data_4QSB
# 
_entry.id   4QSB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.381 
_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   4QSB         pdb_00004qsb 10.2210/pdb4qsb/pdb 
RCSB  RCSB086450   ?            ?                   
WWPDB D_1000086450 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4QSA . unspecified 
PDB 4QSI . unspecified 
PDB 4QSJ . unspecified 
# 
_pdbx_database_status.entry_id                        4QSB 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2014-07-03 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
;Intrinsic Thermodynamics and Structure Correlation of Benzenesulfonamides with a Pyrimidine Moiety Binding to Carbonic Anhydrases I, II, VII, XII, and XIII
;
_citation.journal_abbrev            'Plos One' 
_citation.journal_volume            9 
_citation.page_first                e114106 
_citation.page_last                 e114106 
_citation.year                      2014 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25493428 
_citation.pdbx_database_id_DOI      10.1371/journal.pone.0114106 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kisonaite, M.'     1  ? 
primary 'Zubriene, A.'      2  ? 
primary 'Capkauskaite, E.'  3  ? 
primary 'Smirnov, A.'       4  ? 
primary 'Smirnoviene, J.'   5  ? 
primary 'Kairys, V.'        6  ? 
primary 'Michailoviene, V.' 7  ? 
primary 'Manakova, E.'      8  ? 
primary 'Grazulis, S.'      9  ? 
primary 'Matulis, D.'       10 ? 
# 
_cell.entry_id           4QSB 
_cell.length_a           42.247 
_cell.length_b           40.984 
_cell.length_c           71.480 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.040 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              2 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4QSB 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                             29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                         65.409    1   ?       ? ? ? 
3 non-polymer syn '3-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' 339.390   1   ?       ? ? ? 
4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                             195.237   1   ?       ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                               78.133    2   ?       ? ? ? 
6 water       nat water                                                                              18.015    215 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4QSB 
_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 
# 
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  
EWY non-polymer         . '3-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' ? 'C13 H13 N3 O4 S2' 
339.390 
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 
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  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4QSB 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   39.99 
_exptl_crystal.density_Matthews      2.05 
_exptl_crystal.pdbx_mosaicity        0.62 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    '2.2M sodium malonate pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2011-11-20 
_diffrn_detector.details                'Mirror Bent, vertically focussing' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8123 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.pdbx_wavelength_list        0.8123 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
# 
_reflns.entry_id                     4QSB 
_reflns.d_resolution_high            1.373 
_reflns.d_resolution_low             18.755 
_reflns.number_all                   ? 
_reflns.number_obs                   46809 
_reflns.pdbx_Rmerge_I_obs            0.099 
_reflns.pdbx_netI_over_sigmaI        16.800 
_reflns.pdbx_Rsym_value              0.099 
_reflns.pdbx_redundancy              5.000 
_reflns.percent_possible_obs         99.700 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        13.770 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.40 1.48  ? 33936 ? ? 0.390 1.6 0.390 ? 5.00 ? 2.50  ? 6805 ? ? 0.495 ? 99.90  0.50 0.22 1  1 
1.48 1.57  ? 32746 ? ? 0.302 2.1 0.302 ? 5.10 ? 3.90  ? 6452 ? ? 0.375 ? 100.00 0.38 0.16 2  1 
1.57 1.67  ? 30743 ? ? 0.226 2.7 0.226 ? 5.10 ? 6.00  ? 6044 ? ? 0.285 ? 100.00 0.28 0.12 3  1 
1.67 1.81  ? 28790 ? ? 0.171 3.5 0.171 ? 5.10 ? 9.50  ? 5653 ? ? 0.215 ? 100.00 0.22 0.09 4  1 
1.81 1.98  ? 26385 ? ? 0.120 5.1 0.120 ? 5.10 ? 16.80 ? 5211 ? ? 0.154 ? 100.00 0.15 0.07 5  1 
1.98 2.21  ? 23698 ? ? 0.096 6.4 0.096 ? 5.00 ? 24.60 ? 4730 ? ? 0.122 ? 100.00 0.12 0.05 6  1 
2.21 2.56  ? 20824 ? ? 0.083 7.3 0.083 ? 4.90 ? 30.50 ? 4210 ? ? 0.107 ? 100.00 0.11 0.05 7  1 
2.56 3.13  ? 17208 ? ? 0.077 7.7 0.077 ? 4.90 ? 38.00 ? 3524 ? ? 0.099 ? 100.00 0.10 0.05 8  1 
3.13 4.43  ? 12582 ? ? 0.075 7.6 0.075 ? 4.60 ? 45.30 ? 2747 ? ? 0.098 ? 99.30  0.10 0.05 9  1 
4.43 18.75 ? 5635  ? ? 0.075 7.6 0.075 ? 3.90 ? 43.30 ? 1433 ? ? 0.099 ? 91.80  0.10 0.05 10 1 
# 
_refine.entry_id                                 4QSB 
_refine.ls_d_res_high                            1.400 
_refine.ls_d_res_low                             18.320 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.610 
_refine.ls_number_reflns_obs                     46792 
_refine.ls_number_reflns_all                     46792 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES' 
_refine.ls_R_factor_all                          0.192 
_refine.ls_R_factor_obs                          0.192 
_refine.ls_R_factor_R_work                       0.188 
_refine.ls_wR_factor_R_work                      0.182 
_refine.ls_R_factor_R_free                       0.220 
_refine.ls_wR_factor_R_free                      0.211 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  4709 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               16.535 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.020 
_refine.aniso_B[2][2]                            -1.090 
_refine.aniso_B[3][3]                            0.840 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.550 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_refine.overall_SU_R_Cruickshank_DPI             0.074 
_refine.overall_SU_R_free                        0.076 
_refine.pdbx_overall_ESU_R                       0.074 
_refine.pdbx_overall_ESU_R_Free                  0.076 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.870 
_refine.B_iso_max                                68.25 
_refine.B_iso_min                                5.47 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      3HLJ 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.number_atoms_solvent             215 
_refine_hist.number_atoms_total               2303 
_refine_hist.d_res_high                       1.400 
_refine_hist.d_res_low                        18.320 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       2224 0.025  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3024 2.392  1.975  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 266  7.119  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 101  38.121 24.752 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 362  14.146 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 7    23.786 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         311  0.166  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1723 0.014  0.021  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.400 
_refine_ls_shell.d_res_low                        1.436 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               99.910 
_refine_ls_shell.number_reflns_R_work             3057 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.321 
_refine_ls_shell.R_factor_R_free                  0.354 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             331 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                3388 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  4QSB 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 3-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)thio]acetyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4QSB 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  GLY A 12  ? GLU A 14  ? GLY A 12  GLU A 14  5 ? 3 
HELX_P HELX_P2  2  HIS A 15  ? PHE A 20  ? HIS A 15  PHE A 20  1 ? 6 
HELX_P HELX_P3  3  PRO A 21  ? GLY A 25  ? PRO A 21  GLY A 25  5 ? 5 
HELX_P HELX_P4  4  LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P5  5  ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P6  6  LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P7  7  LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P8  8  ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P9  9  ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P10 10 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.008 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C EWY . N10 B ? A ZN  301 A EWY 302 1_555 ? ? ? ? ? ? ? 1.958 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C EWY . N10 A ? A ZN  301 A EWY 302 1_555 ? ? ? ? ? ? ? 1.975 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 2.12 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 7.34 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 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 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 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 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 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 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O ILE A 91  ? O ILE A 91  N PHE A 70  ? N PHE A 70  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 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 EWY 302 ? 16 'BINDING SITE FOR RESIDUE EWY A 302' 
AC3 Software A MES 303 ? 5  'BINDING SITE FOR RESIDUE MES A 303' 
AC4 Software A DMS 304 ? 2  'BINDING SITE FOR RESIDUE DMS A 304' 
AC5 Software A DMS 305 ? 8  'BINDING SITE FOR RESIDUE DMS A 305' 
# 
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  EWY C .   ? EWY A 302 . ? 1_555 ? 
5  AC2 16 ASN A 62  ? ASN A 62  . ? 1_555 ? 
6  AC2 16 ALA A 65  ? ALA A 65  . ? 1_555 ? 
7  AC2 16 ASN A 67  ? ASN A 67  . ? 1_555 ? 
8  AC2 16 GLN A 92  ? GLN A 92  . ? 1_555 ? 
9  AC2 16 HIS A 94  ? HIS A 94  . ? 1_555 ? 
10 AC2 16 HIS A 96  ? HIS A 96  . ? 1_555 ? 
11 AC2 16 HIS A 119 ? HIS A 119 . ? 1_555 ? 
12 AC2 16 VAL A 121 ? VAL A 121 . ? 1_555 ? 
13 AC2 16 PHE A 130 ? PHE A 131 . ? 1_555 ? 
14 AC2 16 LEU A 197 ? LEU A 198 . ? 1_555 ? 
15 AC2 16 THR A 198 ? THR A 199 . ? 1_555 ? 
16 AC2 16 THR A 199 ? THR A 200 . ? 1_555 ? 
17 AC2 16 PRO A 200 ? PRO A 201 . ? 1_555 ? 
18 AC2 16 TRP A 208 ? TRP A 209 . ? 1_555 ? 
19 AC2 16 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
20 AC2 16 HOH G .   ? HOH A 552 . ? 1_555 ? 
21 AC3 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
22 AC3 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
23 AC3 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
24 AC3 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
25 AC3 5  HOH G .   ? HOH A 579 . ? 1_555 ? 
26 AC4 2  ASP A 242 ? ASP A 243 . ? 1_555 ? 
27 AC4 2  TRP A 244 ? TRP A 245 . ? 1_555 ? 
28 AC5 8  HIS A 4   ? HIS A 4   . ? 1_555 ? 
29 AC5 8  TRP A 5   ? TRP A 5   . ? 1_555 ? 
30 AC5 8  ASN A 11  ? ASN A 11  . ? 1_555 ? 
31 AC5 8  HIS A 15  ? HIS A 15  . ? 1_555 ? 
32 AC5 8  TRP A 16  ? TRP A 16  . ? 1_555 ? 
33 AC5 8  ASP A 19  ? ASP A 19  . ? 1_555 ? 
34 AC5 8  HOH G .   ? HOH A 532 . ? 1_555 ? 
35 AC5 8  HOH G .   ? HOH A 541 . ? 1_655 ? 
# 
_atom_sites.entry_id                    4QSB 
_atom_sites.fract_transf_matrix[1][1]   0.023670 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005919 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024400 
_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]   0.014421 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   A HIS A 1 4   ? 9.329   1.330   8.147   0.50  21.97 ? 4   HIS A N   1 
ATOM   2    N  N   B HIS A 1 4   ? 9.925   1.400   9.085   0.50  23.00 ? 4   HIS A N   1 
ATOM   3    C  CA  A HIS A 1 4   ? 9.772   -0.074  8.166   0.50  21.53 ? 4   HIS A CA  1 
ATOM   4    C  CA  B HIS A 1 4   ? 10.626  0.083   9.211   0.50  20.38 ? 4   HIS A CA  1 
ATOM   5    C  C   A HIS A 1 4   ? 9.195   -0.967  9.252   0.50  18.04 ? 4   HIS A C   1 
ATOM   6    C  C   B HIS A 1 4   ? 9.680   -0.952  9.745   0.50  18.51 ? 4   HIS A C   1 
ATOM   7    O  O   A HIS A 1 4   ? 9.324   -2.143  9.061   0.50  20.18 ? 4   HIS A O   1 
ATOM   8    O  O   B HIS A 1 4   ? 9.866   -2.135  9.580   0.50  19.19 ? 4   HIS A O   1 
ATOM   9    C  CB  A HIS A 1 4   ? 11.315  -0.277  8.174   0.50  22.06 ? 4   HIS A CB  1 
ATOM   10   C  CB  B HIS A 1 4   ? 11.913  0.237   10.067  0.50  22.79 ? 4   HIS A CB  1 
ATOM   11   C  CG  A HIS A 1 4   ? 12.049  0.030   6.851   0.50  25.58 ? 4   HIS A CG  1 
ATOM   12   C  CG  B HIS A 1 4   ? 12.825  -0.979  10.108  0.50  22.80 ? 4   HIS A CG  1 
ATOM   13   N  ND1 A HIS A 1 4   ? 13.401  -0.242  6.675   0.50  25.00 ? 4   HIS A ND1 1 
ATOM   14   N  ND1 B HIS A 1 4   ? 13.655  -1.301  9.102   0.50  25.84 ? 4   HIS A ND1 1 
ATOM   15   C  CD2 A HIS A 1 4   ? 11.611  0.608   5.652   0.50  26.05 ? 4   HIS A CD2 1 
ATOM   16   C  CD2 B HIS A 1 4   ? 13.089  -1.899  11.137  0.50  22.46 ? 4   HIS A CD2 1 
ATOM   17   C  CE1 A HIS A 1 4   ? 13.765  0.138   5.436   0.50  27.14 ? 4   HIS A CE1 1 
ATOM   18   C  CE1 B HIS A 1 4   ? 14.370  -2.412  9.438   0.50  21.82 ? 4   HIS A CE1 1 
ATOM   19   N  NE2 A HIS A 1 4   ? 12.683  0.672   4.820   0.50  28.67 ? 4   HIS A NE2 1 
ATOM   20   N  NE2 B HIS A 1 4   ? 14.033  -2.766  10.686  0.50  22.46 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.627   -0.485  10.384  1.00  19.32 ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 7.840   -1.436  11.243  1.00  16.44 ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 6.825   -2.185  10.453  1.00  15.56 ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.279   -1.685  9.464   1.00  16.50 ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.219   -0.721  12.443  1.00  15.54 ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 6.039   0.126   12.088  1.00  14.86 ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 5.984   1.493   11.750  1.00  15.54 ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.592   -0.359  12.008  1.00  13.03 ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.636   1.890   11.521  1.00  15.72 ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.771   0.791   11.640  1.00  13.79 ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 3.987   -1.569  12.278  1.00  12.26 ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.367   0.714   11.509  1.00  14.74 ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.553   -1.672  12.072  1.00  11.87 ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 1.774   -0.522  11.769  1.00  12.84 ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.613   -3.425  10.925  1.00  14.65 ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.518   -4.199  10.310  1.00  14.59 ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.197   -5.368  11.220  1.00  12.74 ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.228   -5.271  12.447  1.00  13.63 ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 4.884   -6.482  10.598  1.00  15.46 ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 4.546   -7.700  11.363  1.00  16.12 ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 5.351   -8.927  11.031  1.00  22.19 ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 4.933   -10.058 11.306  1.00  24.64 ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 3.055   -8.016  11.194  1.00  13.60 ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 2.128   -6.947  11.730  1.00  12.33 ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 1.717   -6.961  13.055  1.00  12.05 ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 1.661   -5.927  10.910  1.00  11.98 ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 0.869   -5.990  13.552  1.00  11.19 ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 0.812   -4.950  11.398  1.00  11.25 ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 0.420   -4.987  12.720  1.00  11.36 ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? -0.425  -4.019  13.214  1.00  10.68 ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 6.526   -8.720  10.434  1.00  23.32 ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 7.417   -9.875  10.083  1.00  23.81 ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 8.331   -10.288 11.215  1.00  24.04 ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 8.354   -9.749  12.324  1.00  27.78 ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 9.233   -11.234 10.893  1.00  33.25 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 10.230  -11.757 11.852  1.00  33.84 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 11.242  -10.717 12.282  1.00  31.30 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 11.753  -10.697 13.440  1.00  31.18 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 10.980  -12.939 11.198  1.00  45.29 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 11.809  -13.786 12.172  1.00  57.11 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 10.952  -14.849 12.882  1.00  67.12 ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 11.808  -15.879 13.630  1.00  68.25 ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 10.997  -16.985 14.212  1.00  63.86 ? 9   LYS A NZ  1 
ATOM   64   N  N   . HIS A 1 10  ? 11.505  -9.815  11.346  1.00  27.65 ? 10  HIS A N   1 
ATOM   65   C  CA  . HIS A 1 10  ? 12.525  -8.854  11.579  1.00  24.92 ? 10  HIS A CA  1 
ATOM   66   C  C   . HIS A 1 10  ? 12.070  -7.442  11.940  1.00  23.32 ? 10  HIS A C   1 
ATOM   67   O  O   . HIS A 1 10  ? 12.869  -6.645  12.448  1.00  22.06 ? 10  HIS A O   1 
ATOM   68   C  CB  . HIS A 1 10  ? 13.579  -8.890  10.454  1.00  26.69 ? 10  HIS A CB  1 
ATOM   69   C  CG  . HIS A 1 10  ? 14.397  -10.177 10.466  1.00  25.97 ? 10  HIS A CG  1 
ATOM   70   N  ND1 . HIS A 1 10  ? 15.359  -10.428 11.399  1.00  33.91 ? 10  HIS A ND1 1 
ATOM   71   C  CD2 . HIS A 1 10  ? 14.344  -11.275 9.643   1.00  31.00 ? 10  HIS A CD2 1 
ATOM   72   C  CE1 . HIS A 1 10  ? 15.883  -11.637 11.171  1.00  31.20 ? 10  HIS A CE1 1 
ATOM   73   N  NE2 . HIS A 1 10  ? 15.250  -12.160 10.093  1.00  29.36 ? 10  HIS A NE2 1 
ATOM   74   N  N   . ASN A 1 11  ? 10.737  -7.170  11.824  1.00  19.09 ? 11  ASN A N   1 
ATOM   75   C  CA  . ASN A 1 11  ? 10.258  -5.810  12.097  1.00  18.24 ? 11  ASN A CA  1 
ATOM   76   C  C   . ASN A 1 11  ? 8.905   -5.841  12.780  1.00  17.72 ? 11  ASN A C   1 
ATOM   77   O  O   . ASN A 1 11  ? 8.237   -4.830  12.812  1.00  16.09 ? 11  ASN A O   1 
ATOM   78   C  CB  . ASN A 1 11  ? 10.058  -5.063  10.806  1.00  17.36 ? 11  ASN A CB  1 
ATOM   79   C  CG  . ASN A 1 11  ? 8.995   -5.685  9.918   1.00  16.96 ? 11  ASN A CG  1 
ATOM   80   O  OD1 . ASN A 1 11  ? 8.532   -6.774  10.213  1.00  19.60 ? 11  ASN A OD1 1 
ATOM   81   N  ND2 . ASN A 1 11  ? 8.659   -5.040  8.824   1.00  18.84 ? 11  ASN A ND2 1 
ATOM   82   N  N   . GLY A 1 12  ? 8.593   -6.998  13.345  1.00  15.29 ? 12  GLY A N   1 
ATOM   83   C  CA  . GLY A 1 12  ? 7.263   -7.134  13.965  1.00  14.92 ? 12  GLY A CA  1 
ATOM   84   C  C   . GLY A 1 12  ? 7.253   -6.607  15.396  1.00  15.74 ? 12  GLY A C   1 
ATOM   85   O  O   . GLY A 1 12  ? 8.154   -5.926  15.877  1.00  15.06 ? 12  GLY A O   1 
ATOM   86   N  N   . PRO A 1 13  ? 6.149   -6.918  16.113  1.00  13.60 ? 13  PRO A N   1 
ATOM   87   C  CA  . PRO A 1 13  ? 5.924   -6.364  17.432  1.00  14.52 ? 13  PRO A CA  1 
ATOM   88   C  C   . PRO A 1 13  ? 7.031   -6.356  18.433  1.00  13.07 ? 13  PRO A C   1 
ATOM   89   O  O   . PRO A 1 13  ? 7.211   -5.366  19.169  1.00  14.13 ? 13  PRO A O   1 
ATOM   90   C  CB  . PRO A 1 13  ? 4.609   -7.093  17.918  1.00  13.40 ? 13  PRO A CB  1 
ATOM   91   C  CG  . PRO A 1 13  ? 3.903   -7.377  16.690  1.00  13.70 ? 13  PRO A CG  1 
ATOM   92   C  CD  . PRO A 1 13  ? 4.957   -7.695  15.656  1.00  13.09 ? 13  PRO A CD  1 
ATOM   93   N  N   . GLU A 1 14  ? 7.844   -7.403  18.433  1.00  14.36 ? 14  GLU A N   1 
ATOM   94   C  CA  . GLU A 1 14  ? 8.903   -7.444  19.438  1.00  15.70 ? 14  GLU A CA  1 
ATOM   95   C  C   . GLU A 1 14  ? 10.085  -6.461  19.120  1.00  14.25 ? 14  GLU A C   1 
ATOM   96   O  O   . GLU A 1 14  ? 10.929  -6.302  19.984  1.00  16.25 ? 14  GLU A O   1 
ATOM   97   C  CB  . GLU A 1 14  ? 9.421   -8.885  19.521  1.00  18.60 ? 14  GLU A CB  1 
ATOM   98   C  CG  . GLU A 1 14  ? 10.070  -9.464  18.219  1.00  22.76 ? 14  GLU A CG  1 
ATOM   99   C  CD  . GLU A 1 14  ? 9.227   -9.985  16.999  1.00  30.61 ? 14  GLU A CD  1 
ATOM   100  O  OE1 . GLU A 1 14  ? 8.008   -9.672  16.801  1.00  24.16 ? 14  GLU A OE1 1 
ATOM   101  O  OE2 . GLU A 1 14  ? 9.862   -10.706 16.139  1.00  29.99 ? 14  GLU A OE2 1 
ATOM   102  N  N   . HIS A 1 15  ? 10.098  -5.898  17.895  1.00  13.87 ? 15  HIS A N   1 
ATOM   103  C  CA  . HIS A 1 15  ? 11.086  -4.888  17.459  1.00  13.11 ? 15  HIS A CA  1 
ATOM   104  C  C   . HIS A 1 15  ? 10.672  -3.464  17.662  1.00  12.25 ? 15  HIS A C   1 
ATOM   105  O  O   . HIS A 1 15  ? 11.451  -2.558  17.658  1.00  14.36 ? 15  HIS A O   1 
ATOM   106  C  CB  . HIS A 1 15  ? 11.398  -5.117  15.987  1.00  14.72 ? 15  HIS A CB  1 
ATOM   107  C  CG  . HIS A 1 15  ? 12.096  -6.421  15.772  1.00  17.26 ? 15  HIS A CG  1 
ATOM   108  N  ND1 . HIS A 1 15  ? 13.457  -6.567  15.976  1.00  20.91 ? 15  HIS A ND1 1 
ATOM   109  C  CD2 . HIS A 1 15  ? 11.604  -7.654  15.405  1.00  18.10 ? 15  HIS A CD2 1 
ATOM   110  C  CE1 . HIS A 1 15  ? 13.766  -7.881  15.767  1.00  19.52 ? 15  HIS A CE1 1 
ATOM   111  N  NE2 . HIS A 1 15  ? 12.683  -8.533  15.401  1.00  21.91 ? 15  HIS A NE2 1 
ATOM   112  N  N   . TRP A 1 16  ? 9.346   -3.235  17.809  1.00  11.58 ? 16  TRP A N   1 
ATOM   113  C  CA  . TRP A 1 16  ? 8.838   -1.876  17.806  1.00  12.07 ? 16  TRP A CA  1 
ATOM   114  C  C   . TRP A 1 16  ? 9.422   -0.953  18.834  1.00  10.90 ? 16  TRP A C   1 
ATOM   115  O  O   . TRP A 1 16  ? 9.544   0.245   18.525  1.00  11.28 ? 16  TRP A O   1 
ATOM   116  C  CB  . TRP A 1 16  ? 7.270   -1.913  17.969  1.00  9.78  ? 16  TRP A CB  1 
ATOM   117  C  CG  . TRP A 1 16  ? 6.617   -2.572  16.769  1.00  10.97 ? 16  TRP A CG  1 
ATOM   118  C  CD1 . TRP A 1 16  ? 7.110   -2.980  15.526  1.00  10.25 ? 16  TRP A CD1 1 
ATOM   119  C  CD2 . TRP A 1 16  ? 5.190   -2.913  16.723  1.00  9.53  ? 16  TRP A CD2 1 
ATOM   120  N  NE1 . TRP A 1 16  ? 6.136   -3.539  14.746  1.00  11.42 ? 16  TRP A NE1 1 
ATOM   121  C  CE2 . TRP A 1 16  ? 4.922   -3.439  15.406  1.00  10.35 ? 16  TRP A CE2 1 
ATOM   122  C  CE3 . TRP A 1 16  ? 4.120   -2.725  17.614  1.00  10.90 ? 16  TRP A CE3 1 
ATOM   123  C  CZ2 . TRP A 1 16  ? 3.652   -3.886  15.046  1.00  10.21 ? 16  TRP A CZ2 1 
ATOM   124  C  CZ3 . TRP A 1 16  ? 2.881   -3.140  17.223  1.00  10.15 ? 16  TRP A CZ3 1 
ATOM   125  C  CH2 . TRP A 1 16  ? 2.621   -3.666  15.980  1.00  11.32 ? 16  TRP A CH2 1 
ATOM   126  N  N   . HIS A 1 17  ? 9.792   -1.445  20.010  1.00  12.26 ? 17  HIS A N   1 
ATOM   127  C  CA  . HIS A 1 17  ? 10.323  -0.576  21.045  1.00  12.27 ? 17  HIS A CA  1 
ATOM   128  C  C   . HIS A 1 17  ? 11.625  0.214   20.689  1.00  12.35 ? 17  HIS A C   1 
ATOM   129  O  O   . HIS A 1 17  ? 11.807  1.262   21.238  1.00  13.00 ? 17  HIS A O   1 
ATOM   130  C  CB  . HIS A 1 17  ? 10.562  -1.316  22.323  1.00  12.74 ? 17  HIS A CB  1 
ATOM   131  C  CG  . HIS A 1 17  ? 11.760  -2.234  22.227  1.00  13.46 ? 17  HIS A CG  1 
ATOM   132  N  ND1 . HIS A 1 17  ? 12.993  -1.829  22.718  1.00  17.07 ? 17  HIS A ND1 1 
ATOM   133  C  CD2 . HIS A 1 17  ? 11.930  -3.411  21.611  1.00  14.29 ? 17  HIS A CD2 1 
ATOM   134  C  CE1 . HIS A 1 17  ? 13.887  -2.787  22.432  1.00  15.36 ? 17  HIS A CE1 1 
ATOM   135  N  NE2 . HIS A 1 17  ? 13.294  -3.741  21.757  1.00  17.15 ? 17  HIS A NE2 1 
ATOM   136  N  N   . LYS A 1 18  ? 12.306  -0.294  19.654  1.00  14.91 ? 18  LYS A N   1 
ATOM   137  C  CA  . LYS A 1 18  ? 13.589  0.352   19.317  1.00  14.73 ? 18  LYS A CA  1 
ATOM   138  C  C   . LYS A 1 18  ? 13.256  1.645   18.546  1.00  17.04 ? 18  LYS A C   1 
ATOM   139  O  O   . LYS A 1 18  ? 13.943  2.647   18.720  1.00  20.15 ? 18  LYS A O   1 
ATOM   140  C  CB  . LYS A 1 18  ? 14.386  -0.552  18.409  1.00  17.24 ? 18  LYS A CB  1 
ATOM   141  C  CG  . LYS A 1 18  ? 14.887  -1.772  19.127  1.00  18.14 ? 18  LYS A CG  1 
ATOM   142  C  CD  . LYS A 1 18  ? 15.657  -2.670  18.167  1.00  18.79 ? 18  LYS A CD  1 
ATOM   143  C  CE  . LYS A 1 18  ? 14.698  -3.692  17.532  1.00  18.89 ? 18  LYS A CE  1 
ATOM   144  N  NZ  . LYS A 1 18  ? 15.322  -4.581  16.468  1.00  16.60 ? 18  LYS A NZ  1 
ATOM   145  N  N   . ASP A 1 19  ? 12.175  1.738   17.744  1.00  16.27 ? 19  ASP A N   1 
ATOM   146  C  CA  . ASP A 1 19  ? 11.767  3.072   17.254  1.00  16.55 ? 19  ASP A CA  1 
ATOM   147  C  C   . ASP A 1 19  ? 10.739  3.819   18.071  1.00  15.24 ? 19  ASP A C   1 
ATOM   148  O  O   . ASP A 1 19  ? 10.619  5.029   17.956  1.00  16.34 ? 19  ASP A O   1 
ATOM   149  C  CB  . ASP A 1 19  ? 11.290  3.027   15.815  1.00  17.37 ? 19  ASP A CB  1 
ATOM   150  C  CG  . ASP A 1 19  ? 12.435  2.702   14.878  1.00  23.11 ? 19  ASP A CG  1 
ATOM   151  O  OD1 . ASP A 1 19  ? 13.234  3.596   14.643  1.00  26.82 ? 19  ASP A OD1 1 
ATOM   152  O  OD2 . ASP A 1 19  ? 12.585  1.519   14.552  1.00  30.55 ? 19  ASP A OD2 1 
ATOM   153  N  N   . PHE A 1 20  ? 10.007  3.087   18.939  1.00  14.04 ? 20  PHE A N   1 
ATOM   154  C  CA  . PHE A 1 20  ? 8.853   3.682   19.596  1.00  13.77 ? 20  PHE A CA  1 
ATOM   155  C  C   . PHE A 1 20  ? 8.949   3.163   21.017  1.00  12.57 ? 20  PHE A C   1 
ATOM   156  O  O   . PHE A 1 20  ? 8.291   2.161   21.418  1.00  12.96 ? 20  PHE A O   1 
ATOM   157  C  CB  . PHE A 1 20  ? 7.514   3.207   18.931  1.00  13.67 ? 20  PHE A CB  1 
ATOM   158  C  CG  . PHE A 1 20  ? 7.440   3.565   17.540  1.00  12.43 ? 20  PHE A CG  1 
ATOM   159  C  CD1 . PHE A 1 20  ? 7.139   4.878   17.180  1.00  14.72 ? 20  PHE A CD1 1 
ATOM   160  C  CD2 . PHE A 1 20  ? 7.752   2.664   16.584  1.00  14.95 ? 20  PHE A CD2 1 
ATOM   161  C  CE1 . PHE A 1 20  ? 7.118   5.239   15.808  1.00  13.36 ? 20  PHE A CE1 1 
ATOM   162  C  CE2 . PHE A 1 20  ? 7.786   2.998   15.255  1.00  13.55 ? 20  PHE A CE2 1 
ATOM   163  C  CZ  . PHE A 1 20  ? 7.458   4.307   14.858  1.00  14.14 ? 20  PHE A CZ  1 
ATOM   164  N  N   . PRO A 1 21  ? 9.786   3.786   21.880  1.00  13.79 ? 21  PRO A N   1 
ATOM   165  C  CA  . PRO A 1 21  ? 10.071  3.269   23.224  1.00  13.35 ? 21  PRO A CA  1 
ATOM   166  C  C   . PRO A 1 21  ? 8.832   3.149   24.123  1.00  12.77 ? 21  PRO A C   1 
ATOM   167  O  O   . PRO A 1 21  ? 8.864   2.426   25.067  1.00  14.33 ? 21  PRO A O   1 
ATOM   168  C  CB  . PRO A 1 21  ? 11.103  4.297   23.815  1.00  16.05 ? 21  PRO A CB  1 
ATOM   169  C  CG  . PRO A 1 21  ? 11.745  4.858   22.582  1.00  20.12 ? 21  PRO A CG  1 
ATOM   170  C  CD  . PRO A 1 21  ? 10.731  4.852   21.465  1.00  16.44 ? 21  PRO A CD  1 
ATOM   171  N  N   A ILE A 1 22  ? 7.776   3.904   23.825  0.50  12.65 ? 22  ILE A N   1 
ATOM   172  N  N   B ILE A 1 22  ? 7.801   3.923   23.734  0.50  11.81 ? 22  ILE A N   1 
ATOM   173  C  CA  A ILE A 1 22  ? 6.513   3.768   24.612  0.50  12.45 ? 22  ILE A CA  1 
ATOM   174  C  CA  B ILE A 1 22  ? 6.508   3.878   24.440  0.50  11.63 ? 22  ILE A CA  1 
ATOM   175  C  C   A ILE A 1 22  ? 5.960   2.348   24.457  0.50  12.52 ? 22  ILE A C   1 
ATOM   176  C  C   B ILE A 1 22  ? 5.905   2.513   24.283  0.50  11.37 ? 22  ILE A C   1 
ATOM   177  O  O   A ILE A 1 22  ? 5.124   1.875   25.279  0.50  10.79 ? 22  ILE A O   1 
ATOM   178  O  O   B ILE A 1 22  ? 4.995   2.248   24.953  0.50  9.10  ? 22  ILE A O   1 
ATOM   179  C  CB  A ILE A 1 22  ? 5.513   4.800   24.114  0.50  11.88 ? 22  ILE A CB  1 
ATOM   180  C  CB  B ILE A 1 22  ? 5.572   5.026   24.022  0.50  10.71 ? 22  ILE A CB  1 
ATOM   181  C  CG1 A ILE A 1 22  ? 4.422   5.066   25.165  0.50  14.08 ? 22  ILE A CG1 1 
ATOM   182  C  CG1 B ILE A 1 22  ? 4.469   5.242   25.056  0.50  11.84 ? 22  ILE A CG1 1 
ATOM   183  C  CG2 A ILE A 1 22  ? 4.961   4.328   22.777  0.50  12.09 ? 22  ILE A CG2 1 
ATOM   184  C  CG2 B ILE A 1 22  ? 4.939   4.767   22.658  0.50  11.84 ? 22  ILE A CG2 1 
ATOM   185  C  CD1 A ILE A 1 22  ? 4.907   5.859   26.365  0.50  15.37 ? 22  ILE A CD1 1 
ATOM   186  C  CD1 B ILE A 1 22  ? 3.531   6.338   24.671  0.50  11.41 ? 22  ILE A CD1 1 
ATOM   187  N  N   . ALA A 1 23  ? 6.443   1.612   23.455  1.00  11.92 ? 23  ALA A N   1 
ATOM   188  C  CA  . ALA A 1 23  ? 6.002   0.146   23.360  1.00  10.89 ? 23  ALA A CA  1 
ATOM   189  C  C   . ALA A 1 23  ? 6.100   -0.559  24.683  1.00  12.12 ? 23  ALA A C   1 
ATOM   190  O  O   . ALA A 1 23  ? 5.395   -1.566  24.881  1.00  11.96 ? 23  ALA A O   1 
ATOM   191  C  CB  . ALA A 1 23  ? 6.914   -0.620  22.358  1.00  11.74 ? 23  ALA A CB  1 
ATOM   192  N  N   . LYS A 1 24  ? 7.031   -0.139  25.587  1.00  13.11 ? 24  LYS A N   1 
ATOM   193  C  CA  . LYS A 1 24  ? 7.222   -0.727  26.922  1.00  12.73 ? 24  LYS A CA  1 
ATOM   194  C  C   . LYS A 1 24  ? 6.630   0.157   27.945  1.00  14.00 ? 24  LYS A C   1 
ATOM   195  O  O   . LYS A 1 24  ? 6.986   0.023   29.133  1.00  14.89 ? 24  LYS A O   1 
ATOM   196  C  CB  . LYS A 1 24  ? 8.758   -0.995  27.193  1.00  14.68 ? 24  LYS A CB  1 
ATOM   197  C  CG  . LYS A 1 24  ? 9.334   -2.073  26.272  1.00  16.86 ? 24  LYS A CG  1 
ATOM   198  C  CD  . LYS A 1 24  ? 10.880  -2.195  26.470  1.00  21.88 ? 24  LYS A CD  1 
ATOM   199  C  CE  . LYS A 1 24  ? 11.445  -3.294  25.559  1.00  23.44 ? 24  LYS A CE  1 
ATOM   200  N  NZ  . LYS A 1 24  ? 11.267  -4.592  26.265  1.00  26.07 ? 24  LYS A NZ  1 
ATOM   201  N  N   . GLY A 1 25  ? 5.617   0.977   27.574  1.00  14.51 ? 25  GLY A N   1 
ATOM   202  C  CA  . GLY A 1 25  ? 4.978   1.904   28.527  1.00  14.88 ? 25  GLY A CA  1 
ATOM   203  C  C   . GLY A 1 25  ? 3.992   1.328   29.520  1.00  12.05 ? 25  GLY A C   1 
ATOM   204  O  O   . GLY A 1 25  ? 3.824   0.123   29.601  1.00  13.89 ? 25  GLY A O   1 
ATOM   205  N  N   . GLU A 1 26  ? 3.352   2.246   30.284  1.00  13.16 ? 26  GLU A N   1 
ATOM   206  C  CA  . GLU A 1 26  ? 2.479   1.823   31.333  1.00  15.23 ? 26  GLU A CA  1 
ATOM   207  C  C   . GLU A 1 26  ? 1.058   1.565   30.978  1.00  13.64 ? 26  GLU A C   1 
ATOM   208  O  O   . GLU A 1 26  ? 0.318   1.041   31.806  1.00  12.85 ? 26  GLU A O   1 
ATOM   209  C  CB  . GLU A 1 26  ? 2.486   2.930   32.413  1.00  19.48 ? 26  GLU A CB  1 
ATOM   210  C  CG  . GLU A 1 26  ? 3.883   3.203   33.026  1.00  25.08 ? 26  GLU A CG  1 
ATOM   211  C  CD  . GLU A 1 26  ? 4.563   1.924   33.597  1.00  32.40 ? 26  GLU A CD  1 
ATOM   212  O  OE1 . GLU A 1 26  ? 3.941   1.172   34.442  1.00  32.30 ? 26  GLU A OE1 1 
ATOM   213  O  OE2 . GLU A 1 26  ? 5.716   1.640   33.150  1.00  34.95 ? 26  GLU A OE2 1 
ATOM   214  N  N   . ARG A 1 27  ? 0.626   1.911   29.770  1.00  11.90 ? 27  ARG A N   1 
ATOM   215  C  CA  . ARG A 1 27  ? -0.788  1.653   29.418  1.00  10.60 ? 27  ARG A CA  1 
ATOM   216  C  C   . ARG A 1 27  ? -0.824  1.260   27.906  1.00  9.03  ? 27  ARG A C   1 
ATOM   217  O  O   . ARG A 1 27  ? -1.447  1.923   27.055  1.00  8.84  ? 27  ARG A O   1 
ATOM   218  C  CB  . ARG A 1 27  ? -1.660  2.906   29.804  1.00  13.32 ? 27  ARG A CB  1 
ATOM   219  C  CG  . ARG A 1 27  ? -1.385  4.210   29.102  1.00  14.64 ? 27  ARG A CG  1 
ATOM   220  C  CD  . ARG A 1 27  ? -2.409  5.382   29.391  1.00  21.60 ? 27  ARG A CD  1 
ATOM   221  N  NE  . ARG A 1 27  ? -3.567  5.284   28.505  1.00  18.47 ? 27  ARG A NE  1 
ATOM   222  C  CZ  . ARG A 1 27  ? -4.425  6.271   28.269  1.00  16.44 ? 27  ARG A CZ  1 
ATOM   223  N  NH1 . ARG A 1 27  ? -4.267  7.449   28.857  1.00  13.45 ? 27  ARG A NH1 1 
ATOM   224  N  NH2 . ARG A 1 27  ? -5.445  6.079   27.443  1.00  17.21 ? 27  ARG A NH2 1 
ATOM   225  N  N   . GLN A 1 28  ? -0.126  0.140   27.632  1.00  8.38  ? 28  GLN A N   1 
ATOM   226  C  CA  . GLN A 1 28  ? -0.095  -0.376  26.223  1.00  8.03  ? 28  GLN A CA  1 
ATOM   227  C  C   . GLN A 1 28  ? -1.267  -1.348  25.957  1.00  8.60  ? 28  GLN A C   1 
