data_3MHI
# 
_entry.id   3MHI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.380 
_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   3MHI         pdb_00003mhi 10.2210/pdb3mhi/pdb 
RCSB  RCSB058552   ?            ?                   
WWPDB D_1000058552 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3M2N 'The same protein with other ligand' unspecified 
PDB 3M3X 'The same protein with other ligand' unspecified 
PDB 3M5E 'The same protein with other ligand' unspecified 
PDB 3M40 'The same protein with other ligand' unspecified 
PDB 3MHL 'The same protein with other ligand' unspecified 
PDB 3MHM 'The same protein with other ligand' unspecified 
PDB 3MHO 'The same protein with other ligand' unspecified 
# 
_pdbx_database_status.entry_id                        3MHI 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2010-04-08 
_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.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'  1 
'Manakova, E.'  2 
'Golovenko, D.' 3 
# 
_citation.id                        primary 
_citation.title                     
'4-[N-(Substituted 4-pyrimidinyl)amino]benzenesulfonamides as inhibitors of carbonic anhydrase isozymes I, II, VII, and XIII' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            18 
_citation.page_first                7413 
_citation.page_last                 7421 
_citation.year                      2010 
_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   20889345 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2010.09.011 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sudzius, J.'       1  ? 
primary 'Baranauskiene, L.' 2  ? 
primary 'Golovenko, D.'     3  ? 
primary 'Matuliene, J.'     4  ? 
primary 'Michailoviene, V.' 5  ? 
primary 'Torresan, J.'      6  ? 
primary 'Jachno, J.'        7  ? 
primary 'Sukackaite, R.'    8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Tumkevicius, S.'   11 ? 
primary 'Matulis, D.'       12 ? 
# 
_cell.entry_id           3MHI 
_cell.length_a           42.242 
_cell.length_b           41.240 
_cell.length_c           71.950 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.430 
_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                         3MHI 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                         29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                     65.409    1   ?       ? ? ? 
3 non-polymer syn '4-{[(5-nitro-6-oxo-1,6-dihydropyrimidin-4-yl)amino]methyl}benzenesulfonamide' 325.301   2   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                           78.133    2   ?       ? ? ? 
5 water       nat water                                                                          18.015    280 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonic anhydrase II, CA-II, Carbonate dehydratase II, Carbonic anhydrase C, CAC' 
# 
_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                 ? 
_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              3MHI 
_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 
J90 non-polymer         . '4-{[(5-nitro-6-oxo-1,6-dihydropyrimidin-4-yl)amino]methyl}benzenesulfonamide' 
'4-{[(5-nitro-6-oxo-1,6-dihydro-4-pyrimidinyl)amino]methyl}benzenesulfonamide' 'C11 H11 N5 O5 S' 325.301 
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 
MET 'L-peptide linking' y METHIONINE                                                                     ? 'C5 H11 N O2 S'   
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                  ? 'C9 H11 N O2'     
165.189 
PRO 'L-peptide linking' y PROLINE                                                                        ? 'C5 H9 N O2'      
115.130 
SER 'L-peptide linking' y SERINE                                                                         ? 'C3 H7 N O3'      
105.093 
THR 'L-peptide linking' y THREONINE                                                                      ? 'C4 H9 N O3'      
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                     ? 'C11 H12 N2 O2'   
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                       ? 'C9 H11 N O3'     
181.189 
VAL 'L-peptide linking' y VALINE                                                                         ? 'C5 H11 N O2'     
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                     ? 'Zn 2'            
65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3MHI 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   40.64 
_exptl_crystal.density_Matthews      2.07 
_exptl_crystal.pdbx_mosaicity        ? 
_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' 
_exptl_crystal_grow.pH              9 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.pdbx_details    '0.1M Na-bicine pH 9, 2.6M Na-malonate pH 7, VAPOR DIFFUSION, temperature 293K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS IV++' 
_diffrn_detector.pdbx_collection_date   2010-03-13 
_diffrn_detector.details                'Osmic mirrors' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    '0.5 mm' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU RUH3R' 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
# 
_reflns.entry_id                     3MHI 
_reflns.d_resolution_high            1.700 
_reflns.d_resolution_low             21.101 
_reflns.number_all                   26720 
_reflns.number_obs                   26639 
_reflns.pdbx_Rmerge_I_obs            0.045 
_reflns.pdbx_netI_over_sigmaI        31.200 
_reflns.pdbx_Rsym_value              0.045 
_reflns.pdbx_redundancy              9.400 
_reflns.percent_possible_obs         99.900 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        16.0 
_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_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.70 
_reflns_shell.d_res_low              1.79 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    33975 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.185 
_reflns_shell.meanI_over_sigI_obs    10.7 
_reflns_shell.pdbx_Rsym_value        0.185 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_redundancy        8.80 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      3843 
_reflns_shell.percent_possible_all   99.30 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3MHI 
_refine.ls_d_res_high                            1.700 
_refine.ls_d_res_low                             21.100 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.890 
_refine.ls_number_reflns_obs                     26628 
_refine.ls_number_reflns_all                     26628 
_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                          0.167 
_refine.ls_R_factor_obs                          0.167 
_refine.ls_R_factor_R_work                       0.162 
_refine.ls_wR_factor_R_work                      0.170 
_refine.ls_R_factor_R_free                       0.215 
_refine.ls_wR_factor_R_free                      0.223 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  2678 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               14.065 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             isotropic 
_refine.aniso_B[1][1]                            0.180 
_refine.aniso_B[2][2]                            -0.010 
_refine.aniso_B[3][3]                            -0.180 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.030 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.938 
_refine.overall_SU_R_Cruickshank_DPI             0.118 
_refine.overall_SU_R_free                        0.121 
_refine.pdbx_overall_ESU_R                       0.118 
_refine.pdbx_overall_ESU_R_Free                  0.121 
_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                   0.851 
_refine.B_iso_max                                56.94 
_refine.B_iso_min                                2.68 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          0 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3HLJ' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_diffrn_id                           1 
_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         53 
_refine_hist.number_atoms_solvent             280 
_refine_hist.number_atoms_total               2382 
_refine_hist.d_res_high                       1.700 
_refine_hist.d_res_low                        21.100 
# 
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_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         2224 0.029  0.021  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      3030 2.234  1.971  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   269  6.865  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   102  35.407 24.804 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   361  13.358 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   7    20.531 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           311  0.171  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     1739 0.014  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            1179 0.221  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          1479 0.309  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    235  0.162  0.200  ? 'X-RAY DIFFRACTION' ? 
r_metal_ion_refined      2    0.052  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   63   0.251  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 50   0.195  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              1323 1.467  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             2144 2.204  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              901  3.258  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             886  4.848  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.700 
_refine_ls_shell.d_res_low                        1.744 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               98.550 
_refine_ls_shell.number_reflns_R_work             1725 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.299 
_refine_ls_shell.R_factor_R_free                  0.479 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             182 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1907 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3MHI 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 4-{[(5-nitro-6-oxo-1,6-dihydro-4-pyrimidinyl)amino]methyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3MHI 
_struct_keywords.text            'DRUG DESIGN, CARBONIC ANHYDRASE, SULFONAMIDE, LYASE-LYASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -2.35 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 7.74  
# 
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  THR A 87  ? TRP A 97  ? THR A 87  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  THR A 87  ? TRP A 97  ? THR A 87  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  262 ? 4  'BINDING SITE FOR RESIDUE ZN A 262'  
AC2 Software A J90 263 ? 15 'BINDING SITE FOR RESIDUE J90 A 263' 
AC3 Software A J90 264 ? 13 'BINDING SITE FOR RESIDUE J90 A 264' 
AC4 Software A DMS 265 ? 5  'BINDING SITE FOR RESIDUE DMS A 265' 
AC5 Software A DMS 266 ? 5  'BINDING SITE FOR RESIDUE DMS A 266' 
# 
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  J90 C .   ? J90 A 263 . ? 1_555 ? 
5  AC2 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
6  AC2 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
7  AC2 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
8  AC2 15 VAL A 142 ? VAL A 143 . ? 1_555 ? 
9  AC2 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
10 AC2 15 THR A 198 ? THR A 199 . ? 1_555 ? 
11 AC2 15 THR A 199 ? THR A 200 . ? 1_555 ? 
12 AC2 15 PRO A 201 ? PRO A 202 . ? 1_555 ? 
13 AC2 15 TRP A 208 ? TRP A 209 . ? 1_555 ? 
14 AC2 15 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
15 AC2 15 DMS F .   ? DMS A 266 . ? 1_555 ? 
16 AC2 15 HOH G .   ? HOH A 271 . ? 1_555 ? 
17 AC2 15 HOH G .   ? HOH A 400 . ? 1_555 ? 
18 AC2 15 HOH G .   ? HOH A 413 . ? 1_555 ? 
19 AC2 15 HOH G .   ? HOH A 486 . ? 1_555 ? 
20 AC3 13 HIS A 4   ? HIS A 4   . ? 1_555 ? 
21 AC3 13 TRP A 5   ? TRP A 5   . ? 1_555 ? 
22 AC3 13 HIS A 10  ? HIS A 10  . ? 1_555 ? 
23 AC3 13 ASN A 11  ? ASN A 11  . ? 1_555 ? 
24 AC3 13 HIS A 15  ? HIS A 15  . ? 1_555 ? 
25 AC3 13 TRP A 16  ? TRP A 16  . ? 1_555 ? 
26 AC3 13 ASP A 19  ? ASP A 19  . ? 1_555 ? 
27 AC3 13 PRO A 154 ? PRO A 155 . ? 1_655 ? 
28 AC3 13 GLY A 155 ? GLY A 156 . ? 1_655 ? 
29 AC3 13 GLY A 182 ? GLY A 183 . ? 1_655 ? 
30 AC3 13 HOH G .   ? HOH A 347 . ? 1_655 ? 
31 AC3 13 HOH G .   ? HOH A 466 . ? 1_555 ? 
32 AC3 13 HOH G .   ? HOH A 484 . ? 1_555 ? 
33 AC4 5  TYR A 7   ? TYR A 7   . ? 1_555 ? 
34 AC4 5  ASP A 242 ? ASP A 243 . ? 1_555 ? 
35 AC4 5  TRP A 244 ? TRP A 245 . ? 1_555 ? 
36 AC4 5  HOH G .   ? HOH A 399 . ? 1_555 ? 
37 AC4 5  HOH G .   ? HOH A 520 . ? 1_555 ? 
38 AC5 5  ILE A 91  ? ILE A 91  . ? 1_555 ? 
39 AC5 5  GLN A 92  ? GLN A 92  . ? 1_555 ? 
40 AC5 5  PHE A 130 ? PHE A 131 . ? 1_555 ? 
41 AC5 5  J90 C .   ? J90 A 263 . ? 1_555 ? 
42 AC5 5  HOH G .   ? HOH A 375 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3MHI 
_atom_sites.fract_transf_matrix[1][1]   0.023673 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006091 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024248 
_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]   0.014351 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 11.012  -0.100  8.046   1.00 23.77 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 9.641   0.218   8.631   1.00 21.15 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.064   -0.935  9.500   1.00 18.08 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.242   -2.079  9.207   1.00 15.25 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 8.658   0.420   7.500   1.00 23.71 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 7.433   1.183   7.896   1.00 30.86 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 7.452   2.548   8.124   1.00 37.29 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 6.145   0.779   8.107   1.00 30.58 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 6.232   2.946   8.476   1.00 36.92 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 5.419   1.894   8.446   1.00 34.17 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.292   -0.582  10.504  1.00 15.00 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.626   -1.582  11.334  1.00 12.31 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.586   -2.320  10.519  1.00 12.51 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.011   -1.764  9.544   1.00 12.43 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 6.901   -0.871  12.489  1.00 11.25 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 5.738   -0.005  12.089  1.00 13.01 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.751   1.349   11.780  1.00 12.91 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.379   -0.419  12.022  1.00 11.67 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.447   1.789   11.544  1.00 11.79 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.604   0.716   11.635  1.00 11.49 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 3.735   -1.648  12.251  1.00 8.99  ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.187   0.671   11.473  1.00 11.71 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.299   -1.702  12.013  1.00 9.01  ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.565   -0.496  11.717  1.00 12.56 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.261   -3.521  10.959  1.00 10.84 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.299   -4.316  10.271  1.00 12.36 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 4.951   -5.475  11.206  1.00 11.88 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 4.934   -5.355  12.471  1.00 10.51 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 4.700   -6.624  10.570  1.00 12.93 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.370   -7.817  11.308  1.00 13.43 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.093   -8.978  10.675  1.00 17.69 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 4.603   -10.150 10.746  1.00 17.41 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 2.891   -8.124  11.156  1.00 13.09 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 1.982   -7.060  11.701  1.00 10.08 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.604   -7.079  13.052  1.00 10.79 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.518   -6.033  10.881  1.00 8.29  ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 0.727   -6.070  13.588  1.00 9.10  ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.530   -5.100  11.356  1.00 8.90  ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.168   -5.140  12.734  1.00 11.77 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.663  -4.154  13.202  1.00 9.09  ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.180   -8.687  9.986   1.00 16.29 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 6.895   -9.750  9.293   1.00 18.04 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 7.861   -10.464 10.222  1.00 18.92 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 7.903   -10.210 11.440  1.00 17.41 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 8.708   -11.333 9.615   1.00 19.61 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 9.687   -12.069 10.447  1.00 21.39 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 10.694  -11.210 11.271  1.00 22.02 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.234  -11.748 12.235  1.00 22.34 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 10.402  -13.151 9.598   1.00 23.68 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 9.514   -14.370 9.211   1.00 28.03 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 9.414   -15.387 10.378  1.00 32.98 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 9.152   -16.850 9.872   1.00 34.14 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 9.846   -17.989 10.646  1.00 32.41 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 10.971  -9.935  10.862  1.00 19.07 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 12.115  -9.095  11.345  1.00 18.12 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 11.735  -7.676  11.803  1.00 15.26 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 12.562  -6.914  12.264  1.00 16.05 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 13.207  -8.934  10.221  1.00 17.31 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 13.728  -10.255 9.736   1.00 20.68 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 14.720  -10.947 10.405  1.00 19.07 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 13.334  -11.047 8.690   1.00 19.54 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 14.876  -12.135 9.827   1.00 18.69 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 14.064  -12.210 8.773   1.00 20.46 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 10.436  -7.319  11.690  1.00 12.77 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 10.029  -5.969  12.034  1.00 12.00 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 8.667   -5.989  12.806  1.00 11.54 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 7.995   -4.956  12.864  1.00 11.64 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 9.860   -5.168  10.761  1.00 11.34 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 8.732   -5.696  9.876   1.00 12.13 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 8.207   -6.825  10.083  1.00 11.54 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 8.423   -4.922  8.760   1.00 14.34 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 8.387   -7.162  13.414  1.00 10.68 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 7.062   -7.411  14.042  1.00 11.73 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 7.025   -6.778  15.436  1.00 11.64 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 7.910   -5.982  15.857  1.00 11.44 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 5.942   -7.091  16.171  1.00 12.42 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 5.677   -6.437  17.445  1.00 12.74 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 6.795   -6.408  18.472  1.00 10.68 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 6.900   -5.396  19.208  1.00 11.60 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 4.448   -7.241  17.968  1.00 11.02 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 3.678   -7.448  16.719  1.00 10.21 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 4.776   -7.897  15.737  1.00 12.73 ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 7.660   -7.432  18.495  1.00 9.08  ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 8.726   -7.506  19.544  1.00 10.43 ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 9.870   -6.459  19.192  1.00 7.69  ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 10.744  -6.244  19.958  1.00 10.89 ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 9.248   -8.933  19.527  1.00 13.34 ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 9.926   -9.335  18.200  1.00 13.43 ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 9.028   -9.996  17.074  1.00 20.64 ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 7.803   -9.657  16.918  1.00 16.97 ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 9.657   -10.786 16.250  1.00 18.90 ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 9.850   -5.911  17.988  1.00 8.51  ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 10.818  -4.921  17.515  1.00 8.13  ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 10.398  -3.436  17.642  1.00 10.84 ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 11.294  -2.513  17.517  1.00 9.00  ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 11.169  -5.137  16.045  1.00 10.53 ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 11.819  -6.483  15.782  1.00 15.35 ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 13.179  -6.708  15.964  1.00 15.40 ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 11.288  -7.664  15.364  1.00 16.03 ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 13.434  -7.991  15.695  1.00 17.39 ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 12.311  -8.587  15.338  1.00 18.07 ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 9.079   -3.197  17.834  1.00 8.51  ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 8.592   -1.838  17.756  1.00 9.57  ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 9.193   -0.878  18.791  1.00 6.97  ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 9.309   0.340   18.491  1.00 8.95  ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 7.049   -1.820  17.873  1.00 6.90  ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 6.364   -2.602  16.751  1.00 11.09 ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 6.917   -3.138  15.588  1.00 7.56  ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 4.945   -2.878  16.681  1.00 9.00  ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 5.939   -3.753  14.832  1.00 8.02  ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 4.713   -3.595  15.450  1.00 9.70  ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 3.868   -2.593  17.536  1.00 8.12  ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 3.393   -4.025  15.059  1.00 10.57 ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 2.630   -3.024  17.206  1.00 7.70  ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 2.361   -3.715  15.970  1.00 9.37  ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 9.596   -1.430  19.946  1.00 6.90  ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 10.065  -0.594  21.063  1.00 8.73  ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 11.317  0.216   20.666  1.00 9.24  ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 11.535  1.288   21.185  1.00 9.99  ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 10.301  -1.402  22.324  1.00 8.58  ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 11.446  -2.341  22.208  1.00 9.89  ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 12.709  -1.995  22.631  1.00 15.15 ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 11.567  -3.510  21.532  1.00 12.47 ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 13.545  -2.979  22.348  1.00 10.64 ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 12.888  -3.905  21.665  1.00 13.69 ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 18  ? 12.105  -0.365  19.748  1.00 10.37 ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 18  ? 13.353  0.306   19.302  1.00 13.32 ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 18  ? 13.094  1.605   18.548  1.00 12.47 ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 18  ? 13.883  2.517   18.659  1.00 13.69 ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 18  ? 14.144  -0.655  18.414  1.00 12.80 ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 18  ? 14.765  -1.834  19.121  1.00 13.16 ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 18  ? 15.391  -2.753  18.095  1.00 13.13 ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 18  ? 14.417  -3.782  17.495  1.00 14.60 ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 18  ? 15.139  -4.572  16.432  1.00 12.70 ? 18  LYS A NZ  1 
ATOM   135  N  N   . ASP A 1 19  ? 11.982  1.722   17.792  1.00 12.51 ? 19  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 19  ? 11.585  3.024   17.289  1.00 13.79 ? 19  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 19  ? 10.490  3.809   18.041  1.00 13.85 ? 19  ASP A C   1 
ATOM   138  O  O   . ASP A 1 19  ? 10.361  5.053   17.863  1.00 12.35 ? 19  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 19  ? 11.251  2.911   15.819  1.00 14.75 ? 19  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 19  ? 12.529  2.678   15.006  1.00 19.48 ? 19  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 19  ? 13.207  3.652   14.721  1.00 20.69 ? 19  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 19  ? 12.861  1.498   14.767  1.00 21.97 ? 19  ASP A OD2 1 
ATOM   143  N  N   . PHE A 1 20  ? 9.722   3.059   18.858  1.00 11.46 ? 20  PHE A N   1 
ATOM   144  C  CA  . PHE A 1 20  ? 8.612   3.612   19.603  1.00 10.56 ? 20  PHE A CA  1 
ATOM   145  C  C   . PHE A 1 20  ? 8.690   3.154   21.058  1.00 10.11 ? 20  PHE A C   1 
ATOM   146  O  O   . PHE A 1 20  ? 8.026   2.176   21.431  1.00 10.38 ? 20  PHE A O   1 
ATOM   147  C  CB  . PHE A 1 20  ? 7.303   3.124   18.927  1.00 10.51 ? 20  PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 20  ? 7.221   3.546   17.518  1.00 8.33  ? 20  PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 20  ? 6.868   4.875   17.200  1.00 13.00 ? 20  PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 20  ? 7.602   2.635   16.493  1.00 12.01 ? 20  PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 20  ? 6.782   5.247   15.872  1.00 13.96 ? 20  PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 20  ? 7.578   2.990   15.147  1.00 13.43 ? 20  PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 20  ? 7.179   4.303   14.839  1.00 14.27 ? 20  PHE A CZ  1 
ATOM   154  N  N   . PRO A 1 21  ? 9.569   3.789   21.866  1.00 11.35 ? 21  PRO A N   1 
ATOM   155  C  CA  . PRO A 1 21  ? 9.866   3.331   23.240  1.00 10.20 ? 21  PRO A CA  1 
ATOM   156  C  C   . PRO A 1 21  ? 8.610   3.184   24.124  1.00 10.03 ? 21  PRO A C   1 
ATOM   157  O  O   . PRO A 1 21  ? 8.627   2.387   25.077  1.00 9.34  ? 21  PRO A O   1 
ATOM   158  C  CB  . PRO A 1 21  ? 10.900  4.350   23.783  1.00 13.17 ? 21  PRO A CB  1 
ATOM   159  C  CG  . PRO A 1 21  ? 10.963  5.451   22.726  1.00 12.24 ? 21  PRO A CG  1 
ATOM   160  C  CD  . PRO A 1 21  ? 10.479  4.885   21.425  1.00 11.19 ? 21  PRO A CD  1 
ATOM   161  N  N   A ILE A 1 22  ? 7.569   3.953   23.796  0.50 9.47  ? 22  ILE A N   1 
ATOM   162  N  N   B ILE A 1 22  ? 7.569   3.956   23.797  0.50 9.14  ? 22  ILE A N   1 
ATOM   163  C  CA  A ILE A 1 22  ? 6.297   3.851   24.514  0.50 9.41  ? 22  ILE A CA  1 
ATOM   164  C  CA  B ILE A 1 22  ? 6.277   3.853   24.489  0.50 8.70  ? 22  ILE A CA  1 
ATOM   165  C  C   A ILE A 1 22  ? 5.655   2.467   24.345  0.50 8.43  ? 22  ILE A C   1 
ATOM   166  C  C   B ILE A 1 22  ? 5.712   2.426   24.423  0.50 8.33  ? 22  ILE A C   1 
ATOM   167  O  O   A ILE A 1 22  ? 4.681   2.163   25.034  0.50 7.48  ? 22  ILE A O   1 
ATOM   168  O  O   B ILE A 1 22  ? 4.859   2.050   25.266  0.50 7.83  ? 22  ILE A O   1 
ATOM   169  C  CB  A ILE A 1 22  ? 5.322   4.990   24.100  0.50 8.44  ? 22  ILE A CB  1 
ATOM   170  C  CB  B ILE A 1 22  ? 5.266   4.876   23.914  0.50 7.37  ? 22  ILE A CB  1 
ATOM   171  C  CG1 A ILE A 1 22  ? 4.266   5.234   25.179  0.50 11.05 ? 22  ILE A CG1 1 
ATOM   172  C  CG1 B ILE A 1 22  ? 4.215   5.239   24.963  0.50 8.69  ? 22  ILE A CG1 1 
ATOM   173  C  CG2 A ILE A 1 22  ? 4.758   4.690   22.688  0.50 8.49  ? 22  ILE A CG2 1 
ATOM   174  C  CG2 B ILE A 1 22  ? 4.775   4.365   22.528  0.50 5.65  ? 22  ILE A CG2 1 
ATOM   175  C  CD1 A ILE A 1 22  ? 4.803   5.787   26.470  0.50 11.45 ? 22  ILE A CD1 1 
ATOM   176  C  CD1 B ILE A 1 22  ? 3.365   6.423   24.636  0.50 3.90  ? 22  ILE A CD1 1 
ATOM   177  N  N   . ALA A 1 23  ? 6.208   1.596   23.487  1.00 8.83  ? 23  ALA A N   1 
ATOM   178  C  CA  . ALA A 1 23  ? 5.774   0.156   23.388  1.00 9.38  ? 23  ALA A CA  1 
ATOM   179  C  C   . ALA A 1 23  ? 5.822   -0.564  24.722  1.00 10.89 ? 23  ALA A C   1 
ATOM   180  O  O   . ALA A 1 23  ? 5.061   -1.513  24.940  1.00 8.75  ? 23  ALA A O   1 
ATOM   181  C  CB  . ALA A 1 23  ? 6.645   -0.604  22.371  1.00 9.76  ? 23  ALA A CB  1 
ATOM   182  N  N   . LYS A 1 24  ? 6.754   -0.129  25.579  1.00 10.67 ? 24  LYS A N   1 
ATOM   183  C  CA  . LYS A 1 24  ? 6.910   -0.764  26.921  1.00 12.57 ? 24  LYS A CA  1 
ATOM   184  C  C   . LYS A 1 24  ? 6.343   0.157   27.998  1.00 12.47 ? 24  LYS A C   1 
ATOM   185  O  O   . LYS A 1 24  ? 6.777   0.072   29.181  1.00 11.52 ? 24  LYS A O   1 
ATOM   186  C  CB  . LYS A 1 24  ? 8.376   -1.030  27.216  1.00 12.89 ? 24  LYS A CB  1 
ATOM   187  C  CG  . LYS A 1 24  ? 9.066   -2.017  26.305  1.00 15.79 ? 24  LYS A CG  1 
ATOM   188  C  CD  . LYS A 1 24  ? 10.562  -2.001  26.669  1.00 19.77 ? 24  LYS A CD  1 
ATOM   189  C  CE  . LYS A 1 24  ? 11.392  -3.016  25.818  1.00 21.06 ? 24  LYS A CE  1 
ATOM   190  N  NZ  . LYS A 1 24  ? 10.853  -4.374  25.751  1.00 24.62 ? 24  LYS A NZ  1 
ATOM   191  N  N   . GLY A 1 25  ? 5.375   1.000   27.626  1.00 8.50  ? 25  GLY A N   1 
ATOM   192  C  CA  . GLY A 1 25  ? 4.820   2.018   28.542  1.00 11.08 ? 25  GLY A CA  1 
ATOM   193  C  C   . GLY A 1 25  ? 3.797   1.412   29.523  1.00 9.21  ? 25  GLY A C   1 
ATOM   194  O  O   . GLY A 1 25  ? 3.655   0.173   29.656  1.00 9.39  ? 25  GLY A O   1 
ATOM   195  N  N   . GLU A 1 26  ? 3.128   2.314   30.251  1.00 9.77  ? 26  GLU A N   1 
ATOM   196  C  CA  . GLU A 1 26  ? 2.271   1.925   31.377  1.00 9.83  ? 26  GLU A CA  1 
ATOM   197  C  C   . GLU A 1 26  ? 0.815   1.634   30.997  1.00 8.54  ? 26  GLU A C   1 
ATOM   198  O  O   . GLU A 1 26  ? 0.035   1.095   31.826  1.00 10.03 ? 26  GLU A O   1 
ATOM   199  C  CB  . GLU A 1 26  ? 2.282   3.036   32.460  1.00 13.29 ? 26  GLU A CB  1 
ATOM   200  C  CG  . GLU A 1 26  ? 3.723   3.237   33.107  1.00 17.11 ? 26  GLU A CG  1 
ATOM   201  C  CD  . GLU A 1 26  ? 4.350   1.912   33.686  1.00 21.80 ? 26  GLU A CD  1 
ATOM   202  O  OE1 . GLU A 1 26  ? 3.734   1.184   34.524  1.00 28.68 ? 26  GLU A OE1 1 
ATOM   203  O  OE2 . GLU A 1 26  ? 5.452   1.545   33.257  1.00 26.01 ? 26  GLU A OE2 1 
ATOM   204  N  N   . ARG A 1 27  ? 0.454   1.953   29.753  1.00 8.49  ? 27  ARG A N   1 
ATOM   205  C  CA  . ARG A 1 27  ? -0.982  1.792   29.387  1.00 7.75  ? 27  ARG A CA  1 
ATOM   206  C  C   . ARG A 1 27  ? -1.099  1.337   27.918  1.00 6.95  ? 27  ARG A C   1 
ATOM   207  O  O   . ARG A 1 27  ? -1.841  1.946   27.081  1.00 7.81  ? 27  ARG A O   1 
ATOM   208  C  CB  . ARG A 1 27  ? -1.861  3.020   29.741  1.00 7.83  ? 27  ARG A CB  1 
ATOM   209  C  CG  . ARG A 1 27  ? -1.542  4.269   28.964  1.00 9.81  ? 27  ARG A CG  1 
ATOM   210  C  CD  . ARG A 1 27  ? -2.578  5.401   29.294  1.00 14.74 ? 27  ARG A CD  1 
ATOM   211  N  NE  . ARG A 1 27  ? -3.745  5.346   28.366  1.00 12.45 ? 27  ARG A NE  1 
ATOM   212  C  CZ  . ARG A 1 27  ? -4.671  6.262   28.318  1.00 12.47 ? 27  ARG A CZ  1 
ATOM   213  N  NH1 . ARG A 1 27  ? -4.612  7.338   29.124  1.00 12.47 ? 27  ARG A NH1 1 
ATOM   214  N  NH2 . ARG A 1 27  ? -5.659  6.126   27.458  1.00 14.66 ? 27  ARG A NH2 1 
ATOM   215  N  N   . GLN A 1 28  ? -0.366  0.221   27.651  1.00 6.59  ? 28  GLN A N   1 
ATOM   216  C  CA  . GLN A 1 28  ? -0.309  -0.291  26.231  1.00 7.33  ? 28  GLN A CA  1 
ATOM   217  C  C   . GLN A 1 28  ? -1.493  -1.252  25.978  1.00 6.58  ? 28  GLN A C   1 
ATOM   218  O  O   . GLN A 1 28  ? -2.001  -1.899  26.922  1.00 6.77  ? 28  GLN A O   1 
