data_4HT0
# 
_entry.id   4HT0 
# 
_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   4HT0         pdb_00004ht0 10.2210/pdb4ht0/pdb 
RCSB  RCSB075883   ?            ?                   
WWPDB D_1000075883 ?            ?                   
# 
_pdbx_database_status.entry_id                        4HT0 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2012-10-31 
_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.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'4-Substituted-2,3,5,6-tetrafluorobenzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, XII, and XIII.' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            21 
_citation.page_first                2093 
_citation.page_last                 2106 
_citation.year                      2013 
_citation.journal_id_ASTM           BMECEP 
_citation.country                   UK 
_citation.journal_id_ISSN           0968-0896 
_citation.journal_id_CSD            1200 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23394791 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2013.01.008 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dudutiene, V.' 1 ? 
primary 'Zubriene, A.'  2 ? 
primary 'Smirnov, A.'   3 ? 
primary 'Gylyte, J.'    4 ? 
primary 'Timm, D.'      5 ? 
primary 'Manakova, E.'  6 ? 
primary 'Grazulis, S.'  7 ? 
primary 'Matulis, D.'   8 ? 
# 
_cell.entry_id           4HT0 
_cell.length_a           42.018 
_cell.length_b           40.898 
_cell.length_c           71.604 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.040 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              2 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4HT0 
_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 ? 
'human carbonic anhydrase II' ? 
2 non-polymer syn 'ZINC ION'                                                                   65.409    1   ?       ? ? ? 
3 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                       195.237   1   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                         78.133    1   ?       ? ? ? 
5 non-polymer syn '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' 367.342   1   ?       ? ? ? 
6 water       nat water                                                                        18.015    270 ?       ? ? ? 
# 
_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              4HT0 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                      ? 'C3 H7 N O2'         
89.093  
ARG 'L-peptide linking' y ARGININE                                                                     ? 'C6 H15 N4 O2 1'     
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                   ? 'C4 H8 N2 O3'        
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                              ? 'C4 H7 N O4'         
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                     ? 'C3 H7 N O2 S'       
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                         ? 'C2 H6 O S'          
78.133  
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 
V50 non-polymer         . '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' ? 'C12 H9 F4 N3 O2 S2' 
367.342 
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          4HT0 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   40.0 
_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              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
;0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate, VAPOR DIFFUSION, SITTING DROP, temperature 291K
;
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR555 FLAT PANEL' 
_diffrn_detector.pdbx_collection_date   2011-11-16 
_diffrn_detector.details                'Detector swing-out angle up to 30 degrees' 
# 
_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   0.815 
_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        0.815 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X11 
# 
_reflns.entry_id                     4HT0 
_reflns.d_resolution_high            1.600 
_reflns.d_resolution_low             19.800 
_reflns.number_all                   ? 
_reflns.number_obs                   30222 
_reflns.pdbx_netI_over_sigmaI        21.800 
_reflns.pdbx_Rsym_value              0.061 
_reflns.pdbx_redundancy              7.500 
_reflns.percent_possible_obs         96.500 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            0.061 
_reflns.B_iso_Wilson_estimate        14.734 
_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 
1.60 1.69  ? 34420 ? 0.123 5.3  0.123 ? 7.80 ? 4428 97.00 1  1 
1.69 1.79  ? 32491 ? 0.099 6.6  0.099 ? 7.80 ? 4178 97.40 2  1 
1.79 1.91  ? 30728 ? 0.079 7.8  0.079 ? 7.80 ? 3958 97.50 3  1 
1.91 2.07  ? 28331 ? 0.069 8.8  0.069 ? 7.70 ? 3657 97.90 4  1 
2.07 2.26  ? 26445 ? 0.063 9.5  0.063 ? 7.70 ? 3417 98.20 5  1 
2.26 2.53  ? 23964 ? 0.060 9.9  0.060 ? 7.70 ? 3108 98.60 6  1 
2.53 2.92  ? 21123 ? 0.057 10.1 0.057 ? 7.70 ? 2761 98.70 7  1 
2.92 3.58  ? 16366 ? 0.053 11.6 0.053 ? 7.00 ? 2327 98.50 8  1 
3.58 5.06  ? 9092  ? 0.049 13.3 0.049 ? 5.70 ? 1599 87.00 9  1 
5.06 19.80 ? 4117  ? 0.051 12.6 0.051 ? 5.20 ? 789  75.80 10 1 
# 
_refine.entry_id                                 4HT0 
_refine.ls_d_res_high                            1.600 
_refine.ls_d_res_low                             19.800 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    96.170 
_refine.ls_number_reflns_obs                     30208 
_refine.ls_number_reflns_all                     30222 
_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                          0.172 
_refine.ls_R_factor_obs                          0.172 
_refine.ls_R_factor_R_work                       0.168 
_refine.ls_wR_factor_R_work                      0.186 
_refine.ls_R_factor_R_free                       0.210 
_refine.ls_wR_factor_R_free                      0.231 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  3032 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               15.521 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.480 
_refine.aniso_B[2][2]                            -0.730 
_refine.aniso_B[3][3]                            0.220 
_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               0.956 
_refine.correlation_coeff_Fo_to_Fc_free          0.930 
_refine.overall_SU_R_Cruickshank_DPI             0.106 
_refine.overall_SU_R_free                        0.106 
_refine.pdbx_overall_ESU_R                       0.106 
_refine.pdbx_overall_ESU_R_Free                  0.106 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.861 
_refine.B_iso_max                                49.00 
_refine.B_iso_min                                4.03 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      '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_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             270 
_refine_hist.number_atoms_total               2355 
_refine_hist.d_res_high                       1.600 
_refine_hist.d_res_low                        19.800 
# 
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         2247 0.029  0.022  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      3062 2.562  1.965  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   277  6.943  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   101  33.977 24.752 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   379  14.151 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   7    23.320 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr           314  0.272  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     1746 0.014  0.020  ? ? 'X-RAY DIFFRACTION' 
r_nbd_refined            1230 0.231  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          1518 0.318  0.200  ? ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    253  0.164  0.200  ? ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      4    0.056  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   76   0.230  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 44   0.213  0.200  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_it              1346 1.577  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcangle_it             2186 2.313  2.000  ? ? 'X-RAY DIFFRACTION' 
r_scbond_it              901  3.214  3.000  ? ? 'X-RAY DIFFRACTION' 
r_scangle_it             876  4.578  4.500  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.600 
_refine_ls_shell.d_res_low                        1.641 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               96.760 
_refine_ls_shell.number_reflns_R_work             2039 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.225 
_refine_ls_shell.R_factor_R_free                  0.308 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             204 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                2243 
_refine_ls_shell.number_reflns_obs                2039 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4HT0 
_struct.title                     'Crystal structure of human carbonic anhydrase isozyme II with the inhibitor.' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4HT0 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, carbon-oxygen lyase activity' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  GLY A 12  ? GLU A 14  ? GLY A 12  GLU A 14  5 ? 3 
HELX_P HELX_P2  2  HIS A 15  ? PHE A 20  ? HIS A 15  PHE A 20  1 ? 6 
HELX_P HELX_P3  3  PRO A 21  ? GLY A 25  ? PRO A 21  GLY A 25  5 ? 5 
HELX_P HELX_P4  4  LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P5  5  ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P6  6  LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P7  7  LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P8  8  ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P9  9  ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P10 10 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.994 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E V50 . N23 ? ? A ZN  301 A V50 304 1_555 ? ? ? ? ? ? ? 1.980 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -1.75 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 6.44  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O 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 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A MES 302 ? 5  'BINDING SITE FOR RESIDUE MES A 302' 
AC3 Software A DMS 303 ? 4  'BINDING SITE FOR RESIDUE DMS A 303' 
AC4 Software A V50 304 ? 15 'BINDING SITE FOR RESIDUE V50 A 304' 
# 
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  V50 E .   ? V50 A 304 . ? 1_555 ? 
5  AC2 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
6  AC2 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
7  AC2 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
8  AC2 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
9  AC2 5  HOH F .   ? HOH A 564 . ? 1_555 ? 
10 AC3 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
11 AC3 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
12 AC3 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
13 AC3 4  HOH F .   ? HOH A 655 . ? 1_555 ? 
14 AC4 15 GLN A 92  ? GLN A 92  . ? 1_555 ? 
15 AC4 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
16 AC4 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
17 AC4 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
18 AC4 15 VAL A 121 ? VAL A 121 . ? 1_555 ? 
19 AC4 15 PHE A 130 ? PHE A 131 . ? 1_555 ? 
20 AC4 15 VAL A 134 ? VAL A 135 . ? 1_555 ? 
21 AC4 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
22 AC4 15 THR A 198 ? THR A 199 . ? 1_555 ? 
23 AC4 15 THR A 199 ? THR A 200 . ? 1_555 ? 
24 AC4 15 PRO A 200 ? PRO A 201 . ? 1_555 ? 
25 AC4 15 PRO A 201 ? PRO A 202 . ? 1_555 ? 
26 AC4 15 TRP A 208 ? TRP A 209 . ? 1_555 ? 
27 AC4 15 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
28 AC4 15 HOH F .   ? HOH A 665 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4HT0 
_atom_sites.fract_transf_matrix[1][1]   0.023799 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005951 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024451 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.014396 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 9.519   1.102   8.367   1.00 26.40 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.380  -0.072  8.765   1.00 24.02 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.455   -1.063  9.497   1.00 21.51 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.581   -2.253  9.291   1.00 20.61 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 11.654  0.291   9.645   1.00 26.86 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 12.615  -0.858  9.862   1.00 27.67 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 12.691  -1.566  11.056  1.00 36.44 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 13.531  -1.431  9.033   1.00 37.07 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 13.605  -2.529  10.942  1.00 34.59 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 14.128  -2.468  9.728   1.00 37.71 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.564   -0.574  10.350  1.00 17.44 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.876   -1.547  11.262  1.00 13.42 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.854   -2.296  10.463  1.00 10.91 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.287   -1.807  9.460   1.00 13.68 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.189   -0.878  12.484  1.00 13.23 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 5.980   0.015   12.062  1.00 15.57 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.972   1.350   11.707  1.00 13.65 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.595   -0.411  11.991  1.00 11.22 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.663   1.800   11.489  1.00 16.97 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.821   0.712   11.579  1.00 14.22 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 3.934   -1.651  12.266  1.00 12.65 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.445   0.675   11.423  1.00 13.12 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.503   -1.677  12.049  1.00 11.02 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.791   -0.514  11.710  1.00 14.36 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.577   -3.493  10.954  1.00 12.88 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.542   -4.303  10.325  1.00 12.33 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.214   -5.455  11.257  1.00 13.69 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.254   -5.354  12.478  1.00 11.68 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 4.904   -6.612  10.627  1.00 15.13 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.533   -7.790  11.416  1.00 16.30 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.417   -9.043  11.268  1.00 21.59 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.095   -10.077 11.912  1.00 23.45 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.086   -8.121  11.159  1.00 14.96 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.167   -7.034  11.720  1.00 11.95 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.748   -7.056  13.056  1.00 12.70 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.715   -6.024  10.884  1.00 8.32  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 0.851   -6.020  13.531  1.00 9.35  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.812   -4.968  11.346  1.00 9.75  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.378   -5.053  12.689  1.00 9.28  ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.427  -4.089  13.162  1.00 8.84  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.533   -8.924  10.512  1.00 22.93 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.532   -10.071 10.443  1.00 21.91 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.522   -10.352 11.539  1.00 23.59 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.599   -9.681  12.634  1.00 25.62 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.401   -11.368 11.281  1.00 25.80 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.435  -11.799 12.300  1.00 25.73 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.351  -10.679 12.628  1.00 24.65 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.782  -10.576 13.813  1.00 25.37 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.308  -12.988 11.847  1.00 27.03 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 12.085  -13.678 12.968  0.01 25.90 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 12.964  -14.824 12.428  0.01 25.80 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 13.850  -15.435 13.516  0.01 25.69 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 13.047  -16.186 14.554  0.01 25.71 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 11.580  -9.841  11.604  1.00 22.63 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 12.581  -8.837  11.701  1.00 22.07 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 12.085  -7.459  12.011  1.00 19.31 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 12.862  -6.642  12.469  1.00 19.38 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 13.537  -8.913  10.480  1.00 21.59 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 14.317  -10.215 10.448  1.00 22.24 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 15.293  -10.530 11.379  1.00 27.75 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 14.222  -11.286 9.630   1.00 26.88 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 15.777  -11.730 11.121  1.00 25.12 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 15.137  -12.218 10.067  1.00 23.64 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 10.754  -7.237  11.880  1.00 18.36 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 10.238  -5.886  12.104  1.00 15.66 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 8.872   -5.924  12.850  1.00 14.76 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 8.189   -4.896  12.933  1.00 14.68 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 10.050  -5.126  10.803  1.00 15.21 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 8.986   -5.735  9.924   1.00 14.33 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 8.440   -6.805  10.235  1.00 18.57 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 8.660   -5.077  8.836   1.00 18.89 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 8.591   -7.078  13.415  1.00 14.05 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 7.265   -7.274  14.038  1.00 14.34 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 7.222   -6.677  15.435  1.00 12.93 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 8.121   -5.949  15.955  1.00 12.38 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 6.114   -6.966  16.140  1.00 13.49 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 5.876   -6.319  17.427  1.00 14.51 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 6.989   -6.304  18.458  1.00 10.44 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 7.107   -5.329  19.220  1.00 13.07 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 4.695   -7.159  17.991  1.00 14.44 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 3.888   -7.451  16.761  1.00 11.84 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 4.936   -7.714  15.638  1.00 12.18 ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 7.804   -7.359  18.535  1.00 12.07 ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 8.844   -7.383  19.523  1.00 14.41 ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 9.998   -6.434  19.179  1.00 13.12 ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 10.862  -6.166  20.061  1.00 14.42 ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 9.398   -8.818  19.594  1.00 16.20 ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 10.044  -9.268  18.239  1.00 21.10 ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 9.188   -9.910  17.092  1.00 28.23 ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 7.982   -9.604  17.023  1.00 19.22 ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 9.738   -10.705 16.306  1.00 25.09 ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 9.978   -5.954  17.930  1.00 12.79 ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 10.949  -4.922  17.462  1.00 11.98 ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 10.534  -3.487  17.635  1.00 13.69 ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 11.359  -2.583  17.579  1.00 11.43 ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 11.282  -5.112  15.982  1.00 13.14 ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 11.998  -6.396  15.781  1.00 17.09 ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 13.378  -6.513  15.950  1.00 20.01 ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 11.525  -7.637  15.500  1.00 17.43 ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 13.711  -7.787  15.775  1.00 21.33 ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 12.633  -8.481  15.475  1.00 20.82 ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 9.247   -3.253  17.886  1.00 10.92 ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 8.779   -1.915  17.813  1.00 10.81 ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 9.363   -0.963  18.818  1.00 9.71  ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 9.413   0.249   18.478  1.00 12.02 ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 7.229   -1.943  17.925  1.00 8.98  ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 6.587   -2.632  16.776  1.00 10.02 ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 7.125   -3.066  15.562  1.00 7.30  ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 5.125   -2.946  16.676  1.00 9.10  ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 6.138   -3.670  14.762  1.00 9.74  ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 4.911   -3.531  15.395  1.00 9.45  ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 4.045   -2.745  17.535  1.00 11.48 ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 3.644   -3.956  14.972  1.00 9.81  ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 2.801   -3.133  17.116  1.00 11.84 ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 2.577   -3.689  15.872  1.00 10.24 ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 9.774   -1.470  19.977  1.00 10.14 ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 10.253  -0.559  21.006  1.00 11.63 ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 11.467  0.253   20.555  1.00 11.50 ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 11.715  1.298   21.181  1.00 12.55 ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 10.545  -1.267  22.292  1.00 9.81  ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 11.715  -2.190  22.198  1.00 12.51 ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 12.940  -1.848  22.716  1.00 18.36 ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 11.868  -3.376  21.578  1.00 15.68 ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 13.805  -2.819  22.446  1.00 15.45 ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 13.189  -3.747  21.750  1.00 14.19 ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 18  ? 12.195  -0.300  19.569  1.00 13.54 ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 18  ? 13.484  0.380   19.221  1.00 14.21 ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 18  ? 13.121  1.681   18.532  1.00 16.41 ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 18  ? 13.774  2.713   18.822  1.00 19.19 ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 18  ? 14.279  -0.518  18.301  1.00 16.86 ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 18  ? 14.887  -1.649  19.027  1.00 15.29 ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 18  ? 15.603  -2.579  17.994  1.00 15.13 ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 18  ? 14.616  -3.630  17.354  1.00 16.21 ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 18  ? 15.256  -4.528  16.339  1.00 14.57 ? 18  LYS A NZ  1 
ATOM   135  N  N   . ASP A 1 19  ? 12.089  1.718   17.675  1.00 16.21 ? 19  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 19  ? 11.659  3.017   17.077  1.00 16.97 ? 19  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 19  ? 10.659  3.785   17.954  1.00 15.84 ? 19  ASP A C   1 
ATOM   138  O  O   . ASP A 1 19  ? 10.567  4.987   17.846  1.00 16.00 ? 19  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 19  ? 11.097  2.871   15.694  1.00 17.67 ? 19  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 19  ? 12.173  2.710   14.609  1.00 26.38 ? 19  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 19  ? 13.243  3.275   14.780  1.00 27.11 ? 19  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 19  ? 11.929  2.037   13.597  1.00 35.70 ? 19  ASP A OD2 1 
ATOM   143  N  N   . PHE A 1 20  ? 9.911   3.056   18.814  1.00 13.06 ? 20  PHE A N   1 
ATOM   144  C  CA  . PHE A 1 20  ? 8.764   3.619   19.530  1.00 13.14 ? 20  PHE A CA  1 
ATOM   145  C  C   . PHE A 1 20  ? 8.875   3.140   20.966  1.00 13.36 ? 20  PHE A C   1 
ATOM   146  O  O   . PHE A 1 20  ? 8.251   2.158   21.394  1.00 12.36 ? 20  PHE A O   1 
ATOM   147  C  CB  . PHE A 1 20  ? 7.493   3.082   18.871  1.00 12.50 ? 20  PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 20  ? 7.371   3.552   17.481  1.00 11.77 ? 20  PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 20  ? 6.948   4.868   17.218  1.00 17.54 ? 20  PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 20  ? 7.696   2.692   16.398  1.00 12.70 ? 20  PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 20  ? 6.847   5.284   15.927  1.00 14.97 ? 20  PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 20  ? 7.673   3.146   15.058  1.00 14.00 ? 20  PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 20  ? 7.224   4.463   14.831  1.00 15.63 ? 20  PHE A CZ  1 
ATOM   154  N  N   . PRO A 1 21  ? 9.738   3.778   21.761  1.00 14.05 ? 21  PRO A N   1 
ATOM   155  C  CA  . PRO A 1 21  ? 10.011  3.308   23.111  1.00 12.52 ? 21  PRO A CA  1 
ATOM   156  C  C   . PRO A 1 21  ? 8.790   3.164   24.004  1.00 12.13 ? 21  PRO A C   1 
ATOM   157  O  O   . PRO A 1 21  ? 8.829   2.432   24.947  1.00 12.85 ? 21  PRO A O   1 
ATOM   158  C  CB  . PRO A 1 21  ? 10.995  4.336   23.721  1.00 15.62 ? 21  PRO A CB  1 
ATOM   159  C  CG  . PRO A 1 21  ? 11.366  5.220   22.549  1.00 18.08 ? 21  PRO A CG  1 
ATOM   160  C  CD  . PRO A 1 21  ? 10.615  4.889   21.300  1.00 14.55 ? 21  PRO A CD  1 
ATOM   161  N  N   . ILE A 1 22  ? 7.733   3.955   23.702  1.00 10.73 ? 22  ILE A N   1 
ATOM   162  C  CA  . ILE A 1 22  ? 6.489   3.835   24.459  1.00 11.17 ? 22  ILE A CA  1 
ATOM   163  C  C   . ILE A 1 22  ? 5.856   2.405   24.300  1.00 8.47  ? 22  ILE A C   1 
ATOM   164  O  O   . ILE A 1 22  ? 4.912   2.084   25.033  1.00 9.29  ? 22  ILE A O   1 
ATOM   165  C  CB  . ILE A 1 22  ? 5.512   4.921   23.964  1.00 8.86  ? 22  ILE A CB  1 
ATOM   166  C  CG1 . ILE A 1 22  ? 4.464   5.212   24.991  1.00 10.57 ? 22  ILE A CG1 1 
ATOM   167  C  CG2 . ILE A 1 22  ? 4.897   4.508   22.580  1.00 12.07 ? 22  ILE A CG2 1 
ATOM   168  C  CD1 . ILE A 1 22  ? 3.463   6.308   24.558  1.00 15.33 ? 22  ILE A CD1 1 
ATOM   169  N  N   . ALA A 1 23  ? 6.397   1.588   23.400  1.00 9.80  ? 23  ALA A N   1 
ATOM   170  C  CA  . ALA A 1 23  ? 5.935   0.179   23.302  1.00 9.98  ? 23  ALA A CA  1 
ATOM   171  C  C   . ALA A 1 23  ? 6.014   -0.527  24.646  1.00 11.51 ? 23  ALA A C   1 
ATOM   172  O  O   . ALA A 1 23  ? 5.313   -1.515  24.848  1.00 10.80 ? 23  ALA A O   1 
ATOM   173  C  CB  . ALA A 1 23  ? 6.870   -0.641  22.310  1.00 12.19 ? 23  ALA A CB  1 
ATOM   174  N  N   . LYS A 1 24  ? 6.922   -0.115  25.550  1.00 11.68 ? 24  LYS A N   1 
ATOM   175  C  CA  . LYS A 1 24  ? 7.150   -0.770  26.865  1.00 12.80 ? 24  LYS A CA  1 
ATOM   176  C  C   . LYS A 1 24  ? 6.554   0.172   27.909  1.00 13.21 ? 24  LYS A C   1 
ATOM   177  O  O   . LYS A 1 24  ? 6.976   0.132   29.097  1.00 15.59 ? 24  LYS A O   1 
ATOM   178  C  CB  . LYS A 1 24  ? 8.677   -0.938  27.074  1.00 13.80 ? 24  LYS A CB  1 
ATOM   179  C  CG  . LYS A 1 24  ? 9.248   -1.945  26.210  1.00 16.97 ? 24  LYS A CG  1 
ATOM   180  C  CD  . LYS A 1 24  ? 10.707  -2.162  26.630  1.00 23.20 ? 24  LYS A CD  1 
ATOM   181  C  CE  . LYS A 1 24  ? 11.356  -3.092  25.629  1.00 21.99 ? 24  LYS A CE  1 
ATOM   182  N  NZ  . LYS A 1 24  ? 11.120  -4.529  26.057  1.00 24.11 ? 24  LYS A NZ  1 
ATOM   183  N  N   . GLY A 1 25  ? 5.540   0.999   27.529  1.00 11.63 ? 25  GLY A N   1 
ATOM   184  C  CA  . GLY A 1 25  ? 4.952   1.937   28.446  1.00 13.45 ? 25  GLY A CA  1 
ATOM   185  C  C   . GLY A 1 25  ? 3.975   1.359   29.457  1.00 11.67 ? 25  GLY A C   1 
ATOM   186  O  O   . GLY A 1 25  ? 3.769   0.125   29.544  1.00 15.06 ? 25  GLY A O   1 
ATOM   187  N  N   . GLU A 1 26  ? 3.344   2.279   30.190  1.00 13.05 ? 26  GLU A N   1 
ATOM   188  C  CA  . GLU A 1 26  ? 2.519   1.863   31.300  1.00 13.04 ? 26  GLU A CA  1 
ATOM   189  C  C   . GLU A 1 26  ? 1.076   1.580   30.957  1.00 12.33 ? 26  GLU A C   1 
ATOM   190  O  O   . GLU A 1 26  ? 0.341   1.057   31.800  1.00 13.47 ? 26  GLU A O   1 
ATOM   191  C  CB  . GLU A 1 26  ? 2.517   2.943   32.419  1.00 16.66 ? 26  GLU A CB  1 
ATOM   192  C  CG  . GLU A 1 26  ? 3.910   3.277   32.997  1.00 19.83 ? 26  GLU A CG  1 
ATOM   193  C  CD  . GLU A 1 26  ? 4.500   2.019   33.611  1.00 30.31 ? 26  GLU A CD  1 
ATOM   194  O  OE1 . GLU A 1 26  ? 3.835   1.373   34.509  1.00 33.00 ? 26  GLU A OE1 1 
ATOM   195  O  OE2 . GLU A 1 26  ? 5.608   1.634   33.161  1.00 34.93 ? 26  GLU A OE2 1 
ATOM   196  N  N   . ARG A 1 27  ? 0.650   1.931   29.725  1.00 11.08 ? 27  ARG A N   1 
ATOM   197  C  CA  . ARG A 1 27  ? -0.770  1.666   29.405  1.00 10.46 ? 27  ARG A CA  1 
ATOM   198  C  C   . ARG A 1 27  ? -0.870  1.182   27.922  1.00 8.22  ? 27  ARG A C   1 
ATOM   199  O  O   . ARG A 1 27  ? -1.587  1.788   27.105  1.00 8.55  ? 27  ARG A O   1 
ATOM   200  C  CB  . ARG A 1 27  ? -1.695  2.878   29.686  1.00 10.52 ? 27  ARG A CB  1 
ATOM   201  C  CG  . ARG A 1 27  ? -1.393  4.151   28.919  1.00 13.18 ? 27  ARG A CG  1 
ATOM   202  C  CD  . ARG A 1 27  ? -2.392  5.309   29.294  1.00 17.39 ? 27  ARG A CD  1 
ATOM   203  N  NE  . ARG A 1 27  ? -3.527  5.240   28.415  1.00 17.72 ? 27  ARG A NE  1 
ATOM   204  C  CZ  . ARG A 1 27  ? -4.442  6.191   28.252  1.00 13.94 ? 27  ARG A CZ  1 
ATOM   205  N  NH1 . ARG A 1 27  ? -4.343  7.336   28.915  1.00 15.47 ? 27  ARG A NH1 1 
ATOM   206  N  NH2 . ARG A 1 27  ? -5.442  6.004   27.406  1.00 13.59 ? 27  ARG A NH2 1 
ATOM   207  N  N   . GLN A 1 28  ? -0.157  0.116   27.595  1.00 8.99  ? 28  GLN A N   1 
ATOM   208  C  CA  . GLN A 1 28  ? -0.113  -0.352  26.189  1.00 6.64  ? 28  GLN A CA  1 
ATOM   209  C  C   . GLN A 1 28  ? -1.280  -1.347  25.982  1.00 7.26  ? 28  GLN A C   1 
ATOM   210  O  O   . GLN A 1 28  ? -1.783  -2.010  26.894  1.00 7.42  ? 28  GLN A O   1 
ATOM   211  C  CB  . GLN A 1 28  ? 1.201   -1.107  25.939  1.00 6.64  ? 28  GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 28  ? 2.371   -0.058  25.882  1.00 7.25  ? 28  GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 28  ? 2.221   0.798   24.549  1.00 6.89  ? 28  GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 28  ? 2.430   0.258   23.468  1.00 8.29  ? 28  GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 28  ? 1.856   2.094   24.662  1.00 7.49  ? 28  GLN A NE2 1 
ATOM   216  N  N   . SER A 1 29  ? -1.669  -1.410  24.714  1.00 5.98  ? 29  SER A N   1 
ATOM   217  C  CA  . SER A 1 29  ? -2.721  -2.336  24.228  1.00 6.78  ? 29  SER A CA  1 
ATOM   218  C  C   . SER A 1 29  ? -2.175  -3.198  23.074  1.00 5.37  ? 29  SER A C   1 
ATOM   219  O  O   . SER A 1 29  ? -1.222  -2.769  22.358  1.00 7.14  ? 29  SER A O   1 
ATOM   220  C  CB  . SER A 1 29  ? -3.853  -1.483  23.655  1.00 6.11  ? 29  SER A CB  1 
ATOM   221  O  OG  . SER A 1 29  ? -4.483  -0.798  24.804  1.00 6.40  ? 29  SER A OG  1 
ATOM   222  N  N   . PRO A 1 30  ? -2.817  -4.353  22.827  1.00 5.99  ? 30  PRO A N   1 
ATOM   223  C  CA  . PRO A 1 30  ? -3.954  -4.904  23.550  1.00 5.56  ? 30  PRO A CA  1 
ATOM   224  C  C   . PRO A 1 30  ? -3.583  -5.553  24.851  1.00 7.16  ? 30  PRO A C   1 
ATOM   225  O  O   . PRO A 1 30  ? -2.397  -5.573  25.198  1.00 7.77  ? 30  PRO A O   1 
ATOM   226  C  CB  . PRO A 1 30  ? -4.443  -5.968  22.553  1.00 7.11  ? 30  PRO A CB  1 
ATOM   227  C  CG  . PRO A 1 30  ? -3.162  -6.579  21.941  1.00 6.86  ? 30  PRO A CG  1 
ATOM   228  C  CD  . PRO A 1 30  ? -2.345  -5.252  21.759  1.00 7.40  ? 30  PRO A CD  1 
ATOM   229  N  N   . VAL A 1 31  ? -4.605  -6.079  25.543  1.00 6.02  ? 31  VAL A N   1 
ATOM   230  C  CA  . VAL A 1 31  ? -4.369  -6.845  26.745  1.00 7.92  ? 31  VAL A CA  1 
