data_3M96
# 
_entry.id   3M96 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   3M96         pdb_00003m96 10.2210/pdb3m96/pdb 
RCSB  RCSB058265   ?            ?                   
WWPDB D_1000058265 ?            ?                   
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          3M98 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.entry_id                        3M96 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2010-03-20 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'  1 
'Manakova, E.'  2 
'Golovenko, D.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Indapamide-like benzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, and XIII.' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            18 
_citation.page_first                7357 
_citation.page_last                 7364 
_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   20926301 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2010.09.016 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Baranauskiene, L.' 1 ? 
primary 'Golovenko, D.'     2 ? 
primary 'Manakova, E.'      3 ? 
primary 'Grazulis, S.'      4 ? 
primary 'Tumkevicius, S.'   5 ? 
primary 'Matulis, D.'       6 ? 
# 
_cell.entry_id           3M96 
_cell.length_a           42.050 
_cell.length_b           40.921 
_cell.length_c           71.468 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.140 
_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                         3M96 
_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 '5-{[(5-bromo-1H-benzimidazol-2-yl)sulfanyl]acetyl}-2-chlorobenzenesulfonamide' 460.753   1   ?       ? ? ? 
5 water       nat water                                                                           18.015    239 ?       ? ? ? 
# 
_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                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3M96 
_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  
E38 non-polymer         . '5-{[(5-bromo-1H-benzimidazol-2-yl)sulfanyl]acetyl}-2-chlorobenzenesulfonamide' ? 
'C15 H11 Br Cl N3 O3 S2' 460.753 
GLN 'L-peptide linking' y GLUTAMINE                                                                       ? 'C5 H10 N2 O3' 146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                 ? 'C5 H9 N O4' 147.129 
GLY 'peptide linking'   y GLYCINE                                                                         ? 'C2 H5 N O2' 75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                       ? 'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                                                           ? 'H2 O' 18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                      ? 'C6 H13 N O2' 131.173 
LEU 'L-peptide linking' y LEUCINE                                                                         ? 'C6 H13 N O2' 131.173 
LYS 'L-peptide linking' y LYSINE                                                                          ? 'C6 H15 N2 O2 1' 
147.195 
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          3M96 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   39.58 
_exptl_crystal.density_Matthews      2.04 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9.0, 0.2 M ammonium sulfate and 2M sodium malonate, pH 7.0 made from 1M sodium BICINE and 3.4M sodium malonate, vapor diffusion, sitting drop, temperature 291K
;
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2009-12-17 
_diffrn_detector.details                ? 
# 
_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   0.9443 
_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        0.9443 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X12 
# 
_reflns.entry_id                     3M96 
_reflns.d_resolution_high            1.400 
_reflns.d_resolution_low             28.884 
_reflns.number_all                   46670 
_reflns.number_obs                   46297 
_reflns.pdbx_Rmerge_I_obs            0.095 
_reflns.pdbx_netI_over_sigmaI        22.900 
_reflns.pdbx_Rsym_value              0.095 
_reflns.pdbx_redundancy              9.300 
_reflns.percent_possible_obs         99.200 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   ? 
_reflns.B_iso_Wilson_estimate        14.3 
_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             1.40 
_reflns_shell.d_res_low              1.48 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    49268 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.253 
_reflns_shell.meanI_over_sigI_obs    4.4 
_reflns_shell.pdbx_Rsym_value        0.253 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_redundancy        7.40 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      6614 
_reflns_shell.percent_possible_all   98.10 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3M96 
_refine.ls_d_res_high                            1.400 
_refine.ls_d_res_low                             28.470 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.230 
_refine.ls_number_reflns_obs                     46284 
_refine.ls_number_reflns_all                     46670 
_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                          ? 
_refine.ls_R_factor_obs                          0.180 
_refine.ls_R_factor_R_work                       0.176 
_refine.ls_wR_factor_R_work                      0.179 
_refine.ls_R_factor_R_free                       0.213 
_refine.ls_wR_factor_R_free                      0.217 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  4647 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               15.552 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.120 
_refine.aniso_B[2][2]                            -0.510 
_refine.aniso_B[3][3]                            0.440 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.110 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.overall_SU_R_Cruickshank_DPI             0.069 
_refine.overall_SU_R_free                        0.074 
_refine.pdbx_overall_ESU_R                       0.069 
_refine.pdbx_overall_ESU_R_Free                  0.074 
_refine.overall_SU_ML                            0.043 
_refine.overall_SU_B                             1.049 
_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                   0.877 
_refine.B_iso_max                                47.97 
_refine.B_iso_min                                5.24 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB entry 3HLJ' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_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         34 
_refine_hist.number_atoms_solvent             239 
_refine_hist.number_atoms_total               2322 
_refine_hist.d_res_high                       1.400 
_refine_hist.d_res_low                        28.470 
# 
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         2188 0.032  0.022  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      2980 2.587  1.965  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   267  6.952  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   98   35.393 24.694 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   359  13.325 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   7    22.122 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           311  0.186  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     1695 0.017  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            1062 0.226  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          1482 0.325  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    205  0.150  0.200  ? 'X-RAY DIFFRACTION' ? 
r_metal_ion_refined      3    0.078  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   60   0.187  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 58   0.212  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              1360 1.840  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             2135 2.474  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              990  3.309  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             845  4.879  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.400 
_refine_ls_shell.d_res_low                        1.436 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               98.260 
_refine_ls_shell.number_reflns_R_work             2989 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.278 
_refine_ls_shell.R_factor_R_free                  0.341 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             334 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                3323 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3M96 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 5-{[(5-bromo-1H-benzimidazol-2-yl)sulfanyl]acetyl}-2-chlorobenzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3M96 
_struct_keywords.text            'drug design, carbonic anhydrase, benzenesulfonamide, lyase' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 HIS A 15  ? PHE A 20  ? HIS A 15  PHE A 20  1 ? 6 
HELX_P HELX_P2 2 PRO A 21  ? GLY A 25  ? PRO A 21  GLY A 25  5 ? 5 
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 -3.63 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 2.58  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  262 ? 4  'BINDING SITE FOR RESIDUE ZN A 262'  
AC2 Software A DMS 263 ? 3  'BINDING SITE FOR RESIDUE DMS A 263' 
AC3 Software A DMS 264 ? 3  'BINDING SITE FOR RESIDUE DMS A 264' 
AC4 Software A E38 265 ? 15 'BINDING SITE FOR RESIDUE E38 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  E38 E .   ? E38 A 265 . ? 1_555 ? 
5  AC2 3  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 3  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 3  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC3 3  GLN A 92  ? GLN A 92  . ? 1_555 ? 
9  AC3 3  E38 E .   ? E38 A 265 . ? 1_555 ? 
10 AC3 3  HOH F .   ? HOH A 345 . ? 1_555 ? 
11 AC4 15 ASN A 62  ? ASN A 62  . ? 1_555 ? 
12 AC4 15 ASN A 67  ? ASN A 67  . ? 1_555 ? 
13 AC4 15 GLN A 92  ? GLN A 92  . ? 1_555 ? 
14 AC4 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