ATOM   219  C  CB  . GLN A 1 28  ? 1.046   -1.009  26.005  1.00 7.77  ? 28  GLN A CB  1 
ATOM   220  C  CG  . GLN A 1 28  ? 2.168   0.038   25.924  1.00 7.85  ? 28  GLN A CG  1 
ATOM   221  C  CD  . GLN A 1 28  ? 2.007   0.893   24.602  1.00 6.07  ? 28  GLN A CD  1 
ATOM   222  O  OE1 . GLN A 1 28  ? 2.271   0.339   23.550  1.00 7.06  ? 28  GLN A OE1 1 
ATOM   223  N  NE2 . GLN A 1 28  ? 1.619   2.196   24.674  1.00 6.52  ? 28  GLN A NE2 1 
ATOM   224  N  N   . SER A 1 29  ? -1.852  -1.324  24.707  1.00 5.95  ? 29  SER A N   1 
ATOM   225  C  CA  . SER A 1 29  ? -2.924  -2.188  24.215  1.00 5.56  ? 29  SER A CA  1 
ATOM   226  C  C   . SER A 1 29  ? -2.358  -3.131  23.103  1.00 5.57  ? 29  SER A C   1 
ATOM   227  O  O   . SER A 1 29  ? -1.395  -2.725  22.394  1.00 6.11  ? 29  SER A O   1 
ATOM   228  C  CB  . SER A 1 29  ? -4.044  -1.405  23.645  1.00 3.54  ? 29  SER A CB  1 
ATOM   229  O  OG  . SER A 1 29  ? -4.673  -0.654  24.753  1.00 5.21  ? 29  SER A OG  1 
ATOM   230  N  N   . PRO A 1 30  ? -3.009  -4.283  22.885  1.00 6.38  ? 30  PRO A N   1 
ATOM   231  C  CA  . PRO A 1 30  ? -4.199  -4.847  23.588  1.00 4.97  ? 30  PRO A CA  1 
ATOM   232  C  C   . PRO A 1 30  ? -3.791  -5.473  24.903  1.00 4.07  ? 30  PRO A C   1 
ATOM   233  O  O   . PRO A 1 30  ? -2.572  -5.456  25.241  1.00 6.48  ? 30  PRO A O   1 
ATOM   234  C  CB  . PRO A 1 30  ? -4.738  -5.861  22.554  1.00 4.96  ? 30  PRO A CB  1 
ATOM   235  C  CG  . PRO A 1 30  ? -3.404  -6.460  21.999  1.00 6.08  ? 30  PRO A CG  1 
ATOM   236  C  CD  . PRO A 1 30  ? -2.506  -5.207  21.802  1.00 6.22  ? 30  PRO A CD  1 
ATOM   237  N  N   . VAL A 1 31  ? -4.805  -5.981  25.623  1.00 6.43  ? 31  VAL A N   1 
ATOM   238  C  CA  . VAL A 1 31  ? -4.595  -6.722  26.858  1.00 5.78  ? 31  VAL A CA  1 
ATOM   239  C  C   . VAL A 1 31  ? -5.529  -7.923  26.824  1.00 8.30  ? 31  VAL A C   1 
ATOM   240  O  O   . VAL A 1 31  ? -6.481  -7.995  26.026  1.00 7.34  ? 31  VAL A O   1 
ATOM   241  C  CB  . VAL A 1 31  ? -4.831  -5.911  28.130  1.00 9.51  ? 31  VAL A CB  1 
ATOM   242  C  CG1 . VAL A 1 31  ? -3.874  -4.694  28.151  1.00 6.94  ? 31  VAL A CG1 1 
ATOM   243  C  CG2 . VAL A 1 31  ? -6.358  -5.540  28.252  1.00 9.58  ? 31  VAL A CG2 1 
ATOM   244  N  N   . ASP A 1 32  ? -5.134  -8.916  27.641  1.00 8.04  ? 32  ASP A N   1 
ATOM   245  C  CA  . ASP A 1 32  ? -5.987  -10.043 27.941  1.00 7.92  ? 32  ASP A CA  1 
ATOM   246  C  C   . ASP A 1 32  ? -7.099  -9.478  28.892  1.00 9.02  ? 32  ASP A C   1 
ATOM   247  O  O   . ASP A 1 32  ? -6.799  -8.765  29.891  1.00 9.51  ? 32  ASP A O   1 
ATOM   248  C  CB  . ASP A 1 32  ? -5.222  -11.253 28.544  1.00 9.79  ? 32  ASP A CB  1 
ATOM   249  C  CG  . ASP A 1 32  ? -6.195  -12.382 28.844  1.00 10.10 ? 32  ASP A CG  1 
ATOM   250  O  OD1 . ASP A 1 32  ? -6.992  -12.792 27.881  1.00 8.38  ? 32  ASP A OD1 1 
ATOM   251  O  OD2 . ASP A 1 32  ? -6.195  -12.803 30.049  1.00 10.67 ? 32  ASP A OD2 1 
ATOM   252  N  N   . ILE A 1 33  ? -8.338  -9.844  28.599  1.00 8.02  ? 33  ILE A N   1 
ATOM   253  C  CA  . ILE A 1 33  ? -9.474  -9.477  29.417  1.00 7.35  ? 33  ILE A CA  1 
ATOM   254  C  C   . ILE A 1 33  ? -9.776  -10.705 30.309  1.00 7.21  ? 33  ILE A C   1 
ATOM   255  O  O   . ILE A 1 33  ? -10.250 -11.760 29.861  1.00 9.57  ? 33  ILE A O   1 
ATOM   256  C  CB  . ILE A 1 33  ? -10.719 -9.027  28.648  1.00 6.69  ? 33  ILE A CB  1 
ATOM   257  C  CG1 . ILE A 1 33  ? -10.467 -7.664  27.904  1.00 8.72  ? 33  ILE A CG1 1 
ATOM   258  C  CG2 . ILE A 1 33  ? -11.895 -8.807  29.709  1.00 5.66  ? 33  ILE A CG2 1 
ATOM   259  C  CD1 . ILE A 1 33  ? -11.350 -7.541  26.632  1.00 10.01 ? 33  ILE A CD1 1 
ATOM   260  N  N   . ASP A 1 34  ? -9.375  -10.554 31.553  1.00 8.38  ? 34  ASP A N   1 
ATOM   261  C  CA  . ASP A 1 34  ? -9.630  -11.681 32.537  1.00 10.54 ? 34  ASP A CA  1 
ATOM   262  C  C   . ASP A 1 34  ? -11.081 -11.475 33.084  1.00 12.94 ? 34  ASP A C   1 
ATOM   263  O  O   . ASP A 1 34  ? -11.286 -10.547 33.898  1.00 14.46 ? 34  ASP A O   1 
ATOM   264  C  CB  . ASP A 1 34  ? -8.568  -11.634 33.677  1.00 10.83 ? 34  ASP A CB  1 
ATOM   265  C  CG  . ASP A 1 34  ? -8.706  -12.846 34.620  1.00 19.51 ? 34  ASP A CG  1 
ATOM   266  O  OD1 . ASP A 1 34  ? -9.721  -12.918 35.320  1.00 20.73 ? 34  ASP A OD1 1 
ATOM   267  O  OD2 . ASP A 1 34  ? -7.912  -13.827 34.480  1.00 26.89 ? 34  ASP A OD2 1 
ATOM   268  N  N   . THR A 1 35  ? -12.056 -12.213 32.571  1.00 12.96 ? 35  THR A N   1 
ATOM   269  C  CA  . THR A 1 35  ? -13.502 -11.934 32.778  1.00 15.15 ? 35  THR A CA  1 
ATOM   270  C  C   . THR A 1 35  ? -13.827 -12.061 34.274  1.00 16.72 ? 35  THR A C   1 
ATOM   271  O  O   . THR A 1 35  ? -14.788 -11.422 34.790  1.00 16.41 ? 35  THR A O   1 
ATOM   272  C  CB  . THR A 1 35  ? -14.378 -12.947 32.009  1.00 17.09 ? 35  THR A CB  1 
ATOM   273  O  OG1 . THR A 1 35  ? -14.122 -14.287 32.454  1.00 13.71 ? 35  THR A OG1 1 
ATOM   274  C  CG2 . THR A 1 35  ? -14.072 -12.865 30.503  1.00 14.74 ? 35  THR A CG2 1 
ATOM   275  N  N   . HIS A 1 36  ? -13.033 -12.915 34.967  1.00 15.68 ? 36  HIS A N   1 
ATOM   276  C  CA  . HIS A 1 36  ? -13.299 -13.179 36.368  1.00 16.40 ? 36  HIS A CA  1 
ATOM   277  C  C   . HIS A 1 36  ? -12.914 -11.991 37.248  1.00 18.35 ? 36  HIS A C   1 
ATOM   278  O  O   . HIS A 1 36  ? -13.639 -11.673 38.232  1.00 21.57 ? 36  HIS A O   1 
ATOM   279  C  CB  . HIS A 1 36  ? -12.820 -14.589 36.783  1.00 16.14 ? 36  HIS A CB  1 
ATOM   280  C  CG  . HIS A 1 36  ? -13.780 -15.643 36.307  1.00 13.19 ? 36  HIS A CG  1 
ATOM   281  N  ND1 . HIS A 1 36  ? -13.476 -16.577 35.326  1.00 19.47 ? 36  HIS A ND1 1 
ATOM   282  C  CD2 . HIS A 1 36  ? -15.115 -15.783 36.574  1.00 16.86 ? 36  HIS A CD2 1 
ATOM   283  C  CE1 . HIS A 1 36  ? -14.557 -17.309 35.085  1.00 19.89 ? 36  HIS A CE1 1 
ATOM   284  N  NE2 . HIS A 1 36  ? -15.567 -16.834 35.803  1.00 26.55 ? 36  HIS A NE2 1 
ATOM   285  N  N   . THR A 1 37  ? -11.872 -11.263 36.847  1.00 17.98 ? 37  THR A N   1 
ATOM   286  C  CA  . THR A 1 37  ? -11.369 -10.144 37.637  1.00 18.79 ? 37  THR A CA  1 
ATOM   287  C  C   . THR A 1 37  ? -11.835 -8.721  37.182  1.00 17.11 ? 37  THR A C   1 
ATOM   288  O  O   . THR A 1 37  ? -11.593 -7.743  37.892  1.00 18.74 ? 37  THR A O   1 
ATOM   289  C  CB  . THR A 1 37  ? -9.859  -10.160 37.849  1.00 19.74 ? 37  THR A CB  1 
ATOM   290  O  OG1 . THR A 1 37  ? -9.189  -9.959  36.615  1.00 28.00 ? 37  THR A OG1 1 
ATOM   291  C  CG2 . THR A 1 37  ? -9.369  -11.484 38.380  1.00 17.55 ? 37  THR A CG2 1 
ATOM   292  N  N   . ALA A 1 38  ? -12.441 -8.619  36.005  1.00 15.55 ? 38  ALA A N   1 
ATOM   293  C  CA  . ALA A 1 38  ? -13.022 -7.342  35.534  1.00 14.61 ? 38  ALA A CA  1 
ATOM   294  C  C   . ALA A 1 38  ? -14.216 -7.111  36.488  1.00 16.11 ? 38  ALA A C   1 
ATOM   295  O  O   . ALA A 1 38  ? -15.087 -7.959  36.623  1.00 18.79 ? 38  ALA A O   1 
ATOM   296  C  CB  . ALA A 1 38  ? -13.461 -7.407  34.112  1.00 16.15 ? 38  ALA A CB  1 
ATOM   297  N  N   . LYS A 1 39  ? -14.274 -5.941  37.086  1.00 16.13 ? 39  LYS A N   1 
ATOM   298  C  CA  . LYS A 1 39  ? -15.364 -5.735  38.006  1.00 17.37 ? 39  LYS A CA  1 
ATOM   299  C  C   . LYS A 1 39  ? -16.518 -5.002  37.333  1.00 15.94 ? 39  LYS A C   1 
ATOM   300  O  O   . LYS A 1 39  ? -16.360 -3.956  36.604  1.00 11.87 ? 39  LYS A O   1 
ATOM   301  C  CB  . LYS A 1 39  ? -14.853 -4.982  39.173  1.00 17.90 ? 39  LYS A CB  1 
ATOM   302  C  CG  . LYS A 1 39  ? -15.795 -4.993  40.428  1.00 23.63 ? 39  LYS A CG  1 
ATOM   303  C  CD  . LYS A 1 39  ? -15.204 -3.977  41.379  1.00 24.89 ? 39  LYS A CD  1 
ATOM   304  C  CE  . LYS A 1 39  ? -16.209 -3.361  42.312  1.00 31.05 ? 39  LYS A CE  1 
ATOM   305  N  NZ  . LYS A 1 39  ? -16.624 -4.319  43.378  1.00 28.12 ? 39  LYS A NZ  1 
ATOM   306  N  N   . TYR A 1 40  ? -17.715 -5.485  37.624  1.00 16.76 ? 40  TYR A N   1 
ATOM   307  C  CA  . TYR A 1 40  ? -18.910 -4.800  37.192  1.00 17.20 ? 40  TYR A CA  1 
ATOM   308  C  C   . TYR A 1 40  ? -18.960 -3.419  37.840  1.00 16.80 ? 40  TYR A C   1 
ATOM   309  O  O   . TYR A 1 40  ? -18.774 -3.278  39.114  1.00 17.45 ? 40  TYR A O   1 
ATOM   310  C  CB  . TYR A 1 40  ? -20.139 -5.617  37.639  1.00 19.16 ? 40  TYR A CB  1 
ATOM   311  C  CG  . TYR A 1 40  ? -21.386 -4.862  37.525  1.00 21.28 ? 40  TYR A CG  1 
ATOM   312  C  CD1 . TYR A 1 40  ? -21.811 -4.332  36.293  1.00 19.17 ? 40  TYR A CD1 1 
ATOM   313  C  CD2 . TYR A 1 40  ? -22.202 -4.675  38.643  1.00 29.03 ? 40  TYR A CD2 1 
ATOM   314  C  CE1 . TYR A 1 40  ? -22.976 -3.663  36.173  1.00 23.54 ? 40  TYR A CE1 1 
ATOM   315  C  CE2 . TYR A 1 40  ? -23.402 -3.989  38.536  1.00 26.65 ? 40  TYR A CE2 1 
ATOM   316  C  CZ  . TYR A 1 40  ? -23.777 -3.486  37.305  1.00 26.37 ? 40  TYR A CZ  1 
ATOM   317  O  OH  . TYR A 1 40  ? -24.942 -2.802  37.207  1.00 26.09 ? 40  TYR A OH  1 
ATOM   318  N  N   . ASP A 1 41  ? -19.228 -2.408  37.027  1.00 14.46 ? 41  ASP A N   1 
ATOM   319  C  CA  . ASP A 1 41  ? -19.222 -1.026  37.506  1.00 16.13 ? 41  ASP A CA  1 
ATOM   320  C  C   . ASP A 1 41  ? -20.587 -0.445  37.225  1.00 18.71 ? 41  ASP A C   1 
ATOM   321  O  O   . ASP A 1 41  ? -20.884 -0.075  36.083  1.00 15.22 ? 41  ASP A O   1 
ATOM   322  C  CB  . ASP A 1 41  ? -18.139 -0.180  36.825  1.00 17.26 ? 41  ASP A CB  1 
ATOM   323  C  CG  . ASP A 1 41  ? -18.119 1.261   37.344  1.00 20.89 ? 41  ASP A CG  1 
ATOM   324  O  OD1 . ASP A 1 41  ? -19.048 1.662   38.055  1.00 21.05 ? 41  ASP A OD1 1 
ATOM   325  O  OD2 . ASP A 1 41  ? -17.195 2.006   36.988  1.00 21.79 ? 41  ASP A OD2 1 
ATOM   326  N  N   . PRO A 1 42  ? -21.432 -0.356  38.269  1.00 20.45 ? 42  PRO A N   1 
ATOM   327  C  CA  . PRO A 1 42  ? -22.845 0.031   37.995  1.00 22.44 ? 42  PRO A CA  1 
ATOM   328  C  C   . PRO A 1 42  ? -22.940 1.537   37.676  1.00 22.26 ? 42  PRO A C   1 
ATOM   329  O  O   . PRO A 1 42  ? -24.000 2.016   37.226  1.00 23.41 ? 42  PRO A O   1 
ATOM   330  C  CB  . PRO A 1 42  ? -23.540 -0.323  39.340  1.00 22.88 ? 42  PRO A CB  1 
ATOM   331  C  CG  . PRO A 1 42  ? -22.535 0.131   40.321  1.00 21.99 ? 42  PRO A CG  1 
ATOM   332  C  CD  . PRO A 1 42  ? -21.220 -0.564  39.721  1.00 22.21 ? 42  PRO A CD  1 
ATOM   333  N  N   . SER A 1 43  ? -21.866 2.289   37.900  1.00 22.21 ? 43  SER A N   1 
ATOM   334  C  CA  . SER A 1 43  ? -21.794 3.658   37.419  1.00 24.07 ? 43  SER A CA  1 
ATOM   335  C  C   . SER A 1 43  ? -21.530 3.784   35.895  1.00 23.15 ? 43  SER A C   1 
ATOM   336  O  O   . SER A 1 43  ? -21.626 4.889   35.347  1.00 24.39 ? 43  SER A O   1 
ATOM   337  C  CB  . SER A 1 43  ? -20.747 4.484   38.185  1.00 23.98 ? 43  SER A CB  1 
ATOM   338  O  OG  . SER A 1 43  ? -19.389 4.246   37.769  1.00 24.30 ? 43  SER A OG  1 
ATOM   339  N  N   . LEU A 1 44  ? -21.177 2.688   35.204  1.00 21.51 ? 44  LEU A N   1 
ATOM   340  C  CA  . LEU A 1 44  ? -21.082 2.772   33.727  1.00 20.70 ? 44  LEU A CA  1 
ATOM   341  C  C   . LEU A 1 44  ? -22.476 2.938   33.102  1.00 22.85 ? 44  LEU A C   1 
ATOM   342  O  O   . LEU A 1 44  ? -23.475 2.358   33.581  1.00 22.95 ? 44  LEU A O   1 
ATOM   343  C  CB  . LEU A 1 44  ? -20.376 1.555   33.104  1.00 17.64 ? 44  LEU A CB  1 
ATOM   344  C  CG  . LEU A 1 44  ? -18.864 1.480   33.385  1.00 15.52 ? 44  LEU A CG  1 
ATOM   345  C  CD1 . LEU A 1 44  ? -18.265 0.062   33.135  1.00 16.93 ? 44  LEU A CD1 1 
ATOM   346  C  CD2 . LEU A 1 44  ? -18.067 2.666   32.715  1.00 15.33 ? 44  LEU A CD2 1 
ATOM   347  N  N   . LYS A 1 45  ? -22.523 3.719   32.032  1.00 22.26 ? 45  LYS A N   1 
ATOM   348  C  CA  . LYS A 1 45  ? -23.775 3.893   31.259  1.00 21.26 ? 45  LYS A CA  1 
ATOM   349  C  C   . LYS A 1 45  ? -23.790 3.014   30.042  1.00 21.43 ? 45  LYS A C   1 
ATOM   350  O  O   . LYS A 1 45  ? -22.750 2.439   29.634  1.00 21.55 ? 45  LYS A O   1 
ATOM   351  C  CB  . LYS A 1 45  ? -23.876 5.267   30.744  1.00 21.04 ? 45  LYS A CB  1 
ATOM   352  C  CG  . LYS A 1 45  ? -23.769 6.267   31.823  1.00 21.61 ? 45  LYS A CG  1 
ATOM   353  C  CD  . LYS A 1 45  ? -23.892 7.659   31.198  1.00 27.20 ? 45  LYS A CD  1 
ATOM   354  C  CE  . LYS A 1 45  ? -23.270 8.711   32.115  1.00 36.80 ? 45  LYS A CE  1 
ATOM   355  N  NZ  . LYS A 1 45  ? -24.175 8.935   33.298  1.00 37.48 ? 45  LYS A NZ  1 
ATOM   356  N  N   . PRO A 1 46  ? -25.002 2.856   29.484  1.00 20.32 ? 46  PRO A N   1 
ATOM   357  C  CA  . PRO A 1 46  ? -25.119 2.152   28.215  1.00 19.39 ? 46  PRO A CA  1 
ATOM   358  C  C   . PRO A 1 46  ? -24.299 2.950   27.193  1.00 15.66 ? 46  PRO A C   1 
ATOM   359  O  O   . PRO A 1 46  ? -24.281 4.179   27.258  1.00 15.29 ? 46  PRO A O   1 
ATOM   360  C  CB  . PRO A 1 46  ? -26.644 2.243   27.911  1.00 18.63 ? 46  PRO A CB  1 
ATOM   361  C  CG  . PRO A 1 46  ? -27.334 2.326   29.337  1.00 22.70 ? 46  PRO A CG  1 
ATOM   362  C  CD  . PRO A 1 46  ? -26.327 3.299   30.032  1.00 21.24 ? 46  PRO A CD  1 
ATOM   363  N  N   . LEU A 1 47  ? -23.705 2.257   26.235  1.00 16.45 ? 47  LEU A N   1 
ATOM   364  C  CA  . LEU A 1 47  ? -22.978 2.895   25.185  1.00 15.33 ? 47  LEU A CA  1 
ATOM   365  C  C   . LEU A 1 47  ? -24.034 3.515   24.283  1.00 17.24 ? 47  LEU A C   1 
ATOM   366  O  O   . LEU A 1 47  ? -25.116 2.879   24.070  1.00 16.47 ? 47  LEU A O   1 
ATOM   367  C  CB  . LEU A 1 47  ? -22.264 1.760   24.437  1.00 16.76 ? 47  LEU A CB  1 
ATOM   368  C  CG  . LEU A 1 47  ? -21.087 2.074   23.595  1.00 19.03 ? 47  LEU A CG  1 
ATOM   369  C  CD1 . LEU A 1 47  ? -20.143 3.112   24.312  1.00 15.23 ? 47  LEU A CD1 1 
ATOM   370  C  CD2 . LEU A 1 47  ? -20.393 0.801   23.117  1.00 17.87 ? 47  LEU A CD2 1 
ATOM   371  N  N   . SER A 1 48  ? -23.747 4.677   23.711  1.00 11.90 ? 48  SER A N   1 
ATOM   372  C  CA  . SER A 1 48  ? -24.619 5.201   22.651  1.00 13.29 ? 48  SER A CA  1 
ATOM   373  C  C   . SER A 1 48  ? -23.843 5.267   21.355  1.00 13.06 ? 48  SER A C   1 
ATOM   374  O  O   . SER A 1 48  ? -22.881 6.058   21.216  1.00 11.33 ? 48  SER A O   1 
ATOM   375  C  CB  . SER A 1 48  ? -25.092 6.612   23.068  1.00 13.21 ? 48  SER A CB  1 
ATOM   376  O  OG  . SER A 1 48  ? -25.688 7.323   22.006  1.00 14.42 ? 48  SER A OG  1 
ATOM   377  N  N   . VAL A 1 49  ? -24.278 4.448   20.407  1.00 12.19 ? 49  VAL A N   1 
ATOM   378  C  CA  . VAL A 1 49  ? -23.710 4.371   19.078  1.00 14.91 ? 49  VAL A CA  1 
ATOM   379  C  C   . VAL A 1 49  ? -24.727 5.038   18.108  1.00 15.04 ? 49  VAL A C   1 
ATOM   380  O  O   . VAL A 1 49  ? -25.826 4.548   17.948  1.00 16.70 ? 49  VAL A O   1 
ATOM   381  C  CB  . VAL A 1 49  ? -23.415 2.916   18.678  1.00 15.67 ? 49  VAL A CB  1 
ATOM   382  C  CG1 . VAL A 1 49  ? -22.611 2.861   17.361  1.00 18.12 ? 49  VAL A CG1 1 
ATOM   383  C  CG2 . VAL A 1 49  ? -22.647 2.187   19.811  1.00 16.24 ? 49  VAL A CG2 1 
ATOM   384  N  N   . SER A 1 50  ? -24.391 6.196   17.564  1.00 14.15 ? 50  SER A N   1 
ATOM   385  C  CA  . SER A 1 50  ? -25.320 6.929   16.673  1.00 15.56 ? 50  SER A CA  1 
ATOM   386  C  C   . SER A 1 50  ? -24.691 6.987   15.264  1.00 13.85 ? 50  SER A C   1 
ATOM   387  O  O   . SER A 1 50  ? -23.981 7.934   14.950  1.00 13.32 ? 50  SER A O   1 
ATOM   388  C  CB  . SER A 1 50  ? -25.688 8.317   17.256  1.00 16.24 ? 50  SER A CB  1 
ATOM   389  O  OG  . SER A 1 50  ? -26.410 8.166   18.474  1.00 23.37 ? 50  SER A OG  1 
ATOM   390  N  N   . TYR A 1 51  ? -24.927 5.950   14.464  1.00 13.79 ? 51  TYR A N   1 
ATOM   391  C  CA  . TYR A 1 51  ? -24.314 5.818   13.149  1.00 11.64 ? 51  TYR A CA  1 
ATOM   392  C  C   . TYR A 1 51  ? -25.309 6.030   11.978  1.00 13.69 ? 51  TYR A C   1 
ATOM   393  O  O   . TYR A 1 51  ? -24.958 5.800   10.849  1.00 14.81 ? 51  TYR A O   1 
ATOM   394  C  CB  . TYR A 1 51  ? -23.671 4.440   12.979  1.00 12.03 ? 51  TYR A CB  1 
ATOM   395  C  CG  . TYR A 1 51  ? -22.376 4.158   13.741  1.00 10.39 ? 51  TYR A CG  1 
ATOM   396  C  CD1 . TYR A 1 51  ? -21.679 5.159   14.405  1.00 7.91  ? 51  TYR A CD1 1 
ATOM   397  C  CD2 . TYR A 1 51  ? -21.862 2.870   13.792  1.00 10.24 ? 51  TYR A CD2 1 
ATOM   398  C  CE1 . TYR A 1 51  ? -20.502 4.876   15.109  1.00 7.86  ? 51  TYR A CE1 1 
ATOM   399  C  CE2 . TYR A 1 51  ? -20.704 2.580   14.479  1.00 10.70 ? 51  TYR A CE2 1 
ATOM   400  C  CZ  . TYR A 1 51  ? -20.016 3.578   15.131  1.00 10.31 ? 51  TYR A CZ  1 
ATOM   401  O  OH  . TYR A 1 51  ? -18.871 3.231   15.801  1.00 9.67  ? 51  TYR A OH  1 
ATOM   402  N  N   A ASP A 1 52  ? -26.532 6.451   12.293  0.50 15.10 ? 52  ASP A N   1 
ATOM   403  N  N   B ASP A 1 52  ? -26.540 6.425   12.284  0.50 15.37 ? 52  ASP A N   1 
ATOM   404  C  CA  A ASP A 1 52  ? -27.618 6.639   11.282  0.50 15.78 ? 52  ASP A CA  1 
ATOM   405  C  CA  B ASP A 1 52  ? -27.579 6.632   11.239  0.50 16.29 ? 52  ASP A CA  1 
ATOM   406  C  C   A ASP A 1 52  ? -27.235 7.611   10.139  0.50 16.41 ? 52  ASP A C   1 
ATOM   407  C  C   B ASP A 1 52  ? -27.031 7.488   10.086  0.50 16.77 ? 52  ASP A C   1 
ATOM   408  O  O   A ASP A 1 52  ? -27.707 7.450   8.972   0.50 15.37 ? 52  ASP A O   1 
ATOM   409  O  O   B ASP A 1 52  ? -27.186 7.137   8.878   0.50 16.35 ? 52  ASP A O   1 
ATOM   410  C  CB  A ASP A 1 52  ? -28.928 7.075   11.988  0.50 16.97 ? 52  ASP A CB  1 
ATOM   411  C  CB  B ASP A 1 52  ? -28.832 7.298   11.851  0.50 17.64 ? 52  ASP A CB  1 
ATOM   412  C  CG  A ASP A 1 52  ? -28.704 8.216   12.990  0.50 16.44 ? 52  ASP A CG  1 
ATOM   413  C  CG  B ASP A 1 52  ? -29.972 7.349   10.894  0.50 18.14 ? 52  ASP A CG  1 
ATOM   414  O  OD1 A ASP A 1 52  ? -28.152 8.010   14.112  0.50 20.32 ? 52  ASP A OD1 1 
ATOM   415  O  OD1 B ASP A 1 52  ? -30.369 6.256   10.401  0.50 20.74 ? 52  ASP A OD1 1 
ATOM   416  O  OD2 A ASP A 1 52  ? -29.079 9.333   12.634  0.50 25.67 ? 52  ASP A OD2 1 
ATOM   417  O  OD2 B ASP A 1 52  ? -30.460 8.474   10.612  0.50 24.02 ? 52  ASP A OD2 1 
ATOM   418  N  N   . GLN A 1 53  ? -26.388 8.595   10.450  1.00 15.17 ? 53  GLN A N   1 
ATOM   419  C  CA  . GLN A 1 53  ? -25.896 9.549   9.441   1.00 17.61 ? 53  GLN A CA  1 
ATOM   420  C  C   . GLN A 1 53  ? -24.448 9.329   9.007   1.00 15.40 ? 53  GLN A C   1 
ATOM   421  O  O   . GLN A 1 53  ? -23.912 10.217  8.343   1.00 14.55 ? 53  GLN A O   1 
ATOM   422  C  CB  . GLN A 1 53  ? -26.003 10.999  9.932   1.00 17.17 ? 53  GLN A CB  1 
ATOM   423  C  CG  . GLN A 1 53  ? -27.341 11.344  10.541  1.00 26.33 ? 53  GLN A CG  1 
ATOM   424  C  CD  . GLN A 1 53  ? -28.364 11.557  9.497   1.00 32.84 ? 53  GLN A CD  1 
ATOM   425  O  OE1 . GLN A 1 53  ? -28.714 10.618  8.756   1.00 35.39 ? 53  GLN A OE1 1 
ATOM   426  N  NE2 . GLN A 1 53  ? -28.896 12.800  9.422   1.00 40.14 ? 53  GLN A NE2 1 
ATOM   427  N  N   . ALA A 1 54  ? -23.823 8.194   9.369   1.00 16.10 ? 54  ALA A N   1 
ATOM   428  C  CA  . ALA A 1 54  ? -22.471 7.873   8.906   1.00 12.86 ? 54  ALA A CA  1 
ATOM   429  C  C   . ALA A 1 54  ? -22.285 8.048   7.378   1.00 14.90 ? 54  ALA A C   1 
ATOM   430  O  O   . ALA A 1 54  ? -23.149 7.659   6.599   1.00 14.54 ? 54  ALA A O   1 
ATOM   431  C  CB  . ALA A 1 54  ? -22.032 6.389   9.367   1.00 14.00 ? 54  ALA A CB  1 
ATOM   432  N  N   . THR A 1 55  ? -21.200 8.690   6.955   1.00 13.24 ? 55  THR A N   1 
ATOM   433  C  CA  . THR A 1 55  ? -20.889 8.806   5.542   1.00 15.54 ? 55  THR A CA  1 
ATOM   434  C  C   . THR A 1 55  ? -19.533 8.223   5.280   1.00 12.88 ? 55  THR A C   1 
ATOM   435  O  O   . THR A 1 55  ? -18.495 8.907   5.471   1.00 10.63 ? 55  THR A O   1 
ATOM   436  C  CB  . THR A 1 55  ? -20.798 10.299  5.052   1.00 17.75 ? 55  THR A CB  1 
ATOM   437  O  OG1 . THR A 1 55  ? -21.962 11.001  5.436   1.00 19.74 ? 55  THR A OG1 1 
ATOM   438  C  CG2 . THR A 1 55  ? -20.776 10.298  3.580   1.00 20.06 ? 55  THR A CG2 1 
ATOM   439  N  N   . SER A 1 56  ? -19.522 6.992   4.811   1.00 10.53 ? 56  SER A N   1 
ATOM   440  C  CA  . SER A 1 56  ? -18.245 6.430   4.347   1.00 12.19 ? 56  SER A CA  1 
ATOM   441  C  C   . SER A 1 56  ? -17.771 7.151   3.058   1.00 12.70 ? 56  SER A C   1 
ATOM   442  O  O   . SER A 1 56  ? -18.591 7.638   2.236   1.00 14.35 ? 56  SER A O   1 
ATOM   443  C  CB  . SER A 1 56  ? -18.263 4.899   4.189   1.00 12.96 ? 56  SER A CB  1 
ATOM   444  O  OG  . SER A 1 56  ? -19.166 4.563   3.124   1.00 14.26 ? 56  SER A OG  1 
ATOM   445  N  N   . LEU A 1 57  ? -16.472 7.189   2.840   1.00 12.61 ? 57  LEU A N   1 
ATOM   446  C  CA  . LEU A 1 57  ? -15.970 7.774   1.586   1.00 13.51 ? 57  LEU A CA  1 
ATOM   447  C  C   . LEU A 1 57  ? -15.057 6.854   0.722   1.00 14.06 ? 57  LEU A C   1 
ATOM   448  O  O   . LEU A 1 57  ? -15.084 6.875   -0.523  1.00 13.18 ? 57  LEU A O   1 
ATOM   449  C  CB  . LEU A 1 57  ? -15.187 9.038   1.943   1.00 15.79 ? 57  LEU A CB  1 
ATOM   450  C  CG  . LEU A 1 57  ? -16.062 10.064  2.705   1.00 19.73 ? 57  LEU A CG  1 
ATOM   451  C  CD1 . LEU A 1 57  ? -15.079 11.177  3.152   1.00 24.42 ? 57  LEU A CD1 1 
ATOM   452  C  CD2 . LEU A 1 57  ? -17.296 10.613  1.878   1.00 24.47 ? 57  LEU A CD2 1 
ATOM   453  N  N   . ARG A 1 58  ? -14.223 6.079   1.415   1.00 11.32 ? 58  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 58  ? -13.120 5.443   0.734   1.00 9.54  ? 58  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 58  ? -12.649 4.284   1.546   1.00 10.37 ? 58  ARG A C   1 
ATOM   456  O  O   . ARG A 1 58  ? -12.797 4.289   2.796   1.00 8.22  ? 58  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 58  ? -11.967 6.455   0.570   1.00 13.14 ? 58  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 58  ? -10.975 6.022   -0.470  1.00 13.54 ? 58  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 58  ? -9.897  7.112   -0.602  1.00 18.13 ? 58  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 58  ? -9.096  7.207   0.641   1.00 16.55 ? 58  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 58  ? -7.784  7.389   0.624   1.00 12.95 ? 58  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 58  ? -7.197  7.603   -0.531  1.00 11.99 ? 58  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 58  ? -7.080  7.439   1.757   1.00 17.57 ? 58  ARG A NH2 1 
ATOM   464  N  N   . ILE A 1 59  ? -12.032 3.351   0.836   1.00 10.04 ? 59  ILE A N   1 
ATOM   465  C  CA  . ILE A 1 59  ? -11.350 2.247   1.499   1.00 10.53 ? 59  ILE A CA  1 
ATOM   466  C  C   . ILE A 1 59  ? -9.924  2.200   1.012   1.00 9.88  ? 59  ILE A C   1 
ATOM   467  O  O   . ILE A 1 59  ? -9.663  2.328   -0.199  1.00 10.19 ? 59  ILE A O   1 
ATOM   468  C  CB  . ILE A 1 59  ? -12.143 0.910   1.299   1.00 10.83 ? 59  ILE A CB  1 
ATOM   469  C  CG1 . ILE A 1 59  ? -11.539 -0.244  2.149   1.00 11.12 ? 59  ILE A CG1 1 
ATOM   470  C  CG2 . ILE A 1 59  ? -12.256 0.483   -0.250  1.00 8.14  ? 59  ILE A CG2 1 
ATOM   471  C  CD1 . ILE A 1 59  ? -12.329 -1.599  2.100   1.00 12.22 ? 59  ILE A CD1 1 
ATOM   472  N  N   . LEU A 1 60  ? -8.991  2.020   1.952   1.00 8.78  ? 60  LEU A N   1 
ATOM   473  C  CA  . LEU A 1 60  ? -7.566  2.156   1.644   1.00 8.92  ? 60  LEU A CA  1 
ATOM   474  C  C   . LEU A 1 60  ? -6.788  0.936   2.197   1.00 10.24 ? 60  LEU A C   1 
ATOM   475  O  O   . LEU A 1 60  ? -6.930  0.560   3.402   1.00 9.41  ? 60  LEU A O   1 
ATOM   476  C  CB  . LEU A 1 60  ? -7.050  3.462   2.357   1.00 9.76  ? 60  LEU A CB  1 
ATOM   477  C  CG  . LEU A 1 60  ? -5.525  3.634   2.323   1.00 12.73 ? 60  LEU A CG  1 
ATOM   478  C  CD1 . LEU A 1 60  ? -4.890  3.688   0.858   1.00 13.26 ? 60  LEU A CD1 1 
ATOM   479  C  CD2 . LEU A 1 60  ? -5.018  4.745   3.288   1.00 9.37  ? 60  LEU A CD2 1 
ATOM   480  N  N   . ASN A 1 61  ? -5.910  0.349   1.374   1.00 8.06  ? 61  ASN A N   1 
ATOM   481  C  CA  . ASN A 1 61  ? -4.950  -0.632  1.890   1.00 10.10 ? 61  ASN A CA  1 
ATOM   482  C  C   . ASN A 1 61  ? -3.697  0.158   2.277   1.00 10.86 ? 61  ASN A C   1 
ATOM   483  O  O   . ASN A 1 61  ? -3.031  0.667   1.410   1.00 9.85  ? 61  ASN A O   1 
ATOM   484  C  CB  . ASN A 1 61  ? -4.592  -1.712  0.825   1.00 10.28 ? 61  ASN A CB  1 
ATOM   485  C  CG  . ASN A 1 61  ? -3.506  -2.677  1.266   1.00 11.58 ? 61  ASN A CG  1 
ATOM   486  O  OD1 . ASN A 1 61  ? -2.656  -2.391  2.139   1.00 10.41 ? 61  ASN A OD1 1 
ATOM   487  N  ND2 . ASN A 1 61  ? -3.508  -3.874  0.653   1.00 13.08 ? 61  ASN A ND2 1 
ATOM   488  N  N   . ASN A 1 62  ? -3.380  0.236   3.559   1.00 9.18  ? 62  ASN A N   1 
ATOM   489  C  CA  . ASN A 1 62  ? -2.251  1.142   3.985   1.00 10.22 ? 62  ASN A CA  1 
ATOM   490  C  C   . ASN A 1 62  ? -1.006  0.344   4.221   1.00 10.63 ? 62  ASN A C   1 
ATOM   491  O  O   . ASN A 1 62  ? -0.046  0.881   4.782   1.00 11.93 ? 62  ASN A O   1 
ATOM   492  C  CB  . ASN A 1 62  ? -2.610  2.012   5.240   1.00 12.65 ? 62  ASN A CB  1 
ATOM   493  C  CG  . ASN A 1 62  ? -2.965  1.154   6.474   1.00 11.95 ? 62  ASN A CG  1 
ATOM   494  O  OD1 . ASN A 1 62  ? -2.704  -0.062  6.506   1.00 8.92  ? 62  ASN A OD1 1 
ATOM   495  N  ND2 . ASN A 1 62  ? -3.626  1.765   7.445   1.00 13.83 ? 62  ASN A ND2 1 
ATOM   496  N  N   . GLY A 1 63  ? -1.017  -0.961  3.874   1.00 8.95  ? 63  GLY A N   1 
ATOM   497  C  CA  . GLY A 1 63  ? 0.104   -1.811  3.981   1.00 10.31 ? 63  GLY A CA  1 
ATOM   498  C  C   . GLY A 1 63  ? 0.159   -2.554  5.313   1.00 10.52 ? 63  GLY A C   1 
ATOM   499  O  O   . GLY A 1 63  ? 1.061   -3.401  5.515   1.00 13.49 ? 63  GLY A O   1 
ATOM   500  N  N   A HIS A 1 64  ? -0.758  -2.232  6.218   0.50 9.16  ? 64  HIS A N   1 
ATOM   501  N  N   B HIS A 1 64  ? -0.771  -2.261  6.238   0.50 8.97  ? 64  HIS A N   1 
ATOM   502  C  CA  A HIS A 1 64  ? -0.784  -2.926  7.506   0.50 9.24  ? 64  HIS A CA  1 
ATOM   503  C  CA  B HIS A 1 64  ? -0.868  -3.034  7.528   0.50 8.84  ? 64  HIS A CA  1 
ATOM   504  C  C   A HIS A 1 64  ? -2.193  -3.573  7.638   0.50 10.04 ? 64  HIS A C   1 
ATOM   505  C  C   B HIS A 1 64  ? -2.287  -3.452  7.906   0.50 9.40  ? 64  HIS A C   1 
ATOM   506  O  O   A HIS A 1 64  ? -2.279  -4.756  8.037   0.50 9.78  ? 64  HIS A O   1 
ATOM   507  O  O   B HIS A 1 64  ? -2.502  -4.275  8.817   0.50 7.71  ? 64  HIS A O   1 
ATOM   508  C  CB  A HIS A 1 64  ? -0.386  -1.999  8.686   0.50 9.61  ? 64  HIS A CB  1 
ATOM   509  C  CB  B HIS A 1 64  ? -0.253  -2.338  8.731   0.50 9.62  ? 64  HIS A CB  1 
ATOM   510  C  CG  A HIS A 1 64  ? 0.933   -1.254  8.489   0.50 10.31 ? 64  HIS A CG  1 
ATOM   511  C  CG  B HIS A 1 64  ? -0.722  -0.938  8.979   0.50 10.13 ? 64  HIS A CG  1 
ATOM   512  N  ND1 A HIS A 1 64  ? 2.181   -1.817  8.706   0.50 11.66 ? 64  HIS A ND1 1 
ATOM   513  N  ND1 B HIS A 1 64  ? -0.024  0.148   8.487   0.50 10.86 ? 64  HIS A ND1 1 
ATOM   514  C  CD2 A HIS A 1 64  ? 1.167   0.033   8.136   0.50 10.94 ? 64  HIS A CD2 1 
ATOM   515  C  CD2 B HIS A 1 64  ? -1.682  -0.431  9.799   0.50 11.04 ? 64  HIS A CD2 1 
ATOM   516  C  CE1 A HIS A 1 64  ? 3.122   -0.918  8.487   0.50 10.78 ? 64  HIS A CE1 1 
ATOM   517  C  CE1 B HIS A 1 64  ? -0.585  1.259   8.929   0.50 13.24 ? 64  HIS A CE1 1 
ATOM   518  N  NE2 A HIS A 1 64  ? 2.536   0.212   8.119   0.50 8.47  ? 64  HIS A NE2 1 
ATOM   519  N  NE2 B HIS A 1 64  ? -1.550  0.936   9.773   0.50 11.52 ? 64  HIS A NE2 1 
ATOM   520  N  N   . ALA A 1 65  ? -3.248  -2.828  7.248   1.00 9.16  ? 65  ALA A N   1 
ATOM   521  C  CA  . ALA A 1 65  ? -4.644  -3.287  7.303   1.00 8.72  ? 65  ALA A CA  1 
ATOM   522  C  C   . ALA A 1 65  ? -5.379  -2.600  6.138   1.00 8.39  ? 65  ALA A C   1 
ATOM   523  O  O   . ALA A 1 65  ? -4.702  -1.938  5.272   1.00 10.24 ? 65  ALA A O   1 
ATOM   524  C  CB  . ALA A 1 65  ? -5.301  -3.049  8.712   1.00 8.19  ? 65  ALA A CB  1 
ATOM   525  N  N   . PHE A 1 66  ? -6.689  -2.704  6.100   1.00 6.67  ? 66  PHE A N   1 
ATOM   526  C  CA  . PHE A 1 66  ? -7.450  -1.774  5.217   1.00 7.12  ? 66  PHE A CA  1 
ATOM   527  C  C   . PHE A 1 66  ? -8.358  -0.897  6.094   1.00 8.85  ? 66  PHE A C   1 
ATOM   528  O  O   . PHE A 1 66  ? -8.989  -1.375  7.084   1.00 8.46  ? 66  PHE A O   1 
ATOM   529  C  CB  . PHE A 1 66  ? -8.240  -2.472  4.144   1.00 8.72  ? 66  PHE A CB  1 
ATOM   530  C  CG  . PHE A 1 66  ? -9.300  -3.434  4.709   1.00 8.64  ? 66  PHE A CG  1 
ATOM   531  C  CD1 . PHE A 1 66  ? -10.600 -2.968  5.033   1.00 8.72  ? 66  PHE A CD1 1 
ATOM   532  C  CD2 . PHE A 1 66  ? -9.003  -4.821  4.853   1.00 10.04 ? 66  PHE A CD2 1 
ATOM   533  C  CE1 . PHE A 1 66  ? -11.600 -3.819  5.558   1.00 13.64 ? 66  PHE A CE1 1 
ATOM   534  C  CE2 . PHE A 1 66  ? -10.030 -5.695  5.456   1.00 8.44  ? 66  PHE A CE2 1 
ATOM   535  C  CZ  . PHE A 1 66  ? -11.284 -5.195  5.774   1.00 9.42  ? 66  PHE A CZ  1 
ATOM   536  N  N   . ASN A 1 67  ? -8.449  0.372   5.773   1.00 7.89  ? 67  ASN A N   1 
ATOM   537  C  CA  . ASN A 1 67  ? -9.288  1.255   6.559   1.00 7.14  ? 67  ASN A CA  1 
ATOM   538  C  C   . ASN A 1 67  ? -10.458 1.684   5.705   1.00 8.87  ? 67  ASN A C   1 
ATOM   539  O  O   . ASN A 1 67  ? -10.241 2.122   4.551   1.00 8.16  ? 67  ASN A O   1 
ATOM   540  C  CB  . ASN A 1 67  ? -8.511  2.541   6.916   1.00 9.04  ? 67  ASN A CB  1 
ATOM   541  C  CG  . ASN A 1 67  ? -7.350  2.273   7.895   1.00 11.15 ? 67  ASN A CG  1 
ATOM   542  O  OD1 . ASN A 1 67  ? -7.212  1.158   8.405   1.00 12.60 ? 67  ASN A OD1 1 
ATOM   543  N  ND2 . ASN A 1 67  ? -6.485  3.266   8.081   1.00 13.78 ? 67  ASN A ND2 1 
ATOM   544  N  N   . VAL A 1 68  ? -11.647 1.644   6.294   1.00 8.42  ? 68  VAL A N   1 
ATOM   545  C  CA  . VAL A 1 68  ? -12.821 2.235   5.690   1.00 8.84  ? 68  VAL A CA  1 
ATOM   546  C  C   . VAL A 1 68  ? -12.965 3.596   6.355   1.00 10.82 ? 68  VAL A C   1 
ATOM   547  O  O   . VAL A 1 68  ? -13.077 3.665   7.616   1.00 9.15  ? 68  VAL A O   1 
ATOM   548  C  CB  . VAL A 1 68  ? -14.060 1.364   5.867   1.00 8.44  ? 68  VAL A CB  1 
ATOM   549  C  CG1 . VAL A 1 68  ? -15.364 2.203   5.469   1.00 10.34 ? 68  VAL A CG1 1 
ATOM   550  C  CG2 . VAL A 1 68  ? -13.890 0.019   5.082   1.00 9.20  ? 68  VAL A CG2 1 
ATOM   551  N  N   . GLU A 1 69  ? -12.774 4.662   5.558   1.00 9.82  ? 69  GLU A N   1 
ATOM   552  C  CA  . GLU A 1 69  ? -12.730 6.075   6.024   1.00 9.95  ? 69  GLU A CA  1 
ATOM   553  C  C   . GLU A 1 69  ? -14.091 6.771   5.895   1.00 11.42 ? 69  GLU A C   1 
ATOM   554  O  O   . GLU A 1 69  ? -14.848 6.533   4.937   1.00 11.98 ? 69  GLU A O   1 
ATOM   555  C  CB  . GLU A 1 69  ? -11.756 6.854   5.156   1.00 11.47 ? 69  GLU A CB  1 
ATOM   556  C  CG  . GLU A 1 69  ? -10.340 6.339   5.306   1.00 11.60 ? 69  GLU A CG  1 
ATOM   557  C  CD  . GLU A 1 69  ? -9.444  6.749   4.104   1.00 13.89 ? 69  GLU A CD  1 
ATOM   558  O  OE1 . GLU A 1 69  ? -9.997  7.368   3.155   1.00 15.67 ? 69  GLU A OE1 1 
ATOM   559  O  OE2 . GLU A 1 69  ? -8.260  6.350   4.124   1.00 16.67 ? 69  GLU A OE2 1 
ATOM   560  N  N   . PHE A 1 70  ? -14.358 7.593   6.906   1.00 10.16 ? 70  PHE A N   1 
ATOM   561  C  CA  . PHE A 1 70  ? -15.605 8.313   6.998   1.00 11.13 ? 70  PHE A CA  1 
ATOM   562  C  C   . PHE A 1 70  ? -15.337 9.843   6.947   1.00 11.80 ? 70  PHE A C   1 
ATOM   563  O  O   . PHE A 1 70  ? -14.262 10.332  7.331   1.00 11.70 ? 70  PHE A O   1 
ATOM   564  C  CB  . PHE A 1 70  ? -16.363 7.944   8.292   1.00 10.83 ? 70  PHE A CB  1 
ATOM   565  C  CG  . PHE A 1 70  ? -16.905 6.590   8.283   1.00 9.57  ? 70  PHE A CG  1 
ATOM   566  C  CD1 . PHE A 1 70  ? -16.076 5.485   8.487   1.00 9.48  ? 70  PHE A CD1 1 
ATOM   567  C  CD2 . PHE A 1 70  ? -18.268 6.335   7.986   1.00 10.12 ? 70  PHE A CD2 1 
ATOM   568  C  CE1 . PHE A 1 70  ? -16.597 4.141   8.438   1.00 7.11  ? 70  PHE A CE1 1 
ATOM   569  C  CE2 . PHE A 1 70  ? -18.775 5.060   7.946   1.00 7.73  ? 70  PHE A CE2 1 
ATOM   570  C  CZ  . PHE A 1 70  ? -17.937 3.942   8.120   1.00 12.58 ? 70  PHE A CZ  1 
ATOM   571  N  N   . ASP A 1 71  ? -16.341 10.567  6.465   1.00 14.56 ? 71  ASP A N   1 
ATOM   572  C  CA  . ASP A 1 71  ? -16.343 12.007  6.525   1.00 14.07 ? 71  ASP A CA  1 
ATOM   573  C  C   . ASP A 1 71  ? -16.616 12.445  7.960   1.00 14.71 ? 71  ASP A C   1 
ATOM   574  O  O   . ASP A 1 71  ? -17.704 12.210  8.520   1.00 16.77 ? 71  ASP A O   1 
ATOM   575  C  CB  . ASP A 1 71  ? -17.385 12.529  5.581   1.00 15.88 ? 71  ASP A CB  1 
ATOM   576  C  CG  . ASP A 1 71  ? -17.535 14.075  5.631   1.00 19.27 ? 71  ASP A CG  1 
ATOM   577  O  OD1 . ASP A 1 71  ? -16.770 14.747  6.358   1.00 19.32 ? 71  ASP A OD1 1 
ATOM   578  O  OD2 . ASP A 1 71  ? -18.427 14.555  4.884   1.00 28.09 ? 71  ASP A OD2 1 
ATOM   579  N  N   . ASP A 1 72  ? -15.597 12.959  8.625   1.00 14.38 ? 72  ASP A N   1 
ATOM   580  C  CA  . ASP A 1 72  ? -15.748 13.371  10.044  1.00 15.80 ? 72  ASP A CA  1 
ATOM   581  C  C   . ASP A 1 72  ? -15.732 14.918  10.176  1.00 17.95 ? 72  ASP A C   1 
ATOM   582  O  O   . ASP A 1 72  ? -15.335 15.432  11.241  1.00 15.74 ? 72  ASP A O   1 
ATOM   583  C  CB  . ASP A 1 72  ? -14.668 12.737  10.937  1.00 16.48 ? 72  ASP A CB  1 
ATOM   584  C  CG  . ASP A 1 72  ? -13.243 13.182  10.568  1.00 18.82 ? 72  ASP A CG  1 
ATOM   585  O  OD1 . ASP A 1 72  ? -13.041 13.747  9.467   1.00 17.35 ? 72  ASP A OD1 1 
ATOM   586  O  OD2 . ASP A 1 72  ? -12.309 12.951  11.345  1.00 16.37 ? 72  ASP A OD2 1 
ATOM   587  N  N   . SER A 1 73  ? -16.070 15.612  9.088   1.00 18.22 ? 73  SER A N   1 
