data_3SBH
# 
_entry.id   3SBH 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_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   3SBH         pdb_00003sbh 10.2210/pdb3sbh/pdb 
RCSB  RCSB066000   ?            ?                   
WWPDB D_1000066000 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3S9T 'human carbonic anhydrase II with 2-chloro-5-{[(4,6-dimethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'      
unspecified 
PDB 3SAX 'human carbonic anhydrase II with 2-chloro-5-{[(5-ethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'           
unspecified 
PDB 3S8X 'human carbonic anhydrase II with 4-{[(4-methyl-6-oxo-1,6-dihydro-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide' 
unspecified 
PDB 3SAP 'human carbonic anhydrase II with 4-{[(5-butyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'                    
unspecified 
PDB 3SBI .                                                                                                                   
unspecified 
# 
_pdbx_database_status.entry_id                        3SBH 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2011-06-05 
_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.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'     1 
'Manakova, E.'     2 
'Tamulaitiene, G.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            51 
_citation.page_first                259 
_citation.page_last                 270 
_citation.year                      2012 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22440859 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2012.02.050 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1 ? 
primary 'Zubriene, A.'      2 ? 
primary 'Baranauskiene, L.' 3 ? 
primary 'Tamulaitiene, G.'  4 ? 
primary 'Manakova, E.'      5 ? 
primary 'Kairys, V.'        6 ? 
primary 'Grazulis, S.'      7 ? 
primary 'Tumkevicius, S.'   8 ? 
primary 'Matulis, D.'       9 ? 
# 
_cell.entry_id           3SBH 
_cell.length_a           42.093 
_cell.length_b           41.090 
_cell.length_c           71.839 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.170 
_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                         3SBH 
_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 BICINE                                                               163.172   1   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                 78.133    2   ?       ? ? ? 
5 non-polymer syn '4-{[(4,6-dimethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' 337.417   1   ?       ? ? ? 
6 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                               195.237   1   ?       ? ? ? 
7 water       nat water                                                                18.015    303 ?       ? ? ? 
# 
_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     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               '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              3SBH 
_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 
BCN non-polymer         . BICINE                                                               ? 'C6 H13 N O4'      163.172 
CYS 'L-peptide linking' y CYSTEINE                                                             ? 'C3 H7 N O2 S'     121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                 ? 'C2 H6 O S'        78.133  
E65 non-polymer         . '4-{[(4,6-dimethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' ? 'C14 H15 N3 O3 S2' 337.417 
GLN 'L-peptide linking' y GLUTAMINE                                                            ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                      ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                                                              ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE                                                            ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                                                ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                           ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                                                              ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                                               ? 'C6 H15 N2 O2 1'   147.195 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                               ? 'C6 H13 N O4 S'    195.237 
MET 'L-peptide linking' y METHIONINE                                                           ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                        ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                                              ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                                               ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                                            ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                           ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                                                             ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                                                               ? 'C5 H11 N O2'      117.146 
ZN  non-polymer         . 'ZINC ION'                                                           ? 'Zn 2'             65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3SBH 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   40.1 
_exptl_crystal.density_Matthews      2.1 
_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              9 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '0.1M Na-bicine pH 9, 2M Na-malonate pH 7.55, VAPOR DIFFUSION, SITTING DROP, temperature 298K' 
_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                   'MAR555 FLAT PANEL' 
_diffrn_detector.pdbx_collection_date   2010-11-14 
_diffrn_detector.details                'Bent, vertically focussing' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8174 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X11' 
_diffrn_source.pdbx_wavelength_list        0.8174 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X11 
# 
_reflns.entry_id                     3SBH 
_reflns.d_resolution_high            1.65 
_reflns.d_resolution_low             28.55 
_reflns.number_all                   ? 
_reflns.number_obs                   28165 
_reflns.pdbx_Rmerge_I_obs            0.058 
_reflns.pdbx_netI_over_sigmaI        30.700 
_reflns.pdbx_Rsym_value              0.058 
_reflns.pdbx_redundancy              7.600 
_reflns.percent_possible_obs         97.700 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        16.2 
_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.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.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.65 1.74  ? 31050 ? 0.278 2.1  0.278 ? 7.70 ? 4038 96.80 1  1 
1.74 1.84  ? 29849 ? 0.180 3.4  0.180 ? 7.70 ? 3860 97.20 2  1 
1.84 1.97  ? 28266 ? 0.116 5.4  0.116 ? 7.80 ? 3637 97.70 3  1 
1.97 2.13  ? 26128 ? 0.081 7.9  0.081 ? 7.80 ? 3370 97.60 4  1 
2.13 2.33  ? 24184 ? 0.063 10.0 0.063 ? 7.70 ? 3127 98.00 5  1 
2.33 2.61  ? 22072 ? 0.054 11.7 0.054 ? 7.70 ? 2861 98.50 6  1 
2.61 3.01  ? 19488 ? 0.046 13.2 0.046 ? 7.70 ? 2539 98.60 7  1 
3.01 3.69  ? 16149 ? 0.039 15.0 0.039 ? 7.50 ? 2160 99.20 8  1 
3.69 5.22  ? 11109 ? 0.035 15.7 0.035 ? 6.60 ? 1671 98.10 9  1 
5.22 28.55 ? 5303  ? 0.035 14.5 0.035 ? 5.90 ? 902  93.80 10 1 
# 
_refine.entry_id                                 3SBH 
_refine.ls_d_res_high                            1.650 
_refine.ls_d_res_low                             25.230 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    97.370 
_refine.ls_number_reflns_obs                     28153 
_refine.ls_number_reflns_all                     28153 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          0.178 
_refine.ls_R_factor_obs                          0.178 
_refine.ls_R_factor_R_work                       0.172 
_refine.ls_wR_factor_R_work                      0.179 
_refine.ls_R_factor_R_free                       0.228 
_refine.ls_wR_factor_R_free                      0.234 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  2850 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               15.461 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.110 
_refine.aniso_B[2][2]                            -0.370 
_refine.aniso_B[3][3]                            0.230 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.060 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.927 
_refine.overall_SU_R_Cruickshank_DPI             0.120 
_refine.overall_SU_R_free                        0.124 
_refine.pdbx_overall_ESU_R_Free                  0.124 
_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          MR 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.849 
_refine.B_iso_max                                56.28 
_refine.B_iso_min                                3.92 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.pdbx_ls_sigma_I                          0 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB entry 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_overall_ESU_R                       ? 
_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        2065 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_refine_hist.number_atoms_solvent             303 
_refine_hist.number_atoms_total               2418 
_refine_hist.d_res_high                       1.650 
_refine_hist.d_res_low                        25.230 
# 
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         2264 0.029  0.021  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      3084 2.335  1.965  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   279  7.146  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   104  33.403 24.904 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   368  13.670 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   7    23.322 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr           317  0.174  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     1770 0.013  0.020  ? ? 'X-RAY DIFFRACTION' 
r_nbd_refined            1214 0.227  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          1499 0.316  0.200  ? ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    238  0.145  0.200  ? ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      3    0.039  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   100  0.233  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 80   0.217  0.200  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_it              1357 1.538  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcangle_it             2204 2.257  2.000  ? ? 'X-RAY DIFFRACTION' 
r_scbond_it              907  3.283  3.000  ? ? 'X-RAY DIFFRACTION' 
r_scangle_it             880  4.597  4.500  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.650 
_refine_ls_shell.d_res_low                        1.693 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               96.020 
_refine_ls_shell.number_reflns_R_work             1831 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.278 
_refine_ls_shell.R_factor_R_free                  0.428 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             194 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                2025 
_refine_ls_shell.number_reflns_obs                1831 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3SBH 
_struct.title                     
'Crystal structure of human carbonic anhydrase isozyme II with 4-{[(4,6-dimethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3SBH 
_struct_keywords.text            'drug design, sulfonamide, 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 4 ? 
F N N 5 ? 
G N N 6 ? 
H 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  ? TRP A 16  ? GLY A 12  TRP A 16  5 ? 5 
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 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
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  262 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  262 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  262 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F E65 . N22 ? ? A ZN  262 A E65 266 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
# 
_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 -4.38 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 2.66  
# 
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 VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
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  262 ? 4  'BINDING SITE FOR RESIDUE ZN A 262'  
AC2 Software A BCN 263 ? 10 'BINDING SITE FOR RESIDUE BCN A 263' 
AC3 Software A DMS 264 ? 4  'BINDING SITE FOR RESIDUE DMS A 264' 
AC4 Software A DMS 265 ? 7  'BINDING SITE FOR RESIDUE DMS A 265' 
AC5 Software A E65 266 ? 13 'BINDING SITE FOR RESIDUE E65 A 266' 
AC6 Software A MES 267 ? 6  'BINDING SITE FOR RESIDUE MES A 267' 
# 
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  E65 F .   ? E65 A 266 . ? 1_555 ? 
5  AC2 10 LYS A 148 ? LYS A 149 . ? 1_555 ? 
6  AC2 10 LYS A 212 ? LYS A 213 . ? 1_555 ? 
7  AC2 10 GLU A 213 ? GLU A 214 . ? 1_555 ? 
8  AC2 10 PRO A 214 ? PRO A 215 . ? 1_555 ? 
9  AC2 10 HOH H .   ? HOH A 283 . ? 1_555 ? 
10 AC2 10 HOH H .   ? HOH A 299 . ? 1_555 ? 
11 AC2 10 HOH H .   ? HOH A 339 . ? 1_555 ? 
12 AC2 10 HOH H .   ? HOH A 354 . ? 1_555 ? 
13 AC2 10 HOH H .   ? HOH A 478 . ? 1_555 ? 
14 AC2 10 HOH H .   ? HOH A 529 . ? 1_555 ? 
15 AC3 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
16 AC3 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
17 AC3 4  HOH H .   ? HOH A 277 . ? 1_555 ? 
18 AC3 4  HOH H .   ? HOH A 467 . ? 1_555 ? 
19 AC4 7  ASN A 67  ? ASN A 67  . ? 1_555 ? 
20 AC4 7  ILE A 91  ? ILE A 91  . ? 1_555 ? 
21 AC4 7  GLN A 92  ? GLN A 92  . ? 1_555 ? 
22 AC4 7  PHE A 130 ? PHE A 131 . ? 1_555 ? 
23 AC4 7  E65 F .   ? E65 A 266 . ? 1_555 ? 
24 AC4 7  HOH H .   ? HOH A 461 . ? 1_555 ? 
25 AC4 7  HOH H .   ? HOH A 550 . ? 1_555 ? 
26 AC5 13 HIS A 94  ? HIS A 94  . ? 1_555 ? 
27 AC5 13 HIS A 96  ? HIS A 96  . ? 1_555 ? 
28 AC5 13 HIS A 119 ? HIS A 119 . ? 1_555 ? 
29 AC5 13 PHE A 130 ? PHE A 131 . ? 1_555 ? 
30 AC5 13 VAL A 142 ? VAL A 143 . ? 1_555 ? 
31 AC5 13 LEU A 197 ? LEU A 198 . ? 1_555 ? 
32 AC5 13 THR A 198 ? THR A 199 . ? 1_555 ? 
33 AC5 13 THR A 199 ? THR A 200 . ? 1_555 ? 
34 AC5 13 PRO A 201 ? PRO A 202 . ? 1_555 ? 
35 AC5 13 TRP A 208 ? TRP A 209 . ? 1_555 ? 
36 AC5 13 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
37 AC5 13 DMS E .   ? DMS A 265 . ? 1_555 ? 
38 AC5 13 HOH H .   ? HOH A 468 . ? 1_555 ? 
39 AC6 6  LEU A 163 ? LEU A 164 . ? 1_555 ? 
40 AC6 6  ASP A 164 ? ASP A 165 . ? 1_555 ? 
41 AC6 6  LYS A 224 ? LYS A 225 . ? 1_555 ? 
42 AC6 6  LYS A 227 ? LYS A 228 . ? 1_555 ? 
43 AC6 6  LEU A 228 ? LEU A 229 . ? 1_555 ? 
44 AC6 6  HOH H .   ? HOH A 302 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3SBH 
_atom_sites.fract_transf_matrix[1][1]   0.023757 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005998 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024337 
_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]   0.014357 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 2   ? 15.618  0.958   4.252   1.00 39.41 ? 2   SER A N   1 
ATOM   2    C  CA  . SER A 1 2   ? 14.181  0.992   4.501   1.00 37.25 ? 2   SER A CA  1 
ATOM   3    C  C   . SER A 1 2   ? 13.748  -0.168  5.391   1.00 36.65 ? 2   SER A C   1 
ATOM   4    O  O   . SER A 1 2   ? 13.351  -1.225  4.901   1.00 37.88 ? 2   SER A O   1 
ATOM   5    C  CB  . SER A 1 2   ? 13.408  0.958   3.181   1.00 41.01 ? 2   SER A CB  1 
ATOM   6    O  OG  . SER A 1 2   ? 14.127  1.615   2.152   1.00 44.42 ? 2   SER A OG  1 
ATOM   7    N  N   . HIS A 1 3   ? 13.828  0.037   6.702   1.00 33.63 ? 3   HIS A N   1 
ATOM   8    C  CA  . HIS A 1 3   ? 13.443  -0.991  7.664   1.00 32.00 ? 3   HIS A CA  1 
ATOM   9    C  C   . HIS A 1 3   ? 12.329  -0.485  8.577   1.00 31.38 ? 3   HIS A C   1 
ATOM   10   O  O   . HIS A 1 3   ? 12.518  -0.292  9.776   1.00 31.14 ? 3   HIS A O   1 
ATOM   11   C  CB  . HIS A 1 3   ? 14.643  -1.449  8.489   1.00 32.55 ? 3   HIS A CB  1 
ATOM   12   C  CG  . HIS A 1 3   ? 14.421  -2.748  9.198   1.00 34.00 ? 3   HIS A CG  1 
ATOM   13   N  ND1 . HIS A 1 3   ? 13.943  -2.818  10.489  1.00 33.83 ? 3   HIS A ND1 1 
ATOM   14   C  CD2 . HIS A 1 3   ? 14.603  -4.027  8.794   1.00 32.68 ? 3   HIS A CD2 1 
ATOM   15   C  CE1 . HIS A 1 3   ? 13.848  -4.084  10.851  1.00 33.97 ? 3   HIS A CE1 1 
ATOM   16   N  NE2 . HIS A 1 3   ? 14.241  -4.838  9.841   1.00 34.73 ? 3   HIS A NE2 1 
ATOM   17   N  N   . HIS A 1 4   ? 11.167  -0.277  7.974   1.00 28.05 ? 4   HIS A N   1 
ATOM   18   C  CA  . HIS A 1 4   ? 9.983   0.257   8.632   1.00 24.87 ? 4   HIS A CA  1 
ATOM   19   C  C   . HIS A 1 4   ? 9.294   -0.881  9.436   1.00 20.94 ? 4   HIS A C   1 
ATOM   20   O  O   . HIS A 1 4   ? 9.441   -2.071  9.140   1.00 18.70 ? 4   HIS A O   1 
ATOM   21   C  CB  . HIS A 1 4   ? 9.074   0.685   7.468   1.00 26.22 ? 4   HIS A CB  1 
ATOM   22   C  CG  . HIS A 1 4   ? 7.738   1.226   7.882   1.00 31.82 ? 4   HIS A CG  1 
ATOM   23   N  ND1 . HIS A 1 4   ? 7.536   2.553   8.227   1.00 35.76 ? 4   HIS A ND1 1 
ATOM   24   C  CD2 . HIS A 1 4   ? 6.526   0.615   7.991   1.00 34.64 ? 4   HIS A CD2 1 
ATOM   25   C  CE1 . HIS A 1 4   ? 6.256   2.728   8.537   1.00 36.92 ? 4   HIS A CE1 1 
ATOM   26   N  NE2 . HIS A 1 4   ? 5.624   1.566   8.395   1.00 36.07 ? 4   HIS A NE2 1 
ATOM   27   N  N   . TRP A 1 5   ? 8.486   -0.487  10.394  1.00 17.60 ? 5   TRP A N   1 
ATOM   28   C  CA  . TRP A 1 5   ? 7.793   -1.492  11.266  1.00 14.62 ? 5   TRP A CA  1 
ATOM   29   C  C   . TRP A 1 5   ? 6.822   -2.275  10.424  1.00 13.28 ? 5   TRP A C   1 
ATOM   30   O  O   . TRP A 1 5   ? 6.318   -1.778  9.401   1.00 13.56 ? 5   TRP A O   1 
ATOM   31   C  CB  . TRP A 1 5   ? 7.058   -0.818  12.434  1.00 15.03 ? 5   TRP A CB  1 
ATOM   32   C  CG  . TRP A 1 5   ? 5.941   0.030   12.052  1.00 16.51 ? 5   TRP A CG  1 
ATOM   33   C  CD1 . TRP A 1 5   ? 5.961   1.358   11.705  1.00 15.85 ? 5   TRP A CD1 1 
ATOM   34   C  CD2 . TRP A 1 5   ? 4.578   -0.403  11.994  1.00 13.90 ? 5   TRP A CD2 1 
ATOM   35   N  NE1 . TRP A 1 5   ? 4.673   1.777   11.407  1.00 16.19 ? 5   TRP A NE1 1 
ATOM   36   C  CE2 . TRP A 1 5   ? 3.806   0.713   11.585  1.00 14.88 ? 5   TRP A CE2 1 
ATOM   37   C  CE3 . TRP A 1 5   ? 3.944   -1.638  12.301  1.00 11.59 ? 5   TRP A CE3 1 
ATOM   38   C  CZ2 . TRP A 1 5   ? 2.419   0.667   11.428  1.00 13.37 ? 5   TRP A CZ2 1 
ATOM   39   C  CZ3 . TRP A 1 5   ? 2.545   -1.721  12.058  1.00 10.91 ? 5   TRP A CZ3 1 
ATOM   40   C  CH2 . TRP A 1 5   ? 1.798   -0.535  11.663  1.00 12.85 ? 5   TRP A CH2 1 
ATOM   41   N  N   . GLY A 1 6   ? 6.497   -3.475  10.906  1.00 14.30 ? 6   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 6   ? 5.482   -4.276  10.269  1.00 12.52 ? 6   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 6   ? 5.116   -5.437  11.201  1.00 12.74 ? 6   GLY A C   1 
ATOM   44   O  O   . GLY A 1 6   ? 5.153   -5.313  12.434  1.00 11.05 ? 6   GLY A O   1 
ATOM   45   N  N   . TYR A 1 7   ? 4.729   -6.547  10.566  1.00 15.81 ? 7   TYR A N   1 
ATOM   46   C  CA  . TYR A 1 7   ? 4.408   -7.769  11.342  1.00 16.43 ? 7   TYR A CA  1 
ATOM   47   C  C   . TYR A 1 7   ? 5.230   -9.010  10.891  1.00 22.65 ? 7   TYR A C   1 
ATOM   48   O  O   . TYR A 1 7   ? 4.628   -10.086 10.631  1.00 25.05 ? 7   TYR A O   1 
ATOM   49   C  CB  . TYR A 1 7   ? 2.939   -8.065  11.201  1.00 16.60 ? 7   TYR A CB  1 
ATOM   50   C  CG  . TYR A 1 7   ? 2.015   -6.966  11.729  1.00 12.72 ? 7   TYR A CG  1 
ATOM   51   C  CD1 . TYR A 1 7   ? 1.547   -7.004  13.063  1.00 11.00 ? 7   TYR A CD1 1 
ATOM   52   C  CD2 . TYR A 1 7   ? 1.573   -5.955  10.870  1.00 9.76  ? 7   TYR A CD2 1 
ATOM   53   C  CE1 . TYR A 1 7   ? 0.682   -5.945  13.590  1.00 9.36  ? 7   TYR A CE1 1 
ATOM   54   C  CE2 . TYR A 1 7   ? 0.708   -4.885  11.351  1.00 9.45  ? 7   TYR A CE2 1 
ATOM   55   C  CZ  . TYR A 1 7   ? 0.238   -4.957  12.713  1.00 11.38 ? 7   TYR A CZ  1 
ATOM   56   O  OH  . TYR A 1 7   ? -0.601  -3.928  13.085  1.00 9.58  ? 7   TYR A OH  1 
ATOM   57   N  N   . GLY A 1 8   ? 6.551   -8.866  10.711  1.00 22.64 ? 8   GLY A N   1 
ATOM   58   C  CA  . GLY A 1 8   ? 7.443   -10.087 10.630  1.00 20.86 ? 8   GLY A CA  1 
ATOM   59   C  C   . GLY A 1 8   ? 8.510   -10.291 11.664  1.00 22.78 ? 8   GLY A C   1 
ATOM   60   O  O   . GLY A 1 8   ? 8.555   -9.620  12.759  1.00 24.90 ? 8   GLY A O   1 
ATOM   61   N  N   . LYS A 1 9   ? 9.455   -11.216 11.344  1.00 25.07 ? 9   LYS A N   1 
ATOM   62   C  CA  . LYS A 1 9   ? 10.485  -11.663 12.320  1.00 25.33 ? 9   LYS A CA  1 
ATOM   63   C  C   . LYS A 1 9   ? 11.375  -10.560 12.699  1.00 25.38 ? 9   LYS A C   1 
ATOM   64   O  O   . LYS A 1 9   ? 11.759  -10.492 13.915  1.00 25.60 ? 9   LYS A O   1 
ATOM   65   C  CB  . LYS A 1 9   ? 11.345  -12.776 11.798  1.00 26.10 ? 9   LYS A CB  1 
ATOM   66   C  CG  . LYS A 1 9   ? 12.493  -13.251 12.704  1.00 26.60 ? 9   LYS A CG  1 
ATOM   67   C  CD  . LYS A 1 9   ? 12.944  -14.573 12.059  1.00 31.13 ? 9   LYS A CD  1 
ATOM   68   C  CE  . LYS A 1 9   ? 14.434  -14.883 12.255  1.00 35.58 ? 9   LYS A CE  1 
ATOM   69   N  NZ  . LYS A 1 9   ? 14.992  -15.555 10.988  1.00 35.59 ? 9   LYS A NZ  1 
ATOM   70   N  N   . HIS A 1 10  ? 11.693  -9.724  11.677  1.00 23.90 ? 10  HIS A N   1 
ATOM   71   C  CA  . HIS A 1 10  ? 12.692  -8.715  11.896  1.00 23.17 ? 10  HIS A CA  1 
ATOM   72   C  C   . HIS A 1 10  ? 12.099  -7.386  12.063  1.00 20.08 ? 10  HIS A C   1 
ATOM   73   O  O   . HIS A 1 10  ? 12.822  -6.561  12.527  1.00 18.63 ? 10  HIS A O   1 
ATOM   74   C  CB  . HIS A 1 10  ? 13.827  -8.722  10.819  1.00 21.10 ? 10  HIS A CB  1 
ATOM   75   C  CG  . HIS A 1 10  ? 14.395  -10.118 10.606  1.00 23.05 ? 10  HIS A CG  1 
ATOM   76   N  ND1 . HIS A 1 10  ? 15.391  -10.656 11.410  1.00 26.72 ? 10  HIS A ND1 1 
ATOM   77   C  CD2 . HIS A 1 10  ? 14.058  -11.075 9.724   1.00 22.01 ? 10  HIS A CD2 1 
ATOM   78   C  CE1 . HIS A 1 10  ? 15.664  -11.884 10.995  1.00 25.78 ? 10  HIS A CE1 1 
ATOM   79   N  NE2 . HIS A 1 10  ? 14.837  -12.182 10.002  1.00 21.26 ? 10  HIS A NE2 1 
ATOM   80   N  N   . ASN A 1 11  ? 10.774  -7.197  11.787  1.00 19.68 ? 11  ASN A N   1 
ATOM   81   C  CA  . ASN A 1 11  ? 10.179  -5.862  12.067  1.00 17.31 ? 11  ASN A CA  1 
ATOM   82   C  C   . ASN A 1 11  ? 8.819   -5.887  12.815  1.00 16.47 ? 11  ASN A C   1 
ATOM   83   O  O   . ASN A 1 11  ? 8.147   -4.856  12.859  1.00 15.26 ? 11  ASN A O   1 
ATOM   84   C  CB  . ASN A 1 11  ? 9.957   -5.098  10.756  1.00 14.52 ? 11  ASN A CB  1 
ATOM   85   C  CG  . ASN A 1 11  ? 8.900   -5.680  9.884   1.00 14.92 ? 11  ASN A CG  1 
ATOM   86   O  OD1 . ASN A 1 11  ? 8.325   -6.796  10.124  1.00 17.73 ? 11  ASN A OD1 1 
ATOM   87   N  ND2 . ASN A 1 11  ? 8.571   -4.932  8.841   1.00 17.77 ? 11  ASN A ND2 1 
ATOM   88   N  N   . GLY A 1 12  ? 8.448   -7.037  13.338  1.00 14.07 ? 12  GLY A N   1 
ATOM   89   C  CA  . GLY A 1 12  ? 7.094   -7.124  13.995  1.00 14.26 ? 12  GLY A CA  1 
ATOM   90   C  C   . GLY A 1 12  ? 7.130   -6.597  15.431  1.00 13.95 ? 12  GLY A C   1 
ATOM   91   O  O   . GLY A 1 12  ? 8.044   -5.865  15.952  1.00 12.15 ? 12  GLY A O   1 
ATOM   92   N  N   . PRO A 1 13  ? 6.036   -6.902  16.165  1.00 13.48 ? 13  PRO A N   1 
ATOM   93   C  CA  . PRO A 1 13  ? 5.775   -6.257  17.437  1.00 14.39 ? 13  PRO A CA  1 
ATOM   94   C  C   . PRO A 1 13  ? 6.895   -6.258  18.467  1.00 12.93 ? 13  PRO A C   1 
ATOM   95   O  O   . PRO A 1 13  ? 7.107   -5.264  19.157  1.00 14.02 ? 13  PRO A O   1 
ATOM   96   C  CB  . PRO A 1 13  ? 4.547   -7.055  17.979  1.00 13.75 ? 13  PRO A CB  1 
ATOM   97   C  CG  . PRO A 1 13  ? 3.820   -7.424  16.845  1.00 11.37 ? 13  PRO A CG  1 
ATOM   98   C  CD  . PRO A 1 13  ? 4.914   -7.753  15.721  1.00 14.04 ? 13  PRO A CD  1 
ATOM   99   N  N   . GLU A 1 14  ? 7.631   -7.353  18.560  1.00 12.95 ? 14  GLU A N   1 
ATOM   100  C  CA  . GLU A 1 14  ? 8.764   -7.410  19.465  1.00 14.38 ? 14  GLU A CA  1 
ATOM   101  C  C   . GLU A 1 14  ? 9.963   -6.436  19.132  1.00 11.62 ? 14  GLU A C   1 
ATOM   102  O  O   . GLU A 1 14  ? 10.805  -6.240  19.975  1.00 13.60 ? 14  GLU A O   1 
ATOM   103  C  CB  . GLU A 1 14  ? 9.286   -8.837  19.483  1.00 17.08 ? 14  GLU A CB  1 
ATOM   104  C  CG  . GLU A 1 14  ? 10.069  -9.241  18.205  1.00 19.33 ? 14  GLU A CG  1 
ATOM   105  C  CD  . GLU A 1 14  ? 9.207   -9.866  17.102  1.00 26.68 ? 14  GLU A CD  1 
ATOM   106  O  OE1 . GLU A 1 14  ? 7.989   -9.596  17.056  1.00 16.06 ? 14  GLU A OE1 1 
ATOM   107  O  OE2 . GLU A 1 14  ? 9.759   -10.628 16.275  1.00 21.83 ? 14  GLU A OE2 1 
ATOM   108  N  N   . HIS A 1 15  ? 9.955   -5.884  17.925  1.00 11.52 ? 15  HIS A N   1 
ATOM   109  C  CA  . HIS A 1 15  ? 10.918  -4.899  17.452  1.00 10.90 ? 15  HIS A CA  1 
ATOM   110  C  C   . HIS A 1 15  ? 10.501  -3.470  17.622  1.00 13.63 ? 15  HIS A C   1 
ATOM   111  O  O   . HIS A 1 15  ? 11.365  -2.549  17.612  1.00 12.46 ? 15  HIS A O   1 
ATOM   112  C  CB  . HIS A 1 15  ? 11.291  -5.102  15.986  1.00 12.36 ? 15  HIS A CB  1 
ATOM   113  C  CG  . HIS A 1 15  ? 11.998  -6.402  15.778  1.00 17.40 ? 15  HIS A CG  1 
ATOM   114  N  ND1 . HIS A 1 15  ? 13.370  -6.525  15.959  1.00 16.83 ? 15  HIS A ND1 1 
ATOM   115  C  CD2 . HIS A 1 15  ? 11.538  -7.628  15.434  1.00 18.20 ? 15  HIS A CD2 1 
ATOM   116  C  CE1 . HIS A 1 15  ? 13.708  -7.792  15.759  1.00 19.19 ? 15  HIS A CE1 1 
ATOM   117  N  NE2 . HIS A 1 15  ? 12.634  -8.480  15.435  1.00 17.57 ? 15  HIS A NE2 1 
ATOM   118  N  N   . TRP A 1 16  ? 9.202   -3.257  17.865  1.00 10.11 ? 16  TRP A N   1 
ATOM   119  C  CA  . TRP A 1 16  ? 8.729   -1.900  17.815  1.00 11.79 ? 16  TRP A CA  1 
ATOM   120  C  C   . TRP A 1 16  ? 9.305   -0.927  18.848  1.00 9.39  ? 16  TRP A C   1 
ATOM   121  O  O   . TRP A 1 16  ? 9.351   0.298   18.504  1.00 12.35 ? 16  TRP A O   1 
ATOM   122  C  CB  . TRP A 1 16  ? 7.183   -1.930  17.947  1.00 10.02 ? 16  TRP A CB  1 
ATOM   123  C  CG  . TRP A 1 16  ? 6.509   -2.546  16.755  1.00 8.86  ? 16  TRP A CG  1 
ATOM   124  C  CD1 . TRP A 1 16  ? 7.058   -3.005  15.554  1.00 7.75  ? 16  TRP A CD1 1 
ATOM   125  C  CD2 . TRP A 1 16  ? 5.080   -2.874  16.661  1.00 6.77  ? 16  TRP A CD2 1 
ATOM   126  N  NE1 . TRP A 1 16  ? 6.089   -3.589  14.757  1.00 10.44 ? 16  TRP A NE1 1 
ATOM   127  C  CE2 . TRP A 1 16  ? 4.872   -3.467  15.389  1.00 8.83  ? 16  TRP A CE2 1 
ATOM   128  C  CE3 . TRP A 1 16  ? 3.988   -2.647  17.541  1.00 11.53 ? 16  TRP A CE3 1 
ATOM   129  C  CZ2 . TRP A 1 16  ? 3.597   -3.876  14.958  1.00 12.14 ? 16  TRP A CZ2 1 
ATOM   130  C  CZ3 . TRP A 1 16  ? 2.773   -3.045  17.121  1.00 10.91 ? 16  TRP A CZ3 1 
ATOM   131  C  CH2 . TRP A 1 16  ? 2.559   -3.649  15.880  1.00 10.62 ? 16  TRP A CH2 1 
ATOM   132  N  N   . HIS A 1 17  ? 9.740   -1.422  20.005  1.00 10.88 ? 17  HIS A N   1 
ATOM   133  C  CA  . HIS A 1 17  ? 10.220  -0.547  21.068  1.00 11.02 ? 17  HIS A CA  1 
ATOM   134  C  C   . HIS A 1 17  ? 11.449  0.276   20.623  1.00 12.01 ? 17  HIS A C   1 
ATOM   135  O  O   . HIS A 1 17  ? 11.682  1.301   21.220  1.00 12.56 ? 17  HIS A O   1 
ATOM   136  C  CB  . HIS A 1 17  ? 10.508  -1.289  22.334  1.00 10.81 ? 17  HIS A CB  1 
ATOM   137  C  CG  . HIS A 1 17  ? 11.695  -2.194  22.217  1.00 13.39 ? 17  HIS A CG  1 
ATOM   138  N  ND1 . HIS A 1 17  ? 12.934  -1.806  22.663  1.00 18.73 ? 17  HIS A ND1 1 
ATOM   139  C  CD2 . HIS A 1 17  ? 11.860  -3.394  21.627  1.00 16.77 ? 17  HIS A CD2 1 
ATOM   140  C  CE1 . HIS A 1 17  ? 13.819  -2.738  22.351  1.00 13.42 ? 17  HIS A CE1 1 
ATOM   141  N  NE2 . HIS A 1 17  ? 13.197  -3.709  21.716  1.00 14.61 ? 17  HIS A NE2 1 
ATOM   142  N  N   . LYS A 1 18  ? 12.186  -0.242  19.635  1.00 14.23 ? 18  LYS A N   1 
ATOM   143  C  CA  . LYS A 1 18  ? 13.458  0.443   19.210  1.00 16.65 ? 18  LYS A CA  1 
ATOM   144  C  C   . LYS A 1 18  ? 13.105  1.777   18.541  1.00 16.59 ? 18  LYS A C   1 
ATOM   145  O  O   . LYS A 1 18  ? 13.611  2.818   18.981  1.00 19.96 ? 18  LYS A O   1 
ATOM   146  C  CB  . LYS A 1 18  ? 14.276  -0.458  18.274  1.00 16.98 ? 18  LYS A CB  1 
ATOM   147  C  CG  . LYS A 1 18  ? 14.947  -1.657  19.021  1.00 14.14 ? 18  LYS A CG  1 
ATOM   148  C  CD  . LYS A 1 18  ? 15.550  -2.699  17.994  1.00 17.39 ? 18  LYS A CD  1 
ATOM   149  C  CE  . LYS A 1 18  ? 14.534  -3.617  17.322  1.00 15.63 ? 18  LYS A CE  1 
ATOM   150  N  NZ  . LYS A 1 18  ? 15.248  -4.510  16.338  1.00 14.20 ? 18  LYS A NZ  1 
ATOM   151  N  N   . ASP A 1 19  ? 12.115  1.795   17.632  1.00 15.79 ? 19  ASP A N   1 
ATOM   152  C  CA  . ASP A 1 19  ? 11.636  3.086   17.071  1.00 16.42 ? 19  ASP A CA  1 
ATOM   153  C  C   . ASP A 1 19  ? 10.629  3.848   17.970  1.00 16.42 ? 19  ASP A C   1 
ATOM   154  O  O   . ASP A 1 19  ? 10.528  5.063   17.929  1.00 16.16 ? 19  ASP A O   1 
ATOM   155  C  CB  . ASP A 1 19  ? 11.099  2.942   15.659  1.00 17.78 ? 19  ASP A CB  1 
ATOM   156  C  CG  . ASP A 1 19  ? 12.198  2.942   14.616  1.00 24.77 ? 19  ASP A CG  1 
ATOM   157  O  OD1 . ASP A 1 19  ? 13.221  3.555   14.859  1.00 28.80 ? 19  ASP A OD1 1 
ATOM   158  O  OD2 . ASP A 1 19  ? 12.044  2.273   13.590  1.00 31.61 ? 19  ASP A OD2 1 
ATOM   159  N  N   . PHE A 1 20  ? 9.893   3.089   18.804  1.00 13.41 ? 20  PHE A N   1 
ATOM   160  C  CA  . PHE A 1 20  ? 8.719   3.615   19.558  1.00 13.19 ? 20  PHE A CA  1 
ATOM   161  C  C   . PHE A 1 20  ? 8.830   3.140   20.965  1.00 13.86 ? 20  PHE A C   1 
ATOM   162  O  O   . PHE A 1 20  ? 8.233   2.147   21.379  1.00 12.21 ? 20  PHE A O   1 
ATOM   163  C  CB  . PHE A 1 20  ? 7.384   3.157   18.878  1.00 11.54 ? 20  PHE A CB  1 
ATOM   164  C  CG  . PHE A 1 20  ? 7.276   3.589   17.480  1.00 11.21 ? 20  PHE A CG  1 
ATOM   165  C  CD1 . PHE A 1 20  ? 6.888   4.887   17.142  1.00 14.47 ? 20  PHE A CD1 1 
ATOM   166  C  CD2 . PHE A 1 20  ? 7.667   2.711   16.426  1.00 11.26 ? 20  PHE A CD2 1 
ATOM   167  C  CE1 . PHE A 1 20  ? 6.841   5.215   15.820  1.00 13.52 ? 20  PHE A CE1 1 
ATOM   168  C  CE2 . PHE A 1 20  ? 7.626   3.069   15.061  1.00 15.69 ? 20  PHE A CE2 1 
ATOM   169  C  CZ  . PHE A 1 20  ? 7.261   4.328   14.785  1.00 14.23 ? 20  PHE A CZ  1 
ATOM   170  N  N   . PRO A 1 21  ? 9.692   3.788   21.775  1.00 13.55 ? 21  PRO A N   1 
ATOM   171  C  CA  . PRO A 1 21  ? 9.968   3.236   23.049  1.00 12.80 ? 21  PRO A CA  1 
ATOM   172  C  C   . PRO A 1 21  ? 8.774   3.104   24.010  1.00 12.76 ? 21  PRO A C   1 
ATOM   173  O  O   . PRO A 1 21  ? 8.814   2.385   24.947  1.00 11.90 ? 21  PRO A O   1 
ATOM   174  C  CB  . PRO A 1 21  ? 11.100  4.131   23.648  1.00 16.00 ? 21  PRO A CB  1 
ATOM   175  C  CG  . PRO A 1 21  ? 11.531  5.032   22.524  1.00 18.33 ? 21  PRO A CG  1 
ATOM   176  C  CD  . PRO A 1 21  ? 10.560  4.925   21.369  1.00 14.28 ? 21  PRO A CD  1 
ATOM   177  N  N   . ILE A 1 22  ? 7.711   3.917   23.742  1.00 10.78 ? 22  ILE A N   1 
ATOM   178  C  CA  . ILE A 1 22  ? 6.497   3.844   24.502  1.00 11.51 ? 22  ILE A CA  1 
ATOM   179  C  C   . ILE A 1 22  ? 5.889   2.445   24.323  1.00 8.58  ? 22  ILE A C   1 
ATOM   180  O  O   . ILE A 1 22  ? 4.942   2.103   25.068  1.00 9.41  ? 22  ILE A O   1 
ATOM   181  C  CB  . ILE A 1 22  ? 5.475   4.939   24.015  1.00 8.60  ? 22  ILE A CB  1 
ATOM   182  C  CG1 . ILE A 1 22  ? 4.477   5.328   25.059  1.00 11.67 ? 22  ILE A CG1 1 
ATOM   183  C  CG2 . ILE A 1 22  ? 4.877   4.499   22.615  1.00 12.01 ? 22  ILE A CG2 1 
ATOM   184  C  CD1 . ILE A 1 22  ? 3.451   6.403   24.580  1.00 13.99 ? 22  ILE A CD1 1 
ATOM   185  N  N   . ALA A 1 23  ? 6.393   1.638   23.393  1.00 9.95  ? 23  ALA A N   1 
ATOM   186  C  CA  . ALA A 1 23  ? 5.960   0.205   23.306  1.00 12.16 ? 23  ALA A CA  1 
ATOM   187  C  C   . ALA A 1 23  ? 6.028   -0.528  24.644  1.00 12.28 ? 23  ALA A C   1 
ATOM   188  O  O   . ALA A 1 23  ? 5.283   -1.530  24.830  1.00 10.73 ? 23  ALA A O   1 
ATOM   189  C  CB  . ALA A 1 23  ? 6.731   -0.623  22.258  1.00 12.68 ? 23  ALA A CB  1 
ATOM   190  N  N   . LYS A 1 24  ? 6.936   -0.133  25.572  1.00 13.06 ? 24  LYS A N   1 
ATOM   191  C  CA  . LYS A 1 24  ? 7.124   -0.807  26.900  1.00 13.05 ? 24  LYS A CA  1 
ATOM   192  C  C   . LYS A 1 24  ? 6.528   0.105   27.989  1.00 13.82 ? 24  LYS A C   1 
ATOM   193  O  O   . LYS A 1 24  ? 6.917   0.019   29.181  1.00 15.09 ? 24  LYS A O   1 
ATOM   194  C  CB  . LYS A 1 24  ? 8.664   -0.986  27.164  1.00 11.84 ? 24  LYS A CB  1 
ATOM   195  C  CG  . LYS A 1 24  ? 9.321   -1.914  26.176  1.00 16.25 ? 24  LYS A CG  1 
ATOM   196  C  CD  . LYS A 1 24  ? 10.707  -2.180  26.758  1.00 21.48 ? 24  LYS A CD  1 
ATOM   197  C  CE  . LYS A 1 24  ? 11.575  -3.003  25.804  1.00 19.83 ? 24  LYS A CE  1 
ATOM   198  N  NZ  . LYS A 1 24  ? 11.147  -4.407  25.832  1.00 24.06 ? 24  LYS A NZ  1 
ATOM   199  N  N   . GLY A 1 25  ? 5.571   0.989   27.599  1.00 10.85 ? 25  GLY A N   1 
ATOM   200  C  CA  . GLY A 1 25  ? 4.929   1.952   28.490  1.00 11.61 ? 25  GLY A CA  1 
ATOM   201  C  C   . GLY A 1 25  ? 3.952   1.370   29.491  1.00 11.00 ? 25  GLY A C   1 
ATOM   202  O  O   . GLY A 1 25  ? 3.770   0.105   29.640  1.00 13.77 ? 25  GLY A O   1 
ATOM   203  N  N   . GLU A 1 26  ? 3.296   2.297   30.189  1.00 11.77 ? 26  GLU A N   1 
ATOM   204  C  CA  . GLU A 1 26  ? 2.456   1.896   31.308  1.00 11.19 ? 26  GLU A CA  1 
ATOM   205  C  C   . GLU A 1 26  ? 1.000   1.659   30.928  1.00 9.32  ? 26  GLU A C   1 
ATOM   206  O  O   . GLU A 1 26  ? 0.251   1.116   31.771  1.00 10.63 ? 26  GLU A O   1 
ATOM   207  C  CB  . GLU A 1 26  ? 2.434   2.977   32.413  1.00 14.37 ? 26  GLU A CB  1 
ATOM   208  C  CG  . GLU A 1 26  ? 3.815   3.239   33.027  1.00 16.63 ? 26  GLU A CG  1 
ATOM   209  C  CD  . GLU A 1 26  ? 4.360   1.957   33.625  1.00 26.91 ? 26  GLU A CD  1 
ATOM   210  O  OE1 . GLU A 1 26  ? 3.665   1.324   34.494  1.00 29.72 ? 26  GLU A OE1 1 
