data_3MHL
# 
_entry.id   3MHL 
# 
_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   3MHL         pdb_00003mhl 10.2210/pdb3mhl/pdb 
RCSB  RCSB058555   ?            ?                   
WWPDB D_1000058555 ?            ?                   
# 
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 3MHI '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                        3MHL 
_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           3MHL 
_cell.length_a           41.712 
_cell.length_b           40.677 
_cell.length_c           70.716 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.130 
_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                         3MHL 
_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 'DIMETHYL SULFOXIDE'                                                   78.133    2   ?       ? ? ? 
4 non-polymer syn '4-{[(6-methoxy-5-nitropyrimidin-4-yl)amino]methyl}benzenesulfonamide' 339.327   1   ?       ? ? ? 
5 water       nat water                                                                  18.015    117 ?       ? ? ? 
# 
_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              3MHL 
_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 
J71 non-polymer         . '4-{[(6-methoxy-5-nitropyrimidin-4-yl)amino]methyl}benzenesulfonamide' 
'4-{[N-(6-methoxy-5-nitropyrimidin-4-yl)amino]methyl}benzenesulfonamide' 'C12 H13 N5 O5 S' 339.327 
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          3MHL 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   38.08 
_exptl_crystal.density_Matthews      1.99 
_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               CCD 
_diffrn_detector.type                   'MARMOSAIC 225 mm CCD' 
_diffrn_detector.pdbx_collection_date   2009-12-15 
_diffrn_detector.details                'Vertically focussing mirror' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Double crystal Si(111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9720 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X12' 
_diffrn_source.pdbx_wavelength_list        0.9720 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X12 
# 
_reflns.entry_id                     3MHL 
_reflns.d_resolution_high            1.900 
_reflns.d_resolution_low             40.689 
_reflns.number_all                   18388 
_reflns.number_obs                   18388 
_reflns.pdbx_Rmerge_I_obs            0.076 
_reflns.pdbx_netI_over_sigmaI        37.900 
_reflns.pdbx_Rsym_value              0.076 
_reflns.pdbx_redundancy              15.300 
_reflns.percent_possible_obs         100.000 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        24.1 
_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             1.90 
_reflns_shell.d_res_low              2.00 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    30321 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.252 
_reflns_shell.meanI_over_sigI_obs    7.5 
_reflns_shell.pdbx_Rsym_value        0.252 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_redundancy        11.50 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      2642 
_reflns_shell.percent_possible_all   100.00 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3MHL 
_refine.ls_d_res_high                            1.900 
_refine.ls_d_res_low                             40.460 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    100.000 
_refine.ls_number_reflns_obs                     18377 
_refine.ls_number_reflns_all                     18377 
_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                          0.168 
_refine.ls_R_factor_obs                          0.168 
_refine.ls_R_factor_R_work                       0.162 
_refine.ls_wR_factor_R_work                      0.159 
_refine.ls_R_factor_R_free                       0.219 
_refine.ls_wR_factor_R_free                      0.211 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  1849 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               25.533 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             isotropic 
_refine.aniso_B[1][1]                            -0.310 
_refine.aniso_B[2][2]                            -1.430 
_refine.aniso_B[3][3]                            1.390 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.710 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.943 
_refine.overall_SU_R_Cruickshank_DPI             0.170 
_refine.overall_SU_R_free                        0.157 
_refine.pdbx_overall_ESU_R                       0.170 
_refine.pdbx_overall_ESU_R_Free                  0.157 
_refine.overall_SU_ML                            0.104 
_refine.overall_SU_B                             3.489 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.861 
_refine.B_iso_max                                66.50 
_refine.B_iso_min                                10.74 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.pdbx_ls_sigma_I                          0 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 2NNO' 
_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         32 
_refine_hist.number_atoms_solvent             117 
_refine_hist.number_atoms_total               2198 
_refine_hist.d_res_high                       1.900 
_refine_hist.d_res_low                        40.460 
# 
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         2142 0.023  0.022  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      2911 1.998  1.964  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   260  7.200  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   96   35.629 24.583 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   349  15.689 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   7    15.074 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           304  0.345  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     1653 0.011  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            1031 0.207  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          1415 0.321  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    138  0.150  0.200  ? 'X-RAY DIFFRACTION' ? 
r_metal_ion_refined      2    0.070  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   58   0.192  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 22   0.231  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              1326 1.483  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             2084 2.219  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              960  3.528  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             826  4.994  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.900 
_refine_ls_shell.d_res_low                        1.949 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               100.000 
_refine_ls_shell.number_reflns_R_work             1173 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.202 
_refine_ls_shell.R_factor_R_free                  0.270 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             174 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1347 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3MHL 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 4-{[N-(6-methoxy-5-nitropyrimidin-4-yl)amino]methyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3MHL 
_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 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 -1.47 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 8.64  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N VAL A 142 ? N VAL A 143 
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 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N LYS A 148 ? N LYS A 149 O VAL A 217 ? O VAL A 218 
# 
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 DMS 263 ? 4  'BINDING SITE FOR RESIDUE DMS A 263' 
AC3 Software A DMS 264 ? 5  'BINDING SITE FOR RESIDUE DMS A 264' 
AC4 Software A J71 265 ? 12 'BINDING SITE FOR RESIDUE J71 A 265' 
# 
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  J71 E .   ? J71 A 265 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  PRO A 246 ? PRO A 247 . ? 1_555 ? 
9  AC3 5  ASN A 62  ? ASN A 62  . ? 1_555 ? 
10 AC3 5  ASN A 67  ? ASN A 67  . ? 1_555 ? 
11 AC3 5  GLN A 92  ? GLN A 92  . ? 1_555 ? 
12 AC3 5  HIS A 94  ? HIS A 94  . ? 1_555 ? 
13 AC3 5  J71 E .   ? J71 A 265 . ? 1_555 ? 
14 AC4 12 ILE A 91  ? ILE A 91  . ? 1_555 ? 
15 AC4 12 GLN A 92  ? GLN A 92  . ? 1_555 ? 
16 AC4 12 HIS A 94  ? HIS A 94  . ? 1_555 ? 
17 AC4 12 HIS A 96  ? HIS A 96  . ? 1_555 ? 
18 AC4 12 HIS A 119 ? HIS A 119 . ? 1_555 ? 
19 AC4 12 PHE A 130 ? PHE A 131 . ? 1_555 ? 
20 AC4 12 LEU A 197 ? LEU A 198 . ? 1_555 ? 
21 AC4 12 THR A 198 ? THR A 199 . ? 1_555 ? 
22 AC4 12 THR A 199 ? THR A 200 . ? 1_555 ? 
23 AC4 12 TRP A 208 ? TRP A 209 . ? 1_555 ? 
24 AC4 12 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
25 AC4 12 DMS D .   ? DMS A 264 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3MHL 
_atom_sites.fract_transf_matrix[1][1]   0.023974 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006035 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024584 
_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]   0.014582 
_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   ? 10.536  -0.259  7.029   1.00 40.73 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 10.001  0.323   8.303   1.00 40.16 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.312   -0.713  9.236   1.00 37.51 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.635   -1.913  9.200   1.00 38.81 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 9.142   1.553   8.002   1.00 40.48 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 9.697   2.837   8.582   1.00 48.30 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 9.421   3.259   9.877   1.00 51.87 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 10.485  3.805   8.032   1.00 51.20 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 10.019  4.423   10.098  1.00 56.16 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 10.666  4.780   8.993   1.00 55.16 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.399   -0.288  10.099  1.00 33.89 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.806   -1.262  11.018  1.00 30.18 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.812   -2.108  10.255  1.00 28.24 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.285   -1.718  9.198   1.00 26.64 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 7.151   -0.607  12.248  1.00 28.11 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 5.953   0.173   11.877  1.00 29.12 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.893   1.506   11.474  1.00 27.16 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.619   -0.320  11.850  1.00 24.30 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.576   1.842   11.188  1.00 27.55 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.781   0.744   11.396  1.00 25.66 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 4.056   -1.575  12.111  1.00 25.91 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.371   0.612   11.281  1.00 26.97 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.634   -1.717  11.988  1.00 26.26 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.829   -0.626  11.576  1.00 26.55 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.591   -3.306  10.774  1.00 27.80 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.627   -4.179  10.168  1.00 28.13 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.317   -5.338  11.072  1.00 27.01 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.373   -5.215  12.268  1.00 25.19 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 5.023   -6.488  10.471  1.00 28.77 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.669   -7.652  11.269  1.00 27.68 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.522   -8.907  11.085  1.00 30.10 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.100   -9.993  11.502  1.00 28.92 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.202   -7.983  11.068  1.00 26.60 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.284   -6.952  11.647  1.00 21.23 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.914   -6.996  12.987  1.00 21.44 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.763   -5.964  10.828  1.00 21.26 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 1.043   -6.030  13.512  1.00 22.70 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.879   -5.001  11.310  1.00 22.96 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.542   -5.038  12.651  1.00 22.55 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.324  -4.069  13.142  1.00 23.53 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.710   -8.750  10.506  1.00 31.46 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.589   -9.897  10.224  1.00 33.19 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.516   -10.268 11.357  1.00 33.91 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.461   -9.701  12.472  1.00 34.01 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.423   -11.208 11.069  1.00 34.94 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.403  -11.651 12.085  1.00 36.06 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.357  -10.523 12.400  1.00 35.39 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.817  -10.387 13.561  1.00 35.89 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.158  -12.906 11.625  1.00 37.06 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 10.198  -14.111 11.396  1.00 40.17 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 10.409  -14.767 10.114  0.00 49.42 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 9.403   -15.904 9.999   0.00 48.29 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 9.922   -17.205 10.518  0.00 54.08 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 11.567  -9.671  11.389  1.00 35.08 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 12.613  -8.644  11.458  1.00 34.70 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 12.137  -7.192  11.720  1.00 34.21 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 12.943  -6.324  12.089  1.00 34.72 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 13.549  -8.777  10.241  1.00 34.40 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 14.249  -10.101 10.221  1.00 34.90 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 15.211  -10.441 11.157  1.00 37.20 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 14.058  -11.205 9.459   1.00 40.84 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 15.607  -11.683 10.946  1.00 36.22 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 14.915  -12.177 9.930   1.00 39.22 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 10.842  -6.944  11.578  1.00 32.46 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 10.302  -5.614  11.850  1.00 30.94 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 8.978   -5.669  12.638  1.00 30.62 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 8.237   -4.682  12.652  1.00 28.67 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 10.070  -4.892  10.540  1.00 30.26 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 9.064   -5.601  9.641   1.00 32.98 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 8.555   -6.680  9.950   1.00 37.26 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 8.800   -5.013  8.505   1.00 29.63 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 8.729   -6.814  13.290  1.00 29.58 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 7.405   -7.113  13.894  1.00 26.38 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 7.289   -6.554  15.269  1.00 26.37 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 8.193   -5.826  15.749  1.00 26.46 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 6.139   -6.833  15.934  1.00 24.90 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 5.873   -6.226  17.213  1.00 24.39 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 7.010   -6.228  18.222  1.00 24.64 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 7.162   -5.258  18.967  1.00 24.90 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 4.631   -7.020  17.721  1.00 22.98 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 3.956   -7.538  16.496  1.00 21.01 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 4.958   -7.570  15.391  1.00 24.33 ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 7.795   -7.323  18.284  1.00 24.09 ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 8.901   -7.437  19.241  1.00 26.15 ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 10.053  -6.416  18.904  1.00 23.98 ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 10.855  -6.094  19.742  1.00 25.81 ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 9.417   -8.900  19.218  1.00 27.85 ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 10.033  -9.279  17.864  1.00 31.78 ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 9.107   -9.797  16.708  1.00 40.14 ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 7.873   -9.561  16.678  1.00 34.52 ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 9.683   -10.429 15.751  1.00 44.13 ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 10.089  -5.920  17.692  1.00 22.81 ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 11.048  -4.902  17.294  1.00 23.26 ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 10.625  -3.458  17.510  1.00 24.39 ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 11.454  -2.521  17.427  1.00 24.21 ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 11.364  -5.116  15.831  1.00 25.22 ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 12.150  -6.373  15.604  1.00 31.83 ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 13.529  -6.420  15.697  1.00 36.01 ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 11.743  -7.651  15.398  1.00 37.11 ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 13.938  -7.662  15.482  1.00 38.09 ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 12.875  -8.431  15.315  1.00 37.04 ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 9.329   -3.229  17.732  1.00 22.18 ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 8.828   -1.866  17.664  1.00 21.41 ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 9.408   -0.924  18.680  1.00 19.94 ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 9.455   0.288   18.408  1.00 22.47 ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 7.267   -1.813  17.754  1.00 18.23 ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 6.613   -2.492  16.620  1.00 17.67 ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 7.151   -2.857  15.390  1.00 17.37 ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 5.201   -2.816  16.546  1.00 17.60 ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 6.191   -3.485  14.610  1.00 19.20 ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 4.976   -3.418  15.286  1.00 17.43 ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 4.134   -2.667  17.453  1.00 17.13 ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 3.710   -3.894  14.893  1.00 20.54 ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 2.879   -3.159  17.082  1.00 15.05 ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 2.680   -3.749  15.801  1.00 18.96 ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 9.838   -1.428  19.830  1.00 21.74 ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 10.179  -0.553  20.931  1.00 23.41 ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 11.443  0.266   20.566  1.00 24.47 ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 11.675  1.280   21.163  1.00 24.43 ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 10.441  -1.319  22.208  1.00 23.93 ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 11.639  -2.206  22.075  1.00 29.64 ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 12.882  -1.851  22.576  1.00 35.33 ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 11.822  -3.350  21.375  1.00 29.65 ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 13.763  -2.776  22.238  1.00 30.97 ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 13.154  -3.694  21.512  1.00 29.95 ? 17  HIS A NE2 1 
ATOM   126  N  N   . LYS A 1 18  ? 12.220  -0.205  19.597  1.00 24.91 ? 18  LYS A N   1 
ATOM   127  C  CA  . LYS A 1 18  ? 13.477  0.452   19.149  1.00 27.48 ? 18  LYS A CA  1 
ATOM   128  C  C   . LYS A 1 18  ? 13.225  1.798   18.466  1.00 27.65 ? 18  LYS A C   1 
ATOM   129  O  O   . LYS A 1 18  ? 13.892  2.769   18.747  1.00 30.26 ? 18  LYS A O   1 
ATOM   130  C  CB  . LYS A 1 18  ? 14.228  -0.489  18.195  1.00 26.30 ? 18  LYS A CB  1 
ATOM   131  C  CG  . LYS A 1 18  ? 14.889  -1.720  18.922  1.00 27.61 ? 18  LYS A CG  1 
ATOM   132  C  CD  . LYS A 1 18  ? 15.572  -2.606  17.938  1.00 26.61 ? 18  LYS A CD  1 
ATOM   133  C  CE  . LYS A 1 18  ? 14.634  -3.689  17.391  1.00 28.68 ? 18  LYS A CE  1 
ATOM   134  N  NZ  . LYS A 1 18  ? 15.257  -4.450  16.213  1.00 25.60 ? 18  LYS A NZ  1 
ATOM   135  N  N   . ASP A 1 19  ? 12.221  1.876   17.628  1.00 27.30 ? 19  ASP A N   1 
ATOM   136  C  CA  . ASP A 1 19  ? 11.770  3.170   17.096  1.00 28.16 ? 19  ASP A CA  1 
ATOM   137  C  C   . ASP A 1 19  ? 10.708  3.874   17.920  1.00 27.57 ? 19  ASP A C   1 
ATOM   138  O  O   . ASP A 1 19  ? 10.555  5.086   17.783  1.00 28.89 ? 19  ASP A O   1 
ATOM   139  C  CB  . ASP A 1 19  ? 11.352  3.058   15.625  1.00 27.63 ? 19  ASP A CB  1 
ATOM   140  C  CG  . ASP A 1 19  ? 12.551  2.922   14.708  1.00 31.75 ? 19  ASP A CG  1 
ATOM   141  O  OD1 . ASP A 1 19  ? 13.292  3.905   14.540  1.00 34.34 ? 19  ASP A OD1 1 
ATOM   142  O  OD2 . ASP A 1 19  ? 12.829  1.782   14.249  1.00 41.70 ? 19  ASP A OD2 1 
ATOM   143  N  N   . PHE A 1 20  ? 9.992   3.159   18.797  1.00 26.19 ? 20  PHE A N   1 
ATOM   144  C  CA  . PHE A 1 20  ? 8.878   3.752   19.538  1.00 26.03 ? 20  PHE A CA  1 
ATOM   145  C  C   . PHE A 1 20  ? 8.958   3.163   20.909  1.00 26.48 ? 20  PHE A C   1 
ATOM   146  O  O   . PHE A 1 20  ? 8.348   2.110   21.156  1.00 27.73 ? 20  PHE A O   1 
ATOM   147  C  CB  . PHE A 1 20  ? 7.488   3.447   18.872  1.00 25.11 ? 20  PHE A CB  1 
ATOM   148  C  CG  . PHE A 1 20  ? 7.457   3.727   17.417  1.00 23.80 ? 20  PHE A CG  1 
ATOM   149  C  CD1 . PHE A 1 20  ? 7.102   5.001   16.924  1.00 23.18 ? 20  PHE A CD1 1 
ATOM   150  C  CD2 . PHE A 1 20  ? 7.850   2.747   16.508  1.00 25.42 ? 20  PHE A CD2 1 
ATOM   151  C  CE1 . PHE A 1 20  ? 7.117   5.230   15.537  1.00 21.52 ? 20  PHE A CE1 1 
ATOM   152  C  CE2 . PHE A 1 20  ? 7.876   2.972   15.167  1.00 24.07 ? 20  PHE A CE2 1 
ATOM   153  C  CZ  . PHE A 1 20  ? 7.519   4.245   14.675  1.00 28.24 ? 20  PHE A CZ  1 
ATOM   154  N  N   . PRO A 1 21  ? 9.804   3.768   21.783  1.00 26.29 ? 21  PRO A N   1 
ATOM   155  C  CA  . PRO A 1 21  ? 10.028  3.301   23.112  1.00 25.64 ? 21  PRO A CA  1 
ATOM   156  C  C   . PRO A 1 21  ? 8.796   3.180   23.981  1.00 24.11 ? 21  PRO A C   1 
ATOM   157  O  O   . PRO A 1 21  ? 8.824   2.446   24.946  1.00 21.97 ? 21  PRO A O   1 
ATOM   158  C  CB  . PRO A 1 21  ? 11.071  4.322   23.680  1.00 27.19 ? 21  PRO A CB  1 
ATOM   159  C  CG  . PRO A 1 21  ? 11.893  4.597   22.468  1.00 28.14 ? 21  PRO A CG  1 
ATOM   160  C  CD  . PRO A 1 21  ? 10.753  4.858   21.450  1.00 26.67 ? 21  PRO A CD  1 
ATOM   161  N  N   . ILE A 1 22  ? 7.753   3.949   23.672  1.00 23.13 ? 22  ILE A N   1 
ATOM   162  C  CA  . ILE A 1 22  ? 6.466   3.838   24.401  1.00 22.34 ? 22  ILE A CA  1 
ATOM   163  C  C   . ILE A 1 22  ? 5.880   2.397   24.309  1.00 21.43 ? 22  ILE A C   1 
ATOM   164  O  O   . ILE A 1 22  ? 5.038   1.998   25.144  1.00 21.90 ? 22  ILE A O   1 
ATOM   165  C  CB  . ILE A 1 22  ? 5.492   4.948   23.935  1.00 20.35 ? 22  ILE A CB  1 
ATOM   166  C  CG1 . ILE A 1 22  ? 4.357   5.208   24.912  1.00 22.37 ? 22  ILE A CG1 1 
ATOM   167  C  CG2 . ILE A 1 22  ? 4.849   4.576   22.655  1.00 24.24 ? 22  ILE A CG2 1 
ATOM   168  C  CD1 . ILE A 1 22  ? 4.734   5.635   26.253  1.00 26.36 ? 22  ILE A CD1 1 
ATOM   169  N  N   . ALA A 1 23  ? 6.385   1.605   23.354  1.00 21.27 ? 23  ALA A N   1 
ATOM   170  C  CA  . ALA A 1 23  ? 6.038   0.161   23.273  1.00 22.17 ? 23  ALA A CA  1 
ATOM   171  C  C   . ALA A 1 23  ? 6.145   -0.557  24.601  1.00 23.53 ? 23  ALA A C   1 
ATOM   172  O  O   . ALA A 1 23  ? 5.425   -1.539  24.865  1.00 23.59 ? 23  ALA A O   1 
ATOM   173  C  CB  . ALA A 1 23  ? 6.901   -0.566  22.171  1.00 19.20 ? 23  ALA A CB  1 
ATOM   174  N  N   . LYS A 1 24  ? 7.055   -0.091  25.469  1.00 24.96 ? 24  LYS A N   1 
ATOM   175  C  CA  . LYS A 1 24  ? 7.222   -0.712  26.760  1.00 27.54 ? 24  LYS A CA  1 
ATOM   176  C  C   . LYS A 1 24  ? 6.597   0.142   27.847  1.00 28.31 ? 24  LYS A C   1 
ATOM   177  O  O   . LYS A 1 24  ? 6.915   -0.024  28.999  1.00 29.97 ? 24  LYS A O   1 
ATOM   178  C  CB  . LYS A 1 24  ? 8.726   -0.984  27.030  1.00 27.81 ? 24  LYS A CB  1 
ATOM   179  C  CG  . LYS A 1 24  ? 9.330   -1.793  25.890  1.00 29.59 ? 24  LYS A CG  1 
ATOM   180  C  CD  . LYS A 1 24  ? 10.804  -2.095  26.135  1.00 32.39 ? 24  LYS A CD  1 
ATOM   181  C  CE  . LYS A 1 24  ? 11.261  -3.310  25.242  1.00 32.88 ? 24  LYS A CE  1 
ATOM   182  N  NZ  . LYS A 1 24  ? 11.090  -4.595  26.032  1.00 31.26 ? 24  LYS A NZ  1 
ATOM   183  N  N   . GLY A 1 25  ? 5.666   1.027   27.491  1.00 29.22 ? 25  GLY A N   1 
ATOM   184  C  CA  . GLY A 1 25  ? 5.116   1.967   28.437  1.00 27.43 ? 25  GLY A CA  1 
ATOM   185  C  C   . GLY A 1 25  ? 4.091   1.348   29.344  1.00 28.15 ? 25  GLY A C   1 
ATOM   186  O  O   . GLY A 1 25  ? 3.825   0.118   29.306  1.00 27.86 ? 25  GLY A O   1 
ATOM   187  N  N   . GLU A 1 26  ? 3.537   2.210   30.181  1.00 27.32 ? 26  GLU A N   1 
ATOM   188  C  CA  . GLU A 1 26  ? 2.623   1.805   31.202  1.00 28.02 ? 26  GLU A CA  1 
ATOM   189  C  C   . GLU A 1 26  ? 1.164   1.510   30.766  1.00 25.26 ? 26  GLU A C   1 
ATOM   190  O  O   . GLU A 1 26  ? 0.423   0.962   31.562  1.00 25.52 ? 26  GLU A O   1 
ATOM   191  C  CB  . GLU A 1 26  ? 2.579   2.871   32.333  1.00 29.66 ? 26  GLU A CB  1 
ATOM   192  C  CG  . GLU A 1 26  ? 3.868   3.035   33.258  1.00 36.31 ? 26  GLU A CG  1 
ATOM   193  C  CD  . GLU A 1 26  ? 4.631   1.714   33.566  1.00 46.59 ? 26  GLU A CD  1 
ATOM   194  O  OE1 . GLU A 1 26  ? 4.082   0.777   34.247  1.00 46.21 ? 26  GLU A OE1 1 
ATOM   195  O  OE2 . GLU A 1 26  ? 5.820   1.634   33.110  1.00 48.01 ? 26  GLU A OE2 1 
ATOM   196  N  N   . ARG A 1 27  ? 0.733   1.897   29.561  1.00 23.96 ? 27  ARG A N   1 
ATOM   197  C  CA  . ARG A 1 27  ? -0.689  1.715   29.178  1.00 22.88 ? 27  ARG A CA  1 
ATOM   198  C  C   . ARG A 1 27  ? -0.785  1.254   27.728  1.00 21.53 ? 27  ARG A C   1 
ATOM   199  O  O   . ARG A 1 27  ? -1.504  1.852   26.898  1.00 20.03 ? 27  ARG A O   1 
ATOM   200  C  CB  . ARG A 1 27  ? -1.589  2.911   29.531  1.00 23.90 ? 27  ARG A CB  1 
ATOM   201  C  CG  . ARG A 1 27  ? -1.305  4.196   28.773  1.00 26.95 ? 27  ARG A CG  1 
ATOM   202  C  CD  . ARG A 1 27  ? -2.239  5.428   29.072  1.00 30.03 ? 27  ARG A CD  1 
ATOM   203  N  NE  . ARG A 1 27  ? -3.504  5.303   28.328  1.00 29.61 ? 27  ARG A NE  1 
ATOM   204  C  CZ  . ARG A 1 27  ? -4.357  6.286   28.003  1.00 29.36 ? 27  ARG A CZ  1 
ATOM   205  N  NH1 . ARG A 1 27  ? -4.186  7.575   28.299  1.00 23.64 ? 27  ARG A NH1 1 
ATOM   206  N  NH2 . ARG A 1 27  ? -5.391  5.961   27.322  1.00 25.08 ? 27  ARG A NH2 1 
ATOM   207  N  N   . GLN A 1 28  ? -0.055  0.169   27.428  1.00 17.86 ? 28  GLN A N   1 
ATOM   208  C  CA  . GLN A 1 28  ? 0.011   -0.384  26.091  1.00 16.81 ? 28  GLN A CA  1 
ATOM   209  C  C   . GLN A 1 28  ? -1.132  -1.393  25.783  1.00 14.83 ? 28  GLN A C   1 
ATOM   210  O  O   . GLN A 1 28  ? -1.644  -2.123  26.664  1.00 16.03 ? 28  GLN A O   1 
ATOM   211  C  CB  . GLN A 1 28  ? 1.356   -1.081  25.904  1.00 19.00 ? 28  GLN A CB  1 
ATOM   212  C  CG  . GLN A 1 28  ? 2.539   -0.068  25.657  1.00 16.75 ? 28  GLN A CG  1 
