3333 0.2077 0.2688 -0.0073 -0.0274 -0.0147 554 HOH   A O   
2258 O  O   . HOH   E .   ? 0.2301 0.1962 0.3601 -0.0139 -0.0052 -0.0218 555 HOH   A O   
2259 O  O   . HOH   E .   ? 0.3612 0.4419 0.4002 0.0773  0.0475  -0.0836 556 HOH   A O   
2260 O  O   . HOH   E .   ? 0.2637 0.1619 0.3226 0.0337  -0.0429 -0.0134 557 HOH   A O   
2261 O  O   . HOH   E .   ? 0.2615 0.2172 0.3130 -0.0111 -0.0104 0.0493  558 HOH   A O   
2262 O  O   . HOH   E .   ? 0.2576 0.3228 0.4968 0.0359  0.0519  -0.0674 559 HOH   A O   
2263 O  O   . HOH   E .   ? 0.3940 0.2111 0.3427 0.1512  -0.0093 -0.0474 560 HOH   A O   
2264 O  O   . HOH   E .   ? 0.3632 0.3996 0.4512 -0.0244 -0.0657 0.0064  561 HOH   A O   
2265 O  O   . HOH   E .   ? 0.1648 0.3359 0.3970 0.0531  -0.0479 -0.0013 562 HOH   A O   
2266 O  O   . HOH   E .   ? 0.2014 0.8442 0.5899 -0.1192 0.0019  -0.0183 563 HOH   A O   
2267 O  O   . HOH   E .   ? 0.3389 0.2734 0.4875 0.0399  0.0930  0.0171  564 HOH   A O   
2268 O  O   . HOH   E .   ? 0.2269 0.3006 0.4785 -0.0051 0.0010  0.0956  565 HOH   A O   
2269 O  O   . HOH   E .   ? 0.3740 0.2287 0.5337 0.0334  -0.1511 -0.0473 566 HOH   A O   
2270 O  O   . HOH   E .   ? 0.1874 0.1536 0.3990 -0.0964 -0.0301 -0.0378 567 HOH   A O   
2271 O  O   . HOH   E .   ? 0.2515 0.3357 0.2965 -0.1400 -0.0493 -0.0074 568 HOH   A O   
2272 O  O   . HOH   E .   ? 0.5995 0.3376 0.3989 0.0077  -0.0833 0.0209  569 HOH   A O   
2273 O  O   . HOH   E .   ? 0.4394 0.4117 0.4514 -0.0212 -0.0647 -0.0385 570 HOH   A O   
2274 O  O   . HOH   E .   ? 0.4821 0.1477 0.4018 -0.1251 -0.0310 -0.0604 571 HOH   A O   
2275 O  O   . HOH   E .   ? 0.1600 0.2574 0.2651 -0.0311 -0.1028 0.0399  572 HOH   A O   
2276 O  O   . HOH   E .   ? 0.6287 0.3140 0.4994 -0.1002 -0.0194 -0.0324 573 HOH   A O   
2277 O  O   . HOH   E .   ? 0.2481 0.2592 0.3618 -0.0182 -0.0751 0.0145  574 HOH   A O   
2278 O  O   . HOH   E .   ? 0.2109 0.3691 0.4203 -0.0554 -0.0817 0.0509  575 HOH   A O   
2279 O  O   . HOH   E .   ? 0.6819 0.2427 0.4280 0.0352  -0.1289 -0.0408 576 HOH   A O   
2280 O  O   . HOH   E .   ? 0.5747 0.3814 0.4038 0.0493  -0.1029 -0.0704 577 HOH   A O   
2281 O  O   . HOH   E .   ? 0.3272 0.3082 0.3591 -0.0483 0.0176  0.0087  578 HOH   A O   
2282 O  O   . HOH   E .   ? 0.6821 0.6649 0.3321 0.0013  -0.1237 -0.0956 579 HOH   A O   
2283 O  O   . HOH   E .   ? 0.3907 0.4339 0.3832 -0.0258 -0.0162 -0.1162 580 HOH   A O   
2284 O  O   . HOH   E .   ? 0.2196 0.2635 0.3845 0.0148  -0.0155 -0.0351 581 HOH   A O   