ATOM   231  C  C   . VAL A 1 31  ? -5.267  -8.067  26.766  1.00 9.56  ? 31  VAL A C   1 
ATOM   232  O  O   . VAL A 1 31  ? -6.216  -8.187  25.990  1.00 8.57  ? 31  VAL A O   1 
ATOM   233  C  CB  . VAL A 1 31  ? -4.682  -6.039  28.023  1.00 10.02 ? 31  VAL A CB  1 
ATOM   234  C  CG1 . VAL A 1 31  ? -3.704  -4.838  28.130  1.00 7.10  ? 31  VAL A CG1 1 
ATOM   235  C  CG2 . VAL A 1 31  ? -6.157  -5.600  28.132  1.00 9.17  ? 31  VAL A CG2 1 
ATOM   236  N  N   . ASP A 1 32  ? -4.903  -9.042  27.614  1.00 8.21  ? 32  ASP A N   1 
ATOM   237  C  CA  . ASP A 1 32  ? -5.838  -10.133 27.819  1.00 7.12  ? 32  ASP A CA  1 
ATOM   238  C  C   . ASP A 1 32  ? -6.894  -9.620  28.845  1.00 9.04  ? 32  ASP A C   1 
ATOM   239  O  O   . ASP A 1 32  ? -6.548  -8.974  29.846  1.00 9.44  ? 32  ASP A O   1 
ATOM   240  C  CB  . ASP A 1 32  ? -5.097  -11.312 28.405  1.00 8.68  ? 32  ASP A CB  1 
ATOM   241  C  CG  . ASP A 1 32  ? -6.027  -12.455 28.767  1.00 10.53 ? 32  ASP A CG  1 
ATOM   242  O  OD1 . ASP A 1 32  ? -6.729  -12.903 27.863  1.00 10.27 ? 32  ASP A OD1 1 
ATOM   243  O  OD2 . ASP A 1 32  ? -6.010  -12.909 29.986  1.00 14.18 ? 32  ASP A OD2 1 
ATOM   244  N  N   . ILE A 1 33  ? -8.159  -9.882  28.529  1.00 8.32  ? 33  ILE A N   1 
ATOM   245  C  CA  . ILE A 1 33  ? -9.275  -9.570  29.368  1.00 8.80  ? 33  ILE A CA  1 
ATOM   246  C  C   . ILE A 1 33  ? -9.568  -10.807 30.197  1.00 9.65  ? 33  ILE A C   1 
ATOM   247  O  O   . ILE A 1 33  ? -10.141 -11.809 29.681  1.00 9.58  ? 33  ILE A O   1 
ATOM   248  C  CB  . ILE A 1 33  ? -10.465 -9.162  28.541  1.00 9.91  ? 33  ILE A CB  1 
ATOM   249  C  CG1 . ILE A 1 33  ? -10.114 -7.895  27.754  1.00 8.67  ? 33  ILE A CG1 1 
ATOM   250  C  CG2 . ILE A 1 33  ? -11.651 -8.865  29.511  1.00 12.09 ? 33  ILE A CG2 1 
ATOM   251  C  CD1 . ILE A 1 33  ? -11.159 -7.520  26.652  1.00 9.63  ? 33  ILE A CD1 1 
ATOM   252  N  N   A ASP A 1 34  ? -9.111  -10.769 31.447  0.50 11.15 ? 34  ASP A N   1 
ATOM   253  N  N   B ASP A 1 34  ? -9.124  -10.721 31.461  0.50 10.57 ? 34  ASP A N   1 
ATOM   254  C  CA  A ASP A 1 34  ? -9.445  -11.912 32.345  0.50 11.14 ? 34  ASP A CA  1 
ATOM   255  C  CA  B ASP A 1 34  ? -9.458  -11.778 32.472  0.50 10.81 ? 34  ASP A CA  1 
ATOM   256  C  C   A ASP A 1 34  ? -10.826 -11.613 32.933  0.50 12.54 ? 34  ASP A C   1 
ATOM   257  C  C   B ASP A 1 34  ? -10.905 -11.523 32.930  0.50 12.02 ? 34  ASP A C   1 
ATOM   258  O  O   A ASP A 1 34  ? -10.946 -10.709 33.752  0.50 14.06 ? 34  ASP A O   1 
ATOM   259  O  O   B ASP A 1 34  ? -11.162 -10.547 33.644  0.50 13.79 ? 34  ASP A O   1 
ATOM   260  C  CB  A ASP A 1 34  ? -8.385  -12.022 33.436  0.50 12.81 ? 34  ASP A CB  1 
ATOM   261  C  CB  B ASP A 1 34  ? -8.480  -11.654 33.656  0.50 11.37 ? 34  ASP A CB  1 
ATOM   262  C  CG  A ASP A 1 34  ? -8.564  -13.271 34.274  0.50 15.06 ? 34  ASP A CG  1 
ATOM   263  C  CG  B ASP A 1 34  ? -8.622  -12.793 34.659  0.50 13.21 ? 34  ASP A CG  1 
ATOM   264  O  OD1 A ASP A 1 34  ? -9.039  -13.095 35.421  0.50 19.55 ? 34  ASP A OD1 1 
ATOM   265  O  OD1 B ASP A 1 34  ? -9.750  -13.259 34.869  0.50 11.70 ? 34  ASP A OD1 1 
ATOM   266  O  OD2 A ASP A 1 34  ? -8.264  -14.393 33.754  0.50 17.68 ? 34  ASP A OD2 1 
ATOM   267  O  OD2 B ASP A 1 34  ? -7.593  -13.220 35.223  0.50 17.98 ? 34  ASP A OD2 1 
ATOM   268  N  N   . THR A 1 35  ? -11.828 -12.344 32.461  1.00 13.25 ? 35  THR A N   1 
ATOM   269  C  CA  . THR A 1 35  ? -13.247 -12.013 32.669  1.00 14.58 ? 35  THR A CA  1 
ATOM   270  C  C   . THR A 1 35  ? -13.652 -12.166 34.093  1.00 14.30 ? 35  THR A C   1 
ATOM   271  O  O   . THR A 1 35  ? -14.613 -11.516 34.545  1.00 15.74 ? 35  THR A O   1 
ATOM   272  C  CB  . THR A 1 35  ? -14.178 -12.903 31.882  1.00 15.31 ? 35  THR A CB  1 
ATOM   273  O  OG1 . THR A 1 35  ? -14.074 -14.248 32.364  1.00 14.38 ? 35  THR A OG1 1 
ATOM   274  C  CG2 . THR A 1 35  ? -13.931 -12.865 30.423  1.00 13.30 ? 35  THR A CG2 1 
ATOM   275  N  N   . HIS A 1 36  ? -12.881 -12.979 34.842  1.00 15.06 ? 36  HIS A N   1 
ATOM   276  C  CA  . HIS A 1 36  ? -13.231 -13.188 36.238  1.00 16.82 ? 36  HIS A CA  1 
ATOM   277  C  C   . HIS A 1 36  ? -12.767 -12.042 37.101  1.00 18.25 ? 36  HIS A C   1 
ATOM   278  O  O   . HIS A 1 36  ? -13.431 -11.741 38.109  1.00 20.98 ? 36  HIS A O   1 
ATOM   279  C  CB  . HIS A 1 36  ? -12.667 -14.554 36.647  1.00 18.02 ? 36  HIS A CB  1 
ATOM   280  C  CG  . HIS A 1 36  ? -13.510 -15.649 36.101  1.00 17.71 ? 36  HIS A CG  1 
ATOM   281  N  ND1 . HIS A 1 36  ? -13.081 -16.496 35.095  1.00 21.78 ? 36  HIS A ND1 1 
ATOM   282  C  CD2 . HIS A 1 36  ? -14.827 -15.908 36.294  1.00 19.91 ? 36  HIS A CD2 1 
ATOM   283  C  CE1 . HIS A 1 36  ? -14.072 -17.301 34.776  1.00 20.49 ? 36  HIS A CE1 1 
ATOM   284  N  NE2 . HIS A 1 36  ? -15.143 -16.963 35.465  1.00 23.06 ? 36  HIS A NE2 1 
ATOM   285  N  N   . THR A 1 37  ? -11.661 -11.404 36.726  1.00 16.64 ? 37  THR A N   1 
ATOM   286  C  CA  . THR A 1 37  ? -11.129 -10.293 37.478  1.00 17.78 ? 37  THR A CA  1 
ATOM   287  C  C   . THR A 1 37  ? -11.532 -8.871  36.986  1.00 16.89 ? 37  THR A C   1 
ATOM   288  O  O   . THR A 1 37  ? -11.269 -7.872  37.650  1.00 17.90 ? 37  THR A O   1 
ATOM   289  C  CB  . THR A 1 37  ? -9.676  -10.394 37.737  1.00 20.51 ? 37  THR A CB  1 
ATOM   290  O  OG1 . THR A 1 37  ? -8.984  -10.399 36.531  1.00 24.11 ? 37  THR A OG1 1 
ATOM   291  C  CG2 . THR A 1 37  ? -9.334  -11.678 38.396  1.00 21.26 ? 37  THR A CG2 1 
ATOM   292  N  N   . ALA A 1 38  ? -12.244 -8.806  35.878  1.00 14.93 ? 38  ALA A N   1 
ATOM   293  C  CA  . ALA A 1 38  ? -12.782 -7.515  35.429  1.00 11.88 ? 38  ALA A CA  1 
ATOM   294  C  C   . ALA A 1 38  ? -13.847 -7.088  36.494  1.00 14.98 ? 38  ALA A C   1 
ATOM   295  O  O   . ALA A 1 38  ? -14.577 -7.933  36.992  1.00 17.74 ? 38  ALA A O   1 
ATOM   296  C  CB  . ALA A 1 38  ? -13.466 -7.721  34.050  1.00 14.39 ? 38  ALA A CB  1 
ATOM   297  N  N   . LYS A 1 39  ? -13.863 -5.822  36.872  1.00 15.11 ? 39  LYS A N   1 
ATOM   298  C  CA  . LYS A 1 39  ? -14.751 -5.337  37.915  1.00 16.33 ? 39  LYS A CA  1 
ATOM   299  C  C   . LYS A 1 39  ? -16.058 -4.891  37.253  1.00 16.52 ? 39  LYS A C   1 
ATOM   300  O  O   . LYS A 1 39  ? -16.080 -3.976  36.479  1.00 14.71 ? 39  LYS A O   1 
ATOM   301  C  CB  . LYS A 1 39  ? -14.030 -4.138  38.509  1.00 17.73 ? 39  LYS A CB  1 
ATOM   302  C  CG  . LYS A 1 39  ? -14.788 -3.287  39.573  1.00 19.80 ? 39  LYS A CG  1 
ATOM   303  C  CD  . LYS A 1 39  ? -14.924 -3.972  40.891  1.00 19.97 ? 39  LYS A CD  1 
ATOM   304  C  CE  . LYS A 1 39  ? -15.799 -3.180  41.837  1.00 22.49 ? 39  LYS A CE  1 
ATOM   305  N  NZ  . LYS A 1 39  ? -16.078 -3.997  43.020  1.00 25.57 ? 39  LYS A NZ  1 
ATOM   306  N  N   . TYR A 1 40  ? -17.177 -5.478  37.650  1.00 17.08 ? 40  TYR A N   1 
ATOM   307  C  CA  . TYR A 1 40  ? -18.438 -4.831  37.246  1.00 19.46 ? 40  TYR A CA  1 
ATOM   308  C  C   . TYR A 1 40  ? -18.575 -3.414  37.836  1.00 18.94 ? 40  TYR A C   1 
ATOM   309  O  O   . TYR A 1 40  ? -18.354 -3.168  39.075  1.00 18.13 ? 40  TYR A O   1 
ATOM   310  C  CB  . TYR A 1 40  ? -19.603 -5.726  37.638  1.00 20.97 ? 40  TYR A CB  1 
ATOM   311  C  CG  . TYR A 1 40  ? -20.928 -5.059  37.499  1.00 23.82 ? 40  TYR A CG  1 
ATOM   312  C  CD1 . TYR A 1 40  ? -21.430 -4.686  36.227  1.00 23.40 ? 40  TYR A CD1 1 
ATOM   313  C  CD2 . TYR A 1 40  ? -21.719 -4.870  38.628  1.00 29.24 ? 40  TYR A CD2 1 
ATOM   314  C  CE1 . TYR A 1 40  ? -22.621 -4.136  36.083  1.00 24.94 ? 40  TYR A CE1 1 
ATOM   315  C  CE2 . TYR A 1 40  ? -22.975 -4.279  38.504  1.00 23.99 ? 40  TYR A CE2 1 
ATOM   316  C  CZ  . TYR A 1 40  ? -23.405 -3.900  37.234  1.00 27.13 ? 40  TYR A CZ  1 
ATOM   317  O  OH  . TYR A 1 40  ? -24.632 -3.291  37.129  1.00 30.01 ? 40  TYR A OH  1 
ATOM   318  N  N   . ASP A 1 41  ? -18.997 -2.469  36.982  1.00 18.39 ? 41  ASP A N   1 
ATOM   319  C  CA  . ASP A 1 41  ? -19.144 -1.090  37.448  1.00 20.16 ? 41  ASP A CA  1 
ATOM   320  C  C   . ASP A 1 41  ? -20.575 -0.704  37.132  1.00 23.50 ? 41  ASP A C   1 
ATOM   321  O  O   . ASP A 1 41  ? -20.972 -0.521  35.947  1.00 21.46 ? 41  ASP A O   1 
ATOM   322  C  CB  . ASP A 1 41  ? -18.159 -0.129  36.828  1.00 23.07 ? 41  ASP A CB  1 
ATOM   323  C  CG  . ASP A 1 41  ? -18.313 1.296   37.388  1.00 24.23 ? 41  ASP A CG  1 
ATOM   324  O  OD1 . ASP A 1 41  ? -19.259 1.530   38.143  1.00 28.95 ? 41  ASP A OD1 1 
ATOM   325  O  OD2 . ASP A 1 41  ? -17.470 2.133   37.058  1.00 26.66 ? 41  ASP A OD2 1 
ATOM   326  N  N   . PRO A 1 42  ? -21.402 -0.649  38.197  1.00 26.20 ? 42  PRO A N   1 
ATOM   327  C  CA  . PRO A 1 42  ? -22.822 -0.449  37.951  1.00 26.36 ? 42  PRO A CA  1 
ATOM   328  C  C   . PRO A 1 42  ? -23.073 0.998   37.548  1.00 26.58 ? 42  PRO A C   1 
ATOM   329  O  O   . PRO A 1 42  ? -24.175 1.306   37.010  1.00 28.70 ? 42  PRO A O   1 
ATOM   330  C  CB  . PRO A 1 42  ? -23.458 -0.775  39.333  1.00 27.59 ? 42  PRO A CB  1 
ATOM   331  C  CG  . PRO A 1 42  ? -22.409 -0.153  40.289  1.00 26.71 ? 42  PRO A CG  1 
ATOM   332  C  CD  . PRO A 1 42  ? -21.087 -0.723  39.645  1.00 27.35 ? 42  PRO A CD  1 
ATOM   333  N  N   . SER A 1 43  ? -22.098 1.880   37.752  1.00 25.58 ? 43  SER A N   1 
ATOM   334  C  CA  . SER A 1 43  ? -22.235 3.269   37.287  1.00 26.76 ? 43  SER A CA  1 
ATOM   335  C  C   . SER A 1 43  ? -21.773 3.483   35.810  1.00 25.71 ? 43  SER A C   1 
ATOM   336  O  O   . SER A 1 43  ? -21.778 4.634   35.282  1.00 26.83 ? 43  SER A O   1 
ATOM   337  C  CB  . SER A 1 43  ? -21.419 4.193   38.165  1.00 28.21 ? 43  SER A CB  1 
ATOM   338  O  OG  . SER A 1 43  ? -20.028 4.031   37.846  1.00 29.16 ? 43  SER A OG  1 
ATOM   339  N  N   . LEU A 1 44  ? -21.324 2.411   35.137  1.00 24.90 ? 44  LEU A N   1 
ATOM   340  C  CA  . LEU A 1 44  ? -21.011 2.612   33.687  1.00 20.70 ? 44  LEU A CA  1 
ATOM   341  C  C   . LEU A 1 44  ? -22.329 2.722   32.933  1.00 21.69 ? 44  LEU A C   1 
ATOM   342  O  O   . LEU A 1 44  ? -23.195 1.922   33.148  1.00 23.03 ? 44  LEU A O   1 
ATOM   343  C  CB  . LEU A 1 44  ? -20.253 1.447   33.089  1.00 20.19 ? 44  LEU A CB  1 
ATOM   344  C  CG  . LEU A 1 44  ? -18.773 1.404   33.457  1.00 17.81 ? 44  LEU A CG  1 
ATOM   345  C  CD1 . LEU A 1 44  ? -18.299 -0.007  33.061  1.00 14.68 ? 44  LEU A CD1 1 
ATOM   346  C  CD2 . LEU A 1 44  ? -17.913 2.537   32.809  1.00 18.25 ? 44  LEU A CD2 1 
ATOM   347  N  N   . LYS A 1 45  ? -22.418 3.651   31.985  1.00 20.00 ? 45  LYS A N   1 
ATOM   348  C  CA  . LYS A 1 45  ? -23.699 3.858   31.243  1.00 19.92 ? 45  LYS A CA  1 
ATOM   349  C  C   . LYS A 1 45  ? -23.728 2.998   29.999  1.00 19.84 ? 45  LYS A C   1 
ATOM   350  O  O   . LYS A 1 45  ? -22.660 2.503   29.528  1.00 18.74 ? 45  LYS A O   1 
ATOM   351  C  CB  . LYS A 1 45  ? -23.778 5.298   30.763  1.00 20.57 ? 45  LYS A CB  1 
ATOM   352  C  CG  . LYS A 1 45  ? -23.689 6.417   31.845  1.00 24.31 ? 45  LYS A CG  1 
ATOM   353  C  CD  . LYS A 1 45  ? -24.626 7.585   31.542  0.01 23.34 ? 45  LYS A CD  1 
ATOM   354  C  CE  . LYS A 1 45  ? -24.128 8.450   30.392  0.01 23.50 ? 45  LYS A CE  1 
ATOM   355  N  NZ  . LYS A 1 45  ? -25.084 9.545   30.071  0.01 23.53 ? 45  LYS A NZ  1 
ATOM   356  N  N   . PRO A 1 46  ? -24.926 2.799   29.414  1.00 18.34 ? 46  PRO A N   1 
ATOM   357  C  CA  . PRO A 1 46  ? -24.987 2.121   28.125  1.00 17.60 ? 46  PRO A CA  1 
ATOM   358  C  C   . PRO A 1 46  ? -24.160 2.883   27.082  1.00 15.69 ? 46  PRO A C   1 
ATOM   359  O  O   . PRO A 1 46  ? -24.142 4.100   27.096  1.00 15.98 ? 46  PRO A O   1 
ATOM   360  C  CB  . PRO A 1 46  ? -26.481 2.125   27.756  1.00 17.92 ? 46  PRO A CB  1 
ATOM   361  C  CG  . PRO A 1 46  ? -27.152 2.230   29.068  1.00 20.66 ? 46  PRO A CG  1 
ATOM   362  C  CD  . PRO A 1 46  ? -26.273 3.115   29.945  1.00 19.18 ? 46  PRO A CD  1 
ATOM   363  N  N   . LEU A 1 47  ? -23.489 2.148   26.183  1.00 16.60 ? 47  LEU A N   1 
ATOM   364  C  CA  . LEU A 1 47  ? -22.744 2.774   25.121  1.00 14.74 ? 47  LEU A CA  1 
ATOM   365  C  C   . LEU A 1 47  ? -23.780 3.386   24.130  1.00 17.48 ? 47  LEU A C   1 
ATOM   366  O  O   . LEU A 1 47  ? -24.816 2.737   23.860  1.00 17.74 ? 47  LEU A O   1 
ATOM   367  C  CB  . LEU A 1 47  ? -21.859 1.730   24.455  1.00 17.66 ? 47  LEU A CB  1 
ATOM   368  C  CG  . LEU A 1 47  ? -20.938 2.216   23.384  1.00 20.99 ? 47  LEU A CG  1 
ATOM   369  C  CD1 . LEU A 1 47  ? -19.863 3.126   24.031  1.00 19.97 ? 47  LEU A CD1 1 
ATOM   370  C  CD2 . LEU A 1 47  ? -20.285 0.977   22.751  1.00 21.72 ? 47  LEU A CD2 1 
ATOM   371  N  N   . SER A 1 48  ? -23.538 4.591   23.672  1.00 13.92 ? 48  SER A N   1 
ATOM   372  C  CA  . SER A 1 48  ? -24.335 5.213   22.613  1.00 15.40 ? 48  SER A CA  1 
ATOM   373  C  C   . SER A 1 48  ? -23.586 5.208   21.316  1.00 15.82 ? 48  SER A C   1 
ATOM   374  O  O   . SER A 1 48  ? -22.627 5.958   21.134  1.00 14.59 ? 48  SER A O   1 
ATOM   375  C  CB  . SER A 1 48  ? -24.638 6.663   23.003  1.00 16.36 ? 48  SER A CB  1 
ATOM   376  O  OG  . SER A 1 48  ? -25.355 7.343   21.982  1.00 20.24 ? 48  SER A OG  1 
ATOM   377  N  N   . VAL A 1 49  ? -24.110 4.462   20.375  1.00 16.02 ? 49  VAL A N   1 
ATOM   378  C  CA  . VAL A 1 49  ? -23.557 4.389   19.041  1.00 16.48 ? 49  VAL A CA  1 
ATOM   379  C  C   . VAL A 1 49  ? -24.510 5.048   18.057  1.00 18.57 ? 49  VAL A C   1 
ATOM   380  O  O   . VAL A 1 49  ? -25.649 4.635   17.907  1.00 21.46 ? 49  VAL A O   1 
ATOM   381  C  CB  . VAL A 1 49  ? -23.301 2.927   18.644  1.00 18.27 ? 49  VAL A CB  1 
ATOM   382  C  CG1 . VAL A 1 49  ? -22.717 2.915   17.192  1.00 18.73 ? 49  VAL A CG1 1 
ATOM   383  C  CG2 . VAL A 1 49  ? -22.428 2.194   19.715  1.00 21.09 ? 49  VAL A CG2 1 
ATOM   384  N  N   . SER A 1 50  ? -24.152 6.170   17.521  1.00 16.86 ? 50  SER A N   1 
ATOM   385  C  CA  . SER A 1 50  ? -25.080 6.888   16.667  1.00 18.59 ? 50  SER A CA  1 
ATOM   386  C  C   . SER A 1 50  ? -24.489 6.980   15.336  1.00 18.23 ? 50  SER A C   1 
ATOM   387  O  O   . SER A 1 50  ? -23.758 7.916   15.031  1.00 17.54 ? 50  SER A O   1 
ATOM   388  C  CB  . SER A 1 50  ? -25.503 8.261   17.234  1.00 18.42 ? 50  SER A CB  1 
ATOM   389  O  OG  . SER A 1 50  ? -25.864 8.138   18.558  1.00 26.15 ? 50  SER A OG  1 
ATOM   390  N  N   . TYR A 1 51  ? -24.733 5.922   14.549  1.00 17.61 ? 51  TYR A N   1 
ATOM   391  C  CA  . TYR A 1 51  ? -24.185 5.789   13.217  1.00 14.76 ? 51  TYR A CA  1 
ATOM   392  C  C   . TYR A 1 51  ? -25.164 5.996   12.014  1.00 15.34 ? 51  TYR A C   1 
ATOM   393  O  O   . TYR A 1 51  ? -24.721 5.890   10.871  1.00 15.21 ? 51  TYR A O   1 
ATOM   394  C  CB  . TYR A 1 51  ? -23.530 4.422   13.026  1.00 16.42 ? 51  TYR A CB  1 
ATOM   395  C  CG  . TYR A 1 51  ? -22.237 4.125   13.783  1.00 15.82 ? 51  TYR A CG  1 
ATOM   396  C  CD1 . TYR A 1 51  ? -21.456 5.150   14.388  1.00 16.06 ? 51  TYR A CD1 1 
ATOM   397  C  CD2 . TYR A 1 51  ? -21.743 2.832   13.814  1.00 12.96 ? 51  TYR A CD2 1 
ATOM   398  C  CE1 . TYR A 1 51  ? -20.271 4.798   15.092  1.00 13.24 ? 51  TYR A CE1 1 
ATOM   399  C  CE2 . TYR A 1 51  ? -20.606 2.457   14.557  1.00 13.63 ? 51  TYR A CE2 1 
ATOM   400  C  CZ  . TYR A 1 51  ? -19.822 3.509   15.152  1.00 15.57 ? 51  TYR A CZ  1 
ATOM   401  O  OH  . TYR A 1 51  ? -18.660 3.208   15.820  1.00 12.53 ? 51  TYR A OH  1 
ATOM   402  N  N   . ASP A 1 52  ? -26.412 6.358   12.313  1.00 19.21 ? 52  ASP A N   1 
ATOM   403  C  CA  . ASP A 1 52  ? -27.424 6.630   11.244  1.00 20.92 ? 52  ASP A CA  1 
ATOM   404  C  C   . ASP A 1 52  ? -26.927 7.614   10.189  1.00 21.44 ? 52  ASP A C   1 
ATOM   405  O  O   . ASP A 1 52  ? -27.198 7.434   9.003   1.00 23.38 ? 52  ASP A O   1 
ATOM   406  C  CB  . ASP A 1 52  ? -28.760 7.086   11.845  1.00 23.63 ? 52  ASP A CB  1 
ATOM   407  C  CG  . ASP A 1 52  ? -28.575 8.165   12.882  1.00 25.61 ? 52  ASP A CG  1 
ATOM   408  O  OD1 . ASP A 1 52  ? -28.094 7.888   14.043  1.00 36.58 ? 52  ASP A OD1 1 
ATOM   409  O  OD2 . ASP A 1 52  ? -28.889 9.312   12.529  1.00 37.76 ? 52  ASP A OD2 1 
ATOM   410  N  N   . GLN A 1 53  ? -26.158 8.596   10.575  1.00 21.67 ? 53  GLN A N   1 
ATOM   411  C  CA  . GLN A 1 53  ? -25.755 9.546   9.524   1.00 23.57 ? 53  GLN A CA  1 
ATOM   412  C  C   . GLN A 1 53  ? -24.334 9.386   8.969   1.00 21.53 ? 53  GLN A C   1 
ATOM   413  O  O   . GLN A 1 53  ? -23.798 10.331  8.360   1.00 21.37 ? 53  GLN A O   1 
ATOM   414  C  CB  . GLN A 1 53  ? -26.041 10.959  9.982   1.00 24.97 ? 53  GLN A CB  1 
ATOM   415  C  CG  . GLN A 1 53  ? -27.603 11.256  10.047  1.00 30.36 ? 53  GLN A CG  1 
ATOM   416  C  CD  . GLN A 1 53  ? -28.280 10.955  8.687   1.00 38.09 ? 53  GLN A CD  1 
ATOM   417  O  OE1 . GLN A 1 53  ? -27.783 11.393  7.614   1.00 42.63 ? 53  GLN A OE1 1 
ATOM   418  N  NE2 . GLN A 1 53  ? -29.355 10.155  8.708   1.00 37.77 ? 53  GLN A NE2 1 
ATOM   419  N  N   . ALA A 1 54  ? -23.710 8.202   9.210   1.00 18.68 ? 54  ALA A N   1 
ATOM   420  C  CA  . ALA A 1 54  ? -22.390 7.907   8.783   1.00 15.16 ? 54  ALA A CA  1 
ATOM   421  C  C   . ALA A 1 54  ? -22.198 8.131   7.274   1.00 17.02 ? 54  ALA A C   1 
ATOM   422  O  O   . ALA A 1 54  ? -23.092 7.761   6.423   1.00 16.36 ? 54  ALA A O   1 
ATOM   423  C  CB  . ALA A 1 54  ? -22.009 6.466   9.167   1.00 15.12 ? 54  ALA A CB  1 
ATOM   424  N  N   . THR A 1 55  ? -21.112 8.795   6.948   1.00 14.07 ? 55  THR A N   1 
ATOM   425  C  CA  . THR A 1 55  ? -20.642 8.976   5.564   1.00 14.72 ? 55  THR A CA  1 
ATOM   426  C  C   . THR A 1 55  ? -19.357 8.297   5.294   1.00 14.13 ? 55  THR A C   1 
ATOM   427  O  O   . THR A 1 55  ? -18.315 8.852   5.587   1.00 12.32 ? 55  THR A O   1 
ATOM   428  C  CB  . THR A 1 55  ? -20.468 10.486  5.204   1.00 13.92 ? 55  THR A CB  1 
ATOM   429  O  OG1 . THR A 1 55  ? -21.755 11.044  5.261   1.00 18.92 ? 55  THR A OG1 1 
ATOM   430  C  CG2 . THR A 1 55  ? -19.936 10.588  3.716   1.00 15.91 ? 55  THR A CG2 1 
ATOM   431  N  N   . SER A 1 56  ? -19.368 7.043   4.772   1.00 14.25 ? 56  SER A N   1 
ATOM   432  C  CA  . SER A 1 56  ? -18.129 6.463   4.370   1.00 13.52 ? 56  SER A CA  1 
ATOM   433  C  C   . SER A 1 56  ? -17.607 7.127   3.127   1.00 15.27 ? 56  SER A C   1 
ATOM   434  O  O   . SER A 1 56  ? -18.448 7.621   2.309   1.00 17.55 ? 56  SER A O   1 
ATOM   435  C  CB  . SER A 1 56  ? -18.183 4.908   4.134   1.00 15.77 ? 56  SER A CB  1 
ATOM   436  O  OG  . SER A 1 56  ? -19.132 4.573   3.093   1.00 16.80 ? 56  SER A OG  1 
ATOM   437  N  N   . LEU A 1 57  ? -16.314 7.145   2.950   1.00 14.48 ? 57  LEU A N   1 
ATOM   438  C  CA  . LEU A 1 57  ? -15.792 7.774   1.768   1.00 15.86 ? 57  LEU A CA  1 
ATOM   439  C  C   . LEU A 1 57  ? -14.940 6.869   0.889   1.00 15.93 ? 57  LEU A C   1 
ATOM   440  O  O   . LEU A 1 57  ? -15.009 6.942   -0.370  1.00 15.97 ? 57  LEU A O   1 
ATOM   441  C  CB  . LEU A 1 57  ? -14.929 8.999   2.138   1.00 17.89 ? 57  LEU A CB  1 
ATOM   442  C  CG  . LEU A 1 57  ? -15.738 10.161  2.769   1.00 18.20 ? 57  LEU A CG  1 
ATOM   443  C  CD1 . LEU A 1 57  ? -14.805 11.249  3.201   1.00 20.45 ? 57  LEU A CD1 1 
ATOM   444  C  CD2 . LEU A 1 57  ? -16.923 10.749  1.884   1.00 19.13 ? 57  LEU A CD2 1 
ATOM   445  N  N   . ARG A 1 58  ? -14.021 6.152   1.549   1.00 13.84 ? 58  ARG A N   1 
ATOM   446  C  CA  . ARG A 1 58  ? -12.955 5.507   0.812   1.00 14.26 ? 58  ARG A CA  1 
ATOM   447  C  C   . ARG A 1 58  ? -12.559 4.294   1.618   1.00 13.90 ? 58  ARG A C   1 
ATOM   448  O  O   . ARG A 1 58  ? -12.706 4.286   2.844   1.00 13.63 ? 58  ARG A O   1 
ATOM   449  C  CB  . ARG A 1 58  ? -11.745 6.453   0.696   1.00 17.04 ? 58  ARG A CB  1 
ATOM   450  C  CG  . ARG A 1 58  ? -10.832 6.180   -0.376  1.00 19.57 ? 58  ARG A CG  1 
ATOM   451  C  CD  . ARG A 1 58  ? -9.967  7.440   -0.511  1.00 23.59 ? 58  ARG A CD  1 
ATOM   452  N  NE  . ARG A 1 58  ? -9.180  7.433   0.720   1.00 22.40 ? 58  ARG A NE  1 
ATOM   453  C  CZ  . ARG A 1 58  ? -7.851  7.511   0.733   1.00 23.70 ? 58  ARG A CZ  1 
ATOM   454  N  NH1 . ARG A 1 58  ? -7.207  7.669   -0.414  1.00 20.82 ? 58  ARG A NH1 1 
ATOM   455  N  NH2 . ARG A 1 58  ? -7.202  7.527   1.901   1.00 20.39 ? 58  ARG A NH2 1 
ATOM   456  N  N   . ILE A 1 59  ? -11.925 3.374   0.886   1.00 11.76 ? 59  ILE A N   1 
ATOM   457  C  CA  . ILE A 1 59  ? -11.308 2.262   1.551   1.00 13.14 ? 59  ILE A CA  1 
ATOM   458  C  C   . ILE A 1 59  ? -9.894  2.225   1.067   1.00 13.84 ? 59  ILE A C   1 
ATOM   459  O  O   . ILE A 1 59  ? -9.575  2.376   -0.138  1.00 14.35 ? 59  ILE A O   1 
ATOM   460  C  CB  . ILE A 1 59  ? -12.038 0.925   1.272   1.00 10.18 ? 59  ILE A CB  1 
ATOM   461  C  CG1 . ILE A 1 59  ? -11.379 -0.201  2.121   1.00 13.36 ? 59  ILE A CG1 1 
ATOM   462  C  CG2 . ILE A 1 59  ? -11.950 0.514   -0.227  1.00 12.46 ? 59  ILE A CG2 1 
ATOM   463  C  CD1 . ILE A 1 59  ? -12.365 -1.547  2.066   1.00 12.19 ? 59  ILE A CD1 1 
ATOM   464  N  N   . LEU A 1 60  ? -8.940  1.987   2.001   1.00 14.71 ? 60  LEU A N   1 
ATOM   465  C  CA  . LEU A 1 60  ? -7.545  2.117   1.724   1.00 13.06 ? 60  LEU A CA  1 
ATOM   466  C  C   . LEU A 1 60  ? -6.680  0.965   2.248   1.00 14.82 ? 60  LEU A C   1 
ATOM   467  O  O   . LEU A 1 60  ? -6.902  0.591   3.397   1.00 13.66 ? 60  LEU A O   1 
ATOM   468  C  CB  . LEU A 1 60  ? -7.018  3.466   2.377   1.00 13.46 ? 60  LEU A CB  1 
ATOM   469  C  CG  . LEU A 1 60  ? -5.521  3.661   2.288   1.00 13.73 ? 60  LEU A CG  1 
ATOM   470  C  CD1 . LEU A 1 60  ? -4.938  3.832   0.862   1.00 17.78 ? 60  LEU A CD1 1 
ATOM   471  C  CD2 . LEU A 1 60  ? -5.047  4.820   3.265   1.00 14.25 ? 60  LEU A CD2 1 
ATOM   472  N  N   . ASN A 1 61  ? -5.772  0.384   1.432   1.00 11.81 ? 61  ASN A N   1 
ATOM   473  C  CA  . ASN A 1 61  ? -4.780  -0.568  1.926   1.00 11.69 ? 61  ASN A CA  1 
ATOM   474  C  C   . ASN A 1 61  ? -3.557  0.252   2.280   1.00 14.98 ? 61  ASN A C   1 
ATOM   475  O  O   . ASN A 1 61  ? -2.952  0.890   1.405   1.00 15.32 ? 61  ASN A O   1 
ATOM   476  C  CB  . ASN A 1 61  ? -4.425  -1.650  0.883   1.00 11.73 ? 61  ASN A CB  1 
ATOM   477  C  CG  . ASN A 1 61  ? -3.322  -2.574  1.315   1.00 14.88 ? 61  ASN A CG  1 
ATOM   478  O  OD1 . ASN A 1 61  ? -2.427  -2.277  2.149   1.00 16.93 ? 61  ASN A OD1 1 
ATOM   479  N  ND2 . ASN A 1 61  ? -3.319  -3.792  0.695   1.00 14.95 ? 61  ASN A ND2 1 
ATOM   480  N  N   . ASN A 1 62  ? -3.279  0.368   3.574   1.00 13.89 ? 62  ASN A N   1 
ATOM   481  C  CA  . ASN A 1 62  ? -2.139  1.256   3.978   1.00 15.27 ? 62  ASN A CA  1 
ATOM   482  C  C   . ASN A 1 62  ? -0.901  0.392   4.226   1.00 16.08 ? 62  ASN A C   1 
ATOM   483  O  O   . ASN A 1 62  ? 0.167   0.875   4.787   1.00 20.05 ? 62  ASN A O   1 
ATOM   484  C  CB  . ASN A 1 62  ? -2.486  2.085   5.203   1.00 14.93 ? 62  ASN A CB  1 
ATOM   485  C  CG  . ASN A 1 62  ? -2.781  1.189   6.418   1.00 14.23 ? 62  ASN A CG  1 
ATOM   486  O  OD1 . ASN A 1 62  ? -2.463  -0.047  6.420   1.00 12.58 ? 62  ASN A OD1 1 
ATOM   487  N  ND2 . ASN A 1 62  ? -3.429  1.817   7.432   1.00 16.35 ? 62  ASN A ND2 1 
ATOM   488  N  N   . GLY A 1 63  ? -0.910  -0.864  3.794   1.00 14.68 ? 63  GLY A N   1 
ATOM   489  C  CA  . GLY A 1 63  ? 0.226   -1.661  4.076   1.00 10.93 ? 63  GLY A CA  1 
ATOM   490  C  C   . GLY A 1 63  ? 0.293   -2.429  5.411   1.00 11.67 ? 63  GLY A C   1 
ATOM   491  O  O   . GLY A 1 63  ? 1.178   -3.257  5.603   1.00 14.31 ? 63  GLY A O   1 
ATOM   492  N  N   A HIS A 1 64  ? -0.650  -2.132  6.290   0.50 10.92 ? 64  HIS A N   1 
ATOM   493  N  N   B HIS A 1 64  ? -0.598  -2.109  6.361   0.50 10.59 ? 64  HIS A N   1 
ATOM   494  C  CA  A HIS A 1 64  ? -0.677  -2.791  7.596   0.50 11.69 ? 64  HIS A CA  1 
ATOM   495  C  CA  B HIS A 1 64  ? -0.690  -2.914  7.638   0.50 10.95 ? 64  HIS A CA  1 
ATOM   496  C  C   A HIS A 1 64  ? -2.015  -3.518  7.734   0.50 12.10 ? 64  HIS A C   1 
ATOM   497  C  C   B HIS A 1 64  ? -2.100  -3.378  8.000   0.50 10.26 ? 64  HIS A C   1 
ATOM   498  O  O   A HIS A 1 64  ? -2.052  -4.755  8.087   0.50 12.15 ? 64  HIS A O   1 
ATOM   499  O  O   B HIS A 1 64  ? -2.281  -4.304  8.817   0.50 9.75  ? 64  HIS A O   1 
ATOM   500  C  CB  A HIS A 1 64  ? -0.437  -1.729  8.667   0.50 11.47 ? 64  HIS A CB  1 
ATOM   501  C  CB  B HIS A 1 64  ? -0.076  -2.229  8.861   0.50 11.38 ? 64  HIS A CB  1 
ATOM   502  C  CG  A HIS A 1 64  ? 0.907   -1.063  8.528   0.50 12.47 ? 64  HIS A CG  1 
ATOM   503  C  CG  B HIS A 1 64  ? -0.532  -0.819  9.096   0.50 13.51 ? 64  HIS A CG  1 
ATOM   504  N  ND1 A HIS A 1 64  ? 2.079   -1.754  8.713   0.50 14.55 ? 64  HIS A ND1 1 
ATOM   505  N  ND1 B HIS A 1 64  ? 0.138   0.267   8.551   0.50 15.09 ? 64  HIS A ND1 1 
ATOM   506  C  CD2 A HIS A 1 64  ? 1.266   0.204   8.212   0.50 15.27 ? 64  HIS A CD2 1 
ATOM   507  C  CD2 B HIS A 1 64  ? -1.513  -0.303  9.885   0.50 15.95 ? 64  HIS A CD2 1 
ATOM   508  C  CE1 A HIS A 1 64  ? 3.110   -0.942  8.561   0.50 12.34 ? 64  HIS A CE1 1 
ATOM   509  C  CE1 B HIS A 1 64  ? -0.438  1.384   8.971   0.50 17.46 ? 64  HIS A CE1 1 
ATOM   510  N  NE2 A HIS A 1 64  ? 2.646   0.246   8.239   0.50 11.42 ? 64  HIS A NE2 1 
ATOM   511  N  NE2 B HIS A 1 64  ? -1.416  1.066   9.806   0.50 17.32 ? 64  HIS A NE2 1 
ATOM   512  N  N   . ALA A 1 65  ? -3.064  -2.805  7.311   1.00 11.88 ? 65  ALA A N   1 
ATOM   513  C  CA  . ALA A 1 65  ? -4.455  -3.286  7.291   1.00 10.87 ? 65  ALA A CA  1 
ATOM   514  C  C   . ALA A 1 65  ? -5.197  -2.548  6.168   1.00 10.80 ? 65  ALA A C   1 
ATOM   515  O  O   . ALA A 1 65  ? -4.554  -1.881  5.291   1.00 12.55 ? 65  ALA A O   1 
ATOM   516  C  CB  . ALA A 1 65  ? -5.117  -3.023  8.665   1.00 9.86  ? 65  ALA A CB  1 
ATOM   517  N  N   . PHE A 1 66  ? -6.512  -2.695  6.113   1.00 9.80  ? 66  PHE A N   1 
ATOM   518  C  CA  . PHE A 1 66  ? -7.266  -1.747  5.231   1.00 11.08 ? 66  PHE A CA  1 
ATOM   519  C  C   . PHE A 1 66  ? -8.167  -0.901  6.086   1.00 11.53 ? 66  PHE A C   1 
ATOM   520  O  O   . PHE A 1 66  ? -8.810  -1.397  7.052   1.00 10.56 ? 66  PHE A O   1 
ATOM   521  C  CB  . PHE A 1 66  ? -8.054  -2.462  4.120   1.00 10.84 ? 66  PHE A CB  1 
ATOM   522  C  CG  . PHE A 1 66  ? -9.135  -3.410  4.643   1.00 8.28  ? 66  PHE A CG  1 
ATOM   523  C  CD1 . PHE A 1 66  ? -10.402 -2.954  4.984   1.00 10.53 ? 66  PHE A CD1 1 
ATOM   524  C  CD2 . PHE A 1 66  ? -8.825  -4.778  4.790   1.00 12.24 ? 66  PHE A CD2 1 
ATOM   525  C  CE1 . PHE A 1 66  ? -11.361 -3.839  5.469   1.00 12.20 ? 66  PHE A CE1 1 
ATOM   526  C  CE2 . PHE A 1 66  ? -9.811  -5.636  5.390   1.00 9.70  ? 66  PHE A CE2 1 
ATOM   527  C  CZ  . PHE A 1 66  ? -11.026 -5.188  5.693   1.00 11.97 ? 66  PHE A CZ  1 
ATOM   528  N  N   . ASN A 1 67  ? -8.277  0.406   5.795   1.00 10.88 ? 67  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 67  ? -9.125  1.268   6.610   1.00 10.42 ? 67  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 67  ? -10.356 1.670   5.802   1.00 11.52 ? 67  ASN A C   1 
ATOM   531  O  O   . ASN A 1 67  ? -10.172 2.092   4.649   1.00 13.00 ? 67  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 67  ? -8.422  2.574   6.925   1.00 9.95  ? 67  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 67  ? -7.350  2.396   7.982   1.00 10.69 ? 67  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 67  ? -7.105  1.251   8.435   1.00 12.91 ? 67  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 67  ? -6.518  3.448   8.174   1.00 13.37 ? 67  ASN A ND2 1 
ATOM   536  N  N   . VAL A 1 68  ? -11.542 1.589   6.355   1.00 10.73 ? 68  VAL A N   1 
ATOM   537  C  CA  . VAL A 1 68  ? -12.719 2.198   5.709   1.00 10.50 ? 68  VAL A CA  1 
ATOM   538  C  C   . VAL A 1 68  ? -12.838 3.581   6.401   1.00 14.60 ? 68  VAL A C   1 
ATOM   539  O  O   . VAL A 1 68  ? -13.028 3.647   7.642   1.00 11.11 ? 68  VAL A O   1 
ATOM   540  C  CB  . VAL A 1 68  ? -13.960 1.397   5.853   1.00 11.72 ? 68  VAL A CB  1 
ATOM   541  C  CG1 . VAL A 1 68  ? -15.188 2.229   5.382   1.00 13.52 ? 68  VAL A CG1 1 
ATOM   542  C  CG2 . VAL A 1 68  ? -13.820 0.076   5.087   1.00 12.92 ? 68  VAL A CG2 1 
ATOM   543  N  N   . GLU A 1 69  ? -12.624 4.682   5.627   1.00 14.93 ? 69  GLU A N   1 
ATOM   544  C  CA  . GLU A 1 69  ? -12.571 6.073   6.181   1.00 13.77 ? 69  GLU A CA  1 
ATOM   545  C  C   . GLU A 1 69  ? -13.949 6.716   6.066   1.00 15.84 ? 69  GLU A C   1 
ATOM   546  O  O   . GLU A 1 69  ? -14.781 6.424   5.092   1.00 15.51 ? 69  GLU A O   1 
ATOM   547  C  CB  . GLU A 1 69  ? -11.613 6.881   5.335   1.00 14.05 ? 69  GLU A CB  1 
ATOM   548  C  CG  . GLU A 1 69  ? -10.280 6.317   5.337   1.00 16.11 ? 69  GLU A CG  1 
ATOM   549  C  CD  . GLU A 1 69  ? -9.503  6.831   4.224   1.00 22.00 ? 69  GLU A CD  1 
ATOM   550  O  OE1 . GLU A 1 69  ? -10.142 7.514   3.340   1.00 20.95 ? 69  GLU A OE1 1 
ATOM   551  O  OE2 . GLU A 1 69  ? -8.270  6.542   4.248   1.00 17.98 ? 69  GLU A OE2 1 
ATOM   552  N  N   . PHE A 1 70  ? -14.198 7.606   7.013   1.00 12.00 ? 70  PHE A N   1 
ATOM   553  C  CA  . PHE A 1 70  ? -15.478 8.308   7.065   1.00 13.36 ? 70  PHE A CA  1 
ATOM   554  C  C   . PHE A 1 70  ? -15.227 9.795   7.031   1.00 13.07 ? 70  PHE A C   1 
ATOM   555  O  O   . PHE A 1 70  ? -14.154 10.234  7.411   1.00 12.72 ? 70  PHE A O   1 
ATOM   556  C  CB  . PHE A 1 70  ? -16.221 7.947   8.325   1.00 12.79 ? 70  PHE A CB  1 
ATOM   557  C  CG  . PHE A 1 70  ? -16.764 6.555   8.287   1.00 11.41 ? 70  PHE A CG  1 
ATOM   558  C  CD1 . PHE A 1 70  ? -15.876 5.446   8.446   1.00 10.34 ? 70  PHE A CD1 1 
ATOM   559  C  CD2 . PHE A 1 70  ? -18.075 6.341   7.950   1.00 10.30 ? 70  PHE A CD2 1 
ATOM   560  C  CE1 . PHE A 1 70  ? -16.378 4.111   8.319   1.00 12.34 ? 70  PHE A CE1 1 
ATOM   561  C  CE2 . PHE A 1 70  ? -18.580 5.057   7.834   1.00 10.61 ? 70  PHE A CE2 1 
ATOM   562  C  CZ  . PHE A 1 70  ? -17.696 3.935   8.034   1.00 13.79 ? 70  PHE A CZ  1 
ATOM   563  N  N   . ASP A 1 71  ? -16.272 10.519  6.599   1.00 13.69 ? 71  ASP A N   1 
ATOM   564  C  CA  . ASP A 1 71  ? -16.240 11.985  6.788   1.00 14.19 ? 71  ASP A CA  1 
ATOM   565  C  C   . ASP A 1 71  ? -16.440 12.339  8.268   1.00 13.69 ? 71  ASP A C   1 
ATOM   566  O  O   . ASP A 1 71  ? -17.467 12.099  8.887   1.00 15.93 ? 71  ASP A O   1 
ATOM   567  C  CB  . ASP A 1 71  ? -17.371 12.598  5.934   1.00 12.58 ? 71  ASP A CB  1 
ATOM   568  C  CG  . ASP A 1 71  ? -17.558 14.108  6.240   1.00 16.61 ? 71  ASP A CG  1 
ATOM   569  O  OD1 . ASP A 1 71  ? -16.622 14.735  6.820   1.00 15.73 ? 71  ASP A OD1 1 
ATOM   570  O  OD2 . ASP A 1 71  ? -18.658 14.643  5.983   1.00 20.91 ? 71  ASP A OD2 1 
ATOM   571  N  N   . ASP A 1 72  ? -15.360 12.854  8.867   1.00 13.39 ? 72  ASP A N   1 
ATOM   572  C  CA  . ASP A 1 72  ? -15.410 13.197  10.278  1.00 12.97 ? 72  ASP A CA  1 
ATOM   573  C  C   . ASP A 1 72  ? -15.338 14.723  10.461  1.00 15.88 ? 72  ASP A C   1 
ATOM   574  O  O   . ASP A 1 72  ? -14.867 15.174  11.480  1.00 13.74 ? 72  ASP A O   1 
ATOM   575  C  CB  . ASP A 1 72  ? -14.218 12.513  11.048  1.00 13.04 ? 72  ASP A CB  1 
ATOM   576  C  CG  . ASP A 1 72  ? -12.854 13.053  10.612  1.00 14.90 ? 72  ASP A CG  1 
ATOM   577  O  OD1 . ASP A 1 72  ? -12.737 13.728  9.531   1.00 14.59 ? 72  ASP A OD1 1 
ATOM   578  O  OD2 . ASP A 1 72  ? -11.804 12.733  11.264  1.00 15.65 ? 72  ASP A OD2 1 
ATOM   579  N  N   . SER A 1 73  ? -15.871 15.457  9.480   1.00 14.72 ? 73  SER A N   1 
ATOM   580  C  CA  . SER A 1 73  ? -15.778 16.954  9.493   1.00 15.04 ? 73  SER A CA  1 
ATOM   581  C  C   . SER A 1 73  ? -17.089 17.506  10.084  1.00 17.19 ? 73  SER A C   1 
ATOM   582  O  O   . SER A 1 73  ? -17.252 18.736  10.236  1.00 17.29 ? 73  SER A O   1 
ATOM   583  C  CB  . SER A 1 73  ? -15.501 17.474  8.076   1.00 17.00 ? 73  SER A CB  1 
ATOM   584  O  OG  . SER A 1 73  ? -16.703 17.352  7.345   1.00 15.30 ? 73  SER A OG  1 
ATOM   585  N  N   . GLN A 1 74  ? -17.990 16.610  10.534  1.00 15.96 ? 74  GLN A N   1 
ATOM   586  C  CA  . GLN A 1 74  ? -19.155 17.014  11.270  1.00 18.44 ? 74  GLN A CA  1 
ATOM   587  C  C   . GLN A 1 74  ? -19.556 15.835  12.161  1.00 19.23 ? 74  GLN A C   1 
ATOM   588  O  O   . GLN A 1 74  ? -19.024 14.725  11.959  1.00 18.93 ? 74  GLN A O   1 
ATOM   589  C  CB  . GLN A 1 74  ? -20.336 17.275  10.298  1.00 20.27 ? 74  GLN A CB  1 
ATOM   590  C  CG  . GLN A 1 74  ? -20.326 18.474  9.462   1.00 24.65 ? 74  GLN A CG  1 
ATOM   591  C  CD  . GLN A 1 74  ? -21.687 18.521  8.765   1.00 24.53 ? 74  GLN A CD  1 
ATOM   592  O  OE1 . GLN A 1 74  ? -22.662 19.076  9.312   1.00 34.34 ? 74  GLN A OE1 1 
ATOM   593  N  NE2 . GLN A 1 74  ? -21.788 17.871  7.637   1.00 21.20 ? 74  GLN A NE2 1 
ATOM   594  N  N   . ASP A 1 75  ? -20.464 16.065  13.123  1.00 19.91 ? 75  ASP A N   1 
ATOM   595  C  CA  . ASP A 1 75  ? -20.890 14.973  14.018  1.00 21.83 ? 75  ASP A CA  1 
ATOM   596  C  C   . ASP A 1 75  ? -21.909 14.141  13.223  1.00 22.58 ? 75  ASP A C   1 
ATOM   597  O  O   . ASP A 1 75  ? -23.116 14.467  13.227  1.00 28.48 ? 75  ASP A O   1 
ATOM   598  C  CB  . ASP A 1 75  ? -21.486 15.490  15.319  1.00 23.73 ? 75  ASP A CB  1 
ATOM   599  C  CG  . ASP A 1 75  ? -20.432 15.973  16.299  1.00 25.63 ? 75  ASP A CG  1 