ATOM   213  C  CD  . GLN A 1 28  ? 2.345   0.766   24.394  1.00 19.58 ? 28  GLN A CD  1 
ATOM   214  O  OE1 . GLN A 1 28  ? 2.529   0.262   23.304  1.00 23.18 ? 28  GLN A OE1 1 
ATOM   215  N  NE2 . GLN A 1 28  ? 1.997   2.053   24.533  1.00 18.50 ? 28  GLN A NE2 1 
ATOM   216  N  N   . SER A 1 29  ? -1.513  -1.393  24.531  1.00 16.02 ? 29  SER A N   1 
ATOM   217  C  CA  . SER A 1 29  ? -2.573  -2.254  24.039  1.00 17.40 ? 29  SER A CA  1 
ATOM   218  C  C   . SER A 1 29  ? -2.031  -3.129  22.918  1.00 16.74 ? 29  SER A C   1 
ATOM   219  O  O   . SER A 1 29  ? -1.118  -2.721  22.204  1.00 17.54 ? 29  SER A O   1 
ATOM   220  C  CB  . SER A 1 29  ? -3.771  -1.457  23.532  1.00 16.80 ? 29  SER A CB  1 
ATOM   221  O  OG  . SER A 1 29  ? -4.350  -0.772  24.622  1.00 18.28 ? 29  SER A OG  1 
ATOM   222  N  N   . PRO A 1 30  ? -2.682  -4.286  22.680  1.00 17.98 ? 30  PRO A N   1 
ATOM   223  C  CA  . PRO A 1 30  ? -3.836  -4.824  23.389  1.00 16.76 ? 30  PRO A CA  1 
ATOM   224  C  C   . PRO A 1 30  ? -3.426  -5.515  24.654  1.00 18.39 ? 30  PRO A C   1 
ATOM   225  O  O   . PRO A 1 30  ? -2.211  -5.552  24.956  1.00 17.59 ? 30  PRO A O   1 
ATOM   226  C  CB  . PRO A 1 30  ? -4.344  -5.876  22.445  1.00 16.98 ? 30  PRO A CB  1 
ATOM   227  C  CG  . PRO A 1 30  ? -3.046  -6.436  21.774  1.00 15.82 ? 30  PRO A CG  1 
ATOM   228  C  CD  . PRO A 1 30  ? -2.269  -5.125  21.536  1.00 17.88 ? 30  PRO A CD  1 
ATOM   229  N  N   . VAL A 1 31  ? -4.432  -6.076  25.351  1.00 17.51 ? 31  VAL A N   1 
ATOM   230  C  CA  . VAL A 1 31  ? -4.271  -6.806  26.569  1.00 18.16 ? 31  VAL A CA  1 
ATOM   231  C  C   . VAL A 1 31  ? -5.138  -8.031  26.567  1.00 19.28 ? 31  VAL A C   1 
ATOM   232  O  O   . VAL A 1 31  ? -6.086  -8.162  25.770  1.00 16.66 ? 31  VAL A O   1 
ATOM   233  C  CB  . VAL A 1 31  ? -4.569  -5.978  27.844  1.00 19.20 ? 31  VAL A CB  1 
ATOM   234  C  CG1 . VAL A 1 31  ? -3.605  -4.760  27.914  1.00 19.36 ? 31  VAL A CG1 1 
ATOM   235  C  CG2 . VAL A 1 31  ? -6.049  -5.557  27.926  1.00 17.35 ? 31  VAL A CG2 1 
ATOM   236  N  N   . ASP A 1 32  ? -4.804  -8.964  27.470  1.00 19.34 ? 32  ASP A N   1 
ATOM   237  C  CA  . ASP A 1 32  ? -5.685  -10.070 27.647  1.00 19.95 ? 32  ASP A CA  1 
ATOM   238  C  C   . ASP A 1 32  ? -6.806  -9.583  28.563  1.00 19.45 ? 32  ASP A C   1 
ATOM   239  O  O   . ASP A 1 32  ? -6.532  -8.978  29.552  1.00 20.68 ? 32  ASP A O   1 
ATOM   240  C  CB  . ASP A 1 32  ? -4.973  -11.274 28.259  1.00 20.37 ? 32  ASP A CB  1 
ATOM   241  C  CG  . ASP A 1 32  ? -5.973  -12.419 28.542  1.00 24.50 ? 32  ASP A CG  1 
ATOM   242  O  OD1 . ASP A 1 32  ? -6.671  -12.843 27.561  1.00 22.87 ? 32  ASP A OD1 1 
ATOM   243  O  OD2 . ASP A 1 32  ? -6.104  -12.810 29.727  1.00 24.48 ? 32  ASP A OD2 1 
ATOM   244  N  N   . ILE A 1 33  ? -8.048  -9.839  28.209  1.00 20.02 ? 33  ILE A N   1 
ATOM   245  C  CA  . ILE A 1 33  ? -9.172  -9.553  29.075  1.00 21.61 ? 33  ILE A CA  1 
ATOM   246  C  C   . ILE A 1 33  ? -9.515  -10.764 29.886  1.00 22.44 ? 33  ILE A C   1 
ATOM   247  O  O   . ILE A 1 33  ? -10.035 -11.755 29.392  1.00 23.56 ? 33  ILE A O   1 
ATOM   248  C  CB  . ILE A 1 33  ? -10.385 -9.070  28.292  1.00 21.40 ? 33  ILE A CB  1 
ATOM   249  C  CG1 . ILE A 1 33  ? -9.989  -7.791  27.534  1.00 20.10 ? 33  ILE A CG1 1 
ATOM   250  C  CG2 . ILE A 1 33  ? -11.602 -8.756  29.259  1.00 21.89 ? 33  ILE A CG2 1 
ATOM   251  C  CD1 . ILE A 1 33  ? -11.017 -7.495  26.455  1.00 18.95 ? 33  ILE A CD1 1 
ATOM   252  N  N   . ASP A 1 34  ? -9.168  -10.660 31.135  1.00 22.85 ? 34  ASP A N   1 
ATOM   253  C  CA  . ASP A 1 34  ? -9.434  -11.722 32.115  1.00 26.78 ? 34  ASP A CA  1 
ATOM   254  C  C   . ASP A 1 34  ? -10.882 -11.462 32.666  1.00 26.03 ? 34  ASP A C   1 
ATOM   255  O  O   . ASP A 1 34  ? -11.102 -10.576 33.512  1.00 26.40 ? 34  ASP A O   1 
ATOM   256  C  CB  . ASP A 1 34  ? -8.321  -11.711 33.180  1.00 25.50 ? 34  ASP A CB  1 
ATOM   257  C  CG  . ASP A 1 34  ? -8.580  -12.684 34.355  1.00 32.85 ? 34  ASP A CG  1 
ATOM   258  O  OD1 . ASP A 1 34  ? -9.640  -13.376 34.438  1.00 32.03 ? 34  ASP A OD1 1 
ATOM   259  O  OD2 . ASP A 1 34  ? -7.692  -12.700 35.242  1.00 41.49 ? 34  ASP A OD2 1 
ATOM   260  N  N   . THR A 1 35  ? -11.848 -12.207 32.145  1.00 25.46 ? 35  THR A N   1 
ATOM   261  C  CA  . THR A 1 35  ? -13.258 -11.865 32.352  1.00 29.16 ? 35  THR A CA  1 
ATOM   262  C  C   . THR A 1 35  ? -13.681 -12.067 33.772  1.00 30.77 ? 35  THR A C   1 
ATOM   263  O  O   . THR A 1 35  ? -14.745 -11.616 34.161  1.00 32.06 ? 35  THR A O   1 
ATOM   264  C  CB  . THR A 1 35  ? -14.238 -12.690 31.464  1.00 29.53 ? 35  THR A CB  1 
ATOM   265  O  OG1 . THR A 1 35  ? -14.257 -14.071 31.899  1.00 31.38 ? 35  THR A OG1 1 
ATOM   266  C  CG2 . THR A 1 35  ? -13.805 -12.625 30.030  1.00 30.47 ? 35  THR A CG2 1 
ATOM   267  N  N   . HIS A 1 36  ? -12.860 -12.768 34.547  1.00 32.43 ? 36  HIS A N   1 
ATOM   268  C  CA  . HIS A 1 36  ? -13.197 -13.053 35.923  1.00 33.32 ? 36  HIS A CA  1 
ATOM   269  C  C   . HIS A 1 36  ? -12.650 -11.983 36.803  1.00 34.16 ? 36  HIS A C   1 
ATOM   270  O  O   . HIS A 1 36  ? -13.309 -11.614 37.770  1.00 36.82 ? 36  HIS A O   1 
ATOM   271  C  CB  . HIS A 1 36  ? -12.718 -14.458 36.338  1.00 34.18 ? 36  HIS A CB  1 
ATOM   272  C  CG  . HIS A 1 36  ? -13.229 -15.544 35.444  1.00 32.15 ? 36  HIS A CG  1 
ATOM   273  N  ND1 . HIS A 1 36  ? -14.548 -15.928 35.422  1.00 34.34 ? 36  HIS A ND1 1 
ATOM   274  C  CD2 . HIS A 1 36  ? -12.608 -16.265 34.477  1.00 32.72 ? 36  HIS A CD2 1 
ATOM   275  C  CE1 . HIS A 1 36  ? -14.715 -16.867 34.504  1.00 31.12 ? 36  HIS A CE1 1 
ATOM   276  N  NE2 . HIS A 1 36  ? -13.546 -17.088 33.925  1.00 33.05 ? 36  HIS A NE2 1 
ATOM   277  N  N   . THR A 1 37  ? -11.523 -11.402 36.453  1.00 32.27 ? 37  THR A N   1 
ATOM   278  C  CA  . THR A 1 37  ? -11.029 -10.260 37.231  1.00 32.71 ? 37  THR A CA  1 
ATOM   279  C  C   . THR A 1 37  ? -11.457 -8.839  36.715  1.00 30.73 ? 37  THR A C   1 
ATOM   280  O  O   . THR A 1 37  ? -11.144 -7.826  37.340  1.00 31.42 ? 37  THR A O   1 
ATOM   281  C  CB  . THR A 1 37  ? -9.506  -10.337 37.482  1.00 32.23 ? 37  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 37  ? -8.845  -10.184 36.242  1.00 37.04 ? 37  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 37  ? -9.135  -11.659 38.127  1.00 34.50 ? 37  THR A CG2 1 
ATOM   284  N  N   . ALA A 1 38  ? -12.200 -8.768  35.618  1.00 29.39 ? 38  ALA A N   1 
ATOM   285  C  CA  . ALA A 1 38  ? -12.788 -7.482  35.222  1.00 29.49 ? 38  ALA A CA  1 
ATOM   286  C  C   . ALA A 1 38  ? -13.826 -7.024  36.276  1.00 29.70 ? 38  ALA A C   1 
ATOM   287  O  O   . ALA A 1 38  ? -14.591 -7.837  36.787  1.00 29.16 ? 38  ALA A O   1 
ATOM   288  C  CB  . ALA A 1 38  ? -13.396 -7.584  33.852  1.00 26.94 ? 38  ALA A CB  1 
ATOM   289  N  N   . LYS A 1 39  ? -13.836 -5.739  36.602  1.00 29.51 ? 39  LYS A N   1 
ATOM   290  C  CA  . LYS A 1 39  ? -14.720 -5.263  37.639  1.00 29.98 ? 39  LYS A CA  1 
ATOM   291  C  C   . LYS A 1 39  ? -16.034 -4.771  37.022  1.00 31.38 ? 39  LYS A C   1 
ATOM   292  O  O   . LYS A 1 39  ? -16.065 -3.805  36.184  1.00 28.38 ? 39  LYS A O   1 
ATOM   293  C  CB  . LYS A 1 39  ? -14.088 -4.164  38.490  1.00 31.40 ? 39  LYS A CB  1 
ATOM   294  C  CG  . LYS A 1 39  ? -14.789 -4.076  39.894  1.00 33.09 ? 39  LYS A CG  1 
ATOM   295  C  CD  . LYS A 1 39  ? -14.651 -2.740  40.591  1.00 39.44 ? 39  LYS A CD  1 
ATOM   296  C  CE  . LYS A 1 39  ? -15.900 -2.390  41.469  1.00 38.23 ? 39  LYS A CE  1 
ATOM   297  N  NZ  . LYS A 1 39  ? -16.284 -3.463  42.485  1.00 40.51 ? 39  LYS A NZ  1 
ATOM   298  N  N   . TYR A 1 40  ? -17.122 -5.413  37.444  1.00 32.00 ? 40  TYR A N   1 
ATOM   299  C  CA  . TYR A 1 40  ? -18.434 -4.886  37.058  1.00 35.25 ? 40  TYR A CA  1 
ATOM   300  C  C   . TYR A 1 40  ? -18.622 -3.492  37.645  1.00 35.11 ? 40  TYR A C   1 
ATOM   301  O  O   . TYR A 1 40  ? -18.297 -3.239  38.815  1.00 35.52 ? 40  TYR A O   1 
ATOM   302  C  CB  . TYR A 1 40  ? -19.567 -5.873  37.363  1.00 36.95 ? 40  TYR A CB  1 
ATOM   303  C  CG  . TYR A 1 40  ? -20.915 -5.239  37.244  1.00 39.72 ? 40  TYR A CG  1 
ATOM   304  C  CD1 . TYR A 1 40  ? -21.381 -4.787  36.007  1.00 40.66 ? 40  TYR A CD1 1 
ATOM   305  C  CD2 . TYR A 1 40  ? -21.724 -5.064  38.369  1.00 41.54 ? 40  TYR A CD2 1 
ATOM   306  C  CE1 . TYR A 1 40  ? -22.617 -4.175  35.877  1.00 41.88 ? 40  TYR A CE1 1 
ATOM   307  C  CE2 . TYR A 1 40  ? -22.992 -4.442  38.256  1.00 44.97 ? 40  TYR A CE2 1 
ATOM   308  C  CZ  . TYR A 1 40  ? -23.426 -4.000  37.006  1.00 43.20 ? 40  TYR A CZ  1 
ATOM   309  O  OH  . TYR A 1 40  ? -24.662 -3.406  36.868  1.00 42.44 ? 40  TYR A OH  1 
ATOM   310  N  N   . ASP A 1 41  ? -19.025 -2.557  36.793  1.00 35.13 ? 41  ASP A N   1 
ATOM   311  C  CA  . ASP A 1 41  ? -19.248 -1.206  37.241  1.00 37.15 ? 41  ASP A CA  1 
ATOM   312  C  C   . ASP A 1 41  ? -20.689 -0.694  36.885  1.00 38.11 ? 41  ASP A C   1 
ATOM   313  O  O   . ASP A 1 41  ? -20.897 -0.136  35.800  1.00 37.80 ? 41  ASP A O   1 
ATOM   314  C  CB  . ASP A 1 41  ? -18.173 -0.268  36.700  1.00 36.03 ? 41  ASP A CB  1 
ATOM   315  C  CG  . ASP A 1 41  ? -18.267 1.130   37.315  1.00 38.77 ? 41  ASP A CG  1 
ATOM   316  O  OD1 . ASP A 1 41  ? -19.239 1.367   38.097  1.00 41.24 ? 41  ASP A OD1 1 
ATOM   317  O  OD2 . ASP A 1 41  ? -17.380 1.975   37.028  1.00 39.51 ? 41  ASP A OD2 1 
ATOM   318  N  N   . PRO A 1 42  ? -21.690 -0.929  37.788  1.00 38.95 ? 42  PRO A N   1 
ATOM   319  C  CA  . PRO A 1 42  ? -23.061 -0.406  37.589  1.00 39.36 ? 42  PRO A CA  1 
ATOM   320  C  C   . PRO A 1 42  ? -23.146 1.121   37.378  1.00 39.79 ? 42  PRO A C   1 
ATOM   321  O  O   . PRO A 1 42  ? -24.205 1.623   36.972  1.00 40.90 ? 42  PRO A O   1 
ATOM   322  C  CB  . PRO A 1 42  ? -23.800 -0.828  38.880  1.00 40.04 ? 42  PRO A CB  1 
ATOM   323  C  CG  . PRO A 1 42  ? -22.649 -1.153  39.905  1.00 40.71 ? 42  PRO A CG  1 
ATOM   324  C  CD  . PRO A 1 42  ? -21.584 -1.732  39.026  1.00 38.73 ? 42  PRO A CD  1 
ATOM   325  N  N   . SER A 1 43  ? -22.051 1.846   37.625  1.00 40.04 ? 43  SER A N   1 
ATOM   326  C  CA  . SER A 1 43  ? -21.981 3.265   37.271  1.00 40.27 ? 43  SER A CA  1 
ATOM   327  C  C   . SER A 1 43  ? -21.718 3.553   35.771  1.00 40.47 ? 43  SER A C   1 
ATOM   328  O  O   . SER A 1 43  ? -21.799 4.714   35.330  1.00 41.23 ? 43  SER A O   1 
ATOM   329  C  CB  . SER A 1 43  ? -20.918 3.940   38.124  1.00 41.38 ? 43  SER A CB  1 
ATOM   330  O  OG  . SER A 1 43  ? -20.191 4.911   37.381  1.00 43.98 ? 43  SER A OG  1 
ATOM   331  N  N   . LEU A 1 44  ? -21.356 2.527   34.993  1.00 38.53 ? 44  LEU A N   1 
ATOM   332  C  CA  . LEU A 1 44  ? -21.004 2.719   33.583  1.00 36.45 ? 44  LEU A CA  1 
ATOM   333  C  C   . LEU A 1 44  ? -22.279 2.884   32.765  1.00 36.11 ? 44  LEU A C   1 
ATOM   334  O  O   . LEU A 1 44  ? -23.223 2.120   32.933  1.00 36.74 ? 44  LEU A O   1 
ATOM   335  C  CB  . LEU A 1 44  ? -20.193 1.516   33.072  1.00 35.30 ? 44  LEU A CB  1 
ATOM   336  C  CG  . LEU A 1 44  ? -18.697 1.477   33.313  1.00 31.67 ? 44  LEU A CG  1 
ATOM   337  C  CD1 . LEU A 1 44  ? -18.242 0.080   32.890  1.00 28.56 ? 44  LEU A CD1 1 
ATOM   338  C  CD2 . LEU A 1 44  ? -18.066 2.540   32.456  1.00 29.63 ? 44  LEU A CD2 1 
ATOM   339  N  N   . LYS A 1 45  ? -22.293 3.866   31.870  1.00 36.14 ? 45  LYS A N   1 
ATOM   340  C  CA  . LYS A 1 45  ? -23.459 4.153   31.037  1.00 36.23 ? 45  LYS A CA  1 
ATOM   341  C  C   . LYS A 1 45  ? -23.492 3.219   29.859  1.00 35.66 ? 45  LYS A C   1 
ATOM   342  O  O   . LYS A 1 45  ? -22.437 2.599   29.511  1.00 35.75 ? 45  LYS A O   1 
ATOM   343  C  CB  . LYS A 1 45  ? -23.466 5.614   30.614  1.00 36.53 ? 45  LYS A CB  1 
ATOM   344  C  CG  . LYS A 1 45  ? -23.601 6.527   31.857  1.00 40.74 ? 45  LYS A CG  1 
ATOM   345  C  CD  . LYS A 1 45  ? -23.690 8.010   31.551  1.00 46.88 ? 45  LYS A CD  1 
ATOM   346  C  CE  . LYS A 1 45  ? -22.430 8.512   30.848  1.00 52.69 ? 45  LYS A CE  1 
ATOM   347  N  NZ  . LYS A 1 45  ? -21.446 9.189   31.747  1.00 51.68 ? 45  LYS A NZ  1 
ATOM   348  N  N   . PRO A 1 46  ? -24.696 3.014   29.290  1.00 34.41 ? 46  PRO A N   1 
ATOM   349  C  CA  . PRO A 1 46  ? -24.683 2.241   28.061  1.00 33.59 ? 46  PRO A CA  1 
ATOM   350  C  C   . PRO A 1 46  ? -23.864 3.033   27.052  1.00 33.13 ? 46  PRO A C   1 
ATOM   351  O  O   . PRO A 1 46  ? -23.807 4.282   27.135  1.00 32.38 ? 46  PRO A O   1 
ATOM   352  C  CB  . PRO A 1 46  ? -26.169 2.195   27.646  1.00 32.54 ? 46  PRO A CB  1 
ATOM   353  C  CG  . PRO A 1 46  ? -26.919 2.383   28.898  1.00 34.96 ? 46  PRO A CG  1 
ATOM   354  C  CD  . PRO A 1 46  ? -26.076 3.369   29.694  1.00 34.38 ? 46  PRO A CD  1 
ATOM   355  N  N   . LEU A 1 47  ? -23.209 2.317   26.150  1.00 32.17 ? 47  LEU A N   1 
ATOM   356  C  CA  . LEU A 1 47  ? -22.553 2.928   25.035  1.00 32.24 ? 47  LEU A CA  1 
ATOM   357  C  C   . LEU A 1 47  ? -23.638 3.569   24.168  1.00 32.84 ? 47  LEU A C   1 
ATOM   358  O  O   . LEU A 1 47  ? -24.698 2.988   23.990  1.00 30.62 ? 47  LEU A O   1 
ATOM   359  C  CB  . LEU A 1 47  ? -21.902 1.862   24.170  1.00 32.73 ? 47  LEU A CB  1 
ATOM   360  C  CG  . LEU A 1 47  ? -20.415 1.722   24.110  1.00 35.48 ? 47  LEU A CG  1 
ATOM   361  C  CD1 . LEU A 1 47  ? -20.174 0.661   23.045  1.00 39.16 ? 47  LEU A CD1 1 
ATOM   362  C  CD2 . LEU A 1 47  ? -19.701 3.052   23.790  1.00 39.16 ? 47  LEU A CD2 1 
ATOM   363  N  N   . SER A 1 48  ? -23.365 4.755   23.636  1.00 31.68 ? 48  SER A N   1 
ATOM   364  C  CA  . SER A 1 48  ? -24.220 5.310   22.623  1.00 32.97 ? 48  SER A CA  1 
ATOM   365  C  C   . SER A 1 48  ? -23.441 5.308   21.308  1.00 32.09 ? 48  SER A C   1 
ATOM   366  O  O   . SER A 1 48  ? -22.499 6.043   21.165  1.00 32.50 ? 48  SER A O   1 
ATOM   367  C  CB  . SER A 1 48  ? -24.658 6.716   23.018  1.00 32.66 ? 48  SER A CB  1 
ATOM   368  O  OG  . SER A 1 48  ? -25.226 7.370   21.890  1.00 37.70 ? 48  SER A OG  1 
ATOM   369  N  N   . VAL A 1 49  ? -23.838 4.454   20.386  1.00 31.63 ? 49  VAL A N   1 
ATOM   370  C  CA  . VAL A 1 49  ? -23.242 4.369   19.045  1.00 32.03 ? 49  VAL A CA  1 
ATOM   371  C  C   . VAL A 1 49  ? -24.226 5.022   18.097  1.00 32.05 ? 49  VAL A C   1 
ATOM   372  O  O   . VAL A 1 49  ? -25.315 4.518   17.882  1.00 33.29 ? 49  VAL A O   1 
ATOM   373  C  CB  . VAL A 1 49  ? -23.032 2.908   18.620  1.00 32.51 ? 49  VAL A CB  1 
ATOM   374  C  CG1 . VAL A 1 49  ? -22.199 2.825   17.324  1.00 31.71 ? 49  VAL A CG1 1 
ATOM   375  C  CG2 . VAL A 1 49  ? -22.337 2.118   19.751  1.00 33.35 ? 49  VAL A CG2 1 
ATOM   376  N  N   . SER A 1 50  ? -23.855 6.173   17.559  1.00 30.73 ? 50  SER A N   1 
ATOM   377  C  CA  . SER A 1 50  ? -24.730 6.918   16.698  1.00 29.70 ? 50  SER A CA  1 
ATOM   378  C  C   . SER A 1 50  ? -24.185 6.986   15.318  1.00 28.01 ? 50  SER A C   1 
ATOM   379  O  O   . SER A 1 50  ? -23.479 7.893   15.021  1.00 27.31 ? 50  SER A O   1 
ATOM   380  C  CB  . SER A 1 50  ? -24.891 8.342   17.212  1.00 30.48 ? 50  SER A CB  1 
ATOM   381  O  OG  . SER A 1 50  ? -25.909 8.393   18.170  1.00 32.73 ? 50  SER A OG  1 
ATOM   382  N  N   . TYR A 1 51  ? -24.552 6.020   14.477  1.00 27.61 ? 51  TYR A N   1 
ATOM   383  C  CA  . TYR A 1 51  ? -23.922 5.796   13.175  1.00 28.05 ? 51  TYR A CA  1 
ATOM   384  C  C   . TYR A 1 51  ? -24.895 6.027   11.990  1.00 27.72 ? 51  TYR A C   1 
ATOM   385  O  O   . TYR A 1 51  ? -24.519 5.842   10.816  1.00 27.94 ? 51  TYR A O   1 
ATOM   386  C  CB  . TYR A 1 51  ? -23.351 4.364   13.131  1.00 25.76 ? 51  TYR A CB  1 
ATOM   387  C  CG  . TYR A 1 51  ? -22.045 4.118   13.871  1.00 26.74 ? 51  TYR A CG  1 
ATOM   388  C  CD1 . TYR A 1 51  ? -21.340 5.141   14.515  1.00 21.12 ? 51  TYR A CD1 1 
ATOM   389  C  CD2 . TYR A 1 51  ? -21.481 2.836   13.881  1.00 23.64 ? 51  TYR A CD2 1 
ATOM   390  C  CE1 . TYR A 1 51  ? -20.094 4.875   15.149  1.00 23.14 ? 51  TYR A CE1 1 
ATOM   391  C  CE2 . TYR A 1 51  ? -20.284 2.576   14.470  1.00 24.53 ? 51  TYR A CE2 1 
ATOM   392  C  CZ  . TYR A 1 51  ? -19.601 3.580   15.131  1.00 24.23 ? 51  TYR A CZ  1 
ATOM   393  O  OH  . TYR A 1 51  ? -18.428 3.262   15.736  1.00 23.43 ? 51  TYR A OH  1 
ATOM   394  N  N   . ASP A 1 52  ? -26.137 6.435   12.301  1.00 29.93 ? 52  ASP A N   1 
ATOM   395  C  CA  . ASP A 1 52  ? -27.154 6.763   11.265  1.00 31.86 ? 52  ASP A CA  1 
ATOM   396  C  C   . ASP A 1 52  ? -26.645 7.659   10.145  1.00 31.14 ? 52  ASP A C   1 
ATOM   397  O  O   . ASP A 1 52  ? -26.961 7.435   8.986   1.00 33.04 ? 52  ASP A O   1 
ATOM   398  C  CB  . ASP A 1 52  ? -28.434 7.366   11.863  1.00 33.00 ? 52  ASP A CB  1 
ATOM   399  C  CG  . ASP A 1 52  ? -28.193 8.108   13.168  1.00 38.78 ? 52  ASP A CG  1 
ATOM   400  O  OD1 . ASP A 1 52  ? -27.534 7.517   14.092  1.00 45.30 ? 52  ASP A OD1 1 
ATOM   401  O  OD2 . ASP A 1 52  ? -28.702 9.262   13.295  1.00 42.55 ? 52  ASP A OD2 1 
ATOM   402  N  N   . GLN A 1 53  ? -25.804 8.629   10.455  1.00 30.93 ? 53  GLN A N   1 
ATOM   403  C  CA  . GLN A 1 53  ? -25.415 9.558   9.411   1.00 29.88 ? 53  GLN A CA  1 
ATOM   404  C  C   . GLN A 1 53  ? -24.007 9.343   8.928   1.00 28.49 ? 53  GLN A C   1 
ATOM   405  O  O   . GLN A 1 53  ? -23.416 10.228  8.325   1.00 26.48 ? 53  GLN A O   1 
ATOM   406  C  CB  . GLN A 1 53  ? -25.655 11.002  9.849   1.00 30.61 ? 53  GLN A CB  1 
ATOM   407  C  CG  . GLN A 1 53  ? -27.142 11.359  10.112  1.00 35.63 ? 53  GLN A CG  1 
ATOM   408  C  CD  . GLN A 1 53  ? -28.044 11.065  8.904   1.00 42.72 ? 53  GLN A CD  1 
ATOM   409  O  OE1 . GLN A 1 53  ? -29.042 10.327  9.023   1.00 43.22 ? 53  GLN A OE1 1 
ATOM   410  N  NE2 . GLN A 1 53  ? -27.690 11.629  7.726   1.00 44.46 ? 53  GLN A NE2 1 
ATOM   411  N  N   . ALA A 1 54  ? -23.465 8.134   9.104   1.00 27.30 ? 54  ALA A N   1 
ATOM   412  C  CA  . ALA A 1 54  ? -22.109 7.874   8.679   1.00 25.09 ? 54  ALA A CA  1 
ATOM   413  C  C   . ALA A 1 54  ? -21.890 8.094   7.194   1.00 25.00 ? 54  ALA A C   1 
ATOM   414  O  O   . ALA A 1 54  ? -22.662 7.597   6.355   1.00 22.72 ? 54  ALA A O   1 
ATOM   415  C  CB  . ALA A 1 54  ? -21.665 6.423   9.090   1.00 25.91 ? 54  ALA A CB  1 
ATOM   416  N  N   . THR A 1 55  ? -20.800 8.788   6.877   1.00 22.68 ? 55  THR A N   1 
ATOM   417  C  CA  . THR A 1 55  ? -20.305 8.900   5.501   1.00 23.83 ? 55  THR A CA  1 
ATOM   418  C  C   . THR A 1 55  ? -18.955 8.262   5.202   1.00 24.49 ? 55  THR A C   1 
ATOM   419  O  O   . THR A 1 55  ? -17.924 8.922   5.370   1.00 25.31 ? 55  THR A O   1 
ATOM   420  C  CB  . THR A 1 55  ? -20.183 10.412  5.068   1.00 23.28 ? 55  THR A CB  1 
ATOM   421  O  OG1 . THR A 1 55  ? -21.472 10.981  5.129   1.00 25.51 ? 55  THR A OG1 1 
ATOM   422  C  CG2 . THR A 1 55  ? -19.784 10.533  3.644   1.00 23.91 ? 55  THR A CG2 1 
ATOM   423  N  N   . SER A 1 56  ? -18.954 7.018   4.686   1.00 23.71 ? 56  SER A N   1 
ATOM   424  C  CA  . SER A 1 56  ? -17.723 6.433   4.264   1.00 23.15 ? 56  SER A CA  1 
ATOM   425  C  C   . SER A 1 56  ? -17.264 7.139   2.965   1.00 23.25 ? 56  SER A C   1 
ATOM   426  O  O   . SER A 1 56  ? -18.072 7.586   2.119   1.00 22.82 ? 56  SER A O   1 
ATOM   427  C  CB  . SER A 1 56  ? -17.869 4.895   4.080   1.00 22.39 ? 56  SER A CB  1 
ATOM   428  O  OG  . SER A 1 56  ? -18.903 4.615   3.125   1.00 20.69 ? 56  SER A OG  1 
ATOM   429  N  N   . LEU A 1 57  ? -15.960 7.221   2.803   1.00 22.40 ? 57  LEU A N   1 
ATOM   430  C  CA  . LEU A 1 57  ? -15.400 7.851   1.625   1.00 24.26 ? 57  LEU A CA  1 
ATOM   431  C  C   . LEU A 1 57  ? -14.560 6.937   0.765   1.00 24.30 ? 57  LEU A C   1 
ATOM   432  O  O   . LEU A 1 57  ? -14.699 6.966   -0.450  1.00 22.07 ? 57  LEU A O   1 
ATOM   433  C  CB  . LEU A 1 57  ? -14.526 9.049   2.023   1.00 24.48 ? 57  LEU A CB  1 
ATOM   434  C  CG  . LEU A 1 57  ? -15.311 10.117  2.823   1.00 27.06 ? 57  LEU A CG  1 
ATOM   435  C  CD1 . LEU A 1 57  ? -14.305 11.038  3.467   1.00 25.96 ? 57  LEU A CD1 1 
ATOM   436  C  CD2 . LEU A 1 57  ? -16.337 10.854  1.898   1.00 27.08 ? 57  LEU A CD2 1 
ATOM   437  N  N   . ARG A 1 58  ? -13.645 6.194   1.398   1.00 24.20 ? 58  ARG A N   1 
ATOM   438  C  CA  . ARG A 1 58  ? -12.648 5.489   0.661   1.00 26.85 ? 58  ARG A CA  1 
ATOM   439  C  C   . ARG A 1 58  ? -12.133 4.286   1.485   1.00 26.29 ? 58  ARG A C   1 
ATOM   440  O  O   . ARG A 1 58  ? -12.246 4.249   2.720   1.00 23.91 ? 58  ARG A O   1 
ATOM   441  C  CB  . ARG A 1 58  ? -11.419 6.370   0.430   1.00 28.15 ? 58  ARG A CB  1 
ATOM   442  C  CG  . ARG A 1 58  ? -11.459 7.423   -0.678  1.00 34.18 ? 58  ARG A CG  1 
ATOM   443  C  CD  . ARG A 1 58  ? -9.984  7.715   -1.015  1.00 40.79 ? 58  ARG A CD  1 
ATOM   444  N  NE  . ARG A 1 58  ? -9.208  7.529   0.224   1.00 45.38 ? 58  ARG A NE  1 
ATOM   445  C  CZ  . ARG A 1 58  ? -7.879  7.559   0.288   1.00 46.45 ? 58  ARG A CZ  1 
ATOM   446  N  NH1 . ARG A 1 58  ? -7.175  7.742   -0.827  1.00 50.54 ? 58  ARG A NH1 1 
ATOM   447  N  NH2 . ARG A 1 58  ? -7.252  7.417   1.455   1.00 45.07 ? 58  ARG A NH2 1 
ATOM   448  N  N   . ILE A 1 59  ? -11.525 3.360   0.759   1.00 24.19 ? 59  ILE A N   1 
ATOM   449  C  CA  . ILE A 1 59  ? -10.882 2.226   1.377   1.00 23.52 ? 59  ILE A CA  1 
ATOM   450  C  C   . ILE A 1 59  ? -9.490  2.131   0.878   1.00 23.83 ? 59  ILE A C   1 
ATOM   451  O  O   . ILE A 1 59  ? -9.192  2.247   -0.339  1.00 24.41 ? 59  ILE A O   1 
ATOM   452  C  CB  . ILE A 1 59  ? -11.716 0.888   1.189   1.00 22.34 ? 59  ILE A CB  1 
ATOM   453  C  CG1 . ILE A 1 59  ? -11.152 -0.225  2.093   1.00 23.48 ? 59  ILE A CG1 1 
ATOM   454  C  CG2 . ILE A 1 59  ? -11.744 0.419   -0.283  1.00 22.52 ? 59  ILE A CG2 1 
ATOM   455  C  CD1 . ILE A 1 59  ? -12.073 -1.411  2.177   1.00 23.53 ? 59  ILE A CD1 1 
ATOM   456  N  N   . LEU A 1 60  ? -8.589  1.934   1.818   1.00 23.83 ? 60  LEU A N   1 
ATOM   457  C  CA  . LEU A 1 60  ? -7.190  2.047   1.521   1.00 25.15 ? 60  LEU A CA  1 
ATOM   458  C  C   . LEU A 1 60  ? -6.413  0.847   2.067   1.00 24.58 ? 60  LEU A C   1 
ATOM   459  O  O   . LEU A 1 60  ? -6.639  0.430   3.198   1.00 24.22 ? 60  LEU A O   1 
ATOM   460  C  CB  . LEU A 1 60  ? -6.664  3.363   2.171   1.00 25.87 ? 60  LEU A CB  1 
ATOM   461  C  CG  . LEU A 1 60  ? -5.152  3.566   2.300   1.00 29.83 ? 60  LEU A CG  1 
ATOM   462  C  CD1 . LEU A 1 60  ? -4.468  3.835   0.938   1.00 31.05 ? 60  LEU A CD1 1 
ATOM   463  C  CD2 . LEU A 1 60  ? -4.931  4.691   3.290   1.00 32.62 ? 60  LEU A CD2 1 
ATOM   464  N  N   . ASN A 1 61  ? -5.491  0.332   1.282   1.00 22.97 ? 61  ASN A N   1 
ATOM   465  C  CA  . ASN A 1 61  ? -4.493  -0.584  1.787   1.00 23.83 ? 61  ASN A CA  1 
ATOM   466  C  C   . ASN A 1 61  ? -3.231  0.211   2.080   1.00 24.19 ? 61  ASN A C   1 
ATOM   467  O  O   . ASN A 1 61  ? -2.590  0.747   1.164   1.00 23.41 ? 61  ASN A O   1 
ATOM   468  C  CB  . ASN A 1 61  ? -4.248  -1.716  0.794   1.00 23.56 ? 61  ASN A CB  1 
ATOM   469  C  CG  . ASN A 1 61  ? -3.101  -2.629  1.177   1.00 24.40 ? 61  ASN A CG  1 
ATOM   470  O  OD1 . ASN A 1 61  ? -2.260  -2.337  2.036   1.00 26.25 ? 61  ASN A OD1 1 
ATOM   471  N  ND2 . ASN A 1 61  ? -3.075  -3.796  0.531   1.00 23.43 ? 61  ASN A ND2 1 
ATOM   472  N  N   . ASN A 1 62  ? -2.898  0.291   3.368   1.00 25.43 ? 62  ASN A N   1 
ATOM   473  C  CA  . ASN A 1 62  ? -1.824  1.157   3.825   1.00 27.33 ? 62  ASN A CA  1 
ATOM   474  C  C   . ASN A 1 62  ? -0.587  0.326   4.116   1.00 27.31 ? 62  ASN A C   1 
ATOM   475  O  O   . ASN A 1 62  ? 0.392   0.794   4.713   1.00 29.13 ? 62  ASN A O   1 
ATOM   476  C  CB  . ASN A 1 62  ? -2.281  1.970   5.032   1.00 28.07 ? 62  ASN A CB  1 
ATOM   477  C  CG  . ASN A 1 62  ? -2.529  1.109   6.254   1.00 28.98 ? 62  ASN A CG  1 
ATOM   478  O  OD1 . ASN A 1 62  ? -2.241  -0.083  6.266   1.00 25.43 ? 62  ASN A OD1 1 
ATOM   479  N  ND2 . ASN A 1 62  ? -3.044  1.720   7.287   1.00 32.01 ? 62  ASN A ND2 1 
ATOM   480  N  N   . GLY A 1 63  ? -0.588  -0.905  3.637   1.00 25.80 ? 63  GLY A N   1 
ATOM   481  C  CA  . GLY A 1 63  ? 0.544   -1.759  3.868   1.00 25.37 ? 63  GLY A CA  1 
ATOM   482  C  C   . GLY A 1 63  ? 0.572   -2.467  5.198   1.00 24.85 ? 63  GLY A C   1 
ATOM   483  O  O   . GLY A 1 63  ? 1.415   -3.311  5.388   1.00 25.94 ? 63  GLY A O   1 
ATOM   484  N  N   . HIS A 1 64  ? -0.368  -2.163  6.104   1.00 25.39 ? 64  HIS A N   1 
ATOM   485  C  CA  . HIS A 1 64  ? -0.453  -2.845  7.383   1.00 25.14 ? 64  HIS A CA  1 
ATOM   486  C  C   . HIS A 1 64  ? -1.818  -3.498  7.590   1.00 24.88 ? 64  HIS A C   1 
ATOM   487  O  O   . HIS A 1 64  ? -1.878  -4.569  8.172   1.00 24.87 ? 64  HIS A O   1 
ATOM   488  C  CB  . HIS A 1 64  ? -0.202  -1.920  8.555   1.00 26.58 ? 64  HIS A CB  1 
ATOM   489  C  CG  . HIS A 1 64  ? 1.088   -1.160  8.434   1.00 31.42 ? 64  HIS A CG  1 
ATOM   490  N  ND1 . HIS A 1 64  ? 1.129   0.198   8.225   1.00 36.00 ? 64  HIS A ND1 1 
ATOM   491  C  CD2 . HIS A 1 64  ? 2.380   -1.580  8.489   1.00 31.40 ? 64  HIS A CD2 1 
ATOM   492  C  CE1 . HIS A 1 64  ? 2.399   0.589   8.155   1.00 33.58 ? 64  HIS A CE1 1 
ATOM   493  N  NE2 . HIS A 1 64  ? 3.176   -0.470  8.323   1.00 33.32 ? 64  HIS A NE2 1 
ATOM   494  N  N   . ALA A 1 65  ? -2.869  -2.830  7.132   1.00 23.34 ? 65  ALA A N   1 
ATOM   495  C  CA  . ALA A 1 65  ? -4.243  -3.316  7.143   1.00 22.69 ? 65  ALA A CA  1 
ATOM   496  C  C   . ALA A 1 65  ? -4.959  -2.599  5.997   1.00 21.81 ? 65  ALA A C   1 
ATOM   497  O  O   . ALA A 1 65  ? -4.324  -1.940  5.157   1.00 22.59 ? 65  ALA A O   1 
ATOM   498  C  CB  . ALA A 1 65  ? -4.915  -3.052  8.549   1.00 19.53 ? 65  ALA A CB  1 
ATOM   499  N  N   . PHE A 1 66  ? -6.272  -2.751  5.895   1.00 20.93 ? 66  PHE A N   1 
ATOM   500  C  CA  . PHE A 1 66  ? -7.032  -1.862  5.044   1.00 21.34 ? 66  PHE A CA  1 
ATOM   501  C  C   . PHE A 1 66  ? -7.895  -1.007  5.940   1.00 21.38 ? 66  PHE A C   1 
ATOM   502  O  O   . PHE A 1 66  ? -8.406  -1.484  6.984   1.00 21.63 ? 66  PHE A O   1 
ATOM   503  C  CB  . PHE A 1 66  ? -7.860  -2.629  3.968   1.00 21.19 ? 66  PHE A CB  1 
ATOM   504  C  CG  . PHE A 1 66  ? -8.880  -3.590  4.547   1.00 22.09 ? 66  PHE A CG  1 
ATOM   505  C  CD1 . PHE A 1 66  ? -8.556  -4.935  4.753   1.00 21.76 ? 66  PHE A CD1 1 
ATOM   506  C  CD2 . PHE A 1 66  ? -10.174 -3.150  4.870   1.00 21.46 ? 66  PHE A CD2 1 
ATOM   507  C  CE1 . PHE A 1 66  ? -9.474  -5.797  5.305   1.00 19.27 ? 66  PHE A CE1 1 
ATOM   508  C  CE2 . PHE A 1 66  ? -11.097 -3.995  5.387   1.00 21.75 ? 66  PHE A CE2 1 
ATOM   509  C  CZ  . PHE A 1 66  ? -10.765 -5.329  5.603   1.00 19.01 ? 66  PHE A CZ  1 
ATOM   510  N  N   . ASN A 1 67  ? -7.988  0.276   5.614   1.00 21.80 ? 67  ASN A N   1 
ATOM   511  C  CA  . ASN A 1 67  ? -8.839  1.187   6.368   1.00 22.63 ? 67  ASN A CA  1 
ATOM   512  C  C   . ASN A 1 67  ? -9.994  1.605   5.519   1.00 21.68 ? 67  ASN A C   1 
ATOM   513  O  O   . ASN A 1 67  ? -9.811  1.935   4.345   1.00 22.93 ? 67  ASN A O   1 
ATOM   514  C  CB  . ASN A 1 67  ? -8.165  2.542   6.766   1.00 23.98 ? 67  ASN A CB  1 
ATOM   515  C  CG  . ASN A 1 67  ? -6.926  2.385   7.550   1.00 30.47 ? 67  ASN A CG  1 
ATOM   516  O  OD1 . ASN A 1 67  ? -5.998  3.219   7.435   1.00 37.47 ? 67  ASN A OD1 1 
ATOM   517  N  ND2 . ASN A 1 67  ? -6.859  1.337   8.369   1.00 28.10 ? 67  ASN A ND2 1 
ATOM   518  N  N   . VAL A 1 68  ? -11.152 1.647   6.133   1.00 19.72 ? 68  VAL A N   1 
ATOM   519  C  CA  . VAL A 1 68  ? -12.260 2.378   5.553   1.00 22.12 ? 68  VAL A CA  1 
ATOM   520  C  C   . VAL A 1 68  ? -12.316 3.732   6.306   1.00 21.15 ? 68  VAL A C   1 
ATOM   521  O  O   . VAL A 1 68  ? -12.459 3.756   7.496   1.00 20.66 ? 68  VAL A O   1 
ATOM   522  C  CB  . VAL A 1 68  ? -13.566 1.633   5.723   1.00 22.18 ? 68  VAL A CB  1 
ATOM   523  C  CG1 . VAL A 1 68  ? -14.800 2.502   5.239   1.00 20.50 ? 68  VAL A CG1 1 
ATOM   524  C  CG2 . VAL A 1 68  ? -13.506 0.298   4.904   1.00 22.91 ? 68  VAL A CG2 1 
ATOM   525  N  N   . GLU A 1 69  ? -12.229 4.814   5.567   1.00 23.59 ? 69  GLU A N   1 
ATOM   526  C  CA  . GLU A 1 69  ? -12.236 6.177   6.088   1.00 24.79 ? 69  GLU A CA  1 
ATOM   527  C  C   . GLU A 1 69  ? -13.581 6.840   5.852   1.00 24.50 ? 69  GLU A C   1 
ATOM   528  O  O   . GLU A 1 69  ? -14.253 6.560   4.826   1.00 25.52 ? 69  GLU A O   1 