2285 O  O   . HOH   E .   ? 0.3330 0.6283 0.5249 0.1516  0.0013  0.2606  582 HOH   A O   
2286 O  O   . HOH   E .   ? 0.3710 0.2201 0.6828 -0.0398 -0.0350 -0.1606 583 HOH   A O   
2287 O  O   . HOH   E .   ? 0.3222 0.1894 0.3971 0.0604  -0.0038 -0.0320 584 HOH   A O   
2288 O  O   . HOH   E .   ? 0.3835 0.2222 0.4506 -0.0134 0.1327  0.0354  585 HOH   A O   
2289 O  O   . HOH   E .   ? 0.3556 0.2093 0.3604 0.0248  -0.0083 -0.0100 586 HOH   A O   
2290 O  O   . HOH   E .   ? 0.4331 0.2961 0.4095 -0.0734 -0.0798 0.1051  587 HOH   A O   
2291 O  O   . HOH   E .   ? 0.3227 0.3522 0.3404 -0.0192 -0.0319 0.0326  588 HOH   A O   
2292 O  O   . HOH   E .   ? 0.3114 0.4134 0.4277 -0.0438 -0.0422 -0.0264 589 HOH   A O   
2293 O  O   . HOH   E .   ? 0.4562 0.4450 0.4878 0.0282  -0.1371 -0.1207 590 HOH   A O   
2294 O  O   . HOH   E .   ? 0.3080 0.1687 0.4060 -0.0453 -0.1427 -0.0106 591 HOH   A O   
2295 O  O   . HOH   E .   ? 0.3386 0.7020 0.5848 -0.0578 0.1188  0.1233  592 HOH   A O   
2296 O  O   . HOH   E .   ? 0.6549 0.2586 1.1327 -0.0732 -0.0719 -0.0527 593 HOH   A O   
2297 O  O   . HOH   E .   ? 0.2330 0.2929 0.4833 0.0002  0.0229  -0.0693 594 HOH   A O   
2298 O  O   . HOH   E .   ? 0.4996 0.4945 0.7113 -0.0370 -0.2724 0.0726  595 HOH   A O   
2299 O  O   . HOH   E .   ? 0.5443 0.3406 0.4200 -0.1230 -0.0035 0.0907  596 HOH   A O   
2300 O  O   . HOH   E .   ? 0.3094 0.2454 0.5503 0.0602  0.0062  -0.0876 597 HOH   A O   
2301 O  O   . HOH   E .   ? 0.1705 0.2587 0.3926 0.0395  -0.1085 -0.0596 598 HOH   A O   
2302 O  O   . HOH   E .   ? 0.3184 0.4053 0.7343 0.0639  0.1221  -0.0455 599 HOH   A O   
2303 O  O   . HOH   E .   ? 0.2924 0.1180 0.3825 0.0527  -0.0209 -0.0179 600 HOH   A O   
2304 O  O   . HOH   E .   ? 0.3747 0.7840 0.4616 -0.1425 -0.0096 -0.1928 601 HOH   A O   
2305 O  O   . HOH   E .   ? 0.4607 0.4014 0.6027 -0.0408 -0.1621 0.0432  602 HOH   A O   
2306 O  O   . HOH   E .   ? 0.2810 0.5752 0.5554 0.2160  -0.1009 -0.0618 603 HOH   A O   
2307 O  O   . HOH   E .   ? 0.4666 0.3735 0.3607 0.0542  0.0111  0.0856  604 HOH   A O   
2308 O  O   . HOH   E .   ? 0.2713 0.3295 0.7165 -0.1494 0.0049  0.0477  605 HOH   A O   
2309 O  O   . HOH   E .   ? 0.2995 0.2036 0.3669 0.0508  -0.0756 0.0568  606 HOH   A O   
2310 O  O   . HOH   E .   ? 0.2078 0.1898 0.4706 0.0685  0.0156  -0.0296 607 HOH   A O   
2311 O  O   . HOH   E .   ? 0.1644 0.1127 0.3137 0.0209  -0.0170 0.0120  608 HOH   A O   
2312 O  O   . HOH   E .   ? 0.2086 0.2610 0.3068 0.0497  -0.0168 -0.0129 609 HOH   A O   