ATOM   600  O  OD1 . ASP A 1 75  ? -19.239 16.018  15.913  1.00 29.70 ? 75  ASP A OD1 1 
ATOM   601  O  OD2 . ASP A 1 75  ? -20.799 16.312  17.451  1.00 37.34 ? 75  ASP A OD2 1 
ATOM   602  N  N   . LYS A 1 76  ? -21.460 13.096  12.565  1.00 21.02 ? 76  LYS A N   1 
ATOM   603  C  CA  . LYS A 1 76  ? -22.343 12.223  11.752  1.00 19.78 ? 76  LYS A CA  1 
ATOM   604  C  C   . LYS A 1 76  ? -22.405 10.750  12.175  1.00 20.58 ? 76  LYS A C   1 
ATOM   605  O  O   . LYS A 1 76  ? -23.399 10.004  11.952  1.00 22.69 ? 76  LYS A O   1 
ATOM   606  C  CB  . LYS A 1 76  ? -21.764 12.140  10.367  1.00 18.72 ? 76  LYS A CB  1 
ATOM   607  C  CG  . LYS A 1 76  ? -22.076 13.334  9.579   1.00 21.94 ? 76  LYS A CG  1 
ATOM   608  C  CD  . LYS A 1 76  ? -21.353 13.200  8.292   1.00 20.62 ? 76  LYS A CD  1 
ATOM   609  C  CE  . LYS A 1 76  ? -21.952 14.193  7.340   1.00 24.75 ? 76  LYS A CE  1 
ATOM   610  N  NZ  . LYS A 1 76  ? -21.516 13.956  6.022   1.00 22.22 ? 76  LYS A NZ  1 
ATOM   611  N  N   . ALA A 1 77  ? -21.302 10.295  12.695  1.00 17.47 ? 77  ALA A N   1 
ATOM   612  C  CA  . ALA A 1 77  ? -21.159 8.903   13.202  1.00 15.19 ? 77  ALA A CA  1 
ATOM   613  C  C   . ALA A 1 77  ? -20.371 9.144   14.510  1.00 15.96 ? 77  ALA A C   1 
ATOM   614  O  O   . ALA A 1 77  ? -19.209 9.402   14.438  1.00 16.93 ? 77  ALA A O   1 
ATOM   615  C  CB  . ALA A 1 77  ? -20.264 8.129   12.221  1.00 14.70 ? 77  ALA A CB  1 
ATOM   616  N  N   . VAL A 1 78  ? -21.036 9.067   15.629  1.00 12.81 ? 78  VAL A N   1 
ATOM   617  C  CA  . VAL A 1 78  ? -20.412 9.381   16.949  1.00 13.77 ? 78  VAL A CA  1 
ATOM   618  C  C   . VAL A 1 78  ? -20.687 8.299   17.994  1.00 14.61 ? 78  VAL A C   1 
ATOM   619  O  O   . VAL A 1 78  ? -21.720 7.607   18.040  1.00 14.28 ? 78  VAL A O   1 
ATOM   620  C  CB  . VAL A 1 78  ? -20.854 10.737  17.558  1.00 16.01 ? 78  VAL A CB  1 
ATOM   621  C  CG1 . VAL A 1 78  ? -20.453 11.992  16.627  1.00 18.27 ? 78  VAL A CG1 1 
ATOM   622  C  CG2 . VAL A 1 78  ? -22.284 10.615  17.976  1.00 18.81 ? 78  VAL A CG2 1 
ATOM   623  N  N   . LEU A 1 79  ? -19.689 8.179   18.853  1.00 11.31 ? 79  LEU A N   1 
ATOM   624  C  CA  . LEU A 1 79  ? -19.763 7.322   19.979  1.00 12.40 ? 79  LEU A CA  1 
ATOM   625  C  C   . LEU A 1 79  ? -19.764 8.238   21.204  1.00 13.88 ? 79  LEU A C   1 
ATOM   626  O  O   . LEU A 1 79  ? -19.032 9.249   21.314  1.00 12.26 ? 79  LEU A O   1 
ATOM   627  C  CB  . LEU A 1 79  ? -18.533 6.360   19.958  1.00 13.65 ? 79  LEU A CB  1 
ATOM   628  C  CG  . LEU A 1 79  ? -18.404 5.407   21.071  1.00 14.77 ? 79  LEU A CG  1 
ATOM   629  C  CD1 . LEU A 1 79  ? -19.494 4.345   20.874  1.00 18.19 ? 79  LEU A CD1 1 
ATOM   630  C  CD2 . LEU A 1 79  ? -17.075 4.628   21.028  1.00 11.23 ? 79  LEU A CD2 1 
ATOM   631  N  N   . LYS A 1 80  ? -20.629 7.958   22.123  1.00 12.99 ? 80  LYS A N   1 
ATOM   632  C  CA  . LYS A 1 80  ? -20.590 8.647   23.437  1.00 15.56 ? 80  LYS A CA  1 
ATOM   633  C  C   . LYS A 1 80  ? -21.223 7.755   24.487  1.00 14.07 ? 80  LYS A C   1 
ATOM   634  O  O   . LYS A 1 80  ? -21.530 6.573   24.191  1.00 12.91 ? 80  LYS A O   1 
ATOM   635  C  CB  . LYS A 1 80  ? -21.260 10.024  23.360  1.00 18.65 ? 80  LYS A CB  1 
ATOM   636  C  CG  . LYS A 1 80  ? -22.590 9.961   22.673  1.00 22.40 ? 80  LYS A CG  1 
ATOM   637  C  CD  . LYS A 1 80  ? -23.285 11.399  22.462  1.00 21.72 ? 80  LYS A CD  1 
ATOM   638  C  CE  . LYS A 1 80  ? -22.930 12.177  21.178  1.00 30.97 ? 80  LYS A CE  1 
ATOM   639  N  NZ  . LYS A 1 80  ? -24.017 13.170  20.675  1.00 31.40 ? 80  LYS A NZ  1 
ATOM   640  N  N   . GLY A 1 81  ? -21.415 8.289   25.697  1.00 14.05 ? 81  GLY A N   1 
ATOM   641  C  CA  . GLY A 1 81  ? -21.896 7.521   26.833  1.00 13.50 ? 81  GLY A CA  1 
ATOM   642  C  C   . GLY A 1 81  ? -20.927 6.414   27.131  1.00 15.83 ? 81  GLY A C   1 
ATOM   643  O  O   . GLY A 1 81  ? -19.727 6.604   26.948  1.00 13.85 ? 81  GLY A O   1 
ATOM   644  N  N   . GLY A 1 82  ? -21.403 5.253   27.547  1.00 16.12 ? 82  GLY A N   1 
ATOM   645  C  CA  . GLY A 1 82  ? -20.470 4.222   28.004  1.00 15.68 ? 82  GLY A CA  1 
ATOM   646  C  C   . GLY A 1 82  ? -19.586 4.813   29.121  1.00 14.45 ? 82  GLY A C   1 
ATOM   647  O  O   . GLY A 1 82  ? -20.079 5.523   30.027  1.00 19.53 ? 82  GLY A O   1 
ATOM   648  N  N   . PRO A 1 83  ? -18.221 4.600   29.062  1.00 13.86 ? 83  PRO A N   1 
ATOM   649  C  CA  . PRO A 1 83  ? -17.303 5.197   30.006  1.00 12.95 ? 83  PRO A CA  1 
ATOM   650  C  C   . PRO A 1 83  ? -16.890 6.615   29.598  1.00 15.18 ? 83  PRO A C   1 
ATOM   651  O  O   . PRO A 1 83  ? -16.137 7.268   30.299  1.00 17.70 ? 83  PRO A O   1 
ATOM   652  C  CB  . PRO A 1 83  ? -16.041 4.296   29.896  1.00 15.06 ? 83  PRO A CB  1 
ATOM   653  C  CG  . PRO A 1 83  ? -16.066 3.900   28.472  1.00 10.82 ? 83  PRO A CG  1 
ATOM   654  C  CD  . PRO A 1 83  ? -17.516 3.770   28.037  1.00 12.05 ? 83  PRO A CD  1 
ATOM   655  N  N   . LEU A 1 84  ? -17.416 7.123   28.499  1.00 13.33 ? 84  LEU A N   1 
ATOM   656  C  CA  . LEU A 1 84  ? -16.853 8.348   27.930  1.00 13.71 ? 84  LEU A CA  1 
ATOM   657  C  C   . LEU A 1 84  ? -17.544 9.601   28.523  1.00 17.13 ? 84  LEU A C   1 
ATOM   658  O  O   . LEU A 1 84  ? -18.760 9.599   28.722  1.00 17.54 ? 84  LEU A O   1 
ATOM   659  C  CB  . LEU A 1 84  ? -17.050 8.361   26.437  1.00 11.43 ? 84  LEU A CB  1 
ATOM   660  C  CG  . LEU A 1 84  ? -16.487 7.062   25.777  1.00 10.48 ? 84  LEU A CG  1 
ATOM   661  C  CD1 . LEU A 1 84  ? -16.937 6.932   24.349  1.00 14.39 ? 84  LEU A CD1 1 
ATOM   662  C  CD2 . LEU A 1 84  ? -14.852 7.064   25.890  1.00 13.98 ? 84  LEU A CD2 1 
ATOM   663  N  N   . ASP A 1 85  ? -16.735 10.662  28.573  1.00 20.34 ? 85  ASP A N   1 
ATOM   664  C  CA  . ASP A 1 85  ? -17.196 12.049  28.694  1.00 24.17 ? 85  ASP A CA  1 
ATOM   665  C  C   . ASP A 1 85  ? -17.259 12.692  27.305  1.00 24.03 ? 85  ASP A C   1 
ATOM   666  O  O   . ASP A 1 85  ? -16.305 12.695  26.492  1.00 27.42 ? 85  ASP A O   1 
ATOM   667  C  CB  . ASP A 1 85  ? -16.295 12.816  29.688  1.00 25.64 ? 85  ASP A CB  1 
ATOM   668  C  CG  . ASP A 1 85  ? -16.329 12.222  31.071  1.00 32.97 ? 85  ASP A CG  1 
ATOM   669  O  OD1 . ASP A 1 85  ? -17.425 11.781  31.529  1.00 33.70 ? 85  ASP A OD1 1 
ATOM   670  O  OD2 . ASP A 1 85  ? -15.264 12.269  31.767  1.00 39.07 ? 85  ASP A OD2 1 
ATOM   671  N  N   . GLY A 1 86  ? -18.350 13.352  27.007  1.00 26.30 ? 86  GLY A N   1 
ATOM   672  C  CA  . GLY A 1 86  ? -18.429 13.869  25.659  1.00 24.06 ? 86  GLY A CA  1 
ATOM   673  C  C   . GLY A 1 86  ? -18.320 12.883  24.453  1.00 22.35 ? 86  GLY A C   1 
ATOM   674  O  O   . GLY A 1 86  ? -18.540 11.640  24.566  1.00 21.82 ? 86  GLY A O   1 
ATOM   675  N  N   . THR A 1 87  ? -17.963 13.469  23.305  1.00 17.50 ? 87  THR A N   1 
ATOM   676  C  CA  . THR A 1 87  ? -18.389 12.978  22.021  1.00 16.80 ? 87  THR A CA  1 
ATOM   677  C  C   . THR A 1 87  ? -17.209 12.661  21.162  1.00 14.48 ? 87  THR A C   1 
ATOM   678  O  O   . THR A 1 87  ? -16.295 13.493  21.049  1.00 13.38 ? 87  THR A O   1 
ATOM   679  C  CB  . THR A 1 87  ? -19.223 14.000  21.305  1.00 18.80 ? 87  THR A CB  1 
ATOM   680  O  OG1 . THR A 1 87  ? -20.373 14.251  22.160  1.00 22.68 ? 87  THR A OG1 1 
ATOM   681  C  CG2 . THR A 1 87  ? -19.635 13.473  19.834  1.00 20.83 ? 87  THR A CG2 1 
ATOM   682  N  N   . TYR A 1 88  ? -17.254 11.459  20.569  1.00 12.14 ? 88  TYR A N   1 
ATOM   683  C  CA  . TYR A 1 88  ? -16.130 11.042  19.764  1.00 11.76 ? 88  TYR A CA  1 
ATOM   684  C  C   . TYR A 1 88  ? -16.581 10.663  18.373  1.00 12.57 ? 88  TYR A C   1 
ATOM   685  O  O   . TYR A 1 88  ? -17.544 9.926   18.206  1.00 14.57 ? 88  TYR A O   1 
ATOM   686  C  CB  . TYR A 1 88  ? -15.542 9.783   20.346  1.00 11.18 ? 88  TYR A CB  1 
ATOM   687  C  CG  . TYR A 1 88  ? -14.786 9.934   21.671  1.00 8.70  ? 88  TYR A CG  1 
ATOM   688  C  CD1 . TYR A 1 88  ? -15.446 10.335  22.813  1.00 7.51  ? 88  TYR A CD1 1 
ATOM   689  C  CD2 . TYR A 1 88  ? -13.347 9.760   21.715  1.00 10.55 ? 88  TYR A CD2 1 
ATOM   690  C  CE1 . TYR A 1 88  ? -14.759 10.445  24.118  1.00 9.99  ? 88  TYR A CE1 1 
ATOM   691  C  CE2 . TYR A 1 88  ? -12.652 9.969   22.942  1.00 10.62 ? 88  TYR A CE2 1 
ATOM   692  C  CZ  . TYR A 1 88  ? -13.340 10.231  24.106  1.00 9.98  ? 88  TYR A CZ  1 
ATOM   693  O  OH  . TYR A 1 88  ? -12.763 10.382  25.317  1.00 10.41 ? 88  TYR A OH  1 
ATOM   694  N  N   . ARG A 1 89  ? -15.926 11.226  17.400  1.00 10.59 ? 89  ARG A N   1 
ATOM   695  C  CA  . ARG A 1 89  ? -16.308 11.064  15.968  1.00 12.64 ? 89  ARG A CA  1 
ATOM   696  C  C   . ARG A 1 89  ? -15.635 9.896   15.325  1.00 9.79  ? 89  ARG A C   1 
ATOM   697  O  O   . ARG A 1 89  ? -14.439 9.770   15.393  1.00 8.41  ? 89  ARG A O   1 
ATOM   698  C  CB  . ARG A 1 89  ? -15.987 12.260  15.090  1.00 13.85 ? 89  ARG A CB  1 
ATOM   699  C  CG  . ARG A 1 89  ? -16.920 13.375  15.352  1.00 19.73 ? 89  ARG A CG  1 
ATOM   700  C  CD  . ARG A 1 89  ? -16.689 14.447  14.322  1.00 19.22 ? 89  ARG A CD  1 
ATOM   701  N  NE  . ARG A 1 89  ? -17.381 15.656  14.681  1.00 23.20 ? 89  ARG A NE  1 
ATOM   702  C  CZ  . ARG A 1 89  ? -17.052 16.845  14.256  1.00 23.57 ? 89  ARG A CZ  1 
ATOM   703  N  NH1 . ARG A 1 89  ? -15.984 17.012  13.552  1.00 17.75 ? 89  ARG A NH1 1 
ATOM   704  N  NH2 . ARG A 1 89  ? -17.777 17.904  14.664  1.00 29.04 ? 89  ARG A NH2 1 
ATOM   705  N  N   . LEU A 1 90  ? -16.400 9.087   14.580  1.00 8.70  ? 90  LEU A N   1 
ATOM   706  C  CA  . LEU A 1 90  ? -15.791 7.984   13.839  1.00 8.95  ? 90  LEU A CA  1 
ATOM   707  C  C   . LEU A 1 90  ? -14.966 8.496   12.691  1.00 10.00 ? 90  LEU A C   1 
ATOM   708  O  O   . LEU A 1 90  ? -15.445 9.289   11.794  1.00 11.61 ? 90  LEU A O   1 
ATOM   709  C  CB  . LEU A 1 90  ? -16.940 7.113   13.226  1.00 9.09  ? 90  LEU A CB  1 
ATOM   710  C  CG  . LEU A 1 90  ? -16.453 5.921   12.392  1.00 8.89  ? 90  LEU A CG  1 
ATOM   711  C  CD1 . LEU A 1 90  ? -15.654 4.845   13.135  1.00 11.50 ? 90  LEU A CD1 1 
ATOM   712  C  CD2 . LEU A 1 90  ? -17.695 5.136   11.770  1.00 11.73 ? 90  LEU A CD2 1 
ATOM   713  N  N   . ILE A 1 91  ? -13.709 8.094   12.652  1.00 7.56  ? 91  ILE A N   1 
ATOM   714  C  CA  . ILE A 1 91  ? -12.815 8.480   11.523  1.00 8.78  ? 91  ILE A CA  1 
ATOM   715  C  C   . ILE A 1 91  ? -12.559 7.320   10.555  1.00 9.38  ? 91  ILE A C   1 
ATOM   716  O  O   . ILE A 1 91  ? -12.522 7.487   9.352   1.00 10.08 ? 91  ILE A O   1 
ATOM   717  C  CB  . ILE A 1 91  ? -11.483 9.172   11.991  1.00 7.84  ? 91  ILE A CB  1 
ATOM   718  C  CG1 . ILE A 1 91  ? -10.621 9.441   10.793  1.00 9.84  ? 91  ILE A CG1 1 
ATOM   719  C  CG2 . ILE A 1 91  ? -10.716 8.326   13.038  1.00 8.95  ? 91  ILE A CG2 1 
ATOM   720  C  CD1 . ILE A 1 91  ? -9.398  10.363  11.159  1.00 11.16 ? 91  ILE A CD1 1 
ATOM   721  N  N   . GLN A 1 92  ? -12.347 6.103   11.129  1.00 8.34  ? 92  GLN A N   1 
ATOM   722  C  CA  . GLN A 1 92  ? -12.117 4.958   10.235  1.00 7.91  ? 92  GLN A CA  1 
ATOM   723  C  C   . GLN A 1 92  ? -12.325 3.691   11.044  1.00 9.59  ? 92  GLN A C   1 
ATOM   724  O  O   . GLN A 1 92  ? -12.308 3.712   12.259  1.00 7.85  ? 92  GLN A O   1 
ATOM   725  C  CB  . GLN A 1 92  ? -10.743 4.909   9.572   1.00 10.48 ? 92  GLN A CB  1 
ATOM   726  C  CG  . GLN A 1 92  ? -9.550  5.093   10.604  1.00 10.07 ? 92  GLN A CG  1 
ATOM   727  C  CD  . GLN A 1 92  ? -8.875  3.830   11.131  1.00 13.44 ? 92  GLN A CD  1 
ATOM   728  O  OE1 . GLN A 1 92  ? -9.413  2.748   11.004  1.00 10.27 ? 92  GLN A OE1 1 
ATOM   729  N  NE2 . GLN A 1 92  ? -7.700  4.023   11.774  1.00 14.46 ? 92  GLN A NE2 1 
ATOM   730  N  N   . PHE A 1 93  ? -12.616 2.588   10.331  1.00 7.42  ? 93  PHE A N   1 
ATOM   731  C  CA  . PHE A 1 93  ? -12.422 1.291   10.932  1.00 6.88  ? 93  PHE A CA  1 
ATOM   732  C  C   . PHE A 1 93  ? -11.506 0.439   10.125  1.00 7.39  ? 93  PHE A C   1 
ATOM   733  O  O   . PHE A 1 93  ? -11.319 0.602   8.965   1.00 8.30  ? 93  PHE A O   1 
ATOM   734  C  CB  . PHE A 1 93  ? -13.757 0.594   11.202  1.00 6.30  ? 93  PHE A CB  1 
ATOM   735  C  CG  . PHE A 1 93  ? -14.522 0.131   9.961   1.00 9.87  ? 93  PHE A CG  1 
ATOM   736  C  CD1 . PHE A 1 93  ? -14.175 -1.036  9.311   1.00 9.39  ? 93  PHE A CD1 1 
ATOM   737  C  CD2 . PHE A 1 93  ? -15.648 0.904   9.538   1.00 9.03  ? 93  PHE A CD2 1 
ATOM   738  C  CE1 . PHE A 1 93  ? -14.867 -1.497  8.168   1.00 9.49  ? 93  PHE A CE1 1 
ATOM   739  C  CE2 . PHE A 1 93  ? -16.389 0.425   8.428   1.00 11.19 ? 93  PHE A CE2 1 
ATOM   740  C  CZ  . PHE A 1 93  ? -15.953 -0.736  7.736   1.00 12.90 ? 93  PHE A CZ  1 
ATOM   741  N  N   . HIS A 1 94  ? -10.979 -0.593  10.782  1.00 6.06  ? 94  HIS A N   1 
ATOM   742  C  CA  . HIS A 1 94  ? -10.123 -1.550  10.204  1.00 5.61  ? 94  HIS A CA  1 
ATOM   743  C  C   . HIS A 1 94  ? -10.201 -2.814  11.065  1.00 6.70  ? 94  HIS A C   1 
ATOM   744  O  O   . HIS A 1 94  ? -10.840 -2.824  12.114  1.00 7.07  ? 94  HIS A O   1 
ATOM   745  C  CB  . HIS A 1 94  ? -8.590  -1.079  10.111  1.00 8.49  ? 94  HIS A CB  1 
ATOM   746  C  CG  . HIS A 1 94  ? -8.043  -0.760  11.490  1.00 6.95  ? 94  HIS A CG  1 
ATOM   747  N  ND1 . HIS A 1 94  ? -8.244  0.477   12.125  1.00 8.09  ? 94  HIS A ND1 1 
ATOM   748  C  CD2 . HIS A 1 94  ? -7.433  -1.555  12.402  1.00 7.43  ? 94  HIS A CD2 1 
ATOM   749  C  CE1 . HIS A 1 94  ? -7.730  0.403   13.348  1.00 5.77  ? 94  HIS A CE1 1 
ATOM   750  N  NE2 . HIS A 1 94  ? -7.262  -0.832  13.546  1.00 6.08  ? 94  HIS A NE2 1 
ATOM   751  N  N   . PHE A 1 95  ? -9.457  -3.818  10.582  1.00 6.51  ? 95  PHE A N   1 
ATOM   752  C  CA  . PHE A 1 95  ? -9.421  -5.102  11.254  1.00 5.78  ? 95  PHE A CA  1 
ATOM   753  C  C   . PHE A 1 95  ? -7.988  -5.597  11.405  1.00 6.41  ? 95  PHE A C   1 
ATOM   754  O  O   . PHE A 1 95  ? -7.089  -5.098  10.723  1.00 8.60  ? 95  PHE A O   1 
ATOM   755  C  CB  . PHE A 1 95  ? -10.138 -6.221  10.398  1.00 8.13  ? 95  PHE A CB  1 
ATOM   756  C  CG  . PHE A 1 95  ? -11.578 -5.921  10.078  1.00 5.07  ? 95  PHE A CG  1 
ATOM   757  C  CD1 . PHE A 1 95  ? -11.899 -5.112  9.001   1.00 8.96  ? 95  PHE A CD1 1 
ATOM   758  C  CD2 . PHE A 1 95  ? -12.595 -6.613  10.754  1.00 7.23  ? 95  PHE A CD2 1 
ATOM   759  C  CE1 . PHE A 1 95  ? -13.223 -4.878  8.658   1.00 7.94  ? 95  PHE A CE1 1 
ATOM   760  C  CE2 . PHE A 1 95  ? -13.916 -6.337  10.494  1.00 7.22  ? 95  PHE A CE2 1 
ATOM   761  C  CZ  . PHE A 1 95  ? -14.266 -5.481  9.362   1.00 7.49  ? 95  PHE A CZ  1 
ATOM   762  N  N   . HIS A 1 96  ? -7.835  -6.516  12.341  1.00 6.25  ? 96  HIS A N   1 
ATOM   763  C  CA  . HIS A 1 96  ? -6.640  -7.325  12.507  1.00 6.82  ? 96  HIS A CA  1 
ATOM   764  C  C   . HIS A 1 96  ? -7.072  -8.761  12.378  1.00 7.73  ? 96  HIS A C   1 
ATOM   765  O  O   . HIS A 1 96  ? -8.109  -9.139  12.952  1.00 7.96  ? 96  HIS A O   1 
ATOM   766  C  CB  . HIS A 1 96  ? -5.969  -7.090  13.862  1.00 8.87  ? 96  HIS A CB  1 
ATOM   767  C  CG  . HIS A 1 96  ? -5.714  -5.645  14.166  1.00 7.29  ? 96  HIS A CG  1 
ATOM   768  N  ND1 . HIS A 1 96  ? -4.467  -5.078  13.925  1.00 7.25  ? 96  HIS A ND1 1 
ATOM   769  C  CD2 . HIS A 1 96  ? -6.526  -4.624  14.569  1.00 5.87  ? 96  HIS A CD2 1 
ATOM   770  C  CE1 . HIS A 1 96  ? -4.494  -3.805  14.346  1.00 9.85  ? 96  HIS A CE1 1 
ATOM   771  N  NE2 . HIS A 1 96  ? -5.733  -3.470  14.627  1.00 7.65  ? 96  HIS A NE2 1 
ATOM   772  N  N   . TRP A 1 97  ? -6.263  -9.563  11.681  1.00 6.76  ? 97  TRP A N   1 
ATOM   773  C  CA  . TRP A 1 97  ? -6.679  -11.000 11.527  1.00 7.44  ? 97  TRP A CA  1 
ATOM   774  C  C   . TRP A 1 97  ? -5.497  -11.920 11.410  1.00 8.38  ? 97  TRP A C   1 
ATOM   775  O  O   . TRP A 1 97  ? -4.337  -11.442 11.253  1.00 7.29  ? 97  TRP A O   1 
ATOM   776  C  CB  . TRP A 1 97  ? -7.575  -11.170 10.314  1.00 7.44  ? 97  TRP A CB  1 
ATOM   777  C  CG  . TRP A 1 97  ? -6.953  -10.752 9.000   1.00 8.62  ? 97  TRP A CG  1 
ATOM   778  C  CD1 . TRP A 1 97  ? -6.189  -11.569 8.149   1.00 8.69  ? 97  TRP A CD1 1 
ATOM   779  C  CD2 . TRP A 1 97  ? -6.854  -9.409  8.481   1.00 8.25  ? 97  TRP A CD2 1 
ATOM   780  N  NE1 . TRP A 1 97  ? -5.775  -10.805 7.042   1.00 10.71 ? 97  TRP A NE1 1 
ATOM   781  C  CE2 . TRP A 1 97  ? -6.154  -9.491  7.226   1.00 9.74  ? 97  TRP A CE2 1 
ATOM   782  C  CE3 . TRP A 1 97  ? -7.396  -8.168  8.884   1.00 9.22  ? 97  TRP A CE3 1 
ATOM   783  C  CZ2 . TRP A 1 97  ? -5.950  -8.370  6.412   1.00 9.33  ? 97  TRP A CZ2 1 
ATOM   784  C  CZ3 . TRP A 1 97  ? -7.121  -6.986  8.070   1.00 9.39  ? 97  TRP A CZ3 1 
ATOM   785  C  CH2 . TRP A 1 97  ? -6.426  -7.121  6.888   1.00 8.88  ? 97  TRP A CH2 1 
ATOM   786  N  N   . GLY A 1 98  ? -5.808  -13.206 11.408  1.00 8.25  ? 98  GLY A N   1 
ATOM   787  C  CA  . GLY A 1 98  ? -4.771  -14.241 11.445  1.00 8.42  ? 98  GLY A CA  1 
ATOM   788  C  C   . GLY A 1 98  ? -4.498  -14.929 10.088  1.00 9.09  ? 98  GLY A C   1 
ATOM   789  O  O   . GLY A 1 98  ? -5.216  -14.728 9.132   1.00 9.24  ? 98  GLY A O   1 
ATOM   790  N  N   . SER A 1 99  ? -3.487  -15.781 10.081  1.00 9.08  ? 99  SER A N   1 
ATOM   791  C  CA  . SER A 1 99  ? -3.215  -16.681 8.960   1.00 11.38 ? 99  SER A CA  1 
ATOM   792  C  C   . SER A 1 99  ? -4.091  -17.919 9.055   1.00 11.59 ? 99  SER A C   1 
ATOM   793  O  O   . SER A 1 99  ? -4.147  -18.696 8.105   1.00 13.42 ? 99  SER A O   1 
ATOM   794  C  CB  . SER A 1 99  ? -1.754  -17.030 8.988   1.00 10.98 ? 99  SER A CB  1 
ATOM   795  O  OG  . SER A 1 99  ? -1.379  -17.581 10.178  1.00 12.90 ? 99  SER A OG  1 
ATOM   796  N  N   . LEU A 1 100 ? -4.725  -18.105 10.204  1.00 11.22 ? 100 LEU A N   1 
ATOM   797  C  CA  . LEU A 1 100 ? -5.481  -19.264 10.594  1.00 11.24 ? 100 LEU A CA  1 
ATOM   798  C  C   . LEU A 1 100 ? -6.678  -18.805 11.401  1.00 11.29 ? 100 LEU A C   1 
ATOM   799  O  O   . LEU A 1 100 ? -6.578  -17.798 12.145  1.00 11.29 ? 100 LEU A O   1 
ATOM   800  C  CB  . LEU A 1 100 ? -4.621  -20.117 11.594  1.00 14.41 ? 100 LEU A CB  1 
ATOM   801  C  CG  . LEU A 1 100 ? -3.314  -20.667 11.025  1.00 19.55 ? 100 LEU A CG  1 
ATOM   802  C  CD1 . LEU A 1 100 ? -2.392  -20.997 12.160  1.00 24.81 ? 100 LEU A CD1 1 
ATOM   803  C  CD2 . LEU A 1 100 ? -3.628  -21.964 10.193  1.00 25.28 ? 100 LEU A CD2 1 
ATOM   804  N  N   . ASP A 1 101 ? -7.794  -19.525 11.331  1.00 9.65  ? 101 ASP A N   1 
ATOM   805  C  CA  . ASP A 1 101 ? -8.926  -19.086 12.219  1.00 11.31 ? 101 ASP A CA  1 
ATOM   806  C  C   . ASP A 1 101 ? -8.667  -19.059 13.755  1.00 10.88 ? 101 ASP A C   1 
ATOM   807  O  O   . ASP A 1 101 ? -9.371  -18.344 14.450  1.00 14.32 ? 101 ASP A O   1 
ATOM   808  C  CB  . ASP A 1 101 ? -10.153 -19.965 11.940  1.00 10.26 ? 101 ASP A CB  1 
ATOM   809  C  CG  . ASP A 1 101 ? -10.599 -19.927 10.491  1.00 17.18 ? 101 ASP A CG  1 
ATOM   810  O  OD1 . ASP A 1 101 ? -10.140 -19.052 9.728   1.00 14.89 ? 101 ASP A OD1 1 
ATOM   811  O  OD2 . ASP A 1 101 ? -11.428 -20.786 10.123  1.00 20.64 ? 101 ASP A OD2 1 
ATOM   812  N  N   . GLY A 1 102 ? -7.642  -19.836 14.251  1.00 12.01 ? 102 GLY A N   1 
ATOM   813  C  CA  . GLY A 1 102 ? -7.278  -19.848 15.669  1.00 11.69 ? 102 GLY A CA  1 
ATOM   814  C  C   . GLY A 1 102 ? -6.547  -18.646 16.217  1.00 9.09  ? 102 GLY A C   1 
ATOM   815  O  O   . GLY A 1 102 ? -6.246  -18.607 17.406  1.00 11.27 ? 102 GLY A O   1 
ATOM   816  N  N   . GLN A 1 103 ? -6.321  -17.648 15.379  1.00 8.53  ? 103 GLN A N   1 
ATOM   817  C  CA  . GLN A 1 103 ? -5.600  -16.442 15.869  1.00 7.91  ? 103 GLN A CA  1 
ATOM   818  C  C   . GLN A 1 103 ? -5.961  -15.258 14.993  1.00 7.56  ? 103 GLN A C   1 
ATOM   819  O  O   . GLN A 1 103 ? -6.518  -15.438 13.910  1.00 8.76  ? 103 GLN A O   1 
ATOM   820  C  CB  . GLN A 1 103 ? -4.088  -16.723 15.908  1.00 9.86  ? 103 GLN A CB  1 
ATOM   821  C  CG  . GLN A 1 103 ? -3.498  -16.798 14.473  1.00 9.94  ? 103 GLN A CG  1 
ATOM   822  C  CD  . GLN A 1 103 ? -2.062  -17.364 14.541  1.00 13.83 ? 103 GLN A CD  1 
ATOM   823  O  OE1 . GLN A 1 103 ? -1.782  -18.224 15.408  1.00 21.57 ? 103 GLN A OE1 1 
ATOM   824  N  NE2 . GLN A 1 103 ? -1.175  -16.936 13.669  1.00 14.67 ? 103 GLN A NE2 1 
ATOM   825  N  N   . GLY A 1 104 ? -5.617  -14.060 15.491  1.00 7.19  ? 104 GLY A N   1 
ATOM   826  C  CA  . GLY A 1 104 ? -5.948  -12.896 14.685  1.00 5.58  ? 104 GLY A CA  1 
ATOM   827  C  C   . GLY A 1 104 ? -6.383  -11.680 15.540  1.00 6.51  ? 104 GLY A C   1 
ATOM   828  O  O   . GLY A 1 104 ? -6.079  -10.524 15.211  1.00 8.40  ? 104 GLY A O   1 
ATOM   829  N  N   . SER A 1 105 ? -7.047  -11.979 16.675  1.00 4.54  ? 105 SER A N   1 
ATOM   830  C  CA  . SER A 1 105 ? -7.502  -10.834 17.515  1.00 6.12  ? 105 SER A CA  1 
ATOM   831  C  C   . SER A 1 105 ? -6.277  -10.343 18.290  1.00 6.81  ? 105 SER A C   1 
ATOM   832  O  O   . SER A 1 105 ? -5.231  -11.021 18.458  1.00 7.98  ? 105 SER A O   1 
ATOM   833  C  CB  . SER A 1 105 ? -8.594  -11.222 18.493  1.00 6.52  ? 105 SER A CB  1 
ATOM   834  O  OG  . SER A 1 105 ? -8.192  -12.176 19.408  1.00 7.75  ? 105 SER A OG  1 
ATOM   835  N  N   . GLU A 1 106 ? -6.379  -9.102  18.607  1.00 6.19  ? 106 GLU A N   1 
ATOM   836  C  CA  . GLU A 1 106 ? -5.367  -8.394  19.481  1.00 5.87  ? 106 GLU A CA  1 
ATOM   837  C  C   . GLU A 1 106 ? -5.732  -8.567  20.978  1.00 7.11  ? 106 GLU A C   1 
ATOM   838  O  O   . GLU A 1 106 ? -4.975  -9.150  21.734  1.00 6.70  ? 106 GLU A O   1 
ATOM   839  C  CB  . GLU A 1 106 ? -5.352  -6.887  19.095  1.00 5.38  ? 106 GLU A CB  1 
ATOM   840  C  CG  . GLU A 1 106 ? -4.851  -6.790  17.656  1.00 6.20  ? 106 GLU A CG  1 
ATOM   841  C  CD  . GLU A 1 106 ? -4.249  -5.462  17.292  1.00 9.24  ? 106 GLU A CD  1 
ATOM   842  O  OE1 . GLU A 1 106 ? -4.834  -4.412  17.530  1.00 8.10  ? 106 GLU A OE1 1 
ATOM   843  O  OE2 . GLU A 1 106 ? -3.049  -5.550  16.853  1.00 8.84  ? 106 GLU A OE2 1 
ATOM   844  N  N   . HIS A 1 107 ? -6.946  -8.113  21.421  1.00 5.94  ? 107 HIS A N   1 
ATOM   845  C  CA  . HIS A 1 107 ? -7.371  -8.489  22.724  1.00 4.38  ? 107 HIS A CA  1 
ATOM   846  C  C   . HIS A 1 107 ? -7.691  -9.963  22.702  1.00 5.36  ? 107 HIS A C   1 
ATOM   847  O  O   . HIS A 1 107 ? -8.034  -10.559 21.630  1.00 6.70  ? 107 HIS A O   1 
ATOM   848  C  CB  . HIS A 1 107 ? -8.658  -7.679  23.077  1.00 4.88  ? 107 HIS A CB  1 
ATOM   849  C  CG  . HIS A 1 107 ? -8.341  -6.232  23.258  1.00 4.43  ? 107 HIS A CG  1 
ATOM   850  N  ND1 . HIS A 1 107 ? -8.395  -5.337  22.204  1.00 7.00  ? 107 HIS A ND1 1 
ATOM   851  C  CD2 . HIS A 1 107 ? -7.889  -5.536  24.347  1.00 5.76  ? 107 HIS A CD2 1 
ATOM   852  C  CE1 . HIS A 1 107 ? -7.920  -4.162  22.625  1.00 7.69  ? 107 HIS A CE1 1 
ATOM   853  N  NE2 . HIS A 1 107 ? -7.631  -4.241  23.944  1.00 4.37  ? 107 HIS A NE2 1 
ATOM   854  N  N   . THR A 1 108 ? -7.529  -10.542 23.879  1.00 5.93  ? 108 THR A N   1 
ATOM   855  C  CA  . THR A 1 108 ? -7.920  -11.919 24.061  1.00 5.79  ? 108 THR A CA  1 
ATOM   856  C  C   . THR A 1 108 ? -8.890  -11.924 25.259  1.00 7.02  ? 108 THR A C   1 
ATOM   857  O  O   . THR A 1 108 ? -8.900  -11.002 26.095  1.00 8.95  ? 108 THR A O   1 
ATOM   858  C  CB  . THR A 1 108 ? -6.712  -12.832 24.270  1.00 6.61  ? 108 THR A CB  1 
ATOM   859  O  OG1 . THR A 1 108 ? -5.946  -12.315 25.389  1.00 8.46  ? 108 THR A OG1 1 
ATOM   860  C  CG2 . THR A 1 108 ? -5.846  -12.914 23.033  1.00 6.56  ? 108 THR A CG2 1 
ATOM   861  N  N   . VAL A 1 109 ? -9.661  -13.040 25.390  1.00 7.22  ? 109 VAL A N   1 
ATOM   862  C  CA  . VAL A 1 109 ? -10.692 -13.098 26.529  1.00 7.43  ? 109 VAL A CA  1 
ATOM   863  C  C   . VAL A 1 109 ? -10.346 -14.424 27.229  1.00 9.90  ? 109 VAL A C   1 
ATOM   864  O  O   . VAL A 1 109 ? -10.476 -15.488 26.655  1.00 10.47 ? 109 VAL A O   1 
ATOM   865  C  CB  . VAL A 1 109 ? -12.145 -13.145 25.946  1.00 11.69 ? 109 VAL A CB  1 
ATOM   866  C  CG1 . VAL A 1 109 ? -13.151 -13.265 27.047  1.00 9.44  ? 109 VAL A CG1 1 
ATOM   867  C  CG2 . VAL A 1 109 ? -12.384 -11.841 25.086  1.00 11.57 ? 109 VAL A CG2 1 
ATOM   868  N  N   . ASP A 1 110 ? -9.884  -14.298 28.434  1.00 8.78  ? 110 ASP A N   1 
ATOM   869  C  CA  . ASP A 1 110 ? -9.373  -15.504 29.224  1.00 9.15  ? 110 ASP A CA  1 
ATOM   870  C  C   . ASP A 1 110 ? -8.433  -16.334 28.304  1.00 9.14  ? 110 ASP A C   1 
ATOM   871  O  O   . ASP A 1 110 ? -8.486  -17.611 28.175  1.00 10.75 ? 110 ASP A O   1 
ATOM   872  C  CB  . ASP A 1 110 ? -10.585 -16.364 29.661  1.00 10.23 ? 110 ASP A CB  1 
ATOM   873  C  CG  . ASP A 1 110 ? -11.475 -15.593 30.656  1.00 8.78  ? 110 ASP A CG  1 
ATOM   874  O  OD1 . ASP A 1 110 ? -10.946 -14.789 31.349  1.00 13.63 ? 110 ASP A OD1 1 
ATOM   875  O  OD2 . ASP A 1 110 ? -12.685 -15.921 30.719  1.00 16.79 ? 110 ASP A OD2 1 
ATOM   876  N  N   . LYS A 1 111 ? -7.554  -15.578 27.644  1.00 8.60  ? 111 LYS A N   1 
ATOM   877  C  CA  . LYS A 1 111 ? -6.469  -16.065 26.756  1.00 10.35 ? 111 LYS A CA  1 
ATOM   878  C  C   . LYS A 1 111 ? -6.954  -16.628 25.397  1.00 8.37  ? 111 LYS A C   1 
ATOM   879  O  O   . LYS A 1 111 ? -6.133  -17.046 24.570  1.00 10.15 ? 111 LYS A O   1 
ATOM   880  C  CB  . LYS A 1 111 ? -5.579  -17.130 27.464  1.00 13.00 ? 111 LYS A CB  1 
ATOM   881  C  CG  . LYS A 1 111 ? -4.992  -16.686 28.748  1.00 15.63 ? 111 LYS A CG  1 
ATOM   882  C  CD  . LYS A 1 111 ? -4.079  -15.599 28.478  1.00 21.20 ? 111 LYS A CD  1 
ATOM   883  C  CE  . LYS A 1 111 ? -3.437  -15.083 29.789  1.00 27.30 ? 111 LYS A CE  1 
ATOM   884  N  NZ  . LYS A 1 111 ? -2.037  -15.530 29.704  1.00 25.92 ? 111 LYS A NZ  1 
ATOM   885  N  N   . LYS A 1 112 ? -8.281  -16.579 25.176  1.00 8.02  ? 112 LYS A N   1 
ATOM   886  C  CA  . LYS A 1 112 ? -8.835  -16.996 23.943  1.00 10.34 ? 112 LYS A CA  1 
ATOM   887  C  C   . LYS A 1 112 ? -8.553  -15.927 22.874  1.00 9.58  ? 112 LYS A C   1 
ATOM   888  O  O   . LYS A 1 112 ? -8.853  -14.716 23.045  1.00 9.65  ? 112 LYS A O   1 
ATOM   889  C  CB  . LYS A 1 112 ? -10.362 -17.179 24.094  1.00 12.36 ? 112 LYS A CB  1 
ATOM   890  C  CG  . LYS A 1 112 ? -11.126 -17.423 22.728  1.00 15.77 ? 112 LYS A CG  1 
ATOM   891  C  CD  . LYS A 1 112 ? -12.696 -17.414 23.021  1.00 15.64 ? 112 LYS A CD  1 
ATOM   892  C  CE  . LYS A 1 112 ? -13.435 -17.466 21.650  1.00 20.71 ? 112 LYS A CE  1 
ATOM   893  N  NZ  . LYS A 1 112 ? -13.090 -18.756 21.006  1.00 19.42 ? 112 LYS A NZ  1 
ATOM   894  N  N   A LYS A 1 113 ? -8.041  -16.424 21.763  0.50 8.95  ? 113 LYS A N   1 
ATOM   895  N  N   B LYS A 1 113 ? -8.045  -16.426 21.754  0.50 8.80  ? 113 LYS A N   1 
ATOM   896  C  CA  A LYS A 1 113 ? -7.876  -15.608 20.535  0.50 8.66  ? 113 LYS A CA  1 
ATOM   897  C  CA  B LYS A 1 113 ? -7.848  -15.615 20.513  0.50 8.24  ? 113 LYS A CA  1 
ATOM   898  C  C   A LYS A 1 113 ? -9.055  -15.840 19.610  0.50 8.90  ? 113 LYS A C   1 
ATOM   899  C  C   B LYS A 1 113 ? -8.968  -15.845 19.508  0.50 8.59  ? 113 LYS A C   1 
ATOM   900  O  O   A LYS A 1 113 ? -9.531  -16.984 19.446  0.50 8.76  ? 113 LYS A O   1 
ATOM   901  O  O   B LYS A 1 113 ? -9.309  -16.997 19.174  0.50 8.79  ? 113 LYS A O   1 
ATOM   902  C  CB  A LYS A 1 113 ? -6.586  -15.967 19.812  0.50 8.89  ? 113 LYS A CB  1 
ATOM   903  C  CB  B LYS A 1 113 ? -6.502  -15.922 19.855  0.50 8.65  ? 113 LYS A CB  1 
ATOM   904  C  CG  A LYS A 1 113 ? -5.334  -15.799 20.652  0.50 8.02  ? 113 LYS A CG  1 
ATOM   905  C  CG  B LYS A 1 113 ? -5.304  -15.338 20.605  0.50 6.25  ? 113 LYS A CG  1 
ATOM   906  C  CD  A LYS A 1 113 ? -4.186  -16.315 19.793  0.50 8.79  ? 113 LYS A CD  1 
ATOM   907  C  CD  B LYS A 1 113 ? -4.019  -16.050 20.159  0.50 10.47 ? 113 LYS A CD  1 
ATOM   908  C  CE  A LYS A 1 113 ? -2.829  -15.799 20.296  0.50 9.67  ? 113 LYS A CE  1 
ATOM   909  C  CE  B LYS A 1 113 ? -2.763  -15.562 20.900  0.50 10.58 ? 113 LYS A CE  1 
ATOM   910  N  NZ  A LYS A 1 113 ? -2.494  -16.402 21.652  0.50 13.35 ? 113 LYS A NZ  1 
ATOM   911  N  NZ  B LYS A 1 113 ? -1.578  -16.380 20.416  0.50 14.41 ? 113 LYS A NZ  1 
ATOM   912  N  N   . TYR A 1 114 ? -9.532  -14.730 19.046  1.00 8.80  ? 114 TYR A N   1 
ATOM   913  C  CA  . TYR A 1 114 ? -10.540 -14.798 18.018  1.00 8.26  ? 114 TYR A CA  1 
ATOM   914  C  C   . TYR A 1 114 ? -9.938  -14.717 16.638  1.00 7.97  ? 114 TYR A C   1 
ATOM   915  O  O   . TYR A 1 114 ? -8.749  -14.350 16.479  1.00 8.82  ? 114 TYR A O   1 
ATOM   916  C  CB  . TYR A 1 114 ? -11.632 -13.701 18.157  1.00 8.60  ? 114 TYR A CB  1 
ATOM   917  C  CG  . TYR A 1 114 ? -12.592 -13.926 19.304  1.00 6.21  ? 114 TYR A CG  1 
ATOM   918  C  CD1 . TYR A 1 114 ? -12.277 -13.508 20.590  1.00 10.66 ? 114 TYR A CD1 1 
ATOM   919  C  CD2 . TYR A 1 114 ? -13.813 -14.554 19.100  1.00 9.01  ? 114 TYR A CD2 1 
ATOM   920  C  CE1 . TYR A 1 114 ? -13.151 -13.712 21.642  1.00 10.73 ? 114 TYR A CE1 1 
ATOM   921  C  CE2 . TYR A 1 114 ? -14.694 -14.761 20.145  1.00 12.66 ? 114 TYR A CE2 1 
ATOM   922  C  CZ  . TYR A 1 114 ? -14.358 -14.338 21.414  1.00 12.94 ? 114 TYR A CZ  1 
ATOM   923  O  OH  . TYR A 1 114 ? -15.231 -14.542 22.457  1.00 16.78 ? 114 TYR A OH  1 
ATOM   924  N  N   . ALA A 1 115 ? -10.683 -15.050 15.578  1.00 7.24  ? 115 ALA A N   1 
ATOM   925  C  CA  . ALA A 1 115 ? -10.097 -15.054 14.245  1.00 6.80  ? 115 ALA A CA  1 
ATOM   926  C  C   . ALA A 1 115 ? -9.675  -13.655 13.707  1.00 7.49  ? 115 ALA A C   1 
ATOM   927  O  O   . ALA A 1 115 ? -8.833  -13.490 12.788  1.00 8.37  ? 115 ALA A O   1 
ATOM   928  C  CB  . ALA A 1 115 ? -11.168 -15.672 13.248  1.00 8.62  ? 115 ALA A CB  1 
ATOM   929  N  N   . ALA A 1 116 ? -10.415 -12.672 14.256  1.00 8.01  ? 116 ALA A N   1 
ATOM   930  C  CA  . ALA A 1 116 ? -10.071 -11.300 13.849  1.00 6.90  ? 116 ALA A CA  1 
ATOM   931  C  C   . ALA A 1 116 ? -10.691 -10.313 14.888  1.00 6.60  ? 116 ALA A C   1 
ATOM   932  O  O   . ALA A 1 116 ? -11.427 -10.704 15.779  1.00 6.52  ? 116 ALA A O   1 
ATOM   933  C  CB  . ALA A 1 116 ? -10.613 -10.986 12.443  1.00 6.93  ? 116 ALA A CB  1 
ATOM   934  N  N   . GLU A 1 117 ? -10.318 -9.040  14.749  1.00 7.38  ? 117 GLU A N   1 
ATOM   935  C  CA  . GLU A 1 117 ? -10.867 -8.026  15.630  1.00 6.00  ? 117 GLU A CA  1 
ATOM   936  C  C   . GLU A 1 117 ? -11.003 -6.754  14.820  1.00 8.20  ? 117 GLU A C   1 
ATOM   937  O  O   . GLU A 1 117 ? -10.113 -6.336  14.120  1.00 7.33  ? 117 GLU A O   1 
ATOM   938  C  CB  . GLU A 1 117 ? -9.900  -7.815  16.805  1.00 6.09  ? 117 GLU A CB  1 
ATOM   939  C  CG  . GLU A 1 117 ? -10.370 -6.749  17.809  1.00 5.58  ? 117 GLU A CG  1 
ATOM   940  C  CD  . GLU A 1 117 ? -9.493  -6.734  19.054  1.00 7.41  ? 117 GLU A CD  1 
ATOM   941  O  OE1 . GLU A 1 117 ? -8.846  -7.798  19.346  1.00 7.69  ? 117 GLU A OE1 1 
ATOM   942  O  OE2 . GLU A 1 117 ? -9.400  -5.652  19.696  1.00 8.48  ? 117 GLU A OE2 1 
ATOM   943  N  N   . LEU A 1 118 ? -12.207 -6.214  14.904  1.00 6.57  ? 118 LEU A N   1 
ATOM   944  C  CA  . LEU A 1 118 ? -12.568 -4.960  14.272  1.00 5.75  ? 118 LEU A CA  1 
ATOM   945  C  C   . LEU A 1 118 ? -12.364 -3.780  15.252  1.00 6.85  ? 118 LEU A C   1 
ATOM   946  O  O   . LEU A 1 118 ? -12.756 -3.849  16.396  1.00 6.59  ? 118 LEU A O   1 
ATOM   947  C  CB  . LEU A 1 118 ? -14.059 -5.053  13.887  1.00 6.42  ? 118 LEU A CB  1 
ATOM   948  C  CG  . LEU A 1 118 ? -14.883 -3.729  13.600  1.00 6.24  ? 118 LEU A CG  1 
ATOM   949  C  CD1 . LEU A 1 118 ? -14.315 -3.160  12.349  1.00 8.25  ? 118 LEU A CD1 1 
ATOM   950  C  CD2 . LEU A 1 118 ? -16.368 -4.127  13.294  1.00 8.08  ? 118 LEU A CD2 1 
ATOM   951  N  N   . HIS A 1 119 ? -11.738 -2.719  14.746  1.00 5.53  ? 119 HIS A N   1 
ATOM   952  C  CA  . HIS A 1 119 ? -11.529 -1.516  15.541  1.00 5.99  ? 119 HIS A CA  1 
ATOM   953  C  C   . HIS A 1 119 ? -12.232 -0.371  14.826  1.00 5.84  ? 119 HIS A C   1 
ATOM   954  O  O   . HIS A 1 119 ? -11.807 0.000   13.709  1.00 6.84  ? 119 HIS A O   1 
ATOM   955  C  CB  . HIS A 1 119 ? -10.044 -1.236  15.603  1.00 4.66  ? 119 HIS A CB  1 
ATOM   956  C  CG  . HIS A 1 119 ? -9.356  -2.179  16.521  1.00 5.37  ? 119 HIS A CG  1 
ATOM   957  N  ND1 . HIS A 1 119 ? -7.999  -2.405  16.425  1.00 6.32  ? 119 HIS A ND1 1 
ATOM   958  C  CD2 . HIS A 1 119 ? -9.853  -3.004  17.459  1.00 5.81  ? 119 HIS A CD2 1 
ATOM   959  C  CE1 . HIS A 1 119 ? -7.657  -3.301  17.324  1.00 4.03  ? 119 HIS A CE1 1 
ATOM   960  N  NE2 . HIS A 1 119 ? -8.772  -3.679  17.995  1.00 5.67  ? 119 HIS A NE2 1 
ATOM   961  N  N   . LEU A 1 120 ? -13.230 0.226   15.503  1.00 5.45  ? 120 LEU A N   1 
ATOM   962  C  CA  . LEU A 1 120 ? -13.894 1.470   15.046  1.00 6.93  ? 120 LEU A CA  1 
ATOM   963  C  C   . LEU A 1 120 ? -13.280 2.591   15.829  1.00 6.05  ? 120 LEU A C   1 
ATOM   964  O  O   . LEU A 1 120 ? -13.410 2.641   17.060  1.00 6.55  ? 120 LEU A O   1 
ATOM   965  C  CB  . LEU A 1 120 ? -15.369 1.398   15.290  1.00 6.99  ? 120 LEU A CB  1 
ATOM   966  C  CG  . LEU A 1 120 ? -16.029 0.276   14.442  1.00 8.19  ? 120 LEU A CG  1 
ATOM   967  C  CD1 . LEU A 1 120 ? -16.885 -0.658  15.224  1.00 10.86 ? 120 LEU A CD1 1 
ATOM   968  C  CD2 . LEU A 1 120 ? -16.866 0.968   13.302  1.00 9.68  ? 120 LEU A CD2 1 
ATOM   969  N  N   . VAL A 1 121 ? -12.534 3.406   15.066  1.00 5.76  ? 121 VAL A N   1 
