data_6T4P
# 
_entry.id   6T4P 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_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   6T4P         pdb_00006t4p 10.2210/pdb6t4p/pdb 
WWPDB D_1292104505 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2020-10-14 
2 'Structure model' 1 1 2020-10-28 
3 'Structure model' 1 2 2024-01-24 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation                      
2 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' database_2                    
5 3 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'            
2 2 'Structure model' '_citation.page_first'                
3 2 'Structure model' '_citation.page_last'                 
4 3 'Structure model' '_database_2.pdbx_DOI'                
5 3 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6T4P 
_pdbx_database_status.recvd_initial_deposition_date   2019-10-14 
_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.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'PDB entries for the same citation' 6T4N unspecified 
PDB 'PDB entries for the same citation' 6T4O unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biophys.J. 
_citation.journal_id_ASTM           BIOJAU 
_citation.journal_id_CSD            0030 
_citation.journal_id_ISSN           1542-0086 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            119 
_citation.language                  ? 
_citation.page_first                1513 
_citation.page_last                 1524 
_citation.title                     
'Isoform-Selective Enzyme Inhibitors by Exploring Pocket Size According to the Lock-and-Key Principle.' 
_citation.year                      2020 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bpj.2020.08.037 
_citation.pdbx_database_id_PubMed   32971003 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dudutiene, V.'   1  ? 
primary 'Zubriene, A.'    2  ? 
primary 'Kairys, V.'      3  ? 
primary 'Smirnov, A.'     4  ? 
primary 'Smirnoviene, J.' 5  ? 
primary 'Leitans, J.'     6  ? 
primary 'Kazaks, A.'      7  ? 
primary 'Tars, K.'        8  ? 
primary 'Manakova, L.'    9  ? 
primary 'Grazulis, S.'    10 ? 
primary 'Matulis, D.'     11 ? 
# 
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 ? 'Human Carbonic anhydrase II' ? 
2 non-polymer syn 'ZINC ION'                             65.409    1   ?       ? ?                             ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                   78.133    2   ?       ? ?                             ? 
4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237   1   ?       ? ?                             ? 
5 non-polymer syn naphthalene-1-sulfonamide              207.249   1   ?       ? ?                             ? 
6 non-polymer syn 'SODIUM ION'                           22.990    1   ?       ? ?                             ? 
7 water       nat water                                  18.015    247 ?       ? ?                             ? 
# 
_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 'DIMETHYL SULFOXIDE'                   DMS 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 
5 naphthalene-1-sulfonamide              MHK 
6 'SODIUM ION'                           NA  
7 water                                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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 
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 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' ? 'C6 H13 N O4 S'  195.237 
MET 'L-peptide linking' y METHIONINE                             ? 'C5 H11 N O2 S'  149.211 
MHK non-polymer         . naphthalene-1-sulfonamide              ? 'C10 H9 N O2 S'  207.249 
NA  non-polymer         . 'SODIUM ION'                           ? 'Na 1'           22.990  
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 
# 
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 DMS 1   302 1   DMS DMS A . 
D 4 MES 1   303 2   MES MES A . 
E 3 DMS 1   304 3   DMS DMS A . 
F 5 MHK 1   305 1   MHK V16 A . 
G 6 NA  1   306 1   NA  NA  A . 
H 7 HOH 1   401 171 HOH HOH A . 
H 7 HOH 2   402 245 HOH HOH A . 
H 7 HOH 3   403 197 HOH HOH A . 
H 7 HOH 4   404 191 HOH HOH A . 
H 7 HOH 5   405 62  HOH HOH A . 
H 7 HOH 6   406 107 HOH HOH A . 
H 7 HOH 7   407 187 HOH HOH A . 
H 7 HOH 8   408 155 HOH HOH A . 
H 7 HOH 9   409 209 HOH HOH A . 
H 7 HOH 10  410 79  HOH HOH A . 
H 7 HOH 11  411 215 HOH HOH A . 
H 7 HOH 12  412 110 HOH HOH A . 
H 7 HOH 13  413 33  HOH HOH A . 
H 7 HOH 14  414 88  HOH HOH A . 
H 7 HOH 15  415 59  HOH HOH A . 
H 7 HOH 16  416 101 HOH HOH A . 
H 7 HOH 17  417 132 HOH HOH A . 
H 7 HOH 18  418 45  HOH HOH A . 
H 7 HOH 19  419 129 HOH HOH A . 
H 7 HOH 20  420 85  HOH HOH A . 
H 7 HOH 21  421 122 HOH HOH A . 
H 7 HOH 22  422 217 HOH HOH A . 
H 7 HOH 23  423 225 HOH HOH A . 
H 7 HOH 24  424 42  HOH HOH A . 
H 7 HOH 25  425 240 HOH HOH A . 
H 7 HOH 26  426 146 HOH HOH A . 
H 7 HOH 27  427 50  HOH HOH A . 
H 7 HOH 28  428 165 HOH HOH A . 
H 7 HOH 29  429 144 HOH HOH A . 
H 7 HOH 30  430 102 HOH HOH A . 
H 7 HOH 31  431 227 HOH HOH A . 
H 7 HOH 32  432 1   HOH HOH A . 
H 7 HOH 33  433 57  HOH HOH A . 
H 7 HOH 34  434 133 HOH HOH A . 
H 7 HOH 35  435 237 HOH HOH A . 
H 7 HOH 36  436 198 HOH HOH A . 
H 7 HOH 37  437 46  HOH HOH A . 
H 7 HOH 38  438 201 HOH HOH A . 
H 7 HOH 39  439 143 HOH HOH A . 
H 7 HOH 40  440 182 HOH HOH A . 
H 7 HOH 41  441 167 HOH HOH A . 
H 7 HOH 42  442 243 HOH HOH A . 
H 7 HOH 43  443 194 HOH HOH A . 
H 7 HOH 44  444 97  HOH HOH A . 
H 7 HOH 45  445 31  HOH HOH A . 
H 7 HOH 46  446 139 HOH HOH A . 
H 7 HOH 47  447 136 HOH HOH A . 
H 7 HOH 48  448 214 HOH HOH A . 
H 7 HOH 49  449 244 HOH HOH A . 
H 7 HOH 50  450 82  HOH HOH A . 
H 7 HOH 51  451 17  HOH HOH A . 
H 7 HOH 52  452 216 HOH HOH A . 
H 7 HOH 53  453 47  HOH HOH A . 
H 7 HOH 54  454 126 HOH HOH A . 
H 7 HOH 55  455 172 HOH HOH A . 
H 7 HOH 56  456 179 HOH HOH A . 
H 7 HOH 57  457 68  HOH HOH A . 
H 7 HOH 58  458 142 HOH HOH A . 
H 7 HOH 59  459 7   HOH HOH A . 
H 7 HOH 60  460 5   HOH HOH A . 
H 7 HOH 61  461 27  HOH HOH A . 
H 7 HOH 62  462 224 HOH HOH A . 
H 7 HOH 63  463 89  HOH HOH A . 
H 7 HOH 64  464 233 HOH HOH A . 
H 7 HOH 65  465 115 HOH HOH A . 
H 7 HOH 66  466 156 HOH HOH A . 
H 7 HOH 67  467 190 HOH HOH A . 
H 7 HOH 68  468 41  HOH HOH A . 
H 7 HOH 69  469 81  HOH HOH A . 
H 7 HOH 70  470 28  HOH HOH A . 
H 7 HOH 71  471 184 HOH HOH A . 
H 7 HOH 72  472 26  HOH HOH A . 
H 7 HOH 73  473 40  HOH HOH A . 
H 7 HOH 74  474 128 HOH HOH A . 
H 7 HOH 75  475 74  HOH HOH A . 
H 7 HOH 76  476 67  HOH HOH A . 
H 7 HOH 77  477 188 HOH HOH A . 
H 7 HOH 78  478 100 HOH HOH A . 
H 7 HOH 79  479 61  HOH HOH A . 
H 7 HOH 80  480 134 HOH HOH A . 
H 7 HOH 81  481 71  HOH HOH A . 
H 7 HOH 82  482 118 HOH HOH A . 
H 7 HOH 83  483 219 HOH HOH A . 
H 7 HOH 84  484 43  HOH HOH A . 
H 7 HOH 85  485 75  HOH HOH A . 
H 7 HOH 86  486 83  HOH HOH A . 
H 7 HOH 87  487 13  HOH HOH A . 
H 7 HOH 88  488 12  HOH HOH A . 
H 7 HOH 89  489 2   HOH HOH A . 
H 7 HOH 90  490 185 HOH HOH A . 
H 7 HOH 91  491 175 HOH HOH A . 
H 7 HOH 92  492 160 HOH HOH A . 
H 7 HOH 93  493 72  HOH HOH A . 
H 7 HOH 94  494 116 HOH HOH A . 
H 7 HOH 95  495 60  HOH HOH A . 
H 7 HOH 96  496 64  HOH HOH A . 
H 7 HOH 97  497 206 HOH HOH A . 
H 7 HOH 98  498 11  HOH HOH A . 
H 7 HOH 99  499 4   HOH HOH A . 
H 7 HOH 100 500 91  HOH HOH A . 
H 7 HOH 101 501 189 HOH HOH A . 
H 7 HOH 102 502 162 HOH HOH A . 
H 7 HOH 103 503 6   HOH HOH A . 
H 7 HOH 104 504 174 HOH HOH A . 
H 7 HOH 105 505 161 HOH HOH A . 
H 7 HOH 106 506 54  HOH HOH A . 
H 7 HOH 107 507 63  HOH HOH A . 
H 7 HOH 108 508 159 HOH HOH A . 
H 7 HOH 109 509 3   HOH HOH A . 
H 7 HOH 110 510 205 HOH HOH A . 
H 7 HOH 111 511 29  HOH HOH A . 
H 7 HOH 112 512 104 HOH HOH A . 
H 7 HOH 113 513 130 HOH HOH A . 
H 7 HOH 114 514 213 HOH HOH A . 
H 7 HOH 115 515 35  HOH HOH A . 
H 7 HOH 116 516 87  HOH HOH A . 
H 7 HOH 117 517 151 HOH HOH A . 
H 7 HOH 118 518 20  HOH HOH A . 
H 7 HOH 119 519 199 HOH HOH A . 
H 7 HOH 120 520 51  HOH HOH A . 
H 7 HOH 121 521 65  HOH HOH A . 
H 7 HOH 122 522 10  HOH HOH A . 
H 7 HOH 123 523 210 HOH HOH A . 
H 7 HOH 124 524 158 HOH HOH A . 
H 7 HOH 125 525 18  HOH HOH A . 
H 7 HOH 126 526 38  HOH HOH A . 
H 7 HOH 127 527 90  HOH HOH A . 
H 7 HOH 128 528 24  HOH HOH A . 
H 7 HOH 129 529 58  HOH HOH A . 
H 7 HOH 130 530 181 HOH HOH A . 
H 7 HOH 131 531 231 HOH HOH A . 
H 7 HOH 132 532 32  HOH HOH A . 
H 7 HOH 133 533 96  HOH HOH A . 
H 7 HOH 134 534 8   HOH HOH A . 
H 7 HOH 135 535 124 HOH HOH A . 
H 7 HOH 136 536 238 HOH HOH A . 
H 7 HOH 137 537 229 HOH HOH A . 
H 7 HOH 138 538 22  HOH HOH A . 
H 7 HOH 139 539 49  HOH HOH A . 
H 7 HOH 140 540 53  HOH HOH A . 
H 7 HOH 141 541 37  HOH HOH A . 
H 7 HOH 142 542 70  HOH HOH A . 
H 7 HOH 143 543 178 HOH HOH A . 
H 7 HOH 144 544 55  HOH HOH A . 
H 7 HOH 145 545 196 HOH HOH A . 
H 7 HOH 146 546 14  HOH HOH A . 
H 7 HOH 147 547 15  HOH HOH A . 
H 7 HOH 148 548 180 HOH HOH A . 
H 7 HOH 149 549 21  HOH HOH A . 
H 7 HOH 150 550 103 HOH HOH A . 
H 7 HOH 151 551 73  HOH HOH A . 
H 7 HOH 152 552 48  HOH HOH A . 
H 7 HOH 153 553 16  HOH HOH A . 
H 7 HOH 154 554 123 HOH HOH A . 
H 7 HOH 155 555 39  HOH HOH A . 
H 7 HOH 156 556 150 HOH HOH A . 
H 7 HOH 157 557 221 HOH HOH A . 
H 7 HOH 158 558 145 HOH HOH A . 
H 7 HOH 159 559 23  HOH HOH A . 
H 7 HOH 160 560 106 HOH HOH A . 
H 7 HOH 161 561 52  HOH HOH A . 
H 7 HOH 162 562 114 HOH HOH A . 
H 7 HOH 163 563 9   HOH HOH A . 
H 7 HOH 164 564 34  HOH HOH A . 
H 7 HOH 165 565 121 HOH HOH A . 
H 7 HOH 166 566 234 HOH HOH A . 
H 7 HOH 167 567 36  HOH HOH A . 
H 7 HOH 168 568 109 HOH HOH A . 
H 7 HOH 169 569 69  HOH HOH A . 
H 7 HOH 170 570 105 HOH HOH A . 
H 7 HOH 171 571 78  HOH HOH A . 
H 7 HOH 172 572 246 HOH HOH A . 
H 7 HOH 173 573 228 HOH HOH A . 
H 7 HOH 174 574 25  HOH HOH A . 
H 7 HOH 175 575 19  HOH HOH A . 
H 7 HOH 176 576 170 HOH HOH A . 
H 7 HOH 177 577 76  HOH HOH A . 
H 7 HOH 178 578 111 HOH HOH A . 
H 7 HOH 179 579 223 HOH HOH A . 
H 7 HOH 180 580 212 HOH HOH A . 
H 7 HOH 181 581 149 HOH HOH A . 
H 7 HOH 182 582 193 HOH HOH A . 
H 7 HOH 183 583 84  HOH HOH A . 
H 7 HOH 184 584 177 HOH HOH A . 
H 7 HOH 185 585 154 HOH HOH A . 
H 7 HOH 186 586 226 HOH HOH A . 
H 7 HOH 187 587 131 HOH HOH A . 
H 7 HOH 188 588 195 HOH HOH A . 
H 7 HOH 189 589 108 HOH HOH A . 
H 7 HOH 190 590 94  HOH HOH A . 
H 7 HOH 191 591 30  HOH HOH A . 
H 7 HOH 192 592 173 HOH HOH A . 
H 7 HOH 193 593 119 HOH HOH A . 
H 7 HOH 194 594 232 HOH HOH A . 
H 7 HOH 195 595 66  HOH HOH A . 
H 7 HOH 196 596 153 HOH HOH A . 
H 7 HOH 197 597 176 HOH HOH A . 
H 7 HOH 198 598 44  HOH HOH A . 
H 7 HOH 199 599 112 HOH HOH A . 
H 7 HOH 200 600 211 HOH HOH A . 
H 7 HOH 201 601 86  HOH HOH A . 
H 7 HOH 202 602 239 HOH HOH A . 
H 7 HOH 203 603 56  HOH HOH A . 
H 7 HOH 204 604 166 HOH HOH A . 
H 7 HOH 205 605 77  HOH HOH A . 
H 7 HOH 206 606 137 HOH HOH A . 
H 7 HOH 207 607 140 HOH HOH A . 
H 7 HOH 208 608 95  HOH HOH A . 
H 7 HOH 209 609 218 HOH HOH A . 
H 7 HOH 210 610 169 HOH HOH A . 
H 7 HOH 211 611 200 HOH HOH A . 
H 7 HOH 212 612 207 HOH HOH A . 
H 7 HOH 213 613 135 HOH HOH A . 
H 7 HOH 214 614 235 HOH HOH A . 
H 7 HOH 215 615 192 HOH HOH A . 
H 7 HOH 216 616 241 HOH HOH A . 
H 7 HOH 217 617 141 HOH HOH A . 
H 7 HOH 218 618 183 HOH HOH A . 
H 7 HOH 219 619 230 HOH HOH A . 
H 7 HOH 220 620 204 HOH HOH A . 
H 7 HOH 221 621 157 HOH HOH A . 
H 7 HOH 222 622 127 HOH HOH A . 
H 7 HOH 223 623 202 HOH HOH A . 
H 7 HOH 224 624 148 HOH HOH A . 
H 7 HOH 225 625 208 HOH HOH A . 
H 7 HOH 226 626 93  HOH HOH A . 
H 7 HOH 227 627 113 HOH HOH A . 
H 7 HOH 228 628 220 HOH HOH A . 
H 7 HOH 229 629 99  HOH HOH A . 
H 7 HOH 230 630 168 HOH HOH A . 
H 7 HOH 231 631 236 HOH HOH A . 
H 7 HOH 232 632 92  HOH HOH A . 
H 7 HOH 233 633 117 HOH HOH A . 
H 7 HOH 234 634 125 HOH HOH A . 
H 7 HOH 235 635 147 HOH HOH A . 
H 7 HOH 236 636 186 HOH HOH A . 
H 7 HOH 237 637 242 HOH HOH A . 
H 7 HOH 238 638 222 HOH HOH A . 
H 7 HOH 239 639 164 HOH HOH A . 
H 7 HOH 240 640 163 HOH HOH A . 
H 7 HOH 241 641 120 HOH HOH A . 
H 7 HOH 242 642 247 HOH HOH A . 
H 7 HOH 243 643 203 HOH HOH A . 
H 7 HOH 244 644 98  HOH HOH A . 
H 7 HOH 245 645 152 HOH HOH A . 
H 7 HOH 246 646 138 HOH HOH A . 
H 7 HOH 247 647 80  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 9   ? CD  ? A LYS 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
4  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
5  1 Y 1 A LYS 170 ? NZ  ? A LYS 169 NZ  
6  1 Y 1 A LYS 172 ? NZ  ? A LYS 171 NZ  
7  1 Y 1 A LYS 228 ? CE  ? A LYS 227 CE  
8  1 Y 1 A LYS 228 ? NZ  ? A LYS 227 NZ  
9  1 Y 1 A LYS 257 ? CE  ? A LYS 256 CE  
10 1 Y 1 A LYS 257 ? NZ  ? A LYS 256 NZ  
11 1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
12 1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
13 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
14 1 N 1 A MES 303 ? S   ? D MES 1   S   
15 1 N 1 A MES 303 ? O1S ? D MES 1   O1S 
16 1 N 1 A MES 303 ? O2S ? D MES 1   O2S 
17 1 N 1 A MES 303 ? O3S ? D MES 1   O3S 
# 
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 reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? .        1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.2.19   2 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25     4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.080 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6T4P 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.072 
_cell.length_a_esd                 ? 
_cell.length_b                     41.159 
_cell.length_b_esd                 ? 
_cell.length_c                     71.704 
_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             ? 
# 
_symmetry.entry_id                         6T4P 
_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                   6T4P 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.06 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.17 
_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_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            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_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                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MAR555 FLAT PANEL' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2011-11-19 
_diffrn_detector.pdbx_frequency               ? 
# 
_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   0.8150 
_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                        'EMBL/DESY, HAMBURG BEAMLINE X11' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8150 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X11 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6T4P 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.750 
_reflns.d_resolution_low                 31.960 
_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                       23997 
_reflns.number_obs                       23997 
_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             98.900 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.800 
_reflns.pdbx_Rmerge_I_obs                0.071 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.071 
_reflns.pdbx_netI_over_av_sigmaI         7.300 
_reflns.pdbx_netI_over_sigmaI            23.300 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.081 
_reflns.pdbx_Rpim_I_all                  0.031 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         163532 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
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_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_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_Rsym_value 
_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 
1.750 1.840  ? 5.300  19108 ? ? ? 3508 99.600  ? ? ? ? 0.115 ? ? ? ? ? ? ? ? 5.400 0.115 ? ? 8.600  0.140 0.058 ? 1  1 ? ? ? 
1.840 1.960  ? 6.200  21054 ? ? ? 3328 100.000 ? ? ? ? 0.099 ? ? ? ? ? ? ? ? 6.300 0.099 ? ? 13.600 0.116 0.045 ? 2  1 ? ? ? 
1.960 2.090  ? 6.500  23084 ? ? ? 3125 100.000 ? ? ? ? 0.092 ? ? ? ? ? ? ? ? 7.400 0.092 ? ? 19.400 0.104 0.038 ? 3  1 ? ? ? 
2.090 2.260  ? 7.600  21692 ? ? ? 2914 100.000 ? ? ? ? 0.080 ? ? ? ? ? ? ? ? 7.400 0.080 ? ? 23.700 0.091 0.033 ? 4  1 ? ? ? 
2.260 2.470  ? 8.600  20163 ? ? ? 2708 100.000 ? ? ? ? 0.072 ? ? ? ? ? ? ? ? 7.400 0.072 ? ? 27.100 0.082 0.030 ? 5  1 ? ? ? 
2.470 2.770  ? 8.800  18182 ? ? ? 2439 100.000 ? ? ? ? 0.068 ? ? ? ? ? ? ? ? 7.500 0.068 ? ? 30.500 0.077 0.028 ? 6  1 ? ? ? 
2.770 3.200  ? 9.100  15945 ? ? ? 2154 100.000 ? ? ? ? 0.065 ? ? ? ? ? ? ? ? 7.400 0.065 ? ? 34.400 0.075 0.028 ? 7  1 ? ? ? 
3.200 3.910  ? 9.900  12710 ? ? ? 1819 98.900  ? ? ? ? 0.065 ? ? ? ? ? ? ? ? 7.000 0.065 ? ? 36.200 0.074 0.029 ? 8  1 ? ? ? 
3.910 5.530  ? 10.600 8016  ? ? ? 1321 92.700  ? ? ? ? 0.062 ? ? ? ? ? ? ? ? 6.100 0.062 ? ? 34.100 0.071 0.029 ? 9  1 ? ? ? 
5.530 31.960 ? 9.300  3578  ? ? ? 681  83.200  ? ? ? ? 0.066 ? ? ? ? ? ? ? ? 5.300 0.066 ? ? 31.400 0.076 0.034 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.0900 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            -0.3500 
_refine.aniso_B[2][2]                            -0.2500 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.4600 
_refine.B_iso_max                                62.890 
_refine.B_iso_mean                               16.0510 
_refine.B_iso_min                                4.840 
_refine.correlation_coeff_Fo_to_Fc               0.9580 
_refine.correlation_coeff_Fo_to_Fc_free          0.9420 
_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                                 6T4P 
_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                            1.7500 
_refine.ls_d_res_low                             26.5700 
_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                     21618 
_refine.ls_number_reflns_R_free                  2367 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.7600 
_refine.ls_percent_reflns_R_free                 9.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1652 
_refine.ls_R_factor_R_free                       0.1993 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1615 
_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                    ? 
_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                      4HT0 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.1280 
_refine.pdbx_overall_ESU_R_Free                  0.1190 
_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                       1.7500 
_refine_hist.d_res_low                        26.5700 
_refine_hist.number_atoms_solvent             247 
_refine_hist.number_atoms_total               2315 
_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           21.77 
_refine_hist.pdbx_B_iso_mean_solvent          27.14 
_refine_hist.pdbx_number_atoms_protein        2036 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.012  2151 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.849  1.643  2925 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.042  5.000  261  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 34.086 23.714 105  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.936 15.000 344  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 21.508 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.133  0.200  260  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  1673 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.7500 
_refine_ls_shell.d_res_low                        1.7950 
_refine_ls_shell.number_reflns_all                1756 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             177 
_refine_ls_shell.number_reflns_R_work             1579 
_refine_ls_shell.percent_reflns_obs               98.8700 
_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                  0.2950 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.2310 
_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                    ? 
# 
_struct.entry_id                     6T4P 
_struct.title                        'Human Carbonic anhydrase II bound by napthalene-1-sulfonamide' 
_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        6T4P 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, 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 3 ? 
F N N 5 ? 
G N N 6 ? 
H N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              6T4P 
_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)' 880   ? 
1 MORE         4     ? 
1 'SSA (A^2)'  11120 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A SER 73  OG  ? ? ? 1_555 G NA  . NA  ? ? A SER 73  A NA  306 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc2  metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
metalc3  metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc4  metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
metalc5  metalc ? ? A SER 219 OG  ? ? ? 1_555 G NA  . NA  ? ? A SER 220 A NA  306 1_545 ? ? ? ? ? ? ? 2.667 ? ? 
metalc6  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F MHK . N10 ? ? A ZN  301 A MHK 305 1_555 ? ? ? ? ? ? ? 1.999 ? ? 
metalc7  metalc ? ? G NA  .   NA  ? ? ? 1_555 H HOH . O   ? ? A NA  306 A HOH 450 1_565 ? ? ? ? ? ? ? 2.242 ? ? 
metalc8  metalc ? ? G NA  .   NA  ? ? ? 1_555 H HOH . O   ? ? A NA  306 A HOH 464 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc9  metalc ? ? G NA  .   NA  ? ? ? 1_555 H HOH . O   ? ? A NA  306 A HOH 498 1_565 ? ? ? ? ? ? ? 2.565 ? ? 
metalc10 metalc ? ? G NA  .   NA  ? ? ? 1_555 H HOH . O   ? ? A NA  306 A HOH 597 1_565 ? ? ? ? ? ? ? 2.348 ? ? 
# 
_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  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 OG  ? A SER 219 ? A SER 220 ? 1_555 46.7  ? 
2  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 450 ? 1_565 166.4 ? 
3  OG  ? A SER 219 ? A SER 220 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 450 ? 1_565 131.8 ? 
4  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 464 ? 1_555 78.7  ? 
5  OG  ? A SER 219 ? A SER 220 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 464 ? 1_555 49.4  ? 
6  O   ? H HOH .   ? A HOH 450 ? 1_565 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 464 ? 1_555 91.8  ? 
7  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 498 ? 1_565 86.0  ? 
8  OG  ? A SER 219 ? A SER 220 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 498 ? 1_565 126.5 ? 
9  O   ? H HOH .   ? A HOH 450 ? 1_565 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 498 ? 1_565 87.8  ? 
10 O   ? H HOH .   ? A HOH 464 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 498 ? 1_565 107.7 ? 
11 OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 597 ? 1_565 94.9  ? 
12 OG  ? A SER 219 ? A SER 220 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 597 ? 1_565 62.4  ? 
13 O   ? H HOH .   ? A HOH 450 ? 1_565 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 597 ? 1_565 94.5  ? 
14 O   ? H HOH .   ? A HOH 464 ? 1_555 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 597 ? 1_565 88.6  ? 
15 O   ? H HOH .   ? A HOH 498 ? 1_565 NA ? G NA . ? A NA 306 ? 1_555 O   ? H HOH .   ? A HOH 597 ? 1_565 163.5 ? 
16 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 104.7 ? 
17 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_555 113.0 ? 
18 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.5  ? 
19 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? F MHK .   ? A MHK 305 ? 1_555 113.1 ? 
20 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? F MHK .   ? A MHK 305 ? 1_555 111.0 ? 
21 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 ? F MHK .   ? A MHK 305 ? 1_555 114.3 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -4.74 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 3.30  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O THR A 207 ? O THR A 208 N LEU A 140 ? N LEU A 141 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A DMS 302 ? 4  'binding site for residue DMS A 302' 
AC3 Software A MES 303 ? 4  'binding site for residue MES A 303' 
AC4 Software A DMS 304 ? 7  'binding site for residue DMS A 304' 
AC5 Software A MHK 305 ? 11 'binding site for residue MHK A 305' 
AC6 Software A NA  306 ? 6  'binding site for residue NA A 306'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  MHK F .   ? MHK A 305 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  HOH H .   ? HOH A 536 . ? 1_555 ? 
9  AC3 4  LEU A 163 ? LEU A 164 . ? 1_555 ? 
10 AC3 4  ASP A 164 ? ASP A 165 . ? 1_555 ? 
11 AC3 4  LYS A 224 ? LYS A 225 . ? 1_555 ? 
12 AC3 4  LYS A 227 ? LYS A 228 . ? 1_555 ? 
13 AC4 7  HIS A 4   ? HIS A 4   . ? 1_555 ? 
14 AC4 7  TRP A 5   ? TRP A 5   . ? 1_555 ? 
15 AC4 7  ASN A 11  ? ASN A 11  . ? 1_555 ? 
16 AC4 7  HIS A 15  ? HIS A 15  . ? 1_555 ? 
17 AC4 7  TRP A 16  ? TRP A 16  . ? 1_555 ? 
18 AC4 7  ASP A 19  ? ASP A 19  . ? 1_555 ? 
19 AC4 7  PHE A 20  ? PHE A 20  . ? 1_555 ? 
20 AC5 11 HIS A 94  ? HIS A 94  . ? 1_555 ? 
21 AC5 11 HIS A 96  ? HIS A 96  . ? 1_555 ? 
22 AC5 11 HIS A 119 ? HIS A 119 . ? 1_555 ? 
23 AC5 11 VAL A 121 ? VAL A 121 . ? 1_555 ? 
24 AC5 11 PHE A 130 ? PHE A 131 . ? 1_555 ? 
25 AC5 11 VAL A 142 ? VAL A 143 . ? 1_555 ? 
26 AC5 11 LEU A 197 ? LEU A 198 . ? 1_555 ? 
27 AC5 11 THR A 198 ? THR A 199 . ? 1_555 ? 
28 AC5 11 THR A 199 ? THR A 200 . ? 1_555 ? 
29 AC5 11 TRP A 208 ? TRP A 209 . ? 1_555 ? 
30 AC5 11 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
31 AC6 6  SER A 73  ? SER A 73  . ? 1_555 ? 
32 AC6 6  SER A 219 ? SER A 220 . ? 1_565 ? 
33 AC6 6  HOH H .   ? HOH A 450 . ? 1_565 ? 
34 AC6 6  HOH H .   ? HOH A 464 . ? 1_555 ? 
35 AC6 6  HOH H .   ? HOH A 498 . ? 1_565 ? 
36 AC6 6  HOH H .   ? HOH A 597 . ? 1_565 ? 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              89 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              89 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              89 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                98.27 
_pdbx_validate_rmsd_angle.angle_target_value         111.80 
_pdbx_validate_rmsd_angle.angle_deviation            -13.53 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -145.53 17.14   
2 1 ARG A 27  ? ? -143.93 56.02   
3 1 PHE A 176 ? ? -151.22 75.21   
4 1 ASN A 244 ? ? -97.76  51.82   
5 1 LYS A 252 ? ? 58.90   -137.19 
# 
_pdbx_entry_details.entry_id                 6T4P 
_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         ? 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MES O1   O  N N 240 
MES C2   C  N N 241 
MES C3   C  N N 242 
MES N4   N  N N 243 
MES C5   C  N N 244 
MES C6   C  N N 245 
MES C7   C  N N 246 
MES C8   C  N N 247 
MES S    S  N N 248 
MES O1S  O  N N 249 
MES O2S  O  N N 250 
MES O3S  O  N N 251 
MES H21  H  N N 252 
MES H22  H  N N 253 
MES H31  H  N N 254 
MES H32  H  N N 255 
MES HN4  H  N N 256 
MES H51  H  N N 257 
MES H52  H  N N 258 
MES H61  H  N N 259 
MES H62  H  N N 260 
MES H71  H  N N 261 
MES H72  H  N N 262 
MES H81  H  N N 263 
MES H82  H  N N 264 
MET N    N  N N 265 
MET CA   C  N S 266 
MET C    C  N N 267 
MET O    O  N N 268 
MET CB   C  N N 269 
MET CG   C  N N 270 
MET SD   S  N N 271 
MET CE   C  N N 272 
MET OXT  O  N N 273 
MET H    H  N N 274 
MET H2   H  N N 275 
MET HA   H  N N 276 
MET HB2  H  N N 277 
MET HB3  H  N N 278 
MET HG2  H  N N 279 
MET HG3  H  N N 280 
MET HE1  H  N N 281 
MET HE2  H  N N 282 
MET HE3  H  N N 283 
MET HXT  H  N N 284 
MHK C1   C  Y N 285 
MHK C11  C  Y N 286 
MHK C2   C  Y N 287 
MHK C3   C  Y N 288 
MHK C4   C  Y N 289 
MHK C5   C  Y N 290 
MHK C6   C  Y N 291 
MHK O9   O  N N 292 
MHK S7   S  N N 293 
MHK O8   O  N N 294 
MHK N10  N  N N 295 
MHK C14  C  Y N 296 
MHK C13  C  Y N 297 
MHK C12  C  Y N 298 
MHK H1   H  N N 299 
MHK H2   H  N N 300 
MHK H3   H  N N 301 
MHK H4   H  N N 302 
MHK H5   H  N N 303 
MHK H6   H  N N 304 
MHK H7   H  N N 305 
MHK H8   H  N N 306 
MHK H9   H  N N 307 
NA  NA   NA N N 308 
PHE N    N  N N 309 
PHE CA   C  N S 310 
PHE C    C  N N 311 
PHE O    O  N N 312 
PHE CB   C  N N 313 
PHE CG   C  Y N 314 
PHE CD1  C  Y N 315 
PHE CD2  C  Y N 316 
PHE CE1  C  Y N 317 
PHE CE2  C  Y N 318 
PHE CZ   C  Y N 319 
PHE OXT  O  N N 320 
PHE H    H  N N 321 
PHE H2   H  N N 322 
PHE HA   H  N N 323 
PHE HB2  H  N N 324 
PHE HB3  H  N N 325 
PHE HD1  H  N N 326 
PHE HD2  H  N N 327 
PHE HE1  H  N N 328 
PHE HE2  H  N N 329 
PHE HZ   H  N N 330 
PHE HXT  H  N N 331 
PRO N    N  N N 332 
PRO CA   C  N S 333 
PRO C    C  N N 334 
PRO O    O  N N 335 
PRO CB   C  N N 336 
PRO CG   C  N N 337 
PRO CD   C  N N 338 
PRO OXT  O  N N 339 
PRO H    H  N N 340 
PRO HA   H  N N 341 
PRO HB2  H  N N 342 
PRO HB3  H  N N 343 
PRO HG2  H  N N 344 
PRO HG3  H  N N 345 
PRO HD2  H  N N 346 
PRO HD3  H  N N 347 
PRO HXT  H  N N 348 
SER N    N  N N 349 
SER CA   C  N S 350 
SER C    C  N N 351 
SER O    O  N N 352 
SER CB   C  N N 353 
SER OG   O  N N 354 
SER OXT  O  N N 355 
SER H    H  N N 356 
SER H2   H  N N 357 
SER HA   H  N N 358 
SER HB2  H  N N 359 
SER HB3  H  N N 360 
SER HG   H  N N 361 
SER HXT  H  N N 362 
THR N    N  N N 363 
THR CA   C  N S 364 
THR C    C  N N 365 
THR O    O  N N 366 
THR CB   C  N R 367 
THR OG1  O  N N 368 
THR CG2  C  N N 369 
THR OXT  O  N N 370 
THR H    H  N N 371 
THR H2   H  N N 372 
THR HA   H  N N 373 
THR HB   H  N N 374 
THR HG1  H  N N 375 
THR HG21 H  N N 376 
THR HG22 H  N N 377 
THR HG23 H  N N 378 
THR HXT  H  N N 379 
TRP N    N  N N 380 
TRP CA   C  N S 381 
TRP C    C  N N 382 
TRP O    O  N N 383 
TRP CB   C  N N 384 
TRP CG   C  Y N 385 
TRP CD1  C  Y N 386 
TRP CD2  C  Y N 387 
TRP NE1  N  Y N 388 
TRP CE2  C  Y N 389 
TRP CE3  C  Y N 390 
TRP CZ2  C  Y N 391 
TRP CZ3  C  Y N 392 
TRP CH2  C  Y N 393 
TRP OXT  O  N N 394 
TRP H    H  N N 395 
TRP H2   H  N N 396 
TRP HA   H  N N 397 
TRP HB2  H  N N 398 
TRP HB3  H  N N 399 
TRP HD1  H  N N 400 
TRP HE1  H  N N 401 
TRP HE3  H  N N 402 
TRP HZ2  H  N N 403 
TRP HZ3  H  N N 404 
TRP HH2  H  N N 405 
TRP HXT  H  N N 406 
TYR N    N  N N 407 
TYR CA   C  N S 408 
TYR C    C  N N 409 
TYR O    O  N N 410 
TYR CB   C  N N 411 
TYR CG   C  Y N 412 
TYR CD1  C  Y N 413 
TYR CD2  C  Y N 414 
TYR CE1  C  Y N 415 
TYR CE2  C  Y N 416 
TYR CZ   C  Y N 417 
TYR OH   O  N N 418 
TYR OXT  O  N N 419 
TYR H    H  N N 420 
TYR H2   H  N N 421 
TYR HA   H  N N 422 
TYR HB2  H  N N 423 
TYR HB3  H  N N 424 
TYR HD1  H  N N 425 
TYR HD2  H  N N 426 
TYR HE1  H  N N 427 
TYR HE2  H  N N 428 
TYR HH   H  N N 429 
TYR HXT  H  N N 430 
VAL N    N  N N 431 
VAL CA   C  N S 432 
VAL C    C  N N 433 
VAL O    O  N N 434 
VAL CB   C  N N 435 
VAL CG1  C  N N 436 
VAL CG2  C  N N 437 
VAL OXT  O  N N 438 
VAL H    H  N N 439 
VAL H2   H  N N 440 
VAL HA   H  N N 441 
VAL HB   H  N N 442 
VAL HG11 H  N N 443 
VAL HG12 H  N N 444 
VAL HG13 H  N N 445 
VAL HG21 H  N N 446 
VAL HG22 H  N N 447 
VAL HG23 H  N N 448 
VAL HXT  H  N N 449 
ZN  ZN   ZN N N 450 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MES O1  C2   sing N N 227 
MES O1  C6   sing N N 228 
MES C2  C3   sing N N 229 
MES C2  H21  sing N N 230 
MES C2  H22  sing N N 231 
MES C3  N4   sing N N 232 
MES C3  H31  sing N N 233 
MES C3  H32  sing N N 234 
MES N4  C5   sing N N 235 
MES N4  C7   sing N N 236 
MES N4  HN4  sing N N 237 
MES C5  C6   sing N N 238 
MES C5  H51  sing N N 239 
MES C5  H52  sing N N 240 
MES C6  H61  sing N N 241 
MES C6  H62  sing N N 242 
MES C7  C8   sing N N 243 
MES C7  H71  sing N N 244 
MES C7  H72  sing N N 245 
MES C8  S    sing N N 246 
MES C8  H81  sing N N 247 
MES C8  H82  sing N N 248 
MES S   O1S  doub N N 249 
MES S   O2S  doub N N 250 
MES S   O3S  sing N N 251 
MET N   CA   sing N N 252 
MET N   H    sing N N 253 
MET N   H2   sing N N 254 
MET CA  C    sing N N 255 
MET CA  CB   sing N N 256 
MET CA  HA   sing N N 257 
MET C   O    doub N N 258 
MET C   OXT  sing N N 259 
MET CB  CG   sing N N 260 
MET CB  HB2  sing N N 261 
MET CB  HB3  sing N N 262 
MET CG  SD   sing N N 263 
MET CG  HG2  sing N N 264 
MET CG  HG3  sing N N 265 
MET SD  CE   sing N N 266 
MET CE  HE1  sing N N 267 
MET CE  HE2  sing N N 268 
MET CE  HE3  sing N N 269 
MET OXT HXT  sing N N 270 
MHK C6  C1   doub Y N 271 
MHK C6  C5   sing Y N 272 
MHK C1  C2   sing Y N 273 
MHK C5  C4   doub Y N 274 
MHK C2  C11  doub Y N 275 
MHK C2  C3   sing Y N 276 
MHK C11 C12  sing Y N 277 
MHK C4  C3   sing Y N 278 
MHK C4  S7   sing N N 279 
MHK C3  C14  doub Y N 280 
MHK N10 S7   sing N N 281 
MHK O9  S7   doub N N 282 
MHK C12 C13  doub Y N 283 
MHK S7  O8   doub N N 284 
MHK C14 C13  sing Y N 285 
MHK C1  H1   sing N N 286 
MHK C11 H2   sing N N 287 
MHK C5  H3   sing N N 288 
MHK C6  H4   sing N N 289 
MHK N10 H5   sing N N 290 
MHK N10 H6   sing N N 291 
MHK C14 H7   sing N N 292 
MHK C13 H8   sing N N 293 
MHK C12 H9   sing N N 294 
PHE N   CA   sing N N 295 
PHE N   H    sing N N 296 
PHE N   H2   sing N N 297 
PHE CA  C    sing N N 298 
PHE CA  CB   sing N N 299 
PHE CA  HA   sing N N 300 
PHE C   O    doub N N 301 
PHE C   OXT  sing N N 302 
PHE CB  CG   sing N N 303 
PHE CB  HB2  sing N N 304 
PHE CB  HB3  sing N N 305 
PHE CG  CD1  doub Y N 306 
PHE CG  CD2  sing Y N 307 
PHE CD1 CE1  sing Y N 308 
PHE CD1 HD1  sing N N 309 
PHE CD2 CE2  doub Y N 310 
PHE CD2 HD2  sing N N 311 
PHE CE1 CZ   doub Y N 312 
PHE CE1 HE1  sing N N 313 
PHE CE2 CZ   sing Y N 314 
PHE CE2 HE2  sing N N 315 
PHE CZ  HZ   sing N N 316 
PHE OXT HXT  sing N N 317 
PRO N   CA   sing N N 318 
PRO N   CD   sing N N 319 
PRO N   H    sing N N 320 
PRO CA  C    sing N N 321 
PRO CA  CB   sing N N 322 
PRO CA  HA   sing N N 323 
PRO C   O    doub N N 324 
PRO C   OXT  sing N N 325 
PRO CB  CG   sing N N 326 
PRO CB  HB2  sing N N 327 
PRO CB  HB3  sing N N 328 
PRO CG  CD   sing N N 329 
PRO CG  HG2  sing N N 330 
PRO CG  HG3  sing N N 331 
PRO CD  HD2  sing N N 332 
PRO CD  HD3  sing N N 333 
PRO OXT HXT  sing N N 334 
SER N   CA   sing N N 335 
SER N   H    sing N N 336 
SER N   H2   sing N N 337 
SER CA  C    sing N N 338 
SER CA  CB   sing N N 339 
SER CA  HA   sing N N 340 
SER C   O    doub N N 341 
SER C   OXT  sing N N 342 
SER CB  OG   sing N N 343 
SER CB  HB2  sing N N 344 
SER CB  HB3  sing N N 345 
SER OG  HG   sing N N 346 
SER OXT HXT  sing N N 347 
THR N   CA   sing N N 348 
THR N   H    sing N N 349 
THR N   H2   sing N N 350 
THR CA  C    sing N N 351 
THR CA  CB   sing N N 352 
THR CA  HA   sing N N 353 
THR C   O    doub N N 354 
THR C   OXT  sing N N 355 
THR CB  OG1  sing N N 356 
THR CB  CG2  sing N N 357 
THR CB  HB   sing N N 358 
THR OG1 HG1  sing N N 359 
THR CG2 HG21 sing N N 360 
THR CG2 HG22 sing N N 361 
THR CG2 HG23 sing N N 362 
THR OXT HXT  sing N N 363 
TRP N   CA   sing N N 364 
TRP N   H    sing N N 365 
TRP N   H2   sing N N 366 
TRP CA  C    sing N N 367 
TRP CA  CB   sing N N 368 
TRP CA  HA   sing N N 369 
TRP C   O    doub N N 370 
TRP C   OXT  sing N N 371 
TRP CB  CG   sing N N 372 
TRP CB  HB2  sing N N 373 
TRP CB  HB3  sing N N 374 
TRP CG  CD1  doub Y N 375 
TRP CG  CD2  sing Y N 376 
TRP CD1 NE1  sing Y N 377 
TRP CD1 HD1  sing N N 378 
TRP CD2 CE2  doub Y N 379 
TRP CD2 CE3  sing Y N 380 
TRP NE1 CE2  sing Y N 381 
TRP NE1 HE1  sing N N 382 
TRP CE2 CZ2  sing Y N 383 
TRP CE3 CZ3  doub Y N 384 
TRP CE3 HE3  sing N N 385 
TRP CZ2 CH2  doub Y N 386 
TRP CZ2 HZ2  sing N N 387 
TRP CZ3 CH2  sing Y N 388 
TRP CZ3 HZ3  sing N N 389 
TRP CH2 HH2  sing N N 390 
TRP OXT HXT  sing N N 391 
TYR N   CA   sing N N 392 
TYR N   H    sing N N 393 
TYR N   H2   sing N N 394 
TYR CA  C    sing N N 395 
TYR CA  CB   sing N N 396 
TYR CA  HA   sing N N 397 
TYR C   O    doub N N 398 
TYR C   OXT  sing N N 399 
TYR CB  CG   sing N N 400 
TYR CB  HB2  sing N N 401 
TYR CB  HB3  sing N N 402 
TYR CG  CD1  doub Y N 403 
TYR CG  CD2  sing Y N 404 
TYR CD1 CE1  sing Y N 405 
TYR CD1 HD1  sing N N 406 
TYR CD2 CE2  doub Y N 407 
TYR CD2 HD2  sing N N 408 
TYR CE1 CZ   doub Y N 409 
TYR CE1 HE1  sing N N 410 
TYR CE2 CZ   sing Y N 411 
TYR CE2 HE2  sing N N 412 
TYR CZ  OH   sing N N 413 
TYR OH  HH   sing N N 414 
TYR OXT HXT  sing N N 415 
VAL N   CA   sing N N 416 
VAL N   H    sing N N 417 
VAL N   H2   sing N N 418 
VAL CA  C    sing N N 419 
VAL CA  CB   sing N N 420 
VAL CA  HA   sing N N 421 
VAL C   O    doub N N 422 
VAL C   OXT  sing N N 423 
VAL CB  CG1  sing N N 424 
VAL CB  CG2  sing N N 425 
VAL CB  HB   sing N N 426 
VAL CG1 HG11 sing N N 427 
VAL CG1 HG12 sing N N 428 
VAL CG1 HG13 sing N N 429 
VAL CG2 HG21 sing N N 430 
VAL CG2 HG22 sing N N 431 
VAL CG2 HG23 sing N N 432 
VAL OXT HXT  sing N N 433 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        MHK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   MHK 
_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        ? 
