data_4QSI
# 
_entry.id   4QSI 
# 
_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   4QSI         pdb_00004qsi 10.2210/pdb4qsi/pdb 
RCSB  RCSB086457   ?            ?                   
WWPDB D_1000086457 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4QSA . unspecified 
PDB 4QSB . unspecified 
PDB 4QSJ . unspecified 
# 
_pdbx_database_status.entry_id                        4QSI 
_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   2014-07-04 
_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 
'Manakova, E.' 1 
'Smirnov, A.'  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           4QSI 
_cell.length_a           42.062 
_cell.length_b           40.918 
_cell.length_c           71.594 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.010 
_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                         4QSI 
_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 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                                          195.237   1   ? 
? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                            78.133    1   ? 
? ? ? 
5 non-polymer syn 'SODIUM ION'                                                                                    22.990    1   ? 
? ? ? 
6 non-polymer syn '5-{[(4-tert-butyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}-2-chlorobenzenesulfonamide' 415.915   1   ? 
? ? ? 
7 water       nat water                                                                                           18.015    176 ? 
? ? ? 
# 
_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              4QSI 
_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  
EWZ non-polymer         . '5-{[(4-tert-butyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}-2-chlorobenzenesulfonamide' ? 
'C16 H18 Cl N3 O4 S2' 415.915 
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 
NA  non-polymer         . 'SODIUM ION'                                                                                    ? 'Na 1' 
22.990  
PHE 'L-peptide linking' y PHENYLALANINE                                                                                   ? 
'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                                                         ? 
'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                                                          ? 
'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                                                                       ? 
'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                      ? 
'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                        ? 
'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                                                                          ? 
'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                                                                      ? 'Zn 2' 
65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4QSI 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   39.73 
_exptl_crystal.density_Matthews      2.04 
_exptl_crystal.pdbx_mosaicity        1.13 
_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 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
'0.1M sodium BICINE, pH 9, 3.1M sodium malonate pH 7, 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               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS IV++' 
_diffrn_detector.pdbx_collection_date   2010-05-17 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'VARIMAX-HF MIRROR' 
_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   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
# 
_reflns.entry_id                     4QSI 
_reflns.d_resolution_high            1.800 
_reflns.d_resolution_low             24.361 
_reflns.number_all                   ? 
_reflns.number_obs                   16250 
_reflns.pdbx_Rmerge_I_obs            0.048 
_reflns.pdbx_netI_over_sigmaI        28.100 
_reflns.pdbx_Rsym_value              0.048 
_reflns.pdbx_redundancy              6.800 
_reflns.percent_possible_obs         93.600 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        21.123 
_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 
1.95 2.06  ? 14345 ? ? 0.263 2.8  0.263 ? 6.50 ? 6.30  ? 2223 ? ? 0.302 ? 89.10 0.30 0.12 1  1 
2.06 2.18  ? 13893 ? ? 0.162 4.6  0.162 ? 6.30 ? 10.40 ? 2195 ? ? 0.190 ? 91.50 0.19 0.08 2  1 
2.18 2.33  ? 13566 ? ? 0.104 7.0  0.104 ? 6.60 ? 16.40 ? 2060 ? ? 0.121 ? 92.50 0.12 0.05 3  1 
2.33 2.52  ? 13719 ? ? 0.075 9.6  0.075 ? 7.00 ? 20.60 ? 1963 ? ? 0.087 ? 94.10 0.09 0.03 4  1 
2.52 2.76  ? 12996 ? ? 0.059 12.0 0.059 ? 7.10 ? 26.80 ? 1832 ? ? 0.068 ? 94.40 0.07 0.03 5  1 
2.76 3.08  ? 11819 ? ? 0.045 14.8 0.045 ? 7.10 ? 35.20 ? 1666 ? ? 0.052 ? 95.70 0.05 0.02 6  1 
3.08 3.56  ? 10492 ? ? 0.035 18.0 0.035 ? 7.10 ? 46.30 ? 1476 ? ? 0.040 ? 95.50 0.04 0.01 7  1 
3.56 4.36  ? 8975  ? ? 0.030 19.8 0.030 ? 7.00 ? 58.50 ? 1274 ? ? 0.034 ? 96.90 0.03 0.01 8  1 
4.36 6.17  ? 6945  ? ? 0.027 20.7 0.027 ? 7.00 ? 60.60 ? 998  ? ? 0.030 ? 97.00 0.03 0.01 9  1 
6.17 24.36 ? 3752  ? ? 0.025 24.8 0.025 ? 6.70 ? 61.20 ? 563  ? ? 0.029 ? 96.40 0.03 0.01 10 1 
# 
_refine.entry_id                                 4QSI 
_refine.ls_d_res_high                            1.950 
_refine.ls_d_res_low                             24.360 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    92.990 
_refine.ls_number_reflns_obs                     16242 
_refine.ls_number_reflns_all                     16242 
_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                          0.162 
_refine.ls_R_factor_obs                          0.162 
_refine.ls_R_factor_R_work                       0.157 
_refine.ls_wR_factor_R_work                      0.150 
_refine.ls_R_factor_R_free                       0.209 
_refine.ls_wR_factor_R_free                      0.199 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  1640 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.583 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.210 
_refine.aniso_B[2][2]                            -0.870 
_refine.aniso_B[3][3]                            0.590 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.130 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.939 
_refine.overall_SU_R_Cruickshank_DPI             0.211 
_refine.overall_SU_R_free                        0.171 
_refine.pdbx_overall_ESU_R                       0.211 
_refine.pdbx_overall_ESU_R_Free                  0.171 
_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                   0.872 
_refine.B_iso_max                                81.86 
_refine.B_iso_min                                7.82 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_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         44 
_refine_hist.number_atoms_solvent             176 
_refine_hist.number_atoms_total               2269 
_refine_hist.d_res_high                       1.950 
_refine_hist.d_res_low                        24.360 
# 
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       2175 0.018  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    2959 1.892  1.985  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 255  7.102  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 98   34.457 24.694 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 349  15.784 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 7    21.632 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         306  0.134  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1667 0.011  0.021  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.950 
_refine_ls_shell.d_res_low                        2.000 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               87.340 
_refine_ls_shell.number_reflns_R_work             972 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.289 
_refine_ls_shell.R_factor_R_free                  0.348 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             111 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1083 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  4QSI 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 5-{[(4-tert-buthyl-6-oxo-1,6-dihydropyrimidin-2-yl)thio]acetyl}-2-chlorobenzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4QSI 
_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 6 ? 
G N N 7 ? 
# 
_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  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? ASP A 161 ? LEU A 157 ASP A 162 1 ? 6 
HELX_P HELX_P7 7 VAL A 162 ? LYS A 167 ? VAL A 163 LYS A 168 5 ? 6 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 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 ? ? ? ? ? ? ? 1.980 ? ? 
metalc2  metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc3  metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc4  metalc ? ? A SER 219 OG  ? ? ? 1_555 E NA  . NA  ? ? A SER 220 A NA  304 1_555 ? ? ? ? ? ? ? 2.564 ? ? 
metalc5  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F EWZ . N26 A ? A ZN  301 A EWZ 305 1_555 ? ? ? ? ? ? ? 2.163 ? ? 
metalc6  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F EWZ . N26 B ? A ZN  301 A EWZ 305 1_555 ? ? ? ? ? ? ? 2.410 ? ? 
metalc7  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F EWZ . S22 A ? A ZN  301 A EWZ 305 1_555 ? ? ? ? ? ? ? 2.997 ? ? 
metalc8  metalc ? ? E NA  .   NA  ? ? ? 1_555 G HOH . O   ? ? A NA  304 A HOH 469 1_555 ? ? ? ? ? ? ? 2.526 ? ? 
metalc9  metalc ? ? E NA  .   NA  ? ? ? 1_555 G HOH . O   ? ? A NA  304 A HOH 485 1_555 ? ? ? ? ? ? ? 2.289 ? ? 
metalc10 metalc ? ? E NA  .   NA  ? ? ? 1_555 G HOH . O   ? ? A NA  304 A HOH 539 1_555 ? ? ? ? ? ? ? 2.519 ? ? 
# 
_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 -1.97 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 9.84  
# 
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 LEU A 211 ? O LEU A 212 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 PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O ASN A 67  ? O ASN A 67  N LEU A 60  ? N LEU A 60  
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 MES 302 ? 5  'BINDING SITE FOR RESIDUE MES A 302' 
AC3 Software A DMS 303 ? 3  'BINDING SITE FOR RESIDUE DMS A 303' 
AC4 Software A NA  304 ? 5  'BINDING SITE FOR RESIDUE NA A 304'  
AC5 Software A EWZ 305 ? 17 'BINDING SITE FOR RESIDUE EWZ 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  EWZ F .   ? EWZ A 305 . ? 1_555 ? 
5  AC2 5  VAL A 160 ? VAL A 161 . ? 1_555 ? 
6  AC2 5  ASP A 161 ? ASP A 162 . ? 1_555 ? 
7  AC2 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
8  AC2 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
9  AC2 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
10 AC3 3  TYR A 7   ? TYR A 7   . ? 1_555 ? 
11 AC3 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
12 AC3 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
13 AC4 5  SER A 73  ? SER A 73  . ? 1_545 ? 
14 AC4 5  SER A 219 ? SER A 220 . ? 1_555 ? 
15 AC4 5  HOH G .   ? HOH A 469 . ? 1_555 ? 
16 AC4 5  HOH G .   ? HOH A 485 . ? 1_555 ? 
17 AC4 5  HOH G .   ? HOH A 539 . ? 1_555 ? 
18 AC5 17 TRP A 5   ? TRP A 5   . ? 1_555 ? 
19 AC5 17 ASN A 62  ? ASN A 62  . ? 1_555 ? 
20 AC5 17 ASN A 67  ? ASN A 67  . ? 1_555 ? 
21 AC5 17 GLN A 92  ? GLN A 92  . ? 1_555 ? 
22 AC5 17 HIS A 94  ? HIS A 94  . ? 1_555 ? 
23 AC5 17 HIS A 96  ? HIS A 96  . ? 1_555 ? 
24 AC5 17 HIS A 119 ? HIS A 119 . ? 1_555 ? 
25 AC5 17 VAL A 121 ? VAL A 121 . ? 1_555 ? 
26 AC5 17 PHE A 130 ? PHE A 131 . ? 1_555 ? 
27 AC5 17 LEU A 140 ? LEU A 141 . ? 1_555 ? 
28 AC5 17 VAL A 142 ? VAL A 143 . ? 1_555 ? 
29 AC5 17 LEU A 197 ? LEU A 198 . ? 1_555 ? 
30 AC5 17 THR A 198 ? THR A 199 . ? 1_555 ? 
31 AC5 17 THR A 199 ? THR A 200 . ? 1_555 ? 
32 AC5 17 PRO A 201 ? PRO A 202 . ? 1_555 ? 
33 AC5 17 TRP A 208 ? TRP A 209 . ? 1_555 ? 
34 AC5 17 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4QSI 
_atom_sites.fract_transf_matrix[1][1]   0.023775 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005931 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024439 
_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]   0.014396 
_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  
CL 
N  
NA 
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 9.279   1.292   8.196   1.00   27.97 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.061  0.074   8.663   1.00   32.88 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.378   -0.942  9.562   1.00   27.51 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.600   -2.165  9.414   1.00   29.17 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 11.305  0.489   9.418   1.00   40.35 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 12.360  -0.589  9.494   1.00   44.99 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 13.058  -0.995  8.418   1.00   51.01 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 12.821  -1.344  10.570  1.00   47.57 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 13.922  -1.961  8.783   1.00   55.32 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 13.776  -2.174  10.101  1.00   52.89 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.556   -0.495  10.490  1.00   23.24 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.875   -1.461  11.383  1.00   20.69 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.923   -2.272  10.599  1.00   19.23 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.421   -1.822  9.574   1.00   17.52 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.164   -0.751  12.550  1.00   19.87 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 5.941   0.078   12.151  1.00   19.45 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.885   1.442   11.831  1.00   19.78 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.551   -0.401  12.028  1.00   18.17 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.574   1.819   11.580  1.00   19.70 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.739   0.761   11.655  1.00   18.17 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 3.921   -1.629  12.225  1.00   18.71 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.360   0.672   11.465  1.00   19.93 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.522   -1.697  12.048  1.00   19.49 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.771   -0.575  11.677  1.00   18.14 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.648   -3.485  11.049  1.00   19.59 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.662   -4.299  10.332  1.00   19.36 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.264   -5.448  11.229  1.00   19.86 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.270   -5.295  12.458  1.00   16.70 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 4.903   -6.596  10.630  1.00   20.39 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.488   -7.761  11.419  1.00   19.59 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.369   -9.020  11.149  1.00   24.08 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.022   -10.120 11.600  1.00   26.51 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 2.977   -8.076  11.252  1.00   16.54 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.065   -6.980  11.798  1.00   15.93 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.654   -6.994  13.123  1.00   14.44 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.662   -5.925  10.975  1.00   15.44 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 0.851   -5.986  13.626  1.00   15.52 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.836   -4.925  11.430  1.00   16.43 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.434   -4.974  12.771  1.00   15.98 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.357  -3.992  13.241  1.00   15.60 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.500   -8.850  10.470  1.00   23.83 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.462   -9.988  10.256  1.00   23.97 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.436   -10.377 11.368  1.00   25.11 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.480   -9.764  12.460  1.00   24.09 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.287   -11.382 11.083  1.00   29.30 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.308  -11.828 12.059  1.00   29.96 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.271  -10.706 12.418  1.00   29.98 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.748  -10.605 13.584  1.00   30.71 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.094  -13.050 11.526  1.00   37.89 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.042  -13.690 12.537  1.00   41.66 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 11.322  -14.219 13.802  1.00   52.13 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 11.498  -13.300 15.023  1.00   52.61 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 10.856  -13.828 16.255  1.00   56.06 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 11.511  -9.820  11.445  1.00   27.14 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 12.569  -8.809  11.655  1.00   27.05 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 12.108  -7.438  12.038  1.00   24.16 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 12.888  -6.640  12.530  1.00   25.52 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 13.560  -8.832  10.471  1.00   25.69 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 14.287  -10.161 10.378  1.00   26.03 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 15.201  -10.555 11.312  1.00   29.15 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 14.143  -11.221 9.500   1.00   29.20 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 15.631  -11.779 11.031  1.00   26.85 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 14.976  -12.205 9.923   1.00   30.05 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 10.820  -7.181  11.845  1.00   25.02 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 10.229  -5.867  12.082  1.00   23.27 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 8.868   -5.887  12.849  1.00   21.31 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 8.216   -4.849  12.956  1.00   18.57 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 10.096  -5.134  10.751  1.00   23.18 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 9.019   -5.720  9.858   1.00   24.73 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 8.535   -6.830  10.082  1.00   26.49 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 8.647   -4.981  8.824   1.00   21.03 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 8.520   -7.066  13.399  1.00   20.81 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 7.295   -7.370  14.162  1.00   18.87 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 7.136   -6.709  15.539  1.00   18.81 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 8.016   -5.929  15.967  1.00   18.69 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 6.022   -7.021  16.253  1.00   18.30 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 5.777   -6.380  17.540  1.00   18.76 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 6.942   -6.375  18.521  1.00   18.44 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 7.140   -5.380  19.223  1.00   15.94 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 4.573   -7.173  18.107  1.00   18.47 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 3.818   -7.578  16.871  1.00   18.93 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 4.850   -7.805  15.807  1.00   17.30 ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 7.710   -7.472  18.585  1.00   19.14 ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 8.845   -7.562  19.487  1.00   20.30 ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 9.950   -6.514  19.196  1.00   18.36 ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 10.775  -6.225  20.063  1.00   18.69 ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 9.413   -8.989  19.410  1.00   23.12 ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 10.069  -9.282  18.049  1.00   27.06 ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 9.200   -9.953  16.931  1.00   35.38 ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 7.952   -9.706  16.827  1.00   30.55 ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 9.817   -10.700 16.093  1.00   35.29 ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 9.995   -5.980  17.979  1.00   16.98 ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 10.985  -4.970  17.602  1.00   16.35 ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 10.533  -3.522  17.768  1.00   16.81 ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 11.363  -2.612  17.732  1.00   17.65 ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 11.406  -5.172  16.150  1.00   19.59 ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 12.117  -6.484  15.902  1.00   21.61 ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 13.459  -6.628  16.061  1.00   22.63 ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 11.630  -7.729  15.516  1.00   21.76 ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 13.817  -7.911  15.768  1.00   23.43 ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 12.702  -8.596  15.470  1.00   24.12 ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 9.235   -3.275  17.912  1.00   15.12 ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 8.723   -1.917  17.861  1.00   13.84 ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 9.300   -1.042  18.910  1.00   13.75 ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 9.376   0.176   18.688  1.00   14.46 ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 7.200   -1.861  18.004  1.00   12.70 ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 6.497   -2.568  16.858  1.00   13.98 ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 7.034   -2.952  15.615  1.00   13.14 ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 5.073   -2.922  16.791  1.00   13.15 ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 6.073   -3.575  14.836  1.00   14.28 ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 4.854   -3.526  15.460  1.00   13.63 ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 4.007   -2.766  17.637  1.00   12.35 ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 3.601   -4.021  15.071  1.00   13.91 ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 2.756   -3.258  17.235  1.00   12.91 ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 2.560   -3.850  15.976  1.00   13.55 ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 9.726   -1.597  20.045  1.00   14.25 ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 10.215  -0.706  21.104  1.00   16.06 ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 11.439  0.119   20.742  1.00   17.83 ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 11.691  1.142   21.395  1.00   16.67 ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 10.483  -1.444  22.389  1.00   17.33 ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 11.691  -2.336  22.291  1.00   18.59 ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 12.927  -1.947  22.717  1.00   22.11 ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 11.844  -3.562  21.723  1.00   17.83 ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 13.794  -2.913  22.487  1.00   19.01 ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 13.143  -3.905  21.855  1.00   19.09 ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 18  ? 12.216  -0.326  19.745  1.00   16.77 ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 18  ? 13.468  0.341   19.382  1.00   18.58 ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 18  ? 13.142  1.679   18.692  1.00   20.51 ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 18  ? 13.774  2.678   18.939  1.00   21.53 ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 18  ? 14.290  -0.581  18.463  1.00   19.21 ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 18  ? 14.867  -1.851  19.157  1.00   18.23 ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 18  ? 15.593  -2.738  18.185  1.00   17.76 ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 18  ? 14.656  -3.755  17.584  1.00   17.10 ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 18  ? 15.318  -4.526  16.497  1.00   14.68 ? 18  LYS A NZ  1 
ATOM   135  N  N   . ASP A 1 19  ? 12.110  1.726   17.870  1.00   20.47 ? 19  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 19  ? 11.689  3.026   17.332  1.00   22.61 ? 19  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 19  ? 10.730  3.786   18.231  1.00   22.98 ? 19  ASP A C   1 
ATOM   138  O  O   . ASP A 1 19  ? 10.640  5.001   18.155  1.00   21.10 ? 19  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 19  ? 11.090  2.854   15.948  1.00   24.64 ? 19  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 19  ? 12.126  2.786   14.867  1.00   30.54 ? 19  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 19  ? 13.158  3.446   14.982  1.00   31.78 ? 19  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 19  ? 11.899  2.082   13.873  1.00   38.76 ? 19  ASP A OD2 1 
ATOM   143  N  N   . PHE A 1 20  ? 9.939   3.066   19.039  1.00   20.42 ? 20  PHE A N   1 
ATOM   144  C  CA  . PHE A 1 20  ? 8.810   3.702   19.787  1.00   19.79 ? 20  PHE A CA  1 
ATOM   145  C  C   . PHE A 1 20  ? 8.889   3.157   21.179  1.00   18.44 ? 20  PHE A C   1 
ATOM   146  O  O   . PHE A 1 20  ? 8.288   2.115   21.476  1.00   18.46 ? 20  PHE A O   1 
ATOM   147  C  CB  . PHE A 1 20  ? 7.441   3.412   19.135  1.00   18.28 ? 20  PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 20  ? 7.427   3.686   17.655  1.00   19.49 ? 20  PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 20  ? 7.112   4.972   17.165  1.00   19.42 ? 20  PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 20  ? 7.769   2.685   16.750  1.00   19.51 ? 20  PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 20  ? 7.117   5.230   15.808  1.00   18.31 ? 20  PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 20  ? 7.810   2.934   15.379  1.00   17.77 ? 20  PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 20  ? 7.467   4.210   14.918  1.00   20.68 ? 20  PHE A CZ  1 
ATOM   154  N  N   . PRO A 1 21  ? 9.707   3.815   22.025  1.00   17.86 ? 21  PRO A N   1 
ATOM   155  C  CA  . PRO A 1 21  ? 10.024  3.322   23.345  1.00   17.73 ? 21  PRO A CA  1 
ATOM   156  C  C   . PRO A 1 21  ? 8.816   3.172   24.246  1.00   16.14 ? 21  PRO A C   1 
ATOM   157  O  O   . PRO A 1 21  ? 8.834   2.421   25.222  1.00   15.23 ? 21  PRO A O   1 
ATOM   158  C  CB  . PRO A 1 21  ? 11.024  4.405   23.873  1.00   19.27 ? 21  PRO A CB  1 
ATOM   159  C  CG  . PRO A 1 21  ? 11.790  4.750   22.627  1.00   19.71 ? 21  PRO A CG  1 
ATOM   160  C  CD  . PRO A 1 21  ? 10.609  4.944   21.675  1.00   19.86 ? 21  PRO A CD  1 
ATOM   161  N  N   . ILE A 1 22  ? 7.756   3.895   23.909  1.00   14.79 ? 22  ILE A N   1 
ATOM   162  C  CA  . ILE A 1 22  ? 6.543   3.773   24.647  1.00   15.16 ? 22  ILE A CA  1 
ATOM   163  C  C   . ILE A 1 22  ? 5.932   2.370   24.484  1.00   14.97 ? 22  ILE A C   1 
ATOM   164  O  O   . ILE A 1 22  ? 5.072   1.992   25.277  1.00   16.29 ? 22  ILE A O   1 
ATOM   165  C  CB  . ILE A 1 22  ? 5.519   4.890   24.205  1.00   12.80 ? 22  ILE A CB  1 
ATOM   166  C  CG1 . ILE A 1 22  ? 4.385   4.953   25.185  1.00   13.58 ? 22  ILE A CG1 1 
ATOM   167  C  CG2 . ILE A 1 22  ? 4.905   4.504   22.864  1.00   14.26 ? 22  ILE A CG2 1 
ATOM   168  C  CD1 . ILE A 1 22  ? 4.666   5.723   26.453  1.00   16.37 ? 22  ILE A CD1 1 
ATOM   169  N  N   . ALA A 1 23  ? 6.382   1.578   23.504  1.00   17.01 ? 23  ALA A N   1 
ATOM   170  C  CA  . ALA A 1 23  ? 5.989   0.139   23.448  1.00   17.45 ? 23  ALA A CA  1 
ATOM   171  C  C   . ALA A 1 23  ? 6.075   -0.553  24.804  1.00   18.50 ? 23  ALA A C   1 
ATOM   172  O  O   . ALA A 1 23  ? 5.315   -1.505  25.071  1.00   17.81 ? 23  ALA A O   1 
ATOM   173  C  CB  . ALA A 1 23  ? 6.815   -0.670  22.417  1.00   15.05 ? 23  ALA A CB  1 
ATOM   174  N  N   . LYS A 1 24  ? 7.008   -0.111  25.653  1.00   20.13 ? 24  LYS A N   1 
ATOM   175  C  CA  . LYS A 1 24  ? 7.155   -0.731  26.979  1.00   19.80 ? 24  LYS A CA  1 
ATOM   176  C  C   . LYS A 1 24  ? 6.509   0.089   28.076  1.00   20.54 ? 24  LYS A C   1 
ATOM   177  O  O   . LYS A 1 24  ? 6.900   -0.048  29.244  1.00   20.51 ? 24  LYS A O   1 
ATOM   178  C  CB  . LYS A 1 24  ? 8.643   -0.961  27.286  1.00   23.19 ? 24  LYS A CB  1 
ATOM   179  C  CG  . LYS A 1 24  ? 9.271   -2.034  26.407  1.00   26.67 ? 24  LYS A CG  1 
ATOM   180  C  CD  . LYS A 1 24  ? 10.769  -2.117  26.690  1.00   31.60 ? 24  LYS A CD  1 
ATOM   181  C  CE  . LYS A 1 24  ? 11.461  -3.087  25.719  1.00   32.26 ? 24  LYS A CE  1 
ATOM   182  N  NZ  . LYS A 1 24  ? 11.319  -4.497  26.197  1.00   32.14 ? 24  LYS A NZ  1 
ATOM   183  N  N   . GLY A 1 25  ? 5.502   0.918   27.743  1.00   17.88 ? 25  GLY A N   1 
ATOM   184  C  CA  . GLY A 1 25  ? 4.971   1.851   28.720  1.00   16.98 ? 25  GLY A CA  1 
ATOM   185  C  C   . GLY A 1 25  ? 3.928   1.282   29.652  1.00   16.69 ? 25  GLY A C   1 
ATOM   186  O  O   . GLY A 1 25  ? 3.727   0.045   29.721  1.00   16.17 ? 25  GLY A O   1 
ATOM   187  N  N   . GLU A 1 26  ? 3.311   2.189   30.420  1.00   17.45 ? 26  GLU A N   1 
ATOM   188  C  CA  . GLU A 1 26  ? 2.402   1.826   31.495  1.00   19.57 ? 26  GLU A CA  1 
ATOM   189  C  C   . GLU A 1 26  ? 0.973   1.516   31.069  1.00   18.06 ? 26  GLU A C   1 
ATOM   190  O  O   . GLU A 1 26  ? 0.197   1.018   31.889  1.00   15.87 ? 26  GLU A O   1 
ATOM   191  C  CB  . GLU A 1 26  ? 2.351   2.934   32.616  1.00   25.37 ? 26  GLU A CB  1 
ATOM   192  C  CG  . GLU A 1 26  ? 3.680   3.325   33.290  1.00   35.18 ? 26  GLU A CG  1 
ATOM   193  C  CD  . GLU A 1 26  ? 4.576   2.129   33.668  1.00   41.16 ? 26  GLU A CD  1 
ATOM   194  O  OE1 . GLU A 1 26  ? 4.168   1.284   34.523  1.00   45.23 ? 26  GLU A OE1 1 
ATOM   195  O  OE2 . GLU A 1 26  ? 5.702   2.039   33.106  1.00   40.42 ? 26  GLU A OE2 1 
ATOM   196  N  N   . ARG A 1 27  ? 0.589   1.839   29.831  1.00   16.34 ? 27  ARG A N   1 
ATOM   197  C  CA  . ARG A 1 27  ? -0.800  1.628   29.425  1.00   14.53 ? 27  ARG A CA  1 
ATOM   198  C  C   . ARG A 1 27  ? -0.897  1.209   27.940  1.00   14.69 ? 27  ARG A C   1 
ATOM   199  O  O   . ARG A 1 27  ? -1.623  1.800   27.123  1.00   13.04 ? 27  ARG A O   1 
ATOM   200  C  CB  . ARG A 1 27  ? -1.646  2.890   29.774  1.00   15.28 ? 27  ARG A CB  1 
ATOM   201  C  CG  . ARG A 1 27  ? -1.481  4.138   28.917  1.00   17.22 ? 27  ARG A CG  1 
ATOM   202  C  CD  . ARG A 1 27  ? -2.389  5.328   29.341  1.00   20.76 ? 27  ARG A CD  1 
ATOM   203  N  NE  . ARG A 1 27  ? -3.648  5.276   28.585  1.00   18.53 ? 27  ARG A NE  1 
ATOM   204  C  CZ  . ARG A 1 27  ? -4.461  6.303   28.345  1.00   17.95 ? 27  ARG A CZ  1 
ATOM   205  N  NH1 . ARG A 1 27  ? -4.180  7.516   28.803  1.00   16.89 ? 27  ARG A NH1 1 
ATOM   206  N  NH2 . ARG A 1 27  ? -5.572  6.108   27.642  1.00   19.06 ? 27  ARG A NH2 1 
ATOM   207  N  N   . GLN A 1 28  ? -0.133  0.157   27.614  1.00   12.40 ? 28  GLN A N   1 
ATOM   208  C  CA  . GLN A 1 28  ? -0.104  -0.388  26.268  1.00   11.09 ? 28  GLN A CA  1 
ATOM   209  C  C   . GLN A 1 28  ? -1.287  -1.361  26.036  1.00   10.54 ? 28  GLN A C   1 
ATOM   210  O  O   . GLN A 1 28  ? -1.848  -2.006  26.947  1.00   9.99  ? 28  GLN A O   1 