ATOM   970  C  CA  . VAL A 1 121 ? -11.674 4.422   15.746  1.00 6.93  ? 121 VAL A CA  1 
ATOM   971  C  C   . VAL A 1 121 ? -12.342 5.739   15.785  1.00 7.99  ? 121 VAL A C   1 
ATOM   972  O  O   . VAL A 1 121 ? -12.750 6.244   14.702  1.00 7.02  ? 121 VAL A O   1 
ATOM   973  C  CB  . VAL A 1 121 ? -10.366 4.517   15.002  1.00 6.67  ? 121 VAL A CB  1 
ATOM   974  C  CG1 . VAL A 1 121 ? -9.474  5.639   15.566  1.00 6.27  ? 121 VAL A CG1 1 
ATOM   975  C  CG2 . VAL A 1 121 ? -9.679  3.125   14.857  1.00 8.91  ? 121 VAL A CG2 1 
ATOM   976  N  N   . HIS A 1 122 ? -12.448 6.340   16.991  1.00 6.95  ? 122 HIS A N   1 
ATOM   977  C  CA  . HIS A 1 122 ? -13.127 7.609   17.109  1.00 7.24  ? 122 HIS A CA  1 
ATOM   978  C  C   . HIS A 1 122 ? -12.306 8.619   17.895  1.00 7.95  ? 122 HIS A C   1 
ATOM   979  O  O   . HIS A 1 122 ? -11.544 8.238   18.763  1.00 7.45  ? 122 HIS A O   1 
ATOM   980  C  CB  . HIS A 1 122 ? -14.434 7.471   17.927  1.00 8.12  ? 122 HIS A CB  1 
ATOM   981  C  CG  . HIS A 1 122 ? -15.338 6.346   17.518  1.00 9.28  ? 122 HIS A CG  1 
ATOM   982  N  ND1 . HIS A 1 122 ? -15.030 5.023   17.815  1.00 7.37  ? 122 HIS A ND1 1 
ATOM   983  C  CD2 . HIS A 1 122 ? -16.535 6.320   16.860  1.00 11.38 ? 122 HIS A CD2 1 
ATOM   984  C  CE1 . HIS A 1 122 ? -16.028 4.235   17.358  1.00 9.16  ? 122 HIS A CE1 1 
ATOM   985  N  NE2 . HIS A 1 122 ? -16.934 4.998   16.758  1.00 10.66 ? 122 HIS A NE2 1 
ATOM   986  N  N   . TRP A 1 123 ? -12.401 9.898   17.522  1.00 7.27  ? 123 TRP A N   1 
ATOM   987  C  CA  . TRP A 1 123 ? -11.564 10.907  18.282  1.00 5.92  ? 123 TRP A CA  1 
ATOM   988  C  C   . TRP A 1 123 ? -12.432 11.948  18.944  1.00 8.29  ? 123 TRP A C   1 
ATOM   989  O  O   . TRP A 1 123 ? -13.549 12.301  18.497  1.00 9.63  ? 123 TRP A O   1 
ATOM   990  C  CB  . TRP A 1 123 ? -10.570 11.604  17.312  1.00 8.37  ? 123 TRP A CB  1 
ATOM   991  C  CG  . TRP A 1 123 ? -11.202 12.214  16.110  1.00 8.01  ? 123 TRP A CG  1 
ATOM   992  C  CD1 . TRP A 1 123 ? -11.410 11.593  14.869  1.00 10.80 ? 123 TRP A CD1 1 
ATOM   993  C  CD2 . TRP A 1 123 ? -11.686 13.572  15.996  1.00 9.54  ? 123 TRP A CD2 1 
ATOM   994  N  NE1 . TRP A 1 123 ? -12.056 12.512  13.997  1.00 10.05 ? 123 TRP A NE1 1 
ATOM   995  C  CE2 . TRP A 1 123 ? -12.177 13.738  14.640  1.00 11.82 ? 123 TRP A CE2 1 
ATOM   996  C  CE3 . TRP A 1 123 ? -11.712 14.686  16.866  1.00 11.82 ? 123 TRP A CE3 1 
ATOM   997  C  CZ2 . TRP A 1 123 ? -12.698 14.958  14.178  1.00 14.17 ? 123 TRP A CZ2 1 
ATOM   998  C  CZ3 . TRP A 1 123 ? -12.254 15.879  16.377  1.00 12.64 ? 123 TRP A CZ3 1 
ATOM   999  C  CH2 . TRP A 1 123 ? -12.769 16.008  15.080  1.00 11.26 ? 123 TRP A CH2 1 
ATOM   1000 N  N   . ASN A 1 124 ? -11.949 12.419  20.078  1.00 8.14  ? 124 ASN A N   1 
ATOM   1001 C  CA  . ASN A 1 124 ? -12.720 13.314  20.924  1.00 7.74  ? 124 ASN A CA  1 
ATOM   1002 C  C   . ASN A 1 124 ? -12.868 14.693  20.308  1.00 8.10  ? 124 ASN A C   1 
ATOM   1003 O  O   . ASN A 1 124 ? -11.896 15.340  20.035  1.00 8.74  ? 124 ASN A O   1 
ATOM   1004 C  CB  . ASN A 1 124 ? -11.875 13.438  22.189  1.00 8.59  ? 124 ASN A CB  1 
ATOM   1005 C  CG  . ASN A 1 124 ? -12.693 14.003  23.364  1.00 11.09 ? 124 ASN A CG  1 
ATOM   1006 O  OD1 . ASN A 1 124 ? -13.559 14.828  23.143  1.00 10.73 ? 124 ASN A OD1 1 
ATOM   1007 N  ND2 . ASN A 1 124 ? -12.467 13.495  24.571  1.00 11.51 ? 124 ASN A ND2 1 
ATOM   1008 N  N   . THR A 1 125 ? -14.108 15.133  20.147  1.00 11.49 ? 125 THR A N   1 
ATOM   1009 C  CA  . THR A 1 125 ? -14.318 16.389  19.435  1.00 13.07 ? 125 THR A CA  1 
ATOM   1010 C  C   . THR A 1 125 ? -13.760 17.627  20.114  1.00 12.93 ? 125 THR A C   1 
ATOM   1011 O  O   . THR A 1 125 ? -13.518 18.636  19.454  1.00 14.23 ? 125 THR A O   1 
ATOM   1012 C  CB  . THR A 1 125 ? -15.844 16.571  19.123  1.00 15.22 ? 125 THR A CB  1 
ATOM   1013 O  OG1 . THR A 1 125 ? -16.551 16.609  20.341  1.00 16.33 ? 125 THR A OG1 1 
ATOM   1014 C  CG2 . THR A 1 125 ? -16.337 15.401  18.288  1.00 17.17 ? 125 THR A CG2 1 
ATOM   1015 N  N   . LYS A 1 126 ? -13.370 17.257  21.644  1.00 10.81 ? 127 LYS A N   1 
ATOM   1016 C  CA  . LYS A 1 126 ? -12.949 18.540  22.194  1.00 12.05 ? 127 LYS A CA  1 
ATOM   1017 C  C   . LYS A 1 126 ? -11.563 18.928  21.691  1.00 13.97 ? 127 LYS A C   1 
ATOM   1018 O  O   . LYS A 1 126 ? -11.077 20.025  21.965  1.00 16.65 ? 127 LYS A O   1 
ATOM   1019 C  CB  . LYS A 1 126 ? -12.960 18.496  23.724  1.00 15.28 ? 127 LYS A CB  1 
ATOM   1020 C  CG  . LYS A 1 126 ? -12.083 17.407  24.320  1.00 15.26 ? 127 LYS A CG  1 
ATOM   1021 C  CD  . LYS A 1 126 ? -12.332 17.253  25.811  1.00 23.00 ? 127 LYS A CD  1 
ATOM   1022 C  CE  . LYS A 1 126 ? -11.398 16.222  26.423  1.00 25.45 ? 127 LYS A CE  1 
ATOM   1023 N  NZ  . LYS A 1 126 ? -10.776 16.714  27.683  1.00 29.51 ? 127 LYS A NZ  1 
ATOM   1024 N  N   . TYR A 1 127 ? -10.931 18.020  20.954  1.00 9.58  ? 128 TYR A N   1 
ATOM   1025 C  CA  . TYR A 1 127 ? -9.572  18.271  20.399  1.00 10.68 ? 128 TYR A CA  1 
ATOM   1026 C  C   . TYR A 1 127 ? -9.512  18.654  18.901  1.00 12.32 ? 128 TYR A C   1 
ATOM   1027 O  O   . TYR A 1 127 ? -8.371  18.866  18.286  1.00 11.61 ? 128 TYR A O   1 
ATOM   1028 C  CB  . TYR A 1 127 ? -8.630  17.068  20.676  1.00 9.21  ? 128 TYR A CB  1 
ATOM   1029 C  CG  . TYR A 1 127 ? -8.547  16.823  22.101  1.00 9.45  ? 128 TYR A CG  1 
ATOM   1030 C  CD1 . TYR A 1 127 ? -8.131  17.885  22.966  1.00 11.25 ? 128 TYR A CD1 1 
ATOM   1031 C  CD2 . TYR A 1 127 ? -8.871  15.557  22.696  1.00 10.38 ? 128 TYR A CD2 1 
ATOM   1032 C  CE1 . TYR A 1 127 ? -7.999  17.604  24.351  1.00 10.34 ? 128 TYR A CE1 1 
ATOM   1033 C  CE2 . TYR A 1 127 ? -8.767  15.275  24.068  1.00 12.60 ? 128 TYR A CE2 1 
ATOM   1034 C  CZ  . TYR A 1 127 ? -8.320  16.354  24.905  1.00 13.38 ? 128 TYR A CZ  1 
ATOM   1035 O  OH  . TYR A 1 127 ? -8.258  16.101  26.249  1.00 13.64 ? 128 TYR A OH  1 
ATOM   1036 N  N   . GLY A 1 128 ? -10.713 18.716  18.299  1.00 11.44 ? 129 GLY A N   1 
ATOM   1037 C  CA  . GLY A 1 128 ? -10.863 19.354  16.988  1.00 13.95 ? 129 GLY A CA  1 
ATOM   1038 C  C   . GLY A 1 128 ? -10.397 18.513  15.781  1.00 12.98 ? 129 GLY A C   1 
ATOM   1039 O  O   . GLY A 1 128 ? -10.897 18.603  14.598  1.00 13.39 ? 129 GLY A O   1 
ATOM   1040 N  N   . ASP A 1 129 ? -9.396  17.637  15.976  1.00 11.52 ? 130 ASP A N   1 
ATOM   1041 C  CA  . ASP A 1 129 ? -9.041  16.707  14.874  1.00 13.66 ? 130 ASP A CA  1 
ATOM   1042 C  C   . ASP A 1 129 ? -8.277  15.511  15.454  1.00 13.28 ? 130 ASP A C   1 
ATOM   1043 O  O   . ASP A 1 129 ? -7.817  15.507  16.630  1.00 12.63 ? 130 ASP A O   1 
ATOM   1044 C  CB  . ASP A 1 129 ? -8.382  17.346  13.649  1.00 15.60 ? 130 ASP A CB  1 
ATOM   1045 C  CG  . ASP A 1 129 ? -6.947  17.792  13.884  1.00 18.11 ? 130 ASP A CG  1 
ATOM   1046 O  OD1 . ASP A 1 129 ? -6.271  17.347  14.841  1.00 24.14 ? 130 ASP A OD1 1 
ATOM   1047 O  OD2 . ASP A 1 129 ? -6.487  18.613  13.066  1.00 21.89 ? 130 ASP A OD2 1 
ATOM   1048 N  N   . PHE A 1 130 ? -8.161  14.484  14.597  1.00 13.40 ? 131 PHE A N   1 
ATOM   1049 C  CA  . PHE A 1 130 ? -7.478  13.257  14.993  1.00 12.12 ? 131 PHE A CA  1 
ATOM   1050 C  C   . PHE A 1 130 ? -6.050  13.480  15.424  1.00 11.24 ? 131 PHE A C   1 
ATOM   1051 O  O   . PHE A 1 130 ? -5.595  12.895  16.403  1.00 11.27 ? 131 PHE A O   1 
ATOM   1052 C  CB  . PHE A 1 130 ? -7.577  12.233  13.824  1.00 10.65 ? 131 PHE A CB  1 
ATOM   1053 C  CG  . PHE A 1 130 ? -6.891  10.905  14.114  1.00 11.51 ? 131 PHE A CG  1 
ATOM   1054 C  CD1 . PHE A 1 130 ? -7.592  9.859   14.827  1.00 10.39 ? 131 PHE A CD1 1 
ATOM   1055 C  CD2 . PHE A 1 130 ? -5.563  10.705  13.748  1.00 12.61 ? 131 PHE A CD2 1 
ATOM   1056 C  CE1 . PHE A 1 130 ? -6.941  8.720   15.124  1.00 13.03 ? 131 PHE A CE1 1 
ATOM   1057 C  CE2 . PHE A 1 130 ? -4.961  9.505   14.029  1.00 14.17 ? 131 PHE A CE2 1 
ATOM   1058 C  CZ  . PHE A 1 130 ? -5.701  8.507   14.737  1.00 15.76 ? 131 PHE A CZ  1 
ATOM   1059 N  N   . GLY A 1 131 ? -5.299  14.285  14.634  1.00 11.27 ? 132 GLY A N   1 
ATOM   1060 C  CA  . GLY A 1 131 ? -3.886  14.439  14.904  1.00 13.87 ? 132 GLY A CA  1 
ATOM   1061 C  C   . GLY A 1 131 ? -3.640  15.083  16.263  1.00 11.59 ? 132 GLY A C   1 
ATOM   1062 O  O   . GLY A 1 131 ? -2.653  14.751  16.937  1.00 13.97 ? 132 GLY A O   1 
ATOM   1063 N  N   A LYS A 1 132 ? -4.477  16.027  16.659  0.50 13.02 ? 133 LYS A N   1 
ATOM   1064 N  N   B LYS A 1 132 ? -4.491  16.068  16.607  0.50 13.22 ? 133 LYS A N   1 
ATOM   1065 C  CA  A LYS A 1 132 ? -4.273  16.568  17.984  0.50 11.76 ? 133 LYS A CA  1 
ATOM   1066 C  CA  B LYS A 1 132 ? -4.463  16.673  17.948  0.50 12.64 ? 133 LYS A CA  1 
ATOM   1067 C  C   A LYS A 1 132 ? -4.870  15.665  19.100  0.50 11.27 ? 133 LYS A C   1 
ATOM   1068 C  C   B LYS A 1 132 ? -4.861  15.657  19.037  0.50 11.82 ? 133 LYS A C   1 
ATOM   1069 O  O   A LYS A 1 132 ? -4.344  15.586  20.217  0.50 11.03 ? 133 LYS A O   1 
ATOM   1070 O  O   B LYS A 1 132 ? -4.216  15.510  20.066  0.50 11.04 ? 133 LYS A O   1 
ATOM   1071 C  CB  A LYS A 1 132 ? -4.814  17.986  17.997  0.50 12.48 ? 133 LYS A CB  1 
ATOM   1072 C  CB  B LYS A 1 132 ? -5.406  17.882  18.012  0.50 13.59 ? 133 LYS A CB  1 
ATOM   1073 C  CG  A LYS A 1 132 ? -3.859  18.977  17.280  0.50 12.73 ? 133 LYS A CG  1 
ATOM   1074 C  CG  B LYS A 1 132 ? -4.735  19.218  17.783  0.50 15.42 ? 133 LYS A CG  1 
ATOM   1075 C  CD  A LYS A 1 132 ? -2.645  19.338  18.164  0.50 18.01 ? 133 LYS A CD  1 
ATOM   1076 C  CD  B LYS A 1 132 ? -3.594  19.354  18.851  0.50 15.42 ? 133 LYS A CD  1 
ATOM   1077 C  CE  A LYS A 1 132 ? -2.721  20.700  18.903  0.50 18.66 ? 133 LYS A CE  1 
ATOM   1078 C  CE  B LYS A 1 132 ? -3.825  20.448  19.994  0.50 18.16 ? 133 LYS A CE  1 
ATOM   1079 N  NZ  A LYS A 1 132 ? -1.313  21.219  19.060  0.50 26.37 ? 133 LYS A NZ  1 
ATOM   1080 N  NZ  B LYS A 1 132 ? -4.686  20.189  21.303  0.50 9.95  ? 133 LYS A NZ  1 
ATOM   1081 N  N   . ALA A 1 133 ? -5.946  14.947  18.767  1.00 11.54 ? 134 ALA A N   1 
ATOM   1082 C  CA  . ALA A 1 133 ? -6.487  14.033  19.783  1.00 10.16 ? 134 ALA A CA  1 
ATOM   1083 C  C   . ALA A 1 133 ? -5.504  12.944  20.239  1.00 8.23  ? 134 ALA A C   1 
ATOM   1084 O  O   . ALA A 1 133 ? -5.486  12.492  21.414  1.00 9.50  ? 134 ALA A O   1 
ATOM   1085 C  CB  . ALA A 1 133 ? -7.778  13.330  19.211  1.00 8.63  ? 134 ALA A CB  1 
ATOM   1086 N  N   . VAL A 1 134 ? -4.764  12.393  19.272  1.00 8.08  ? 135 VAL A N   1 
ATOM   1087 C  CA  . VAL A 1 134 ? -3.804  11.259  19.676  1.00 10.19 ? 135 VAL A CA  1 
ATOM   1088 C  C   . VAL A 1 134 ? -2.691  11.708  20.632  1.00 8.89  ? 135 VAL A C   1 
ATOM   1089 O  O   . VAL A 1 134 ? -1.997  10.896  21.235  1.00 10.54 ? 135 VAL A O   1 
ATOM   1090 C  CB  . VAL A 1 134 ? -3.156  10.510  18.486  1.00 10.88 ? 135 VAL A CB  1 
ATOM   1091 C  CG1 . VAL A 1 134 ? -4.229  9.855   17.668  1.00 12.08 ? 135 VAL A CG1 1 
ATOM   1092 C  CG2 . VAL A 1 134 ? -2.260  11.480  17.637  1.00 13.38 ? 135 VAL A CG2 1 
ATOM   1093 N  N   A GLN A 1 135 ? -2.529  13.025  20.774  0.50 9.95  ? 136 GLN A N   1 
ATOM   1094 N  N   B GLN A 1 135 ? -2.606  13.042  20.786  0.50 9.84  ? 136 GLN A N   1 
ATOM   1095 C  CA  A GLN A 1 135 ? -1.499  13.472  21.712  0.50 11.67 ? 136 GLN A CA  1 
ATOM   1096 C  CA  B GLN A 1 135 ? -1.633  13.670  21.697  0.50 11.82 ? 136 GLN A CA  1 
ATOM   1097 C  C   A GLN A 1 135 ? -2.062  13.542  23.134  0.50 11.20 ? 136 GLN A C   1 
ATOM   1098 C  C   B GLN A 1 135 ? -2.184  13.828  23.091  0.50 12.10 ? 136 GLN A C   1 
ATOM   1099 O  O   A GLN A 1 135 ? -1.321  13.897  24.052  0.50 10.92 ? 136 GLN A O   1 
ATOM   1100 O  O   B GLN A 1 135 ? -1.597  14.541  23.946  0.50 9.77  ? 136 GLN A O   1 
ATOM   1101 C  CB  A GLN A 1 135 ? -0.873  14.818  21.202  0.50 11.14 ? 136 GLN A CB  1 
ATOM   1102 C  CB  B GLN A 1 135 ? -1.256  15.052  21.112  0.50 10.25 ? 136 GLN A CB  1 
ATOM   1103 C  CG  A GLN A 1 135 ? 0.031   14.625  19.918  0.50 13.16 ? 136 GLN A CG  1 
ATOM   1104 C  CG  B GLN A 1 135 ? -0.658  14.863  19.748  0.50 12.37 ? 136 GLN A CG  1 
ATOM   1105 C  CD  A GLN A 1 135 ? 1.275   13.764  20.158  0.50 13.77 ? 136 GLN A CD  1 
ATOM   1106 C  CD  B GLN A 1 135 ? -0.036  16.112  19.217  0.50 19.73 ? 136 GLN A CD  1 
ATOM   1107 O  OE1 A GLN A 1 135 ? 1.832   13.767  21.237  0.50 20.25 ? 136 GLN A OE1 1 
ATOM   1108 O  OE1 B GLN A 1 135 ? 0.803   16.744  19.876  0.50 23.75 ? 136 GLN A OE1 1 
ATOM   1109 N  NE2 A GLN A 1 135 ? 1.719   13.017  19.117  0.50 15.60 ? 136 GLN A NE2 1 
ATOM   1110 N  NE2 B GLN A 1 135 ? -0.445  16.484  18.022  0.50 19.48 ? 136 GLN A NE2 1 
ATOM   1111 N  N   . GLN A 1 136 ? -3.383  13.280  23.321  1.00 10.53 ? 137 GLN A N   1 
ATOM   1112 C  CA  . GLN A 1 136 ? -4.054  13.507  24.571  1.00 9.82  ? 137 GLN A CA  1 
ATOM   1113 C  C   . GLN A 1 136 ? -4.490  12.182  25.197  1.00 10.68 ? 137 GLN A C   1 
ATOM   1114 O  O   . GLN A 1 136 ? -4.875  11.237  24.512  1.00 7.85  ? 137 GLN A O   1 
ATOM   1115 C  CB  . GLN A 1 136 ? -5.318  14.351  24.435  1.00 11.31 ? 137 GLN A CB  1 
ATOM   1116 C  CG  . GLN A 1 136 ? -5.057  15.678  23.658  1.00 15.68 ? 137 GLN A CG  1 
ATOM   1117 C  CD  . GLN A 1 136 ? -4.084  16.583  24.439  1.00 14.69 ? 137 GLN A CD  1 
ATOM   1118 O  OE1 . GLN A 1 136 ? -3.941  16.469  25.623  1.00 19.06 ? 137 GLN A OE1 1 
ATOM   1119 N  NE2 . GLN A 1 136 ? -3.294  17.372  23.686  1.00 30.02 ? 137 GLN A NE2 1 
ATOM   1120 N  N   . PRO A 1 137 ? -4.476  12.087  26.539  1.00 10.88 ? 138 PRO A N   1 
ATOM   1121 C  CA  . PRO A 1 137 ? -4.728  10.780  27.168  1.00 11.42 ? 138 PRO A CA  1 
ATOM   1122 C  C   . PRO A 1 137 ? -6.164  10.331  27.043  1.00 10.37 ? 138 PRO A C   1 
ATOM   1123 O  O   . PRO A 1 137 ? -6.412  9.125   27.234  1.00 12.66 ? 138 PRO A O   1 
ATOM   1124 C  CB  . PRO A 1 137 ? -4.412  10.982  28.686  1.00 11.77 ? 138 PRO A CB  1 
ATOM   1125 C  CG  . PRO A 1 137 ? -4.253  12.454  28.803  1.00 16.25 ? 138 PRO A CG  1 
ATOM   1126 C  CD  . PRO A 1 137 ? -4.102  13.183  27.487  1.00 11.68 ? 138 PRO A CD  1 
ATOM   1127 N  N   . ASP A 1 138 ? -7.087  11.253  26.707  1.00 7.51  ? 139 ASP A N   1 
ATOM   1128 C  CA  . ASP A 1 138 ? -8.499  10.833  26.527  1.00 9.73  ? 139 ASP A CA  1 
ATOM   1129 C  C   . ASP A 1 138 ? -8.828  11.217  25.034  1.00 8.68  ? 139 ASP A C   1 
ATOM   1130 O  O   . ASP A 1 138 ? -9.988  11.653  24.745  1.00 10.59 ? 139 ASP A O   1 
ATOM   1131 C  CB  . ASP A 1 138 ? -9.436  11.590  27.467  1.00 9.76  ? 139 ASP A CB  1 
ATOM   1132 C  CG  . ASP A 1 138 ? -9.255  13.108  27.403  1.00 10.17 ? 139 ASP A CG  1 
ATOM   1133 O  OD1 . ASP A 1 138 ? -8.299  13.593  26.755  1.00 13.52 ? 139 ASP A OD1 1 
ATOM   1134 O  OD2 . ASP A 1 138 ? -10.078 13.815  28.023  1.00 17.20 ? 139 ASP A OD2 1 
ATOM   1135 N  N   . GLY A 1 139 ? -7.867  11.113  24.098  1.00 7.34  ? 140 GLY A N   1 
ATOM   1136 C  CA  . GLY A 1 139 ? -8.129  11.591  22.777  1.00 8.05  ? 140 GLY A CA  1 
ATOM   1137 C  C   . GLY A 1 139 ? -8.968  10.700  21.893  1.00 8.96  ? 140 GLY A C   1 
ATOM   1138 O  O   . GLY A 1 139 ? -9.637  11.187  21.005  1.00 7.30  ? 140 GLY A O   1 
ATOM   1139 N  N   . LEU A 1 140 ? -8.808  9.393   22.058  1.00 6.56  ? 141 LEU A N   1 
ATOM   1140 C  CA  . LEU A 1 140 ? -9.493  8.404   21.218  1.00 6.54  ? 141 LEU A CA  1 
ATOM   1141 C  C   . LEU A 1 140 ? -10.383 7.498   22.004  1.00 7.64  ? 141 LEU A C   1 
ATOM   1142 O  O   . LEU A 1 140 ? -10.128 7.237   23.147  1.00 6.90  ? 141 LEU A O   1 
ATOM   1143 C  CB  . LEU A 1 140 ? -8.502  7.498   20.532  1.00 6.42  ? 141 LEU A CB  1 
ATOM   1144 C  CG  . LEU A 1 140 ? -7.537  8.196   19.546  1.00 10.99 ? 141 LEU A CG  1 
ATOM   1145 C  CD1 . LEU A 1 140 ? -6.911  7.144   18.576  1.00 9.23  ? 141 LEU A CD1 1 
ATOM   1146 C  CD2 . LEU A 1 140 ? -8.120  9.304   18.665  1.00 12.13 ? 141 LEU A CD2 1 
ATOM   1147 N  N   . ALA A 1 141 ? -11.437 7.035   21.344  1.00 6.40  ? 142 ALA A N   1 
ATOM   1148 C  CA  . ALA A 1 141 ? -12.235 5.905   21.877  1.00 6.23  ? 142 ALA A CA  1 
ATOM   1149 C  C   . ALA A 1 141 ? -12.314 4.871   20.751  1.00 5.58  ? 142 ALA A C   1 
ATOM   1150 O  O   . ALA A 1 141 ? -12.644 5.237   19.642  1.00 7.08  ? 142 ALA A O   1 
ATOM   1151 C  CB  . ALA A 1 141 ? -13.578 6.356   22.319  1.00 6.94  ? 142 ALA A CB  1 
ATOM   1152 N  N   . VAL A 1 142 ? -11.713 3.678   21.021  1.00 6.26  ? 143 VAL A N   1 
ATOM   1153 C  CA  . VAL A 1 142 ? -11.769 2.641   20.029  1.00 6.76  ? 143 VAL A CA  1 
ATOM   1154 C  C   . VAL A 1 142 ? -12.756 1.579   20.484  1.00 8.68  ? 143 VAL A C   1 
ATOM   1155 O  O   . VAL A 1 142 ? -12.604 1.047   21.564  1.00 7.24  ? 143 VAL A O   1 
ATOM   1156 C  CB  . VAL A 1 142 ? -10.385 2.041   19.669  1.00 8.29  ? 143 VAL A CB  1 
ATOM   1157 C  CG1 . VAL A 1 142 ? -10.511 1.063   18.516  1.00 7.38  ? 143 VAL A CG1 1 
ATOM   1158 C  CG2 . VAL A 1 142 ? -9.400  3.176   19.263  1.00 7.54  ? 143 VAL A CG2 1 
ATOM   1159 N  N   . LEU A 1 143 ? -13.689 1.232   19.621  1.00 6.76  ? 144 LEU A N   1 
ATOM   1160 C  CA  . LEU A 1 143 ? -14.710 0.215   19.916  1.00 7.53  ? 144 LEU A CA  1 
ATOM   1161 C  C   . LEU A 1 143 ? -14.154 -1.047  19.233  1.00 8.42  ? 144 LEU A C   1 
ATOM   1162 O  O   . LEU A 1 143 ? -14.028 -1.050  17.972  1.00 7.80  ? 144 LEU A O   1 
ATOM   1163 C  CB  . LEU A 1 143 ? -16.087 0.623   19.324  1.00 7.18  ? 144 LEU A CB  1 
ATOM   1164 C  CG  . LEU A 1 143 ? -17.201 -0.363  19.438  1.00 7.40  ? 144 LEU A CG  1 
ATOM   1165 C  CD1 . LEU A 1 143 ? -17.390 -0.776  20.831  1.00 10.37 ? 144 LEU A CD1 1 
ATOM   1166 C  CD2 . LEU A 1 143 ? -18.472 0.267   18.787  1.00 8.78  ? 144 LEU A CD2 1 
ATOM   1167 N  N   . GLY A 1 144 ? -13.841 -2.096  20.055  1.00 6.42  ? 145 GLY A N   1 
ATOM   1168 C  CA  . GLY A 1 144 ? -13.276 -3.330  19.540  1.00 5.81  ? 145 GLY A CA  1 
ATOM   1169 C  C   . GLY A 1 144 ? -14.340 -4.428  19.523  1.00 5.43  ? 145 GLY A C   1 
ATOM   1170 O  O   . GLY A 1 144 ? -15.113 -4.526  20.493  1.00 6.57  ? 145 GLY A O   1 
ATOM   1171 N  N   . ILE A 1 145 ? -14.422 -5.139  18.389  1.00 5.25  ? 146 ILE A N   1 
ATOM   1172 C  CA  . ILE A 1 145 ? -15.509 -6.187  18.285  1.00 4.67  ? 146 ILE A CA  1 
ATOM   1173 C  C   . ILE A 1 145 ? -14.738 -7.435  17.745  1.00 6.36  ? 146 ILE A C   1 
ATOM   1174 O  O   . ILE A 1 145 ? -14.041 -7.371  16.728  1.00 6.86  ? 146 ILE A O   1 
ATOM   1175 C  CB  . ILE A 1 145 ? -16.532 -5.710  17.248  1.00 4.75  ? 146 ILE A CB  1 
ATOM   1176 C  CG1 . ILE A 1 145 ? -17.125 -4.444  17.767  1.00 5.90  ? 146 ILE A CG1 1 
ATOM   1177 C  CG2 . ILE A 1 145 ? -17.634 -6.790  17.065  1.00 6.00  ? 146 ILE A CG2 1 
ATOM   1178 C  CD1 . ILE A 1 145 ? -18.257 -3.812  16.843  1.00 7.07  ? 146 ILE A CD1 1 
ATOM   1179 N  N   . PHE A 1 146 ? -14.905 -8.546  18.420  1.00 7.04  ? 147 PHE A N   1 
ATOM   1180 C  CA  . PHE A 1 146 ? -14.226 -9.790  17.968  1.00 6.13  ? 147 PHE A CA  1 
ATOM   1181 C  C   . PHE A 1 146 ? -15.020 -10.439 16.840  1.00 6.47  ? 147 PHE A C   1 
ATOM   1182 O  O   . PHE A 1 146 ? -16.243 -10.314 16.793  1.00 8.39  ? 147 PHE A O   1 
ATOM   1183 C  CB  . PHE A 1 146 ? -14.294 -10.749 19.138  1.00 7.05  ? 147 PHE A CB  1 
ATOM   1184 C  CG  . PHE A 1 146 ? -13.466 -10.261 20.271  1.00 5.55  ? 147 PHE A CG  1 
ATOM   1185 C  CD1 . PHE A 1 146 ? -12.071 -10.141 20.087  1.00 5.60  ? 147 PHE A CD1 1 
ATOM   1186 C  CD2 . PHE A 1 146 ? -14.010 -10.021 21.496  1.00 6.74  ? 147 PHE A CD2 1 
ATOM   1187 C  CE1 . PHE A 1 146 ? -11.224 -9.672  21.141  1.00 5.43  ? 147 PHE A CE1 1 
ATOM   1188 C  CE2 . PHE A 1 146 ? -13.207 -9.613  22.590  1.00 8.45  ? 147 PHE A CE2 1 
ATOM   1189 C  CZ  . PHE A 1 146 ? -11.801 -9.485  22.369  1.00 7.59  ? 147 PHE A CZ  1 
ATOM   1190 N  N   . LEU A 1 147 ? -14.272 -11.080 15.960  1.00 6.10  ? 148 LEU A N   1 
ATOM   1191 C  CA  . LEU A 1 147 ? -14.913 -11.890 14.885  1.00 7.08  ? 148 LEU A CA  1 
ATOM   1192 C  C   . LEU A 1 147 ? -14.617 -13.333 15.115  1.00 9.15  ? 148 LEU A C   1 
ATOM   1193 O  O   . LEU A 1 147 ? -13.431 -13.691 15.246  1.00 9.54  ? 148 LEU A O   1 
ATOM   1194 C  CB  . LEU A 1 147 ? -14.305 -11.485 13.518  1.00 8.32  ? 148 LEU A CB  1 
ATOM   1195 C  CG  . LEU A 1 147 ? -14.956 -10.264 12.841  1.00 6.07  ? 148 LEU A CG  1 
ATOM   1196 C  CD1 . LEU A 1 147 ? -14.752 -8.934  13.716  1.00 9.54  ? 148 LEU A CD1 1 
ATOM   1197 C  CD2 . LEU A 1 147 ? -14.275 -10.047 11.465  1.00 9.07  ? 148 LEU A CD2 1 
ATOM   1198 N  N   . LYS A 1 148 ? -15.668 -14.178 15.064  1.00 8.89  ? 149 LYS A N   1 
ATOM   1199 C  CA  . LYS A 1 148 ? -15.432 -15.633 15.081  1.00 8.96  ? 149 LYS A CA  1 
ATOM   1200 C  C   . LYS A 1 148 ? -15.924 -16.135 13.726  1.00 11.27 ? 149 LYS A C   1 
ATOM   1201 O  O   . LYS A 1 148 ? -16.751 -15.468 13.053  1.00 9.32  ? 149 LYS A O   1 
ATOM   1202 C  CB  . LYS A 1 148 ? -16.225 -16.355 16.148  1.00 10.53 ? 149 LYS A CB  1 
ATOM   1203 C  CG  . LYS A 1 148 ? -17.759 -16.150 16.091  1.00 13.26 ? 149 LYS A CG  1 
ATOM   1204 C  CD  . LYS A 1 148 ? -18.348 -16.955 17.253  1.00 22.82 ? 149 LYS A CD  1 
ATOM   1205 C  CE  . LYS A 1 148 ? -19.832 -16.773 17.257  1.00 25.15 ? 149 LYS A CE  1 
ATOM   1206 N  NZ  . LYS A 1 148 ? -20.482 -17.607 18.314  1.00 33.80 ? 149 LYS A NZ  1 
ATOM   1207 N  N   . VAL A 1 149 ? -15.445 -17.297 13.307  1.00 10.67 ? 150 VAL A N   1 
ATOM   1208 C  CA  . VAL A 1 149 ? -15.835 -17.823 11.992  1.00 10.23 ? 150 VAL A CA  1 
ATOM   1209 C  C   . VAL A 1 149 ? -17.036 -18.792 12.244  1.00 10.11 ? 150 VAL A C   1 
ATOM   1210 O  O   . VAL A 1 149 ? -16.986 -19.749 13.062  1.00 11.86 ? 150 VAL A O   1 
ATOM   1211 C  CB  . VAL A 1 149 ? -14.670 -18.638 11.414  1.00 10.06 ? 150 VAL A CB  1 
ATOM   1212 C  CG1 . VAL A 1 149 ? -15.090 -19.317 10.100  1.00 13.65 ? 150 VAL A CG1 1 
ATOM   1213 C  CG2 . VAL A 1 149 ? -13.521 -17.697 11.109  1.00 12.67 ? 150 VAL A CG2 1 
ATOM   1214 N  N   . GLY A 1 150 ? -18.033 -18.554 11.435  1.00 9.15  ? 151 GLY A N   1 
ATOM   1215 C  CA  . GLY A 1 150 ? -19.221 -19.396 11.474  1.00 10.89 ? 151 GLY A CA  1 
ATOM   1216 C  C   . GLY A 1 150 ? -20.115 -18.937 10.322  1.00 8.88  ? 151 GLY A C   1 
ATOM   1217 O  O   . GLY A 1 150 ? -19.743 -19.006 9.143   1.00 11.91 ? 151 GLY A O   1 
ATOM   1218 N  N   A SER A 1 151 ? -21.324 -18.464 10.682  0.50 11.68 ? 152 SER A N   1 
ATOM   1219 N  N   B SER A 1 151 ? -21.285 -18.425 10.725  0.50 11.48 ? 152 SER A N   1 
ATOM   1220 C  CA  A SER A 1 151 ? -22.234 -17.938 9.627   0.50 12.36 ? 152 SER A CA  1 
ATOM   1221 C  CA  B SER A 1 151 ? -22.185 -17.808 9.745   0.50 12.53 ? 152 SER A CA  1 
ATOM   1222 C  C   A SER A 1 151 ? -21.693 -16.590 9.120   0.50 13.13 ? 152 SER A C   1 
ATOM   1223 C  C   B SER A 1 151 ? -21.542 -16.557 9.073   0.50 13.21 ? 152 SER A C   1 
ATOM   1224 O  O   A SER A 1 151 ? -21.030 -15.886 9.905   0.50 11.19 ? 152 SER A O   1 
ATOM   1225 O  O   B SER A 1 151 ? -20.660 -15.879 9.659   0.50 11.43 ? 152 SER A O   1 
ATOM   1226 C  CB  A SER A 1 151 ? -23.594 -17.706 10.204  0.50 15.03 ? 152 SER A CB  1 
ATOM   1227 C  CB  B SER A 1 151 ? -23.414 -17.402 10.477  0.50 14.37 ? 152 SER A CB  1 
ATOM   1228 O  OG  A SER A 1 151 ? -23.535 -16.704 11.224  0.50 17.61 ? 152 SER A OG  1 
ATOM   1229 O  OG  B SER A 1 151 ? -24.141 -18.568 10.846  0.50 17.12 ? 152 SER A OG  1 
ATOM   1230 N  N   . ALA A 1 152 ? -21.958 -16.255 7.841   1.00 12.46 ? 153 ALA A N   1 
ATOM   1231 C  CA  . ALA A 1 152 ? -21.512 -15.000 7.236   1.00 12.04 ? 153 ALA A CA  1 
ATOM   1232 C  C   . ALA A 1 152 ? -22.180 -13.770 7.963   1.00 10.95 ? 153 ALA A C   1 
ATOM   1233 O  O   . ALA A 1 152 ? -23.313 -13.865 8.543   1.00 12.37 ? 153 ALA A O   1 
ATOM   1234 C  CB  . ALA A 1 152 ? -21.947 -14.930 5.727   1.00 12.49 ? 153 ALA A CB  1 
ATOM   1235 N  N   . LYS A 1 153 ? -21.443 -12.626 7.894   1.00 11.49 ? 154 LYS A N   1 
ATOM   1236 C  CA  . LYS A 1 153 ? -22.012 -11.358 8.341   1.00 13.39 ? 154 LYS A CA  1 
ATOM   1237 C  C   . LYS A 1 153 ? -22.400 -10.599 7.074   1.00 11.29 ? 154 LYS A C   1 
ATOM   1238 O  O   . LYS A 1 153 ? -21.573 -10.165 6.302   1.00 11.54 ? 154 LYS A O   1 
ATOM   1239 C  CB  . LYS A 1 153 ? -20.979 -10.528 9.173   1.00 14.36 ? 154 LYS A CB  1 
ATOM   1240 C  CG  . LYS A 1 153 ? -21.591 -9.379  9.975   1.00 14.72 ? 154 LYS A CG  1 
ATOM   1241 C  CD  . LYS A 1 153 ? -22.581 -9.789  11.048  1.00 15.68 ? 154 LYS A CD  1 
ATOM   1242 C  CE  . LYS A 1 153 ? -22.893 -8.662  12.038  1.00 19.33 ? 154 LYS A CE  1 
ATOM   1243 N  NZ  . LYS A 1 153 ? -23.871 -9.112  12.972  1.00 22.98 ? 154 LYS A NZ  1 
ATOM   1244 N  N   . PRO A 1 154 ? -23.728 -10.543 6.795   1.00 13.17 ? 155 PRO A N   1 
ATOM   1245 C  CA  . PRO A 1 154 ? -24.172 -9.929  5.500   1.00 13.32 ? 155 PRO A CA  1 
ATOM   1246 C  C   . PRO A 1 154 ? -23.689 -8.500  5.384   1.00 13.09 ? 155 PRO A C   1 
ATOM   1247 O  O   . PRO A 1 154 ? -23.168 -8.130  4.317   1.00 14.09 ? 155 PRO A O   1 
ATOM   1248 C  CB  . PRO A 1 154 ? -25.706 -10.008 5.569   1.00 16.23 ? 155 PRO A CB  1 
ATOM   1249 C  CG  . PRO A 1 154 ? -25.984 -11.101 6.647   1.00 16.75 ? 155 PRO A CG  1 
ATOM   1250 C  CD  . PRO A 1 154 ? -24.839 -11.027 7.624   1.00 15.49 ? 155 PRO A CD  1 
ATOM   1251 N  N   . GLY A 1 155 ? -23.674 -7.804  6.522   1.00 12.69 ? 156 GLY A N   1 
ATOM   1252 C  CA  . GLY A 1 155 ? -23.261 -6.394  6.498   1.00 13.92 ? 156 GLY A CA  1 
ATOM   1253 C  C   . GLY A 1 155 ? -21.760 -6.194  6.225   1.00 13.45 ? 156 GLY A C   1 
ATOM   1254 O  O   . GLY A 1 155 ? -21.293 -5.032  6.034   1.00 17.06 ? 156 GLY A O   1 
ATOM   1255 N  N   . LEU A 1 156 ? -20.960 -7.268  6.326   1.00 12.14 ? 157 LEU A N   1 
ATOM   1256 C  CA  . LEU A 1 156 ? -19.565 -7.213  5.957   1.00 10.23 ? 157 LEU A CA  1 
ATOM   1257 C  C   . LEU A 1 156 ? -19.233 -7.417  4.495   1.00 10.34 ? 157 LEU A C   1 
ATOM   1258 O  O   . LEU A 1 156 ? -18.094 -7.136  3.962   1.00 11.84 ? 157 LEU A O   1 
ATOM   1259 C  CB  . LEU A 1 156 ? -18.709 -8.183  6.844   1.00 10.54 ? 157 LEU A CB  1 
ATOM   1260 C  CG  . LEU A 1 156 ? -17.204 -8.384  6.562   1.00 10.06 ? 157 LEU A CG  1 
ATOM   1261 C  CD1 . LEU A 1 156 ? -16.498 -7.002  6.945   1.00 11.38 ? 157 LEU A CD1 1 
ATOM   1262 C  CD2 . LEU A 1 156 ? -16.617 -9.535  7.486   1.00 11.11 ? 157 LEU A CD2 1 
ATOM   1263 N  N   . GLN A 1 157 ? -20.213 -7.989  3.743   1.00 11.39 ? 158 GLN A N   1 
ATOM   1264 C  CA  . GLN A 1 157 ? -19.895 -8.438  2.419   1.00 13.13 ? 158 GLN A CA  1 
ATOM   1265 C  C   . GLN A 1 157 ? -19.477 -7.312  1.461   1.00 8.61  ? 158 GLN A C   1 
ATOM   1266 O  O   . GLN A 1 157 ? -18.598 -7.531  0.667   1.00 12.09 ? 158 GLN A O   1 
ATOM   1267 C  CB  . GLN A 1 157 ? -21.005 -9.305  1.830   1.00 13.85 ? 158 GLN A CB  1 
ATOM   1268 C  CG  . GLN A 1 157 ? -20.505 -9.935  0.485   1.00 16.34 ? 158 GLN A CG  1 
ATOM   1269 C  CD  . GLN A 1 157 ? -19.428 -11.014 0.725   1.00 15.17 ? 158 GLN A CD  1 
ATOM   1270 O  OE1 . GLN A 1 157 ? -19.366 -11.606 1.842   1.00 16.83 ? 158 GLN A OE1 1 
ATOM   1271 N  NE2 . GLN A 1 157 ? -18.562 -11.263 -0.256  1.00 17.56 ? 158 GLN A NE2 1 
ATOM   1272 N  N   A LYS A 1 158 ? -20.044 -6.100  1.560   0.50 12.29 ? 159 LYS A N   1 
ATOM   1273 N  N   B LYS A 1 158 ? -20.101 -6.114  1.620   0.50 12.49 ? 159 LYS A N   1 
ATOM   1274 C  CA  A LYS A 1 158 ? -19.540 -5.069  0.637   0.50 12.25 ? 159 LYS A CA  1 
ATOM   1275 C  CA  B LYS A 1 158 ? -19.685 -4.963  0.805   0.50 12.91 ? 159 LYS A CA  1 
ATOM   1276 C  C   A LYS A 1 158 ? -18.009 -4.741  0.847   0.50 11.49 ? 159 LYS A C   1 
ATOM   1277 C  C   B LYS A 1 158 ? -18.153 -4.655  0.905   0.50 13.16 ? 159 LYS A C   1 
ATOM   1278 O  O   A LYS A 1 158 ? -17.227 -4.498  -0.086  0.50 12.73 ? 159 LYS A O   1 
ATOM   1279 O  O   B LYS A 1 158 ? -17.537 -4.288  -0.053  0.50 14.89 ? 159 LYS A O   1 
ATOM   1280 C  CB  A LYS A 1 158 ? -20.450 -3.862  0.764   0.50 12.47 ? 159 LYS A CB  1 
ATOM   1281 C  CB  B LYS A 1 158 ? -20.500 -3.724  1.157   0.50 13.87 ? 159 LYS A CB  1 
ATOM   1282 C  CG  A LYS A 1 158 ? -20.047 -2.655  0.031   0.50 15.51 ? 159 LYS A CG  1 
ATOM   1283 C  CG  B LYS A 1 158 ? -21.927 -3.674  0.698   0.50 15.52 ? 159 LYS A CG  1 
ATOM   1284 C  CD  A LYS A 1 158 ? -20.769 -2.482  -1.314  0.50 18.54 ? 159 LYS A CD  1 
ATOM   1285 C  CD  B LYS A 1 158 ? -22.350 -2.194  0.840   0.50 15.56 ? 159 LYS A CD  1 
ATOM   1286 C  CE  A LYS A 1 158 ? -20.100 -1.345  -2.141  0.50 16.13 ? 159 LYS A CE  1 
ATOM   1287 C  CE  B LYS A 1 158 ? -21.050 -1.360  0.583   0.50 10.14 ? 159 LYS A CE  1 
ATOM   1288 N  NZ  A LYS A 1 158 ? -20.697 -0.023  -1.931  0.50 17.57 ? 159 LYS A NZ  1 
ATOM   1289 N  NZ  B LYS A 1 158 ? -20.988 0.106   0.272   0.50 17.09 ? 159 LYS A NZ  1 
ATOM   1290 N  N   . VAL A 1 159 ? -17.586 -4.782  2.124   1.00 11.66 ? 160 VAL A N   1 
ATOM   1291 C  CA  . VAL A 1 159 ? -16.164 -4.546  2.361   1.00 12.38 ? 160 VAL A CA  1 
ATOM   1292 C  C   . VAL A 1 159 ? -15.386 -5.684  1.648   1.00 11.42 ? 160 VAL A C   1 
ATOM   1293 O  O   . VAL A 1 159 ? -14.481 -5.464  0.938   1.00 12.73 ? 160 VAL A O   1 
ATOM   1294 C  CB  . VAL A 1 159 ? -15.925 -4.639  3.843   1.00 13.25 ? 160 VAL A CB  1 
ATOM   1295 C  CG1 . VAL A 1 159 ? -14.444 -4.606  4.148   1.00 13.61 ? 160 VAL A CG1 1 
ATOM   1296 C  CG2 . VAL A 1 159 ? -16.702 -3.482  4.534   1.00 14.47 ? 160 VAL A CG2 1 
ATOM   1297 N  N   . VAL A 1 160 ? -15.789 -6.959  1.886   1.00 11.28 ? 161 VAL A N   1 
ATOM   1298 C  CA  . VAL A 1 160 ? -15.051 -8.087  1.404   1.00 13.40 ? 161 VAL A CA  1 
ATOM   1299 C  C   . VAL A 1 160 ? -15.032 -8.051  -0.126  1.00 11.93 ? 161 VAL A C   1 
ATOM   1300 O  O   . VAL A 1 160 ? -14.004 -8.279  -0.744  1.00 13.34 ? 161 VAL A O   1 
ATOM   1301 C  CB  . VAL A 1 160 ? -15.760 -9.464  1.933   1.00 15.09 ? 161 VAL A CB  1 
ATOM   1302 C  CG1 . VAL A 1 160 ? -15.392 -10.684 1.057   1.00 20.54 ? 161 VAL A CG1 1 
ATOM   1303 C  CG2 . VAL A 1 160 ? -15.435 -9.604  3.436   1.00 17.68 ? 161 VAL A CG2 1 
ATOM   1304 N  N   . ASP A 1 161 ? -16.101 -7.567  -0.715  1.00 13.96 ? 162 ASP A N   1 
ATOM   1305 C  CA  . ASP A 1 161 ? -16.139 -7.657  -2.160  1.00 17.63 ? 162 ASP A CA  1 
ATOM   1306 C  C   . ASP A 1 161 ? -15.226 -6.626  -2.884  1.00 17.60 ? 162 ASP A C   1 
ATOM   1307 O  O   . ASP A 1 161 ? -14.801 -6.848  -4.033  1.00 20.67 ? 162 ASP A O   1 
ATOM   1308 C  CB  . ASP A 1 161 ? -17.537 -7.551  -2.595  1.00 17.09 ? 162 ASP A CB  1 
ATOM   1309 C  CG  . ASP A 1 161 ? -18.236 -8.883  -2.618  1.00 20.54 ? 162 ASP A CG  1 
ATOM   1310 O  OD1 . ASP A 1 161 ? -17.540 -9.937  -2.705  1.00 21.71 ? 162 ASP A OD1 1 
ATOM   1311 O  OD2 . ASP A 1 161 ? -19.475 -8.839  -2.524  1.00 23.07 ? 162 ASP A OD2 1 
ATOM   1312 N  N   . VAL A 1 162 ? -14.895 -5.528  -2.182  1.00 15.67 ? 163 VAL A N   1 
ATOM   1313 C  CA  . VAL A 1 162 ? -14.034 -4.469  -2.776  1.00 17.32 ? 163 VAL A CA  1 
ATOM   1314 C  C   . VAL A 1 162 ? -12.516 -4.751  -2.623  1.00 15.85 ? 163 VAL A C   1 
ATOM   1315 O  O   . VAL A 1 162 ? -11.663 -4.060  -3.181  1.00 15.31 ? 163 VAL A O   1 
ATOM   1316 C  CB  . VAL A 1 162 ? -14.461 -3.101  -2.203  1.00 18.08 ? 163 VAL A CB  1 
ATOM   1317 C  CG1 . VAL A 1 162 ? -13.644 -2.786  -1.025  1.00 17.09 ? 163 VAL A CG1 1 
ATOM   1318 C  CG2 . VAL A 1 162 ? -14.258 -1.898  -3.184  1.00 19.84 ? 163 VAL A CG2 1 
ATOM   1319 N  N   . LEU A 1 163 ? -12.143 -5.742  -1.763  1.00 15.44 ? 164 LEU A N   1 
ATOM   1320 C  CA  . LEU A 1 163 ? -10.726 -6.036  -1.439  1.00 14.76 ? 164 LEU A CA  1 
ATOM   1321 C  C   . LEU A 1 163 ? -9.793  -6.313  -2.621  1.00 15.45 ? 164 LEU A C   1 
ATOM   1322 O  O   . LEU A 1 163 ? -8.687  -5.887  -2.619  1.00 15.49 ? 164 LEU A O   1 
ATOM   1323 C  CB  . LEU A 1 163 ? -10.500 -7.040  -0.286  1.00 13.48 ? 164 LEU A CB  1 
ATOM   1324 C  CG  . LEU A 1 163 ? -11.269 -6.656  0.991   1.00 13.79 ? 164 LEU A CG  1 
ATOM   1325 C  CD1 . LEU A 1 163 ? -11.096 -7.814  2.026   1.00 15.88 ? 164 LEU A CD1 1 
ATOM   1326 C  CD2 . LEU A 1 163 ? -10.710 -5.328  1.526   1.00 11.48 ? 164 LEU A CD2 1 
ATOM   1327 N  N   . ASP A 1 164 ? -10.317 -7.001  -3.636  1.00 18.39 ? 165 ASP A N   1 
ATOM   1328 C  CA  . ASP A 1 164 ? -9.491  -7.272  -4.781  1.00 21.18 ? 165 ASP A CA  1 
ATOM   1329 C  C   . ASP A 1 164 ? -9.093  -5.940  -5.488  1.00 20.36 ? 165 ASP A C   1 
ATOM   1330 O  O   . ASP A 1 164 ? -8.078  -5.933  -6.177  1.00 23.03 ? 165 ASP A O   1 
ATOM   1331 C  CB  . ASP A 1 164 ? -10.296 -8.196  -5.712  1.00 22.26 ? 165 ASP A CB  1 
ATOM   1332 C  CG  . ASP A 1 164 ? -11.254 -7.436  -6.465  1.00 23.25 ? 165 ASP A CG  1 
ATOM   1333 O  OD1 . ASP A 1 164 ? -12.271 -7.012  -5.886  1.00 23.61 ? 165 ASP A OD1 1 
ATOM   1334 O  OD2 . ASP A 1 164 ? -10.946 -7.138  -7.663  1.00 28.96 ? 165 ASP A OD2 1 
ATOM   1335 N  N   . SER A 1 165 ? -9.809  -4.835  -5.263  1.00 18.50 ? 166 SER A N   1 
ATOM   1336 C  CA  . SER A 1 165 ? -9.459  -3.550  -5.868  1.00 19.61 ? 166 SER A CA  1 
ATOM   1337 C  C   . SER A 1 165 ? -8.385  -2.787  -5.087  1.00 19.93 ? 166 SER A C   1 
ATOM   1338 O  O   . SER A 1 165 ? -7.792  -1.833  -5.618  1.00 20.31 ? 166 SER A O   1 