# 
_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                    6T4P 
_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.fract_transf_matrix[1][1]   0.023769 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005959 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024296 
_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]   0.014378 
_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  
NA 
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   ? 30.348 2.939   8.036   1.00 29.68 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 31.193 1.893   8.635   1.00 28.81 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.293 0.913   9.381   1.00 23.86 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.422 -0.281  9.158   1.00 22.52 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 32.292 2.466   9.567   1.00 38.75 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 33.218 1.438   10.145  1.00 41.51 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 33.241 1.139   11.505  1.00 45.31 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 34.114 0.605   9.563   1.00 47.50 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 34.109 0.166   11.734  1.00 48.37 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 34.673 -0.179  10.553  1.00 49.10 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.424 1.410   10.275  1.00 19.26 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 28.742 0.478   11.174  1.00 15.23 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 27.746 -0.368  10.391  1.00 13.58 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.181 0.064   9.391   1.00 12.64 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.060 1.163   12.382  1.00 15.16 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 26.864 1.987   12.024  1.00 14.96 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 26.808 3.316   11.714  1.00 14.29 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.509 1.500   11.991  1.00 13.40 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.498 3.671   11.464  1.00 15.24 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.688 2.578   11.617  1.00 13.55 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 24.932 0.246   12.253  1.00 12.55 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.299 2.456   11.542  1.00 13.07 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.569 0.109   12.086  1.00 12.19 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 22.765 1.210   11.777  1.00 14.01 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.564 -1.590  10.875  1.00 12.80 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.477 -2.383  10.334  1.00 13.17 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.131 -3.522  11.282  1.00 12.80 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.117 -3.358  12.498  1.00 12.54 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 25.862 -4.685  10.689  1.00 14.25 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.445 -5.842  11.457  1.00 14.95 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.284 -7.070  11.108  1.00 19.61 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 25.915 -8.168  11.509  1.00 19.08 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 23.963 -6.092  11.180  1.00 12.80 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.058 -5.023  11.748  1.00 10.87 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.651 -5.062  13.082  1.00 11.42 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.544 -4.034  10.919  1.00 10.00 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.825 -4.072  13.601  1.00 9.27  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.662 -3.071  11.405  1.00 9.56  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.313 -3.109  12.748  1.00 9.99  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.481 -2.145  13.206  1.00 10.45 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.438 -6.889  10.438  1.00 20.59 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.301 -8.033  10.138  1.00 21.13 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.283 -8.406  11.247  1.00 23.14 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.317 -7.799  12.316  1.00 26.41 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.159 -9.397  10.965  1.00 27.42 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.152 -9.845  11.951  1.00 28.82 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.158 -8.739  12.267  1.00 28.79 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.678 -8.656  13.390  1.00 30.85 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 31.924 -11.097 11.501  1.00 31.72 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 33.025 -11.544 12.465  1.00 29.80 ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? 32.381 -7.863  11.288  1.00 23.52 ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? 33.477 -6.923  11.425  1.00 22.23 ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? 32.980 -5.537  11.819  1.00 19.05 ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? 33.768 -4.681  12.192  1.00 17.21 ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? 34.330 -6.963  10.145  1.00 24.13 ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? 34.862 -8.337  9.887   1.00 26.72 ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? 35.818 -8.912  10.690  1.00 28.25 ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? 34.567 -9.244  8.915   1.00 32.22 ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? 36.097 -10.132 10.255  1.00 28.93 ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? 35.348 -10.360 9.137   1.00 29.78 ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? 31.656 -5.315  11.805  1.00 17.15 ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? 31.200 -3.954  12.042  1.00 15.90 ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? 29.874 -3.983  12.814  1.00 15.65 ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? 29.172 -2.977  12.866  1.00 15.46 ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? 31.017 -3.226  10.712  1.00 16.06 ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? 29.912 -3.783  9.827   1.00 18.06 ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? 29.349 -4.838  10.105  1.00 21.44 ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 29.596 -3.090  8.755   1.00 18.38 ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? 29.578 -5.136  13.420  1.00 14.50 ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? 28.261 -5.348  14.027  1.00 14.47 ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? 28.176 -4.742  15.429  1.00 13.92 ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? 29.051 -4.005  15.876  1.00 14.04 ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? 27.082 -5.019  16.190  1.00 12.92 ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? 26.855 -4.362  17.478  1.00 12.96 ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? 28.021 -4.373  18.473  1.00 12.32 ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? 28.185 -3.425  19.235  1.00 12.06 ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? 25.678 -5.231  18.010  1.00 14.34 ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? 24.876 -5.519  16.759  1.00 13.79 ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? 25.958 -5.862  15.756  1.00 13.68 ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? 28.826 -5.448  18.495  1.00 12.86 ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? 29.889 -5.515  19.488  1.00 14.72 ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? 31.043 -4.548  19.147  1.00 13.68 ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? 31.940 -4.350  19.990  1.00 13.90 ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? 30.389 -6.963  19.542  1.00 19.46 ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? 30.991 -7.460  18.198  1.00 22.46 ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? 30.201 -8.089  17.031  1.00 28.26 ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? 29.003 -7.771  16.890  1.00 22.30 ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? 30.796 -8.888  16.280  1.00 26.80 ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? 31.034 -3.991  17.937  1.00 12.18 ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? 32.021 -3.031  17.429  1.00 12.29 ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? 31.591 -1.588  17.677  1.00 12.97 ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? 32.405 -0.665  17.662  1.00 11.26 ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? 32.295 -3.225  15.923  1.00 14.17 ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? 33.026 -4.504  15.658  1.00 17.35 ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? 34.407 -4.590  15.794  1.00 18.42 ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? 32.595 -5.726  15.267  1.00 17.19 ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? 34.789 -5.829  15.504  1.00 20.22 ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? 33.711 -6.546  15.200  1.00 20.47 ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? 30.297 -1.363  17.856  1.00 10.74 ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? 29.776 -0.011  17.777  1.00 10.35 ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? 30.363 0.947   18.814  1.00 10.10 ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? 30.423 2.142   18.522  1.00 11.10 ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? 28.245 -0.011  17.886  1.00 9.49  ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? 27.576 -0.699  16.740  1.00 10.42 ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? 28.095 -1.116  15.546  1.00 10.15 ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? 26.169 -0.991  16.693  1.00 9.47  ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? 27.109 -1.676  14.755  1.00 10.74 ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? 25.909 -1.586  15.438  1.00 10.70 ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? 25.134 -0.771  17.597  1.00 10.25 ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? 24.649 -2.056  15.087  1.00 11.52 ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? 23.873 -1.215  17.248  1.00 9.71  ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? 23.637 -1.846  16.012  1.00 10.47 ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? 30.803 0.442   19.970  1.00 10.86 ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? 31.256 1.342   21.015  1.00 12.35 ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? 32.493 2.135   20.586  1.00 12.05 ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? 32.774 3.174   21.181  1.00 11.20 ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? 31.484 0.613   22.339  1.00 11.94 ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? 32.670 -0.291  22.251  1.00 13.63 ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? 33.921 0.086   22.706  1.00 15.03 ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? 32.820 -1.476  21.656  1.00 13.77 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? 34.786 -0.878  22.444  1.00 14.67 ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? 34.154 -1.830  21.801  1.00 15.29 ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? 33.234 1.624   19.593  1.00 13.67 ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? 34.499 2.279   19.252  1.00 13.91 ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? 34.210 3.591   18.527  1.00 16.52 ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? 34.953 4.552   18.707  1.00 16.98 ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? 35.320 1.358   18.343  1.00 15.72 ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? 35.914 0.138   19.033  1.00 16.11 ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? 36.624 -0.761  18.046  1.00 16.02 ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? 35.720 -1.815  17.456  1.00 16.40 ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? 36.377 -2.552  16.348  1.00 13.95 ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? 33.102 3.663   17.752  1.00 14.23 ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? 32.732 4.954   17.188  1.00 15.70 ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? 31.663 5.685   17.990  1.00 16.34 ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? 31.525 6.897   17.822  1.00 16.01 ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? 32.288 4.842   15.740  1.00 18.40 ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? 33.526 4.600   14.909  1.00 25.42 ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? 34.236 5.565   14.672  1.00 26.25 ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? 33.823 3.420   14.640  1.00 30.17 ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? 30.904 4.947   18.818  1.00 13.27 ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? 29.776 5.502   19.562  1.00 13.65 ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? 29.877 5.029   20.998  1.00 13.06 ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? 29.267 4.054   21.381  1.00 12.15 ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? 28.465 5.046   18.908  1.00 14.07 ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? 28.392 5.474   17.474  1.00 14.51 ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? 27.959 6.756   17.140  1.00 14.53 ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? 28.765 4.596   16.464  1.00 14.78 ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? 27.905 7.122   15.811  1.00 14.86 ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? 28.726 4.974   15.133  1.00 16.31 ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? 28.301 6.251   14.819  1.00 16.42 ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? 30.736 5.663   21.822  1.00 13.24 ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? 31.044 5.172   23.160  1.00 12.90 ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? 29.823 5.081   24.079  1.00 12.46 ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? 29.835 4.348   25.072  1.00 11.70 ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? 32.171 6.086   23.701  1.00 15.18 ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? 32.349 7.176   22.664  1.00 15.10 ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? 31.530 6.838   21.427  1.00 13.89 ? 21  PRO A CD  1 
ATOM   158  N  N   . ILE A 1 22  ? 28.742 5.813   23.722  1.00 11.21 ? 22  ILE A N   1 
ATOM   159  C  CA  . ILE A 1 22  ? 27.499 5.720   24.474  1.00 11.49 ? 22  ILE A CA  1 
ATOM   160  C  C   . ILE A 1 22  ? 26.897 4.313   24.355  1.00 10.70 ? 22  ILE A C   1 
ATOM   161  O  O   . ILE A 1 22  ? 25.964 3.987   25.107  1.00 11.04 ? 22  ILE A O   1 
ATOM   162  C  CB  . ILE A 1 22  ? 26.497 6.823   24.047  1.00 10.59 ? 22  ILE A CB  1 
ATOM   163  C  CG1 . ILE A 1 22  ? 25.437 7.103   25.123  1.00 11.76 ? 22  ILE A CG1 1 
ATOM   164  C  CG2 . ILE A 1 22  ? 25.909 6.530   22.662  1.00 10.51 ? 22  ILE A CG2 1 
ATOM   165  C  CD1 . ILE A 1 22  ? 24.442 8.230   24.772  1.00 12.55 ? 22  ILE A CD1 1 
ATOM   166  N  N   . ALA A 1 23  ? 27.441 3.471   23.460  1.00 10.94 ? 23  ALA A N   1 
ATOM   167  C  CA  . ALA A 1 23  ? 27.028 2.062   23.382  1.00 11.63 ? 23  ALA A CA  1 
ATOM   168  C  C   . ALA A 1 23  ? 27.071 1.345   24.725  1.00 12.98 ? 23  ALA A C   1 
ATOM   169  O  O   . ALA A 1 23  ? 26.357 0.343   24.927  1.00 11.84 ? 23  ALA A O   1 
ATOM   170  C  CB  . ALA A 1 23  ? 27.893 1.302   22.384  1.00 11.98 ? 23  ALA A CB  1 
ATOM   171  N  N   . LYS A 1 24  ? 28.000 1.767   25.604  1.00 13.59 ? 24  LYS A N   1 
ATOM   172  C  CA  . LYS A 1 24  ? 28.148 1.120   26.903  1.00 13.58 ? 24  LYS A CA  1 
ATOM   173  C  C   . LYS A 1 24  ? 27.543 2.022   27.970  1.00 14.67 ? 24  LYS A C   1 
ATOM   174  O  O   . LYS A 1 24  ? 27.927 1.915   29.135  1.00 15.61 ? 24  LYS A O   1 
ATOM   175  C  CB  . LYS A 1 24  ? 29.641 0.953   27.209  1.00 15.53 ? 24  LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 24  ? 30.336 0.018   26.231  1.00 17.24 ? 24  LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 24  ? 31.788 -0.235  26.622  1.00 22.75 ? 24  LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 24  ? 32.479 -1.156  25.627  1.00 23.18 ? 24  LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 24  ? 32.150 -2.584  25.880  1.00 25.32 ? 24  LYS A NZ  1 
ATOM   180  N  N   . GLY A 1 25  ? 26.559 2.859   27.587  1.00 13.10 ? 25  GLY A N   1 
ATOM   181  C  CA  . GLY A 1 25  ? 26.035 3.833   28.534  1.00 12.68 ? 25  GLY A CA  1 
ATOM   182  C  C   . GLY A 1 25  ? 24.975 3.290   29.497  1.00 12.27 ? 25  GLY A C   1 
ATOM   183  O  O   . GLY A 1 25  ? 24.734 2.078   29.622  1.00 13.45 ? 25  GLY A O   1 
ATOM   184  N  N   . GLU A 1 26  ? 24.347 4.226   30.224  1.00 12.55 ? 26  GLU A N   1 
ATOM   185  C  CA  . GLU A 1 26  ? 23.558 3.824   31.379  1.00 14.47 ? 26  GLU A CA  1 
ATOM   186  C  C   . GLU A 1 26  ? 22.113 3.498   30.991  1.00 13.04 ? 26  GLU A C   1 
ATOM   187  O  O   . GLU A 1 26  ? 21.358 2.989   31.830  1.00 11.79 ? 26  GLU A O   1 
ATOM   188  C  CB  . GLU A 1 26  ? 23.560 4.935   32.446  1.00 19.76 ? 26  GLU A CB  1 
ATOM   189  C  CG  . GLU A 1 26  ? 24.899 5.124   33.158  1.00 25.69 ? 26  GLU A CG  1 
ATOM   190  C  CD  . GLU A 1 26  ? 25.497 3.847   33.754  1.00 31.06 ? 26  GLU A CD  1 
ATOM   191  O  OE1 . GLU A 1 26  ? 24.813 3.175   34.576  1.00 34.58 ? 26  GLU A OE1 1 
ATOM   192  O  OE2 . GLU A 1 26  ? 26.628 3.475   33.346  1.00 33.30 ? 26  GLU A OE2 1 
ATOM   193  N  N   . ARG A 1 27  ? 21.697 3.815   29.755  1.00 10.66 ? 27  ARG A N   1 
ATOM   194  C  CA  . ARG A 1 27  ? 20.297 3.538   29.418  1.00 10.29 ? 27  ARG A CA  1 
ATOM   195  C  C   . ARG A 1 27  ? 20.170 3.087   27.950  1.00 9.01  ? 27  ARG A C   1 
ATOM   196  O  O   . ARG A 1 27  ? 19.449 3.688   27.129  1.00 8.22  ? 27  ARG A O   1 
ATOM   197  C  CB  . ARG A 1 27  ? 19.372 4.721   29.757  1.00 12.01 ? 27  ARG A CB  1 
ATOM   198  C  CG  . ARG A 1 27  ? 19.622 6.048   29.064  1.00 13.33 ? 27  ARG A CG  1 
ATOM   199  C  CD  . ARG A 1 27  ? 18.682 7.247   29.333  1.00 16.84 ? 27  ARG A CD  1 
ATOM   200  N  NE  . ARG A 1 27  ? 17.479 7.199   28.494  1.00 15.78 ? 27  ARG A NE  1 
ATOM   201  C  CZ  . ARG A 1 27  ? 16.610 8.195   28.368  1.00 16.21 ? 27  ARG A CZ  1 
ATOM   202  N  NH1 . ARG A 1 27  ? 16.801 9.327   29.025  1.00 13.73 ? 27  ARG A NH1 1 
ATOM   203  N  NH2 . ARG A 1 27  ? 15.553 8.058   27.587  1.00 14.62 ? 27  ARG A NH2 1 
ATOM   204  N  N   . GLN A 1 28  ? 20.916 2.022   27.610  1.00 8.20  ? 28  GLN A N   1 
ATOM   205  C  CA  . GLN A 1 28  ? 20.907 1.512   26.240  1.00 7.48  ? 28  GLN A CA  1 
ATOM   206  C  C   . GLN A 1 28  ? 19.745 0.541   26.002  1.00 7.42  ? 28  GLN A C   1 
ATOM   207  O  O   . GLN A 1 28  ? 19.290 -0.158  26.889  1.00 7.89  ? 28  GLN A O   1 
ATOM   208  C  CB  . GLN A 1 28  ? 22.253 0.815   25.991  1.00 8.35  ? 28  GLN A CB  1 
ATOM   209  C  CG  . GLN A 1 28  ? 23.377 1.860   25.856  1.00 7.30  ? 28  GLN A CG  1 
ATOM   210  C  CD  . GLN A 1 28  ? 23.210 2.662   24.573  1.00 7.58  ? 28  GLN A CD  1 
ATOM   211  O  OE1 . GLN A 1 28  ? 23.413 2.176   23.469  1.00 7.79  ? 28  GLN A OE1 1 
ATOM   212  N  NE2 . GLN A 1 28  ? 22.868 3.943   24.688  1.00 6.97  ? 28  GLN A NE2 1 
ATOM   213  N  N   . SER A 1 29  ? 19.314 0.481   24.740  1.00 7.04  ? 29  SER A N   1 
ATOM   214  C  CA  . SER A 1 29  ? 18.258 -0.405  24.277  1.00 6.41  ? 29  SER A CA  1 
ATOM   215  C  C   . SER A 1 29  ? 18.807 -1.276  23.156  1.00 6.38  ? 29  SER A C   1 
ATOM   216  O  O   . SER A 1 29  ? 19.742 -0.883  22.456  1.00 6.63  ? 29  SER A O   1 
ATOM   217  C  CB  . SER A 1 29  ? 17.125 0.422   23.700  1.00 6.13  ? 29  SER A CB  1 
ATOM   218  O  OG  . SER A 1 29  ? 16.509 1.159   24.775  1.00 6.27  ? 29  SER A OG  1 
ATOM   219  N  N   . PRO A 1 30  ? 18.187 -2.426  22.845  1.00 6.32  ? 30  PRO A N   1 
ATOM   220  C  CA  . PRO A 1 30  ? 17.047 -2.952  23.601  1.00 6.78  ? 30  PRO A CA  1 
ATOM   221  C  C   . PRO A 1 30  ? 17.440 -3.611  24.915  1.00 7.05  ? 30  PRO A C   1 
ATOM   222  O  O   . PRO A 1 30  ? 18.623 -3.640  25.260  1.00 6.98  ? 30  PRO A O   1 
ATOM   223  C  CB  . PRO A 1 30  ? 16.541 -3.989  22.578  1.00 6.42  ? 30  PRO A CB  1 
ATOM   224  C  CG  . PRO A 1 30  ? 17.838 -4.590  22.018  1.00 6.23  ? 30  PRO A CG  1 
ATOM   225  C  CD  . PRO A 1 30  ? 18.624 -3.321  21.748  1.00 6.39  ? 30  PRO A CD  1 
ATOM   226  N  N   . VAL A 1 31  ? 16.445 -4.236  25.576  1.00 7.54  ? 31  VAL A N   1 
ATOM   227  C  CA  . VAL A 1 31  ? 16.615 -4.966  26.824  1.00 7.63  ? 31  VAL A CA  1 
ATOM   228  C  C   . VAL A 1 31  ? 15.702 -6.191  26.806  1.00 8.22  ? 31  VAL A C   1 
ATOM   229  O  O   . VAL A 1 31  ? 14.719 -6.277  26.069  1.00 8.15  ? 31  VAL A O   1 
ATOM   230  C  CB  . VAL A 1 31  ? 16.292 -4.091  28.056  1.00 8.72  ? 31  VAL A CB  1 
ATOM   231  C  CG1 . VAL A 1 31  ? 17.251 -2.905  28.190  1.00 8.49  ? 31  VAL A CG1 1 
ATOM   232  C  CG2 . VAL A 1 31  ? 14.829 -3.679  28.100  1.00 8.27  ? 31  VAL A CG2 1 
ATOM   233  N  N   . ASP A 1 32  ? 16.072 -7.181  27.600  1.00 8.66  ? 32  ASP A N   1 
ATOM   234  C  CA  . ASP A 1 32  ? 15.172 -8.279  27.886  1.00 9.30  ? 32  ASP A CA  1 
ATOM   235  C  C   . ASP A 1 32  ? 14.110 -7.752  28.850  1.00 9.61  ? 32  ASP A C   1 
ATOM   236  O  O   . ASP A 1 32  ? 14.431 -7.100  29.846  1.00 9.61  ? 32  ASP A O   1 
ATOM   237  C  CB  . ASP A 1 32  ? 15.960 -9.441  28.496  1.00 10.12 ? 32  ASP A CB  1 
ATOM   238  C  CG  . ASP A 1 32  ? 15.012 -10.589 28.845  1.00 11.59 ? 32  ASP A CG  1 
ATOM   239  O  OD1 . ASP A 1 32  ? 14.298 -11.051 27.924  1.00 10.59 ? 32  ASP A OD1 1 
ATOM   240  O  OD2 . ASP A 1 32  ? 15.013 -11.038 30.045  1.00 11.75 ? 32  ASP A OD2 1 
ATOM   241  N  N   . ILE A 1 33  ? 12.843 -8.026  28.533  1.00 9.20  ? 33  ILE A N   1 
ATOM   242  C  CA  . ILE A 1 33  ? 11.718 -7.682  29.385  1.00 9.75  ? 33  ILE A CA  1 
ATOM   243  C  C   . ILE A 1 33  ? 11.415 -8.918  30.240  1.00 10.28 ? 33  ILE A C   1 
ATOM   244  O  O   . ILE A 1 33  ? 10.878 -9.924  29.769  1.00 11.71 ? 33  ILE A O   1 
ATOM   245  C  CB  . ILE A 1 33  ? 10.494 -7.254  28.568  1.00 9.52  ? 33  ILE A CB  1 
ATOM   246  C  CG1 . ILE A 1 33  ? 10.816 -5.999  27.742  1.00 9.17  ? 33  ILE A CG1 1 
ATOM   247  C  CG2 . ILE A 1 33  ? 9.360  -6.964  29.567  1.00 8.69  ? 33  ILE A CG2 1 
ATOM   248  C  CD1 . ILE A 1 33  ? 9.828  -5.734  26.579  1.00 9.58  ? 33  ILE A CD1 1 
ATOM   249  N  N   . ASP A 1 34  ? 11.860 -8.852  31.492  1.00 12.78 ? 34  ASP A N   1 
ATOM   250  C  CA  . ASP A 1 34  ? 11.569 -9.912  32.468  1.00 14.68 ? 34  ASP A CA  1 
ATOM   251  C  C   . ASP A 1 34  ? 10.161 -9.687  33.026  1.00 14.30 ? 34  ASP A C   1 
ATOM   252  O  O   . ASP A 1 34  ? 9.957  -8.764  33.801  1.00 16.45 ? 34  ASP A O   1 
ATOM   253  C  CB  . ASP A 1 34  ? 12.631 -9.934  33.575  1.00 16.55 ? 34  ASP A CB  1 
ATOM   254  C  CG  . ASP A 1 34  ? 12.457 -11.139 34.504  1.00 24.96 ? 34  ASP A CG  1 
ATOM   255  O  OD1 . ASP A 1 34  ? 11.390 -11.264 35.086  1.00 24.27 ? 34  ASP A OD1 1 
ATOM   256  O  OD2 . ASP A 1 34  ? 13.365 -11.987 34.557  1.00 32.11 ? 34  ASP A OD2 1 
ATOM   257  N  N   . THR A 1 35  ? 9.188  -10.504 32.615  1.00 15.50 ? 35  THR A N   1 
ATOM   258  C  CA  . THR A 1 35  ? 7.795  -10.116 32.769  1.00 17.39 ? 35  THR A CA  1 
ATOM   259  C  C   . THR A 1 35  ? 7.404  -10.261 34.226  1.00 17.74 ? 35  THR A C   1 
ATOM   260  O  O   . THR A 1 35  ? 6.411  -9.666  34.660  1.00 19.84 ? 35  THR A O   1 
ATOM   261  C  CB  . THR A 1 35  ? 6.844  -11.012 31.973  1.00 20.22 ? 35  THR A CB  1 
ATOM   262  O  OG1 . THR A 1 35  ? 7.044  -12.344 32.450  1.00 18.08 ? 35  THR A OG1 1 
ATOM   263  C  CG2 . THR A 1 35  ? 7.076  -10.947 30.479  1.00 17.29 ? 35  THR A CG2 1 
ATOM   264  N  N   . HIS A 1 36  ? 8.167  -11.109 34.935  1.00 17.71 ? 36  HIS A N   1 
ATOM   265  C  CA  . HIS A 1 36  ? 7.942  -11.344 36.351  1.00 19.37 ? 36  HIS A CA  1 
ATOM   266  C  C   . HIS A 1 36  ? 8.363  -10.149 37.208  1.00 21.45 ? 36  HIS A C   1 
ATOM   267  O  O   . HIS A 1 36  ? 7.652  -9.820  38.161  1.00 26.41 ? 36  HIS A O   1 
ATOM   268  C  CB  . HIS A 1 36  ? 8.445  -12.753 36.715  1.00 19.49 ? 36  HIS A CB  1 
ATOM   269  C  CG  . HIS A 1 36  ? 7.522  -13.777 36.136  1.00 19.11 ? 36  HIS A CG  1 
ATOM   270  N  ND1 . HIS A 1 36  ? 7.911  -14.706 35.200  1.00 20.52 ? 36  HIS A ND1 1 
ATOM   271  C  CD2 . HIS A 1 36  ? 6.191  -13.942 36.303  1.00 21.01 ? 36  HIS A CD2 1 
ATOM   272  C  CE1 . HIS A 1 36  ? 6.863  -15.422 34.851  1.00 19.24 ? 36  HIS A CE1 1 
ATOM   273  N  NE2 . HIS A 1 36  ? 5.806  -14.973 35.486  1.00 25.81 ? 36  HIS A NE2 1 
ATOM   274  N  N   . THR A 1 37  ? 9.405  -9.421  36.803  1.00 18.89 ? 37  THR A N   1 
ATOM   275  C  CA  . THR A 1 37  ? 9.963  -8.341  37.600  1.00 19.38 ? 37  THR A CA  1 
ATOM   276  C  C   . THR A 1 37  ? 9.579  -6.946  37.085  1.00 17.53 ? 37  THR A C   1 
ATOM   277  O  O   . THR A 1 37  ? 9.918  -5.946  37.708  1.00 16.27 ? 37  THR A O   1 
ATOM   278  C  CB  . THR A 1 37  ? 11.465 -8.504  37.827  1.00 24.20 ? 37  THR A CB  1 
ATOM   279  O  OG1 . THR A 1 37  ? 12.124 -8.416  36.575  1.00 25.80 ? 37  THR A OG1 1 
ATOM   280  C  CG2 . THR A 1 37  ? 11.852 -9.800  38.504  1.00 27.03 ? 37  THR A CG2 1 
ATOM   281  N  N   . ALA A 1 38  ? 8.832  -6.883  35.980  1.00 16.52 ? 38  ALA A N   1 
ATOM   282  C  CA  . ALA A 1 38  ? 8.232  -5.621  35.547  1.00 15.58 ? 38  ALA A CA  1 
ATOM   283  C  C   . ALA A 1 38  ? 7.188  -5.237  36.604  1.00 16.85 ? 38  ALA A C   1 
ATOM   284  O  O   . ALA A 1 38  ? 6.498  -6.085  37.143  1.00 18.78 ? 38  ALA A O   1 
ATOM   285  C  CB  . ALA A 1 38  ? 7.582  -5.830  34.205  1.00 16.90 ? 38  ALA A CB  1 
ATOM   286  N  N   . LYS A 1 39  ? 7.122  -3.961  36.944  1.00 17.06 ? 39  LYS A N   1 
ATOM   287  C  CA  . LYS A 1 39  ? 6.229  -3.479  37.990  1.00 18.71 ? 39  LYS A CA  1 
ATOM   288  C  C   . LYS A 1 39  ? 4.940  -2.987  37.322  1.00 18.66 ? 39  LYS A C   1 
ATOM   289  O  O   . LYS A 1 39  ? 4.946  -2.058  36.500  1.00 16.53 ? 39  LYS A O   1 
ATOM   290  C  CB  . LYS A 1 39  ? 6.953  -2.300  38.644  1.00 19.88 ? 39  LYS A CB  1 
ATOM   291  C  CG  . LYS A 1 39  ? 6.147  -1.457  39.632  1.00 21.98 ? 39  LYS A CG  1 
ATOM   292  C  CD  . LYS A 1 39  ? 6.035  -2.110  41.001  1.00 19.34 ? 39  LYS A CD  1 
ATOM   293  C  CE  . LYS A 1 39  ? 5.206  -1.258  41.944  1.00 26.08 ? 39  LYS A CE  1 
ATOM   294  N  NZ  . LYS A 1 39  ? 4.860  -2.027  43.156  1.00 28.06 ? 39  LYS A NZ  1 
ATOM   295  N  N   . TYR A 1 40  ? 3.814  -3.568  37.714  1.00 19.63 ? 40  TYR A N   1 
ATOM   296  C  CA  . TYR A 1 40  ? 2.537  -2.980  37.333  1.00 20.56 ? 40  TYR A CA  1 
ATOM   297  C  C   . TYR A 1 40  ? 2.374  -1.598  37.976  1.00 20.51 ? 40  TYR A C   1 
ATOM   298  O  O   . TYR A 1 40  ? 2.546  -1.420  39.198  1.00 17.15 ? 40  TYR A O   1 
ATOM   299  C  CB  . TYR A 1 40  ? 1.380  -3.928  37.664  1.00 23.44 ? 40  TYR A CB  1 
ATOM   300  C  CG  . TYR A 1 40  ? 0.033  -3.267  37.541  1.00 23.94 ? 40  TYR A CG  1 
ATOM   301  C  CD1 . TYR A 1 40  ? -0.431 -2.830  36.303  1.00 24.01 ? 40  TYR A CD1 1 
ATOM   302  C  CD2 . TYR A 1 40  ? -0.771 -3.062  38.657  1.00 29.97 ? 40  TYR A CD2 1 
ATOM   303  C  CE1 . TYR A 1 40  ? -1.666 -2.231  36.160  1.00 24.75 ? 40  TYR A CE1 1 
ATOM   304  C  CE2 . TYR A 1 40  ? -2.009 -2.436  38.537  1.00 27.32 ? 40  TYR A CE2 1 
ATOM   305  C  CZ  . TYR A 1 40  ? -2.450 -2.033  37.285  1.00 29.47 ? 40  TYR A CZ  1 
ATOM   306  O  OH  . TYR A 1 40  ? -3.646 -1.409  37.139  1.00 31.95 ? 40  TYR A OH  1 
ATOM   307  N  N   . ASP A 1 41  ? 1.990  -0.621  37.129  1.00 19.21 ? 41  ASP A N   1 
ATOM   308  C  CA  . ASP A 1 41  ? 1.823  0.748   37.588  1.00 21.89 ? 41  ASP A CA  1 
ATOM   309  C  C   . ASP A 1 41  ? 0.400  1.166   37.255  1.00 25.77 ? 41  ASP A C   1 
ATOM   310  O  O   . ASP A 1 41  ? 0.080  1.416   36.095  1.00 24.18 ? 41  ASP A O   1 
ATOM   311  C  CB  . ASP A 1 41  ? 2.868  1.708   37.029  1.00 23.62 ? 41  ASP A CB  1 
ATOM   312  C  CG  . ASP A 1 41  ? 2.678  3.137   37.518  1.00 28.64 ? 41  ASP A CG  1 
ATOM   313  O  OD1 . ASP A 1 41  ? 1.682  3.394   38.225  1.00 28.24 ? 41  ASP A OD1 1 
ATOM   314  O  OD2 . ASP A 1 41  ? 3.525  3.977   37.172  1.00 29.72 ? 41  ASP A OD2 1 
ATOM   315  N  N   . PRO A 1 42  ? -0.513 1.168   38.253  1.00 29.34 ? 42  PRO A N   1 
ATOM   316  C  CA  . PRO A 1 42  ? -1.926 1.450   37.996  1.00 28.76 ? 42  PRO A CA  1 
ATOM   317  C  C   . PRO A 1 42  ? -2.104 2.914   37.626  1.00 27.84 ? 42  PRO A C   1 
ATOM   318  O  O   . PRO A 1 42  ? -3.162 3.273   37.129  1.00 32.30 ? 42  PRO A O   1 
ATOM   319  C  CB  . PRO A 1 42  ? -2.598 1.150   39.350  1.00 28.88 ? 42  PRO A CB  1 
ATOM   320  C  CG  . PRO A 1 42  ? -1.488 1.477   40.338  1.00 29.99 ? 42  PRO A CG  1 
ATOM   321  C  CD  . PRO A 1 42  ? -0.237 0.922   39.682  1.00 33.07 ? 42  PRO A CD  1 
ATOM   322  N  N   . SER A 1 43  ? -1.068 3.743   37.837  1.00 27.73 ? 43  SER A N   1 
ATOM   323  C  CA  . SER A 1 43  ? -1.141 5.142   37.426  1.00 29.64 ? 43  SER A CA  1 
ATOM   324  C  C   . SER A 1 43  ? -0.834 5.367   35.932  1.00 27.36 ? 43  SER A C   1 
ATOM   325  O  O   . SER A 1 43  ? -1.097 6.442   35.390  1.00 26.79 ? 43  SER A O   1 
ATOM   326  C  CB  . SER A 1 43  ? -0.285 6.012   38.303  1.00 34.68 ? 43  SER A CB  1 
ATOM   327  O  OG  . SER A 1 43  ? 1.068  6.004   37.890  1.00 39.68 ? 43  SER A OG  1 
ATOM   328  N  N   . LEU A 1 44  ? -0.270 4.371   35.238  1.00 22.08 ? 44  LEU A N   1 
ATOM   329  C  CA  . LEU A 1 44  ? -0.030 4.532   33.807  1.00 19.23 ? 44  LEU A CA  1 