15 AC4 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
16 AC4 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
17 AC4 15 LEU A 140 ? LEU A 141 . ? 1_555 ? 
18 AC4 15 VAL A 142 ? VAL A 143 . ? 1_555 ? 
19 AC4 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
20 AC4 15 THR A 198 ? THR A 199 . ? 1_555 ? 
21 AC4 15 THR A 199 ? THR A 200 . ? 1_555 ? 
22 AC4 15 PRO A 201 ? PRO A 202 . ? 1_555 ? 
23 AC4 15 TRP A 208 ? TRP A 209 . ? 1_555 ? 
24 AC4 15 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
25 AC4 15 DMS D .   ? DMS A 264 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3M96 
_atom_sites.fract_transf_matrix[1][1]   0.023781 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005993 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024438 
_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]   0.014430 
_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 
BR 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . HIS A 1 4   ? 9.343   1.489   8.356   1.00 26.75 ? 4   HIS A N    1 
ATOM   2    C  CA   . HIS A 1 4   ? 9.596   0.054   8.183   1.00 26.68 ? 4   HIS A CA   1 
ATOM   3    C  C    . HIS A 1 4   ? 9.216   -0.874  9.321   1.00 21.35 ? 4   HIS A C    1 
ATOM   4    O  O    . HIS A 1 4   ? 9.499   -2.040  9.243   1.00 20.58 ? 4   HIS A O    1 
ATOM   5    C  CB   . HIS A 1 4   ? 10.959  -0.256  7.492   1.00 26.85 ? 4   HIS A CB   1 
ATOM   6    C  CG   . HIS A 1 4   ? 12.121  -0.622  8.364   1.00 34.34 ? 4   HIS A CG   1 
ATOM   7    N  ND1  . HIS A 1 4   ? 13.301  -1.093  7.792   1.00 35.66 ? 4   HIS A ND1  1 
ATOM   8    C  CD2  . HIS A 1 4   ? 12.329  -0.583  9.712   1.00 31.72 ? 4   HIS A CD2  1 
ATOM   9    C  CE1  . HIS A 1 4   ? 14.169  -1.362  8.757   1.00 38.97 ? 4   HIS A CE1  1 
ATOM   10   N  NE2  . HIS A 1 4   ? 13.599  -1.079  9.927   1.00 40.99 ? 4   HIS A NE2  1 
ATOM   11   N  N    . TRP A 1 5   ? 8.421   -0.393  10.262  1.00 19.12 ? 5   TRP A N    1 
ATOM   12   C  CA   . TRP A 1 5   ? 7.730   -1.400  11.141  1.00 14.48 ? 5   TRP A CA   1 
ATOM   13   C  C    . TRP A 1 5   ? 6.702   -2.182  10.322  1.00 12.36 ? 5   TRP A C    1 
ATOM   14   O  O    . TRP A 1 5   ? 6.148   -1.697  9.343   1.00 15.03 ? 5   TRP A O    1 
ATOM   15   C  CB   . TRP A 1 5   ? 7.044   -0.729  12.367  1.00 15.10 ? 5   TRP A CB   1 
ATOM   16   C  CG   . TRP A 1 5   ? 5.805   0.060   12.011  1.00 15.86 ? 5   TRP A CG   1 
ATOM   17   C  CD1  . TRP A 1 5   ? 5.700   1.446   11.710  1.00 15.65 ? 5   TRP A CD1  1 
ATOM   18   C  CD2  . TRP A 1 5   ? 4.426   -0.449  11.988  1.00 12.95 ? 5   TRP A CD2  1 
ATOM   19   N  NE1  . TRP A 1 5   ? 4.390   1.772   11.493  1.00 16.75 ? 5   TRP A NE1  1 
ATOM   20   C  CE2  . TRP A 1 5   ? 3.594   0.643   11.641  1.00 13.88 ? 5   TRP A CE2  1 
ATOM   21   C  CE3  . TRP A 1 5   ? 3.836   -1.713  12.224  1.00 12.15 ? 5   TRP A CE3  1 
ATOM   22   C  CZ2  . TRP A 1 5   ? 2.197   0.522   11.533  1.00 14.87 ? 5   TRP A CZ2  1 
ATOM   23   C  CZ3  . TRP A 1 5   ? 2.404   -1.800  12.092  1.00 13.21 ? 5   TRP A CZ3  1 
ATOM   24   C  CH2  . TRP A 1 5   ? 1.626   -0.697  11.770  1.00 13.72 ? 5   TRP A CH2  1 
ATOM   25   N  N    . GLY A 1 6   ? 6.507   -3.423  10.825  1.00 12.64 ? 6   GLY A N    1 
ATOM   26   C  CA   . GLY A 1 6   ? 5.448   -4.231  10.240  1.00 12.49 ? 6   GLY A CA   1 
ATOM   27   C  C    . GLY A 1 6   ? 5.106   -5.349  11.200  1.00 11.89 ? 6   GLY A C    1 
ATOM   28   O  O    . GLY A 1 6   ? 5.145   -5.213  12.398  1.00 11.83 ? 6   GLY A O    1 
ATOM   29   N  N    . TYR A 1 7   ? 4.785   -6.469  10.606  1.00 12.86 ? 7   TYR A N    1 
ATOM   30   C  CA   . TYR A 1 7   ? 4.385   -7.659  11.415  1.00 15.33 ? 7   TYR A CA   1 
ATOM   31   C  C    . TYR A 1 7   ? 5.277   -8.918  11.292  1.00 18.57 ? 7   TYR A C    1 
ATOM   32   O  O    . TYR A 1 7   ? 4.996   -9.944  11.941  1.00 19.90 ? 7   TYR A O    1 
ATOM   33   C  CB   . TYR A 1 7   ? 2.934   -7.984  11.136  1.00 13.84 ? 7   TYR A CB   1 
ATOM   34   C  CG   . TYR A 1 7   ? 2.047   -6.895  11.686  1.00 10.93 ? 7   TYR A CG   1 
ATOM   35   C  CD1  . TYR A 1 7   ? 1.676   -6.928  13.040  1.00 10.39 ? 7   TYR A CD1  1 
ATOM   36   C  CD2  . TYR A 1 7   ? 1.467   -5.911  10.863  1.00 10.93 ? 7   TYR A CD2  1 
ATOM   37   C  CE1  . TYR A 1 7   ? 0.772   -5.931  13.549  1.00 8.36  ? 7   TYR A CE1  1 
ATOM   38   C  CE2  . TYR A 1 7   ? 0.632   -4.882  11.376  1.00 10.20 ? 7   TYR A CE2  1 
ATOM   39   C  CZ   . TYR A 1 7   ? 0.293   -4.968  12.748  1.00 9.01  ? 7   TYR A CZ   1 
ATOM   40   O  OH   . TYR A 1 7   ? -0.576  -4.004  13.196  1.00 9.83  ? 7   TYR A OH   1 
ATOM   41   N  N    . GLY A 1 8   ? 6.433   -8.762  10.612  1.00 17.87 ? 8   GLY A N    1 
ATOM   42   C  CA   . GLY A 1 8   ? 7.415   -9.905  10.350  1.00 17.51 ? 8   GLY A CA   1 
ATOM   43   C  C    . GLY A 1 8   ? 8.383   -10.146 11.507  1.00 16.61 ? 8   GLY A C    1 
ATOM   44   O  O    . GLY A 1 8   ? 8.475   -9.480  12.567  1.00 20.07 ? 8   GLY A O    1 
ATOM   45   N  N    . LYS A 1 9   ? 9.297   -11.143 11.319  1.00 20.95 ? 9   LYS A N    1 
ATOM   46   C  CA   . LYS A 1 9   ? 10.289  -11.579 12.339  1.00 21.65 ? 9   LYS A CA   1 
ATOM   47   C  C    . LYS A 1 9   ? 11.243  -10.460 12.594  1.00 19.96 ? 9   LYS A C    1 
ATOM   48   O  O    . LYS A 1 9   ? 11.756  -10.354 13.743  1.00 20.49 ? 9   LYS A O    1 
ATOM   49   C  CB   . LYS A 1 9   ? 11.175  -12.781 11.905  1.00 22.82 ? 9   LYS A CB   1 
ATOM   50   C  CG   . LYS A 1 9   ? 12.245  -13.207 12.952  1.00 24.01 ? 9   LYS A CG   1 
ATOM   51   C  CD   . LYS A 1 9   ? 11.624  -13.976 14.112  0.01 23.41 ? 9   LYS A CD   1 
ATOM   52   C  CE   . LYS A 1 9   ? 12.677  -14.395 15.124  0.01 23.33 ? 9   LYS A CE   1 
ATOM   53   N  NZ   . LYS A 1 9   ? 12.076  -15.105 16.286  0.01 23.50 ? 9   LYS A NZ   1 
ATOM   54   N  N    . HIS A 1 10  ? 11.494  -9.712  11.507  1.00 20.40 ? 10  HIS A N    1 
ATOM   55   C  CA   . HIS A 1 10  ? 12.531  -8.694  11.669  1.00 20.55 ? 10  HIS A CA   1 
ATOM   56   C  C    . HIS A 1 10  ? 12.026  -7.303  11.930  1.00 18.44 ? 10  HIS A C    1 
ATOM   57   O  O    . HIS A 1 10  ? 12.828  -6.494  12.386  1.00 18.87 ? 10  HIS A O    1 
ATOM   58   C  CB   . HIS A 1 10  ? 13.582  -8.732  10.537  1.00 19.06 ? 10  HIS A CB   1 
ATOM   59   C  CG   . HIS A 1 10  ? 14.317  -10.066 10.455  1.00 18.86 ? 10  HIS A CG   1 
ATOM   60   N  ND1  . HIS A 1 10  ? 15.343  -10.444 11.309  1.00 23.83 ? 10  HIS A ND1  1 
ATOM   61   C  CD2  . HIS A 1 10  ? 14.082  -11.110 9.659   1.00 22.63 ? 10  HIS A CD2  1 
ATOM   62   C  CE1  . HIS A 1 10  ? 15.759  -11.654 10.984  1.00 21.61 ? 10  HIS A CE1  1 
ATOM   63   N  NE2  . HIS A 1 10  ? 14.938  -12.111 10.040  1.00 18.53 ? 10  HIS A NE2  1 
ATOM   64   N  N    . ASN A 1 11  ? 10.675  -7.051  11.692  1.00 17.61 ? 11  ASN A N    1 
ATOM   65   C  CA   . ASN A 1 11  ? 10.191  -5.710  11.987  1.00 14.01 ? 11  ASN A CA   1 
ATOM   66   C  C    . ASN A 1 11  ? 8.840   -5.752  12.763  1.00 14.97 ? 11  ASN A C    1 
ATOM   67   O  O    . ASN A 1 11  ? 8.194   -4.725  12.829  1.00 14.12 ? 11  ASN A O    1 
ATOM   68   C  CB   . ASN A 1 11  ? 9.968   -5.009  10.712  1.00 13.44 ? 11  ASN A CB   1 
ATOM   69   C  CG   . ASN A 1 11  ? 8.913   -5.661  9.857   1.00 15.22 ? 11  ASN A CG   1 
ATOM   70   O  OD1  . ASN A 1 11  ? 8.371   -6.713  10.255  1.00 18.10 ? 11  ASN A OD1  1 
ATOM   71   N  ND2  . ASN A 1 11  ? 8.591   -5.089  8.721   1.00 14.73 ? 11  ASN A ND2  1 
ATOM   72   N  N    . GLY A 1 12  ? 8.528   -6.892  13.321  1.00 13.75 ? 12  GLY A N    1 
ATOM   73   C  CA   . GLY A 1 12  ? 7.169   -7.078  13.999  1.00 12.44 ? 12  GLY A CA   1 
ATOM   74   C  C    . GLY A 1 12  ? 7.223   -6.600  15.408  1.00 12.88 ? 12  GLY A C    1 
ATOM   75   O  O    . GLY A 1 12  ? 8.099   -5.821  15.883  1.00 13.93 ? 12  GLY A O    1 
ATOM   76   N  N    . PRO A 1 13  ? 6.102   -6.851  16.152  1.00 11.95 ? 13  PRO A N    1 
ATOM   77   C  CA   . PRO A 1 13  ? 5.892   -6.324  17.443  1.00 14.05 ? 13  PRO A CA   1 
ATOM   78   C  C    . PRO A 1 13  ? 7.034   -6.341  18.419  1.00 13.36 ? 13  PRO A C    1 
ATOM   79   O  O    . PRO A 1 13  ? 7.177   -5.410  19.259  1.00 13.54 ? 13  PRO A O    1 
ATOM   80   C  CB   . PRO A 1 13  ? 4.664   -7.128  17.911  1.00 12.93 ? 13  PRO A CB   1 
ATOM   81   C  CG   . PRO A 1 13  ? 3.909   -7.404  16.765  1.00 13.16 ? 13  PRO A CG   1 
ATOM   82   C  CD   . PRO A 1 13  ? 4.938   -7.646  15.659  1.00 11.92 ? 13  PRO A CD   1 
ATOM   83   N  N    . GLU A 1 14  ? 7.874   -7.376  18.361  1.00 12.43 ? 14  GLU A N    1 
ATOM   84   C  CA   . GLU A 1 14  ? 8.974   -7.400  19.347  1.00 15.32 ? 14  GLU A CA   1 
ATOM   85   C  C    . GLU A 1 14  ? 10.149  -6.419  19.048  1.00 12.54 ? 14  GLU A C    1 
ATOM   86   O  O    . GLU A 1 14  ? 10.975  -6.196  19.931  1.00 14.72 ? 14  GLU A O    1 
ATOM   87   C  CB   . GLU A 1 14  ? 9.573   -8.785  19.458  1.00 18.55 ? 14  GLU A CB   1 
ATOM   88   C  CG   . GLU A 1 14  ? 8.518   -9.899  19.778  1.00 23.37 ? 14  GLU A CG   1 
ATOM   89   C  CD   . GLU A 1 14  ? 7.598   -9.590  21.014  1.00 37.26 ? 14  GLU A CD   1 
ATOM   90   O  OE1  . GLU A 1 14  ? 8.207   -9.286  22.078  1.00 42.36 ? 14  GLU A OE1  1 
ATOM   91   O  OE2  . GLU A 1 14  ? 6.302   -9.676  20.926  1.00 35.42 ? 14  GLU A OE2  1 
ATOM   92   N  N    . HIS A 1 15  ? 10.079  -5.796  17.883  1.00 12.25 ? 15  HIS A N    1 
ATOM   93   C  CA   . HIS A 1 15  ? 11.032  -4.785  17.436  1.00 12.61 ? 15  HIS A CA   1 
ATOM   94   C  C    . HIS A 1 15  ? 10.599  -3.360  17.664  1.00 13.20 ? 15  HIS A C    1 
ATOM   95   O  O    . HIS A 1 15  ? 11.385  -2.456  17.651  1.00 13.50 ? 15  HIS A O    1 
ATOM   96   C  CB   . HIS A 1 15  ? 11.345  -4.967  15.941  1.00 11.71 ? 15  HIS A CB   1 
ATOM   97   C  CG   . HIS A 1 15  ? 12.075  -6.245  15.701  1.00 14.52 ? 15  HIS A CG   1 
ATOM   98   N  ND1  . HIS A 1 15  ? 13.445  -6.285  15.865  1.00 18.80 ? 15  HIS A ND1  1 
ATOM   99   C  CD2  . HIS A 1 15  ? 11.685  -7.485  15.308  1.00 17.90 ? 15  HIS A CD2  1 
ATOM   100  C  CE1  . HIS A 1 15  ? 13.876  -7.508  15.600  1.00 21.98 ? 15  HIS A CE1  1 
ATOM   101  N  NE2  . HIS A 1 15  ? 12.845  -8.264  15.291  1.00 18.64 ? 15  HIS A NE2  1 