ATOM   211  C  CB  . GLN A 1 28  ? 1.247   -1.067  26.070  1.00   11.61 ? 28  GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 28  ? 2.386   -0.046  25.973  1.00   10.35 ? 28  GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 28  ? 2.246   0.742   24.660  1.00   10.65 ? 28  GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 28  ? 2.467   0.188   23.625  1.00   10.13 ? 28  GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 28  ? 1.812   2.009   24.723  1.00   10.75 ? 28  GLN A NE2 1 
ATOM   216  N  N   . SER A 1 29  ? -1.626  -1.464  24.764  1.00   10.17 ? 29  SER A N   1 
ATOM   217  C  CA  . SER A 1 29  ? -2.711  -2.308  24.312  1.00   9.51  ? 29  SER A CA  1 
ATOM   218  C  C   . SER A 1 29  ? -2.131  -3.195  23.179  1.00   8.70  ? 29  SER A C   1 
ATOM   219  O  O   . SER A 1 29  ? -1.152  -2.822  22.529  1.00   9.20  ? 29  SER A O   1 
ATOM   220  C  CB  . SER A 1 29  ? -3.872  -1.474  23.793  1.00   9.05  ? 29  SER A CB  1 
ATOM   221  O  OG  . SER A 1 29  ? -4.493  -0.768  24.873  1.00   10.14 ? 29  SER A OG  1 
ATOM   222  N  N   . PRO A 1 30  ? -2.781  -4.349  22.912  1.00   8.91  ? 30  PRO A N   1 
ATOM   223  C  CA  . PRO A 1 30  ? -3.957  -4.856  23.621  1.00   9.21  ? 30  PRO A CA  1 
ATOM   224  C  C   . PRO A 1 30  ? -3.546  -5.590  24.909  1.00   10.02 ? 30  PRO A C   1 
ATOM   225  O  O   . PRO A 1 30  ? -2.339  -5.660  25.224  1.00   9.78  ? 30  PRO A O   1 
ATOM   226  C  CB  . PRO A 1 30  ? -4.545  -5.850  22.602  1.00   9.46  ? 30  PRO A CB  1 
ATOM   227  C  CG  . PRO A 1 30  ? -3.314  -6.455  22.001  1.00   9.57  ? 30  PRO A CG  1 
ATOM   228  C  CD  . PRO A 1 30  ? -2.457  -5.190  21.734  1.00   9.29  ? 30  PRO A CD  1 
ATOM   229  N  N   . VAL A 1 31  ? -4.521  -6.202  25.575  1.00   9.65  ? 31  VAL A N   1 
ATOM   230  C  CA  . VAL A 1 31  ? -4.365  -6.912  26.829  1.00   10.46 ? 31  VAL A CA  1 
ATOM   231  C  C   . VAL A 1 31  ? -5.256  -8.149  26.786  1.00   11.55 ? 31  VAL A C   1 
ATOM   232  O  O   . VAL A 1 31  ? -6.253  -8.184  26.031  1.00   11.06 ? 31  VAL A O   1 
ATOM   233  C  CB  . VAL A 1 31  ? -4.744  -6.044  28.084  1.00   10.42 ? 31  VAL A CB  1 
ATOM   234  C  CG1 . VAL A 1 31  ? -3.851  -4.772  28.154  1.00   10.13 ? 31  VAL A CG1 1 
ATOM   235  C  CG2 . VAL A 1 31  ? -6.214  -5.638  28.067  1.00   10.17 ? 31  VAL A CG2 1 
ATOM   236  N  N   . ASP A 1 32  ? -4.915  -9.143  27.608  1.00   11.73 ? 32  ASP A N   1 
ATOM   237  C  CA  . ASP A 1 32  ? -5.832  -10.201 27.894  1.00   12.14 ? 32  ASP A CA  1 
ATOM   238  C  C   . ASP A 1 32  ? -6.952  -9.698  28.809  1.00   12.30 ? 32  ASP A C   1 
ATOM   239  O  O   . ASP A 1 32  ? -6.671  -9.090  29.824  1.00   11.65 ? 32  ASP A O   1 
ATOM   240  C  CB  . ASP A 1 32  ? -5.111  -11.381 28.576  1.00   12.72 ? 32  ASP A CB  1 
ATOM   241  C  CG  . ASP A 1 32  ? -6.064  -12.533 28.805  1.00   15.30 ? 32  ASP A CG  1 
ATOM   242  O  OD1 . ASP A 1 32  ? -6.693  -12.957 27.791  1.00   13.54 ? 32  ASP A OD1 1 
ATOM   243  O  OD2 . ASP A 1 32  ? -6.217  -12.990 29.964  1.00   12.96 ? 32  ASP A OD2 1 
ATOM   244  N  N   . ILE A 1 33  ? -8.220  -9.961  28.474  1.00   12.08 ? 33  ILE A N   1 
ATOM   245  C  CA  . ILE A 1 33  ? -9.321  -9.608  29.344  1.00   13.74 ? 33  ILE A CA  1 
ATOM   246  C  C   . ILE A 1 33  ? -9.659  -10.865 30.152  1.00   14.92 ? 33  ILE A C   1 
ATOM   247  O  O   . ILE A 1 33  ? -10.207 -11.844 29.619  1.00   14.21 ? 33  ILE A O   1 
ATOM   248  C  CB  . ILE A 1 33  ? -10.554 -9.180  28.551  1.00   14.20 ? 33  ILE A CB  1 
ATOM   249  C  CG1 . ILE A 1 33  ? -10.277 -7.851  27.845  1.00   13.75 ? 33  ILE A CG1 1 
ATOM   250  C  CG2 . ILE A 1 33  ? -11.772 -9.046  29.456  1.00   15.58 ? 33  ILE A CG2 1 
ATOM   251  C  CD1 . ILE A 1 33  ? -11.241 -7.668  26.663  1.00   13.79 ? 33  ILE A CD1 1 
ATOM   252  N  N   . ASP A 1 34  ? -9.243  -10.834 31.412  1.00   16.07 ? 34  ASP A N   1 
ATOM   253  C  CA  . ASP A 1 34  ? -9.570  -11.886 32.395  1.00   18.16 ? 34  ASP A CA  1 
ATOM   254  C  C   . ASP A 1 34  ? -11.009 -11.617 32.913  1.00   18.11 ? 34  ASP A C   1 
ATOM   255  O  O   . ASP A 1 34  ? -11.233 -10.728 33.784  1.00   19.15 ? 34  ASP A O   1 
ATOM   256  C  CB  . ASP A 1 34  ? -8.521  -11.819 33.515  1.00   20.01 ? 34  ASP A CB  1 
ATOM   257  C  CG  . ASP A 1 34  ? -8.789  -12.859 34.679  1.00   25.02 ? 34  ASP A CG  1 
ATOM   258  O  OD1 . ASP A 1 34  ? -9.890  -13.423 34.819  1.00   23.49 ? 34  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A 1 34  ? -7.849  -13.101 35.447  1.00   29.68 ? 34  ASP A OD2 1 
ATOM   260  N  N   . THR A 1 35  ? -11.979 -12.369 32.396  1.00   16.54 ? 35  THR A N   1 
ATOM   261  C  CA  . THR A 1 35  ? -13.361 -12.050 32.608  1.00   18.85 ? 35  THR A CA  1 
ATOM   262  C  C   . THR A 1 35  ? -13.723 -12.213 34.089  1.00   21.41 ? 35  THR A C   1 
ATOM   263  O  O   . THR A 1 35  ? -14.727 -11.634 34.556  1.00   20.36 ? 35  THR A O   1 
ATOM   264  C  CB  . THR A 1 35  ? -14.335 -12.956 31.835  1.00   19.71 ? 35  THR A CB  1 
ATOM   265  O  OG1 . THR A 1 35  ? -14.129 -14.303 32.247  1.00   19.36 ? 35  THR A OG1 1 
ATOM   266  C  CG2 . THR A 1 35  ? -14.107 -12.842 30.342  1.00   17.60 ? 35  THR A CG2 1 
ATOM   267  N  N   . HIS A 1 36  ? -12.916 -13.004 34.808  1.00   21.17 ? 36  HIS A N   1 
ATOM   268  C  CA  . HIS A 1 36  ? -13.183 -13.210 36.229  1.00   22.93 ? 36  HIS A CA  1 
ATOM   269  C  C   . HIS A 1 36  ? -12.725 -12.113 37.125  1.00   22.49 ? 36  HIS A C   1 
ATOM   270  O  O   . HIS A 1 36  ? -13.418 -11.791 38.076  1.00   27.61 ? 36  HIS A O   1 
ATOM   271  C  CB  . HIS A 1 36  ? -12.741 -14.618 36.669  1.00   21.35 ? 36  HIS A CB  1 
ATOM   272  C  CG  . HIS A 1 36  ? -13.574 -15.713 36.018  1.00   20.33 ? 36  HIS A CG  1 
ATOM   273  N  ND1 . HIS A 1 36  ? -13.083 -16.538 35.069  1.00   21.47 ? 36  HIS A ND1 1 
ATOM   274  C  CD2 . HIS A 1 36  ? -14.923 -15.995 36.117  1.00   21.77 ? 36  HIS A CD2 1 
ATOM   275  C  CE1 . HIS A 1 36  ? -14.053 -17.356 34.629  1.00   22.77 ? 36  HIS A CE1 1 
ATOM   276  N  NE2 . HIS A 1 36  ? -15.184 -17.022 35.246  1.00   24.74 ? 36  HIS A NE2 1 
ATOM   277  N  N   . THR A 1 37  ? -11.606 -11.480 36.821  1.00   23.65 ? 37  THR A N   1 
ATOM   278  C  CA  . THR A 1 37  ? -11.149 -10.360 37.648  1.00   22.72 ? 37  THR A CA  1 
ATOM   279  C  C   . THR A 1 37  ? -11.480 -8.944  37.071  1.00   23.47 ? 37  THR A C   1 
ATOM   280  O  O   . THR A 1 37  ? -11.138 -7.930  37.663  1.00   20.79 ? 37  THR A O   1 
ATOM   281  C  CB  . THR A 1 37  ? -9.659  -10.471 37.924  1.00   24.31 ? 37  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 37  ? -8.974  -10.328 36.682  1.00   26.30 ? 37  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 37  ? -9.323  -11.834 38.564  1.00   23.90 ? 37  THR A CG2 1 
ATOM   284  N  N   . ALA A 1 38  ? -12.166 -8.871  35.927  1.00   22.20 ? 38  ALA A N   1 
ATOM   285  C  CA  . ALA A 1 38  ? -12.686 -7.575  35.511  1.00   21.93 ? 38  ALA A CA  1 
ATOM   286  C  C   . ALA A 1 38  ? -13.733 -7.154  36.551  1.00   23.35 ? 38  ALA A C   1 
ATOM   287  O  O   . ALA A 1 38  ? -14.530 -7.952  37.024  1.00   23.34 ? 38  ALA A O   1 
ATOM   288  C  CB  . ALA A 1 38  ? -13.307 -7.703  34.135  1.00   21.11 ? 38  ALA A CB  1 
ATOM   289  N  N   . LYS A 1 39  ? -13.747 -5.886  36.906  1.00   22.29 ? 39  LYS A N   1 
ATOM   290  C  CA  . LYS A 1 39  ? -14.615 -5.406  37.958  1.00   22.33 ? 39  LYS A CA  1 
ATOM   291  C  C   . LYS A 1 39  ? -15.989 -4.952  37.373  1.00   22.42 ? 39  LYS A C   1 
ATOM   292  O  O   . LYS A 1 39  ? -16.077 -4.011  36.524  1.00   19.20 ? 39  LYS A O   1 
ATOM   293  C  CB  . LYS A 1 39  ? -13.856 -4.265  38.650  1.00   24.87 ? 39  LYS A CB  1 
ATOM   294  C  CG  . LYS A 1 39  ? -14.675 -3.385  39.586  1.00   26.51 ? 39  LYS A CG  1 
ATOM   295  C  CD  . LYS A 1 39  ? -14.735 -3.920  41.019  1.00   23.98 ? 39  LYS A CD  1 
ATOM   296  C  CE  . LYS A 1 39  ? -15.757 -3.110  41.821  1.00   27.97 ? 39  LYS A CE  1 
ATOM   297  N  NZ  . LYS A 1 39  ? -16.255 -3.846  43.004  1.00   30.10 ? 39  LYS A NZ  1 
ATOM   298  N  N   . TYR A 1 40  ? -17.076 -5.587  37.791  1.00   22.46 ? 40  TYR A N   1 
ATOM   299  C  CA  . TYR A 1 40  ? -18.375 -4.985  37.444  1.00   27.45 ? 40  TYR A CA  1 
ATOM   300  C  C   . TYR A 1 40  ? -18.597 -3.561  38.037  1.00   30.02 ? 40  TYR A C   1 
ATOM   301  O  O   . TYR A 1 40  ? -18.352 -3.305  39.234  1.00   26.33 ? 40  TYR A O   1 
ATOM   302  C  CB  . TYR A 1 40  ? -19.548 -5.930  37.725  1.00   29.30 ? 40  TYR A CB  1 
ATOM   303  C  CG  . TYR A 1 40  ? -20.892 -5.236  37.573  1.00   33.89 ? 40  TYR A CG  1 
ATOM   304  C  CD1 . TYR A 1 40  ? -21.457 -5.033  36.302  1.00   34.42 ? 40  TYR A CD1 1 
ATOM   305  C  CD2 . TYR A 1 40  ? -21.596 -4.760  38.697  1.00   35.63 ? 40  TYR A CD2 1 
ATOM   306  C  CE1 . TYR A 1 40  ? -22.682 -4.412  36.147  1.00   34.21 ? 40  TYR A CE1 1 
ATOM   307  C  CE2 . TYR A 1 40  ? -22.839 -4.133  38.546  1.00   37.27 ? 40  TYR A CE2 1 
ATOM   308  C  CZ  . TYR A 1 40  ? -23.366 -3.964  37.274  1.00   37.87 ? 40  TYR A CZ  1 
ATOM   309  O  OH  . TYR A 1 40  ? -24.569 -3.338  37.120  1.00   41.93 ? 40  TYR A OH  1 
ATOM   310  N  N   . ASP A 1 41  ? -19.057 -2.634  37.185  1.00   28.11 ? 41  ASP A N   1 
ATOM   311  C  CA  . ASP A 1 41  ? -19.300 -1.278  37.635  1.00   30.30 ? 41  ASP A CA  1 
ATOM   312  C  C   . ASP A 1 41  ? -20.693 -0.792  37.252  1.00   35.18 ? 41  ASP A C   1 
ATOM   313  O  O   . ASP A 1 41  ? -20.889 -0.312  36.127  1.00   32.67 ? 41  ASP A O   1 
ATOM   314  C  CB  . ASP A 1 41  ? -18.254 -0.306  37.121  1.00   29.99 ? 41  ASP A CB  1 
ATOM   315  C  CG  . ASP A 1 41  ? -18.466 1.116   37.691  1.00   33.53 ? 41  ASP A CG  1 
ATOM   316  O  OD1 . ASP A 1 41  ? -19.513 1.300   38.378  1.00   35.81 ? 41  ASP A OD1 1 
ATOM   317  O  OD2 . ASP A 1 41  ? -17.603 2.009   37.461  1.00   30.07 ? 41  ASP A OD2 1 
ATOM   318  N  N   . PRO A 1 42  ? -21.660 -0.869  38.204  1.00   38.83 ? 42  PRO A N   1 
ATOM   319  C  CA  . PRO A 1 42  ? -23.037 -0.497  37.884  1.00   39.72 ? 42  PRO A CA  1 
ATOM   320  C  C   . PRO A 1 42  ? -23.170 1.012   37.615  1.00   38.15 ? 42  PRO A C   1 
ATOM   321  O  O   . PRO A 1 42  ? -24.209 1.435   37.137  1.00   40.18 ? 42  PRO A O   1 
ATOM   322  C  CB  . PRO A 1 42  ? -23.810 -0.923  39.137  1.00   43.28 ? 42  PRO A CB  1 
ATOM   323  C  CG  . PRO A 1 42  ? -22.830 -0.710  40.237  1.00   44.20 ? 42  PRO A CG  1 
ATOM   324  C  CD  . PRO A 1 42  ? -21.456 -0.971  39.663  1.00   44.80 ? 42  PRO A CD  1 
ATOM   325  N  N   . SER A 1 43  ? -22.131 1.819   37.877  1.00   34.28 ? 43  SER A N   1 
ATOM   326  C  CA  . SER A 1 43  ? -22.220 3.219   37.460  1.00   34.76 ? 43  SER A CA  1 
ATOM   327  C  C   . SER A 1 43  ? -21.851 3.437   35.962  1.00   35.38 ? 43  SER A C   1 
ATOM   328  O  O   . SER A 1 43  ? -22.001 4.541   35.447  1.00   34.30 ? 43  SER A O   1 
ATOM   329  C  CB  . SER A 1 43  ? -21.410 4.126   38.374  1.00   36.53 ? 43  SER A CB  1 
ATOM   330  O  OG  . SER A 1 43  ? -20.162 4.472   37.795  1.00   41.54 ? 43  SER A OG  1 
ATOM   331  N  N   . LEU A 1 44  ? -21.351 2.404   35.264  1.00   32.20 ? 44  LEU A N   1 
ATOM   332  C  CA  . LEU A 1 44  ? -21.065 2.573   33.829  1.00   26.37 ? 44  LEU A CA  1 
ATOM   333  C  C   . LEU A 1 44  ? -22.375 2.788   33.056  1.00   27.41 ? 44  LEU A C   1 
ATOM   334  O  O   . LEU A 1 44  ? -23.365 2.095   33.321  1.00   27.04 ? 44  LEU A O   1 
ATOM   335  C  CB  . LEU A 1 44  ? -20.303 1.359   33.291  1.00   24.50 ? 44  LEU A CB  1 
ATOM   336  C  CG  . LEU A 1 44  ? -18.813 1.324   33.648  1.00   22.50 ? 44  LEU A CG  1 
ATOM   337  C  CD1 . LEU A 1 44  ? -18.255 -0.035  33.289  1.00   22.36 ? 44  LEU A CD1 1 
ATOM   338  C  CD2 . LEU A 1 44  ? -18.048 2.422   32.940  1.00   20.87 ? 44  LEU A CD2 1 
ATOM   339  N  N   . LYS A 1 45  ? -22.394 3.742   32.115  1.00   27.84 ? 45  LYS A N   1 
ATOM   340  C  CA  . LYS A 1 45  ? -23.598 4.033   31.316  1.00   26.88 ? 45  LYS A CA  1 
ATOM   341  C  C   . LYS A 1 45  ? -23.686 3.082   30.126  1.00   28.41 ? 45  LYS A C   1 
ATOM   342  O  O   . LYS A 1 45  ? -22.660 2.527   29.710  1.00   26.27 ? 45  LYS A O   1 
ATOM   343  C  CB  . LYS A 1 45  ? -23.559 5.457   30.803  1.00   31.68 ? 45  LYS A CB  1 
ATOM   344  C  CG  . LYS A 1 45  ? -23.964 6.500   31.839  1.00   36.61 ? 45  LYS A CG  1 
ATOM   345  C  CD  . LYS A 1 45  ? -23.586 7.895   31.373  1.00   40.66 ? 45  LYS A CD  1 
ATOM   346  C  CE  . LYS A 1 45  ? -22.861 8.618   32.506  1.00   45.91 ? 45  LYS A CE  1 
ATOM   347  N  NZ  . LYS A 1 45  ? -21.600 9.279   32.040  1.00   45.37 ? 45  LYS A NZ  1 
ATOM   348  N  N   . PRO A 1 46  ? -24.908 2.852   29.583  1.00   27.29 ? 46  PRO A N   1 
ATOM   349  C  CA  . PRO A 1 46  ? -24.949 2.106   28.299  1.00   25.87 ? 46  PRO A CA  1 
ATOM   350  C  C   . PRO A 1 46  ? -24.127 2.882   27.242  1.00   24.26 ? 46  PRO A C   1 
ATOM   351  O  O   . PRO A 1 46  ? -24.030 4.102   27.297  1.00   23.01 ? 46  PRO A O   1 
ATOM   352  C  CB  . PRO A 1 46  ? -26.449 2.104   27.944  1.00   27.30 ? 46  PRO A CB  1 
ATOM   353  C  CG  . PRO A 1 46  ? -27.154 2.258   29.247  1.00   27.06 ? 46  PRO A CG  1 
ATOM   354  C  CD  . PRO A 1 46  ? -26.263 3.143   30.102  1.00   26.19 ? 46  PRO A CD  1 
ATOM   355  N  N   . LEU A 1 47  ? -23.513 2.177   26.319  1.00   20.40 ? 47  LEU A N   1 
ATOM   356  C  CA  . LEU A 1 47  ? -22.777 2.810   25.276  1.00   20.88 ? 47  LEU A CA  1 
ATOM   357  C  C   . LEU A 1 47  ? -23.783 3.446   24.305  1.00   22.03 ? 47  LEU A C   1 
ATOM   358  O  O   . LEU A 1 47  ? -24.851 2.888   24.076  1.00   20.23 ? 47  LEU A O   1 
ATOM   359  C  CB  . LEU A 1 47  ? -22.024 1.702   24.572  1.00   22.05 ? 47  LEU A CB  1 
ATOM   360  C  CG  . LEU A 1 47  ? -20.841 2.117   23.781  1.00   25.64 ? 47  LEU A CG  1 
ATOM   361  C  CD1 . LEU A 1 47  ? -19.767 2.741   24.684  1.00   24.46 ? 47  LEU A CD1 1 
ATOM   362  C  CD2 . LEU A 1 47  ? -20.411 0.800   23.142  1.00   23.97 ? 47  LEU A CD2 1 
ATOM   363  N  N   . SER A 1 48  ? -23.471 4.619   23.765  1.00   19.29 ? 48  SER A N   1 
ATOM   364  C  CA  . SER A 1 48  ? -24.334 5.211   22.780  1.00   21.73 ? 48  SER A CA  1 
ATOM   365  C  C   . SER A 1 48  ? -23.671 5.250   21.445  1.00   21.44 ? 48  SER A C   1 
ATOM   366  O  O   . SER A 1 48  ? -22.714 5.986   21.249  1.00   20.42 ? 48  SER A O   1 
ATOM   367  C  CB  . SER A 1 48  ? -24.794 6.619   23.185  1.00   22.17 ? 48  SER A CB  1 
ATOM   368  O  OG  . SER A 1 48  ? -25.639 7.142   22.165  1.00   25.82 ? 48  SER A OG  1 
ATOM   369  N  N   . VAL A 1 49  ? -24.184 4.456   20.517  1.00   20.56 ? 49  VAL A N   1 
ATOM   370  C  CA  . VAL A 1 49  ? -23.590 4.367   19.177  1.00   21.25 ? 49  VAL A CA  1 
ATOM   371  C  C   . VAL A 1 49  ? -24.547 5.064   18.187  1.00   23.70 ? 49  VAL A C   1 
ATOM   372  O  O   . VAL A 1 49  ? -25.636 4.562   17.945  1.00   25.08 ? 49  VAL A O   1 
ATOM   373  C  CB  . VAL A 1 49  ? -23.391 2.907   18.782  1.00   21.91 ? 49  VAL A CB  1 
ATOM   374  C  CG1 . VAL A 1 49  ? -22.604 2.832   17.470  1.00   23.23 ? 49  VAL A CG1 1 
ATOM   375  C  CG2 . VAL A 1 49  ? -22.621 2.186   19.879  1.00   20.18 ? 49  VAL A CG2 1 
ATOM   376  N  N   . SER A 1 50  ? -24.210 6.266   17.707  1.00   22.84 ? 50  SER A N   1 
ATOM   377  C  CA  . SER A 1 50  ? -25.083 6.946   16.749  1.00   22.16 ? 50  SER A CA  1 
ATOM   378  C  C   . SER A 1 50  ? -24.472 7.002   15.398  1.00   21.39 ? 50  SER A C   1 
ATOM   379  O  O   . SER A 1 50  ? -23.762 7.942   15.109  1.00   20.63 ? 50  SER A O   1 
ATOM   380  C  CB  . SER A 1 50  ? -25.426 8.368   17.174  1.00   23.71 ? 50  SER A CB  1 
ATOM   381  O  OG  . SER A 1 50  ? -26.200 8.274   18.316  1.00   27.19 ? 50  SER A OG  1 
ATOM   382  N  N   . TYR A 1 51  ? -24.779 5.990   14.587  1.00   19.64 ? 51  TYR A N   1 
ATOM   383  C  CA  . TYR A 1 51  ? -24.194 5.802   13.298  1.00   20.35 ? 51  TYR A CA  1 
ATOM   384  C  C   . TYR A 1 51  ? -25.214 6.021   12.184  1.00   21.30 ? 51  TYR A C   1 
ATOM   385  O  O   . TYR A 1 51  ? -24.893 5.813   11.016  1.00   20.10 ? 51  TYR A O   1 
ATOM   386  C  CB  . TYR A 1 51  ? -23.595 4.374   13.182  1.00   18.65 ? 51  TYR A CB  1 
ATOM   387  C  CG  . TYR A 1 51  ? -22.308 4.064   13.929  1.00   18.99 ? 51  TYR A CG  1 
ATOM   388  C  CD1 . TYR A 1 51  ? -21.532 5.081   14.532  1.00   19.53 ? 51  TYR A CD1 1 
ATOM   389  C  CD2 . TYR A 1 51  ? -21.802 2.747   13.968  1.00   18.28 ? 51  TYR A CD2 1 
ATOM   390  C  CE1 . TYR A 1 51  ? -20.324 4.788   15.199  1.00   17.93 ? 51  TYR A CE1 1 
ATOM   391  C  CE2 . TYR A 1 51  ? -20.634 2.441   14.636  1.00   18.08 ? 51  TYR A CE2 1 
ATOM   392  C  CZ  . TYR A 1 51  ? -19.880 3.461   15.260  1.00   18.72 ? 51  TYR A CZ  1 
ATOM   393  O  OH  . TYR A 1 51  ? -18.667 3.155   15.865  1.00   16.27 ? 51  TYR A OH  1 
ATOM   394  N  N   . ASP A 1 52  ? -26.415 6.501   12.519  1.00   25.45 ? 52  ASP A N   1 
ATOM   395  C  CA  . ASP A 1 52  ? -27.471 6.698   11.462  1.00   29.62 ? 52  ASP A CA  1 
ATOM   396  C  C   . ASP A 1 52  ? -27.027 7.584   10.266  1.00   28.57 ? 52  ASP A C   1 
ATOM   397  O  O   . ASP A 1 52  ? -27.465 7.380   9.130   1.00   26.65 ? 52  ASP A O   1 
ATOM   398  C  CB  . ASP A 1 52  ? -28.791 7.206   12.052  1.00   32.43 ? 52  ASP A CB  1 
ATOM   399  C  CG  . ASP A 1 52  ? -28.588 8.147   13.245  1.00   41.69 ? 52  ASP A CG  1 
ATOM   400  O  OD1 . ASP A 1 52  ? -28.063 7.700   14.319  1.00   44.60 ? 52  ASP A OD1 1 
ATOM   401  O  OD2 . ASP A 1 52  ? -28.978 9.337   13.118  1.00   45.10 ? 52  ASP A OD2 1 
ATOM   402  N  N   . GLN A 1 53  ? -26.135 8.530   10.525  1.00   26.87 ? 53  GLN A N   1 
ATOM   403  C  CA  . GLN A 1 53  ? -25.765 9.525   9.500   1.00   31.18 ? 53  GLN A CA  1 
ATOM   404  C  C   . GLN A 1 53  ? -24.349 9.355   8.977   1.00   27.48 ? 53  GLN A C   1 
ATOM   405  O  O   . GLN A 1 53  ? -23.759 10.312  8.447   1.00   22.55 ? 53  GLN A O   1 
ATOM   406  C  CB  . GLN A 1 53  ? -25.945 10.937  10.086  1.00   38.75 ? 53  GLN A CB  1 
ATOM   407  C  CG  . GLN A 1 53  ? -27.383 11.218  10.536  1.00   45.28 ? 53  GLN A CG  1 
ATOM   408  C  CD  . GLN A 1 53  ? -28.343 11.052  9.363   1.00   49.97 ? 53  GLN A CD  1 
ATOM   409  O  OE1 . GLN A 1 53  ? -28.146 11.673  8.316   1.00   55.45 ? 53  GLN A OE1 1 
ATOM   410  N  NE2 . GLN A 1 53  ? -29.346 10.178  9.508   1.00   50.21 ? 53  GLN A NE2 1 
ATOM   411  N  N   . ALA A 1 54  ? -23.785 8.145   9.129   1.00   22.35 ? 54  ALA A N   1 
ATOM   412  C  CA  . ALA A 1 54  ? -22.406 7.946   8.828   1.00   18.26 ? 54  ALA A CA  1 
ATOM   413  C  C   . ALA A 1 54  ? -22.181 8.167   7.342   1.00   21.23 ? 54  ALA A C   1 
ATOM   414  O  O   . ALA A 1 54  ? -22.947 7.694   6.491   1.00   19.86 ? 54  ALA A O   1 
ATOM   415  C  CB  . ALA A 1 54  ? -21.913 6.536   9.252   1.00   17.87 ? 54  ALA A CB  1 
ATOM   416  N  N   . THR A 1 55  ? -21.102 8.856   7.012   1.00   19.44 ? 55  THR A N   1 
ATOM   417  C  CA  . THR A 1 55  ? -20.727 8.969   5.621   1.00   20.26 ? 55  THR A CA  1 
ATOM   418  C  C   . THR A 1 55  ? -19.418 8.247   5.366   1.00   20.03 ? 55  THR A C   1 
ATOM   419  O  O   . THR A 1 55  ? -18.358 8.839   5.612   1.00   21.49 ? 55  THR A O   1 
ATOM   420  C  CB  . THR A 1 55  ? -20.585 10.463  5.204   1.00   21.17 ? 55  THR A CB  1 
ATOM   421  O  OG1 . THR A 1 55  ? -21.863 11.073  5.364   1.00   23.10 ? 55  THR A OG1 1 
ATOM   422  C  CG2 . THR A 1 55  ? -20.199 10.569  3.749   1.00   23.30 ? 55  THR A CG2 1 
ATOM   423  N  N   . SER A 1 56  ? -19.470 7.013   4.841   1.00   18.19 ? 56  SER A N   1 
ATOM   424  C  CA  . SER A 1 56  ? -18.240 6.414   4.383   1.00   18.36 ? 56  SER A CA  1 
ATOM   425  C  C   . SER A 1 56  ? -17.861 7.124   3.098   1.00   18.86 ? 56  SER A C   1 
ATOM   426  O  O   . SER A 1 56  ? -18.739 7.560   2.342   1.00   18.66 ? 56  SER A O   1 
ATOM   427  C  CB  . SER A 1 56  ? -18.333 4.891   4.151   1.00   16.93 ? 56  SER A CB  1 
ATOM   428  O  OG  . SER A 1 56  ? -19.239 4.565   3.081   1.00   17.35 ? 56  SER A OG  1 
ATOM   429  N  N   . LEU A 1 57  ? -16.555 7.166   2.871   1.00   17.50 ? 57  LEU A N   1 
ATOM   430  C  CA  . LEU A 1 57  ? -15.896 7.836   1.752   1.00   21.12 ? 57  LEU A CA  1 
ATOM   431  C  C   . LEU A 1 57  ? -15.040 6.926   0.900   1.00   20.07 ? 57  LEU A C   1 
ATOM   432  O  O   . LEU A 1 57  ? -15.130 6.930   -0.325  1.00   17.92 ? 57  LEU A O   1 
ATOM   433  C  CB  . LEU A 1 57  ? -14.947 8.938   2.268   1.00   20.52 ? 57  LEU A CB  1 
ATOM   434  C  CG  . LEU A 1 57  ? -15.676 10.142  2.940   1.00   22.35 ? 57  LEU A CG  1 
ATOM   435  C  CD1 . LEU A 1 57  ? -14.649 11.087  3.575   1.00   22.93 ? 57  LEU A CD1 1 
ATOM   436  C  CD2 . LEU A 1 57  ? -16.579 10.841  1.930   1.00   23.60 ? 57  LEU A CD2 1 
ATOM   437  N  N   . ARG A 1 58  ? -14.139 6.193   1.557   1.00   18.89 ? 58  ARG A N   1 
ATOM   438  C  CA  . ARG A 1 58  ? -13.109 5.549   0.846   1.00   17.88 ? 58  ARG A CA  1 
ATOM   439  C  C   . ARG A 1 58  ? -12.536 4.331   1.620   1.00   17.12 ? 58  ARG A C   1 
ATOM   440  O  O   . ARG A 1 58  ? -12.612 4.252   2.874   1.00   14.78 ? 58  ARG A O   1 
ATOM   441  C  CB  . ARG A 1 58  ? -12.037 6.607   0.607   1.00   21.57 ? 58  ARG A CB  1 
ATOM   442  C  CG  . ARG A 1 58  ? -11.166 6.325   -0.582  1.00   25.88 ? 58  ARG A CG  1 
ATOM   443  C  CD  . ARG A 1 58  ? -10.053 7.360   -0.726  1.00   29.40 ? 58  ARG A CD  1 
ATOM   444  N  NE  . ARG A 1 58  ? -9.281  7.355   0.520   1.00   28.98 ? 58  ARG A NE  1 
ATOM   445  C  CZ  . ARG A 1 58  ? -7.973  7.546   0.606   1.00   28.99 ? 58  ARG A CZ  1 
ATOM   446  N  NH1 . ARG A 1 58  ? -7.250  7.774   -0.484  1.00   27.46 ? 58  ARG A NH1 1 
ATOM   447  N  NH2 . ARG A 1 58  ? -7.389  7.552   1.805   1.00   27.49 ? 58  ARG A NH2 1 
ATOM   448  N  N   . ILE A 1 59  ? -11.981 3.377   0.879   1.00   15.34 ? 59  ILE A N   1 
ATOM   449  C  CA  . ILE A 1 59  ? -11.291 2.254   1.519   1.00   15.43 ? 59  ILE A CA  1 
ATOM   450  C  C   . ILE A 1 59  ? -9.860  2.222   1.049   1.00   16.36 ? 59  ILE A C   1 
ATOM   451  O  O   . ILE A 1 59  ? -9.574  2.346   -0.159  1.00   18.07 ? 59  ILE A O   1 
ATOM   452  C  CB  . ILE A 1 59  ? -12.005 0.894   1.289   1.00   15.10 ? 59  ILE A CB  1 
ATOM   453  C  CG1 . ILE A 1 59  ? -11.374 -0.244  2.128   1.00   15.94 ? 59  ILE A CG1 1 
ATOM   454  C  CG2 . ILE A 1 59  ? -11.911 0.430   -0.175  1.00   14.71 ? 59  ILE A CG2 1 
ATOM   455  C  CD1 . ILE A 1 59  ? -12.289 -1.460  2.199   1.00   16.18 ? 59  ILE A CD1 1 
ATOM   456  N  N   . LEU A 1 60  ? -8.942  2.038   1.985   1.00   16.11 ? 60  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 60  ? -7.510  2.093   1.683   1.00   18.17 ? 60  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 60  ? -6.752  0.896   2.235   1.00   17.74 ? 60  LEU A C   1 
ATOM   459  O  O   . LEU A 1 60  ? -6.961  0.519   3.403   1.00   16.47 ? 60  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 60  ? -6.928  3.415   2.341   1.00   18.88 ? 60  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 60  ? -5.407  3.652   2.440   1.00   21.51 ? 60  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 60  ? -4.872  3.984   1.044   1.00   25.12 ? 60  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 60  ? -5.077  4.790   3.414   1.00   18.96 ? 60  LEU A CD2 1 
ATOM   464  N  N   . ASN A 1 61  ? -5.809  0.361   1.453   1.00   16.62 ? 61  ASN A N   1 
ATOM   465  C  CA  . ASN A 1 61  ? -4.778  -0.554  1.934   1.00   17.14 ? 61  ASN A CA  1 
ATOM   466  C  C   . ASN A 1 61  ? -3.532  0.275   2.269   1.00   19.96 ? 61  ASN A C   1 
ATOM   467  O  O   . ASN A 1 61  ? -2.902  0.864   1.370   1.00   19.34 ? 61  ASN A O   1 
ATOM   468  C  CB  . ASN A 1 61  ? -4.436  -1.589  0.848   1.00   16.51 ? 61  ASN A CB  1 
ATOM   469  C  CG  . ASN A 1 61  ? -3.330  -2.553  1.252   1.00   16.81 ? 61  ASN A CG  1 
ATOM   470  O  OD1 . ASN A 1 61  ? -2.516  -2.284  2.141   1.00   18.88 ? 61  ASN A OD1 1 
ATOM   471  N  ND2 . ASN A 1 61  ? -3.259  -3.698  0.566   1.00   17.28 ? 61  ASN A ND2 1 
ATOM   472  N  N   . ASN A 1 62  ? -3.179  0.357   3.558   1.00   19.83 ? 62  ASN A N   1 
ATOM   473  C  CA  . ASN A 1 62  ? -2.112  1.269   3.963   1.00   18.75 ? 62  ASN A CA  1 
ATOM   474  C  C   . ASN A 1 62  ? -0.866  0.456   4.225   1.00   21.59 ? 62  ASN A C   1 
ATOM   475  O  O   . ASN A 1 62  ? 0.055   0.934   4.908   1.00   25.20 ? 62  ASN A O   1 
ATOM   476  C  CB  . ASN A 1 62  ? -2.493  2.046   5.238   1.00   20.78 ? 62  ASN A CB  1 
ATOM   477  C  CG  . ASN A 1 62  ? -2.720  1.125   6.457   1.00   19.55 ? 62  ASN A CG  1 
ATOM   478  O  OD1 . ASN A 1 62  ? -2.297  -0.032  6.486   1.00   18.55 ? 62  ASN A OD1 1 
ATOM   479  N  ND2 . ASN A 1 62  ? -3.414  1.647   7.462   1.00   21.09 ? 62  ASN A ND2 1 
ATOM   480  N  N   . GLY A 1 63  ? -0.836  -0.786  3.709   1.00   19.69 ? 63  GLY A N   1 
ATOM   481  C  CA  . GLY A 1 63  ? 0.243   -1.718  3.989   1.00   17.50 ? 63  GLY A CA  1 
ATOM   482  C  C   . GLY A 1 63  ? 0.307   -2.406  5.340   1.00   18.56 ? 63  GLY A C   1 
ATOM   483  O  O   . GLY A 1 63  ? 1.148   -3.273  5.520   1.00   18.47 ? 63  GLY A O   1 
ATOM   484  N  N   . HIS A 1 64  ? -0.589  -2.058  6.262   1.00   17.10 ? 64  HIS A N   1 
ATOM   485  C  CA  . HIS A 1 64  ? -0.658  -2.708  7.603   1.00   19.63 ? 64  HIS A CA  1 
ATOM   486  C  C   . HIS A 1 64  ? -2.011  -3.387  7.778   1.00   17.78 ? 64  HIS A C   1 
ATOM   487  O  O   . HIS A 1 64  ? -2.099  -4.424  8.420   1.00   21.12 ? 64  HIS A O   1 
ATOM   488  C  CB  . HIS A 1 64  ? -0.403  -1.696  8.748   1.00   22.12 ? 64  HIS A CB  1 
ATOM   489  C  CG  . HIS A 1 64  ? 0.922   -0.949  8.611   1.00   27.81 ? 64  HIS A CG  1 
ATOM   490  N  ND1 . HIS A 1 64  ? 2.149   -1.559  8.823   1.00   29.17 ? 64  HIS A ND1 1 
ATOM   491  C  CD2 . HIS A 1 64  ? 1.202   0.343   8.169   1.00   31.59 ? 64  HIS A CD2 1 
ATOM   492  C  CE1 . HIS A 1 64  ? 3.145   -0.679  8.563   1.00   30.15 ? 64  HIS A CE1 1 
ATOM   493  N  NE2 . HIS A 1 64  ? 2.574   0.484   8.152   1.00   32.98 ? 64  HIS A NE2 1 
ATOM   494  N  N   . ALA A 1 65  ? -3.057  -2.783  7.229   1.00   16.15 ? 65  ALA A N   1 
ATOM   495  C  CA  . ALA A 1 65  ? -4.400  -3.300  7.275   1.00   16.17 ? 65  ALA A CA  1 
ATOM   496  C  C   . ALA A 1 65  ? -5.188  -2.608  6.163   1.00   16.15 ? 65  ALA A C   1 
ATOM   497  O  O   . ALA A 1 65  ? -4.603  -1.864  5.362   1.00   15.82 ? 65  ALA A O   1 
ATOM   498  C  CB  . ALA A 1 65  ? -5.039  -3.035  8.674   1.00   15.36 ? 65  ALA A CB  1 
ATOM   499  N  N   . PHE A 1 66  ? -6.521  -2.780  6.119   1.00   15.20 ? 66  PHE A N   1 
ATOM   500  C  CA  . PHE A 1 66  ? -7.280  -1.830  5.305   1.00   15.89 ? 66  PHE A CA  1 
ATOM   501  C  C   . PHE A 1 66  ? -8.157  -0.951  6.131   1.00   14.85 ? 66  PHE A C   1 
ATOM   502  O  O   . PHE A 1 66  ? -8.781  -1.414  7.145   1.00   15.16 ? 66  PHE A O   1 
ATOM   503  C  CB  . PHE A 1 66  ? -8.085  -2.569  4.202   1.00   16.26 ? 66  PHE A CB  1 
ATOM   504  C  CG  . PHE A 1 66  ? -9.104  -3.522  4.746   1.00   16.20 ? 66  PHE A CG  1 
ATOM   505  C  CD1 . PHE A 1 66  ? -10.378 -3.070  5.042   1.00   17.12 ? 66  PHE A CD1 1 
ATOM   506  C  CD2 . PHE A 1 66  ? -8.801  -4.870  4.930   1.00   16.58 ? 66  PHE A CD2 1 
ATOM   507  C  CE1 . PHE A 1 66  ? -11.350 -3.938  5.541   1.00   16.76 ? 66  PHE A CE1 1 
ATOM   508  C  CE2 . PHE A 1 66  ? -9.771  -5.728  5.441   1.00   16.18 ? 66  PHE A CE2 1 
ATOM   509  C  CZ  . PHE A 1 66  ? -11.030 -5.276  5.724   1.00   15.48 ? 66  PHE A CZ  1 
ATOM   510  N  N   . ASN A 1 67  ? -8.208  0.335   5.774   1.00   14.79 ? 67  ASN A N   1 
ATOM   511  C  CA  . ASN A 1 67  ? -9.062  1.260   6.510   1.00   15.11 ? 67  ASN A CA  1 
ATOM   512  C  C   . ASN A 1 67  ? -10.261 1.687   5.700   1.00   15.43 ? 67  ASN A C   1 
ATOM   513  O  O   . ASN A 1 67  ? -10.136 2.159   4.557   1.00   15.51 ? 67  ASN A O   1 
ATOM   514  C  CB  . ASN A 1 67  ? -8.330  2.561   6.952   1.00   15.56 ? 67  ASN A CB  1 
ATOM   515  C  CG  . ASN A 1 67  ? -7.202  2.303   7.941   1.00   18.43 ? 67  ASN A CG  1 
ATOM   516  O  OD1 . ASN A 1 67  ? -7.135  1.237   8.536   1.00   18.73 ? 67  ASN A OD1 1 
ATOM   517  N  ND2 . ASN A 1 67  ? -6.279  3.293   8.103   1.00   18.46 ? 67  ASN A ND2 1 
ATOM   518  N  N   . VAL A 1 68  ? -11.414 1.639   6.323   1.00   13.67 ? 68  VAL A N   1 
ATOM   519  C  CA  . VAL A 1 68  ? -12.563 2.266   5.703   1.00   14.40 ? 68  VAL A CA  1 
ATOM   520  C  C   . VAL A 1 68  ? -12.689 3.616   6.419   1.00   15.39 ? 68  VAL A C   1 
ATOM   521  O  O   . VAL A 1 68  ? -12.894 3.671   7.654   1.00   14.51 ? 68  VAL A O   1 
ATOM   522  C  CB  . VAL A 1 68  ? -13.814 1.415   5.863   1.00   13.64 ? 68  VAL A CB  1 
ATOM   523  C  CG1 . VAL A 1 68  ? -15.078 2.242   5.511   1.00   13.64 ? 68  VAL A CG1 1 
ATOM   524  C  CG2 . VAL A 1 68  ? -13.664 0.174   4.976   1.00   13.70 ? 68  VAL A CG2 1 
ATOM   525  N  N   . GLU A 1 69  ? -12.595 4.686   5.665   1.00   16.62 ? 69  GLU A N   1 
ATOM   526  C  CA  . GLU A 1 69  ? -12.678 6.048   6.259   1.00   18.13 ? 69  GLU A CA  1 
ATOM   527  C  C   . GLU A 1 69  ? -14.019 6.731   6.054   1.00   18.06 ? 69  GLU A C   1 
ATOM   528  O  O   . GLU A 1 69  ? -14.689 6.507   5.020   1.00   18.30 ? 69  GLU A O   1 
ATOM   529  C  CB  . GLU A 1 69  ? -11.651 6.915   5.594   1.00   20.26 ? 69  GLU A CB  1 
ATOM   530  C  CG  . GLU A 1 69  ? -10.328 6.229   5.449   1.00   24.16 ? 69  GLU A CG  1 
ATOM   531  C  CD  . GLU A 1 69  ? -9.509  6.830   4.307   1.00   30.24 ? 69  GLU A CD  1 
ATOM   532  O  OE1 . GLU A 1 69  ? -10.115 7.524   3.453   1.00   32.16 ? 69  GLU A OE1 1 
ATOM   533  O  OE2 . GLU A 1 69  ? -8.278  6.555   4.228   1.00   32.22 ? 69  GLU A OE2 1 
ATOM   534  N  N   . PHE A 1 70  ? -14.359 7.614   7.007   1.00   14.37 ? 70  PHE A N   1 
ATOM   535  C  CA  . PHE A 1 70  ? -15.637 8.311   7.083   1.00   14.20 ? 70  PHE A CA  1 
ATOM   536  C  C   . PHE A 1 70  ? -15.397 9.825   7.095   1.00   14.20 ? 70  PHE A C   1 
ATOM   537  O  O   . PHE A 1 70  ? -14.295 10.274  7.395   1.00   13.31 ? 70  PHE A O   1 
ATOM   538  C  CB  . PHE A 1 70  ? -16.405 7.910   8.356   1.00   13.87 ? 70  PHE A CB  1 
ATOM   539  C  CG  . PHE A 1 70  ? -16.937 6.509   8.308   1.00   15.01 ? 70  PHE A CG  1 
ATOM   540  C  CD1 . PHE A 1 70  ? -16.083 5.430   8.470   1.00   14.26 ? 70  PHE A CD1 1 
ATOM   541  C  CD2 . PHE A 1 70  ? -18.264 6.273   8.000   1.00   15.37 ? 70  PHE A CD2 1 
ATOM   542  C  CE1 . PHE A 1 70  ? -16.555 4.122   8.391   1.00   14.15 ? 70  PHE A CE1 1 
ATOM   543  C  CE2 . PHE A 1 70  ? -18.758 4.942   7.910   1.00   14.57 ? 70  PHE A CE2 1 
ATOM   544  C  CZ  . PHE A 1 70  ? -17.887 3.881   8.098   1.00   14.71 ? 70  PHE A CZ  1 
ATOM   545  N  N   . ASP A 1 71  ? -16.424 10.592  6.756   1.00   14.03 ? 71  ASP A N   1 
ATOM   546  C  CA  . ASP A 1 71  ? -16.334 12.034  6.808   1.00   15.48 ? 71  ASP A CA  1 
ATOM   547  C  C   . ASP A 1 71  ? -16.507 12.387  8.292   1.00   14.61 ? 71  ASP A C   1 
ATOM   548  O  O   . ASP A 1 71  ? -17.617 12.215  8.855   1.00   15.43 ? 71  ASP A O   1 
ATOM   549  C  CB  . ASP A 1 71  ? -17.490 12.634  5.988   1.00   16.90 ? 71  ASP A CB  1 
ATOM   550  C  CG  . ASP A 1 71  ? -17.724 14.147  6.285   1.00   18.19 ? 71  ASP A CG  1 
ATOM   551  O  OD1 . ASP A 1 71  ? -16.780 14.816  6.729   1.00   18.73 ? 71  ASP A OD1 1 
ATOM   552  O  OD2 . ASP A 1 71  ? -18.875 14.635  6.192   1.00   19.11 ? 71  ASP A OD2 1 
ATOM   553  N  N   . ASP A 1 72  ? -15.431 12.830  8.929   1.00   14.52 ? 72  ASP A N   1 
ATOM   554  C  CA  . ASP A 1 72  ? -15.479 13.256  10.345  1.00   15.54 ? 72  ASP A CA  1 
ATOM   555  C  C   . ASP A 1 72  ? -15.429 14.790  10.514  1.00   16.46 ? 72  ASP A C   1 
ATOM   556  O  O   . ASP A 1 72  ? -15.020 15.261  11.556  1.00   16.08 ? 72  ASP A O   1 
ATOM   557  C  CB  . ASP A 1 72  ? -14.319 12.626  11.146  1.00   17.39 ? 72  ASP A CB  1 
ATOM   558  C  CG  . ASP A 1 72  ? -12.937 13.101  10.682  1.00   17.39 ? 72  ASP A CG  1 