ATOM   529  C  CB  . GLU A 1 69  ? -11.147 6.913   5.358   1.00 27.18 ? 69  GLU A CB  1 
ATOM   530  C  CG  . GLU A 1 69  ? -9.823  6.207   5.544   1.00 35.79 ? 69  GLU A CG  1 
ATOM   531  C  CD  . GLU A 1 69  ? -8.688  6.585   4.552   1.00 45.39 ? 69  GLU A CD  1 
ATOM   532  O  OE1 . GLU A 1 69  ? -8.555  5.895   3.506   1.00 49.90 ? 69  GLU A OE1 1 
ATOM   533  O  OE2 . GLU A 1 69  ? -7.862  7.485   4.865   1.00 47.88 ? 69  GLU A OE2 1 
ATOM   534  N  N   . PHE A 1 70  ? -14.030 7.609   6.845   1.00 22.25 ? 70  PHE A N   1 
ATOM   535  C  CA  . PHE A 1 70  ? -15.284 8.312   6.903   1.00 22.24 ? 70  PHE A CA  1 
ATOM   536  C  C   . PHE A 1 70  ? -15.032 9.849   6.957   1.00 22.11 ? 70  PHE A C   1 
ATOM   537  O  O   . PHE A 1 70  ? -13.975 10.303  7.331   1.00 22.44 ? 70  PHE A O   1 
ATOM   538  C  CB  . PHE A 1 70  ? -16.044 7.956   8.177   1.00 20.43 ? 70  PHE A CB  1 
ATOM   539  C  CG  . PHE A 1 70  ? -16.587 6.545   8.156   1.00 20.23 ? 70  PHE A CG  1 
ATOM   540  C  CD1 . PHE A 1 70  ? -15.714 5.462   8.349   1.00 21.77 ? 70  PHE A CD1 1 
ATOM   541  C  CD2 . PHE A 1 70  ? -17.891 6.312   7.850   1.00 22.43 ? 70  PHE A CD2 1 
ATOM   542  C  CE1 . PHE A 1 70  ? -16.190 4.131   8.294   1.00 22.87 ? 70  PHE A CE1 1 
ATOM   543  C  CE2 . PHE A 1 70  ? -18.407 4.996   7.836   1.00 22.65 ? 70  PHE A CE2 1 
ATOM   544  C  CZ  . PHE A 1 70  ? -17.496 3.907   8.048   1.00 21.46 ? 70  PHE A CZ  1 
ATOM   545  N  N   . ASP A 1 71  ? -16.034 10.610  6.572   1.00 23.69 ? 71  ASP A N   1 
ATOM   546  C  CA  . ASP A 1 71  ? -15.941 12.066  6.651   1.00 22.83 ? 71  ASP A CA  1 
ATOM   547  C  C   . ASP A 1 71  ? -16.203 12.422  8.111   1.00 21.10 ? 71  ASP A C   1 
ATOM   548  O  O   . ASP A 1 71  ? -17.287 12.209  8.660   1.00 23.70 ? 71  ASP A O   1 
ATOM   549  C  CB  . ASP A 1 71  ? -16.946 12.651  5.669   1.00 23.72 ? 71  ASP A CB  1 
ATOM   550  C  CG  . ASP A 1 71  ? -17.318 14.098  6.001   1.00 27.83 ? 71  ASP A CG  1 
ATOM   551  O  OD1 . ASP A 1 71  ? -16.489 14.790  6.648   1.00 28.10 ? 71  ASP A OD1 1 
ATOM   552  O  OD2 . ASP A 1 71  ? -18.473 14.469  5.681   1.00 30.05 ? 71  ASP A OD2 1 
ATOM   553  N  N   . ASP A 1 72  ? -15.176 12.874  8.800   1.00 20.40 ? 72  ASP A N   1 
ATOM   554  C  CA  . ASP A 1 72  ? -15.328 13.189  10.218  1.00 21.59 ? 72  ASP A CA  1 
ATOM   555  C  C   . ASP A 1 72  ? -15.308 14.714  10.395  1.00 21.77 ? 72  ASP A C   1 
ATOM   556  O  O   . ASP A 1 72  ? -14.901 15.170  11.451  1.00 22.22 ? 72  ASP A O   1 
ATOM   557  C  CB  . ASP A 1 72  ? -14.122 12.614  11.030  1.00 22.12 ? 72  ASP A CB  1 
ATOM   558  C  CG  . ASP A 1 72  ? -12.747 13.151  10.526  1.00 22.06 ? 72  ASP A CG  1 
ATOM   559  O  OD1 . ASP A 1 72  ? -12.676 13.807  9.453   1.00 26.46 ? 72  ASP A OD1 1 
ATOM   560  O  OD2 . ASP A 1 72  ? -11.696 12.866  11.151  1.00 24.95 ? 72  ASP A OD2 1 
ATOM   561  N  N   . SER A 1 73  ? -15.736 15.465  9.388   1.00 23.78 ? 73  SER A N   1 
ATOM   562  C  CA  . SER A 1 73  ? -15.763 16.978  9.484   1.00 25.23 ? 73  SER A CA  1 
ATOM   563  C  C   . SER A 1 73  ? -17.076 17.528  10.117  1.00 26.66 ? 73  SER A C   1 
ATOM   564  O  O   . SER A 1 73  ? -17.206 18.746  10.373  1.00 26.41 ? 73  SER A O   1 
ATOM   565  C  CB  . SER A 1 73  ? -15.482 17.566  8.101   1.00 23.95 ? 73  SER A CB  1 
ATOM   566  O  OG  . SER A 1 73  ? -16.579 17.228  7.235   1.00 24.80 ? 73  SER A OG  1 
ATOM   567  N  N   . GLN A 1 74  ? -18.050 16.654  10.418  1.00 26.56 ? 74  GLN A N   1 
ATOM   568  C  CA  . GLN A 1 74  ? -19.174 17.061  11.246  1.00 28.58 ? 74  GLN A CA  1 
ATOM   569  C  C   . GLN A 1 74  ? -19.495 15.899  12.160  1.00 30.23 ? 74  GLN A C   1 
ATOM   570  O  O   . GLN A 1 74  ? -18.956 14.818  11.957  1.00 29.50 ? 74  GLN A O   1 
ATOM   571  C  CB  . GLN A 1 74  ? -20.450 17.334  10.433  1.00 28.84 ? 74  GLN A CB  1 
ATOM   572  C  CG  . GLN A 1 74  ? -20.274 18.317  9.308   1.00 32.37 ? 74  GLN A CG  1 
ATOM   573  C  CD  . GLN A 1 74  ? -21.509 18.387  8.456   1.00 32.99 ? 74  GLN A CD  1 
ATOM   574  O  OE1 . GLN A 1 74  ? -22.540 18.927  8.893   1.00 41.87 ? 74  GLN A OE1 1 
ATOM   575  N  NE2 . GLN A 1 74  ? -21.440 17.824  7.271   1.00 29.38 ? 74  GLN A NE2 1 
ATOM   576  N  N   . ASP A 1 75  ? -20.424 16.115  13.102  1.00 31.68 ? 75  ASP A N   1 
ATOM   577  C  CA  . ASP A 1 75  ? -20.820 15.064  14.055  1.00 33.73 ? 75  ASP A CA  1 
ATOM   578  C  C   . ASP A 1 75  ? -21.806 14.087  13.448  1.00 34.31 ? 75  ASP A C   1 
ATOM   579  O  O   . ASP A 1 75  ? -22.966 14.087  13.812  1.00 36.84 ? 75  ASP A O   1 
ATOM   580  C  CB  . ASP A 1 75  ? -21.417 15.634  15.323  1.00 35.11 ? 75  ASP A CB  1 
ATOM   581  C  CG  . ASP A 1 75  ? -20.348 16.132  16.287  1.00 39.12 ? 75  ASP A CG  1 
ATOM   582  O  OD1 . ASP A 1 75  ? -19.136 15.957  16.009  1.00 41.53 ? 75  ASP A OD1 1 
ATOM   583  O  OD2 . ASP A 1 75  ? -20.732 16.707  17.323  1.00 46.14 ? 75  ASP A OD2 1 
ATOM   584  N  N   . LYS A 1 76  ? -21.326 13.246  12.550  1.00 32.85 ? 76  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 76  ? -22.172 12.368  11.741  1.00 32.61 ? 76  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 76  ? -22.271 10.945  12.325  1.00 32.64 ? 76  LYS A C   1 
ATOM   587  O  O   . LYS A 1 76  ? -23.355 10.344  12.372  1.00 34.52 ? 76  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 76  ? -21.568 12.279  10.351  1.00 32.31 ? 76  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 76  ? -22.068 13.322  9.408   1.00 34.24 ? 76  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 76  ? -21.207 13.340  8.188   1.00 35.86 ? 76  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 76  ? -21.913 14.159  7.083   1.00 38.31 ? 76  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 76  ? -21.359 13.874  5.740   1.00 36.52 ? 76  LYS A NZ  1 
ATOM   593  N  N   . ALA A 1 77  ? -21.122 10.375  12.642  1.00 29.91 ? 77  ALA A N   1 
ATOM   594  C  CA  . ALA A 1 77  ? -21.062 9.009   13.191  1.00 27.79 ? 77  ALA A CA  1 
ATOM   595  C  C   . ALA A 1 77  ? -20.327 9.169   14.502  1.00 26.06 ? 77  ALA A C   1 
ATOM   596  O  O   . ALA A 1 77  ? -19.080 9.340   14.542  1.00 26.26 ? 77  ALA A O   1 
ATOM   597  C  CB  . ALA A 1 77  ? -20.281 8.123   12.240  1.00 26.67 ? 77  ALA A CB  1 
ATOM   598  N  N   . VAL A 1 78  ? -21.050 9.178   15.586  1.00 24.09 ? 78  VAL A N   1 
ATOM   599  C  CA  . VAL A 1 78  ? -20.377 9.389   16.866  1.00 24.46 ? 78  VAL A CA  1 
ATOM   600  C  C   . VAL A 1 78  ? -20.572 8.278   17.925  1.00 23.21 ? 78  VAL A C   1 
ATOM   601  O  O   . VAL A 1 78  ? -21.590 7.606   17.989  1.00 22.03 ? 78  VAL A O   1 
ATOM   602  C  CB  . VAL A 1 78  ? -20.749 10.783  17.482  1.00 25.35 ? 78  VAL A CB  1 
ATOM   603  C  CG1 . VAL A 1 78  ? -20.505 11.929  16.425  1.00 24.14 ? 78  VAL A CG1 1 
ATOM   604  C  CG2 . VAL A 1 78  ? -22.229 10.782  17.980  1.00 27.61 ? 78  VAL A CG2 1 
ATOM   605  N  N   . LEU A 1 79  ? -19.552 8.157   18.745  1.00 22.84 ? 79  LEU A N   1 
ATOM   606  C  CA  . LEU A 1 79  ? -19.580 7.373   19.950  1.00 23.78 ? 79  LEU A CA  1 
ATOM   607  C  C   . LEU A 1 79  ? -19.622 8.295   21.172  1.00 24.41 ? 79  LEU A C   1 
ATOM   608  O  O   . LEU A 1 79  ? -18.865 9.282   21.282  1.00 26.13 ? 79  LEU A O   1 
ATOM   609  C  CB  . LEU A 1 79  ? -18.327 6.526   19.953  1.00 24.32 ? 79  LEU A CB  1 
ATOM   610  C  CG  . LEU A 1 79  ? -18.279 5.395   20.956  1.00 24.79 ? 79  LEU A CG  1 
ATOM   611  C  CD1 . LEU A 1 79  ? -19.386 4.353   20.642  1.00 25.65 ? 79  LEU A CD1 1 
ATOM   612  C  CD2 . LEU A 1 79  ? -16.841 4.782   20.912  1.00 21.53 ? 79  LEU A CD2 1 
ATOM   613  N  N   . LYS A 1 80  ? -20.516 7.999   22.084  1.00 24.09 ? 80  LYS A N   1 
ATOM   614  C  CA  . LYS A 1 80  ? -20.498 8.680   23.362  1.00 26.79 ? 80  LYS A CA  1 
ATOM   615  C  C   . LYS A 1 80  ? -21.046 7.775   24.465  1.00 25.40 ? 80  LYS A C   1 
ATOM   616  O  O   . LYS A 1 80  ? -21.356 6.610   24.201  1.00 22.78 ? 80  LYS A O   1 
ATOM   617  C  CB  . LYS A 1 80  ? -21.228 10.025  23.304  1.00 27.27 ? 80  LYS A CB  1 
ATOM   618  C  CG  . LYS A 1 80  ? -22.737 9.899   23.154  1.00 31.54 ? 80  LYS A CG  1 
ATOM   619  C  CD  . LYS A 1 80  ? -23.351 11.258  22.794  1.00 37.71 ? 80  LYS A CD  1 
ATOM   620  C  CE  . LYS A 1 80  ? -22.727 11.739  21.511  1.00 38.70 ? 80  LYS A CE  1 
ATOM   621  N  NZ  . LYS A 1 80  ? -23.211 13.083  21.030  1.00 46.82 ? 80  LYS A NZ  1 
ATOM   622  N  N   . GLY A 1 81  ? -21.122 8.310   25.674  1.00 26.00 ? 81  GLY A N   1 
ATOM   623  C  CA  . GLY A 1 81  ? -21.684 7.595   26.786  1.00 26.73 ? 81  GLY A CA  1 
ATOM   624  C  C   . GLY A 1 81  ? -20.719 6.488   27.162  1.00 27.62 ? 81  GLY A C   1 
ATOM   625  O  O   . GLY A 1 81  ? -19.474 6.672   27.101  1.00 28.04 ? 81  GLY A O   1 
ATOM   626  N  N   . GLY A 1 82  ? -21.249 5.308   27.472  1.00 27.91 ? 82  GLY A N   1 
ATOM   627  C  CA  . GLY A 1 82  ? -20.344 4.248   27.999  1.00 28.09 ? 82  GLY A CA  1 
ATOM   628  C  C   . GLY A 1 82  ? -19.411 4.852   29.031  1.00 27.92 ? 82  GLY A C   1 
ATOM   629  O  O   . GLY A 1 82  ? -19.865 5.569   29.928  1.00 30.02 ? 82  GLY A O   1 
ATOM   630  N  N   . PRO A 1 83  ? -18.080 4.608   28.927  1.00 26.72 ? 83  PRO A N   1 
ATOM   631  C  CA  . PRO A 1 83  ? -17.234 5.217   29.914  1.00 25.30 ? 83  PRO A CA  1 
ATOM   632  C  C   . PRO A 1 83  ? -16.812 6.630   29.554  1.00 27.45 ? 83  PRO A C   1 
ATOM   633  O  O   . PRO A 1 83  ? -15.978 7.172   30.231  1.00 29.22 ? 83  PRO A O   1 
ATOM   634  C  CB  . PRO A 1 83  ? -15.979 4.336   29.880  1.00 26.68 ? 83  PRO A CB  1 
ATOM   635  C  CG  . PRO A 1 83  ? -15.893 3.901   28.429  1.00 23.06 ? 83  PRO A CG  1 
ATOM   636  C  CD  . PRO A 1 83  ? -17.317 3.835   27.919  1.00 24.84 ? 83  PRO A CD  1 
ATOM   637  N  N   . LEU A 1 84  ? -17.360 7.233   28.507  1.00 27.12 ? 84  LEU A N   1 
ATOM   638  C  CA  . LEU A 1 84  ? -16.688 8.388   27.916  1.00 28.40 ? 84  LEU A CA  1 
ATOM   639  C  C   . LEU A 1 84  ? -17.329 9.651   28.457  1.00 30.51 ? 84  LEU A C   1 
ATOM   640  O  O   . LEU A 1 84  ? -18.539 9.662   28.719  1.00 29.90 ? 84  LEU A O   1 
ATOM   641  C  CB  . LEU A 1 84  ? -16.792 8.355   26.384  1.00 25.88 ? 84  LEU A CB  1 
ATOM   642  C  CG  . LEU A 1 84  ? -16.218 7.089   25.692  1.00 24.92 ? 84  LEU A CG  1 
ATOM   643  C  CD1 . LEU A 1 84  ? -16.749 7.029   24.305  1.00 21.29 ? 84  LEU A CD1 1 
ATOM   644  C  CD2 . LEU A 1 84  ? -14.635 6.990   25.736  1.00 22.11 ? 84  LEU A CD2 1 
ATOM   645  N  N   . ASP A 1 85  ? -16.503 10.687  28.612  1.00 32.51 ? 85  ASP A N   1 
ATOM   646  C  CA  . ASP A 1 85  ? -16.991 12.046  28.814  1.00 36.01 ? 85  ASP A CA  1 
ATOM   647  C  C   . ASP A 1 85  ? -16.923 12.704  27.445  1.00 37.42 ? 85  ASP A C   1 
ATOM   648  O  O   . ASP A 1 85  ? -15.960 12.550  26.698  1.00 40.40 ? 85  ASP A O   1 
ATOM   649  C  CB  . ASP A 1 85  ? -16.149 12.790  29.877  1.00 36.73 ? 85  ASP A CB  1 
ATOM   650  C  CG  . ASP A 1 85  ? -16.208 12.195  31.210  0.00 44.46 ? 85  ASP A CG  1 
ATOM   651  O  OD1 . ASP A 1 85  ? -17.282 11.739  31.657  0.00 46.30 ? 85  ASP A OD1 1 
ATOM   652  O  OD2 . ASP A 1 85  ? -15.129 12.154  31.843  0.00 47.60 ? 85  ASP A OD2 1 
ATOM   653  N  N   . GLY A 1 86  ? -17.943 13.429  27.052  1.00 37.68 ? 86  GLY A N   1 
ATOM   654  C  CA  . GLY A 1 86  ? -17.835 13.972  25.705  1.00 37.02 ? 86  GLY A CA  1 
ATOM   655  C  C   . GLY A 1 86  ? -17.861 12.962  24.559  1.00 36.38 ? 86  GLY A C   1 
ATOM   656  O  O   . GLY A 1 86  ? -18.117 11.746  24.744  1.00 37.05 ? 86  GLY A O   1 
ATOM   657  N  N   . THR A 1 87  ? -17.592 13.475  23.371  1.00 32.28 ? 87  THR A N   1 
ATOM   658  C  CA  . THR A 1 87  ? -18.160 12.944  22.141  1.00 28.83 ? 87  THR A CA  1 
ATOM   659  C  C   . THR A 1 87  ? -17.031 12.639  21.201  1.00 25.94 ? 87  THR A C   1 
ATOM   660  O  O   . THR A 1 87  ? -16.085 13.428  21.045  1.00 24.14 ? 87  THR A O   1 
ATOM   661  C  CB  . THR A 1 87  ? -19.124 14.028  21.541  1.00 30.99 ? 87  THR A CB  1 
ATOM   662  O  OG1 . THR A 1 87  ? -20.237 14.196  22.459  1.00 34.92 ? 87  THR A OG1 1 
ATOM   663  C  CG2 . THR A 1 87  ? -19.656 13.639  20.165  1.00 30.29 ? 87  THR A CG2 1 
ATOM   664  N  N   . TYR A 1 88  ? -17.090 11.463  20.587  1.00 24.05 ? 88  TYR A N   1 
ATOM   665  C  CA  . TYR A 1 88  ? -16.001 11.009  19.739  1.00 20.97 ? 88  TYR A CA  1 
ATOM   666  C  C   . TYR A 1 88  ? -16.507 10.710  18.362  1.00 21.40 ? 88  TYR A C   1 
ATOM   667  O  O   . TYR A 1 88  ? -17.534 10.036  18.208  1.00 23.13 ? 88  TYR A O   1 
ATOM   668  C  CB  . TYR A 1 88  ? -15.386 9.782   20.382  1.00 20.59 ? 88  TYR A CB  1 
ATOM   669  C  CG  . TYR A 1 88  ? -14.625 9.986   21.648  1.00 17.19 ? 88  TYR A CG  1 
ATOM   670  C  CD1 . TYR A 1 88  ? -15.298 10.243  22.858  1.00 16.63 ? 88  TYR A CD1 1 
ATOM   671  C  CD2 . TYR A 1 88  ? -13.217 9.810   21.658  1.00 16.25 ? 88  TYR A CD2 1 
ATOM   672  C  CE1 . TYR A 1 88  ? -14.599 10.470  23.994  1.00 18.73 ? 88  TYR A CE1 1 
ATOM   673  C  CE2 . TYR A 1 88  ? -12.485 9.988   22.814  1.00 14.33 ? 88  TYR A CE2 1 
ATOM   674  C  CZ  . TYR A 1 88  ? -13.190 10.253  23.989  1.00 18.22 ? 88  TYR A CZ  1 
ATOM   675  O  OH  . TYR A 1 88  ? -12.497 10.373  25.114  1.00 20.75 ? 88  TYR A OH  1 
ATOM   676  N  N   . ARG A 1 89  ? -15.864 11.258  17.343  1.00 20.91 ? 89  ARG A N   1 
ATOM   677  C  CA  . ARG A 1 89  ? -16.295 11.093  15.962  1.00 20.44 ? 89  ARG A CA  1 
ATOM   678  C  C   . ARG A 1 89  ? -15.554 9.947   15.294  1.00 20.07 ? 89  ARG A C   1 
ATOM   679  O  O   . ARG A 1 89  ? -14.324 9.885   15.366  1.00 19.76 ? 89  ARG A O   1 
ATOM   680  C  CB  . ARG A 1 89  ? -15.945 12.318  15.117  1.00 22.92 ? 89  ARG A CB  1 
ATOM   681  C  CG  . ARG A 1 89  ? -16.924 13.480  15.212  1.00 24.16 ? 89  ARG A CG  1 
ATOM   682  C  CD  . ARG A 1 89  ? -16.487 14.561  14.245  1.00 26.96 ? 89  ARG A CD  1 
ATOM   683  N  NE  . ARG A 1 89  ? -17.182 15.803  14.628  1.00 29.16 ? 89  ARG A NE  1 
ATOM   684  C  CZ  . ARG A 1 89  ? -16.860 17.016  14.170  1.00 33.48 ? 89  ARG A CZ  1 
ATOM   685  N  NH1 . ARG A 1 89  ? -15.836 17.188  13.331  1.00 32.04 ? 89  ARG A NH1 1 
ATOM   686  N  NH2 . ARG A 1 89  ? -17.571 18.071  14.563  1.00 34.84 ? 89  ARG A NH2 1 
ATOM   687  N  N   . LEU A 1 90  ? -16.301 9.138   14.527  1.00 18.92 ? 90  LEU A N   1 
ATOM   688  C  CA  . LEU A 1 90  ? -15.707 8.009   13.770  1.00 17.33 ? 90  LEU A CA  1 
ATOM   689  C  C   . LEU A 1 90  ? -14.873 8.543   12.646  1.00 16.65 ? 90  LEU A C   1 
ATOM   690  O  O   . LEU A 1 90  ? -15.345 9.276   11.770  1.00 17.96 ? 90  LEU A O   1 
ATOM   691  C  CB  . LEU A 1 90  ? -16.827 7.118   13.174  1.00 17.22 ? 90  LEU A CB  1 
ATOM   692  C  CG  . LEU A 1 90  ? -16.386 5.956   12.248  1.00 19.61 ? 90  LEU A CG  1 
ATOM   693  C  CD1 . LEU A 1 90  ? -15.560 4.924   12.996  1.00 19.98 ? 90  LEU A CD1 1 
ATOM   694  C  CD2 . LEU A 1 90  ? -17.642 5.204   11.703  1.00 17.93 ? 90  LEU A CD2 1 
ATOM   695  N  N   . ILE A 1 91  ? -13.619 8.167   12.626  1.00 16.66 ? 91  ILE A N   1 
ATOM   696  C  CA  . ILE A 1 91  ? -12.791 8.495   11.470  1.00 17.58 ? 91  ILE A CA  1 
ATOM   697  C  C   . ILE A 1 91  ? -12.506 7.338   10.499  1.00 17.40 ? 91  ILE A C   1 
ATOM   698  O  O   . ILE A 1 91  ? -12.405 7.506   9.259   1.00 17.24 ? 91  ILE A O   1 
ATOM   699  C  CB  . ILE A 1 91  ? -11.451 9.165   11.931  1.00 18.15 ? 91  ILE A CB  1 
ATOM   700  C  CG1 . ILE A 1 91  ? -10.564 9.549   10.700  1.00 19.33 ? 91  ILE A CG1 1 
ATOM   701  C  CG2 . ILE A 1 91  ? -10.740 8.328   12.992  1.00 21.20 ? 91  ILE A CG2 1 
ATOM   702  C  CD1 . ILE A 1 91  ? -9.333  10.473  11.113  1.00 19.41 ? 91  ILE A CD1 1 
ATOM   703  N  N   . GLN A 1 92  ? -12.344 6.120   11.059  1.00 17.48 ? 92  GLN A N   1 
ATOM   704  C  CA  . GLN A 1 92  ? -11.994 5.000   10.183  1.00 16.21 ? 92  GLN A CA  1 
ATOM   705  C  C   . GLN A 1 92  ? -12.256 3.716   10.958  1.00 14.68 ? 92  GLN A C   1 
ATOM   706  O  O   . GLN A 1 92  ? -12.392 3.758   12.158  1.00 13.80 ? 92  GLN A O   1 
ATOM   707  C  CB  . GLN A 1 92  ? -10.500 5.069   9.699   1.00 17.16 ? 92  GLN A CB  1 
ATOM   708  C  CG  . GLN A 1 92  ? -9.469  5.076   10.814  1.00 19.50 ? 92  GLN A CG  1 
ATOM   709  C  CD  . GLN A 1 92  ? -8.676  3.703   10.873  1.00 26.40 ? 92  GLN A CD  1 
ATOM   710  O  OE1 . GLN A 1 92  ? -9.264  2.672   10.974  1.00 21.76 ? 92  GLN A OE1 1 
ATOM   711  N  NE2 . GLN A 1 92  ? -7.383  3.758   10.899  1.00 29.83 ? 92  GLN A NE2 1 
ATOM   712  N  N   . PHE A 1 93  ? -12.445 2.625   10.219  1.00 14.77 ? 93  PHE A N   1 
ATOM   713  C  CA  . PHE A 1 93  ? -12.294 1.298   10.820  1.00 13.96 ? 93  PHE A CA  1 
ATOM   714  C  C   . PHE A 1 93  ? -11.341 0.438   10.020  1.00 14.44 ? 93  PHE A C   1 
ATOM   715  O  O   . PHE A 1 93  ? -11.096 0.649   8.865   1.00 16.67 ? 93  PHE A O   1 
ATOM   716  C  CB  . PHE A 1 93  ? -13.665 0.640   11.093  1.00 12.20 ? 93  PHE A CB  1 
ATOM   717  C  CG  . PHE A 1 93  ? -14.366 0.202   9.871   1.00 15.89 ? 93  PHE A CG  1 
ATOM   718  C  CD1 . PHE A 1 93  ? -13.934 -0.941  9.161   1.00 20.87 ? 93  PHE A CD1 1 
ATOM   719  C  CD2 . PHE A 1 93  ? -15.478 0.928   9.385   1.00 13.60 ? 93  PHE A CD2 1 
ATOM   720  C  CE1 . PHE A 1 93  ? -14.604 -1.375  8.037   1.00 15.64 ? 93  PHE A CE1 1 
ATOM   721  C  CE2 . PHE A 1 93  ? -16.171 0.500   8.244   1.00 20.37 ? 93  PHE A CE2 1 
ATOM   722  C  CZ  . PHE A 1 93  ? -15.696 -0.636  7.543   1.00 17.80 ? 93  PHE A CZ  1 
ATOM   723  N  N   . HIS A 1 94  ? -10.734 -0.529  10.696  1.00 16.91 ? 94  HIS A N   1 
ATOM   724  C  CA  . HIS A 1 94  ? -9.818  -1.439  10.073  1.00 14.80 ? 94  HIS A CA  1 
ATOM   725  C  C   . HIS A 1 94  ? -9.936  -2.727  10.904  1.00 14.18 ? 94  HIS A C   1 
ATOM   726  O  O   . HIS A 1 94  ? -10.614 -2.773  11.925  1.00 13.70 ? 94  HIS A O   1 
ATOM   727  C  CB  . HIS A 1 94  ? -8.381  -0.886  10.067  1.00 15.31 ? 94  HIS A CB  1 
ATOM   728  C  CG  . HIS A 1 94  ? -7.867  -0.638  11.440  1.00 14.79 ? 94  HIS A CG  1 
ATOM   729  N  ND1 . HIS A 1 94  ? -8.123  0.530   12.163  1.00 15.30 ? 94  HIS A ND1 1 
ATOM   730  C  CD2 . HIS A 1 94  ? -7.269  -1.489  12.286  1.00 14.87 ? 94  HIS A CD2 1 
ATOM   731  C  CE1 . HIS A 1 94  ? -7.583  0.403   13.371  1.00 15.30 ? 94  HIS A CE1 1 
ATOM   732  N  NE2 . HIS A 1 94  ? -7.057  -0.829  13.470  1.00 13.17 ? 94  HIS A NE2 1 
ATOM   733  N  N   . PHE A 1 95  ? -9.230  -3.743  10.451  1.00 13.80 ? 95  PHE A N   1 
ATOM   734  C  CA  . PHE A 1 95  ? -9.226  -5.054  11.127  1.00 12.34 ? 95  PHE A CA  1 
ATOM   735  C  C   . PHE A 1 95  ? -7.795  -5.535  11.305  1.00 12.75 ? 95  PHE A C   1 
ATOM   736  O  O   . PHE A 1 95  ? -6.874  -5.072  10.634  1.00 12.60 ? 95  PHE A O   1 
ATOM   737  C  CB  . PHE A 1 95  ? -9.897  -6.100  10.194  1.00 13.07 ? 95  PHE A CB  1 
ATOM   738  C  CG  . PHE A 1 95  ? -11.365 -5.845  9.926   1.00 13.71 ? 95  PHE A CG  1 
ATOM   739  C  CD1 . PHE A 1 95  ? -11.756 -5.043  8.832   1.00 13.50 ? 95  PHE A CD1 1 
ATOM   740  C  CD2 . PHE A 1 95  ? -12.341 -6.463  10.695  1.00 15.95 ? 95  PHE A CD2 1 
ATOM   741  C  CE1 . PHE A 1 95  ? -13.126 -4.871  8.506   1.00 15.89 ? 95  PHE A CE1 1 
ATOM   742  C  CE2 . PHE A 1 95  ? -13.666 -6.299  10.366  1.00 17.49 ? 95  PHE A CE2 1 
ATOM   743  C  CZ  . PHE A 1 95  ? -14.044 -5.494  9.281   1.00 18.83 ? 95  PHE A CZ  1 
ATOM   744  N  N   . HIS A 1 96  ? -7.642  -6.501  12.198  1.00 12.11 ? 96  HIS A N   1 
ATOM   745  C  CA  . HIS A 1 96  ? -6.370  -7.282  12.294  1.00 13.28 ? 96  HIS A CA  1 
ATOM   746  C  C   . HIS A 1 96  ? -6.840  -8.702  12.157  1.00 14.30 ? 96  HIS A C   1 
ATOM   747  O  O   . HIS A 1 96  ? -7.925  -9.016  12.633  1.00 14.23 ? 96  HIS A O   1 
ATOM   748  C  CB  . HIS A 1 96  ? -5.765  -7.112  13.648  1.00 13.17 ? 96  HIS A CB  1 
ATOM   749  C  CG  . HIS A 1 96  ? -5.515  -5.670  13.972  1.00 13.75 ? 96  HIS A CG  1 
ATOM   750  N  ND1 . HIS A 1 96  ? -4.324  -5.065  13.636  1.00 16.00 ? 96  HIS A ND1 1 
ATOM   751  C  CD2 . HIS A 1 96  ? -6.353  -4.673  14.396  1.00 15.25 ? 96  HIS A CD2 1 
ATOM   752  C  CE1 . HIS A 1 96  ? -4.389  -3.775  13.987  1.00 19.26 ? 96  HIS A CE1 1 
ATOM   753  N  NE2 . HIS A 1 96  ? -5.624  -3.505  14.396  1.00 16.35 ? 96  HIS A NE2 1 
ATOM   754  N  N   . TRP A 1 97  ? -6.059  -9.523  11.489  1.00 12.90 ? 97  TRP A N   1 
ATOM   755  C  CA  . TRP A 1 97  ? -6.554  -10.932 11.272  1.00 15.92 ? 97  TRP A CA  1 
ATOM   756  C  C   . TRP A 1 97  ? -5.382  -11.877 11.244  1.00 17.03 ? 97  TRP A C   1 
ATOM   757  O  O   . TRP A 1 97  ? -4.212  -11.424 11.227  1.00 17.67 ? 97  TRP A O   1 
ATOM   758  C  CB  . TRP A 1 97  ? -7.385  -11.103 10.022  1.00 15.07 ? 97  TRP A CB  1 
ATOM   759  C  CG  . TRP A 1 97  ? -6.699  -10.672 8.807   1.00 18.14 ? 97  TRP A CG  1 
ATOM   760  C  CD1 . TRP A 1 97  ? -5.968  -11.457 7.939   1.00 15.66 ? 97  TRP A CD1 1 
ATOM   761  C  CD2 . TRP A 1 97  ? -6.714  -9.371  8.258   1.00 16.71 ? 97  TRP A CD2 1 
ATOM   762  N  NE1 . TRP A 1 97  ? -5.453  -10.698 6.952   1.00 18.74 ? 97  TRP A NE1 1 
ATOM   763  C  CE2 . TRP A 1 97  ? -5.905  -9.405  7.107   1.00 18.10 ? 97  TRP A CE2 1 
ATOM   764  C  CE3 . TRP A 1 97  ? -7.248  -8.128  8.699   1.00 18.78 ? 97  TRP A CE3 1 
ATOM   765  C  CZ2 . TRP A 1 97  ? -5.674  -8.263  6.310   1.00 20.66 ? 97  TRP A CZ2 1 
ATOM   766  C  CZ3 . TRP A 1 97  ? -7.034  -6.968  7.879   1.00 14.59 ? 97  TRP A CZ3 1 
ATOM   767  C  CH2 . TRP A 1 97  ? -6.229  -7.053  6.718   1.00 16.28 ? 97  TRP A CH2 1 
ATOM   768  N  N   . GLY A 1 98  ? -5.689  -13.197 11.201  1.00 17.31 ? 98  GLY A N   1 
ATOM   769  C  CA  . GLY A 1 98  ? -4.597  -14.127 11.263  1.00 17.01 ? 98  GLY A CA  1 
ATOM   770  C  C   . GLY A 1 98  ? -4.392  -14.873 9.941   1.00 17.95 ? 98  GLY A C   1 
ATOM   771  O  O   . GLY A 1 98  ? -5.146  -14.699 8.948   1.00 18.37 ? 98  GLY A O   1 
ATOM   772  N  N   . SER A 1 99  ? -3.384  -15.727 9.977   1.00 18.86 ? 99  SER A N   1 
ATOM   773  C  CA  . SER A 1 99  ? -3.059  -16.605 8.853   1.00 20.13 ? 99  SER A CA  1 
ATOM   774  C  C   . SER A 1 99  ? -3.950  -17.854 8.899   1.00 21.42 ? 99  SER A C   1 
ATOM   775  O  O   . SER A 1 99  ? -4.018  -18.616 7.915   1.00 23.92 ? 99  SER A O   1 
ATOM   776  C  CB  . SER A 1 99  ? -1.584  -16.984 8.928   1.00 20.54 ? 99  SER A CB  1 
ATOM   777  O  OG  . SER A 1 99  ? -1.243  -17.528 10.222  1.00 21.08 ? 99  SER A OG  1 
ATOM   778  N  N   . LEU A 1 100 ? -4.588  -18.069 10.027  1.00 22.03 ? 100 LEU A N   1 
ATOM   779  C  CA  . LEU A 1 100 ? -5.511  -19.152 10.263  1.00 24.62 ? 100 LEU A CA  1 
ATOM   780  C  C   . LEU A 1 100 ? -6.601  -18.623 11.166  1.00 24.24 ? 100 LEU A C   1 
ATOM   781  O  O   . LEU A 1 100 ? -6.387  -17.658 11.901  1.00 23.40 ? 100 LEU A O   1 
ATOM   782  C  CB  . LEU A 1 100 ? -4.855  -20.306 11.066  1.00 26.37 ? 100 LEU A CB  1 
ATOM   783  C  CG  . LEU A 1 100 ? -3.475  -20.823 10.774  1.00 28.85 ? 100 LEU A CG  1 
ATOM   784  C  CD1 . LEU A 1 100 ? -2.445  -20.241 11.745  1.00 34.60 ? 100 LEU A CD1 1 
ATOM   785  C  CD2 . LEU A 1 100 ? -3.626  -22.354 10.970  1.00 39.22 ? 100 LEU A CD2 1 
ATOM   786  N  N   . ASP A 1 101 ? -7.713  -19.341 11.224  1.00 24.33 ? 101 ASP A N   1 
ATOM   787  C  CA  . ASP A 1 101 ? -8.867  -18.921 12.057  1.00 24.71 ? 101 ASP A CA  1 
ATOM   788  C  C   . ASP A 1 101 ? -8.612  -18.929 13.541  1.00 24.02 ? 101 ASP A C   1 
ATOM   789  O  O   . ASP A 1 101 ? -9.285  -18.230 14.335  1.00 23.52 ? 101 ASP A O   1 
ATOM   790  C  CB  . ASP A 1 101 ? -10.086 -19.792 11.775  1.00 24.01 ? 101 ASP A CB  1 
ATOM   791  C  CG  . ASP A 1 101 ? -10.560 -19.771 10.347  1.00 28.83 ? 101 ASP A CG  1 
ATOM   792  O  OD1 . ASP A 1 101 ? -10.187 -18.935 9.504   1.00 25.69 ? 101 ASP A OD1 1 
ATOM   793  O  OD2 . ASP A 1 101 ? -11.407 -20.655 10.053  1.00 32.03 ? 101 ASP A OD2 1 
ATOM   794  N  N   . GLY A 1 102 ? -7.603  -19.701 13.966  1.00 23.48 ? 102 GLY A N   1 
ATOM   795  C  CA  . GLY A 1 102 ? -7.328  -19.819 15.381  1.00 21.54 ? 102 GLY A CA  1 
ATOM   796  C  C   . GLY A 1 102 ? -6.585  -18.603 15.983  1.00 19.99 ? 102 GLY A C   1 
ATOM   797  O  O   . GLY A 1 102 ? -6.295  -18.538 17.137  1.00 19.65 ? 102 GLY A O   1 
ATOM   798  N  N   . GLN A 1 103 ? -6.245  -17.640 15.150  1.00 18.78 ? 103 GLN A N   1 
ATOM   799  C  CA  . GLN A 1 103 ? -5.569  -16.442 15.696  1.00 18.43 ? 103 GLN A CA  1 
ATOM   800  C  C   . GLN A 1 103 ? -5.915  -15.264 14.842  1.00 16.58 ? 103 GLN A C   1 
ATOM   801  O  O   . GLN A 1 103 ? -6.418  -15.444 13.762  1.00 17.83 ? 103 GLN A O   1 
ATOM   802  C  CB  . GLN A 1 103 ? -4.038  -16.635 15.707  1.00 18.03 ? 103 GLN A CB  1 
ATOM   803  C  CG  . GLN A 1 103 ? -3.351  -16.716 14.336  1.00 19.16 ? 103 GLN A CG  1 
ATOM   804  C  CD  . GLN A 1 103 ? -1.976  -17.345 14.505  1.00 27.33 ? 103 GLN A CD  1 
ATOM   805  O  OE1 . GLN A 1 103 ? -1.830  -18.290 15.298  1.00 29.24 ? 103 GLN A OE1 1 
ATOM   806  N  NE2 . GLN A 1 103 ? -0.986  -16.862 13.776  1.00 20.71 ? 103 GLN A NE2 1 
ATOM   807  N  N   . GLY A 1 104 ? -5.599  -14.061 15.309  1.00 19.00 ? 104 GLY A N   1 
ATOM   808  C  CA  . GLY A 1 104 ? -5.836  -12.899 14.484  1.00 14.41 ? 104 GLY A CA  1 
ATOM   809  C  C   . GLY A 1 104 ? -6.250  -11.668 15.287  1.00 16.70 ? 104 GLY A C   1 
ATOM   810  O  O   . GLY A 1 104 ? -5.886  -10.525 14.963  1.00 15.58 ? 104 GLY A O   1 
ATOM   811  N  N   . SER A 1 105 ? -7.021  -11.893 16.354  1.00 14.97 ? 105 SER A N   1 
ATOM   812  C  CA  . SER A 1 105 ? -7.347  -10.841 17.261  1.00 15.82 ? 105 SER A CA  1 
ATOM   813  C  C   . SER A 1 105 ? -6.173  -10.273 18.058  1.00 15.39 ? 105 SER A C   1 
ATOM   814  O  O   . SER A 1 105 ? -5.169  -10.927 18.306  1.00 15.89 ? 105 SER A O   1 
ATOM   815  C  CB  . SER A 1 105 ? -8.514  -11.203 18.221  1.00 12.55 ? 105 SER A CB  1 
ATOM   816  O  OG  . SER A 1 105 ? -8.086  -12.057 19.261  1.00 17.66 ? 105 SER A OG  1 
ATOM   817  N  N   . GLU A 1 106 ? -6.316  -8.993  18.440  1.00 15.29 ? 106 GLU A N   1 
ATOM   818  C  CA  . GLU A 1 106 ? -5.298  -8.361  19.259  1.00 15.31 ? 106 GLU A CA  1 
ATOM   819  C  C   . GLU A 1 106 ? -5.634  -8.567  20.743  1.00 14.80 ? 106 GLU A C   1 
ATOM   820  O  O   . GLU A 1 106 ? -4.825  -9.117  21.528  1.00 15.62 ? 106 GLU A O   1 
ATOM   821  C  CB  . GLU A 1 106 ? -5.284  -6.852  18.860  1.00 15.20 ? 106 GLU A CB  1 
ATOM   822  C  CG  . GLU A 1 106 ? -4.919  -6.689  17.382  1.00 16.25 ? 106 GLU A CG  1 
ATOM   823  C  CD  . GLU A 1 106 ? -4.152  -5.431  17.141  1.00 19.59 ? 106 GLU A CD  1 
ATOM   824  O  OE1 . GLU A 1 106 ? -4.735  -4.331  17.335  1.00 17.87 ? 106 GLU A OE1 1 
ATOM   825  O  OE2 . GLU A 1 106 ? -2.994  -5.538  16.752  1.00 15.20 ? 106 GLU A OE2 1 
ATOM   826  N  N   . HIS A 1 107 ? -6.823  -8.129  21.175  1.00 14.74 ? 107 HIS A N   1 
ATOM   827  C  CA  . HIS A 1 107 ? -7.277  -8.464  22.494  1.00 13.66 ? 107 HIS A CA  1 
ATOM   828  C  C   . HIS A 1 107 ? -7.588  -9.946  22.521  1.00 14.33 ? 107 HIS A C   1 
ATOM   829  O  O   . HIS A 1 107 ? -7.852  -10.555 21.471  1.00 16.17 ? 107 HIS A O   1 
ATOM   830  C  CB  . HIS A 1 107 ? -8.501  -7.661  22.867  1.00 14.35 ? 107 HIS A CB  1 
ATOM   831  C  CG  . HIS A 1 107 ? -8.199  -6.188  23.053  1.00 15.61 ? 107 HIS A CG  1 
ATOM   832  N  ND1 . HIS A 1 107 ? -8.237  -5.290  22.020  1.00 16.63 ? 107 HIS A ND1 1 
ATOM   833  C  CD2 . HIS A 1 107 ? -7.816  -5.492  24.140  1.00 12.89 ? 107 HIS A CD2 1 
ATOM   834  C  CE1 . HIS A 1 107 ? -7.899  -4.102  22.466  1.00 16.56 ? 107 HIS A CE1 1 
ATOM   835  N  NE2 . HIS A 1 107 ? -7.602  -4.212  23.746  1.00 14.58 ? 107 HIS A NE2 1 
ATOM   836  N  N   . THR A 1 108 ? -7.379  -10.535 23.682  1.00 15.53 ? 108 THR A N   1 
ATOM   837  C  CA  . THR A 1 108 ? -7.822  -11.904 23.908  1.00 16.73 ? 108 THR A CA  1 
ATOM   838  C  C   . THR A 1 108 ? -8.801  -11.884 25.073  1.00 17.53 ? 108 THR A C   1 
ATOM   839  O  O   . THR A 1 108 ? -8.766  -10.974 25.921  1.00 19.52 ? 108 THR A O   1 
ATOM   840  C  CB  . THR A 1 108 ? -6.655  -12.812 24.157  1.00 15.32 ? 108 THR A CB  1 
ATOM   841  O  OG1 . THR A 1 108 ? -5.860  -12.284 25.197  1.00 17.90 ? 108 THR A OG1 1 
ATOM   842  C  CG2 . THR A 1 108 ? -5.771  -12.909 22.857  1.00 14.68 ? 108 THR A CG2 1 
ATOM   843  N  N   . VAL A 1 109 ? -9.601  -12.937 25.194  1.00 17.36 ? 109 VAL A N   1 