ATOM   102  N  N    . TRP A 1 16  ? 9.263   -3.163  17.776  1.00 10.72 ? 16  TRP A N    1 
ATOM   103  C  CA   . TRP A 1 16  ? 8.719   -1.810  17.720  1.00 11.07 ? 16  TRP A CA   1 
ATOM   104  C  C    . TRP A 1 16  ? 9.292   -0.866  18.745  1.00 10.36 ? 16  TRP A C    1 
ATOM   105  O  O    . TRP A 1 16  ? 9.378   0.351   18.483  1.00 12.06 ? 16  TRP A O    1 
ATOM   106  C  CB   . TRP A 1 16  ? 7.170   -1.912  17.851  1.00 9.57  ? 16  TRP A CB   1 
ATOM   107  C  CG   . TRP A 1 16  ? 6.541   -2.547  16.696  1.00 10.26 ? 16  TRP A CG   1 
ATOM   108  C  CD1  . TRP A 1 16  ? 7.039   -2.930  15.510  1.00 9.34  ? 16  TRP A CD1  1 
ATOM   109  C  CD2  . TRP A 1 16  ? 5.119   -2.919  16.671  1.00 8.96  ? 16  TRP A CD2  1 
ATOM   110  N  NE1  . TRP A 1 16  ? 6.071   -3.516  14.691  1.00 9.98  ? 16  TRP A NE1  1 
ATOM   111  C  CE2  . TRP A 1 16  ? 4.871   -3.455  15.411  1.00 9.63  ? 16  TRP A CE2  1 
ATOM   112  C  CE3  . TRP A 1 16  ? 4.041   -2.693  17.584  1.00 9.48  ? 16  TRP A CE3  1 
ATOM   113  C  CZ2  . TRP A 1 16  ? 3.570   -3.943  15.036  1.00 8.73  ? 16  TRP A CZ2  1 
ATOM   114  C  CZ3  . TRP A 1 16  ? 2.763   -3.182  17.205  1.00 9.29  ? 16  TRP A CZ3  1 
ATOM   115  C  CH2  . TRP A 1 16  ? 2.515   -3.678  15.961  1.00 10.28 ? 16  TRP A CH2  1 
ATOM   116  N  N    . HIS A 1 17  ? 9.704   -1.362  19.872  1.00 10.02 ? 17  HIS A N    1 
ATOM   117  C  CA   . HIS A 1 17  ? 10.220  -0.522  20.954  1.00 11.60 ? 17  HIS A CA   1 
ATOM   118  C  C    . HIS A 1 17  ? 11.508  0.292   20.578  1.00 12.16 ? 17  HIS A C    1 
ATOM   119  O  O    . HIS A 1 17  ? 11.717  1.355   21.162  1.00 12.50 ? 17  HIS A O    1 
ATOM   120  C  CB   . HIS A 1 17  ? 10.512  -1.258  22.240  1.00 12.29 ? 17  HIS A CB   1 
ATOM   121  C  CG   . HIS A 1 17  ? 11.710  -2.159  22.100  1.00 11.63 ? 17  HIS A CG   1 
ATOM   122  N  ND1  . HIS A 1 17  ? 12.927  -1.770  22.648  1.00 17.87 ? 17  HIS A ND1  1 
ATOM   123  C  CD2  . HIS A 1 17  ? 11.872  -3.366  21.555  1.00 16.76 ? 17  HIS A CD2  1 
ATOM   124  C  CE1  . HIS A 1 17  ? 13.804  -2.715  22.345  1.00 14.69 ? 17  HIS A CE1  1 
ATOM   125  N  NE2  . HIS A 1 17  ? 13.211  -3.690  21.710  1.00 16.65 ? 17  HIS A NE2  1 
ATOM   126  N  N    . LYS A 1 18  ? 12.190  -0.225  19.579  1.00 13.31 ? 18  LYS A N    1 
ATOM   127  C  CA   . LYS A 1 18  ? 13.466  0.493   19.238  1.00 13.83 ? 18  LYS A CA   1 
ATOM   128  C  C    . LYS A 1 18  ? 13.070  1.822   18.613  1.00 15.82 ? 18  LYS A C    1 
ATOM   129  O  O    . LYS A 1 18  ? 13.651  2.905   18.971  1.00 18.09 ? 18  LYS A O    1 
ATOM   130  C  CB   . LYS A 1 18  ? 14.284  -0.357  18.311  1.00 14.70 ? 18  LYS A CB   1 
ATOM   131  C  CG   . LYS A 1 18  ? 14.904  -1.524  19.074  1.00 17.21 ? 18  LYS A CG   1 
ATOM   132  C  CD   . LYS A 1 18  ? 15.686  -2.457  18.158  1.00 14.62 ? 18  LYS A CD   1 
ATOM   133  C  CE   . LYS A 1 18  ? 14.684  -3.399  17.389  1.00 15.49 ? 18  LYS A CE   1 
ATOM   134  N  NZ   . LYS A 1 18  ? 15.273  -4.325  16.352  1.00 15.27 ? 18  LYS A NZ   1 
ATOM   135  N  N    . ASP A 1 19  ? 12.078  1.845   17.678  1.00 13.82 ? 19  ASP A N    1 
ATOM   136  C  CA   . ASP A 1 19  ? 11.680  3.133   17.143  1.00 15.66 ? 19  ASP A CA   1 
ATOM   137  C  C    . ASP A 1 19  ? 10.633  3.868   17.957  1.00 16.03 ? 19  ASP A C    1 
ATOM   138  O  O    . ASP A 1 19  ? 10.466  5.044   17.783  1.00 15.70 ? 19  ASP A O    1 
ATOM   139  C  CB   . ASP A 1 19  ? 11.075  2.989   15.770  1.00 18.10 ? 19  ASP A CB   1 
ATOM   140  C  CG   . ASP A 1 19  ? 12.105  3.103   14.630  1.00 23.38 ? 19  ASP A CG   1 
ATOM   141  O  OD1  . ASP A 1 19  ? 13.175  3.604   14.906  1.00 27.47 ? 19  ASP A OD1  1 
ATOM   142  O  OD2  . ASP A 1 19  ? 11.812  2.744   13.450  1.00 31.05 ? 19  ASP A OD2  1 
ATOM   143  N  N    . PHE A 1 20  ? 9.916   3.127   18.828  1.00 15.69 ? 20  PHE A N    1 
ATOM   144  C  CA   . PHE A 1 20  ? 8.758   3.689   19.528  1.00 13.32 ? 20  PHE A CA   1 
ATOM   145  C  C    . PHE A 1 20  ? 8.837   3.194   20.985  1.00 12.90 ? 20  PHE A C    1 
ATOM   146  O  O    . PHE A 1 20  ? 8.212   2.173   21.364  1.00 12.10 ? 20  PHE A O    1 
ATOM   147  C  CB   . PHE A 1 20  ? 7.416   3.201   18.847  1.00 12.47 ? 20  PHE A CB   1 
ATOM   148  C  CG   . PHE A 1 20  ? 7.336   3.554   17.436  1.00 11.58 ? 20  PHE A CG   1 
ATOM   149  C  CD1  . PHE A 1 20  ? 7.002   4.856   17.070  1.00 15.09 ? 20  PHE A CD1  1 
ATOM   150  C  CD2  . PHE A 1 20  ? 7.669   2.674   16.424  1.00 11.52 ? 20  PHE A CD2  1 
ATOM   151  C  CE1  . PHE A 1 20  ? 6.972   5.171   15.673  1.00 13.81 ? 20  PHE A CE1  1 
ATOM   152  C  CE2  . PHE A 1 20  ? 7.672   2.979   15.140  1.00 12.46 ? 20  PHE A CE2  1 
ATOM   153  C  CZ   . PHE A 1 20  ? 7.298   4.279   14.755  1.00 14.26 ? 20  PHE A CZ   1 
ATOM   154  N  N    . PRO A 1 21  ? 9.757   3.760   21.757  1.00 12.82 ? 21  PRO A N    1 
ATOM   155  C  CA   . PRO A 1 21  ? 10.049  3.267   23.044  1.00 11.85 ? 21  PRO A CA   1 
ATOM   156  C  C    . PRO A 1 21  ? 8.821   3.181   23.985  1.00 14.26 ? 21  PRO A C    1 
ATOM   157  O  O    . PRO A 1 21  ? 8.795   2.416   24.914  1.00 13.94 ? 21  PRO A O    1 
ATOM   158  C  CB   . PRO A 1 21  ? 11.132  4.299   23.611  1.00 15.50 ? 21  PRO A CB   1 
ATOM   159  C  CG   . PRO A 1 21  ? 11.207  5.331   22.506  1.00 17.96 ? 21  PRO A CG   1 
ATOM   160  C  CD   . PRO A 1 21  ? 10.670  4.828   21.274  1.00 15.49 ? 21  PRO A CD   1 
ATOM   161  N  N    A ILE A 1 22  ? 7.747   3.965   23.807  0.50 12.33 ? 22  ILE A N    1 
ATOM   162  N  N    B ILE A 1 22  ? 7.819   3.977   23.554  0.50 11.35 ? 22  ILE A N    1 
ATOM   163  C  CA   A ILE A 1 22  ? 6.490   3.765   24.625  0.50 11.10 ? 22  ILE A CA   1 
ATOM   164  C  CA   B ILE A 1 22  ? 6.526   3.958   24.240  0.50 11.49 ? 22  ILE A CA   1 
ATOM   165  C  C    A ILE A 1 22  ? 5.888   2.347   24.421  0.50 10.18 ? 22  ILE A C    1 
ATOM   166  C  C    B ILE A 1 22  ? 5.874   2.546   24.227  0.50 10.17 ? 22  ILE A C    1 
ATOM   167  O  O    A ILE A 1 22  ? 5.037   1.926   25.246  0.50 10.12 ? 22  ILE A O    1 
ATOM   168  O  O    B ILE A 1 22  ? 5.024   2.316   25.027  0.50 8.84  ? 22  ILE A O    1 
ATOM   169  C  CB   A ILE A 1 22  ? 5.393   4.771   24.176  0.50 8.94  ? 22  ILE A CB   1 
ATOM   170  C  CB   B ILE A 1 22  ? 5.587   5.147   23.765  0.50 8.22  ? 22  ILE A CB   1 
ATOM   171  C  CG1  A ILE A 1 22  ? 4.353   5.087   25.266  0.50 12.01 ? 22  ILE A CG1  1 
ATOM   172  C  CG1  B ILE A 1 22  ? 4.487   5.406   24.812  0.50 10.05 ? 22  ILE A CG1  1 
ATOM   173  C  CG2  A ILE A 1 22  ? 4.764   4.229   22.854  0.50 8.78  ? 22  ILE A CG2  1 
ATOM   174  C  CG2  B ILE A 1 22  ? 4.907   4.803   22.418  0.50 10.59 ? 22  ILE A CG2  1 
ATOM   175  C  CD1  A ILE A 1 22  ? 4.894   5.914   26.460  0.50 13.90 ? 22  ILE A CD1  1 
ATOM   176  C  CD1  B ILE A 1 22  ? 3.490   6.421   24.451  0.50 11.60 ? 22  ILE A CD1  1 
ATOM   177  N  N    . ALA A 1 23  ? 6.397   1.618   23.431  1.00 10.37 ? 23  ALA A N    1 
ATOM   178  C  CA   . ALA A 1 23  ? 5.941   0.217   23.343  1.00 10.99 ? 23  ALA A CA   1 
ATOM   179  C  C    . ALA A 1 23  ? 6.022   -0.473  24.651  1.00 11.69 ? 23  ALA A C    1 
ATOM   180  O  O    . ALA A 1 23  ? 5.357   -1.509  24.863  1.00 12.28 ? 23  ALA A O    1 
ATOM   181  C  CB   . ALA A 1 23  ? 6.785   -0.555  22.343  1.00 11.84 ? 23  ALA A CB   1 
ATOM   182  N  N    . LYS A 1 24  ? 6.980   -0.066  25.511  1.00 11.66 ? 24  LYS A N    1 
ATOM   183  C  CA   . LYS A 1 24  ? 7.166   -0.683  26.857  1.00 12.88 ? 24  LYS A CA   1 
ATOM   184  C  C    . LYS A 1 24  ? 6.612   0.192   27.935  1.00 13.62 ? 24  LYS A C    1 
ATOM   185  O  O    . LYS A 1 24  ? 6.926   0.037   29.118  1.00 16.63 ? 24  LYS A O    1 
ATOM   186  C  CB   . LYS A 1 24  ? 8.661   -0.960  27.179  1.00 14.80 ? 24  LYS A CB   1 
ATOM   187  C  CG   . LYS A 1 24  ? 9.251   -1.864  26.223  1.00 18.13 ? 24  LYS A CG   1 
ATOM   188  C  CD   . LYS A 1 24  ? 10.690  -2.119  26.717  1.00 22.83 ? 24  LYS A CD   1 
ATOM   189  C  CE   . LYS A 1 24  ? 11.385  -2.802  25.625  1.00 22.44 ? 24  LYS A CE   1 
ATOM   190  N  NZ   . LYS A 1 24  ? 11.164  -4.193  25.738  1.00 25.11 ? 24  LYS A NZ   1 
ATOM   191  N  N    . GLY A 1 25  ? 5.583   1.017   27.575  1.00 13.37 ? 25  GLY A N    1 
ATOM   192  C  CA   . GLY A 1 25  ? 4.935   1.970   28.483  1.00 14.84 ? 25  GLY A CA   1 
ATOM   193  C  C    . GLY A 1 25  ? 3.974   1.341   29.457  1.00 10.95 ? 25  GLY A C    1 
ATOM   194  O  O    . GLY A 1 25  ? 3.780   0.138   29.578  1.00 13.80 ? 25  GLY A O    1 
ATOM   195  N  N    . GLU A 1 26  ? 3.347   2.283   30.163  1.00 13.24 ? 26  GLU A N    1 
ATOM   196  C  CA   . GLU A 1 26  ? 2.458   1.878   31.156  1.00 13.67 ? 26  GLU A CA   1 
ATOM   197  C  C    . GLU A 1 26  ? 0.997   1.635   30.852  1.00 13.01 ? 26  GLU A C    1 
ATOM   198  O  O    . GLU A 1 26  ? 0.272   1.158   31.702  1.00 12.61 ? 26  GLU A O    1 
ATOM   199  C  CB   . GLU A 1 26  ? 2.455   2.973   32.285  1.00 16.21 ? 26  GLU A CB   1 
ATOM   200  C  CG   . GLU A 1 26  ? 3.819   3.215   33.044  1.00 18.44 ? 26  GLU A CG   1 
ATOM   201  C  CD   . GLU A 1 26  ? 4.408   1.915   33.616  1.00 25.34 ? 26  GLU A CD   1 
ATOM   202  O  OE1  . GLU A 1 26  ? 3.749   1.247   34.486  1.00 30.00 ? 26  GLU A OE1  1 
ATOM   203  O  OE2  . GLU A 1 26  ? 5.504   1.511   33.131  1.00 31.28 ? 26  GLU A OE2  1 
ATOM   204  N  N    . ARG A 1 27  ? 0.575   1.951   29.602  1.00 11.13 ? 27  ARG A N    1 
ATOM   205  C  CA   . ARG A 1 27  ? -0.873  1.694   29.306  1.00 10.59 ? 27  ARG A CA   1 
ATOM   206  C  C    . ARG A 1 27  ? -0.872  1.276   27.812  1.00 8.98  ? 27  ARG A C    1 
ATOM   207  O  O    . ARG A 1 27  ? -1.552  1.927   26.967  1.00 8.62  ? 27  ARG A O    1 
ATOM   208  C  CB   . ARG A 1 27  ? -1.727  2.944   29.589  1.00 11.00 ? 27  ARG A CB   1 
ATOM   209  C  CG   . ARG A 1 27  ? -1.360  4.236   28.957  1.00 15.81 ? 27  ARG A CG   1 
ATOM   210  C  CD   . ARG A 1 27  ? -2.441  5.383   29.186  1.00 16.48 ? 27  ARG A CD   1 
ATOM   211  N  NE   . ARG A 1 27  ? -3.585  5.241   28.253  1.00 14.00 ? 27  ARG A NE   1 
ATOM   212  C  CZ   . ARG A 1 27  ? -4.540  6.157   28.195  1.00 12.82 ? 27  ARG A CZ   1 
ATOM   213  N  NH1  . ARG A 1 27  ? -4.446  7.341   28.862  1.00 14.41 ? 27  ARG A NH1  1 