ATOM   588  C  CA  . SER A 1 73  ? -16.065 17.138  9.102   1.00 20.59 ? 73  SER A CA  1 
ATOM   589  C  C   . SER A 1 73  ? -17.350 17.706  9.748   1.00 21.86 ? 73  SER A C   1 
ATOM   590  O  O   . SER A 1 73  ? -17.514 18.914  9.890   1.00 20.74 ? 73  SER A O   1 
ATOM   591  C  CB  . SER A 1 73  ? -15.850 17.725  7.704   1.00 18.85 ? 73  SER A CB  1 
ATOM   592  O  OG  . SER A 1 73  ? -16.938 17.386  6.838   1.00 18.86 ? 73  SER A OG  1 
ATOM   593  N  N   . GLN A 1 74  ? -18.244 16.815  10.188  1.00 22.22 ? 74  GLN A N   1 
ATOM   594  C  CA  . GLN A 1 74  ? -19.487 17.258  10.801  1.00 24.20 ? 74  GLN A CA  1 
ATOM   595  C  C   . GLN A 1 74  ? -19.871 16.206  11.815  1.00 23.23 ? 74  GLN A C   1 
ATOM   596  O  O   . GLN A 1 74  ? -19.362 15.120  11.772  1.00 21.13 ? 74  GLN A O   1 
ATOM   597  C  CB  . GLN A 1 74  ? -20.602 17.259  9.771   1.00 24.91 ? 74  GLN A CB  1 
ATOM   598  C  CG  . GLN A 1 74  ? -20.566 18.267  8.650   1.00 29.34 ? 74  GLN A CG  1 
ATOM   599  C  CD  . GLN A 1 74  ? -21.927 18.384  8.078   1.00 32.73 ? 74  GLN A CD  1 
ATOM   600  O  OE1 . GLN A 1 74  ? -22.175 17.983  6.941   1.00 33.29 ? 74  GLN A OE1 1 
ATOM   601  N  NE2 . GLN A 1 74  ? -22.854 18.900  8.888   1.00 36.36 ? 74  GLN A NE2 1 
ATOM   602  N  N   A ASP A 1 75  ? -20.727 16.538  12.795  0.50 23.57 ? 75  ASP A N   1 
ATOM   603  N  N   B ASP A 1 75  ? -20.869 16.601  12.587  0.50 22.90 ? 75  ASP A N   1 
ATOM   604  C  CA  A ASP A 1 75  ? -21.085 15.586  13.884  0.50 23.77 ? 75  ASP A CA  1 
ATOM   605  C  CA  B ASP A 1 75  ? -21.451 15.885  13.673  0.50 23.19 ? 75  ASP A CA  1 
ATOM   606  C  C   A ASP A 1 75  ? -22.213 14.660  13.409  0.50 24.88 ? 75  ASP A C   1 
ATOM   607  C  C   B ASP A 1 75  ? -22.338 14.784  13.051  0.50 24.21 ? 75  ASP A C   1 
ATOM   608  O  O   A ASP A 1 75  ? -23.416 14.894  13.664  0.50 25.42 ? 75  ASP A O   1 
ATOM   609  O  O   B ASP A 1 75  ? -23.544 15.027  12.833  0.50 25.34 ? 75  ASP A O   1 
ATOM   610  C  CB  A ASP A 1 75  ? -21.478 16.283  15.206  0.50 25.16 ? 75  ASP A CB  1 
ATOM   611  C  CB  B ASP A 1 75  ? -22.301 16.942  14.412  0.50 22.93 ? 75  ASP A CB  1 
ATOM   612  C  CG  A ASP A 1 75  ? -20.482 16.037  16.375  0.50 23.50 ? 75  ASP A CG  1 
ATOM   613  C  CG  B ASP A 1 75  ? -22.840 16.457  15.735  0.50 22.46 ? 75  ASP A CG  1 
ATOM   614  O  OD1 A ASP A 1 75  ? -19.736 15.028  16.405  0.50 22.52 ? 75  ASP A OD1 1 
ATOM   615  O  OD1 B ASP A 1 75  ? -22.406 15.388  16.178  0.50 17.80 ? 75  ASP A OD1 1 
ATOM   616  O  OD2 A ASP A 1 75  ? -20.502 16.854  17.328  0.50 30.45 ? 75  ASP A OD2 1 
ATOM   617  O  OD2 B ASP A 1 75  ? -23.702 17.159  16.323  0.50 21.50 ? 75  ASP A OD2 1 
ATOM   618  N  N   . LYS A 1 76  ? -21.780 13.607  12.735  1.00 24.07 ? 76  LYS A N   1 
ATOM   619  C  CA  . LYS A 1 76  ? -22.615 12.602  12.016  1.00 25.81 ? 76  LYS A CA  1 
ATOM   620  C  C   . LYS A 1 76  ? -22.715 11.147  12.556  1.00 25.92 ? 76  LYS A C   1 
ATOM   621  O  O   . LYS A 1 76  ? -23.835 10.531  12.560  1.00 31.66 ? 76  LYS A O   1 
ATOM   622  C  CB  . LYS A 1 76  ? -22.173 12.529  10.540  1.00 25.71 ? 76  LYS A CB  1 
ATOM   623  C  CG  . LYS A 1 76  ? -22.904 13.479  9.567   1.00 29.07 ? 76  LYS A CG  1 
ATOM   624  C  CD  . LYS A 1 76  ? -22.062 13.410  8.277   1.00 31.05 ? 76  LYS A CD  1 
ATOM   625  C  CE  . LYS A 1 76  ? -22.440 14.426  7.194   1.00 34.45 ? 76  LYS A CE  1 
ATOM   626  N  NZ  . LYS A 1 76  ? -21.286 14.437  6.262   1.00 31.23 ? 76  LYS A NZ  1 
ATOM   627  N  N   . ALA A 1 77  ? -21.600 10.554  12.890  1.00 22.31 ? 77  ALA A N   1 
ATOM   628  C  CA  . ALA A 1 77  ? -21.541 9.119   13.338  1.00 18.30 ? 77  ALA A CA  1 
ATOM   629  C  C   . ALA A 1 77  ? -20.768 9.290   14.653  1.00 18.01 ? 77  ALA A C   1 
ATOM   630  O  O   . ALA A 1 77  ? -19.568 9.566   14.621  1.00 19.48 ? 77  ALA A O   1 
ATOM   631  C  CB  . ALA A 1 77  ? -20.743 8.289   12.357  1.00 17.93 ? 77  ALA A CB  1 
ATOM   632  N  N   . VAL A 1 78  ? -21.454 9.234   15.764  1.00 16.08 ? 78  VAL A N   1 
ATOM   633  C  CA  . VAL A 1 78  ? -20.788 9.510   17.077  1.00 14.54 ? 78  VAL A CA  1 
ATOM   634  C  C   . VAL A 1 78  ? -21.011 8.407   18.119  1.00 13.05 ? 78  VAL A C   1 
ATOM   635  O  O   . VAL A 1 78  ? -22.103 7.712   18.185  1.00 13.90 ? 78  VAL A O   1 
ATOM   636  C  CB  . VAL A 1 78  ? -21.259 10.862  17.705  1.00 17.03 ? 78  VAL A CB  1 
ATOM   637  C  CG1 . VAL A 1 78  ? -21.002 12.066  16.760  1.00 17.02 ? 78  VAL A CG1 1 
ATOM   638  C  CG2 . VAL A 1 78  ? -22.634 10.784  18.098  1.00 15.61 ? 78  VAL A CG2 1 
ATOM   639  N  N   . LEU A 1 79  ? -20.000 8.268   18.959  1.00 11.73 ? 79  LEU A N   1 
ATOM   640  C  CA  . LEU A 1 79  ? -20.020 7.356   20.048  1.00 11.65 ? 79  LEU A CA  1 
ATOM   641  C  C   . LEU A 1 79  ? -19.966 8.249   21.296  1.00 12.55 ? 79  LEU A C   1 
ATOM   642  O  O   . LEU A 1 79  ? -19.174 9.209   21.392  1.00 11.13 ? 79  LEU A O   1 
ATOM   643  C  CB  . LEU A 1 79  ? -18.739 6.471   19.910  1.00 10.46 ? 79  LEU A CB  1 
ATOM   644  C  CG  . LEU A 1 79  ? -18.664 5.473   21.049  1.00 12.56 ? 79  LEU A CG  1 
ATOM   645  C  CD1 . LEU A 1 79  ? -19.765 4.435   20.990  1.00 13.25 ? 79  LEU A CD1 1 
ATOM   646  C  CD2 . LEU A 1 79  ? -17.303 4.742   21.069  1.00 10.48 ? 79  LEU A CD2 1 
ATOM   647  N  N   . LYS A 1 80  ? -20.810 7.902   22.259  1.00 10.73 ? 80  LYS A N   1 
ATOM   648  C  CA  . LYS A 1 80  ? -20.897 8.599   23.536  1.00 13.85 ? 80  LYS A CA  1 
ATOM   649  C  C   . LYS A 1 80  ? -21.480 7.729   24.616  1.00 13.66 ? 80  LYS A C   1 
ATOM   650  O  O   . LYS A 1 80  ? -21.840 6.585   24.348  1.00 12.26 ? 80  LYS A O   1 
ATOM   651  C  CB  . LYS A 1 80  ? -21.676 9.916   23.401  1.00 16.61 ? 80  LYS A CB  1 
ATOM   652  C  CG  . LYS A 1 80  ? -23.181 9.805   23.189  1.00 15.75 ? 80  LYS A CG  1 
ATOM   653  C  CD  . LYS A 1 80  ? -23.769 11.249  22.981  1.00 19.88 ? 80  LYS A CD  1 
ATOM   654  C  CE  . LYS A 1 80  ? -23.024 11.943  21.839  1.00 27.26 ? 80  LYS A CE  1 
ATOM   655  N  NZ  . LYS A 1 80  ? -23.961 12.657  20.852  1.00 38.35 ? 80  LYS A NZ  1 
ATOM   656  N  N   . GLY A 1 81  ? -21.516 8.254   25.841  1.00 11.95 ? 81  GLY A N   1 
ATOM   657  C  CA  . GLY A 1 81  ? -22.022 7.456   26.962  1.00 13.43 ? 81  GLY A CA  1 
ATOM   658  C  C   . GLY A 1 81  ? -21.055 6.361   27.224  1.00 15.28 ? 81  GLY A C   1 
ATOM   659  O  O   . GLY A 1 81  ? -19.837 6.545   27.004  1.00 14.01 ? 81  GLY A O   1 
ATOM   660  N  N   . GLY A 1 82  ? -21.543 5.247   27.777  1.00 15.91 ? 82  GLY A N   1 
ATOM   661  C  CA  . GLY A 1 82  ? -20.571 4.179   28.161  1.00 15.26 ? 82  GLY A CA  1 
ATOM   662  C  C   . GLY A 1 82  ? -19.687 4.783   29.281  1.00 13.73 ? 82  GLY A C   1 
ATOM   663  O  O   . GLY A 1 82  ? -20.210 5.499   30.183  1.00 15.35 ? 82  GLY A O   1 
ATOM   664  N  N   . PRO A 1 83  ? -18.315 4.622   29.205  1.00 11.81 ? 83  PRO A N   1 
ATOM   665  C  CA  . PRO A 1 83  ? -17.412 5.229   30.186  1.00 12.09 ? 83  PRO A CA  1 
ATOM   666  C  C   . PRO A 1 83  ? -17.006 6.674   29.787  1.00 12.62 ? 83  PRO A C   1 
ATOM   667  O  O   . PRO A 1 83  ? -16.228 7.345   30.468  1.00 16.05 ? 83  PRO A O   1 
ATOM   668  C  CB  . PRO A 1 83  ? -16.131 4.383   30.044  1.00 13.49 ? 83  PRO A CB  1 
ATOM   669  C  CG  . PRO A 1 83  ? -16.117 4.000   28.585  1.00 11.44 ? 83  PRO A CG  1 
ATOM   670  C  CD  . PRO A 1 83  ? -17.557 3.841   28.162  1.00 10.39 ? 83  PRO A CD  1 
ATOM   671  N  N   . LEU A 1 84  ? -17.503 7.134   28.637  1.00 12.30 ? 84  LEU A N   1 
ATOM   672  C  CA  . LEU A 1 84  ? -16.974 8.361   28.014  1.00 11.01 ? 84  LEU A CA  1 
ATOM   673  C  C   . LEU A 1 84  ? -17.673 9.612   28.563  1.00 14.35 ? 84  LEU A C   1 
ATOM   674  O  O   . LEU A 1 84  ? -18.899 9.611   28.886  1.00 15.32 ? 84  LEU A O   1 
ATOM   675  C  CB  . LEU A 1 84  ? -17.204 8.341   26.523  1.00 11.21 ? 84  LEU A CB  1 
ATOM   676  C  CG  . LEU A 1 84  ? -16.671 7.106   25.788  1.00 9.94  ? 84  LEU A CG  1 
ATOM   677  C  CD1 . LEU A 1 84  ? -17.166 7.066   24.340  1.00 10.09 ? 84  LEU A CD1 1 
ATOM   678  C  CD2 . LEU A 1 84  ? -15.037 7.095   25.836  1.00 10.57 ? 84  LEU A CD2 1 
ATOM   679  N  N   . ASP A 1 85  ? -16.868 10.661  28.607  1.00 15.40 ? 85  ASP A N   1 
ATOM   680  C  CA  . ASP A 1 85  ? -17.337 12.046  28.792  1.00 19.97 ? 85  ASP A CA  1 
ATOM   681  C  C   . ASP A 1 85  ? -17.286 12.693  27.436  1.00 20.64 ? 85  ASP A C   1 
ATOM   682  O  O   . ASP A 1 85  ? -16.263 12.702  26.718  1.00 22.33 ? 85  ASP A O   1 
ATOM   683  C  CB  . ASP A 1 85  ? -16.399 12.767  29.771  1.00 21.06 ? 85  ASP A CB  1 
ATOM   684  C  CG  . ASP A 1 85  ? -16.532 12.232  31.172  1.00 28.72 ? 85  ASP A CG  1 
ATOM   685  O  OD1 . ASP A 1 85  ? -17.654 11.776  31.554  1.00 31.96 ? 85  ASP A OD1 1 
ATOM   686  O  OD2 . ASP A 1 85  ? -15.513 12.279  31.921  1.00 32.91 ? 85  ASP A OD2 1 
ATOM   687  N  N   . GLY A 1 86  ? -18.398 13.260  27.031  1.00 21.57 ? 86  GLY A N   1 
ATOM   688  C  CA  . GLY A 1 86  ? -18.411 14.008  25.802  1.00 19.33 ? 86  GLY A CA  1 
ATOM   689  C  C   . GLY A 1 86  ? -18.668 13.107  24.585  1.00 19.32 ? 86  GLY A C   1 
ATOM   690  O  O   . GLY A 1 86  ? -19.203 11.968  24.720  1.00 20.00 ? 86  GLY A O   1 
ATOM   691  N  N   . THR A 1 87  ? -18.232 13.603  23.436  1.00 15.59 ? 87  THR A N   1 
ATOM   692  C  CA  . THR A 1 87  ? -18.703 13.155  22.144  1.00 16.77 ? 87  THR A CA  1 
ATOM   693  C  C   . THR A 1 87  ? -17.493 12.782  21.288  1.00 14.69 ? 87  THR A C   1 
ATOM   694  O  O   . THR A 1 87  ? -16.529 13.546  21.188  1.00 12.20 ? 87  THR A O   1 
ATOM   695  C  CB  . THR A 1 87  ? -19.550 14.287  21.476  1.00 18.36 ? 87  THR A CB  1 
ATOM   696  O  OG1 . THR A 1 87  ? -20.854 14.236  22.116  1.00 24.89 ? 87  THR A OG1 1 
ATOM   697  C  CG2 . THR A 1 87  ? -19.673 14.054  19.974  1.00 24.64 ? 87  THR A CG2 1 
ATOM   698  N  N   . TYR A 1 88  ? -17.524 11.574  20.720  1.00 10.82 ? 88  TYR A N   1 
ATOM   699  C  CA  . TYR A 1 88  ? -16.371 11.091  19.924  1.00 10.72 ? 88  TYR A CA  1 
ATOM   700  C  C   . TYR A 1 88  ? -16.887 10.812  18.517  1.00 10.53 ? 88  TYR A C   1 
ATOM   701  O  O   . TYR A 1 88  ? -17.885 10.064  18.342  1.00 12.67 ? 88  TYR A O   1 
ATOM   702  C  CB  . TYR A 1 88  ? -15.735 9.828   20.504  1.00 8.91  ? 88  TYR A CB  1 
ATOM   703  C  CG  . TYR A 1 88  ? -14.986 10.044  21.853  1.00 10.61 ? 88  TYR A CG  1 
ATOM   704  C  CD1 . TYR A 1 88  ? -15.680 10.354  23.033  1.00 8.95  ? 88  TYR A CD1 1 
ATOM   705  C  CD2 . TYR A 1 88  ? -13.554 9.907   21.925  1.00 9.32  ? 88  TYR A CD2 1 
ATOM   706  C  CE1 . TYR A 1 88  ? -14.966 10.536  24.246  1.00 8.08  ? 88  TYR A CE1 1 
ATOM   707  C  CE2 . TYR A 1 88  ? -12.818 10.093  23.127  1.00 8.24  ? 88  TYR A CE2 1 
ATOM   708  C  CZ  . TYR A 1 88  ? -13.544 10.414  24.259  1.00 8.62  ? 88  TYR A CZ  1 
ATOM   709  O  OH  . TYR A 1 88  ? -12.890 10.505  25.405  1.00 7.77  ? 88  TYR A OH  1 
ATOM   710  N  N   . ARG A 1 89  ? -16.200 11.295  17.513  1.00 8.45  ? 89  ARG A N   1 
ATOM   711  C  CA  . ARG A 1 89  ? -16.682 11.171  16.140  1.00 8.01  ? 89  ARG A CA  1 
ATOM   712  C  C   . ARG A 1 89  ? -15.962 10.027  15.372  1.00 9.02  ? 89  ARG A C   1 
ATOM   713  O  O   . ARG A 1 89  ? -14.718 9.947   15.433  1.00 6.85  ? 89  ARG A O   1 
ATOM   714  C  CB  . ARG A 1 89  ? -16.379 12.474  15.430  1.00 12.12 ? 89  ARG A CB  1 
ATOM   715  C  CG  . ARG A 1 89  ? -17.123 12.636  14.224  1.00 15.44 ? 89  ARG A CG  1 
ATOM   716  C  CD  . ARG A 1 89  ? -16.801 14.132  13.729  1.00 14.43 ? 89  ARG A CD  1 
ATOM   717  N  NE  . ARG A 1 89  ? -17.524 15.145  14.509  1.00 18.57 ? 89  ARG A NE  1 
ATOM   718  C  CZ  . ARG A 1 89  ? -17.415 16.453  14.303  1.00 21.80 ? 89  ARG A CZ  1 
ATOM   719  N  NH1 . ARG A 1 89  ? -16.610 16.907  13.345  1.00 21.05 ? 89  ARG A NH1 1 
ATOM   720  N  NH2 . ARG A 1 89  ? -18.132 17.310  15.033  1.00 20.03 ? 89  ARG A NH2 1 
ATOM   721  N  N   . LEU A 1 90  ? -16.728 9.191   14.658  1.00 7.53  ? 90  LEU A N   1 
ATOM   722  C  CA  . LEU A 1 90  ? -16.144 8.114   13.884  1.00 7.34  ? 90  LEU A CA  1 
ATOM   723  C  C   . LEU A 1 90  ? -15.256 8.690   12.726  1.00 7.59  ? 90  LEU A C   1 
ATOM   724  O  O   . LEU A 1 90  ? -15.752 9.485   11.860  1.00 8.82  ? 90  LEU A O   1 
ATOM   725  C  CB  . LEU A 1 90  ? -17.286 7.294   13.277  1.00 7.40  ? 90  LEU A CB  1 
ATOM   726  C  CG  . LEU A 1 90  ? -16.827 6.096   12.438  1.00 9.08  ? 90  LEU A CG  1 
ATOM   727  C  CD1 . LEU A 1 90  ? -15.999 5.164   13.335  1.00 8.69  ? 90  LEU A CD1 1 
ATOM   728  C  CD2 . LEU A 1 90  ? -18.077 5.391   11.810  1.00 10.50 ? 90  LEU A CD2 1 
ATOM   729  N  N   . ILE A 1 91  ? -14.028 8.195   12.634  1.00 7.16  ? 91  ILE A N   1 
ATOM   730  C  CA  . ILE A 1 91  ? -13.149 8.598   11.511  1.00 8.23  ? 91  ILE A CA  1 
ATOM   731  C  C   . ILE A 1 91  ? -12.851 7.404   10.567  1.00 7.00  ? 91  ILE A C   1 
ATOM   732  O  O   . ILE A 1 91  ? -12.798 7.589   9.386   1.00 9.64  ? 91  ILE A O   1 
ATOM   733  C  CB  . ILE A 1 91  ? -11.846 9.262   12.022  1.00 9.03  ? 91  ILE A CB  1 
ATOM   734  C  CG1 . ILE A 1 91  ? -10.930 9.597   10.805  1.00 8.93  ? 91  ILE A CG1 1 
ATOM   735  C  CG2 . ILE A 1 91  ? -11.126 8.439   13.066  1.00 9.08  ? 91  ILE A CG2 1 
ATOM   736  C  CD1 . ILE A 1 91  ? -9.780  10.614  11.213  1.00 10.43 ? 91  ILE A CD1 1 
ATOM   737  N  N   . GLN A 1 92  ? -12.727 6.190   11.131  1.00 5.30  ? 92  GLN A N   1 
ATOM   738  C  CA  . GLN A 1 92  ? -12.395 5.053   10.250  1.00 5.46  ? 92  GLN A CA  1 
ATOM   739  C  C   . GLN A 1 92  ? -12.629 3.758   11.034  1.00 7.63  ? 92  GLN A C   1 
ATOM   740  O  O   . GLN A 1 92  ? -12.675 3.785   12.267  1.00 7.00  ? 92  GLN A O   1 
ATOM   741  C  CB  . GLN A 1 92  ? -10.915 5.129   9.737   1.00 6.07  ? 92  GLN A CB  1 
ATOM   742  C  CG  . GLN A 1 92  ? -9.862  5.200   10.975  1.00 9.21  ? 92  GLN A CG  1 
ATOM   743  C  CD  . GLN A 1 92  ? -9.101  3.844   11.220  1.00 9.63  ? 92  GLN A CD  1 
ATOM   744  O  OE1 . GLN A 1 92  ? -9.691  2.767   11.076  1.00 7.41  ? 92  GLN A OE1 1 
ATOM   745  N  NE2 . GLN A 1 92  ? -7.798  3.942   11.562  1.00 11.90 ? 92  GLN A NE2 1 
ATOM   746  N  N   . PHE A 1 93  ? -12.838 2.667   10.311  1.00 6.43  ? 93  PHE A N   1 
ATOM   747  C  CA  . PHE A 1 93  ? -12.693 1.350   10.941  1.00 6.31  ? 93  PHE A CA  1 
ATOM   748  C  C   . PHE A 1 93  ? -11.737 0.465   10.180  1.00 6.79  ? 93  PHE A C   1 
ATOM   749  O  O   . PHE A 1 93  ? -11.520 0.673   8.984   1.00 6.76  ? 93  PHE A O   1 
ATOM   750  C  CB  . PHE A 1 93  ? -14.028 0.659   11.222  1.00 4.77  ? 93  PHE A CB  1 
ATOM   751  C  CG  . PHE A 1 93  ? -14.749 0.206   9.976   1.00 6.52  ? 93  PHE A CG  1 
ATOM   752  C  CD1 . PHE A 1 93  ? -14.311 -0.916  9.255   1.00 8.53  ? 93  PHE A CD1 1 
ATOM   753  C  CD2 . PHE A 1 93  ? -15.960 0.914   9.564   1.00 10.32 ? 93  PHE A CD2 1 
ATOM   754  C  CE1 . PHE A 1 93  ? -15.010 -1.388  8.123   1.00 9.11  ? 93  PHE A CE1 1 
ATOM   755  C  CE2 . PHE A 1 93  ? -16.678 0.461   8.444   1.00 9.03  ? 93  PHE A CE2 1 
ATOM   756  C  CZ  . PHE A 1 93  ? -16.198 -0.693  7.697   1.00 9.35  ? 93  PHE A CZ  1 
ATOM   757  N  N   . HIS A 1 94  ? -11.151 -0.516  10.862  1.00 6.70  ? 94  HIS A N   1 
ATOM   758  C  CA  . HIS A 1 94  ? -10.282 -1.476  10.223  1.00 3.90  ? 94  HIS A CA  1 
ATOM   759  C  C   . HIS A 1 94  ? -10.375 -2.776  11.086  1.00 5.85  ? 94  HIS A C   1 
ATOM   760  O  O   . HIS A 1 94  ? -10.995 -2.802  12.139  1.00 6.15  ? 94  HIS A O   1 
ATOM   761  C  CB  . HIS A 1 94  ? -8.808  -1.038  10.203  1.00 6.52  ? 94  HIS A CB  1 
ATOM   762  C  CG  . HIS A 1 94  ? -8.310  -0.699  11.598  1.00 5.90  ? 94  HIS A CG  1 
ATOM   763  N  ND1 . HIS A 1 94  ? -8.547  0.526   12.229  1.00 6.64  ? 94  HIS A ND1 1 
ATOM   764  C  CD2 . HIS A 1 94  ? -7.640  -1.468  12.472  1.00 8.09  ? 94  HIS A CD2 1 
ATOM   765  C  CE1 . HIS A 1 94  ? -8.005  0.465   13.451  1.00 5.71  ? 94  HIS A CE1 1 
ATOM   766  N  NE2 . HIS A 1 94  ? -7.494  -0.751  13.625  1.00 7.91  ? 94  HIS A NE2 1 
ATOM   767  N  N   . PHE A 1 95  ? -9.672  -3.756  10.599  1.00 3.57  ? 95  PHE A N   1 
ATOM   768  C  CA  . PHE A 1 95  ? -9.680  -5.091  11.303  1.00 6.52  ? 95  PHE A CA  1 
ATOM   769  C  C   . PHE A 1 95  ? -8.237  -5.556  11.487  1.00 7.00  ? 95  PHE A C   1 
ATOM   770  O  O   . PHE A 1 95  ? -7.305  -5.101  10.786  1.00 6.75  ? 95  PHE A O   1 
ATOM   771  C  CB  . PHE A 1 95  ? -10.370 -6.184  10.474  1.00 8.52  ? 95  PHE A CB  1 
ATOM   772  C  CG  . PHE A 1 95  ? -11.793 -5.880  10.146  1.00 5.71  ? 95  PHE A CG  1 
ATOM   773  C  CD1 . PHE A 1 95  ? -12.110 -5.035  9.061   1.00 7.00  ? 95  PHE A CD1 1 
ATOM   774  C  CD2 . PHE A 1 95  ? -12.824 -6.560  10.827  1.00 10.11 ? 95  PHE A CD2 1 
ATOM   775  C  CE1 . PHE A 1 95  ? -13.468 -4.827  8.716   1.00 8.50  ? 95  PHE A CE1 1 
ATOM   776  C  CE2 . PHE A 1 95  ? -14.164 -6.354  10.490  1.00 9.52  ? 95  PHE A CE2 1 
ATOM   777  C  CZ  . PHE A 1 95  ? -14.457 -5.497  9.394   1.00 7.49  ? 95  PHE A CZ  1 
ATOM   778  N  N   . HIS A 1 96  ? -8.079  -6.514  12.410  1.00 5.74  ? 96  HIS A N   1 
ATOM   779  C  CA  . HIS A 1 96  ? -6.800  -7.288  12.585  1.00 4.74  ? 96  HIS A CA  1 
ATOM   780  C  C   . HIS A 1 96  ? -7.183  -8.747  12.463  1.00 5.05  ? 96  HIS A C   1 
ATOM   781  O  O   . HIS A 1 96  ? -8.271  -9.118  12.957  1.00 6.19  ? 96  HIS A O   1 
ATOM   782  C  CB  . HIS A 1 96  ? -6.151  -7.047  13.924  1.00 6.76  ? 96  HIS A CB  1 
ATOM   783  C  CG  . HIS A 1 96  ? -5.923  -5.574  14.225  1.00 5.94  ? 96  HIS A CG  1 
ATOM   784  N  ND1 . HIS A 1 96  ? -4.702  -4.976  13.950  1.00 6.75  ? 96  HIS A ND1 1 
ATOM   785  C  CD2 . HIS A 1 96  ? -6.759  -4.577  14.626  1.00 7.33  ? 96  HIS A CD2 1 
ATOM   786  C  CE1 . HIS A 1 96  ? -4.737  -3.711  14.359  1.00 8.85  ? 96  HIS A CE1 1 
ATOM   787  N  NE2 . HIS A 1 96  ? -6.001  -3.412  14.663  1.00 7.35  ? 96  HIS A NE2 1 
ATOM   788  N  N   . TRP A 1 97  ? -6.413  -9.538  11.739  1.00 4.42  ? 97  TRP A N   1 
ATOM   789  C  CA  . TRP A 1 97  ? -6.898  -10.946 11.617  1.00 7.61  ? 97  TRP A CA  1 
ATOM   790  C  C   . TRP A 1 97  ? -5.736  -11.867 11.483  1.00 5.94  ? 97  TRP A C   1 
ATOM   791  O  O   . TRP A 1 97  ? -4.577  -11.431 11.371  1.00 7.47  ? 97  TRP A O   1 
ATOM   792  C  CB  . TRP A 1 97  ? -7.846  -11.091 10.442  1.00 5.37  ? 97  TRP A CB  1 
ATOM   793  C  CG  . TRP A 1 97  ? -7.200  -10.697 9.098   1.00 6.85  ? 97  TRP A CG  1 
ATOM   794  C  CD1 . TRP A 1 97  ? -6.520  -11.559 8.245   1.00 6.95  ? 97  TRP A CD1 1 
ATOM   795  C  CD2 . TRP A 1 97  ? -7.134  -9.382  8.518   1.00 9.14  ? 97  TRP A CD2 1 
ATOM   796  N  NE1 . TRP A 1 97  ? -6.111  -10.841 7.081   1.00 8.40  ? 97  TRP A NE1 1 
ATOM   797  C  CE2 . TRP A 1 97  ? -6.430  -9.506  7.250   1.00 7.98  ? 97  TRP A CE2 1 
ATOM   798  C  CE3 . TRP A 1 97  ? -7.545  -8.071  8.965   1.00 6.35  ? 97  TRP A CE3 1 
ATOM   799  C  CZ2 . TRP A 1 97  ? -6.189  -8.401  6.402   1.00 8.15  ? 97  TRP A CZ2 1 
ATOM   800  C  CZ3 . TRP A 1 97  ? -7.337  -6.932  8.049   1.00 6.34  ? 97  TRP A CZ3 1 
ATOM   801  C  CH2 . TRP A 1 97  ? -6.653  -7.116  6.826   1.00 8.95  ? 97  TRP A CH2 1 
ATOM   802  N  N   . GLY A 1 98  ? -6.080  -13.176 11.483  1.00 6.06  ? 98  GLY A N   1 
ATOM   803  C  CA  . GLY A 1 98  ? -5.027  -14.211 11.477  1.00 7.30  ? 98  GLY A CA  1 
ATOM   804  C  C   . GLY A 1 98  ? -4.763  -14.885 10.156  1.00 8.17  ? 98  GLY A C   1 
ATOM   805  O  O   . GLY A 1 98  ? -5.498  -14.703 9.159   1.00 8.92  ? 98  GLY A O   1 
ATOM   806  N  N   . SER A 1 99  ? -3.761  -15.775 10.169  1.00 8.39  ? 99  SER A N   1 
ATOM   807  C  CA  . SER A 1 99  ? -3.533  -16.614 9.014   1.00 9.83  ? 99  SER A CA  1 
ATOM   808  C  C   . SER A 1 99  ? -4.388  -17.881 9.128   1.00 10.81 ? 99  SER A C   1 
ATOM   809  O  O   . SER A 1 99  ? -4.501  -18.683 8.156   1.00 12.41 ? 99  SER A O   1 
ATOM   810  C  CB  . SER A 1 99  ? -2.054  -17.039 9.028   1.00 10.19 ? 99  SER A CB  1 
ATOM   811  O  OG  . SER A 1 99  ? -1.649  -17.599 10.283  1.00 10.15 ? 99  SER A OG  1 
ATOM   812  N  N   . LEU A 1 100 ? -4.940  -18.085 10.326  1.00 9.00  ? 100 LEU A N   1 
ATOM   813  C  CA  . LEU A 1 100 ? -5.726  -19.271 10.656  1.00 10.56 ? 100 LEU A CA  1 
ATOM   814  C  C   . LEU A 1 100 ? -6.919  -18.784 11.500  1.00 11.61 ? 100 LEU A C   1 
ATOM   815  O  O   . LEU A 1 100 ? -6.798  -17.789 12.220  1.00 8.94  ? 100 LEU A O   1 
ATOM   816  C  CB  . LEU A 1 100 ? -4.878  -20.278 11.511  1.00 12.51 ? 100 LEU A CB  1 
ATOM   817  C  CG  . LEU A 1 100 ? -3.540  -20.635 10.886  1.00 13.97 ? 100 LEU A CG  1 
ATOM   818  C  CD1 . LEU A 1 100 ? -2.665  -21.152 11.985  1.00 21.76 ? 100 LEU A CD1 1 
ATOM   819  C  CD2 . LEU A 1 100 ? -3.879  -21.750 9.908   1.00 16.80 ? 100 LEU A CD2 1 
ATOM   820  N  N   . ASP A 1 101 ? -8.010  -19.580 11.559  1.00 10.18 ? 101 ASP A N   1 
ATOM   821  C  CA  . ASP A 1 101 ? -9.194  -19.067 12.329  1.00 11.83 ? 101 ASP A CA  1 
ATOM   822  C  C   . ASP A 1 101 ? -8.896  -19.035 13.835  1.00 10.68 ? 101 ASP A C   1 
ATOM   823  O  O   . ASP A 1 101 ? -9.524  -18.268 14.584  1.00 11.85 ? 101 ASP A O   1 
ATOM   824  C  CB  . ASP A 1 101 ? -10.465 -19.918 12.146  1.00 10.66 ? 101 ASP A CB  1 
ATOM   825  C  CG  . ASP A 1 101 ? -10.936 -19.994 10.716  1.00 15.28 ? 101 ASP A CG  1 
ATOM   826  O  OD1 . ASP A 1 101 ? -10.564 -19.198 9.830   1.00 14.80 ? 101 ASP A OD1 1 
ATOM   827  O  OD2 . ASP A 1 101 ? -11.664 -20.974 10.463  1.00 20.32 ? 101 ASP A OD2 1 
ATOM   828  N  N   . GLY A 1 102 ? -7.885  -19.824 14.268  1.00 10.59 ? 102 GLY A N   1 
ATOM   829  C  CA  . GLY A 1 102 ? -7.552  -19.868 15.704  1.00 10.46 ? 102 GLY A CA  1 
ATOM   830  C  C   . GLY A 1 102 ? -6.832  -18.657 16.263  1.00 8.53  ? 102 GLY A C   1 
ATOM   831  O  O   . GLY A 1 102 ? -6.539  -18.591 17.460  1.00 9.29  ? 102 GLY A O   1 
ATOM   832  N  N   . GLN A 1 103 ? -6.553  -17.636 15.433  1.00 9.26  ? 103 GLN A N   1 
ATOM   833  C  CA  . GLN A 1 103 ? -5.846  -16.453 15.980  1.00 8.26  ? 103 GLN A CA  1 
ATOM   834  C  C   . GLN A 1 103 ? -6.159  -15.246 15.104  1.00 8.85  ? 103 GLN A C   1 
ATOM   835  O  O   . GLN A 1 103 ? -6.758  -15.410 14.007  1.00 7.56  ? 103 GLN A O   1 
ATOM   836  C  CB  . GLN A 1 103 ? -4.330  -16.695 15.991  1.00 9.35  ? 103 GLN A CB  1 
ATOM   837  C  CG  . GLN A 1 103 ? -3.776  -16.911 14.574  1.00 10.65 ? 103 GLN A CG  1 
ATOM   838  C  CD  . GLN A 1 103 ? -2.291  -17.367 14.693  1.00 18.88 ? 103 GLN A CD  1 
ATOM   839  O  OE1 . GLN A 1 103 ? -1.926  -18.050 15.654  1.00 21.01 ? 103 GLN A OE1 1 
ATOM   840  N  NE2 . GLN A 1 103 ? -1.440  -16.956 13.750  1.00 14.48 ? 103 GLN A NE2 1 
ATOM   841  N  N   . GLY A 1 104 ? -5.841  -14.073 15.633  1.00 8.85  ? 104 GLY A N   1 
ATOM   842  C  CA  . GLY A 1 104 ? -6.137  -12.897 14.850  1.00 7.39  ? 104 GLY A CA  1 
ATOM   843  C  C   . GLY A 1 104 ? -6.591  -11.717 15.654  1.00 8.61  ? 104 GLY A C   1 
ATOM   844  O  O   . GLY A 1 104 ? -6.358  -10.566 15.215  1.00 6.89  ? 104 GLY A O   1 
ATOM   845  N  N   . SER A 1 105 ? -7.305  -11.952 16.769  1.00 7.56  ? 105 SER A N   1 
ATOM   846  C  CA  . SER A 1 105 ? -7.756  -10.793 17.552  1.00 8.03  ? 105 SER A CA  1 
ATOM   847  C  C   . SER A 1 105 ? -6.492  -10.253 18.325  1.00 6.52  ? 105 SER A C   1 
ATOM   848  O  O   . SER A 1 105 ? -5.489  -10.983 18.526  1.00 7.98  ? 105 SER A O   1 
ATOM   849  C  CB  . SER A 1 105 ? -8.843  -11.195 18.528  1.00 6.44  ? 105 SER A CB  1 
ATOM   850  O  OG  . SER A 1 105 ? -8.405  -12.122 19.521  1.00 7.03  ? 105 SER A OG  1 
ATOM   851  N  N   . GLU A 1 106 ? -6.591  -9.016  18.775  1.00 8.47  ? 106 GLU A N   1 
ATOM   852  C  CA  . GLU A 1 106 ? -5.549  -8.366  19.544  1.00 6.63  ? 106 GLU A CA  1 
ATOM   853  C  C   . GLU A 1 106 ? -5.924  -8.523  21.027  1.00 6.44  ? 106 GLU A C   1 
ATOM   854  O  O   . GLU A 1 106 ? -5.186  -9.023  21.811  1.00 8.21  ? 106 GLU A O   1 
ATOM   855  C  CB  . GLU A 1 106 ? -5.542  -6.828  19.146  1.00 3.34  ? 106 GLU A CB  1 
ATOM   856  C  CG  . GLU A 1 106 ? -5.192  -6.654  17.654  1.00 8.65  ? 106 GLU A CG  1 
ATOM   857  C  CD  . GLU A 1 106 ? -4.532  -5.309  17.312  1.00 3.77  ? 106 GLU A CD  1 
ATOM   858  O  OE1 . GLU A 1 106 ? -5.108  -4.243  17.587  1.00 8.20  ? 106 GLU A OE1 1 
ATOM   859  O  OE2 . GLU A 1 106 ? -3.391  -5.430  16.865  1.00 8.39  ? 106 GLU A OE2 1 
ATOM   860  N  N   . HIS A 1 107 ? -7.136  -8.056  21.409  1.00 6.34  ? 107 HIS A N   1 
ATOM   861  C  CA  . HIS A 1 107 ? -7.576  -8.412  22.733  1.00 5.75  ? 107 HIS A CA  1 
ATOM   862  C  C   . HIS A 1 107 ? -7.955  -9.868  22.770  1.00 5.87  ? 107 HIS A C   1 
ATOM   863  O  O   . HIS A 1 107 ? -8.251  -10.442 21.719  1.00 7.67  ? 107 HIS A O   1 
ATOM   864  C  CB  . HIS A 1 107 ? -8.832  -7.625  23.119  1.00 6.89  ? 107 HIS A CB  1 
ATOM   865  C  CG  . HIS A 1 107 ? -8.551  -6.181  23.291  1.00 6.12  ? 107 HIS A CG  1 
ATOM   866  N  ND1 . HIS A 1 107 ? -8.653  -5.278  22.247  1.00 5.29  ? 107 HIS A ND1 1 
ATOM   867  C  CD2 . HIS A 1 107 ? -8.067  -5.496  24.350  1.00 8.37  ? 107 HIS A CD2 1 
ATOM   868  C  CE1 . HIS A 1 107 ? -8.221  -4.093  22.673  1.00 7.86  ? 107 HIS A CE1 1 
ATOM   869  N  NE2 . HIS A 1 107 ? -7.852  -4.205  23.943  1.00 6.81  ? 107 HIS A NE2 1 
ATOM   870  N  N   . THR A 1 108 ? -7.750  -10.416 23.956  1.00 6.34  ? 108 THR A N   1 
ATOM   871  C  CA  . THR A 1 108 ? -8.159  -11.823 24.244  1.00 5.08  ? 108 THR A CA  1 
ATOM   872  C  C   . THR A 1 108 ? -9.096  -11.876 25.452  1.00 7.04  ? 108 THR A C   1 
ATOM   873  O  O   . THR A 1 108 ? -9.165  -10.889 26.248  1.00 7.92  ? 108 THR A O   1 
ATOM   874  C  CB  . THR A 1 108 ? -6.948  -12.698 24.428  1.00 6.90  ? 108 THR A CB  1 
ATOM   875  O  OG1 . THR A 1 108 ? -6.071  -12.219 25.487  1.00 7.32  ? 108 THR A OG1 1 
ATOM   876  C  CG2 . THR A 1 108 ? -6.151  -12.798 23.122  1.00 5.80  ? 108 THR A CG2 1 
ATOM   877  N  N   . VAL A 1 109 ? -9.839  -12.988 25.581  1.00 7.13  ? 109 VAL A N   1 
ATOM   878  C  CA  . VAL A 1 109 ? -10.861 -13.071 26.671  1.00 8.15  ? 109 VAL A CA  1 
ATOM   879  C  C   . VAL A 1 109 ? -10.526 -14.371 27.413  1.00 8.15  ? 109 VAL A C   1 
ATOM   880  O  O   . VAL A 1 109 ? -10.655 -15.463 26.853  1.00 5.75  ? 109 VAL A O   1 
ATOM   881  C  CB  . VAL A 1 109 ? -12.312 -13.077 26.095  1.00 10.71 ? 109 VAL A CB  1 
ATOM   882  C  CG1 . VAL A 1 109 ? -13.393 -13.272 27.184  1.00 9.58  ? 109 VAL A CG1 1 
ATOM   883  C  CG2 . VAL A 1 109 ? -12.519 -11.709 25.339  1.00 8.84  ? 109 VAL A CG2 1 
ATOM   884  N  N   . ASP A 1 110 ? -10.081 -14.239 28.637  1.00 8.03  ? 110 ASP A N   1 
ATOM   885  C  CA  . ASP A 1 110 ? -9.464  -15.342 29.336  1.00 9.98  ? 110 ASP A CA  1 
ATOM   886  C  C   . ASP A 1 110 ? -8.524  -16.161 28.419  1.00 10.10 ? 110 ASP A C   1 
ATOM   887  O  O   . ASP A 1 110 ? -8.648  -17.396 28.371  1.00 10.22 ? 110 ASP A O   1 
ATOM   888  C  CB  . ASP A 1 110 ? -10.581 -16.203 29.883  1.00 10.26 ? 110 ASP A CB  1 
ATOM   889  C  CG  . ASP A 1 110 ? -11.495 -15.403 30.871  1.00 6.79  ? 110 ASP A CG  1 
ATOM   890  O  OD1 . ASP A 1 110 ? -10.930 -14.518 31.521  1.00 13.22 ? 110 ASP A OD1 1 
ATOM   891  O  OD2 . ASP A 1 110 ? -12.679 -15.766 30.976  1.00 15.16 ? 110 ASP A OD2 1 
ATOM   892  N  N   . LYS A 1 111 ? -7.610  -15.454 27.709  1.00 8.94  ? 111 LYS A N   1 
ATOM   893  C  CA  . LYS A 1 111 ? -6.594  -16.021 26.777  1.00 9.10  ? 111 LYS A CA  1 
ATOM   894  C  C   . LYS A 1 111 ? -7.173  -16.578 25.443  1.00 7.65  ? 111 LYS A C   1 
ATOM   895  O  O   . LYS A 1 111 ? -6.393  -16.989 24.558  1.00 9.61  ? 111 LYS A O   1 
ATOM   896  C  CB  . LYS A 1 111 ? -5.665  -17.028 27.504  1.00 10.85 ? 111 LYS A CB  1 
ATOM   897  C  CG  . LYS A 1 111 ? -5.037  -16.402 28.749  1.00 11.78 ? 111 LYS A CG  1 
ATOM   898  C  CD  . LYS A 1 111 ? -4.040  -15.260 28.312  1.00 14.06 ? 111 LYS A CD  1 
ATOM   899  C  CE  . LYS A 1 111 ? -3.291  -14.692 29.566  1.00 18.88 ? 111 LYS A CE  1 
ATOM   900  N  NZ  . LYS A 1 111 ? -2.208  -15.565 29.966  1.00 22.63 ? 111 LYS A NZ  1 
ATOM   901  N  N   . LYS A 1 112 ? -8.488  -16.547 25.289  1.00 5.84  ? 112 LYS A N   1 
ATOM   902  C  CA  . LYS A 1 112 ? -9.136  -16.972 24.055  1.00 7.12  ? 112 LYS A CA  1 
ATOM   903  C  C   . LYS A 1 112 ? -8.765  -15.912 22.944  1.00 9.21  ? 112 LYS A C   1 
ATOM   904  O  O   . LYS A 1 112 ? -9.001  -14.712 23.151  1.00 8.69  ? 112 LYS A O   1 
ATOM   905  C  CB  . LYS A 1 112 ? -10.628 -17.060 24.198  1.00 7.65  ? 112 LYS A CB  1 
ATOM   906  C  CG  . LYS A 1 112 ? -11.273 -17.422 22.833  1.00 9.10  ? 112 LYS A CG  1 
ATOM   907  C  CD  . LYS A 1 112 ? -12.787 -17.466 23.002  1.00 13.37 ? 112 LYS A CD  1 
ATOM   908  C  CE  . LYS A 1 112 ? -13.446 -17.526 21.605  1.00 13.78 ? 112 LYS A CE  1 
ATOM   909  N  NZ  . LYS A 1 112 ? -13.319 -18.936 21.100  1.00 10.65 ? 112 LYS A NZ  1 
ATOM   910  N  N   . LYS A 1 113 ? -8.242  -16.394 21.800  1.00 8.93  ? 113 LYS A N   1 
ATOM   911  C  CA  . LYS A 1 113 ? -7.994  -15.515 20.592  1.00 9.44  ? 113 LYS A CA  1 
ATOM   912  C  C   . LYS A 1 113 ? -9.160  -15.756 19.575  1.00 9.45  ? 113 LYS A C   1 
ATOM   913  O  O   . LYS A 1 113 ? -9.574  -16.918 19.332  1.00 10.06 ? 113 LYS A O   1 
ATOM   914  C  CB  . LYS A 1 113 ? -6.631  -15.881 19.942  1.00 10.84 ? 113 LYS A CB  1 
ATOM   915  C  CG  . LYS A 1 113 ? -5.481  -15.602 20.805  1.00 9.02  ? 113 LYS A CG  1 
ATOM   916  C  CD  . LYS A 1 113 ? -4.318  -16.285 20.093  1.00 10.46 ? 113 LYS A CD  1 
ATOM   917  C  CE  . LYS A 1 113 ? -3.059  -15.555 20.482  1.00 14.70 ? 113 LYS A CE  1 
ATOM   918  N  NZ  . LYS A 1 113 ? -2.510  -16.321 21.569  1.00 20.25 ? 113 LYS A NZ  1 
ATOM   919  N  N   . TYR A 1 114 ? -9.801  -14.650 19.133  1.00 7.50  ? 114 TYR A N   1 
ATOM   920  C  CA  . TYR A 1 114 ? -10.799 -14.744 18.100  1.00 8.41  ? 114 TYR A CA  1 
ATOM   921  C  C   . TYR A 1 114 ? -10.140 -14.704 16.708  1.00 7.24  ? 114 TYR A C   1 
ATOM   922  O  O   . TYR A 1 114 ? -8.937  -14.415 16.624  1.00 7.07  ? 114 TYR A O   1 
ATOM   923  C  CB  . TYR A 1 114 ? -11.799 -13.617 18.219  1.00 6.35  ? 114 TYR A CB  1 
ATOM   924  C  CG  . TYR A 1 114 ? -12.790 -13.852 19.347  1.00 8.80  ? 114 TYR A CG  1 
ATOM   925  C  CD1 . TYR A 1 114 ? -12.478 -13.424 20.661  1.00 9.23  ? 114 TYR A CD1 1 
ATOM   926  C  CD2 . TYR A 1 114 ? -13.996 -14.522 19.126  1.00 8.72  ? 114 TYR A CD2 1 
ATOM   927  C  CE1 . TYR A 1 114 ? -13.391 -13.678 21.764  1.00 11.44 ? 114 TYR A CE1 1 
ATOM   928  C  CE2 . TYR A 1 114 ? -14.948 -14.693 20.179  1.00 12.25 ? 114 TYR A CE2 1 
ATOM   929  C  CZ  . TYR A 1 114 ? -14.598 -14.274 21.504  1.00 11.88 ? 114 TYR A CZ  1 
ATOM   930  O  OH  . TYR A 1 114 ? -15.489 -14.422 22.580  1.00 14.53 ? 114 TYR A OH  1 
ATOM   931  N  N   . ALA A 1 115 ? -10.929 -14.954 15.647  1.00 8.01  ? 115 ALA A N   1 
ATOM   932  C  CA  . ALA A 1 115 ? -10.355 -15.078 14.311  1.00 8.35  ? 115 ALA A CA  1 
ATOM   933  C  C   . ALA A 1 115 ? -9.981  -13.670 13.823  1.00 6.68  ? 115 ALA A C   1 
ATOM   934  O  O   . ALA A 1 115 ? -9.129  -13.526 12.948  1.00 8.14  ? 115 ALA A O   1 
ATOM   935  C  CB  . ALA A 1 115 ? -11.430 -15.727 13.371  1.00 9.43  ? 115 ALA A CB  1 
ATOM   936  N  N   . ALA A 1 116 ? -10.653 -12.631 14.363  1.00 6.03  ? 116 ALA A N   1 
ATOM   937  C  CA  . ALA A 1 116 ? -10.319 -11.276 13.908  1.00 6.52  ? 116 ALA A CA  1 
ATOM   938  C  C   . ALA A 1 116 ? -10.886 -10.286 14.944  1.00 5.85  ? 116 ALA A C   1 
ATOM   939  O  O   . ALA A 1 116 ? -11.600 -10.684 15.896  1.00 6.71  ? 116 ALA A O   1 
ATOM   940  C  CB  . ALA A 1 116 ? -10.835 -10.916 12.440  1.00 5.73  ? 116 ALA A CB  1 
ATOM   941  N  N   . GLU A 1 117 ? -10.575 -9.031  14.749  1.00 5.81  ? 117 GLU A N   1 
ATOM   942  C  CA  . GLU A 1 117 ? -11.096 -8.019  15.655  1.00 6.62  ? 117 GLU A CA  1 
ATOM   943  C  C   . GLU A 1 117 ? -11.306 -6.699  14.863  1.00 6.96  ? 117 GLU A C   1 
ATOM   944  O  O   . GLU A 1 117 ? -10.433 -6.299  14.112  1.00 6.98  ? 117 GLU A O   1 
ATOM   945  C  CB  . GLU A 1 117 ? -10.136 -7.760  16.829  1.00 6.84  ? 117 GLU A CB  1 
ATOM   946  C  CG  . GLU A 1 117 ? -10.678 -6.768  17.930  1.00 6.29  ? 117 GLU A CG  1 
ATOM   947  C  CD  . GLU A 1 117 ? -9.703  -6.709  19.102  1.00 5.85  ? 117 GLU A CD  1 
ATOM   948  O  OE1 . GLU A 1 117 ? -9.068  -7.757  19.443  1.00 7.78  ? 117 GLU A OE1 1 
ATOM   949  O  OE2 . GLU A 1 117 ? -9.678  -5.621  19.748  1.00 10.03 ? 117 GLU A OE2 1 
ATOM   950  N  N   . LEU A 1 118 ? -12.507 -6.154  14.927  1.00 5.53  ? 118 LEU A N   1 
ATOM   951  C  CA  . LEU A 1 118 ? -12.843 -4.895  14.257  1.00 4.08  ? 118 LEU A CA  1 
ATOM   952  C  C   . LEU A 1 118 ? -12.623 -3.705  15.265  1.00 4.45  ? 118 LEU A C   1 
ATOM   953  O  O   . LEU A 1 118 ? -12.984 -3.791  16.449  1.00 4.52  ? 118 LEU A O   1 
ATOM   954  C  CB  . LEU A 1 118 ? -14.361 -4.988  13.908  1.00 4.42  ? 118 LEU A CB  1 
ATOM   955  C  CG  . LEU A 1 118 ? -15.093 -3.673  13.543  1.00 7.20  ? 118 LEU A CG  1 
ATOM   956  C  CD1 . LEU A 1 118 ? -14.471 -3.073  12.192  1.00 7.93  ? 118 LEU A CD1 1 
ATOM   957  C  CD2 . LEU A 1 118 ? -16.602 -3.977  13.420  1.00 6.39  ? 118 LEU A CD2 1 