ATOM   330  C  C   . LEU A 1 44  ? -1.357 4.637   33.055  1.00 20.41 ? 44  LEU A C   1 
ATOM   331  O  O   . LEU A 1 44  ? -2.257 3.830   33.265  1.00 21.67 ? 44  LEU A O   1 
ATOM   332  C  CB  . LEU A 1 44  ? 0.739  3.319   33.278  1.00 17.74 ? 44  LEU A CB  1 
ATOM   333  C  CG  . LEU A 1 44  ? 2.238  3.337   33.549  1.00 16.57 ? 44  LEU A CG  1 
ATOM   334  C  CD1 . LEU A 1 44  ? 2.853  1.973   33.200  1.00 16.62 ? 44  LEU A CD1 1 
ATOM   335  C  CD2 . LEU A 1 44  ? 2.884  4.460   32.755  1.00 16.79 ? 44  LEU A CD2 1 
ATOM   336  N  N   . LYS A 1 45  ? -1.432 5.587   32.118  1.00 19.80 ? 45  LYS A N   1 
ATOM   337  C  CA  . LYS A 1 45  ? -2.643 5.824   31.337  1.00 21.57 ? 45  LYS A CA  1 
ATOM   338  C  C   . LYS A 1 45  ? -2.655 4.914   30.123  1.00 19.55 ? 45  LYS A C   1 
ATOM   339  O  O   . LYS A 1 45  ? -1.593 4.444   29.700  1.00 17.54 ? 45  LYS A O   1 
ATOM   340  C  CB  . LYS A 1 45  ? -2.650 7.253   30.801  1.00 23.70 ? 45  LYS A CB  1 
ATOM   341  C  CG  . LYS A 1 45  ? -2.654 8.330   31.881  1.00 30.41 ? 45  LYS A CG  1 
ATOM   342  C  CD  . LYS A 1 45  ? -2.646 9.752   31.333  1.00 36.86 ? 45  LYS A CD  1 
ATOM   343  C  CE  . LYS A 1 45  ? -2.022 10.755  32.291  1.00 42.98 ? 45  LYS A CE  1 
ATOM   344  N  NZ  . LYS A 1 45  ? -2.686 10.713  33.617  1.00 43.29 ? 45  LYS A NZ  1 
ATOM   345  N  N   . PRO A 1 46  ? -3.848 4.639   29.531  1.00 17.21 ? 46  PRO A N   1 
ATOM   346  C  CA  . PRO A 1 46  ? -3.918 3.996   28.221  1.00 17.26 ? 46  PRO A CA  1 
ATOM   347  C  C   . PRO A 1 46  ? -3.066 4.773   27.219  1.00 15.14 ? 46  PRO A C   1 
ATOM   348  O  O   . PRO A 1 46  ? -3.013 6.003   27.274  1.00 14.44 ? 46  PRO A O   1 
ATOM   349  C  CB  . PRO A 1 46  ? -5.395 4.202   27.816  1.00 19.00 ? 46  PRO A CB  1 
ATOM   350  C  CG  . PRO A 1 46  ? -6.141 4.240   29.127  1.00 19.08 ? 46  PRO A CG  1 
ATOM   351  C  CD  . PRO A 1 46  ? -5.191 4.916   30.111  1.00 18.66 ? 46  PRO A CD  1 
ATOM   352  N  N   . LEU A 1 47  ? -2.451 4.053   26.272  1.00 15.89 ? 47  LEU A N   1 
ATOM   353  C  CA  . LEU A 1 47  ? -1.748 4.711   25.187  1.00 15.48 ? 47  LEU A CA  1 
ATOM   354  C  C   . LEU A 1 47  ? -2.792 5.300   24.245  1.00 16.88 ? 47  LEU A C   1 
ATOM   355  O  O   . LEU A 1 47  ? -3.841 4.678   24.041  1.00 16.72 ? 47  LEU A O   1 
ATOM   356  C  CB  . LEU A 1 47  ? -0.974 3.609   24.458  1.00 17.66 ? 47  LEU A CB  1 
ATOM   357  C  CG  . LEU A 1 47  ? 0.153  3.989   23.519  1.00 20.59 ? 47  LEU A CG  1 
ATOM   358  C  CD1 . LEU A 1 47  ? 1.195  4.874   24.209  1.00 21.24 ? 47  LEU A CD1 1 
ATOM   359  C  CD2 . LEU A 1 47  ? 0.764  2.688   22.997  1.00 21.05 ? 47  LEU A CD2 1 
ATOM   360  N  N   . SER A 1 48  ? -2.496 6.482   23.696  1.00 13.34 ? 48  SER A N   1 
ATOM   361  C  CA  . SER A 1 48  ? -3.321 7.135   22.689  1.00 15.81 ? 48  SER A CA  1 
ATOM   362  C  C   . SER A 1 48  ? -2.580 7.142   21.363  1.00 15.54 ? 48  SER A C   1 
ATOM   363  O  O   . SER A 1 48  ? -1.628 7.906   21.180  1.00 14.49 ? 48  SER A O   1 
ATOM   364  C  CB  . SER A 1 48  ? -3.714 8.523   23.105  1.00 16.70 ? 48  SER A CB  1 
ATOM   365  O  OG  . SER A 1 48  ? -4.388 9.179   22.037  1.00 19.40 ? 48  SER A OG  1 
ATOM   366  N  N   . VAL A 1 49  ? -3.063 6.317   20.433  1.00 15.34 ? 49  VAL A N   1 
ATOM   367  C  CA  . VAL A 1 49  ? -2.524 6.275   19.083  1.00 17.89 ? 49  VAL A CA  1 
ATOM   368  C  C   . VAL A 1 49  ? -3.507 6.957   18.125  1.00 19.59 ? 49  VAL A C   1 
ATOM   369  O  O   . VAL A 1 49  ? -4.576 6.422   17.842  1.00 19.83 ? 49  VAL A O   1 
ATOM   370  C  CB  . VAL A 1 49  ? -2.285 4.811   18.672  1.00 19.51 ? 49  VAL A CB  1 
ATOM   371  C  CG1 . VAL A 1 49  ? -1.695 4.717   17.266  1.00 22.10 ? 49  VAL A CG1 1 
ATOM   372  C  CG2 . VAL A 1 49  ? -1.394 4.088   19.692  1.00 19.14 ? 49  VAL A CG2 1 
ATOM   373  N  N   . SER A 1 50  ? -3.163 8.139   17.612  1.00 16.46 ? 50  SER A N   1 
ATOM   374  C  CA  . SER A 1 50  ? -4.060 8.864   16.716  1.00 19.07 ? 50  SER A CA  1 
ATOM   375  C  C   . SER A 1 50  ? -3.454 8.908   15.329  1.00 17.82 ? 50  SER A C   1 
ATOM   376  O  O   . SER A 1 50  ? -2.743 9.845   15.020  1.00 16.27 ? 50  SER A O   1 
ATOM   377  C  CB  . SER A 1 50  ? -4.349 10.276  17.168  1.00 21.43 ? 50  SER A CB  1 
ATOM   378  O  OG  . SER A 1 50  ? -4.949 10.244  18.435  1.00 26.26 ? 50  SER A OG  1 
ATOM   379  N  N   . TYR A 1 51  ? -3.733 7.883   14.522  1.00 19.46 ? 51  TYR A N   1 
ATOM   380  C  CA  . TYR A 1 51  ? -3.099 7.762   13.217  1.00 17.50 ? 51  TYR A CA  1 
ATOM   381  C  C   . TYR A 1 51  ? -4.088 7.981   12.064  1.00 19.09 ? 51  TYR A C   1 
ATOM   382  O  O   . TYR A 1 51  ? -3.743 7.767   10.911  1.00 17.04 ? 51  TYR A O   1 
ATOM   383  C  CB  . TYR A 1 51  ? -2.453 6.377   13.063  1.00 15.63 ? 51  TYR A CB  1 
ATOM   384  C  CG  . TYR A 1 51  ? -1.186 6.057   13.833  1.00 15.16 ? 51  TYR A CG  1 
ATOM   385  C  CD1 . TYR A 1 51  ? -0.435 7.025   14.483  1.00 13.56 ? 51  TYR A CD1 1 
ATOM   386  C  CD2 . TYR A 1 51  ? -0.701 4.756   13.844  1.00 12.90 ? 51  TYR A CD2 1 
ATOM   387  C  CE1 . TYR A 1 51  ? 0.709  6.683   15.198  1.00 11.94 ? 51  TYR A CE1 1 
ATOM   388  C  CE2 . TYR A 1 51  ? 0.467  4.397   14.510  1.00 13.16 ? 51  TYR A CE2 1 
ATOM   389  C  CZ  . TYR A 1 51  ? 1.189  5.384   15.184  1.00 12.88 ? 51  TYR A CZ  1 
ATOM   390  O  OH  . TYR A 1 51  ? 2.364  5.031   15.815  1.00 11.69 ? 51  TYR A OH  1 
ATOM   391  N  N   . ASP A 1 52  ? -5.310 8.441   12.370  1.00 20.32 ? 52  ASP A N   1 
ATOM   392  C  CA  . ASP A 1 52  ? -6.347 8.685   11.373  1.00 24.78 ? 52  ASP A CA  1 
ATOM   393  C  C   . ASP A 1 52  ? -5.867 9.579   10.219  1.00 22.86 ? 52  ASP A C   1 
ATOM   394  O  O   . ASP A 1 52  ? -6.209 9.312   9.070   1.00 24.60 ? 52  ASP A O   1 
ATOM   395  C  CB  . ASP A 1 52  ? -7.634 9.182   12.045  1.00 27.29 ? 52  ASP A CB  1 
ATOM   396  C  CG  . ASP A 1 52  ? -7.396 10.189  13.169  1.00 35.67 ? 52  ASP A CG  1 
ATOM   397  O  OD1 . ASP A 1 52  ? -6.781 9.810   14.261  1.00 34.12 ? 52  ASP A OD1 1 
ATOM   398  O  OD2 . ASP A 1 52  ? -7.787 11.368  12.958  1.00 42.43 ? 52  ASP A OD2 1 
ATOM   399  N  N   . GLN A 1 53  ? -5.068 10.612  10.489  1.00 22.17 ? 53  GLN A N   1 
ATOM   400  C  CA  . GLN A 1 53  ? -4.710 11.525  9.406   1.00 24.49 ? 53  GLN A CA  1 
ATOM   401  C  C   . GLN A 1 53  ? -3.264 11.335  8.931   1.00 20.19 ? 53  GLN A C   1 
ATOM   402  O  O   . GLN A 1 53  ? -2.676 12.255  8.349   1.00 19.70 ? 53  GLN A O   1 
ATOM   403  C  CB  . GLN A 1 53  ? -5.000 12.971  9.816   1.00 27.79 ? 53  GLN A CB  1 
ATOM   404  C  CG  . GLN A 1 53  ? -6.494 13.325  9.796   1.00 34.74 ? 53  GLN A CG  1 
ATOM   405  C  CD  . GLN A 1 53  ? -7.254 12.798  8.596   1.00 42.24 ? 53  GLN A CD  1 
ATOM   406  O  OE1 . GLN A 1 53  ? -6.860 12.959  7.424   1.00 42.50 ? 53  GLN A OE1 1 
ATOM   407  N  NE2 . GLN A 1 53  ? -8.374 12.145  8.879   1.00 38.41 ? 53  GLN A NE2 1 
ATOM   408  N  N   . ALA A 1 54  ? -2.708 10.129  9.113   1.00 17.41 ? 54  ALA A N   1 
ATOM   409  C  CA  . ALA A 1 54  ? -1.317 9.890   8.758   1.00 14.39 ? 54  ALA A CA  1 
ATOM   410  C  C   . ALA A 1 54  ? -1.106 10.115  7.250   1.00 15.92 ? 54  ALA A C   1 
ATOM   411  O  O   . ALA A 1 54  ? -1.943 9.726   6.404   1.00 13.92 ? 54  ALA A O   1 
ATOM   412  C  CB  . ALA A 1 54  ? -0.878 8.507   9.213   1.00 15.09 ? 54  ALA A CB  1 
ATOM   413  N  N   . THR A 1 55  ? 0.011  10.770  6.924   1.00 13.17 ? 55  THR A N   1 
ATOM   414  C  CA  . THR A 1 55  ? 0.423  10.937  5.536   1.00 13.90 ? 55  THR A CA  1 
ATOM   415  C  C   . THR A 1 55  ? 1.755  10.258  5.274   1.00 13.50 ? 55  THR A C   1 
ATOM   416  O  O   . THR A 1 55  ? 2.807  10.842  5.513   1.00 12.26 ? 55  THR A O   1 
ATOM   417  C  CB  . THR A 1 55  ? 0.608  12.420  5.169   1.00 14.75 ? 55  THR A CB  1 
ATOM   418  O  OG1 . THR A 1 55  ? -0.713 12.930  5.258   1.00 18.59 ? 55  THR A OG1 1 
ATOM   419  C  CG2 . THR A 1 55  ? 1.078  12.568  3.733   1.00 16.56 ? 55  THR A CG2 1 
ATOM   420  N  N   . SER A 1 56  ? 1.737  9.020   4.735   1.00 13.83 ? 56  SER A N   1 
ATOM   421  C  CA  . SER A 1 56  ? 2.998  8.442   4.338   1.00 14.34 ? 56  SER A CA  1 
ATOM   422  C  C   . SER A 1 56  ? 3.496  9.100   3.050   1.00 15.70 ? 56  SER A C   1 
ATOM   423  O  O   . SER A 1 56  ? 2.700  9.589   2.242   1.00 17.89 ? 56  SER A O   1 
ATOM   424  C  CB  . SER A 1 56  ? 2.896  6.923   4.207   1.00 14.01 ? 56  SER A CB  1 
ATOM   425  O  OG  . SER A 1 56  ? 1.969  6.565   3.173   1.00 15.51 ? 56  SER A OG  1 
ATOM   426  N  N   . LEU A 1 57  ? 4.810  9.152   2.878   1.00 14.11 ? 57  LEU A N   1 
ATOM   427  C  CA  . LEU A 1 57  ? 5.361  9.809   1.698   1.00 16.52 ? 57  LEU A CA  1 
ATOM   428  C  C   . LEU A 1 57  ? 6.187  8.855   0.836   1.00 16.58 ? 57  LEU A C   1 
ATOM   429  O  O   . LEU A 1 57  ? 6.125  8.889   -0.394  1.00 15.99 ? 57  LEU A O   1 
ATOM   430  C  CB  . LEU A 1 57  ? 6.247  10.978  2.130   1.00 17.77 ? 57  LEU A CB  1 
ATOM   431  C  CG  . LEU A 1 57  ? 5.487  12.099  2.839   1.00 20.62 ? 57  LEU A CG  1 
ATOM   432  C  CD1 . LEU A 1 57  ? 6.487  13.168  3.253   1.00 19.99 ? 57  LEU A CD1 1 
ATOM   433  C  CD2 . LEU A 1 57  ? 4.397  12.690  1.937   1.00 22.40 ? 57  LEU A CD2 1 
ATOM   434  N  N   . ARG A 1 58  ? 7.046  8.073   1.481   1.00 15.06 ? 58  ARG A N   1 
ATOM   435  C  CA  . ARG A 1 58  ? 8.115  7.420   0.769   1.00 15.17 ? 58  ARG A CA  1 
ATOM   436  C  C   . ARG A 1 58  ? 8.582  6.231   1.596   1.00 15.24 ? 58  ARG A C   1 
ATOM   437  O  O   . ARG A 1 58  ? 8.405  6.223   2.827   1.00 13.33 ? 58  ARG A O   1 
ATOM   438  C  CB  . ARG A 1 58  ? 9.238  8.448   0.666   1.00 17.91 ? 58  ARG A CB  1 
ATOM   439  C  CG  . ARG A 1 58  ? 10.337 8.094   -0.308  1.00 22.57 ? 58  ARG A CG  1 
ATOM   440  C  CD  . ARG A 1 58  ? 11.110 9.396   -0.431  1.00 26.20 ? 58  ARG A CD  1 
ATOM   441  N  NE  . ARG A 1 58  ? 11.932 9.350   0.765   1.00 26.57 ? 58  ARG A NE  1 
ATOM   442  C  CZ  . ARG A 1 58  ? 13.257 9.434   0.770   1.00 26.52 ? 58  ARG A CZ  1 
ATOM   443  N  NH1 . ARG A 1 58  ? 13.917 9.569   -0.368  1.00 26.04 ? 58  ARG A NH1 1 
ATOM   444  N  NH2 . ARG A 1 58  ? 13.919 9.382   1.912   1.00 26.32 ? 58  ARG A NH2 1 
ATOM   445  N  N   . ILE A 1 59  ? 9.170  5.257   0.887   1.00 13.51 ? 59  ILE A N   1 
ATOM   446  C  CA  . ILE A 1 59  ? 9.810  4.119   1.531   1.00 14.18 ? 59  ILE A CA  1 
ATOM   447  C  C   . ILE A 1 59  ? 11.244 4.067   1.024   1.00 14.79 ? 59  ILE A C   1 
ATOM   448  O  O   . ILE A 1 59  ? 11.507 4.227   -0.182  1.00 14.85 ? 59  ILE A O   1 
ATOM   449  C  CB  . ILE A 1 59  ? 9.026  2.801   1.308   1.00 12.68 ? 59  ILE A CB  1 
ATOM   450  C  CG1 . ILE A 1 59  ? 9.623  1.645   2.137   1.00 13.42 ? 59  ILE A CG1 1 
ATOM   451  C  CG2 . ILE A 1 59  ? 8.953  2.436   -0.178  1.00 13.05 ? 59  ILE A CG2 1 
ATOM   452  C  CD1 . ILE A 1 59  ? 8.841  0.305   2.002   1.00 12.81 ? 59  ILE A CD1 1 
ATOM   453  N  N   . LEU A 1 60  ? 12.197 3.865   1.951   1.00 14.85 ? 60  LEU A N   1 
ATOM   454  C  CA  . LEU A 1 60  ? 13.610 3.995   1.662   1.00 14.94 ? 60  LEU A CA  1 
ATOM   455  C  C   . LEU A 1 60  ? 14.386 2.809   2.225   1.00 14.16 ? 60  LEU A C   1 
ATOM   456  O  O   . LEU A 1 60  ? 14.207 2.444   3.398   1.00 13.84 ? 60  LEU A O   1 
ATOM   457  C  CB  . LEU A 1 60  ? 14.099 5.284   2.358   1.00 17.39 ? 60  LEU A CB  1 
ATOM   458  C  CG  . LEU A 1 60  ? 15.611 5.482   2.321   1.00 18.94 ? 60  LEU A CG  1 
ATOM   459  C  CD1 . LEU A 1 60  ? 16.116 5.679   0.895   1.00 21.70 ? 60  LEU A CD1 1 
ATOM   460  C  CD2 . LEU A 1 60  ? 16.091 6.597   3.261   1.00 18.67 ? 60  LEU A CD2 1 
ATOM   461  N  N   . ASN A 1 61  ? 15.285 2.244   1.412   1.00 12.12 ? 61  ASN A N   1 
ATOM   462  C  CA  . ASN A 1 61  ? 16.295 1.332   1.943   1.00 13.99 ? 61  ASN A CA  1 
ATOM   463  C  C   . ASN A 1 61  ? 17.537 2.145   2.310   1.00 15.12 ? 61  ASN A C   1 
ATOM   464  O  O   . ASN A 1 61  ? 18.192 2.709   1.431   1.00 15.87 ? 61  ASN A O   1 
ATOM   465  C  CB  . ASN A 1 61  ? 16.649 0.255   0.915   1.00 13.60 ? 61  ASN A CB  1 
ATOM   466  C  CG  . ASN A 1 61  ? 17.721 -0.728  1.307   1.00 13.92 ? 61  ASN A CG  1 
ATOM   467  O  OD1 . ASN A 1 61  ? 18.550 -0.466  2.178   1.00 16.33 ? 61  ASN A OD1 1 
ATOM   468  N  ND2 . ASN A 1 61  ? 17.737 -1.897  0.667   1.00 14.21 ? 61  ASN A ND2 1 
ATOM   469  N  N   . ASN A 1 62  ? 17.903 2.146   3.602   1.00 14.93 ? 62  ASN A N   1 
ATOM   470  C  CA  . ASN A 1 62  ? 18.966 3.032   4.062   1.00 15.14 ? 62  ASN A CA  1 
ATOM   471  C  C   . ASN A 1 62  ? 20.204 2.201   4.348   1.00 16.72 ? 62  ASN A C   1 
ATOM   472  O  O   . ASN A 1 62  ? 21.155 2.673   4.996   1.00 19.50 ? 62  ASN A O   1 
ATOM   473  C  CB  . ASN A 1 62  ? 18.559 3.849   5.299   1.00 17.20 ? 62  ASN A CB  1 
ATOM   474  C  CG  . ASN A 1 62  ? 18.330 2.964   6.512   1.00 15.96 ? 62  ASN A CG  1 
ATOM   475  O  OD1 . ASN A 1 62  ? 18.510 1.736   6.457   1.00 15.20 ? 62  ASN A OD1 1 
ATOM   476  N  ND2 . ASN A 1 62  ? 18.008 3.579   7.630   1.00 18.16 ? 62  ASN A ND2 1 
ATOM   477  N  N   . GLY A 1 63  ? 20.221 0.976   3.815   1.00 13.65 ? 63  GLY A N   1 
ATOM   478  C  CA  . GLY A 1 63  ? 21.351 0.092   3.973   1.00 13.34 ? 63  GLY A CA  1 
ATOM   479  C  C   . GLY A 1 63  ? 21.394 -0.616  5.326   1.00 13.97 ? 63  GLY A C   1 
ATOM   480  O  O   . GLY A 1 63  ? 22.294 -1.419  5.519   1.00 12.68 ? 63  GLY A O   1 
ATOM   481  N  N   . HIS A 1 64  ? 20.422 -0.337  6.225   1.00 13.76 ? 64  HIS A N   1 
ATOM   482  C  CA  . HIS A 1 64  ? 20.373 -1.009  7.528   1.00 14.30 ? 64  HIS A CA  1 
ATOM   483  C  C   . HIS A 1 64  ? 19.008 -1.671  7.701   1.00 14.67 ? 64  HIS A C   1 
ATOM   484  O  O   . HIS A 1 64  ? 18.910 -2.764  8.279   1.00 17.39 ? 64  HIS A O   1 
ATOM   485  C  CB  . HIS A 1 64  ? 20.575 -0.021  8.681   1.00 15.64 ? 64  HIS A CB  1 
ATOM   486  C  CG  . HIS A 1 64  ? 21.821 0.786   8.489   1.00 18.35 ? 64  HIS A CG  1 
ATOM   487  N  ND1 . HIS A 1 64  ? 23.087 0.200   8.598   1.00 19.69 ? 64  HIS A ND1 1 
ATOM   488  C  CD2 . HIS A 1 64  ? 22.016 2.086   8.192   1.00 18.45 ? 64  HIS A CD2 1 
ATOM   489  C  CE1 . HIS A 1 64  ? 24.015 1.113   8.395   1.00 18.43 ? 64  HIS A CE1 1 
ATOM   490  N  NE2 . HIS A 1 64  ? 23.395 2.268   8.141   1.00 18.50 ? 64  HIS A NE2 1 
ATOM   491  N  N   . ALA A 1 65  ? 17.967 -1.008  7.188   1.00 13.10 ? 65  ALA A N   1 
ATOM   492  C  CA  . ALA A 1 65  ? 16.603 -1.488  7.246   1.00 12.68 ? 65  ALA A CA  1 
ATOM   493  C  C   . ALA A 1 65  ? 15.860 -0.749  6.137   1.00 11.92 ? 65  ALA A C   1 
ATOM   494  O  O   . ALA A 1 65  ? 16.535 -0.102  5.305   1.00 12.30 ? 65  ALA A O   1 
ATOM   495  C  CB  . ALA A 1 65  ? 15.997 -1.221  8.628   1.00 10.99 ? 65  ALA A CB  1 
ATOM   496  N  N   . PHE A 1 66  ? 14.523 -0.871  6.084   1.00 11.31 ? 66  PHE A N   1 
ATOM   497  C  CA  . PHE A 1 66  ? 13.774 0.071   5.253   1.00 11.96 ? 66  PHE A CA  1 
ATOM   498  C  C   . PHE A 1 66  ? 12.903 0.963   6.123   1.00 11.98 ? 66  PHE A C   1 
ATOM   499  O  O   . PHE A 1 66  ? 12.306 0.500   7.102   1.00 12.19 ? 66  PHE A O   1 
ATOM   500  C  CB  . PHE A 1 66  ? 12.952 -0.630  4.159   1.00 12.26 ? 66  PHE A CB  1 
ATOM   501  C  CG  . PHE A 1 66  ? 11.882 -1.564  4.686   1.00 12.30 ? 66  PHE A CG  1 
ATOM   502  C  CD1 . PHE A 1 66  ? 10.591 -1.123  4.981   1.00 12.84 ? 66  PHE A CD1 1 
ATOM   503  C  CD2 . PHE A 1 66  ? 12.182 -2.912  4.854   1.00 13.44 ? 66  PHE A CD2 1 
ATOM   504  C  CE1 . PHE A 1 66  ? 9.638  -2.003  5.485   1.00 11.79 ? 66  PHE A CE1 1 
ATOM   505  C  CE2 . PHE A 1 66  ? 11.232 -3.780  5.369   1.00 12.58 ? 66  PHE A CE2 1 
ATOM   506  C  CZ  . PHE A 1 66  ? 9.973  -3.340  5.669   1.00 11.46 ? 66  PHE A CZ  1 
ATOM   507  N  N   . ASN A 1 67  ? 12.821 2.252   5.772   1.00 12.04 ? 67  ASN A N   1 
ATOM   508  C  CA  . ASN A 1 67  ? 12.013 3.163   6.549   1.00 12.14 ? 67  ASN A CA  1 
ATOM   509  C  C   . ASN A 1 67  ? 10.808 3.593   5.724   1.00 11.93 ? 67  ASN A C   1 
ATOM   510  O  O   . ASN A 1 67  ? 10.965 4.014   4.587   1.00 13.09 ? 67  ASN A O   1 
ATOM   511  C  CB  . ASN A 1 67  ? 12.762 4.462   6.883   1.00 14.07 ? 67  ASN A CB  1 
ATOM   512  C  CG  . ASN A 1 67  ? 13.920 4.263   7.828   1.00 16.18 ? 67  ASN A CG  1 
ATOM   513  O  OD1 . ASN A 1 67  ? 14.019 3.211   8.438   1.00 15.75 ? 67  ASN A OD1 1 
ATOM   514  N  ND2 . ASN A 1 67  ? 14.802 5.260   7.956   1.00 16.96 ? 67  ASN A ND2 1 
ATOM   515  N  N   . VAL A 1 68  ? 9.619  3.557   6.308   1.00 11.40 ? 68  VAL A N   1 
ATOM   516  C  CA  . VAL A 1 68  ? 8.489  4.248   5.705   1.00 12.27 ? 68  VAL A CA  1 
ATOM   517  C  C   . VAL A 1 68  ? 8.351  5.589   6.434   1.00 15.03 ? 68  VAL A C   1 
ATOM   518  O  O   . VAL A 1 68  ? 8.124  5.615   7.646   1.00 11.80 ? 68  VAL A O   1 
ATOM   519  C  CB  . VAL A 1 68  ? 7.216  3.403   5.848   1.00 13.13 ? 68  VAL A CB  1 
ATOM   520  C  CG1 . VAL A 1 68  ? 5.968  4.225   5.464   1.00 14.50 ? 68  VAL A CG1 1 
ATOM   521  C  CG2 . VAL A 1 68  ? 7.334  2.161   4.970   1.00 14.80 ? 68  VAL A CG2 1 
ATOM   522  N  N   . GLU A 1 69  ? 8.433  6.689   5.681   1.00 15.32 ? 69  GLU A N   1 
ATOM   523  C  CA  . GLU A 1 69  ? 8.500  8.024   6.260   1.00 16.81 ? 69  GLU A CA  1 
ATOM   524  C  C   . GLU A 1 69  ? 7.193  8.752   6.032   1.00 15.89 ? 69  GLU A C   1 
ATOM   525  O  O   . GLU A 1 69  ? 6.458  8.482   5.060   1.00 16.71 ? 69  GLU A O   1 
ATOM   526  C  CB  . GLU A 1 69  ? 9.529  8.848   5.520   1.00 19.37 ? 69  GLU A CB  1 
ATOM   527  C  CG  . GLU A 1 69  ? 10.841 8.138   5.455   1.00 23.04 ? 69  GLU A CG  1 
ATOM   528  C  CD  . GLU A 1 69  ? 11.693 8.662   4.323   1.00 26.83 ? 69  GLU A CD  1 
ATOM   529  O  OE1 . GLU A 1 69  ? 11.094 9.194   3.346   1.00 31.56 ? 69  GLU A OE1 1 
ATOM   530  O  OE2 . GLU A 1 69  ? 12.942 8.572   4.442   1.00 28.70 ? 69  GLU A OE2 1 
ATOM   531  N  N   . PHE A 1 70  ? 6.907  9.634   6.990   1.00 13.50 ? 70  PHE A N   1 
ATOM   532  C  CA  . PHE A 1 70  ? 5.623  10.301  7.081   1.00 12.27 ? 70  PHE A CA  1 
ATOM   533  C  C   . PHE A 1 70  ? 5.867  11.807  7.065   1.00 12.50 ? 70  PHE A C   1 
ATOM   534  O  O   . PHE A 1 70  ? 6.938  12.249  7.418   1.00 13.13 ? 70  PHE A O   1 
ATOM   535  C  CB  . PHE A 1 70  ? 4.916  9.908   8.379   1.00 12.70 ? 70  PHE A CB  1 
ATOM   536  C  CG  . PHE A 1 70  ? 4.363  8.505   8.307   1.00 12.62 ? 70  PHE A CG  1 
ATOM   537  C  CD1 . PHE A 1 70  ? 5.184  7.407   8.530   1.00 12.97 ? 70  PHE A CD1 1 
ATOM   538  C  CD2 . PHE A 1 70  ? 3.039  8.287   7.974   1.00 13.28 ? 70  PHE A CD2 1 
ATOM   539  C  CE1 . PHE A 1 70  ? 4.660  6.115   8.485   1.00 13.62 ? 70  PHE A CE1 1 
ATOM   540  C  CE2 . PHE A 1 70  ? 2.506  7.002   7.931   1.00 12.34 ? 70  PHE A CE2 1 
ATOM   541  C  CZ  . PHE A 1 70  ? 3.343  5.915   8.114   1.00 13.16 ? 70  PHE A CZ  1 
ATOM   542  N  N   . ASP A 1 71  ? 4.870  12.566  6.637   1.00 13.74 ? 71  ASP A N   1 
ATOM   543  C  CA  . ASP A 1 71  ? 4.924  14.012  6.787   1.00 14.47 ? 71  ASP A CA  1 
ATOM   544  C  C   . ASP A 1 71  ? 4.671  14.365  8.249   1.00 13.54 ? 71  ASP A C   1 
ATOM   545  O  O   . ASP A 1 71  ? 3.589  14.088  8.789   1.00 16.55 ? 71  ASP A O   1 
ATOM   546  C  CB  . ASP A 1 71  ? 3.807  14.617  5.947   1.00 15.24 ? 71  ASP A CB  1 
ATOM   547  C  CG  . ASP A 1 71  ? 3.548  16.093  6.272   1.00 18.96 ? 71  ASP A CG  1 
ATOM   548  O  OD1 . ASP A 1 71  ? 4.452  16.746  6.820   1.00 18.30 ? 71  ASP A OD1 1 
ATOM   549  O  OD2 . ASP A 1 71  ? 2.437  16.557  6.025   1.00 19.92 ? 71  ASP A OD2 1 
ATOM   550  N  N   . ASP A 1 72  ? 5.686  14.943  8.892   1.00 13.95 ? 72  ASP A N   1 
ATOM   551  C  CA  . ASP A 1 72  ? 5.607  15.253  10.318  1.00 13.78 ? 72  ASP A CA  1 
ATOM   552  C  C   . ASP A 1 72  ? 5.639  16.770  10.529  1.00 15.45 ? 72  ASP A C   1 
ATOM   553  O  O   . ASP A 1 72  ? 6.043  17.235  11.595  1.00 13.74 ? 72  ASP A O   1 
ATOM   554  C  CB  . ASP A 1 72  ? 6.798  14.622  11.055  1.00 13.66 ? 72  ASP A CB  1 
ATOM   555  C  CG  . ASP A 1 72  ? 8.160  15.137  10.633  1.00 16.09 ? 72  ASP A CG  1 
ATOM   556  O  OD1 . ASP A 1 72  ? 8.270  15.791  9.555   1.00 15.16 ? 72  ASP A OD1 1 
ATOM   557  O  OD2 . ASP A 1 72  ? 9.125  14.887  11.368  1.00 14.45 ? 72  ASP A OD2 1 
ATOM   558  N  N   . SER A 1 73  ? 5.146  17.518  9.533   1.00 15.91 ? 73  SER A N   1 
ATOM   559  C  CA  . SER A 1 73  ? 5.166  18.979  9.580   1.00 20.04 ? 73  SER A CA  1 
ATOM   560  C  C   . SER A 1 73  ? 3.867  19.537  10.161  1.00 21.96 ? 73  SER A C   1 
ATOM   561  O  O   . SER A 1 73  ? 3.709  20.757  10.253  1.00 21.18 ? 73  SER A O   1 
ATOM   562  C  CB  . SER A 1 73  ? 5.453  19.572  8.238   1.00 18.93 ? 73  SER A CB  1 
ATOM   563  O  OG  . SER A 1 73  ? 4.331  19.361  7.374   1.00 18.23 ? 73  SER A OG  1 
ATOM   564  N  N   . GLN A 1 74  ? 2.936  18.654  10.563  1.00 19.45 ? 74  GLN A N   1 
ATOM   565  C  CA  . GLN A 1 74  ? 1.770  19.070  11.319  1.00 20.43 ? 74  GLN A CA  1 
ATOM   566  C  C   . GLN A 1 74  ? 1.421  17.867  12.171  1.00 21.73 ? 74  GLN A C   1 
ATOM   567  O  O   . GLN A 1 74  ? 1.987  16.814  11.908  1.00 20.92 ? 74  GLN A O   1 
ATOM   568  C  CB  . GLN A 1 74  ? 0.559  19.288  10.404  1.00 21.45 ? 74  GLN A CB  1 
ATOM   569  C  CG  . GLN A 1 74  ? 0.650  20.439  9.424   1.00 25.45 ? 74  GLN A CG  1 
ATOM   570  C  CD  . GLN A 1 74  ? -0.679 20.512  8.703   1.00 29.76 ? 74  GLN A CD  1 
ATOM   571  O  OE1 . GLN A 1 74  ? -1.665 21.032  9.229   1.00 40.37 ? 74  GLN A OE1 1 
ATOM   572  N  NE2 . GLN A 1 74  ? -0.726 19.974  7.503   1.00 27.13 ? 74  GLN A NE2 1 
ATOM   573  N  N   . ASP A 1 75  ? 0.562  18.062  13.191  1.00 24.81 ? 75  ASP A N   1 
ATOM   574  C  CA  . ASP A 1 75  ? 0.021  16.990  14.013  1.00 26.77 ? 75  ASP A CA  1 
ATOM   575  C  C   . ASP A 1 75  ? -0.988 16.214  13.174  1.00 26.78 ? 75  ASP A C   1 
ATOM   576  O  O   . ASP A 1 75  ? -2.133 16.640  13.020  1.00 33.69 ? 75  ASP A O   1 
ATOM   577  C  CB  . ASP A 1 75  ? -0.694 17.491  15.276  1.00 31.51 ? 75  ASP A CB  1 
ATOM   578  C  CG  . ASP A 1 75  ? 0.244  18.027  16.345  1.00 33.81 ? 75  ASP A CG  1 
ATOM   579  O  OD1 . ASP A 1 75  ? 1.461  17.815  16.216  1.00 32.19 ? 75  ASP A OD1 1 
ATOM   580  O  OD2 . ASP A 1 75  ? -0.258 18.645  17.302  1.00 36.88 ? 75  ASP A OD2 1 
ATOM   581  N  N   . LYS A 1 76  ? -0.547 15.086  12.640  1.00 22.36 ? 76  LYS A N   1 
ATOM   582  C  CA  . LYS A 1 76  ? -1.371 14.245  11.783  1.00 22.11 ? 76  LYS A CA  1 
ATOM   583  C  C   . LYS A 1 76  ? -1.427 12.807  12.298  1.00 23.91 ? 76  LYS A C   1 
ATOM   584  O  O   . LYS A 1 76  ? -2.463 12.142  12.241  1.00 31.39 ? 76  LYS A O   1 
ATOM   585  C  CB  . LYS A 1 76  ? -0.725 14.181  10.406  1.00 20.93 ? 76  LYS A CB  1 
ATOM   586  C  CG  . LYS A 1 76  ? -0.966 15.402  9.537   1.00 23.56 ? 76  LYS A CG  1 
ATOM   587  C  CD  . LYS A 1 76  ? -0.297 15.270  8.186   1.00 23.65 ? 76  LYS A CD  1 
ATOM   588  C  CE  . LYS A 1 76  ? -0.915 16.240  7.200   1.00 25.25 ? 76  LYS A CE  1 
ATOM   589  N  NZ  . LYS A 1 76  ? -0.514 15.958  5.808   1.00 22.99 ? 76  LYS A NZ  1 
ATOM   590  N  N   . ALA A 1 77  ? -0.271 12.257  12.657  1.00 19.44 ? 77  ALA A N   1 
ATOM   591  C  CA  . ALA A 1 77  ? -0.230 10.922  13.259  1.00 15.91 ? 77  ALA A CA  1 
ATOM   592  C  C   . ALA A 1 77  ? 0.544  11.104  14.563  1.00 15.83 ? 77  ALA A C   1 
ATOM   593  O  O   . ALA A 1 77  ? 1.739  11.381  14.505  1.00 16.06 ? 77  ALA A O   1 
ATOM   594  C  CB  . ALA A 1 77  ? 0.516  10.018  12.327  1.00 15.39 ? 77  ALA A CB  1 
ATOM   595  N  N   . VAL A 1 78  ? -0.123 11.013  15.712  1.00 14.06 ? 78  VAL A N   1 
ATOM   596  C  CA  . VAL A 1 78  ? 0.579  11.294  16.962  1.00 14.91 ? 78  VAL A CA  1 
ATOM   597  C  C   . VAL A 1 78  ? 0.306  10.203  18.000  1.00 14.39 ? 78  VAL A C   1 
ATOM   598  O  O   . VAL A 1 78  ? -0.750 9.536   18.025  1.00 15.90 ? 78  VAL A O   1 
ATOM   599  C  CB  . VAL A 1 78  ? 0.165  12.662  17.552  1.00 17.16 ? 78  VAL A CB  1 
ATOM   600  C  CG1 . VAL A 1 78  ? 0.539  13.861  16.670  1.00 17.73 ? 78  VAL A CG1 1 
ATOM   601  C  CG2 . VAL A 1 78  ? -1.296 12.641  17.960  1.00 17.52 ? 78  VAL A CG2 1 
ATOM   602  N  N   . LEU A 1 79  ? 1.305  10.080  18.893  1.00 13.37 ? 79  LEU A N   1 
ATOM   603  C  CA  . LEU A 1 79  ? 1.222  9.220   20.050  1.00 13.55 ? 79  LEU A CA  1 
ATOM   604  C  C   . LEU A 1 79  ? 1.220  10.128  21.274  1.00 13.13 ? 79  LEU A C   1 
ATOM   605  O  O   . LEU A 1 79  ? 1.967  11.108  21.354  1.00 13.81 ? 79  LEU A O   1 
ATOM   606  C  CB  . LEU A 1 79  ? 2.479  8.345   20.030  1.00 12.82 ? 79  LEU A CB  1 
ATOM   607  C  CG  . LEU A 1 79  ? 2.528  7.247   21.077  1.00 13.89 ? 79  LEU A CG  1 
ATOM   608  C  CD1 . LEU A 1 79  ? 1.506  6.142   20.753  1.00 16.60 ? 79  LEU A CD1 1 
ATOM   609  C  CD2 . LEU A 1 79  ? 3.955  6.673   21.115  1.00 12.81 ? 79  LEU A CD2 1 
ATOM   610  N  N   . LYS A 1 80  ? 0.347  9.813   22.216  1.00 13.32 ? 80  LYS A N   1 
ATOM   611  C  CA  . LYS A 1 80  ? 0.329  10.538  23.480  1.00 16.06 ? 80  LYS A CA  1 
ATOM   612  C  C   . LYS A 1 80  ? -0.255 9.606   24.539  1.00 14.72 ? 80  LYS A C   1 
ATOM   613  O  O   . LYS A 1 80  ? -0.534 8.448   24.237  1.00 13.92 ? 80  LYS A O   1 
ATOM   614  C  CB  . LYS A 1 80  ? -0.375 11.897  23.366  1.00 19.80 ? 80  LYS A CB  1 
ATOM   615  C  CG  . LYS A 1 80  ? -1.754 11.830  22.738  1.00 21.43 ? 80  LYS A CG  1 
ATOM   616  C  CD  . LYS A 1 80  ? -2.458 13.207  22.618  1.00 24.13 ? 80  LYS A CD  1 
ATOM   617  C  CE  . LYS A 1 80  ? -1.979 14.080  21.480  1.00 28.42 ? 80  LYS A CE  1 
ATOM   618  N  N   . GLY A 1 81  ? -0.362 10.113  25.776  1.00 14.86 ? 81  GLY A N   1 
ATOM   619  C  CA  . GLY A 1 81  ? -0.907 9.324   26.850  1.00 15.84 ? 81  GLY A CA  1 
ATOM   620  C  C   . GLY A 1 81  ? 0.099  8.238   27.182  1.00 16.34 ? 81  GLY A C   1 
ATOM   621  O  O   . GLY A 1 81  ? 1.291  8.449   26.998  1.00 16.09 ? 81  GLY A O   1 
ATOM   622  N  N   . GLY A 1 82  ? -0.387 7.098   27.680  1.00 16.08 ? 82  GLY A N   1 
ATOM   623  C  CA  . GLY A 1 82  ? 0.565  6.093   28.110  1.00 16.30 ? 82  GLY A CA  1 
ATOM   624  C  C   . GLY A 1 82  ? 1.465  6.676   29.197  1.00 17.09 ? 82  GLY A C   1 
ATOM   625  O  O   . GLY A 1 82  ? 0.962  7.372   30.096  1.00 18.83 ? 82  GLY A O   1 
ATOM   626  N  N   . PRO A 1 83  ? 2.810  6.500   29.128  1.00 15.03 ? 83  PRO A N   1 
ATOM   627  C  CA  . PRO A 1 83  ? 3.690  7.105   30.125  1.00 14.04 ? 83  PRO A CA  1 
ATOM   628  C  C   . PRO A 1 83  ? 4.107  8.516   29.707  1.00 15.89 ? 83  PRO A C   1 
ATOM   629  O  O   . PRO A 1 83  ? 4.962  9.127   30.343  1.00 16.55 ? 83  PRO A O   1 
ATOM   630  C  CB  . PRO A 1 83  ? 4.938  6.208   30.027  1.00 16.55 ? 83  PRO A CB  1 
ATOM   631  C  CG  . PRO A 1 83  ? 4.987  5.829   28.545  1.00 12.60 ? 83  PRO A CG  1 
ATOM   632  C  CD  . PRO A 1 83  ? 3.547  5.711   28.099  1.00 13.47 ? 83  PRO A CD  1 
ATOM   633  N  N   . LEU A 1 84  ? 3.511  9.052   28.632  1.00 14.31 ? 84  LEU A N   1 
ATOM   634  C  CA  . LEU A 1 84  ? 4.120  10.224  28.030  1.00 14.79 ? 84  LEU A CA  1 
ATOM   635  C  C   . LEU A 1 84  ? 3.445  11.476  28.571  1.00 18.98 ? 84  LEU A C   1 
ATOM   636  O  O   . LEU A 1 84  ? 2.234  11.454  28.778  1.00 19.13 ? 84  LEU A O   1 
ATOM   637  C  CB  . LEU A 1 84  ? 3.985  10.172  26.507  1.00 14.39 ? 84  LEU A CB  1 
ATOM   638  C  CG  . LEU A 1 84  ? 4.579  8.913   25.876  1.00 13.29 ? 84  LEU A CG  1 
ATOM   639  C  CD1 . LEU A 1 84  ? 4.131  8.814   24.430  1.00 13.50 ? 84  LEU A CD1 1 
ATOM   640  C  CD2 . LEU A 1 84  ? 6.125  8.942   25.936  1.00 13.72 ? 84  LEU A CD2 1 
ATOM   641  N  N   . ASP A 1 85  ? 4.228  12.566  28.589  1.00 22.79 ? 85  ASP A N   1 
ATOM   642  C  CA  . ASP A 1 85  ? 3.753  13.887  28.957  1.00 27.76 ? 85  ASP A CA  1 
ATOM   643  C  C   . ASP A 1 85  ? 3.351  14.690  27.732  1.00 30.96 ? 85  ASP A C   1 
ATOM   644  O  O   . ASP A 1 85  ? 2.379  15.442  27.782  1.00 39.44 ? 85  ASP A O   1 
ATOM   645  C  CB  . ASP A 1 85  ? 4.852  14.704  29.627  1.00 32.92 ? 85  ASP A CB  1 
ATOM   646  C  CG  . ASP A 1 85  ? 4.993  14.327  31.072  1.00 41.37 ? 85  ASP A CG  1 
ATOM   647  O  OD1 . ASP A 1 85  ? 4.007  13.760  31.618  1.00 42.90 ? 85  ASP A OD1 1 
ATOM   648  O  OD2 . ASP A 1 85  ? 6.085  14.600  31.636  1.00 45.00 ? 85  ASP A OD2 1 
ATOM   649  N  N   . GLY A 1 86  ? 4.119  14.597  26.652  1.00 26.26 ? 86  GLY A N   1 
ATOM   650  C  CA  . GLY A 1 86  ? 3.747  15.466  25.556  1.00 27.52 ? 86  GLY A CA  1 
ATOM   651  C  C   . GLY A 1 86  ? 2.995  14.740  24.442  1.00 25.08 ? 86  GLY A C   1 
ATOM   652  O  O   . GLY A 1 86  ? 2.433  13.662  24.659  1.00 25.83 ? 86  GLY A O   1 
ATOM   653  N  N   . THR A 1 87  ? 2.973  15.401  23.278  1.00 18.89 ? 87  THR A N   1 
ATOM   654  C  CA  . THR A 1 87  ? 2.488  14.863  22.024  1.00 18.38 ? 87  THR A CA  1 
ATOM   655  C  C   . THR A 1 87  ? 3.710  14.535  21.184  1.00 15.60 ? 87  THR A C   1 
ATOM   656  O  O   . THR A 1 87  ? 4.616  15.348  21.091  1.00 12.75 ? 87  THR A O   1 
ATOM   657  C  CB  . THR A 1 87  ? 1.750  15.959  21.243  1.00 23.32 ? 87  THR A CB  1 
ATOM   658  O  OG1 . THR A 1 87  ? 0.597  16.172  22.060  1.00 27.69 ? 87  THR A OG1 1 
ATOM   659  C  CG2 . THR A 1 87  ? 1.322  15.518  19.857  1.00 23.82 ? 87  THR A CG2 1 
ATOM   660  N  N   . TYR A 1 88  ? 3.739  13.321  20.647  1.00 13.00 ? 88  TYR A N   1 
ATOM   661  C  CA  . TYR A 1 88  ? 4.859  12.901  19.829  1.00 12.11 ? 88  TYR A CA  1 
ATOM   662  C  C   . TYR A 1 88  ? 4.360  12.606  18.416  1.00 12.36 ? 88  TYR A C   1 
ATOM   663  O  O   . TYR A 1 88  ? 3.399  11.862  18.229  1.00 13.67 ? 88  TYR A O   1 
ATOM   664  C  CB  . TYR A 1 88  ? 5.501  11.678  20.495  1.00 10.46 ? 88  TYR A CB  1 