ATOM   214  N  NH2  . ARG A 1 27  ? -5.424  6.045   27.338  1.00 14.55 ? 27  ARG A NH2  1 
ATOM   215  N  N    . GLN A 1 28  ? -0.162  0.205   27.486  1.00 9.01  ? 28  GLN A N    1 
ATOM   216  C  CA   . GLN A 1 28  ? -0.118  -0.370  26.122  1.00 7.25  ? 28  GLN A CA   1 
ATOM   217  C  C    . GLN A 1 28  ? -1.285  -1.363  25.887  1.00 8.77  ? 28  GLN A C    1 
ATOM   218  O  O    . GLN A 1 28  ? -1.789  -1.995  26.786  1.00 8.20  ? 28  GLN A O    1 
ATOM   219  C  CB   . GLN A 1 28  ? 1.237   -1.025  25.869  1.00 9.22  ? 28  GLN A CB   1 
ATOM   220  C  CG   . GLN A 1 28  ? 2.338   0.043   25.849  1.00 10.32 ? 28  GLN A CG   1 
ATOM   221  C  CD   . GLN A 1 28  ? 2.178   0.841   24.509  1.00 9.48  ? 28  GLN A CD   1 
ATOM   222  O  OE1  . GLN A 1 28  ? 2.412   0.308   23.442  1.00 8.71  ? 28  GLN A OE1  1 
ATOM   223  N  NE2  . GLN A 1 28  ? 1.873   2.134   24.599  1.00 8.78  ? 28  GLN A NE2  1 
ATOM   224  N  N    . SER A 1 29  ? -1.645  -1.361  24.619  1.00 7.31  ? 29  SER A N    1 
ATOM   225  C  CA   . SER A 1 29  ? -2.729  -2.259  24.186  1.00 6.48  ? 29  SER A CA   1 
ATOM   226  C  C    . SER A 1 29  ? -2.182  -3.159  23.059  1.00 8.54  ? 29  SER A C    1 
ATOM   227  O  O    . SER A 1 29  ? -1.275  -2.773  22.358  1.00 7.78  ? 29  SER A O    1 
ATOM   228  C  CB   . SER A 1 29  ? -3.826  -1.392  23.586  1.00 7.98  ? 29  SER A CB   1 
ATOM   229  O  OG   . SER A 1 29  ? -4.489  -0.724  24.664  1.00 7.71  ? 29  SER A OG   1 
ATOM   230  N  N    . PRO A 1 30  ? -2.824  -4.269  22.799  1.00 7.02  ? 30  PRO A N    1 
ATOM   231  C  CA   . PRO A 1 30  ? -3.997  -4.809  23.524  1.00 7.04  ? 30  PRO A CA   1 
ATOM   232  C  C    . PRO A 1 30  ? -3.637  -5.466  24.808  1.00 7.96  ? 30  PRO A C    1 
ATOM   233  O  O    . PRO A 1 30  ? -2.403  -5.542  25.119  1.00 9.02  ? 30  PRO A O    1 
ATOM   234  C  CB   . PRO A 1 30  ? -4.551  -5.799  22.543  1.00 6.60  ? 30  PRO A CB   1 
ATOM   235  C  CG   . PRO A 1 30  ? -3.209  -6.489  21.900  1.00 7.70  ? 30  PRO A CG   1 
ATOM   236  C  CD   . PRO A 1 30  ? -2.332  -5.196  21.754  1.00 8.44  ? 30  PRO A CD   1 
ATOM   237  N  N    . VAL A 1 31  ? -4.576  -6.095  25.469  1.00 7.48  ? 31  VAL A N    1 
ATOM   238  C  CA   . VAL A 1 31  ? -4.354  -6.850  26.701  1.00 6.85  ? 31  VAL A CA   1 
ATOM   239  C  C    . VAL A 1 31  ? -5.240  -8.032  26.647  1.00 7.39  ? 31  VAL A C    1 
ATOM   240  O  O    . VAL A 1 31  ? -6.253  -8.103  25.933  1.00 8.06  ? 31  VAL A O    1 
ATOM   241  C  CB   . VAL A 1 31  ? -4.700  -5.978  27.976  1.00 8.37  ? 31  VAL A CB   1 
ATOM   242  C  CG1  . VAL A 1 31  ? -3.757  -4.802  28.092  1.00 10.38 ? 31  VAL A CG1  1 
ATOM   243  C  CG2  . VAL A 1 31  ? -6.178  -5.570  27.975  1.00 8.88  ? 31  VAL A CG2  1 
ATOM   244  N  N    . ASP A 1 32  ? -4.972  -8.967  27.526  1.00 7.97  ? 32  ASP A N    1 
ATOM   245  C  CA   . ASP A 1 32  ? -5.851  -10.061 27.810  1.00 7.49  ? 32  ASP A CA   1 
ATOM   246  C  C    . ASP A 1 32  ? -6.939  -9.523  28.782  1.00 9.54  ? 32  ASP A C    1 
ATOM   247  O  O    . ASP A 1 32  ? -6.630  -8.895  29.795  1.00 10.38 ? 32  ASP A O    1 
ATOM   248  C  CB   . ASP A 1 32  ? -5.102  -11.287 28.399  1.00 9.59  ? 32  ASP A CB   1 
ATOM   249  C  CG   . ASP A 1 32  ? -6.025  -12.436 28.746  1.00 12.40 ? 32  ASP A CG   1 
ATOM   250  O  OD1  . ASP A 1 32  ? -6.768  -12.849 27.813  1.00 9.69  ? 32  ASP A OD1  1 
ATOM   251  O  OD2  . ASP A 1 32  ? -6.099  -12.891 29.953  1.00 13.61 ? 32  ASP A OD2  1 
ATOM   252  N  N    . ILE A 1 33  ? -8.205  -9.853  28.462  1.00 9.58  ? 33  ILE A N    1 
ATOM   253  C  CA   . ILE A 1 33  ? -9.293  -9.514  29.342  1.00 10.61 ? 33  ILE A CA   1 
ATOM   254  C  C    . ILE A 1 33  ? -9.590  -10.730 30.173  1.00 10.56 ? 33  ILE A C    1 
ATOM   255  O  O    . ILE A 1 33  ? -10.066 -11.728 29.714  1.00 11.57 ? 33  ILE A O    1 
ATOM   256  C  CB   . ILE A 1 33  ? -10.476 -9.044  28.524  1.00 9.58  ? 33  ILE A CB   1 
ATOM   257  C  CG1  . ILE A 1 33  ? -10.109 -7.768  27.695  1.00 9.50  ? 33  ILE A CG1  1 
ATOM   258  C  CG2  . ILE A 1 33  ? -11.703 -8.837  29.457  1.00 11.11 ? 33  ILE A CG2  1 
ATOM   259  C  CD1  . ILE A 1 33  ? -11.206 -7.513  26.535  1.00 10.87 ? 33  ILE A CD1  1 
ATOM   260  N  N    . ASP A 1 34  ? -9.202  -10.628 31.428  1.00 12.94 ? 34  ASP A N    1 
ATOM   261  C  CA   . ASP A 1 34  ? -9.497  -11.748 32.361  1.00 12.76 ? 34  ASP A CA   1 
ATOM   262  C  C    . ASP A 1 34  ? -10.909 -11.489 32.865  1.00 12.89 ? 34  ASP A C    1 
ATOM   263  O  O    . ASP A 1 34  ? -11.084 -10.526 33.656  1.00 14.05 ? 34  ASP A O    1 
ATOM   264  C  CB   . ASP A 1 34  ? -8.429  -11.768 33.468  1.00 14.17 ? 34  ASP A CB   1 
ATOM   265  C  CG   . ASP A 1 34  ? -8.734  -12.748 34.673  1.00 18.42 ? 34  ASP A CG   1 
ATOM   266  O  OD1  . ASP A 1 34  ? -9.871  -13.145 34.871  1.00 22.68 ? 34  ASP A OD1  1 
ATOM   267  O  OD2  . ASP A 1 34  ? -7.687  -13.041 35.346  1.00 31.26 ? 34  ASP A OD2  1 
ATOM   268  N  N    . THR A 1 35  ? -11.894 -12.188 32.360  1.00 12.84 ? 35  THR A N    1 
ATOM   269  C  CA   . THR A 1 35  ? -13.278 -11.881 32.641  1.00 15.11 ? 35  THR A CA   1 
ATOM   270  C  C    . THR A 1 35  ? -13.685 -12.025 34.079  1.00 17.61 ? 35  THR A C    1 
ATOM   271  O  O    . THR A 1 35  ? -14.677 -11.396 34.542  1.00 18.01 ? 35  THR A O    1 
ATOM   272  C  CB   . THR A 1 35  ? -14.234 -12.789 31.871  1.00 15.54 ? 35  THR A CB   1 
ATOM   273  O  OG1  . THR A 1 35  ? -14.018 -14.140 32.330  1.00 17.14 ? 35  THR A OG1  1 
ATOM   274  C  CG2  . THR A 1 35  ? -14.011 -12.741 30.346  1.00 16.62 ? 35  THR A CG2  1 
ATOM   275  N  N    . HIS A 1 36  ? -12.956 -12.864 34.797  1.00 17.29 ? 36  HIS A N    1 
ATOM   276  C  CA   . HIS A 1 36  ? -13.266 -13.025 36.234  1.00 16.64 ? 36  HIS A CA   1 
ATOM   277  C  C    . HIS A 1 36  ? -12.736 -11.871 37.046  1.00 18.23 ? 36  HIS A C    1 
ATOM   278  O  O    . HIS A 1 36  ? -13.413 -11.571 38.066  1.00 19.65 ? 36  HIS A O    1 
ATOM   279  C  CB   . HIS A 1 36  ? -12.816 -14.457 36.647  1.00 16.00 ? 36  HIS A CB   1 
ATOM   280  C  CG   . HIS A 1 36  ? -13.719 -15.511 36.054  1.00 17.44 ? 36  HIS A CG   1 
ATOM   281  N  ND1  . HIS A 1 36  ? -15.045 -15.569 36.441  1.00 22.41 ? 36  HIS A ND1  1 
ATOM   282  C  CD2  . HIS A 1 36  ? -13.542 -16.494 35.125  1.00 19.58 ? 36  HIS A CD2  1 
ATOM   283  C  CE1  . HIS A 1 36  ? -15.655 -16.532 35.767  1.00 27.75 ? 36  HIS A CE1  1 
ATOM   284  N  NE2  . HIS A 1 36  ? -14.769 -17.090 34.945  1.00 23.44 ? 36  HIS A NE2  1 
ATOM   285  N  N    A THR A 1 37  ? -11.644 -11.211 36.655  0.50 17.43 ? 37  THR A N    1 
ATOM   286  N  N    B THR A 1 37  ? -11.571 -11.289 36.688  0.50 17.09 ? 37  THR A N    1 
ATOM   287  C  CA   A THR A 1 37  ? -11.167 -10.098 37.435  0.50 17.77 ? 37  THR A CA   1 
ATOM   288  C  CA   B THR A 1 37  ? -10.962 -10.160 37.382  0.50 17.02 ? 37  THR A CA   1 
ATOM   289  C  C    A THR A 1 37  ? -11.459 -8.675  36.932  0.50 15.78 ? 37  THR A C    1 
ATOM   290  C  C    B THR A 1 37  ? -11.641 -8.782  37.015  0.50 15.21 ? 37  THR A C    1 
ATOM   291  O  O    A THR A 1 37  ? -10.949 -7.668  37.514  0.50 16.24 ? 37  THR A O    1 
ATOM   292  O  O    B THR A 1 37  ? -11.685 -7.892  37.816  0.50 15.01 ? 37  THR A O    1 
ATOM   293  C  CB   A THR A 1 37  ? -9.714  -10.162 37.676  0.50 18.35 ? 37  THR A CB   1 
ATOM   294  C  CB   B THR A 1 37  ? -9.398  -10.121 37.228  0.50 19.39 ? 37  THR A CB   1 
ATOM   295  O  OG1  A THR A 1 37  ? -8.986  -10.288 36.428  0.50 18.88 ? 37  THR A OG1  1 
ATOM   296  O  OG1  B THR A 1 37  ? -8.833  -11.325 37.765  0.50 20.28 ? 37  THR A OG1  1 
ATOM   297  C  CG2  A THR A 1 37  ? -9.398  -11.344 38.567  0.50 18.84 ? 37  THR A CG2  1 
ATOM   298  C  CG2  B THR A 1 37  ? -8.727  -8.956  38.002  0.50 16.49 ? 37  THR A CG2  1 
ATOM   299  N  N    . ALA A 1 38  ? -12.183 -8.654  35.817  1.00 15.48 ? 38  ALA A N    1 
ATOM   300  C  CA   . ALA A 1 38  ? -12.869 -7.414  35.371  1.00 15.10 ? 38  ALA A CA   1 
ATOM   301  C  C    . ALA A 1 38  ? -13.915 -7.093  36.425  1.00 16.71 ? 38  ALA A C    1 
ATOM   302  O  O    . ALA A 1 38  ? -14.670 -7.928  36.879  1.00 19.99 ? 38  ALA A O    1 
ATOM   303  C  CB   . ALA A 1 38  ? -13.480 -7.627  34.004  1.00 15.72 ? 38  ALA A CB   1 
ATOM   304  N  N    . LYS A 1 39  ? -13.925 -5.830  36.778  1.00 15.19 ? 39  LYS A N    1 
ATOM   305  C  CA   . LYS A 1 39  ? -14.902 -5.384  37.756  1.00 16.80 ? 39  LYS A CA   1 
ATOM   306  C  C    . LYS A 1 39  ? -16.222 -4.908  37.048  1.00 14.68 ? 39  LYS A C    1 
ATOM   307  O  O    . LYS A 1 39  ? -16.191 -3.892  36.349  1.00 13.61 ? 39  LYS A O    1 
ATOM   308  C  CB   . LYS A 1 39  ? -14.207 -4.187  38.397  1.00 18.92 ? 39  LYS A CB   1 
ATOM   309  C  CG   . LYS A 1 39  ? -14.975 -3.430  39.461  1.00 23.04 ? 39  LYS A CG   1 
ATOM   310  C  CD   . LYS A 1 39  ? -15.056 -4.142  40.853  1.00 20.85 ? 39  LYS A CD   1 
ATOM   311  C  CE   . LYS A 1 39  ? -15.937 -3.251  41.756  1.00 25.38 ? 39  LYS A CE   1 
ATOM   312  N  NZ   . LYS A 1 39  ? -16.267 -3.894  43.032  1.00 30.00 ? 39  LYS A NZ   1 
ATOM   313  N  N    . TYR A 1 40  ? -17.375 -5.429  37.496  1.00 16.53 ? 40  TYR A N    1 
ATOM   314  C  CA   . TYR A 1 40  ? -18.625 -4.807  37.137  1.00 15.96 ? 40  TYR A CA   1 
ATOM   315  C  C    . TYR A 1 40  ? -18.726 -3.390  37.703  1.00 16.05 ? 40  TYR A C    1 
ATOM   316  O  O    . TYR A 1 40  ? -18.572 -3.167  38.954  1.00 16.62 ? 40  TYR A O    1 
ATOM   317  C  CB   . TYR A 1 40  ? -19.794 -5.721  37.476  1.00 20.21 ? 40  TYR A CB   1 
ATOM   318  C  CG   . TYR A 1 40  ? -21.105 -5.056  37.379  1.00 21.21 ? 40  TYR A CG   1 
ATOM   319  C  CD1  . TYR A 1 40  ? -21.606 -4.622  36.143  1.00 22.10 ? 40  TYR A CD1  1 
ATOM   320  C  CD2  . TYR A 1 40  ? -21.943 -4.941  38.518  1.00 23.21 ? 40  TYR A CD2  1 
ATOM   321  C  CE1  . TYR A 1 40  ? -22.793 -4.033  35.982  1.00 25.39 ? 40  TYR A CE1  1 
ATOM   322  C  CE2  . TYR A 1 40  ? -23.193 -4.327  38.361  1.00 26.93 ? 40  TYR A CE2  1 
ATOM   323  C  CZ   . TYR A 1 40  ? -23.604 -3.886  37.089  1.00 25.68 ? 40  TYR A CZ   1 
ATOM   324  O  OH   . TYR A 1 40  ? -24.840 -3.258  36.945  1.00 29.37 ? 40  TYR A OH   1 