2313 O  O   . HOH   E .   ? 0.3996 0.2587 0.4320 -0.0387 -0.0195 -0.0464 610 HOH   A O   
2314 O  O   . HOH   E .   ? 0.3964 0.2504 0.4914 0.0754  0.0040  -0.0187 611 HOH   A O   
2315 O  O   . HOH   E .   ? 0.5754 0.3297 0.4728 -0.0089 0.2011  -0.0174 612 HOH   A O   
2316 O  O   . HOH   E .   ? 0.4571 0.2562 0.3389 0.0230  -0.0478 0.0879  613 HOH   A O   
2317 O  O   . HOH   E .   ? 0.3737 0.3320 0.3494 -0.0675 -0.0960 0.0083  614 HOH   A O   
2318 O  O   . HOH   E .   ? 0.2605 0.1456 0.5154 0.1071  -0.0376 0.0204  615 HOH   A O   
2319 O  O   . HOH   E .   ? 0.6979 0.4657 0.5065 -0.2327 0.0901  -0.0806 616 HOH   A O   
2320 O  O   . HOH   E .   ? 0.5161 0.2554 0.4239 0.1229  -0.0945 -0.0595 617 HOH   A O   
2321 O  O   . HOH   E .   ? 0.4827 0.1500 0.4054 0.0366  -0.0096 0.0601  618 HOH   A O   
2322 O  O   . HOH   E .   ? 0.4154 0.4139 0.2530 0.0017  -0.0472 -0.0118 619 HOH   A O   
2323 O  O   . HOH   E .   ? 0.3455 0.2046 0.4052 0.0849  0.0734  0.0633  620 HOH   A O   
2324 O  O   . HOH   E .   ? 0.2564 0.5643 0.3397 0.0175  0.0057  0.1327  621 HOH   A O   
2325 O  O   . HOH   E .   ? 0.3867 0.5184 0.5001 -0.1802 -0.0968 0.0183  622 HOH   A O   
2326 O  O   . HOH   E .   ? 0.6208 0.4402 0.5067 -0.3930 0.1364  -0.1794 623 HOH   A O   
2327 O  O   . HOH   E .   ? 0.4139 0.3131 0.5771 0.0070  -0.0277 0.0032  624 HOH   A O   
2328 O  O   . HOH   E .   ? 0.2828 0.4869 0.4533 0.1342  0.0242  0.1785  625 HOH   A O   
2329 O  O   . HOH   E .   ? 0.4621 0.3373 0.2743 0.1986  -0.0622 0.0015  626 HOH   A O   
2330 O  O   . HOH   E .   ? 0.4493 0.4021 0.3516 0.0242  -0.1967 -0.0106 627 HOH   A O   
2331 O  O   . HOH   E .   ? 0.2875 0.3235 0.4131 0.0790  0.0029  0.0560  628 HOH   A O   
2332 O  O   . HOH   E .   ? 0.3658 0.4948 0.6200 0.1113  -0.0841 -0.0279 629 HOH   A O   
2333 O  O   . HOH   E .   ? 0.7801 0.4655 0.5841 -0.0452 0.1643  0.1729  630 HOH   A O   
2334 O  O   . HOH   E .   ? 0.1263 0.2122 0.3389 0.0084  -0.0276 -0.0219 631 HOH   A O   
2335 O  O   . HOH   E .   ? 0.4182 0.3908 0.5330 0.0022  -0.0559 0.0263  632 HOH   A O   
2336 O  O   . HOH   E .   ? 0.5074 0.5005 0.5679 -0.0565 0.0089  -0.2148 633 HOH   A O   
2337 O  O   . HOH   E .   ? 0.1953 0.3761 0.6792 -0.0539 -0.0873 -0.0160 634 HOH   A O   
2338 O  O   . HOH   E .   ? 0.4841 0.4489 0.6003 -0.0567 0.0810  0.0083  635 HOH   A O   
2339 O  O   . HOH   E .   ? 0.2710 0.8507 0.5005 -0.1987 -0.0381 -0.1999 636 HOH   A O   
2340 O  O   . HOH   E .   ? 0.3543 0.4009 0.7180 0.1185  -0.0292 -0.0004 637 HOH   A O   