ATOM   665  C  CG  . TYR A 1 88  ? 6.229  11.889  21.813  1.00 10.58 ? 88  TYR A CG  1 
ATOM   666  C  CD1 . TYR A 1 88  ? 5.548  12.202  22.980  1.00 10.19 ? 88  TYR A CD1 1 
ATOM   667  C  CD2 . TYR A 1 88  ? 7.617  11.714  21.889  1.00 9.95  ? 88  TYR A CD2 1 
ATOM   668  C  CE1 . TYR A 1 88  ? 6.217  12.422  24.181  1.00 10.19 ? 88  TYR A CE1 1 
ATOM   669  C  CE2 . TYR A 1 88  ? 8.305  11.911  23.086  1.00 9.05  ? 88  TYR A CE2 1 
ATOM   670  C  CZ  . TYR A 1 88  ? 7.601  12.261  24.226  1.00 9.63  ? 88  TYR A CZ  1 
ATOM   671  O  OH  . TYR A 1 88  ? 8.240  12.401  25.412  1.00 9.37  ? 88  TYR A OH  1 
ATOM   672  N  N   . ARG A 1 89  ? 5.025  13.160  17.411  1.00 10.98 ? 89  ARG A N   1 
ATOM   673  C  CA  . ARG A 1 89  ? 4.587  12.978  16.037  1.00 11.18 ? 89  ARG A CA  1 
ATOM   674  C  C   . ARG A 1 89  ? 5.346  11.847  15.351  1.00 9.58  ? 89  ARG A C   1 
ATOM   675  O  O   . ARG A 1 89  ? 6.572  11.775  15.435  1.00 9.35  ? 89  ARG A O   1 
ATOM   676  C  CB  . ARG A 1 89  ? 4.966  14.188  15.181  1.00 14.37 ? 89  ARG A CB  1 
ATOM   677  C  CG  . ARG A 1 89  ? 4.026  15.357  15.360  1.00 18.08 ? 89  ARG A CG  1 
ATOM   678  C  CD  . ARG A 1 89  ? 4.402  16.342  14.266  1.00 18.11 ? 89  ARG A CD  1 
ATOM   679  N  NE  . ARG A 1 89  ? 3.691  17.488  14.766  1.00 22.25 ? 89  ARG A NE  1 
ATOM   680  C  CZ  . ARG A 1 89  ? 3.955  18.744  14.426  1.00 25.08 ? 89  ARG A CZ  1 
ATOM   681  N  NH1 . ARG A 1 89  ? 4.930  19.007  13.572  1.00 21.89 ? 89  ARG A NH1 1 
ATOM   682  N  NH2 . ARG A 1 89  ? 3.245  19.732  14.939  1.00 28.23 ? 89  ARG A NH2 1 
ATOM   683  N  N   . LEU A 1 90  ? 4.601  10.985  14.626  1.00 8.98  ? 90  LEU A N   1 
ATOM   684  C  CA  . LEU A 1 90  ? 5.206  9.912   13.834  1.00 8.54  ? 90  LEU A CA  1 
ATOM   685  C  C   . LEU A 1 90  ? 6.055  10.484  12.699  1.00 9.17  ? 90  LEU A C   1 
ATOM   686  O  O   . LEU A 1 90  ? 5.575  11.257  11.854  1.00 10.87 ? 90  LEU A O   1 
ATOM   687  C  CB  . LEU A 1 90  ? 4.099  9.037   13.237  1.00 9.37  ? 90  LEU A CB  1 
ATOM   688  C  CG  . LEU A 1 90  ? 4.593  7.831   12.440  1.00 9.03  ? 90  LEU A CG  1 
ATOM   689  C  CD1 . LEU A 1 90  ? 5.375  6.832   13.296  1.00 10.50 ? 90  LEU A CD1 1 
ATOM   690  C  CD2 . LEU A 1 90  ? 3.374  7.100   11.833  1.00 9.64  ? 90  LEU A CD2 1 
ATOM   691  N  N   . ILE A 1 91  ? 7.307  10.045  12.655  1.00 8.45  ? 91  ILE A N   1 
ATOM   692  C  CA  . ILE A 1 91  ? 8.213  10.422  11.572  1.00 9.14  ? 91  ILE A CA  1 
ATOM   693  C  C   . ILE A 1 91  ? 8.473  9.258   10.623  1.00 8.96  ? 91  ILE A C   1 
ATOM   694  O  O   . ILE A 1 91  ? 8.500  9.428   9.405   1.00 9.07  ? 91  ILE A O   1 
ATOM   695  C  CB  . ILE A 1 91  ? 9.505  11.106  12.074  1.00 9.41  ? 91  ILE A CB  1 
ATOM   696  C  CG1 . ILE A 1 91  ? 10.388 11.457  10.865  1.00 10.14 ? 91  ILE A CG1 1 
ATOM   697  C  CG2 . ILE A 1 91  ? 10.259 10.263  13.102  1.00 9.70  ? 91  ILE A CG2 1 
ATOM   698  C  CD1 . ILE A 1 91  ? 11.523 12.456  11.210  1.00 12.15 ? 91  ILE A CD1 1 
ATOM   699  N  N   . GLN A 1 92  ? 8.720  8.037   11.147  1.00 9.06  ? 92  GLN A N   1 
ATOM   700  C  CA  . GLN A 1 92  ? 8.989  6.912   10.250  1.00 8.72  ? 92  GLN A CA  1 
ATOM   701  C  C   . GLN A 1 92  ? 8.708  5.637   11.044  1.00 8.82  ? 92  GLN A C   1 
ATOM   702  O  O   . GLN A 1 92  ? 8.679  5.702   12.257  1.00 8.08  ? 92  GLN A O   1 
ATOM   703  C  CB  . GLN A 1 92  ? 10.458 6.870   9.782   1.00 9.65  ? 92  GLN A CB  1 
ATOM   704  C  CG  . GLN A 1 92  ? 11.523 6.935   10.894  1.00 9.45  ? 92  GLN A CG  1 
ATOM   705  C  CD  . GLN A 1 92  ? 12.211 5.606   11.161  1.00 11.55 ? 92  GLN A CD  1 
ATOM   706  O  OE1 . GLN A 1 92  ? 11.589 4.557   11.180  1.00 10.03 ? 92  GLN A OE1 1 
ATOM   707  N  NE2 . GLN A 1 92  ? 13.504 5.641   11.503  1.00 12.93 ? 92  GLN A NE2 1 
ATOM   708  N  N   . PHE A 1 93  ? 8.469  4.527   10.340  1.00 7.83  ? 93  PHE A N   1 
ATOM   709  C  CA  . PHE A 1 93  ? 8.602  3.212   10.950  1.00 8.34  ? 93  PHE A CA  1 
ATOM   710  C  C   . PHE A 1 93  ? 9.550  2.332   10.145  1.00 7.48  ? 93  PHE A C   1 
ATOM   711  O  O   . PHE A 1 93  ? 9.780  2.510   8.962   1.00 7.63  ? 93  PHE A O   1 
ATOM   712  C  CB  . PHE A 1 93  ? 7.236  2.539   11.227  1.00 7.66  ? 93  PHE A CB  1 
ATOM   713  C  CG  . PHE A 1 93  ? 6.501  2.058   9.994   1.00 9.19  ? 93  PHE A CG  1 
ATOM   714  C  CD1 . PHE A 1 93  ? 6.901  0.921   9.296   1.00 9.44  ? 93  PHE A CD1 1 
ATOM   715  C  CD2 . PHE A 1 93  ? 5.405  2.775   9.524   1.00 9.43  ? 93  PHE A CD2 1 
ATOM   716  C  CE1 . PHE A 1 93  ? 6.203  0.496   8.171   1.00 10.08 ? 93  PHE A CE1 1 
ATOM   717  C  CE2 . PHE A 1 93  ? 4.673  2.311   8.429   1.00 10.12 ? 93  PHE A CE2 1 
ATOM   718  C  CZ  . PHE A 1 93  ? 5.105  1.205   7.728   1.00 10.13 ? 93  PHE A CZ  1 
ATOM   719  N  N   . HIS A 1 94  ? 10.084 1.293   10.805  1.00 6.82  ? 94  HIS A N   1 
ATOM   720  C  CA  . HIS A 1 94  ? 10.984 0.345   10.184  1.00 6.90  ? 94  HIS A CA  1 
ATOM   721  C  C   . HIS A 1 94  ? 10.867 -0.924  11.019  1.00 6.62  ? 94  HIS A C   1 
ATOM   722  O  O   . HIS A 1 94  ? 10.146 -0.936  12.023  1.00 6.63  ? 94  HIS A O   1 
ATOM   723  C  CB  . HIS A 1 94  ? 12.449 0.845   10.195  1.00 6.74  ? 94  HIS A CB  1 
ATOM   724  C  CG  . HIS A 1 94  ? 12.926 1.109   11.602  1.00 6.26  ? 94  HIS A CG  1 
ATOM   725  N  ND1 . HIS A 1 94  ? 12.724 2.323   12.256  1.00 6.09  ? 94  HIS A ND1 1 
ATOM   726  C  CD2 . HIS A 1 94  ? 13.509 0.280   12.504  1.00 5.95  ? 94  HIS A CD2 1 
ATOM   727  C  CE1 . HIS A 1 94  ? 13.198 2.236   13.500  1.00 6.21  ? 94  HIS A CE1 1 
ATOM   728  N  NE2 . HIS A 1 94  ? 13.678 0.965   13.677  1.00 5.85  ? 94  HIS A NE2 1 
ATOM   729  N  N   . PHE A 1 95  ? 11.573 -1.960  10.580  1.00 6.33  ? 95  PHE A N   1 
ATOM   730  C  CA  . PHE A 1 95  ? 11.560 -3.234  11.281  1.00 6.82  ? 95  PHE A CA  1 
ATOM   731  C  C   . PHE A 1 95  ? 12.999 -3.741  11.434  1.00 6.74  ? 95  PHE A C   1 
ATOM   732  O  O   . PHE A 1 95  ? 13.945 -3.256  10.787  1.00 7.64  ? 95  PHE A O   1 
ATOM   733  C  CB  . PHE A 1 95  ? 10.873 -4.319  10.427  1.00 6.45  ? 95  PHE A CB  1 
ATOM   734  C  CG  . PHE A 1 95  ? 9.418  -4.042  10.097  1.00 6.67  ? 95  PHE A CG  1 
ATOM   735  C  CD1 . PHE A 1 95  ? 9.088  -3.159  9.070   1.00 7.44  ? 95  PHE A CD1 1 
ATOM   736  C  CD2 . PHE A 1 95  ? 8.402  -4.706  10.768  1.00 7.49  ? 95  PHE A CD2 1 
ATOM   737  C  CE1 . PHE A 1 95  ? 7.768  -2.949  8.693   1.00 7.20  ? 95  PHE A CE1 1 
ATOM   738  C  CE2 . PHE A 1 95  ? 7.071  -4.482  10.424  1.00 7.33  ? 95  PHE A CE2 1 
ATOM   739  C  CZ  . PHE A 1 95  ? 6.771  -3.628  9.368   1.00 7.59  ? 95  PHE A CZ  1 
ATOM   740  N  N   . HIS A 1 96  ? 13.150 -4.707  12.343  1.00 6.54  ? 96  HIS A N   1 
ATOM   741  C  CA  . HIS A 1 96  ? 14.355 -5.499  12.515  1.00 6.73  ? 96  HIS A CA  1 
ATOM   742  C  C   . HIS A 1 96  ? 13.934 -6.957  12.342  1.00 6.94  ? 96  HIS A C   1 
ATOM   743  O  O   . HIS A 1 96  ? 12.889 -7.301  12.880  1.00 7.27  ? 96  HIS A O   1 
ATOM   744  C  CB  . HIS A 1 96  ? 14.946 -5.291  13.921  1.00 7.46  ? 96  HIS A CB  1 
ATOM   745  C  CG  . HIS A 1 96  ? 15.245 -3.850  14.178  1.00 7.40  ? 96  HIS A CG  1 
ATOM   746  N  ND1 . HIS A 1 96  ? 16.507 -3.304  13.926  1.00 7.59  ? 96  HIS A ND1 1 
ATOM   747  C  CD2 . HIS A 1 96  ? 14.442 -2.833  14.574  1.00 7.59  ? 96  HIS A CD2 1 
ATOM   748  C  CE1 . HIS A 1 96  ? 16.484 -2.021  14.260  1.00 7.81  ? 96  HIS A CE1 1 
ATOM   749  N  NE2 . HIS A 1 96  ? 15.197 -1.694  14.592  1.00 7.56  ? 96  HIS A NE2 1 
ATOM   750  N  N   . TRP A 1 97  ? 14.719 -7.796  11.640  1.00 6.64  ? 97  TRP A N   1 
ATOM   751  C  CA  . TRP A 1 97  ? 14.304 -9.193  11.483  1.00 7.55  ? 97  TRP A CA  1 
ATOM   752  C  C   . TRP A 1 97  ? 15.492 -10.121 11.375  1.00 7.40  ? 97  TRP A C   1 
ATOM   753  O  O   . TRP A 1 97  ? 16.641 -9.679  11.224  1.00 8.06  ? 97  TRP A O   1 
ATOM   754  C  CB  . TRP A 1 97  ? 13.414 -9.387  10.252  1.00 8.12  ? 97  TRP A CB  1 
ATOM   755  C  CG  . TRP A 1 97  ? 14.045 -8.939  8.955   1.00 8.97  ? 97  TRP A CG  1 
ATOM   756  C  CD1 . TRP A 1 97  ? 14.749 -9.728  8.089   1.00 9.56  ? 97  TRP A CD1 1 
ATOM   757  C  CD2 . TRP A 1 97  ? 14.102 -7.595  8.423   1.00 8.81  ? 97  TRP A CD2 1 
ATOM   758  N  NE1 . TRP A 1 97  ? 15.172 -8.983  7.002   1.00 10.22 ? 97  TRP A NE1 1 
ATOM   759  C  CE2 . TRP A 1 97  ? 14.780 -7.675  7.185   1.00 9.42  ? 97  TRP A CE2 1 
ATOM   760  C  CE3 . TRP A 1 97  ? 13.599 -6.345  8.843   1.00 8.19  ? 97  TRP A CE3 1 
ATOM   761  C  CZ2 . TRP A 1 97  ? 15.007 -6.549  6.378   1.00 9.12  ? 97  TRP A CZ2 1 
ATOM   762  C  CZ3 . TRP A 1 97  ? 13.846 -5.218  8.049   1.00 8.21  ? 97  TRP A CZ3 1 
ATOM   763  C  CH2 . TRP A 1 97  ? 14.498 -5.339  6.822   1.00 8.69  ? 97  TRP A CH2 1 
ATOM   764  N  N   . GLY A 1 98  ? 15.172 -11.428 11.379  1.00 7.66  ? 98  GLY A N   1 
ATOM   765  C  CA  . GLY A 1 98  ? 16.217 -12.425 11.478  1.00 7.89  ? 98  GLY A CA  1 
ATOM   766  C  C   . GLY A 1 98  ? 16.451 -13.149 10.146  1.00 8.24  ? 98  GLY A C   1 
ATOM   767  O  O   . GLY A 1 98  ? 15.762 -12.910 9.153   1.00 8.38  ? 98  GLY A O   1 
ATOM   768  N  N   . SER A 1 99  ? 17.471 -14.000 10.143  1.00 9.10  ? 99  SER A N   1 
ATOM   769  C  CA  . SER A 1 99  ? 17.719 -14.886 9.009   1.00 11.32 ? 99  SER A CA  1 
ATOM   770  C  C   . SER A 1 99  ? 16.811 -16.117 9.108   1.00 12.58 ? 99  SER A C   1 
ATOM   771  O  O   . SER A 1 99  ? 16.726 -16.898 8.167   1.00 14.44 ? 99  SER A O   1 
ATOM   772  C  CB  . SER A 1 99  ? 19.182 -15.247 9.023   1.00 10.59 ? 99  SER A CB  1 
ATOM   773  O  OG  . SER A 1 99  ? 19.564 -15.875 10.244  1.00 12.32 ? 99  SER A OG  1 
ATOM   774  N  N   . LEU A 1 100 ? 16.197 -16.323 10.281  1.00 12.96 ? 100 LEU A N   1 
ATOM   775  C  CA  . LEU A 1 100 ? 15.394 -17.478 10.629  1.00 14.11 ? 100 LEU A CA  1 
ATOM   776  C  C   . LEU A 1 100 ? 14.223 -16.963 11.455  1.00 13.89 ? 100 LEU A C   1 
ATOM   777  O  O   . LEU A 1 100 ? 14.348 -15.942 12.122  1.00 13.09 ? 100 LEU A O   1 
ATOM   778  C  CB  . LEU A 1 100 ? 16.211 -18.376 11.571  1.00 17.94 ? 100 LEU A CB  1 
ATOM   779  C  CG  . LEU A 1 100 ? 17.498 -18.938 10.990  1.00 20.21 ? 100 LEU A CG  1 
ATOM   780  C  CD1 . LEU A 1 100 ? 18.430 -19.395 12.101  1.00 28.71 ? 100 LEU A CD1 1 
ATOM   781  C  CD2 . LEU A 1 100 ? 17.160 -20.058 10.017  1.00 25.93 ? 100 LEU A CD2 1 
ATOM   782  N  N   . ASP A 1 101 ? 13.154 -17.756 11.529  1.00 12.62 ? 101 ASP A N   1 
ATOM   783  C  CA  . ASP A 1 101 ? 11.986 -17.269 12.258  1.00 12.12 ? 101 ASP A CA  1 
ATOM   784  C  C   . ASP A 1 101 ? 12.235 -17.206 13.768  1.00 12.43 ? 101 ASP A C   1 
ATOM   785  O  O   . ASP A 1 101 ? 11.520 -16.494 14.486  1.00 13.69 ? 101 ASP A O   1 
ATOM   786  C  CB  . ASP A 1 101 ? 10.742 -18.101 11.941  1.00 13.78 ? 101 ASP A CB  1 
ATOM   787  C  CG  . ASP A 1 101 ? 10.272 -18.111 10.495  1.00 16.58 ? 101 ASP A CG  1 
ATOM   788  O  OD1 . ASP A 1 101 ? 10.620 -17.216 9.706   1.00 15.54 ? 101 ASP A OD1 1 
ATOM   789  O  OD2 . ASP A 1 101 ? 9.489  -19.009 10.188  1.00 18.95 ? 101 ASP A OD2 1 
ATOM   790  N  N   . GLY A 1 102 ? 13.255 -17.923 14.264  1.00 12.41 ? 102 GLY A N   1 
ATOM   791  C  CA  . GLY A 1 102 ? 13.500 -17.974 15.699  1.00 12.38 ? 102 GLY A CA  1 
ATOM   792  C  C   . GLY A 1 102 ? 14.290 -16.780 16.245  1.00 11.05 ? 102 GLY A C   1 
ATOM   793  O  O   . GLY A 1 102 ? 14.626 -16.737 17.434  1.00 11.84 ? 102 GLY A O   1 
ATOM   794  N  N   . GLN A 1 103 ? 14.600 -15.791 15.399  1.00 10.61 ? 103 GLN A N   1 
ATOM   795  C  CA  . GLN A 1 103 ? 15.273 -14.617 15.943  1.00 10.08 ? 103 GLN A CA  1 
ATOM   796  C  C   . GLN A 1 103 ? 14.945 -13.435 15.046  1.00 9.67  ? 103 GLN A C   1 
ATOM   797  O  O   . GLN A 1 103 ? 14.375 -13.624 13.977  1.00 9.23  ? 103 GLN A O   1 
ATOM   798  C  CB  . GLN A 1 103 ? 16.796 -14.838 15.986  1.00 12.56 ? 103 GLN A CB  1 
ATOM   799  C  CG  . GLN A 1 103 ? 17.395 -14.980 14.587  1.00 15.04 ? 103 GLN A CG  1 
ATOM   800  C  CD  . GLN A 1 103 ? 18.770 -15.596 14.660  1.00 18.58 ? 103 GLN A CD  1 
ATOM   801  O  OE1 . GLN A 1 103 ? 18.991 -16.514 15.451  1.00 22.86 ? 103 GLN A OE1 1 
ATOM   802  N  NE2 . GLN A 1 103 ? 19.678 -15.157 13.792  1.00 16.14 ? 103 GLN A NE2 1 
ATOM   803  N  N   . GLY A 1 104 ? 15.317 -12.228 15.482  1.00 8.76  ? 104 GLY A N   1 
ATOM   804  C  CA  . GLY A 1 104 ? 15.001 -11.050 14.676  1.00 7.51  ? 104 GLY A CA  1 
ATOM   805  C  C   . GLY A 1 104 ? 14.606 -9.854  15.540  1.00 7.77  ? 104 GLY A C   1 
ATOM   806  O  O   . GLY A 1 104 ? 14.923 -8.701  15.207  1.00 8.64  ? 104 GLY A O   1 
ATOM   807  N  N   . SER A 1 105 ? 13.871 -10.124 16.638  1.00 7.54  ? 105 SER A N   1 
ATOM   808  C  CA  . SER A 1 105 ? 13.468 -9.000  17.493  1.00 7.53  ? 105 SER A CA  1 
ATOM   809  C  C   . SER A 1 105 ? 14.655 -8.445  18.292  1.00 6.79  ? 105 SER A C   1 
ATOM   810  O  O   . SER A 1 105 ? 15.668 -9.106  18.514  1.00 8.03  ? 105 SER A O   1 
ATOM   811  C  CB  . SER A 1 105 ? 12.327 -9.350  18.425  1.00 6.96  ? 105 SER A CB  1 
ATOM   812  O  OG  . SER A 1 105 ? 12.774 -10.266 19.418  1.00 7.82  ? 105 SER A OG  1 
ATOM   813  N  N   . GLU A 1 106 ? 14.521 -7.186  18.695  1.00 6.41  ? 106 GLU A N   1 
ATOM   814  C  CA  . GLU A 1 106 ? 15.557 -6.543  19.506  1.00 6.30  ? 106 GLU A CA  1 
ATOM   815  C  C   . GLU A 1 106 ? 15.230 -6.716  20.980  1.00 6.00  ? 106 GLU A C   1 
ATOM   816  O  O   . GLU A 1 106 ? 16.021 -7.269  21.749  1.00 6.35  ? 106 GLU A O   1 
ATOM   817  C  CB  . GLU A 1 106 ? 15.651 -5.070  19.126  1.00 6.61  ? 106 GLU A CB  1 
ATOM   818  C  CG  . GLU A 1 106 ? 16.091 -4.920  17.671  1.00 7.05  ? 106 GLU A CG  1 
ATOM   819  C  CD  . GLU A 1 106 ? 16.768 -3.620  17.310  1.00 7.32  ? 106 GLU A CD  1 
ATOM   820  O  OE1 . GLU A 1 106 ? 16.183 -2.543  17.536  1.00 7.50  ? 106 GLU A OE1 1 
ATOM   821  O  OE2 . GLU A 1 106 ? 17.944 -3.677  16.857  1.00 7.94  ? 106 GLU A OE2 1 
ATOM   822  N  N   . HIS A 1 107 ? 14.040 -6.268  21.402  1.00 5.86  ? 107 HIS A N   1 
ATOM   823  C  CA  . HIS A 1 107 ? 13.615 -6.610  22.746  1.00 5.73  ? 107 HIS A CA  1 
ATOM   824  C  C   . HIS A 1 107 ? 13.263 -8.086  22.751  1.00 6.37  ? 107 HIS A C   1 
ATOM   825  O  O   . HIS A 1 107 ? 12.965 -8.670  21.685  1.00 5.90  ? 107 HIS A O   1 
ATOM   826  C  CB  . HIS A 1 107 ? 12.367 -5.789  23.126  1.00 5.94  ? 107 HIS A CB  1 
ATOM   827  C  CG  . HIS A 1 107 ? 12.676 -4.337  23.269  1.00 6.10  ? 107 HIS A CG  1 
ATOM   828  N  ND1 . HIS A 1 107 ? 12.611 -3.455  22.210  1.00 6.05  ? 107 HIS A ND1 1 
ATOM   829  C  CD2 . HIS A 1 107 ? 13.091 -3.624  24.339  1.00 6.03  ? 107 HIS A CD2 1 
ATOM   830  C  CE1 . HIS A 1 107 ? 13.050 -2.256  22.615  1.00 6.30  ? 107 HIS A CE1 1 
ATOM   831  N  NE2 . HIS A 1 107 ? 13.345 -2.340  23.922  1.00 5.94  ? 107 HIS A NE2 1 
ATOM   832  N  N   . THR A 1 108 ? 13.457 -8.687  23.923  1.00 7.05  ? 108 THR A N   1 
ATOM   833  C  CA  . THR A 1 108 ? 13.028 -10.062 24.138  1.00 8.19  ? 108 THR A CA  1 
ATOM   834  C  C   . THR A 1 108 ? 12.068 -10.081 25.333  1.00 9.00  ? 108 THR A C   1 
ATOM   835  O  O   . THR A 1 108 ? 12.031 -9.139  26.131  1.00 9.45  ? 108 THR A O   1 
ATOM   836  C  CB  . THR A 1 108 ? 14.237 -10.961 24.370  1.00 7.98  ? 108 THR A CB  1 
ATOM   837  O  OG1 . THR A 1 108 ? 15.032 -10.472 25.459  1.00 8.57  ? 108 THR A OG1 1 
ATOM   838  C  CG2 . THR A 1 108 ? 15.062 -11.147 23.097  1.00 8.07  ? 108 THR A CG2 1 
ATOM   839  N  N   . VAL A 1 109 ? 11.294 -11.162 25.460  1.00 9.31  ? 109 VAL A N   1 
ATOM   840  C  CA  . VAL A 1 109 ? 10.345 -11.232 26.561  1.00 9.46  ? 109 VAL A CA  1 
ATOM   841  C  C   . VAL A 1 109 ? 10.624 -12.539 27.304  1.00 10.82 ? 109 VAL A C   1 
ATOM   842  O  O   . VAL A 1 109 ? 10.472 -13.596 26.710  1.00 11.59 ? 109 VAL A O   1 
ATOM   843  C  CB  . VAL A 1 109 ? 8.906  -11.241 26.011  1.00 10.30 ? 109 VAL A CB  1 
ATOM   844  C  CG1 . VAL A 1 109 ? 7.916  -11.374 27.151  1.00 9.96  ? 109 VAL A CG1 1 
ATOM   845  C  CG2 . VAL A 1 109 ? 8.586  -9.964  25.220  1.00 9.14  ? 109 VAL A CG2 1 
ATOM   846  N  N   . ASP A 1 110 ? 11.116 -12.448 28.536  1.00 10.26 ? 110 ASP A N   1 
ATOM   847  C  CA  . ASP A 1 110 ? 11.647 -13.624 29.238  1.00 13.08 ? 110 ASP A CA  1 
ATOM   848  C  C   . ASP A 1 110 ? 12.595 -14.431 28.353  1.00 12.35 ? 110 ASP A C   1 
ATOM   849  O  O   . ASP A 1 110 ? 12.484 -15.679 28.286  1.00 11.79 ? 110 ASP A O   1 
ATOM   850  C  CB  . ASP A 1 110 ? 10.501 -14.468 29.808  1.00 13.98 ? 110 ASP A CB  1 
ATOM   851  C  CG  . ASP A 1 110 ? 9.674  -13.678 30.792  1.00 15.17 ? 110 ASP A CG  1 
ATOM   852  O  OD1 . ASP A 1 110 ? 10.269 -12.858 31.513  1.00 17.31 ? 110 ASP A OD1 1 
ATOM   853  O  OD2 . ASP A 1 110 ? 8.459  -13.928 30.838  1.00 17.52 ? 110 ASP A OD2 1 
ATOM   854  N  N   . LYS A 1 111 ? 13.521 -13.707 27.695  1.00 11.11 ? 111 LYS A N   1 
ATOM   855  C  CA  . LYS A 1 111 ? 14.539 -14.212 26.771  1.00 12.50 ? 111 LYS A CA  1 
ATOM   856  C  C   . LYS A 1 111 ? 13.985 -14.736 25.446  1.00 11.59 ? 111 LYS A C   1 
ATOM   857  O  O   . LYS A 1 111 ? 14.768 -15.166 24.604  1.00 11.77 ? 111 LYS A O   1 
ATOM   858  C  CB  . LYS A 1 111 ? 15.367 -15.316 27.425  1.00 13.51 ? 111 LYS A CB  1 
ATOM   859  C  CG  . LYS A 1 111 ? 15.999 -14.924 28.750  1.00 16.37 ? 111 LYS A CG  1 
ATOM   860  C  CD  . LYS A 1 111 ? 17.050 -13.892 28.526  1.00 19.27 ? 111 LYS A CD  1 
ATOM   861  C  CE  . LYS A 1 111 ? 17.649 -13.415 29.828  1.00 23.94 ? 111 LYS A CE  1 
ATOM   862  N  NZ  . LYS A 1 111 ? 19.107 -13.647 29.776  1.00 26.99 ? 111 LYS A NZ  1 
ATOM   863  N  N   . LYS A 1 112 ? 12.668 -14.679 25.244  1.00 10.59 ? 112 LYS A N   1 
ATOM   864  C  CA  . LYS A 1 112 ? 12.103 -15.133 23.987  1.00 11.82 ? 112 LYS A CA  1 
ATOM   865  C  C   . LYS A 1 112 ? 12.363 -14.075 22.901  1.00 11.34 ? 112 LYS A C   1 
ATOM   866  O  O   . LYS A 1 112 ? 12.074 -12.897 23.072  1.00 10.95 ? 112 LYS A O   1 
ATOM   867  C  CB  . LYS A 1 112 ? 10.606 -15.403 24.121  1.00 14.12 ? 112 LYS A CB  1 
ATOM   868  C  CG  . LYS A 1 112 ? 9.883  -15.614 22.791  1.00 15.83 ? 112 LYS A CG  1 
ATOM   869  C  CD  . LYS A 1 112 ? 8.344  -15.557 23.016  1.00 18.63 ? 112 LYS A CD  1 
ATOM   870  C  CE  . LYS A 1 112 ? 7.564  -15.689 21.719  1.00 24.54 ? 112 LYS A CE  1 
ATOM   871  N  NZ  . LYS A 1 112 ? 8.010  -16.878 20.970  1.00 24.21 ? 112 LYS A NZ  1 
ATOM   872  N  N   A LYS A 1 113 ? 12.905 -14.543 21.773  0.50 10.99 ? 113 LYS A N   1 
ATOM   873  N  N   B LYS A 1 113 ? 12.909 -14.541 21.774  0.50 11.12 ? 113 LYS A N   1 
ATOM   874  C  CA  A LYS A 1 113 ? 13.095 -13.703 20.591  0.50 10.26 ? 113 LYS A CA  1 
ATOM   875  C  CA  B LYS A 1 113 ? 13.089 -13.698 20.595  0.50 10.47 ? 113 LYS A CA  1 
ATOM   876  C  C   A LYS A 1 113 ? 11.960 -13.950 19.607  0.50 10.03 ? 113 LYS A C   1 
ATOM   877  C  C   B LYS A 1 113 ? 11.954 -13.948 19.614  0.50 10.16 ? 113 LYS A C   1 
ATOM   878  O  O   A LYS A 1 113 ? 11.568 -15.100 19.394  0.50 10.30 ? 113 LYS A O   1 
ATOM   879  O  O   B LYS A 1 113 ? 11.565 -15.099 19.401  0.50 10.41 ? 113 LYS A O   1 
ATOM   880  C  CB  A LYS A 1 113 ? 14.429 -14.051 19.929  0.50 10.36 ? 113 LYS A CB  1 
ATOM   881  C  CB  B LYS A 1 113 ? 14.402 -14.058 19.900  0.50 10.76 ? 113 LYS A CB  1 
ATOM   882  C  CG  A LYS A 1 113 ? 15.646 -13.751 20.790  0.50 10.23 ? 113 LYS A CG  1 
ATOM   883  C  CG  B LYS A 1 113 ? 15.648 -13.818 20.735  0.50 10.92 ? 113 LYS A CG  1 
ATOM   884  C  CD  A LYS A 1 113 ? 16.923 -14.287 20.173  0.50 10.38 ? 113 LYS A CD  1 
ATOM   885  C  CD  B LYS A 1 113 ? 16.870 -14.288 19.981  0.50 11.12 ? 113 LYS A CD  1 
ATOM   886  C  CE  A LYS A 1 113 ? 18.170 -13.718 20.825  0.50 9.79  ? 113 LYS A CE  1 
ATOM   887  C  CE  B LYS A 1 113 ? 18.161 -13.718 20.536  0.50 10.71 ? 113 LYS A CE  1 
ATOM   888  N  NZ  A LYS A 1 113 ? 19.398 -14.457 20.436  0.50 9.76  ? 113 LYS A NZ  1 
ATOM   889  N  NZ  B LYS A 1 113 ? 18.640 -14.506 21.695  0.50 11.27 ? 113 LYS A NZ  1 
ATOM   890  N  N   . TYR A 1 114 ? 11.397 -12.864 19.056  1.00 9.22  ? 114 TYR A N   1 
ATOM   891  C  CA  . TYR A 1 114 ? 10.379 -12.958 18.020  1.00 8.81  ? 114 TYR A CA  1 
ATOM   892  C  C   . TYR A 1 114 ? 11.038 -12.915 16.642  1.00 8.75  ? 114 TYR A C   1 
ATOM   893  O  O   . TYR A 1 114 ? 12.217 -12.613 16.547  1.00 8.46  ? 114 TYR A O   1 
ATOM   894  C  CB  . TYR A 1 114 ? 9.341  -11.849 18.165  1.00 8.96  ? 114 TYR A CB  1 
ATOM   895  C  CG  . TYR A 1 114 ? 8.388  -12.082 19.323  1.00 9.89  ? 114 TYR A CG  1 
ATOM   896  C  CD1 . TYR A 1 114 ? 8.700  -11.672 20.608  1.00 10.93 ? 114 TYR A CD1 1 
ATOM   897  C  CD2 . TYR A 1 114 ? 7.191  -12.760 19.130  1.00 11.55 ? 114 TYR A CD2 1 
ATOM   898  C  CE1 . TYR A 1 114 ? 7.849  -11.897 21.684  1.00 12.71 ? 114 TYR A CE1 1 
ATOM   899  C  CE2 . TYR A 1 114 ? 6.300  -12.937 20.180  1.00 12.70 ? 114 TYR A CE2 1 
ATOM   900  C  CZ  . TYR A 1 114 ? 6.633  -12.510 21.452  1.00 13.88 ? 114 TYR A CZ  1 
ATOM   901  O  OH  . TYR A 1 114 ? 5.776  -12.707 22.494  1.00 17.89 ? 114 TYR A OH  1 
ATOM   902  N  N   . ALA A 1 115 ? 10.256 -13.163 15.566  1.00 8.91  ? 115 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 115 ? 10.801 -13.222 14.221  1.00 8.37  ? 115 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 115 ? 11.202 -11.828 13.755  1.00 8.33  ? 115 ALA A C   1 
ATOM   905  O  O   . ALA A 1 115 ? 12.026 -11.697 12.850  1.00 9.36  ? 115 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 115 ? 9.773  -13.827 13.280  1.00 8.73  ? 115 ALA A CB  1 
ATOM   907  N  N   . ALA A 1 116 ? 10.525 -10.798 14.287  1.00 7.50  ? 116 ALA A N   1 
ATOM   908  C  CA  . ALA A 1 116 ? 10.891 -9.461  13.879  1.00 7.00  ? 116 ALA A CA  1 
ATOM   909  C  C   . ALA A 1 116 ? 10.320 -8.477  14.888  1.00 6.60  ? 116 ALA A C   1 
ATOM   910  O  O   . ALA A 1 116 ? 9.578  -8.867  15.804  1.00 6.83  ? 116 ALA A O   1 
ATOM   911  C  CB  . ALA A 1 116 ? 10.376 -9.141  12.485  1.00 6.46  ? 116 ALA A CB  1 
ATOM   912  N  N   . GLU A 1 117 ? 10.714 -7.200  14.736  1.00 6.39  ? 117 GLU A N   1 
ATOM   913  C  CA  . GLU A 1 117 ? 10.124 -6.183  15.600  1.00 6.26  ? 117 GLU A CA  1 
ATOM   914  C  C   . GLU A 1 117 ? 9.887  -4.933  14.761  1.00 6.67  ? 117 GLU A C   1 
ATOM   915  O  O   . GLU A 1 117 ? 10.793 -4.500  14.054  1.00 7.76  ? 117 GLU A O   1 
ATOM   916  C  CB  . GLU A 1 117 ? 11.106 -5.916  16.758  1.00 6.30  ? 117 GLU A CB  1 
ATOM   917  C  CG  . GLU A 1 117 ? 10.555 -4.973  17.849  1.00 6.46  ? 117 GLU A CG  1 
ATOM   918  C  CD  . GLU A 1 117 ? 11.484 -4.913  19.065  1.00 7.14  ? 117 GLU A CD  1 
ATOM   919  O  OE1 . GLU A 1 117 ? 12.104 -5.947  19.404  1.00 7.82  ? 117 GLU A OE1 1 
ATOM   920  O  OE2 . GLU A 1 117 ? 11.459 -3.861  19.764  1.00 8.46  ? 117 GLU A OE2 1 
ATOM   921  N  N   . LEU A 1 118 ? 8.690  -4.348  14.893  1.00 6.67  ? 118 LEU A N   1 
ATOM   922  C  CA  . LEU A 1 118 ? 8.348  -3.077  14.256  1.00 5.83  ? 118 LEU A CA  1 
ATOM   923  C  C   . LEU A 1 118 ? 8.596  -1.933  15.248  1.00 5.53  ? 118 LEU A C   1 
ATOM   924  O  O   . LEU A 1 118 ? 8.205  -1.997  16.402  1.00 5.87  ? 118 LEU A O   1 
ATOM   925  C  CB  . LEU A 1 118 ? 6.871  -3.134  13.841  1.00 5.84  ? 118 LEU A CB  1 
ATOM   926  C  CG  . LEU A 1 118 ? 6.157  -1.815  13.495  1.00 6.23  ? 118 LEU A CG  1 
ATOM   927  C  CD1 . LEU A 1 118 ? 6.721  -1.229  12.195  1.00 6.69  ? 118 LEU A CD1 1 
ATOM   928  C  CD2 . LEU A 1 118 ? 4.646  -2.145  13.303  1.00 7.06  ? 118 LEU A CD2 1 
ATOM   929  N  N   . HIS A 1 119 ? 9.188  -0.847  14.755  1.00 5.15  ? 119 HIS A N   1 
ATOM   930  C  CA  . HIS A 1 119 ? 9.436  0.341   15.538  1.00 5.56  ? 119 HIS A CA  1 
ATOM   931  C  C   . HIS A 1 119 ? 8.765  1.514   14.836  1.00 5.77  ? 119 HIS A C   1 
ATOM   932  O  O   . HIS A 1 119 ? 9.208  1.864   13.715  1.00 6.85  ? 119 HIS A O   1 
ATOM   933  C  CB  . HIS A 1 119 ? 10.962 0.574   15.605  1.00 4.92  ? 119 HIS A CB  1 
ATOM   934  C  CG  . HIS A 1 119 ? 11.606 -0.379  16.549  1.00 4.84  ? 119 HIS A CG  1 
ATOM   935  N  ND1 . HIS A 1 119 ? 12.967 -0.684  16.514  1.00 5.02  ? 119 HIS A ND1 1 
ATOM   936  C  CD2 . HIS A 1 119 ? 11.067 -1.159  17.503  1.00 4.89  ? 119 HIS A CD2 1 
ATOM   937  C  CE1 . HIS A 1 119 ? 13.251 -1.565  17.489  1.00 5.27  ? 119 HIS A CE1 1 
ATOM   938  N  NE2 . HIS A 1 119 ? 12.096 -1.937  18.053  1.00 5.10  ? 119 HIS A NE2 1 
ATOM   939  N  N   . LEU A 1 120 ? 7.772  2.135   15.515  1.00 6.27  ? 120 LEU A N   1 
ATOM   940  C  CA  . LEU A 1 120 ? 7.150  3.373   15.051  1.00 6.66  ? 120 LEU A CA  1 
ATOM   941  C  C   . LEU A 1 120 ? 7.730  4.532   15.833  1.00 6.56  ? 120 LEU A C   1 
ATOM   942  O  O   . LEU A 1 120 ? 7.608  4.554   17.057  1.00 7.15  ? 120 LEU A O   1 
ATOM   943  C  CB  . LEU A 1 120 ? 5.642  3.291   15.239  1.00 6.90  ? 120 LEU A CB  1 
ATOM   944  C  CG  . LEU A 1 120 ? 4.995  2.217   14.361  1.00 7.75  ? 120 LEU A CG  1 
ATOM   945  C  CD1 . LEU A 1 120 ? 4.212  1.270   15.230  1.00 8.48  ? 120 LEU A CD1 1 
ATOM   946  C  CD2 . LEU A 1 120 ? 4.147  2.829   13.231  1.00 7.94  ? 120 LEU A CD2 1 
ATOM   947  N  N   . VAL A 1 121 ? 8.472  5.380   15.110  1.00 6.99  ? 121 VAL A N   1 
ATOM   948  C  CA  . VAL A 1 121 ? 9.342  6.374   15.744  1.00 6.94  ? 121 VAL A CA  1 
ATOM   949  C  C   . VAL A 1 121 ? 8.638  7.720   15.801  1.00 7.42  ? 121 VAL A C   1 
ATOM   950  O  O   . VAL A 1 121 ? 8.248  8.248   14.747  1.00 7.02  ? 121 VAL A O   1 
ATOM   951  C  CB  . VAL A 1 121 ? 10.693 6.490   14.990  1.00 6.66  ? 121 VAL A CB  1 
ATOM   952  C  CG1 . VAL A 1 121 ? 11.623 7.534   15.619  1.00 6.24  ? 121 VAL A CG1 1 
ATOM   953  C  CG2 . VAL A 1 121 ? 11.398 5.167   14.765  1.00 6.60  ? 121 VAL A CG2 1 
ATOM   954  N  N   . HIS A 1 122 ? 8.573  8.343   17.011  1.00 7.21  ? 122 HIS A N   1 
ATOM   955  C  CA  . HIS A 1 122 ? 7.813  9.589   17.169  1.00 7.83  ? 122 HIS A CA  1 
ATOM   956  C  C   . HIS A 1 122 ? 8.664  10.586  17.948  1.00 7.96  ? 122 HIS A C   1 
ATOM   957  O  O   . HIS A 1 122 ? 9.424  10.190  18.829  1.00 8.00  ? 122 HIS A O   1 
ATOM   958  C  CB  . HIS A 1 122 ? 6.515  9.399   17.960  1.00 7.69  ? 122 HIS A CB  1 
ATOM   959  C  CG  . HIS A 1 122 ? 5.656  8.255   17.534  1.00 8.20  ? 122 HIS A CG  1 
ATOM   960  N  ND1 . HIS A 1 122 ? 5.986  6.951   17.800  1.00 7.87  ? 122 HIS A ND1 1 
ATOM   961  C  CD2 . HIS A 1 122 ? 4.439  8.237   16.929  1.00 8.86  ? 122 HIS A CD2 1 
ATOM   962  C  CE1 . HIS A 1 122 ? 5.008  6.146   17.354  1.00 9.31  ? 122 HIS A CE1 1 
ATOM   963  N  NE2 . HIS A 1 122 ? 4.052  6.908   16.816  1.00 8.75  ? 122 HIS A NE2 1 
ATOM   964  N  N   . TRP A 1 123 ? 8.556  11.866  17.600  1.00 8.53  ? 123 TRP A N   1 
ATOM   965  C  CA  . TRP A 1 123 ? 9.342  12.863  18.317  1.00 8.59  ? 123 TRP A CA  1 
ATOM   966  C  C   . TRP A 1 123 ? 8.448  13.891  19.018  1.00 9.08  ? 123 TRP A C   1 
ATOM   967  O  O   . TRP A 1 123 ? 7.380  14.246  18.524  1.00 9.14  ? 123 TRP A O   1 
ATOM   968  C  CB  . TRP A 1 123 ? 10.346 13.520  17.367  1.00 9.92  ? 123 TRP A CB  1 
ATOM   969  C  CG  . TRP A 1 123 ? 9.751  14.195  16.167  1.00 10.73 ? 123 TRP A CG  1 
ATOM   970  C  CD1 . TRP A 1 123 ? 9.575  13.631  14.929  1.00 12.15 ? 123 TRP A CD1 1 
ATOM   971  C  CD2 . TRP A 1 123 ? 9.314  15.563  16.061  1.00 12.59 ? 123 TRP A CD2 1 
ATOM   972  N  NE1 . TRP A 1 123 ? 9.015  14.538  14.071  1.00 12.84 ? 123 TRP A NE1 1 
ATOM   973  C  CE2 . TRP A 1 123 ? 8.851  15.736  14.732  1.00 12.49 ? 123 TRP A CE2 1 
ATOM   974  C  CE3 . TRP A 1 123 ? 9.259  16.647  16.950  1.00 12.40 ? 123 TRP A CE3 1 
ATOM   975  C  CZ2 . TRP A 1 123 ? 8.320  16.944  14.271  1.00 13.42 ? 123 TRP A CZ2 1 
ATOM   976  C  CZ3 . TRP A 1 123 ? 8.690  17.832  16.505  1.00 13.58 ? 123 TRP A CZ3 1 
ATOM   977  C  CH2 . TRP A 1 123 ? 8.288  17.991  15.161  1.00 13.98 ? 123 TRP A CH2 1 
ATOM   978  N  N   . ASN A 1 124 ? 8.938  14.365  20.177  1.00 9.42  ? 124 ASN A N   1 
ATOM   979  C  CA  . ASN A 1 124 ? 8.226  15.269  21.071  1.00 9.64  ? 124 ASN A CA  1 
ATOM   980  C  C   . ASN A 1 124 ? 8.071  16.654  20.441  1.00 9.94  ? 124 ASN A C   1 
ATOM   981  O  O   . ASN A 1 124 ? 9.058  17.312  20.158  1.00 8.51  ? 124 ASN A O   1 
ATOM   982  C  CB  . ASN A 1 124 ? 9.019  15.388  22.367  1.00 10.90 ? 124 ASN A CB  1 
ATOM   983  C  CG  . ASN A 1 124 ? 8.156  15.942  23.478  1.00 11.61 ? 124 ASN A CG  1 
ATOM   984  O  OD1 . ASN A 1 124 ? 7.335  16.825  23.220  1.00 13.19 ? 124 ASN A OD1 1 
ATOM   985  N  ND2 . ASN A 1 124 ? 8.332  15.404  24.678  1.00 12.83 ? 124 ASN A ND2 1 
ATOM   986  N  N   . THR A 1 125 ? 6.821  17.124  20.240  1.00 11.17 ? 125 THR A N   1 
ATOM   987  C  CA  . THR A 1 125 ? 6.618  18.336  19.452  1.00 13.29 ? 125 THR A CA  1 
ATOM   988  C  C   . THR A 1 125 ? 7.047  19.590  20.209  1.00 13.76 ? 125 THR A C   1 
ATOM   989  O  O   . THR A 1 125 ? 6.963  20.679  19.600  1.00 14.80 ? 125 THR A O   1 
ATOM   990  C  CB  . THR A 1 125 ? 5.133  18.518  19.105  1.00 13.93 ? 125 THR A CB  1 
ATOM   991  O  OG1 . THR A 1 125 ? 4.400  18.466  20.326  1.00 15.90 ? 125 THR A OG1 1 
ATOM   992  C  CG2 . THR A 1 125 ? 4.600  17.373  18.263  1.00 16.35 ? 125 THR A CG2 1 
ATOM   993  N  N   . LYS A 1 126 ? 7.424  19.455  21.483  1.00 13.44 ? 127 LYS A N   1 
ATOM   994  C  CA  . LYS A 1 126 ? 7.879  20.657  22.227  1.00 14.59 ? 127 LYS A CA  1 
ATOM   995  C  C   . LYS A 1 126 ? 9.303  20.981  21.773  1.00 14.83 ? 127 LYS A C   1 
ATOM   996  O  O   . LYS A 1 126 ? 9.792  22.060  22.092  1.00 15.63 ? 127 LYS A O   1 
ATOM   997  C  CB  . LYS A 1 126 ? 7.761  20.493  23.747  1.00 16.22 ? 127 LYS A CB  1 
ATOM   998  C  CG  . LYS A 1 126 ? 8.814  19.629  24.404  1.00 18.08 ? 127 LYS A CG  1 