ATOM   325  N  N    . ASP A 1 41  ? -19.001 -2.392  36.860  1.00 14.85 ? 41  ASP A N    1 
ATOM   326  C  CA   . ASP A 1 41  ? -19.096 -1.004  37.310  1.00 16.14 ? 41  ASP A CA   1 
ATOM   327  C  C    . ASP A 1 41  ? -20.525 -0.497  37.076  1.00 20.17 ? 41  ASP A C    1 
ATOM   328  O  O    . ASP A 1 41  ? -20.858 -0.199  35.968  1.00 16.57 ? 41  ASP A O    1 
ATOM   329  C  CB   . ASP A 1 41  ? -18.043 -0.148  36.610  1.00 18.97 ? 41  ASP A CB   1 
ATOM   330  C  CG   . ASP A 1 41  ? -18.028 1.288   37.143  1.00 26.24 ? 41  ASP A CG   1 
ATOM   331  O  OD1  . ASP A 1 41  ? -18.942 1.671   37.912  1.00 24.37 ? 41  ASP A OD1  1 
ATOM   332  O  OD2  . ASP A 1 41  ? -17.069 2.004   36.789  1.00 24.38 ? 41  ASP A OD2  1 
ATOM   333  N  N    . PRO A 1 42  ? -21.403 -0.513  38.121  1.00 21.72 ? 42  PRO A N    1 
ATOM   334  C  CA   . PRO A 1 42  ? -22.804 -0.131  37.894  1.00 24.49 ? 42  PRO A CA   1 
ATOM   335  C  C    . PRO A 1 42  ? -22.894 1.377   37.560  1.00 24.47 ? 42  PRO A C    1 
ATOM   336  O  O    . PRO A 1 42  ? -23.939 1.806   37.038  1.00 29.05 ? 42  PRO A O    1 
ATOM   337  C  CB   . PRO A 1 42  ? -23.496 -0.515  39.229  1.00 25.68 ? 42  PRO A CB   1 
ATOM   338  C  CG   . PRO A 1 42  ? -22.406 -0.478  40.244  1.00 24.98 ? 42  PRO A CG   1 
ATOM   339  C  CD   . PRO A 1 42  ? -21.133 -0.913  39.529  1.00 22.40 ? 42  PRO A CD   1 
ATOM   340  N  N    . SER A 1 43  ? -21.853 2.180   37.768  1.00 25.79 ? 43  SER A N    1 
ATOM   341  C  CA   . SER A 1 43  ? -21.867 3.582   37.282  1.00 26.18 ? 43  SER A CA   1 
ATOM   342  C  C    . SER A 1 43  ? -21.591 3.761   35.781  1.00 25.48 ? 43  SER A C    1 
ATOM   343  O  O    . SER A 1 43  ? -21.766 4.872   35.256  1.00 27.86 ? 43  SER A O    1 
ATOM   344  C  CB   . SER A 1 43  ? -20.838 4.491   38.001  1.00 26.63 ? 43  SER A CB   1 
ATOM   345  O  OG   . SER A 1 43  ? -19.514 4.234   37.632  1.00 28.20 ? 43  SER A OG   1 
ATOM   346  N  N    . LEU A 1 44  ? -21.133 2.721   35.072  1.00 23.71 ? 44  LEU A N    1 
ATOM   347  C  CA   . LEU A 1 44  ? -20.921 2.822   33.597  1.00 22.80 ? 44  LEU A CA   1 
ATOM   348  C  C    . LEU A 1 44  ? -22.272 2.935   32.948  1.00 24.58 ? 44  LEU A C    1 
ATOM   349  O  O    . LEU A 1 44  ? -23.233 2.316   33.414  1.00 24.78 ? 44  LEU A O    1 
ATOM   350  C  CB   . LEU A 1 44  ? -20.229 1.545   33.079  1.00 19.45 ? 44  LEU A CB   1 
ATOM   351  C  CG   . LEU A 1 44  ? -18.721 1.540   33.369  1.00 17.82 ? 44  LEU A CG   1 
ATOM   352  C  CD1  . LEU A 1 44  ? -18.172 0.190   32.955  1.00 16.46 ? 44  LEU A CD1  1 
ATOM   353  C  CD2  . LEU A 1 44  ? -18.032 2.691   32.615  1.00 17.40 ? 44  LEU A CD2  1 
ATOM   354  N  N    . LYS A 1 45  ? -22.323 3.719   31.877  1.00 22.75 ? 45  LYS A N    1 
ATOM   355  C  CA   . LYS A 1 45  ? -23.601 3.959   31.135  1.00 23.73 ? 45  LYS A CA   1 
ATOM   356  C  C    . LYS A 1 45  ? -23.656 3.094   29.930  1.00 22.01 ? 45  LYS A C    1 
ATOM   357  O  O    . LYS A 1 45  ? -22.614 2.494   29.533  1.00 21.81 ? 45  LYS A O    1 
ATOM   358  C  CB   . LYS A 1 45  ? -23.650 5.375   30.695  1.00 25.44 ? 45  LYS A CB   1 
ATOM   359  C  CG   . LYS A 1 45  ? -23.476 6.351   31.834  1.00 28.71 ? 45  LYS A CG   1 
ATOM   360  C  CD   . LYS A 1 45  ? -23.467 7.750   31.295  1.00 31.85 ? 45  LYS A CD   1 
ATOM   361  C  CE   . LYS A 1 45  ? -24.180 8.653   32.242  1.00 39.68 ? 45  LYS A CE   1 
ATOM   362  N  NZ   . LYS A 1 45  ? -25.010 9.483   31.312  1.00 42.29 ? 45  LYS A NZ   1 
ATOM   363  N  N    . PRO A 1 46  ? -24.901 2.880   29.405  1.00 18.97 ? 46  PRO A N    1 
ATOM   364  C  CA   . PRO A 1 46  ? -24.978 2.173   28.127  1.00 17.83 ? 46  PRO A CA   1 
ATOM   365  C  C    . PRO A 1 46  ? -24.129 2.941   27.137  1.00 15.71 ? 46  PRO A C    1 
ATOM   366  O  O    . PRO A 1 46  ? -24.092 4.161   27.135  1.00 15.07 ? 46  PRO A O    1 
ATOM   367  C  CB   . PRO A 1 46  ? -26.487 2.287   27.753  1.00 16.49 ? 46  PRO A CB   1 
ATOM   368  C  CG   . PRO A 1 46  ? -27.193 2.516   29.079  1.00 19.59 ? 46  PRO A CG   1 
ATOM   369  C  CD   . PRO A 1 46  ? -26.231 3.190   30.013  1.00 20.18 ? 46  PRO A CD   1 
ATOM   370  N  N    . LEU A 1 47  ? -23.555 2.171   26.225  1.00 19.01 ? 47  LEU A N    1 
ATOM   371  C  CA   . LEU A 1 47  ? -22.823 2.760   25.145  1.00 15.83 ? 47  LEU A CA   1 
ATOM   372  C  C    . LEU A 1 47  ? -23.835 3.438   24.201  1.00 18.70 ? 47  LEU A C    1 
ATOM   373  O  O    . LEU A 1 47  ? -24.907 2.814   23.936  1.00 20.33 ? 47  LEU A O    1 
ATOM   374  C  CB   . LEU A 1 47  ? -22.058 1.670   24.465  1.00 20.22 ? 47  LEU A CB   1 
ATOM   375  C  CG   . LEU A 1 47  ? -20.998 2.141   23.565  1.00 20.59 ? 47  LEU A CG   1 
ATOM   376  C  CD1  . LEU A 1 47  ? -19.929 3.037   24.356  1.00 21.23 ? 47  LEU A CD1  1 
ATOM   377  C  CD2  . LEU A 1 47  ? -20.379 0.862   22.929  1.00 21.40 ? 47  LEU A CD2  1 
ATOM   378  N  N    . SER A 1 48  ? -23.552 4.597   23.652  1.00 14.76 ? 48  SER A N    1 
ATOM   379  C  CA   . SER A 1 48  ? -24.440 5.209   22.675  1.00 14.84 ? 48  SER A CA   1 
ATOM   380  C  C    . SER A 1 48  ? -23.656 5.205   21.372  1.00 15.14 ? 48  SER A C    1 
ATOM   381  O  O    . SER A 1 48  ? -22.656 5.969   21.226  1.00 13.96 ? 48  SER A O    1 
ATOM   382  C  CB   . SER A 1 48  ? -24.765 6.663   23.146  1.00 17.76 ? 48  SER A CB   1 
ATOM   383  O  OG   . SER A 1 48  ? -25.310 7.457   22.117  1.00 19.72 ? 48  SER A OG   1 
ATOM   384  N  N    . VAL A 1 49  ? -24.154 4.525   20.393  1.00 15.49 ? 49  VAL A N    1 
ATOM   385  C  CA   . VAL A 1 49  ? -23.578 4.423   19.095  1.00 16.80 ? 49  VAL A CA   1 
ATOM   386  C  C    . VAL A 1 49  ? -24.521 5.012   18.091  1.00 18.18 ? 49  VAL A C    1 
ATOM   387  O  O    . VAL A 1 49  ? -25.605 4.415   17.875  1.00 18.47 ? 49  VAL A O    1 
ATOM   388  C  CB   . VAL A 1 49  ? -23.280 2.945   18.755  1.00 18.50 ? 49  VAL A CB   1 
ATOM   389  C  CG1  . VAL A 1 49  ? -22.684 2.813   17.367  1.00 23.71 ? 49  VAL A CG1  1 
ATOM   390  C  CG2  . VAL A 1 49  ? -22.421 2.302   19.831  1.00 17.63 ? 49  VAL A CG2  1 
ATOM   391  N  N    . SER A 1 50  ? -24.198 6.139   17.482  1.00 16.52 ? 50  SER A N    1 
ATOM   392  C  CA   . SER A 1 50  ? -25.164 6.854   16.613  1.00 18.98 ? 50  SER A CA   1 
ATOM   393  C  C    . SER A 1 50  ? -24.531 6.943   15.304  1.00 16.84 ? 50  SER A C    1 
ATOM   394  O  O    . SER A 1 50  ? -23.869 7.865   14.921  1.00 16.32 ? 50  SER A O    1 
ATOM   395  C  CB   . SER A 1 50  ? -25.605 8.213   17.234  1.00 18.57 ? 50  SER A CB   1 
ATOM   396  O  OG   . SER A 1 50  ? -26.158 7.957   18.494  1.00 25.82 ? 50  SER A OG   1 
ATOM   397  N  N    . TYR A 1 51  ? -24.794 5.920   14.515  1.00 16.61 ? 51  TYR A N    1 
ATOM   398  C  CA   . TYR A 1 51  ? -24.235 5.777   13.172  1.00 15.63 ? 51  TYR A CA   1 
ATOM   399  C  C    . TYR A 1 51  ? -25.219 5.989   12.004  1.00 16.86 ? 51  TYR A C    1 
ATOM   400  O  O    . TYR A 1 51  ? -24.803 5.836   10.885  1.00 16.59 ? 51  TYR A O    1 
ATOM   401  C  CB   . TYR A 1 51  ? -23.550 4.401   13.009  1.00 15.05 ? 51  TYR A CB   1 
ATOM   402  C  CG   . TYR A 1 51  ? -22.234 4.166   13.795  1.00 13.19 ? 51  TYR A CG   1 
ATOM   403  C  CD1  . TYR A 1 51  ? -21.501 5.208   14.392  1.00 14.11 ? 51  TYR A CD1  1 
ATOM   404  C  CD2  . TYR A 1 51  ? -21.756 2.877   13.872  1.00 13.04 ? 51  TYR A CD2  1 
ATOM   405  C  CE1  . TYR A 1 51  ? -20.296 4.852   15.092  1.00 11.89 ? 51  TYR A CE1  1 
ATOM   406  C  CE2  . TYR A 1 51  ? -20.562 2.539   14.512  1.00 13.97 ? 51  TYR A CE2  1 
ATOM   407  C  CZ   . TYR A 1 51  ? -19.835 3.576   15.108  1.00 11.98 ? 51  TYR A CZ   1 
ATOM   408  O  OH   . TYR A 1 51  ? -18.731 3.196   15.781  1.00 12.32 ? 51  TYR A OH   1 
ATOM   409  N  N    . ASP A 1 52  ? -26.417 6.510   12.318  1.00 19.36 ? 52  ASP A N    1 
ATOM   410  C  CA   . ASP A 1 52  ? -27.434 6.651   11.202  1.00 22.88 ? 52  ASP A CA   1 
ATOM   411  C  C    . ASP A 1 52  ? -26.978 7.564   10.067  1.00 22.77 ? 52  ASP A C    1 
ATOM   412  O  O    . ASP A 1 52  ? -27.308 7.331   8.888   1.00 23.79 ? 52  ASP A O    1 
ATOM   413  C  CB   . ASP A 1 52  ? -28.774 7.134   11.705  1.00 24.16 ? 52  ASP A CB   1 
ATOM   414  C  CG   . ASP A 1 52  ? -28.667 8.347   12.648  1.00 31.03 ? 52  ASP A CG   1 
ATOM   415  O  OD1  . ASP A 1 52  ? -28.205 8.228   13.834  1.00 41.20 ? 52  ASP A OD1  1 
ATOM   416  O  OD2  . ASP A 1 52  ? -29.111 9.440   12.221  1.00 43.24 ? 52  ASP A OD2  1 
ATOM   417  N  N    . GLN A 1 53  ? -26.116 8.515   10.378  1.00 21.66 ? 53  GLN A N    1 
ATOM   418  C  CA   . GLN A 1 53  ? -25.732 9.536   9.355   1.00 22.95 ? 53  GLN A CA   1 
ATOM   419  C  C    . GLN A 1 53  ? -24.274 9.323   8.910   1.00 19.91 ? 53  GLN A C    1 
ATOM   420  O  O    . GLN A 1 53  ? -23.683 10.182  8.310   1.00 19.83 ? 53  GLN A O    1 
ATOM   421  C  CB   . GLN A 1 53  ? -25.920 10.935  9.947   1.00 23.96 ? 53  GLN A CB   1 
ATOM   422  C  CG   . GLN A 1 53  ? -27.394 11.292  10.277  1.00 30.25 ? 53  GLN A CG   1 
ATOM   423  C  CD   . GLN A 1 53  ? -28.254 11.218  9.054   1.00 38.74 ? 53  GLN A CD   1 
ATOM   424  O  OE1  . GLN A 1 53  ? -27.817 11.597  7.943   1.00 44.49 ? 53  GLN A OE1  1 
ATOM   425  N  NE2  . GLN A 1 53  ? -29.481 10.703  9.216   1.00 44.40 ? 53  GLN A NE2  1 
ATOM   426  N  N    . ALA A 1 54  ? -23.689 8.174   9.237   1.00 18.65 ? 54  ALA A N    1 
ATOM   427  C  CA   . ALA A 1 54  ? -22.287 7.930   8.900   1.00 16.06 ? 54  ALA A CA   1 
ATOM   428  C  C    . ALA A 1 54  ? -22.079 8.075   7.391   1.00 17.25 ? 54  ALA A C    1 
ATOM   429  O  O    . ALA A 1 54  ? -23.027 7.648   6.603   1.00 19.80 ? 54  ALA A O    1 
ATOM   430  C  CB   . ALA A 1 54  ? -21.784 6.484   9.392   1.00 17.58 ? 54  ALA A CB   1 
ATOM   431  N  N    . THR A 1 55  ? -20.984 8.694   6.986   1.00 15.02 ? 55  THR A N    1 
ATOM   432  C  CA   . THR A 1 55  ? -20.630 8.907   5.590   1.00 15.35 ? 55  THR A CA   1 
ATOM   433  C  C    . THR A 1 55  ? -19.294 8.324   5.280   1.00 13.44 ? 55  THR A C    1 
ATOM   434  O  O    . THR A 1 55  ? -18.286 8.962   5.540   1.00 13.17 ? 55  THR A O    1 
ATOM   435  C  CB   . THR A 1 55  ? -20.622 10.475  5.253   1.00 19.01 ? 55  THR A CB   1 