2341 O  O   . HOH   E .   ? 0.4291 0.4581 0.4692 0.0038  0.0870  -0.0173 638 HOH   A O   
2342 O  O   . HOH   E .   ? 0.3688 0.4738 0.5902 0.0807  0.1332  0.1152  639 HOH   A O   
2343 O  O   . HOH   E .   ? 0.5965 0.3210 0.5589 0.2132  -0.0749 0.0174  640 HOH   A O   
2344 O  O   . HOH   E .   ? 0.5773 0.2739 0.4649 0.0639  -0.0662 0.0254  641 HOH   A O   
2345 O  O   . HOH   E .   ? 0.3910 0.4255 0.7095 -0.1185 -0.1198 -0.0929 642 HOH   A O   
2346 O  O   . HOH   E .   ? 0.2021 0.6707 0.3516 0.0986  -0.0240 0.0937  643 HOH   A O   
2347 O  O   . HOH   E .   ? 0.7580 0.7917 0.3016 0.0824  -0.0556 -0.1311 644 HOH   A O   
2348 O  O   . HOH   E .   ? 0.2821 0.3113 0.8907 -0.0483 0.0063  -0.1557 645 HOH   A O   
2349 O  O   . HOH   E .   ? 0.5690 0.4079 0.6414 -0.1979 -0.3617 0.0983  646 HOH   A O   
2350 O  O   . HOH   E .   ? 0.2244 0.1188 0.2689 0.0104  -0.0313 0.0032  647 HOH   A O   
2351 O  O   . HOH   E .   ? 0.3334 0.4074 0.4509 0.1286  -0.1132 -0.1076 648 HOH   A O   
2352 O  O   . HOH   E .   ? 0.4266 0.7296 1.2307 0.2790  0.2989  0.3335  649 HOH   A O   
2353 O  O   . HOH   E .   ? 0.7195 0.2256 0.6495 0.0769  0.3136  0.0655  650 HOH   A O   
2354 O  O   . HOH   E .   ? 0.1921 0.4585 0.8452 0.0063  -0.0324 -0.3677 651 HOH   A O   
2355 O  O   . HOH   E .   ? 0.4515 0.2520 0.6301 0.0725  0.1289  -0.0570 652 HOH   A O   
2356 O  O   . HOH   E .   ? 0.6018 0.7109 0.4674 0.1916  -0.3404 -0.0825 653 HOH   A O   
2357 O  O   . HOH   E .   ? 0.2346 0.2754 0.3940 0.0158  -0.0687 0.0099  654 HOH   A O   
2358 O  O   . HOH   E .   ? 0.2740 0.3417 0.6718 0.0372  -0.1298 -0.0188 655 HOH   A O   
2359 O  O   . HOH   E .   ? 0.4918 0.5158 0.3855 0.0121  0.0092  -0.0134 656 HOH   A O   
2360 O  O   . HOH   E .   ? 0.6687 0.3587 0.6394 0.0587  0.2534  0.0059  657 HOH   A O   
2361 O  O   . HOH   E .   ? 0.3283 0.3908 0.9394 -0.0646 0.0217  -0.0502 658 HOH   A O   
2362 O  O   . HOH   E .   ? 0.7354 0.2408 0.8503 -0.2348 0.0204  0.0170  659 HOH   A O   
2363 O  O   . HOH   E .   ? 0.3685 0.4359 0.5837 0.0319  -0.0362 0.1215  660 HOH   A O   
2364 O  O   . HOH   E .   ? 0.3032 0.3978 0.4535 0.0463  -0.0110 0.0215  661 HOH   A O   
2365 O  O   . HOH   E .   ? 0.3540 0.3981 0.8647 0.0958  0.1750  0.0154  662 HOH   A O   
2366 O  O   . HOH   E .   ? 0.7016 0.3735 0.7468 -0.0380 -0.1514 0.1655  663 HOH   A O   
2367 O  O   . HOH   E .   ? 0.4107 0.5572 0.3389 0.1000  -0.0335 0.1018  664 HOH   A O   
2368 O  O   . HOH   E .   ? 0.4590 0.8282 0.4189 0.2032  0.0373  0.0602  665 HOH   A O   