ATOM   999  C  CD  . LYS A 1 126 ? 8.447  19.368  25.864  1.00 22.76 ? 127 LYS A CD  1 
ATOM   1000 C  CE  . LYS A 1 126 ? 9.529  18.509  26.462  1.00 23.53 ? 127 LYS A CE  1 
ATOM   1001 N  NZ  . LYS A 1 126 ? 9.182  17.958  27.794  1.00 31.20 ? 127 LYS A NZ  1 
ATOM   1002 N  N   . TYR A 1 127 ? 9.994  20.072  21.073  1.00 12.39 ? 128 TYR A N   1 
ATOM   1003 C  CA  . TYR A 1 127 ? 11.351 20.345  20.593  1.00 12.89 ? 128 TYR A CA  1 
ATOM   1004 C  C   . TYR A 1 127 ? 11.390 20.802  19.129  1.00 14.91 ? 128 TYR A C   1 
ATOM   1005 O  O   . TYR A 1 127 ? 12.463 21.099  18.592  1.00 15.86 ? 128 TYR A O   1 
ATOM   1006 C  CB  . TYR A 1 127 ? 12.261 19.134  20.786  1.00 12.48 ? 128 TYR A CB  1 
ATOM   1007 C  CG  . TYR A 1 127 ? 12.423 18.860  22.252  1.00 11.91 ? 128 TYR A CG  1 
ATOM   1008 C  CD1 . TYR A 1 127 ? 12.839 19.874  23.114  1.00 14.45 ? 128 TYR A CD1 1 
ATOM   1009 C  CD2 . TYR A 1 127 ? 12.110 17.625  22.791  1.00 12.29 ? 128 TYR A CD2 1 
ATOM   1010 C  CE1 . TYR A 1 127 ? 12.954 19.625  24.477  1.00 13.08 ? 128 TYR A CE1 1 
ATOM   1011 C  CE2 . TYR A 1 127 ? 12.215 17.355  24.144  1.00 12.94 ? 128 TYR A CE2 1 
ATOM   1012 C  CZ  . TYR A 1 127 ? 12.680 18.369  24.980  1.00 13.53 ? 128 TYR A CZ  1 
ATOM   1013 O  OH  . TYR A 1 127 ? 12.772 18.116  26.309  1.00 14.24 ? 128 TYR A OH  1 
ATOM   1014 N  N   . GLY A 1 128 ? 10.219 20.869  18.501  1.00 12.81 ? 129 GLY A N   1 
ATOM   1015 C  CA  . GLY A 1 128 ? 10.087 21.546  17.210  1.00 13.93 ? 129 GLY A CA  1 
ATOM   1016 C  C   . GLY A 1 128 ? 10.513 20.707  16.000  1.00 14.92 ? 129 GLY A C   1 
ATOM   1017 O  O   . GLY A 1 128 ? 9.947  20.835  14.900  1.00 14.75 ? 129 GLY A O   1 
ATOM   1018 N  N   . ASP A 1 129 ? 11.567 19.902  16.139  1.00 14.11 ? 130 ASP A N   1 
ATOM   1019 C  CA  . ASP A 1 129 ? 11.806 18.940  15.065  1.00 16.92 ? 130 ASP A CA  1 
ATOM   1020 C  C   . ASP A 1 129 ? 12.544 17.715  15.581  1.00 16.87 ? 130 ASP A C   1 
ATOM   1021 O  O   . ASP A 1 129 ? 12.968 17.675  16.739  1.00 14.45 ? 130 ASP A O   1 
ATOM   1022 C  CB  . ASP A 1 129 ? 12.479 19.567  13.841  1.00 19.92 ? 130 ASP A CB  1 
ATOM   1023 C  CG  . ASP A 1 129 ? 13.914 20.004  13.990  1.00 23.29 ? 130 ASP A CG  1 
ATOM   1024 O  OD1 . ASP A 1 129 ? 14.579 19.656  14.978  1.00 26.46 ? 130 ASP A OD1 1 
ATOM   1025 O  OD2 . ASP A 1 129 ? 14.393 20.620  13.053  1.00 29.65 ? 130 ASP A OD2 1 
ATOM   1026 N  N   . PHE A 1 130 ? 12.690 16.732  14.682  1.00 14.66 ? 131 PHE A N   1 
ATOM   1027 C  CA  . PHE A 1 130 ? 13.345 15.485  15.033  1.00 15.24 ? 131 PHE A CA  1 
ATOM   1028 C  C   . PHE A 1 130 ? 14.812 15.677  15.407  1.00 14.45 ? 131 PHE A C   1 
ATOM   1029 O  O   . PHE A 1 130 ? 15.287 15.052  16.349  1.00 12.10 ? 131 PHE A O   1 
ATOM   1030 C  CB  . PHE A 1 130 ? 13.167 14.465  13.906  1.00 14.74 ? 131 PHE A CB  1 
ATOM   1031 C  CG  . PHE A 1 130 ? 13.994 13.230  14.099  1.00 14.94 ? 131 PHE A CG  1 
ATOM   1032 C  CD1 . PHE A 1 130 ? 15.313 13.187  13.670  1.00 18.09 ? 131 PHE A CD1 1 
ATOM   1033 C  CD2 . PHE A 1 130 ? 13.469 12.131  14.760  1.00 15.08 ? 131 PHE A CD2 1 
ATOM   1034 C  CE1 . PHE A 1 130 ? 16.096 12.058  13.860  1.00 18.84 ? 131 PHE A CE1 1 
ATOM   1035 C  CE2 . PHE A 1 130 ? 14.242 11.000  14.933  1.00 16.93 ? 131 PHE A CE2 1 
ATOM   1036 C  CZ  . PHE A 1 130 ? 15.551 10.969  14.502  1.00 21.06 ? 131 PHE A CZ  1 
ATOM   1037 N  N   . GLY A 1 131 ? 15.548 16.487  14.626  1.00 13.49 ? 132 GLY A N   1 
ATOM   1038 C  CA  . GLY A 1 131 ? 16.956 16.702  14.918  1.00 14.80 ? 132 GLY A CA  1 
ATOM   1039 C  C   . GLY A 1 131 ? 17.191 17.297  16.309  1.00 14.71 ? 132 GLY A C   1 
ATOM   1040 O  O   . GLY A 1 131 ? 18.178 16.974  16.957  1.00 17.32 ? 132 GLY A O   1 
ATOM   1041 N  N   . LYS A 1 132 ? 16.300 18.179  16.781  1.00 14.03 ? 133 LYS A N   1 
ATOM   1042 C  CA  . LYS A 1 132 ? 16.489 18.711  18.128  1.00 13.52 ? 133 LYS A CA  1 
ATOM   1043 C  C   . LYS A 1 132 ? 16.056 17.693  19.173  1.00 13.57 ? 133 LYS A C   1 
ATOM   1044 O  O   . LYS A 1 132 ? 16.623 17.605  20.261  1.00 12.85 ? 133 LYS A O   1 
ATOM   1045 C  CB  . LYS A 1 132 ? 15.660 19.975  18.336  1.00 15.57 ? 133 LYS A CB  1 
ATOM   1046 C  CG  . LYS A 1 132 ? 16.188 21.208  17.602  1.00 21.21 ? 133 LYS A CG  1 
ATOM   1047 C  CD  . LYS A 1 132 ? 17.700 21.235  17.387  1.00 24.65 ? 133 LYS A CD  1 
ATOM   1048 C  CE  . LYS A 1 132 ? 18.463 21.603  18.645  1.00 30.70 ? 133 LYS A CE  1 
ATOM   1049 N  NZ  . LYS A 1 132 ? 17.847 22.779  19.322  1.00 33.82 ? 133 LYS A NZ  1 
ATOM   1050 N  N   . ALA A 1 133 ? 14.970 16.990  18.870  1.00 12.15 ? 134 ALA A N   1 
ATOM   1051 C  CA  . ALA A 1 133 ? 14.433 16.022  19.818  1.00 11.82 ? 134 ALA A CA  1 
ATOM   1052 C  C   . ALA A 1 133 ? 15.430 14.924  20.197  1.00 11.55 ? 134 ALA A C   1 
ATOM   1053 O  O   . ALA A 1 133 ? 15.407 14.480  21.351  1.00 12.46 ? 134 ALA A O   1 
ATOM   1054 C  CB  . ALA A 1 133 ? 13.130 15.447  19.257  1.00 10.06 ? 134 ALA A CB  1 
ATOM   1055 N  N   . VAL A 1 134 ? 16.273 14.441  19.269  1.00 11.26 ? 135 VAL A N   1 
ATOM   1056 C  CA  . VAL A 1 134 ? 17.158 13.324  19.615  1.00 12.96 ? 135 VAL A CA  1 
ATOM   1057 C  C   . VAL A 1 134 ? 18.235 13.791  20.596  1.00 12.30 ? 135 VAL A C   1 
ATOM   1058 O  O   . VAL A 1 134 ? 18.963 12.986  21.169  1.00 11.80 ? 135 VAL A O   1 
ATOM   1059 C  CB  . VAL A 1 134 ? 17.844 12.652  18.396  1.00 14.17 ? 135 VAL A CB  1 
ATOM   1060 C  CG1 . VAL A 1 134 ? 16.865 11.909  17.536  1.00 14.79 ? 135 VAL A CG1 1 
ATOM   1061 C  CG2 . VAL A 1 134 ? 18.730 13.601  17.590  1.00 14.53 ? 135 VAL A CG2 1 
ATOM   1062 N  N   . GLN A 1 135 ? 18.353 15.107  20.776  1.00 11.67 ? 136 GLN A N   1 
ATOM   1063 C  CA  . GLN A 1 135 ? 19.351 15.626  21.696  1.00 14.73 ? 136 GLN A CA  1 
ATOM   1064 C  C   . GLN A 1 135 ? 18.811 15.734  23.129  1.00 13.83 ? 136 GLN A C   1 
ATOM   1065 O  O   . GLN A 1 135 ? 19.479 16.253  24.038  1.00 13.53 ? 136 GLN A O   1 
ATOM   1066 C  CB  . GLN A 1 135 ? 19.896 16.963  21.133  1.00 16.22 ? 136 GLN A CB  1 
ATOM   1067 C  CG  . GLN A 1 135 ? 20.719 16.789  19.862  1.00 21.31 ? 136 GLN A CG  1 
ATOM   1068 C  CD  . GLN A 1 135 ? 21.961 15.910  20.011  1.00 28.60 ? 136 GLN A CD  1 
ATOM   1069 O  OE1 . GLN A 1 135 ? 22.644 15.892  21.041  1.00 36.17 ? 136 GLN A OE1 1 
ATOM   1070 N  NE2 . GLN A 1 135 ? 22.289 15.149  18.970  1.00 33.06 ? 136 GLN A NE2 1 
ATOM   1071 N  N   . GLN A 1 136 ? 17.570 15.297  23.352  1.00 12.62 ? 137 GLN A N   1 
ATOM   1072 C  CA  . GLN A 1 136 ? 16.913 15.524  24.639  1.00 11.86 ? 137 GLN A CA  1 
ATOM   1073 C  C   . GLN A 1 136 ? 16.524 14.191  25.263  1.00 11.55 ? 137 GLN A C   1 
ATOM   1074 O  O   . GLN A 1 136 ? 16.111 13.248  24.576  1.00 9.09  ? 137 GLN A O   1 
ATOM   1075 C  CB  . GLN A 1 136 ? 15.631 16.337  24.498  1.00 12.55 ? 137 GLN A CB  1 
ATOM   1076 C  CG  . GLN A 1 136 ? 15.763 17.593  23.643  1.00 17.33 ? 137 GLN A CG  1 
ATOM   1077 C  CD  . GLN A 1 136 ? 16.794 18.539  24.206  1.00 19.76 ? 137 GLN A CD  1 
ATOM   1078 O  OE1 . GLN A 1 136 ? 16.946 18.645  25.414  1.00 18.76 ? 137 GLN A OE1 1 
ATOM   1079 N  NE2 . GLN A 1 136 ? 17.589 19.114  23.310  1.00 26.32 ? 137 GLN A NE2 1 
ATOM   1080 N  N   . PRO A 1 137 ? 16.598 14.066  26.607  1.00 11.50 ? 138 PRO A N   1 
ATOM   1081 C  CA  . PRO A 1 137 ? 16.325 12.776  27.249  1.00 12.15 ? 138 PRO A CA  1 
ATOM   1082 C  C   . PRO A 1 137 ? 14.883 12.305  27.100  1.00 12.27 ? 138 PRO A C   1 
ATOM   1083 O  O   . PRO A 1 137 ? 14.617 11.098  27.225  1.00 12.16 ? 138 PRO A O   1 
ATOM   1084 C  CB  . PRO A 1 137 ? 16.708 12.994  28.718  1.00 13.66 ? 138 PRO A CB  1 
ATOM   1085 C  CG  . PRO A 1 137 ? 16.660 14.503  28.884  1.00 14.69 ? 138 PRO A CG  1 
ATOM   1086 C  CD  . PRO A 1 137 ? 16.952 15.153  27.535  1.00 14.81 ? 138 PRO A CD  1 
ATOM   1087 N  N   . ASP A 1 138 ? 13.959 13.236  26.806  1.00 10.21 ? 139 ASP A N   1 
ATOM   1088 C  CA  . ASP A 1 138 ? 12.571 12.835  26.570  1.00 11.08 ? 139 ASP A CA  1 
ATOM   1089 C  C   . ASP A 1 138 ? 12.124 13.223  25.151  1.00 9.46  ? 139 ASP A C   1 
ATOM   1090 O  O   . ASP A 1 138 ? 10.972 13.635  24.932  1.00 9.73  ? 139 ASP A O   1 
ATOM   1091 C  CB  . ASP A 1 138 ? 11.635 13.503  27.596  1.00 12.29 ? 139 ASP A CB  1 
ATOM   1092 C  CG  . ASP A 1 138 ? 11.743 15.009  27.638  1.00 13.99 ? 139 ASP A CG  1 
ATOM   1093 O  OD1 . ASP A 1 138 ? 12.640 15.570  26.987  1.00 16.30 ? 139 ASP A OD1 1 
ATOM   1094 O  OD2 . ASP A 1 138 ? 10.886 15.614  28.278  1.00 17.39 ? 139 ASP A OD2 1 
ATOM   1095 N  N   . GLY A 1 139 ? 13.055 13.132  24.181  1.00 8.76  ? 140 GLY A N   1 
ATOM   1096 C  CA  . GLY A 1 139 ? 12.784 13.680  22.863  1.00 7.87  ? 140 GLY A CA  1 
ATOM   1097 C  C   . GLY A 1 139 ? 12.008 12.725  21.970  1.00 7.90  ? 140 GLY A C   1 
ATOM   1098 O  O   . GLY A 1 139 ? 11.314 13.186  21.077  1.00 7.44  ? 140 GLY A O   1 
ATOM   1099 N  N   . LEU A 1 140 ? 12.175 11.410  22.185  1.00 7.77  ? 141 LEU A N   1 
ATOM   1100 C  CA  . LEU A 1 140 ? 11.613 10.419  21.271  1.00 7.51  ? 141 LEU A CA  1 
ATOM   1101 C  C   . LEU A 1 140 ? 10.701 9.463   22.042  1.00 7.21  ? 141 LEU A C   1 
ATOM   1102 O  O   . LEU A 1 140 ? 10.916 9.159   23.219  1.00 7.09  ? 141 LEU A O   1 
ATOM   1103 C  CB  . LEU A 1 140 ? 12.739 9.577   20.642  1.00 9.08  ? 141 LEU A CB  1 
ATOM   1104 C  CG  . LEU A 1 140 ? 13.425 10.101  19.385  1.00 12.75 ? 141 LEU A CG  1 
ATOM   1105 C  CD1 . LEU A 1 140 ? 12.431 10.121  18.231  1.00 14.15 ? 141 LEU A CD1 1 
ATOM   1106 C  CD2 . LEU A 1 140 ? 13.903 11.518  19.604  1.00 13.85 ? 141 LEU A CD2 1 
ATOM   1107 N  N   . ALA A 1 141 ? 9.666  8.979   21.355  1.00 6.83  ? 142 ALA A N   1 
ATOM   1108 C  CA  . ALA A 1 141 ? 8.904  7.834   21.894  1.00 6.75  ? 142 ALA A CA  1 
ATOM   1109 C  C   . ALA A 1 141 ? 8.822  6.791   20.764  1.00 7.02  ? 142 ALA A C   1 
ATOM   1110 O  O   . ALA A 1 141 ? 8.459  7.131   19.653  1.00 7.39  ? 142 ALA A O   1 
ATOM   1111 C  CB  . ALA A 1 141 ? 7.529  8.282   22.342  1.00 7.52  ? 142 ALA A CB  1 
ATOM   1112 N  N   . VAL A 1 142 ? 9.261  5.549   21.032  1.00 7.10  ? 143 VAL A N   1 
ATOM   1113 C  CA  . VAL A 1 142 ? 9.273  4.513   20.013  1.00 6.61  ? 143 VAL A CA  1 
ATOM   1114 C  C   . VAL A 1 142 ? 8.289  3.440   20.468  1.00 6.58  ? 143 VAL A C   1 
ATOM   1115 O  O   . VAL A 1 142 ? 8.444  2.924   21.589  1.00 6.77  ? 143 VAL A O   1 
ATOM   1116 C  CB  . VAL A 1 142 ? 10.661 3.929   19.668  1.00 6.67  ? 143 VAL A CB  1 
ATOM   1117 C  CG1 . VAL A 1 142 ? 10.541 2.967   18.480  1.00 7.16  ? 143 VAL A CG1 1 
ATOM   1118 C  CG2 . VAL A 1 142 ? 11.600 5.068   19.252  1.00 7.63  ? 143 VAL A CG2 1 
ATOM   1119 N  N   . LEU A 1 143 ? 7.308  3.142   19.605  1.00 5.69  ? 144 LEU A N   1 
ATOM   1120 C  CA  . LEU A 1 143 ? 6.319  2.112   19.919  1.00 6.56  ? 144 LEU A CA  1 
ATOM   1121 C  C   . LEU A 1 143 ? 6.834  0.851   19.230  1.00 6.51  ? 144 LEU A C   1 
ATOM   1122 O  O   . LEU A 1 143 ? 6.995  0.865   18.015  1.00 7.30  ? 144 LEU A O   1 
ATOM   1123 C  CB  . LEU A 1 143 ? 4.950  2.571   19.360  1.00 7.01  ? 144 LEU A CB  1 
ATOM   1124 C  CG  . LEU A 1 143 ? 3.804  1.573   19.468  1.00 7.32  ? 144 LEU A CG  1 
ATOM   1125 C  CD1 . LEU A 1 143 ? 3.557  1.251   20.939  1.00 7.90  ? 144 LEU A CD1 1 
ATOM   1126 C  CD2 . LEU A 1 143 ? 2.555  2.153   18.786  1.00 8.28  ? 144 LEU A CD2 1 
ATOM   1127 N  N   . GLY A 1 144 ? 7.142  -0.195  20.020  1.00 6.33  ? 145 GLY A N   1 
ATOM   1128 C  CA  . GLY A 1 144 ? 7.702  -1.428  19.497  1.00 6.28  ? 145 GLY A CA  1 
ATOM   1129 C  C   . GLY A 1 144 ? 6.636  -2.513  19.500  1.00 6.60  ? 145 GLY A C   1 
ATOM   1130 O  O   . GLY A 1 144 ? 5.918  -2.663  20.480  1.00 6.68  ? 145 GLY A O   1 
ATOM   1131 N  N   . ILE A 1 145 ? 6.545  -3.257  18.397  1.00 6.88  ? 146 ILE A N   1 
ATOM   1132 C  CA  . ILE A 1 145 ? 5.522  -4.291  18.268  1.00 6.80  ? 146 ILE A CA  1 
ATOM   1133 C  C   . ILE A 1 145 ? 6.234  -5.549  17.775  1.00 7.16  ? 146 ILE A C   1 
ATOM   1134 O  O   . ILE A 1 145 ? 6.925  -5.506  16.772  1.00 7.26  ? 146 ILE A O   1 
ATOM   1135 C  CB  . ILE A 1 145 ? 4.449  -3.810  17.269  1.00 7.03  ? 146 ILE A CB  1 
ATOM   1136 C  CG1 . ILE A 1 145 ? 3.837  -2.480  17.740  1.00 7.11  ? 146 ILE A CG1 1 
ATOM   1137 C  CG2 . ILE A 1 145 ? 3.414  -4.931  17.087  1.00 7.64  ? 146 ILE A CG2 1 
ATOM   1138 C  CD1 . ILE A 1 145 ? 2.717  -1.908  16.822  1.00 7.30  ? 146 ILE A CD1 1 
ATOM   1139 N  N   . PHE A 1 146 ? 6.059  -6.676  18.467  1.00 8.22  ? 147 PHE A N   1 
ATOM   1140 C  CA  . PHE A 1 146 ? 6.709  -7.910  18.024  1.00 6.90  ? 147 PHE A CA  1 
ATOM   1141 C  C   . PHE A 1 146 ? 5.922  -8.557  16.879  1.00 7.78  ? 147 PHE A C   1 
ATOM   1142 O  O   . PHE A 1 146 ? 4.714  -8.382  16.775  1.00 7.39  ? 147 PHE A O   1 
ATOM   1143 C  CB  . PHE A 1 146 ? 6.715  -8.895  19.195  1.00 7.09  ? 147 PHE A CB  1 
ATOM   1144 C  CG  . PHE A 1 146 ? 7.556  -8.416  20.356  1.00 6.93  ? 147 PHE A CG  1 
ATOM   1145 C  CD1 . PHE A 1 146 ? 8.931  -8.267  20.198  1.00 7.63  ? 147 PHE A CD1 1 
ATOM   1146 C  CD2 . PHE A 1 146 ? 7.009  -8.164  21.599  1.00 7.68  ? 147 PHE A CD2 1 
ATOM   1147 C  CE1 . PHE A 1 146 ? 9.737  -7.852  21.251  1.00 7.28  ? 147 PHE A CE1 1 
ATOM   1148 C  CE2 . PHE A 1 146 ? 7.806  -7.776  22.670  1.00 8.22  ? 147 PHE A CE2 1 
ATOM   1149 C  CZ  . PHE A 1 146 ? 9.170  -7.617  22.487  1.00 7.89  ? 147 PHE A CZ  1 
ATOM   1150 N  N   . LEU A 1 147 ? 6.641  -9.262  16.000  1.00 7.44  ? 148 LEU A N   1 
ATOM   1151 C  CA  . LEU A 1 147 ? 6.032  -10.036 14.919  1.00 7.68  ? 148 LEU A CA  1 
ATOM   1152 C  C   . LEU A 1 147 ? 6.357  -11.498 15.170  1.00 8.66  ? 148 LEU A C   1 
ATOM   1153 O  O   . LEU A 1 147 ? 7.519  -11.827 15.322  1.00 7.80  ? 148 LEU A O   1 
ATOM   1154 C  CB  . LEU A 1 147 ? 6.646  -9.594  13.570  1.00 7.89  ? 148 LEU A CB  1 
ATOM   1155 C  CG  . LEU A 1 147 ? 6.020  -8.382  12.861  1.00 7.88  ? 148 LEU A CG  1 
ATOM   1156 C  CD1 . LEU A 1 147 ? 6.184  -7.082  13.688  1.00 8.29  ? 148 LEU A CD1 1 
ATOM   1157 C  CD2 . LEU A 1 147 ? 6.699  -8.201  11.509  1.00 8.38  ? 148 LEU A CD2 1 
ATOM   1158 N  N   . LYS A 1 148 ? 5.320  -12.356 15.127  1.00 9.44  ? 149 LYS A N   1 
ATOM   1159 C  CA  . LYS A 1 148 ? 5.542  -13.779 15.091  1.00 9.99  ? 149 LYS A CA  1 
ATOM   1160 C  C   . LYS A 1 148 ? 5.073  -14.273 13.721  1.00 10.97 ? 149 LYS A C   1 
ATOM   1161 O  O   . LYS A 1 148 ? 4.226  -13.672 13.072  1.00 10.18 ? 149 LYS A O   1 
ATOM   1162 C  CB  . LYS A 1 148 ? 4.809  -14.484 16.234  1.00 12.16 ? 149 LYS A CB  1 
ATOM   1163 C  CG  . LYS A 1 148 ? 3.294  -14.370 16.189  1.00 15.43 ? 149 LYS A CG  1 
ATOM   1164 C  CD  . LYS A 1 148 ? 2.683  -15.107 17.393  1.00 20.88 ? 149 LYS A CD  1 
ATOM   1165 C  CE  . LYS A 1 148 ? 1.177  -15.217 17.268  1.00 23.85 ? 149 LYS A CE  1 
ATOM   1166 N  NZ  . LYS A 1 148 ? 0.497  -15.394 18.580  1.00 29.99 ? 149 LYS A NZ  1 
ATOM   1167 N  N   . VAL A 1 149 ? 5.598  -15.431 13.329  1.00 11.44 ? 150 VAL A N   1 
ATOM   1168 C  CA  . VAL A 1 149 ? 5.213  -15.990 12.051  1.00 11.93 ? 150 VAL A CA  1 
ATOM   1169 C  C   . VAL A 1 149 ? 4.014  -16.919 12.285  1.00 12.84 ? 150 VAL A C   1 
ATOM   1170 O  O   . VAL A 1 149 ? 4.017  -17.838 13.140  1.00 13.52 ? 150 VAL A O   1 
ATOM   1171 C  CB  . VAL A 1 149 ? 6.408  -16.732 11.433  1.00 13.30 ? 150 VAL A CB  1 
ATOM   1172 C  CG1 . VAL A 1 149 ? 5.983  -17.533 10.207  1.00 13.58 ? 150 VAL A CG1 1 
ATOM   1173 C  CG2 . VAL A 1 149 ? 7.493  -15.754 11.034  1.00 13.83 ? 150 VAL A CG2 1 
ATOM   1174 N  N   . GLY A 1 150 ? 3.009  -16.689 11.460  1.00 10.83 ? 151 GLY A N   1 
ATOM   1175 C  CA  . GLY A 1 150 ? 1.742  -17.407 11.520  1.00 12.95 ? 151 GLY A CA  1 
ATOM   1176 C  C   . GLY A 1 150 ? 0.830  -17.013 10.358  1.00 11.22 ? 151 GLY A C   1 
ATOM   1177 O  O   . GLY A 1 150 ? 1.216  -17.145 9.194   1.00 11.05 ? 151 GLY A O   1 
ATOM   1178 N  N   . SER A 1 151 ? -0.385 -16.519 10.700  1.00 13.49 ? 152 SER A N   1 
ATOM   1179 C  CA  . SER A 1 151 ? -1.264 -15.986 9.657   1.00 14.85 ? 152 SER A CA  1 
ATOM   1180 C  C   . SER A 1 151 ? -0.687 -14.666 9.106   1.00 16.25 ? 152 SER A C   1 
ATOM   1181 O  O   . SER A 1 151 ? 0.104  -14.004 9.786   1.00 13.71 ? 152 SER A O   1 
ATOM   1182 C  CB  . SER A 1 151 ? -2.660 -15.848 10.182  1.00 20.18 ? 152 SER A CB  1 
ATOM   1183 O  OG  . SER A 1 151 ? -2.766 -14.691 10.999  1.00 24.13 ? 152 SER A OG  1 
ATOM   1184 N  N   . ALA A 1 152 ? -0.968 -14.340 7.826   1.00 13.17 ? 153 ALA A N   1 
ATOM   1185 C  CA  . ALA A 1 152 ? -0.509 -13.087 7.237   1.00 12.14 ? 153 ALA A CA  1 
ATOM   1186 C  C   . ALA A 1 152 ? -1.158 -11.897 7.947   1.00 12.19 ? 153 ALA A C   1 
ATOM   1187 O  O   . ALA A 1 152 ? -2.262 -12.002 8.492   1.00 12.72 ? 153 ALA A O   1 
ATOM   1188 C  CB  . ALA A 1 152 ? -0.778 -13.045 5.740   1.00 13.96 ? 153 ALA A CB  1 
ATOM   1189 N  N   . LYS A 1 153 ? -0.480 -10.741 7.852   1.00 11.76 ? 154 LYS A N   1 
ATOM   1190 C  CA  . LYS A 1 153 ? -1.031 -9.474  8.312   1.00 11.76 ? 154 LYS A CA  1 
ATOM   1191 C  C   . LYS A 1 153 ? -1.419 -8.695  7.060   1.00 12.15 ? 154 LYS A C   1 
ATOM   1192 O  O   . LYS A 1 153 ? -0.563 -8.211  6.309   1.00 12.36 ? 154 LYS A O   1 
ATOM   1193 C  CB  . LYS A 1 153 ? 0.026  -8.670  9.093   1.00 12.75 ? 154 LYS A CB  1 
ATOM   1194 C  CG  . LYS A 1 153 ? -0.521 -7.503  9.888   1.00 14.09 ? 154 LYS A CG  1 
ATOM   1195 C  CD  . LYS A 1 153 ? -1.404 -7.936  11.022  1.00 13.90 ? 154 LYS A CD  1 
ATOM   1196 C  CE  . LYS A 1 153 ? -1.717 -6.771  11.950  1.00 16.67 ? 154 LYS A CE  1 
ATOM   1197 N  NZ  . LYS A 1 153 ? -2.598 -7.216  13.044  1.00 16.39 ? 154 LYS A NZ  1 
ATOM   1198 N  N   A PRO A 1 154 ? -2.723 -8.628  6.715   0.50 12.79 ? 155 PRO A N   1 
ATOM   1199 N  N   B PRO A 1 154 ? -2.739 -8.572  6.783   0.50 13.23 ? 155 PRO A N   1 
ATOM   1200 C  CA  A PRO A 1 154 ? -3.117 -8.001  5.445   0.50 13.19 ? 155 PRO A CA  1 
ATOM   1201 C  CA  B PRO A 1 154 ? -3.199 -7.975  5.522   0.50 13.85 ? 155 PRO A CA  1 
ATOM   1202 C  C   A PRO A 1 154 ? -2.644 -6.551  5.340   0.50 13.08 ? 155 PRO A C   1 
ATOM   1203 C  C   B PRO A 1 154 ? -2.617 -6.577  5.363   0.50 13.49 ? 155 PRO A C   1 
ATOM   1204 O  O   A PRO A 1 154 ? -2.247 -6.117  4.262   0.50 13.38 ? 155 PRO A O   1 
ATOM   1205 O  O   B PRO A 1 154 ? -2.146 -6.208  4.290   0.50 13.85 ? 155 PRO A O   1 
ATOM   1206 C  CB  A PRO A 1 154 ? -4.648 -8.184  5.442   0.50 13.03 ? 155 PRO A CB  1 
ATOM   1207 C  CB  B PRO A 1 154 ? -4.727 -7.873  5.689   0.50 14.03 ? 155 PRO A CB  1 
ATOM   1208 C  CG  A PRO A 1 154 ? -4.847 -9.443  6.289   0.50 12.90 ? 155 PRO A CG  1 
ATOM   1209 C  CG  B PRO A 1 154 ? -5.081 -8.863  6.794   0.50 14.31 ? 155 PRO A CG  1 
ATOM   1210 C  CD  A PRO A 1 154 ? -3.850 -9.259  7.423   0.50 12.85 ? 155 PRO A CD  1 
ATOM   1211 C  CD  B PRO A 1 154 ? -3.838 -9.039  7.645   0.50 13.71 ? 155 PRO A CD  1 
ATOM   1212 N  N   . GLY A 1 155 ? -2.620 -5.831  6.467   1.00 13.87 ? 156 GLY A N   1 
ATOM   1213 C  CA  . GLY A 1 155 ? -2.219 -4.428  6.463   1.00 15.05 ? 156 GLY A CA  1 
ATOM   1214 C  C   . GLY A 1 155 ? -0.720 -4.214  6.254   1.00 16.03 ? 156 GLY A C   1 
ATOM   1215 O  O   . GLY A 1 155 ? -0.294 -3.085  6.008   1.00 17.73 ? 156 GLY A O   1 
ATOM   1216 N  N   . LEU A 1 156 ? 0.061  -5.309  6.280   1.00 13.31 ? 157 LEU A N   1 
ATOM   1217 C  CA  . LEU A 1 156 ? 1.478  -5.265  5.945   1.00 12.35 ? 157 LEU A CA  1 
ATOM   1218 C  C   . LEU A 1 156 ? 1.752  -5.490  4.464   1.00 11.96 ? 157 LEU A C   1 
ATOM   1219 O  O   . LEU A 1 156 ? 2.866  -5.241  3.993   1.00 11.95 ? 157 LEU A O   1 
ATOM   1220 C  CB  . LEU A 1 156 ? 2.227  -6.300  6.800   1.00 11.97 ? 157 LEU A CB  1 
ATOM   1221 C  CG  . LEU A 1 156 ? 3.740  -6.414  6.561   1.00 10.66 ? 157 LEU A CG  1 
ATOM   1222 C  CD1 . LEU A 1 156 ? 4.460  -5.103  6.952   1.00 11.32 ? 157 LEU A CD1 1 
ATOM   1223 C  CD2 . LEU A 1 156 ? 4.315  -7.555  7.401   1.00 10.84 ? 157 LEU A CD2 1 
ATOM   1224 N  N   . GLN A 1 157 ? 0.758  -5.983  3.705   1.00 12.96 ? 158 GLN A N   1 
ATOM   1225 C  CA  . GLN A 1 157 ? 1.081  -6.491  2.385   1.00 13.20 ? 158 GLN A CA  1 
ATOM   1226 C  C   . GLN A 1 157 ? 1.515  -5.384  1.433   1.00 11.85 ? 158 GLN A C   1 
ATOM   1227 O  O   . GLN A 1 157 ? 2.368  -5.637  0.608   1.00 12.92 ? 158 GLN A O   1 
ATOM   1228 C  CB  . GLN A 1 157 ? -0.047 -7.342  1.806   1.00 13.65 ? 158 GLN A CB  1 
ATOM   1229 C  CG  . GLN A 1 157 ? 0.389  -8.069  0.524   1.00 14.45 ? 158 GLN A CG  1 
ATOM   1230 C  CD  . GLN A 1 157 ? 1.429  -9.139  0.783   1.00 15.35 ? 158 GLN A CD  1 
ATOM   1231 O  OE1 . GLN A 1 157 ? 1.528  -9.737  1.858   1.00 16.02 ? 158 GLN A OE1 1 
ATOM   1232 N  NE2 . GLN A 1 157 ? 2.251  -9.385  -0.211  1.00 15.35 ? 158 GLN A NE2 1 
ATOM   1233 N  N   . LYS A 1 158 ? 0.960  -4.173  1.536   1.00 13.72 ? 159 LYS A N   1 
ATOM   1234 C  CA  . LYS A 1 158 ? 1.356  -3.104  0.641   1.00 13.42 ? 159 LYS A CA  1 
ATOM   1235 C  C   . LYS A 1 158 ? 2.842  -2.794  0.833   1.00 13.38 ? 159 LYS A C   1 
ATOM   1236 O  O   . LYS A 1 158 ? 3.528  -2.448  -0.123  1.00 14.06 ? 159 LYS A O   1 
ATOM   1237 C  CB  . LYS A 1 158 ? 0.423  -1.897  0.848   1.00 17.81 ? 159 LYS A CB  1 
ATOM   1238 C  CG  . LYS A 1 158 ? 0.798  -0.605  0.121   1.00 25.20 ? 159 LYS A CG  1 
ATOM   1239 C  CD  . LYS A 1 158 ? -0.017 0.632   0.593   1.00 25.06 ? 159 LYS A CD  1 
ATOM   1240 C  CE  . LYS A 1 158 ? 0.296  1.953   -0.106  1.00 29.63 ? 159 LYS A CE  1 
ATOM   1241 N  NZ  . LYS A 1 158 ? 0.039  1.896   -1.579  1.00 31.12 ? 159 LYS A NZ  1 
ATOM   1242 N  N   . VAL A 1 159 ? 3.328  -2.914  2.078   1.00 12.49 ? 160 VAL A N   1 
ATOM   1243 C  CA  . VAL A 1 159 ? 4.751  -2.747  2.346   1.00 12.19 ? 160 VAL A CA  1 
ATOM   1244 C  C   . VAL A 1 159 ? 5.552  -3.847  1.646   1.00 11.79 ? 160 VAL A C   1 
ATOM   1245 O  O   . VAL A 1 159 ? 6.560  -3.588  0.976   1.00 12.88 ? 160 VAL A O   1 
ATOM   1246 C  CB  . VAL A 1 159 ? 5.003  -2.736  3.862   1.00 12.46 ? 160 VAL A CB  1 
ATOM   1247 C  CG1 . VAL A 1 159 ? 6.505  -2.728  4.167   1.00 12.04 ? 160 VAL A CG1 1 
ATOM   1248 C  CG2 . VAL A 1 159 ? 4.300  -1.554  4.500   1.00 12.75 ? 160 VAL A CG2 1 
ATOM   1249 N  N   . VAL A 1 160 ? 5.171  -5.099  1.883   1.00 11.10 ? 161 VAL A N   1 
ATOM   1250 C  CA  . VAL A 1 160 ? 5.946  -6.228  1.375   1.00 14.30 ? 161 VAL A CA  1 
ATOM   1251 C  C   . VAL A 1 160 ? 5.999  -6.139  -0.152  1.00 14.01 ? 161 VAL A C   1 
ATOM   1252 O  O   . VAL A 1 160 ? 7.026  -6.382  -0.761  1.00 13.30 ? 161 VAL A O   1 
ATOM   1253 C  CB  . VAL A 1 160 ? 5.260  -7.541  1.841   1.00 16.06 ? 161 VAL A CB  1 
ATOM   1254 C  CG1 . VAL A 1 160 ? 5.628  -8.769  0.998   1.00 18.27 ? 161 VAL A CG1 1 
ATOM   1255 C  CG2 . VAL A 1 160 ? 5.536  -7.789  3.318   1.00 17.30 ? 161 VAL A CG2 1 
ATOM   1256 N  N   . ASP A 1 161 ? 4.911  -5.680  -0.759  1.00 15.96 ? 162 ASP A N   1 
ATOM   1257 C  CA  . ASP A 1 161 ? 4.817  -5.713  -2.214  1.00 18.93 ? 162 ASP A CA  1 
ATOM   1258 C  C   . ASP A 1 161 ? 5.673  -4.651  -2.907  1.00 20.76 ? 162 ASP A C   1 
ATOM   1259 O  O   . ASP A 1 161 ? 5.909  -4.809  -4.100  1.00 23.65 ? 162 ASP A O   1 
ATOM   1260 C  CB  . ASP A 1 161 ? 3.371  -5.581  -2.686  1.00 22.53 ? 162 ASP A CB  1 
ATOM   1261 C  CG  . ASP A 1 161 ? 2.668  -6.929  -2.734  1.00 23.68 ? 162 ASP A CG  1 
ATOM   1262 O  OD1 . ASP A 1 161 ? 3.368  -7.959  -2.830  1.00 26.94 ? 162 ASP A OD1 1 
ATOM   1263 O  OD2 . ASP A 1 161 ? 1.434  -6.942  -2.648  1.00 28.89 ? 162 ASP A OD2 1 
ATOM   1264 N  N   . VAL A 1 162 ? 6.114  -3.587  -2.199  1.00 15.46 ? 163 VAL A N   1 
ATOM   1265 C  CA  . VAL A 1 162 ? 6.936  -2.546  -2.806  1.00 16.96 ? 163 VAL A CA  1 
ATOM   1266 C  C   . VAL A 1 162 ? 8.427  -2.832  -2.608  1.00 14.59 ? 163 VAL A C   1 
ATOM   1267 O  O   . VAL A 1 162 ? 9.292  -2.123  -3.153  1.00 14.62 ? 163 VAL A O   1 
ATOM   1268 C  CB  . VAL A 1 162 ? 6.523  -1.167  -2.248  1.00 16.31 ? 163 VAL A CB  1 
ATOM   1269 C  CG1 . VAL A 1 162 ? 7.182  -0.897  -0.902  1.00 17.66 ? 163 VAL A CG1 1 
ATOM   1270 C  CG2 . VAL A 1 162 ? 6.805  -0.004  -3.209  1.00 18.74 ? 163 VAL A CG2 1 
ATOM   1271 N  N   . LEU A 1 163 ? 8.792  -3.837  -1.781  1.00 15.53 ? 164 LEU A N   1 
ATOM   1272 C  CA  . LEU A 1 163 ? 10.198 -4.052  -1.420  1.00 14.89 ? 164 LEU A CA  1 
ATOM   1273 C  C   . LEU A 1 163 ? 11.106 -4.341  -2.621  1.00 15.54 ? 164 LEU A C   1 
ATOM   1274 O  O   . LEU A 1 163 ? 12.282 -3.995  -2.617  1.00 14.58 ? 164 LEU A O   1 
ATOM   1275 C  CB  . LEU A 1 163 ? 10.357 -5.135  -0.345  1.00 14.28 ? 164 LEU A CB  1 
ATOM   1276 C  CG  . LEU A 1 163 ? 9.683  -4.827  1.003   1.00 14.61 ? 164 LEU A CG  1 
ATOM   1277 C  CD1 . LEU A 1 163 ? 9.892  -5.985  1.989   1.00 13.85 ? 164 LEU A CD1 1 
ATOM   1278 C  CD2 . LEU A 1 163 ? 10.195 -3.526  1.608   1.00 14.87 ? 164 LEU A CD2 1 
ATOM   1279 N  N   . ASP A 1 164 ? 10.564 -5.021  -3.643  1.00 17.71 ? 165 ASP A N   1 
ATOM   1280 C  CA  . ASP A 1 164 ? 11.319 -5.309  -4.849  1.00 20.21 ? 165 ASP A CA  1 
ATOM   1281 C  C   . ASP A 1 164 ? 11.846 -4.031  -5.517  1.00 20.82 ? 165 ASP A C   1 
ATOM   1282 O  O   . ASP A 1 164 ? 12.896 -4.085  -6.150  1.00 23.35 ? 165 ASP A O   1 
ATOM   1283 C  CB  . ASP A 1 164 ? 10.502 -6.201  -5.802  1.00 23.04 ? 165 ASP A CB  1 
ATOM   1284 C  CG  . ASP A 1 164 ? 9.486  -5.400  -6.597  1.00 28.88 ? 165 ASP A CG  1 
ATOM   1285 O  OD1 . ASP A 1 164 ? 8.501  -4.924  -5.996  1.00 27.18 ? 165 ASP A OD1 1 
ATOM   1286 O  OD2 . ASP A 1 164 ? 9.709  -5.202  -7.825  1.00 34.40 ? 165 ASP A OD2 1 
ATOM   1287 N  N   . SER A 1 165 ? 11.185 -2.887  -5.307  1.00 19.45 ? 166 SER A N   1 
ATOM   1288 C  CA  . SER A 1 165 ? 11.559 -1.616  -5.921  1.00 18.34 ? 166 SER A CA  1 
ATOM   1289 C  C   . SER A 1 165 ? 12.623 -0.844  -5.135  1.00 19.59 ? 166 SER A C   1 
ATOM   1290 O  O   . SER A 1 165 ? 13.176 0.143   -5.643  1.00 16.81 ? 166 SER A O   1 
ATOM   1291 C  CB  . SER A 1 165 ? 10.334 -0.784  -6.232  1.00 21.82 ? 166 SER A CB  1 
ATOM   1292 O  OG  . SER A 1 165 ? 9.857  -0.152  -5.057  1.00 27.75 ? 166 SER A OG  1 
ATOM   1293 N  N   . ILE A 1 166 ? 12.940 -1.296  -3.902  1.00 15.62 ? 167 ILE A N   1 
ATOM   1294 C  CA  . ILE A 1 166 ? 13.982 -0.659  -3.095  1.00 15.01 ? 167 ILE A CA  1 
ATOM   1295 C  C   . ILE A 1 166 ? 14.929 -1.733  -2.569  1.00 15.34 ? 167 ILE A C   1 
ATOM   1296 O  O   . ILE A 1 166 ? 15.279 -1.764  -1.399  1.00 15.13 ? 167 ILE A O   1 
ATOM   1297 C  CB  . ILE A 1 166 ? 13.333 0.134   -1.931  1.00 14.87 ? 167 ILE A CB  1 
ATOM   1298 C  CG1 . ILE A 1 166 ? 12.509 -0.815  -1.056  1.00 13.99 ? 167 ILE A CG1 1 
ATOM   1299 C  CG2 . ILE A 1 166 ? 12.468 1.294   -2.459  1.00 14.06 ? 167 ILE A CG2 1 
ATOM   1300 C  CD1 . ILE A 1 166 ? 12.399 -0.365  0.389   1.00 16.91 ? 167 ILE A CD1 1 
ATOM   1301 N  N   . LYS A 1 167 ? 15.312 -2.662  -3.445  1.00 16.34 ? 168 LYS A N   1 
ATOM   1302 C  CA  . LYS A 1 167 ? 16.112 -3.801  -3.046  1.00 16.54 ? 168 LYS A CA  1 
ATOM   1303 C  C   . LYS A 1 167 ? 17.448 -3.425  -2.407  1.00 15.91 ? 168 LYS A C   1 
ATOM   1304 O  O   . LYS A 1 167 ? 17.831 -4.094  -1.458  1.00 13.90 ? 168 LYS A O   1 
ATOM   1305 C  CB  . LYS A 1 167 ? 16.366 -4.722  -4.247  1.00 18.79 ? 168 LYS A CB  1 
ATOM   1306 C  CG  . LYS A 1 167 ? 17.288 -5.888  -3.922  1.00 19.75 ? 168 LYS A CG  1 
ATOM   1307 C  CD  . LYS A 1 167 ? 17.564 -6.841  -5.073  1.00 24.35 ? 168 LYS A CD  1 
ATOM   1308 C  CE  . LYS A 1 167 ? 17.855 -8.230  -4.556  1.00 27.85 ? 168 LYS A CE  1 
ATOM   1309 N  NZ  . LYS A 1 167 ? 18.297 -9.132  -5.652  1.00 35.88 ? 168 LYS A NZ  1 
ATOM   1310 N  N   . THR A 1 168 ? 18.146 -2.394  -2.915  1.00 13.67 ? 169 THR A N   1 
ATOM   1311 C  CA  . THR A 1 168 ? 19.511 -2.075  -2.516  1.00 13.66 ? 169 THR A CA  1 
ATOM   1312 C  C   . THR A 1 168 ? 19.562 -0.736  -1.785  1.00 12.68 ? 169 THR A C   1 
ATOM   1313 O  O   . THR A 1 168 ? 18.660 0.078   -1.919  1.00 14.01 ? 169 THR A O   1 
ATOM   1314 C  CB  . THR A 1 168 ? 20.454 -2.127  -3.733  1.00 15.44 ? 169 THR A CB  1 
ATOM   1315 O  OG1 . THR A 1 168 ? 19.802 -1.370  -4.767  1.00 15.55 ? 169 THR A OG1 1 
ATOM   1316 C  CG2 . THR A 1 168 ? 20.748 -3.555  -4.154  1.00 15.99 ? 169 THR A CG2 1 
ATOM   1317 N  N   . LYS A 1 169 ? 20.657 -0.530  -1.051  1.00 14.79 ? 170 LYS A N   1 
ATOM   1318 C  CA  . LYS A 1 169 ? 20.937 0.656   -0.248  1.00 16.74 ? 170 LYS A CA  1 
ATOM   1319 C  C   . LYS A 1 169 ? 20.819 1.930   -1.072  1.00 18.22 ? 170 LYS A C   1 
ATOM   1320 O  O   . LYS A 1 169 ? 21.353 1.980   -2.183  1.00 22.19 ? 170 LYS A O   1 
ATOM   1321 C  CB  . LYS A 1 169 ? 22.343 0.538   0.332   1.00 17.06 ? 170 LYS A CB  1 
ATOM   1322 C  CG  . LYS A 1 169 ? 22.814 1.733   1.172   1.00 18.02 ? 170 LYS A CG  1 
ATOM   1323 C  CD  . LYS A 1 169 ? 24.201 1.483   1.750   1.00 21.37 ? 170 LYS A CD  1 
ATOM   1324 C  CE  . LYS A 1 169 ? 24.933 2.751   2.143   1.00 26.78 ? 170 LYS A CE  1 
ATOM   1325 N  N   . GLY A 1 170 ? 20.062 2.906   -0.560  1.00 17.92 ? 171 GLY A N   1 
ATOM   1326 C  CA  . GLY A 1 170 ? 19.863 4.188   -1.232  1.00 19.52 ? 171 GLY A CA  1 
ATOM   1327 C  C   . GLY A 1 170 ? 18.661 4.271   -2.168  1.00 21.48 ? 171 GLY A C   1 
ATOM   1328 O  O   . GLY A 1 170 ? 18.274 5.385   -2.545  1.00 23.58 ? 171 GLY A O   1 
ATOM   1329 N  N   . LYS A 1 171 ? 18.033 3.130   -2.520  1.00 16.55 ? 172 LYS A N   1 
ATOM   1330 C  CA  . LYS A 1 171 ? 16.808 3.174   -3.303  1.00 17.65 ? 172 LYS A CA  1 
ATOM   1331 C  C   . LYS A 1 171 ? 15.621 3.631   -2.462  1.00 18.51 ? 172 LYS A C   1 
ATOM   1332 O  O   . LYS A 1 171 ? 15.478 3.240   -1.294  1.00 17.80 ? 172 LYS A O   1 
ATOM   1333 C  CB  . LYS A 1 171 ? 16.508 1.839   -3.994  1.00 19.01 ? 172 LYS A CB  1 