ATOM   1339 C  CB  . SER A 1 165 ? -10.711 -2.725  -6.117  1.00 21.35 ? 166 SER A CB  1 
ATOM   1340 O  OG  . SER A 1 165 ? -11.186 -2.157  -4.944  1.00 22.91 ? 166 SER A OG  1 
ATOM   1341 N  N   . ILE A 1 166 ? -8.065  -3.232  -3.849  1.00 15.95 ? 167 ILE A N   1 
ATOM   1342 C  CA  . ILE A 1 166 ? -7.015  -2.573  -3.044  1.00 15.56 ? 167 ILE A CA  1 
ATOM   1343 C  C   . ILE A 1 166 ? -6.064  -3.647  -2.511  1.00 14.40 ? 167 ILE A C   1 
ATOM   1344 O  O   . ILE A 1 166 ? -5.660  -3.681  -1.362  1.00 14.68 ? 167 ILE A O   1 
ATOM   1345 C  CB  . ILE A 1 166 ? -7.680  -1.746  -1.876  1.00 14.83 ? 167 ILE A CB  1 
ATOM   1346 C  CG1 . ILE A 1 166 ? -8.579  -2.635  -1.004  1.00 14.96 ? 167 ILE A CG1 1 
ATOM   1347 C  CG2 . ILE A 1 166 ? -8.540  -0.530  -2.437  1.00 16.36 ? 167 ILE A CG2 1 
ATOM   1348 C  CD1 . ILE A 1 166 ? -8.684  -2.134  0.368   1.00 17.64 ? 167 ILE A CD1 1 
ATOM   1349 N  N   . LYS A 1 167 ? -5.716  -4.591  -3.376  1.00 15.41 ? 168 LYS A N   1 
ATOM   1350 C  CA  . LYS A 1 167 ? -4.863  -5.649  -2.975  1.00 13.08 ? 168 LYS A CA  1 
ATOM   1351 C  C   . LYS A 1 167 ? -3.526  -5.298  -2.349  1.00 14.27 ? 168 LYS A C   1 
ATOM   1352 O  O   . LYS A 1 167 ? -3.157  -5.939  -1.390  1.00 12.99 ? 168 LYS A O   1 
ATOM   1353 C  CB  . LYS A 1 167 ? -4.517  -6.569  -4.198  1.00 14.22 ? 168 LYS A CB  1 
ATOM   1354 C  CG  . LYS A 1 167 ? -3.771  -7.750  -3.783  1.00 16.29 ? 168 LYS A CG  1 
ATOM   1355 C  CD  . LYS A 1 167 ? -3.499  -8.640  -5.041  1.00 25.48 ? 168 LYS A CD  1 
ATOM   1356 C  CE  . LYS A 1 167 ? -2.606  -9.774  -4.733  1.00 29.56 ? 168 LYS A CE  1 
ATOM   1357 N  NZ  . LYS A 1 167 ? -3.383  -10.944 -4.245  1.00 36.88 ? 168 LYS A NZ  1 
ATOM   1358 N  N   . THR A 1 168 ? -2.852  -4.261  -2.856  1.00 11.81 ? 169 THR A N   1 
ATOM   1359 C  CA  . THR A 1 168 ? -1.495  -3.940  -2.476  1.00 13.48 ? 169 THR A CA  1 
ATOM   1360 C  C   . THR A 1 168 ? -1.462  -2.549  -1.787  1.00 11.58 ? 169 THR A C   1 
ATOM   1361 O  O   . THR A 1 168 ? -2.359  -1.731  -1.896  1.00 16.52 ? 169 THR A O   1 
ATOM   1362 C  CB  . THR A 1 168 ? -0.588  -3.883  -3.735  1.00 15.35 ? 169 THR A CB  1 
ATOM   1363 O  OG1 . THR A 1 168 ? -1.318  -3.092  -4.716  1.00 17.57 ? 169 THR A OG1 1 
ATOM   1364 C  CG2 . THR A 1 168 ? -0.409  -5.265  -4.197  1.00 18.67 ? 169 THR A CG2 1 
ATOM   1365 N  N   . LYS A 1 169 ? -0.423  -2.392  -1.010  1.00 16.47 ? 170 LYS A N   1 
ATOM   1366 C  CA  . LYS A 1 169 ? -0.134  -1.180  -0.237  1.00 18.55 ? 170 LYS A CA  1 
ATOM   1367 C  C   . LYS A 1 169 ? -0.268  0.108   -1.028  1.00 18.79 ? 170 LYS A C   1 
ATOM   1368 O  O   . LYS A 1 169 ? 0.253   0.164   -2.146  1.00 22.10 ? 170 LYS A O   1 
ATOM   1369 C  CB  . LYS A 1 169 ? 1.231   -1.341  0.343   1.00 18.72 ? 170 LYS A CB  1 
ATOM   1370 C  CG  . LYS A 1 169 ? 1.744   -0.088  1.074   1.00 18.95 ? 170 LYS A CG  1 
ATOM   1371 C  CD  . LYS A 1 169 ? 2.982   -0.486  1.789   1.00 23.35 ? 170 LYS A CD  1 
ATOM   1372 C  CE  . LYS A 1 169 ? 3.398   0.626   2.692   1.00 31.82 ? 170 LYS A CE  1 
ATOM   1373 N  NZ  . LYS A 1 169 ? 4.853   0.911   2.534   1.00 38.23 ? 170 LYS A NZ  1 
ATOM   1374 N  N   . GLY A 1 170 ? -1.018  1.072   -0.541  1.00 19.75 ? 171 GLY A N   1 
ATOM   1375 C  CA  . GLY A 1 170 ? -1.212  2.325   -1.288  1.00 20.47 ? 171 GLY A CA  1 
ATOM   1376 C  C   . GLY A 1 170 ? -2.438  2.416   -2.133  1.00 20.84 ? 171 GLY A C   1 
ATOM   1377 O  O   . GLY A 1 170 ? -2.872  3.544   -2.492  1.00 21.94 ? 171 GLY A O   1 
ATOM   1378 N  N   . LYS A 1 171 ? -3.049  1.269   -2.482  1.00 17.63 ? 172 LYS A N   1 
ATOM   1379 C  CA  . LYS A 1 171 ? -4.297  1.311   -3.188  1.00 19.41 ? 172 LYS A CA  1 
ATOM   1380 C  C   . LYS A 1 171 ? -5.517  1.805   -2.398  1.00 18.11 ? 172 LYS A C   1 
ATOM   1381 O  O   . LYS A 1 171 ? -5.724  1.403   -1.215  1.00 19.19 ? 172 LYS A O   1 
ATOM   1382 C  CB  . LYS A 1 171 ? -4.596  -0.077  -3.809  1.00 18.29 ? 172 LYS A CB  1 
ATOM   1383 C  CG  . LYS A 1 171 ? -3.623  -0.432  -4.926  1.00 21.32 ? 172 LYS A CG  1 
ATOM   1384 C  CD  . LYS A 1 171 ? -4.089  -1.548  -5.960  1.00 24.52 ? 172 LYS A CD  1 
ATOM   1385 C  CE  . LYS A 1 171 ? -5.319  -1.098  -6.832  1.00 26.51 ? 172 LYS A CE  1 
ATOM   1386 N  NZ  . LYS A 1 171 ? -5.834  -2.128  -7.901  1.00 31.14 ? 172 LYS A NZ  1 
ATOM   1387 N  N   . SER A 1 172 ? -6.377  2.566   -3.049  1.00 16.78 ? 173 SER A N   1 
ATOM   1388 C  CA  . SER A 1 172 ? -7.620  2.998   -2.469  1.00 17.13 ? 173 SER A CA  1 
ATOM   1389 C  C   . SER A 1 172 ? -8.726  2.896   -3.462  1.00 17.28 ? 173 SER A C   1 
ATOM   1390 O  O   . SER A 1 172 ? -8.528  2.811   -4.733  1.00 18.65 ? 173 SER A O   1 
ATOM   1391 C  CB  . SER A 1 172 ? -7.551  4.428   -1.907  1.00 19.12 ? 173 SER A CB  1 
ATOM   1392 O  OG  . SER A 1 172 ? -7.372  5.314   -3.015  1.00 19.79 ? 173 SER A OG  1 
ATOM   1393 N  N   . ALA A 1 173 ? -9.904  2.908   -2.943  1.00 18.92 ? 174 ALA A N   1 
ATOM   1394 C  CA  . ALA A 1 173 ? -11.052 2.865   -3.782  1.00 19.31 ? 174 ALA A CA  1 
ATOM   1395 C  C   . ALA A 1 173 ? -12.144 3.661   -3.128  1.00 20.92 ? 174 ALA A C   1 
ATOM   1396 O  O   . ALA A 1 173 ? -12.223 3.781   -1.882  1.00 19.67 ? 174 ALA A O   1 
ATOM   1397 C  CB  . ALA A 1 173 ? -11.424 1.486   -4.059  1.00 19.23 ? 174 ALA A CB  1 
ATOM   1398 N  N   . ASP A 1 174 ? -13.005 4.240   -3.961  1.00 20.51 ? 175 ASP A N   1 
ATOM   1399 C  CA  . ASP A 1 174 ? -14.227 4.861   -3.489  1.00 22.25 ? 175 ASP A CA  1 
ATOM   1400 C  C   . ASP A 1 174 ? -15.027 3.884   -2.693  1.00 21.39 ? 175 ASP A C   1 
ATOM   1401 O  O   . ASP A 1 174 ? -15.177 2.702   -3.056  1.00 20.62 ? 175 ASP A O   1 
ATOM   1402 C  CB  . ASP A 1 174 ? -15.114 5.314   -4.660  1.00 23.54 ? 175 ASP A CB  1 
ATOM   1403 C  CG  . ASP A 1 174 ? -14.440 6.354   -5.477  1.00 31.22 ? 175 ASP A CG  1 
ATOM   1404 O  OD1 . ASP A 1 174 ? -13.770 7.232   -4.882  1.00 35.33 ? 175 ASP A OD1 1 
ATOM   1405 O  OD2 . ASP A 1 174 ? -14.560 6.314   -6.724  1.00 37.47 ? 175 ASP A OD2 1 
ATOM   1406 N  N   . PHE A 1 175 ? -15.522 4.362   -1.559  1.00 17.88 ? 176 PHE A N   1 
ATOM   1407 C  CA  . PHE A 1 175 ? -16.353 3.458   -0.728  1.00 15.26 ? 176 PHE A CA  1 
ATOM   1408 C  C   . PHE A 1 175 ? -17.426 4.197   -0.007  1.00 18.12 ? 176 PHE A C   1 
ATOM   1409 O  O   . PHE A 1 175 ? -17.278 4.519   1.164   1.00 18.82 ? 176 PHE A O   1 
ATOM   1410 C  CB  . PHE A 1 175 ? -15.394 2.585   0.161   1.00 14.66 ? 176 PHE A CB  1 
ATOM   1411 C  CG  . PHE A 1 175 ? -16.016 1.372   0.675   1.00 15.34 ? 176 PHE A CG  1 
ATOM   1412 C  CD1 . PHE A 1 175 ? -16.320 0.293   -0.193  1.00 16.13 ? 176 PHE A CD1 1 
ATOM   1413 C  CD2 . PHE A 1 175 ? -16.299 1.239   2.032   1.00 14.25 ? 176 PHE A CD2 1 
ATOM   1414 C  CE1 . PHE A 1 175 ? -16.914 -0.891  0.309   1.00 16.59 ? 176 PHE A CE1 1 
ATOM   1415 C  CE2 . PHE A 1 175 ? -17.000 0.109   2.576   1.00 14.86 ? 176 PHE A CE2 1 
ATOM   1416 C  CZ  . PHE A 1 175 ? -17.281 -0.993  1.688   1.00 15.52 ? 176 PHE A CZ  1 
ATOM   1417 N  N   . THR A 1 176 ? -18.456 4.590   -0.754  1.00 14.59 ? 177 THR A N   1 
ATOM   1418 C  CA  . THR A 1 176 ? -19.519 5.405   -0.220  1.00 15.41 ? 177 THR A CA  1 
ATOM   1419 C  C   . THR A 1 176 ? -20.694 4.562   0.257   1.00 13.13 ? 177 THR A C   1 
ATOM   1420 O  O   . THR A 1 176 ? -20.853 3.389   -0.228  1.00 15.69 ? 177 THR A O   1 
ATOM   1421 C  CB  . THR A 1 176 ? -19.958 6.447   -1.281  1.00 15.42 ? 177 THR A CB  1 
ATOM   1422 O  OG1 . THR A 1 176 ? -20.408 5.729   -2.445  1.00 17.36 ? 177 THR A OG1 1 
ATOM   1423 C  CG2 . THR A 1 176 ? -18.784 7.354   -1.579  1.00 19.27 ? 177 THR A CG2 1 
ATOM   1424 N  N   . ASN A 1 177 ? -21.536 5.113   1.101   1.00 12.96 ? 178 ASN A N   1 
ATOM   1425 C  CA  . ASN A 1 177 ? -22.786 4.539   1.524   1.00 12.96 ? 178 ASN A CA  1 
ATOM   1426 C  C   . ASN A 1 177 ? -22.657 3.195   2.266   1.00 14.01 ? 178 ASN A C   1 
ATOM   1427 O  O   . ASN A 1 177 ? -23.587 2.444   2.294   1.00 17.08 ? 178 ASN A O   1 
ATOM   1428 C  CB  . ASN A 1 177 ? -23.702 4.337   0.291   1.00 13.11 ? 178 ASN A CB  1 
ATOM   1429 C  CG  . ASN A 1 177 ? -24.035 5.722   -0.409  1.00 16.68 ? 178 ASN A CG  1 
ATOM   1430 O  OD1 . ASN A 1 177 ? -24.737 6.552   0.175   1.00 16.00 ? 178 ASN A OD1 1 
ATOM   1431 N  ND2 . ASN A 1 177 ? -23.319 6.008   -1.501  1.00 14.90 ? 178 ASN A ND2 1 
ATOM   1432 N  N   . PHE A 1 178 ? -21.499 3.011   2.902   1.00 13.82 ? 179 PHE A N   1 
ATOM   1433 C  CA  . PHE A 1 178 ? -21.311 1.800   3.731   1.00 13.99 ? 179 PHE A CA  1 
ATOM   1434 C  C   . PHE A 1 178 ? -21.820 2.081   5.083   1.00 14.41 ? 179 PHE A C   1 
ATOM   1435 O  O   . PHE A 1 178 ? -21.357 3.071   5.692   1.00 14.29 ? 179 PHE A O   1 
ATOM   1436 C  CB  . PHE A 1 178 ? -19.887 1.391   3.835   1.00 13.68 ? 179 PHE A CB  1 
ATOM   1437 C  CG  . PHE A 1 178 ? -19.731 0.125   4.664   1.00 12.61 ? 179 PHE A CG  1 
ATOM   1438 C  CD1 . PHE A 1 178 ? -20.181 -1.102  4.179   1.00 15.63 ? 179 PHE A CD1 1 
ATOM   1439 C  CD2 . PHE A 1 178 ? -19.282 0.217   5.957   1.00 9.20  ? 179 PHE A CD2 1 
ATOM   1440 C  CE1 . PHE A 1 178 ? -20.084 -2.243  4.971   1.00 14.94 ? 179 PHE A CE1 1 
ATOM   1441 C  CE2 . PHE A 1 178 ? -19.221 -0.917  6.750   1.00 12.06 ? 179 PHE A CE2 1 
ATOM   1442 C  CZ  . PHE A 1 178 ? -19.583 -2.119  6.284   1.00 13.41 ? 179 PHE A CZ  1 
ATOM   1443 N  N   . ASP A 1 179 ? -22.638 1.160   5.609   1.00 13.86 ? 180 ASP A N   1 
ATOM   1444 C  CA  . ASP A 1 179 ? -23.280 1.408   6.849   1.00 14.00 ? 180 ASP A CA  1 
ATOM   1445 C  C   . ASP A 1 179 ? -22.643 0.590   7.948   1.00 12.75 ? 180 ASP A C   1 
ATOM   1446 O  O   . ASP A 1 179 ? -22.893 -0.601  8.044   1.00 13.25 ? 180 ASP A O   1 
ATOM   1447 C  CB  . ASP A 1 179 ? -24.751 0.998   6.772   1.00 15.66 ? 180 ASP A CB  1 
ATOM   1448 C  CG  . ASP A 1 179 ? -25.541 1.440   7.964   1.00 16.36 ? 180 ASP A CG  1 
ATOM   1449 O  OD1 . ASP A 1 179 ? -24.987 1.735   9.076   1.00 11.84 ? 180 ASP A OD1 1 
ATOM   1450 O  OD2 . ASP A 1 179 ? -26.798 1.475   7.858   1.00 23.40 ? 180 ASP A OD2 1 
ATOM   1451 N  N   . PRO A 1 180 ? -21.871 1.232   8.839   1.00 10.05 ? 181 PRO A N   1 
ATOM   1452 C  CA  . PRO A 1 180 ? -21.128 0.402   9.866   1.00 11.75 ? 181 PRO A CA  1 
ATOM   1453 C  C   . PRO A 1 180 ? -22.048 -0.243  10.890  1.00 12.23 ? 181 PRO A C   1 
ATOM   1454 O  O   . PRO A 1 180 ? -21.581 -1.186  11.627  1.00 10.06 ? 181 PRO A O   1 
ATOM   1455 C  CB  . PRO A 1 180 ? -20.144 1.399   10.455  1.00 12.00 ? 181 PRO A CB  1 
ATOM   1456 C  CG  . PRO A 1 180 ? -20.800 2.750   10.345  1.00 12.17 ? 181 PRO A CG  1 
ATOM   1457 C  CD  . PRO A 1 180 ? -21.624 2.684   8.995   1.00 11.81 ? 181 PRO A CD  1 
ATOM   1458 N  N   . ARG A 1 181 ? -23.335 0.165   10.966  1.00 11.15 ? 182 ARG A N   1 
ATOM   1459 C  CA  . ARG A 1 181 ? -24.285 -0.539  11.885  1.00 12.19 ? 182 ARG A CA  1 
ATOM   1460 C  C   . ARG A 1 181 ? -24.340 -2.063  11.537  1.00 12.10 ? 182 ARG A C   1 
ATOM   1461 O  O   . ARG A 1 181 ? -24.737 -2.837  12.381  1.00 13.59 ? 182 ARG A O   1 
ATOM   1462 C  CB  . ARG A 1 181 ? -25.690 0.093   11.794  1.00 12.21 ? 182 ARG A CB  1 
ATOM   1463 C  CG  . ARG A 1 181 ? -25.553 1.523   12.376  1.00 14.01 ? 182 ARG A CG  1 
ATOM   1464 C  CD  . ARG A 1 181 ? -26.936 2.282   12.319  1.00 15.76 ? 182 ARG A CD  1 
ATOM   1465 N  NE  . ARG A 1 181 ? -27.290 2.418   10.905  1.00 18.50 ? 182 ARG A NE  1 
ATOM   1466 C  CZ  . ARG A 1 181 ? -28.404 2.996   10.475  1.00 24.01 ? 182 ARG A CZ  1 
ATOM   1467 N  NH1 . ARG A 1 181 ? -29.260 3.446   11.360  1.00 20.97 ? 182 ARG A NH1 1 
ATOM   1468 N  NH2 . ARG A 1 181 ? -28.645 3.063   9.168   1.00 20.99 ? 182 ARG A NH2 1 
ATOM   1469 N  N   . GLY A 1 182 ? -24.034 -2.402  10.277  1.00 11.73 ? 183 GLY A N   1 
ATOM   1470 C  CA  . GLY A 1 182 ? -24.151 -3.801  9.820   1.00 12.57 ? 183 GLY A CA  1 
ATOM   1471 C  C   . GLY A 1 182 ? -23.043 -4.686  10.398  1.00 14.36 ? 183 GLY A C   1 
ATOM   1472 O  O   . GLY A 1 182 ? -23.055 -5.917  10.189  1.00 14.20 ? 183 GLY A O   1 
ATOM   1473 N  N   . LEU A 1 183 ? -22.090 -4.054  11.097  1.00 12.09 ? 184 LEU A N   1 
ATOM   1474 C  CA  . LEU A 1 183 ? -20.950 -4.816  11.682  1.00 12.79 ? 184 LEU A CA  1 
ATOM   1475 C  C   . LEU A 1 183 ? -21.116 -5.007  13.162  1.00 12.16 ? 184 LEU A C   1 
ATOM   1476 O  O   . LEU A 1 183 ? -20.157 -5.565  13.767  1.00 13.65 ? 184 LEU A O   1 
ATOM   1477 C  CB  . LEU A 1 183 ? -19.633 -4.048  11.481  1.00 12.78 ? 184 LEU A CB  1 
ATOM   1478 C  CG  . LEU A 1 183 ? -19.270 -3.888  9.979   1.00 13.79 ? 184 LEU A CG  1 
ATOM   1479 C  CD1 . LEU A 1 183 ? -18.030 -3.010  9.737   1.00 14.24 ? 184 LEU A CD1 1 
ATOM   1480 C  CD2 . LEU A 1 183 ? -19.171 -5.245  9.267   1.00 15.43 ? 184 LEU A CD2 1 
ATOM   1481 N  N   . LEU A 1 184 ? -22.206 -4.576  13.791  1.00 10.87 ? 185 LEU A N   1 
ATOM   1482 C  CA  . LEU A 1 184 ? -22.316 -4.568  15.287  1.00 9.95  ? 185 LEU A CA  1 
ATOM   1483 C  C   . LEU A 1 184 ? -23.137 -5.825  15.720  1.00 12.37 ? 185 LEU A C   1 
ATOM   1484 O  O   . LEU A 1 184 ? -24.213 -6.124  15.187  1.00 14.77 ? 185 LEU A O   1 
ATOM   1485 C  CB  . LEU A 1 184 ? -23.137 -3.360  15.853  1.00 9.34  ? 185 LEU A CB  1 
ATOM   1486 C  CG  . LEU A 1 184 ? -22.575 -2.007  15.416  1.00 10.03 ? 185 LEU A CG  1 
ATOM   1487 C  CD1 . LEU A 1 184 ? -23.463 -0.818  15.819  1.00 12.46 ? 185 LEU A CD1 1 
ATOM   1488 C  CD2 . LEU A 1 184 ? -21.121 -1.823  15.897  1.00 12.46 ? 185 LEU A CD2 1 
ATOM   1489 N  N   . PRO A 1 185 ? -22.739 -6.441  16.813  1.00 11.63 ? 186 PRO A N   1 
ATOM   1490 C  CA  . PRO A 1 185 ? -23.489 -7.532  17.358  1.00 11.26 ? 186 PRO A CA  1 
ATOM   1491 C  C   . PRO A 1 185 ? -24.762 -6.994  18.014  1.00 11.97 ? 186 PRO A C   1 
ATOM   1492 O  O   . PRO A 1 185 ? -24.930 -5.777  18.157  1.00 13.19 ? 186 PRO A O   1 
ATOM   1493 C  CB  . PRO A 1 185 ? -22.527 -8.135  18.411  1.00 11.42 ? 186 PRO A CB  1 
ATOM   1494 C  CG  . PRO A 1 185 ? -21.829 -6.942  18.978  1.00 9.28  ? 186 PRO A CG  1 
ATOM   1495 C  CD  . PRO A 1 185 ? -21.595 -6.030  17.682  1.00 9.96  ? 186 PRO A CD  1 
ATOM   1496 N  N   . GLU A 1 186 ? -25.616 -7.907  18.516  1.00 13.72 ? 187 GLU A N   1 
ATOM   1497 C  CA  . GLU A 1 186 ? -26.853 -7.463  19.105  1.00 14.12 ? 187 GLU A CA  1 
ATOM   1498 C  C   . GLU A 1 186 ? -26.594 -6.723  20.441  1.00 13.36 ? 187 GLU A C   1 
ATOM   1499 O  O   . GLU A 1 186 ? -27.190 -5.674  20.705  1.00 14.21 ? 187 GLU A O   1 
ATOM   1500 C  CB  . GLU A 1 186 ? -27.709 -8.745  19.228  1.00 14.92 ? 187 GLU A CB  1 
ATOM   1501 C  CG  . GLU A 1 186 ? -28.569 -8.716  20.344  1.00 19.95 ? 187 GLU A CG  1 
ATOM   1502 C  CD  . GLU A 1 186 ? -29.369 -10.070 20.565  1.00 19.75 ? 187 GLU A CD  1 
ATOM   1503 O  OE1 . GLU A 1 186 ? -29.307 -10.978 19.701  1.00 20.67 ? 187 GLU A OE1 1 
ATOM   1504 O  OE2 . GLU A 1 186 ? -30.076 -10.079 21.632  1.00 26.82 ? 187 GLU A OE2 1 
ATOM   1505 N  N   . SER A 1 187 ? -25.721 -7.257  21.316  1.00 11.52 ? 188 SER A N   1 
ATOM   1506 C  CA  . SER A 1 187 ? -25.547 -6.678  22.589  1.00 11.26 ? 188 SER A CA  1 
ATOM   1507 C  C   . SER A 1 187 ? -24.419 -5.624  22.552  1.00 12.62 ? 188 SER A C   1 
ATOM   1508 O  O   . SER A 1 187 ? -23.407 -5.887  21.909  1.00 13.15 ? 188 SER A O   1 
ATOM   1509 C  CB  . SER A 1 187 ? -25.129 -7.730  23.613  1.00 12.81 ? 188 SER A CB  1 
ATOM   1510 O  OG  . SER A 1 187 ? -24.937 -7.100  24.843  1.00 14.03 ? 188 SER A OG  1 
ATOM   1511 N  N   . LEU A 1 188 ? -24.596 -4.518  23.278  1.00 11.16 ? 189 LEU A N   1 
ATOM   1512 C  CA  . LEU A 1 188 ? -23.479 -3.508  23.470  1.00 12.10 ? 189 LEU A CA  1 
ATOM   1513 C  C   . LEU A 1 188 ? -22.851 -3.641  24.863  1.00 10.59 ? 189 LEU A C   1 
ATOM   1514 O  O   . LEU A 1 188 ? -22.189 -2.684  25.326  1.00 13.05 ? 189 LEU A O   1 
ATOM   1515 C  CB  . LEU A 1 188 ? -23.979 -2.079  23.191  1.00 11.69 ? 189 LEU A CB  1 
ATOM   1516 C  CG  . LEU A 1 188 ? -24.427 -1.857  21.737  1.00 12.90 ? 189 LEU A CG  1 
ATOM   1517 C  CD1 . LEU A 1 188 ? -25.001 -0.447  21.600  1.00 17.32 ? 189 LEU A CD1 1 
ATOM   1518 C  CD2 . LEU A 1 188 ? -23.348 -2.049  20.670  1.00 14.04 ? 189 LEU A CD2 1 
ATOM   1519 N  N   . ASP A 1 189 ? -23.016 -4.788  25.537  1.00 11.32 ? 190 ASP A N   1 
ATOM   1520 C  CA  . ASP A 1 189 ? -22.265 -5.045  26.795  1.00 11.02 ? 190 ASP A CA  1 
ATOM   1521 C  C   . ASP A 1 189 ? -20.775 -4.996  26.470  1.00 10.73 ? 190 ASP A C   1 
ATOM   1522 O  O   . ASP A 1 189 ? -20.332 -5.488  25.456  1.00 10.81 ? 190 ASP A O   1 
ATOM   1523 C  CB  . ASP A 1 189 ? -22.603 -6.391  27.400  1.00 13.25 ? 190 ASP A CB  1 
ATOM   1524 C  CG  . ASP A 1 189 ? -24.009 -6.397  28.066  1.00 16.78 ? 190 ASP A CG  1 
ATOM   1525 O  OD1 . ASP A 1 189 ? -24.557 -5.334  28.314  1.00 20.35 ? 190 ASP A OD1 1 
ATOM   1526 O  OD2 . ASP A 1 189 ? -24.482 -7.494  28.288  1.00 23.78 ? 190 ASP A OD2 1 
ATOM   1527 N  N   . TYR A 1 190 ? -20.037 -4.328  27.360  1.00 8.19  ? 191 TYR A N   1 
ATOM   1528 C  CA  . TYR A 1 190 ? -18.625 -4.115  27.015  1.00 8.76  ? 191 TYR A CA  1 
ATOM   1529 C  C   . TYR A 1 190 ? -17.701 -4.239  28.253  1.00 8.90  ? 191 TYR A C   1 
ATOM   1530 O  O   . TYR A 1 190 ? -18.159 -4.066  29.399  1.00 9.01  ? 191 TYR A O   1 
ATOM   1531 C  CB  . TYR A 1 190 ? -18.440 -2.703  26.346  1.00 10.68 ? 191 TYR A CB  1 
ATOM   1532 C  CG  . TYR A 1 190 ? -18.866 -1.570  27.266  1.00 8.84  ? 191 TYR A CG  1 
ATOM   1533 C  CD1 . TYR A 1 190 ? -17.924 -0.991  28.172  1.00 7.99  ? 191 TYR A CD1 1 
ATOM   1534 C  CD2 . TYR A 1 190 ? -20.157 -1.052  27.194  1.00 10.88 ? 191 TYR A CD2 1 
ATOM   1535 C  CE1 . TYR A 1 190 ? -18.299 0.034   29.063  1.00 9.71  ? 191 TYR A CE1 1 
ATOM   1536 C  CE2 . TYR A 1 190 ? -20.544 0.004   28.019  1.00 12.18 ? 191 TYR A CE2 1 
ATOM   1537 C  CZ  . TYR A 1 190 ? -19.604 0.563   28.946  1.00 11.04 ? 191 TYR A CZ  1 
ATOM   1538 O  OH  . TYR A 1 190 ? -20.036 1.563   29.738  1.00 12.71 ? 191 TYR A OH  1 
ATOM   1539 N  N   . TRP A 1 191 ? -16.397 -4.393  27.981  1.00 7.36  ? 192 TRP A N   1 
ATOM   1540 C  CA  . TRP A 1 191 ? -15.333 -4.097  28.937  1.00 6.58  ? 192 TRP A CA  1 
ATOM   1541 C  C   . TRP A 1 191 ? -14.584 -2.841  28.512  1.00 7.60  ? 192 TRP A C   1 
ATOM   1542 O  O   . TRP A 1 191 ? -14.658 -2.415  27.364  1.00 7.51  ? 192 TRP A O   1 
ATOM   1543 C  CB  . TRP A 1 191 ? -14.265 -5.195  28.840  1.00 7.37  ? 192 TRP A CB  1 
ATOM   1544 C  CG  . TRP A 1 191 ? -14.732 -6.580  29.265  1.00 7.27  ? 192 TRP A CG  1 
ATOM   1545 C  CD1 . TRP A 1 191 ? -14.976 -7.048  30.564  1.00 7.93  ? 192 TRP A CD1 1 
ATOM   1546 C  CD2 . TRP A 1 191 ? -14.987 -7.678  28.396  1.00 9.40  ? 192 TRP A CD2 1 
ATOM   1547 N  NE1 . TRP A 1 191 ? -15.368 -8.358  30.520  1.00 11.03 ? 192 TRP A NE1 1 
ATOM   1548 C  CE2 . TRP A 1 191 ? -15.406 -8.772  29.220  1.00 10.69 ? 192 TRP A CE2 1 
ATOM   1549 C  CE3 . TRP A 1 191 ? -14.930 -7.854  27.027  1.00 11.86 ? 192 TRP A CE3 1 
ATOM   1550 C  CZ2 . TRP A 1 191 ? -15.699 -10.039 28.673  1.00 7.63  ? 192 TRP A CZ2 1 
ATOM   1551 C  CZ3 . TRP A 1 191 ? -15.209 -9.092  26.517  1.00 10.46 ? 192 TRP A CZ3 1 
ATOM   1552 C  CH2 . TRP A 1 191 ? -15.602 -10.173 27.353  1.00 10.85 ? 192 TRP A CH2 1 
ATOM   1553 N  N   . THR A 1 192 ? -14.020 -2.152  29.491  1.00 4.61  ? 193 THR A N   1 
ATOM   1554 C  CA  . THR A 1 192 ? -13.305 -0.911  29.114  1.00 7.11  ? 193 THR A CA  1 
ATOM   1555 C  C   . THR A 1 192 ? -12.110 -0.684  30.037  1.00 8.35  ? 193 THR A C   1 
ATOM   1556 O  O   . THR A 1 192 ? -12.050 -1.132  31.175  1.00 9.49  ? 193 THR A O   1 
ATOM   1557 C  CB  . THR A 1 192 ? -14.269 0.345   29.228  1.00 8.05  ? 193 THR A CB  1 
ATOM   1558 O  OG1 . THR A 1 192 ? -13.577 1.535   28.788  1.00 8.74  ? 193 THR A OG1 1 
ATOM   1559 C  CG2 . THR A 1 192 ? -14.731 0.610   30.725  1.00 8.48  ? 193 THR A CG2 1 
ATOM   1560 N  N   . TYR A 1 193 ? -11.038 -0.115  29.415  1.00 8.72  ? 194 TYR A N   1 
ATOM   1561 C  CA  . TYR A 1 193 ? -9.786  0.155   30.138  1.00 7.42  ? 194 TYR A CA  1 
ATOM   1562 C  C   . TYR A 1 193 ? -8.993  1.168   29.369  1.00 8.65  ? 194 TYR A C   1 
ATOM   1563 O  O   . TYR A 1 193 ? -9.292  1.364   28.197  1.00 6.62  ? 194 TYR A O   1 
ATOM   1564 C  CB  . TYR A 1 193 ? -8.970  -1.126  30.339  1.00 6.78  ? 194 TYR A CB  1 
ATOM   1565 C  CG  . TYR A 1 193 ? -8.267  -1.592  29.071  1.00 7.35  ? 194 TYR A CG  1 
ATOM   1566 C  CD1 . TYR A 1 193 ? -8.980  -2.332  28.029  1.00 7.16  ? 194 TYR A CD1 1 
ATOM   1567 C  CD2 . TYR A 1 193 ? -6.910  -1.266  28.885  1.00 8.30  ? 194 TYR A CD2 1 
ATOM   1568 C  CE1 . TYR A 1 193 ? -8.304  -2.705  26.882  1.00 6.07  ? 194 TYR A CE1 1 
ATOM   1569 C  CE2 . TYR A 1 193 ? -6.208  -1.581  27.681  1.00 9.13  ? 194 TYR A CE2 1 
ATOM   1570 C  CZ  . TYR A 1 193 ? -6.926  -2.283  26.701  1.00 7.27  ? 194 TYR A CZ  1 
ATOM   1571 O  OH  . TYR A 1 193 ? -6.285  -2.643  25.578  1.00 7.22  ? 194 TYR A OH  1 
ATOM   1572 N  N   . PRO A 1 194 ? -8.105  1.874   30.059  1.00 6.60  ? 195 PRO A N   1 
ATOM   1573 C  CA  . PRO A 1 194 ? -7.230  2.854   29.327  1.00 6.41  ? 195 PRO A CA  1 
ATOM   1574 C  C   . PRO A 1 194 ? -6.033  2.212   28.704  1.00 7.70  ? 195 PRO A C   1 
ATOM   1575 O  O   . PRO A 1 194 ? -5.358  1.464   29.376  1.00 7.53  ? 195 PRO A O   1 
ATOM   1576 C  CB  . PRO A 1 194 ? -6.719  3.810   30.479  1.00 8.86  ? 195 PRO A CB  1 
ATOM   1577 C  CG  . PRO A 1 194 ? -6.817  2.953   31.739  1.00 8.99  ? 195 PRO A CG  1 
ATOM   1578 C  CD  . PRO A 1 194 ? -7.869  1.846   31.525  1.00 8.77  ? 195 PRO A CD  1 
ATOM   1579 N  N   . GLY A 1 195 ? -5.827  2.512   27.402  1.00 6.43  ? 196 GLY A N   1 
ATOM   1580 C  CA  . GLY A 1 195 ? -4.685  1.843   26.715  1.00 6.60  ? 196 GLY A CA  1 
ATOM   1581 C  C   . GLY A 1 195 ? -4.103  2.715   25.633  1.00 7.20  ? 196 GLY A C   1 
ATOM   1582 O  O   . GLY A 1 195 ? -4.064  3.956   25.743  1.00 6.36  ? 196 GLY A O   1 
ATOM   1583 N  N   . SER A 1 196 ? -3.753  2.044   24.535  1.00 7.30  ? 197 SER A N   1 
ATOM   1584 C  CA  . SER A 1 196 ? -2.957  2.753   23.511  1.00 7.95  ? 197 SER A CA  1 
ATOM   1585 C  C   . SER A 1 196 ? -3.430  2.361   22.101  1.00 5.70  ? 197 SER A C   1 
ATOM   1586 O  O   . SER A 1 196 ? -4.152  1.346   21.945  1.00 5.99  ? 197 SER A O   1 
ATOM   1587 C  CB  . SER A 1 196 ? -1.523  2.307   23.589  1.00 9.92  ? 197 SER A CB  1 
ATOM   1588 O  OG  . SER A 1 196 ? -1.284  0.921   23.215  1.00 6.51  ? 197 SER A OG  1 
ATOM   1589 N  N   . LEU A 1 197 ? -2.854  3.061   21.133  1.00 6.58  ? 198 LEU A N   1 
ATOM   1590 C  CA  . LEU A 1 197 ? -2.944  2.517   19.744  1.00 6.68  ? 198 LEU A CA  1 
ATOM   1591 C  C   . LEU A 1 197 ? -2.147  1.228   19.755  1.00 6.53  ? 198 LEU A C   1 
ATOM   1592 O  O   . LEU A 1 197 ? -1.137  1.048   20.496  1.00 6.91  ? 198 LEU A O   1 
ATOM   1593 C  CB  . LEU A 1 197 ? -2.280  3.506   18.777  1.00 9.24  ? 198 LEU A CB  1 
ATOM   1594 C  CG  . LEU A 1 197 ? -2.939  4.861   18.729  1.00 11.48 ? 198 LEU A CG  1 
ATOM   1595 C  CD1 . LEU A 1 197 ? -2.019  5.728   17.855  1.00 16.01 ? 198 LEU A CD1 1 
ATOM   1596 C  CD2 . LEU A 1 197 ? -4.273  4.782   18.163  1.00 17.33 ? 198 LEU A CD2 1 
ATOM   1597 N  N   . THR A 1 198 ? -2.640  0.251   18.978  1.00 5.17  ? 199 THR A N   1 
ATOM   1598 C  CA  . THR A 1 198 ? -1.925  -1.079  18.919  1.00 4.70  ? 199 THR A CA  1 
ATOM   1599 C  C   . THR A 1 198 ? -0.923  -1.168  17.760  1.00 7.49  ? 199 THR A C   1 
ATOM   1600 O  O   . THR A 1 198 ? -0.300  -2.231  17.623  1.00 9.31  ? 199 THR A O   1 
ATOM   1601 C  CB  . THR A 1 198 ? -2.948  -2.223  18.779  1.00 5.72  ? 199 THR A CB  1 
ATOM   1602 O  OG1 . THR A 1 198 ? -3.567  -2.159  17.524  1.00 6.81  ? 199 THR A OG1 1 
ATOM   1603 C  CG2 . THR A 1 198 ? -3.860  -2.263  20.015  1.00 6.43  ? 199 THR A CG2 1 
ATOM   1604 N  N   . THR A 1 199 ? -0.810  -0.073  16.965  1.00 8.93  ? 200 THR A N   1 
ATOM   1605 C  CA  . THR A 1 199 ? 0.275   0.007   15.959  1.00 9.51  ? 200 THR A CA  1 
ATOM   1606 C  C   . THR A 1 199 ? 1.090   1.264   16.279  1.00 7.79  ? 200 THR A C   1 
ATOM   1607 O  O   . THR A 1 199 ? 0.573   2.252   16.844  1.00 9.10  ? 200 THR A O   1 
ATOM   1608 C  CB  . THR A 1 199 ? -0.247  0.223   14.572  1.00 9.68  ? 200 THR A CB  1 
ATOM   1609 O  OG1 . THR A 1 199 ? -1.182  1.287   14.572  1.00 14.67 ? 200 THR A OG1 1 
ATOM   1610 C  CG2 . THR A 1 199 ? -0.970  -1.069  14.153  1.00 12.09 ? 200 THR A CG2 1 
ATOM   1611 N  N   . PRO A 1 200 ? 2.357   1.246   15.830  1.00 9.17  ? 201 PRO A N   1 
ATOM   1612 C  CA  . PRO A 1 200 ? 3.073   2.501   15.968  1.00 8.01  ? 201 PRO A CA  1 
ATOM   1613 C  C   . PRO A 1 200 ? 2.213   3.643   15.405  1.00 9.57  ? 201 PRO A C   1 
ATOM   1614 O  O   . PRO A 1 200 ? 1.567   3.512   14.318  1.00 11.01 ? 201 PRO A O   1 
ATOM   1615 C  CB  . PRO A 1 200 ? 4.334   2.184   15.102  1.00 7.92  ? 201 PRO A CB  1 
ATOM   1616 C  CG  . PRO A 1 200 ? 4.598   0.801   15.240  1.00 8.97  ? 201 PRO A CG  1 
ATOM   1617 C  CD  . PRO A 1 200 ? 3.171   0.147   15.282  1.00 9.57  ? 201 PRO A CD  1 
ATOM   1618 N  N   . PRO A 1 201 ? 2.258   4.828   16.013  1.00 9.54  ? 202 PRO A N   1 
ATOM   1619 C  CA  . PRO A 1 201 ? 3.158   5.249   17.130  1.00 11.21 ? 202 PRO A CA  1 
ATOM   1620 C  C   . PRO A 1 201 ? 2.831   4.788   18.568  1.00 8.14  ? 202 PRO A C   1 
ATOM   1621 O  O   . PRO A 1 201 ? 3.463   5.219   19.559  1.00 9.56  ? 202 PRO A O   1 
ATOM   1622 C  CB  . PRO A 1 201 ? 3.117   6.785   17.030  1.00 10.61 ? 202 PRO A CB  1 
ATOM   1623 C  CG  . PRO A 1 201 ? 1.694   7.092   16.583  1.00 11.56 ? 202 PRO A CG  1 
ATOM   1624 C  CD  . PRO A 1 201 ? 1.395   5.948   15.541  1.00 8.44  ? 202 PRO A CD  1 
ATOM   1625 N  N   . LEU A 1 202 ? 1.831   3.866   18.692  1.00 7.71  ? 203 LEU A N   1 
ATOM   1626 C  CA  . LEU A 1 202 ? 1.593   3.238   20.031  1.00 6.51  ? 203 LEU A CA  1 
ATOM   1627 C  C   . LEU A 1 202 ? 1.233   4.263   21.153  1.00 5.12  ? 203 LEU A C   1 
ATOM   1628 O  O   . LEU A 1 202 ? 1.368   4.012   22.315  1.00 7.65  ? 203 LEU A O   1 
ATOM   1629 C  CB  . LEU A 1 202 ? 2.801   2.326   20.517  1.00 6.46  ? 203 LEU A CB  1 
ATOM   1630 C  CG  . LEU A 1 202 ? 3.093   1.273   19.419  1.00 7.64  ? 203 LEU A CG  1 
ATOM   1631 C  CD1 . LEU A 1 202 ? 4.366   0.628   19.891  1.00 9.94  ? 203 LEU A CD1 1 
ATOM   1632 C  CD2 . LEU A 1 202 ? 1.955   0.202   19.445  1.00 11.11 ? 203 LEU A CD2 1 
ATOM   1633 N  N   . LEU A 1 203 ? 0.610   5.363   20.718  1.00 6.23  ? 204 LEU A N   1 
ATOM   1634 C  CA  . LEU A 1 203 ? 0.391   6.487   21.679  1.00 7.48  ? 204 LEU A CA  1 
ATOM   1635 C  C   . LEU A 1 203 ? -0.674  6.112   22.677  1.00 7.95  ? 204 LEU A C   1 
ATOM   1636 O  O   . LEU A 1 203 ? -1.673  5.370   22.341  1.00 7.08  ? 204 LEU A O   1 
ATOM   1637 C  CB  . LEU A 1 203 ? -0.105  7.723   20.896  1.00 8.54  ? 204 LEU A CB  1 
ATOM   1638 C  CG  . LEU A 1 203 ? 0.981   8.299   19.950  1.00 11.67 ? 204 LEU A CG  1 
ATOM   1639 C  CD1 . LEU A 1 203 ? 0.394   9.399   19.031  1.00 14.93 ? 204 LEU A CD1 1 
ATOM   1640 C  CD2 . LEU A 1 203 ? 2.129   8.808   20.792  1.00 13.63 ? 204 LEU A CD2 1 
ATOM   1641 N  N   . GLU A 1 204 ? -0.461  6.564   23.907  1.00 8.06  ? 205 GLU A N   1 
ATOM   1642 C  CA  . GLU A 1 204 ? -1.295  6.155   24.993  1.00 7.60  ? 205 GLU A CA  1 
ATOM   1643 C  C   . GLU A 1 204 ? -2.488  7.124   25.105  1.00 8.23  ? 205 GLU A C   1 
ATOM   1644 O  O   . GLU A 1 204 ? -2.564  7.894   26.096  1.00 9.24  ? 205 GLU A O   1 
ATOM   1645 C  CB  . GLU A 1 204 ? -0.462  6.035   26.308  1.00 10.07 ? 205 GLU A CB  1 
ATOM   1646 C  CG  . GLU A 1 204 ? 0.439   4.737   26.139  1.00 8.52  ? 205 GLU A CG  1 
ATOM   1647 C  CD  . GLU A 1 204 ? 1.423   4.497   27.260  1.00 12.27 ? 205 GLU A CD  1 
ATOM   1648 O  OE1 . GLU A 1 204 ? 1.714   5.479   28.007  1.00 12.26 ? 205 GLU A OE1 1 
ATOM   1649 O  OE2 . GLU A 1 204 ? 1.772   3.335   27.407  1.00 10.93 ? 205 GLU A OE2 1 
ATOM   1650 N  N   . CYS A 1 205 ? -3.384  7.009   24.114  1.00 7.51  ? 206 CYS A N   1 
ATOM   1651 C  CA  . CYS A 1 205 ? -4.464  8.057   23.973  1.00 6.35  ? 206 CYS A CA  1 
ATOM   1652 C  C   . CYS A 1 205 ? -5.819  7.400   23.845  1.00 8.16  ? 206 CYS A C   1 
ATOM   1653 O  O   . CYS A 1 205 ? -6.748  8.112   23.520  1.00 8.05  ? 206 CYS A O   1 
ATOM   1654 C  CB  . CYS A 1 205 ? -4.207  8.869   22.749  1.00 7.37  ? 206 CYS A CB  1 
ATOM   1655 S  SG  . CYS A 1 205 ? -4.106  7.853   21.244  1.00 9.09  ? 206 CYS A SG  1 
ATOM   1656 N  N   . VAL A 1 206 ? -5.939  6.101   24.147  1.00 6.29  ? 207 VAL A N   1 
ATOM   1657 C  CA  . VAL A 1 206 ? -7.180  5.368   23.771  1.00 6.60  ? 207 VAL A CA  1 
ATOM   1658 C  C   . VAL A 1 206 ? -7.966  4.943   25.013  1.00 6.28  ? 207 VAL A C   1 
ATOM   1659 O  O   . VAL A 1 206 ? -7.387  4.304   25.894  1.00 7.53  ? 207 VAL A O   1 
ATOM   1660 C  CB  . VAL A 1 206 ? -6.830  4.108   23.029  1.00 5.83  ? 207 VAL A CB  1 
ATOM   1661 C  CG1 . VAL A 1 206 ? -8.155  3.383   22.648  1.00 5.76  ? 207 VAL A CG1 1 
ATOM   1662 C  CG2 . VAL A 1 206 ? -6.128  4.406   21.686  1.00 8.25  ? 207 VAL A CG2 1 
ATOM   1663 N  N   . THR A 1 207 ? -9.281  5.248   25.084  1.00 6.11  ? 208 THR A N   1 
ATOM   1664 C  CA  . THR A 1 207 ? -10.182 4.522   25.946  1.00 6.55  ? 208 THR A CA  1 
ATOM   1665 C  C   . THR A 1 207 ? -10.683 3.370   25.145  1.00 7.20  ? 208 THR A C   1 
ATOM   1666 O  O   . THR A 1 207 ? -11.377 3.577   24.122  1.00 7.37  ? 208 THR A O   1 
ATOM   1667 C  CB  . THR A 1 207 ? -11.401 5.457   26.379  1.00 8.12  ? 208 THR A CB  1 
ATOM   1668 O  OG1 . THR A 1 207 ? -10.809 6.546   27.187  1.00 6.59  ? 208 THR A OG1 1 
ATOM   1669 C  CG2 . THR A 1 207 ? -12.340 4.682   27.237  1.00 7.71  ? 208 THR A CG2 1 
ATOM   1670 N  N   . TRP A 1 208 ? -10.303 2.177   25.546  1.00 6.50  ? 209 TRP A N   1 
ATOM   1671 C  CA  . TRP A 1 208 ? -10.773 0.980   24.838  1.00 5.94  ? 209 TRP A CA  1 
ATOM   1672 C  C   . TRP A 1 208 ? -12.146 0.562   25.346  1.00 6.73  ? 209 TRP A C   1 
ATOM   1673 O  O   . TRP A 1 208 ? -12.340 0.477   26.564  1.00 8.04  ? 209 TRP A O   1 
ATOM   1674 C  CB  . TRP A 1 208 ? -9.779  -0.246  25.050  1.00 6.04  ? 209 TRP A CB  1 
ATOM   1675 C  CG  . TRP A 1 208 ? -8.670  -0.085  24.104  1.00 5.23  ? 209 TRP A CG  1 
ATOM   1676 C  CD1 . TRP A 1 208 ? -7.390  0.492   24.298  1.00 7.47  ? 209 TRP A CD1 1 
ATOM   1677 C  CD2 . TRP A 1 208 ? -8.708  -0.502  22.746  1.00 5.39  ? 209 TRP A CD2 1 
ATOM   1678 N  NE1 . TRP A 1 208 ? -6.717  0.488   23.125  1.00 6.23  ? 209 TRP A NE1 1 
ATOM   1679 C  CE2 . TRP A 1 208 ? -7.444  -0.151  22.149  1.00 6.04  ? 209 TRP A CE2 1 
ATOM   1680 C  CE3 . TRP A 1 208 ? -9.695  -1.133  21.955  1.00 5.75  ? 209 TRP A CE3 1 
ATOM   1681 C  CZ2 . TRP A 1 208 ? -7.151  -0.359  20.832  1.00 5.39  ? 209 TRP A CZ2 1 
ATOM   1682 C  CZ3 . TRP A 1 208 ? -9.418  -1.397  20.667  1.00 4.31  ? 209 TRP A CZ3 1 
ATOM   1683 C  CH2 . TRP A 1 208 ? -8.153  -1.027  20.024  1.00 6.49  ? 209 TRP A CH2 1 
ATOM   1684 N  N   . ILE A 1 209 ? -13.010 0.241   24.360  1.00 5.60  ? 210 ILE A N   1 
ATOM   1685 C  CA  . ILE A 1 209 ? -14.355 -0.274  24.761  1.00 5.16  ? 210 ILE A CA  1 
ATOM   1686 C  C   . ILE A 1 209 ? -14.446 -1.567  23.905  1.00 8.57  ? 210 ILE A C   1 
ATOM   1687 O  O   . ILE A 1 209 ? -14.587 -1.464  22.699  1.00 6.30  ? 210 ILE A O   1 
ATOM   1688 C  CB  . ILE A 1 209 ? -15.439 0.790   24.374  1.00 7.54  ? 210 ILE A CB  1 
ATOM   1689 C  CG1 . ILE A 1 209 ? -15.168 2.050   25.171  1.00 9.00  ? 210 ILE A CG1 1 
ATOM   1690 C  CG2 . ILE A 1 209 ? -16.863 0.117   24.635  1.00 8.09  ? 210 ILE A CG2 1 
ATOM   1691 C  CD1 . ILE A 1 209 ? -15.966 3.265   24.622  1.00 13.07 ? 210 ILE A CD1 1 
ATOM   1692 N  N   . VAL A 1 210 ? -14.366 -2.736  24.532  1.00 7.64  ? 211 VAL A N   1 
ATOM   1693 C  CA  . VAL A 1 210 ? -14.369 -4.022  23.794  1.00 6.28  ? 211 VAL A CA  1 
ATOM   1694 C  C   . VAL A 1 210 ? -15.679 -4.735  24.043  1.00 6.41  ? 211 VAL A C   1 
ATOM   1695 O  O   . VAL A 1 210 ? -16.005 -4.941  25.204  1.00 6.83  ? 211 VAL A O   1 
ATOM   1696 C  CB  . VAL A 1 210 ? -13.190 -4.892  24.237  1.00 6.70  ? 211 VAL A CB  1 
ATOM   1697 C  CG1 . VAL A 1 210 ? -13.170 -6.256  23.480  1.00 6.63  ? 211 VAL A CG1 1 
ATOM   1698 C  CG2 . VAL A 1 210 ? -11.859 -4.073  23.946  1.00 6.24  ? 211 VAL A CG2 1 
ATOM   1699 N  N   . LEU A 1 211 ? -16.446 -4.951  22.972  1.00 6.40  ? 212 LEU A N   1 
ATOM   1700 C  CA  . LEU A 1 211 ? -17.732 -5.646  23.169  1.00 6.69  ? 212 LEU A CA  1 
ATOM   1701 C  C   . LEU A 1 211 ? -17.558 -7.083  23.568  1.00 6.54  ? 212 LEU A C   1 
ATOM   1702 O  O   . LEU A 1 211 ? -16.683 -7.834  23.053  1.00 7.77  ? 212 LEU A O   1 
ATOM   1703 C  CB  . LEU A 1 211 ? -18.507 -5.580  21.808  1.00 7.08  ? 212 LEU A CB  1 
ATOM   1704 C  CG  . LEU A 1 211 ? -18.901 -4.160  21.393  1.00 8.27  ? 212 LEU A CG  1 
ATOM   1705 C  CD1 . LEU A 1 211 ? -19.960 -4.250  20.185  1.00 11.20 ? 212 LEU A CD1 1 
ATOM   1706 C  CD2 . LEU A 1 211 ? -19.353 -3.257  22.542  1.00 8.29  ? 212 LEU A CD2 1 
ATOM   1707 N  N   A LYS A 1 212 ? -18.468 -7.493  24.460  0.50 9.06  ? 213 LYS A N   1 
ATOM   1708 N  N   B LYS A 1 212 ? -18.399 -7.569  24.499  0.50 9.48  ? 213 LYS A N   1 