ATOM   228  O  O   . GLN A 1 28  ? -1.731  -2.024  26.850  1.00  8.58  ? 28  GLN A O   1 
ATOM   229  C  CB  . GLN A 1 28  ? 1.245   -1.049  25.983  1.00  8.46  ? 28  GLN A CB  1 
ATOM   230  C  CG  . GLN A 1 28  ? 2.375   -0.034  25.946  1.00  8.79  ? 28  GLN A CG  1 
ATOM   231  C  CD  . GLN A 1 28  ? 2.243   0.807   24.631  1.00  8.86  ? 28  GLN A CD  1 
ATOM   232  O  OE1 . GLN A 1 28  ? 2.452   0.268   23.550  1.00  9.39  ? 28  GLN A OE1 1 
ATOM   233  N  NE2 . GLN A 1 28  ? 1.923   2.088   24.701  1.00  8.88  ? 28  GLN A NE2 1 
ATOM   234  N  N   . SER A 1 29  ? -1.638  -1.404  24.695  1.00  7.01  ? 29  SER A N   1 
ATOM   235  C  CA  . SER A 1 29  ? -2.722  -2.317  24.233  1.00  7.76  ? 29  SER A CA  1 
ATOM   236  C  C   . SER A 1 29  ? -2.198  -3.175  23.086  1.00  7.68  ? 29  SER A C   1 
ATOM   237  O  O   . SER A 1 29  ? -1.196  -2.781  22.415  1.00  7.67  ? 29  SER A O   1 
ATOM   238  C  CB  . SER A 1 29  ? -3.866  -1.448  23.656  1.00  7.67  ? 29  SER A CB  1 
ATOM   239  O  OG  . SER A 1 29  ? -4.494  -0.746  24.794  1.00  7.31  ? 29  SER A OG  1 
ATOM   240  N  N   . PRO A 1 30  ? -2.793  -4.304  22.828  1.00  7.03  ? 30  PRO A N   1 
ATOM   241  C  CA  . PRO A 1 30  ? -4.009  -4.856  23.532  1.00  7.42  ? 30  PRO A CA  1 
ATOM   242  C  C   . PRO A 1 30  ? -3.594  -5.508  24.841  1.00  7.41  ? 30  PRO A C   1 
ATOM   243  O  O   . PRO A 1 30  ? -2.402  -5.593  25.196  1.00  8.26  ? 30  PRO A O   1 
ATOM   244  C  CB  . PRO A 1 30  ? -4.552  -5.877  22.553  1.00  7.68  ? 30  PRO A CB  1 
ATOM   245  C  CG  . PRO A 1 30  ? -3.225  -6.488  21.937  1.00  6.94  ? 30  PRO A CG  1 
ATOM   246  C  CD  . PRO A 1 30  ? -2.337  -5.242  21.753  1.00  8.08  ? 30  PRO A CD  1 
ATOM   247  N  N   . VAL A 1 31  ? -4.578  -6.136  25.480  1.00  6.86  ? 31  VAL A N   1 
ATOM   248  C  CA  . VAL A 1 31  ? -4.389  -6.889  26.729  1.00  7.82  ? 31  VAL A CA  1 
ATOM   249  C  C   . VAL A 1 31  ? -5.274  -8.093  26.735  1.00  7.82  ? 31  VAL A C   1 
ATOM   250  O  O   . VAL A 1 31  ? -6.225  -8.190  25.957  1.00  8.73  ? 31  VAL A O   1 
ATOM   251  C  CB  . VAL A 1 31  ? -4.750  -6.029  28.034  1.00  7.96  ? 31  VAL A CB  1 
ATOM   252  C  CG1 . VAL A 1 31  ? -3.804  -4.797  28.117  1.00  8.62  ? 31  VAL A CG1 1 
ATOM   253  C  CG2 . VAL A 1 31  ? -6.242  -5.679  28.085  1.00  9.07  ? 31  VAL A CG2 1 
ATOM   254  N  N   . ASP A 1 32  ? -4.996  -9.083  27.567  1.00  8.46  ? 32  ASP A N   1 
ATOM   255  C  CA  . ASP A 1 32  ? -5.871  -10.185 27.800  1.00  8.19  ? 32  ASP A CA  1 
ATOM   256  C  C   . ASP A 1 32  ? -6.932  -9.653  28.777  1.00  7.77  ? 32  ASP A C   1 
ATOM   257  O  O   . ASP A 1 32  ? -6.604  -8.997  29.779  1.00  10.09 ? 32  ASP A O   1 
ATOM   258  C  CB  . ASP A 1 32  ? -5.105  -11.376 28.419  1.00  9.84  ? 32  ASP A CB  1 
ATOM   259  C  CG  . ASP A 1 32  ? -6.027  -12.541 28.733  1.00  12.28 ? 32  ASP A CG  1 
ATOM   260  O  OD1 . ASP A 1 32  ? -6.753  -12.959 27.804  1.00  11.20 ? 32  ASP A OD1 1 
ATOM   261  O  OD2 . ASP A 1 32  ? -6.129  -12.986 29.930  1.00  14.53 ? 32  ASP A OD2 1 
ATOM   262  N  N   . ILE A 1 33  ? -8.186  -10.003 28.475  1.00  9.33  ? 33  ILE A N   1 
ATOM   263  C  CA  . ILE A 1 33  ? -9.327  -9.629  29.290  1.00  10.78 ? 33  ILE A CA  1 
ATOM   264  C  C   . ILE A 1 33  ? -9.622  -10.893 30.093  1.00  10.30 ? 33  ILE A C   1 
ATOM   265  O  O   . ILE A 1 33  ? -10.140 -11.871 29.611  1.00  11.52 ? 33  ILE A O   1 
ATOM   266  C  CB  . ILE A 1 33  ? -10.512 -9.187  28.456  1.00  11.44 ? 33  ILE A CB  1 
ATOM   267  C  CG1 . ILE A 1 33  ? -10.138 -7.905  27.677  1.00  10.46 ? 33  ILE A CG1 1 
ATOM   268  C  CG2 . ILE A 1 33  ? -11.699 -8.864  29.401  1.00  11.48 ? 33  ILE A CG2 1 
ATOM   269  C  CD1 . ILE A 1 33  ? -11.158 -7.597  26.510  1.00  10.71 ? 33  ILE A CD1 1 
ATOM   270  N  N   A ASP A 1 34  ? -9.236  -10.822 31.379  0.50  13.07 ? 34  ASP A N   1 
ATOM   271  N  N   B ASP A 1 34  ? -9.276  -10.844 31.366  0.50  13.02 ? 34  ASP A N   1 
ATOM   272  C  CA  A ASP A 1 34  ? -9.534  -11.879 32.387  0.50  12.73 ? 34  ASP A CA  1 
ATOM   273  C  CA  B ASP A 1 34  ? -9.545  -11.990 32.214  0.50  12.54 ? 34  ASP A CA  1 
ATOM   274  C  C   A ASP A 1 34  ? -10.984 -11.617 32.832  0.50  13.03 ? 34  ASP A C   1 
ATOM   275  C  C   B ASP A 1 34  ? -10.901 -11.709 32.832  0.50  13.00 ? 34  ASP A C   1 
ATOM   276  O  O   A ASP A 1 34  ? -11.227 -10.637 33.553  0.50  14.16 ? 34  ASP A O   1 
ATOM   277  O  O   B ASP A 1 34  ? -10.967 -10.815 33.682  0.50  14.10 ? 34  ASP A O   1 
ATOM   278  C  CB  A ASP A 1 34  ? -8.556  -11.755 33.569  0.50  14.95 ? 34  ASP A CB  1 
ATOM   279  C  CB  B ASP A 1 34  ? -8.460  -12.054 33.254  0.50  14.01 ? 34  ASP A CB  1 
ATOM   280  C  CG  A ASP A 1 34  ? -8.711  -12.888 34.588  0.50  16.58 ? 34  ASP A CG  1 
ATOM   281  C  CG  B ASP A 1 34  ? -8.611  -13.227 34.147  0.50  16.47 ? 34  ASP A CG  1 
ATOM   282  O  OD1 A ASP A 1 34  ? -9.842  -13.362 34.727  0.50  14.95 ? 34  ASP A OD1 1 
ATOM   283  O  OD1 B ASP A 1 34  ? -8.250  -14.340 33.733  0.50  16.50 ? 34  ASP A OD1 1 
ATOM   284  O  OD2 A ASP A 1 34  ? -7.684  -13.320 35.186  0.50  18.80 ? 34  ASP A OD2 1 
ATOM   285  O  OD2 B ASP A 1 34  ? -9.024  -12.971 35.274  0.50  15.83 ? 34  ASP A OD2 1 
ATOM   286  N  N   . THR A 1 35  ? -11.923 -12.412 32.354  1.00  13.58 ? 35  THR A N   1 
ATOM   287  C  CA  . THR A 1 35  ? -13.362 -12.099 32.563  1.00  14.35 ? 35  THR A CA  1 
ATOM   288  C  C   . THR A 1 35  ? -13.736 -12.208 34.032  1.00  16.12 ? 35  THR A C   1 
ATOM   289  O  O   . THR A 1 35  ? -14.666 -11.498 34.489  1.00  17.96 ? 35  THR A O   1 
ATOM   290  C  CB  . THR A 1 35  ? -14.309 -12.991 31.745  1.00  17.47 ? 35  THR A CB  1 
ATOM   291  O  OG1 . THR A 1 35  ? -14.138 -14.352 32.160  1.00  16.37 ? 35  THR A OG1 1 
ATOM   292  C  CG2 . THR A 1 35  ? -14.073 -12.914 30.254  1.00  16.94 ? 35  THR A CG2 1 
ATOM   293  N  N   . HIS A 1 36  ? -12.979 -13.023 34.755  1.00  16.48 ? 36  HIS A N   1 
ATOM   294  C  CA  . HIS A 1 36  ? -13.288 -13.269 36.170  1.00  17.79 ? 36  HIS A CA  1 
ATOM   295  C  C   . HIS A 1 36  ? -12.832 -12.173 37.038  1.00  20.32 ? 36  HIS A C   1 
ATOM   296  O  O   . HIS A 1 36  ? -13.513 -11.831 38.000  1.00  25.39 ? 36  HIS A O   1 
ATOM   297  C  CB  . HIS A 1 36  ? -12.797 -14.699 36.488  1.00  18.23 ? 36  HIS A CB  1 
ATOM   298  C  CG  . HIS A 1 36  ? -13.807 -15.715 36.048  1.00  18.70 ? 36  HIS A CG  1 
ATOM   299  N  ND1 . HIS A 1 36  ? -13.603 -16.627 35.071  1.00  21.05 ? 36  HIS A ND1 1 
ATOM   300  C  CD2 . HIS A 1 36  ? -15.154 -15.825 36.422  1.00  20.14 ? 36  HIS A CD2 1 
ATOM   301  C  CE1 . HIS A 1 36  ? -14.740 -17.313 34.867  1.00  21.35 ? 36  HIS A CE1 1 
ATOM   302  N  NE2 . HIS A 1 36  ? -15.686 -16.829 35.696  1.00  27.93 ? 36  HIS A NE2 1 
ATOM   303  N  N   . THR A 1 37  ? -11.709 -11.574 36.708  1.00  20.45 ? 37  THR A N   1 
ATOM   304  C  CA  . THR A 1 37  ? -11.208 -10.432 37.447  1.00  20.84 ? 37  THR A CA  1 
ATOM   305  C  C   . THR A 1 37  ? -11.599 -8.999  36.909  1.00  19.23 ? 37  THR A C   1 
ATOM   306  O  O   . THR A 1 37  ? -11.243 -7.991  37.514  1.00  20.45 ? 37  THR A O   1 
ATOM   307  C  CB  . THR A 1 37  ? -9.710  -10.484 37.662  1.00  23.55 ? 37  THR A CB  1 
ATOM   308  O  OG1 . THR A 1 37  ? -9.082  -10.503 36.391  1.00  23.50 ? 37  THR A OG1 1 
ATOM   309  C  CG2 . THR A 1 37  ? -9.251  -11.741 38.378  1.00  24.03 ? 37  THR A CG2 1 
ATOM   310  N  N   . ALA A 1 38  ? -12.291 -8.917  35.767  1.00  16.56 ? 38  ALA A N   1 
ATOM   311  C  CA  . ALA A 1 38  ? -12.942 -7.643  35.357  1.00  16.18 ? 38  ALA A CA  1 
ATOM   312  C  C   . ALA A 1 38  ? -13.896 -7.186  36.482  1.00  17.48 ? 38  ALA A C   1 
ATOM   313  O  O   . ALA A 1 38  ? -14.603 -8.022  37.070  1.00  19.92 ? 38  ALA A O   1 
ATOM   314  C  CB  . ALA A 1 38  ? -13.666 -7.788  34.014  1.00  16.61 ? 38  ALA A CB  1 
ATOM   315  N  N   . LYS A 1 39  ? -13.859 -5.896  36.807  1.00  16.35 ? 39  LYS A N   1 
ATOM   316  C  CA  . LYS A 1 39  ? -14.721 -5.320  37.873  1.00  17.26 ? 39  LYS A CA  1 
ATOM   317  C  C   . LYS A 1 39  ? -16.043 -4.858  37.257  1.00  18.02 ? 39  LYS A C   1 
ATOM   318  O  O   . LYS A 1 39  ? -16.045 -3.904  36.437  1.00  13.98 ? 39  LYS A O   1 
ATOM   319  C  CB  . LYS A 1 39  ? -13.932 -4.159  38.513  1.00  19.41 ? 39  LYS A CB  1 
ATOM   320  C  CG  . LYS A 1 39  ? -14.740 -3.254  39.499  1.00  21.81 ? 39  LYS A CG  1 
ATOM   321  C  CD  . LYS A 1 39  ? -14.933 -3.941  40.844  1.00  21.20 ? 39  LYS A CD  1 
ATOM   322  C  CE  . LYS A 1 39  ? -15.898 -3.131  41.734  1.00  24.62 ? 39  LYS A CE  1 
ATOM   323  N  NZ  . LYS A 1 39  ? -16.174 -3.838  43.031  1.00  24.54 ? 39  LYS A NZ  1 
ATOM   324  N  N   . TYR A 1 40  ? -17.151 -5.437  37.689  1.00  17.11 ? 40  TYR A N   1 
ATOM   325  C  CA  . TYR A 1 40  ? -18.453 -4.835  37.297  1.00  18.04 ? 40  TYR A CA  1 
ATOM   326  C  C   . TYR A 1 40  ? -18.637 -3.419  37.853  1.00  19.12 ? 40  TYR A C   1 
ATOM   327  O  O   . TYR A 1 40  ? -18.452 -3.179  39.088  1.00  17.55 ? 40  TYR A O   1 
ATOM   328  C  CB  . TYR A 1 40  ? -19.606 -5.744  37.704  1.00  21.81 ? 40  TYR A CB  1 
ATOM   329  C  CG  . TYR A 1 40  ? -20.974 -5.111  37.576  1.00  23.76 ? 40  TYR A CG  1 
ATOM   330  C  CD1 . TYR A 1 40  ? -21.497 -4.779  36.331  1.00  25.58 ? 40  TYR A CD1 1 
ATOM   331  C  CD2 . TYR A 1 40  ? -21.766 -4.896  38.718  1.00  26.18 ? 40  TYR A CD2 1 
ATOM   332  C  CE1 . TYR A 1 40  ? -22.732 -4.218  36.183  1.00  27.60 ? 40  TYR A CE1 1 
ATOM   333  C  CE2 . TYR A 1 40  ? -23.030 -4.327  38.580  1.00  27.92 ? 40  TYR A CE2 1 
ATOM   334  C  CZ  . TYR A 1 40  ? -23.487 -3.995  37.323  1.00  30.23 ? 40  TYR A CZ  1 
ATOM   335  O  OH  . TYR A 1 40  ? -24.721 -3.435  37.169  1.00  36.65 ? 40  TYR A OH  1 
ATOM   336  N  N   . ASP A 1 41  ? -19.036 -2.475  37.012  1.00  18.09 ? 41  ASP A N   1 
ATOM   337  C  CA  . ASP A 1 41  ? -19.183 -1.103  37.478  1.00  20.26 ? 41  ASP A CA  1 
ATOM   338  C  C   . ASP A 1 41  ? -20.620 -0.695  37.210  1.00  25.58 ? 41  ASP A C   1 
ATOM   339  O  O   . ASP A 1 41  ? -20.951 -0.420  36.094  1.00  23.85 ? 41  ASP A O   1 
ATOM   340  C  CB  . ASP A 1 41  ? -18.217 -0.151  36.842  1.00  23.70 ? 41  ASP A CB  1 
ATOM   341  C  CG  . ASP A 1 41  ? -18.340 1.274   37.423  1.00  28.63 ? 41  ASP A CG  1 
ATOM   342  O  OD1 . ASP A 1 41  ? -19.312 1.502   38.198  1.00  30.18 ? 41  ASP A OD1 1 
ATOM   343  O  OD2 . ASP A 1 41  ? -17.463 2.098   37.116  1.00  29.60 ? 41  ASP A OD2 1 
ATOM   344  N  N   . PRO A 1 42  ? -21.504 -0.704  38.221  1.00  26.53 ? 42  PRO A N   1 
ATOM   345  C  CA  . PRO A 1 42  ? -22.933 -0.500  37.922  1.00  26.31 ? 42  PRO A CA  1 
ATOM   346  C  C   . PRO A 1 42  ? -23.211 0.944   37.576  1.00  28.33 ? 42  PRO A C   1 
ATOM   347  O  O   . PRO A 1 42  ? -24.321 1.240   37.120  1.00  36.11 ? 42  PRO A O   1 
ATOM   348  C  CB  . PRO A 1 42  ? -23.645 -0.903  39.240  1.00  28.22 ? 42  PRO A CB  1 
ATOM   349  C  CG  . PRO A 1 42  ? -22.600 -0.689  40.285  1.00  28.94 ? 42  PRO A CG  1 
ATOM   350  C  CD  . PRO A 1 42  ? -21.228 -0.913  39.658  1.00  27.30 ? 42  PRO A CD  1 
ATOM   351  N  N   . SER A 1 43  ? -22.224 1.827   37.745  1.00  26.63 ? 43  SER A N   1 
ATOM   352  C  CA  . SER A 1 43  ? -22.364 3.243   37.343  1.00  28.93 ? 43  SER A CA  1 
ATOM   353  C  C   . SER A 1 43  ? -21.897 3.497   35.885  1.00  28.32 ? 43  SER A C   1 
ATOM   354  O  O   . SER A 1 43  ? -22.040 4.611   35.352  1.00  32.86 ? 43  SER A O   1 
ATOM   355  C  CB  . SER A 1 43  ? -21.638 4.168   38.314  1.00  32.86 ? 43  SER A CB  1 
ATOM   356  O  OG  . SER A 1 43  ? -20.255 4.318   37.971  1.00  30.01 ? 43  SER A OG  1 
ATOM   357  N  N   . LEU A 1 44  ? -21.326 2.490   35.212  1.00  28.06 ? 44  LEU A N   1 
ATOM   358  C  CA  . LEU A 1 44  ? -21.117 2.654   33.757  1.00  23.06 ? 44  LEU A CA  1 
ATOM   359  C  C   . LEU A 1 44  ? -22.466 2.767   33.025  1.00  23.10 ? 44  LEU A C   1 
ATOM   360  O  O   . LEU A 1 44  ? -23.331 1.949   33.195  1.00  24.51 ? 44  LEU A O   1 
ATOM   361  C  CB  . LEU A 1 44  ? -20.378 1.458   33.204  1.00  21.34 ? 44  LEU A CB  1 
ATOM   362  C  CG  . LEU A 1 44  ? -18.878 1.448   33.473  1.00  18.06 ? 44  LEU A CG  1 
ATOM   363  C  CD1 . LEU A 1 44  ? -18.302 0.074   33.092  1.00  17.36 ? 44  LEU A CD1 1 
ATOM   364  C  CD2 . LEU A 1 44  ? -18.106 2.575   32.818  1.00  17.89 ? 44  LEU A CD2 1 
ATOM   365  N  N   . LYS A 1 45  ? -22.536 3.711   32.095  1.00  22.65 ? 45  LYS A N   1 
ATOM   366  C  CA  . LYS A 1 45  ? -23.750 3.957   31.247  1.00  20.85 ? 45  LYS A CA  1 
ATOM   367  C  C   . LYS A 1 45  ? -23.756 3.068   30.026  1.00  20.12 ? 45  LYS A C   1 
ATOM   368  O  O   . LYS A 1 45  ? -22.702 2.545   29.627  1.00  20.02 ? 45  LYS A O   1 
ATOM   369  C  CB  . LYS A 1 45  ? -23.792 5.416   30.837  1.00  25.30 ? 45  LYS A CB  1 
ATOM   370  C  CG  . LYS A 1 45  ? -23.765 6.307   32.075  1.00  32.24 ? 45  LYS A CG  1 
ATOM   371  C  CD  . LYS A 1 45  ? -24.848 7.380   32.113  1.00  38.49 ? 45  LYS A CD  1 
ATOM   372  C  CE  . LYS A 1 45  ? -24.254 8.749   31.789  1.00  43.58 ? 45  LYS A CE  1 
ATOM   373  N  NZ  . LYS A 1 45  ? -23.024 9.008   32.598  1.00  45.53 ? 45  LYS A NZ  1 
ATOM   374  N  N   . PRO A 1 46  ? -24.943 2.789   29.450  1.00  17.94 ? 46  PRO A N   1 
ATOM   375  C  CA  . PRO A 1 46  ? -25.037 2.167   28.157  1.00  17.23 ? 46  PRO A CA  1 
ATOM   376  C  C   . PRO A 1 46  ? -24.188 2.936   27.135  1.00  15.98 ? 46  PRO A C   1 
ATOM   377  O  O   . PRO A 1 46  ? -24.121 4.145   27.178  1.00  13.74 ? 46  PRO A O   1 
ATOM   378  C  CB  . PRO A 1 46  ? -26.536 2.271   27.780  1.00  17.84 ? 46  PRO A CB  1 
ATOM   379  C  CG  . PRO A 1 46  ? -27.219 2.481   29.076  1.00  19.10 ? 46  PRO A CG  1 
ATOM   380  C  CD  . PRO A 1 46  ? -26.272 3.157   30.021  1.00  18.22 ? 46  PRO A CD  1 
ATOM   381  N  N   . LEU A 1 47  ? -23.587 2.167   26.217  1.00  17.11 ? 47  LEU A N   1 
ATOM   382  C  CA  . LEU A 1 47  ? -22.848 2.796   25.147  1.00  16.28 ? 47  LEU A CA  1 
ATOM   383  C  C   . LEU A 1 47  ? -23.893 3.437   24.179  1.00  17.79 ? 47  LEU A C   1 
ATOM   384  O  O   . LEU A 1 47  ? -24.980 2.854   23.961  1.00  19.15 ? 47  LEU A O   1 
ATOM   385  C  CB  . LEU A 1 47  ? -21.979 1.727   24.492  1.00  20.57 ? 47  LEU A CB  1 
ATOM   386  C  CG  . LEU A 1 47  ? -20.955 2.206   23.514  1.00  23.59 ? 47  LEU A CG  1 
ATOM   387  C  CD1 . LEU A 1 47  ? -19.899 3.002   24.291  1.00  20.57 ? 47  LEU A CD1 1 
ATOM   388  C  CD2 . LEU A 1 47  ? -20.353 0.928   22.915  1.00  20.93 ? 47  LEU A CD2 1 
ATOM   389  N  N   . SER A 1 48  ? -23.661 4.642   23.697  1.00  14.22 ? 48  SER A N   1 
ATOM   390  C  CA  . SER A 1 48  ? -24.504 5.284   22.711  1.00  16.24 ? 48  SER A CA  1 
ATOM   391  C  C   . SER A 1 48  ? -23.740 5.281   21.382  1.00  16.45 ? 48  SER A C   1 
ATOM   392  O  O   . SER A 1 48  ? -22.766 6.050   21.182  1.00  16.08 ? 48  SER A O   1 
ATOM   393  C  CB  . SER A 1 48  ? -24.826 6.691   23.143  1.00  17.50 ? 48  SER A CB  1 
ATOM   394  O  OG  . SER A 1 48  ? -25.556 7.378   22.141  1.00  20.52 ? 48  SER A OG  1 
ATOM   395  N  N   . VAL A 1 49  ? -24.190 4.496   20.448  1.00  17.91 ? 49  VAL A N   1 
ATOM   396  C  CA  . VAL A 1 49  ? -23.619 4.408   19.110  1.00  20.06 ? 49  VAL A CA  1 
ATOM   397  C  C   . VAL A 1 49  ? -24.584 5.053   18.151  1.00  22.11 ? 49  VAL A C   1 
ATOM   398  O  O   . VAL A 1 49  ? -25.682 4.526   17.929  1.00  22.72 ? 49  VAL A O   1 
ATOM   399  C  CB  . VAL A 1 49  ? -23.403 2.925   18.718  1.00  23.14 ? 49  VAL A CB  1 
ATOM   400  C  CG1 . VAL A 1 49  ? -22.735 2.838   17.337  1.00  24.79 ? 49  VAL A CG1 1 
ATOM   401  C  CG2 . VAL A 1 49  ? -22.620 2.165   19.791  1.00  21.50 ? 49  VAL A CG2 1 
ATOM   402  N  N   . SER A 1 50  ? -24.259 6.200   17.597  1.00  18.48 ? 50  SER A N   1 
ATOM   403  C  CA  . SER A 1 50  ? -25.166 6.952   16.722  1.00  19.47 ? 50  SER A CA  1 
ATOM   404  C  C   . SER A 1 50  ? -24.578 7.032   15.382  1.00  15.90 ? 50  SER A C   1 
ATOM   405  O  O   . SER A 1 50  ? -23.905 8.000   15.025  1.00  17.16 ? 50  SER A O   1 
ATOM   406  C  CB  . SER A 1 50  ? -25.540 8.362   17.240  1.00  21.67 ? 50  SER A CB  1 
ATOM   407  O  OG  . SER A 1 50  ? -26.114 8.223   18.475  1.00  30.76 ? 50  SER A OG  1 
ATOM   408  N  N   . TYR A 1 51  ? -24.834 5.982   14.597  1.00  16.65 ? 51  TYR A N   1 
ATOM   409  C  CA  . TYR A 1 51  ? -24.285 5.828   13.250  1.00  15.04 ? 51  TYR A CA  1 
ATOM   410  C  C   . TYR A 1 51  ? -25.279 6.082   12.086  1.00  17.70 ? 51  TYR A C   1 
ATOM   411  O  O   . TYR A 1 51  ? -24.883 5.898   10.938  1.00  18.67 ? 51  TYR A O   1 
ATOM   412  C  CB  . TYR A 1 51  ? -23.632 4.446   13.089  1.00  15.63 ? 51  TYR A CB  1 
ATOM   413  C  CG  . TYR A 1 51  ? -22.316 4.153   13.857  1.00  15.46 ? 51  TYR A CG  1 
ATOM   414  C  CD1 . TYR A 1 51  ? -21.607 5.178   14.565  1.00  15.23 ? 51  TYR A CD1 1 
ATOM   415  C  CD2 . TYR A 1 51  ? -21.801 2.894   13.848  1.00  13.62 ? 51  TYR A CD2 1 
ATOM   416  C  CE1 . TYR A 1 51  ? -20.410 4.858   15.215  1.00  14.88 ? 51  TYR A CE1 1 
ATOM   417  C  CE2 . TYR A 1 51  ? -20.668 2.564   14.509  1.00  15.13 ? 51  TYR A CE2 1 
ATOM   418  C  CZ  . TYR A 1 51  ? -19.958 3.581   15.204  1.00  13.50 ? 51  TYR A CZ  1 
ATOM   419  O  OH  . TYR A 1 51  ? -18.793 3.188   15.845  1.00  12.50 ? 51  TYR A OH  1 
ATOM   420  N  N   . ASP A 1 52  ? -26.520 6.539   12.403  1.00  21.02 ? 52  ASP A N   1 
ATOM   421  C  CA  . ASP A 1 52  ? -27.513 6.737   11.323  1.00  22.83 ? 52  ASP A CA  1 
ATOM   422  C  C   . ASP A 1 52  ? -27.031 7.691   10.206  1.00  22.23 ? 52  ASP A C   1 
ATOM   423  O  O   . ASP A 1 52  ? -27.226 7.391   9.005   1.00  25.89 ? 52  ASP A O   1 
ATOM   424  C  CB  . ASP A 1 52  ? -28.875 7.140   11.868  1.00  25.71 ? 52  ASP A CB  1 
ATOM   425  C  CG  . ASP A 1 52  ? -28.764 8.050   13.054  1.00  30.66 ? 52  ASP A CG  1 
ATOM   426  O  OD1 . ASP A 1 52  ? -28.224 7.639   14.142  1.00  38.95 ? 52  ASP A OD1 1 
ATOM   427  O  OD2 . ASP A 1 52  ? -29.177 9.221   12.891  1.00  41.73 ? 52  ASP A OD2 1 
ATOM   428  N  N   . GLN A 1 53  ? -26.329 8.742   10.553  1.00  22.45 ? 53  GLN A N   1 
ATOM   429  C  CA  . GLN A 1 53  ? -25.903 9.669   9.475   1.00  27.01 ? 53  GLN A CA  1 
ATOM   430  C  C   . GLN A 1 53  ? -24.488 9.445   8.973   1.00  21.74 ? 53  GLN A C   1 
ATOM   431  O  O   . GLN A 1 53  ? -23.887 10.376  8.400   1.00  21.67 ? 53  GLN A O   1 
ATOM   432  C  CB  . GLN A 1 53  ? -26.123 11.138  9.877   1.00  30.45 ? 53  GLN A CB  1 
ATOM   433  C  CG  . GLN A 1 53  ? -27.622 11.508  9.931   1.00  36.35 ? 53  GLN A CG  1 
ATOM   434  C  CD  . GLN A 1 53  ? -28.265 11.264  8.574   1.00  41.23 ? 53  GLN A CD  1 
ATOM   435  O  OE1 . GLN A 1 53  ? -27.780 11.773  7.539   1.00  42.18 ? 53  GLN A OE1 1 
ATOM   436  N  NE2 . GLN A 1 53  ? -29.302 10.417  8.546   1.00  41.73 ? 53  GLN A NE2 1 
ATOM   437  N  N   . ALA A 1 54  ? -23.939 8.232   9.172   1.00  17.61 ? 54  ALA A N   1 
ATOM   438  C  CA  . ALA A 1 54  ? -22.558 8.027   8.758   1.00  15.19 ? 54  ALA A CA  1 
ATOM   439  C  C   . ALA A 1 54  ? -22.369 8.222   7.295   1.00  16.33 ? 54  ALA A C   1 
ATOM   440  O  O   . ALA A 1 54  ? -23.269 7.875   6.452   1.00  16.97 ? 54  ALA A O   1 
ATOM   441  C  CB  . ALA A 1 54  ? -21.987 6.640   9.148   1.00  17.45 ? 54  ALA A CB  1 
ATOM   442  N  N   . THR A 1 55  ? -21.200 8.733   6.981   1.00  13.39 ? 55  THR A N   1 
ATOM   443  C  CA  . THR A 1 55  ? -20.780 8.962   5.590   1.00  12.38 ? 55  THR A CA  1 
ATOM   444  C  C   . THR A 1 55  ? -19.454 8.330   5.301   1.00  11.56 ? 55  THR A C   1 
ATOM   445  O  O   . THR A 1 55  ? -18.438 8.942   5.582   1.00  11.77 ? 55  THR A O   1 
ATOM   446  C  CB  . THR A 1 55  ? -20.688 10.502  5.277   1.00  15.19 ? 55  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 55  ? -22.005 11.048  5.388   1.00  18.63 ? 55  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 55  ? -20.140 10.660  3.778   1.00  16.76 ? 55  THR A CG2 1 
ATOM   449  N  N   . SER A 1 56  ? -19.396 7.084   4.753   1.00  12.92 ? 56  SER A N   1 
ATOM   450  C  CA  . SER A 1 56  ? -18.144 6.515   4.370   1.00  13.62 ? 56  SER A CA  1 
ATOM   451  C  C   . SER A 1 56  ? -17.696 7.165   3.105   1.00  14.35 ? 56  SER A C   1 
ATOM   452  O  O   . SER A 1 56  ? -18.557 7.628   2.273   1.00  13.65 ? 56  SER A O   1 
ATOM   453  C  CB  . SER A 1 56  ? -18.220 4.969   4.182   1.00  12.28 ? 56  SER A CB  1 
ATOM   454  O  OG  . SER A 1 56  ? -19.206 4.663   3.114   1.00  14.74 ? 56  SER A OG  1 
ATOM   455  N  N   . LEU A 1 57  ? -16.417 7.166   2.911   1.00  12.89 ? 57  LEU A N   1 
ATOM   456  C  CA  . LEU A 1 57  ? -15.849 7.852   1.758   1.00  16.61 ? 57  LEU A CA  1 
ATOM   457  C  C   . LEU A 1 57  ? -15.041 6.931   0.906   1.00  17.64 ? 57  LEU A C   1 
ATOM   458  O  O   . LEU A 1 57  ? -15.139 6.946   -0.354  1.00  16.20 ? 57  LEU A O   1 
ATOM   459  C  CB  . LEU A 1 57  ? -14.946 8.993   2.256   1.00  17.93 ? 57  LEU A CB  1 
ATOM   460  C  CG  . LEU A 1 57  ? -15.733 10.193  2.853   1.00  20.75 ? 57  LEU A CG  1 
ATOM   461  C  CD1 . LEU A 1 57  ? -14.701 11.196  3.310   1.00  20.93 ? 57  LEU A CD1 1 
ATOM   462  C  CD2 . LEU A 1 57  ? -16.706 10.828  1.839   1.00  21.02 ? 57  LEU A CD2 1 
ATOM   463  N  N   . ARG A 1 58  ? -14.162 6.147   1.511   1.00  14.91 ? 58  ARG A N   1 
ATOM   464  C  CA  . ARG A 1 58  ? -13.096 5.507   0.799   1.00  15.71 ? 58  ARG A CA  1 
ATOM   465  C  C   . ARG A 1 58  ? -12.668 4.283   1.607   1.00  15.09 ? 58  ARG A C   1 
ATOM   466  O  O   . ARG A 1 58  ? -12.835 4.281   2.845   1.00  13.91 ? 58  ARG A O   1 
ATOM   467  C  CB  . ARG A 1 58  ? -11.989 6.544   0.703   1.00  19.19 ? 58  ARG A CB  1 
ATOM   468  C  CG  . ARG A 1 58  ? -10.995 6.241   -0.346  1.00  22.20 ? 58  ARG A CG  1 
ATOM   469  C  CD  . ARG A 1 58  ? -10.042 7.419   -0.502  1.00  24.45 ? 58  ARG A CD  1 
ATOM   470  N  NE  . ARG A 1 58  ? -9.221  7.387   0.697   1.00  21.28 ? 58  ARG A NE  1 
ATOM   471  C  CZ  . ARG A 1 58  ? -7.891  7.466   0.695   1.00  18.98 ? 58  ARG A CZ  1 
ATOM   472  N  NH1 . ARG A 1 58  ? -7.224  7.684   -0.441  1.00  21.62 ? 58  ARG A NH1 1 
ATOM   473  N  NH2 . ARG A 1 58  ? -7.254  7.455   1.869   1.00  19.04 ? 58  ARG A NH2 1 
ATOM   474  N  N   . ILE A 1 59  ? -12.052 3.330   0.948   1.00  13.89 ? 59  ILE A N   1 
ATOM   475  C  CA  . ILE A 1 59  ? -11.414 2.217   1.550   1.00  13.20 ? 59  ILE A CA  1 
ATOM   476  C  C   . ILE A 1 59  ? -9.958  2.248   1.087   1.00  12.69 ? 59  ILE A C   1 
ATOM   477  O  O   . ILE A 1 59  ? -9.632  2.416   -0.125  1.00  15.90 ? 59  ILE A O   1 
ATOM   478  C  CB  . ILE A 1 59  ? -12.090 0.898   1.290   1.00  12.13 ? 59  ILE A CB  1 
ATOM   479  C  CG1 . ILE A 1 59  ? -11.473 -0.253  2.153   1.00  15.37 ? 59  ILE A CG1 1 
ATOM   480  C  CG2 . ILE A 1 59  ? -12.056 0.498   -0.225  1.00  13.24 ? 59  ILE A CG2 1 
ATOM   481  C  CD1 . ILE A 1 59  ? -12.330 -1.530  2.123   1.00  14.53 ? 59  ILE A CD1 1 
ATOM   482  N  N   . LEU A 1 60  ? -9.009  2.023   1.996   1.00  14.60 ? 60  LEU A N   1 
ATOM   483  C  CA  . LEU A 1 60  ? -7.587  2.155   1.731   1.00  13.37 ? 60  LEU A CA  1 
ATOM   484  C  C   . LEU A 1 60  ? -6.757  1.001   2.253   1.00  14.07 ? 60  LEU A C   1 
ATOM   485  O  O   . LEU A 1 60  ? -6.926  0.582   3.425   1.00  14.37 ? 60  LEU A O   1 
ATOM   486  C  CB  . LEU A 1 60  ? -7.060  3.470   2.459   1.00  15.34 ? 60  LEU A CB  1 
ATOM   487  C  CG  . LEU A 1 60  ? -5.544  3.717   2.340   1.00  15.43 ? 60  LEU A CG  1 
ATOM   488  C  CD1 . LEU A 1 60  ? -5.062  3.920   0.897   1.00  18.85 ? 60  LEU A CD1 1 
ATOM   489  C  CD2 . LEU A 1 60  ? -5.008  4.788   3.334   1.00  16.68 ? 60  LEU A CD2 1 
ATOM   490  N  N   . ASN A 1 61  ? -5.870  0.418   1.470   1.00  12.45 ? 61  ASN A N   1 
ATOM   491  C  CA  . ASN A 1 61  ? -4.824  -0.490  1.920   1.00  12.74 ? 61  ASN A CA  1 
ATOM   492  C  C   . ASN A 1 61  ? -3.595  0.319   2.273   1.00  15.99 ? 61  ASN A C   1 
ATOM   493  O  O   . ASN A 1 61  ? -2.890  0.864   1.426   1.00  16.61 ? 61  ASN A O   1 
ATOM   494  C  CB  . ASN A 1 61  ? -4.457  -1.587  0.868   1.00  12.48 ? 61  ASN A CB  1 
ATOM   495  C  CG  . ASN A 1 61  ? -3.381  -2.519  1.289   1.00  12.82 ? 61  ASN A CG  1 
ATOM   496  O  OD1 . ASN A 1 61  ? -2.539  -2.244  2.187   1.00  14.60 ? 61  ASN A OD1 1 
ATOM   497  N  ND2 . ASN A 1 61  ? -3.374  -3.735  0.684   1.00  13.81 ? 61  ASN A ND2 1 
ATOM   498  N  N   . ASN A 1 62  ? -3.298  0.386   3.561   1.00  13.57 ? 62  ASN A N   1 
ATOM   499  C  CA  . ASN A 1 62  ? -2.197  1.233   4.033   1.00  14.37 ? 62  ASN A CA  1 
ATOM   500  C  C   . ASN A 1 62  ? -0.931  0.482   4.251   1.00  14.83 ? 62  ASN A C   1 
ATOM   501  O  O   . ASN A 1 62  ? 0.118   1.026   4.794   1.00  18.74 ? 62  ASN A O   1 
ATOM   502  C  CB  . ASN A 1 62  ? -2.600  2.022   5.279   1.00  15.91 ? 62  ASN A CB  1 
ATOM   503  C  CG  . ASN A 1 62  ? -2.749  1.143   6.498   1.00  14.86 ? 62  ASN A CG  1 
ATOM   504  O  OD1 . ASN A 1 62  ? -2.528  -0.052  6.460   1.00  14.75 ? 62  ASN A OD1 1 
ATOM   505  N  ND2 . ASN A 1 62  ? -2.971  1.791   7.647   1.00  19.86 ? 62  ASN A ND2 1 
ATOM   506  N  N   . GLY A 1 63  ? -0.901  -0.810  3.875   1.00  13.67 ? 63  GLY A N   1 
ATOM   507  C  CA  . GLY A 1 63  ? 0.283   -1.608  4.045   1.00  13.38 ? 63  GLY A CA  1 
ATOM   508  C  C   . GLY A 1 63  ? 0.382   -2.416  5.377   1.00  13.90 ? 63  GLY A C   1 
ATOM   509  O  O   . GLY A 1 63  ? 1.266   -3.211  5.621   1.00  14.13 ? 63  GLY A O   1 
ATOM   510  N  N   . HIS A 1 64  ? -0.605  -2.134  6.230   1.00  12.83 ? 64  HIS A N   1 
ATOM   511  C  CA  . HIS A 1 64  ? -0.701  -2.778  7.592   1.00  12.83 ? 64  HIS A CA  1 
ATOM   512  C  C   . HIS A 1 64  ? -2.052  -3.428  7.716   1.00  12.83 ? 64  HIS A C   1 
ATOM   513  O  O   . HIS A 1 64  ? -2.144  -4.516  8.356   1.00  16.48 ? 64  HIS A O   1 
ATOM   514  C  CB  . HIS A 1 64  ? -0.456  -1.796  8.770   1.00  14.99 ? 64  HIS A CB  1 
ATOM   515  C  CG  . HIS A 1 64  ? 0.812   -0.987  8.591   1.00  15.89 ? 64  HIS A CG  1 
ATOM   516  N  ND1 . HIS A 1 64  ? 2.032   -1.579  8.610   1.00  18.74 ? 64  HIS A ND1 1 
ATOM   517  C  CD2 . HIS A 1 64  ? 1.007   0.356   8.368   1.00  17.67 ? 64  HIS A CD2 1 
ATOM   518  C  CE1 . HIS A 1 64  ? 2.992   -0.646  8.432   1.00  18.45 ? 64  HIS A CE1 1 
ATOM   519  N  NE2 . HIS A 1 64  ? 2.404   0.526   8.246   1.00  20.57 ? 64  HIS A NE2 1 
ATOM   520  N  N   . ALA A 1 65  ? -3.064  -2.801  7.219   1.00  12.19 ? 65  ALA A N   1 
ATOM   521  C  CA  . ALA A 1 65  ? -4.453  -3.288  7.259   1.00  11.28 ? 65  ALA A CA  1 
ATOM   522  C  C   . ALA A 1 65  ? -5.237  -2.631  6.129   1.00  12.42 ? 65  ALA A C   1 
ATOM   523  O  O   . ALA A 1 65  ? -4.586  -1.948  5.284   1.00  13.82 ? 65  ALA A O   1 
ATOM   524  C  CB  . ALA A 1 65  ? -5.141  -3.070  8.694   1.00  12.06 ? 65  ALA A CB  1 
ATOM   525  N  N   . PHE A 1 66  ? -6.555  -2.771  6.070   1.00  12.58 ? 66  PHE A N   1 
ATOM   526  C  CA  . PHE A 1 66  ? -7.362  -1.859  5.280   1.00  13.46 ? 66  PHE A CA  1 
ATOM   527  C  C   . PHE A 1 66  ? -8.239  -0.953  6.117   1.00  14.19 ? 66  PHE A C   1 
ATOM   528  O  O   . PHE A 1 66  ? -8.744  -1.429  7.171   1.00  13.08 ? 66  PHE A O   1 
ATOM   529  C  CB  . PHE A 1 66  ? -8.163  -2.596  4.174   1.00  13.36 ? 66  PHE A CB  1 
ATOM   530  C  CG  . PHE A 1 66  ? -9.164  -3.556  4.700   1.00  11.76 ? 66  PHE A CG  1 
ATOM   531  C  CD1 . PHE A 1 66  ? -10.403 -3.066  4.958   1.00  12.28 ? 66  PHE A CD1 1 
ATOM   532  C  CD2 . PHE A 1 66  ? -8.900  -4.891  4.856   1.00  13.07 ? 66  PHE A CD2 1 
ATOM   533  C  CE1 . PHE A 1 66  ? -11.380 -3.868  5.500   1.00  12.59 ? 66  PHE A CE1 1 
ATOM   534  C  CE2 . PHE A 1 66  ? -9.864  -5.705  5.431   1.00  13.69 ? 66  PHE A CE2 1 
ATOM   535  C  CZ  . PHE A 1 66  ? -11.136 -5.207  5.685   1.00  12.55 ? 66  PHE A CZ  1 
ATOM   536  N  N   A ASN A 1 67  ? -8.293  0.370   5.833   0.50  12.66 ? 67  ASN A N   1 
ATOM   537  N  N   B ASN A 1 67  ? -8.594  0.205   5.584   0.50  15.13 ? 67  ASN A N   1 
ATOM   538  C  CA  A ASN A 1 67  ? -9.159  1.315   6.596   0.50  12.72 ? 67  ASN A CA  1 
ATOM   539  C  CA  B ASN A 1 67  ? -9.188  1.243   6.381   0.50  14.81 ? 67  ASN A CA  1 
ATOM   540  C  C   A ASN A 1 67  ? -10.355 1.637   5.741   0.50  11.31 ? 67  ASN A C   1 
ATOM   541  C  C   B ASN A 1 67  ? -10.397 1.864   5.720   0.50  12.32 ? 67  ASN A C   1 
ATOM   542  O  O   A ASN A 1 67  ? -10.152 1.834   4.517   0.50  12.80 ? 67  ASN A O   1 
ATOM   543  O  O   B ASN A 1 67  ? -10.298 2.471   4.607   0.50  11.78 ? 67  ASN A O   1 
ATOM   544  C  CB  A ASN A 1 67  ? -8.427  2.636   6.912   0.50  12.49 ? 67  ASN A CB  1 
ATOM   545  C  CB  B ASN A 1 67  ? -8.093  2.264   6.646   0.50  16.68 ? 67  ASN A CB  1 
ATOM   546  C  CG  A ASN A 1 67  ? -7.182  2.424   7.796   0.50  11.79 ? 67  ASN A CG  1 
ATOM   547  C  CG  B ASN A 1 67  ? -6.927  1.653   7.392   0.50  19.89 ? 67  ASN A CG  1 
ATOM   548  O  OD1 A ASN A 1 67  ? -6.923  1.285   8.312   0.50  11.63 ? 67  ASN A OD1 1 
ATOM   549  O  OD1 B ASN A 1 67  ? -6.925  1.597   8.614   0.50  19.35 ? 67  ASN A OD1 1 
ATOM   550  N  ND2 A ASN A 1 67  ? -6.359  3.457   7.929   0.50  14.41 ? 67  ASN A ND2 1 
ATOM   551  N  ND2 B ASN A 1 67  ? -5.986  1.105   6.668   0.50  19.25 ? 67  ASN A ND2 1 
ATOM   552  N  N   . VAL A 1 68  ? -11.557 1.703   6.314   1.00  10.89 ? 68  VAL A N   1 
ATOM   553  C  CA  . VAL A 1 68  ? -12.741 2.300   5.685   1.00  10.83 ? 68  VAL A CA  1 
ATOM   554  C  C   . VAL A 1 68  ? -12.914 3.673   6.356   1.00  13.73 ? 68  VAL A C   1 
ATOM   555  O  O   . VAL A 1 68  ? -13.028 3.740   7.603   1.00  11.67 ? 68  VAL A O   1 
ATOM   556  C  CB  . VAL A 1 68  ? -13.987 1.448   5.887   1.00  12.72 ? 68  VAL A CB  1 
ATOM   557  C  CG1 . VAL A 1 68  ? -15.258 2.205   5.412   1.00  12.64 ? 68  VAL A CG1 1 
ATOM   558  C  CG2 . VAL A 1 68  ? -13.879 0.131   5.138   1.00  13.70 ? 68  VAL A CG2 1 
ATOM   559  N  N   . GLU A 1 69  ? -12.906 4.758   5.598   1.00  14.27 ? 69  GLU A N   1 
ATOM   560  C  CA  . GLU A 1 69  ? -12.682 6.112   6.187   1.00  13.67 ? 69  GLU A CA  1 
ATOM   561  C  C   . GLU A 1 69  ? -14.002 6.801   6.065   1.00  14.05 ? 69  GLU A C   1 
ATOM   562  O  O   . GLU A 1 69  ? -14.783 6.552   5.076   1.00  15.16 ? 69  GLU A O   1 
ATOM   563  C  CB  . GLU A 1 69  ? -11.781 6.916   5.338   1.00  15.22 ? 69  GLU A CB  1 
ATOM   564  C  CG  . GLU A 1 69  ? -10.381 6.427   5.356   1.00  15.85 ? 69  GLU A CG  1 
ATOM   565  C  CD  . GLU A 1 69  ? -9.619  6.849   4.152   1.00  21.41 ? 69  GLU A CD  1 
ATOM   566  O  OE1 . GLU A 1 69  ? -10.297 7.436   3.252   1.00  22.96 ? 69  GLU A OE1 1 
ATOM   567  O  OE2 . GLU A 1 69  ? -8.400  6.535   4.108   1.00  23.33 ? 69  GLU A OE2 1 
ATOM   568  N  N   . PHE A 1 70  ? -14.292 7.680   7.020   1.00  12.54 ? 70  PHE A N   1 
ATOM   569  C  CA  . PHE A 1 70  ? -15.553 8.382   7.104   1.00  11.88 ? 70  PHE A CA  1 
ATOM   570  C  C   . PHE A 1 70  ? -15.328 9.882   7.108   1.00  11.09 ? 70  PHE A C   1 
ATOM   571  O  O   . PHE A 1 70  ? -14.207 10.353  7.396   1.00  12.63 ? 70  PHE A O   1 
ATOM   572  C  CB  . PHE A 1 70  ? -16.254 7.989   8.345   1.00  11.50 ? 70  PHE A CB  1 
ATOM   573  C  CG  . PHE A 1 70  ? -16.837 6.595   8.266   1.00  11.61 ? 70  PHE A CG  1 
ATOM   574  C  CD1 . PHE A 1 70  ? -16.040 5.497   8.457   1.00  12.61 ? 70  PHE A CD1 1 
ATOM   575  C  CD2 . PHE A 1 70  ? -18.219 6.399   7.997   1.00  11.24 ? 70  PHE A CD2 1 
ATOM   576  C  CE1 . PHE A 1 70  ? -16.588 4.170   8.329   1.00  13.24 ? 70  PHE A CE1 1 
ATOM   577  C  CE2 . PHE A 1 70  ? -18.762 5.103   7.847   1.00  10.54 ? 70  PHE A CE2 1 
ATOM   578  C  CZ  . PHE A 1 70  ? -17.946 3.980   8.007   1.00  11.78 ? 70  PHE A CZ  1 
ATOM   579  N  N   . ASP A 1 71  ? -16.358 10.602  6.686   1.00  12.62 ? 71  ASP A N   1 
ATOM   580  C  CA  . ASP A 1 71  ? -16.283 12.058  6.815   1.00  13.33 ? 71  ASP A CA  1 
ATOM   581  C  C   . ASP A 1 71  ? -16.476 12.398  8.261   1.00  13.09 ? 71  ASP A C   1 
ATOM   582  O  O   . ASP A 1 71  ? -17.569 12.178  8.824   1.00  16.91 ? 71  ASP A O   1 
ATOM   583  C  CB  . ASP A 1 71  ? -17.352 12.679  5.911   1.00  14.75 ? 71  ASP A CB  1 
ATOM   584  C  CG  . ASP A 1 71  ? -17.620 14.187  6.233   1.00  16.37 ? 71  ASP A CG  1 
ATOM   585  O  OD1 . ASP A 1 71  ? -16.738 14.825  6.806   1.00  16.16 ? 71  ASP A OD1 1 