ATOM   1334 C  CG  . LYS A 1 171 ? 17.545 1.477   -5.049  1.00 21.13 ? 172 LYS A CG  1 
ATOM   1335 C  CD  . LYS A 1 171 ? 17.272 0.182   -5.771  1.00 25.81 ? 172 LYS A CD  1 
ATOM   1336 C  CE  . LYS A 1 171 ? 17.297 0.290   -7.286  1.00 32.97 ? 172 LYS A CE  1 
ATOM   1337 N  N   . SER A 1 172 ? 14.747 4.409   -3.099  1.00 16.93 ? 173 SER A N   1 
ATOM   1338 C  CA  . SER A 1 172 ? 13.496 4.856   -2.498  1.00 17.86 ? 173 SER A CA  1 
ATOM   1339 C  C   . SER A 1 172 ? 12.366 4.762   -3.510  1.00 20.62 ? 173 SER A C   1 
ATOM   1340 O  O   . SER A 1 172 ? 12.603 4.689   -4.721  1.00 19.46 ? 173 SER A O   1 
ATOM   1341 C  CB  . SER A 1 172 ? 13.609 6.275   -1.967  1.00 20.71 ? 173 SER A CB  1 
ATOM   1342 O  OG  . SER A 1 172 ? 13.791 7.170   -3.049  1.00 21.51 ? 173 SER A OG  1 
ATOM   1343 N  N   . ALA A 1 173 ? 11.134 4.773   -2.997  1.00 19.48 ? 174 ALA A N   1 
ATOM   1344 C  CA  . ALA A 1 173 ? 9.954  4.670   -3.832  1.00 19.01 ? 174 ALA A CA  1 
ATOM   1345 C  C   . ALA A 1 173 ? 8.888  5.527   -3.184  1.00 21.37 ? 174 ALA A C   1 
ATOM   1346 O  O   . ALA A 1 173 ? 8.826  5.635   -1.954  1.00 17.72 ? 174 ALA A O   1 
ATOM   1347 C  CB  . ALA A 1 173 ? 9.510  3.240   -3.979  1.00 18.95 ? 174 ALA A CB  1 
ATOM   1348 N  N   . ASP A 1 174 ? 8.039  6.124   -4.031  1.00 19.53 ? 175 ASP A N   1 
ATOM   1349 C  CA  . ASP A 1 174 ? 6.881  6.819   -3.497  1.00 21.97 ? 175 ASP A CA  1 
ATOM   1350 C  C   . ASP A 1 174 ? 6.031  5.802   -2.740  1.00 21.37 ? 175 ASP A C   1 
ATOM   1351 O  O   . ASP A 1 174 ? 5.882  4.639   -3.155  1.00 20.81 ? 175 ASP A O   1 
ATOM   1352 C  CB  . ASP A 1 174 ? 6.053  7.515   -4.594  1.00 25.81 ? 175 ASP A CB  1 
ATOM   1353 C  CG  . ASP A 1 174 ? 6.890  8.512   -5.382  1.00 34.37 ? 175 ASP A CG  1 
ATOM   1354 O  OD1 . ASP A 1 174 ? 7.613  9.309   -4.730  1.00 34.63 ? 175 ASP A OD1 1 
ATOM   1355 O  OD2 . ASP A 1 174 ? 6.838  8.477   -6.655  1.00 40.53 ? 175 ASP A OD2 1 
ATOM   1356 N  N   . PHE A 1 175 ? 5.467  6.258   -1.616  1.00 17.99 ? 176 PHE A N   1 
ATOM   1357 C  CA  . PHE A 1 175 ? 4.713  5.347   -0.764  1.00 16.46 ? 176 PHE A CA  1 
ATOM   1358 C  C   . PHE A 1 175 ? 3.647  6.151   -0.037  1.00 16.81 ? 176 PHE A C   1 
ATOM   1359 O  O   . PHE A 1 175 ? 3.760  6.419   1.157   1.00 19.33 ? 176 PHE A O   1 
ATOM   1360 C  CB  . PHE A 1 175 ? 5.656  4.507   0.118   1.00 15.18 ? 176 PHE A CB  1 
ATOM   1361 C  CG  . PHE A 1 175 ? 5.022  3.250   0.660   1.00 15.98 ? 176 PHE A CG  1 
ATOM   1362 C  CD1 . PHE A 1 175 ? 4.684  2.190   -0.180  1.00 15.46 ? 176 PHE A CD1 1 
ATOM   1363 C  CD2 . PHE A 1 175 ? 4.719  3.131   2.015   1.00 14.89 ? 176 PHE A CD2 1 
ATOM   1364 C  CE1 . PHE A 1 175 ? 4.098  1.035   0.343   1.00 16.09 ? 176 PHE A CE1 1 
ATOM   1365 C  CE2 . PHE A 1 175 ? 4.161  1.977   2.533   1.00 15.38 ? 176 PHE A CE2 1 
ATOM   1366 C  CZ  . PHE A 1 175 ? 3.831  0.931   1.697   1.00 15.67 ? 176 PHE A CZ  1 
ATOM   1367 N  N   . THR A 1 176 ? 2.587  6.517   -0.772  1.00 14.13 ? 177 THR A N   1 
ATOM   1368 C  CA  . THR A 1 176 ? 1.547  7.370   -0.236  1.00 14.53 ? 177 THR A CA  1 
ATOM   1369 C  C   . THR A 1 176 ? 0.377  6.507   0.195   1.00 13.67 ? 177 THR A C   1 
ATOM   1370 O  O   . THR A 1 176 ? 0.221  5.371   -0.276  1.00 14.18 ? 177 THR A O   1 
ATOM   1371 C  CB  . THR A 1 176 ? 1.129  8.422   -1.271  1.00 16.70 ? 177 THR A CB  1 
ATOM   1372 O  OG1 . THR A 1 176 ? 0.615  7.697   -2.391  1.00 19.47 ? 177 THR A OG1 1 
ATOM   1373 C  CG2 . THR A 1 176 ? 2.271  9.340   -1.649  1.00 19.48 ? 177 THR A CG2 1 
ATOM   1374 N  N   . ASN A 1 177 ? -0.439 7.097   1.064   1.00 12.82 ? 178 ASN A N   1 
ATOM   1375 C  CA  . ASN A 1 177 ? -1.708 6.551   1.497   1.00 13.00 ? 178 ASN A CA  1 
ATOM   1376 C  C   . ASN A 1 177 ? -1.503 5.219   2.223   1.00 13.21 ? 178 ASN A C   1 
ATOM   1377 O  O   . ASN A 1 177 ? -2.412 4.417   2.202   1.00 15.30 ? 178 ASN A O   1 
ATOM   1378 C  CB  . ASN A 1 177 ? -2.697 6.393   0.330   1.00 14.05 ? 178 ASN A CB  1 
ATOM   1379 C  CG  . ASN A 1 177 ? -2.906 7.743   -0.334  1.00 16.20 ? 178 ASN A CG  1 
ATOM   1380 O  OD1 . ASN A 1 177 ? -3.551 8.599   0.248   1.00 16.00 ? 178 ASN A OD1 1 
ATOM   1381 N  ND2 . ASN A 1 177 ? -2.267 7.967   -1.465  1.00 16.79 ? 178 ASN A ND2 1 
ATOM   1382 N  N   . PHE A 1 178 ? -0.349 5.002   2.875   1.00 13.17 ? 179 PHE A N   1 
ATOM   1383 C  CA  . PHE A 1 178 ? -0.247 3.776   3.663   1.00 12.90 ? 179 PHE A CA  1 
ATOM   1384 C  C   . PHE A 1 178 ? -0.804 4.069   5.052   1.00 13.23 ? 179 PHE A C   1 
ATOM   1385 O  O   . PHE A 1 178 ? -0.395 5.050   5.667   1.00 15.49 ? 179 PHE A O   1 
ATOM   1386 C  CB  . PHE A 1 178 ? 1.192  3.283   3.763   1.00 12.20 ? 179 PHE A CB  1 
ATOM   1387 C  CG  . PHE A 1 178 ? 1.308  2.046   4.619   1.00 13.18 ? 179 PHE A CG  1 
ATOM   1388 C  CD1 . PHE A 1 178 ? 0.893  0.817   4.140   1.00 13.39 ? 179 PHE A CD1 1 
ATOM   1389 C  CD2 . PHE A 1 178 ? 1.666  2.164   5.958   1.00 13.77 ? 179 PHE A CD2 1 
ATOM   1390 C  CE1 . PHE A 1 178 ? 0.935  -0.305  4.964   1.00 14.47 ? 179 PHE A CE1 1 
ATOM   1391 C  CE2 . PHE A 1 178 ? 1.714  1.043   6.782   1.00 12.90 ? 179 PHE A CE2 1 
ATOM   1392 C  CZ  . PHE A 1 178 ? 1.354  -0.188  6.289   1.00 13.58 ? 179 PHE A CZ  1 
ATOM   1393 N  N   . ASP A 1 179 ? -1.633 3.160   5.575   1.00 12.56 ? 180 ASP A N   1 
ATOM   1394 C  CA  . ASP A 1 179 ? -2.268 3.353   6.865   1.00 13.32 ? 180 ASP A CA  1 
ATOM   1395 C  C   . ASP A 1 179 ? -1.598 2.497   7.947   1.00 11.81 ? 180 ASP A C   1 
ATOM   1396 O  O   . ASP A 1 179 ? -1.835 1.284   8.006   1.00 10.73 ? 180 ASP A O   1 
ATOM   1397 C  CB  . ASP A 1 179 ? -3.732 2.948   6.794   1.00 16.40 ? 180 ASP A CB  1 
ATOM   1398 C  CG  . ASP A 1 179 ? -4.558 3.301   8.024   1.00 18.77 ? 180 ASP A CG  1 
ATOM   1399 O  OD1 . ASP A 1 179 ? -3.979 3.623   9.119   1.00 16.18 ? 180 ASP A OD1 1 
ATOM   1400 O  OD2 . ASP A 1 179 ? -5.790 3.287   7.878   1.00 25.19 ? 180 ASP A OD2 1 
ATOM   1401 N  N   . PRO A 1 180 ? -0.816 3.093   8.882   1.00 11.46 ? 181 PRO A N   1 
ATOM   1402 C  CA  . PRO A 1 180 ? -0.081 2.311   9.887   1.00 11.94 ? 181 PRO A CA  1 
ATOM   1403 C  C   . PRO A 1 180 ? -0.986 1.655   10.928  1.00 11.17 ? 181 PRO A C   1 
ATOM   1404 O  O   . PRO A 1 180 ? -0.547 0.742   11.651  1.00 10.55 ? 181 PRO A O   1 
ATOM   1405 C  CB  . PRO A 1 180 ? 0.919  3.358   10.425  1.00 13.47 ? 181 PRO A CB  1 
ATOM   1406 C  CG  . PRO A 1 180 ? 0.154  4.648   10.351  1.00 13.00 ? 181 PRO A CG  1 
ATOM   1407 C  CD  . PRO A 1 180 ? -0.549 4.541   9.009   1.00 12.67 ? 181 PRO A CD  1 
ATOM   1408 N  N   . ARG A 1 181 ? -2.280 2.023   10.928  1.00 10.49 ? 182 ARG A N   1 
ATOM   1409 C  CA  . ARG A 1 181 ? -3.194 1.383   11.881  1.00 11.76 ? 182 ARG A CA  1 
ATOM   1410 C  C   . ARG A 1 181 ? -3.354 -0.108  11.565  1.00 11.97 ? 182 ARG A C   1 
ATOM   1411 O  O   . ARG A 1 181 ? -3.734 -0.900  12.439  1.00 11.88 ? 182 ARG A O   1 
ATOM   1412 C  CB  . ARG A 1 181 ? -4.555 2.085   11.902  1.00 12.90 ? 182 ARG A CB  1 
ATOM   1413 C  CG  . ARG A 1 181 ? -4.462 3.535   12.376  1.00 14.28 ? 182 ARG A CG  1 
ATOM   1414 C  CD  . ARG A 1 181 ? -5.787 4.267   12.315  1.00 15.27 ? 182 ARG A CD  1 
ATOM   1415 N  NE  . ARG A 1 181 ? -6.213 4.402   10.930  1.00 17.28 ? 182 ARG A NE  1 
ATOM   1416 C  CZ  . ARG A 1 181 ? -7.311 5.056   10.560  1.00 20.56 ? 182 ARG A CZ  1 
ATOM   1417 N  NH1 . ARG A 1 181 ? -8.062 5.602   11.497  1.00 20.26 ? 182 ARG A NH1 1 
ATOM   1418 N  NH2 . ARG A 1 181 ? -7.645 5.163   9.276   1.00 20.12 ? 182 ARG A NH2 1 
ATOM   1419 N  N   . GLY A 1 182 ? -3.005 -0.488  10.340  1.00 11.37 ? 183 GLY A N   1 
ATOM   1420 C  CA  . GLY A 1 182 ? -3.141 -1.862  9.879   1.00 12.13 ? 183 GLY A CA  1 
ATOM   1421 C  C   . GLY A 1 182 ? -1.988 -2.738  10.346  1.00 13.41 ? 183 GLY A C   1 
ATOM   1422 O  O   . GLY A 1 182 ? -1.916 -3.916  9.987   1.00 13.65 ? 183 GLY A O   1 
ATOM   1423 N  N   . LEU A 1 183 ? -1.077 -2.148  11.129  1.00 12.11 ? 184 LEU A N   1 
ATOM   1424 C  CA  . LEU A 1 183 ? 0.055  -2.913  11.661  1.00 11.63 ? 184 LEU A CA  1 
ATOM   1425 C  C   . LEU A 1 183 ? -0.109 -3.149  13.163  1.00 11.26 ? 184 LEU A C   1 
ATOM   1426 O  O   . LEU A 1 183 ? 0.792  -3.737  13.756  1.00 13.54 ? 184 LEU A O   1 
ATOM   1427 C  CB  . LEU A 1 183 ? 1.361  -2.149  11.418  1.00 11.49 ? 184 LEU A CB  1 
ATOM   1428 C  CG  . LEU A 1 183 ? 1.712  -1.910  9.948   1.00 11.86 ? 184 LEU A CG  1 
ATOM   1429 C  CD1 . LEU A 1 183 ? 2.907  -0.984  9.827   1.00 13.67 ? 184 LEU A CD1 1 
ATOM   1430 C  CD2 . LEU A 1 183 ? 1.861  -3.217  9.165   1.00 12.77 ? 184 LEU A CD2 1 
ATOM   1431 N  N   . LEU A 1 184 ? -1.221 -2.708  13.781  1.00 11.09 ? 185 LEU A N   1 
ATOM   1432 C  CA  . LEU A 1 184 ? -1.316 -2.716  15.245  1.00 10.83 ? 185 LEU A CA  1 
ATOM   1433 C  C   . LEU A 1 184 ? -2.026 -3.994  15.682  1.00 12.65 ? 185 LEU A C   1 
ATOM   1434 O  O   . LEU A 1 184 ? -2.942 -4.454  14.986  1.00 15.23 ? 185 LEU A O   1 
ATOM   1435 C  CB  . LEU A 1 184 ? -2.091 -1.499  15.778  1.00 10.81 ? 185 LEU A CB  1 
ATOM   1436 C  CG  . LEU A 1 184 ? -1.525 -0.129  15.382  1.00 11.57 ? 185 LEU A CG  1 
ATOM   1437 C  CD1 . LEU A 1 184 ? -2.363 1.005   15.921  1.00 14.52 ? 185 LEU A CD1 1 
ATOM   1438 C  CD2 . LEU A 1 184 ? -0.070 0.036   15.805  1.00 13.16 ? 185 LEU A CD2 1 
ATOM   1439 N  N   . PRO A 1 185 ? -1.688 -4.565  16.852  1.00 11.15 ? 186 PRO A N   1 
ATOM   1440 C  CA  . PRO A 1 185 ? -2.467 -5.681  17.372  1.00 11.54 ? 186 PRO A CA  1 
ATOM   1441 C  C   . PRO A 1 185 ? -3.755 -5.129  17.999  1.00 11.83 ? 186 PRO A C   1 
ATOM   1442 O  O   . PRO A 1 185 ? -3.970 -3.927  18.071  1.00 11.40 ? 186 PRO A O   1 
ATOM   1443 C  CB  . PRO A 1 185 ? -1.547 -6.240  18.457  1.00 10.77 ? 186 PRO A CB  1 
ATOM   1444 C  CG  . PRO A 1 185 ? -0.848 -5.016  18.971  1.00 9.27  ? 186 PRO A CG  1 
ATOM   1445 C  CD  . PRO A 1 185 ? -0.548 -4.177  17.722  1.00 10.14 ? 186 PRO A CD  1 
ATOM   1446 N  N   . GLU A 1 186 ? -4.581 -6.022  18.549  1.00 13.75 ? 187 GLU A N   1 
ATOM   1447 C  CA  . GLU A 1 186 ? -5.851 -5.575  19.081  1.00 14.08 ? 187 GLU A CA  1 
ATOM   1448 C  C   . GLU A 1 186 ? -5.637 -4.826  20.398  1.00 14.96 ? 187 GLU A C   1 
ATOM   1449 O  O   . GLU A 1 186 ? -6.298 -3.825  20.637  1.00 16.11 ? 187 GLU A O   1 
ATOM   1450 C  CB  . GLU A 1 186 ? -6.714 -6.842  19.167  1.00 16.68 ? 187 GLU A CB  1 
ATOM   1451 C  CG  . GLU A 1 186 ? -7.713 -6.869  20.287  1.00 22.20 ? 187 GLU A CG  1 
ATOM   1452 C  CD  . GLU A 1 186 ? -8.330 -8.253  20.516  1.00 24.20 ? 187 GLU A CD  1 
ATOM   1453 O  OE1 . GLU A 1 186 ? -8.142 -9.154  19.645  1.00 21.79 ? 187 GLU A OE1 1 
ATOM   1454 O  OE2 . GLU A 1 186 ? -9.006 -8.410  21.566  1.00 28.56 ? 187 GLU A OE2 1 
ATOM   1455 N  N   . SER A 1 187 ? -4.725 -5.309  21.271  1.00 12.37 ? 188 SER A N   1 
ATOM   1456 C  CA  . SER A 1 187 ? -4.534 -4.722  22.588  1.00 12.88 ? 188 SER A CA  1 
ATOM   1457 C  C   . SER A 1 187 ? -3.436 -3.667  22.532  1.00 12.25 ? 188 SER A C   1 
ATOM   1458 O  O   . SER A 1 187 ? -2.415 -3.909  21.880  1.00 13.33 ? 188 SER A O   1 
ATOM   1459 C  CB  . SER A 1 187 ? -4.136 -5.791  23.585  1.00 13.50 ? 188 SER A CB  1 
ATOM   1460 O  OG  . SER A 1 187 ? -3.920 -5.232  24.880  1.00 12.89 ? 188 SER A OG  1 
ATOM   1461 N  N   . LEU A 1 188 ? -3.586 -2.596  23.323  1.00 10.59 ? 189 LEU A N   1 
ATOM   1462 C  CA  . LEU A 1 188 ? -2.490 -1.639  23.502  1.00 12.48 ? 189 LEU A CA  1 
ATOM   1463 C  C   . LEU A 1 188 ? -1.839 -1.757  24.895  1.00 11.66 ? 189 LEU A C   1 
ATOM   1464 O  O   . LEU A 1 188 ? -1.205 -0.793  25.368  1.00 13.95 ? 189 LEU A O   1 
ATOM   1465 C  CB  . LEU A 1 188 ? -3.012 -0.207  23.250  1.00 12.12 ? 189 LEU A CB  1 
ATOM   1466 C  CG  . LEU A 1 188 ? -3.484 0.137   21.823  1.00 13.60 ? 189 LEU A CG  1 
ATOM   1467 C  CD1 . LEU A 1 188 ? -3.871 1.632   21.755  1.00 14.95 ? 189 LEU A CD1 1 
ATOM   1468 C  CD2 . LEU A 1 188 ? -2.432 -0.186  20.753  1.00 14.36 ? 189 LEU A CD2 1 
ATOM   1469 N  N   . ASP A 1 189 ? -1.987 -2.908  25.583  1.00 12.13 ? 190 ASP A N   1 
ATOM   1470 C  CA  . ASP A 1 189 ? -1.240 -3.118  26.817  1.00 12.04 ? 190 ASP A CA  1 
ATOM   1471 C  C   . ASP A 1 189 ? 0.254  -3.059  26.491  1.00 10.70 ? 190 ASP A C   1 
ATOM   1472 O  O   . ASP A 1 189 ? 0.686  -3.563  25.425  1.00 10.10 ? 190 ASP A O   1 
ATOM   1473 C  CB  . ASP A 1 189 ? -1.555 -4.445  27.504  1.00 13.13 ? 190 ASP A CB  1 
ATOM   1474 C  CG  . ASP A 1 189 ? -2.973 -4.515  28.068  1.00 17.43 ? 190 ASP A CG  1 
ATOM   1475 O  OD1 . ASP A 1 189 ? -3.547 -3.471  28.341  1.00 18.73 ? 190 ASP A OD1 1 
ATOM   1476 O  OD2 . ASP A 1 189 ? -3.462 -5.628  28.190  1.00 20.89 ? 190 ASP A OD2 1 
ATOM   1477 N  N   . TYR A 1 190 ? 1.026  -2.433  27.405  1.00 9.78  ? 191 TYR A N   1 
ATOM   1478 C  CA  . TYR A 1 190 ? 2.426  -2.200  27.055  1.00 8.89  ? 191 TYR A CA  1 
ATOM   1479 C  C   . TYR A 1 190 ? 3.344  -2.328  28.279  1.00 9.31  ? 191 TYR A C   1 
ATOM   1480 O  O   . TYR A 1 190 ? 2.914  -2.188  29.426  1.00 9.09  ? 191 TYR A O   1 
ATOM   1481 C  CB  . TYR A 1 190 ? 2.596  -0.790  26.437  1.00 8.52  ? 191 TYR A CB  1 
ATOM   1482 C  CG  . TYR A 1 190 ? 2.173  0.344   27.353  1.00 9.14  ? 191 TYR A CG  1 
ATOM   1483 C  CD1 . TYR A 1 190 ? 3.066  0.961   28.232  1.00 9.41  ? 191 TYR A CD1 1 
ATOM   1484 C  CD2 . TYR A 1 190 ? 0.868  0.824   27.326  1.00 9.24  ? 191 TYR A CD2 1 
ATOM   1485 C  CE1 . TYR A 1 190 ? 2.658  1.962   29.115  1.00 9.68  ? 191 TYR A CE1 1 
ATOM   1486 C  CE2 . TYR A 1 190 ? 0.452  1.870   28.147  1.00 10.13 ? 191 TYR A CE2 1 
ATOM   1487 C  CZ  . TYR A 1 190 ? 1.351  2.429   29.057  1.00 10.84 ? 191 TYR A CZ  1 
ATOM   1488 O  OH  . TYR A 1 190 ? 0.942  3.444   29.860  1.00 9.87  ? 191 TYR A OH  1 
ATOM   1489 N  N   . TRP A 1 191 ? 4.654  -2.487  28.013  1.00 8.27  ? 192 TRP A N   1 
ATOM   1490 C  CA  . TRP A 1 191 ? 5.714  -2.228  28.974  1.00 8.11  ? 192 TRP A CA  1 
ATOM   1491 C  C   . TRP A 1 191 ? 6.416  -0.940  28.561  1.00 7.80  ? 192 TRP A C   1 
ATOM   1492 O  O   . TRP A 1 191 ? 6.348  -0.559  27.397  1.00 6.97  ? 192 TRP A O   1 
ATOM   1493 C  CB  . TRP A 1 191 ? 6.735  -3.362  28.888  1.00 8.76  ? 192 TRP A CB  1 
ATOM   1494 C  CG  . TRP A 1 191 ? 6.225  -4.696  29.321  1.00 8.73  ? 192 TRP A CG  1 
ATOM   1495 C  CD1 . TRP A 1 191 ? 6.072  -5.156  30.606  1.00 8.75  ? 192 TRP A CD1 1 
ATOM   1496 C  CD2 . TRP A 1 191 ? 6.004  -5.813  28.457  1.00 9.16  ? 192 TRP A CD2 1 
ATOM   1497 N  NE1 . TRP A 1 191 ? 5.647  -6.472  30.574  1.00 9.36  ? 192 TRP A NE1 1 
ATOM   1498 C  CE2 . TRP A 1 191 ? 5.592  -6.887  29.273  1.00 9.69  ? 192 TRP A CE2 1 
ATOM   1499 C  CE3 . TRP A 1 191 ? 6.040  -5.975  27.066  1.00 9.39  ? 192 TRP A CE3 1 
ATOM   1500 C  CZ2 . TRP A 1 191 ? 5.283  -8.128  28.721  1.00 9.85  ? 192 TRP A CZ2 1 
ATOM   1501 C  CZ3 . TRP A 1 191 ? 5.697  -7.191  26.517  1.00 9.84  ? 192 TRP A CZ3 1 
ATOM   1502 C  CH2 . TRP A 1 191 ? 5.374  -8.262  27.350  1.00 10.56 ? 192 TRP A CH2 1 
ATOM   1503 N  N   . THR A 1 192 ? 7.015  -0.232  29.522  1.00 6.95  ? 193 THR A N   1 
ATOM   1504 C  CA  . THR A 1 192 ? 7.704  1.009   29.181  1.00 8.04  ? 193 THR A CA  1 
ATOM   1505 C  C   . THR A 1 192 ? 8.955  1.179   30.042  1.00 8.39  ? 193 THR A C   1 
ATOM   1506 O  O   . THR A 1 192 ? 8.979  0.774   31.206  1.00 8.95  ? 193 THR A O   1 
ATOM   1507 C  CB  . THR A 1 192 ? 6.784  2.239   29.265  1.00 8.02  ? 193 THR A CB  1 
ATOM   1508 O  OG1 . THR A 1 192 ? 7.449  3.442   28.834  1.00 9.10  ? 193 THR A OG1 1 
ATOM   1509 C  CG2 . THR A 1 192 ? 6.224  2.501   30.648  1.00 8.26  ? 193 THR A CG2 1 
ATOM   1510 N  N   . TYR A 1 193 ? 9.997  1.796   29.442  1.00 8.25  ? 194 TYR A N   1 
ATOM   1511 C  CA  . TYR A 1 193 ? 11.250 2.010   30.162  1.00 8.04  ? 194 TYR A CA  1 
ATOM   1512 C  C   . TYR A 1 193 ? 12.043 3.046   29.376  1.00 7.50  ? 194 TYR A C   1 
ATOM   1513 O  O   . TYR A 1 193 ? 11.735 3.301   28.201  1.00 6.75  ? 194 TYR A O   1 
ATOM   1514 C  CB  . TYR A 1 193 ? 12.058 0.713   30.344  1.00 7.62  ? 194 TYR A CB  1 
ATOM   1515 C  CG  . TYR A 1 193 ? 12.747 0.256   29.077  1.00 7.84  ? 194 TYR A CG  1 
ATOM   1516 C  CD1 . TYR A 1 193 ? 12.073 -0.495  28.119  1.00 7.33  ? 194 TYR A CD1 1 
ATOM   1517 C  CD2 . TYR A 1 193 ? 14.063 0.613   28.847  1.00 7.31  ? 194 TYR A CD2 1 
ATOM   1518 C  CE1 . TYR A 1 193 ? 12.712 -0.846  26.927  1.00 6.80  ? 194 TYR A CE1 1 
ATOM   1519 C  CE2 . TYR A 1 193 ? 14.713 0.302   27.657  1.00 7.75  ? 194 TYR A CE2 1 
ATOM   1520 C  CZ  . TYR A 1 193 ? 14.032 -0.459  26.726  1.00 7.39  ? 194 TYR A CZ  1 
ATOM   1521 O  OH  . TYR A 1 193 ? 14.700 -0.760  25.575  1.00 8.10  ? 194 TYR A OH  1 
ATOM   1522 N  N   . PRO A 1 194 ? 12.962 3.772   30.036  1.00 7.81  ? 195 PRO A N   1 
ATOM   1523 C  CA  . PRO A 1 194 ? 13.760 4.796   29.353  1.00 7.55  ? 195 PRO A CA  1 
ATOM   1524 C  C   . PRO A 1 194 ? 14.977 4.152   28.712  1.00 7.81  ? 195 PRO A C   1 
ATOM   1525 O  O   . PRO A 1 194 ? 15.646 3.366   29.357  1.00 7.37  ? 195 PRO A O   1 
ATOM   1526 C  CB  . PRO A 1 194 ? 14.231 5.742   30.485  1.00 8.83  ? 195 PRO A CB  1 
ATOM   1527 C  CG  . PRO A 1 194 ? 14.223 4.876   31.713  1.00 8.20  ? 195 PRO A CG  1 
ATOM   1528 C  CD  . PRO A 1 194 ? 13.170 3.793   31.505  1.00 7.89  ? 195 PRO A CD  1 
ATOM   1529 N  N   . GLY A 1 195 ? 15.224 4.447   27.424  1.00 7.18  ? 196 GLY A N   1 
ATOM   1530 C  CA  . GLY A 1 195 ? 16.337 3.782   26.757  1.00 7.08  ? 196 GLY A CA  1 
ATOM   1531 C  C   . GLY A 1 195 ? 16.883 4.655   25.633  1.00 6.91  ? 196 GLY A C   1 
ATOM   1532 O  O   . GLY A 1 195 ? 16.961 5.868   25.775  1.00 6.70  ? 196 GLY A O   1 
ATOM   1533 N  N   . SER A 1 196 ? 17.259 4.015   24.521  1.00 7.17  ? 197 SER A N   1 
ATOM   1534 C  CA  . SER A 1 196 ? 18.062 4.697   23.520  1.00 6.38  ? 197 SER A CA  1 
ATOM   1535 C  C   . SER A 1 196 ? 17.660 4.291   22.114  1.00 6.54  ? 197 SER A C   1 
ATOM   1536 O  O   . SER A 1 196 ? 16.907 3.341   21.940  1.00 6.75  ? 197 SER A O   1 
ATOM   1537 C  CB  . SER A 1 196 ? 19.527 4.285   23.722  1.00 6.30  ? 197 SER A CB  1 
ATOM   1538 O  OG  . SER A 1 196 ? 19.723 2.922   23.264  1.00 6.06  ? 197 SER A OG  1 
ATOM   1539 N  N   . LEU A 1 197 ? 18.243 4.977   21.116  1.00 6.87  ? 198 LEU A N   1 
ATOM   1540 C  CA  . LEU A 1 197 ? 18.187 4.410   19.775  1.00 7.25  ? 198 LEU A CA  1 
ATOM   1541 C  C   . LEU A 1 197 ? 18.890 3.070   19.836  1.00 7.85  ? 198 LEU A C   1 
ATOM   1542 O  O   . LEU A 1 197 ? 19.868 2.901   20.579  1.00 7.77  ? 198 LEU A O   1 
ATOM   1543 C  CB  . LEU A 1 197 ? 18.974 5.327   18.838  1.00 8.31  ? 198 LEU A CB  1 
ATOM   1544 C  CG  . LEU A 1 197 ? 18.239 6.483   18.180  1.00 10.61 ? 198 LEU A CG  1 
ATOM   1545 C  CD1 . LEU A 1 197 ? 17.641 7.426   19.205  1.00 10.78 ? 198 LEU A CD1 1 
ATOM   1546 C  CD2 . LEU A 1 197 ? 19.237 7.206   17.265  1.00 11.67 ? 198 LEU A CD2 1 
ATOM   1547 N  N   . THR A 1 198 ? 18.412 2.104   19.036  1.00 6.38  ? 199 THR A N   1 
ATOM   1548 C  CA  . THR A 1 198 ? 19.121 0.830   19.013  1.00 7.07  ? 199 THR A CA  1 
ATOM   1549 C  C   . THR A 1 198 ? 20.108 0.743   17.844  1.00 7.41  ? 199 THR A C   1 
ATOM   1550 O  O   . THR A 1 198 ? 20.727 -0.314  17.685  1.00 8.40  ? 199 THR A O   1 
ATOM   1551 C  CB  . THR A 1 198 ? 18.152 -0.348  18.851  1.00 6.56  ? 199 THR A CB  1 
ATOM   1552 O  OG1 . THR A 1 198 ? 17.564 -0.370  17.547  1.00 6.86  ? 199 THR A OG1 1 
ATOM   1553 C  CG2 . THR A 1 198 ? 17.140 -0.342  19.980  1.00 6.11  ? 199 THR A CG2 1 
ATOM   1554 N  N   . THR A 1 199 ? 20.202 1.798   17.025  1.00 9.09  ? 200 THR A N   1 
ATOM   1555 C  CA  . THR A 1 199 ? 21.312 1.845   16.068  1.00 9.79  ? 200 THR A CA  1 
ATOM   1556 C  C   . THR A 1 199 ? 22.155 3.062   16.369  1.00 8.99  ? 200 THR A C   1 
ATOM   1557 O  O   . THR A 1 199 ? 21.669 4.049   16.926  1.00 8.01  ? 200 THR A O   1 
ATOM   1558 C  CB  . THR A 1 199 ? 20.833 2.049   14.630  1.00 11.95 ? 200 THR A CB  1 
ATOM   1559 O  OG1 . THR A 1 199 ? 20.150 3.296   14.423  1.00 14.83 ? 200 THR A OG1 1 
ATOM   1560 C  CG2 . THR A 1 199 ? 19.854 0.965   14.248  1.00 11.63 ? 200 THR A CG2 1 
ATOM   1561 N  N   . PRO A 1 200 ? 23.412 3.077   15.880  1.00 8.81  ? 201 PRO A N   1 
ATOM   1562 C  CA  . PRO A 1 200 ? 24.171 4.323   15.953  1.00 8.67  ? 201 PRO A CA  1 
ATOM   1563 C  C   . PRO A 1 200 ? 23.297 5.473   15.438  1.00 9.09  ? 201 PRO A C   1 
ATOM   1564 O  O   . PRO A 1 200 ? 22.605 5.368   14.386  1.00 10.27 ? 201 PRO A O   1 
ATOM   1565 C  CB  . PRO A 1 200 ? 25.395 3.961   15.079  1.00 7.96  ? 201 PRO A CB  1 
ATOM   1566 C  CG  . PRO A 1 200 ? 25.600 2.482   15.304  1.00 8.99  ? 201 PRO A CG  1 
ATOM   1567 C  CD  . PRO A 1 200 ? 24.171 1.934   15.329  1.00 8.38  ? 201 PRO A CD  1 
ATOM   1568 N  N   . PRO A 1 201 ? 23.341 6.689   16.030  1.00 8.66  ? 202 PRO A N   1 
ATOM   1569 C  CA  . PRO A 1 201 ? 24.242 7.054   17.138  1.00 9.28  ? 202 PRO A CA  1 
ATOM   1570 C  C   . PRO A 1 201 ? 23.886 6.693   18.576  1.00 8.47  ? 202 PRO A C   1 
ATOM   1571 O  O   . PRO A 1 201 ? 24.544 7.160   19.508  1.00 8.70  ? 202 PRO A O   1 
ATOM   1572 C  CB  . PRO A 1 201 ? 24.292 8.582   17.015  1.00 9.06  ? 202 PRO A CB  1 
ATOM   1573 C  CG  . PRO A 1 201 ? 22.896 8.933   16.537  1.00 9.54  ? 202 PRO A CG  1 
ATOM   1574 C  CD  . PRO A 1 201 ? 22.596 7.858   15.513  1.00 9.55  ? 202 PRO A CD  1 
ATOM   1575 N  N   . LEU A 1 202 ? 22.889 5.791   18.759  1.00 8.37  ? 203 LEU A N   1 
ATOM   1576 C  CA  . LEU A 1 202 ? 22.606 5.163   20.047  1.00 7.04  ? 203 LEU A CA  1 
ATOM   1577 C  C   . LEU A 1 202 ? 22.247 6.200   21.126  1.00 6.77  ? 203 LEU A C   1 
ATOM   1578 O  O   . LEU A 1 202 ? 22.448 5.937   22.307  1.00 7.08  ? 203 LEU A O   1 
ATOM   1579 C  CB  . LEU A 1 202 ? 23.787 4.282   20.507  1.00 7.61  ? 203 LEU A CB  1 
ATOM   1580 C  CG  . LEU A 1 202 ? 24.156 3.147   19.553  1.00 7.08  ? 203 LEU A CG  1 
ATOM   1581 C  CD1 . LEU A 1 202 ? 25.408 2.448   20.084  1.00 6.98  ? 203 LEU A CD1 1 
ATOM   1582 C  CD2 . LEU A 1 202 ? 23.033 2.115   19.509  1.00 7.03  ? 203 LEU A CD2 1 
ATOM   1583 N  N   . LEU A 1 203 ? 21.657 7.330   20.724  1.00 7.75  ? 204 LEU A N   1 
ATOM   1584 C  CA  . LEU A 1 203 ? 21.409 8.446   21.652  1.00 8.33  ? 204 LEU A CA  1 
ATOM   1585 C  C   . LEU A 1 203 ? 20.350 8.036   22.680  1.00 8.87  ? 204 LEU A C   1 
ATOM   1586 O  O   . LEU A 1 203 ? 19.378 7.336   22.355  1.00 8.86  ? 204 LEU A O   1 
ATOM   1587 C  CB  . LEU A 1 203 ? 20.945 9.695   20.875  1.00 8.78  ? 204 LEU A CB  1 
ATOM   1588 C  CG  . LEU A 1 203 ? 22.023 10.244  19.915  1.00 9.96  ? 204 LEU A CG  1 
ATOM   1589 C  CD1 . LEU A 1 203 ? 21.437 11.309  19.007  1.00 11.15 ? 204 LEU A CD1 1 
ATOM   1590 C  CD2 . LEU A 1 203 ? 23.199 10.830  20.704  1.00 12.34 ? 204 LEU A CD2 1 
ATOM   1591 N  N   . GLU A 1 204 ? 20.524 8.519   23.920  1.00 8.26  ? 205 GLU A N   1 
ATOM   1592 C  CA  . GLU A 1 204 ? 19.698 8.114   25.044  1.00 8.74  ? 205 GLU A CA  1 
ATOM   1593 C  C   . GLU A 1 204 ? 18.530 9.092   25.175  1.00 8.64  ? 205 GLU A C   1 
ATOM   1594 O  O   . GLU A 1 204 ? 18.486 9.876   26.134  1.00 8.91  ? 205 GLU A O   1 
ATOM   1595 C  CB  . GLU A 1 204 ? 20.594 8.002   26.292  1.00 9.50  ? 205 GLU A CB  1 
ATOM   1596 C  CG  . GLU A 1 204 ? 21.402 6.696   26.210  1.00 9.56  ? 205 GLU A CG  1 
ATOM   1597 C  CD  . GLU A 1 204 ? 22.397 6.432   27.325  1.00 10.87 ? 205 GLU A CD  1 
ATOM   1598 O  OE1 . GLU A 1 204 ? 22.726 7.396   28.063  1.00 11.03 ? 205 GLU A OE1 1 
ATOM   1599 O  OE2 . GLU A 1 204 ? 22.854 5.275   27.436  1.00 10.97 ? 205 GLU A OE2 1 
ATOM   1600 N  N   . CYS A 1 205 ? 17.617 9.044   24.190  1.00 7.75  ? 206 CYS A N   1 
ATOM   1601 C  CA  . CYS A 1 205 ? 16.572 10.062  24.092  1.00 7.67  ? 206 CYS A CA  1 
ATOM   1602 C  C   . CYS A 1 205 ? 15.194 9.409   23.984  1.00 7.04  ? 206 CYS A C   1 
ATOM   1603 O  O   . CYS A 1 205 ? 14.223 10.103  23.699  1.00 7.97  ? 206 CYS A O   1 
ATOM   1604 C  CB  . CYS A 1 205 ? 16.803 10.923  22.853  1.00 8.04  ? 206 CYS A CB  1 
ATOM   1605 S  SG  . CYS A 1 205 ? 16.872 9.933   21.321  1.00 10.12 ? 206 CYS A SG  1 
ATOM   1606 N  N   . VAL A 1 206 ? 15.113 8.100   24.227  1.00 6.76  ? 207 VAL A N   1 
ATOM   1607 C  CA  . VAL A 1 206 ? 13.908 7.333   23.858  1.00 6.31  ? 207 VAL A CA  1 
ATOM   1608 C  C   . VAL A 1 206 ? 13.113 6.898   25.095  1.00 6.71  ? 207 VAL A C   1 
ATOM   1609 O  O   . VAL A 1 206 ? 13.641 6.235   25.986  1.00 8.21  ? 207 VAL A O   1 
ATOM   1610 C  CB  . VAL A 1 206 ? 14.220 6.074   23.020  1.00 6.34  ? 207 VAL A CB  1 
ATOM   1611 C  CG1 . VAL A 1 206 ? 12.859 5.430   22.637  1.00 5.52  ? 207 VAL A CG1 1 
ATOM   1612 C  CG2 . VAL A 1 206 ? 14.996 6.451   21.751  1.00 6.79  ? 207 VAL A CG2 1 
ATOM   1613 N  N   . THR A 1 207 ? 11.790 7.184   25.097  1.00 6.48  ? 208 THR A N   1 
ATOM   1614 C  CA  . THR A 1 207 ? 10.860 6.476   25.968  1.00 6.59  ? 208 THR A CA  1 
ATOM   1615 C  C   . THR A 1 207 ? 10.378 5.291   25.152  1.00 6.65  ? 208 THR A C   1 
ATOM   1616 O  O   . THR A 1 207 ? 9.667  5.492   24.155  1.00 7.21  ? 208 THR A O   1 
ATOM   1617 C  CB  . THR A 1 207 ? 9.677  7.367   26.423  1.00 7.38  ? 208 THR A CB  1 
ATOM   1618 O  OG1 . THR A 1 207 ? 10.222 8.416   27.240  1.00 7.00  ? 208 THR A OG1 1 
ATOM   1619 C  CG2 . THR A 1 207 ? 8.689  6.574   27.254  1.00 7.06  ? 208 THR A CG2 1 
ATOM   1620 N  N   . TRP A 1 208 ? 10.736 4.080   25.575  1.00 6.72  ? 209 TRP A N   1 
ATOM   1621 C  CA  . TRP A 1 208 ? 10.288 2.882   24.867  1.00 6.29  ? 209 TRP A CA  1 
ATOM   1622 C  C   . TRP A 1 208 ? 8.926  2.448   25.401  1.00 6.59  ? 209 TRP A C   1 
ATOM   1623 O  O   . TRP A 1 208 ? 8.750  2.326   26.607  1.00 7.36  ? 209 TRP A O   1 
ATOM   1624 C  CB  . TRP A 1 208 ? 11.292 1.715   25.051  1.00 6.32  ? 209 TRP A CB  1 
ATOM   1625 C  CG  . TRP A 1 208 ? 12.412 1.853   24.064  1.00 6.13  ? 209 TRP A CG  1 
ATOM   1626 C  CD1 . TRP A 1 208 ? 13.640 2.445   24.233  1.00 6.44  ? 209 TRP A CD1 1 
ATOM   1627 C  CD2 . TRP A 1 208 ? 12.336 1.464   22.682  1.00 6.28  ? 209 TRP A CD2 1 
ATOM   1628 N  NE1 . TRP A 1 208 ? 14.310 2.471   23.043  1.00 6.63  ? 209 TRP A NE1 1 
ATOM   1629 C  CE2 . TRP A 1 208 ? 13.578 1.788   22.101  1.00 5.98  ? 209 TRP A CE2 1 
ATOM   1630 C  CE3 . TRP A 1 208 ? 11.351 0.809   21.918  1.00 5.95  ? 209 TRP A CE3 1 
ATOM   1631 C  CZ2 . TRP A 1 208 ? 13.840 1.575   20.750  1.00 6.10  ? 209 TRP A CZ2 1 
ATOM   1632 C  CZ3 . TRP A 1 208 ? 11.626 0.530   20.601  1.00 5.97  ? 209 TRP A CZ3 1 
ATOM   1633 C  CH2 . TRP A 1 208 ? 12.857 0.904   20.042  1.00 5.81  ? 209 TRP A CH2 1 
ATOM   1634 N  N   . ILE A 1 209 ? 8.029  2.164   24.459  1.00 6.70  ? 210 ILE A N   1 
ATOM   1635 C  CA  . ILE A 1 209 ? 6.724  1.607   24.778  1.00 6.57  ? 210 ILE A CA  1 
ATOM   1636 C  C   . ILE A 1 209 ? 6.617  0.333   23.943  1.00 7.11  ? 210 ILE A C   1 
ATOM   1637 O  O   . ILE A 1 209 ? 6.521  0.433   22.730  1.00 7.57  ? 210 ILE A O   1 
ATOM   1638 C  CB  . ILE A 1 209 ? 5.639  2.640   24.413  1.00 7.37  ? 210 ILE A CB  1 
ATOM   1639 C  CG1 . ILE A 1 209 ? 5.864  3.931   25.209  1.00 7.86  ? 210 ILE A CG1 1 
ATOM   1640 C  CG2 . ILE A 1 209 ? 4.251  2.012   24.702  1.00 7.54  ? 210 ILE A CG2 1 
ATOM   1641 C  CD1 . ILE A 1 209 ? 5.123  5.144   24.585  1.00 8.82  ? 210 ILE A CD1 1 
ATOM   1642 N  N   . VAL A 1 210 ? 6.615  -0.846  24.580  1.00 6.74  ? 211 VAL A N   1 
ATOM   1643 C  CA  . VAL A 1 210 ? 6.646  -2.081  23.806  1.00 6.41  ? 211 VAL A CA  1 
ATOM   1644 C  C   . VAL A 1 210 ? 5.337  -2.814  24.088  1.00 7.10  ? 211 VAL A C   1 
ATOM   1645 O  O   . VAL A 1 210 ? 5.038  -3.055  25.259  1.00 7.05  ? 211 VAL A O   1 
ATOM   1646 C  CB  . VAL A 1 210 ? 7.854  -2.939  24.237  1.00 6.30  ? 211 VAL A CB  1 
ATOM   1647 C  CG1 . VAL A 1 210 ? 7.851  -4.299  23.524  1.00 6.19  ? 211 VAL A CG1 1 
ATOM   1648 C  CG2 . VAL A 1 210 ? 9.211  -2.227  23.984  1.00 5.99  ? 211 VAL A CG2 1 
ATOM   1649 N  N   . LEU A 1 211 ? 4.563  -3.087  23.034  1.00 7.16  ? 212 LEU A N   1 
ATOM   1650 C  CA  . LEU A 1 211 ? 3.275  -3.762  23.198  1.00 7.69  ? 212 LEU A CA  1 
ATOM   1651 C  C   . LEU A 1 211 ? 3.442  -5.218  23.605  1.00 8.69  ? 212 LEU A C   1 
ATOM   1652 O  O   . LEU A 1 211 ? 4.323  -5.924  23.129  1.00 9.46  ? 212 LEU A O   1 
ATOM   1653 C  CB  . LEU A 1 211 ? 2.490  -3.659  21.887  1.00 7.59  ? 212 LEU A CB  1 
ATOM   1654 C  CG  . LEU A 1 211 ? 2.093  -2.246  21.448  1.00 8.25  ? 212 LEU A CG  1 
ATOM   1655 C  CD1 . LEU A 1 211 ? 1.038  -2.296  20.330  1.00 8.65  ? 212 LEU A CD1 1 
ATOM   1656 C  CD2 . LEU A 1 211 ? 1.568  -1.363  22.606  1.00 7.74  ? 212 LEU A CD2 1 
ATOM   1657 N  N   . LYS A 1 212 ? 2.589  -5.659  24.545  1.00 10.11 ? 213 LYS A N   1 
ATOM   1658 C  CA  . LYS A 1 212 ? 2.612  -7.046  25.011  1.00 11.09 ? 213 LYS A CA  1 
ATOM   1659 C  C   . LYS A 1 212 ? 2.155  -7.992  23.902  1.00 10.50 ? 213 LYS A C   1 
ATOM   1660 O  O   . LYS A 1 212 ? 2.627  -9.124  23.822  1.00 11.37 ? 213 LYS A O   1 
ATOM   1661 C  CB  . LYS A 1 212 ? 1.698  -7.159  26.249  1.00 16.36 ? 213 LYS A CB  1 
ATOM   1662 C  CG  . LYS A 1 212 ? 1.270  -8.592  26.584  1.00 21.76 ? 213 LYS A CG  1 
ATOM   1663 C  CD  . LYS A 1 212 ? 0.369  -8.744  27.816  1.00 27.61 ? 213 LYS A CD  1 
ATOM   1664 C  CE  . LYS A 1 212 ? -1.116 -8.936  27.553  1.00 31.79 ? 213 LYS A CE  1 
ATOM   1665 N  NZ  . LYS A 1 212 ? -1.714 -7.874  26.698  1.00 36.26 ? 213 LYS A NZ  1 
ATOM   1666 N  N   . GLU A 1 213 ? 1.215  -7.546  23.066  1.00 9.48  ? 214 GLU A N   1 
ATOM   1667 C  CA  . GLU A 1 213 ? 0.598  -8.479  22.121  1.00 10.59 ? 214 GLU A CA  1 
ATOM   1668 C  C   . GLU A 1 213 ? 1.320  -8.401  20.775  1.00 9.17  ? 214 GLU A C   1 