ATOM   559  O  OD1 . ASP A 1 72  ? -12.815 13.787  9.637   1.00   18.17 ? 72  ASP A OD1 1 
ATOM   560  O  OD2 . ASP A 1 72  ? -11.927 12.772  11.354  1.00   19.73 ? 72  ASP A OD2 1 
ATOM   561  N  N   . SER A 1 73  ? -15.858 15.548  9.505   1.00   16.99 ? 73  SER A N   1 
ATOM   562  C  CA  . SER A 1 73  ? -15.840 17.030  9.568   1.00   18.17 ? 73  SER A CA  1 
ATOM   563  C  C   . SER A 1 73  ? -17.123 17.562  10.192  1.00   19.19 ? 73  SER A C   1 
ATOM   564  O  O   . SER A 1 73  ? -17.280 18.789  10.376  1.00   19.07 ? 73  SER A O   1 
ATOM   565  C  CB  . SER A 1 73  ? -15.619 17.613  8.158   1.00   18.04 ? 73  SER A CB  1 
ATOM   566  O  OG  . SER A 1 73  ? -16.797 17.334  7.378   1.00   18.49 ? 73  SER A OG  1 
ATOM   567  N  N   . GLN A 1 74  ? -18.056 16.662  10.537  1.00   18.48 ? 74  GLN A N   1 
ATOM   568  C  CA  . GLN A 1 74  ? -19.261 17.053  11.270  1.00   21.34 ? 74  GLN A CA  1 
ATOM   569  C  C   . GLN A 1 74  ? -19.592 15.875  12.180  1.00   22.76 ? 74  GLN A C   1 
ATOM   570  O  O   . GLN A 1 74  ? -19.084 14.774  11.968  1.00   23.19 ? 74  GLN A O   1 
ATOM   571  C  CB  . GLN A 1 74  ? -20.496 17.303  10.358  1.00   22.20 ? 74  GLN A CB  1 
ATOM   572  C  CG  . GLN A 1 74  ? -20.336 18.286  9.237   1.00   25.34 ? 74  GLN A CG  1 
ATOM   573  C  CD  . GLN A 1 74  ? -21.612 18.391  8.383   1.00   26.45 ? 74  GLN A CD  1 
ATOM   574  O  OE1 . GLN A 1 74  ? -22.631 18.813  8.875   1.00   31.32 ? 74  GLN A OE1 1 
ATOM   575  N  NE2 . GLN A 1 74  ? -21.546 17.986  7.126   1.00   27.85 ? 74  GLN A NE2 1 
ATOM   576  N  N   . ASP A 1 75  ? -20.416 16.119  13.203  1.00   25.96 ? 75  ASP A N   1 
ATOM   577  C  CA  . ASP A 1 75  ? -20.896 15.052  14.105  1.00   28.12 ? 75  ASP A CA  1 
ATOM   578  C  C   . ASP A 1 75  ? -21.972 14.274  13.348  1.00   30.51 ? 75  ASP A C   1 
ATOM   579  O  O   . ASP A 1 75  ? -23.139 14.688  13.355  1.00   33.55 ? 75  ASP A O   1 
ATOM   580  C  CB  . ASP A 1 75  ? -21.569 15.603  15.382  1.00   30.16 ? 75  ASP A CB  1 
ATOM   581  C  CG  . ASP A 1 75  ? -20.590 16.221  16.374  1.00   33.39 ? 75  ASP A CG  1 
ATOM   582  O  OD1 . ASP A 1 75  ? -19.364 16.268  16.119  1.00   35.14 ? 75  ASP A OD1 1 
ATOM   583  O  OD2 . ASP A 1 75  ? -21.078 16.681  17.425  1.00   32.73 ? 75  ASP A OD2 1 
ATOM   584  N  N   . LYS A 1 76  ? -21.594 13.174  12.722  1.00   23.92 ? 76  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 76  ? -22.498 12.388  11.886  1.00   25.06 ? 76  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 76  ? -22.576 10.931  12.381  1.00   26.79 ? 76  LYS A C   1 
ATOM   587  O  O   . LYS A 1 76  ? -23.634 10.251  12.274  1.00   33.82 ? 76  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 76  ? -21.948 12.347  10.458  1.00   24.47 ? 76  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 76  ? -22.255 13.570  9.589   1.00   23.91 ? 76  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 76  ? -21.560 13.373  8.263   1.00   22.70 ? 76  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 76  ? -22.027 14.392  7.241   1.00   24.25 ? 76  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 76  ? -21.733 13.798  5.915   1.00   20.03 ? 76  LYS A NZ  1 
ATOM   593  N  N   . ALA A 1 77  ? -21.425 10.411  12.787  1.00   21.07 ? 77  ALA A N   1 
ATOM   594  C  CA  . ALA A 1 77  ? -21.348 9.044   13.391  1.00   20.41 ? 77  ALA A CA  1 
ATOM   595  C  C   . ALA A 1 77  ? -20.568 9.276   14.667  1.00   18.19 ? 77  ALA A C   1 
ATOM   596  O  O   . ALA A 1 77  ? -19.349 9.538   14.618  1.00   20.94 ? 77  ALA A O   1 
ATOM   597  C  CB  . ALA A 1 77  ? -20.596 8.110   12.462  1.00   16.94 ? 77  ALA A CB  1 
ATOM   598  N  N   . VAL A 1 78  ? -21.254 9.213   15.797  1.00   17.88 ? 78  VAL A N   1 
ATOM   599  C  CA  . VAL A 1 78  ? -20.600 9.457   17.074  1.00   17.33 ? 78  VAL A CA  1 
ATOM   600  C  C   . VAL A 1 78  ? -20.772 8.325   18.105  1.00   15.98 ? 78  VAL A C   1 
ATOM   601  O  O   . VAL A 1 78  ? -21.813 7.654   18.168  1.00   14.45 ? 78  VAL A O   1 
ATOM   602  C  CB  . VAL A 1 78  ? -21.049 10.811  17.697  1.00   17.86 ? 78  VAL A CB  1 
ATOM   603  C  CG1 . VAL A 1 78  ? -20.707 12.010  16.760  1.00   17.25 ? 78  VAL A CG1 1 
ATOM   604  C  CG2 . VAL A 1 78  ? -22.562 10.783  17.970  1.00   18.71 ? 78  VAL A CG2 1 
ATOM   605  N  N   . LEU A 1 79  ? -19.742 8.179   18.929  1.00   14.94 ? 79  LEU A N   1 
ATOM   606  C  CA  . LEU A 1 79  ? -19.778 7.327   20.103  1.00   15.70 ? 79  LEU A CA  1 
ATOM   607  C  C   . LEU A 1 79  ? -19.814 8.206   21.354  1.00   15.45 ? 79  LEU A C   1 
ATOM   608  O  O   . LEU A 1 79  ? -19.078 9.198   21.489  1.00   13.93 ? 79  LEU A O   1 
ATOM   609  C  CB  . LEU A 1 79  ? -18.514 6.490   20.117  1.00   16.79 ? 79  LEU A CB  1 
ATOM   610  C  CG  . LEU A 1 79  ? -18.415 5.421   21.174  1.00   17.86 ? 79  LEU A CG  1 
ATOM   611  C  CD1 . LEU A 1 79  ? -19.537 4.397   20.966  1.00   18.42 ? 79  LEU A CD1 1 
ATOM   612  C  CD2 . LEU A 1 79  ? -17.021 4.769   21.181  1.00   17.24 ? 79  LEU A CD2 1 
ATOM   613  N  N   . LYS A 1 80  ? -20.713 7.889   22.255  1.00   16.19 ? 80  LYS A N   1 
ATOM   614  C  CA  . LYS A 1 80  ? -20.716 8.595   23.525  1.00   19.94 ? 80  LYS A CA  1 
ATOM   615  C  C   . LYS A 1 80  ? -21.265 7.702   24.623  1.00   19.19 ? 80  LYS A C   1 
ATOM   616  O  O   . LYS A 1 80  ? -21.558 6.543   24.367  1.00   17.66 ? 80  LYS A O   1 
ATOM   617  C  CB  . LYS A 1 80  ? -21.438 9.934   23.451  1.00   22.63 ? 80  LYS A CB  1 
ATOM   618  C  CG  . LYS A 1 80  ? -22.871 9.836   22.977  1.00   30.79 ? 80  LYS A CG  1 
ATOM   619  C  CD  . LYS A 1 80  ? -23.640 11.107  23.389  1.00   37.68 ? 80  LYS A CD  1 
ATOM   620  C  CE  . LYS A 1 80  ? -23.815 12.037  22.210  1.00   40.61 ? 80  LYS A CE  1 
ATOM   621  N  NZ  . LYS A 1 80  ? -22.503 12.348  21.593  1.00   48.14 ? 80  LYS A NZ  1 
ATOM   622  N  N   . GLY A 1 81  ? -21.363 8.232   25.825  1.00   19.94 ? 81  GLY A N   1 
ATOM   623  C  CA  . GLY A 1 81  ? -21.975 7.480   26.895  1.00   19.91 ? 81  GLY A CA  1 
ATOM   624  C  C   . GLY A 1 81  ? -21.005 6.375   27.313  1.00   21.39 ? 81  GLY A C   1 
ATOM   625  O  O   . GLY A 1 81  ? -19.777 6.584   27.247  1.00   20.34 ? 81  GLY A O   1 
ATOM   626  N  N   . GLY A 1 82  ? -21.516 5.221   27.758  1.00   19.16 ? 82  GLY A N   1 
ATOM   627  C  CA  . GLY A 1 82  ? -20.566 4.196   28.188  1.00   19.90 ? 82  GLY A CA  1 
ATOM   628  C  C   . GLY A 1 82  ? -19.621 4.787   29.227  1.00   21.40 ? 82  GLY A C   1 
ATOM   629  O  O   . GLY A 1 82  ? -20.094 5.501   30.101  1.00   23.95 ? 82  GLY A O   1 
ATOM   630  N  N   . PRO A 1 83  ? -18.280 4.525   29.141  1.00   18.89 ? 83  PRO A N   1 
ATOM   631  C  CA  . PRO A 1 83  ? -17.401 5.114   30.134  1.00   17.83 ? 83  PRO A CA  1 
ATOM   632  C  C   . PRO A 1 83  ? -17.020 6.559   29.767  1.00   19.17 ? 83  PRO A C   1 
ATOM   633  O  O   . PRO A 1 83  ? -16.193 7.148   30.423  1.00   20.06 ? 83  PRO A O   1 
ATOM   634  C  CB  . PRO A 1 83  ? -16.149 4.218   30.044  1.00   19.69 ? 83  PRO A CB  1 
ATOM   635  C  CG  . PRO A 1 83  ? -16.102 3.827   28.596  1.00   15.82 ? 83  PRO A CG  1 
ATOM   636  C  CD  . PRO A 1 83  ? -17.539 3.683   28.162  1.00   17.02 ? 83  PRO A CD  1 
ATOM   637  N  N   . LEU A 1 84  ? -17.633 7.168   28.761  1.00   17.62 ? 84  LEU A N   1 
ATOM   638  C  CA  . LEU A 1 84  ? -16.986 8.373   28.196  1.00   18.45 ? 84  LEU A CA  1 
ATOM   639  C  C   . LEU A 1 84  ? -17.658 9.655   28.681  1.00   21.19 ? 84  LEU A C   1 
ATOM   640  O  O   . LEU A 1 84  ? -18.857 9.664   28.793  1.00   20.78 ? 84  LEU A O   1 
ATOM   641  C  CB  . LEU A 1 84  ? -17.023 8.330   26.643  1.00   15.54 ? 84  LEU A CB  1 
ATOM   642  C  CG  . LEU A 1 84  ? -16.464 7.037   26.000  1.00   15.87 ? 84  LEU A CG  1 
ATOM   643  C  CD1 . LEU A 1 84  ? -16.959 6.901   24.565  1.00   15.61 ? 84  LEU A CD1 1 
ATOM   644  C  CD2 . LEU A 1 84  ? -14.927 7.007   25.955  1.00   14.82 ? 84  LEU A CD2 1 
ATOM   645  N  N   . ASP A 1 85  ? -16.912 10.756  28.860  1.00   23.64 ? 85  ASP A N   1 
ATOM   646  C  CA  . ASP A 1 85  ? -17.597 12.023  29.120  1.00   30.09 ? 85  ASP A CA  1 
ATOM   647  C  C   . ASP A 1 85  ? -17.673 12.841  27.837  1.00   30.94 ? 85  ASP A C   1 
ATOM   648  O  O   . ASP A 1 85  ? -18.635 13.554  27.620  1.00   34.84 ? 85  ASP A O   1 
ATOM   649  C  CB  . ASP A 1 85  ? -16.999 12.804  30.315  1.00   33.51 ? 85  ASP A CB  1 
ATOM   650  C  CG  . ASP A 1 85  ? -17.202 12.082  31.668  1.00   37.92 ? 85  ASP A CG  1 
ATOM   651  O  OD1 . ASP A 1 85  ? -18.324 11.569  31.991  1.00   37.79 ? 85  ASP A OD1 1 
ATOM   652  O  OD2 . ASP A 1 85  ? -16.201 12.022  32.416  1.00   42.07 ? 85  ASP A OD2 1 
ATOM   653  N  N   . GLY A 1 86  ? -16.723 12.677  26.942  1.00   29.66 ? 86  GLY A N   1 
ATOM   654  C  CA  . GLY A 1 86  ? -16.836 13.317  25.657  1.00   29.51 ? 86  GLY A CA  1 
ATOM   655  C  C   . GLY A 1 86  ? -17.734 12.693  24.588  1.00   29.79 ? 86  GLY A C   1 
ATOM   656  O  O   . GLY A 1 86  ? -18.395 11.643  24.779  1.00   28.39 ? 86  GLY A O   1 
ATOM   657  N  N   . THR A 1 87  ? -17.780 13.397  23.460  1.00   25.94 ? 87  THR A N   1 
ATOM   658  C  CA  . THR A 1 87  ? -18.342 12.916  22.221  1.00   23.89 ? 87  THR A CA  1 
ATOM   659  C  C   . THR A 1 87  ? -17.183 12.628  21.291  1.00   20.51 ? 87  THR A C   1 
ATOM   660  O  O   . THR A 1 87  ? -16.234 13.466  21.133  1.00   16.95 ? 87  THR A O   1 
ATOM   661  C  CB  . THR A 1 87  ? -19.187 13.994  21.558  1.00   27.93 ? 87  THR A CB  1 
ATOM   662  O  OG1 . THR A 1 87  ? -20.347 14.226  22.370  1.00   32.49 ? 87  THR A OG1 1 
ATOM   663  C  CG2 . THR A 1 87  ? -19.598 13.560  20.141  1.00   26.31 ? 87  THR A CG2 1 
ATOM   664  N  N   . TYR A 1 88  ? -17.248 11.463  20.664  1.00   16.23 ? 88  TYR A N   1 
ATOM   665  C  CA  . TYR A 1 88  ? -16.153 11.021  19.831  1.00   14.91 ? 88  TYR A CA  1 
ATOM   666  C  C   . TYR A 1 88  ? -16.700 10.710  18.442  1.00   14.16 ? 88  TYR A C   1 
ATOM   667  O  O   . TYR A 1 88  ? -17.673 10.000  18.355  1.00   16.82 ? 88  TYR A O   1 
ATOM   668  C  CB  . TYR A 1 88  ? -15.475 9.800   20.448  1.00   13.53 ? 88  TYR A CB  1 
ATOM   669  C  CG  . TYR A 1 88  ? -14.761 10.014  21.767  1.00   13.17 ? 88  TYR A CG  1 
ATOM   670  C  CD1 . TYR A 1 88  ? -15.481 10.203  22.946  1.00   12.75 ? 88  TYR A CD1 1 
ATOM   671  C  CD2 . TYR A 1 88  ? -13.339 9.921   21.846  1.00   13.11 ? 88  TYR A CD2 1 
ATOM   672  C  CE1 . TYR A 1 88  ? -14.826 10.363  24.140  1.00   13.66 ? 88  TYR A CE1 1 
ATOM   673  C  CE2 . TYR A 1 88  ? -12.647 10.072  23.061  1.00   13.20 ? 88  TYR A CE2 1 
ATOM   674  C  CZ  . TYR A 1 88  ? -13.413 10.296  24.200  1.00   13.25 ? 88  TYR A CZ  1 
ATOM   675  O  OH  . TYR A 1 88  ? -12.812 10.445  25.397  1.00   14.61 ? 88  TYR A OH  1 
ATOM   676  N  N   . ARG A 1 89  ? -16.166 11.350  17.410  1.00   14.10 ? 89  ARG A N   1 
ATOM   677  C  CA  . ARG A 1 89  ? -16.515 11.115  15.988  1.00   14.96 ? 89  ARG A CA  1 
ATOM   678  C  C   . ARG A 1 89  ? -15.734 9.963   15.354  1.00   13.14 ? 89  ARG A C   1 
ATOM   679  O  O   . ARG A 1 89  ? -14.518 9.852   15.488  1.00   12.83 ? 89  ARG A O   1 
ATOM   680  C  CB  . ARG A 1 89  ? -16.206 12.335  15.105  1.00   16.21 ? 89  ARG A CB  1 
ATOM   681  C  CG  . ARG A 1 89  ? -17.090 13.566  15.300  1.00   18.81 ? 89  ARG A CG  1 
ATOM   682  C  CD  . ARG A 1 89  ? -16.536 14.672  14.417  1.00   16.80 ? 89  ARG A CD  1 
ATOM   683  N  NE  . ARG A 1 89  ? -17.311 15.881  14.644  1.00   20.54 ? 89  ARG A NE  1 
ATOM   684  C  CZ  . ARG A 1 89  ? -16.968 17.088  14.191  1.00   22.11 ? 89  ARG A CZ  1 
ATOM   685  N  NH1 . ARG A 1 89  ? -15.839 17.238  13.506  1.00   22.80 ? 89  ARG A NH1 1 
ATOM   686  N  NH2 . ARG A 1 89  ? -17.762 18.139  14.421  1.00   21.81 ? 89  ARG A NH2 1 
ATOM   687  N  N   . LEU A 1 90  ? -16.469 9.062   14.715  1.00   13.85 ? 90  LEU A N   1 
ATOM   688  C  CA  . LEU A 1 90  ? -15.894 7.991   13.911  1.00   12.47 ? 90  LEU A CA  1 
ATOM   689  C  C   . LEU A 1 90  ? -15.059 8.529   12.793  1.00   12.46 ? 90  LEU A C   1 
ATOM   690  O  O   . LEU A 1 90  ? -15.534 9.278   11.913  1.00   13.88 ? 90  LEU A O   1 
ATOM   691  C  CB  . LEU A 1 90  ? -17.047 7.146   13.313  1.00   12.92 ? 90  LEU A CB  1 
ATOM   692  C  CG  . LEU A 1 90  ? -16.661 5.942   12.435  1.00   13.41 ? 90  LEU A CG  1 
ATOM   693  C  CD1 . LEU A 1 90  ? -15.894 4.882   13.192  1.00   14.45 ? 90  LEU A CD1 1 
ATOM   694  C  CD2 . LEU A 1 90  ? -17.940 5.241   11.940  1.00   13.68 ? 90  LEU A CD2 1 
ATOM   695  N  N   . ILE A 1 91  ? -13.803 8.160   12.780  1.00   11.12 ? 91  ILE A N   1 
ATOM   696  C  CA  . ILE A 1 91  ? -12.942 8.513   11.664  1.00   11.07 ? 91  ILE A CA  1 
ATOM   697  C  C   . ILE A 1 91  ? -12.708 7.370   10.684  1.00   11.20 ? 91  ILE A C   1 
ATOM   698  O  O   . ILE A 1 91  ? -12.680 7.575   9.428   1.00   10.56 ? 91  ILE A O   1 
ATOM   699  C  CB  . ILE A 1 91  ? -11.591 9.166   12.117  1.00   11.36 ? 91  ILE A CB  1 
ATOM   700  C  CG1 . ILE A 1 91  ? -10.688 9.503   10.889  1.00   11.33 ? 91  ILE A CG1 1 
ATOM   701  C  CG2 . ILE A 1 91  ? -10.864 8.281   13.121  1.00   10.94 ? 91  ILE A CG2 1 
ATOM   702  C  CD1 . ILE A 1 91  ? -9.554  10.460  11.267  1.00   14.06 ? 91  ILE A CD1 1 
ATOM   703  N  N   . GLN A 1 92  ? -12.589 6.151   11.225  1.00   11.48 ? 92  GLN A N   1 
ATOM   704  C  CA  . GLN A 1 92  ? -12.272 4.995   10.348  1.00   11.34 ? 92  GLN A CA  1 
ATOM   705  C  C   . GLN A 1 92  ? -12.511 3.713   11.126  1.00   10.78 ? 92  GLN A C   1 
ATOM   706  O  O   . GLN A 1 92  ? -12.598 3.793   12.333  1.00   10.64 ? 92  GLN A O   1 
ATOM   707  C  CB  . GLN A 1 92  ? -10.822 5.049   9.793   1.00   12.61 ? 92  GLN A CB  1 
ATOM   708  C  CG  . GLN A 1 92  ? -9.638  5.081   10.774  1.00   13.85 ? 92  GLN A CG  1 
ATOM   709  C  CD  . GLN A 1 92  ? -8.974  3.731   11.013  1.00   15.44 ? 92  GLN A CD  1 
ATOM   710  O  OE1 . GLN A 1 92  ? -9.626  2.693   11.133  1.00   14.78 ? 92  GLN A OE1 1 
ATOM   711  N  NE2 . GLN A 1 92  ? -7.670  3.756   11.189  1.00   18.62 ? 92  GLN A NE2 1 
ATOM   712  N  N   . PHE A 1 93  ? -12.657 2.582   10.418  1.00   9.62  ? 93  PHE A N   1 
ATOM   713  C  CA  . PHE A 1 93  ? -12.519 1.248   11.002  1.00   9.36  ? 93  PHE A CA  1 
ATOM   714  C  C   . PHE A 1 93  ? -11.573 0.358   10.188  1.00   9.47  ? 93  PHE A C   1 
ATOM   715  O  O   . PHE A 1 93  ? -11.322 0.580   8.988   1.00   9.46  ? 93  PHE A O   1 
ATOM   716  C  CB  . PHE A 1 93  ? -13.928 0.611   11.260  1.00   9.06  ? 93  PHE A CB  1 
ATOM   717  C  CG  . PHE A 1 93  ? -14.625 0.127   10.020  1.00   9.79  ? 93  PHE A CG  1 
ATOM   718  C  CD1 . PHE A 1 93  ? -14.195 -1.004  9.346   1.00   11.14 ? 93  PHE A CD1 1 
ATOM   719  C  CD2 . PHE A 1 93  ? -15.765 0.812   9.528   1.00   10.46 ? 93  PHE A CD2 1 
ATOM   720  C  CE1 . PHE A 1 93  ? -14.847 -1.482  8.187   1.00   11.36 ? 93  PHE A CE1 1 
ATOM   721  C  CE2 . PHE A 1 93  ? -16.443 0.330   8.404   1.00   12.44 ? 93  PHE A CE2 1 
ATOM   722  C  CZ  . PHE A 1 93  ? -15.973 -0.802  7.711   1.00   11.77 ? 93  PHE A CZ  1 
ATOM   723  N  N   . HIS A 1 94  ? -10.965 -0.650  10.847  1.00   9.96  ? 94  HIS A N   1 
ATOM   724  C  CA  . HIS A 1 94  ? -10.009 -1.515  10.201  1.00   9.24  ? 94  HIS A CA  1 
ATOM   725  C  C   . HIS A 1 94  ? -10.119 -2.762  11.028  1.00   9.54  ? 94  HIS A C   1 
ATOM   726  O  O   . HIS A 1 94  ? -10.855 -2.778  12.058  1.00   8.67  ? 94  HIS A O   1 
ATOM   727  C  CB  . HIS A 1 94  ? -8.544  -0.935  10.216  1.00   9.82  ? 94  HIS A CB  1 
ATOM   728  C  CG  . HIS A 1 94  ? -8.054  -0.648  11.634  1.00   10.57 ? 94  HIS A CG  1 
ATOM   729  N  ND1 . HIS A 1 94  ? -8.354  0.488   12.291  1.00   10.10 ? 94  HIS A ND1 1 
ATOM   730  C  CD2 . HIS A 1 94  ? -7.329  -1.440  12.535  1.00   9.71  ? 94  HIS A CD2 1 
ATOM   731  C  CE1 . HIS A 1 94  ? -7.812  0.448   13.530  1.00   9.85  ? 94  HIS A CE1 1 
ATOM   732  N  NE2 . HIS A 1 94  ? -7.185  -0.727  13.675  1.00   9.69  ? 94  HIS A NE2 1 
ATOM   733  N  N   . PHE A 1 95  ? -9.379  -3.798  10.618  1.00   8.72  ? 95  PHE A N   1 
ATOM   734  C  CA  . PHE A 1 95  ? -9.438  -5.097  11.279  1.00   8.73  ? 95  PHE A CA  1 
ATOM   735  C  C   . PHE A 1 95  ? -8.006  -5.578  11.438  1.00   8.57  ? 95  PHE A C   1 
ATOM   736  O  O   . PHE A 1 95  ? -7.078  -5.063  10.802  1.00   8.49  ? 95  PHE A O   1 
ATOM   737  C  CB  . PHE A 1 95  ? -10.153 -6.170  10.379  1.00   8.98  ? 95  PHE A CB  1 
ATOM   738  C  CG  . PHE A 1 95  ? -11.628 -5.898  10.075  1.00   9.61  ? 95  PHE A CG  1 
ATOM   739  C  CD1 . PHE A 1 95  ? -11.991 -5.124  8.968   1.00   10.21 ? 95  PHE A CD1 1 
ATOM   740  C  CD2 . PHE A 1 95  ? -12.647 -6.519  10.809  1.00   10.54 ? 95  PHE A CD2 1 
ATOM   741  C  CE1 . PHE A 1 95  ? -13.310 -4.933  8.597   1.00   10.31 ? 95  PHE A CE1 1 
ATOM   742  C  CE2 . PHE A 1 95  ? -13.975 -6.343  10.453  1.00   10.06 ? 95  PHE A CE2 1 
ATOM   743  C  CZ  . PHE A 1 95  ? -14.319 -5.546  9.338   1.00   11.07 ? 95  PHE A CZ  1 
ATOM   744  N  N   . HIS A 1 96  ? -7.827  -6.531  12.349  1.00   8.26  ? 96  HIS A N   1 
ATOM   745  C  CA  . HIS A 1 96  ? -6.599  -7.324  12.431  1.00   8.39  ? 96  HIS A CA  1 
ATOM   746  C  C   . HIS A 1 96  ? -7.024  -8.753  12.318  1.00   8.92  ? 96  HIS A C   1 
ATOM   747  O  O   . HIS A 1 96  ? -8.079  -9.086  12.861  1.00   8.74  ? 96  HIS A O   1 
ATOM   748  C  CB  . HIS A 1 96  ? -5.950  -7.099  13.779  1.00   8.77  ? 96  HIS A CB  1 
ATOM   749  C  CG  . HIS A 1 96  ? -5.674  -5.620  14.068  1.00   9.19  ? 96  HIS A CG  1 
ATOM   750  N  ND1 . HIS A 1 96  ? -4.472  -5.068  13.833  1.00   8.91  ? 96  HIS A ND1 1 
ATOM   751  C  CD2 . HIS A 1 96  ? -6.500  -4.582  14.536  1.00   9.35  ? 96  HIS A CD2 1 
ATOM   752  C  CE1 . HIS A 1 96  ? -4.477  -3.773  14.242  1.00   9.84  ? 96  HIS A CE1 1 
ATOM   753  N  NE2 . HIS A 1 96  ? -5.716  -3.453  14.602  1.00   10.25 ? 96  HIS A NE2 1 
ATOM   754  N  N   . TRP A 1 97  ? -6.213  -9.620  11.672  1.00   9.18  ? 97  TRP A N   1 
ATOM   755  C  CA  . TRP A 1 97  ? -6.678  -11.011 11.473  1.00   10.09 ? 97  TRP A CA  1 
ATOM   756  C  C   . TRP A 1 97  ? -5.536  -11.972 11.386  1.00   9.91  ? 97  TRP A C   1 
ATOM   757  O  O   . TRP A 1 97  ? -4.405  -11.545 11.289  1.00   10.71 ? 97  TRP A O   1 
ATOM   758  C  CB  . TRP A 1 97  ? -7.598  -11.125 10.268  1.00   10.62 ? 97  TRP A CB  1 
ATOM   759  C  CG  . TRP A 1 97  ? -6.917  -10.725 8.970   1.00   11.67 ? 97  TRP A CG  1 
ATOM   760  C  CD1 . TRP A 1 97  ? -6.188  -11.532 8.068   1.00   11.88 ? 97  TRP A CD1 1 
ATOM   761  C  CD2 . TRP A 1 97  ? -6.867  -9.384  8.430   1.00   12.16 ? 97  TRP A CD2 1 
ATOM   762  N  NE1 . TRP A 1 97  ? -5.703  -10.787 7.025   1.00   12.31 ? 97  TRP A NE1 1 
ATOM   763  C  CE2 . TRP A 1 97  ? -6.108  -9.460  7.184   1.00   12.69 ? 97  TRP A CE2 1 
ATOM   764  C  CE3 . TRP A 1 97  ? -7.389  -8.136  8.845   1.00   12.51 ? 97  TRP A CE3 1 
ATOM   765  C  CZ2 . TRP A 1 97  ? -5.863  -8.326  6.407   1.00   12.71 ? 97  TRP A CZ2 1 
ATOM   766  C  CZ3 . TRP A 1 97  ? -7.133  -7.000  8.045   1.00   11.58 ? 97  TRP A CZ3 1 
ATOM   767  C  CH2 . TRP A 1 97  ? -6.406  -7.097  6.851   1.00   12.43 ? 97  TRP A CH2 1 
ATOM   768  N  N   . GLY A 1 98  ? -5.807  -13.275 11.349  1.00   9.23  ? 98  GLY A N   1 
ATOM   769  C  CA  . GLY A 1 98  ? -4.706  -14.208 11.434  1.00   9.78  ? 98  GLY A CA  1 
ATOM   770  C  C   . GLY A 1 98  ? -4.465  -14.972 10.133  1.00   10.96 ? 98  GLY A C   1 
ATOM   771  O  O   . GLY A 1 98  ? -5.166  -14.751 9.156   1.00   10.37 ? 98  GLY A O   1 
ATOM   772  N  N   . SER A 1 99  ? -3.429  -15.817 10.112  1.00   11.70 ? 99  SER A N   1 
ATOM   773  C  CA  . SER A 1 99  ? -3.166  -16.679 8.956   1.00   13.97 ? 99  SER A CA  1 
ATOM   774  C  C   . SER A 1 99  ? -4.071  -17.927 9.057   1.00   15.47 ? 99  SER A C   1 
ATOM   775  O  O   . SER A 1 99  ? -4.240  -18.661 8.090   1.00   16.94 ? 99  SER A O   1 
ATOM   776  C  CB  . SER A 1 99  ? -1.720  -17.094 9.036   1.00   13.47 ? 99  SER A CB  1 
ATOM   777  O  OG  . SER A 1 99  ? -1.437  -17.574 10.371  1.00   13.93 ? 99  SER A OG  1 
ATOM   778  N  N   . LEU A 1 100 ? -4.627  -18.142 10.250  1.00   16.36 ? 100 LEU A N   1 
ATOM   779  C  CA  . LEU A 1 100 ? -5.489  -19.276 10.600  1.00   18.12 ? 100 LEU A CA  1 
ATOM   780  C  C   . LEU A 1 100 ? -6.691  -18.810 11.390  1.00   16.81 ? 100 LEU A C   1 
ATOM   781  O  O   . LEU A 1 100 ? -6.624  -17.798 12.099  1.00   14.73 ? 100 LEU A O   1 
ATOM   782  C  CB  . LEU A 1 100 ? -4.720  -20.189 11.551  1.00   20.06 ? 100 LEU A CB  1 
ATOM   783  C  CG  . LEU A 1 100 ? -3.491  -20.831 10.979  1.00   24.45 ? 100 LEU A CG  1 
ATOM   784  C  CD1 . LEU A 1 100 ? -2.369  -20.635 11.988  1.00   29.69 ? 100 LEU A CD1 1 
ATOM   785  C  CD2 . LEU A 1 100 ? -3.765  -22.312 10.704  1.00   27.52 ? 100 LEU A CD2 1 
ATOM   786  N  N   . ASP A 1 101 ? -7.806  -19.547 11.307  1.00   16.83 ? 101 ASP A N   1 
ATOM   787  C  CA  . ASP A 1 101 ? -8.979  -19.137 12.096  1.00   15.57 ? 101 ASP A CA  1 
ATOM   788  C  C   . ASP A 1 101 ? -8.692  -19.142 13.599  1.00   16.39 ? 101 ASP A C   1 
ATOM   789  O  O   . ASP A 1 101 ? -9.350  -18.457 14.332  1.00   15.95 ? 101 ASP A O   1 
ATOM   790  C  CB  . ASP A 1 101 ? -10.187 -20.009 11.826  1.00   16.77 ? 101 ASP A CB  1 
ATOM   791  C  CG  . ASP A 1 101 ? -10.665 -19.919 10.417  1.00   19.21 ? 101 ASP A CG  1 
ATOM   792  O  OD1 . ASP A 1 101 ? -10.235 -19.029 9.649   1.00   16.93 ? 101 ASP A OD1 1 
ATOM   793  O  OD2 . ASP A 1 101 ? -11.479 -20.774 10.082  1.00   21.49 ? 101 ASP A OD2 1 
ATOM   794  N  N   . GLY A 1 102 ? -7.705  -19.904 14.066  1.00   15.51 ? 102 GLY A N   1 
ATOM   795  C  CA  . GLY A 1 102 ? -7.409  -19.932 15.511  1.00   14.79 ? 102 GLY A CA  1 
ATOM   796  C  C   . GLY A 1 102 ? -6.732  -18.690 16.134  1.00   14.43 ? 102 GLY A C   1 
ATOM   797  O  O   . GLY A 1 102 ? -6.494  -18.634 17.332  1.00   13.67 ? 102 GLY A O   1 
ATOM   798  N  N   . GLN A 1 103 ? -6.408  -17.682 15.332  1.00   13.08 ? 103 GLN A N   1 
ATOM   799  C  CA  . GLN A 1 103 ? -5.766  -16.496 15.861  1.00   13.30 ? 103 GLN A CA  1 
ATOM   800  C  C   . GLN A 1 103 ? -6.095  -15.299 14.983  1.00   13.47 ? 103 GLN A C   1 
ATOM   801  O  O   . GLN A 1 103 ? -6.661  -15.467 13.944  1.00   13.57 ? 103 GLN A O   1 
ATOM   802  C  CB  . GLN A 1 103 ? -4.246  -16.664 15.895  1.00   13.86 ? 103 GLN A CB  1 
ATOM   803  C  CG  . GLN A 1 103 ? -3.599  -16.955 14.523  1.00   16.05 ? 103 GLN A CG  1 
ATOM   804  C  CD  . GLN A 1 103 ? -2.147  -17.436 14.642  1.00   20.13 ? 103 GLN A CD  1 
ATOM   805  O  OE1 . GLN A 1 103 ? -1.249  -16.915 13.979  1.00   20.46 ? 103 GLN A OE1 1 
ATOM   806  N  NE2 . GLN A 1 103 ? -1.915  -18.396 15.530  1.00   19.22 ? 103 GLN A NE2 1 
ATOM   807  N  N   . GLY A 1 104 ? -5.657  -14.104 15.376  1.00   12.53 ? 104 GLY A N   1 
ATOM   808  C  CA  . GLY A 1 104 ? -5.996  -12.935 14.608  1.00   11.17 ? 104 GLY A CA  1 
ATOM   809  C  C   . GLY A 1 104 ? -6.396  -11.746 15.505  1.00   11.74 ? 104 GLY A C   1 
ATOM   810  O  O   . GLY A 1 104 ? -6.062  -10.583 15.160  1.00   11.33 ? 104 GLY A O   1 
ATOM   811  N  N   . SER A 1 105 ? -7.124  -12.008 16.603  1.00   10.73 ? 105 SER A N   1 
ATOM   812  C  CA  . SER A 1 105 ? -7.511  -10.909 17.499  1.00   10.72 ? 105 SER A CA  1 
ATOM   813  C  C   . SER A 1 105 ? -6.302  -10.324 18.265  1.00   10.38 ? 105 SER A C   1 
ATOM   814  O  O   . SER A 1 105 ? -5.263  -10.981 18.510  1.00   10.70 ? 105 SER A O   1 
ATOM   815  C  CB  . SER A 1 105 ? -8.632  -11.239 18.472  1.00   10.45 ? 105 SER A CB  1 
ATOM   816  O  OG  . SER A 1 105 ? -8.204  -12.204 19.424  1.00   10.53 ? 105 SER A OG  1 
ATOM   817  N  N   . GLU A 1 106 ? -6.440  -9.062  18.637  1.00   9.70  ? 106 GLU A N   1 
ATOM   818  C  CA  . GLU A 1 106 ? -5.391  -8.414  19.432  1.00   9.56  ? 106 GLU A CA  1 
ATOM   819  C  C   . GLU A 1 106 ? -5.716  -8.610  20.924  1.00   9.60  ? 106 GLU A C   1 
ATOM   820  O  O   . GLU A 1 106 ? -4.895  -9.171  21.685  1.00   10.16 ? 106 GLU A O   1 
ATOM   821  C  CB  . GLU A 1 106 ? -5.324  -6.920  19.017  1.00   8.99  ? 106 GLU A CB  1 
ATOM   822  C  CG  . GLU A 1 106 ? -4.931  -6.782  17.567  1.00   8.49  ? 106 GLU A CG  1 
ATOM   823  C  CD  . GLU A 1 106 ? -4.178  -5.485  17.295  1.00   9.59  ? 106 GLU A CD  1 
ATOM   824  O  OE1 . GLU A 1 106 ? -4.774  -4.406  17.514  1.00   9.83  ? 106 GLU A OE1 1 
ATOM   825  O  OE2 . GLU A 1 106 ? -2.976  -5.531  16.923  1.00   9.58  ? 106 GLU A OE2 1 
ATOM   826  N  N   . HIS A 1 107 ? -6.914  -8.168  21.354  1.00   9.48  ? 107 HIS A N   1 
ATOM   827  C  CA  . HIS A 1 107 ? -7.396  -8.518  22.663  1.00   9.49  ? 107 HIS A CA  1 
ATOM   828  C  C   . HIS A 1 107 ? -7.740  -9.963  22.684  1.00   10.67 ? 107 HIS A C   1 
ATOM   829  O  O   . HIS A 1 107 ? -8.036  -10.589 21.625  1.00   11.13 ? 107 HIS A O   1 
ATOM   830  C  CB  . HIS A 1 107 ? -8.632  -7.707  23.014  1.00   9.24  ? 107 HIS A CB  1 
ATOM   831  C  CG  . HIS A 1 107 ? -8.318  -6.232  23.184  1.00   9.03  ? 107 HIS A CG  1 
ATOM   832  N  ND1 . HIS A 1 107 ? -8.300  -5.391  22.150  1.00   9.22  ? 107 HIS A ND1 1 
ATOM   833  C  CD2 . HIS A 1 107 ? -7.913  -5.510  24.296  1.00   8.78  ? 107 HIS A CD2 1 
ATOM   834  C  CE1 . HIS A 1 107 ? -7.971  -4.150  22.585  1.00   9.36  ? 107 HIS A CE1 1 
ATOM   835  N  NE2 . HIS A 1 107 ? -7.719  -4.244  23.906  1.00   9.47  ? 107 HIS A NE2 1 
ATOM   836  N  N   . THR A 1 108 ? -7.588  -10.539 23.861  1.00   11.62 ? 108 THR A N   1 
ATOM   837  C  CA  . THR A 1 108 ? -7.970  -11.962 24.091  1.00   12.46 ? 108 THR A CA  1 
ATOM   838  C  C   . THR A 1 108 ? -8.937  -11.987 25.267  1.00   13.39 ? 108 THR A C   1 
ATOM   839  O  O   . THR A 1 108 ? -8.978  -11.030 26.084  1.00   14.21 ? 108 THR A O   1 
ATOM   840  C  CB  . THR A 1 108 ? -6.726  -12.857 24.362  1.00   12.37 ? 108 THR A CB  1 
ATOM   841  O  OG1 . THR A 1 108 ? -5.928  -12.321 25.423  1.00   11.22 ? 108 THR A OG1 1 
ATOM   842  C  CG2 . THR A 1 108 ? -5.862  -13.004 23.056  1.00   11.06 ? 108 THR A CG2 1 
ATOM   843  N  N   . VAL A 1 109 ? -9.725  -13.047 25.401  1.00   14.16 ? 109 VAL A N   1 
ATOM   844  C  CA  . VAL A 1 109 ? -10.679 -13.120 26.513  1.00   15.44 ? 109 VAL A CA  1 
ATOM   845  C  C   . VAL A 1 109 ? -10.423 -14.433 27.246  1.00   16.85 ? 109 VAL A C   1 
ATOM   846  O  O   . VAL A 1 109 ? -10.570 -15.511 26.646  1.00   16.01 ? 109 VAL A O   1 
ATOM   847  C  CB  . VAL A 1 109 ? -12.122 -13.119 25.995  1.00   17.87 ? 109 VAL A CB  1 
ATOM   848  C  CG1 . VAL A 1 109 ? -13.060 -13.255 27.188  1.00   17.89 ? 109 VAL A CG1 1 
ATOM   849  C  CG2 . VAL A 1 109 ? -12.403 -11.835 25.167  1.00   15.01 ? 109 VAL A CG2 1 
ATOM   850  N  N   . ASP A 1 110 ? -9.987  -14.346 28.495  1.00   14.66 ? 110 ASP A N   1 
ATOM   851  C  CA  . ASP A 1 110 ? -9.493  -15.542 29.166  1.00   17.19 ? 110 ASP A CA  1 
ATOM   852  C  C   . ASP A 1 110 ? -8.488  -16.316 28.323  1.00   16.54 ? 110 ASP A C   1 
ATOM   853  O  O   . ASP A 1 110 ? -8.585  -17.529 28.237  1.00   15.20 ? 110 ASP A O   1 
ATOM   854  C  CB  . ASP A 1 110 ? -10.722 -16.393 29.625  1.00   16.22 ? 110 ASP A CB  1 
ATOM   855  C  CG  . ASP A 1 110 ? -11.550 -15.650 30.637  1.00   17.00 ? 110 ASP A CG  1 
ATOM   856  O  OD1 . ASP A 1 110 ? -10.919 -14.843 31.332  1.00   15.19 ? 110 ASP A OD1 1 
ATOM   857  O  OD2 . ASP A 1 110 ? -12.817 -15.782 30.673  1.00   17.53 ? 110 ASP A OD2 1 
ATOM   858  N  N   . LYS A 1 111 ? -7.524  -15.603 27.698  1.00   16.11 ? 111 LYS A N   1 
ATOM   859  C  CA  . LYS A 1 111 ? -6.494  -16.152 26.819  1.00   18.45 ? 111 LYS A CA  1 
ATOM   860  C  C   . LYS A 1 111 ? -6.981  -16.716 25.472  1.00   16.53 ? 111 LYS A C   1 
ATOM   861  O  O   . LYS A 1 111 ? -6.153  -17.099 24.677  1.00   16.76 ? 111 LYS A O   1 
ATOM   862  C  CB  . LYS A 1 111 ? -5.611  -17.239 27.511  1.00   21.09 ? 111 LYS A CB  1 
ATOM   863  C  CG  . LYS A 1 111 ? -4.917  -16.773 28.785  1.00   24.67 ? 111 LYS A CG  1 
ATOM   864  C  CD  . LYS A 1 111 ? -3.880  -15.737 28.434  1.00   26.81 ? 111 LYS A CD  1 
ATOM   865  C  CE  . LYS A 1 111 ? -3.560  -14.883 29.657  1.00   31.64 ? 111 LYS A CE  1 
ATOM   866  N  NZ  . LYS A 1 111 ? -2.411  -15.456 30.397  1.00   32.76 ? 111 LYS A NZ  1 
ATOM   867  N  N   . LYS A 1 112 ? -8.278  -16.679 25.214  1.00   15.28 ? 112 LYS A N   1 
ATOM   868  C  CA  . LYS A 1 112 ? -8.796  -17.115 23.958  1.00   17.22 ? 112 LYS A CA  1 
ATOM   869  C  C   . LYS A 1 112 ? -8.576  -16.054 22.872  1.00   17.27 ? 112 LYS A C   1 
ATOM   870  O  O   . LYS A 1 112 ? -8.920  -14.854 23.084  1.00   15.58 ? 112 LYS A O   1 
ATOM   871  C  CB  . LYS A 1 112 ? -10.293 -17.408 24.084  1.00   19.64 ? 112 LYS A CB  1 
ATOM   872  C  CG  . LYS A 1 112 ? -10.869 -17.864 22.781  1.00   21.24 ? 112 LYS A CG  1 
ATOM   873  C  CD  . LYS A 1 112 ? -12.372 -17.714 22.649  1.00   29.03 ? 112 LYS A CD  1 
ATOM   874  C  CE  . LYS A 1 112 ? -12.741 -18.176 21.225  1.00   28.71 ? 112 LYS A CE  1 
ATOM   875  N  NZ  . LYS A 1 112 ? -14.192 -18.547 21.061  1.00   30.25 ? 112 LYS A NZ  1 
ATOM   876  N  N   . LYS A 1 113 ? -7.978  -16.497 21.754  1.00   14.69 ? 113 LYS A N   1 
ATOM   877  C  CA  . LYS A 1 113 ? -7.915  -15.691 20.488  1.00   15.57 ? 113 LYS A CA  1 
ATOM   878  C  C   . LYS A 1 113 ? -9.091  -15.912 19.533  1.00   14.70 ? 113 LYS A C   1 
ATOM   879  O  O   . LYS A 1 113 ? -9.590  -17.047 19.370  1.00   14.34 ? 113 LYS A O   1 
ATOM   880  C  CB  . LYS A 1 113 ? -6.616  -15.913 19.710  1.00   14.72 ? 113 LYS A CB  1 
ATOM   881  C  CG  . LYS A 1 113 ? -5.384  -15.647 20.527  1.00   15.03 ? 113 LYS A CG  1 
ATOM   882  C  CD  . LYS A 1 113 ? -4.171  -16.307 19.885  1.00   16.19 ? 113 LYS A CD  1 
ATOM   883  C  CE  . LYS A 1 113 ? -2.857  -15.617 20.219  1.00   17.19 ? 113 LYS A CE  1 
ATOM   884  N  NZ  . LYS A 1 113 ? -2.118  -16.422 21.212  1.00   18.45 ? 113 LYS A NZ  1 
ATOM   885  N  N   . TYR A 1 114 ? -9.524  -14.819 18.907  1.00   13.44 ? 114 TYR A N   1 
ATOM   886  C  CA  . TYR A 1 114 ? -10.598 -14.841 17.957  1.00   12.93 ? 114 TYR A CA  1 
ATOM   887  C  C   . TYR A 1 114 ? -9.944  -14.766 16.586  1.00   12.88 ? 114 TYR A C   1 
ATOM   888  O  O   . TYR A 1 114 ? -8.733  -14.529 16.491  1.00   12.88 ? 114 TYR A O   1 
ATOM   889  C  CB  . TYR A 1 114 ? -11.581 -13.685 18.238  1.00   12.93 ? 114 TYR A CB  1 
ATOM   890  C  CG  . TYR A 1 114 ? -12.540 -14.007 19.343  1.00   14.31 ? 114 TYR A CG  1 
ATOM   891  C  CD1 . TYR A 1 114 ? -12.241 -13.703 20.645  1.00   16.37 ? 114 TYR A CD1 1 
ATOM   892  C  CD2 . TYR A 1 114 ? -13.763 -14.644 19.087  1.00   15.91 ? 114 TYR A CD2 1 
ATOM   893  C  CE1 . TYR A 1 114 ? -13.130 -13.985 21.694  1.00   17.22 ? 114 TYR A CE1 1 
ATOM   894  C  CE2 . TYR A 1 114 ? -14.640 -14.943 20.119  1.00   17.19 ? 114 TYR A CE2 1 
ATOM   895  C  CZ  . TYR A 1 114 ? -14.310 -14.599 21.416  1.00   18.55 ? 114 TYR A CZ  1 
ATOM   896  O  OH  . TYR A 1 114 ? -15.163 -14.838 22.455  1.00   20.71 ? 114 TYR A OH  1 
ATOM   897  N  N   . ALA A 1 115 ? -10.689 -15.079 15.546  1.00   12.43 ? 115 ALA A N   1 
ATOM   898  C  CA  . ALA A 1 115 ? -10.118 -15.082 14.187  1.00   12.75 ? 115 ALA A CA  1 
ATOM   899  C  C   . ALA A 1 115 ? -9.792  -13.684 13.710  1.00   11.80 ? 115 ALA A C   1 
ATOM   900  O  O   . ALA A 1 115 ? -9.007  -13.512 12.779  1.00   12.98 ? 115 ALA A O   1 
ATOM   901  C  CB  . ALA A 1 115 ? -11.089 -15.712 13.208  1.00   13.37 ? 115 ALA A CB  1 
ATOM   902  N  N   . ALA A 1 116 ? -10.465 -12.674 14.279  1.00   11.36 ? 116 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 116 ? -10.180 -11.333 13.845  1.00   10.13 ? 116 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 116 ? -10.729 -10.361 14.901  1.00   9.36  ? 116 ALA A C   1 