ATOM   586  O  OD2 . ASP A 1 71  ? -18.749 14.684  6.041   1.00  21.17 ? 71  ASP A OD2 1 
ATOM   587  N  N   . ASP A 1 72  ? -15.452 12.898  8.921   1.00  11.35 ? 72  ASP A N   1 
ATOM   588  C  CA  . ASP A 1 72  ? -15.515 13.268  10.333  1.00  13.05 ? 72  ASP A CA  1 
ATOM   589  C  C   . ASP A 1 72  ? -15.429 14.788  10.457  1.00  12.45 ? 72  ASP A C   1 
ATOM   590  O  O   . ASP A 1 72  ? -14.971 15.270  11.522  1.00  15.01 ? 72  ASP A O   1 
ATOM   591  C  CB  . ASP A 1 72  ? -14.314 12.621  11.091  1.00  13.47 ? 72  ASP A CB  1 
ATOM   592  C  CG  . ASP A 1 72  ? -12.979 13.099  10.638  1.00  15.21 ? 72  ASP A CG  1 
ATOM   593  O  OD1 . ASP A 1 72  ? -12.882 13.768  9.566   1.00  15.92 ? 72  ASP A OD1 1 
ATOM   594  O  OD2 . ASP A 1 72  ? -11.952 12.812  11.290  1.00  15.15 ? 72  ASP A OD2 1 
ATOM   595  N  N   . SER A 1 73  ? -15.976 15.510  9.480   1.00  12.13 ? 73  SER A N   1 
ATOM   596  C  CA  . SER A 1 73  ? -15.947 16.999  9.558   1.00  13.73 ? 73  SER A CA  1 
ATOM   597  C  C   . SER A 1 73  ? -17.227 17.528  10.219  1.00  14.16 ? 73  SER A C   1 
ATOM   598  O  O   . SER A 1 73  ? -17.392 18.764  10.356  1.00  14.02 ? 73  SER A O   1 
ATOM   599  C  CB  . SER A 1 73  ? -15.638 17.598  8.186   1.00  14.50 ? 73  SER A CB  1 
ATOM   600  O  OG  . SER A 1 73  ? -16.773 17.395  7.408   1.00  14.95 ? 73  SER A OG  1 
ATOM   601  N  N   . GLN A 1 74  ? -18.142 16.641  10.666  1.00  15.62 ? 74  GLN A N   1 
ATOM   602  C  CA  . GLN A 1 74  ? -19.368 16.999  11.358  1.00  15.49 ? 74  GLN A CA  1 
ATOM   603  C  C   . GLN A 1 74  ? -19.723 15.830  12.219  1.00  17.34 ? 74  GLN A C   1 
ATOM   604  O  O   . GLN A 1 74  ? -19.202 14.766  12.005  1.00  16.90 ? 74  GLN A O   1 
ATOM   605  C  CB  . GLN A 1 74  ? -20.585 17.211  10.405  1.00  19.88 ? 74  GLN A CB  1 
ATOM   606  C  CG  . GLN A 1 74  ? -20.424 18.315  9.401   1.00  21.93 ? 74  GLN A CG  1 
ATOM   607  C  CD  . GLN A 1 74  ? -21.750 18.479  8.659   1.00  27.72 ? 74  GLN A CD  1 
ATOM   608  O  OE1 . GLN A 1 74  ? -22.723 18.984  9.249   1.00  31.27 ? 74  GLN A OE1 1 
ATOM   609  N  NE2 . GLN A 1 74  ? -21.804 18.033  7.413   1.00  24.79 ? 74  GLN A NE2 1 
ATOM   610  N  N   . ASP A 1 75  ? -20.609 16.047  13.163  1.00  17.49 ? 75  ASP A N   1 
ATOM   611  C  CA  . ASP A 1 75  ? -21.070 15.021  14.143  1.00  20.90 ? 75  ASP A CA  1 
ATOM   612  C  C   . ASP A 1 75  ? -22.093 14.082  13.474  1.00  22.92 ? 75  ASP A C   1 
ATOM   613  O  O   . ASP A 1 75  ? -23.298 14.096  13.818  1.00  31.13 ? 75  ASP A O   1 
ATOM   614  C  CB  . ASP A 1 75  ? -21.734 15.649  15.396  1.00  26.15 ? 75  ASP A CB  1 
ATOM   615  C  CG  . ASP A 1 75  ? -20.720 16.239  16.376  1.00  28.61 ? 75  ASP A CG  1 
ATOM   616  O  OD1 . ASP A 1 75  ? -19.494 16.137  16.134  1.00  29.01 ? 75  ASP A OD1 1 
ATOM   617  O  OD2 . ASP A 1 75  ? -21.160 16.826  17.414  1.00  35.31 ? 75  ASP A OD2 1 
ATOM   618  N  N   . LYS A 1 76  ? -21.628 13.266  12.555  1.00  20.96 ? 76  LYS A N   1 
ATOM   619  C  CA  . LYS A 1 76  ? -22.511 12.393  11.790  1.00  19.53 ? 76  LYS A CA  1 
ATOM   620  C  C   . LYS A 1 76  ? -22.609 10.904  12.255  1.00  19.84 ? 76  LYS A C   1 
ATOM   621  O  O   . LYS A 1 76  ? -23.629 10.185  12.087  1.00  24.72 ? 76  LYS A O   1 
ATOM   622  C  CB  . LYS A 1 76  ? -21.960 12.294  10.417  1.00  20.89 ? 76  LYS A CB  1 
ATOM   623  C  CG  . LYS A 1 76  ? -22.360 13.476  9.597   1.00  23.52 ? 76  LYS A CG  1 
ATOM   624  C  CD  . LYS A 1 76  ? -21.574 13.319  8.305   1.00  24.66 ? 76  LYS A CD  1 
ATOM   625  C  CE  . LYS A 1 76  ? -22.050 14.363  7.300   1.00  24.67 ? 76  LYS A CE  1 
ATOM   626  N  NZ  . LYS A 1 76  ? -21.523 13.989  5.990   1.00  23.37 ? 76  LYS A NZ  1 
ATOM   627  N  N   . ALA A 1 77  ? -21.484 10.397  12.703  1.00  16.87 ? 77  ALA A N   1 
ATOM   628  C  CA  . ALA A 1 77  ? -21.384 9.041   13.285  1.00  16.74 ? 77  ALA A CA  1 
ATOM   629  C  C   . ALA A 1 77  ? -20.573 9.249   14.560  1.00  16.75 ? 77  ALA A C   1 
ATOM   630  O  O   . ALA A 1 77  ? -19.326 9.435   14.487  1.00  18.10 ? 77  ALA A O   1 
ATOM   631  C  CB  . ALA A 1 77  ? -20.539 8.233   12.298  1.00  18.56 ? 77  ALA A CB  1 
ATOM   632  N  N   . VAL A 1 78  ? -21.192 9.150   15.690  1.00  13.20 ? 78  VAL A N   1 
ATOM   633  C  CA  . VAL A 1 78  ? -20.537 9.436   16.970  1.00  14.67 ? 78  VAL A CA  1 
ATOM   634  C  C   . VAL A 1 78  ? -20.787 8.358   18.018  1.00  14.54 ? 78  VAL A C   1 
ATOM   635  O  O   . VAL A 1 78  ? -21.839 7.681   18.074  1.00  15.20 ? 78  VAL A O   1 
ATOM   636  C  CB  . VAL A 1 78  ? -20.946 10.798  17.604  1.00  17.26 ? 78  VAL A CB  1 
ATOM   637  C  CG1 . VAL A 1 78  ? -20.715 11.956  16.641  1.00  19.03 ? 78  VAL A CG1 1 
ATOM   638  C  CG2 . VAL A 1 78  ? -22.395 10.744  18.031  1.00  17.89 ? 78  VAL A CG2 1 
ATOM   639  N  N   . LEU A 1 79  ? -19.784 8.225   18.869  1.00  13.59 ? 79  LEU A N   1 
ATOM   640  C  CA  . LEU A 1 79  ? -19.855 7.410   20.046  1.00  14.42 ? 79  LEU A CA  1 
ATOM   641  C  C   . LEU A 1 79  ? -19.837 8.291   21.253  1.00  14.80 ? 79  LEU A C   1 
ATOM   642  O  O   . LEU A 1 79  ? -19.081 9.266   21.333  1.00  12.91 ? 79  LEU A O   1 
ATOM   643  C  CB  . LEU A 1 79  ? -18.629 6.498   20.079  1.00  13.83 ? 79  LEU A CB  1 
ATOM   644  C  CG  . LEU A 1 79  ? -18.535 5.436   21.130  1.00  14.25 ? 79  LEU A CG  1 
ATOM   645  C  CD1 . LEU A 1 79  ? -19.683 4.450   20.958  1.00  16.96 ? 79  LEU A CD1 1 
ATOM   646  C  CD2 . LEU A 1 79  ? -17.192 4.720   21.069  1.00  14.24 ? 79  LEU A CD2 1 
ATOM   647  N  N   . LYS A 1 80  ? -20.751 8.018   22.177  1.00  13.51 ? 80  LYS A N   1 
ATOM   648  C  CA  . LYS A 1 80  ? -20.772 8.678   23.468  1.00  15.95 ? 80  LYS A CA  1 
ATOM   649  C  C   . LYS A 1 80  ? -21.394 7.775   24.501  1.00  13.74 ? 80  LYS A C   1 
ATOM   650  O  O   . LYS A 1 80  ? -21.597 6.572   24.256  1.00  13.09 ? 80  LYS A O   1 
ATOM   651  C  CB  . LYS A 1 80  ? -21.471 10.014  23.417  1.00  21.86 ? 80  LYS A CB  1 
ATOM   652  C  CG  . LYS A 1 80  ? -22.817 9.933   22.706  1.00  25.87 ? 80  LYS A CG  1 
ATOM   653  C  CD  . LYS A 1 80  ? -23.515 11.284  22.472  1.00  30.46 ? 80  LYS A CD  1 
ATOM   654  C  CE  . LYS A 1 80  ? -23.001 12.058  21.269  1.00  42.00 ? 80  LYS A CE  1 
ATOM   655  N  NZ  . LYS A 1 80  ? -23.914 13.201  20.893  1.00  49.24 ? 80  LYS A NZ  1 
ATOM   656  N  N   . GLY A 1 81  ? -21.507 8.319   25.713  1.00  15.21 ? 81  GLY A N   1 
ATOM   657  C  CA  . GLY A 1 81  ? -22.026 7.473   26.805  1.00  16.08 ? 81  GLY A CA  1 
ATOM   658  C  C   . GLY A 1 81  ? -21.045 6.385   27.175  1.00  16.11 ? 81  GLY A C   1 
ATOM   659  O  O   . GLY A 1 81  ? -19.794 6.598   27.009  1.00  15.14 ? 81  GLY A O   1 
ATOM   660  N  N   . GLY A 1 82  ? -21.514 5.254   27.683  1.00  17.70 ? 82  GLY A N   1 
ATOM   661  C  CA  . GLY A 1 82  ? -20.560 4.210   28.085  1.00  19.41 ? 82  GLY A CA  1 
ATOM   662  C  C   . GLY A 1 82  ? -19.662 4.768   29.182  1.00  19.81 ? 82  GLY A C   1 
ATOM   663  O  O   . GLY A 1 82  ? -20.168 5.437   30.111  1.00  23.10 ? 82  GLY A O   1 
ATOM   664  N  N   . PRO A 1 83  ? -18.318 4.573   29.094  1.00  16.81 ? 83  PRO A N   1 
ATOM   665  C  CA  . PRO A 1 83  ? -17.425 5.206   30.056  1.00  15.77 ? 83  PRO A CA  1 
ATOM   666  C  C   . PRO A 1 83  ? -16.937 6.632   29.698  1.00  19.19 ? 83  PRO A C   1 
ATOM   667  O  O   . PRO A 1 83  ? -16.136 7.254   30.429  1.00  19.72 ? 83  PRO A O   1 
ATOM   668  C  CB  . PRO A 1 83  ? -16.169 4.283   29.998  1.00  17.59 ? 83  PRO A CB  1 
ATOM   669  C  CG  . PRO A 1 83  ? -16.141 3.939   28.496  1.00  14.13 ? 83  PRO A CG  1 
ATOM   670  C  CD  . PRO A 1 83  ? -17.563 3.733   28.113  1.00  14.29 ? 83  PRO A CD  1 
ATOM   671  N  N   . LEU A 1 84  ? -17.470 7.183   28.623  1.00  17.53 ? 84  LEU A N   1 
ATOM   672  C  CA  . LEU A 1 84  ? -16.933 8.407   28.026  1.00  16.13 ? 84  LEU A CA  1 
ATOM   673  C  C   . LEU A 1 84  ? -17.666 9.617   28.576  1.00  18.52 ? 84  LEU A C   1 
ATOM   674  O  O   . LEU A 1 84  ? -18.895 9.612   28.751  1.00  18.39 ? 84  LEU A O   1 
ATOM   675  C  CB  . LEU A 1 84  ? -17.109 8.398   26.521  1.00  13.95 ? 84  LEU A CB  1 
ATOM   676  C  CG  . LEU A 1 84  ? -16.518 7.098   25.889  1.00  11.28 ? 84  LEU A CG  1 
ATOM   677  C  CD1 . LEU A 1 84  ? -16.843 7.069   24.429  1.00  14.38 ? 84  LEU A CD1 1 
ATOM   678  C  CD2 . LEU A 1 84  ? -14.925 7.065   25.986  1.00  13.15 ? 84  LEU A CD2 1 
ATOM   679  N  N   . ASP A 1 85  ? -16.877 10.658  28.714  1.00  22.20 ? 85  ASP A N   1 
ATOM   680  C  CA  . ASP A 1 85  ? -17.394 12.018  28.892  1.00  29.80 ? 85  ASP A CA  1 
ATOM   681  C  C   . ASP A 1 85  ? -17.374 12.688  27.519  1.00  28.85 ? 85  ASP A C   1 
ATOM   682  O  O   . ASP A 1 85  ? -16.461 12.503  26.728  1.00  37.56 ? 85  ASP A O   1 
ATOM   683  C  CB  . ASP A 1 85  ? -16.518 12.728  29.925  1.00  31.34 ? 85  ASP A CB  1 
ATOM   684  C  CG  . ASP A 1 85  ? -16.798 12.251  31.357  1.00  41.93 ? 85  ASP A CG  1 
ATOM   685  O  OD1 . ASP A 1 85  ? -17.937 11.813  31.668  1.00  40.57 ? 85  ASP A OD1 1 
ATOM   686  O  OD2 . ASP A 1 85  ? -15.855 12.340  32.187  1.00  50.07 ? 85  ASP A OD2 1 
ATOM   687  N  N   . GLY A 1 86  ? -18.375 13.480  27.169  1.00  32.30 ? 86  GLY A N   1 
ATOM   688  C  CA  . GLY A 1 86  ? -18.314 13.961  25.781  1.00  28.98 ? 86  GLY A CA  1 
ATOM   689  C  C   . GLY A 1 86  ? -18.254 12.947  24.588  1.00  27.88 ? 86  GLY A C   1 
ATOM   690  O  O   . GLY A 1 86  ? -18.391 11.681  24.716  1.00  24.38 ? 86  GLY A O   1 
ATOM   691  N  N   . THR A 1 87  ? -18.064 13.520  23.399  1.00  20.57 ? 87  THR A N   1 
ATOM   692  C  CA  . THR A 1 87  ? -18.508 12.889  22.216  1.00  20.84 ? 87  THR A CA  1 
ATOM   693  C  C   . THR A 1 87  ? -17.372 12.676  21.280  1.00  16.18 ? 87  THR A C   1 
ATOM   694  O  O   . THR A 1 87  ? -16.445 13.500  21.160  1.00  15.21 ? 87  THR A O   1 
ATOM   695  C  CB  . THR A 1 87  ? -19.779 13.459  21.550  1.00  30.48 ? 87  THR A CB  1 
ATOM   696  O  OG1 . THR A 1 87  ? -19.557 13.899  20.193  1.00  32.97 ? 87  THR A OG1 1 
ATOM   697  C  CG2 . THR A 1 87  ? -20.507 14.470  22.426  1.00  27.46 ? 87  THR A CG2 1 
ATOM   698  N  N   . TYR A 1 88  ? -17.418 11.487  20.697  1.00  13.72 ? 88  TYR A N   1 
ATOM   699  C  CA  . TYR A 1 88  ? -16.286 11.064  19.861  1.00  12.00 ? 88  TYR A CA  1 
ATOM   700  C  C   . TYR A 1 88  ? -16.725 10.753  18.464  1.00  11.95 ? 88  TYR A C   1 
ATOM   701  O  O   . TYR A 1 88  ? -17.705 10.010  18.305  1.00  14.52 ? 88  TYR A O   1 
ATOM   702  C  CB  . TYR A 1 88  ? -15.614 9.845   20.487  1.00  11.04 ? 88  TYR A CB  1 
ATOM   703  C  CG  . TYR A 1 88  ? -14.866 10.047  21.781  1.00  10.72 ? 88  TYR A CG  1 
ATOM   704  C  CD1 . TYR A 1 88  ? -15.544 10.331  22.955  1.00  11.51 ? 88  TYR A CD1 1 
ATOM   705  C  CD2 . TYR A 1 88  ? -13.486 9.888   21.838  1.00  10.90 ? 88  TYR A CD2 1 
ATOM   706  C  CE1 . TYR A 1 88  ? -14.864 10.490  24.146  1.00  10.33 ? 88  TYR A CE1 1 
ATOM   707  C  CE2 . TYR A 1 88  ? -12.798 10.045  23.021  1.00  9.88  ? 88  TYR A CE2 1 
ATOM   708  C  CZ  . TYR A 1 88  ? -13.487 10.346  24.169  1.00  9.73  ? 88  TYR A CZ  1 
ATOM   709  O  OH  . TYR A 1 88  ? -12.776 10.498  25.335  1.00  10.62 ? 88  TYR A OH  1 
ATOM   710  N  N   . ARG A 1 89  ? -16.067 11.292  17.427  1.00  12.16 ? 89  ARG A N   1 
ATOM   711  C  CA  . ARG A 1 89  ? -16.452 11.124  16.011  1.00  12.20 ? 89  ARG A CA  1 
ATOM   712  C  C   . ARG A 1 89  ? -15.811 9.991   15.372  1.00  9.49  ? 89  ARG A C   1 
ATOM   713  O  O   . ARG A 1 89  ? -14.544 9.857   15.458  1.00  8.82  ? 89  ARG A O   1 
ATOM   714  C  CB  . ARG A 1 89  ? -16.083 12.347  15.162  1.00  14.44 ? 89  ARG A CB  1 
ATOM   715  C  CG  . ARG A 1 89  ? -17.004 13.514  15.387  1.00  17.45 ? 89  ARG A CG  1 
ATOM   716  C  CD  . ARG A 1 89  ? -16.655 14.540  14.313  1.00  18.13 ? 89  ARG A CD  1 
ATOM   717  N  NE  . ARG A 1 89  ? -17.390 15.740  14.670  1.00  20.50 ? 89  ARG A NE  1 
ATOM   718  C  CZ  . ARG A 1 89  ? -17.056 16.966  14.309  1.00  21.88 ? 89  ARG A CZ  1 
ATOM   719  N  NH1 . ARG A 1 89  ? -15.998 17.171  13.541  1.00  18.56 ? 89  ARG A NH1 1 
ATOM   720  N  NH2 . ARG A 1 89  ? -17.800 17.985  14.707  1.00  28.08 ? 89  ARG A NH2 1 
ATOM   721  N  N   . LEU A 1 90  ? -16.610 9.140   14.699  1.00  9.19  ? 90  LEU A N   1 
ATOM   722  C  CA  . LEU A 1 90  ? -15.998 8.035   13.940  1.00  9.92  ? 90  LEU A CA  1 
ATOM   723  C  C   . LEU A 1 90  ? -15.131 8.588   12.784  1.00  9.97  ? 90  LEU A C   1 
ATOM   724  O  O   . LEU A 1 90  ? -15.662 9.382   11.909  1.00  12.80 ? 90  LEU A O   1 
ATOM   725  C  CB  . LEU A 1 90  ? -17.084 7.168   13.300  1.00  10.73 ? 90  LEU A CB  1 
ATOM   726  C  CG  . LEU A 1 90  ? -16.591 5.999   12.414  1.00  10.21 ? 90  LEU A CG  1 
ATOM   727  C  CD1 . LEU A 1 90  ? -15.904 4.931   13.213  1.00  11.37 ? 90  LEU A CD1 1 
ATOM   728  C  CD2 . LEU A 1 90  ? -17.846 5.313   11.853  1.00  12.75 ? 90  LEU A CD2 1 
ATOM   729  N  N   . ILE A 1 91  ? -13.855 8.214   12.707  1.00  9.19  ? 91  ILE A N   1 
ATOM   730  C  CA  . ILE A 1 91  ? -12.991 8.573   11.600  1.00  10.12 ? 91  ILE A CA  1 
ATOM   731  C  C   . ILE A 1 91  ? -12.713 7.397   10.710  1.00  9.46  ? 91  ILE A C   1 
ATOM   732  O  O   . ILE A 1 91  ? -12.688 7.611   9.468   1.00  10.19 ? 91  ILE A O   1 
ATOM   733  C  CB  . ILE A 1 91  ? -11.615 9.163   12.063  1.00  10.52 ? 91  ILE A CB  1 
ATOM   734  C  CG1 . ILE A 1 91  ? -10.724 9.577   10.856  1.00  10.91 ? 91  ILE A CG1 1 
ATOM   735  C  CG2 . ILE A 1 91  ? -10.939 8.323   13.101  1.00  10.96 ? 91  ILE A CG2 1 
ATOM   736  C  CD1 . ILE A 1 91  ? -9.538  10.403  11.286  1.00  14.11 ? 91  ILE A CD1 1 
ATOM   737  N  N   . GLN A 1 92  ? -12.569 6.155   11.176  1.00  8.57  ? 92  GLN A N   1 
ATOM   738  C  CA  . GLN A 1 92  ? -12.314 5.007   10.305  1.00  9.47  ? 92  GLN A CA  1 
ATOM   739  C  C   . GLN A 1 92  ? -12.534 3.732   11.006  1.00  8.38  ? 92  GLN A C   1 
ATOM   740  O  O   . GLN A 1 92  ? -12.592 3.788   12.267  1.00  7.77  ? 92  GLN A O   1 
ATOM   741  C  CB  . GLN A 1 92  ? -10.898 5.025   9.788   1.00  11.08 ? 92  GLN A CB  1 
ATOM   742  C  CG  . GLN A 1 92  ? -9.765  4.982   10.862  1.00  11.56 ? 92  GLN A CG  1 
ATOM   743  C  CD  . GLN A 1 92  ? -9.045  3.646   10.899  1.00  13.67 ? 92  GLN A CD  1 
ATOM   744  O  OE1 . GLN A 1 92  ? -9.626  2.679   11.187  1.00  11.11 ? 92  GLN A OE1 1 
ATOM   745  N  NE2 . GLN A 1 92  ? -7.914  3.561   10.238  1.00  20.29 ? 92  GLN A NE2 1 
ATOM   746  N  N   . PHE A 1 93  ? -12.694 2.629   10.330  1.00  8.55  ? 93  PHE A N   1 
ATOM   747  C  CA  . PHE A 1 93  ? -12.555 1.328   10.942  1.00  8.22  ? 93  PHE A CA  1 
ATOM   748  C  C   . PHE A 1 93  ? -11.579 0.489   10.171  1.00  7.77  ? 93  PHE A C   1 
ATOM   749  O  O   . PHE A 1 93  ? -11.368 0.680   8.964   1.00  9.16  ? 93  PHE A O   1 
ATOM   750  C  CB  . PHE A 1 93  ? -13.919 0.615   11.168  1.00  9.30  ? 93  PHE A CB  1 
ATOM   751  C  CG  . PHE A 1 93  ? -14.638 0.135   9.922   1.00  10.19 ? 93  PHE A CG  1 
ATOM   752  C  CD1 . PHE A 1 93  ? -14.253 -1.026  9.264   1.00  10.39 ? 93  PHE A CD1 1 
ATOM   753  C  CD2 . PHE A 1 93  ? -15.730 0.875   9.489   1.00  9.81  ? 93  PHE A CD2 1 
ATOM   754  C  CE1 . PHE A 1 93  ? -14.965 -1.453  8.130   1.00  10.88 ? 93  PHE A CE1 1 
ATOM   755  C  CE2 . PHE A 1 93  ? -16.452 0.422   8.357   1.00  11.63 ? 93  PHE A CE2 1 
ATOM   756  C  CZ  . PHE A 1 93  ? -16.060 -0.727  7.724   1.00  11.44 ? 93  PHE A CZ  1 
ATOM   757  N  N   . HIS A 1 94  ? -11.011 -0.509  10.808  1.00  6.87  ? 94  HIS A N   1 
ATOM   758  C  CA  . HIS A 1 94  ? -10.178 -1.497  10.232  1.00  6.37  ? 94  HIS A CA  1 
ATOM   759  C  C   . HIS A 1 94  ? -10.171 -2.765  10.965  1.00  7.93  ? 94  HIS A C   1 
ATOM   760  O  O   . HIS A 1 94  ? -10.878 -2.795  12.026  1.00  6.66  ? 94  HIS A O   1 
ATOM   761  C  CB  . HIS A 1 94  ? -8.704  -1.002  10.143  1.00  6.33  ? 94  HIS A CB  1 
ATOM   762  C  CG  . HIS A 1 94  ? -8.161  -0.711  11.530  1.00  6.69  ? 94  HIS A CG  1 
ATOM   763  N  ND1 . HIS A 1 94  ? -8.345  0.471   12.136  1.00  6.94  ? 94  HIS A ND1 1 
ATOM   764  C  CD2 . HIS A 1 94  ? -7.551  -1.551  12.351  1.00  6.79  ? 94  HIS A CD2 1 
ATOM   765  C  CE1 . HIS A 1 94  ? -7.802  0.333   13.412  1.00  6.37  ? 94  HIS A CE1 1 
ATOM   766  N  NE2 . HIS A 1 94  ? -7.335  -0.898  13.558  1.00  5.87  ? 94  HIS A NE2 1 
ATOM   767  N  N   . PHE A 1 95  ? -9.508  -3.791  10.543  1.00  8.09  ? 95  PHE A N   1 
ATOM   768  C  CA  . PHE A 1 95  ? -9.465  -5.084  11.203  1.00  7.72  ? 95  PHE A CA  1 
ATOM   769  C  C   . PHE A 1 95  ? -8.068  -5.571  11.390  1.00  7.74  ? 95  PHE A C   1 
ATOM   770  O  O   . PHE A 1 95  ? -7.122  -5.055  10.740  1.00  8.28  ? 95  PHE A O   1 
ATOM   771  C  CB  . PHE A 1 95  ? -10.185 -6.194  10.360  1.00  8.44  ? 95  PHE A CB  1 
ATOM   772  C  CG  . PHE A 1 95  ? -11.646 -5.870  10.048  1.00  7.29  ? 95  PHE A CG  1 
ATOM   773  C  CD1 . PHE A 1 95  ? -12.026 -5.060  8.943   1.00  8.67  ? 95  PHE A CD1 1 
ATOM   774  C  CD2 . PHE A 1 95  ? -12.632 -6.561  10.726  1.00  8.74  ? 95  PHE A CD2 1 
ATOM   775  C  CE1 . PHE A 1 95  ? -13.390 -4.880  8.687   1.00  8.74  ? 95  PHE A CE1 1 
ATOM   776  C  CE2 . PHE A 1 95  ? -13.993 -6.344  10.468  1.00  8.75  ? 95  PHE A CE2 1 
ATOM   777  C  CZ  . PHE A 1 95  ? -14.383 -5.518  9.414   1.00  9.17  ? 95  PHE A CZ  1 
ATOM   778  N  N   . HIS A 1 96  ? -7.894  -6.487  12.332  1.00  7.77  ? 96  HIS A N   1 
ATOM   779  C  CA  . HIS A 1 96  ? -6.678  -7.284  12.464  1.00  7.14  ? 96  HIS A CA  1 
ATOM   780  C  C   . HIS A 1 96  ? -7.093  -8.703  12.309  1.00  8.38  ? 96  HIS A C   1 
ATOM   781  O  O   . HIS A 1 96  ? -8.161  -9.098  12.839  1.00  8.78  ? 96  HIS A O   1 
ATOM   782  C  CB  . HIS A 1 96  ? -6.003  -7.058  13.856  1.00  7.32  ? 96  HIS A CB  1 
ATOM   783  C  CG  . HIS A 1 96  ? -5.724  -5.598  14.106  1.00  6.38  ? 96  HIS A CG  1 
ATOM   784  N  ND1 . HIS A 1 96  ? -4.476  -5.051  13.943  1.00  6.85  ? 96  HIS A ND1 1 
ATOM   785  C  CD2 . HIS A 1 96  ? -6.550  -4.547  14.495  1.00  6.75  ? 96  HIS A CD2 1 
ATOM   786  C  CE1 . HIS A 1 96  ? -4.513  -3.748  14.247  1.00  7.86  ? 96  HIS A CE1 1 
ATOM   787  N  NE2 . HIS A 1 96  ? -5.839  -3.430  14.553  1.00  7.40  ? 96  HIS A NE2 1 
ATOM   788  N  N   . TRP A 1 97  ? -6.312  -9.551  11.698  1.00  7.67  ? 97  TRP A N   1 
ATOM   789  C  CA  . TRP A 1 97  ? -6.710  -10.945 11.472  1.00  8.29  ? 97  TRP A CA  1 
ATOM   790  C  C   . TRP A 1 97  ? -5.506  -11.884 11.335  1.00  7.32  ? 97  TRP A C   1 
ATOM   791  O  O   . TRP A 1 97  ? -4.320  -11.443 11.242  1.00  9.17  ? 97  TRP A O   1 
ATOM   792  C  CB  . TRP A 1 97  ? -7.588  -11.107 10.195  1.00  8.84  ? 97  TRP A CB  1 
ATOM   793  C  CG  . TRP A 1 97  ? -6.967  -10.674 8.902   1.00  8.46  ? 97  TRP A CG  1 
ATOM   794  C  CD1 . TRP A 1 97  ? -6.240  -11.518 8.089   1.00  9.21  ? 97  TRP A CD1 1 
ATOM   795  C  CD2 . TRP A 1 97  ? -6.912  -9.354  8.419   1.00  7.96  ? 97  TRP A CD2 1 
ATOM   796  N  NE1 . TRP A 1 97  ? -5.835  -10.747 6.992   1.00  10.02 ? 97  TRP A NE1 1 
ATOM   797  C  CE2 . TRP A 1 97  ? -6.144  -9.439  7.162   1.00  8.02  ? 97  TRP A CE2 1 
ATOM   798  C  CE3 . TRP A 1 97  ? -7.435  -8.108  8.821   1.00  8.38  ? 97  TRP A CE3 1 
ATOM   799  C  CZ2 . TRP A 1 97  ? -5.938  -8.342  6.341   1.00  9.51  ? 97  TRP A CZ2 1 
ATOM   800  C  CZ3 . TRP A 1 97  ? -7.147  -6.953  7.988   1.00  9.51  ? 97  TRP A CZ3 1 
ATOM   801  C  CH2 . TRP A 1 97  ? -6.416  -7.087  6.767   1.00  9.30  ? 97  TRP A CH2 1 
ATOM   802  N  N   . GLY A 1 98  ? -5.791  -13.200 11.368  1.00  7.93  ? 98  GLY A N   1 
ATOM   803  C  CA  . GLY A 1 98  ? -4.745  -14.204 11.353  1.00  9.39  ? 98  GLY A CA  1 
ATOM   804  C  C   . GLY A 1 98  ? -4.525  -14.910 10.012  1.00  9.53  ? 98  GLY A C   1 
ATOM   805  O  O   . GLY A 1 98  ? -5.280  -14.724 9.049   1.00  10.72 ? 98  GLY A O   1 
ATOM   806  N  N   . SER A 1 99  ? -3.505  -15.772 10.091  1.00  11.09 ? 99  SER A N   1 
ATOM   807  C  CA  . SER A 1 99  ? -3.248  -16.709 8.966   1.00  12.13 ? 99  SER A CA  1 
ATOM   808  C  C   . SER A 1 99  ? -4.120  -17.938 9.085   1.00  13.40 ? 99  SER A C   1 
ATOM   809  O  O   . SER A 1 99  ? -4.184  -18.692 8.075   1.00  16.91 ? 99  SER A O   1 
ATOM   810  C  CB  . SER A 1 99  ? -1.745  -17.056 8.967   1.00  12.36 ? 99  SER A CB  1 
ATOM   811  O  OG  . SER A 1 99  ? -1.365  -17.577 10.215  1.00  14.13 ? 99  SER A OG  1 
ATOM   812  N  N   . LEU A 1 100 ? -4.797  -18.155 10.237  1.00  13.98 ? 100 LEU A N   1 
ATOM   813  C  CA  . LEU A 1 100 ? -5.578  -19.322 10.540  1.00  15.80 ? 100 LEU A CA  1 
ATOM   814  C  C   . LEU A 1 100 ? -6.735  -18.875 11.383  1.00  14.19 ? 100 LEU A C   1 
ATOM   815  O  O   . LEU A 1 100 ? -6.638  -17.857 12.134  1.00  12.15 ? 100 LEU A O   1 
ATOM   816  C  CB  . LEU A 1 100 ? -4.748  -20.248 11.492  1.00  21.50 ? 100 LEU A CB  1 
ATOM   817  C  CG  . LEU A 1 100 ? -3.470  -20.814 10.904  1.00  25.90 ? 100 LEU A CG  1 
ATOM   818  C  CD1 . LEU A 1 100 ? -2.389  -20.784 11.953  1.00  29.16 ? 100 LEU A CD1 1 
ATOM   819  C  CD2 . LEU A 1 100 ? -3.736  -22.239 10.386  1.00  28.82 ? 100 LEU A CD2 1 
ATOM   820  N  N   . ASP A 1 101 ? -7.845  -19.581 11.306  1.00  12.32 ? 101 ASP A N   1 
ATOM   821  C  CA  . ASP A 1 101 ? -9.031  -19.148 12.144  1.00  11.91 ? 101 ASP A CA  1 
ATOM   822  C  C   . ASP A 1 101 ? -8.748  -19.073 13.635  1.00  11.73 ? 101 ASP A C   1 
ATOM   823  O  O   . ASP A 1 101 ? -9.422  -18.327 14.333  1.00  15.02 ? 101 ASP A O   1 
ATOM   824  C  CB  . ASP A 1 101 ? -10.259 -20.032 11.843  1.00  13.37 ? 101 ASP A CB  1 
ATOM   825  C  CG  . ASP A 1 101 ? -10.686 -19.965 10.389  1.00  16.82 ? 101 ASP A CG  1 
ATOM   826  O  OD1 . ASP A 1 101 ? -10.209 -19.064 9.668   1.00  15.35 ? 101 ASP A OD1 1 
ATOM   827  O  OD2 . ASP A 1 101 ? -11.500 -20.815 9.967   1.00  21.79 ? 101 ASP A OD2 1 
ATOM   828  N  N   . GLY A 1 102 ? -7.746  -19.836 14.136  1.00  11.33 ? 102 GLY A N   1 
ATOM   829  C  CA  . GLY A 1 102 ? -7.400  -19.867 15.568  1.00  12.35 ? 102 GLY A CA  1 
ATOM   830  C  C   . GLY A 1 102 ? -6.649  -18.679 16.152  1.00  11.29 ? 102 GLY A C   1 
ATOM   831  O  O   . GLY A 1 102 ? -6.320  -18.655 17.337  1.00  13.19 ? 102 GLY A O   1 
ATOM   832  N  N   . GLN A 1 103 ? -6.381  -17.684 15.333  1.00  11.06 ? 103 GLN A N   1 
ATOM   833  C  CA  . GLN A 1 103 ? -5.666  -16.473 15.845  1.00  10.42 ? 103 GLN A CA  1 
ATOM   834  C  C   . GLN A 1 103 ? -6.025  -15.330 14.972  1.00  9.19  ? 103 GLN A C   1 
ATOM   835  O  O   . GLN A 1 103 ? -6.571  -15.487 13.868  1.00  10.04 ? 103 GLN A O   1 
ATOM   836  C  CB  . GLN A 1 103 ? -4.109  -16.701 15.862  1.00  11.43 ? 103 GLN A CB  1 
ATOM   837  C  CG  . GLN A 1 103 ? -3.540  -16.929 14.446  1.00  12.49 ? 103 GLN A CG  1 
ATOM   838  C  CD  . GLN A 1 103 ? -2.169  -17.504 14.560  1.00  17.10 ? 103 GLN A CD  1 
ATOM   839  O  OE1 . GLN A 1 103 ? -1.931  -18.448 15.336  1.00  20.48 ? 103 GLN A OE1 1 
ATOM   840  N  NE2 . GLN A 1 103 ? -1.273  -16.990 13.796  1.00  15.72 ? 103 GLN A NE2 1 
ATOM   841  N  N   . GLY A 1 104 ? -5.654  -14.107 15.425  1.00  9.23  ? 104 GLY A N   1 
ATOM   842  C  CA  . GLY A 1 104 ? -5.916  -12.943 14.614  1.00  8.06  ? 104 GLY A CA  1 
ATOM   843  C  C   . GLY A 1 104 ? -6.334  -11.705 15.422  1.00  7.70  ? 104 GLY A C   1 
ATOM   844  O  O   . GLY A 1 104 ? -6.100  -10.550 15.135  1.00  8.39  ? 104 GLY A O   1 
ATOM   845  N  N   . SER A 1 105 ? -7.089  -11.968 16.551  1.00  6.90  ? 105 SER A N   1 
ATOM   846  C  CA  . SER A 1 105 ? -7.527  -10.851 17.433  1.00  8.04  ? 105 SER A CA  1 
ATOM   847  C  C   . SER A 1 105 ? -6.314  -10.329 18.243  1.00  7.07  ? 105 SER A C   1 
ATOM   848  O  O   . SER A 1 105 ? -5.244  -10.984 18.396  1.00  7.85  ? 105 SER A O   1 
ATOM   849  C  CB  . SER A 1 105 ? -8.629  -11.254 18.403  1.00  8.06  ? 105 SER A CB  1 
ATOM   850  O  OG  . SER A 1 105 ? -8.243  -12.182 19.336  1.00  8.12  ? 105 SER A OG  1 
ATOM   851  N  N   . GLU A 1 106 ? -6.431  -9.068  18.583  1.00  6.60  ? 106 GLU A N   1 
ATOM   852  C  CA  . GLU A 1 106 ? -5.388  -8.391  19.445  1.00  6.47  ? 106 GLU A CA  1 
ATOM   853  C  C   . GLU A 1 106 ? -5.669  -8.560  20.921  1.00  7.22  ? 106 GLU A C   1 
ATOM   854  O  O   . GLU A 1 106 ? -4.940  -9.156  21.649  1.00  7.82  ? 106 GLU A O   1 
ATOM   855  C  CB  . GLU A 1 106 ? -5.304  -6.910  19.015  1.00  6.77  ? 106 GLU A CB  1 
ATOM   856  C  CG  . GLU A 1 106 ? -4.984  -6.774  17.512  1.00  7.73  ? 106 GLU A CG  1 
ATOM   857  C  CD  . GLU A 1 106 ? -4.274  -5.522  17.283  1.00  7.63  ? 106 GLU A CD  1 
ATOM   858  O  OE1 . GLU A 1 106 ? -4.784  -4.435  17.477  1.00  7.07  ? 106 GLU A OE1 1 
ATOM   859  O  OE2 . GLU A 1 106 ? -3.061  -5.536  16.871  1.00  9.02  ? 106 GLU A OE2 1 
ATOM   860  N  N   . HIS A 1 107 ? -6.908  -8.160  21.315  1.00  6.89  ? 107 HIS A N   1 
ATOM   861  C  CA  . HIS A 1 107 ? -7.364  -8.514  22.665  1.00  6.32  ? 107 HIS A CA  1 
ATOM   862  C  C   . HIS A 1 107 ? -7.681  -9.992  22.685  1.00  7.36  ? 107 HIS A C   1 
ATOM   863  O  O   . HIS A 1 107 ? -8.002  -10.594 21.613  1.00  7.71  ? 107 HIS A O   1 
ATOM   864  C  CB  . HIS A 1 107 ? -8.614  -7.735  23.007  1.00  6.51  ? 107 HIS A CB  1 
ATOM   865  C  CG  . HIS A 1 107 ? -8.337  -6.260  23.170  1.00  6.05  ? 107 HIS A CG  1 
ATOM   866  N  ND1 . HIS A 1 107 ? -8.411  -5.344  22.162  1.00  6.15  ? 107 HIS A ND1 1 
ATOM   867  C  CD2 . HIS A 1 107 ? -7.864  -5.544  24.270  1.00  6.43  ? 107 HIS A CD2 1 
ATOM   868  C  CE1 . HIS A 1 107 ? -7.964  -4.171  22.537  1.00  6.06  ? 107 HIS A CE1 1 
ATOM   869  N  NE2 . HIS A 1 107 ? -7.639  -4.257  23.877  1.00  6.57  ? 107 HIS A NE2 1 
ATOM   870  N  N   . THR A 1 108 ? -7.534  -10.588 23.823  1.00  8.12  ? 108 THR A N   1 
ATOM   871  C  CA  . THR A 1 108 ? -7.965  -11.964 24.064  1.00  8.40  ? 108 THR A CA  1 
ATOM   872  C  C   . THR A 1 108 ? -8.938  -11.982 25.256  1.00  7.93  ? 108 THR A C   1 
ATOM   873  O  O   . THR A 1 108 ? -8.943  -11.031 26.024  1.00  9.26  ? 108 THR A O   1 
ATOM   874  C  CB  . THR A 1 108 ? -6.735  -12.866 24.256  1.00  8.64  ? 108 THR A CB  1 
ATOM   875  O  OG1 . THR A 1 108 ? -5.956  -12.393 25.343  1.00  9.16  ? 108 THR A OG1 1 
ATOM   876  C  CG2 . THR A 1 108 ? -5.854  -12.983 23.001  1.00  8.90  ? 108 THR A CG2 1 
ATOM   877  N  N   . VAL A 1 109 ? -9.695  -13.068 25.355  1.00  8.38  ? 109 VAL A N   1 
ATOM   878  C  CA  . VAL A 1 109 ? -10.702 -13.184 26.473  1.00  10.35 ? 109 VAL A CA  1 
ATOM   879  C  C   . VAL A 1 109 ? -10.376 -14.488 27.159  1.00  11.71 ? 109 VAL A C   1 
ATOM   880  O  O   . VAL A 1 109 ? -10.450 -15.532 26.562  1.00  11.88 ? 109 VAL A O   1 
ATOM   881  C  CB  . VAL A 1 109 ? -12.120 -13.208 25.894  1.00  12.76 ? 109 VAL A CB  1 
ATOM   882  C  CG1 . VAL A 1 109 ? -13.187 -13.349 27.005  1.00  13.52 ? 109 VAL A CG1 1 
ATOM   883  C  CG2 . VAL A 1 109 ? -12.414 -11.917 25.063  1.00  12.31 ? 109 VAL A CG2 1 
ATOM   884  N  N   . ASP A 1 110 ? -9.919  -14.357 28.392  1.00  10.84 ? 110 ASP A N   1 
ATOM   885  C  CA  . ASP A 1 110 ? -9.440  -15.592 29.126  1.00  12.80 ? 110 ASP A CA  1 
ATOM   886  C  C   . ASP A 1 110 ? -8.481  -16.390 28.268  1.00  12.25 ? 110 ASP A C   1 
ATOM   887  O  O   . ASP A 1 110 ? -8.509  -17.637 28.204  1.00  13.03 ? 110 ASP A O   1 
ATOM   888  C  CB  . ASP A 1 110 ? -10.634 -16.457 29.579  1.00  13.76 ? 110 ASP A CB  1 
ATOM   889  C  CG  . ASP A 1 110 ? -11.547 -15.688 30.542  1.00  13.87 ? 110 ASP A CG  1 
ATOM   890  O  OD1 . ASP A 1 110 ? -10.990 -14.915 31.292  1.00  16.30 ? 110 ASP A OD1 1 
ATOM   891  O  OD2 . ASP A 1 110 ? -12.761 -15.951 30.535  1.00  18.76 ? 110 ASP A OD2 1 
ATOM   892  N  N   . LYS A 1 111 ? -7.582  -15.647 27.597  1.00  10.85 ? 111 LYS A N   1 
ATOM   893  C  CA  . LYS A 1 111 ? -6.448  -16.137 26.715  1.00  12.16 ? 111 LYS A CA  1 
ATOM   894  C  C   . LYS A 1 111 ? -6.953  -16.670 25.389  1.00  10.80 ? 111 LYS A C   1 
ATOM   895  O  O   . LYS A 1 111 ? -6.150  -17.048 24.530  1.00  12.80 ? 111 LYS A O   1 
ATOM   896  C  CB  . LYS A 1 111 ? -5.548  -17.158 27.415  1.00  15.88 ? 111 LYS A CB  1 
ATOM   897  C  CG  . LYS A 1 111 ? -5.024  -16.720 28.730  1.00  18.34 ? 111 LYS A CG  1 
ATOM   898  C  CD  . LYS A 1 111 ? -4.000  -15.697 28.497  1.00  18.93 ? 111 LYS A CD  1 
ATOM   899  C  CE  . LYS A 1 111 ? -3.394  -15.283 29.849  1.00  24.90 ? 111 LYS A CE  1 
ATOM   900  N  NZ  . LYS A 1 111 ? -1.936  -15.328 29.665  1.00  30.05 ? 111 LYS A NZ  1 
ATOM   901  N  N   . LYS A 1 112 ? -8.259  -16.648 25.142  1.00  10.34 ? 112 LYS A N   1 
ATOM   902  C  CA  . LYS A 1 112 ? -8.798  -17.125 23.854  1.00  10.57 ? 112 LYS A CA  1 
ATOM   903  C  C   . LYS A 1 112 ? -8.583  -16.007 22.819  1.00  11.80 ? 112 LYS A C   1 
ATOM   904  O  O   . LYS A 1 112 ? -8.939  -14.830 23.023  1.00  11.23 ? 112 LYS A O   1 
ATOM   905  C  CB  . LYS A 1 112 ? -10.322 -17.420 23.945  1.00  15.14 ? 112 LYS A CB  1 
ATOM   906  C  CG  . LYS A 1 112 ? -11.150 -17.428 22.663  1.00  17.66 ? 112 LYS A CG  1 
ATOM   907  C  CD  . LYS A 1 112 ? -12.668 -17.592 23.032  1.00  22.34 ? 112 LYS A CD  1 
ATOM   908  C  CE  . LYS A 1 112 ? -13.578 -17.996 21.842  1.00  31.46 ? 112 LYS A CE  1 
ATOM   909  N  NZ  . LYS A 1 112 ? -12.823 -18.303 20.622  1.00  32.11 ? 112 LYS A NZ  1 
ATOM   910  N  N   A LYS A 1 113 ? -8.111  -16.469 21.674  0.50  10.66 ? 113 LYS A N   1 
ATOM   911  N  N   B LYS A 1 113 ? -8.075  -16.431 21.682  0.50  10.83 ? 113 LYS A N   1 
ATOM   912  C  CA  A LYS A 1 113 ? -7.998  -15.695 20.431  0.50  10.45 ? 113 LYS A CA  1 
ATOM   913  C  CA  B LYS A 1 113 ? -7.877  -15.610 20.476  0.50  10.89 ? 113 LYS A CA  1 
ATOM   914  C  C   A LYS A 1 113 ? -9.163  -15.910 19.507  0.50  9.18  ? 113 LYS A C   1 
ATOM   915  C  C   B LYS A 1 113 ? -8.988  -15.859 19.474  0.50  9.49  ? 113 LYS A C   1 
ATOM   916  O  O   A LYS A 1 113 ? -9.689  -17.044 19.347  0.50  9.74  ? 113 LYS A O   1 
ATOM   917  O  O   B LYS A 1 113 ? -9.238  -17.006 19.155  0.50  10.59 ? 113 LYS A O   1 
ATOM   918  C  CB  A LYS A 1 113 ? -6.695  -16.005 19.688  0.50  10.18 ? 113 LYS A CB  1 
ATOM   919  C  CB  B LYS A 1 113 ? -6.531  -15.991 19.835  0.50  10.33 ? 113 LYS A CB  1 
ATOM   920  C  CG  A LYS A 1 113 ? -5.433  -15.845 20.506  0.50  10.37 ? 113 LYS A CG  1 
ATOM   921  C  CG  B LYS A 1 113 ? -5.316  -15.443 20.552  0.50  10.48 ? 113 LYS A CG  1 
ATOM   922  C  CD  A LYS A 1 113 ? -4.197  -16.283 19.697  0.50  11.19 ? 113 LYS A CD  1 
ATOM   923  C  CD  B LYS A 1 113 ? -4.035  -16.185 20.228  0.50  10.77 ? 113 LYS A CD  1 
ATOM   924  C  CE  A LYS A 1 113 ? -2.886  -15.818 20.335  0.50  11.67 ? 113 LYS A CE  1 
ATOM   925  C  CE  B LYS A 1 113 ? -2.869  -15.463 20.859  0.50  11.52 ? 113 LYS A CE  1 
ATOM   926  N  NZ  A LYS A 1 113 ? -2.539  -16.438 21.657  0.50  14.26 ? 113 LYS A NZ  1 
ATOM   927  N  NZ  B LYS A 1 113 ? -1.730  -16.309 20.471  0.50  13.48 ? 113 LYS A NZ  1 
ATOM   928  N  N   . TYR A 1 114 ? -9.610  -14.782 18.971  1.00  9.20  ? 114 TYR A N   1 
ATOM   929  C  CA  . TYR A 1 114 ? -10.626 -14.806 17.951  1.00  8.44  ? 114 TYR A CA  1 
ATOM   930  C  C   . TYR A 1 114 ? -9.997  -14.778 16.527  1.00  7.69  ? 114 TYR A C   1 
ATOM   931  O  O   . TYR A 1 114 ? -8.781  -14.493 16.434  1.00  8.80  ? 114 TYR A O   1 
ATOM   932  C  CB  . TYR A 1 114 ? -11.640 -13.697 18.136  1.00  10.22 ? 114 TYR A CB  1 
ATOM   933  C  CG  . TYR A 1 114 ? -12.609 -13.972 19.258  1.00  10.69 ? 114 TYR A CG  1 
ATOM   934  C  CD1 . TYR A 1 114 ? -12.299 -13.604 20.554  1.00  10.86 ? 114 TYR A CD1 1 
ATOM   935  C  CD2 . TYR A 1 114 ? -13.840 -14.582 19.021  1.00  11.23 ? 114 TYR A CD2 1 
ATOM   936  C  CE1 . TYR A 1 114 ? -13.177 -13.832 21.589  1.00  13.15 ? 114 TYR A CE1 1 
ATOM   937  C  CE2 . TYR A 1 114 ? -14.726 -14.817 20.062  1.00  13.54 ? 114 TYR A CE2 1 
ATOM   938  C  CZ  . TYR A 1 114 ? -14.380 -14.438 21.345  1.00  13.42 ? 114 TYR A CZ  1 
ATOM   939  O  OH  . TYR A 1 114 ? -15.222 -14.646 22.411  1.00  19.88 ? 114 TYR A OH  1 
ATOM   940  N  N   . ALA A 1 115 ? -10.706 -15.042 15.455  1.00  8.16  ? 115 ALA A N   1 
ATOM   941  C  CA  . ALA A 1 115 ? -10.121 -15.032 14.081  1.00  8.91  ? 115 ALA A CA  1 
ATOM   942  C  C   . ALA A 1 115 ? -9.749  -13.675 13.649  1.00  8.67  ? 115 ALA A C   1 
ATOM   943  O  O   . ALA A 1 115 ? -8.911  -13.494 12.736  1.00  9.10  ? 115 ALA A O   1 