ATOM   211  O  OE2 . GLU A 1 26  ? 5.455   1.550   33.194  1.00 30.65 ? 26  GLU A OE2 1 
ATOM   212  N  N   . ARG A 1 27  ? 0.606   2.033   29.700  1.00 9.00  ? 27  ARG A N   1 
ATOM   213  C  CA  . ARG A 1 27  ? -0.823  1.753   29.376  1.00 9.52  ? 27  ARG A CA  1 
ATOM   214  C  C   . ARG A 1 27  ? -0.917  1.260   27.918  1.00 8.38  ? 27  ARG A C   1 
ATOM   215  O  O   . ARG A 1 27  ? -1.604  1.855   27.046  1.00 8.89  ? 27  ARG A O   1 
ATOM   216  C  CB  . ARG A 1 27  ? -1.778  2.933   29.724  1.00 7.40  ? 27  ARG A CB  1 
ATOM   217  C  CG  . ARG A 1 27  ? -1.462  4.210   28.970  1.00 12.89 ? 27  ARG A CG  1 
ATOM   218  C  CD  . ARG A 1 27  ? -2.454  5.301   29.310  1.00 20.78 ? 27  ARG A CD  1 
ATOM   219  N  NE  . ARG A 1 27  ? -3.604  5.285   28.413  1.00 16.20 ? 27  ARG A NE  1 
ATOM   220  C  CZ  . ARG A 1 27  ? -4.492  6.268   28.324  1.00 13.42 ? 27  ARG A CZ  1 
ATOM   221  N  NH1 . ARG A 1 27  ? -4.363  7.348   29.082  1.00 12.67 ? 27  ARG A NH1 1 
ATOM   222  N  NH2 . ARG A 1 27  ? -5.510  6.172   27.480  1.00 14.03 ? 27  ARG A NH2 1 
ATOM   223  N  N   . GLN A 1 28  ? -0.188  0.141   27.646  1.00 8.30  ? 28  GLN A N   1 
ATOM   224  C  CA  . GLN A 1 28  ? -0.132  -0.318  26.240  1.00 7.87  ? 28  GLN A CA  1 
ATOM   225  C  C   . GLN A 1 28  ? -1.304  -1.303  25.978  1.00 7.65  ? 28  GLN A C   1 
ATOM   226  O  O   . GLN A 1 28  ? -1.790  -1.994  26.882  1.00 8.03  ? 28  GLN A O   1 
ATOM   227  C  CB  . GLN A 1 28  ? 1.208   -1.051  25.968  1.00 9.96  ? 28  GLN A CB  1 
ATOM   228  C  CG  . GLN A 1 28  ? 2.356   0.052   25.869  1.00 7.68  ? 28  GLN A CG  1 
ATOM   229  C  CD  . GLN A 1 28  ? 2.186   0.861   24.531  1.00 5.46  ? 28  GLN A CD  1 
ATOM   230  O  OE1 . GLN A 1 28  ? 2.337   0.313   23.455  1.00 9.41  ? 28  GLN A OE1 1 
ATOM   231  N  NE2 . GLN A 1 28  ? 1.817   2.161   24.628  1.00 6.91  ? 28  GLN A NE2 1 
ATOM   232  N  N   . SER A 1 29  ? -1.681  -1.330  24.711  1.00 6.64  ? 29  SER A N   1 
ATOM   233  C  CA  . SER A 1 29  ? -2.734  -2.227  24.198  1.00 7.16  ? 29  SER A CA  1 
ATOM   234  C  C   . SER A 1 29  ? -2.212  -3.134  23.090  1.00 5.36  ? 29  SER A C   1 
ATOM   235  O  O   . SER A 1 29  ? -1.311  -2.746  22.335  1.00 7.38  ? 29  SER A O   1 
ATOM   236  C  CB  . SER A 1 29  ? -3.898  -1.403  23.606  1.00 4.16  ? 29  SER A CB  1 
ATOM   237  O  OG  . SER A 1 29  ? -4.522  -0.724  24.766  1.00 5.98  ? 29  SER A OG  1 
ATOM   238  N  N   . PRO A 1 30  ? -2.906  -4.281  22.871  1.00 6.04  ? 30  PRO A N   1 
ATOM   239  C  CA  . PRO A 1 30  ? -4.041  -4.850  23.580  1.00 5.31  ? 30  PRO A CA  1 
ATOM   240  C  C   . PRO A 1 30  ? -3.626  -5.548  24.895  1.00 4.88  ? 30  PRO A C   1 
ATOM   241  O  O   . PRO A 1 30  ? -2.376  -5.514  25.228  1.00 6.62  ? 30  PRO A O   1 
ATOM   242  C  CB  . PRO A 1 30  ? -4.567  -5.876  22.529  1.00 5.62  ? 30  PRO A CB  1 
ATOM   243  C  CG  . PRO A 1 30  ? -3.290  -6.477  21.937  1.00 8.64  ? 30  PRO A CG  1 
ATOM   244  C  CD  . PRO A 1 30  ? -2.410  -5.176  21.803  1.00 5.92  ? 30  PRO A CD  1 
ATOM   245  N  N   . VAL A 1 31  ? -4.634  -6.060  25.586  1.00 5.96  ? 31  VAL A N   1 
ATOM   246  C  CA  . VAL A 1 31  ? -4.480  -6.807  26.809  1.00 7.12  ? 31  VAL A CA  1 
ATOM   247  C  C   . VAL A 1 31  ? -5.374  -8.015  26.801  1.00 7.80  ? 31  VAL A C   1 
ATOM   248  O  O   . VAL A 1 31  ? -6.333  -8.111  26.048  1.00 8.18  ? 31  VAL A O   1 
ATOM   249  C  CB  . VAL A 1 31  ? -4.733  -5.924  28.089  1.00 9.24  ? 31  VAL A CB  1 
ATOM   250  C  CG1 . VAL A 1 31  ? -3.725  -4.706  28.158  1.00 5.99  ? 31  VAL A CG1 1 
ATOM   251  C  CG2 . VAL A 1 31  ? -6.216  -5.486  28.205  1.00 9.02  ? 31  VAL A CG2 1 
ATOM   252  N  N   . ASP A 1 32  ? -4.958  -8.985  27.610  1.00 7.64  ? 32  ASP A N   1 
ATOM   253  C  CA  . ASP A 1 32  ? -5.859  -10.110 27.907  1.00 7.67  ? 32  ASP A CA  1 
ATOM   254  C  C   . ASP A 1 32  ? -6.926  -9.580  28.879  1.00 8.86  ? 32  ASP A C   1 
ATOM   255  O  O   . ASP A 1 32  ? -6.605  -8.910  29.875  1.00 8.50  ? 32  ASP A O   1 
ATOM   256  C  CB  . ASP A 1 32  ? -5.081  -11.241 28.527  1.00 9.83  ? 32  ASP A CB  1 
ATOM   257  C  CG  . ASP A 1 32  ? -6.002  -12.456 28.836  1.00 10.05 ? 32  ASP A CG  1 
ATOM   258  O  OD1 . ASP A 1 32  ? -6.729  -12.890 27.913  1.00 8.88  ? 32  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A 1 32  ? -6.039  -12.939 30.044  1.00 12.51 ? 32  ASP A OD2 1 
ATOM   260  N  N   . ILE A 1 33  ? -8.183  -9.884  28.586  1.00 7.79  ? 33  ILE A N   1 
ATOM   261  C  CA  . ILE A 1 33  ? -9.311  -9.541  29.455  1.00 8.09  ? 33  ILE A CA  1 
ATOM   262  C  C   . ILE A 1 33  ? -9.631  -10.762 30.332  1.00 8.62  ? 33  ILE A C   1 
ATOM   263  O  O   . ILE A 1 33  ? -10.183 -11.776 29.852  1.00 10.07 ? 33  ILE A O   1 
ATOM   264  C  CB  . ILE A 1 33  ? -10.573 -9.084  28.665  1.00 7.77  ? 33  ILE A CB  1 
ATOM   265  C  CG1 . ILE A 1 33  ? -10.228 -7.767  27.904  1.00 8.37  ? 33  ILE A CG1 1 
ATOM   266  C  CG2 . ILE A 1 33  ? -11.707 -8.778  29.663  1.00 8.59  ? 33  ILE A CG2 1 
ATOM   267  C  CD1 . ILE A 1 33  ? -11.149 -7.512  26.649  1.00 8.82  ? 33  ILE A CD1 1 
ATOM   268  N  N   . ASP A 1 34  ? -9.135  -10.679 31.534  1.00 11.28 ? 34  ASP A N   1 
ATOM   269  C  CA  . ASP A 1 34  ? -9.442  -11.743 32.546  1.00 10.72 ? 34  ASP A CA  1 
ATOM   270  C  C   . ASP A 1 34  ? -10.877 -11.479 33.111  1.00 13.18 ? 34  ASP A C   1 
ATOM   271  O  O   . ASP A 1 34  ? -11.076 -10.510 33.907  1.00 12.46 ? 34  ASP A O   1 
ATOM   272  C  CB  . ASP A 1 34  ? -8.355  -11.678 33.635  1.00 11.87 ? 34  ASP A CB  1 
ATOM   273  C  CG  . ASP A 1 34  ? -8.600  -12.669 34.809  1.00 18.08 ? 34  ASP A CG  1 
ATOM   274  O  OD1 . ASP A 1 34  ? -9.732  -13.088 35.080  1.00 18.40 ? 34  ASP A OD1 1 
ATOM   275  O  OD2 . ASP A 1 34  ? -7.611  -13.052 35.485  1.00 28.38 ? 34  ASP A OD2 1 
ATOM   276  N  N   . THR A 1 35  ? -11.850 -12.231 32.629  1.00 12.81 ? 35  THR A N   1 
ATOM   277  C  CA  . THR A 1 35  ? -13.250 -11.885 32.844  1.00 13.82 ? 35  THR A CA  1 
ATOM   278  C  C   . THR A 1 35  ? -13.674 -12.067 34.292  1.00 15.30 ? 35  THR A C   1 
ATOM   279  O  O   . THR A 1 35  ? -14.670 -11.467 34.782  1.00 14.89 ? 35  THR A O   1 
ATOM   280  C  CB  . THR A 1 35  ? -14.195 -12.849 32.054  1.00 16.35 ? 35  THR A CB  1 
ATOM   281  O  OG1 . THR A 1 35  ? -13.963 -14.183 32.505  1.00 14.39 ? 35  THR A OG1 1 
ATOM   282  C  CG2 . THR A 1 35  ? -13.964 -12.798 30.542  1.00 10.57 ? 35  THR A CG2 1 
ATOM   283  N  N   . HIS A 1 36  ? -12.893 -12.899 35.018  1.00 14.40 ? 36  HIS A N   1 
ATOM   284  C  CA  . HIS A 1 36  ? -13.191 -13.111 36.450  1.00 16.13 ? 36  HIS A CA  1 
ATOM   285  C  C   . HIS A 1 36  ? -12.700 -11.929 37.327  1.00 18.23 ? 36  HIS A C   1 
ATOM   286  O  O   . HIS A 1 36  ? -13.387 -11.569 38.306  1.00 20.25 ? 36  HIS A O   1 
ATOM   287  C  CB  . HIS A 1 36  ? -12.722 -14.562 36.797  1.00 17.66 ? 36  HIS A CB  1 
ATOM   288  C  CG  . HIS A 1 36  ? -13.693 -15.584 36.273  1.00 18.63 ? 36  HIS A CG  1 
ATOM   289  N  ND1 . HIS A 1 36  ? -13.416 -16.549 35.315  1.00 17.52 ? 36  HIS A ND1 1 
ATOM   290  C  CD2 . HIS A 1 36  ? -15.014 -15.725 36.590  1.00 17.23 ? 36  HIS A CD2 1 
ATOM   291  C  CE1 . HIS A 1 36  ? -14.526 -17.223 35.057  1.00 18.60 ? 36  HIS A CE1 1 
ATOM   292  N  NE2 . HIS A 1 36  ? -15.505 -16.752 35.815  1.00 28.45 ? 36  HIS A NE2 1 
ATOM   293  N  N   . THR A 1 37  ? -11.634 -11.232 36.899  1.00 16.43 ? 37  THR A N   1 
ATOM   294  C  CA  . THR A 1 37  ? -10.968 -10.116 37.610  1.00 16.69 ? 37  THR A CA  1 
ATOM   295  C  C   . THR A 1 37  ? -11.531 -8.715  37.155  1.00 16.37 ? 37  THR A C   1 
ATOM   296  O  O   . THR A 1 37  ? -11.283 -7.689  37.821  1.00 17.22 ? 37  THR A O   1 
ATOM   297  C  CB  . THR A 1 37  ? -9.441  -10.200 37.392  1.00 20.51 ? 37  THR A CB  1 
ATOM   298  O  OG1 . THR A 1 37  ? -8.955  -11.276 38.205  1.00 24.55 ? 37  THR A OG1 1 
ATOM   299  C  CG2 . THR A 1 37  ? -8.680  -8.919  37.883  1.00 22.43 ? 37  THR A CG2 1 
ATOM   300  N  N   . ALA A 1 38  ? -12.259 -8.703  36.030  1.00 14.10 ? 38  ALA A N   1 
ATOM   301  C  CA  . ALA A 1 38  ? -12.886 -7.407  35.503  1.00 14.12 ? 38  ALA A CA  1 
ATOM   302  C  C   . ALA A 1 38  ? -13.993 -7.045  36.555  1.00 15.46 ? 38  ALA A C   1 
ATOM   303  O  O   . ALA A 1 38  ? -14.712 -7.929  36.987  1.00 20.31 ? 38  ALA A O   1 
ATOM   304  C  CB  . ALA A 1 38  ? -13.524 -7.619  34.167  1.00 15.44 ? 38  ALA A CB  1 
ATOM   305  N  N   . LYS A 1 39  ? -14.037 -5.792  36.977  1.00 16.73 ? 39  LYS A N   1 
ATOM   306  C  CA  . LYS A 1 39  ? -14.961 -5.405  38.050  1.00 17.98 ? 39  LYS A CA  1 
ATOM   307  C  C   . LYS A 1 39  ? -16.256 -4.938  37.362  1.00 15.19 ? 39  LYS A C   1 
ATOM   308  O  O   . LYS A 1 39  ? -16.216 -3.976  36.596  1.00 14.16 ? 39  LYS A O   1 
ATOM   309  C  CB  . LYS A 1 39  ? -14.268 -4.231  38.676  1.00 18.33 ? 39  LYS A CB  1 
ATOM   310  C  CG  . LYS A 1 39  ? -15.041 -3.440  39.774  1.00 22.18 ? 39  LYS A CG  1 
ATOM   311  C  CD  . LYS A 1 39  ? -15.047 -4.077  41.176  1.00 20.35 ? 39  LYS A CD  1 
ATOM   312  C  CE  . LYS A 1 39  ? -16.112 -3.370  41.997  1.00 24.37 ? 39  LYS A CE  1 
ATOM   313  N  NZ  . LYS A 1 39  ? -16.298 -3.932  43.375  1.00 29.08 ? 39  LYS A NZ  1 
ATOM   314  N  N   . TYR A 1 40  ? -17.408 -5.534  37.645  1.00 17.16 ? 40  TYR A N   1 
ATOM   315  C  CA  . TYR A 1 40  ? -18.638 -4.872  37.218  1.00 17.10 ? 40  TYR A CA  1 
ATOM   316  C  C   . TYR A 1 40  ? -18.777 -3.463  37.838  1.00 16.38 ? 40  TYR A C   1 
ATOM   317  O  O   . TYR A 1 40  ? -18.584 -3.264  39.090  1.00 16.95 ? 40  TYR A O   1 
ATOM   318  C  CB  . TYR A 1 40  ? -19.825 -5.768  37.552  1.00 20.59 ? 40  TYR A CB  1 
ATOM   319  C  CG  . TYR A 1 40  ? -21.109 -5.063  37.491  1.00 21.66 ? 40  TYR A CG  1 
ATOM   320  C  CD1 . TYR A 1 40  ? -21.589 -4.568  36.260  1.00 21.78 ? 40  TYR A CD1 1 
ATOM   321  C  CD2 . TYR A 1 40  ? -21.886 -4.908  38.632  1.00 27.76 ? 40  TYR A CD2 1 
ATOM   322  C  CE1 . TYR A 1 40  ? -22.750 -3.929  36.150  1.00 24.30 ? 40  TYR A CE1 1 
ATOM   323  C  CE2 . TYR A 1 40  ? -23.136 -4.222  38.530  1.00 23.17 ? 40  TYR A CE2 1 
ATOM   324  C  CZ  . TYR A 1 40  ? -23.533 -3.743  37.286  1.00 26.40 ? 40  TYR A CZ  1 
ATOM   325  O  OH  . TYR A 1 40  ? -24.702 -3.059  37.130  1.00 26.81 ? 40  TYR A OH  1 
ATOM   326  N  N   . ASP A 1 41  ? -19.165 -2.484  37.017  1.00 15.51 ? 41  ASP A N   1 
ATOM   327  C  CA  . ASP A 1 41  ? -19.146 -1.102  37.510  1.00 17.38 ? 41  ASP A CA  1 
ATOM   328  C  C   . ASP A 1 41  ? -20.531 -0.531  37.224  1.00 19.84 ? 41  ASP A C   1 
ATOM   329  O  O   . ASP A 1 41  ? -20.841 -0.165  36.077  1.00 18.94 ? 41  ASP A O   1 
ATOM   330  C  CB  . ASP A 1 41  ? -18.020 -0.245  36.894  1.00 18.42 ? 41  ASP A CB  1 
ATOM   331  C  CG  . ASP A 1 41  ? -18.073 1.204   37.374  1.00 23.03 ? 41  ASP A CG  1 
ATOM   332  O  OD1 . ASP A 1 41  ? -19.011 1.583   38.094  1.00 23.72 ? 41  ASP A OD1 1 
ATOM   333  O  OD2 . ASP A 1 41  ? -17.148 1.984   37.056  1.00 25.53 ? 41  ASP A OD2 1 
ATOM   334  N  N   . PRO A 1 42  ? -21.400 -0.526  38.263  1.00 22.77 ? 42  PRO A N   1 
ATOM   335  C  CA  . PRO A 1 42  ? -22.799 -0.148  38.030  1.00 22.84 ? 42  PRO A CA  1 
ATOM   336  C  C   . PRO A 1 42  ? -22.917 1.339   37.647  1.00 22.50 ? 42  PRO A C   1 
ATOM   337  O  O   . PRO A 1 42  ? -23.976 1.761   37.083  1.00 24.55 ? 42  PRO A O   1 
ATOM   338  C  CB  . PRO A 1 42  ? -23.463 -0.451  39.408  1.00 23.35 ? 42  PRO A CB  1 
ATOM   339  C  CG  . PRO A 1 42  ? -22.376 -0.097  40.356  1.00 22.61 ? 42  PRO A CG  1 
ATOM   340  C  CD  . PRO A 1 42  ? -21.178 -0.853  39.683  1.00 21.83 ? 42  PRO A CD  1 
ATOM   341  N  N   . SER A 1 43  ? -21.880 2.138   37.892  1.00 21.90 ? 43  SER A N   1 
ATOM   342  C  CA  . SER A 1 43  ? -21.879 3.530   37.380  1.00 22.02 ? 43  SER A CA  1 
ATOM   343  C  C   . SER A 1 43  ? -21.592 3.678   35.873  1.00 22.41 ? 43  SER A C   1 
ATOM   344  O  O   . SER A 1 43  ? -21.697 4.798   35.330  1.00 23.72 ? 43  SER A O   1 
ATOM   345  C  CB  . SER A 1 43  ? -20.901 4.418   38.142  1.00 22.41 ? 43  SER A CB  1 
ATOM   346  O  OG  . SER A 1 43  ? -19.588 4.076   37.815  1.00 25.22 ? 43  SER A OG  1 
ATOM   347  N  N   . LEU A 1 44  ? -21.196 2.594   35.177  1.00 22.15 ? 44  LEU A N   1 
ATOM   348  C  CA  . LEU A 1 44  ? -20.990 2.743   33.698  1.00 20.30 ? 44  LEU A CA  1 
ATOM   349  C  C   . LEU A 1 44  ? -22.344 2.939   33.025  1.00 22.19 ? 44  LEU A C   1 
ATOM   350  O  O   . LEU A 1 44  ? -23.298 2.254   33.381  1.00 21.01 ? 44  LEU A O   1 
ATOM   351  C  CB  . LEU A 1 44  ? -20.323 1.500   33.111  1.00 19.35 ? 44  LEU A CB  1 
ATOM   352  C  CG  . LEU A 1 44  ? -18.848 1.439   33.470  1.00 14.69 ? 44  LEU A CG  1 
ATOM   353  C  CD1 . LEU A 1 44  ? -18.352 -0.016  33.103  1.00 14.06 ? 44  LEU A CD1 1 
ATOM   354  C  CD2 . LEU A 1 44  ? -18.030 2.538   32.783  1.00 14.86 ? 44  LEU A CD2 1 
ATOM   355  N  N   . LYS A 1 45  ? -22.430 3.834   32.046  1.00 21.19 ? 45  LYS A N   1 
ATOM   356  C  CA  . LYS A 1 45  ? -23.730 3.968   31.302  1.00 21.34 ? 45  LYS A CA  1 
ATOM   357  C  C   . LYS A 1 45  ? -23.752 3.045   30.092  1.00 20.50 ? 45  LYS A C   1 
ATOM   358  O  O   . LYS A 1 45  ? -22.706 2.549   29.609  1.00 19.53 ? 45  LYS A O   1 
ATOM   359  C  CB  . LYS A 1 45  ? -23.945 5.353   30.778  1.00 21.76 ? 45  LYS A CB  1 
ATOM   360  C  CG  . LYS A 1 45  ? -23.494 6.436   31.744  1.00 24.36 ? 45  LYS A CG  1 
ATOM   361  C  CD  . LYS A 1 45  ? -23.586 7.826   31.209  1.00 29.61 ? 45  LYS A CD  1 
ATOM   362  C  CE  . LYS A 1 45  ? -23.919 8.768   32.351  0.00 39.86 ? 45  LYS A CE  1 
ATOM   363  N  NZ  . LYS A 1 45  ? -25.376 8.825   32.649  0.00 44.80 ? 45  LYS A NZ  1 
ATOM   364  N  N   . PRO A 1 46  ? -24.976 2.827   29.549  1.00 19.25 ? 46  PRO A N   1 
ATOM   365  C  CA  . PRO A 1 46  ? -25.085 2.129   28.274  1.00 18.08 ? 46  PRO A CA  1 
ATOM   366  C  C   . PRO A 1 46  ? -24.215 2.876   27.209  1.00 15.89 ? 46  PRO A C   1 
ATOM   367  O  O   . PRO A 1 46  ? -24.165 4.107   27.256  1.00 15.11 ? 46  PRO A O   1 
ATOM   368  C  CB  . PRO A 1 46  ? -26.581 2.232   27.939  1.00 17.19 ? 46  PRO A CB  1 
ATOM   369  C  CG  . PRO A 1 46  ? -27.264 2.365   29.264  1.00 19.24 ? 46  PRO A CG  1 
ATOM   370  C  CD  . PRO A 1 46  ? -26.293 3.115   30.148  1.00 19.14 ? 46  PRO A CD  1 
ATOM   371  N  N   . LEU A 1 47  ? -23.538 2.119   26.329  1.00 17.18 ? 47  LEU A N   1 
ATOM   372  C  CA  . LEU A 1 47  ? -22.827 2.731   25.219  1.00 14.31 ? 47  LEU A CA  1 
ATOM   373  C  C   . LEU A 1 47  ? -23.869 3.314   24.244  1.00 17.09 ? 47  LEU A C   1 
ATOM   374  O  O   . LEU A 1 47  ? -24.887 2.616   23.941  1.00 16.03 ? 47  LEU A O   1 
ATOM   375  C  CB  . LEU A 1 47  ? -22.013 1.693   24.462  1.00 17.26 ? 47  LEU A CB  1 
ATOM   376  C  CG  . LEU A 1 47  ? -20.894 2.146   23.608  1.00 19.71 ? 47  LEU A CG  1 
ATOM   377  C  CD1 . LEU A 1 47  ? -19.855 2.911   24.475  1.00 19.85 ? 47  LEU A CD1 1 
ATOM   378  C  CD2 . LEU A 1 47  ? -20.323 0.902   22.924  1.00 19.57 ? 47  LEU A CD2 1 
ATOM   379  N  N   . SER A 1 48  ? -23.587 4.508   23.746  1.00 13.34 ? 48  SER A N   1 
ATOM   380  C  CA  . SER A 1 48  ? -24.392 5.172   22.702  1.00 13.60 ? 48  SER A CA  1 
ATOM   381  C  C   . SER A 1 48  ? -23.681 5.239   21.365  1.00 13.94 ? 48  SER A C   1 
ATOM   382  O  O   . SER A 1 48  ? -22.688 5.968   21.183  1.00 13.30 ? 48  SER A O   1 
ATOM   383  C  CB  . SER A 1 48  ? -24.820 6.592   23.150  1.00 15.33 ? 48  SER A CB  1 
ATOM   384  O  OG  . SER A 1 48  ? -25.386 7.317   22.107  1.00 17.60 ? 48  SER A OG  1 
ATOM   385  N  N   . VAL A 1 49  ? -24.161 4.454   20.442  1.00 13.96 ? 49  VAL A N   1 
ATOM   386  C  CA  . VAL A 1 49  ? -23.561 4.400   19.137  1.00 15.03 ? 49  VAL A CA  1 
ATOM   387  C  C   . VAL A 1 49  ? -24.557 5.023   18.143  1.00 17.34 ? 49  VAL A C   1 
ATOM   388  O  O   . VAL A 1 49  ? -25.591 4.494   17.917  1.00 17.69 ? 49  VAL A O   1 
ATOM   389  C  CB  . VAL A 1 49  ? -23.275 2.918   18.679  1.00 17.34 ? 49  VAL A CB  1 
ATOM   390  C  CG1 . VAL A 1 49  ? -22.641 2.859   17.242  1.00 21.85 ? 49  VAL A CG1 1 
ATOM   391  C  CG2 . VAL A 1 49  ? -22.457 2.091   19.740  1.00 17.37 ? 49  VAL A CG2 1 
ATOM   392  N  N   . SER A 1 50  ? -24.259 6.178   17.649  1.00 15.24 ? 50  SER A N   1 
ATOM   393  C  CA  . SER A 1 50  ? -25.192 6.897   16.759  1.00 18.04 ? 50  SER A CA  1 
ATOM   394  C  C   . SER A 1 50  ? -24.609 6.915   15.350  1.00 17.86 ? 50  SER A C   1 
ATOM   395  O  O   . SER A 1 50  ? -23.923 7.876   14.967  1.00 17.87 ? 50  SER A O   1 
ATOM   396  C  CB  . SER A 1 50  ? -25.542 8.282   17.314  1.00 17.20 ? 50  SER A CB  1 
ATOM   397  O  OG  . SER A 1 50  ? -26.210 8.148   18.561  1.00 25.67 ? 50  SER A OG  1 
ATOM   398  N  N   . TYR A 1 51  ? -24.807 5.822   14.580  1.00 17.73 ? 51  TYR A N   1 
ATOM   399  C  CA  . TYR A 1 51  ? -24.253 5.708   13.207  1.00 15.32 ? 51  TYR A CA  1 
ATOM   400  C  C   . TYR A 1 51  ? -25.206 5.980   11.970  1.00 15.35 ? 51  TYR A C   1 
ATOM   401  O  O   . TYR A 1 51  ? -24.701 5.887   10.823  1.00 14.68 ? 51  TYR A O   1 
ATOM   402  C  CB  . TYR A 1 51  ? -23.498 4.381   12.952  1.00 16.26 ? 51  TYR A CB  1 
ATOM   403  C  CG  . TYR A 1 51  ? -22.242 4.126   13.753  1.00 14.35 ? 51  TYR A CG  1 
ATOM   404  C  CD1 . TYR A 1 51  ? -21.527 5.162   14.373  1.00 13.85 ? 51  TYR A CD1 1 
ATOM   405  C  CD2 . TYR A 1 51  ? -21.758 2.824   13.862  1.00 11.40 ? 51  TYR A CD2 1 
ATOM   406  C  CE1 . TYR A 1 51  ? -20.335 4.852   15.144  1.00 7.47  ? 51  TYR A CE1 1 
ATOM   407  C  CE2 . TYR A 1 51  ? -20.600 2.480   14.597  1.00 12.00 ? 51  TYR A CE2 1 
ATOM   408  C  CZ  . TYR A 1 51  ? -19.867 3.531   15.219  1.00 13.40 ? 51  TYR A CZ  1 
ATOM   409  O  OH  . TYR A 1 51  ? -18.726 3.220   15.920  1.00 11.39 ? 51  TYR A OH  1 
ATOM   410  N  N   . ASP A 1 52  ? -26.461 6.380   12.258  1.00 19.44 ? 52  ASP A N   1 
ATOM   411  C  CA  . ASP A 1 52  ? -27.511 6.691   11.193  1.00 20.47 ? 52  ASP A CA  1 
ATOM   412  C  C   . ASP A 1 52  ? -26.977 7.587   10.081  1.00 21.65 ? 52  ASP A C   1 
ATOM   413  O  O   . ASP A 1 52  ? -27.158 7.308   8.894   1.00 23.65 ? 52  ASP A O   1 
ATOM   414  C  CB  . ASP A 1 52  ? -28.848 7.270   11.777  1.00 21.39 ? 52  ASP A CB  1 
ATOM   415  C  CG  . ASP A 1 52  ? -28.619 8.212   12.956  1.00 27.20 ? 52  ASP A CG  1 
ATOM   416  O  OD1 . ASP A 1 52  ? -28.179 7.770   14.061  1.00 36.99 ? 52  ASP A OD1 1 
ATOM   417  O  OD2 . ASP A 1 52  ? -28.878 9.427   12.797  1.00 37.96 ? 52  ASP A OD2 1 
ATOM   418  N  N   . GLN A 1 53  ? -26.188 8.563   10.445  1.00 20.59 ? 53  GLN A N   1 
ATOM   419  C  CA  . GLN A 1 53  ? -25.730 9.511   9.438   1.00 22.10 ? 53  GLN A CA  1 
ATOM   420  C  C   . GLN A 1 53  ? -24.285 9.370   8.990   1.00 19.85 ? 53  GLN A C   1 
ATOM   421  O  O   . GLN A 1 53  ? -23.762 10.294  8.383   1.00 19.05 ? 53  GLN A O   1 
ATOM   422  C  CB  . GLN A 1 53  ? -25.958 10.915  9.988   1.00 23.51 ? 53  GLN A CB  1 
ATOM   423  C  CG  . GLN A 1 53  ? -27.457 11.194  10.270  1.00 30.48 ? 53  GLN A CG  1 
ATOM   424  C  CD  . GLN A 1 53  ? -28.345 10.855  9.052   1.00 33.47 ? 53  GLN A CD  1 
ATOM   425  O  OE1 . GLN A 1 53  ? -27.939 11.020  7.889   1.00 42.50 ? 53  GLN A OE1 1 
ATOM   426  N  NE2 . GLN A 1 53  ? -29.549 10.338  9.320   1.00 40.91 ? 53  GLN A NE2 1 
ATOM   427  N  N   . ALA A 1 54  ? -23.625 8.244   9.318   1.00 17.81 ? 54  ALA A N   1 
ATOM   428  C  CA  . ALA A 1 54  ? -22.287 7.968   8.860   1.00 15.36 ? 54  ALA A CA  1 
ATOM   429  C  C   . ALA A 1 54  ? -22.093 8.118   7.348   1.00 17.18 ? 54  ALA A C   1 
ATOM   430  O  O   . ALA A 1 54  ? -22.982 7.732   6.558   1.00 18.30 ? 54  ALA A O   1 
ATOM   431  C  CB  . ALA A 1 54  ? -21.840 6.516   9.338   1.00 16.20 ? 54  ALA A CB  1 
ATOM   432  N  N   . THR A 1 55  ? -21.020 8.808   6.942   1.00 14.38 ? 55  THR A N   1 
ATOM   433  C  CA  . THR A 1 55  ? -20.645 8.949   5.557   1.00 14.59 ? 55  THR A CA  1 
ATOM   434  C  C   . THR A 1 55  ? -19.320 8.353   5.293   1.00 14.29 ? 55  THR A C   1 
ATOM   435  O  O   . THR A 1 55  ? -18.280 8.970   5.571   1.00 12.75 ? 55  THR A O   1 
ATOM   436  C  CB  . THR A 1 55  ? -20.505 10.456  5.185   1.00 16.69 ? 55  THR A CB  1 
ATOM   437  O  OG1 . THR A 1 55  ? -21.719 11.082  5.489   1.00 23.32 ? 55  THR A OG1 1 
ATOM   438  C  CG2 . THR A 1 55  ? -20.193 10.561  3.699   1.00 19.55 ? 55  THR A CG2 1 
ATOM   439  N  N   . SER A 1 56  ? -19.312 7.120   4.788   1.00 13.43 ? 56  SER A N   1 
ATOM   440  C  CA  . SER A 1 56  ? -18.066 6.538   4.387   1.00 14.86 ? 56  SER A CA  1 
ATOM   441  C  C   . SER A 1 56  ? -17.543 7.217   3.094   1.00 16.31 ? 56  SER A C   1 
ATOM   442  O  O   . SER A 1 56  ? -18.329 7.710   2.236   1.00 19.16 ? 56  SER A O   1 
ATOM   443  C  CB  . SER A 1 56  ? -18.176 5.009   4.164   1.00 15.31 ? 56  SER A CB  1 
ATOM   444  O  OG  . SER A 1 56  ? -19.101 4.663   3.080   1.00 19.61 ? 56  SER A OG  1 
ATOM   445  N  N   . LEU A 1 57  ? -16.258 7.286   2.942   1.00 15.90 ? 57  LEU A N   1 
ATOM   446  C  CA  . LEU A 1 57  ? -15.676 7.894   1.748   1.00 16.68 ? 57  LEU A CA  1 
ATOM   447  C  C   . LEU A 1 57  ? -14.848 6.951   0.824   1.00 16.26 ? 57  LEU A C   1 
ATOM   448  O  O   . LEU A 1 57  ? -14.838 7.037   -0.430  1.00 16.82 ? 57  LEU A O   1 
ATOM   449  C  CB  . LEU A 1 57  ? -14.762 9.005   2.147   1.00 17.63 ? 57  LEU A CB  1 
ATOM   450  C  CG  . LEU A 1 57  ? -15.570 10.204  2.730   1.00 23.27 ? 57  LEU A CG  1 
ATOM   451  C  CD1 . LEU A 1 57  ? -14.496 11.255  3.065   1.00 23.45 ? 57  LEU A CD1 1 
ATOM   452  C  CD2 . LEU A 1 57  ? -16.788 10.769  1.832   1.00 24.79 ? 57  LEU A CD2 1 
ATOM   453  N  N   . ARG A 1 58  ? -13.990 6.194   1.460   1.00 14.48 ? 58  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 58  ? -12.931 5.533   0.736   1.00 13.18 ? 58  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 58  ? -12.440 4.359   1.559   1.00 14.33 ? 58  ARG A C   1 
ATOM   456  O  O   . ARG A 1 58  ? -12.529 4.375   2.804   1.00 12.68 ? 58  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 58  ? -11.760 6.510   0.624   1.00 14.71 ? 58  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 58  ? -10.847 6.178   -0.400  1.00 18.14 ? 58  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 58  ? -9.895  7.373   -0.511  1.00 24.54 ? 58  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 58  ? -9.053  7.313   0.677   1.00 19.01 ? 58  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 58  ? -7.735  7.368   0.641   1.00 20.12 ? 58  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 58  ? -7.161  7.541   -0.518  1.00 18.50 ? 58  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 58  ? -7.018  7.374   1.776   1.00 17.58 ? 58  ARG A NH2 1 
ATOM   464  N  N   . ILE A 1 59  ? -11.875 3.402   0.825   1.00 13.09 ? 59  ILE A N   1 
ATOM   465  C  CA  . ILE A 1 59  ? -11.195 2.275   1.489   1.00 13.82 ? 59  ILE A CA  1 
ATOM   466  C  C   . ILE A 1 59  ? -9.766  2.233   0.977   1.00 14.06 ? 59  ILE A C   1 
ATOM   467  O  O   . ILE A 1 59  ? -9.516  2.351   -0.225  1.00 14.06 ? 59  ILE A O   1 
ATOM   468  C  CB  . ILE A 1 59  ? -11.981 0.978   1.286   1.00 13.62 ? 59  ILE A CB  1 
ATOM   469  C  CG1 . ILE A 1 59  ? -11.390 -0.174  2.137   1.00 14.32 ? 59  ILE A CG1 1 
ATOM   470  C  CG2 . ILE A 1 59  ? -12.044 0.609   -0.205  1.00 13.54 ? 59  ILE A CG2 1 
ATOM   471  C  CD1 . ILE A 1 59  ? -12.288 -1.502  1.945   1.00 13.35 ? 59  ILE A CD1 1 
ATOM   472  N  N   . LEU A 1 60  ? -8.790  1.979   1.882   1.00 13.85 ? 60  LEU A N   1 
ATOM   473  C  CA  . LEU A 1 60  ? -7.415  2.125   1.674   1.00 13.07 ? 60  LEU A CA  1 
ATOM   474  C  C   . LEU A 1 60  ? -6.610  0.938   2.231   1.00 14.11 ? 60  LEU A C   1 
ATOM   475  O  O   . LEU A 1 60  ? -6.771  0.541   3.428   1.00 12.72 ? 60  LEU A O   1 
ATOM   476  C  CB  . LEU A 1 60  ? -6.942  3.412   2.445   1.00 14.82 ? 60  LEU A CB  1 
ATOM   477  C  CG  . LEU A 1 60  ? -5.424  3.585   2.325   1.00 13.88 ? 60  LEU A CG  1 
ATOM   478  C  CD1 . LEU A 1 60  ? -4.765  3.624   0.883   1.00 16.72 ? 60  LEU A CD1 1 
ATOM   479  C  CD2 . LEU A 1 60  ? -4.870  4.761   3.283   1.00 13.26 ? 60  LEU A CD2 1 
ATOM   480  N  N   . ASN A 1 61  ? -5.817  0.330   1.377   1.00 11.59 ? 61  ASN A N   1 
ATOM   481  C  CA  . ASN A 1 61  ? -4.828  -0.608  1.876   1.00 12.73 ? 61  ASN A CA  1 
ATOM   482  C  C   . ASN A 1 61  ? -3.558  0.208   2.251   1.00 14.66 ? 61  ASN A C   1 
ATOM   483  O  O   . ASN A 1 61  ? -2.891  0.763   1.370   1.00 14.07 ? 61  ASN A O   1 
ATOM   484  C  CB  . ASN A 1 61  ? -4.542  -1.718  0.849   1.00 13.72 ? 61  ASN A CB  1 
ATOM   485  C  CG  . ASN A 1 61  ? -3.385  -2.643  1.225   1.00 14.77 ? 61  ASN A CG  1 
ATOM   486  O  OD1 . ASN A 1 61  ? -2.468  -2.373  2.047   1.00 16.73 ? 61  ASN A OD1 1 
ATOM   487  N  ND2 . ASN A 1 61  ? -3.381  -3.835  0.552   1.00 15.74 ? 61  ASN A ND2 1 
ATOM   488  N  N   . ASN A 1 62  ? -3.254  0.309   3.549   1.00 13.93 ? 62  ASN A N   1 
ATOM   489  C  CA  . ASN A 1 62  ? -2.130  1.142   3.985   1.00 14.96 ? 62  ASN A CA  1 
ATOM   490  C  C   . ASN A 1 62  ? -0.845  0.288   4.211   1.00 15.77 ? 62  ASN A C   1 
ATOM   491  O  O   . ASN A 1 62  ? 0.210   0.743   4.828   1.00 19.09 ? 62  ASN A O   1 
ATOM   492  C  CB  . ASN A 1 62  ? -2.514  1.938   5.243   1.00 15.61 ? 62  ASN A CB  1 
ATOM   493  C  CG  . ASN A 1 62  ? -2.711  1.028   6.466   1.00 16.89 ? 62  ASN A CG  1 
ATOM   494  O  OD1 . ASN A 1 62  ? -2.479  -0.209  6.412   1.00 13.42 ? 62  ASN A OD1 1 
ATOM   495  N  ND2 . ASN A 1 62  ? -3.096  1.660   7.573   1.00 22.31 ? 62  ASN A ND2 1 
ATOM   496  N  N   . GLY A 1 63  ? -0.861  -0.968  3.728   1.00 13.56 ? 63  GLY A N   1 
ATOM   497  C  CA  . GLY A 1 63  ? 0.239   -1.804  3.920   1.00 13.31 ? 63  GLY A CA  1 
ATOM   498  C  C   . GLY A 1 63  ? 0.312   -2.597  5.242   1.00 13.88 ? 63  GLY A C   1 
ATOM   499  O  O   . GLY A 1 63  ? 1.181   -3.439  5.445   1.00 16.02 ? 63  GLY A O   1 
ATOM   500  N  N   . HIS A 1 64  ? -0.645  -2.336  6.133   1.00 13.26 ? 64  HIS A N   1 
ATOM   501  C  CA  . HIS A 1 64  ? -0.681  -3.001  7.506   1.00 15.44 ? 64  HIS A CA  1 
ATOM   502  C  C   . HIS A 1 64  ? -2.066  -3.607  7.720   1.00 16.05 ? 64  HIS A C   1 
ATOM   503  O  O   . HIS A 1 64  ? -2.217  -4.706  8.345   1.00 16.17 ? 64  HIS A O   1 
ATOM   504  C  CB  . HIS A 1 64  ? -0.439  -2.011  8.624   1.00 15.51 ? 64  HIS A CB  1 
ATOM   505  C  CG  . HIS A 1 64  ? 0.848   -1.278  8.493   1.00 22.51 ? 64  HIS A CG  1 
ATOM   506  N  ND1 . HIS A 1 64  ? 2.069   -1.904  8.645   1.00 22.19 ? 64  HIS A ND1 1 
ATOM   507  C  CD2 . HIS A 1 64  ? 1.111   0.026   8.264   1.00 19.35 ? 64  HIS A CD2 1 
ATOM   508  C  CE1 . HIS A 1 64  ? 3.040   -1.019  8.524   1.00 22.58 ? 64  HIS A CE1 1 
ATOM   509  N  NE2 . HIS A 1 64  ? 2.489   0.159   8.273   1.00 20.65 ? 64  HIS A NE2 1 
ATOM   510  N  N   . ALA A 1 65  ? -3.064  -2.952  7.158   1.00 13.68 ? 65  ALA A N   1 
ATOM   511  C  CA  . ALA A 1 65  ? -4.469  -3.405  7.203   1.00 12.40 ? 65  ALA A CA  1 
ATOM   512  C  C   . ALA A 1 65  ? -5.221  -2.661  6.056   1.00 12.70 ? 65  ALA A C   1 
ATOM   513  O  O   . ALA A 1 65  ? -4.574  -1.994  5.193   1.00 13.27 ? 65  ALA A O   1 
ATOM   514  C  CB  . ALA A 1 65  ? -5.089  -3.121  8.578   1.00 11.73 ? 65  ALA A CB  1 
ATOM   515  N  N   . PHE A 1 66  ? -6.541  -2.715  6.046   1.00 9.04  ? 66  PHE A N   1 
ATOM   516  C  CA  . PHE A 1 66  ? -7.330  -1.766  5.221   1.00 9.73  ? 66  PHE A CA  1 
ATOM   517  C  C   . PHE A 1 66  ? -8.214  -0.892  6.129   1.00 10.99 ? 66  PHE A C   1 
ATOM   518  O  O   . PHE A 1 66  ? -8.823  -1.361  7.129   1.00 9.34  ? 66  PHE A O   1 
ATOM   519  C  CB  . PHE A 1 66  ? -8.139  -2.454  4.144   1.00 10.95 ? 66  PHE A CB  1 
ATOM   520  C  CG  . PHE A 1 66  ? -9.161  -3.422  4.709   1.00 10.01 ? 66  PHE A CG  1 
ATOM   521  C  CD1 . PHE A 1 66  ? -10.470 -2.972  5.068   1.00 11.22 ? 66  PHE A CD1 1 
ATOM   522  C  CD2 . PHE A 1 66  ? -8.865  -4.781  4.775   1.00 9.81  ? 66  PHE A CD2 1 
ATOM   523  C  CE1 . PHE A 1 66  ? -11.482 -3.784  5.556   1.00 12.65 ? 66  PHE A CE1 1 
ATOM   524  C  CE2 . PHE A 1 66  ? -9.882  -5.643  5.373   1.00 9.01  ? 66  PHE A CE2 1 
ATOM   525  C  CZ  . PHE A 1 66  ? -11.164 -5.190  5.729   1.00 12.03 ? 66  PHE A CZ  1 
ATOM   526  N  N   . ASN A 1 67  ? -8.311  0.415   5.795   1.00 10.03 ? 67  ASN A N   1 
ATOM   527  C  CA  . ASN A 1 67  ? -9.154  1.324   6.559   1.00 11.60 ? 67  ASN A CA  1 
ATOM   528  C  C   . ASN A 1 67  ? -10.353 1.714   5.740   1.00 12.37 ? 67  ASN A C   1 
ATOM   529  O  O   . ASN A 1 67  ? -10.155 2.171   4.626   1.00 13.97 ? 67  ASN A O   1 
ATOM   530  C  CB  . ASN A 1 67  ? -8.429  2.633   6.921   1.00 11.99 ? 67  ASN A CB  1 
ATOM   531  C  CG  . ASN A 1 67  ? -7.241  2.406   7.807   1.00 15.84 ? 67  ASN A CG  1 
ATOM   532  O  OD1 . ASN A 1 67  ? -7.056  1.340   8.412   1.00 13.26 ? 67  ASN A OD1 1 
ATOM   533  N  ND2 . ASN A 1 67  ? -6.405  3.444   7.900   1.00 18.60 ? 67  ASN A ND2 1 
ATOM   534  N  N   . VAL A 1 68  ? -11.524 1.597   6.298   1.00 11.18 ? 68  VAL A N   1 
ATOM   535  C  CA  . VAL A 1 68  ? -12.697 2.263   5.712   1.00 11.43 ? 68  VAL A CA  1 
ATOM   536  C  C   . VAL A 1 68  ? -12.803 3.661   6.374   1.00 14.74 ? 68  VAL A C   1 
ATOM   537  O  O   . VAL A 1 68  ? -12.960 3.736   7.598   1.00 11.93 ? 68  VAL A O   1 
ATOM   538  C  CB  . VAL A 1 68  ? -13.990 1.466   5.890   1.00 12.85 ? 68  VAL A CB  1 
ATOM   539  C  CG1 . VAL A 1 68  ? -15.170 2.311   5.320   1.00 13.91 ? 68  VAL A CG1 1 
ATOM   540  C  CG2 . VAL A 1 68  ? -13.885 0.121   5.141   1.00 14.88 ? 68  VAL A CG2 1 
ATOM   541  N  N   . GLU A 1 69  ? -12.757 4.748   5.570   1.00 14.47 ? 69  GLU A N   1 
ATOM   542  C  CA  . GLU A 1 69  ? -12.627 6.100   6.098   1.00 14.93 ? 69  GLU A CA  1 
ATOM   543  C  C   . GLU A 1 69  ? -13.958 6.818   6.009   1.00 16.30 ? 69  GLU A C   1 
ATOM   544  O  O   . GLU A 1 69  ? -14.795 6.554   5.083   1.00 15.99 ? 69  GLU A O   1 
ATOM   545  C  CB  . GLU A 1 69  ? -11.677 6.855   5.226   1.00 17.29 ? 69  GLU A CB  1 
ATOM   546  C  CG  . GLU A 1 69  ? -10.251 6.345   5.324   1.00 17.36 ? 69  GLU A CG  1 
ATOM   547  C  CD  . GLU A 1 69  ? -9.503  6.735   4.102   1.00 19.14 ? 69  GLU A CD  1 
ATOM   548  O  OE1 . GLU A 1 69  ? -10.127 7.443   3.205   1.00 19.01 ? 69  GLU A OE1 1 
ATOM   549  O  OE2 . GLU A 1 69  ? -8.300  6.390   4.012   1.00 17.81 ? 69  GLU A OE2 1 
ATOM   550  N  N   . PHE A 1 70  ? -14.129 7.733   6.952   1.00 12.61 ? 70  PHE A N   1 
ATOM   551  C  CA  . PHE A 1 70  ? -15.404 8.408   7.026   1.00 12.15 ? 70  PHE A CA  1 
ATOM   552  C  C   . PHE A 1 70  ? -15.163 9.882   6.956   1.00 13.12 ? 70  PHE A C   1 
ATOM   553  O  O   . PHE A 1 70  ? -14.132 10.353  7.340   1.00 12.42 ? 70  PHE A O   1 
ATOM   554  C  CB  . PHE A 1 70  ? -16.145 8.062   8.304   1.00 11.65 ? 70  PHE A CB  1 
ATOM   555  C  CG  . PHE A 1 70  ? -16.730 6.657   8.280   1.00 9.97  ? 70  PHE A CG  1 
ATOM   556  C  CD1 . PHE A 1 70  ? -15.908 5.523   8.454   1.00 13.73 ? 70  PHE A CD1 1 
ATOM   557  C  CD2 . PHE A 1 70  ? -18.088 6.468   7.950   1.00 12.75 ? 70  PHE A CD2 1 
ATOM   558  C  CE1 . PHE A 1 70  ? -16.446 4.191   8.405   1.00 12.10 ? 70  PHE A CE1 1 
ATOM   559  C  CE2 . PHE A 1 70  ? -18.626 5.166   7.852   1.00 9.67  ? 70  PHE A CE2 1 
ATOM   560  C  CZ  . PHE A 1 70  ? -17.765 4.025   8.056   1.00 13.70 ? 70  PHE A CZ  1 
ATOM   561  N  N   A ASP A 1 71  ? -16.203 10.576  6.510   0.50 13.65 ? 71  ASP A N   1 
ATOM   562  N  N   B ASP A 1 71  ? -16.106 10.617  6.396   0.50 13.37 ? 71  ASP A N   1 
ATOM   563  C  CA  A ASP A 1 71  ? -16.219 12.011  6.693   0.50 14.24 ? 71  ASP A CA  1 
ATOM   564  C  CA  B ASP A 1 71  ? -16.006 12.077  6.510   0.50 13.53 ? 71  ASP A CA  1 
ATOM   565  C  C   A ASP A 1 71  ? -16.460 12.353  8.150   0.50 14.25 ? 71  ASP A C   1 
ATOM   566  C  C   B ASP A 1 71  ? -16.448 12.526  7.939   0.50 13.90 ? 71  ASP A C   1 
ATOM   567  O  O   A ASP A 1 71  ? -17.504 12.059  8.719   0.50 15.84 ? 71  ASP A O   1 
ATOM   568  O  O   B ASP A 1 71  ? -17.632 12.440  8.265   0.50 14.89 ? 71  ASP A O   1 
ATOM   569  C  CB  A ASP A 1 71  ? -17.335 12.602  5.903   0.50 13.53 ? 71  ASP A CB  1 
ATOM   570  C  CB  B ASP A 1 71  ? -16.893 12.646  5.423   0.50 13.30 ? 71  ASP A CB  1 
ATOM   571  C  CG  A ASP A 1 71  ? -17.325 14.101  5.957   0.50 14.95 ? 71  ASP A CG  1 
ATOM   572  C  CG  B ASP A 1 71  ? -16.996 14.148  5.461   0.50 14.75 ? 71  ASP A CG  1 
ATOM   573  O  OD1 A ASP A 1 71  ? -16.263 14.745  6.279   0.50 15.39 ? 71  ASP A OD1 1 
ATOM   574  O  OD1 B ASP A 1 71  ? -17.215 14.680  4.321   0.50 17.21 ? 71  ASP A OD1 1 
ATOM   575  O  OD2 A ASP A 1 71  ? -18.385 14.628  5.631   0.50 15.88 ? 71  ASP A OD2 1 
ATOM   576  O  OD2 B ASP A 1 71  ? -16.916 14.751  6.605   0.50 15.54 ? 71  ASP A OD2 1 
ATOM   577  N  N   . ASP A 1 72  ? -15.493 12.999  8.753   1.00 13.39 ? 72  ASP A N   1 
ATOM   578  C  CA  . ASP A 1 72  ? -15.652 13.370  10.160  1.00 13.56 ? 72  ASP A CA  1 
ATOM   579  C  C   . ASP A 1 72  ? -15.614 14.908  10.293  1.00 16.65 ? 72  ASP A C   1 
ATOM   580  O  O   . ASP A 1 72  ? -15.273 15.383  11.343  1.00 15.64 ? 72  ASP A O   1 
ATOM   581  C  CB  . ASP A 1 72  ? -14.536 12.754  10.999  1.00 15.05 ? 72  ASP A CB  1 
ATOM   582  C  CG  . ASP A 1 72  ? -13.158 13.233  10.581  1.00 14.13 ? 72  ASP A CG  1 
ATOM   583  O  OD1 . ASP A 1 72  ? -13.050 13.906  9.533   1.00 15.37 ? 72  ASP A OD1 1 
ATOM   584  O  OD2 . ASP A 1 72  ? -12.181 12.937  11.298  1.00 15.04 ? 72  ASP A OD2 1 
ATOM   585  N  N   . SER A 1 73  ? -15.969 15.606  9.220   1.00 16.96 ? 73  SER A N   1 
ATOM   586  C  CA  . SER A 1 73  ? -15.981 17.140  9.256   1.00 19.03 ? 73  SER A CA  1 
ATOM   587  C  C   . SER A 1 73  ? -17.303 17.655  9.838   1.00 20.06 ? 73  SER A C   1 
ATOM   588  O  O   . SER A 1 73  ? -17.528 18.889  9.982   1.00 18.80 ? 73  SER A O   1 
ATOM   589  C  CB  . SER A 1 73  ? -15.717 17.732  7.872   1.00 18.80 ? 73  SER A CB  1 
ATOM   590  O  OG  . SER A 1 73  ? -16.783 17.373  7.014   1.00 17.62 ? 73  SER A OG  1 
ATOM   591  N  N   . GLN A 1 74  ? -18.185 16.746  10.215  1.00 20.47 ? 74  GLN A N   1 
ATOM   592  C  CA  . GLN A 1 74  ? -19.451 17.173  10.825  1.00 23.23 ? 74  GLN A CA  1 