ATOM   844  C  CA  . VAL A 1 109 ? -10.565 -12.993 26.299  1.00 18.19 ? 109 VAL A CA  1 
ATOM   845  C  C   . VAL A 1 109 ? -10.276 -14.286 27.059  1.00 18.75 ? 109 VAL A C   1 
ATOM   846  O  O   . VAL A 1 109 ? -10.399 -15.339 26.485  1.00 20.18 ? 109 VAL A O   1 
ATOM   847  C  CB  . VAL A 1 109 ? -11.974 -13.068 25.718  1.00 17.69 ? 109 VAL A CB  1 
ATOM   848  C  CG1 . VAL A 1 109 ? -12.973 -13.164 26.857  1.00 19.17 ? 109 VAL A CG1 1 
ATOM   849  C  CG2 . VAL A 1 109 ? -12.221 -11.835 24.863  1.00 20.04 ? 109 VAL A CG2 1 
ATOM   850  N  N   . ASP A 1 110 ? -9.794  -14.198 28.258  1.00 17.94 ? 110 ASP A N   1 
ATOM   851  C  CA  . ASP A 1 110 ? -9.321  -15.411 28.952  1.00 21.83 ? 110 ASP A CA  1 
ATOM   852  C  C   . ASP A 1 110 ? -8.402  -16.207 28.081  1.00 22.66 ? 110 ASP A C   1 
ATOM   853  O  O   . ASP A 1 110 ? -8.554  -17.450 27.954  1.00 22.62 ? 110 ASP A O   1 
ATOM   854  C  CB  . ASP A 1 110 ? -10.540 -16.244 29.393  1.00 21.28 ? 110 ASP A CB  1 
ATOM   855  C  CG  . ASP A 1 110 ? -11.375 -15.499 30.384  1.00 22.52 ? 110 ASP A CG  1 
ATOM   856  O  OD1 . ASP A 1 110 ? -10.807 -14.747 31.171  1.00 26.18 ? 110 ASP A OD1 1 
ATOM   857  O  OD2 . ASP A 1 110 ? -12.590 -15.631 30.341  1.00 29.59 ? 110 ASP A OD2 1 
ATOM   858  N  N   . LYS A 1 111 ? -7.445  -15.496 27.469  1.00 22.27 ? 111 LYS A N   1 
ATOM   859  C  CA  . LYS A 1 111 ? -6.437  -16.082 26.634  1.00 23.82 ? 111 LYS A CA  1 
ATOM   860  C  C   . LYS A 1 111 ? -6.916  -16.599 25.289  1.00 22.40 ? 111 LYS A C   1 
ATOM   861  O  O   . LYS A 1 111 ? -6.097  -16.938 24.459  1.00 21.99 ? 111 LYS A O   1 
ATOM   862  C  CB  . LYS A 1 111 ? -5.693  -17.172 27.426  1.00 27.92 ? 111 LYS A CB  1 
ATOM   863  C  CG  . LYS A 1 111 ? -4.959  -16.645 28.660  1.00 29.18 ? 111 LYS A CG  1 
ATOM   864  C  CD  . LYS A 1 111 ? -3.796  -15.887 28.221  1.00 33.86 ? 111 LYS A CD  1 
ATOM   865  C  CE  . LYS A 1 111 ? -3.231  -15.094 29.411  1.00 39.60 ? 111 LYS A CE  1 
ATOM   866  N  NZ  . LYS A 1 111 ? -1.743  -15.193 29.384  1.00 42.13 ? 111 LYS A NZ  1 
ATOM   867  N  N   . LYS A 1 112 ? -8.215  -16.564 25.011  1.00 20.94 ? 112 LYS A N   1 
ATOM   868  C  CA  . LYS A 1 112 ? -8.728  -16.991 23.719  1.00 22.69 ? 112 LYS A CA  1 
ATOM   869  C  C   . LYS A 1 112 ? -8.486  -15.908 22.627  1.00 23.22 ? 112 LYS A C   1 
ATOM   870  O  O   . LYS A 1 112 ? -8.832  -14.723 22.823  1.00 20.91 ? 112 LYS A O   1 
ATOM   871  C  CB  . LYS A 1 112 ? -10.236 -17.329 23.812  1.00 23.82 ? 112 LYS A CB  1 
ATOM   872  C  CG  . LYS A 1 112 ? -10.825 -17.799 22.455  1.00 26.30 ? 112 LYS A CG  1 
ATOM   873  C  CD  . LYS A 1 112 ? -12.345 -17.584 22.245  1.00 27.69 ? 112 LYS A CD  1 
ATOM   874  C  CE  . LYS A 1 112 ? -12.661 -18.004 20.748  1.00 28.08 ? 112 LYS A CE  1 
ATOM   875  N  NZ  . LYS A 1 112 ? -14.054 -18.579 20.572  1.00 33.13 ? 112 LYS A NZ  1 
ATOM   876  N  N   . LYS A 1 113 ? -7.878  -16.332 21.500  1.00 20.36 ? 113 LYS A N   1 
ATOM   877  C  CA  . LYS A 1 113 ? -7.712  -15.460 20.328  1.00 20.90 ? 113 LYS A CA  1 
ATOM   878  C  C   . LYS A 1 113 ? -8.900  -15.707 19.396  1.00 20.30 ? 113 LYS A C   1 
ATOM   879  O  O   . LYS A 1 113 ? -9.321  -16.863 19.198  1.00 21.07 ? 113 LYS A O   1 
ATOM   880  C  CB  . LYS A 1 113 ? -6.400  -15.769 19.563  1.00 17.83 ? 113 LYS A CB  1 
ATOM   881  C  CG  . LYS A 1 113 ? -5.184  -15.704 20.470  1.00 24.55 ? 113 LYS A CG  1 
ATOM   882  C  CD  . LYS A 1 113 ? -3.822  -15.944 19.738  1.00 22.47 ? 113 LYS A CD  1 
ATOM   883  C  CE  . LYS A 1 113 ? -2.704  -15.779 20.760  1.00 29.32 ? 113 LYS A CE  1 
ATOM   884  N  NZ  . LYS A 1 113 ? -1.422  -16.378 20.302  1.00 34.57 ? 113 LYS A NZ  1 
ATOM   885  N  N   . TYR A 1 114 ? -9.430  -14.651 18.780  1.00 17.27 ? 114 TYR A N   1 
ATOM   886  C  CA  . TYR A 1 114 ? -10.472 -14.787 17.820  1.00 16.16 ? 114 TYR A CA  1 
ATOM   887  C  C   . TYR A 1 114 ? -9.843  -14.708 16.466  1.00 16.81 ? 114 TYR A C   1 
ATOM   888  O  O   . TYR A 1 114 ? -8.586  -14.468 16.382  1.00 17.22 ? 114 TYR A O   1 
ATOM   889  C  CB  . TYR A 1 114 ? -11.518 -13.673 18.039  1.00 16.15 ? 114 TYR A CB  1 
ATOM   890  C  CG  . TYR A 1 114 ? -12.450 -13.937 19.204  1.00 19.66 ? 114 TYR A CG  1 
ATOM   891  C  CD1 . TYR A 1 114 ? -13.651 -14.575 18.978  1.00 20.80 ? 114 TYR A CD1 1 
ATOM   892  C  CD2 . TYR A 1 114 ? -12.154 -13.560 20.499  1.00 20.50 ? 114 TYR A CD2 1 
ATOM   893  C  CE1 . TYR A 1 114 ? -14.548 -14.813 20.005  1.00 23.88 ? 114 TYR A CE1 1 
ATOM   894  C  CE2 . TYR A 1 114 ? -13.071 -13.812 21.544  1.00 23.58 ? 114 TYR A CE2 1 
ATOM   895  C  CZ  . TYR A 1 114 ? -14.261 -14.443 21.252  1.00 22.57 ? 114 TYR A CZ  1 
ATOM   896  O  OH  . TYR A 1 114 ? -15.232 -14.687 22.215  1.00 26.31 ? 114 TYR A OH  1 
ATOM   897  N  N   . ALA A 1 115 ? -10.634 -14.976 15.411  1.00 16.64 ? 115 ALA A N   1 
ATOM   898  C  CA  . ALA A 1 115 ? -10.074 -15.022 14.034  1.00 17.92 ? 115 ALA A CA  1 
ATOM   899  C  C   . ALA A 1 115 ? -9.629  -13.620 13.567  1.00 17.93 ? 115 ALA A C   1 
ATOM   900  O  O   . ALA A 1 115 ? -8.735  -13.457 12.697  1.00 17.56 ? 115 ALA A O   1 
ATOM   901  C  CB  . ALA A 1 115 ? -11.090 -15.623 13.024  1.00 20.13 ? 115 ALA A CB  1 
ATOM   902  N  N   . ALA A 1 116 ? -10.250 -12.608 14.166  1.00 15.84 ? 116 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 116 ? -9.958  -11.245 13.722  1.00 15.52 ? 116 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 116 ? -10.540 -10.282 14.745  1.00 14.63 ? 116 ALA A C   1 
ATOM   905  O  O   . ALA A 1 116 ? -11.222 -10.680 15.701  1.00 15.37 ? 116 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 116 ? -10.519 -10.957 12.338  1.00 13.12 ? 116 ALA A CB  1 
ATOM   907  N  N   . GLU A 1 117 ? -10.212 -9.002  14.560  1.00 15.37 ? 117 GLU A N   1 
ATOM   908  C  CA  . GLU A 1 117 ? -10.692 -7.996  15.466  1.00 13.79 ? 117 GLU A CA  1 
ATOM   909  C  C   . GLU A 1 117 ? -10.917 -6.729  14.645  1.00 14.73 ? 117 GLU A C   1 
ATOM   910  O  O   . GLU A 1 117 ? -10.055 -6.330  13.878  1.00 14.86 ? 117 GLU A O   1 
ATOM   911  C  CB  . GLU A 1 117 ? -9.701  -7.746  16.597  1.00 15.57 ? 117 GLU A CB  1 
ATOM   912  C  CG  . GLU A 1 117 ? -10.279 -6.855  17.717  1.00 15.61 ? 117 GLU A CG  1 
ATOM   913  C  CD  . GLU A 1 117 ? -9.370  -6.738  18.924  1.00 15.22 ? 117 GLU A CD  1 
ATOM   914  O  OE1 . GLU A 1 117 ? -8.717  -7.742  19.227  1.00 16.07 ? 117 GLU A OE1 1 
ATOM   915  O  OE2 . GLU A 1 117 ? -9.364  -5.643  19.582  1.00 18.31 ? 117 GLU A OE2 1 
ATOM   916  N  N   . LEU A 1 118 ? -12.104 -6.159  14.795  1.00 13.74 ? 118 LEU A N   1 
ATOM   917  C  CA  . LEU A 1 118 ? -12.460 -4.906  14.105  1.00 13.05 ? 118 LEU A CA  1 
ATOM   918  C  C   . LEU A 1 118 ? -12.219 -3.736  15.060  1.00 11.96 ? 118 LEU A C   1 
ATOM   919  O  O   . LEU A 1 118 ? -12.609 -3.784  16.181  1.00 13.83 ? 118 LEU A O   1 
ATOM   920  C  CB  . LEU A 1 118 ? -13.957 -4.947  13.738  1.00 13.57 ? 118 LEU A CB  1 
ATOM   921  C  CG  . LEU A 1 118 ? -14.703 -3.655  13.364  1.00 13.08 ? 118 LEU A CG  1 
ATOM   922  C  CD1 . LEU A 1 118 ? -14.154 -3.075  12.152  1.00 11.33 ? 118 LEU A CD1 1 
ATOM   923  C  CD2 . LEU A 1 118 ? -16.220 -4.068  13.191  1.00 14.04 ? 118 LEU A CD2 1 
ATOM   924  N  N   . HIS A 1 119 ? -11.666 -2.634  14.549  1.00 13.16 ? 119 HIS A N   1 
ATOM   925  C  CA  . HIS A 1 119 ? -11.456 -1.473  15.353  1.00 12.85 ? 119 HIS A CA  1 
ATOM   926  C  C   . HIS A 1 119 ? -12.140 -0.301  14.689  1.00 11.40 ? 119 HIS A C   1 
ATOM   927  O  O   . HIS A 1 119 ? -11.847 -0.020  13.559  1.00 12.61 ? 119 HIS A O   1 
ATOM   928  C  CB  . HIS A 1 119 ? -9.911  -1.211  15.450  1.00 12.39 ? 119 HIS A CB  1 
ATOM   929  C  CG  . HIS A 1 119 ? -9.232  -2.188  16.374  1.00 15.44 ? 119 HIS A CG  1 
ATOM   930  N  ND1 . HIS A 1 119 ? -7.873  -2.435  16.375  1.00 15.13 ? 119 HIS A ND1 1 
ATOM   931  C  CD2 . HIS A 1 119 ? -9.753  -2.960  17.355  1.00 11.00 ? 119 HIS A CD2 1 
ATOM   932  C  CE1 . HIS A 1 119 ? -7.588  -3.315  17.330  1.00 15.48 ? 119 HIS A CE1 1 
ATOM   933  N  NE2 . HIS A 1 119 ? -8.716  -3.684  17.905  1.00 15.92 ? 119 HIS A NE2 1 
ATOM   934  N  N   . LEU A 1 120 ? -13.114 0.297   15.385  1.00 13.77 ? 120 LEU A N   1 
ATOM   935  C  CA  . LEU A 1 120 ? -13.821 1.493   14.911  1.00 13.51 ? 120 LEU A CA  1 
ATOM   936  C  C   . LEU A 1 120 ? -13.212 2.638   15.737  1.00 13.08 ? 120 LEU A C   1 
ATOM   937  O  O   . LEU A 1 120 ? -13.287 2.657   16.922  1.00 14.25 ? 120 LEU A O   1 
ATOM   938  C  CB  . LEU A 1 120 ? -15.292 1.321   15.203  1.00 14.75 ? 120 LEU A CB  1 
ATOM   939  C  CG  . LEU A 1 120 ? -15.948 0.255   14.289  1.00 16.18 ? 120 LEU A CG  1 
ATOM   940  C  CD1 . LEU A 1 120 ? -16.684 -0.619  15.179  1.00 15.28 ? 120 LEU A CD1 1 
ATOM   941  C  CD2 . LEU A 1 120 ? -16.893 0.994   13.250  1.00 15.14 ? 120 LEU A CD2 1 
ATOM   942  N  N   . VAL A 1 121 ? -12.480 3.473   15.068  1.00 15.00 ? 121 VAL A N   1 
ATOM   943  C  CA  . VAL A 1 121 ? -11.577 4.422   15.719  1.00 15.57 ? 121 VAL A CA  1 
ATOM   944  C  C   . VAL A 1 121 ? -12.251 5.772   15.706  1.00 15.56 ? 121 VAL A C   1 
ATOM   945  O  O   . VAL A 1 121 ? -12.677 6.251   14.628  1.00 16.32 ? 121 VAL A O   1 
ATOM   946  C  CB  . VAL A 1 121 ? -10.283 4.578   14.830  1.00 16.08 ? 121 VAL A CB  1 
ATOM   947  C  CG1 . VAL A 1 121 ? -9.278  5.614   15.444  1.00 13.46 ? 121 VAL A CG1 1 
ATOM   948  C  CG2 . VAL A 1 121 ? -9.567  3.185   14.631  1.00 13.70 ? 121 VAL A CG2 1 
ATOM   949  N  N   . HIS A 1 122 ? -12.279 6.427   16.867  1.00 15.96 ? 122 HIS A N   1 
ATOM   950  C  CA  . HIS A 1 122 ? -13.098 7.642   17.012  1.00 15.98 ? 122 HIS A CA  1 
ATOM   951  C  C   . HIS A 1 122 ? -12.205 8.633   17.756  1.00 17.11 ? 122 HIS A C   1 
ATOM   952  O  O   . HIS A 1 122 ? -11.441 8.207   18.617  1.00 17.35 ? 122 HIS A O   1 
ATOM   953  C  CB  . HIS A 1 122 ? -14.322 7.425   17.908  1.00 15.61 ? 122 HIS A CB  1 
ATOM   954  C  CG  . HIS A 1 122 ? -15.223 6.308   17.505  1.00 17.61 ? 122 HIS A CG  1 
ATOM   955  N  ND1 . HIS A 1 122 ? -14.891 4.980   17.721  1.00 14.74 ? 122 HIS A ND1 1 
ATOM   956  C  CD2 . HIS A 1 122 ? -16.429 6.308   16.872  1.00 17.31 ? 122 HIS A CD2 1 
ATOM   957  C  CE1 . HIS A 1 122 ? -15.884 4.209   17.277  1.00 14.82 ? 122 HIS A CE1 1 
ATOM   958  N  NE2 . HIS A 1 122 ? -16.819 4.988   16.744  1.00 15.84 ? 122 HIS A NE2 1 
ATOM   959  N  N   . TRP A 1 123 ? -12.289 9.934   17.435  1.00 16.44 ? 123 TRP A N   1 
ATOM   960  C  CA  . TRP A 1 123 ? -11.489 10.937  18.174  1.00 15.90 ? 123 TRP A CA  1 
ATOM   961  C  C   . TRP A 1 123 ? -12.330 11.968  18.904  1.00 18.14 ? 123 TRP A C   1 
ATOM   962  O  O   . TRP A 1 123 ? -13.465 12.249  18.515  1.00 17.65 ? 123 TRP A O   1 
ATOM   963  C  CB  . TRP A 1 123 ? -10.461 11.612  17.279  1.00 17.33 ? 123 TRP A CB  1 
ATOM   964  C  CG  . TRP A 1 123 ? -11.059 12.205  15.999  1.00 20.49 ? 123 TRP A CG  1 
ATOM   965  C  CD1 . TRP A 1 123 ? -11.283 11.574  14.778  1.00 22.83 ? 123 TRP A CD1 1 
ATOM   966  C  CD2 . TRP A 1 123 ? -11.530 13.555  15.848  1.00 21.13 ? 123 TRP A CD2 1 
ATOM   967  N  NE1 . TRP A 1 123 ? -11.848 12.479  13.885  1.00 23.61 ? 123 TRP A NE1 1 
ATOM   968  C  CE2 . TRP A 1 123 ? -12.027 13.687  14.532  1.00 20.61 ? 123 TRP A CE2 1 
ATOM   969  C  CE3 . TRP A 1 123 ? -11.654 14.631  16.729  1.00 21.00 ? 123 TRP A CE3 1 
ATOM   970  C  CZ2 . TRP A 1 123 ? -12.621 14.894  14.060  1.00 21.96 ? 123 TRP A CZ2 1 
ATOM   971  C  CZ3 . TRP A 1 123 ? -12.231 15.837  16.249  1.00 20.25 ? 123 TRP A CZ3 1 
ATOM   972  C  CH2 . TRP A 1 123 ? -12.669 15.955  14.918  1.00 20.15 ? 123 TRP A CH2 1 
ATOM   973  N  N   . ASN A 1 124 ? -11.774 12.477  19.999  1.00 19.57 ? 124 ASN A N   1 
ATOM   974  C  CA  . ASN A 1 124 ? -12.470 13.304  20.948  1.00 20.80 ? 124 ASN A CA  1 
ATOM   975  C  C   . ASN A 1 124 ? -12.742 14.651  20.279  1.00 21.42 ? 124 ASN A C   1 
ATOM   976  O  O   . ASN A 1 124 ? -11.810 15.327  19.787  1.00 19.80 ? 124 ASN A O   1 
ATOM   977  C  CB  . ASN A 1 124 ? -11.637 13.491  22.221  1.00 20.81 ? 124 ASN A CB  1 
ATOM   978  C  CG  . ASN A 1 124 ? -12.492 14.002  23.379  1.00 22.24 ? 124 ASN A CG  1 
ATOM   979  O  OD1 . ASN A 1 124 ? -13.284 14.893  23.192  1.00 25.68 ? 124 ASN A OD1 1 
ATOM   980  N  ND2 . ASN A 1 124 ? -12.333 13.434  24.561  1.00 23.91 ? 124 ASN A ND2 1 
ATOM   981  N  N   . THR A 1 125 ? -14.013 15.039  20.223  1.00 22.31 ? 125 THR A N   1 
ATOM   982  C  CA  . THR A 1 125 ? -14.364 16.271  19.439  1.00 24.46 ? 125 THR A CA  1 
ATOM   983  C  C   . THR A 1 125 ? -13.695 17.543  20.043  1.00 25.54 ? 125 THR A C   1 
ATOM   984  O  O   . THR A 1 125 ? -13.488 18.561  19.377  1.00 26.69 ? 125 THR A O   1 
ATOM   985  C  CB  . THR A 1 125 ? -15.902 16.457  19.283  1.00 24.30 ? 125 THR A CB  1 
ATOM   986  O  OG1 . THR A 1 125 ? -16.521 16.356  20.554  1.00 25.55 ? 125 THR A OG1 1 
ATOM   987  C  CG2 . THR A 1 125 ? -16.471 15.389  18.387  1.00 24.59 ? 125 THR A CG2 1 
ATOM   988  N  N   . LYS A 1 126 ? -13.320 17.472  21.291  1.00 25.75 ? 127 LYS A N   1 
ATOM   989  C  CA  . LYS A 1 126 ? -12.792 18.668  21.915  1.00 26.13 ? 127 LYS A CA  1 
ATOM   990  C  C   . LYS A 1 126 ? -11.371 18.983  21.427  1.00 26.48 ? 127 LYS A C   1 
ATOM   991  O  O   . LYS A 1 126 ? -10.854 20.080  21.642  1.00 26.87 ? 127 LYS A O   1 
ATOM   992  C  CB  . LYS A 1 126 ? -13.001 18.518  23.416  1.00 27.05 ? 127 LYS A CB  1 
ATOM   993  C  CG  . LYS A 1 126 ? -11.989 17.731  24.121  1.00 29.68 ? 127 LYS A CG  1 
ATOM   994  C  CD  . LYS A 1 126 ? -12.432 17.483  25.572  1.00 35.27 ? 127 LYS A CD  1 
ATOM   995  C  CE  . LYS A 1 126 ? -11.412 16.580  26.261  1.00 38.51 ? 127 LYS A CE  1 
ATOM   996  N  NZ  . LYS A 1 126 ? -11.293 16.659  27.764  1.00 44.57 ? 127 LYS A NZ  1 
ATOM   997  N  N   . TYR A 1 127 ? -10.739 18.063  20.701  1.00 24.29 ? 128 TYR A N   1 
ATOM   998  C  CA  . TYR A 1 127 ? -9.374  18.342  20.207  1.00 24.69 ? 128 TYR A CA  1 
ATOM   999  C  C   . TYR A 1 127 ? -9.378  18.720  18.767  1.00 25.02 ? 128 TYR A C   1 
ATOM   1000 O  O   . TYR A 1 127 ? -8.315  18.888  18.140  1.00 26.20 ? 128 TYR A O   1 
ATOM   1001 C  CB  . TYR A 1 127 ? -8.451  17.150  20.467  1.00 24.58 ? 128 TYR A CB  1 
ATOM   1002 C  CG  . TYR A 1 127 ? -8.367  16.840  21.928  1.00 23.29 ? 128 TYR A CG  1 
ATOM   1003 C  CD1 . TYR A 1 127 ? -7.880  17.803  22.839  1.00 24.49 ? 128 TYR A CD1 1 
ATOM   1004 C  CD2 . TYR A 1 127 ? -8.709  15.611  22.412  1.00 23.97 ? 128 TYR A CD2 1 
ATOM   1005 C  CE1 . TYR A 1 127 ? -7.770  17.544  24.139  1.00 24.05 ? 128 TYR A CE1 1 
ATOM   1006 C  CE2 . TYR A 1 127 ? -8.626  15.321  23.770  1.00 22.62 ? 128 TYR A CE2 1 
ATOM   1007 C  CZ  . TYR A 1 127 ? -8.146  16.327  24.612  1.00 26.21 ? 128 TYR A CZ  1 
ATOM   1008 O  OH  . TYR A 1 127 ? -8.016  16.115  25.912  1.00 26.09 ? 128 TYR A OH  1 
ATOM   1009 N  N   . GLY A 1 128 ? -10.577 18.763  18.206  1.00 24.02 ? 129 GLY A N   1 
ATOM   1010 C  CA  . GLY A 1 128 ? -10.757 19.295  16.880  1.00 25.88 ? 129 GLY A CA  1 
ATOM   1011 C  C   . GLY A 1 128 ? -10.326 18.466  15.696  1.00 25.87 ? 129 GLY A C   1 
ATOM   1012 O  O   . GLY A 1 128 ? -10.842 18.617  14.600  1.00 25.84 ? 129 GLY A O   1 
ATOM   1013 N  N   . ASP A 1 129 ? -9.317  17.637  15.845  1.00 26.27 ? 130 ASP A N   1 
ATOM   1014 C  CA  . ASP A 1 129 ? -9.095  16.683  14.791  1.00 27.25 ? 130 ASP A CA  1 
ATOM   1015 C  C   . ASP A 1 129 ? -8.297  15.517  15.275  1.00 26.82 ? 130 ASP A C   1 
ATOM   1016 O  O   . ASP A 1 129 ? -7.854  15.546  16.397  1.00 26.64 ? 130 ASP A O   1 
ATOM   1017 C  CB  . ASP A 1 129 ? -8.512  17.277  13.533  1.00 29.02 ? 130 ASP A CB  1 
ATOM   1018 C  CG  . ASP A 1 129 ? -7.134  17.788  13.704  1.00 30.13 ? 130 ASP A CG  1 
ATOM   1019 O  OD1 . ASP A 1 129 ? -6.591  17.778  14.780  1.00 35.29 ? 130 ASP A OD1 1 
ATOM   1020 O  OD2 . ASP A 1 129 ? -6.573  18.238  12.724  1.00 34.35 ? 130 ASP A OD2 1 
ATOM   1021 N  N   . PHE A 1 130 ? -8.153  14.513  14.407  1.00 25.75 ? 131 PHE A N   1 
ATOM   1022 C  CA  . PHE A 1 130 ? -7.544  13.244  14.770  1.00 24.95 ? 131 PHE A CA  1 
ATOM   1023 C  C   . PHE A 1 130 ? -6.086  13.495  15.095  1.00 23.51 ? 131 PHE A C   1 
ATOM   1024 O  O   . PHE A 1 130 ? -5.587  12.997  16.088  1.00 19.81 ? 131 PHE A O   1 
ATOM   1025 C  CB  . PHE A 1 130 ? -7.629  12.208  13.634  1.00 21.78 ? 131 PHE A CB  1 
ATOM   1026 C  CG  . PHE A 1 130 ? -6.942  10.947  13.976  1.00 24.05 ? 131 PHE A CG  1 
ATOM   1027 C  CD1 . PHE A 1 130 ? -7.616  9.957   14.668  1.00 23.63 ? 131 PHE A CD1 1 
ATOM   1028 C  CD2 . PHE A 1 130 ? -5.598  10.748  13.694  1.00 24.01 ? 131 PHE A CD2 1 
ATOM   1029 C  CE1 . PHE A 1 130 ? -6.970  8.775   15.004  1.00 23.88 ? 131 PHE A CE1 1 
ATOM   1030 C  CE2 . PHE A 1 130 ? -4.933  9.577   14.075  1.00 27.95 ? 131 PHE A CE2 1 
ATOM   1031 C  CZ  . PHE A 1 130 ? -5.624  8.597   14.752  1.00 28.48 ? 131 PHE A CZ  1 
ATOM   1032 N  N   . GLY A 1 131 ? -5.391  14.247  14.232  1.00 23.24 ? 132 GLY A N   1 
ATOM   1033 C  CA  . GLY A 1 131 ? -3.966  14.451  14.486  1.00 24.30 ? 132 GLY A CA  1 
ATOM   1034 C  C   . GLY A 1 131 ? -3.646  15.093  15.825  1.00 24.21 ? 132 GLY A C   1 
ATOM   1035 O  O   . GLY A 1 131 ? -2.619  14.781  16.457  1.00 25.70 ? 132 GLY A O   1 
ATOM   1036 N  N   . LYS A 1 132 ? -4.532  15.966  16.295  1.00 24.22 ? 133 LYS A N   1 
ATOM   1037 C  CA  . LYS A 1 132 ? -4.344  16.560  17.621  1.00 24.25 ? 133 LYS A CA  1 
ATOM   1038 C  C   . LYS A 1 132 ? -4.804  15.625  18.709  1.00 23.68 ? 133 LYS A C   1 
ATOM   1039 O  O   . LYS A 1 132 ? -4.164  15.539  19.740  1.00 24.26 ? 133 LYS A O   1 
ATOM   1040 C  CB  . LYS A 1 132 ? -5.127  17.867  17.759  1.00 24.12 ? 133 LYS A CB  1 
ATOM   1041 C  CG  . LYS A 1 132 ? -4.575  19.040  16.907  1.00 30.21 ? 133 LYS A CG  1 
ATOM   1042 C  CD  . LYS A 1 132 ? -3.220  19.598  17.355  1.00 39.65 ? 133 LYS A CD  1 
ATOM   1043 C  CE  . LYS A 1 132 ? -3.283  20.203  18.738  1.00 41.01 ? 133 LYS A CE  1 
ATOM   1044 N  NZ  . LYS A 1 132 ? -1.876  20.689  19.028  1.00 46.88 ? 133 LYS A NZ  1 
ATOM   1045 N  N   . ALA A 1 133 ? -5.950  14.976  18.525  1.00 21.82 ? 134 ALA A N   1 
ATOM   1046 C  CA  . ALA A 1 133 ? -6.462  14.027  19.560  1.00 22.37 ? 134 ALA A CA  1 
ATOM   1047 C  C   . ALA A 1 133 ? -5.417  12.940  19.970  1.00 21.71 ? 134 ALA A C   1 
ATOM   1048 O  O   . ALA A 1 133 ? -5.337  12.586  21.150  1.00 20.94 ? 134 ALA A O   1 
ATOM   1049 C  CB  . ALA A 1 133 ? -7.767  13.356  19.069  1.00 21.87 ? 134 ALA A CB  1 
ATOM   1050 N  N   . VAL A 1 134 ? -4.676  12.386  19.009  1.00 21.32 ? 135 VAL A N   1 
ATOM   1051 C  CA  . VAL A 1 134 ? -3.705  11.298  19.334  1.00 23.96 ? 135 VAL A CA  1 
ATOM   1052 C  C   . VAL A 1 134 ? -2.582  11.701  20.228  1.00 24.77 ? 135 VAL A C   1 
ATOM   1053 O  O   . VAL A 1 134 ? -1.932  10.847  20.842  1.00 25.88 ? 135 VAL A O   1 
ATOM   1054 C  CB  . VAL A 1 134 ? -3.088  10.541  18.103  1.00 25.15 ? 135 VAL A CB  1 
ATOM   1055 C  CG1 . VAL A 1 134 ? -4.129  9.837   17.433  1.00 23.77 ? 135 VAL A CG1 1 
ATOM   1056 C  CG2 . VAL A 1 134 ? -2.289  11.474  17.152  1.00 23.29 ? 135 VAL A CG2 1 
ATOM   1057 N  N   . GLN A 1 135 ? -2.371  13.008  20.345  1.00 24.93 ? 136 GLN A N   1 
ATOM   1058 C  CA  . GLN A 1 135 ? -1.380  13.524  21.256  1.00 26.44 ? 136 GLN A CA  1 
ATOM   1059 C  C   . GLN A 1 135 ? -1.958  13.706  22.634  1.00 25.09 ? 136 GLN A C   1 
ATOM   1060 O  O   . GLN A 1 135 ? -1.314  14.295  23.499  1.00 25.55 ? 136 GLN A O   1 
ATOM   1061 C  CB  . GLN A 1 135 ? -0.878  14.870  20.717  1.00 25.85 ? 136 GLN A CB  1 
ATOM   1062 C  CG  . GLN A 1 135 ? -0.335  14.742  19.301  1.00 28.29 ? 136 GLN A CG  1 
ATOM   1063 C  CD  . GLN A 1 135 ? -0.124  16.143  18.632  1.00 33.48 ? 136 GLN A CD  1 
ATOM   1064 O  OE1 . GLN A 1 135 ? 0.154   16.216  17.420  1.00 44.63 ? 136 GLN A OE1 1 
ATOM   1065 N  NE2 . GLN A 1 135 ? -0.267  17.250  19.423  1.00 41.05 ? 136 GLN A NE2 1 
ATOM   1066 N  N   . GLN A 1 136 ? -3.190  13.275  22.875  1.00 23.87 ? 137 GLN A N   1 
ATOM   1067 C  CA  . GLN A 1 136 ? -3.788  13.488  24.202  1.00 22.15 ? 137 GLN A CA  1 
ATOM   1068 C  C   . GLN A 1 136 ? -4.174  12.193  24.900  1.00 21.34 ? 137 GLN A C   1 
ATOM   1069 O  O   . GLN A 1 136 ? -4.587  11.259  24.240  1.00 21.72 ? 137 GLN A O   1 
ATOM   1070 C  CB  . GLN A 1 136 ? -5.025  14.318  24.110  1.00 21.79 ? 137 GLN A CB  1 
ATOM   1071 C  CG  . GLN A 1 136 ? -4.957  15.489  23.157  1.00 24.79 ? 137 GLN A CG  1 
ATOM   1072 C  CD  . GLN A 1 136 ? -3.958  16.568  23.600  1.00 30.08 ? 137 GLN A CD  1 
ATOM   1073 O  OE1 . GLN A 1 136 ? -3.330  17.261  22.743  1.00 36.11 ? 137 GLN A OE1 1 
ATOM   1074 N  NE2 . GLN A 1 136 ? -3.815  16.719  24.896  1.00 24.41 ? 137 GLN A NE2 1 
ATOM   1075 N  N   . PRO A 1 137 ? -4.143  12.162  26.225  1.00 21.86 ? 138 PRO A N   1 
ATOM   1076 C  CA  . PRO A 1 137 ? -4.399  10.880  26.915  1.00 21.57 ? 138 PRO A CA  1 
ATOM   1077 C  C   . PRO A 1 137 ? -5.823  10.410  26.783  1.00 22.96 ? 138 PRO A C   1 
ATOM   1078 O  O   . PRO A 1 137 ? -6.062  9.198   26.918  1.00 22.79 ? 138 PRO A O   1 
ATOM   1079 C  CB  . PRO A 1 137 ? -4.076  11.174  28.381  1.00 22.31 ? 138 PRO A CB  1 
ATOM   1080 C  CG  . PRO A 1 137 ? -4.396  12.729  28.473  1.00 23.02 ? 138 PRO A CG  1 
ATOM   1081 C  CD  . PRO A 1 137 ? -3.830  13.263  27.166  1.00 22.19 ? 138 PRO A CD  1 
ATOM   1082 N  N   . ASP A 1 138 ? -6.762  11.329  26.499  1.00 21.00 ? 139 ASP A N   1 
ATOM   1083 C  CA  . ASP A 1 138 ? -8.133  10.974  26.249  1.00 22.30 ? 139 ASP A CA  1 
ATOM   1084 C  C   . ASP A 1 138 ? -8.562  11.277  24.784  1.00 19.85 ? 139 ASP A C   1 
ATOM   1085 O  O   . ASP A 1 138 ? -9.702  11.612  24.511  1.00 21.55 ? 139 ASP A O   1 
ATOM   1086 C  CB  . ASP A 1 138 ? -9.046  11.687  27.263  1.00 23.50 ? 139 ASP A CB  1 
ATOM   1087 C  CG  . ASP A 1 138 ? -8.908  13.177  27.190  1.00 27.64 ? 139 ASP A CG  1 
ATOM   1088 O  OD1 . ASP A 1 138 ? -7.924  13.678  26.550  1.00 26.46 ? 139 ASP A OD1 1 
ATOM   1089 O  OD2 . ASP A 1 138 ? -9.809  13.838  27.749  1.00 30.48 ? 139 ASP A OD2 1 
ATOM   1090 N  N   . GLY A 1 139 ? -7.634  11.122  23.855  1.00 19.64 ? 140 GLY A N   1 
ATOM   1091 C  CA  . GLY A 1 139 ? -7.787  11.591  22.530  1.00 17.44 ? 140 GLY A CA  1 
ATOM   1092 C  C   . GLY A 1 139 ? -8.701  10.695  21.712  1.00 16.58 ? 140 GLY A C   1 
ATOM   1093 O  O   . GLY A 1 139 ? -9.408  11.191  20.852  1.00 16.21 ? 140 GLY A O   1 
ATOM   1094 N  N   . LEU A 1 140 ? -8.657  9.378   21.969  1.00 15.24 ? 141 LEU A N   1 
ATOM   1095 C  CA  . LEU A 1 140 ? -9.345  8.411   21.099  1.00 15.95 ? 141 LEU A CA  1 
ATOM   1096 C  C   . LEU A 1 140 ? -10.204 7.483   21.904  1.00 16.26 ? 141 LEU A C   1 
ATOM   1097 O  O   . LEU A 1 140 ? -9.975  7.251   23.126  1.00 17.22 ? 141 LEU A O   1 
ATOM   1098 C  CB  . LEU A 1 140 ? -8.354  7.573   20.227  1.00 15.99 ? 141 LEU A CB  1 
ATOM   1099 C  CG  . LEU A 1 140 ? -7.405  8.230   19.230  1.00 21.89 ? 141 LEU A CG  1 
ATOM   1100 C  CD1 . LEU A 1 140 ? -6.686  7.186   18.319  1.00 21.15 ? 141 LEU A CD1 1 
ATOM   1101 C  CD2 . LEU A 1 140 ? -8.072  9.326   18.363  1.00 24.32 ? 141 LEU A CD2 1 
ATOM   1102 N  N   . ALA A 1 141 ? -11.215 6.965   21.223  1.00 16.38 ? 142 ALA A N   1 
ATOM   1103 C  CA  . ALA A 1 141 ? -12.043 5.884   21.751  1.00 16.65 ? 142 ALA A CA  1 
ATOM   1104 C  C   . ALA A 1 141 ? -12.083 4.878   20.614  1.00 16.46 ? 142 ALA A C   1 
ATOM   1105 O  O   . ALA A 1 141 ? -12.471 5.213   19.521  1.00 14.83 ? 142 ALA A O   1 
ATOM   1106 C  CB  . ALA A 1 141 ? -13.477 6.369   22.105  1.00 17.58 ? 142 ALA A CB  1 
ATOM   1107 N  N   . VAL A 1 142 ? -11.598 3.655   20.881  1.00 16.77 ? 143 VAL A N   1 
ATOM   1108 C  CA  . VAL A 1 142 ? -11.594 2.667   19.821  1.00 16.47 ? 143 VAL A CA  1 
ATOM   1109 C  C   . VAL A 1 142 ? -12.516 1.554   20.286  1.00 15.08 ? 143 VAL A C   1 
ATOM   1110 O  O   . VAL A 1 142 ? -12.347 1.042   21.402  1.00 15.54 ? 143 VAL A O   1 
ATOM   1111 C  CB  . VAL A 1 142 ? -10.227 2.102   19.455  1.00 16.75 ? 143 VAL A CB  1 
ATOM   1112 C  CG1 . VAL A 1 142 ? -10.445 1.060   18.333  1.00 15.65 ? 143 VAL A CG1 1 
ATOM   1113 C  CG2 . VAL A 1 142 ? -9.265  3.236   18.995  1.00 14.40 ? 143 VAL A CG2 1 
ATOM   1114 N  N   . LEU A 1 143 ? -13.503 1.266   19.452  1.00 14.60 ? 144 LEU A N   1 
ATOM   1115 C  CA  . LEU A 1 143 ? -14.509 0.206   19.742  1.00 15.43 ? 144 LEU A CA  1 
ATOM   1116 C  C   . LEU A 1 143 ? -13.993 -1.040  19.013  1.00 14.41 ? 144 LEU A C   1 
ATOM   1117 O  O   . LEU A 1 143 ? -13.864 -1.029  17.817  1.00 16.02 ? 144 LEU A O   1 
ATOM   1118 C  CB  . LEU A 1 143 ? -15.885 0.634   19.202  1.00 15.40 ? 144 LEU A CB  1 
ATOM   1119 C  CG  . LEU A 1 143 ? -17.027 -0.329  19.376  1.00 16.98 ? 144 LEU A CG  1 
ATOM   1120 C  CD1 . LEU A 1 143 ? -17.183 -0.535  20.849  1.00 13.45 ? 144 LEU A CD1 1 
ATOM   1121 C  CD2 . LEU A 1 143 ? -18.369 0.183   18.765  1.00 17.12 ? 144 LEU A CD2 1 
ATOM   1122 N  N   . GLY A 1 144 ? -13.687 -2.075  19.798  1.00 15.03 ? 145 GLY A N   1 
ATOM   1123 C  CA  . GLY A 1 144 ? -13.121 -3.356  19.342  1.00 14.61 ? 145 GLY A CA  1 
ATOM   1124 C  C   . GLY A 1 144 ? -14.196 -4.405  19.332  1.00 11.29 ? 145 GLY A C   1 
ATOM   1125 O  O   . GLY A 1 144 ? -14.863 -4.546  20.319  1.00 14.63 ? 145 GLY A O   1 
ATOM   1126 N  N   . ILE A 1 145 ? -14.291 -5.164  18.248  1.00 13.30 ? 146 ILE A N   1 
ATOM   1127 C  CA  . ILE A 1 145 ? -15.327 -6.150  18.106  1.00 13.92 ? 146 ILE A CA  1 
ATOM   1128 C  C   . ILE A 1 145 ? -14.567 -7.353  17.572  1.00 13.79 ? 146 ILE A C   1 
ATOM   1129 O  O   . ILE A 1 145 ? -13.914 -7.307  16.529  1.00 14.16 ? 146 ILE A O   1 
ATOM   1130 C  CB  . ILE A 1 145 ? -16.396 -5.687  17.067  1.00 12.53 ? 146 ILE A CB  1 
ATOM   1131 C  CG1 . ILE A 1 145 ? -17.058 -4.393  17.613  1.00 14.63 ? 146 ILE A CG1 1 
ATOM   1132 C  CG2 . ILE A 1 145 ? -17.415 -6.825  16.828  1.00 15.92 ? 146 ILE A CG2 1 
ATOM   1133 C  CD1 . ILE A 1 145 ? -18.185 -3.777  16.652  1.00 13.30 ? 146 ILE A CD1 1 
ATOM   1134 N  N   . PHE A 1 146 ? -14.693 -8.434  18.317  1.00 16.23 ? 147 PHE A N   1 
ATOM   1135 C  CA  . PHE A 1 146 ? -14.066 -9.728  17.877  1.00 15.70 ? 147 PHE A CA  1 
ATOM   1136 C  C   . PHE A 1 146 ? -14.837 -10.363 16.750  1.00 15.76 ? 147 PHE A C   1 
ATOM   1137 O  O   . PHE A 1 146 ? -16.048 -10.215 16.668  1.00 14.94 ? 147 PHE A O   1 
ATOM   1138 C  CB  . PHE A 1 146 ? -14.040 -10.689 19.042  1.00 15.26 ? 147 PHE A CB  1 
ATOM   1139 C  CG  . PHE A 1 146 ? -13.279 -10.208 20.184  1.00 15.44 ? 147 PHE A CG  1 
ATOM   1140 C  CD1 . PHE A 1 146 ? -11.888 -10.087 20.089  1.00 18.37 ? 147 PHE A CD1 1 
ATOM   1141 C  CD2 . PHE A 1 146 ? -13.880 -9.972  21.399  1.00 15.77 ? 147 PHE A CD2 1 
ATOM   1142 C  CE1 . PHE A 1 146 ? -11.137 -9.690  21.191  1.00 15.36 ? 147 PHE A CE1 1 
ATOM   1143 C  CE2 . PHE A 1 146 ? -13.147 -9.556  22.485  1.00 16.83 ? 147 PHE A CE2 1 
ATOM   1144 C  CZ  . PHE A 1 146 ? -11.773 -9.431  22.387  1.00 17.98 ? 147 PHE A CZ  1 
ATOM   1145 N  N   . LEU A 1 147 ? -14.117 -10.981 15.797  1.00 16.08 ? 148 LEU A N   1 
ATOM   1146 C  CA  . LEU A 1 147 ? -14.725 -11.810 14.774  1.00 15.02 ? 148 LEU A CA  1 
ATOM   1147 C  C   . LEU A 1 147 ? -14.421 -13.266 14.998  1.00 17.53 ? 148 LEU A C   1 
ATOM   1148 O  O   . LEU A 1 147 ? -13.255 -13.615 15.173  1.00 16.02 ? 148 LEU A O   1 
ATOM   1149 C  CB  . LEU A 1 147 ? -14.236 -11.477 13.367  1.00 15.45 ? 148 LEU A CB  1 
ATOM   1150 C  CG  . LEU A 1 147 ? -14.836 -10.221 12.658  1.00 13.39 ? 148 LEU A CG  1 
ATOM   1151 C  CD1 . LEU A 1 147 ? -14.696 -8.914  13.470  1.00 15.74 ? 148 LEU A CD1 1 
ATOM   1152 C  CD2 . LEU A 1 147 ? -14.077 -10.035 11.355  1.00 16.39 ? 148 LEU A CD2 1 
ATOM   1153 N  N   . LYS A 1 148 ? -15.461 -14.110 14.975  1.00 19.28 ? 149 LYS A N   1 
ATOM   1154 C  CA  . LYS A 1 148 ? -15.239 -15.567 14.891  1.00 21.05 ? 149 LYS A CA  1 
ATOM   1155 C  C   . LYS A 1 148 ? -15.799 -16.112 13.613  1.00 20.86 ? 149 LYS A C   1 
ATOM   1156 O  O   . LYS A 1 148 ? -16.627 -15.480 12.984  1.00 19.67 ? 149 LYS A O   1 
ATOM   1157 C  CB  . LYS A 1 148 ? -15.854 -16.325 16.057  1.00 22.84 ? 149 LYS A CB  1 
ATOM   1158 C  CG  . LYS A 1 148 ? -17.372 -16.340 16.109  1.00 25.35 ? 149 LYS A CG  1 