ATOM   958  N  N   . HIS A 1 119 ? -12.017 -2.642  14.744  1.00 4.60  ? 119 HIS A N   1 
ATOM   959  C  CA  . HIS A 1 119 ? -11.771 -1.443  15.518  1.00 5.31  ? 119 HIS A CA  1 
ATOM   960  C  C   . HIS A 1 119 ? -12.472 -0.268  14.885  1.00 6.26  ? 119 HIS A C   1 
ATOM   961  O  O   . HIS A 1 119 ? -12.066 0.067   13.751  1.00 5.84  ? 119 HIS A O   1 
ATOM   962  C  CB  . HIS A 1 119 ? -10.228 -1.225  15.591  1.00 4.79  ? 119 HIS A CB  1 
ATOM   963  C  CG  . HIS A 1 119 ? -9.569  -2.206  16.535  1.00 4.89  ? 119 HIS A CG  1 
ATOM   964  N  ND1 . HIS A 1 119 ? -8.203  -2.435  16.560  1.00 6.80  ? 119 HIS A ND1 1 
ATOM   965  C  CD2 . HIS A 1 119 ? -10.102 -3.031  17.494  1.00 5.89  ? 119 HIS A CD2 1 
ATOM   966  C  CE1 . HIS A 1 119 ? -7.916  -3.333  17.465  1.00 4.29  ? 119 HIS A CE1 1 
ATOM   967  N  NE2 . HIS A 1 119 ? -9.041  -3.700  18.070  1.00 7.78  ? 119 HIS A NE2 1 
ATOM   968  N  N   . LEU A 1 120 ? -13.534 0.271   15.531  1.00 5.51  ? 120 LEU A N   1 
ATOM   969  C  CA  . LEU A 1 120 ? -14.252 1.511   15.050  1.00 5.86  ? 120 LEU A CA  1 
ATOM   970  C  C   . LEU A 1 120 ? -13.617 2.678   15.797  1.00 5.50  ? 120 LEU A C   1 
ATOM   971  O  O   . LEU A 1 120 ? -13.734 2.747   17.042  1.00 5.60  ? 120 LEU A O   1 
ATOM   972  C  CB  . LEU A 1 120 ? -15.736 1.491   15.356  1.00 7.18  ? 120 LEU A CB  1 
ATOM   973  C  CG  . LEU A 1 120 ? -16.347 0.380   14.457  1.00 7.24  ? 120 LEU A CG  1 
ATOM   974  C  CD1 . LEU A 1 120 ? -17.136 -0.655  15.194  1.00 10.94 ? 120 LEU A CD1 1 
ATOM   975  C  CD2 . LEU A 1 120 ? -17.144 0.986   13.248  1.00 6.54  ? 120 LEU A CD2 1 
ATOM   976  N  N   . VAL A 1 121 ? -12.920 3.520   15.059  1.00 6.38  ? 121 VAL A N   1 
ATOM   977  C  CA  . VAL A 1 121 ? -12.002 4.473   15.730  1.00 6.71  ? 121 VAL A CA  1 
ATOM   978  C  C   . VAL A 1 121 ? -12.678 5.840   15.769  1.00 6.60  ? 121 VAL A C   1 
ATOM   979  O  O   . VAL A 1 121 ? -13.095 6.361   14.704  1.00 5.62  ? 121 VAL A O   1 
ATOM   980  C  CB  . VAL A 1 121 ? -10.625 4.566   14.937  1.00 7.79  ? 121 VAL A CB  1 
ATOM   981  C  CG1 . VAL A 1 121 ? -9.573  5.593   15.652  1.00 7.07  ? 121 VAL A CG1 1 
ATOM   982  C  CG2 . VAL A 1 121 ? -9.998  3.175   14.610  1.00 7.71  ? 121 VAL A CG2 1 
ATOM   983  N  N   . HIS A 1 122 ? -12.718 6.425   16.978  1.00 6.85  ? 122 HIS A N   1 
ATOM   984  C  CA  . HIS A 1 122 ? -13.439 7.715   17.168  1.00 7.38  ? 122 HIS A CA  1 
ATOM   985  C  C   . HIS A 1 122 ? -12.583 8.733   17.889  1.00 7.39  ? 122 HIS A C   1 
ATOM   986  O  O   . HIS A 1 122 ? -11.797 8.319   18.766  1.00 6.00  ? 122 HIS A O   1 
ATOM   987  C  CB  . HIS A 1 122 ? -14.756 7.561   17.960  1.00 8.20  ? 122 HIS A CB  1 
ATOM   988  C  CG  . HIS A 1 122 ? -15.634 6.443   17.517  1.00 8.99  ? 122 HIS A CG  1 
ATOM   989  N  ND1 . HIS A 1 122 ? -15.348 5.145   17.816  1.00 7.63  ? 122 HIS A ND1 1 
ATOM   990  C  CD2 . HIS A 1 122 ? -16.832 6.428   16.876  1.00 6.96  ? 122 HIS A CD2 1 
ATOM   991  C  CE1 . HIS A 1 122 ? -16.306 4.342   17.347  1.00 11.34 ? 122 HIS A CE1 1 
ATOM   992  N  NE2 . HIS A 1 122 ? -17.225 5.099   16.768  1.00 7.66  ? 122 HIS A NE2 1 
ATOM   993  N  N   . TRP A 1 123 ? -12.686 10.051  17.538  1.00 7.90  ? 123 TRP A N   1 
ATOM   994  C  CA  . TRP A 1 123 ? -11.866 11.074  18.266  1.00 6.98  ? 123 TRP A CA  1 
ATOM   995  C  C   . TRP A 1 123 ? -12.754 12.115  18.980  1.00 7.37  ? 123 TRP A C   1 
ATOM   996  O  O   . TRP A 1 123 ? -13.881 12.439  18.533  1.00 9.23  ? 123 TRP A O   1 
ATOM   997  C  CB  . TRP A 1 123 ? -10.887 11.747  17.285  1.00 9.71  ? 123 TRP A CB  1 
ATOM   998  C  CG  . TRP A 1 123 ? -11.560 12.385  16.097  1.00 9.48  ? 123 TRP A CG  1 
ATOM   999  C  CD1 . TRP A 1 123 ? -11.851 11.793  14.871  1.00 11.74 ? 123 TRP A CD1 1 
ATOM   1000 C  CD2 . TRP A 1 123 ? -12.024 13.750  16.007  1.00 12.38 ? 123 TRP A CD2 1 
ATOM   1001 N  NE1 . TRP A 1 123 ? -12.449 12.705  14.032  1.00 13.13 ? 123 TRP A NE1 1 
ATOM   1002 C  CE2 . TRP A 1 123 ? -12.576 13.918  14.691  1.00 13.07 ? 123 TRP A CE2 1 
ATOM   1003 C  CE3 . TRP A 1 123 ? -11.966 14.857  16.890  1.00 11.79 ? 123 TRP A CE3 1 
ATOM   1004 C  CZ2 . TRP A 1 123 ? -13.118 15.145  14.254  1.00 13.15 ? 123 TRP A CZ2 1 
ATOM   1005 C  CZ3 . TRP A 1 123 ? -12.552 16.082  16.468  1.00 13.21 ? 123 TRP A CZ3 1 
ATOM   1006 C  CH2 . TRP A 1 123 ? -13.112 16.209  15.147  1.00 13.25 ? 123 TRP A CH2 1 
ATOM   1007 N  N   . ASN A 1 124 ? -12.267 12.509  20.134  1.00 7.88  ? 124 ASN A N   1 
ATOM   1008 C  CA  . ASN A 1 124 ? -12.940 13.410  21.078  1.00 8.60  ? 124 ASN A CA  1 
ATOM   1009 C  C   . ASN A 1 124 ? -13.079 14.800  20.414  1.00 8.75  ? 124 ASN A C   1 
ATOM   1010 O  O   . ASN A 1 124 ? -12.069 15.472  20.156  1.00 8.80  ? 124 ASN A O   1 
ATOM   1011 C  CB  . ASN A 1 124 ? -12.125 13.514  22.369  1.00 7.80  ? 124 ASN A CB  1 
ATOM   1012 C  CG  . ASN A 1 124 ? -12.954 14.087  23.494  1.00 11.14 ? 124 ASN A CG  1 
ATOM   1013 O  OD1 . ASN A 1 124 ? -13.865 14.901  23.213  1.00 8.74  ? 124 ASN A OD1 1 
ATOM   1014 N  ND2 . ASN A 1 124 ? -12.760 13.592  24.708  1.00 10.62 ? 124 ASN A ND2 1 
ATOM   1015 N  N   . THR A 1 125 ? -14.344 15.200  20.190  1.00 10.10 ? 125 THR A N   1 
ATOM   1016 C  CA  . THR A 1 125 ? -14.584 16.467  19.458  1.00 11.96 ? 125 THR A CA  1 
ATOM   1017 C  C   . THR A 1 125 ? -14.053 17.728  20.251  1.00 12.73 ? 125 THR A C   1 
ATOM   1018 O  O   . THR A 1 125 ? -13.790 18.749  19.665  1.00 11.83 ? 125 THR A O   1 
ATOM   1019 C  CB  . THR A 1 125 ? -16.078 16.627  19.078  1.00 12.97 ? 125 THR A CB  1 
ATOM   1020 O  OG1 . THR A 1 125 ? -16.864 16.600  20.271  1.00 17.19 ? 125 THR A OG1 1 
ATOM   1021 C  CG2 . THR A 1 125 ? -16.527 15.426  18.144  1.00 12.39 ? 125 THR A CG2 1 
ATOM   1022 N  N   . LYS A 1 126 ? -13.806 17.593  21.548  1.00 11.06 ? 127 LYS A N   1 
ATOM   1023 C  CA  . LYS A 1 126 ? -13.265 18.781  22.301  1.00 11.39 ? 127 LYS A CA  1 
ATOM   1024 C  C   . LYS A 1 126 ? -11.824 19.121  21.857  1.00 10.34 ? 127 LYS A C   1 
ATOM   1025 O  O   . LYS A 1 126 ? -11.324 20.206  22.166  1.00 12.57 ? 127 LYS A O   1 
ATOM   1026 C  CB  . LYS A 1 126 ? -13.380 18.528  23.771  1.00 12.71 ? 127 LYS A CB  1 
ATOM   1027 C  CG  . LYS A 1 126 ? -12.362 17.731  24.343  1.00 12.99 ? 127 LYS A CG  1 
ATOM   1028 C  CD  . LYS A 1 126 ? -12.779 17.321  25.770  1.00 20.63 ? 127 LYS A CD  1 
ATOM   1029 C  CE  . LYS A 1 126 ? -11.585 16.900  26.521  1.00 26.36 ? 127 LYS A CE  1 
ATOM   1030 N  NZ  . LYS A 1 126 ? -11.959 16.033  27.759  1.00 29.43 ? 127 LYS A NZ  1 
ATOM   1031 N  N   . TYR A 1 127 ? -11.181 18.196  21.121  1.00 9.05  ? 128 TYR A N   1 
ATOM   1032 C  CA  . TYR A 1 127 ? -9.839  18.435  20.574  1.00 9.94  ? 128 TYR A CA  1 
ATOM   1033 C  C   . TYR A 1 127 ? -9.797  18.866  19.107  1.00 11.83 ? 128 TYR A C   1 
ATOM   1034 O  O   . TYR A 1 127 ? -8.686  19.137  18.546  1.00 11.16 ? 128 TYR A O   1 
ATOM   1035 C  CB  . TYR A 1 127 ? -8.903  17.256  20.865  1.00 9.80  ? 128 TYR A CB  1 
ATOM   1036 C  CG  . TYR A 1 127 ? -8.815  16.996  22.325  1.00 7.35  ? 128 TYR A CG  1 
ATOM   1037 C  CD1 . TYR A 1 127 ? -8.460  17.985  23.240  1.00 12.53 ? 128 TYR A CD1 1 
ATOM   1038 C  CD2 . TYR A 1 127 ? -9.079  15.689  22.821  1.00 7.74  ? 128 TYR A CD2 1 
ATOM   1039 C  CE1 . TYR A 1 127 ? -8.387  17.705  24.655  1.00 10.04 ? 128 TYR A CE1 1 
ATOM   1040 C  CE2 . TYR A 1 127 ? -8.981  15.396  24.139  1.00 8.10  ? 128 TYR A CE2 1 
ATOM   1041 C  CZ  . TYR A 1 127 ? -8.709  16.433  25.090  1.00 9.82  ? 128 TYR A CZ  1 
ATOM   1042 O  OH  . TYR A 1 127 ? -8.586  16.068  26.443  1.00 12.33 ? 128 TYR A OH  1 
ATOM   1043 N  N   . GLY A 1 128 ? -10.975 19.022  18.532  1.00 10.63 ? 129 GLY A N   1 
ATOM   1044 C  CA  . GLY A 1 128 ? -11.091 19.751  17.221  1.00 10.74 ? 129 GLY A CA  1 
ATOM   1045 C  C   . GLY A 1 128 ? -10.725 18.869  16.033  1.00 11.84 ? 129 GLY A C   1 
ATOM   1046 O  O   . GLY A 1 128 ? -11.357 18.987  14.974  1.00 12.44 ? 129 GLY A O   1 
ATOM   1047 N  N   . ASP A 1 129 ? -9.674  18.071  16.154  1.00 12.43 ? 130 ASP A N   1 
ATOM   1048 C  CA  . ASP A 1 129 ? -9.388  17.094  15.123  1.00 13.98 ? 130 ASP A CA  1 
ATOM   1049 C  C   . ASP A 1 129 ? -8.624  15.872  15.571  1.00 14.40 ? 130 ASP A C   1 
ATOM   1050 O  O   . ASP A 1 129 ? -8.160  15.799  16.695  1.00 13.34 ? 130 ASP A O   1 
ATOM   1051 C  CB  . ASP A 1 129 ? -8.750  17.726  13.889  1.00 12.96 ? 130 ASP A CB  1 
ATOM   1052 C  CG  . ASP A 1 129 ? -7.314  18.122  14.106  1.00 17.59 ? 130 ASP A CG  1 
ATOM   1053 O  OD1 . ASP A 1 129 ? -6.751  17.855  15.172  1.00 23.75 ? 130 ASP A OD1 1 
ATOM   1054 O  OD2 . ASP A 1 129 ? -6.720  18.692  13.189  1.00 23.65 ? 130 ASP A OD2 1 
ATOM   1055 N  N   . PHE A 1 130 ? -8.517  14.906  14.665  1.00 12.84 ? 131 PHE A N   1 
ATOM   1056 C  CA  . PHE A 1 130 ? -7.841  13.655  14.982  1.00 13.39 ? 131 PHE A CA  1 
ATOM   1057 C  C   . PHE A 1 130 ? -6.381  13.822  15.423  1.00 11.49 ? 131 PHE A C   1 
ATOM   1058 O  O   . PHE A 1 130 ? -5.927  13.213  16.421  1.00 10.33 ? 131 PHE A O   1 
ATOM   1059 C  CB  . PHE A 1 130 ? -7.895  12.669  13.807  1.00 12.67 ? 131 PHE A CB  1 
ATOM   1060 C  CG  . PHE A 1 130 ? -7.335  11.313  14.151  1.00 12.52 ? 131 PHE A CG  1 
ATOM   1061 C  CD1 . PHE A 1 130 ? -8.157  10.372  14.793  1.00 9.51  ? 131 PHE A CD1 1 
ATOM   1062 C  CD2 . PHE A 1 130 ? -5.973  10.975  13.953  1.00 12.13 ? 131 PHE A CD2 1 
ATOM   1063 C  CE1 . PHE A 1 130 ? -7.649  9.141   15.179  1.00 12.95 ? 131 PHE A CE1 1 
ATOM   1064 C  CE2 . PHE A 1 130 ? -5.491  9.735   14.304  1.00 14.11 ? 131 PHE A CE2 1 
ATOM   1065 C  CZ  . PHE A 1 130 ? -6.350  8.811   14.928  1.00 13.38 ? 131 PHE A CZ  1 
ATOM   1066 N  N   . GLY A 1 131 ? -5.627  14.615  14.639  1.00 10.57 ? 132 GLY A N   1 
ATOM   1067 C  CA  . GLY A 1 131 ? -4.254  14.787  14.952  1.00 10.86 ? 132 GLY A CA  1 
ATOM   1068 C  C   . GLY A 1 131 ? -4.008  15.380  16.344  1.00 12.26 ? 132 GLY A C   1 
ATOM   1069 O  O   . GLY A 1 131 ? -3.023  15.023  17.010  1.00 12.73 ? 132 GLY A O   1 
ATOM   1070 N  N   . LYS A 1 132 ? -4.890  16.277  16.784  1.00 10.27 ? 133 LYS A N   1 
ATOM   1071 C  CA  . LYS A 1 132 ? -4.733  16.854  18.115  1.00 10.74 ? 133 LYS A CA  1 
ATOM   1072 C  C   . LYS A 1 132 ? -5.212  15.878  19.217  1.00 10.87 ? 133 LYS A C   1 
ATOM   1073 O  O   . LYS A 1 132 ? -4.603  15.750  20.287  1.00 10.19 ? 133 LYS A O   1 
ATOM   1074 C  CB  . LYS A 1 132 ? -5.505  18.114  18.222  1.00 12.09 ? 133 LYS A CB  1 
ATOM   1075 C  CG  . LYS A 1 132 ? -4.859  19.286  17.424  1.00 13.61 ? 133 LYS A CG  1 
ATOM   1076 C  CD  . LYS A 1 132 ? -3.582  19.674  18.191  1.00 24.82 ? 133 LYS A CD  1 
ATOM   1077 C  CE  . LYS A 1 132 ? -3.086  21.085  17.864  1.00 27.02 ? 133 LYS A CE  1 
ATOM   1078 N  NZ  . LYS A 1 132 ? -2.217  21.451  19.036  1.00 32.71 ? 133 LYS A NZ  1 
ATOM   1079 N  N   . ALA A 1 133 ? -6.287  15.191  18.891  1.00 10.47 ? 134 ALA A N   1 
ATOM   1080 C  CA  . ALA A 1 133 ? -6.894  14.193  19.854  1.00 11.18 ? 134 ALA A CA  1 
ATOM   1081 C  C   . ALA A 1 133 ? -5.867  13.117  20.275  1.00 9.26  ? 134 ALA A C   1 
ATOM   1082 O  O   . ALA A 1 133 ? -5.803  12.699  21.470  1.00 10.79 ? 134 ALA A O   1 
ATOM   1083 C  CB  . ALA A 1 133 ? -8.092  13.542  19.234  1.00 10.95 ? 134 ALA A CB  1 
ATOM   1084 N  N   . VAL A 1 134 ? -5.077  12.611  19.318  1.00 9.26  ? 135 VAL A N   1 
ATOM   1085 C  CA  . VAL A 1 134 ? -4.115  11.479  19.659  1.00 10.61 ? 135 VAL A CA  1 
ATOM   1086 C  C   . VAL A 1 134 ? -2.973  11.899  20.631  1.00 9.38  ? 135 VAL A C   1 
ATOM   1087 O  O   . VAL A 1 134 ? -2.249  11.009  21.213  1.00 9.95  ? 135 VAL A O   1 
ATOM   1088 C  CB  . VAL A 1 134 ? -3.469  10.773  18.400  1.00 10.41 ? 135 VAL A CB  1 
ATOM   1089 C  CG1 . VAL A 1 134 ? -4.620  10.126  17.544  1.00 12.10 ? 135 VAL A CG1 1 
ATOM   1090 C  CG2 . VAL A 1 134 ? -2.551  11.720  17.613  1.00 11.71 ? 135 VAL A CG2 1 
ATOM   1091 N  N   . GLN A 1 135 ? -2.858  13.233  20.787  1.00 8.40  ? 136 GLN A N   1 
ATOM   1092 C  CA  . GLN A 1 135 ? -1.914  13.788  21.784  1.00 11.76 ? 136 GLN A CA  1 
ATOM   1093 C  C   . GLN A 1 135 ? -2.461  13.836  23.204  1.00 11.57 ? 136 GLN A C   1 
ATOM   1094 O  O   . GLN A 1 135 ? -1.790  14.267  24.142  1.00 12.44 ? 136 GLN A O   1 
ATOM   1095 C  CB  . GLN A 1 135 ? -1.505  15.200  21.315  1.00 11.84 ? 136 GLN A CB  1 
ATOM   1096 C  CG  . GLN A 1 135 ? -0.910  15.063  19.953  1.00 16.17 ? 136 GLN A CG  1 
ATOM   1097 C  CD  . GLN A 1 135 ? -0.322  16.320  19.387  1.00 23.37 ? 136 GLN A CD  1 
ATOM   1098 O  OE1 . GLN A 1 135 ? 0.592   16.915  20.001  1.00 27.03 ? 136 GLN A OE1 1 
ATOM   1099 N  NE2 . GLN A 1 135 ? -0.801  16.723  18.174  1.00 18.85 ? 136 GLN A NE2 1 
ATOM   1100 N  N   . GLN A 1 136 ? -3.721  13.463  23.369  1.00 11.31 ? 137 GLN A N   1 
ATOM   1101 C  CA  . GLN A 1 136 ? -4.371  13.615  24.694  1.00 10.69 ? 137 GLN A CA  1 
ATOM   1102 C  C   . GLN A 1 136 ? -4.736  12.216  25.254  1.00 9.92  ? 137 GLN A C   1 
ATOM   1103 O  O   . GLN A 1 136 ? -5.154  11.307  24.490  1.00 7.69  ? 137 GLN A O   1 
ATOM   1104 C  CB  . GLN A 1 136 ? -5.632  14.407  24.563  1.00 10.05 ? 137 GLN A CB  1 
ATOM   1105 C  CG  . GLN A 1 136 ? -5.485  15.679  23.628  1.00 14.77 ? 137 GLN A CG  1 
ATOM   1106 C  CD  . GLN A 1 136 ? -4.477  16.655  24.203  1.00 19.80 ? 137 GLN A CD  1 
ATOM   1107 O  OE1 . GLN A 1 136 ? -4.310  16.745  25.415  1.00 19.12 ? 137 GLN A OE1 1 
ATOM   1108 N  NE2 . GLN A 1 136 ? -3.732  17.305  23.325  1.00 25.14 ? 137 GLN A NE2 1 
ATOM   1109 N  N   . PRO A 1 137 ? -4.697  12.073  26.599  1.00 11.09 ? 138 PRO A N   1 
ATOM   1110 C  CA  . PRO A 1 137 ? -4.966  10.752  27.212  1.00 9.47  ? 138 PRO A CA  1 
ATOM   1111 C  C   . PRO A 1 137 ? -6.397  10.320  27.017  1.00 9.64  ? 138 PRO A C   1 
ATOM   1112 O  O   . PRO A 1 137 ? -6.687  9.118   27.112  1.00 8.67  ? 138 PRO A O   1 
ATOM   1113 C  CB  . PRO A 1 137 ? -4.726  10.963  28.752  1.00 10.95 ? 138 PRO A CB  1 
ATOM   1114 C  CG  . PRO A 1 137 ? -4.552  12.407  28.918  1.00 15.52 ? 138 PRO A CG  1 
ATOM   1115 C  CD  . PRO A 1 137 ? -4.377  13.124  27.595  1.00 13.64 ? 138 PRO A CD  1 
ATOM   1116 N  N   . ASP A 1 138 ? -7.317  11.251  26.806  1.00 6.94  ? 139 ASP A N   1 
ATOM   1117 C  CA  . ASP A 1 138 ? -8.694  10.875  26.559  1.00 7.60  ? 139 ASP A CA  1 
ATOM   1118 C  C   . ASP A 1 138 ? -9.076  11.293  25.077  1.00 7.34  ? 139 ASP A C   1 
ATOM   1119 O  O   . ASP A 1 138 ? -10.206 11.667  24.791  1.00 8.01  ? 139 ASP A O   1 
ATOM   1120 C  CB  . ASP A 1 138 ? -9.686  11.539  27.544  1.00 10.30 ? 139 ASP A CB  1 
ATOM   1121 C  CG  . ASP A 1 138 ? -9.583  13.057  27.589  1.00 8.12  ? 139 ASP A CG  1 
ATOM   1122 O  OD1 . ASP A 1 138 ? -8.691  13.607  26.942  1.00 10.02 ? 139 ASP A OD1 1 
ATOM   1123 O  OD2 . ASP A 1 138 ? -10.458 13.717  28.226  1.00 13.34 ? 139 ASP A OD2 1 
ATOM   1124 N  N   . GLY A 1 139 ? -8.099  11.250  24.155  1.00 7.59  ? 140 GLY A N   1 
ATOM   1125 C  CA  . GLY A 1 139 ? -8.319  11.701  22.809  1.00 7.05  ? 140 GLY A CA  1 
ATOM   1126 C  C   . GLY A 1 139 ? -9.167  10.816  21.922  1.00 6.63  ? 140 GLY A C   1 
ATOM   1127 O  O   . GLY A 1 139 ? -9.932  11.325  21.060  1.00 5.58  ? 140 GLY A O   1 
ATOM   1128 N  N   . LEU A 1 140 ? -9.069  9.499   22.115  1.00 5.79  ? 141 LEU A N   1 
ATOM   1129 C  CA  . LEU A 1 140 ? -9.724  8.554   21.203  1.00 4.79  ? 141 LEU A CA  1 
ATOM   1130 C  C   . LEU A 1 140 ? -10.632 7.595   22.013  1.00 4.64  ? 141 LEU A C   1 
ATOM   1131 O  O   . LEU A 1 140 ? -10.366 7.315   23.178  1.00 6.09  ? 141 LEU A O   1 
ATOM   1132 C  CB  . LEU A 1 140 ? -8.716  7.765   20.433  1.00 5.72  ? 141 LEU A CB  1 
ATOM   1133 C  CG  . LEU A 1 140 ? -7.812  8.431   19.398  1.00 12.01 ? 141 LEU A CG  1 
ATOM   1134 C  CD1 . LEU A 1 140 ? -7.235  7.287   18.496  1.00 8.76  ? 141 LEU A CD1 1 
ATOM   1135 C  CD2 . LEU A 1 140 ? -8.381  9.558   18.519  1.00 10.92 ? 141 LEU A CD2 1 
ATOM   1136 N  N   . ALA A 1 141 ? -11.685 7.104   21.355  1.00 6.11  ? 142 ALA A N   1 
ATOM   1137 C  CA  . ALA A 1 141 ? -12.437 5.927   21.894  1.00 5.98  ? 142 ALA A CA  1 
ATOM   1138 C  C   . ALA A 1 141 ? -12.432 4.939   20.733  1.00 6.29  ? 142 ALA A C   1 
ATOM   1139 O  O   . ALA A 1 141 ? -12.913 5.335   19.597  1.00 7.64  ? 142 ALA A O   1 
ATOM   1140 C  CB  . ALA A 1 141 ? -13.797 6.348   22.257  1.00 6.86  ? 142 ALA A CB  1 
ATOM   1141 N  N   . VAL A 1 142 ? -11.925 3.728   21.000  1.00 7.66  ? 143 VAL A N   1 
ATOM   1142 C  CA  . VAL A 1 142 ? -11.981 2.673   20.006  1.00 6.49  ? 143 VAL A CA  1 
ATOM   1143 C  C   . VAL A 1 142 ? -12.916 1.607   20.506  1.00 7.58  ? 143 VAL A C   1 
ATOM   1144 O  O   . VAL A 1 142 ? -12.744 1.099   21.593  1.00 6.54  ? 143 VAL A O   1 
ATOM   1145 C  CB  . VAL A 1 142 ? -10.599 2.144   19.609  1.00 6.47  ? 143 VAL A CB  1 
ATOM   1146 C  CG1 . VAL A 1 142 ? -10.649 1.068   18.471  1.00 9.06  ? 143 VAL A CG1 1 
ATOM   1147 C  CG2 . VAL A 1 142 ? -9.625  3.299   19.294  1.00 4.60  ? 143 VAL A CG2 1 
ATOM   1148 N  N   . LEU A 1 143 ? -13.874 1.296   19.646  1.00 5.60  ? 144 LEU A N   1 
ATOM   1149 C  CA  . LEU A 1 143 ? -14.893 0.261   19.910  1.00 5.44  ? 144 LEU A CA  1 
ATOM   1150 C  C   . LEU A 1 143 ? -14.335 -0.993  19.199  1.00 6.21  ? 144 LEU A C   1 
ATOM   1151 O  O   . LEU A 1 143 ? -14.279 -1.014  17.952  1.00 7.72  ? 144 LEU A O   1 
ATOM   1152 C  CB  . LEU A 1 143 ? -16.261 0.693   19.341  1.00 8.56  ? 144 LEU A CB  1 
ATOM   1153 C  CG  . LEU A 1 143 ? -17.451 -0.218  19.461  1.00 9.21  ? 144 LEU A CG  1 
ATOM   1154 C  CD1 . LEU A 1 143 ? -17.612 -0.554  20.997  1.00 11.27 ? 144 LEU A CD1 1 
ATOM   1155 C  CD2 . LEU A 1 143 ? -18.734 0.347   18.817  1.00 8.89  ? 144 LEU A CD2 1 
ATOM   1156 N  N   . GLY A 1 144 ? -14.065 -2.019  20.014  1.00 5.16  ? 145 GLY A N   1 
ATOM   1157 C  CA  . GLY A 1 144 ? -13.420 -3.283  19.605  1.00 2.68  ? 145 GLY A CA  1 
ATOM   1158 C  C   . GLY A 1 144 ? -14.540 -4.352  19.523  1.00 6.16  ? 145 GLY A C   1 
ATOM   1159 O  O   . GLY A 1 144 ? -15.334 -4.438  20.455  1.00 7.79  ? 145 GLY A O   1 
ATOM   1160 N  N   . ILE A 1 145 ? -14.588 -5.169  18.485  1.00 7.21  ? 146 ILE A N   1 
ATOM   1161 C  CA  . ILE A 1 145 ? -15.683 -6.168  18.301  1.00 5.22  ? 146 ILE A CA  1 
ATOM   1162 C  C   . ILE A 1 145 ? -15.043 -7.400  17.744  1.00 6.93  ? 146 ILE A C   1 
ATOM   1163 O  O   . ILE A 1 145 ? -14.332 -7.335  16.731  1.00 7.23  ? 146 ILE A O   1 
ATOM   1164 C  CB  . ILE A 1 145 ? -16.772 -5.668  17.230  1.00 5.59  ? 146 ILE A CB  1 
ATOM   1165 C  CG1 . ILE A 1 145 ? -17.398 -4.380  17.819  1.00 4.81  ? 146 ILE A CG1 1 
ATOM   1166 C  CG2 . ILE A 1 145 ? -17.817 -6.726  17.001  1.00 6.25  ? 146 ILE A CG2 1 
ATOM   1167 C  CD1 . ILE A 1 145 ? -18.472 -3.714  16.897  1.00 6.22  ? 146 ILE A CD1 1 
ATOM   1168 N  N   . PHE A 1 146 ? -15.215 -8.480  18.491  1.00 6.52  ? 147 PHE A N   1 
ATOM   1169 C  CA  . PHE A 1 146 ? -14.541 -9.747  18.070  1.00 4.83  ? 147 PHE A CA  1 
ATOM   1170 C  C   . PHE A 1 146 ? -15.301 -10.347 16.869  1.00 7.39  ? 147 PHE A C   1 
ATOM   1171 O  O   . PHE A 1 146 ? -16.545 -10.214 16.783  1.00 6.53  ? 147 PHE A O   1 
ATOM   1172 C  CB  . PHE A 1 146 ? -14.551 -10.707 19.216  1.00 6.51  ? 147 PHE A CB  1 
ATOM   1173 C  CG  . PHE A 1 146 ? -13.665 -10.249 20.367  1.00 5.55  ? 147 PHE A CG  1 
ATOM   1174 C  CD1 . PHE A 1 146 ? -12.244 -10.063 20.210  1.00 5.98  ? 147 PHE A CD1 1 
ATOM   1175 C  CD2 . PHE A 1 146 ? -14.250 -10.009 21.583  1.00 6.92  ? 147 PHE A CD2 1 
ATOM   1176 C  CE1 . PHE A 1 146 ? -11.422 -9.687  21.323  1.00 6.59  ? 147 PHE A CE1 1 
ATOM   1177 C  CE2 . PHE A 1 146 ? -13.478 -9.552  22.715  1.00 7.27  ? 147 PHE A CE2 1 
ATOM   1178 C  CZ  . PHE A 1 146 ? -12.019 -9.411  22.562  1.00 6.36  ? 147 PHE A CZ  1 
ATOM   1179 N  N   . LEU A 1 147 ? -14.573 -10.991 15.966  1.00 6.33  ? 148 LEU A N   1 
ATOM   1180 C  CA  . LEU A 1 147 ? -15.175 -11.819 14.897  1.00 6.76  ? 148 LEU A CA  1 
ATOM   1181 C  C   . LEU A 1 147 ? -14.825 -13.312 15.138  1.00 8.27  ? 148 LEU A C   1 
ATOM   1182 O  O   . LEU A 1 147 ? -13.624 -13.635 15.382  1.00 6.63  ? 148 LEU A O   1 
ATOM   1183 C  CB  . LEU A 1 147 ? -14.602 -11.426 13.530  1.00 8.16  ? 148 LEU A CB  1 
ATOM   1184 C  CG  . LEU A 1 147 ? -15.182 -10.193 12.816  1.00 8.92  ? 148 LEU A CG  1 
ATOM   1185 C  CD1 . LEU A 1 147 ? -15.028 -8.922  13.733  1.00 9.39  ? 148 LEU A CD1 1 
ATOM   1186 C  CD2 . LEU A 1 147 ? -14.475 -10.034 11.490  1.00 9.12  ? 148 LEU A CD2 1 
ATOM   1187 N  N   . LYS A 1 148 ? -15.858 -14.183 15.151  1.00 9.48  ? 149 LYS A N   1 
ATOM   1188 C  CA  . LYS A 1 148 ? -15.701 -15.659 15.079  1.00 9.71  ? 149 LYS A CA  1 
ATOM   1189 C  C   . LYS A 1 148 ? -16.210 -16.141 13.713  1.00 11.67 ? 149 LYS A C   1 
ATOM   1190 O  O   . LYS A 1 148 ? -17.049 -15.526 13.078  1.00 10.68 ? 149 LYS A O   1 
ATOM   1191 C  CB  . LYS A 1 148 ? -16.400 -16.462 16.187  1.00 11.48 ? 149 LYS A CB  1 
ATOM   1192 C  CG  . LYS A 1 148 ? -17.918 -16.421 16.082  1.00 15.66 ? 149 LYS A CG  1 
ATOM   1193 C  CD  . LYS A 1 148 ? -18.554 -17.052 17.291  1.00 21.46 ? 149 LYS A CD  1 
ATOM   1194 C  CE  . LYS A 1 148 ? -20.059 -17.125 17.084  1.00 27.15 ? 149 LYS A CE  1 
ATOM   1195 N  NZ  . LYS A 1 148 ? -20.804 -17.881 18.182  1.00 33.31 ? 149 LYS A NZ  1 
ATOM   1196 N  N   . VAL A 1 149 ? -15.662 -17.275 13.296  1.00 10.70 ? 150 VAL A N   1 
ATOM   1197 C  CA  . VAL A 1 149 ? -16.043 -17.862 11.999  1.00 11.28 ? 150 VAL A CA  1 
ATOM   1198 C  C   . VAL A 1 149 ? -17.289 -18.760 12.236  1.00 11.56 ? 150 VAL A C   1 
ATOM   1199 O  O   . VAL A 1 149 ? -17.284 -19.733 13.011  1.00 12.61 ? 150 VAL A O   1 
ATOM   1200 C  CB  . VAL A 1 149 ? -14.802 -18.642 11.378  1.00 11.61 ? 150 VAL A CB  1 
ATOM   1201 C  CG1 . VAL A 1 149 ? -15.215 -19.481 10.098  1.00 12.87 ? 150 VAL A CG1 1 
ATOM   1202 C  CG2 . VAL A 1 149 ? -13.733 -17.633 11.030  1.00 9.97  ? 150 VAL A CG2 1 
ATOM   1203 N  N   . GLY A 1 150 ? -18.290 -18.501 11.442  1.00 11.20 ? 151 GLY A N   1 
ATOM   1204 C  CA  . GLY A 1 150 ? -19.546 -19.271 11.522  1.00 13.04 ? 151 GLY A CA  1 
ATOM   1205 C  C   . GLY A 1 150 ? -20.475 -18.864 10.405  1.00 11.58 ? 151 GLY A C   1 
ATOM   1206 O  O   . GLY A 1 150 ? -20.121 -19.012 9.241   1.00 12.06 ? 151 GLY A O   1 
ATOM   1207 N  N   A SER A 1 151 ? -21.637 -18.320 10.760  0.50 11.64 ? 152 SER A N   1 
ATOM   1208 N  N   B SER A 1 151 ? -21.641 -18.319 10.757  0.50 11.60 ? 152 SER A N   1 
ATOM   1209 C  CA  A SER A 1 151 ? -22.584 -17.804 9.753   0.50 12.32 ? 152 SER A CA  1 
ATOM   1210 C  CA  B SER A 1 151 ? -22.548 -17.786 9.722   0.50 12.16 ? 152 SER A CA  1 
ATOM   1211 C  C   A SER A 1 151 ? -22.027 -16.518 9.143   0.50 11.47 ? 152 SER A C   1 
ATOM   1212 C  C   B SER A 1 151 ? -21.914 -16.550 9.100   0.50 11.51 ? 152 SER A C   1 
ATOM   1213 O  O   A SER A 1 151 ? -21.342 -15.759 9.861   0.50 10.71 ? 152 SER A O   1 
ATOM   1214 O  O   B SER A 1 151 ? -21.078 -15.876 9.742   0.50 10.01 ? 152 SER A O   1 
ATOM   1215 C  CB  A SER A 1 151 ? -23.939 -17.543 10.402  0.50 14.10 ? 152 SER A CB  1 
ATOM   1216 C  CB  B SER A 1 151 ? -23.944 -17.463 10.269  0.50 14.01 ? 152 SER A CB  1 
ATOM   1217 O  OG  A SER A 1 151 ? -23.798 -16.612 11.465  0.50 14.44 ? 152 SER A OG  1 
ATOM   1218 O  OG  B SER A 1 151 ? -24.442 -18.509 11.084  0.50 13.90 ? 152 SER A OG  1 
ATOM   1219 N  N   . ALA A 1 152 ? -22.219 -16.291 7.833   1.00 10.96 ? 153 ALA A N   1 
ATOM   1220 C  CA  . ALA A 1 152 ? -21.798 -15.027 7.231   1.00 8.32  ? 153 ALA A CA  1 
ATOM   1221 C  C   . ALA A 1 152 ? -22.484 -13.782 7.958   1.00 10.11 ? 153 ALA A C   1 
ATOM   1222 O  O   . ALA A 1 152 ? -23.559 -13.878 8.515   1.00 11.86 ? 153 ALA A O   1 
ATOM   1223 C  CB  . ALA A 1 152 ? -22.074 -14.940 5.634   1.00 9.93  ? 153 ALA A CB  1 
ATOM   1224 N  N   . LYS A 1 153 ? -21.794 -12.660 7.894   1.00 11.16 ? 154 LYS A N   1 
ATOM   1225 C  CA  . LYS A 1 153 ? -22.343 -11.356 8.284   1.00 12.77 ? 154 LYS A CA  1 
ATOM   1226 C  C   . LYS A 1 153 ? -22.738 -10.619 6.985   1.00 11.69 ? 154 LYS A C   1 
ATOM   1227 O  O   . LYS A 1 153 ? -21.844 -10.071 6.236   1.00 10.85 ? 154 LYS A O   1 
ATOM   1228 C  CB  . LYS A 1 153 ? -21.264 -10.565 9.112   1.00 12.88 ? 154 LYS A CB  1 
ATOM   1229 C  CG  . LYS A 1 153 ? -21.795 -9.337  9.866   1.00 17.07 ? 154 LYS A CG  1 
ATOM   1230 C  CD  . LYS A 1 153 ? -22.585 -9.859  11.134  1.00 18.58 ? 154 LYS A CD  1 
ATOM   1231 C  CE  . LYS A 1 153 ? -22.981 -8.711  12.059  1.00 22.82 ? 154 LYS A CE  1 
ATOM   1232 N  NZ  . LYS A 1 153 ? -23.872 -9.237  13.112  1.00 20.15 ? 154 LYS A NZ  1 
ATOM   1233 N  N   . PRO A 1 154 ? -24.053 -10.581 6.680   1.00 14.51 ? 155 PRO A N   1 
ATOM   1234 C  CA  . PRO A 1 154 ? -24.430 -9.933  5.395   1.00 14.10 ? 155 PRO A CA  1 
ATOM   1235 C  C   . PRO A 1 154 ? -23.912 -8.498  5.305   1.00 12.23 ? 155 PRO A C   1 
ATOM   1236 O  O   . PRO A 1 154 ? -23.417 -8.111  4.214   1.00 13.58 ? 155 PRO A O   1 
ATOM   1237 C  CB  . PRO A 1 154 ? -25.996 -10.017 5.357   1.00 15.46 ? 155 PRO A CB  1 
ATOM   1238 C  CG  . PRO A 1 154 ? -26.296 -11.118 6.276   1.00 17.65 ? 155 PRO A CG  1 
ATOM   1239 C  CD  . PRO A 1 154 ? -25.259 -11.100 7.369   1.00 13.49 ? 155 PRO A CD  1 
ATOM   1240 N  N   . GLY A 1 155 ? -23.841 -7.791  6.435   1.00 12.13 ? 156 GLY A N   1 
ATOM   1241 C  CA  . GLY A 1 155 ? -23.419 -6.355  6.449   1.00 13.47 ? 156 GLY A CA  1 
ATOM   1242 C  C   . GLY A 1 155 ? -21.948 -6.144  6.136   1.00 13.66 ? 156 GLY A C   1 
ATOM   1243 O  O   . GLY A 1 155 ? -21.549 -5.031  5.759   1.00 14.81 ? 156 GLY A O   1 
ATOM   1244 N  N   . LEU A 1 156 ? -21.178 -7.228  6.218   1.00 11.38 ? 157 LEU A N   1 
ATOM   1245 C  CA  . LEU A 1 156 ? -19.733 -7.225  5.842   1.00 10.51 ? 157 LEU A CA  1 
ATOM   1246 C  C   . LEU A 1 156 ? -19.435 -7.432  4.368   1.00 10.58 ? 157 LEU A C   1 
ATOM   1247 O  O   . LEU A 1 156 ? -18.353 -7.110  3.885   1.00 10.11 ? 157 LEU A O   1 
ATOM   1248 C  CB  . LEU A 1 156 ? -18.967 -8.263  6.691   1.00 10.49 ? 157 LEU A CB  1 
ATOM   1249 C  CG  . LEU A 1 156 ? -17.434 -8.376  6.560   1.00 10.26 ? 157 LEU A CG  1 
ATOM   1250 C  CD1 . LEU A 1 156 ? -16.819 -6.940  6.941   1.00 10.00 ? 157 LEU A CD1 1 
ATOM   1251 C  CD2 . LEU A 1 156 ? -16.895 -9.560  7.390   1.00 10.92 ? 157 LEU A CD2 1 
ATOM   1252 N  N   . GLN A 1 157 ? -20.402 -8.009  3.623   1.00 10.67 ? 158 GLN A N   1 
ATOM   1253 C  CA  . GLN A 1 157 ? -20.095 -8.507  2.291   1.00 12.58 ? 158 GLN A CA  1 
ATOM   1254 C  C   . GLN A 1 157 ? -19.609 -7.366  1.354   1.00 10.74 ? 158 GLN A C   1 
ATOM   1255 O  O   . GLN A 1 157 ? -18.711 -7.566  0.528   1.00 12.47 ? 158 GLN A O   1 
ATOM   1256 C  CB  . GLN A 1 157 ? -21.291 -9.316  1.682   1.00 13.45 ? 158 GLN A CB  1 
ATOM   1257 C  CG  . GLN A 1 157 ? -20.781 -10.116 0.384   1.00 12.52 ? 158 GLN A CG  1 
ATOM   1258 C  CD  . GLN A 1 157 ? -19.667 -11.117 0.715   1.00 13.07 ? 158 GLN A CD  1 
ATOM   1259 O  OE1 . GLN A 1 157 ? -19.634 -11.685 1.838   1.00 14.06 ? 158 GLN A OE1 1 
ATOM   1260 N  NE2 . GLN A 1 157 ? -18.729 -11.317 -0.232  1.00 11.96 ? 158 GLN A NE2 1 
ATOM   1261 N  N   . LYS A 1 158 ? -20.163 -6.161  1.508   1.00 13.43 ? 159 LYS A N   1 
ATOM   1262 C  CA  . LYS A 1 158 ? -19.770 -5.056  0.570   1.00 13.54 ? 159 LYS A CA  1 
ATOM   1263 C  C   . LYS A 1 158 ? -18.307 -4.744  0.802   1.00 12.56 ? 159 LYS A C   1 
ATOM   1264 O  O   . LYS A 1 158 ? -17.592 -4.378  -0.089  1.00 14.08 ? 159 LYS A O   1 
ATOM   1265 C  CB  . LYS A 1 158 ? -20.607 -3.754  0.761   1.00 14.94 ? 159 LYS A CB  1 
ATOM   1266 C  CG  . LYS A 1 158 ? -21.938 -3.847  0.028   1.00 20.77 ? 159 LYS A CG  1 
ATOM   1267 C  CD  . LYS A 1 158 ? -22.860 -2.673  0.356   1.00 22.22 ? 159 LYS A CD  1 
ATOM   1268 C  CE  . LYS A 1 158 ? -24.105 -2.693  -0.608  1.00 27.83 ? 159 LYS A CE  1 
ATOM   1269 N  NZ  . LYS A 1 158 ? -25.322 -1.864  -0.078  1.00 26.28 ? 159 LYS A NZ  1 
ATOM   1270 N  N   . VAL A 1 159 ? -17.861 -4.865  2.067   1.00 11.97 ? 160 VAL A N   1 
ATOM   1271 C  CA  . VAL A 1 159 ? -16.427 -4.636  2.328   1.00 10.81 ? 160 VAL A CA  1 
ATOM   1272 C  C   . VAL A 1 159 ? -15.641 -5.769  1.659   1.00 10.00 ? 160 VAL A C   1 
ATOM   1273 O  O   . VAL A 1 159 ? -14.657 -5.524  0.981   1.00 9.77  ? 160 VAL A O   1 
ATOM   1274 C  CB  . VAL A 1 159 ? -16.121 -4.639  3.815   1.00 10.35 ? 160 VAL A CB  1 
ATOM   1275 C  CG1 . VAL A 1 159 ? -14.546 -4.592  4.079   1.00 9.94  ? 160 VAL A CG1 1 
ATOM   1276 C  CG2 . VAL A 1 159 ? -16.902 -3.500  4.542   1.00 12.89 ? 160 VAL A CG2 1 
ATOM   1277 N  N   . VAL A 1 160 ? -16.039 -7.014  1.880   1.00 9.66  ? 161 VAL A N   1 
ATOM   1278 C  CA  . VAL A 1 160 ? -15.286 -8.128  1.328   1.00 12.47 ? 161 VAL A CA  1 
ATOM   1279 C  C   . VAL A 1 160 ? -15.180 -8.027  -0.171  1.00 11.87 ? 161 VAL A C   1 
ATOM   1280 O  O   . VAL A 1 160 ? -14.130 -8.262  -0.737  1.00 12.13 ? 161 VAL A O   1 
ATOM   1281 C  CB  . VAL A 1 160 ? -15.954 -9.528  1.746   1.00 13.32 ? 161 VAL A CB  1 
ATOM   1282 C  CG1 . VAL A 1 160 ? -15.369 -10.702 0.933   1.00 19.03 ? 161 VAL A CG1 1 
ATOM   1283 C  CG2 . VAL A 1 160 ? -15.700 -9.732  3.252   1.00 15.46 ? 161 VAL A CG2 1 
ATOM   1284 N  N   . ASP A 1 161 ? -16.242 -7.613  -0.796  1.00 13.37 ? 162 ASP A N   1 
ATOM   1285 C  CA  . ASP A 1 161 ? -16.281 -7.651  -2.247  1.00 15.98 ? 162 ASP A CA  1 
ATOM   1286 C  C   . ASP A 1 161 ? -15.329 -6.608  -2.884  1.00 17.15 ? 162 ASP A C   1 
ATOM   1287 O  O   . ASP A 1 161 ? -14.766 -6.860  -3.959  1.00 20.58 ? 162 ASP A O   1 
ATOM   1288 C  CB  . ASP A 1 161 ? -17.691 -7.576  -2.737  1.00 15.83 ? 162 ASP A CB  1 
ATOM   1289 C  CG  . ASP A 1 161 ? -18.388 -8.919  -2.650  1.00 19.59 ? 162 ASP A CG  1 
ATOM   1290 O  OD1 . ASP A 1 161 ? -17.711 -10.022 -2.712  1.00 21.97 ? 162 ASP A OD1 1 
ATOM   1291 O  OD2 . ASP A 1 161 ? -19.608 -8.844  -2.536  1.00 26.38 ? 162 ASP A OD2 1 
ATOM   1292 N  N   . VAL A 1 162 ? -15.112 -5.462  -2.229  1.00 13.33 ? 163 VAL A N   1 
ATOM   1293 C  CA  . VAL A 1 162 ? -14.211 -4.424  -2.773  1.00 13.49 ? 163 VAL A CA  1 
ATOM   1294 C  C   . VAL A 1 162 ? -12.720 -4.739  -2.589  1.00 12.33 ? 163 VAL A C   1 
ATOM   1295 O  O   . VAL A 1 162 ? -11.863 -4.049  -3.127  1.00 11.72 ? 163 VAL A O   1 
ATOM   1296 C  CB  . VAL A 1 162 ? -14.569 -3.063  -2.121  1.00 13.78 ? 163 VAL A CB  1 
ATOM   1297 C  CG1 . VAL A 1 162 ? -14.022 -2.915  -0.691  1.00 12.91 ? 163 VAL A CG1 1 
ATOM   1298 C  CG2 . VAL A 1 162 ? -14.164 -1.843  -3.048  1.00 14.28 ? 163 VAL A CG2 1 
ATOM   1299 N  N   . LEU A 1 163 ? -12.360 -5.700  -1.703  1.00 13.85 ? 164 LEU A N   1 
ATOM   1300 C  CA  . LEU A 1 163 ? -10.908 -5.948  -1.369  1.00 13.35 ? 164 LEU A CA  1 
ATOM   1301 C  C   . LEU A 1 163 ? -10.027 -6.317  -2.561  1.00 13.93 ? 164 LEU A C   1 
ATOM   1302 O  O   . LEU A 1 163 ? -8.862  -5.941  -2.635  1.00 13.30 ? 164 LEU A O   1 
ATOM   1303 C  CB  . LEU A 1 163 ? -10.763 -7.027  -0.284  1.00 13.78 ? 164 LEU A CB  1 
ATOM   1304 C  CG  . LEU A 1 163 ? -11.468 -6.754  1.081   1.00 12.39 ? 164 LEU A CG  1 
ATOM   1305 C  CD1 . LEU A 1 163 ? -11.149 -7.979  2.006   1.00 12.90 ? 164 LEU A CD1 1 
ATOM   1306 C  CD2 . LEU A 1 163 ? -11.011 -5.411  1.650   1.00 10.06 ? 164 LEU A CD2 1 
ATOM   1307 N  N   . ASP A 1 164 ? -10.611 -6.994  -3.537  1.00 15.88 ? 165 ASP A N   1 
ATOM   1308 C  CA  . ASP A 1 164 ? -9.787  -7.365  -4.687  1.00 18.65 ? 165 ASP A CA  1 
ATOM   1309 C  C   . ASP A 1 164 ? -9.366  -6.070  -5.490  1.00 16.84 ? 165 ASP A C   1 
ATOM   1310 O  O   . ASP A 1 164 ? -8.360  -6.103  -6.204  1.00 19.91 ? 165 ASP A O   1 
ATOM   1311 C  CB  . ASP A 1 164 ? -10.541 -8.393  -5.554  1.00 20.83 ? 165 ASP A CB  1 
ATOM   1312 C  CG  . ASP A 1 164 ? -11.395 -7.731  -6.527  1.00 27.00 ? 165 ASP A CG  1 
ATOM   1313 O  OD1 . ASP A 1 164 ? -12.396 -7.077  -6.098  1.00 29.92 ? 165 ASP A OD1 1 
ATOM   1314 O  OD2 . ASP A 1 164 ? -10.999 -7.762  -7.731  1.00 34.26 ? 165 ASP A OD2 1 
ATOM   1315 N  N   . SER A 1 165 ? -10.116 -4.983  -5.339  1.00 13.59 ? 166 SER A N   1 
ATOM   1316 C  CA  . SER A 1 165 ? -9.741  -3.691  -5.944  1.00 13.74 ? 166 SER A CA  1 
ATOM   1317 C  C   . SER A 1 165 ? -8.623  -2.941  -5.194  1.00 14.38 ? 166 SER A C   1 
ATOM   1318 O  O   . SER A 1 165 ? -8.065  -1.917  -5.722  1.00 13.90 ? 166 SER A O   1 
ATOM   1319 C  CB  . SER A 1 165 ? -10.978 -2.835  -6.185  1.00 15.28 ? 166 SER A CB  1 
ATOM   1320 O  OG  . SER A 1 165 ? -11.365 -2.153  -5.014  1.00 16.91 ? 166 SER A OG  1 
ATOM   1321 N  N   . ILE A 1 166 ? -8.294  -3.399  -3.952  1.00 11.17 ? 167 ILE A N   1 
ATOM   1322 C  CA  . ILE A 1 166 ? -7.238  -2.727  -3.145  1.00 11.37 ? 167 ILE A CA  1 
ATOM   1323 C  C   . ILE A 1 166 ? -6.213  -3.755  -2.612  1.00 10.35 ? 167 ILE A C   1 
ATOM   1324 O  O   . ILE A 1 166 ? -5.812  -3.780  -1.382  1.00 11.28 ? 167 ILE A O   1 
ATOM   1325 C  CB  . ILE A 1 166 ? -7.851  -1.854  -1.996  1.00 11.04 ? 167 ILE A CB  1 
ATOM   1326 C  CG1 . ILE A 1 166 ? -8.718  -2.762  -1.130  1.00 11.14 ? 167 ILE A CG1 1 
ATOM   1327 C  CG2 . ILE A 1 166 ? -8.665  -0.667  -2.583  1.00 11.36 ? 167 ILE A CG2 1 