ATOM   593  C  C   . GLN A 1 74  ? -19.810 16.142  11.864  1.00 22.83 ? 74  GLN A C   1 
ATOM   594  O  O   . GLN A 1 74  ? -19.291 15.048  11.848  1.00 20.20 ? 74  GLN A O   1 
ATOM   595  C  CB  . GLN A 1 74  ? -20.619 17.209  9.791   1.00 24.09 ? 74  GLN A CB  1 
ATOM   596  C  CG  . GLN A 1 74  ? -20.766 18.454  8.946   1.00 28.81 ? 74  GLN A CG  1 
ATOM   597  C  CD  . GLN A 1 74  ? -22.024 18.344  8.083   1.00 27.16 ? 74  GLN A CD  1 
ATOM   598  O  OE1 . GLN A 1 74  ? -23.128 18.686  8.528   1.00 39.39 ? 74  GLN A OE1 1 
ATOM   599  N  NE2 . GLN A 1 74  ? -21.888 17.827  6.898   1.00 29.07 ? 74  GLN A NE2 1 
ATOM   600  N  N   A ASP A 1 75  ? -20.686 16.475  12.827  0.50 23.48 ? 75  ASP A N   1 
ATOM   601  N  N   B ASP A 1 75  ? -20.779 16.559  12.664  0.50 23.20 ? 75  ASP A N   1 
ATOM   602  C  CA  A ASP A 1 75  ? -20.982 15.548  13.933  0.50 23.20 ? 75  ASP A CA  1 
ATOM   603  C  CA  B ASP A 1 75  ? -21.343 15.830  13.730  0.50 23.23 ? 75  ASP A CA  1 
ATOM   604  C  C   A ASP A 1 75  ? -22.100 14.619  13.454  0.50 24.32 ? 75  ASP A C   1 
ATOM   605  C  C   B ASP A 1 75  ? -22.229 14.712  13.154  0.50 24.05 ? 75  ASP A C   1 
ATOM   606  O  O   A ASP A 1 75  ? -23.294 14.910  13.635  0.50 22.91 ? 75  ASP A O   1 
ATOM   607  O  O   B ASP A 1 75  ? -23.437 14.942  13.021  0.50 23.45 ? 75  ASP A O   1 
ATOM   608  C  CB  A ASP A 1 75  ? -21.415 16.298  15.211  0.50 24.39 ? 75  ASP A CB  1 
ATOM   609  C  CB  B ASP A 1 75  ? -22.211 16.860  14.487  0.50 22.52 ? 75  ASP A CB  1 
ATOM   610  C  CG  A ASP A 1 75  ? -20.577 15.935  16.466  0.50 20.89 ? 75  ASP A CG  1 
ATOM   611  C  CG  B ASP A 1 75  ? -22.788 16.319  15.743  0.50 22.57 ? 75  ASP A CG  1 
ATOM   612  O  OD1 A ASP A 1 75  ? -19.761 14.978  16.468  0.50 18.18 ? 75  ASP A OD1 1 
ATOM   613  O  OD1 B ASP A 1 75  ? -22.326 15.236  16.167  0.50 18.11 ? 75  ASP A OD1 1 
ATOM   614  O  OD2 A ASP A 1 75  ? -20.777 16.633  17.493  0.50 28.72 ? 75  ASP A OD2 1 
ATOM   615  O  OD2 B ASP A 1 75  ? -23.697 16.993  16.294  0.50 21.20 ? 75  ASP A OD2 1 
ATOM   616  N  N   . LYS A 1 76  ? -21.675 13.533  12.822  1.00 23.80 ? 76  LYS A N   1 
ATOM   617  C  CA  . LYS A 1 76  ? -22.558 12.491  12.108  1.00 24.59 ? 76  LYS A CA  1 
ATOM   618  C  C   . LYS A 1 76  ? -22.657 11.014  12.582  1.00 25.24 ? 76  LYS A C   1 
ATOM   619  O  O   . LYS A 1 76  ? -23.730 10.315  12.449  1.00 30.03 ? 76  LYS A O   1 
ATOM   620  C  CB  . LYS A 1 76  ? -22.136 12.401  10.635  1.00 24.51 ? 76  LYS A CB  1 
ATOM   621  C  CG  . LYS A 1 76  ? -22.823 13.390  9.614   1.00 27.94 ? 76  LYS A CG  1 
ATOM   622  C  CD  . LYS A 1 76  ? -21.853 13.465  8.450   1.00 27.44 ? 76  LYS A CD  1 
ATOM   623  C  CE  . LYS A 1 76  ? -22.356 14.098  7.109   1.00 31.35 ? 76  LYS A CE  1 
ATOM   624  N  NZ  . LYS A 1 76  ? -21.149 14.441  6.289   1.00 28.73 ? 76  LYS A NZ  1 
ATOM   625  N  N   . ALA A 1 77  ? -21.521 10.483  12.933  1.00 20.58 ? 77  ALA A N   1 
ATOM   626  C  CA  . ALA A 1 77  ? -21.350 9.060   13.367  1.00 16.93 ? 77  ALA A CA  1 
ATOM   627  C  C   . ALA A 1 77  ? -20.580 9.237   14.700  1.00 16.60 ? 77  ALA A C   1 
ATOM   628  O  O   . ALA A 1 77  ? -19.392 9.452   14.649  1.00 18.94 ? 77  ALA A O   1 
ATOM   629  C  CB  . ALA A 1 77  ? -20.472 8.325   12.354  1.00 15.75 ? 77  ALA A CB  1 
ATOM   630  N  N   . VAL A 1 78  ? -21.275 9.211   15.806  1.00 15.06 ? 78  VAL A N   1 
ATOM   631  C  CA  . VAL A 1 78  ? -20.675 9.497   17.102  1.00 14.90 ? 78  VAL A CA  1 
ATOM   632  C  C   . VAL A 1 78  ? -20.875 8.405   18.144  1.00 15.13 ? 78  VAL A C   1 
ATOM   633  O  O   . VAL A 1 78  ? -21.960 7.713   18.218  1.00 13.90 ? 78  VAL A O   1 
ATOM   634  C  CB  . VAL A 1 78  ? -21.199 10.819  17.698  1.00 17.79 ? 78  VAL A CB  1 
ATOM   635  C  CG1 . VAL A 1 78  ? -20.793 11.995  16.828  1.00 19.52 ? 78  VAL A CG1 1 
ATOM   636  C  CG2 . VAL A 1 78  ? -22.707 10.763  17.873  1.00 18.11 ? 78  VAL A CG2 1 
ATOM   637  N  N   . LEU A 1 79  ? -19.825 8.240   18.972  1.00 11.95 ? 79  LEU A N   1 
ATOM   638  C  CA  . LEU A 1 79  ? -19.859 7.337   20.072  1.00 13.64 ? 79  LEU A CA  1 
ATOM   639  C  C   . LEU A 1 79  ? -19.830 8.224   21.304  1.00 14.22 ? 79  LEU A C   1 
ATOM   640  O  O   . LEU A 1 79  ? -19.043 9.207   21.393  1.00 12.80 ? 79  LEU A O   1 
ATOM   641  C  CB  . LEU A 1 79  ? -18.615 6.418   19.967  1.00 13.05 ? 79  LEU A CB  1 
ATOM   642  C  CG  . LEU A 1 79  ? -18.533 5.430   21.081  1.00 13.44 ? 79  LEU A CG  1 
ATOM   643  C  CD1 . LEU A 1 79  ? -19.539 4.322   20.933  1.00 15.23 ? 79  LEU A CD1 1 
ATOM   644  C  CD2 . LEU A 1 79  ? -17.153 4.754   21.067  1.00 10.66 ? 79  LEU A CD2 1 
ATOM   645  N  N   . LYS A 1 80  ? -20.712 7.906   22.247  1.00 13.69 ? 80  LYS A N   1 
ATOM   646  C  CA  . LYS A 1 80  ? -20.724 8.571   23.563  1.00 13.98 ? 80  LYS A CA  1 
ATOM   647  C  C   . LYS A 1 80  ? -21.325 7.679   24.640  1.00 15.02 ? 80  LYS A C   1 
ATOM   648  O  O   . LYS A 1 80  ? -21.668 6.498   24.328  1.00 11.57 ? 80  LYS A O   1 
ATOM   649  C  CB  . LYS A 1 80  ? -21.409 9.945   23.479  1.00 16.28 ? 80  LYS A CB  1 
ATOM   650  C  CG  . LYS A 1 80  ? -22.840 9.859   23.156  1.00 19.81 ? 80  LYS A CG  1 
ATOM   651  C  CD  . LYS A 1 80  ? -23.390 11.301  22.934  1.00 21.25 ? 80  LYS A CD  1 
ATOM   652  C  CE  . LYS A 1 80  ? -24.933 11.312  22.813  1.00 32.33 ? 80  LYS A CE  1 
ATOM   653  N  NZ  . LYS A 1 80  ? -25.614 10.634  23.979  1.00 36.91 ? 80  LYS A NZ  1 
ATOM   654  N  N   . GLY A 1 81  ? -21.471 8.208   25.866  1.00 14.80 ? 81  GLY A N   1 
ATOM   655  C  CA  . GLY A 1 81  ? -21.978 7.426   26.990  1.00 14.02 ? 81  GLY A CA  1 
ATOM   656  C  C   . GLY A 1 81  ? -20.986 6.325   27.258  1.00 15.42 ? 81  GLY A C   1 
ATOM   657  O  O   . GLY A 1 81  ? -19.797 6.558   27.008  1.00 14.05 ? 81  GLY A O   1 
ATOM   658  N  N   . GLY A 1 82  ? -21.434 5.145   27.705  1.00 16.18 ? 82  GLY A N   1 
ATOM   659  C  CA  . GLY A 1 82  ? -20.483 4.158   28.190  1.00 16.38 ? 82  GLY A CA  1 
ATOM   660  C  C   . GLY A 1 82  ? -19.573 4.719   29.293  1.00 15.46 ? 82  GLY A C   1 
ATOM   661  O  O   . GLY A 1 82  ? -20.029 5.460   30.225  1.00 16.16 ? 82  GLY A O   1 
ATOM   662  N  N   . PRO A 1 83  ? -18.210 4.503   29.162  1.00 13.14 ? 83  PRO A N   1 
ATOM   663  C  CA  . PRO A 1 83  ? -17.292 5.111   30.102  1.00 12.18 ? 83  PRO A CA  1 
ATOM   664  C  C   . PRO A 1 83  ? -16.892 6.541   29.717  1.00 13.37 ? 83  PRO A C   1 
ATOM   665  O  O   . PRO A 1 83  ? -16.137 7.210   30.458  1.00 16.40 ? 83  PRO A O   1 
ATOM   666  C  CB  . PRO A 1 83  ? -16.040 4.227   29.940  1.00 15.87 ? 83  PRO A CB  1 
ATOM   667  C  CG  . PRO A 1 83  ? -16.066 3.898   28.438  1.00 13.01 ? 83  PRO A CG  1 
ATOM   668  C  CD  . PRO A 1 83  ? -17.485 3.714   28.106  1.00 10.71 ? 83  PRO A CD  1 
ATOM   669  N  N   . LEU A 1 84  ? -17.429 7.046   28.623  1.00 12.31 ? 84  LEU A N   1 
ATOM   670  C  CA  . LEU A 1 84  ? -16.876 8.314   28.029  1.00 13.23 ? 84  LEU A CA  1 
ATOM   671  C  C   . LEU A 1 84  ? -17.553 9.544   28.563  1.00 16.51 ? 84  LEU A C   1 
ATOM   672  O  O   . LEU A 1 84  ? -18.761 9.525   28.846  1.00 16.18 ? 84  LEU A O   1 
ATOM   673  C  CB  . LEU A 1 84  ? -17.083 8.319   26.541  1.00 12.00 ? 84  LEU A CB  1 
ATOM   674  C  CG  . LEU A 1 84  ? -16.515 7.074   25.839  1.00 11.85 ? 84  LEU A CG  1 
ATOM   675  C  CD1 . LEU A 1 84  ? -17.006 7.014   24.349  1.00 11.41 ? 84  LEU A CD1 1 
ATOM   676  C  CD2 . LEU A 1 84  ? -14.895 6.970   26.065  1.00 11.94 ? 84  LEU A CD2 1 
ATOM   677  N  N   A ASP A 1 85  ? -16.744 10.607  28.574  0.50 16.90 ? 85  ASP A N   1 
ATOM   678  N  N   B ASP A 1 85  ? -16.790 10.615  28.676  0.50 17.30 ? 85  ASP A N   1 
ATOM   679  C  CA  A ASP A 1 85  ? -17.185 11.971  28.817  0.50 19.25 ? 85  ASP A CA  1 
ATOM   680  C  CA  B ASP A 1 85  ? -17.427 11.898  28.880  0.50 19.49 ? 85  ASP A CA  1 
ATOM   681  C  C   A ASP A 1 85  ? -17.232 12.644  27.447  0.50 19.50 ? 85  ASP A C   1 
ATOM   682  C  C   B ASP A 1 85  ? -17.288 12.610  27.532  0.50 19.76 ? 85  ASP A C   1 
ATOM   683  O  O   A ASP A 1 85  ? -16.271 12.590  26.646  0.50 20.66 ? 85  ASP A O   1 
ATOM   684  O  O   B ASP A 1 85  ? -16.267 12.515  26.832  0.50 21.90 ? 85  ASP A O   1 
ATOM   685  C  CB  A ASP A 1 85  ? -16.212 12.678  29.802  0.50 19.29 ? 85  ASP A CB  1 
ATOM   686  C  CB  B ASP A 1 85  ? -16.833 12.643  30.091  0.50 20.06 ? 85  ASP A CB  1 
ATOM   687  C  CG  A ASP A 1 85  ? -16.371 12.185  31.242  0.50 21.38 ? 85  ASP A CG  1 
ATOM   688  C  CG  B ASP A 1 85  ? -15.330 12.704  30.058  0.50 20.85 ? 85  ASP A CG  1 
ATOM   689  O  OD1 A ASP A 1 85  ? -17.502 11.758  31.563  0.50 21.44 ? 85  ASP A OD1 1 
ATOM   690  O  OD1 B ASP A 1 85  ? -14.766 12.530  28.963  0.50 20.80 ? 85  ASP A OD1 1 
ATOM   691  O  OD2 A ASP A 1 85  ? -15.387 12.223  32.056  0.50 23.64 ? 85  ASP A OD2 1 
ATOM   692  O  OD2 B ASP A 1 85  ? -14.680 12.934  31.113  0.50 23.26 ? 85  ASP A OD2 1 
ATOM   693  N  N   . GLY A 1 86  ? -18.325 13.322  27.135  1.00 21.82 ? 86  GLY A N   1 
ATOM   694  C  CA  . GLY A 1 86  ? -18.312 13.991  25.882  1.00 19.22 ? 86  GLY A CA  1 
ATOM   695  C  C   . GLY A 1 86  ? -18.517 13.057  24.659  1.00 19.37 ? 86  GLY A C   1 
ATOM   696  O  O   . GLY A 1 86  ? -19.071 11.941  24.763  1.00 20.91 ? 86  GLY A O   1 
ATOM   697  N  N   A THR A 1 87  ? -18.058 13.521  23.508  0.50 16.49 ? 87  THR A N   1 
ATOM   698  N  N   B THR A 1 87  ? -18.088 13.520  23.511  0.50 16.35 ? 87  THR A N   1 
ATOM   699  C  CA  A THR A 1 87  ? -18.490 12.974  22.230  0.50 14.62 ? 87  THR A CA  1 
ATOM   700  C  CA  B THR A 1 87  ? -18.509 12.891  22.290  0.50 14.20 ? 87  THR A CA  1 
ATOM   701  C  C   A THR A 1 87  ? -17.368 12.687  21.273  0.50 13.75 ? 87  THR A C   1 
ATOM   702  C  C   B THR A 1 87  ? -17.323 12.621  21.426  0.50 14.03 ? 87  THR A C   1 
ATOM   703  O  O   A THR A 1 87  ? -16.533 13.543  20.993  0.50 10.87 ? 87  THR A O   1 
ATOM   704  O  O   B THR A 1 87  ? -16.379 13.419  21.389  0.50 11.73 ? 87  THR A O   1 
ATOM   705  C  CB  A THR A 1 87  ? -19.457 13.945  21.519  0.50 16.08 ? 87  THR A CB  1 
ATOM   706  C  CB  B THR A 1 87  ? -19.536 13.774  21.542  0.50 15.62 ? 87  THR A CB  1 
ATOM   707  O  OG1 A THR A 1 87  ? -20.549 14.234  22.412  0.50 15.94 ? 87  THR A OG1 1 
ATOM   708  O  OG1 B THR A 1 87  ? -19.041 15.117  21.441  0.50 13.40 ? 87  THR A OG1 1 
ATOM   709  C  CG2 A THR A 1 87  ? -19.971 13.338  20.182  0.50 16.18 ? 87  THR A CG2 1 
ATOM   710  C  CG2 B THR A 1 87  ? -20.876 13.798  22.331  0.50 14.36 ? 87  THR A CG2 1 
ATOM   711  N  N   . TYR A 1 88  ? -17.356 11.456  20.782  1.00 11.51 ? 88  TYR A N   1 
ATOM   712  C  CA  . TYR A 1 88  ? -16.251 11.021  19.933  1.00 11.41 ? 88  TYR A CA  1 
ATOM   713  C  C   . TYR A 1 88  ? -16.732 10.718  18.530  1.00 10.72 ? 88  TYR A C   1 
ATOM   714  O  O   . TYR A 1 88  ? -17.708 9.966   18.356  1.00 14.33 ? 88  TYR A O   1 
ATOM   715  C  CB  . TYR A 1 88  ? -15.620 9.752   20.476  1.00 8.08  ? 88  TYR A CB  1 
ATOM   716  C  CG  . TYR A 1 88  ? -14.880 9.949   21.846  1.00 9.23  ? 88  TYR A CG  1 
ATOM   717  C  CD1 . TYR A 1 88  ? -15.574 10.327  23.042  1.00 6.51  ? 88  TYR A CD1 1 
ATOM   718  C  CD2 . TYR A 1 88  ? -13.437 9.804   21.885  1.00 10.13 ? 88  TYR A CD2 1 
ATOM   719  C  CE1 . TYR A 1 88  ? -14.854 10.498  24.261  1.00 10.22 ? 88  TYR A CE1 1 
ATOM   720  C  CE2 . TYR A 1 88  ? -12.726 10.005  23.088  1.00 9.54  ? 88  TYR A CE2 1 
ATOM   721  C  CZ  . TYR A 1 88  ? -13.430 10.297  24.259  1.00 10.03 ? 88  TYR A CZ  1 
ATOM   722  O  OH  . TYR A 1 88  ? -12.785 10.400  25.406  1.00 9.52  ? 88  TYR A OH  1 
ATOM   723  N  N   . ARG A 1 89  ? -16.018 11.249  17.550  1.00 9.55  ? 89  ARG A N   1 
ATOM   724  C  CA  . ARG A 1 89  ? -16.491 11.155  16.168  1.00 10.02 ? 89  ARG A CA  1 
ATOM   725  C  C   . ARG A 1 89  ? -15.787 9.992   15.428  1.00 7.48  ? 89  ARG A C   1 
ATOM   726  O  O   . ARG A 1 89  ? -14.560 9.896   15.468  1.00 8.37  ? 89  ARG A O   1 
ATOM   727  C  CB  . ARG A 1 89  ? -16.231 12.469  15.449  1.00 15.05 ? 89  ARG A CB  1 
ATOM   728  C  CG  . ARG A 1 89  ? -17.069 12.654  14.347  1.00 17.52 ? 89  ARG A CG  1 
ATOM   729  C  CD  . ARG A 1 89  ? -16.944 14.062  13.793  1.00 18.86 ? 89  ARG A CD  1 
ATOM   730  N  NE  . ARG A 1 89  ? -17.595 15.078  14.602  1.00 20.62 ? 89  ARG A NE  1 
ATOM   731  C  CZ  . ARG A 1 89  ? -17.483 16.392  14.390  1.00 20.03 ? 89  ARG A CZ  1 
ATOM   732  N  NH1 . ARG A 1 89  ? -16.751 16.863  13.404  1.00 17.91 ? 89  ARG A NH1 1 
ATOM   733  N  NH2 . ARG A 1 89  ? -18.100 17.256  15.183  1.00 17.76 ? 89  ARG A NH2 1 
ATOM   734  N  N   . LEU A 1 90  ? -16.550 9.142   14.711  1.00 8.34  ? 90  LEU A N   1 
ATOM   735  C  CA  . LEU A 1 90  ? -15.946 8.047   13.928  1.00 7.44  ? 90  LEU A CA  1 
ATOM   736  C  C   . LEU A 1 90  ? -15.117 8.614   12.761  1.00 9.08  ? 90  LEU A C   1 
ATOM   737  O  O   . LEU A 1 90  ? -15.633 9.485   11.955  1.00 9.85  ? 90  LEU A O   1 
ATOM   738  C  CB  . LEU A 1 90  ? -17.085 7.206   13.328  1.00 8.25  ? 90  LEU A CB  1 
ATOM   739  C  CG  . LEU A 1 90  ? -16.551 6.052   12.458  1.00 8.20  ? 90  LEU A CG  1 
ATOM   740  C  CD1 . LEU A 1 90  ? -15.772 4.998   13.198  1.00 10.77 ? 90  LEU A CD1 1 
ATOM   741  C  CD2 . LEU A 1 90  ? -17.829 5.372   11.776  1.00 10.40 ? 90  LEU A CD2 1 
ATOM   742  N  N   . ILE A 1 91  ? -13.877 8.153   12.635  1.00 8.37  ? 91  ILE A N   1 
ATOM   743  C  CA  . ILE A 1 91  ? -12.947 8.589   11.539  1.00 8.09  ? 91  ILE A CA  1 
ATOM   744  C  C   . ILE A 1 91  ? -12.616 7.426   10.578  1.00 7.52  ? 91  ILE A C   1 
ATOM   745  O  O   . ILE A 1 91  ? -12.608 7.582   9.401   1.00 9.95  ? 91  ILE A O   1 
ATOM   746  C  CB  . ILE A 1 91  ? -11.626 9.232   12.088  1.00 7.49  ? 91  ILE A CB  1 
ATOM   747  C  CG1 . ILE A 1 91  ? -10.756 9.550   10.865  1.00 9.41  ? 91  ILE A CG1 1 
ATOM   748  C  CG2 . ILE A 1 91  ? -10.891 8.362   13.112  1.00 9.12  ? 91  ILE A CG2 1 
ATOM   749  C  CD1 . ILE A 1 91  ? -9.596  10.514  11.251  1.00 12.10 ? 91  ILE A CD1 1 
ATOM   750  N  N   . GLN A 1 92  ? -12.421 6.191   11.168  1.00 8.03  ? 92  GLN A N   1 
ATOM   751  C  CA  . GLN A 1 92  ? -12.147 5.055   10.271  1.00 8.10  ? 92  GLN A CA  1 
ATOM   752  C  C   . GLN A 1 92  ? -12.437 3.787   11.041  1.00 8.55  ? 92  GLN A C   1 
ATOM   753  O  O   . GLN A 1 92  ? -12.445 3.797   12.269  1.00 7.32  ? 92  GLN A O   1 
ATOM   754  C  CB  . GLN A 1 92  ? -10.733 5.032   9.725   1.00 9.96  ? 92  GLN A CB  1 
ATOM   755  C  CG  . GLN A 1 92  ? -9.646  5.149   10.879  1.00 12.10 ? 92  GLN A CG  1 
ATOM   756  C  CD  . GLN A 1 92  ? -8.928  3.799   11.199  1.00 13.93 ? 92  GLN A CD  1 
ATOM   757  O  OE1 . GLN A 1 92  ? -9.513  2.744   11.073  1.00 8.60  ? 92  GLN A OE1 1 
ATOM   758  N  NE2 . GLN A 1 92  ? -7.642  3.880   11.561  1.00 18.40 ? 92  GLN A NE2 1 
ATOM   759  N  N   . PHE A 1 93  ? -12.655 2.696   10.291  1.00 6.86  ? 93  PHE A N   1 
ATOM   760  C  CA  . PHE A 1 93  ? -12.498 1.361   10.928  1.00 7.41  ? 93  PHE A CA  1 
ATOM   761  C  C   . PHE A 1 93  ? -11.556 0.470   10.167  1.00 8.19  ? 93  PHE A C   1 
ATOM   762  O  O   . PHE A 1 93  ? -11.298 0.676   9.017   1.00 8.77  ? 93  PHE A O   1 
ATOM   763  C  CB  . PHE A 1 93  ? -13.819 0.668   11.199  1.00 7.07  ? 93  PHE A CB  1 
ATOM   764  C  CG  . PHE A 1 93  ? -14.558 0.202   9.937   1.00 10.06 ? 93  PHE A CG  1 
ATOM   765  C  CD1 . PHE A 1 93  ? -14.181 -0.968  9.276   1.00 10.77 ? 93  PHE A CD1 1 
ATOM   766  C  CD2 . PHE A 1 93  ? -15.655 0.935   9.473   1.00 10.41 ? 93  PHE A CD2 1 
ATOM   767  C  CE1 . PHE A 1 93  ? -14.888 -1.433  8.120   1.00 9.05  ? 93  PHE A CE1 1 
ATOM   768  C  CE2 . PHE A 1 93  ? -16.399 0.444   8.348   1.00 11.27 ? 93  PHE A CE2 1 
ATOM   769  C  CZ  . PHE A 1 93  ? -15.977 -0.698  7.673   1.00 13.68 ? 93  PHE A CZ  1 
ATOM   770  N  N   . HIS A 1 94  ? -11.082 -0.616  10.823  1.00 7.08  ? 94  HIS A N   1 
ATOM   771  C  CA  . HIS A 1 94  ? -10.159 -1.521  10.213  1.00 5.31  ? 94  HIS A CA  1 
ATOM   772  C  C   . HIS A 1 94  ? -10.212 -2.776  11.049  1.00 6.94  ? 94  HIS A C   1 
ATOM   773  O  O   . HIS A 1 94  ? -10.854 -2.795  12.081  1.00 6.83  ? 94  HIS A O   1 
ATOM   774  C  CB  . HIS A 1 94  ? -8.698  -1.036  10.157  1.00 8.75  ? 94  HIS A CB  1 
ATOM   775  C  CG  . HIS A 1 94  ? -8.172  -0.744  11.542  1.00 6.90  ? 94  HIS A CG  1 
ATOM   776  N  ND1 . HIS A 1 94  ? -8.367  0.470   12.175  1.00 8.14  ? 94  HIS A ND1 1 
ATOM   777  C  CD2 . HIS A 1 94  ? -7.545  -1.539  12.450  1.00 4.92  ? 94  HIS A CD2 1 
ATOM   778  C  CE1 . HIS A 1 94  ? -7.865  0.415   13.398  1.00 6.61  ? 94  HIS A CE1 1 
ATOM   779  N  NE2 . HIS A 1 94  ? -7.365  -0.801  13.594  1.00 9.16  ? 94  HIS A NE2 1 
ATOM   780  N  N   . PHE A 1 95  ? -9.486  -3.795  10.580  1.00 6.47  ? 95  PHE A N   1 
ATOM   781  C  CA  . PHE A 1 95  ? -9.529  -5.110  11.230  1.00 7.17  ? 95  PHE A CA  1 
ATOM   782  C  C   . PHE A 1 95  ? -8.061  -5.554  11.451  1.00 7.34  ? 95  PHE A C   1 
ATOM   783  O  O   . PHE A 1 95  ? -7.152  -5.085  10.729  1.00 8.06  ? 95  PHE A O   1 
ATOM   784  C  CB  . PHE A 1 95  ? -10.226 -6.186  10.330  1.00 7.69  ? 95  PHE A CB  1 
ATOM   785  C  CG  . PHE A 1 95  ? -11.653 -5.897  10.054  1.00 5.77  ? 95  PHE A CG  1 
ATOM   786  C  CD1 . PHE A 1 95  ? -11.966 -5.051  9.038   1.00 9.71  ? 95  PHE A CD1 1 
ATOM   787  C  CD2 . PHE A 1 95  ? -12.713 -6.545  10.762  1.00 8.12  ? 95  PHE A CD2 1 
ATOM   788  C  CE1 . PHE A 1 95  ? -13.305 -4.812  8.677   1.00 6.74  ? 95  PHE A CE1 1 
ATOM   789  C  CE2 . PHE A 1 95  ? -14.118 -6.299  10.472  1.00 7.91  ? 95  PHE A CE2 1 
ATOM   790  C  CZ  . PHE A 1 95  ? -14.378 -5.431  9.353   1.00 9.25  ? 95  PHE A CZ  1 
ATOM   791  N  N   . HIS A 1 96  ? -7.936  -6.536  12.339  1.00 6.99  ? 96  HIS A N   1 
ATOM   792  C  CA  . HIS A 1 96  ? -6.729  -7.324  12.540  1.00 7.52  ? 96  HIS A CA  1 
ATOM   793  C  C   . HIS A 1 96  ? -7.089  -8.770  12.405  1.00 7.16  ? 96  HIS A C   1 
ATOM   794  O  O   . HIS A 1 96  ? -8.129  -9.146  12.969  1.00 7.32  ? 96  HIS A O   1 
ATOM   795  C  CB  . HIS A 1 96  ? -6.120  -7.047  13.911  1.00 8.46  ? 96  HIS A CB  1 
ATOM   796  C  CG  . HIS A 1 96  ? -5.839  -5.614  14.193  1.00 8.80  ? 96  HIS A CG  1 
ATOM   797  N  ND1 . HIS A 1 96  ? -4.585  -5.071  14.019  1.00 7.96  ? 96  HIS A ND1 1 
ATOM   798  C  CD2 . HIS A 1 96  ? -6.648  -4.594  14.603  1.00 7.54  ? 96  HIS A CD2 1 
ATOM   799  C  CE1 . HIS A 1 96  ? -4.596  -3.788  14.431  1.00 7.34  ? 96  HIS A CE1 1 
ATOM   800  N  NE2 . HIS A 1 96  ? -5.845  -3.465  14.731  1.00 6.52  ? 96  HIS A NE2 1 
ATOM   801  N  N   . TRP A 1 97  ? -6.309  -9.562  11.654  1.00 6.44  ? 97  TRP A N   1 
ATOM   802  C  CA  . TRP A 1 97  ? -6.745  -10.993 11.560  1.00 9.04  ? 97  TRP A CA  1 
ATOM   803  C  C   . TRP A 1 97  ? -5.603  -11.929 11.462  1.00 7.46  ? 97  TRP A C   1 
ATOM   804  O  O   . TRP A 1 97  ? -4.429  -11.475 11.276  1.00 7.43  ? 97  TRP A O   1 
ATOM   805  C  CB  . TRP A 1 97  ? -7.693  -11.161 10.360  1.00 7.79  ? 97  TRP A CB  1 
ATOM   806  C  CG  . TRP A 1 97  ? -7.063  -10.770 9.042   1.00 9.31  ? 97  TRP A CG  1 
ATOM   807  C  CD1 . TRP A 1 97  ? -6.333  -11.580 8.232   1.00 10.15 ? 97  TRP A CD1 1 
ATOM   808  C  CD2 . TRP A 1 97  ? -7.000  -9.440  8.467   1.00 10.10 ? 97  TRP A CD2 1 
ATOM   809  N  NE1 . TRP A 1 97  ? -5.886  -10.838 7.072   1.00 10.15 ? 97  TRP A NE1 1 
ATOM   810  C  CE2 . TRP A 1 97  ? -6.248  -9.527  7.233   1.00 10.68 ? 97  TRP A CE2 1 
ATOM   811  C  CE3 . TRP A 1 97  ? -7.506  -8.172  8.883   1.00 9.63  ? 97  TRP A CE3 1 
ATOM   812  C  CZ2 . TRP A 1 97  ? -6.065  -8.459  6.394   1.00 9.48  ? 97  TRP A CZ2 1 
ATOM   813  C  CZ3 . TRP A 1 97  ? -7.250  -7.017  7.992   1.00 11.04 ? 97  TRP A CZ3 1 
ATOM   814  C  CH2 . TRP A 1 97  ? -6.557  -7.188  6.794   1.00 7.67  ? 97  TRP A CH2 1 
ATOM   815  N  N   . GLY A 1 98  ? -5.956  -13.225 11.524  1.00 8.00  ? 98  GLY A N   1 
ATOM   816  C  CA  . GLY A 1 98  ? -4.915  -14.230 11.495  1.00 7.64  ? 98  GLY A CA  1 
ATOM   817  C  C   . GLY A 1 98  ? -4.633  -14.928 10.136  1.00 8.64  ? 98  GLY A C   1 
ATOM   818  O  O   . GLY A 1 98  ? -5.322  -14.744 9.144   1.00 8.67  ? 98  GLY A O   1 
ATOM   819  N  N   . SER A 1 99  ? -3.588  -15.742 10.112  1.00 8.62  ? 99  SER A N   1 
ATOM   820  C  CA  . SER A 1 99  ? -3.369  -16.666 9.011   1.00 11.29 ? 99  SER A CA  1 
ATOM   821  C  C   . SER A 1 99  ? -4.230  -17.924 9.124   1.00 11.11 ? 99  SER A C   1 
ATOM   822  O  O   . SER A 1 99  ? -4.276  -18.695 8.155   1.00 13.34 ? 99  SER A O   1 
ATOM   823  C  CB  . SER A 1 99  ? -1.898  -17.078 9.030   1.00 10.97 ? 99  SER A CB  1 
ATOM   824  O  OG  . SER A 1 99  ? -1.457  -17.637 10.241  1.00 12.00 ? 99  SER A OG  1 
ATOM   825  N  N   . LEU A 1 100 ? -4.846  -18.125 10.301  1.00 11.04 ? 100 LEU A N   1 
ATOM   826  C  CA  . LEU A 1 100 ? -5.617  -19.289 10.635  1.00 12.03 ? 100 LEU A CA  1 
ATOM   827  C  C   . LEU A 1 100 ? -6.806  -18.802 11.472  1.00 11.28 ? 100 LEU A C   1 
ATOM   828  O  O   . LEU A 1 100 ? -6.708  -17.811 12.203  1.00 10.95 ? 100 LEU A O   1 
ATOM   829  C  CB  . LEU A 1 100 ? -4.807  -20.241 11.518  1.00 13.96 ? 100 LEU A CB  1 
ATOM   830  C  CG  . LEU A 1 100 ? -3.436  -20.595 11.019  1.00 16.85 ? 100 LEU A CG  1 
ATOM   831  C  CD1 . LEU A 1 100 ? -2.490  -20.975 12.135  1.00 24.48 ? 100 LEU A CD1 1 
ATOM   832  C  CD2 . LEU A 1 100 ? -3.678  -21.672 9.963   1.00 22.62 ? 100 LEU A CD2 1 
ATOM   833  N  N   . ASP A 1 101 ? -7.917  -19.534 11.446  1.00 8.58  ? 101 ASP A N   1 
ATOM   834  C  CA  . ASP A 1 101 ? -9.003  -19.096 12.337  1.00 9.46  ? 101 ASP A CA  1 
ATOM   835  C  C   . ASP A 1 101 ? -8.739  -19.034 13.831  1.00 10.38 ? 101 ASP A C   1 
ATOM   836  O  O   . ASP A 1 101 ? -9.381  -18.281 14.530  1.00 12.17 ? 101 ASP A O   1 
ATOM   837  C  CB  . ASP A 1 101 ? -10.254 -19.974 12.130  1.00 8.71  ? 101 ASP A CB  1 
ATOM   838  C  CG  . ASP A 1 101 ? -10.717 -20.015 10.683  1.00 11.99 ? 101 ASP A CG  1 
ATOM   839  O  OD1 . ASP A 1 101 ? -10.320 -19.140 9.887   1.00 11.18 ? 101 ASP A OD1 1 
ATOM   840  O  OD2 . ASP A 1 101 ? -11.494 -20.930 10.337  1.00 21.17 ? 101 ASP A OD2 1 
ATOM   841  N  N   . GLY A 1 102 ? -7.756  -19.852 14.321  1.00 10.52 ? 102 GLY A N   1 
ATOM   842  C  CA  . GLY A 1 102 ? -7.472  -19.826 15.751  1.00 9.96  ? 102 GLY A CA  1 
ATOM   843  C  C   . GLY A 1 102 ? -6.676  -18.637 16.300  1.00 7.14  ? 102 GLY A C   1 
ATOM   844  O  O   . GLY A 1 102 ? -6.325  -18.595 17.475  1.00 9.70  ? 102 GLY A O   1 
ATOM   845  N  N   . GLN A 1 103 ? -6.381  -17.667 15.440  1.00 7.29  ? 103 GLN A N   1 
ATOM   846  C  CA  . GLN A 1 103 ? -5.735  -16.447 15.997  1.00 8.34  ? 103 GLN A CA  1 
ATOM   847  C  C   . GLN A 1 103 ? -6.071  -15.285 15.086  1.00 9.36  ? 103 GLN A C   1 
ATOM   848  O  O   . GLN A 1 103 ? -6.674  -15.479 13.984  1.00 8.48  ? 103 GLN A O   1 
ATOM   849  C  CB  . GLN A 1 103 ? -4.224  -16.686 16.014  1.00 9.21  ? 103 GLN A CB  1 
ATOM   850  C  CG  . GLN A 1 103 ? -3.609  -16.873 14.602  1.00 8.56  ? 103 GLN A CG  1 
ATOM   851  C  CD  . GLN A 1 103 ? -2.166  -17.364 14.662  1.00 12.31 ? 103 GLN A CD  1 
ATOM   852  O  OE1 . GLN A 1 103 ? -1.810  -18.169 15.537  1.00 19.09 ? 103 GLN A OE1 1 
ATOM   853  N  NE2 . GLN A 1 103 ? -1.314  -16.919 13.718  1.00 13.76 ? 103 GLN A NE2 1 
ATOM   854  N  N   . GLY A 1 104 ? -5.712  -14.087 15.565  1.00 8.20  ? 104 GLY A N   1 
ATOM   855  C  CA  . GLY A 1 104 ? -5.987  -12.924 14.776  1.00 8.09  ? 104 GLY A CA  1 
ATOM   856  C  C   . GLY A 1 104 ? -6.470  -11.756 15.630  1.00 7.64  ? 104 GLY A C   1 
ATOM   857  O  O   . GLY A 1 104 ? -6.214  -10.594 15.241  1.00 8.10  ? 104 GLY A O   1 
ATOM   858  N  N   . SER A 1 105 ? -7.207  -12.018 16.711  1.00 6.57  ? 105 SER A N   1 
ATOM   859  C  CA  . SER A 1 105 ? -7.644  -10.807 17.531  1.00 6.37  ? 105 SER A CA  1 
ATOM   860  C  C   . SER A 1 105 ? -6.400  -10.292 18.281  1.00 6.37  ? 105 SER A C   1 
ATOM   861  O  O   . SER A 1 105 ? -5.356  -11.008 18.455  1.00 7.11  ? 105 SER A O   1 
ATOM   862  C  CB  . SER A 1 105 ? -8.734  -11.149 18.521  1.00 6.69  ? 105 SER A CB  1 
ATOM   863  O  OG  . SER A 1 105 ? -8.313  -12.138 19.469  1.00 6.74  ? 105 SER A OG  1 
ATOM   864  N  N   . GLU A 1 106 ? -6.528  -9.035  18.652  1.00 7.30  ? 106 GLU A N   1 
ATOM   865  C  CA  . GLU A 1 106 ? -5.498  -8.376  19.532  1.00 6.51  ? 106 GLU A CA  1 
ATOM   866  C  C   . GLU A 1 106 ? -5.864  -8.537  21.006  1.00 7.96  ? 106 GLU A C   1 
ATOM   867  O  O   . GLU A 1 106 ? -5.096  -9.098  21.795  1.00 6.53  ? 106 GLU A O   1 
ATOM   868  C  CB  . GLU A 1 106 ? -5.428  -6.854  19.119  1.00 4.64  ? 106 GLU A CB  1 
ATOM   869  C  CG  . GLU A 1 106 ? -4.876  -6.764  17.719  1.00 9.24  ? 106 GLU A CG  1 
ATOM   870  C  CD  . GLU A 1 106 ? -4.312  -5.441  17.319  1.00 8.96  ? 106 GLU A CD  1 
ATOM   871  O  OE1 . GLU A 1 106 ? -4.898  -4.412  17.601  1.00 6.44  ? 106 GLU A OE1 1 
ATOM   872  O  OE2 . GLU A 1 106 ? -3.132  -5.507  16.843  1.00 9.29  ? 106 GLU A OE2 1 
ATOM   873  N  N   . HIS A 1 107 ? -7.069  -8.075  21.408  1.00 6.33  ? 107 HIS A N   1 
ATOM   874  C  CA  . HIS A 1 107 ? -7.483  -8.432  22.733  1.00 5.40  ? 107 HIS A CA  1 
ATOM   875  C  C   . HIS A 1 107 ? -7.787  -9.939  22.751  1.00 5.07  ? 107 HIS A C   1 
ATOM   876  O  O   . HIS A 1 107 ? -8.178  -10.502 21.715  1.00 6.54  ? 107 HIS A O   1 
ATOM   877  C  CB  . HIS A 1 107 ? -8.734  -7.627  23.104  1.00 6.39  ? 107 HIS A CB  1 
ATOM   878  C  CG  . HIS A 1 107 ? -8.408  -6.189  23.291  1.00 4.64  ? 107 HIS A CG  1 
ATOM   879  N  ND1 . HIS A 1 107 ? -8.450  -5.301  22.246  1.00 6.70  ? 107 HIS A ND1 1 
ATOM   880  C  CD2 . HIS A 1 107 ? -7.903  -5.520  24.358  1.00 6.85  ? 107 HIS A CD2 1 
ATOM   881  C  CE1 . HIS A 1 107 ? -8.035  -4.103  22.673  1.00 7.95  ? 107 HIS A CE1 1 
ATOM   882  N  NE2 . HIS A 1 107 ? -7.695  -4.201  23.944  1.00 5.75  ? 107 HIS A NE2 1 
ATOM   883  N  N   . THR A 1 108 ? -7.604  -10.509 23.943  1.00 6.55  ? 108 THR A N   1 
ATOM   884  C  CA  . THR A 1 108 ? -8.011  -11.902 24.193  1.00 4.19  ? 108 THR A CA  1 
ATOM   885  C  C   . THR A 1 108 ? -8.924  -11.935 25.393  1.00 7.18  ? 108 THR A C   1 
ATOM   886  O  O   . THR A 1 108 ? -9.000  -11.025 26.226  1.00 8.26  ? 108 THR A O   1 
ATOM   887  C  CB  . THR A 1 108 ? -6.769  -12.783 24.376  1.00 3.92  ? 108 THR A CB  1 
ATOM   888  O  OG1 . THR A 1 108 ? -5.954  -12.273 25.465  1.00 6.72  ? 108 THR A OG1 1 
ATOM   889  C  CG2 . THR A 1 108 ? -5.886  -12.829 23.041  1.00 5.96  ? 108 THR A CG2 1 
ATOM   890  N  N   . VAL A 1 109 ? -9.697  -13.012 25.478  1.00 5.75  ? 109 VAL A N   1 
ATOM   891  C  CA  . VAL A 1 109 ? -10.720 -13.070 26.622  1.00 6.89  ? 109 VAL A CA  1 
ATOM   892  C  C   . VAL A 1 109 ? -10.387 -14.369 27.403  1.00 8.79  ? 109 VAL A C   1 
ATOM   893  O  O   . VAL A 1 109 ? -10.529 -15.478 26.837  1.00 8.20  ? 109 VAL A O   1 
ATOM   894  C  CB  . VAL A 1 109 ? -12.152 -13.142 26.082  1.00 9.40  ? 109 VAL A CB  1 
ATOM   895  C  CG1 . VAL A 1 109 ? -13.178 -13.279 27.243  1.00 11.27 ? 109 VAL A CG1 1 
ATOM   896  C  CG2 . VAL A 1 109 ? -12.498 -11.823 25.280  1.00 9.78  ? 109 VAL A CG2 1 
ATOM   897  N  N   . ASP A 1 110 ? -9.871  -14.225 28.613  1.00 8.48  ? 110 ASP A N   1 
ATOM   898  C  CA  . ASP A 1 110 ? -9.346  -15.430 29.379  1.00 10.93 ? 110 ASP A CA  1 
ATOM   899  C  C   . ASP A 1 110 ? -8.432  -16.238 28.451  1.00 8.68  ? 110 ASP A C   1 
ATOM   900  O  O   . ASP A 1 110 ? -8.595  -17.516 28.368  1.00 10.27 ? 110 ASP A O   1 
ATOM   901  C  CB  . ASP A 1 110 ? -10.544 -16.251 29.821  1.00 9.60  ? 110 ASP A CB  1 
ATOM   902  C  CG  . ASP A 1 110 ? -11.448 -15.436 30.871  1.00 5.99  ? 110 ASP A CG  1 
ATOM   903  O  OD1 . ASP A 1 110 ? -10.815 -14.571 31.541  1.00 12.94 ? 110 ASP A OD1 1 
ATOM   904  O  OD2 . ASP A 1 110 ? -12.649 -15.777 30.996  1.00 15.34 ? 110 ASP A OD2 1 
ATOM   905  N  N   . LYS A 1 111 ? -7.543  -15.509 27.733  1.00 8.10  ? 111 LYS A N   1 
ATOM   906  C  CA  . LYS A 1 111 ? -6.511  -16.045 26.803  1.00 8.18  ? 111 LYS A CA  1 
ATOM   907  C  C   . LYS A 1 111 ? -7.065  -16.606 25.479  1.00 7.06  ? 111 LYS A C   1 
ATOM   908  O  O   . LYS A 1 111 ? -6.304  -17.007 24.611  1.00 8.11  ? 111 LYS A O   1 
ATOM   909  C  CB  . LYS A 1 111 ? -5.650  -17.125 27.524  1.00 9.69  ? 111 LYS A CB  1 
ATOM   910  C  CG  . LYS A 1 111 ? -4.879  -16.509 28.748  1.00 12.69 ? 111 LYS A CG  1 
ATOM   911  C  CD  . LYS A 1 111 ? -3.909  -15.390 28.259  1.00 15.89 ? 111 LYS A CD  1 
ATOM   912  C  CE  . LYS A 1 111 ? -3.086  -14.785 29.460  1.00 17.15 ? 111 LYS A CE  1 
ATOM   913  N  NZ  . LYS A 1 111 ? -1.877  -15.553 29.660  1.00 20.70 ? 111 LYS A NZ  1 
ATOM   914  N  N   . LYS A 1 112 ? -8.394  -16.532 25.283  1.00 4.80  ? 112 LYS A N   1 
ATOM   915  C  CA  . LYS A 1 112 ? -9.006  -16.981 24.031  1.00 8.54  ? 112 LYS A CA  1 
ATOM   916  C  C   . LYS A 1 112 ? -8.673  -15.909 22.954  1.00 9.46  ? 112 LYS A C   1 
ATOM   917  O  O   . LYS A 1 112 ? -8.924  -14.685 23.129  1.00 7.89  ? 112 LYS A O   1 
ATOM   918  C  CB  . LYS A 1 112 ? -10.527 -17.071 24.132  1.00 8.16  ? 112 LYS A CB  1 
ATOM   919  C  CG  . LYS A 1 112 ? -11.220 -17.433 22.776  1.00 11.29 ? 112 LYS A CG  1 
ATOM   920  C  CD  . LYS A 1 112 ? -12.779 -17.343 22.975  1.00 11.92 ? 112 LYS A CD  1 
ATOM   921  C  CE  . LYS A 1 112 ? -13.380 -17.499 21.535  1.00 14.11 ? 112 LYS A CE  1 
ATOM   922  N  NZ  . LYS A 1 112 ? -13.161 -18.899 21.122  1.00 12.82 ? 112 LYS A NZ  1 
ATOM   923  N  N   A LYS A 1 113 ? -8.118  -16.400 21.853  0.50 9.23  ? 113 LYS A N   1 
ATOM   924  N  N   B LYS A 1 113 ? -8.109  -16.407 21.850  0.50 9.28  ? 113 LYS A N   1 
ATOM   925  C  CA  A LYS A 1 113 ? -7.967  -15.606 20.630  0.50 9.42  ? 113 LYS A CA  1 
ATOM   926  C  CA  B LYS A 1 113 ? -7.916  -15.635 20.600  0.50 9.63  ? 113 LYS A CA  1 
ATOM   927  C  C   A LYS A 1 113 ? -9.149  -15.839 19.667  0.50 8.17  ? 113 LYS A C   1 
ATOM   928  C  C   B LYS A 1 113 ? -9.058  -15.836 19.551  0.50 8.23  ? 113 LYS A C   1 
ATOM   929  O  O   A LYS A 1 113 ? -9.576  -16.984 19.477  0.50 6.84  ? 113 LYS A O   1 
ATOM   930  O  O   B LYS A 1 113 ? -9.357  -16.958 19.157  0.50 7.64  ? 113 LYS A O   1 
ATOM   931  C  CB  A LYS A 1 113 ? -6.652  -15.990 19.929  0.50 9.95  ? 113 LYS A CB  1 
ATOM   932  C  CB  B LYS A 1 113 ? -6.551  -16.000 19.951  0.50 9.87  ? 113 LYS A CB  1 
ATOM   933  C  CG  A LYS A 1 113 ? -5.471  -15.827 20.809  0.50 8.43  ? 113 LYS A CG  1 
ATOM   934  C  CG  B LYS A 1 113 ? -5.366  -15.365 20.638  0.50 8.38  ? 113 LYS A CG  1 
ATOM   935  C  CD  A LYS A 1 113 ? -4.298  -16.466 20.080  0.50 7.75  ? 113 LYS A CD  1 
ATOM   936  C  CD  B LYS A 1 113 ? -4.058  -15.838 19.998  0.50 9.87  ? 113 LYS A CD  1 
ATOM   937  C  CE  A LYS A 1 113 ? -2.989  -15.768 20.515  0.50 8.77  ? 113 LYS A CE  1 
ATOM   938  C  CE  B LYS A 1 113 ? -2.849  -15.520 20.895  0.50 8.58  ? 113 LYS A CE  1 
ATOM   939  N  NZ  A LYS A 1 113 ? -2.511  -16.458 21.734  0.50 8.53  ? 113 LYS A NZ  1 
ATOM   940  N  NZ  B LYS A 1 113 ? -1.616  -16.297 20.556  0.50 12.03 ? 113 LYS A NZ  1 
ATOM   941  N  N   . TYR A 1 114 ? -9.685  -14.743 19.121  1.00 8.80  ? 114 TYR A N   1 
ATOM   942  C  CA  . TYR A 1 114 ? -10.670 -14.818 18.099  1.00 8.16  ? 114 TYR A CA  1 
ATOM   943  C  C   . TYR A 1 114 ? -10.038 -14.768 16.731  1.00 7.95  ? 114 TYR A C   1 
ATOM   944  O  O   . TYR A 1 114 ? -8.857  -14.430 16.603  1.00 8.36  ? 114 TYR A O   1 
ATOM   945  C  CB  . TYR A 1 114 ? -11.733 -13.668 18.212  1.00 8.13  ? 114 TYR A CB  1 
ATOM   946  C  CG  . TYR A 1 114 ? -12.716 -13.855 19.404  1.00 6.28  ? 114 TYR A CG  1 
ATOM   947  C  CD1 . TYR A 1 114 ? -12.382 -13.504 20.688  1.00 7.94  ? 114 TYR A CD1 1 
ATOM   948  C  CD2 . TYR A 1 114 ? -13.958 -14.517 19.188  1.00 11.00 ? 114 TYR A CD2 1 
ATOM   949  C  CE1 . TYR A 1 114 ? -13.224 -13.708 21.737  1.00 8.57  ? 114 TYR A CE1 1 
ATOM   950  C  CE2 . TYR A 1 114 ? -14.881 -14.682 20.208  1.00 9.57  ? 114 TYR A CE2 1 
ATOM   951  C  CZ  . TYR A 1 114 ? -14.488 -14.289 21.505  1.00 9.99  ? 114 TYR A CZ  1 
ATOM   952  O  OH  . TYR A 1 114 ? -15.322 -14.418 22.560  1.00 13.05 ? 114 TYR A OH  1 
ATOM   953  N  N   . ALA A 1 115 ? -10.803 -15.050 15.653  1.00 7.62  ? 115 ALA A N   1 
ATOM   954  C  CA  . ALA A 1 115 ? -10.283 -15.092 14.277  1.00 8.27  ? 115 ALA A CA  1 
ATOM   955  C  C   . ALA A 1 115 ? -9.839  -13.705 13.748  1.00 7.32  ? 115 ALA A C   1 
ATOM   956  O  O   . ALA A 1 115 ? -8.967  -13.533 12.892  1.00 8.24  ? 115 ALA A O   1 
ATOM   957  C  CB  . ALA A 1 115 ? -11.372 -15.717 13.309  1.00 9.07  ? 115 ALA A CB  1 
ATOM   958  N  N   . ALA A 1 116 ? -10.541 -12.691 14.313  1.00 8.24  ? 116 ALA A N   1 
ATOM   959  C  CA  . ALA A 1 116 ? -10.194 -11.326 13.922  1.00 6.39  ? 116 ALA A CA  1 
ATOM   960  C  C   . ALA A 1 116 ? -10.747 -10.326 14.901  1.00 7.55  ? 116 ALA A C   1 
ATOM   961  O  O   . ALA A 1 116 ? -11.482 -10.707 15.852  1.00 5.89  ? 116 ALA A O   1 
ATOM   962  C  CB  . ALA A 1 116 ? -10.687 -11.015 12.482  1.00 7.32  ? 116 ALA A CB  1 
ATOM   963  N  N   . GLU A 1 117 ? -10.387 -9.050  14.697  1.00 7.01  ? 117 GLU A N   1 
ATOM   964  C  CA  . GLU A 1 117 ? -10.946 -8.060  15.595  1.00 6.70  ? 117 GLU A CA  1 
ATOM   965  C  C   . GLU A 1 117 ? -11.143 -6.756  14.799  1.00 8.51  ? 117 GLU A C   1 
ATOM   966  O  O   . GLU A 1 117 ? -10.279 -6.370  14.080  1.00 7.72  ? 117 GLU A O   1 
ATOM   967  C  CB  . GLU A 1 117 ? -9.960  -7.764  16.765  1.00 5.90  ? 117 GLU A CB  1 
ATOM   968  C  CG  . GLU A 1 117 ? -10.512 -6.741  17.861  1.00 5.48  ? 117 GLU A CG  1 
ATOM   969  C  CD  . GLU A 1 117 ? -9.573  -6.706  19.056  1.00 7.53  ? 117 GLU A CD  1 
ATOM   970  O  OE1 . GLU A 1 117 ? -8.942  -7.765  19.369  1.00 7.59  ? 117 GLU A OE1 1 
ATOM   971  O  OE2 . GLU A 1 117 ? -9.619  -5.658  19.779  1.00 8.90  ? 117 GLU A OE2 1 
ATOM   972  N  N   . LEU A 1 118 ? -12.313 -6.188  14.922  1.00 6.41  ? 118 LEU A N   1 
ATOM   973  C  CA  . LEU A 1 118 ? -12.660 -4.934  14.263  1.00 6.22  ? 118 LEU A CA  1 
ATOM   974  C  C   . LEU A 1 118 ? -12.467 -3.728  15.245  1.00 5.42  ? 118 LEU A C   1 
ATOM   975  O  O   . LEU A 1 118 ? -12.860 -3.818  16.400  1.00 6.00  ? 118 LEU A O   1 