ATOM   1159 C  CD  . LYS A 1 148 ? -17.864 -16.962 17.409  1.00 32.04 ? 149 LYS A CD  1 
ATOM   1160 C  CE  . LYS A 1 148 ? -19.403 -16.931 17.325  1.00 37.82 ? 149 LYS A CE  1 
ATOM   1161 N  NZ  . LYS A 1 148 ? -20.120 -17.129 18.630  1.00 46.03 ? 149 LYS A NZ  1 
ATOM   1162 N  N   . VAL A 1 149 ? -15.337 -17.319 13.233  1.00 20.53 ? 150 VAL A N   1 
ATOM   1163 C  CA  . VAL A 1 149 ? -15.665 -17.870 11.961  1.00 19.94 ? 150 VAL A CA  1 
ATOM   1164 C  C   . VAL A 1 149 ? -16.912 -18.753 12.193  1.00 21.82 ? 150 VAL A C   1 
ATOM   1165 O  O   . VAL A 1 149 ? -16.973 -19.619 13.118  1.00 21.04 ? 150 VAL A O   1 
ATOM   1166 C  CB  . VAL A 1 149 ? -14.502 -18.609 11.316  1.00 21.23 ? 150 VAL A CB  1 
ATOM   1167 C  CG1 . VAL A 1 149 ? -14.891 -19.320 10.036  1.00 17.06 ? 150 VAL A CG1 1 
ATOM   1168 C  CG2 . VAL A 1 149 ? -13.358 -17.635 10.999  1.00 20.85 ? 150 VAL A CG2 1 
ATOM   1169 N  N   . GLY A 1 150 ? -17.901 -18.493 11.358  1.00 19.93 ? 151 GLY A N   1 
ATOM   1170 C  CA  . GLY A 1 150 ? -19.158 -19.230 11.389  1.00 21.38 ? 151 GLY A CA  1 
ATOM   1171 C  C   . GLY A 1 150 ? -20.035 -18.793 10.247  1.00 19.28 ? 151 GLY A C   1 
ATOM   1172 O  O   . GLY A 1 150 ? -19.627 -18.840 9.081   1.00 19.63 ? 151 GLY A O   1 
ATOM   1173 N  N   A SER A 1 151 ? -21.258 -18.390 10.574  0.50 20.81 ? 152 SER A N   1 
ATOM   1174 N  N   B SER A 1 151 ? -21.266 -18.394 10.563  0.50 21.05 ? 152 SER A N   1 
ATOM   1175 C  CA  A SER A 1 151 ? -22.127 -17.800 9.548   0.50 20.73 ? 152 SER A CA  1 
ATOM   1176 C  CA  B SER A 1 151 ? -22.163 -17.844 9.522   0.50 21.29 ? 152 SER A CA  1 
ATOM   1177 C  C   A SER A 1 151 ? -21.508 -16.496 9.020   0.50 20.78 ? 152 SER A C   1 
ATOM   1178 C  C   B SER A 1 151 ? -21.630 -16.481 9.063   0.50 21.06 ? 152 SER A C   1 
ATOM   1179 O  O   A SER A 1 151 ? -20.704 -15.867 9.690   0.50 19.81 ? 152 SER A O   1 
ATOM   1180 O  O   B SER A 1 151 ? -21.006 -15.783 9.847   0.50 20.35 ? 152 SER A O   1 
ATOM   1181 C  CB  A SER A 1 151 ? -23.531 -17.555 10.070  0.50 21.19 ? 152 SER A CB  1 
ATOM   1182 C  CB  B SER A 1 151 ? -23.602 -17.703 10.008  0.50 21.66 ? 152 SER A CB  1 
ATOM   1183 O  OG  A SER A 1 151 ? -23.500 -16.641 11.144  0.50 20.24 ? 152 SER A OG  1 
ATOM   1184 O  OG  B SER A 1 151 ? -23.820 -18.452 11.186  0.50 23.37 ? 152 SER A OG  1 
ATOM   1185 N  N   . ALA A 1 152 ? -21.834 -16.154 7.788   1.00 21.10 ? 153 ALA A N   1 
ATOM   1186 C  CA  . ALA A 1 152 ? -21.407 -14.878 7.198   1.00 20.69 ? 153 ALA A CA  1 
ATOM   1187 C  C   . ALA A 1 152 ? -21.981 -13.675 7.916   1.00 21.97 ? 153 ALA A C   1 
ATOM   1188 O  O   . ALA A 1 152 ? -23.019 -13.778 8.575   1.00 23.13 ? 153 ALA A O   1 
ATOM   1189 C  CB  . ALA A 1 152 ? -21.789 -14.842 5.755   1.00 20.61 ? 153 ALA A CB  1 
ATOM   1190 N  N   . LYS A 1 153 ? -21.304 -12.524 7.802   1.00 21.99 ? 154 LYS A N   1 
ATOM   1191 C  CA  . LYS A 1 153 ? -21.848 -11.265 8.285   1.00 22.12 ? 154 LYS A CA  1 
ATOM   1192 C  C   . LYS A 1 153 ? -22.194 -10.502 7.015   1.00 21.70 ? 154 LYS A C   1 
ATOM   1193 O  O   . LYS A 1 153 ? -21.296 -10.063 6.253   1.00 20.67 ? 154 LYS A O   1 
ATOM   1194 C  CB  . LYS A 1 153 ? -20.775 -10.484 9.104   1.00 23.17 ? 154 LYS A CB  1 
ATOM   1195 C  CG  . LYS A 1 153 ? -21.346 -9.326  9.918   1.00 23.30 ? 154 LYS A CG  1 
ATOM   1196 C  CD  . LYS A 1 153 ? -22.168 -9.882  11.094  1.00 25.65 ? 154 LYS A CD  1 
ATOM   1197 C  CE  . LYS A 1 153 ? -22.657 -8.745  12.044  1.00 24.96 ? 154 LYS A CE  1 
ATOM   1198 N  NZ  . LYS A 1 153 ? -23.689 -9.173  13.030  1.00 26.23 ? 154 LYS A NZ  1 
ATOM   1199 N  N   . PRO A 1 154 ? -23.500 -10.431 6.683   1.00 22.76 ? 155 PRO A N   1 
ATOM   1200 C  CA  . PRO A 1 154 ? -23.887 -9.888  5.375   1.00 22.70 ? 155 PRO A CA  1 
ATOM   1201 C  C   . PRO A 1 154 ? -23.359 -8.439  5.257   1.00 22.22 ? 155 PRO A C   1 
ATOM   1202 O  O   . PRO A 1 154 ? -22.896 -8.017  4.172   1.00 23.90 ? 155 PRO A O   1 
ATOM   1203 C  CB  . PRO A 1 154 ? -25.448 -9.864  5.452   1.00 24.10 ? 155 PRO A CB  1 
ATOM   1204 C  CG  . PRO A 1 154 ? -25.803 -10.785 6.530   1.00 24.45 ? 155 PRO A CG  1 
ATOM   1205 C  CD  . PRO A 1 154 ? -24.667 -10.810 7.511   1.00 23.72 ? 155 PRO A CD  1 
ATOM   1206 N  N   . GLY A 1 155 ? -23.364 -7.726  6.390   1.00 22.56 ? 156 GLY A N   1 
ATOM   1207 C  CA  . GLY A 1 155 ? -22.975 -6.304  6.435   1.00 24.21 ? 156 GLY A CA  1 
ATOM   1208 C  C   . GLY A 1 155 ? -21.501 -6.067  6.197   1.00 24.82 ? 156 GLY A C   1 
ATOM   1209 O  O   . GLY A 1 155 ? -21.096 -4.932  5.984   1.00 26.66 ? 156 GLY A O   1 
ATOM   1210 N  N   . LEU A 1 156 ? -20.696 -7.141  6.217   1.00 22.81 ? 157 LEU A N   1 
ATOM   1211 C  CA  . LEU A 1 156 ? -19.295 -7.075  5.876   1.00 20.65 ? 157 LEU A CA  1 
ATOM   1212 C  C   . LEU A 1 156 ? -19.059 -7.324  4.453   1.00 20.04 ? 157 LEU A C   1 
ATOM   1213 O  O   . LEU A 1 156 ? -17.973 -7.114  3.940   1.00 17.65 ? 157 LEU A O   1 
ATOM   1214 C  CB  . LEU A 1 156 ? -18.517 -8.135  6.721   1.00 21.86 ? 157 LEU A CB  1 
ATOM   1215 C  CG  . LEU A 1 156 ? -16.991 -8.307  6.523   1.00 17.87 ? 157 LEU A CG  1 
ATOM   1216 C  CD1 . LEU A 1 156 ? -16.217 -7.044  6.988   1.00 17.11 ? 157 LEU A CD1 1 
ATOM   1217 C  CD2 . LEU A 1 156 ? -16.449 -9.490  7.261   1.00 17.87 ? 157 LEU A CD2 1 
ATOM   1218 N  N   . GLN A 1 157 ? -20.048 -7.853  3.736   1.00 22.10 ? 158 GLN A N   1 
ATOM   1219 C  CA  . GLN A 1 157 ? -19.684 -8.297  2.378   1.00 22.62 ? 158 GLN A CA  1 
ATOM   1220 C  C   . GLN A 1 157 ? -19.273 -7.185  1.419   1.00 22.69 ? 158 GLN A C   1 
ATOM   1221 O  O   . GLN A 1 157 ? -18.414 -7.383  0.574   1.00 22.23 ? 158 GLN A O   1 
ATOM   1222 C  CB  . GLN A 1 157 ? -20.765 -9.189  1.766   1.00 23.59 ? 158 GLN A CB  1 
ATOM   1223 C  CG  . GLN A 1 157 ? -20.312 -9.838  0.472   1.00 25.18 ? 158 GLN A CG  1 
ATOM   1224 C  CD  . GLN A 1 157 ? -19.295 -10.940 0.694   1.00 23.93 ? 158 GLN A CD  1 
ATOM   1225 O  OE1 . GLN A 1 157 ? -19.231 -11.528 1.760   1.00 25.94 ? 158 GLN A OE1 1 
ATOM   1226 N  NE2 . GLN A 1 157 ? -18.490 -11.188 -0.291  1.00 25.94 ? 158 GLN A NE2 1 
ATOM   1227 N  N   . LYS A 1 158 ? -19.876 -6.013  1.537   1.00 24.31 ? 159 LYS A N   1 
ATOM   1228 C  CA  . LYS A 1 158 ? -19.492 -4.919  0.662   1.00 25.60 ? 159 LYS A CA  1 
ATOM   1229 C  C   . LYS A 1 158 ? -18.013 -4.652  0.810   1.00 23.26 ? 159 LYS A C   1 
ATOM   1230 O  O   . LYS A 1 158 ? -17.308 -4.326  -0.152  1.00 21.33 ? 159 LYS A O   1 
ATOM   1231 C  CB  . LYS A 1 158 ? -20.306 -3.640  0.975   1.00 28.32 ? 159 LYS A CB  1 
ATOM   1232 C  CG  . LYS A 1 158 ? -21.824 -3.782  0.774   1.00 33.34 ? 159 LYS A CG  1 
ATOM   1233 C  CD  . LYS A 1 158 ? -22.560 -2.399  0.711   1.00 32.94 ? 159 LYS A CD  1 
ATOM   1234 C  CE  . LYS A 1 158 ? -24.016 -2.535  0.159   1.00 37.76 ? 159 LYS A CE  1 
ATOM   1235 N  NZ  . LYS A 1 158 ? -24.959 -1.325  0.519   1.00 40.68 ? 159 LYS A NZ  1 
ATOM   1236 N  N   . VAL A 1 159 ? -17.511 -4.833  2.029   1.00 22.19 ? 160 VAL A N   1 
ATOM   1237 C  CA  . VAL A 1 159 ? -16.096 -4.628  2.262   1.00 20.66 ? 160 VAL A CA  1 
ATOM   1238 C  C   . VAL A 1 159 ? -15.289 -5.714  1.581   1.00 20.49 ? 160 VAL A C   1 
ATOM   1239 O  O   . VAL A 1 159 ? -14.280 -5.445  0.918   1.00 20.63 ? 160 VAL A O   1 
ATOM   1240 C  CB  . VAL A 1 159 ? -15.819 -4.626  3.790   1.00 20.45 ? 160 VAL A CB  1 
ATOM   1241 C  CG1 . VAL A 1 159 ? -14.315 -4.765  4.087   1.00 22.90 ? 160 VAL A CG1 1 
ATOM   1242 C  CG2 . VAL A 1 159 ? -16.432 -3.377  4.463   1.00 20.75 ? 160 VAL A CG2 1 
ATOM   1243 N  N   . VAL A 1 160 ? -15.689 -6.976  1.827   1.00 20.49 ? 161 VAL A N   1 
ATOM   1244 C  CA  . VAL A 1 160 ? -14.958 -8.132  1.282   1.00 22.83 ? 161 VAL A CA  1 
ATOM   1245 C  C   . VAL A 1 160 ? -14.860 -8.031  -0.243  1.00 21.68 ? 161 VAL A C   1 
ATOM   1246 O  O   . VAL A 1 160 ? -13.793 -8.212  -0.834  1.00 20.16 ? 161 VAL A O   1 
ATOM   1247 C  CB  . VAL A 1 160 ? -15.677 -9.469  1.829   1.00 23.61 ? 161 VAL A CB  1 
ATOM   1248 C  CG1 . VAL A 1 160 ? -15.379 -10.632 0.972   1.00 25.72 ? 161 VAL A CG1 1 
ATOM   1249 C  CG2 . VAL A 1 160 ? -15.227 -9.691  3.241   1.00 24.76 ? 161 VAL A CG2 1 
ATOM   1250 N  N   . ASP A 1 161 ? -15.945 -7.625  -0.887  1.00 24.45 ? 162 ASP A N   1 
ATOM   1251 C  CA  . ASP A 1 161 ? -15.932 -7.557  -2.348  1.00 26.97 ? 162 ASP A CA  1 
ATOM   1252 C  C   . ASP A 1 161 ? -15.028 -6.524  -3.040  1.00 28.12 ? 162 ASP A C   1 
ATOM   1253 O  O   . ASP A 1 161 ? -14.746 -6.682  -4.243  1.00 30.44 ? 162 ASP A O   1 
ATOM   1254 C  CB  . ASP A 1 161 ? -17.363 -7.388  -2.868  1.00 27.87 ? 162 ASP A CB  1 
ATOM   1255 C  CG  . ASP A 1 161 ? -18.186 -8.655  -2.689  1.00 31.89 ? 162 ASP A CG  1 
ATOM   1256 O  OD1 . ASP A 1 161 ? -17.569 -9.745  -2.719  1.00 33.73 ? 162 ASP A OD1 1 
ATOM   1257 O  OD2 . ASP A 1 161 ? -19.439 -8.543  -2.478  1.00 35.84 ? 162 ASP A OD2 1 
ATOM   1258 N  N   . VAL A 1 162 ? -14.624 -5.465  -2.328  1.00 27.34 ? 163 VAL A N   1 
ATOM   1259 C  CA  . VAL A 1 162 ? -13.773 -4.408  -2.899  1.00 26.41 ? 163 VAL A CA  1 
ATOM   1260 C  C   . VAL A 1 162 ? -12.299 -4.730  -2.719  1.00 25.11 ? 163 VAL A C   1 
ATOM   1261 O  O   . VAL A 1 162 ? -11.449 -4.144  -3.375  1.00 25.23 ? 163 VAL A O   1 
ATOM   1262 C  CB  . VAL A 1 162 ? -14.180 -3.034  -2.312  1.00 26.68 ? 163 VAL A CB  1 
ATOM   1263 C  CG1 . VAL A 1 162 ? -13.489 -2.778  -1.025  1.00 24.24 ? 163 VAL A CG1 1 
ATOM   1264 C  CG2 . VAL A 1 162 ? -13.858 -1.914  -3.242  1.00 31.16 ? 163 VAL A CG2 1 
ATOM   1265 N  N   . LEU A 1 163 ? -11.963 -5.692  -1.836  1.00 24.34 ? 164 LEU A N   1 
ATOM   1266 C  CA  . LEU A 1 163 ? -10.556 -5.914  -1.482  1.00 23.59 ? 164 LEU A CA  1 
ATOM   1267 C  C   . LEU A 1 163 ? -9.634  -6.232  -2.662  1.00 24.25 ? 164 LEU A C   1 
ATOM   1268 O  O   . LEU A 1 163 ? -8.465  -5.898  -2.639  1.00 22.19 ? 164 LEU A O   1 
ATOM   1269 C  CB  . LEU A 1 163 ? -10.381 -6.991  -0.412  1.00 22.36 ? 164 LEU A CB  1 
ATOM   1270 C  CG  . LEU A 1 163 ? -11.009 -6.751  0.973   1.00 22.17 ? 164 LEU A CG  1 
ATOM   1271 C  CD1 . LEU A 1 163 ? -10.619 -7.918  1.850   1.00 25.96 ? 164 LEU A CD1 1 
ATOM   1272 C  CD2 . LEU A 1 163 ? -10.633 -5.427  1.679   1.00 23.08 ? 164 LEU A CD2 1 
ATOM   1273 N  N   . ASP A 1 164 ? -10.155 -6.913  -3.682  1.00 27.15 ? 165 ASP A N   1 
ATOM   1274 C  CA  . ASP A 1 164 ? -9.337  -7.260  -4.861  1.00 30.37 ? 165 ASP A CA  1 
ATOM   1275 C  C   . ASP A 1 164 ? -8.890  -5.956  -5.652  1.00 31.08 ? 165 ASP A C   1 
ATOM   1276 O  O   . ASP A 1 164 ? -7.845  -5.943  -6.323  1.00 31.35 ? 165 ASP A O   1 
ATOM   1277 C  CB  . ASP A 1 164 ? -10.166 -8.182  -5.738  1.00 32.65 ? 165 ASP A CB  1 
ATOM   1278 C  CG  . ASP A 1 164 ? -11.250 -7.416  -6.496  1.00 37.27 ? 165 ASP A CG  1 
ATOM   1279 O  OD1 . ASP A 1 164 ? -12.311 -7.070  -5.899  1.00 44.02 ? 165 ASP A OD1 1 
ATOM   1280 O  OD2 . ASP A 1 164 ? -11.030 -7.107  -7.703  1.00 43.10 ? 165 ASP A OD2 1 
ATOM   1281 N  N   . SER A 1 165 ? -9.674  -4.874  -5.531  1.00 30.47 ? 166 SER A N   1 
ATOM   1282 C  CA  . SER A 1 165 ? -9.299  -3.546  -6.044  1.00 31.56 ? 166 SER A CA  1 
ATOM   1283 C  C   . SER A 1 165 ? -8.200  -2.821  -5.216  1.00 29.77 ? 166 SER A C   1 
ATOM   1284 O  O   . SER A 1 165 ? -7.558  -1.880  -5.701  1.00 28.73 ? 166 SER A O   1 
ATOM   1285 C  CB  . SER A 1 165 ? -10.546 -2.661  -6.235  1.00 31.62 ? 166 SER A CB  1 
ATOM   1286 O  OG  . SER A 1 165 ? -11.080 -2.224  -4.986  1.00 37.41 ? 166 SER A OG  1 
ATOM   1287 N  N   . ILE A 1 166 ? -7.986  -3.252  -3.964  1.00 27.43 ? 167 ILE A N   1 
ATOM   1288 C  CA  . ILE A 1 166 ? -6.913  -2.672  -3.132  1.00 25.61 ? 167 ILE A CA  1 
ATOM   1289 C  C   . ILE A 1 166 ? -5.898  -3.720  -2.680  1.00 25.56 ? 167 ILE A C   1 
ATOM   1290 O  O   . ILE A 1 166 ? -5.554  -3.782  -1.527  1.00 23.51 ? 167 ILE A O   1 
ATOM   1291 C  CB  . ILE A 1 166 ? -7.511  -1.835  -1.939  1.00 25.31 ? 167 ILE A CB  1 
ATOM   1292 C  CG1 . ILE A 1 166 ? -8.436  -2.677  -1.043  1.00 23.82 ? 167 ILE A CG1 1 
ATOM   1293 C  CG2 . ILE A 1 166 ? -8.290  -0.666  -2.507  1.00 27.00 ? 167 ILE A CG2 1 
ATOM   1294 C  CD1 . ILE A 1 166 ? -8.558  -2.213  0.400   1.00 22.92 ? 167 ILE A CD1 1 
ATOM   1295 N  N   . LYS A 1 167 ? -5.434  -4.575  -3.598  1.00 26.20 ? 168 LYS A N   1 
ATOM   1296 C  CA  . LYS A 1 167 ? -4.635  -5.713  -3.168  1.00 27.23 ? 168 LYS A CA  1 
ATOM   1297 C  C   . LYS A 1 167 ? -3.314  -5.372  -2.522  1.00 26.88 ? 168 LYS A C   1 
ATOM   1298 O  O   . LYS A 1 167 ? -2.906  -6.034  -1.551  1.00 24.40 ? 168 LYS A O   1 
ATOM   1299 C  CB  . LYS A 1 167 ? -4.395  -6.692  -4.327  1.00 27.75 ? 168 LYS A CB  1 
ATOM   1300 C  CG  . LYS A 1 167 ? -3.562  -7.929  -3.932  1.00 28.91 ? 168 LYS A CG  1 
ATOM   1301 C  CD  . LYS A 1 167 ? -3.440  -8.972  -5.117  1.00 28.97 ? 168 LYS A CD  1 
ATOM   1302 C  CE  . LYS A 1 167 ? -2.690  -10.218 -4.624  1.00 31.47 ? 168 LYS A CE  1 
ATOM   1303 N  NZ  . LYS A 1 167 ? -2.783  -11.520 -5.491  1.00 38.20 ? 168 LYS A NZ  1 
ATOM   1304 N  N   . THR A 1 168 ? -2.629  -4.355  -3.060  1.00 25.78 ? 169 THR A N   1 
ATOM   1305 C  CA  . THR A 1 168 ? -1.291  -4.050  -2.581  1.00 26.71 ? 169 THR A CA  1 
ATOM   1306 C  C   . THR A 1 168 ? -1.175  -2.675  -1.888  1.00 26.43 ? 169 THR A C   1 
ATOM   1307 O  O   . THR A 1 168 ? -2.025  -1.848  -2.051  1.00 27.08 ? 169 THR A O   1 
ATOM   1308 C  CB  . THR A 1 168 ? -0.285  -4.109  -3.734  1.00 26.78 ? 169 THR A CB  1 
ATOM   1309 O  OG1 . THR A 1 168 ? -0.803  -3.332  -4.801  1.00 26.97 ? 169 THR A OG1 1 
ATOM   1310 C  CG2 . THR A 1 168 ? -0.130  -5.533  -4.236  1.00 28.32 ? 169 THR A CG2 1 
ATOM   1311 N  N   . LYS A 1 169 ? -0.088  -2.496  -1.155  1.00 28.87 ? 170 LYS A N   1 
ATOM   1312 C  CA  . LYS A 1 169 ? 0.220   -1.272  -0.368  1.00 30.05 ? 170 LYS A CA  1 
ATOM   1313 C  C   . LYS A 1 169 ? 0.004   -0.007  -1.173  1.00 29.62 ? 170 LYS A C   1 
ATOM   1314 O  O   . LYS A 1 169 ? 0.532   0.128   -2.272  1.00 30.46 ? 170 LYS A O   1 
ATOM   1315 C  CB  . LYS A 1 169 ? 1.647   -1.320  0.182   1.00 29.74 ? 170 LYS A CB  1 
ATOM   1316 C  CG  . LYS A 1 169 ? 1.961   -0.103  1.088   1.00 30.08 ? 170 LYS A CG  1 
ATOM   1317 C  CD  . LYS A 1 169 ? 3.381   -0.097  1.606   1.00 34.14 ? 170 LYS A CD  1 
ATOM   1318 C  CE  . LYS A 1 169 ? 3.488   1.012   2.697   1.00 40.71 ? 170 LYS A CE  1 
ATOM   1319 N  NZ  . LYS A 1 169 ? 4.769   1.841   2.769   1.00 46.26 ? 170 LYS A NZ  1 
ATOM   1320 N  N   . GLY A 1 170 ? -0.839  0.879   -0.670  1.00 29.75 ? 171 GLY A N   1 
ATOM   1321 C  CA  . GLY A 1 170 ? -0.987  2.170   -1.257  1.00 29.11 ? 171 GLY A CA  1 
ATOM   1322 C  C   . GLY A 1 170 ? -2.134  2.279   -2.186  1.00 30.69 ? 171 GLY A C   1 
ATOM   1323 O  O   . GLY A 1 170 ? -2.525  3.401   -2.522  1.00 31.71 ? 171 GLY A O   1 
ATOM   1324 N  N   . LYS A 1 171 ? -2.733  1.146   -2.602  1.00 28.06 ? 172 LYS A N   1 
ATOM   1325 C  CA  . LYS A 1 171 ? -3.915  1.229   -3.430  1.00 28.37 ? 172 LYS A CA  1 
ATOM   1326 C  C   . LYS A 1 171 ? -5.095  1.671   -2.593  1.00 28.70 ? 172 LYS A C   1 
ATOM   1327 O  O   . LYS A 1 171 ? -5.226  1.290   -1.395  1.00 27.63 ? 172 LYS A O   1 
ATOM   1328 C  CB  . LYS A 1 171 ? -4.253  -0.118  -4.124  1.00 27.66 ? 172 LYS A CB  1 
ATOM   1329 C  CG  . LYS A 1 171 ? -3.240  -0.556  -5.176  1.00 30.71 ? 172 LYS A CG  1 
ATOM   1330 C  CD  . LYS A 1 171 ? -3.709  -1.792  -5.880  1.00 37.91 ? 172 LYS A CD  1 
ATOM   1331 C  CE  . LYS A 1 171 ? -3.349  -1.799  -7.381  1.00 40.10 ? 172 LYS A CE  1 
ATOM   1332 N  NZ  . LYS A 1 171 ? -4.491  -2.425  -8.129  1.00 44.29 ? 172 LYS A NZ  1 
ATOM   1333 N  N   . SER A 1 172 ? -5.990  2.438   -3.231  1.00 27.31 ? 173 SER A N   1 
ATOM   1334 C  CA  . SER A 1 172 ? -7.201  2.912   -2.605  1.00 29.21 ? 173 SER A CA  1 
ATOM   1335 C  C   . SER A 1 172 ? -8.330  2.890   -3.578  1.00 28.90 ? 173 SER A C   1 
ATOM   1336 O  O   . SER A 1 172 ? -8.110  2.876   -4.794  1.00 27.88 ? 173 SER A O   1 
ATOM   1337 C  CB  . SER A 1 172 ? -7.066  4.344   -2.026  1.00 31.10 ? 173 SER A CB  1 
ATOM   1338 O  OG  . SER A 1 172 ? -6.639  5.258   -3.011  1.00 32.74 ? 173 SER A OG  1 
ATOM   1339 N  N   . ALA A 1 173 ? -9.549  2.878   -3.054  1.00 28.27 ? 174 ALA A N   1 
ATOM   1340 C  CA  . ALA A 1 173 ? -10.726 2.902   -3.893  1.00 29.03 ? 174 ALA A CA  1 
ATOM   1341 C  C   . ALA A 1 173 ? -11.793 3.739   -3.252  1.00 30.22 ? 174 ALA A C   1 
ATOM   1342 O  O   . ALA A 1 173 ? -11.938 3.761   -2.039  1.00 28.56 ? 174 ALA A O   1 
ATOM   1343 C  CB  . ALA A 1 173 ? -11.246 1.499   -4.121  1.00 28.92 ? 174 ALA A CB  1 
ATOM   1344 N  N   . ASP A 1 174 ? -12.585 4.420   -4.074  1.00 30.67 ? 175 ASP A N   1 
ATOM   1345 C  CA  . ASP A 1 174 ? -13.761 5.083   -3.528  1.00 31.36 ? 175 ASP A CA  1 
ATOM   1346 C  C   . ASP A 1 174 ? -14.585 4.014   -2.821  1.00 29.93 ? 175 ASP A C   1 
ATOM   1347 O  O   . ASP A 1 174 ? -14.606 2.853   -3.273  1.00 29.20 ? 175 ASP A O   1 
ATOM   1348 C  CB  . ASP A 1 174 ? -14.545 5.876   -4.616  1.00 32.70 ? 175 ASP A CB  1 
ATOM   1349 C  CG  . ASP A 1 174 ? -13.686 6.985   -5.255  1.00 37.41 ? 175 ASP A CG  1 
ATOM   1350 O  OD1 . ASP A 1 174 ? -13.114 7.818   -4.529  1.00 39.40 ? 175 ASP A OD1 1 
ATOM   1351 O  OD2 . ASP A 1 174 ? -13.566 7.043   -6.520  1.00 46.52 ? 175 ASP A OD2 1 
ATOM   1352 N  N   . PHE A 1 175 ? -15.255 4.385   -1.719  1.00 25.70 ? 176 PHE A N   1 
ATOM   1353 C  CA  . PHE A 1 175 ? -15.991 3.395   -0.897  1.00 26.88 ? 176 PHE A CA  1 
ATOM   1354 C  C   . PHE A 1 175 ? -17.050 4.186   -0.169  1.00 26.02 ? 176 PHE A C   1 
ATOM   1355 O  O   . PHE A 1 175 ? -16.917 4.483   1.028   1.00 29.75 ? 176 PHE A O   1 
ATOM   1356 C  CB  . PHE A 1 175 ? -15.029 2.568   0.052   1.00 22.90 ? 176 PHE A CB  1 
ATOM   1357 C  CG  . PHE A 1 175 ? -15.638 1.318   0.591   1.00 26.27 ? 176 PHE A CG  1 
ATOM   1358 C  CD1 . PHE A 1 175 ? -15.894 0.227   -0.257  1.00 27.05 ? 176 PHE A CD1 1 
ATOM   1359 C  CD2 . PHE A 1 175 ? -15.960 1.199   1.941   1.00 23.01 ? 176 PHE A CD2 1 
ATOM   1360 C  CE1 . PHE A 1 175 ? -16.460 -0.941  0.250   1.00 26.43 ? 176 PHE A CE1 1 
ATOM   1361 C  CE2 . PHE A 1 175 ? -16.521 0.034   2.427   1.00 25.09 ? 176 PHE A CE2 1 
ATOM   1362 C  CZ  . PHE A 1 175 ? -16.760 -1.039  1.566   1.00 21.86 ? 176 PHE A CZ  1 
ATOM   1363 N  N   . THR A 1 176 ? -18.083 4.582   -0.908  1.00 24.90 ? 177 THR A N   1 
ATOM   1364 C  CA  . THR A 1 176 ? -19.208 5.315   -0.350  1.00 23.71 ? 177 THR A CA  1 
ATOM   1365 C  C   . THR A 1 176 ? -20.388 4.497   0.055   1.00 23.21 ? 177 THR A C   1 
ATOM   1366 O  O   . THR A 1 176 ? -20.544 3.350   -0.412  1.00 23.94 ? 177 THR A O   1 
ATOM   1367 C  CB  . THR A 1 176 ? -19.717 6.422   -1.337  1.00 25.04 ? 177 THR A CB  1 
ATOM   1368 O  OG1 . THR A 1 176 ? -20.142 5.789   -2.559  1.00 26.71 ? 177 THR A OG1 1 
ATOM   1369 C  CG2 . THR A 1 176 ? -18.603 7.402   -1.610  1.00 25.10 ? 177 THR A CG2 1 
ATOM   1370 N  N   . ASN A 1 177 ? -21.177 5.067   0.967   1.00 20.15 ? 178 ASN A N   1 
ATOM   1371 C  CA  . ASN A 1 177 ? -22.452 4.544   1.497   1.00 23.06 ? 178 ASN A CA  1 
ATOM   1372 C  C   . ASN A 1 177 ? -22.347 3.194   2.238   1.00 23.46 ? 178 ASN A C   1 
ATOM   1373 O  O   . ASN A 1 177 ? -23.330 2.425   2.282   1.00 25.66 ? 178 ASN A O   1 
ATOM   1374 C  CB  . ASN A 1 177 ? -23.577 4.431   0.440   1.00 24.35 ? 178 ASN A CB  1 
ATOM   1375 C  CG  . ASN A 1 177 ? -23.814 5.728   -0.302  1.00 23.71 ? 178 ASN A CG  1 
ATOM   1376 O  OD1 . ASN A 1 177 ? -24.471 6.593   0.215   1.00 31.65 ? 178 ASN A OD1 1 
ATOM   1377 N  ND2 . ASN A 1 177 ? -23.249 5.854   -1.487  1.00 24.96 ? 178 ASN A ND2 1 
ATOM   1378 N  N   . PHE A 1 178 ? -21.185 2.947   2.814   1.00 24.50 ? 179 PHE A N   1 
ATOM   1379 C  CA  . PHE A 1 178 ? -21.020 1.760   3.679   1.00 24.19 ? 179 PHE A CA  1 
ATOM   1380 C  C   . PHE A 1 178 ? -21.544 2.072   5.044   1.00 22.61 ? 179 PHE A C   1 
ATOM   1381 O  O   . PHE A 1 178 ? -21.142 3.059   5.646   1.00 24.54 ? 179 PHE A O   1 
ATOM   1382 C  CB  . PHE A 1 178 ? -19.588 1.296   3.800   1.00 23.39 ? 179 PHE A CB  1 
ATOM   1383 C  CG  . PHE A 1 178 ? -19.473 0.046   4.660   1.00 23.38 ? 179 PHE A CG  1 
ATOM   1384 C  CD1 . PHE A 1 178 ? -19.807 -1.200  4.117   1.00 21.87 ? 179 PHE A CD1 1 
ATOM   1385 C  CD2 . PHE A 1 178 ? -19.252 0.146   6.022   1.00 20.90 ? 179 PHE A CD2 1 
ATOM   1386 C  CE1 . PHE A 1 178 ? -19.756 -2.351  4.917   1.00 19.77 ? 179 PHE A CE1 1 
ATOM   1387 C  CE2 . PHE A 1 178 ? -19.232 -1.014  6.848   1.00 20.22 ? 179 PHE A CE2 1 
ATOM   1388 C  CZ  . PHE A 1 178 ? -19.518 -2.253  6.289   1.00 16.83 ? 179 PHE A CZ  1 
ATOM   1389 N  N   . ASP A 1 179 ? -22.429 1.230   5.526   1.00 22.36 ? 180 ASP A N   1 
ATOM   1390 C  CA  . ASP A 1 179 ? -23.051 1.399   6.794   1.00 22.87 ? 180 ASP A CA  1 
ATOM   1391 C  C   . ASP A 1 179 ? -22.390 0.548   7.908   1.00 23.47 ? 180 ASP A C   1 
ATOM   1392 O  O   . ASP A 1 179 ? -22.611 -0.698  7.958   1.00 21.11 ? 180 ASP A O   1 
ATOM   1393 C  CB  . ASP A 1 179 ? -24.506 1.037   6.685   1.00 25.37 ? 180 ASP A CB  1 
ATOM   1394 C  CG  . ASP A 1 179 ? -25.248 1.295   7.948   1.00 26.50 ? 180 ASP A CG  1 
ATOM   1395 O  OD1 . ASP A 1 179 ? -24.647 1.725   8.950   1.00 26.15 ? 180 ASP A OD1 1 
ATOM   1396 O  OD2 . ASP A 1 179 ? -26.455 1.073   7.969   1.00 35.56 ? 180 ASP A OD2 1 
ATOM   1397 N  N   . PRO A 1 180 ? -21.605 1.194   8.811   1.00 22.01 ? 181 PRO A N   1 
ATOM   1398 C  CA  . PRO A 1 180 ? -20.886 0.400   9.849   1.00 21.20 ? 181 PRO A CA  1 
ATOM   1399 C  C   . PRO A 1 180 ? -21.775 -0.269  10.843  1.00 20.88 ? 181 PRO A C   1 
ATOM   1400 O  O   . PRO A 1 180 ? -21.315 -1.159  11.566  1.00 20.15 ? 181 PRO A O   1 
ATOM   1401 C  CB  . PRO A 1 180 ? -19.958 1.465   10.537  1.00 22.75 ? 181 PRO A CB  1 
ATOM   1402 C  CG  . PRO A 1 180 ? -20.742 2.794   10.353  1.00 20.31 ? 181 PRO A CG  1 
ATOM   1403 C  CD  . PRO A 1 180 ? -21.239 2.632   8.893   1.00 22.05 ? 181 PRO A CD  1 
ATOM   1404 N  N   . ARG A 1 181 ? -23.061 0.103   10.875  1.00 19.95 ? 182 ARG A N   1 
ATOM   1405 C  CA  . ARG A 1 181 ? -23.952 -0.478  11.847  1.00 19.96 ? 182 ARG A CA  1 
ATOM   1406 C  C   . ARG A 1 181 ? -24.122 -1.980  11.545  1.00 21.50 ? 182 ARG A C   1 
ATOM   1407 O  O   . ARG A 1 181 ? -24.547 -2.734  12.415  1.00 21.93 ? 182 ARG A O   1 
ATOM   1408 C  CB  . ARG A 1 181 ? -25.346 0.199   11.796  1.00 21.88 ? 182 ARG A CB  1 
ATOM   1409 C  CG  . ARG A 1 181 ? -25.309 1.684   12.282  1.00 18.93 ? 182 ARG A CG  1 
ATOM   1410 C  CD  . ARG A 1 181 ? -26.709 2.235   12.213  1.00 20.64 ? 182 ARG A CD  1 
ATOM   1411 N  NE  . ARG A 1 181 ? -27.068 2.359   10.837  1.00 23.87 ? 182 ARG A NE  1 
ATOM   1412 C  CZ  . ARG A 1 181 ? -28.120 3.032   10.412  1.00 26.22 ? 182 ARG A CZ  1 
ATOM   1413 N  NH1 . ARG A 1 181 ? -28.867 3.648   11.292  1.00 26.38 ? 182 ARG A NH1 1 
ATOM   1414 N  NH2 . ARG A 1 181 ? -28.394 3.097   9.122   1.00 27.90 ? 182 ARG A NH2 1 
ATOM   1415 N  N   . GLY A 1 182 ? -23.815 -2.359  10.315  1.00 21.69 ? 183 GLY A N   1 
ATOM   1416 C  CA  . GLY A 1 182 ? -23.968 -3.740  9.886   1.00 23.71 ? 183 GLY A CA  1 
ATOM   1417 C  C   . GLY A 1 182 ? -22.770 -4.592  10.308  1.00 23.81 ? 183 GLY A C   1 
ATOM   1418 O  O   . GLY A 1 182 ? -22.720 -5.776  9.993   1.00 24.72 ? 183 GLY A O   1 
ATOM   1419 N  N   . LEU A 1 183 ? -21.824 -4.004  11.042  1.00 23.48 ? 184 LEU A N   1 
ATOM   1420 C  CA  . LEU A 1 183 ? -20.704 -4.758  11.625  1.00 21.59 ? 184 LEU A CA  1 
ATOM   1421 C  C   . LEU A 1 183 ? -20.868 -4.963  13.122  1.00 21.22 ? 184 LEU A C   1 
ATOM   1422 O  O   . LEU A 1 183 ? -19.977 -5.504  13.773  1.00 21.88 ? 184 LEU A O   1 
ATOM   1423 C  CB  . LEU A 1 183 ? -19.378 -4.040  11.317  1.00 20.51 ? 184 LEU A CB  1 
ATOM   1424 C  CG  . LEU A 1 183 ? -19.089 -3.676  9.892   1.00 18.18 ? 184 LEU A CG  1 
ATOM   1425 C  CD1 . LEU A 1 183 ? -17.919 -2.869  9.989   1.00 18.59 ? 184 LEU A CD1 1 
ATOM   1426 C  CD2 . LEU A 1 183 ? -18.842 -4.885  9.033   1.00 19.09 ? 184 LEU A CD2 1 
ATOM   1427 N  N   . LEU A 1 184 ? -21.987 -4.535  13.716  1.00 20.44 ? 185 LEU A N   1 
ATOM   1428 C  CA  . LEU A 1 184 ? -22.087 -4.547  15.164  1.00 20.42 ? 185 LEU A CA  1 
ATOM   1429 C  C   . LEU A 1 184 ? -22.828 -5.835  15.573  1.00 22.91 ? 185 LEU A C   1 
ATOM   1430 O  O   . LEU A 1 184 ? -23.711 -6.298  14.824  1.00 25.77 ? 185 LEU A O   1 
ATOM   1431 C  CB  . LEU A 1 184 ? -22.853 -3.307  15.689  1.00 20.92 ? 185 LEU A CB  1 
ATOM   1432 C  CG  . LEU A 1 184 ? -22.324 -1.912  15.277  1.00 21.09 ? 185 LEU A CG  1 
ATOM   1433 C  CD1 . LEU A 1 184 ? -23.215 -0.868  15.916  1.00 25.54 ? 185 LEU A CD1 1 
ATOM   1434 C  CD2 . LEU A 1 184 ? -20.839 -1.734  15.762  1.00 19.16 ? 185 LEU A CD2 1 
ATOM   1435 N  N   . PRO A 1 185 ? -22.476 -6.414  16.732  1.00 20.98 ? 186 PRO A N   1 
ATOM   1436 C  CA  . PRO A 1 185 ? -23.213 -7.559  17.201  1.00 21.97 ? 186 PRO A CA  1 
ATOM   1437 C  C   . PRO A 1 185 ? -24.486 -6.997  17.848  1.00 23.24 ? 186 PRO A C   1 
ATOM   1438 O  O   . PRO A 1 185 ? -24.618 -5.788  17.979  1.00 21.42 ? 186 PRO A O   1 
ATOM   1439 C  CB  . PRO A 1 185 ? -22.293 -8.153  18.307  1.00 20.74 ? 186 PRO A CB  1 
ATOM   1440 C  CG  . PRO A 1 185 ? -21.536 -7.000  18.793  1.00 21.13 ? 186 PRO A CG  1 
ATOM   1441 C  CD  . PRO A 1 185 ? -21.390 -6.028  17.644  1.00 19.04 ? 186 PRO A CD  1 
ATOM   1442 N  N   . GLU A 1 186 ? -25.316 -7.884  18.391  1.00 24.01 ? 187 GLU A N   1 
ATOM   1443 C  CA  . GLU A 1 186 ? -26.567 -7.467  18.970  1.00 25.38 ? 187 GLU A CA  1 
ATOM   1444 C  C   . GLU A 1 186 ? -26.390 -6.801  20.320  1.00 25.48 ? 187 GLU A C   1 
ATOM   1445 O  O   . GLU A 1 186 ? -27.038 -5.820  20.626  1.00 27.12 ? 187 GLU A O   1 
ATOM   1446 C  CB  . GLU A 1 186 ? -27.443 -8.704  18.978  1.00 25.31 ? 187 GLU A CB  1 
ATOM   1447 C  CG  . GLU A 1 186 ? -28.433 -8.800  20.042  1.00 32.67 ? 187 GLU A CG  1 
ATOM   1448 C  CD  . GLU A 1 186 ? -28.977 -10.269 20.144  1.00 35.44 ? 187 GLU A CD  1 
ATOM   1449 O  OE1 . GLU A 1 186 ? -29.460 -10.577 21.243  1.00 42.30 ? 187 GLU A OE1 1 
ATOM   1450 O  OE2 . GLU A 1 186 ? -28.892 -11.049 19.143  1.00 32.43 ? 187 GLU A OE2 1 
ATOM   1451 N  N   . SER A 1 187 ? -25.490 -7.306  21.146  1.00 23.89 ? 188 SER A N   1 
ATOM   1452 C  CA  . SER A 1 187 ? -25.288 -6.690  22.428  1.00 23.26 ? 188 SER A CA  1 
ATOM   1453 C  C   . SER A 1 187 ? -24.204 -5.610  22.404  1.00 22.33 ? 188 SER A C   1 
ATOM   1454 O  O   . SER A 1 187 ? -23.194 -5.807  21.740  1.00 22.03 ? 188 SER A O   1 
ATOM   1455 C  CB  . SER A 1 187 ? -24.930 -7.766  23.451  1.00 23.57 ? 188 SER A CB  1 
ATOM   1456 O  OG  . SER A 1 187 ? -24.707 -7.166  24.687  1.00 20.47 ? 188 SER A OG  1 
ATOM   1457 N  N   . LEU A 1 188 ? -24.415 -4.512  23.157  1.00 22.61 ? 189 LEU A N   1 
ATOM   1458 C  CA  . LEU A 1 188 ? -23.381 -3.469  23.395  1.00 23.18 ? 189 LEU A CA  1 
ATOM   1459 C  C   . LEU A 1 188 ? -22.701 -3.589  24.770  1.00 23.05 ? 189 LEU A C   1 
ATOM   1460 O  O   . LEU A 1 188 ? -22.070 -2.654  25.236  1.00 23.48 ? 189 LEU A O   1 
ATOM   1461 C  CB  . LEU A 1 188 ? -23.923 -2.020  23.133  1.00 22.76 ? 189 LEU A CB  1 
ATOM   1462 C  CG  . LEU A 1 188 ? -24.248 -1.639  21.689  1.00 23.96 ? 189 LEU A CG  1 
ATOM   1463 C  CD1 . LEU A 1 188 ? -24.608 -0.079  21.572  1.00 25.90 ? 189 LEU A CD1 1 
ATOM   1464 C  CD2 . LEU A 1 188 ? -23.155 -2.051  20.694  1.00 25.05 ? 189 LEU A CD2 1 
ATOM   1465 N  N   . ASP A 1 189 ? -22.845 -4.739  25.447  1.00 21.88 ? 190 ASP A N   1 
ATOM   1466 C  CA  . ASP A 1 189 ? -22.132 -4.991  26.708  1.00 21.44 ? 190 ASP A CA  1 
ATOM   1467 C  C   . ASP A 1 189 ? -20.633 -4.942  26.380  1.00 20.39 ? 190 ASP A C   1 
ATOM   1468 O  O   . ASP A 1 189 ? -20.266 -5.364  25.288  1.00 21.02 ? 190 ASP A O   1 
ATOM   1469 C  CB  . ASP A 1 189 ? -22.439 -6.366  27.176  1.00 20.31 ? 190 ASP A CB  1 
ATOM   1470 C  CG  . ASP A 1 189 ? -23.814 -6.463  27.888  1.00 26.27 ? 190 ASP A CG  1 
ATOM   1471 O  OD1 . ASP A 1 189 ? -24.465 -5.433  28.133  1.00 32.53 ? 190 ASP A OD1 1 
ATOM   1472 O  OD2 . ASP A 1 189 ? -24.170 -7.585  28.240  1.00 28.54 ? 190 ASP A OD2 1 
ATOM   1473 N  N   . TYR A 1 190 ? -19.827 -4.323  27.246  1.00 21.53 ? 191 TYR A N   1 
ATOM   1474 C  CA  . TYR A 1 190 ? -18.426 -4.063  26.884  1.00 20.34 ? 191 TYR A CA  1 