ATOM   944  C  CB  . ALA A 1 115 ? -11.140 -15.688 13.126  1.00  9.89  ? 115 ALA A CB  1 
ATOM   945  N  N   . ALA A 1 116 ? -10.418 -12.660 14.227  1.00  8.15  ? 116 ALA A N   1 
ATOM   946  C  CA  . ALA A 1 116 ? -10.109 -11.314 13.769  1.00  7.77  ? 116 ALA A CA  1 
ATOM   947  C  C   . ALA A 1 116 ? -10.684 -10.343 14.802  1.00  6.97  ? 116 ALA A C   1 
ATOM   948  O  O   . ALA A 1 116 ? -11.472 -10.734 15.727  1.00  7.32  ? 116 ALA A O   1 
ATOM   949  C  CB  . ALA A 1 116 ? -10.730 -10.987 12.413  1.00  8.57  ? 116 ALA A CB  1 
ATOM   950  N  N   . GLU A 1 117 ? -10.357 -9.075  14.674  1.00  6.86  ? 117 GLU A N   1 
ATOM   951  C  CA  . GLU A 1 117 ? -10.906 -8.034  15.547  1.00  6.73  ? 117 GLU A CA  1 
ATOM   952  C  C   . GLU A 1 117 ? -11.117 -6.797  14.735  1.00  7.15  ? 117 GLU A C   1 
ATOM   953  O  O   . GLU A 1 117 ? -10.231 -6.331  14.013  1.00  8.44  ? 117 GLU A O   1 
ATOM   954  C  CB  . GLU A 1 117 ? -9.947  -7.754  16.733  1.00  7.52  ? 117 GLU A CB  1 
ATOM   955  C  CG  . GLU A 1 117 ? -10.513 -6.871  17.876  1.00  7.39  ? 117 GLU A CG  1 
ATOM   956  C  CD  . GLU A 1 117 ? -9.534  -6.775  19.078  1.00  7.16  ? 117 GLU A CD  1 
ATOM   957  O  OE1 . GLU A 1 117 ? -8.891  -7.809  19.313  1.00  7.88  ? 117 GLU A OE1 1 
ATOM   958  O  OE2 . GLU A 1 117 ? -9.500  -5.661  19.703  1.00  7.73  ? 117 GLU A OE2 1 
ATOM   959  N  N   . LEU A 1 118 ? -12.292 -6.207  14.828  1.00  7.13  ? 118 LEU A N   1 
ATOM   960  C  CA  . LEU A 1 118 ? -12.698 -4.942  14.198  1.00  6.31  ? 118 LEU A CA  1 
ATOM   961  C  C   . LEU A 1 118 ? -12.500 -3.788  15.138  1.00  6.12  ? 118 LEU A C   1 
ATOM   962  O  O   . LEU A 1 118 ? -12.835 -3.887  16.341  1.00  7.01  ? 118 LEU A O   1 
ATOM   963  C  CB  . LEU A 1 118 ? -14.245 -5.032  13.891  1.00  7.10  ? 118 LEU A CB  1 
ATOM   964  C  CG  . LEU A 1 118 ? -14.982 -3.731  13.589  1.00  7.41  ? 118 LEU A CG  1 
ATOM   965  C  CD1 . LEU A 1 118 ? -14.429 -3.084  12.343  1.00  8.14  ? 118 LEU A CD1 1 
ATOM   966  C  CD2 . LEU A 1 118 ? -16.477 -4.070  13.344  1.00  8.34  ? 118 LEU A CD2 1 
ATOM   967  N  N   . HIS A 1 119 ? -11.860 -2.701  14.738  1.00  5.93  ? 119 HIS A N   1 
ATOM   968  C  CA  . HIS A 1 119 ? -11.646 -1.492  15.519  1.00  6.33  ? 119 HIS A CA  1 
ATOM   969  C  C   . HIS A 1 119 ? -12.349 -0.336  14.858  1.00  7.06  ? 119 HIS A C   1 
ATOM   970  O  O   . HIS A 1 119 ? -11.946 0.025   13.684  1.00  7.46  ? 119 HIS A O   1 
ATOM   971  C  CB  . HIS A 1 119 ? -10.124 -1.224  15.578  1.00  5.72  ? 119 HIS A CB  1 
ATOM   972  C  CG  . HIS A 1 119 ? -9.456  -2.184  16.467  1.00  5.52  ? 119 HIS A CG  1 
ATOM   973  N  ND1 . HIS A 1 119 ? -8.037  -2.393  16.431  1.00  5.47  ? 119 HIS A ND1 1 
ATOM   974  C  CD2 . HIS A 1 119 ? -9.966  -2.996  17.446  1.00  7.33  ? 119 HIS A CD2 1 
ATOM   975  C  CE1 . HIS A 1 119 ? -7.726  -3.285  17.347  1.00  6.72  ? 119 HIS A CE1 1 
ATOM   976  N  NE2 . HIS A 1 119 ? -8.901  -3.697  17.995  1.00  7.41  ? 119 HIS A NE2 1 
ATOM   977  N  N   . LEU A 1 120 ? -13.358 0.270   15.514  1.00  6.61  ? 120 LEU A N   1 
ATOM   978  C  CA  . LEU A 1 120 ? -13.998 1.474   15.027  1.00  7.35  ? 120 LEU A CA  1 
ATOM   979  C  C   . LEU A 1 120 ? -13.437 2.615   15.784  1.00  6.63  ? 120 LEU A C   1 
ATOM   980  O  O   . LEU A 1 120 ? -13.520 2.659   17.027  1.00  6.13  ? 120 LEU A O   1 
ATOM   981  C  CB  . LEU A 1 120 ? -15.504 1.354   15.265  1.00  7.31  ? 120 LEU A CB  1 
ATOM   982  C  CG  . LEU A 1 120 ? -16.182 0.268   14.392  1.00  8.39  ? 120 LEU A CG  1 
ATOM   983  C  CD1 . LEU A 1 120 ? -17.137 -0.595  15.227  1.00  11.20 ? 120 LEU A CD1 1 
ATOM   984  C  CD2 . LEU A 1 120 ? -16.998 0.986   13.287  1.00  10.18 ? 120 LEU A CD2 1 
ATOM   985  N  N   . VAL A 1 121 ? -12.658 3.457   15.137  1.00  7.15  ? 121 VAL A N   1 
ATOM   986  C  CA  . VAL A 1 121 ? -11.803 4.461   15.785  1.00  7.66  ? 121 VAL A CA  1 
ATOM   987  C  C   . VAL A 1 121 ? -12.511 5.781   15.829  1.00  8.37  ? 121 VAL A C   1 
ATOM   988  O  O   . VAL A 1 121 ? -12.929 6.284   14.750  1.00  8.59  ? 121 VAL A O   1 
ATOM   989  C  CB  . VAL A 1 121 ? -10.445 4.556   14.995  1.00  7.79  ? 121 VAL A CB  1 
ATOM   990  C  CG1 . VAL A 1 121 ? -9.590  5.668   15.601  1.00  7.84  ? 121 VAL A CG1 1 
ATOM   991  C  CG2 . VAL A 1 121 ? -9.669  3.211   14.823  1.00  7.44  ? 121 VAL A CG2 1 
ATOM   992  N  N   . HIS A 1 122 ? -12.651 6.385   17.000  1.00  7.34  ? 122 HIS A N   1 
ATOM   993  C  CA  . HIS A 1 122 ? -13.249 7.685   17.152  1.00  7.30  ? 122 HIS A CA  1 
ATOM   994  C  C   . HIS A 1 122 ? -12.386 8.636   17.914  1.00  8.38  ? 122 HIS A C   1 
ATOM   995  O  O   . HIS A 1 122 ? -11.588 8.251   18.774  1.00  9.22  ? 122 HIS A O   1 
ATOM   996  C  CB  . HIS A 1 122 ? -14.532 7.516   18.008  1.00  7.47  ? 122 HIS A CB  1 
ATOM   997  C  CG  . HIS A 1 122 ? -15.431 6.380   17.583  1.00  8.04  ? 122 HIS A CG  1 
ATOM   998  N  ND1 . HIS A 1 122 ? -15.138 5.092   17.832  1.00  7.72  ? 122 HIS A ND1 1 
ATOM   999  C  CD2 . HIS A 1 122 ? -16.673 6.390   16.951  1.00  8.87  ? 122 HIS A CD2 1 
ATOM   1000 C  CE1 . HIS A 1 122 ? -16.131 4.313   17.362  1.00  8.73  ? 122 HIS A CE1 1 
ATOM   1001 N  NE2 . HIS A 1 122 ? -17.069 5.106   16.823  1.00  9.12  ? 122 HIS A NE2 1 
ATOM   1002 N  N   . TRP A 1 123 ? -12.533 9.925   17.608  1.00  8.81  ? 123 TRP A N   1 
ATOM   1003 C  CA  . TRP A 1 123 ? -11.694 11.012  18.261  1.00  8.98  ? 123 TRP A CA  1 
ATOM   1004 C  C   . TRP A 1 123 ? -12.561 11.994  19.010  1.00  10.16 ? 123 TRP A C   1 
ATOM   1005 O  O   . TRP A 1 123 ? -13.667 12.359  18.556  1.00  9.95  ? 123 TRP A O   1 
ATOM   1006 C  CB  . TRP A 1 123 ? -10.660 11.664  17.375  1.00  9.78  ? 123 TRP A CB  1 
ATOM   1007 C  CG  . TRP A 1 123 ? -11.298 12.278  16.189  1.00  9.42  ? 123 TRP A CG  1 
ATOM   1008 C  CD1 . TRP A 1 123 ? -11.490 11.681  14.961  1.00  10.87 ? 123 TRP A CD1 1 
ATOM   1009 C  CD2 . TRP A 1 123 ? -11.759 13.631  16.047  1.00  9.85  ? 123 TRP A CD2 1 
ATOM   1010 N  NE1 . TRP A 1 123 ? -12.073 12.555  14.093  1.00  11.62 ? 123 TRP A NE1 1 
ATOM   1011 C  CE2 . TRP A 1 123 ? -12.211 13.776  14.646  1.00  10.70 ? 123 TRP A CE2 1 
ATOM   1012 C  CE3 . TRP A 1 123 ? -11.785 14.747  16.877  1.00  10.97 ? 123 TRP A CE3 1 
ATOM   1013 C  CZ2 . TRP A 1 123 ? -12.777 14.973  14.195  1.00  12.70 ? 123 TRP A CZ2 1 
ATOM   1014 C  CZ3 . TRP A 1 123 ? -12.329 15.935  16.366  1.00  11.72 ? 123 TRP A CZ3 1 
ATOM   1015 C  CH2 . TRP A 1 123 ? -12.798 16.046  15.043  1.00  12.59 ? 123 TRP A CH2 1 
ATOM   1016 N  N   . ASN A 1 124 ? -12.017 12.424  20.136  1.00  9.48  ? 124 ASN A N   1 
ATOM   1017 C  CA  . ASN A 1 124 ? -12.766 13.350  21.035  1.00  10.47 ? 124 ASN A CA  1 
ATOM   1018 C  C   . ASN A 1 124 ? -12.902 14.727  20.421  1.00  10.73 ? 124 ASN A C   1 
ATOM   1019 O  O   . ASN A 1 124 ? -11.892 15.407  20.097  1.00  10.82 ? 124 ASN A O   1 
ATOM   1020 C  CB  . ASN A 1 124 ? -11.967 13.454  22.326  1.00  9.98  ? 124 ASN A CB  1 
ATOM   1021 C  CG  . ASN A 1 124 ? -12.775 14.043  23.488  1.00  12.24 ? 124 ASN A CG  1 
ATOM   1022 O  OD1 . ASN A 1 124 ? -13.580 14.914  23.266  1.00  14.09 ? 124 ASN A OD1 1 
ATOM   1023 N  ND2 . ASN A 1 124 ? -12.547 13.531  24.713  1.00  12.97 ? 124 ASN A ND2 1 
ATOM   1024 N  N   . THR A 1 125 ? -14.147 15.143  20.203  1.00  12.02 ? 125 THR A N   1 
ATOM   1025 C  CA  . THR A 1 125 ? -14.394 16.433  19.472  1.00  13.30 ? 125 THR A CA  1 
ATOM   1026 C  C   . THR A 1 125 ? -13.815 17.671  20.185  1.00  12.83 ? 125 THR A C   1 
ATOM   1027 O  O   . THR A 1 125 ? -13.570 18.686  19.529  1.00  15.87 ? 125 THR A O   1 
ATOM   1028 C  CB  . THR A 1 125 ? -15.924 16.666  19.196  1.00  14.64 ? 125 THR A CB  1 
ATOM   1029 O  OG1 . THR A 1 125 ? -16.592 16.652  20.430  1.00  16.73 ? 125 THR A OG1 1 
ATOM   1030 C  CG2 . THR A 1 125 ? -16.433 15.513  18.272  1.00  17.58 ? 125 THR A CG2 1 
ATOM   1031 N  N   . LYS A 1 126 ? -13.540 17.548  21.534  1.00  13.60 ? 127 LYS A N   1 
ATOM   1032 C  CA  . LYS A 1 126 ? -12.987 18.731  22.143  1.00  16.13 ? 127 LYS A CA  1 
ATOM   1033 C  C   . LYS A 1 126 ? -11.571 19.014  21.627  1.00  17.06 ? 127 LYS A C   1 
ATOM   1034 O  O   . LYS A 1 126 ? -11.055 20.173  21.812  1.00  18.65 ? 127 LYS A O   1 
ATOM   1035 C  CB  . LYS A 1 126 ? -13.069 18.533  23.649  1.00  19.40 ? 127 LYS A CB  1 
ATOM   1036 C  CG  . LYS A 1 126 ? -12.061 17.664  24.290  1.00  18.16 ? 127 LYS A CG  1 
ATOM   1037 C  CD  . LYS A 1 126 ? -12.483 17.420  25.758  1.00  22.60 ? 127 LYS A CD  1 
ATOM   1038 C  CE  . LYS A 1 126 ? -11.458 16.469  26.298  1.00  26.69 ? 127 LYS A CE  1 
ATOM   1039 N  NZ  . LYS A 1 126 ? -11.211 16.517  27.780  1.00  34.30 ? 127 LYS A NZ  1 
ATOM   1040 N  N   . TYR A 1 127 ? -10.913 18.088  20.927  1.00  14.81 ? 128 TYR A N   1 
ATOM   1041 C  CA  . TYR A 1 127 ? -9.557  18.357  20.381  1.00  14.92 ? 128 TYR A CA  1 
ATOM   1042 C  C   . TYR A 1 127 ? -9.494  18.750  18.918  1.00  13.25 ? 128 TYR A C   1 
ATOM   1043 O  O   . TYR A 1 127 ? -8.405  18.934  18.313  1.00  14.84 ? 128 TYR A O   1 
ATOM   1044 C  CB  . TYR A 1 127 ? -8.612  17.165  20.628  1.00  13.53 ? 128 TYR A CB  1 
ATOM   1045 C  CG  . TYR A 1 127 ? -8.529  16.888  22.058  1.00  12.16 ? 128 TYR A CG  1 
ATOM   1046 C  CD1 . TYR A 1 127 ? -8.072  17.910  22.910  1.00  14.79 ? 128 TYR A CD1 1 
ATOM   1047 C  CD2 . TYR A 1 127 ? -8.836  15.626  22.603  1.00  13.37 ? 128 TYR A CD2 1 
ATOM   1048 C  CE1 . TYR A 1 127 ? -8.016  17.678  24.277  1.00  13.94 ? 128 TYR A CE1 1 
ATOM   1049 C  CE2 . TYR A 1 127 ? -8.753  15.407  23.960  1.00  13.44 ? 128 TYR A CE2 1 
ATOM   1050 C  CZ  . TYR A 1 127 ? -8.346  16.469  24.786  1.00  14.51 ? 128 TYR A CZ  1 
ATOM   1051 O  OH  . TYR A 1 127 ? -8.240  16.245  26.111  1.00  17.01 ? 128 TYR A OH  1 
ATOM   1052 N  N   . GLY A 1 128 ? -10.664 18.790  18.310  1.00  13.60 ? 129 GLY A N   1 
ATOM   1053 C  CA  . GLY A 1 128 ? -10.848 19.396  16.994  1.00  13.83 ? 129 GLY A CA  1 
ATOM   1054 C  C   . GLY A 1 128 ? -10.408 18.593  15.787  1.00  13.29 ? 129 GLY A C   1 
ATOM   1055 O  O   . GLY A 1 128 ? -10.961 18.707  14.650  1.00  15.86 ? 129 GLY A O   1 
ATOM   1056 N  N   . ASP A 1 129 ? -9.438  17.700  15.941  1.00  12.44 ? 130 ASP A N   1 
ATOM   1057 C  CA  . ASP A 1 129 ? -9.060  16.748  14.865  1.00  15.06 ? 130 ASP A CA  1 
ATOM   1058 C  C   . ASP A 1 129 ? -8.303  15.563  15.428  1.00  15.77 ? 130 ASP A C   1 
ATOM   1059 O  O   . ASP A 1 129 ? -7.865  15.567  16.612  1.00  15.28 ? 130 ASP A O   1 
ATOM   1060 C  CB  . ASP A 1 129 ? -8.430  17.376  13.612  1.00  17.35 ? 130 ASP A CB  1 
ATOM   1061 C  CG  . ASP A 1 129 ? -7.019  17.808  13.791  1.00  20.33 ? 130 ASP A CG  1 
ATOM   1062 O  OD1 . ASP A 1 129 ? -6.373  17.466  14.803  1.00  25.38 ? 130 ASP A OD1 1 
ATOM   1063 O  OD2 . ASP A 1 129 ? -6.561  18.507  12.863  1.00  23.99 ? 130 ASP A OD2 1 
ATOM   1064 N  N   . PHE A 1 130 ? -8.163  14.526  14.588  1.00  14.53 ? 131 PHE A N   1 
ATOM   1065 C  CA  . PHE A 1 130 ? -7.597  13.265  15.029  1.00  14.74 ? 131 PHE A CA  1 
ATOM   1066 C  C   . PHE A 1 130 ? -6.119  13.521  15.409  1.00  12.77 ? 131 PHE A C   1 
ATOM   1067 O  O   . PHE A 1 130 ? -5.619  12.967  16.374  1.00  11.34 ? 131 PHE A O   1 
ATOM   1068 C  CB  . PHE A 1 130 ? -7.659  12.242  13.856  1.00  12.09 ? 131 PHE A CB  1 
ATOM   1069 C  CG  . PHE A 1 130 ? -7.018  10.936  14.142  1.00  12.54 ? 131 PHE A CG  1 
ATOM   1070 C  CD1 . PHE A 1 130 ? -7.737  9.900   14.839  1.00  11.50 ? 131 PHE A CD1 1 
ATOM   1071 C  CD2 . PHE A 1 130 ? -5.655  10.726  13.805  1.00  14.07 ? 131 PHE A CD2 1 
ATOM   1072 C  CE1 . PHE A 1 130 ? -7.100  8.726   15.082  1.00  12.01 ? 131 PHE A CE1 1 
ATOM   1073 C  CE2 . PHE A 1 130 ? -5.031  9.535   14.068  1.00  16.23 ? 131 PHE A CE2 1 
ATOM   1074 C  CZ  . PHE A 1 130 ? -5.746  8.533   14.717  1.00  12.91 ? 131 PHE A CZ  1 
ATOM   1075 N  N   . GLY A 1 131 ? -5.363  14.324  14.612  1.00  13.52 ? 132 GLY A N   1 
ATOM   1076 C  CA  . GLY A 1 131 ? -3.944  14.459  14.922  1.00  14.00 ? 132 GLY A CA  1 
ATOM   1077 C  C   . GLY A 1 131 ? -3.671  15.146  16.240  1.00  12.55 ? 132 GLY A C   1 
ATOM   1078 O  O   . GLY A 1 131 ? -2.655  14.841  16.897  1.00  15.69 ? 132 GLY A O   1 
ATOM   1079 N  N   . LYS A 1 132 ? -4.556  16.074  16.602  1.00  13.55 ? 133 LYS A N   1 
ATOM   1080 C  CA  . LYS A 1 132 ? -4.437  16.621  17.942  1.00  15.00 ? 133 LYS A CA  1 
ATOM   1081 C  C   . LYS A 1 132 ? -4.882  15.667  19.062  1.00  13.70 ? 133 LYS A C   1 
ATOM   1082 O  O   . LYS A 1 132 ? -4.274  15.583  20.108  1.00  13.67 ? 133 LYS A O   1 
ATOM   1083 C  CB  . LYS A 1 132 ? -5.202  17.928  18.110  1.00  16.74 ? 133 LYS A CB  1 
ATOM   1084 C  CG  . LYS A 1 132 ? -4.813  19.156  17.281  1.00  22.40 ? 133 LYS A CG  1 
ATOM   1085 C  CD  . LYS A 1 132 ? -3.329  19.178  16.974  1.00  26.25 ? 133 LYS A CD  1 
ATOM   1086 C  CE  . LYS A 1 132 ? -2.531  19.632  18.200  1.00  35.45 ? 133 LYS A CE  1 
ATOM   1087 N  NZ  . LYS A 1 132 ? -3.058  20.892  18.845  1.00  39.49 ? 133 LYS A NZ  1 
ATOM   1088 N  N   . ALA A 1 133 ? -5.996  14.979  18.837  1.00  12.03 ? 134 ALA A N   1 
ATOM   1089 C  CA  . ALA A 1 133 ? -6.546  14.029  19.783  1.00  11.06 ? 134 ALA A CA  1 
ATOM   1090 C  C   . ALA A 1 133 ? -5.517  12.937  20.151  1.00  10.79 ? 134 ALA A C   1 
ATOM   1091 O  O   . ALA A 1 133 ? -5.456  12.539  21.321  1.00  10.33 ? 134 ALA A O   1 
ATOM   1092 C  CB  . ALA A 1 133 ? -7.839  13.361  19.205  1.00  10.51 ? 134 ALA A CB  1 
ATOM   1093 N  N   . VAL A 1 134 ? -4.724  12.381  19.233  1.00  10.44 ? 135 VAL A N   1 
ATOM   1094 C  CA  . VAL A 1 134 ? -3.842  11.311  19.624  1.00  11.09 ? 135 VAL A CA  1 
ATOM   1095 C  C   . VAL A 1 134 ? -2.692  11.741  20.577  1.00  11.15 ? 135 VAL A C   1 
ATOM   1096 O  O   . VAL A 1 134 ? -1.990  10.919  21.130  1.00  12.77 ? 135 VAL A O   1 
ATOM   1097 C  CB  . VAL A 1 134 ? -3.167  10.553  18.434  1.00  12.23 ? 135 VAL A CB  1 
ATOM   1098 C  CG1 . VAL A 1 134 ? -4.246  9.870   17.609  1.00  12.88 ? 135 VAL A CG1 1 
ATOM   1099 C  CG2 . VAL A 1 134 ? -2.258  11.445  17.562  1.00  12.08 ? 135 VAL A CG2 1 
ATOM   1100 N  N   . GLN A 1 135 ? -2.529  13.071  20.720  1.00  11.92 ? 136 GLN A N   1 
ATOM   1101 C  CA  . GLN A 1 135 ? -1.548  13.589  21.653  1.00  14.58 ? 136 GLN A CA  1 
ATOM   1102 C  C   . GLN A 1 135 ? -2.080  13.700  23.050  1.00  13.78 ? 136 GLN A C   1 
ATOM   1103 O  O   . GLN A 1 135 ? -1.412  14.248  23.956  1.00  15.50 ? 136 GLN A O   1 
ATOM   1104 C  CB  . GLN A 1 135 ? -1.056  14.991  21.104  1.00  17.04 ? 136 GLN A CB  1 
ATOM   1105 C  CG  . GLN A 1 135 ? -0.316  14.857  19.775  1.00  19.42 ? 136 GLN A CG  1 
ATOM   1106 C  CD  . GLN A 1 135 ? 0.848   13.887  19.766  1.00  26.87 ? 136 GLN A CD  1 
ATOM   1107 O  OE1 . GLN A 1 135 ? 1.562   13.727  20.762  1.00  32.78 ? 136 GLN A OE1 1 
ATOM   1108 N  NE2 . GLN A 1 135 ? 1.063   13.231  18.608  1.00  31.07 ? 136 GLN A NE2 1 
ATOM   1109 N  N   . GLN A 1 136 ? -3.344  13.337  23.263  1.00  12.28 ? 137 GLN A N   1 
ATOM   1110 C  CA  . GLN A 1 136 ? -4.017  13.547  24.555  1.00  12.44 ? 137 GLN A CA  1 
ATOM   1111 C  C   . GLN A 1 136 ? -4.388  12.257  25.174  1.00  12.74 ? 137 GLN A C   1 
ATOM   1112 O  O   . GLN A 1 136 ? -4.759  11.293  24.502  1.00  11.28 ? 137 GLN A O   1 
ATOM   1113 C  CB  . GLN A 1 136 ? -5.277  14.363  24.406  1.00  13.12 ? 137 GLN A CB  1 
ATOM   1114 C  CG  . GLN A 1 136 ? -5.167  15.615  23.487  1.00  18.86 ? 137 GLN A CG  1 
ATOM   1115 C  CD  . GLN A 1 136 ? -4.190  16.622  24.003  1.00  20.61 ? 137 GLN A CD  1 
ATOM   1116 O  OE1 . GLN A 1 136 ? -3.970  16.676  25.197  1.00  19.18 ? 137 GLN A OE1 1 
ATOM   1117 N  NE2 . GLN A 1 136 ? -3.521  17.372  23.083  1.00  29.11 ? 137 GLN A NE2 1 
ATOM   1118 N  N   . PRO A 1 137 ? -4.417  12.191  26.536  1.00  11.64 ? 138 PRO A N   1 
ATOM   1119 C  CA  . PRO A 1 137 ? -4.646  10.928  27.200  1.00  11.88 ? 138 PRO A CA  1 
ATOM   1120 C  C   . PRO A 1 137 ? -6.106  10.427  27.049  1.00  11.60 ? 138 PRO A C   1 
ATOM   1121 O  O   . PRO A 1 137 ? -6.336  9.185   27.241  1.00  12.88 ? 138 PRO A O   1 
ATOM   1122 C  CB  . PRO A 1 137 ? -4.328  11.179  28.709  1.00  13.14 ? 138 PRO A CB  1 
ATOM   1123 C  CG  . PRO A 1 137 ? -4.300  12.637  28.774  1.00  17.03 ? 138 PRO A CG  1 
ATOM   1124 C  CD  . PRO A 1 137 ? -4.084  13.296  27.457  1.00  12.56 ? 138 PRO A CD  1 
ATOM   1125 N  N   . ASP A 1 138 ? -7.028  11.314  26.688  1.00  10.47 ? 139 ASP A N   1 
ATOM   1126 C  CA  . ASP A 1 138 ? -8.396  10.909  26.464  1.00  11.39 ? 139 ASP A CA  1 
ATOM   1127 C  C   . ASP A 1 138 ? -8.824  11.302  25.032  1.00  10.52 ? 139 ASP A C   1 
ATOM   1128 O  O   . ASP A 1 138 ? -9.970  11.714  24.773  1.00  11.04 ? 139 ASP A O   1 
ATOM   1129 C  CB  . ASP A 1 138 ? -9.328  11.631  27.450  1.00  13.17 ? 139 ASP A CB  1 
ATOM   1130 C  CG  . ASP A 1 138 ? -9.216  13.141  27.377  1.00  16.11 ? 139 ASP A CG  1 
ATOM   1131 O  OD1 . ASP A 1 138 ? -8.297  13.652  26.703  1.00  15.96 ? 139 ASP A OD1 1 
ATOM   1132 O  OD2 . ASP A 1 138 ? -10.046 13.836  28.005  1.00  20.33 ? 139 ASP A OD2 1 
ATOM   1133 N  N   . GLY A 1 139 ? -7.875  11.189  24.096  1.00  9.67  ? 140 GLY A N   1 
ATOM   1134 C  CA  . GLY A 1 139 ? -8.169  11.640  22.757  1.00  9.44  ? 140 GLY A CA  1 
ATOM   1135 C  C   . GLY A 1 139 ? -8.982  10.698  21.896  1.00  8.56  ? 140 GLY A C   1 
ATOM   1136 O  O   . GLY A 1 139 ? -9.705  11.196  21.023  1.00  8.26  ? 140 GLY A O   1 
ATOM   1137 N  N   . LEU A 1 140 ? -8.836  9.384   22.093  1.00  7.62  ? 141 LEU A N   1 
ATOM   1138 C  CA  . LEU A 1 140 ? -9.529  8.416   21.249  1.00  7.88  ? 141 LEU A CA  1 
ATOM   1139 C  C   . LEU A 1 140 ? -10.439 7.507   22.013  1.00  7.55  ? 141 LEU A C   1 
ATOM   1140 O  O   . LEU A 1 140 ? -10.182 7.262   23.222  1.00  8.47  ? 141 LEU A O   1 
ATOM   1141 C  CB  . LEU A 1 140 ? -8.511  7.573   20.476  1.00  8.72  ? 141 LEU A CB  1 
ATOM   1142 C  CG  . LEU A 1 140 ? -7.554  8.229   19.477  1.00  11.07 ? 141 LEU A CG  1 
ATOM   1143 C  CD1 . LEU A 1 140 ? -6.984  7.134   18.589  1.00  10.61 ? 141 LEU A CD1 1 
ATOM   1144 C  CD2 . LEU A 1 140 ? -8.239  9.306   18.648  1.00  12.14 ? 141 LEU A CD2 1 
ATOM   1145 N  N   . ALA A 1 141 ? -11.471 7.033   21.347  1.00  7.36  ? 142 ALA A N   1 
ATOM   1146 C  CA  . ALA A 1 141 ? -12.301 5.921   21.892  1.00  7.39  ? 142 ALA A CA  1 
ATOM   1147 C  C   . ALA A 1 141 ? -12.330 4.908   20.772  1.00  6.51  ? 142 ALA A C   1 
ATOM   1148 O  O   . ALA A 1 141 ? -12.759 5.246   19.661  1.00  7.83  ? 142 ALA A O   1 
ATOM   1149 C  CB  . ALA A 1 141 ? -13.703 6.329   22.347  1.00  8.03  ? 142 ALA A CB  1 
ATOM   1150 N  N   . VAL A 1 142 ? -11.772 3.709   21.003  1.00  7.35  ? 143 VAL A N   1 
ATOM   1151 C  CA  . VAL A 1 142 ? -11.777 2.660   19.976  1.00  7.89  ? 143 VAL A CA  1 
ATOM   1152 C  C   . VAL A 1 142 ? -12.794 1.570   20.459  1.00  7.31  ? 143 VAL A C   1 
ATOM   1153 O  O   . VAL A 1 142 ? -12.623 1.051   21.546  1.00  6.87  ? 143 VAL A O   1 
ATOM   1154 C  CB  . VAL A 1 142 ? -10.347 2.094   19.593  1.00  7.77  ? 143 VAL A CB  1 
ATOM   1155 C  CG1 . VAL A 1 142 ? -10.528 1.082   18.467  1.00  8.06  ? 143 VAL A CG1 1 
ATOM   1156 C  CG2 . VAL A 1 142 ? -9.386  3.210   19.189  1.00  8.37  ? 143 VAL A CG2 1 
ATOM   1157 N  N   . LEU A 1 143 ? -13.776 1.263   19.607  1.00  6.54  ? 144 LEU A N   1 
ATOM   1158 C  CA  . LEU A 1 143 ? -14.728 0.210   19.900  1.00  7.50  ? 144 LEU A CA  1 
ATOM   1159 C  C   . LEU A 1 143 ? -14.195 -1.045  19.201  1.00  7.18  ? 144 LEU A C   1 
ATOM   1160 O  O   . LEU A 1 143 ? -14.040 -1.088  17.953  1.00  8.02  ? 144 LEU A O   1 
ATOM   1161 C  CB  . LEU A 1 143 ? -16.124 0.669   19.360  1.00  8.17  ? 144 LEU A CB  1 
ATOM   1162 C  CG  . LEU A 1 143 ? -17.263 -0.319  19.458  1.00  8.36  ? 144 LEU A CG  1 
ATOM   1163 C  CD1 . LEU A 1 143 ? -17.488 -0.648  20.929  1.00  8.67  ? 144 LEU A CD1 1 
ATOM   1164 C  CD2 . LEU A 1 143 ? -18.514 0.277   18.861  1.00  9.84  ? 144 LEU A CD2 1 
ATOM   1165 N  N   . GLY A 1 144 ? -13.911 -2.067  19.982  1.00  7.26  ? 145 GLY A N   1 
ATOM   1166 C  CA  . GLY A 1 144 ? -13.338 -3.319  19.505  1.00  6.58  ? 145 GLY A CA  1 
ATOM   1167 C  C   . GLY A 1 144 ? -14.406 -4.414  19.482  1.00  6.68  ? 145 GLY A C   1 
ATOM   1168 O  O   . GLY A 1 144 ? -15.148 -4.557  20.523  1.00  8.27  ? 145 GLY A O   1 
ATOM   1169 N  N   . ILE A 1 145 ? -14.487 -5.166  18.392  1.00  6.63  ? 146 ILE A N   1 
ATOM   1170 C  CA  . ILE A 1 145 ? -15.540 -6.198  18.290  1.00  6.87  ? 146 ILE A CA  1 
ATOM   1171 C  C   . ILE A 1 145 ? -14.781 -7.420  17.771  1.00  7.63  ? 146 ILE A C   1 
ATOM   1172 O  O   . ILE A 1 145 ? -14.125 -7.401  16.706  1.00  7.60  ? 146 ILE A O   1 
ATOM   1173 C  CB  . ILE A 1 145 ? -16.596 -5.721  17.260  1.00  7.48  ? 146 ILE A CB  1 
ATOM   1174 C  CG1 . ILE A 1 145 ? -17.229 -4.439  17.757  1.00  9.44  ? 146 ILE A CG1 1 
ATOM   1175 C  CG2 . ILE A 1 145 ? -17.684 -6.798  17.082  1.00  9.18  ? 146 ILE A CG2 1 
ATOM   1176 C  CD1 . ILE A 1 145 ? -18.373 -3.842  16.883  1.00  8.84  ? 146 ILE A CD1 1 
ATOM   1177 N  N   . PHE A 1 146 ? -14.962 -8.530  18.429  1.00  6.92  ? 147 PHE A N   1 
ATOM   1178 C  CA  . PHE A 1 146 ? -14.340 -9.811  17.973  1.00  7.78  ? 147 PHE A CA  1 
ATOM   1179 C  C   . PHE A 1 146 ? -15.111 -10.459 16.834  1.00  8.69  ? 147 PHE A C   1 
ATOM   1180 O  O   . PHE A 1 146 ? -16.335 -10.333 16.762  1.00  9.19  ? 147 PHE A O   1 
ATOM   1181 C  CB  . PHE A 1 146 ? -14.314 -10.759 19.170  1.00  7.38  ? 147 PHE A CB  1 
ATOM   1182 C  CG  . PHE A 1 146 ? -13.446 -10.276 20.289  1.00  6.75  ? 147 PHE A CG  1 
ATOM   1183 C  CD1 . PHE A 1 146 ? -12.056 -10.152 20.076  1.00  7.15  ? 147 PHE A CD1 1 
ATOM   1184 C  CD2 . PHE A 1 146 ? -13.985 -10.006 21.530  1.00  8.55  ? 147 PHE A CD2 1 
ATOM   1185 C  CE1 . PHE A 1 146 ? -11.241 -9.749  21.110  1.00  7.61  ? 147 PHE A CE1 1 
ATOM   1186 C  CE2 . PHE A 1 146 ? -13.225 -9.610  22.605  1.00  9.01  ? 147 PHE A CE2 1 
ATOM   1187 C  CZ  . PHE A 1 146 ? -11.810 -9.526  22.378  1.00  7.76  ? 147 PHE A CZ  1 
ATOM   1188 N  N   . LEU A 1 147 ? -14.376 -11.135 15.962  1.00  8.52  ? 148 LEU A N   1 
ATOM   1189 C  CA  . LEU A 1 147 ? -14.992 -11.909 14.840  1.00  8.45  ? 148 LEU A CA  1 
ATOM   1190 C  C   . LEU A 1 147 ? -14.635 -13.387 15.076  1.00  8.22  ? 148 LEU A C   1 
ATOM   1191 O  O   . LEU A 1 147 ? -13.458 -13.761 15.248  1.00  9.32  ? 148 LEU A O   1 
ATOM   1192 C  CB  . LEU A 1 147 ? -14.406 -11.511 13.464  1.00  9.58  ? 148 LEU A CB  1 
ATOM   1193 C  CG  . LEU A 1 147 ? -14.986 -10.248 12.892  1.00  8.63  ? 148 LEU A CG  1 
ATOM   1194 C  CD1 . LEU A 1 147 ? -14.671 -8.956  13.654  1.00  10.71 ? 148 LEU A CD1 1 
ATOM   1195 C  CD2 . LEU A 1 147 ? -14.435 -10.094 11.484  1.00  10.61 ? 148 LEU A CD2 1 
ATOM   1196 N  N   . LYS A 1 148 ? -15.674 -14.223 15.123  1.00  8.90  ? 149 LYS A N   1 
ATOM   1197 C  CA  . LYS A 1 148 ? -15.520 -15.672 15.086  1.00  9.76  ? 149 LYS A CA  1 
ATOM   1198 C  C   . LYS A 1 148 ? -16.009 -16.213 13.756  1.00  10.22 ? 149 LYS A C   1 
ATOM   1199 O  O   . LYS A 1 148 ? -16.798 -15.588 13.084  1.00  10.41 ? 149 LYS A O   1 
ATOM   1200 C  CB  . LYS A 1 148 ? -16.262 -16.353 16.219  1.00  12.42 ? 149 LYS A CB  1 
ATOM   1201 C  CG  . LYS A 1 148 ? -17.768 -16.212 16.174  1.00  15.10 ? 149 LYS A CG  1 
ATOM   1202 C  CD  . LYS A 1 148 ? -18.398 -17.029 17.338  1.00  20.90 ? 149 LYS A CD  1 
ATOM   1203 C  CE  . LYS A 1 148 ? -19.892 -16.737 17.398  1.00  23.83 ? 149 LYS A CE  1 
ATOM   1204 N  NZ  . LYS A 1 148 ? -20.469 -17.483 18.545  1.00  32.47 ? 149 LYS A NZ  1 
ATOM   1205 N  N   . VAL A 1 149 ? -15.465 -17.357 13.370  1.00  11.37 ? 150 VAL A N   1 
ATOM   1206 C  CA  . VAL A 1 149 ? -15.856 -17.910 12.063  1.00  12.61 ? 150 VAL A CA  1 
ATOM   1207 C  C   . VAL A 1 149 ? -17.060 -18.851 12.284  1.00  13.37 ? 150 VAL A C   1 
ATOM   1208 O  O   . VAL A 1 149 ? -17.050 -19.764 13.155  1.00  14.48 ? 150 VAL A O   1 
ATOM   1209 C  CB  . VAL A 1 149 ? -14.655 -18.646 11.438  1.00  12.66 ? 150 VAL A CB  1 
ATOM   1210 C  CG1 . VAL A 1 149 ? -15.061 -19.433 10.204  1.00  13.69 ? 150 VAL A CG1 1 
ATOM   1211 C  CG2 . VAL A 1 149 ? -13.530 -17.710 11.015  1.00  14.47 ? 150 VAL A CG2 1 
ATOM   1212 N  N   . GLY A 1 150 ? -18.061 -18.641 11.466  1.00  11.24 ? 151 GLY A N   1 
ATOM   1213 C  CA  . GLY A 1 150 ? -19.368 -19.380 11.601  1.00  11.37 ? 151 GLY A CA  1 
ATOM   1214 C  C   . GLY A 1 150 ? -20.243 -18.936 10.464  1.00  11.00 ? 151 GLY A C   1 
ATOM   1215 O  O   . GLY A 1 150 ? -19.855 -19.046 9.317   1.00  12.45 ? 151 GLY A O   1 
ATOM   1216 N  N   . SER A 1 151 ? -21.477 -18.508 10.801  1.00  12.61 ? 152 SER A N   1 
ATOM   1217 C  CA  . SER A 1 151 ? -22.367 -17.946 9.755   1.00  12.61 ? 152 SER A CA  1 
ATOM   1218 C  C   . SER A 1 151 ? -21.791 -16.633 9.144   1.00  13.09 ? 152 SER A C   1 
ATOM   1219 O  O   . SER A 1 151 ? -21.028 -15.945 9.823   1.00  12.99 ? 152 SER A O   1 
ATOM   1220 C  CB  . SER A 1 151 ? -23.776 -17.790 10.246  1.00  19.02 ? 152 SER A CB  1 
ATOM   1221 O  OG  . SER A 1 151 ? -23.808 -16.722 11.161  1.00  24.48 ? 152 SER A OG  1 
ATOM   1222 N  N   . ALA A 1 152 ? -22.069 -16.326 7.876   1.00  12.71 ? 153 ALA A N   1 
ATOM   1223 C  CA  . ALA A 1 152 ? -21.637 -15.053 7.268   1.00  11.92 ? 153 ALA A CA  1 
ATOM   1224 C  C   . ALA A 1 152 ? -22.251 -13.861 7.995   1.00  11.51 ? 153 ALA A C   1 
ATOM   1225 O  O   . ALA A 1 152 ? -23.373 -13.938 8.512   1.00  13.31 ? 153 ALA A O   1 
ATOM   1226 C  CB  . ALA A 1 152 ? -21.980 -14.959 5.747   1.00  14.13 ? 153 ALA A CB  1 
ATOM   1227 N  N   . LYS A 1 153 ? -21.553 -12.710 7.944   1.00  11.54 ? 154 LYS A N   1 
ATOM   1228 C  CA  . LYS A 1 153 ? -22.129 -11.432 8.383   1.00  12.95 ? 154 LYS A CA  1 
ATOM   1229 C  C   . LYS A 1 153 ? -22.532 -10.663 7.111   1.00  12.71 ? 154 LYS A C   1 
ATOM   1230 O  O   . LYS A 1 153 ? -21.706 -10.225 6.387   1.00  12.33 ? 154 LYS A O   1 
ATOM   1231 C  CB  . LYS A 1 153 ? -21.025 -10.684 9.182   1.00  13.26 ? 154 LYS A CB  1 
ATOM   1232 C  CG  . LYS A 1 153 ? -21.545 -9.474  9.930   1.00  14.92 ? 154 LYS A CG  1 
ATOM   1233 C  CD  . LYS A 1 153 ? -22.533 -9.825  11.048  1.00  15.69 ? 154 LYS A CD  1 
ATOM   1234 C  CE  . LYS A 1 153 ? -22.818 -8.661  12.054  1.00  17.14 ? 154 LYS A CE  1 
ATOM   1235 N  NZ  . LYS A 1 153 ? -23.759 -9.100  13.048  1.00  21.84 ? 154 LYS A NZ  1 
ATOM   1236 N  N   . PRO A 1 154 ? -23.851 -10.571 6.854   1.00  13.52 ? 155 PRO A N   1 
ATOM   1237 C  CA  . PRO A 1 154 ? -24.184 -9.986  5.501   1.00  15.95 ? 155 PRO A CA  1 
ATOM   1238 C  C   . PRO A 1 154 ? -23.724 -8.514  5.385   1.00  14.32 ? 155 PRO A C   1 
ATOM   1239 O  O   . PRO A 1 154 ? -23.260 -8.118  4.297   1.00  14.93 ? 155 PRO A O   1 
ATOM   1240 C  CB  . PRO A 1 154 ? -25.744 -10.072 5.487   1.00  16.33 ? 155 PRO A CB  1 
ATOM   1241 C  CG  . PRO A 1 154 ? -26.047 -11.186 6.425   1.00  17.93 ? 155 PRO A CG  1 
ATOM   1242 C  CD  . PRO A 1 154 ? -25.048 -11.050 7.578   1.00  15.86 ? 155 PRO A CD  1 
ATOM   1243 N  N   . GLY A 1 155 ? -23.681 -7.798  6.510   1.00  12.74 ? 156 GLY A N   1 
ATOM   1244 C  CA  . GLY A 1 155 ? -23.323 -6.357  6.426   1.00  13.83 ? 156 GLY A CA  1 
ATOM   1245 C  C   . GLY A 1 155 ? -21.832 -6.211  6.266   1.00  13.79 ? 156 GLY A C   1 
ATOM   1246 O  O   . GLY A 1 155 ? -21.354 -5.040  6.049   1.00  16.28 ? 156 GLY A O   1 
ATOM   1247 N  N   . LEU A 1 156 ? -21.079 -7.312  6.342   1.00  11.55 ? 157 LEU A N   1 
ATOM   1248 C  CA  . LEU A 1 156 ? -19.654 -7.279  5.982   1.00  11.71 ? 157 LEU A CA  1 
ATOM   1249 C  C   . LEU A 1 156 ? -19.360 -7.440  4.519   1.00  12.46 ? 157 LEU A C   1 
ATOM   1250 O  O   . LEU A 1 156 ? -18.240 -7.138  4.017   1.00  11.41 ? 157 LEU A O   1 
ATOM   1251 C  CB  . LEU A 1 156 ? -18.823 -8.252  6.838   1.00  11.52 ? 157 LEU A CB  1 
ATOM   1252 C  CG  . LEU A 1 156 ? -17.288 -8.424  6.609   1.00  10.82 ? 157 LEU A CG  1 
ATOM   1253 C  CD1 . LEU A 1 156 ? -16.582 -7.105  6.955   1.00  11.30 ? 157 LEU A CD1 1 
ATOM   1254 C  CD2 . LEU A 1 156 ? -16.716 -9.555  7.469   1.00  13.03 ? 157 LEU A CD2 1 
ATOM   1255 N  N   . GLN A 1 157 ? -20.347 -7.983  3.759   1.00  13.83 ? 158 GLN A N   1 
ATOM   1256 C  CA  . GLN A 1 157 ? -19.968 -8.447  2.417   1.00  13.82 ? 158 GLN A CA  1 
ATOM   1257 C  C   . GLN A 1 157 ? -19.604 -7.334  1.447   1.00  10.38 ? 158 GLN A C   1 
ATOM   1258 O  O   . GLN A 1 157 ? -18.669 -7.543  0.655   1.00  12.45 ? 158 GLN A O   1 
ATOM   1259 C  CB  . GLN A 1 157 ? -21.060 -9.285  1.824   1.00  14.86 ? 158 GLN A CB  1 
ATOM   1260 C  CG  . GLN A 1 157 ? -20.609 -10.025 0.544   1.00  15.07 ? 158 GLN A CG  1 
ATOM   1261 C  CD  . GLN A 1 157 ? -19.526 -11.020 0.813   1.00  14.87 ? 158 GLN A CD  1 
ATOM   1262 O  OE1 . GLN A 1 157 ? -19.422 -11.602 1.930   1.00  15.34 ? 158 GLN A OE1 1 
ATOM   1263 N  NE2 . GLN A 1 157 ? -18.695 -11.283 -0.190  1.00  15.72 ? 158 GLN A NE2 1 
ATOM   1264 N  N   . LYS A 1 158 ? -20.182 -6.109  1.602   1.00  13.92 ? 159 LYS A N   1 
ATOM   1265 C  CA  . LYS A 1 158 ? -19.782 -5.002  0.767   1.00  13.31 ? 159 LYS A CA  1 
ATOM   1266 C  C   . LYS A 1 158 ? -18.235 -4.672  0.867   1.00  13.52 ? 159 LYS A C   1 
ATOM   1267 O  O   . LYS A 1 158 ? -17.525 -4.304  -0.058  1.00  16.46 ? 159 LYS A O   1 
ATOM   1268 C  CB  . LYS A 1 158 ? -20.750 -3.807  1.077   1.00  18.60 ? 159 LYS A CB  1 
ATOM   1269 C  CG  . LYS A 1 158 ? -20.520 -2.530  0.242   1.00  27.08 ? 159 LYS A CG  1 
ATOM   1270 C  CD  . LYS A 1 158 ? -21.342 -1.300  0.732   1.00  30.17 ? 159 LYS A CD  1 
ATOM   1271 C  CE  . LYS A 1 158 ? -20.995 0.041   0.035   1.00  30.75 ? 159 LYS A CE  1 
ATOM   1272 N  NZ  . LYS A 1 158 ? -21.302 0.046   -1.453  1.00  32.42 ? 159 LYS A NZ  1 
ATOM   1273 N  N   . VAL A 1 159 ? -17.717 -4.858  2.094   1.00  13.37 ? 160 VAL A N   1 
ATOM   1274 C  CA  . VAL A 1 159 ? -16.307 -4.600  2.366   1.00  13.12 ? 160 VAL A CA  1 
ATOM   1275 C  C   . VAL A 1 159 ? -15.499 -5.703  1.680   1.00  13.02 ? 160 VAL A C   1 
ATOM   1276 O  O   . VAL A 1 159 ? -14.525 -5.454  0.951   1.00  14.16 ? 160 VAL A O   1 
ATOM   1277 C  CB  . VAL A 1 159 ? -16.049 -4.657  3.901   1.00  13.12 ? 160 VAL A CB  1 
ATOM   1278 C  CG1 . VAL A 1 159 ? -14.555 -4.638  4.194   1.00  13.91 ? 160 VAL A CG1 1 
ATOM   1279 C  CG2 . VAL A 1 159 ? -16.785 -3.519  4.608   1.00  13.87 ? 160 VAL A CG2 1 
ATOM   1280 N  N   . VAL A 1 160 ? -15.899 -6.984  1.941   1.00  13.16 ? 161 VAL A N   1 
ATOM   1281 C  CA  . VAL A 1 160 ? -15.140 -8.121  1.383   1.00  14.87 ? 161 VAL A CA  1 
ATOM   1282 C  C   . VAL A 1 160 ? -15.091 -8.045  -0.170  1.00  13.36 ? 161 VAL A C   1 
ATOM   1283 O  O   . VAL A 1 160 ? -14.044 -8.309  -0.777  1.00  15.06 ? 161 VAL A O   1 
ATOM   1284 C  CB  . VAL A 1 160 ? -15.767 -9.500  1.873   1.00  17.77 ? 161 VAL A CB  1 
ATOM   1285 C  CG1 . VAL A 1 160 ? -15.278 -10.701 1.036   1.00  19.50 ? 161 VAL A CG1 1 
ATOM   1286 C  CG2 . VAL A 1 160 ? -15.475 -9.633  3.363   1.00  17.28 ? 161 VAL A CG2 1 
ATOM   1287 N  N   . ASP A 1 161 ? -16.197 -7.620  -0.770  1.00  15.66 ? 162 ASP A N   1 
ATOM   1288 C  CA  . ASP A 1 161 ? -16.227 -7.688  -2.231  1.00  18.12 ? 162 ASP A CA  1 
ATOM   1289 C  C   . ASP A 1 161 ? -15.402 -6.622  -2.911  1.00  20.91 ? 162 ASP A C   1 
ATOM   1290 O  O   . ASP A 1 161 ? -15.136 -6.746  -4.095  1.00  25.76 ? 162 ASP A O   1 
ATOM   1291 C  CB  . ASP A 1 161 ? -17.623 -7.577  -2.681  1.00  18.22 ? 162 ASP A CB  1 
ATOM   1292 C  CG  . ASP A 1 161 ? -18.331 -8.921  -2.662  1.00  19.37 ? 162 ASP A CG  1 
ATOM   1293 O  OD1 . ASP A 1 161 ? -17.655 -9.970  -2.772  1.00  26.73 ? 162 ASP A OD1 1 
ATOM   1294 O  OD2 . ASP A 1 161 ? -19.567 -8.838  -2.482  1.00  25.05 ? 162 ASP A OD2 1 
ATOM   1295 N  N   . VAL A 1 162 ? -14.971 -5.572  -2.197  1.00  17.73 ? 163 VAL A N   1 
ATOM   1296 C  CA  . VAL A 1 162 ? -14.169 -4.471  -2.786  1.00  18.48 ? 163 VAL A CA  1 
ATOM   1297 C  C   . VAL A 1 162 ? -12.651 -4.747  -2.627  1.00  14.42 ? 163 VAL A C   1 
ATOM   1298 O  O   . VAL A 1 162 ? -11.798 -4.026  -3.164  1.00  16.99 ? 163 VAL A O   1 
ATOM   1299 C  CB  . VAL A 1 162 ? -14.695 -3.080  -2.252  1.00  19.71 ? 163 VAL A CB  1 
ATOM   1300 C  CG1 . VAL A 1 162 ? -14.173 -2.747  -0.871  1.00  17.50 ? 163 VAL A CG1 1 
ATOM   1301 C  CG2 . VAL A 1 162 ? -14.430 -1.913  -3.221  1.00  21.88 ? 163 VAL A CG2 1 