ATOM   976  C  CB  . LEU A 1 118 ? -14.189 -4.984  13.886  1.00 4.08  ? 118 LEU A CB  1 
ATOM   977  C  CG  . LEU A 1 118 ? -14.912 -3.634  13.549  1.00 7.41  ? 118 LEU A CG  1 
ATOM   978  C  CD1 . LEU A 1 118 ? -14.330 -3.083  12.305  1.00 9.19  ? 118 LEU A CD1 1 
ATOM   979  C  CD2 . LEU A 1 118 ? -16.425 -4.010  13.308  1.00 8.36  ? 118 LEU A CD2 1 
ATOM   980  N  N   . HIS A 1 119 ? -11.837 -2.634  14.769  1.00 5.09  ? 119 HIS A N   1 
ATOM   981  C  CA  . HIS A 1 119 ? -11.615 -1.463  15.555  1.00 4.53  ? 119 HIS A CA  1 
ATOM   982  C  C   . HIS A 1 119 ? -12.324 -0.308  14.854  1.00 5.61  ? 119 HIS A C   1 
ATOM   983  O  O   . HIS A 1 119 ? -11.965 0.017   13.682  1.00 6.79  ? 119 HIS A O   1 
ATOM   984  C  CB  . HIS A 1 119 ? -10.108 -1.253  15.598  1.00 5.33  ? 119 HIS A CB  1 
ATOM   985  C  CG  . HIS A 1 119 ? -9.478  -2.222  16.515  1.00 4.07  ? 119 HIS A CG  1 
ATOM   986  N  ND1 . HIS A 1 119 ? -8.110  -2.438  16.530  1.00 7.07  ? 119 HIS A ND1 1 
ATOM   987  C  CD2 . HIS A 1 119 ? -10.013 -3.009  17.488  1.00 4.67  ? 119 HIS A CD2 1 
ATOM   988  C  CE1 . HIS A 1 119 ? -7.817  -3.355  17.434  1.00 6.51  ? 119 HIS A CE1 1 
ATOM   989  N  NE2 . HIS A 1 119 ? -8.952  -3.726  18.043  1.00 5.61  ? 119 HIS A NE2 1 
ATOM   990  N  N   . LEU A 1 120 ? -13.317 0.273   15.532  1.00 5.53  ? 120 LEU A N   1 
ATOM   991  C  CA  . LEU A 1 120 ? -13.994 1.527   15.072  1.00 6.77  ? 120 LEU A CA  1 
ATOM   992  C  C   . LEU A 1 120 ? -13.391 2.668   15.809  1.00 5.76  ? 120 LEU A C   1 
ATOM   993  O  O   . LEU A 1 120 ? -13.505 2.716   17.056  1.00 5.85  ? 120 LEU A O   1 
ATOM   994  C  CB  . LEU A 1 120 ? -15.462 1.464   15.302  1.00 4.83  ? 120 LEU A CB  1 
ATOM   995  C  CG  . LEU A 1 120 ? -16.065 0.331   14.420  1.00 7.76  ? 120 LEU A CG  1 
ATOM   996  C  CD1 . LEU A 1 120 ? -16.912 -0.570  15.184  1.00 11.23 ? 120 LEU A CD1 1 
ATOM   997  C  CD2 . LEU A 1 120 ? -16.869 1.006   13.247  1.00 10.90 ? 120 LEU A CD2 1 
ATOM   998  N  N   . VAL A 1 121 ? -12.625 3.491   15.065  1.00 5.86  ? 121 VAL A N   1 
ATOM   999  C  CA  . VAL A 1 121 ? -11.788 4.482   15.791  1.00 6.24  ? 121 VAL A CA  1 
ATOM   1000 C  C   . VAL A 1 121 ? -12.480 5.844   15.827  1.00 7.08  ? 121 VAL A C   1 
ATOM   1001 O  O   . VAL A 1 121 ? -12.881 6.336   14.739  1.00 7.37  ? 121 VAL A O   1 
ATOM   1002 C  CB  . VAL A 1 121 ? -10.470 4.638   14.991  1.00 6.94  ? 121 VAL A CB  1 
ATOM   1003 C  CG1 . VAL A 1 121 ? -9.496  5.653   15.625  1.00 5.71  ? 121 VAL A CG1 1 
ATOM   1004 C  CG2 . VAL A 1 121 ? -9.762  3.246   14.788  1.00 7.62  ? 121 VAL A CG2 1 
ATOM   1005 N  N   . HIS A 1 122 ? -12.523 6.464   17.016  1.00 5.74  ? 122 HIS A N   1 
ATOM   1006 C  CA  . HIS A 1 122 ? -13.254 7.716   17.152  1.00 5.87  ? 122 HIS A CA  1 
ATOM   1007 C  C   . HIS A 1 122 ? -12.384 8.711   17.881  1.00 7.72  ? 122 HIS A C   1 
ATOM   1008 O  O   . HIS A 1 122 ? -11.648 8.333   18.803  1.00 5.95  ? 122 HIS A O   1 
ATOM   1009 C  CB  . HIS A 1 122 ? -14.532 7.577   17.960  1.00 9.38  ? 122 HIS A CB  1 
ATOM   1010 C  CG  . HIS A 1 122 ? -15.435 6.421   17.581  1.00 9.01  ? 122 HIS A CG  1 
ATOM   1011 N  ND1 . HIS A 1 122 ? -15.125 5.106   17.864  1.00 6.98  ? 122 HIS A ND1 1 
ATOM   1012 C  CD2 . HIS A 1 122 ? -16.654 6.381   16.926  1.00 10.33 ? 122 HIS A CD2 1 
ATOM   1013 C  CE1 . HIS A 1 122 ? -16.087 4.301   17.374  1.00 10.44 ? 122 HIS A CE1 1 
ATOM   1014 N  NE2 . HIS A 1 122 ? -17.031 5.054   16.818  1.00 10.64 ? 122 HIS A NE2 1 
ATOM   1015 N  N   . TRP A 1 123 ? -12.509 10.009  17.502  1.00 6.72  ? 123 TRP A N   1 
ATOM   1016 C  CA  . TRP A 1 123 ? -11.696 11.004  18.248  1.00 6.16  ? 123 TRP A CA  1 
ATOM   1017 C  C   . TRP A 1 123 ? -12.579 12.019  19.014  1.00 8.54  ? 123 TRP A C   1 
ATOM   1018 O  O   . TRP A 1 123 ? -13.719 12.354  18.579  1.00 10.56 ? 123 TRP A O   1 
ATOM   1019 C  CB  . TRP A 1 123 ? -10.732 11.719  17.297  1.00 8.83  ? 123 TRP A CB  1 
ATOM   1020 C  CG  . TRP A 1 123 ? -11.390 12.349  16.126  1.00 8.23  ? 123 TRP A CG  1 
ATOM   1021 C  CD1 . TRP A 1 123 ? -11.634 11.767  14.889  1.00 8.16  ? 123 TRP A CD1 1 
ATOM   1022 C  CD2 . TRP A 1 123 ? -11.896 13.729  16.025  1.00 12.11 ? 123 TRP A CD2 1 
ATOM   1023 N  NE1 . TRP A 1 123 ? -12.319 12.663  14.052  1.00 8.78  ? 123 TRP A NE1 1 
ATOM   1024 C  CE2 . TRP A 1 123 ? -12.458 13.879  14.712  1.00 11.89 ? 123 TRP A CE2 1 
ATOM   1025 C  CE3 . TRP A 1 123 ? -11.945 14.835  16.923  1.00 10.96 ? 123 TRP A CE3 1 
ATOM   1026 C  CZ2 . TRP A 1 123 ? -13.051 15.097  14.283  1.00 13.46 ? 123 TRP A CZ2 1 
ATOM   1027 C  CZ3 . TRP A 1 123 ? -12.535 16.020  16.478  1.00 11.62 ? 123 TRP A CZ3 1 
ATOM   1028 C  CH2 . TRP A 1 123 ? -13.041 16.163  15.191  1.00 9.33  ? 123 TRP A CH2 1 
ATOM   1029 N  N   . ASN A 1 124 ? -12.058 12.454  20.151  1.00 8.29  ? 124 ASN A N   1 
ATOM   1030 C  CA  . ASN A 1 124 ? -12.779 13.350  21.059  1.00 7.70  ? 124 ASN A CA  1 
ATOM   1031 C  C   . ASN A 1 124 ? -12.983 14.763  20.441  1.00 8.52  ? 124 ASN A C   1 
ATOM   1032 O  O   . ASN A 1 124 ? -12.009 15.428  20.120  1.00 7.17  ? 124 ASN A O   1 
ATOM   1033 C  CB  . ASN A 1 124 ? -11.959 13.419  22.352  1.00 8.36  ? 124 ASN A CB  1 
ATOM   1034 C  CG  . ASN A 1 124 ? -12.759 13.997  23.513  1.00 10.09 ? 124 ASN A CG  1 
ATOM   1035 O  OD1 . ASN A 1 124 ? -13.686 14.802  23.275  1.00 10.92 ? 124 ASN A OD1 1 
ATOM   1036 N  ND2 . ASN A 1 124 ? -12.524 13.512  24.729  1.00 9.78  ? 124 ASN A ND2 1 
ATOM   1037 N  N   . THR A 1 125 ? -14.255 15.183  20.292  1.00 10.03 ? 125 THR A N   1 
ATOM   1038 C  CA  . THR A 1 125 ? -14.503 16.418  19.552  1.00 12.68 ? 125 THR A CA  1 
ATOM   1039 C  C   . THR A 1 125 ? -13.946 17.662  20.286  1.00 12.42 ? 125 THR A C   1 
ATOM   1040 O  O   . THR A 1 125 ? -13.702 18.678  19.615  1.00 13.10 ? 125 THR A O   1 
ATOM   1041 C  CB  . THR A 1 125 ? -15.999 16.597  19.219  1.00 13.07 ? 125 THR A CB  1 
ATOM   1042 O  OG1 . THR A 1 125 ? -16.775 16.442  20.408  1.00 15.36 ? 125 THR A OG1 1 
ATOM   1043 C  CG2 . THR A 1 125 ? -16.396 15.484  18.226  1.00 14.70 ? 125 THR A CG2 1 
ATOM   1044 N  N   . LYS A 1 126 ? -13.631 17.386  21.661  1.00 9.05  ? 127 LYS A N   1 
ATOM   1045 C  CA  . LYS A 1 126 ? -13.105 18.579  22.406  1.00 11.05 ? 127 LYS A CA  1 
ATOM   1046 C  C   . LYS A 1 126 ? -11.687 18.980  21.892  1.00 11.22 ? 127 LYS A C   1 
ATOM   1047 O  O   . LYS A 1 126 ? -11.175 20.062  22.248  1.00 13.59 ? 127 LYS A O   1 
ATOM   1048 C  CB  . LYS A 1 126 ? -13.137 18.334  23.920  1.00 12.98 ? 127 LYS A CB  1 
ATOM   1049 C  CG  . LYS A 1 126 ? -12.152 17.414  24.432  1.00 14.36 ? 127 LYS A CG  1 
ATOM   1050 C  CD  . LYS A 1 126 ? -12.391 17.255  25.976  1.00 20.15 ? 127 LYS A CD  1 
ATOM   1051 C  CE  . LYS A 1 126 ? -11.429 16.354  26.624  1.00 26.45 ? 127 LYS A CE  1 
ATOM   1052 N  NZ  . LYS A 1 126 ? -10.861 17.041  27.893  1.00 30.62 ? 127 LYS A NZ  1 
ATOM   1053 N  N   . TYR A 1 127 ? -11.021 18.082  21.145  1.00 7.96  ? 128 TYR A N   1 
ATOM   1054 C  CA  . TYR A 1 127 ? -9.689  18.356  20.610  1.00 9.48  ? 128 TYR A CA  1 
ATOM   1055 C  C   . TYR A 1 127 ? -9.664  18.786  19.136  1.00 9.42  ? 128 TYR A C   1 
ATOM   1056 O  O   . TYR A 1 127 ? -8.565  18.991  18.556  1.00 9.93  ? 128 TYR A O   1 
ATOM   1057 C  CB  . TYR A 1 127 ? -8.681  17.206  20.900  1.00 9.50  ? 128 TYR A CB  1 
ATOM   1058 C  CG  . TYR A 1 127 ? -8.617  16.942  22.351  1.00 8.67  ? 128 TYR A CG  1 
ATOM   1059 C  CD1 . TYR A 1 127 ? -8.203  17.933  23.263  1.00 13.07 ? 128 TYR A CD1 1 
ATOM   1060 C  CD2 . TYR A 1 127 ? -8.935  15.668  22.871  1.00 7.95  ? 128 TYR A CD2 1 
ATOM   1061 C  CE1 . TYR A 1 127 ? -8.139  17.639  24.635  1.00 8.35  ? 128 TYR A CE1 1 
ATOM   1062 C  CE2 . TYR A 1 127 ? -8.858  15.345  24.210  1.00 8.60  ? 128 TYR A CE2 1 
ATOM   1063 C  CZ  . TYR A 1 127 ? -8.449  16.397  25.115  1.00 10.17 ? 128 TYR A CZ  1 
ATOM   1064 O  OH  . TYR A 1 127 ? -8.436  16.097  26.438  1.00 12.60 ? 128 TYR A OH  1 
ATOM   1065 N  N   . GLY A 1 128 ? -10.836 18.886  18.513  1.00 9.91  ? 129 GLY A N   1 
ATOM   1066 C  CA  . GLY A 1 128 ? -10.951 19.607  17.218  1.00 11.89 ? 129 GLY A CA  1 
ATOM   1067 C  C   . GLY A 1 128 ? -10.592 18.716  15.993  1.00 12.13 ? 129 GLY A C   1 
ATOM   1068 O  O   . GLY A 1 128 ? -11.206 18.802  14.916  1.00 14.05 ? 129 GLY A O   1 
ATOM   1069 N  N   . ASP A 1 129 ? -9.613  17.803  16.116  1.00 11.84 ? 130 ASP A N   1 
ATOM   1070 C  CA  . ASP A 1 129 ? -9.377  16.865  14.996  1.00 12.80 ? 130 ASP A CA  1 
ATOM   1071 C  C   . ASP A 1 129 ? -8.611  15.654  15.553  1.00 13.27 ? 130 ASP A C   1 
ATOM   1072 O  O   . ASP A 1 129 ? -8.155  15.667  16.713  1.00 10.62 ? 130 ASP A O   1 
ATOM   1073 C  CB  . ASP A 1 129 ? -8.725  17.483  13.751  1.00 12.83 ? 130 ASP A CB  1 
ATOM   1074 C  CG  . ASP A 1 129 ? -7.295  17.973  13.978  1.00 13.80 ? 130 ASP A CG  1 
ATOM   1075 O  OD1 . ASP A 1 129 ? -6.685  17.722  15.039  1.00 17.99 ? 130 ASP A OD1 1 
ATOM   1076 O  OD2 . ASP A 1 129 ? -6.773  18.630  13.052  1.00 15.09 ? 130 ASP A OD2 1 
ATOM   1077 N  N   . PHE A 1 130 ? -8.469  14.654  14.694  1.00 12.92 ? 131 PHE A N   1 
ATOM   1078 C  CA  . PHE A 1 130 ? -7.741  13.446  15.042  1.00 12.82 ? 131 PHE A CA  1 
ATOM   1079 C  C   . PHE A 1 130 ? -6.282  13.705  15.429  1.00 11.40 ? 131 PHE A C   1 
ATOM   1080 O  O   . PHE A 1 130 ? -5.822  13.173  16.469  1.00 8.88  ? 131 PHE A O   1 
ATOM   1081 C  CB  . PHE A 1 130 ? -7.846  12.427  13.883  1.00 12.32 ? 131 PHE A CB  1 
ATOM   1082 C  CG  . PHE A 1 130 ? -7.131  11.129  14.129  1.00 12.55 ? 131 PHE A CG  1 
ATOM   1083 C  CD1 . PHE A 1 130 ? -7.759  10.084  14.838  1.00 9.87  ? 131 PHE A CD1 1 
ATOM   1084 C  CD2 . PHE A 1 130 ? -5.824  10.942  13.711  1.00 14.99 ? 131 PHE A CD2 1 
ATOM   1085 C  CE1 . PHE A 1 130 ? -7.088  8.897   15.101  1.00 13.70 ? 131 PHE A CE1 1 
ATOM   1086 C  CE2 . PHE A 1 130 ? -5.190  9.711   13.921  1.00 12.83 ? 131 PHE A CE2 1 
ATOM   1087 C  CZ  . PHE A 1 130 ? -5.845  8.695   14.651  1.00 11.25 ? 131 PHE A CZ  1 
ATOM   1088 N  N   . GLY A 1 131 ? -5.568  14.516  14.612  1.00 11.72 ? 132 GLY A N   1 
ATOM   1089 C  CA  . GLY A 1 131 ? -4.182  14.713  14.893  1.00 12.69 ? 132 GLY A CA  1 
ATOM   1090 C  C   . GLY A 1 131 ? -3.883  15.314  16.242  1.00 11.96 ? 132 GLY A C   1 
ATOM   1091 O  O   . GLY A 1 131 ? -2.872  14.968  16.898  1.00 15.34 ? 132 GLY A O   1 
ATOM   1092 N  N   . LYS A 1 132 ? -4.696  16.284  16.671  1.00 11.78 ? 133 LYS A N   1 
ATOM   1093 C  CA  . LYS A 1 132 ? -4.516  16.806  18.024  1.00 11.07 ? 133 LYS A CA  1 
ATOM   1094 C  C   . LYS A 1 132 ? -5.014  15.852  19.148  1.00 11.74 ? 133 LYS A C   1 
ATOM   1095 O  O   . LYS A 1 132 ? -4.417  15.716  20.225  1.00 11.87 ? 133 LYS A O   1 
ATOM   1096 C  CB  . LYS A 1 132 ? -5.280  18.106  18.136  1.00 13.03 ? 133 LYS A CB  1 
ATOM   1097 C  CG  . LYS A 1 132 ? -4.649  19.275  17.307  1.00 17.84 ? 133 LYS A CG  1 
ATOM   1098 C  CD  . LYS A 1 132 ? -3.117  19.516  17.522  1.00 25.89 ? 133 LYS A CD  1 
ATOM   1099 C  CE  . LYS A 1 132 ? -2.893  20.921  18.241  1.00 28.92 ? 133 LYS A CE  1 
ATOM   1100 N  NZ  . LYS A 1 132 ? -1.493  21.339  18.732  1.00 29.71 ? 133 LYS A NZ  1 
ATOM   1101 N  N   . ALA A 1 133 ? -6.102  15.189  18.849  1.00 10.13 ? 134 ALA A N   1 
ATOM   1102 C  CA  . ALA A 1 133 ? -6.626  14.227  19.781  1.00 9.72  ? 134 ALA A CA  1 
ATOM   1103 C  C   . ALA A 1 133 ? -5.650  13.142  20.277  1.00 7.78  ? 134 ALA A C   1 
ATOM   1104 O  O   . ALA A 1 133 ? -5.652  12.744  21.483  1.00 8.64  ? 134 ALA A O   1 
ATOM   1105 C  CB  . ALA A 1 133 ? -7.902  13.529  19.120  1.00 8.11  ? 134 ALA A CB  1 
ATOM   1106 N  N   . VAL A 1 134 ? -4.895  12.570  19.315  1.00 7.88  ? 135 VAL A N   1 
ATOM   1107 C  CA  . VAL A 1 134 ? -3.926  11.472  19.679  1.00 10.01 ? 135 VAL A CA  1 
ATOM   1108 C  C   . VAL A 1 134 ? -2.815  11.906  20.623  1.00 8.75  ? 135 VAL A C   1 
ATOM   1109 O  O   . VAL A 1 134 ? -2.116  11.083  21.155  1.00 9.09  ? 135 VAL A O   1 
ATOM   1110 C  CB  . VAL A 1 134 ? -3.328  10.752  18.429  1.00 9.45  ? 135 VAL A CB  1 
ATOM   1111 C  CG1 . VAL A 1 134 ? -4.470  10.168  17.586  1.00 10.54 ? 135 VAL A CG1 1 
ATOM   1112 C  CG2 . VAL A 1 134 ? -2.428  11.651  17.596  1.00 13.50 ? 135 VAL A CG2 1 
ATOM   1113 N  N   . GLN A 1 135 ? -2.720  13.217  20.818  1.00 8.73  ? 136 GLN A N   1 
ATOM   1114 C  CA  . GLN A 1 135 ? -1.676  13.717  21.762  1.00 11.27 ? 136 GLN A CA  1 
ATOM   1115 C  C   . GLN A 1 135 ? -2.248  13.843  23.174  1.00 12.22 ? 136 GLN A C   1 
ATOM   1116 O  O   . GLN A 1 135 ? -1.602  14.399  24.130  1.00 14.04 ? 136 GLN A O   1 
ATOM   1117 C  CB  . GLN A 1 135 ? -1.173  15.107  21.258  1.00 11.42 ? 136 GLN A CB  1 
ATOM   1118 C  CG  . GLN A 1 135 ? -0.610  15.003  19.884  1.00 13.88 ? 136 GLN A CG  1 
ATOM   1119 C  CD  . GLN A 1 135 ? -0.100  16.290  19.336  1.00 24.38 ? 136 GLN A CD  1 
ATOM   1120 O  OE1 . GLN A 1 135 ? -0.459  16.681  18.206  1.00 27.53 ? 136 GLN A OE1 1 
ATOM   1121 N  NE2 . GLN A 1 135 ? 0.706   16.980  20.126  1.00 21.77 ? 136 GLN A NE2 1 
ATOM   1122 N  N   . GLN A 1 136 ? -3.476  13.382  23.369  1.00 11.20 ? 137 GLN A N   1 
ATOM   1123 C  CA  . GLN A 1 136 ? -4.134  13.582  24.654  1.00 10.75 ? 137 GLN A CA  1 
ATOM   1124 C  C   . GLN A 1 136 ? -4.545  12.238  25.268  1.00 10.80 ? 137 GLN A C   1 
ATOM   1125 O  O   . GLN A 1 136 ? -4.884  11.300  24.537  1.00 7.75  ? 137 GLN A O   1 
ATOM   1126 C  CB  . GLN A 1 136 ? -5.398  14.411  24.506  1.00 10.71 ? 137 GLN A CB  1 
ATOM   1127 C  CG  . GLN A 1 136 ? -5.122  15.821  23.771  1.00 15.26 ? 137 GLN A CG  1 
ATOM   1128 C  CD  . GLN A 1 136 ? -4.213  16.696  24.654  1.00 15.62 ? 137 GLN A CD  1 
ATOM   1129 O  OE1 . GLN A 1 136 ? -4.200  16.541  25.858  1.00 20.90 ? 137 GLN A OE1 1 
ATOM   1130 N  NE2 . GLN A 1 136 ? -3.403  17.552  24.036  1.00 27.15 ? 137 GLN A NE2 1 
ATOM   1131 N  N   . PRO A 1 137 ? -4.539  12.141  26.595  1.00 10.37 ? 138 PRO A N   1 
ATOM   1132 C  CA  . PRO A 1 137 ? -4.750  10.785  27.228  1.00 11.88 ? 138 PRO A CA  1 
ATOM   1133 C  C   . PRO A 1 137 ? -6.197  10.292  27.090  1.00 10.95 ? 138 PRO A C   1 
ATOM   1134 O  O   . PRO A 1 137 ? -6.440  9.069   27.152  1.00 11.55 ? 138 PRO A O   1 
ATOM   1135 C  CB  . PRO A 1 137 ? -4.380  10.971  28.721  1.00 12.06 ? 138 PRO A CB  1 
ATOM   1136 C  CG  . PRO A 1 137 ? -4.231  12.448  28.918  1.00 17.21 ? 138 PRO A CG  1 
ATOM   1137 C  CD  . PRO A 1 137 ? -4.167  13.185  27.584  1.00 12.46 ? 138 PRO A CD  1 
ATOM   1138 N  N   . ASP A 1 138 ? -7.127  11.221  26.826  1.00 8.18  ? 139 ASP A N   1 
ATOM   1139 C  CA  . ASP A 1 138 ? -8.519  10.856  26.584  1.00 8.27  ? 139 ASP A CA  1 
ATOM   1140 C  C   . ASP A 1 138 ? -8.885  11.239  25.090  1.00 6.92  ? 139 ASP A C   1 
ATOM   1141 O  O   . ASP A 1 138 ? -10.058 11.618  24.806  1.00 8.78  ? 139 ASP A O   1 
ATOM   1142 C  CB  . ASP A 1 138 ? -9.504  11.560  27.557  1.00 8.85  ? 139 ASP A CB  1 
ATOM   1143 C  CG  . ASP A 1 138 ? -9.368  13.078  27.555  1.00 7.44  ? 139 ASP A CG  1 
ATOM   1144 O  OD1 . ASP A 1 138 ? -8.403  13.627  26.948  1.00 11.40 ? 139 ASP A OD1 1 
ATOM   1145 O  OD2 . ASP A 1 138 ? -10.252 13.670  28.248  1.00 12.98 ? 139 ASP A OD2 1 
ATOM   1146 N  N   . GLY A 1 139 ? -7.935  11.173  24.107  1.00 6.36  ? 140 GLY A N   1 
ATOM   1147 C  CA  . GLY A 1 139 ? -8.182  11.680  22.778  1.00 6.13  ? 140 GLY A CA  1 
ATOM   1148 C  C   . GLY A 1 139 ? -9.049  10.780  21.887  1.00 6.60  ? 140 GLY A C   1 
ATOM   1149 O  O   . GLY A 1 139 ? -9.785  11.274  21.052  1.00 5.94  ? 140 GLY A O   1 
ATOM   1150 N  N   . LEU A 1 140 ? -8.879  9.457   22.096  1.00 6.43  ? 141 LEU A N   1 
ATOM   1151 C  CA  . LEU A 1 140 ? -9.580  8.510   21.235  1.00 4.93  ? 141 LEU A CA  1 
ATOM   1152 C  C   . LEU A 1 140 ? -10.443 7.527   22.014  1.00 6.40  ? 141 LEU A C   1 
ATOM   1153 O  O   . LEU A 1 140 ? -10.151 7.257   23.149  1.00 6.96  ? 141 LEU A O   1 
ATOM   1154 C  CB  . LEU A 1 140 ? -8.530  7.703   20.442  1.00 5.79  ? 141 LEU A CB  1 
ATOM   1155 C  CG  . LEU A 1 140 ? -7.592  8.365   19.437  1.00 10.37 ? 141 LEU A CG  1 
ATOM   1156 C  CD1 . LEU A 1 140 ? -6.987  7.274   18.571  1.00 10.20 ? 141 LEU A CD1 1 
ATOM   1157 C  CD2 . LEU A 1 140 ? -8.284  9.422   18.603  1.00 13.32 ? 141 LEU A CD2 1 
ATOM   1158 N  N   . ALA A 1 141 ? -11.513 7.027   21.344  1.00 6.28  ? 142 ALA A N   1 
ATOM   1159 C  CA  . ALA A 1 141 ? -12.289 5.934   21.934  1.00 5.89  ? 142 ALA A CA  1 
ATOM   1160 C  C   . ALA A 1 141 ? -12.312 4.912   20.766  1.00 6.86  ? 142 ALA A C   1 
ATOM   1161 O  O   . ALA A 1 141 ? -12.676 5.253   19.641  1.00 8.02  ? 142 ALA A O   1 
ATOM   1162 C  CB  . ALA A 1 141 ? -13.681 6.399   22.307  1.00 6.58  ? 142 ALA A CB  1 
ATOM   1163 N  N   . VAL A 1 142 ? -11.772 3.702   21.046  1.00 6.49  ? 143 VAL A N   1 
ATOM   1164 C  CA  . VAL A 1 142 ? -11.823 2.698   20.002  1.00 6.35  ? 143 VAL A CA  1 
ATOM   1165 C  C   . VAL A 1 142 ? -12.777 1.612   20.469  1.00 6.26  ? 143 VAL A C   1 
ATOM   1166 O  O   . VAL A 1 142 ? -12.644 1.047   21.560  1.00 6.99  ? 143 VAL A O   1 
ATOM   1167 C  CB  . VAL A 1 142 ? -10.437 2.101   19.608  1.00 8.10  ? 143 VAL A CB  1 
ATOM   1168 C  CG1 . VAL A 1 142 ? -10.515 1.112   18.430  1.00 9.44  ? 143 VAL A CG1 1 
ATOM   1169 C  CG2 . VAL A 1 142 ? -9.483  3.242   19.247  1.00 6.70  ? 143 VAL A CG2 1 
ATOM   1170 N  N   . LEU A 1 143 ? -13.720 1.301   19.628  1.00 5.59  ? 144 LEU A N   1 
ATOM   1171 C  CA  . LEU A 1 143 ? -14.702 0.243   19.916  1.00 5.20  ? 144 LEU A CA  1 
ATOM   1172 C  C   . LEU A 1 143 ? -14.195 -0.986  19.215  1.00 4.96  ? 144 LEU A C   1 
ATOM   1173 O  O   . LEU A 1 143 ? -14.105 -0.990  17.976  1.00 5.80  ? 144 LEU A O   1 
ATOM   1174 C  CB  . LEU A 1 143 ? -16.087 0.705   19.439  1.00 7.12  ? 144 LEU A CB  1 
ATOM   1175 C  CG  . LEU A 1 143 ? -17.243 -0.262  19.451  1.00 5.63  ? 144 LEU A CG  1 
ATOM   1176 C  CD1 . LEU A 1 143 ? -17.508 -0.682  20.870  1.00 10.03 ? 144 LEU A CD1 1 
ATOM   1177 C  CD2 . LEU A 1 143 ? -18.514 0.322   18.783  1.00 7.75  ? 144 LEU A CD2 1 
ATOM   1178 N  N   . GLY A 1 144 ? -13.922 -2.054  20.020  1.00 5.61  ? 145 GLY A N   1 
ATOM   1179 C  CA  . GLY A 1 144 ? -13.349 -3.288  19.530  1.00 4.05  ? 145 GLY A CA  1 
ATOM   1180 C  C   . GLY A 1 144 ? -14.447 -4.382  19.555  1.00 4.29  ? 145 GLY A C   1 
ATOM   1181 O  O   . GLY A 1 144 ? -15.178 -4.491  20.503  1.00 5.43  ? 145 GLY A O   1 
ATOM   1182 N  N   . ILE A 1 145 ? -14.536 -5.111  18.456  1.00 6.16  ? 146 ILE A N   1 
ATOM   1183 C  CA  . ILE A 1 145 ? -15.631 -6.150  18.277  1.00 4.70  ? 146 ILE A CA  1 
ATOM   1184 C  C   . ILE A 1 145 ? -14.895 -7.384  17.720  1.00 6.29  ? 146 ILE A C   1 
ATOM   1185 O  O   . ILE A 1 145 ? -14.227 -7.309  16.691  1.00 6.72  ? 146 ILE A O   1 
ATOM   1186 C  CB  . ILE A 1 145 ? -16.648 -5.648  17.303  1.00 4.04  ? 146 ILE A CB  1 
ATOM   1187 C  CG1 . ILE A 1 145 ? -17.215 -4.351  17.815  1.00 5.52  ? 146 ILE A CG1 1 
ATOM   1188 C  CG2 . ILE A 1 145 ? -17.708 -6.769  17.074  1.00 5.91  ? 146 ILE A CG2 1 
ATOM   1189 C  CD1 . ILE A 1 145 ? -18.315 -3.809  16.810  1.00 7.26  ? 146 ILE A CD1 1 
ATOM   1190 N  N   . PHE A 1 146 ? -15.031 -8.489  18.427  1.00 7.31  ? 147 PHE A N   1 
ATOM   1191 C  CA  . PHE A 1 146 ? -14.368 -9.757  17.996  1.00 5.47  ? 147 PHE A CA  1 
ATOM   1192 C  C   . PHE A 1 146 ? -15.174 -10.363 16.812  1.00 7.91  ? 147 PHE A C   1 
ATOM   1193 O  O   . PHE A 1 146 ? -16.433 -10.270 16.810  1.00 8.96  ? 147 PHE A O   1 
ATOM   1194 C  CB  . PHE A 1 146 ? -14.416 -10.721 19.173  1.00 4.11  ? 147 PHE A CB  1 
ATOM   1195 C  CG  . PHE A 1 146 ? -13.585 -10.248 20.354  1.00 4.17  ? 147 PHE A CG  1 
ATOM   1196 C  CD1 . PHE A 1 146 ? -12.174 -10.120 20.158  1.00 6.78  ? 147 PHE A CD1 1 
ATOM   1197 C  CD2 . PHE A 1 146 ? -14.103 -10.060 21.604  1.00 7.94  ? 147 PHE A CD2 1 
ATOM   1198 C  CE1 . PHE A 1 146 ? -11.281 -9.662  21.193  1.00 4.84  ? 147 PHE A CE1 1 
ATOM   1199 C  CE2 . PHE A 1 146 ? -13.249 -9.626  22.689  1.00 8.56  ? 147 PHE A CE2 1 
ATOM   1200 C  CZ  . PHE A 1 146 ? -11.823 -9.508  22.445  1.00 6.18  ? 147 PHE A CZ  1 
ATOM   1201 N  N   . LEU A 1 147 ? -14.441 -11.041 15.914  1.00 7.07  ? 148 LEU A N   1 
ATOM   1202 C  CA  . LEU A 1 147 ? -15.027 -11.842 14.865  1.00 7.01  ? 148 LEU A CA  1 
ATOM   1203 C  C   . LEU A 1 147 ? -14.713 -13.309 15.134  1.00 9.19  ? 148 LEU A C   1 
ATOM   1204 O  O   . LEU A 1 147 ? -13.544 -13.642 15.360  1.00 8.48  ? 148 LEU A O   1 
ATOM   1205 C  CB  . LEU A 1 147 ? -14.440 -11.424 13.517  1.00 8.56  ? 148 LEU A CB  1 
ATOM   1206 C  CG  . LEU A 1 147 ? -15.056 -10.187 12.827  1.00 9.26  ? 148 LEU A CG  1 
ATOM   1207 C  CD1 . LEU A 1 147 ? -14.887 -8.944  13.751  1.00 9.73  ? 148 LEU A CD1 1 
ATOM   1208 C  CD2 . LEU A 1 147 ? -14.308 -10.031 11.534  1.00 12.37 ? 148 LEU A CD2 1 
ATOM   1209 N  N   . LYS A 1 148 ? -15.742 -14.154 15.036  1.00 8.46  ? 149 LYS A N   1 
ATOM   1210 C  CA  . LYS A 1 148 ? -15.505 -15.601 14.981  1.00 8.55  ? 149 LYS A CA  1 
ATOM   1211 C  C   . LYS A 1 148 ? -16.008 -16.102 13.620  1.00 9.34  ? 149 LYS A C   1 
ATOM   1212 O  O   . LYS A 1 148 ? -16.840 -15.461 12.951  1.00 9.79  ? 149 LYS A O   1 
ATOM   1213 C  CB  . LYS A 1 148 ? -16.283 -16.339 16.104  1.00 9.98  ? 149 LYS A CB  1 
ATOM   1214 C  CG  . LYS A 1 148 ? -17.829 -16.208 16.012  1.00 11.76 ? 149 LYS A CG  1 
ATOM   1215 C  CD  . LYS A 1 148 ? -18.367 -16.943 17.211  1.00 21.25 ? 149 LYS A CD  1 
ATOM   1216 C  CE  . LYS A 1 148 ? -19.767 -16.585 17.369  1.00 24.12 ? 149 LYS A CE  1 
ATOM   1217 N  NZ  . LYS A 1 148 ? -20.585 -17.772 17.822  1.00 32.66 ? 149 LYS A NZ  1 
ATOM   1218 N  N   . VAL A 1 149 ? -15.488 -17.258 13.227  1.00 8.71  ? 150 VAL A N   1 
ATOM   1219 C  CA  . VAL A 1 149 ? -15.943 -17.821 11.966  1.00 9.88  ? 150 VAL A CA  1 
ATOM   1220 C  C   . VAL A 1 149 ? -17.184 -18.759 12.171  1.00 9.55  ? 150 VAL A C   1 
ATOM   1221 O  O   . VAL A 1 149 ? -17.151 -19.734 12.950  1.00 11.29 ? 150 VAL A O   1 
ATOM   1222 C  CB  . VAL A 1 149 ? -14.796 -18.630 11.365  1.00 10.37 ? 150 VAL A CB  1 
ATOM   1223 C  CG1 . VAL A 1 149 ? -15.209 -19.393 10.090  1.00 10.37 ? 150 VAL A CG1 1 
ATOM   1224 C  CG2 . VAL A 1 149 ? -13.599 -17.628 10.999  1.00 11.19 ? 150 VAL A CG2 1 
ATOM   1225 N  N   . GLY A 1 150 ? -18.207 -18.500 11.382  1.00 9.68  ? 151 GLY A N   1 
ATOM   1226 C  CA  . GLY A 1 150 ? -19.409 -19.356 11.418  1.00 12.23 ? 151 GLY A CA  1 
ATOM   1227 C  C   . GLY A 1 150 ? -20.308 -18.862 10.294  1.00 10.01 ? 151 GLY A C   1 
ATOM   1228 O  O   . GLY A 1 150 ? -19.951 -18.940 9.150   1.00 10.48 ? 151 GLY A O   1 
ATOM   1229 N  N   A SER A 1 151 ? -21.503 -18.372 10.652  0.50 12.63 ? 152 SER A N   1 
ATOM   1230 N  N   B SER A 1 151 ? -21.492 -18.361 10.663  0.50 12.39 ? 152 SER A N   1 
ATOM   1231 C  CA  A SER A 1 151 ? -22.391 -17.803 9.607   0.50 13.20 ? 152 SER A CA  1 
ATOM   1232 C  CA  B SER A 1 151 ? -22.361 -17.762 9.631   0.50 12.72 ? 152 SER A CA  1 
ATOM   1233 C  C   A SER A 1 151 ? -21.842 -16.468 9.095   0.50 13.55 ? 152 SER A C   1 
ATOM   1234 C  C   B SER A 1 151 ? -21.701 -16.513 9.034   0.50 13.52 ? 152 SER A C   1 
ATOM   1235 O  O   A SER A 1 151 ? -21.170 -15.740 9.863   0.50 12.45 ? 152 SER A O   1 
ATOM   1236 O  O   B SER A 1 151 ? -20.824 -15.890 9.672   0.50 12.57 ? 152 SER A O   1 
ATOM   1237 C  CB  A SER A 1 151 ? -23.801 -17.590 10.137  0.50 15.25 ? 152 SER A CB  1 
ATOM   1238 C  CB  B SER A 1 151 ? -23.705 -17.374 10.222  0.50 14.40 ? 152 SER A CB  1 
ATOM   1239 O  OG  A SER A 1 151 ? -23.808 -16.698 11.248  0.50 17.71 ? 152 SER A OG  1 
ATOM   1240 O  OG  B SER A 1 151 ? -24.298 -18.470 10.910  0.50 14.64 ? 152 SER A OG  1 
ATOM   1241 N  N   . ALA A 1 152 ? -22.105 -16.158 7.810   1.00 12.24 ? 153 ALA A N   1 
ATOM   1242 C  CA  . ALA A 1 152 ? -21.691 -14.895 7.183   1.00 12.17 ? 153 ALA A CA  1 
ATOM   1243 C  C   . ALA A 1 152 ? -22.299 -13.679 7.898   1.00 9.88  ? 153 ALA A C   1 
ATOM   1244 O  O   . ALA A 1 152 ? -23.375 -13.748 8.437   1.00 11.88 ? 153 ALA A O   1 
ATOM   1245 C  CB  . ALA A 1 152 ? -22.064 -14.875 5.630   1.00 12.05 ? 153 ALA A CB  1 
ATOM   1246 N  N   . LYS A 1 153 ? -21.563 -12.580 7.836   1.00 11.87 ? 154 LYS A N   1 
ATOM   1247 C  CA  . LYS A 1 153 ? -22.083 -11.266 8.247   1.00 12.64 ? 154 LYS A CA  1 
ATOM   1248 C  C   . LYS A 1 153 ? -22.484 -10.472 6.988   1.00 10.47 ? 154 LYS A C   1 
ATOM   1249 O  O   . LYS A 1 153 ? -21.663 -10.039 6.209   1.00 11.03 ? 154 LYS A O   1 
ATOM   1250 C  CB  . LYS A 1 153 ? -21.007 -10.498 9.055   1.00 12.90 ? 154 LYS A CB  1 
ATOM   1251 C  CG  . LYS A 1 153 ? -21.570 -9.344  9.894   1.00 15.98 ? 154 LYS A CG  1 
ATOM   1252 C  CD  . LYS A 1 153 ? -22.496 -9.770  11.021  1.00 13.46 ? 154 LYS A CD  1 
ATOM   1253 C  CE  . LYS A 1 153 ? -22.814 -8.567  11.935  1.00 18.74 ? 154 LYS A CE  1 
ATOM   1254 N  NZ  . LYS A 1 153 ? -23.914 -8.854  12.879  1.00 22.81 ? 154 LYS A NZ  1 
ATOM   1255 N  N   . PRO A 1 154 ? -23.810 -10.438 6.679   1.00 14.42 ? 155 PRO A N   1 
ATOM   1256 C  CA  . PRO A 1 154 ? -24.274 -9.835  5.399   1.00 13.38 ? 155 PRO A CA  1 
ATOM   1257 C  C   . PRO A 1 154 ? -23.811 -8.421  5.331   1.00 13.42 ? 155 PRO A C   1 
ATOM   1258 O  O   . PRO A 1 154 ? -23.352 -8.005  4.268   1.00 13.54 ? 155 PRO A O   1 
ATOM   1259 C  CB  . PRO A 1 154 ? -25.822 -9.894  5.506   1.00 15.61 ? 155 PRO A CB  1 
ATOM   1260 C  CG  . PRO A 1 154 ? -26.118 -11.026 6.485   1.00 18.48 ? 155 PRO A CG  1 
ATOM   1261 C  CD  . PRO A 1 154 ? -24.933 -11.011 7.460   1.00 13.89 ? 155 PRO A CD  1 
ATOM   1262 N  N   . GLY A 1 155 ? -23.789 -7.730  6.469   1.00 14.18 ? 156 GLY A N   1 
ATOM   1263 C  CA  . GLY A 1 155 ? -23.314 -6.327  6.435   1.00 14.39 ? 156 GLY A CA  1 
ATOM   1264 C  C   . GLY A 1 155 ? -21.841 -6.098  6.086   1.00 15.60 ? 156 GLY A C   1 
ATOM   1265 O  O   . GLY A 1 155 ? -21.441 -4.939  5.854   1.00 15.87 ? 156 GLY A O   1 
ATOM   1266 N  N   . LEU A 1 156 ? -21.008 -7.154  6.173   1.00 11.96 ? 157 LEU A N   1 
ATOM   1267 C  CA  . LEU A 1 156 ? -19.636 -7.148  5.843   1.00 9.15  ? 157 LEU A CA  1 
ATOM   1268 C  C   . LEU A 1 156 ? -19.292 -7.324  4.362   1.00 10.62 ? 157 LEU A C   1 
ATOM   1269 O  O   . LEU A 1 156 ? -18.182 -7.027  3.863   1.00 11.05 ? 157 LEU A O   1 
ATOM   1270 C  CB  . LEU A 1 156 ? -18.863 -8.134  6.753   1.00 10.79 ? 157 LEU A CB  1 
ATOM   1271 C  CG  . LEU A 1 156 ? -17.347 -8.303  6.528   1.00 9.95  ? 157 LEU A CG  1 
ATOM   1272 C  CD1 . LEU A 1 156 ? -16.550 -6.933  6.842   1.00 13.61 ? 157 LEU A CD1 1 
ATOM   1273 C  CD2 . LEU A 1 156 ? -16.741 -9.437  7.430   1.00 10.22 ? 157 LEU A CD2 1 
ATOM   1274 N  N   . GLN A 1 157 ? -20.262 -7.908  3.617   1.00 11.85 ? 158 GLN A N   1 
ATOM   1275 C  CA  . GLN A 1 157 ? -19.947 -8.365  2.289   1.00 13.92 ? 158 GLN A CA  1 
ATOM   1276 C  C   . GLN A 1 157 ? -19.543 -7.229  1.342   1.00 11.39 ? 158 GLN A C   1 
ATOM   1277 O  O   . GLN A 1 157 ? -18.647 -7.440  0.570   1.00 12.67 ? 158 GLN A O   1 
ATOM   1278 C  CB  . GLN A 1 157 ? -21.075 -9.263  1.730   1.00 14.72 ? 158 GLN A CB  1 
ATOM   1279 C  CG  . GLN A 1 157 ? -20.676 -9.998  0.436   1.00 16.04 ? 158 GLN A CG  1 
ATOM   1280 C  CD  . GLN A 1 157 ? -19.550 -11.005 0.687   1.00 15.81 ? 158 GLN A CD  1 
ATOM   1281 O  OE1 . GLN A 1 157 ? -19.459 -11.579 1.781   1.00 17.77 ? 158 GLN A OE1 1 
ATOM   1282 N  NE2 . GLN A 1 157 ? -18.739 -11.225 -0.291  1.00 15.25 ? 158 GLN A NE2 1 
ATOM   1283 N  N   A LYS A 1 158 ? -20.152 -6.031  1.406   0.50 13.60 ? 159 LYS A N   1 
ATOM   1284 N  N   B LYS A 1 158 ? -20.148 -6.046  1.472   0.50 13.82 ? 159 LYS A N   1 
ATOM   1285 C  CA  A LYS A 1 158 ? -19.662 -4.965  0.512   0.50 13.31 ? 159 LYS A CA  1 
ATOM   1286 C  CA  B LYS A 1 158 ? -19.774 -4.888  0.647   0.50 13.55 ? 159 LYS A CA  1 
ATOM   1287 C  C   A LYS A 1 158 ? -18.145 -4.684  0.750   0.50 12.47 ? 159 LYS A C   1 
ATOM   1288 C  C   B LYS A 1 158 ? -18.262 -4.540  0.801   0.50 12.95 ? 159 LYS A C   1 
ATOM   1289 O  O   A LYS A 1 158 ? -17.392 -4.460  -0.184  0.50 13.78 ? 159 LYS A O   1 
ATOM   1290 O  O   B LYS A 1 158 ? -17.616 -4.148  -0.143  0.50 14.08 ? 159 LYS A O   1 
ATOM   1291 C  CB  A LYS A 1 158 ? -20.436 -3.673  0.691   0.50 12.53 ? 159 LYS A CB  1 
ATOM   1292 C  CB  B LYS A 1 158 ? -20.673 -3.678  0.930   0.50 13.41 ? 159 LYS A CB  1 
ATOM   1293 C  CG  A LYS A 1 158 ? -19.894 -2.446  -0.058  0.50 13.61 ? 159 LYS A CG  1 
ATOM   1294 C  CG  B LYS A 1 158 ? -22.064 -3.865  0.364   0.50 13.05 ? 159 LYS A CG  1 
ATOM   1295 C  CD  A LYS A 1 158 ? -19.852 -2.626  -1.582  0.00 23.57 ? 159 LYS A CD  1 
ATOM   1296 C  CD  B LYS A 1 158 ? -22.963 -2.686  0.635   0.00 20.83 ? 159 LYS A CD  1 
ATOM   1297 C  CE  A LYS A 1 158 ? -21.242 -2.814  -2.181  0.00 22.02 ? 159 LYS A CE  1 
ATOM   1298 C  CE  B LYS A 1 158 ? -24.399 -3.059  0.345   0.00 22.05 ? 159 LYS A CE  1 
ATOM   1299 N  NZ  A LYS A 1 158 ? -21.247 -2.547  -3.650  0.00 24.90 ? 159 LYS A NZ  1 
ATOM   1300 N  NZ  B LYS A 1 158 ? -25.182 -1.864  -0.046  0.00 22.84 ? 159 LYS A NZ  1 
ATOM   1301 N  N   . VAL A 1 159 ? -17.725 -4.715  2.026   1.00 13.10 ? 160 VAL A N   1 
ATOM   1302 C  CA  . VAL A 1 159 ? -16.290 -4.552  2.328   1.00 12.38 ? 160 VAL A CA  1 
ATOM   1303 C  C   . VAL A 1 159 ? -15.492 -5.706  1.640   1.00 11.89 ? 160 VAL A C   1 
ATOM   1304 O  O   . VAL A 1 159 ? -14.532 -5.452  0.907   1.00 11.11 ? 160 VAL A O   1 
ATOM   1305 C  CB  . VAL A 1 159 ? -16.036 -4.570  3.845   1.00 13.47 ? 160 VAL A CB  1 
ATOM   1306 C  CG1 . VAL A 1 159 ? -14.535 -4.591  4.171   1.00 12.50 ? 160 VAL A CG1 1 
ATOM   1307 C  CG2 . VAL A 1 159 ? -16.811 -3.422  4.598   1.00 13.70 ? 160 VAL A CG2 1 
ATOM   1308 N  N   . VAL A 1 160 ? -15.909 -6.961  1.870   1.00 11.53 ? 161 VAL A N   1 
ATOM   1309 C  CA  . VAL A 1 160 ? -15.196 -8.087  1.290   1.00 14.88 ? 161 VAL A CA  1 
ATOM   1310 C  C   . VAL A 1 160 ? -15.130 -7.996  -0.253  1.00 12.89 ? 161 VAL A C   1 
ATOM   1311 O  O   . VAL A 1 160 ? -14.124 -8.194  -0.843  1.00 13.57 ? 161 VAL A O   1 
ATOM   1312 C  CB  . VAL A 1 160 ? -15.903 -9.446  1.769   1.00 15.03 ? 161 VAL A CB  1 
ATOM   1313 C  CG1 . VAL A 1 160 ? -15.479 -10.634 0.893   1.00 18.37 ? 161 VAL A CG1 1 
ATOM   1314 C  CG2 . VAL A 1 160 ? -15.658 -9.604  3.306   1.00 15.03 ? 161 VAL A CG2 1 
ATOM   1315 N  N   . ASP A 1 161 ? -16.228 -7.603  -0.868  1.00 15.50 ? 162 ASP A N   1 
ATOM   1316 C  CA  . ASP A 1 161 ? -16.248 -7.574  -2.304  1.00 17.07 ? 162 ASP A CA  1 
ATOM   1317 C  C   . ASP A 1 161 ? -15.325 -6.500  -2.932  1.00 16.86 ? 162 ASP A C   1 
ATOM   1318 O  O   . ASP A 1 161 ? -14.867 -6.680  -4.053  1.00 20.56 ? 162 ASP A O   1 
ATOM   1319 C  CB  . ASP A 1 161 ? -17.658 -7.447  -2.792  1.00 18.22 ? 162 ASP A CB  1 
ATOM   1320 C  CG  . ASP A 1 161 ? -18.416 -8.786  -2.747  1.00 18.75 ? 162 ASP A CG  1 
ATOM   1321 O  OD1 . ASP A 1 161 ? -17.774 -9.882  -2.837  1.00 21.84 ? 162 ASP A OD1 1 
ATOM   1322 O  OD2 . ASP A 1 161 ? -19.643 -8.693  -2.587  1.00 22.65 ? 162 ASP A OD2 1 
ATOM   1323 N  N   . VAL A 1 162 ? -14.980 -5.408  -2.213  1.00 14.50 ? 163 VAL A N   1 
ATOM   1324 C  CA  . VAL A 1 162 ? -14.099 -4.410  -2.800  1.00 16.41 ? 163 VAL A CA  1 
ATOM   1325 C  C   . VAL A 1 162 ? -12.592 -4.677  -2.613  1.00 14.09 ? 163 VAL A C   1 
ATOM   1326 O  O   . VAL A 1 162 ? -11.725 -3.995  -3.160  1.00 12.91 ? 163 VAL A O   1 
ATOM   1327 C  CB  . VAL A 1 162 ? -14.569 -3.034  -2.300  1.00 17.77 ? 163 VAL A CB  1 
ATOM   1328 C  CG1 . VAL A 1 162 ? -14.022 -2.734  -0.935  1.00 19.09 ? 163 VAL A CG1 1 
ATOM   1329 C  CG2 . VAL A 1 162 ? -14.182 -1.916  -3.264  1.00 18.32 ? 163 VAL A CG2 1 
ATOM   1330 N  N   . LEU A 1 163 ? -12.220 -5.648  -1.730  1.00 13.19 ? 164 LEU A N   1 
ATOM   1331 C  CA  . LEU A 1 163 ? -10.799 -5.946  -1.458  1.00 13.54 ? 164 LEU A CA  1 
ATOM   1332 C  C   . LEU A 1 163 ? -9.894  -6.337  -2.664  1.00 14.04 ? 164 LEU A C   1 
ATOM   1333 O  O   . LEU A 1 163 ? -8.714  -6.001  -2.698  1.00 14.69 ? 164 LEU A O   1 
ATOM   1334 C  CB  . LEU A 1 163 ? -10.682 -6.982  -0.332  1.00 11.45 ? 164 LEU A CB  1 
ATOM   1335 C  CG  . LEU A 1 163 ? -11.311 -6.703  1.031   1.00 12.63 ? 164 LEU A CG  1 
ATOM   1336 C  CD1 . LEU A 1 163 ? -10.990 -7.916  1.967   1.00 15.52 ? 164 LEU A CD1 1 
ATOM   1337 C  CD2 . LEU A 1 163 ? -10.754 -5.358  1.568   1.00 12.56 ? 164 LEU A CD2 1 
ATOM   1338 N  N   . ASP A 1 164 ? -10.469 -7.038  -3.662  1.00 18.20 ? 165 ASP A N   1 
ATOM   1339 C  CA  . ASP A 1 164 ? -9.651  -7.414  -4.808  1.00 20.11 ? 165 ASP A CA  1 
ATOM   1340 C  C   . ASP A 1 164 ? -9.126  -6.107  -5.547  1.00 19.12 ? 165 ASP A C   1 
ATOM   1341 O  O   . ASP A 1 164 ? -7.990  -6.143  -6.120  1.00 20.60 ? 165 ASP A O   1 
ATOM   1342 C  CB  . ASP A 1 164 ? -10.497 -8.284  -5.717  1.00 20.79 ? 165 ASP A CB  1 
ATOM   1343 C  CG  . ASP A 1 164 ? -11.417 -7.484  -6.536  1.00 23.66 ? 165 ASP A CG  1 
ATOM   1344 O  OD1 . ASP A 1 164 ? -12.439 -7.001  -6.021  1.00 25.98 ? 165 ASP A OD1 1 
ATOM   1345 O  OD2 . ASP A 1 164 ? -11.059 -7.239  -7.729  1.00 28.16 ? 165 ASP A OD2 1 
ATOM   1346 N  N   . SER A 1 165 ? -9.889  -5.001  -5.392  1.00 18.57 ? 166 SER A N   1 
ATOM   1347 C  CA  . SER A 1 165 ? -9.559  -3.685  -5.940  1.00 19.00 ? 166 SER A CA  1 
ATOM   1348 C  C   . SER A 1 165 ? -8.444  -2.908  -5.176  1.00 19.76 ? 166 SER A C   1 
ATOM   1349 O  O   . SER A 1 165 ? -7.944  -1.881  -5.692  1.00 18.51 ? 166 SER A O   1 
ATOM   1350 C  CB  . SER A 1 165 ? -10.803 -2.817  -6.160  1.00 18.93 ? 166 SER A CB  1 
ATOM   1351 O  OG  . SER A 1 165 ? -11.241 -2.139  -5.031  1.00 20.52 ? 166 SER A OG  1 
ATOM   1352 N  N   . ILE A 1 166 ? -8.105  -3.353  -3.950  1.00 15.09 ? 167 ILE A N   1 
ATOM   1353 C  CA  . ILE A 1 166 ? -7.076  -2.716  -3.118  1.00 16.09 ? 167 ILE A CA  1 
ATOM   1354 C  C   . ILE A 1 166 ? -6.101  -3.765  -2.635  1.00 16.09 ? 167 ILE A C   1 
ATOM   1355 O  O   . ILE A 1 166 ? -5.626  -3.772  -1.474  1.00 16.02 ? 167 ILE A O   1 
ATOM   1356 C  CB  . ILE A 1 166 ? -7.696  -1.831  -1.931  1.00 15.10 ? 167 ILE A CB  1 
ATOM   1357 C  CG1 . ILE A 1 166 ? -8.686  -2.650  -1.120  1.00 12.79 ? 167 ILE A CG1 1 
ATOM   1358 C  CG2 . ILE A 1 166 ? -8.473  -0.627  -2.515  1.00 15.08 ? 167 ILE A CG2 1 
ATOM   1359 C  CD1 . ILE A 1 166 ? -8.796  -2.193  0.365   1.00 18.91 ? 167 ILE A CD1 1 