ATOM   1475 C  C   . TYR A 1 190 ? -17.518 -4.146  28.108  1.00 19.94 ? 191 TYR A C   1 
ATOM   1476 O  O   . TYR A 1 190 ? -17.961 -4.103  29.251  1.00 19.48 ? 191 TYR A O   1 
ATOM   1477 C  CB  . TYR A 1 190 ? -18.302 -2.677  26.164  1.00 20.31 ? 191 TYR A CB  1 
ATOM   1478 C  CG  . TYR A 1 190 ? -18.689 -1.503  27.098  1.00 19.44 ? 191 TYR A CG  1 
ATOM   1479 C  CD1 . TYR A 1 190 ? -17.779 -0.945  28.002  1.00 18.52 ? 191 TYR A CD1 1 
ATOM   1480 C  CD2 . TYR A 1 190 ? -19.991 -0.993  27.071  1.00 17.86 ? 191 TYR A CD2 1 
ATOM   1481 C  CE1 . TYR A 1 190 ? -18.149 0.162   28.853  1.00 20.41 ? 191 TYR A CE1 1 
ATOM   1482 C  CE2 . TYR A 1 190 ? -20.375 0.076   27.926  1.00 22.75 ? 191 TYR A CE2 1 
ATOM   1483 C  CZ  . TYR A 1 190 ? -19.473 0.615   28.820  1.00 21.67 ? 191 TYR A CZ  1 
ATOM   1484 O  OH  . TYR A 1 190 ? -19.896 1.652   29.628  1.00 21.02 ? 191 TYR A OH  1 
ATOM   1485 N  N   . TRP A 1 191 ? -16.232 -4.335  27.837  1.00 18.61 ? 192 TRP A N   1 
ATOM   1486 C  CA  . TRP A 1 191 ? -15.184 -4.101  28.766  1.00 19.19 ? 192 TRP A CA  1 
ATOM   1487 C  C   . TRP A 1 191 ? -14.497 -2.804  28.299  1.00 17.83 ? 192 TRP A C   1 
ATOM   1488 O  O   . TRP A 1 191 ? -14.461 -2.451  27.089  1.00 17.56 ? 192 TRP A O   1 
ATOM   1489 C  CB  . TRP A 1 191 ? -14.122 -5.205  28.694  1.00 20.17 ? 192 TRP A CB  1 
ATOM   1490 C  CG  . TRP A 1 191 ? -14.628 -6.559  29.085  1.00 20.91 ? 192 TRP A CG  1 
ATOM   1491 C  CD1 . TRP A 1 191 ? -14.904 -6.985  30.350  1.00 20.17 ? 192 TRP A CD1 1 
ATOM   1492 C  CD2 . TRP A 1 191 ? -14.885 -7.663  28.201  1.00 16.66 ? 192 TRP A CD2 1 
ATOM   1493 N  NE1 . TRP A 1 191 ? -15.340 -8.308  30.319  1.00 19.61 ? 192 TRP A NE1 1 
ATOM   1494 C  CE2 . TRP A 1 191 ? -15.328 -8.741  29.011  1.00 23.29 ? 192 TRP A CE2 1 
ATOM   1495 C  CE3 . TRP A 1 191 ? -14.808 -7.834  26.804  1.00 20.63 ? 192 TRP A CE3 1 
ATOM   1496 C  CZ2 . TRP A 1 191 ? -15.692 -9.960  28.480  1.00 20.88 ? 192 TRP A CZ2 1 
ATOM   1497 C  CZ3 . TRP A 1 191 ? -15.161 -9.065  26.259  1.00 18.82 ? 192 TRP A CZ3 1 
ATOM   1498 C  CH2 . TRP A 1 191 ? -15.561 -10.131 27.115  1.00 19.11 ? 192 TRP A CH2 1 
ATOM   1499 N  N   . THR A 1 192 ? -13.952 -2.099  29.249  1.00 17.06 ? 193 THR A N   1 
ATOM   1500 C  CA  . THR A 1 192 ? -13.200 -0.890  28.916  1.00 18.68 ? 193 THR A CA  1 
ATOM   1501 C  C   . THR A 1 192 ? -11.964 -0.720  29.799  1.00 18.02 ? 193 THR A C   1 
ATOM   1502 O  O   . THR A 1 192 ? -11.963 -1.144  30.993  1.00 19.79 ? 193 THR A O   1 
ATOM   1503 C  CB  . THR A 1 192 ? -14.154 0.407   28.982  1.00 18.01 ? 193 THR A CB  1 
ATOM   1504 O  OG1 . THR A 1 192 ? -13.449 1.565   28.549  1.00 20.03 ? 193 THR A OG1 1 
ATOM   1505 C  CG2 . THR A 1 192 ? -14.638 0.665   30.404  1.00 18.64 ? 193 THR A CG2 1 
ATOM   1506 N  N   . TYR A 1 193 ? -10.893 -0.143  29.238  1.00 18.07 ? 194 TYR A N   1 
ATOM   1507 C  CA  . TYR A 1 193 ? -9.676  0.069   29.990  1.00 17.89 ? 194 TYR A CA  1 
ATOM   1508 C  C   . TYR A 1 193 ? -8.913  1.127   29.216  1.00 19.19 ? 194 TYR A C   1 
ATOM   1509 O  O   . TYR A 1 193 ? -9.157  1.276   27.994  1.00 18.85 ? 194 TYR A O   1 
ATOM   1510 C  CB  . TYR A 1 193 ? -8.871  -1.266  30.146  1.00 17.39 ? 194 TYR A CB  1 
ATOM   1511 C  CG  . TYR A 1 193 ? -8.131  -1.633  28.888  1.00 14.45 ? 194 TYR A CG  1 
ATOM   1512 C  CD1 . TYR A 1 193 ? -8.780  -2.308  27.853  1.00 12.48 ? 194 TYR A CD1 1 
ATOM   1513 C  CD2 . TYR A 1 193 ? -6.784  -1.283  28.723  1.00 15.16 ? 194 TYR A CD2 1 
ATOM   1514 C  CE1 . TYR A 1 193 ? -8.126  -2.624  26.639  1.00 13.14 ? 194 TYR A CE1 1 
ATOM   1515 C  CE2 . TYR A 1 193 ? -6.120  -1.569  27.497  1.00 14.49 ? 194 TYR A CE2 1 
ATOM   1516 C  CZ  . TYR A 1 193 ? -6.793  -2.274  26.510  1.00 13.48 ? 194 TYR A CZ  1 
ATOM   1517 O  OH  . TYR A 1 193 ? -6.166  -2.547  25.340  1.00 15.81 ? 194 TYR A OH  1 
ATOM   1518 N  N   . PRO A 1 194 ? -7.998  1.878   29.889  1.00 18.51 ? 195 PRO A N   1 
ATOM   1519 C  CA  . PRO A 1 194 ? -7.182  2.858   29.186  1.00 18.53 ? 195 PRO A CA  1 
ATOM   1520 C  C   . PRO A 1 194 ? -5.950  2.217   28.516  1.00 17.17 ? 195 PRO A C   1 
ATOM   1521 O  O   . PRO A 1 194 ? -5.253  1.429   29.160  1.00 17.27 ? 195 PRO A O   1 
ATOM   1522 C  CB  . PRO A 1 194 ? -6.703  3.799   30.332  1.00 19.24 ? 195 PRO A CB  1 
ATOM   1523 C  CG  . PRO A 1 194 ? -6.747  2.973   31.595  1.00 21.61 ? 195 PRO A CG  1 
ATOM   1524 C  CD  . PRO A 1 194 ? -7.778  1.889   31.356  1.00 20.02 ? 195 PRO A CD  1 
ATOM   1525 N  N   . GLY A 1 195 ? -5.646  2.575   27.276  1.00 16.61 ? 196 GLY A N   1 
ATOM   1526 C  CA  . GLY A 1 195 ? -4.563  1.870   26.555  1.00 16.38 ? 196 GLY A CA  1 
ATOM   1527 C  C   . GLY A 1 195 ? -4.033  2.719   25.416  1.00 16.55 ? 196 GLY A C   1 
ATOM   1528 O  O   . GLY A 1 195 ? -4.038  3.961   25.498  1.00 16.74 ? 196 GLY A O   1 
ATOM   1529 N  N   . SER A 1 196 ? -3.541  2.077   24.372  1.00 16.94 ? 197 SER A N   1 
ATOM   1530 C  CA  . SER A 1 196 ? -2.798  2.791   23.353  1.00 16.50 ? 197 SER A CA  1 
ATOM   1531 C  C   . SER A 1 196 ? -3.227  2.403   21.945  1.00 16.25 ? 197 SER A C   1 
ATOM   1532 O  O   . SER A 1 196 ? -3.977  1.423   21.799  1.00 15.24 ? 197 SER A O   1 
ATOM   1533 C  CB  . SER A 1 196 ? -1.326  2.400   23.512  1.00 17.69 ? 197 SER A CB  1 
ATOM   1534 O  OG  . SER A 1 196 ? -1.111  1.037   23.047  1.00 17.99 ? 197 SER A OG  1 
ATOM   1535 N  N   . LEU A 1 197 ? -2.680  3.083   20.909  1.00 14.77 ? 198 LEU A N   1 
ATOM   1536 C  CA  . LEU A 1 197 ? -2.699  2.531   19.564  1.00 15.77 ? 198 LEU A CA  1 
ATOM   1537 C  C   . LEU A 1 197 ? -2.020  1.172   19.639  1.00 17.18 ? 198 LEU A C   1 
ATOM   1538 O  O   . LEU A 1 197 ? -1.033  1.010   20.419  1.00 16.78 ? 198 LEU A O   1 
ATOM   1539 C  CB  . LEU A 1 197 ? -1.973  3.431   18.566  1.00 17.17 ? 198 LEU A CB  1 
ATOM   1540 C  CG  . LEU A 1 197 ? -2.441  4.905   18.503  1.00 16.84 ? 198 LEU A CG  1 
ATOM   1541 C  CD1 . LEU A 1 197 ? -1.568  5.661   17.582  1.00 18.20 ? 198 LEU A CD1 1 
ATOM   1542 C  CD2 . LEU A 1 197 ? -3.901  5.046   18.054  1.00 15.62 ? 198 LEU A CD2 1 
ATOM   1543 N  N   . THR A 1 198 ? -2.457  0.219   18.786  1.00 15.28 ? 199 THR A N   1 
ATOM   1544 C  CA  . THR A 1 198 ? -1.804  -1.081  18.815  1.00 15.54 ? 199 THR A CA  1 
ATOM   1545 C  C   . THR A 1 198 ? -0.776  -1.244  17.694  1.00 17.02 ? 199 THR A C   1 
ATOM   1546 O  O   . THR A 1 198 ? -0.218  -2.385  17.450  1.00 19.03 ? 199 THR A O   1 
ATOM   1547 C  CB  . THR A 1 198 ? -2.824  -2.231  18.643  1.00 12.18 ? 199 THR A CB  1 
ATOM   1548 O  OG1 . THR A 1 198 ? -3.422  -2.142  17.344  1.00 16.76 ? 199 THR A OG1 1 
ATOM   1549 C  CG2 . THR A 1 198 ? -3.808  -2.247  19.849  1.00 11.65 ? 199 THR A CG2 1 
ATOM   1550 N  N   . THR A 1 199 ? -0.601  -0.148  16.955  1.00 17.47 ? 200 THR A N   1 
ATOM   1551 C  CA  . THR A 1 199 ? 0.465   -0.054  15.998  1.00 17.88 ? 200 THR A CA  1 
ATOM   1552 C  C   . THR A 1 199 ? 1.306   1.215   16.277  1.00 19.08 ? 200 THR A C   1 
ATOM   1553 O  O   . THR A 1 199 ? 0.828   2.174   16.901  1.00 17.36 ? 200 THR A O   1 
ATOM   1554 C  CB  . THR A 1 199 ? -0.038  0.058   14.568  1.00 19.65 ? 200 THR A CB  1 
ATOM   1555 O  OG1 . THR A 1 199 ? -0.648  1.359   14.332  1.00 21.34 ? 200 THR A OG1 1 
ATOM   1556 C  CG2 . THR A 1 199 ? -1.003  -1.118  14.187  1.00 18.21 ? 200 THR A CG2 1 
ATOM   1557 N  N   . PRO A 1 200 ? 2.547   1.228   15.770  1.00 20.06 ? 201 PRO A N   1 
ATOM   1558 C  CA  . PRO A 1 200 ? 3.314   2.440   15.820  1.00 19.90 ? 201 PRO A CA  1 
ATOM   1559 C  C   . PRO A 1 200 ? 2.439   3.541   15.322  1.00 19.79 ? 201 PRO A C   1 
ATOM   1560 O  O   . PRO A 1 200 ? 1.807   3.383   14.282  1.00 20.76 ? 201 PRO A O   1 
ATOM   1561 C  CB  . PRO A 1 200 ? 4.425   2.157   14.809  1.00 17.67 ? 201 PRO A CB  1 
ATOM   1562 C  CG  . PRO A 1 200 ? 4.746   0.714   15.065  1.00 21.00 ? 201 PRO A CG  1 
ATOM   1563 C  CD  . PRO A 1 200 ? 3.315   0.112   15.187  1.00 20.52 ? 201 PRO A CD  1 
ATOM   1564 N  N   . PRO A 1 201 ? 2.457   4.717   15.972  1.00 20.49 ? 202 PRO A N   1 
ATOM   1565 C  CA  . PRO A 1 201 ? 3.351   5.204   17.055  1.00 20.64 ? 202 PRO A CA  1 
ATOM   1566 C  C   . PRO A 1 201 ? 3.007   4.795   18.430  1.00 18.10 ? 202 PRO A C   1 
ATOM   1567 O  O   . PRO A 1 201 ? 3.700   5.199   19.352  1.00 18.56 ? 202 PRO A O   1 
ATOM   1568 C  CB  . PRO A 1 201 ? 3.251   6.746   16.937  1.00 20.44 ? 202 PRO A CB  1 
ATOM   1569 C  CG  . PRO A 1 201 ? 1.994   7.032   16.284  1.00 22.99 ? 202 PRO A CG  1 
ATOM   1570 C  CD  . PRO A 1 201 ? 1.602   5.809   15.432  1.00 20.40 ? 202 PRO A CD  1 
ATOM   1571 N  N   . LEU A 1 202 ? 2.062   3.848   18.578  1.00 17.99 ? 203 LEU A N   1 
ATOM   1572 C  CA  . LEU A 1 202 ? 1.763   3.251   19.905  1.00 16.91 ? 203 LEU A CA  1 
ATOM   1573 C  C   . LEU A 1 202 ? 1.399   4.277   20.975  1.00 16.31 ? 203 LEU A C   1 
ATOM   1574 O  O   . LEU A 1 202 ? 1.567   4.043   22.171  1.00 15.95 ? 203 LEU A O   1 
ATOM   1575 C  CB  . LEU A 1 202 ? 2.853   2.307   20.399  1.00 18.68 ? 203 LEU A CB  1 
ATOM   1576 C  CG  . LEU A 1 202 ? 3.286   1.191   19.387  1.00 17.64 ? 203 LEU A CG  1 
ATOM   1577 C  CD1 . LEU A 1 202 ? 4.536   0.540   19.906  1.00 19.69 ? 203 LEU A CD1 1 
ATOM   1578 C  CD2 . LEU A 1 202 ? 2.149   0.091   19.337  1.00 16.38 ? 203 LEU A CD2 1 
ATOM   1579 N  N   . LEU A 1 203 ? 0.799   5.389   20.557  1.00 17.23 ? 204 LEU A N   1 
ATOM   1580 C  CA  . LEU A 1 203 ? 0.543   6.492   21.512  1.00 18.16 ? 204 LEU A CA  1 
ATOM   1581 C  C   . LEU A 1 203 ? -0.511  6.099   22.523  1.00 19.44 ? 204 LEU A C   1 
ATOM   1582 O  O   . LEU A 1 203 ? -1.517  5.477   22.191  1.00 18.48 ? 204 LEU A O   1 
ATOM   1583 C  CB  . LEU A 1 203 ? 0.135   7.770   20.775  1.00 16.97 ? 204 LEU A CB  1 
ATOM   1584 C  CG  . LEU A 1 203 ? 1.183   8.255   19.773  1.00 20.55 ? 204 LEU A CG  1 
ATOM   1585 C  CD1 . LEU A 1 203 ? 0.648   9.284   18.790  1.00 24.83 ? 204 LEU A CD1 1 
ATOM   1586 C  CD2 . LEU A 1 203 ? 2.432   8.765   20.543  1.00 25.94 ? 204 LEU A CD2 1 
ATOM   1587 N  N   . GLU A 1 204 ? -0.298  6.518   23.749  1.00 18.05 ? 205 GLU A N   1 
ATOM   1588 C  CA  . GLU A 1 204 ? -1.188  6.168   24.845  1.00 20.58 ? 205 GLU A CA  1 
ATOM   1589 C  C   . GLU A 1 204 ? -2.345  7.160   24.996  1.00 20.22 ? 205 GLU A C   1 
ATOM   1590 O  O   . GLU A 1 204 ? -2.406  7.925   25.974  1.00 19.38 ? 205 GLU A O   1 
ATOM   1591 C  CB  . GLU A 1 204 ? -0.361  6.032   26.107  1.00 20.01 ? 205 GLU A CB  1 
ATOM   1592 C  CG  . GLU A 1 204 ? 0.586   4.788   25.971  1.00 21.41 ? 205 GLU A CG  1 
ATOM   1593 C  CD  . GLU A 1 204 ? 1.427   4.529   27.187  1.00 26.33 ? 205 GLU A CD  1 
ATOM   1594 O  OE1 . GLU A 1 204 ? 1.683   5.463   28.013  1.00 23.54 ? 205 GLU A OE1 1 
ATOM   1595 O  OE2 . GLU A 1 204 ? 1.818   3.358   27.355  1.00 21.61 ? 205 GLU A OE2 1 
ATOM   1596 N  N   . CYS A 1 205 ? -3.274  7.076   24.045  1.00 18.53 ? 206 CYS A N   1 
ATOM   1597 C  CA  . CYS A 1 205 ? -4.320  8.100   23.849  1.00 18.56 ? 206 CYS A CA  1 
ATOM   1598 C  C   . CYS A 1 205 ? -5.689  7.444   23.757  1.00 18.25 ? 206 CYS A C   1 
ATOM   1599 O  O   . CYS A 1 205 ? -6.661  8.072   23.420  1.00 18.04 ? 206 CYS A O   1 
ATOM   1600 C  CB  . CYS A 1 205 ? -4.011  8.808   22.547  1.00 17.21 ? 206 CYS A CB  1 
ATOM   1601 S  SG  . CYS A 1 205 ? -3.984  7.782   20.976  1.00 20.88 ? 206 CYS A SG  1 
ATOM   1602 N  N   . VAL A 1 206 ? -5.760  6.131   23.986  1.00 17.00 ? 207 VAL A N   1 
ATOM   1603 C  CA  . VAL A 1 206 ? -6.991  5.392   23.631  1.00 17.24 ? 207 VAL A CA  1 
ATOM   1604 C  C   . VAL A 1 206 ? -7.777  4.936   24.857  1.00 15.35 ? 207 VAL A C   1 
ATOM   1605 O  O   . VAL A 1 206 ? -7.219  4.390   25.824  1.00 18.83 ? 207 VAL A O   1 
ATOM   1606 C  CB  . VAL A 1 206 ? -6.655  4.136   22.783  1.00 17.29 ? 207 VAL A CB  1 
ATOM   1607 C  CG1 . VAL A 1 206 ? -7.951  3.451   22.368  1.00 16.30 ? 207 VAL A CG1 1 
ATOM   1608 C  CG2 . VAL A 1 206 ? -5.888  4.498   21.536  1.00 19.07 ? 207 VAL A CG2 1 
ATOM   1609 N  N   . THR A 1 207 ? -9.058  5.249   24.882  1.00 16.78 ? 208 THR A N   1 
ATOM   1610 C  CA  . THR A 1 207 ? -9.991  4.555   25.753  1.00 17.23 ? 208 THR A CA  1 
ATOM   1611 C  C   . THR A 1 207 ? -10.531 3.390   24.949  1.00 15.81 ? 208 THR A C   1 
ATOM   1612 O  O   . THR A 1 207 ? -11.189 3.573   23.916  1.00 15.43 ? 208 THR A O   1 
ATOM   1613 C  CB  . THR A 1 207 ? -11.172 5.479   26.276  1.00 16.89 ? 208 THR A CB  1 
ATOM   1614 O  OG1 . THR A 1 207 ? -10.624 6.470   27.159  1.00 15.25 ? 208 THR A OG1 1 
ATOM   1615 C  CG2 . THR A 1 207 ? -12.279 4.685   27.009  1.00 17.51 ? 208 THR A CG2 1 
ATOM   1616 N  N   . TRP A 1 208 ? -10.134 2.185   25.365  1.00 15.40 ? 209 TRP A N   1 
ATOM   1617 C  CA  . TRP A 1 208 ? -10.570 0.992   24.656  1.00 15.80 ? 209 TRP A CA  1 
ATOM   1618 C  C   . TRP A 1 208 ? -11.934 0.544   25.137  1.00 16.21 ? 209 TRP A C   1 
ATOM   1619 O  O   . TRP A 1 208 ? -12.141 0.460   26.337  1.00 18.23 ? 209 TRP A O   1 
ATOM   1620 C  CB  . TRP A 1 208 ? -9.590  -0.181  24.876  1.00 13.17 ? 209 TRP A CB  1 
ATOM   1621 C  CG  . TRP A 1 208 ? -8.476  -0.014  23.830  1.00 10.97 ? 209 TRP A CG  1 
ATOM   1622 C  CD1 . TRP A 1 208 ? -7.220  0.518   24.051  1.00 13.86 ? 209 TRP A CD1 1 
ATOM   1623 C  CD2 . TRP A 1 208 ? -8.510  -0.463  22.474  1.00 16.15 ? 209 TRP A CD2 1 
ATOM   1624 N  NE1 . TRP A 1 208 ? -6.516  0.523   22.848  1.00 13.38 ? 209 TRP A NE1 1 
ATOM   1625 C  CE2 . TRP A 1 208 ? -7.282  -0.096  21.879  1.00 10.74 ? 209 TRP A CE2 1 
ATOM   1626 C  CE3 . TRP A 1 208 ? -9.515  -1.053  21.662  1.00 15.56 ? 209 TRP A CE3 1 
ATOM   1627 C  CZ2 . TRP A 1 208 ? -7.009  -0.325  20.536  1.00 12.20 ? 209 TRP A CZ2 1 
ATOM   1628 C  CZ3 . TRP A 1 208 ? -9.236  -1.304  20.350  1.00 13.30 ? 209 TRP A CZ3 1 
ATOM   1629 C  CH2 . TRP A 1 208 ? -7.988  -0.949  19.785  1.00 15.22 ? 209 TRP A CH2 1 
ATOM   1630 N  N   . ILE A 1 209 ? -12.805 0.241   24.197  1.00 17.02 ? 210 ILE A N   1 
ATOM   1631 C  CA  . ILE A 1 209 ? -14.145 -0.235  24.520  1.00 15.47 ? 210 ILE A CA  1 
ATOM   1632 C  C   . ILE A 1 209 ? -14.258 -1.545  23.688  1.00 14.80 ? 210 ILE A C   1 
ATOM   1633 O  O   . ILE A 1 209 ? -14.295 -1.498  22.521  1.00 14.10 ? 210 ILE A O   1 
ATOM   1634 C  CB  . ILE A 1 209 ? -15.260 0.838   24.175  1.00 15.24 ? 210 ILE A CB  1 
ATOM   1635 C  CG1 . ILE A 1 209 ? -15.027 2.090   25.061  1.00 15.88 ? 210 ILE A CG1 1 
ATOM   1636 C  CG2 . ILE A 1 209 ? -16.634 0.193   24.402  1.00 16.90 ? 210 ILE A CG2 1 
ATOM   1637 C  CD1 . ILE A 1 209 ? -15.778 3.386   24.427  1.00 16.23 ? 210 ILE A CD1 1 
ATOM   1638 N  N   . VAL A 1 210 ? -14.153 -2.684  24.350  1.00 15.19 ? 211 VAL A N   1 
ATOM   1639 C  CA  . VAL A 1 210 ? -14.209 -4.016  23.662  1.00 14.72 ? 211 VAL A CA  1 
ATOM   1640 C  C   . VAL A 1 210 ? -15.594 -4.707  23.933  1.00 16.47 ? 211 VAL A C   1 
ATOM   1641 O  O   . VAL A 1 210 ? -15.975 -4.911  25.069  1.00 16.29 ? 211 VAL A O   1 
ATOM   1642 C  CB  . VAL A 1 210 ? -13.025 -4.879  24.113  1.00 15.75 ? 211 VAL A CB  1 
ATOM   1643 C  CG1 . VAL A 1 210 ? -13.025 -6.233  23.313  1.00 13.17 ? 211 VAL A CG1 1 
ATOM   1644 C  CG2 . VAL A 1 210 ? -11.709 -4.109  23.817  1.00 14.02 ? 211 VAL A CG2 1 
ATOM   1645 N  N   . LEU A 1 211 ? -16.314 -5.004  22.864  1.00 16.26 ? 212 LEU A N   1 
ATOM   1646 C  CA  . LEU A 1 211 ? -17.605 -5.614  23.001  1.00 17.69 ? 212 LEU A CA  1 
ATOM   1647 C  C   . LEU A 1 211 ? -17.410 -7.075  23.414  1.00 18.36 ? 212 LEU A C   1 
ATOM   1648 O  O   . LEU A 1 211 ? -16.583 -7.788  22.881  1.00 17.18 ? 212 LEU A O   1 
ATOM   1649 C  CB  . LEU A 1 211 ? -18.453 -5.526  21.748  1.00 15.39 ? 212 LEU A CB  1 
ATOM   1650 C  CG  . LEU A 1 211 ? -18.781 -4.079  21.270  1.00 20.10 ? 212 LEU A CG  1 
ATOM   1651 C  CD1 . LEU A 1 211 ? -19.849 -4.135  20.152  1.00 17.30 ? 212 LEU A CD1 1 
ATOM   1652 C  CD2 . LEU A 1 211 ? -19.256 -3.231  22.474  1.00 16.64 ? 212 LEU A CD2 1 
ATOM   1653 N  N   . LYS A 1 212 ? -18.248 -7.446  24.370  1.00 19.79 ? 213 LYS A N   1 
ATOM   1654 C  CA  . LYS A 1 212 ? -18.326 -8.806  24.897  1.00 22.72 ? 213 LYS A CA  1 
ATOM   1655 C  C   . LYS A 1 212 ? -18.694 -9.818  23.784  1.00 21.30 ? 213 LYS A C   1 
ATOM   1656 O  O   . LYS A 1 212 ? -18.150 -10.936 23.716  1.00 20.20 ? 213 LYS A O   1 
ATOM   1657 C  CB  . LYS A 1 212 ? -19.357 -8.790  26.070  1.00 22.29 ? 213 LYS A CB  1 
ATOM   1658 C  CG  . LYS A 1 212 ? -19.976 -10.167 26.453  1.00 29.68 ? 213 LYS A CG  1 
ATOM   1659 C  CD  . LYS A 1 212 ? -21.336 -10.048 27.206  1.00 27.27 ? 213 LYS A CD  1 
ATOM   1660 C  CE  . LYS A 1 212 ? -22.531 -9.891  26.204  1.00 33.69 ? 213 LYS A CE  1 
ATOM   1661 N  NZ  . LYS A 1 212 ? -23.925 -9.601  26.861  1.00 35.08 ? 213 LYS A NZ  1 
ATOM   1662 N  N   . GLU A 1 213 ? -19.640 -9.457  22.933  1.00 20.47 ? 214 GLU A N   1 
ATOM   1663 C  CA  . GLU A 1 213 ? -20.184 -10.416 21.938  1.00 22.14 ? 214 GLU A CA  1 
ATOM   1664 C  C   . GLU A 1 213 ? -19.464 -10.300 20.593  1.00 19.36 ? 214 GLU A C   1 
ATOM   1665 O  O   . GLU A 1 213 ? -19.442 -9.205  20.024  1.00 19.18 ? 214 GLU A O   1 
ATOM   1666 C  CB  . GLU A 1 213 ? -21.661 -10.109 21.748  1.00 21.91 ? 214 GLU A CB  1 
ATOM   1667 C  CG  . GLU A 1 213 ? -22.320 -11.049 20.819  1.00 26.13 ? 214 GLU A CG  1 
ATOM   1668 C  CD  . GLU A 1 213 ? -23.825 -10.758 20.565  1.00 26.64 ? 214 GLU A CD  1 
ATOM   1669 O  OE1 . GLU A 1 213 ? -24.355 -11.361 19.607  1.00 35.41 ? 214 GLU A OE1 1 
ATOM   1670 O  OE2 . GLU A 1 213 ? -24.440 -9.940  21.247  1.00 25.89 ? 214 GLU A OE2 1 
ATOM   1671 N  N   . PRO A 1 214 ? -18.856 -11.382 20.092  1.00 19.39 ? 215 PRO A N   1 
ATOM   1672 C  CA  . PRO A 1 214 ? -18.226 -11.363 18.776  1.00 19.53 ? 215 PRO A CA  1 
ATOM   1673 C  C   . PRO A 1 214 ? -19.288 -11.329 17.703  1.00 20.33 ? 215 PRO A C   1 
ATOM   1674 O  O   . PRO A 1 214 ? -20.459 -11.693 17.955  1.00 20.28 ? 215 PRO A O   1 
ATOM   1675 C  CB  . PRO A 1 214 ? -17.381 -12.697 18.698  1.00 20.65 ? 215 PRO A CB  1 
ATOM   1676 C  CG  . PRO A 1 214 ? -17.713 -13.442 19.954  1.00 20.97 ? 215 PRO A CG  1 
ATOM   1677 C  CD  . PRO A 1 214 ? -18.797 -12.732 20.711  1.00 20.91 ? 215 PRO A CD  1 
ATOM   1678 N  N   . ILE A 1 215 ? -18.897 -10.885 16.512  1.00 17.80 ? 216 ILE A N   1 
ATOM   1679 C  CA  . ILE A 1 215 ? -19.710 -11.099 15.385  1.00 18.56 ? 216 ILE A CA  1 
ATOM   1680 C  C   . ILE A 1 215 ? -19.195 -12.356 14.685  1.00 19.35 ? 216 ILE A C   1 
ATOM   1681 O  O   . ILE A 1 215 ? -18.018 -12.718 14.833  1.00 20.65 ? 216 ILE A O   1 
ATOM   1682 C  CB  . ILE A 1 215 ? -19.719 -9.902  14.413  1.00 18.21 ? 216 ILE A CB  1 
ATOM   1683 C  CG1 . ILE A 1 215 ? -18.288 -9.516  13.942  1.00 16.81 ? 216 ILE A CG1 1 
ATOM   1684 C  CG2 . ILE A 1 215 ? -20.452 -8.632  15.080  1.00 18.38 ? 216 ILE A CG2 1 
ATOM   1685 C  CD1 . ILE A 1 215 ? -18.370 -8.516  12.686  1.00 15.96 ? 216 ILE A CD1 1 
ATOM   1686 N  N   . SER A 1 216 ? -20.065 -13.016 13.936  1.00 20.79 ? 217 SER A N   1 
ATOM   1687 C  CA  . SER A 1 216 ? -19.642 -14.172 13.062  1.00 21.88 ? 217 SER A CA  1 
ATOM   1688 C  C   . SER A 1 216 ? -19.445 -13.728 11.665  1.00 20.68 ? 217 SER A C   1 
ATOM   1689 O  O   . SER A 1 216 ? -20.266 -13.002 11.105  1.00 23.36 ? 217 SER A O   1 
ATOM   1690 C  CB  . SER A 1 216 ? -20.689 -15.298 12.985  1.00 23.79 ? 217 SER A CB  1 
ATOM   1691 O  OG  . SER A 1 216 ? -20.871 -15.810 14.256  1.00 34.48 ? 217 SER A OG  1 
ATOM   1692 N  N   . VAL A 1 217 ? -18.339 -14.153 11.095  1.00 18.07 ? 218 VAL A N   1 
ATOM   1693 C  CA  . VAL A 1 217 ? -18.062 -13.995 9.725   1.00 18.67 ? 218 VAL A CA  1 
ATOM   1694 C  C   . VAL A 1 217 ? -17.794 -15.372 9.107   1.00 18.17 ? 218 VAL A C   1 
ATOM   1695 O  O   . VAL A 1 217 ? -17.422 -16.333 9.816   1.00 18.64 ? 218 VAL A O   1 
ATOM   1696 C  CB  . VAL A 1 217 ? -16.880 -13.068 9.513   1.00 18.52 ? 218 VAL A CB  1 
ATOM   1697 C  CG1 . VAL A 1 217 ? -17.224 -11.718 10.188  1.00 18.51 ? 218 VAL A CG1 1 
ATOM   1698 C  CG2 . VAL A 1 217 ? -15.567 -13.708 10.155  1.00 17.97 ? 218 VAL A CG2 1 
ATOM   1699 N  N   . SER A 1 218 ? -17.955 -15.465 7.807   1.00 18.56 ? 219 SER A N   1 
ATOM   1700 C  CA  . SER A 1 218 ? -17.754 -16.786 7.186   1.00 19.28 ? 219 SER A CA  1 
ATOM   1701 C  C   . SER A 1 218 ? -16.322 -16.992 6.895   1.00 19.48 ? 219 SER A C   1 
ATOM   1702 O  O   . SER A 1 218 ? -15.508 -16.077 6.968   1.00 18.46 ? 219 SER A O   1 
ATOM   1703 C  CB  . SER A 1 218 ? -18.577 -16.954 5.959   1.00 16.53 ? 219 SER A CB  1 
ATOM   1704 O  OG  . SER A 1 218 ? -18.053 -16.171 4.945   1.00 20.00 ? 219 SER A OG  1 
ATOM   1705 N  N   . SER A 1 219 ? -15.966 -18.258 6.679   1.00 19.83 ? 220 SER A N   1 
ATOM   1706 C  CA  A SER A 1 219 ? -14.592 -18.618 6.441   0.50 18.99 ? 220 SER A CA  1 
ATOM   1707 C  CA  B SER A 1 219 ? -14.601 -18.620 6.450   0.50 19.68 ? 220 SER A CA  1 
ATOM   1708 C  C   . SER A 1 219 ? -14.182 -17.929 5.148   1.00 21.15 ? 220 SER A C   1 
ATOM   1709 O  O   . SER A 1 219 ? -13.043 -17.470 5.000   1.00 20.64 ? 220 SER A O   1 
ATOM   1710 C  CB  A SER A 1 219 ? -14.439 -20.169 6.381   0.50 19.82 ? 220 SER A CB  1 
ATOM   1711 C  CB  B SER A 1 219 ? -14.516 -20.171 6.409   0.50 20.59 ? 220 SER A CB  1 
ATOM   1712 O  OG  A SER A 1 219 ? -15.141 -20.747 5.281   0.50 16.49 ? 220 SER A OG  1 
ATOM   1713 O  OG  B SER A 1 219 ? -13.281 -20.635 5.917   0.50 21.26 ? 220 SER A OG  1 
ATOM   1714 N  N   . GLU A 1 220 ? -15.120 -17.840 4.190   1.00 21.61 ? 221 GLU A N   1 
ATOM   1715 C  CA  . GLU A 1 220 ? -14.832 -17.242 2.892   1.00 21.70 ? 221 GLU A CA  1 
ATOM   1716 C  C   . GLU A 1 220 ? -14.585 -15.730 3.041   1.00 19.53 ? 221 GLU A C   1 
ATOM   1717 O  O   . GLU A 1 220 ? -13.718 -15.156 2.373   1.00 18.19 ? 221 GLU A O   1 
ATOM   1718 C  CB  . GLU A 1 220 ? -15.990 -17.421 1.930   1.00 23.07 ? 221 GLU A CB  1 
ATOM   1719 C  CG  . GLU A 1 220 ? -16.240 -18.850 1.462   1.00 27.03 ? 221 GLU A CG  1 
ATOM   1720 C  CD  . GLU A 1 220 ? -17.329 -19.501 2.266   1.00 32.23 ? 221 GLU A CD  1 
ATOM   1721 O  OE1 . GLU A 1 220 ? -17.812 -18.953 3.291   1.00 32.91 ? 221 GLU A OE1 1 
ATOM   1722 O  OE2 . GLU A 1 220 ? -17.745 -20.591 1.840   1.00 37.90 ? 221 GLU A OE2 1 
ATOM   1723 N  N   . GLN A 1 221 ? -15.359 -15.102 3.907   1.00 18.97 ? 222 GLN A N   1 
ATOM   1724 C  CA  . GLN A 1 221 ? -15.137 -13.644 4.203   1.00 19.78 ? 222 GLN A CA  1 
ATOM   1725 C  C   . GLN A 1 221 ? -13.688 -13.378 4.731   1.00 20.96 ? 222 GLN A C   1 
ATOM   1726 O  O   . GLN A 1 221 ? -12.941 -12.548 4.181   1.00 20.61 ? 222 GLN A O   1 
ATOM   1727 C  CB  . GLN A 1 221 ? -16.211 -13.204 5.162   1.00 17.80 ? 222 GLN A CB  1 
ATOM   1728 C  CG  . GLN A 1 221 ? -17.535 -12.944 4.385   1.00 21.13 ? 222 GLN A CG  1 
ATOM   1729 C  CD  . GLN A 1 221 ? -18.609 -12.422 5.277   1.00 18.02 ? 222 GLN A CD  1 
ATOM   1730 O  OE1 . GLN A 1 221 ? -18.688 -12.816 6.446   1.00 20.23 ? 222 GLN A OE1 1 
ATOM   1731 N  NE2 . GLN A 1 221 ? -19.480 -11.553 4.734   1.00 17.46 ? 222 GLN A NE2 1 
ATOM   1732 N  N   . VAL A 1 222 ? -13.239 -14.132 5.747   1.00 22.26 ? 223 VAL A N   1 
ATOM   1733 C  CA  . VAL A 1 222 ? -11.867 -13.900 6.288   1.00 22.20 ? 223 VAL A CA  1 
ATOM   1734 C  C   . VAL A 1 222 ? -10.769 -14.370 5.334   1.00 23.16 ? 223 VAL A C   1 
ATOM   1735 O  O   . VAL A 1 222 ? -9.687  -13.782 5.262   1.00 21.35 ? 223 VAL A O   1 
ATOM   1736 C  CB  . VAL A 1 222 ? -11.719 -14.455 7.733   1.00 24.37 ? 223 VAL A CB  1 
ATOM   1737 C  CG1 . VAL A 1 222 ? -11.903 -15.917 7.716   1.00 22.39 ? 223 VAL A CG1 1 
ATOM   1738 C  CG2 . VAL A 1 222 ? -10.341 -14.075 8.330   1.00 22.64 ? 223 VAL A CG2 1 
ATOM   1739 N  N   . LEU A 1 223 ? -11.067 -15.401 4.534   1.00 22.79 ? 224 LEU A N   1 
ATOM   1740 C  CA  . LEU A 1 223 ? -10.109 -15.868 3.544   1.00 24.40 ? 224 LEU A CA  1 
ATOM   1741 C  C   . LEU A 1 223 ? -9.780  -14.747 2.587   1.00 23.82 ? 224 LEU A C   1 
ATOM   1742 O  O   . LEU A 1 223 ? -8.650  -14.632 2.130   1.00 23.73 ? 224 LEU A O   1 
ATOM   1743 C  CB  . LEU A 1 223 ? -10.760 -17.009 2.743   1.00 25.59 ? 224 LEU A CB  1 
ATOM   1744 C  CG  . LEU A 1 223 ? -9.944  -18.008 1.973   1.00 29.95 ? 224 LEU A CG  1 
ATOM   1745 C  CD1 . LEU A 1 223 ? -8.458  -18.048 2.434   1.00 32.09 ? 224 LEU A CD1 1 
ATOM   1746 C  CD2 . LEU A 1 223 ? -10.687 -19.425 2.102   1.00 32.48 ? 224 LEU A CD2 1 
ATOM   1747 N  N   . LYS A 1 224 ? -10.766 -13.911 2.285   1.00 21.92 ? 225 LYS A N   1 
ATOM   1748 C  CA  . LYS A 1 224 ? -10.530 -12.774 1.378   1.00 23.05 ? 225 LYS A CA  1 
ATOM   1749 C  C   . LYS A 1 224 ? -9.656  -11.634 1.991   1.00 22.18 ? 225 LYS A C   1 
ATOM   1750 O  O   . LYS A 1 224 ? -8.933  -10.968 1.243   1.00 21.89 ? 225 LYS A O   1 
ATOM   1751 C  CB  . LYS A 1 224 ? -11.865 -12.274 0.855   1.00 22.32 ? 225 LYS A CB  1 
ATOM   1752 C  CG  . LYS A 1 224 ? -12.525 -13.310 -0.115  1.00 28.09 ? 225 LYS A CG  1 
ATOM   1753 C  CD  . LYS A 1 224 ? -13.740 -12.746 -0.830  1.00 36.17 ? 225 LYS A CD  1 
ATOM   1754 C  CE  . LYS A 1 224 ? -13.467 -12.204 -2.252  1.00 40.59 ? 225 LYS A CE  1 
ATOM   1755 N  NZ  . LYS A 1 224 ? -14.796 -11.883 -2.904  1.00 41.18 ? 225 LYS A NZ  1 
ATOM   1756 N  N   . PHE A 1 225 ? -9.671  -11.467 3.324   1.00 20.20 ? 226 PHE A N   1 
ATOM   1757 C  CA  . PHE A 1 225 ? -8.709  -10.627 4.053   1.00 20.34 ? 226 PHE A CA  1 
ATOM   1758 C  C   . PHE A 1 225 ? -7.312  -11.102 3.812   1.00 20.20 ? 226 PHE A C   1 
ATOM   1759 O  O   . PHE A 1 225 ? -6.396  -10.318 3.638   1.00 20.58 ? 226 PHE A O   1 
ATOM   1760 C  CB  . PHE A 1 225 ? -8.905  -10.639 5.588   1.00 17.78 ? 226 PHE A CB  1 
ATOM   1761 C  CG  . PHE A 1 225 ? -10.143 -9.912  6.125   1.00 19.53 ? 226 PHE A CG  1 
ATOM   1762 C  CD1 . PHE A 1 225 ? -11.149 -9.419  5.287   1.00 19.71 ? 226 PHE A CD1 1 
ATOM   1763 C  CD2 . PHE A 1 225 ? -10.324 -9.802  7.537   1.00 20.65 ? 226 PHE A CD2 1 
ATOM   1764 C  CE1 . PHE A 1 225 ? -12.246 -8.765  5.847   1.00 20.00 ? 226 PHE A CE1 1 
ATOM   1765 C  CE2 . PHE A 1 225 ? -11.419 -9.172  8.099   1.00 21.84 ? 226 PHE A CE2 1 
ATOM   1766 C  CZ  . PHE A 1 225 ? -12.369 -8.632  7.244   1.00 19.61 ? 226 PHE A CZ  1 
ATOM   1767 N  N   . ARG A 1 226 ? -7.140  -12.426 3.851   1.00 21.76 ? 227 ARG A N   1 
ATOM   1768 C  CA  . ARG A 1 226 ? -5.829  -13.087 3.688   1.00 19.62 ? 227 ARG A CA  1 
ATOM   1769 C  C   . ARG A 1 226 ? -5.223  -13.029 2.316   1.00 21.04 ? 227 ARG A C   1 
ATOM   1770 O  O   . ARG A 1 226 ? -4.073  -13.361 2.181   1.00 24.27 ? 227 ARG A O   1 
ATOM   1771 C  CB  . ARG A 1 226 ? -5.911  -14.559 4.154   1.00 18.65 ? 227 ARG A CB  1 
ATOM   1772 C  CG  . ARG A 1 226 ? -6.416  -14.713 5.593   1.00 15.36 ? 227 ARG A CG  1 
ATOM   1773 C  CD  . ARG A 1 226 ? -6.227  -16.133 6.091   1.00 18.19 ? 227 ARG A CD  1 
ATOM   1774 N  NE  . ARG A 1 226 ? -6.791  -16.286 7.420   1.00 19.19 ? 227 ARG A NE  1 
ATOM   1775 C  CZ  . ARG A 1 226 ? -7.831  -17.075 7.727   1.00 23.54 ? 227 ARG A CZ  1 
ATOM   1776 N  NH1 . ARG A 1 226 ? -8.379  -17.869 6.800   1.00 22.45 ? 227 ARG A NH1 1 
ATOM   1777 N  NH2 . ARG A 1 226 ? -8.300  -17.099 8.977   1.00 19.68 ? 227 ARG A NH2 1 
ATOM   1778 N  N   . LYS A 1 227 ? -5.957  -12.598 1.319   1.00 21.39 ? 228 LYS A N   1 
ATOM   1779 C  CA  . LYS A 1 227 ? -5.454  -12.476 -0.060  1.00 21.75 ? 228 LYS A CA  1 
ATOM   1780 C  C   . LYS A 1 227 ? -4.866  -11.077 -0.343  1.00 21.73 ? 228 LYS A C   1 
ATOM   1781 O  O   . LYS A 1 227 ? -4.157  -10.847 -1.324  1.00 21.49 ? 228 LYS A O   1 
ATOM   1782 C  CB  . LYS A 1 227 ? -6.575  -12.798 -1.039  1.00 21.73 ? 228 LYS A CB  1 
ATOM   1783 C  CG  . LYS A 1 227 ? -6.905  -14.318 -1.143  1.00 25.93 ? 228 LYS A CG  1 
ATOM   1784 C  CD  . LYS A 1 227 ? -8.185  -14.451 -1.983  1.00 37.19 ? 228 LYS A CD  1 
ATOM   1785 C  CE  . LYS A 1 227 ? -8.185  -15.643 -2.965  1.00 41.21 ? 228 LYS A CE  1 
ATOM   1786 N  NZ  . LYS A 1 227 ? -9.016  -16.810 -2.476  1.00 45.25 ? 228 LYS A NZ  1 
ATOM   1787 N  N   . LEU A 1 228 ? -5.063  -10.173 0.592   1.00 22.10 ? 229 LEU A N   1 
ATOM   1788 C  CA  . LEU A 1 228 ? -4.365  -8.881  0.512   1.00 22.47 ? 229 LEU A CA  1 
ATOM   1789 C  C   . LEU A 1 228 ? -2.854  -8.998  0.641   1.00 23.56 ? 229 LEU A C   1 
ATOM   1790 O  O   . LEU A 1 228 ? -2.328  -10.003 1.152   1.00 22.29 ? 229 LEU A O   1 