ATOM   1328 C  CD1 . ILE A 1 166 ? -8.904  -2.332  0.275   1.00 11.60 ? 167 ILE A CD1 1 
ATOM   1329 N  N   . LYS A 1 167 ? -5.822  -4.696  -3.507  1.00 11.19 ? 168 LYS A N   1 
ATOM   1330 C  CA  . LYS A 1 167 ? -5.043  -5.817  -3.067  1.00 13.88 ? 168 LYS A CA  1 
ATOM   1331 C  C   . LYS A 1 167 ? -3.716  -5.419  -2.349  1.00 11.92 ? 168 LYS A C   1 
ATOM   1332 O  O   . LYS A 1 167 ? -3.318  -6.067  -1.387  1.00 10.39 ? 168 LYS A O   1 
ATOM   1333 C  CB  . LYS A 1 167 ? -4.713  -6.744  -4.254  1.00 13.25 ? 168 LYS A CB  1 
ATOM   1334 C  CG  . LYS A 1 167 ? -3.943  -7.950  -3.863  1.00 17.34 ? 168 LYS A CG  1 
ATOM   1335 C  CD  . LYS A 1 167 ? -3.696  -8.897  -5.046  1.00 20.04 ? 168 LYS A CD  1 
ATOM   1336 C  CE  . LYS A 1 167 ? -3.451  -10.304 -4.451  1.00 30.86 ? 168 LYS A CE  1 
ATOM   1337 N  NZ  . LYS A 1 167 ? -3.144  -11.335 -5.553  1.00 33.83 ? 168 LYS A NZ  1 
ATOM   1338 N  N   . THR A 1 168 ? -3.048  -4.384  -2.870  1.00 9.60  ? 169 THR A N   1 
ATOM   1339 C  CA  . THR A 1 168 ? -1.691  -4.038  -2.460  1.00 10.27 ? 169 THR A CA  1 
ATOM   1340 C  C   . THR A 1 168 ? -1.599  -2.653  -1.767  1.00 11.38 ? 169 THR A C   1 
ATOM   1341 O  O   . THR A 1 168 ? -2.490  -1.824  -1.921  1.00 10.06 ? 169 THR A O   1 
ATOM   1342 C  CB  . THR A 1 168 ? -0.723  -4.066  -3.703  1.00 11.84 ? 169 THR A CB  1 
ATOM   1343 O  OG1 . THR A 1 168 ? -1.319  -3.326  -4.787  1.00 12.65 ? 169 THR A OG1 1 
ATOM   1344 C  CG2 . THR A 1 168 ? -0.480  -5.555  -4.092  1.00 13.01 ? 169 THR A CG2 1 
ATOM   1345 N  N   . LYS A 1 169 ? -0.548  -2.482  -0.978  1.00 10.15 ? 170 LYS A N   1 
ATOM   1346 C  CA  . LYS A 1 169 ? -0.246  -1.288  -0.238  1.00 12.21 ? 170 LYS A CA  1 
ATOM   1347 C  C   . LYS A 1 169 ? -0.385  -0.016  -1.088  1.00 12.18 ? 170 LYS A C   1 
ATOM   1348 O  O   . LYS A 1 169 ? 0.178   0.021   -2.218  1.00 13.95 ? 170 LYS A O   1 
ATOM   1349 C  CB  . LYS A 1 169 ? 1.159   -1.374  0.341   1.00 11.47 ? 170 LYS A CB  1 
ATOM   1350 C  CG  . LYS A 1 169 ? 1.609   -0.136  1.118   1.00 13.56 ? 170 LYS A CG  1 
ATOM   1351 C  CD  . LYS A 1 169 ? 2.996   -0.449  1.669   1.00 21.40 ? 170 LYS A CD  1 
ATOM   1352 C  CE  . LYS A 1 169 ? 3.413   0.618   2.715   1.00 27.85 ? 170 LYS A CE  1 
ATOM   1353 N  NZ  . LYS A 1 169 ? 4.936   0.604   2.805   1.00 35.40 ? 170 LYS A NZ  1 
ATOM   1354 N  N   . GLY A 1 170 ? -1.102  0.967   -0.565  1.00 13.04 ? 171 GLY A N   1 
ATOM   1355 C  CA  . GLY A 1 170 ? -1.319  2.262   -1.266  1.00 11.84 ? 171 GLY A CA  1 
ATOM   1356 C  C   . GLY A 1 170 ? -2.483  2.312   -2.262  1.00 13.58 ? 171 GLY A C   1 
ATOM   1357 O  O   . GLY A 1 170 ? -2.771  3.411   -2.812  1.00 13.75 ? 171 GLY A O   1 
ATOM   1358 N  N   . LYS A 1 171 ? -3.157  1.190   -2.528  1.00 10.80 ? 172 LYS A N   1 
ATOM   1359 C  CA  . LYS A 1 171 ? -4.374  1.205   -3.315  1.00 12.08 ? 172 LYS A CA  1 
ATOM   1360 C  C   . LYS A 1 171 ? -5.564  1.672   -2.486  1.00 12.13 ? 172 LYS A C   1 
ATOM   1361 O  O   . LYS A 1 171 ? -5.746  1.244   -1.359  1.00 11.67 ? 172 LYS A O   1 
ATOM   1362 C  CB  . LYS A 1 171 ? -4.675  -0.159  -3.974  1.00 12.24 ? 172 LYS A CB  1 
ATOM   1363 C  CG  . LYS A 1 171 ? -3.626  -0.439  -5.046  1.00 12.87 ? 172 LYS A CG  1 
ATOM   1364 C  CD  . LYS A 1 171 ? -3.992  -1.672  -5.963  1.00 18.11 ? 172 LYS A CD  1 
ATOM   1365 C  CE  . LYS A 1 171 ? -5.210  -1.338  -6.908  1.00 24.07 ? 172 LYS A CE  1 
ATOM   1366 N  NZ  . LYS A 1 171 ? -5.621  -2.355  -7.932  1.00 22.90 ? 172 LYS A NZ  1 
ATOM   1367 N  N   . SER A 1 172 ? -6.404  2.481   -3.108  1.00 12.54 ? 173 SER A N   1 
ATOM   1368 C  CA  . SER A 1 172 ? -7.637  2.931   -2.486  1.00 11.08 ? 173 SER A CA  1 
ATOM   1369 C  C   . SER A 1 172 ? -8.793  2.808   -3.491  1.00 13.78 ? 173 SER A C   1 
ATOM   1370 O  O   . SER A 1 172 ? -8.578  2.746   -4.747  1.00 14.48 ? 173 SER A O   1 
ATOM   1371 C  CB  . SER A 1 172 ? -7.472  4.364   -2.000  1.00 11.75 ? 173 SER A CB  1 
ATOM   1372 O  OG  . SER A 1 172 ? -7.422  5.248   -3.099  1.00 13.03 ? 173 SER A OG  1 
ATOM   1373 N  N   . ALA A 1 173 ? -10.026 2.752   -2.973  1.00 13.78 ? 174 ALA A N   1 
ATOM   1374 C  CA  . ALA A 1 173 ? -11.207 2.667   -3.809  1.00 13.65 ? 174 ALA A CA  1 
ATOM   1375 C  C   . ALA A 1 173 ? -12.366 3.412   -3.195  1.00 15.16 ? 174 ALA A C   1 
ATOM   1376 O  O   . ALA A 1 173 ? -12.498 3.499   -1.982  1.00 12.45 ? 174 ALA A O   1 
ATOM   1377 C  CB  . ALA A 1 173 ? -11.594 1.224   -4.201  1.00 13.58 ? 174 ALA A CB  1 
ATOM   1378 N  N   . ASP A 1 174 ? -13.152 4.064   -4.072  1.00 14.44 ? 175 ASP A N   1 
ATOM   1379 C  CA  . ASP A 1 174 ? -14.357 4.729   -3.617  1.00 14.40 ? 175 ASP A CA  1 
ATOM   1380 C  C   . ASP A 1 174 ? -15.221 3.785   -2.809  1.00 14.14 ? 175 ASP A C   1 
ATOM   1381 O  O   . ASP A 1 174 ? -15.335 2.606   -3.150  1.00 15.04 ? 175 ASP A O   1 
ATOM   1382 C  CB  . ASP A 1 174 ? -15.164 5.337   -4.801  1.00 15.51 ? 175 ASP A CB  1 
ATOM   1383 C  CG  . ASP A 1 174 ? -14.306 6.385   -5.543  1.00 20.59 ? 175 ASP A CG  1 
ATOM   1384 O  OD1 . ASP A 1 174 ? -13.534 7.136   -4.875  1.00 23.53 ? 175 ASP A OD1 1 
ATOM   1385 O  OD2 . ASP A 1 174 ? -14.384 6.453   -6.790  1.00 28.13 ? 175 ASP A OD2 1 
ATOM   1386 N  N   . PHE A 1 175 ? -15.772 4.298   -1.694  1.00 13.22 ? 176 PHE A N   1 
ATOM   1387 C  CA  . PHE A 1 175 ? -16.487 3.347   -0.771  1.00 13.51 ? 176 PHE A CA  1 
ATOM   1388 C  C   . PHE A 1 175 ? -17.514 4.133   -0.025  1.00 13.58 ? 176 PHE A C   1 
ATOM   1389 O  O   . PHE A 1 175 ? -17.356 4.471   1.153   1.00 14.60 ? 176 PHE A O   1 
ATOM   1390 C  CB  . PHE A 1 175 ? -15.544 2.552   0.130   1.00 13.85 ? 176 PHE A CB  1 
ATOM   1391 C  CG  . PHE A 1 175 ? -16.159 1.296   0.650   1.00 13.06 ? 176 PHE A CG  1 
ATOM   1392 C  CD1 . PHE A 1 175 ? -16.452 0.241   -0.225  1.00 13.46 ? 176 PHE A CD1 1 
ATOM   1393 C  CD2 . PHE A 1 175 ? -16.533 1.197   2.006   1.00 14.81 ? 176 PHE A CD2 1 
ATOM   1394 C  CE1 . PHE A 1 175 ? -17.062 -0.976  0.269   1.00 17.06 ? 176 PHE A CE1 1 
ATOM   1395 C  CE2 . PHE A 1 175 ? -17.109 0.032   2.515   1.00 12.25 ? 176 PHE A CE2 1 
ATOM   1396 C  CZ  . PHE A 1 175 ? -17.423 -1.049  1.643   1.00 16.24 ? 176 PHE A CZ  1 
ATOM   1397 N  N   . THR A 1 176 ? -18.551 4.515   -0.774  1.00 11.39 ? 177 THR A N   1 
ATOM   1398 C  CA  . THR A 1 176 ? -19.632 5.336   -0.238  1.00 12.41 ? 177 THR A CA  1 
ATOM   1399 C  C   . THR A 1 176 ? -20.820 4.496   0.204   1.00 10.87 ? 177 THR A C   1 
ATOM   1400 O  O   . THR A 1 176 ? -21.002 3.375   -0.279  1.00 13.09 ? 177 THR A O   1 
ATOM   1401 C  CB  . THR A 1 176 ? -20.121 6.452   -1.305  1.00 11.47 ? 177 THR A CB  1 
ATOM   1402 O  OG1 . THR A 1 176 ? -20.516 5.812   -2.492  1.00 14.99 ? 177 THR A OG1 1 
ATOM   1403 C  CG2 . THR A 1 176 ? -19.076 7.488   -1.570  1.00 18.89 ? 177 THR A CG2 1 
ATOM   1404 N  N   . ASN A 1 177 ? -21.622 5.105   1.079   1.00 9.52  ? 178 ASN A N   1 
ATOM   1405 C  CA  . ASN A 1 177 ? -22.933 4.631   1.505   1.00 10.18 ? 178 ASN A CA  1 
ATOM   1406 C  C   . ASN A 1 177 ? -22.825 3.300   2.295   1.00 11.20 ? 178 ASN A C   1 
ATOM   1407 O  O   . ASN A 1 177 ? -23.790 2.568   2.379   1.00 13.35 ? 178 ASN A O   1 
ATOM   1408 C  CB  . ASN A 1 177 ? -23.878 4.499   0.318   1.00 9.99  ? 178 ASN A CB  1 
ATOM   1409 C  CG  . ASN A 1 177 ? -24.128 5.874   -0.315  1.00 14.25 ? 178 ASN A CG  1 
ATOM   1410 O  OD1 . ASN A 1 177 ? -24.822 6.696   0.273   1.00 12.36 ? 178 ASN A OD1 1 
ATOM   1411 N  ND2 . ASN A 1 177 ? -23.436 6.163   -1.413  1.00 14.11 ? 178 ASN A ND2 1 
ATOM   1412 N  N   . PHE A 1 178 ? -21.669 3.078   2.919   1.00 9.22  ? 179 PHE A N   1 
ATOM   1413 C  CA  . PHE A 1 178 ? -21.519 1.800   3.689   1.00 10.79 ? 179 PHE A CA  1 
ATOM   1414 C  C   . PHE A 1 178 ? -22.012 2.106   5.077   1.00 10.85 ? 179 PHE A C   1 
ATOM   1415 O  O   . PHE A 1 178 ? -21.514 3.002   5.702   1.00 12.07 ? 179 PHE A O   1 
ATOM   1416 C  CB  . PHE A 1 178 ? -20.078 1.304   3.736   1.00 11.02 ? 179 PHE A CB  1 
ATOM   1417 C  CG  . PHE A 1 178 ? -19.934 0.058   4.540   1.00 8.18  ? 179 PHE A CG  1 
ATOM   1418 C  CD1 . PHE A 1 178 ? -20.355 -1.181  4.033   1.00 11.30 ? 179 PHE A CD1 1 
ATOM   1419 C  CD2 . PHE A 1 178 ? -19.529 0.171   5.880   1.00 8.12  ? 179 PHE A CD2 1 
ATOM   1420 C  CE1 . PHE A 1 178 ? -20.312 -2.327  4.804   1.00 9.95  ? 179 PHE A CE1 1 
ATOM   1421 C  CE2 . PHE A 1 178 ? -19.474 -1.043  6.716   1.00 7.97  ? 179 PHE A CE2 1 
ATOM   1422 C  CZ  . PHE A 1 178 ? -19.864 -2.236  6.187   1.00 9.25  ? 179 PHE A CZ  1 
ATOM   1423 N  N   . ASP A 1 179 ? -22.885 1.264   5.600   1.00 12.76 ? 180 ASP A N   1 
ATOM   1424 C  CA  . ASP A 1 179 ? -23.494 1.494   6.898   1.00 11.79 ? 180 ASP A CA  1 
ATOM   1425 C  C   . ASP A 1 179 ? -22.810 0.613   7.973   1.00 10.44 ? 180 ASP A C   1 
ATOM   1426 O  O   . ASP A 1 179 ? -23.045 -0.619  8.005   1.00 9.47  ? 180 ASP A O   1 
ATOM   1427 C  CB  . ASP A 1 179 ? -24.979 1.160   6.800   1.00 13.81 ? 180 ASP A CB  1 
ATOM   1428 C  CG  . ASP A 1 179 ? -25.742 1.458   8.097   1.00 14.56 ? 180 ASP A CG  1 
ATOM   1429 O  OD1 . ASP A 1 179 ? -25.123 1.749   9.158   1.00 10.58 ? 180 ASP A OD1 1 
ATOM   1430 O  OD2 . ASP A 1 179 ? -26.976 1.359   8.010   1.00 20.30 ? 180 ASP A OD2 1 
ATOM   1431 N  N   . PRO A 1 180 ? -21.964 1.240   8.858   1.00 9.70  ? 181 PRO A N   1 
ATOM   1432 C  CA  . PRO A 1 180 ? -21.214 0.377   9.868   1.00 10.69 ? 181 PRO A CA  1 
ATOM   1433 C  C   . PRO A 1 180 ? -22.156 -0.299  10.917  1.00 10.64 ? 181 PRO A C   1 
ATOM   1434 O  O   . PRO A 1 180 ? -21.717 -1.206  11.650  1.00 9.71  ? 181 PRO A O   1 
ATOM   1435 C  CB  . PRO A 1 180 ? -20.247 1.358   10.501  1.00 12.27 ? 181 PRO A CB  1 
ATOM   1436 C  CG  . PRO A 1 180 ? -21.005 2.763   10.411  1.00 7.95  ? 181 PRO A CG  1 
ATOM   1437 C  CD  . PRO A 1 180 ? -21.641 2.689   8.996   1.00 8.73  ? 181 PRO A CD  1 
ATOM   1438 N  N   . ARG A 1 181 ? -23.430 0.134   10.961  1.00 9.66  ? 182 ARG A N   1 
ATOM   1439 C  CA  . ARG A 1 181 ? -24.398 -0.577  11.884  1.00 10.00 ? 182 ARG A CA  1 
ATOM   1440 C  C   . ARG A 1 181 ? -24.500 -2.064  11.539  1.00 10.51 ? 182 ARG A C   1 
ATOM   1441 O  O   . ARG A 1 181 ? -24.879 -2.832  12.431  1.00 11.99 ? 182 ARG A O   1 
ATOM   1442 C  CB  . ARG A 1 181 ? -25.778 0.072   11.913  1.00 10.17 ? 182 ARG A CB  1 
ATOM   1443 C  CG  . ARG A 1 181 ? -25.651 1.591   12.343  1.00 10.55 ? 182 ARG A CG  1 
ATOM   1444 C  CD  . ARG A 1 181 ? -27.021 2.293   12.376  1.00 11.00 ? 182 ARG A CD  1 
ATOM   1445 N  NE  . ARG A 1 181 ? -27.492 2.403   11.007  1.00 14.39 ? 182 ARG A NE  1 
ATOM   1446 C  CZ  . ARG A 1 181 ? -28.622 2.960   10.654  1.00 18.55 ? 182 ARG A CZ  1 
ATOM   1447 N  NH1 . ARG A 1 181 ? -29.414 3.479   11.590  1.00 16.73 ? 182 ARG A NH1 1 
ATOM   1448 N  NH2 . ARG A 1 181 ? -28.935 2.976   9.369   1.00 16.57 ? 182 ARG A NH2 1 
ATOM   1449 N  N   . GLY A 1 182 ? -24.218 -2.441  10.284  1.00 9.98  ? 183 GLY A N   1 
ATOM   1450 C  CA  . GLY A 1 182 ? -24.298 -3.831  9.836   1.00 11.54 ? 183 GLY A CA  1 
ATOM   1451 C  C   . GLY A 1 182 ? -23.175 -4.695  10.381  1.00 13.21 ? 183 GLY A C   1 
ATOM   1452 O  O   . GLY A 1 182 ? -23.188 -5.898  10.180  1.00 14.31 ? 183 GLY A O   1 
ATOM   1453 N  N   . LEU A 1 183 ? -22.233 -4.077  11.102  1.00 10.35 ? 184 LEU A N   1 
ATOM   1454 C  CA  . LEU A 1 183 ? -21.076 -4.753  11.706  1.00 10.68 ? 184 LEU A CA  1 
ATOM   1455 C  C   . LEU A 1 183 ? -21.256 -4.974  13.212  1.00 10.92 ? 184 LEU A C   1 
ATOM   1456 O  O   . LEU A 1 183 ? -20.337 -5.496  13.841  1.00 13.23 ? 184 LEU A O   1 
ATOM   1457 C  CB  . LEU A 1 183 ? -19.763 -3.924  11.514  1.00 9.29  ? 184 LEU A CB  1 
ATOM   1458 C  CG  . LEU A 1 183 ? -19.444 -3.916  9.993   1.00 10.78 ? 184 LEU A CG  1 
ATOM   1459 C  CD1 . LEU A 1 183 ? -18.226 -3.091  9.734   1.00 13.33 ? 184 LEU A CD1 1 
ATOM   1460 C  CD2 . LEU A 1 183 ? -19.424 -5.283  9.281   1.00 10.63 ? 184 LEU A CD2 1 
ATOM   1461 N  N   . LEU A 1 184 ? -22.362 -4.456  13.828  1.00 9.55  ? 185 LEU A N   1 
ATOM   1462 C  CA  . LEU A 1 184 ? -22.503 -4.494  15.329  1.00 8.62  ? 185 LEU A CA  1 
ATOM   1463 C  C   . LEU A 1 184 ? -23.211 -5.828  15.761  1.00 9.92  ? 185 LEU A C   1 
ATOM   1464 O  O   . LEU A 1 184 ? -24.032 -6.426  14.980  1.00 13.08 ? 185 LEU A O   1 
ATOM   1465 C  CB  . LEU A 1 184 ? -23.379 -3.344  15.857  1.00 7.56  ? 185 LEU A CB  1 
ATOM   1466 C  CG  . LEU A 1 184 ? -22.817 -1.944  15.492  1.00 7.46  ? 185 LEU A CG  1 
ATOM   1467 C  CD1 . LEU A 1 184 ? -23.654 -0.748  15.887  1.00 13.06 ? 185 LEU A CD1 1 
ATOM   1468 C  CD2 . LEU A 1 184 ? -21.383 -1.822  16.067  1.00 10.70 ? 185 LEU A CD2 1 
ATOM   1469 N  N   . PRO A 1 185 ? -22.861 -6.324  16.955  1.00 9.41  ? 186 PRO A N   1 
ATOM   1470 C  CA  . PRO A 1 185 ? -23.555 -7.543  17.434  1.00 9.20  ? 186 PRO A CA  1 
ATOM   1471 C  C   . PRO A 1 185 ? -24.931 -7.083  17.980  1.00 10.43 ? 186 PRO A C   1 
ATOM   1472 O  O   . PRO A 1 185 ? -25.198 -5.883  18.054  1.00 9.99  ? 186 PRO A O   1 
ATOM   1473 C  CB  . PRO A 1 185 ? -22.643 -8.038  18.592  1.00 12.23 ? 186 PRO A CB  1 
ATOM   1474 C  CG  . PRO A 1 185 ? -22.014 -6.841  19.101  1.00 6.16  ? 186 PRO A CG  1 
ATOM   1475 C  CD  . PRO A 1 185 ? -21.768 -5.888  17.836  1.00 9.09  ? 186 PRO A CD  1 
ATOM   1476 N  N   . GLU A 1 186 ? -25.704 -7.992  18.560  1.00 10.47 ? 187 GLU A N   1 
ATOM   1477 C  CA  . GLU A 1 186 ? -27.001 -7.528  19.051  1.00 12.07 ? 187 GLU A CA  1 
ATOM   1478 C  C   . GLU A 1 186 ? -26.810 -6.779  20.414  1.00 11.20 ? 187 GLU A C   1 
ATOM   1479 O  O   . GLU A 1 186 ? -27.474 -5.795  20.673  1.00 11.16 ? 187 GLU A O   1 
ATOM   1480 C  CB  . GLU A 1 186 ? -27.851 -8.790  19.237  1.00 12.76 ? 187 GLU A CB  1 
ATOM   1481 C  CG  . GLU A 1 186 ? -28.969 -8.631  20.197  1.00 15.31 ? 187 GLU A CG  1 
ATOM   1482 C  CD  . GLU A 1 186 ? -29.632 -10.035 20.516  1.00 17.15 ? 187 GLU A CD  1 
ATOM   1483 O  OE1 . GLU A 1 186 ? -29.426 -10.985 19.700  1.00 15.32 ? 187 GLU A OE1 1 
ATOM   1484 O  OE2 . GLU A 1 186 ? -30.315 -10.102 21.608  1.00 23.23 ? 187 GLU A OE2 1 
ATOM   1485 N  N   . SER A 1 187 ? -25.955 -7.302  21.292  1.00 9.19  ? 188 SER A N   1 
ATOM   1486 C  CA  . SER A 1 187 ? -25.767 -6.689  22.638  1.00 10.49 ? 188 SER A CA  1 
ATOM   1487 C  C   . SER A 1 187 ? -24.628 -5.626  22.606  1.00 9.08  ? 188 SER A C   1 
ATOM   1488 O  O   . SER A 1 187 ? -23.595 -5.888  21.985  1.00 10.75 ? 188 SER A O   1 
ATOM   1489 C  CB  . SER A 1 187 ? -25.412 -7.746  23.711  1.00 12.71 ? 188 SER A CB  1 
ATOM   1490 O  OG  . SER A 1 187 ? -25.212 -7.151  24.994  1.00 11.27 ? 188 SER A OG  1 
ATOM   1491 N  N   . LEU A 1 188 ? -24.783 -4.558  23.369  1.00 8.10  ? 189 LEU A N   1 
ATOM   1492 C  CA  . LEU A 1 188 ? -23.679 -3.565  23.485  1.00 10.78 ? 189 LEU A CA  1 
ATOM   1493 C  C   . LEU A 1 188 ? -23.015 -3.702  24.896  1.00 8.83  ? 189 LEU A C   1 
ATOM   1494 O  O   . LEU A 1 188 ? -22.403 -2.729  25.341  1.00 11.70 ? 189 LEU A O   1 
ATOM   1495 C  CB  . LEU A 1 188 ? -24.221 -2.108  23.277  1.00 11.39 ? 189 LEU A CB  1 
ATOM   1496 C  CG  . LEU A 1 188 ? -24.720 -1.817  21.858  1.00 13.64 ? 189 LEU A CG  1 
ATOM   1497 C  CD1 . LEU A 1 188 ? -25.219 -0.330  21.683  1.00 16.56 ? 189 LEU A CD1 1 
ATOM   1498 C  CD2 . LEU A 1 188 ? -23.694 -2.253  20.751  1.00 14.74 ? 189 LEU A CD2 1 
ATOM   1499 N  N   . ASP A 1 189 ? -23.207 -4.842  25.614  1.00 9.67  ? 190 ASP A N   1 
ATOM   1500 C  CA  . ASP A 1 189 ? -22.465 -5.097  26.859  1.00 9.26  ? 190 ASP A CA  1 
ATOM   1501 C  C   . ASP A 1 189 ? -20.955 -5.016  26.511  1.00 8.06  ? 190 ASP A C   1 
ATOM   1502 O  O   . ASP A 1 189 ? -20.525 -5.480  25.447  1.00 7.38  ? 190 ASP A O   1 
ATOM   1503 C  CB  . ASP A 1 189 ? -22.743 -6.434  27.488  1.00 10.14 ? 190 ASP A CB  1 
ATOM   1504 C  CG  . ASP A 1 189 ? -24.180 -6.544  28.050  1.00 12.37 ? 190 ASP A CG  1 
ATOM   1505 O  OD1 . ASP A 1 189 ? -24.849 -5.501  28.228  1.00 15.63 ? 190 ASP A OD1 1 
ATOM   1506 O  OD2 . ASP A 1 189 ? -24.580 -7.683  28.329  1.00 21.78 ? 190 ASP A OD2 1 
ATOM   1507 N  N   . TYR A 1 190 ? -20.200 -4.397  27.410  1.00 7.92  ? 191 TYR A N   1 
ATOM   1508 C  CA  . TYR A 1 190 ? -18.776 -4.134  27.095  1.00 5.69  ? 191 TYR A CA  1 
ATOM   1509 C  C   . TYR A 1 190 ? -17.860 -4.224  28.314  1.00 8.05  ? 191 TYR A C   1 
ATOM   1510 O  O   . TYR A 1 190 ? -18.285 -4.047  29.451  1.00 8.33  ? 191 TYR A O   1 
ATOM   1511 C  CB  . TYR A 1 190 ? -18.610 -2.738  26.394  1.00 7.98  ? 191 TYR A CB  1 
ATOM   1512 C  CG  . TYR A 1 190 ? -19.024 -1.576  27.244  1.00 6.59  ? 191 TYR A CG  1 
ATOM   1513 C  CD1 . TYR A 1 190 ? -18.098 -0.969  28.169  1.00 6.94  ? 191 TYR A CD1 1 
ATOM   1514 C  CD2 . TYR A 1 190 ? -20.372 -1.110  27.205  1.00 5.60  ? 191 TYR A CD2 1 
ATOM   1515 C  CE1 . TYR A 1 190 ? -18.471 0.140   28.987  1.00 10.48 ? 191 TYR A CE1 1 
ATOM   1516 C  CE2 . TYR A 1 190 ? -20.764 -0.043  28.035  1.00 9.75  ? 191 TYR A CE2 1 
ATOM   1517 C  CZ  . TYR A 1 190 ? -19.806 0.570   28.940  1.00 9.85  ? 191 TYR A CZ  1 
ATOM   1518 O  OH  . TYR A 1 190 ? -20.237 1.591   29.696  1.00 11.26 ? 191 TYR A OH  1 
ATOM   1519 N  N   . TRP A 1 191 ? -16.584 -4.370  28.015  1.00 6.52  ? 192 TRP A N   1 
ATOM   1520 C  CA  . TRP A 1 191 ? -15.498 -4.095  29.000  1.00 6.85  ? 192 TRP A CA  1 
ATOM   1521 C  C   . TRP A 1 191 ? -14.793 -2.797  28.612  1.00 5.99  ? 192 TRP A C   1 
ATOM   1522 O  O   . TRP A 1 191 ? -14.792 -2.425  27.443  1.00 7.11  ? 192 TRP A O   1 
ATOM   1523 C  CB  . TRP A 1 191 ? -14.470 -5.162  28.883  1.00 6.10  ? 192 TRP A CB  1 
ATOM   1524 C  CG  . TRP A 1 191 ? -14.987 -6.501  29.381  1.00 5.70  ? 192 TRP A CG  1 
ATOM   1525 C  CD1 . TRP A 1 191 ? -15.223 -6.883  30.682  1.00 7.32  ? 192 TRP A CD1 1 
ATOM   1526 C  CD2 . TRP A 1 191 ? -15.228 -7.630  28.553  1.00 7.13  ? 192 TRP A CD2 1 
ATOM   1527 N  NE1 . TRP A 1 191 ? -15.605 -8.264  30.694  1.00 9.35  ? 192 TRP A NE1 1 
ATOM   1528 C  CE2 . TRP A 1 191 ? -15.656 -8.708  29.394  1.00 11.07 ? 192 TRP A CE2 1 
ATOM   1529 C  CE3 . TRP A 1 191 ? -15.168 -7.839  27.161  1.00 8.10  ? 192 TRP A CE3 1 
ATOM   1530 C  CZ2 . TRP A 1 191 ? -15.918 -10.021 28.863  1.00 10.26 ? 192 TRP A CZ2 1 
ATOM   1531 C  CZ3 . TRP A 1 191 ? -15.414 -9.129  26.678  1.00 5.71  ? 192 TRP A CZ3 1 
ATOM   1532 C  CH2 . TRP A 1 191 ? -15.829 -10.184 27.536  1.00 9.85  ? 192 TRP A CH2 1 
ATOM   1533 N  N   . THR A 1 192 ? -14.231 -2.100  29.591  1.00 5.07  ? 193 THR A N   1 
ATOM   1534 C  CA  . THR A 1 192 ? -13.506 -0.869  29.212  1.00 6.27  ? 193 THR A CA  1 
ATOM   1535 C  C   . THR A 1 192 ? -12.267 -0.626  30.058  1.00 6.46  ? 193 THR A C   1 
ATOM   1536 O  O   . THR A 1 192 ? -12.240 -1.004  31.231  1.00 8.05  ? 193 THR A O   1 
ATOM   1537 C  CB  . THR A 1 192 ? -14.420 0.373   29.309  1.00 6.99  ? 193 THR A CB  1 
ATOM   1538 O  OG1 . THR A 1 192 ? -13.727 1.565   28.859  1.00 5.70  ? 193 THR A OG1 1 
ATOM   1539 C  CG2 . THR A 1 192 ? -15.013 0.664   30.796  1.00 7.65  ? 193 THR A CG2 1 
ATOM   1540 N  N   . TYR A 1 193 ? -11.244 0.010   29.481  1.00 5.86  ? 194 TYR A N   1 
ATOM   1541 C  CA  . TYR A 1 193 ? -9.998  0.210   30.251  1.00 6.42  ? 194 TYR A CA  1 
ATOM   1542 C  C   . TYR A 1 193 ? -9.220  1.273   29.450  1.00 5.90  ? 194 TYR A C   1 
ATOM   1543 O  O   . TYR A 1 193 ? -9.476  1.411   28.234  1.00 5.58  ? 194 TYR A O   1 
ATOM   1544 C  CB  . TYR A 1 193 ? -9.162  -1.081  30.402  1.00 6.71  ? 194 TYR A CB  1 
ATOM   1545 C  CG  . TYR A 1 193 ? -8.464  -1.527  29.137  1.00 6.92  ? 194 TYR A CG  1 
ATOM   1546 C  CD1 . TYR A 1 193 ? -9.159  -2.208  28.125  1.00 6.22  ? 194 TYR A CD1 1 
ATOM   1547 C  CD2 . TYR A 1 193 ? -7.143  -1.110  28.885  1.00 4.87  ? 194 TYR A CD2 1 
ATOM   1548 C  CE1 . TYR A 1 193 ? -8.499  -2.629  26.915  1.00 6.49  ? 194 TYR A CE1 1 
ATOM   1549 C  CE2 . TYR A 1 193 ? -6.490  -1.472  27.669  1.00 9.06  ? 194 TYR A CE2 1 
ATOM   1550 C  CZ  . TYR A 1 193 ? -7.182  -2.174  26.698  1.00 7.63  ? 194 TYR A CZ  1 
ATOM   1551 O  OH  . TYR A 1 193 ? -6.528  -2.480  25.518  1.00 7.16  ? 194 TYR A OH  1 
ATOM   1552 N  N   . PRO A 1 194 ? -8.298  1.953   30.115  1.00 7.76  ? 195 PRO A N   1 
ATOM   1553 C  CA  . PRO A 1 194 ? -7.475  2.985   29.413  1.00 6.70  ? 195 PRO A CA  1 
ATOM   1554 C  C   . PRO A 1 194 ? -6.297  2.271   28.723  1.00 9.48  ? 195 PRO A C   1 
ATOM   1555 O  O   . PRO A 1 194 ? -5.621  1.506   29.374  1.00 7.90  ? 195 PRO A O   1 
ATOM   1556 C  CB  . PRO A 1 194 ? -6.938  3.894   30.592  1.00 9.92  ? 195 PRO A CB  1 
ATOM   1557 C  CG  . PRO A 1 194 ? -6.893  2.958   31.734  1.00 10.42 ? 195 PRO A CG  1 
ATOM   1558 C  CD  . PRO A 1 194 ? -8.067  1.991   31.578  1.00 6.66  ? 195 PRO A CD  1 
ATOM   1559 N  N   . GLY A 1 195 ? -6.057  2.597   27.445  1.00 6.92  ? 196 GLY A N   1 
ATOM   1560 C  CA  . GLY A 1 195 ? -4.953  1.881   26.721  1.00 7.43  ? 196 GLY A CA  1 
ATOM   1561 C  C   . GLY A 1 195 ? -4.393  2.813   25.632  1.00 6.43  ? 196 GLY A C   1 
ATOM   1562 O  O   . GLY A 1 195 ? -4.319  4.032   25.775  1.00 5.23  ? 196 GLY A O   1 
ATOM   1563 N  N   . SER A 1 196 ? -3.966  2.183   24.561  1.00 5.27  ? 197 SER A N   1 
ATOM   1564 C  CA  . SER A 1 196 ? -3.156  2.859   23.538  1.00 5.26  ? 197 SER A CA  1 
ATOM   1565 C  C   . SER A 1 196 ? -3.596  2.438   22.126  1.00 4.45  ? 197 SER A C   1 
ATOM   1566 O  O   . SER A 1 196 ? -4.307  1.427   21.960  1.00 4.94  ? 197 SER A O   1 
ATOM   1567 C  CB  . SER A 1 196 ? -1.679  2.416   23.639  1.00 6.18  ? 197 SER A CB  1 
ATOM   1568 O  OG  . SER A 1 196 ? -1.485  1.022   23.292  1.00 4.88  ? 197 SER A OG  1 
ATOM   1569 N  N   . LEU A 1 197 ? -3.095  3.163   21.110  1.00 5.28  ? 198 LEU A N   1 
ATOM   1570 C  CA  . LEU A 1 197 ? -3.111  2.605   19.722  1.00 6.07  ? 198 LEU A CA  1 
ATOM   1571 C  C   . LEU A 1 197 ? -2.319  1.266   19.786  1.00 4.69  ? 198 LEU A C   1 
ATOM   1572 O  O   . LEU A 1 197 ? -1.284  1.147   20.488  1.00 6.05  ? 198 LEU A O   1 
ATOM   1573 C  CB  . LEU A 1 197 ? -2.341  3.542   18.821  1.00 7.31  ? 198 LEU A CB  1 
ATOM   1574 C  CG  . LEU A 1 197 ? -2.836  4.972   18.761  1.00 4.34  ? 198 LEU A CG  1 
ATOM   1575 C  CD1 . LEU A 1 197 ? -2.027  5.704   17.699  1.00 7.50  ? 198 LEU A CD1 1 
ATOM   1576 C  CD2 . LEU A 1 197 ? -4.352  5.161   18.471  1.00 8.66  ? 198 LEU A CD2 1 
ATOM   1577 N  N   . THR A 1 198 ? -2.790  0.264   19.035  1.00 6.14  ? 199 THR A N   1 
ATOM   1578 C  CA  . THR A 1 198 ? -2.092  -1.020  18.981  1.00 4.89  ? 199 THR A CA  1 
ATOM   1579 C  C   . THR A 1 198 ? -1.069  -1.088  17.832  1.00 5.38  ? 199 THR A C   1 
ATOM   1580 O  O   . THR A 1 198 ? -0.507  -2.219  17.632  1.00 5.12  ? 199 THR A O   1 
ATOM   1581 C  CB  . THR A 1 198 ? -3.116  -2.245  18.831  1.00 6.43  ? 199 THR A CB  1 
ATOM   1582 O  OG1 . THR A 1 198 ? -3.822  -2.097  17.580  1.00 4.32  ? 199 THR A OG1 1 
ATOM   1583 C  CG2 . THR A 1 198 ? -4.149  -2.245  19.993  1.00 9.22  ? 199 THR A CG2 1 
ATOM   1584 N  N   . THR A 1 199 ? -0.925  -0.015  17.032  1.00 5.69  ? 200 THR A N   1 
ATOM   1585 C  CA  . THR A 1 199 ? 0.144   0.035   16.035  1.00 6.93  ? 200 THR A CA  1 
ATOM   1586 C  C   . THR A 1 199 ? 0.995   1.248   16.317  1.00 6.43  ? 200 THR A C   1 
ATOM   1587 O  O   . THR A 1 199 ? 0.508   2.271   16.927  1.00 6.02  ? 200 THR A O   1 
ATOM   1588 C  CB  . THR A 1 199 ? -0.418  0.112   14.581  1.00 7.63  ? 200 THR A CB  1 
ATOM   1589 O  OG1 . THR A 1 199 ? -1.422  1.164   14.490  1.00 10.60 ? 200 THR A OG1 1 
ATOM   1590 C  CG2 . THR A 1 199 ? -1.010  -1.235  14.172  1.00 7.21  ? 200 THR A CG2 1 
ATOM   1591 N  N   . PRO A 1 200 ? 2.282   1.173   15.862  1.00 7.99  ? 201 PRO A N   1 
ATOM   1592 C  CA  . PRO A 1 200 ? 3.008   2.465   15.969  1.00 8.44  ? 201 PRO A CA  1 
ATOM   1593 C  C   . PRO A 1 200 ? 2.182   3.648   15.384  1.00 9.46  ? 201 PRO A C   1 
ATOM   1594 O  O   . PRO A 1 200 ? 1.546   3.513   14.277  1.00 10.38 ? 201 PRO A O   1 
ATOM   1595 C  CB  . PRO A 1 200 ? 4.295   2.160   15.159  1.00 9.89  ? 201 PRO A CB  1 
ATOM   1596 C  CG  . PRO A 1 200 ? 4.499   0.726   15.315  1.00 9.90  ? 201 PRO A CG  1 
ATOM   1597 C  CD  . PRO A 1 200 ? 3.121   0.087   15.325  1.00 9.77  ? 201 PRO A CD  1 
ATOM   1598 N  N   . PRO A 1 201 ? 2.216   4.857   16.022  1.00 10.51 ? 202 PRO A N   1 
ATOM   1599 C  CA  . PRO A 1 201 ? 3.073   5.255   17.142  1.00 9.67  ? 202 PRO A CA  1 
ATOM   1600 C  C   . PRO A 1 201 ? 2.664   4.860   18.575  1.00 7.57  ? 202 PRO A C   1 
ATOM   1601 O  O   . PRO A 1 201 ? 3.336   5.292   19.566  1.00 8.17  ? 202 PRO A O   1 
ATOM   1602 C  CB  . PRO A 1 201 ? 3.130   6.794   16.997  1.00 11.87 ? 202 PRO A CB  1 
ATOM   1603 C  CG  . PRO A 1 201 ? 1.797   7.167   16.461  1.00 12.65 ? 202 PRO A CG  1 
ATOM   1604 C  CD  . PRO A 1 201 ? 1.457   6.050   15.500  1.00 11.38 ? 202 PRO A CD  1 
ATOM   1605 N  N   . LEU A 1 202 ? 1.678   3.929   18.716  1.00 7.34  ? 203 LEU A N   1 
ATOM   1606 C  CA  . LEU A 1 202 ? 1.421   3.299   20.036  1.00 6.86  ? 203 LEU A CA  1 
ATOM   1607 C  C   . LEU A 1 202 ? 1.063   4.352   21.158  1.00 6.10  ? 203 LEU A C   1 
ATOM   1608 O  O   . LEU A 1 202 ? 1.249   4.078   22.345  1.00 5.67  ? 203 LEU A O   1 
ATOM   1609 C  CB  . LEU A 1 202 ? 2.563   2.360   20.547  1.00 8.27  ? 203 LEU A CB  1 
ATOM   1610 C  CG  . LEU A 1 202 ? 2.948   1.232   19.571  1.00 8.10  ? 203 LEU A CG  1 
ATOM   1611 C  CD1 . LEU A 1 202 ? 4.220   0.520   20.150  1.00 7.40  ? 203 LEU A CD1 1 
ATOM   1612 C  CD2 . LEU A 1 202 ? 1.806   0.209   19.497  1.00 7.58  ? 203 LEU A CD2 1 
ATOM   1613 N  N   . LEU A 1 203 ? 0.438   5.438   20.711  1.00 6.20  ? 204 LEU A N   1 
ATOM   1614 C  CA  . LEU A 1 203 ? 0.126   6.588   21.595  1.00 7.80  ? 204 LEU A CA  1 
ATOM   1615 C  C   . LEU A 1 203 ? -0.857  6.159   22.674  1.00 7.88  ? 204 LEU A C   1 
ATOM   1616 O  O   . LEU A 1 203 ? -1.839  5.486   22.399  1.00 6.77  ? 204 LEU A O   1 
ATOM   1617 C  CB  . LEU A 1 203 ? -0.391  7.809   20.790  1.00 8.57  ? 204 LEU A CB  1 
ATOM   1618 C  CG  . LEU A 1 203 ? 0.725   8.342   19.839  1.00 9.13  ? 204 LEU A CG  1 
ATOM   1619 C  CD1 . LEU A 1 203 ? 0.093   9.383   18.887  1.00 14.24 ? 204 LEU A CD1 1 
ATOM   1620 C  CD2 . LEU A 1 203 ? 1.974   8.918   20.651  1.00 11.95 ? 204 LEU A CD2 1 
ATOM   1621 N  N   . GLU A 1 204 ? -0.645  6.664   23.888  1.00 6.88  ? 205 GLU A N   1 
ATOM   1622 C  CA  . GLU A 1 204 ? -1.493  6.281   25.004  1.00 5.76  ? 205 GLU A CA  1 
ATOM   1623 C  C   . GLU A 1 204 ? -2.686  7.214   25.169  1.00 7.40  ? 205 GLU A C   1 
ATOM   1624 O  O   . GLU A 1 204 ? -2.783  7.973   26.145  1.00 8.29  ? 205 GLU A O   1 
ATOM   1625 C  CB  . GLU A 1 204 ? -0.645  6.159   26.319  1.00 6.32  ? 205 GLU A CB  1 
ATOM   1626 C  CG  . GLU A 1 204 ? 0.205   4.840   26.113  1.00 5.92  ? 205 GLU A CG  1 
ATOM   1627 C  CD  . GLU A 1 204 ? 1.198   4.593   27.291  1.00 10.17 ? 205 GLU A CD  1 
ATOM   1628 O  OE1 . GLU A 1 204 ? 1.481   5.595   28.025  1.00 10.29 ? 205 GLU A OE1 1 
ATOM   1629 O  OE2 . GLU A 1 204 ? 1.649   3.437   27.467  1.00 9.51  ? 205 GLU A OE2 1 
ATOM   1630 N  N   . CYS A 1 205 ? -3.538  7.192   24.145  1.00 6.26  ? 206 CYS A N   1 
ATOM   1631 C  CA  . CYS A 1 205 ? -4.645  8.188   24.016  1.00 6.82  ? 206 CYS A CA  1 
ATOM   1632 C  C   . CYS A 1 205 ? -5.983  7.505   23.893  1.00 7.45  ? 206 CYS A C   1 
ATOM   1633 O  O   . CYS A 1 205 ? -6.928  8.177   23.461  1.00 8.28  ? 206 CYS A O   1 
ATOM   1634 C  CB  . CYS A 1 205 ? -4.377  9.021   22.781  1.00 7.38  ? 206 CYS A CB  1 
ATOM   1635 S  SG  . CYS A 1 205 ? -4.275  7.964   21.242  1.00 9.38  ? 206 CYS A SG  1 
ATOM   1636 N  N   . VAL A 1 206 ? -6.110  6.170   24.196  1.00 5.58  ? 207 VAL A N   1 
ATOM   1637 C  CA  . VAL A 1 206 ? -7.369  5.472   23.841  1.00 5.54  ? 207 VAL A CA  1 
ATOM   1638 C  C   . VAL A 1 206 ? -8.201  4.996   25.027  1.00 4.40  ? 207 VAL A C   1 
ATOM   1639 O  O   . VAL A 1 206 ? -7.604  4.370   25.946  1.00 6.31  ? 207 VAL A O   1 
ATOM   1640 C  CB  . VAL A 1 206 ? -7.085  4.208   22.965  1.00 5.99  ? 207 VAL A CB  1 
ATOM   1641 C  CG1 . VAL A 1 206 ? -8.437  3.443   22.583  1.00 5.95  ? 207 VAL A CG1 1 
ATOM   1642 C  CG2 . VAL A 1 206 ? -6.219  4.658   21.671  1.00 8.77  ? 207 VAL A CG2 1 
ATOM   1643 N  N   . THR A 1 207 ? -9.496  5.352   25.082  1.00 4.32  ? 208 THR A N   1 
ATOM   1644 C  CA  . THR A 1 207 ? -10.374 4.649   26.005  1.00 6.10  ? 208 THR A CA  1 
ATOM   1645 C  C   . THR A 1 207 ? -10.847 3.452   25.166  1.00 5.59  ? 208 THR A C   1 
ATOM   1646 O  O   . THR A 1 207 ? -11.596 3.654   24.137  1.00 6.32  ? 208 THR A O   1 
ATOM   1647 C  CB  . THR A 1 207 ? -11.608 5.543   26.439  1.00 5.33  ? 208 THR A CB  1 
ATOM   1648 O  OG1 . THR A 1 207 ? -11.052 6.646   27.180  1.00 6.87  ? 208 THR A OG1 1 
ATOM   1649 C  CG2 . THR A 1 207 ? -12.517 4.730   27.344  1.00 8.31  ? 208 THR A CG2 1 
ATOM   1650 N  N   . TRP A 1 208 ? -10.498 2.236   25.631  1.00 7.35  ? 209 TRP A N   1 
ATOM   1651 C  CA  . TRP A 1 208 ? -10.916 1.031   24.887  1.00 4.58  ? 209 TRP A CA  1 
ATOM   1652 C  C   . TRP A 1 208 ? -12.313 0.630   25.382  1.00 6.76  ? 209 TRP A C   1 
ATOM   1653 O  O   . TRP A 1 208 ? -12.542 0.552   26.571  1.00 7.34  ? 209 TRP A O   1 
ATOM   1654 C  CB  . TRP A 1 208 ? -9.949  -0.112  25.111  1.00 7.08  ? 209 TRP A CB  1 
ATOM   1655 C  CG  . TRP A 1 208 ? -8.808  0.017   24.122  1.00 7.59  ? 209 TRP A CG  1 
ATOM   1656 C  CD1 . TRP A 1 208 ? -7.557  0.616   24.306  1.00 8.74  ? 209 TRP A CD1 1 
ATOM   1657 C  CD2 . TRP A 1 208 ? -8.911  -0.318  22.740  1.00 9.17  ? 209 TRP A CD2 1 
ATOM   1658 N  NE1 . TRP A 1 208 ? -6.837  0.619   23.107  1.00 6.96  ? 209 TRP A NE1 1 
ATOM   1659 C  CE2 . TRP A 1 208 ? -7.652  0.024   22.125  1.00 7.06  ? 209 TRP A CE2 1 
ATOM   1660 C  CE3 . TRP A 1 208 ? -9.932  -0.934  21.959  1.00 6.79  ? 209 TRP A CE3 1 
ATOM   1661 C  CZ2 . TRP A 1 208 ? -7.400  -0.251  20.780  1.00 8.32  ? 209 TRP A CZ2 1 
ATOM   1662 C  CZ3 . TRP A 1 208 ? -9.700  -1.200  20.621  1.00 6.66  ? 209 TRP A CZ3 1 
ATOM   1663 C  CH2 . TRP A 1 208 ? -8.434  -0.889  20.040  1.00 7.84  ? 209 TRP A CH2 1 
ATOM   1664 N  N   . ILE A 1 209 ? -13.176 0.370   24.429  1.00 4.72  ? 210 ILE A N   1 
ATOM   1665 C  CA  . ILE A 1 209 ? -14.491 -0.201  24.751  1.00 6.42  ? 210 ILE A CA  1 
ATOM   1666 C  C   . ILE A 1 209 ? -14.625 -1.528  23.952  1.00 7.24  ? 210 ILE A C   1 
ATOM   1667 O  O   . ILE A 1 209 ? -14.726 -1.473  22.705  1.00 8.07  ? 210 ILE A O   1 
ATOM   1668 C  CB  . ILE A 1 209 ? -15.579 0.811   24.422  1.00 7.25  ? 210 ILE A CB  1 
ATOM   1669 C  CG1 . ILE A 1 209 ? -15.373 2.091   25.247  1.00 6.48  ? 210 ILE A CG1 1 
ATOM   1670 C  CG2 . ILE A 1 209 ? -16.977 0.122   24.637  1.00 6.85  ? 210 ILE A CG2 1 
ATOM   1671 C  CD1 . ILE A 1 209 ? -16.255 3.280   24.646  1.00 8.99  ? 210 ILE A CD1 1 
ATOM   1672 N  N   . VAL A 1 210 ? -14.676 -2.688  24.606  1.00 7.15  ? 211 VAL A N   1 
ATOM   1673 C  CA  . VAL A 1 210 ? -14.557 -3.953  23.852  1.00 6.41  ? 211 VAL A CA  1 
ATOM   1674 C  C   . VAL A 1 210 ? -15.841 -4.712  24.104  1.00 6.55  ? 211 VAL A C   1 
ATOM   1675 O  O   . VAL A 1 210 ? -16.181 -4.979  25.261  1.00 6.76  ? 211 VAL A O   1 
ATOM   1676 C  CB  . VAL A 1 210 ? -13.354 -4.873  24.334  1.00 6.36  ? 211 VAL A CB  1 
ATOM   1677 C  CG1 . VAL A 1 210 ? -13.297 -6.182  23.552  1.00 6.69  ? 211 VAL A CG1 1 
ATOM   1678 C  CG2 . VAL A 1 210 ? -12.034 -4.095  24.031  1.00 6.28  ? 211 VAL A CG2 1 
ATOM   1679 N  N   . LEU A 1 211 ? -16.608 -4.899  23.047  1.00 6.02  ? 212 LEU A N   1 
ATOM   1680 C  CA  . LEU A 1 211 ? -17.856 -5.598  23.210  1.00 6.75  ? 212 LEU A CA  1 
ATOM   1681 C  C   . LEU A 1 211 ? -17.714 -7.066  23.584  1.00 6.12  ? 212 LEU A C   1 
ATOM   1682 O  O   . LEU A 1 211 ? -16.897 -7.835  23.028  1.00 7.28  ? 212 LEU A O   1 
ATOM   1683 C  CB  . LEU A 1 211 ? -18.716 -5.459  21.932  1.00 5.23  ? 212 LEU A CB  1 
ATOM   1684 C  CG  . LEU A 1 211 ? -19.099 -4.090  21.420  1.00 7.48  ? 212 LEU A CG  1 
ATOM   1685 C  CD1 . LEU A 1 211 ? -20.155 -4.267  20.229  1.00 7.90  ? 212 LEU A CD1 1 
ATOM   1686 C  CD2 . LEU A 1 211 ? -19.645 -3.269  22.613  1.00 5.20  ? 212 LEU A CD2 1 
ATOM   1687 N  N   . LYS A 1 212 ? -18.582 -7.523  24.515  1.00 7.28  ? 213 LYS A N   1 
ATOM   1688 C  CA  . LYS A 1 212 ? -18.547 -8.978  24.924  1.00 8.93  ? 213 LYS A CA  1 
ATOM   1689 C  C   . LYS A 1 212 ? -19.014 -9.927  23.835  1.00 8.71  ? 213 LYS A C   1 
ATOM   1690 O  O   . LYS A 1 212 ? -18.482 -10.961 23.684  1.00 9.42  ? 213 LYS A O   1 
ATOM   1691 C  CB  . LYS A 1 212 ? -19.308 -9.178  26.246  1.00 11.01 ? 213 LYS A CB  1 
ATOM   1692 C  CG  . LYS A 1 212 ? -19.630 -10.673 26.611  1.00 10.74 ? 213 LYS A CG  1 
ATOM   1693 C  CD  . LYS A 1 212 ? -20.438 -10.807 27.940  1.00 14.98 ? 213 LYS A CD  1 
ATOM   1694 C  CE  . LYS A 1 212 ? -20.473 -12.271 28.407  1.00 23.23 ? 213 LYS A CE  1 
ATOM   1695 N  NZ  . LYS A 1 212 ? -21.506 -12.400 29.549  1.00 33.01 ? 213 LYS A NZ  1 
ATOM   1696 N  N   . GLU A 1 213 ? -20.011 -9.531  23.078  1.00 7.56  ? 214 GLU A N   1 
ATOM   1697 C  CA  . GLU A 1 213 ? -20.607 -10.409 22.054  1.00 7.57  ? 214 GLU A CA  1 