ATOM   1302 N  N   . LEU A 1 163 ? -12.271 -5.751  -1.794  1.00  15.04 ? 164 LEU A N   1 
ATOM   1303 C  CA  . LEU A 1 163 ? -10.853 -5.955  -1.440  1.00  15.27 ? 164 LEU A CA  1 
ATOM   1304 C  C   . LEU A 1 163 ? -9.901  -6.232  -2.602  1.00  14.08 ? 164 LEU A C   1 
ATOM   1305 O  O   . LEU A 1 163 ? -8.751  -5.888  -2.588  1.00  15.50 ? 164 LEU A O   1 
ATOM   1306 C  CB  . LEU A 1 163 ? -10.627 -6.990  -0.320  1.00  14.00 ? 164 LEU A CB  1 
ATOM   1307 C  CG  . LEU A 1 163 ? -11.351 -6.651  1.005   1.00  14.85 ? 164 LEU A CG  1 
ATOM   1308 C  CD1 . LEU A 1 163 ? -11.262 -7.859  1.971   1.00  15.11 ? 164 LEU A CD1 1 
ATOM   1309 C  CD2 . LEU A 1 163 ? -10.802 -5.323  1.539   1.00  13.98 ? 164 LEU A CD2 1 
ATOM   1310 N  N   . ASP A 1 164 ? -10.492 -6.877  -3.607  1.00  21.05 ? 165 ASP A N   1 
ATOM   1311 C  CA  . ASP A 1 164 ? -9.702  -7.249  -4.762  1.00  23.89 ? 165 ASP A CA  1 
ATOM   1312 C  C   . ASP A 1 164 ? -9.247  -5.966  -5.510  1.00  23.87 ? 165 ASP A C   1 
ATOM   1313 O  O   . ASP A 1 164 ? -8.217  -6.012  -6.210  1.00  26.12 ? 165 ASP A O   1 
ATOM   1314 C  CB  . ASP A 1 164 ? -10.567 -8.157  -5.699  1.00  26.34 ? 165 ASP A CB  1 
ATOM   1315 C  CG  . ASP A 1 164 ? -11.556 -7.361  -6.492  1.00  28.03 ? 165 ASP A CG  1 
ATOM   1316 O  OD1 . ASP A 1 164 ? -12.631 -6.973  -5.956  1.00  29.06 ? 165 ASP A OD1 1 
ATOM   1317 O  OD2 . ASP A 1 164 ? -11.279 -7.082  -7.718  1.00  34.46 ? 165 ASP A OD2 1 
ATOM   1318 N  N   . SER A 1 165 ? -9.933  -4.833  -5.302  1.00  18.77 ? 166 SER A N   1 
ATOM   1319 C  CA  . SER A 1 165 ? -9.546  -3.545  -5.917  1.00  20.01 ? 166 SER A CA  1 
ATOM   1320 C  C   . SER A 1 165 ? -8.490  -2.784  -5.135  1.00  20.99 ? 166 SER A C   1 
ATOM   1321 O  O   . SER A 1 165 ? -7.861  -1.854  -5.655  1.00  20.99 ? 166 SER A O   1 
ATOM   1322 C  CB  . SER A 1 165 ? -10.800 -2.678  -6.157  1.00  24.87 ? 166 SER A CB  1 
ATOM   1323 O  OG  . SER A 1 165 ? -11.325 -2.201  -4.939  1.00  26.09 ? 166 SER A OG  1 
ATOM   1324 N  N   . ILE A 1 166 ? -8.218  -3.206  -3.869  1.00  17.67 ? 167 ILE A N   1 
ATOM   1325 C  CA  . ILE A 1 166 ? -7.153  -2.578  -3.063  1.00  16.50 ? 167 ILE A CA  1 
ATOM   1326 C  C   . ILE A 1 166 ? -6.085  -3.570  -2.547  1.00  15.75 ? 167 ILE A C   1 
ATOM   1327 O  O   . ILE A 1 166 ? -5.733  -3.603  -1.353  1.00  15.44 ? 167 ILE A O   1 
ATOM   1328 C  CB  . ILE A 1 166 ? -7.800  -1.767  -1.866  1.00  15.80 ? 167 ILE A CB  1 
ATOM   1329 C  CG1 . ILE A 1 166 ? -8.621  -2.697  -1.000  1.00  14.72 ? 167 ILE A CG1 1 
ATOM   1330 C  CG2 . ILE A 1 166 ? -8.656  -0.607  -2.398  1.00  16.34 ? 167 ILE A CG2 1 
ATOM   1331 C  CD1 . ILE A 1 166 ? -8.632  -2.214  0.446   1.00  16.11 ? 167 ILE A CD1 1 
ATOM   1332 N  N   . LYS A 1 167 ? -5.697  -4.520  -3.398  1.00  15.61 ? 168 LYS A N   1 
ATOM   1333 C  CA  . LYS A 1 167 ? -4.912  -5.643  -3.006  1.00  14.05 ? 168 LYS A CA  1 
ATOM   1334 C  C   . LYS A 1 167 ? -3.625  -5.278  -2.376  1.00  16.06 ? 168 LYS A C   1 
ATOM   1335 O  O   . LYS A 1 167 ? -3.239  -5.920  -1.400  1.00  15.77 ? 168 LYS A O   1 
ATOM   1336 C  CB  . LYS A 1 167 ? -4.632  -6.556  -4.242  1.00  17.02 ? 168 LYS A CB  1 
ATOM   1337 C  CG  . LYS A 1 167 ? -3.882  -7.841  -3.848  1.00  20.51 ? 168 LYS A CG  1 
ATOM   1338 C  CD  . LYS A 1 167 ? -3.698  -8.772  -5.059  1.00  25.97 ? 168 LYS A CD  1 
ATOM   1339 C  CE  . LYS A 1 167 ? -2.802  -9.931  -4.701  1.00  28.97 ? 168 LYS A CE  1 
ATOM   1340 N  NZ  . LYS A 1 167 ? -3.603  -10.853 -3.834  1.00  39.80 ? 168 LYS A NZ  1 
ATOM   1341 N  N   . THR A 1 168 ? -2.947  -4.243  -2.892  1.00  14.25 ? 169 THR A N   1 
ATOM   1342 C  CA  . THR A 1 168 ? -1.587  -3.928  -2.521  1.00  15.81 ? 169 THR A CA  1 
ATOM   1343 C  C   . THR A 1 168 ? -1.528  -2.532  -1.787  1.00  12.40 ? 169 THR A C   1 
ATOM   1344 O  O   . THR A 1 168 ? -2.432  -1.711  -1.882  1.00  14.28 ? 169 THR A O   1 
ATOM   1345 C  CB  . THR A 1 168 ? -0.669  -3.933  -3.793  1.00  18.62 ? 169 THR A CB  1 
ATOM   1346 O  OG1 . THR A 1 168 ? -1.329  -3.171  -4.780  1.00  18.71 ? 169 THR A OG1 1 
ATOM   1347 C  CG2 . THR A 1 168 ? -0.498  -5.439  -4.207  1.00  18.77 ? 169 THR A CG2 1 
ATOM   1348 N  N   . LYS A 1 169 ? -0.460  -2.367  -1.066  1.00  17.07 ? 170 LYS A N   1 
ATOM   1349 C  CA  . LYS A 1 169 ? -0.175  -1.144  -0.263  1.00  17.09 ? 170 LYS A CA  1 
ATOM   1350 C  C   . LYS A 1 169 ? -0.317  0.137   -1.045  1.00  17.82 ? 170 LYS A C   1 
ATOM   1351 O  O   . LYS A 1 169 ? 0.229   0.236   -2.164  1.00  21.46 ? 170 LYS A O   1 
ATOM   1352 C  CB  . LYS A 1 169 ? 1.222   -1.276  0.267   1.00  17.58 ? 170 LYS A CB  1 
ATOM   1353 C  CG  . LYS A 1 169 ? 1.716   -0.099  1.104   1.00  19.44 ? 170 LYS A CG  1 
ATOM   1354 C  CD  . LYS A 1 169 ? 3.062   -0.434  1.711   1.00  23.22 ? 170 LYS A CD  1 
ATOM   1355 C  CE  . LYS A 1 169 ? 3.633   0.752   2.454   1.00  33.21 ? 170 LYS A CE  1 
ATOM   1356 N  NZ  . LYS A 1 169 ? 5.115   0.845   2.264   1.00  39.91 ? 170 LYS A NZ  1 
ATOM   1357 N  N   . GLY A 1 170 ? -1.085  1.073   -0.554  1.00  20.01 ? 171 GLY A N   1 
ATOM   1358 C  CA  . GLY A 1 170 ? -1.281  2.347   -1.296  1.00  22.10 ? 171 GLY A CA  1 
ATOM   1359 C  C   . GLY A 1 170 ? -2.534  2.442   -2.132  1.00  24.21 ? 171 GLY A C   1 
ATOM   1360 O  O   . GLY A 1 170 ? -2.950  3.563   -2.545  1.00  25.31 ? 171 GLY A O   1 
ATOM   1361 N  N   . LYS A 1 171 ? -3.139  1.297   -2.458  1.00  17.51 ? 172 LYS A N   1 
ATOM   1362 C  CA  . LYS A 1 171 ? -4.345  1.353   -3.209  1.00  18.19 ? 172 LYS A CA  1 
ATOM   1363 C  C   . LYS A 1 171 ? -5.556  1.832   -2.464  1.00  17.92 ? 172 LYS A C   1 
ATOM   1364 O  O   . LYS A 1 171 ? -5.755  1.450   -1.273  1.00  17.44 ? 172 LYS A O   1 
ATOM   1365 C  CB  . LYS A 1 171 ? -4.613  -0.005  -3.907  1.00  18.96 ? 172 LYS A CB  1 
ATOM   1366 C  CG  . LYS A 1 171 ? -3.568  -0.355  -5.000  1.00  22.28 ? 172 LYS A CG  1 
ATOM   1367 C  CD  . LYS A 1 171 ? -3.982  -1.320  -6.086  1.00  30.74 ? 172 LYS A CD  1 
ATOM   1368 C  CE  . LYS A 1 171 ? -5.106  -0.787  -6.974  1.00  32.12 ? 172 LYS A CE  1 
ATOM   1369 N  NZ  . LYS A 1 171 ? -5.587  -1.877  -7.893  1.00  37.44 ? 172 LYS A NZ  1 
ATOM   1370 N  N   . SER A 1 172 ? -6.428  2.570   -3.107  1.00  18.95 ? 173 SER A N   1 
ATOM   1371 C  CA  . SER A 1 172 ? -7.689  2.938   -2.547  1.00  17.49 ? 173 SER A CA  1 
ATOM   1372 C  C   . SER A 1 172 ? -8.859  2.880   -3.509  1.00  17.24 ? 173 SER A C   1 
ATOM   1373 O  O   . SER A 1 172 ? -8.706  2.801   -4.768  1.00  17.88 ? 173 SER A O   1 
ATOM   1374 C  CB  . SER A 1 172 ? -7.610  4.349   -1.950  1.00  21.31 ? 173 SER A CB  1 
ATOM   1375 O  OG  . SER A 1 172 ? -7.344  5.314   -2.984  1.00  24.89 ? 173 SER A OG  1 
ATOM   1376 N  N   . ALA A 1 173 ? -10.041 2.949   -2.983  1.00  18.44 ? 174 ALA A N   1 
ATOM   1377 C  CA  . ALA A 1 173 ? -11.223 2.839   -3.814  1.00  19.64 ? 174 ALA A CA  1 
ATOM   1378 C  C   . ALA A 1 173 ? -12.345 3.593   -3.163  1.00  21.94 ? 174 ALA A C   1 
ATOM   1379 O  O   . ALA A 1 173 ? -12.470 3.673   -1.934  1.00  17.41 ? 174 ALA A O   1 
ATOM   1380 C  CB  . ALA A 1 173 ? -11.621 1.394   -4.032  1.00  22.57 ? 174 ALA A CB  1 
ATOM   1381 N  N   . ASP A 1 174 ? -13.150 4.217   -3.979  1.00  21.23 ? 175 ASP A N   1 
ATOM   1382 C  CA  . ASP A 1 174 ? -14.275 4.919   -3.474  1.00  23.26 ? 175 ASP A CA  1 
ATOM   1383 C  C   . ASP A 1 174 ? -15.107 3.908   -2.711  1.00  23.46 ? 175 ASP A C   1 
ATOM   1384 O  O   . ASP A 1 174 ? -15.263 2.751   -3.120  1.00  22.53 ? 175 ASP A O   1 
ATOM   1385 C  CB  . ASP A 1 174 ? -15.031 5.639   -4.651  1.00  28.75 ? 175 ASP A CB  1 
ATOM   1386 C  CG  . ASP A 1 174 ? -14.164 6.745   -5.296  1.00  40.58 ? 175 ASP A CG  1 
ATOM   1387 O  OD1 . ASP A 1 174 ? -13.700 7.667   -4.582  1.00  36.90 ? 175 ASP A OD1 1 
ATOM   1388 O  OD2 . ASP A 1 174 ? -13.909 6.700   -6.538  1.00  49.03 ? 175 ASP A OD2 1 
ATOM   1389 N  N   . PHE A 1 175 ? -15.660 4.353   -1.584  1.00  18.98 ? 176 PHE A N   1 
ATOM   1390 C  CA  . PHE A 1 175 ? -16.475 3.450   -0.748  1.00  15.12 ? 176 PHE A CA  1 
ATOM   1391 C  C   . PHE A 1 175 ? -17.571 4.167   -0.025  1.00  18.36 ? 176 PHE A C   1 
ATOM   1392 O  O   . PHE A 1 175 ? -17.480 4.382   1.172   1.00  19.06 ? 176 PHE A O   1 
ATOM   1393 C  CB  . PHE A 1 175 ? -15.542 2.635   0.208   1.00  15.58 ? 176 PHE A CB  1 
ATOM   1394 C  CG  . PHE A 1 175 ? -16.142 1.355   0.708   1.00  15.46 ? 176 PHE A CG  1 
ATOM   1395 C  CD1 . PHE A 1 175 ? -16.428 0.273   -0.137  1.00  15.71 ? 176 PHE A CD1 1 
ATOM   1396 C  CD2 . PHE A 1 175 ? -16.467 1.221   2.040   1.00  14.15 ? 176 PHE A CD2 1 
ATOM   1397 C  CE1 . PHE A 1 175 ? -16.966 -0.895  0.374   1.00  15.01 ? 176 PHE A CE1 1 
ATOM   1398 C  CE2 . PHE A 1 175 ? -17.063 0.062   2.576   1.00  15.18 ? 176 PHE A CE2 1 
ATOM   1399 C  CZ  . PHE A 1 175 ? -17.285 -1.013  1.719   1.00  16.37 ? 176 PHE A CZ  1 
ATOM   1400 N  N   . THR A 1 176 ? -18.568 4.635   -0.747  1.00  15.50 ? 177 THR A N   1 
ATOM   1401 C  CA  . THR A 1 176 ? -19.717 5.374   -0.205  1.00  15.64 ? 177 THR A CA  1 
ATOM   1402 C  C   . THR A 1 176 ? -20.905 4.549   0.277   1.00  11.86 ? 177 THR A C   1 
ATOM   1403 O  O   . THR A 1 176 ? -21.029 3.387   -0.183  1.00  13.86 ? 177 THR A O   1 
ATOM   1404 C  CB  . THR A 1 176 ? -20.127 6.438   -1.262  1.00  16.54 ? 177 THR A CB  1 
ATOM   1405 O  OG1 . THR A 1 176 ? -20.491 5.749   -2.467  1.00  20.98 ? 177 THR A OG1 1 
ATOM   1406 C  CG2 . THR A 1 176 ? -18.877 7.386   -1.580  1.00  20.19 ? 177 THR A CG2 1 
ATOM   1407 N  N   . ASN A 1 177 ? -21.744 5.109   1.123   1.00  12.71 ? 178 ASN A N   1 
ATOM   1408 C  CA  . ASN A 1 177 ? -22.979 4.545   1.507   1.00  13.63 ? 178 ASN A CA  1 
ATOM   1409 C  C   . ASN A 1 177 ? -22.796 3.181   2.252   1.00  15.77 ? 178 ASN A C   1 
ATOM   1410 O  O   . ASN A 1 177 ? -23.708 2.363   2.247   1.00  18.09 ? 178 ASN A O   1 
ATOM   1411 C  CB  . ASN A 1 177 ? -23.861 4.378   0.256   1.00  13.96 ? 178 ASN A CB  1 
ATOM   1412 C  CG  . ASN A 1 177 ? -24.164 5.735   -0.388  1.00  15.58 ? 178 ASN A CG  1 
ATOM   1413 O  OD1 . ASN A 1 177 ? -24.814 6.602   0.243   1.00  17.89 ? 178 ASN A OD1 1 
ATOM   1414 N  ND2 . ASN A 1 177 ? -23.489 5.984   -1.538  1.00  14.41 ? 178 ASN A ND2 1 
ATOM   1415 N  N   . PHE A 1 178 ? -21.626 3.027   2.928   1.00  12.94 ? 179 PHE A N   1 
ATOM   1416 C  CA  . PHE A 1 178 ? -21.392 1.817   3.745   1.00  13.74 ? 179 PHE A CA  1 
ATOM   1417 C  C   . PHE A 1 178 ? -21.955 2.113   5.124   1.00  12.63 ? 179 PHE A C   1 
ATOM   1418 O  O   . PHE A 1 178 ? -21.574 3.126   5.709   1.00  12.95 ? 179 PHE A O   1 
ATOM   1419 C  CB  . PHE A 1 178 ? -19.972 1.392   3.829   1.00  13.49 ? 179 PHE A CB  1 
ATOM   1420 C  CG  . PHE A 1 178 ? -19.853 0.130   4.667   1.00  12.30 ? 179 PHE A CG  1 
ATOM   1421 C  CD1 . PHE A 1 178 ? -20.295 -1.095  4.171   1.00  13.35 ? 179 PHE A CD1 1 
ATOM   1422 C  CD2 . PHE A 1 178 ? -19.367 0.212   5.954   1.00  12.52 ? 179 PHE A CD2 1 
ATOM   1423 C  CE1 . PHE A 1 178 ? -20.250 -2.236  4.955   1.00  12.78 ? 179 PHE A CE1 1 
ATOM   1424 C  CE2 . PHE A 1 178 ? -19.379 -0.947  6.750   1.00  11.68 ? 179 PHE A CE2 1 
ATOM   1425 C  CZ  . PHE A 1 178 ? -19.748 -2.142  6.243   1.00  11.29 ? 179 PHE A CZ  1 
ATOM   1426 N  N   . ASP A 1 179 ? -22.824 1.242   5.644   1.00  13.23 ? 180 ASP A N   1 
ATOM   1427 C  CA  . ASP A 1 179 ? -23.467 1.473   6.920   1.00  14.77 ? 180 ASP A CA  1 
ATOM   1428 C  C   . ASP A 1 179 ? -22.783 0.613   7.998   1.00  13.18 ? 180 ASP A C   1 
ATOM   1429 O  O   . ASP A 1 179 ? -22.981 -0.605  8.030   1.00  13.12 ? 180 ASP A O   1 
ATOM   1430 C  CB  . ASP A 1 179 ? -24.921 1.074   6.820   1.00  16.33 ? 180 ASP A CB  1 
ATOM   1431 C  CG  . ASP A 1 179 ? -25.713 1.428   8.030   1.00  20.01 ? 180 ASP A CG  1 
ATOM   1432 O  OD1 . ASP A 1 179 ? -25.182 1.704   9.117   1.00  16.40 ? 180 ASP A OD1 1 
ATOM   1433 O  OD2 . ASP A 1 179 ? -26.968 1.435   7.957   1.00  24.20 ? 180 ASP A OD2 1 
ATOM   1434 N  N   . PRO A 1 180 ? -22.036 1.248   8.924   1.00  10.97 ? 181 PRO A N   1 
ATOM   1435 C  CA  . PRO A 1 180 ? -21.295 0.422   9.904   1.00  11.11 ? 181 PRO A CA  1 
ATOM   1436 C  C   . PRO A 1 180 ? -22.196 -0.221  10.928  1.00  11.81 ? 181 PRO A C   1 
ATOM   1437 O  O   . PRO A 1 180 ? -21.721 -1.144  11.656  1.00  11.15 ? 181 PRO A O   1 
ATOM   1438 C  CB  . PRO A 1 180 ? -20.303 1.425   10.514  1.00  12.23 ? 181 PRO A CB  1 
ATOM   1439 C  CG  . PRO A 1 180 ? -21.054 2.722   10.445  1.00  11.67 ? 181 PRO A CG  1 
ATOM   1440 C  CD  . PRO A 1 180 ? -21.716 2.687   9.059   1.00  11.03 ? 181 PRO A CD  1 
ATOM   1441 N  N   . ARG A 1 181 ? -23.463 0.159   10.994  1.00  11.34 ? 182 ARG A N   1 
ATOM   1442 C  CA  . ARG A 1 181 ? -24.384 -0.569  11.908  1.00  12.21 ? 182 ARG A CA  1 
ATOM   1443 C  C   . ARG A 1 181 ? -24.492 -2.050  11.557  1.00  13.28 ? 182 ARG A C   1 
ATOM   1444 O  O   . ARG A 1 181 ? -24.820 -2.851  12.404  1.00  14.39 ? 182 ARG A O   1 
ATOM   1445 C  CB  . ARG A 1 181 ? -25.760 0.086   11.898  1.00  13.41 ? 182 ARG A CB  1 
ATOM   1446 C  CG  . ARG A 1 181 ? -25.708 1.522   12.473  1.00  15.34 ? 182 ARG A CG  1 
ATOM   1447 C  CD  . ARG A 1 181 ? -27.022 2.267   12.332  1.00  15.53 ? 182 ARG A CD  1 
ATOM   1448 N  NE  . ARG A 1 181 ? -27.400 2.446   10.941  1.00  16.82 ? 182 ARG A NE  1 
ATOM   1449 C  CZ  . ARG A 1 181 ? -28.518 3.106   10.595  1.00  20.32 ? 182 ARG A CZ  1 
ATOM   1450 N  NH1 . ARG A 1 181 ? -29.254 3.639   11.560  1.00  22.22 ? 182 ARG A NH1 1 
ATOM   1451 N  NH2 . ARG A 1 181 ? -28.869 3.234   9.305   1.00  19.61 ? 182 ARG A NH2 1 
ATOM   1452 N  N   . GLY A 1 182 ? -24.290 -2.404  10.291  1.00  12.06 ? 183 GLY A N   1 
ATOM   1453 C  CA  . GLY A 1 182 ? -24.272 -3.819  9.867   1.00  12.39 ? 183 GLY A CA  1 
ATOM   1454 C  C   . GLY A 1 182 ? -23.151 -4.677  10.410  1.00  14.57 ? 183 GLY A C   1 
ATOM   1455 O  O   . GLY A 1 182 ? -23.134 -5.898  10.128  1.00  15.24 ? 183 GLY A O   1 
ATOM   1456 N  N   . LEU A 1 183 ? -22.209 -4.073  11.164  1.00  12.89 ? 184 LEU A N   1 
ATOM   1457 C  CA  . LEU A 1 183 ? -21.068 -4.835  11.721  1.00  12.94 ? 184 LEU A CA  1 
ATOM   1458 C  C   . LEU A 1 183 ? -21.183 -5.050  13.193  1.00  12.70 ? 184 LEU A C   1 
ATOM   1459 O  O   . LEU A 1 183 ? -20.230 -5.594  13.784  1.00  14.83 ? 184 LEU A O   1 
ATOM   1460 C  CB  . LEU A 1 183 ? -19.755 -4.099  11.425  1.00  12.25 ? 184 LEU A CB  1 
ATOM   1461 C  CG  . LEU A 1 183 ? -19.427 -3.903  9.936   1.00  13.10 ? 184 LEU A CG  1 
ATOM   1462 C  CD1 . LEU A 1 183 ? -18.174 -3.045  9.787   1.00  12.78 ? 184 LEU A CD1 1 
ATOM   1463 C  CD2 . LEU A 1 183 ? -19.276 -5.249  9.294   1.00  14.65 ? 184 LEU A CD2 1 
ATOM   1464 N  N   . LEU A 1 184 ? -22.289 -4.632  13.785  1.00  10.99 ? 185 LEU A N   1 
ATOM   1465 C  CA  . LEU A 1 184 ? -22.427 -4.619  15.267  1.00  11.14 ? 185 LEU A CA  1 
ATOM   1466 C  C   . LEU A 1 184 ? -23.135 -5.904  15.694  1.00  13.58 ? 185 LEU A C   1 
ATOM   1467 O  O   . LEU A 1 184 ? -24.007 -6.410  15.002  1.00  17.69 ? 185 LEU A O   1 
ATOM   1468 C  CB  . LEU A 1 184 ? -23.255 -3.398  15.745  1.00  10.87 ? 185 LEU A CB  1 
ATOM   1469 C  CG  . LEU A 1 184 ? -22.676 -2.012  15.391  1.00  11.42 ? 185 LEU A CG  1 
ATOM   1470 C  CD1 . LEU A 1 184 ? -23.545 -0.891  15.935  1.00  13.98 ? 185 LEU A CD1 1 
ATOM   1471 C  CD2 . LEU A 1 184 ? -21.211 -1.950  15.890  1.00  14.12 ? 185 LEU A CD2 1 
ATOM   1472 N  N   . PRO A 1 185 ? -22.834 -6.439  16.854  1.00  11.70 ? 186 PRO A N   1 
ATOM   1473 C  CA  . PRO A 1 185 ? -23.572 -7.563  17.368  1.00  12.00 ? 186 PRO A CA  1 
ATOM   1474 C  C   . PRO A 1 185 ? -24.845 -7.015  18.017  1.00  12.62 ? 186 PRO A C   1 
ATOM   1475 O  O   . PRO A 1 185 ? -25.028 -5.851  18.059  1.00  14.06 ? 186 PRO A O   1 
ATOM   1476 C  CB  . PRO A 1 185 ? -22.632 -8.130  18.476  1.00  11.53 ? 186 PRO A CB  1 
ATOM   1477 C  CG  . PRO A 1 185 ? -21.890 -6.933  18.997  1.00  9.81  ? 186 PRO A CG  1 
ATOM   1478 C  CD  . PRO A 1 185 ? -21.678 -6.084  17.706  1.00  11.22 ? 186 PRO A CD  1 
ATOM   1479 N  N   . GLU A 1 186 ? -25.693 -7.905  18.538  1.00  14.82 ? 187 GLU A N   1 
ATOM   1480 C  CA  . GLU A 1 186 ? -26.953 -7.528  19.105  1.00  14.33 ? 187 GLU A CA  1 
ATOM   1481 C  C   . GLU A 1 186 ? -26.719 -6.789  20.406  1.00  15.01 ? 187 GLU A C   1 
ATOM   1482 O  O   . GLU A 1 186 ? -27.349 -5.746  20.634  1.00  17.05 ? 187 GLU A O   1 
ATOM   1483 C  CB  . GLU A 1 186 ? -27.750 -8.848  19.253  1.00  17.37 ? 187 GLU A CB  1 
ATOM   1484 C  CG  . GLU A 1 186 ? -28.755 -8.805  20.353  1.00  23.08 ? 187 GLU A CG  1 
ATOM   1485 C  CD  . GLU A 1 186 ? -29.486 -10.146 20.554  1.00  24.69 ? 187 GLU A CD  1 
ATOM   1486 O  OE1 . GLU A 1 186 ? -29.368 -11.042 19.702  1.00  23.95 ? 187 GLU A OE1 1 
ATOM   1487 O  OE2 . GLU A 1 186 ? -30.159 -10.205 21.628  1.00  28.22 ? 187 GLU A OE2 1 
ATOM   1488 N  N   . SER A 1 187 ? -25.838 -7.301  21.285  1.00  12.72 ? 188 SER A N   1 
ATOM   1489 C  CA  . SER A 1 187 ? -25.631 -6.717  22.585  1.00  14.36 ? 188 SER A CA  1 
ATOM   1490 C  C   . SER A 1 187 ? -24.509 -5.649  22.541  1.00  12.36 ? 188 SER A C   1 
ATOM   1491 O  O   . SER A 1 187 ? -23.476 -5.863  21.865  1.00  14.05 ? 188 SER A O   1 
ATOM   1492 C  CB  . SER A 1 187 ? -25.189 -7.722  23.609  1.00  13.17 ? 188 SER A CB  1 
ATOM   1493 O  OG  . SER A 1 187 ? -24.969 -7.123  24.898  1.00  13.73 ? 188 SER A OG  1 
ATOM   1494 N  N   . LEU A 1 188 ? -24.690 -4.562  23.278  1.00  10.70 ? 189 LEU A N   1 
ATOM   1495 C  CA  . LEU A 1 188 ? -23.609 -3.512  23.447  1.00  13.11 ? 189 LEU A CA  1 
ATOM   1496 C  C   . LEU A 1 188 ? -23.010 -3.628  24.869  1.00  11.17 ? 189 LEU A C   1 
ATOM   1497 O  O   . LEU A 1 188 ? -22.294 -2.683  25.303  1.00  13.06 ? 189 LEU A O   1 
ATOM   1498 C  CB  . LEU A 1 188 ? -24.104 -2.076  23.121  1.00  11.54 ? 189 LEU A CB  1 
ATOM   1499 C  CG  . LEU A 1 188 ? -24.543 -1.818  21.672  1.00  14.13 ? 189 LEU A CG  1 
ATOM   1500 C  CD1 . LEU A 1 188 ? -24.973 -0.371  21.524  1.00  17.40 ? 189 LEU A CD1 1 
ATOM   1501 C  CD2 . LEU A 1 188 ? -23.410 -2.150  20.701  1.00  14.40 ? 189 LEU A CD2 1 
ATOM   1502 N  N   . ASP A 1 189 ? -23.130 -4.767  25.528  1.00  12.16 ? 190 ASP A N   1 
ATOM   1503 C  CA  . ASP A 1 189 ? -22.382 -5.029  26.780  1.00  11.59 ? 190 ASP A CA  1 
ATOM   1504 C  C   . ASP A 1 189 ? -20.855 -4.939  26.479  1.00  10.37 ? 190 ASP A C   1 
ATOM   1505 O  O   . ASP A 1 189 ? -20.416 -5.457  25.413  1.00  11.08 ? 190 ASP A O   1 
ATOM   1506 C  CB  . ASP A 1 189 ? -22.724 -6.409  27.356  1.00  13.58 ? 190 ASP A CB  1 
ATOM   1507 C  CG  . ASP A 1 189 ? -24.125 -6.446  28.039  1.00  17.35 ? 190 ASP A CG  1 
ATOM   1508 O  OD1 . ASP A 1 189 ? -24.605 -5.381  28.359  1.00  20.34 ? 190 ASP A OD1 1 
ATOM   1509 O  OD2 . ASP A 1 189 ? -24.581 -7.582  28.166  1.00  21.24 ? 190 ASP A OD2 1 
ATOM   1510 N  N   . TYR A 1 190 ? -20.109 -4.362  27.402  1.00  9.74  ? 191 TYR A N   1 
ATOM   1511 C  CA  . TYR A 1 190 ? -18.665 -4.117  27.027  1.00  9.05  ? 191 TYR A CA  1 
ATOM   1512 C  C   . TYR A 1 190 ? -17.771 -4.239  28.221  1.00  9.99  ? 191 TYR A C   1 
ATOM   1513 O  O   . TYR A 1 190 ? -18.137 -4.093  29.406  1.00  10.95 ? 191 TYR A O   1 
ATOM   1514 C  CB  . TYR A 1 190 ? -18.494 -2.713  26.376  1.00  10.71 ? 191 TYR A CB  1 
ATOM   1515 C  CG  . TYR A 1 190 ? -18.899 -1.575  27.275  1.00  9.97  ? 191 TYR A CG  1 
ATOM   1516 C  CD1 . TYR A 1 190 ? -17.988 -0.969  28.190  1.00  10.22 ? 191 TYR A CD1 1 
ATOM   1517 C  CD2 . TYR A 1 190 ? -20.207 -1.095  27.242  1.00  9.52  ? 191 TYR A CD2 1 
ATOM   1518 C  CE1 . TYR A 1 190 ? -18.397 0.095   29.028  1.00  10.34 ? 191 TYR A CE1 1 
ATOM   1519 C  CE2 . TYR A 1 190 ? -20.618 -0.013  28.060  1.00  11.29 ? 191 TYR A CE2 1 
ATOM   1520 C  CZ  . TYR A 1 190 ? -19.737 0.556   28.997  1.00  10.98 ? 191 TYR A CZ  1 
ATOM   1521 O  OH  . TYR A 1 190 ? -20.100 1.589   29.843  1.00  12.63 ? 191 TYR A OH  1 
ATOM   1522 N  N   . TRP A 1 191 ? -16.469 -4.386  27.984  1.00  7.62  ? 192 TRP A N   1 
ATOM   1523 C  CA  . TRP A 1 191 ? -15.365 -4.115  28.912  1.00  8.00  ? 192 TRP A CA  1 
ATOM   1524 C  C   . TRP A 1 191 ? -14.679 -2.814  28.553  1.00  8.60  ? 192 TRP A C   1 
ATOM   1525 O  O   . TRP A 1 191 ? -14.680 -2.438  27.352  1.00  8.45  ? 192 TRP A O   1 
ATOM   1526 C  CB  . TRP A 1 191 ? -14.327 -5.196  28.792  1.00  8.96  ? 192 TRP A CB  1 
ATOM   1527 C  CG  . TRP A 1 191 ? -14.816 -6.583  29.207  1.00  9.54  ? 192 TRP A CG  1 
ATOM   1528 C  CD1 . TRP A 1 191 ? -15.021 -7.070  30.518  1.00  10.03 ? 192 TRP A CD1 1 
ATOM   1529 C  CD2 . TRP A 1 191 ? -15.034 -7.717  28.376  1.00  9.54  ? 192 TRP A CD2 1 
ATOM   1530 N  NE1 . TRP A 1 191 ? -15.375 -8.375  30.459  1.00  10.12 ? 192 TRP A NE1 1 
ATOM   1531 C  CE2 . TRP A 1 191 ? -15.503 -8.823  29.217  1.00  10.65 ? 192 TRP A CE2 1 
ATOM   1532 C  CE3 . TRP A 1 191 ? -15.009 -7.915  26.979  1.00  8.96  ? 192 TRP A CE3 1 
ATOM   1533 C  CZ2 . TRP A 1 191 ? -15.756 -10.080 28.687  1.00  10.75 ? 192 TRP A CZ2 1 
ATOM   1534 C  CZ3 . TRP A 1 191 ? -15.290 -9.162  26.468  1.00  9.61  ? 192 TRP A CZ3 1 
ATOM   1535 C  CH2 . TRP A 1 191 ? -15.611 -10.229 27.298  1.00  11.67 ? 192 TRP A CH2 1 
ATOM   1536 N  N   . THR A 1 192 ? -14.062 -2.116  29.485  1.00  7.49  ? 193 THR A N   1 
ATOM   1537 C  CA  . THR A 1 192 ? -13.349 -0.907  29.112  1.00  7.81  ? 193 THR A CA  1 
ATOM   1538 C  C   . THR A 1 192 ? -12.099 -0.731  29.966  1.00  8.34  ? 193 THR A C   1 
ATOM   1539 O  O   . THR A 1 192 ? -12.018 -1.151  31.158  1.00  9.02  ? 193 THR A O   1 
ATOM   1540 C  CB  . THR A 1 192 ? -14.273 0.323   29.201  1.00  8.18  ? 193 THR A CB  1 
ATOM   1541 O  OG1 . THR A 1 192 ? -13.609 1.531   28.810  1.00  8.59  ? 193 THR A OG1 1 
ATOM   1542 C  CG2 . THR A 1 192 ? -14.754 0.553   30.664  1.00  9.30  ? 193 THR A CG2 1 
ATOM   1543 N  N   . TYR A 1 193 ? -11.056 -0.128  29.423  1.00  8.21  ? 194 TYR A N   1 
ATOM   1544 C  CA  . TYR A 1 193 ? -9.790  0.104   30.154  1.00  8.75  ? 194 TYR A CA  1 
ATOM   1545 C  C   . TYR A 1 193 ? -9.003  1.145   29.369  1.00  8.34  ? 194 TYR A C   1 
ATOM   1546 O  O   . TYR A 1 193 ? -9.268  1.341   28.170  1.00  8.21  ? 194 TYR A O   1 
ATOM   1547 C  CB  . TYR A 1 193 ? -8.950  -1.163  30.358  1.00  8.89  ? 194 TYR A CB  1 
ATOM   1548 C  CG  . TYR A 1 193 ? -8.283  -1.647  29.095  1.00  7.55  ? 194 TYR A CG  1 
ATOM   1549 C  CD1 . TYR A 1 193 ? -8.963  -2.380  28.107  1.00  7.47  ? 194 TYR A CD1 1 
ATOM   1550 C  CD2 . TYR A 1 193 ? -6.922  -1.318  28.880  1.00  7.83  ? 194 TYR A CD2 1 
ATOM   1551 C  CE1 . TYR A 1 193 ? -8.284  -2.702  26.893  1.00  6.58  ? 194 TYR A CE1 1 
ATOM   1552 C  CE2 . TYR A 1 193 ? -6.275  -1.644  27.640  1.00  7.06  ? 194 TYR A CE2 1 
ATOM   1553 C  CZ  . TYR A 1 193 ? -6.958  -2.310  26.730  1.00  7.50  ? 194 TYR A CZ  1 
ATOM   1554 O  OH  . TYR A 1 193 ? -6.380  -2.627  25.536  1.00  7.21  ? 194 TYR A OH  1 
ATOM   1555 N  N   . PRO A 1 194 ? -8.088  1.896   29.989  1.00  6.96  ? 195 PRO A N   1 
ATOM   1556 C  CA  . PRO A 1 194 ? -7.254  2.866   29.295  1.00  8.22  ? 195 PRO A CA  1 
ATOM   1557 C  C   . PRO A 1 194 ? -6.024  2.227   28.726  1.00  7.20  ? 195 PRO A C   1 
ATOM   1558 O  O   . PRO A 1 194 ? -5.346  1.465   29.374  1.00  9.06  ? 195 PRO A O   1 
ATOM   1559 C  CB  . PRO A 1 194 ? -6.776  3.824   30.439  1.00  8.57  ? 195 PRO A CB  1 
ATOM   1560 C  CG  . PRO A 1 194 ? -6.857  2.996   31.674  1.00  9.49  ? 195 PRO A CG  1 
ATOM   1561 C  CD  . PRO A 1 194 ? -7.917  1.919   31.493  1.00  8.53  ? 195 PRO A CD  1 
ATOM   1562 N  N   . GLY A 1 195 ? -5.755  2.505   27.455  1.00  7.04  ? 196 GLY A N   1 
ATOM   1563 C  CA  . GLY A 1 195 ? -4.671  1.834   26.763  1.00  7.93  ? 196 GLY A CA  1 
ATOM   1564 C  C   . GLY A 1 195 ? -3.933  2.670   25.740  1.00  6.65  ? 196 GLY A C   1 
ATOM   1565 O  O   . GLY A 1 195 ? -3.536  3.803   26.015  1.00  7.01  ? 196 GLY A O   1 
ATOM   1566 N  N   . SER A 1 196 ? -3.741  2.102   24.553  1.00  7.74  ? 197 SER A N   1 
ATOM   1567 C  CA  . SER A 1 196 ? -2.932  2.770   23.489  1.00  7.14  ? 197 SER A CA  1 
ATOM   1568 C  C   . SER A 1 196 ? -3.398  2.398   22.124  1.00  6.51  ? 197 SER A C   1 
ATOM   1569 O  O   . SER A 1 196 ? -4.106  1.416   21.937  1.00  7.63  ? 197 SER A O   1 
ATOM   1570 C  CB  . SER A 1 196 ? -1.408  2.413   23.559  1.00  7.74  ? 197 SER A CB  1 
ATOM   1571 O  OG  . SER A 1 196 ? -1.182  1.000   23.239  1.00  7.55  ? 197 SER A OG  1 
ATOM   1572 N  N   . LEU A 1 197 ? -2.811  3.078   21.132  1.00  7.23  ? 198 LEU A N   1 
ATOM   1573 C  CA  . LEU A 1 197 ? -2.863  2.533   19.773  1.00  7.45  ? 198 LEU A CA  1 
ATOM   1574 C  C   . LEU A 1 197 ? -2.160  1.190   19.816  1.00  7.63  ? 198 LEU A C   1 
ATOM   1575 O  O   . LEU A 1 197 ? -1.094  1.035   20.524  1.00  7.92  ? 198 LEU A O   1 
ATOM   1576 C  CB  . LEU A 1 197 ? -2.158  3.401   18.805  1.00  9.10  ? 198 LEU A CB  1 
ATOM   1577 C  CG  . LEU A 1 197 ? -2.641  4.837   18.732  1.00  8.93  ? 198 LEU A CG  1 
ATOM   1578 C  CD1 . LEU A 1 197 ? -1.743  5.681   17.757  1.00  11.22 ? 198 LEU A CD1 1 
ATOM   1579 C  CD2 . LEU A 1 197 ? -4.109  5.031   18.408  1.00  12.08 ? 198 LEU A CD2 1 
ATOM   1580 N  N   . THR A 1 198 ? -2.594  0.196   19.014  1.00  6.80  ? 199 THR A N   1 
ATOM   1581 C  CA  . THR A 1 198 ? -1.928  -1.113  18.977  1.00  7.05  ? 199 THR A CA  1 
ATOM   1582 C  C   . THR A 1 198 ? -0.863  -1.155  17.827  1.00  6.56  ? 199 THR A C   1 
ATOM   1583 O  O   . THR A 1 198 ? -0.309  -2.217  17.710  1.00  7.47  ? 199 THR A O   1 
ATOM   1584 C  CB  . THR A 1 198 ? -2.946  -2.233  18.853  1.00  7.29  ? 199 THR A CB  1 
ATOM   1585 O  OG1 . THR A 1 198 ? -3.497  -2.167  17.512  1.00  6.62  ? 199 THR A OG1 1 
ATOM   1586 C  CG2 . THR A 1 198 ? -4.013  -2.221  19.953  1.00  8.50  ? 199 THR A CG2 1 
ATOM   1587 N  N   . THR A 1 199 ? -0.758  -0.060  17.074  1.00  7.72  ? 200 THR A N   1 
ATOM   1588 C  CA  . THR A 1 199 ? 0.396   -0.053  16.091  1.00  8.79  ? 200 THR A CA  1 
ATOM   1589 C  C   . THR A 1 199 ? 1.191   1.211   16.411  1.00  10.41 ? 200 THR A C   1 
ATOM   1590 O  O   . THR A 1 199 ? 0.746   2.158   16.984  1.00  9.55  ? 200 THR A O   1 
ATOM   1591 C  CB  . THR A 1 199 ? -0.018  0.021   14.615  1.00  11.65 ? 200 THR A CB  1 
ATOM   1592 O  OG1 . THR A 1 199 ? -0.502  1.282   14.339  1.00  15.50 ? 200 THR A OG1 1 
ATOM   1593 C  CG2 . THR A 1 199 ? -1.139  -0.944  14.299  1.00  12.37 ? 200 THR A CG2 1 
ATOM   1594 N  N   . PRO A 1 200 ? 2.452   1.217   15.975  1.00  9.29  ? 201 PRO A N   1 
ATOM   1595 C  CA  . PRO A 1 200 ? 3.151   2.453   16.034  1.00  9.81  ? 201 PRO A CA  1 
ATOM   1596 C  C   . PRO A 1 200 ? 2.325   3.616   15.490  1.00  9.73  ? 201 PRO A C   1 
ATOM   1597 O  O   . PRO A 1 200 ? 1.641   3.488   14.426  1.00  10.18 ? 201 PRO A O   1 
ATOM   1598 C  CB  . PRO A 1 200 ? 4.389   2.128   15.106  1.00  10.32 ? 201 PRO A CB  1 
ATOM   1599 C  CG  . PRO A 1 200 ? 4.617   0.692   15.371  1.00  11.93 ? 201 PRO A CG  1 
ATOM   1600 C  CD  . PRO A 1 200 ? 3.208   0.107   15.358  1.00  10.39 ? 201 PRO A CD  1 
ATOM   1601 N  N   . PRO A 1 201 ? 2.361   4.809   16.108  1.00  10.08 ? 202 PRO A N   1 
ATOM   1602 C  CA  . PRO A 1 201 ? 3.252   5.194   17.216  1.00  11.48 ? 202 PRO A CA  1 
ATOM   1603 C  C   . PRO A 1 201 ? 2.956   4.783   18.649  1.00  11.22 ? 202 PRO A C   1 
ATOM   1604 O  O   . PRO A 1 201 ? 3.638   5.227   19.575  1.00  11.70 ? 202 PRO A O   1 
ATOM   1605 C  CB  . PRO A 1 201 ? 3.248   6.728   17.051  1.00  11.77 ? 202 PRO A CB  1 
ATOM   1606 C  CG  . PRO A 1 201 ? 1.859   7.084   16.560  1.00  12.93 ? 202 PRO A CG  1 
ATOM   1607 C  CD  . PRO A 1 201 ? 1.576   5.965   15.578  1.00  11.16 ? 202 PRO A CD  1 
ATOM   1608 N  N   . LEU A 1 202 ? 1.910   3.922   18.838  1.00  9.80  ? 203 LEU A N   1 
ATOM   1609 C  CA  . LEU A 1 202 ? 1.679   3.265   20.131  1.00  8.65  ? 203 LEU A CA  1 
ATOM   1610 C  C   . LEU A 1 202 ? 1.275   4.317   21.185  1.00  8.33  ? 203 LEU A C   1 
ATOM   1611 O  O   . LEU A 1 202 ? 1.460   4.042   22.351  1.00  7.83  ? 203 LEU A O   1 
ATOM   1612 C  CB  . LEU A 1 202 ? 2.875   2.389   20.587  1.00  8.93  ? 203 LEU A CB  1 
ATOM   1613 C  CG  . LEU A 1 202 ? 3.175   1.223   19.586  1.00  9.22  ? 203 LEU A CG  1 
ATOM   1614 C  CD1 . LEU A 1 202 ? 4.450   0.521   20.021  1.00  11.09 ? 203 LEU A CD1 1 
ATOM   1615 C  CD2 . LEU A 1 202 ? 2.095   0.121   19.525  1.00  9.78  ? 203 LEU A CD2 1 
ATOM   1616 N  N   . LEU A 1 203 ? 0.722   5.442   20.761  1.00  8.66  ? 204 LEU A N   1 
ATOM   1617 C  CA  . LEU A 1 203 ? 0.418   6.568   21.675  1.00  8.57  ? 204 LEU A CA  1 
ATOM   1618 C  C   . LEU A 1 203 ? -0.653  6.144   22.683  1.00  9.45  ? 204 LEU A C   1 
ATOM   1619 O  O   . LEU A 1 203 ? -1.616  5.395   22.376  1.00  8.88  ? 204 LEU A O   1 
ATOM   1620 C  CB  . LEU A 1 203 ? -0.019  7.790   20.856  1.00  10.64 ? 204 LEU A CB  1 
ATOM   1621 C  CG  . LEU A 1 203 ? 1.115   8.366   19.950  1.00  12.01 ? 204 LEU A CG  1 
ATOM   1622 C  CD1 . LEU A 1 203 ? 0.586   9.451   19.023  1.00  13.81 ? 204 LEU A CD1 1 
ATOM   1623 C  CD2 . LEU A 1 203 ? 2.282   8.967   20.787  1.00  14.68 ? 204 LEU A CD2 1 
ATOM   1624 N  N   . GLU A 1 204 ? -0.448  6.531   23.951  1.00  9.27  ? 205 GLU A N   1 
ATOM   1625 C  CA  . GLU A 1 204 ? -1.320  6.159   25.074  1.00  9.50  ? 205 GLU A CA  1 
ATOM   1626 C  C   . GLU A 1 204 ? -2.472  7.129   25.183  1.00  9.50  ? 205 GLU A C   1 
ATOM   1627 O  O   . GLU A 1 204 ? -2.550  7.918   26.127  1.00  11.47 ? 205 GLU A O   1 
ATOM   1628 C  CB  . GLU A 1 204 ? -0.481  6.059   26.358  1.00  10.15 ? 205 GLU A CB  1 
ATOM   1629 C  CG  . GLU A 1 204 ? 0.467   4.836   26.193  1.00  10.95 ? 205 GLU A CG  1 
ATOM   1630 C  CD  . GLU A 1 204 ? 1.392   4.540   27.369  1.00  11.45 ? 205 GLU A CD  1 
ATOM   1631 O  OE1 . GLU A 1 204 ? 1.719   5.515   28.077  1.00  14.55 ? 205 GLU A OE1 1 
ATOM   1632 O  OE2 . GLU A 1 204 ? 1.783   3.386   27.514  1.00  10.50 ? 205 GLU A OE2 1 
ATOM   1633 N  N   . CYS A 1 205 ? -3.339  7.082   24.199  1.00  8.34  ? 206 CYS A N   1 
ATOM   1634 C  CA  . CYS A 1 205 ? -4.420  8.061   24.015  1.00  8.10  ? 206 CYS A CA  1 
ATOM   1635 C  C   . CYS A 1 205 ? -5.801  7.433   23.916  1.00  7.21  ? 206 CYS A C   1 
ATOM   1636 O  O   . CYS A 1 205 ? -6.725  8.164   23.544  1.00  8.59  ? 206 CYS A O   1 
ATOM   1637 C  CB  . CYS A 1 205 ? -4.171  8.884   22.740  1.00  8.50  ? 206 CYS A CB  1 
ATOM   1638 S  SG  . CYS A 1 205 ? -4.110  7.896   21.223  1.00  10.08 ? 206 CYS A SG  1 
ATOM   1639 N  N   . VAL A 1 206 ? -5.928  6.121   24.137  1.00  7.18  ? 207 VAL A N   1 
ATOM   1640 C  CA  . VAL A 1 206 ? -7.155  5.389   23.812  1.00  7.27  ? 207 VAL A CA  1 
ATOM   1641 C  C   . VAL A 1 206 ? -7.943  4.952   25.051  1.00  7.15  ? 207 VAL A C   1 
ATOM   1642 O  O   . VAL A 1 206 ? -7.407  4.292   25.921  1.00  9.49  ? 207 VAL A O   1 
ATOM   1643 C  CB  . VAL A 1 206 ? -6.831  4.108   23.005  1.00  6.54  ? 207 VAL A CB  1 
ATOM   1644 C  CG1 . VAL A 1 206 ? -8.163  3.434   22.616  1.00  6.82  ? 207 VAL A CG1 1 
ATOM   1645 C  CG2 . VAL A 1 206 ? -6.092  4.431   21.648  1.00  8.35  ? 207 VAL A CG2 1 
ATOM   1646 N  N   . THR A 1 207 ? -9.238  5.279   25.093  1.00  7.26  ? 208 THR A N   1 
ATOM   1647 C  CA  . THR A 1 207 ? -10.184 4.558   25.940  1.00  7.68  ? 208 THR A CA  1 
ATOM   1648 C  C   . THR A 1 207 ? -10.690 3.390   25.136  1.00  7.11  ? 208 THR A C   1 
ATOM   1649 O  O   . THR A 1 207 ? -11.381 3.600   24.100  1.00  7.06  ? 208 THR A O   1 
ATOM   1650 C  CB  . THR A 1 207 ? -11.359 5.469   26.379  1.00  8.24  ? 208 THR A CB  1 
ATOM   1651 O  OG1 . THR A 1 207 ? -10.828 6.529   27.187  1.00  8.79  ? 208 THR A OG1 1 
ATOM   1652 C  CG2 . THR A 1 207 ? -12.251 4.663   27.252  1.00  8.61  ? 208 THR A CG2 1 
ATOM   1653 N  N   . TRP A 1 208 ? -10.271 2.180   25.510  1.00  6.85  ? 209 TRP A N   1 
ATOM   1654 C  CA  . TRP A 1 208 ? -10.788 0.949   24.862  1.00  7.43  ? 209 TRP A CA  1 
ATOM   1655 C  C   . TRP A 1 208 ? -12.167 0.553   25.309  1.00  7.67  ? 209 TRP A C   1 
ATOM   1656 O  O   . TRP A 1 208 ? -12.337 0.469   26.528  1.00  7.33  ? 209 TRP A O   1 
ATOM   1657 C  CB  . TRP A 1 208 ? -9.725  -0.231  25.016  1.00  8.22  ? 209 TRP A CB  1 
ATOM   1658 C  CG  . TRP A 1 208 ? -8.610  -0.107  24.041  1.00  6.19  ? 209 TRP A CG  1 
ATOM   1659 C  CD1 . TRP A 1 208 ? -7.351  0.504   24.233  1.00  7.20  ? 209 TRP A CD1 1 