ATOM   1791 C  CB  . LEU A 1 228 ? -4.936  -7.976  1.600   1.00 22.18 ? 229 LEU A CB  1 
ATOM   1792 C  CG  . LEU A 1 228 ? -6.384  -7.611  1.430   1.00 18.79 ? 229 LEU A CG  1 
ATOM   1793 C  CD1 . LEU A 1 228 ? -6.839  -6.981  2.758   1.00 19.02 ? 229 LEU A CD1 1 
ATOM   1794 C  CD2 . LEU A 1 228 ? -6.450  -6.599  0.324   1.00 21.06 ? 229 LEU A CD2 1 
ATOM   1795 N  N   . ASN A 1 229 ? -2.137  -7.966  0.187   1.00 24.39 ? 230 ASN A N   1 
ATOM   1796 C  CA  . ASN A 1 229 ? -0.704  -7.957  0.354   1.00 25.17 ? 230 ASN A CA  1 
ATOM   1797 C  C   . ASN A 1 229 ? -0.144  -6.800  1.241   1.00 25.16 ? 230 ASN A C   1 
ATOM   1798 O  O   . ASN A 1 229 ? -0.628  -5.684  1.173   1.00 24.62 ? 230 ASN A O   1 
ATOM   1799 C  CB  . ASN A 1 229 ? -0.006  -7.848  -1.007  1.00 26.15 ? 230 ASN A CB  1 
ATOM   1800 C  CG  . ASN A 1 229 ? -0.254  -9.027  -1.953  1.00 28.45 ? 230 ASN A CG  1 
ATOM   1801 O  OD1 . ASN A 1 229 ? 0.053   -8.885  -3.135  1.00 31.59 ? 230 ASN A OD1 1 
ATOM   1802 N  ND2 . ASN A 1 229 ? -0.766  -10.187 -1.454  1.00 27.31 ? 230 ASN A ND2 1 
ATOM   1803 N  N   . PHE A 1 230 ? 0.907   -7.094  2.023   1.00 26.10 ? 231 PHE A N   1 
ATOM   1804 C  CA  . PHE A 1 230 ? 1.686   -6.091  2.779   1.00 27.16 ? 231 PHE A CA  1 
ATOM   1805 C  C   . PHE A 1 230 ? 2.507   -5.216  1.798   1.00 29.56 ? 231 PHE A C   1 
ATOM   1806 O  O   . PHE A 1 230 ? 2.573   -3.986  1.969   1.00 29.75 ? 231 PHE A O   1 
ATOM   1807 C  CB  . PHE A 1 230 ? 2.702   -6.731  3.689   1.00 26.84 ? 231 PHE A CB  1 
ATOM   1808 C  CG  . PHE A 1 230 ? 2.128   -7.329  4.984   1.00 27.12 ? 231 PHE A CG  1 
ATOM   1809 C  CD1 . PHE A 1 230 ? 1.351   -6.573  5.861   1.00 25.61 ? 231 PHE A CD1 1 
ATOM   1810 C  CD2 . PHE A 1 230 ? 2.449   -8.650  5.322   1.00 26.75 ? 231 PHE A CD2 1 
ATOM   1811 C  CE1 . PHE A 1 230 ? 0.864   -7.141  7.085   1.00 25.69 ? 231 PHE A CE1 1 
ATOM   1812 C  CE2 . PHE A 1 230 ? 1.976   -9.233  6.489   1.00 24.96 ? 231 PHE A CE2 1 
ATOM   1813 C  CZ  . PHE A 1 230 ? 1.198   -8.495  7.393   1.00 22.93 ? 231 PHE A CZ  1 
ATOM   1814 N  N   . ASN A 1 231 ? 3.065   -5.866  0.775   1.00 30.38 ? 232 ASN A N   1 
ATOM   1815 C  CA  . ASN A 1 231 ? 3.958   -5.260  -0.266  1.00 31.93 ? 232 ASN A CA  1 
ATOM   1816 C  C   . ASN A 1 231 ? 3.269   -4.358  -1.232  1.00 32.29 ? 232 ASN A C   1 
ATOM   1817 O  O   . ASN A 1 231 ? 2.057   -4.466  -1.446  1.00 31.42 ? 232 ASN A O   1 
ATOM   1818 C  CB  . ASN A 1 231 ? 4.591   -6.369  -1.110  1.00 33.11 ? 232 ASN A CB  1 
ATOM   1819 C  CG  . ASN A 1 231 ? 3.554   -7.265  -1.749  1.00 34.30 ? 232 ASN A CG  1 
ATOM   1820 O  OD1 . ASN A 1 231 ? 3.181   -8.265  -1.176  1.00 34.86 ? 232 ASN A OD1 1 
ATOM   1821 N  ND2 . ASN A 1 231 ? 3.097   -6.907  -2.936  1.00 33.52 ? 232 ASN A ND2 1 
ATOM   1822 N  N   . GLY A 1 232 ? 4.014   -3.470  -1.876  1.00 33.12 ? 233 GLY A N   1 
ATOM   1823 C  CA  . GLY A 1 232 ? 3.379   -2.687  -2.938  1.00 34.22 ? 233 GLY A CA  1 
ATOM   1824 C  C   . GLY A 1 232 ? 3.385   -3.507  -4.244  1.00 35.68 ? 233 GLY A C   1 
ATOM   1825 O  O   . GLY A 1 232 ? 4.183   -4.417  -4.362  1.00 34.67 ? 233 GLY A O   1 
ATOM   1826 N  N   . GLU A 1 233 ? 2.496   -3.166  -5.185  1.00 38.42 ? 234 GLU A N   1 
ATOM   1827 C  CA  . GLU A 1 233 ? 2.480   -3.681  -6.579  1.00 42.18 ? 234 GLU A CA  1 
ATOM   1828 C  C   . GLU A 1 233 ? 3.875   -3.655  -7.237  1.00 43.43 ? 234 GLU A C   1 
ATOM   1829 O  O   . GLU A 1 233 ? 4.471   -2.604  -7.341  1.00 43.37 ? 234 GLU A O   1 
ATOM   1830 C  CB  . GLU A 1 233 ? 1.461   -2.890  -7.420  1.00 41.47 ? 234 GLU A CB  1 
ATOM   1831 C  CG  . GLU A 1 233 ? 1.158   -3.465  -8.822  1.00 42.89 ? 234 GLU A CG  1 
ATOM   1832 C  CD  . GLU A 1 233 ? 0.244   -2.534  -9.654  1.00 43.93 ? 234 GLU A CD  1 
ATOM   1833 O  OE1 . GLU A 1 233 ? -0.198  -1.496  -9.112  1.00 45.58 ? 234 GLU A OE1 1 
ATOM   1834 O  OE2 . GLU A 1 233 ? -0.030  -2.812  -10.849 1.00 43.48 ? 234 GLU A OE2 1 
ATOM   1835 N  N   . GLY A 1 234 ? 4.412   -4.821  -7.633  1.00 45.51 ? 235 GLY A N   1 
ATOM   1836 C  CA  . GLY A 1 234 ? 5.799   -4.884  -8.176  1.00 47.35 ? 235 GLY A CA  1 
ATOM   1837 C  C   . GLY A 1 234 ? 6.964   -5.091  -7.203  1.00 48.66 ? 235 GLY A C   1 
ATOM   1838 O  O   . GLY A 1 234 ? 8.145   -5.041  -7.586  1.00 48.70 ? 235 GLY A O   1 
ATOM   1839 N  N   . GLU A 1 235 ? 6.643   -5.293  -5.925  1.00 49.00 ? 236 GLU A N   1 
ATOM   1840 C  CA  . GLU A 1 235 ? 7.610   -5.836  -4.951  1.00 49.43 ? 236 GLU A CA  1 
ATOM   1841 C  C   . GLU A 1 235 ? 7.153   -7.290  -4.727  1.00 47.47 ? 236 GLU A C   1 
ATOM   1842 O  O   . GLU A 1 235 ? 5.994   -7.618  -5.055  1.00 47.72 ? 236 GLU A O   1 
ATOM   1843 C  CB  . GLU A 1 235 ? 7.601   -5.018  -3.647  1.00 49.30 ? 236 GLU A CB  1 
ATOM   1844 C  CG  . GLU A 1 235 ? 7.351   -3.507  -3.859  1.00 51.56 ? 236 GLU A CG  1 
ATOM   1845 C  CD  . GLU A 1 235 ? 7.132   -2.700  -2.551  1.00 52.87 ? 236 GLU A CD  1 
ATOM   1846 O  OE1 . GLU A 1 235 ? 7.401   -1.460  -2.564  1.00 58.56 ? 236 GLU A OE1 1 
ATOM   1847 O  OE2 . GLU A 1 235 ? 6.685   -3.278  -1.518  1.00 56.00 ? 236 GLU A OE2 1 
ATOM   1848 N  N   . PRO A 1 236 ? 8.052   -8.182  -4.236  1.00 46.54 ? 237 PRO A N   1 
ATOM   1849 C  CA  . PRO A 1 236 ? 7.672   -9.589  -3.912  1.00 44.76 ? 237 PRO A CA  1 
ATOM   1850 C  C   . PRO A 1 236 ? 6.417   -9.724  -3.003  1.00 42.99 ? 237 PRO A C   1 
ATOM   1851 O  O   . PRO A 1 236 ? 6.202   -8.904  -2.093  1.00 42.47 ? 237 PRO A O   1 
ATOM   1852 C  CB  . PRO A 1 236 ? 8.917   -10.144 -3.223  1.00 44.91 ? 237 PRO A CB  1 
ATOM   1853 C  CG  . PRO A 1 236 ? 10.043  -9.355  -3.819  1.00 45.90 ? 237 PRO A CG  1 
ATOM   1854 C  CD  . PRO A 1 236 ? 9.496   -7.955  -4.024  1.00 47.00 ? 237 PRO A CD  1 
ATOM   1855 N  N   . GLU A 1 237 ? 5.604   -10.742 -3.276  1.00 39.96 ? 238 GLU A N   1 
ATOM   1856 C  CA  . GLU A 1 237 ? 4.308   -10.863 -2.648  1.00 37.09 ? 238 GLU A CA  1 
ATOM   1857 C  C   . GLU A 1 237 ? 4.404   -11.433 -1.221  1.00 34.63 ? 238 GLU A C   1 
ATOM   1858 O  O   . GLU A 1 237 ? 4.919   -12.514 -1.022  1.00 33.05 ? 238 GLU A O   1 
ATOM   1859 C  CB  . GLU A 1 237 ? 3.363   -11.715 -3.526  1.00 37.87 ? 238 GLU A CB  1 
ATOM   1860 C  CG  . GLU A 1 237 ? 1.997   -11.834 -2.894  1.00 36.46 ? 238 GLU A CG  1 
ATOM   1861 C  CD  . GLU A 1 237 ? 0.975   -12.595 -3.711  1.00 38.95 ? 238 GLU A CD  1 
ATOM   1862 O  OE1 . GLU A 1 237 ? 1.346   -13.515 -4.482  1.00 44.88 ? 238 GLU A OE1 1 
ATOM   1863 O  OE2 . GLU A 1 237 ? -0.220  -12.284 -3.536  1.00 37.87 ? 238 GLU A OE2 1 
ATOM   1864 N  N   . GLU A 1 238 ? 3.912   -10.681 -0.234  1.00 32.36 ? 239 GLU A N   1 
ATOM   1865 C  CA  . GLU A 1 238 ? 3.843   -11.132 1.143   1.00 32.37 ? 239 GLU A CA  1 
ATOM   1866 C  C   . GLU A 1 238 ? 2.370   -11.015 1.538   1.00 28.42 ? 239 GLU A C   1 
ATOM   1867 O  O   . GLU A 1 238 ? 1.842   -9.907  1.549   1.00 26.66 ? 239 GLU A O   1 
ATOM   1868 C  CB  . GLU A 1 238 ? 4.597   -10.185 2.058   1.00 32.39 ? 239 GLU A CB  1 
ATOM   1869 C  CG  . GLU A 1 238 ? 5.858   -9.548  1.489   1.00 39.54 ? 239 GLU A CG  1 
ATOM   1870 C  CD  . GLU A 1 238 ? 6.274   -8.240  2.266   1.00 40.29 ? 239 GLU A CD  1 
ATOM   1871 O  OE1 . GLU A 1 238 ? 6.843   -7.326  1.607   1.00 50.36 ? 239 GLU A OE1 1 
ATOM   1872 O  OE2 . GLU A 1 238 ? 6.015   -8.132  3.516   1.00 48.32 ? 239 GLU A OE2 1 
ATOM   1873 N  N   . LEU A 1 239 ? 1.684   -12.128 1.785   1.00 24.71 ? 240 LEU A N   1 
ATOM   1874 C  CA  . LEU A 1 239 ? 0.256   -11.991 2.107   1.00 23.18 ? 240 LEU A CA  1 
ATOM   1875 C  C   . LEU A 1 239 ? 0.114   -11.201 3.433   1.00 21.60 ? 240 LEU A C   1 
ATOM   1876 O  O   . LEU A 1 239 ? 0.857   -11.412 4.377   1.00 21.42 ? 240 LEU A O   1 
ATOM   1877 C  CB  . LEU A 1 239 ? -0.381  -13.345 2.341   1.00 22.46 ? 240 LEU A CB  1 
ATOM   1878 C  CG  . LEU A 1 239 ? -0.468  -14.241 1.126   1.00 26.10 ? 240 LEU A CG  1 
ATOM   1879 C  CD1 . LEU A 1 239 ? -1.320  -15.467 1.574   1.00 23.99 ? 240 LEU A CD1 1 
ATOM   1880 C  CD2 . LEU A 1 239 ? -1.146  -13.521 -0.029  1.00 26.41 ? 240 LEU A CD2 1 
ATOM   1881 N  N   . MET A 1 240 ? -0.884  -10.326 3.459   1.00 21.45 ? 241 MET A N   1 
ATOM   1882 C  CA  . MET A 1 240 ? -1.269  -9.597  4.644   1.00 20.16 ? 241 MET A CA  1 
ATOM   1883 C  C   . MET A 1 240 ? -2.045  -10.500 5.579   1.00 18.16 ? 241 MET A C   1 
ATOM   1884 O  O   . MET A 1 240 ? -3.239  -10.655 5.426   1.00 17.71 ? 241 MET A O   1 
ATOM   1885 C  CB  . MET A 1 240 ? -2.175  -8.427  4.254   1.00 18.74 ? 241 MET A CB  1 
ATOM   1886 C  CG  . MET A 1 240 ? -2.400  -7.410  5.466   1.00 21.68 ? 241 MET A CG  1 
ATOM   1887 S  SD  . MET A 1 240 ? -3.302  -6.063  4.855   1.00 23.18 ? 241 MET A SD  1 
ATOM   1888 C  CE  . MET A 1 240 ? -2.007  -4.967  4.159   1.00 22.56 ? 241 MET A CE  1 
ATOM   1889 N  N   . VAL A 1 241 ? -1.333  -11.127 6.503   1.00 18.45 ? 242 VAL A N   1 
ATOM   1890 C  CA  . VAL A 1 241 ? -1.894  -12.006 7.493   1.00 19.42 ? 242 VAL A CA  1 
ATOM   1891 C  C   . VAL A 1 241 ? -1.071  -11.790 8.736   1.00 19.02 ? 242 VAL A C   1 
ATOM   1892 O  O   . VAL A 1 241 ? 0.107   -11.366 8.612   1.00 20.39 ? 242 VAL A O   1 
ATOM   1893 C  CB  . VAL A 1 241 ? -1.825  -13.504 7.068   1.00 19.50 ? 242 VAL A CB  1 
ATOM   1894 C  CG1 . VAL A 1 241 ? -2.688  -13.748 5.806   1.00 20.80 ? 242 VAL A CG1 1 
ATOM   1895 C  CG2 . VAL A 1 241 ? -0.371  -13.970 6.846   1.00 19.81 ? 242 VAL A CG2 1 
ATOM   1896 N  N   . ASP A 1 242 ? -1.669  -12.099 9.895   1.00 17.59 ? 243 ASP A N   1 
ATOM   1897 C  CA  . ASP A 1 242 ? -1.026  -11.967 11.172  1.00 18.30 ? 243 ASP A CA  1 
ATOM   1898 C  C   . ASP A 1 242 ? -0.536  -10.521 11.399  1.00 17.78 ? 243 ASP A C   1 
ATOM   1899 O  O   . ASP A 1 242 ? 0.551   -10.283 11.898  1.00 18.82 ? 243 ASP A O   1 
ATOM   1900 C  CB  . ASP A 1 242 ? 0.100   -13.019 11.441  1.00 18.79 ? 243 ASP A CB  1 
ATOM   1901 C  CG  . ASP A 1 242 ? -0.425  -14.418 11.543  1.00 20.63 ? 243 ASP A CG  1 
ATOM   1902 O  OD1 . ASP A 1 242 ? -1.476  -14.606 12.205  1.00 19.29 ? 243 ASP A OD1 1 
ATOM   1903 O  OD2 . ASP A 1 242 ? 0.185   -15.334 10.952  1.00 19.62 ? 243 ASP A OD2 1 
ATOM   1904 N  N   . ASN A 1 243 ? -1.407  -9.571  11.093  1.00 16.12 ? 244 ASN A N   1 
ATOM   1905 C  CA  . ASN A 1 243 ? -1.103  -8.140  11.352  1.00 15.65 ? 244 ASN A CA  1 
ATOM   1906 C  C   . ASN A 1 243 ? -1.691  -7.737  12.718  1.00 15.48 ? 244 ASN A C   1 
ATOM   1907 O  O   . ASN A 1 243 ? -2.292  -6.657  12.862  1.00 17.65 ? 244 ASN A O   1 
ATOM   1908 C  CB  . ASN A 1 243 ? -1.669  -7.279  10.216  1.00 15.62 ? 244 ASN A CB  1 
ATOM   1909 C  CG  . ASN A 1 243 ? -3.220  -7.484  9.955   1.00 18.88 ? 244 ASN A CG  1 
ATOM   1910 O  OD1 . ASN A 1 243 ? -3.846  -8.407  10.449  1.00 19.89 ? 244 ASN A OD1 1 
ATOM   1911 N  ND2 . ASN A 1 243 ? -3.814  -6.534  9.246   1.00 20.22 ? 244 ASN A ND2 1 
ATOM   1912 N  N   . TRP A 1 244 ? -1.407  -8.552  13.716  1.00 15.49 ? 245 TRP A N   1 
ATOM   1913 C  CA  . TRP A 1 244 ? -1.832  -8.273  15.076  1.00 16.40 ? 245 TRP A CA  1 
ATOM   1914 C  C   . TRP A 1 244 ? -0.671  -8.166  16.005  1.00 18.05 ? 245 TRP A C   1 
ATOM   1915 O  O   . TRP A 1 244 ? 0.384   -8.821  15.802  1.00 17.47 ? 245 TRP A O   1 
ATOM   1916 C  CB  . TRP A 1 244 ? -2.863  -9.332  15.563  1.00 13.93 ? 245 TRP A CB  1 
ATOM   1917 C  CG  . TRP A 1 244 ? -2.396  -10.774 15.387  1.00 14.17 ? 245 TRP A CG  1 
ATOM   1918 C  CD1 . TRP A 1 244 ? -2.512  -11.514 14.292  1.00 14.71 ? 245 TRP A CD1 1 
ATOM   1919 C  CD2 . TRP A 1 244 ? -1.786  -11.614 16.379  1.00 16.22 ? 245 TRP A CD2 1 
ATOM   1920 N  NE1 . TRP A 1 244 ? -2.007  -12.788 14.489  1.00 13.92 ? 245 TRP A NE1 1 
ATOM   1921 C  CE2 . TRP A 1 244 ? -1.560  -12.888 15.767  1.00 18.47 ? 245 TRP A CE2 1 
ATOM   1922 C  CE3 . TRP A 1 244 ? -1.504  -11.462 17.761  1.00 17.85 ? 245 TRP A CE3 1 
ATOM   1923 C  CZ2 . TRP A 1 244 ? -0.962  -14.000 16.471  1.00 14.82 ? 245 TRP A CZ2 1 
ATOM   1924 C  CZ3 . TRP A 1 244 ? -0.893  -12.533 18.462  1.00 17.44 ? 245 TRP A CZ3 1 
ATOM   1925 C  CH2 . TRP A 1 244 ? -0.669  -13.803 17.803  1.00 19.49 ? 245 TRP A CH2 1 
ATOM   1926 N  N   . ARG A 1 245 ? -0.849  -7.325  17.030  1.00 16.43 ? 246 ARG A N   1 
ATOM   1927 C  CA  . ARG A 1 245 ? 0.079   -7.221  18.123  1.00 16.13 ? 246 ARG A CA  1 
ATOM   1928 C  C   . ARG A 1 245 ? -0.378  -8.089  19.226  1.00 18.53 ? 246 ARG A C   1 
ATOM   1929 O  O   . ARG A 1 245 ? -1.567  -8.088  19.571  1.00 18.65 ? 246 ARG A O   1 
ATOM   1930 C  CB  . ARG A 1 245 ? 0.130   -5.730  18.621  1.00 16.80 ? 246 ARG A CB  1 
ATOM   1931 C  CG  . ARG A 1 245 ? 1.215   -5.510  19.623  1.00 16.01 ? 246 ARG A CG  1 
ATOM   1932 C  CD  . ARG A 1 245 ? 1.169   -4.130  20.342  1.00 16.78 ? 246 ARG A CD  1 
ATOM   1933 N  NE  . ARG A 1 245 ? 2.445   -3.823  21.014  1.00 15.92 ? 246 ARG A NE  1 
ATOM   1934 C  CZ  . ARG A 1 245 ? 2.608   -2.779  21.838  1.00 21.74 ? 246 ARG A CZ  1 
ATOM   1935 N  NH1 . ARG A 1 245 ? 1.607   -1.927  22.133  1.00 16.54 ? 246 ARG A NH1 1 
ATOM   1936 N  NH2 . ARG A 1 245 ? 3.784   -2.544  22.340  1.00 23.86 ? 246 ARG A NH2 1 
ATOM   1937 N  N   . PRO A 1 246 ? 0.541   -8.874  19.823  1.00 19.86 ? 247 PRO A N   1 
ATOM   1938 C  CA  . PRO A 1 246 ? 0.140   -9.652  20.963  1.00 19.41 ? 247 PRO A CA  1 
ATOM   1939 C  C   . PRO A 1 246 ? -0.213  -8.854  22.226  1.00 18.52 ? 247 PRO A C   1 
ATOM   1940 O  O   . PRO A 1 246 ? 0.179   -7.701  22.409  1.00 18.01 ? 247 PRO A O   1 
ATOM   1941 C  CB  . PRO A 1 246 ? 1.393   -10.514 21.246  1.00 21.31 ? 247 PRO A CB  1 
ATOM   1942 C  CG  . PRO A 1 246 ? 2.282   -10.374 20.025  1.00 22.13 ? 247 PRO A CG  1 
ATOM   1943 C  CD  . PRO A 1 246 ? 1.966   -9.049  19.478  1.00 20.98 ? 247 PRO A CD  1 
ATOM   1944 N  N   . ALA A 1 247 ? -0.864  -9.528  23.158  1.00 18.83 ? 248 ALA A N   1 
ATOM   1945 C  CA  . ALA A 1 247 ? -1.220  -8.947  24.408  1.00 19.37 ? 248 ALA A CA  1 
ATOM   1946 C  C   . ALA A 1 247 ? -0.010  -8.457  25.175  1.00 21.52 ? 248 ALA A C   1 
ATOM   1947 O  O   . ALA A 1 247 ? 1.069   -9.071  25.176  1.00 19.34 ? 248 ALA A O   1 
ATOM   1948 C  CB  . ALA A 1 247 ? -2.070  -9.950  25.266  1.00 19.23 ? 248 ALA A CB  1 
ATOM   1949 N  N   . GLN A 1 248 ? -0.221  -7.322  25.820  1.00 19.14 ? 249 GLN A N   1 
ATOM   1950 C  CA  . GLN A 1 248 ? 0.788   -6.584  26.486  1.00 20.76 ? 249 GLN A CA  1 
ATOM   1951 C  C   . GLN A 1 248 ? 0.417   -6.643  27.944  1.00 21.08 ? 249 GLN A C   1 
ATOM   1952 O  O   . GLN A 1 248 ? -0.736  -6.878  28.278  1.00 21.38 ? 249 GLN A O   1 
ATOM   1953 C  CB  . GLN A 1 248 ? 0.810   -5.108  25.998  1.00 18.63 ? 249 GLN A CB  1 
ATOM   1954 C  CG  . GLN A 1 248 ? 1.179   -4.947  24.495  1.00 19.86 ? 249 GLN A CG  1 
ATOM   1955 C  CD  . GLN A 1 248 ? 2.459   -5.645  24.154  1.00 23.15 ? 249 GLN A CD  1 
ATOM   1956 O  OE1 . GLN A 1 248 ? 3.480   -5.367  24.785  1.00 27.37 ? 249 GLN A OE1 1 
ATOM   1957 N  NE2 . GLN A 1 248 ? 2.432   -6.574  23.166  1.00 18.48 ? 249 GLN A NE2 1 
ATOM   1958 N  N   . PRO A 1 249 ? 1.401   -6.397  28.815  1.00 22.71 ? 250 PRO A N   1 
ATOM   1959 C  CA  . PRO A 1 249 ? 1.258   -6.421  30.226  1.00 22.69 ? 250 PRO A CA  1 
ATOM   1960 C  C   . PRO A 1 249 ? 0.228   -5.422  30.670  1.00 22.83 ? 250 PRO A C   1 
ATOM   1961 O  O   . PRO A 1 249 ? 0.324   -4.246  30.284  1.00 23.02 ? 250 PRO A O   1 
ATOM   1962 C  CB  . PRO A 1 249 ? 2.630   -5.936  30.711  1.00 23.59 ? 250 PRO A CB  1 
ATOM   1963 C  CG  . PRO A 1 249 ? 3.546   -6.268  29.606  1.00 24.42 ? 250 PRO A CG  1 
ATOM   1964 C  CD  . PRO A 1 249 ? 2.763   -5.999  28.402  1.00 21.47 ? 250 PRO A CD  1 
ATOM   1965 N  N   . LEU A 1 250 ? -0.680  -5.847  31.543  1.00 22.97 ? 251 LEU A N   1 
ATOM   1966 C  CA  . LEU A 1 250 ? -1.713  -4.951  32.068  1.00 25.88 ? 251 LEU A CA  1 
ATOM   1967 C  C   . LEU A 1 250 ? -1.117  -3.871  32.992  1.00 26.37 ? 251 LEU A C   1 
ATOM   1968 O  O   . LEU A 1 250 ? -1.620  -2.726  33.013  1.00 25.70 ? 251 LEU A O   1 
ATOM   1969 C  CB  . LEU A 1 250 ? -2.862  -5.732  32.738  1.00 25.98 ? 251 LEU A CB  1 
ATOM   1970 C  CG  . LEU A 1 250 ? -4.184  -4.988  32.997  1.00 25.61 ? 251 LEU A CG  1 
ATOM   1971 C  CD1 . LEU A 1 250 ? -4.809  -4.410  31.726  1.00 19.57 ? 251 LEU A CD1 1 
ATOM   1972 C  CD2 . LEU A 1 250 ? -5.148  -5.924  33.729  1.00 29.13 ? 251 LEU A CD2 1 
ATOM   1973 N  N   . LYS A 1 251 ? -0.012  -4.211  33.691  1.00 26.07 ? 252 LYS A N   1 
ATOM   1974 C  CA  . LYS A 1 251 ? 0.659   -3.286  34.608  1.00 26.46 ? 252 LYS A CA  1 
ATOM   1975 C  C   . LYS A 1 251 ? -0.399  -2.750  35.599  1.00 27.28 ? 252 LYS A C   1 
ATOM   1976 O  O   . LYS A 1 251 ? -1.235  -3.506  36.102  1.00 28.25 ? 252 LYS A O   1 
ATOM   1977 C  CB  . LYS A 1 251 ? 1.380   -2.193  33.820  1.00 25.73 ? 252 LYS A CB  1 
ATOM   1978 C  CG  . LYS A 1 251 ? 2.549   -2.746  33.059  1.00 27.34 ? 252 LYS A CG  1 
ATOM   1979 C  CD  . LYS A 1 251 ? 3.553   -1.764  32.628  1.00 33.46 ? 252 LYS A CD  1 
ATOM   1980 C  CE  . LYS A 1 251 ? 4.629   -2.532  31.848  1.00 34.04 ? 252 LYS A CE  1 
ATOM   1981 N  NZ  . LYS A 1 251 ? 5.391   -1.573  31.057  1.00 38.10 ? 252 LYS A NZ  1 
ATOM   1982 N  N   . ASN A 1 252 ? -0.425  -1.493  35.921  1.00 29.26 ? 253 ASN A N   1 
ATOM   1983 C  CA  . ASN A 1 252 ? -1.412  -1.179  36.957  1.00 33.76 ? 253 ASN A CA  1 
ATOM   1984 C  C   . ASN A 1 252 ? -2.686  -0.524  36.330  1.00 34.34 ? 253 ASN A C   1 
ATOM   1985 O  O   . ASN A 1 252 ? -2.856  0.741   36.397  1.00 37.70 ? 253 ASN A O   1 
ATOM   1986 C  CB  . ASN A 1 252 ? -0.830  -0.401  38.165  1.00 34.79 ? 253 ASN A CB  1 
ATOM   1987 C  CG  . ASN A 1 252 ? -1.776  0.165   39.051  0.00 42.88 ? 253 ASN A CG  1 
ATOM   1988 O  OD1 . ASN A 1 252 ? -2.204  1.306   39.225  0.00 49.26 ? 253 ASN A OD1 1 
ATOM   1989 N  ND2 . ASN A 1 252 ? -2.126  -0.857  39.823  0.00 46.77 ? 253 ASN A ND2 1 
ATOM   1990 N  N   . ARG A 1 253 ? -3.479  -1.367  35.635  1.00 31.78 ? 254 ARG A N   1 
ATOM   1991 C  CA  . ARG A 1 253 ? -4.767  -0.966  35.059  1.00 30.04 ? 254 ARG A CA  1 
ATOM   1992 C  C   . ARG A 1 253 ? -5.827  -1.990  35.444  1.00 31.02 ? 254 ARG A C   1 
ATOM   1993 O  O   . ARG A 1 253 ? -5.508  -3.173  35.587  1.00 31.52 ? 254 ARG A O   1 
ATOM   1994 C  CB  . ARG A 1 253 ? -4.707  -0.804  33.520  1.00 28.28 ? 254 ARG A CB  1 
ATOM   1995 C  CG  . ARG A 1 253 ? -3.608  0.083   33.046  1.00 25.79 ? 254 ARG A CG  1 
ATOM   1996 C  CD  . ARG A 1 253 ? -3.567  0.132   31.570  1.00 23.21 ? 254 ARG A CD  1 
ATOM   1997 N  NE  . ARG A 1 253 ? -2.707  -0.963  31.062  1.00 24.25 ? 254 ARG A NE  1 
ATOM   1998 C  CZ  . ARG A 1 253 ? -2.529  -1.247  29.783  1.00 21.66 ? 254 ARG A CZ  1 
ATOM   1999 N  NH1 . ARG A 1 253 ? -3.235  -0.548  28.861  1.00 14.46 ? 254 ARG A NH1 1 
ATOM   2000 N  NH2 . ARG A 1 253 ? -1.662  -2.218  29.422  1.00 17.14 ? 254 ARG A NH2 1 
ATOM   2001 N  N   . GLN A 1 254 ? -7.075  -1.554  35.655  1.00 30.90 ? 255 GLN A N   1 
ATOM   2002 C  CA  . GLN A 1 254 ? -8.142  -2.531  35.812  1.00 33.32 ? 255 GLN A CA  1 
ATOM   2003 C  C   . GLN A 1 254 ? -9.147  -2.414  34.653  1.00 30.77 ? 255 GLN A C   1 
ATOM   2004 O  O   . GLN A 1 254 ? -9.522  -1.325  34.188  1.00 30.82 ? 255 GLN A O   1 
ATOM   2005 C  CB  . GLN A 1 254 ? -8.808  -2.515  37.211  1.00 33.47 ? 255 GLN A CB  1 
ATOM   2006 C  CG  . GLN A 1 254 ? -9.751  -1.369  37.500  1.00 38.48 ? 255 GLN A CG  1 
ATOM   2007 C  CD  . GLN A 1 254 ? -10.820 -1.720  38.590  1.00 40.11 ? 255 GLN A CD  1 
ATOM   2008 O  OE1 . GLN A 1 254 ? -11.613 -0.847  38.997  1.00 49.67 ? 255 GLN A OE1 1 
ATOM   2009 N  NE2 . GLN A 1 254 ? -10.832 -2.995  39.061  1.00 44.74 ? 255 GLN A NE2 1 
ATOM   2010 N  N   . ILE A 1 255 ? -9.526  -3.557  34.149  1.00 27.58 ? 256 ILE A N   1 
ATOM   2011 C  CA  . ILE A 1 255 ? -10.559 -3.634  33.147  1.00 25.19 ? 256 ILE A CA  1 
ATOM   2012 C  C   . ILE A 1 255 ? -11.916 -3.603  33.833  1.00 25.17 ? 256 ILE A C   1 
ATOM   2013 O  O   . ILE A 1 255 ? -12.154 -4.336  34.804  1.00 23.32 ? 256 ILE A O   1 
ATOM   2014 C  CB  . ILE A 1 255 ? -10.379 -4.885  32.273  1.00 24.08 ? 256 ILE A CB  1 
ATOM   2015 C  CG1 . ILE A 1 255 ? -8.929  -4.864  31.729  1.00 23.66 ? 256 ILE A CG1 1 
ATOM   2016 C  CG2 . ILE A 1 255 ? -11.493 -4.913  31.160  1.00 22.13 ? 256 ILE A CG2 1 
ATOM   2017 C  CD1 . ILE A 1 255 ? -8.555  -6.177  30.997  1.00 21.99 ? 256 ILE A CD1 1 
ATOM   2018 N  N   . LYS A 1 256 ? -12.760 -2.677  33.383  1.00 23.08 ? 257 LYS A N   1 
ATOM   2019 C  CA  . LYS A 1 256 ? -14.106 -2.579  33.913  1.00 24.76 ? 257 LYS A CA  1 
ATOM   2020 C  C   . LYS A 1 256 ? -15.074 -3.252  32.982  1.00 23.80 ? 257 LYS A C   1 
ATOM   2021 O  O   . LYS A 1 256 ? -14.857 -3.278  31.794  1.00 23.91 ? 257 LYS A O   1 
ATOM   2022 C  CB  . LYS A 1 256 ? -14.513 -1.089  34.082  1.00 24.55 ? 257 LYS A CB  1 
ATOM   2023 C  CG  . LYS A 1 256 ? -13.976 -0.511  35.355  1.00 31.10 ? 257 LYS A CG  1 
ATOM   2024 C  CD  . LYS A 1 256 ? -12.620 0.112   35.203  1.00 37.32 ? 257 LYS A CD  1 
ATOM   2025 C  CE  . LYS A 1 256 ? -12.372 1.134   36.356  1.00 44.63 ? 257 LYS A CE  1 
ATOM   2026 N  NZ  . LYS A 1 256 ? -13.673 1.845   36.789  1.00 46.51 ? 257 LYS A NZ  1 
ATOM   2027 N  N   . ALA A 1 257 ? -16.186 -3.747  33.492  1.00 24.99 ? 258 ALA A N   1 
ATOM   2028 C  CA  . ALA A 1 257 ? -17.166 -4.340  32.632  1.00 24.80 ? 258 ALA A CA  1 
ATOM   2029 C  C   . ALA A 1 257 ? -18.431 -3.571  32.846  1.00 25.77 ? 258 ALA A C   1 
ATOM   2030 O  O   . ALA A 1 257 ? -18.718 -3.117  33.980  1.00 25.26 ? 258 ALA A O   1 
ATOM   2031 C  CB  . ALA A 1 257 ? -17.399 -5.819  32.976  1.00 24.99 ? 258 ALA A CB  1 
ATOM   2032 N  N   . SER A 1 258 ? -19.201 -3.466  31.769  1.00 27.03 ? 259 SER A N   1 
ATOM   2033 C  CA  . SER A 1 258 ? -20.507 -2.782  31.795  1.00 27.71 ? 259 SER A CA  1 
ATOM   2034 C  C   . SER A 1 258 ? -21.583 -3.746  32.224  1.00 28.89 ? 259 SER A C   1 
ATOM   2035 O  O   . SER A 1 258 ? -22.720 -3.341  32.398  1.00 28.76 ? 259 SER A O   1 
ATOM   2036 C  CB  . SER A 1 258 ? -20.879 -2.227  30.422  1.00 25.91 ? 259 SER A CB  1 
ATOM   2037 O  OG  . SER A 1 258 ? -21.220 -3.248  29.527  1.00 26.41 ? 259 SER A OG  1 
ATOM   2038 N  N   . PHE A 1 259 ? -21.218 -5.013  32.409  1.00 30.41 ? 260 PHE A N   1 
ATOM   2039 C  CA  . PHE A 1 259 ? -22.172 -6.116  32.552  1.00 31.40 ? 260 PHE A CA  1 
ATOM   2040 C  C   . PHE A 1 259 ? -21.715 -7.163  33.566  1.00 35.34 ? 260 PHE A C   1 
ATOM   2041 O  O   . PHE A 1 259 ? -20.514 -7.267  33.941  1.00 32.92 ? 260 PHE A O   1 
ATOM   2042 C  CB  . PHE A 1 259 ? -22.398 -6.812  31.207  1.00 31.24 ? 260 PHE A CB  1 
ATOM   2043 C  CG  . PHE A 1 259 ? -21.176 -7.545  30.701  1.00 29.86 ? 260 PHE A CG  1 
ATOM   2044 C  CD1 . PHE A 1 259 ? -20.117 -6.852  30.117  1.00 31.29 ? 260 PHE A CD1 1 
ATOM   2045 C  CD2 . PHE A 1 259 ? -21.047 -8.905  30.909  1.00 29.00 ? 260 PHE A CD2 1 
ATOM   2046 C  CE1 . PHE A 1 259 ? -18.951 -7.524  29.700  1.00 31.43 ? 260 PHE A CE1 1 
ATOM   2047 C  CE2 . PHE A 1 259 ? -19.923 -9.564  30.511  1.00 33.29 ? 260 PHE A CE2 1 
ATOM   2048 C  CZ  . PHE A 1 259 ? -18.859 -8.862  29.874  1.00 32.55 ? 260 PHE A CZ  1 
ATOM   2049 N  N   . LYS A 1 260 ? -22.754 -7.882  34.005  1.00 39.21 ? 261 LYS A N   1 
ATOM   2050 C  CA  . LYS A 1 260 ? -22.795 -9.092  34.843  1.00 44.63 ? 261 LYS A CA  1 
ATOM   2051 C  C   . LYS A 1 260 ? -22.101 -9.082  36.181  1.00 46.22 ? 261 LYS A C   1 
ATOM   2052 O  O   . LYS A 1 260 ? -22.760 -9.152  37.243  1.00 48.25 ? 261 LYS A O   1 
ATOM   2053 C  CB  . LYS A 1 260 ? -22.585 -10.370 34.028  1.00 43.52 ? 261 LYS A CB  1 
ATOM   2054 C  CG  . LYS A 1 260 ? -23.800 -10.611 33.101  1.00 46.41 ? 261 LYS A CG  1 
ATOM   2055 C  CD  . LYS A 1 260 ? -23.948 -12.076 32.601  1.00 47.92 ? 261 LYS A CD  1 
ATOM   2056 C  CE  . LYS A 1 260 ? -25.451 -12.478 32.446  1.00 51.60 ? 261 LYS A CE  1 
ATOM   2057 N  NZ  . LYS A 1 260 ? -25.861 -13.773 33.154  1.00 51.57 ? 261 LYS A NZ  1 
ATOM   2058 O  OXT . LYS A 1 260 ? -20.874 -8.929  36.244  1.00 49.27 ? 261 LYS A OXT 1 
HETATM 2059 ZN ZN  . ZN  B 2 .   ? -6.429  -1.682  15.121  1.00 16.32 ? 262 ZN  A ZN  1 
HETATM 2060 S  S   . DMS C 3 .   ? 1.660   -11.694 14.776  1.00 38.42 ? 263 DMS A S   1 
HETATM 2061 O  O   . DMS C 3 .   ? 2.792   -10.586 13.892  1.00 39.16 ? 263 DMS A O   1 
HETATM 2062 C  C1  . DMS C 3 .   ? 2.312   -13.342 14.471  1.00 36.04 ? 263 DMS A C1  1 
HETATM 2063 C  C2  . DMS C 3 .   ? 1.967   -11.588 16.548  1.00 35.01 ? 263 DMS A C2  1 
HETATM 2064 S  S   . DMS D 3 .   ? -4.060  0.666   10.676  1.00 66.50 ? 264 DMS A S   1 
HETATM 2065 O  O   . DMS D 3 .   ? -4.057  -0.490  12.046  1.00 65.46 ? 264 DMS A O   1 
HETATM 2066 C  C1  . DMS D 3 .   ? -4.684  2.257   11.268  1.00 64.42 ? 264 DMS A C1  1 
HETATM 2067 C  C2  . DMS D 3 .   ? -2.319  1.081   10.342  1.00 65.11 ? 264 DMS A C2  1 
HETATM 2068 N  N1  . J71 E 4 .   ? -3.301  9.857   11.059  1.00 42.90 ? 265 J71 A N1  1 
HETATM 2069 C  C2  . J71 E 4 .   ? -2.437  9.148   11.818  1.00 45.54 ? 265 J71 A C2  1 
HETATM 2070 N  N3  . J71 E 4 .   ? -2.759  7.936   12.313  1.00 47.90 ? 265 J71 A N3  1 
HETATM 2071 C  C4  . J71 E 4 .   ? -3.975  7.392   12.033  1.00 47.15 ? 265 J71 A C4  1 
HETATM 2072 C  C5  . J71 E 4 .   ? -4.908  8.106   11.201  1.00 47.49 ? 265 J71 A C5  1 
HETATM 2073 C  C6  . J71 E 4 .   ? -4.527  9.411   10.698  1.00 45.44 ? 265 J71 A C6  1 
HETATM 2074 N  N7  . J71 E 4 .   ? -4.288  6.113   12.570  1.00 41.45 ? 265 J71 A N7  1 
HETATM 2075 C  C8  . J71 E 4 .   ? -4.082  4.329   14.215  1.00 25.13 ? 265 J71 A C8  1 
HETATM 2076 C  C9  . J71 E 4 .   ? -5.445  4.327   14.596  1.00 18.30 ? 265 J71 A C9  1 
HETATM 2077 C  C10 . J71 E 4 .   ? -5.895  3.215   15.396  1.00 14.72 ? 265 J71 A C10 1 
HETATM 2078 C  C11 . J71 E 4 .   ? -5.013  2.135   15.674  1.00 18.86 ? 265 J71 A C11 1 
HETATM 2079 C  C12 . J71 E 4 .   ? -3.674  2.164   15.304  1.00 18.80 ? 265 J71 A C12 1 
HETATM 2080 C  C13 . J71 E 4 .   ? -3.229  3.251   14.537  1.00 23.20 ? 265 J71 A C13 1 
HETATM 2081 S  S14 . J71 E 4 .   ? -5.634  0.851   16.648  1.00 16.54 ? 265 J71 A S14 1 
HETATM 2082 O  O15 . J71 E 4 .   ? -5.120  0.910   17.966  1.00 15.46 ? 265 J71 A O15 1 
HETATM 2083 O  O16 . J71 E 4 .   ? -7.090  0.859   16.460  1.00 16.24 ? 265 J71 A O16 1 
HETATM 2084 N  N17 . J71 E 4 .   ? -4.920  -0.492  15.945  1.00 17.23 ? 265 J71 A N17 1 
HETATM 2085 N  N18 . J71 E 4 .   ? -6.219  7.391   10.946  1.00 46.90 ? 265 J71 A N18 1 
HETATM 2086 O  O19 . J71 E 4 .   ? -6.274  6.399   10.325  1.00 53.11 ? 265 J71 A O19 1 
HETATM 2087 O  O20 . J71 E 4 .   ? -7.377  7.866   11.383  1.00 52.25 ? 265 J71 A O20 1 
HETATM 2088 O  O21 . J71 E 4 .   ? -5.276  10.385  9.814   1.00 47.46 ? 265 J71 A O21 1 
HETATM 2089 C  C22 . J71 E 4 .   ? -5.704  11.698  10.190  1.00 48.46 ? 265 J71 A C22 1 
HETATM 2090 C  C23 . J71 E 4 .   ? -3.392  5.404   13.393  1.00 34.98 ? 265 J71 A C23 1 
HETATM 2091 O  O   . HOH F 5 .   ? -1.171  -4.179  15.465  1.00 16.57 ? 266 HOH A O   1 
HETATM 2092 O  O   . HOH F 5 .   ? -4.327  -13.428 17.705  1.00 13.02 ? 267 HOH A O   1 
HETATM 2093 O  O   . HOH F 5 .   ? -21.333 -7.168  23.364  1.00 19.91 ? 268 HOH A O   1 
HETATM 2094 O  O   . HOH F 5 .   ? -17.749 -20.340 7.941   1.00 19.72 ? 269 HOH A O   1 
HETATM 2095 O  O   . HOH F 5 .   ? 4.993   -4.989  20.781  1.00 20.35 ? 270 HOH A O   1 
HETATM 2096 O  O   . HOH F 5 .   ? -7.640  -15.345 11.048  1.00 13.64 ? 271 HOH A O   1 
HETATM 2097 O  O   . HOH F 5 .   ? -16.711 -8.404  20.308  1.00 17.53 ? 272 HOH A O   1 
HETATM 2098 O  O   . HOH F 5 .   ? -3.126  -13.202 24.938  1.00 19.64 ? 273 HOH A O   1 
HETATM 2099 O  O   . HOH F 5 .   ? -21.552 5.636   4.694   1.00 20.10 ? 274 HOH A O   1 
HETATM 2100 O  O   . HOH F 5 .   ? -1.774  -12.306 22.694  1.00 23.33 ? 275 HOH A O   1 
HETATM 2101 O  O   . HOH F 5 .   ? 1.346   -1.689  29.175  1.00 26.91 ? 276 HOH A O   1 
HETATM 2102 O  O   . HOH F 5 .   ? 3.641   4.889   29.635  1.00 27.19 ? 277 HOH A O   1 
HETATM 2103 O  O   . HOH F 5 .   ? -2.460  -8.819  28.841  1.00 20.51 ? 278 HOH A O   1 
HETATM 2104 O  O   . HOH F 5 .   ? -10.459 8.638   25.450  1.00 19.76 ? 279 HOH A O   1 
HETATM 2105 O  O   . HOH F 5 .   ? 8.665   -3.846  20.886  1.00 28.23 ? 280 HOH A O   1 
HETATM 2106 O  O   . HOH F 5 .   ? -3.473  -15.875 24.173  1.00 21.92 ? 281 HOH A O   1 