ATOM   1360 N  N   . LYS A 1 167 ? -5.775  -4.719  -3.536  1.00 17.44 ? 168 LYS A N   1 
ATOM   1361 C  CA  . LYS A 1 167 ? -4.930  -5.815  -3.080  1.00 17.80 ? 168 LYS A CA  1 
ATOM   1362 C  C   . LYS A 1 167 ? -3.600  -5.431  -2.386  1.00 16.16 ? 168 LYS A C   1 
ATOM   1363 O  O   . LYS A 1 167 ? -3.156  -6.109  -1.446  1.00 13.23 ? 168 LYS A O   1 
ATOM   1364 C  CB  . LYS A 1 167 ? -4.612  -6.836  -4.193  1.00 17.51 ? 168 LYS A CB  1 
ATOM   1365 C  CG  . LYS A 1 167 ? -3.632  -7.895  -3.721  1.00 20.64 ? 168 LYS A CG  1 
ATOM   1366 C  CD  . LYS A 1 167 ? -3.011  -8.709  -4.895  1.00 25.10 ? 168 LYS A CD  1 
ATOM   1367 C  CE  . LYS A 1 167 ? -3.586  -10.085 -4.919  1.00 32.33 ? 168 LYS A CE  1 
ATOM   1368 N  NZ  . LYS A 1 167 ? -3.286  -10.807 -3.619  1.00 35.56 ? 168 LYS A NZ  1 
ATOM   1369 N  N   . THR A 1 168 ? -2.928  -4.381  -2.900  1.00 13.46 ? 169 THR A N   1 
ATOM   1370 C  CA  . THR A 1 168 ? -1.589  -4.109  -2.547  1.00 13.75 ? 169 THR A CA  1 
ATOM   1371 C  C   . THR A 1 168 ? -1.437  -2.740  -1.871  1.00 13.56 ? 169 THR A C   1 
ATOM   1372 O  O   . THR A 1 168 ? -2.280  -1.879  -2.036  1.00 15.69 ? 169 THR A O   1 
ATOM   1373 C  CB  . THR A 1 168 ? -0.652  -4.161  -3.800  1.00 16.37 ? 169 THR A CB  1 
ATOM   1374 O  OG1 . THR A 1 168 ? -1.268  -3.351  -4.846  1.00 16.51 ? 169 THR A OG1 1 
ATOM   1375 C  CG2 . THR A 1 168 ? -0.459  -5.656  -4.196  1.00 19.08 ? 169 THR A CG2 1 
ATOM   1376 N  N   A LYS A 1 169 ? -0.358  -2.603  -1.113  0.50 15.06 ? 170 LYS A N   1 
ATOM   1377 N  N   B LYS A 1 169 ? -0.384  -2.602  -1.096  0.50 14.71 ? 170 LYS A N   1 
ATOM   1378 C  CA  A LYS A 1 169 ? -0.004  -1.404  -0.378  0.50 16.28 ? 170 LYS A CA  1 
ATOM   1379 C  CA  B LYS A 1 169 ? -0.135  -1.434  -0.296  0.50 15.92 ? 170 LYS A CA  1 
ATOM   1380 C  C   A LYS A 1 169 ? -0.288  -0.117  -1.163  0.50 16.48 ? 170 LYS A C   1 
ATOM   1381 C  C   B LYS A 1 169 ? -0.240  -0.138  -1.094  0.50 16.21 ? 170 LYS A C   1 
ATOM   1382 O  O   A LYS A 1 169 ? 0.037   -0.029  -2.353  0.50 17.45 ? 170 LYS A O   1 
ATOM   1383 O  O   B LYS A 1 169 ? 0.280   -0.075  -2.219  0.50 17.59 ? 170 LYS A O   1 
ATOM   1384 C  CB  A LYS A 1 169 ? 1.452   -1.476  0.050   0.50 17.09 ? 170 LYS A CB  1 
ATOM   1385 C  CB  B LYS A 1 169 ? 1.226   -1.580  0.326   0.50 15.83 ? 170 LYS A CB  1 
ATOM   1386 C  CG  A LYS A 1 169 ? 1.941   -0.247  0.882   0.50 16.45 ? 170 LYS A CG  1 
ATOM   1387 C  CG  B LYS A 1 169 ? 1.718   -0.348  1.083   0.50 15.16 ? 170 LYS A CG  1 
ATOM   1388 C  CD  A LYS A 1 169 ? 3.083   -0.596  1.809   0.50 19.68 ? 170 LYS A CD  1 
ATOM   1389 C  CD  B LYS A 1 169 ? 3.028   -0.621  1.736   0.50 16.47 ? 170 LYS A CD  1 
ATOM   1390 C  CE  A LYS A 1 169 ? 3.580   0.612   2.623   0.50 19.92 ? 170 LYS A CE  1 
ATOM   1391 C  CE  B LYS A 1 169 ? 4.062   -1.122  0.735   0.50 15.84 ? 170 LYS A CE  1 
ATOM   1392 N  NZ  A LYS A 1 169 ? 4.821   1.259   2.017   0.50 24.71 ? 170 LYS A NZ  1 
ATOM   1393 N  NZ  B LYS A 1 169 ? 5.386   -1.326  1.406   0.50 18.88 ? 170 LYS A NZ  1 
ATOM   1394 N  N   . GLY A 1 170 ? -0.924  0.851   -0.520  1.00 17.51 ? 171 GLY A N   1 
ATOM   1395 C  CA  . GLY A 1 170 ? -1.238  2.177   -1.224  1.00 18.15 ? 171 GLY A CA  1 
ATOM   1396 C  C   . GLY A 1 170 ? -2.363  2.263   -2.256  1.00 19.06 ? 171 GLY A C   1 
ATOM   1397 O  O   . GLY A 1 170 ? -2.739  3.395   -2.758  1.00 19.58 ? 171 GLY A O   1 
ATOM   1398 N  N   . LYS A 1 171 ? -2.993  1.123   -2.586  1.00 15.75 ? 172 LYS A N   1 
ATOM   1399 C  CA  . LYS A 1 171 ? -4.250  1.180   -3.267  1.00 17.01 ? 172 LYS A CA  1 
ATOM   1400 C  C   . LYS A 1 171 ? -5.492  1.684   -2.501  1.00 17.37 ? 172 LYS A C   1 
ATOM   1401 O  O   . LYS A 1 171 ? -5.756  1.261   -1.343  1.00 17.99 ? 172 LYS A O   1 
ATOM   1402 C  CB  . LYS A 1 171 ? -4.543  -0.176  -3.905  1.00 16.62 ? 172 LYS A CB  1 
ATOM   1403 C  CG  . LYS A 1 171 ? -3.513  -0.507  -5.007  1.00 19.14 ? 172 LYS A CG  1 
ATOM   1404 C  CD  . LYS A 1 171 ? -4.080  -1.600  -6.055  1.00 20.54 ? 172 LYS A CD  1 
ATOM   1405 C  CE  . LYS A 1 171 ? -5.267  -1.050  -6.928  1.00 24.99 ? 172 LYS A CE  1 
ATOM   1406 N  NZ  . LYS A 1 171 ? -5.842  -2.088  -7.933  1.00 23.33 ? 172 LYS A NZ  1 
ATOM   1407 N  N   . SER A 1 172 ? -6.300  2.517   -3.149  1.00 16.82 ? 173 SER A N   1 
ATOM   1408 C  CA  . SER A 1 172 ? -7.512  2.975   -2.556  1.00 17.79 ? 173 SER A CA  1 
ATOM   1409 C  C   . SER A 1 172 ? -8.655  2.889   -3.539  1.00 17.86 ? 173 SER A C   1 
ATOM   1410 O  O   . SER A 1 172 ? -8.436  2.761   -4.789  1.00 20.26 ? 173 SER A O   1 
ATOM   1411 C  CB  . SER A 1 172 ? -7.369  4.403   -2.005  1.00 18.98 ? 173 SER A CB  1 
ATOM   1412 O  OG  . SER A 1 172 ? -7.102  5.309   -3.036  1.00 20.61 ? 173 SER A OG  1 
ATOM   1413 N  N   . ALA A 1 173 ? -9.858  2.979   -3.024  1.00 18.79 ? 174 ALA A N   1 
ATOM   1414 C  CA  . ALA A 1 173 ? -11.045 2.956   -3.846  1.00 19.10 ? 174 ALA A CA  1 
ATOM   1415 C  C   . ALA A 1 173 ? -12.155 3.711   -3.166  1.00 20.71 ? 174 ALA A C   1 
ATOM   1416 O  O   . ALA A 1 173 ? -12.265 3.727   -1.904  1.00 17.46 ? 174 ALA A O   1 
ATOM   1417 C  CB  . ALA A 1 173 ? -11.459 1.575   -4.132  1.00 19.19 ? 174 ALA A CB  1 
ATOM   1418 N  N   . ASP A 1 174 ? -13.004 4.315   -3.995  1.00 20.23 ? 175 ASP A N   1 
ATOM   1419 C  CA  . ASP A 1 174 ? -14.249 4.945   -3.519  1.00 22.27 ? 175 ASP A CA  1 
ATOM   1420 C  C   . ASP A 1 174 ? -15.045 3.946   -2.754  1.00 21.16 ? 175 ASP A C   1 
ATOM   1421 O  O   . ASP A 1 174 ? -15.132 2.795   -3.154  1.00 21.53 ? 175 ASP A O   1 
ATOM   1422 C  CB  . ASP A 1 174 ? -15.102 5.496   -4.688  1.00 22.13 ? 175 ASP A CB  1 
ATOM   1423 C  CG  . ASP A 1 174 ? -14.322 6.506   -5.494  1.00 29.72 ? 175 ASP A CG  1 
ATOM   1424 O  OD1 . ASP A 1 174 ? -13.504 7.220   -4.880  1.00 33.69 ? 175 ASP A OD1 1 
ATOM   1425 O  OD2 . ASP A 1 174 ? -14.488 6.598   -6.748  1.00 37.52 ? 175 ASP A OD2 1 
ATOM   1426 N  N   . PHE A 1 175 ? -15.584 4.393   -1.627  1.00 18.53 ? 176 PHE A N   1 
ATOM   1427 C  CA  . PHE A 1 175 ? -16.350 3.484   -0.749  1.00 18.39 ? 176 PHE A CA  1 
ATOM   1428 C  C   . PHE A 1 175 ? -17.400 4.258   0.010   1.00 18.53 ? 176 PHE A C   1 
ATOM   1429 O  O   . PHE A 1 175 ? -17.247 4.590   1.184   1.00 18.36 ? 176 PHE A O   1 
ATOM   1430 C  CB  . PHE A 1 175 ? -15.386 2.659   0.145   1.00 17.01 ? 176 PHE A CB  1 
ATOM   1431 C  CG  . PHE A 1 175 ? -15.999 1.421   0.676   1.00 17.15 ? 176 PHE A CG  1 
ATOM   1432 C  CD1 . PHE A 1 175 ? -16.317 0.334   -0.189  1.00 15.71 ? 176 PHE A CD1 1 
ATOM   1433 C  CD2 . PHE A 1 175 ? -16.261 1.301   2.043   1.00 18.67 ? 176 PHE A CD2 1 
ATOM   1434 C  CE1 . PHE A 1 175 ? -16.923 -0.833  0.368   1.00 19.43 ? 176 PHE A CE1 1 
ATOM   1435 C  CE2 . PHE A 1 175 ? -16.862 0.160   2.605   1.00 18.87 ? 176 PHE A CE2 1 
ATOM   1436 C  CZ  . PHE A 1 175 ? -17.204 -0.914  1.763   1.00 18.59 ? 176 PHE A CZ  1 
ATOM   1437 N  N   . THR A 1 176 ? -18.444 4.655   -0.706  1.00 14.84 ? 177 THR A N   1 
ATOM   1438 C  CA  . THR A 1 176 ? -19.502 5.472   -0.138  1.00 15.98 ? 177 THR A CA  1 
ATOM   1439 C  C   . THR A 1 176 ? -20.686 4.644   0.315   1.00 14.44 ? 177 THR A C   1 
ATOM   1440 O  O   . THR A 1 176 ? -20.866 3.508   -0.183  1.00 14.63 ? 177 THR A O   1 
ATOM   1441 C  CB  . THR A 1 176 ? -19.917 6.542   -1.218  1.00 17.41 ? 177 THR A CB  1 
ATOM   1442 O  OG1 . THR A 1 176 ? -20.442 5.875   -2.365  1.00 18.54 ? 177 THR A OG1 1 
ATOM   1443 C  CG2 . THR A 1 176 ? -18.738 7.200   -1.635  1.00 20.06 ? 177 THR A CG2 1 
ATOM   1444 N  N   . ASN A 1 177 ? -21.518 5.216   1.175   1.00 13.26 ? 178 ASN A N   1 
ATOM   1445 C  CA  . ASN A 1 177 ? -22.807 4.698   1.571   1.00 14.21 ? 178 ASN A CA  1 
ATOM   1446 C  C   . ASN A 1 177 ? -22.671 3.331   2.324   1.00 15.38 ? 178 ASN A C   1 
ATOM   1447 O  O   . ASN A 1 177 ? -23.656 2.650   2.506   1.00 17.70 ? 178 ASN A O   1 
ATOM   1448 C  CB  . ASN A 1 177 ? -23.735 4.567   0.351   1.00 13.17 ? 178 ASN A CB  1 
ATOM   1449 C  CG  . ASN A 1 177 ? -23.974 5.981   -0.301  1.00 16.03 ? 178 ASN A CG  1 
ATOM   1450 O  OD1 . ASN A 1 177 ? -24.648 6.821   0.292   1.00 18.46 ? 178 ASN A OD1 1 
ATOM   1451 N  ND2 . ASN A 1 177 ? -23.308 6.237   -1.383  1.00 14.42 ? 178 ASN A ND2 1 
ATOM   1452 N  N   . PHE A 1 178 ? -21.477 3.111   2.873   1.00 12.62 ? 179 PHE A N   1 
ATOM   1453 C  CA  . PHE A 1 178 ? -21.277 1.880   3.691   1.00 13.45 ? 179 PHE A CA  1 
ATOM   1454 C  C   . PHE A 1 178 ? -21.802 2.157   5.067   1.00 13.55 ? 179 PHE A C   1 
ATOM   1455 O  O   . PHE A 1 178 ? -21.333 3.109   5.718   1.00 13.95 ? 179 PHE A O   1 
ATOM   1456 C  CB  . PHE A 1 178 ? -19.861 1.425   3.785   1.00 13.51 ? 179 PHE A CB  1 
ATOM   1457 C  CG  . PHE A 1 178 ? -19.753 0.187   4.604   1.00 11.38 ? 179 PHE A CG  1 
ATOM   1458 C  CD1 . PHE A 1 178 ? -20.203 -1.028  4.086   1.00 16.33 ? 179 PHE A CD1 1 
ATOM   1459 C  CD2 . PHE A 1 178 ? -19.305 0.277   5.921   1.00 11.25 ? 179 PHE A CD2 1 
ATOM   1460 C  CE1 . PHE A 1 178 ? -20.211 -2.166  4.878   1.00 13.78 ? 179 PHE A CE1 1 
ATOM   1461 C  CE2 . PHE A 1 178 ? -19.318 -0.881  6.730   1.00 11.57 ? 179 PHE A CE2 1 
ATOM   1462 C  CZ  . PHE A 1 178 ? -19.757 -2.078  6.208   1.00 13.91 ? 179 PHE A CZ  1 
ATOM   1463 N  N   . ASP A 1 179 ? -22.681 1.287   5.570   1.00 15.20 ? 180 ASP A N   1 
ATOM   1464 C  CA  . ASP A 1 179 ? -23.324 1.536   6.821   1.00 13.20 ? 180 ASP A CA  1 
ATOM   1465 C  C   . ASP A 1 179 ? -22.677 0.710   7.944   1.00 11.20 ? 180 ASP A C   1 
ATOM   1466 O  O   . ASP A 1 179 ? -22.903 -0.517  8.001   1.00 10.35 ? 180 ASP A O   1 
ATOM   1467 C  CB  . ASP A 1 179 ? -24.808 1.134   6.752   1.00 16.73 ? 180 ASP A CB  1 
ATOM   1468 C  CG  . ASP A 1 179 ? -25.593 1.576   7.990   1.00 18.19 ? 180 ASP A CG  1 
ATOM   1469 O  OD1 . ASP A 1 179 ? -25.008 1.799   9.115   1.00 12.63 ? 180 ASP A OD1 1 
ATOM   1470 O  OD2 . ASP A 1 179 ? -26.846 1.788   7.808   1.00 20.48 ? 180 ASP A OD2 1 
ATOM   1471 N  N   . PRO A 1 180 ? -21.895 1.333   8.858   1.00 10.34 ? 181 PRO A N   1 
ATOM   1472 C  CA  . PRO A 1 180 ? -21.213 0.470   9.856   1.00 11.58 ? 181 PRO A CA  1 
ATOM   1473 C  C   . PRO A 1 180 ? -22.108 -0.220  10.909  1.00 11.64 ? 181 PRO A C   1 
ATOM   1474 O  O   . PRO A 1 180 ? -21.624 -1.147  11.630  1.00 9.28  ? 181 PRO A O   1 
ATOM   1475 C  CB  . PRO A 1 180 ? -20.173 1.412   10.458  1.00 12.63 ? 181 PRO A CB  1 
ATOM   1476 C  CG  . PRO A 1 180 ? -20.846 2.748   10.488  1.00 13.19 ? 181 PRO A CG  1 
ATOM   1477 C  CD  . PRO A 1 180 ? -21.507 2.734   9.036   1.00 12.44 ? 181 PRO A CD  1 
ATOM   1478 N  N   . ARG A 1 181 ? -23.407 0.161   10.959  1.00 10.50 ? 182 ARG A N   1 
ATOM   1479 C  CA  . ARG A 1 181 ? -24.379 -0.505  11.871  1.00 11.00 ? 182 ARG A CA  1 
ATOM   1480 C  C   . ARG A 1 181 ? -24.489 -1.996  11.517  1.00 11.07 ? 182 ARG A C   1 
ATOM   1481 O  O   . ARG A 1 181 ? -24.846 -2.776  12.388  1.00 13.42 ? 182 ARG A O   1 
ATOM   1482 C  CB  . ARG A 1 181 ? -25.765 0.173   11.786  1.00 10.70 ? 182 ARG A CB  1 
ATOM   1483 C  CG  . ARG A 1 181 ? -25.658 1.646   12.300  1.00 12.69 ? 182 ARG A CG  1 
ATOM   1484 C  CD  . ARG A 1 181 ? -26.978 2.401   12.216  1.00 13.52 ? 182 ARG A CD  1 
ATOM   1485 N  NE  . ARG A 1 181 ? -27.371 2.459   10.831  1.00 16.71 ? 182 ARG A NE  1 
ATOM   1486 C  CZ  . ARG A 1 181 ? -28.475 3.095   10.446  1.00 21.97 ? 182 ARG A CZ  1 
ATOM   1487 N  NH1 . ARG A 1 181 ? -29.215 3.654   11.370  1.00 19.75 ? 182 ARG A NH1 1 
ATOM   1488 N  NH2 . ARG A 1 181 ? -28.835 3.143   9.168   1.00 22.78 ? 182 ARG A NH2 1 
ATOM   1489 N  N   . GLY A 1 182 ? -24.208 -2.334  10.254  1.00 11.05 ? 183 GLY A N   1 
ATOM   1490 C  CA  . GLY A 1 182 ? -24.300 -3.765  9.815   1.00 11.04 ? 183 GLY A CA  1 
ATOM   1491 C  C   . GLY A 1 182 ? -23.197 -4.627  10.430  1.00 13.92 ? 183 GLY A C   1 
ATOM   1492 O  O   . GLY A 1 182 ? -23.189 -5.855  10.200  1.00 15.18 ? 183 GLY A O   1 
ATOM   1493 N  N   . LEU A 1 183 ? -22.204 -3.988  11.074  1.00 11.14 ? 184 LEU A N   1 
ATOM   1494 C  CA  . LEU A 1 183 ? -21.055 -4.754  11.645  1.00 11.86 ? 184 LEU A CA  1 
ATOM   1495 C  C   . LEU A 1 183 ? -21.197 -4.964  13.128  1.00 12.43 ? 184 LEU A C   1 
ATOM   1496 O  O   . LEU A 1 183 ? -20.260 -5.525  13.740  1.00 14.25 ? 184 LEU A O   1 
ATOM   1497 C  CB  . LEU A 1 183 ? -19.717 -4.023  11.412  1.00 11.69 ? 184 LEU A CB  1 
ATOM   1498 C  CG  . LEU A 1 183 ? -19.370 -3.859  9.905   1.00 12.55 ? 184 LEU A CG  1 
ATOM   1499 C  CD1 . LEU A 1 183 ? -18.102 -3.142  9.651   1.00 13.37 ? 184 LEU A CD1 1 
ATOM   1500 C  CD2 . LEU A 1 183 ? -19.531 -5.182  9.125   1.00 17.39 ? 184 LEU A CD2 1 
ATOM   1501 N  N   . LEU A 1 184 ? -22.293 -4.514  13.765  1.00 10.90 ? 185 LEU A N   1 
ATOM   1502 C  CA  . LEU A 1 184 ? -22.419 -4.525  15.252  1.00 9.42  ? 185 LEU A CA  1 
ATOM   1503 C  C   . LEU A 1 184 ? -23.161 -5.820  15.708  1.00 12.33 ? 185 LEU A C   1 
ATOM   1504 O  O   . LEU A 1 184 ? -24.189 -6.227  15.101  1.00 16.29 ? 185 LEU A O   1 
ATOM   1505 C  CB  . LEU A 1 184 ? -23.228 -3.291  15.804  1.00 10.30 ? 185 LEU A CB  1 
ATOM   1506 C  CG  . LEU A 1 184 ? -22.632 -1.933  15.486  1.00 8.48  ? 185 LEU A CG  1 
ATOM   1507 C  CD1 . LEU A 1 184 ? -23.550 -0.686  15.849  1.00 10.94 ? 185 LEU A CD1 1 
ATOM   1508 C  CD2 . LEU A 1 184 ? -21.202 -1.865  15.999  1.00 10.79 ? 185 LEU A CD2 1 
ATOM   1509 N  N   . PRO A 1 185 ? -22.747 -6.387  16.825  1.00 12.65 ? 186 PRO A N   1 
ATOM   1510 C  CA  . PRO A 1 185 ? -23.526 -7.498  17.334  1.00 11.00 ? 186 PRO A CA  1 
ATOM   1511 C  C   . PRO A 1 185 ? -24.822 -6.963  18.001  1.00 11.12 ? 186 PRO A C   1 
ATOM   1512 O  O   . PRO A 1 185 ? -24.997 -5.709  18.148  1.00 13.23 ? 186 PRO A O   1 
ATOM   1513 C  CB  . PRO A 1 185 ? -22.564 -8.095  18.409  1.00 12.85 ? 186 PRO A CB  1 
ATOM   1514 C  CG  . PRO A 1 185 ? -21.880 -6.866  18.991  1.00 8.73  ? 186 PRO A CG  1 
ATOM   1515 C  CD  . PRO A 1 185 ? -21.633 -5.975  17.730  1.00 10.63 ? 186 PRO A CD  1 
ATOM   1516 N  N   A GLU A 1 186 ? -25.680 -7.886  18.457  0.50 11.68 ? 187 GLU A N   1 
ATOM   1517 N  N   B GLU A 1 186 ? -25.698 -7.855  18.498  0.50 12.17 ? 187 GLU A N   1 
ATOM   1518 C  CA  A GLU A 1 186 ? -26.909 -7.506  19.091  0.50 11.69 ? 187 GLU A CA  1 
ATOM   1519 C  CA  B GLU A 1 186 ? -26.945 -7.428  19.136  0.50 12.89 ? 187 GLU A CA  1 
ATOM   1520 C  C   A GLU A 1 186 ? -26.671 -6.719  20.390  0.50 11.79 ? 187 GLU A C   1 
ATOM   1521 C  C   B GLU A 1 186 ? -26.741 -6.733  20.487  0.50 12.29 ? 187 GLU A C   1 
ATOM   1522 O  O   A GLU A 1 186 ? -27.252 -5.635  20.558  0.50 12.63 ? 187 GLU A O   1 
ATOM   1523 O  O   B GLU A 1 186 ? -27.425 -5.757  20.832  0.50 12.21 ? 187 GLU A O   1 
ATOM   1524 C  CB  A GLU A 1 186 ? -27.766 -8.785  19.374  0.50 11.14 ? 187 GLU A CB  1 
ATOM   1525 C  CB  B GLU A 1 186 ? -27.867 -8.675  19.332  0.50 12.69 ? 187 GLU A CB  1 
ATOM   1526 C  CG  A GLU A 1 186 ? -28.884 -8.536  20.364  0.50 12.84 ? 187 GLU A CG  1 
ATOM   1527 C  CG  B GLU A 1 186 ? -28.065 -9.446  18.057  0.50 14.92 ? 187 GLU A CG  1 
ATOM   1528 C  CD  A GLU A 1 186 ? -29.536 -9.834  20.920  0.50 13.12 ? 187 GLU A CD  1 
ATOM   1529 C  CD  B GLU A 1 186 ? -29.063 -10.599 18.165  0.50 17.61 ? 187 GLU A CD  1 
ATOM   1530 O  OE1 A GLU A 1 186 ? -29.410 -10.868 20.257  0.50 10.73 ? 187 GLU A OE1 1 
ATOM   1531 O  OE1 B GLU A 1 186 ? -29.419 -10.941 19.293  0.50 15.00 ? 187 GLU A OE1 1 
ATOM   1532 O  OE2 A GLU A 1 186 ? -30.092 -9.821  22.058  0.50 12.47 ? 187 GLU A OE2 1 
ATOM   1533 O  OE2 B GLU A 1 186 ? -29.456 -11.166 17.110  0.50 25.19 ? 187 GLU A OE2 1 
ATOM   1534 N  N   . SER A 1 187 ? -25.806 -7.212  21.298  1.00 11.34 ? 188 SER A N   1 
ATOM   1535 C  CA  . SER A 1 187 ? -25.652 -6.646  22.630  1.00 11.32 ? 188 SER A CA  1 
ATOM   1536 C  C   . SER A 1 187 ? -24.492 -5.625  22.610  1.00 10.79 ? 188 SER A C   1 
ATOM   1537 O  O   . SER A 1 187 ? -23.473 -5.930  21.978  1.00 12.73 ? 188 SER A O   1 
ATOM   1538 C  CB  . SER A 1 187 ? -25.303 -7.704  23.696  1.00 13.01 ? 188 SER A CB  1 
ATOM   1539 O  OG  . SER A 1 187 ? -25.070 -7.103  24.956  1.00 12.44 ? 188 SER A OG  1 
ATOM   1540 N  N   . LEU A 1 188 ? -24.674 -4.518  23.311  1.00 11.35 ? 189 LEU A N   1 
ATOM   1541 C  CA  . LEU A 1 188 ? -23.557 -3.546  23.567  1.00 12.35 ? 189 LEU A CA  1 
ATOM   1542 C  C   . LEU A 1 188 ? -22.927 -3.670  24.936  1.00 11.26 ? 189 LEU A C   1 
ATOM   1543 O  O   . LEU A 1 188 ? -22.236 -2.719  25.392  1.00 12.57 ? 189 LEU A O   1 
ATOM   1544 C  CB  . LEU A 1 188 ? -24.025 -2.095  23.282  1.00 11.74 ? 189 LEU A CB  1 
ATOM   1545 C  CG  . LEU A 1 188 ? -24.506 -1.829  21.861  1.00 12.48 ? 189 LEU A CG  1 
ATOM   1546 C  CD1 . LEU A 1 188 ? -25.002 -0.368  21.844  1.00 17.03 ? 189 LEU A CD1 1 
ATOM   1547 C  CD2 . LEU A 1 188 ? -23.367 -2.015  20.803  1.00 13.09 ? 189 LEU A CD2 1 
ATOM   1548 N  N   . ASP A 1 189 ? -23.100 -4.827  25.609  1.00 10.80 ? 190 ASP A N   1 
ATOM   1549 C  CA  . ASP A 1 189 ? -22.341 -5.125  26.853  1.00 10.96 ? 190 ASP A CA  1 
ATOM   1550 C  C   . ASP A 1 189 ? -20.821 -5.051  26.479  1.00 10.07 ? 190 ASP A C   1 
ATOM   1551 O  O   . ASP A 1 189 ? -20.389 -5.475  25.383  1.00 10.05 ? 190 ASP A O   1 
ATOM   1552 C  CB  . ASP A 1 189 ? -22.664 -6.492  27.394  1.00 11.95 ? 190 ASP A CB  1 
ATOM   1553 C  CG  . ASP A 1 189 ? -24.072 -6.564  28.071  1.00 16.05 ? 190 ASP A CG  1 
ATOM   1554 O  OD1 . ASP A 1 189 ? -24.657 -5.517  28.369  1.00 20.67 ? 190 ASP A OD1 1 
ATOM   1555 O  OD2 . ASP A 1 189 ? -24.528 -7.697  28.242  1.00 24.04 ? 190 ASP A OD2 1 
ATOM   1556 N  N   . TYR A 1 190 ? -20.066 -4.402  27.368  1.00 9.07  ? 191 TYR A N   1 
ATOM   1557 C  CA  . TYR A 1 190 ? -18.639 -4.157  27.031  1.00 8.63  ? 191 TYR A CA  1 
ATOM   1558 C  C   . TYR A 1 190 ? -17.710 -4.233  28.299  1.00 8.51  ? 191 TYR A C   1 
ATOM   1559 O  O   . TYR A 1 190 ? -18.160 -4.098  29.489  1.00 8.17  ? 191 TYR A O   1 
ATOM   1560 C  CB  . TYR A 1 190 ? -18.470 -2.773  26.355  1.00 8.82  ? 191 TYR A CB  1 
ATOM   1561 C  CG  . TYR A 1 190 ? -18.877 -1.630  27.263  1.00 7.39  ? 191 TYR A CG  1 
ATOM   1562 C  CD1 . TYR A 1 190 ? -17.932 -1.022  28.172  1.00 8.31  ? 191 TYR A CD1 1 
ATOM   1563 C  CD2 . TYR A 1 190 ? -20.185 -1.130  27.212  1.00 10.09 ? 191 TYR A CD2 1 
ATOM   1564 C  CE1 . TYR A 1 190 ? -18.378 0.037   29.036  1.00 9.89  ? 191 TYR A CE1 1 
ATOM   1565 C  CE2 . TYR A 1 190 ? -20.634 -0.065  28.061  1.00 11.32 ? 191 TYR A CE2 1 
ATOM   1566 C  CZ  . TYR A 1 190 ? -19.703 0.532   28.980  1.00 11.46 ? 191 TYR A CZ  1 
ATOM   1567 O  OH  . TYR A 1 190 ? -20.088 1.546   29.819  1.00 12.33 ? 191 TYR A OH  1 
ATOM   1568 N  N   . TRP A 1 191 ? -16.406 -4.405  28.032  1.00 6.74  ? 192 TRP A N   1 
ATOM   1569 C  CA  . TRP A 1 191 ? -15.341 -4.151  29.039  1.00 5.19  ? 192 TRP A CA  1 
ATOM   1570 C  C   . TRP A 1 191 ? -14.615 -2.860  28.554  1.00 5.85  ? 192 TRP A C   1 
ATOM   1571 O  O   . TRP A 1 191 ? -14.665 -2.460  27.405  1.00 7.11  ? 192 TRP A O   1 
ATOM   1572 C  CB  . TRP A 1 191 ? -14.289 -5.238  28.910  1.00 7.70  ? 192 TRP A CB  1 
ATOM   1573 C  CG  . TRP A 1 191 ? -14.799 -6.582  29.366  1.00 8.50  ? 192 TRP A CG  1 
ATOM   1574 C  CD1 . TRP A 1 191 ? -15.031 -6.995  30.660  1.00 10.18 ? 192 TRP A CD1 1 
ATOM   1575 C  CD2 . TRP A 1 191 ? -15.089 -7.693  28.507  1.00 9.32  ? 192 TRP A CD2 1 
ATOM   1576 N  NE1 . TRP A 1 191 ? -15.438 -8.330  30.644  1.00 11.66 ? 192 TRP A NE1 1 
ATOM   1577 C  CE2 . TRP A 1 191 ? -15.529 -8.765  29.339  1.00 9.49  ? 192 TRP A CE2 1 
ATOM   1578 C  CE3 . TRP A 1 191 ? -15.014 -7.890  27.102  1.00 10.26 ? 192 TRP A CE3 1 
ATOM   1579 C  CZ2 . TRP A 1 191 ? -15.829 -10.063 28.809  1.00 8.06  ? 192 TRP A CZ2 1 
ATOM   1580 C  CZ3 . TRP A 1 191 ? -15.316 -9.172  26.590  1.00 8.76  ? 192 TRP A CZ3 1 
ATOM   1581 C  CH2 . TRP A 1 191 ? -15.737 -10.232 27.459  1.00 9.23  ? 192 TRP A CH2 1 
ATOM   1582 N  N   . THR A 1 192 ? -14.057 -2.176  29.518  1.00 4.29  ? 193 THR A N   1 
ATOM   1583 C  CA  . THR A 1 192 ? -13.386 -0.892  29.173  1.00 6.87  ? 193 THR A CA  1 
ATOM   1584 C  C   . THR A 1 192 ? -12.157 -0.696  30.029  1.00 7.65  ? 193 THR A C   1 
ATOM   1585 O  O   . THR A 1 192 ? -12.152 -1.105  31.175  1.00 8.53  ? 193 THR A O   1 
ATOM   1586 C  CB  . THR A 1 192 ? -14.325 0.328   29.267  1.00 8.44  ? 193 THR A CB  1 
ATOM   1587 O  OG1 . THR A 1 192 ? -13.621 1.537   28.874  1.00 9.21  ? 193 THR A OG1 1 
ATOM   1588 C  CG2 . THR A 1 192 ? -14.868 0.629   30.772  1.00 6.09  ? 193 THR A CG2 1 
ATOM   1589 N  N   . TYR A 1 193 ? -11.086 -0.115  29.432  1.00 7.75  ? 194 TYR A N   1 
ATOM   1590 C  CA  . TYR A 1 193 ? -9.842  0.120   30.182  1.00 7.92  ? 194 TYR A CA  1 
ATOM   1591 C  C   . TYR A 1 193 ? -9.062  1.148   29.389  1.00 6.57  ? 194 TYR A C   1 
ATOM   1592 O  O   . TYR A 1 193 ? -9.359  1.391   28.186  1.00 6.66  ? 194 TYR A O   1 
ATOM   1593 C  CB  . TYR A 1 193 ? -9.062  -1.182  30.381  1.00 7.27  ? 194 TYR A CB  1 
ATOM   1594 C  CG  . TYR A 1 193 ? -8.361  -1.601  29.132  1.00 8.16  ? 194 TYR A CG  1 
ATOM   1595 C  CD1 . TYR A 1 193 ? -9.048  -2.356  28.131  1.00 4.82  ? 194 TYR A CD1 1 
ATOM   1596 C  CD2 . TYR A 1 193 ? -7.000  -1.231  28.919  1.00 8.90  ? 194 TYR A CD2 1 
ATOM   1597 C  CE1 . TYR A 1 193 ? -8.361  -2.780  26.919  1.00 5.54  ? 194 TYR A CE1 1 
ATOM   1598 C  CE2 . TYR A 1 193 ? -6.302  -1.544  27.698  1.00 9.51  ? 194 TYR A CE2 1 
ATOM   1599 C  CZ  . TYR A 1 193 ? -7.011  -2.303  26.712  1.00 6.50  ? 194 TYR A CZ  1 
ATOM   1600 O  OH  . TYR A 1 193 ? -6.326  -2.586  25.567  1.00 6.18  ? 194 TYR A OH  1 
ATOM   1601 N  N   . PRO A 1 194 ? -8.162  1.851   30.104  1.00 7.06  ? 195 PRO A N   1 
ATOM   1602 C  CA  . PRO A 1 194 ? -7.330  2.901   29.419  1.00 6.79  ? 195 PRO A CA  1 
ATOM   1603 C  C   . PRO A 1 194 ? -6.106  2.262   28.716  1.00 8.37  ? 195 PRO A C   1 
ATOM   1604 O  O   . PRO A 1 194 ? -5.403  1.412   29.375  1.00 7.79  ? 195 PRO A O   1 
ATOM   1605 C  CB  . PRO A 1 194 ? -6.829  3.777   30.623  1.00 8.12  ? 195 PRO A CB  1 
ATOM   1606 C  CG  . PRO A 1 194 ? -6.817  2.928   31.734  1.00 8.84  ? 195 PRO A CG  1 
ATOM   1607 C  CD  . PRO A 1 194 ? -7.943  1.853   31.549  1.00 8.10  ? 195 PRO A CD  1 
ATOM   1608 N  N   . GLY A 1 195 ? -5.892  2.553   27.442  1.00 6.28  ? 196 GLY A N   1 
ATOM   1609 C  CA  . GLY A 1 195 ? -4.726  1.920   26.749  1.00 7.02  ? 196 GLY A CA  1 
ATOM   1610 C  C   . GLY A 1 195 ? -4.202  2.779   25.660  1.00 6.89  ? 196 GLY A C   1 
ATOM   1611 O  O   . GLY A 1 195 ? -4.152  3.993   25.793  1.00 6.08  ? 196 GLY A O   1 
ATOM   1612 N  N   . SER A 1 196 ? -3.856  2.158   24.567  1.00 8.49  ? 197 SER A N   1 
ATOM   1613 C  CA  . SER A 1 196 ? -3.055  2.814   23.521  1.00 8.86  ? 197 SER A CA  1 
ATOM   1614 C  C   . SER A 1 196 ? -3.493  2.392   22.118  1.00 6.91  ? 197 SER A C   1 
ATOM   1615 O  O   . SER A 1 196 ? -4.179  1.375   21.937  1.00 7.83  ? 197 SER A O   1 
ATOM   1616 C  CB  . SER A 1 196 ? -1.581  2.416   23.630  1.00 9.60  ? 197 SER A CB  1 
ATOM   1617 O  OG  . SER A 1 196 ? -1.390  1.010   23.233  1.00 6.67  ? 197 SER A OG  1 
ATOM   1618 N  N   . LEU A 1 197 ? -2.982  3.099   21.115  1.00 7.30  ? 198 LEU A N   1 
ATOM   1619 C  CA  . LEU A 1 197 ? -3.020  2.609   19.727  1.00 6.68  ? 198 LEU A CA  1 
ATOM   1620 C  C   . LEU A 1 197 ? -2.225  1.271   19.743  1.00 6.72  ? 198 LEU A C   1 
ATOM   1621 O  O   . LEU A 1 197 ? -1.203  1.121   20.483  1.00 6.88  ? 198 LEU A O   1 
ATOM   1622 C  CB  . LEU A 1 197 ? -2.332  3.656   18.845  1.00 8.86  ? 198 LEU A CB  1 
ATOM   1623 C  CG  . LEU A 1 197 ? -2.953  5.016   18.742  1.00 12.87 ? 198 LEU A CG  1 
ATOM   1624 C  CD1 . LEU A 1 197 ? -2.008  5.803   17.821  1.00 13.68 ? 198 LEU A CD1 1 
ATOM   1625 C  CD2 . LEU A 1 197 ? -4.196  4.879   18.051  1.00 11.58 ? 198 LEU A CD2 1 
ATOM   1626 N  N   . THR A 1 198 ? -2.687  0.303   18.951  1.00 6.18  ? 199 THR A N   1 
ATOM   1627 C  CA  . THR A 1 198 ? -1.968  -1.041  18.917  1.00 5.29  ? 199 THR A CA  1 
ATOM   1628 C  C   . THR A 1 198 ? -0.969  -1.074  17.772  1.00 7.06  ? 199 THR A C   1 
ATOM   1629 O  O   . THR A 1 198 ? -0.374  -2.179  17.568  1.00 7.78  ? 199 THR A O   1 
ATOM   1630 C  CB  . THR A 1 198 ? -3.022  -2.197  18.796  1.00 6.85  ? 199 THR A CB  1 
ATOM   1631 O  OG1 . THR A 1 198 ? -3.607  -2.143  17.525  1.00 6.87  ? 199 THR A OG1 1 
ATOM   1632 C  CG2 . THR A 1 198 ? -3.961  -2.155  19.989  1.00 7.08  ? 199 THR A CG2 1 
ATOM   1633 N  N   . THR A 1 199 ? -0.868  -0.010  16.956  1.00 7.32  ? 200 THR A N   1 
ATOM   1634 C  CA  . THR A 1 199 ? 0.218   0.067   15.973  1.00 8.75  ? 200 THR A CA  1 
ATOM   1635 C  C   . THR A 1 199 ? 1.086   1.282   16.296  1.00 8.34  ? 200 THR A C   1 
ATOM   1636 O  O   . THR A 1 199 ? 0.571   2.239   16.865  1.00 7.61  ? 200 THR A O   1 
ATOM   1637 C  CB  . THR A 1 199 ? -0.248  0.133   14.536  1.00 9.65  ? 200 THR A CB  1 
ATOM   1638 O  OG1 . THR A 1 199 ? -0.999  1.373   14.284  1.00 14.93 ? 200 THR A OG1 1 
ATOM   1639 C  CG2 . THR A 1 199 ? -1.147  -1.054  14.248  1.00 10.12 ? 200 THR A CG2 1 
ATOM   1640 N  N   . PRO A 1 200 ? 2.358   1.237   15.850  1.00 9.82  ? 201 PRO A N   1 
ATOM   1641 C  CA  . PRO A 1 200 ? 3.056   2.529   15.922  1.00 9.66  ? 201 PRO A CA  1 
ATOM   1642 C  C   . PRO A 1 200 ? 2.164   3.679   15.365  1.00 8.16  ? 201 PRO A C   1 
ATOM   1643 O  O   . PRO A 1 200 ? 1.497   3.545   14.270  1.00 9.52  ? 201 PRO A O   1 
ATOM   1644 C  CB  . PRO A 1 200 ? 4.282   2.287   14.996  1.00 9.56  ? 201 PRO A CB  1 
ATOM   1645 C  CG  . PRO A 1 200 ? 4.597   0.909   15.127  1.00 8.92  ? 201 PRO A CG  1 
ATOM   1646 C  CD  . PRO A 1 200 ? 3.168   0.210   15.145  1.00 11.49 ? 201 PRO A CD  1 
ATOM   1647 N  N   . PRO A 1 201 ? 2.260   4.904   16.000  1.00 10.24 ? 202 PRO A N   1 
ATOM   1648 C  CA  . PRO A 1 201 ? 3.136   5.290   17.108  1.00 11.09 ? 202 PRO A CA  1 
ATOM   1649 C  C   . PRO A 1 201 ? 2.818   4.852   18.543  1.00 7.60  ? 202 PRO A C   1 
ATOM   1650 O  O   . PRO A 1 201 ? 3.456   5.304   19.510  1.00 8.97  ? 202 PRO A O   1 
ATOM   1651 C  CB  . PRO A 1 201 ? 3.174   6.820   16.971  1.00 9.84  ? 202 PRO A CB  1 
ATOM   1652 C  CG  . PRO A 1 201 ? 1.849   7.152   16.513  1.00 12.18 ? 202 PRO A CG  1 
ATOM   1653 C  CD  . PRO A 1 201 ? 1.494   6.092   15.499  1.00 10.21 ? 202 PRO A CD  1 
ATOM   1654 N  N   . LEU A 1 202 ? 1.806   3.912   18.683  1.00 7.28  ? 203 LEU A N   1 
ATOM   1655 C  CA  . LEU A 1 202 ? 1.540   3.326   19.991  1.00 6.88  ? 203 LEU A CA  1 
ATOM   1656 C  C   . LEU A 1 202 ? 1.159   4.323   21.135  1.00 6.87  ? 203 LEU A C   1 
ATOM   1657 O  O   . LEU A 1 202 ? 1.365   4.065   22.312  1.00 7.81  ? 203 LEU A O   1 
ATOM   1658 C  CB  . LEU A 1 202 ? 2.677   2.418   20.490  1.00 7.99  ? 203 LEU A CB  1 
ATOM   1659 C  CG  . LEU A 1 202 ? 3.041   1.290   19.501  1.00 6.43  ? 203 LEU A CG  1 
ATOM   1660 C  CD1 . LEU A 1 202 ? 4.395   0.672   19.956  1.00 11.04 ? 203 LEU A CD1 1 
ATOM   1661 C  CD2 . LEU A 1 202 ? 1.892   0.218   19.514  1.00 10.31 ? 203 LEU A CD2 1 
ATOM   1662 N  N   . LEU A 1 203 ? 0.584   5.448   20.708  1.00 6.41  ? 204 LEU A N   1 
ATOM   1663 C  CA  . LEU A 1 203 ? 0.333   6.591   21.609  1.00 8.18  ? 204 LEU A CA  1 
ATOM   1664 C  C   . LEU A 1 203 ? -0.684  6.135   22.679  1.00 8.64  ? 204 LEU A C   1 
ATOM   1665 O  O   . LEU A 1 203 ? -1.700  5.413   22.371  1.00 7.40  ? 204 LEU A O   1 
ATOM   1666 C  CB  . LEU A 1 203 ? -0.208  7.805   20.818  1.00 6.97  ? 204 LEU A CB  1 
ATOM   1667 C  CG  . LEU A 1 203 ? 0.863   8.375   19.849  1.00 9.68  ? 204 LEU A CG  1 
ATOM   1668 C  CD1 . LEU A 1 203 ? 0.262   9.440   18.964  1.00 12.79 ? 204 LEU A CD1 1 
ATOM   1669 C  CD2 . LEU A 1 203 ? 2.058   8.967   20.712  1.00 14.18 ? 204 LEU A CD2 1 
ATOM   1670 N  N   . GLU A 1 204 ? -0.490  6.594   23.890  1.00 8.17  ? 205 GLU A N   1 
ATOM   1671 C  CA  . GLU A 1 204 ? -1.328  6.199   25.024  1.00 6.70  ? 205 GLU A CA  1 
ATOM   1672 C  C   . GLU A 1 204 ? -2.514  7.193   25.147  1.00 7.96  ? 205 GLU A C   1 
ATOM   1673 O  O   . GLU A 1 204 ? -2.649  7.959   26.163  1.00 8.83  ? 205 GLU A O   1 
ATOM   1674 C  CB  . GLU A 1 204 ? -0.448  6.105   26.303  1.00 9.95  ? 205 GLU A CB  1 
ATOM   1675 C  CG  . GLU A 1 204 ? 0.362   4.776   26.159  1.00 8.84  ? 205 GLU A CG  1 
ATOM   1676 C  CD  . GLU A 1 204 ? 1.390   4.570   27.294  1.00 14.11 ? 205 GLU A CD  1 
ATOM   1677 O  OE1 . GLU A 1 204 ? 1.717   5.580   28.031  1.00 12.36 ? 205 GLU A OE1 1 
ATOM   1678 O  OE2 . GLU A 1 204 ? 1.814   3.412   27.413  1.00 11.68 ? 205 GLU A OE2 1 
ATOM   1679 N  N   . CYS A 1 205 ? -3.388  7.104   24.143  1.00 6.22  ? 206 CYS A N   1 
ATOM   1680 C  CA  . CYS A 1 205 ? -4.465  8.126   24.024  1.00 6.21  ? 206 CYS A CA  1 
ATOM   1681 C  C   . CYS A 1 205 ? -5.834  7.485   23.895  1.00 7.03  ? 206 CYS A C   1 
ATOM   1682 O  O   . CYS A 1 205 ? -6.759  8.176   23.472  1.00 8.04  ? 206 CYS A O   1 
ATOM   1683 C  CB  . CYS A 1 205 ? -4.204  8.978   22.777  1.00 7.16  ? 206 CYS A CB  1 
ATOM   1684 S  SG  . CYS A 1 205 ? -4.109  7.966   21.267  1.00 8.82  ? 206 CYS A SG  1 
ATOM   1685 N  N   . VAL A 1 206 ? -5.965  6.187   24.206  1.00 6.14  ? 207 VAL A N   1 
ATOM   1686 C  CA  . VAL A 1 206 ? -7.209  5.447   23.823  1.00 4.61  ? 207 VAL A CA  1 
ATOM   1687 C  C   . VAL A 1 206 ? -8.004  4.974   25.043  1.00 4.88  ? 207 VAL A C   1 
ATOM   1688 O  O   . VAL A 1 206 ? -7.413  4.379   25.963  1.00 7.75  ? 207 VAL A O   1 
ATOM   1689 C  CB  . VAL A 1 206 ? -6.870  4.170   23.023  1.00 6.08  ? 207 VAL A CB  1 
ATOM   1690 C  CG1 . VAL A 1 206 ? -8.246  3.492   22.627  1.00 5.82  ? 207 VAL A CG1 1 
ATOM   1691 C  CG2 . VAL A 1 206 ? -6.159  4.533   21.702  1.00 7.10  ? 207 VAL A CG2 1 
ATOM   1692 N  N   . THR A 1 207 ? -9.315  5.272   25.098  1.00 5.45  ? 208 THR A N   1 
ATOM   1693 C  CA  . THR A 1 207 ? -10.236 4.572   25.988  1.00 4.95  ? 208 THR A CA  1 
ATOM   1694 C  C   . THR A 1 207 ? -10.727 3.412   25.155  1.00 6.27  ? 208 THR A C   1 
ATOM   1695 O  O   . THR A 1 207 ? -11.427 3.632   24.144  1.00 5.65  ? 208 THR A O   1 
ATOM   1696 C  CB  . THR A 1 207 ? -11.448 5.460   26.487  1.00 5.92  ? 208 THR A CB  1 
ATOM   1697 O  OG1 . THR A 1 207 ? -10.904 6.598   27.193  1.00 7.22  ? 208 THR A OG1 1 
ATOM   1698 C  CG2 . THR A 1 207 ? -12.302 4.671   27.313  1.00 6.37  ? 208 THR A CG2 1 
ATOM   1699 N  N   . TRP A 1 208 ? -10.390 2.208   25.583  1.00 7.35  ? 209 TRP A N   1 
ATOM   1700 C  CA  . TRP A 1 208 ? -10.845 1.018   24.885  1.00 5.65  ? 209 TRP A CA  1 
ATOM   1701 C  C   . TRP A 1 208 ? -12.205 0.549   25.392  1.00 6.95  ? 209 TRP A C   1 
ATOM   1702 O  O   . TRP A 1 208 ? -12.386 0.419   26.612  1.00 6.26  ? 209 TRP A O   1 
ATOM   1703 C  CB  . TRP A 1 208 ? -9.815  -0.102  25.019  1.00 5.78  ? 209 TRP A CB  1 
ATOM   1704 C  CG  . TRP A 1 208 ? -8.713  0.005   24.020  1.00 6.13  ? 209 TRP A CG  1 
ATOM   1705 C  CD1 . TRP A 1 208 ? -7.473  0.536   24.220  1.00 6.61  ? 209 TRP A CD1 1 
ATOM   1706 C  CD2 . TRP A 1 208 ? -8.754  -0.417  22.653  1.00 6.28  ? 209 TRP A CD2 1 
ATOM   1707 N  NE1 . TRP A 1 208 ? -6.736  0.466   23.063  1.00 7.44  ? 209 TRP A NE1 1 
ATOM   1708 C  CE2 . TRP A 1 208 ? -7.501  -0.116  22.085  1.00 5.85  ? 209 TRP A CE2 1 
ATOM   1709 C  CE3 . TRP A 1 208 ? -9.728  -1.023  21.854  1.00 6.64  ? 209 TRP A CE3 1 
ATOM   1710 C  CZ2 . TRP A 1 208 ? -7.196  -0.400  20.757  1.00 7.09  ? 209 TRP A CZ2 1 
ATOM   1711 C  CZ3 . TRP A 1 208 ? -9.424  -1.305  20.536  1.00 4.72  ? 209 TRP A CZ3 1 
ATOM   1712 C  CH2 . TRP A 1 208 ? -8.168  -0.993  20.000  1.00 6.23  ? 209 TRP A CH2 1 
ATOM   1713 N  N   . ILE A 1 209 ? -13.093 0.304   24.420  1.00 4.26  ? 210 ILE A N   1 
ATOM   1714 C  CA  . ILE A 1 209 ? -14.395 -0.278  24.788  1.00 6.33  ? 210 ILE A CA  1 
ATOM   1715 C  C   . ILE A 1 209 ? -14.496 -1.560  23.926  1.00 6.44  ? 210 ILE A C   1 
ATOM   1716 O  O   . ILE A 1 209 ? -14.602 -1.432  22.742  1.00 5.33  ? 210 ILE A O   1 
ATOM   1717 C  CB  . ILE A 1 209 ? -15.450 0.765   24.414  1.00 6.15  ? 210 ILE A CB  1 
ATOM   1718 C  CG1 . ILE A 1 209 ? -15.247 2.042   25.235  1.00 9.22  ? 210 ILE A CG1 1 
ATOM   1719 C  CG2 . ILE A 1 209 ? -16.875 0.115   24.756  1.00 6.89  ? 210 ILE A CG2 1 
ATOM   1720 C  CD1 . ILE A 1 209 ? -16.035 3.266   24.678  1.00 11.31 ? 210 ILE A CD1 1 
ATOM   1721 N  N   . VAL A 1 210 ? -14.467 -2.724  24.547  1.00 6.03  ? 211 VAL A N   1 
ATOM   1722 C  CA  . VAL A 1 210 ? -14.468 -4.012  23.834  1.00 4.89  ? 211 VAL A CA  1 
ATOM   1723 C  C   . VAL A 1 210 ? -15.751 -4.726  24.133  1.00 5.29  ? 211 VAL A C   1 
ATOM   1724 O  O   . VAL A 1 210 ? -16.065 -4.961  25.283  1.00 7.30  ? 211 VAL A O   1 
ATOM   1725 C  CB  . VAL A 1 210 ? -13.224 -4.897  24.260  1.00 5.52  ? 211 VAL A CB  1 
ATOM   1726 C  CG1 . VAL A 1 210 ? -13.224 -6.255  23.488  1.00 5.98  ? 211 VAL A CG1 1 
ATOM   1727 C  CG2 . VAL A 1 210 ? -11.883 -4.059  23.952  1.00 4.57  ? 211 VAL A CG2 1 
ATOM   1728 N  N   . LEU A 1 211 ? -16.485 -4.965  23.075  1.00 5.75  ? 212 LEU A N   1 
ATOM   1729 C  CA  . LEU A 1 211 ? -17.760 -5.656  23.247  1.00 6.40  ? 212 LEU A CA  1 
ATOM   1730 C  C   . LEU A 1 211 ? -17.572 -7.128  23.555  1.00 5.01  ? 212 LEU A C   1 
ATOM   1731 O  O   . LEU A 1 211 ? -16.697 -7.821  22.991  1.00 6.93  ? 212 LEU A O   1 
ATOM   1732 C  CB  . LEU A 1 211 ? -18.493 -5.550  21.894  1.00 6.91  ? 212 LEU A CB  1 
ATOM   1733 C  CG  . LEU A 1 211 ? -18.981 -4.141  21.447  1.00 8.64  ? 212 LEU A CG  1 
ATOM   1734 C  CD1 . LEU A 1 211 ? -20.083 -4.192  20.277  1.00 10.39 ? 212 LEU A CD1 1 
ATOM   1735 C  CD2 . LEU A 1 211 ? -19.408 -3.213  22.614  1.00 7.35  ? 212 LEU A CD2 1 
ATOM   1736 N  N   . LYS A 1 212 ? -18.445 -7.568  24.491  1.00 8.12  ? 213 LYS A N   1 
ATOM   1737 C  CA  . LYS A 1 212 ? -18.409 -8.988  24.896  1.00 7.25  ? 213 LYS A CA  1 
ATOM   1738 C  C   . LYS A 1 212 ? -18.927 -9.930  23.785  1.00 7.94  ? 213 LYS A C   1 
ATOM   1739 O  O   . LYS A 1 212 ? -18.408 -11.020 23.608  1.00 8.89  ? 213 LYS A O   1 
ATOM   1740 C  CB  . LYS A 1 212 ? -19.169 -9.189  26.204  1.00 9.37  ? 213 LYS A CB  1 
ATOM   1741 C  CG  . LYS A 1 212 ? -19.411 -10.675 26.529  1.00 12.16 ? 213 LYS A CG  1 
ATOM   1742 C  CD  . LYS A 1 212 ? -20.229 -10.861 27.780  1.00 17.95 ? 213 LYS A CD  1 