2369 O  O   . HOH   E .   ? 0.3928 0.5058 0.6009 0.0680  -0.0436 0.2428  666 HOH   A O   
2370 O  O   . HOH   E .   ? 0.2057 0.8126 0.7637 -0.0859 -0.1763 0.0334  667 HOH   A O   
2371 O  O   . HOH   E .   ? 0.7519 0.3797 0.4518 -0.1918 0.0363  0.0416  668 HOH   A O   
2372 O  O   . HOH   E .   ? 0.3998 0.3823 0.4664 0.0652  0.1060  0.0312  669 HOH   A O   
2373 O  O   . HOH   E .   ? 0.7736 0.5633 0.3376 0.0106  -0.0555 -0.0590 670 HOH   A O   
2374 O  O   . HOH   E .   ? 0.2786 0.3579 0.3856 -0.0055 -0.0282 -0.0754 671 HOH   A O   
2375 O  O   . HOH   E .   ? 0.3680 0.3057 0.5897 0.0233  0.0376  -0.0201 672 HOH   A O   
2376 O  O   . HOH   E .   ? 0.4747 0.3574 0.5113 0.0664  0.1584  0.0800  673 HOH   A O   
2377 O  O   . HOH   E .   ? 0.2682 0.5920 0.6203 -0.0675 0.0293  0.0232  674 HOH   A O   
2378 O  O   . HOH   E .   ? 0.2711 1.0261 0.4642 0.0484  0.0377  0.0670  675 HOH   A O   
2379 O  O   . HOH   E .   ? 0.3994 0.4936 0.7160 -0.0093 0.0725  -0.2329 676 HOH   A O   
2380 O  O   . HOH   E .   ? 0.4431 0.4897 0.6523 0.0499  0.0795  0.0570  677 HOH   A O   
2381 O  O   . HOH   E .   ? 0.4928 0.2858 0.3956 -0.0105 -0.0357 -0.0773 678 HOH   A O   
2382 O  O   . HOH   E .   ? 0.4384 0.2536 0.6668 0.0341  -0.1637 -0.0217 679 HOH   A O   
2383 O  O   . HOH   E .   ? 0.3190 0.2894 0.4697 -0.0442 -0.0301 -0.0295 680 HOH   A O   
2384 O  O   . HOH   E .   ? 0.3137 0.2914 0.3968 0.0370  -0.1979 0.0054  681 HOH   A O   
2385 O  O   . HOH   E .   ? 0.6294 0.3628 0.5794 0.0516  0.1544  -0.1740 682 HOH   A O   
2386 O  O   . HOH   E .   ? 0.3881 0.4438 0.7618 -0.0533 0.0871  0.1522  683 HOH   A O   
2387 O  O   . HOH   E .   ? 0.2900 0.4266 0.3890 -0.1097 -0.0215 -0.0383 684 HOH   A O   
2388 O  O   . HOH   E .   ? 0.3572 0.5708 0.3495 0.0176  -0.0091 0.0823  685 HOH   A O   
2389 O  O   . HOH   E .   ? 0.2532 0.3811 0.3528 0.0185  -0.0210 0.0399  686 HOH   A O   
2390 O  O   . HOH   E .   ? 0.5305 0.4532 0.5492 0.0487  -0.0708 -0.0914 687 HOH   A O   
2391 O  O   . HOH   E .   ? 0.4029 0.3988 0.3958 0.1444  -0.0424 0.0182  688 HOH   A O   
2392 O  O   . HOH   E .   ? 0.5043 0.3531 0.6427 -0.0632 -0.0994 0.0337  689 HOH   A O   
2393 O  O   . HOH   E .   ? 0.4262 0.4424 0.6049 0.0793  0.1430  0.1805  690 HOH   A O   
2394 O  O   . HOH   E .   ? 0.3589 0.3881 0.3306 0.0973  -0.0230 -0.0074 691 HOH   A O   
2395 O  O   . HOH   E .   ? 0.3794 0.7062 0.4783 0.0555  -0.0771 0.0673  692 HOH   A O   