ATOM   436  O  OG1  . THR A 1 55  ? -21.954 10.938  5.417   1.00 27.60 ? 55  THR A OG1  1 
ATOM   437  C  CG2  . THR A 1 55  ? -20.188 10.595  3.716   1.00 22.52 ? 55  THR A CG2  1 
ATOM   438  N  N    . SER A 1 56  ? -19.252 7.089   4.740   1.00 14.63 ? 56  SER A N    1 
ATOM   439  C  CA   . SER A 1 56  ? -17.994 6.547   4.399   1.00 15.81 ? 56  SER A CA   1 
ATOM   440  C  C    . SER A 1 56  ? -17.454 7.206   3.134   1.00 15.10 ? 56  SER A C    1 
ATOM   441  O  O    . SER A 1 56  ? -18.294 7.729   2.296   1.00 17.25 ? 56  SER A O    1 
ATOM   442  C  CB   . SER A 1 56  ? -18.018 4.995   4.218   1.00 12.85 ? 56  SER A CB   1 
ATOM   443  O  OG   . SER A 1 56  ? -18.903 4.643   3.102   1.00 16.99 ? 56  SER A OG   1 
ATOM   444  N  N    . LEU A 1 57  ? -16.173 7.231   2.944   1.00 15.80 ? 57  LEU A N    1 
ATOM   445  C  CA   . LEU A 1 57  ? -15.565 7.911   1.750   1.00 18.00 ? 57  LEU A CA   1 
ATOM   446  C  C    . LEU A 1 57  ? -14.802 6.962   0.859   1.00 20.71 ? 57  LEU A C    1 
ATOM   447  O  O    . LEU A 1 57  ? -14.822 6.990   -0.380  1.00 18.13 ? 57  LEU A O    1 
ATOM   448  C  CB   . LEU A 1 57  ? -14.577 8.998   2.182   1.00 19.54 ? 57  LEU A CB   1 
ATOM   449  C  CG   . LEU A 1 57  ? -15.292 10.240  2.812   1.00 23.04 ? 57  LEU A CG   1 
ATOM   450  C  CD1  . LEU A 1 57  ? -14.241 11.271  3.132   1.00 23.21 ? 57  LEU A CD1  1 
ATOM   451  C  CD2  . LEU A 1 57  ? -16.463 10.759  1.936   1.00 29.35 ? 57  LEU A CD2  1 
ATOM   452  N  N    . ARG A 1 58  ? -13.965 6.178   1.486   1.00 17.42 ? 58  ARG A N    1 
ATOM   453  C  CA   . ARG A 1 58  ? -12.967 5.490   0.764   1.00 15.98 ? 58  ARG A CA   1 
ATOM   454  C  C    . ARG A 1 58  ? -12.519 4.307   1.584   1.00 17.69 ? 58  ARG A C    1 
ATOM   455  O  O    . ARG A 1 58  ? -12.672 4.315   2.833   1.00 15.72 ? 58  ARG A O    1 
ATOM   456  C  CB   . ARG A 1 58  ? -11.761 6.380   0.633   1.00 17.90 ? 58  ARG A CB   1 
ATOM   457  C  CG   . ARG A 1 58  ? -10.871 6.063   -0.435  1.00 21.88 ? 58  ARG A CG   1 
ATOM   458  C  CD   . ARG A 1 58  ? -9.941  7.272   -0.513  1.00 28.43 ? 58  ARG A CD   1 
ATOM   459  N  NE   . ARG A 1 58  ? -9.085  7.239   0.685   1.00 20.94 ? 58  ARG A NE   1 
ATOM   460  C  CZ   . ARG A 1 58  ? -7.745  7.314   0.623   1.00 17.98 ? 58  ARG A CZ   1 
ATOM   461  N  NH1  . ARG A 1 58  ? -7.156  7.537   -0.535  1.00 23.10 ? 58  ARG A NH1  1 
ATOM   462  N  NH2  . ARG A 1 58  ? -7.055  7.328   1.788   1.00 22.12 ? 58  ARG A NH2  1 
ATOM   463  N  N    . ILE A 1 59  ? -11.870 3.366   0.918   1.00 16.11 ? 59  ILE A N    1 
ATOM   464  C  CA   . ILE A 1 59  ? -11.192 2.235   1.581   1.00 15.25 ? 59  ILE A CA   1 
ATOM   465  C  C    . ILE A 1 59  ? -9.773  2.213   1.079   1.00 15.34 ? 59  ILE A C    1 
ATOM   466  O  O    . ILE A 1 59  ? -9.455  2.381   -0.155  1.00 16.56 ? 59  ILE A O    1 
ATOM   467  C  CB   . ILE A 1 59  ? -11.927 0.956   1.324   1.00 14.51 ? 59  ILE A CB   1 
ATOM   468  C  CG1  . ILE A 1 59  ? -11.348 -0.203  2.209   1.00 14.97 ? 59  ILE A CG1  1 
ATOM   469  C  CG2  . ILE A 1 59  ? -11.878 0.628   -0.202  1.00 16.67 ? 59  ILE A CG2  1 
ATOM   470  C  CD1  . ILE A 1 59  ? -12.112 -1.535  2.080   1.00 17.53 ? 59  ILE A CD1  1 
ATOM   471  N  N    . LEU A 1 60  ? -8.790  2.048   1.954   1.00 15.54 ? 60  LEU A N    1 
ATOM   472  C  CA   . LEU A 1 60  ? -7.442  2.112   1.687   1.00 13.97 ? 60  LEU A CA   1 
ATOM   473  C  C    . LEU A 1 60  ? -6.640  0.933   2.217   1.00 13.90 ? 60  LEU A C    1 
ATOM   474  O  O    . LEU A 1 60  ? -6.835  0.604   3.428   1.00 13.54 ? 60  LEU A O    1 
ATOM   475  C  CB   . LEU A 1 60  ? -6.950  3.444   2.384   1.00 15.81 ? 60  LEU A CB   1 
ATOM   476  C  CG   . LEU A 1 60  ? -5.461  3.574   2.271   1.00 15.01 ? 60  LEU A CG   1 
ATOM   477  C  CD1  . LEU A 1 60  ? -4.891  3.728   0.784   1.00 19.67 ? 60  LEU A CD1  1 
ATOM   478  C  CD2  . LEU A 1 60  ? -4.921  4.752   3.286   1.00 16.38 ? 60  LEU A CD2  1 
ATOM   479  N  N    . ASN A 1 61  ? -5.763  0.318   1.422   1.00 12.71 ? 61  ASN A N    1 
ATOM   480  C  CA   . ASN A 1 61  ? -4.748  -0.591  1.863   1.00 12.59 ? 61  ASN A CA   1 
ATOM   481  C  C    . ASN A 1 61  ? -3.498  0.177   2.224   1.00 16.82 ? 61  ASN A C    1 
ATOM   482  O  O    . ASN A 1 61  ? -2.772  0.725   1.364   1.00 17.31 ? 61  ASN A O    1 
ATOM   483  C  CB   . ASN A 1 61  ? -4.404  -1.714  0.830   1.00 11.96 ? 61  ASN A CB   1 
ATOM   484  C  CG   . ASN A 1 61  ? -3.347  -2.672  1.255   1.00 13.50 ? 61  ASN A CG   1 
ATOM   485  O  OD1  . ASN A 1 61  ? -2.459  -2.447  2.124   1.00 13.13 ? 61  ASN A OD1  1 
ATOM   486  N  ND2  . ASN A 1 61  ? -3.387  -3.900  0.645   1.00 13.05 ? 61  ASN A ND2  1 
ATOM   487  N  N    . ASN A 1 62  ? -3.159  0.188   3.502   1.00 14.16 ? 62  ASN A N    1 
ATOM   488  C  CA   . ASN A 1 62  ? -2.097  1.106   3.982   1.00 13.99 ? 62  ASN A CA   1 
ATOM   489  C  C    . ASN A 1 62  ? -0.845  0.304   4.239   1.00 15.07 ? 62  ASN A C    1 
ATOM   490  O  O    . ASN A 1 62  ? 0.246   0.773   4.779   1.00 20.01 ? 62  ASN A O    1 
ATOM   491  C  CB   . ASN A 1 62  ? -2.530  1.931   5.206   1.00 15.11 ? 62  ASN A CB   1 
ATOM   492  C  CG   . ASN A 1 62  ? -2.769  1.034   6.443   1.00 14.91 ? 62  ASN A CG   1 
ATOM   493  O  OD1  . ASN A 1 62  ? -2.427  -0.165  6.444   1.00 13.90 ? 62  ASN A OD1  1 
ATOM   494  N  ND2  . ASN A 1 62  ? -3.099  1.703   7.543   1.00 22.93 ? 62  ASN A ND2  1 
ATOM   495  N  N    . GLY A 1 63  ? -0.831  -0.983  3.790   1.00 13.19 ? 63  GLY A N    1 
ATOM   496  C  CA   . GLY A 1 63  ? 0.275   -1.826  3.985   1.00 13.36 ? 63  GLY A CA   1 
ATOM   497  C  C    . GLY A 1 63  ? 0.407   -2.607  5.303   1.00 11.99 ? 63  GLY A C    1 
ATOM   498  O  O    . GLY A 1 63  ? 1.234   -3.438  5.525   1.00 14.20 ? 63  GLY A O    1 
ATOM   499  N  N    . HIS A 1 64  ? -0.560  -2.303  6.176   1.00 13.41 ? 64  HIS A N    1 
ATOM   500  C  CA   . HIS A 1 64  ? -0.714  -2.960  7.536   1.00 12.39 ? 64  HIS A CA   1 
ATOM   501  C  C    . HIS A 1 64  ? -2.085  -3.568  7.700   1.00 13.13 ? 64  HIS A C    1 
ATOM   502  O  O    . HIS A 1 64  ? -2.172  -4.651  8.289   1.00 17.13 ? 64  HIS A O    1 
ATOM   503  C  CB   . HIS A 1 64  ? -0.481  -1.925  8.690   1.00 13.53 ? 64  HIS A CB   1 
ATOM   504  C  CG   . HIS A 1 64  ? 0.813   -1.162  8.542   1.00 14.54 ? 64  HIS A CG   1 
ATOM   505  N  ND1  . HIS A 1 64  ? 2.034   -1.802  8.649   1.00 16.74 ? 64  HIS A ND1  1 
ATOM   506  C  CD2  . HIS A 1 64  ? 1.067   0.135   8.271   1.00 18.84 ? 64  HIS A CD2  1 
ATOM   507  C  CE1  . HIS A 1 64  ? 3.006   -0.915  8.471   1.00 16.21 ? 64  HIS A CE1  1 
ATOM   508  N  NE2  . HIS A 1 64  ? 2.455   0.249   8.207   1.00 16.19 ? 64  HIS A NE2  1 
ATOM   509  N  N    . ALA A 1 65  ? -3.096  -2.911  7.182   1.00 11.64 ? 65  ALA A N    1 
ATOM   510  C  CA   . ALA A 1 65  ? -4.444  -3.462  7.218   1.00 12.06 ? 65  ALA A CA   1 
ATOM   511  C  C    . ALA A 1 65  ? -5.191  -2.689  6.095   1.00 11.66 ? 65  ALA A C    1 
ATOM   512  O  O    . ALA A 1 65  ? -4.510  -2.010  5.251   1.00 12.30 ? 65  ALA A O    1 
ATOM   513  C  CB   . ALA A 1 65  ? -5.096  -3.294  8.646   1.00 12.54 ? 65  ALA A CB   1 
ATOM   514  N  N    . PHE A 1 66  ? -6.516  -2.691  6.107   1.00 11.17 ? 66  PHE A N    1 
ATOM   515  C  CA   . PHE A 1 66  ? -7.246  -1.720  5.261   1.00 11.29 ? 66  PHE A CA   1 
ATOM   516  C  C    . PHE A 1 66  ? -8.101  -0.826  6.147   1.00 12.08 ? 66  PHE A C    1 
ATOM   517  O  O    . PHE A 1 66  ? -8.717  -1.316  7.114   1.00 11.46 ? 66  PHE A O    1 
ATOM   518  C  CB   . PHE A 1 66  ? -8.030  -2.419  4.143   1.00 12.58 ? 66  PHE A CB   1 
ATOM   519  C  CG   . PHE A 1 66  ? -9.086  -3.381  4.637   1.00 12.23 ? 66  PHE A CG   1 
ATOM   520  C  CD1  . PHE A 1 66  ? -10.370 -2.875  4.965   1.00 11.64 ? 66  PHE A CD1  1 
ATOM   521  C  CD2  . PHE A 1 66  ? -8.870  -4.753  4.739   1.00 11.69 ? 66  PHE A CD2  1 
ATOM   522  C  CE1  . PHE A 1 66  ? -11.356 -3.675  5.439   1.00 11.97 ? 66  PHE A CE1  1 
ATOM   523  C  CE2  . PHE A 1 66  ? -9.870  -5.562  5.264   1.00 11.08 ? 66  PHE A CE2  1 
ATOM   524  C  CZ   . PHE A 1 66  ? -11.127 -5.012  5.580   1.00 10.43 ? 66  PHE A CZ   1 
ATOM   525  N  N    . ASN A 1 67  ? -8.187  0.474   5.814   1.00 12.48 ? 67  ASN A N    1 
ATOM   526  C  CA   . ASN A 1 67  ? -9.016  1.415   6.592   1.00 13.16 ? 67  ASN A CA   1 
ATOM   527  C  C    . ASN A 1 67  ? -10.252 1.793   5.800   1.00 11.95 ? 67  ASN A C    1 
ATOM   528  O  O    . ASN A 1 67  ? -10.064 2.185   4.602   1.00 13.71 ? 67  ASN A O    1 
ATOM   529  C  CB   . ASN A 1 67  ? -8.264  2.682   6.957   1.00 13.98 ? 67  ASN A CB   1 
ATOM   530  C  CG   . ASN A 1 67  ? -7.134  2.455   7.852   1.00 18.31 ? 67  ASN A CG   1 
ATOM   531  O  OD1  . ASN A 1 67  ? -6.984  1.420   8.512   1.00 16.69 ? 67  ASN A OD1  1 
ATOM   532  N  ND2  . ASN A 1 67  ? -6.212  3.426   7.856   1.00 23.94 ? 67  ASN A ND2  1 
ATOM   533  N  N    . VAL A 1 68  ? -11.424 1.683   6.329   1.00 11.09 ? 68  VAL A N    1 
ATOM   534  C  CA   . VAL A 1 68  ? -12.606 2.317   5.720   1.00 11.10 ? 68  VAL A CA   1 
ATOM   535  C  C    . VAL A 1 68  ? -12.742 3.703   6.384   1.00 15.46 ? 68  VAL A C    1 
ATOM   536  O  O    . VAL A 1 68  ? -12.924 3.764   7.633   1.00 12.46 ? 68  VAL A O    1 
ATOM   537  C  CB   . VAL A 1 68  ? -13.794 1.484   5.928   1.00 14.37 ? 68  VAL A CB   1 
ATOM   538  C  CG1  . VAL A 1 68  ? -15.183 2.207   5.468   1.00 13.40 ? 68  VAL A CG1  1 
ATOM   539  C  CG2  . VAL A 1 68  ? -13.678 0.135   5.138   1.00 14.94 ? 68  VAL A CG2  1 
ATOM   540  N  N    . GLU A 1 69  ? -12.774 4.737   5.579   1.00 16.23 ? 69  GLU A N    1 
ATOM   541  C  CA   . GLU A 1 69  ? -12.582 6.080   6.138   1.00 15.73 ? 69  GLU A CA   1 
ATOM   542  C  C    . GLU A 1 69  ? -13.894 6.798   6.042   1.00 16.69 ? 69  GLU A C    1 
ATOM   543  O  O    . GLU A 1 69  ? -14.686 6.542   5.059   1.00 16.85 ? 69  GLU A O    1 
ATOM   544  C  CB   . GLU A 1 69  ? -11.713 6.857   5.244   1.00 16.36 ? 69  GLU A CB   1 
ATOM   545  C  CG   . GLU A 1 69  ? -10.273 6.341   5.288   1.00 17.19 ? 69  GLU A CG   1 
ATOM   546  C  CD   . GLU A 1 69  ? -9.528  6.699   4.065   1.00 22.46 ? 69  GLU A CD   1 
ATOM   547  O  OE1  . GLU A 1 69  ? -10.210 7.316   3.170   1.00 18.89 ? 69  GLU A OE1  1 