ATOM   1660 C  CD2 . TRP A 1 208 ? -8.723  -0.468  22.682  1.00  6.89  ? 209 TRP A CD2 1 
ATOM   1661 N  NE1 . TRP A 1 208 ? -6.680  0.499   23.019  1.00  7.66  ? 209 TRP A NE1 1 
ATOM   1662 C  CE2 . TRP A 1 208 ? -7.429  -0.113  22.084  1.00  6.31  ? 209 TRP A CE2 1 
ATOM   1663 C  CE3 . TRP A 1 208 ? -9.720  -1.115  21.910  1.00  5.82  ? 209 TRP A CE3 1 
ATOM   1664 C  CZ2 . TRP A 1 208 ? -7.174  -0.268  20.730  1.00  6.33  ? 209 TRP A CZ2 1 
ATOM   1665 C  CZ3 . TRP A 1 208 ? -9.439  -1.356  20.553  1.00  6.97  ? 209 TRP A CZ3 1 
ATOM   1666 C  CH2 . TRP A 1 208 ? -8.162  -0.914  19.967  1.00  6.55  ? 209 TRP A CH2 1 
ATOM   1667 N  N   . ILE A 1 209 ? -13.001 0.174   24.394  1.00  7.05  ? 210 ILE A N   1 
ATOM   1668 C  CA  . ILE A 1 209 ? -14.352 -0.336  24.739  1.00  7.23  ? 210 ILE A CA  1 
ATOM   1669 C  C   . ILE A 1 209 ? -14.448 -1.586  23.908  1.00  7.10  ? 210 ILE A C   1 
ATOM   1670 O  O   . ILE A 1 209 ? -14.510 -1.486  22.636  1.00  7.42  ? 210 ILE A O   1 
ATOM   1671 C  CB  . ILE A 1 209 ? -15.386 0.702   24.374  1.00  7.80  ? 210 ILE A CB  1 
ATOM   1672 C  CG1 . ILE A 1 209 ? -15.194 2.008   25.160  1.00  10.06 ? 210 ILE A CG1 1 
ATOM   1673 C  CG2 . ILE A 1 209 ? -16.828 0.083   24.620  1.00  9.10  ? 210 ILE A CG2 1 
ATOM   1674 C  CD1 . ILE A 1 209 ? -16.050 3.211   24.711  1.00  11.20 ? 210 ILE A CD1 1 
ATOM   1675 N  N   . VAL A 1 210 ? -14.437 -2.741  24.522  1.00  7.71  ? 211 VAL A N   1 
ATOM   1676 C  CA  . VAL A 1 210 ? -14.376 -4.047  23.829  1.00  7.54  ? 211 VAL A CA  1 
ATOM   1677 C  C   . VAL A 1 210 ? -15.763 -4.749  24.018  1.00  7.18  ? 211 VAL A C   1 
ATOM   1678 O  O   . VAL A 1 210 ? -16.087 -4.948  25.206  1.00  7.80  ? 211 VAL A O   1 
ATOM   1679 C  CB  . VAL A 1 210 ? -13.174 -4.877  24.226  1.00  7.91  ? 211 VAL A CB  1 
ATOM   1680 C  CG1 . VAL A 1 210 ? -13.209 -6.234  23.512  1.00  7.68  ? 211 VAL A CG1 1 
ATOM   1681 C  CG2 . VAL A 1 210 ? -11.826 -4.132  23.865  1.00  8.02  ? 211 VAL A CG2 1 
ATOM   1682 N  N   . LEU A 1 211 ? -16.499 -5.052  22.965  1.00  7.32  ? 212 LEU A N   1 
ATOM   1683 C  CA  . LEU A 1 211 ? -17.868 -5.659  23.172  1.00  7.70  ? 212 LEU A CA  1 
ATOM   1684 C  C   . LEU A 1 211 ? -17.659 -7.110  23.563  1.00  7.72  ? 212 LEU A C   1 
ATOM   1685 O  O   . LEU A 1 211 ? -16.782 -7.869  23.083  1.00  9.03  ? 212 LEU A O   1 
ATOM   1686 C  CB  . LEU A 1 211 ? -18.608 -5.593  21.833  1.00  7.87  ? 212 LEU A CB  1 
ATOM   1687 C  CG  . LEU A 1 211 ? -18.983 -4.172  21.416  1.00  9.07  ? 212 LEU A CG  1 
ATOM   1688 C  CD1 . LEU A 1 211 ? -20.024 -4.177  20.260  1.00  11.00 ? 212 LEU A CD1 1 
ATOM   1689 C  CD2 . LEU A 1 211 ? -19.462 -3.349  22.624  1.00  8.91  ? 212 LEU A CD2 1 
ATOM   1690 N  N   . LYS A 1 212 ? -18.514 -7.566  24.554  1.00  9.73  ? 213 LYS A N   1 
ATOM   1691 C  CA  . LYS A 1 212 ? -18.447 -8.965  24.964  1.00  10.82 ? 213 LYS A CA  1 
ATOM   1692 C  C   . LYS A 1 212 ? -18.918 -9.960  23.879  1.00  10.13 ? 213 LYS A C   1 
ATOM   1693 O  O   . LYS A 1 212 ? -18.402 -11.066 23.787  1.00  11.86 ? 213 LYS A O   1 
ATOM   1694 C  CB  . LYS A 1 212 ? -19.378 -9.096  26.220  1.00  14.41 ? 213 LYS A CB  1 
ATOM   1695 C  CG  . LYS A 1 212 ? -20.055 -10.425 26.562  1.00  20.40 ? 213 LYS A CG  1 
ATOM   1696 C  CD  . LYS A 1 212 ? -21.224 -10.076 27.483  1.00  21.78 ? 213 LYS A CD  1 
ATOM   1697 C  CE  . LYS A 1 212 ? -22.622 -10.152 26.881  1.00  26.95 ? 213 LYS A CE  1 
ATOM   1698 N  NZ  . LYS A 1 212 ? -22.666 -9.695  25.453  1.00  30.50 ? 213 LYS A NZ  1 
ATOM   1699 N  N   . GLU A 1 213 ? -19.888 -9.549  23.053  1.00  8.61  ? 214 GLU A N   1 
ATOM   1700 C  CA  . GLU A 1 213 ? -20.462 -10.480 22.032  1.00  10.73 ? 214 GLU A CA  1 
ATOM   1701 C  C   . GLU A 1 213 ? -19.721 -10.340 20.695  1.00  9.31  ? 214 GLU A C   1 
ATOM   1702 O  O   . GLU A 1 213 ? -19.667 -9.246  20.140  1.00  9.16  ? 214 GLU A O   1 
ATOM   1703 C  CB  . GLU A 1 213 ? -21.936 -10.123 21.838  1.00  11.19 ? 214 GLU A CB  1 
ATOM   1704 C  CG  . GLU A 1 213 ? -22.611 -11.039 20.848  1.00  13.83 ? 214 GLU A CG  1 
ATOM   1705 C  CD  . GLU A 1 213 ? -24.112 -10.837 20.656  1.00  17.23 ? 214 GLU A CD  1 
ATOM   1706 O  OE1 . GLU A 1 213 ? -24.704 -9.988  21.280  1.00  15.04 ? 214 GLU A OE1 1 
ATOM   1707 O  OE2 . GLU A 1 213 ? -24.634 -11.708 19.886  1.00  24.85 ? 214 GLU A OE2 1 
ATOM   1708 N  N   . PRO A 1 214 ? -19.123 -11.432 20.260  1.00  9.03  ? 215 PRO A N   1 
ATOM   1709 C  CA  . PRO A 1 214 ? -18.468 -11.435 18.922  1.00  10.36 ? 215 PRO A CA  1 
ATOM   1710 C  C   . PRO A 1 214 ? -19.488 -11.427 17.831  1.00  11.29 ? 215 PRO A C   1 
ATOM   1711 O  O   . PRO A 1 214 ? -20.675 -11.780 18.035  1.00  12.79 ? 215 PRO A O   1 
ATOM   1712 C  CB  . PRO A 1 214 ? -17.685 -12.761 18.851  1.00  10.83 ? 215 PRO A CB  1 
ATOM   1713 C  CG  . PRO A 1 214 ? -17.993 -13.474 20.176  1.00  16.65 ? 215 PRO A CG  1 
ATOM   1714 C  CD  . PRO A 1 214 ? -19.139 -12.774 20.895  1.00  10.97 ? 215 PRO A CD  1 
ATOM   1715 N  N   . ILE A 1 215 ? -19.103 -10.959 16.655  1.00  9.75  ? 216 ILE A N   1 
ATOM   1716 C  CA  . ILE A 1 215 ? -19.963 -11.161 15.500  1.00  10.22 ? 216 ILE A CA  1 
ATOM   1717 C  C   . ILE A 1 215 ? -19.436 -12.403 14.802  1.00  9.74  ? 216 ILE A C   1 
ATOM   1718 O  O   . ILE A 1 215 ? -18.243 -12.805 14.999  1.00  10.66 ? 216 ILE A O   1 
ATOM   1719 C  CB  . ILE A 1 215 ? -19.966 -9.986  14.476  1.00  9.74  ? 216 ILE A CB  1 
ATOM   1720 C  CG1 . ILE A 1 215 ? -18.504 -9.622  14.041  1.00  9.54  ? 216 ILE A CG1 1 
ATOM   1721 C  CG2 . ILE A 1 215 ? -20.694 -8.753  15.112  1.00  10.59 ? 216 ILE A CG2 1 
ATOM   1722 C  CD1 . ILE A 1 215 ? -18.571 -8.650  12.811  1.00  11.32 ? 216 ILE A CD1 1 
ATOM   1723 N  N   A SER A 1 216 ? -20.323 -13.109 14.083  0.50  11.05 ? 217 SER A N   1 
ATOM   1724 N  N   B SER A 1 216 ? -20.275 -13.086 14.031  0.50  11.06 ? 217 SER A N   1 
ATOM   1725 C  CA  A SER A 1 216 ? -19.894 -14.251 13.259  0.50  10.66 ? 217 SER A CA  1 
ATOM   1726 C  CA  B SER A 1 216 ? -19.728 -14.210 13.297  0.50  10.65 ? 217 SER A CA  1 
ATOM   1727 C  C   A SER A 1 216 ? -19.655 -13.808 11.837  0.50  10.81 ? 217 SER A C   1 
ATOM   1728 C  C   B SER A 1 216 ? -19.668 -13.885 11.858  0.50  10.72 ? 217 SER A C   1 
ATOM   1729 O  O   A SER A 1 216 ? -20.473 -13.030 11.285  0.50  11.74 ? 217 SER A O   1 
ATOM   1730 O  O   B SER A 1 216 ? -20.624 -13.303 11.316  0.50  11.14 ? 217 SER A O   1 
ATOM   1731 C  CB  A SER A 1 216 ? -20.929 -15.393 13.324  0.50  12.18 ? 217 SER A CB  1 
ATOM   1732 C  CB  B SER A 1 216 ? -20.566 -15.415 13.553  0.50  11.81 ? 217 SER A CB  1 
ATOM   1733 O  OG  A SER A 1 216 ? -21.039 -15.953 14.644  0.50  13.68 ? 217 SER A OG  1 
ATOM   1734 O  OG  B SER A 1 216 ? -21.847 -15.157 13.040  0.50  12.73 ? 217 SER A OG  1 
ATOM   1735 N  N   . VAL A 1 217 ? -18.587 -14.310 11.244  1.00  10.31 ? 218 VAL A N   1 
ATOM   1736 C  CA  . VAL A 1 217 ? -18.365 -14.077 9.820   1.00  10.04 ? 218 VAL A CA  1 
ATOM   1737 C  C   . VAL A 1 217 ? -18.082 -15.454 9.208   1.00  10.68 ? 218 VAL A C   1 
ATOM   1738 O  O   . VAL A 1 217 ? -17.722 -16.414 9.892   1.00  10.67 ? 218 VAL A O   1 
ATOM   1739 C  CB  . VAL A 1 217 ? -17.129 -13.106 9.556   1.00  10.24 ? 218 VAL A CB  1 
ATOM   1740 C  CG1 . VAL A 1 217 ? -17.434 -11.770 10.201  1.00  11.37 ? 218 VAL A CG1 1 
ATOM   1741 C  CG2 . VAL A 1 217 ? -15.828 -13.722 10.086  1.00  11.35 ? 218 VAL A CG2 1 
ATOM   1742 N  N   . SER A 1 218 ? -18.239 -15.549 7.887   1.00  10.89 ? 219 SER A N   1 
ATOM   1743 C  CA  . SER A 1 218 ? -17.989 -16.878 7.338   1.00  11.71 ? 219 SER A CA  1 
ATOM   1744 C  C   . SER A 1 218 ? -16.529 -17.123 7.045   1.00  11.13 ? 219 SER A C   1 
ATOM   1745 O  O   . SER A 1 218 ? -15.684 -16.183 6.924   1.00  10.17 ? 219 SER A O   1 
ATOM   1746 C  CB  . SER A 1 218 ? -18.811 -17.064 6.085   1.00  13.08 ? 219 SER A CB  1 
ATOM   1747 O  OG  . SER A 1 218 ? -18.262 -16.238 5.073   1.00  13.42 ? 219 SER A OG  1 
ATOM   1748 N  N   . SER A 1 219 ? -16.155 -18.408 6.873   1.00  12.06 ? 220 SER A N   1 
ATOM   1749 C  CA  . SER A 1 219 ? -14.796 -18.718 6.530   1.00  12.84 ? 220 SER A CA  1 
ATOM   1750 C  C   . SER A 1 219 ? -14.412 -18.052 5.210   1.00  13.35 ? 220 SER A C   1 
ATOM   1751 O  O   . SER A 1 219 ? -13.262 -17.645 5.057   1.00  15.05 ? 220 SER A O   1 
ATOM   1752 C  CB  . SER A 1 219 ? -14.624 -20.294 6.439   1.00  13.66 ? 220 SER A CB  1 
ATOM   1753 O  OG  . SER A 1 219 ? -15.623 -20.811 5.571   1.00  17.46 ? 220 SER A OG  1 
ATOM   1754 N  N   . GLU A 1 220 ? -15.344 -17.943 4.254   1.00  14.07 ? 221 GLU A N   1 
ATOM   1755 C  CA  . GLU A 1 220 ? -14.975 -17.364 2.972   1.00  15.06 ? 221 GLU A CA  1 
ATOM   1756 C  C   . GLU A 1 220 ? -14.725 -15.823 3.152   1.00  13.17 ? 221 GLU A C   1 
ATOM   1757 O  O   . GLU A 1 220 ? -13.886 -15.236 2.471   1.00  14.05 ? 221 GLU A O   1 
ATOM   1758 C  CB  . GLU A 1 220 ? -16.083 -17.496 1.972   1.00  17.46 ? 221 GLU A CB  1 
ATOM   1759 C  CG  . GLU A 1 220 ? -16.309 -18.938 1.480   1.00  21.13 ? 221 GLU A CG  1 
ATOM   1760 C  CD  . GLU A 1 220 ? -17.456 -19.586 2.212   1.00  23.79 ? 221 GLU A CD  1 
ATOM   1761 O  OE1 . GLU A 1 220 ? -17.925 -19.159 3.299   1.00  22.41 ? 221 GLU A OE1 1 
ATOM   1762 O  OE2 . GLU A 1 220 ? -17.918 -20.661 1.746   1.00  28.01 ? 221 GLU A OE2 1 
ATOM   1763 N  N   . GLN A 1 221 ? -15.476 -15.168 4.084   1.00  12.57 ? 222 GLN A N   1 
ATOM   1764 C  CA  . GLN A 1 221 ? -15.281 -13.724 4.267   1.00  11.24 ? 222 GLN A CA  1 
ATOM   1765 C  C   . GLN A 1 221 ? -13.860 -13.488 4.815   1.00  12.20 ? 222 GLN A C   1 
ATOM   1766 O  O   . GLN A 1 221 ? -13.109 -12.630 4.345   1.00  12.19 ? 222 GLN A O   1 
ATOM   1767 C  CB  . GLN A 1 221 ? -16.311 -13.225 5.240   1.00  12.14 ? 222 GLN A CB  1 
ATOM   1768 C  CG  . GLN A 1 221 ? -17.683 -13.098 4.515   1.00  11.38 ? 222 GLN A CG  1 
ATOM   1769 C  CD  . GLN A 1 221 ? -18.824 -12.533 5.379   1.00  10.40 ? 222 GLN A CD  1 
ATOM   1770 O  OE1 . GLN A 1 221 ? -18.927 -12.893 6.528   1.00  11.06 ? 222 GLN A OE1 1 
ATOM   1771 N  NE2 . GLN A 1 221 ? -19.609 -11.652 4.844   1.00  9.79  ? 222 GLN A NE2 1 
ATOM   1772 N  N   . VAL A 1 222 ? -13.449 -14.260 5.812   1.00  12.36 ? 223 VAL A N   1 
ATOM   1773 C  CA  . VAL A 1 222 ? -12.062 -14.096 6.337   1.00  12.24 ? 223 VAL A CA  1 
ATOM   1774 C  C   . VAL A 1 222 ? -10.964 -14.547 5.368   1.00  15.89 ? 223 VAL A C   1 
ATOM   1775 O  O   . VAL A 1 222 ? -9.906  -13.939 5.300   1.00  14.01 ? 223 VAL A O   1 
ATOM   1776 C  CB  . VAL A 1 222 ? -11.915 -14.664 7.783   1.00  14.60 ? 223 VAL A CB  1 
ATOM   1777 C  CG1 . VAL A 1 222 ? -11.964 -16.158 7.778   1.00  17.09 ? 223 VAL A CG1 1 
ATOM   1778 C  CG2 . VAL A 1 222 ? -10.661 -14.105 8.479   1.00  16.07 ? 223 VAL A CG2 1 
ATOM   1779 N  N   . LEU A 1 223 ? -11.281 -15.548 4.567   1.00  14.06 ? 224 LEU A N   1 
ATOM   1780 C  CA  . LEU A 1 223 ? -10.326 -15.989 3.571   1.00  16.92 ? 224 LEU A CA  1 
ATOM   1781 C  C   . LEU A 1 223 ? -9.983  -14.842 2.626   1.00  16.64 ? 224 LEU A C   1 
ATOM   1782 O  O   . LEU A 1 223 ? -8.823  -14.705 2.214   1.00  18.02 ? 224 LEU A O   1 
ATOM   1783 C  CB  . LEU A 1 223 ? -10.896 -17.200 2.810   1.00  20.12 ? 224 LEU A CB  1 
ATOM   1784 C  CG  . LEU A 1 223 ? -9.708  -17.895 2.155   1.00  29.61 ? 224 LEU A CG  1 
ATOM   1785 C  CD1 . LEU A 1 223 ? -9.012  -18.837 3.156   1.00  30.90 ? 224 LEU A CD1 1 
ATOM   1786 C  CD2 . LEU A 1 223 ? -10.161 -18.661 0.901   1.00  31.89 ? 224 LEU A CD2 1 
ATOM   1787 N  N   . LYS A 1 224 ? -10.973 -14.017 2.323   1.00  14.28 ? 225 LYS A N   1 
ATOM   1788 C  CA  . LYS A 1 224 ? -10.773 -12.898 1.384   1.00  16.11 ? 225 LYS A CA  1 
ATOM   1789 C  C   . LYS A 1 224 ? -9.879  -11.829 2.034   1.00  14.29 ? 225 LYS A C   1 
ATOM   1790 O  O   . LYS A 1 224 ? -9.106  -11.199 1.345   1.00  13.80 ? 225 LYS A O   1 
ATOM   1791 C  CB  . LYS A 1 224 ? -12.096 -12.367 0.821   1.00  16.93 ? 225 LYS A CB  1 
ATOM   1792 C  CG  . LYS A 1 224 ? -12.687 -13.387 -0.224  1.00  23.67 ? 225 LYS A CG  1 
ATOM   1793 C  CD  . LYS A 1 224 ? -14.101 -13.110 -0.715  1.00  31.83 ? 225 LYS A CD  1 
ATOM   1794 C  CE  . LYS A 1 224 ? -14.683 -14.277 -1.572  1.00  34.78 ? 225 LYS A CE  1 
ATOM   1795 N  NZ  . LYS A 1 224 ? -16.065 -14.012 -2.103  1.00  39.23 ? 225 LYS A NZ  1 
ATOM   1796 N  N   . PHE A 1 225 ? -9.957  -11.593 3.386   1.00  12.39 ? 226 PHE A N   1 
ATOM   1797 C  CA  . PHE A 1 225 ? -9.023  -10.659 4.033   1.00  12.60 ? 226 PHE A CA  1 
ATOM   1798 C  C   . PHE A 1 225 ? -7.585  -11.151 3.824   1.00  12.26 ? 226 PHE A C   1 
ATOM   1799 O  O   . PHE A 1 225 ? -6.640  -10.352 3.615   1.00  11.39 ? 226 PHE A O   1 
ATOM   1800 C  CB  . PHE A 1 225 ? -9.194  -10.683 5.599   1.00  11.36 ? 226 PHE A CB  1 
ATOM   1801 C  CG  . PHE A 1 225 ? -10.437 -9.987  6.163   1.00  11.24 ? 226 PHE A CG  1 
ATOM   1802 C  CD1 . PHE A 1 225 ? -11.512 -9.585  5.386   1.00  13.03 ? 226 PHE A CD1 1 
ATOM   1803 C  CD2 . PHE A 1 225 ? -10.501 -9.757  7.536   1.00  14.49 ? 226 PHE A CD2 1 
ATOM   1804 C  CE1 . PHE A 1 225 ? -12.609 -8.954  5.974   1.00  15.19 ? 226 PHE A CE1 1 
ATOM   1805 C  CE2 . PHE A 1 225 ? -11.604 -9.152  8.130   1.00  16.21 ? 226 PHE A CE2 1 
ATOM   1806 C  CZ  . PHE A 1 225 ? -12.662 -8.760  7.343   1.00  14.01 ? 226 PHE A CZ  1 
ATOM   1807 N  N   . ARG A 1 226 ? -7.391  -12.475 3.906   1.00  11.27 ? 227 ARG A N   1 
ATOM   1808 C  CA  . ARG A 1 226 ? -6.028  -13.090 3.732   1.00  11.70 ? 227 ARG A CA  1 
ATOM   1809 C  C   . ARG A 1 226 ? -5.443  -13.070 2.310   1.00  13.13 ? 227 ARG A C   1 
ATOM   1810 O  O   . ARG A 1 226 ? -4.317  -13.432 2.194   1.00  15.97 ? 227 ARG A O   1 
ATOM   1811 C  CB  . ARG A 1 226 ? -6.026  -14.548 4.237   1.00  12.43 ? 227 ARG A CB  1 
ATOM   1812 C  CG  . ARG A 1 226 ? -6.517  -14.710 5.679   1.00  12.92 ? 227 ARG A CG  1 
ATOM   1813 C  CD  . ARG A 1 226 ? -6.435  -16.158 6.085   1.00  14.77 ? 227 ARG A CD  1 
ATOM   1814 N  NE  . ARG A 1 226 ? -6.946  -16.311 7.448   1.00  13.88 ? 227 ARG A NE  1 
ATOM   1815 C  CZ  . ARG A 1 226 ? -7.942  -17.126 7.806   1.00  13.36 ? 227 ARG A CZ  1 
ATOM   1816 N  NH1 . ARG A 1 226 ? -8.361  -18.063 6.913   1.00  17.08 ? 227 ARG A NH1 1 
ATOM   1817 N  NH2 . ARG A 1 226 ? -8.379  -17.178 9.032   1.00  13.00 ? 227 ARG A NH2 1 
ATOM   1818 N  N   . LYS A 1 227 ? -6.212  -12.589 1.360   1.00  13.75 ? 228 LYS A N   1 
ATOM   1819 C  CA  . LYS A 1 227 ? -5.655  -12.491 -0.010  1.00  15.41 ? 228 LYS A CA  1 
ATOM   1820 C  C   . LYS A 1 227 ? -5.086  -11.133 -0.229  1.00  16.36 ? 228 LYS A C   1 
ATOM   1821 O  O   . LYS A 1 227 ? -4.451  -10.862 -1.258  1.00  16.46 ? 228 LYS A O   1 
ATOM   1822 C  CB  . LYS A 1 227 ? -6.789  -12.778 -0.989  1.00  19.44 ? 228 LYS A CB  1 
ATOM   1823 C  CG  . LYS A 1 227 ? -7.161  -14.270 -1.026  1.00  20.85 ? 228 LYS A CG  1 
ATOM   1824 C  CD  . LYS A 1 227 ? -8.360  -14.525 -1.927  1.00  28.70 ? 228 LYS A CD  1 
ATOM   1825 C  CE  . LYS A 1 227 ? -8.039  -15.727 -2.837  1.00  37.73 ? 228 LYS A CE  1 
ATOM   1826 N  NZ  . LYS A 1 227 ? -9.164  -16.734 -2.926  1.00  35.21 ? 228 LYS A NZ  1 
ATOM   1827 N  N   . LEU A 1 228 ? -5.321  -10.191 0.733   1.00  13.89 ? 229 LEU A N   1 
ATOM   1828 C  CA  . LEU A 1 228 ? -4.642  -8.901  0.622   1.00  13.77 ? 229 LEU A CA  1 
ATOM   1829 C  C   . LEU A 1 228 ? -3.108  -9.035  0.770   1.00  13.97 ? 229 LEU A C   1 
ATOM   1830 O  O   . LEU A 1 228 ? -2.561  -10.040 1.189   1.00  14.96 ? 229 LEU A O   1 
ATOM   1831 C  CB  . LEU A 1 228 ? -5.181  -7.900  1.673   1.00  13.34 ? 229 LEU A CB  1 
ATOM   1832 C  CG  . LEU A 1 228 ? -6.636  -7.492  1.486   1.00  14.02 ? 229 LEU A CG  1 
ATOM   1833 C  CD1 . LEU A 1 228 ? -7.078  -6.879  2.798   1.00  15.68 ? 229 LEU A CD1 1 
ATOM   1834 C  CD2 . LEU A 1 228 ? -6.695  -6.462  0.366   1.00  14.81 ? 229 LEU A CD2 1 
ATOM   1835 N  N   . ASN A 1 229 ? -2.391  -7.953  0.464   1.00  14.81 ? 230 ASN A N   1 
ATOM   1836 C  CA  . ASN A 1 229 ? -0.964  -7.928  0.464   1.00  15.11 ? 230 ASN A CA  1 
ATOM   1837 C  C   . ASN A 1 229 ? -0.422  -6.730  1.287   1.00  14.09 ? 230 ASN A C   1 
ATOM   1838 O  O   . ASN A 1 229 ? -0.943  -5.623  1.206   1.00  14.42 ? 230 ASN A O   1 
ATOM   1839 C  CB  . ASN A 1 229 ? -0.478  -7.698  -1.001  1.00  15.73 ? 230 ASN A CB  1 
ATOM   1840 C  CG  . ASN A 1 229 ? -0.433  -8.953  -1.892  1.00  18.07 ? 230 ASN A CG  1 
ATOM   1841 O  OD1 . ASN A 1 229 ? 0.181   -8.814  -3.007  1.00  20.50 ? 230 ASN A OD1 1 
ATOM   1842 N  ND2 . ASN A 1 229 ? -1.092  -10.064 -1.543  1.00  18.04 ? 230 ASN A ND2 1 
ATOM   1843 N  N   . PHE A 1 230 ? 0.642   -7.031  2.024   1.00  15.19 ? 231 PHE A N   1 
ATOM   1844 C  CA  . PHE A 1 230 ? 1.390   -6.023  2.760   1.00  15.65 ? 231 PHE A CA  1 
ATOM   1845 C  C   . PHE A 1 230 ? 2.236   -5.163  1.782   1.00  18.14 ? 231 PHE A C   1 
ATOM   1846 O  O   . PHE A 1 230 ? 2.407   -3.974  2.020   1.00  17.18 ? 231 PHE A O   1 
ATOM   1847 C  CB  . PHE A 1 230 ? 2.392   -6.604  3.711   1.00  14.21 ? 231 PHE A CB  1 
ATOM   1848 C  CG  . PHE A 1 230 ? 1.819   -7.173  4.999   1.00  14.00 ? 231 PHE A CG  1 
ATOM   1849 C  CD1 . PHE A 1 230 ? 1.065   -6.412  5.890   1.00  13.04 ? 231 PHE A CD1 1 
ATOM   1850 C  CD2 . PHE A 1 230 ? 2.121   -8.478  5.350   1.00  14.12 ? 231 PHE A CD2 1 
ATOM   1851 C  CE1 . PHE A 1 230 ? 0.592   -6.968  7.074   1.00  13.45 ? 231 PHE A CE1 1 
ATOM   1852 C  CE2 . PHE A 1 230 ? 1.656   -9.035  6.526   1.00  12.98 ? 231 PHE A CE2 1 
ATOM   1853 C  CZ  . PHE A 1 230 ? 0.888   -8.282  7.389   1.00  12.90 ? 231 PHE A CZ  1 
ATOM   1854 N  N   . ASN A 1 231 ? 2.725   -5.821  0.728   1.00  18.03 ? 232 ASN A N   1 
ATOM   1855 C  CA  . ASN A 1 231 ? 3.550   -5.146  -0.300  1.00  18.88 ? 232 ASN A CA  1 
ATOM   1856 C  C   . ASN A 1 231 ? 2.796   -4.283  -1.241  1.00  17.04 ? 232 ASN A C   1 
ATOM   1857 O  O   . ASN A 1 231 ? 1.563   -4.384  -1.402  1.00  17.31 ? 232 ASN A O   1 
ATOM   1858 C  CB  . ASN A 1 231 ? 4.223   -6.225  -1.089  1.00  19.73 ? 232 ASN A CB  1 
ATOM   1859 C  CG  . ASN A 1 231 ? 3.238   -7.181  -1.692  1.00  18.18 ? 232 ASN A CG  1 
ATOM   1860 O  OD1 . ASN A 1 231 ? 2.731   -8.085  -1.024  1.00  19.94 ? 232 ASN A OD1 1 
ATOM   1861 N  ND2 . ASN A 1 231 ? 2.946   -7.007  -3.014  1.00  19.24 ? 232 ASN A ND2 1 
ATOM   1862 N  N   . GLY A 1 232 ? 3.553   -3.346  -1.869  1.00  18.64 ? 233 GLY A N   1 
ATOM   1863 C  CA  . GLY A 1 232 ? 3.022   -2.581  -3.011  1.00  20.38 ? 233 GLY A CA  1 
ATOM   1864 C  C   . GLY A 1 232 ? 2.995   -3.390  -4.298  1.00  18.26 ? 233 GLY A C   1 
ATOM   1865 O  O   . GLY A 1 232 ? 3.656   -4.412  -4.396  1.00  20.12 ? 233 GLY A O   1 
ATOM   1866 N  N   . GLU A 1 233 ? 2.174   -2.927  -5.263  1.00  20.35 ? 234 GLU A N   1 
ATOM   1867 C  CA  . GLU A 1 233 ? 2.140   -3.526  -6.585  1.00  20.39 ? 234 GLU A CA  1 
ATOM   1868 C  C   . GLU A 1 233 ? 3.535   -3.574  -7.193  1.00  18.51 ? 234 GLU A C   1 
ATOM   1869 O  O   . GLU A 1 233 ? 4.313   -2.666  -7.050  1.00  20.36 ? 234 GLU A O   1 
ATOM   1870 C  CB  . GLU A 1 233 ? 1.208   -2.703  -7.479  1.00  21.38 ? 234 GLU A CB  1 
ATOM   1871 C  CG  . GLU A 1 233 ? 0.816   -3.369  -8.809  1.00  23.38 ? 234 GLU A CG  1 
ATOM   1872 C  CD  . GLU A 1 233 ? -0.028  -2.479  -9.686  1.00  32.85 ? 234 GLU A CD  1 
ATOM   1873 O  OE1 . GLU A 1 233 ? -0.395  -1.329  -9.259  1.00  34.82 ? 234 GLU A OE1 1 
ATOM   1874 O  OE2 . GLU A 1 233 ? -0.292  -2.912  -10.849 1.00  33.82 ? 234 GLU A OE2 1 
ATOM   1875 N  N   . GLY A 1 234 ? 3.803   -4.703  -7.838  1.00  21.79 ? 235 GLY A N   1 
ATOM   1876 C  CA  . GLY A 1 234 ? 5.119   -4.895  -8.454  1.00  26.64 ? 235 GLY A CA  1 
ATOM   1877 C  C   . GLY A 1 234 ? 6.239   -5.210  -7.497  1.00  27.69 ? 235 GLY A C   1 
ATOM   1878 O  O   . GLY A 1 234 ? 7.419   -5.086  -7.854  1.00  30.58 ? 235 GLY A O   1 
ATOM   1879 N  N   . GLU A 1 235 ? 5.880   -5.627  -6.271  1.00  26.88 ? 236 GLU A N   1 
ATOM   1880 C  CA  . GLU A 1 235 ? 6.880   -6.086  -5.281  1.00  27.88 ? 236 GLU A CA  1 
ATOM   1881 C  C   . GLU A 1 235 ? 6.494   -7.517  -4.974  1.00  30.02 ? 236 GLU A C   1 
ATOM   1882 O  O   . GLU A 1 235 ? 5.324   -7.909  -5.243  1.00  28.05 ? 236 GLU A O   1 
ATOM   1883 C  CB  . GLU A 1 235 ? 6.770   -5.268  -3.984  1.00  33.68 ? 236 GLU A CB  1 
ATOM   1884 C  CG  . GLU A 1 235 ? 7.394   -3.909  -4.066  1.00  34.64 ? 236 GLU A CG  1 
ATOM   1885 C  CD  . GLU A 1 235 ? 7.112   -3.074  -2.828  1.00  44.07 ? 236 GLU A CD  1 
ATOM   1886 O  OE1 . GLU A 1 235 ? 6.275   -3.496  -1.963  1.00  40.37 ? 236 GLU A OE1 1 
ATOM   1887 O  OE2 . GLU A 1 235 ? 7.733   -1.994  -2.705  1.00  48.80 ? 236 GLU A OE2 1 
ATOM   1888 N  N   . PRO A 1 236 ? 7.459   -8.336  -4.459  1.00  27.58 ? 237 PRO A N   1 
ATOM   1889 C  CA  . PRO A 1 236 ? 7.092   -9.707  -4.190  1.00  29.14 ? 237 PRO A CA  1 
ATOM   1890 C  C   . PRO A 1 236 ? 5.926   -9.827  -3.185  1.00  26.07 ? 237 PRO A C   1 
ATOM   1891 O  O   . PRO A 1 236 ? 5.811   -9.006  -2.272  1.00  25.16 ? 237 PRO A O   1 
ATOM   1892 C  CB  . PRO A 1 236 ? 8.374   -10.305 -3.586  1.00  30.18 ? 237 PRO A CB  1 
ATOM   1893 C  CG  . PRO A 1 236 ? 9.479   -9.461  -4.134  1.00  33.33 ? 237 PRO A CG  1 
ATOM   1894 C  CD  . PRO A 1 236 ? 8.894   -8.083  -4.161  1.00  33.18 ? 237 PRO A CD  1 
ATOM   1895 N  N   . GLU A 1 237 ? 5.129   -10.869 -3.386  1.00  26.34 ? 238 GLU A N   1 
ATOM   1896 C  CA  . GLU A 1 237 ? 3.885   -11.004 -2.651  1.00  22.99 ? 238 GLU A CA  1 
ATOM   1897 C  C   . GLU A 1 237 ? 4.145   -11.451 -1.222  1.00  21.39 ? 238 GLU A C   1 
ATOM   1898 O  O   . GLU A 1 237 ? 4.648   -12.494 -0.957  1.00  18.88 ? 238 GLU A O   1 
ATOM   1899 C  CB  . GLU A 1 237 ? 2.911   -11.950 -3.356  1.00  24.29 ? 238 GLU A CB  1 
ATOM   1900 C  CG  . GLU A 1 237 ? 1.628   -12.039 -2.582  1.00  25.74 ? 238 GLU A CG  1 
ATOM   1901 C  CD  . GLU A 1 237 ? 0.522   -12.793 -3.278  1.00  25.71 ? 238 GLU A CD  1 
ATOM   1902 O  OE1 . GLU A 1 237 ? 0.822   -13.884 -3.866  1.00  31.35 ? 238 GLU A OE1 1 
ATOM   1903 O  OE2 . GLU A 1 237 ? -0.640  -12.320 -3.248  1.00  22.00 ? 238 GLU A OE2 1 
ATOM   1904 N  N   . GLU A 1 238 ? 3.639   -10.654 -0.288  1.00  19.06 ? 239 GLU A N   1 
ATOM   1905 C  CA  . GLU A 1 238 ? 3.695   -11.029 1.093   1.00  20.73 ? 239 GLU A CA  1 
ATOM   1906 C  C   . GLU A 1 238 ? 2.231   -10.918 1.597   1.00  15.38 ? 239 GLU A C   1 
ATOM   1907 O  O   . GLU A 1 238 ? 1.648   -9.843  1.624   1.00  18.32 ? 239 GLU A O   1 
ATOM   1908 C  CB  . GLU A 1 238 ? 4.552   -10.033 1.798   1.00  21.23 ? 239 GLU A CB  1 
ATOM   1909 C  CG  . GLU A 1 238 ? 4.845   -10.380 3.234   1.00  30.21 ? 239 GLU A CG  1 
ATOM   1910 C  CD  . GLU A 1 238 ? 5.582   -11.696 3.386   1.00  38.63 ? 239 GLU A CD  1 
ATOM   1911 O  OE1 . GLU A 1 238 ? 6.660   -11.832 2.723   1.00  42.56 ? 239 GLU A OE1 1 
ATOM   1912 O  OE2 . GLU A 1 238 ? 5.095   -12.557 4.184   1.00  35.41 ? 239 GLU A OE2 1 
ATOM   1913 N  N   . LEU A 1 239 ? 1.619   -12.055 1.911   1.00  16.67 ? 240 LEU A N   1 
ATOM   1914 C  CA  . LEU A 1 239 ? 0.158   -11.973 2.182   1.00  13.38 ? 240 LEU A CA  1 
ATOM   1915 C  C   . LEU A 1 239 ? -0.044  -11.174 3.505   1.00  12.75 ? 240 LEU A C   1 
ATOM   1916 O  O   . LEU A 1 239 ? 0.709   -11.332 4.481   1.00  14.58 ? 240 LEU A O   1 
ATOM   1917 C  CB  . LEU A 1 239 ? -0.391  -13.373 2.459   1.00  14.56 ? 240 LEU A CB  1 
ATOM   1918 C  CG  . LEU A 1 239 ? -0.531  -14.297 1.239   1.00  16.96 ? 240 LEU A CG  1 
ATOM   1919 C  CD1 . LEU A 1 239 ? -1.207  -15.610 1.612   1.00  19.12 ? 240 LEU A CD1 1 
ATOM   1920 C  CD2 . LEU A 1 239 ? -1.295  -13.606 0.118   1.00  18.72 ? 240 LEU A CD2 1 
ATOM   1921 N  N   . MET A 1 240 ? -1.116  -10.405 3.502   1.00  12.17 ? 241 MET A N   1 
ATOM   1922 C  CA  . MET A 1 240 ? -1.444  -9.571  4.702   1.00  12.25 ? 241 MET A CA  1 
ATOM   1923 C  C   . MET A 1 240 ? -2.278  -10.483 5.623   1.00  11.48 ? 241 MET A C   1 
ATOM   1924 O  O   . MET A 1 240 ? -3.501  -10.640 5.493   1.00  11.98 ? 241 MET A O   1 
ATOM   1925 C  CB  . MET A 1 240 ? -2.178  -8.327  4.229   1.00  12.23 ? 241 MET A CB  1 
ATOM   1926 C  CG  . MET A 1 240 ? -2.630  -7.402  5.465   1.00  13.08 ? 241 MET A CG  1 
ATOM   1927 S  SD  . MET A 1 240 ? -3.568  -6.008  4.959   1.00  14.30 ? 241 MET A SD  1 
ATOM   1928 C  CE  . MET A 1 240 ? -2.308  -4.935  4.268   1.00  12.95 ? 241 MET A CE  1 
ATOM   1929 N  N   . VAL A 1 241 ? -1.479  -11.113 6.479   1.00  11.07 ? 242 VAL A N   1 
ATOM   1930 C  CA  . VAL A 1 241 ? -2.033  -12.023 7.526   1.00  11.36 ? 242 VAL A CA  1 
ATOM   1931 C  C   . VAL A 1 241 ? -1.239  -11.773 8.821   1.00  12.69 ? 242 VAL A C   1 
ATOM   1932 O  O   . VAL A 1 241 ? -0.041  -11.366 8.802   1.00  11.38 ? 242 VAL A O   1 
ATOM   1933 C  CB  . VAL A 1 241 ? -1.965  -13.530 7.163   1.00  12.04 ? 242 VAL A CB  1 
ATOM   1934 C  CG1 . VAL A 1 241 ? -2.797  -13.781 5.891   1.00  13.82 ? 242 VAL A CG1 1 
ATOM   1935 C  CG2 . VAL A 1 241 ? -0.537  -13.999 6.955   1.00  13.32 ? 242 VAL A CG2 1 
ATOM   1936 N  N   . ASP A 1 242 ? -1.841  -12.110 9.960   1.00  9.82  ? 243 ASP A N   1 
ATOM   1937 C  CA  . ASP A 1 242 ? -1.195  -11.950 11.278  1.00  9.92  ? 243 ASP A CA  1 
ATOM   1938 C  C   . ASP A 1 242 ? -0.708  -10.537 11.512  1.00  7.81  ? 243 ASP A C   1 
ATOM   1939 O  O   . ASP A 1 242 ? 0.417   -10.303 11.997  1.00  10.47 ? 243 ASP A O   1 
ATOM   1940 C  CB  . ASP A 1 242 ? -0.094  -12.974 11.562  1.00  10.12 ? 243 ASP A CB  1 
ATOM   1941 C  CG  . ASP A 1 242 ? -0.643  -14.364 11.604  1.00  11.25 ? 243 ASP A CG  1 
ATOM   1942 O  OD1 . ASP A 1 242 ? -1.723  -14.641 12.195  1.00  10.07 ? 243 ASP A OD1 1 
ATOM   1943 O  OD2 . ASP A 1 242 ? -0.030  -15.322 11.015  1.00  12.34 ? 243 ASP A OD2 1 
ATOM   1944 N  N   . ASN A 1 243 ? -1.589  -9.597  11.231  1.00  8.26  ? 244 ASN A N   1 
ATOM   1945 C  CA  . ASN A 1 243 ? -1.300  -8.158  11.495  1.00  8.60  ? 244 ASN A CA  1 
ATOM   1946 C  C   . ASN A 1 243 ? -1.882  -7.747  12.868  1.00  9.70  ? 244 ASN A C   1 
ATOM   1947 O  O   . ASN A 1 243 ? -2.525  -6.720  12.918  1.00  9.57  ? 244 ASN A O   1 
ATOM   1948 C  CB  . ASN A 1 243 ? -1.857  -7.273  10.344  1.00  10.16 ? 244 ASN A CB  1 
ATOM   1949 C  CG  . ASN A 1 243 ? -3.360  -7.437  10.137  1.00  10.51 ? 244 ASN A CG  1 
ATOM   1950 O  OD1 . ASN A 1 243 ? -4.017  -8.328  10.675  1.00  10.08 ? 244 ASN A OD1 1 
ATOM   1951 N  ND2 . ASN A 1 243 ? -3.916  -6.543  9.328   1.00  13.04 ? 244 ASN A ND2 1 
ATOM   1952 N  N   . TRP A 1 244 ? -1.586  -8.530  13.885  1.00  9.00  ? 245 TRP A N   1 
ATOM   1953 C  CA  . TRP A 1 244 ? -2.012  -8.309  15.262  1.00  8.34  ? 245 TRP A CA  1 
ATOM   1954 C  C   . TRP A 1 244 ? -0.830  -8.154  16.139  1.00  8.86  ? 245 TRP A C   1 
ATOM   1955 O  O   . TRP A 1 244 ? 0.189   -8.864  15.951  1.00  9.17  ? 245 TRP A O   1 
ATOM   1956 C  CB  . TRP A 1 244 ? -2.982  -9.397  15.740  1.00  8.97  ? 245 TRP A CB  1 
ATOM   1957 C  CG  . TRP A 1 244 ? -2.550  -10.815 15.519  1.00  7.79  ? 245 TRP A CG  1 
ATOM   1958 C  CD1 . TRP A 1 244 ? -2.680  -11.558 14.332  1.00  8.92  ? 245 TRP A CD1 1 
ATOM   1959 C  CD2 . TRP A 1 244 ? -1.915  -11.681 16.482  1.00  8.63  ? 245 TRP A CD2 1 
ATOM   1960 N  NE1 . TRP A 1 244 ? -2.139  -12.833 14.529  1.00  8.35  ? 245 TRP A NE1 1 
ATOM   1961 C  CE2 . TRP A 1 244 ? -1.694  -12.949 15.844  1.00  8.51  ? 245 TRP A CE2 1 
ATOM   1962 C  CE3 . TRP A 1 244 ? -1.616  -11.558 17.882  1.00  8.69  ? 245 TRP A CE3 1 
ATOM   1963 C  CZ2 . TRP A 1 244 ? -1.081  -14.011 16.515  1.00  8.70  ? 245 TRP A CZ2 1 
ATOM   1964 C  CZ3 . TRP A 1 244 ? -0.990  -12.598 18.492  1.00  9.48  ? 245 TRP A CZ3 1 
ATOM   1965 C  CH2 . TRP A 1 244 ? -0.818  -13.859 17.859  1.00  9.38  ? 245 TRP A CH2 1 
ATOM   1966 N  N   . ARG A 1 245 ? -0.937  -7.312  17.179  1.00  8.15  ? 246 ARG A N   1 
ATOM   1967 C  CA  . ARG A 1 245 ? 0.006   -7.200  18.270  1.00  8.32  ? 246 ARG A CA  1 
ATOM   1968 C  C   . ARG A 1 245 ? -0.436  -8.156  19.389  1.00  8.30  ? 246 ARG A C   1 
ATOM   1969 O  O   . ARG A 1 245 ? -1.660  -8.152  19.679  1.00  9.47  ? 246 ARG A O   1 
ATOM   1970 C  CB  . ARG A 1 245 ? 0.014   -5.769  18.785  1.00  9.24  ? 246 ARG A CB  1 
ATOM   1971 C  CG  . ARG A 1 245 ? 1.113   -5.547  19.807  1.00  9.03  ? 246 ARG A CG  1 
ATOM   1972 C  CD  . ARG A 1 245 ? 1.063   -4.156  20.422  1.00  8.30  ? 246 ARG A CD  1 
ATOM   1973 N  NE  . ARG A 1 245 ? 2.345   -3.846  21.054  1.00  9.79  ? 246 ARG A NE  1 
ATOM   1974 C  CZ  . ARG A 1 245 ? 2.549   -2.858  21.920  1.00  9.74  ? 246 ARG A CZ  1 
ATOM   1975 N  NH1 . ARG A 1 245 ? 1.556   -2.055  22.273  1.00  9.54  ? 246 ARG A NH1 1 
ATOM   1976 N  NH2 . ARG A 1 245 ? 3.754   -2.677  22.438  1.00  11.32 ? 246 ARG A NH2 1 
ATOM   1977 N  N   . PRO A 1 246 ? 0.409   -8.979  20.006  1.00  9.11  ? 247 PRO A N   1 
ATOM   1978 C  CA  . PRO A 1 246 ? 0.013   -9.810  21.128  1.00  9.71  ? 247 PRO A CA  1 
ATOM   1979 C  C   . PRO A 1 246 ? -0.323  -8.945  22.328  1.00  9.56  ? 247 PRO A C   1 
ATOM   1980 O  O   . PRO A 1 246 ? -0.015  -7.769  22.438  1.00  8.95  ? 247 PRO A O   1 
ATOM   1981 C  CB  . PRO A 1 246 ? 1.274   -10.623 21.443  1.00  13.85 ? 247 PRO A CB  1 
ATOM   1982 C  CG  . PRO A 1 246 ? 2.111   -10.560 20.169  1.00  15.35 ? 247 PRO A CG  1 
ATOM   1983 C  CD  . PRO A 1 246 ? 1.856   -9.151  19.619  1.00  11.07 ? 247 PRO A CD  1 
ATOM   1984 N  N   . ALA A 1 247 ? -1.013  -9.635  23.252  1.00  10.49 ? 248 ALA A N   1 
ATOM   1985 C  CA  . ALA A 1 247 ? -1.330  -9.044  24.528  1.00  9.11  ? 248 ALA A CA  1 
ATOM   1986 C  C   . ALA A 1 247 ? -0.107  -8.491  25.283  1.00  10.04 ? 248 ALA A C   1 
ATOM   1987 O  O   . ALA A 1 247 ? 0.958   -9.115  25.294  1.00  11.30 ? 248 ALA A O   1 
ATOM   1988 C  CB  . ALA A 1 247 ? -2.158  -10.039 25.389  1.00  10.52 ? 248 ALA A CB  1 
ATOM   1989 N  N   . GLN A 1 248 ? -0.266  -7.311  25.878  1.00  8.62  ? 249 GLN A N   1 
ATOM   1990 C  CA  . GLN A 1 248 ? 0.735   -6.586  26.595  1.00  10.47 ? 249 GLN A CA  1 
ATOM   1991 C  C   . GLN A 1 248 ? 0.445   -6.638  28.068  1.00  9.96  ? 249 GLN A C   1 
ATOM   1992 O  O   . GLN A 1 248 ? -0.726  -6.837  28.497  1.00  11.08 ? 249 GLN A O   1 
ATOM   1993 C  CB  . GLN A 1 248 ? 0.791   -5.145  26.097  1.00  10.40 ? 249 GLN A CB  1 
ATOM   1994 C  CG  . GLN A 1 248 ? 1.137   -5.059  24.566  1.00  11.37 ? 249 GLN A CG  1 
ATOM   1995 C  CD  . GLN A 1 248 ? 2.508   -5.712  24.237  1.00  14.05 ? 249 GLN A CD  1 
ATOM   1996 O  OE1 . GLN A 1 248 ? 3.561   -5.415  24.894  1.00  16.28 ? 249 GLN A OE1 1 
ATOM   1997 N  NE2 . GLN A 1 248 ? 2.510   -6.624  23.256  1.00  12.84 ? 249 GLN A NE2 1 
ATOM   1998 N  N   . PRO A 1 249 ? 1.457   -6.413  28.944  1.00  12.64 ? 250 PRO A N   1 
ATOM   1999 C  CA  . PRO A 1 249 ? 1.221   -6.440  30.390  1.00  12.89 ? 250 PRO A CA  1 
ATOM   2000 C  C   . PRO A 1 249 ? 0.123   -5.442  30.860  1.00  11.28 ? 250 PRO A C   1 
ATOM   2001 O  O   . PRO A 1 249 ? 0.168   -4.268  30.445  1.00  12.19 ? 250 PRO A O   1 
ATOM   2002 C  CB  . PRO A 1 249 ? 2.566   -6.049  30.970  1.00  15.19 ? 250 PRO A CB  1 
ATOM   2003 C  CG  . PRO A 1 249 ? 3.522   -6.460  29.915  1.00  15.41 ? 250 PRO A CG  1 
ATOM   2004 C  CD  . PRO A 1 249 ? 2.850   -6.092  28.613  1.00  14.18 ? 250 PRO A CD  1 
ATOM   2005 N  N   . LEU A 1 250 ? -0.774  -5.907  31.740  1.00  14.03 ? 251 LEU A N   1 
ATOM   2006 C  CA  . LEU A 1 250 ? -1.816  -5.023  32.189  1.00  14.54 ? 251 LEU A CA  1 
ATOM   2007 C  C   . LEU A 1 250 ? -1.232  -3.888  33.107  1.00  14.15 ? 251 LEU A C   1 
ATOM   2008 O  O   . LEU A 1 250 ? -1.675  -2.718  33.138  1.00  12.08 ? 251 LEU A O   1 
ATOM   2009 C  CB  . LEU A 1 250 ? -2.877  -5.847  32.883  1.00  16.15 ? 251 LEU A CB  1 
ATOM   2010 C  CG  . LEU A 1 250 ? -4.160  -5.143  33.242  1.00  16.39 ? 251 LEU A CG  1 
ATOM   2011 C  CD1 . LEU A 1 250 ? -4.919  -4.607  32.030  1.00  15.21 ? 251 LEU A CD1 1 
ATOM   2012 C  CD2 . LEU A 1 250 ? -4.915  -6.180  34.009  1.00  18.61 ? 251 LEU A CD2 1 
ATOM   2013 N  N   . LYS A 1 251 ? -0.173  -4.207  33.820  1.00  14.81 ? 252 LYS A N   1 
ATOM   2014 C  CA  . LYS A 1 251 ? 0.488   -3.225  34.726  1.00  14.33 ? 252 LYS A CA  1 
ATOM   2015 C  C   . LYS A 1 251 ? -0.489  -2.710  35.763  1.00  15.32 ? 252 LYS A C   1 
ATOM   2016 O  O   . LYS A 1 251 ? -1.297  -3.484  36.320  1.00  17.79 ? 252 LYS A O   1 
ATOM   2017 C  CB  . LYS A 1 251 ? 1.290   -2.160  33.969  1.00  15.86 ? 252 LYS A CB  1 