2396 O  O   . HOH   E .   ? 0.7115 0.4156 0.4038 0.0280  -0.2077 -0.0093 693 HOH   A O   
2397 O  O   . HOH   E .   ? 0.3087 0.3689 0.6740 -0.0019 -0.0267 0.0285  694 HOH   A O   
2398 O  O   . HOH   E .   ? 0.5058 0.4394 0.7924 -0.0483 0.2104  0.1655  695 HOH   A O   
2399 O  O   . HOH   E .   ? 0.2772 0.3012 0.4398 0.0379  -0.0424 0.0389  696 HOH   A O   
2400 O  O   . HOH   E .   ? 0.5513 0.4420 0.5723 0.0368  0.0425  0.1878  697 HOH   A O   
2401 O  O   . HOH   E .   ? 0.3751 0.3050 0.5273 0.0446  0.0584  0.0599  698 HOH   A O   
2402 O  O   . HOH   E .   ? 0.2710 0.2870 0.3617 -0.0375 -0.0274 0.0633  699 HOH   A O   
2403 O  O   . HOH   E .   ? 0.4067 0.5302 0.5005 -0.0966 -0.0886 0.0414  700 HOH   A O   
2404 O  O   . HOH   E .   ? 0.6552 0.2551 0.5477 0.0798  -0.1433 -0.0523 701 HOH   A O   
2405 O  O   . HOH   E .   ? 0.2143 0.3458 0.5172 -0.0372 -0.0485 -0.0723 702 HOH   A O   
2406 O  O   . HOH   E .   ? 0.3728 0.3780 0.7569 -0.1499 -0.2447 0.1238  703 HOH   A O   
2407 O  O   . HOH   E .   ? 0.2294 0.5310 0.4016 0.0862  -0.0122 0.0863  704 HOH   A O   
2408 O  O   . HOH   E .   ? 0.3470 0.3672 0.4249 0.0911  -0.1029 0.0097  705 HOH   A O   
2409 O  O   . HOH   E .   ? 0.5022 0.2426 0.9498 0.1111  -0.0885 0.0348  706 HOH   A O   
2410 O  O   . HOH   E .   ? 0.6226 0.2480 0.4083 0.0600  -0.0915 -0.0315 707 HOH   A O   
2411 O  O   . HOH   E .   ? 0.5922 0.5316 0.4469 0.1789  -0.0221 -0.0510 708 HOH   A O   
2412 O  O   . HOH   E .   ? 0.5258 0.2570 0.5763 0.0663  0.0149  -0.0469 709 HOH   A O   
2413 O  O   . HOH   E .   ? 0.4404 0.6727 0.5335 -0.1222 -0.0158 -0.2543 710 HOH   A O   
2414 O  O   . HOH   E .   ? 0.4716 0.2450 0.7461 -0.0560 -0.1175 0.0563  711 HOH   A O   
2415 O  O   . HOH   E .   ? 0.4745 0.3806 0.4320 -0.0370 -0.0162 -0.0748 712 HOH   A O   
2416 O  O   . HOH   E .   ? 0.4729 0.3772 0.6038 -0.1913 0.1389  -0.0760 713 HOH   A O   
2417 O  O   . HOH   E .   ? 0.2708 0.5429 0.4697 -0.0859 -0.0691 0.0223  714 HOH   A O   
2418 O  O   . HOH   E .   ? 0.3406 0.1669 0.5405 0.0111  0.0575  -0.0059 715 HOH   A O   
2419 O  O   . HOH   E .   ? 0.6052 0.4417 0.5352 0.0884  -0.1920 -0.2757 716 HOH   A O   
2420 O  O   . HOH   E .   ? 0.5982 0.4910 0.5445 0.0560  -0.2603 -0.1193 717 HOH   A O   
2421 O  O   . HOH   E .   ? 0.1849 0.2949 0.3058 0.0044  -0.0043 -0.0357 718 HOH   A O   
2422 O  O   . HOH   E .   ? 0.3150 0.4149 0.6516 0.0609  0.0099  0.2151  719 HOH   A O   
2423 O  O   . HOH   E .   ? 0.4473 0.5381 0.4973 0.0244  -0.0482 0.0013  720 HOH   A O   