ATOM   548  O  OE2  . GLU A 1 69  ? -8.312  6.379   3.990   1.00 24.08 ? 69  GLU A OE2  1 
ATOM   549  N  N    . PHE A 1 70  ? -14.168 7.653   7.009   1.00 14.18 ? 70  PHE A N    1 
ATOM   550  C  CA   . PHE A 1 70  ? -15.413 8.405   7.074   1.00 13.86 ? 70  PHE A CA   1 
ATOM   551  C  C    . PHE A 1 70  ? -15.152 9.884   7.003   1.00 14.17 ? 70  PHE A C    1 
ATOM   552  O  O    . PHE A 1 70  ? -14.083 10.373  7.369   1.00 14.49 ? 70  PHE A O    1 
ATOM   553  C  CB   . PHE A 1 70  ? -16.122 8.049   8.353   1.00 12.25 ? 70  PHE A CB   1 
ATOM   554  C  CG   . PHE A 1 70  ? -16.714 6.659   8.284   1.00 13.12 ? 70  PHE A CG   1 
ATOM   555  C  CD1  . PHE A 1 70  ? -15.928 5.542   8.487   1.00 12.02 ? 70  PHE A CD1  1 
ATOM   556  C  CD2  . PHE A 1 70  ? -18.014 6.442   7.953   1.00 11.94 ? 70  PHE A CD2  1 
ATOM   557  C  CE1  . PHE A 1 70  ? -16.477 4.239   8.340   1.00 13.35 ? 70  PHE A CE1  1 
ATOM   558  C  CE2  . PHE A 1 70  ? -18.521 5.185   7.812   1.00 11.31 ? 70  PHE A CE2  1 
ATOM   559  C  CZ   . PHE A 1 70  ? -17.713 4.038   8.013   1.00 13.74 ? 70  PHE A CZ   1 
ATOM   560  N  N    . ASP A 1 71  ? -16.162 10.601  6.462   1.00 15.31 ? 71  ASP A N    1 
ATOM   561  C  CA   . ASP A 1 71  ? -16.094 12.078  6.576   1.00 15.03 ? 71  ASP A CA   1 
ATOM   562  C  C    . ASP A 1 71  ? -16.426 12.462  8.007   1.00 14.93 ? 71  ASP A C    1 
ATOM   563  O  O    . ASP A 1 71  ? -17.529 12.257  8.445   1.00 17.83 ? 71  ASP A O    1 
ATOM   564  C  CB   . ASP A 1 71  ? -17.191 12.608  5.699   1.00 17.91 ? 71  ASP A CB   1 
ATOM   565  C  CG   . ASP A 1 71  ? -17.344 14.117  5.856   1.00 20.28 ? 71  ASP A CG   1 
ATOM   566  O  OD1  . ASP A 1 71  ? -16.465 14.753  6.462   1.00 21.01 ? 71  ASP A OD1  1 
ATOM   567  O  OD2  . ASP A 1 71  ? -18.359 14.604  5.335   1.00 29.61 ? 71  ASP A OD2  1 
ATOM   568  N  N    . ASP A 1 72  ? -15.448 12.913  8.741   1.00 11.91 ? 72  ASP A N    1 
ATOM   569  C  CA   . ASP A 1 72  ? -15.575 13.278  10.102  1.00 12.82 ? 72  ASP A CA   1 
ATOM   570  C  C    . ASP A 1 72  ? -15.557 14.823  10.254  1.00 15.48 ? 72  ASP A C    1 
ATOM   571  O  O    . ASP A 1 72  ? -15.147 15.328  11.312  1.00 16.01 ? 72  ASP A O    1 
ATOM   572  C  CB   . ASP A 1 72  ? -14.459 12.633  10.925  1.00 13.30 ? 72  ASP A CB   1 
ATOM   573  C  CG   . ASP A 1 72  ? -13.104 13.163  10.601  1.00 15.67 ? 72  ASP A CG   1 
ATOM   574  O  OD1  . ASP A 1 72  ? -12.931 13.852  9.535   1.00 16.62 ? 72  ASP A OD1  1 
ATOM   575  O  OD2  . ASP A 1 72  ? -12.149 12.832  11.301  1.00 15.89 ? 72  ASP A OD2  1 
ATOM   576  N  N    . SER A 1 73  ? -16.055 15.510  9.211   1.00 15.41 ? 73  SER A N    1 
ATOM   577  C  CA   . SER A 1 73  ? -15.991 17.004  9.328   1.00 17.53 ? 73  SER A CA   1 
ATOM   578  C  C    . SER A 1 73  ? -17.308 17.533  9.835   1.00 18.58 ? 73  SER A C    1 
ATOM   579  O  O    . SER A 1 73  ? -17.465 18.761  10.021  1.00 17.05 ? 73  SER A O    1 
ATOM   580  C  CB   . SER A 1 73  ? -15.673 17.615  7.975   1.00 19.36 ? 73  SER A CB   1 
ATOM   581  O  OG   . SER A 1 73  ? -16.729 17.392  7.112   1.00 20.03 ? 73  SER A OG   1 
ATOM   582  N  N    . GLN A 1 74  ? -18.283 16.658  10.122  1.00 19.44 ? 74  GLN A N    1 
ATOM   583  C  CA   . GLN A 1 74  ? -19.433 17.120  10.885  1.00 22.01 ? 74  GLN A CA   1 
ATOM   584  C  C    . GLN A 1 74  ? -19.796 16.089  11.893  1.00 22.81 ? 74  GLN A C    1 
ATOM   585  O  O    . GLN A 1 74  ? -19.251 14.990  11.876  1.00 18.37 ? 74  GLN A O    1 
ATOM   586  C  CB   . GLN A 1 74  ? -20.644 17.297  9.982   1.00 22.76 ? 74  GLN A CB   1 
ATOM   587  C  CG   . GLN A 1 74  ? -20.573 18.387  8.939   1.00 28.29 ? 74  GLN A CG   1 
ATOM   588  C  CD   . GLN A 1 74  ? -21.807 18.305  8.059   1.00 32.37 ? 74  GLN A CD   1 
ATOM   589  O  OE1  . GLN A 1 74  ? -22.883 18.752  8.464   1.00 40.19 ? 74  GLN A OE1  1 
ATOM   590  N  NE2  . GLN A 1 74  ? -21.675 17.738  6.871   1.00 29.91 ? 74  GLN A NE2  1 
ATOM   591  N  N    . ASP A 1 75  ? -20.784 16.433  12.716  1.00 25.02 ? 75  ASP A N    1 
ATOM   592  C  CA   . ASP A 1 75  ? -21.216 15.579  13.745  1.00 27.09 ? 75  ASP A CA   1 
ATOM   593  C  C    . ASP A 1 75  ? -22.201 14.573  13.220  1.00 26.19 ? 75  ASP A C    1 
ATOM   594  O  O    . ASP A 1 75  ? -23.448 14.832  13.198  1.00 26.46 ? 75  ASP A O    1 
ATOM   595  C  CB   . ASP A 1 75  ? -21.854 16.392  14.846  1.00 30.49 ? 75  ASP A CB   1 
ATOM   596  C  CG   . ASP A 1 75  ? -21.514 15.808  16.162  1.00 36.26 ? 75  ASP A CG   1 
ATOM   597  O  OD1  . ASP A 1 75  ? -20.265 15.819  16.519  1.00 37.85 ? 75  ASP A OD1  1 
ATOM   598  O  OD2  . ASP A 1 75  ? -22.461 15.230  16.749  1.00 39.76 ? 75  ASP A OD2  1 
ATOM   599  N  N    . LYS A 1 76  ? -21.672 13.471  12.750  1.00 22.63 ? 76  LYS A N    1 
ATOM   600  C  CA   . LYS A 1 76  ? -22.548 12.531  12.100  1.00 25.61 ? 76  LYS A CA   1 
ATOM   601  C  C    . LYS A 1 76  ? -22.551 11.281  12.977  1.00 26.76 ? 76  LYS A C    1 
ATOM   602  O  O    . LYS A 1 76  ? -23.415 11.156  13.877  1.00 31.60 ? 76  LYS A O    1 
ATOM   603  C  CB   . LYS A 1 76  ? -22.143 12.291  10.645  1.00 23.99 ? 76  LYS A CB   1 
ATOM   604  C  CG   . LYS A 1 76  ? -22.711 13.410  9.653   1.00 27.87 ? 76  LYS A CG   1 
ATOM   605  C  CD   . LYS A 1 76  ? -21.812 13.477  8.410   1.00 31.72 ? 76  LYS A CD   1 
ATOM   606  C  CE   . LYS A 1 76  ? -22.495 14.122  7.173   1.00 35.30 ? 76  LYS A CE   1 
ATOM   607  N  NZ   . LYS A 1 76  ? -21.556 14.127  6.002   1.00 34.27 ? 76  LYS A NZ   1 
ATOM   608  N  N    . ALA A 1 77  ? -21.562 10.432  12.765  1.00 22.61 ? 77  ALA A N    1 
ATOM   609  C  CA   . ALA A 1 77  ? -21.388 9.060   13.359  1.00 17.88 ? 77  ALA A CA   1 
ATOM   610  C  C    . ALA A 1 77  ? -20.633 9.225   14.717  1.00 16.36 ? 77  ALA A C    1 
ATOM   611  O  O    . ALA A 1 77  ? -19.382 9.384   14.692  1.00 20.71 ? 77  ALA A O    1 
ATOM   612  C  CB   . ALA A 1 77  ? -20.485 8.331   12.404  1.00 18.74 ? 77  ALA A CB   1 
ATOM   613  N  N    . VAL A 1 78  ? -21.323 9.211   15.815  1.00 13.17 ? 78  VAL A N    1 
ATOM   614  C  CA   . VAL A 1 78  ? -20.645 9.522   17.092  1.00 16.09 ? 78  VAL A CA   1 
ATOM   615  C  C    . VAL A 1 78  ? -20.861 8.386   18.082  1.00 13.72 ? 78  VAL A C    1 
ATOM   616  O  O    . VAL A 1 78  ? -21.917 7.710   18.176  1.00 12.95 ? 78  VAL A O    1 
ATOM   617  C  CB   . VAL A 1 78  ? -21.103 10.881  17.701  1.00 20.73 ? 78  VAL A CB   1 
ATOM   618  C  CG1  . VAL A 1 78  ? -21.000 11.964  16.730  1.00 21.99 ? 78  VAL A CG1  1 
ATOM   619  C  CG2  . VAL A 1 78  ? -22.443 10.737  18.159  1.00 20.85 ? 78  VAL A CG2  1 
ATOM   620  N  N    . LEU A 1 79  ? -19.826 8.216   18.912  1.00 12.34 ? 79  LEU A N    1 
ATOM   621  C  CA   . LEU A 1 79  ? -19.835 7.365   20.039  1.00 13.64 ? 79  LEU A CA   1 
ATOM   622  C  C    . LEU A 1 79  ? -19.797 8.252   21.262  1.00 12.64 ? 79  LEU A C    1 
ATOM   623  O  O    . LEU A 1 79  ? -18.992 9.200   21.383  1.00 13.51 ? 79  LEU A O    1 
ATOM   624  C  CB   . LEU A 1 79  ? -18.556 6.458   19.954  1.00 13.74 ? 79  LEU A CB   1 
ATOM   625  C  CG   . LEU A 1 79  ? -18.414 5.448   21.049  1.00 13.17 ? 79  LEU A CG   1 
ATOM   626  C  CD1  . LEU A 1 79  ? -19.550 4.413   20.901  1.00 18.51 ? 79  LEU A CD1  1 
ATOM   627  C  CD2  . LEU A 1 79  ? -17.082 4.850   20.965  1.00 12.93 ? 79  LEU A CD2  1 
ATOM   628  N  N    . LYS A 1 80  ? -20.656 7.958   22.190  1.00 13.18 ? 80  LYS A N    1 
ATOM   629  C  CA   . LYS A 1 80  ? -20.699 8.638   23.494  1.00 13.04 ? 80  LYS A CA   1 
ATOM   630  C  C    . LYS A 1 80  ? -21.252 7.696   24.555  1.00 13.06 ? 80  LYS A C    1 
ATOM   631  O  O    . LYS A 1 80  ? -21.521 6.512   24.317  1.00 12.26 ? 80  LYS A O    1 
ATOM   632  C  CB   . LYS A 1 80  ? -21.418 9.976   23.442  1.00 16.74 ? 80  LYS A CB   1 
ATOM   633  C  CG   . LYS A 1 80  ? -22.896 9.734   23.192  1.00 19.85 ? 80  LYS A CG   1 
ATOM   634  C  CD   . LYS A 1 80  ? -23.708 11.139  23.213  0.01 18.42 ? 80  LYS A CD   1 
ATOM   635  C  CE   . LYS A 1 80  ? -23.806 11.705  24.456  0.01 18.77 ? 80  LYS A CE   1 
ATOM   636  N  NZ   . LYS A 1 80  ? -24.302 13.114  24.363  0.01 19.00 ? 80  LYS A NZ   1 
ATOM   637  N  N    . GLY A 1 81  ? -21.321 8.213   25.775  1.00 13.80 ? 81  GLY A N    1 
ATOM   638  C  CA   . GLY A 1 81  ? -21.853 7.402   26.833  1.00 13.61 ? 81  GLY A CA   1 
ATOM   639  C  C    . GLY A 1 81  ? -20.877 6.317   27.212  1.00 15.74 ? 81  GLY A C    1 
ATOM   640  O  O    . GLY A 1 81  ? -19.662 6.521   27.026  1.00 15.52 ? 81  GLY A O    1 
ATOM   641  N  N    . GLY A 1 82  ? -21.360 5.186   27.698  1.00 17.53 ? 82  GLY A N    1 
ATOM   642  C  CA   . GLY A 1 82  ? -20.388 4.125   28.089  1.00 18.27 ? 82  GLY A CA   1 
ATOM   643  C  C    . GLY A 1 82  ? -19.499 4.777   29.186  1.00 17.41 ? 82  GLY A C    1 
ATOM   644  O  O    . GLY A 1 82  ? -19.969 5.527   30.074  1.00 19.73 ? 82  GLY A O    1 
ATOM   645  N  N    . PRO A 1 83  ? -18.151 4.575   29.156  1.00 16.43 ? 83  PRO A N    1 
ATOM   646  C  CA   . PRO A 1 83  ? -17.203 5.203   30.038  1.00 13.01 ? 83  PRO A CA   1 
ATOM   647  C  C    . PRO A 1 83  ? -16.746 6.627   29.637  1.00 15.24 ? 83  PRO A C    1 
ATOM   648  O  O    . PRO A 1 83  ? -15.993 7.238   30.352  1.00 16.49 ? 83  PRO A O    1 
ATOM   649  C  CB   . PRO A 1 83  ? -15.986 4.198   29.974  1.00 15.87 ? 83  PRO A CB   1 
ATOM   650  C  CG   . PRO A 1 83  ? -15.955 3.944   28.517  1.00 12.25 ? 83  PRO A CG   1 
ATOM   651  C  CD   . PRO A 1 83  ? -17.480 3.717   28.137  1.00 13.61 ? 83  PRO A CD   1 
ATOM   652  N  N    . LEU A 1 84  ? -17.292 7.170   28.558  1.00 13.94 ? 84  LEU A N    1 
ATOM   653  C  CA   . LEU A 1 84  ? -16.766 8.375   27.895  1.00 12.92 ? 84  LEU A CA   1 
ATOM   654  C  C    . LEU A 1 84  ? -17.384 9.608   28.528  1.00 16.06 ? 84  LEU A C    1 
ATOM   655  O  O    . LEU A 1 84  ? -18.593 9.593   28.813  1.00 16.68 ? 84  LEU A O    1 
ATOM   656  C  CB   . LEU A 1 84  ? -16.977 8.314   26.395  1.00 11.78 ? 84  LEU A CB   1 
ATOM   657  C  CG   . LEU A 1 84  ? -16.454 7.024   25.707  1.00 9.96  ? 84  LEU A CG   1 
ATOM   658  C  CD1  . LEU A 1 84  ? -16.911 6.997   24.342  1.00 10.78 ? 84  LEU A CD1  1 