ATOM   1709 C  CA  A LYS A 1 212 ? -18.445 -8.867  24.985  0.50 9.76  ? 213 LYS A CA  1 
ATOM   1710 C  CA  B LYS A 1 212 ? -18.263 -9.014  24.895  0.50 8.27  ? 213 LYS A CA  1 
ATOM   1711 C  C   A LYS A 1 212 ? -18.862 -9.898  23.918  0.50 9.04  ? 213 LYS A C   1 
ATOM   1712 C  C   B LYS A 1 212 ? -18.800 -9.953  23.810  0.50 8.39  ? 213 LYS A C   1 
ATOM   1713 O  O   A LYS A 1 212 ? -18.330 -11.008 23.843  0.50 9.75  ? 213 LYS A O   1 
ATOM   1714 O  O   B LYS A 1 212 ? -18.313 -11.068 23.632  0.50 8.05  ? 213 LYS A O   1 
ATOM   1715 C  CB  A LYS A 1 212 ? -19.419 -8.898  26.204  0.50 10.39 ? 213 LYS A CB  1 
ATOM   1716 C  CB  B LYS A 1 212 ? -19.009 -9.312  26.240  0.50 10.34 ? 213 LYS A CB  1 
ATOM   1717 C  CG  A LYS A 1 212 ? -19.905 -10.293 26.673  0.50 12.40 ? 213 LYS A CG  1 
ATOM   1718 C  CG  B LYS A 1 212 ? -19.256 -10.847 26.598  0.50 11.14 ? 213 LYS A CG  1 
ATOM   1719 C  CD  A LYS A 1 212 ? -21.168 -10.182 27.529  0.50 13.73 ? 213 LYS A CD  1 
ATOM   1720 C  CD  B LYS A 1 212 ? -19.854 -11.095 27.980  0.50 11.06 ? 213 LYS A CD  1 
ATOM   1721 C  CE  A LYS A 1 212 ? -22.484 -9.984  26.731  0.50 15.69 ? 213 LYS A CE  1 
ATOM   1722 C  CE  B LYS A 1 212 ? -20.030 -12.587 28.321  0.50 15.98 ? 213 LYS A CE  1 
ATOM   1723 N  NZ  A LYS A 1 212 ? -22.537 -9.616  25.238  0.50 10.35 ? 213 LYS A NZ  1 
ATOM   1724 N  NZ  B LYS A 1 212 ? -20.156 -12.905 29.773  0.50 21.39 ? 213 LYS A NZ  1 
ATOM   1725 N  N   . GLU A 1 213 ? -19.803 -9.503  23.071  1.00 8.73  ? 214 GLU A N   1 
ATOM   1726 C  CA  . GLU A 1 213 ? -20.379 -10.402 22.087  1.00 10.82 ? 214 GLU A CA  1 
ATOM   1727 C  C   . GLU A 1 213 ? -19.608 -10.300 20.753  1.00 7.59  ? 214 GLU A C   1 
ATOM   1728 O  O   . GLU A 1 213 ? -19.610 -9.223  20.129  1.00 8.43  ? 214 GLU A O   1 
ATOM   1729 C  CB  . GLU A 1 213 ? -21.833 -10.055 21.871  1.00 9.54  ? 214 GLU A CB  1 
ATOM   1730 C  CG  . GLU A 1 213 ? -22.499 -11.087 20.856  1.00 11.14 ? 214 GLU A CG  1 
ATOM   1731 C  CD  . GLU A 1 213 ? -24.001 -10.907 20.604  1.00 16.30 ? 214 GLU A CD  1 
ATOM   1732 O  OE1 . GLU A 1 213 ? -24.617 -10.027 21.193  1.00 13.17 ? 214 GLU A OE1 1 
ATOM   1733 O  OE2 . GLU A 1 213 ? -24.543 -11.751 19.824  1.00 23.73 ? 214 GLU A OE2 1 
ATOM   1734 N  N   . PRO A 1 214 ? -19.035 -11.389 20.267  1.00 9.91  ? 215 PRO A N   1 
ATOM   1735 C  CA  . PRO A 1 214 ? -18.410 -11.365 18.947  1.00 9.09  ? 215 PRO A CA  1 
ATOM   1736 C  C   . PRO A 1 214 ? -19.438 -11.373 17.834  1.00 9.57  ? 215 PRO A C   1 
ATOM   1737 O  O   . PRO A 1 214 ? -20.636 -11.724 18.050  1.00 11.63 ? 215 PRO A O   1 
ATOM   1738 C  CB  . PRO A 1 214 ? -17.633 -12.699 18.838  1.00 9.79  ? 215 PRO A CB  1 
ATOM   1739 C  CG  . PRO A 1 214 ? -18.168 -13.546 19.903  1.00 16.27 ? 215 PRO A CG  1 
ATOM   1740 C  CD  . PRO A 1 214 ? -18.992 -12.716 20.919  1.00 10.07 ? 215 PRO A CD  1 
ATOM   1741 N  N   . ILE A 1 215 ? -19.014 -10.965 16.667  1.00 7.29  ? 216 ILE A N   1 
ATOM   1742 C  CA  . ILE A 1 215 ? -19.879 -11.200 15.479  1.00 8.70  ? 216 ILE A CA  1 
ATOM   1743 C  C   . ILE A 1 215 ? -19.368 -12.374 14.772  1.00 9.74  ? 216 ILE A C   1 
ATOM   1744 O  O   . ILE A 1 215 ? -18.164 -12.727 14.867  1.00 10.22 ? 216 ILE A O   1 
ATOM   1745 C  CB  . ILE A 1 215 ? -19.900 -9.960  14.485  1.00 9.53  ? 216 ILE A CB  1 
ATOM   1746 C  CG1 . ILE A 1 215 ? -18.475 -9.539  14.047  1.00 7.94  ? 216 ILE A CG1 1 
ATOM   1747 C  CG2 . ILE A 1 215 ? -20.644 -8.736  15.184  1.00 10.29 ? 216 ILE A CG2 1 
ATOM   1748 C  CD1 . ILE A 1 215 ? -18.485 -8.548  12.757  1.00 7.16  ? 216 ILE A CD1 1 
ATOM   1749 N  N   A SER A 1 216 ? -20.230 -13.045 14.013  0.50 9.76  ? 217 SER A N   1 
ATOM   1750 N  N   B SER A 1 216 ? -20.268 -13.042 14.026  0.50 9.25  ? 217 SER A N   1 
ATOM   1751 C  CA  A SER A 1 216 ? -19.670 -14.185 13.277  0.50 9.74  ? 217 SER A CA  1 
ATOM   1752 C  CA  B SER A 1 216 ? -19.803 -14.189 13.203  0.50 9.11  ? 217 SER A CA  1 
ATOM   1753 C  C   A SER A 1 216 ? -19.593 -13.797 11.826  0.50 10.08 ? 217 SER A C   1 
ATOM   1754 C  C   B SER A 1 216 ? -19.593 -13.745 11.766  0.50 9.63  ? 217 SER A C   1 
ATOM   1755 O  O   A SER A 1 216 ? -20.490 -13.110 11.313  0.50 11.46 ? 217 SER A O   1 
ATOM   1756 O  O   B SER A 1 216 ? -20.386 -12.971 11.193  0.50 11.11 ? 217 SER A O   1 
ATOM   1757 C  CB  A SER A 1 216 ? -20.545 -15.403 13.450  0.50 11.39 ? 217 SER A CB  1 
ATOM   1758 C  CB  B SER A 1 216 ? -20.799 -15.379 13.244  0.50 10.21 ? 217 SER A CB  1 
ATOM   1759 O  OG  A SER A 1 216 ? -21.811 -15.121 12.919  0.50 13.24 ? 217 SER A OG  1 
ATOM   1760 O  OG  B SER A 1 216 ? -20.888 -15.936 14.557  0.50 9.79  ? 217 SER A OG  1 
ATOM   1761 N  N   . VAL A 1 217 ? -18.510 -14.247 11.188  1.00 10.48 ? 218 VAL A N   1 
ATOM   1762 C  CA  . VAL A 1 217 ? -18.283 -14.070 9.805   1.00 7.80  ? 218 VAL A CA  1 
ATOM   1763 C  C   . VAL A 1 217 ? -17.957 -15.375 9.145   1.00 8.32  ? 218 VAL A C   1 
ATOM   1764 O  O   . VAL A 1 217 ? -17.541 -16.348 9.844   1.00 9.38  ? 218 VAL A O   1 
ATOM   1765 C  CB  . VAL A 1 217 ? -17.069 -13.072 9.599   1.00 9.38  ? 218 VAL A CB  1 
ATOM   1766 C  CG1 . VAL A 1 217 ? -17.353 -11.697 10.226  1.00 9.92  ? 218 VAL A CG1 1 
ATOM   1767 C  CG2 . VAL A 1 217 ? -15.651 -13.676 10.047  1.00 10.88 ? 218 VAL A CG2 1 
ATOM   1768 N  N   . SER A 1 218 ? -18.096 -15.506 7.842   1.00 8.93  ? 219 SER A N   1 
ATOM   1769 C  CA  . SER A 1 218 ? -17.849 -16.857 7.270   1.00 10.81 ? 219 SER A CA  1 
ATOM   1770 C  C   . SER A 1 218 ? -16.403 -17.098 6.974   1.00 9.76  ? 219 SER A C   1 
ATOM   1771 O  O   . SER A 1 218 ? -15.598 -16.154 6.854   1.00 9.40  ? 219 SER A O   1 
ATOM   1772 C  CB  . SER A 1 218 ? -18.673 -17.037 5.995   1.00 11.47 ? 219 SER A CB  1 
ATOM   1773 O  OG  . SER A 1 218 ? -18.180 -16.167 5.016   1.00 13.31 ? 219 SER A OG  1 
ATOM   1774 N  N   . SER A 1 219 ? -16.034 -18.380 6.842   1.00 11.16 ? 220 SER A N   1 
ATOM   1775 C  CA  . SER A 1 219 ? -14.712 -18.680 6.439   1.00 13.55 ? 220 SER A CA  1 
ATOM   1776 C  C   . SER A 1 219 ? -14.409 -18.027 5.092   1.00 12.79 ? 220 SER A C   1 
ATOM   1777 O  O   . SER A 1 219 ? -13.278 -17.519 4.948   1.00 11.43 ? 220 SER A O   1 
ATOM   1778 C  CB  . SER A 1 219 ? -14.591 -20.216 6.413   1.00 14.97 ? 220 SER A CB  1 
ATOM   1779 O  OG  . SER A 1 219 ? -15.596 -20.717 5.554   1.00 16.64 ? 220 SER A OG  1 
ATOM   1780 N  N   . GLU A 1 220 ? -15.400 -17.941 4.138   1.00 12.49 ? 221 GLU A N   1 
ATOM   1781 C  CA  . GLU A 1 220 ? -15.159 -17.311 2.822   1.00 12.43 ? 221 GLU A CA  1 
ATOM   1782 C  C   . GLU A 1 220 ? -14.821 -15.776 3.039   1.00 12.71 ? 221 GLU A C   1 
ATOM   1783 O  O   . GLU A 1 220 ? -13.943 -15.225 2.370   1.00 12.68 ? 221 GLU A O   1 
ATOM   1784 C  CB  . GLU A 1 220 ? -16.353 -17.409 1.958   1.00 15.99 ? 221 GLU A CB  1 
ATOM   1785 C  CG  . GLU A 1 220 ? -16.473 -18.845 1.447   1.00 20.19 ? 221 GLU A CG  1 
ATOM   1786 C  CD  . GLU A 1 220 ? -17.465 -19.605 2.273   1.00 25.21 ? 221 GLU A CD  1 
ATOM   1787 O  OE1 . GLU A 1 220 ? -17.939 -19.131 3.324   1.00 20.82 ? 221 GLU A OE1 1 
ATOM   1788 O  OE2 . GLU A 1 220 ? -17.802 -20.756 1.885   1.00 30.95 ? 221 GLU A OE2 1 
ATOM   1789 N  N   . GLN A 1 221 ? -15.519 -15.135 4.003   1.00 10.96 ? 222 GLN A N   1 
ATOM   1790 C  CA  . GLN A 1 221 ? -15.208 -13.712 4.225   1.00 12.12 ? 222 GLN A CA  1 
ATOM   1791 C  C   . GLN A 1 221 ? -13.779 -13.520 4.733   1.00 12.24 ? 222 GLN A C   1 
ATOM   1792 O  O   . GLN A 1 221 ? -13.049 -12.651 4.213   1.00 11.52 ? 222 GLN A O   1 
ATOM   1793 C  CB  . GLN A 1 221 ? -16.222 -13.146 5.211   1.00 10.85 ? 222 GLN A CB  1 
ATOM   1794 C  CG  . GLN A 1 221 ? -17.599 -13.056 4.518   1.00 12.06 ? 222 GLN A CG  1 
ATOM   1795 C  CD  . GLN A 1 221 ? -18.683 -12.492 5.385   1.00 10.96 ? 222 GLN A CD  1 
ATOM   1796 O  OE1 . GLN A 1 221 ? -18.811 -12.875 6.525   1.00 11.04 ? 222 GLN A OE1 1 
ATOM   1797 N  NE2 . GLN A 1 221 ? -19.516 -11.598 4.810   1.00 10.40 ? 222 GLN A NE2 1 
ATOM   1798 N  N   A VAL A 1 222 ? -13.377 -14.302 5.744   0.50 11.01 ? 223 VAL A N   1 
ATOM   1799 N  N   B VAL A 1 222 ? -13.357 -14.292 5.755   0.50 11.47 ? 223 VAL A N   1 
ATOM   1800 C  CA  A VAL A 1 222 ? -12.044 -14.046 6.334   0.50 10.95 ? 223 VAL A CA  1 
ATOM   1801 C  CA  B VAL A 1 222 ? -11.981 -14.061 6.317   0.50 11.79 ? 223 VAL A CA  1 
ATOM   1802 C  C   A VAL A 1 222 ? -10.879 -14.547 5.412   0.50 11.41 ? 223 VAL A C   1 
ATOM   1803 C  C   B VAL A 1 222 ? -10.889 -14.463 5.298   0.50 11.89 ? 223 VAL A C   1 
ATOM   1804 O  O   A VAL A 1 222 ? -9.756  -14.026 5.426   0.50 12.18 ? 223 VAL A O   1 
ATOM   1805 O  O   B VAL A 1 222 ? -9.848  -13.807 5.115   0.50 11.40 ? 223 VAL A O   1 
ATOM   1806 C  CB  A VAL A 1 222 ? -11.955 -14.624 7.767   0.50 11.99 ? 223 VAL A CB  1 
ATOM   1807 C  CB  B VAL A 1 222 ? -11.775 -14.795 7.683   0.50 13.18 ? 223 VAL A CB  1 
ATOM   1808 C  CG1 A VAL A 1 222 ? -11.916 -16.178 7.702   0.50 10.40 ? 223 VAL A CG1 1 
ATOM   1809 C  CG1 B VAL A 1 222 ? -10.270 -14.619 8.236   0.50 11.83 ? 223 VAL A CG1 1 
ATOM   1810 C  CG2 A VAL A 1 222 ? -10.755 -13.926 8.550   0.50 10.18 ? 223 VAL A CG2 1 
ATOM   1811 C  CG2 B VAL A 1 222 ? -12.785 -14.281 8.671   0.50 13.95 ? 223 VAL A CG2 1 
ATOM   1812 N  N   . LEU A 1 223 ? -11.199 -15.499 4.534   1.00 12.89 ? 224 LEU A N   1 
ATOM   1813 C  CA  . LEU A 1 223 ? -10.252 -15.971 3.533   1.00 15.11 ? 224 LEU A CA  1 
ATOM   1814 C  C   . LEU A 1 223 ? -9.968  -14.838 2.589   1.00 15.19 ? 224 LEU A C   1 
ATOM   1815 O  O   . LEU A 1 223 ? -8.822  -14.738 2.156   1.00 16.90 ? 224 LEU A O   1 
ATOM   1816 C  CB  . LEU A 1 223 ? -10.843 -17.155 2.762   1.00 17.07 ? 224 LEU A CB  1 
ATOM   1817 C  CG  . LEU A 1 223 ? -10.565 -18.473 3.496   1.00 23.89 ? 224 LEU A CG  1 
ATOM   1818 C  CD1 . LEU A 1 223 ? -11.445 -19.622 2.806   1.00 29.58 ? 224 LEU A CD1 1 
ATOM   1819 C  CD2 . LEU A 1 223 ? -9.084  -18.802 3.433   1.00 26.68 ? 224 LEU A CD2 1 
ATOM   1820 N  N   A LYS A 1 224 ? -10.968 -14.005 2.316   0.50 13.55 ? 225 LYS A N   1 
ATOM   1821 N  N   B LYS A 1 224 ? -10.963 -14.006 2.288   0.50 12.80 ? 225 LYS A N   1 
ATOM   1822 C  CA  A LYS A 1 224 ? -10.790 -12.893 1.384   0.50 15.40 ? 225 LYS A CA  1 
ATOM   1823 C  CA  B LYS A 1 224 ? -10.727 -12.880 1.378   0.50 14.37 ? 225 LYS A CA  1 
ATOM   1824 C  C   A LYS A 1 224 ? -9.966  -11.745 2.010   0.50 13.63 ? 225 LYS A C   1 
ATOM   1825 C  C   B LYS A 1 224 ? -9.772  -11.889 2.055   0.50 12.19 ? 225 LYS A C   1 
ATOM   1826 O  O   A LYS A 1 224 ? -9.357  -10.974 1.278   0.50 13.79 ? 225 LYS A O   1 
ATOM   1827 O  O   B LYS A 1 224 ? -8.863  -11.370 1.419   0.50 12.47 ? 225 LYS A O   1 
ATOM   1828 C  CB  A LYS A 1 224 ? -12.147 -12.421 0.785   0.50 14.48 ? 225 LYS A CB  1 
ATOM   1829 C  CB  B LYS A 1 224 ? -12.049 -12.189 0.921   0.50 11.86 ? 225 LYS A CB  1 
ATOM   1830 C  CG  A LYS A 1 224 ? -12.724 -13.481 -0.288  0.50 16.98 ? 225 LYS A CG  1 
ATOM   1831 C  CG  B LYS A 1 224 ? -12.845 -13.050 -0.125  0.50 17.76 ? 225 LYS A CG  1 
ATOM   1832 C  CD  A LYS A 1 224 ? -14.171 -13.199 -0.732  0.50 18.59 ? 225 LYS A CD  1 
ATOM   1833 C  CD  B LYS A 1 224 ? -13.858 -12.197 -0.847  0.50 17.20 ? 225 LYS A CD  1 
ATOM   1834 C  CE  A LYS A 1 224 ? -14.758 -14.377 -1.576  0.50 18.04 ? 225 LYS A CE  1 
ATOM   1835 C  CE  B LYS A 1 224 ? -13.960 -12.553 -2.326  0.50 19.32 ? 225 LYS A CE  1 
ATOM   1836 N  NZ  A LYS A 1 224 ? -15.910 -14.016 -2.494  0.50 22.59 ? 225 LYS A NZ  1 
ATOM   1837 N  NZ  B LYS A 1 224 ? -14.768 -11.516 -2.996  0.50 25.33 ? 225 LYS A NZ  1 
ATOM   1838 N  N   . PHE A 1 225 ? -9.984  -11.599 3.349   1.00 11.12 ? 226 PHE A N   1 
ATOM   1839 C  CA  . PHE A 1 225 ? -9.007  -10.727 4.039   1.00 10.48 ? 226 PHE A CA  1 
ATOM   1840 C  C   . PHE A 1 225 ? -7.576  -11.191 3.802   1.00 11.33 ? 226 PHE A C   1 
ATOM   1841 O  O   . PHE A 1 225 ? -6.653  -10.370 3.532   1.00 11.42 ? 226 PHE A O   1 
ATOM   1842 C  CB  . PHE A 1 225 ? -9.194  -10.734 5.605   1.00 9.12  ? 226 PHE A CB  1 
ATOM   1843 C  CG  . PHE A 1 225 ? -10.383 -9.985  6.128   1.00 10.81 ? 226 PHE A CG  1 
ATOM   1844 C  CD1 . PHE A 1 225 ? -11.393 -9.510  5.304   1.00 11.15 ? 226 PHE A CD1 1 
ATOM   1845 C  CD2 . PHE A 1 225 ? -10.484 -9.780  7.490   1.00 12.55 ? 226 PHE A CD2 1 
ATOM   1846 C  CE1 . PHE A 1 225 ? -12.471 -8.828  5.868   1.00 15.45 ? 226 PHE A CE1 1 
ATOM   1847 C  CE2 . PHE A 1 225 ? -11.546 -9.110  8.040   1.00 14.78 ? 226 PHE A CE2 1 
ATOM   1848 C  CZ  . PHE A 1 225 ? -12.542 -8.633  7.238   1.00 13.51 ? 226 PHE A CZ  1 
ATOM   1849 N  N   . ARG A 1 226 ? -7.368  -12.499 3.896   1.00 11.07 ? 227 ARG A N   1 
ATOM   1850 C  CA  . ARG A 1 226 ? -6.041  -13.107 3.762   1.00 11.10 ? 227 ARG A CA  1 
ATOM   1851 C  C   . ARG A 1 226 ? -5.425  -13.081 2.352   1.00 10.63 ? 227 ARG A C   1 
ATOM   1852 O  O   . ARG A 1 226 ? -4.219  -13.448 2.197   1.00 14.35 ? 227 ARG A O   1 
ATOM   1853 C  CB  . ARG A 1 226 ? -6.003  -14.538 4.300   1.00 11.81 ? 227 ARG A CB  1 
ATOM   1854 C  CG  . ARG A 1 226 ? -6.598  -14.679 5.719   1.00 11.18 ? 227 ARG A CG  1 
ATOM   1855 C  CD  . ARG A 1 226 ? -6.513  -16.163 6.132   1.00 13.57 ? 227 ARG A CD  1 
ATOM   1856 N  NE  . ARG A 1 226 ? -7.044  -16.313 7.518   1.00 12.16 ? 227 ARG A NE  1 
ATOM   1857 C  CZ  . ARG A 1 226 ? -7.985  -17.164 7.920   1.00 12.90 ? 227 ARG A CZ  1 
ATOM   1858 N  NH1 . ARG A 1 226 ? -8.406  -18.142 7.086   1.00 15.05 ? 227 ARG A NH1 1 
ATOM   1859 N  NH2 . ARG A 1 226 ? -8.385  -17.156 9.195   1.00 13.23 ? 227 ARG A NH2 1 
ATOM   1860 N  N   . LYS A 1 227 ? -6.211  -12.583 1.408   1.00 13.32 ? 228 LYS A N   1 
ATOM   1861 C  CA  . LYS A 1 227 ? -5.682  -12.458 0.018   1.00 14.58 ? 228 LYS A CA  1 
ATOM   1862 C  C   . LYS A 1 227 ? -5.093  -11.121 -0.225  1.00 15.82 ? 228 LYS A C   1 
ATOM   1863 O  O   . LYS A 1 227 ? -4.420  -10.894 -1.228  1.00 15.03 ? 228 LYS A O   1 
ATOM   1864 C  CB  . LYS A 1 227 ? -6.739  -12.750 -1.004  1.00 14.79 ? 228 LYS A CB  1 
ATOM   1865 C  CG  . LYS A 1 227 ? -7.105  -14.187 -1.007  1.00 17.38 ? 228 LYS A CG  1 
ATOM   1866 C  CD  . LYS A 1 227 ? -8.297  -14.337 -1.873  1.00 22.01 ? 228 LYS A CD  1 
ATOM   1867 C  CE  . LYS A 1 227 ? -8.230  -15.708 -2.535  1.00 32.91 ? 228 LYS A CE  1 
ATOM   1868 N  NZ  . LYS A 1 227 ? -9.631  -16.309 -2.608  1.00 34.56 ? 228 LYS A NZ  1 
ATOM   1869 N  N   . LEU A 1 228 ? -5.268  -10.213 0.747   1.00 13.66 ? 229 LEU A N   1 
ATOM   1870 C  CA  . LEU A 1 228 ? -4.593  -8.918  0.652   1.00 12.79 ? 229 LEU A CA  1 
ATOM   1871 C  C   . LEU A 1 228 ? -3.092  -9.035  0.800   1.00 14.07 ? 229 LEU A C   1 
ATOM   1872 O  O   . LEU A 1 228 ? -2.555  -10.043 1.245   1.00 12.08 ? 229 LEU A O   1 
ATOM   1873 C  CB  . LEU A 1 228 ? -5.127  -7.931  1.733   1.00 10.99 ? 229 LEU A CB  1 
ATOM   1874 C  CG  . LEU A 1 228 ? -6.562  -7.582  1.561   1.00 9.98  ? 229 LEU A CG  1 
ATOM   1875 C  CD1 . LEU A 1 228 ? -6.964  -6.952  2.857   1.00 12.35 ? 229 LEU A CD1 1 
ATOM   1876 C  CD2 . LEU A 1 228 ? -6.579  -6.466  0.511   1.00 12.40 ? 229 LEU A CD2 1 
ATOM   1877 N  N   . ASN A 1 229 ? -2.410  -7.922  0.506   1.00 15.74 ? 230 ASN A N   1 
ATOM   1878 C  CA  . ASN A 1 229 ? -0.975  -7.972  0.449   1.00 14.36 ? 230 ASN A CA  1 
ATOM   1879 C  C   . ASN A 1 229 ? -0.408  -6.816  1.325   1.00 13.42 ? 230 ASN A C   1 
ATOM   1880 O  O   . ASN A 1 229 ? -0.936  -5.711  1.280   1.00 14.06 ? 230 ASN A O   1 
ATOM   1881 C  CB  . ASN A 1 229 ? -0.463  -7.691  -0.989  1.00 14.28 ? 230 ASN A CB  1 
ATOM   1882 C  CG  . ASN A 1 229 ? -0.451  -8.940  -1.914  1.00 17.63 ? 230 ASN A CG  1 
ATOM   1883 O  OD1 . ASN A 1 229 ? 0.111   -8.800  -3.032  1.00 20.23 ? 230 ASN A OD1 1 
ATOM   1884 N  ND2 . ASN A 1 229 ? -1.034  -10.095 -1.500  1.00 18.23 ? 230 ASN A ND2 1 
ATOM   1885 N  N   . PHE A 1 230 ? 0.637   -7.112  2.039   1.00 14.46 ? 231 PHE A N   1 
ATOM   1886 C  CA  . PHE A 1 230 ? 1.320   -5.993  2.760   1.00 15.32 ? 231 PHE A CA  1 
ATOM   1887 C  C   . PHE A 1 230 ? 2.236   -5.196  1.805   1.00 17.76 ? 231 PHE A C   1 
ATOM   1888 O  O   . PHE A 1 230 ? 2.503   -4.023  2.056   1.00 17.94 ? 231 PHE A O   1 
ATOM   1889 C  CB  . PHE A 1 230 ? 2.305   -6.493  3.741   1.00 14.81 ? 231 PHE A CB  1 
ATOM   1890 C  CG  . PHE A 1 230 ? 1.737   -7.126  5.018   1.00 13.10 ? 231 PHE A CG  1 
ATOM   1891 C  CD1 . PHE A 1 230 ? 0.962   -6.384  5.917   1.00 12.19 ? 231 PHE A CD1 1 
ATOM   1892 C  CD2 . PHE A 1 230 ? 2.170   -8.437  5.344   1.00 10.34 ? 231 PHE A CD2 1 
ATOM   1893 C  CE1 . PHE A 1 230 ? 0.507   -6.993  7.177   1.00 14.27 ? 231 PHE A CE1 1 
ATOM   1894 C  CE2 . PHE A 1 230 ? 1.737   -9.102  6.581   1.00 14.95 ? 231 PHE A CE2 1 
ATOM   1895 C  CZ  . PHE A 1 230 ? 0.909   -8.352  7.510   1.00 12.03 ? 231 PHE A CZ  1 
ATOM   1896 N  N   . ASN A 1 231 ? 2.704   -5.869  0.758   1.00 18.04 ? 232 ASN A N   1 
ATOM   1897 C  CA  . ASN A 1 231 ? 3.563   -5.187  -0.262  1.00 17.74 ? 232 ASN A CA  1 
ATOM   1898 C  C   . ASN A 1 231 ? 2.836   -4.229  -1.207  1.00 19.48 ? 232 ASN A C   1 
ATOM   1899 O  O   . ASN A 1 231 ? 1.621   -4.320  -1.343  1.00 17.59 ? 232 ASN A O   1 
ATOM   1900 C  CB  . ASN A 1 231 ? 4.239   -6.276  -1.064  1.00 19.43 ? 232 ASN A CB  1 
ATOM   1901 C  CG  . ASN A 1 231 ? 3.230   -7.199  -1.676  1.00 18.38 ? 232 ASN A CG  1 
ATOM   1902 O  OD1 . ASN A 1 231 ? 2.759   -8.118  -1.026  1.00 22.02 ? 232 ASN A OD1 1 
ATOM   1903 N  ND2 . ASN A 1 231 ? 2.917   -7.005  -2.994  1.00 18.38 ? 232 ASN A ND2 1 
ATOM   1904 N  N   . GLY A 1 232 ? 3.591   -3.355  -1.915  1.00 19.18 ? 233 GLY A N   1 
ATOM   1905 C  CA  . GLY A 1 232 ? 3.011   -2.566  -3.026  1.00 20.02 ? 233 GLY A CA  1 
ATOM   1906 C  C   . GLY A 1 232 ? 3.002   -3.400  -4.295  1.00 20.49 ? 233 GLY A C   1 
ATOM   1907 O  O   . GLY A 1 232 ? 3.686   -4.411  -4.401  1.00 20.44 ? 233 GLY A O   1 
ATOM   1908 N  N   . GLU A 1 233 ? 2.170   -2.990  -5.248  1.00 21.02 ? 234 GLU A N   1 
ATOM   1909 C  CA  . GLU A 1 233 ? 2.144   -3.568  -6.563  1.00 21.44 ? 234 GLU A CA  1 
ATOM   1910 C  C   . GLU A 1 233 ? 3.541   -3.639  -7.177  1.00 22.03 ? 234 GLU A C   1 
ATOM   1911 O  O   . GLU A 1 233 ? 4.339   -2.693  -7.076  1.00 21.83 ? 234 GLU A O   1 
ATOM   1912 C  CB  . GLU A 1 233 ? 1.264   -2.694  -7.444  1.00 21.19 ? 234 GLU A CB  1 
ATOM   1913 C  CG  . GLU A 1 233 ? 0.891   -3.286  -8.772  1.00 21.96 ? 234 GLU A CG  1 
ATOM   1914 C  CD  . GLU A 1 233 ? -0.066  -2.409  -9.557  1.00 31.30 ? 234 GLU A CD  1 
ATOM   1915 O  OE1 . GLU A 1 233 ? -0.372  -1.228  -9.149  1.00 31.43 ? 234 GLU A OE1 1 
ATOM   1916 O  OE2 . GLU A 1 233 ? -0.494  -2.906  -10.627 1.00 33.11 ? 234 GLU A OE2 1 
ATOM   1917 N  N   . GLY A 1 234 ? 3.829   -4.794  -7.771  1.00 22.94 ? 235 GLY A N   1 
ATOM   1918 C  CA  . GLY A 1 234 ? 5.127   -4.985  -8.373  1.00 25.66 ? 235 GLY A CA  1 
ATOM   1919 C  C   . GLY A 1 234 ? 6.250   -5.279  -7.434  1.00 27.20 ? 235 GLY A C   1 
ATOM   1920 O  O   . GLY A 1 234 ? 7.412   -5.291  -7.842  1.00 26.26 ? 235 GLY A O   1 
ATOM   1921 N  N   . GLU A 1 235 ? 5.899   -5.542  -6.173  1.00 28.48 ? 236 GLU A N   1 
ATOM   1922 C  CA  . GLU A 1 235 ? 6.840   -6.029  -5.168  1.00 27.80 ? 236 GLU A CA  1 
ATOM   1923 C  C   . GLU A 1 235 ? 6.453   -7.454  -4.891  1.00 28.62 ? 236 GLU A C   1 
ATOM   1924 O  O   . GLU A 1 235 ? 5.328   -7.886  -5.208  1.00 27.08 ? 236 GLU A O   1 
ATOM   1925 C  CB  . GLU A 1 235 ? 6.758   -5.208  -3.869  1.00 30.39 ? 236 GLU A CB  1 
ATOM   1926 C  CG  . GLU A 1 235 ? 7.492   -3.926  -3.890  1.00 32.38 ? 236 GLU A CG  1 
ATOM   1927 C  CD  . GLU A 1 235 ? 7.009   -2.945  -2.844  1.00 41.04 ? 236 GLU A CD  1 
ATOM   1928 O  OE1 . GLU A 1 235 ? 6.376   -3.365  -1.818  1.00 42.43 ? 236 GLU A OE1 1 
ATOM   1929 O  OE2 . GLU A 1 235 ? 7.252   -1.735  -3.045  1.00 44.21 ? 236 GLU A OE2 1 
ATOM   1930 N  N   . PRO A 1 236 ? 7.384   -8.231  -4.337  1.00 26.43 ? 237 PRO A N   1 
ATOM   1931 C  CA  . PRO A 1 236 ? 7.150   -9.630  -4.089  1.00 26.53 ? 237 PRO A CA  1 
ATOM   1932 C  C   . PRO A 1 236 ? 5.971   -9.799  -3.090  1.00 24.35 ? 237 PRO A C   1 
ATOM   1933 O  O   . PRO A 1 236 ? 5.884   -9.044  -2.134  1.00 22.77 ? 237 PRO A O   1 
ATOM   1934 C  CB  . PRO A 1 236 ? 8.473   -10.086 -3.464  1.00 27.41 ? 237 PRO A CB  1 
ATOM   1935 C  CG  . PRO A 1 236 ? 9.497   -9.095  -3.884  1.00 28.58 ? 237 PRO A CG  1 
ATOM   1936 C  CD  . PRO A 1 236 ? 8.755   -7.796  -3.971  1.00 29.30 ? 237 PRO A CD  1 
ATOM   1937 N  N   . GLU A 1 237 ? 5.154   -10.828 -3.305  1.00 24.21 ? 238 GLU A N   1 
ATOM   1938 C  CA  . GLU A 1 237 ? 3.868   -10.931 -2.625  1.00 21.40 ? 238 GLU A CA  1 
ATOM   1939 C  C   . GLU A 1 237 ? 4.130   -11.371 -1.208  1.00 21.10 ? 238 GLU A C   1 
ATOM   1940 O  O   . GLU A 1 237 ? 4.678   -12.426 -0.986  1.00 18.20 ? 238 GLU A O   1 
ATOM   1941 C  CB  . GLU A 1 237 ? 2.936   -11.944 -3.306  1.00 22.93 ? 238 GLU A CB  1 
ATOM   1942 C  CG  . GLU A 1 237 ? 1.579   -11.966 -2.572  1.00 23.88 ? 238 GLU A CG  1 
ATOM   1943 C  CD  . GLU A 1 237 ? 0.467   -12.694 -3.308  1.00 26.27 ? 238 GLU A CD  1 
ATOM   1944 O  OE1 . GLU A 1 237 ? 0.782   -13.705 -3.993  1.00 29.87 ? 238 GLU A OE1 1 
ATOM   1945 O  OE2 . GLU A 1 237 ? -0.703  -12.248 -3.253  1.00 16.10 ? 238 GLU A OE2 1 
ATOM   1946 N  N   . GLU A 1 238 ? 3.588   -10.586 -0.261  1.00 19.22 ? 239 GLU A N   1 
ATOM   1947 C  CA  . GLU A 1 238 ? 3.638   -10.970 1.137   1.00 19.61 ? 239 GLU A CA  1 
ATOM   1948 C  C   . GLU A 1 238 ? 2.204   -10.897 1.633   1.00 14.95 ? 239 GLU A C   1 
ATOM   1949 O  O   . GLU A 1 238 ? 1.620   -9.804  1.602   1.00 15.53 ? 239 GLU A O   1 
ATOM   1950 C  CB  . GLU A 1 238 ? 4.497   -10.021 1.937   1.00 16.58 ? 239 GLU A CB  1 
ATOM   1951 C  CG  . GLU A 1 238 ? 4.789   -10.532 3.363   1.00 26.26 ? 239 GLU A CG  1 
ATOM   1952 C  CD  . GLU A 1 238 ? 5.010   -12.072 3.620   1.00 37.10 ? 239 GLU A CD  1 
ATOM   1953 O  OE1 . GLU A 1 238 ? 5.029   -12.395 4.837   1.00 38.92 ? 239 GLU A OE1 1 
ATOM   1954 O  OE2 . GLU A 1 238 ? 5.173   -12.942 2.703   1.00 38.77 ? 239 GLU A OE2 1 
ATOM   1955 N  N   . LEU A 1 239 ? 1.587   -12.058 1.963   1.00 15.37 ? 240 LEU A N   1 
ATOM   1956 C  CA  . LEU A 1 239 ? 0.126   -12.014 2.287   1.00 13.57 ? 240 LEU A CA  1 
ATOM   1957 C  C   . LEU A 1 239 ? -0.086  -11.163 3.569   1.00 10.89 ? 240 LEU A C   1 
ATOM   1958 O  O   . LEU A 1 239 ? 0.693   -11.286 4.534   1.00 13.52 ? 240 LEU A O   1 
ATOM   1959 C  CB  . LEU A 1 239 ? -0.370  -13.423 2.558   1.00 12.99 ? 240 LEU A CB  1 
ATOM   1960 C  CG  . LEU A 1 239 ? -0.535  -14.313 1.289   1.00 14.16 ? 240 LEU A CG  1 
ATOM   1961 C  CD1 . LEU A 1 239 ? -1.256  -15.641 1.715   1.00 16.53 ? 240 LEU A CD1 1 
ATOM   1962 C  CD2 . LEU A 1 239 ? -1.329  -13.581 0.201   1.00 15.11 ? 240 LEU A CD2 1 
ATOM   1963 N  N   . MET A 1 240 ? -1.148  -10.378 3.564   1.00 12.15 ? 241 MET A N   1 
ATOM   1964 C  CA  . MET A 1 240 ? -1.480  -9.513  4.709   1.00 11.84 ? 241 MET A CA  1 
ATOM   1965 C  C   . MET A 1 240 ? -2.217  -10.494 5.639   1.00 11.82 ? 241 MET A C   1 
ATOM   1966 O  O   . MET A 1 240 ? -3.441  -10.661 5.539   1.00 11.74 ? 241 MET A O   1 
ATOM   1967 C  CB  . MET A 1 240 ? -2.352  -8.335  4.304   1.00 12.63 ? 241 MET A CB  1 
ATOM   1968 C  CG  . MET A 1 240 ? -2.640  -7.293  5.539   1.00 12.89 ? 241 MET A CG  1 
ATOM   1969 S  SD  . MET A 1 240 ? -3.596  -5.974  5.013   1.00 14.73 ? 241 MET A SD  1 
ATOM   1970 C  CE  . MET A 1 240 ? -2.288  -4.869  4.377   1.00 13.46 ? 241 MET A CE  1 
ATOM   1971 N  N   . VAL A 1 241 ? -1.421  -11.160 6.497   1.00 10.77 ? 242 VAL A N   1 
ATOM   1972 C  CA  . VAL A 1 241 ? -2.023  -12.051 7.540   1.00 10.88 ? 242 VAL A CA  1 
ATOM   1973 C  C   . VAL A 1 241 ? -1.214  -11.783 8.850   1.00 9.72  ? 242 VAL A C   1 
ATOM   1974 O  O   . VAL A 1 241 ? -0.024  -11.379 8.833   1.00 10.71 ? 242 VAL A O   1 
ATOM   1975 C  CB  . VAL A 1 241 ? -1.965  -13.553 7.197   1.00 10.46 ? 242 VAL A CB  1 
ATOM   1976 C  CG1 . VAL A 1 241 ? -2.999  -13.855 5.969   1.00 10.68 ? 242 VAL A CG1 1 
ATOM   1977 C  CG2 . VAL A 1 241 ? -0.481  -14.070 7.040   1.00 12.77 ? 242 VAL A CG2 1 
ATOM   1978 N  N   . ASP A 1 242 ? -1.856  -12.111 9.972   1.00 8.56  ? 243 ASP A N   1 
ATOM   1979 C  CA  . ASP A 1 242 ? -1.157  -11.941 11.281  1.00 7.59  ? 243 ASP A CA  1 
ATOM   1980 C  C   . ASP A 1 242 ? -0.645  -10.521 11.508  1.00 7.62  ? 243 ASP A C   1 
ATOM   1981 O  O   . ASP A 1 242 ? 0.466   -10.291 12.007  1.00 10.19 ? 243 ASP A O   1 
ATOM   1982 C  CB  . ASP A 1 242 ? -0.076  -13.014 11.569  1.00 7.47  ? 243 ASP A CB  1 
ATOM   1983 C  CG  . ASP A 1 242 ? -0.643  -14.418 11.630  1.00 12.44 ? 243 ASP A CG  1 
ATOM   1984 O  OD1 . ASP A 1 242 ? -1.716  -14.613 12.221  1.00 10.21 ? 243 ASP A OD1 1 
ATOM   1985 O  OD2 . ASP A 1 242 ? -0.016  -15.328 10.959  1.00 11.69 ? 243 ASP A OD2 1 
ATOM   1986 N  N   . ASN A 1 243 ? -1.550  -9.604  11.216  1.00 7.94  ? 244 ASN A N   1 
ATOM   1987 C  CA  . ASN A 1 243 ? -1.245  -8.146  11.498  1.00 7.51  ? 244 ASN A CA  1 
ATOM   1988 C  C   . ASN A 1 243 ? -1.845  -7.764  12.849  1.00 9.46  ? 244 ASN A C   1 
ATOM   1989 O  O   . ASN A 1 243 ? -2.562  -6.752  12.893  1.00 9.07  ? 244 ASN A O   1 
ATOM   1990 C  CB  . ASN A 1 243 ? -1.828  -7.267  10.359  1.00 7.72  ? 244 ASN A CB  1 
ATOM   1991 C  CG  . ASN A 1 243 ? -3.377  -7.434  10.136  1.00 10.50 ? 244 ASN A CG  1 
ATOM   1992 O  OD1 . ASN A 1 243 ? -4.035  -8.349  10.702  1.00 8.91  ? 244 ASN A OD1 1 
ATOM   1993 N  ND2 . ASN A 1 243 ? -3.979  -6.458  9.378   1.00 12.97 ? 244 ASN A ND2 1 
ATOM   1994 N  N   . TRP A 1 244 ? -1.552  -8.563  13.875  1.00 7.66  ? 245 TRP A N   1 
ATOM   1995 C  CA  . TRP A 1 244 ? -2.018  -8.292  15.214  1.00 7.08  ? 245 TRP A CA  1 
ATOM   1996 C  C   . TRP A 1 244 ? -0.851  -8.189  16.152  1.00 9.26  ? 245 TRP A C   1 
ATOM   1997 O  O   . TRP A 1 244 ? 0.160   -8.906  15.977  1.00 8.14  ? 245 TRP A O   1 
ATOM   1998 C  CB  . TRP A 1 244 ? -3.011  -9.426  15.654  1.00 9.56  ? 245 TRP A CB  1 
ATOM   1999 C  CG  . TRP A 1 244 ? -2.504  -10.839 15.487  1.00 5.49  ? 245 TRP A CG  1 
ATOM   2000 C  CD1 . TRP A 1 244 ? -2.677  -11.556 14.380  1.00 8.70  ? 245 TRP A CD1 1 
ATOM   2001 C  CD2 . TRP A 1 244 ? -1.955  -11.691 16.471  1.00 7.86  ? 245 TRP A CD2 1 
ATOM   2002 N  NE1 . TRP A 1 244 ? -2.166  -12.848 14.577  1.00 8.17  ? 245 TRP A NE1 1 
ATOM   2003 C  CE2 . TRP A 1 244 ? -1.739  -12.940 15.868  1.00 9.42  ? 245 TRP A CE2 1 
ATOM   2004 C  CE3 . TRP A 1 244 ? -1.680  -11.559 17.843  1.00 9.12  ? 245 TRP A CE3 1 
ATOM   2005 C  CZ2 . TRP A 1 244 ? -1.123  -13.988 16.519  1.00 8.27  ? 245 TRP A CZ2 1 
ATOM   2006 C  CZ3 . TRP A 1 244 ? -1.050  -12.652 18.514  1.00 10.84 ? 245 TRP A CZ3 1 
ATOM   2007 C  CH2 . TRP A 1 244 ? -0.845  -13.865 17.818  1.00 9.67  ? 245 TRP A CH2 1 
ATOM   2008 N  N   . ARG A 1 245 ? -0.993  -7.285  17.127  1.00 6.53  ? 246 ARG A N   1 
ATOM   2009 C  CA  . ARG A 1 245 ? -0.042  -7.179  18.235  1.00 7.27  ? 246 ARG A CA  1 
ATOM   2010 C  C   . ARG A 1 245 ? -0.534  -8.125  19.340  1.00 7.49  ? 246 ARG A C   1 
ATOM   2011 O  O   . ARG A 1 245 ? -1.720  -8.175  19.657  1.00 8.78  ? 246 ARG A O   1 
ATOM   2012 C  CB  . ARG A 1 245 ? -0.073  -5.775  18.792  1.00 7.51  ? 246 ARG A CB  1 
ATOM   2013 C  CG  . ARG A 1 245 ? 1.056   -5.528  19.731  1.00 7.32  ? 246 ARG A CG  1 
ATOM   2014 C  CD  . ARG A 1 245 ? 1.017   -4.156  20.295  1.00 8.15  ? 246 ARG A CD  1 
ATOM   2015 N  NE  . ARG A 1 245 ? 2.284   -3.829  20.966  1.00 10.88 ? 246 ARG A NE  1 
ATOM   2016 C  CZ  . ARG A 1 245 ? 2.468   -2.848  21.853  1.00 12.44 ? 246 ARG A CZ  1 
ATOM   2017 N  NH1 . ARG A 1 245 ? 1.473   -2.047  22.206  1.00 7.41  ? 246 ARG A NH1 1 
ATOM   2018 N  NH2 . ARG A 1 245 ? 3.666   -2.666  22.394  1.00 11.09 ? 246 ARG A NH2 1 
ATOM   2019 N  N   . PRO A 1 246 ? 0.359   -8.906  19.950  1.00 8.08  ? 247 PRO A N   1 
ATOM   2020 C  CA  . PRO A 1 246 ? -0.065  -9.760  21.064  1.00 6.95  ? 247 PRO A CA  1 
ATOM   2021 C  C   . PRO A 1 246 ? -0.367  -8.934  22.326  1.00 7.83  ? 247 PRO A C   1 
ATOM   2022 O  O   . PRO A 1 246 ? 0.023   -7.761  22.450  1.00 9.11  ? 247 PRO A O   1 
ATOM   2023 C  CB  . PRO A 1 246 ? 1.202   -10.613 21.412  1.00 11.67 ? 247 PRO A CB  1 
ATOM   2024 C  CG  . PRO A 1 246 ? 2.135   -10.361 20.252  1.00 12.55 ? 247 PRO A CG  1 
ATOM   2025 C  CD  . PRO A 1 246 ? 1.819   -9.029  19.630  1.00 9.45  ? 247 PRO A CD  1 
ATOM   2026 N  N   . ALA A 1 247 ? -1.009  -9.609  23.277  1.00 8.29  ? 248 ALA A N   1 
ATOM   2027 C  CA  . ALA A 1 247 ? -1.344  -8.999  24.551  1.00 7.24  ? 248 ALA A CA  1 
ATOM   2028 C  C   . ALA A 1 247 ? -0.117  -8.453  25.277  1.00 9.30  ? 248 ALA A C   1 
ATOM   2029 O  O   . ALA A 1 247 ? 0.972   -9.114  25.239  1.00 11.72 ? 248 ALA A O   1 
ATOM   2030 C  CB  . ALA A 1 247 ? -2.087  -10.021 25.435  1.00 9.17  ? 248 ALA A CB  1 
ATOM   2031 N  N   . GLN A 1 248 ? -0.274  -7.293  25.864  1.00 7.89  ? 249 GLN A N   1 
ATOM   2032 C  CA  . GLN A 1 248 ? 0.758   -6.569  26.571  1.00 9.96  ? 249 GLN A CA  1 
ATOM   2033 C  C   . GLN A 1 248 ? 0.458   -6.543  28.082  1.00 10.34 ? 249 GLN A C   1 
ATOM   2034 O  O   . GLN A 1 248 ? -0.671  -6.726  28.523  1.00 8.71  ? 249 GLN A O   1 
ATOM   2035 C  CB  . GLN A 1 248 ? 0.739   -5.145  26.049  1.00 10.64 ? 249 GLN A CB  1 
ATOM   2036 C  CG  . GLN A 1 248 ? 1.100   -5.082  24.531  1.00 9.14  ? 249 GLN A CG  1 
ATOM   2037 C  CD  . GLN A 1 248 ? 2.457   -5.698  24.189  1.00 11.44 ? 249 GLN A CD  1 
ATOM   2038 O  OE1 . GLN A 1 248 ? 3.459   -5.381  24.847  1.00 13.24 ? 249 GLN A OE1 1 
ATOM   2039 N  NE2 . GLN A 1 248 ? 2.491   -6.645  23.246  1.00 11.84 ? 249 GLN A NE2 1 
ATOM   2040 N  N   . PRO A 1 249 ? 1.493   -6.286  28.917  1.00 11.77 ? 250 PRO A N   1 
ATOM   2041 C  CA  . PRO A 1 249 ? 1.237   -6.339  30.376  1.00 12.08 ? 250 PRO A CA  1 
ATOM   2042 C  C   . PRO A 1 249 ? 0.192   -5.301  30.827  1.00 9.87  ? 250 PRO A C   1 
ATOM   2043 O  O   . PRO A 1 249 ? 0.186   -4.158  30.404  1.00 12.04 ? 250 PRO A O   1 
ATOM   2044 C  CB  . PRO A 1 249 ? 2.619   -6.041  30.985  1.00 14.42 ? 250 PRO A CB  1 
ATOM   2045 C  CG  . PRO A 1 249 ? 3.600   -6.469  29.907  1.00 15.59 ? 250 PRO A CG  1 
ATOM   2046 C  CD  . PRO A 1 249 ? 2.887   -6.030  28.555  1.00 12.02 ? 250 PRO A CD  1 
ATOM   2047 N  N   . LEU A 1 250 ? -0.723  -5.800  31.646  1.00 11.23 ? 251 LEU A N   1 
ATOM   2048 C  CA  . LEU A 1 250 ? -1.775  -4.965  32.177  1.00 11.21 ? 251 LEU A CA  1 
ATOM   2049 C  C   . LEU A 1 250 ? -1.207  -3.851  33.090  1.00 12.31 ? 251 LEU A C   1 
ATOM   2050 O  O   . LEU A 1 250 ? -1.740  -2.724  33.154  1.00 11.13 ? 251 LEU A O   1 
ATOM   2051 C  CB  . LEU A 1 250 ? -2.831  -5.796  32.892  1.00 12.98 ? 251 LEU A CB  1 
ATOM   2052 C  CG  . LEU A 1 250 ? -4.110  -5.103  33.300  1.00 13.91 ? 251 LEU A CG  1 
ATOM   2053 C  CD1 . LEU A 1 250 ? -4.802  -4.487  32.082  1.00 14.76 ? 251 LEU A CD1 1 
ATOM   2054 C  CD2 . LEU A 1 250 ? -5.002  -6.127  34.054  1.00 15.61 ? 251 LEU A CD2 1 
ATOM   2055 N  N   . LYS A 1 251 ? -0.160  -4.191  33.833  1.00 13.16 ? 252 LYS A N   1 
ATOM   2056 C  CA  . LYS A 1 251 ? 0.495   -3.167  34.692  1.00 13.07 ? 252 LYS A CA  1 
ATOM   2057 C  C   . LYS A 1 251 ? -0.530  -2.649  35.671  1.00 13.81 ? 252 LYS A C   1 
ATOM   2058 O  O   . LYS A 1 251 ? -1.358  -3.439  36.193  1.00 14.86 ? 252 LYS A O   1 
ATOM   2059 C  CB  . LYS A 1 251 ? 1.210   -2.094  33.847  1.00 12.78 ? 252 LYS A CB  1 
ATOM   2060 C  CG  . LYS A 1 251 ? 2.439   -2.773  33.097  1.00 15.28 ? 252 LYS A CG  1 
ATOM   2061 C  CD  . LYS A 1 251 ? 3.391   -1.770  32.544  1.00 17.23 ? 252 LYS A CD  1 
ATOM   2062 C  CE  . LYS A 1 251 ? 4.445   -2.507  31.792  1.00 18.40 ? 252 LYS A CE  1 
ATOM   2063 N  NZ  . LYS A 1 251 ? 5.418   -1.557  31.320  1.00 21.13 ? 252 LYS A NZ  1 
ATOM   2064 N  N   . ASN A 1 252 ? -0.541  -1.366  35.900  1.00 14.44 ? 253 ASN A N   1 
ATOM   2065 C  CA  . ASN A 1 252 ? -1.336  -0.868  36.963  1.00 18.66 ? 253 ASN A CA  1 
ATOM   2066 C  C   . ASN A 1 252 ? -2.670  -0.445  36.409  1.00 18.54 ? 253 ASN A C   1 
ATOM   2067 O  O   . ASN A 1 252 ? -2.897  0.856   36.430  1.00 19.81 ? 253 ASN A O   1 
ATOM   2068 C  CB  . ASN A 1 252 ? -0.641  0.378   37.569  1.00 20.21 ? 253 ASN A CB  1 
ATOM   2069 C  CG  . ASN A 1 252 ? -1.369  0.929   38.811  1.00 26.79 ? 253 ASN A CG  1 
ATOM   2070 O  OD1 . ASN A 1 252 ? -2.017  0.183   39.562  1.00 33.41 ? 253 ASN A OD1 1 
ATOM   2071 N  ND2 . ASN A 1 252 ? -1.307  2.240   38.994  1.00 32.32 ? 253 ASN A ND2 1 
ATOM   2072 N  N   . ARG A 1 253 ? -3.417  -1.445  35.806  1.00 13.68 ? 254 ARG A N   1 
ATOM   2073 C  CA  . ARG A 1 253 ? -4.759  -1.136  35.319  1.00 12.48 ? 254 ARG A CA  1 
ATOM   2074 C  C   . ARG A 1 253 ? -5.857  -2.111  35.716  1.00 14.38 ? 254 ARG A C   1 
ATOM   2075 O  O   . ARG A 1 253 ? -5.593  -3.280  35.868  1.00 15.70 ? 254 ARG A O   1 
ATOM   2076 C  CB  . ARG A 1 253 ? -4.787  -0.968  33.744  1.00 11.77 ? 254 ARG A CB  1 
ATOM   2077 C  CG  . ARG A 1 253 ? -3.852  0.147   33.204  1.00 10.02 ? 254 ARG A CG  1 