ATOM   905  O  O   . ALA A 1 116 ? -11.388 -10.792 15.863  1.00   9.26  ? 116 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 116 ? -10.771 -11.032 12.447  1.00   9.51  ? 116 ALA A CB  1 
ATOM   907  N  N   . GLU A 1 117 ? -10.344 -9.076  14.769  1.00   9.12  ? 117 GLU A N   1 
ATOM   908  C  CA  . GLU A 1 117 ? -10.834 -8.059  15.661  1.00   8.89  ? 117 GLU A CA  1 
ATOM   909  C  C   . GLU A 1 117 ? -11.110 -6.779  14.842  1.00   8.92  ? 117 GLU A C   1 
ATOM   910  O  O   . GLU A 1 117 ? -10.243 -6.317  14.156  1.00   10.28 ? 117 GLU A O   1 
ATOM   911  C  CB  . GLU A 1 117 ? -9.848  -7.807  16.788  1.00   9.37  ? 117 GLU A CB  1 
ATOM   912  C  CG  . GLU A 1 117 ? -10.393 -6.849  17.856  1.00   8.93  ? 117 GLU A CG  1 
ATOM   913  C  CD  . GLU A 1 117 ? -9.492  -6.833  19.066  1.00   9.32  ? 117 GLU A CD  1 
ATOM   914  O  OE1 . GLU A 1 117 ? -8.906  -7.866  19.338  1.00   8.61  ? 117 GLU A OE1 1 
ATOM   915  O  OE2 . GLU A 1 117 ? -9.369  -5.767  19.730  1.00   9.36  ? 117 GLU A OE2 1 
ATOM   916  N  N   . LEU A 1 118 ? -12.307 -6.230  14.942  1.00   8.78  ? 118 LEU A N   1 
ATOM   917  C  CA  . LEU A 1 118 ? -12.666 -4.925  14.296  1.00   8.28  ? 118 LEU A CA  1 
ATOM   918  C  C   . LEU A 1 118 ? -12.393 -3.763  15.266  1.00   8.66  ? 118 LEU A C   1 
ATOM   919  O  O   . LEU A 1 118 ? -12.743 -3.857  16.421  1.00   9.40  ? 118 LEU A O   1 
ATOM   920  C  CB  . LEU A 1 118 ? -14.151 -4.957  13.948  1.00   7.82  ? 118 LEU A CB  1 
ATOM   921  C  CG  . LEU A 1 118 ? -14.891 -3.632  13.546  1.00   8.53  ? 118 LEU A CG  1 
ATOM   922  C  CD1 . LEU A 1 118 ? -14.337 -3.118  12.229  1.00   8.16  ? 118 LEU A CD1 1 
ATOM   923  C  CD2 . LEU A 1 118 ? -16.334 -4.074  13.405  1.00   8.31  ? 118 LEU A CD2 1 
ATOM   924  N  N   . HIS A 1 119 ? -11.838 -2.656  14.773  1.00   8.67  ? 119 HIS A N   1 
ATOM   925  C  CA  . HIS A 1 119 ? -11.598 -1.474  15.574  1.00   8.92  ? 119 HIS A CA  1 
ATOM   926  C  C   . HIS A 1 119 ? -12.272 -0.301  14.914  1.00   8.59  ? 119 HIS A C   1 
ATOM   927  O  O   . HIS A 1 119 ? -11.953 -0.010  13.750  1.00   8.44  ? 119 HIS A O   1 
ATOM   928  C  CB  . HIS A 1 119 ? -10.096 -1.234  15.639  1.00   8.06  ? 119 HIS A CB  1 
ATOM   929  C  CG  . HIS A 1 119 ? -9.374  -2.244  16.546  1.00   8.70  ? 119 HIS A CG  1 
ATOM   930  N  ND1 . HIS A 1 119 ? -8.012  -2.416  16.573  1.00   9.03  ? 119 HIS A ND1 1 
ATOM   931  C  CD2 . HIS A 1 119 ? -9.884  -3.098  17.518  1.00   8.45  ? 119 HIS A CD2 1 
ATOM   932  C  CE1 . HIS A 1 119 ? -7.691  -3.353  17.502  1.00   8.51  ? 119 HIS A CE1 1 
ATOM   933  N  NE2 . HIS A 1 119 ? -8.816  -3.794  18.053  1.00   8.36  ? 119 HIS A NE2 1 
ATOM   934  N  N   . LEU A 1 120 ? -13.281 0.262   15.579  1.00   8.85  ? 120 LEU A N   1 
ATOM   935  C  CA  . LEU A 1 120 ? -13.985 1.460   15.074  1.00   8.58  ? 120 LEU A CA  1 
ATOM   936  C  C   . LEU A 1 120 ? -13.369 2.606   15.855  1.00   8.80  ? 120 LEU A C   1 
ATOM   937  O  O   . LEU A 1 120 ? -13.511 2.661   17.078  1.00   8.42  ? 120 LEU A O   1 
ATOM   938  C  CB  . LEU A 1 120 ? -15.486 1.362   15.294  1.00   9.72  ? 120 LEU A CB  1 
ATOM   939  C  CG  . LEU A 1 120 ? -16.153 0.248   14.432  1.00   10.18 ? 120 LEU A CG  1 
ATOM   940  C  CD1 . LEU A 1 120 ? -16.905 -0.718  15.327  1.00   10.41 ? 120 LEU A CD1 1 
ATOM   941  C  CD2 . LEU A 1 120 ? -17.044 0.901   13.360  1.00   10.23 ? 120 LEU A CD2 1 
ATOM   942  N  N   . VAL A 1 121 ? -12.621 3.447   15.160  1.00   9.56  ? 121 VAL A N   1 
ATOM   943  C  CA  . VAL A 1 121 ? -11.738 4.438   15.832  1.00   10.20 ? 121 VAL A CA  1 
ATOM   944  C  C   . VAL A 1 121 ? -12.478 5.763   15.864  1.00   10.60 ? 121 VAL A C   1 
ATOM   945  O  O   . VAL A 1 121 ? -12.929 6.223   14.798  1.00   11.50 ? 121 VAL A O   1 
ATOM   946  C  CB  . VAL A 1 121 ? -10.409 4.626   15.041  1.00   10.91 ? 121 VAL A CB  1 
ATOM   947  C  CG1 . VAL A 1 121 ? -9.437  5.623   15.714  1.00   10.23 ? 121 VAL A CG1 1 
ATOM   948  C  CG2 . VAL A 1 121 ? -9.718  3.290   14.784  1.00   9.95  ? 121 VAL A CG2 1 
ATOM   949  N  N   . HIS A 1 122 ? -12.549 6.408   17.040  1.00   9.43  ? 122 HIS A N   1 
ATOM   950  C  CA  . HIS A 1 122 ? -13.280 7.666   17.190  1.00   9.83  ? 122 HIS A CA  1 
ATOM   951  C  C   . HIS A 1 122 ? -12.403 8.655   17.967  1.00   10.74 ? 122 HIS A C   1 
ATOM   952  O  O   . HIS A 1 122 ? -11.636 8.245   18.811  1.00   10.47 ? 122 HIS A O   1 
ATOM   953  C  CB  . HIS A 1 122 ? -14.603 7.499   17.961  1.00   10.04 ? 122 HIS A CB  1 
ATOM   954  C  CG  . HIS A 1 122 ? -15.480 6.307   17.557  1.00   9.76  ? 122 HIS A CG  1 
ATOM   955  N  ND1 . HIS A 1 122 ? -15.156 5.029   17.831  1.00   9.72  ? 122 HIS A ND1 1 
ATOM   956  C  CD2 . HIS A 1 122 ? -16.752 6.271   16.980  1.00   10.67 ? 122 HIS A CD2 1 
ATOM   957  C  CE1 . HIS A 1 122 ? -16.137 4.211   17.404  1.00   10.41 ? 122 HIS A CE1 1 
ATOM   958  N  NE2 . HIS A 1 122 ? -17.118 4.975   16.883  1.00   10.12 ? 122 HIS A NE2 1 
ATOM   959  N  N   . TRP A 1 123 ? -12.478 9.952   17.641  1.00   11.28 ? 123 TRP A N   1 
ATOM   960  C  CA  . TRP A 1 123 ? -11.692 10.982  18.337  1.00   12.00 ? 123 TRP A CA  1 
ATOM   961  C  C   . TRP A 1 123 ? -12.546 12.047  19.033  1.00   12.17 ? 123 TRP A C   1 
ATOM   962  O  O   . TRP A 1 123 ? -13.668 12.381  18.602  1.00   10.54 ? 123 TRP A O   1 
ATOM   963  C  CB  . TRP A 1 123 ? -10.644 11.587  17.426  1.00   13.14 ? 123 TRP A CB  1 
ATOM   964  C  CG  . TRP A 1 123 ? -11.195 12.224  16.177  1.00   14.08 ? 123 TRP A CG  1 
ATOM   965  C  CD1 . TRP A 1 123 ? -11.401 11.612  14.927  1.00   14.81 ? 123 TRP A CD1 1 
ATOM   966  C  CD2 . TRP A 1 123 ? -11.682 13.600  16.028  1.00   14.84 ? 123 TRP A CD2 1 
ATOM   967  N  NE1 . TRP A 1 123 ? -11.949 12.517  14.031  1.00   15.85 ? 123 TRP A NE1 1 
ATOM   968  C  CE2 . TRP A 1 123 ? -12.140 13.731  14.646  1.00   15.39 ? 123 TRP A CE2 1 
ATOM   969  C  CE3 . TRP A 1 123 ? -11.786 14.697  16.885  1.00   15.64 ? 123 TRP A CE3 1 
ATOM   970  C  CZ2 . TRP A 1 123 ? -12.656 14.928  14.148  1.00   15.79 ? 123 TRP A CZ2 1 
ATOM   971  C  CZ3 . TRP A 1 123 ? -12.315 15.892  16.377  1.00   16.54 ? 123 TRP A CZ3 1 
ATOM   972  C  CH2 . TRP A 1 123 ? -12.727 16.005  15.039  1.00   16.49 ? 123 TRP A CH2 1 
ATOM   973  N  N   . ASN A 1 124 ? -12.031 12.501  20.169  1.00   11.96 ? 124 ASN A N   1 
ATOM   974  C  CA  . ASN A 1 124 ? -12.774 13.345  21.107  1.00   13.10 ? 124 ASN A CA  1 
ATOM   975  C  C   . ASN A 1 124 ? -12.964 14.749  20.460  1.00   13.08 ? 124 ASN A C   1 
ATOM   976  O  O   . ASN A 1 124 ? -11.984 15.395  20.066  1.00   13.34 ? 124 ASN A O   1 
ATOM   977  C  CB  . ASN A 1 124 ? -11.965 13.401  22.401  1.00   13.49 ? 124 ASN A CB  1 
ATOM   978  C  CG  . ASN A 1 124 ? -12.738 13.978  23.536  1.00   14.04 ? 124 ASN A CG  1 
ATOM   979  O  OD1 . ASN A 1 124 ? -13.410 14.962  23.347  1.00   14.81 ? 124 ASN A OD1 1 
ATOM   980  N  ND2 . ASN A 1 124 ? -12.629 13.374  24.739  1.00   13.88 ? 124 ASN A ND2 1 
ATOM   981  N  N   . THR A 1 125 ? -14.221 15.138  20.229  1.00   13.92 ? 125 THR A N   1 
ATOM   982  C  CA  . THR A 1 125 ? -14.532 16.334  19.432  1.00   16.35 ? 125 THR A CA  1 
ATOM   983  C  C   . THR A 1 125 ? -13.907 17.566  20.059  1.00   16.69 ? 125 THR A C   1 
ATOM   984  O  O   . THR A 1 125 ? -13.783 18.607  19.412  1.00   16.50 ? 125 THR A O   1 
ATOM   985  C  CB  . THR A 1 125 ? -16.054 16.590  19.292  1.00   17.54 ? 125 THR A CB  1 
ATOM   986  O  OG1 . THR A 1 125 ? -16.650 16.484  20.576  1.00   18.68 ? 125 THR A OG1 1 
ATOM   987  C  CG2 . THR A 1 125 ? -16.755 15.491  18.357  1.00   17.88 ? 125 THR A CG2 1 
ATOM   988  N  N   . LYS A 1 126 ? -13.522 17.452  21.324  1.00   17.63 ? 127 LYS A N   1 
ATOM   989  C  CA  . LYS A 1 126 ? -12.975 18.603  22.027  1.00   20.62 ? 127 LYS A CA  1 
ATOM   990  C  C   . LYS A 1 126 ? -11.559 18.977  21.584  1.00   19.71 ? 127 LYS A C   1 
ATOM   991  O  O   . LYS A 1 126 ? -11.119 20.095  21.853  1.00   20.38 ? 127 LYS A O   1 
ATOM   992  C  CB  . LYS A 1 126 ? -13.108 18.467  23.561  1.00   22.49 ? 127 LYS A CB  1 
ATOM   993  C  CG  . LYS A 1 126 ? -12.060 17.629  24.284  1.00   24.18 ? 127 LYS A CG  1 
ATOM   994  C  CD  . LYS A 1 126 ? -12.452 17.418  25.737  1.00   27.12 ? 127 LYS A CD  1 
ATOM   995  C  CE  . LYS A 1 126 ? -11.429 16.563  26.467  1.00   28.78 ? 127 LYS A CE  1 
ATOM   996  N  NZ  . LYS A 1 126 ? -11.424 16.832  27.931  1.00   33.13 ? 127 LYS A NZ  1 
ATOM   997  N  N   . TYR A 1 127 ? -10.863 18.068  20.908  1.00   17.19 ? 128 TYR A N   1 
ATOM   998  C  CA  . TYR A 1 127 ? -9.545  18.348  20.400  1.00   16.03 ? 128 TYR A CA  1 
ATOM   999  C  C   . TYR A 1 127 ? -9.528  18.742  18.931  1.00   17.01 ? 128 TYR A C   1 
ATOM   1000 O  O   . TYR A 1 127 ? -8.430  18.894  18.310  1.00   18.13 ? 128 TYR A O   1 
ATOM   1001 C  CB  . TYR A 1 127 ? -8.613  17.175  20.637  1.00   13.97 ? 128 TYR A CB  1 
ATOM   1002 C  CG  . TYR A 1 127 ? -8.480  16.913  22.084  1.00   15.40 ? 128 TYR A CG  1 
ATOM   1003 C  CD1 . TYR A 1 127 ? -8.024  17.927  22.969  1.00   14.76 ? 128 TYR A CD1 1 
ATOM   1004 C  CD2 . TYR A 1 127 ? -8.874  15.696  22.622  1.00   14.72 ? 128 TYR A CD2 1 
ATOM   1005 C  CE1 . TYR A 1 127 ? -7.915  17.658  24.337  1.00   15.01 ? 128 TYR A CE1 1 
ATOM   1006 C  CE2 . TYR A 1 127 ? -8.728  15.425  23.978  1.00   15.72 ? 128 TYR A CE2 1 
ATOM   1007 C  CZ  . TYR A 1 127 ? -8.285  16.445  24.835  1.00   14.57 ? 128 TYR A CZ  1 
ATOM   1008 O  OH  . TYR A 1 127 ? -8.177  16.182  26.188  1.00   15.30 ? 128 TYR A OH  1 
ATOM   1009 N  N   . GLY A 1 128 ? -10.716 18.857  18.347  1.00   15.83 ? 129 GLY A N   1 
ATOM   1010 C  CA  . GLY A 1 128 ? -10.785 19.414  16.993  1.00   17.49 ? 129 GLY A CA  1 
ATOM   1011 C  C   . GLY A 1 128 ? -10.354 18.524  15.817  1.00   17.86 ? 129 GLY A C   1 
ATOM   1012 O  O   . GLY A 1 128 ? -10.873 18.678  14.708  1.00   16.66 ? 129 GLY A O   1 
ATOM   1013 N  N   . ASP A 1 129 ? -9.358  17.671  15.983  1.00   17.55 ? 130 ASP A N   1 
ATOM   1014 C  CA  . ASP A 1 129 ? -9.087  16.721  14.896  1.00   18.57 ? 130 ASP A CA  1 
ATOM   1015 C  C   . ASP A 1 129 ? -8.332  15.510  15.410  1.00   18.32 ? 130 ASP A C   1 
ATOM   1016 O  O   . ASP A 1 129 ? -7.882  15.509  16.543  1.00   17.68 ? 130 ASP A O   1 
ATOM   1017 C  CB  . ASP A 1 129 ? -8.416  17.365  13.666  1.00   20.72 ? 130 ASP A CB  1 
ATOM   1018 C  CG  . ASP A 1 129 ? -7.030  17.857  13.933  1.00   23.05 ? 130 ASP A CG  1 
ATOM   1019 O  OD1 . ASP A 1 129 ? -6.378  17.510  14.929  1.00   27.34 ? 130 ASP A OD1 1 
ATOM   1020 O  OD2 . ASP A 1 129 ? -6.539  18.609  13.101  1.00   25.93 ? 130 ASP A OD2 1 
ATOM   1021 N  N   . PHE A 1 130 ? -8.191  14.502  14.554  1.00   17.03 ? 131 PHE A N   1 
ATOM   1022 C  CA  . PHE A 1 130 ? -7.587  13.248  14.931  1.00   17.60 ? 131 PHE A CA  1 
ATOM   1023 C  C   . PHE A 1 130 ? -6.119  13.438  15.364  1.00   17.14 ? 131 PHE A C   1 
ATOM   1024 O  O   . PHE A 1 130 ? -5.693  12.849  16.351  1.00   14.37 ? 131 PHE A O   1 
ATOM   1025 C  CB  . PHE A 1 130 ? -7.721  12.231  13.780  1.00   15.42 ? 131 PHE A CB  1 
ATOM   1026 C  CG  . PHE A 1 130 ? -7.037  10.946  14.056  1.00   19.28 ? 131 PHE A CG  1 
ATOM   1027 C  CD1 . PHE A 1 130 ? -7.687  9.912   14.788  1.00   18.82 ? 131 PHE A CD1 1 
ATOM   1028 C  CD2 . PHE A 1 130 ? -5.726  10.743  13.662  1.00   20.13 ? 131 PHE A CD2 1 
ATOM   1029 C  CE1 . PHE A 1 130 ? -7.036  8.716   15.073  1.00   20.03 ? 131 PHE A CE1 1 
ATOM   1030 C  CE2 . PHE A 1 130 ? -5.082  9.551   13.958  1.00   23.31 ? 131 PHE A CE2 1 
ATOM   1031 C  CZ  . PHE A 1 130 ? -5.738  8.539   14.672  1.00   23.45 ? 131 PHE A CZ  1 
ATOM   1032 N  N   . GLY A 1 131 ? -5.365  14.266  14.615  1.00   16.67 ? 132 GLY A N   1 
ATOM   1033 C  CA  . GLY A 1 131 ? -3.928  14.462  14.881  1.00   16.96 ? 132 GLY A CA  1 
ATOM   1034 C  C   . GLY A 1 131 ? -3.684  15.062  16.255  1.00   16.46 ? 132 GLY A C   1 
ATOM   1035 O  O   . GLY A 1 131 ? -2.739  14.678  16.937  1.00   16.07 ? 132 GLY A O   1 
ATOM   1036 N  N   . LYS A 1 132 ? -4.504  16.030  16.647  1.00   16.05 ? 133 LYS A N   1 
ATOM   1037 C  CA  . LYS A 1 132 ? -4.415  16.598  18.000  1.00   16.83 ? 133 LYS A CA  1 
ATOM   1038 C  C   . LYS A 1 132 ? -4.911  15.633  19.092  1.00   16.01 ? 133 LYS A C   1 
ATOM   1039 O  O   . LYS A 1 132 ? -4.316  15.536  20.150  1.00   13.00 ? 133 LYS A O   1 
ATOM   1040 C  CB  . LYS A 1 132 ? -5.248  17.868  18.099  1.00   21.55 ? 133 LYS A CB  1 
ATOM   1041 C  CG  . LYS A 1 132 ? -4.733  19.039  17.299  1.00   26.74 ? 133 LYS A CG  1 
ATOM   1042 C  CD  . LYS A 1 132 ? -3.433  19.584  17.860  1.00   32.95 ? 133 LYS A CD  1 
ATOM   1043 C  CE  . LYS A 1 132 ? -3.684  20.322  19.167  1.00   35.62 ? 133 LYS A CE  1 
ATOM   1044 N  NZ  . LYS A 1 132 ? -2.513  21.203  19.486  1.00   42.98 ? 133 LYS A NZ  1 
ATOM   1045 N  N   . ALA A 1 133 ? -6.044  14.975  18.856  1.00   13.80 ? 134 ALA A N   1 
ATOM   1046 C  CA  . ALA A 1 133 ? -6.568  13.992  19.813  1.00   14.90 ? 134 ALA A CA  1 
ATOM   1047 C  C   . ALA A 1 133 ? -5.539  12.885  20.231  1.00   13.73 ? 134 ALA A C   1 
ATOM   1048 O  O   . ALA A 1 133 ? -5.525  12.463  21.417  1.00   13.99 ? 134 ALA A O   1 
ATOM   1049 C  CB  . ALA A 1 133 ? -7.863  13.366  19.238  1.00   13.76 ? 134 ALA A CB  1 
ATOM   1050 N  N   . VAL A 1 134 ? -4.705  12.394  19.298  1.00   13.61 ? 135 VAL A N   1 
ATOM   1051 C  CA  . VAL A 1 134 ? -3.784  11.279  19.635  1.00   14.54 ? 135 VAL A CA  1 
ATOM   1052 C  C   . VAL A 1 134 ? -2.675  11.725  20.552  1.00   16.93 ? 135 VAL A C   1 
ATOM   1053 O  O   . VAL A 1 134 ? -1.961  10.881  21.137  1.00   15.47 ? 135 VAL A O   1 
ATOM   1054 C  CB  . VAL A 1 134 ? -3.181  10.489  18.416  1.00   14.77 ? 135 VAL A CB  1 
ATOM   1055 C  CG1 . VAL A 1 134 ? -4.307  9.889   17.598  1.00   15.24 ? 135 VAL A CG1 1 
ATOM   1056 C  CG2 . VAL A 1 134 ? -2.368  11.407  17.524  1.00   14.00 ? 135 VAL A CG2 1 
ATOM   1057 N  N   . GLN A 1 135 ? -2.544  13.050  20.705  1.00   17.97 ? 136 GLN A N   1 
ATOM   1058 C  CA  . GLN A 1 135 ? -1.536  13.564  21.587  1.00   20.50 ? 136 GLN A CA  1 
ATOM   1059 C  C   . GLN A 1 135 ? -2.104  13.740  23.026  1.00   20.31 ? 136 GLN A C   1 
ATOM   1060 O  O   . GLN A 1 135 ? -1.443  14.326  23.892  1.00   21.70 ? 136 GLN A O   1 
ATOM   1061 C  CB  . GLN A 1 135 ? -0.971  14.917  21.020  1.00   24.40 ? 136 GLN A CB  1 
ATOM   1062 C  CG  . GLN A 1 135 ? -0.223  14.800  19.669  1.00   31.05 ? 136 GLN A CG  1 
ATOM   1063 C  CD  . GLN A 1 135 ? 1.006   13.844  19.695  1.00   40.48 ? 136 GLN A CD  1 
ATOM   1064 O  OE1 . GLN A 1 135 ? 1.634   13.612  20.757  1.00   44.35 ? 136 GLN A OE1 1 
ATOM   1065 N  NE2 . GLN A 1 135 ? 1.351   13.273  18.515  1.00   39.30 ? 136 GLN A NE2 1 
ATOM   1066 N  N   . GLN A 1 136 ? -3.323  13.271  23.270  1.00   16.82 ? 137 GLN A N   1 
ATOM   1067 C  CA  . GLN A 1 136 ? -4.015  13.471  24.556  1.00   15.72 ? 137 GLN A CA  1 
ATOM   1068 C  C   . GLN A 1 136 ? -4.401  12.162  25.218  1.00   14.44 ? 137 GLN A C   1 
ATOM   1069 O  O   . GLN A 1 136 ? -4.873  11.262  24.536  1.00   14.27 ? 137 GLN A O   1 
ATOM   1070 C  CB  . GLN A 1 136 ? -5.305  14.266  24.361  1.00   15.93 ? 137 GLN A CB  1 
ATOM   1071 C  CG  . GLN A 1 136 ? -5.145  15.521  23.466  1.00   19.24 ? 137 GLN A CG  1 
ATOM   1072 C  CD  . GLN A 1 136 ? -4.135  16.531  24.050  1.00   20.41 ? 137 GLN A CD  1 
ATOM   1073 O  OE1 . GLN A 1 136 ? -4.075  16.725  25.267  1.00   19.29 ? 137 GLN A OE1 1 
ATOM   1074 N  NE2 . GLN A 1 136 ? -3.345  17.178  23.158  1.00   23.43 ? 137 GLN A NE2 1 
ATOM   1075 N  N   . PRO A 1 137 ? -4.301  12.079  26.566  1.00   13.95 ? 138 PRO A N   1 
ATOM   1076 C  CA  . PRO A 1 137 ? -4.559  10.797  27.250  1.00   12.84 ? 138 PRO A CA  1 
ATOM   1077 C  C   . PRO A 1 137 ? -6.023  10.368  27.064  1.00   13.91 ? 138 PRO A C   1 
ATOM   1078 O  O   . PRO A 1 137 ? -6.351  9.168   27.213  1.00   13.94 ? 138 PRO A O   1 
ATOM   1079 C  CB  . PRO A 1 137 ? -4.202  11.080  28.716  1.00   13.73 ? 138 PRO A CB  1 
ATOM   1080 C  CG  . PRO A 1 137 ? -4.272  12.582  28.850  1.00   15.05 ? 138 PRO A CG  1 
ATOM   1081 C  CD  . PRO A 1 137 ? -4.039  13.210  27.492  1.00   14.68 ? 138 PRO A CD  1 
ATOM   1082 N  N   . ASP A 1 138 ? -6.911  11.312  26.735  1.00   12.69 ? 139 ASP A N   1 
ATOM   1083 C  CA  . ASP A 1 138 ? -8.322  10.960  26.468  1.00   14.16 ? 139 ASP A CA  1 
ATOM   1084 C  C   . ASP A 1 138 ? -8.752  11.309  25.036  1.00   12.76 ? 139 ASP A C   1 
ATOM   1085 O  O   . ASP A 1 138 ? -9.913  11.686  24.794  1.00   12.57 ? 139 ASP A O   1 
ATOM   1086 C  CB  . ASP A 1 138 ? -9.277  11.664  27.462  1.00   16.28 ? 139 ASP A CB  1 
ATOM   1087 C  CG  . ASP A 1 138 ? -9.158  13.166  27.418  1.00   18.13 ? 139 ASP A CG  1 
ATOM   1088 O  OD1 . ASP A 1 138 ? -8.186  13.704  26.794  1.00   19.38 ? 139 ASP A OD1 1 
ATOM   1089 O  OD2 . ASP A 1 138 ? -10.014 13.832  28.056  1.00   17.85 ? 139 ASP A OD2 1 
ATOM   1090 N  N   . GLY A 1 139 ? -7.830  11.177  24.087  1.00   13.21 ? 140 GLY A N   1 
ATOM   1091 C  CA  . GLY A 1 139 ? -8.086  11.668  22.753  1.00   11.53 ? 140 GLY A CA  1 
ATOM   1092 C  C   . GLY A 1 139 ? -8.961  10.746  21.923  1.00   11.53 ? 140 GLY A C   1 
ATOM   1093 O  O   . GLY A 1 139 ? -9.686  11.218  21.059  1.00   11.17 ? 140 GLY A O   1 
ATOM   1094 N  N   . LEU A 1 140 ? -8.848  9.429   22.134  1.00   11.19 ? 141 LEU A N   1 
ATOM   1095 C  CA  . LEU A 1 140 ? -9.515  8.448   21.276  1.00   10.47 ? 141 LEU A CA  1 
ATOM   1096 C  C   . LEU A 1 140 ? -10.425 7.511   22.084  1.00   11.54 ? 141 LEU A C   1 
ATOM   1097 O  O   . LEU A 1 140 ? -10.174 7.247   23.286  1.00   11.46 ? 141 LEU A O   1 
ATOM   1098 C  CB  . LEU A 1 140 ? -8.449  7.581   20.567  1.00   10.56 ? 141 LEU A CB  1 
ATOM   1099 C  CG  . LEU A 1 140 ? -7.523  8.222   19.484  1.00   11.35 ? 141 LEU A CG  1 
ATOM   1100 C  CD1 . LEU A 1 140 ? -6.824  7.193   18.580  1.00   11.40 ? 141 LEU A CD1 1 
ATOM   1101 C  CD2 . LEU A 1 140 ? -8.243  9.327   18.627  1.00   11.09 ? 141 LEU A CD2 1 
ATOM   1102 N  N   . ALA A 1 141 ? -11.471 6.985   21.432  1.00   10.99 ? 142 ALA A N   1 
ATOM   1103 C  CA  . ALA A 1 141 ? -12.266 5.904   22.019  1.00   10.01 ? 142 ALA A CA  1 
ATOM   1104 C  C   . ALA A 1 141 ? -12.331 4.867   20.924  1.00   10.85 ? 142 ALA A C   1 
ATOM   1105 O  O   . ALA A 1 141 ? -12.737 5.211   19.802  1.00   10.47 ? 142 ALA A O   1 
ATOM   1106 C  CB  . ALA A 1 141 ? -13.676 6.366   22.329  1.00   10.33 ? 142 ALA A CB  1 
ATOM   1107 N  N   . VAL A 1 142 ? -11.864 3.648   21.198  1.00   9.84  ? 143 VAL A N   1 
ATOM   1108 C  CA  . VAL A 1 142 ? -11.897 2.674   20.114  1.00   9.92  ? 143 VAL A CA  1 
ATOM   1109 C  C   . VAL A 1 142 ? -12.866 1.561   20.540  1.00   9.94  ? 143 VAL A C   1 
ATOM   1110 O  O   . VAL A 1 142 ? -12.778 1.043   21.674  1.00   9.32  ? 143 VAL A O   1 
ATOM   1111 C  CB  . VAL A 1 142 ? -10.520 2.085   19.725  1.00   9.62  ? 143 VAL A CB  1 
ATOM   1112 C  CG1 . VAL A 1 142 ? -10.637 1.063   18.578  1.00   9.06  ? 143 VAL A CG1 1 
ATOM   1113 C  CG2 . VAL A 1 142 ? -9.528  3.159   19.337  1.00   10.21 ? 143 VAL A CG2 1 
ATOM   1114 N  N   . LEU A 1 143 ? -13.816 1.268   19.649  1.00   9.20  ? 144 LEU A N   1 
ATOM   1115 C  CA  . LEU A 1 143 ? -14.752 0.171   19.899  1.00   9.89  ? 144 LEU A CA  1 
ATOM   1116 C  C   . LEU A 1 143 ? -14.217 -1.090  19.230  1.00   10.20 ? 144 LEU A C   1 
ATOM   1117 O  O   . LEU A 1 143 ? -14.130 -1.131  18.024  1.00   10.12 ? 144 LEU A O   1 
ATOM   1118 C  CB  . LEU A 1 143 ? -16.168 0.572   19.433  1.00   10.36 ? 144 LEU A CB  1 
ATOM   1119 C  CG  . LEU A 1 143 ? -17.276 -0.456  19.547  1.00   10.63 ? 144 LEU A CG  1 
ATOM   1120 C  CD1 . LEU A 1 143 ? -17.529 -0.706  21.029  1.00   11.19 ? 144 LEU A CD1 1 
ATOM   1121 C  CD2 . LEU A 1 143 ? -18.513 0.063   18.853  1.00   10.51 ? 144 LEU A CD2 1 
ATOM   1122 N  N   . GLY A 1 144 ? -13.853 -2.100  20.035  1.00   9.58  ? 145 GLY A N   1 
ATOM   1123 C  CA  . GLY A 1 144 ? -13.258 -3.341  19.551  1.00   9.26  ? 145 GLY A CA  1 
ATOM   1124 C  C   . GLY A 1 144 ? -14.349 -4.418  19.509  1.00   9.83  ? 145 GLY A C   1 
ATOM   1125 O  O   . GLY A 1 144 ? -15.047 -4.642  20.506  1.00   10.55 ? 145 GLY A O   1 
ATOM   1126 N  N   . ILE A 1 145 ? -14.461 -5.145  18.401  1.00   9.70  ? 146 ILE A N   1 
ATOM   1127 C  CA  . ILE A 1 145 ? -15.476 -6.175  18.274  1.00   9.49  ? 146 ILE A CA  1 
ATOM   1128 C  C   . ILE A 1 145 ? -14.738 -7.451  17.741  1.00   10.02 ? 146 ILE A C   1 
ATOM   1129 O  O   . ILE A 1 145 ? -14.056 -7.430  16.738  1.00   9.55  ? 146 ILE A O   1 
ATOM   1130 C  CB  . ILE A 1 145 ? -16.586 -5.721  17.289  1.00   8.90  ? 146 ILE A CB  1 
ATOM   1131 C  CG1 . ILE A 1 145 ? -17.223 -4.425  17.768  1.00   9.24  ? 146 ILE A CG1 1 
ATOM   1132 C  CG2 . ILE A 1 145 ? -17.616 -6.839  17.058  1.00   9.34  ? 146 ILE A CG2 1 
ATOM   1133 C  CD1 . ILE A 1 145 ? -18.260 -3.814  16.841  1.00   9.72  ? 146 ILE A CD1 1 
ATOM   1134 N  N   . PHE A 1 146 ? -14.871 -8.556  18.438  1.00   10.35 ? 147 PHE A N   1 
ATOM   1135 C  CA  . PHE A 1 146 ? -14.262 -9.853  17.999  1.00   10.09 ? 147 PHE A CA  1 
ATOM   1136 C  C   . PHE A 1 146 ? -15.006 -10.469 16.852  1.00   10.32 ? 147 PHE A C   1 
ATOM   1137 O  O   . PHE A 1 146 ? -16.216 -10.323 16.746  1.00   10.31 ? 147 PHE A O   1 
ATOM   1138 C  CB  . PHE A 1 146 ? -14.312 -10.764 19.219  1.00   10.35 ? 147 PHE A CB  1 
ATOM   1139 C  CG  . PHE A 1 146 ? -13.452 -10.273 20.370  1.00   10.17 ? 147 PHE A CG  1 
ATOM   1140 C  CD1 . PHE A 1 146 ? -12.086 -10.181 20.212  1.00   10.86 ? 147 PHE A CD1 1 
ATOM   1141 C  CD2 . PHE A 1 146 ? -13.991 -9.991  21.613  1.00   10.86 ? 147 PHE A CD2 1 
ATOM   1142 C  CE1 . PHE A 1 146 ? -11.237 -9.777  21.259  1.00   10.18 ? 147 PHE A CE1 1 
ATOM   1143 C  CE2 . PHE A 1 146 ? -13.174 -9.582  22.668  1.00   10.95 ? 147 PHE A CE2 1 
ATOM   1144 C  CZ  . PHE A 1 146 ? -11.801 -9.497  22.496  1.00   10.81 ? 147 PHE A CZ  1 
ATOM   1145 N  N   . LEU A 1 147 ? -14.287 -11.067 15.912  1.00   10.77 ? 148 LEU A N   1 
ATOM   1146 C  CA  . LEU A 1 147 ? -14.899 -11.878 14.898  1.00   10.58 ? 148 LEU A CA  1 
ATOM   1147 C  C   . LEU A 1 147 ? -14.578 -13.335 15.196  1.00   11.43 ? 148 LEU A C   1 
ATOM   1148 O  O   . LEU A 1 147 ? -13.386 -13.668 15.341  1.00   11.01 ? 148 LEU A O   1 
ATOM   1149 C  CB  . LEU A 1 147 ? -14.356 -11.526 13.478  1.00   9.79  ? 148 LEU A CB  1 
ATOM   1150 C  CG  . LEU A 1 147 ? -14.969 -10.243 12.811  1.00   9.16  ? 148 LEU A CG  1 
ATOM   1151 C  CD1 . LEU A 1 147 ? -14.772 -8.983  13.670  1.00   9.35  ? 148 LEU A CD1 1 
ATOM   1152 C  CD2 . LEU A 1 147 ? -14.369 -9.959  11.436  1.00   10.03 ? 148 LEU A CD2 1 
ATOM   1153 N  N   . LYS A 1 148 ? -15.623 -14.176 15.202  1.00   12.85 ? 149 LYS A N   1 
ATOM   1154 C  CA  . LYS A 1 148 ? -15.454 -15.646 15.122  1.00   15.46 ? 149 LYS A CA  1 
ATOM   1155 C  C   . LYS A 1 148 ? -15.942 -16.186 13.756  1.00   15.46 ? 149 LYS A C   1 
ATOM   1156 O  O   . LYS A 1 148 ? -16.817 -15.614 13.110  1.00   14.19 ? 149 LYS A O   1 
ATOM   1157 C  CB  . LYS A 1 148 ? -16.141 -16.372 16.245  1.00   16.89 ? 149 LYS A CB  1 
ATOM   1158 C  CG  . LYS A 1 148 ? -17.660 -16.297 16.214  1.00   21.81 ? 149 LYS A CG  1 
ATOM   1159 C  CD  . LYS A 1 148 ? -18.281 -17.009 17.428  1.00   26.93 ? 149 LYS A CD  1 
ATOM   1160 C  CE  . LYS A 1 148 ? -19.807 -17.053 17.334  1.00   32.18 ? 149 LYS A CE  1 
ATOM   1161 N  NZ  . LYS A 1 148 ? -20.467 -17.852 18.430  1.00   39.01 ? 149 LYS A NZ  1 
ATOM   1162 N  N   . VAL A 1 149 ? -15.375 -17.312 13.344  1.00   15.73 ? 150 VAL A N   1 
ATOM   1163 C  CA  . VAL A 1 149 ? -15.747 -17.910 12.062  1.00   15.23 ? 150 VAL A CA  1 
ATOM   1164 C  C   . VAL A 1 149 ? -16.988 -18.825 12.280  1.00   15.25 ? 150 VAL A C   1 
ATOM   1165 O  O   . VAL A 1 149 ? -17.000 -19.726 13.193  1.00   14.20 ? 150 VAL A O   1 
ATOM   1166 C  CB  . VAL A 1 149 ? -14.584 -18.703 11.475  1.00   15.44 ? 150 VAL A CB  1 
ATOM   1167 C  CG1 . VAL A 1 149 ? -15.053 -19.455 10.223  1.00   14.51 ? 150 VAL A CG1 1 
ATOM   1168 C  CG2 . VAL A 1 149 ? -13.416 -17.732 11.168  1.00   16.09 ? 150 VAL A CG2 1 
ATOM   1169 N  N   . GLY A 1 150 ? -18.025 -18.560 11.491  1.00   13.18 ? 151 GLY A N   1 
ATOM   1170 C  CA  . GLY A 1 150 ? -19.256 -19.362 11.565  1.00   14.91 ? 151 GLY A CA  1 
ATOM   1171 C  C   . GLY A 1 150 ? -20.155 -18.997 10.417  1.00   14.22 ? 151 GLY A C   1 
ATOM   1172 O  O   . GLY A 1 150 ? -19.753 -19.053 9.245   1.00   15.04 ? 151 GLY A O   1 
ATOM   1173 N  N   . SER A 1 151 ? -21.351 -18.564 10.734  1.00   14.99 ? 152 SER A N   1 
ATOM   1174 C  CA  . SER A 1 151 ? -22.210 -18.007 9.653   1.00   17.94 ? 152 SER A CA  1 
ATOM   1175 C  C   . SER A 1 151 ? -21.627 -16.638 9.141   1.00   16.92 ? 152 SER A C   1 
ATOM   1176 O  O   . SER A 1 151 ? -20.898 -15.942 9.875   1.00   14.47 ? 152 SER A O   1 
ATOM   1177 C  CB  . SER A 1 151 ? -23.639 -17.849 10.129  1.00   19.54 ? 152 SER A CB  1 
ATOM   1178 O  OG  . SER A 1 151 ? -23.576 -16.905 11.181  1.00   24.25 ? 152 SER A OG  1 
ATOM   1179 N  N   . ALA A 1 152 ? -21.880 -16.313 7.877   1.00   15.31 ? 153 ALA A N   1 
ATOM   1180 C  CA  . ALA A 1 152 ? -21.499 -15.018 7.304   1.00   15.46 ? 153 ALA A CA  1 
ATOM   1181 C  C   . ALA A 1 152 ? -22.153 -13.831 8.018   1.00   15.77 ? 153 ALA A C   1 
ATOM   1182 O  O   . ALA A 1 152 ? -23.281 -13.945 8.552   1.00   17.67 ? 153 ALA A O   1 
ATOM   1183 C  CB  . ALA A 1 152 ? -21.856 -14.956 5.814   1.00   15.67 ? 153 ALA A CB  1 
ATOM   1184 N  N   . LYS A 1 153 ? -21.459 -12.694 8.005   1.00   14.83 ? 154 LYS A N   1 
ATOM   1185 C  CA  . LYS A 1 153 ? -22.025 -11.418 8.438   1.00   15.51 ? 154 LYS A CA  1 
ATOM   1186 C  C   . LYS A 1 153 ? -22.411 -10.635 7.144   1.00   15.29 ? 154 LYS A C   1 
ATOM   1187 O  O   . LYS A 1 153 ? -21.524 -10.209 6.373   1.00   13.92 ? 154 LYS A O   1 
ATOM   1188 C  CB  . LYS A 1 153 ? -20.964 -10.632 9.246   1.00   17.20 ? 154 LYS A CB  1 
ATOM   1189 C  CG  . LYS A 1 153 ? -21.554 -9.474  10.031  1.00   18.41 ? 154 LYS A CG  1 
ATOM   1190 C  CD  . LYS A 1 153 ? -22.612 -9.904  11.037  1.00   17.26 ? 154 LYS A CD  1 
ATOM   1191 C  CE  . LYS A 1 153 ? -22.732 -8.868  12.169  1.00   19.83 ? 154 LYS A CE  1 
ATOM   1192 N  NZ  . LYS A 1 153 ? -23.924 -9.150  13.032  1.00   19.48 ? 154 LYS A NZ  1 
ATOM   1193 N  N   . PRO A 1 154 ? -23.740 -10.551 6.827   1.00   16.61 ? 155 PRO A N   1 
ATOM   1194 C  CA  . PRO A 1 154 ? -24.116 -10.011 5.516   1.00   16.89 ? 155 PRO A CA  1 
ATOM   1195 C  C   . PRO A 1 154 ? -23.609 -8.591  5.418   1.00   17.00 ? 155 PRO A C   1 
ATOM   1196 O  O   . PRO A 1 154 ? -23.170 -8.205  4.362   1.00   17.91 ? 155 PRO A O   1 
ATOM   1197 C  CB  . PRO A 1 154 ? -25.651 -9.958  5.565   1.00   17.51 ? 155 PRO A CB  1 
ATOM   1198 C  CG  . PRO A 1 154 ? -26.023 -10.970 6.605   1.00   17.14 ? 155 PRO A CG  1 
ATOM   1199 C  CD  . PRO A 1 154 ? -24.925 -10.892 7.637   1.00   17.33 ? 155 PRO A CD  1 
ATOM   1200 N  N   . GLY A 1 155 ? -23.668 -7.868  6.543   1.00   16.33 ? 156 GLY A N   1 
ATOM   1201 C  CA  . GLY A 1 155 ? -23.231 -6.486  6.664   1.00   15.78 ? 156 GLY A CA  1 
ATOM   1202 C  C   . GLY A 1 155 ? -21.755 -6.210  6.400   1.00   16.51 ? 156 GLY A C   1 
ATOM   1203 O  O   . GLY A 1 155 ? -21.377 -5.057  6.187   1.00   17.41 ? 156 GLY A O   1 
ATOM   1204 N  N   . LEU A 1 156 ? -20.938 -7.270  6.376   1.00   14.41 ? 157 LEU A N   1 
ATOM   1205 C  CA  . LEU A 1 156 ? -19.531 -7.172  6.010   1.00   13.56 ? 157 LEU A CA  1 
ATOM   1206 C  C   . LEU A 1 156 ? -19.217 -7.398  4.550   1.00   13.32 ? 157 LEU A C   1 
ATOM   1207 O  O   . LEU A 1 156 ? -18.122 -7.161  4.107   1.00   12.28 ? 157 LEU A O   1 
ATOM   1208 C  CB  . LEU A 1 156 ? -18.741 -8.215  6.843   1.00   12.14 ? 157 LEU A CB  1 
ATOM   1209 C  CG  . LEU A 1 156 ? -17.220 -8.372  6.630   1.00   12.81 ? 157 LEU A CG  1 
ATOM   1210 C  CD1 . LEU A 1 156 ? -16.539 -7.053  7.015   1.00   12.05 ? 157 LEU A CD1 1 
ATOM   1211 C  CD2 . LEU A 1 156 ? -16.682 -9.578  7.454   1.00   10.38 ? 157 LEU A CD2 1 
ATOM   1212 N  N   . GLN A 1 157 ? -20.147 -7.983  3.825   1.00   14.56 ? 158 GLN A N   1 
ATOM   1213 C  CA  . GLN A 1 157 ? -19.811 -8.465  2.492   1.00   14.88 ? 158 GLN A CA  1 
ATOM   1214 C  C   . GLN A 1 157 ? -19.473 -7.358  1.550   1.00   14.84 ? 158 GLN A C   1 
ATOM   1215 O  O   . GLN A 1 157 ? -18.637 -7.555  0.682   1.00   12.97 ? 158 GLN A O   1 
ATOM   1216 C  CB  . GLN A 1 157 ? -20.937 -9.303  1.896   1.00   16.41 ? 158 GLN A CB  1 
ATOM   1217 C  CG  . GLN A 1 157 ? -20.532 -10.075 0.638   1.00   15.96 ? 158 GLN A CG  1 
ATOM   1218 C  CD  . GLN A 1 157 ? -19.441 -11.105 0.885   1.00   17.15 ? 158 GLN A CD  1 
ATOM   1219 O  OE1 . GLN A 1 157 ? -19.323 -11.706 1.965   1.00   19.44 ? 158 GLN A OE1 1 
ATOM   1220 N  NE2 . GLN A 1 157 ? -18.598 -11.276 -0.099  1.00   17.27 ? 158 GLN A NE2 1 
ATOM   1221 N  N   . LYS A 1 158 ? -20.110 -6.196  1.684   1.00   16.43 ? 159 LYS A N   1 
ATOM   1222 C  CA  . LYS A 1 158 ? -19.784 -5.087  0.732   1.00   17.47 ? 159 LYS A CA  1 
ATOM   1223 C  C   . LYS A 1 158 ? -18.293 -4.709  0.905   1.00   16.99 ? 159 LYS A C   1 
ATOM   1224 O  O   . LYS A 1 158 ? -17.589 -4.335  -0.044  1.00   16.47 ? 159 LYS A O   1 
ATOM   1225 C  CB  . LYS A 1 158 ? -20.762 -3.903  0.882   1.00   21.35 ? 159 LYS A CB  1 
ATOM   1226 C  CG  . LYS A 1 158 ? -20.311 -2.525  0.309   1.00   29.50 ? 159 LYS A CG  1 
ATOM   1227 C  CD  . LYS A 1 158 ? -20.474 -2.288  -1.220  1.00   36.63 ? 159 LYS A CD  1 
ATOM   1228 C  CE  . LYS A 1 158 ? -20.354 -0.804  -1.683  1.00   39.77 ? 159 LYS A CE  1 
ATOM   1229 N  NZ  . LYS A 1 158 ? -21.313 0.190   -1.090  1.00   37.83 ? 159 LYS A NZ  1 
ATOM   1230 N  N   . VAL A 1 159 ? -17.783 -4.909  2.122   1.00   14.87 ? 160 VAL A N   1 
ATOM   1231 C  CA  . VAL A 1 159 ? -16.347 -4.687  2.389   1.00   13.41 ? 160 VAL A CA  1 
ATOM   1232 C  C   . VAL A 1 159 ? -15.498 -5.784  1.722   1.00   12.53 ? 160 VAL A C   1 
ATOM   1233 O  O   . VAL A 1 159 ? -14.525 -5.496  1.044   1.00   14.62 ? 160 VAL A O   1 
ATOM   1234 C  CB  . VAL A 1 159 ? -16.084 -4.668  3.901   1.00   11.76 ? 160 VAL A CB  1 
ATOM   1235 C  CG1 . VAL A 1 159 ? -14.593 -4.779  4.181   1.00   13.24 ? 160 VAL A CG1 1 
ATOM   1236 C  CG2 . VAL A 1 159 ? -16.648 -3.408  4.523   1.00   13.28 ? 160 VAL A CG2 1 
ATOM   1237 N  N   . VAL A 1 160 ? -15.836 -7.046  1.949   1.00   12.11 ? 161 VAL A N   1 
ATOM   1238 C  CA  . VAL A 1 160 ? -15.059 -8.148  1.437   1.00   14.03 ? 161 VAL A CA  1 
ATOM   1239 C  C   . VAL A 1 160 ? -15.022 -8.075  -0.091  1.00   14.73 ? 161 VAL A C   1 
ATOM   1240 O  O   . VAL A 1 160 ? -14.002 -8.272  -0.706  1.00   14.59 ? 161 VAL A O   1 
ATOM   1241 C  CB  . VAL A 1 160 ? -15.735 -9.483  1.890   1.00   15.80 ? 161 VAL A CB  1 
ATOM   1242 C  CG1 . VAL A 1 160 ? -15.378 -10.625 0.951   1.00   16.89 ? 161 VAL A CG1 1 
ATOM   1243 C  CG2 . VAL A 1 160 ? -15.377 -9.732  3.336   1.00   14.53 ? 161 VAL A CG2 1 
ATOM   1244 N  N   . ASP A 1 161 ? -16.131 -7.688  -0.696  1.00   18.43 ? 162 ASP A N   1 
ATOM   1245 C  CA  . ASP A 1 161 ? -16.177 -7.635  -2.159  1.00   21.87 ? 162 ASP A CA  1 
ATOM   1246 C  C   . ASP A 1 161 ? -15.358 -6.578  -2.891  1.00   23.82 ? 162 ASP A C   1 
ATOM   1247 O  O   . ASP A 1 161 ? -15.207 -6.687  -4.118  1.00   24.74 ? 162 ASP A O   1 
ATOM   1248 C  CB  . ASP A 1 161 ? -17.612 -7.520  -2.604  1.00   28.83 ? 162 ASP A CB  1 
ATOM   1249 C  CG  . ASP A 1 161 ? -18.293 -8.873  -2.698  1.00   33.22 ? 162 ASP A CG  1 
ATOM   1250 O  OD1 . ASP A 1 161 ? -17.604 -9.925  -2.869  1.00   32.86 ? 162 ASP A OD1 1 
ATOM   1251 O  OD2 . ASP A 1 161 ? -19.537 -8.867  -2.579  1.00   38.74 ? 162 ASP A OD2 1 
ATOM   1252 N  N   . VAL A 1 162 ? -14.886 -5.544  -2.193  1.00   18.84 ? 163 VAL A N   1 