ATOM   1698 C  C   . GLU A 1 213 ? -19.850 -10.311 20.759  1.00 6.55  ? 214 GLU A C   1 
ATOM   1699 O  O   . GLU A 1 213 ? -19.860 -9.260  20.123  1.00 7.31  ? 214 GLU A O   1 
ATOM   1700 C  CB  . GLU A 1 213 ? -22.101 -10.016 21.867  1.00 7.54  ? 214 GLU A CB  1 
ATOM   1701 C  CG  . GLU A 1 213 ? -22.768 -11.065 21.033  1.00 10.58 ? 214 GLU A CG  1 
ATOM   1702 C  CD  . GLU A 1 213 ? -24.203 -10.812 20.723  1.00 18.51 ? 214 GLU A CD  1 
ATOM   1703 O  OE1 . GLU A 1 213 ? -24.854 -9.963  21.341  1.00 13.69 ? 214 GLU A OE1 1 
ATOM   1704 O  OE2 . GLU A 1 213 ? -24.682 -11.535 19.836  1.00 25.71 ? 214 GLU A OE2 1 
ATOM   1705 N  N   . PRO A 1 214 ? -19.265 -11.407 20.297  1.00 8.35  ? 215 PRO A N   1 
ATOM   1706 C  CA  . PRO A 1 214 ? -18.642 -11.325 18.984  1.00 9.83  ? 215 PRO A CA  1 
ATOM   1707 C  C   . PRO A 1 214 ? -19.696 -11.362 17.874  1.00 10.18 ? 215 PRO A C   1 
ATOM   1708 O  O   . PRO A 1 214 ? -20.842 -11.792 18.125  1.00 11.52 ? 215 PRO A O   1 
ATOM   1709 C  CB  . PRO A 1 214 ? -17.832 -12.621 18.893  1.00 9.55  ? 215 PRO A CB  1 
ATOM   1710 C  CG  . PRO A 1 214 ? -18.547 -13.595 19.864  1.00 13.95 ? 215 PRO A CG  1 
ATOM   1711 C  CD  . PRO A 1 214 ? -19.342 -12.785 20.852  1.00 10.39 ? 215 PRO A CD  1 
ATOM   1712 N  N   . ILE A 1 215 ? -19.326 -10.857 16.704  1.00 9.48  ? 216 ILE A N   1 
ATOM   1713 C  CA  . ILE A 1 215 ? -20.115 -11.106 15.499  1.00 9.68  ? 216 ILE A CA  1 
ATOM   1714 C  C   . ILE A 1 215 ? -19.604 -12.342 14.752  1.00 10.26 ? 216 ILE A C   1 
ATOM   1715 O  O   . ILE A 1 215 ? -18.402 -12.637 14.832  1.00 9.08  ? 216 ILE A O   1 
ATOM   1716 C  CB  . ILE A 1 215 ? -20.094 -9.884  14.508  1.00 7.97  ? 216 ILE A CB  1 
ATOM   1717 C  CG1 . ILE A 1 215 ? -18.645 -9.568  14.044  1.00 7.59  ? 216 ILE A CG1 1 
ATOM   1718 C  CG2 . ILE A 1 215 ? -20.820 -8.630  15.197  1.00 13.04 ? 216 ILE A CG2 1 
ATOM   1719 C  CD1 . ILE A 1 215 ? -18.613 -8.598  12.797  1.00 9.10  ? 216 ILE A CD1 1 
ATOM   1720 N  N   . SER A 1 216 ? -20.500 -13.001 13.991  1.00 9.66  ? 217 SER A N   1 
ATOM   1721 C  CA  . SER A 1 216 ? -20.130 -14.209 13.181  1.00 11.87 ? 217 SER A CA  1 
ATOM   1722 C  C   . SER A 1 216 ? -19.897 -13.754 11.756  1.00 9.90  ? 217 SER A C   1 
ATOM   1723 O  O   . SER A 1 216 ? -20.706 -12.972 11.271  1.00 11.57 ? 217 SER A O   1 
ATOM   1724 C  CB  . SER A 1 216 ? -21.281 -15.282 13.121  1.00 13.41 ? 217 SER A CB  1 
ATOM   1725 O  OG  . SER A 1 216 ? -21.308 -15.907 14.402  1.00 22.26 ? 217 SER A OG  1 
ATOM   1726 N  N   . VAL A 1 217 ? -18.814 -14.206 11.158  1.00 9.94  ? 218 VAL A N   1 
ATOM   1727 C  CA  . VAL A 1 217 ? -18.499 -14.009 9.754   1.00 9.40  ? 218 VAL A CA  1 
ATOM   1728 C  C   . VAL A 1 217 ? -18.194 -15.380 9.160   1.00 10.93 ? 218 VAL A C   1 
ATOM   1729 O  O   . VAL A 1 217 ? -17.910 -16.323 9.900   1.00 11.24 ? 218 VAL A O   1 
ATOM   1730 C  CB  . VAL A 1 217 ? -17.266 -13.049 9.561   1.00 8.38  ? 218 VAL A CB  1 
ATOM   1731 C  CG1 . VAL A 1 217 ? -17.582 -11.736 10.266  1.00 8.78  ? 218 VAL A CG1 1 
ATOM   1732 C  CG2 . VAL A 1 217 ? -15.959 -13.718 10.060  1.00 11.68 ? 218 VAL A CG2 1 
ATOM   1733 N  N   . SER A 1 218 ? -18.381 -15.530 7.841   1.00 10.69 ? 219 SER A N   1 
ATOM   1734 C  CA  . SER A 1 218 ? -18.146 -16.872 7.266   1.00 10.70 ? 219 SER A CA  1 
ATOM   1735 C  C   . SER A 1 218 ? -16.650 -17.111 7.019   1.00 10.12 ? 219 SER A C   1 
ATOM   1736 O  O   . SER A 1 218 ? -15.822 -16.165 6.880   1.00 9.40  ? 219 SER A O   1 
ATOM   1737 C  CB  . SER A 1 218 ? -18.967 -17.026 5.992   1.00 10.46 ? 219 SER A CB  1 
ATOM   1738 O  OG  . SER A 1 218 ? -18.410 -16.133 5.047   1.00 10.47 ? 219 SER A OG  1 
ATOM   1739 N  N   A SER A 1 219 ? -16.281 -18.386 6.922   0.50 10.09 ? 220 SER A N   1 
ATOM   1740 N  N   B SER A 1 219 ? -16.315 -18.387 6.928   0.50 10.10 ? 220 SER A N   1 
ATOM   1741 C  CA  A SER A 1 219 ? -14.933 -18.761 6.515   0.50 11.11 ? 220 SER A CA  1 
ATOM   1742 C  CA  B SER A 1 219 ? -14.991 -18.769 6.549   0.50 11.25 ? 220 SER A CA  1 
ATOM   1743 C  C   A SER A 1 219 ? -14.567 -18.059 5.203   0.50 10.96 ? 220 SER A C   1 
ATOM   1744 C  C   B SER A 1 219 ? -14.594 -18.069 5.234   0.50 10.90 ? 220 SER A C   1 
ATOM   1745 O  O   A SER A 1 219 ? -13.436 -17.510 5.070   0.50 12.28 ? 220 SER A O   1 
ATOM   1746 O  O   B SER A 1 219 ? -13.473 -17.505 5.150   0.50 12.42 ? 220 SER A O   1 
ATOM   1747 C  CB  A SER A 1 219 ? -14.811 -20.282 6.402   0.50 10.94 ? 220 SER A CB  1 
ATOM   1748 C  CB  B SER A 1 219 ? -14.878 -20.290 6.507   0.50 10.70 ? 220 SER A CB  1 
ATOM   1749 O  OG  A SER A 1 219 ? -15.869 -20.764 5.593   0.50 9.64  ? 220 SER A OG  1 
ATOM   1750 O  OG  B SER A 1 219 ? -13.586 -20.648 6.123   0.50 11.41 ? 220 SER A OG  1 
ATOM   1751 N  N   . GLU A 1 220 ? -15.499 -18.008 4.240   1.00 12.17 ? 221 GLU A N   1 
ATOM   1752 C  CA  . GLU A 1 220 ? -15.225 -17.373 2.919   1.00 11.77 ? 221 GLU A CA  1 
ATOM   1753 C  C   . GLU A 1 220 ? -14.915 -15.854 3.101   1.00 12.17 ? 221 GLU A C   1 
ATOM   1754 O  O   . GLU A 1 220 ? -13.979 -15.295 2.457   1.00 11.23 ? 221 GLU A O   1 
ATOM   1755 C  CB  . GLU A 1 220 ? -16.349 -17.596 1.929   1.00 14.24 ? 221 GLU A CB  1 
ATOM   1756 C  CG  . GLU A 1 220 ? -16.590 -19.120 1.629   1.00 17.72 ? 221 GLU A CG  1 
ATOM   1757 C  CD  . GLU A 1 220 ? -17.599 -19.770 2.588   1.00 23.38 ? 221 GLU A CD  1 
ATOM   1758 O  OE1 . GLU A 1 220 ? -17.933 -19.261 3.676   1.00 21.13 ? 221 GLU A OE1 1 
ATOM   1759 O  OE2 . GLU A 1 220 ? -18.058 -20.874 2.250   1.00 30.58 ? 221 GLU A OE2 1 
ATOM   1760 N  N   . GLN A 1 221 ? -15.678 -15.197 3.998   1.00 10.08 ? 222 GLN A N   1 
ATOM   1761 C  CA  . GLN A 1 221 ? -15.416 -13.759 4.303   1.00 10.76 ? 222 GLN A CA  1 
ATOM   1762 C  C   . GLN A 1 221 ? -13.997 -13.518 4.819   1.00 11.52 ? 222 GLN A C   1 
ATOM   1763 O  O   . GLN A 1 221 ? -13.249 -12.718 4.214   1.00 9.54  ? 222 GLN A O   1 
ATOM   1764 C  CB  . GLN A 1 221 ? -16.492 -13.206 5.245   1.00 11.00 ? 222 GLN A CB  1 
ATOM   1765 C  CG  . GLN A 1 221 ? -17.809 -12.965 4.443   1.00 10.53 ? 222 GLN A CG  1 
ATOM   1766 C  CD  . GLN A 1 221 ? -18.994 -12.498 5.310   1.00 9.92  ? 222 GLN A CD  1 
ATOM   1767 O  OE1 . GLN A 1 221 ? -19.129 -12.916 6.474   1.00 10.71 ? 222 GLN A OE1 1 
ATOM   1768 N  NE2 . GLN A 1 221 ? -19.871 -11.665 4.742   1.00 9.55  ? 222 GLN A NE2 1 
ATOM   1769 N  N   . VAL A 1 222 ? -13.590 -14.253 5.877   1.00 10.72 ? 223 VAL A N   1 
ATOM   1770 C  CA  . VAL A 1 222 ? -12.249 -14.051 6.474   1.00 11.53 ? 223 VAL A CA  1 
ATOM   1771 C  C   . VAL A 1 222 ? -11.129 -14.522 5.482   1.00 11.29 ? 223 VAL A C   1 
ATOM   1772 O  O   . VAL A 1 222 ? -10.109 -13.871 5.373   1.00 10.91 ? 223 VAL A O   1 
ATOM   1773 C  CB  . VAL A 1 222 ? -12.154 -14.652 7.903   1.00 12.27 ? 223 VAL A CB  1 
ATOM   1774 C  CG1 . VAL A 1 222 ? -12.153 -16.162 7.814   1.00 14.78 ? 223 VAL A CG1 1 
ATOM   1775 C  CG2 . VAL A 1 222 ? -10.834 -14.110 8.579   1.00 11.04 ? 223 VAL A CG2 1 
ATOM   1776 N  N   . LEU A 1 223 ? -11.429 -15.549 4.653   1.00 11.31 ? 224 LEU A N   1 
ATOM   1777 C  CA  . LEU A 1 223 ? -10.496 -15.962 3.581   1.00 12.51 ? 224 LEU A CA  1 
ATOM   1778 C  C   . LEU A 1 223 ? -10.157 -14.849 2.651   1.00 12.79 ? 224 LEU A C   1 
ATOM   1779 O  O   . LEU A 1 223 ? -8.954  -14.690 2.297   1.00 12.28 ? 224 LEU A O   1 
ATOM   1780 C  CB  . LEU A 1 223 ? -11.029 -17.177 2.772   1.00 13.75 ? 224 LEU A CB  1 
ATOM   1781 C  CG  . LEU A 1 223 ? -10.801 -18.375 3.648   1.00 18.68 ? 224 LEU A CG  1 
ATOM   1782 C  CD1 . LEU A 1 223 ? -11.848 -19.576 3.336   1.00 22.81 ? 224 LEU A CD1 1 
ATOM   1783 C  CD2 . LEU A 1 223 ? -9.307  -18.812 3.617   1.00 21.22 ? 224 LEU A CD2 1 
ATOM   1784 N  N   . LYS A 1 224 ? -11.176 -14.077 2.306   1.00 12.74 ? 225 LYS A N   1 
ATOM   1785 C  CA  . LYS A 1 224 ? -10.972 -12.898 1.445   1.00 14.74 ? 225 LYS A CA  1 
ATOM   1786 C  C   . LYS A 1 224 ? -10.060 -11.873 2.135   1.00 12.57 ? 225 LYS A C   1 
ATOM   1787 O  O   . LYS A 1 224 ? -9.234  -11.239 1.427   1.00 12.37 ? 225 LYS A O   1 
ATOM   1788 C  CB  . LYS A 1 224 ? -12.306 -12.392 0.867   1.00 14.66 ? 225 LYS A CB  1 
ATOM   1789 C  CG  . LYS A 1 224 ? -12.810 -13.471 -0.227  1.00 16.17 ? 225 LYS A CG  1 
ATOM   1790 C  CD  . LYS A 1 224 ? -14.196 -13.176 -0.820  1.00 18.40 ? 225 LYS A CD  1 
ATOM   1791 C  CE  . LYS A 1 224 ? -14.645 -14.292 -1.807  1.00 19.75 ? 225 LYS A CE  1 
ATOM   1792 N  NZ  . LYS A 1 224 ? -15.954 -13.972 -2.474  1.00 23.51 ? 225 LYS A NZ  1 
ATOM   1793 N  N   . PHE A 1 225 ? -10.177 -11.636 3.458   1.00 10.22 ? 226 PHE A N   1 
ATOM   1794 C  CA  . PHE A 1 225 ? -9.237  -10.681 4.107   1.00 9.48  ? 226 PHE A CA  1 
ATOM   1795 C  C   . PHE A 1 225 ? -7.801  -11.164 3.859   1.00 8.97  ? 226 PHE A C   1 
ATOM   1796 O  O   . PHE A 1 225 ? -6.855  -10.384 3.658   1.00 10.13 ? 226 PHE A O   1 
ATOM   1797 C  CB  . PHE A 1 225 ? -9.460  -10.751 5.622   1.00 9.68  ? 226 PHE A CB  1 
ATOM   1798 C  CG  . PHE A 1 225 ? -10.652 -9.952  6.135   1.00 8.06  ? 226 PHE A CG  1 
ATOM   1799 C  CD1 . PHE A 1 225 ? -11.716 -9.578  5.304   1.00 11.78 ? 226 PHE A CD1 1 
ATOM   1800 C  CD2 . PHE A 1 225 ? -10.759 -9.737  7.496   1.00 10.57 ? 226 PHE A CD2 1 
ATOM   1801 C  CE1 . PHE A 1 225 ? -12.813 -8.823  5.850   1.00 12.25 ? 226 PHE A CE1 1 
ATOM   1802 C  CE2 . PHE A 1 225 ? -11.846 -9.038  8.025   1.00 13.85 ? 226 PHE A CE2 1 
ATOM   1803 C  CZ  . PHE A 1 225 ? -12.840 -8.574  7.206   1.00 13.51 ? 226 PHE A CZ  1 
ATOM   1804 N  N   . ARG A 1 226 ? -7.632  -12.481 3.989   1.00 9.60  ? 227 ARG A N   1 
ATOM   1805 C  CA  . ARG A 1 226 ? -6.272  -13.103 3.881   1.00 11.81 ? 227 ARG A CA  1 
ATOM   1806 C  C   . ARG A 1 226 ? -5.661  -13.128 2.477   1.00 11.01 ? 227 ARG A C   1 
ATOM   1807 O  O   . ARG A 1 226 ? -4.477  -13.554 2.327   1.00 13.53 ? 227 ARG A O   1 
ATOM   1808 C  CB  . ARG A 1 226 ? -6.314  -14.550 4.413   1.00 11.15 ? 227 ARG A CB  1 
ATOM   1809 C  CG  . ARG A 1 226 ? -6.718  -14.716 5.868   1.00 9.88  ? 227 ARG A CG  1 
ATOM   1810 C  CD  . ARG A 1 226 ? -6.645  -16.212 6.392   1.00 10.47 ? 227 ARG A CD  1 
ATOM   1811 N  NE  . ARG A 1 226 ? -7.290  -16.294 7.753   1.00 9.95  ? 227 ARG A NE  1 
ATOM   1812 C  CZ  . ARG A 1 226 ? -8.329  -17.080 8.070   1.00 11.65 ? 227 ARG A CZ  1 
ATOM   1813 N  NH1 . ARG A 1 226 ? -8.787  -17.990 7.176   1.00 16.43 ? 227 ARG A NH1 1 
ATOM   1814 N  NH2 . ARG A 1 226 ? -8.821  -17.055 9.302   1.00 11.69 ? 227 ARG A NH2 1 
ATOM   1815 N  N   . LYS A 1 227 ? -6.409  -12.644 1.478   1.00 9.93  ? 228 LYS A N   1 
ATOM   1816 C  CA  . LYS A 1 227 ? -5.875  -12.524 0.128   1.00 11.84 ? 228 LYS A CA  1 
ATOM   1817 C  C   . LYS A 1 227 ? -5.233  -11.179 -0.120  1.00 11.71 ? 228 LYS A C   1 
ATOM   1818 O  O   . LYS A 1 227 ? -4.586  -10.977 -1.148  1.00 13.06 ? 228 LYS A O   1 
ATOM   1819 C  CB  . LYS A 1 227 ? -6.980  -12.745 -0.908  1.00 12.11 ? 228 LYS A CB  1 
ATOM   1820 C  CG  . LYS A 1 227 ? -7.270  -14.255 -1.056  1.00 17.19 ? 228 LYS A CG  1 
ATOM   1821 C  CD  . LYS A 1 227 ? -8.422  -14.333 -2.065  1.00 30.08 ? 228 LYS A CD  1 
ATOM   1822 C  CE  . LYS A 1 227 ? -8.146  -15.257 -3.231  1.00 38.30 ? 228 LYS A CE  1 
ATOM   1823 N  NZ  . LYS A 1 227 ? -8.878  -16.573 -3.031  1.00 43.71 ? 228 LYS A NZ  1 
ATOM   1824 N  N   . LEU A 1 228 ? -5.494  -10.231 0.793   1.00 9.99  ? 229 LEU A N   1 
ATOM   1825 C  CA  . LEU A 1 228 ? -4.839  -8.922  0.716   1.00 9.60  ? 229 LEU A CA  1 
ATOM   1826 C  C   . LEU A 1 228 ? -3.293  -9.123  0.848   1.00 9.16  ? 229 LEU A C   1 
ATOM   1827 O  O   . LEU A 1 228 ? -2.782  -10.188 1.244   1.00 10.02 ? 229 LEU A O   1 
ATOM   1828 C  CB  . LEU A 1 228 ? -5.299  -7.973  1.813   1.00 6.46  ? 229 LEU A CB  1 
ATOM   1829 C  CG  . LEU A 1 228 ? -6.750  -7.504  1.544   1.00 12.00 ? 229 LEU A CG  1 
ATOM   1830 C  CD1 . LEU A 1 228 ? -7.408  -6.911  2.756   1.00 11.80 ? 229 LEU A CD1 1 
ATOM   1831 C  CD2 . LEU A 1 228 ? -6.825  -6.440  0.362   1.00 11.56 ? 229 LEU A CD2 1 
ATOM   1832 N  N   . ASN A 1 229 ? -2.578  -8.062  0.487   1.00 10.68 ? 230 ASN A N   1 
ATOM   1833 C  CA  . ASN A 1 229 ? -1.118  -8.058  0.472   1.00 10.44 ? 230 ASN A CA  1 
ATOM   1834 C  C   . ASN A 1 229 ? -0.530  -6.898  1.359   1.00 9.71  ? 230 ASN A C   1 
ATOM   1835 O  O   . ASN A 1 229 ? -1.062  -5.746  1.307   1.00 8.10  ? 230 ASN A O   1 
ATOM   1836 C  CB  . ASN A 1 229 ? -0.657  -7.802  -0.972  1.00 12.14 ? 230 ASN A CB  1 
ATOM   1837 C  CG  . ASN A 1 229 ? -0.593  -9.071  -1.880  1.00 11.88 ? 230 ASN A CG  1 
ATOM   1838 O  OD1 . ASN A 1 229 ? -0.056  -8.933  -2.993  1.00 15.00 ? 230 ASN A OD1 1 
ATOM   1839 N  ND2 . ASN A 1 229 ? -1.220  -10.196 -1.515  1.00 7.74  ? 230 ASN A ND2 1 
ATOM   1840 N  N   . PHE A 1 230 ? 0.526   -7.184  2.162   1.00 10.53 ? 231 PHE A N   1 
ATOM   1841 C  CA  . PHE A 1 230 ? 1.271   -6.113  2.877   1.00 10.45 ? 231 PHE A CA  1 
ATOM   1842 C  C   . PHE A 1 230 ? 2.093   -5.257  1.873   1.00 11.23 ? 231 PHE A C   1 
ATOM   1843 O  O   . PHE A 1 230 ? 2.288   -4.027  2.092   1.00 11.22 ? 231 PHE A O   1 
ATOM   1844 C  CB  . PHE A 1 230 ? 2.275   -6.663  3.851   1.00 12.76 ? 231 PHE A CB  1 
ATOM   1845 C  CG  . PHE A 1 230 ? 1.670   -7.269  5.103   1.00 10.73 ? 231 PHE A CG  1 
ATOM   1846 C  CD1 . PHE A 1 230 ? 0.792   -6.502  5.932   1.00 9.99  ? 231 PHE A CD1 1 
ATOM   1847 C  CD2 . PHE A 1 230 ? 1.990   -8.594  5.479   1.00 10.63 ? 231 PHE A CD2 1 
ATOM   1848 C  CE1 . PHE A 1 230 ? 0.249   -7.087  7.150   1.00 11.06 ? 231 PHE A CE1 1 
ATOM   1849 C  CE2 . PHE A 1 230 ? 1.501   -9.171  6.689   1.00 11.93 ? 231 PHE A CE2 1 
ATOM   1850 C  CZ  . PHE A 1 230 ? 0.608   -8.414  7.524   1.00 12.21 ? 231 PHE A CZ  1 
ATOM   1851 N  N   . ASN A 1 231 ? 2.520   -5.949  0.807   1.00 11.57 ? 232 ASN A N   1 
ATOM   1852 C  CA  . ASN A 1 231 ? 3.438   -5.319  -0.156  1.00 11.60 ? 232 ASN A CA  1 
ATOM   1853 C  C   . ASN A 1 231 ? 2.690   -4.401  -1.149  1.00 11.29 ? 232 ASN A C   1 
ATOM   1854 O  O   . ASN A 1 231 ? 1.441   -4.550  -1.351  1.00 12.48 ? 232 ASN A O   1 
ATOM   1855 C  CB  . ASN A 1 231 ? 4.120   -6.428  -0.944  1.00 11.49 ? 232 ASN A CB  1 
ATOM   1856 C  CG  . ASN A 1 231 ? 3.126   -7.329  -1.617  1.00 11.65 ? 232 ASN A CG  1 
ATOM   1857 O  OD1 . ASN A 1 231 ? 2.526   -8.190  -0.952  1.00 14.10 ? 232 ASN A OD1 1 
ATOM   1858 N  ND2 . ASN A 1 231 ? 2.872   -7.099  -2.938  1.00 13.37 ? 232 ASN A ND2 1 
ATOM   1859 N  N   . GLY A 1 232 ? 3.447   -3.491  -1.778  1.00 13.03 ? 233 GLY A N   1 
ATOM   1860 C  CA  . GLY A 1 232 ? 2.919   -2.743  -2.957  1.00 14.67 ? 233 GLY A CA  1 
ATOM   1861 C  C   . GLY A 1 232 ? 2.886   -3.569  -4.201  1.00 14.46 ? 233 GLY A C   1 
ATOM   1862 O  O   . GLY A 1 232 ? 3.580   -4.603  -4.314  1.00 15.34 ? 233 GLY A O   1 
ATOM   1863 N  N   . GLU A 1 233 ? 2.151   -3.048  -5.165  1.00 15.51 ? 234 GLU A N   1 
ATOM   1864 C  CA  . GLU A 1 233 ? 2.099   -3.585  -6.490  1.00 16.37 ? 234 GLU A CA  1 
ATOM   1865 C  C   . GLU A 1 233 ? 3.486   -3.774  -7.110  1.00 16.43 ? 234 GLU A C   1 
ATOM   1866 O  O   . GLU A 1 233 ? 4.326   -2.860  -7.097  1.00 16.68 ? 234 GLU A O   1 
ATOM   1867 C  CB  . GLU A 1 233 ? 1.275   -2.684  -7.402  1.00 14.94 ? 234 GLU A CB  1 
ATOM   1868 C  CG  . GLU A 1 233 ? 0.932   -3.317  -8.699  1.00 16.05 ? 234 GLU A CG  1 
ATOM   1869 C  CD  . GLU A 1 233 ? 0.172   -2.398  -9.624  1.00 24.14 ? 234 GLU A CD  1 
ATOM   1870 O  OE1 . GLU A 1 233 ? -0.132  -1.198  -9.227  1.00 21.52 ? 234 GLU A OE1 1 
ATOM   1871 O  OE2 . GLU A 1 233 ? -0.067  -2.870  -10.771 1.00 24.52 ? 234 GLU A OE2 1 
ATOM   1872 N  N   . GLY A 1 234 ? 3.626   -4.949  -7.723  1.00 18.11 ? 235 GLY A N   1 
ATOM   1873 C  CA  . GLY A 1 234 ? 4.868   -5.380  -8.368  1.00 22.46 ? 235 GLY A CA  1 
ATOM   1874 C  C   . GLY A 1 234 ? 6.014   -5.580  -7.392  1.00 24.15 ? 235 GLY A C   1 
ATOM   1875 O  O   . GLY A 1 234 ? 7.197   -5.489  -7.779  1.00 25.12 ? 235 GLY A O   1 
ATOM   1876 N  N   . GLU A 1 235 ? 5.674   -5.822  -6.119  1.00 22.62 ? 236 GLU A N   1 
ATOM   1877 C  CA  . GLU A 1 235 ? 6.665   -6.311  -5.152  1.00 22.27 ? 236 GLU A CA  1 
ATOM   1878 C  C   . GLU A 1 235 ? 6.359   -7.744  -4.852  1.00 21.07 ? 236 GLU A C   1 
ATOM   1879 O  O   . GLU A 1 235 ? 5.279   -8.254  -5.220  1.00 23.37 ? 236 GLU A O   1 
ATOM   1880 C  CB  . GLU A 1 235 ? 6.662   -5.486  -3.871  1.00 21.84 ? 236 GLU A CB  1 
ATOM   1881 C  CG  . GLU A 1 235 ? 6.980   -4.054  -4.165  1.00 23.49 ? 236 GLU A CG  1 
ATOM   1882 C  CD  . GLU A 1 235 ? 6.941   -3.170  -2.929  1.00 30.98 ? 236 GLU A CD  1 
ATOM   1883 O  OE1 . GLU A 1 235 ? 6.279   -3.512  -1.895  1.00 25.65 ? 236 GLU A OE1 1 
ATOM   1884 O  OE2 . GLU A 1 235 ? 7.612   -2.121  -2.976  1.00 35.34 ? 236 GLU A OE2 1 
ATOM   1885 N  N   . PRO A 1 236 ? 7.324   -8.442  -4.222  1.00 22.33 ? 237 PRO A N   1 
ATOM   1886 C  CA  . PRO A 1 236 ? 7.120   -9.883  -3.869  1.00 21.10 ? 237 PRO A CA  1 
ATOM   1887 C  C   . PRO A 1 236 ? 5.884   -9.985  -2.928  1.00 19.20 ? 237 PRO A C   1 
ATOM   1888 O  O   . PRO A 1 236 ? 5.672   -9.127  -2.081  1.00 18.28 ? 237 PRO A O   1 
ATOM   1889 C  CB  . PRO A 1 236 ? 8.431   -10.281 -3.175  1.00 21.58 ? 237 PRO A CB  1 
ATOM   1890 C  CG  . PRO A 1 236 ? 9.474   -9.285  -3.772  1.00 24.31 ? 237 PRO A CG  1 
ATOM   1891 C  CD  . PRO A 1 236 ? 8.648   -7.958  -3.769  1.00 22.12 ? 237 PRO A CD  1 
ATOM   1892 N  N   . GLU A 1 237 ? 5.043   -10.955 -3.223  1.00 17.54 ? 238 GLU A N   1 
ATOM   1893 C  CA  . GLU A 1 237 ? 3.771   -11.058 -2.534  1.00 17.05 ? 238 GLU A CA  1 
ATOM   1894 C  C   . GLU A 1 237 ? 4.004   -11.576 -1.099  1.00 17.00 ? 238 GLU A C   1 
ATOM   1895 O  O   . GLU A 1 237 ? 4.591   -12.635 -0.876  1.00 16.49 ? 238 GLU A O   1 
ATOM   1896 C  CB  . GLU A 1 237 ? 2.775   -11.960 -3.267  1.00 18.57 ? 238 GLU A CB  1 
ATOM   1897 C  CG  . GLU A 1 237 ? 1.378   -11.896 -2.603  1.00 17.83 ? 238 GLU A CG  1 
ATOM   1898 C  CD  . GLU A 1 237 ? 0.303   -12.711 -3.260  1.00 22.05 ? 238 GLU A CD  1 
ATOM   1899 O  OE1 . GLU A 1 237 ? 0.661   -13.794 -3.821  1.00 30.44 ? 238 GLU A OE1 1 
ATOM   1900 O  OE2 . GLU A 1 237 ? -0.898  -12.345 -3.183  1.00 16.86 ? 238 GLU A OE2 1 
ATOM   1901 N  N   . GLU A 1 238 ? 3.422   -10.831 -0.145  1.00 14.55 ? 239 GLU A N   1 
ATOM   1902 C  CA  . GLU A 1 238 ? 3.445   -11.120 1.285   1.00 16.33 ? 239 GLU A CA  1 
ATOM   1903 C  C   . GLU A 1 238 ? 1.967   -11.022 1.652   1.00 12.69 ? 239 GLU A C   1 
ATOM   1904 O  O   . GLU A 1 238 ? 1.416   -9.914  1.579   1.00 12.66 ? 239 GLU A O   1 
ATOM   1905 C  CB  . GLU A 1 238 ? 4.175   -10.046 2.099   1.00 14.15 ? 239 GLU A CB  1 
ATOM   1906 C  CG  . GLU A 1 238 ? 5.541   -9.611  1.557   1.00 21.52 ? 239 GLU A CG  1 
ATOM   1907 C  CD  . GLU A 1 238 ? 6.043   -8.240  2.162   1.00 21.54 ? 239 GLU A CD  1 
ATOM   1908 O  OE1 . GLU A 1 238 ? 5.750   -7.901  3.350   1.00 24.55 ? 239 GLU A OE1 1 
ATOM   1909 O  OE2 . GLU A 1 238 ? 6.695   -7.499  1.405   1.00 35.30 ? 239 GLU A OE2 1 
ATOM   1910 N  N   . LEU A 1 239 ? 1.291   -12.159 1.901   1.00 10.42 ? 240 LEU A N   1 
ATOM   1911 C  CA  . LEU A 1 239 ? -0.121  -12.074 2.284   1.00 9.24  ? 240 LEU A CA  1 
ATOM   1912 C  C   . LEU A 1 239 ? -0.268  -11.253 3.579   1.00 6.36  ? 240 LEU A C   1 
ATOM   1913 O  O   . LEU A 1 239 ? 0.559   -11.389 4.528   1.00 9.02  ? 240 LEU A O   1 
ATOM   1914 C  CB  . LEU A 1 239 ? -0.710  -13.494 2.594   1.00 9.07  ? 240 LEU A CB  1 
ATOM   1915 C  CG  . LEU A 1 239 ? -0.680  -14.385 1.305   1.00 11.55 ? 240 LEU A CG  1 
ATOM   1916 C  CD1 . LEU A 1 239 ? -1.218  -15.734 1.760   1.00 15.76 ? 240 LEU A CD1 1 
ATOM   1917 C  CD2 . LEU A 1 239 ? -1.446  -13.716 0.130   1.00 13.96 ? 240 LEU A CD2 1 
ATOM   1918 N  N   . MET A 1 240 ? -1.348  -10.458 3.553   1.00 8.05  ? 241 MET A N   1 
ATOM   1919 C  CA  . MET A 1 240 ? -1.786  -9.638  4.723   1.00 9.69  ? 241 MET A CA  1 
ATOM   1920 C  C   . MET A 1 240 ? -2.515  -10.589 5.703   1.00 7.54  ? 241 MET A C   1 
ATOM   1921 O  O   . MET A 1 240 ? -3.703  -10.773 5.600   1.00 9.57  ? 241 MET A O   1 
ATOM   1922 C  CB  . MET A 1 240 ? -2.735  -8.501  4.308   1.00 9.73  ? 241 MET A CB  1 
ATOM   1923 C  CG  . MET A 1 240 ? -2.902  -7.449  5.519   1.00 10.29 ? 241 MET A CG  1 
ATOM   1924 S  SD  . MET A 1 240 ? -3.838  -6.039  4.997   1.00 12.41 ? 241 MET A SD  1 
ATOM   1925 C  CE  . MET A 1 240 ? -2.561  -4.980  4.303   1.00 8.55  ? 241 MET A CE  1 
ATOM   1926 N  N   . VAL A 1 241 ? -1.699  -11.127 6.625   1.00 7.99  ? 242 VAL A N   1 
ATOM   1927 C  CA  . VAL A 1 241 ? -2.280  -12.075 7.666   1.00 6.85  ? 242 VAL A CA  1 
ATOM   1928 C  C   . VAL A 1 241 ? -1.459  -11.806 8.960   1.00 8.59  ? 242 VAL A C   1 
ATOM   1929 O  O   . VAL A 1 241 ? -0.264  -11.360 8.906   1.00 8.34  ? 242 VAL A O   1 
ATOM   1930 C  CB  . VAL A 1 241 ? -2.176  -13.586 7.274   1.00 6.81  ? 242 VAL A CB  1 
ATOM   1931 C  CG1 . VAL A 1 241 ? -3.075  -13.879 5.985   1.00 7.56  ? 242 VAL A CG1 1 
ATOM   1932 C  CG2 . VAL A 1 241 ? -0.688  -13.987 7.161   1.00 7.77  ? 242 VAL A CG2 1 
ATOM   1933 N  N   . ASP A 1 242 ? -2.063  -12.182 10.103  1.00 6.14  ? 243 ASP A N   1 
ATOM   1934 C  CA  . ASP A 1 242 ? -1.400  -12.020 11.401  1.00 7.14  ? 243 ASP A CA  1 
ATOM   1935 C  C   . ASP A 1 242 ? -0.900  -10.544 11.592  1.00 7.61  ? 243 ASP A C   1 
ATOM   1936 O  O   . ASP A 1 242 ? 0.211   -10.270 12.118  1.00 8.03  ? 243 ASP A O   1 
ATOM   1937 C  CB  . ASP A 1 242 ? -0.320  -13.067 11.647  1.00 7.57  ? 243 ASP A CB  1 
ATOM   1938 C  CG  . ASP A 1 242 ? -0.885  -14.462 11.691  1.00 7.98  ? 243 ASP A CG  1 
ATOM   1939 O  OD1 . ASP A 1 242 ? -1.909  -14.608 12.320  1.00 7.48  ? 243 ASP A OD1 1 
ATOM   1940 O  OD2 . ASP A 1 242 ? -0.261  -15.397 11.076  1.00 9.72  ? 243 ASP A OD2 1 
ATOM   1941 N  N   . ASN A 1 243 ? -1.812  -9.604  11.272  1.00 6.88  ? 244 ASN A N   1 
ATOM   1942 C  CA  . ASN A 1 243 ? -1.511  -8.146  11.483  1.00 7.34  ? 244 ASN A CA  1 
ATOM   1943 C  C   . ASN A 1 243 ? -2.087  -7.719  12.862  1.00 7.54  ? 244 ASN A C   1 
ATOM   1944 O  O   . ASN A 1 243 ? -2.769  -6.675  12.937  1.00 6.93  ? 244 ASN A O   1 
ATOM   1945 C  CB  . ASN A 1 243 ? -2.054  -7.310  10.326  1.00 8.13  ? 244 ASN A CB  1 
ATOM   1946 C  CG  . ASN A 1 243 ? -3.571  -7.441  10.152  1.00 6.69  ? 244 ASN A CG  1 
ATOM   1947 O  OD1 . ASN A 1 243 ? -4.210  -8.398  10.754  1.00 7.73  ? 244 ASN A OD1 1 
ATOM   1948 N  ND2 . ASN A 1 243 ? -4.201  -6.504  9.325   1.00 11.84 ? 244 ASN A ND2 1 
ATOM   1949 N  N   . TRP A 1 244 ? -1.794  -8.530  13.918  1.00 7.53  ? 245 TRP A N   1 
ATOM   1950 C  CA  . TRP A 1 244 ? -2.334  -8.300  15.303  1.00 8.12  ? 245 TRP A CA  1 
ATOM   1951 C  C   . TRP A 1 244 ? -1.117  -8.186  16.224  1.00 8.03  ? 245 TRP A C   1 
ATOM   1952 O  O   . TRP A 1 244 ? -0.082  -8.876  16.019  1.00 7.29  ? 245 TRP A O   1 
ATOM   1953 C  CB  . TRP A 1 244 ? -3.252  -9.428  15.799  1.00 6.39  ? 245 TRP A CB  1 
ATOM   1954 C  CG  . TRP A 1 244 ? -2.736  -10.775 15.561  1.00 6.95  ? 245 TRP A CG  1 
ATOM   1955 C  CD1 . TRP A 1 244 ? -2.925  -11.561 14.408  1.00 9.33  ? 245 TRP A CD1 1 
ATOM   1956 C  CD2 . TRP A 1 244 ? -2.188  -11.638 16.552  1.00 6.86  ? 245 TRP A CD2 1 
ATOM   1957 N  NE1 . TRP A 1 244 ? -2.403  -12.835 14.638  1.00 5.86  ? 245 TRP A NE1 1 
ATOM   1958 C  CE2 . TRP A 1 244 ? -1.947  -12.892 15.936  1.00 9.00  ? 245 TRP A CE2 1 
ATOM   1959 C  CE3 . TRP A 1 244 ? -1.904  -11.488 17.916  1.00 7.36  ? 245 TRP A CE3 1 
ATOM   1960 C  CZ2 . TRP A 1 244 ? -1.366  -13.991 16.647  1.00 10.26 ? 245 TRP A CZ2 1 
ATOM   1961 C  CZ3 . TRP A 1 244 ? -1.307  -12.568 18.618  1.00 7.49  ? 245 TRP A CZ3 1 
ATOM   1962 C  CH2 . TRP A 1 244 ? -1.026  -13.781 17.973  1.00 9.52  ? 245 TRP A CH2 1 
ATOM   1963 N  N   . ARG A 1 245 ? -1.226  -7.272  17.203  1.00 6.21  ? 246 ARG A N   1 
ATOM   1964 C  CA  . ARG A 1 245 ? -0.267  -7.181  18.303  1.00 7.03  ? 246 ARG A CA  1 
ATOM   1965 C  C   . ARG A 1 245 ? -0.732  -8.135  19.441  1.00 7.05  ? 246 ARG A C   1 
ATOM   1966 O  O   . ARG A 1 245 ? -1.919  -8.154  19.753  1.00 8.97  ? 246 ARG A O   1 
ATOM   1967 C  CB  . ARG A 1 245 ? -0.226  -5.704  18.764  1.00 7.35  ? 246 ARG A CB  1 
ATOM   1968 C  CG  . ARG A 1 245 ? 0.901   -5.565  19.792  1.00 4.14  ? 246 ARG A CG  1 
ATOM   1969 C  CD  . ARG A 1 245 ? 0.849   -4.098  20.367  1.00 8.88  ? 246 ARG A CD  1 
ATOM   1970 N  NE  . ARG A 1 245 ? 2.140   -3.812  21.093  1.00 10.00 ? 246 ARG A NE  1 
ATOM   1971 C  CZ  . ARG A 1 245 ? 2.343   -2.796  21.963  1.00 10.24 ? 246 ARG A CZ  1 
ATOM   1972 N  NH1 . ARG A 1 245 ? 1.336   -1.974  22.282  1.00 8.22  ? 246 ARG A NH1 1 
ATOM   1973 N  NH2 . ARG A 1 245 ? 3.593   -2.550  22.506  1.00 9.13  ? 246 ARG A NH2 1 
ATOM   1974 N  N   . PRO A 1 246 ? 0.189   -8.900  20.064  1.00 9.19  ? 247 PRO A N   1 
ATOM   1975 C  CA  . PRO A 1 246 ? -0.191  -9.739  21.180  1.00 8.05  ? 247 PRO A CA  1 
ATOM   1976 C  C   . PRO A 1 246 ? -0.550  -8.863  22.410  1.00 7.79  ? 247 PRO A C   1 
ATOM   1977 O  O   . PRO A 1 246 ? -0.228  -7.693  22.508  1.00 7.68  ? 247 PRO A O   1 
ATOM   1978 C  CB  . PRO A 1 246 ? 1.049   -10.565 21.511  1.00 9.12  ? 247 PRO A CB  1 
ATOM   1979 C  CG  . PRO A 1 246 ? 2.060   -10.147 20.541  1.00 11.55 ? 247 PRO A CG  1 
ATOM   1980 C  CD  . PRO A 1 246 ? 1.628   -8.956  19.782  1.00 10.44 ? 247 PRO A CD  1 
ATOM   1981 N  N   . ALA A 1 247 ? -1.249  -9.521  23.322  1.00 10.22 ? 248 ALA A N   1 
ATOM   1982 C  CA  . ALA A 1 247 ? -1.573  -8.942  24.637  1.00 6.68  ? 248 ALA A CA  1 
ATOM   1983 C  C   . ALA A 1 247 ? -0.318  -8.391  25.349  1.00 8.03  ? 248 ALA A C   1 
ATOM   1984 O  O   . ALA A 1 247 ? 0.736   -9.066  25.378  1.00 8.66  ? 248 ALA A O   1 
ATOM   1985 C  CB  . ALA A 1 247 ? -2.290  -10.042 25.517  1.00 9.29  ? 248 ALA A CB  1 
ATOM   1986 N  N   . GLN A 1 248 ? -0.473  -7.196  25.938  1.00 7.70  ? 249 GLN A N   1 
ATOM   1987 C  CA  . GLN A 1 248 ? 0.573   -6.491  26.676  1.00 8.76  ? 249 GLN A CA  1 
ATOM   1988 C  C   . GLN A 1 248 ? 0.299   -6.462  28.175  1.00 9.93  ? 249 GLN A C   1 
ATOM   1989 O  O   . GLN A 1 248 ? -0.849  -6.601  28.600  1.00 9.39  ? 249 GLN A O   1 
ATOM   1990 C  CB  . GLN A 1 248 ? 0.594   -5.029  26.195  1.00 8.60  ? 249 GLN A CB  1 
ATOM   1991 C  CG  . GLN A 1 248 ? 0.905   -4.913  24.651  1.00 8.43  ? 249 GLN A CG  1 
ATOM   1992 C  CD  . GLN A 1 248 ? 2.258   -5.599  24.328  1.00 12.67 ? 249 GLN A CD  1 
ATOM   1993 O  OE1 . GLN A 1 248 ? 3.373   -5.253  24.872  1.00 11.78 ? 249 GLN A OE1 1 
ATOM   1994 N  NE2 . GLN A 1 248 ? 2.171   -6.570  23.442  1.00 10.57 ? 249 GLN A NE2 1 
ATOM   1995 N  N   . PRO A 1 249 ? 1.332   -6.215  28.988  1.00 10.12 ? 250 PRO A N   1 
ATOM   1996 C  CA  . PRO A 1 249 ? 1.139   -6.234  30.468  1.00 10.40 ? 250 PRO A CA  1 
ATOM   1997 C  C   . PRO A 1 249 ? 0.031   -5.219  30.896  1.00 9.80  ? 250 PRO A C   1 
ATOM   1998 O  O   . PRO A 1 249 ? 0.026   -4.048  30.450  1.00 9.68  ? 250 PRO A O   1 
ATOM   1999 C  CB  . PRO A 1 249 ? 2.554   -5.810  31.014  1.00 11.22 ? 250 PRO A CB  1 
ATOM   2000 C  CG  . PRO A 1 249 ? 3.498   -6.188  29.948  1.00 13.43 ? 250 PRO A CG  1 
ATOM   2001 C  CD  . PRO A 1 249 ? 2.746   -6.041  28.600  1.00 10.50 ? 250 PRO A CD  1 
ATOM   2002 N  N   . LEU A 1 250 ? -0.861  -5.711  31.772  1.00 10.29 ? 251 LEU A N   1 
ATOM   2003 C  CA  . LEU A 1 250 ? -1.945  -4.865  32.210  1.00 9.27  ? 251 LEU A CA  1 
ATOM   2004 C  C   . LEU A 1 250 ? -1.393  -3.774  33.153  1.00 9.77  ? 251 LEU A C   1 
ATOM   2005 O  O   . LEU A 1 250 ? -1.961  -2.662  33.208  1.00 8.81  ? 251 LEU A O   1 
ATOM   2006 C  CB  . LEU A 1 250 ? -3.040  -5.716  32.910  1.00 8.54  ? 251 LEU A CB  1 
ATOM   2007 C  CG  . LEU A 1 250 ? -4.299  -4.987  33.396  1.00 11.43 ? 251 LEU A CG  1 
ATOM   2008 C  CD1 . LEU A 1 250 ? -5.035  -4.324  32.232  1.00 9.54  ? 251 LEU A CD1 1 
ATOM   2009 C  CD2 . LEU A 1 250 ? -5.349  -5.895  34.215  1.00 12.02 ? 251 LEU A CD2 1 
ATOM   2010 N  N   . LYS A 1 251 ? -0.331  -4.109  33.908  1.00 11.20 ? 252 LYS A N   1 
ATOM   2011 C  CA  . LYS A 1 251 ? 0.288   -3.071  34.835  1.00 12.54 ? 252 LYS A CA  1 
ATOM   2012 C  C   . LYS A 1 251 ? -0.791  -2.558  35.830  1.00 11.29 ? 252 LYS A C   1 
ATOM   2013 O  O   . LYS A 1 251 ? -1.545  -3.385  36.367  1.00 13.81 ? 252 LYS A O   1 
ATOM   2014 C  CB  . LYS A 1 251 ? 1.042   -1.991  34.059  1.00 11.68 ? 252 LYS A CB  1 
ATOM   2015 C  CG  . LYS A 1 251 ? 2.325   -2.685  33.375  1.00 15.61 ? 252 LYS A CG  1 
ATOM   2016 C  CD  . LYS A 1 251 ? 3.168   -1.746  32.634  1.00 20.31 ? 252 LYS A CD  1 
ATOM   2017 C  CE  . LYS A 1 251 ? 4.454   -2.489  32.272  1.00 26.85 ? 252 LYS A CE  1 
ATOM   2018 N  NZ  . LYS A 1 251 ? 5.119   -1.665  31.231  1.00 25.99 ? 252 LYS A NZ  1 
ATOM   2019 N  N   . ASN A 1 252 ? -0.822  -1.284  36.067  1.00 13.01 ? 253 ASN A N   1 
ATOM   2020 C  CA  . ASN A 1 252 ? -1.571  -0.679  37.116  1.00 19.30 ? 253 ASN A CA  1 
ATOM   2021 C  C   . ASN A 1 252 ? -2.930  -0.232  36.519  1.00 18.08 ? 253 ASN A C   1 
ATOM   2022 O  O   . ASN A 1 252 ? -3.185  1.047   36.516  1.00 20.83 ? 253 ASN A O   1 
ATOM   2023 C  CB  . ASN A 1 252 ? -0.813  0.577   37.659  1.00 21.84 ? 253 ASN A CB  1 
ATOM   2024 C  CG  . ASN A 1 252 ? -1.518  1.205   38.878  1.00 27.66 ? 253 ASN A CG  1 
ATOM   2025 O  OD1 . ASN A 1 252 ? -2.100  0.495   39.725  1.00 31.37 ? 253 ASN A OD1 1 
ATOM   2026 N  ND2 . ASN A 1 252 ? -1.501  2.540   38.944  1.00 32.52 ? 253 ASN A ND2 1 
ATOM   2027 N  N   . ARG A 1 253 ? -3.694  -1.221  35.948  1.00 13.70 ? 254 ARG A N   1 
ATOM   2028 C  CA  . ARG A 1 253 ? -5.016  -0.890  35.338  1.00 11.07 ? 254 ARG A CA  1 
ATOM   2029 C  C   . ARG A 1 253 ? -6.090  -1.828  35.709  1.00 13.05 ? 254 ARG A C   1 
ATOM   2030 O  O   . ARG A 1 253 ? -5.804  -3.000  35.908  1.00 14.25 ? 254 ARG A O   1 
ATOM   2031 C  CB  . ARG A 1 253 ? -4.975  -0.851  33.785  1.00 10.17 ? 254 ARG A CB  1 
ATOM   2032 C  CG  . ARG A 1 253 ? -4.082  0.306   33.265  1.00 9.92  ? 254 ARG A CG  1 
ATOM   2033 C  CD  . ARG A 1 253 ? -4.038  0.215   31.713  1.00 8.18  ? 254 ARG A CD  1 
ATOM   2034 N  NE  . ARG A 1 253 ? -3.124  -0.895  31.291  1.00 10.01 ? 254 ARG A NE  1 
ATOM   2035 C  CZ  . ARG A 1 253 ? -2.880  -1.178  30.005  1.00 7.39  ? 254 ARG A CZ  1 
ATOM   2036 N  NH1 . ARG A 1 253 ? -3.476  -0.425  29.033  1.00 6.98  ? 254 ARG A NH1 1 
ATOM   2037 N  NH2 . ARG A 1 253 ? -2.015  -2.161  29.736  1.00 5.00  ? 254 ARG A NH2 1 
ATOM   2038 N  N   A GLN A 1 254 ? -7.325  -1.306  35.815  0.50 12.12 ? 255 GLN A N   1 
ATOM   2039 N  N   B GLN A 1 254 ? -7.334  -1.311  35.718  0.50 11.72 ? 255 GLN A N   1 
ATOM   2040 C  CA  A GLN A 1 254 ? -8.496  -2.157  36.034  0.50 13.24 ? 255 GLN A CA  1 
ATOM   2041 C  CA  B GLN A 1 254 ? -8.520  -2.084  36.085  0.50 13.50 ? 255 GLN A CA  1 
ATOM   2042 C  C   A GLN A 1 254 ? -9.306  -2.137  34.727  0.50 12.12 ? 255 GLN A C   1 
ATOM   2043 C  C   B GLN A 1 254 ? -9.454  -2.123  34.871  0.50 12.31 ? 255 GLN A C   1 
ATOM   2044 O  O   A GLN A 1 254 ? -9.432  -1.092  34.036  0.50 11.66 ? 255 GLN A O   1 
ATOM   2045 O  O   B GLN A 1 254 ? -9.851  -1.059  34.399  0.50 12.45 ? 255 GLN A O   1 
ATOM   2046 C  CB  A GLN A 1 254 ? -9.333  -1.708  37.274  0.50 13.73 ? 255 GLN A CB  1 
ATOM   2047 C  CB  B GLN A 1 254 ? -9.234  -1.383  37.263  0.50 13.91 ? 255 GLN A CB  1 
ATOM   2048 C  CG  A GLN A 1 254 ? -10.669 -2.466  37.500  0.50 13.80 ? 255 GLN A CG  1 
ATOM   2049 C  CG  B GLN A 1 254 ? -8.363  -1.277  38.533  0.50 15.35 ? 255 GLN A CG  1 
ATOM   2050 C  CD  A GLN A 1 254 ? -11.111 -2.642  38.976  0.50 17.45 ? 255 GLN A CD  1 
ATOM   2051 C  CD  B GLN A 1 254 ? -9.166  -1.125  39.813  0.50 17.38 ? 255 GLN A CD  1 
ATOM   2052 O  OE1 A GLN A 1 254 ? -10.304 -3.043  39.839  0.50 24.31 ? 255 GLN A OE1 1 
ATOM   2053 O  OE1 B GLN A 1 254 ? -10.406 -1.051  39.791  0.50 22.05 ? 255 GLN A OE1 1 
ATOM   2054 N  NE2 A GLN A 1 254 ? -12.435 -2.402  39.256  0.50 19.69 ? 255 GLN A NE2 1 
ATOM   2055 N  NE2 B GLN A 1 254 ? -8.462  -1.055  40.948  0.50 20.57 ? 255 GLN A NE2 1 
ATOM   2056 N  N   . ILE A 1 255 ? -9.772  -3.323  34.380  1.00 10.40 ? 256 ILE A N   1 
ATOM   2057 C  CA  . ILE A 1 255 ? -10.789 -3.473  33.336  1.00 10.80 ? 256 ILE A CA  1 
ATOM   2058 C  C   . ILE A 1 255 ? -12.184 -3.528  34.028  1.00 9.57  ? 256 ILE A C   1 
ATOM   2059 O  O   . ILE A 1 255 ? -12.354 -4.280  34.992  1.00 9.09  ? 256 ILE A O   1 
ATOM   2060 C  CB  . ILE A 1 255 ? -10.571 -4.761  32.505  1.00 12.26 ? 256 ILE A CB  1 
ATOM   2061 C  CG1 . ILE A 1 255 ? -9.155  -4.705  31.938  1.00 11.89 ? 256 ILE A CG1 1 
ATOM   2062 C  CG2 . ILE A 1 255 ? -11.634 -4.865  31.363  1.00 12.16 ? 256 ILE A CG2 1 
ATOM   2063 C  CD1 . ILE A 1 255 ? -8.781  -6.020  31.173  1.00 11.05 ? 256 ILE A CD1 1 
ATOM   2064 N  N   . LYS A 1 256 ? -13.063 -2.623  33.616  1.00 10.56 ? 257 LYS A N   1 
ATOM   2065 C  CA  . LYS A 1 256 ? -14.443 -2.574  34.165  1.00 8.20  ? 257 LYS A CA  1 
ATOM   2066 C  C   . LYS A 1 256 ? -15.438 -3.217  33.210  1.00 9.56  ? 257 LYS A C   1 
ATOM   2067 O  O   . LYS A 1 256 ? -15.302 -3.048  31.976  1.00 10.86 ? 257 LYS A O   1 
ATOM   2068 C  CB  . LYS A 1 256 ? -14.813 -1.080  34.370  1.00 8.67  ? 257 LYS A CB  1 