ATOM   2078 C  CD  . ARG A 1 253 ? -3.774  0.112   31.732  1.00 12.25 ? 254 ARG A CD  1 
ATOM   2079 N  NE  . ARG A 1 253 ? -2.910  -1.027  31.287  1.00 10.16 ? 254 ARG A NE  1 
ATOM   2080 C  CZ  . ARG A 1 253 ? -2.679  -1.269  30.003  1.00 7.53  ? 254 ARG A CZ  1 
ATOM   2081 N  NH1 . ARG A 1 253 ? -3.232  -0.491  29.027  1.00 8.57  ? 254 ARG A NH1 1 
ATOM   2082 N  NH2 . ARG A 1 253 ? -1.888  -2.265  29.679  1.00 8.97  ? 254 ARG A NH2 1 
ATOM   2083 N  N   . GLN A 1 254 ? -7.098  -1.582  35.843  1.00 13.41 ? 255 GLN A N   1 
ATOM   2084 C  CA  . GLN A 1 254 ? -8.262  -2.472  36.105  1.00 17.88 ? 255 GLN A CA  1 
ATOM   2085 C  C   . GLN A 1 254 ? -9.218  -2.385  34.888  1.00 14.24 ? 255 GLN A C   1 
ATOM   2086 O  O   . GLN A 1 254 ? -9.495  -1.303  34.358  1.00 18.25 ? 255 GLN A O   1 
ATOM   2087 C  CB  . GLN A 1 254 ? -9.022  -2.124  37.408  1.00 18.62 ? 255 GLN A CB  1 
ATOM   2088 C  CG  . GLN A 1 254 ? -9.525  -3.447  38.097  1.00 25.53 ? 255 GLN A CG  1 
ATOM   2089 C  CD  . GLN A 1 254 ? -10.593 -3.308  39.227  1.00 26.35 ? 255 GLN A CD  1 
ATOM   2090 O  OE1 . GLN A 1 254 ? -11.477 -2.441  39.167  1.00 36.97 ? 255 GLN A OE1 1 
ATOM   2091 N  NE2 . GLN A 1 254 ? -10.570 -4.274  40.188  1.00 33.50 ? 255 GLN A NE2 1 
ATOM   2092 N  N   . ILE A 1 255 ? -9.557  -3.557  34.371  1.00 12.85 ? 256 ILE A N   1 
ATOM   2093 C  CA  . ILE A 1 255 ? -10.571 -3.641  33.341  1.00 11.47 ? 256 ILE A CA  1 
ATOM   2094 C  C   . ILE A 1 255 ? -11.930 -3.672  34.025  1.00 10.38 ? 256 ILE A C   1 
ATOM   2095 O  O   . ILE A 1 255 ? -12.125 -4.345  35.028  1.00 10.75 ? 256 ILE A O   1 
ATOM   2096 C  CB  . ILE A 1 255 ? -10.348 -4.885  32.492  1.00 11.61 ? 256 ILE A CB  1 
ATOM   2097 C  CG1 . ILE A 1 255 ? -8.946  -4.802  31.845  1.00 15.49 ? 256 ILE A CG1 1 
ATOM   2098 C  CG2 . ILE A 1 255 ? -11.498 -5.105  31.423  1.00 11.06 ? 256 ILE A CG2 1 
ATOM   2099 C  CD1 . ILE A 1 255 ? -8.634  -6.077  31.076  1.00 16.23 ? 256 ILE A CD1 1 
ATOM   2100 N  N   . LYS A 1 256 ? -12.786 -2.777  33.545  1.00 9.36  ? 257 LYS A N   1 
ATOM   2101 C  CA  . LYS A 1 256 ? -14.164 -2.586  34.104  1.00 10.72 ? 257 LYS A CA  1 
ATOM   2102 C  C   . LYS A 1 256 ? -15.128 -3.240  33.135  1.00 11.09 ? 257 LYS A C   1 
ATOM   2103 O  O   . LYS A 1 256 ? -14.946 -3.216  31.927  1.00 10.35 ? 257 LYS A O   1 
ATOM   2104 C  CB  . LYS A 1 256 ? -14.494 -1.085  34.283  1.00 11.43 ? 257 LYS A CB  1 
ATOM   2105 C  CG  . LYS A 1 256 ? -13.612 -0.413  35.366  1.00 15.11 ? 257 LYS A CG  1 
ATOM   2106 C  CD  . LYS A 1 256 ? -13.987 -0.884  36.766  0.01 13.81 ? 257 LYS A CD  1 
ATOM   2107 C  CE  . LYS A 1 256 ? -13.414 0.021   37.844  0.01 14.00 ? 257 LYS A CE  1 
ATOM   2108 N  NZ  . LYS A 1 256 ? -14.230 1.251   38.029  0.01 13.68 ? 257 LYS A NZ  1 
ATOM   2109 N  N   . ALA A 1 257 ? -16.200 -3.819  33.658  1.00 10.92 ? 258 ALA A N   1 
ATOM   2110 C  CA  . ALA A 1 257 ? -17.269 -4.402  32.881  1.00 10.86 ? 258 ALA A CA  1 
ATOM   2111 C  C   . ALA A 1 257 ? -18.563 -3.673  33.069  1.00 11.57 ? 258 ALA A C   1 
ATOM   2112 O  O   . ALA A 1 257 ? -18.936 -3.274  34.206  1.00 11.50 ? 258 ALA A O   1 
ATOM   2113 C  CB  . ALA A 1 257 ? -17.431 -5.911  33.169  1.00 10.63 ? 258 ALA A CB  1 
ATOM   2114 N  N   . SER A 1 258 ? -19.312 -3.577  31.982  1.00 9.58  ? 259 SER A N   1 
ATOM   2115 C  CA  . SER A 1 258 ? -20.579 -2.844  32.032  1.00 11.64 ? 259 SER A CA  1 
ATOM   2116 C  C   . SER A 1 258 ? -21.654 -3.833  32.435  1.00 14.21 ? 259 SER A C   1 
ATOM   2117 O  O   . SER A 1 258 ? -22.820 -3.416  32.605  1.00 17.65 ? 259 SER A O   1 
ATOM   2118 C  CB  . SER A 1 258 ? -20.951 -2.223  30.685  1.00 13.12 ? 259 SER A CB  1 
ATOM   2119 O  OG  . SER A 1 258 ? -21.394 -3.202  29.734  1.00 12.49 ? 259 SER A OG  1 
ATOM   2120 N  N   . PHE A 1 259 ? -21.330 -5.087  32.615  1.00 14.01 ? 260 PHE A N   1 
ATOM   2121 C  CA  . PHE A 1 259 ? -22.351 -6.128  32.757  1.00 15.57 ? 260 PHE A CA  1 
ATOM   2122 C  C   . PHE A 1 259 ? -21.884 -7.085  33.830  1.00 19.45 ? 260 PHE A C   1 
ATOM   2123 O  O   . PHE A 1 259 ? -20.677 -7.170  34.182  1.00 17.14 ? 260 PHE A O   1 
ATOM   2124 C  CB  . PHE A 1 259 ? -22.594 -6.856  31.463  1.00 17.76 ? 260 PHE A CB  1 
ATOM   2125 C  CG  . PHE A 1 259 ? -21.329 -7.584  30.951  1.00 16.46 ? 260 PHE A CG  1 
ATOM   2126 C  CD1 . PHE A 1 259 ? -20.334 -6.841  30.274  1.00 16.30 ? 260 PHE A CD1 1 
ATOM   2127 C  CD2 . PHE A 1 259 ? -21.104 -8.916  31.278  1.00 16.98 ? 260 PHE A CD2 1 
ATOM   2128 C  CE1 . PHE A 1 259 ? -19.145 -7.451  29.852  1.00 17.84 ? 260 PHE A CE1 1 
ATOM   2129 C  CE2 . PHE A 1 259 ? -19.889 -9.525  30.936  1.00 18.89 ? 260 PHE A CE2 1 
ATOM   2130 C  CZ  . PHE A 1 259 ? -18.891 -8.776  30.179  1.00 17.03 ? 260 PHE A CZ  1 
ATOM   2131 N  N   . LYS A 1 260 ? -22.909 -7.851  34.235  1.00 24.28 ? 261 LYS A N   1 
ATOM   2132 C  CA  . LYS A 1 260 ? -22.914 -9.037  35.101  1.00 31.50 ? 261 LYS A CA  1 
ATOM   2133 C  C   . LYS A 1 260 ? -22.441 -8.905  36.534  1.00 34.03 ? 261 LYS A C   1 
ATOM   2134 O  O   . LYS A 1 260 ? -21.911 -7.862  36.998  0.01 36.87 ? 261 LYS A O   1 
ATOM   2135 C  CB  . LYS A 1 260 ? -22.435 -10.324 34.382  1.00 31.69 ? 261 LYS A CB  1 
ATOM   2136 C  CG  . LYS A 1 260 ? -23.465 -10.782 33.319  1.00 33.47 ? 261 LYS A CG  1 
ATOM   2137 C  CD  . LYS A 1 260 ? -23.213 -12.155 32.630  1.00 32.66 ? 261 LYS A CD  1 
ATOM   2138 C  CE  . LYS A 1 260 ? -21.707 -12.451 32.372  1.00 34.21 ? 261 LYS A CE  1 
ATOM   2139 N  NZ  . LYS A 1 260 ? -21.296 -13.896 32.134  1.00 36.89 ? 261 LYS A NZ  1 
ATOM   2140 O  OXT . LYS A 1 260 ? -22.708 -9.844  37.297  1.00 36.41 ? 261 LYS A OXT 1 
HETATM 2141 ZN ZN  . ZN  B 2 .   ? -6.551  -1.696  15.197  1.00 7.51  ? 301 ZN  A ZN  1 
HETATM 2142 O  O1  . MES C 3 .   ? -7.435  -9.098  -2.533  1.00 28.75 ? 302 MES A O1  1 
HETATM 2143 C  C2  . MES C 3 .   ? -7.216  -9.889  -3.800  1.00 28.78 ? 302 MES A C2  1 
HETATM 2144 C  C3  . MES C 3 .   ? -8.427  -10.766 -4.158  1.00 27.32 ? 302 MES A C3  1 
HETATM 2145 N  N4  . MES C 3 .   ? -9.549  -10.937 -3.211  1.00 26.93 ? 302 MES A N4  1 
HETATM 2146 C  C5  . MES C 3 .   ? -9.627  -10.156 -1.953  1.00 24.30 ? 302 MES A C5  1 
HETATM 2147 C  C6  . MES C 3 .   ? -8.406  -9.607  -1.536  1.00 23.86 ? 302 MES A C6  1 
HETATM 2148 C  C7  . MES C 3 .   ? -10.710 -11.866 -3.413  1.00 29.79 ? 302 MES A C7  1 
HETATM 2149 C  C8  . MES C 3 .   ? -12.153 -11.193 -3.322  1.00 28.65 ? 302 MES A C8  1 
HETATM 2150 S  S   . DMS D 4 .   ? 1.434   -11.670 14.882  1.00 29.67 ? 303 DMS A S   1 
HETATM 2151 O  O   . DMS D 4 .   ? 2.599   -10.623 13.852  1.00 29.76 ? 303 DMS A O   1 
HETATM 2152 C  C1  . DMS D 4 .   ? 2.058   -13.309 14.654  1.00 26.43 ? 303 DMS A C1  1 
HETATM 2153 C  C2  . DMS D 4 .   ? 1.807   -11.608 16.625  1.00 22.06 ? 303 DMS A C2  1 
HETATM 2154 F  F13 . V50 E 5 .   ? -2.858  1.546   16.530  1.00 33.38 ? 304 V50 A F13 1 
HETATM 2155 C  C4  . V50 E 5 .   ? -3.570  2.473   15.934  1.00 31.92 ? 304 V50 A C4  1 
HETATM 2156 C  C5  . V50 E 5 .   ? -4.969  2.280   15.945  1.00 27.20 ? 304 V50 A C5  1 
HETATM 2157 S  S7  . V50 E 5 .   ? -5.833  0.975   16.828  1.00 27.39 ? 304 V50 A S7  1 
HETATM 2158 O  O9  . V50 E 5 .   ? -5.266  0.713   18.108  1.00 17.24 ? 304 V50 A O9  1 
HETATM 2159 N  N23 . V50 E 5 .   ? -5.371  -0.326  16.004  1.00 12.55 ? 304 V50 A N23 1 
HETATM 2160 O  O8  . V50 E 5 .   ? -7.259  0.794   16.486  1.00 20.41 ? 304 V50 A O8  1 
HETATM 2161 C  C6  . V50 E 5 .   ? -5.676  3.280   15.278  1.00 31.05 ? 304 V50 A C6  1 
HETATM 2162 F  F11 . V50 E 5 .   ? -6.992  3.162   15.322  1.00 35.74 ? 304 V50 A F11 1 
HETATM 2163 C  C1  . V50 E 5 .   ? -5.067  4.374   14.600  1.00 31.51 ? 304 V50 A C1  1 
HETATM 2164 F  F10 . V50 E 5 .   ? -5.839  5.277   13.968  1.00 32.04 ? 304 V50 A F10 1 
HETATM 2165 C  C3  . V50 E 5 .   ? -2.905  3.554   15.260  1.00 32.24 ? 304 V50 A C3  1 
HETATM 2166 F  F12 . V50 E 5 .   ? -1.520  3.721   15.191  1.00 31.95 ? 304 V50 A F12 1 
HETATM 2167 C  C2  . V50 E 5 .   ? -3.654  4.539   14.620  1.00 32.41 ? 304 V50 A C2  1 
HETATM 2168 S  S14 . V50 E 5 .   ? -2.701  5.794   13.764  1.00 34.67 ? 304 V50 A S14 1 
HETATM 2169 C  C15 . V50 E 5 .   ? -2.093  7.517   13.780  1.00 43.08 ? 304 V50 A C15 1 
HETATM 2170 N  N20 . V50 E 5 .   ? -2.513  8.184   12.661  1.00 45.72 ? 304 V50 A N20 1 
HETATM 2171 C  C19 . V50 E 5 .   ? -2.142  9.490   12.478  1.00 42.36 ? 304 V50 A C19 1 
HETATM 2172 C  C21 . V50 E 5 .   ? -2.693  10.202  11.267  1.00 42.54 ? 304 V50 A C21 1 
HETATM 2173 C  C18 . V50 E 5 .   ? -1.333  10.202  13.324  1.00 42.68 ? 304 V50 A C18 1 
HETATM 2174 C  C17 . V50 E 5 .   ? -0.896  9.435   14.388  1.00 42.43 ? 304 V50 A C17 1 
HETATM 2175 N  N16 . V50 E 5 .   ? -1.223  8.116   14.655  1.00 45.13 ? 304 V50 A N16 1 
HETATM 2176 C  C22 . V50 E 5 .   ? 0.028   10.198  15.315  1.00 43.27 ? 304 V50 A C22 1 
HETATM 2177 O  O   . HOH F 6 .   ? -4.425  -13.575 18.023  1.00 10.12 ? 401 HOH A O   1 
HETATM 2178 O  O   . HOH F 6 .   ? -1.153  -4.136  15.649  1.00 8.07  ? 402 HOH A O   1 
HETATM 2179 O  O   . HOH F 6 .   ? -10.609 8.633   25.509  1.00 9.61  ? 403 HOH A O   1 
HETATM 2180 O  O   . HOH F 6 .   ? -2.399  -8.785  29.093  1.00 11.74 ? 404 HOH A O   1 
HETATM 2181 O  O   . HOH F 6 .   ? -1.946  -12.378 22.860  1.00 11.09 ? 405 HOH A O   1 
HETATM 2182 O  O   . HOH F 6 .   ? -3.425  -11.143 20.843  1.00 10.71 ? 406 HOH A O   1 
HETATM 2183 O  O   . HOH F 6 .   ? -21.492 -7.153  23.523  1.00 11.95 ? 407 HOH A O   1 
HETATM 2184 O  O   . HOH F 6 .   ? -21.732 5.626   4.700   1.00 14.37 ? 408 HOH A O   1 
HETATM 2185 O  O   . HOH F 6 .   ? -16.894 -8.452  20.371  1.00 7.39  ? 409 HOH A O   1 
HETATM 2186 O  O   . HOH F 6 .   ? -7.806  -15.410 11.330  1.00 10.95 ? 410 HOH A O   1 
HETATM 2187 O  O   . HOH F 6 .   ? -3.414  -13.251 25.156  1.00 11.69 ? 411 HOH A O   1 
HETATM 2188 O  O   . HOH F 6 .   ? 1.268   -1.687  29.375  1.00 14.68 ? 412 HOH A O   1 
HETATM 2189 O  O   . HOH F 6 .   ? -17.845 -20.476 8.025   1.00 13.41 ? 413 HOH A O   1 
HETATM 2190 O  O   . HOH F 6 .   ? -3.699  -15.915 24.319  1.00 11.10 ? 414 HOH A O   1 
HETATM 2191 O  O   . HOH F 6 .   ? 5.440   7.089   20.102  1.00 15.06 ? 415 HOH A O   1 
HETATM 2192 O  O   . HOH F 6 .   ? -16.207 -9.929  32.807  1.00 16.28 ? 416 HOH A O   1 
HETATM 2193 O  O   . HOH F 6 .   ? -12.666 -17.256 16.863  1.00 16.87 ? 417 HOH A O   1 
HETATM 2194 O  O   . HOH F 6 .   ? 8.592   -3.857  21.116  1.00 14.01 ? 418 HOH A O   1 
HETATM 2195 O  O   . HOH F 6 .   ? -26.746 -2.669  14.308  1.00 18.76 ? 419 HOH A O   1 
HETATM 2196 O  O   . HOH F 6 .   ? -23.606 -0.929  3.826   1.00 21.67 ? 420 HOH A O   1 
HETATM 2197 O  O   . HOH F 6 .   ? 7.627   6.049   21.670  1.00 15.99 ? 421 HOH A O   1 
HETATM 2198 O  O   . HOH F 6 .   ? -16.052 -12.325 24.361  1.00 15.82 ? 422 HOH A O   1 
HETATM 2199 O  O   . HOH F 6 .   ? -17.763 -22.009 6.068   1.00 10.31 ? 423 HOH A O   1 
HETATM 2200 O  O   . HOH F 6 .   ? -23.882 -0.791  26.429  1.00 15.62 ? 424 HOH A O   1 
HETATM 2201 O  O   . HOH F 6 .   ? -9.765  14.608  12.083  1.00 17.37 ? 425 HOH A O   1 
HETATM 2202 O  O   . HOH F 6 .   ? -0.389  10.799  23.463  1.00 15.57 ? 426 HOH A O   1 
HETATM 2203 O  O   . HOH F 6 .   ? -23.155 -2.994  6.723   1.00 18.30 ? 427 HOH A O   1 
HETATM 2204 O  O   . HOH F 6 .   ? -17.864 10.280  11.301  1.00 15.74 ? 428 HOH A O   1 
HETATM 2205 O  O   . HOH F 6 .   ? 4.476   -3.509  26.334  1.00 17.43 ? 429 HOH A O   1 
HETATM 2206 O  O   . HOH F 6 .   ? 3.786   4.996   29.669  1.00 20.88 ? 430 HOH A O   1 
HETATM 2207 O  O   . HOH F 6 .   ? -13.997 10.485  27.690  1.00 19.27 ? 431 HOH A O   1 
HETATM 2208 O  O   . HOH F 6 .   ? -9.604  -8.185  33.873  1.00 20.44 ? 432 HOH A O   1 
HETATM 2209 O  O   . HOH F 6 .   ? -13.344 -18.575 14.581  1.00 24.49 ? 433 HOH A O   1 
HETATM 2210 O  O   . HOH F 6 .   ? 1.349   8.688   24.428  1.00 17.83 ? 434 HOH A O   1 
HETATM 2211 O  O   . HOH F 6 .   ? -19.361 9.979   8.952   1.00 14.53 ? 435 HOH A O   1 
HETATM 2212 O  O   . HOH F 6 .   ? -2.327  -3.302  11.408  1.00 18.36 ? 436 HOH A O   1 
HETATM 2213 O  O   . HOH F 6 .   ? -11.814 2.780   30.704  1.00 26.36 ? 437 HOH A O   1 
HETATM 2214 O  O   . HOH F 6 .   ? 8.012   -5.862  -10.510 1.00 22.54 ? 438 HOH A O   1 
HETATM 2215 O  O   . HOH F 6 .   ? -6.830  -14.890 31.479  1.00 16.26 ? 439 HOH A O   1 
HETATM 2216 O  O   . HOH F 6 .   ? 0.029   -0.934  -4.716  1.00 18.57 ? 440 HOH A O   1 
HETATM 2217 O  O   . HOH F 6 .   ? -8.577  -3.888  7.858   1.00 10.95 ? 441 HOH A O   1 
HETATM 2218 O  O   . HOH F 6 .   ? -10.291 -18.243 16.952  1.00 17.97 ? 442 HOH A O   1 
HETATM 2219 O  O   . HOH F 6 .   ? -6.592  -20.242 19.507  1.00 19.49 ? 443 HOH A O   1 
HETATM 2220 O  O   . HOH F 6 .   ? -7.224  -8.788  32.594  1.00 15.80 ? 444 HOH A O   1 
HETATM 2221 O  O   . HOH F 6 .   ? -8.916  -6.051  35.757  1.00 15.28 ? 445 HOH A O   1 
HETATM 2222 O  O   . HOH F 6 .   ? -14.239 -16.641 28.776  1.00 22.45 ? 446 HOH A O   1 
HETATM 2223 O  O   . HOH F 6 .   ? -22.415 3.520   -2.917  1.00 22.45 ? 447 HOH A O   1 
HETATM 2224 O  O   . HOH F 6 .   ? -5.882  -4.495  -6.426  1.00 23.97 ? 448 HOH A O   1 
HETATM 2225 O  O   . HOH F 6 .   ? -13.661 -8.861  -5.265  1.00 20.82 ? 449 HOH A O   1 
HETATM 2226 O  O   . HOH F 6 .   ? 1.593   -11.717 24.991  1.00 19.73 ? 450 HOH A O   1 
HETATM 2227 O  O   . HOH F 6 .   ? -24.829 -7.838  9.020   1.00 15.67 ? 451 HOH A O   1 
HETATM 2228 O  O   . HOH F 6 .   ? -22.585 -5.860  2.746   1.00 17.09 ? 452 HOH A O   1 
HETATM 2229 O  O   . HOH F 6 .   ? -30.608 1.508   25.953  1.00 23.68 ? 453 HOH A O   1 
HETATM 2230 O  O   . HOH F 6 .   ? 2.726   -4.153  7.773   1.00 22.09 ? 454 HOH A O   1 
HETATM 2231 O  O   . HOH F 6 .   ? -20.924 -12.691 -1.776  1.00 13.56 ? 455 HOH A O   1 
HETATM 2232 O  O   . HOH F 6 .   ? -1.646  -13.244 27.321  1.00 22.53 ? 456 HOH A O   1 
HETATM 2233 O  O   . HOH F 6 .   ? -8.458  0.706   -6.547  1.00 25.16 ? 457 HOH A O   1 
HETATM 2234 O  O   . HOH F 6 .   ? -14.769 -21.068 17.464  1.00 28.55 ? 458 HOH A O   1 
HETATM 2235 O  O   . HOH F 6 .   ? 4.350   -2.513  28.656  1.00 24.21 ? 459 HOH A O   1 
HETATM 2236 O  O   . HOH F 6 .   ? -8.069  -19.375 21.654  1.00 16.75 ? 460 HOH A O   1 
HETATM 2237 O  O   . HOH F 6 .   ? -20.356 10.876  26.435  1.00 16.10 ? 461 HOH A O   1 
HETATM 2238 O  O   . HOH F 6 .   ? -26.801 -4.085  24.940  1.00 19.11 ? 462 HOH A O   1 
HETATM 2239 O  O   . HOH F 6 .   ? -11.048 -19.252 6.972   1.00 27.82 ? 463 HOH A O   1 
HETATM 2240 O  O   . HOH F 6 .   ? 4.521   -6.445  7.836   1.00 25.61 ? 464 HOH A O   1 
HETATM 2241 O  O   . HOH F 6 .   ? -0.162  -14.207 22.251  1.00 23.95 ? 465 HOH A O   1 
HETATM 2242 O  O   . HOH F 6 .   ? -24.601 -9.393  2.019   1.00 21.58 ? 466 HOH A O   1 
HETATM 2243 O  O   . HOH F 6 .   ? -4.229  -8.540  31.033  1.00 20.68 ? 467 HOH A O   1 
HETATM 2244 O  O   . HOH F 6 .   ? -21.795 -18.504 13.609  1.00 24.99 ? 468 HOH A O   1 
HETATM 2245 O  O   . HOH F 6 .   ? -23.247 -13.386 11.360  1.00 26.74 ? 469 HOH A O   1 
HETATM 2246 O  O   . HOH F 6 .   ? -30.958 -6.763  22.453  1.00 25.77 ? 470 HOH A O   1 
HETATM 2247 O  O   . HOH F 6 .   ? -16.042 15.782  23.647  1.00 17.33 ? 471 HOH A O   1 
HETATM 2248 O  O   . HOH F 6 .   ? 8.814   -4.651  23.649  1.00 25.56 ? 472 HOH A O   1 
HETATM 2249 O  O   . HOH F 6 .   ? 2.715   -11.407 9.323   1.00 24.21 ? 473 HOH A O   1 
HETATM 2250 O  O   . HOH F 6 .   ? -5.700  -11.566 36.353  1.00 30.52 ? 474 HOH A O   1 
HETATM 2251 O  O   . HOH F 6 .   ? -19.308 -20.692 4.889   1.00 19.90 ? 475 HOH A O   1 
HETATM 2252 O  O   . HOH F 6 .   ? -14.416 -18.450 18.779  1.00 20.43 ? 476 HOH A O   1 
HETATM 2253 O  O   . HOH F 6 .   ? -23.484 8.381   3.434   1.00 20.67 ? 477 HOH A O   1 
HETATM 2254 O  O   . HOH F 6 .   ? -18.695 12.082  12.840  1.00 23.94 ? 478 HOH A O   1 
HETATM 2255 O  O   . HOH F 6 .   ? 9.699   -4.551  -7.958  1.00 22.21 ? 479 HOH A O   1 
HETATM 2256 O  O   . HOH F 6 .   ? -10.914 -15.402 33.942  1.00 27.25 ? 480 HOH A O   1 
HETATM 2257 O  O   . HOH F 6 .   ? -5.599  3.639   -5.718  1.00 29.71 ? 481 HOH A O   1 
HETATM 2258 O  O   . HOH F 6 .   ? -0.250  -19.601 6.556   1.00 29.97 ? 482 HOH A O   1 
HETATM 2259 O  O   . HOH F 6 .   ? -26.200 3.743   15.231  1.00 25.99 ? 483 HOH A O   1 
HETATM 2260 O  O   . HOH F 6 .   ? -1.196  9.211   27.831  1.00 24.64 ? 484 HOH A O   1 
HETATM 2261 O  O   . HOH F 6 .   ? 2.358   8.105   27.561  1.00 31.79 ? 485 HOH A O   1 
HETATM 2262 O  O   . HOH F 6 .   ? -13.188 -22.349 11.383  1.00 29.08 ? 486 HOH A O   1 
HETATM 2263 O  O   . HOH F 6 .   ? -1.907  -17.520 25.332  1.00 25.59 ? 487 HOH A O   1 
HETATM 2264 O  O   . HOH F 6 .   ? -26.606 -1.373  25.959  1.00 22.17 ? 488 HOH A O   1 
HETATM 2265 O  O   . HOH F 6 .   ? -7.093  5.897   6.553   1.00 24.28 ? 489 HOH A O   1 
HETATM 2266 O  O   . HOH F 6 .   ? -18.299 3.724   -3.684  1.00 33.92 ? 490 HOH A O   1 
HETATM 2267 O  O   . HOH F 6 .   ? -17.232 -16.312 21.805  1.00 31.59 ? 491 HOH A O   1 
HETATM 2268 O  O   . HOH F 6 .   ? -17.711 -21.231 17.556  1.00 23.94 ? 492 HOH A O   1 
HETATM 2269 O  O   . HOH F 6 .   ? -0.276  -8.700  32.313  1.00 23.41 ? 493 HOH A O   1 
HETATM 2270 O  O   . HOH F 6 .   ? -6.121  -19.853 23.901  1.00 22.26 ? 494 HOH A O   1 
HETATM 2271 O  O   . HOH F 6 .   ? -4.461  -11.995 31.867  1.00 20.04 ? 495 HOH A O   1 
HETATM 2272 O  O   . HOH F 6 .   ? -25.823 6.108   26.813  1.00 21.80 ? 496 HOH A O   1 
HETATM 2273 O  O   . HOH F 6 .   ? -15.045 -21.604 13.134  1.00 28.33 ? 497 HOH A O   1 
HETATM 2274 O  O   . HOH F 6 .   ? 2.115   -15.613 9.228   1.00 23.09 ? 498 HOH A O   1 
HETATM 2275 O  O   . HOH F 6 .   ? -24.068 8.602   20.117  1.00 22.89 ? 499 HOH A O   1 
HETATM 2276 O  O   . HOH F 6 .   ? -1.113  -17.670 17.941  1.00 28.42 ? 500 HOH A O   1 
HETATM 2277 O  O   . HOH F 6 .   ? -22.988 -0.641  34.300  1.00 25.39 ? 501 HOH A O   1 
HETATM 2278 O  O   . HOH F 6 .   ? -28.281 -0.273  6.541   1.00 28.84 ? 502 HOH A O   1 
HETATM 2279 O  O   . HOH F 6 .   ? -25.637 9.557   13.263  1.00 32.34 ? 503 HOH A O   1 
HETATM 2280 O  O   . HOH F 6 .   ? -25.527 -10.578 17.852  1.00 22.13 ? 504 HOH A O   1 
HETATM 2281 O  O   . HOH F 6 .   ? -24.933 4.374   8.332   1.00 28.48 ? 505 HOH A O   1 
HETATM 2282 O  O   . HOH F 6 .   ? -16.737 -13.909 26.373  1.00 23.12 ? 506 HOH A O   1 
HETATM 2283 O  O   . HOH F 6 .   ? 2.336   -14.115 20.545  1.00 31.35 ? 507 HOH A O   1 
HETATM 2284 O  O   . HOH F 6 .   ? -4.498  -15.796 0.661   1.00 26.62 ? 508 HOH A O   1 
HETATM 2285 O  O   . HOH F 6 .   ? -18.539 -9.034  34.309  1.00 24.10 ? 509 HOH A O   1 
HETATM 2286 O  O   . HOH F 6 .   ? -1.956  -12.193 31.252  1.00 25.88 ? 510 HOH A O   1 
HETATM 2287 O  O   . HOH F 6 .   ? -15.658 9.029   -1.922  1.00 24.17 ? 511 HOH A O   1 
HETATM 2288 O  O   . HOH F 6 .   ? -2.072  -4.581  -6.802  1.00 30.20 ? 512 HOH A O   1 
HETATM 2289 O  O   . HOH F 6 .   ? 10.242  -6.845  -8.788  1.00 30.56 ? 513 HOH A O   1 
HETATM 2290 O  O   . HOH F 6 .   ? -15.204 -16.507 25.538  1.00 34.31 ? 514 HOH A O   1 
HETATM 2291 O  O   . HOH F 6 .   ? -28.885 -5.777  24.530  1.00 22.78 ? 515 HOH A O   1 
HETATM 2292 O  O   . HOH F 6 .   ? -9.152  6.676   -3.689  1.00 32.52 ? 516 HOH A O   1 
HETATM 2293 O  O   . HOH F 6 .   ? -5.304  -9.587  34.649  1.00 34.44 ? 517 HOH A O   1 
HETATM 2294 O  O   . HOH F 6 .   ? -26.028 -6.498  13.092  1.00 23.92 ? 518 HOH A O   1 
HETATM 2295 O  O   . HOH F 6 .   ? -25.527 -15.330 7.865   1.00 27.05 ? 519 HOH A O   1 
HETATM 2296 O  O   . HOH F 6 .   ? -27.893 5.020   25.320  1.00 28.56 ? 520 HOH A O   1 
HETATM 2297 O  O   . HOH F 6 .   ? -6.498  -8.390  -7.299  1.00 40.13 ? 521 HOH A O   1 
HETATM 2298 O  O   . HOH F 6 .   ? -19.356 -4.373  41.267  1.00 30.67 ? 522 HOH A O   1 
HETATM 2299 O  O   . HOH F 6 .   ? -4.143  -15.424 -2.104  1.00 34.73 ? 523 HOH A O   1 
HETATM 2300 O  O   . HOH F 6 .   ? -12.954 3.298   -6.714  1.00 35.20 ? 524 HOH A O   1 
HETATM 2301 O  O   . HOH F 6 .   ? -8.441  -19.830 26.455  1.00 26.02 ? 525 HOH A O   1 
HETATM 2302 O  O   . HOH F 6 .   ? -31.398 3.856   8.046   1.00 44.86 ? 526 HOH A O   1 
HETATM 2303 O  O   . HOH F 6 .   ? -12.627 7.997   28.863  1.00 29.54 ? 527 HOH A O   1 
HETATM 2304 O  O   . HOH F 6 .   ? -10.372 -19.369 19.872  1.00 22.23 ? 528 HOH A O   1 
HETATM 2305 O  O   . HOH F 6 .   ? -9.143  5.826   29.142  1.00 28.74 ? 529 HOH A O   1 
HETATM 2306 O  O   . HOH F 6 .   ? -22.891 -11.733 14.150  1.00 19.02 ? 530 HOH A O   1 
HETATM 2307 O  O   . HOH F 6 .   ? 2.607   -13.039 5.184   1.00 26.26 ? 531 HOH A O   1 
HETATM 2308 O  O   . HOH F 6 .   ? -23.782 -2.446  29.031  1.00 25.37 ? 532 HOH A O   1 
HETATM 2309 O  O   . HOH F 6 .   ? 9.551   1.945   11.933  1.00 28.32 ? 533 HOH A O   1 
HETATM 2310 O  O   . HOH F 6 .   ? 14.587  0.015   14.996  1.00 26.73 ? 534 HOH A O   1 
HETATM 2311 O  O   . HOH F 6 .   ? 13.017  -3.863  13.426  1.00 25.51 ? 535 HOH A O   1 
HETATM 2312 O  O   . HOH F 6 .   ? 11.597  -0.511  16.101  1.00 26.16 ? 536 HOH A O   1 
HETATM 2313 O  O   . HOH F 6 .   ? 4.937   -4.949  20.842  1.00 12.70 ? 537 HOH A O   1 
HETATM 2314 O  O   . HOH F 6 .   ? 5.580   -6.862  22.385  1.00 30.93 ? 538 HOH A O   1 
HETATM 2315 O  O   . HOH F 6 .   ? 13.493  0.169   24.367  1.00 21.59 ? 539 HOH A O   1 
HETATM 2316 O  O   . HOH F 6 .   ? 8.297   3.164   27.626  1.00 25.11 ? 540 HOH A O   1 
HETATM 2317 O  O   . HOH F 6 .   ? -16.348 -15.222 32.742  1.00 31.54 ? 541 HOH A O   1 
HETATM 2318 O  O   . HOH F 6 .   ? -12.893 -16.861 26.534  1.00 19.50 ? 542 HOH A O   1 
HETATM 2319 O  O   . HOH F 6 .   ? -7.702  -18.971 30.467  1.00 25.32 ? 543 HOH A O   1 
HETATM 2320 O  O   . HOH F 6 .   ? -8.315  -15.084 36.936  1.00 25.78 ? 544 HOH A O   1 
HETATM 2321 O  O   . HOH F 6 .   ? -16.846 -14.108 37.449  1.00 29.43 ? 545 HOH A O   1 
HETATM 2322 O  O   . HOH F 6 .   ? -27.439 2.584   23.489  1.00 28.07 ? 546 HOH A O   1 
HETATM 2323 O  O   . HOH F 6 .   ? -19.450 17.313  6.124   1.00 18.89 ? 547 HOH A O   1 
HETATM 2324 O  O   . HOH F 6 .   ? 0.741   3.441   2.223   1.00 37.81 ? 548 HOH A O   1 
HETATM 2325 O  O   . HOH F 6 .   ? -24.684 12.051  6.387   1.00 32.30 ? 549 HOH A O   1 
HETATM 2326 O  O   . HOH F 6 .   ? -12.334 16.302  8.949   1.00 24.31 ? 550 HOH A O   1 
HETATM 2327 O  O   . HOH F 6 .   ? -20.862 8.201   29.902  1.00 26.39 ? 551 HOH A O   1 
HETATM 2328 O  O   . HOH F 6 .   ? -4.260  -20.443 6.296   1.00 35.69 ? 552 HOH A O   1 
HETATM 2329 O  O   . HOH F 6 .   ? -7.037  -16.928 1.447   1.00 21.24 ? 553 HOH A O   1 
HETATM 2330 O  O   . HOH F 6 .   ? -13.484 -21.031 14.894  1.00 28.22 ? 554 HOH A O   1 
HETATM 2331 O  O   . HOH F 6 .   ? -14.192 14.307  26.946  1.00 26.84 ? 555 HOH A O   1 
HETATM 2332 O  O   . HOH F 6 .   ? -5.966  15.121  11.891  1.00 30.80 ? 556 HOH A O   1 
HETATM 2333 O  O   . HOH F 6 .   ? -5.979  17.342  27.144  1.00 29.40 ? 557 HOH A O   1 
HETATM 2334 O  O   . HOH F 6 .   ? -1.371  11.181  25.950  1.00 25.48 ? 558 HOH A O   1 
HETATM 2335 O  O   . HOH F 6 .   ? 5.639   9.027   21.685  1.00 26.93 ? 559 HOH A O   1 
HETATM 2336 O  O   . HOH F 6 .   ? 1.688   12.184  23.019  1.00 30.53 ? 560 HOH A O   1 
HETATM 2337 O  O   . HOH F 6 .   ? -16.661 -18.072 20.161  1.00 34.12 ? 561 HOH A O   1 
HETATM 2338 O  O   . HOH F 6 .   ? -17.367 -23.035 4.027   1.00 23.22 ? 562 HOH A O   1 
HETATM 2339 O  O   . HOH F 6 .   ? -18.385 -3.791  -2.615  1.00 26.97 ? 563 HOH A O   1 
HETATM 2340 O  O   . HOH F 6 .   ? -12.770 -8.987  -3.097  1.00 26.87 ? 564 HOH A O   1 
HETATM 2341 O  O   . HOH F 6 .   ? 3.156   1.621   -1.966  1.00 37.81 ? 565 HOH A O   1 
HETATM 2342 O  O   . HOH F 6 .   ? -27.071 -12.783 20.293  1.00 33.29 ? 566 HOH A O   1 
HETATM 2343 O  O   . HOH F 6 .   ? -3.544  -12.948 -2.823  1.00 26.50 ? 567 HOH A O   1 
HETATM 2344 O  O   . HOH F 6 .   ? 7.815   -4.556  -0.281  1.00 37.25 ? 568 HOH A O   1 
HETATM 2345 O  O   . HOH F 6 .   ? 2.862   -13.302 8.045   1.00 31.63 ? 569 HOH A O   1 
HETATM 2346 O  O   . HOH F 6 .   ? 1.293   -6.490  34.467  1.00 22.43 ? 570 HOH A O   1 
HETATM 2347 O  O   . HOH F 6 .   ? -1.140  -6.243  36.167  1.00 31.97 ? 571 HOH A O   1 
HETATM 2348 O  O   . HOH F 6 .   ? -4.848  0.830   9.875   1.00 15.07 ? 572 HOH A O   1 
HETATM 2349 O  O   . HOH F 6 .   ? -3.804  -0.932  11.571  1.00 20.64 ? 573 HOH A O   1 
HETATM 2350 O  O   . HOH F 6 .   ? -4.286  4.013   10.269  1.00 25.89 ? 574 HOH A O   1 
HETATM 2351 O  O   . HOH F 6 .   ? -1.760  3.035   11.438  1.00 32.38 ? 575 HOH A O   1 
HETATM 2352 O  O   . HOH F 6 .   ? 3.740   9.663   23.719  1.00 25.44 ? 576 HOH A O   1 
HETATM 2353 O  O   . HOH F 6 .   ? 6.538   5.201   28.508  1.00 26.88 ? 577 HOH A O   1 
HETATM 2354 O  O   . HOH F 6 .   ? 10.552  -2.713  13.471  1.00 37.68 ? 578 HOH A O   1 
HETATM 2355 O  O   . HOH F 6 .   ? -1.010  -11.209 28.896  1.00 16.92 ? 579 HOH A O   1 
HETATM 2356 O  O   . HOH F 6 .   ? 0.423   -19.352 10.707  1.00 29.97 ? 580 HOH A O   1 
HETATM 2357 O  O   . HOH F 6 .   ? 15.162  3.377   20.969  1.00 34.59 ? 581 HOH A O   1 
HETATM 2358 O  O   . HOH F 6 .   ? -17.823 -12.235 31.684  1.00 32.20 ? 582 HOH A O   1 
HETATM 2359 O  O   . HOH F 6 .   ? -8.284  -17.229 34.866  1.00 26.25 ? 583 HOH A O   1 
HETATM 2360 O  O   . HOH F 6 .   ? -23.609 -0.235  31.647  1.00 32.33 ? 584 HOH A O   1 
HETATM 2361 O  O   . HOH F 6 .   ? -28.022 -1.384  28.335  1.00 32.76 ? 585 HOH A O   1 
HETATM 2362 O  O   . HOH F 6 .   ? -29.790 4.068   27.266  1.00 30.35 ? 586 HOH A O   1 
HETATM 2363 O  O   . HOH F 6 .   ? -12.216 9.464   3.201   1.00 27.39 ? 587 HOH A O   1 
HETATM 2364 O  O   . HOH F 6 .   ? -3.633  4.880   6.880   1.00 34.03 ? 588 HOH A O   1 
HETATM 2365 O  O   . HOH F 6 .   ? 6.013   0.761   8.429   1.00 37.49 ? 589 HOH A O   1 
HETATM 2366 O  O   . HOH F 6 .   ? -11.073 17.116  12.065  1.00 26.87 ? 590 HOH A O   1 
HETATM 2367 O  O   . HOH F 6 .   ? -21.058 18.786  13.786  1.00 27.37 ? 591 HOH A O   1 
HETATM 2368 O  O   . HOH F 6 .   ? -25.840 7.988   6.310   1.00 33.84 ? 592 HOH A O   1 
HETATM 2369 O  O   . HOH F 6 .   ? -25.204 11.160  19.586  1.00 43.23 ? 593 HOH A O   1 
HETATM 2370 O  O   . HOH F 6 .   ? -14.988 9.143   31.358  1.00 32.40 ? 594 HOH A O   1 
HETATM 2371 O  O   . HOH F 6 .   ? -2.718  -17.724 5.435   1.00 31.45 ? 595 HOH A O   1 
HETATM 2372 O  O   . HOH F 6 .   ? 1.680   -17.524 7.123   1.00 29.44 ? 596 HOH A O   1 
HETATM 2373 O  O   . HOH F 6 .   ? -12.733 -22.034 8.414   1.00 31.89 ? 597 HOH A O   1 
HETATM 2374 O  O   . HOH F 6 .   ? -12.374 -18.452 32.194  1.00 29.53 ? 598 HOH A O   1 
HETATM 2375 O  O   . HOH F 6 .   ? -4.447  -17.233 32.782  1.00 40.38 ? 599 HOH A O   1 
HETATM 2376 O  O   . HOH F 6 .   ? -0.260  13.944  16.228  1.00 27.68 ? 600 HOH A O   1 
HETATM 2377 O  O   . HOH F 6 .   ? -6.394  12.207  10.163  1.00 36.58 ? 601 HOH A O   1 
HETATM 2378 O  O   . HOH F 6 .   ? -8.958  18.936  28.368  1.00 28.07 ? 602 HOH A O   1 
HETATM 2379 O  O   . HOH F 6 .   ? -7.924  7.133   27.594  1.00 29.87 ? 603 HOH A O   1 
HETATM 2380 O  O   . HOH F 6 .   ? -21.728 -14.311 18.324  1.00 32.58 ? 604 HOH A O   1 
HETATM 2381 O  O   . HOH F 6 .   ? -18.619 -20.622 14.850  1.00 33.71 ? 605 HOH A O   1 
HETATM 2382 O  O   . HOH F 6 .   ? -24.409 -17.604 6.859   1.00 29.45 ? 606 HOH A O   1 
HETATM 2383 O  O   . HOH F 6 .   ? -21.017 -19.499 6.523   1.00 28.46 ? 607 HOH A O   1 
HETATM 2384 O  O   . HOH F 6 .   ? -23.595 -3.405  3.961   1.00 35.98 ? 608 HOH A O   1 
HETATM 2385 O  O   . HOH F 6 .   ? -24.077 -0.171  1.053   1.00 32.42 ? 609 HOH A O   1 
HETATM 2386 O  O   . HOH F 6 .   ? -15.604 -10.209 -4.719  1.00 31.42 ? 610 HOH A O   1 
HETATM 2387 O  O   . HOH F 6 .   ? -14.065 -4.908  -6.407  1.00 25.13 ? 611 HOH A O   1 
HETATM 2388 O  O   . HOH F 6 .   ? -16.744 -5.179  -5.887  1.00 36.11 ? 612 HOH A O   1 
HETATM 2389 O  O   . HOH F 6 .   ? -3.036  6.233   -1.185  1.00 30.81 ? 613 HOH A O   1 
HETATM 2390 O  O   . HOH F 6 .   ? -26.097 -7.336  30.439  1.00 28.71 ? 614 HOH A O   1 
HETATM 2391 O  O   . HOH F 6 .   ? 7.670   -7.500  -0.848  1.00 28.21 ? 615 HOH A O   1 
HETATM 2392 O  O   . HOH F 6 .   ? 4.175   -11.505 23.653  1.00 37.82 ? 616 HOH A O   1 
HETATM 2393 O  O   . HOH F 6 .   ? 1.810   -9.957  31.036  1.00 31.33 ? 617 HOH A O   1 
HETATM 2394 O  O   . HOH F 6 .   ? 3.190   -9.728  29.252  1.00 32.31 ? 618 HOH A O   1 
HETATM 2395 O  O   . HOH F 6 .   ? 9.959   -13.312 9.424   1.00 42.49 ? 619 HOH A O   1 
HETATM 2396 O  O   . HOH F 6 .   ? -7.967  -22.231 10.414  1.00 19.56 ? 620 HOH A O   1 
HETATM 2397 O  O   . HOH F 6 .   ? -23.788 -6.978  0.251   1.00 27.89 ? 621 HOH A O   1 
HETATM 2398 O  O   . HOH F 6 .   ? -20.984 -6.908  -1.741  1.00 29.46 ? 622 HOH A O   1 
HETATM 2399 O  O   . HOH F 6 .   ? 0.402   1.035   34.416  1.00 25.40 ? 623 HOH A O   1 
HETATM 2400 O  O   . HOH F 6 .   ? -11.780 10.765  0.873   1.00 28.92 ? 624 HOH A O   1 
HETATM 2401 O  O   . HOH F 6 .   ? -12.089 10.670  5.814   1.00 23.56 ? 625 HOH A O   1 
HETATM 2402 O  O   . HOH F 6 .   ? -12.943 -19.438 25.997  1.00 23.48 ? 626 HOH A O   1 
HETATM 2403 O  O   . HOH F 6 .   ? -17.002 -7.386  39.588  1.00 29.45 ? 627 HOH A O   1 
HETATM 2404 O  O   . HOH F 6 .   ? -19.926 -15.527 22.335  1.00 29.72 ? 628 HOH A O   1 
HETATM 2405 O  O   . HOH F 6 .   ? -6.343  -19.468 5.206   1.00 32.74 ? 629 HOH A O   1 
HETATM 2406 O  O   . HOH F 6 .   ? -15.067 -10.341 36.983  1.00 34.71 ? 630 HOH A O   1 
HETATM 2407 O  O   . HOH F 6 .   ? -16.727 -14.704 28.572  1.00 34.85 ? 631 HOH A O   1 
HETATM 2408 O  O   . HOH F 6 .   ? -15.163 -19.989 23.124  1.00 33.77 ? 632 HOH A O   1 
HETATM 2409 O  O   . HOH F 6 .   ? 2.974   11.053  16.755  1.00 41.15 ? 633 HOH A O   1 
HETATM 2410 O  O   . HOH F 6 .   ? 1.716   -4.393  -12.174 1.00 30.66 ? 634 HOH A O   1 
HETATM 2411 O  O   . HOH F 6 .   ? -0.174  -7.046  -7.143  1.00 39.48 ? 635 HOH A O   1 
HETATM 2412 O  O   . HOH F 6 .   ? 6.083   -10.722 14.092  1.00 49.00 ? 636 HOH A O   1 
HETATM 2413 O  O   . HOH F 6 .   ? 6.536   -5.292  27.330  1.00 30.27 ? 637 HOH A O   1 
HETATM 2414 O  O   . HOH F 6 .   ? 9.366   7.409   18.447  1.00 39.70 ? 638 HOH A O   1 
HETATM 2415 O  O   . HOH F 6 .   ? -18.091 6.083   33.768  1.00 29.95 ? 639 HOH A O   1 
HETATM 2416 O  O   . HOH F 6 .   ? -12.312 12.764  28.983  1.00 26.06 ? 640 HOH A O   1 
HETATM 2417 O  O   . HOH F 6 .   ? -10.657 8.834   7.598   1.00 28.88 ? 641 HOH A O   1 
HETATM 2418 O  O   . HOH F 6 .   ? -24.149 -14.130 19.497  1.00 31.18 ? 642 HOH A O   1 
HETATM 2419 O  O   . HOH F 6 .   ? 8.697   -11.242 6.678   1.00 38.90 ? 643 HOH A O   1 
HETATM 2420 O  O   . HOH F 6 .   ? 11.750  0.798   28.468  1.00 32.26 ? 644 HOH A O   1 
HETATM 2421 O  O   . HOH F 6 .   ? 7.209   -3.570  29.773  1.00 39.11 ? 645 HOH A O   1 
HETATM 2422 O  O   . HOH F 6 .   ? -27.909 5.690   19.024  1.00 33.47 ? 646 HOH A O   1 
HETATM 2423 O  O   . HOH F 6 .   ? -18.819 14.178  2.666   1.00 45.37 ? 647 HOH A O   1 
HETATM 2424 O  O   . HOH F 6 .   ? -20.024 17.930  3.874   1.00 35.48 ? 648 HOH A O   1 
HETATM 2425 O  O   . HOH F 6 .   ? -20.682 5.719   32.489  1.00 30.62 ? 649 HOH A O   1 
HETATM 2426 O  O   . HOH F 6 .   ? -3.221  17.656  21.501  1.00 29.98 ? 650 HOH A O   1 
HETATM 2427 O  O   . HOH F 6 .   ? 4.124   -2.850  4.097   1.00 40.00 ? 651 HOH A O   1 
HETATM 2428 O  O   . HOH F 6 .   ? -27.033 -7.929  26.403  1.00 42.31 ? 652 HOH A O   1 
HETATM 2429 O  O   . HOH F 6 .   ? -7.067  1.570   35.147  1.00 35.54 ? 653 HOH A O   1 
HETATM 2430 O  O   . HOH F 6 .   ? -19.566 -14.964 25.776  1.00 37.47 ? 654 HOH A O   1 
HETATM 2431 O  O   . HOH F 6 .   ? 3.659   -13.738 12.414  1.00 32.13 ? 655 HOH A O   1 
HETATM 2432 O  O   . HOH F 6 .   ? 2.901   -2.200  37.122  1.00 38.09 ? 656 HOH A O   1 
HETATM 2433 O  O   . HOH F 6 .   ? 12.136  -6.702  7.967   1.00 28.99 ? 657 HOH A O   1 
HETATM 2434 O  O   . HOH F 6 .   ? -23.093 -21.244 11.966  1.00 35.66 ? 658 HOH A O   1 
HETATM 2435 O  O   . HOH F 6 .   ? 10.684  -9.140  9.189   1.00 36.12 ? 659 HOH A O   1 
HETATM 2436 O  O   . HOH F 6 .   ? 3.542   -8.995  25.589  1.00 32.94 ? 660 HOH A O   1 
HETATM 2437 O  O   . HOH F 6 .   ? -6.905  -15.668 38.646  1.00 31.63 ? 661 HOH A O   1 
HETATM 2438 O  O   . HOH F 6 .   ? -15.955 16.638  26.679  1.00 43.47 ? 662 HOH A O   1 
HETATM 2439 O  O   . HOH F 6 .   ? 1.163   14.881  24.264  1.00 30.99 ? 663 HOH A O   1 
HETATM 2440 O  O   . HOH F 6 .   ? -13.541 -0.908  -6.254  1.00 32.94 ? 664 HOH A O   1 
HETATM 2441 O  O   . HOH F 6 .   ? -3.908  0.714   13.752  1.00 13.87 ? 665 HOH A O   1 
HETATM 2442 O  O   . HOH F 6 .   ? -5.018  2.485   12.129  1.00 25.83 ? 666 HOH A O   1 
HETATM 2443 O  O   . HOH F 6 .   ? -6.424  7.011   11.344  1.00 41.22 ? 667 HOH A O   1 
HETATM 2444 O  O   . HOH F 6 .   ? -8.307  7.745   8.359   1.00 33.04 ? 668 HOH A O   1 
HETATM 2445 O  O   . HOH F 6 .   ? -11.201 1.022   -7.718  1.00 30.00 ? 669 HOH A O   1 
HETATM 2446 O  O   . HOH F 6 .   ? -6.276  -5.164  37.604  1.00 30.00 ? 670 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 MES 1   302 1   MES MES A . 