ATOM   1743 C  CE  . LYS A 1 212 ? -20.137 -12.267 28.335  1.00 27.35 ? 213 LYS A CE  1 
ATOM   1744 N  NZ  . LYS A 1 212 ? -21.019 -12.253 29.594  1.00 31.83 ? 213 LYS A NZ  1 
ATOM   1745 N  N   . GLU A 1 213 ? -19.932 -9.495  23.049  1.00 7.57  ? 214 GLU A N   1 
ATOM   1746 C  CA  . GLU A 1 213 ? -20.532 -10.383 22.030  1.00 9.32  ? 214 GLU A CA  1 
ATOM   1747 C  C   . GLU A 1 213 ? -19.779 -10.293 20.728  1.00 6.68  ? 214 GLU A C   1 
ATOM   1748 O  O   . GLU A 1 213 ? -19.740 -9.206  20.116  1.00 8.07  ? 214 GLU A O   1 
ATOM   1749 C  CB  . GLU A 1 213 ? -22.005 -9.998  21.810  1.00 8.04  ? 214 GLU A CB  1 
ATOM   1750 C  CG  . GLU A 1 213 ? -22.610 -10.959 20.783  1.00 11.56 ? 214 GLU A CG  1 
ATOM   1751 C  CD  . GLU A 1 213 ? -24.104 -10.844 20.599  1.00 17.19 ? 214 GLU A CD  1 
ATOM   1752 O  OE1 . GLU A 1 213 ? -24.676 -9.987  21.218  1.00 12.87 ? 214 GLU A OE1 1 
ATOM   1753 O  OE2 . GLU A 1 213 ? -24.675 -11.762 19.965  1.00 25.74 ? 214 GLU A OE2 1 
ATOM   1754 N  N   . PRO A 1 214 ? -19.180 -11.392 20.248  1.00 8.66  ? 215 PRO A N   1 
ATOM   1755 C  CA  . PRO A 1 214 ? -18.508 -11.346 18.913  1.00 7.49  ? 215 PRO A CA  1 
ATOM   1756 C  C   . PRO A 1 214 ? -19.491 -11.343 17.761  1.00 8.35  ? 215 PRO A C   1 
ATOM   1757 O  O   . PRO A 1 214 ? -20.713 -11.708 18.023  1.00 11.36 ? 215 PRO A O   1 
ATOM   1758 C  CB  . PRO A 1 214 ? -17.705 -12.670 18.856  1.00 8.19  ? 215 PRO A CB  1 
ATOM   1759 C  CG  . PRO A 1 214 ? -18.472 -13.616 19.705  1.00 12.93 ? 215 PRO A CG  1 
ATOM   1760 C  CD  . PRO A 1 214 ? -19.191 -12.759 20.830  1.00 9.11  ? 215 PRO A CD  1 
ATOM   1761 N  N   . ILE A 1 215 ? -19.090 -10.855 16.597  1.00 7.88  ? 216 ILE A N   1 
ATOM   1762 C  CA  . ILE A 1 215 ? -19.970 -11.091 15.446  1.00 9.39  ? 216 ILE A CA  1 
ATOM   1763 C  C   . ILE A 1 215 ? -19.449 -12.329 14.731  1.00 10.43 ? 216 ILE A C   1 
ATOM   1764 O  O   . ILE A 1 215 ? -18.264 -12.680 14.819  1.00 10.03 ? 216 ILE A O   1 
ATOM   1765 C  CB  . ILE A 1 215 ? -20.004 -9.928  14.444  1.00 8.76  ? 216 ILE A CB  1 
ATOM   1766 C  CG1 . ILE A 1 215 ? -18.545 -9.545  13.977  1.00 7.84  ? 216 ILE A CG1 1 
ATOM   1767 C  CG2 . ILE A 1 215 ? -20.730 -8.680  15.113  1.00 11.33 ? 216 ILE A CG2 1 
ATOM   1768 C  CD1 . ILE A 1 215 ? -18.520 -8.519  12.690  1.00 9.23  ? 216 ILE A CD1 1 
ATOM   1769 N  N   . SER A 1 216 ? -20.369 -12.985 13.994  1.00 9.50  ? 217 SER A N   1 
ATOM   1770 C  CA  . SER A 1 216 ? -19.944 -14.137 13.163  1.00 10.01 ? 217 SER A CA  1 
ATOM   1771 C  C   . SER A 1 216 ? -19.754 -13.661 11.713  1.00 9.85  ? 217 SER A C   1 
ATOM   1772 O  O   . SER A 1 216 ? -20.566 -12.878 11.153  1.00 11.11 ? 217 SER A O   1 
ATOM   1773 C  CB  . SER A 1 216 ? -21.022 -15.245 13.134  1.00 12.49 ? 217 SER A CB  1 
ATOM   1774 O  OG  . SER A 1 216 ? -21.093 -15.823 14.425  1.00 18.96 ? 217 SER A OG  1 
ATOM   1775 N  N   . VAL A 1 217 ? -18.666 -14.142 11.120  1.00 8.85  ? 218 VAL A N   1 
ATOM   1776 C  CA  . VAL A 1 217 ? -18.326 -13.969 9.720   1.00 8.47  ? 218 VAL A CA  1 
ATOM   1777 C  C   . VAL A 1 217 ? -18.070 -15.337 9.075   1.00 8.75  ? 218 VAL A C   1 
ATOM   1778 O  O   . VAL A 1 217 ? -17.659 -16.297 9.781   1.00 9.19  ? 218 VAL A O   1 
ATOM   1779 C  CB  . VAL A 1 217 ? -17.103 -12.983 9.450   1.00 9.33  ? 218 VAL A CB  1 
ATOM   1780 C  CG1 . VAL A 1 217 ? -17.479 -11.670 10.125  1.00 8.90  ? 218 VAL A CG1 1 
ATOM   1781 C  CG2 . VAL A 1 217 ? -15.707 -13.619 9.950   1.00 10.74 ? 218 VAL A CG2 1 
ATOM   1782 N  N   . SER A 1 218 ? -18.296 -15.492 7.799   1.00 8.44  ? 219 SER A N   1 
ATOM   1783 C  CA  . SER A 1 218 ? -18.079 -16.812 7.189   1.00 9.73  ? 219 SER A CA  1 
ATOM   1784 C  C   . SER A 1 218 ? -16.574 -17.074 6.948   1.00 9.13  ? 219 SER A C   1 
ATOM   1785 O  O   . SER A 1 218 ? -15.714 -16.154 6.811   1.00 8.52  ? 219 SER A O   1 
ATOM   1786 C  CB  . SER A 1 218 ? -18.852 -16.946 5.848   1.00 8.50  ? 219 SER A CB  1 
ATOM   1787 O  OG  . SER A 1 218 ? -18.318 -16.060 4.941   1.00 11.49 ? 219 SER A OG  1 
ATOM   1788 N  N   A SER A 1 219 ? -16.229 -18.346 6.827   0.50 9.25  ? 220 SER A N   1 
ATOM   1789 N  N   B SER A 1 219 ? -16.238 -18.345 6.824   0.50 9.45  ? 220 SER A N   1 
ATOM   1790 C  CA  A SER A 1 219 ? -14.895 -18.722 6.360   0.50 11.62 ? 220 SER A CA  1 
ATOM   1791 C  CA  B SER A 1 219 ? -14.902 -18.706 6.387   0.50 12.09 ? 220 SER A CA  1 
ATOM   1792 C  C   A SER A 1 219 ? -14.527 -18.011 5.028   0.50 12.41 ? 220 SER A C   1 
ATOM   1793 C  C   B SER A 1 219 ? -14.528 -18.011 5.040   0.50 12.70 ? 220 SER A C   1 
ATOM   1794 O  O   A SER A 1 219 ? -13.402 -17.502 4.894   0.50 11.76 ? 220 SER A O   1 
ATOM   1795 O  O   B SER A 1 219 ? -13.398 -17.491 4.921   0.50 12.22 ? 220 SER A O   1 
ATOM   1796 C  CB  A SER A 1 219 ? -14.818 -20.258 6.270   0.50 11.74 ? 220 SER A CB  1 
ATOM   1797 C  CB  B SER A 1 219 ? -14.769 -20.243 6.391   0.50 12.01 ? 220 SER A CB  1 
ATOM   1798 O  OG  A SER A 1 219 ? -15.853 -20.727 5.426   0.50 9.65  ? 220 SER A OG  1 
ATOM   1799 O  OG  B SER A 1 219 ? -13.419 -20.639 6.311   0.50 13.10 ? 220 SER A OG  1 
ATOM   1800 N  N   . GLU A 1 220 ? -15.463 -17.940 4.055   1.00 12.42 ? 221 GLU A N   1 
ATOM   1801 C  CA  . GLU A 1 220 ? -15.205 -17.276 2.730   1.00 12.09 ? 221 GLU A CA  1 
ATOM   1802 C  C   . GLU A 1 220 ? -14.891 -15.756 2.942   1.00 11.19 ? 221 GLU A C   1 
ATOM   1803 O  O   . GLU A 1 220 ? -13.948 -15.241 2.328   1.00 11.89 ? 221 GLU A O   1 
ATOM   1804 C  CB  . GLU A 1 220 ? -16.390 -17.433 1.804   1.00 14.48 ? 221 GLU A CB  1 
ATOM   1805 C  CG  . GLU A 1 220 ? -16.576 -18.949 1.478   1.00 17.40 ? 221 GLU A CG  1 
ATOM   1806 C  CD  . GLU A 1 220 ? -17.551 -19.665 2.420   1.00 26.08 ? 221 GLU A CD  1 
ATOM   1807 O  OE1 . GLU A 1 220 ? -18.064 -19.084 3.394   1.00 17.85 ? 221 GLU A OE1 1 
ATOM   1808 O  OE2 . GLU A 1 220 ? -17.754 -20.889 2.206   1.00 29.18 ? 221 GLU A OE2 1 
ATOM   1809 N  N   . GLN A 1 221 ? -15.617 -15.130 3.866   1.00 10.51 ? 222 GLN A N   1 
ATOM   1810 C  CA  . GLN A 1 221 ? -15.350 -13.691 4.181   1.00 10.47 ? 222 GLN A CA  1 
ATOM   1811 C  C   . GLN A 1 221 ? -13.894 -13.481 4.689   1.00 11.06 ? 222 GLN A C   1 
ATOM   1812 O  O   . GLN A 1 221 ? -13.154 -12.683 4.148   1.00 10.02 ? 222 GLN A O   1 
ATOM   1813 C  CB  . GLN A 1 221 ? -16.400 -13.160 5.162   1.00 11.73 ? 222 GLN A CB  1 
ATOM   1814 C  CG  . GLN A 1 221 ? -17.719 -12.910 4.377   1.00 11.82 ? 222 GLN A CG  1 
ATOM   1815 C  CD  . GLN A 1 221 ? -18.871 -12.435 5.264   1.00 10.97 ? 222 GLN A CD  1 
ATOM   1816 O  OE1 . GLN A 1 221 ? -19.003 -12.842 6.420   1.00 11.30 ? 222 GLN A OE1 1 
ATOM   1817 N  NE2 . GLN A 1 221 ? -19.725 -11.578 4.704   1.00 11.77 ? 222 GLN A NE2 1 
ATOM   1818 N  N   . VAL A 1 222 ? -13.480 -14.261 5.712   1.00 10.82 ? 223 VAL A N   1 
ATOM   1819 C  CA  . VAL A 1 222 ? -12.136 -14.053 6.290   1.00 11.61 ? 223 VAL A CA  1 
ATOM   1820 C  C   . VAL A 1 222 ? -11.001 -14.533 5.328   1.00 11.46 ? 223 VAL A C   1 
ATOM   1821 O  O   . VAL A 1 222 ? -9.964  -13.920 5.212   1.00 11.12 ? 223 VAL A O   1 
ATOM   1822 C  CB  . VAL A 1 222 ? -12.022 -14.632 7.731   1.00 13.40 ? 223 VAL A CB  1 
ATOM   1823 C  CG1 . VAL A 1 222 ? -12.080 -16.140 7.714   1.00 14.55 ? 223 VAL A CG1 1 
ATOM   1824 C  CG2 . VAL A 1 222 ? -10.743 -14.101 8.411   1.00 12.70 ? 223 VAL A CG2 1 
ATOM   1825 N  N   . LEU A 1 223 ? -11.338 -15.551 4.508   1.00 12.40 ? 224 LEU A N   1 
ATOM   1826 C  CA  . LEU A 1 223 ? -10.396 -15.988 3.472   1.00 14.71 ? 224 LEU A CA  1 
ATOM   1827 C  C   . LEU A 1 223 ? -10.061 -14.846 2.488   1.00 16.14 ? 224 LEU A C   1 
ATOM   1828 O  O   . LEU A 1 223 ? -8.912  -14.718 2.063   1.00 15.15 ? 224 LEU A O   1 
ATOM   1829 C  CB  . LEU A 1 223 ? -11.005 -17.205 2.741   1.00 15.34 ? 224 LEU A CB  1 
ATOM   1830 C  CG  . LEU A 1 223 ? -10.648 -18.414 3.603   1.00 16.47 ? 224 LEU A CG  1 
ATOM   1831 C  CD1 . LEU A 1 223 ? -11.517 -19.689 3.351   1.00 26.26 ? 224 LEU A CD1 1 
ATOM   1832 C  CD2 . LEU A 1 223 ? -9.162  -18.717 3.372   1.00 19.36 ? 224 LEU A CD2 1 
ATOM   1833 N  N   . LYS A 1 224 ? -11.085 -14.052 2.141   1.00 13.39 ? 225 LYS A N   1 
ATOM   1834 C  CA  . LYS A 1 224 ? -10.910 -12.872 1.292   1.00 15.36 ? 225 LYS A CA  1 
ATOM   1835 C  C   . LYS A 1 224 ? -10.002 -11.856 1.988   1.00 12.94 ? 225 LYS A C   1 
ATOM   1836 O  O   . LYS A 1 224 ? -9.159  -11.223 1.285   1.00 13.16 ? 225 LYS A O   1 
ATOM   1837 C  CB  . LYS A 1 224 ? -12.255 -12.304 0.802   1.00 13.29 ? 225 LYS A CB  1 
ATOM   1838 C  CG  . LYS A 1 224 ? -12.874 -13.362 -0.314  1.00 16.17 ? 225 LYS A CG  1 
ATOM   1839 C  CD  . LYS A 1 224 ? -14.318 -13.085 -0.870  1.00 19.41 ? 225 LYS A CD  1 
ATOM   1840 C  CE  . LYS A 1 224 ? -14.860 -14.270 -1.802  1.00 23.81 ? 225 LYS A CE  1 
ATOM   1841 N  NZ  . LYS A 1 224 ? -16.027 -13.886 -2.735  1.00 21.26 ? 225 LYS A NZ  1 
ATOM   1842 N  N   . PHE A 1 225 ? -10.099 -11.669 3.330   1.00 11.82 ? 226 PHE A N   1 
ATOM   1843 C  CA  . PHE A 1 225 ? -9.171  -10.734 4.024   1.00 10.70 ? 226 PHE A CA  1 
ATOM   1844 C  C   . PHE A 1 225 ? -7.723  -11.226 3.834   1.00 10.08 ? 226 PHE A C   1 
ATOM   1845 O  O   . PHE A 1 225 ? -6.802  -10.439 3.623   1.00 11.31 ? 226 PHE A O   1 
ATOM   1846 C  CB  . PHE A 1 225 ? -9.366  -10.799 5.546   1.00 11.17 ? 226 PHE A CB  1 
ATOM   1847 C  CG  . PHE A 1 225 ? -10.525 -10.004 6.088   1.00 10.34 ? 226 PHE A CG  1 
ATOM   1848 C  CD1 . PHE A 1 225 ? -11.536 -9.531  5.276   1.00 11.49 ? 226 PHE A CD1 1 
ATOM   1849 C  CD2 . PHE A 1 225 ? -10.605 -9.763  7.452   1.00 12.99 ? 226 PHE A CD2 1 
ATOM   1850 C  CE1 . PHE A 1 225 ? -12.597 -8.817  5.821   1.00 12.71 ? 226 PHE A CE1 1 
ATOM   1851 C  CE2 . PHE A 1 225 ? -11.656 -9.055  7.997   1.00 13.95 ? 226 PHE A CE2 1 
ATOM   1852 C  CZ  . PHE A 1 225 ? -12.651 -8.582  7.182   1.00 11.95 ? 226 PHE A CZ  1 
ATOM   1853 N  N   . ARG A 1 226 ? -7.546  -12.535 3.880   1.00 10.19 ? 227 ARG A N   1 
ATOM   1854 C  CA  . ARG A 1 226 ? -6.224  -13.132 3.755   1.00 11.51 ? 227 ARG A CA  1 
ATOM   1855 C  C   . ARG A 1 226 ? -5.584  -13.171 2.354   1.00 10.75 ? 227 ARG A C   1 
ATOM   1856 O  O   . ARG A 1 226 ? -4.412  -13.580 2.232   1.00 12.74 ? 227 ARG A O   1 
ATOM   1857 C  CB  . ARG A 1 226 ? -6.215  -14.550 4.332   1.00 11.85 ? 227 ARG A CB  1 
ATOM   1858 C  CG  . ARG A 1 226 ? -6.647  -14.661 5.769   1.00 11.31 ? 227 ARG A CG  1 
ATOM   1859 C  CD  . ARG A 1 226 ? -6.630  -16.173 6.251   1.00 11.08 ? 227 ARG A CD  1 
ATOM   1860 N  NE  . ARG A 1 226 ? -7.266  -16.224 7.594   1.00 10.89 ? 227 ARG A NE  1 
ATOM   1861 C  CZ  . ARG A 1 226 ? -8.198  -17.119 7.998   1.00 13.87 ? 227 ARG A CZ  1 
ATOM   1862 N  NH1 . ARG A 1 226 ? -8.539  -18.140 7.177   1.00 13.67 ? 227 ARG A NH1 1 
ATOM   1863 N  NH2 . ARG A 1 226 ? -8.717  -17.096 9.234   1.00 16.29 ? 227 ARG A NH2 1 
ATOM   1864 N  N   . LYS A 1 227 ? -6.317  -12.671 1.360   1.00 10.62 ? 228 LYS A N   1 
ATOM   1865 C  CA  . LYS A 1 227 ? -5.825  -12.573 -0.012  1.00 12.64 ? 228 LYS A CA  1 
ATOM   1866 C  C   . LYS A 1 227 ? -5.223  -11.184 -0.253  1.00 13.39 ? 228 LYS A C   1 
ATOM   1867 O  O   . LYS A 1 227 ? -4.533  -10.965 -1.234  1.00 13.23 ? 228 LYS A O   1 
ATOM   1868 C  CB  . LYS A 1 227 ? -6.955  -12.768 -0.971  1.00 13.76 ? 228 LYS A CB  1 
ATOM   1869 C  CG  . LYS A 1 227 ? -7.300  -14.238 -1.061  1.00 16.64 ? 228 LYS A CG  1 
ATOM   1870 C  CD  . LYS A 1 227 ? -8.511  -14.394 -1.952  1.00 19.56 ? 228 LYS A CD  1 
ATOM   1871 C  CE  . LYS A 1 227 ? -8.145  -13.865 -3.339  1.00 27.95 ? 228 LYS A CE  1 
ATOM   1872 N  NZ  . LYS A 1 227 ? -8.626  -14.699 -4.484  1.00 30.00 ? 228 LYS A NZ  1 
ATOM   1873 N  N   . LEU A 1 228 ? -5.499  -10.246 0.678   1.00 13.19 ? 229 LEU A N   1 
ATOM   1874 C  CA  . LEU A 1 228 ? -4.708  -8.993  0.663   1.00 13.46 ? 229 LEU A CA  1 
ATOM   1875 C  C   . LEU A 1 228 ? -3.176  -9.139  0.776   1.00 13.63 ? 229 LEU A C   1 
ATOM   1876 O  O   . LEU A 1 228 ? -2.637  -10.123 1.251   1.00 11.79 ? 229 LEU A O   1 
ATOM   1877 C  CB  . LEU A 1 228 ? -5.196  -8.037  1.764   1.00 10.99 ? 229 LEU A CB  1 
ATOM   1878 C  CG  . LEU A 1 228 ? -6.625  -7.586  1.553   1.00 12.64 ? 229 LEU A CG  1 
ATOM   1879 C  CD1 . LEU A 1 228 ? -7.092  -6.970  2.824   1.00 13.23 ? 229 LEU A CD1 1 
ATOM   1880 C  CD2 . LEU A 1 228 ? -6.722  -6.596  0.345   1.00 12.57 ? 229 LEU A CD2 1 
ATOM   1881 N  N   . ASN A 1 229 ? -2.480  -8.061  0.418   1.00 14.40 ? 230 ASN A N   1 
ATOM   1882 C  CA  . ASN A 1 229 ? -1.058  -8.122  0.359   1.00 13.27 ? 230 ASN A CA  1 
ATOM   1883 C  C   . ASN A 1 229 ? -0.484  -6.990  1.223   1.00 14.08 ? 230 ASN A C   1 
ATOM   1884 O  O   . ASN A 1 229 ? -1.009  -5.870  1.169   1.00 13.87 ? 230 ASN A O   1 
ATOM   1885 C  CB  . ASN A 1 229 ? -0.600  -7.857  -1.081  1.00 14.63 ? 230 ASN A CB  1 
ATOM   1886 C  CG  . ASN A 1 229 ? -0.684  -9.090  -2.020  1.00 18.27 ? 230 ASN A CG  1 
ATOM   1887 O  OD1 . ASN A 1 229 ? -0.221  -8.981  -3.177  1.00 19.81 ? 230 ASN A OD1 1 
ATOM   1888 N  ND2 . ASN A 1 229 ? -1.217  -10.240 -1.549  1.00 14.07 ? 230 ASN A ND2 1 
ATOM   1889 N  N   . PHE A 1 230 ? 0.557   -7.291  1.986   1.00 12.80 ? 231 PHE A N   1 
ATOM   1890 C  CA  . PHE A 1 230 ? 1.298   -6.206  2.680   1.00 13.26 ? 231 PHE A CA  1 
ATOM   1891 C  C   . PHE A 1 230 ? 2.216   -5.476  1.664   1.00 15.21 ? 231 PHE A C   1 
ATOM   1892 O  O   . PHE A 1 230 ? 2.647   -4.348  1.930   1.00 16.07 ? 231 PHE A O   1 
ATOM   1893 C  CB  . PHE A 1 230 ? 2.309   -6.700  3.649   1.00 14.75 ? 231 PHE A CB  1 
ATOM   1894 C  CG  . PHE A 1 230 ? 1.750   -7.306  4.956   1.00 14.75 ? 231 PHE A CG  1 
ATOM   1895 C  CD1 . PHE A 1 230 ? 0.884   -6.565  5.801   1.00 13.87 ? 231 PHE A CD1 1 
ATOM   1896 C  CD2 . PHE A 1 230 ? 2.157   -8.613  5.304   1.00 11.46 ? 231 PHE A CD2 1 
ATOM   1897 C  CE1 . PHE A 1 230 ? 0.390   -7.128  7.062   1.00 14.77 ? 231 PHE A CE1 1 
ATOM   1898 C  CE2 . PHE A 1 230 ? 1.713   -9.232  6.552   1.00 13.26 ? 231 PHE A CE2 1 
ATOM   1899 C  CZ  . PHE A 1 230 ? 0.823   -8.481  7.435   1.00 12.70 ? 231 PHE A CZ  1 
ATOM   1900 N  N   . ASN A 1 231 ? 2.624   -6.152  0.619   1.00 17.24 ? 232 ASN A N   1 
ATOM   1901 C  CA  . ASN A 1 231 ? 3.538   -5.476  -0.339  1.00 18.31 ? 232 ASN A CA  1 
ATOM   1902 C  C   . ASN A 1 231 ? 2.792   -4.546  -1.322  1.00 18.29 ? 232 ASN A C   1 
ATOM   1903 O  O   . ASN A 1 231 ? 1.551   -4.689  -1.507  1.00 16.17 ? 232 ASN A O   1 
ATOM   1904 C  CB  . ASN A 1 231 ? 4.229   -6.583  -1.081  1.00 19.08 ? 232 ASN A CB  1 
ATOM   1905 C  CG  . ASN A 1 231 ? 3.219   -7.477  -1.750  1.00 20.29 ? 232 ASN A CG  1 
ATOM   1906 O  OD1 . ASN A 1 231 ? 2.639   -8.350  -1.100  1.00 23.20 ? 232 ASN A OD1 1 
ATOM   1907 N  ND2 . ASN A 1 231 ? 2.965   -7.238  -3.039  1.00 20.79 ? 232 ASN A ND2 1 
ATOM   1908 N  N   . GLY A 1 232 ? 3.529   -3.625  -2.008  1.00 16.94 ? 233 GLY A N   1 
ATOM   1909 C  CA  . GLY A 1 232 ? 2.903   -2.829  -3.123  1.00 19.10 ? 233 GLY A CA  1 
ATOM   1910 C  C   . GLY A 1 232 ? 2.930   -3.635  -4.405  1.00 19.42 ? 233 GLY A C   1 
ATOM   1911 O  O   . GLY A 1 232 ? 3.684   -4.611  -4.471  1.00 20.65 ? 233 GLY A O   1 
ATOM   1912 N  N   . GLU A 1 233 ? 2.115   -3.203  -5.384  1.00 19.22 ? 234 GLU A N   1 
ATOM   1913 C  CA  . GLU A 1 233 ? 2.001   -3.768  -6.694  1.00 20.97 ? 234 GLU A CA  1 
ATOM   1914 C  C   . GLU A 1 233 ? 3.397   -3.848  -7.328  1.00 22.63 ? 234 GLU A C   1 
ATOM   1915 O  O   . GLU A 1 233 ? 4.226   -2.942  -7.197  1.00 20.72 ? 234 GLU A O   1 
ATOM   1916 C  CB  . GLU A 1 233 ? 1.112   -2.869  -7.530  1.00 20.21 ? 234 GLU A CB  1 
ATOM   1917 C  CG  . GLU A 1 233 ? 0.882   -3.350  -8.960  1.00 23.44 ? 234 GLU A CG  1 
ATOM   1918 C  CD  . GLU A 1 233 ? 0.008   -2.422  -9.760  1.00 28.51 ? 234 GLU A CD  1 
ATOM   1919 O  OE1 . GLU A 1 233 ? -0.381  -1.305  -9.253  1.00 30.96 ? 234 GLU A OE1 1 
ATOM   1920 O  OE2 . GLU A 1 233 ? -0.224  -2.748  -10.958 1.00 27.07 ? 234 GLU A OE2 1 
ATOM   1921 N  N   . GLY A 1 234 ? 3.637   -4.956  -8.011  1.00 24.31 ? 235 GLY A N   1 
ATOM   1922 C  CA  . GLY A 1 234 ? 4.948   -5.164  -8.590  1.00 26.63 ? 235 GLY A CA  1 
ATOM   1923 C  C   . GLY A 1 234 ? 6.042   -5.535  -7.617  1.00 26.03 ? 235 GLY A C   1 
ATOM   1924 O  O   . GLY A 1 234 ? 7.210   -5.405  -7.956  1.00 26.64 ? 235 GLY A O   1 
ATOM   1925 N  N   . GLU A 1 235 ? 5.682   -5.956  -6.400  1.00 25.84 ? 236 GLU A N   1 
ATOM   1926 C  CA  . GLU A 1 235 ? 6.671   -6.493  -5.418  1.00 23.76 ? 236 GLU A CA  1 
ATOM   1927 C  C   . GLU A 1 235 ? 6.231   -7.919  -5.095  1.00 24.94 ? 236 GLU A C   1 
ATOM   1928 O  O   . GLU A 1 235 ? 5.114   -8.310  -5.458  1.00 24.82 ? 236 GLU A O   1 
ATOM   1929 C  CB  . GLU A 1 235 ? 6.711   -5.686  -4.123  1.00 24.96 ? 236 GLU A CB  1 
ATOM   1930 C  CG  . GLU A 1 235 ? 7.177   -4.297  -4.343  1.00 26.81 ? 236 GLU A CG  1 
ATOM   1931 C  CD  . GLU A 1 235 ? 6.896   -3.428  -3.154  1.00 31.41 ? 236 GLU A CD  1 
ATOM   1932 O  OE1 . GLU A 1 235 ? 6.200   -3.874  -2.209  1.00 28.97 ? 236 GLU A OE1 1 
ATOM   1933 O  OE2 . GLU A 1 235 ? 7.363   -2.276  -3.135  1.00 28.37 ? 236 GLU A OE2 1 
ATOM   1934 N  N   . PRO A 1 236 ? 7.133   -8.702  -4.498  1.00 22.59 ? 237 PRO A N   1 
ATOM   1935 C  CA  . PRO A 1 236 ? 6.810   -10.114 -4.295  1.00 23.62 ? 237 PRO A CA  1 
ATOM   1936 C  C   . PRO A 1 236 ? 5.696   -10.194 -3.255  1.00 22.71 ? 237 PRO A C   1 
ATOM   1937 O  O   . PRO A 1 236 ? 5.608   -9.321  -2.367  1.00 19.49 ? 237 PRO A O   1 
ATOM   1938 C  CB  . PRO A 1 236 ? 8.119   -10.717 -3.760  1.00 24.23 ? 237 PRO A CB  1 
ATOM   1939 C  CG  . PRO A 1 236 ? 9.182   -9.756  -4.164  1.00 25.28 ? 237 PRO A CG  1 
ATOM   1940 C  CD  . PRO A 1 236 ? 8.509   -8.407  -4.038  1.00 25.91 ? 237 PRO A CD  1 
ATOM   1941 N  N   . GLU A 1 237 ? 4.871   -11.225 -3.411  1.00 21.59 ? 238 GLU A N   1 
ATOM   1942 C  CA  . GLU A 1 237 ? 3.663   -11.253 -2.668  1.00 19.39 ? 238 GLU A CA  1 
ATOM   1943 C  C   . GLU A 1 237 ? 3.978   -11.678 -1.216  1.00 19.84 ? 238 GLU A C   1 
ATOM   1944 O  O   . GLU A 1 237 ? 4.570   -12.722 -0.967  1.00 16.36 ? 238 GLU A O   1 
ATOM   1945 C  CB  . GLU A 1 237 ? 2.617   -12.168 -3.307  1.00 20.22 ? 238 GLU A CB  1 
ATOM   1946 C  CG  . GLU A 1 237 ? 1.354   -12.206 -2.506  1.00 19.33 ? 238 GLU A CG  1 
ATOM   1947 C  CD  . GLU A 1 237 ? 0.253   -12.910 -3.231  1.00 22.59 ? 238 GLU A CD  1 
ATOM   1948 O  OE1 . GLU A 1 237 ? 0.615   -14.011 -3.793  1.00 26.39 ? 238 GLU A OE1 1 
ATOM   1949 O  OE2 . GLU A 1 237 ? -0.909  -12.389 -3.331  1.00 17.13 ? 238 GLU A OE2 1 
ATOM   1950 N  N   . GLU A 1 238 ? 3.492   -10.848 -0.288  1.00 17.65 ? 239 GLU A N   1 
ATOM   1951 C  CA  . GLU A 1 238 ? 3.560   -11.134 1.125   1.00 19.07 ? 239 GLU A CA  1 
ATOM   1952 C  C   . GLU A 1 238 ? 2.108   -11.086 1.579   1.00 14.10 ? 239 GLU A C   1 
ATOM   1953 O  O   . GLU A 1 238 ? 1.503   -10.011 1.557   1.00 14.26 ? 239 GLU A O   1 
ATOM   1954 C  CB  . GLU A 1 238 ? 4.294   -10.017 1.887   1.00 16.91 ? 239 GLU A CB  1 
ATOM   1955 C  CG  . GLU A 1 238 ? 5.546   -9.471  1.253   1.00 24.75 ? 239 GLU A CG  1 
ATOM   1956 C  CD  . GLU A 1 238 ? 5.929   -8.066  1.838   1.00 26.44 ? 239 GLU A CD  1 
ATOM   1957 O  OE1 . GLU A 1 238 ? 5.618   -7.772  3.029   1.00 29.66 ? 239 GLU A OE1 1 
ATOM   1958 O  OE2 . GLU A 1 238 ? 6.495   -7.262  1.067   1.00 35.51 ? 239 GLU A OE2 1 
ATOM   1959 N  N   . LEU A 1 239 ? 1.476   -12.235 1.881   1.00 13.81 ? 240 LEU A N   1 
ATOM   1960 C  CA  . LEU A 1 239 ? 0.038   -12.123 2.206   1.00 11.03 ? 240 LEU A CA  1 
ATOM   1961 C  C   . LEU A 1 239 ? -0.159  -11.278 3.521   1.00 9.34  ? 240 LEU A C   1 
ATOM   1962 O  O   . LEU A 1 239 ? 0.626   -11.425 4.493   1.00 12.88 ? 240 LEU A O   1 
ATOM   1963 C  CB  . LEU A 1 239 ? -0.580  -13.520 2.461   1.00 12.39 ? 240 LEU A CB  1 
ATOM   1964 C  CG  . LEU A 1 239 ? -0.659  -14.433 1.196   1.00 11.16 ? 240 LEU A CG  1 
ATOM   1965 C  CD1 . LEU A 1 239 ? -1.181  -15.769 1.655   1.00 20.83 ? 240 LEU A CD1 1 
ATOM   1966 C  CD2 . LEU A 1 239 ? -1.514  -13.810 0.057   1.00 15.08 ? 240 LEU A CD2 1 
ATOM   1967 N  N   . MET A 1 240 ? -1.233  -10.512 3.493   1.00 11.91 ? 241 MET A N   1 
ATOM   1968 C  CA  . MET A 1 240 ? -1.602  -9.667  4.635   1.00 12.07 ? 241 MET A CA  1 
ATOM   1969 C  C   . MET A 1 240 ? -2.359  -10.597 5.621   1.00 10.69 ? 241 MET A C   1 
ATOM   1970 O  O   . MET A 1 240 ? -3.534  -10.745 5.522   1.00 11.62 ? 241 MET A O   1 
ATOM   1971 C  CB  . MET A 1 240 ? -2.470  -8.492  4.217   1.00 12.61 ? 241 MET A CB  1 
ATOM   1972 C  CG  . MET A 1 240 ? -2.825  -7.451  5.434   1.00 12.98 ? 241 MET A CG  1 
ATOM   1973 S  SD  . MET A 1 240 ? -3.774  -6.100  4.846   1.00 16.33 ? 241 MET A SD  1 
ATOM   1974 C  CE  . MET A 1 240 ? -2.508  -4.982  4.155   1.00 15.97 ? 241 MET A CE  1 
ATOM   1975 N  N   . VAL A 1 241 ? -1.573  -11.251 6.492   1.00 9.94  ? 242 VAL A N   1 
ATOM   1976 C  CA  . VAL A 1 241 ? -2.173  -12.108 7.596   1.00 10.49 ? 242 VAL A CA  1 
ATOM   1977 C  C   . VAL A 1 241 ? -1.345  -11.831 8.882   1.00 10.38 ? 242 VAL A C   1 
ATOM   1978 O  O   . VAL A 1 241 ? -0.108  -11.448 8.789   1.00 9.62  ? 242 VAL A O   1 
ATOM   1979 C  CB  . VAL A 1 241 ? -2.064  -13.597 7.228   1.00 9.91  ? 242 VAL A CB  1 
ATOM   1980 C  CG1 . VAL A 1 241 ? -2.986  -13.864 5.928   1.00 9.68  ? 242 VAL A CG1 1 
ATOM   1981 C  CG2 . VAL A 1 241 ? -0.551  -14.046 7.124   1.00 9.75  ? 242 VAL A CG2 1 
ATOM   1982 N  N   . ASP A 1 242 ? -1.929  -12.121 10.051  1.00 7.41  ? 243 ASP A N   1 
ATOM   1983 C  CA  . ASP A 1 242 ? -1.217  -12.009 11.305  1.00 7.22  ? 243 ASP A CA  1 
ATOM   1984 C  C   . ASP A 1 242 ? -0.761  -10.565 11.511  1.00 6.41  ? 243 ASP A C   1 
ATOM   1985 O  O   . ASP A 1 242 ? 0.315   -10.337 12.018  1.00 10.42 ? 243 ASP A O   1 
ATOM   1986 C  CB  . ASP A 1 242 ? -0.142  -13.071 11.595  1.00 8.19  ? 243 ASP A CB  1 
ATOM   1987 C  CG  . ASP A 1 242 ? -0.738  -14.489 11.631  1.00 11.84 ? 243 ASP A CG  1 
ATOM   1988 O  OD1 . ASP A 1 242 ? -1.821  -14.659 12.232  1.00 9.31  ? 243 ASP A OD1 1 
ATOM   1989 O  OD2 . ASP A 1 242 ? -0.126  -15.411 11.011  1.00 11.29 ? 243 ASP A OD2 1 
ATOM   1990 N  N   . ASN A 1 243 ? -1.698  -9.643  11.236  1.00 7.25  ? 244 ASN A N   1 
ATOM   1991 C  CA  . ASN A 1 243 ? -1.360  -8.216  11.482  1.00 8.27  ? 244 ASN A CA  1 
ATOM   1992 C  C   . ASN A 1 243 ? -1.985  -7.793  12.837  1.00 8.35  ? 244 ASN A C   1 
ATOM   1993 O  O   . ASN A 1 243 ? -2.654  -6.708  12.862  1.00 8.26  ? 244 ASN A O   1 
ATOM   1994 C  CB  . ASN A 1 243 ? -1.870  -7.352  10.311  1.00 10.13 ? 244 ASN A CB  1 
ATOM   1995 C  CG  . ASN A 1 243 ? -3.414  -7.526  10.064  1.00 8.72  ? 244 ASN A CG  1 
ATOM   1996 O  OD1 . ASN A 1 243 ? -4.068  -8.366  10.731  1.00 10.14 ? 244 ASN A OD1 1 
ATOM   1997 N  ND2 . ASN A 1 243 ? -4.019  -6.635  9.191   1.00 14.13 ? 244 ASN A ND2 1 
ATOM   1998 N  N   . TRP A 1 244 ? -1.684  -8.554  13.880  1.00 7.93  ? 245 TRP A N   1 
ATOM   1999 C  CA  . TRP A 1 244 ? -2.166  -8.295  15.226  1.00 7.04  ? 245 TRP A CA  1 
ATOM   2000 C  C   . TRP A 1 244 ? -0.974  -8.161  16.133  1.00 9.49  ? 245 TRP A C   1 
ATOM   2001 O  O   . TRP A 1 244 ? 0.101   -8.864  15.953  1.00 8.74  ? 245 TRP A O   1 
ATOM   2002 C  CB  . TRP A 1 244 ? -3.116  -9.472  15.734  1.00 7.81  ? 245 TRP A CB  1 
ATOM   2003 C  CG  . TRP A 1 244 ? -2.616  -10.820 15.540  1.00 7.88  ? 245 TRP A CG  1 
ATOM   2004 C  CD1 . TRP A 1 244 ? -2.758  -11.563 14.379  1.00 9.32  ? 245 TRP A CD1 1 
ATOM   2005 C  CD2 . TRP A 1 244 ? -2.080  -11.680 16.516  1.00 7.40  ? 245 TRP A CD2 1 
ATOM   2006 N  NE1 . TRP A 1 244 ? -2.212  -12.841 14.581  1.00 9.65  ? 245 TRP A NE1 1 
ATOM   2007 C  CE2 . TRP A 1 244 ? -1.820  -12.924 15.886  1.00 7.78  ? 245 TRP A CE2 1 
ATOM   2008 C  CE3 . TRP A 1 244 ? -1.795  -11.556 17.887  1.00 8.53  ? 245 TRP A CE3 1 
ATOM   2009 C  CZ2 . TRP A 1 244 ? -1.215  -13.997 16.581  1.00 9.06  ? 245 TRP A CZ2 1 
ATOM   2010 C  CZ3 . TRP A 1 244 ? -1.186  -12.647 18.580  1.00 9.49  ? 245 TRP A CZ3 1 
ATOM   2011 C  CH2 . TRP A 1 244 ? -0.945  -13.819 17.933  1.00 8.58  ? 245 TRP A CH2 1 
ATOM   2012 N  N   . ARG A 1 245 ? -1.103  -7.259  17.125  1.00 6.13  ? 246 ARG A N   1 
ATOM   2013 C  CA  . ARG A 1 245 ? -0.133  -7.184  18.212  1.00 7.57  ? 246 ARG A CA  1 
ATOM   2014 C  C   . ARG A 1 245 ? -0.616  -8.121  19.326  1.00 6.87  ? 246 ARG A C   1 
ATOM   2015 O  O   . ARG A 1 245 ? -1.802  -8.148  19.661  1.00 9.46  ? 246 ARG A O   1 
ATOM   2016 C  CB  . ARG A 1 245 ? -0.176  -5.713  18.745  1.00 7.47  ? 246 ARG A CB  1 
ATOM   2017 C  CG  . ARG A 1 245 ? 0.986   -5.553  19.766  1.00 4.90  ? 246 ARG A CG  1 
ATOM   2018 C  CD  . ARG A 1 245 ? 0.954   -4.132  20.371  1.00 7.67  ? 246 ARG A CD  1 
ATOM   2019 N  NE  . ARG A 1 245 ? 2.241   -3.858  21.118  1.00 12.17 ? 246 ARG A NE  1 
ATOM   2020 C  CZ  . ARG A 1 245 ? 2.473   -2.812  21.899  1.00 15.61 ? 246 ARG A CZ  1 
ATOM   2021 N  NH1 . ARG A 1 245 ? 1.470   -1.977  22.214  1.00 9.47  ? 246 ARG A NH1 1 
ATOM   2022 N  NH2 . ARG A 1 245 ? 3.694   -2.654  22.429  1.00 12.69 ? 246 ARG A NH2 1 
ATOM   2023 N  N   . PRO A 1 246 ? 0.262   -8.885  19.981  1.00 9.08  ? 247 PRO A N   1 
ATOM   2024 C  CA  . PRO A 1 246 ? -0.163  -9.735  21.115  1.00 7.97  ? 247 PRO A CA  1 
ATOM   2025 C  C   . PRO A 1 246 ? -0.441  -8.914  22.384  1.00 6.65  ? 247 PRO A C   1 
ATOM   2026 O  O   . PRO A 1 246 ? -0.101  -7.723  22.481  1.00 8.23  ? 247 PRO A O   1 
ATOM   2027 C  CB  . PRO A 1 246 ? 1.041   -10.627 21.438  1.00 10.29 ? 247 PRO A CB  1 
ATOM   2028 C  CG  . PRO A 1 246 ? 2.047   -10.230 20.443  1.00 12.56 ? 247 PRO A CG  1 
ATOM   2029 C  CD  . PRO A 1 246 ? 1.714   -8.993  19.681  1.00 11.34 ? 247 PRO A CD  1 
ATOM   2030 N  N   . ALA A 1 247 ? -1.068  -9.579  23.351  1.00 8.19  ? 248 ALA A N   1 
ATOM   2031 C  CA  . ALA A 1 247 ? -1.457  -8.979  24.600  1.00 6.86  ? 248 ALA A CA  1 
ATOM   2032 C  C   . ALA A 1 247 ? -0.189  -8.440  25.295  1.00 8.40  ? 248 ALA A C   1 
ATOM   2033 O  O   . ALA A 1 247 ? 0.909   -9.096  25.247  1.00 10.09 ? 248 ALA A O   1 
ATOM   2034 C  CB  . ALA A 1 247 ? -2.136  -10.064 25.463  1.00 8.96  ? 248 ALA A CB  1 
ATOM   2035 N  N   . GLN A 1 248 ? -0.351  -7.267  25.887  1.00 7.16  ? 249 GLN A N   1 
ATOM   2036 C  CA  . GLN A 1 248 ? 0.724   -6.555  26.607  1.00 7.92  ? 249 GLN A CA  1 
ATOM   2037 C  C   . GLN A 1 248 ? 0.399   -6.498  28.114  1.00 9.49  ? 249 GLN A C   1 
ATOM   2038 O  O   . GLN A 1 248 ? -0.759  -6.666  28.573  1.00 8.64  ? 249 GLN A O   1 
ATOM   2039 C  CB  . GLN A 1 248 ? 0.770   -5.121  26.036  1.00 9.97  ? 249 GLN A CB  1 
ATOM   2040 C  CG  . GLN A 1 248 ? 1.062   -5.051  24.556  1.00 5.48  ? 249 GLN A CG  1 
ATOM   2041 C  CD  . GLN A 1 248 ? 2.395   -5.669  24.201  1.00 13.02 ? 249 GLN A CD  1 
ATOM   2042 O  OE1 . GLN A 1 248 ? 3.456   -5.357  24.815  1.00 14.02 ? 249 GLN A OE1 1 
ATOM   2043 N  NE2 . GLN A 1 248 ? 2.349   -6.656  23.286  1.00 12.57 ? 249 GLN A NE2 1 
ATOM   2044 N  N   . PRO A 1 249 ? 1.410   -6.227  28.955  1.00 9.17  ? 250 PRO A N   1 
ATOM   2045 C  CA  . PRO A 1 249 ? 1.199   -6.264  30.392  1.00 11.14 ? 250 PRO A CA  1 
ATOM   2046 C  C   . PRO A 1 249 ? 0.157   -5.244  30.850  1.00 8.10  ? 250 PRO A C   1 
ATOM   2047 O  O   . PRO A 1 249 ? 0.188   -4.086  30.440  1.00 10.77 ? 250 PRO A O   1 
ATOM   2048 C  CB  . PRO A 1 249 ? 2.595   -5.798  30.955  1.00 12.31 ? 250 PRO A CB  1 
ATOM   2049 C  CG  . PRO A 1 249 ? 3.552   -6.070  29.920  1.00 15.25 ? 250 PRO A CG  1 
ATOM   2050 C  CD  . PRO A 1 249 ? 2.793   -6.011  28.573  1.00 12.08 ? 250 PRO A CD  1 
ATOM   2051 N  N   . LEU A 1 250 ? -0.724  -5.723  31.721  1.00 10.08 ? 251 LEU A N   1 
ATOM   2052 C  CA  . LEU A 1 250 ? -1.805  -4.905  32.199  1.00 10.15 ? 251 LEU A CA  1 
ATOM   2053 C  C   . LEU A 1 250 ? -1.234  -3.791  33.120  1.00 11.13 ? 251 LEU A C   1 
ATOM   2054 O  O   . LEU A 1 250 ? -1.737  -2.658  33.166  1.00 9.68  ? 251 LEU A O   1 
ATOM   2055 C  CB  . LEU A 1 250 ? -2.826  -5.764  32.884  1.00 11.03 ? 251 LEU A CB  1 
ATOM   2056 C  CG  . LEU A 1 250 ? -4.083  -5.018  33.395  1.00 10.67 ? 251 LEU A CG  1 
ATOM   2057 C  CD1 . LEU A 1 250 ? -4.847  -4.397  32.190  1.00 13.33 ? 251 LEU A CD1 1 
ATOM   2058 C  CD2 . LEU A 1 250 ? -5.025  -6.030  34.211  1.00 14.90 ? 251 LEU A CD2 1 
ATOM   2059 N  N   . LYS A 1 251 ? -0.161  -4.117  33.858  1.00 12.03 ? 252 LYS A N   1 
ATOM   2060 C  CA  . LYS A 1 251 ? 0.470   -3.036  34.750  1.00 12.56 ? 252 LYS A CA  1 
ATOM   2061 C  C   . LYS A 1 251 ? -0.560  -2.404  35.722  1.00 13.89 ? 252 LYS A C   1 
ATOM   2062 O  O   . LYS A 1 251 ? -0.593  -1.172  35.945  1.00 15.71 ? 252 LYS A O   1 
ATOM   2063 C  CB  . LYS A 1 251 ? 1.237   -2.009  33.902  1.00 13.28 ? 252 LYS A CB  1 
ATOM   2064 C  CG  . LYS A 1 251 ? 2.457   -2.736  33.215  1.00 17.99 ? 252 LYS A CG  1 
ATOM   2065 C  CD  . LYS A 1 251 ? 3.401   -1.781  32.564  1.00 20.40 ? 252 LYS A CD  1 
ATOM   2066 C  CE  . LYS A 1 251 ? 4.538   -2.539  32.103  1.00 22.11 ? 252 LYS A CE  1 
ATOM   2067 N  NZ  . LYS A 1 251 ? 5.141   -1.676  31.143  1.00 21.81 ? 252 LYS A NZ  1 
ATOM   2068 N  N   . ASN A 1 252 ? -1.384  -3.285  36.273  1.00 15.14 ? 253 ASN A N   1 
ATOM   2069 C  CA  . ASN A 1 252 ? -2.352  -2.925  37.346  1.00 20.77 ? 253 ASN A CA  1 
ATOM   2070 C  C   . ASN A 1 252 ? -3.513  -1.992  37.047  1.00 20.62 ? 253 ASN A C   1 
ATOM   2071 O  O   . ASN A 1 252 ? -4.335  -1.669  37.993  1.00 23.72 ? 253 ASN A O   1 
ATOM   2072 C  CB  . ASN A 1 252 ? -1.625  -2.276  38.514  1.00 21.32 ? 253 ASN A CB  1 
ATOM   2073 C  CG  . ASN A 1 252 ? -0.888  -3.283  39.335  1.00 28.05 ? 253 ASN A CG  1 
ATOM   2074 O  OD1 . ASN A 1 252 ? -1.480  -4.281  39.846  1.00 34.77 ? 253 ASN A OD1 1 
ATOM   2075 N  ND2 . ASN A 1 252 ? 0.442   -3.088  39.429  1.00 32.20 ? 253 ASN A ND2 1 
ATOM   2076 N  N   . ARG A 1 253 ? -3.559  -1.502  35.809  1.00 15.64 ? 254 ARG A N   1 
ATOM   2077 C  CA  . ARG A 1 253 ? -4.815  -0.943  35.305  1.00 12.75 ? 254 ARG A CA  1 
ATOM   2078 C  C   . ARG A 1 253 ? -5.927  -1.913  35.659  1.00 13.55 ? 254 ARG A C   1 
ATOM   2079 O  O   . ARG A 1 253 ? -5.676  -3.094  35.862  1.00 14.86 ? 254 ARG A O   1 
ATOM   2080 C  CB  . ARG A 1 253 ? -4.780  -0.801  33.749  1.00 13.29 ? 254 ARG A CB  1 
ATOM   2081 C  CG  . ARG A 1 253 ? -3.770  0.277   33.231  1.00 8.92  ? 254 ARG A CG  1 
ATOM   2082 C  CD  . ARG A 1 253 ? -3.748  0.190   31.740  1.00 9.73  ? 254 ARG A CD  1 
ATOM   2083 N  NE  . ARG A 1 253 ? -2.881  -0.977  31.292  1.00 8.92  ? 254 ARG A NE  1 
ATOM   2084 C  CZ  . ARG A 1 253 ? -2.629  -1.232  29.995  1.00 8.23  ? 254 ARG A CZ  1 
ATOM   2085 N  NH1 . ARG A 1 253 ? -3.222  -0.471  29.049  1.00 8.51  ? 254 ARG A NH1 1 
ATOM   2086 N  NH2 . ARG A 1 253 ? -1.803  -2.230  29.677  1.00 8.35  ? 254 ARG A NH2 1 
ATOM   2087 N  N   A GLN A 1 254 ? -7.145  -1.401  35.765  0.50 11.65 ? 255 GLN A N   1 
ATOM   2088 N  N   B GLN A 1 254 ? -7.134  -1.363  35.802  0.50 11.50 ? 255 GLN A N   1 
ATOM   2089 C  CA  A GLN A 1 254 ? -8.317  -2.245  36.054  0.50 13.23 ? 255 GLN A CA  1 
ATOM   2090 C  CA  B GLN A 1 254 ? -8.383  -2.120  36.044  0.50 12.95 ? 255 GLN A CA  1 
ATOM   2091 C  C   A GLN A 1 254 ? -9.293  -2.169  34.888  0.50 12.50 ? 255 GLN A C   1 
ATOM   2092 C  C   B GLN A 1 254 ? -9.124  -2.165  34.715  0.50 12.24 ? 255 GLN A C   1 
ATOM   2093 O  O   A GLN A 1 254 ? -9.734  -1.057  34.447  0.50 11.84 ? 255 GLN A O   1 
ATOM   2094 O  O   B GLN A 1 254 ? -9.236  -1.115  33.995  0.50 11.32 ? 255 GLN A O   1 
ATOM   2095 C  CB  A GLN A 1 254 ? -9.032  -1.800  37.320  0.50 14.60 ? 255 GLN A CB  1 
ATOM   2096 C  CB  B GLN A 1 254 ? -9.307  -1.443  37.098  0.50 14.04 ? 255 GLN A CB  1 
ATOM   2097 C  CG  A GLN A 1 254 ? -9.554  -2.927  38.174  0.50 18.31 ? 255 GLN A CG  1 
ATOM   2098 C  CG  B GLN A 1 254 ? -8.900  -1.678  38.529  0.50 17.74 ? 255 GLN A CG  1 
ATOM   2099 C  CD  A GLN A 1 254 ? -10.346 -2.384  39.324  0.50 24.69 ? 255 GLN A CD  1 
ATOM   2100 C  CD  B GLN A 1 254 ? -7.560  -1.144  38.842  0.50 20.56 ? 255 GLN A CD  1 
ATOM   2101 O  OE1 A GLN A 1 254 ? -9.863  -1.510  40.075  0.50 28.34 ? 255 GLN A OE1 1 
ATOM   2102 O  OE1 B GLN A 1 254 ? -7.192  -0.015  38.452  0.50 24.26 ? 255 GLN A OE1 1 
ATOM   2103 N  NE2 A GLN A 1 254 ? -11.600 -2.837  39.448  0.50 23.72 ? 255 GLN A NE2 1 
ATOM   2104 N  NE2 B GLN A 1 254 ? -6.773  -1.956  39.567  0.50 23.49 ? 255 GLN A NE2 1 
ATOM   2105 N  N   . ILE A 1 255 ? -9.632  -3.361  34.392  1.00 11.31 ? 256 ILE A N   1 
ATOM   2106 C  CA  . ILE A 1 255 ? -10.641 -3.495  33.347  1.00 10.62 ? 256 ILE A CA  1 
ATOM   2107 C  C   . ILE A 1 255 ? -12.028 -3.576  34.047  1.00 9.89  ? 256 ILE A C   1 
ATOM   2108 O  O   . ILE A 1 255 ? -12.213 -4.296  35.012  1.00 10.48 ? 256 ILE A O   1 
ATOM   2109 C  CB  . ILE A 1 255 ? -10.378 -4.808  32.513  1.00 11.17 ? 256 ILE A CB  1 
ATOM   2110 C  CG1 . ILE A 1 255 ? -8.983  -4.700  31.867  1.00 11.61 ? 256 ILE A CG1 1 
ATOM   2111 C  CG2 . ILE A 1 255 ? -11.503 -5.063  31.473  1.00 9.93  ? 256 ILE A CG2 1 
ATOM   2112 C  CD1 . ILE A 1 255 ? -8.626  -6.031  31.138  1.00 12.79 ? 256 ILE A CD1 1 
ATOM   2113 N  N   . LYS A 1 256 ? -12.901 -2.692  33.628  1.00 10.10 ? 257 LYS A N   1 
ATOM   2114 C  CA  . LYS A 1 256 ? -14.286 -2.568  34.172  1.00 11.23 ? 257 LYS A CA  1 
ATOM   2115 C  C   . LYS A 1 256 ? -15.231 -3.189  33.205  1.00 10.46 ? 257 LYS A C   1 
ATOM   2116 O  O   . LYS A 1 256 ? -15.022 -3.109  31.986  1.00 9.81  ? 257 LYS A O   1 
ATOM   2117 C  CB  . LYS A 1 256 ? -14.600 -1.054  34.443  1.00 11.19 ? 257 LYS A CB  1 
ATOM   2118 C  CG  . LYS A 1 256 ? -13.637 -0.498  35.532  1.00 15.17 ? 257 LYS A CG  1 
ATOM   2119 C  CD  . LYS A 1 256 ? -13.742 1.012   35.655  1.00 19.73 ? 257 LYS A CD  1 
ATOM   2120 C  CE  . LYS A 1 256 ? -12.740 1.586   36.805  1.00 22.56 ? 257 LYS A CE  1 
ATOM   2121 N  NZ  . LYS A 1 256 ? -12.889 3.119   36.841  1.00 25.83 ? 257 LYS A NZ  1 
ATOM   2122 N  N   . ALA A 1 257 ? -16.272 -3.847  33.717  1.00 10.60 ? 258 ALA A N   1 
ATOM   2123 C  CA  . ALA A 1 257 ? -17.350 -4.468  32.903  1.00 11.49 ? 258 ALA A CA  1 
ATOM   2124 C  C   . ALA A 1 257 ? -18.656 -3.735  33.099  1.00 9.49  ? 258 ALA A C   1 
ATOM   2125 O  O   . ALA A 1 257 ? -18.973 -3.308  34.249  1.00 10.45 ? 258 ALA A O   1 