ATOM   2069 C  CG  . LYS A 1 256 ? -13.762 -0.255  35.156  1.00 16.51 ? 257 LYS A CG  1 
ATOM   2070 C  CD  . LYS A 1 256 ? -13.823 -0.389  36.609  1.00 28.23 ? 257 LYS A CD  1 
ATOM   2071 C  CE  . LYS A 1 256 ? -12.818 0.662   37.224  1.00 33.85 ? 257 LYS A CE  1 
ATOM   2072 N  NZ  . LYS A 1 256 ? -12.813 2.059   36.564  1.00 39.05 ? 257 LYS A NZ  1 
ATOM   2073 N  N   . ALA A 1 257 ? -16.475 -3.858  33.751  1.00 7.70  ? 258 ALA A N   1 
ATOM   2074 C  CA  . ALA A 1 257 ? -17.541 -4.490  32.929  1.00 9.55  ? 258 ALA A CA  1 
ATOM   2075 C  C   . ALA A 1 257 ? -18.796 -3.652  33.102  1.00 9.81  ? 258 ALA A C   1 
ATOM   2076 O  O   . ALA A 1 257 ? -19.107 -3.184  34.224  1.00 9.52  ? 258 ALA A O   1 
ATOM   2077 C  CB  . ALA A 1 257 ? -17.814 -5.927  33.292  1.00 10.85 ? 258 ALA A CB  1 
ATOM   2078 N  N   . SER A 1 258 ? -19.517 -3.465  32.004  1.00 7.67  ? 259 SER A N   1 
ATOM   2079 C  CA  . SER A 1 258 ? -20.766 -2.723  32.034  1.00 10.36 ? 259 SER A CA  1 
ATOM   2080 C  C   . SER A 1 258 ? -21.920 -3.594  32.459  1.00 11.88 ? 259 SER A C   1 
ATOM   2081 O  O   . SER A 1 258 ? -23.028 -3.113  32.592  1.00 14.39 ? 259 SER A O   1 
ATOM   2082 C  CB  . SER A 1 258 ? -21.081 -2.155  30.666  1.00 12.16 ? 259 SER A CB  1 
ATOM   2083 O  OG  . SER A 1 258 ? -21.491 -3.180  29.805  1.00 10.79 ? 259 SER A OG  1 
ATOM   2084 N  N   . PHE A 1 259 ? -21.647 -4.874  32.652  1.00 13.64 ? 260 PHE A N   1 
ATOM   2085 C  CA  . PHE A 1 259 ? -22.690 -5.875  32.841  1.00 15.74 ? 260 PHE A CA  1 
ATOM   2086 C  C   . PHE A 1 259 ? -22.371 -6.792  34.018  1.00 20.42 ? 260 PHE A C   1 
ATOM   2087 O  O   . PHE A 1 259 ? -21.216 -7.049  34.331  1.00 18.47 ? 260 PHE A O   1 
ATOM   2088 C  CB  . PHE A 1 259 ? -22.843 -6.730  31.589  1.00 14.80 ? 260 PHE A CB  1 
ATOM   2089 C  CG  . PHE A 1 259 ? -21.587 -7.423  31.200  1.00 15.66 ? 260 PHE A CG  1 
ATOM   2090 C  CD1 . PHE A 1 259 ? -20.650 -6.774  30.431  1.00 12.84 ? 260 PHE A CD1 1 
ATOM   2091 C  CD2 . PHE A 1 259 ? -21.312 -8.702  31.641  1.00 14.61 ? 260 PHE A CD2 1 
ATOM   2092 C  CE1 . PHE A 1 259 ? -19.493 -7.387  30.079  1.00 13.89 ? 260 PHE A CE1 1 
ATOM   2093 C  CE2 . PHE A 1 259 ? -20.139 -9.312  31.286  1.00 18.54 ? 260 PHE A CE2 1 
ATOM   2094 C  CZ  . PHE A 1 259 ? -19.232 -8.645  30.507  1.00 14.61 ? 260 PHE A CZ  1 
ATOM   2095 N  N   . LYS A 1 260 ? -23.448 -7.288  34.615  1.00 26.49 ? 261 LYS A N   1 
ATOM   2096 C  CA  . LYS A 1 260 ? -23.477 -8.465  35.480  1.00 32.85 ? 261 LYS A CA  1 
ATOM   2097 C  C   . LYS A 1 260 ? -22.761 -8.324  36.809  1.00 35.77 ? 261 LYS A C   1 
ATOM   2098 O  O   . LYS A 1 260 ? -22.764 -9.251  37.597  1.00 38.24 ? 261 LYS A O   1 
ATOM   2099 C  CB  . LYS A 1 260 ? -23.074 -9.746  34.758  1.00 32.16 ? 261 LYS A CB  1 
ATOM   2100 C  CG  . LYS A 1 260 ? -24.130 -10.246 33.801  1.00 33.83 ? 261 LYS A CG  1 
ATOM   2101 C  CD  . LYS A 1 260 ? -23.801 -11.613 33.265  1.00 34.78 ? 261 LYS A CD  1 
ATOM   2102 C  CE  . LYS A 1 260 ? -22.413 -11.636 32.695  1.00 38.31 ? 261 LYS A CE  1 
ATOM   2103 N  NZ  . LYS A 1 260 ? -22.067 -12.976 32.172  1.00 41.43 ? 261 LYS A NZ  1 
ATOM   2104 O  OXT . LYS A 1 260 ? -22.060 -7.308  37.084  1.00 38.74 ? 261 LYS A OXT 1 
HETATM 2105 ZN ZN  . ZN  B 2 .   ? -6.777  -1.617  15.264  1.00 9.30  ? 262 ZN  A ZN  1 
HETATM 2106 N  N1  . J90 C 3 .   ? -0.405  9.072   14.654  1.00 22.29 ? 263 J90 A N1  1 
HETATM 2107 C  C2  . J90 C 3 .   ? -1.548  8.802   15.237  1.00 18.47 ? 263 J90 A C2  1 
HETATM 2108 N  N3  . J90 C 3 .   ? -2.308  7.805   14.825  1.00 18.20 ? 263 J90 A N3  1 
HETATM 2109 C  C4  . J90 C 3 .   ? -2.029  7.004   13.783  1.00 19.67 ? 263 J90 A C4  1 
HETATM 2110 C  C5  . J90 C 3 .   ? -0.809  7.200   13.129  1.00 21.89 ? 263 J90 A C5  1 
HETATM 2111 C  C6  . J90 C 3 .   ? -0.031  8.268   13.622  1.00 23.25 ? 263 J90 A C6  1 
HETATM 2112 N  N7  . J90 C 3 .   ? -2.890  5.936   13.448  1.00 19.63 ? 263 J90 A N7  1 
HETATM 2113 C  C8  . J90 C 3 .   ? -4.679  4.685   14.556  1.00 8.80  ? 263 J90 A C8  1 
HETATM 2114 C  C9  . J90 C 3 .   ? -3.705  3.668   14.877  1.00 8.39  ? 263 J90 A C9  1 
HETATM 2115 C  C10 . J90 C 3 .   ? -4.117  2.495   15.606  1.00 4.95  ? 263 J90 A C10 1 
HETATM 2116 C  C11 . J90 C 3 .   ? -5.461  2.375   15.928  1.00 5.54  ? 263 J90 A C11 1 
HETATM 2117 C  C12 . J90 C 3 .   ? -6.374  3.359   15.577  1.00 6.20  ? 263 J90 A C12 1 
HETATM 2118 C  C13 . J90 C 3 .   ? -6.012  4.549   14.880  1.00 7.50  ? 263 J90 A C13 1 
HETATM 2119 S  S14 . J90 C 3 .   ? -6.073  0.908   16.770  1.00 5.81  ? 263 J90 A S14 1 
HETATM 2120 O  O15 . J90 C 3 .   ? -5.491  0.983   18.141  1.00 5.74  ? 263 J90 A O15 1 
HETATM 2121 O  O16 . J90 C 3 .   ? -7.560  0.925   16.601  1.00 6.31  ? 263 J90 A O16 1 
HETATM 2122 N  N17 . J90 C 3 .   ? -5.293  -0.371  16.035  1.00 9.09  ? 263 J90 A N17 1 
HETATM 2123 N  N18 . J90 C 3 .   ? -0.340  6.341   11.953  1.00 28.01 ? 263 J90 A N18 1 
HETATM 2124 O  O19 . J90 C 3 .   ? 0.746   6.701   11.608  1.00 35.02 ? 263 J90 A O19 1 
HETATM 2125 O  O20 . J90 C 3 .   ? -1.160  5.549   11.686  1.00 28.87 ? 263 J90 A O20 1 
HETATM 2126 O  O21 . J90 C 3 .   ? 1.157   8.545   12.978  1.00 25.02 ? 263 J90 A O21 1 
HETATM 2127 C  C22 . J90 C 3 .   ? -4.267  5.929   13.768  1.00 14.40 ? 263 J90 A C22 1 
HETATM 2128 N  N1  . J90 D 3 .   ? 15.046  -7.262  7.513   1.00 52.25 ? 264 J90 A N1  1 
HETATM 2129 C  C2  . J90 D 3 .   ? 15.785  -6.495  8.295   1.00 55.17 ? 264 J90 A C2  1 
HETATM 2130 N  N3  . J90 D 3 .   ? 15.278  -5.431  8.884   1.00 53.99 ? 264 J90 A N3  1 
HETATM 2131 C  C4  . J90 D 3 .   ? 14.003  -5.084  8.690   1.00 52.96 ? 264 J90 A C4  1 
HETATM 2132 C  C5  . J90 D 3 .   ? 13.150  -5.853  7.859   1.00 53.79 ? 264 J90 A C5  1 
HETATM 2133 C  C6  . J90 D 3 .   ? 13.767  -7.002  7.269   1.00 54.50 ? 264 J90 A C6  1 
HETATM 2134 N  N7  . J90 D 3 .   ? 13.551  -3.932  9.336   1.00 48.84 ? 264 J90 A N7  1 
HETATM 2135 C  C8  . J90 D 3 .   ? 13.411  -2.460  11.102  1.00 33.47 ? 264 J90 A C8  1 
HETATM 2136 C  C9  . J90 D 3 .   ? 12.899  -3.267  12.146  1.00 35.03 ? 264 J90 A C9  1 
HETATM 2137 C  C10 . J90 D 3 .   ? 12.004  -2.754  13.062  1.00 33.59 ? 264 J90 A C10 1 
HETATM 2138 C  C11 . J90 D 3 .   ? 11.645  -1.409  12.901  1.00 30.40 ? 264 J90 A C11 1 
HETATM 2139 C  C12 . J90 D 3 .   ? 12.132  -0.576  11.854  1.00 32.21 ? 264 J90 A C12 1 
HETATM 2140 C  C13 . J90 D 3 .   ? 13.022  -1.117  10.911  1.00 34.71 ? 264 J90 A C13 1 
HETATM 2141 S  S14 . J90 D 3 .   ? 10.495  -0.762  14.127  1.00 27.84 ? 264 J90 A S14 1 
HETATM 2142 O  O15 . J90 D 3 .   ? 9.989   0.564   13.581  1.00 24.21 ? 264 J90 A O15 1 
HETATM 2143 O  O16 . J90 D 3 .   ? 9.552   -1.950  14.278  1.00 25.95 ? 264 J90 A O16 1 
HETATM 2144 N  N17 . J90 D 3 .   ? 11.329  -0.545  15.703  1.00 19.04 ? 264 J90 A N17 1 
HETATM 2145 N  N18 . J90 D 3 .   ? 11.702  -5.473  7.651   1.00 56.23 ? 264 J90 A N18 1 
HETATM 2146 O  O19 . J90 D 3 .   ? 11.506  -4.278  7.649   1.00 54.49 ? 264 J90 A O19 1 
HETATM 2147 O  O20 . J90 D 3 .   ? 11.158  -6.508  7.564   1.00 56.94 ? 264 J90 A O20 1 
HETATM 2148 O  O21 . J90 D 3 .   ? 13.143  -7.946  6.416   1.00 54.44 ? 264 J90 A O21 1 
HETATM 2149 C  C22 . J90 D 3 .   ? 14.347  -3.131  10.152  1.00 36.89 ? 264 J90 A C22 1 
HETATM 2150 S  S   . DMS E 4 .   ? 1.291   -11.567 14.917  1.00 33.84 ? 265 DMS A S   1 
HETATM 2151 O  O   . DMS E 4 .   ? 2.397   -10.939 13.589  1.00 31.07 ? 265 DMS A O   1 
HETATM 2152 C  C1  . DMS E 4 .   ? 1.726   -13.358 14.983  1.00 33.18 ? 265 DMS A C1  1 
HETATM 2153 C  C2  . DMS E 4 .   ? 1.621   -11.232 16.649  1.00 24.95 ? 265 DMS A C2  1 
HETATM 2154 S  S   . DMS F 4 .   ? -6.362  7.213   10.823  1.00 43.01 ? 266 DMS A S   1 
HETATM 2155 O  O   . DMS F 4 .   ? -4.770  7.997   11.213  1.00 43.24 ? 266 DMS A O   1 
HETATM 2156 C  C1  . DMS F 4 .   ? -7.264  6.811   12.330  1.00 41.34 ? 266 DMS A C1  1 
HETATM 2157 C  C2  . DMS F 4 .   ? -7.076  8.823   10.346  1.00 42.75 ? 266 DMS A C2  1 
HETATM 2158 O  O   . HOH G 5 .   ? -12.536 12.503  29.237  1.00 19.03 ? 126 HOH A O   1 
HETATM 2159 O  O   . HOH G 5 .   ? -26.658 -10.679 12.433  1.00 41.44 ? 267 HOH A O   1 
HETATM 2160 O  O   . HOH G 5 .   ? -28.148 6.239   21.597  1.00 28.93 ? 268 HOH A O   1 
HETATM 2161 O  O   . HOH G 5 .   ? -21.797 -13.912 22.896  1.00 25.71 ? 269 HOH A O   1 
HETATM 2162 O  O   . HOH G 5 .   ? -24.366 -14.327 19.656  1.00 31.00 ? 270 HOH A O   1 
HETATM 2163 O  O   . HOH G 5 .   ? 1.296   10.978  15.504  1.00 30.49 ? 271 HOH A O   1 
HETATM 2164 O  O   . HOH G 5 .   ? 3.706   -13.032 21.692  1.00 42.29 ? 272 HOH A O   1 
HETATM 2165 O  O   . HOH G 5 .   ? 5.578   -9.768  21.095  1.00 25.40 ? 273 HOH A O   1 
HETATM 2166 O  O   . HOH G 5 .   ? -28.092 -1.393  28.241  1.00 26.22 ? 274 HOH A O   1 
HETATM 2167 O  O   . HOH G 5 .   ? -20.141 -0.736  -2.193  1.00 43.12 ? 275 HOH A O   1 
HETATM 2168 O  O   . HOH G 5 .   ? -12.323 -23.455 6.997   1.00 32.39 ? 276 HOH A O   1 
HETATM 2169 O  O   . HOH G 5 .   ? -5.078  -20.910 21.509  1.00 19.38 ? 277 HOH A O   1 
HETATM 2170 O  O   . HOH G 5 .   ? -8.194  11.727  7.599   1.00 34.02 ? 278 HOH A O   1 
HETATM 2171 O  O   . HOH G 5 .   ? 6.240   -5.378  27.359  1.00 31.80 ? 279 HOH A O   1 
HETATM 2172 O  O   . HOH G 5 .   ? 13.517  -0.125  6.308   1.00 31.74 ? 280 HOH A O   1 
HETATM 2173 O  O   . HOH G 5 .   ? -1.315  -4.130  15.733  1.00 7.60  ? 281 HOH A O   1 
HETATM 2174 O  O   . HOH G 5 .   ? -8.053  -15.431 11.313  1.00 6.69  ? 282 HOH A O   1 
HETATM 2175 O  O   . HOH G 5 .   ? -4.681  -13.461 18.079  1.00 7.14  ? 283 HOH A O   1 
HETATM 2176 O  O   . HOH G 5 .   ? -21.930 5.615   4.788   1.00 10.06 ? 284 HOH A O   1 
HETATM 2177 O  O   . HOH G 5 .   ? -21.755 -7.185  23.695  1.00 10.10 ? 285 HOH A O   1 
HETATM 2178 O  O   . HOH G 5 .   ? -17.153 -8.352  20.405  1.00 9.16  ? 286 HOH A O   1 
HETATM 2179 O  O   . HOH G 5 .   ? -10.826 8.715   25.498  1.00 9.56  ? 287 HOH A O   1 
HETATM 2180 O  O   . HOH G 5 .   ? 3.448   5.118   29.843  1.00 13.77 ? 288 HOH A O   1 
HETATM 2181 O  O   . HOH G 5 .   ? 4.791   -4.908  20.980  1.00 10.86 ? 289 HOH A O   1 
HETATM 2182 O  O   . HOH G 5 .   ? -2.155  -12.315 22.811  1.00 9.64  ? 290 HOH A O   1 
HETATM 2183 O  O   . HOH G 5 .   ? 1.115   -1.392  29.431  1.00 11.32 ? 291 HOH A O   1 
HETATM 2184 O  O   . HOH G 5 .   ? -3.647  -11.005 20.951  1.00 10.26 ? 292 HOH A O   1 
HETATM 2185 O  O   . HOH G 5 .   ? -24.318 8.675   20.168  1.00 18.37 ? 293 HOH A O   1 
HETATM 2186 O  O   . HOH G 5 .   ? -8.799  -3.880  7.866   1.00 9.55  ? 294 HOH A O   1 
HETATM 2187 O  O   . HOH G 5 .   ? -10.473 -18.205 17.106  1.00 12.68 ? 295 HOH A O   1 
HETATM 2188 O  O   . HOH G 5 .   ? 8.451   -3.916  21.014  1.00 14.43 ? 296 HOH A O   1 
HETATM 2189 O  O   . HOH G 5 .   ? -14.059 10.363  27.947  1.00 15.73 ? 297 HOH A O   1 
HETATM 2190 O  O   . HOH G 5 .   ? 5.213   7.141   20.236  1.00 10.85 ? 298 HOH A O   1 
HETATM 2191 O  O   . HOH G 5 .   ? -23.879 -0.923  3.983   1.00 14.15 ? 299 HOH A O   1 
HETATM 2192 O  O   . HOH G 5 .   ? -9.814  -7.977  34.038  1.00 16.43 ? 300 HOH A O   1 
HETATM 2193 O  O   . HOH G 5 .   ? -21.240 7.789   1.831   1.00 12.62 ? 301 HOH A O   1 
HETATM 2194 O  O   . HOH G 5 .   ? -17.862 -21.139 17.483  1.00 19.34 ? 302 HOH A O   1 
HETATM 2195 O  O   . HOH G 5 .   ? 7.478   6.042   21.643  1.00 11.19 ? 303 HOH A O   1 
HETATM 2196 O  O   . HOH G 5 .   ? 1.137   8.827   24.369  1.00 13.91 ? 304 HOH A O   1 
HETATM 2197 O  O   . HOH G 5 .   ? -2.640  -3.509  11.380  1.00 14.00 ? 305 HOH A O   1 
HETATM 2198 O  O   . HOH G 5 .   ? -18.101 10.588  11.255  1.00 16.42 ? 306 HOH A O   1 
HETATM 2199 O  O   . HOH G 5 .   ? -3.904  -15.901 24.339  1.00 10.86 ? 307 HOH A O   1 
HETATM 2200 O  O   . HOH G 5 .   ? -18.189 -20.410 8.030   1.00 14.03 ? 308 HOH A O   1 
HETATM 2201 O  O   . HOH G 5 .   ? -5.056  0.705   9.736   1.00 14.77 ? 309 HOH A O   1 
HETATM 2202 O  O   . HOH G 5 .   ? -3.538  -13.179 25.140  1.00 8.46  ? 310 HOH A O   1 
HETATM 2203 O  O   . HOH G 5 .   ? -14.353 -16.640 29.116  1.00 15.87 ? 311 HOH A O   1 
HETATM 2204 O  O   . HOH G 5 .   ? -6.216  -4.672  -6.372  1.00 20.29 ? 312 HOH A O   1 
HETATM 2205 O  O   . HOH G 5 .   ? -15.078 -21.082 17.689  1.00 13.94 ? 313 HOH A O   1 
HETATM 2206 O  O   . HOH G 5 .   ? -23.044 -11.689 14.188  1.00 18.32 ? 314 HOH A O   1 
HETATM 2207 O  O   . HOH G 5 .   ? -24.055 -0.887  26.542  1.00 14.40 ? 315 HOH A O   1 
HETATM 2208 O  O   . HOH G 5 .   ? -19.910 -16.942 3.001   1.00 16.49 ? 316 HOH A O   1 
HETATM 2209 O  O   . HOH G 5 .   ? -2.657  -8.698  29.187  1.00 10.10 ? 317 HOH A O   1 
HETATM 2210 O  O   . HOH G 5 .   ? -7.018  5.807   6.399   1.00 16.36 ? 318 HOH A O   1 
HETATM 2211 O  O   . HOH G 5 .   ? -13.071 -16.836 26.593  1.00 10.05 ? 319 HOH A O   1 
HETATM 2212 O  O   . HOH G 5 .   ? -26.872 -2.585  14.510  1.00 15.24 ? 320 HOH A O   1 
HETATM 2213 O  O   . HOH G 5 .   ? -26.320 3.536   15.382  1.00 17.22 ? 321 HOH A O   1 
HETATM 2214 O  O   . HOH G 5 .   ? -8.389  -19.386 21.766  1.00 13.64 ? 322 HOH A O   1 
HETATM 2215 O  O   . HOH G 5 .   ? -1.355  9.347   28.075  1.00 20.28 ? 323 HOH A O   1 
HETATM 2216 O  O   . HOH G 5 .   ? -13.604 -18.498 14.645  1.00 15.09 ? 324 HOH A O   1 
HETATM 2217 O  O   . HOH G 5 .   ? -14.821 -18.545 18.774  1.00 14.13 ? 325 HOH A O   1 
HETATM 2218 O  O   . HOH G 5 .   ? -16.314 -9.946  33.050  1.00 15.29 ? 326 HOH A O   1 
HETATM 2219 O  O   . HOH G 5 .   ? -12.185 2.895   30.812  1.00 17.78 ? 327 HOH A O   1 
HETATM 2220 O  O   . HOH G 5 .   ? -12.943 -17.173 16.944  1.00 13.78 ? 328 HOH A O   1 
HETATM 2221 O  O   . HOH G 5 .   ? -16.266 -12.199 24.414  1.00 12.80 ? 329 HOH A O   1 
HETATM 2222 O  O   . HOH G 5 .   ? -11.215 -19.403 7.150   1.00 21.60 ? 330 HOH A O   1 
HETATM 2223 O  O   . HOH G 5 .   ? -6.955  -20.223 19.519  1.00 12.43 ? 331 HOH A O   1 
HETATM 2224 O  O   . HOH G 5 .   ? -19.457 9.986   8.797   1.00 13.62 ? 332 HOH A O   1 
HETATM 2225 O  O   . HOH G 5 .   ? -29.262 -5.824  24.492  1.00 21.57 ? 333 HOH A O   1 
HETATM 2226 O  O   . HOH G 5 .   ? 4.262   -6.503  7.860   1.00 14.29 ? 334 HOH A O   1 
HETATM 2227 O  O   . HOH G 5 .   ? 0.097   -1.002  -4.740  1.00 13.67 ? 335 HOH A O   1 
HETATM 2228 O  O   . HOH G 5 .   ? -31.007 -7.089  22.392  1.00 19.29 ? 336 HOH A O   1 
HETATM 2229 O  O   . HOH G 5 .   ? -2.125  -17.449 25.660  1.00 19.52 ? 337 HOH A O   1 
HETATM 2230 O  O   . HOH G 5 .   ? 4.387   -2.664  29.088  1.00 19.70 ? 338 HOH A O   1 
HETATM 2231 O  O   . HOH G 5 .   ? 2.616   -4.387  7.722   1.00 17.24 ? 339 HOH A O   1 
HETATM 2232 O  O   . HOH G 5 .   ? -22.884 -5.760  2.707   1.00 16.29 ? 340 HOH A O   1 
HETATM 2233 O  O   . HOH G 5 .   ? -10.734 -19.485 19.954  1.00 14.69 ? 341 HOH A O   1 
HETATM 2234 O  O   . HOH G 5 .   ? -1.298  -11.113 29.122  1.00 12.74 ? 342 HOH A O   1 
HETATM 2235 O  O   . HOH G 5 .   ? -13.174 -22.145 8.595   1.00 17.54 ? 343 HOH A O   1 
HETATM 2236 O  O   . HOH G 5 .   ? 2.907   1.145   -1.964  1.00 27.71 ? 344 HOH A O   1 
HETATM 2237 O  O   . HOH G 5 .   ? -20.545 10.808  26.704  1.00 15.68 ? 345 HOH A O   1 
HETATM 2238 O  O   . HOH G 5 .   ? -15.541 -21.839 13.003  1.00 16.53 ? 346 HOH A O   1 
HETATM 2239 O  O   . HOH G 5 .   ? -24.926 -7.962  8.973   1.00 20.32 ? 347 HOH A O   1 
HETATM 2240 O  O   . HOH G 5 .   ? -14.240 14.415  27.174  1.00 19.81 ? 348 HOH A O   1 
HETATM 2241 O  O   . HOH G 5 .   ? 2.554   -11.346 9.382   1.00 17.72 ? 349 HOH A O   1 
HETATM 2242 O  O   . HOH G 5 .   ? -13.031 -19.548 26.068  1.00 17.47 ? 350 HOH A O   1 
HETATM 2243 O  O   . HOH G 5 .   ? -1.560  -13.032 27.159  1.00 18.09 ? 351 HOH A O   1 
HETATM 2244 O  O   . HOH G 5 .   ? -9.300  -10.044 -1.165  1.00 18.52 ? 352 HOH A O   1 
HETATM 2245 O  O   . HOH G 5 .   ? -7.405  -17.020 1.631   1.00 16.78 ? 353 HOH A O   1 
HETATM 2246 O  O   . HOH G 5 .   ? 5.019   -7.248  22.343  1.00 21.27 ? 354 HOH A O   1 
HETATM 2247 O  O   . HOH G 5 .   ? -23.230 -3.098  6.719   1.00 15.82 ? 355 HOH A O   1 
HETATM 2248 O  O   . HOH G 5 .   ? -18.467 -3.677  -2.562  1.00 21.11 ? 356 HOH A O   1 
HETATM 2249 O  O   . HOH G 5 .   ? -4.968  -11.882 32.114  1.00 18.11 ? 357 HOH A O   1 
HETATM 2250 O  O   . HOH G 5 .   ? 1.624   12.411  22.558  1.00 20.75 ? 358 HOH A O   1 
HETATM 2251 O  O   . HOH G 5 .   ? -8.799  -19.857 26.628  1.00 18.75 ? 359 HOH A O   1 
HETATM 2252 O  O   . HOH G 5 .   ? -5.454  2.192   12.076  1.00 11.37 ? 360 HOH A O   1 
HETATM 2253 O  O   . HOH G 5 .   ? -6.910  5.396   35.505  1.00 27.21 ? 361 HOH A O   1 
HETATM 2254 O  O   . HOH G 5 .   ? -7.448  -8.593  32.664  1.00 14.31 ? 362 HOH A O   1 
HETATM 2255 O  O   . HOH G 5 .   ? -27.054 -3.997  24.867  1.00 19.57 ? 363 HOH A O   1 
HETATM 2256 O  O   . HOH G 5 .   ? -9.216  -5.800  35.985  1.00 14.57 ? 364 HOH A O   1 
HETATM 2257 O  O   . HOH G 5 .   ? 8.439   -4.536  23.612  1.00 19.23 ? 365 HOH A O   1 
HETATM 2258 O  O   . HOH G 5 .   ? -17.074 -18.024 20.184  1.00 18.25 ? 366 HOH A O   1 
HETATM 2259 O  O   . HOH G 5 .   ? -1.716  11.466  25.921  1.00 23.44 ? 367 HOH A O   1 
HETATM 2260 O  O   . HOH G 5 .   ? -12.936 7.892   28.912  1.00 20.74 ? 368 HOH A O   1 
HETATM 2261 O  O   . HOH G 5 .   ? -11.211 1.112   33.545  1.00 18.88 ? 369 HOH A O   1 
HETATM 2262 O  O   . HOH G 5 .   ? -13.795 -21.249 15.111  1.00 15.85 ? 370 HOH A O   1 
HETATM 2263 O  O   . HOH G 5 .   ? -9.381  5.969   29.235  1.00 20.09 ? 371 HOH A O   1 
HETATM 2264 O  O   . HOH G 5 .   ? -22.329 -18.251 13.652  1.00 18.89 ? 372 HOH A O   1 
HETATM 2265 O  O   . HOH G 5 .   ? -0.317  -19.953 6.777   1.00 17.74 ? 373 HOH A O   1 
HETATM 2266 O  O   . HOH G 5 .   ? 2.352   -13.272 5.364   1.00 22.03 ? 374 HOH A O   1 
HETATM 2267 O  O   . HOH G 5 .   ? -8.202  7.303   8.342   1.00 24.97 ? 375 HOH A O   1 
HETATM 2268 O  O   . HOH G 5 .   ? -0.717  10.906  23.327  1.00 16.36 ? 376 HOH A O   1 
HETATM 2269 O  O   . HOH G 5 .   ? -12.680 3.411   -6.923  1.00 21.69 ? 377 HOH A O   1 
HETATM 2270 O  O   . HOH G 5 .   ? -24.950 4.610   8.175   1.00 24.25 ? 378 HOH A O   1 
HETATM 2271 O  O   . HOH G 5 .   ? -16.503 -16.358 -3.952  1.00 25.66 ? 379 HOH A O   1 
HETATM 2272 O  O   . HOH G 5 .   ? -21.427 -19.740 6.595   1.00 28.23 ? 380 HOH A O   1 
HETATM 2273 O  O   . HOH G 5 .   ? -19.267 -20.768 5.245   1.00 22.45 ? 381 HOH A O   1 
HETATM 2274 O  O   . HOH G 5 .   ? 8.179   3.299   27.733  1.00 31.83 ? 382 HOH A O   1 
HETATM 2275 O  O   . HOH G 5 .   ? -0.393  -14.159 22.242  1.00 19.11 ? 383 HOH A O   1 
HETATM 2276 O  O   . HOH G 5 .   ? -10.320 1.576   39.125  1.00 24.01 ? 384 HOH A O   1 
HETATM 2277 O  O   . HOH G 5 .   ? -16.951 -13.887 26.317  1.00 15.99 ? 385 HOH A O   1 
HETATM 2278 O  O   . HOH G 5 .   ? 4.011   -3.369  26.589  1.00 17.77 ? 386 HOH A O   1 
HETATM 2279 O  O   . HOH G 5 .   ? -16.421 15.767  23.651  1.00 19.97 ? 387 HOH A O   1 
HETATM 2280 O  O   . HOH G 5 .   ? -11.588 10.656  0.529   1.00 20.64 ? 388 HOH A O   1 
HETATM 2281 O  O   . HOH G 5 .   ? -6.353  -19.716 23.883  1.00 20.85 ? 389 HOH A O   1 
HETATM 2282 O  O   . HOH G 5 .   ? -0.709  -8.535  32.586  1.00 22.07 ? 390 HOH A O   1 
HETATM 2283 O  O   . HOH G 5 .   ? 7.641   -7.770  -0.625  1.00 26.79 ? 391 HOH A O   1 
HETATM 2284 O  O   . HOH G 5 .   ? -17.894 6.222   38.373  1.00 25.12 ? 392 HOH A O   1 
HETATM 2285 O  O   . HOH G 5 .   ? -3.704  -12.961 -2.684  1.00 17.77 ? 393 HOH A O   1 
HETATM 2286 O  O   . HOH G 5 .   ? -1.433  -17.315 4.945   1.00 28.07 ? 394 HOH A O   1 
HETATM 2287 O  O   . HOH G 5 .   ? -18.736 3.461   -3.472  1.00 26.00 ? 395 HOH A O   1 
HETATM 2288 O  O   . HOH G 5 .   ? -12.154 10.701  5.675   1.00 22.61 ? 396 HOH A O   1 
HETATM 2289 O  O   . HOH G 5 .   ? -9.385  3.220   34.911  1.00 17.74 ? 397 HOH A O   1 
HETATM 2290 O  O   . HOH G 5 .   ? 3.596   9.804   23.688  1.00 22.06 ? 398 HOH A O   1 
HETATM 2291 O  O   . HOH G 5 .   ? 5.297   -10.273 13.235  1.00 28.31 ? 399 HOH A O   1 
HETATM 2292 O  O   . HOH G 5 .   ? -4.023  0.237   13.484  1.00 11.00 ? 400 HOH A O   1 
HETATM 2293 O  O   . HOH G 5 .   ? 11.122  1.282   25.749  1.00 20.97 ? 401 HOH A O   1 
HETATM 2294 O  O   . HOH G 5 .   ? -10.349 14.944  12.256  1.00 18.14 ? 402 HOH A O   1 
HETATM 2295 O  O   . HOH G 5 .   ? -17.394 -16.254 22.195  1.00 21.29 ? 403 HOH A O   1 
HETATM 2296 O  O   . HOH G 5 .   ? -2.033  -4.441  -6.945  1.00 24.12 ? 404 HOH A O   1 
HETATM 2297 O  O   . HOH G 5 .   ? -12.052 9.203   2.751   1.00 22.15 ? 405 HOH A O   1 
HETATM 2298 O  O   . HOH G 5 .   ? -28.866 0.132   24.459  1.00 18.85 ? 406 HOH A O   1 
HETATM 2299 O  O   . HOH G 5 .   ? -2.260  -11.882 31.582  1.00 25.22 ? 407 HOH A O   1 
HETATM 2300 O  O   . HOH G 5 .   ? -17.167 18.462  22.367  1.00 37.30 ? 408 HOH A O   1 
HETATM 2301 O  O   . HOH G 5 .   ? -23.343 -0.557  34.575  1.00 20.19 ? 409 HOH A O   1 
HETATM 2302 O  O   . HOH G 5 .   ? -6.918  -14.911 31.615  1.00 19.58 ? 410 HOH A O   1 
HETATM 2303 O  O   . HOH G 5 .   ? -24.266 -6.946  0.456   1.00 23.93 ? 411 HOH A O   1 
HETATM 2304 O  O   . HOH G 5 .   ? -5.232  2.304   37.270  1.00 30.80 ? 412 HOH A O   1 
HETATM 2305 O  O   . HOH G 5 .   ? -0.633  3.137   12.848  1.00 19.22 ? 413 HOH A O   1 
HETATM 2306 O  O   . HOH G 5 .   ? 2.817   -13.515 8.283   1.00 24.70 ? 414 HOH A O   1 
HETATM 2307 O  O   . HOH G 5 .   ? -15.834 8.811   -2.230  1.00 22.85 ? 415 HOH A O   1 
HETATM 2308 O  O   . HOH G 5 .   ? 9.207   -9.921  13.708  1.00 21.43 ? 416 HOH A O   1 
HETATM 2309 O  O   . HOH G 5 .   ? -8.725  -15.304 36.749  1.00 24.82 ? 417 HOH A O   1 
HETATM 2310 O  O   . HOH G 5 .   ? -24.646 11.967  6.255   1.00 23.66 ? 418 HOH A O   1 
HETATM 2311 O  O   . HOH G 5 .   ? -6.269  -11.547 36.552  1.00 21.82 ? 419 HOH A O   1 
HETATM 2312 O  O   . HOH G 5 .   ? -7.227  1.584   35.241  1.00 20.01 ? 420 HOH A O   1 
HETATM 2313 O  O   . HOH G 5 .   ? -23.466 -13.096 11.218  1.00 17.41 ? 421 HOH A O   1 
HETATM 2314 O  O   . HOH G 5 .   ? -11.284 15.352  32.182  1.00 14.58 ? 422 HOH A O   1 
HETATM 2315 O  O   . HOH G 5 .   ? -28.240 5.739   18.981  1.00 24.59 ? 423 HOH A O   1 
HETATM 2316 O  O   . HOH G 5 .   ? -7.378  -15.570 38.742  1.00 19.28 ? 424 HOH A O   1 
HETATM 2317 O  O   . HOH G 5 .   ? -10.666 -20.441 24.835  1.00 19.33 ? 425 HOH A O   1 
HETATM 2318 O  O   . HOH G 5 .   ? -2.404  -9.094  34.788  1.00 26.12 ? 426 HOH A O   1 
HETATM 2319 O  O   . HOH G 5 .   ? -12.889 -9.063  -3.085  1.00 26.02 ? 427 HOH A O   1 
HETATM 2320 O  O   . HOH G 5 .   ? -4.473  -8.455  31.178  1.00 17.00 ? 428 HOH A O   1 
HETATM 2321 O  O   . HOH G 5 .   ? 3.867   -11.725 23.600  1.00 31.94 ? 429 HOH A O   1 
HETATM 2322 O  O   . HOH G 5 .   ? 6.222   5.443   28.802  1.00 23.76 ? 430 HOH A O   1 
HETATM 2323 O  O   . HOH G 5 .   ? -23.377 -10.877 17.118  1.00 22.01 ? 431 HOH A O   1 
HETATM 2324 O  O   . HOH G 5 .   ? -8.613  0.649   -6.586  1.00 19.99 ? 432 HOH A O   1 
HETATM 2325 O  O   . HOH G 5 .   ? -17.824 5.972   34.602  1.00 29.99 ? 433 HOH A O   1 
HETATM 2326 O  O   . HOH G 5 .   ? -24.910 -9.565  1.895   1.00 26.19 ? 434 HOH A O   1 
HETATM 2327 O  O   . HOH G 5 .   ? -7.417  -8.692  -2.361  1.00 23.80 ? 435 HOH A O   1 
HETATM 2328 O  O   . HOH G 5 .   ? -0.444  1.230   34.522  1.00 25.85 ? 436 HOH A O   1 
HETATM 2329 O  O   . HOH G 5 .   ? 5.900   -14.124 8.995   1.00 28.95 ? 437 HOH A O   1 
HETATM 2330 O  O   . HOH G 5 .   ? 1.747   -15.665 9.266   1.00 22.86 ? 438 HOH A O   1 
HETATM 2331 O  O   . HOH G 5 .   ? -17.990 -11.972 31.709  1.00 20.28 ? 439 HOH A O   1 
HETATM 2332 O  O   . HOH G 5 .   ? -18.560 -12.313 -3.499  1.00 21.24 ? 440 HOH A O   1 
HETATM 2333 O  O   . HOH G 5 .   ? -10.200 15.946  29.484  1.00 28.97 ? 441 HOH A O   1 
HETATM 2334 O  O   . HOH G 5 .   ? -20.591 13.782  28.561  1.00 25.67 ? 442 HOH A O   1 
HETATM 2335 O  O   . HOH G 5 .   ? -17.057 -1.052  40.136  1.00 29.30 ? 443 HOH A O   1 
HETATM 2336 O  O   . HOH G 5 .   ? -6.145  -20.856 26.083  1.00 30.42 ? 444 HOH A O   1 
HETATM 2337 O  O   . HOH G 5 .   ? -31.871 5.443   12.734  1.00 34.93 ? 445 HOH A O   1 
HETATM 2338 O  O   . HOH G 5 .   ? -1.130  23.637  17.981  1.00 31.93 ? 446 HOH A O   1 
HETATM 2339 O  O   . HOH G 5 .   ? -18.175 -8.683  34.818  1.00 30.19 ? 447 HOH A O   1 
HETATM 2340 O  O   . HOH G 5 .   ? -8.093  18.988  10.397  1.00 22.30 ? 448 HOH A O   1 
HETATM 2341 O  O   . HOH G 5 .   ? -26.622 2.829   20.807  1.00 21.10 ? 449 HOH A O   1 
HETATM 2342 O  O   . HOH G 5 .   ? -20.124 -15.623 22.422  1.00 20.94 ? 450 HOH A O   1 
HETATM 2343 O  O   . HOH G 5 .   ? -11.312 1.029   -7.797  1.00 30.10 ? 451 HOH A O   1 
HETATM 2344 O  O   . HOH G 5 .   ? -28.418 2.092   22.531  1.00 29.08 ? 452 HOH A O   1 
HETATM 2345 O  O   . HOH G 5 .   ? 1.378   -9.744  31.455  1.00 28.21 ? 453 HOH A O   1 
HETATM 2346 O  O   . HOH G 5 .   ? 1.390   -6.269  34.448  1.00 18.65 ? 454 HOH A O   1 
HETATM 2347 O  O   . HOH G 5 .   ? -2.718  -14.841 32.737  1.00 28.19 ? 455 HOH A O   1 
HETATM 2348 O  O   . HOH G 5 .   ? -3.848  -1.054  11.354  1.00 20.22 ? 456 HOH A O   1 
HETATM 2349 O  O   . HOH G 5 .   ? -26.058 6.361   27.200  1.00 23.12 ? 457 HOH A O   1 
HETATM 2350 O  O   . HOH G 5 .   ? -18.733 -21.094 14.812  1.00 22.68 ? 458 HOH A O   1 
HETATM 2351 O  O   . HOH G 5 .   ? -5.650  4.089   -5.705  1.00 28.92 ? 459 HOH A O   1 
HETATM 2352 O  O   . HOH G 5 .   ? -3.022  5.957   -1.674  1.00 22.86 ? 460 HOH A O   1 
HETATM 2353 O  O   . HOH G 5 .   ? -0.679  14.064  16.091  1.00 21.21 ? 461 HOH A O   1 
HETATM 2354 O  O   . HOH G 5 .   ? -12.567 6.575   31.117  1.00 26.99 ? 462 HOH A O   1 
HETATM 2355 O  O   . HOH G 5 .   ? -22.102 -21.652 12.227  1.00 30.89 ? 463 HOH A O   1 
HETATM 2356 O  O   . HOH G 5 .   ? -19.814 -4.356  41.481  1.00 29.00 ? 464 HOH A O   1 
HETATM 2357 O  O   . HOH G 5 .   ? -4.545  -15.825 0.828   1.00 25.51 ? 465 HOH A O   1 
HETATM 2358 O  O   . HOH G 5 .   ? 9.287   2.003   11.699  1.00 26.36 ? 466 HOH A O   1 
HETATM 2359 O  O   . HOH G 5 .   ? -1.282  -6.075  36.589  1.00 26.90 ? 467 HOH A O   1 
HETATM 2360 O  O   . HOH G 5 .   ? -21.214 -6.771  -2.166  1.00 33.08 ? 468 HOH A O   1 
HETATM 2361 O  O   . HOH G 5 .   ? 3.995   -15.803 -6.839  1.00 25.42 ? 469 HOH A O   1 
HETATM 2362 O  O   . HOH G 5 .   ? 15.168  -6.545  12.232  1.00 34.83 ? 470 HOH A O   1 
HETATM 2363 O  O   . HOH G 5 .   ? -15.577 -16.541 25.680  1.00 23.32 ? 471 HOH A O   1 
HETATM 2364 O  O   . HOH G 5 .   ? -25.914 -15.399 8.175   1.00 22.61 ? 472 HOH A O   1 
HETATM 2365 O  O   . HOH G 5 .   ? -7.290  -10.069 -4.533  1.00 26.07 ? 473 HOH A O   1 
HETATM 2366 O  O   . HOH G 5 .   ? 12.382  4.054   27.440  1.00 31.54 ? 474 HOH A O   1 
HETATM 2367 O  O   . HOH G 5 .   ? -16.402 16.932  26.507  1.00 28.12 ? 475 HOH A O   1 
HETATM 2368 O  O   . HOH G 5 .   ? -0.103  1.072   -10.763 1.00 26.93 ? 476 HOH A O   1 
HETATM 2369 O  O   . HOH G 5 .   ? 1.261   -11.692 25.165  1.00 19.96 ? 477 HOH A O   1 
HETATM 2370 O  O   . HOH G 5 .   ? 5.340   9.139   21.758  1.00 21.80 ? 478 HOH A O   1 
HETATM 2371 O  O   . HOH G 5 .   ? -23.943 -3.505  3.776   1.00 27.00 ? 479 HOH A O   1 
HETATM 2372 O  O   . HOH G 5 .   ? -3.648  18.073  21.447  1.00 27.75 ? 480 HOH A O   1 
HETATM 2373 O  O   . HOH G 5 .   ? -15.687 -10.345 37.405  1.00 33.18 ? 481 HOH A O   1 
HETATM 2374 O  O   . HOH G 5 .   ? -6.246  15.517  11.875  1.00 26.73 ? 482 HOH A O   1 
HETATM 2375 O  O   . HOH G 5 .   ? 6.341   -5.325  3.646   1.00 27.65 ? 483 HOH A O   1 
HETATM 2376 O  O   . HOH G 5 .   ? 10.258  -8.749  8.402   1.00 28.92 ? 484 HOH A O   1 
HETATM 2377 O  O   . HOH G 5 .   ? -13.265 13.339  31.774  1.00 27.51 ? 485 HOH A O   1 
HETATM 2378 O  O   . HOH G 5 .   ? -3.381  3.639   11.260  1.00 29.10 ? 486 HOH A O   1 
HETATM 2379 O  O   . HOH G 5 .   ? -10.354 6.011   -4.156  1.00 30.37 ? 487 HOH A O   1 
HETATM 2380 O  O   . HOH G 5 .   ? -10.503 -5.595  38.509  1.00 27.58 ? 488 HOH A O   1 
HETATM 2381 O  O   . HOH G 5 .   ? -24.174 -2.005  28.861  1.00 27.51 ? 489 HOH A O   1 
HETATM 2382 O  O   . HOH G 5 .   ? 7.732   -5.043  -0.333  1.00 36.46 ? 490 HOH A O   1 
HETATM 2383 O  O   . HOH G 5 .   ? 9.513   -4.945  -7.866  1.00 27.67 ? 491 HOH A O   1 
HETATM 2384 O  O   . HOH G 5 .   ? 7.184   3.817   31.415  1.00 37.11 ? 492 HOH A O   1 
HETATM 2385 O  O   . HOH G 5 .   ? -24.080 -0.136  1.161   1.00 27.68 ? 493 HOH A O   1 
HETATM 2386 O  O   . HOH G 5 .   ? -11.737 -3.489  42.059  1.00 26.17 ? 494 HOH A O   1 
HETATM 2387 O  O   . HOH G 5 .   ? -27.905 4.084   23.655  1.00 29.34 ? 495 HOH A O   1 
HETATM 2388 O  O   . HOH G 5 .   ? -16.167 3.648   35.281  1.00 29.71 ? 496 HOH A O   1 
HETATM 2389 O  O   . HOH G 5 .   ? -8.246  14.955  10.611  1.00 31.05 ? 497 HOH A O   1 
HETATM 2390 O  O   . HOH G 5 .   ? -25.565 11.026  19.414  1.00 29.49 ? 498 HOH A O   1 
HETATM 2391 O  O   . HOH G 5 .   ? 6.156   -11.284 15.436  1.00 28.24 ? 499 HOH A O   1 
HETATM 2392 O  O   . HOH G 5 .   ? -10.653 13.365  8.492   1.00 30.41 ? 500 HOH A O   1 
HETATM 2393 O  O   . HOH G 5 .   ? 1.302   2.400   35.818  1.00 35.26 ? 501 HOH A O   1 
HETATM 2394 O  O   . HOH G 5 .   ? -19.996 -13.999 24.470  1.00 28.29 ? 502 HOH A O   1 
HETATM 2395 O  O   . HOH G 5 .   ? 0.832   14.689  24.199  1.00 29.39 ? 503 HOH A O   1 
HETATM 2396 O  O   . HOH G 5 .   ? -6.740  12.556  10.283  1.00 32.04 ? 504 HOH A O   1 
HETATM 2397 O  O   . HOH G 5 .   ? 6.333   -5.712  6.718   1.00 24.95 ? 505 HOH A O   1 
HETATM 2398 O  O   . HOH G 5 .   ? -13.606 -0.821  -6.267  1.00 24.34 ? 506 HOH A O   1 
HETATM 2399 O  O   . HOH G 5 .   ? -21.157 0.388   0.087   1.00 35.15 ? 507 HOH A O   1 
HETATM 2400 O  O   . HOH G 5 .   ? 2.223   -14.584 -0.980  1.00 23.22 ? 508 HOH A O   1 
HETATM 2401 O  O   . HOH G 5 .   ? -17.244 -14.151 37.512  1.00 27.08 ? 509 HOH A O   1 
HETATM 2402 O  O   . HOH G 5 .   ? -1.287  4.240   -4.913  1.00 25.56 ? 510 HOH A O   1 
HETATM 2403 O  O   . HOH G 5 .   ? -20.828 8.458   30.156  1.00 27.76 ? 511 HOH A O   1 
HETATM 2404 O  O   . HOH G 5 .   ? -21.663 -20.463 14.604  1.00 27.69 ? 512 HOH A O   1 
HETATM 2405 O  O   . HOH G 5 .   ? -3.645  -20.072 27.043  1.00 29.37 ? 513 HOH A O   1 
HETATM 2406 O  O   . HOH G 5 .   ? -16.647 -14.763 28.784  1.00 32.59 ? 514 HOH A O   1 
HETATM 2407 O  O   . HOH G 5 .   ? -26.941 -1.362  25.987  1.00 22.53 ? 515 HOH A O   1 
HETATM 2408 O  O   . HOH G 5 .   ? -25.563 9.638   13.075  1.00 26.76 ? 516 HOH A O   1 
HETATM 2409 O  O   . HOH G 5 .   ? 2.025   -15.124 -5.040  1.00 28.52 ? 517 HOH A O   1 
HETATM 2410 O  O   . HOH G 5 .   ? 16.363  -3.473  6.526   1.00 24.37 ? 518 HOH A O   1 
HETATM 2411 O  O   . HOH G 5 .   ? -14.537 3.577   33.251  1.00 20.84 ? 519 HOH A O   1 
HETATM 2412 O  O   . HOH G 5 .   ? 3.468   -13.847 12.718  1.00 27.12 ? 520 HOH A O   1 
HETATM 2413 O  O   . HOH G 5 .   ? -3.493  -17.752 -0.122  1.00 26.60 ? 521 HOH A O   1 
HETATM 2414 O  O   . HOH G 5 .   ? -0.978  -17.452 -1.804  1.00 29.70 ? 522 HOH A O   1 
HETATM 2415 O  O   . HOH G 5 .   ? 1.322   -16.388 -1.926  1.00 29.54 ? 523 HOH A O   1 
HETATM 2416 O  O   . HOH G 5 .   ? -22.738 -9.586  25.312  1.00 21.43 ? 524 HOH A O   1 
HETATM 2417 O  O   . HOH G 5 .   ? 1.862   -14.207 20.419  1.00 23.93 ? 525 HOH A O   1 
HETATM 2418 O  O   . HOH G 5 .   ? -10.700 8.492   7.728   1.00 22.59 ? 526 HOH A O   1 
HETATM 2419 O  O   . HOH G 5 .   ? -5.405  -2.300  40.654  1.00 35.79 ? 527 HOH A O   1 
HETATM 2420 O  O   . HOH G 5 .   ? -25.683 -9.837  15.130  1.00 33.26 ? 528 HOH A O   1 
HETATM 2421 O  O   . HOH G 5 .   ? -25.792 -10.837 17.687  1.00 25.64 ? 529 HOH A O   1 
HETATM 2422 O  O   . HOH G 5 .   ? -14.894 6.046   32.700  1.00 28.72 ? 530 HOH A O   1 
HETATM 2423 O  O   . HOH G 5 .   ? 5.885   -2.882  7.050   1.00 29.04 ? 531 HOH A O   1 
HETATM 2424 O  O   . HOH G 5 .   ? 4.958   -12.978 -5.547  1.00 28.21 ? 532 HOH A O   1 
HETATM 2425 O  O   . HOH G 5 .   ? -26.453 -7.685  30.345  1.00 28.15 ? 533 HOH A O   1 
HETATM 2426 O  O   . HOH G 5 .   ? -22.031 19.286  17.469  1.00 31.64 ? 534 HOH A O   1 
HETATM 2427 O  O   . HOH G 5 .   ? -11.295 17.741  12.369  1.00 25.16 ? 535 HOH A O   1 
HETATM 2428 O  O   . HOH G 5 .   ? -15.143 2.678   38.567  1.00 27.42 ? 536 HOH A O   1 
HETATM 2429 O  O   . HOH G 5 .   ? -22.039 -14.177 18.842  1.00 27.13 ? 537 HOH A O   1 
HETATM 2430 O  O   . HOH G 5 .   ? 3.228   4.364   11.922  1.00 28.66 ? 538 HOH A O   1 
HETATM 2431 O  O   . HOH G 5 .   ? 14.891  -0.133  15.107  1.00 26.22 ? 539 HOH A O   1 
HETATM 2432 O  O   . HOH G 5 .   ? 4.757   -3.137  3.154   1.00 32.56 ? 540 HOH A O   1 
HETATM 2433 O  O   . HOH G 5 .   ? 0.756   3.620   9.681   1.00 42.00 ? 541 HOH A O   1 
HETATM 2434 O  O   . HOH G 5 .   ? -2.664  -19.213 6.287   1.00 26.67 ? 542 HOH A O   1 
HETATM 2435 O  O   . HOH G 5 .   ? 6.365   -0.258  -1.503  1.00 39.93 ? 543 HOH A O   1 
HETATM 2436 O  O   . HOH G 5 .   ? -27.367 -5.325  27.457  1.00 27.01 ? 544 HOH A O   1 
HETATM 2437 O  O   . HOH G 5 .   ? 12.121  -11.011 14.281  1.00 28.78 ? 545 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   262 1   ZN  ZN  A . 