D 4 DMS 1   303 2   DMS DMS A . 
E 5 V50 1   304 1   V50 V50 A . 
F 6 HOH 1   401 1   HOH HOH A . 
F 6 HOH 2   402 2   HOH HOH A . 
F 6 HOH 3   403 3   HOH HOH A . 
F 6 HOH 4   404 4   HOH HOH A . 
F 6 HOH 5   405 5   HOH HOH A . 
F 6 HOH 6   406 6   HOH HOH A . 
F 6 HOH 7   407 7   HOH HOH A . 
F 6 HOH 8   408 8   HOH HOH A . 
F 6 HOH 9   409 9   HOH HOH A . 
F 6 HOH 10  410 10  HOH HOH A . 
F 6 HOH 11  411 11  HOH HOH A . 
F 6 HOH 12  412 12  HOH HOH A . 
F 6 HOH 13  413 13  HOH HOH A . 
F 6 HOH 14  414 14  HOH HOH A . 
F 6 HOH 15  415 15  HOH HOH A . 
F 6 HOH 16  416 16  HOH HOH A . 
F 6 HOH 17  417 17  HOH HOH A . 
F 6 HOH 18  418 18  HOH HOH A . 
F 6 HOH 19  419 19  HOH HOH A . 
F 6 HOH 20  420 20  HOH HOH A . 
F 6 HOH 21  421 21  HOH HOH A . 
F 6 HOH 22  422 22  HOH HOH A . 
F 6 HOH 23  423 23  HOH HOH A . 
F 6 HOH 24  424 24  HOH HOH A . 
F 6 HOH 25  425 25  HOH HOH A . 
F 6 HOH 26  426 26  HOH HOH A . 
F 6 HOH 27  427 27  HOH HOH A . 
F 6 HOH 28  428 28  HOH HOH A . 
F 6 HOH 29  429 29  HOH HOH A . 
F 6 HOH 30  430 30  HOH HOH A . 
F 6 HOH 31  431 31  HOH HOH A . 
F 6 HOH 32  432 32  HOH HOH A . 
F 6 HOH 33  433 33  HOH HOH A . 
F 6 HOH 34  434 34  HOH HOH A . 
F 6 HOH 35  435 35  HOH HOH A . 
F 6 HOH 36  436 36  HOH HOH A . 
F 6 HOH 37  437 37  HOH HOH A . 
F 6 HOH 38  438 38  HOH HOH A . 
F 6 HOH 39  439 39  HOH HOH A . 
F 6 HOH 40  440 40  HOH HOH A . 
F 6 HOH 41  441 41  HOH HOH A . 
F 6 HOH 42  442 42  HOH HOH A . 
F 6 HOH 43  443 43  HOH HOH A . 
F 6 HOH 44  444 44  HOH HOH A . 
F 6 HOH 45  445 45  HOH HOH A . 
F 6 HOH 46  446 46  HOH HOH A . 
F 6 HOH 47  447 47  HOH HOH A . 
F 6 HOH 48  448 48  HOH HOH A . 
F 6 HOH 49  449 49  HOH HOH A . 
F 6 HOH 50  450 50  HOH HOH A . 
F 6 HOH 51  451 51  HOH HOH A . 
F 6 HOH 52  452 52  HOH HOH A . 
F 6 HOH 53  453 53  HOH HOH A . 
F 6 HOH 54  454 54  HOH HOH A . 
F 6 HOH 55  455 55  HOH HOH A . 
F 6 HOH 56  456 56  HOH HOH A . 
F 6 HOH 57  457 57  HOH HOH A . 
F 6 HOH 58  458 58  HOH HOH A . 
F 6 HOH 59  459 59  HOH HOH A . 
F 6 HOH 60  460 60  HOH HOH A . 
F 6 HOH 61  461 61  HOH HOH A . 
F 6 HOH 62  462 62  HOH HOH A . 
F 6 HOH 63  463 63  HOH HOH A . 
F 6 HOH 64  464 64  HOH HOH A . 
F 6 HOH 65  465 65  HOH HOH A . 
F 6 HOH 66  466 66  HOH HOH A . 
F 6 HOH 67  467 67  HOH HOH A . 
F 6 HOH 68  468 68  HOH HOH A . 
F 6 HOH 69  469 69  HOH HOH A . 
F 6 HOH 70  470 70  HOH HOH A . 
F 6 HOH 71  471 71  HOH HOH A . 
F 6 HOH 72  472 72  HOH HOH A . 
F 6 HOH 73  473 73  HOH HOH A . 
F 6 HOH 74  474 74  HOH HOH A . 
F 6 HOH 75  475 75  HOH HOH A . 
F 6 HOH 76  476 76  HOH HOH A . 
F 6 HOH 77  477 77  HOH HOH A . 
F 6 HOH 78  478 78  HOH HOH A . 
F 6 HOH 79  479 79  HOH HOH A . 
F 6 HOH 80  480 80  HOH HOH A . 
F 6 HOH 81  481 81  HOH HOH A . 
F 6 HOH 82  482 82  HOH HOH A . 
F 6 HOH 83  483 83  HOH HOH A . 
F 6 HOH 84  484 84  HOH HOH A . 
F 6 HOH 85  485 85  HOH HOH A . 
F 6 HOH 86  486 86  HOH HOH A . 
F 6 HOH 87  487 87  HOH HOH A . 
F 6 HOH 88  488 88  HOH HOH A . 
F 6 HOH 89  489 89  HOH HOH A . 
F 6 HOH 90  490 90  HOH HOH A . 
F 6 HOH 91  491 91  HOH HOH A . 
F 6 HOH 92  492 92  HOH HOH A . 
F 6 HOH 93  493 93  HOH HOH A . 
F 6 HOH 94  494 94  HOH HOH A . 
F 6 HOH 95  495 95  HOH HOH A . 
F 6 HOH 96  496 96  HOH HOH A . 
F 6 HOH 97  497 97  HOH HOH A . 
F 6 HOH 98  498 98  HOH HOH A . 
F 6 HOH 99  499 99  HOH HOH A . 
F 6 HOH 100 500 100 HOH HOH A . 
F 6 HOH 101 501 101 HOH HOH A . 
F 6 HOH 102 502 102 HOH HOH A . 
F 6 HOH 103 503 103 HOH HOH A . 
F 6 HOH 104 504 104 HOH HOH A . 
F 6 HOH 105 505 105 HOH HOH A . 
F 6 HOH 106 506 106 HOH HOH A . 
F 6 HOH 107 507 107 HOH HOH A . 
F 6 HOH 108 508 108 HOH HOH A . 
F 6 HOH 109 509 109 HOH HOH A . 
F 6 HOH 110 510 110 HOH HOH A . 
F 6 HOH 111 511 111 HOH HOH A . 
F 6 HOH 112 512 112 HOH HOH A . 
F 6 HOH 113 513 113 HOH HOH A . 
F 6 HOH 114 514 114 HOH HOH A . 
F 6 HOH 115 515 115 HOH HOH A . 
F 6 HOH 116 516 116 HOH HOH A . 
F 6 HOH 117 517 117 HOH HOH A . 
F 6 HOH 118 518 118 HOH HOH A . 
F 6 HOH 119 519 119 HOH HOH A . 
F 6 HOH 120 520 120 HOH HOH A . 
F 6 HOH 121 521 121 HOH HOH A . 
F 6 HOH 122 522 122 HOH HOH A . 
F 6 HOH 123 523 123 HOH HOH A . 
F 6 HOH 124 524 124 HOH HOH A . 
F 6 HOH 125 525 125 HOH HOH A . 
F 6 HOH 126 526 126 HOH HOH A . 
F 6 HOH 127 527 127 HOH HOH A . 
F 6 HOH 128 528 128 HOH HOH A . 
F 6 HOH 129 529 129 HOH HOH A . 
F 6 HOH 130 530 130 HOH HOH A . 
F 6 HOH 131 531 131 HOH HOH A . 
F 6 HOH 132 532 132 HOH HOH A . 
F 6 HOH 133 533 133 HOH HOH A . 
F 6 HOH 134 534 134 HOH HOH A . 
F 6 HOH 135 535 135 HOH HOH A . 
F 6 HOH 136 536 136 HOH HOH A . 
F 6 HOH 137 537 137 HOH HOH A . 
F 6 HOH 138 538 138 HOH HOH A . 
F 6 HOH 139 539 139 HOH HOH A . 
F 6 HOH 140 540 140 HOH HOH A . 
F 6 HOH 141 541 141 HOH HOH A . 
F 6 HOH 142 542 142 HOH HOH A . 
F 6 HOH 143 543 143 HOH HOH A . 
F 6 HOH 144 544 144 HOH HOH A . 
F 6 HOH 145 545 145 HOH HOH A . 
F 6 HOH 146 546 146 HOH HOH A . 
F 6 HOH 147 547 147 HOH HOH A . 
F 6 HOH 148 548 148 HOH HOH A . 
F 6 HOH 149 549 149 HOH HOH A . 
F 6 HOH 150 550 150 HOH HOH A . 
F 6 HOH 151 551 151 HOH HOH A . 
F 6 HOH 152 552 152 HOH HOH A . 
F 6 HOH 153 553 153 HOH HOH A . 
F 6 HOH 154 554 154 HOH HOH A . 
F 6 HOH 155 555 155 HOH HOH A . 
F 6 HOH 156 556 156 HOH HOH A . 
F 6 HOH 157 557 157 HOH HOH A . 
F 6 HOH 158 558 158 HOH HOH A . 
F 6 HOH 159 559 159 HOH HOH A . 
F 6 HOH 160 560 160 HOH HOH A . 
F 6 HOH 161 561 161 HOH HOH A . 
F 6 HOH 162 562 162 HOH HOH A . 
F 6 HOH 163 563 163 HOH HOH A . 
F 6 HOH 164 564 164 HOH HOH A . 
F 6 HOH 165 565 165 HOH HOH A . 
F 6 HOH 166 566 166 HOH HOH A . 
F 6 HOH 167 567 167 HOH HOH A . 
F 6 HOH 168 568 168 HOH HOH A . 
F 6 HOH 169 569 169 HOH HOH A . 
F 6 HOH 170 570 170 HOH HOH A . 
F 6 HOH 171 571 171 HOH HOH A . 
F 6 HOH 172 572 172 HOH HOH A . 
F 6 HOH 173 573 173 HOH HOH A . 
F 6 HOH 174 574 174 HOH HOH A . 
F 6 HOH 175 575 175 HOH HOH A . 
F 6 HOH 176 576 176 HOH HOH A . 
F 6 HOH 177 577 177 HOH HOH A . 
F 6 HOH 178 578 178 HOH HOH A . 
F 6 HOH 179 579 179 HOH HOH A . 
F 6 HOH 180 580 180 HOH HOH A . 
F 6 HOH 181 581 181 HOH HOH A . 
F 6 HOH 182 582 182 HOH HOH A . 
F 6 HOH 183 583 183 HOH HOH A . 
F 6 HOH 184 584 184 HOH HOH A . 
F 6 HOH 185 585 185 HOH HOH A . 
F 6 HOH 186 586 186 HOH HOH A . 
F 6 HOH 187 587 187 HOH HOH A . 
F 6 HOH 188 588 188 HOH HOH A . 
F 6 HOH 189 589 189 HOH HOH A . 
F 6 HOH 190 590 190 HOH HOH A . 
F 6 HOH 191 591 191 HOH HOH A . 
F 6 HOH 192 592 192 HOH HOH A . 
F 6 HOH 193 593 193 HOH HOH A . 
F 6 HOH 194 594 194 HOH HOH A . 
F 6 HOH 195 595 195 HOH HOH A . 
F 6 HOH 196 596 196 HOH HOH A . 
F 6 HOH 197 597 197 HOH HOH A . 
F 6 HOH 198 598 198 HOH HOH A . 
F 6 HOH 199 599 199 HOH HOH A . 
F 6 HOH 200 600 200 HOH HOH A . 
F 6 HOH 201 601 201 HOH HOH A . 
F 6 HOH 202 602 202 HOH HOH A . 
F 6 HOH 203 603 203 HOH HOH A . 
F 6 HOH 204 604 204 HOH HOH A . 
F 6 HOH 205 605 205 HOH HOH A . 
F 6 HOH 206 606 206 HOH HOH A . 
F 6 HOH 207 607 207 HOH HOH A . 
F 6 HOH 208 608 208 HOH HOH A . 
F 6 HOH 209 609 209 HOH HOH A . 
F 6 HOH 210 610 210 HOH HOH A . 
F 6 HOH 211 611 211 HOH HOH A . 
F 6 HOH 212 612 212 HOH HOH A . 
F 6 HOH 213 613 213 HOH HOH A . 
F 6 HOH 214 614 214 HOH HOH A . 
F 6 HOH 215 615 215 HOH HOH A . 
F 6 HOH 216 616 216 HOH HOH A . 
F 6 HOH 217 617 217 HOH HOH A . 
F 6 HOH 218 618 218 HOH HOH A . 
F 6 HOH 219 619 219 HOH HOH A . 
F 6 HOH 220 620 220 HOH HOH A . 
F 6 HOH 221 621 221 HOH HOH A . 
F 6 HOH 222 622 222 HOH HOH A . 
F 6 HOH 223 623 223 HOH HOH A . 
F 6 HOH 224 624 224 HOH HOH A . 
F 6 HOH 225 625 225 HOH HOH A . 
F 6 HOH 226 626 226 HOH HOH A . 
F 6 HOH 227 627 227 HOH HOH A . 
F 6 HOH 228 628 228 HOH HOH A . 
F 6 HOH 229 629 229 HOH HOH A . 
F 6 HOH 230 630 230 HOH HOH A . 
F 6 HOH 231 631 231 HOH HOH A . 
F 6 HOH 232 632 232 HOH HOH A . 
F 6 HOH 233 633 233 HOH HOH A . 
F 6 HOH 234 634 234 HOH HOH A . 
F 6 HOH 235 635 235 HOH HOH A . 
F 6 HOH 236 636 236 HOH HOH A . 
F 6 HOH 237 637 237 HOH HOH A . 
F 6 HOH 238 638 238 HOH HOH A . 
F 6 HOH 239 639 239 HOH HOH A . 
F 6 HOH 240 640 240 HOH HOH A . 
F 6 HOH 241 641 241 HOH HOH A . 
F 6 HOH 242 642 242 HOH HOH A . 
F 6 HOH 243 643 243 HOH HOH A . 
F 6 HOH 244 644 244 HOH HOH A . 
F 6 HOH 245 645 245 HOH HOH A . 
F 6 HOH 246 646 246 HOH HOH A . 
F 6 HOH 247 647 247 HOH HOH A . 
F 6 HOH 248 648 248 HOH HOH A . 
F 6 HOH 249 649 249 HOH HOH A . 
F 6 HOH 250 650 250 HOH HOH A . 
F 6 HOH 251 651 251 HOH HOH A . 
F 6 HOH 252 652 252 HOH HOH A . 
F 6 HOH 253 653 253 HOH HOH A . 
F 6 HOH 254 654 254 HOH HOH A . 
F 6 HOH 255 655 255 HOH HOH A . 
F 6 HOH 256 656 256 HOH HOH A . 
F 6 HOH 257 657 257 HOH HOH A . 
F 6 HOH 258 658 258 HOH HOH A . 
F 6 HOH 259 659 259 HOH HOH A . 
F 6 HOH 260 660 260 HOH HOH A . 
F 6 HOH 261 661 261 HOH HOH A . 
F 6 HOH 262 662 262 HOH HOH A . 
F 6 HOH 263 663 263 HOH HOH A . 
F 6 HOH 264 664 264 HOH HOH A . 
F 6 HOH 265 665 265 HOH HOH A . 
F 6 HOH 266 666 266 HOH HOH A . 
F 6 HOH 267 667 267 HOH HOH A . 
F 6 HOH 268 668 268 HOH HOH A . 
F 6 HOH 269 669 269 HOH HOH A . 
F 6 HOH 270 670 270 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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 106.8 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 113.5 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.7  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 ? E V50 .   ? A V50 304 ? 1_555 104.5 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 ? E V50 .   ? A V50 304 ? 1_555 118.5 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 ? E V50 .   ? A V50 304 ? 1_555 114.9 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2013-04-10 
2 'Structure model' 1 1 2017-09-27 
3 'Structure model' 1 2 2023-09-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Derived calculations'   
5 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' diffrn_detector               
2 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' database_2                    
5 3 'Structure model' diffrn_source                 
6 3 'Structure model' pdbx_initial_refinement_model 
7 3 'Structure model' pdbx_struct_conn_angle        
8 3 'Structure model' struct_conn                   
9 3 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_diffrn_detector.detector'                   
2  3 'Structure model' '_database_2.pdbx_DOI'                        
3  3 'Structure model' '_database_2.pdbx_database_accession'         
4  3 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
17 3 'Structure model' '_pdbx_struct_conn_angle.value'               
18 3 'Structure model' '_struct_conn.pdbx_dist_value'                
19 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
20 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
21 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
22 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
23 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
24 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
25 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
26 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
27 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
28 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
29 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
30 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
31 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
32 3 '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       3.3.20 2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345dtb   .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            THR 
_pdbx_validate_rmsd_bond.auth_seq_id_1             125 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            N 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             127 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.622 
_pdbx_validate_rmsd_bond.bond_target_value         1.336 
_pdbx_validate_rmsd_bond.bond_deviation            0.286 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.023 
_pdbx_validate_rmsd_bond.linker_flag               Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C  A THR 125 ? ? N  A LYS 127 ? ? CA A LYS 127 ? ? 102.98 121.70 -18.72 2.50 Y 
2 1 CD A LYS 159 ? B CE A LYS 159 ? B NZ A LYS 159 ? B 126.08 111.70 14.38  2.30 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -141.26 15.44   
2 1 ARG A 27  ? ? -141.40 56.72   
3 1 ASN A 244 ? ? -96.12  50.89   
4 1 LYS A 252 ? ? 59.91   -138.45 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    86 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   THR 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    87 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.76 
# 
_pdbx_validate_polymer_linkage.id               1 
_pdbx_validate_polymer_linkage.PDB_model_num    1 
_pdbx_validate_polymer_linkage.auth_atom_id_1   C 
_pdbx_validate_polymer_linkage.auth_asym_id_1   A 
_pdbx_validate_polymer_linkage.auth_comp_id_1   THR 
_pdbx_validate_polymer_linkage.auth_seq_id_1    125 
_pdbx_validate_polymer_linkage.PDB_ins_code_1   ? 
_pdbx_validate_polymer_linkage.label_alt_id_1   ? 
_pdbx_validate_polymer_linkage.auth_atom_id_2   N 
_pdbx_validate_polymer_linkage.auth_asym_id_2   A 
_pdbx_validate_polymer_linkage.auth_comp_id_2   LYS 
_pdbx_validate_polymer_linkage.auth_seq_id_2    127 
_pdbx_validate_polymer_linkage.PDB_ins_code_2   ? 
_pdbx_validate_polymer_linkage.label_alt_id_2   ? 
_pdbx_validate_polymer_linkage.dist             1.62 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 A MES 302 ? S   ? C MES 1 S   
2 1 N 1 A MES 302 ? O1S ? C MES 1 O1S 
3 1 N 1 A MES 302 ? O2S ? C MES 1 O2S 
4 1 N 1 A MES 302 ? O3S ? C MES 1 O3S 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MES O1   O  N N 240 
MES C2   C  N N 241 
MES C3   C  N N 242 
MES N4   N  N N 243 
MES C5   C  N N 244 
MES C6   C  N N 245 
MES C7   C  N N 246 
MES C8   C  N N 247 
MES S    S  N N 248 
MES O1S  O  N N 249 
MES O2S  O  N N 250 
MES O3S  O  N N 251 
MES H21  H  N N 252 
MES H22  H  N N 253 
MES H31  H  N N 254 
MES H32  H  N N 255 
MES HN4  H  N N 256 
MES H51  H  N N 257 
MES H52  H  N N 258 
MES H61  H  N N 259 
MES H62  H  N N 260 
MES H71  H  N N 261 
MES H72  H  N N 262 
MES H81  H  N N 263 
MES H82  H  N N 264 
MET N    N  N N 265 
MET CA   C  N S 266 
MET C    C  N N 267 
MET O    O  N N 268 
MET CB   C  N N 269 
MET CG   C  N N 270 
MET SD   S  N N 271 
MET CE   C  N N 272 
MET OXT  O  N N 273 
MET H    H  N N 274 
MET H2   H  N N 275 
MET HA   H  N N 276 
MET HB2  H  N N 277 
MET HB3  H  N N 278 
MET HG2  H  N N 279 
MET HG3  H  N N 280 
MET HE1  H  N N 281 
MET HE2  H  N N 282 
MET HE3  H  N N 283 
MET HXT  H  N N 284 
PHE N    N  N N 285 
PHE CA   C  N S 286 
PHE C    C  N N 287 
PHE O    O  N N 288 
PHE CB   C  N N 289 
PHE CG   C  Y N 290 
PHE CD1  C  Y N 291 
PHE CD2  C  Y N 292 
PHE CE1  C  Y N 293 
PHE CE2  C  Y N 294 
PHE CZ   C  Y N 295 
PHE OXT  O  N N 296 
PHE H    H  N N 297 
PHE H2   H  N N 298 
PHE HA   H  N N 299 
PHE HB2  H  N N 300 
PHE HB3  H  N N 301 
PHE HD1  H  N N 302 
PHE HD2  H  N N 303 
PHE HE1  H  N N 304 
PHE HE2  H  N N 305 
PHE HZ   H  N N 306 
PHE HXT  H  N N 307 
PRO N    N  N N 308 
PRO CA   C  N S 309 
PRO C    C  N N 310 
PRO O    O  N N 311 
PRO CB   C  N N 312 
PRO CG   C  N N 313 
PRO CD   C  N N 314 
PRO OXT  O  N N 315 
PRO H    H  N N 316 
PRO HA   H  N N 317 
PRO HB2  H  N N 318 
PRO HB3  H  N N 319 
PRO HG2  H  N N 320 
PRO HG3  H  N N 321 
PRO HD2  H  N N 322 
PRO HD3  H  N N 323 
PRO HXT  H  N N 324 
SER N    N  N N 325 
SER CA   C  N S 326 
SER C    C  N N 327 
SER O    O  N N 328 
SER CB   C  N N 329 
SER OG   O  N N 330 
SER OXT  O  N N 331 
SER H    H  N N 332 
SER H2   H  N N 333 
SER HA   H  N N 334 
SER HB2  H  N N 335 
SER HB3  H  N N 336 
SER HG   H  N N 337 
SER HXT  H  N N 338 
THR N    N  N N 339 
THR CA   C  N S 340 
THR C    C  N N 341 
THR O    O  N N 342 
THR CB   C  N R 343 
THR OG1  O  N N 344 
THR CG2  C  N N 345 
THR OXT  O  N N 346 
THR H    H  N N 347 
THR H2   H  N N 348 
THR HA   H  N N 349 
THR HB   H  N N 350 
THR HG1  H  N N 351 
THR HG21 H  N N 352 
THR HG22 H  N N 353 
THR HG23 H  N N 354 
THR HXT  H  N N 355 
TRP N    N  N N 356 
TRP CA   C  N S 357 
TRP C    C  N N 358 
TRP O    O  N N 359 
TRP CB   C  N N 360 
TRP CG   C  Y N 361 
TRP CD1  C  Y N 362 
TRP CD2  C  Y N 363 
TRP NE1  N  Y N 364 
TRP CE2  C  Y N 365 
TRP CE3  C  Y N 366 
TRP CZ2  C  Y N 367 
TRP CZ3  C  Y N 368 
TRP CH2  C  Y N 369 
TRP OXT  O  N N 370 
TRP H    H  N N 371 
TRP H2   H  N N 372 
TRP HA   H  N N 373 
TRP HB2  H  N N 374 
TRP HB3  H  N N 375 
TRP HD1  H  N N 376 
TRP HE1  H  N N 377 
TRP HE3  H  N N 378 
TRP HZ2  H  N N 379 
TRP HZ3  H  N N 380 
TRP HH2  H  N N 381 
TRP HXT  H  N N 382 
TYR N    N  N N 383 
TYR CA   C  N S 384 
TYR C    C  N N 385 
TYR O    O  N N 386 
TYR CB   C  N N 387 
TYR CG   C  Y N 388 
TYR CD1  C  Y N 389 
TYR CD2  C  Y N 390 
TYR CE1  C  Y N 391 
TYR CE2  C  Y N 392 
TYR CZ   C  Y N 393 
TYR OH   O  N N 394 
TYR OXT  O  N N 395 
TYR H    H  N N 396 
TYR H2   H  N N 397 
TYR HA   H  N N 398 
TYR HB2  H  N N 399 
TYR HB3  H  N N 400 
TYR HD1  H  N N 401 
TYR HD2  H  N N 402 
TYR HE1  H  N N 403 
TYR HE2  H  N N 404 
TYR HH   H  N N 405 
TYR HXT  H  N N 406 
V50 F13  F  N N 407 
V50 C4   C  Y N 408 
V50 C5   C  Y N 409 
V50 S7   S  N N 410 
V50 O9   O  N N 411 
V50 N23  N  N N 412 
V50 O8   O  N N 413 
V50 C6   C  Y N 414 
V50 F11  F  N N 415 
V50 C1   C  Y N 416 
V50 F10  F  N N 417 
V50 C3   C  Y N 418 
V50 F12  F  N N 419 
V50 C2   C  Y N 420 
V50 S14  S  N N 421 
V50 C15  C  Y N 422 
V50 N20  N  Y N 423 
V50 C19  C  Y N 424 
V50 C21  C  N N 425 
V50 C18  C  Y N 426 
V50 C17  C  Y N 427 
V50 N16  N  Y N 428 
V50 C22  C  N N 429 
V50 H1   H  N N 430 
V50 H2   H  N N 431 
V50 H3   H  N N 432 
V50 H4   H  N N 433 
V50 H5   H  N N 434 
V50 H6   H  N N 435 
V50 H7   H  N N 436 
V50 H8   H  N N 437 
V50 H9   H  N N 438 
VAL N    N  N N 439 
VAL CA   C  N S 440 
VAL C    C  N N 441 
VAL O    O  N N 442 
VAL CB   C  N N 443 
VAL CG1  C  N N 444 
VAL CG2  C  N N 445 
VAL OXT  O  N N 446 
VAL H    H  N N 447 
VAL H2   H  N N 448 
VAL HA   H  N N 449 
VAL HB   H  N N 450 
VAL HG11 H  N N 451 
VAL HG12 H  N N 452 
VAL HG13 H  N N 453 
VAL HG21 H  N N 454 
VAL HG22 H  N N 455 
VAL HG23 H  N N 456 
VAL HXT  H  N N 457 
ZN  ZN   ZN N N 458 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MES O1  C2   sing N N 227 
MES O1  C6   sing N N 228 
MES C2  C3   sing N N 229 
MES C2  H21  sing N N 230 
MES C2  H22  sing N N 231 
MES C3  N4   sing N N 232 
MES C3  H31  sing N N 233 
MES C3  H32  sing N N 234 
MES N4  C5   sing N N 235 
MES N4  C7   sing N N 236 
MES N4  HN4  sing N N 237 
MES C5  C6   sing N N 238 
MES C5  H51  sing N N 239 
MES C5  H52  sing N N 240 
MES C6  H61  sing N N 241 
MES C6  H62  sing N N 242 
MES C7  C8   sing N N 243 
MES C7  H71  sing N N 244 
MES C7  H72  sing N N 245 
MES C8  S    sing N N 246 
MES C8  H81  sing N N 247 
MES C8  H82  sing N N 248 
MES S   O1S  doub N N 249 
MES S   O2S  doub N N 250 
MES S   O3S  sing N N 251 
MET N   CA   sing N N 252 
MET N   H    sing N N 253 
MET N   H2   sing N N 254 
MET CA  C    sing N N 255 
MET CA  CB   sing N N 256 
MET CA  HA   sing N N 257 
MET C   O    doub N N 258 
MET C   OXT  sing N N 259 
MET CB  CG   sing N N 260 
MET CB  HB2  sing N N 261 
MET CB  HB3  sing N N 262 
MET CG  SD   sing N N 263 
MET CG  HG2  sing N N 264 
MET CG  HG3  sing N N 265 
MET SD  CE   sing N N 266 
MET CE  HE1  sing N N 267 
MET CE  HE2  sing N N 268 
MET CE  HE3  sing N N 269 
MET OXT HXT  sing N N 270 
PHE N   CA   sing N N 271 
PHE N   H    sing N N 272 
PHE N   H2   sing N N 273 
PHE CA  C    sing N N 274 
PHE CA  CB   sing N N 275 
PHE CA  HA   sing N N 276 
PHE C   O    doub N N 277 
PHE C   OXT  sing N N 278 
PHE CB  CG   sing N N 279 
PHE CB  HB2  sing N N 280 
PHE CB  HB3  sing N N 281 
PHE CG  CD1  doub Y N 282 
PHE CG  CD2  sing Y N 283 
PHE CD1 CE1  sing Y N 284 
PHE CD1 HD1  sing N N 285 
PHE CD2 CE2  doub Y N 286 
PHE CD2 HD2  sing N N 287 
PHE CE1 CZ   doub Y N 288 
PHE CE1 HE1  sing N N 289 
PHE CE2 CZ   sing Y N 290 
PHE CE2 HE2  sing N N 291 
PHE CZ  HZ   sing N N 292 
PHE OXT HXT  sing N N 293 
PRO N   CA   sing N N 294 
PRO N   CD   sing N N 295 
PRO N   H    sing N N 296 
PRO CA  C    sing N N 297 
PRO CA  CB   sing N N 298 
PRO CA  HA   sing N N 299 
PRO C   O    doub N N 300 
PRO C   OXT  sing N N 301 
PRO CB  CG   sing N N 302 
PRO CB  HB2  sing N N 303 
PRO CB  HB3  sing N N 304 
PRO CG  CD   sing N N 305 
PRO CG  HG2  sing N N 306 
PRO CG  HG3  sing N N 307 
PRO CD  HD2  sing N N 308 
PRO CD  HD3  sing N N 309 
PRO OXT HXT  sing N N 310 
SER N   CA   sing N N 311 
SER N   H    sing N N 312 
SER N   H2   sing N N 313 
SER CA  C    sing N N 314 
SER CA  CB   sing N N 315 
SER CA  HA   sing N N 316 
SER C   O    doub N N 317 
SER C   OXT  sing N N 318 
SER CB  OG   sing N N 319 
SER CB  HB2  sing N N 320 
SER CB  HB3  sing N N 321 
SER OG  HG   sing N N 322 
SER OXT HXT  sing N N 323 
THR N   CA   sing N N 324 
THR N   H    sing N N 325 
THR N   H2   sing N N 326 
THR CA  C    sing N N 327 
THR CA  CB   sing N N 328 
THR CA  HA   sing N N 329 
THR C   O    doub N N 330 
THR C   OXT  sing N N 331 
THR CB  OG1  sing N N 332 
THR CB  CG2  sing N N 333 
THR CB  HB   sing N N 334 
THR OG1 HG1  sing N N 335 
THR CG2 HG21 sing N N 336 
THR CG2 HG22 sing N N 337 
THR CG2 HG23 sing N N 338 
THR OXT HXT  sing N N 339 
TRP N   CA   sing N N 340 
TRP N   H    sing N N 341 
TRP N   H2   sing N N 342 
TRP CA  C    sing N N 343 
TRP CA  CB   sing N N 344 
TRP CA  HA   sing N N 345 
TRP C   O    doub N N 346 
TRP C   OXT  sing N N 347 
TRP CB  CG   sing N N 348 
TRP CB  HB2  sing N N 349 
TRP CB  HB3  sing N N 350 
TRP CG  CD1  doub Y N 351 
TRP CG  CD2  sing Y N 352 
TRP CD1 NE1  sing Y N 353 
TRP CD1 HD1  sing N N 354 
TRP CD2 CE2  doub Y N 355 
TRP CD2 CE3  sing Y N 356 
TRP NE1 CE2  sing Y N 357 
TRP NE1 HE1  sing N N 358 
TRP CE2 CZ2  sing Y N 359 
TRP CE3 CZ3  doub Y N 360 
TRP CE3 HE3  sing N N 361 
TRP CZ2 CH2  doub Y N 362 
TRP CZ2 HZ2  sing N N 363 
TRP CZ3 CH2  sing Y N 364 
TRP CZ3 HZ3  sing N N 365 
TRP CH2 HH2  sing N N 366 
TRP OXT HXT  sing N N 367 
TYR N   CA   sing N N 368 
TYR N   H    sing N N 369 
TYR N   H2   sing N N 370 
TYR CA  C    sing N N 371 
TYR CA  CB   sing N N 372 
TYR CA  HA   sing N N 373 
TYR C   O    doub N N 374 
TYR C   OXT  sing N N 375 
TYR CB  CG   sing N N 376 
TYR CB  HB2  sing N N 377 
TYR CB  HB3  sing N N 378 
TYR CG  CD1  doub Y N 379 
TYR CG  CD2  sing Y N 380 
TYR CD1 CE1  sing Y N 381 
TYR CD1 HD1  sing N N 382 
TYR CD2 CE2  doub Y N 383 
TYR CD2 HD2  sing N N 384 
TYR CE1 CZ   doub Y N 385 
TYR CE1 HE1  sing N N 386 
TYR CE2 CZ   sing Y N 387 
TYR CE2 HE2  sing N N 388 
TYR CZ  OH   sing N N 389 
TYR OH  HH   sing N N 390 
TYR OXT HXT  sing N N 391 
V50 C21 C19  sing N N 392 
V50 C19 N20  doub Y N 393 
V50 C19 C18  sing Y N 394 
V50 N20 C15  sing Y N 395 
V50 C18 C17  doub Y N 396 
V50 S14 C15  sing N N 397 
V50 S14 C2   sing N N 398 
V50 C15 N16  doub Y N 399 
V50 F10 C1   sing N N 400 
V50 C17 N16  sing Y N 401 
V50 C17 C22  sing N N 402 
V50 C1  C2   doub Y N 403 
V50 C1  C6   sing Y N 404 
V50 C2  C3   sing Y N 405 
V50 F12 C3   sing N N 406 
V50 C3  C4   doub Y N 407 
V50 C6  F11  sing N N 408 
V50 C6  C5   doub Y N 409 
V50 C4  C5   sing Y N 410 
V50 C4  F13  sing N N 411 
V50 C5  S7   sing N N 412 
V50 N23 S7   sing N N 413 
V50 O8  S7   doub N N 414 
V50 S7  O9   doub N N 415 
V50 N23 H1   sing N N 416 
V50 N23 H2   sing N N 417 
V50 C21 H3   sing N N 418 
V50 C21 H4   sing N N 419 
V50 C21 H5   sing N N 420 
V50 C18 H6   sing N N 421 
V50 C22 H7   sing N N 422 
V50 C22 H8   sing N N 423 
V50 C22 H9   sing N N 424 
VAL N   CA   sing N N 425 
VAL N   H    sing N N 426 
VAL N   H2   sing N N 427 
VAL CA  C    sing N N 428 
VAL CA  CB   sing N N 429 
VAL CA  HA   sing N N 430 
VAL C   O    doub N N 431 
VAL C   OXT  sing N N 432 
VAL CB  CG1  sing N N 433 
VAL CB  CG2  sing N N 434 
VAL CB  HB   sing N N 435 
VAL CG1 HG11 sing N N 436 
VAL CG1 HG12 sing N N 437 
VAL CG1 HG13 sing N N 438 
VAL CG2 HG21 sing N N 439 
VAL CG2 HG22 sing N N 440 
VAL CG2 HG23 sing N N 441 
VAL OXT HXT  sing N N 442 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                   ZN  
3 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                       MES 
4 'DIMETHYL SULFOXIDE'                                                         DMS 
5 '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' V50 
6 water                                                                        HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HLJ 
_pdbx_initial_refinement_model.details          'PDB ENTRY 3HLJ' 
# 