HETATM 2107 O  O   . HOH F 5 .   ? 5.592   7.043   19.967  1.00 26.10 ? 282 HOH A O   1 
HETATM 2108 O  O   . HOH F 5 .   ? -16.270 -9.876  32.776  1.00 26.15 ? 283 HOH A O   1 
HETATM 2109 O  O   . HOH F 5 .   ? -17.689 10.387  11.203  1.00 26.59 ? 284 HOH A O   1 
HETATM 2110 O  O   . HOH F 5 .   ? -13.912 10.533  27.622  1.00 28.77 ? 285 HOH A O   1 
HETATM 2111 O  O   . HOH F 5 .   ? -3.250  -11.127 20.573  1.00 23.29 ? 286 HOH A O   1 
HETATM 2112 O  O   . HOH F 5 .   ? -19.116 10.021  8.789   1.00 22.16 ? 287 HOH A O   1 
HETATM 2113 O  O   . HOH F 5 .   ? -10.382 -18.193 16.729  1.00 30.22 ? 288 HOH A O   1 
HETATM 2114 O  O   . HOH F 5 .   ? 7.786   6.252   21.461  1.00 27.47 ? 289 HOH A O   1 
HETATM 2115 O  O   . HOH F 5 .   ? -20.726 7.715   1.741   1.00 27.73 ? 290 HOH A O   1 
HETATM 2116 O  O   . HOH F 5 .   ? 4.641   -3.400  26.083  1.00 27.39 ? 291 HOH A O   1 
HETATM 2117 O  O   . HOH F 5 .   ? 11.357  1.423   25.656  1.00 28.36 ? 292 HOH A O   1 
HETATM 2118 O  O   . HOH F 5 .   ? -20.034 10.731  26.513  1.00 29.21 ? 293 HOH A O   1 
HETATM 2119 O  O   . HOH F 5 .   ? -2.852  7.472   -5.009  1.00 29.87 ? 294 HOH A O   1 
HETATM 2120 O  O   . HOH F 5 .   ? 1.534   -11.909 24.884  1.00 29.65 ? 295 HOH A O   1 
HETATM 2121 O  O   . HOH F 5 .   ? 1.554   8.604   24.223  1.00 27.54 ? 296 HOH A O   1 
HETATM 2122 O  O   . HOH F 5 .   ? -11.737 3.146   30.646  1.00 27.74 ? 297 HOH A O   1 
HETATM 2123 O  O   . HOH F 5 .   ? -13.163 -18.533 14.831  1.00 25.82 ? 298 HOH A O   1 
HETATM 2124 O  O   . HOH F 5 .   ? -1.382  -13.151 27.082  1.00 36.56 ? 299 HOH A O   1 
HETATM 2125 O  O   . HOH F 5 .   ? -25.314 9.655   13.447  1.00 37.83 ? 300 HOH A O   1 
HETATM 2126 O  O   . HOH F 5 .   ? -22.768 -11.637 13.995  1.00 30.86 ? 301 HOH A O   1 
HETATM 2127 O  O   . HOH F 5 .   ? -5.558  -4.353  -6.453  1.00 33.64 ? 302 HOH A O   1 
HETATM 2128 O  O   . HOH F 5 .   ? 13.418  0.372   24.078  1.00 34.01 ? 303 HOH A O   1 
HETATM 2129 O  O   . HOH F 5 .   ? -26.353 -2.477  14.235  1.00 25.98 ? 304 HOH A O   1 
HETATM 2130 O  O   . HOH F 5 .   ? 5.117   -7.411  22.224  1.00 39.85 ? 305 HOH A O   1 
HETATM 2131 O  O   . HOH F 5 .   ? -24.406 -7.713  8.922   1.00 25.16 ? 306 HOH A O   1 
HETATM 2132 O  O   . HOH F 5 .   ? -22.567 -14.216 11.079  1.00 34.34 ? 307 HOH A O   1 
HETATM 2133 O  O   . HOH F 5 .   ? -26.324 -11.303 2.084   1.00 27.93 ? 308 HOH A O   1 
HETATM 2134 O  O   . HOH F 5 .   ? -4.360  -11.767 31.863  1.00 34.74 ? 309 HOH A O   1 
HETATM 2135 O  O   . HOH F 5 .   ? -15.837 -12.519 24.091  1.00 25.36 ? 310 HOH A O   1 
HETATM 2136 O  O   . HOH F 5 .   ? 2.780   -11.370 9.751   1.00 27.89 ? 311 HOH A O   1 
HETATM 2137 O  O   . HOH F 5 .   ? -23.671 -0.735  26.309  1.00 29.46 ? 312 HOH A O   1 
HETATM 2138 O  O   . HOH F 5 .   ? -7.907  -19.092 21.446  1.00 29.77 ? 313 HOH A O   1 
HETATM 2139 O  O   . HOH F 5 .   ? -2.057  -3.126  11.248  1.00 30.52 ? 314 HOH A O   1 
HETATM 2140 O  O   . HOH F 5 .   ? 4.701   -6.587  7.931   1.00 33.81 ? 315 HOH A O   1 
HETATM 2141 O  O   . HOH F 5 .   ? -22.805 -2.912  6.413   1.00 29.04 ? 316 HOH A O   1 
HETATM 2142 O  O   . HOH F 5 .   ? -3.351  -12.978 -3.031  1.00 35.42 ? 317 HOH A O   1 
HETATM 2143 O  O   . HOH F 5 .   ? -8.857  -6.014  35.548  1.00 28.74 ? 318 HOH A O   1 
HETATM 2144 O  O   . HOH F 5 .   ? -18.283 -9.122  34.293  1.00 39.61 ? 319 HOH A O   1 
HETATM 2145 O  O   . HOH F 5 .   ? -24.460 -9.208  1.895   1.00 35.47 ? 320 HOH A O   1 
HETATM 2146 O  O   . HOH F 5 .   ? -25.537 6.398   26.908  1.00 33.12 ? 321 HOH A O   1 
HETATM 2147 O  O   . HOH F 5 .   ? -26.567 -4.001  25.009  1.00 30.73 ? 322 HOH A O   1 
HETATM 2148 O  O   . HOH F 5 .   ? -7.976  -22.130 10.313  1.00 30.01 ? 323 HOH A O   1 
HETATM 2149 O  O   . HOH F 5 .   ? -19.482 -16.896 3.016   1.00 35.83 ? 324 HOH A O   1 
HETATM 2150 O  O   . HOH F 5 .   ? -23.369 -0.992  3.962   1.00 24.31 ? 325 HOH A O   1 
HETATM 2151 O  O   . HOH F 5 .   ? -22.326 -5.718  2.757   1.00 33.24 ? 326 HOH A O   1 
HETATM 2152 O  O   . HOH F 5 .   ? -15.703 15.858  23.489  1.00 35.76 ? 327 HOH A O   1 
HETATM 2153 O  O   . HOH F 5 .   ? -21.740 -18.250 13.665  1.00 31.20 ? 328 HOH A O   1 
HETATM 2154 O  O   . HOH F 5 .   ? -25.516 -15.089 8.107   1.00 26.18 ? 329 HOH A O   1 
HETATM 2155 O  O   . HOH F 5 .   ? -18.564 -12.210 -3.246  1.00 37.87 ? 330 HOH A O   1 
HETATM 2156 O  O   . HOH F 5 .   ? -24.465 12.028  6.291   1.00 35.18 ? 331 HOH A O   1 
HETATM 2157 O  O   . HOH F 5 .   ? -26.064 3.869   15.418  1.00 39.64 ? 332 HOH A O   1 
HETATM 2158 O  O   . HOH F 5 .   ? -6.778  -14.962 31.405  1.00 34.15 ? 333 HOH A O   1 
HETATM 2159 O  O   . HOH F 5 .   ? 0.213   -14.326 21.930  1.00 41.94 ? 334 HOH A O   1 
HETATM 2160 O  O   . HOH F 5 .   ? -17.908 3.587   -3.902  1.00 29.91 ? 335 HOH A O   1 
HETATM 2161 O  O   . HOH F 5 .   ? -28.444 -5.944  24.556  1.00 35.02 ? 336 HOH A O   1 
HETATM 2162 O  O   . HOH F 5 .   ? 8.456   2.977   27.419  1.00 41.87 ? 337 HOH A O   1 
HETATM 2163 O  O   . HOH F 5 .   ? -0.806  -17.678 17.970  1.00 46.29 ? 338 HOH A O   1 
HETATM 2164 O  O   . HOH F 5 .   ? -12.426 9.602   29.073  1.00 45.27 ? 339 HOH A O   1 
HETATM 2165 O  O   . HOH F 5 .   ? -17.182 -16.478 21.416  1.00 43.88 ? 340 HOH A O   1 
HETATM 2166 O  O   . HOH F 5 .   ? -8.201  0.643   -6.561  1.00 35.23 ? 341 HOH A O   1 
HETATM 2167 O  O   . HOH F 5 .   ? -5.027  3.326   -5.916  1.00 40.18 ? 342 HOH A O   1 
HETATM 2168 O  O   . HOH F 5 .   ? -2.684  -17.681 5.113   1.00 34.84 ? 343 HOH A O   1 
HETATM 2169 O  O   . HOH F 5 .   ? -15.197 -10.110 36.780  1.00 37.50 ? 344 HOH A O   1 
HETATM 2170 O  O   . HOH F 5 .   ? 3.517   -14.640 2.200   1.00 34.79 ? 345 HOH A O   1 
HETATM 2171 O  O   . HOH F 5 .   ? -26.640 3.336   20.820  1.00 38.43 ? 346 HOH A O   1 
HETATM 2172 O  O   . HOH F 5 .   ? -19.131 -20.463 5.087   1.00 29.83 ? 347 HOH A O   1 
HETATM 2173 O  O   . HOH F 5 .   ? 2.172   -15.411 9.282   1.00 29.89 ? 348 HOH A O   1 
HETATM 2174 O  O   . HOH F 5 .   ? -9.965  -5.936  38.009  1.00 41.88 ? 349 HOH A O   1 
HETATM 2175 O  O   . HOH F 5 .   ? 8.831   -4.650  23.465  1.00 37.30 ? 350 HOH A O   1 
HETATM 2176 O  O   . HOH F 5 .   ? -11.071 -19.206 6.539   1.00 34.73 ? 351 HOH A O   1 
HETATM 2177 O  O   . HOH F 5 .   ? -16.909 -13.878 36.868  1.00 32.98 ? 352 HOH A O   1 
HETATM 2178 O  O   . HOH F 5 .   ? 7.973   -5.890  -10.829 1.00 41.25 ? 353 HOH A O   1 
HETATM 2179 O  O   . HOH F 5 .   ? -3.670  -18.630 1.658   1.00 45.00 ? 354 HOH A O   1 
HETATM 2180 O  O   . HOH F 5 .   ? -0.950  -11.146 28.921  1.00 33.47 ? 355 HOH A O   1 
HETATM 2181 O  O   . HOH F 5 .   ? -0.172  10.881  22.938  1.00 35.33 ? 356 HOH A O   1 
HETATM 2182 O  O   . HOH F 5 .   ? -1.948  -4.592  -7.093  1.00 45.36 ? 357 HOH A O   1 
HETATM 2183 O  O   . HOH F 5 .   ? -8.769  9.725   7.323   1.00 46.19 ? 358 HOH A O   1 
HETATM 2184 O  O   . HOH F 5 .   ? -20.101 -16.117 21.582  1.00 46.69 ? 359 HOH A O   1 
HETATM 2185 O  O   . HOH F 5 .   ? -5.901  -19.883 23.742  1.00 43.17 ? 360 HOH A O   1 
HETATM 2186 O  O   . HOH F 5 .   ? 3.075   -4.130  7.980   1.00 39.43 ? 361 HOH A O   1 
HETATM 2187 O  O   . HOH F 5 .   ? -8.548  -3.814  7.786   1.00 33.33 ? 362 HOH A O   1 
HETATM 2188 O  O   . HOH F 5 .   ? -17.573 18.933  5.954   1.00 21.63 ? 363 HOH A O   1 
HETATM 2189 O  O   . HOH F 5 .   ? 11.003  -4.801  -7.948  1.00 37.47 ? 364 HOH A O   1 
HETATM 2190 O  O   . HOH F 5 .   ? -13.008 -22.166 11.811  1.00 33.24 ? 365 HOH A O   1 
HETATM 2191 O  O   . HOH F 5 .   ? -8.985  -9.890  -1.639  1.00 37.13 ? 366 HOH A O   1 
HETATM 2192 O  O   . HOH F 5 .   ? -9.411  -8.078  33.815  1.00 39.38 ? 367 HOH A O   1 
HETATM 2193 O  O   . HOH F 5 .   ? -13.783 -21.093 3.166   1.00 45.28 ? 368 HOH A O   1 
HETATM 2194 O  O   . HOH F 5 .   ? -25.616 -6.142  12.793  1.00 41.48 ? 369 HOH A O   1 
HETATM 2195 O  O   . HOH F 5 .   ? -13.364 -17.937 18.220  1.00 48.62 ? 370 HOH A O   1 
HETATM 2196 O  O   . HOH F 5 .   ? -0.983  -8.585  32.462  1.00 36.67 ? 371 HOH A O   1 
HETATM 2197 O  O   . HOH F 5 .   ? 2.345   8.044   27.367  1.00 36.47 ? 372 HOH A O   1 
HETATM 2198 O  O   . HOH F 5 .   ? -18.481 11.808  12.805  1.00 32.83 ? 373 HOH A O   1 
HETATM 2199 O  O   . HOH F 5 .   ? 10.217  -2.208  13.644  1.00 41.79 ? 374 HOH A O   1 
HETATM 2200 O  O   . HOH F 5 .   ? -20.999 18.723  13.729  1.00 32.15 ? 375 HOH A O   1 
HETATM 2201 O  O   . HOH F 5 .   ? -6.418  -19.359 5.030   1.00 43.82 ? 376 HOH A O   1 
HETATM 2202 O  O   . HOH F 5 .   ? -7.265  1.384   35.680  1.00 46.68 ? 377 HOH A O   1 
HETATM 2203 O  O   . HOH F 5 .   ? 9.712   -6.987  -9.173  1.00 43.29 ? 378 HOH A O   1 
HETATM 2204 O  O   . HOH F 5 .   ? -17.703 -12.322 31.424  1.00 34.58 ? 379 HOH A O   1 
HETATM 2205 O  O   . HOH F 5 .   ? -24.820 9.452   26.178  1.00 43.00 ? 380 HOH A O   1 
HETATM 2206 O  O   . HOH F 5 .   ? 5.686   -10.384 17.410  1.00 42.96 ? 381 HOH A O   1 
HETATM 2207 O  O   . HOH F 5 .   ? -2.225  4.538   -5.693  1.00 48.81 ? 382 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 DMS 1   263 1   DMS DMS A . 
D 3 DMS 1   264 2   DMS DMS A . 
E 4 J71 1   265 1   J71 J71 A . 
F 5 HOH 1   266 1   HOH HOH A . 
F 5 HOH 2   267 2   HOH HOH A . 
F 5 HOH 3   268 3   HOH HOH A . 
F 5 HOH 4   269 4   HOH HOH A . 
F 5 HOH 5   270 5   HOH HOH A . 
F 5 HOH 6   271 6   HOH HOH A . 
F 5 HOH 7   272 7   HOH HOH A . 
F 5 HOH 8   273 8   HOH HOH A . 
F 5 HOH 9   274 9   HOH HOH A . 
F 5 HOH 10  275 10  HOH HOH A . 
F 5 HOH 11  276 11  HOH HOH A . 
F 5 HOH 12  277 12  HOH HOH A . 
F 5 HOH 13  278 13  HOH HOH A . 
F 5 HOH 14  279 14  HOH HOH A . 
F 5 HOH 15  280 15  HOH HOH A . 
F 5 HOH 16  281 16  HOH HOH A . 
F 5 HOH 17  282 17  HOH HOH A . 
F 5 HOH 18  283 18  HOH HOH A . 
F 5 HOH 19  284 19  HOH HOH A . 
F 5 HOH 20  285 20  HOH HOH A . 
F 5 HOH 21  286 21  HOH HOH A . 
F 5 HOH 22  287 22  HOH HOH A . 
F 5 HOH 23  288 23  HOH HOH A . 
F 5 HOH 24  289 24  HOH HOH A . 
F 5 HOH 25  290 25  HOH HOH A . 
F 5 HOH 26  291 26  HOH HOH A . 
F 5 HOH 27  292 27  HOH HOH A . 
F 5 HOH 28  293 28  HOH HOH A . 
F 5 HOH 29  294 29  HOH HOH A . 
F 5 HOH 30  295 30  HOH HOH A . 
F 5 HOH 31  296 31  HOH HOH A . 
F 5 HOH 32  297 32  HOH HOH A . 
F 5 HOH 33  298 33  HOH HOH A . 
F 5 HOH 34  299 34  HOH HOH A . 
F 5 HOH 35  300 35  HOH HOH A . 
F 5 HOH 36  301 36  HOH HOH A . 
F 5 HOH 37  302 37  HOH HOH A . 
F 5 HOH 38  303 38  HOH HOH A . 
F 5 HOH 39  304 39  HOH HOH A . 
F 5 HOH 40  305 40  HOH HOH A . 
F 5 HOH 41  306 41  HOH HOH A . 
F 5 HOH 42  307 42  HOH HOH A . 
F 5 HOH 43  308 43  HOH HOH A . 
F 5 HOH 44  309 44  HOH HOH A . 
F 5 HOH 45  310 45  HOH HOH A . 
F 5 HOH 46  311 46  HOH HOH A . 
F 5 HOH 47  312 47  HOH HOH A . 
F 5 HOH 48  313 48  HOH HOH A . 
F 5 HOH 49  314 49  HOH HOH A . 
F 5 HOH 50  315 50  HOH HOH A . 
F 5 HOH 51  316 51  HOH HOH A . 
F 5 HOH 52  317 52  HOH HOH A . 
F 5 HOH 53  318 53  HOH HOH A . 
F 5 HOH 54  319 54  HOH HOH A . 
F 5 HOH 55  320 55  HOH HOH A . 
F 5 HOH 56  321 56  HOH HOH A . 
F 5 HOH 57  322 57  HOH HOH A . 
F 5 HOH 58  323 58  HOH HOH A . 
F 5 HOH 59  324 59  HOH HOH A . 
F 5 HOH 60  325 60  HOH HOH A . 
F 5 HOH 61  326 61  HOH HOH A . 
F 5 HOH 62  327 62  HOH HOH A . 
F 5 HOH 63  328 63  HOH HOH A . 
F 5 HOH 64  329 64  HOH HOH A . 
F 5 HOH 65  330 65  HOH HOH A . 
F 5 HOH 66  331 66  HOH HOH A . 
F 5 HOH 67  332 67  HOH HOH A . 
F 5 HOH 68  333 68  HOH HOH A . 
F 5 HOH 69  334 69  HOH HOH A . 
F 5 HOH 70  335 70  HOH HOH A . 
F 5 HOH 71  336 71  HOH HOH A . 
F 5 HOH 72  337 72  HOH HOH A . 
F 5 HOH 73  338 73  HOH HOH A . 
F 5 HOH 74  339 74  HOH HOH A . 
F 5 HOH 75  340 75  HOH HOH A . 
F 5 HOH 76  341 76  HOH HOH A . 
F 5 HOH 77  342 77  HOH HOH A . 
F 5 HOH 78  343 78  HOH HOH A . 
F 5 HOH 79  344 79  HOH HOH A . 
F 5 HOH 80  345 80  HOH HOH A . 
F 5 HOH 81  346 81  HOH HOH A . 
F 5 HOH 82  347 82  HOH HOH A . 
F 5 HOH 83  348 83  HOH HOH A . 
F 5 HOH 84  349 84  HOH HOH A . 
F 5 HOH 85  350 85  HOH HOH A . 
F 5 HOH 86  351 86  HOH HOH A . 
F 5 HOH 87  352 87  HOH HOH A . 
F 5 HOH 88  353 88  HOH HOH A . 
F 5 HOH 89  354 89  HOH HOH A . 
F 5 HOH 90  355 90  HOH HOH A . 
F 5 HOH 91  356 91  HOH HOH A . 
F 5 HOH 92  357 92  HOH HOH A . 
F 5 HOH 93  358 93  HOH HOH A . 
F 5 HOH 94  359 94  HOH HOH A . 
F 5 HOH 95  360 95  HOH HOH A . 
F 5 HOH 96  361 96  HOH HOH A . 
F 5 HOH 97  362 97  HOH HOH A . 
F 5 HOH 98  363 98  HOH HOH A . 
F 5 HOH 99  364 99  HOH HOH A . 
F 5 HOH 100 365 100 HOH HOH A . 
F 5 HOH 101 366 101 HOH HOH A . 
F 5 HOH 102 367 102 HOH HOH A . 
F 5 HOH 103 368 103 HOH HOH A . 
F 5 HOH 104 369 104 HOH HOH A . 
F 5 HOH 105 370 105 HOH HOH A . 
F 5 HOH 106 371 106 HOH HOH A . 
F 5 HOH 107 372 107 HOH HOH A . 
F 5 HOH 108 373 108 HOH HOH A . 
F 5 HOH 109 374 109 HOH HOH A . 
F 5 HOH 110 375 110 HOH HOH A . 
F 5 HOH 111 376 111 HOH HOH A . 
F 5 HOH 112 377 112 HOH HOH A . 
F 5 HOH 113 378 113 HOH HOH A . 
F 5 HOH 114 379 114 HOH HOH A . 
F 5 HOH 115 380 115 HOH HOH A . 
F 5 HOH 116 381 116 HOH HOH A . 
F 5 HOH 117 382 117 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_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' Advisory                    
3 3 'Structure model' 'Refinement description'    
4 4 'Structure model' Advisory                    
5 4 'Structure model' 'Data collection'           
6 4 'Structure model' 'Database references'       
7 4 'Structure model' 'Derived calculations'      
8 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' pdbx_unobs_or_zero_occ_atoms  
2 3 'Structure model' software                      
3 4 'Structure model' chem_comp_atom                
4 4 'Structure model' chem_comp_bond                
5 4 'Structure model' database_2                    
6 4 'Structure model' diffrn_source                 
7 4 'Structure model' pdbx_initial_refinement_model 
8 4 'Structure model' pdbx_unobs_or_zero_occ_atoms  
9 4 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_software.name'                       
2 4 'Structure model' '_database_2.pdbx_DOI'                 
3 4 'Structure model' '_database_2.pdbx_database_accession'  
4 4 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
5 4 'Structure model' '_struct_site.pdbx_auth_asym_id'       
6 4 'Structure model' '_struct_site.pdbx_auth_comp_id'       
7 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 
MAR345      'v. 0.10.22 on RedHat Linux 8' ?               ?       ?                    ?                        'data collection' 
?                                            ?          ? 5 
O           .                              ?               ?       ?                    ?                        'model building'  
?                                            ?          ? 6 
# 
_pdbx_entry_details.entry_id                 3MHL 
_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_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH1 A ARG 27  ? ? 124.96 120.30 4.66  0.50 N 
2 1 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH2 A ARG 27  ? ? 117.16 120.30 -3.14 0.50 N 
3 1 CB A ASP 101 ? ? CG A ASP 101 ? ? OD1 A ASP 101 ? ? 123.90 118.30 5.60  0.90 N 
4 1 CB A ASN 253 ? ? CG A ASN 253 ? ? OD1 A ASN 253 ? ? 133.79 121.60 12.19 2.00 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 111 ? ? 71.39   -4.49   
2 1 PHE A 176 ? ? -156.10 74.21   
3 1 ASN A 244 ? ? -94.56  49.10   
4 1 LYS A 252 ? ? 53.12   -137.23 
5 1 ASN A 253 ? ? -102.22 72.65   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    86 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   THR 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    87 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.22 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 0 A LYS 9   ? CD  ? A LYS 9   CD  
2 1 Y 0 A LYS 9   ? CE  ? A LYS 9   CE  
3 1 Y 0 A LYS 9   ? NZ  ? A LYS 9   NZ  
4 1 Y 0 A ASP 85  ? CG  ? A ASP 85  CG  
5 1 Y 0 A ASP 85  ? OD1 ? A ASP 85  OD1 
6 1 Y 0 A ASP 85  ? OD2 ? A ASP 85  OD2 
7 1 Y 0 A ASN 253 ? CG  ? A ASN 252 CG  
8 1 Y 0 A ASN 253 ? OD1 ? A ASN 252 OD1 
9 1 Y 0 A ASN 253 ? ND2 ? A ASN 252 ND2 
# 
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 
J71 N1   N  Y N 193 
J71 C2   C  Y N 194 
J71 N3   N  Y N 195 
J71 C4   C  Y N 196 
J71 C5   C  Y N 197 
J71 C6   C  Y N 198 
J71 N7   N  N N 199 
J71 C8   C  Y N 200 
J71 C9   C  Y N 201 
J71 C10  C  Y N 202 
J71 C11  C  Y N 203 
J71 C12  C  Y N 204 
J71 C13  C  Y N 205 
J71 S14  S  N N 206 
J71 O15  O  N N 207 
J71 O16  O  N N 208 
J71 N17  N  N N 209 
J71 N18  N  N N 210 
J71 O19  O  N N 211 
J71 O20  O  N N 212 
J71 O21  O  N N 213 
J71 C22  C  N N 214 
J71 C23  C  N N 215 
J71 H2   H  N N 216 
J71 HN7  H  N N 217 
J71 H9   H  N N 218 
J71 H10  H  N N 219 
J71 H12  H  N N 220 
J71 H13  H  N N 221 
J71 HN17 H  N N 222 
J71 HN1A H  N N 223 
J71 H22  H  N N 224 
J71 H22A H  N N 225 
J71 H22B H  N N 226 
J71 H23  H  N N 227 
J71 H23A H  N N 228 
LEU N    N  N N 229 
LEU CA   C  N S 230 
LEU C    C  N N 231 
LEU O    O  N N 232 
LEU CB   C  N N 233 
LEU CG   C  N N 234 
LEU CD1  C  N N 235 
LEU CD2  C  N N 236 
LEU OXT  O  N N 237 
LEU H    H  N N 238 
LEU H2   H  N N 239 
LEU HA   H  N N 240 
LEU HB2  H  N N 241 
LEU HB3  H  N N 242 
LEU HG   H  N N 243 
LEU HD11 H  N N 244 
LEU HD12 H  N N 245 
LEU HD13 H  N N 246 
LEU HD21 H  N N 247 
LEU HD22 H  N N 248 
LEU HD23 H  N N 249 
LEU HXT  H  N N 250 
LYS N    N  N N 251 
LYS CA   C  N S 252 
LYS C    C  N N 253 
LYS O    O  N N 254 
LYS CB   C  N N 255 
LYS CG   C  N N 256 
LYS CD   C  N N 257 
LYS CE   C  N N 258 
LYS NZ   N  N N 259 
LYS OXT  O  N N 260 
LYS H    H  N N 261 
LYS H2   H  N N 262 
LYS HA   H  N N 263 
LYS HB2  H  N N 264 
LYS HB3  H  N N 265 
LYS HG2  H  N N 266 
LYS HG3  H  N N 267 
LYS HD2  H  N N 268 
LYS HD3  H  N N 269 
LYS HE2  H  N N 270 
LYS HE3  H  N N 271 
LYS HZ1  H  N N 272 
LYS HZ2  H  N N 273 
LYS HZ3  H  N N 274 
LYS HXT  H  N N 275 
MET N    N  N N 276 
MET CA   C  N S 277 
MET C    C  N N 278 
MET O    O  N N 279 
MET CB   C  N N 280 
MET CG   C  N N 281 
MET SD   S  N N 282 
MET CE   C  N N 283 
MET OXT  O  N N 284 
MET H    H  N N 285 
MET H2   H  N N 286 
MET HA   H  N N 287 
MET HB2  H  N N 288 
MET HB3  H  N N 289 
MET HG2  H  N N 290 
MET HG3  H  N N 291 
MET HE1  H  N N 292 
MET HE2  H  N N 293 
MET HE3  H  N N 294 
MET HXT  H  N N 295 
PHE N    N  N N 296 
PHE CA   C  N S 297 
PHE C    C  N N 298 
PHE O    O  N N 299 
PHE CB   C  N N 300 
PHE CG   C  Y N 301 
PHE CD1  C  Y N 302 
PHE CD2  C  Y N 303 
PHE CE1  C  Y N 304 
PHE CE2  C  Y N 305 
PHE CZ   C  Y N 306 
PHE OXT  O  N N 307 
PHE H    H  N N 308 
PHE H2   H  N N 309 
PHE HA   H  N N 310 
PHE HB2  H  N N 311 
PHE HB3  H  N N 312 
PHE HD1  H  N N 313 
PHE HD2  H  N N 314 
PHE HE1  H  N N 315 
PHE HE2  H  N N 316 
PHE HZ   H  N N 317 
PHE HXT  H  N N 318 
PRO N    N  N N 319 
PRO CA   C  N S 320 
PRO C    C  N N 321 
PRO O    O  N N 322 
PRO CB   C  N N 323 
PRO CG   C  N N 324 
PRO CD   C  N N 325 
PRO OXT  O  N N 326 
PRO H    H  N N 327 
PRO HA   H  N N 328 
PRO HB2  H  N N 329 
PRO HB3  H  N N 330 
PRO HG2  H  N N 331 
PRO HG3  H  N N 332 
PRO HD2  H  N N 333 
PRO HD3  H  N N 334 
PRO HXT  H  N N 335 
SER N    N  N N 336 
SER CA   C  N S 337 
SER C    C  N N 338 
SER O    O  N N 339 
SER CB   C  N N 340 
SER OG   O  N N 341 
SER OXT  O  N N 342 
SER H    H  N N 343 
SER H2   H  N N 344 
SER HA   H  N N 345 
SER HB2  H  N N 346 
SER HB3  H  N N 347 
SER HG   H  N N 348 
SER HXT  H  N N 349 
THR N    N  N N 350 
THR CA   C  N S 351 
THR C    C  N N 352 
THR O    O  N N 353 
THR CB   C  N R 354 
THR OG1  O  N N 355 
THR CG2  C  N N 356 
THR OXT  O  N N 357 
THR H    H  N N 358 
THR H2   H  N N 359 
THR HA   H  N N 360 
THR HB   H  N N 361 
THR HG1  H  N N 362 
THR HG21 H  N N 363 
THR HG22 H  N N 364 
THR HG23 H  N N 365 
THR HXT  H  N N 366 
TRP N    N  N N 367 
TRP CA   C  N S 368 
TRP C    C  N N 369 
TRP O    O  N N 370 
TRP CB   C  N N 371 
TRP CG   C  Y N 372 
TRP CD1  C  Y N 373 
TRP CD2  C  Y N 374 
TRP NE1  N  Y N 375 
TRP CE2  C  Y N 376 
TRP CE3  C  Y N 377 
TRP CZ2  C  Y N 378 
TRP CZ3  C  Y N 379 
TRP CH2  C  Y N 380 
TRP OXT  O  N N 381 
TRP H    H  N N 382 
TRP H2   H  N N 383 
TRP HA   H  N N 384 
TRP HB2  H  N N 385 
TRP HB3  H  N N 386 
TRP HD1  H  N N 387 
TRP HE1  H  N N 388 
TRP HE3  H  N N 389 
TRP HZ2  H  N N 390 
TRP HZ3  H  N N 391 
TRP HH2  H  N N 392 
TRP HXT  H  N N 393 
TYR N    N  N N 394 
TYR CA   C  N S 395 
TYR C    C  N N 396 
TYR O    O  N N 397 
TYR CB   C  N N 398 
TYR CG   C  Y N 399 
TYR CD1  C  Y N 400 
TYR CD2  C  Y N 401 
TYR CE1  C  Y N 402 
TYR CE2  C  Y N 403 
TYR CZ   C  Y N 404 
TYR OH   O  N N 405 
TYR OXT  O  N N 406 
TYR H    H  N N 407 
TYR H2   H  N N 408 
TYR HA   H  N N 409 
TYR HB2  H  N N 410 
TYR HB3  H  N N 411 
TYR HD1  H  N N 412 
TYR HD2  H  N N 413 
TYR HE1  H  N N 414 
TYR HE2  H  N N 415 
TYR HH   H  N N 416 
TYR HXT  H  N N 417 
VAL N    N  N N 418 
VAL CA   C  N S 419 
VAL C    C  N N 420 
VAL O    O  N N 421 
VAL CB   C  N N 422 
VAL CG1  C  N N 423 
VAL CG2  C  N N 424 
VAL OXT  O  N N 425 
VAL H    H  N N 426 
VAL H2   H  N N 427 
VAL HA   H  N N 428 
VAL HB   H  N N 429 
VAL HG11 H  N N 430 
VAL HG12 H  N N 431 
VAL HG13 H  N N 432 
VAL HG21 H  N N 433 
VAL HG22 H  N N 434 
VAL HG23 H  N N 435 
VAL HXT  H  N N 436 
ZN  ZN   ZN N N 437 
# 
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 
J71 N1  C2   doub Y N 182 
J71 N1  C6   sing Y N 183 
J71 C2  N3   sing Y N 184 
J71 N3  C4   doub Y N 185 
J71 C4  C5   sing Y N 186 
J71 C4  N7   sing N N 187 
J71 C5  C6   doub Y N 188 
J71 C5  N18  sing N N 189 
J71 C6  O21  sing N N 190 
J71 N7  C23  sing N N 191 
J71 C8  C9   doub Y N 192 
J71 C8  C13  sing Y N 193 
J71 C8  C23  sing N N 194 
J71 C9  C10  sing Y N 195 
J71 C10 C11  doub Y N 196 
J71 C11 C12  sing Y N 197 
J71 C11 S14  sing N N 198 
J71 C12 C13  doub Y N 199 
J71 S14 O15  doub N N 200 
J71 S14 O16  doub N N 201 
J71 S14 N17  sing N N 202 
J71 N18 O19  sing N N 203 
J71 N18 O20  doub N N 204 
J71 O21 C22  sing N N 205 
J71 C2  H2   sing N N 206 
J71 N7  HN7  sing N N 207 
J71 C9  H9   sing N N 208 
J71 C10 H10  sing N N 209 
J71 C12 H12  sing N N 210 
J71 C13 H13  sing N N 211 
J71 N17 HN17 sing N N 212 
J71 N17 HN1A sing N N 213 
J71 C22 H22  sing N N 214 
J71 C22 H22A sing N N 215 
J71 C22 H22B sing N N 216 
J71 C23 H23  sing N N 217 
J71 C23 H23A sing N N 218 
LEU N   CA   sing N N 219 
LEU N   H    sing N N 220 
LEU N   H2   sing N N 221 
LEU CA  C    sing N N 222 
LEU CA  CB   sing N N 223 
LEU CA  HA   sing N N 224 
LEU C   O    doub N N 225 
LEU C   OXT  sing N N 226 
LEU CB  CG   sing N N 227 
LEU CB  HB2  sing N N 228 
LEU CB  HB3  sing N N 229 
LEU CG  CD1  sing N N 230 
LEU CG  CD2  sing N N 231 
LEU CG  HG   sing N N 232 
LEU CD1 HD11 sing N N 233 
LEU CD1 HD12 sing N N 234 
LEU CD1 HD13 sing N N 235 
LEU CD2 HD21 sing N N 236 
LEU CD2 HD22 sing N N 237 
LEU CD2 HD23 sing N N 238 
LEU OXT HXT  sing N N 239 
LYS N   CA   sing N N 240 
LYS N   H    sing N N 241 
LYS N   H2   sing N N 242 
LYS CA  C    sing N N 243 
LYS CA  CB   sing N N 244 
LYS CA  HA   sing N N 245 
LYS C   O    doub N N 246 
LYS C   OXT  sing N N 247 
LYS CB  CG   sing N N 248 
LYS CB  HB2  sing N N 249 
LYS CB  HB3  sing N N 250 
LYS CG  CD   sing N N 251 
LYS CG  HG2  sing N N 252 
LYS CG  HG3  sing N N 253 
LYS CD  CE   sing N N 254 
LYS CD  HD2  sing N N 255 
LYS CD  HD3  sing N N 256 
LYS CE  NZ   sing N N 257 
LYS CE  HE2  sing N N 258 
LYS CE  HE3  sing N N 259 
LYS NZ  HZ1  sing N N 260 
LYS NZ  HZ2  sing N N 261 
LYS NZ  HZ3  sing N N 262 
LYS OXT HXT  sing N N 263 
MET N   CA   sing N N 264 
MET N   H    sing N N 265 
MET N   H2   sing N N 266 
MET CA  C    sing N N 267 
MET CA  CB   sing N N 268 
MET CA  HA   sing N N 269 
MET C   O    doub N N 270 
MET C   OXT  sing N N 271 
MET CB  CG   sing N N 272 
MET CB  HB2  sing N N 273 
MET CB  HB3  sing N N 274 
MET CG  SD   sing N N 275 
MET CG  HG2  sing N N 276 
MET CG  HG3  sing N N 277 
MET SD  CE   sing N N 278 
MET CE  HE1  sing N N 279 
MET CE  HE2  sing N N 280 
MET CE  HE3  sing N N 281 
MET OXT HXT  sing N N 282 
PHE N   CA   sing N N 283 
PHE N   H    sing N N 284 
PHE N   H2   sing N N 285 
PHE CA  C    sing N N 286 
PHE CA  CB   sing N N 287 
PHE CA  HA   sing N N 288 
PHE C   O    doub N N 289 
PHE C   OXT  sing N N 290 
PHE CB  CG   sing N N 291 
PHE CB  HB2  sing N N 292 
PHE CB  HB3  sing N N 293 
PHE CG  CD1  doub Y N 294 
PHE CG  CD2  sing Y N 295 
PHE CD1 CE1  sing Y N 296 
PHE CD1 HD1  sing N N 297 
PHE CD2 CE2  doub Y N 298 
PHE CD2 HD2  sing N N 299 
PHE CE1 CZ   doub Y N 300 
PHE CE1 HE1  sing N N 301 
PHE CE2 CZ   sing Y N 302 
PHE CE2 HE2  sing N N 303 
PHE CZ  HZ   sing N N 304 
PHE OXT HXT  sing N N 305 
PRO N   CA   sing N N 306 
PRO N   CD   sing N N 307 
PRO N   H    sing N N 308 
PRO CA  C    sing N N 309 
PRO CA  CB   sing N N 310 
PRO CA  HA   sing N N 311 
PRO C   O    doub N N 312 
PRO C   OXT  sing N N 313 
PRO CB  CG   sing N N 314 
PRO CB  HB2  sing N N 315 
PRO CB  HB3  sing N N 316 
PRO CG  CD   sing N N 317 
PRO CG  HG2  sing N N 318 
PRO CG  HG3  sing N N 319 
PRO CD  HD2  sing N N 320 
PRO CD  HD3  sing N N 321 
PRO OXT HXT  sing N N 322 
SER N   CA   sing N N 323 
SER N   H    sing N N 324 
SER N   H2   sing N N 325 
SER CA  C    sing N N 326 
SER CA  CB   sing N N 327 
SER CA  HA   sing N N 328 
SER C   O    doub N N 329 
SER C   OXT  sing N N 330 
SER CB  OG   sing N N 331 
SER CB  HB2  sing N N 332 
SER CB  HB3  sing N N 333 
SER OG  HG   sing N N 334 
SER OXT HXT  sing N N 335 
THR N   CA   sing N N 336 
THR N   H    sing N N 337 
THR N   H2   sing N N 338 
THR CA  C    sing N N 339 
THR CA  CB   sing N N 340 
THR CA  HA   sing N N 341 
THR C   O    doub N N 342 
THR C   OXT  sing N N 343 
THR CB  OG1  sing N N 344 
THR CB  CG2  sing N N 345 
THR CB  HB   sing N N 346 
THR OG1 HG1  sing N N 347 
THR CG2 HG21 sing N N 348 
THR CG2 HG22 sing N N 349 
THR CG2 HG23 sing N N 350 
THR OXT HXT  sing N N 351 
TRP N   CA   sing N N 352 
TRP N   H    sing N N 353 
TRP N   H2   sing N N 354 
TRP CA  C    sing N N 355 
TRP CA  CB   sing N N 356 
TRP CA  HA   sing N N 357 
TRP C   O    doub N N 358 
TRP C   OXT  sing N N 359 
TRP CB  CG   sing N N 360 
TRP CB  HB2  sing N N 361 
TRP CB  HB3  sing N N 362 
TRP CG  CD1  doub Y N 363 
TRP CG  CD2  sing Y N 364 
TRP CD1 NE1  sing Y N 365 
TRP CD1 HD1  sing N N 366 
TRP CD2 CE2  doub Y N 367 
TRP CD2 CE3  sing Y N 368 
TRP NE1 CE2  sing Y N 369 
TRP NE1 HE1  sing N N 370 
TRP CE2 CZ2  sing Y N 371 
TRP CE3 CZ3  doub Y N 372 
TRP CE3 HE3  sing N N 373 
TRP CZ2 CH2  doub Y N 374 
TRP CZ2 HZ2  sing N N 375 
TRP CZ3 CH2  sing Y N 376 
TRP CZ3 HZ3  sing N N 377 
TRP CH2 HH2  sing N N 378 
TRP OXT HXT  sing N N 379 
TYR N   CA   sing N N 380 
TYR N   H    sing N N 381 
TYR N   H2   sing N N 382 
TYR CA  C    sing N N 383 
TYR CA  CB   sing N N 384 
TYR CA  HA   sing N N 385 
TYR C   O    doub N N 386 
TYR C   OXT  sing N N 387 
TYR CB  CG   sing N N 388 
TYR CB  HB2  sing N N 389 
TYR CB  HB3  sing N N 390 
TYR CG  CD1  doub Y N 391 
TYR CG  CD2  sing Y N 392 
TYR CD1 CE1  sing Y N 393 
TYR CD1 HD1  sing N N 394 
TYR CD2 CE2  doub Y N 395 
TYR CD2 HD2  sing N N 396 
TYR CE1 CZ   doub Y N 397 
TYR CE1 HE1  sing N N 398 
TYR CE2 CZ   sing Y N 399 
TYR CE2 HE2  sing N N 400 
TYR CZ  OH   sing N N 401 
TYR OH  HH   sing N N 402 
TYR OXT HXT  sing N N 403 
VAL N   CA   sing N N 404 
VAL N   H    sing N N 405 
VAL N   H2   sing N N 406 
VAL CA  C    sing N N 407 
VAL CA  CB   sing N N 408 
VAL CA  HA   sing N N 409 
VAL C   O    doub N N 410 
VAL C   OXT  sing N N 411 
VAL CB  CG1  sing N N 412 
VAL CB  CG2  sing N N 413 
VAL CB  HB   sing N N 414 
VAL CG1 HG11 sing N N 415 
VAL CG1 HG12 sing N N 416 
VAL CG1 HG13 sing N N 417 
VAL CG2 HG21 sing N N 418 
VAL CG2 HG22 sing N N 419 
VAL CG2 HG23 sing N N 420 
VAL OXT HXT  sing N N 421 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                             ZN  
3 'DIMETHYL SULFOXIDE'                                                   DMS 
4 '4-{[(6-methoxy-5-nitropyrimidin-4-yl)amino]methyl}benzenesulfonamide' J71 
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   2NNO 
_pdbx_initial_refinement_model.details          'PDB ENTRY 2NNO' 
# 