C 3 J90 1   263 1   J90 J90 A . 
D 3 J90 1   264 2   J90 J90 A . 
E 4 DMS 1   265 1   DMS DMS A . 
F 4 DMS 1   266 2   DMS DMS A . 
G 5 HOH 1   126 126 HOH HOH A . 
G 5 HOH 2   267 267 HOH HOH A . 
G 5 HOH 3   268 268 HOH HOH A . 
G 5 HOH 4   269 269 HOH HOH A . 
G 5 HOH 5   270 270 HOH HOH A . 
G 5 HOH 6   271 271 HOH HOH A . 
G 5 HOH 7   272 272 HOH HOH A . 
G 5 HOH 8   273 273 HOH HOH A . 
G 5 HOH 9   274 274 HOH HOH A . 
G 5 HOH 10  275 275 HOH HOH A . 
G 5 HOH 11  276 276 HOH HOH A . 
G 5 HOH 12  277 277 HOH HOH A . 
G 5 HOH 13  278 278 HOH HOH A . 
G 5 HOH 14  279 279 HOH HOH A . 
G 5 HOH 15  280 280 HOH HOH A . 
G 5 HOH 16  281 1   HOH HOH A . 
G 5 HOH 17  282 2   HOH HOH A . 
G 5 HOH 18  283 3   HOH HOH A . 
G 5 HOH 19  284 4   HOH HOH A . 
G 5 HOH 20  285 5   HOH HOH A . 
G 5 HOH 21  286 6   HOH HOH A . 
G 5 HOH 22  287 7   HOH HOH A . 
G 5 HOH 23  288 8   HOH HOH A . 
G 5 HOH 24  289 9   HOH HOH A . 
G 5 HOH 25  290 10  HOH HOH A . 
G 5 HOH 26  291 11  HOH HOH A . 
G 5 HOH 27  292 12  HOH HOH A . 
G 5 HOH 28  293 13  HOH HOH A . 
G 5 HOH 29  294 14  HOH HOH A . 
G 5 HOH 30  295 15  HOH HOH A . 
G 5 HOH 31  296 16  HOH HOH A . 
G 5 HOH 32  297 17  HOH HOH A . 
G 5 HOH 33  298 18  HOH HOH A . 
G 5 HOH 34  299 19  HOH HOH A . 
G 5 HOH 35  300 20  HOH HOH A . 
G 5 HOH 36  301 21  HOH HOH A . 
G 5 HOH 37  302 22  HOH HOH A . 
G 5 HOH 38  303 23  HOH HOH A . 
G 5 HOH 39  304 24  HOH HOH A . 
G 5 HOH 40  305 25  HOH HOH A . 
G 5 HOH 41  306 26  HOH HOH A . 
G 5 HOH 42  307 27  HOH HOH A . 
G 5 HOH 43  308 28  HOH HOH A . 
G 5 HOH 44  309 29  HOH HOH A . 
G 5 HOH 45  310 30  HOH HOH A . 
G 5 HOH 46  311 31  HOH HOH A . 
G 5 HOH 47  312 32  HOH HOH A . 
G 5 HOH 48  313 33  HOH HOH A . 
G 5 HOH 49  314 34  HOH HOH A . 
G 5 HOH 50  315 35  HOH HOH A . 
G 5 HOH 51  316 36  HOH HOH A . 
G 5 HOH 52  317 37  HOH HOH A . 
G 5 HOH 53  318 38  HOH HOH A . 
G 5 HOH 54  319 39  HOH HOH A . 
G 5 HOH 55  320 40  HOH HOH A . 
G 5 HOH 56  321 41  HOH HOH A . 
G 5 HOH 57  322 42  HOH HOH A . 
G 5 HOH 58  323 43  HOH HOH A . 
G 5 HOH 59  324 44  HOH HOH A . 
G 5 HOH 60  325 45  HOH HOH A . 
G 5 HOH 61  326 46  HOH HOH A . 
G 5 HOH 62  327 47  HOH HOH A . 
G 5 HOH 63  328 48  HOH HOH A . 
G 5 HOH 64  329 49  HOH HOH A . 
G 5 HOH 65  330 50  HOH HOH A . 
G 5 HOH 66  331 51  HOH HOH A . 
G 5 HOH 67  332 52  HOH HOH A . 
G 5 HOH 68  333 53  HOH HOH A . 
G 5 HOH 69  334 54  HOH HOH A . 
G 5 HOH 70  335 55  HOH HOH A . 
G 5 HOH 71  336 56  HOH HOH A . 
G 5 HOH 72  337 57  HOH HOH A . 
G 5 HOH 73  338 58  HOH HOH A . 
G 5 HOH 74  339 59  HOH HOH A . 
G 5 HOH 75  340 60  HOH HOH A . 
G 5 HOH 76  341 61  HOH HOH A . 
G 5 HOH 77  342 62  HOH HOH A . 
G 5 HOH 78  343 63  HOH HOH A . 
G 5 HOH 79  344 64  HOH HOH A . 
G 5 HOH 80  345 65  HOH HOH A . 
G 5 HOH 81  346 66  HOH HOH A . 
G 5 HOH 82  347 67  HOH HOH A . 
G 5 HOH 83  348 68  HOH HOH A . 
G 5 HOH 84  349 69  HOH HOH A . 
G 5 HOH 85  350 70  HOH HOH A . 
G 5 HOH 86  351 71  HOH HOH A . 
G 5 HOH 87  352 72  HOH HOH A . 
G 5 HOH 88  353 73  HOH HOH A . 
G 5 HOH 89  354 74  HOH HOH A . 
G 5 HOH 90  355 75  HOH HOH A . 
G 5 HOH 91  356 76  HOH HOH A . 
G 5 HOH 92  357 77  HOH HOH A . 
G 5 HOH 93  358 78  HOH HOH A . 
G 5 HOH 94  359 79  HOH HOH A . 
G 5 HOH 95  360 80  HOH HOH A . 
G 5 HOH 96  361 81  HOH HOH A . 
G 5 HOH 97  362 82  HOH HOH A . 
G 5 HOH 98  363 83  HOH HOH A . 
G 5 HOH 99  364 84  HOH HOH A . 
G 5 HOH 100 365 85  HOH HOH A . 
G 5 HOH 101 366 86  HOH HOH A . 
G 5 HOH 102 367 87  HOH HOH A . 
G 5 HOH 103 368 88  HOH HOH A . 
G 5 HOH 104 369 89  HOH HOH A . 
G 5 HOH 105 370 90  HOH HOH A . 
G 5 HOH 106 371 91  HOH HOH A . 
G 5 HOH 107 372 92  HOH HOH A . 
G 5 HOH 108 373 93  HOH HOH A . 
G 5 HOH 109 374 94  HOH HOH A . 
G 5 HOH 110 375 95  HOH HOH A . 
G 5 HOH 111 376 96  HOH HOH A . 
G 5 HOH 112 377 97  HOH HOH A . 
G 5 HOH 113 378 98  HOH HOH A . 
G 5 HOH 114 379 99  HOH HOH A . 
G 5 HOH 115 380 100 HOH HOH A . 
G 5 HOH 116 381 101 HOH HOH A . 
G 5 HOH 117 382 102 HOH HOH A . 
G 5 HOH 118 383 103 HOH HOH A . 
G 5 HOH 119 384 104 HOH HOH A . 
G 5 HOH 120 385 105 HOH HOH A . 
G 5 HOH 121 386 106 HOH HOH A . 
G 5 HOH 122 387 107 HOH HOH A . 
G 5 HOH 123 388 108 HOH HOH A . 
G 5 HOH 124 389 109 HOH HOH A . 
G 5 HOH 125 390 110 HOH HOH A . 
G 5 HOH 126 391 111 HOH HOH A . 
G 5 HOH 127 392 112 HOH HOH A . 
G 5 HOH 128 393 113 HOH HOH A . 
G 5 HOH 129 394 114 HOH HOH A . 
G 5 HOH 130 395 115 HOH HOH A . 
G 5 HOH 131 396 116 HOH HOH A . 
G 5 HOH 132 397 117 HOH HOH A . 
G 5 HOH 133 398 118 HOH HOH A . 
G 5 HOH 134 399 119 HOH HOH A . 
G 5 HOH 135 400 120 HOH HOH A . 
G 5 HOH 136 401 121 HOH HOH A . 
G 5 HOH 137 402 122 HOH HOH A . 
G 5 HOH 138 403 123 HOH HOH A . 
G 5 HOH 139 404 124 HOH HOH A . 
G 5 HOH 140 405 125 HOH HOH A . 
G 5 HOH 141 406 127 HOH HOH A . 
G 5 HOH 142 407 128 HOH HOH A . 
G 5 HOH 143 408 129 HOH HOH A . 
G 5 HOH 144 409 130 HOH HOH A . 
G 5 HOH 145 410 131 HOH HOH A . 
G 5 HOH 146 411 132 HOH HOH A . 
G 5 HOH 147 412 133 HOH HOH A . 
G 5 HOH 148 413 134 HOH HOH A . 
G 5 HOH 149 414 135 HOH HOH A . 
G 5 HOH 150 415 136 HOH HOH A . 
G 5 HOH 151 416 137 HOH HOH A . 
G 5 HOH 152 417 138 HOH HOH A . 
G 5 HOH 153 418 139 HOH HOH A . 
G 5 HOH 154 419 140 HOH HOH A . 
G 5 HOH 155 420 141 HOH HOH A . 
G 5 HOH 156 421 142 HOH HOH A . 
G 5 HOH 157 422 143 HOH HOH A . 
G 5 HOH 158 423 144 HOH HOH A . 
G 5 HOH 159 424 145 HOH HOH A . 
G 5 HOH 160 425 146 HOH HOH A . 
G 5 HOH 161 426 147 HOH HOH A . 
G 5 HOH 162 427 148 HOH HOH A . 
G 5 HOH 163 428 149 HOH HOH A . 
G 5 HOH 164 429 150 HOH HOH A . 
G 5 HOH 165 430 151 HOH HOH A . 
G 5 HOH 166 431 152 HOH HOH A . 
G 5 HOH 167 432 153 HOH HOH A . 
G 5 HOH 168 433 154 HOH HOH A . 
G 5 HOH 169 434 155 HOH HOH A . 
G 5 HOH 170 435 156 HOH HOH A . 
G 5 HOH 171 436 157 HOH HOH A . 
G 5 HOH 172 437 158 HOH HOH A . 
G 5 HOH 173 438 159 HOH HOH A . 
G 5 HOH 174 439 160 HOH HOH A . 
G 5 HOH 175 440 161 HOH HOH A . 
G 5 HOH 176 441 162 HOH HOH A . 
G 5 HOH 177 442 163 HOH HOH A . 
G 5 HOH 178 443 164 HOH HOH A . 
G 5 HOH 179 444 165 HOH HOH A . 
G 5 HOH 180 445 166 HOH HOH A . 
G 5 HOH 181 446 167 HOH HOH A . 
G 5 HOH 182 447 168 HOH HOH A . 
G 5 HOH 183 448 169 HOH HOH A . 
G 5 HOH 184 449 170 HOH HOH A . 
G 5 HOH 185 450 171 HOH HOH A . 
G 5 HOH 186 451 172 HOH HOH A . 
G 5 HOH 187 452 173 HOH HOH A . 
G 5 HOH 188 453 174 HOH HOH A . 
G 5 HOH 189 454 175 HOH HOH A . 
G 5 HOH 190 455 176 HOH HOH A . 
G 5 HOH 191 456 177 HOH HOH A . 
G 5 HOH 192 457 178 HOH HOH A . 
G 5 HOH 193 458 179 HOH HOH A . 
G 5 HOH 194 459 180 HOH HOH A . 
G 5 HOH 195 460 181 HOH HOH A . 
G 5 HOH 196 461 182 HOH HOH A . 
G 5 HOH 197 462 183 HOH HOH A . 
G 5 HOH 198 463 184 HOH HOH A . 
G 5 HOH 199 464 185 HOH HOH A . 
G 5 HOH 200 465 186 HOH HOH A . 
G 5 HOH 201 466 187 HOH HOH A . 
G 5 HOH 202 467 188 HOH HOH A . 
G 5 HOH 203 468 189 HOH HOH A . 
G 5 HOH 204 469 190 HOH HOH A . 
G 5 HOH 205 470 191 HOH HOH A . 
G 5 HOH 206 471 192 HOH HOH A . 
G 5 HOH 207 472 193 HOH HOH A . 
G 5 HOH 208 473 194 HOH HOH A . 
G 5 HOH 209 474 195 HOH HOH A . 
G 5 HOH 210 475 196 HOH HOH A . 
G 5 HOH 211 476 197 HOH HOH A . 
G 5 HOH 212 477 198 HOH HOH A . 
G 5 HOH 213 478 199 HOH HOH A . 
G 5 HOH 214 479 200 HOH HOH A . 
G 5 HOH 215 480 201 HOH HOH A . 
G 5 HOH 216 481 202 HOH HOH A . 
G 5 HOH 217 482 203 HOH HOH A . 
G 5 HOH 218 483 204 HOH HOH A . 
G 5 HOH 219 484 205 HOH HOH A . 
G 5 HOH 220 485 206 HOH HOH A . 
G 5 HOH 221 486 207 HOH HOH A . 
G 5 HOH 222 487 208 HOH HOH A . 
G 5 HOH 223 488 209 HOH HOH A . 
G 5 HOH 224 489 210 HOH HOH A . 
G 5 HOH 225 490 211 HOH HOH A . 
G 5 HOH 226 491 212 HOH HOH A . 
G 5 HOH 227 492 213 HOH HOH A . 
G 5 HOH 228 493 214 HOH HOH A . 
G 5 HOH 229 494 215 HOH HOH A . 
G 5 HOH 230 495 216 HOH HOH A . 
G 5 HOH 231 496 217 HOH HOH A . 
G 5 HOH 232 497 218 HOH HOH A . 
G 5 HOH 233 498 219 HOH HOH A . 
G 5 HOH 234 499 220 HOH HOH A . 
G 5 HOH 235 500 221 HOH HOH A . 
G 5 HOH 236 501 222 HOH HOH A . 
G 5 HOH 237 502 223 HOH HOH A . 
G 5 HOH 238 503 224 HOH HOH A . 
G 5 HOH 239 504 225 HOH HOH A . 
G 5 HOH 240 505 226 HOH HOH A . 
G 5 HOH 241 506 227 HOH HOH A . 
G 5 HOH 242 507 228 HOH HOH A . 
G 5 HOH 243 508 229 HOH HOH A . 
G 5 HOH 244 509 230 HOH HOH A . 
G 5 HOH 245 510 231 HOH HOH A . 
G 5 HOH 246 511 232 HOH HOH A . 
G 5 HOH 247 512 233 HOH HOH A . 
G 5 HOH 248 513 234 HOH HOH A . 
G 5 HOH 249 514 235 HOH HOH A . 
G 5 HOH 250 515 236 HOH HOH A . 
G 5 HOH 251 516 237 HOH HOH A . 
G 5 HOH 252 517 238 HOH HOH A . 
G 5 HOH 253 518 239 HOH HOH A . 
G 5 HOH 254 519 240 HOH HOH A . 
G 5 HOH 255 520 241 HOH HOH A . 
G 5 HOH 256 521 242 HOH HOH A . 
G 5 HOH 257 522 243 HOH HOH A . 
G 5 HOH 258 523 244 HOH HOH A . 
G 5 HOH 259 524 245 HOH HOH A . 
G 5 HOH 260 525 246 HOH HOH A . 
G 5 HOH 261 526 247 HOH HOH A . 
G 5 HOH 262 527 248 HOH HOH A . 
G 5 HOH 263 528 249 HOH HOH A . 
G 5 HOH 264 529 250 HOH HOH A . 
G 5 HOH 265 530 251 HOH HOH A . 
G 5 HOH 266 531 252 HOH HOH A . 
G 5 HOH 267 532 253 HOH HOH A . 
G 5 HOH 268 533 254 HOH HOH A . 
G 5 HOH 269 534 255 HOH HOH A . 
G 5 HOH 270 535 256 HOH HOH A . 
G 5 HOH 271 536 257 HOH HOH A . 
G 5 HOH 272 537 258 HOH HOH A . 
G 5 HOH 273 538 259 HOH HOH A . 
G 5 HOH 274 539 260 HOH HOH A . 
G 5 HOH 275 540 261 HOH HOH A . 
G 5 HOH 276 541 262 HOH HOH A . 
G 5 HOH 277 542 263 HOH HOH A . 
G 5 HOH 278 543 264 HOH HOH A . 
G 5 HOH 279 544 265 HOH HOH A . 
G 5 HOH 280 545 266 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_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 2010-10-20 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-08 
4 'Structure model' 1 3 2023-11-01 
# 
_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' 'Version format compliance' 
2 3 'Structure model' 'Refinement description'    
3 4 'Structure model' 'Data collection'           
4 4 'Structure model' 'Database references'       
5 4 'Structure model' 'Derived calculations'      
6 4 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' software                      
2 4 'Structure model' chem_comp_atom                
3 4 'Structure model' chem_comp_bond                
4 4 'Structure model' database_2                    
5 4 'Structure model' pdbx_initial_refinement_model 
6 4 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_database_2.pdbx_DOI'                
2 4 'Structure model' '_database_2.pdbx_database_accession' 
3 4 'Structure model' '_struct_site.pdbx_auth_asym_id'      
4 4 'Structure model' '_struct_site.pdbx_auth_comp_id'      
5 4 'Structure model' '_struct_site.pdbx_auth_seq_id'       
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.2.19 22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
O           .      ?               ?       ?                    ?                        'model building'  ? ?          ? 5 
# 
_pdbx_entry_details.entry_id                 3MHI 
_pdbx_entry_details.nonpolymer_details       'METAL ION NATURALLY OCCURS IN CARBONIC ANHYDRASES.' 
_pdbx_entry_details.sequence_details         '126 IS SKIPPED IN THE NUMBERING.' 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A LYS 76  ? ? O A HOH 516 ? ? 2.01 
2 1 NE2 A GLN 137 ? ? O A HOH 480 ? ? 2.03 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -144.79 53.71   
2 1 LYS A 111 ? ? 71.37   -2.67   
3 1 PHE A 176 ? ? -153.61 71.46   
4 1 ASN A 244 ? ? -94.98  48.26   
5 1 LYS A 252 ? ? 58.03   -137.60 
6 1 ASN A 253 ? ? -94.70  58.20   
# 
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 
J90 N1   N  N N 193 
J90 C2   C  N N 194 
J90 N3   N  N N 195 
J90 C4   C  N N 196 
J90 C5   C  N N 197 
J90 C6   C  N N 198 
J90 N7   N  N N 199 
J90 C8   C  Y N 200 
J90 C9   C  Y N 201 
J90 C10  C  Y N 202 
J90 C11  C  Y N 203 
J90 C12  C  Y N 204 
J90 C13  C  Y N 205 
J90 S14  S  N N 206 
J90 O15  O  N N 207 
J90 O16  O  N N 208 
J90 N17  N  N N 209 
J90 N18  N  N N 210 
J90 O19  O  N N 211 
J90 O20  O  N N 212 
J90 O21  O  N N 213 
J90 C22  C  N N 214 
J90 HN1  H  N N 215 
J90 H2   H  N N 216 
J90 HN7  H  N N 217 
J90 H9   H  N N 218 
J90 H10  H  N N 219 
J90 H12  H  N N 220 
J90 H13  H  N N 221 
J90 HN17 H  N N 222 
J90 HN1A H  N N 223 
J90 H22  H  N N 224 
J90 H22A H  N N 225 
LEU N    N  N N 226 
LEU CA   C  N S 227 
LEU C    C  N N 228 
LEU O    O  N N 229 
LEU CB   C  N N 230 
LEU CG   C  N N 231 
LEU CD1  C  N N 232 
LEU CD2  C  N N 233 
LEU OXT  O  N N 234 
LEU H    H  N N 235 
LEU H2   H  N N 236 
LEU HA   H  N N 237 
LEU HB2  H  N N 238 
LEU HB3  H  N N 239 
LEU HG   H  N N 240 
LEU HD11 H  N N 241 
LEU HD12 H  N N 242 
LEU HD13 H  N N 243 
LEU HD21 H  N N 244 
LEU HD22 H  N N 245 
LEU HD23 H  N N 246 
LEU HXT  H  N N 247 
LYS N    N  N N 248 
LYS CA   C  N S 249 
LYS C    C  N N 250 
LYS O    O  N N 251 
LYS CB   C  N N 252 
LYS CG   C  N N 253 
LYS CD   C  N N 254 
LYS CE   C  N N 255 
LYS NZ   N  N N 256 
LYS OXT  O  N N 257 
LYS H    H  N N 258 
LYS H2   H  N N 259 
LYS HA   H  N N 260 
LYS HB2  H  N N 261 
LYS HB3  H  N N 262 
LYS HG2  H  N N 263 
LYS HG3  H  N N 264 
LYS HD2  H  N N 265 
LYS HD3  H  N N 266 
LYS HE2  H  N N 267 
LYS HE3  H  N N 268 
LYS HZ1  H  N N 269 
LYS HZ2  H  N N 270 
LYS HZ3  H  N N 271 
LYS HXT  H  N N 272 
MET N    N  N N 273 
MET CA   C  N S 274 
MET C    C  N N 275 
MET O    O  N N 276 
MET CB   C  N N 277 
MET CG   C  N N 278 
MET SD   S  N N 279 
MET CE   C  N N 280 
MET OXT  O  N N 281 
MET H    H  N N 282 
MET H2   H  N N 283 
MET HA   H  N N 284 
MET HB2  H  N N 285 
MET HB3  H  N N 286 
MET HG2  H  N N 287 
MET HG3  H  N N 288 
MET HE1  H  N N 289 
MET HE2  H  N N 290 
MET HE3  H  N N 291 
MET HXT  H  N N 292 
PHE N    N  N N 293 
PHE CA   C  N S 294 
PHE C    C  N N 295 
PHE O    O  N N 296 
PHE CB   C  N N 297 
PHE CG   C  Y N 298 
PHE CD1  C  Y N 299 
PHE CD2  C  Y N 300 
PHE CE1  C  Y N 301 
PHE CE2  C  Y N 302 
PHE CZ   C  Y N 303 
PHE OXT  O  N N 304 
PHE H    H  N N 305 
PHE H2   H  N N 306 
PHE HA   H  N N 307 
PHE HB2  H  N N 308 
PHE HB3  H  N N 309 
PHE HD1  H  N N 310 
PHE HD2  H  N N 311 
PHE HE1  H  N N 312 
PHE HE2  H  N N 313 
PHE HZ   H  N N 314 
PHE HXT  H  N N 315 
PRO N    N  N N 316 
PRO CA   C  N S 317 
PRO C    C  N N 318 
PRO O    O  N N 319 
PRO CB   C  N N 320 
PRO CG   C  N N 321 
PRO CD   C  N N 322 
PRO OXT  O  N N 323 
PRO H    H  N N 324 
PRO HA   H  N N 325 
PRO HB2  H  N N 326 
PRO HB3  H  N N 327 
PRO HG2  H  N N 328 
PRO HG3  H  N N 329 
PRO HD2  H  N N 330 
PRO HD3  H  N N 331 
PRO HXT  H  N N 332 
SER N    N  N N 333 
SER CA   C  N S 334 
SER C    C  N N 335 
SER O    O  N N 336 
SER CB   C  N N 337 
SER OG   O  N N 338 
SER OXT  O  N N 339 
SER H    H  N N 340 
SER H2   H  N N 341 
SER HA   H  N N 342 
SER HB2  H  N N 343 
SER HB3  H  N N 344 
SER HG   H  N N 345 
SER HXT  H  N N 346 
THR N    N  N N 347 
THR CA   C  N S 348 
THR C    C  N N 349 
THR O    O  N N 350 
THR CB   C  N R 351 
THR OG1  O  N N 352 
THR CG2  C  N N 353 
THR OXT  O  N N 354 
THR H    H  N N 355 
THR H2   H  N N 356 
THR HA   H  N N 357 
THR HB   H  N N 358 
THR HG1  H  N N 359 
THR HG21 H  N N 360 
THR HG22 H  N N 361 
THR HG23 H  N N 362 
THR HXT  H  N N 363 
TRP N    N  N N 364 
TRP CA   C  N S 365 
TRP C    C  N N 366 
TRP O    O  N N 367 
TRP CB   C  N N 368 
TRP CG   C  Y N 369 
TRP CD1  C  Y N 370 
TRP CD2  C  Y N 371 
TRP NE1  N  Y N 372 
TRP CE2  C  Y N 373 
TRP CE3  C  Y N 374 
TRP CZ2  C  Y N 375 
TRP CZ3  C  Y N 376 
TRP CH2  C  Y N 377 
TRP OXT  O  N N 378 
TRP H    H  N N 379 
TRP H2   H  N N 380 
TRP HA   H  N N 381 
TRP HB2  H  N N 382 
TRP HB3  H  N N 383 
TRP HD1  H  N N 384 
TRP HE1  H  N N 385 
TRP HE3  H  N N 386 
TRP HZ2  H  N N 387 
TRP HZ3  H  N N 388 
TRP HH2  H  N N 389 
TRP HXT  H  N N 390 
TYR N    N  N N 391 
TYR CA   C  N S 392 
TYR C    C  N N 393 
TYR O    O  N N 394 
TYR CB   C  N N 395 
TYR CG   C  Y N 396 
TYR CD1  C  Y N 397 
TYR CD2  C  Y N 398 
TYR CE1  C  Y N 399 
TYR CE2  C  Y N 400 
TYR CZ   C  Y N 401 
TYR OH   O  N N 402 
TYR OXT  O  N N 403 
TYR H    H  N N 404 
TYR H2   H  N N 405 
TYR HA   H  N N 406 
TYR HB2  H  N N 407 
TYR HB3  H  N N 408 
TYR HD1  H  N N 409 
TYR HD2  H  N N 410 
TYR HE1  H  N N 411 
TYR HE2  H  N N 412 
TYR HH   H  N N 413 
TYR HXT  H  N N 414 
VAL N    N  N N 415 
VAL CA   C  N S 416 
VAL C    C  N N 417 
VAL O    O  N N 418 
VAL CB   C  N N 419 
VAL CG1  C  N N 420 
VAL CG2  C  N N 421 
VAL OXT  O  N N 422 
VAL H    H  N N 423 
VAL H2   H  N N 424 
VAL HA   H  N N 425 
VAL HB   H  N N 426 
VAL HG11 H  N N 427 
VAL HG12 H  N N 428 
VAL HG13 H  N N 429 
VAL HG21 H  N N 430 
VAL HG22 H  N N 431 
VAL HG23 H  N N 432 
VAL HXT  H  N N 433 
ZN  ZN   ZN N N 434 
# 
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 
J90 N1  C2   sing N N 182 
J90 N1  C6   sing N N 183 
J90 C2  N3   doub N N 184 
J90 N3  C4   sing N N 185 
J90 C4  C5   doub N N 186 
J90 C4  N7   sing N N 187 
J90 C5  C6   sing N N 188 
J90 C5  N18  sing N N 189 
J90 C6  O21  doub N N 190 
J90 N7  C22  sing N N 191 
J90 C8  C9   doub Y N 192 
J90 C8  C13  sing Y N 193 
J90 C8  C22  sing N N 194 
J90 C9  C10  sing Y N 195 
J90 C10 C11  doub Y N 196 
J90 C11 C12  sing Y N 197 
J90 C11 S14  sing N N 198 
J90 C12 C13  doub Y N 199 
J90 S14 O15  doub N N 200 
J90 S14 O16  doub N N 201 
J90 S14 N17  sing N N 202 
J90 N18 O19  sing N N 203 
J90 N18 O20  doub N N 204 
J90 N1  HN1  sing N N 205 
J90 C2  H2   sing N N 206 
J90 N7  HN7  sing N N 207 
J90 C9  H9   sing N N 208 
J90 C10 H10  sing N N 209 
J90 C12 H12  sing N N 210 
J90 C13 H13  sing N N 211 
J90 N17 HN17 sing N N 212 
J90 N17 HN1A sing N N 213 
J90 C22 H22  sing N N 214 
J90 C22 H22A sing N N 215 
LEU N   CA   sing N N 216 
LEU N   H    sing N N 217 
LEU N   H2   sing N N 218 
LEU CA  C    sing N N 219 
LEU CA  CB   sing N N 220 
LEU CA  HA   sing N N 221 
LEU C   O    doub N N 222 
LEU C   OXT  sing N N 223 
LEU CB  CG   sing N N 224 
LEU CB  HB2  sing N N 225 
LEU CB  HB3  sing N N 226 
LEU CG  CD1  sing N N 227 
LEU CG  CD2  sing N N 228 
LEU CG  HG   sing N N 229 
LEU CD1 HD11 sing N N 230 
LEU CD1 HD12 sing N N 231 
LEU CD1 HD13 sing N N 232 
LEU CD2 HD21 sing N N 233 
LEU CD2 HD22 sing N N 234 
LEU CD2 HD23 sing N N 235 
LEU OXT HXT  sing N N 236 
LYS N   CA   sing N N 237 
LYS N   H    sing N N 238 
LYS N   H2   sing N N 239 
LYS CA  C    sing N N 240 
LYS CA  CB   sing N N 241 
LYS CA  HA   sing N N 242 
LYS C   O    doub N N 243 
LYS C   OXT  sing N N 244 
LYS CB  CG   sing N N 245 
LYS CB  HB2  sing N N 246 
LYS CB  HB3  sing N N 247 
LYS CG  CD   sing N N 248 
LYS CG  HG2  sing N N 249 
LYS CG  HG3  sing N N 250 
LYS CD  CE   sing N N 251 
LYS CD  HD2  sing N N 252 
LYS CD  HD3  sing N N 253 
LYS CE  NZ   sing N N 254 
LYS CE  HE2  sing N N 255 
LYS CE  HE3  sing N N 256 
LYS NZ  HZ1  sing N N 257 
LYS NZ  HZ2  sing N N 258 
LYS NZ  HZ3  sing N N 259 
LYS OXT HXT  sing N N 260 
MET N   CA   sing N N 261 
MET N   H    sing N N 262 
MET N   H2   sing N N 263 
MET CA  C    sing N N 264 
MET CA  CB   sing N N 265 
MET CA  HA   sing N N 266 
MET C   O    doub N N 267 
MET C   OXT  sing N N 268 
MET CB  CG   sing N N 269 
MET CB  HB2  sing N N 270 
MET CB  HB3  sing N N 271 
MET CG  SD   sing N N 272 
MET CG  HG2  sing N N 273 
MET CG  HG3  sing N N 274 
MET SD  CE   sing N N 275 
MET CE  HE1  sing N N 276 
MET CE  HE2  sing N N 277 
MET CE  HE3  sing N N 278 
MET OXT HXT  sing N N 279 
PHE N   CA   sing N N 280 
PHE N   H    sing N N 281 
PHE N   H2   sing N N 282 
PHE CA  C    sing N N 283 
PHE CA  CB   sing N N 284 
PHE CA  HA   sing N N 285 
PHE C   O    doub N N 286 
PHE C   OXT  sing N N 287 
PHE CB  CG   sing N N 288 
PHE CB  HB2  sing N N 289 
PHE CB  HB3  sing N N 290 
PHE CG  CD1  doub Y N 291 
PHE CG  CD2  sing Y N 292 
PHE CD1 CE1  sing Y N 293 
PHE CD1 HD1  sing N N 294 
PHE CD2 CE2  doub Y N 295 
PHE CD2 HD2  sing N N 296 
PHE CE1 CZ   doub Y N 297 
PHE CE1 HE1  sing N N 298 
PHE CE2 CZ   sing Y N 299 
PHE CE2 HE2  sing N N 300 
PHE CZ  HZ   sing N N 301 
PHE OXT HXT  sing N N 302 
PRO N   CA   sing N N 303 
PRO N   CD   sing N N 304 
PRO N   H    sing N N 305 
PRO CA  C    sing N N 306 
PRO CA  CB   sing N N 307 
PRO CA  HA   sing N N 308 
PRO C   O    doub N N 309 
PRO C   OXT  sing N N 310 
PRO CB  CG   sing N N 311 
PRO CB  HB2  sing N N 312 
PRO CB  HB3  sing N N 313 
PRO CG  CD   sing N N 314 
PRO CG  HG2  sing N N 315 
PRO CG  HG3  sing N N 316 
PRO CD  HD2  sing N N 317 
PRO CD  HD3  sing N N 318 
PRO OXT HXT  sing N N 319 
SER N   CA   sing N N 320 
SER N   H    sing N N 321 
SER N   H2   sing N N 322 
SER CA  C    sing N N 323 
SER CA  CB   sing N N 324 
SER CA  HA   sing N N 325 
SER C   O    doub N N 326 
SER C   OXT  sing N N 327 
SER CB  OG   sing N N 328 
SER CB  HB2  sing N N 329 
SER CB  HB3  sing N N 330 
SER OG  HG   sing N N 331 
SER OXT HXT  sing N N 332 
THR N   CA   sing N N 333 
THR N   H    sing N N 334 
THR N   H2   sing N N 335 
THR CA  C    sing N N 336 
THR CA  CB   sing N N 337 
THR CA  HA   sing N N 338 
THR C   O    doub N N 339 
THR C   OXT  sing N N 340 
THR CB  OG1  sing N N 341 
THR CB  CG2  sing N N 342 
THR CB  HB   sing N N 343 
THR OG1 HG1  sing N N 344 
THR CG2 HG21 sing N N 345 
THR CG2 HG22 sing N N 346 
THR CG2 HG23 sing N N 347 
THR OXT HXT  sing N N 348 
TRP N   CA   sing N N 349 
TRP N   H    sing N N 350 
TRP N   H2   sing N N 351 
TRP CA  C    sing N N 352 
TRP CA  CB   sing N N 353 
TRP CA  HA   sing N N 354 
TRP C   O    doub N N 355 
TRP C   OXT  sing N N 356 
TRP CB  CG   sing N N 357 
TRP CB  HB2  sing N N 358 
TRP CB  HB3  sing N N 359 
TRP CG  CD1  doub Y N 360 
TRP CG  CD2  sing Y N 361 
TRP CD1 NE1  sing Y N 362 
TRP CD1 HD1  sing N N 363 
TRP CD2 CE2  doub Y N 364 
TRP CD2 CE3  sing Y N 365 
TRP NE1 CE2  sing Y N 366 
TRP NE1 HE1  sing N N 367 
TRP CE2 CZ2  sing Y N 368 
TRP CE3 CZ3  doub Y N 369 
TRP CE3 HE3  sing N N 370 
TRP CZ2 CH2  doub Y N 371 
TRP CZ2 HZ2  sing N N 372 
TRP CZ3 CH2  sing Y N 373 
TRP CZ3 HZ3  sing N N 374 
TRP CH2 HH2  sing N N 375 
TRP OXT HXT  sing N N 376 
TYR N   CA   sing N N 377 
TYR N   H    sing N N 378 
TYR N   H2   sing N N 379 
TYR CA  C    sing N N 380 
TYR CA  CB   sing N N 381 
TYR CA  HA   sing N N 382 
TYR C   O    doub N N 383 
TYR C   OXT  sing N N 384 
TYR CB  CG   sing N N 385 
TYR CB  HB2  sing N N 386 
TYR CB  HB3  sing N N 387 
TYR CG  CD1  doub Y N 388 
TYR CG  CD2  sing Y N 389 
TYR CD1 CE1  sing Y N 390 
TYR CD1 HD1  sing N N 391 
TYR CD2 CE2  doub Y N 392 
TYR CD2 HD2  sing N N 393 
TYR CE1 CZ   doub Y N 394 
TYR CE1 HE1  sing N N 395 
TYR CE2 CZ   sing Y N 396 
TYR CE2 HE2  sing N N 397 
TYR CZ  OH   sing N N 398 
TYR OH  HH   sing N N 399 
TYR OXT HXT  sing N N 400 
VAL N   CA   sing N N 401 
VAL N   H    sing N N 402 
VAL N   H2   sing N N 403 
VAL CA  C    sing N N 404 
VAL CA  CB   sing N N 405 
VAL CA  HA   sing N N 406 
VAL C   O    doub N N 407 
VAL C   OXT  sing N N 408 
VAL CB  CG1  sing N N 409 
VAL CB  CG2  sing N N 410 
VAL CB  HB   sing N N 411 
VAL CG1 HG11 sing N N 412 
VAL CG1 HG12 sing N N 413 
VAL CG1 HG13 sing N N 414 
VAL CG2 HG21 sing N N 415 
VAL CG2 HG22 sing N N 416 
VAL CG2 HG23 sing N N 417 
VAL OXT HXT  sing N N 418 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                     ZN  
3 '4-{[(5-nitro-6-oxo-1,6-dihydropyrimidin-4-yl)amino]methyl}benzenesulfonamide' J90 
4 'DIMETHYL SULFOXIDE'                                                           DMS 
5 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' 
# 