ATOM   1253 C  CA  . VAL A 1 162 ? -14.046 -4.481  -2.821  1.00   17.59 ? 163 VAL A CA  1 
ATOM   1254 C  C   . VAL A 1 162 ? -12.568 -4.767  -2.589  1.00   17.25 ? 163 VAL A C   1 
ATOM   1255 O  O   . VAL A 1 162 ? -11.694 -4.141  -3.184  1.00   19.62 ? 163 VAL A O   1 
ATOM   1256 C  CB  . VAL A 1 162 ? -14.472 -3.117  -2.225  1.00   16.92 ? 163 VAL A CB  1 
ATOM   1257 C  CG1 . VAL A 1 162 ? -13.835 -2.932  -0.870  1.00   16.82 ? 163 VAL A CG1 1 
ATOM   1258 C  CG2 . VAL A 1 162 ? -14.240 -1.896  -3.138  1.00   18.72 ? 163 VAL A CG2 1 
ATOM   1259 N  N   . LEU A 1 163 ? -12.224 -5.743  -1.741  1.00   17.44 ? 164 LEU A N   1 
ATOM   1260 C  CA  . LEU A 1 163 ? -10.800 -5.963  -1.371  1.00   17.26 ? 164 LEU A CA  1 
ATOM   1261 C  C   . LEU A 1 163 ? -9.836  -6.202  -2.549  1.00   18.83 ? 164 LEU A C   1 
ATOM   1262 O  O   . LEU A 1 163 ? -8.639  -5.825  -2.491  1.00   17.31 ? 164 LEU A O   1 
ATOM   1263 C  CB  . LEU A 1 163 ? -10.636 -7.081  -0.332  1.00   15.87 ? 164 LEU A CB  1 
ATOM   1264 C  CG  . LEU A 1 163 ? -11.293 -6.758  1.031   1.00   15.11 ? 164 LEU A CG  1 
ATOM   1265 C  CD1 . LEU A 1 163 ? -11.163 -7.933  1.985   1.00   16.13 ? 164 LEU A CD1 1 
ATOM   1266 C  CD2 . LEU A 1 163 ? -10.747 -5.476  1.682   1.00   15.26 ? 164 LEU A CD2 1 
ATOM   1267 N  N   . ASP A 1 164 ? -10.371 -6.840  -3.590  1.00   19.51 ? 165 ASP A N   1 
ATOM   1268 C  CA  . ASP A 1 164 ? -9.612  -7.178  -4.777  1.00   23.92 ? 165 ASP A CA  1 
ATOM   1269 C  C   . ASP A 1 164 ? -9.167  -5.887  -5.510  1.00   23.58 ? 165 ASP A C   1 
ATOM   1270 O  O   . ASP A 1 164 ? -8.121  -5.870  -6.137  1.00   24.90 ? 165 ASP A O   1 
ATOM   1271 C  CB  . ASP A 1 164 ? -10.431 -8.091  -5.715  1.00   26.35 ? 165 ASP A CB  1 
ATOM   1272 C  CG  . ASP A 1 164 ? -11.396 -7.296  -6.589  1.00   30.96 ? 165 ASP A CG  1 
ATOM   1273 O  OD1 . ASP A 1 164 ? -12.474 -6.810  -6.107  1.00   31.55 ? 165 ASP A OD1 1 
ATOM   1274 O  OD2 . ASP A 1 164 ? -11.078 -7.111  -7.788  1.00   33.03 ? 165 ASP A OD2 1 
ATOM   1275 N  N   . SER A 1 165 ? -9.936  -4.812  -5.392  1.00   23.06 ? 166 SER A N   1 
ATOM   1276 C  CA  . SER A 1 165 ? -9.521  -3.518  -5.933  1.00   24.93 ? 166 SER A CA  1 
ATOM   1277 C  C   . SER A 1 165 ? -8.458  -2.768  -5.106  1.00   23.98 ? 166 SER A C   1 
ATOM   1278 O  O   . SER A 1 165 ? -7.923  -1.808  -5.601  1.00   22.39 ? 166 SER A O   1 
ATOM   1279 C  CB  . SER A 1 165 ? -10.720 -2.631  -6.215  1.00   24.89 ? 166 SER A CB  1 
ATOM   1280 O  OG  . SER A 1 165 ? -11.272 -2.181  -4.993  1.00   31.00 ? 166 SER A OG  1 
ATOM   1281 N  N   . ILE A 1 166 ? -8.155  -3.198  -3.859  1.00   19.26 ? 167 ILE A N   1 
ATOM   1282 C  CA  . ILE A 1 166 ? -7.094  -2.541  -3.034  1.00   17.89 ? 167 ILE A CA  1 
ATOM   1283 C  C   . ILE A 1 166 ? -6.072  -3.583  -2.545  1.00   17.17 ? 167 ILE A C   1 
ATOM   1284 O  O   . ILE A 1 166 ? -5.752  -3.679  -1.339  1.00   15.04 ? 167 ILE A O   1 
ATOM   1285 C  CB  . ILE A 1 166 ? -7.722  -1.778  -1.825  1.00   16.70 ? 167 ILE A CB  1 
ATOM   1286 C  CG1 . ILE A 1 166 ? -8.557  -2.754  -0.966  1.00   15.62 ? 167 ILE A CG1 1 
ATOM   1287 C  CG2 . ILE A 1 166 ? -8.619  -0.658  -2.332  1.00   16.53 ? 167 ILE A CG2 1 
ATOM   1288 C  CD1 . ILE A 1 166 ? -8.852  -2.312  0.459   1.00   14.02 ? 167 ILE A CD1 1 
ATOM   1289 N  N   . LYS A 1 167 ? -5.632  -4.450  -3.455  1.00   17.70 ? 168 LYS A N   1 
ATOM   1290 C  CA  . LYS A 1 167 ? -4.879  -5.629  -3.032  1.00   20.27 ? 168 LYS A CA  1 
ATOM   1291 C  C   . LYS A 1 167 ? -3.533  -5.294  -2.410  1.00   21.13 ? 168 LYS A C   1 
ATOM   1292 O  O   . LYS A 1 167 ? -3.089  -5.955  -1.443  1.00   18.79 ? 168 LYS A O   1 
ATOM   1293 C  CB  . LYS A 1 167 ? -4.673  -6.587  -4.231  1.00   20.59 ? 168 LYS A CB  1 
ATOM   1294 C  CG  . LYS A 1 167 ? -3.724  -7.748  -3.926  1.00   23.62 ? 168 LYS A CG  1 
ATOM   1295 C  CD  . LYS A 1 167 ? -3.528  -8.638  -5.166  1.00   27.60 ? 168 LYS A CD  1 
ATOM   1296 C  CE  . LYS A 1 167 ? -2.700  -9.851  -4.777  1.00   31.21 ? 168 LYS A CE  1 
ATOM   1297 N  NZ  . LYS A 1 167 ? -2.660  -10.834 -5.888  1.00   41.43 ? 168 LYS A NZ  1 
ATOM   1298 N  N   . THR A 1 168 ? -2.870  -4.270  -2.963  1.00   19.39 ? 169 THR A N   1 
ATOM   1299 C  CA  . THR A 1 168 ? -1.520  -3.958  -2.521  1.00   19.07 ? 169 THR A CA  1 
ATOM   1300 C  C   . THR A 1 168 ? -1.470  -2.593  -1.823  1.00   18.44 ? 169 THR A C   1 
ATOM   1301 O  O   . THR A 1 168 ? -2.370  -1.752  -1.971  1.00   21.07 ? 169 THR A O   1 
ATOM   1302 C  CB  . THR A 1 168 ? -0.488  -3.987  -3.703  1.00   19.89 ? 169 THR A CB  1 
ATOM   1303 O  OG1 . THR A 1 168 ? -0.968  -3.153  -4.753  1.00   20.55 ? 169 THR A OG1 1 
ATOM   1304 C  CG2 . THR A 1 168 ? -0.305  -5.333  -4.222  1.00   20.10 ? 169 THR A CG2 1 
ATOM   1305 N  N   . LYS A 1 169 ? -0.443  -2.425  -1.013  1.00   19.57 ? 170 LYS A N   1 
ATOM   1306 C  CA  . LYS A 1 169 ? -0.136  -1.196  -0.248  1.00   19.71 ? 170 LYS A CA  1 
ATOM   1307 C  C   . LYS A 1 169 ? -0.254  0.090   -1.021  1.00   19.37 ? 170 LYS A C   1 
ATOM   1308 O  O   . LYS A 1 169 ? 0.263   0.234   -2.132  1.00   20.24 ? 170 LYS A O   1 
ATOM   1309 C  CB  . LYS A 1 169 ? 1.290   -1.339  0.304   1.00   22.44 ? 170 LYS A CB  1 
ATOM   1310 C  CG  . LYS A 1 169 ? 1.860   -0.100  1.017   1.00   24.05 ? 170 LYS A CG  1 
ATOM   1311 C  CD  . LYS A 1 169 ? 3.196   -0.520  1.589   1.00   28.95 ? 170 LYS A CD  1 
ATOM   1312 C  CE  . LYS A 1 169 ? 3.825   0.647   2.318   1.00   37.09 ? 170 LYS A CE  1 
ATOM   1313 N  NZ  . LYS A 1 169 ? 5.301   0.475   2.232   1.00   44.39 ? 170 LYS A NZ  1 
ATOM   1314 N  N   . GLY A 1 170 ? -1.016  1.019   -0.486  1.00   20.99 ? 171 GLY A N   1 
ATOM   1315 C  CA  . GLY A 1 170 ? -1.220  2.243   -1.199  1.00   21.35 ? 171 GLY A CA  1 
ATOM   1316 C  C   . GLY A 1 170 ? -2.451  2.333   -2.058  1.00   26.11 ? 171 GLY A C   1 
ATOM   1317 O  O   . GLY A 1 170 ? -2.844  3.474   -2.375  1.00   25.82 ? 171 GLY A O   1 
ATOM   1318 N  N   . LYS A 1 171 ? -3.079  1.197   -2.450  1.00   19.66 ? 172 LYS A N   1 
ATOM   1319 C  CA  . LYS A 1 171 ? -4.297  1.292   -3.249  1.00   20.39 ? 172 LYS A CA  1 
ATOM   1320 C  C   . LYS A 1 171 ? -5.465  1.772   -2.427  1.00   20.77 ? 172 LYS A C   1 
ATOM   1321 O  O   . LYS A 1 171 ? -5.566  1.431   -1.231  1.00   18.40 ? 172 LYS A O   1 
ATOM   1322 C  CB  . LYS A 1 171 ? -4.643  -0.021  -3.973  1.00   22.84 ? 172 LYS A CB  1 
ATOM   1323 C  CG  . LYS A 1 171 ? -3.490  -0.523  -4.832  1.00   24.46 ? 172 LYS A CG  1 
ATOM   1324 C  CD  . LYS A 1 171 ? -3.913  -1.510  -5.892  1.00   32.24 ? 172 LYS A CD  1 
ATOM   1325 C  CE  . LYS A 1 171 ? -4.882  -0.872  -6.891  1.00   37.36 ? 172 LYS A CE  1 
ATOM   1326 N  NZ  . LYS A 1 171 ? -5.371  -1.849  -7.929  1.00   40.52 ? 172 LYS A NZ  1 
ATOM   1327 N  N   . SER A 1 172 ? -6.354  2.544   -3.065  1.00   19.25 ? 173 SER A N   1 
ATOM   1328 C  CA  . SER A 1 172 ? -7.566  3.009   -2.456  1.00   20.61 ? 173 SER A CA  1 
ATOM   1329 C  C   . SER A 1 172 ? -8.717  2.932   -3.434  1.00   23.58 ? 173 SER A C   1 
ATOM   1330 O  O   . SER A 1 172 ? -8.535  2.846   -4.675  1.00   22.72 ? 173 SER A O   1 
ATOM   1331 C  CB  . SER A 1 172 ? -7.431  4.453   -1.939  1.00   23.21 ? 173 SER A CB  1 
ATOM   1332 O  OG  . SER A 1 172 ? -7.287  5.368   -3.019  1.00   24.16 ? 173 SER A OG  1 
ATOM   1333 N  N   . ALA A 1 173 ? -9.913  2.928   -2.895  1.00   21.96 ? 174 ALA A N   1 
ATOM   1334 C  CA  . ALA A 1 173 ? -11.054 2.872   -3.764  1.00   24.69 ? 174 ALA A CA  1 
ATOM   1335 C  C   . ALA A 1 173 ? -12.159 3.618   -3.100  1.00   25.25 ? 174 ALA A C   1 
ATOM   1336 O  O   . ALA A 1 173 ? -12.255 3.677   -1.842  1.00   22.84 ? 174 ALA A O   1 
ATOM   1337 C  CB  . ALA A 1 173 ? -11.450 1.431   -4.033  1.00   24.92 ? 174 ALA A CB  1 
ATOM   1338 N  N   . ASP A 1 174 ? -12.981 4.235   -3.951  1.00   27.22 ? 175 ASP A N   1 
ATOM   1339 C  CA  . ASP A 1 174 ? -14.231 4.893   -3.504  1.00   28.10 ? 175 ASP A CA  1 
ATOM   1340 C  C   . ASP A 1 174 ? -15.087 3.873   -2.735  1.00   24.85 ? 175 ASP A C   1 
ATOM   1341 O  O   . ASP A 1 174 ? -15.208 2.696   -3.144  1.00   20.96 ? 175 ASP A O   1 
ATOM   1342 C  CB  . ASP A 1 174 ? -14.993 5.529   -4.702  1.00   32.66 ? 175 ASP A CB  1 
ATOM   1343 C  CG  . ASP A 1 174 ? -14.164 6.646   -5.402  1.00   39.98 ? 175 ASP A CG  1 
ATOM   1344 O  OD1 . ASP A 1 174 ? -13.600 7.541   -4.703  1.00   43.78 ? 175 ASP A OD1 1 
ATOM   1345 O  OD2 . ASP A 1 174 ? -14.071 6.638   -6.660  1.00   48.14 ? 175 ASP A OD2 1 
ATOM   1346 N  N   . PHE A 1 175 ? -15.618 4.297   -1.590  1.00   19.43 ? 176 PHE A N   1 
ATOM   1347 C  CA  . PHE A 1 175 ? -16.393 3.364   -0.754  1.00   20.21 ? 176 PHE A CA  1 
ATOM   1348 C  C   . PHE A 1 175 ? -17.519 4.086   -0.012  1.00   19.99 ? 176 PHE A C   1 
ATOM   1349 O  O   . PHE A 1 175 ? -17.465 4.329   1.208   1.00   25.03 ? 176 PHE A O   1 
ATOM   1350 C  CB  . PHE A 1 175 ? -15.447 2.595   0.189   1.00   17.56 ? 176 PHE A CB  1 
ATOM   1351 C  CG  . PHE A 1 175 ? -16.059 1.338   0.753   1.00   19.20 ? 176 PHE A CG  1 
ATOM   1352 C  CD1 . PHE A 1 175 ? -16.283 0.220   -0.070  1.00   18.23 ? 176 PHE A CD1 1 
ATOM   1353 C  CD2 . PHE A 1 175 ? -16.409 1.259   2.116   1.00   19.73 ? 176 PHE A CD2 1 
ATOM   1354 C  CE1 . PHE A 1 175 ? -16.874 -0.946  0.454   1.00   20.68 ? 176 PHE A CE1 1 
ATOM   1355 C  CE2 . PHE A 1 175 ? -16.962 0.093   2.641   1.00   19.05 ? 176 PHE A CE2 1 
ATOM   1356 C  CZ  . PHE A 1 175 ? -17.206 -1.001  1.796   1.00   20.71 ? 176 PHE A CZ  1 
ATOM   1357 N  N   . THR A 1 176 ? -18.528 4.498   -0.749  1.00   17.76 ? 177 THR A N   1 
ATOM   1358 C  CA  . THR A 1 176 ? -19.587 5.343   -0.211  1.00   16.69 ? 177 THR A CA  1 
ATOM   1359 C  C   . THR A 1 176 ? -20.773 4.516   0.218   1.00   15.57 ? 177 THR A C   1 
ATOM   1360 O  O   . THR A 1 176 ? -20.891 3.376   -0.246  1.00   17.08 ? 177 THR A O   1 
ATOM   1361 C  CB  . THR A 1 176 ? -20.067 6.341   -1.294  1.00   19.03 ? 177 THR A CB  1 
ATOM   1362 O  OG1 . THR A 1 176 ? -20.510 5.601   -2.450  1.00   18.03 ? 177 THR A OG1 1 
ATOM   1363 C  CG2 . THR A 1 176 ? -18.959 7.231   -1.687  1.00   19.77 ? 177 THR A CG2 1 
ATOM   1364 N  N   . ASN A 1 177 ? -21.564 5.061   1.142   1.00   13.11 ? 178 ASN A N   1 
ATOM   1365 C  CA  . ASN A 1 177 ? -22.903 4.556   1.582   1.00   15.15 ? 178 ASN A CA  1 
ATOM   1366 C  C   . ASN A 1 177 ? -22.743 3.187   2.281   1.00   15.12 ? 178 ASN A C   1 
ATOM   1367 O  O   . ASN A 1 177 ? -23.624 2.321   2.192   1.00   16.91 ? 178 ASN A O   1 
ATOM   1368 C  CB  . ASN A 1 177 ? -23.877 4.411   0.418   1.00   15.49 ? 178 ASN A CB  1 
ATOM   1369 C  CG  . ASN A 1 177 ? -24.170 5.740   -0.269  1.00   16.61 ? 178 ASN A CG  1 
ATOM   1370 O  OD1 . ASN A 1 177 ? -24.884 6.568   0.267   1.00   18.26 ? 178 ASN A OD1 1 
ATOM   1371 N  ND2 . ASN A 1 177 ? -23.603 5.941   -1.438  1.00   17.70 ? 178 ASN A ND2 1 
ATOM   1372 N  N   . PHE A 1 178 ? -21.578 2.979   2.883   1.00   15.33 ? 179 PHE A N   1 
ATOM   1373 C  CA  . PHE A 1 178 ? -21.404 1.792   3.758   1.00   14.34 ? 179 PHE A CA  1 
ATOM   1374 C  C   . PHE A 1 178 ? -21.941 2.066   5.178   1.00   14.37 ? 179 PHE A C   1 
ATOM   1375 O  O   . PHE A 1 178 ? -21.539 3.048   5.782   1.00   14.13 ? 179 PHE A O   1 
ATOM   1376 C  CB  . PHE A 1 178 ? -19.937 1.303   3.767   1.00   12.82 ? 179 PHE A CB  1 
ATOM   1377 C  CG  . PHE A 1 178 ? -19.763 0.073   4.632   1.00   12.89 ? 179 PHE A CG  1 
ATOM   1378 C  CD1 . PHE A 1 178 ? -20.169 -1.188  4.143   1.00   12.72 ? 179 PHE A CD1 1 
ATOM   1379 C  CD2 . PHE A 1 178 ? -19.396 0.197   5.982   1.00   12.97 ? 179 PHE A CD2 1 
ATOM   1380 C  CE1 . PHE A 1 178 ? -20.096 -2.329  4.948   1.00   13.47 ? 179 PHE A CE1 1 
ATOM   1381 C  CE2 . PHE A 1 178 ? -19.314 -0.938  6.783   1.00   13.58 ? 179 PHE A CE2 1 
ATOM   1382 C  CZ  . PHE A 1 178 ? -19.693 -2.185  6.291   1.00   13.66 ? 179 PHE A CZ  1 
ATOM   1383 N  N   . ASP A 1 179 ? -22.853 1.230   5.701   1.00   14.35 ? 180 ASP A N   1 
ATOM   1384 C  CA  . ASP A 1 179 ? -23.466 1.438   7.003   1.00   15.76 ? 180 ASP A CA  1 
ATOM   1385 C  C   . ASP A 1 179 ? -22.762 0.602   8.087   1.00   15.41 ? 180 ASP A C   1 
ATOM   1386 O  O   . ASP A 1 179 ? -22.934 -0.649  8.103   1.00   14.88 ? 180 ASP A O   1 
ATOM   1387 C  CB  . ASP A 1 179 ? -24.913 0.990   6.950   1.00   17.51 ? 180 ASP A CB  1 
ATOM   1388 C  CG  . ASP A 1 179 ? -25.681 1.390   8.162   1.00   20.48 ? 180 ASP A CG  1 
ATOM   1389 O  OD1 . ASP A 1 179 ? -25.083 1.638   9.217   1.00   18.75 ? 180 ASP A OD1 1 
ATOM   1390 O  OD2 . ASP A 1 179 ? -26.915 1.498   8.062   1.00   24.54 ? 180 ASP A OD2 1 
ATOM   1391 N  N   . PRO A 1 180 ? -21.959 1.245   8.964   1.00   14.48 ? 181 PRO A N   1 
ATOM   1392 C  CA  . PRO A 1 180 ? -21.176 0.407   9.916   1.00   14.46 ? 181 PRO A CA  1 
ATOM   1393 C  C   . PRO A 1 180 ? -22.055 -0.280  10.960  1.00   13.94 ? 181 PRO A C   1 
ATOM   1394 O  O   . PRO A 1 180 ? -21.592 -1.175  11.692  1.00   12.67 ? 181 PRO A O   1 
ATOM   1395 C  CB  . PRO A 1 180 ? -20.237 1.422   10.585  1.00   15.23 ? 181 PRO A CB  1 
ATOM   1396 C  CG  . PRO A 1 180 ? -20.969 2.746   10.443  1.00   14.51 ? 181 PRO A CG  1 
ATOM   1397 C  CD  . PRO A 1 180 ? -21.578 2.667   9.078   1.00   14.49 ? 181 PRO A CD  1 
ATOM   1398 N  N   . ARG A 1 181 ? -23.341 0.064   10.986  1.00   14.08 ? 182 ARG A N   1 
ATOM   1399 C  CA  . ARG A 1 181 ? -24.292 -0.611  11.940  1.00   14.36 ? 182 ARG A CA  1 
ATOM   1400 C  C   . ARG A 1 181 ? -24.459 -2.085  11.612  1.00   14.94 ? 182 ARG A C   1 
ATOM   1401 O  O   . ARG A 1 181 ? -24.847 -2.868  12.471  1.00   15.84 ? 182 ARG A O   1 
ATOM   1402 C  CB  . ARG A 1 181 ? -25.677 0.058   11.898  1.00   15.04 ? 182 ARG A CB  1 
ATOM   1403 C  CG  . ARG A 1 181 ? -25.628 1.447   12.568  1.00   16.00 ? 182 ARG A CG  1 
ATOM   1404 C  CD  . ARG A 1 181 ? -26.965 2.162   12.436  1.00   15.81 ? 182 ARG A CD  1 
ATOM   1405 N  NE  . ARG A 1 181 ? -27.351 2.303   11.020  1.00   16.88 ? 182 ARG A NE  1 
ATOM   1406 C  CZ  . ARG A 1 181 ? -28.415 2.988   10.617  1.00   18.55 ? 182 ARG A CZ  1 
ATOM   1407 N  NH1 . ARG A 1 181 ? -29.158 3.633   11.512  1.00   21.96 ? 182 ARG A NH1 1 
ATOM   1408 N  NH2 . ARG A 1 181 ? -28.707 3.076   9.327   1.00   20.30 ? 182 ARG A NH2 1 
ATOM   1409 N  N   . GLY A 1 182 ? -24.157 -2.447  10.369  1.00   15.44 ? 183 GLY A N   1 
ATOM   1410 C  CA  . GLY A 1 182 ? -24.197 -3.829  9.925   1.00   15.69 ? 183 GLY A CA  1 
ATOM   1411 C  C   . GLY A 1 182 ? -23.020 -4.665  10.406  1.00   15.89 ? 183 GLY A C   1 
ATOM   1412 O  O   . GLY A 1 182 ? -22.976 -5.847  10.146  1.00   16.46 ? 183 GLY A O   1 
ATOM   1413 N  N   . LEU A 1 183 ? -22.105 -4.080  11.176  1.00   15.61 ? 184 LEU A N   1 
ATOM   1414 C  CA  . LEU A 1 183 ? -20.968 -4.832  11.769  1.00   14.98 ? 184 LEU A CA  1 
ATOM   1415 C  C   . LEU A 1 183 ? -21.111 -5.077  13.274  1.00   15.52 ? 184 LEU A C   1 
ATOM   1416 O  O   . LEU A 1 183 ? -20.172 -5.620  13.927  1.00   16.24 ? 184 LEU A O   1 
ATOM   1417 C  CB  . LEU A 1 183 ? -19.647 -4.114  11.516  1.00   13.28 ? 184 LEU A CB  1 
ATOM   1418 C  CG  . LEU A 1 183 ? -19.380 -3.844  10.034  1.00   13.96 ? 184 LEU A CG  1 
ATOM   1419 C  CD1 . LEU A 1 183 ? -18.210 -2.876  9.957   1.00   15.64 ? 184 LEU A CD1 1 
ATOM   1420 C  CD2 . LEU A 1 183 ? -19.080 -5.121  9.251   1.00   15.03 ? 184 LEU A CD2 1 
ATOM   1421 N  N   . LEU A 1 184 ? -22.234 -4.661  13.836  1.00   14.47 ? 185 LEU A N   1 
ATOM   1422 C  CA  . LEU A 1 184 ? -22.394 -4.657  15.302  1.00   15.17 ? 185 LEU A CA  1 
ATOM   1423 C  C   . LEU A 1 184 ? -23.064 -5.943  15.765  1.00   18.23 ? 185 LEU A C   1 
ATOM   1424 O  O   . LEU A 1 184 ? -23.979 -6.454  15.090  1.00   22.71 ? 185 LEU A O   1 
ATOM   1425 C  CB  . LEU A 1 184 ? -23.190 -3.411  15.767  1.00   13.98 ? 185 LEU A CB  1 
ATOM   1426 C  CG  . LEU A 1 184 ? -22.531 -2.049  15.480  1.00   13.56 ? 185 LEU A CG  1 
ATOM   1427 C  CD1 . LEU A 1 184 ? -23.418 -1.025  16.138  1.00   15.00 ? 185 LEU A CD1 1 
ATOM   1428 C  CD2 . LEU A 1 184 ? -21.079 -1.867  15.951  1.00   12.73 ? 185 LEU A CD2 1 
ATOM   1429 N  N   . PRO A 1 185 ? -22.617 -6.490  16.916  1.00   15.94 ? 186 PRO A N   1 
ATOM   1430 C  CA  . PRO A 1 185 ? -23.369 -7.595  17.449  1.00   15.68 ? 186 PRO A CA  1 
ATOM   1431 C  C   . PRO A 1 185 ? -24.692 -7.070  18.062  1.00   17.15 ? 186 PRO A C   1 
ATOM   1432 O  O   . PRO A 1 185 ? -24.946 -5.871  18.082  1.00   15.24 ? 186 PRO A O   1 
ATOM   1433 C  CB  . PRO A 1 185 ? -22.427 -8.156  18.533  1.00   14.18 ? 186 PRO A CB  1 
ATOM   1434 C  CG  . PRO A 1 185 ? -21.792 -6.928  19.066  1.00   14.14 ? 186 PRO A CG  1 
ATOM   1435 C  CD  . PRO A 1 185 ? -21.633 -5.988  17.859  1.00   13.35 ? 186 PRO A CD  1 
ATOM   1436 N  N   . GLU A 1 186 ? -25.508 -7.982  18.597  1.00   16.91 ? 187 GLU A N   1 
ATOM   1437 C  CA  . GLU A 1 186 ? -26.781 -7.632  19.159  1.00   17.11 ? 187 GLU A CA  1 
ATOM   1438 C  C   . GLU A 1 186 ? -26.597 -6.914  20.481  1.00   17.56 ? 187 GLU A C   1 
ATOM   1439 O  O   . GLU A 1 186 ? -27.262 -5.907  20.749  1.00   17.31 ? 187 GLU A O   1 
ATOM   1440 C  CB  . GLU A 1 186 ? -27.547 -8.930  19.325  1.00   19.90 ? 187 GLU A CB  1 
ATOM   1441 C  CG  . GLU A 1 186 ? -28.838 -8.896  20.072  1.00   24.10 ? 187 GLU A CG  1 
ATOM   1442 C  CD  . GLU A 1 186 ? -29.368 -10.319 20.281  1.00   24.05 ? 187 GLU A CD  1 
ATOM   1443 O  OE1 . GLU A 1 186 ? -29.296 -11.173 19.347  1.00   23.66 ? 187 GLU A OE1 1 
ATOM   1444 O  OE2 . GLU A 1 186 ? -29.817 -10.544 21.401  1.00   27.52 ? 187 GLU A OE2 1 
ATOM   1445 N  N   . SER A 1 187 ? -25.681 -7.390  21.324  1.00   15.18 ? 188 SER A N   1 
ATOM   1446 C  CA  . SER A 1 187 ? -25.588 -6.746  22.648  1.00   14.48 ? 188 SER A CA  1 
ATOM   1447 C  C   . SER A 1 187 ? -24.489 -5.666  22.614  1.00   13.58 ? 188 SER A C   1 
ATOM   1448 O  O   . SER A 1 187 ? -23.482 -5.893  21.975  1.00   14.31 ? 188 SER A O   1 
ATOM   1449 C  CB  . SER A 1 187 ? -25.257 -7.811  23.741  1.00   14.67 ? 188 SER A CB  1 
ATOM   1450 O  OG  . SER A 1 187 ? -25.017 -7.189  25.007  1.00   13.84 ? 188 SER A OG  1 
ATOM   1451 N  N   . LEU A 1 188 ? -24.646 -4.576  23.356  1.00   14.87 ? 189 LEU A N   1 
ATOM   1452 C  CA  . LEU A 1 188 ? -23.550 -3.590  23.546  1.00   15.62 ? 189 LEU A CA  1 
ATOM   1453 C  C   . LEU A 1 188 ? -22.873 -3.715  24.922  1.00   15.80 ? 189 LEU A C   1 
ATOM   1454 O  O   . LEU A 1 188 ? -22.152 -2.818  25.332  1.00   15.29 ? 189 LEU A O   1 
ATOM   1455 C  CB  . LEU A 1 188 ? -24.100 -2.150  23.365  1.00   15.93 ? 189 LEU A CB  1 
ATOM   1456 C  CG  . LEU A 1 188 ? -24.582 -1.792  21.959  1.00   16.49 ? 189 LEU A CG  1 
ATOM   1457 C  CD1 . LEU A 1 188 ? -24.972 -0.316  21.829  1.00   16.77 ? 189 LEU A CD1 1 
ATOM   1458 C  CD2 . LEU A 1 188 ? -23.617 -2.219  20.850  1.00   16.80 ? 189 LEU A CD2 1 
ATOM   1459 N  N   . ASP A 1 189 ? -23.115 -4.806  25.656  1.00   15.47 ? 190 ASP A N   1 
ATOM   1460 C  CA  . ASP A 1 189 ? -22.323 -5.049  26.869  1.00   15.93 ? 190 ASP A CA  1 
ATOM   1461 C  C   . ASP A 1 189 ? -20.822 -4.964  26.527  1.00   15.16 ? 190 ASP A C   1 
ATOM   1462 O  O   . ASP A 1 189 ? -20.400 -5.457  25.457  1.00   15.27 ? 190 ASP A O   1 
ATOM   1463 C  CB  . ASP A 1 189 ? -22.642 -6.415  27.418  1.00   16.57 ? 190 ASP A CB  1 
ATOM   1464 C  CG  . ASP A 1 189 ? -24.015 -6.447  28.148  1.00   22.22 ? 190 ASP A CG  1 
ATOM   1465 O  OD1 . ASP A 1 189 ? -24.658 -5.389  28.314  1.00   22.32 ? 190 ASP A OD1 1 
ATOM   1466 O  OD2 . ASP A 1 189 ? -24.432 -7.547  28.532  1.00   23.11 ? 190 ASP A OD2 1 
ATOM   1467 N  N   . TYR A 1 190 ? -20.024 -4.387  27.437  1.00   13.23 ? 191 TYR A N   1 
ATOM   1468 C  CA  . TYR A 1 190 ? -18.612 -4.129  27.137  1.00   12.33 ? 191 TYR A CA  1 
ATOM   1469 C  C   . TYR A 1 190 ? -17.680 -4.210  28.357  1.00   12.56 ? 191 TYR A C   1 
ATOM   1470 O  O   . TYR A 1 190 ? -18.135 -4.178  29.510  1.00   11.85 ? 191 TYR A O   1 
ATOM   1471 C  CB  . TYR A 1 190 ? -18.471 -2.758  26.444  1.00   11.61 ? 191 TYR A CB  1 
ATOM   1472 C  CG  . TYR A 1 190 ? -18.847 -1.588  27.396  1.00   11.87 ? 191 TYR A CG  1 
ATOM   1473 C  CD1 . TYR A 1 190 ? -17.907 -1.035  28.313  1.00   11.42 ? 191 TYR A CD1 1 
ATOM   1474 C  CD2 . TYR A 1 190 ? -20.101 -1.016  27.323  1.00   12.07 ? 191 TYR A CD2 1 
ATOM   1475 C  CE1 . TYR A 1 190 ? -18.262 0.041   29.157  1.00   11.71 ? 191 TYR A CE1 1 
ATOM   1476 C  CE2 . TYR A 1 190 ? -20.464 0.038   28.164  1.00   13.47 ? 191 TYR A CE2 1 
ATOM   1477 C  CZ  . TYR A 1 190 ? -19.546 0.542   29.086  1.00   13.00 ? 191 TYR A CZ  1 
ATOM   1478 O  OH  . TYR A 1 190 ? -19.949 1.605   29.878  1.00   13.76 ? 191 TYR A OH  1 
ATOM   1479 N  N   . TRP A 1 191 ? -16.370 -4.348  28.091  1.00   11.24 ? 192 TRP A N   1 
ATOM   1480 C  CA  . TRP A 1 191 ? -15.313 -4.126  29.049  1.00   10.80 ? 192 TRP A CA  1 
ATOM   1481 C  C   . TRP A 1 191 ? -14.609 -2.849  28.607  1.00   10.99 ? 192 TRP A C   1 
ATOM   1482 O  O   . TRP A 1 191 ? -14.617 -2.482  27.410  1.00   9.96  ? 192 TRP A O   1 
ATOM   1483 C  CB  . TRP A 1 191 ? -14.273 -5.229  28.988  1.00   11.94 ? 192 TRP A CB  1 
ATOM   1484 C  CG  . TRP A 1 191 ? -14.762 -6.600  29.359  1.00   11.70 ? 192 TRP A CG  1 
ATOM   1485 C  CD1 . TRP A 1 191 ? -15.009 -7.088  30.661  1.00   11.53 ? 192 TRP A CD1 1 
ATOM   1486 C  CD2 . TRP A 1 191 ? -15.039 -7.704  28.454  1.00   12.15 ? 192 TRP A CD2 1 
ATOM   1487 N  NE1 . TRP A 1 191 ? -15.438 -8.395  30.596  1.00   12.30 ? 192 TRP A NE1 1 
ATOM   1488 C  CE2 . TRP A 1 191 ? -15.476 -8.817  29.283  1.00   12.79 ? 192 TRP A CE2 1 
ATOM   1489 C  CE3 . TRP A 1 191 ? -14.954 -7.877  27.073  1.00   12.62 ? 192 TRP A CE3 1 
ATOM   1490 C  CZ2 . TRP A 1 191 ? -15.820 -10.034 28.743  1.00   13.38 ? 192 TRP A CZ2 1 
ATOM   1491 C  CZ3 . TRP A 1 191 ? -15.325 -9.098  26.529  1.00   12.61 ? 192 TRP A CZ3 1 
ATOM   1492 C  CH2 . TRP A 1 191 ? -15.717 -10.171 27.337  1.00   14.12 ? 192 TRP A CH2 1 
ATOM   1493 N  N   . THR A 1 192 ? -14.033 -2.124  29.555  1.00   10.93 ? 193 THR A N   1 
ATOM   1494 C  CA  . THR A 1 192 ? -13.313 -0.884  29.221  1.00   11.44 ? 193 THR A CA  1 
ATOM   1495 C  C   . THR A 1 192 ? -12.067 -0.743  30.076  1.00   11.73 ? 193 THR A C   1 
ATOM   1496 O  O   . THR A 1 192 ? -12.057 -1.168  31.233  1.00   12.57 ? 193 THR A O   1 
ATOM   1497 C  CB  . THR A 1 192 ? -14.264 0.370   29.266  1.00   12.10 ? 193 THR A CB  1 
ATOM   1498 O  OG1 . THR A 1 192 ? -13.606 1.584   28.804  1.00   12.23 ? 193 THR A OG1 1 
ATOM   1499 C  CG2 . THR A 1 192 ? -14.822 0.591   30.675  1.00   12.38 ? 193 THR A CG2 1 
ATOM   1500 N  N   . TYR A 1 193 ? -10.987 -0.185  29.493  1.00   11.64 ? 194 TYR A N   1 
ATOM   1501 C  CA  . TYR A 1 193 ? -9.773  0.087   30.219  1.00   10.67 ? 194 TYR A CA  1 
ATOM   1502 C  C   . TYR A 1 193 ? -9.039  1.174   29.444  1.00   11.41 ? 194 TYR A C   1 
ATOM   1503 O  O   . TYR A 1 193 ? -9.330  1.359   28.211  1.00   11.99 ? 194 TYR A O   1 
ATOM   1504 C  CB  . TYR A 1 193 ? -8.927  -1.206  30.408  1.00   10.58 ? 194 TYR A CB  1 
ATOM   1505 C  CG  . TYR A 1 193 ? -8.226  -1.616  29.135  1.00   10.36 ? 194 TYR A CG  1 
ATOM   1506 C  CD1 . TYR A 1 193 ? -8.903  -2.377  28.117  1.00   10.28 ? 194 TYR A CD1 1 
ATOM   1507 C  CD2 . TYR A 1 193 ? -6.919  -1.221  28.895  1.00   10.99 ? 194 TYR A CD2 1 
ATOM   1508 C  CE1 . TYR A 1 193 ? -8.265  -2.750  26.937  1.00   9.47  ? 194 TYR A CE1 1 
ATOM   1509 C  CE2 . TYR A 1 193 ? -6.271  -1.578  27.687  1.00   10.26 ? 194 TYR A CE2 1 
ATOM   1510 C  CZ  . TYR A 1 193 ? -6.949  -2.360  26.753  1.00   10.17 ? 194 TYR A CZ  1 
ATOM   1511 O  OH  . TYR A 1 193 ? -6.294  -2.631  25.565  1.00   10.64 ? 194 TYR A OH  1 
ATOM   1512 N  N   . PRO A 1 194 ? -8.102  1.888   30.116  1.00   10.97 ? 195 PRO A N   1 
ATOM   1513 C  CA  . PRO A 1 194 ? -7.284  2.862   29.422  1.00   10.55 ? 195 PRO A CA  1 
ATOM   1514 C  C   . PRO A 1 194 ? -6.058  2.214   28.755  1.00   10.69 ? 195 PRO A C   1 
ATOM   1515 O  O   . PRO A 1 194 ? -5.322  1.480   29.413  1.00   9.61  ? 195 PRO A O   1 
ATOM   1516 C  CB  . PRO A 1 194 ? -6.844  3.830   30.559  1.00   10.85 ? 195 PRO A CB  1 
ATOM   1517 C  CG  . PRO A 1 194 ? -6.901  3.043   31.838  1.00   11.34 ? 195 PRO A CG  1 
ATOM   1518 C  CD  . PRO A 1 194 ? -7.856  1.896   31.597  1.00   10.98 ? 195 PRO A CD  1 
ATOM   1519 N  N   . GLY A 1 195 ? -5.823  2.506   27.480  1.00   9.76  ? 196 GLY A N   1 
ATOM   1520 C  CA  . GLY A 1 195 ? -4.669  1.880   26.777  1.00   10.51 ? 196 GLY A CA  1 
ATOM   1521 C  C   . GLY A 1 195 ? -4.124  2.724   25.622  1.00   11.02 ? 196 GLY A C   1 
ATOM   1522 O  O   . GLY A 1 195 ? -4.064  3.946   25.769  1.00   10.80 ? 196 GLY A O   1 
ATOM   1523 N  N   . SER A 1 196 ? -3.664  2.090   24.531  1.00   10.15 ? 197 SER A N   1 
ATOM   1524 C  CA  . SER A 1 196 ? -2.859  2.743   23.549  1.00   10.10 ? 197 SER A CA  1 
ATOM   1525 C  C   . SER A 1 196 ? -3.329  2.361   22.137  1.00   10.15 ? 197 SER A C   1 
ATOM   1526 O  O   . SER A 1 196 ? -4.150  1.402   22.021  1.00   9.32  ? 197 SER A O   1 
ATOM   1527 C  CB  . SER A 1 196 ? -1.389  2.299   23.714  1.00   10.71 ? 197 SER A CB  1 
ATOM   1528 O  OG  . SER A 1 196 ? -1.162  0.909   23.251  1.00   10.06 ? 197 SER A OG  1 
ATOM   1529 N  N   . LEU A 1 197 ? -2.838  3.075   21.088  1.00   9.59  ? 198 LEU A N   1 
ATOM   1530 C  CA  . LEU A 1 197 ? -2.852  2.476   19.737  1.00   10.36 ? 198 LEU A CA  1 
ATOM   1531 C  C   . LEU A 1 197 ? -2.117  1.155   19.806  1.00   10.86 ? 198 LEU A C   1 
ATOM   1532 O  O   . LEU A 1 197 ? -1.114  1.012   20.559  1.00   10.99 ? 198 LEU A O   1 
ATOM   1533 C  CB  . LEU A 1 197 ? -2.137  3.319   18.675  1.00   11.48 ? 198 LEU A CB  1 
ATOM   1534 C  CG  . LEU A 1 197 ? -2.320  4.849   18.762  1.00   13.43 ? 198 LEU A CG  1 
ATOM   1535 C  CD1 . LEU A 1 197 ? -1.367  5.564   17.834  1.00   14.84 ? 198 LEU A CD1 1 
ATOM   1536 C  CD2 . LEU A 1 197 ? -3.751  5.269   18.541  1.00   12.77 ? 198 LEU A CD2 1 
ATOM   1537 N  N   . THR A 1 198 ? -2.567  0.186   19.008  1.00   10.57 ? 199 THR A N   1 
ATOM   1538 C  CA  . THR A 1 198 ? -1.915  -1.082  18.966  1.00   10.86 ? 199 THR A CA  1 
ATOM   1539 C  C   . THR A 1 198 ? -0.906  -1.201  17.825  1.00   12.40 ? 199 THR A C   1 
ATOM   1540 O  O   . THR A 1 198 ? -0.307  -2.298  17.654  1.00   12.47 ? 199 THR A O   1 
ATOM   1541 C  CB  . THR A 1 198 ? -2.909  -2.251  18.856  1.00   10.17 ? 199 THR A CB  1 
ATOM   1542 O  OG1 . THR A 1 198 ? -3.590  -2.201  17.585  1.00   9.89  ? 199 THR A OG1 1 
ATOM   1543 C  CG2 . THR A 1 198 ? -3.871  -2.306  20.058  1.00   9.57  ? 199 THR A CG2 1 
ATOM   1544 N  N   . THR A 1 199 ? -0.759  -0.119  17.039  1.00   11.90 ? 200 THR A N   1 
ATOM   1545 C  CA  . THR A 1 199 ? 0.278   -0.002  16.078  1.00   13.41 ? 200 THR A CA  1 
ATOM   1546 C  C   . THR A 1 199 ? 1.134   1.241   16.391  1.00   13.49 ? 200 THR A C   1 
ATOM   1547 O  O   . THR A 1 199 ? 0.639   2.192   16.994  1.00   11.44 ? 200 THR A O   1 
ATOM   1548 C  CB  . THR A 1 199 ? -0.256  0.266   14.674  1.00   14.96 ? 200 THR A CB  1 
ATOM   1549 O  OG1 . THR A 1 199 ? -1.107  1.435   14.717  1.00   15.01 ? 200 THR A OG1 1 
ATOM   1550 C  CG2 . THR A 1 199 ? -0.971  -0.952  14.168  1.00   15.16 ? 200 THR A CG2 1 
ATOM   1551 N  N   . PRO A 1 200 ? 2.402   1.214   15.954  1.00   14.09 ? 201 PRO A N   1 
ATOM   1552 C  CA  . PRO A 1 200 ? 3.166   2.446   16.116  1.00   14.78 ? 201 PRO A CA  1 
ATOM   1553 C  C   . PRO A 1 200 ? 2.341   3.614   15.550  1.00   15.28 ? 201 PRO A C   1 
ATOM   1554 O  O   . PRO A 1 200 ? 1.662   3.454   14.506  1.00   15.95 ? 201 PRO A O   1 
ATOM   1555 C  CB  . PRO A 1 200 ? 4.450   2.178   15.311  1.00   14.22 ? 201 PRO A CB  1 
ATOM   1556 C  CG  . PRO A 1 200 ? 4.606   0.692   15.354  1.00   15.65 ? 201 PRO A CG  1 
ATOM   1557 C  CD  . PRO A 1 200 ? 3.209   0.121   15.368  1.00   14.66 ? 201 PRO A CD  1 
ATOM   1558 N  N   . PRO A 1 201 ? 2.402   4.790   16.197  1.00   15.60 ? 202 PRO A N   1 
ATOM   1559 C  CA  . PRO A 1 201 ? 3.341   5.160   17.297  1.00   14.58 ? 202 PRO A CA  1 
ATOM   1560 C  C   . PRO A 1 201 ? 2.944   4.742   18.732  1.00   13.17 ? 202 PRO A C   1 
ATOM   1561 O  O   . PRO A 1 201 ? 3.632   5.152   19.695  1.00   14.03 ? 202 PRO A O   1 
ATOM   1562 C  CB  . PRO A 1 201 ? 3.425   6.701   17.177  1.00   14.69 ? 202 PRO A CB  1 
ATOM   1563 C  CG  . PRO A 1 201 ? 2.096   7.097   16.661  1.00   14.83 ? 202 PRO A CG  1 
ATOM   1564 C  CD  . PRO A 1 201 ? 1.664   5.977   15.678  1.00   15.27 ? 202 PRO A CD  1 
ATOM   1565 N  N   . LEU A 1 202 ? 1.929   3.864   18.882  1.00   11.69 ? 203 LEU A N   1 
ATOM   1566 C  CA  . LEU A 1 202 ? 1.665   3.208   20.195  1.00   11.28 ? 203 LEU A CA  1 
ATOM   1567 C  C   . LEU A 1 202 ? 1.331   4.267   21.259  1.00   10.66 ? 203 LEU A C   1 
ATOM   1568 O  O   . LEU A 1 202 ? 1.524   4.060   22.454  1.00   10.48 ? 203 LEU A O   1 
ATOM   1569 C  CB  . LEU A 1 202 ? 2.842   2.321   20.643  1.00   11.30 ? 203 LEU A CB  1 
ATOM   1570 C  CG  . LEU A 1 202 ? 3.183   1.142   19.692  1.00   11.39 ? 203 LEU A CG  1 
ATOM   1571 C  CD1 . LEU A 1 202 ? 4.388   0.388   20.217  1.00   11.25 ? 203 LEU A CD1 1 
ATOM   1572 C  CD2 . LEU A 1 202 ? 2.049   0.131   19.577  1.00   11.92 ? 203 LEU A CD2 1 
ATOM   1573 N  N   . LEU A 1 203 ? 0.780   5.379   20.807  1.00   10.88 ? 204 LEU A N   1 
ATOM   1574 C  CA  . LEU A 1 203 ? 0.471   6.505   21.730  1.00   12.47 ? 204 LEU A CA  1 
ATOM   1575 C  C   . LEU A 1 203 ? -0.602  6.095   22.728  1.00   12.77 ? 204 LEU A C   1 
ATOM   1576 O  O   . LEU A 1 203 ? -1.659  5.492   22.366  1.00   11.09 ? 204 LEU A O   1 
ATOM   1577 C  CB  . LEU A 1 203 ? -0.006  7.757   20.925  1.00   12.63 ? 204 LEU A CB  1 
ATOM   1578 C  CG  . LEU A 1 203 ? 1.100   8.328   20.052  1.00   13.63 ? 204 LEU A CG  1 
ATOM   1579 C  CD1 . LEU A 1 203 ? 0.531   9.403   19.115  1.00   15.47 ? 204 LEU A CD1 1 
ATOM   1580 C  CD2 . LEU A 1 203 ? 2.217   8.891   20.949  1.00   13.84 ? 204 LEU A CD2 1 
ATOM   1581 N  N   . GLU A 1 204 ? -0.361  6.479   23.979  1.00   12.16 ? 205 GLU A N   1 
ATOM   1582 C  CA  . GLU A 1 204 ? -1.266  6.119   25.064  1.00   12.57 ? 205 GLU A CA  1 
ATOM   1583 C  C   . GLU A 1 204 ? -2.472  7.124   25.199  1.00   12.81 ? 205 GLU A C   1 
ATOM   1584 O  O   . GLU A 1 204 ? -2.548  7.917   26.153  1.00   11.40 ? 205 GLU A O   1 
ATOM   1585 C  CB  . GLU A 1 204 ? -0.419  5.971   26.350  1.00   13.40 ? 205 GLU A CB  1 
ATOM   1586 C  CG  . GLU A 1 204 ? 0.301   4.619   26.317  1.00   14.08 ? 205 GLU A CG  1 
ATOM   1587 C  CD  . GLU A 1 204 ? 1.357   4.400   27.401  1.00   14.49 ? 205 GLU A CD  1 
ATOM   1588 O  OE1 . GLU A 1 204 ? 1.690   5.336   28.140  1.00   14.06 ? 205 GLU A OE1 1 
ATOM   1589 O  OE2 . GLU A 1 204 ? 1.885   3.283   27.533  1.00   14.39 ? 205 GLU A OE2 1 
ATOM   1590 N  N   . CYS A 1 205 ? -3.426  7.039   24.255  1.00   11.19 ? 206 CYS A N   1 
ATOM   1591 C  CA  . CYS A 1 205 ? -4.442  8.086   24.064  1.00   10.17 ? 206 CYS A CA  1 
ATOM   1592 C  C   . CYS A 1 205 ? -5.822  7.439   23.930  1.00   9.39  ? 206 CYS A C   1 
ATOM   1593 O  O   . CYS A 1 205 ? -6.785  8.083   23.558  1.00   9.87  ? 206 CYS A O   1 
ATOM   1594 C  CB  . CYS A 1 205 ? -4.111  8.837   22.788  1.00   10.62 ? 206 CYS A CB  1 
ATOM   1595 S  SG  . CYS A 1 205 ? -4.111  7.861   21.204  1.00   11.74 ? 206 CYS A SG  1 
ATOM   1596 N  N   . VAL A 1 206 ? -5.909  6.140   24.183  1.00   9.57  ? 207 VAL A N   1 
ATOM   1597 C  CA  . VAL A 1 206 ? -7.151  5.378   23.852  1.00   9.08  ? 207 VAL A CA  1 
ATOM   1598 C  C   . VAL A 1 206 ? -7.937  4.934   25.085  1.00   9.67  ? 207 VAL A C   1 
ATOM   1599 O  O   . VAL A 1 206 ? -7.398  4.281   25.975  1.00   10.18 ? 207 VAL A O   1 
ATOM   1600 C  CB  . VAL A 1 206 ? -6.874  4.097   23.000  1.00   10.09 ? 207 VAL A CB  1 