ATOM   2126 C  CB  . ALA A 1 257 ? -17.532 -6.015  33.295  1.00 10.82 ? 258 ALA A CB  1 
ATOM   2127 N  N   . SER A 1 258 ? -19.388 -3.545  31.999  1.00 8.84  ? 259 SER A N   1 
ATOM   2128 C  CA  . SER A 1 258 ? -20.649 -2.838  31.993  1.00 12.82 ? 259 SER A CA  1 
ATOM   2129 C  C   . SER A 1 258 ? -21.776 -3.775  32.431  1.00 13.93 ? 259 SER A C   1 
ATOM   2130 O  O   . SER A 1 258 ? -22.916 -3.297  32.576  1.00 17.45 ? 259 SER A O   1 
ATOM   2131 C  CB  . SER A 1 258 ? -20.936 -2.280  30.602  1.00 13.31 ? 259 SER A CB  1 
ATOM   2132 O  OG  . SER A 1 258 ? -21.429 -3.249  29.692  1.00 12.98 ? 259 SER A OG  1 
ATOM   2133 N  N   . PHE A 1 259 ? -21.470 -5.040  32.628  1.00 15.30 ? 260 PHE A N   1 
ATOM   2134 C  CA  . PHE A 1 259 ? -22.479 -6.088  32.886  1.00 17.21 ? 260 PHE A CA  1 
ATOM   2135 C  C   . PHE A 1 259 ? -22.061 -6.989  34.054  1.00 19.93 ? 260 PHE A C   1 
ATOM   2136 O  O   . PHE A 1 259 ? -20.843 -7.163  34.350  1.00 17.15 ? 260 PHE A O   1 
ATOM   2137 C  CB  . PHE A 1 259 ? -22.709 -6.937  31.629  1.00 17.00 ? 260 PHE A CB  1 
ATOM   2138 C  CG  . PHE A 1 259 ? -21.429 -7.622  31.132  1.00 17.32 ? 260 PHE A CG  1 
ATOM   2139 C  CD1 . PHE A 1 259 ? -20.526 -6.882  30.378  1.00 15.17 ? 260 PHE A CD1 1 
ATOM   2140 C  CD2 . PHE A 1 259 ? -21.110 -8.926  31.498  1.00 18.73 ? 260 PHE A CD2 1 
ATOM   2141 C  CE1 . PHE A 1 259 ? -19.285 -7.436  29.983  1.00 20.13 ? 260 PHE A CE1 1 
ATOM   2142 C  CE2 . PHE A 1 259 ? -19.907 -9.495  31.093  1.00 19.85 ? 260 PHE A CE2 1 
ATOM   2143 C  CZ  . PHE A 1 259 ? -18.970 -8.739  30.333  1.00 20.56 ? 260 PHE A CZ  1 
ATOM   2144 N  N   . LYS A 1 260 ? -23.105 -7.573  34.687  1.00 24.47 ? 261 LYS A N   1 
ATOM   2145 C  CA  . LYS A 1 260 ? -23.038 -8.580  35.809  1.00 31.26 ? 261 LYS A CA  1 
ATOM   2146 C  C   . LYS A 1 260 ? -22.984 -8.043  37.293  1.00 33.94 ? 261 LYS A C   1 
ATOM   2147 O  O   . LYS A 1 260 ? -23.858 -7.255  37.715  1.00 35.77 ? 261 LYS A O   1 
ATOM   2148 C  CB  . LYS A 1 260 ? -21.948 -9.640  35.569  1.00 32.16 ? 261 LYS A CB  1 
ATOM   2149 C  CG  . LYS A 1 260 ? -22.391 -10.892 34.831  1.00 33.09 ? 261 LYS A CG  1 
ATOM   2150 C  CD  . LYS A 1 260 ? -23.380 -10.675 33.661  1.00 33.24 ? 261 LYS A CD  1 
ATOM   2151 C  CE  . LYS A 1 260 ? -23.439 -11.905 32.703  1.00 33.43 ? 261 LYS A CE  1 
ATOM   2152 N  NZ  . LYS A 1 260 ? -22.042 -12.516 32.460  1.00 36.33 ? 261 LYS A NZ  1 
ATOM   2153 O  OXT . LYS A 1 260 ? -22.100 -8.372  38.119  1.00 36.28 ? 261 LYS A OXT 1 
HETATM 2154 ZN ZN  . ZN  B 2 .   ? -6.644  -1.691  15.269  1.00 8.02  ? 262 ZN  A ZN  1 
HETATM 2155 N  N1  . BCN C 3 .   ? -20.538 -14.585 23.151  1.00 26.62 ? 263 BCN A N1  1 
HETATM 2156 C  C1  . BCN C 3 .   ? -20.036 -15.651 22.370  1.00 20.51 ? 263 BCN A C1  1 
HETATM 2157 C  C2  . BCN C 3 .   ? -20.628 -16.159 21.075  1.00 36.27 ? 263 BCN A C2  1 
HETATM 2158 O  O21 . BCN C 3 .   ? -19.900 -16.767 20.337  1.00 41.28 ? 263 BCN A O21 1 
HETATM 2159 O  O22 . BCN C 3 .   ? -21.795 -15.791 20.559  1.00 40.88 ? 263 BCN A O22 1 
HETATM 2160 C  C3  . BCN C 3 .   ? -21.613 -13.752 23.036  1.00 17.63 ? 263 BCN A C3  1 
HETATM 2161 C  C4  . BCN C 3 .   ? -22.765 -13.350 23.841  1.00 33.47 ? 263 BCN A C4  1 
HETATM 2162 O  O4  . BCN C 3 .   ? -22.249 -12.392 24.792  1.00 28.43 ? 263 BCN A O4  1 
HETATM 2163 C  C5  . BCN C 3 .   ? -19.789 -14.079 24.290  1.00 24.52 ? 263 BCN A C5  1 
HETATM 2164 C  C6  . BCN C 3 .   ? -20.088 -15.201 25.275  1.00 26.93 ? 263 BCN A C6  1 
HETATM 2165 O  O6  . BCN C 3 .   ? -19.345 -15.007 26.392  1.00 23.73 ? 263 BCN A O6  1 
HETATM 2166 S  S   . DMS D 4 .   ? 1.347   -11.648 14.898  1.00 28.46 ? 264 DMS A S   1 
HETATM 2167 O  O   . DMS D 4 .   ? 1.920   -13.301 14.542  1.00 27.86 ? 264 DMS A O   1 
HETATM 2168 C  C1  . DMS D 4 .   ? 1.708   -11.341 16.632  1.00 24.73 ? 264 DMS A C1  1 
HETATM 2169 C  C2  . DMS D 4 .   ? 2.555   -10.590 14.002  1.00 26.75 ? 264 DMS A C2  1 
HETATM 2170 S  S   . DMS E 4 .   ? -6.322  6.984   11.531  1.00 56.28 ? 265 DMS A S   1 
HETATM 2171 O  O   . DMS E 4 .   ? -6.529  5.768   10.207  1.00 55.78 ? 265 DMS A O   1 
HETATM 2172 C  C1  . DMS E 4 .   ? -6.027  8.614   10.734  1.00 55.14 ? 265 DMS A C1  1 
HETATM 2173 C  C2  . DMS E 4 .   ? -7.879  7.253   12.415  1.00 56.09 ? 265 DMS A C2  1 
HETATM 2174 N  N1  . E65 F 5 .   ? -1.356  9.012   11.460  1.00 36.13 ? 266 E65 A N1  1 
HETATM 2175 C  C2  . E65 F 5 .   ? -1.544  7.850   12.112  1.00 34.37 ? 266 E65 A C2  1 
HETATM 2176 N  N3  . E65 F 5 .   ? -1.442  7.954   13.436  1.00 36.45 ? 266 E65 A N3  1 
HETATM 2177 C  C4  . E65 F 5 .   ? -1.190  9.005   14.149  1.00 36.88 ? 266 E65 A C4  1 
HETATM 2178 C  C5  . E65 F 5 .   ? -1.002  10.241  13.511  1.00 38.62 ? 266 E65 A C5  1 
HETATM 2179 C  C6  . E65 F 5 .   ? -1.094  10.192  12.125  1.00 37.81 ? 266 E65 A C6  1 
HETATM 2180 S  S7  . E65 F 5 .   ? -1.887  6.179   11.453  1.00 35.91 ? 266 E65 A S7  1 
HETATM 2181 C  C8  . E65 F 5 .   ? -2.045  5.178   12.948  1.00 27.81 ? 266 E65 A C8  1 
HETATM 2182 C  C9  . E65 F 5 .   ? -3.503  5.249   13.333  1.00 21.73 ? 266 E65 A C9  1 
HETATM 2183 O  O10 . E65 F 5 .   ? -4.195  6.099   12.809  1.00 23.52 ? 266 E65 A O10 1 
HETATM 2184 C  C11 . E65 F 5 .   ? -1.136  8.732   15.579  1.00 35.50 ? 266 E65 A C11 1 
HETATM 2185 C  C12 . E65 F 5 .   ? -0.898  11.497  11.390  1.00 38.48 ? 266 E65 A C12 1 
HETATM 2186 C  C13 . E65 F 5 .   ? -4.180  4.236   14.217  1.00 18.72 ? 266 E65 A C13 1 
HETATM 2187 C  C14 . E65 F 5 .   ? -3.395  3.179   14.578  1.00 17.02 ? 266 E65 A C14 1 
HETATM 2188 C  C15 . E65 F 5 .   ? -3.921  2.182   15.431  1.00 14.73 ? 266 E65 A C15 1 
HETATM 2189 C  C16 . E65 F 5 .   ? -5.253  2.238   15.783  1.00 12.26 ? 266 E65 A C16 1 
HETATM 2190 C  C17 . E65 F 5 .   ? -6.063  3.296   15.387  1.00 13.12 ? 266 E65 A C17 1 
HETATM 2191 C  C18 . E65 F 5 .   ? -5.546  4.327   14.582  1.00 15.36 ? 266 E65 A C18 1 
HETATM 2192 S  S19 . E65 F 5 .   ? -5.903  0.876   16.761  1.00 13.82 ? 266 E65 A S19 1 
HETATM 2193 O  O20 . E65 F 5 .   ? -7.379  0.896   16.553  1.00 11.42 ? 266 E65 A O20 1 
HETATM 2194 O  O21 . E65 F 5 .   ? -5.308  1.000   18.090  1.00 9.77  ? 266 E65 A O21 1 
HETATM 2195 N  N22 . E65 F 5 .   ? -5.219  -0.473  16.014  1.00 10.62 ? 266 E65 A N22 1 
HETATM 2196 O  O1  . MES G 6 .   ? -7.362  -9.097  -2.504  1.00 29.75 ? 267 MES A O1  1 
HETATM 2197 C  C2  . MES G 6 .   ? -7.141  -10.020 -3.668  1.00 33.26 ? 267 MES A C2  1 
HETATM 2198 C  C3  . MES G 6 .   ? -8.441  -10.674 -4.225  1.00 32.13 ? 267 MES A C3  1 
HETATM 2199 N  N4  . MES G 6 .   ? -9.606  -10.832 -3.286  1.00 30.66 ? 267 MES A N4  1 
HETATM 2200 C  C5  . MES G 6 .   ? -9.598  -10.143 -1.941  1.00 27.06 ? 267 MES A C5  1 
HETATM 2201 C  C6  . MES G 6 .   ? -8.257  -9.642  -1.488  1.00 30.66 ? 267 MES A C6  1 
HETATM 2202 C  C7  . MES G 6 .   ? -10.746 -11.758 -3.654  1.00 30.73 ? 267 MES A C7  1 
HETATM 2203 C  C8  . MES G 6 .   ? -12.247 -11.291 -3.403  1.00 28.56 ? 267 MES A C8  1 
HETATM 2204 O  O   . HOH H 7 .   ? -6.674  -15.027 31.495  1.00 20.01 ? 126 HOH A O   1 
HETATM 2205 O  O   . HOH H 7 .   ? -25.664 -9.586  14.934  1.00 32.50 ? 268 HOH A O   1 
HETATM 2206 O  O   . HOH H 7 .   ? 6.312   -8.230  -10.395 1.00 34.29 ? 269 HOH A O   1 
HETATM 2207 O  O   . HOH H 7 .   ? -1.952  16.582  12.370  1.00 28.77 ? 270 HOH A O   1 
HETATM 2208 O  O   . HOH H 7 .   ? -12.556 10.926  -5.217  1.00 29.20 ? 271 HOH A O   1 
HETATM 2209 O  O   . HOH H 7 .   ? -14.849 8.282   34.785  1.00 33.78 ? 272 HOH A O   1 
HETATM 2210 O  O   . HOH H 7 .   ? -16.880 -17.726 24.255  1.00 31.19 ? 273 HOH A O   1 
HETATM 2211 O  O   . HOH H 7 .   ? -19.700 16.658  23.593  1.00 39.56 ? 274 HOH A O   1 
HETATM 2212 O  O   . HOH H 7 .   ? -5.703  -12.685 -5.313  1.00 35.99 ? 275 HOH A O   1 
HETATM 2213 O  O   . HOH H 7 .   ? -17.676 -9.073  36.920  1.00 40.31 ? 276 HOH A O   1 
HETATM 2214 O  O   . HOH H 7 .   ? 1.991   -15.597 14.980  1.00 37.67 ? 277 HOH A O   1 
HETATM 2215 O  O   . HOH H 7 .   ? -14.455 -21.482 3.382   1.00 32.88 ? 278 HOH A O   1 
HETATM 2216 O  O   . HOH H 7 .   ? -0.927  3.891   -5.177  1.00 32.99 ? 279 HOH A O   1 
HETATM 2217 O  O   . HOH H 7 .   ? -17.022 -4.728  -5.401  1.00 33.64 ? 280 HOH A O   1 
HETATM 2218 O  O   . HOH H 7 .   ? -25.478 -1.329  35.215  1.00 35.80 ? 281 HOH A O   1 
HETATM 2219 O  O   . HOH H 7 .   ? -19.176 -11.508 38.358  1.00 36.46 ? 282 HOH A O   1 
HETATM 2220 O  O   . HOH H 7 .   ? -22.590 -9.670  25.299  1.00 19.07 ? 283 HOH A O   1 
HETATM 2221 O  O   . HOH H 7 .   ? 3.463   -9.048  25.302  1.00 29.42 ? 284 HOH A O   1 
HETATM 2222 O  O   . HOH H 7 .   ? -21.263 0.466   0.439   1.00 36.00 ? 285 HOH A O   1 
HETATM 2223 O  O   . HOH H 7 .   ? 6.165   -10.878 15.189  1.00 31.50 ? 286 HOH A O   1 
HETATM 2224 O  O   . HOH H 7 .   ? -13.906 14.802  6.029   1.00 40.81 ? 287 HOH A O   1 
HETATM 2225 O  O   . HOH H 7 .   ? 3.567   -8.968  32.829  1.00 39.91 ? 288 HOH A O   1 
HETATM 2226 O  O   . HOH H 7 .   ? -15.821 16.952  26.644  1.00 36.46 ? 289 HOH A O   1 
HETATM 2227 O  O   . HOH H 7 .   ? -31.913 6.950   15.547  1.00 32.75 ? 290 HOH A O   1 
HETATM 2228 O  O   . HOH H 7 .   ? 0.363   7.079   29.773  1.00 30.11 ? 291 HOH A O   1 
HETATM 2229 O  O   . HOH H 7 .   ? -24.184 -0.029  31.547  1.00 32.87 ? 292 HOH A O   1 
HETATM 2230 O  O   . HOH H 7 .   ? 1.921   -7.000  -8.286  1.00 35.27 ? 293 HOH A O   1 
HETATM 2231 O  O   . HOH H 7 .   ? 2.840   -7.055  40.640  1.00 33.67 ? 294 HOH A O   1 
HETATM 2232 O  O   . HOH H 7 .   ? -24.411 13.521  20.354  1.00 29.46 ? 295 HOH A O   1 
HETATM 2233 O  O   . HOH H 7 .   ? -7.429  -8.568  -7.091  1.00 45.50 ? 296 HOH A O   1 
HETATM 2234 O  O   . HOH H 7 .   ? -24.945 -2.584  -4.268  1.00 35.60 ? 297 HOH A O   1 
HETATM 2235 O  O   . HOH H 7 .   ? -20.705 -0.127  -2.095  1.00 33.20 ? 298 HOH A O   1 
HETATM 2236 O  O   . HOH H 7 .   ? -24.198 -14.435 22.274  1.00 40.52 ? 299 HOH A O   1 
HETATM 2237 O  O   . HOH H 7 .   ? 1.648   -17.789 13.207  1.00 40.61 ? 300 HOH A O   1 
HETATM 2238 O  O   . HOH H 7 .   ? -13.968 -8.643  -5.352  1.00 30.48 ? 301 HOH A O   1 
HETATM 2239 O  O   . HOH H 7 .   ? -12.940 -8.991  -3.051  1.00 29.77 ? 302 HOH A O   1 
HETATM 2240 O  O   . HOH H 7 .   ? 12.917  6.524   16.819  1.00 44.01 ? 303 HOH A O   1 
HETATM 2241 O  O   . HOH H 7 .   ? -1.231  -4.117  15.717  1.00 6.75  ? 304 HOH A O   1 
HETATM 2242 O  O   . HOH H 7 .   ? -4.463  -13.515 18.124  1.00 8.45  ? 305 HOH A O   1 
HETATM 2243 O  O   . HOH H 7 .   ? -2.440  -8.764  29.096  1.00 10.83 ? 306 HOH A O   1 
HETATM 2244 O  O   . HOH H 7 .   ? -10.639 8.655   25.504  1.00 9.15  ? 307 HOH A O   1 
HETATM 2245 O  O   . HOH H 7 .   ? -8.703  -3.856  7.841   1.00 9.46  ? 308 HOH A O   1 
HETATM 2246 O  O   . HOH H 7 .   ? -12.863 -17.194 16.923  1.00 11.97 ? 309 HOH A O   1 
HETATM 2247 O  O   . HOH H 7 .   ? 4.912   -4.947  20.976  1.00 12.48 ? 310 HOH A O   1 
HETATM 2248 O  O   . HOH H 7 .   ? -21.700 5.696   4.685   1.00 14.28 ? 311 HOH A O   1 
HETATM 2249 O  O   . HOH H 7 .   ? -2.059  -12.279 22.769  1.00 8.76  ? 312 HOH A O   1 
HETATM 2250 O  O   . HOH H 7 .   ? -13.985 10.294  27.917  1.00 13.84 ? 313 HOH A O   1 
HETATM 2251 O  O   . HOH H 7 .   ? -17.000 -8.415  20.345  1.00 7.81  ? 314 HOH A O   1 
HETATM 2252 O  O   . HOH H 7 .   ? -9.519  -8.008  34.077  1.00 17.69 ? 315 HOH A O   1 
HETATM 2253 O  O   . HOH H 7 .   ? -21.579 -7.207  23.690  1.00 11.07 ? 316 HOH A O   1 
HETATM 2254 O  O   . HOH H 7 .   ? -3.807  -15.910 24.364  1.00 10.43 ? 317 HOH A O   1 
HETATM 2255 O  O   . HOH H 7 .   ? -16.181 -12.307 24.418  1.00 14.14 ? 318 HOH A O   1 
HETATM 2256 O  O   . HOH H 7 .   ? -17.964 -20.423 7.952   1.00 11.68 ? 319 HOH A O   1 
HETATM 2257 O  O   . HOH H 7 .   ? -3.526  -11.099 20.887  1.00 8.88  ? 320 HOH A O   1 
HETATM 2258 O  O   . HOH H 7 .   ? 3.730   5.053   29.720  1.00 16.41 ? 321 HOH A O   1 
HETATM 2259 O  O   . HOH H 7 .   ? -7.916  -15.440 11.281  1.00 8.17  ? 322 HOH A O   1 
HETATM 2260 O  O   . HOH H 7 .   ? -3.426  -13.286 25.140  1.00 11.39 ? 323 HOH A O   1 
HETATM 2261 O  O   . HOH H 7 .   ? 1.237   -1.524  29.459  1.00 11.60 ? 324 HOH A O   1 
HETATM 2262 O  O   . HOH H 7 .   ? -13.486 -18.505 14.580  1.00 14.95 ? 325 HOH A O   1 
HETATM 2263 O  O   . HOH H 7 .   ? -16.171 -9.948  32.987  1.00 18.47 ? 326 HOH A O   1 
HETATM 2264 O  O   . HOH H 7 .   ? -10.376 -18.282 17.002  1.00 11.61 ? 327 HOH A O   1 
HETATM 2265 O  O   . HOH H 7 .   ? -19.248 10.050  8.887   1.00 14.79 ? 328 HOH A O   1 
HETATM 2266 O  O   . HOH H 7 .   ? 5.385   7.094   20.190  1.00 13.80 ? 329 HOH A O   1 
HETATM 2267 O  O   . HOH H 7 .   ? 1.258   8.858   24.239  1.00 16.20 ? 330 HOH A O   1 
HETATM 2268 O  O   . HOH H 7 .   ? -14.988 -21.123 17.710  1.00 16.38 ? 331 HOH A O   1 
HETATM 2269 O  O   . HOH H 7 .   ? -12.971 -19.521 26.044  1.00 19.40 ? 332 HOH A O   1 
HETATM 2270 O  O   . HOH H 7 .   ? -6.680  -20.230 19.539  1.00 11.70 ? 333 HOH A O   1 
HETATM 2271 O  O   . HOH H 7 .   ? 8.486   -3.844  21.038  1.00 14.58 ? 334 HOH A O   1 
HETATM 2272 O  O   . HOH H 7 .   ? -8.032  -22.311 10.472  1.00 13.32 ? 335 HOH A O   1 
HETATM 2273 O  O   . HOH H 7 .   ? -24.816 -7.759  8.971   1.00 14.67 ? 336 HOH A O   1 
HETATM 2274 O  O   . HOH H 7 .   ? -14.269 -16.613 29.166  1.00 16.91 ? 337 HOH A O   1 
HETATM 2275 O  O   . HOH H 7 .   ? -17.730 -21.169 17.488  1.00 18.46 ? 338 HOH A O   1 
HETATM 2276 O  O   . HOH H 7 .   ? -16.866 -13.913 26.346  1.00 17.54 ? 339 HOH A O   1 
HETATM 2277 O  O   . HOH H 7 .   ? -23.999 -0.743  26.517  1.00 15.35 ? 340 HOH A O   1 
HETATM 2278 O  O   . HOH H 7 .   ? -24.151 8.619   20.062  1.00 21.58 ? 341 HOH A O   1 
HETATM 2279 O  O   . HOH H 7 .   ? -14.639 -18.614 18.829  1.00 13.16 ? 342 HOH A O   1 
HETATM 2280 O  O   . HOH H 7 .   ? -22.893 -11.697 13.958  1.00 19.44 ? 343 HOH A O   1 
HETATM 2281 O  O   . HOH H 7 .   ? -21.039 -12.681 -1.839  1.00 15.06 ? 344 HOH A O   1 
HETATM 2282 O  O   . HOH H 7 .   ? -17.878 10.603  11.336  1.00 15.32 ? 345 HOH A O   1 
HETATM 2283 O  O   . HOH H 7 .   ? -28.688 0.159   24.432  1.00 19.82 ? 346 HOH A O   1 
HETATM 2284 O  O   . HOH H 7 .   ? 11.261  1.277   25.943  1.00 22.26 ? 347 HOH A O   1 
HETATM 2285 O  O   . HOH H 7 .   ? -1.102  -11.132 28.989  1.00 15.03 ? 348 HOH A O   1 
HETATM 2286 O  O   . HOH H 7 .   ? -16.975 -17.915 20.099  1.00 19.60 ? 349 HOH A O   1 
HETATM 2287 O  O   . HOH H 7 .   ? 7.596   6.083   21.672  1.00 14.81 ? 350 HOH A O   1 
HETATM 2288 O  O   . HOH H 7 .   ? -26.854 -2.597  14.337  1.00 16.58 ? 351 HOH A O   1 
HETATM 2289 O  O   . HOH H 7 .   ? -9.015  -5.945  35.965  1.00 15.32 ? 352 HOH A O   1 
HETATM 2290 O  O   . HOH H 7 .   ? -12.156 2.816   30.844  1.00 19.34 ? 353 HOH A O   1 
HETATM 2291 O  O   . HOH H 7 .   ? -17.329 -16.164 22.056  1.00 20.43 ? 354 HOH A O   1 
HETATM 2292 O  O   . HOH H 7 .   ? -13.711 -21.211 15.010  1.00 17.24 ? 355 HOH A O   1 
HETATM 2293 O  O   . HOH H 7 .   ? -1.835  -17.369 25.581  1.00 21.57 ? 356 HOH A O   1 
HETATM 2294 O  O   . HOH H 7 .   ? -12.921 -16.891 26.701  1.00 12.55 ? 357 HOH A O   1 
HETATM 2295 O  O   . HOH H 7 .   ? -6.076  -4.618  -6.494  1.00 20.53 ? 358 HOH A O   1 
HETATM 2296 O  O   . HOH H 7 .   ? 4.374   -3.410  26.514  1.00 16.36 ? 359 HOH A O   1 
HETATM 2297 O  O   . HOH H 7 .   ? 0.055   -1.113  -4.839  1.00 15.06 ? 360 HOH A O   1 
HETATM 2298 O  O   . HOH H 7 .   ? -8.284  -19.395 21.757  1.00 14.45 ? 361 HOH A O   1 
HETATM 2299 O  O   . HOH H 7 .   ? -19.916 -16.793 2.876   1.00 20.74 ? 362 HOH A O   1 
HETATM 2300 O  O   . HOH H 7 .   ? -7.191  -8.723  32.671  1.00 18.97 ? 363 HOH A O   1 
HETATM 2301 O  O   . HOH H 7 .   ? -7.261  -16.886 1.545   1.00 23.11 ? 364 HOH A O   1 
HETATM 2302 O  O   . HOH H 7 .   ? -23.178 -2.920  6.572   1.00 16.78 ? 365 HOH A O   1 
HETATM 2303 O  O   . HOH H 7 .   ? 4.464   -6.509  7.889   1.00 20.01 ? 366 HOH A O   1 
HETATM 2304 O  O   . HOH H 7 .   ? -20.427 10.783  26.687  1.00 15.93 ? 367 HOH A O   1 
HETATM 2305 O  O   . HOH H 7 .   ? -2.497  -3.009  11.367  1.00 20.35 ? 368 HOH A O   1 
HETATM 2306 O  O   . HOH H 7 .   ? -4.773  -11.846 32.044  1.00 18.18 ? 369 HOH A O   1 
HETATM 2307 O  O   . HOH H 7 .   ? -10.275 14.733  12.324  1.00 18.26 ? 370 HOH A O   1 
HETATM 2308 O  O   . HOH H 7 .   ? -22.793 -5.795  2.699   1.00 19.55 ? 371 HOH A O   1 
HETATM 2309 O  O   . HOH H 7 .   ? -15.417 -21.776 13.007  1.00 15.68 ? 372 HOH A O   1 
HETATM 2310 O  O   . HOH H 7 .   ? 4.485   -2.651  28.936  1.00 22.88 ? 373 HOH A O   1 
HETATM 2311 O  O   . HOH H 7 .   ? -10.572 -19.421 19.980  1.00 15.54 ? 374 HOH A O   1 
HETATM 2312 O  O   . HOH H 7 .   ? -16.322 15.825  23.674  1.00 18.09 ? 375 HOH A O   1 
HETATM 2313 O  O   . HOH H 7 .   ? -0.456  10.880  23.468  1.00 16.54 ? 376 HOH A O   1 
HETATM 2314 O  O   . HOH H 7 .   ? -11.130 -19.487 7.058   1.00 27.13 ? 377 HOH A O   1 
HETATM 2315 O  O   . HOH H 7 .   ? -23.555 -0.807  3.874   1.00 18.41 ? 378 HOH A O   1 
HETATM 2316 O  O   . HOH H 7 .   ? -23.225 -0.491  34.507  1.00 23.21 ? 379 HOH A O   1 
HETATM 2317 O  O   . HOH H 7 .   ? -4.303  -8.579  31.091  1.00 18.68 ? 380 HOH A O   1 
HETATM 2318 O  O   . HOH H 7 .   ? -13.981 3.545   33.299  1.00 26.08 ? 381 HOH A O   1 
HETATM 2319 O  O   . HOH H 7 .   ? -3.699  -13.039 -2.776  1.00 20.21 ? 382 HOH A O   1 
HETATM 2320 O  O   . HOH H 7 .   ? -17.966 3.760   -3.753  1.00 32.79 ? 383 HOH A O   1 
HETATM 2321 O  O   . HOH H 7 .   ? -22.130 -18.279 13.506  1.00 18.71 ? 384 HOH A O   1 
HETATM 2322 O  O   . HOH H 7 .   ? 2.535   -11.274 9.371   1.00 26.89 ? 385 HOH A O   1 
HETATM 2323 O  O   . HOH H 7 .   ? -0.274  -14.211 22.247  1.00 19.23 ? 386 HOH A O   1 
HETATM 2324 O  O   . HOH H 7 .   ? -7.044  5.846   6.383   1.00 19.25 ? 387 HOH A O   1 
HETATM 2325 O  O   . HOH H 7 .   ? -15.314 -16.401 25.712  1.00 25.11 ? 388 HOH A O   1 
HETATM 2326 O  O   . HOH H 7 .   ? -11.042 15.329  32.184  1.00 20.02 ? 389 HOH A O   1 
HETATM 2327 O  O   . HOH H 7 .   ? 2.788   -4.441  7.721   1.00 18.28 ? 390 HOH A O   1 
HETATM 2328 O  O   . HOH H 7 .   ? 1.546   -6.210  34.343  1.00 16.33 ? 391 HOH A O   1 
HETATM 2329 O  O   . HOH H 7 .   ? -16.277 -11.364 41.619  1.00 22.91 ? 392 HOH A O   1 
HETATM 2330 O  O   . HOH H 7 .   ? -23.267 -13.116 11.283  1.00 20.49 ? 393 HOH A O   1 
HETATM 2331 O  O   . HOH H 7 .   ? -14.091 14.190  27.221  1.00 19.74 ? 394 HOH A O   1 
HETATM 2332 O  O   . HOH H 7 .   ? -1.391  -13.037 27.014  1.00 18.08 ? 395 HOH A O   1 
HETATM 2333 O  O   . HOH H 7 .   ? -8.389  0.682   -6.458  1.00 25.32 ? 396 HOH A O   1 
HETATM 2334 O  O   . HOH H 7 .   ? -25.697 -10.500 17.818  1.00 22.58 ? 397 HOH A O   1 
HETATM 2335 O  O   . HOH H 7 .   ? 0.263   0.640   -6.814  1.00 30.90 ? 398 HOH A O   1 
HETATM 2336 O  O   . HOH H 7 .   ? -6.228  -19.686 23.761  1.00 16.48 ? 399 HOH A O   1 
HETATM 2337 O  O   . HOH H 7 .   ? -8.461  -19.917 26.682  1.00 15.34 ? 400 HOH A O   1 
HETATM 2338 O  O   . HOH H 7 .   ? 5.430   9.238   21.638  1.00 27.37 ? 401 HOH A O   1 
HETATM 2339 O  O   . HOH H 7 .   ? -0.969  -17.534 17.976  1.00 27.37 ? 402 HOH A O   1 
HETATM 2340 O  O   . HOH H 7 .   ? -9.274  3.029   34.731  1.00 21.94 ? 403 HOH A O   1 
HETATM 2341 O  O   . HOH H 7 .   ? -4.798  -20.720 21.355  1.00 18.46 ? 404 HOH A O   1 
HETATM 2342 O  O   . HOH H 7 .   ? -5.444  3.429   -5.944  1.00 30.02 ? 405 HOH A O   1 
HETATM 2343 O  O   . HOH H 7 .   ? -8.382  -14.681 40.460  1.00 18.57 ? 406 HOH A O   1 
HETATM 2344 O  O   . HOH H 7 .   ? -18.191 -3.709  -2.910  1.00 20.21 ? 407 HOH A O   1 
HETATM 2345 O  O   . HOH H 7 .   ? 10.372  -7.221  -8.883  1.00 23.92 ? 408 HOH A O   1 
HETATM 2346 O  O   . HOH H 7 .   ? 2.617   -13.283 5.342   1.00 21.68 ? 409 HOH A O   1 
HETATM 2347 O  O   . HOH H 7 .   ? -11.092 1.177   33.494  1.00 19.79 ? 410 HOH A O   1 
HETATM 2348 O  O   . HOH H 7 .   ? -13.092 -22.034 8.647   1.00 17.89 ? 411 HOH A O   1 
HETATM 2349 O  O   . HOH H 7 .   ? -25.900 -6.236  13.127  1.00 23.67 ? 412 HOH A O   1 
HETATM 2350 O  O   . HOH H 7 .   ? -29.071 -3.920  13.536  1.00 24.61 ? 413 HOH A O   1 
HETATM 2351 O  O   . HOH H 7 .   ? -24.729 -9.488  2.070   1.00 20.76 ? 414 HOH A O   1 
HETATM 2352 O  O   . HOH H 7 .   ? 5.311   -7.160  22.368  1.00 28.24 ? 415 HOH A O   1 
HETATM 2353 O  O   . HOH H 7 .   ? -26.785 -4.004  24.969  1.00 21.09 ? 416 HOH A O   1 
HETATM 2354 O  O   . HOH H 7 .   ? -17.784 6.304   38.348  1.00 27.93 ? 417 HOH A O   1 
HETATM 2355 O  O   . HOH H 7 .   ? -1.541  11.331  25.924  1.00 27.39 ? 418 HOH A O   1 
HETATM 2356 O  O   . HOH H 7 .   ? -23.942 -7.100  0.206   1.00 26.12 ? 419 HOH A O   1 
HETATM 2357 O  O   . HOH H 7 .   ? -10.077 1.463   39.103  1.00 25.90 ? 420 HOH A O   1 
HETATM 2358 O  O   . HOH H 7 .   ? 8.282   3.222   27.748  1.00 22.94 ? 421 HOH A O   1 
HETATM 2359 O  O   . HOH H 7 .   ? -11.681 -2.949  42.082  1.00 29.76 ? 422 HOH A O   1 
HETATM 2360 O  O   . HOH H 7 .   ? -15.745 9.150   -1.942  1.00 21.96 ? 423 HOH A O   1 
HETATM 2361 O  O   . HOH H 7 .   ? -10.577 -20.386 24.860  1.00 16.34 ? 424 HOH A O   1 
HETATM 2362 O  O   . HOH H 7 .   ? -0.478  -8.498  32.521  1.00 20.56 ? 425 HOH A O   1 
HETATM 2363 O  O   . HOH H 7 .   ? -30.846 -6.822  22.324  1.00 26.72 ? 426 HOH A O   1 
HETATM 2364 O  O   . HOH H 7 .   ? 6.319   -5.414  3.688   1.00 23.71 ? 427 HOH A O   1 
HETATM 2365 O  O   . HOH H 7 .   ? -1.954  -11.917 31.407  1.00 27.88 ? 428 HOH A O   1 
HETATM 2366 O  O   . HOH H 7 .   ? -29.053 -5.746  24.500  1.00 20.60 ? 429 HOH A O   1 
HETATM 2367 O  O   . HOH H 7 .   ? -12.370 12.554  29.197  1.00 23.67 ? 430 HOH A O   1 
HETATM 2368 O  O   . HOH H 7 .   ? 1.376   -11.761 25.134  1.00 18.11 ? 431 HOH A O   1 
HETATM 2369 O  O   . HOH H 7 .   ? -18.552 -20.993 14.720  1.00 21.37 ? 432 HOH A O   1 
HETATM 2370 O  O   . HOH H 7 .   ? -12.817 7.816   28.894  1.00 21.09 ? 433 HOH A O   1 
HETATM 2371 O  O   . HOH H 7 .   ? -10.877 -15.287 34.354  1.00 29.89 ? 434 HOH A O   1 
HETATM 2372 O  O   . HOH H 7 .   ? -8.689  -15.312 36.700  1.00 20.73 ? 435 HOH A O   1 
HETATM 2373 O  O   . HOH H 7 .   ? -22.525 0.029   -4.854  1.00 18.19 ? 436 HOH A O   1 
HETATM 2374 O  O   . HOH H 7 .   ? 8.542   -4.735  23.747  1.00 23.68 ? 437 HOH A O   1 
HETATM 2375 O  O   . HOH H 7 .   ? -26.176 3.432   15.438  1.00 27.35 ? 438 HOH A O   1 
HETATM 2376 O  O   . HOH H 7 .   ? -25.885 6.224   27.148  1.00 22.33 ? 439 HOH A O   1 
HETATM 2377 O  O   . HOH H 7 .   ? -15.092 6.026   32.710  1.00 31.72 ? 440 HOH A O   1 
HETATM 2378 O  O   . HOH H 7 .   ? -25.720 -15.179 8.084   1.00 25.97 ? 441 HOH A O   1 
HETATM 2379 O  O   . HOH H 7 .   ? -23.506 8.404   3.503   1.00 25.85 ? 442 HOH A O   1 
HETATM 2380 O  O   . HOH H 7 .   ? 1.593   3.065   -4.852  1.00 24.84 ? 443 HOH A O   1 
HETATM 2381 O  O   . HOH H 7 .   ? -2.137  -4.683  -6.947  1.00 27.68 ? 444 HOH A O   1 
HETATM 2382 O  O   . HOH H 7 .   ? 0.379   3.220   9.972   1.00 27.57 ? 445 HOH A O   1 
HETATM 2383 O  O   . HOH H 7 .   ? -27.372 -6.882  7.856   1.00 30.65 ? 446 HOH A O   1 
HETATM 2384 O  O   . HOH H 7 .   ? -17.919 -21.832 6.044   1.00 18.91 ? 447 HOH A O   1 
HETATM 2385 O  O   . HOH H 7 .   ? 3.745   9.782   23.720  1.00 23.29 ? 448 HOH A O   1 
HETATM 2386 O  O   . HOH H 7 .   ? -27.539 2.671   23.655  1.00 23.47 ? 449 HOH A O   1 
HETATM 2387 O  O   . HOH H 7 .   ? -7.036  14.929  31.215  1.00 40.21 ? 450 HOH A O   1 
HETATM 2388 O  O   . HOH H 7 .   ? -3.330  18.037  21.700  1.00 28.13 ? 451 HOH A O   1 
HETATM 2389 O  O   . HOH H 7 .   ? -0.268  1.067   -10.758 1.00 30.25 ? 452 HOH A O   1 
HETATM 2390 O  O   . HOH H 7 .   ? -5.005  2.305   37.247  1.00 27.08 ? 453 HOH A O   1 
HETATM 2391 O  O   . HOH H 7 .   ? -20.585 8.288   30.105  1.00 27.12 ? 454 HOH A O   1 
HETATM 2392 O  O   . HOH H 7 .   ? -21.268 -20.320 14.688  1.00 28.26 ? 455 HOH A O   1 
HETATM 2393 O  O   . HOH H 7 .   ? -32.750 1.987   11.722  1.00 28.38 ? 456 HOH A O   1 
HETATM 2394 O  O   . HOH H 7 .   ? -16.263 -15.284 32.854  1.00 27.90 ? 457 HOH A O   1 
HETATM 2395 O  O   . HOH H 7 .   ? -10.439 4.806   31.053  1.00 21.53 ? 458 HOH A O   1 
HETATM 2396 O  O   . HOH H 7 .   ? 2.052   -14.253 20.730  1.00 24.25 ? 459 HOH A O   1 
HETATM 2397 O  O   . HOH H 7 .   ? -26.533 -1.235  26.032  1.00 21.50 ? 460 HOH A O   1 
HETATM 2398 O  O   . HOH H 7 .   ? -8.179  7.597   8.555   1.00 29.08 ? 461 HOH A O   1 
HETATM 2399 O  O   . HOH H 7 .   ? 10.052  -13.329 9.496   1.00 36.04 ? 462 HOH A O   1 
HETATM 2400 O  O   . HOH H 7 .   ? 2.803   1.532   -2.149  1.00 43.02 ? 463 HOH A O   1 
HETATM 2401 O  O   . HOH H 7 .   ? -17.595 -8.525  -6.414  1.00 27.32 ? 464 HOH A O   1 
HETATM 2402 O  O   . HOH H 7 .   ? 1.911   -15.655 9.246   1.00 22.14 ? 465 HOH A O   1 
HETATM 2403 O  O   . HOH H 7 .   ? -10.616 -18.858 34.370  1.00 26.19 ? 466 HOH A O   1 
HETATM 2404 O  O   . HOH H 7 .   ? 3.448   -13.831 12.470  1.00 31.94 ? 467 HOH A O   1 
HETATM 2405 O  O   . HOH H 7 .   ? -4.006  0.381   13.514  1.00 27.76 ? 468 HOH A O   1 
HETATM 2406 O  O   . HOH H 7 .   ? 9.597   -4.871  -7.944  1.00 32.20 ? 469 HOH A O   1 
HETATM 2407 O  O   . HOH H 7 .   ? -17.591 -19.477 35.241  1.00 27.09 ? 470 HOH A O   1 
HETATM 2408 O  O   . HOH H 7 .   ? 2.860   -13.442 8.096   1.00 28.08 ? 471 HOH A O   1 
HETATM 2409 O  O   . HOH H 7 .   ? 1.746   12.494  22.648  1.00 26.84 ? 472 HOH A O   1 
HETATM 2410 O  O   . HOH H 7 .   ? 6.506   -0.633  -1.340  1.00 29.08 ? 473 HOH A O   1 
HETATM 2411 O  O   . HOH H 7 .   ? -15.059 5.603   36.952  1.00 22.76 ? 474 HOH A O   1 
HETATM 2412 O  O   . HOH H 7 .   ? -7.665  -4.764  39.937  1.00 30.55 ? 475 HOH A O   1 
HETATM 2413 O  O   . HOH H 7 .   ? -15.059 9.294   31.214  1.00 34.40 ? 476 HOH A O   1 
HETATM 2414 O  O   . HOH H 7 .   ? -4.689  -15.788 0.536   1.00 22.49 ? 477 HOH A O   1 
HETATM 2415 O  O   . HOH H 7 .   ? -21.953 -14.130 18.663  1.00 25.86 ? 478 HOH A O   1 
HETATM 2416 O  O   . HOH H 7 .   ? -6.075  -11.502 36.569  1.00 25.36 ? 479 HOH A O   1 
HETATM 2417 O  O   . HOH H 7 .   ? -18.179 -20.715 -1.104  1.00 30.91 ? 480 HOH A O   1 
HETATM 2418 O  O   . HOH H 7 .   ? -15.165 -10.270 37.151  1.00 26.54 ? 481 HOH A O   1 
HETATM 2419 O  O   . HOH H 7 .   ? 2.897   -14.527 1.160   1.00 23.56 ? 482 HOH A O   1 
HETATM 2420 O  O   . HOH H 7 .   ? 6.474   5.139   28.561  1.00 27.49 ? 483 HOH A O   1 
HETATM 2421 O  O   . HOH H 7 .   ? -15.110 11.508  34.938  1.00 25.37 ? 484 HOH A O   1 
HETATM 2422 O  O   . HOH H 7 .   ? -21.261 -19.555 6.561   1.00 20.59 ? 485 HOH A O   1 
HETATM 2423 O  O   . HOH H 7 .   ? 14.060  -1.406  28.386  1.00 24.66 ? 486 HOH A O   1 
HETATM 2424 O  O   . HOH H 7 .   ? 10.106  -2.459  13.978  1.00 29.51 ? 487 HOH A O   1 
HETATM 2425 O  O   . HOH H 7 .   ? -11.424 0.873   -7.756  1.00 35.75 ? 488 HOH A O   1 
HETATM 2426 O  O   . HOH H 7 .   ? 1.935   -17.473 7.050   1.00 27.67 ? 489 HOH A O   1 
HETATM 2427 O  O   . HOH H 7 .   ? 11.979  -6.693  7.957   1.00 26.35 ? 490 HOH A O   1 
HETATM 2428 O  O   . HOH H 7 .   ? -11.523 -0.331  43.466  1.00 23.99 ? 491 HOH A O   1 
HETATM 2429 O  O   . HOH H 7 .   ? -31.804 5.678   13.007  1.00 32.28 ? 492 HOH A O   1 
HETATM 2430 O  O   . HOH H 7 .   ? -13.294 -0.662  -6.147  1.00 33.31 ? 493 HOH A O   1 
HETATM 2431 O  O   . HOH H 7 .   ? -28.024 5.216   25.507  1.00 30.29 ? 494 HOH A O   1 
HETATM 2432 O  O   . HOH H 7 .   ? -16.987 -21.849 22.313  1.00 39.71 ? 495 HOH A O   1 
HETATM 2433 O  O   . HOH H 7 .   ? 12.149  4.087   27.308  1.00 29.82 ? 496 HOH A O   1 
HETATM 2434 O  O   . HOH H 7 .   ? -20.836 -6.580  -2.082  1.00 27.96 ? 497 HOH A O   1 
HETATM 2435 O  O   . HOH H 7 .   ? 1.962   8.146   27.774  1.00 29.00 ? 498 HOH A O   1 
HETATM 2436 O  O   . HOH H 7 .   ? -24.053 -21.151 10.402  1.00 28.71 ? 499 HOH A O   1 
HETATM 2437 O  O   . HOH H 7 .   ? 3.180   2.950   -0.016  1.00 29.19 ? 500 HOH A O   1 
HETATM 2438 O  O   . HOH H 7 .   ? -26.877 -6.383  4.786   1.00 31.32 ? 501 HOH A O   1 
HETATM 2439 O  O   . HOH H 7 .   ? -2.657  -17.923 31.018  1.00 28.35 ? 502 HOH A O   1 
HETATM 2440 O  O   . HOH H 7 .   ? 11.549  -0.383  15.990  1.00 27.10 ? 503 HOH A O   1 
HETATM 2441 O  O   . HOH H 7 .   ? -17.786 -12.152 31.530  1.00 21.54 ? 504 HOH A O   1 
HETATM 2442 O  O   . HOH H 7 .   ? 4.085   5.013   2.464   1.00 28.49 ? 505 HOH A O   1 
HETATM 2443 O  O   . HOH H 7 .   ? -27.017 -13.002 20.247  1.00 29.14 ? 506 HOH A O   1 
HETATM 2444 O  O   . HOH H 7 .   ? -4.696  -7.162  37.583  1.00 22.73 ? 507 HOH A O   1 
HETATM 2445 O  O   . HOH H 7 .   ? 10.252  -8.609  8.028   1.00 33.05 ? 508 HOH A O   1 
HETATM 2446 O  O   . HOH H 7 .   ? -14.882 -19.405 33.157  1.00 22.50 ? 509 HOH A O   1 
HETATM 2447 O  O   . HOH H 7 .   ? 8.119   -5.790  -10.542 1.00 26.39 ? 510 HOH A O   1 
HETATM 2448 O  O   . HOH H 7 .   ? 6.240   -5.456  -11.854 1.00 20.10 ? 511 HOH A O   1 
HETATM 2449 O  O   . HOH H 7 .   ? 2.468   -14.686 -5.919  1.00 30.24 ? 512 HOH A O   1 
HETATM 2450 O  O   . HOH H 7 .   ? -14.215 0.445   42.653  1.00 30.58 ? 513 HOH A O   1 
HETATM 2451 O  O   . HOH H 7 .   ? 5.906   -14.012 8.784   1.00 32.12 ? 514 HOH A O   1 
HETATM 2452 O  O   . HOH H 7 .   ? -1.386  1.670   11.394  1.00 29.16 ? 515 HOH A O   1 
HETATM 2453 O  O   . HOH H 7 .   ? -10.753 8.584   7.659   1.00 22.54 ? 516 HOH A O   1 
HETATM 2454 O  O   . HOH H 7 .   ? -15.243 -19.906 23.121  1.00 22.83 ? 517 HOH A O   1 
HETATM 2455 O  O   . HOH H 7 .   ? -1.589  4.238   1.896   1.00 35.21 ? 518 HOH A O   1 
HETATM 2456 O  O   . HOH H 7 .   ? -24.053 -17.736 6.517   1.00 30.37 ? 519 HOH A O   1 
HETATM 2457 O  O   . HOH H 7 .   ? -1.546  -16.896 34.346  1.00 31.61 ? 520 HOH A O   1 
HETATM 2458 O  O   . HOH H 7 .   ? -1.047  -13.221 33.173  1.00 22.07 ? 521 HOH A O   1 
HETATM 2459 O  O   . HOH H 7 .   ? -17.157 -6.500  42.476  1.00 26.47 ? 522 HOH A O   1 
HETATM 2460 O  O   . HOH H 7 .   ? -5.015  -14.161 38.586  1.00 31.47 ? 523 HOH A O   1 
HETATM 2461 O  O   . HOH H 7 .   ? -2.970  -0.345  10.522  1.00 28.20 ? 524 HOH A O   1 
HETATM 2462 O  O   . HOH H 7 .   ? 1.625   -15.925 18.326  1.00 39.50 ? 525 HOH A O   1 
HETATM 2463 O  O   . HOH H 7 .   ? -12.328 -24.704 11.206  1.00 25.91 ? 526 HOH A O   1 
HETATM 2464 O  O   . HOH H 7 .   ? -18.669 -8.983  34.576  1.00 27.84 ? 527 HOH A O   1 
HETATM 2465 O  O   . HOH H 7 .   ? -17.087 -7.330  39.769  1.00 27.58 ? 528 HOH A O   1 
HETATM 2466 O  O   . HOH H 7 .   ? -24.157 -14.091 19.580  1.00 28.58 ? 529 HOH A O   1 
HETATM 2467 O  O   . HOH H 7 .   ? -25.338 10.988  19.423  1.00 31.86 ? 530 HOH A O   1 
HETATM 2468 O  O   . HOH H 7 .   ? -16.316 -12.555 -5.970  1.00 24.58 ? 531 HOH A O   1 
HETATM 2469 O  O   . HOH H 7 .   ? -21.898 -21.635 12.308  1.00 31.32 ? 532 HOH A O   1 
HETATM 2470 O  O   . HOH H 7 .   ? 4.853   -12.971 -5.815  1.00 21.60 ? 533 HOH A O   1 
HETATM 2471 O  O   . HOH H 7 .   ? -28.123 5.763   19.214  1.00 27.42 ? 534 HOH A O   1 
HETATM 2472 O  O   . HOH H 7 .   ? -23.475 -11.016 17.242  1.00 24.93 ? 535 HOH A O   1 
HETATM 2473 O  O   . HOH H 7 .   ? -6.556  -22.457 8.119   1.00 32.04 ? 536 HOH A O   1 
HETATM 2474 O  O   . HOH H 7 .   ? -24.858 4.698   8.228   1.00 28.13 ? 537 HOH A O   1 
HETATM 2475 O  O   . HOH H 7 .   ? -2.481  -19.088 21.366  1.00 28.17 ? 538 HOH A O   1 
HETATM 2476 O  O   . HOH H 7 .   ? -25.223 8.751   26.148  1.00 26.12 ? 539 HOH A O   1 
HETATM 2477 O  O   . HOH H 7 .   ? -12.053 11.181  34.836  1.00 32.44 ? 540 HOH A O   1 
HETATM 2478 O  O   . HOH H 7 .   ? -0.663  6.561   32.118  1.00 27.95 ? 541 HOH A O   1 
HETATM 2479 O  O   . HOH H 7 .   ? -9.006  6.618   -3.746  1.00 29.53 ? 542 HOH A O   1 
HETATM 2480 O  O   . HOH H 7 .   ? -23.948 -2.602  29.129  1.00 26.63 ? 543 HOH A O   1 
HETATM 2481 O  O   . HOH H 7 .   ? 0.365   -9.681  -5.517  1.00 24.31 ? 544 HOH A O   1 
HETATM 2482 O  O   . HOH H 7 .   ? 4.142   -11.626 23.629  1.00 32.99 ? 545 HOH A O   1 
HETATM 2483 O  O   . HOH H 7 .   ? 6.787   -5.781  6.801   1.00 25.78 ? 546 HOH A O   1 
HETATM 2484 O  O   . HOH H 7 .   ? 4.038   4.485   11.162  1.00 37.97 ? 547 HOH A O   1 
HETATM 2485 O  O   . HOH H 7 .   ? 1.646   -9.834  31.397  1.00 24.89 ? 548 HOH A O   1 
HETATM 2486 O  O   . HOH H 7 .   ? -25.781 9.651   13.293  1.00 30.42 ? 549 HOH A O   1 
HETATM 2487 O  O   . HOH H 7 .   ? -4.229  3.867   10.195  1.00 28.99 ? 550 HOH A O   1 
HETATM 2488 O  O   . HOH H 7 .   ? -5.079  0.931   10.152  1.00 28.08 ? 551 HOH A O   1 
HETATM 2489 O  O   . HOH H 7 .   ? -2.771  4.304   8.176   1.00 28.43 ? 552 HOH A O   1 
HETATM 2490 O  O   . HOH H 7 .   ? -19.659 -4.283  41.405  1.00 25.00 ? 553 HOH A O   1 
HETATM 2491 O  O   . HOH H 7 .   ? 3.036   2.792   8.290   1.00 27.99 ? 554 HOH A O   1 
HETATM 2492 O  O   . HOH H 7 .   ? -5.210  0.133   40.214  1.00 29.22 ? 555 HOH A O   1 
HETATM 2493 O  O   . HOH H 7 .   ? -0.882  -17.809 -1.679  1.00 30.69 ? 556 HOH A O   1 
HETATM 2494 O  O   . HOH H 7 .   ? -26.507 2.799   20.880  1.00 27.90 ? 557 HOH A O   1 
HETATM 2495 O  O   . HOH H 7 .   ? -16.310 -14.581 28.897  1.00 31.47 ? 558 HOH A O   1 
HETATM 2496 O  O   . HOH H 7 .   ? -0.480  14.073  16.045  1.00 27.11 ? 559 HOH A O   1 
HETATM 2497 O  O   . HOH H 7 .   ? -26.243 -7.582  30.446  1.00 27.18 ? 560 HOH A O   1 
HETATM 2498 O  O   . HOH H 7 .   ? -16.508 14.564  33.126  1.00 26.73 ? 561 HOH A O   1 
HETATM 2499 O  O   . HOH H 7 .   ? -19.709 -23.560 6.114   1.00 28.40 ? 562 HOH A O   1 
HETATM 2500 O  O   . HOH H 7 .   ? -0.358  -6.938  -7.450  1.00 36.06 ? 563 HOH A O   1 
HETATM 2501 O  O   . HOH H 7 .   ? -12.092 -24.951 8.391   1.00 32.67 ? 564 HOH A O   1 
HETATM 2502 O  O   . HOH H 7 .   ? -18.736 -5.790  45.357  1.00 31.11 ? 565 HOH A O   1 
HETATM 2503 O  O   . HOH H 7 .   ? -12.969 -22.306 12.264  1.00 31.22 ? 566 HOH A O   1 
HETATM 2504 O  O   . HOH H 7 .   ? 4.860   -6.162  33.404  1.00 41.84 ? 567 HOH A O   1 
HETATM 2505 O  O   . HOH H 7 .   ? -5.929  -18.064 3.519   1.00 27.13 ? 568 HOH A O   1 
HETATM 2506 O  O   . HOH H 7 .   ? 0.352   -0.047  -14.501 1.00 29.88 ? 569 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   2   SER SER A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
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   262 1   ZN  ZN  A . 