ATOM   2018 C  CG  . LYS A 1 251 ? 2.456   -2.866  33.286  1.00  18.38 ? 252 LYS A CG  1 
ATOM   2019 C  CD  . LYS A 1 251 ? 3.371   -1.910  32.517  1.00  19.41 ? 252 LYS A CD  1 
ATOM   2020 C  CE  . LYS A 1 251 ? 4.542   -2.629  31.923  1.00  20.72 ? 252 LYS A CE  1 
ATOM   2021 N  NZ  . LYS A 1 251 ? 5.438   -1.692  31.229  1.00  21.90 ? 252 LYS A NZ  1 
ATOM   2022 N  N   . ASN A 1 252 ? -0.483  -1.428  35.911  1.00  16.31 ? 253 ASN A N   1 
ATOM   2023 C  CA  . ASN A 1 252 ? -1.326  -0.936  36.967  1.00  21.93 ? 253 ASN A CA  1 
ATOM   2024 C  C   . ASN A 1 252 ? -2.704  -0.521  36.417  1.00  20.27 ? 253 ASN A C   1 
ATOM   2025 O  O   . ASN A 1 252 ? -2.967  0.749   36.447  1.00  26.13 ? 253 ASN A O   1 
ATOM   2026 C  CB  . ASN A 1 252 ? -0.613  0.283   37.622  1.00  26.78 ? 253 ASN A CB  1 
ATOM   2027 C  CG  . ASN A 1 252 ? -1.294  0.735   38.911  1.00  33.72 ? 253 ASN A CG  1 
ATOM   2028 O  OD1 . ASN A 1 252 ? -1.851  -0.096  39.664  1.00  38.89 ? 253 ASN A OD1 1 
ATOM   2029 N  ND2 . ASN A 1 252 ? -1.300  2.057   39.149  1.00  36.82 ? 253 ASN A ND2 1 
ATOM   2030 N  N   . ARG A 1 253 ? -3.472  -1.486  35.819  1.00  15.00 ? 254 ARG A N   1 
ATOM   2031 C  CA  . ARG A 1 253 ? -4.765  -1.107  35.294  1.00  13.77 ? 254 ARG A CA  1 
ATOM   2032 C  C   . ARG A 1 253 ? -5.767  -2.115  35.732  1.00  14.24 ? 254 ARG A C   1 
ATOM   2033 O  O   . ARG A 1 253 ? -5.439  -3.273  35.856  1.00  17.80 ? 254 ARG A O   1 
ATOM   2034 C  CB  . ARG A 1 253 ? -4.754  -1.011  33.711  1.00  12.52 ? 254 ARG A CB  1 
ATOM   2035 C  CG  . ARG A 1 253 ? -3.960  0.151   33.239  1.00  10.90 ? 254 ARG A CG  1 
ATOM   2036 C  CD  . ARG A 1 253 ? -3.854  0.085   31.704  1.00  10.89 ? 254 ARG A CD  1 
ATOM   2037 N  NE  . ARG A 1 253 ? -2.936  -1.012  31.282  1.00  11.02 ? 254 ARG A NE  1 
ATOM   2038 C  CZ  . ARG A 1 253 ? -2.654  -1.270  29.995  1.00  9.61  ? 254 ARG A CZ  1 
ATOM   2039 N  NH1 . ARG A 1 253 ? -3.290  -0.586  29.047  1.00  8.73  ? 254 ARG A NH1 1 
ATOM   2040 N  NH2 . ARG A 1 253 ? -1.807  -2.253  29.653  1.00  9.59  ? 254 ARG A NH2 1 
ATOM   2041 N  N   . GLN A 1 254 ? -7.052  -1.707  35.855  1.00  15.06 ? 255 GLN A N   1 
ATOM   2042 C  CA  . GLN A 1 254 ? -8.171  -2.617  36.086  1.00  17.38 ? 255 GLN A CA  1 
ATOM   2043 C  C   . GLN A 1 254 ? -9.167  -2.497  34.892  1.00  15.49 ? 255 GLN A C   1 
ATOM   2044 O  O   . GLN A 1 254 ? -9.533  -1.395  34.468  1.00  19.52 ? 255 GLN A O   1 
ATOM   2045 C  CB  . GLN A 1 254 ? -8.926  -2.315  37.436  1.00  22.62 ? 255 GLN A CB  1 
ATOM   2046 C  CG  . GLN A 1 254 ? -9.722  -3.553  37.921  1.00  29.90 ? 255 GLN A CG  1 
ATOM   2047 C  CD  . GLN A 1 254 ? -10.481 -3.388  39.234  1.00  34.26 ? 255 GLN A CD  1 
ATOM   2048 O  OE1 . GLN A 1 254 ? -11.192 -2.405  39.426  1.00  38.69 ? 255 GLN A OE1 1 
ATOM   2049 N  NE2 . GLN A 1 254 ? -10.362 -4.389  40.134  1.00  32.10 ? 255 GLN A NE2 1 
ATOM   2050 N  N   . ILE A 1 255 ? -9.533  -3.656  34.385  1.00  13.44 ? 256 ILE A N   1 
ATOM   2051 C  CA  . ILE A 1 255 ? -10.562 -3.717  33.342  1.00  13.53 ? 256 ILE A CA  1 
ATOM   2052 C  C   . ILE A 1 255 ? -11.930 -3.688  33.987  1.00  12.63 ? 256 ILE A C   1 
ATOM   2053 O  O   . ILE A 1 255 ? -12.116 -4.373  35.002  1.00  13.44 ? 256 ILE A O   1 
ATOM   2054 C  CB  . ILE A 1 255 ? -10.377 -4.939  32.462  1.00  12.74 ? 256 ILE A CB  1 
ATOM   2055 C  CG1 . ILE A 1 255 ? -8.956  -4.922  31.826  1.00  13.91 ? 256 ILE A CG1 1 
ATOM   2056 C  CG2 . ILE A 1 255 ? -11.531 -5.080  31.442  1.00  12.76 ? 256 ILE A CG2 1 
ATOM   2057 C  CD1 . ILE A 1 255 ? -8.661  -6.244  31.072  1.00  14.43 ? 256 ILE A CD1 1 
ATOM   2058 N  N   . LYS A 1 256 ? -12.798 -2.806  33.514  1.00  11.14 ? 257 LYS A N   1 
ATOM   2059 C  CA  . LYS A 1 256 ? -14.178 -2.624  34.040  1.00  11.42 ? 257 LYS A CA  1 
ATOM   2060 C  C   . LYS A 1 256 ? -15.136 -3.260  33.114  1.00  11.79 ? 257 LYS A C   1 
ATOM   2061 O  O   . LYS A 1 256 ? -14.956 -3.250  31.905  1.00  12.10 ? 257 LYS A O   1 
ATOM   2062 C  CB  . LYS A 1 256 ? -14.475 -1.137  34.218  1.00  13.84 ? 257 LYS A CB  1 
ATOM   2063 C  CG  . LYS A 1 256 ? -13.472 -0.423  35.165  1.00  21.13 ? 257 LYS A CG  1 
ATOM   2064 C  CD  . LYS A 1 256 ? -14.181 0.632   36.016  1.00  32.09 ? 257 LYS A CD  1 
ATOM   2065 C  CE  . LYS A 1 256 ? -13.193 1.395   36.917  1.00  35.61 ? 257 LYS A CE  1 
ATOM   2066 N  NZ  . LYS A 1 256 ? -12.949 2.835   36.552  1.00  36.71 ? 257 LYS A NZ  1 
ATOM   2067 N  N   . ALA A 1 257 ? -16.199 -3.865  33.613  1.00  11.93 ? 258 ALA A N   1 
ATOM   2068 C  CA  . ALA A 1 257 ? -17.288 -4.494  32.832  1.00  11.75 ? 258 ALA A CA  1 
ATOM   2069 C  C   . ALA A 1 257 ? -18.586 -3.750  32.986  1.00  12.11 ? 258 ALA A C   1 
ATOM   2070 O  O   . ALA A 1 257 ? -18.948 -3.317  34.141  1.00  12.75 ? 258 ALA A O   1 
ATOM   2071 C  CB  . ALA A 1 257 ? -17.453 -5.987  33.193  1.00  12.12 ? 258 ALA A CB  1 
ATOM   2072 N  N   . SER A 1 258 ? -19.347 -3.622  31.947  1.00  11.73 ? 259 SER A N   1 
ATOM   2073 C  CA  . SER A 1 258 ? -20.642 -2.954  32.036  1.00  12.57 ? 259 SER A CA  1 
ATOM   2074 C  C   . SER A 1 258 ? -21.734 -3.895  32.465  1.00  14.11 ? 259 SER A C   1 
ATOM   2075 O  O   . SER A 1 258 ? -22.920 -3.449  32.599  1.00  17.63 ? 259 SER A O   1 
ATOM   2076 C  CB  . SER A 1 258 ? -21.009 -2.289  30.704  1.00  11.18 ? 259 SER A CB  1 
ATOM   2077 O  OG  . SER A 1 258 ? -21.455 -3.271  29.787  1.00  13.23 ? 259 SER A OG  1 
ATOM   2078 N  N   . PHE A 1 259 ? -21.420 -5.120  32.719  1.00  13.84 ? 260 PHE A N   1 
ATOM   2079 C  CA  . PHE A 1 259 ? -22.432 -6.184  32.829  1.00  16.57 ? 260 PHE A CA  1 
ATOM   2080 C  C   . PHE A 1 259 ? -21.917 -7.180  33.856  1.00  20.86 ? 260 PHE A C   1 
ATOM   2081 O  O   . PHE A 1 259 ? -20.714 -7.269  34.139  1.00  19.29 ? 260 PHE A O   1 
ATOM   2082 C  CB  . PHE A 1 259 ? -22.680 -6.910  31.490  1.00  19.29 ? 260 PHE A CB  1 
ATOM   2083 C  CG  . PHE A 1 259 ? -21.413 -7.615  30.963  1.00  18.15 ? 260 PHE A CG  1 
ATOM   2084 C  CD1 . PHE A 1 259 ? -20.451 -6.881  30.274  1.00  16.91 ? 260 PHE A CD1 1 
ATOM   2085 C  CD2 . PHE A 1 259 ? -21.162 -8.964  31.235  1.00  19.00 ? 260 PHE A CD2 1 
ATOM   2086 C  CE1 . PHE A 1 259 ? -19.262 -7.485  29.834  1.00  16.87 ? 260 PHE A CE1 1 
ATOM   2087 C  CE2 . PHE A 1 259 ? -19.969 -9.569  30.800  1.00  18.00 ? 260 PHE A CE2 1 
ATOM   2088 C  CZ  . PHE A 1 259 ? -19.007 -8.820  30.055  1.00  19.13 ? 260 PHE A CZ  1 
ATOM   2089 N  N   . LYS A 1 260 ? -22.921 -7.839  34.448  1.00  28.55 ? 261 LYS A N   1 
ATOM   2090 C  CA  . LYS A 1 260 ? -22.878 -9.034  35.337  1.00  40.08 ? 261 LYS A CA  1 
ATOM   2091 C  C   . LYS A 1 260 ? -22.503 -8.859  36.792  1.00  47.72 ? 261 LYS A C   1 
ATOM   2092 O  O   . LYS A 1 260 ? -23.038 -9.539  37.662  1.00  56.81 ? 261 LYS A O   1 
ATOM   2093 C  CB  . LYS A 1 260 ? -22.278 -10.285 34.684  1.00  36.10 ? 261 LYS A CB  1 
ATOM   2094 C  CG  . LYS A 1 260 ? -23.201 -10.886 33.627  1.00  32.15 ? 261 LYS A CG  1 
ATOM   2095 C  CD  . LYS A 1 260 ? -22.839 -12.330 33.305  0.010 32.85 ? 261 LYS A CD  1 
ATOM   2096 C  CE  . LYS A 1 260 ? -21.596 -12.435 32.433  0.010 31.89 ? 261 LYS A CE  1 
ATOM   2097 N  NZ  . LYS A 1 260 ? -21.239 -13.850 32.139  0.010 32.09 ? 261 LYS A NZ  1 
ATOM   2098 O  OXT . LYS A 1 260 ? -21.730 -7.979  37.144  1.00  57.71 ? 261 LYS A OXT 1 
HETATM 2099 ZN ZN  . ZN  B 2 .   ? -6.594  -1.675  15.234  1.00  6.83  ? 301 ZN  A ZN  1 
HETATM 2100 O  O20 A EWY C 3 .   ? -6.105  10.667  8.402   0.50  38.02 ? 302 EWY A O20 1 
HETATM 2101 O  O20 B EWY C 3 .   ? -4.010  -0.685  13.964  0.50  33.11 ? 302 EWY A O20 1 
HETATM 2102 C  C18 A EWY C 3 .   ? -5.475  9.875   9.089   0.50  34.36 ? 302 EWY A C18 1 
HETATM 2103 C  C18 B EWY C 3 .   ? -3.837  -0.159  12.869  0.50  26.00 ? 302 EWY A C18 1 
HETATM 2104 C  C22 A EWY C 3 .   ? -4.070  9.853   9.131   0.50  35.03 ? 302 EWY A C22 1 
HETATM 2105 C  C22 B EWY C 3 .   ? -4.625  -0.493  11.815  0.50  25.35 ? 302 EWY A C22 1 
HETATM 2106 C  C17 A EWY C 3 .   ? -3.413  8.898   9.927   0.50  35.25 ? 302 EWY A C17 1 
HETATM 2107 C  C17 B EWY C 3 .   ? -4.446  0.139   10.620  0.50  19.67 ? 302 EWY A C17 1 
HETATM 2108 C  C21 A EWY C 3 .   ? -1.913  8.857   9.989   0.50  33.43 ? 302 EWY A C21 1 
HETATM 2109 C  C21 B EWY C 3 .   ? -5.310  -0.153  9.467   0.50  25.18 ? 302 EWY A C21 1 
HETATM 2110 N  N16 A EWY C 3 .   ? -4.149  8.004   10.656  0.50  32.89 ? 302 EWY A N16 1 
HETATM 2111 N  N16 B EWY C 3 .   ? -3.454  0.968   10.402  0.50  28.70 ? 302 EWY A N16 1 
HETATM 2112 N  N19 A EWY C 3 .   ? -6.158  8.951   9.821   0.50  30.34 ? 302 EWY A N19 1 
HETATM 2113 N  N19 B EWY C 3 .   ? -2.819  0.742   12.657  0.50  32.87 ? 302 EWY A N19 1 
HETATM 2114 C  C15 A EWY C 3 .   ? -5.515  8.042   10.588  0.50  27.02 ? 302 EWY A C15 1 
HETATM 2115 C  C15 B EWY C 3 .   ? -2.662  1.280   11.426  0.50  30.13 ? 302 EWY A C15 1 
HETATM 2116 S  S14 A EWY C 3 .   ? -6.607  6.944   11.440  0.50  22.15 ? 302 EWY A S14 1 
HETATM 2117 S  S14 B EWY C 3 .   ? -1.418  2.436   11.052  0.50  31.77 ? 302 EWY A S14 1 
HETATM 2118 C  C13 A EWY C 3 .   ? -5.333  6.072   12.440  0.50  15.95 ? 302 EWY A C13 1 
HETATM 2119 C  C13 B EWY C 3 .   ? -2.682  3.629   11.577  0.50  29.87 ? 302 EWY A C13 1 
HETATM 2120 C  C11 A EWY C 3 .   ? -5.908  4.953   13.248  0.50  11.84 ? 302 EWY A C11 1 
HETATM 2121 C  C11 B EWY C 3 .   ? -2.769  3.722   13.097  0.50  24.09 ? 302 EWY A C11 1 
HETATM 2122 O  O12 A EWY C 3 .   ? -7.148  4.847   13.214  0.50  12.54 ? 302 EWY A O12 1 
HETATM 2123 O  O12 B EWY C 3 .   ? -1.749  4.143   13.681  0.50  29.10 ? 302 EWY A O12 1 
HETATM 2124 C  C2  A EWY C 3 .   ? -5.099  4.014   14.046  0.50  9.70  ? 302 EWY A C2  1 
HETATM 2125 C  C2  B EWY C 3 .   ? -3.962  3.488   14.008  0.50  20.49 ? 302 EWY A C2  1 
HETATM 2126 C  C3  A EWY C 3 .   ? -5.704  2.998   14.825  0.50  8.91  ? 302 EWY A C3  1 
HETATM 2127 C  C3  B EWY C 3 .   ? -4.223  2.303   14.756  0.50  17.71 ? 302 EWY A C3  1 
HETATM 2128 C  C4  A EWY C 3 .   ? -4.979  2.088   15.570  0.50  7.91  ? 302 EWY A C4  1 
HETATM 2129 C  C4  B EWY C 3 .   ? -5.328  2.259   15.618  0.50  14.44 ? 302 EWY A C4  1 
HETATM 2130 S  S7  A EWY C 3 .   ? -5.761  0.880   16.644  0.50  7.06  ? 302 EWY A S7  1 
HETATM 2131 S  S7  B EWY C 3 .   ? -5.770  0.889   16.643  0.50  12.01 ? 302 EWY A S7  1 
HETATM 2132 O  O9  A EWY C 3 .   ? -7.226  0.930   16.548  0.50  6.63  ? 302 EWY A O9  1 
HETATM 2133 O  O9  B EWY C 3 .   ? -7.263  0.885   16.600  0.50  11.60 ? 302 EWY A O9  1 
HETATM 2134 N  N10 A EWY C 3 .   ? -5.241  -0.544  16.123  0.50  6.94  ? 302 EWY A N10 1 
HETATM 2135 N  N10 B EWY C 3 .   ? -5.187  -0.581  16.045  0.50  13.18 ? 302 EWY A N10 1 
HETATM 2136 O  O8  A EWY C 3 .   ? -5.249  1.119   18.037  0.50  5.92  ? 302 EWY A O8  1 
HETATM 2137 O  O8  B EWY C 3 .   ? -5.241  1.094   18.042  0.50  10.09 ? 302 EWY A O8  1 
HETATM 2138 C  C5  A EWY C 3 .   ? -3.573  2.224   15.600  0.50  8.58  ? 302 EWY A C5  1 
HETATM 2139 C  C5  B EWY C 3 .   ? -6.185  3.333   15.823  0.50  14.91 ? 302 EWY A C5  1 
HETATM 2140 C  C6  A EWY C 3 .   ? -2.965  3.219   14.804  0.50  9.02  ? 302 EWY A C6  1 
HETATM 2141 C  C6  B EWY C 3 .   ? -5.961  4.496   15.091  0.50  16.16 ? 302 EWY A C6  1 
HETATM 2142 C  C1  A EWY C 3 .   ? -3.675  4.159   14.106  0.50  8.81  ? 302 EWY A C1  1 
HETATM 2143 C  C1  B EWY C 3 .   ? -4.879  4.568   14.222  0.50  18.04 ? 302 EWY A C1  1 
HETATM 2144 O  O1  . MES D 4 .   ? -7.259  -9.289  -2.551  1.00  33.28 ? 303 MES A O1  1 
HETATM 2145 C  C2  . MES D 4 .   ? -7.285  -9.903  -3.937  1.00  28.84 ? 303 MES A C2  1 
HETATM 2146 C  C3  . MES D 4 .   ? -8.417  -10.945 -4.156  1.00  29.97 ? 303 MES A C3  1 
HETATM 2147 N  N4  . MES D 4 .   ? -9.623  -10.965 -3.329  1.00  31.00 ? 303 MES A N4  1 
HETATM 2148 C  C5  . MES D 4 .   ? -9.604  -10.215 -2.032  1.00  29.74 ? 303 MES A C5  1 
HETATM 2149 C  C6  . MES D 4 .   ? -8.392  -9.552  -1.668  1.00  29.70 ? 303 MES A C6  1 
HETATM 2150 C  C7  . MES D 4 .   ? -10.880 -11.719 -3.722  1.00  31.40 ? 303 MES A C7  1 
HETATM 2151 C  C8  . MES D 4 .   ? -12.317 -11.327 -3.094  1.00  28.18 ? 303 MES A C8  1 
HETATM 2152 S  S   . DMS E 5 .   ? 1.450   -11.712 14.867  1.00  24.70 ? 304 DMS A S   1 
HETATM 2153 O  O   . DMS E 5 .   ? 2.217   -13.126 14.615  1.00  26.77 ? 304 DMS A O   1 
HETATM 2154 C  C1  . DMS E 5 .   ? 1.797   -11.612 16.562  1.00  16.41 ? 304 DMS A C1  1 
HETATM 2155 C  C2  . DMS E 5 .   ? 2.698   -10.564 14.370  1.00  21.75 ? 304 DMS A C2  1 
HETATM 2156 S  S   . DMS F 5 .   ? 10.900  -1.040  13.938  1.00  55.84 ? 305 DMS A S   1 
HETATM 2157 O  O   . DMS F 5 .   ? 9.664   -0.125  14.556  1.00  41.11 ? 305 DMS A O   1 
HETATM 2158 C  C1  . DMS F 5 .   ? 11.644  -0.894  15.567  1.00  35.34 ? 305 DMS A C1  1 
HETATM 2159 C  C2  . DMS F 5 .   ? 10.343  -2.667  13.879  1.00  31.52 ? 305 DMS A C2  1 
HETATM 2160 O  O   . HOH G 6 .   ? -16.966 -8.451  20.430  1.00  8.72  ? 401 HOH A O   1 
HETATM 2161 O  O   . HOH G 6 .   ? -1.144  -4.093  15.709  1.00  9.41  ? 402 HOH A O   1 
HETATM 2162 O  O   . HOH G 6 .   ? -7.868  -15.437 11.260  1.00  9.89  ? 403 HOH A O   1 
HETATM 2163 O  O   . HOH G 6 .   ? -3.302  -13.349 25.076  1.00  12.88 ? 404 HOH A O   1 
HETATM 2164 O  O   . HOH G 6 .   ? -17.961 -20.510 8.051   1.00  12.04 ? 405 HOH A O   1 
HETATM 2165 O  O   . HOH G 6 .   ? -2.422  -8.835  29.086  1.00  12.28 ? 406 HOH A O   1 
HETATM 2166 O  O   . HOH G 6 .   ? -10.571 8.666   25.641  1.00  10.74 ? 407 HOH A O   1 
HETATM 2167 O  O   . HOH G 6 .   ? 5.020   -4.961  20.918  1.00  13.55 ? 408 HOH A O   1 
HETATM 2168 O  O   . HOH G 6 .   ? -3.623  -15.963 24.238  1.00  13.59 ? 409 HOH A O   1 
HETATM 2169 O  O   . HOH G 6 .   ? -21.522 -7.124  23.454  1.00  11.20 ? 410 HOH A O   1 
HETATM 2170 O  O   . HOH G 6 .   ? -3.442  -11.194 20.810  1.00  11.41 ? 411 HOH A O   1 
HETATM 2171 O  O   . HOH G 6 .   ? -21.924 5.719   4.705   1.00  15.50 ? 412 HOH A O   1 
HETATM 2172 O  O   . HOH G 6 .   ? -1.981  -12.403 22.837  1.00  11.46 ? 413 HOH A O   1 
HETATM 2173 O  O   . HOH G 6 .   ? -24.045 -0.796  26.424  1.00  17.46 ? 414 HOH A O   1 
HETATM 2174 O  O   . HOH G 6 .   ? -21.008 -12.700 -1.821  1.00  15.33 ? 415 HOH A O   1 
HETATM 2175 O  O   . HOH G 6 .   ? -16.346 -10.015 32.710  1.00  15.16 ? 416 HOH A O   1 
HETATM 2176 O  O   . HOH G 6 .   ? -24.933 -7.770  9.027   1.00  16.38 ? 417 HOH A O   1 
HETATM 2177 O  O   . HOH G 6 .   ? 1.313   -1.684  29.434  1.00  13.24 ? 418 HOH A O   1 
HETATM 2178 O  O   . HOH G 6 .   ? -9.938  14.561  12.082  1.00  16.55 ? 419 HOH A O   1 
HETATM 2179 O  O   . HOH G 6 .   ? 3.811   5.072   29.645  1.00  18.80 ? 420 HOH A O   1 
HETATM 2180 O  O   . HOH G 6 .   ? 7.786   6.118   21.724  1.00  16.87 ? 421 HOH A O   1 
HETATM 2181 O  O   . HOH G 6 .   ? -17.792 -21.975 6.020   1.00  12.33 ? 422 HOH A O   1 
HETATM 2182 O  O   . HOH G 6 .   ? -26.815 -2.737  14.357  1.00  20.49 ? 423 HOH A O   1 
HETATM 2183 O  O   . HOH G 6 .   ? -19.458 10.019  8.972   1.00  14.89 ? 424 HOH A O   1 
HETATM 2184 O  O   . HOH G 6 .   ? 5.556   7.170   20.209  1.00  18.36 ? 425 HOH A O   1 
HETATM 2185 O  O   . HOH G 6 .   ? -17.991 10.465  11.352  1.00  18.78 ? 426 HOH A O   1 
HETATM 2186 O  O   . HOH G 6 .   ? 8.668   -3.869  21.116  1.00  14.47 ? 427 HOH A O   1 
HETATM 2187 O  O   . HOH G 6 .   ? -23.810 -0.926  3.887   1.00  22.66 ? 428 HOH A O   1 
HETATM 2188 O  O   . HOH G 6 .   ? -23.234 -3.042  6.605   1.00  17.93 ? 429 HOH A O   1 
HETATM 2189 O  O   . HOH G 6 .   ? -10.271 -18.219 16.814  1.00  19.62 ? 430 HOH A O   1 
HETATM 2190 O  O   . HOH G 6 .   ? -8.903  -6.200  35.681  1.00  17.90 ? 431 HOH A O   1 
HETATM 2191 O  O   . HOH G 6 .   ? -14.184 10.677  27.595  1.00  19.61 ? 432 HOH A O   1 
HETATM 2192 O  O   . HOH G 6 .   ? 1.380   8.813   24.358  1.00  16.58 ? 433 HOH A O   1 
HETATM 2193 O  O   . HOH G 6 .   ? -30.736 1.516   25.972  1.00  23.39 ? 434 HOH A O   1 
HETATM 2194 O  O   . HOH G 6 .   ? 2.659   -11.268 9.545   1.00  24.70 ? 435 HOH A O   1 
HETATM 2195 O  O   . HOH G 6 .   ? -11.949 2.936   30.683  1.00  22.37 ? 436 HOH A O   1 
HETATM 2196 O  O   . HOH G 6 .   ? -10.488 5.530   37.894  1.00  20.23 ? 437 HOH A O   1 
HETATM 2197 O  O   . HOH G 6 .   ? 4.545   -3.508  26.444  1.00  18.95 ? 438 HOH A O   1 
HETATM 2198 O  O   . HOH G 6 .   ? -13.256 -22.367 11.555  1.00  31.66 ? 439 HOH A O   1 
HETATM 2199 O  O   . HOH G 6 .   ? -6.062  -4.531  -6.476  1.00  22.76 ? 440 HOH A O   1 
HETATM 2200 O  O   . HOH G 6 .   ? -20.408 10.848  26.550  1.00  16.88 ? 441 HOH A O   1 
HETATM 2201 O  O   . HOH G 6 .   ? -1.025  -11.234 28.953  1.00  19.76 ? 442 HOH A O   1 
HETATM 2202 O  O   . HOH G 6 .   ? -22.693 -5.884  2.765   1.00  20.59 ? 443 HOH A O   1 
HETATM 2203 O  O   . HOH G 6 .   ? -26.592 -11.337 1.931   1.00  27.92 ? 444 HOH A O   1 
HETATM 2204 O  O   . HOH G 6 .   ? 7.946   -1.897  -10.276 1.00  21.79 ? 445 HOH A O   1 
HETATM 2205 O  O   . HOH G 6 .   ? -8.632  -3.851  7.831   1.00  14.73 ? 446 HOH A O   1 
HETATM 2206 O  O   . HOH G 6 .   ? -8.062  -19.414 21.567  1.00  21.48 ? 447 HOH A O   1 
HETATM 2207 O  O   . HOH G 6 .   ? -16.023 -12.441 24.290  1.00  20.53 ? 448 HOH A O   1 
HETATM 2208 O  O   . HOH G 6 .   ? -11.051 -19.228 6.784   1.00  24.96 ? 449 HOH A O   1 
HETATM 2209 O  O   . HOH G 6 .   ? -28.730 0.147   24.420  1.00  21.77 ? 450 HOH A O   1 
HETATM 2210 O  O   . HOH G 6 .   ? 2.717   -4.155  7.890   1.00  23.24 ? 451 HOH A O   1 
HETATM 2211 O  O   . HOH G 6 .   ? -4.667  -11.956 31.955  1.00  23.49 ? 452 HOH A O   1 
HETATM 2212 O  O   . HOH G 6 .   ? -8.126  -15.186 36.893  1.00  24.15 ? 453 HOH A O   1 
HETATM 2213 O  O   . HOH G 6 .   ? -17.728 -21.392 17.612  1.00  28.64 ? 454 HOH A O   1 
HETATM 2214 O  O   . HOH G 6 .   ? -7.963  7.029   27.728  1.00  25.88 ? 455 HOH A O   1 
HETATM 2215 O  O   . HOH G 6 .   ? 1.509   -11.802 25.090  1.00  23.53 ? 456 HOH A O   1 
HETATM 2216 O  O   . HOH G 6 .   ? -16.097 15.868  23.594  1.00  18.80 ? 457 HOH A O   1 
HETATM 2217 O  O   . HOH G 6 .   ? -26.859 -4.138  25.058  1.00  19.92 ? 458 HOH A O   1 
HETATM 2218 O  O   . HOH G 6 .   ? -18.549 -9.113  34.316  1.00  24.89 ? 459 HOH A O   1 
HETATM 2219 O  O   . HOH G 6 .   ? -0.391  10.873  23.443  1.00  19.36 ? 460 HOH A O   1 
HETATM 2220 O  O   . HOH G 6 .   ? -19.470 -23.688 6.007   1.00  19.59 ? 461 HOH A O   1 
HETATM 2221 O  O   . HOH G 6 .   ? -2.455  -3.191  11.485  1.00  21.10 ? 462 HOH A O   1 
HETATM 2222 O  O   . HOH G 6 .   ? 8.035   -5.931  -10.564 1.00  27.25 ? 463 HOH A O   1 
HETATM 2223 O  O   . HOH G 6 .   ? -6.598  -20.153 19.385  1.00  21.23 ? 464 HOH A O   1 
HETATM 2224 O  O   . HOH G 6 .   ? -25.579 -10.681 17.683  1.00  20.74 ? 465 HOH A O   1 
HETATM 2225 O  O   . HOH G 6 .   ? -26.331 3.587   15.308  1.00  25.87 ? 466 HOH A O   1 
HETATM 2226 O  O   . HOH G 6 .   ? -22.602 -14.512 11.029  1.00  17.91 ? 467 HOH A O   1 
HETATM 2227 O  O   . HOH G 6 .   ? -27.902 4.894   25.182  1.00  28.76 ? 468 HOH A O   1 
HETATM 2228 O  O   . HOH G 6 .   ? -13.018 -18.392 14.674  1.00  28.22 ? 469 HOH A O   1 
HETATM 2229 O  O   . HOH G 6 .   ? 4.533   -6.440  7.894   1.00  25.02 ? 470 HOH A O   1 
HETATM 2230 O  O   . HOH G 6 .   ? -4.174  -8.819  31.190  1.00  24.14 ? 471 HOH A O   1 
HETATM 2231 O  O   . HOH G 6 .   ? 0.204   0.963   34.538  1.00  21.30 ? 472 HOH A O   1 
HETATM 2232 O  O   . HOH G 6 .   ? -23.175 -0.858  34.375  1.00  27.64 ? 473 HOH A O   1 
HETATM 2233 O  O   . HOH G 6 .   ? 0.141   -0.923  -4.759  1.00  22.87 ? 474 HOH A O   1 
HETATM 2234 O  O   . HOH G 6 .   ? -22.072 -18.530 13.552  1.00  22.53 ? 475 HOH A O   1 
HETATM 2235 O  O   . HOH G 6 .   ? -1.165  -17.725 17.884  1.00  27.44 ? 476 HOH A O   1 
HETATM 2236 O  O   . HOH G 6 .   ? -5.608  3.678   -5.738  1.00  28.27 ? 477 HOH A O   1 
HETATM 2237 O  O   . HOH G 6 .   ? -7.323  -8.919  32.551  1.00  21.96 ? 478 HOH A O   1 
HETATM 2238 O  O   . HOH G 6 .   ? -19.464 -20.601 4.934   1.00  22.69 ? 479 HOH A O   1 
HETATM 2239 O  O   . HOH G 6 .   ? 4.348   -2.467  28.775  1.00  29.35 ? 480 HOH A O   1 
HETATM 2240 O  O   . HOH G 6 .   ? -19.839 -16.948 3.075   1.00  24.13 ? 481 HOH A O   1 
HETATM 2241 O  O   . HOH G 6 .   ? -26.097 -6.373  13.099  1.00  28.90 ? 482 HOH A O   1 
HETATM 2242 O  O   . HOH G 6 .   ? -25.616 -15.383 7.875   1.00  27.89 ? 483 HOH A O   1 
HETATM 2243 O  O   . HOH G 6 .   ? -1.686  -13.317 27.485  1.00  26.78 ? 484 HOH A O   1 
HETATM 2244 O  O   . HOH G 6 .   ? -9.590  -8.218  33.787  1.00  24.53 ? 485 HOH A O   1 
HETATM 2245 O  O   . HOH G 6 .   ? -24.703 -9.353  1.986   1.00  26.92 ? 486 HOH A O   1 
HETATM 2246 O  O   . HOH G 6 .   ? 5.467   -7.027  22.446  1.00  30.84 ? 487 HOH A O   1 
HETATM 2247 O  O   . HOH G 6 .   ? -0.443  -8.713  32.231  1.00  23.95 ? 488 HOH A O   1 
HETATM 2248 O  O   . HOH G 6 .   ? -14.165 -16.722 28.756  1.00  30.84 ? 489 HOH A O   1 
HETATM 2249 O  O   . HOH G 6 .   ? 3.954   9.895   23.660  1.00  25.35 ? 490 HOH A O   1 
HETATM 2250 O  O   . HOH G 6 .   ? -23.821 -7.201  0.168   1.00  28.36 ? 491 HOH A O   1 
HETATM 2251 O  O   . HOH G 6 .   ? -1.362  11.299  25.876  1.00  29.07 ? 492 HOH A O   1 
HETATM 2252 O  O   . HOH G 6 .   ? -2.704  -17.816 5.436   1.00  29.49 ? 493 HOH A O   1 
HETATM 2253 O  O   . HOH G 6 .   ? -12.550 -17.359 16.766  1.00  25.81 ? 494 HOH A O   1 
HETATM 2254 O  O   . HOH G 6 .   ? -24.105 8.761   20.170  1.00  24.94 ? 495 HOH A O   1 
HETATM 2255 O  O   . HOH G 6 .   ? 2.801   -12.977 5.186   1.00  26.04 ? 496 HOH A O   1 
HETATM 2256 O  O   . HOH G 6 .   ? 1.530   -17.495 7.226   1.00  32.89 ? 497 HOH A O   1 
HETATM 2257 O  O   . HOH G 6 .   ? 9.864   -4.379  -7.841  1.00  24.67 ? 498 HOH A O   1 
HETATM 2258 O  O   . HOH G 6 .   ? -11.112 -15.403 33.870  1.00  27.27 ? 499 HOH A O   1 
HETATM 2259 O  O   . HOH G 6 .   ? -23.714 16.702  2.604   1.00  29.77 ? 500 HOH A O   1 
HETATM 2260 O  O   . HOH G 6 .   ? -21.177 13.593  1.849   1.00  30.76 ? 501 HOH A O   1 
HETATM 2261 O  O   . HOH G 6 .   ? -16.869 -7.204  39.906  1.00  29.75 ? 502 HOH A O   1 
HETATM 2262 O  O   . HOH G 6 .   ? -0.064  -14.445 22.082  1.00  26.95 ? 503 HOH A O   1 
HETATM 2263 O  O   . HOH G 6 .   ? -7.076  -16.904 1.389   1.00  23.58 ? 504 HOH A O   1 
HETATM 2264 O  O   . HOH G 6 .   ? 2.330   8.122   27.650  1.00  27.03 ? 505 HOH A O   1 
HETATM 2265 O  O   . HOH G 6 .   ? 8.382   3.013   27.691  1.00  26.95 ? 506 HOH A O   1 
HETATM 2266 O  O   . HOH G 6 .   ? -0.244  -19.653 6.509   1.00  30.46 ? 507 HOH A O   1 
HETATM 2267 O  O   . HOH G 6 .   ? -17.266 -8.435  -6.302  1.00  27.16 ? 508 HOH A O   1 
HETATM 2268 O  O   . HOH G 6 .   ? 0.978   -6.743  34.473  1.00  23.60 ? 509 HOH A O   1 
HETATM 2269 O  O   . HOH G 6 .   ? -18.696 -12.185 -3.392  1.00  26.64 ? 510 HOH A O   1 
HETATM 2270 O  O   . HOH G 6 .   ? -17.320 -23.048 3.945   1.00  26.83 ? 511 HOH A O   1 
HETATM 2271 O  O   . HOH G 6 .   ? -14.230 14.437  26.856  1.00  29.46 ? 512 HOH A O   1 
HETATM 2272 O  O   . HOH G 6 .   ? -4.427  -13.576 17.921  1.00  8.79  ? 513 HOH A O   1 
HETATM 2273 O  O   . HOH G 6 .   ? 13.142  -5.805  24.481  1.00  27.56 ? 514 HOH A O   1 
HETATM 2274 O  O   . HOH G 6 .   ? -23.967 -2.471  28.898  1.00  25.52 ? 515 HOH A O   1 
HETATM 2275 O  O   . HOH G 6 .   ? -3.510  -12.913 -2.921  1.00  29.60 ? 516 HOH A O   1 
HETATM 2276 O  O   . HOH G 6 .   ? 2.332   -14.294 20.543  1.00  35.75 ? 517 HOH A O   1 
HETATM 2277 O  O   . HOH G 6 .   ? -16.956 -14.016 37.230  1.00  30.18 ? 518 HOH A O   1 
HETATM 2278 O  O   . HOH G 6 .   ? 1.723   12.549  22.895  1.00  31.63 ? 519 HOH A O   1 
HETATM 2279 O  O   . HOH G 6 .   ? 14.262  -1.627  28.354  1.00  33.09 ? 520 HOH A O   1 
HETATM 2280 O  O   . HOH G 6 .   ? -25.125 -3.046  31.694  1.00  29.30 ? 521 HOH A O   1 
HETATM 2281 O  O   . HOH G 6 .   ? -25.965 6.101   26.877  1.00  26.14 ? 522 HOH A O   1 
HETATM 2282 O  O   . HOH G 6 .   ? -27.672 2.577   23.544  1.00  32.54 ? 523 HOH A O   1 
HETATM 2283 O  O   . HOH G 6 .   ? -25.734 9.732   13.271  1.00  29.00 ? 524 HOH A O   1 
HETATM 2284 O  O   . HOH G 6 .   ? -18.904 12.102  13.053  1.00  23.03 ? 525 HOH A O   1 
HETATM 2285 O  O   . HOH G 6 .   ? -6.262  -19.886 23.969  1.00  31.19 ? 526 HOH A O   1 
HETATM 2286 O  O   . HOH G 6 .   ? -5.840  17.312  27.201  1.00  31.53 ? 527 HOH A O   1 
HETATM 2287 O  O   . HOH G 6 .   ? -24.022 -16.509 3.674   1.00  34.17 ? 528 HOH A O   1 
HETATM 2288 O  O   . HOH G 6 .   ? -13.764 -8.814  -5.237  1.00  23.27 ? 529 HOH A O   1 
HETATM 2289 O  O   . HOH G 6 .   ? -8.509  0.685   -6.567  1.00  24.62 ? 530 HOH A O   1 
HETATM 2290 O  O   . HOH G 6 .   ? 4.536   4.623   -0.689  1.00  25.63 ? 531 HOH A O   1 
HETATM 2291 O  O   . HOH G 6 .   ? 9.550   2.017   12.355  1.00  33.65 ? 532 HOH A O   1 
HETATM 2292 O  O   . HOH G 6 .   ? -9.939  5.269   29.985  1.00  29.09 ? 533 HOH A O   1 
HETATM 2293 O  O   . HOH G 6 .   ? 2.095   -15.531 9.341   1.00  24.32 ? 534 HOH A O   1 
HETATM 2294 O  O   . HOH G 6 .   ? 10.862  -8.705  8.918   1.00  33.78 ? 535 HOH A O   1 
HETATM 2295 O  O   . HOH G 6 .   ? -1.023  9.282   27.839  1.00  28.68 ? 536 HOH A O   1 
HETATM 2296 O  O   . HOH G 6 .   ? 8.831   -4.699  23.615  1.00  27.70 ? 537 HOH A O   1 
HETATM 2297 O  O   . HOH G 6 .   ? -25.092 9.122   26.018  1.00  41.98 ? 538 HOH A O   1 
HETATM 2298 O  O   . HOH G 6 .   ? -4.071  -20.334 6.045   1.00  38.11 ? 539 HOH A O   1 
HETATM 2299 O  O   . HOH G 6 .   ? -22.014 -2.417  -3.898  1.00  35.01 ? 540 HOH A O   1 
HETATM 2300 O  O   . HOH G 6 .   ? -29.112 -3.736  13.418  1.00  28.11 ? 541 HOH A O   1 
HETATM 2301 O  O   . HOH G 6 .   ? -27.487 -0.077  14.991  1.00  28.19 ? 542 HOH A O   1 
HETATM 2302 O  O   . HOH G 6 .   ? -14.099 -21.502 3.418   1.00  33.34 ? 543 HOH A O   1 
HETATM 2303 O  O   . HOH G 6 .   ? 3.626   -8.971  25.615  1.00  32.69 ? 544 HOH A O   1 
HETATM 2304 O  O   . HOH G 6 .   ? -2.028  -12.179 31.241  1.00  30.48 ? 545 HOH A O   1 
HETATM 2305 O  O   . HOH G 6 .   ? -9.170  3.281   34.576  1.00  29.29 ? 546 HOH A O   1 
HETATM 2306 O  O   . HOH G 6 .   ? -14.549 0.675   39.198  1.00  36.59 ? 547 HOH A O   1 
HETATM 2307 O  O   . HOH G 6 .   ? 6.648   5.404   28.405  1.00  30.19 ? 548 HOH A O   1 
HETATM 2308 O  O   . HOH G 6 .   ? -26.690 -1.448  25.830  1.00  23.97 ? 549 HOH A O   1 
HETATM 2309 O  O   . HOH G 6 .   ? 11.296  -6.789  22.321  1.00  31.41 ? 550 HOH A O   1 
HETATM 2310 O  O   . HOH G 6 .   ? -7.187  6.032   6.517   1.00  29.04 ? 551 HOH A O   1 
HETATM 2311 O  O   . HOH G 6 .   ? -8.384  7.491   8.415   1.00  26.54 ? 552 HOH A O   1 
HETATM 2312 O  O   . HOH G 6 .   ? -1.904  7.264   13.750  1.00  33.78 ? 553 HOH A O   1 
HETATM 2313 O  O   . HOH G 6 .   ? -0.349  14.003  16.064  1.00  28.26 ? 554 HOH A O   1 
HETATM 2314 O  O   . HOH G 6 .   ? 6.600   8.516   17.952  1.00  32.99 ? 555 HOH A O   1 
HETATM 2315 O  O   . HOH G 6 .   ? -5.833  15.286  11.767  1.00  32.99 ? 556 HOH A O   1 
HETATM 2316 O  O   . HOH G 6 .   ? -17.454 -16.384 21.772  1.00  31.72 ? 557 HOH A O   1 
HETATM 2317 O  O   . HOH G 6 .   ? -14.359 -18.377 18.758  1.00  35.43 ? 558 HOH A O   1 
HETATM 2318 O  O   . HOH G 6 .   ? -21.177 -22.047 13.844  1.00  28.38 ? 559 HOH A O   1 
HETATM 2319 O  O   . HOH G 6 .   ? -2.831  -9.557  33.909  1.00  39.28 ? 560 HOH A O   1 
HETATM 2320 O  O   . HOH G 6 .   ? -5.642  -11.617 36.111  1.00  35.12 ? 561 HOH A O   1 
HETATM 2321 O  O   . HOH G 6 .   ? -4.674  -20.859 21.331  1.00  26.89 ? 562 HOH A O   1 
HETATM 2322 O  O   . HOH G 6 .   ? -2.307  -19.232 20.967  1.00  33.45 ? 563 HOH A O   1 
HETATM 2323 O  O   . HOH G 6 .   ? -8.440  -20.028 26.732  1.00  29.59 ? 564 HOH A O   1 
HETATM 2324 O  O   . HOH G 6 .   ? -13.155 -16.903 26.182  1.00  28.41 ? 565 HOH A O   1 
HETATM 2325 O  O   . HOH G 6 .   ? -12.486 -18.736 31.789  1.00  34.34 ? 566 HOH A O   1 
HETATM 2326 O  O   . HOH G 6 .   ? -7.821  -19.195 30.552  1.00  30.78 ? 567 HOH A O   1 
HETATM 2327 O  O   . HOH G 6 .   ? -16.490 -15.444 32.552  1.00  34.41 ? 568 HOH A O   1 
HETATM 2328 O  O   . HOH G 6 .   ? -17.848 -12.191 31.819  1.00  28.70 ? 569 HOH A O   1 
HETATM 2329 O  O   . HOH G 6 .   ? -25.057 4.548   8.386   1.00  32.11 ? 570 HOH A O   1 
HETATM 2330 O  O   . HOH G 6 .   ? -26.095 7.908   6.302   1.00  36.32 ? 571 HOH A O   1 
HETATM 2331 O  O   . HOH G 6 .   ? -27.042 -6.592  7.530   1.00  37.21 ? 572 HOH A O   1 
HETATM 2332 O  O   . HOH G 6 .   ? -10.168 13.605  8.967   1.00  28.63 ? 573 HOH A O   1 
HETATM 2333 O  O   . HOH G 6 .   ? 1.192   14.665  24.455  1.00  35.31 ? 574 HOH A O   1 
HETATM 2334 O  O   . HOH G 6 .   ? -26.977 3.287   20.910  1.00  34.26 ? 575 HOH A O   1 
HETATM 2335 O  O   . HOH G 6 .   ? -17.915 -13.414 39.600  1.00  28.11 ? 576 HOH A O   1 
HETATM 2336 O  O   . HOH G 6 .   ? -24.574 -17.713 6.770   1.00  37.37 ? 577 HOH A O   1 
HETATM 2337 O  O   . HOH G 6 .   ? -22.973 -11.742 14.026  1.00  16.89 ? 578 HOH A O   1 
HETATM 2338 O  O   . HOH G 6 .   ? -13.208 -8.952  -3.052  1.00  25.16 ? 579 HOH A O   1 
HETATM 2339 O  O   . HOH G 6 .   ? -13.605 -21.144 14.685  1.00  28.08 ? 580 HOH A O   1 
HETATM 2340 O  O   . HOH G 6 .   ? -0.582  1.164   -10.890 1.00  31.10 ? 581 HOH A O   1 
HETATM 2341 O  O   . HOH G 6 .   ? 6.584   -10.806 14.172  1.00  42.09 ? 582 HOH A O   1 
HETATM 2342 O  O   . HOH G 6 .   ? -11.051 -23.688 12.012  1.00  28.68 ? 583 HOH A O   1 
HETATM 2343 O  O   . HOH G 6 .   ? -12.554 12.718  29.104  1.00  31.93 ? 584 HOH A O   1 
HETATM 2344 O  O   . HOH G 6 .   ? -28.061 5.768   19.346  1.00  35.86 ? 585 HOH A O   1 
HETATM 2345 O  O   . HOH G 6 .   ? -19.050 -4.321  41.388  1.00  33.28 ? 586 HOH A O   1 
HETATM 2346 O  O   . HOH G 6 .   ? -10.160 -19.523 32.211  1.00  31.23 ? 587 HOH A O   1 
HETATM 2347 O  O   . HOH G 6 .   ? -15.908 -10.125 37.797  1.00  46.52 ? 588 HOH A O   1 
HETATM 2348 O  O   . HOH G 6 .   ? -12.057 10.719  5.937   1.00  29.74 ? 589 HOH A O   1 
HETATM 2349 O  O   . HOH G 6 .   ? -17.215 -6.685  42.183  1.00  35.39 ? 590 HOH A O   1 
HETATM 2350 O  O   . HOH G 6 .   ? 2.867   -14.359 0.787   1.00  31.46 ? 591 HOH A O   1 
HETATM 2351 O  O   . HOH G 6 .   ? -14.498 9.166   32.005  1.00  40.09 ? 592 HOH A O   1 
HETATM 2352 O  O   . HOH G 6 .   ? -3.759  -15.645 -1.953  1.00  32.98 ? 593 HOH A O   1 
HETATM 2353 O  O   . HOH G 6 .   ? 5.986   0.945   8.394   1.00  31.86 ? 594 HOH A O   1 
HETATM 2354 O  O   . HOH G 6 .   ? -12.655 8.116   28.844  1.00  33.35 ? 595 HOH A O   1 
HETATM 2355 O  O   . HOH G 6 .   ? -16.909 -14.037 26.384  1.00  31.86 ? 596 HOH A O   1 
HETATM 2356 O  O   . HOH G 6 .   ? 9.267   7.839   18.765  1.00  34.63 ? 597 HOH A O   1 
HETATM 2357 O  O   . HOH G 6 .   ? 3.903   2.919   8.126   1.00  37.86 ? 598 HOH A O   1 
HETATM 2358 O  O   . HOH G 6 .   ? 5.512   9.176   21.780  1.00  36.03 ? 599 HOH A O   1 
HETATM 2359 O  O   . HOH G 6 .   ? 7.149   -3.475  30.001  1.00  35.06 ? 600 HOH A O   1 
HETATM 2360 O  O   . HOH G 6 .   ? -5.077  -9.770  34.060  1.00  40.40 ? 601 HOH A O   1 
HETATM 2361 O  O   . HOH G 6 .   ? -10.014 -19.128 34.372  1.00  29.92 ? 602 HOH A O   1 
HETATM 2362 O  O   . HOH G 6 .   ? -29.699 3.986   27.181  1.00  35.17 ? 603 HOH A O   1 
HETATM 2363 O  O   . HOH G 6 .   ? -11.756 10.594  0.861   1.00  33.19 ? 604 HOH A O   1 
HETATM 2364 O  O   . HOH G 6 .   ? -2.153  4.439   7.929   1.00  38.34 ? 605 HOH A O   1 
HETATM 2365 O  O   . HOH G 6 .   ? 3.827   -2.638  4.419   1.00  36.05 ? 606 HOH A O   1 
HETATM 2366 O  O   . HOH G 6 .   ? -14.079 14.755  5.903   1.00  37.08 ? 607 HOH A O   1 
HETATM 2367 O  O   . HOH G 6 .   ? -12.428 16.313  8.807   1.00  33.78 ? 608 HOH A O   1 
HETATM 2368 O  O   . HOH G 6 .   ? -6.451  -19.486 5.130   1.00  32.45 ? 609 HOH A O   1 
HETATM 2369 O  O   . HOH G 6 .   ? -9.888  -24.140 10.144  1.00  39.36 ? 610 HOH A O   1 
HETATM 2370 O  O   . HOH G 6 .   ? -1.988  -17.581 25.536  1.00  38.34 ? 611 HOH A O   1 
HETATM 2371 O  O   . HOH G 6 .   ? -2.962  -20.340 25.588  1.00  39.49 ? 612 HOH A O   1 
HETATM 2372 O  O   . HOH G 6 .   ? -14.802 20.136  17.433  1.00  35.19 ? 613 HOH A O   1 
HETATM 2373 O  O   . HOH G 6 .   ? 4.438   -11.535 23.359  1.00  35.02 ? 614 HOH A O   1 
HETATM 2374 O  O   . HOH G 6 .   ? 0.858   11.025  15.163  1.00  36.72 ? 615 HOH A O   1 
# 
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 EWY 1   302 1   EWY EWY A . 