ATOM   1601 C  CG1 . VAL A 1 206 ? -8.244  3.459   22.597  1.00   8.76  ? 207 VAL A CG1 1 
ATOM   1602 C  CG2 . VAL A 1 206 ? -6.046  4.432   21.699  1.00   9.20  ? 207 VAL A CG2 1 
ATOM   1603 N  N   . THR A 1 207 ? -9.230  5.230   25.130  1.00   9.18  ? 208 THR A N   1 
ATOM   1604 C  CA  . THR A 1 207 ? -10.129 4.499   26.008  1.00   10.13 ? 208 THR A CA  1 
ATOM   1605 C  C   . THR A 1 207 ? -10.668 3.312   25.194  1.00   10.24 ? 208 THR A C   1 
ATOM   1606 O  O   . THR A 1 207 ? -11.357 3.502   24.203  1.00   11.96 ? 208 THR A O   1 
ATOM   1607 C  CB  . THR A 1 207 ? -11.299 5.421   26.517  1.00   9.49  ? 208 THR A CB  1 
ATOM   1608 O  OG1 . THR A 1 207 ? -10.748 6.499   27.290  1.00   8.44  ? 208 THR A OG1 1 
ATOM   1609 C  CG2 . THR A 1 207 ? -12.389 4.679   27.295  1.00   9.57  ? 208 THR A CG2 1 
ATOM   1610 N  N   . TRP A 1 208 ? -10.352 2.094   25.616  1.00   10.76 ? 209 TRP A N   1 
ATOM   1611 C  CA  . TRP A 1 208 ? -10.749 0.902   24.890  1.00   10.90 ? 209 TRP A CA  1 
ATOM   1612 C  C   . TRP A 1 208 ? -12.078 0.460   25.403  1.00   10.77 ? 209 TRP A C   1 
ATOM   1613 O  O   . TRP A 1 208 ? -12.303 0.425   26.649  1.00   11.31 ? 209 TRP A O   1 
ATOM   1614 C  CB  . TRP A 1 208 ? -9.718  -0.263  25.105  1.00   10.36 ? 209 TRP A CB  1 
ATOM   1615 C  CG  . TRP A 1 208 ? -8.626  -0.146  24.096  1.00   9.80  ? 209 TRP A CG  1 
ATOM   1616 C  CD1 . TRP A 1 208 ? -7.376  0.451   24.241  1.00   10.14 ? 209 TRP A CD1 1 
ATOM   1617 C  CD2 . TRP A 1 208 ? -8.722  -0.507  22.681  1.00   9.93  ? 209 TRP A CD2 1 
ATOM   1618 N  NE1 . TRP A 1 208 ? -6.708  0.453   23.041  1.00   9.74  ? 209 TRP A NE1 1 
ATOM   1619 C  CE2 . TRP A 1 208 ? -7.425  -0.164  22.087  1.00   9.75  ? 209 TRP A CE2 1 
ATOM   1620 C  CE3 . TRP A 1 208 ? -9.712  -1.160  21.881  1.00   9.93  ? 209 TRP A CE3 1 
ATOM   1621 C  CZ2 . TRP A 1 208 ? -7.168  -0.360  20.743  1.00   9.20  ? 209 TRP A CZ2 1 
ATOM   1622 C  CZ3 . TRP A 1 208 ? -9.416  -1.376  20.525  1.00   9.60  ? 209 TRP A CZ3 1 
ATOM   1623 C  CH2 . TRP A 1 208 ? -8.171  -1.030  19.996  1.00   9.08  ? 209 TRP A CH2 1 
ATOM   1624 N  N   . ILE A 1 209 ? -12.975 0.177   24.472  1.00   10.64 ? 210 ILE A N   1 
ATOM   1625 C  CA  . ILE A 1 209 ? -14.353 -0.301  24.760  1.00   10.80 ? 210 ILE A CA  1 
ATOM   1626 C  C   . ILE A 1 209 ? -14.478 -1.611  23.922  1.00   10.73 ? 210 ILE A C   1 
ATOM   1627 O  O   . ILE A 1 209 ? -14.621 -1.569  22.737  1.00   10.06 ? 210 ILE A O   1 
ATOM   1628 C  CB  . ILE A 1 209 ? -15.477 0.736   24.417  1.00   11.46 ? 210 ILE A CB  1 
ATOM   1629 C  CG1 . ILE A 1 209 ? -15.227 2.068   25.181  1.00   13.28 ? 210 ILE A CG1 1 
ATOM   1630 C  CG2 . ILE A 1 209 ? -16.867 0.165   24.822  1.00   12.18 ? 210 ILE A CG2 1 
ATOM   1631 C  CD1 . ILE A 1 209 ? -16.014 3.242   24.620  1.00   13.76 ? 210 ILE A CD1 1 
ATOM   1632 N  N   . VAL A 1 210 ? -14.359 -2.762  24.552  1.00   10.56 ? 211 VAL A N   1 
ATOM   1633 C  CA  . VAL A 1 210 ? -14.322 -4.037  23.798  1.00   10.37 ? 211 VAL A CA  1 
ATOM   1634 C  C   . VAL A 1 210 ? -15.639 -4.749  24.092  1.00   11.15 ? 211 VAL A C   1 
ATOM   1635 O  O   . VAL A 1 210 ? -15.914 -5.048  25.249  1.00   10.93 ? 211 VAL A O   1 
ATOM   1636 C  CB  . VAL A 1 210 ? -13.142 -4.915  24.274  1.00   10.10 ? 211 VAL A CB  1 
ATOM   1637 C  CG1 . VAL A 1 210 ? -13.069 -6.249  23.506  1.00   9.67  ? 211 VAL A CG1 1 
ATOM   1638 C  CG2 . VAL A 1 210 ? -11.800 -4.173  24.114  1.00   8.64  ? 211 VAL A CG2 1 
ATOM   1639 N  N   . LEU A 1 211 ? -16.429 -5.029  23.056  1.00   11.29 ? 212 LEU A N   1 
ATOM   1640 C  CA  . LEU A 1 211 ? -17.715 -5.675  23.236  1.00   11.30 ? 212 LEU A CA  1 
ATOM   1641 C  C   . LEU A 1 211 ? -17.546 -7.125  23.638  1.00   12.13 ? 212 LEU A C   1 
ATOM   1642 O  O   . LEU A 1 211 ? -16.718 -7.855  23.064  1.00   10.75 ? 212 LEU A O   1 
ATOM   1643 C  CB  . LEU A 1 211 ? -18.562 -5.614  21.948  1.00   11.63 ? 212 LEU A CB  1 
ATOM   1644 C  CG  . LEU A 1 211 ? -18.969 -4.193  21.426  1.00   11.84 ? 212 LEU A CG  1 
ATOM   1645 C  CD1 . LEU A 1 211 ? -19.981 -4.296  20.272  1.00   12.02 ? 212 LEU A CD1 1 
ATOM   1646 C  CD2 . LEU A 1 211 ? -19.511 -3.303  22.559  1.00   11.43 ? 212 LEU A CD2 1 
ATOM   1647 N  N   . LYS A 1 212 ? -18.399 -7.526  24.586  1.00   13.19 ? 213 LYS A N   1 
ATOM   1648 C  CA  . LYS A 1 212 ? -18.484 -8.890  25.085  1.00   14.41 ? 213 LYS A CA  1 
ATOM   1649 C  C   . LYS A 1 212 ? -18.885 -9.849  23.967  1.00   13.36 ? 213 LYS A C   1 
ATOM   1650 O  O   . LYS A 1 212 ? -18.365 -10.947 23.875  1.00   12.87 ? 213 LYS A O   1 
ATOM   1651 C  CB  . LYS A 1 212 ? -19.558 -8.935  26.202  1.00   17.82 ? 213 LYS A CB  1 
ATOM   1652 C  CG  . LYS A 1 212 ? -19.968 -10.353 26.598  1.00   22.62 ? 213 LYS A CG  1 
ATOM   1653 C  CD  . LYS A 1 212 ? -21.033 -10.318 27.675  1.00   26.48 ? 213 LYS A CD  1 
ATOM   1654 C  CE  . LYS A 1 212 ? -22.387 -10.711 27.143  1.00   28.26 ? 213 LYS A CE  1 
ATOM   1655 N  NZ  . LYS A 1 212 ? -22.883 -9.680  26.199  1.00   32.14 ? 213 LYS A NZ  1 
ATOM   1656 N  N   . GLU A 1 213 ? -19.861 -9.463  23.165  1.00   12.78 ? 214 GLU A N   1 
ATOM   1657 C  CA  . GLU A 1 213 ? -20.426 -10.415 22.132  1.00   13.98 ? 214 GLU A CA  1 
ATOM   1658 C  C   . GLU A 1 213 ? -19.696 -10.316 20.801  1.00   13.09 ? 214 GLU A C   1 
ATOM   1659 O  O   . GLU A 1 213 ? -19.705 -9.231  20.179  1.00   11.27 ? 214 GLU A O   1 
ATOM   1660 C  CB  . GLU A 1 213 ? -21.887 -10.116 21.875  1.00   15.00 ? 214 GLU A CB  1 
ATOM   1661 C  CG  . GLU A 1 213 ? -22.520 -11.133 20.922  1.00   19.52 ? 214 GLU A CG  1 
ATOM   1662 C  CD  . GLU A 1 213 ? -24.028 -10.954 20.735  1.00   20.97 ? 214 GLU A CD  1 
ATOM   1663 O  OE1 . GLU A 1 213 ? -24.628 -10.058 21.356  1.00   19.11 ? 214 GLU A OE1 1 
ATOM   1664 O  OE2 . GLU A 1 213 ? -24.609 -11.728 19.918  1.00   25.15 ? 214 GLU A OE2 1 
ATOM   1665 N  N   . PRO A 1 214 ? -19.048 -11.417 20.357  1.00   12.40 ? 215 PRO A N   1 
ATOM   1666 C  CA  . PRO A 1 214 ? -18.418 -11.419 19.033  1.00   12.93 ? 215 PRO A CA  1 
ATOM   1667 C  C   . PRO A 1 214 ? -19.439 -11.432 17.919  1.00   12.66 ? 215 PRO A C   1 
ATOM   1668 O  O   . PRO A 1 214 ? -20.573 -11.906 18.123  1.00   12.50 ? 215 PRO A O   1 
ATOM   1669 C  CB  . PRO A 1 214 ? -17.627 -12.752 18.962  1.00   13.75 ? 215 PRO A CB  1 
ATOM   1670 C  CG  . PRO A 1 214 ? -17.914 -13.473 20.248  1.00   15.50 ? 215 PRO A CG  1 
ATOM   1671 C  CD  . PRO A 1 214 ? -18.975 -12.733 21.041  1.00   14.95 ? 215 PRO A CD  1 
ATOM   1672 N  N   . ILE A 1 215 ? -19.056 -10.940 16.725  1.00   11.54 ? 216 ILE A N   1 
ATOM   1673 C  CA  . ILE A 1 215 ? -19.891 -11.190 15.573  1.00   11.03 ? 216 ILE A CA  1 
ATOM   1674 C  C   . ILE A 1 215 ? -19.396 -12.462 14.884  1.00   11.13 ? 216 ILE A C   1 
ATOM   1675 O  O   . ILE A 1 215 ? -18.209 -12.801 14.985  1.00   11.71 ? 216 ILE A O   1 
ATOM   1676 C  CB  . ILE A 1 215 ? -19.898 -9.968  14.582  1.00   11.88 ? 216 ILE A CB  1 
ATOM   1677 C  CG1 . ILE A 1 215 ? -18.497 -9.615  14.088  1.00   12.11 ? 216 ILE A CG1 1 
ATOM   1678 C  CG2 . ILE A 1 215 ? -20.517 -8.674  15.310  1.00   12.31 ? 216 ILE A CG2 1 
ATOM   1679 C  CD1 . ILE A 1 215 ? -18.517 -8.663  12.837  1.00   11.47 ? 216 ILE A CD1 1 
ATOM   1680 N  N   . SER A 1 216 ? -20.274 -13.130 14.144  1.00   12.31 ? 217 SER A N   1 
ATOM   1681 C  CA  . SER A 1 216 ? -19.885 -14.248 13.276  1.00   14.47 ? 217 SER A CA  1 
ATOM   1682 C  C   . SER A 1 216 ? -19.639 -13.802 11.848  1.00   13.55 ? 217 SER A C   1 
ATOM   1683 O  O   . SER A 1 216 ? -20.440 -13.046 11.316  1.00   15.32 ? 217 SER A O   1 
ATOM   1684 C  CB  . SER A 1 216 ? -21.006 -15.306 13.238  1.00   16.16 ? 217 SER A CB  1 
ATOM   1685 O  OG  . SER A 1 216 ? -20.697 -16.111 14.320  1.00   25.16 ? 217 SER A OG  1 
ATOM   1686 N  N   . VAL A 1 217 ? -18.559 -14.274 11.243  1.00   12.50 ? 218 VAL A N   1 
ATOM   1687 C  CA  . VAL A 1 217 ? -18.276 -14.081 9.807   1.00   13.44 ? 218 VAL A CA  1 
ATOM   1688 C  C   . VAL A 1 217 ? -17.956 -15.457 9.208   1.00   12.86 ? 218 VAL A C   1 
ATOM   1689 O  O   . VAL A 1 217 ? -17.532 -16.382 9.937   1.00   14.42 ? 218 VAL A O   1 
ATOM   1690 C  CB  . VAL A 1 217 ? -17.083 -13.116 9.562   1.00   11.95 ? 218 VAL A CB  1 
ATOM   1691 C  CG1 . VAL A 1 217 ? -17.380 -11.804 10.260  1.00   11.49 ? 218 VAL A CG1 1 
ATOM   1692 C  CG2 . VAL A 1 217 ? -15.807 -13.737 10.145  1.00   12.94 ? 218 VAL A CG2 1 
ATOM   1693 N  N   . SER A 1 218 ? -18.123 -15.617 7.904   1.00   12.62 ? 219 SER A N   1 
ATOM   1694 C  CA  . SER A 1 218 ? -17.856 -16.952 7.334   1.00   13.11 ? 219 SER A CA  1 
ATOM   1695 C  C   . SER A 1 218 ? -16.401 -17.143 7.060   1.00   13.20 ? 219 SER A C   1 
ATOM   1696 O  O   . SER A 1 218 ? -15.616 -16.190 6.978   1.00   11.81 ? 219 SER A O   1 
ATOM   1697 C  CB  . SER A 1 218 ? -18.645 -17.188 6.046   1.00   14.16 ? 219 SER A CB  1 
ATOM   1698 O  OG  . SER A 1 218 ? -18.188 -16.345 5.047   1.00   14.23 ? 219 SER A OG  1 
ATOM   1699 N  N   . SER A 1 219 ? -16.040 -18.406 6.852   1.00   15.05 ? 220 SER A N   1 
ATOM   1700 C  CA  . SER A 1 219 ? -14.721 -18.778 6.556   1.00   14.35 ? 220 SER A CA  1 
ATOM   1701 C  C   . SER A 1 219 ? -14.371 -18.072 5.230   1.00   15.84 ? 220 SER A C   1 
ATOM   1702 O  O   . SER A 1 219 ? -13.262 -17.544 5.131   1.00   16.17 ? 220 SER A O   1 
ATOM   1703 C  CB  . SER A 1 219 ? -14.646 -20.308 6.452   1.00   17.02 ? 220 SER A CB  1 
ATOM   1704 O  OG  . SER A 1 219 ? -15.675 -20.735 5.526   1.00   18.58 ? 220 SER A OG  1 
ATOM   1705 N  N   . GLU A 1 220 ? -15.280 -18.019 4.233   1.00   17.02 ? 221 GLU A N   1 
ATOM   1706 C  CA  . GLU A 1 220 ? -14.962 -17.375 2.937   1.00   17.21 ? 221 GLU A CA  1 
ATOM   1707 C  C   . GLU A 1 220 ? -14.704 -15.845 3.085   1.00   16.99 ? 221 GLU A C   1 
ATOM   1708 O  O   . GLU A 1 220 ? -13.806 -15.262 2.409   1.00   16.80 ? 221 GLU A O   1 
ATOM   1709 C  CB  . GLU A 1 220 ? -16.084 -17.555 1.951   1.00   19.35 ? 221 GLU A CB  1 
ATOM   1710 C  CG  . GLU A 1 220 ? -16.321 -19.005 1.556   1.00   23.47 ? 221 GLU A CG  1 
ATOM   1711 C  CD  . GLU A 1 220 ? -17.433 -19.628 2.389   1.00   26.73 ? 221 GLU A CD  1 
ATOM   1712 O  OE1 . GLU A 1 220 ? -17.739 -19.149 3.503   1.00   23.49 ? 221 GLU A OE1 1 
ATOM   1713 O  OE2 . GLU A 1 220 ? -18.013 -20.627 1.931   1.00   31.04 ? 221 GLU A OE2 1 
ATOM   1714 N  N   . GLN A 1 221 ? -15.491 -15.208 3.959   1.00   16.23 ? 222 GLN A N   1 
ATOM   1715 C  CA  . GLN A 1 221 ? -15.248 -13.786 4.303   1.00   15.29 ? 222 GLN A CA  1 
ATOM   1716 C  C   . GLN A 1 221 ? -13.851 -13.556 4.859   1.00   14.81 ? 222 GLN A C   1 
ATOM   1717 O  O   . GLN A 1 221 ? -13.083 -12.710 4.337   1.00   12.71 ? 222 GLN A O   1 
ATOM   1718 C  CB  . GLN A 1 221 ? -16.295 -13.304 5.257   1.00   14.58 ? 222 GLN A CB  1 
ATOM   1719 C  CG  . GLN A 1 221 ? -17.625 -13.120 4.543   1.00   15.43 ? 222 GLN A CG  1 
ATOM   1720 C  CD  . GLN A 1 221 ? -18.728 -12.537 5.407   1.00   13.49 ? 222 GLN A CD  1 
ATOM   1721 O  OE1 . GLN A 1 221 ? -18.869 -12.898 6.557   1.00   15.24 ? 222 GLN A OE1 1 
ATOM   1722 N  NE2 . GLN A 1 221 ? -19.560 -11.672 4.816   1.00   12.97 ? 222 GLN A NE2 1 
ATOM   1723 N  N   . VAL A 1 222 ? -13.481 -14.266 5.923   1.00   15.90 ? 223 VAL A N   1 
ATOM   1724 C  CA  . VAL A 1 222 ? -12.088 -14.092 6.435   1.00   17.61 ? 223 VAL A CA  1 
ATOM   1725 C  C   . VAL A 1 222 ? -11.009 -14.528 5.410   1.00   18.71 ? 223 VAL A C   1 
ATOM   1726 O  O   . VAL A 1 222 ? -9.880  -13.981 5.376   1.00   16.97 ? 223 VAL A O   1 
ATOM   1727 C  CB  . VAL A 1 222 ? -11.883 -14.688 7.845   1.00   19.80 ? 223 VAL A CB  1 
ATOM   1728 C  CG1 . VAL A 1 222 ? -11.887 -16.191 7.785   1.00   21.91 ? 223 VAL A CG1 1 
ATOM   1729 C  CG2 . VAL A 1 222 ? -10.565 -14.184 8.455   1.00   19.69 ? 223 VAL A CG2 1 
ATOM   1730 N  N   . LEU A 1 223 ? -11.335 -15.515 4.567   1.00   19.64 ? 224 LEU A N   1 
ATOM   1731 C  CA  . LEU A 1 223 ? -10.360 -15.984 3.566   1.00   19.97 ? 224 LEU A CA  1 
ATOM   1732 C  C   . LEU A 1 223 ? -9.954  -14.841 2.670   1.00   18.59 ? 224 LEU A C   1 
ATOM   1733 O  O   . LEU A 1 223 ? -8.767  -14.711 2.314   1.00   20.74 ? 224 LEU A O   1 
ATOM   1734 C  CB  . LEU A 1 223 ? -10.954 -17.102 2.682   1.00   21.15 ? 224 LEU A CB  1 
ATOM   1735 C  CG  . LEU A 1 223 ? -10.458 -18.488 3.089   1.00   25.85 ? 224 LEU A CG  1 
ATOM   1736 C  CD1 . LEU A 1 223 ? -11.175 -19.631 2.304   1.00   25.96 ? 224 LEU A CD1 1 
ATOM   1737 C  CD2 . LEU A 1 223 ? -8.930  -18.583 2.948   1.00   29.74 ? 224 LEU A CD2 1 
ATOM   1738 N  N   . LYS A 1 224 ? -10.936 -14.024 2.297   1.00   16.06 ? 225 LYS A N   1 
ATOM   1739 C  CA  . LYS A 1 224 ? -10.669 -12.911 1.393   1.00   16.98 ? 225 LYS A CA  1 
ATOM   1740 C  C   . LYS A 1 224 ? -9.800  -11.827 2.045   1.00   15.87 ? 225 LYS A C   1 
ATOM   1741 O  O   . LYS A 1 224 ? -9.045  -11.195 1.315   1.00   14.53 ? 225 LYS A O   1 
ATOM   1742 C  CB  . LYS A 1 224 ? -11.974 -12.313 0.835   1.00   19.19 ? 225 LYS A CB  1 
ATOM   1743 C  CG  . LYS A 1 224 ? -13.018 -13.327 0.325   1.00   23.34 ? 225 LYS A CG  1 
ATOM   1744 C  CD  . LYS A 1 224 ? -13.165 -13.472 -1.161  1.00   26.91 ? 225 LYS A CD  1 
ATOM   1745 C  CE  . LYS A 1 224 ? -13.962 -12.312 -1.755  1.00   32.14 ? 225 LYS A CE  1 
ATOM   1746 N  NZ  . LYS A 1 224 ? -14.249 -12.493 -3.225  1.00   30.61 ? 225 LYS A NZ  1 
ATOM   1747 N  N   . PHE A 1 225 ? -9.880  -11.622 3.398   1.00   13.94 ? 226 PHE A N   1 
ATOM   1748 C  CA  . PHE A 1 225 ? -8.935  -10.718 4.132   1.00   14.47 ? 226 PHE A CA  1 
ATOM   1749 C  C   . PHE A 1 225 ? -7.497  -11.172 3.906   1.00   13.91 ? 226 PHE A C   1 
ATOM   1750 O  O   . PHE A 1 225 ? -6.593  -10.383 3.713   1.00   14.47 ? 226 PHE A O   1 
ATOM   1751 C  CB  . PHE A 1 225 ? -9.141  -10.741 5.688   1.00   14.34 ? 226 PHE A CB  1 
ATOM   1752 C  CG  . PHE A 1 225 ? -10.343 -9.985  6.230   1.00   15.50 ? 226 PHE A CG  1 
ATOM   1753 C  CD1 . PHE A 1 225 ? -11.376 -9.517  5.422   1.00   15.04 ? 226 PHE A CD1 1 
ATOM   1754 C  CD2 . PHE A 1 225 ? -10.495 -9.867  7.642   1.00   16.00 ? 226 PHE A CD2 1 
ATOM   1755 C  CE1 . PHE A 1 225 ? -12.474 -8.845  5.969   1.00   15.95 ? 226 PHE A CE1 1 
ATOM   1756 C  CE2 . PHE A 1 225 ? -11.580 -9.197  8.191   1.00   18.02 ? 226 PHE A CE2 1 
ATOM   1757 C  CZ  . PHE A 1 225 ? -12.583 -8.684  7.351   1.00   16.86 ? 226 PHE A CZ  1 
ATOM   1758 N  N   . ARG A 1 226 ? -7.282  -12.462 4.012   1.00   14.05 ? 227 ARG A N   1 
ATOM   1759 C  CA  . ARG A 1 226 ? -5.941  -13.085 3.841   1.00   14.61 ? 227 ARG A CA  1 
ATOM   1760 C  C   . ARG A 1 226 ? -5.372  -13.086 2.387   1.00   16.34 ? 227 ARG A C   1 
ATOM   1761 O  O   . ARG A 1 226 ? -4.227  -13.432 2.178   1.00   16.02 ? 227 ARG A O   1 
ATOM   1762 C  CB  . ARG A 1 226 ? -6.047  -14.551 4.313   1.00   15.35 ? 227 ARG A CB  1 
ATOM   1763 C  CG  . ARG A 1 226 ? -6.536  -14.731 5.737   1.00   14.59 ? 227 ARG A CG  1 
ATOM   1764 C  CD  . ARG A 1 226 ? -6.446  -16.184 6.194   1.00   15.09 ? 227 ARG A CD  1 
ATOM   1765 N  NE  . ARG A 1 226 ? -6.969  -16.327 7.559   1.00   14.52 ? 227 ARG A NE  1 
ATOM   1766 C  CZ  . ARG A 1 226 ? -7.926  -17.192 7.897   1.00   14.92 ? 227 ARG A CZ  1 
ATOM   1767 N  NH1 . ARG A 1 226 ? -8.428  -18.027 6.960   1.00   15.59 ? 227 ARG A NH1 1 
ATOM   1768 N  NH2 . ARG A 1 226 ? -8.369  -17.238 9.137   1.00   12.64 ? 227 ARG A NH2 1 
ATOM   1769 N  N   . LYS A 1 227 ? -6.143  -12.639 1.404   1.00   17.17 ? 228 LYS A N   1 
ATOM   1770 C  CA  . LYS A 1 227 ? -5.622  -12.505 0.024   1.00   17.24 ? 228 LYS A CA  1 
ATOM   1771 C  C   . LYS A 1 227 ? -5.038  -11.125 -0.241  1.00   17.14 ? 228 LYS A C   1 
ATOM   1772 O  O   . LYS A 1 227 ? -4.383  -10.884 -1.236  1.00   16.20 ? 228 LYS A O   1 
ATOM   1773 C  CB  . LYS A 1 227 ? -6.723  -12.823 -0.989  1.00   17.52 ? 228 LYS A CB  1 
ATOM   1774 C  CG  . LYS A 1 227 ? -7.072  -14.311 -1.123  1.00   21.31 ? 228 LYS A CG  1 
ATOM   1775 C  CD  . LYS A 1 227 ? -8.331  -14.403 -1.968  1.00   25.37 ? 228 LYS A CD  1 
ATOM   1776 C  CE  . LYS A 1 227 ? -8.185  -15.309 -3.188  1.00   29.80 ? 228 LYS A CE  1 
ATOM   1777 N  NZ  . LYS A 1 227 ? -8.966  -16.580 -2.991  1.00   31.42 ? 228 LYS A NZ  1 
ATOM   1778 N  N   . LEU A 1 228 ? -5.244  -10.212 0.689   1.00   17.79 ? 229 LEU A N   1 
ATOM   1779 C  CA  . LEU A 1 228 ? -4.592  -8.907  0.615   1.00   17.38 ? 229 LEU A CA  1 
ATOM   1780 C  C   . LEU A 1 228 ? -3.073  -8.973  0.787   1.00   17.65 ? 229 LEU A C   1 
ATOM   1781 O  O   . LEU A 1 228 ? -2.555  -9.996  1.240   1.00   16.98 ? 229 LEU A O   1 
ATOM   1782 C  CB  . LEU A 1 228 ? -5.204  -8.003  1.678   1.00   16.35 ? 229 LEU A CB  1 
ATOM   1783 C  CG  . LEU A 1 228 ? -6.642  -7.562  1.455   1.00   16.03 ? 229 LEU A CG  1 
ATOM   1784 C  CD1 . LEU A 1 228 ? -7.076  -6.965  2.772   1.00   13.59 ? 229 LEU A CD1 1 
ATOM   1785 C  CD2 . LEU A 1 228 ? -6.748  -6.517  0.336   1.00   15.26 ? 229 LEU A CD2 1 
ATOM   1786 N  N   . ASN A 1 229 ? -2.347  -7.904  0.385   1.00   17.93 ? 230 ASN A N   1 
ATOM   1787 C  CA  . ASN A 1 229 ? -0.859  -7.894  0.444   1.00   18.12 ? 230 ASN A CA  1 
ATOM   1788 C  C   . ASN A 1 229 ? -0.310  -6.741  1.329   1.00   17.06 ? 230 ASN A C   1 
ATOM   1789 O  O   . ASN A 1 229 ? -0.786  -5.626  1.252   1.00   15.67 ? 230 ASN A O   1 
ATOM   1790 C  CB  . ASN A 1 229 ? -0.223  -7.689  -0.948  1.00   18.14 ? 230 ASN A CB  1 
ATOM   1791 C  CG  . ASN A 1 229 ? -0.401  -8.869  -1.927  1.00   21.68 ? 230 ASN A CG  1 
ATOM   1792 O  OD1 . ASN A 1 229 ? 0.057   -8.762  -3.076  1.00   19.89 ? 230 ASN A OD1 1 
ATOM   1793 N  ND2 . ASN A 1 229 ? -1.026  -9.979  -1.493  1.00   20.74 ? 230 ASN A ND2 1 
ATOM   1794 N  N   . PHE A 1 230 ? 0.722   -7.027  2.118   1.00   18.27 ? 231 PHE A N   1 
ATOM   1795 C  CA  . PHE A 1 230 ? 1.531   -5.986  2.824   1.00   20.18 ? 231 PHE A CA  1 
ATOM   1796 C  C   . PHE A 1 230 ? 2.361   -5.125  1.844   1.00   23.81 ? 231 PHE A C   1 
ATOM   1797 O  O   . PHE A 1 230 ? 2.526   -3.909  2.046   1.00   23.53 ? 231 PHE A O   1 
ATOM   1798 C  CB  . PHE A 1 230 ? 2.511   -6.652  3.769   1.00   19.80 ? 231 PHE A CB  1 
ATOM   1799 C  CG  . PHE A 1 230 ? 1.905   -7.213  5.066   1.00   18.95 ? 231 PHE A CG  1 
ATOM   1800 C  CD1 . PHE A 1 230 ? 1.151   -6.437  5.924   1.00   19.00 ? 231 PHE A CD1 1 
ATOM   1801 C  CD2 . PHE A 1 230 ? 2.213   -8.540  5.467   1.00   18.80 ? 231 PHE A CD2 1 
ATOM   1802 C  CE1 . PHE A 1 230 ? 0.678   -6.966  7.163   1.00   18.39 ? 231 PHE A CE1 1 
ATOM   1803 C  CE2 . PHE A 1 230 ? 1.752   -9.059  6.681   1.00   18.20 ? 231 PHE A CE2 1 
ATOM   1804 C  CZ  . PHE A 1 230 ? 0.998   -8.286  7.526   1.00   16.35 ? 231 PHE A CZ  1 
ATOM   1805 N  N   . ASN A 1 231 ? 2.883   -5.775  0.792   1.00   22.28 ? 232 ASN A N   1 
ATOM   1806 C  CA  . ASN A 1 231 ? 3.702   -5.115  -0.233  1.00   24.59 ? 232 ASN A CA  1 
ATOM   1807 C  C   . ASN A 1 231 ? 2.921   -4.178  -1.156  1.00   26.04 ? 232 ASN A C   1 
ATOM   1808 O  O   . ASN A 1 231 ? 1.683   -4.261  -1.276  1.00   22.79 ? 232 ASN A O   1 
ATOM   1809 C  CB  . ASN A 1 231 ? 4.358   -6.146  -1.125  1.00   23.05 ? 232 ASN A CB  1 
ATOM   1810 C  CG  . ASN A 1 231 ? 3.353   -7.100  -1.743  1.00   22.90 ? 232 ASN A CG  1 
ATOM   1811 O  OD1 . ASN A 1 231 ? 2.842   -8.002  -1.072  1.00   21.24 ? 232 ASN A OD1 1 
ATOM   1812 N  ND2 . ASN A 1 231 ? 3.078   -6.919  -3.029  1.00   22.63 ? 232 ASN A ND2 1 
ATOM   1813 N  N   . GLY A 1 232 ? 3.673   -3.319  -1.832  1.00   25.00 ? 233 GLY A N   1 
ATOM   1814 C  CA  . GLY A 1 232 ? 3.135   -2.509  -2.902  1.00   23.78 ? 233 GLY A CA  1 
ATOM   1815 C  C   . GLY A 1 232 ? 3.083   -3.281  -4.234  1.00   24.17 ? 233 GLY A C   1 
ATOM   1816 O  O   . GLY A 1 232 ? 3.784   -4.283  -4.425  1.00   21.40 ? 233 GLY A O   1 
ATOM   1817 N  N   . GLU A 1 233 ? 2.246   -2.794  -5.154  1.00   26.47 ? 234 GLU A N   1 
ATOM   1818 C  CA  . GLU A 1 233 ? 2.130   -3.423  -6.483  1.00   28.70 ? 234 GLU A CA  1 
ATOM   1819 C  C   . GLU A 1 233 ? 3.494   -3.600  -7.153  1.00   27.85 ? 234 GLU A C   1 
ATOM   1820 O  O   . GLU A 1 233 ? 4.295   -2.686  -7.138  1.00   25.06 ? 234 GLU A O   1 
ATOM   1821 C  CB  . GLU A 1 233 ? 1.204   -2.602  -7.392  1.00   29.92 ? 234 GLU A CB  1 
ATOM   1822 C  CG  . GLU A 1 233 ? 0.866   -3.312  -8.698  1.00   28.89 ? 234 GLU A CG  1 
ATOM   1823 C  CD  . GLU A 1 233 ? 0.047   -2.474  -9.645  1.00   32.70 ? 234 GLU A CD  1 
ATOM   1824 O  OE1 . GLU A 1 233 ? -0.323  -1.300  -9.299  1.00   31.20 ? 234 GLU A OE1 1 
ATOM   1825 O  OE2 . GLU A 1 233 ? -0.197  -2.996  -10.761 1.00   31.93 ? 234 GLU A OE2 1 
ATOM   1826 N  N   . GLY A 1 234 ? 3.732   -4.771  -7.752  1.00   30.30 ? 235 GLY A N   1 
ATOM   1827 C  CA  . GLY A 1 234 ? 5.021   -5.067  -8.374  1.00   36.19 ? 235 GLY A CA  1 
ATOM   1828 C  C   . GLY A 1 234 ? 6.243   -5.204  -7.478  1.00   38.80 ? 235 GLY A C   1 
ATOM   1829 O  O   . GLY A 1 234 ? 7.361   -5.254  -7.970  1.00   36.10 ? 235 GLY A O   1 
ATOM   1830 N  N   . GLU A 1 235 ? 6.050   -5.229  -6.161  1.00   42.10 ? 236 GLU A N   1 
ATOM   1831 C  CA  . GLU A 1 235 ? 7.054   -5.808  -5.249  1.00   41.49 ? 236 GLU A CA  1 
ATOM   1832 C  C   . GLU A 1 235 ? 6.646   -7.263  -4.954  1.00   35.43 ? 236 GLU A C   1 
ATOM   1833 O  O   . GLU A 1 235 ? 5.511   -7.638  -5.226  1.00   34.05 ? 236 GLU A O   1 
ATOM   1834 C  CB  . GLU A 1 235 ? 7.121   -5.033  -3.942  1.00   47.99 ? 236 GLU A CB  1 
ATOM   1835 C  CG  . GLU A 1 235 ? 7.499   -3.577  -4.046  1.00   56.60 ? 236 GLU A CG  1 
ATOM   1836 C  CD  . GLU A 1 235 ? 7.242   -2.843  -2.732  1.00   72.54 ? 236 GLU A CD  1 
ATOM   1837 O  OE1 . GLU A 1 235 ? 6.595   -3.427  -1.819  1.00   81.86 ? 236 GLU A OE1 1 
ATOM   1838 O  OE2 . GLU A 1 235 ? 7.680   -1.676  -2.599  1.00   77.00 ? 236 GLU A OE2 1 
ATOM   1839 N  N   . PRO A 1 236 ? 7.562   -8.094  -4.406  1.00   34.53 ? 237 PRO A N   1 
ATOM   1840 C  CA  . PRO A 1 236 ? 7.201   -9.496  -4.122  1.00   34.42 ? 237 PRO A CA  1 
ATOM   1841 C  C   . PRO A 1 236 ? 6.008   -9.693  -3.133  1.00   32.70 ? 237 PRO A C   1 
ATOM   1842 O  O   . PRO A 1 236 ? 5.759   -8.846  -2.281  1.00   30.75 ? 237 PRO A O   1 
ATOM   1843 C  CB  . PRO A 1 236 ? 8.495   -10.124 -3.570  1.00   35.61 ? 237 PRO A CB  1 
ATOM   1844 C  CG  . PRO A 1 236 ? 9.542   -9.055  -3.553  1.00   38.69 ? 237 PRO A CG  1 
ATOM   1845 C  CD  . PRO A 1 236 ? 9.007   -7.824  -4.242  1.00   37.42 ? 237 PRO A CD  1 
ATOM   1846 N  N   . GLU A 1 237 ? 5.273   -10.799 -3.286  1.00   30.13 ? 238 GLU A N   1 
ATOM   1847 C  CA  . GLU A 1 237 ? 3.992   -10.967 -2.621  1.00   29.43 ? 238 GLU A CA  1 
ATOM   1848 C  C   . GLU A 1 237 ? 4.163   -11.464 -1.176  1.00   27.69 ? 238 GLU A C   1 
ATOM   1849 O  O   . GLU A 1 237 ? 4.668   -12.533 -0.920  1.00   24.46 ? 238 GLU A O   1 
ATOM   1850 C  CB  . GLU A 1 237 ? 3.053   -11.871 -3.418  1.00   28.53 ? 238 GLU A CB  1 
ATOM   1851 C  CG  . GLU A 1 237 ? 1.597   -11.532 -3.185  1.00   32.55 ? 238 GLU A CG  1 
ATOM   1852 C  CD  . GLU A 1 237 ? 0.592   -12.599 -3.632  1.00   32.39 ? 238 GLU A CD  1 
ATOM   1853 O  OE1 . GLU A 1 237 ? 1.017   -13.643 -4.177  1.00   35.72 ? 238 GLU A OE1 1 
ATOM   1854 O  OE2 . GLU A 1 237 ? -0.637  -12.386 -3.411  1.00   26.95 ? 238 GLU A OE2 1 
ATOM   1855 N  N   . GLU A 1 238 ? 3.714   -10.648 -0.236  1.00   26.61 ? 239 GLU A N   1 
ATOM   1856 C  CA  . GLU A 1 238 ? 3.767   -11.015 1.161   1.00   26.10 ? 239 GLU A CA  1 
ATOM   1857 C  C   . GLU A 1 238 ? 2.293   -10.945 1.617   1.00   21.33 ? 239 GLU A C   1 
ATOM   1858 O  O   . GLU A 1 238 ? 1.688   -9.897  1.503   1.00   17.68 ? 239 GLU A O   1 
ATOM   1859 C  CB  . GLU A 1 238 ? 4.642   -9.965  1.828   1.00   31.05 ? 239 GLU A CB  1 
ATOM   1860 C  CG  . GLU A 1 238 ? 4.977   -10.312 3.253   1.00   45.89 ? 239 GLU A CG  1 
ATOM   1861 C  CD  . GLU A 1 238 ? 5.828   -11.569 3.347   1.00   56.30 ? 239 GLU A CD  1 
ATOM   1862 O  OE1 . GLU A 1 238 ? 7.045   -11.472 3.018   1.00   61.40 ? 239 GLU A OE1 1 
ATOM   1863 O  OE2 . GLU A 1 238 ? 5.278   -12.629 3.762   1.00   52.64 ? 239 GLU A OE2 1 
ATOM   1864 N  N   . LEU A 1 239 ? 1.666   -12.062 1.976   1.00   19.22 ? 240 LEU A N   1 
ATOM   1865 C  CA  . LEU A 1 239 ? 0.200   -12.010 2.189   1.00   17.38 ? 240 LEU A CA  1 
ATOM   1866 C  C   . LEU A 1 239 ? -0.072  -11.153 3.462   1.00   17.22 ? 240 LEU A C   1 
ATOM   1867 O  O   . LEU A 1 239 ? 0.705   -11.240 4.401   1.00   17.14 ? 240 LEU A O   1 
ATOM   1868 C  CB  . LEU A 1 239 ? -0.349  -13.396 2.388   1.00   18.22 ? 240 LEU A CB  1 
ATOM   1869 C  CG  . LEU A 1 239 ? -0.403  -14.304 1.164   1.00   18.70 ? 240 LEU A CG  1 
ATOM   1870 C  CD1 . LEU A 1 239 ? -1.163  -15.580 1.570   1.00   19.65 ? 240 LEU A CD1 1 
ATOM   1871 C  CD2 . LEU A 1 239 ? -1.101  -13.577 0.025   1.00   19.27 ? 240 LEU A CD2 1 
ATOM   1872 N  N   . MET A 1 240 ? -1.099  -10.300 3.471   1.00   15.75 ? 241 MET A N   1 
ATOM   1873 C  CA  . MET A 1 240 ? -1.443  -9.540  4.713   1.00   15.08 ? 241 MET A CA  1 
ATOM   1874 C  C   . MET A 1 240 ? -2.166  -10.512 5.651   1.00   13.92 ? 241 MET A C   1 
ATOM   1875 O  O   . MET A 1 240 ? -3.385  -10.739 5.476   1.00   13.26 ? 241 MET A O   1 
ATOM   1876 C  CB  . MET A 1 240 ? -2.335  -8.339  4.390   1.00   14.70 ? 241 MET A CB  1 
ATOM   1877 C  CG  . MET A 1 240 ? -2.540  -7.359  5.559   1.00   15.09 ? 241 MET A CG  1 
ATOM   1878 S  SD  . MET A 1 240 ? -3.533  -5.992  4.985   1.00   17.85 ? 241 MET A SD  1 
ATOM   1879 C  CE  . MET A 1 240 ? -2.269  -4.956  4.269   1.00   17.50 ? 241 MET A CE  1 
ATOM   1880 N  N   . VAL A 1 241 ? -1.394  -11.158 6.531   1.00   13.77 ? 242 VAL A N   1 
ATOM   1881 C  CA  . VAL A 1 241 ? -1.924  -12.044 7.554   1.00   15.22 ? 242 VAL A CA  1 
ATOM   1882 C  C   . VAL A 1 241 ? -1.159  -11.824 8.866   1.00   15.34 ? 242 VAL A C   1 
ATOM   1883 O  O   . VAL A 1 241 ? 0.026   -11.442 8.869   1.00   16.95 ? 242 VAL A O   1 
ATOM   1884 C  CB  . VAL A 1 241 ? -1.842  -13.603 7.201   1.00   15.30 ? 242 VAL A CB  1 
ATOM   1885 C  CG1 . VAL A 1 241 ? -2.704  -13.914 5.961   1.00   17.06 ? 242 VAL A CG1 1 
ATOM   1886 C  CG2 . VAL A 1 241 ? -0.390  -14.066 6.985   1.00   17.41 ? 242 VAL A CG2 1 
ATOM   1887 N  N   . ASP A 1 242 ? -1.801  -12.194 9.958   1.00   12.67 ? 243 ASP A N   1 
ATOM   1888 C  CA  . ASP A 1 242 ? -1.226  -11.987 11.285  1.00   14.37 ? 243 ASP A CA  1 
ATOM   1889 C  C   . ASP A 1 242 ? -0.778  -10.563 11.548  1.00   12.82 ? 243 ASP A C   1 
ATOM   1890 O  O   . ASP A 1 242 ? 0.348   -10.399 12.028  1.00   12.92 ? 243 ASP A O   1 
ATOM   1891 C  CB  . ASP A 1 242 ? -0.071  -12.985 11.614  1.00   14.09 ? 243 ASP A CB  1 
ATOM   1892 C  CG  . ASP A 1 242 ? -0.566  -14.450 11.663  1.00   14.32 ? 243 ASP A CG  1 
ATOM   1893 O  OD1 . ASP A 1 242 ? -1.657  -14.728 12.198  1.00   12.27 ? 243 ASP A OD1 1 
ATOM   1894 O  OD2 . ASP A 1 242 ? 0.116   -15.318 11.108  1.00   16.12 ? 243 ASP A OD2 1 
ATOM   1895 N  N   . ASN A 1 243 ? -1.647  -9.566  11.267  1.00   12.34 ? 244 ASN A N   1 
ATOM   1896 C  CA  . ASN A 1 243 ? -1.233  -8.173  11.487  1.00   12.36 ? 244 ASN A CA  1 
ATOM   1897 C  C   . ASN A 1 243 ? -1.772  -7.744  12.872  1.00   12.57 ? 244 ASN A C   1 
ATOM   1898 O  O   . ASN A 1 243 ? -2.436  -6.703  12.985  1.00   12.62 ? 244 ASN A O   1 
ATOM   1899 C  CB  . ASN A 1 243 ? -1.777  -7.264  10.371  1.00   12.40 ? 244 ASN A CB  1 
ATOM   1900 C  CG  . ASN A 1 243 ? -3.281  -7.430  10.126  1.00   14.54 ? 244 ASN A CG  1 
ATOM   1901 O  OD1 . ASN A 1 243 ? -3.936  -8.367  10.633  1.00   15.00 ? 244 ASN A OD1 1 
ATOM   1902 N  ND2 . ASN A 1 243 ? -3.858  -6.478  9.358   1.00   14.87 ? 244 ASN A ND2 1 
ATOM   1903 N  N   . TRP A 1 244 ? -1.512  -8.555  13.901  1.00   11.37 ? 245 TRP A N   1 
ATOM   1904 C  CA  . TRP A 1 244 ? -1.971  -8.256  15.252  1.00   10.81 ? 245 TRP A CA  1 
ATOM   1905 C  C   . TRP A 1 244 ? -0.798  -8.168  16.177  1.00   11.41 ? 245 TRP A C   1 
ATOM   1906 O  O   . TRP A 1 244 ? 0.266   -8.846  16.003  1.00   11.36 ? 245 TRP A O   1 
ATOM   1907 C  CB  . TRP A 1 244 ? -2.970  -9.348  15.740  1.00   11.39 ? 245 TRP A CB  1 
ATOM   1908 C  CG  . TRP A 1 244 ? -2.471  -10.759 15.526  1.00   11.26 ? 245 TRP A CG  1 
ATOM   1909 C  CD1 . TRP A 1 244 ? -2.501  -11.519 14.346  1.00   11.20 ? 245 TRP A CD1 1 
ATOM   1910 C  CD2 . TRP A 1 244 ? -1.923  -11.640 16.535  1.00   11.35 ? 245 TRP A CD2 1 
ATOM   1911 N  NE1 . TRP A 1 244 ? -2.005  -12.805 14.572  1.00   10.76 ? 245 TRP A NE1 1 
ATOM   1912 C  CE2 . TRP A 1 244 ? -1.637  -12.923 15.867  1.00   11.65 ? 245 TRP A CE2 1 
ATOM   1913 C  CE3 . TRP A 1 244 ? -1.675  -11.519 17.912  1.00   11.41 ? 245 TRP A CE3 1 
ATOM   1914 C  CZ2 . TRP A 1 244 ? -1.083  -14.004 16.559  1.00   11.55 ? 245 TRP A CZ2 1 
ATOM   1915 C  CZ3 . TRP A 1 244 ? -1.085  -12.601 18.573  1.00   12.15 ? 245 TRP A CZ3 1 
ATOM   1916 C  CH2 . TRP A 1 244 ? -0.797  -13.821 17.898  1.00   12.53 ? 245 TRP A CH2 1 
ATOM   1917 N  N   . ARG A 1 245 ? -0.956  -7.314  17.173  1.00   10.87 ? 246 ARG A N   1 
ATOM   1918 C  CA  . ARG A 1 245 ? -0.015  -7.202  18.254  1.00   11.40 ? 246 ARG A CA  1 
ATOM   1919 C  C   . ARG A 1 245 ? -0.459  -8.093  19.373  1.00   11.48 ? 246 ARG A C   1 
ATOM   1920 O  O   . ARG A 1 245 ? -1.656  -8.160  19.720  1.00   12.76 ? 246 ARG A O   1 
ATOM   1921 C  CB  . ARG A 1 245 ? 0.022   -5.742  18.787  1.00   11.07 ? 246 ARG A CB  1 
ATOM   1922 C  CG  . ARG A 1 245 ? 1.193   -5.545  19.741  1.00   11.12 ? 246 ARG A CG  1 
ATOM   1923 C  CD  . ARG A 1 245 ? 1.073   -4.231  20.525  1.00   11.05 ? 246 ARG A CD  1 
ATOM   1924 N  NE  . ARG A 1 245 ? 2.340   -3.906  21.205  1.00   11.08 ? 246 ARG A NE  1 
ATOM   1925 C  CZ  . ARG A 1 245 ? 2.508   -2.862  22.020  1.00   11.87 ? 246 ARG A CZ  1 
ATOM   1926 N  NH1 . ARG A 1 245 ? 1.497   -2.037  22.320  1.00   12.89 ? 246 ARG A NH1 1 
ATOM   1927 N  NH2 . ARG A 1 245 ? 3.687   -2.596  22.513  1.00   12.05 ? 246 ARG A NH2 1 
ATOM   1928 N  N   . PRO A 1 246 ? 0.495   -8.834  19.985  1.00   13.60 ? 247 PRO A N   1 
ATOM   1929 C  CA  . PRO A 1 246 ? 0.023   -9.669  21.075  1.00   13.17 ? 247 PRO A CA  1 
ATOM   1930 C  C   . PRO A 1 246 ? -0.339  -8.878  22.384  1.00   13.05 ? 247 PRO A C   1 
ATOM   1931 O  O   . PRO A 1 246 ? 0.044   -7.693  22.540  1.00   11.80 ? 247 PRO A O   1 
ATOM   1932 C  CB  . PRO A 1 246 ? 1.204   -10.643 21.308  1.00   15.41 ? 247 PRO A CB  1 
ATOM   1933 C  CG  . PRO A 1 246 ? 2.160   -10.448 20.130  1.00   16.30 ? 247 PRO A CG  1 
ATOM   1934 C  CD  . PRO A 1 246 ? 1.935   -9.025  19.720  1.00   14.41 ? 247 PRO A CD  1 
ATOM   1935 N  N   . ALA A 1 247 ? -0.990  -9.575  23.330  1.00   12.90 ? 248 ALA A N   1 
ATOM   1936 C  CA  . ALA A 1 247 ? -1.409  -8.999  24.601  1.00   13.29 ? 248 ALA A CA  1 
ATOM   1937 C  C   . ALA A 1 247 ? -0.191  -8.459  25.324  1.00   14.27 ? 248 ALA A C   1 
ATOM   1938 O  O   . ALA A 1 247 ? 0.878   -9.070  25.305  1.00   13.95 ? 248 ALA A O   1 
ATOM   1939 C  CB  . ALA A 1 247 ? -2.107  -10.061 25.481  1.00   12.61 ? 248 ALA A CB  1 
ATOM   1940 N  N   . GLN A 1 248 ? -0.360  -7.331  25.982  1.00   14.02 ? 249 GLN A N   1 
ATOM   1941 C  CA  . GLN A 1 248 ? 0.735   -6.646  26.654  1.00   13.86 ? 249 GLN A CA  1 
ATOM   1942 C  C   . GLN A 1 248 ? 0.445   -6.677  28.162  1.00   14.16 ? 249 GLN A C   1 
ATOM   1943 O  O   . GLN A 1 248 ? -0.685  -6.921  28.509  1.00   12.70 ? 249 GLN A O   1 
ATOM   1944 C  CB  . GLN A 1 248 ? 0.775   -5.205  26.157  1.00   13.51 ? 249 GLN A CB  1 
ATOM   1945 C  CG  . GLN A 1 248 ? 1.144   -5.112  24.676  1.00   13.46 ? 249 GLN A CG  1 
ATOM   1946 C  CD  . GLN A 1 248 ? 2.483   -5.737  24.394  1.00   13.83 ? 249 GLN A CD  1 
ATOM   1947 O  OE1 . GLN A 1 248 ? 3.454   -5.378  25.020  1.00   16.22 ? 249 GLN A OE1 1 
ATOM   1948 N  NE2 . GLN A 1 248 ? 2.540   -6.668  23.469  1.00   12.84 ? 249 GLN A NE2 1 