2424 O  O   . HOH   E .   ? 0.2940 0.3950 0.4880 0.1265  -0.0502 0.0292  721 HOH   A O   
2425 O  O   . HOH   E .   ? 0.2481 0.2643 0.3005 0.0524  -0.0756 0.0361  722 HOH   A O   
2426 O  O   . HOH   E .   ? 0.6312 0.4027 0.7091 -0.0142 0.0036  0.1224  723 HOH   A O   
2427 O  O   . HOH   E .   ? 0.4434 0.2714 0.5860 -0.1493 -0.0355 0.1232  724 HOH   A O   
2428 O  O   . HOH   E .   ? 0.7960 0.2442 0.4632 -0.0978 0.0034  0.0245  725 HOH   A O   
2429 O  O   . HOH   E .   ? 0.5619 0.4165 0.5037 -0.1297 -0.0315 0.0545  726 HOH   A O   
2430 O  O   . HOH   E .   ? 0.3631 0.2940 0.6463 0.0337  0.0946  0.0545  727 HOH   A O   
2431 O  O   . HOH   E .   ? 0.5662 1.0798 0.6223 0.5235  0.3050  0.5131  728 HOH   A O   
2432 O  O   . HOH   E .   ? 0.3808 0.3452 0.3708 0.0363  0.0075  -0.0116 729 HOH   A O   
2433 O  O   . HOH   E .   ? 0.3358 0.3176 0.6971 0.0538  -0.0210 0.1230  730 HOH   A O   
2434 O  O   . HOH   E .   ? 0.1529 0.6850 0.7138 -0.0475 -0.0574 -0.1489 731 HOH   A O   
2435 O  O   . HOH   E .   ? 0.4409 0.4205 0.4004 -0.0165 0.0075  0.0952  732 HOH   A O   
2436 O  O   . HOH   E .   ? 0.3378 0.4439 0.7429 -0.1928 -0.2059 0.0000  733 HOH   A O   
2437 O  O   . HOH   E .   ? 0.4045 0.2820 0.5802 -0.0639 -0.0556 -0.0036 734 HOH   A O   
2438 O  O   . HOH   E .   ? 0.4523 0.6384 0.5373 0.1967  -0.0508 0.0219  735 HOH   A O   
2439 O  O   . HOH   E .   ? 0.5417 0.3935 0.6760 0.0291  0.1318  0.1252  736 HOH   A O   
2440 O  O   . HOH   E .   ? 0.3473 0.7174 0.4957 0.0361  0.1497  0.1357  737 HOH   A O   
2441 O  O   . HOH   E .   ? 0.6728 0.2460 0.6592 -0.1951 0.0006  0.0666  738 HOH   A O   
2442 O  O   . HOH   E .   ? 0.2830 0.4745 0.4322 -0.1401 -0.0178 0.0768  739 HOH   A O   
2443 O  O   . HOH   E .   ? 0.3708 0.2045 0.5756 0.0040  0.0391  0.0098  740 HOH   A O   
2444 O  O   . HOH   E .   ? 0.6565 0.2762 0.3621 0.1780  -0.0226 0.0303  741 HOH   A O   
2445 O  O   . HOH   E .   ? 0.4492 0.3884 0.5407 0.0458  0.1025  -0.0001 742 HOH   A O   
2446 O  O   . HOH   E .   ? 0.1960 0.2944 0.6169 -0.0283 -0.0834 -0.1446 743 HOH   A O   
2447 O  O   . HOH   E .   ? 0.2118 0.6293 0.7197 0.0386  0.0619  0.0038  744 HOH   A O   
2448 O  O   . HOH   E .   ? 0.1993 0.4708 0.6099 0.0354  0.0174  0.0982  745 HOH   A O   
2449 O  O   . HOH   E .   ? 0.5693 0.4890 0.8150 -0.2572 -0.1824 0.0967  746 HOH   A O   
2450 O  O   . HOH   E .   ? 0.2515 0.4019 0.5398 -0.1560 -0.1013 0.0345  747 HOH   A O   
2451 O  O   . HOH   E .   ? 0.3237 0.3333 0.4985 -0.0614 0.0763  0.0023  748 HOH   A O   
# 