D 4 MES 1   303 3   MES MES A . 
E 5 DMS 1   304 1   DMS DMS A . 
F 5 DMS 1   305 2   DMS DMS A . 
G 6 HOH 1   401 1   HOH HOH A . 
G 6 HOH 2   402 2   HOH HOH A . 
G 6 HOH 3   403 3   HOH HOH A . 
G 6 HOH 4   404 4   HOH HOH A . 
G 6 HOH 5   405 5   HOH HOH A . 
G 6 HOH 6   406 6   HOH HOH A . 
G 6 HOH 7   407 7   HOH HOH A . 
G 6 HOH 8   408 8   HOH HOH A . 
G 6 HOH 9   409 9   HOH HOH A . 
G 6 HOH 10  410 10  HOH HOH A . 
G 6 HOH 11  411 11  HOH HOH A . 
G 6 HOH 12  412 12  HOH HOH A . 
G 6 HOH 13  413 13  HOH HOH A . 
G 6 HOH 14  414 14  HOH HOH A . 
G 6 HOH 15  415 15  HOH HOH A . 
G 6 HOH 16  416 16  HOH HOH A . 
G 6 HOH 17  417 17  HOH HOH A . 
G 6 HOH 18  418 18  HOH HOH A . 
G 6 HOH 19  419 19  HOH HOH A . 
G 6 HOH 20  420 20  HOH HOH A . 
G 6 HOH 21  421 21  HOH HOH A . 
G 6 HOH 22  422 22  HOH HOH A . 
G 6 HOH 23  423 23  HOH HOH A . 
G 6 HOH 24  424 24  HOH HOH A . 
G 6 HOH 25  425 25  HOH HOH A . 
G 6 HOH 26  426 26  HOH HOH A . 
G 6 HOH 27  427 27  HOH HOH A . 
G 6 HOH 28  428 28  HOH HOH A . 
G 6 HOH 29  429 29  HOH HOH A . 
G 6 HOH 30  430 30  HOH HOH A . 
G 6 HOH 31  431 31  HOH HOH A . 
G 6 HOH 32  432 32  HOH HOH A . 
G 6 HOH 33  433 33  HOH HOH A . 
G 6 HOH 34  434 34  HOH HOH A . 
G 6 HOH 35  435 35  HOH HOH A . 
G 6 HOH 36  436 36  HOH HOH A . 
G 6 HOH 37  437 37  HOH HOH A . 
G 6 HOH 38  438 38  HOH HOH A . 
G 6 HOH 39  439 39  HOH HOH A . 
G 6 HOH 40  440 40  HOH HOH A . 
G 6 HOH 41  441 41  HOH HOH A . 
G 6 HOH 42  442 42  HOH HOH A . 
G 6 HOH 43  443 43  HOH HOH A . 
G 6 HOH 44  444 44  HOH HOH A . 
G 6 HOH 45  445 45  HOH HOH A . 
G 6 HOH 46  446 46  HOH HOH A . 
G 6 HOH 47  447 47  HOH HOH A . 
G 6 HOH 48  448 48  HOH HOH A . 
G 6 HOH 49  449 49  HOH HOH A . 
G 6 HOH 50  450 50  HOH HOH A . 
G 6 HOH 51  451 51  HOH HOH A . 
G 6 HOH 52  452 52  HOH HOH A . 
G 6 HOH 53  453 53  HOH HOH A . 
G 6 HOH 54  454 54  HOH HOH A . 
G 6 HOH 55  455 55  HOH HOH A . 
G 6 HOH 56  456 56  HOH HOH A . 
G 6 HOH 57  457 57  HOH HOH A . 
G 6 HOH 58  458 58  HOH HOH A . 
G 6 HOH 59  459 59  HOH HOH A . 
G 6 HOH 60  460 60  HOH HOH A . 
G 6 HOH 61  461 61  HOH HOH A . 
G 6 HOH 62  462 62  HOH HOH A . 
G 6 HOH 63  463 63  HOH HOH A . 
G 6 HOH 64  464 64  HOH HOH A . 
G 6 HOH 65  465 65  HOH HOH A . 
G 6 HOH 66  466 66  HOH HOH A . 
G 6 HOH 67  467 67  HOH HOH A . 
G 6 HOH 68  468 68  HOH HOH A . 
G 6 HOH 69  469 69  HOH HOH A . 
G 6 HOH 70  470 70  HOH HOH A . 
G 6 HOH 71  471 71  HOH HOH A . 
G 6 HOH 72  472 72  HOH HOH A . 
G 6 HOH 73  473 73  HOH HOH A . 
G 6 HOH 74  474 74  HOH HOH A . 
G 6 HOH 75  475 75  HOH HOH A . 
G 6 HOH 76  476 76  HOH HOH A . 
G 6 HOH 77  477 77  HOH HOH A . 
G 6 HOH 78  478 78  HOH HOH A . 
G 6 HOH 79  479 79  HOH HOH A . 
G 6 HOH 80  480 80  HOH HOH A . 
G 6 HOH 81  481 81  HOH HOH A . 
G 6 HOH 82  482 82  HOH HOH A . 
G 6 HOH 83  483 83  HOH HOH A . 
G 6 HOH 84  484 84  HOH HOH A . 
G 6 HOH 85  485 85  HOH HOH A . 
G 6 HOH 86  486 86  HOH HOH A . 
G 6 HOH 87  487 87  HOH HOH A . 
G 6 HOH 88  488 88  HOH HOH A . 
G 6 HOH 89  489 89  HOH HOH A . 
G 6 HOH 90  490 90  HOH HOH A . 
G 6 HOH 91  491 91  HOH HOH A . 
G 6 HOH 92  492 92  HOH HOH A . 
G 6 HOH 93  493 93  HOH HOH A . 
G 6 HOH 94  494 94  HOH HOH A . 
G 6 HOH 95  495 95  HOH HOH A . 
G 6 HOH 96  496 96  HOH HOH A . 
G 6 HOH 97  497 97  HOH HOH A . 
G 6 HOH 98  498 98  HOH HOH A . 
G 6 HOH 99  499 99  HOH HOH A . 
G 6 HOH 100 500 100 HOH HOH A . 
G 6 HOH 101 501 101 HOH HOH A . 
G 6 HOH 102 502 102 HOH HOH A . 
G 6 HOH 103 503 103 HOH HOH A . 
G 6 HOH 104 504 104 HOH HOH A . 
G 6 HOH 105 505 105 HOH HOH A . 
G 6 HOH 106 506 106 HOH HOH A . 
G 6 HOH 107 507 107 HOH HOH A . 
G 6 HOH 108 508 108 HOH HOH A . 
G 6 HOH 109 509 109 HOH HOH A . 
G 6 HOH 110 510 110 HOH HOH A . 
G 6 HOH 111 511 111 HOH HOH A . 
G 6 HOH 112 512 112 HOH HOH A . 
G 6 HOH 113 513 113 HOH HOH A . 
G 6 HOH 114 514 114 HOH HOH A . 
G 6 HOH 115 515 115 HOH HOH A . 
G 6 HOH 116 516 116 HOH HOH A . 
G 6 HOH 117 517 117 HOH HOH A . 
G 6 HOH 118 518 118 HOH HOH A . 
G 6 HOH 119 519 119 HOH HOH A . 
G 6 HOH 120 520 120 HOH HOH A . 
G 6 HOH 121 521 121 HOH HOH A . 
G 6 HOH 122 522 122 HOH HOH A . 
G 6 HOH 123 523 123 HOH HOH A . 
G 6 HOH 124 524 124 HOH HOH A . 
G 6 HOH 125 525 125 HOH HOH A . 
G 6 HOH 126 526 126 HOH HOH A . 
G 6 HOH 127 527 127 HOH HOH A . 
G 6 HOH 128 528 128 HOH HOH A . 
G 6 HOH 129 529 129 HOH HOH A . 
G 6 HOH 130 530 130 HOH HOH A . 
G 6 HOH 131 531 131 HOH HOH A . 
G 6 HOH 132 532 132 HOH HOH A . 
G 6 HOH 133 533 133 HOH HOH A . 
G 6 HOH 134 534 134 HOH HOH A . 
G 6 HOH 135 535 135 HOH HOH A . 
G 6 HOH 136 536 136 HOH HOH A . 
G 6 HOH 137 537 137 HOH HOH A . 
G 6 HOH 138 538 138 HOH HOH A . 
G 6 HOH 139 539 139 HOH HOH A . 
G 6 HOH 140 540 140 HOH HOH A . 
G 6 HOH 141 541 141 HOH HOH A . 
G 6 HOH 142 542 142 HOH HOH A . 
G 6 HOH 143 543 143 HOH HOH A . 
G 6 HOH 144 544 144 HOH HOH A . 
G 6 HOH 145 545 145 HOH HOH A . 
G 6 HOH 146 546 146 HOH HOH A . 
G 6 HOH 147 547 147 HOH HOH A . 
G 6 HOH 148 548 148 HOH HOH A . 
G 6 HOH 149 549 149 HOH HOH A . 
G 6 HOH 150 550 150 HOH HOH A . 
G 6 HOH 151 551 151 HOH HOH A . 
G 6 HOH 152 552 152 HOH HOH A . 
G 6 HOH 153 553 153 HOH HOH A . 
G 6 HOH 154 554 154 HOH HOH A . 
G 6 HOH 155 555 155 HOH HOH A . 
G 6 HOH 156 556 156 HOH HOH A . 
G 6 HOH 157 557 157 HOH HOH A . 
G 6 HOH 158 558 158 HOH HOH A . 
G 6 HOH 159 559 159 HOH HOH A . 
G 6 HOH 160 560 160 HOH HOH A . 
G 6 HOH 161 561 161 HOH HOH A . 
G 6 HOH 162 562 162 HOH HOH A . 
G 6 HOH 163 563 163 HOH HOH A . 
G 6 HOH 164 564 164 HOH HOH A . 
G 6 HOH 165 565 165 HOH HOH A . 
G 6 HOH 166 566 166 HOH HOH A . 
G 6 HOH 167 567 167 HOH HOH A . 
G 6 HOH 168 568 168 HOH HOH A . 
G 6 HOH 169 569 169 HOH HOH A . 
G 6 HOH 170 570 170 HOH HOH A . 
G 6 HOH 171 571 171 HOH HOH A . 
G 6 HOH 172 572 172 HOH HOH A . 
G 6 HOH 173 573 173 HOH HOH A . 
G 6 HOH 174 574 174 HOH HOH A . 
G 6 HOH 175 575 175 HOH HOH A . 
G 6 HOH 176 576 176 HOH HOH A . 
G 6 HOH 177 577 177 HOH HOH A . 
G 6 HOH 178 578 178 HOH HOH A . 
G 6 HOH 179 579 179 HOH HOH A . 
G 6 HOH 180 580 180 HOH HOH A . 
G 6 HOH 181 581 181 HOH HOH A . 
G 6 HOH 182 582 182 HOH HOH A . 
G 6 HOH 183 583 183 HOH HOH A . 
G 6 HOH 184 584 184 HOH HOH A . 
G 6 HOH 185 585 185 HOH HOH A . 
G 6 HOH 186 586 186 HOH HOH A . 
G 6 HOH 187 587 187 HOH HOH A . 
G 6 HOH 188 588 188 HOH HOH A . 
G 6 HOH 189 589 189 HOH HOH A . 
G 6 HOH 190 590 190 HOH HOH A . 
G 6 HOH 191 591 191 HOH HOH A . 
G 6 HOH 192 592 192 HOH HOH A . 
G 6 HOH 193 593 193 HOH HOH A . 
G 6 HOH 194 594 194 HOH HOH A . 
G 6 HOH 195 595 195 HOH HOH A . 
G 6 HOH 196 596 196 HOH HOH A . 
G 6 HOH 197 597 197 HOH HOH A . 
G 6 HOH 198 598 198 HOH HOH A . 
G 6 HOH 199 599 199 HOH HOH A . 
G 6 HOH 200 600 200 HOH HOH A . 
G 6 HOH 201 601 201 HOH HOH A . 
G 6 HOH 202 602 202 HOH HOH A . 
G 6 HOH 203 603 203 HOH HOH A . 
G 6 HOH 204 604 204 HOH HOH A . 
G 6 HOH 205 605 205 HOH HOH A . 
G 6 HOH 206 606 206 HOH HOH A . 
G 6 HOH 207 607 207 HOH HOH A . 
G 6 HOH 208 608 208 HOH HOH A . 
G 6 HOH 209 609 209 HOH HOH A . 
G 6 HOH 210 610 210 HOH HOH A . 
G 6 HOH 211 611 211 HOH HOH A . 
G 6 HOH 212 612 212 HOH HOH A . 
G 6 HOH 213 613 213 HOH HOH A . 
G 6 HOH 214 614 214 HOH HOH A . 
G 6 HOH 215 615 215 HOH HOH A . 
# 
_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 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_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_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 101.2 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 112.0 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.1  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C EWY .   ? A EWY 302 ? 1_555 113.5 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C EWY .   ? A EWY 302 ? 1_555 110.8 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C EWY .   ? A EWY 302 ? 1_555 118.0 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C EWY .   ? A EWY 302 ? 1_555 114.2 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C EWY .   ? A EWY 302 ? 1_555 113.1 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C EWY .   ? A EWY 302 ? 1_555 115.4 ? 
10 N10 B C EWY .   ? A EWY 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C EWY .   ? A EWY 302 ? 1_555 2.9   ? 
# 
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 2015-01-21 
2 'Structure model' 1 1 2023-11-08 
# 
_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' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 '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' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' diffrn_source                 
5 2 'Structure model' pdbx_initial_refinement_model 
6 2 'Structure model' pdbx_struct_conn_angle        
7 2 'Structure model' struct_conn                   
8 2 'Structure model' struct_site                   
# 
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' '_database_2.pdbx_DOI'                        
2  2 'Structure model' '_database_2.pdbx_database_accession'         
3  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_alt_id'  
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_alt_id'  
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
15 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
16 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
17 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
18 2 'Structure model' '_pdbx_struct_conn_angle.value'               
19 2 'Structure model' '_struct_conn.pdbx_dist_value'                
20 2 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
21 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
22 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
23 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
24 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
25 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
26 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
27 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
28 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
29 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
30 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
31 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
32 2 'Structure model' '_struct_site.pdbx_auth_asym_id'              
33 2 'Structure model' '_struct_site.pdbx_auth_comp_id'              
34 2 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.2.19 22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345dtb   .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
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  ? ? -143.44 18.78   
2 1 ASN A 244 ? ? -95.31  49.79   
3 1 LYS A 252 ? ? 58.38   -132.91 
# 
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 N 1 A MES 303 ? S   ? D MES 1 S   
2 1 N 1 A MES 303 ? O1S ? D MES 1 O1S 
3 1 N 1 A MES 303 ? O2S ? D MES 1 O2S 
4 1 N 1 A MES 303 ? O3S ? D MES 1 O3S 
# 
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  
EWY O20  O  N N 98  
EWY C18  C  N N 99  
EWY C22  C  N N 100 
EWY C17  C  N N 101 
EWY C21  C  N N 102 
EWY N16  N  N N 103 
EWY N19  N  N N 104 
EWY C15  C  N N 105 
EWY S14  S  N N 106 
EWY C13  C  N N 107 
EWY C11  C  N N 108 
EWY O12  O  N N 109 
EWY C2   C  Y N 110 
EWY C3   C  Y N 111 
EWY C4   C  Y N 112 
EWY S7   S  N N 113 
EWY O9   O  N N 114 
EWY N10  N  N N 115 
EWY O8   O  N N 116 
EWY C5   C  Y N 117 
EWY C6   C  Y N 118 
EWY C1   C  Y N 119 
EWY H1   H  N N 120 
EWY H3   H  N N 121 
EWY H4   H  N N 122 
EWY H5   H  N N 123 
EWY H6   H  N N 124 
EWY H7   H  N N 125 
EWY H8   H  N N 126 
EWY H9   H  N N 127 
EWY H10  H  N N 128 
EWY H11  H  N N 129 
EWY H12  H  N N 130 
EWY H13  H  N N 131 
EWY H2   H  N N 132 
GLN N    N  N N 133 
GLN CA   C  N S 134 
GLN C    C  N N 135 
GLN O    O  N N 136 
GLN CB   C  N N 137 
GLN CG   C  N N 138 
GLN CD   C  N N 139 
GLN OE1  O  N N 140 
GLN NE2  N  N N 141 
GLN OXT  O  N N 142 
GLN H    H  N N 143 
GLN H2   H  N N 144 
GLN HA   H  N N 145 
GLN HB2  H  N N 146 
GLN HB3  H  N N 147 
GLN HG2  H  N N 148 
GLN HG3  H  N N 149 
GLN HE21 H  N N 150 
GLN HE22 H  N N 151 
GLN HXT  H  N N 152 
GLU N    N  N N 153 
GLU CA   C  N S 154 
GLU C    C  N N 155 
GLU O    O  N N 156 
GLU CB   C  N N 157 
GLU CG   C  N N 158 
GLU CD   C  N N 159 
GLU OE1  O  N N 160 
GLU OE2  O  N N 161 
GLU OXT  O  N N 162 
GLU H    H  N N 163 
GLU H2   H  N N 164 
GLU HA   H  N N 165 
GLU HB2  H  N N 166 
GLU HB3  H  N N 167 
GLU HG2  H  N N 168 
GLU HG3  H  N N 169 
GLU HE2  H  N N 170 
GLU HXT  H  N N 171 
GLY N    N  N N 172 
GLY CA   C  N N 173 
GLY C    C  N N 174 
GLY O    O  N N 175 
GLY OXT  O  N N 176 
GLY H    H  N N 177 
GLY H2   H  N N 178 
GLY HA2  H  N N 179 
GLY HA3  H  N N 180 
GLY HXT  H  N N 181 
HIS N    N  N N 182 
HIS CA   C  N S 183 
HIS C    C  N N 184 
HIS O    O  N N 185 
HIS CB   C  N N 186 
HIS CG   C  Y N 187 
HIS ND1  N  Y N 188 
HIS CD2  C  Y N 189 
HIS CE1  C  Y N 190 
HIS NE2  N  Y N 191 
HIS OXT  O  N N 192 
HIS H    H  N N 193 
HIS H2   H  N N 194 
HIS HA   H  N N 195 
HIS HB2  H  N N 196 
HIS HB3  H  N N 197 
HIS HD1  H  N N 198 
HIS HD2  H  N N 199 
HIS HE1  H  N N 200 
HIS HE2  H  N N 201 
HIS HXT  H  N N 202 
HOH O    O  N N 203 
HOH H1   H  N N 204 
HOH H2   H  N N 205 
ILE N    N  N N 206 
ILE CA   C  N S 207 
ILE C    C  N N 208 
ILE O    O  N N 209 
ILE CB   C  N S 210 
ILE CG1  C  N N 211 
ILE CG2  C  N N 212 
ILE CD1  C  N N 213 
ILE OXT  O  N N 214 
ILE H    H  N N 215 
ILE H2   H  N N 216 
ILE HA   H  N N 217 
ILE HB   H  N N 218 
ILE HG12 H  N N 219 
ILE HG13 H  N N 220 
ILE HG21 H  N N 221 
ILE HG22 H  N N 222 
ILE HG23 H  N N 223 
ILE HD11 H  N N 224 
ILE HD12 H  N N 225 
ILE HD13 H  N N 226 
ILE HXT  H  N N 227 
LEU N    N  N N 228 
LEU CA   C  N S 229 
LEU C    C  N N 230 
LEU O    O  N N 231 
LEU CB   C  N N 232 
LEU CG   C  N N 233 
LEU CD1  C  N N 234 
LEU CD2  C  N N 235 
LEU OXT  O  N N 236 
LEU H    H  N N 237 
LEU H2   H  N N 238 
LEU HA   H  N N 239 
LEU HB2  H  N N 240 
LEU HB3  H  N N 241 
LEU HG   H  N N 242 
LEU HD11 H  N N 243 
LEU HD12 H  N N 244 
LEU HD13 H  N N 245 
LEU HD21 H  N N 246 
LEU HD22 H  N N 247 
LEU HD23 H  N N 248 
LEU HXT  H  N N 249 
LYS N    N  N N 250 
LYS CA   C  N S 251 
LYS C    C  N N 252 
LYS O    O  N N 253 
LYS CB   C  N N 254 
LYS CG   C  N N 255 
LYS CD   C  N N 256 
LYS CE   C  N N 257 
LYS NZ   N  N N 258 
LYS OXT  O  N N 259 
LYS H    H  N N 260 
LYS H2   H  N N 261 
LYS HA   H  N N 262 
LYS HB2  H  N N 263 
LYS HB3  H  N N 264 
LYS HG2  H  N N 265 
LYS HG3  H  N N 266 
LYS HD2  H  N N 267 
LYS HD3  H  N N 268 
LYS HE2  H  N N 269 
LYS HE3  H  N N 270 
LYS HZ1  H  N N 271 
LYS HZ2  H  N N 272 
LYS HZ3  H  N N 273 
LYS HXT  H  N N 274 
MES O1   O  N N 275 
MES C2   C  N N 276 
MES C3   C  N N 277 
MES N4   N  N N 278 
MES C5   C  N N 279 
MES C6   C  N N 280 
MES C7   C  N N 281 
MES C8   C  N N 282 
MES S    S  N N 283 
MES O1S  O  N N 284 
MES O2S  O  N N 285 
MES O3S  O  N N 286 
MES H21  H  N N 287 
MES H22  H  N N 288 
MES H31  H  N N 289 
MES H32  H  N N 290 
MES HN4  H  N N 291 
MES H51  H  N N 292 
MES H52  H  N N 293 
MES H61  H  N N 294 
MES H62  H  N N 295 
MES H71  H  N N 296 
MES H72  H  N N 297 
MES H81  H  N N 298 
MES H82  H  N N 299 
MET N    N  N N 300 
MET CA   C  N S 301 
MET C    C  N N 302 
MET O    O  N N 303 
MET CB   C  N N 304 
MET CG   C  N N 305 
MET SD   S  N N 306 
MET CE   C  N N 307 
MET OXT  O  N N 308 
MET H    H  N N 309 
MET H2   H  N N 310 
MET HA   H  N N 311 
MET HB2  H  N N 312 
MET HB3  H  N N 313 
MET HG2  H  N N 314 
MET HG3  H  N N 315 
MET HE1  H  N N 316 
MET HE2  H  N N 317 
MET HE3  H  N N 318 
MET HXT  H  N N 319 
PHE N    N  N N 320 
PHE CA   C  N S 321 
PHE C    C  N N 322 
PHE O    O  N N 323 
PHE CB   C  N N 324 
PHE CG   C  Y N 325 
PHE CD1  C  Y N 326 
PHE CD2  C  Y N 327 
PHE CE1  C  Y N 328 
PHE CE2  C  Y N 329 
PHE CZ   C  Y N 330 
PHE OXT  O  N N 331 
PHE H    H  N N 332 
PHE H2   H  N N 333 
PHE HA   H  N N 334 
PHE HB2  H  N N 335 
PHE HB3  H  N N 336 
PHE HD1  H  N N 337 
PHE HD2  H  N N 338 
PHE HE1  H  N N 339 
PHE HE2  H  N N 340 
PHE HZ   H  N N 341 
PHE HXT  H  N N 342 
PRO N    N  N N 343 
PRO CA   C  N S 344 
PRO C    C  N N 345 
PRO O    O  N N 346 
PRO CB   C  N N 347 
PRO CG   C  N N 348 
PRO CD   C  N N 349 
PRO OXT  O  N N 350 
PRO H    H  N N 351 
PRO HA   H  N N 352 
PRO HB2  H  N N 353 
PRO HB3  H  N N 354 
PRO HG2  H  N N 355 
PRO HG3  H  N N 356 
PRO HD2  H  N N 357 
PRO HD3  H  N N 358 
PRO HXT  H  N N 359 
SER N    N  N N 360 
SER CA   C  N S 361 
SER C    C  N N 362 
SER O    O  N N 363 
SER CB   C  N N 364 
SER OG   O  N N 365 
SER OXT  O  N N 366 
SER H    H  N N 367 
SER H2   H  N N 368 
SER HA   H  N N 369 
SER HB2  H  N N 370 
SER HB3  H  N N 371 
SER HG   H  N N 372 
SER HXT  H  N N 373 
THR N    N  N N 374 
THR CA   C  N S 375 
THR C    C  N N 376 
THR O    O  N N 377 
THR CB   C  N R 378 
THR OG1  O  N N 379 
THR CG2  C  N N 380 
THR OXT  O  N N 381 
THR H    H  N N 382 
THR H2   H  N N 383 
THR HA   H  N N 384 
THR HB   H  N N 385 
THR HG1  H  N N 386 
THR HG21 H  N N 387 
THR HG22 H  N N 388 
THR HG23 H  N N 389 
THR HXT  H  N N 390 
TRP N    N  N N 391 
TRP CA   C  N S 392 
TRP C    C  N N 393 
TRP O    O  N N 394 
TRP CB   C  N N 395 
TRP CG   C  Y N 396 
TRP CD1  C  Y N 397 
TRP CD2  C  Y N 398 
TRP NE1  N  Y N 399 
TRP CE2  C  Y N 400 
TRP CE3  C  Y N 401 
TRP CZ2  C  Y N 402 
TRP CZ3  C  Y N 403 
TRP CH2  C  Y N 404 
TRP OXT  O  N N 405 
TRP H    H  N N 406 
TRP H2   H  N N 407 
TRP HA   H  N N 408 
TRP HB2  H  N N 409 
TRP HB3  H  N N 410 
TRP HD1  H  N N 411 
TRP HE1  H  N N 412 
TRP HE3  H  N N 413 
TRP HZ2  H  N N 414 
TRP HZ3  H  N N 415 
TRP HH2  H  N N 416 
TRP HXT  H  N N 417 
TYR N    N  N N 418 
TYR CA   C  N S 419 
TYR C    C  N N 420 
TYR O    O  N N 421 
TYR CB   C  N N 422 
TYR CG   C  Y N 423 
TYR CD1  C  Y N 424 
TYR CD2  C  Y N 425 
TYR CE1  C  Y N 426 
TYR CE2  C  Y N 427 
TYR CZ   C  Y N 428 
TYR OH   O  N N 429 
TYR OXT  O  N N 430 
TYR H    H  N N 431 
TYR H2   H  N N 432 
TYR HA   H  N N 433 
TYR HB2  H  N N 434 
TYR HB3  H  N N 435 
TYR HD1  H  N N 436 
TYR HD2  H  N N 437 
TYR HE1  H  N N 438 
TYR HE2  H  N N 439 
TYR HH   H  N N 440 
TYR HXT  H  N N 441 
VAL N    N  N N 442 
VAL CA   C  N S 443 
VAL C    C  N N 444 
VAL O    O  N N 445 
VAL CB   C  N N 446 
VAL CG1  C  N N 447 
VAL CG2  C  N N 448 
VAL OXT  O  N N 449 
VAL H    H  N N 450 
VAL H2   H  N N 451 
VAL HA   H  N N 452 
VAL HB   H  N N 453 
VAL HG11 H  N N 454 
VAL HG12 H  N N 455 
VAL HG13 H  N N 456 
VAL HG21 H  N N 457 
VAL HG22 H  N N 458 
VAL HG23 H  N N 459 
VAL HXT  H  N N 460 
ZN  ZN   ZN N N 461 
# 
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  
EWY O20 C18  doub N N 92  
EWY C18 C22  sing N N 93  
EWY C18 N19  sing N N 94  
EWY C22 C17  doub N N 95  
EWY N19 C15  sing N N 96  
EWY C17 C21  sing N N 97  
EWY C17 N16  sing N N 98  
EWY C15 N16  doub N N 99  
EWY C15 S14  sing N N 100 
EWY S14 C13  sing N N 101 
EWY C13 C11  sing N N 102 
EWY O12 C11  doub N N 103 
EWY C11 C2   sing N N 104 
EWY C2  C1   doub Y N 105 
EWY C2  C3   sing Y N 106 
EWY C1  C6   sing Y N 107 
EWY C6  C5   doub Y N 108 
EWY C3  C4   doub Y N 109 
EWY C4  C5   sing Y N 110 
EWY C4  S7   sing N N 111 
EWY N10 S7   sing N N 112 
EWY O9  S7   doub N N 113 
EWY S7  O8   doub N N 114 
EWY C22 H1   sing N N 115 
EWY C21 H3   sing N N 116 
EWY C21 H4   sing N N 117 
EWY C21 H5   sing N N 118 
EWY C13 H6   sing N N 119 
EWY C13 H7   sing N N 120 
EWY C3  H8   sing N N 121 
EWY N10 H9   sing N N 122 
EWY N10 H10  sing N N 123 
EWY C5  H11  sing N N 124 
EWY C6  H12  sing N N 125 
EWY C1  H13  sing N N 126 
EWY N19 H2   sing N N 127 
GLN N   CA   sing N N 128 
GLN N   H    sing N N 129 
GLN N   H2   sing N N 130 
GLN CA  C    sing N N 131 
GLN CA  CB   sing N N 132 
GLN CA  HA   sing N N 133 
GLN C   O    doub N N 134 
GLN C   OXT  sing N N 135 
GLN CB  CG   sing N N 136 
GLN CB  HB2  sing N N 137 
GLN CB  HB3  sing N N 138 
GLN CG  CD   sing N N 139 
GLN CG  HG2  sing N N 140 
GLN CG  HG3  sing N N 141 
GLN CD  OE1  doub N N 142 
GLN CD  NE2  sing N N 143 
GLN NE2 HE21 sing N N 144 
GLN NE2 HE22 sing N N 145 
GLN OXT HXT  sing N N 146 
GLU N   CA   sing N N 147 
GLU N   H    sing N N 148 
GLU N   H2   sing N N 149 
GLU CA  C    sing N N 150 
GLU CA  CB   sing N N 151 
GLU CA  HA   sing N N 152 
GLU C   O    doub N N 153 
GLU C   OXT  sing N N 154 
GLU CB  CG   sing N N 155 
GLU CB  HB2  sing N N 156 
GLU CB  HB3  sing N N 157 
GLU CG  CD   sing N N 158 
GLU CG  HG2  sing N N 159 
GLU CG  HG3  sing N N 160 
GLU CD  OE1  doub N N 161 
GLU CD  OE2  sing N N 162 
GLU OE2 HE2  sing N N 163 
GLU OXT HXT  sing N N 164 
GLY N   CA   sing N N 165 
GLY N   H    sing N N 166 
GLY N   H2   sing N N 167 
GLY CA  C    sing N N 168 
GLY CA  HA2  sing N N 169 
GLY CA  HA3  sing N N 170 
GLY C   O    doub N N 171 
GLY C   OXT  sing N N 172 
GLY OXT HXT  sing N N 173 
HIS N   CA   sing N N 174 
HIS N   H    sing N N 175 
HIS N   H2   sing N N 176 
HIS CA  C    sing N N 177 
HIS CA  CB   sing N N 178 
HIS CA  HA   sing N N 179 
HIS C   O    doub N N 180 
HIS C   OXT  sing N N 181 
HIS CB  CG   sing N N 182 
HIS CB  HB2  sing N N 183 
HIS CB  HB3  sing N N 184 
HIS CG  ND1  sing Y N 185 
HIS CG  CD2  doub Y N 186 
HIS ND1 CE1  doub Y N 187 
HIS ND1 HD1  sing N N 188 
HIS CD2 NE2  sing Y N 189 
HIS CD2 HD2  sing N N 190 
HIS CE1 NE2  sing Y N 191 
HIS CE1 HE1  sing N N 192 
HIS NE2 HE2  sing N N 193 
HIS OXT HXT  sing N N 194 
HOH O   H1   sing N N 195 
HOH O   H2   sing N N 196 
ILE N   CA   sing N N 197 
ILE N   H    sing N N 198 
ILE N   H2   sing N N 199 
ILE CA  C    sing N N 200 
ILE CA  CB   sing N N 201 
ILE CA  HA   sing N N 202 
ILE C   O    doub N N 203 
ILE C   OXT  sing N N 204 
ILE CB  CG1  sing N N 205 
ILE CB  CG2  sing N N 206 
ILE CB  HB   sing N N 207 
ILE CG1 CD1  sing N N 208 
ILE CG1 HG12 sing N N 209 
ILE CG1 HG13 sing N N 210 
ILE CG2 HG21 sing N N 211 
ILE CG2 HG22 sing N N 212 
ILE CG2 HG23 sing N N 213 
ILE CD1 HD11 sing N N 214 
ILE CD1 HD12 sing N N 215 
ILE CD1 HD13 sing N N 216 
ILE OXT HXT  sing N N 217 
LEU N   CA   sing N N 218 
LEU N   H    sing N N 219 
LEU N   H2   sing N N 220 
LEU CA  C    sing N N 221 
LEU CA  CB   sing N N 222 
LEU CA  HA   sing N N 223 
LEU C   O    doub N N 224 
LEU C   OXT  sing N N 225 
LEU CB  CG   sing N N 226 
LEU CB  HB2  sing N N 227 
LEU CB  HB3  sing N N 228 
LEU CG  CD1  sing N N 229 
LEU CG  CD2  sing N N 230 
LEU CG  HG   sing N N 231 
LEU CD1 HD11 sing N N 232 
LEU CD1 HD12 sing N N 233 
LEU CD1 HD13 sing N N 234 
LEU CD2 HD21 sing N N 235 
LEU CD2 HD22 sing N N 236 
LEU CD2 HD23 sing N N 237 
LEU OXT HXT  sing N N 238 
LYS N   CA   sing N N 239 
LYS N   H    sing N N 240 
LYS N   H2   sing N N 241 
LYS CA  C    sing N N 242 
LYS CA  CB   sing N N 243 
LYS CA  HA   sing N N 244 
LYS C   O    doub N N 245 
LYS C   OXT  sing N N 246 
LYS CB  CG   sing N N 247 
LYS CB  HB2  sing N N 248 
LYS CB  HB3  sing N N 249 
LYS CG  CD   sing N N 250 
LYS CG  HG2  sing N N 251 
LYS CG  HG3  sing N N 252 
LYS CD  CE   sing N N 253 
LYS CD  HD2  sing N N 254 
LYS CD  HD3  sing N N 255 
LYS CE  NZ   sing N N 256 
LYS CE  HE2  sing N N 257 
LYS CE  HE3  sing N N 258 
LYS NZ  HZ1  sing N N 259 
LYS NZ  HZ2  sing N N 260 
LYS NZ  HZ3  sing N N 261 
LYS OXT HXT  sing N N 262 
MES O1  C2   sing N N 263 
MES O1  C6   sing N N 264 
MES C2  C3   sing N N 265 
MES C2  H21  sing N N 266 
MES C2  H22  sing N N 267 
MES C3  N4   sing N N 268 
MES C3  H31  sing N N 269 
MES C3  H32  sing N N 270 
MES N4  C5   sing N N 271 
MES N4  C7   sing N N 272 
MES N4  HN4  sing N N 273 
MES C5  C6   sing N N 274 
MES C5  H51  sing N N 275 
MES C5  H52  sing N N 276 
MES C6  H61  sing N N 277 
MES C6  H62  sing N N 278 
MES C7  C8   sing N N 279 
MES C7  H71  sing N N 280 
MES C7  H72  sing N N 281 
MES C8  S    sing N N 282 
MES C8  H81  sing N N 283 
MES C8  H82  sing N N 284 
MES S   O1S  doub N N 285 
MES S   O2S  doub N N 286 
MES S   O3S  sing N N 287 
MET N   CA   sing N N 288 
MET N   H    sing N N 289 
MET N   H2   sing N N 290 
MET CA  C    sing N N 291 
MET CA  CB   sing N N 292 
MET CA  HA   sing N N 293 
MET C   O    doub N N 294 
MET C   OXT  sing N N 295 
MET CB  CG   sing N N 296 
MET CB  HB2  sing N N 297 
MET CB  HB3  sing N N 298 
MET CG  SD   sing N N 299 
MET CG  HG2  sing N N 300 
MET CG  HG3  sing N N 301 
MET SD  CE   sing N N 302 
MET CE  HE1  sing N N 303 
MET CE  HE2  sing N N 304 
MET CE  HE3  sing N N 305 
MET OXT HXT  sing N N 306 
PHE N   CA   sing N N 307 
PHE N   H    sing N N 308 
PHE N   H2   sing N N 309 
PHE CA  C    sing N N 310 
PHE CA  CB   sing N N 311 
PHE CA  HA   sing N N 312 
PHE C   O    doub N N 313 
PHE C   OXT  sing N N 314 
PHE CB  CG   sing N N 315 
PHE CB  HB2  sing N N 316 
PHE CB  HB3  sing N N 317 
PHE CG  CD1  doub Y N 318 
PHE CG  CD2  sing Y N 319 
PHE CD1 CE1  sing Y N 320 
PHE CD1 HD1  sing N N 321 
PHE CD2 CE2  doub Y N 322 
PHE CD2 HD2  sing N N 323 
PHE CE1 CZ   doub Y N 324 
PHE CE1 HE1  sing N N 325 
PHE CE2 CZ   sing Y N 326 
PHE CE2 HE2  sing N N 327 
PHE CZ  HZ   sing N N 328 
PHE OXT HXT  sing N N 329 
PRO N   CA   sing N N 330 
PRO N   CD   sing N N 331 
PRO N   H    sing N N 332 
PRO CA  C    sing N N 333 
PRO CA  CB   sing N N 334 
PRO CA  HA   sing N N 335 
PRO C   O    doub N N 336 
PRO C   OXT  sing N N 337 
PRO CB  CG   sing N N 338 
PRO CB  HB2  sing N N 339 
PRO CB  HB3  sing N N 340 
PRO CG  CD   sing N N 341 
PRO CG  HG2  sing N N 342 
PRO CG  HG3  sing N N 343 
PRO CD  HD2  sing N N 344 
PRO CD  HD3  sing N N 345 
PRO OXT HXT  sing N N 346 
SER N   CA   sing N N 347 
SER N   H    sing N N 348 
SER N   H2   sing N N 349 
SER CA  C    sing N N 350 
SER CA  CB   sing N N 351 
SER CA  HA   sing N N 352 
SER C   O    doub N N 353 
SER C   OXT  sing N N 354 
SER CB  OG   sing N N 355 
SER CB  HB2  sing N N 356 
SER CB  HB3  sing N N 357 
SER OG  HG   sing N N 358 
SER OXT HXT  sing N N 359 
THR N   CA   sing N N 360 
THR N   H    sing N N 361 
THR N   H2   sing N N 362 
THR CA  C    sing N N 363 
THR CA  CB   sing N N 364 
THR CA  HA   sing N N 365 
THR C   O    doub N N 366 
THR C   OXT  sing N N 367 
THR CB  OG1  sing N N 368 
THR CB  CG2  sing N N 369 
THR CB  HB   sing N N 370 
THR OG1 HG1  sing N N 371 
THR CG2 HG21 sing N N 372 
THR CG2 HG22 sing N N 373 
THR CG2 HG23 sing N N 374 
THR OXT HXT  sing N N 375 
TRP N   CA   sing N N 376 
TRP N   H    sing N N 377 
TRP N   H2   sing N N 378 
TRP CA  C    sing N N 379 
TRP CA  CB   sing N N 380 
TRP CA  HA   sing N N 381 
TRP C   O    doub N N 382 
TRP C   OXT  sing N N 383 
TRP CB  CG   sing N N 384 
TRP CB  HB2  sing N N 385 
TRP CB  HB3  sing N N 386 
TRP CG  CD1  doub Y N 387 
TRP CG  CD2  sing Y N 388 
TRP CD1 NE1  sing Y N 389 
TRP CD1 HD1  sing N N 390 
TRP CD2 CE2  doub Y N 391 
TRP CD2 CE3  sing Y N 392 
TRP NE1 CE2  sing Y N 393 
TRP NE1 HE1  sing N N 394 
TRP CE2 CZ2  sing Y N 395 
TRP CE3 CZ3  doub Y N 396 
TRP CE3 HE3  sing N N 397 
TRP CZ2 CH2  doub Y N 398 
TRP CZ2 HZ2  sing N N 399 
TRP CZ3 CH2  sing Y N 400 
TRP CZ3 HZ3  sing N N 401 
TRP CH2 HH2  sing N N 402 
TRP OXT HXT  sing N N 403 
TYR N   CA   sing N N 404 
TYR N   H    sing N N 405 
TYR N   H2   sing N N 406 
TYR CA  C    sing N N 407 
TYR CA  CB   sing N N 408 
TYR CA  HA   sing N N 409 
TYR C   O    doub N N 410 
TYR C   OXT  sing N N 411 
TYR CB  CG   sing N N 412 
TYR CB  HB2  sing N N 413 
TYR CB  HB3  sing N N 414 
TYR CG  CD1  doub Y N 415 
TYR CG  CD2  sing Y N 416 
TYR CD1 CE1  sing Y N 417 
TYR CD1 HD1  sing N N 418 
TYR CD2 CE2  doub Y N 419 
TYR CD2 HD2  sing N N 420 
TYR CE1 CZ   doub Y N 421 
TYR CE1 HE1  sing N N 422 
TYR CE2 CZ   sing Y N 423 
TYR CE2 HE2  sing N N 424 
TYR CZ  OH   sing N N 425 
TYR OH  HH   sing N N 426 
TYR OXT HXT  sing N N 427 
VAL N   CA   sing N N 428 
VAL N   H    sing N N 429 
VAL N   H2   sing N N 430 
VAL CA  C    sing N N 431 
VAL CA  CB   sing N N 432 
VAL CA  HA   sing N N 433 
VAL C   O    doub N N 434 
VAL C   OXT  sing N N 435 
VAL CB  CG1  sing N N 436 
VAL CB  CG2  sing N N 437 
VAL CB  HB   sing N N 438 
VAL CG1 HG11 sing N N 439 
VAL CG1 HG12 sing N N 440 
VAL CG1 HG13 sing N N 441 
VAL CG2 HG21 sing N N 442 
VAL CG2 HG22 sing N N 443 
VAL CG2 HG23 sing N N 444 
VAL OXT HXT  sing N N 445 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                         ZN  
3 '3-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' EWY 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                             MES 
5 'DIMETHYL SULFOXIDE'                                                               DMS 
6 water                                                                              HOH 
# 
_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   3HLJ 
_pdbx_initial_refinement_model.details          ? 
# 