ATOM   1949 N  N   . PRO A 1 249 ? 1.473   -6.471  29.051  1.00   15.96 ? 250 PRO A N   1 
ATOM   1950 C  CA  . PRO A 1 249 ? 1.190   -6.526  30.498  1.00   16.36 ? 250 PRO A CA  1 
ATOM   1951 C  C   . PRO A 1 249 ? 0.157   -5.460  30.921  1.00   17.27 ? 250 PRO A C   1 
ATOM   1952 O  O   . PRO A 1 249 ? 0.276   -4.246  30.546  1.00   16.53 ? 250 PRO A O   1 
ATOM   1953 C  CB  . PRO A 1 249 ? 2.561   -6.229  31.140  1.00   16.63 ? 250 PRO A CB  1 
ATOM   1954 C  CG  . PRO A 1 249 ? 3.582   -6.474  30.089  1.00   18.06 ? 250 PRO A CG  1 
ATOM   1955 C  CD  . PRO A 1 249 ? 2.876   -6.087  28.812  1.00   16.43 ? 250 PRO A CD  1 
ATOM   1956 N  N   . LEU A 1 250 ? -0.803  -5.894  31.729  1.00   17.40 ? 251 LEU A N   1 
ATOM   1957 C  CA  . LEU A 1 250 ? -1.857  -5.025  32.260  1.00   18.42 ? 251 LEU A CA  1 
ATOM   1958 C  C   . LEU A 1 250 ? -1.302  -3.958  33.228  1.00   20.39 ? 251 LEU A C   1 
ATOM   1959 O  O   . LEU A 1 250 ? -1.816  -2.812  33.294  1.00   18.52 ? 251 LEU A O   1 
ATOM   1960 C  CB  . LEU A 1 250 ? -2.921  -5.855  32.998  1.00   19.65 ? 251 LEU A CB  1 
ATOM   1961 C  CG  . LEU A 1 250 ? -4.234  -5.131  33.324  1.00   18.62 ? 251 LEU A CG  1 
ATOM   1962 C  CD1 . LEU A 1 250 ? -4.829  -4.406  32.123  1.00   16.98 ? 251 LEU A CD1 1 
ATOM   1963 C  CD2 . LEU A 1 250 ? -5.199  -6.141  33.926  1.00   21.85 ? 251 LEU A CD2 1 
ATOM   1964 N  N   . LYS A 1 251 ? -0.276  -4.348  33.986  1.00   19.98 ? 252 LYS A N   1 
ATOM   1965 C  CA  . LYS A 1 251 ? 0.417   -3.414  34.887  1.00   21.93 ? 252 LYS A CA  1 
ATOM   1966 C  C   . LYS A 1 251 ? -0.595  -2.827  35.897  1.00   22.03 ? 252 LYS A C   1 
ATOM   1967 O  O   . LYS A 1 251 ? -1.475  -3.535  36.415  1.00   21.88 ? 252 LYS A O   1 
ATOM   1968 C  CB  . LYS A 1 251 ? 1.225   -2.365  34.116  1.00   21.72 ? 252 LYS A CB  1 
ATOM   1969 C  CG  . LYS A 1 251 ? 2.500   -2.955  33.457  1.00   23.15 ? 252 LYS A CG  1 
ATOM   1970 C  CD  . LYS A 1 251 ? 3.297   -1.909  32.700  1.00   23.39 ? 252 LYS A CD  1 
ATOM   1971 C  CE  . LYS A 1 251 ? 4.554   -2.545  32.084  1.00   25.53 ? 252 LYS A CE  1 
ATOM   1972 N  NZ  . LYS A 1 251 ? 5.308   -1.588  31.218  1.00   24.08 ? 252 LYS A NZ  1 
ATOM   1973 N  N   . ASN A 1 252 ? -0.510  -1.555  36.201  1.00   22.23 ? 253 ASN A N   1 
ATOM   1974 C  CA  . ASN A 1 252 ? -1.437  -1.077  37.223  1.00   29.60 ? 253 ASN A CA  1 
ATOM   1975 C  C   . ASN A 1 252 ? -2.699  -0.500  36.559  1.00   27.77 ? 253 ASN A C   1 
ATOM   1976 O  O   . ASN A 1 252 ? -2.847  0.750   36.567  1.00   26.61 ? 253 ASN A O   1 
ATOM   1977 C  CB  . ASN A 1 252 ? -0.789  -0.030  38.158  1.00   36.62 ? 253 ASN A CB  1 
ATOM   1978 C  CG  . ASN A 1 252 ? -1.755  0.430   39.273  1.00   45.00 ? 253 ASN A CG  1 
ATOM   1979 O  OD1 . ASN A 1 252 ? -2.268  -0.394  40.061  1.00   50.10 ? 253 ASN A OD1 1 
ATOM   1980 N  ND2 . ASN A 1 252 ? -2.024  1.751   39.327  1.00   42.44 ? 253 ASN A ND2 1 
ATOM   1981 N  N   . ARG A 1 253 ? -3.528  -1.391  35.951  1.00   21.48 ? 254 ARG A N   1 
ATOM   1982 C  CA  . ARG A 1 253 ? -4.842  -1.046  35.389  1.00   20.08 ? 254 ARG A CA  1 
ATOM   1983 C  C   . ARG A 1 253 ? -5.898  -2.079  35.808  1.00   21.11 ? 254 ARG A C   1 
ATOM   1984 O  O   . ARG A 1 253 ? -5.579  -3.244  35.946  1.00   22.66 ? 254 ARG A O   1 
ATOM   1985 C  CB  . ARG A 1 253 ? -4.818  -1.012  33.847  1.00   17.49 ? 254 ARG A CB  1 
ATOM   1986 C  CG  . ARG A 1 253 ? -3.944  0.098   33.269  1.00   14.80 ? 254 ARG A CG  1 
ATOM   1987 C  CD  . ARG A 1 253 ? -3.901  -0.022  31.737  1.00   13.59 ? 254 ARG A CD  1 
ATOM   1988 N  NE  . ARG A 1 253 ? -2.950  -1.072  31.272  1.00   12.15 ? 254 ARG A NE  1 
ATOM   1989 C  CZ  . ARG A 1 253 ? -2.625  -1.283  30.000  1.00   11.40 ? 254 ARG A CZ  1 
ATOM   1990 N  NH1 . ARG A 1 253 ? -3.242  -0.546  29.082  1.00   9.54  ? 254 ARG A NH1 1 
ATOM   1991 N  NH2 . ARG A 1 253 ? -1.757  -2.276  29.633  1.00   9.62  ? 254 ARG A NH2 1 
ATOM   1992 N  N   . GLN A 1 254 ? -7.150  -1.655  35.936  1.00   21.67 ? 255 GLN A N   1 
ATOM   1993 C  CA  . GLN A 1 254 ? -8.292  -2.559  36.228  1.00   24.57 ? 255 GLN A CA  1 
ATOM   1994 C  C   . GLN A 1 254 ? -9.216  -2.528  35.032  1.00   23.69 ? 255 GLN A C   1 
ATOM   1995 O  O   . GLN A 1 254 ? -9.565  -1.453  34.562  1.00   23.51 ? 255 GLN A O   1 
ATOM   1996 C  CB  . GLN A 1 254 ? -9.081  -2.060  37.443  1.00   28.87 ? 255 GLN A CB  1 
ATOM   1997 C  CG  . GLN A 1 254 ? -8.959  -3.012  38.615  1.00   39.26 ? 255 GLN A CG  1 
ATOM   1998 C  CD  . GLN A 1 254 ? -10.288 -3.271  39.334  1.00   44.96 ? 255 GLN A CD  1 
ATOM   1999 O  OE1 . GLN A 1 254 ? -11.207 -2.439  39.323  1.00   46.60 ? 255 GLN A OE1 1 
ATOM   2000 N  NE2 . GLN A 1 254 ? -10.391 -4.440  39.966  1.00   46.57 ? 255 GLN A NE2 1 
ATOM   2001 N  N   . ILE A 1 255 ? -9.593  -3.681  34.513  1.00   18.77 ? 256 ILE A N   1 
ATOM   2002 C  CA  . ILE A 1 255 ? -10.550 -3.688  33.434  1.00   17.85 ? 256 ILE A CA  1 
ATOM   2003 C  C   . ILE A 1 255 ? -11.947 -3.645  34.076  1.00   16.18 ? 256 ILE A C   1 
ATOM   2004 O  O   . ILE A 1 255 ? -12.218 -4.391  34.998  1.00   17.25 ? 256 ILE A O   1 
ATOM   2005 C  CB  . ILE A 1 255 ? -10.419 -4.937  32.536  1.00   17.41 ? 256 ILE A CB  1 
ATOM   2006 C  CG1 . ILE A 1 255 ? -8.971  -5.059  31.954  1.00   18.13 ? 256 ILE A CG1 1 
ATOM   2007 C  CG2 . ILE A 1 255 ? -11.563 -4.916  31.501  1.00   15.83 ? 256 ILE A CG2 1 
ATOM   2008 C  CD1 . ILE A 1 255 ? -8.736  -6.264  31.032  1.00   19.60 ? 256 ILE A CD1 1 
ATOM   2009 N  N   . LYS A 1 256 ? -12.799 -2.730  33.656  1.00   15.50 ? 257 LYS A N   1 
ATOM   2010 C  CA  . LYS A 1 256 ? -14.191 -2.676  34.189  1.00   16.33 ? 257 LYS A CA  1 
ATOM   2011 C  C   . LYS A 1 256 ? -15.164 -3.313  33.237  1.00   15.68 ? 257 LYS A C   1 
ATOM   2012 O  O   . LYS A 1 256 ? -14.944 -3.260  32.013  1.00   16.48 ? 257 LYS A O   1 
ATOM   2013 C  CB  . LYS A 1 256 ? -14.595 -1.225  34.423  1.00   19.38 ? 257 LYS A CB  1 
ATOM   2014 C  CG  . LYS A 1 256 ? -13.443 -0.442  35.002  1.00   24.69 ? 257 LYS A CG  1 
ATOM   2015 C  CD  . LYS A 1 256 ? -13.561 -0.252  36.487  1.00   29.71 ? 257 LYS A CD  1 
ATOM   2016 C  CE  . LYS A 1 256 ? -13.876 1.226   36.764  1.00   35.67 ? 257 LYS A CE  1 
ATOM   2017 N  NZ  . LYS A 1 256 ? -14.529 1.463   38.097  1.00   39.46 ? 257 LYS A NZ  1 
ATOM   2018 N  N   . ALA A 1 257 ? -16.220 -3.919  33.766  1.00   15.55 ? 258 ALA A N   1 
ATOM   2019 C  CA  . ALA A 1 257 ? -17.298 -4.455  32.958  1.00   15.20 ? 258 ALA A CA  1 
ATOM   2020 C  C   . ALA A 1 257 ? -18.580 -3.715  33.218  1.00   16.25 ? 258 ALA A C   1 
ATOM   2021 O  O   . ALA A 1 257 ? -18.937 -3.371  34.394  1.00   16.45 ? 258 ALA A O   1 
ATOM   2022 C  CB  . ALA A 1 257 ? -17.497 -5.961  33.102  1.00   14.44 ? 258 ALA A CB  1 
ATOM   2023 N  N   . SER A 1 258 ? -19.295 -3.495  32.113  1.00   16.46 ? 259 SER A N   1 
ATOM   2024 C  CA  . SER A 1 258 ? -20.630 -2.868  32.123  1.00   17.46 ? 259 SER A CA  1 
ATOM   2025 C  C   . SER A 1 258 ? -21.737 -3.844  32.516  1.00   18.53 ? 259 SER A C   1 
ATOM   2026 O  O   . SER A 1 258 ? -22.912 -3.459  32.561  1.00   20.23 ? 259 SER A O   1 
ATOM   2027 C  CB  . SER A 1 258 ? -20.971 -2.366  30.722  1.00   18.42 ? 259 SER A CB  1 
ATOM   2028 O  OG  . SER A 1 258 ? -21.521 -3.433  29.961  1.00   18.44 ? 259 SER A OG  1 
ATOM   2029 N  N   . PHE A 1 259 ? -21.372 -5.091  32.802  1.00   17.19 ? 260 PHE A N   1 
ATOM   2030 C  CA  . PHE A 1 259 ? -22.336 -6.181  32.904  1.00   19.55 ? 260 PHE A CA  1 
ATOM   2031 C  C   . PHE A 1 259 ? -21.878 -7.237  33.867  1.00   23.11 ? 260 PHE A C   1 
ATOM   2032 O  O   . PHE A 1 259 ? -20.685 -7.328  34.192  1.00   21.56 ? 260 PHE A O   1 
ATOM   2033 C  CB  . PHE A 1 259 ? -22.582 -6.864  31.543  1.00   18.61 ? 260 PHE A CB  1 
ATOM   2034 C  CG  . PHE A 1 259 ? -21.360 -7.612  31.008  1.00   20.61 ? 260 PHE A CG  1 
ATOM   2035 C  CD1 . PHE A 1 259 ? -20.345 -6.926  30.315  1.00   19.68 ? 260 PHE A CD1 1 
ATOM   2036 C  CD2 . PHE A 1 259 ? -21.176 -8.987  31.292  1.00   21.08 ? 260 PHE A CD2 1 
ATOM   2037 C  CE1 . PHE A 1 259 ? -19.230 -7.616  29.877  1.00   21.40 ? 260 PHE A CE1 1 
ATOM   2038 C  CE2 . PHE A 1 259 ? -20.051 -9.654  30.860  1.00   23.33 ? 260 PHE A CE2 1 
ATOM   2039 C  CZ  . PHE A 1 259 ? -19.090 -8.969  30.122  1.00   21.84 ? 260 PHE A CZ  1 
ATOM   2040 N  N   . LYS A 1 260 ? -22.903 -7.973  34.311  1.00   28.89 ? 261 LYS A N   1 
ATOM   2041 C  CA  . LYS A 1 260 ? -22.935 -9.284  35.007  1.00   39.80 ? 261 LYS A CA  1 
ATOM   2042 C  C   . LYS A 1 260 ? -22.215 -9.449  36.310  1.00   45.66 ? 261 LYS A C   1 
ATOM   2043 O  O   . LYS A 1 260 ? -22.582 -8.831  37.315  1.00   52.65 ? 261 LYS A O   1 
ATOM   2044 C  CB  . LYS A 1 260 ? -22.660 -10.474 34.066  1.00   35.68 ? 261 LYS A CB  1 
ATOM   2045 C  CG  . LYS A 1 260 ? -23.834 -10.848 33.169  1.00   34.15 ? 261 LYS A CG  1 
ATOM   2046 C  CD  . LYS A 1 260 ? -23.458 -11.767 32.102  0.0000 51.89 ? 261 LYS A CD  1 
ATOM   2047 C  CE  . LYS A 1 260 ? -24.616 -12.451 31.371  0.0000 60.45 ? 261 LYS A CE  1 
ATOM   2048 N  NZ  . LYS A 1 260 ? -25.023 -13.744 32.007  0.0000 56.08 ? 261 LYS A NZ  1 
ATOM   2049 O  OXT . LYS A 1 260 ? -21.286 -10.255 36.371  1.00   62.12 ? 261 LYS A OXT 1 
HETATM 2050 ZN ZN  . ZN  B 2 .   ? -6.575  -1.731  15.269  1.00   10.54 ? 301 ZN  A ZN  1 
HETATM 2051 O  O1  . MES C 3 .   ? -7.470  -9.219  -3.109  1.00   32.17 ? 302 MES A O1  1 
HETATM 2052 C  C2  . MES C 3 .   ? -7.544  -10.334 -4.074  1.00   30.10 ? 302 MES A C2  1 
HETATM 2053 C  C3  . MES C 3 .   ? -8.828  -11.262 -4.033  1.00   32.79 ? 302 MES A C3  1 
HETATM 2054 N  N4  . MES C 3 .   ? -9.955  -10.838 -3.198  1.00   36.80 ? 302 MES A N4  1 
HETATM 2055 C  C5  . MES C 3 .   ? -9.525  -10.243 -1.898  1.00   30.93 ? 302 MES A C5  1 
HETATM 2056 C  C6  . MES C 3 .   ? -8.207  -9.538  -1.909  1.00   28.16 ? 302 MES A C6  1 
HETATM 2057 C  C7  . MES C 3 .   ? -11.457 -11.009 -3.538  1.00   40.93 ? 302 MES A C7  1 
HETATM 2058 C  C8  . MES C 3 .   ? -12.556 -9.777  -3.552  1.00   51.44 ? 302 MES A C8  1 
HETATM 2059 S  S   . MES C 3 .   ? -13.591 -9.404  -5.008  1.00   69.09 ? 302 MES A S   1 
HETATM 2060 O  O1S . MES C 3 .   ? -14.087 -8.145  -5.341  1.00   49.50 ? 302 MES A O1S 1 
HETATM 2061 O  O2S . MES C 3 .   ? -13.051 -10.033 -6.188  1.00   59.39 ? 302 MES A O2S 1 
HETATM 2062 O  O3S . MES C 3 .   ? -14.977 -9.919  -4.661  1.00   70.36 ? 302 MES A O3S 1 
HETATM 2063 S  S   . DMS D 4 .   ? 1.595   -11.655 14.991  1.00   33.66 ? 303 DMS A S   1 
HETATM 2064 O  O   . DMS D 4 .   ? 2.028   -12.998 14.542  1.00   28.83 ? 303 DMS A O   1 
HETATM 2065 C  C1  . DMS D 4 .   ? 2.223   -11.599 16.596  1.00   26.54 ? 303 DMS A C1  1 
HETATM 2066 C  C2  . DMS D 4 .   ? 2.601   -10.468 14.277  1.00   28.46 ? 303 DMS A C2  1 
HETATM 2067 NA NA  . NA  E 5 .   ? -17.915 -21.883 6.016   1.00   26.87 ? 304 NA  A NA  1 
HETATM 2068 O  O7  A EWZ F 6 .   ? 2.204   4.681   10.594  0.010  23.35 ? 305 EWZ A O7  1 
HETATM 2069 O  O7  B EWZ F 6 .   ? -5.018  8.979   10.765  0.010  37.36 ? 305 EWZ A O7  1 
HETATM 2070 C  C2  A EWZ F 6 .   ? 1.015   4.550   10.870  0.010  23.29 ? 305 EWZ A C2  1 
HETATM 2071 C  C2  B EWZ F 6 .   ? -4.238  8.082   11.041  0.010  37.63 ? 305 EWZ A C2  1 
HETATM 2072 C  C3  A EWZ F 6 .   ? 0.244   5.609   11.513  0.010  23.26 ? 305 EWZ A C3  1 
HETATM 2073 C  C3  B EWZ F 6 .   ? -3.110  8.288   11.925  0.010  37.29 ? 305 EWZ A C3  1 
HETATM 2074 C  C4  A EWZ F 6 .   ? -1.032  5.324   11.750  0.010  23.13 ? 305 EWZ A C4  1 
HETATM 2075 C  C4  B EWZ F 6 .   ? -2.356  7.225   12.135  0.010  37.03 ? 305 EWZ A C4  1 
HETATM 2076 C  C8  A EWZ F 6 .   ? -1.871  6.335   12.393  0.010  23.04 ? 305 EWZ A C8  1 
HETATM 2077 C  C8  B EWZ F 6 .   ? -1.208  7.352   13.012  0.010  36.31 ? 305 EWZ A C8  1 
HETATM 2078 C  C15 A EWZ F 6 .   ? -2.881  7.065   11.489  0.010  22.92 ? 305 EWZ A C15 1 
HETATM 2079 C  C15 B EWZ F 6 .   ? -1.594  7.458   14.495  0.010  35.04 ? 305 EWZ A C15 1 
HETATM 2080 C  C14 A EWZ F 6 .   ? -0.846  7.317   13.094  0.010  22.84 ? 305 EWZ A C14 1 
HETATM 2081 C  C14 B EWZ F 6 .   ? -0.399  8.562   12.519  0.010  36.08 ? 305 EWZ A C14 1 
HETATM 2082 C  C9  A EWZ F 6 .   ? -2.492  5.475   13.542  0.010  22.96 ? 305 EWZ A C9  1 
HETATM 2083 C  C9  B EWZ F 6 .   ? -0.427  6.079   12.650  0.010  35.53 ? 305 EWZ A C9  1 
HETATM 2084 N  N5  A EWZ F 6 .   ? -1.628  4.110   11.424  0.010  23.35 ? 305 EWZ A N5  1 
HETATM 2085 N  N5  B EWZ F 6 .   ? -2.588  5.981   11.564  0.010  38.17 ? 305 EWZ A N5  1 
HETATM 2086 N  N1  A EWZ F 6 .   ? 0.383   3.361   10.563  0.010  23.42 ? 305 EWZ A N1  1 
HETATM 2087 N  N1  B EWZ F 6 .   ? -4.433  6.832   10.496  0.010  38.41 ? 305 EWZ A N1  1 
HETATM 2088 C  C6  A EWZ F 6 .   ? -0.984  3.175   10.867  0.50   22.95 ? 305 EWZ A C6  1 
HETATM 2089 C  C6  B EWZ F 6 .   ? -3.566  5.775   10.806  0.50   39.46 ? 305 EWZ A C6  1 
HETATM 2090 S  S10 A EWZ F 6 .   ? -1.862  1.698   10.512  0.50   25.45 ? 305 EWZ A S10 1 
HETATM 2091 S  S10 B EWZ F 6 .   ? -3.735  4.177   10.132  0.50   41.07 ? 305 EWZ A S10 1 
HETATM 2092 C  C11 A EWZ F 6 .   ? -3.057  1.443   11.840  0.50   20.19 ? 305 EWZ A C11 1 
HETATM 2093 C  C11 B EWZ F 6 .   ? -4.355  2.846   11.145  0.50   40.91 ? 305 EWZ A C11 1 
HETATM 2094 C  C12 A EWZ F 6 .   ? -4.103  2.545   12.058  0.50   18.27 ? 305 EWZ A C12 1 
HETATM 2095 C  C12 B EWZ F 6 .   ? -3.738  2.567   12.517  0.50   39.06 ? 305 EWZ A C12 1 
HETATM 2096 O  O13 A EWZ F 6 .   ? -4.362  3.264   11.093  0.50   19.17 ? 305 EWZ A O13 1 
HETATM 2097 O  O13 B EWZ F 6 .   ? -2.679  1.979   12.604  0.50   38.67 ? 305 EWZ A O13 1 
HETATM 2098 C  C16 A EWZ F 6 .   ? -4.806  2.885   13.357  0.50   16.00 ? 305 EWZ A C16 1 
HETATM 2099 C  C16 B EWZ F 6 .   ? -4.467  2.987   13.741  0.50   37.10 ? 305 EWZ A C16 1 
HETATM 2100 C  C21 A EWZ F 6 .   ? -5.306  4.180   13.649  0.50   15.04 ? 305 EWZ A C21 1 
HETATM 2101 C  C21 B EWZ F 6 .   ? -4.855  4.306   14.016  0.50   36.54 ? 305 EWZ A C21 1 
HETATM 2102 C  C20 A EWZ F 6 .   ? -5.918  4.445   14.835  0.50   13.68 ? 305 EWZ A C20 1 
HETATM 2103 C  C20 B EWZ F 6 .   ? -5.545  4.578   15.157  0.50   34.72 ? 305 EWZ A C20 1 
HETATM 2104 C  C19 A EWZ F 6 .   ? -6.047  3.415   15.757  0.50   13.32 ? 305 EWZ A C19 1 
HETATM 2105 C  C19 B EWZ F 6 .   ? -5.854  3.547   16.031  0.50   34.09 ? 305 EWZ A C19 1 
HETATM 2106 CL CL  A EWZ F 6 .   ? -6.807  3.742   17.239  0.50   13.83 ? 305 EWZ A CL  1 
HETATM 2107 CL CL  B EWZ F 6 .   ? -6.707  3.910   17.459  0.50   36.15 ? 305 EWZ A CL  1 
HETATM 2108 C  C17 A EWZ F 6 .   ? -4.945  1.903   14.316  0.50   14.55 ? 305 EWZ A C17 1 
HETATM 2109 C  C17 B EWZ F 6 .   ? -4.790  1.981   14.618  0.50   34.20 ? 305 EWZ A C17 1 
HETATM 2110 C  C18 A EWZ F 6 .   ? -5.544  2.154   15.518  0.50   12.90 ? 305 EWZ A C18 1 
HETATM 2111 C  C18 B EWZ F 6 .   ? -5.467  2.250   15.767  0.50   32.27 ? 305 EWZ A C18 1 
HETATM 2112 S  S22 A EWZ F 6 .   ? -5.780  0.783   16.694  0.50   13.05 ? 305 EWZ A S22 1 
HETATM 2113 S  S22 B EWZ F 6 .   ? -5.853  0.859   16.844  0.50   33.86 ? 305 EWZ A S22 1 
HETATM 2114 O  O23 A EWZ F 6 .   ? -5.152  1.104   18.019  0.50   11.72 ? 305 EWZ A O23 1 
HETATM 2115 O  O23 B EWZ F 6 .   ? -5.418  1.182   18.233  0.50   29.85 ? 305 EWZ A O23 1 
HETATM 2116 O  O25 A EWZ F 6 .   ? -7.200  0.787   16.781  0.50   11.12 ? 305 EWZ A O25 1 
HETATM 2117 O  O25 B EWZ F 6 .   ? -7.280  0.763   16.834  0.50   29.64 ? 305 EWZ A O25 1 
HETATM 2118 N  N26 A EWZ F 6 .   ? -4.928  -0.549  16.022  0.50   10.95 ? 305 EWZ A N26 1 
HETATM 2119 N  N26 B EWZ F 6 .   ? -4.822  -0.384  16.228  0.50   27.59 ? 305 EWZ A N26 1 
HETATM 2120 O  O   . HOH G 7 .   ? -4.393  -13.532 17.915  1.00   9.39  ? 401 HOH A O   1 
HETATM 2121 O  O   . HOH G 7 .   ? -17.011 -8.538  20.532  1.00   11.49 ? 402 HOH A O   1 
HETATM 2122 O  O   . HOH G 7 .   ? -21.472 -7.252  23.551  1.00   10.19 ? 403 HOH A O   1 
HETATM 2123 O  O   . HOH G 7 .   ? -1.120  -4.065  15.693  1.00   10.10 ? 404 HOH A O   1 
HETATM 2124 O  O   . HOH G 7 .   ? -2.616  -8.831  29.145  1.00   13.21 ? 405 HOH A O   1 
HETATM 2125 O  O   . HOH G 7 .   ? -7.775  -15.424 11.170  1.00   10.25 ? 406 HOH A O   1 
HETATM 2126 O  O   . HOH G 7 .   ? -21.926 5.665   4.816   1.00   15.24 ? 407 HOH A O   1 
HETATM 2127 O  O   . HOH G 7 .   ? -10.637 8.629   25.684  1.00   14.40 ? 408 HOH A O   1 
HETATM 2128 O  O   . HOH G 7 .   ? -3.448  -13.302 25.192  1.00   11.39 ? 409 HOH A O   1 
HETATM 2129 O  O   . HOH G 7 .   ? 3.719   4.858   29.852  1.00   20.00 ? 410 HOH A O   1 
HETATM 2130 O  O   . HOH G 7 .   ? -16.370 -10.003 32.972  1.00   16.92 ? 411 HOH A O   1 
HETATM 2131 O  O   . HOH G 7 .   ? -3.725  -15.955 24.336  1.00   13.35 ? 412 HOH A O   1 
HETATM 2132 O  O   . HOH G 7 .   ? -21.252 7.645   1.861   1.00   18.58 ? 413 HOH A O   1 
HETATM 2133 O  O   . HOH G 7 .   ? -14.127 10.617  27.779  1.00   20.23 ? 414 HOH A O   1 
HETATM 2134 O  O   . HOH G 7 .   ? 4.944   -5.014  20.978  1.00   11.23 ? 415 HOH A O   1 
HETATM 2135 O  O   . HOH G 7 .   ? -3.399  -11.199 20.725  1.00   11.27 ? 416 HOH A O   1 
HETATM 2136 O  O   . HOH G 7 .   ? -22.689 -5.823  2.920   1.00   18.54 ? 417 HOH A O   1 
HETATM 2137 O  O   . HOH G 7 .   ? 1.282   -1.679  29.516  1.00   20.43 ? 418 HOH A O   1 
HETATM 2138 O  O   . HOH G 7 .   ? 8.049   -5.834  -10.704 1.00   25.09 ? 419 HOH A O   1 
HETATM 2139 O  O   . HOH G 7 .   ? 8.590   -4.096  21.213  1.00   21.56 ? 420 HOH A O   1 
HETATM 2140 O  O   . HOH G 7 .   ? -24.868 -7.869  9.114   1.00   15.06 ? 421 HOH A O   1 
HETATM 2141 O  O   . HOH G 7 .   ? -1.926  -12.292 22.882  1.00   17.05 ? 422 HOH A O   1 
HETATM 2142 O  O   . HOH G 7 .   ? -19.345 10.134  8.898   1.00   19.07 ? 423 HOH A O   1 
HETATM 2143 O  O   . HOH G 7 .   ? -23.042 -3.006  6.935   1.00   21.10 ? 424 HOH A O   1 
HETATM 2144 O  O   . HOH G 7 .   ? -2.507  -3.217  11.478  1.00   16.55 ? 425 HOH A O   1 
HETATM 2145 O  O   . HOH G 7 .   ? -9.713  -8.396  33.985  1.00   23.87 ? 426 HOH A O   1 
HETATM 2146 O  O   . HOH G 7 .   ? -28.708 0.211   24.401  1.00   24.03 ? 427 HOH A O   1 
HETATM 2147 O  O   . HOH G 7 .   ? -23.067 -11.699 14.277  1.00   18.66 ? 428 HOH A O   1 
HETATM 2148 O  O   . HOH G 7 .   ? 7.753   6.152   21.942  1.00   16.96 ? 429 HOH A O   1 
HETATM 2149 O  O   . HOH G 7 .   ? -10.912 -19.351 6.914   1.00   22.49 ? 430 HOH A O   1 
HETATM 2150 O  O   . HOH G 7 .   ? -7.966  -19.263 21.600  1.00   23.31 ? 431 HOH A O   1 
HETATM 2151 O  O   . HOH G 7 .   ? -22.077 -18.591 13.726  1.00   27.57 ? 432 HOH A O   1 
HETATM 2152 O  O   . HOH G 7 .   ? -28.512 -5.990  25.017  1.00   25.99 ? 433 HOH A O   1 
HETATM 2153 O  O   . HOH G 7 .   ? -23.868 -0.964  4.188   1.00   25.81 ? 434 HOH A O   1 
HETATM 2154 O  O   . HOH G 7 .   ? -17.957 10.413  11.421  1.00   20.67 ? 435 HOH A O   1 
HETATM 2155 O  O   . HOH G 7 .   ? -23.976 -0.756  26.457  1.00   18.25 ? 436 HOH A O   1 
HETATM 2156 O  O   . HOH G 7 .   ? -10.880 -15.243 33.825  1.00   32.48 ? 437 HOH A O   1 
HETATM 2157 O  O   . HOH G 7 .   ? 2.678   -12.948 5.092   1.00   27.21 ? 438 HOH A O   1 
HETATM 2158 O  O   . HOH G 7 .   ? -7.061  -16.808 1.312   1.00   25.84 ? 439 HOH A O   1 
HETATM 2159 O  O   . HOH G 7 .   ? 4.473   -3.619  26.364  1.00   21.34 ? 440 HOH A O   1 
HETATM 2160 O  O   . HOH G 7 .   ? 5.450   6.927   20.105  1.00   20.56 ? 441 HOH A O   1 
HETATM 2161 O  O   . HOH G 7 .   ? -16.378 -12.520 24.291  1.00   20.99 ? 442 HOH A O   1 
HETATM 2162 O  O   . HOH G 7 .   ? -6.048  -11.283 36.334  1.00   35.99 ? 443 HOH A O   1 
HETATM 2163 O  O   . HOH G 7 .   ? -11.781 -3.388  42.567  1.00   31.36 ? 444 HOH A O   1 
HETATM 2164 O  O   . HOH G 7 .   ? -30.685 1.380   25.957  1.00   29.01 ? 445 HOH A O   1 
HETATM 2165 O  O   . HOH G 7 .   ? -8.537  0.627   -6.550  1.00   34.57 ? 446 HOH A O   1 
HETATM 2166 O  O   . HOH G 7 .   ? -8.554  -3.751  7.696   1.00   18.95 ? 447 HOH A O   1 
HETATM 2167 O  O   . HOH G 7 .   ? -26.814 -2.705  14.445  1.00   22.19 ? 448 HOH A O   1 
HETATM 2168 O  O   . HOH G 7 .   ? 8.618   3.064   27.876  1.00   28.10 ? 449 HOH A O   1 
HETATM 2169 O  O   . HOH G 7 .   ? 1.296   -17.288 6.775   1.00   27.15 ? 450 HOH A O   1 
HETATM 2170 O  O   . HOH G 7 .   ? -9.386  5.242   32.725  1.00   24.98 ? 451 HOH A O   1 
HETATM 2171 O  O   . HOH G 7 .   ? 2.834   -11.278 9.698   1.00   25.73 ? 452 HOH A O   1 
HETATM 2172 O  O   . HOH G 7 .   ? 0.231   -1.016  -4.747  1.00   26.83 ? 453 HOH A O   1 
HETATM 2173 O  O   . HOH G 7 .   ? -0.346  10.885  23.339  1.00   22.75 ? 454 HOH A O   1 
HETATM 2174 O  O   . HOH G 7 .   ? -17.236 10.979  -2.157  1.00   24.11 ? 455 HOH A O   1 
HETATM 2175 O  O   . HOH G 7 .   ? -5.704  -4.360  -6.408  1.00   26.00 ? 456 HOH A O   1 
HETATM 2176 O  O   . HOH G 7 .   ? -9.909  14.647  12.085  1.00   15.97 ? 457 HOH A O   1 
HETATM 2177 O  O   . HOH G 7 .   ? -1.199  11.222  25.811  1.00   36.09 ? 458 HOH A O   1 
HETATM 2178 O  O   . HOH G 7 .   ? -11.830 2.952   30.749  1.00   21.09 ? 459 HOH A O   1 
HETATM 2179 O  O   . HOH G 7 .   ? -23.336 -0.937  34.342  1.00   32.95 ? 460 HOH A O   1 
HETATM 2180 O  O   . HOH G 7 .   ? -26.159 -6.487  13.049  1.00   26.19 ? 461 HOH A O   1 
HETATM 2181 O  O   . HOH G 7 .   ? 5.736   -7.034  22.630  1.00   29.84 ? 462 HOH A O   1 
HETATM 2182 O  O   . HOH G 7 .   ? 0.176   0.925   34.439  1.00   24.61 ? 463 HOH A O   1 
HETATM 2183 O  O   . HOH G 7 .   ? -20.285 10.813  26.616  1.00   22.92 ? 464 HOH A O   1 
HETATM 2184 O  O   . HOH G 7 .   ? 4.179   -2.611  28.785  1.00   30.30 ? 465 HOH A O   1 
HETATM 2185 O  O   . HOH G 7 .   ? -29.134 -3.908  13.406  1.00   31.61 ? 466 HOH A O   1 
HETATM 2186 O  O   . HOH G 7 .   ? -0.794  -11.240 28.885  1.00   29.01 ? 467 HOH A O   1 
HETATM 2187 O  O   . HOH G 7 .   ? -13.941 14.203  27.145  1.00   28.89 ? 468 HOH A O   1 
HETATM 2188 O  O   . HOH G 7 .   ? -17.129 -23.058 3.923   1.00   26.08 ? 469 HOH A O   1 
HETATM 2189 O  O   . HOH G 7 .   ? -22.514 -0.044  -5.135  1.00   25.55 ? 470 HOH A O   1 
HETATM 2190 O  O   . HOH G 7 .   ? -7.156  -19.847 19.410  1.00   33.73 ? 471 HOH A O   1 
HETATM 2191 O  O   . HOH G 7 .   ? -4.536  -12.092 32.226  1.00   24.15 ? 472 HOH A O   1 
HETATM 2192 O  O   . HOH G 7 .   ? -23.551 -13.361 11.550  1.00   36.18 ? 473 HOH A O   1 
HETATM 2193 O  O   . HOH G 7 .   ? -18.274 -8.983  34.627  1.00   27.33 ? 474 HOH A O   1 
HETATM 2194 O  O   . HOH G 7 .   ? -10.221 -18.268 16.855  1.00   24.84 ? 475 HOH A O   1 
HETATM 2195 O  O   . HOH G 7 .   ? 1.181   8.675   24.504  1.00   17.68 ? 476 HOH A O   1 
HETATM 2196 O  O   . HOH G 7 .   ? -23.804 -16.630 3.723   1.00   29.70 ? 477 HOH A O   1 
HETATM 2197 O  O   . HOH G 7 .   ? -27.857 2.301   22.975  1.00   32.14 ? 478 HOH A O   1 
HETATM 2198 O  O   . HOH G 7 .   ? -19.716 -16.910 3.087   1.00   22.26 ? 479 HOH A O   1 
HETATM 2199 O  O   . HOH G 7 .   ? -5.739  15.369  11.966  1.00   34.64 ? 480 HOH A O   1 
HETATM 2200 O  O   . HOH G 7 .   ? -16.903 -13.955 37.341  1.00   31.47 ? 481 HOH A O   1 
HETATM 2201 O  O   . HOH G 7 .   ? -7.868  7.176   27.597  1.00   29.48 ? 482 HOH A O   1 
HETATM 2202 O  O   . HOH G 7 .   ? 0.861   -6.595  34.734  1.00   27.90 ? 483 HOH A O   1 
HETATM 2203 O  O   . HOH G 7 .   ? -18.744 12.060  12.873  1.00   29.91 ? 484 HOH A O   1 
HETATM 2204 O  O   . HOH G 7 .   ? -19.448 -23.577 6.159   1.00   29.08 ? 485 HOH A O   1 
HETATM 2205 O  O   . HOH G 7 .   ? -2.814  -17.723 4.790   1.00   29.35 ? 486 HOH A O   1 
HETATM 2206 O  O   . HOH G 7 .   ? -32.483 1.584   12.417  1.00   34.80 ? 487 HOH A O   1 
HETATM 2207 O  O   . HOH G 7 .   ? -15.518 9.007   -2.103  1.00   23.85 ? 488 HOH A O   1 
HETATM 2208 O  O   . HOH G 7 .   ? -10.164 13.327  8.742   1.00   30.14 ? 489 HOH A O   1 
HETATM 2209 O  O   . HOH G 7 .   ? -10.133 -25.008 8.071   1.00   29.89 ? 490 HOH A O   1 
HETATM 2210 O  O   . HOH G 7 .   ? -25.540 -10.585 17.566  1.00   23.82 ? 491 HOH A O   1 
HETATM 2211 O  O   . HOH G 7 .   ? 10.865  -8.910  8.959   1.00   41.01 ? 492 HOH A O   1 
HETATM 2212 O  O   . HOH G 7 .   ? 2.768   1.715   -2.198  1.00   41.77 ? 493 HOH A O   1 
HETATM 2213 O  O   . HOH G 7 .   ? -13.269 22.276  14.893  1.00   24.94 ? 494 HOH A O   1 
HETATM 2214 O  O   . HOH G 7 .   ? -7.248  -8.974  32.483  1.00   17.91 ? 495 HOH A O   1 
HETATM 2215 O  O   . HOH G 7 .   ? -3.361  -12.939 -2.906  1.00   28.38 ? 496 HOH A O   1 
HETATM 2216 O  O   . HOH G 7 .   ? -16.241 5.203   -8.162  1.00   30.24 ? 497 HOH A O   1 
HETATM 2217 O  O   . HOH G 7 .   ? -15.849 15.820  23.705  1.00   26.16 ? 498 HOH A O   1 
HETATM 2218 O  O   . HOH G 7 .   ? -19.993 -15.695 22.642  1.00   32.47 ? 499 HOH A O   1 
HETATM 2219 O  O   . HOH G 7 .   ? -20.783 13.557  1.859   1.00   41.38 ? 500 HOH A O   1 
HETATM 2220 O  O   . HOH G 7 .   ? -9.829  1.260   38.981  1.00   30.67 ? 501 HOH A O   1 
HETATM 2221 O  O   . HOH G 7 .   ? -2.332  -12.088 31.416  1.00   32.09 ? 502 HOH A O   1 
HETATM 2222 O  O   . HOH G 7 .   ? -21.246 -22.077 13.916  1.00   33.05 ? 503 HOH A O   1 
HETATM 2223 O  O   . HOH G 7 .   ? 0.093   -14.402 22.353  1.00   28.10 ? 504 HOH A O   1 
HETATM 2224 O  O   . HOH G 7 .   ? -17.240 -7.219  40.001  1.00   25.05 ? 505 HOH A O   1 
HETATM 2225 O  O   . HOH G 7 .   ? -17.851 -9.528  37.003  1.00   38.27 ? 506 HOH A O   1 
HETATM 2226 O  O   . HOH G 7 .   ? -5.611  3.379   -5.973  1.00   25.82 ? 507 HOH A O   1 
HETATM 2227 O  O   . HOH G 7 .   ? -4.331  -15.927 0.901   1.00   27.70 ? 508 HOH A O   1 
HETATM 2228 O  O   . HOH G 7 .   ? 6.180   -8.066  -10.062 1.00   35.61 ? 509 HOH A O   1 
HETATM 2229 O  O   . HOH G 7 .   ? -18.068 -3.785  -2.614  1.00   26.70 ? 510 HOH A O   1 
HETATM 2230 O  O   . HOH G 7 .   ? -26.520 3.231   20.854  1.00   30.41 ? 511 HOH A O   1 
HETATM 2231 O  O   . HOH G 7 .   ? -1.439  -13.424 27.471  1.00   25.19 ? 512 HOH A O   1 
HETATM 2232 O  O   . HOH G 7 .   ? -23.688 -6.980  -0.016  1.00   26.98 ? 513 HOH A O   1 
HETATM 2233 O  O   . HOH G 7 .   ? -25.814 6.020   27.169  1.00   29.90 ? 514 HOH A O   1 
HETATM 2234 O  O   . HOH G 7 .   ? -12.236 -18.452 32.053  1.00   40.63 ? 515 HOH A O   1 
HETATM 2235 O  O   . HOH G 7 .   ? -13.716 22.572  18.810  1.00   27.33 ? 516 HOH A O   1 
HETATM 2236 O  O   . HOH G 7 .   ? -0.627  -8.744  32.188  1.00   26.25 ? 517 HOH A O   1 
HETATM 2237 O  O   . HOH G 7 .   ? -8.821  -6.126  35.865  1.00   20.97 ? 518 HOH A O   1 
HETATM 2238 O  O   . HOH G 7 .   ? -19.959 -4.553  -3.947  1.00   33.51 ? 519 HOH A O   1 
HETATM 2239 O  O   . HOH G 7 .   ? -5.404  -10.920 39.422  1.00   43.06 ? 520 HOH A O   1 
HETATM 2240 O  O   . HOH G 7 .   ? -13.261 -22.285 11.749  1.00   32.76 ? 521 HOH A O   1 
HETATM 2241 O  O   . HOH G 7 .   ? -24.126 -17.849 6.582   1.00   27.39 ? 522 HOH A O   1 
HETATM 2242 O  O   . HOH G 7 .   ? -11.969 12.663  29.402  1.00   34.14 ? 523 HOH A O   1 
HETATM 2243 O  O   . HOH G 7 .   ? -10.128 0.829   33.893  1.00   29.22 ? 524 HOH A O   1 
HETATM 2244 O  O   . HOH G 7 .   ? 1.785   -10.061 30.556  1.00   26.29 ? 525 HOH A O   1 
HETATM 2245 O  O   . HOH G 7 .   ? -27.824 -4.528  10.071  1.00   42.39 ? 526 HOH A O   1 
HETATM 2246 O  O   . HOH G 7 .   ? -12.077 10.650  6.232   1.00   23.69 ? 527 HOH A O   1 
HETATM 2247 O  O   . HOH G 7 .   ? -24.897 4.705   7.946   1.00   32.55 ? 528 HOH A O   1 
HETATM 2248 O  O   . HOH G 7 .   ? -28.767 -8.043  6.802   1.00   40.29 ? 529 HOH A O   1 
HETATM 2249 O  O   . HOH G 7 .   ? 3.658   4.736   1.963   1.00   30.90 ? 530 HOH A O   1 
HETATM 2250 O  O   . HOH G 7 .   ? -17.005 -16.726 21.814  1.00   33.67 ? 531 HOH A O   1 
HETATM 2251 O  O   . HOH G 7 .   ? 2.429   -14.689 19.631  1.00   41.59 ? 532 HOH A O   1 
HETATM 2252 O  O   . HOH G 7 .   ? -17.665 19.511  17.477  1.00   25.72 ? 533 HOH A O   1 
HETATM 2253 O  O   . HOH G 7 .   ? 2.843   -4.140  7.669   1.00   34.57 ? 534 HOH A O   1 
HETATM 2254 O  O   . HOH G 7 .   ? -15.929 15.672  3.403   1.00   34.32 ? 535 HOH A O   1 
HETATM 2255 O  O   . HOH G 7 .   ? -24.043 -3.329  4.666   1.00   36.94 ? 536 HOH A O   1 
HETATM 2256 O  O   . HOH G 7 .   ? -10.000 -19.123 33.947  1.00   32.73 ? 537 HOH A O   1 
HETATM 2257 O  O   . HOH G 7 .   ? 7.888   -1.711  -10.198 1.00   23.96 ? 538 HOH A O   1 
HETATM 2258 O  O   . HOH G 7 .   ? -17.811 -20.513 8.127   1.00   11.00 ? 539 HOH A O   1 
HETATM 2259 O  O   . HOH G 7 .   ? 4.614   -6.612  7.946   1.00   30.37 ? 540 HOH A O   1 
HETATM 2260 O  O   . HOH G 7 .   ? -6.858  -14.888 31.529  1.00   16.70 ? 541 HOH A O   1 
HETATM 2261 O  O   . HOH G 7 .   ? -15.684 -11.375 40.976  1.00   34.08 ? 542 HOH A O   1 
HETATM 2262 O  O   . HOH G 7 .   ? 0.029   -19.498 6.549   1.00   29.00 ? 543 HOH A O   1 
HETATM 2263 O  O   . HOH G 7 .   ? -26.747 -4.108  25.180  1.00   23.85 ? 544 HOH A O   1 
HETATM 2264 O  O   . HOH G 7 .   ? 8.742   -4.774  23.867  1.00   31.91 ? 545 HOH A O   1 
HETATM 2265 O  O   . HOH G 7 .   ? -6.125  21.134  23.967  1.00   28.28 ? 546 HOH A O   1 
HETATM 2266 O  O   . HOH G 7 .   ? -4.024  -9.765  34.014  1.00   38.88 ? 547 HOH A O   1 
HETATM 2267 O  O   . HOH G 7 .   ? -4.415  -8.605  31.308  1.00   31.39 ? 548 HOH A O   1 
HETATM 2268 O  O   . HOH G 7 .   ? -20.388 -20.147 15.150  1.00   43.32 ? 549 HOH A O   1 
HETATM 2269 O  O   . HOH G 7 .   ? 1.186   11.015  14.948  1.00   35.56 ? 550 HOH A O   1 
HETATM 2270 O  O   . HOH G 7 .   ? -1.414  -17.849 17.777  1.00   27.95 ? 551 HOH A O   1 
HETATM 2271 O  O   . HOH G 7 .   ? -1.713  10.216  32.112  1.00   32.84 ? 552 HOH A O   1 
HETATM 2272 O  O   . HOH G 7 .   ? -10.540 15.112  5.954   1.00   40.99 ? 553 HOH A O   1 
HETATM 2273 O  O   . HOH G 7 .   ? -24.213 10.142  26.910  1.00   32.45 ? 554 HOH A O   1 
HETATM 2274 O  O   . HOH G 7 .   ? -27.956 4.796   25.588  1.00   34.75 ? 555 HOH A O   1 
HETATM 2275 O  O   . HOH G 7 .   ? 0.292   -16.922 29.574  1.00   45.90 ? 556 HOH A O   1 
HETATM 2276 O  O   . HOH G 7 .   ? 9.376   8.107   22.133  1.00   31.82 ? 557 HOH A O   1 
HETATM 2277 O  O   . HOH G 7 .   ? -13.934 -21.443 3.405   1.00   42.08 ? 558 HOH A O   1 
HETATM 2278 O  O   . HOH G 7 .   ? 9.283   -12.652 8.769   1.00   46.92 ? 559 HOH A O   1 
HETATM 2279 O  O   . HOH G 7 .   ? 8.851   1.510   30.467  1.00   41.15 ? 560 HOH A O   1 
HETATM 2280 O  O   . HOH G 7 .   ? -31.216 4.076   7.951   1.00   34.17 ? 561 HOH A O   1 
HETATM 2281 O  O   . HOH G 7 .   ? -12.594 9.512   -2.410  1.00   35.77 ? 562 HOH A O   1 
HETATM 2282 O  O   . HOH G 7 .   ? 0.092   -14.837 26.234  1.00   36.91 ? 563 HOH A O   1 
HETATM 2283 O  O   . HOH G 7 .   ? 6.508   5.454   28.626  1.00   38.42 ? 564 HOH A O   1 
HETATM 2284 O  O   . HOH G 7 .   ? -23.948 8.784   20.227  1.00   33.80 ? 565 HOH A O   1 
HETATM 2285 O  O   . HOH G 7 .   ? -6.862  5.863   6.468   1.00   28.53 ? 566 HOH A O   1 
HETATM 2286 O  O   . HOH G 7 .   ? -10.052 5.193   30.126  1.00   33.71 ? 567 HOH A O   1 
HETATM 2287 O  O   . HOH G 7 .   ? -25.483 -3.485  31.657  1.00   26.62 ? 568 HOH A O   1 
HETATM 2288 O  O   . HOH G 7 .   ? 11.129  -6.809  22.537  1.00   31.64 ? 569 HOH A O   1 
HETATM 2289 O  O   . HOH G 7 .   ? 9.393   7.455   18.626  1.00   32.43 ? 570 HOH A O   1 
HETATM 2290 O  O   . HOH G 7 .   ? 6.994   3.581   31.295  1.00   42.64 ? 571 HOH A O   1 
HETATM 2291 O  O   . HOH G 7 .   ? -14.595 -16.604 28.715  1.00   38.71 ? 572 HOH A O   1 
HETATM 2292 O  O   . HOH G 7 .   ? -3.501  5.323   6.822   1.00   39.67 ? 573 HOH A O   1 
HETATM 2293 O  O   . HOH G 7 .   ? 0.952   3.156   2.264   1.00   33.31 ? 574 HOH A O   1 
HETATM 2294 O  O   . HOH G 7 .   ? -26.884 -6.580  8.092   1.00   46.47 ? 575 HOH A O   1 
HETATM 2295 O  O   . HOH G 7 .   ? 1.378   -12.002 24.939  1.00   28.72 ? 576 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 MES 1   302 1   MES MES A . 