ATOM   1669 O  O   . GLU A 1 213 ? 1.339  -7.352  20.119  1.00 9.40  ? 214 GLU A O   1 
ATOM   1670 C  CB  . GLU A 1 213 ? -0.872 -8.139  21.863  1.00 11.70 ? 214 GLU A CB  1 
ATOM   1671 C  CG  . GLU A 1 213 ? -1.545 -9.177  20.971  1.00 15.93 ? 214 GLU A CG  1 
ATOM   1672 C  CD  . GLU A 1 213 ? -3.035 -8.997  20.715  1.00 18.31 ? 214 GLU A CD  1 
ATOM   1673 O  OE1 . GLU A 1 213 ? -3.642 -8.125  21.338  1.00 15.45 ? 214 GLU A OE1 1 
ATOM   1674 O  OE2 . GLU A 1 213 ? -3.572 -9.759  19.854  1.00 22.88 ? 214 GLU A OE2 1 
ATOM   1675 N  N   . PRO A 1 214 ? 1.889  -9.501  20.271  1.00 9.64  ? 215 PRO A N   1 
ATOM   1676 C  CA  . PRO A 1 214 ? 2.537  -9.461  18.963  1.00 10.11 ? 215 PRO A CA  1 
ATOM   1677 C  C   . PRO A 1 214 ? 1.496  -9.501  17.851  1.00 11.41 ? 215 PRO A C   1 
ATOM   1678 O  O   . PRO A 1 214 ? 0.321  -9.886  18.076  1.00 12.46 ? 215 PRO A O   1 
ATOM   1679 C  CB  . PRO A 1 214 ? 3.378  -10.737 18.898  1.00 10.87 ? 215 PRO A CB  1 
ATOM   1680 C  CG  . PRO A 1 214 ? 2.740  -11.675 19.927  1.00 14.22 ? 215 PRO A CG  1 
ATOM   1681 C  CD  . PRO A 1 214 ? 1.924  -10.833 20.900  1.00 10.96 ? 215 PRO A CD  1 
ATOM   1682 N  N   . ILE A 1 215 ? 1.920  -9.086  16.649  1.00 9.17  ? 216 ILE A N   1 
ATOM   1683 C  CA  . ILE A 1 215 ? 1.107  -9.279  15.461  1.00 9.43  ? 216 ILE A CA  1 
ATOM   1684 C  C   . ILE A 1 215 ? 1.612  -10.542 14.781  1.00 9.95  ? 216 ILE A C   1 
ATOM   1685 O  O   . ILE A 1 215 ? 2.743  -10.953 14.977  1.00 10.40 ? 216 ILE A O   1 
ATOM   1686 C  CB  . ILE A 1 215 ? 1.100  -8.051  14.506  1.00 8.12  ? 216 ILE A CB  1 
ATOM   1687 C  CG1 . ILE A 1 215 ? 2.518  -7.668  14.035  1.00 8.49  ? 216 ILE A CG1 1 
ATOM   1688 C  CG2 . ILE A 1 215 ? 0.351  -6.837  15.174  1.00 8.74  ? 216 ILE A CG2 1 
ATOM   1689 C  CD1 . ILE A 1 215 ? 2.518  -6.693  12.762  1.00 8.11  ? 216 ILE A CD1 1 
ATOM   1690 N  N   A SER A 1 216 ? 0.748  -11.177 13.981  0.50 11.07 ? 217 SER A N   1 
ATOM   1691 N  N   B SER A 1 216 ? 0.761  -11.187 13.989  0.50 10.72 ? 217 SER A N   1 
ATOM   1692 C  CA  A SER A 1 216 ? 1.200  -12.321 13.194  0.50 11.17 ? 217 SER A CA  1 
ATOM   1693 C  CA  B SER A 1 216 ? 1.295  -12.317 13.244  0.50 10.56 ? 217 SER A CA  1 
ATOM   1694 C  C   A SER A 1 216 ? 1.408  -11.900 11.746  0.50 11.31 ? 217 SER A C   1 
ATOM   1695 C  C   B SER A 1 216 ? 1.405  -11.944 11.772  0.50 10.94 ? 217 SER A C   1 
ATOM   1696 O  O   A SER A 1 216 ? 0.595  -11.176 11.184  0.50 12.36 ? 217 SER A O   1 
ATOM   1697 O  O   B SER A 1 216 ? 0.539  -11.270 11.231  0.50 11.85 ? 217 SER A O   1 
ATOM   1698 C  CB  A SER A 1 216 ? 0.230  -13.473 13.237  0.50 12.10 ? 217 SER A CB  1 
ATOM   1699 C  CB  B SER A 1 216 ? 0.467  -13.548 13.416  0.50 11.14 ? 217 SER A CB  1 
ATOM   1700 O  OG  A SER A 1 216 ? 0.136  -13.979 14.556  0.50 12.43 ? 217 SER A OG  1 
ATOM   1701 O  OG  B SER A 1 216 ? -0.889 -13.253 13.138  0.50 10.39 ? 217 SER A OG  1 
ATOM   1702 N  N   . VAL A 1 217 ? 2.491  -12.390 11.152  1.00 11.60 ? 218 VAL A N   1 
ATOM   1703 C  CA  . VAL A 1 217 ? 2.748  -12.161 9.747   1.00 10.79 ? 218 VAL A CA  1 
ATOM   1704 C  C   . VAL A 1 217 ? 3.028  -13.537 9.167   1.00 10.55 ? 218 VAL A C   1 
ATOM   1705 O  O   . VAL A 1 217 ? 3.371  -14.488 9.901   1.00 12.59 ? 218 VAL A O   1 
ATOM   1706 C  CB  . VAL A 1 217 ? 3.941  -11.204 9.534   1.00 10.53 ? 218 VAL A CB  1 
ATOM   1707 C  CG1 . VAL A 1 217 ? 3.635  -9.855  10.177  1.00 10.12 ? 218 VAL A CG1 1 
ATOM   1708 C  CG2 . VAL A 1 217 ? 5.235  -11.827 10.083  1.00 11.58 ? 218 VAL A CG2 1 
ATOM   1709 N  N   . SER A 1 218 ? 2.907  -13.647 7.851   1.00 10.36 ? 219 SER A N   1 
ATOM   1710 C  CA  . SER A 1 218 ? 3.058  -14.961 7.245   1.00 10.93 ? 219 SER A CA  1 
ATOM   1711 C  C   . SER A 1 218 ? 4.519  -15.248 6.982   1.00 11.37 ? 219 SER A C   1 
ATOM   1712 O  O   . SER A 1 218 ? 5.374  -14.356 6.919   1.00 9.47  ? 219 SER A O   1 
ATOM   1713 C  CB  . SER A 1 218 ? 2.241  -15.101 5.977   1.00 10.70 ? 219 SER A CB  1 
ATOM   1714 O  OG  . SER A 1 218 ? 2.785  -14.317 4.940   1.00 12.60 ? 219 SER A OG  1 
ATOM   1715 N  N   . SER A 1 219 ? 4.844  -16.532 6.829   1.00 11.47 ? 220 SER A N   1 
ATOM   1716 C  CA  . SER A 1 219 ? 6.216  -16.847 6.478   1.00 13.85 ? 220 SER A CA  1 
ATOM   1717 C  C   . SER A 1 219 ? 6.592  -16.169 5.151   1.00 14.70 ? 220 SER A C   1 
ATOM   1718 O  O   . SER A 1 219 ? 7.737  -15.732 4.985   1.00 13.57 ? 220 SER A O   1 
ATOM   1719 C  CB  . SER A 1 219 ? 6.429  -18.348 6.426   1.00 16.44 ? 220 SER A CB  1 
ATOM   1720 O  OG  . SER A 1 219 ? 5.482  -18.899 5.523   1.00 19.05 ? 220 SER A OG  1 
ATOM   1721 N  N   . GLU A 1 220 ? 5.643  -16.047 4.197   1.00 13.57 ? 221 GLU A N   1 
ATOM   1722 C  CA  . GLU A 1 220 ? 5.987  -15.470 2.905   1.00 14.77 ? 221 GLU A CA  1 
ATOM   1723 C  C   . GLU A 1 220 ? 6.252  -13.970 3.064   1.00 13.59 ? 221 GLU A C   1 
ATOM   1724 O  O   . GLU A 1 220 ? 7.097  -13.431 2.361   1.00 13.34 ? 221 GLU A O   1 
ATOM   1725 C  CB  . GLU A 1 220 ? 4.892  -15.650 1.854   1.00 16.11 ? 221 GLU A CB  1 
ATOM   1726 C  CG  . GLU A 1 220 ? 4.684  -17.131 1.532   1.00 19.66 ? 221 GLU A CG  1 
ATOM   1727 C  CD  . GLU A 1 220 ? 3.559  -17.803 2.313   1.00 24.08 ? 221 GLU A CD  1 
ATOM   1728 O  OE1 . GLU A 1 220 ? 3.155  -17.302 3.373   1.00 21.65 ? 221 GLU A OE1 1 
ATOM   1729 O  OE2 . GLU A 1 220 ? 3.063  -18.838 1.849   1.00 31.16 ? 221 GLU A OE2 1 
ATOM   1730 N  N   . GLN A 1 221 ? 5.541  -13.323 4.001   1.00 11.81 ? 222 GLN A N   1 
ATOM   1731 C  CA  . GLN A 1 221 ? 5.774  -11.894 4.220   1.00 11.10 ? 222 GLN A CA  1 
ATOM   1732 C  C   . GLN A 1 221 ? 7.194  -11.670 4.729   1.00 11.89 ? 222 GLN A C   1 
ATOM   1733 O  O   . GLN A 1 221 ? 7.927  -10.784 4.238   1.00 9.66  ? 222 GLN A O   1 
ATOM   1734 C  CB  . GLN A 1 221 ? 4.693  -11.350 5.170   1.00 11.55 ? 222 GLN A CB  1 
ATOM   1735 C  CG  . GLN A 1 221 ? 3.340  -11.182 4.448   1.00 12.18 ? 222 GLN A CG  1 
ATOM   1736 C  CD  . GLN A 1 221 ? 2.264  -10.589 5.326   1.00 12.03 ? 222 GLN A CD  1 
ATOM   1737 O  OE1 . GLN A 1 221 ? 2.109  -11.008 6.455   1.00 11.92 ? 222 GLN A OE1 1 
ATOM   1738 N  NE2 . GLN A 1 221 ? 1.429  -9.710  4.783   1.00 12.96 ? 222 GLN A NE2 1 
ATOM   1739 N  N   . VAL A 1 222 ? 7.591  -12.470 5.731   1.00 11.34 ? 223 VAL A N   1 
ATOM   1740 C  CA  . VAL A 1 222 ? 8.914  -12.258 6.323   1.00 12.77 ? 223 VAL A CA  1 
ATOM   1741 C  C   . VAL A 1 222 ? 10.010 -12.702 5.340   1.00 13.55 ? 223 VAL A C   1 
ATOM   1742 O  O   . VAL A 1 222 ? 11.077 -12.088 5.268   1.00 12.19 ? 223 VAL A O   1 
ATOM   1743 C  CB  . VAL A 1 222 ? 9.066  -12.856 7.737   1.00 14.43 ? 223 VAL A CB  1 
ATOM   1744 C  CG1 . VAL A 1 222 ? 9.107  -14.364 7.690   1.00 16.71 ? 223 VAL A CG1 1 
ATOM   1745 C  CG2 . VAL A 1 222 ? 10.359 -12.351 8.401   1.00 15.27 ? 223 VAL A CG2 1 
ATOM   1746 N  N   . LEU A 1 223 ? 9.697  -13.693 4.495   1.00 14.13 ? 224 LEU A N   1 
ATOM   1747 C  CA  . LEU A 1 223 ? 10.654 -14.112 3.486   1.00 16.08 ? 224 LEU A CA  1 
ATOM   1748 C  C   . LEU A 1 223 ? 11.027 -12.964 2.562   1.00 15.80 ? 224 LEU A C   1 
ATOM   1749 O  O   . LEU A 1 223 ? 12.203 -12.861 2.174   1.00 16.10 ? 224 LEU A O   1 
ATOM   1750 C  CB  . LEU A 1 223 ? 10.127 -15.317 2.689   1.00 18.14 ? 224 LEU A CB  1 
ATOM   1751 C  CG  . LEU A 1 223 ? 10.494 -16.692 3.251   1.00 26.05 ? 224 LEU A CG  1 
ATOM   1752 C  CD1 . LEU A 1 223 ? 9.981  -17.808 2.317   1.00 27.57 ? 224 LEU A CD1 1 
ATOM   1753 C  CD2 . LEU A 1 223 ? 12.010 -16.832 3.445   1.00 26.95 ? 224 LEU A CD2 1 
ATOM   1754 N  N   . LYS A 1 224 ? 10.040 -12.119 2.242   1.00 13.25 ? 225 LYS A N   1 
ATOM   1755 C  CA  . LYS A 1 224 ? 10.244 -10.996 1.334   1.00 14.71 ? 225 LYS A CA  1 
ATOM   1756 C  C   . LYS A 1 224 ? 11.154 -9.948  1.977   1.00 13.51 ? 225 LYS A C   1 
ATOM   1757 O  O   . LYS A 1 224 ? 11.975 -9.342  1.273   1.00 12.88 ? 225 LYS A O   1 
ATOM   1758 C  CB  . LYS A 1 224 ? 8.915  -10.492 0.754   1.00 15.61 ? 225 LYS A CB  1 
ATOM   1759 C  CG  . LYS A 1 224 ? 8.286  -11.503 -0.238  1.00 20.75 ? 225 LYS A CG  1 
ATOM   1760 C  CD  . LYS A 1 224 ? 7.023  -11.131 -0.992  1.00 25.85 ? 225 LYS A CD  1 
ATOM   1761 C  CE  . LYS A 1 224 ? 6.389  -12.354 -1.662  1.00 26.13 ? 225 LYS A CE  1 
ATOM   1762 N  NZ  . LYS A 1 224 ? 5.171  -12.016 -2.458  1.00 33.35 ? 225 LYS A NZ  1 
ATOM   1763 N  N   . PHE A 1 225 ? 11.052 -9.741  3.314   1.00 13.32 ? 226 PHE A N   1 
ATOM   1764 C  CA  . PHE A 1 225 ? 12.003 -8.876  4.023   1.00 11.48 ? 226 PHE A CA  1 
ATOM   1765 C  C   . PHE A 1 225 ? 13.434 -9.361  3.808   1.00 11.89 ? 226 PHE A C   1 
ATOM   1766 O  O   . PHE A 1 225 ? 14.333 -8.559  3.623   1.00 11.40 ? 226 PHE A O   1 
ATOM   1767 C  CB  . PHE A 1 225 ? 11.799 -8.891  5.551   1.00 11.64 ? 226 PHE A CB  1 
ATOM   1768 C  CG  . PHE A 1 225 ? 10.628 -8.102  6.102   1.00 12.59 ? 226 PHE A CG  1 
ATOM   1769 C  CD1 . PHE A 1 225 ? 9.579  -7.665  5.304   1.00 12.90 ? 226 PHE A CD1 1 
ATOM   1770 C  CD2 . PHE A 1 225 ? 10.553 -7.865  7.479   1.00 13.25 ? 226 PHE A CD2 1 
ATOM   1771 C  CE1 . PHE A 1 225 ? 8.522  -6.943  5.843   1.00 14.19 ? 226 PHE A CE1 1 
ATOM   1772 C  CE2 . PHE A 1 225 ? 9.487  -7.167  8.026   1.00 15.78 ? 226 PHE A CE2 1 
ATOM   1773 C  CZ  . PHE A 1 225 ? 8.482  -6.679  7.198   1.00 14.66 ? 226 PHE A CZ  1 
ATOM   1774 N  N   . ARG A 1 226 ? 13.633 -10.671 3.852   1.00 10.82 ? 227 ARG A N   1 
ATOM   1775 C  CA  . ARG A 1 226 ? 14.943 -11.313 3.736   1.00 11.83 ? 227 ARG A CA  1 
ATOM   1776 C  C   . ARG A 1 226 ? 15.530 -11.274 2.321   1.00 13.43 ? 227 ARG A C   1 
ATOM   1777 O  O   . ARG A 1 226 ? 16.700 -11.643 2.142   1.00 13.15 ? 227 ARG A O   1 
ATOM   1778 C  CB  . ARG A 1 226 ? 14.841 -12.757 4.228   1.00 11.03 ? 227 ARG A CB  1 
ATOM   1779 C  CG  . ARG A 1 226 ? 14.497 -12.889 5.702   1.00 11.40 ? 227 ARG A CG  1 
ATOM   1780 C  CD  . ARG A 1 226 ? 14.556 -14.334 6.194   1.00 11.30 ? 227 ARG A CD  1 
ATOM   1781 N  NE  . ARG A 1 226 ? 13.965 -14.422 7.550   1.00 12.00 ? 227 ARG A NE  1 
ATOM   1782 C  CZ  . ARG A 1 226 ? 13.018 -15.283 7.908   1.00 12.56 ? 227 ARG A CZ  1 
ATOM   1783 N  NH1 . ARG A 1 226 ? 12.590 -16.226 7.057   1.00 13.99 ? 227 ARG A NH1 1 
ATOM   1784 N  NH2 . ARG A 1 226 ? 12.558 -15.242 9.134   1.00 12.11 ? 227 ARG A NH2 1 
ATOM   1785 N  N   . LYS A 1 227 ? 14.773 -10.775 1.339   1.00 13.26 ? 228 LYS A N   1 
ATOM   1786 C  CA  . LYS A 1 227 ? 15.318 -10.666 -0.008  1.00 14.36 ? 228 LYS A CA  1 
ATOM   1787 C  C   . LYS A 1 227 ? 15.965 -9.305  -0.255  1.00 14.84 ? 228 LYS A C   1 
ATOM   1788 O  O   . LYS A 1 227 ? 16.638 -9.090  -1.264  1.00 15.78 ? 228 LYS A O   1 
ATOM   1789 C  CB  . LYS A 1 227 ? 14.201 -10.924 -1.026  1.00 13.59 ? 228 LYS A CB  1 
ATOM   1790 C  CG  . LYS A 1 227 ? 13.840 -12.399 -1.099  1.00 14.98 ? 228 LYS A CG  1 
ATOM   1791 C  CD  . LYS A 1 227 ? 12.698 -12.624 -2.090  1.00 21.20 ? 228 LYS A CD  1 
ATOM   1792 N  N   . LEU A 1 228 ? 15.775 -8.377  0.687   1.00 14.57 ? 229 LEU A N   1 
ATOM   1793 C  CA  . LEU A 1 228 ? 16.391 -7.066  0.551   1.00 14.37 ? 229 LEU A CA  1 
ATOM   1794 C  C   . LEU A 1 228 ? 17.896 -7.209  0.741   1.00 14.17 ? 229 LEU A C   1 
ATOM   1795 O  O   . LEU A 1 228 ? 18.408 -8.245  1.181   1.00 12.40 ? 229 LEU A O   1 
ATOM   1796 C  CB  . LEU A 1 228 ? 15.853 -6.191  1.687   1.00 12.20 ? 229 LEU A CB  1 
ATOM   1797 C  CG  . LEU A 1 228 ? 14.447 -5.647  1.496   1.00 12.71 ? 229 LEU A CG  1 
ATOM   1798 C  CD1 . LEU A 1 228 ? 13.968 -5.027  2.790   1.00 12.25 ? 229 LEU A CD1 1 
ATOM   1799 C  CD2 . LEU A 1 228 ? 14.458 -4.584  0.425   1.00 11.96 ? 229 LEU A CD2 1 
ATOM   1800 N  N   . ASN A 1 229 ? 18.600 -6.098  0.481   1.00 15.42 ? 230 ASN A N   1 
ATOM   1801 C  CA  . ASN A 1 229 ? 20.047 -6.145  0.416   1.00 14.65 ? 230 ASN A CA  1 
ATOM   1802 C  C   . ASN A 1 229 ? 20.606 -4.993  1.248   1.00 13.81 ? 230 ASN A C   1 
ATOM   1803 O  O   . ASN A 1 229 ? 20.120 -3.878  1.186   1.00 13.39 ? 230 ASN A O   1 
ATOM   1804 C  CB  . ASN A 1 229 ? 20.537 -5.910  -1.024  1.00 14.98 ? 230 ASN A CB  1 
ATOM   1805 C  CG  . ASN A 1 229 ? 20.461 -7.094  -1.967  1.00 17.79 ? 230 ASN A CG  1 
ATOM   1806 O  OD1 . ASN A 1 229 ? 21.016 -6.998  -3.069  1.00 17.78 ? 230 ASN A OD1 1 
ATOM   1807 N  ND2 . ASN A 1 229 ? 19.815 -8.187  -1.576  1.00 16.76 ? 230 ASN A ND2 1 
ATOM   1808 N  N   . PHE A 1 230 ? 21.652 -5.265  2.008   1.00 14.59 ? 231 PHE A N   1 
ATOM   1809 C  CA  . PHE A 1 230 ? 22.367 -4.223  2.735   1.00 14.77 ? 231 PHE A CA  1 
ATOM   1810 C  C   . PHE A 1 230 ? 23.238 -3.397  1.784   1.00 18.05 ? 231 PHE A C   1 
ATOM   1811 O  O   . PHE A 1 230 ? 23.483 -2.217  2.046   1.00 16.56 ? 231 PHE A O   1 
ATOM   1812 C  CB  . PHE A 1 230 ? 23.358 -4.848  3.710   1.00 15.26 ? 231 PHE A CB  1 
ATOM   1813 C  CG  . PHE A 1 230 ? 22.812 -5.431  5.012   1.00 15.23 ? 231 PHE A CG  1 
ATOM   1814 C  CD1 . PHE A 1 230 ? 22.091 -4.656  5.918   1.00 14.68 ? 231 PHE A CD1 1 
ATOM   1815 C  CD2 . PHE A 1 230 ? 23.124 -6.745  5.362   1.00 14.37 ? 231 PHE A CD2 1 
ATOM   1816 C  CE1 . PHE A 1 230 ? 21.656 -5.207  7.130   1.00 14.62 ? 231 PHE A CE1 1 
ATOM   1817 C  CE2 . PHE A 1 230 ? 22.710 -7.301  6.569   1.00 15.06 ? 231 PHE A CE2 1 
ATOM   1818 C  CZ  . PHE A 1 230 ? 21.982 -6.524  7.451   1.00 13.00 ? 231 PHE A CZ  1 
ATOM   1819 N  N   . ASN A 1 231 ? 23.719 -4.052  0.725   1.00 17.31 ? 232 ASN A N   1 
ATOM   1820 C  CA  . ASN A 1 231 ? 24.654 -3.461  -0.228  1.00 19.15 ? 232 ASN A CA  1 
ATOM   1821 C  C   . ASN A 1 231 ? 23.917 -2.546  -1.193  1.00 19.26 ? 232 ASN A C   1 
ATOM   1822 O  O   . ASN A 1 231 ? 22.707 -2.671  -1.359  1.00 16.56 ? 232 ASN A O   1 
ATOM   1823 C  CB  . ASN A 1 231 ? 25.330 -4.559  -1.040  1.00 18.87 ? 232 ASN A CB  1 
ATOM   1824 C  CG  . ASN A 1 231 ? 24.319 -5.440  -1.736  1.00 18.88 ? 232 ASN A CG  1 
ATOM   1825 O  OD1 . ASN A 1 231 ? 23.792 -6.371  -1.118  1.00 19.47 ? 232 ASN A OD1 1 
ATOM   1826 N  ND2 . ASN A 1 231 ? 24.025 -5.136  -3.001  1.00 17.56 ? 232 ASN A ND2 1 
ATOM   1827 N  N   . GLY A 1 232 ? 24.667 -1.634  -1.840  1.00 17.25 ? 233 GLY A N   1 
ATOM   1828 C  CA  . GLY A 1 232 ? 24.111 -0.830  -2.924  1.00 18.02 ? 233 GLY A CA  1 
ATOM   1829 C  C   . GLY A 1 232 ? 24.070 -1.606  -4.241  1.00 18.83 ? 233 GLY A C   1 
ATOM   1830 O  O   . GLY A 1 232 ? 24.762 -2.611  -4.397  1.00 20.50 ? 233 GLY A O   1 
ATOM   1831 N  N   . GLU A 1 233 ? 23.275 -1.099  -5.197  1.00 21.04 ? 234 GLU A N   1 
ATOM   1832 C  CA  . GLU A 1 233 ? 23.153 -1.681  -6.524  1.00 22.73 ? 234 GLU A CA  1 
ATOM   1833 C  C   . GLU A 1 233 ? 24.549 -1.800  -7.138  1.00 23.12 ? 234 GLU A C   1 
ATOM   1834 O  O   . GLU A 1 233 ? 25.379 -0.917  -6.973  1.00 21.14 ? 234 GLU A O   1 
ATOM   1835 C  CB  . GLU A 1 233 ? 22.242 -0.800  -7.376  1.00 23.52 ? 234 GLU A CB  1 
ATOM   1836 C  CG  . GLU A 1 233 ? 22.002 -1.340  -8.775  1.00 24.34 ? 234 GLU A CG  1 
ATOM   1837 C  CD  . GLU A 1 233 ? 21.142 -0.456  -9.649  1.00 29.82 ? 234 GLU A CD  1 
ATOM   1838 O  OE1 . GLU A 1 233 ? 20.819 0.709   -9.216  1.00 26.59 ? 234 GLU A OE1 1 
ATOM   1839 O  OE2 . GLU A 1 233 ? 20.812 -0.928  -10.772 1.00 31.03 ? 234 GLU A OE2 1 
ATOM   1840 N  N   . GLY A 1 234 ? 24.810 -2.932  -7.791  1.00 25.45 ? 235 GLY A N   1 
ATOM   1841 C  CA  . GLY A 1 234 ? 26.097 -3.161  -8.424  1.00 31.24 ? 235 GLY A CA  1 
ATOM   1842 C  C   . GLY A 1 234 ? 27.224 -3.417  -7.426  1.00 32.27 ? 235 GLY A C   1 
ATOM   1843 O  O   . GLY A 1 234 ? 28.391 -3.290  -7.784  1.00 28.81 ? 235 GLY A O   1 
ATOM   1844 N  N   . GLU A 1 235 ? 26.873 -3.764  -6.176  1.00 30.55 ? 236 GLU A N   1 
ATOM   1845 C  CA  . GLU A 1 235 ? 27.847 -4.322  -5.243  1.00 28.50 ? 236 GLU A CA  1 
ATOM   1846 C  C   . GLU A 1 235 ? 27.458 -5.771  -4.985  1.00 29.01 ? 236 GLU A C   1 
ATOM   1847 O  O   . GLU A 1 235 ? 26.339 -6.175  -5.325  1.00 28.44 ? 236 GLU A O   1 
ATOM   1848 C  CB  . GLU A 1 235 ? 27.897 -3.552  -3.922  1.00 32.79 ? 236 GLU A CB  1 
ATOM   1849 C  CG  . GLU A 1 235 ? 28.336 -2.112  -4.074  1.00 36.91 ? 236 GLU A CG  1 
ATOM   1850 C  CD  . GLU A 1 235 ? 28.074 -1.193  -2.883  1.00 46.62 ? 236 GLU A CD  1 
ATOM   1851 O  OE1 . GLU A 1 235 ? 27.494 -1.655  -1.846  1.00 42.72 ? 236 GLU A OE1 1 
ATOM   1852 O  OE2 . GLU A 1 235 ? 28.441 0.002   -2.986  1.00 55.23 ? 236 GLU A OE2 1 
ATOM   1853 N  N   . PRO A 1 236 ? 28.380 -6.594  -4.427  1.00 25.73 ? 237 PRO A N   1 
ATOM   1854 C  CA  . PRO A 1 236 ? 28.113 -8.008  -4.175  1.00 27.18 ? 237 PRO A CA  1 
ATOM   1855 C  C   . PRO A 1 236 ? 26.940 -8.130  -3.200  1.00 25.98 ? 237 PRO A C   1 
ATOM   1856 O  O   . PRO A 1 236 ? 26.825 -7.329  -2.280  1.00 22.88 ? 237 PRO A O   1 
ATOM   1857 C  CB  . PRO A 1 236 ? 29.414 -8.498  -3.512  1.00 29.14 ? 237 PRO A CB  1 
ATOM   1858 C  CG  . PRO A 1 236 ? 30.475 -7.512  -3.956  1.00 29.63 ? 237 PRO A CG  1 
ATOM   1859 C  CD  . PRO A 1 236 ? 29.745 -6.191  -4.029  1.00 29.50 ? 237 PRO A CD  1 
ATOM   1860 N  N   . GLU A 1 237 ? 26.078 -9.122  -3.436  1.00 24.57 ? 238 GLU A N   1 
ATOM   1861 C  CA  . GLU A 1 237 ? 24.841 -9.228  -2.690  1.00 23.93 ? 238 GLU A CA  1 
ATOM   1862 C  C   . GLU A 1 237 ? 25.134 -9.692  -1.259  1.00 21.33 ? 238 GLU A C   1 
ATOM   1863 O  O   . GLU A 1 237 ? 25.723 -10.737 -1.016  1.00 20.87 ? 238 GLU A O   1 
ATOM   1864 C  CB  . GLU A 1 237 ? 23.810 -10.079 -3.432  1.00 22.60 ? 238 GLU A CB  1 
ATOM   1865 C  CG  . GLU A 1 237 ? 22.534 -10.231 -2.646  1.00 22.83 ? 238 GLU A CG  1 
ATOM   1866 C  CD  . GLU A 1 237 ? 21.411 -10.918 -3.397  1.00 26.94 ? 238 GLU A CD  1 
ATOM   1867 O  OE1 . GLU A 1 237 ? 21.706 -11.960 -4.044  1.00 32.72 ? 238 GLU A OE1 1 
ATOM   1868 O  OE2 . GLU A 1 237 ? 20.262 -10.428 -3.343  1.00 19.71 ? 238 GLU A OE2 1 
ATOM   1869 N  N   . GLU A 1 238 ? 24.674 -8.883  -0.306  1.00 19.32 ? 239 GLU A N   1 
ATOM   1870 C  CA  . GLU A 1 238 ? 24.671 -9.264  1.084   1.00 18.95 ? 239 GLU A CA  1 
ATOM   1871 C  C   . GLU A 1 238 ? 23.215 -9.165  1.546   1.00 16.15 ? 239 GLU A C   1 
ATOM   1872 O  O   . GLU A 1 238 ? 22.661 -8.083  1.509   1.00 15.80 ? 239 GLU A O   1 
ATOM   1873 C  CB  . GLU A 1 238 ? 25.491 -8.224  1.846   1.00 20.81 ? 239 GLU A CB  1 
ATOM   1874 C  CG  . GLU A 1 238 ? 25.707 -8.654  3.270   1.00 28.93 ? 239 GLU A CG  1 
ATOM   1875 C  CD  . GLU A 1 238 ? 26.616 -9.864  3.418   1.00 37.37 ? 239 GLU A CD  1 
ATOM   1876 O  OE1 . GLU A 1 238 ? 27.778 -9.789  2.903   1.00 37.43 ? 239 GLU A OE1 1 
ATOM   1877 O  OE2 . GLU A 1 238 ? 26.172 -10.860 4.067   1.00 36.88 ? 239 GLU A OE2 1 
ATOM   1878 N  N   . LEU A 1 239 ? 22.560 -10.295 1.864   1.00 15.41 ? 240 LEU A N   1 
ATOM   1879 C  CA  . LEU A 1 239 ? 21.137 -10.192 2.163   1.00 13.05 ? 240 LEU A CA  1 
ATOM   1880 C  C   . LEU A 1 239 ? 20.943 -9.396  3.464   1.00 11.45 ? 240 LEU A C   1 
ATOM   1881 O  O   . LEU A 1 239 ? 21.701 -9.569  4.426   1.00 12.90 ? 240 LEU A O   1 
ATOM   1882 C  CB  . LEU A 1 239 ? 20.618 -11.614 2.401   1.00 15.02 ? 240 LEU A CB  1 
ATOM   1883 C  CG  . LEU A 1 239 ? 20.466 -12.512 1.171   1.00 15.97 ? 240 LEU A CG  1 
ATOM   1884 C  CD1 . LEU A 1 239 ? 19.742 -13.785 1.598   1.00 19.19 ? 240 LEU A CD1 1 
ATOM   1885 C  CD2 . LEU A 1 239 ? 19.649 -11.786 0.108   1.00 16.81 ? 240 LEU A CD2 1 
ATOM   1886 N  N   . MET A 1 240 ? 19.878 -8.575  3.483   1.00 11.68 ? 241 MET A N   1 
ATOM   1887 C  CA  . MET A 1 240 ? 19.488 -7.796  4.657   1.00 11.16 ? 241 MET A CA  1 
ATOM   1888 C  C   . MET A 1 240 ? 18.721 -8.724  5.606   1.00 10.38 ? 241 MET A C   1 
ATOM   1889 O  O   . MET A 1 240 ? 17.507 -8.885  5.473   1.00 10.76 ? 241 MET A O   1 
ATOM   1890 C  CB  . MET A 1 240 ? 18.631 -6.583  4.280   1.00 12.30 ? 241 MET A CB  1 
ATOM   1891 C  CG  . MET A 1 240 ? 18.344 -5.599  5.503   1.00 11.84 ? 241 MET A CG  1 
ATOM   1892 S  SD  . MET A 1 240 ? 17.384 -4.199  4.956   1.00 14.44 ? 241 MET A SD  1 
ATOM   1893 C  CE  . MET A 1 240 ? 18.711 -3.159  4.319   1.00 12.55 ? 241 MET A CE  1 
ATOM   1894 N  N   . VAL A 1 241 ? 19.480 -9.337  6.525   1.00 9.55  ? 242 VAL A N   1 
ATOM   1895 C  CA  . VAL A 1 241 ? 18.967 -10.232 7.561   1.00 9.79  ? 242 VAL A CA  1 
ATOM   1896 C  C   . VAL A 1 241 ? 19.763 -9.963  8.849   1.00 10.44 ? 242 VAL A C   1 
ATOM   1897 O  O   . VAL A 1 241 ? 20.942 -9.538  8.827   1.00 10.86 ? 242 VAL A O   1 
ATOM   1898 C  CB  . VAL A 1 241 ? 18.984 -11.741 7.200   1.00 9.04  ? 242 VAL A CB  1 
ATOM   1899 C  CG1 . VAL A 1 241 ? 18.123 -12.042 5.960   1.00 9.72  ? 242 VAL A CG1 1 
ATOM   1900 C  CG2 . VAL A 1 241 ? 20.400 -12.298 7.064   1.00 9.78  ? 242 VAL A CG2 1 
ATOM   1901 N  N   . ASP A 1 242 ? 19.140 -10.327 9.982   1.00 8.72  ? 243 ASP A N   1 
ATOM   1902 C  CA  . ASP A 1 242 ? 19.791 -10.180 11.276  1.00 9.38  ? 243 ASP A CA  1 
ATOM   1903 C  C   . ASP A 1 242 ? 20.272 -8.744  11.492  1.00 8.99  ? 243 ASP A C   1 
ATOM   1904 O  O   . ASP A 1 242 ? 21.379 -8.557  12.027  1.00 10.60 ? 243 ASP A O   1 
ATOM   1905 C  CB  . ASP A 1 242 ? 20.898 -11.214 11.569  1.00 10.03 ? 243 ASP A CB  1 
ATOM   1906 C  CG  . ASP A 1 242 ? 20.350 -12.626 11.643  1.00 11.50 ? 243 ASP A CG  1 
ATOM   1907 O  OD1 . ASP A 1 242 ? 19.299 -12.824 12.287  1.00 11.10 ? 243 ASP A OD1 1 
ATOM   1908 O  OD2 . ASP A 1 242 ? 20.940 -13.530 11.001  1.00 12.41 ? 243 ASP A OD2 1 
ATOM   1909 N  N   . ASN A 1 243 ? 19.378 -7.772  11.242  1.00 8.66  ? 244 ASN A N   1 
ATOM   1910 C  CA  . ASN A 1 243 ? 19.711 -6.355  11.452  1.00 8.26  ? 244 ASN A CA  1 
ATOM   1911 C  C   . ASN A 1 243 ? 19.162 -5.931  12.820  1.00 8.57  ? 244 ASN A C   1 
ATOM   1912 O  O   . ASN A 1 243 ? 18.437 -4.923  12.934  1.00 9.00  ? 244 ASN A O   1 
ATOM   1913 C  CB  . ASN A 1 243 ? 19.145 -5.479  10.321  1.00 9.89  ? 244 ASN A CB  1 
ATOM   1914 C  CG  . ASN A 1 243 ? 17.653 -5.661  10.075  1.00 10.59 ? 244 ASN A CG  1 
ATOM   1915 O  OD1 . ASN A 1 243 ? 17.005 -6.534  10.685  1.00 10.79 ? 244 ASN A OD1 1 
ATOM   1916 N  ND2 . ASN A 1 243 ? 17.072 -4.805  9.230   1.00 10.85 ? 244 ASN A ND2 1 
ATOM   1917 N  N   . TRP A 1 244 ? 19.502 -6.703  13.846  1.00 7.85  ? 245 TRP A N   1 
ATOM   1918 C  CA  . TRP A 1 244 ? 18.995 -6.445  15.195  1.00 8.37  ? 245 TRP A CA  1 
ATOM   1919 C  C   . TRP A 1 244 ? 20.163 -6.339  16.152  1.00 8.80  ? 245 TRP A C   1 
ATOM   1920 O  O   . TRP A 1 244 ? 21.170 -7.027  15.985  1.00 9.12  ? 245 TRP A O   1 
ATOM   1921 C  CB  . TRP A 1 244 ? 18.016 -7.531  15.711  1.00 8.51  ? 245 TRP A CB  1 
ATOM   1922 C  CG  . TRP A 1 244 ? 18.504 -8.946  15.526  1.00 8.06  ? 245 TRP A CG  1 
ATOM   1923 C  CD1 . TRP A 1 244 ? 18.342 -9.716  14.409  1.00 8.96  ? 245 TRP A CD1 1 
ATOM   1924 C  CD2 . TRP A 1 244 ? 19.013 -9.832  16.536  1.00 8.99  ? 245 TRP A CD2 1 
ATOM   1925 N  NE1 . TRP A 1 244 ? 18.794 -10.997 14.616  1.00 8.92  ? 245 TRP A NE1 1 
ATOM   1926 C  CE2 . TRP A 1 244 ? 19.245 -11.081 15.910  1.00 9.31  ? 245 TRP A CE2 1 
ATOM   1927 C  CE3 . TRP A 1 244 ? 19.354 -9.683  17.892  1.00 9.20  ? 245 TRP A CE3 1 
ATOM   1928 C  CZ2 . TRP A 1 244 ? 19.842 -12.146 16.585  1.00 9.17  ? 245 TRP A CZ2 1 
ATOM   1929 C  CZ3 . TRP A 1 244 ? 19.941 -10.740 18.572  1.00 9.23  ? 245 TRP A CZ3 1 
ATOM   1930 C  CH2 . TRP A 1 244 ? 20.118 -11.968 17.929  1.00 9.12  ? 245 TRP A CH2 1 
ATOM   1931 N  N   . ARG A 1 245 ? 20.022 -5.446  17.151  1.00 7.68  ? 246 ARG A N   1 
ATOM   1932 C  CA  . ARG A 1 245 ? 20.973 -5.368  18.252  1.00 7.62  ? 246 ARG A CA  1 
ATOM   1933 C  C   . ARG A 1 245 ? 20.466 -6.263  19.372  1.00 7.67  ? 246 ARG A C   1 
ATOM   1934 O  O   . ARG A 1 245 ? 19.272 -6.273  19.673  1.00 8.51  ? 246 ARG A O   1 
ATOM   1935 C  CB  . ARG A 1 245 ? 21.023 -3.919  18.762  1.00 7.32  ? 246 ARG A CB  1 
ATOM   1936 C  CG  . ARG A 1 245 ? 22.132 -3.687  19.788  1.00 7.46  ? 246 ARG A CG  1 
ATOM   1937 C  CD  . ARG A 1 245 ? 22.020 -2.286  20.413  1.00 7.71  ? 246 ARG A CD  1 
ATOM   1938 N  NE  . ARG A 1 245 ? 23.296 -1.988  21.162  1.00 8.47  ? 246 ARG A NE  1 
ATOM   1939 C  CZ  . ARG A 1 245 ? 23.488 -0.944  21.954  1.00 9.71  ? 246 ARG A CZ  1 
ATOM   1940 N  NH1 . ARG A 1 245 ? 22.473 -0.134  22.259  1.00 8.45  ? 246 ARG A NH1 1 
ATOM   1941 N  NH2 . ARG A 1 245 ? 24.695 -0.736  22.476  1.00 10.22 ? 246 ARG A NH2 1 
ATOM   1942 N  N   . PRO A 1 246 ? 21.340 -7.061  20.006  1.00 8.71  ? 247 PRO A N   1 
ATOM   1943 C  CA  . PRO A 1 246 ? 20.974 -7.902  21.142  1.00 8.68  ? 247 PRO A CA  1 
ATOM   1944 C  C   . PRO A 1 246 ? 20.642 -7.049  22.364  1.00 8.77  ? 247 PRO A C   1 
ATOM   1945 O  O   . PRO A 1 246 ? 21.047 -5.885  22.501  1.00 8.62  ? 247 PRO A O   1 
ATOM   1946 C  CB  . PRO A 1 246 ? 22.284 -8.661  21.451  1.00 9.93  ? 247 PRO A CB  1 
ATOM   1947 C  CG  . PRO A 1 246 ? 23.093 -8.516  20.179  1.00 10.40 ? 247 PRO A CG  1 
ATOM   1948 C  CD  . PRO A 1 246 ? 22.769 -7.132  19.685  1.00 9.20  ? 247 PRO A CD  1 
ATOM   1949 N  N   . ALA A 1 247 ? 19.980 -7.711  23.310  1.00 9.00  ? 248 ALA A N   1 
ATOM   1950 C  CA  . ALA A 1 247 ? 19.635 -7.122  24.598  1.00 8.57  ? 248 ALA A CA  1 
ATOM   1951 C  C   . ALA A 1 247 ? 20.887 -6.593  25.306  1.00 9.92  ? 248 ALA A C   1 
ATOM   1952 O  O   . ALA A 1 247 ? 21.973 -7.220  25.304  1.00 10.20 ? 248 ALA A O   1 
ATOM   1953 C  CB  . ALA A 1 247 ? 18.920 -8.209  25.422  1.00 9.38  ? 248 ALA A CB  1 
ATOM   1954 N  N   . GLN A 1 248 ? 20.721 -5.417  25.911  1.00 8.93  ? 249 GLN A N   1 
ATOM   1955 C  CA  . GLN A 1 248 ? 21.765 -4.682  26.623  1.00 9.62  ? 249 GLN A CA  1 
ATOM   1956 C  C   . GLN A 1 248 ? 21.440 -4.675  28.118  1.00 9.93  ? 249 GLN A C   1 
ATOM   1957 O  O   . GLN A 1 248 ? 20.296 -4.843  28.530  1.00 9.38  ? 249 GLN A O   1 
ATOM   1958 C  CB  . GLN A 1 248 ? 21.796 -3.243  26.108  1.00 10.68 ? 249 GLN A CB  1 
ATOM   1959 C  CG  . GLN A 1 248 ? 22.121 -3.139  24.604  1.00 10.18 ? 249 GLN A CG  1 
ATOM   1960 C  CD  . GLN A 1 248 ? 23.459 -3.775  24.251  1.00 11.36 ? 249 GLN A CD  1 
ATOM   1961 O  OE1 . GLN A 1 248 ? 24.505 -3.446  24.834  1.00 14.61 ? 249 GLN A OE1 1 
ATOM   1962 N  NE2 . GLN A 1 248 ? 23.451 -4.713  23.310  1.00 11.79 ? 249 GLN A NE2 1 
ATOM   1963 N  N   . PRO A 1 249 ? 22.442 -4.403  28.990  1.00 11.83 ? 250 PRO A N   1 
ATOM   1964 C  CA  . PRO A 1 249 ? 22.246 -4.430  30.437  1.00 11.85 ? 250 PRO A CA  1 
ATOM   1965 C  C   . PRO A 1 249 ? 21.217 -3.397  30.898  1.00 10.74 ? 250 PRO A C   1 
ATOM   1966 O  O   . PRO A 1 249 ? 21.272 -2.237  30.509  1.00 11.30 ? 250 PRO A O   1 
ATOM   1967 C  CB  . PRO A 1 249 ? 23.623 -3.955  30.949  1.00 12.08 ? 250 PRO A CB  1 
ATOM   1968 C  CG  . PRO A 1 249 ? 24.561 -4.465  29.895  1.00 13.99 ? 250 PRO A CG  1 
ATOM   1969 C  CD  . PRO A 1 249 ? 23.838 -4.121  28.608  1.00 12.45 ? 250 PRO A CD  1 
ATOM   1970 N  N   . LEU A 1 250 ? 20.283 -3.851  31.729  1.00 10.94 ? 251 LEU A N   1 
ATOM   1971 C  CA  . LEU A 1 250 ? 19.200 -2.991  32.189  1.00 11.63 ? 251 LEU A CA  1 
ATOM   1972 C  C   . LEU A 1 250 ? 19.786 -1.937  33.127  1.00 11.79 ? 251 LEU A C   1 
ATOM   1973 O  O   . LEU A 1 250 ? 19.288 -0.813  33.187  1.00 10.94 ? 251 LEU A O   1 
ATOM   1974 C  CB  . LEU A 1 250 ? 18.160 -3.876  32.884  1.00 12.88 ? 251 LEU A CB  1 
ATOM   1975 C  CG  . LEU A 1 250 ? 16.855 -3.205  33.315  1.00 12.87 ? 251 LEU A CG  1 
ATOM   1976 C  CD1 . LEU A 1 250 ? 16.118 -2.616  32.103  1.00 12.65 ? 251 LEU A CD1 1 
ATOM   1977 C  CD2 . LEU A 1 250 ? 15.974 -4.204  34.076  1.00 16.70 ? 251 LEU A CD2 1 
ATOM   1978 N  N   . LYS A 1 251 ? 20.832 -2.313  33.900  1.00 12.23 ? 252 LYS A N   1 
ATOM   1979 C  CA  . LYS A 1 251 ? 21.484 -1.344  34.799  1.00 14.16 ? 252 LYS A CA  1 
ATOM   1980 C  C   . LYS A 1 251 ? 20.459 -0.796  35.784  1.00 15.08 ? 252 LYS A C   1 
ATOM   1981 O  O   . LYS A 1 251 ? 19.639 -1.545  36.307  1.00 16.61 ? 252 LYS A O   1 
ATOM   1982 C  CB  . LYS A 1 251 ? 22.276 -0.281  34.035  1.00 15.89 ? 252 LYS A CB  1 
ATOM   1983 C  CG  . LYS A 1 251 ? 23.419 -0.892  33.219  1.00 17.19 ? 252 LYS A CG  1 
ATOM   1984 C  CD  . LYS A 1 251 ? 24.284 0.123   32.510  1.00 20.00 ? 252 LYS A CD  1 
ATOM   1985 C  CE  . LYS A 1 251 ? 25.583 -0.546  32.090  1.00 22.21 ? 252 LYS A CE  1 
ATOM   1986 N  NZ  . LYS A 1 251 ? 26.454 0.392   31.348  1.00 25.18 ? 252 LYS A NZ  1 
ATOM   1987 N  N   . ASN A 1 252 ? 20.500 0.500   36.015  1.00 15.94 ? 253 ASN A N   1 
ATOM   1988 C  CA  . ASN A 1 252 ? 19.672 1.052   37.066  1.00 23.53 ? 253 ASN A CA  1 
ATOM   1989 C  C   . ASN A 1 252 ? 18.349 1.520   36.463  1.00 24.10 ? 253 ASN A C   1 
ATOM   1990 O  O   . ASN A 1 252 ? 18.135 2.754   36.450  1.00 24.32 ? 253 ASN A O   1 
ATOM   1991 C  CB  . ASN A 1 252 ? 20.383 2.216   37.771  1.00 30.08 ? 253 ASN A CB  1 
ATOM   1992 C  CG  . ASN A 1 252 ? 19.630 2.726   38.987  1.00 35.07 ? 253 ASN A CG  1 
ATOM   1993 O  OD1 . ASN A 1 252 ? 18.991 1.952   39.704  1.00 40.17 ? 253 ASN A OD1 1 
ATOM   1994 N  ND2 . ASN A 1 252 ? 19.698 4.028   39.222  1.00 41.35 ? 253 ASN A ND2 1 
ATOM   1995 N  N   . ARG A 1 253 ? 17.529 0.555   35.937  1.00 16.37 ? 254 ARG A N   1 
ATOM   1996 C  CA  . ARG A 1 253 ? 16.244 0.913   35.339  1.00 13.96 ? 254 ARG A CA  1 
ATOM   1997 C  C   . ARG A 1 253 ? 15.148 -0.067  35.768  1.00 15.50 ? 254 ARG A C   1 
ATOM   1998 O  O   . ARG A 1 253 ? 15.413 -1.251  35.885  1.00 17.41 ? 254 ARG A O   1 
ATOM   1999 C  CB  . ARG A 1 253 ? 16.302 0.953   33.795  1.00 11.91 ? 254 ARG A CB  1 
ATOM   2000 C  CG  . ARG A 1 253 ? 17.150 2.097   33.256  1.00 10.61 ? 254 ARG A CG  1 
ATOM   2001 C  CD  . ARG A 1 253 ? 17.196 2.061   31.726  1.00 10.45 ? 254 ARG A CD  1 
ATOM   2002 N  NE  . ARG A 1 253 ? 18.116 0.972   31.301  1.00 9.70  ? 254 ARG A NE  1 