C 3 BCN 1   263 1   BCN BCN A . 
D 4 DMS 1   264 1   DMS DMS A . 
E 4 DMS 1   265 2   DMS DMS A . 
F 5 E65 1   266 1   E65 E65 A . 
G 6 MES 1   267 1   MES MES A . 
H 7 HOH 1   126 126 HOH HOH A . 
H 7 HOH 2   268 268 HOH HOH A . 
H 7 HOH 3   269 269 HOH HOH A . 
H 7 HOH 4   270 270 HOH HOH A . 
H 7 HOH 5   271 271 HOH HOH A . 
H 7 HOH 6   272 272 HOH HOH A . 
H 7 HOH 7   273 273 HOH HOH A . 
H 7 HOH 8   274 274 HOH HOH A . 
H 7 HOH 9   275 275 HOH HOH A . 
H 7 HOH 10  276 276 HOH HOH A . 
H 7 HOH 11  277 277 HOH HOH A . 
H 7 HOH 12  278 278 HOH HOH A . 
H 7 HOH 13  279 279 HOH HOH A . 
H 7 HOH 14  280 280 HOH HOH A . 
H 7 HOH 15  281 281 HOH HOH A . 
H 7 HOH 16  282 282 HOH HOH A . 
H 7 HOH 17  283 283 HOH HOH A . 
H 7 HOH 18  284 284 HOH HOH A . 
H 7 HOH 19  285 285 HOH HOH A . 
H 7 HOH 20  286 286 HOH HOH A . 
H 7 HOH 21  287 287 HOH HOH A . 
H 7 HOH 22  288 288 HOH HOH A . 
H 7 HOH 23  289 289 HOH HOH A . 
H 7 HOH 24  290 290 HOH HOH A . 
H 7 HOH 25  291 291 HOH HOH A . 
H 7 HOH 26  292 292 HOH HOH A . 
H 7 HOH 27  293 293 HOH HOH A . 
H 7 HOH 28  294 294 HOH HOH A . 
H 7 HOH 29  295 295 HOH HOH A . 
H 7 HOH 30  296 296 HOH HOH A . 
H 7 HOH 31  297 297 HOH HOH A . 
H 7 HOH 32  298 298 HOH HOH A . 
H 7 HOH 33  299 299 HOH HOH A . 
H 7 HOH 34  300 300 HOH HOH A . 
H 7 HOH 35  301 301 HOH HOH A . 
H 7 HOH 36  302 302 HOH HOH A . 
H 7 HOH 37  303 303 HOH HOH A . 
H 7 HOH 38  304 1   HOH HOH A . 
H 7 HOH 39  305 2   HOH HOH A . 
H 7 HOH 40  306 3   HOH HOH A . 
H 7 HOH 41  307 4   HOH HOH A . 
H 7 HOH 42  308 5   HOH HOH A . 
H 7 HOH 43  309 6   HOH HOH A . 
H 7 HOH 44  310 7   HOH HOH A . 
H 7 HOH 45  311 8   HOH HOH A . 
H 7 HOH 46  312 9   HOH HOH A . 
H 7 HOH 47  313 10  HOH HOH A . 
H 7 HOH 48  314 11  HOH HOH A . 
H 7 HOH 49  315 12  HOH HOH A . 
H 7 HOH 50  316 13  HOH HOH A . 
H 7 HOH 51  317 14  HOH HOH A . 
H 7 HOH 52  318 15  HOH HOH A . 
H 7 HOH 53  319 16  HOH HOH A . 
H 7 HOH 54  320 17  HOH HOH A . 
H 7 HOH 55  321 18  HOH HOH A . 
H 7 HOH 56  322 19  HOH HOH A . 
H 7 HOH 57  323 20  HOH HOH A . 
H 7 HOH 58  324 21  HOH HOH A . 
H 7 HOH 59  325 22  HOH HOH A . 
H 7 HOH 60  326 23  HOH HOH A . 
H 7 HOH 61  327 24  HOH HOH A . 
H 7 HOH 62  328 25  HOH HOH A . 
H 7 HOH 63  329 26  HOH HOH A . 
H 7 HOH 64  330 27  HOH HOH A . 
H 7 HOH 65  331 28  HOH HOH A . 
H 7 HOH 66  332 29  HOH HOH A . 
H 7 HOH 67  333 30  HOH HOH A . 
H 7 HOH 68  334 31  HOH HOH A . 
H 7 HOH 69  335 32  HOH HOH A . 
H 7 HOH 70  336 33  HOH HOH A . 
H 7 HOH 71  337 34  HOH HOH A . 
H 7 HOH 72  338 35  HOH HOH A . 
H 7 HOH 73  339 36  HOH HOH A . 
H 7 HOH 74  340 37  HOH HOH A . 
H 7 HOH 75  341 38  HOH HOH A . 
H 7 HOH 76  342 39  HOH HOH A . 
H 7 HOH 77  343 40  HOH HOH A . 
H 7 HOH 78  344 41  HOH HOH A . 
H 7 HOH 79  345 42  HOH HOH A . 
H 7 HOH 80  346 43  HOH HOH A . 
H 7 HOH 81  347 44  HOH HOH A . 
H 7 HOH 82  348 45  HOH HOH A . 
H 7 HOH 83  349 46  HOH HOH A . 
H 7 HOH 84  350 47  HOH HOH A . 
H 7 HOH 85  351 48  HOH HOH A . 
H 7 HOH 86  352 49  HOH HOH A . 
H 7 HOH 87  353 50  HOH HOH A . 
H 7 HOH 88  354 51  HOH HOH A . 
H 7 HOH 89  355 52  HOH HOH A . 
H 7 HOH 90  356 53  HOH HOH A . 
H 7 HOH 91  357 54  HOH HOH A . 
H 7 HOH 92  358 55  HOH HOH A . 
H 7 HOH 93  359 56  HOH HOH A . 
H 7 HOH 94  360 57  HOH HOH A . 
H 7 HOH 95  361 58  HOH HOH A . 
H 7 HOH 96  362 59  HOH HOH A . 
H 7 HOH 97  363 60  HOH HOH A . 
H 7 HOH 98  364 61  HOH HOH A . 
H 7 HOH 99  365 62  HOH HOH A . 
H 7 HOH 100 366 63  HOH HOH A . 
H 7 HOH 101 367 64  HOH HOH A . 
H 7 HOH 102 368 65  HOH HOH A . 
H 7 HOH 103 369 66  HOH HOH A . 
H 7 HOH 104 370 67  HOH HOH A . 
H 7 HOH 105 371 68  HOH HOH A . 
H 7 HOH 106 372 69  HOH HOH A . 
H 7 HOH 107 373 70  HOH HOH A . 
H 7 HOH 108 374 71  HOH HOH A . 
H 7 HOH 109 375 72  HOH HOH A . 
H 7 HOH 110 376 73  HOH HOH A . 
H 7 HOH 111 377 74  HOH HOH A . 
H 7 HOH 112 378 75  HOH HOH A . 
H 7 HOH 113 379 76  HOH HOH A . 
H 7 HOH 114 380 77  HOH HOH A . 
H 7 HOH 115 381 78  HOH HOH A . 
H 7 HOH 116 382 79  HOH HOH A . 
H 7 HOH 117 383 80  HOH HOH A . 
H 7 HOH 118 384 81  HOH HOH A . 
H 7 HOH 119 385 82  HOH HOH A . 
H 7 HOH 120 386 83  HOH HOH A . 
H 7 HOH 121 387 84  HOH HOH A . 
H 7 HOH 122 388 85  HOH HOH A . 
H 7 HOH 123 389 86  HOH HOH A . 
H 7 HOH 124 390 87  HOH HOH A . 
H 7 HOH 125 391 88  HOH HOH A . 
H 7 HOH 126 392 89  HOH HOH A . 
H 7 HOH 127 393 90  HOH HOH A . 
H 7 HOH 128 394 91  HOH HOH A . 
H 7 HOH 129 395 92  HOH HOH A . 
H 7 HOH 130 396 93  HOH HOH A . 
H 7 HOH 131 397 94  HOH HOH A . 
H 7 HOH 132 398 95  HOH HOH A . 
H 7 HOH 133 399 96  HOH HOH A . 
H 7 HOH 134 400 97  HOH HOH A . 
H 7 HOH 135 401 98  HOH HOH A . 
H 7 HOH 136 402 99  HOH HOH A . 
H 7 HOH 137 403 100 HOH HOH A . 
H 7 HOH 138 404 101 HOH HOH A . 
H 7 HOH 139 405 102 HOH HOH A . 
H 7 HOH 140 406 103 HOH HOH A . 
H 7 HOH 141 407 104 HOH HOH A . 
H 7 HOH 142 408 105 HOH HOH A . 
H 7 HOH 143 409 106 HOH HOH A . 
H 7 HOH 144 410 107 HOH HOH A . 
H 7 HOH 145 411 108 HOH HOH A . 
H 7 HOH 146 412 109 HOH HOH A . 
H 7 HOH 147 413 110 HOH HOH A . 
H 7 HOH 148 414 111 HOH HOH A . 
H 7 HOH 149 415 112 HOH HOH A . 
H 7 HOH 150 416 113 HOH HOH A . 
H 7 HOH 151 417 114 HOH HOH A . 
H 7 HOH 152 418 115 HOH HOH A . 
H 7 HOH 153 419 116 HOH HOH A . 
H 7 HOH 154 420 117 HOH HOH A . 
H 7 HOH 155 421 118 HOH HOH A . 
H 7 HOH 156 422 119 HOH HOH A . 
H 7 HOH 157 423 120 HOH HOH A . 
H 7 HOH 158 424 121 HOH HOH A . 
H 7 HOH 159 425 122 HOH HOH A . 
H 7 HOH 160 426 123 HOH HOH A . 
H 7 HOH 161 427 124 HOH HOH A . 
H 7 HOH 162 428 125 HOH HOH A . 
H 7 HOH 163 429 127 HOH HOH A . 
H 7 HOH 164 430 128 HOH HOH A . 
H 7 HOH 165 431 129 HOH HOH A . 
H 7 HOH 166 432 130 HOH HOH A . 
H 7 HOH 167 433 131 HOH HOH A . 
H 7 HOH 168 434 132 HOH HOH A . 
H 7 HOH 169 435 133 HOH HOH A . 
H 7 HOH 170 436 134 HOH HOH A . 
H 7 HOH 171 437 135 HOH HOH A . 
H 7 HOH 172 438 136 HOH HOH A . 
H 7 HOH 173 439 137 HOH HOH A . 
H 7 HOH 174 440 138 HOH HOH A . 
H 7 HOH 175 441 139 HOH HOH A . 
H 7 HOH 176 442 140 HOH HOH A . 
H 7 HOH 177 443 141 HOH HOH A . 
H 7 HOH 178 444 142 HOH HOH A . 
H 7 HOH 179 445 143 HOH HOH A . 
H 7 HOH 180 446 144 HOH HOH A . 
H 7 HOH 181 447 145 HOH HOH A . 
H 7 HOH 182 448 146 HOH HOH A . 
H 7 HOH 183 449 147 HOH HOH A . 
H 7 HOH 184 450 148 HOH HOH A . 
H 7 HOH 185 451 149 HOH HOH A . 
H 7 HOH 186 452 150 HOH HOH A . 
H 7 HOH 187 453 151 HOH HOH A . 
H 7 HOH 188 454 152 HOH HOH A . 
H 7 HOH 189 455 153 HOH HOH A . 
H 7 HOH 190 456 154 HOH HOH A . 
H 7 HOH 191 457 155 HOH HOH A . 
H 7 HOH 192 458 156 HOH HOH A . 
H 7 HOH 193 459 157 HOH HOH A . 
H 7 HOH 194 460 158 HOH HOH A . 
H 7 HOH 195 461 159 HOH HOH A . 
H 7 HOH 196 462 160 HOH HOH A . 
H 7 HOH 197 463 161 HOH HOH A . 
H 7 HOH 198 464 162 HOH HOH A . 
H 7 HOH 199 465 163 HOH HOH A . 
H 7 HOH 200 466 164 HOH HOH A . 
H 7 HOH 201 467 165 HOH HOH A . 
H 7 HOH 202 468 166 HOH HOH A . 
H 7 HOH 203 469 167 HOH HOH A . 
H 7 HOH 204 470 168 HOH HOH A . 
H 7 HOH 205 471 169 HOH HOH A . 
H 7 HOH 206 472 170 HOH HOH A . 
H 7 HOH 207 473 171 HOH HOH A . 
H 7 HOH 208 474 172 HOH HOH A . 
H 7 HOH 209 475 173 HOH HOH A . 
H 7 HOH 210 476 174 HOH HOH A . 
H 7 HOH 211 477 175 HOH HOH A . 
H 7 HOH 212 478 176 HOH HOH A . 
H 7 HOH 213 479 177 HOH HOH A . 
H 7 HOH 214 480 178 HOH HOH A . 
H 7 HOH 215 481 179 HOH HOH A . 
H 7 HOH 216 482 180 HOH HOH A . 
H 7 HOH 217 483 181 HOH HOH A . 
H 7 HOH 218 484 182 HOH HOH A . 
H 7 HOH 219 485 183 HOH HOH A . 
H 7 HOH 220 486 184 HOH HOH A . 
H 7 HOH 221 487 185 HOH HOH A . 
H 7 HOH 222 488 186 HOH HOH A . 
H 7 HOH 223 489 187 HOH HOH A . 
H 7 HOH 224 490 188 HOH HOH A . 
H 7 HOH 225 491 189 HOH HOH A . 
H 7 HOH 226 492 190 HOH HOH A . 
H 7 HOH 227 493 191 HOH HOH A . 
H 7 HOH 228 494 192 HOH HOH A . 
H 7 HOH 229 495 193 HOH HOH A . 
H 7 HOH 230 496 194 HOH HOH A . 
H 7 HOH 231 497 195 HOH HOH A . 
H 7 HOH 232 498 196 HOH HOH A . 
H 7 HOH 233 499 197 HOH HOH A . 
H 7 HOH 234 500 198 HOH HOH A . 
H 7 HOH 235 501 199 HOH HOH A . 
H 7 HOH 236 502 200 HOH HOH A . 
H 7 HOH 237 503 201 HOH HOH A . 
H 7 HOH 238 504 202 HOH HOH A . 
H 7 HOH 239 505 203 HOH HOH A . 
H 7 HOH 240 506 204 HOH HOH A . 
H 7 HOH 241 507 205 HOH HOH A . 
H 7 HOH 242 508 206 HOH HOH A . 
H 7 HOH 243 509 207 HOH HOH A . 
H 7 HOH 244 510 208 HOH HOH A . 
H 7 HOH 245 511 209 HOH HOH A . 
H 7 HOH 246 512 210 HOH HOH A . 
H 7 HOH 247 513 211 HOH HOH A . 
H 7 HOH 248 514 212 HOH HOH A . 
H 7 HOH 249 515 213 HOH HOH A . 
H 7 HOH 250 516 214 HOH HOH A . 
H 7 HOH 251 517 215 HOH HOH A . 
H 7 HOH 252 518 216 HOH HOH A . 
H 7 HOH 253 519 217 HOH HOH A . 
H 7 HOH 254 520 218 HOH HOH A . 
H 7 HOH 255 521 219 HOH HOH A . 
H 7 HOH 256 522 220 HOH HOH A . 
H 7 HOH 257 523 221 HOH HOH A . 
H 7 HOH 258 524 222 HOH HOH A . 
H 7 HOH 259 525 223 HOH HOH A . 
H 7 HOH 260 526 224 HOH HOH A . 
H 7 HOH 261 527 225 HOH HOH A . 
H 7 HOH 262 528 226 HOH HOH A . 
H 7 HOH 263 529 227 HOH HOH A . 
H 7 HOH 264 530 228 HOH HOH A . 
H 7 HOH 265 531 229 HOH HOH A . 
H 7 HOH 266 532 230 HOH HOH A . 
H 7 HOH 267 533 231 HOH HOH A . 
H 7 HOH 268 534 232 HOH HOH A . 
H 7 HOH 269 535 233 HOH HOH A . 
H 7 HOH 270 536 234 HOH HOH A . 
H 7 HOH 271 537 235 HOH HOH A . 
H 7 HOH 272 538 236 HOH HOH A . 
H 7 HOH 273 539 237 HOH HOH A . 
H 7 HOH 274 540 238 HOH HOH A . 
H 7 HOH 275 541 239 HOH HOH A . 
H 7 HOH 276 542 240 HOH HOH A . 
H 7 HOH 277 543 241 HOH HOH A . 
H 7 HOH 278 544 242 HOH HOH A . 
H 7 HOH 279 545 243 HOH HOH A . 
H 7 HOH 280 546 244 HOH HOH A . 
H 7 HOH 281 547 245 HOH HOH A . 
H 7 HOH 282 548 246 HOH HOH A . 
H 7 HOH 283 549 247 HOH HOH A . 
H 7 HOH 284 550 248 HOH HOH A . 
H 7 HOH 285 551 249 HOH HOH A . 
H 7 HOH 286 552 250 HOH HOH A . 
H 7 HOH 287 553 251 HOH HOH A . 
H 7 HOH 288 554 252 HOH HOH A . 
H 7 HOH 289 555 253 HOH HOH A . 
H 7 HOH 290 556 254 HOH HOH A . 
H 7 HOH 291 557 255 HOH HOH A . 
H 7 HOH 292 558 256 HOH HOH A . 
H 7 HOH 293 559 257 HOH HOH A . 
H 7 HOH 294 560 258 HOH HOH A . 
H 7 HOH 295 561 259 HOH HOH A . 
H 7 HOH 296 562 260 HOH HOH A . 
H 7 HOH 297 563 261 HOH HOH A . 
H 7 HOH 298 564 262 HOH HOH A . 
H 7 HOH 299 565 263 HOH HOH A . 
H 7 HOH 300 566 264 HOH HOH A . 
H 7 HOH 301 567 265 HOH HOH A . 
H 7 HOH 302 568 266 HOH HOH A . 
H 7 HOH 303 569 267 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,H 
# 
_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 262 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 107.8 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 114.1 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 97.2  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N22 ? F E65 .   ? A E65 266 ? 1_555 106.9 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N22 ? F E65 .   ? A E65 266 ? 1_555 110.5 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N22 ? F E65 .   ? A E65 266 ? 1_555 119.5 ? 
# 
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 2012-04-11 
2 'Structure model' 1 1 2012-05-16 
3 'Structure model' 1 2 2017-09-27 
4 'Structure model' 1 3 2023-09-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' Advisory                 
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Refinement description' 
5 4 'Structure model' Advisory                 
6 4 'Structure model' 'Data collection'        
7 4 'Structure model' 'Database references'    
8 4 'Structure model' 'Derived calculations'   
9 4 '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  3 'Structure model' diffrn_detector               
2  3 'Structure model' pdbx_unobs_or_zero_occ_atoms  
3  3 'Structure model' software                      
4  4 'Structure model' chem_comp_atom                
5  4 'Structure model' chem_comp_bond                
6  4 'Structure model' database_2                    
7  4 'Structure model' diffrn_source                 
8  4 'Structure model' pdbx_initial_refinement_model 
9  4 'Structure model' pdbx_struct_conn_angle        
10 4 'Structure model' pdbx_unobs_or_zero_occ_atoms  
11 4 'Structure model' struct_conn                   
12 4 '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  3 'Structure model' '_diffrn_detector.detector'                   
2  4 'Structure model' '_database_2.pdbx_DOI'                        
3  4 'Structure model' '_database_2.pdbx_database_accession'         
4  4 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
5  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
6  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
8  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
9  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
10 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
11 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
12 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
13 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
14 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
15 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
16 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
17 4 'Structure model' '_pdbx_struct_conn_angle.value'               
18 4 'Structure model' '_struct_conn.pdbx_dist_value'                
19 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
20 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
21 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
22 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
23 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
24 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
25 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
26 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
27 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
28 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
29 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
30 4 'Structure model' '_struct_site.pdbx_auth_asym_id'              
31 4 'Structure model' '_struct_site.pdbx_auth_comp_id'              
32 4 '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 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OD2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     85 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    B 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     507 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              2.08 
# 
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 ALA A 65  ? ? -161.12 -167.92 
2 1 LYS A 76  ? ? -130.04 -41.85  
3 1 LYS A 170 ? A -39.77  132.67  
4 1 PHE A 176 ? ? -151.07 73.24   
5 1 ASN A 244 ? ? -99.79  53.49   
6 1 ASN A 253 ? ? 66.61   -2.46   
7 1 ARG A 254 ? ? -46.12  154.94  
8 1 ARG A 254 ? ? -46.12  152.84  
# 
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 45  ? CE  ? A LYS 45  CE  
2  1 Y 0 A LYS 45  ? NZ  ? A LYS 45  NZ  
3  1 Y 0 A LYS 159 ? CD  A A LYS 158 CD  
4  1 Y 0 A LYS 159 ? CD  B A LYS 158 CD  
5  1 Y 0 A LYS 159 ? CE  A A LYS 158 CE  
6  1 Y 0 A LYS 159 ? CE  B A LYS 158 CE  
7  1 Y 0 A LYS 159 ? NZ  A A LYS 158 NZ  
8  1 Y 0 A LYS 159 ? NZ  B A LYS 158 NZ  
9  1 N 1 A MES 267 ? S   ? G MES 1   S   
10 1 N 1 A MES 267 ? O1S ? G MES 1   O1S 
11 1 N 1 A MES 267 ? O2S ? G MES 1   O2S 
12 1 N 1 A MES 267 ? O3S ? G MES 1   O3S 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     MET 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    MET 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
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  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
E65 N1   N  Y N 122 
E65 C2   C  Y N 123 
E65 N3   N  Y N 124 
E65 C4   C  Y N 125 
E65 C5   C  Y N 126 
E65 C6   C  Y N 127 
E65 S7   S  N N 128 
E65 C8   C  N N 129 
E65 C9   C  N N 130 
E65 O10  O  N N 131 
E65 C11  C  N N 132 
E65 C12  C  N N 133 
E65 C13  C  Y N 134 
E65 C14  C  Y N 135 
E65 C15  C  Y N 136 
E65 C16  C  Y N 137 
E65 C17  C  Y N 138 
E65 C18  C  Y N 139 
E65 S19  S  N N 140 
E65 O20  O  N N 141 
E65 O21  O  N N 142 
E65 N22  N  N N 143 
E65 H5   H  N N 144 
E65 H8   H  N N 145 
E65 H8A  H  N N 146 
E65 H11  H  N N 147 
E65 H11A H  N N 148 
E65 H11B H  N N 149 
E65 H12  H  N N 150 
E65 H12A H  N N 151 
E65 H12B H  N N 152 
E65 H14  H  N N 153 
E65 H15  H  N N 154 
E65 H17  H  N N 155 
E65 H18  H  N N 156 
E65 HN22 H  N N 157 
E65 HN2A H  N N 158 
GLN N    N  N N 159 
GLN CA   C  N S 160 
GLN C    C  N N 161 
GLN O    O  N N 162 
GLN CB   C  N N 163 
GLN CG   C  N N 164 
GLN CD   C  N N 165 
GLN OE1  O  N N 166 
GLN NE2  N  N N 167 
GLN OXT  O  N N 168 
GLN H    H  N N 169 
GLN H2   H  N N 170 
GLN HA   H  N N 171 
GLN HB2  H  N N 172 
GLN HB3  H  N N 173 
GLN HG2  H  N N 174 
GLN HG3  H  N N 175 
GLN HE21 H  N N 176 
GLN HE22 H  N N 177 
GLN HXT  H  N N 178 
GLU N    N  N N 179 
GLU CA   C  N S 180 
GLU C    C  N N 181 
GLU O    O  N N 182 
GLU CB   C  N N 183 
GLU CG   C  N N 184 
GLU CD   C  N N 185 
GLU OE1  O  N N 186 
GLU OE2  O  N N 187 
GLU OXT  O  N N 188 
GLU H    H  N N 189 
GLU H2   H  N N 190 
GLU HA   H  N N 191 
GLU HB2  H  N N 192 
GLU HB3  H  N N 193 
GLU HG2  H  N N 194 
GLU HG3  H  N N 195 
GLU HE2  H  N N 196 
GLU HXT  H  N N 197 
GLY N    N  N N 198 
GLY CA   C  N N 199 
GLY C    C  N N 200 
GLY O    O  N N 201 
GLY OXT  O  N N 202 
GLY H    H  N N 203 
GLY H2   H  N N 204 
GLY HA2  H  N N 205 
GLY HA3  H  N N 206 
GLY HXT  H  N N 207 
HIS N    N  N N 208 
HIS CA   C  N S 209 
HIS C    C  N N 210 
HIS O    O  N N 211 
HIS CB   C  N N 212 
HIS CG   C  Y N 213 
HIS ND1  N  Y N 214 
HIS CD2  C  Y N 215 
HIS CE1  C  Y N 216 
HIS NE2  N  Y N 217 
HIS OXT  O  N N 218 
HIS H    H  N N 219 
HIS H2   H  N N 220 
HIS HA   H  N N 221 
HIS HB2  H  N N 222 
HIS HB3  H  N N 223 
HIS HD1  H  N N 224 
HIS HD2  H  N N 225 
HIS HE1  H  N N 226 
HIS HE2  H  N N 227 
HIS HXT  H  N N 228 
HOH O    O  N N 229 
HOH H1   H  N N 230 
HOH H2   H  N N 231 
ILE N    N  N N 232 
ILE CA   C  N S 233 
ILE C    C  N N 234 
ILE O    O  N N 235 
ILE CB   C  N S 236 
ILE CG1  C  N N 237 
ILE CG2  C  N N 238 
ILE CD1  C  N N 239 
ILE OXT  O  N N 240 
ILE H    H  N N 241 
ILE H2   H  N N 242 
ILE HA   H  N N 243 
ILE HB   H  N N 244 
ILE HG12 H  N N 245 
ILE HG13 H  N N 246 
ILE HG21 H  N N 247 
ILE HG22 H  N N 248 
ILE HG23 H  N N 249 
ILE HD11 H  N N 250 
ILE HD12 H  N N 251 
ILE HD13 H  N N 252 
ILE HXT  H  N N 253 
LEU N    N  N N 254 
LEU CA   C  N S 255 
LEU C    C  N N 256 
LEU O    O  N N 257 
LEU CB   C  N N 258 
LEU CG   C  N N 259 
LEU CD1  C  N N 260 
LEU CD2  C  N N 261 
LEU OXT  O  N N 262 
LEU H    H  N N 263 
LEU H2   H  N N 264 
LEU HA   H  N N 265 
LEU HB2  H  N N 266 
LEU HB3  H  N N 267 
LEU HG   H  N N 268 
LEU HD11 H  N N 269 
LEU HD12 H  N N 270 
LEU HD13 H  N N 271 
LEU HD21 H  N N 272 
LEU HD22 H  N N 273 
LEU HD23 H  N N 274 
LEU HXT  H  N N 275 
LYS N    N  N N 276 
LYS CA   C  N S 277 
LYS C    C  N N 278 
LYS O    O  N N 279 
LYS CB   C  N N 280 
LYS CG   C  N N 281 
LYS CD   C  N N 282 
LYS CE   C  N N 283 
LYS NZ   N  N N 284 
LYS OXT  O  N N 285 
LYS H    H  N N 286 
LYS H2   H  N N 287 
LYS HA   H  N N 288 
LYS HB2  H  N N 289 
LYS HB3  H  N N 290 
LYS HG2  H  N N 291 
LYS HG3  H  N N 292 
LYS HD2  H  N N 293 
LYS HD3  H  N N 294 
LYS HE2  H  N N 295 
LYS HE3  H  N N 296 
LYS HZ1  H  N N 297 
LYS HZ2  H  N N 298 
LYS HZ3  H  N N 299 
LYS HXT  H  N N 300 
MES O1   O  N N 301 
MES C2   C  N N 302 
MES C3   C  N N 303 
MES N4   N  N N 304 
MES C5   C  N N 305 
MES C6   C  N N 306 
MES C7   C  N N 307 
MES C8   C  N N 308 
MES S    S  N N 309 
MES O1S  O  N N 310 
MES O2S  O  N N 311 
MES O3S  O  N N 312 
MES H21  H  N N 313 
MES H22  H  N N 314 
MES H31  H  N N 315 
MES H32  H  N N 316 
MES HN4  H  N N 317 
MES H51  H  N N 318 
MES H52  H  N N 319 
MES H61  H  N N 320 
MES H62  H  N N 321 
MES H71  H  N N 322 
MES H72  H  N N 323 
MES H81  H  N N 324 
MES H82  H  N N 325 
MET N    N  N N 326 
MET CA   C  N S 327 
MET C    C  N N 328 
MET O    O  N N 329 
MET CB   C  N N 330 
MET CG   C  N N 331 
MET SD   S  N N 332 
MET CE   C  N N 333 
MET OXT  O  N N 334 
MET H    H  N N 335 
MET H2   H  N N 336 
MET HA   H  N N 337 
MET HB2  H  N N 338 
MET HB3  H  N N 339 
MET HG2  H  N N 340 
MET HG3  H  N N 341 
MET HE1  H  N N 342 
MET HE2  H  N N 343 
MET HE3  H  N N 344 
MET HXT  H  N N 345 
PHE N    N  N N 346 
PHE CA   C  N S 347 
PHE C    C  N N 348 
PHE O    O  N N 349 
PHE CB   C  N N 350 
PHE CG   C  Y N 351 
PHE CD1  C  Y N 352 
PHE CD2  C  Y N 353 
PHE CE1  C  Y N 354 
PHE CE2  C  Y N 355 
PHE CZ   C  Y N 356 
PHE OXT  O  N N 357 
PHE H    H  N N 358 
PHE H2   H  N N 359 
PHE HA   H  N N 360 
PHE HB2  H  N N 361 
PHE HB3  H  N N 362 
PHE HD1  H  N N 363 
PHE HD2  H  N N 364 
PHE HE1  H  N N 365 
PHE HE2  H  N N 366 
PHE HZ   H  N N 367 
PHE HXT  H  N N 368 
PRO N    N  N N 369 
PRO CA   C  N S 370 
PRO C    C  N N 371 
PRO O    O  N N 372 
PRO CB   C  N N 373 
PRO CG   C  N N 374 
PRO CD   C  N N 375 
PRO OXT  O  N N 376 
PRO H    H  N N 377 
PRO HA   H  N N 378 
PRO HB2  H  N N 379 
PRO HB3  H  N N 380 
PRO HG2  H  N N 381 
PRO HG3  H  N N 382 
PRO HD2  H  N N 383 
PRO HD3  H  N N 384 
PRO HXT  H  N N 385 
SER N    N  N N 386 
SER CA   C  N S 387 
SER C    C  N N 388 
SER O    O  N N 389 
SER CB   C  N N 390 
SER OG   O  N N 391 
SER OXT  O  N N 392 
SER H    H  N N 393 
SER H2   H  N N 394 
SER HA   H  N N 395 
SER HB2  H  N N 396 
SER HB3  H  N N 397 
SER HG   H  N N 398 
SER HXT  H  N N 399 
THR N    N  N N 400 
THR CA   C  N S 401 
THR C    C  N N 402 
THR O    O  N N 403 
THR CB   C  N R 404 
THR OG1  O  N N 405 
THR CG2  C  N N 406 
THR OXT  O  N N 407 
THR H    H  N N 408 
THR H2   H  N N 409 
THR HA   H  N N 410 
THR HB   H  N N 411 
THR HG1  H  N N 412 
THR HG21 H  N N 413 
THR HG22 H  N N 414 
THR HG23 H  N N 415 
THR HXT  H  N N 416 
TRP N    N  N N 417 
TRP CA   C  N S 418 
TRP C    C  N N 419 
TRP O    O  N N 420 
TRP CB   C  N N 421 
TRP CG   C  Y N 422 
TRP CD1  C  Y N 423 
TRP CD2  C  Y N 424 
TRP NE1  N  Y N 425 
TRP CE2  C  Y N 426 
TRP CE3  C  Y N 427 
TRP CZ2  C  Y N 428 
TRP CZ3  C  Y N 429 
TRP CH2  C  Y N 430 
TRP OXT  O  N N 431 
TRP H    H  N N 432 
TRP H2   H  N N 433 
TRP HA   H  N N 434 
TRP HB2  H  N N 435 
TRP HB3  H  N N 436 
TRP HD1  H  N N 437 
TRP HE1  H  N N 438 
TRP HE3  H  N N 439 
TRP HZ2  H  N N 440 
TRP HZ3  H  N N 441 
TRP HH2  H  N N 442 
TRP HXT  H  N N 443 
TYR N    N  N N 444 
TYR CA   C  N S 445 
TYR C    C  N N 446 
TYR O    O  N N 447 
TYR CB   C  N N 448 
TYR CG   C  Y N 449 
TYR CD1  C  Y N 450 
TYR CD2  C  Y N 451 
TYR CE1  C  Y N 452 
TYR CE2  C  Y N 453 
TYR CZ   C  Y N 454 
TYR OH   O  N N 455 
TYR OXT  O  N N 456 
TYR H    H  N N 457 
TYR H2   H  N N 458 
TYR HA   H  N N 459 
TYR HB2  H  N N 460 
TYR HB3  H  N N 461 
TYR HD1  H  N N 462 
TYR HD2  H  N N 463 
TYR HE1  H  N N 464 
TYR HE2  H  N N 465 
TYR HH   H  N N 466 
TYR HXT  H  N N 467 
VAL N    N  N N 468 
VAL CA   C  N S 469 
VAL C    C  N N 470 
VAL O    O  N N 471 
VAL CB   C  N N 472 
VAL CG1  C  N N 473 
VAL CG2  C  N N 474 
VAL OXT  O  N N 475 
VAL H    H  N N 476 
VAL H2   H  N N 477 
VAL HA   H  N N 478 
VAL HB   H  N N 479 
VAL HG11 H  N N 480 
VAL HG12 H  N N 481 
VAL HG13 H  N N 482 
VAL HG21 H  N N 483 
VAL HG22 H  N N 484 
VAL HG23 H  N N 485 
VAL HXT  H  N N 486 
ZN  ZN   ZN N N 487 
# 
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  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
E65 N1  C2   doub Y N 115 
E65 N1  C6   sing Y N 116 
E65 S7  C2   sing N N 117 
E65 C2  N3   sing Y N 118 
E65 N3  C4   doub Y N 119 
E65 C5  C4   sing Y N 120 
E65 C4  C11  sing N N 121 
E65 C6  C5   doub Y N 122 
E65 C5  H5   sing N N 123 
E65 C12 C6   sing N N 124 
E65 S7  C8   sing N N 125 
E65 C8  C9   sing N N 126 
E65 C8  H8   sing N N 127 
E65 C8  H8A  sing N N 128 
E65 O10 C9   doub N N 129 
E65 C9  C13  sing N N 130 
E65 C11 H11  sing N N 131 
E65 C11 H11A sing N N 132 
E65 C11 H11B sing N N 133 
E65 C12 H12  sing N N 134 
E65 C12 H12A sing N N 135 
E65 C12 H12B sing N N 136 
E65 C13 C14  doub Y N 137 
E65 C13 C18  sing Y N 138 
E65 C14 C15  sing Y N 139 
E65 C14 H14  sing N N 140 
E65 C15 C16  doub Y N 141 
E65 C15 H15  sing N N 142 
E65 C17 C16  sing Y N 143 
E65 C16 S19  sing N N 144 
E65 C18 C17  doub Y N 145 
E65 C17 H17  sing N N 146 
E65 C18 H18  sing N N 147 
E65 N22 S19  sing N N 148 
E65 O20 S19  doub N N 149 
E65 S19 O21  doub N N 150 
E65 N22 HN22 sing N N 151 
E65 N22 HN2A sing N N 152 
GLN N   CA   sing N N 153 
GLN N   H    sing N N 154 
GLN N   H2   sing N N 155 
GLN CA  C    sing N N 156 
GLN CA  CB   sing N N 157 
GLN CA  HA   sing N N 158 
GLN C   O    doub N N 159 
GLN C   OXT  sing N N 160 
GLN CB  CG   sing N N 161 
GLN CB  HB2  sing N N 162 
GLN CB  HB3  sing N N 163 
GLN CG  CD   sing N N 164 
GLN CG  HG2  sing N N 165 
GLN CG  HG3  sing N N 166 
GLN CD  OE1  doub N N 167 
GLN CD  NE2  sing N N 168 
GLN NE2 HE21 sing N N 169 
GLN NE2 HE22 sing N N 170 
GLN OXT HXT  sing N N 171 
GLU N   CA   sing N N 172 
GLU N   H    sing N N 173 
GLU N   H2   sing N N 174 
GLU CA  C    sing N N 175 
GLU CA  CB   sing N N 176 
GLU CA  HA   sing N N 177 
GLU C   O    doub N N 178 
GLU C   OXT  sing N N 179 
GLU CB  CG   sing N N 180 
GLU CB  HB2  sing N N 181 
GLU CB  HB3  sing N N 182 
GLU CG  CD   sing N N 183 
GLU CG  HG2  sing N N 184 
GLU CG  HG3  sing N N 185 
GLU CD  OE1  doub N N 186 
GLU CD  OE2  sing N N 187 
GLU OE2 HE2  sing N N 188 
GLU OXT HXT  sing N N 189 
GLY N   CA   sing N N 190 
GLY N   H    sing N N 191 
GLY N   H2   sing N N 192 
GLY CA  C    sing N N 193 
GLY CA  HA2  sing N N 194 
GLY CA  HA3  sing N N 195 
GLY C   O    doub N N 196 
GLY C   OXT  sing N N 197 
GLY OXT HXT  sing N N 198 
HIS N   CA   sing N N 199 
HIS N   H    sing N N 200 
HIS N   H2   sing N N 201 
HIS CA  C    sing N N 202 
HIS CA  CB   sing N N 203 
HIS CA  HA   sing N N 204 
HIS C   O    doub N N 205 
HIS C   OXT  sing N N 206 
HIS CB  CG   sing N N 207 
HIS CB  HB2  sing N N 208 
HIS CB  HB3  sing N N 209 
HIS CG  ND1  sing Y N 210 
HIS CG  CD2  doub Y N 211 
HIS ND1 CE1  doub Y N 212 
HIS ND1 HD1  sing N N 213 
HIS CD2 NE2  sing Y N 214 
HIS CD2 HD2  sing N N 215 
HIS CE1 NE2  sing Y N 216 
HIS CE1 HE1  sing N N 217 
HIS NE2 HE2  sing N N 218 
HIS OXT HXT  sing N N 219 
HOH O   H1   sing N N 220 
HOH O   H2   sing N N 221 
ILE N   CA   sing N N 222 
ILE N   H    sing N N 223 
ILE N   H2   sing N N 224 
ILE CA  C    sing N N 225 
ILE CA  CB   sing N N 226 
ILE CA  HA   sing N N 227 
ILE C   O    doub N N 228 
ILE C   OXT  sing N N 229 
ILE CB  CG1  sing N N 230 
ILE CB  CG2  sing N N 231 
ILE CB  HB   sing N N 232 
ILE CG1 CD1  sing N N 233 
ILE CG1 HG12 sing N N 234 
ILE CG1 HG13 sing N N 235 
ILE CG2 HG21 sing N N 236 
ILE CG2 HG22 sing N N 237 
ILE CG2 HG23 sing N N 238 
ILE CD1 HD11 sing N N 239 
ILE CD1 HD12 sing N N 240 
ILE CD1 HD13 sing N N 241 
ILE OXT HXT  sing N N 242 
LEU N   CA   sing N N 243 
LEU N   H    sing N N 244 
LEU N   H2   sing N N 245 
LEU CA  C    sing N N 246 
LEU CA  CB   sing N N 247 
LEU CA  HA   sing N N 248 
LEU C   O    doub N N 249 
LEU C   OXT  sing N N 250 
LEU CB  CG   sing N N 251 
LEU CB  HB2  sing N N 252 
LEU CB  HB3  sing N N 253 
LEU CG  CD1  sing N N 254 
LEU CG  CD2  sing N N 255 
LEU CG  HG   sing N N 256 
LEU CD1 HD11 sing N N 257 
LEU CD1 HD12 sing N N 258 
LEU CD1 HD13 sing N N 259 
LEU CD2 HD21 sing N N 260 
LEU CD2 HD22 sing N N 261 
LEU CD2 HD23 sing N N 262 
LEU OXT HXT  sing N N 263 
LYS N   CA   sing N N 264 
LYS N   H    sing N N 265 
LYS N   H2   sing N N 266 
LYS CA  C    sing N N 267 
LYS CA  CB   sing N N 268 
LYS CA  HA   sing N N 269 
LYS C   O    doub N N 270 
LYS C   OXT  sing N N 271 
LYS CB  CG   sing N N 272 
LYS CB  HB2  sing N N 273 
LYS CB  HB3  sing N N 274 
LYS CG  CD   sing N N 275 
LYS CG  HG2  sing N N 276 
LYS CG  HG3  sing N N 277 
LYS CD  CE   sing N N 278 
LYS CD  HD2  sing N N 279 
LYS CD  HD3  sing N N 280 
LYS CE  NZ   sing N N 281 
LYS CE  HE2  sing N N 282 
LYS CE  HE3  sing N N 283 
LYS NZ  HZ1  sing N N 284 
LYS NZ  HZ2  sing N N 285 
LYS NZ  HZ3  sing N N 286 
LYS OXT HXT  sing N N 287 
MES O1  C2   sing N N 288 
MES O1  C6   sing N N 289 
MES C2  C3   sing N N 290 
MES C2  H21  sing N N 291 
MES C2  H22  sing N N 292 
MES C3  N4   sing N N 293 
MES C3  H31  sing N N 294 
MES C3  H32  sing N N 295 
MES N4  C5   sing N N 296 
MES N4  C7   sing N N 297 
MES N4  HN4  sing N N 298 
MES C5  C6   sing N N 299 
MES C5  H51  sing N N 300 
MES C5  H52  sing N N 301 
MES C6  H61  sing N N 302 
MES C6  H62  sing N N 303 
MES C7  C8   sing N N 304 
MES C7  H71  sing N N 305 
MES C7  H72  sing N N 306 
MES C8  S    sing N N 307 
MES C8  H81  sing N N 308 
MES C8  H82  sing N N 309 
MES S   O1S  doub N N 310 
MES S   O2S  doub N N 311 
MES S   O3S  sing N N 312 
MET N   CA   sing N N 313 
MET N   H    sing N N 314 
MET N   H2   sing N N 315 
MET CA  C    sing N N 316 
MET CA  CB   sing N N 317 
MET CA  HA   sing N N 318 
MET C   O    doub N N 319 
MET C   OXT  sing N N 320 
MET CB  CG   sing N N 321 
MET CB  HB2  sing N N 322 
MET CB  HB3  sing N N 323 
MET CG  SD   sing N N 324 
MET CG  HG2  sing N N 325 
MET CG  HG3  sing N N 326 
MET SD  CE   sing N N 327 
MET CE  HE1  sing N N 328 
MET CE  HE2  sing N N 329 
MET CE  HE3  sing N N 330 
MET OXT HXT  sing N N 331 
PHE N   CA   sing N N 332 
PHE N   H    sing N N 333 
PHE N   H2   sing N N 334 
PHE CA  C    sing N N 335 
PHE CA  CB   sing N N 336 
PHE CA  HA   sing N N 337 
PHE C   O    doub N N 338 
PHE C   OXT  sing N N 339 
PHE CB  CG   sing N N 340 
PHE CB  HB2  sing N N 341 
PHE CB  HB3  sing N N 342 
PHE CG  CD1  doub Y N 343 
PHE CG  CD2  sing Y N 344 
PHE CD1 CE1  sing Y N 345 
PHE CD1 HD1  sing N N 346 
PHE CD2 CE2  doub Y N 347 
PHE CD2 HD2  sing N N 348 
PHE CE1 CZ   doub Y N 349 
PHE CE1 HE1  sing N N 350 
PHE CE2 CZ   sing Y N 351 
PHE CE2 HE2  sing N N 352 
PHE CZ  HZ   sing N N 353 
PHE OXT HXT  sing N N 354 
PRO N   CA   sing N N 355 
PRO N   CD   sing N N 356 
PRO N   H    sing N N 357 
PRO CA  C    sing N N 358 
PRO CA  CB   sing N N 359 
PRO CA  HA   sing N N 360 
PRO C   O    doub N N 361 
PRO C   OXT  sing N N 362 
PRO CB  CG   sing N N 363 
PRO CB  HB2  sing N N 364 
PRO CB  HB3  sing N N 365 
PRO CG  CD   sing N N 366 
PRO CG  HG2  sing N N 367 
PRO CG  HG3  sing N N 368 
PRO CD  HD2  sing N N 369 
PRO CD  HD3  sing N N 370 
PRO OXT HXT  sing N N 371 
SER N   CA   sing N N 372 
SER N   H    sing N N 373 
SER N   H2   sing N N 374 
SER CA  C    sing N N 375 
SER CA  CB   sing N N 376 
SER CA  HA   sing N N 377 
SER C   O    doub N N 378 
SER C   OXT  sing N N 379 
SER CB  OG   sing N N 380 
SER CB  HB2  sing N N 381 
SER CB  HB3  sing N N 382 
SER OG  HG   sing N N 383 
SER OXT HXT  sing N N 384 
THR N   CA   sing N N 385 
THR N   H    sing N N 386 
THR N   H2   sing N N 387 
THR CA  C    sing N N 388 
THR CA  CB   sing N N 389 
THR CA  HA   sing N N 390 
THR C   O    doub N N 391 
THR C   OXT  sing N N 392 
THR CB  OG1  sing N N 393 
THR CB  CG2  sing N N 394 
THR CB  HB   sing N N 395 
THR OG1 HG1  sing N N 396 
THR CG2 HG21 sing N N 397 
THR CG2 HG22 sing N N 398 
THR CG2 HG23 sing N N 399 
THR OXT HXT  sing N N 400 
TRP N   CA   sing N N 401 
TRP N   H    sing N N 402 
TRP N   H2   sing N N 403 
TRP CA  C    sing N N 404 
TRP CA  CB   sing N N 405 
TRP CA  HA   sing N N 406 
TRP C   O    doub N N 407 
TRP C   OXT  sing N N 408 
TRP CB  CG   sing N N 409 
TRP CB  HB2  sing N N 410 
TRP CB  HB3  sing N N 411 
TRP CG  CD1  doub Y N 412 
TRP CG  CD2  sing Y N 413 
TRP CD1 NE1  sing Y N 414 
TRP CD1 HD1  sing N N 415 
TRP CD2 CE2  doub Y N 416 
TRP CD2 CE3  sing Y N 417 
TRP NE1 CE2  sing Y N 418 
TRP NE1 HE1  sing N N 419 
TRP CE2 CZ2  sing Y N 420 
TRP CE3 CZ3  doub Y N 421 
TRP CE3 HE3  sing N N 422 
TRP CZ2 CH2  doub Y N 423 
TRP CZ2 HZ2  sing N N 424 
TRP CZ3 CH2  sing Y N 425 
TRP CZ3 HZ3  sing N N 426 
TRP CH2 HH2  sing N N 427 
TRP OXT HXT  sing N N 428 
TYR N   CA   sing N N 429 
TYR N   H    sing N N 430 
TYR N   H2   sing N N 431 
TYR CA  C    sing N N 432 
TYR CA  CB   sing N N 433 
TYR CA  HA   sing N N 434 
TYR C   O    doub N N 435 
TYR C   OXT  sing N N 436 
TYR CB  CG   sing N N 437 
TYR CB  HB2  sing N N 438 
TYR CB  HB3  sing N N 439 
TYR CG  CD1  doub Y N 440 
TYR CG  CD2  sing Y N 441 
TYR CD1 CE1  sing Y N 442 
TYR CD1 HD1  sing N N 443 
TYR CD2 CE2  doub Y N 444 
TYR CD2 HD2  sing N N 445 
TYR CE1 CZ   doub Y N 446 
TYR CE1 HE1  sing N N 447 
TYR CE2 CZ   sing Y N 448 
TYR CE2 HE2  sing N N 449 
TYR CZ  OH   sing N N 450 
TYR OH  HH   sing N N 451 
TYR OXT HXT  sing N N 452 
VAL N   CA   sing N N 453 
VAL N   H    sing N N 454 
VAL N   H2   sing N N 455 
VAL CA  C    sing N N 456 
VAL CA  CB   sing N N 457 
VAL CA  HA   sing N N 458 
VAL C   O    doub N N 459 
VAL C   OXT  sing N N 460 
VAL CB  CG1  sing N N 461 
VAL CB  CG2  sing N N 462 
VAL CB  HB   sing N N 463 
VAL CG1 HG11 sing N N 464 
VAL CG1 HG12 sing N N 465 
VAL CG1 HG13 sing N N 466 
VAL CG2 HG21 sing N N 467 
VAL CG2 HG22 sing N N 468 
VAL CG2 HG23 sing N N 469 
VAL OXT HXT  sing N N 470 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                           ZN  
3 BICINE                                                               BCN 
4 'DIMETHYL SULFOXIDE'                                                 DMS 
5 '4-{[(4,6-dimethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' E65 
6 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                               MES 
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          'PDB entry 3HLJ' 
# 