D 4 DMS 1   303 1   DMS DMS A . 
E 5 NA  1   304 1   NA  NA  A . 
F 6 EWZ 1   305 1   EWZ EWZ A . 
G 7 HOH 1   401 1   HOH HOH A . 
G 7 HOH 2   402 2   HOH HOH A . 
G 7 HOH 3   403 3   HOH HOH A . 
G 7 HOH 4   404 4   HOH HOH A . 
G 7 HOH 5   405 5   HOH HOH A . 
G 7 HOH 6   406 6   HOH HOH A . 
G 7 HOH 7   407 7   HOH HOH A . 
G 7 HOH 8   408 8   HOH HOH A . 
G 7 HOH 9   409 9   HOH HOH A . 
G 7 HOH 10  410 10  HOH HOH A . 
G 7 HOH 11  411 11  HOH HOH A . 
G 7 HOH 12  412 12  HOH HOH A . 
G 7 HOH 13  413 13  HOH HOH A . 
G 7 HOH 14  414 14  HOH HOH A . 
G 7 HOH 15  415 15  HOH HOH A . 
G 7 HOH 16  416 16  HOH HOH A . 
G 7 HOH 17  417 17  HOH HOH A . 
G 7 HOH 18  418 18  HOH HOH A . 
G 7 HOH 19  419 19  HOH HOH A . 
G 7 HOH 20  420 20  HOH HOH A . 
G 7 HOH 21  421 21  HOH HOH A . 
G 7 HOH 22  422 22  HOH HOH A . 
G 7 HOH 23  423 23  HOH HOH A . 
G 7 HOH 24  424 24  HOH HOH A . 
G 7 HOH 25  425 25  HOH HOH A . 
G 7 HOH 26  426 26  HOH HOH A . 
G 7 HOH 27  427 27  HOH HOH A . 
G 7 HOH 28  428 28  HOH HOH A . 
G 7 HOH 29  429 29  HOH HOH A . 
G 7 HOH 30  430 30  HOH HOH A . 
G 7 HOH 31  431 31  HOH HOH A . 
G 7 HOH 32  432 32  HOH HOH A . 
G 7 HOH 33  433 33  HOH HOH A . 
G 7 HOH 34  434 34  HOH HOH A . 
G 7 HOH 35  435 35  HOH HOH A . 
G 7 HOH 36  436 36  HOH HOH A . 
G 7 HOH 37  437 37  HOH HOH A . 
G 7 HOH 38  438 38  HOH HOH A . 
G 7 HOH 39  439 39  HOH HOH A . 
G 7 HOH 40  440 40  HOH HOH A . 
G 7 HOH 41  441 41  HOH HOH A . 
G 7 HOH 42  442 42  HOH HOH A . 
G 7 HOH 43  443 43  HOH HOH A . 
G 7 HOH 44  444 44  HOH HOH A . 
G 7 HOH 45  445 45  HOH HOH A . 
G 7 HOH 46  446 46  HOH HOH A . 
G 7 HOH 47  447 47  HOH HOH A . 
G 7 HOH 48  448 48  HOH HOH A . 
G 7 HOH 49  449 49  HOH HOH A . 
G 7 HOH 50  450 50  HOH HOH A . 
G 7 HOH 51  451 51  HOH HOH A . 
G 7 HOH 52  452 52  HOH HOH A . 
G 7 HOH 53  453 53  HOH HOH A . 
G 7 HOH 54  454 54  HOH HOH A . 
G 7 HOH 55  455 55  HOH HOH A . 
G 7 HOH 56  456 56  HOH HOH A . 
G 7 HOH 57  457 57  HOH HOH A . 
G 7 HOH 58  458 58  HOH HOH A . 
G 7 HOH 59  459 59  HOH HOH A . 
G 7 HOH 60  460 60  HOH HOH A . 
G 7 HOH 61  461 61  HOH HOH A . 
G 7 HOH 62  462 62  HOH HOH A . 
G 7 HOH 63  463 63  HOH HOH A . 
G 7 HOH 64  464 64  HOH HOH A . 
G 7 HOH 65  465 65  HOH HOH A . 
G 7 HOH 66  466 66  HOH HOH A . 
G 7 HOH 67  467 67  HOH HOH A . 
G 7 HOH 68  468 68  HOH HOH A . 
G 7 HOH 69  469 69  HOH HOH A . 
G 7 HOH 70  470 70  HOH HOH A . 
G 7 HOH 71  471 71  HOH HOH A . 
G 7 HOH 72  472 72  HOH HOH A . 
G 7 HOH 73  473 73  HOH HOH A . 
G 7 HOH 74  474 74  HOH HOH A . 
G 7 HOH 75  475 75  HOH HOH A . 
G 7 HOH 76  476 76  HOH HOH A . 
G 7 HOH 77  477 77  HOH HOH A . 
G 7 HOH 78  478 78  HOH HOH A . 
G 7 HOH 79  479 79  HOH HOH A . 
G 7 HOH 80  480 80  HOH HOH A . 
G 7 HOH 81  481 81  HOH HOH A . 
G 7 HOH 82  482 82  HOH HOH A . 
G 7 HOH 83  483 83  HOH HOH A . 
G 7 HOH 84  484 84  HOH HOH A . 
G 7 HOH 85  485 85  HOH HOH A . 
G 7 HOH 86  486 86  HOH HOH A . 
G 7 HOH 87  487 87  HOH HOH A . 
G 7 HOH 88  488 88  HOH HOH A . 
G 7 HOH 89  489 89  HOH HOH A . 
G 7 HOH 90  490 90  HOH HOH A . 
G 7 HOH 91  491 91  HOH HOH A . 
G 7 HOH 92  492 92  HOH HOH A . 
G 7 HOH 93  493 93  HOH HOH A . 
G 7 HOH 94  494 94  HOH HOH A . 
G 7 HOH 95  495 95  HOH HOH A . 
G 7 HOH 96  496 96  HOH HOH A . 
G 7 HOH 97  497 97  HOH HOH A . 
G 7 HOH 98  498 98  HOH HOH A . 
G 7 HOH 99  499 99  HOH HOH A . 
G 7 HOH 100 500 100 HOH HOH A . 
G 7 HOH 101 501 101 HOH HOH A . 
G 7 HOH 102 502 102 HOH HOH A . 
G 7 HOH 103 503 103 HOH HOH A . 
G 7 HOH 104 504 104 HOH HOH A . 
G 7 HOH 105 505 105 HOH HOH A . 
G 7 HOH 106 506 106 HOH HOH A . 
G 7 HOH 107 507 107 HOH HOH A . 
G 7 HOH 108 508 108 HOH HOH A . 
G 7 HOH 109 509 109 HOH HOH A . 
G 7 HOH 110 510 110 HOH HOH A . 
G 7 HOH 111 511 111 HOH HOH A . 
G 7 HOH 112 512 112 HOH HOH A . 
G 7 HOH 113 513 113 HOH HOH A . 
G 7 HOH 114 514 114 HOH HOH A . 
G 7 HOH 115 515 115 HOH HOH A . 
G 7 HOH 116 516 116 HOH HOH A . 
G 7 HOH 117 517 117 HOH HOH A . 
G 7 HOH 118 518 118 HOH HOH A . 
G 7 HOH 119 519 119 HOH HOH A . 
G 7 HOH 120 520 120 HOH HOH A . 
G 7 HOH 121 521 121 HOH HOH A . 
G 7 HOH 122 522 122 HOH HOH A . 
G 7 HOH 123 523 123 HOH HOH A . 
G 7 HOH 124 524 124 HOH HOH A . 
G 7 HOH 125 525 125 HOH HOH A . 
G 7 HOH 126 526 126 HOH HOH A . 
G 7 HOH 127 527 127 HOH HOH A . 
G 7 HOH 128 528 128 HOH HOH A . 
G 7 HOH 129 529 129 HOH HOH A . 
G 7 HOH 130 530 130 HOH HOH A . 
G 7 HOH 131 531 131 HOH HOH A . 
G 7 HOH 132 532 132 HOH HOH A . 
G 7 HOH 133 533 133 HOH HOH A . 
G 7 HOH 134 534 134 HOH HOH A . 
G 7 HOH 135 535 135 HOH HOH A . 
G 7 HOH 136 536 136 HOH HOH A . 
G 7 HOH 137 537 137 HOH HOH A . 
G 7 HOH 138 538 138 HOH HOH A . 
G 7 HOH 139 539 139 HOH HOH A . 
G 7 HOH 140 540 140 HOH HOH A . 
G 7 HOH 141 541 141 HOH HOH A . 
G 7 HOH 142 542 142 HOH HOH A . 
G 7 HOH 143 543 143 HOH HOH A . 
G 7 HOH 144 544 144 HOH HOH A . 
G 7 HOH 145 545 145 HOH HOH A . 
G 7 HOH 146 546 146 HOH HOH A . 
G 7 HOH 147 547 147 HOH HOH A . 
G 7 HOH 148 548 148 HOH HOH A . 
G 7 HOH 149 549 149 HOH HOH A . 
G 7 HOH 150 550 150 HOH HOH A . 
G 7 HOH 151 551 151 HOH HOH A . 
G 7 HOH 152 552 152 HOH HOH A . 
G 7 HOH 153 553 153 HOH HOH A . 
G 7 HOH 154 554 154 HOH HOH A . 
G 7 HOH 155 555 155 HOH HOH A . 
G 7 HOH 156 556 156 HOH HOH A . 
G 7 HOH 157 557 157 HOH HOH A . 
G 7 HOH 158 558 158 HOH HOH A . 
G 7 HOH 159 559 159 HOH HOH A . 
G 7 HOH 160 560 160 HOH HOH A . 
G 7 HOH 161 561 161 HOH HOH A . 
G 7 HOH 162 562 162 HOH HOH A . 
G 7 HOH 163 563 163 HOH HOH A . 
G 7 HOH 164 564 164 HOH HOH A . 
G 7 HOH 165 565 165 HOH HOH A . 
G 7 HOH 166 566 166 HOH HOH A . 
G 7 HOH 167 567 167 HOH HOH A . 
G 7 HOH 168 568 168 HOH HOH A . 
G 7 HOH 169 569 169 HOH HOH A . 
G 7 HOH 170 570 170 HOH HOH A . 
G 7 HOH 171 571 171 HOH HOH A . 
G 7 HOH 172 572 172 HOH HOH A . 
G 7 HOH 173 573 173 HOH HOH A . 
G 7 HOH 174 574 174 HOH HOH A . 
G 7 HOH 175 575 175 HOH HOH A . 
G 7 HOH 176 576 176 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_555 107.2 ? 
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_555 117.6 ? 
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_555 102.7 ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N26 A F EWZ .   ? A EWZ 305 ? 1_555 103.8 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N26 A F EWZ .   ? A EWZ 305 ? 1_555 104.8 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N26 A F EWZ .   ? A EWZ 305 ? 1_555 119.5 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N26 B F EWZ .   ? A EWZ 305 ? 1_555 105.1 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N26 B F EWZ .   ? A EWZ 305 ? 1_555 107.2 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N26 B F EWZ .   ? A EWZ 305 ? 1_555 116.2 ? 
10 N26 A F EWZ .   ? A EWZ 305 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N26 B F EWZ .   ? A EWZ 305 ? 1_555 3.5   ? 
11 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S22 A F EWZ .   ? A EWZ 305 ? 1_555 92.2  ? 
12 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S22 A F EWZ .   ? A EWZ 305 ? 1_555 138.9 ? 
13 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S22 A F EWZ .   ? A EWZ 305 ? 1_555 99.4  ? 
14 N26 A F EWZ .   ? A EWZ 305 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S22 A F EWZ .   ? A EWZ 305 ? 1_555 34.3  ? 
15 N26 B F EWZ .   ? A EWZ 305 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 S22 A F EWZ .   ? A EWZ 305 ? 1_555 31.7  ? 
16 OG  ? A SER 219 ? A SER 220 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? G HOH .   ? A HOH 469 ? 1_555 77.2  ? 
17 OG  ? A SER 219 ? A SER 220 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? G HOH .   ? A HOH 485 ? 1_555 158.2 ? 
18 O   ? G HOH .   ? A HOH 469 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? G HOH .   ? A HOH 485 ? 1_555 85.2  ? 
19 OG  ? A SER 219 ? A SER 220 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? G HOH .   ? A HOH 539 ? 1_555 83.1  ? 
20 O   ? G HOH .   ? A HOH 469 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? G HOH .   ? A HOH 539 ? 1_555 159.2 ? 
21 O   ? G HOH .   ? A HOH 485 ? 1_555 NA ? E NA . ? A NA 304 ? 1_555 O   ? G HOH .   ? A HOH 539 ? 1_555 112.2 ? 
# 
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' pdbx_initial_refinement_model 
5 2 'Structure model' pdbx_struct_conn_angle        
6 2 'Structure model' struct_conn                   
7 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' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
15 2 'Structure model' '_pdbx_struct_conn_angle.value'               
16 2 'Structure model' '_struct_conn.pdbx_dist_value'                
17 2 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
18 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
19 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
20 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
21 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
22 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
23 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
24 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
25 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
26 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
27 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
28 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
29 2 'Structure model' '_struct_site.pdbx_auth_asym_id'              
30 2 'Structure model' '_struct_site.pdbx_auth_comp_id'              
31 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 
MOLREP      .      ?               ?       ?                    ?                        phasing           ? ?          ? 5 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -144.92 53.02   
2 1 LEU A 57  ? ? -122.22 -52.19  
3 1 LYS A 111 ? ? 68.18   -0.73   
4 1 ASN A 244 ? ? -96.68  50.52   
5 1 LYS A 252 ? ? 58.62   -139.48 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 0 A LYS 261 ? CD ? A LYS 260 CD 
2 1 Y 0 A LYS 261 ? CE ? A LYS 260 CE 
3 1 Y 0 A LYS 261 ? NZ ? A LYS 260 NZ 
# 
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  
EWZ O7   O  N N 98  
EWZ C2   C  N N 99  
EWZ C3   C  N N 100 
EWZ C4   C  N N 101 
EWZ C8   C  N N 102 
EWZ C15  C  N N 103 
EWZ C14  C  N N 104 
EWZ C9   C  N N 105 
EWZ N5   N  N N 106 
EWZ N1   N  N N 107 
EWZ C6   C  N N 108 
EWZ S10  S  N N 109 
EWZ C11  C  N N 110 
EWZ C12  C  N N 111 
EWZ O13  O  N N 112 
EWZ C16  C  Y N 113 
EWZ C21  C  Y N 114 
EWZ C20  C  Y N 115 
EWZ C19  C  Y N 116 
EWZ CL   CL N N 117 
EWZ C17  C  Y N 118 
EWZ C18  C  Y N 119 
EWZ S22  S  N N 120 
EWZ O23  O  N N 121 
EWZ O25  O  N N 122 
EWZ N26  N  N N 123 
EWZ H1   H  N N 124 
EWZ H2   H  N N 125 
EWZ H3   H  N N 126 
EWZ H4   H  N N 127 
EWZ H5   H  N N 128 
EWZ H6   H  N N 129 
EWZ H7   H  N N 130 
EWZ H8   H  N N 131 
EWZ H9   H  N N 132 
EWZ H10  H  N N 133 
EWZ H11  H  N N 134 
EWZ H12  H  N N 135 
EWZ H13  H  N N 136 
EWZ H14  H  N N 137 
EWZ H15  H  N N 138 
EWZ H16  H  N N 139 
EWZ H17  H  N N 140 
EWZ H18  H  N N 141 
GLN N    N  N N 142 
GLN CA   C  N S 143 
GLN C    C  N N 144 
GLN O    O  N N 145 
GLN CB   C  N N 146 
GLN CG   C  N N 147 
GLN CD   C  N N 148 
GLN OE1  O  N N 149 
GLN NE2  N  N N 150 
GLN OXT  O  N N 151 
GLN H    H  N N 152 
GLN H2   H  N N 153 
GLN HA   H  N N 154 
GLN HB2  H  N N 155 
GLN HB3  H  N N 156 
GLN HG2  H  N N 157 
GLN HG3  H  N N 158 
GLN HE21 H  N N 159 
GLN HE22 H  N N 160 
GLN HXT  H  N N 161 
GLU N    N  N N 162 
GLU CA   C  N S 163 
GLU C    C  N N 164 
GLU O    O  N N 165 
GLU CB   C  N N 166 
GLU CG   C  N N 167 
GLU CD   C  N N 168 
GLU OE1  O  N N 169 
GLU OE2  O  N N 170 
GLU OXT  O  N N 171 
GLU H    H  N N 172 
GLU H2   H  N N 173 
GLU HA   H  N N 174 
GLU HB2  H  N N 175 
GLU HB3  H  N N 176 
GLU HG2  H  N N 177 
GLU HG3  H  N N 178 
GLU HE2  H  N N 179 
GLU HXT  H  N N 180 
GLY N    N  N N 181 
GLY CA   C  N N 182 
GLY C    C  N N 183 
GLY O    O  N N 184 
GLY OXT  O  N N 185 
GLY H    H  N N 186 
GLY H2   H  N N 187 
GLY HA2  H  N N 188 
GLY HA3  H  N N 189 
GLY HXT  H  N N 190 
HIS N    N  N N 191 
HIS CA   C  N S 192 
HIS C    C  N N 193 
HIS O    O  N N 194 
HIS CB   C  N N 195 
HIS CG   C  Y N 196 
HIS ND1  N  Y N 197 
HIS CD2  C  Y N 198 
HIS CE1  C  Y N 199 
HIS NE2  N  Y N 200 
HIS OXT  O  N N 201 
HIS H    H  N N 202 
HIS H2   H  N N 203 
HIS HA   H  N N 204 
HIS HB2  H  N N 205 
HIS HB3  H  N N 206 
HIS HD1  H  N N 207 
HIS HD2  H  N N 208 
HIS HE1  H  N N 209 
HIS HE2  H  N N 210 
HIS HXT  H  N N 211 
HOH O    O  N N 212 
HOH H1   H  N N 213 
HOH H2   H  N N 214 
ILE N    N  N N 215 
ILE CA   C  N S 216 
ILE C    C  N N 217 
ILE O    O  N N 218 
ILE CB   C  N S 219 
ILE CG1  C  N N 220 
ILE CG2  C  N N 221 
ILE CD1  C  N N 222 
ILE OXT  O  N N 223 
ILE H    H  N N 224 
ILE H2   H  N N 225 
ILE HA   H  N N 226 
ILE HB   H  N N 227 
ILE HG12 H  N N 228 
ILE HG13 H  N N 229 
ILE HG21 H  N N 230 
ILE HG22 H  N N 231 
ILE HG23 H  N N 232 
ILE HD11 H  N N 233 
ILE HD12 H  N N 234 
ILE HD13 H  N N 235 
ILE HXT  H  N N 236 
LEU N    N  N N 237 
LEU CA   C  N S 238 
LEU C    C  N N 239 
LEU O    O  N N 240 
LEU CB   C  N N 241 
LEU CG   C  N N 242 
LEU CD1  C  N N 243 
LEU CD2  C  N N 244 
LEU OXT  O  N N 245 
LEU H    H  N N 246 
LEU H2   H  N N 247 
LEU HA   H  N N 248 
LEU HB2  H  N N 249 
LEU HB3  H  N N 250 
LEU HG   H  N N 251 
LEU HD11 H  N N 252 
LEU HD12 H  N N 253 
LEU HD13 H  N N 254 
LEU HD21 H  N N 255 
LEU HD22 H  N N 256 
LEU HD23 H  N N 257 
LEU HXT  H  N N 258 
LYS N    N  N N 259 
LYS CA   C  N S 260 
LYS C    C  N N 261 
LYS O    O  N N 262 
LYS CB   C  N N 263 
LYS CG   C  N N 264 
LYS CD   C  N N 265 
LYS CE   C  N N 266 
LYS NZ   N  N N 267 
LYS OXT  O  N N 268 
LYS H    H  N N 269 
LYS H2   H  N N 270 
LYS HA   H  N N 271 
LYS HB2  H  N N 272 
LYS HB3  H  N N 273 
LYS HG2  H  N N 274 
LYS HG3  H  N N 275 
LYS HD2  H  N N 276 
LYS HD3  H  N N 277 
LYS HE2  H  N N 278 
LYS HE3  H  N N 279 
LYS HZ1  H  N N 280 
LYS HZ2  H  N N 281 
LYS HZ3  H  N N 282 
LYS HXT  H  N N 283 
MES O1   O  N N 284 
MES C2   C  N N 285 
MES C3   C  N N 286 
MES N4   N  N N 287 
MES C5   C  N N 288 
MES C6   C  N N 289 
MES C7   C  N N 290 
MES C8   C  N N 291 
MES S    S  N N 292 
MES O1S  O  N N 293 
MES O2S  O  N N 294 
MES O3S  O  N N 295 
MES H21  H  N N 296 
MES H22  H  N N 297 
MES H31  H  N N 298 
MES H32  H  N N 299 
MES HN4  H  N N 300 
MES H51  H  N N 301 
MES H52  H  N N 302 
MES H61  H  N N 303 
MES H62  H  N N 304 
MES H71  H  N N 305 
MES H72  H  N N 306 
MES H81  H  N N 307 
MES H82  H  N N 308 
MET N    N  N N 309 
MET CA   C  N S 310 
MET C    C  N N 311 
MET O    O  N N 312 
MET CB   C  N N 313 
MET CG   C  N N 314 
MET SD   S  N N 315 
MET CE   C  N N 316 
MET OXT  O  N N 317 
MET H    H  N N 318 
MET H2   H  N N 319 
MET HA   H  N N 320 
MET HB2  H  N N 321 
MET HB3  H  N N 322 
MET HG2  H  N N 323 
MET HG3  H  N N 324 
MET HE1  H  N N 325 
MET HE2  H  N N 326 
MET HE3  H  N N 327 
MET HXT  H  N N 328 
NA  NA   NA N N 329 
PHE N    N  N N 330 
PHE CA   C  N S 331 
PHE C    C  N N 332 
PHE O    O  N N 333 
PHE CB   C  N N 334 
PHE CG   C  Y N 335 
PHE CD1  C  Y N 336 
PHE CD2  C  Y N 337 
PHE CE1  C  Y N 338 
PHE CE2  C  Y N 339 
PHE CZ   C  Y N 340 
PHE OXT  O  N N 341 
PHE H    H  N N 342 
PHE H2   H  N N 343 
PHE HA   H  N N 344 
PHE HB2  H  N N 345 
PHE HB3  H  N N 346 
PHE HD1  H  N N 347 
PHE HD2  H  N N 348 
PHE HE1  H  N N 349 
PHE HE2  H  N N 350 
PHE HZ   H  N N 351 
PHE HXT  H  N N 352 
PRO N    N  N N 353 
PRO CA   C  N S 354 
PRO C    C  N N 355 
PRO O    O  N N 356 
PRO CB   C  N N 357 
PRO CG   C  N N 358 
PRO CD   C  N N 359 
PRO OXT  O  N N 360 
PRO H    H  N N 361 
PRO HA   H  N N 362 
PRO HB2  H  N N 363 
PRO HB3  H  N N 364 
PRO HG2  H  N N 365 
PRO HG3  H  N N 366 
PRO HD2  H  N N 367 
PRO HD3  H  N N 368 
PRO HXT  H  N N 369 
SER N    N  N N 370 
SER CA   C  N S 371 
SER C    C  N N 372 
SER O    O  N N 373 
SER CB   C  N N 374 
SER OG   O  N N 375 
SER OXT  O  N N 376 
SER H    H  N N 377 
SER H2   H  N N 378 
SER HA   H  N N 379 
SER HB2  H  N N 380 
SER HB3  H  N N 381 
SER HG   H  N N 382 
SER HXT  H  N N 383 
THR N    N  N N 384 
THR CA   C  N S 385 
THR C    C  N N 386 
THR O    O  N N 387 
THR CB   C  N R 388 
THR OG1  O  N N 389 
THR CG2  C  N N 390 
THR OXT  O  N N 391 
THR H    H  N N 392 
THR H2   H  N N 393 
THR HA   H  N N 394 
THR HB   H  N N 395 
THR HG1  H  N N 396 
THR HG21 H  N N 397 
THR HG22 H  N N 398 
THR HG23 H  N N 399 
THR HXT  H  N N 400 
TRP N    N  N N 401 
TRP CA   C  N S 402 
TRP C    C  N N 403 
TRP O    O  N N 404 
TRP CB   C  N N 405 
TRP CG   C  Y N 406 
TRP CD1  C  Y N 407 
TRP CD2  C  Y N 408 
TRP NE1  N  Y N 409 
TRP CE2  C  Y N 410 
TRP CE3  C  Y N 411 
TRP CZ2  C  Y N 412 
TRP CZ3  C  Y N 413 
TRP CH2  C  Y N 414 
TRP OXT  O  N N 415 
TRP H    H  N N 416 
TRP H2   H  N N 417 
TRP HA   H  N N 418 
TRP HB2  H  N N 419 
TRP HB3  H  N N 420 
TRP HD1  H  N N 421 
TRP HE1  H  N N 422 
TRP HE3  H  N N 423 
TRP HZ2  H  N N 424 
TRP HZ3  H  N N 425 
TRP HH2  H  N N 426 
TRP HXT  H  N N 427 
TYR N    N  N N 428 
TYR CA   C  N S 429 
TYR C    C  N N 430 
TYR O    O  N N 431 
TYR CB   C  N N 432 
TYR CG   C  Y N 433 
TYR CD1  C  Y N 434 
TYR CD2  C  Y N 435 
TYR CE1  C  Y N 436 
TYR CE2  C  Y N 437 
TYR CZ   C  Y N 438 
TYR OH   O  N N 439 
TYR OXT  O  N N 440 
TYR H    H  N N 441 
TYR H2   H  N N 442 
TYR HA   H  N N 443 
TYR HB2  H  N N 444 
TYR HB3  H  N N 445 
TYR HD1  H  N N 446 
TYR HD2  H  N N 447 
TYR HE1  H  N N 448 
TYR HE2  H  N N 449 
TYR HH   H  N N 450 
TYR HXT  H  N N 451 
VAL N    N  N N 452 
VAL CA   C  N S 453 
VAL C    C  N N 454 
VAL O    O  N N 455 
VAL CB   C  N N 456 
VAL CG1  C  N N 457 
VAL CG2  C  N N 458 
VAL OXT  O  N N 459 
VAL H    H  N N 460 
VAL H2   H  N N 461 
VAL HA   H  N N 462 
VAL HB   H  N N 463 
VAL HG11 H  N N 464 
VAL HG12 H  N N 465 
VAL HG13 H  N N 466 
VAL HG21 H  N N 467 
VAL HG22 H  N N 468 
VAL HG23 H  N N 469 
VAL HXT  H  N N 470 
ZN  ZN   ZN N N 471 
# 
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  
EWZ S10 C6   sing N N 92  
EWZ S10 C11  sing N N 93  
EWZ N1  C6   sing N N 94  
EWZ N1  C2   sing N N 95  
EWZ O7  C2   doub N N 96  
EWZ C6  N5   doub N N 97  
EWZ C2  C3   sing N N 98  
EWZ O13 C12  doub N N 99  
EWZ N5  C4   sing N N 100 
EWZ C15 C8   sing N N 101 
EWZ C3  C4   doub N N 102 
EWZ C4  C8   sing N N 103 
EWZ C11 C12  sing N N 104 
EWZ C12 C16  sing N N 105 
EWZ C8  C14  sing N N 106 
EWZ C8  C9   sing N N 107 
EWZ C16 C21  sing Y N 108 
EWZ C16 C17  doub Y N 109 
EWZ C21 C20  doub Y N 110 
EWZ C17 C18  sing Y N 111 
EWZ C20 C19  sing Y N 112 
EWZ C18 C19  doub Y N 113 
EWZ C18 S22  sing N N 114 
EWZ C19 CL   sing N N 115 
EWZ N26 S22  sing N N 116 
EWZ S22 O25  doub N N 117 
EWZ S22 O23  doub N N 118 
EWZ C3  H1   sing N N 119 
EWZ C15 H2   sing N N 120 
EWZ C15 H3   sing N N 121 
EWZ C15 H4   sing N N 122 
EWZ C14 H5   sing N N 123 
EWZ C14 H6   sing N N 124 
EWZ C14 H7   sing N N 125 
EWZ C9  H8   sing N N 126 
EWZ C9  H9   sing N N 127 
EWZ C9  H10  sing N N 128 
EWZ N1  H11  sing N N 129 
EWZ C11 H12  sing N N 130 
EWZ C11 H13  sing N N 131 
EWZ C21 H14  sing N N 132 
EWZ C20 H15  sing N N 133 
EWZ C17 H16  sing N N 134 
EWZ N26 H17  sing N N 135 
EWZ N26 H18  sing N N 136 
GLN N   CA   sing N N 137 
GLN N   H    sing N N 138 
GLN N   H2   sing N N 139 
GLN CA  C    sing N N 140 
GLN CA  CB   sing N N 141 
GLN CA  HA   sing N N 142 
GLN C   O    doub N N 143 
GLN C   OXT  sing N N 144 
GLN CB  CG   sing N N 145 
GLN CB  HB2  sing N N 146 
GLN CB  HB3  sing N N 147 
GLN CG  CD   sing N N 148 
GLN CG  HG2  sing N N 149 
GLN CG  HG3  sing N N 150 
GLN CD  OE1  doub N N 151 
GLN CD  NE2  sing N N 152 
GLN NE2 HE21 sing N N 153 
GLN NE2 HE22 sing N N 154 
GLN OXT HXT  sing N N 155 
GLU N   CA   sing N N 156 
GLU N   H    sing N N 157 
GLU N   H2   sing N N 158 
GLU CA  C    sing N N 159 
GLU CA  CB   sing N N 160 
GLU CA  HA   sing N N 161 
GLU C   O    doub N N 162 
GLU C   OXT  sing N N 163 
GLU CB  CG   sing N N 164 
GLU CB  HB2  sing N N 165 
GLU CB  HB3  sing N N 166 
GLU CG  CD   sing N N 167 
GLU CG  HG2  sing N N 168 
GLU CG  HG3  sing N N 169 
GLU CD  OE1  doub N N 170 
GLU CD  OE2  sing N N 171 
GLU OE2 HE2  sing N N 172 
GLU OXT HXT  sing N N 173 
GLY N   CA   sing N N 174 
GLY N   H    sing N N 175 
GLY N   H2   sing N N 176 
GLY CA  C    sing N N 177 
GLY CA  HA2  sing N N 178 
GLY CA  HA3  sing N N 179 
GLY C   O    doub N N 180 
GLY C   OXT  sing N N 181 
GLY OXT HXT  sing N N 182 
HIS N   CA   sing N N 183 
HIS N   H    sing N N 184 
HIS N   H2   sing N N 185 
HIS CA  C    sing N N 186 
HIS CA  CB   sing N N 187 
HIS CA  HA   sing N N 188 
HIS C   O    doub N N 189 
HIS C   OXT  sing N N 190 
HIS CB  CG   sing N N 191 
HIS CB  HB2  sing N N 192 
HIS CB  HB3  sing N N 193 
HIS CG  ND1  sing Y N 194 
HIS CG  CD2  doub Y N 195 
HIS ND1 CE1  doub Y N 196 
HIS ND1 HD1  sing N N 197 
HIS CD2 NE2  sing Y N 198 
HIS CD2 HD2  sing N N 199 
HIS CE1 NE2  sing Y N 200 
HIS CE1 HE1  sing N N 201 
HIS NE2 HE2  sing N N 202 
HIS OXT HXT  sing N N 203 
HOH O   H1   sing N N 204 
HOH O   H2   sing N N 205 
ILE N   CA   sing N N 206 
ILE N   H    sing N N 207 
ILE N   H2   sing N N 208 
ILE CA  C    sing N N 209 
ILE CA  CB   sing N N 210 
ILE CA  HA   sing N N 211 
ILE C   O    doub N N 212 
ILE C   OXT  sing N N 213 
ILE CB  CG1  sing N N 214 
ILE CB  CG2  sing N N 215 
ILE CB  HB   sing N N 216 
ILE CG1 CD1  sing N N 217 
ILE CG1 HG12 sing N N 218 
ILE CG1 HG13 sing N N 219 
ILE CG2 HG21 sing N N 220 
ILE CG2 HG22 sing N N 221 
ILE CG2 HG23 sing N N 222 
ILE CD1 HD11 sing N N 223 
ILE CD1 HD12 sing N N 224 
ILE CD1 HD13 sing N N 225 
ILE OXT HXT  sing N N 226 
LEU N   CA   sing N N 227 
LEU N   H    sing N N 228 
LEU N   H2   sing N N 229 
LEU CA  C    sing N N 230 
LEU CA  CB   sing N N 231 
LEU CA  HA   sing N N 232 
LEU C   O    doub N N 233 
LEU C   OXT  sing N N 234 
LEU CB  CG   sing N N 235 
LEU CB  HB2  sing N N 236 
LEU CB  HB3  sing N N 237 
LEU CG  CD1  sing N N 238 
LEU CG  CD2  sing N N 239 
LEU CG  HG   sing N N 240 
LEU CD1 HD11 sing N N 241 
LEU CD1 HD12 sing N N 242 
LEU CD1 HD13 sing N N 243 
LEU CD2 HD21 sing N N 244 
LEU CD2 HD22 sing N N 245 
LEU CD2 HD23 sing N N 246 
LEU OXT HXT  sing N N 247 
LYS N   CA   sing N N 248 
LYS N   H    sing N N 249 
LYS N   H2   sing N N 250 
LYS CA  C    sing N N 251 
LYS CA  CB   sing N N 252 
LYS CA  HA   sing N N 253 
LYS C   O    doub N N 254 
LYS C   OXT  sing N N 255 
LYS CB  CG   sing N N 256 
LYS CB  HB2  sing N N 257 
LYS CB  HB3  sing N N 258 
LYS CG  CD   sing N N 259 
LYS CG  HG2  sing N N 260 
LYS CG  HG3  sing N N 261 
LYS CD  CE   sing N N 262 
LYS CD  HD2  sing N N 263 
LYS CD  HD3  sing N N 264 
LYS CE  NZ   sing N N 265 
LYS CE  HE2  sing N N 266 
LYS CE  HE3  sing N N 267 
LYS NZ  HZ1  sing N N 268 
LYS NZ  HZ2  sing N N 269 
LYS NZ  HZ3  sing N N 270 
LYS OXT HXT  sing N N 271 
MES O1  C2   sing N N 272 
MES O1  C6   sing N N 273 
MES C2  C3   sing N N 274 
MES C2  H21  sing N N 275 
MES C2  H22  sing N N 276 
MES C3  N4   sing N N 277 
MES C3  H31  sing N N 278 
MES C3  H32  sing N N 279 
MES N4  C5   sing N N 280 
MES N4  C7   sing N N 281 
MES N4  HN4  sing N N 282 
MES C5  C6   sing N N 283 
MES C5  H51  sing N N 284 
MES C5  H52  sing N N 285 
MES C6  H61  sing N N 286 
MES C6  H62  sing N N 287 
MES C7  C8   sing N N 288 
MES C7  H71  sing N N 289 
MES C7  H72  sing N N 290 
MES C8  S    sing N N 291 
MES C8  H81  sing N N 292 
MES C8  H82  sing N N 293 
MES S   O1S  doub N N 294 
MES S   O2S  doub N N 295 
MES S   O3S  sing N N 296 
MET N   CA   sing N N 297 
MET N   H    sing N N 298 
MET N   H2   sing N N 299 
MET CA  C    sing N N 300 
MET CA  CB   sing N N 301 
MET CA  HA   sing N N 302 
MET C   O    doub N N 303 
MET C   OXT  sing N N 304 
MET CB  CG   sing N N 305 
MET CB  HB2  sing N N 306 
MET CB  HB3  sing N N 307 
MET CG  SD   sing N N 308 
MET CG  HG2  sing N N 309 
MET CG  HG3  sing N N 310 
MET SD  CE   sing N N 311 
MET CE  HE1  sing N N 312 
MET CE  HE2  sing N N 313 
MET CE  HE3  sing N N 314 
MET OXT HXT  sing N N 315 
PHE N   CA   sing N N 316 
PHE N   H    sing N N 317 
PHE N   H2   sing N N 318 
PHE CA  C    sing N N 319 
PHE CA  CB   sing N N 320 
PHE CA  HA   sing N N 321 
PHE C   O    doub N N 322 
PHE C   OXT  sing N N 323 
PHE CB  CG   sing N N 324 
PHE CB  HB2  sing N N 325 
PHE CB  HB3  sing N N 326 
PHE CG  CD1  doub Y N 327 
PHE CG  CD2  sing Y N 328 
PHE CD1 CE1  sing Y N 329 
PHE CD1 HD1  sing N N 330 
PHE CD2 CE2  doub Y N 331 
PHE CD2 HD2  sing N N 332 
PHE CE1 CZ   doub Y N 333 
PHE CE1 HE1  sing N N 334 
PHE CE2 CZ   sing Y N 335 
PHE CE2 HE2  sing N N 336 
PHE CZ  HZ   sing N N 337 
PHE OXT HXT  sing N N 338 
PRO N   CA   sing N N 339 
PRO N   CD   sing N N 340 
PRO N   H    sing N N 341 
PRO CA  C    sing N N 342 
PRO CA  CB   sing N N 343 
PRO CA  HA   sing N N 344 
PRO C   O    doub N N 345 
PRO C   OXT  sing N N 346 
PRO CB  CG   sing N N 347 
PRO CB  HB2  sing N N 348 
PRO CB  HB3  sing N N 349 
PRO CG  CD   sing N N 350 
PRO CG  HG2  sing N N 351 
PRO CG  HG3  sing N N 352 
PRO CD  HD2  sing N N 353 
PRO CD  HD3  sing N N 354 
PRO OXT HXT  sing N N 355 
SER N   CA   sing N N 356 
SER N   H    sing N N 357 
SER N   H2   sing N N 358 
SER CA  C    sing N N 359 
SER CA  CB   sing N N 360 
SER CA  HA   sing N N 361 
SER C   O    doub N N 362 
SER C   OXT  sing N N 363 
SER CB  OG   sing N N 364 
SER CB  HB2  sing N N 365 
SER CB  HB3  sing N N 366 
SER OG  HG   sing N N 367 
SER OXT HXT  sing N N 368 
THR N   CA   sing N N 369 
THR N   H    sing N N 370 
THR N   H2   sing N N 371 
THR CA  C    sing N N 372 
THR CA  CB   sing N N 373 
THR CA  HA   sing N N 374 
THR C   O    doub N N 375 
THR C   OXT  sing N N 376 
THR CB  OG1  sing N N 377 
THR CB  CG2  sing N N 378 
THR CB  HB   sing N N 379 
THR OG1 HG1  sing N N 380 
THR CG2 HG21 sing N N 381 
THR CG2 HG22 sing N N 382 
THR CG2 HG23 sing N N 383 
THR OXT HXT  sing N N 384 
TRP N   CA   sing N N 385 
TRP N   H    sing N N 386 
TRP N   H2   sing N N 387 
TRP CA  C    sing N N 388 
TRP CA  CB   sing N N 389 
TRP CA  HA   sing N N 390 
TRP C   O    doub N N 391 
TRP C   OXT  sing N N 392 
TRP CB  CG   sing N N 393 
TRP CB  HB2  sing N N 394 
TRP CB  HB3  sing N N 395 
TRP CG  CD1  doub Y N 396 
TRP CG  CD2  sing Y N 397 
TRP CD1 NE1  sing Y N 398 
TRP CD1 HD1  sing N N 399 
TRP CD2 CE2  doub Y N 400 
TRP CD2 CE3  sing Y N 401 
TRP NE1 CE2  sing Y N 402 
TRP NE1 HE1  sing N N 403 
TRP CE2 CZ2  sing Y N 404 
TRP CE3 CZ3  doub Y N 405 
TRP CE3 HE3  sing N N 406 
TRP CZ2 CH2  doub Y N 407 
TRP CZ2 HZ2  sing N N 408 
TRP CZ3 CH2  sing Y N 409 
TRP CZ3 HZ3  sing N N 410 
TRP CH2 HH2  sing N N 411 
TRP OXT HXT  sing N N 412 
TYR N   CA   sing N N 413 
TYR N   H    sing N N 414 
TYR N   H2   sing N N 415 
TYR CA  C    sing N N 416 
TYR CA  CB   sing N N 417 
TYR CA  HA   sing N N 418 
TYR C   O    doub N N 419 
TYR C   OXT  sing N N 420 
TYR CB  CG   sing N N 421 
TYR CB  HB2  sing N N 422 
TYR CB  HB3  sing N N 423 
TYR CG  CD1  doub Y N 424 
TYR CG  CD2  sing Y N 425 
TYR CD1 CE1  sing Y N 426 
TYR CD1 HD1  sing N N 427 
TYR CD2 CE2  doub Y N 428 
TYR CD2 HD2  sing N N 429 
TYR CE1 CZ   doub Y N 430 
TYR CE1 HE1  sing N N 431 
TYR CE2 CZ   sing Y N 432 
TYR CE2 HE2  sing N N 433 
TYR CZ  OH   sing N N 434 
TYR OH  HH   sing N N 435 
TYR OXT HXT  sing N N 436 
VAL N   CA   sing N N 437 
VAL N   H    sing N N 438 
VAL N   H2   sing N N 439 
VAL CA  C    sing N N 440 
VAL CA  CB   sing N N 441 
VAL CA  HA   sing N N 442 
VAL C   O    doub N N 443 
VAL C   OXT  sing N N 444 
VAL CB  CG1  sing N N 445 
VAL CB  CG2  sing N N 446 
VAL CB  HB   sing N N 447 
VAL CG1 HG11 sing N N 448 
VAL CG1 HG12 sing N N 449 
VAL CG1 HG13 sing N N 450 
VAL CG2 HG21 sing N N 451 
VAL CG2 HG22 sing N N 452 
VAL CG2 HG23 sing N N 453 
VAL OXT HXT  sing N N 454 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                      ZN  
3 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                                          MES 
4 'DIMETHYL SULFOXIDE'                                                                            DMS 
5 'SODIUM ION'                                                                                    NA  
6 '5-{[(4-tert-butyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}-2-chlorobenzenesulfonamide' EWZ 
7 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          ? 
# 