ATOM   2003 C  CZ  . ARG A 1 253 ? 18.387 0.693   30.023  1.00 9.31  ? 254 ARG A CZ  1 
ATOM   2004 N  NH1 . ARG A 1 253 ? 17.749 1.363   29.071  1.00 8.24  ? 254 ARG A NH1 1 
ATOM   2005 N  NH2 . ARG A 1 253 ? 19.227 -0.298  29.712  1.00 8.17  ? 254 ARG A NH2 1 
ATOM   2006 N  N   . GLN A 1 254 ? 13.903 0.436   35.877  1.00 15.76 ? 255 GLN A N   1 
ATOM   2007 C  CA  . GLN A 1 254 ? 12.738 -0.397  36.141  1.00 19.97 ? 255 GLN A CA  1 
ATOM   2008 C  C   . GLN A 1 254 ? 11.849 -0.394  34.893  1.00 15.98 ? 255 GLN A C   1 
ATOM   2009 O  O   . GLN A 1 254 ? 11.599 0.672   34.339  1.00 18.40 ? 255 GLN A O   1 
ATOM   2010 C  CB  . GLN A 1 254 ? 11.948 0.247   37.286  1.00 28.14 ? 255 GLN A CB  1 
ATOM   2011 C  CG  . GLN A 1 254 ? 12.440 -0.213  38.645  1.00 39.18 ? 255 GLN A CG  1 
ATOM   2012 C  CD  . GLN A 1 254 ? 11.726 -1.476  39.066  1.00 49.96 ? 255 GLN A CD  1 
ATOM   2013 O  OE1 . GLN A 1 254 ? 10.517 -1.460  39.310  1.00 56.21 ? 255 GLN A OE1 1 
ATOM   2014 N  NE2 . GLN A 1 254 ? 12.478 -2.570  39.190  1.00 48.24 ? 255 GLN A NE2 1 
ATOM   2015 N  N   . ILE A 1 255 ? 11.446 -1.582  34.427  1.00 13.00 ? 256 ILE A N   1 
ATOM   2016 C  CA  . ILE A 1 255 ? 10.450 -1.666  33.370  1.00 11.62 ? 256 ILE A CA  1 
ATOM   2017 C  C   . ILE A 1 255 ? 9.079  -1.695  34.050  1.00 11.11 ? 256 ILE A C   1 
ATOM   2018 O  O   . ILE A 1 255 ? 8.892  -2.422  35.022  1.00 10.91 ? 256 ILE A O   1 
ATOM   2019 C  CB  . ILE A 1 255 ? 10.696 -2.933  32.529  1.00 11.75 ? 256 ILE A CB  1 
ATOM   2020 C  CG1 . ILE A 1 255 ? 12.085 -2.884  31.880  1.00 12.05 ? 256 ILE A CG1 1 
ATOM   2021 C  CG2 . ILE A 1 255 ? 9.585  -3.144  31.497  1.00 10.99 ? 256 ILE A CG2 1 
ATOM   2022 C  CD1 . ILE A 1 255 ? 12.403 -4.167  31.090  1.00 13.82 ? 256 ILE A CD1 1 
ATOM   2023 N  N   . LYS A 1 256 ? 8.198  -0.789  33.615  1.00 10.89 ? 257 LYS A N   1 
ATOM   2024 C  CA  . LYS A 1 256 ? 6.843  -0.725  34.138  1.00 11.37 ? 257 LYS A CA  1 
ATOM   2025 C  C   . LYS A 1 256 ? 5.870  -1.375  33.176  1.00 11.14 ? 257 LYS A C   1 
ATOM   2026 O  O   . LYS A 1 256 ? 6.045  -1.311  31.959  1.00 11.23 ? 257 LYS A O   1 
ATOM   2027 C  CB  . LYS A 1 256 ? 6.413  0.727   34.343  1.00 13.23 ? 257 LYS A CB  1 
ATOM   2028 C  CG  . LYS A 1 256 ? 7.329  1.607   35.180  1.00 17.48 ? 257 LYS A CG  1 
ATOM   2029 C  CD  . LYS A 1 256 ? 7.974  0.935   36.343  1.00 21.17 ? 257 LYS A CD  1 
ATOM   2030 N  N   . ALA A 1 257 ? 4.814  -1.972  33.720  1.00 10.50 ? 258 ALA A N   1 
ATOM   2031 C  CA  . ALA A 1 257 ? 3.791  -2.568  32.883  1.00 10.88 ? 258 ALA A CA  1 
ATOM   2032 C  C   . ALA A 1 257 ? 2.480  -1.845  33.115  1.00 11.53 ? 258 ALA A C   1 
ATOM   2033 O  O   . ALA A 1 257 ? 2.180  -1.421  34.248  1.00 12.31 ? 258 ALA A O   1 
ATOM   2034 C  CB  . ALA A 1 257 ? 3.638  -4.041  33.127  1.00 11.18 ? 258 ALA A CB  1 
ATOM   2035 N  N   . SER A 1 258 ? 1.729  -1.724  32.021  1.00 10.09 ? 259 SER A N   1 
ATOM   2036 C  CA  . SER A 1 258 ? 0.461  -1.015  32.050  1.00 12.36 ? 259 SER A CA  1 
ATOM   2037 C  C   . SER A 1 258 ? -0.639 -1.986  32.462  1.00 13.45 ? 259 SER A C   1 
ATOM   2038 O  O   . SER A 1 258 ? -1.796 -1.579  32.583  1.00 17.44 ? 259 SER A O   1 
ATOM   2039 C  CB  . SER A 1 258 ? 0.155  -0.396  30.705  1.00 11.82 ? 259 SER A CB  1 
ATOM   2040 O  OG  . SER A 1 258 ? -0.347 -1.385  29.791  1.00 12.40 ? 259 SER A OG  1 
ATOM   2041 N  N   . PHE A 1 259 ? -0.302 -3.239  32.701  1.00 14.39 ? 260 PHE A N   1 
ATOM   2042 C  CA  . PHE A 1 259 ? -1.327 -4.260  32.855  1.00 16.07 ? 260 PHE A CA  1 
ATOM   2043 C  C   . PHE A 1 259 ? -0.879 -5.279  33.886  1.00 22.32 ? 260 PHE A C   1 
ATOM   2044 O  O   . PHE A 1 259 ? 0.314  -5.399  34.148  1.00 18.17 ? 260 PHE A O   1 
ATOM   2045 C  CB  . PHE A 1 259 ? -1.571 -5.008  31.539  1.00 17.70 ? 260 PHE A CB  1 
ATOM   2046 C  CG  . PHE A 1 259 ? -0.322 -5.699  31.023  1.00 16.18 ? 260 PHE A CG  1 
ATOM   2047 C  CD1 . PHE A 1 259 ? 0.617  -4.960  30.329  1.00 15.02 ? 260 PHE A CD1 1 
ATOM   2048 C  CD2 . PHE A 1 259 ? -0.030 -7.019  31.340  1.00 17.27 ? 260 PHE A CD2 1 
ATOM   2049 C  CE1 . PHE A 1 259 ? 1.799  -5.538  29.901  1.00 16.43 ? 260 PHE A CE1 1 
ATOM   2050 C  CE2 . PHE A 1 259 ? 1.148  -7.607  30.903  1.00 18.98 ? 260 PHE A CE2 1 
ATOM   2051 C  CZ  . PHE A 1 259 ? 2.061  -6.859  30.167  1.00 17.77 ? 260 PHE A CZ  1 
ATOM   2052 N  N   . LYS A 1 260 ? -1.905 -5.988  34.409  1.00 27.47 ? 261 LYS A N   1 
ATOM   2053 C  CA  . LYS A 1 260 ? -1.943 -7.239  35.167  1.00 42.17 ? 261 LYS A CA  1 
ATOM   2054 C  C   . LYS A 1 260 ? -1.583 -7.050  36.645  1.00 51.19 ? 261 LYS A C   1 
ATOM   2055 O  O   . LYS A 1 260 ? -1.958 -7.912  37.436  1.00 57.73 ? 261 LYS A O   1 
ATOM   2056 C  CB  . LYS A 1 260 ? -1.391 -8.466  34.430  1.00 38.22 ? 261 LYS A CB  1 
ATOM   2057 C  CG  . LYS A 1 260 ? -2.380 -9.094  33.448  1.00 33.66 ? 261 LYS A CG  1 
ATOM   2058 O  OXT . LYS A 1 260 ? -0.977 -6.070  37.082  1.00 62.89 ? 261 LYS A OXT 1 
HETATM 2059 ZN ZN  . ZN  B 2 .   ? 14.413 0.059   15.293  1.00 7.24  ? 301 ZN  A ZN  1 
HETATM 2060 S  S   . DMS C 3 .   ? 22.412 -9.875  14.955  1.00 22.10 ? 302 DMS A S   1 
HETATM 2061 O  O   . DMS C 3 .   ? 23.008 -11.210 14.537  1.00 22.31 ? 302 DMS A O   1 
HETATM 2062 C  C1  . DMS C 3 .   ? 22.867 -9.713  16.666  1.00 17.28 ? 302 DMS A C1  1 
HETATM 2063 C  C2  . DMS C 3 .   ? 23.521 -8.607  14.284  1.00 19.17 ? 302 DMS A C2  1 
HETATM 2064 O  O1  . MES D 4 .   ? 13.751 -7.621  -2.639  1.00 36.07 ? 303 MES A O1  1 
HETATM 2065 C  C2  . MES D 4 .   ? 12.560 -7.300  -1.921  1.00 29.88 ? 303 MES A C2  1 
HETATM 2066 C  C3  . MES D 4 .   ? 11.516 -8.389  -1.934  1.00 29.21 ? 303 MES A C3  1 
HETATM 2067 N  N4  . MES D 4 .   ? 11.247 -8.833  -3.345  1.00 32.07 ? 303 MES A N4  1 
HETATM 2068 C  C5  . MES D 4 .   ? 12.532 -9.202  -4.036  1.00 31.61 ? 303 MES A C5  1 
HETATM 2069 C  C6  . MES D 4 .   ? 13.501 -8.043  -3.984  1.00 29.40 ? 303 MES A C6  1 
HETATM 2070 C  C7  . MES D 4 .   ? 10.196 -9.905  -3.426  1.00 35.23 ? 303 MES A C7  1 
HETATM 2071 C  C8  . MES D 4 .   ? 10.449 -10.932 -4.520  1.00 35.76 ? 303 MES A C8  1 
HETATM 2072 S  S   . DMS E 3 .   ? 31.786 1.037   14.008  1.00 42.82 ? 304 DMS A S   1 
HETATM 2073 O  O   . DMS E 3 .   ? 30.613 1.910   14.307  1.00 39.40 ? 304 DMS A O   1 
HETATM 2074 C  C1  . DMS E 3 .   ? 32.739 0.999   15.509  1.00 34.24 ? 304 DMS A C1  1 
HETATM 2075 C  C2  . DMS E 3 .   ? 31.268 -0.651  13.925  1.00 28.07 ? 304 DMS A C2  1 
HETATM 2076 C  C1  . MHK F 5 .   ? 16.569 5.826   13.955  1.00 17.42 ? 305 MHK A C1  1 
HETATM 2077 C  C11 . MHK F 5 .   ? 15.731 7.577   15.463  1.00 16.08 ? 305 MHK A C11 1 
HETATM 2078 C  C2  . MHK F 5 .   ? 15.890 6.230   15.107  1.00 16.13 ? 305 MHK A C2  1 
HETATM 2079 C  C3  . MHK F 5 .   ? 15.455 5.240   15.977  1.00 14.24 ? 305 MHK A C3  1 
HETATM 2080 C  C4  . MHK F 5 .   ? 15.760 3.906   15.626  1.00 11.63 ? 305 MHK A C4  1 
HETATM 2081 C  C5  . MHK F 5 .   ? 16.365 3.496   14.440  1.00 14.06 ? 305 MHK A C5  1 
HETATM 2082 C  C6  . MHK F 5 .   ? 16.779 4.504   13.542  1.00 15.13 ? 305 MHK A C6  1 
HETATM 2083 O  O9  . MHK F 5 .   ? 13.716 2.719   16.681  1.00 8.79  ? 305 MHK A O9  1 
HETATM 2084 S  S7  . MHK F 5 .   ? 15.226 2.626   16.707  1.00 9.69  ? 305 MHK A S7  1 
HETATM 2085 O  O8  . MHK F 5 .   ? 15.837 2.825   18.106  1.00 9.26  ? 305 MHK A O8  1 
HETATM 2086 N  N10 . MHK F 5 .   ? 15.807 1.141   16.232  1.00 8.39  ? 305 MHK A N10 1 
HETATM 2087 C  C14 . MHK F 5 .   ? 14.859 5.618   17.220  1.00 14.00 ? 305 MHK A C14 1 
HETATM 2088 C  C13 . MHK F 5 .   ? 14.635 6.975   17.597  1.00 13.72 ? 305 MHK A C13 1 
HETATM 2089 C  C12 . MHK F 5 .   ? 15.106 7.965   16.682  1.00 15.68 ? 305 MHK A C12 1 
HETATM 2090 NA NA  . NA  G 6 .   ? 3.207  20.952  6.001   1.00 20.62 ? 306 NA  A NA  1 
HETATM 2091 O  O   . HOH H 7 .   ? 22.663 14.448  22.788  1.00 27.34 ? 401 HOH A O   1 
HETATM 2092 O  O   . HOH H 7 .   ? 1.892  13.319  32.434  1.00 38.24 ? 402 HOH A O   1 
HETATM 2093 O  O   . HOH H 7 .   ? -6.951 14.000  5.313   1.00 22.89 ? 403 HOH A O   1 
HETATM 2094 O  O   . HOH H 7 .   ? 21.248 -17.577 10.690  1.00 39.72 ? 404 HOH A O   1 
HETATM 2095 O  O   . HOH H 7 .   ? -4.464 -8.790  17.805  1.00 22.19 ? 405 HOH A O   1 
HETATM 2096 O  O   . HOH H 7 .   ? 13.941 7.877   6.553   1.00 26.90 ? 406 HOH A O   1 
HETATM 2097 O  O   . HOH H 7 .   ? 5.667  -8.371  37.479  1.00 30.81 ? 407 HOH A O   1 
HETATM 2098 O  O   . HOH H 7 .   ? 32.225 -5.109  22.316  1.00 26.27 ? 408 HOH A O   1 
HETATM 2099 O  O   . HOH H 7 .   ? 26.541 -10.519 11.999  1.00 35.34 ? 409 HOH A O   1 
HETATM 2100 O  O   . HOH H 7 .   ? -4.605 -3.902  13.206  1.00 25.23 ? 410 HOH A O   1 
HETATM 2101 O  O   . HOH H 7 .   ? 8.255  -20.265 8.394   1.00 38.72 ? 411 HOH A O   1 
HETATM 2102 O  O   . HOH H 7 .   ? 16.181 4.001   37.427  1.00 34.16 ? 412 HOH A O   1 
HETATM 2103 O  O   . HOH H 7 .   ? 14.984 -2.725  -6.586  1.00 22.96 ? 413 HOH A O   1 
HETATM 2104 O  O   . HOH H 7 .   ? 6.078  21.892  17.562  1.00 26.00 ? 414 HOH A O   1 
HETATM 2105 O  O   . HOH H 7 .   ? 16.183 -10.146 32.107  1.00 20.26 ? 415 HOH A O   1 
HETATM 2106 O  O   . HOH H 7 .   ? -0.018 -5.012  -1.873  1.00 31.34 ? 416 HOH A O   1 
HETATM 2107 O  O   . HOH H 7 .   ? 2.290  -10.207 -3.315  1.00 21.95 ? 417 HOH A O   1 
HETATM 2108 O  O   . HOH H 7 .   ? 25.517 -1.549  26.410  1.00 16.06 ? 418 HOH A O   1 
HETATM 2109 O  O   . HOH H 7 .   ? -4.595 11.604  13.538  1.00 29.10 ? 419 HOH A O   1 
HETATM 2110 O  O   . HOH H 7 .   ? 5.710  21.407  13.184  1.00 26.20 ? 420 HOH A O   1 
HETATM 2111 O  O   . HOH H 7 .   ? 36.250 -4.931  11.638  1.00 34.97 ? 421 HOH A O   1 
HETATM 2112 O  O   . HOH H 7 .   ? 15.287 19.227  27.269  1.00 39.02 ? 422 HOH A O   1 
HETATM 2113 O  O   . HOH H 7 .   ? 6.829  -19.367 3.400   1.00 35.95 ? 423 HOH A O   1 
HETATM 2114 O  O   . HOH H 7 .   ? 1.325  -15.040 2.948   1.00 20.54 ? 424 HOH A O   1 
HETATM 2115 O  O   . HOH H 7 .   ? 22.705 4.727   5.055   1.00 42.45 ? 425 HOH A O   1 
HETATM 2116 O  O   . HOH H 7 .   ? 24.473 -7.005  25.881  1.00 30.84 ? 426 HOH A O   1 
HETATM 2117 O  O   . HOH H 7 .   ? -1.933 1.217   34.496  1.00 23.21 ? 427 HOH A O   1 
HETATM 2118 O  O   . HOH H 7 .   ? 6.820  -14.724 29.010  1.00 24.07 ? 428 HOH A O   1 
HETATM 2119 O  O   . HOH H 7 .   ? 18.925 -2.651  -6.831  1.00 30.07 ? 429 HOH A O   1 
HETATM 2120 O  O   . HOH H 7 .   ? 10.235 -13.345 34.080  1.00 31.54 ? 430 HOH A O   1 
HETATM 2121 O  O   . HOH H 7 .   ? 4.598  16.069  33.159  1.00 32.40 ? 431 HOH A O   1 
HETATM 2122 O  O   . HOH H 7 .   ? 19.823 -2.221  15.711  1.00 8.43  ? 432 HOH A O   1 
HETATM 2123 O  O   . HOH H 7 .   ? 7.931  -20.512 11.617  1.00 27.61 ? 433 HOH A O   1 
HETATM 2124 O  O   . HOH H 7 .   ? 8.959  12.647  5.838   1.00 29.75 ? 434 HOH A O   1 
HETATM 2125 O  O   . HOH H 7 .   ? -1.850 17.837  4.614   1.00 36.72 ? 435 HOH A O   1 
HETATM 2126 O  O   . HOH H 7 .   ? 10.354 2.915   33.923  1.00 35.68 ? 436 HOH A O   1 
HETATM 2127 O  O   . HOH H 7 .   ? -3.011 10.485  20.151  1.00 26.83 ? 437 HOH A O   1 
HETATM 2128 O  O   . HOH H 7 .   ? 20.543 16.238  16.160  1.00 26.65 ? 438 HOH A O   1 
HETATM 2129 O  O   . HOH H 7 .   ? -0.649 -12.250 18.577  1.00 27.20 ? 439 HOH A O   1 
HETATM 2130 O  O   . HOH H 7 .   ? 30.918 -2.685  -7.957  1.00 25.55 ? 440 HOH A O   1 
HETATM 2131 O  O   . HOH H 7 .   ? 4.598  -13.217 32.699  1.00 31.15 ? 441 HOH A O   1 
HETATM 2132 O  O   . HOH H 7 .   ? -6.647 8.106   21.292  1.00 39.74 ? 442 HOH A O   1 
HETATM 2133 O  O   . HOH H 7 .   ? 13.013 9.048   27.463  1.00 38.77 ? 443 HOH A O   1 
HETATM 2134 O  O   . HOH H 7 .   ? 6.476  -16.678 18.862  1.00 26.59 ? 444 HOH A O   1 
HETATM 2135 O  O   . HOH H 7 .   ? 12.456 -2.009  7.863   1.00 13.64 ? 445 HOH A O   1 
HETATM 2136 O  O   . HOH H 7 .   ? 22.972 -13.786 9.357   1.00 24.26 ? 446 HOH A O   1 
HETATM 2137 O  O   . HOH H 7 .   ? 1.692  19.119  18.999  1.00 39.21 ? 447 HOH A O   1 
HETATM 2138 O  O   . HOH H 7 .   ? 11.601 7.732   29.382  1.00 42.74 ? 448 HOH A O   1 
HETATM 2139 O  O   . HOH H 7 .   ? 8.790  18.303  8.934   1.00 32.78 ? 449 HOH A O   1 
HETATM 2140 O  O   . HOH H 7 .   ? 1.757  -18.780 5.058   1.00 22.11 ? 450 HOH A O   1 
HETATM 2141 O  O   . HOH H 7 .   ? 24.771 6.939   29.679  1.00 18.48 ? 451 HOH A O   1 
HETATM 2142 O  O   . HOH H 7 .   ? 10.348 -17.414 19.808  1.00 34.45 ? 452 HOH A O   1 
HETATM 2143 O  O   . HOH H 7 .   ? -1.687 -3.989  2.789   1.00 17.90 ? 453 HOH A O   1 
HETATM 2144 O  O   . HOH H 7 .   ? -6.434 4.576   23.514  1.00 38.90 ? 454 HOH A O   1 
HETATM 2145 O  O   . HOH H 7 .   ? 22.047 16.741  24.468  1.00 28.97 ? 455 HOH A O   1 
HETATM 2146 O  O   . HOH H 7 .   ? 21.169 2.983   34.475  1.00 24.84 ? 456 HOH A O   1 
HETATM 2147 O  O   . HOH H 7 .   ? 14.200 -13.045 31.576  1.00 18.97 ? 457 HOH A O   1 
HETATM 2148 O  O   . HOH H 7 .   ? 16.217 22.053  21.291  1.00 27.39 ? 458 HOH A O   1 
HETATM 2149 O  O   . HOH H 7 .   ? 13.127 -13.592 11.343  1.00 10.66 ? 459 HOH A O   1 
HETATM 2150 O  O   . HOH H 7 .   ? 17.558 -9.263  20.877  1.00 11.74 ? 460 HOH A O   1 
HETATM 2151 O  O   . HOH H 7 .   ? 7.028  12.386  27.786  1.00 19.94 ? 461 HOH A O   1 
HETATM 2152 O  O   . HOH H 7 .   ? 17.855 7.908   -1.785  1.00 35.20 ? 462 HOH A O   1 
HETATM 2153 O  O   . HOH H 7 .   ? 36.836 5.596   15.271  1.00 25.24 ? 463 HOH A O   1 
HETATM 2154 O  O   . HOH H 7 .   ? 1.557  19.339  6.275   1.00 21.42 ? 464 HOH A O   1 
HETATM 2155 O  O   . HOH H 7 .   ? 3.869  -14.466 21.843  1.00 26.48 ? 465 HOH A O   1 
HETATM 2156 O  O   . HOH H 7 .   ? 19.988 -15.875 17.856  1.00 29.81 ? 466 HOH A O   1 
HETATM 2157 O  O   . HOH H 7 .   ? 2.269  22.229  14.959  1.00 35.94 ? 467 HOH A O   1 
HETATM 2158 O  O   . HOH H 7 .   ? -2.061 -1.098  6.792   1.00 18.98 ? 468 HOH A O   1 
HETATM 2159 O  O   . HOH H 7 .   ? 14.338 -18.346 19.563  1.00 24.82 ? 469 HOH A O   1 
HETATM 2160 O  O   . HOH H 7 .   ? 22.475 -9.846  25.056  1.00 21.76 ? 470 HOH A O   1 
HETATM 2161 O  O   . HOH H 7 .   ? 8.625  14.535  29.244  1.00 27.42 ? 471 HOH A O   1 
HETATM 2162 O  O   . HOH H 7 .   ? 29.589 -1.979  21.019  1.00 17.04 ? 472 HOH A O   1 
HETATM 2163 O  O   . HOH H 7 .   ? 23.640 -11.281 5.175   1.00 24.26 ? 473 HOH A O   1 
HETATM 2164 O  O   . HOH H 7 .   ? 14.614 -3.316  37.418  1.00 25.82 ? 474 HOH A O   1 
HETATM 2165 O  O   . HOH H 7 .   ? 19.893 11.035  28.118  1.00 27.12 ? 475 HOH A O   1 
HETATM 2166 O  O   . HOH H 7 .   ? 4.839  17.760  23.659  1.00 22.50 ? 476 HOH A O   1 
HETATM 2167 O  O   . HOH H 7 .   ? 36.596 5.027   20.800  1.00 42.58 ? 477 HOH A O   1 
HETATM 2168 O  O   . HOH H 7 .   ? 7.481  21.945  14.954  1.00 26.98 ? 478 HOH A O   1 
HETATM 2169 O  O   . HOH H 7 .   ? 3.097  12.235  11.383  1.00 16.57 ? 479 HOH A O   1 
HETATM 2170 O  O   . HOH H 7 .   ? 10.887 15.768  8.865   1.00 30.23 ? 480 HOH A O   1 
HETATM 2171 O  O   . HOH H 7 .   ? 36.376 -0.585  14.483  1.00 20.28 ? 481 HOH A O   1 
HETATM 2172 O  O   . HOH H 7 .   ? 12.565 2.600   -6.612  1.00 26.70 ? 482 HOH A O   1 
HETATM 2173 O  O   . HOH H 7 .   ? 6.925  -2.746  -6.355  1.00 31.15 ? 483 HOH A O   1 
HETATM 2174 O  O   . HOH H 7 .   ? 10.658 -16.379 17.058  1.00 19.12 ? 484 HOH A O   1 
HETATM 2175 O  O   . HOH H 7 .   ? 2.579  -1.736  -2.566  1.00 23.90 ? 485 HOH A O   1 
HETATM 2176 O  O   . HOH H 7 .   ? 0.159  10.125  29.922  1.00 23.91 ? 486 HOH A O   1 
HETATM 2177 O  O   . HOH H 7 .   ? 10.427 10.576  25.593  1.00 12.89 ? 487 HOH A O   1 
HETATM 2178 O  O   . HOH H 7 .   ? 26.461 9.005   20.129  1.00 13.04 ? 488 HOH A O   1 
HETATM 2179 O  O   . HOH H 7 .   ? 16.528 -11.640 17.955  1.00 8.29  ? 489 HOH A O   1 
HETATM 2180 O  O   . HOH H 7 .   ? 23.415 10.027  27.786  1.00 30.41 ? 490 HOH A O   1 
HETATM 2181 O  O   . HOH H 7 .   ? -0.048 9.680   1.873   1.00 16.01 ? 491 HOH A O   1 
HETATM 2182 O  O   . HOH H 7 .   ? 34.485 2.114   24.453  1.00 21.28 ? 492 HOH A O   1 
HETATM 2183 O  O   . HOH H 7 .   ? 25.566 -4.685  7.967   1.00 20.69 ? 493 HOH A O   1 
HETATM 2184 O  O   . HOH H 7 .   ? -4.401 -1.862  31.788  1.00 35.84 ? 494 HOH A O   1 
HETATM 2185 O  O   . HOH H 7 .   ? 20.614 12.841  23.354  1.00 21.20 ? 495 HOH A O   1 
HETATM 2186 O  O   . HOH H 7 .   ? 16.828 -6.791  31.145  1.00 22.97 ? 496 HOH A O   1 
HETATM 2187 O  O   . HOH H 7 .   ? 27.916 -1.616  30.182  1.00 37.57 ? 497 HOH A O   1 
HETATM 2188 O  O   . HOH H 7 .   ? 3.180  -18.704 8.079   1.00 12.72 ? 498 HOH A O   1 
HETATM 2189 O  O   . HOH H 7 .   ? -0.664 7.602   4.680   1.00 13.16 ? 499 HOH A O   1 
HETATM 2190 O  O   . HOH H 7 .   ? -3.923 6.521   8.466   1.00 26.40 ? 500 HOH A O   1 
HETATM 2191 O  O   . HOH H 7 .   ? 24.847 -0.671  4.814   1.00 38.57 ? 501 HOH A O   1 
HETATM 2192 O  O   . HOH H 7 .   ? 16.499 -13.919 0.607   1.00 27.55 ? 502 HOH A O   1 
HETATM 2193 O  O   . HOH H 7 .   ? 18.538 -6.861  29.179  1.00 11.13 ? 503 HOH A O   1 
HETATM 2194 O  O   . HOH H 7 .   ? 22.546 -4.418  34.379  1.00 21.73 ? 504 HOH A O   1 
HETATM 2195 O  O   . HOH H 7 .   ? 13.860 -14.919 1.388   1.00 24.82 ? 505 HOH A O   1 
HETATM 2196 O  O   . HOH H 7 .   ? 21.368 0.906   -4.765  1.00 20.13 ? 506 HOH A O   1 
HETATM 2197 O  O   . HOH H 7 .   ? -5.710 -2.145  25.037  1.00 20.67 ? 507 HOH A O   1 
HETATM 2198 O  O   . HOH H 7 .   ? 32.298 3.392   25.896  1.00 22.48 ? 508 HOH A O   1 
HETATM 2199 O  O   . HOH H 7 .   ? 4.115  -6.566  20.436  1.00 8.16  ? 509 HOH A O   1 
HETATM 2200 O  O   . HOH H 7 .   ? 22.692 4.405   35.864  1.00 36.18 ? 510 HOH A O   1 
HETATM 2201 O  O   . HOH H 7 .   ? 15.821 3.136   10.540  1.00 24.58 ? 511 HOH A O   1 
HETATM 2202 O  O   . HOH H 7 .   ? -4.918 8.009   27.127  1.00 25.35 ? 512 HOH A O   1 
HETATM 2203 O  O   . HOH H 7 .   ? -3.609 13.986  6.397   1.00 26.21 ? 513 HOH A O   1 
HETATM 2204 O  O   . HOH H 7 .   ? -6.797 7.641   18.967  1.00 34.87 ? 514 HOH A O   1 
HETATM 2205 O  O   . HOH H 7 .   ? 7.581  -16.765 14.735  1.00 23.98 ? 515 HOH A O   1 
HETATM 2206 O  O   . HOH H 7 .   ? 17.486 -11.214 -2.834  1.00 29.71 ? 516 HOH A O   1 
HETATM 2207 O  O   . HOH H 7 .   ? -4.473 -5.166  33.739  1.00 39.08 ? 517 HOH A O   1 
HETATM 2208 O  O   . HOH H 7 .   ? -0.528 -5.303  23.631  1.00 12.18 ? 518 HOH A O   1 
HETATM 2209 O  O   . HOH H 7 .   ? 30.218 9.293   18.350  1.00 35.26 ? 519 HOH A O   1 
HETATM 2210 O  O   . HOH H 7 .   ? 0.638  12.717  26.561  1.00 14.80 ? 520 HOH A O   1 
HETATM 2211 O  O   . HOH H 7 .   ? 8.071  -14.984 26.481  1.00 22.90 ? 521 HOH A O   1 
HETATM 2212 O  O   . HOH H 7 .   ? 17.654 -11.383 25.257  1.00 10.74 ? 522 HOH A O   1 
HETATM 2213 O  O   . HOH H 7 .   ? 12.635 -13.386 36.850  1.00 28.12 ? 523 HOH A O   1 
HETATM 2214 O  O   . HOH H 7 .   ? 29.467 5.067   27.736  1.00 24.99 ? 524 HOH A O   1 
HETATM 2215 O  O   . HOH H 7 .   ? 4.980  -10.507 24.375  1.00 16.11 ? 525 HOH A O   1 
HETATM 2216 O  O   . HOH H 7 .   ? 23.839 -2.408  7.968   1.00 26.39 ? 526 HOH A O   1 
HETATM 2217 O  O   . HOH H 7 .   ? -4.703 -13.294 8.103   1.00 22.78 ? 527 HOH A O   1 
HETATM 2218 O  O   . HOH H 7 .   ? 1.806  11.944  8.905   1.00 15.27 ? 528 HOH A O   1 
HETATM 2219 O  O   . HOH H 7 .   ? -3.790 -5.900  9.002   1.00 15.92 ? 529 HOH A O   1 
HETATM 2220 O  O   . HOH H 7 .   ? 5.420  10.958  -2.137  1.00 27.76 ? 530 HOH A O   1 
HETATM 2221 O  O   . HOH H 7 .   ? 23.770 -12.550 -5.837  1.00 38.10 ? 531 HOH A O   1 
HETATM 2222 O  O   . HOH H 7 .   ? 18.623 -1.049  11.412  1.00 16.84 ? 532 HOH A O   1 
HETATM 2223 O  O   . HOH H 7 .   ? 2.463  -7.201  34.402  1.00 22.34 ? 533 HOH A O   1 
HETATM 2224 O  O   . HOH H 7 .   ? 17.344 -14.046 24.403  1.00 13.34 ? 534 HOH A O   1 
HETATM 2225 O  O   . HOH H 7 .   ? 34.186 -3.949  24.489  1.00 26.32 ? 535 HOH A O   1 
HETATM 2226 O  O   . HOH H 7 .   ? 24.392 -11.766 12.137  1.00 34.08 ? 536 HOH A O   1 
HETATM 2227 O  O   . HOH H 7 .   ? 18.674 6.312   7.909   1.00 32.76 ? 537 HOH A O   1 
HETATM 2228 O  O   . HOH H 7 .   ? -2.893 1.181   26.504  1.00 16.17 ? 538 HOH A O   1 
HETATM 2229 O  O   . HOH H 7 .   ? 25.374 -0.575  28.846  1.00 26.09 ? 539 HOH A O   1 
HETATM 2230 O  O   . HOH H 7 .   ? 13.767 -6.880  32.597  1.00 17.73 ? 540 HOH A O   1 
HETATM 2231 O  O   . HOH H 7 .   ? 13.086 -20.295 10.261  1.00 21.71 ? 541 HOH A O   1 
HETATM 2232 O  O   . HOH H 7 .   ? 23.683 -9.452  9.575   1.00 21.03 ? 542 HOH A O   1 
HETATM 2233 O  O   . HOH H 7 .   ? 11.042 16.829  12.171  1.00 15.90 ? 543 HOH A O   1 
HETATM 2234 O  O   . HOH H 7 .   ? 9.961  -17.497 6.953   1.00 25.90 ? 544 HOH A O   1 
HETATM 2235 O  O   . HOH H 7 .   ? 8.254  -7.106  -3.229  1.00 24.60 ? 545 HOH A O   1 
HETATM 2236 O  O   . HOH H 7 .   ? 25.943 -3.144  20.977  1.00 12.33 ? 546 HOH A O   1 
HETATM 2237 O  O   . HOH H 7 .   ? 4.800  -8.112  32.875  1.00 15.07 ? 547 HOH A O   1 
HETATM 2238 O  O   . HOH H 7 .   ? 4.072  -5.516  39.797  1.00 30.91 ? 548 HOH A O   1 
HETATM 2239 O  O   . HOH H 7 .   ? -2.568 0.997   3.938   1.00 18.60 ? 549 HOH A O   1 
HETATM 2240 O  O   . HOH H 7 .   ? 8.366  9.831   28.927  1.00 26.88 ? 550 HOH A O   1 
HETATM 2241 O  O   . HOH H 7 .   ? 13.187 -17.346 30.528  1.00 29.88 ? 551 HOH A O   1 
HETATM 2242 O  O   . HOH H 7 .   ? 29.127 -3.839  -10.522 1.00 22.14 ? 552 HOH A O   1 
HETATM 2243 O  O   . HOH H 7 .   ? 22.341 0.197   29.345  1.00 13.50 ? 553 HOH A O   1 
HETATM 2244 O  O   . HOH H 7 .   ? 36.413 2.411   15.447  1.00 34.30 ? 554 HOH A O   1 
HETATM 2245 O  O   . HOH H 7 .   ? 11.395 -6.252  33.954  1.00 20.34 ? 555 HOH A O   1 
HETATM 2246 O  O   . HOH H 7 .   ? -5.182 -5.382  30.514  1.00 33.22 ? 556 HOH A O   1 
HETATM 2247 O  O   . HOH H 7 .   ? 7.491  0.922   -6.357  1.00 37.24 ? 557 HOH A O   1 
HETATM 2248 O  O   . HOH H 7 .   ? 8.310  5.461   -6.848  1.00 31.05 ? 558 HOH A O   1 
HETATM 2249 O  O   . HOH H 7 .   ? -1.816 -9.813  14.134  1.00 17.22 ? 559 HOH A O   1 
HETATM 2250 O  O   . HOH H 7 .   ? 14.711 -17.999 23.928  1.00 31.69 ? 560 HOH A O   1 
HETATM 2251 O  O   . HOH H 7 .   ? 12.154 -4.026  35.847  1.00 18.13 ? 561 HOH A O   1 
HETATM 2252 O  O   . HOH H 7 .   ? -3.076 -15.941 6.600   1.00 33.09 ? 562 HOH A O   1 
HETATM 2253 O  O   . HOH H 7 .   ? 19.064 -10.474 22.944  1.00 13.12 ? 563 HOH A O   1 
HETATM 2254 O  O   . HOH H 7 .   ? 22.335 10.784  24.385  1.00 15.48 ? 564 HOH A O   1 
HETATM 2255 O  O   . HOH H 7 .   ? 27.067 -1.058  6.678   1.00 38.14 ? 565 HOH A O   1 
HETATM 2256 O  O   . HOH H 7 .   ? 14.471 -17.681 5.322   1.00 29.02 ? 566 HOH A O   1 
HETATM 2257 O  O   . HOH H 7 .   ? 9.074  4.886   30.821  1.00 23.50 ? 567 HOH A O   1 
HETATM 2258 O  O   . HOH H 7 .   ? 2.362  14.039  12.836  1.00 33.61 ? 568 HOH A O   1 
HETATM 2259 O  O   . HOH H 7 .   ? -1.056 -16.552 13.580  1.00 20.07 ? 569 HOH A O   1 
HETATM 2260 O  O   . HOH H 7 .   ? 6.907  16.140  27.163  1.00 29.93 ? 570 HOH A O   1 
HETATM 2261 O  O   . HOH H 7 .   ? 12.978 -17.509 21.753  1.00 20.42 ? 571 HOH A O   1 
HETATM 2262 O  O   . HOH H 7 .   ? -2.982 1.701   1.142   1.00 38.81 ? 572 HOH A O   1 
HETATM 2263 O  O   . HOH H 7 .   ? 13.949 3.387   35.277  1.00 30.67 ? 573 HOH A O   1 
HETATM 2264 O  O   . HOH H 7 .   ? 28.733 8.037   21.687  1.00 16.88 ? 574 HOH A O   1 
HETATM 2265 O  O   . HOH H 7 .   ? 16.871 5.763   10.122  1.00 21.08 ? 575 HOH A O   1 
HETATM 2266 O  O   . HOH H 7 .   ? 12.495 -18.187 26.565  1.00 29.36 ? 576 HOH A O   1 
HETATM 2267 O  O   . HOH H 7 .   ? 15.546 5.681   -5.746  1.00 27.13 ? 577 HOH A O   1 
HETATM 2268 O  O   . HOH H 7 .   ? 20.457 -6.825  32.352  1.00 23.57 ? 578 HOH A O   1 
HETATM 2269 O  O   . HOH H 7 .   ? 22.982 -2.388  -12.361 1.00 32.54 ? 579 HOH A O   1 
HETATM 2270 O  O   . HOH H 7 .   ? -3.244 1.621   31.389  1.00 35.28 ? 580 HOH A O   1 
HETATM 2271 O  O   . HOH H 7 .   ? -3.045 -0.245  28.886  1.00 25.69 ? 581 HOH A O   1 
HETATM 2272 O  O   . HOH H 7 .   ? 15.009 17.723  11.872  1.00 34.78 ? 582 HOH A O   1 
HETATM 2273 O  O   . HOH H 7 .   ? 19.672 3.621   11.408  1.00 29.56 ? 583 HOH A O   1 
HETATM 2274 O  O   . HOH H 7 .   ? -0.040 -17.715 6.427   1.00 26.06 ? 584 HOH A O   1 
HETATM 2275 O  O   . HOH H 7 .   ? 26.334 -5.324  22.353  1.00 34.54 ? 585 HOH A O   1 
HETATM 2276 O  O   . HOH H 7 .   ? 28.859 -5.537  -0.775  1.00 28.52 ? 586 HOH A O   1 
HETATM 2277 O  O   . HOH H 7 .   ? 4.009  -3.181  -5.938  1.00 37.01 ? 587 HOH A O   1 
HETATM 2278 O  O   . HOH H 7 .   ? -2.574 -11.121 11.579  1.00 28.71 ? 588 HOH A O   1 
HETATM 2279 O  O   . HOH H 7 .   ? 21.104 2.639   -6.759  1.00 28.41 ? 589 HOH A O   1 
HETATM 2280 O  O   . HOH H 7 .   ? -3.710 -7.566  1.875   1.00 29.17 ? 590 HOH A O   1 
HETATM 2281 O  O   . HOH H 7 .   ? 19.408 -11.426 27.497  1.00 20.25 ? 591 HOH A O   1 
HETATM 2282 O  O   . HOH H 7 .   ? 19.586 13.107  25.923  1.00 25.59 ? 592 HOH A O   1 
HETATM 2283 O  O   . HOH H 7 .   ? -5.325 4.136   39.362  1.00 37.93 ? 593 HOH A O   1 
HETATM 2284 O  O   . HOH H 7 .   ? 22.322 -14.242 -1.828  1.00 42.47 ? 594 HOH A O   1 
HETATM 2285 O  O   . HOH H 7 .   ? 2.857  5.563   -3.881  1.00 35.80 ? 595 HOH A O   1 
HETATM 2286 O  O   . HOH H 7 .   ? 29.747 -2.920  23.713  1.00 27.25 ? 596 HOH A O   1 
HETATM 2287 O  O   . HOH H 7 .   ? 3.796  -21.239 3.976   1.00 27.52 ? 597 HOH A O   1 
HETATM 2288 O  O   . HOH H 7 .   ? 8.324  -15.506 16.806  1.00 19.56 ? 598 HOH A O   1 
HETATM 2289 O  O   . HOH H 7 .   ? 20.962 -12.293 22.456  1.00 23.48 ? 599 HOH A O   1 
HETATM 2290 O  O   . HOH H 7 .   ? 3.405  -7.320  37.025  1.00 35.56 ? 600 HOH A O   1 
HETATM 2291 O  O   . HOH H 7 .   ? 15.231 -9.686  36.410  1.00 28.71 ? 601 HOH A O   1 
HETATM 2292 O  O   . HOH H 7 .   ? 25.792 -11.396 -5.906  1.00 37.08 ? 602 HOH A O   1 
HETATM 2293 O  O   . HOH H 7 .   ? 3.333  21.801  17.657  1.00 24.65 ? 603 HOH A O   1 
HETATM 2294 O  O   . HOH H 7 .   ? 5.950  -14.528 25.383  1.00 30.93 ? 604 HOH A O   1 
HETATM 2295 O  O   . HOH H 7 .   ? 18.015 1.756   10.568  1.00 22.64 ? 605 HOH A O   1 
HETATM 2296 O  O   . HOH H 7 .   ? 15.327 8.578   11.150  1.00 28.33 ? 606 HOH A O   1 
HETATM 2297 O  O   . HOH H 7 .   ? 23.858 -11.437 8.190   1.00 29.18 ? 607 HOH A O   1 
HETATM 2298 O  O   . HOH H 7 .   ? 12.712 -15.476 34.829  1.00 24.43 ? 608 HOH A O   1 
HETATM 2299 O  O   . HOH H 7 .   ? -2.670 -1.520  3.774   1.00 32.31 ? 609 HOH A O   1 
HETATM 2300 O  O   . HOH H 7 .   ? 4.236  -12.271 37.358  1.00 28.48 ? 610 HOH A O   1 
HETATM 2301 O  O   . HOH H 7 .   ? 18.530 -16.015 5.100   1.00 35.57 ? 611 HOH A O   1 
HETATM 2302 O  O   . HOH H 7 .   ? 18.699 -10.326 31.296  1.00 36.16 ? 612 HOH A O   1 
HETATM 2303 O  O   . HOH H 7 .   ? 22.225 5.185   2.411   1.00 40.92 ? 613 HOH A O   1 
HETATM 2304 O  O   . HOH H 7 .   ? 19.940 7.377   41.061  1.00 42.67 ? 614 HOH A O   1 
HETATM 2305 O  O   . HOH H 7 .   ? 4.261  -16.192 20.151  1.00 29.69 ? 615 HOH A O   1 
HETATM 2306 O  O   . HOH H 7 .   ? 27.542 -3.473  27.285  1.00 32.64 ? 616 HOH A O   1 
HETATM 2307 O  O   . HOH H 7 .   ? 19.172 -15.471 25.441  1.00 27.34 ? 617 HOH A O   1 
HETATM 2308 O  O   . HOH H 7 .   ? -5.996 -4.473  7.969   1.00 36.52 ? 618 HOH A O   1 
HETATM 2309 O  O   . HOH H 7 .   ? 27.289 -6.249  -10.140 1.00 41.92 ? 619 HOH A O   1 
HETATM 2310 O  O   . HOH H 7 .   ? 31.394 8.625   14.270  1.00 39.62 ? 620 HOH A O   1 
HETATM 2311 O  O   . HOH H 7 .   ? -6.900 6.810   25.378  1.00 28.13 ? 621 HOH A O   1 
HETATM 2312 O  O   . HOH H 7 .   ? 15.630 -7.786  34.835  1.00 33.96 ? 622 HOH A O   1 
HETATM 2313 O  O   . HOH H 7 .   ? 21.429 5.200   9.969   1.00 33.85 ? 623 HOH A O   1 
HETATM 2314 O  O   . HOH H 7 .   ? 12.898 9.662   8.306   1.00 37.22 ? 624 HOH A O   1 
HETATM 2315 O  O   . HOH H 7 .   ? 23.014 -12.595 20.508  1.00 39.34 ? 625 HOH A O   1 
HETATM 2316 O  O   . HOH H 7 .   ? 36.474 0.542   25.895  1.00 25.90 ? 626 HOH A O   1 
HETATM 2317 O  O   . HOH H 7 .   ? -2.874 -4.989  0.237   1.00 32.77 ? 627 HOH A O   1 
HETATM 2318 O  O   . HOH H 7 .   ? 9.616  3.100   -7.723  1.00 36.96 ? 628 HOH A O   1 
HETATM 2319 O  O   . HOH H 7 .   ? 4.197  -12.033 26.442  1.00 24.86 ? 629 HOH A O   1 
HETATM 2320 O  O   . HOH H 7 .   ? 3.329  -10.299 31.793  1.00 31.74 ? 630 HOH A O   1 
HETATM 2321 O  O   . HOH H 7 .   ? 4.896  18.906  26.215  1.00 31.62 ? 631 HOH A O   1 
HETATM 2322 O  O   . HOH H 7 .   ? 22.704 -15.595 7.160   1.00 31.25 ? 632 HOH A O   1 
HETATM 2323 O  O   . HOH H 7 .   ? 0.968  -13.575 22.609  1.00 32.13 ? 633 HOH A O   1 
HETATM 2324 O  O   . HOH H 7 .   ? 33.286 6.024   27.348  1.00 28.71 ? 634 HOH A O   1 
HETATM 2325 O  O   . HOH H 7 .   ? 25.289 -9.664  23.579  1.00 27.49 ? 635 HOH A O   1 
HETATM 2326 O  O   . HOH H 7 .   ? 20.065 -9.337  29.011  1.00 18.68 ? 636 HOH A O   1 
HETATM 2327 O  O   . HOH H 7 .   ? 23.651 -11.068 27.095  1.00 31.83 ? 637 HOH A O   1 
HETATM 2328 O  O   . HOH H 7 .   ? 20.516 -5.012  -7.475  1.00 31.67 ? 638 HOH A O   1 
HETATM 2329 O  O   . HOH H 7 .   ? 16.451 3.012   43.406  1.00 28.20 ? 639 HOH A O   1 
HETATM 2330 O  O   . HOH H 7 .   ? 16.985 -13.641 -2.295  1.00 30.97 ? 640 HOH A O   1 
HETATM 2331 O  O   . HOH H 7 .   ? 27.486 7.369   28.435  1.00 29.61 ? 641 HOH A O   1 
HETATM 2332 O  O   . HOH H 7 .   ? 24.257 4.918   0.228   1.00 41.54 ? 642 HOH A O   1 
HETATM 2333 O  O   . HOH H 7 .   ? 27.647 10.417  18.075  1.00 31.74 ? 643 HOH A O   1 
HETATM 2334 O  O   . HOH H 7 .   ? 26.513 10.950  21.938  1.00 21.97 ? 644 HOH A O   1 
HETATM 2335 O  O   . HOH H 7 .   ? 35.116 0.432   28.388  1.00 34.53 ? 645 HOH A O   1 
HETATM 2336 O  O   . HOH H 7 .   ? 19.427 9.604   14.370  1.00 37.31 ? 646 HOH A O   1 
HETATM 2337 O  O   . HOH H 7 .   ? 24.878 11.672  23.638  1.00 24.85 ? 647 HOH A O   1 
# 