ATOM   659  C  CD2  . LEU A 1 84  ? -14.857 7.010   25.847  1.00 11.75 ? 84  LEU A CD2  1 
ATOM   660  N  N    . ASP A 1 85  ? -16.566 10.631  28.561  1.00 17.13 ? 85  ASP A N    1 
ATOM   661  C  CA   . ASP A 1 85  ? -17.010 11.960  28.972  1.00 21.59 ? 85  ASP A CA   1 
ATOM   662  C  C    . ASP A 1 85  ? -17.387 12.881  27.913  1.00 24.81 ? 85  ASP A C    1 
ATOM   663  O  O    . ASP A 1 85  ? -17.953 13.966  28.222  1.00 28.18 ? 85  ASP A O    1 
ATOM   664  C  CB   . ASP A 1 85  ? -15.966 12.634  29.878  1.00 21.06 ? 85  ASP A CB   1 
ATOM   665  C  CG   . ASP A 1 85  ? -16.163 12.244  31.282  1.00 29.92 ? 85  ASP A CG   1 
ATOM   666  O  OD1  . ASP A 1 85  ? -17.339 11.829  31.535  1.00 31.78 ? 85  ASP A OD1  1 
ATOM   667  O  OD2  . ASP A 1 85  ? -15.189 12.383  32.092  1.00 29.88 ? 85  ASP A OD2  1 
ATOM   668  N  N    . GLY A 1 86  ? -17.076 12.658  26.675  1.00 24.00 ? 86  GLY A N    1 
ATOM   669  C  CA   . GLY A 1 86  ? -17.823 13.641  25.857  1.00 22.46 ? 86  GLY A CA   1 
ATOM   670  C  C    . GLY A 1 86  ? -18.331 12.958  24.605  1.00 20.89 ? 86  GLY A C    1 
ATOM   671  O  O    . GLY A 1 86  ? -19.007 11.952  24.720  1.00 23.28 ? 86  GLY A O    1 
ATOM   672  N  N    A THR A 1 87  ? -18.049 13.519  23.427  0.50 17.98 ? 87  THR A N    1 
ATOM   673  N  N    B THR A 1 87  ? -17.940 13.438  23.439  0.50 16.60 ? 87  THR A N    1 
ATOM   674  C  CA   A THR A 1 87  ? -18.537 12.963  22.164  0.50 16.81 ? 87  THR A CA   1 
ATOM   675  C  CA   B THR A 1 87  ? -18.443 12.838  22.232  0.50 14.26 ? 87  THR A CA   1 
ATOM   676  C  C    A THR A 1 87  ? -17.282 12.613  21.380  0.50 13.87 ? 87  THR A C    1 
ATOM   677  C  C    B THR A 1 87  ? -17.301 12.670  21.238  0.50 12.29 ? 87  THR A C    1 
ATOM   678  O  O    A THR A 1 87  ? -16.314 13.357  21.410  0.50 11.68 ? 87  THR A O    1 
ATOM   679  O  O    B THR A 1 87  ? -16.466 13.581  20.949  0.50 10.92 ? 87  THR A O    1 
ATOM   680  C  CB   A THR A 1 87  ? -19.354 14.032  21.327  0.50 17.59 ? 87  THR A CB   1 
ATOM   681  C  CB   B THR A 1 87  ? -19.494 13.727  21.582  0.50 14.29 ? 87  THR A CB   1 
ATOM   682  O  OG1  A THR A 1 87  ? -20.591 14.383  21.979  0.50 19.31 ? 87  THR A OG1  1 
ATOM   683  O  OG1  B THR A 1 87  ? -18.910 15.020  21.408  0.50 12.26 ? 87  THR A OG1  1 
ATOM   684  C  CG2  A THR A 1 87  ? -19.639 13.523  19.911  0.50 19.04 ? 87  THR A CG2  1 
ATOM   685  C  CG2  B THR A 1 87  ? -20.798 13.859  22.470  0.50 14.96 ? 87  THR A CG2  1 
ATOM   686  N  N    . TYR A 1 88  ? -17.323 11.447  20.731  1.00 11.86 ? 88  TYR A N    1 
ATOM   687  C  CA   . TYR A 1 88  ? -16.200 11.041  19.901  1.00 10.58 ? 88  TYR A CA   1 
ATOM   688  C  C    . TYR A 1 88  ? -16.678 10.740  18.514  1.00 10.36 ? 88  TYR A C    1 
ATOM   689  O  O    . TYR A 1 88  ? -17.708 10.024  18.404  1.00 13.21 ? 88  TYR A O    1 
ATOM   690  C  CB   . TYR A 1 88  ? -15.564 9.761   20.467  1.00 10.00 ? 88  TYR A CB   1 
ATOM   691  C  CG   . TYR A 1 88  ? -14.818 9.956   21.777  1.00 8.39  ? 88  TYR A CG   1 
ATOM   692  C  CD1  . TYR A 1 88  ? -15.483 10.313  22.880  1.00 9.99  ? 88  TYR A CD1  1 
ATOM   693  C  CD2  . TYR A 1 88  ? -13.402 9.788   21.844  1.00 8.48  ? 88  TYR A CD2  1 
ATOM   694  C  CE1  . TYR A 1 88  ? -14.778 10.518  24.117  1.00 9.31  ? 88  TYR A CE1  1 
ATOM   695  C  CE2  . TYR A 1 88  ? -12.734 9.972   23.049  1.00 6.63  ? 88  TYR A CE2  1 
ATOM   696  C  CZ   . TYR A 1 88  ? -13.379 10.280  24.138  1.00 9.15  ? 88  TYR A CZ   1 
ATOM   697  O  OH   . TYR A 1 88  ? -12.707 10.355  25.319  1.00 9.99  ? 88  TYR A OH   1 
ATOM   698  N  N    . ARG A 1 89  ? -16.019 11.197  17.494  1.00 10.10 ? 89  ARG A N    1 
ATOM   699  C  CA   . ARG A 1 89  ? -16.510 11.092  16.110  1.00 10.88 ? 89  ARG A CA   1 
ATOM   700  C  C    . ARG A 1 89  ? -15.790 9.962   15.407  1.00 8.53  ? 89  ARG A C    1 
ATOM   701  O  O    . ARG A 1 89  ? -14.534 9.875   15.396  1.00 8.73  ? 89  ARG A O    1 
ATOM   702  C  CB   . ARG A 1 89  ? -16.226 12.400  15.400  1.00 12.46 ? 89  ARG A CB   1 
ATOM   703  C  CG   . ARG A 1 89  ? -16.971 12.500  14.156  1.00 16.64 ? 89  ARG A CG   1 
ATOM   704  C  CD   . ARG A 1 89  ? -16.866 13.990  13.651  1.00 17.24 ? 89  ARG A CD   1 
ATOM   705  N  NE   . ARG A 1 89  ? -17.551 14.950  14.519  1.00 15.85 ? 89  ARG A NE   1 
ATOM   706  C  CZ   . ARG A 1 89  ? -17.383 16.266  14.372  1.00 16.19 ? 89  ARG A CZ   1 
ATOM   707  N  NH1  . ARG A 1 89  ? -16.637 16.769  13.410  1.00 17.14 ? 89  ARG A NH1  1 
ATOM   708  N  NH2  . ARG A 1 89  ? -18.041 17.093  15.162  1.00 20.23 ? 89  ARG A NH2  1 
ATOM   709  N  N    . LEU A 1 90  ? -16.539 9.153   14.653  1.00 8.82  ? 90  LEU A N    1 
ATOM   710  C  CA   . LEU A 1 90  ? -15.922 8.089   13.890  1.00 8.55  ? 90  LEU A CA   1 
ATOM   711  C  C    . LEU A 1 90  ? -15.078 8.610   12.762  1.00 9.30  ? 90  LEU A C    1 
ATOM   712  O  O    . LEU A 1 90  ? -15.593 9.478   11.949  1.00 11.37 ? 90  LEU A O    1 
ATOM   713  C  CB   . LEU A 1 90  ? -17.072 7.190   13.295  1.00 8.68  ? 90  LEU A CB   1 
ATOM   714  C  CG   . LEU A 1 90  ? -16.632 6.070   12.423  1.00 9.73  ? 90  LEU A CG   1 
ATOM   715  C  CD1  . LEU A 1 90  ? -15.868 4.973   13.210  1.00 11.55 ? 90  LEU A CD1  1 
ATOM   716  C  CD2  . LEU A 1 90  ? -17.868 5.380   11.841  1.00 11.94 ? 90  LEU A CD2  1 
ATOM   717  N  N    . ILE A 1 91  ? -13.837 8.187   12.647  1.00 8.24  ? 91  ILE A N    1 
ATOM   718  C  CA   . ILE A 1 91  ? -12.977 8.540   11.566  1.00 9.39  ? 91  ILE A CA   1 
ATOM   719  C  C    . ILE A 1 91  ? -12.673 7.382   10.651  1.00 10.44 ? 91  ILE A C    1 
ATOM   720  O  O    . ILE A 1 91  ? -12.574 7.538   9.428   1.00 9.31  ? 91  ILE A O    1 
ATOM   721  C  CB   . ILE A 1 91  ? -11.653 9.205   12.061  1.00 8.77  ? 91  ILE A CB   1 
ATOM   722  C  CG1  . ILE A 1 91  ? -10.833 9.593   10.849  1.00 10.73 ? 91  ILE A CG1  1 
ATOM   723  C  CG2  . ILE A 1 91  ? -10.946 8.370   13.019  1.00 11.64 ? 91  ILE A CG2  1 
ATOM   724  C  CD1  . ILE A 1 91  ? -9.655  10.579  11.200  1.00 13.14 ? 91  ILE A CD1  1 
ATOM   725  N  N    . GLN A 1 92  ? -12.516 6.151   11.201  1.00 8.76  ? 92  GLN A N    1 
ATOM   726  C  CA   . GLN A 1 92  ? -12.212 5.025   10.293  1.00 9.26  ? 92  GLN A CA   1 
ATOM   727  C  C    . GLN A 1 92  ? -12.474 3.745   11.040  1.00 8.75  ? 92  GLN A C    1 
ATOM   728  O  O    . GLN A 1 92  ? -12.595 3.798   12.216  1.00 8.12  ? 92  GLN A O    1 
ATOM   729  C  CB   . GLN A 1 92  ? -10.795 5.046   9.748   1.00 10.66 ? 92  GLN A CB   1 
ATOM   730  C  CG   . GLN A 1 92  ? -9.703  5.078   10.891  1.00 11.60 ? 92  GLN A CG   1 
ATOM   731  C  CD   . GLN A 1 92  ? -8.965  3.774   11.050  1.00 12.06 ? 92  GLN A CD   1 
ATOM   732  O  OE1  . GLN A 1 92  ? -9.602  2.731   11.184  1.00 9.97  ? 92  GLN A OE1  1 
ATOM   733  N  NE2  . GLN A 1 92  ? -7.694  3.789   11.015  1.00 17.26 ? 92  GLN A NE2  1 
ATOM   734  N  N    . PHE A 1 93  ? -12.690 2.625   10.306  1.00 8.38  ? 93  PHE A N    1 
ATOM   735  C  CA   . PHE A 1 93  ? -12.500 1.297   10.896  1.00 8.87  ? 93  PHE A CA   1 
ATOM   736  C  C    . PHE A 1 93  ? -11.588 0.494   10.109  1.00 7.29  ? 93  PHE A C    1 
ATOM   737  O  O    . PHE A 1 93  ? -11.337 0.694   8.963   1.00 9.02  ? 93  PHE A O    1 
ATOM   738  C  CB   . PHE A 1 93  ? -13.782 0.623   11.159  1.00 9.51  ? 93  PHE A CB   1 
ATOM   739  C  CG   . PHE A 1 93  ? -14.572 0.184   9.944   1.00 12.30 ? 93  PHE A CG   1 
ATOM   740  C  CD1  . PHE A 1 93  ? -14.222 -1.005  9.266   1.00 12.19 ? 93  PHE A CD1  1 
ATOM   741  C  CD2  . PHE A 1 93  ? -15.660 0.962   9.482   1.00 11.31 ? 93  PHE A CD2  1 
ATOM   742  C  CE1  . PHE A 1 93  ? -14.952 -1.435  8.120   1.00 12.66 ? 93  PHE A CE1  1 
ATOM   743  C  CE2  . PHE A 1 93  ? -16.407 0.485   8.365   1.00 12.97 ? 93  PHE A CE2  1 
ATOM   744  C  CZ   . PHE A 1 93  ? -16.085 -0.709  7.717   1.00 12.10 ? 93  PHE A CZ   1 
ATOM   745  N  N    . HIS A 1 94  ? -11.029 -0.520  10.804  1.00 7.53  ? 94  HIS A N    1 
ATOM   746  C  CA   . HIS A 1 94  ? -10.148 -1.511  10.173  1.00 7.15  ? 94  HIS A CA   1 
ATOM   747  C  C    . HIS A 1 94  ? -10.204 -2.795  11.038  1.00 6.18  ? 94  HIS A C    1 
ATOM   748  O  O    . HIS A 1 94  ? -10.861 -2.806  12.069  1.00 6.64  ? 94  HIS A O    1 
ATOM   749  C  CB   . HIS A 1 94  ? -8.687  -1.061  10.127  1.00 8.04  ? 94  HIS A CB   1 
ATOM   750  C  CG   . HIS A 1 94  ? -8.143  -0.755  11.496  1.00 8.55  ? 94  HIS A CG   1 
ATOM   751  N  ND1  . HIS A 1 94  ? -8.320  0.475   12.123  1.00 7.75  ? 94  HIS A ND1  1 
ATOM   752  C  CD2  . HIS A 1 94  ? -7.549  -1.577  12.385  1.00 8.17  ? 94  HIS A CD2  1 
ATOM   753  C  CE1  . HIS A 1 94  ? -7.823  0.371   13.353  1.00 6.73  ? 94  HIS A CE1  1 
ATOM   754  N  NE2  . HIS A 1 94  ? -7.373  -0.867  13.545  1.00 7.52  ? 94  HIS A NE2  1 
ATOM   755  N  N    . PHE A 1 95  ? -9.532  -3.829  10.516  1.00 7.98  ? 95  PHE A N    1 
ATOM   756  C  CA   . PHE A 1 95  ? -9.535  -5.078  11.229  1.00 8.10  ? 95  PHE A CA   1 
ATOM   757  C  C    . PHE A 1 95  ? -8.091  -5.549  11.399  1.00 7.70  ? 95  PHE A C    1 
ATOM   758  O  O    . PHE A 1 95  ? -7.162  -5.061  10.768  1.00 8.16  ? 95  PHE A O    1 
ATOM   759  C  CB   . PHE A 1 95  ? -10.223 -6.189  10.378  1.00 7.39  ? 95  PHE A CB   1 
ATOM   760  C  CG   . PHE A 1 95  ? -11.660 -5.870  10.066  1.00 6.75  ? 95  PHE A CG   1 
ATOM   761  C  CD1  . PHE A 1 95  ? -12.018 -5.025  9.003   1.00 8.91  ? 95  PHE A CD1  1 
ATOM   762  C  CD2  . PHE A 1 95  ? -12.670 -6.521  10.691  1.00 8.32  ? 95  PHE A CD2  1 
ATOM   763  C  CE1  . PHE A 1 95  ? -13.375 -4.816  8.652   1.00 8.92  ? 95  PHE A CE1  1 
ATOM   764  C  CE2  . PHE A 1 95  ? -14.002 -6.281  10.390  1.00 10.44 ? 95  PHE A CE2  1 
ATOM   765  C  CZ   . PHE A 1 95  ? -14.348 -5.438  9.350   1.00 9.23  ? 95  PHE A CZ   1 
ATOM   766  N  N    . HIS A 1 96  ? -7.943  -6.487  12.321  1.00 7.29  ? 96  HIS A N    1 
ATOM   767  C  CA   . HIS A 1 96  ? -6.754  -7.315  12.492  1.00 7.10  ? 96  HIS A CA   1 
ATOM   768  C  C    . HIS A 1 96  ? -7.155  -8.768  12.369  1.00 7.54  ? 96  HIS A C    1 
ATOM   769  O  O    . HIS A 1 96  ? -8.202  -9.117  12.868  1.00 7.34  ? 96  HIS A O    1 
ATOM   770  C  CB   . HIS A 1 96  ? -6.050  -7.071  13.897  1.00 6.51  ? 96  HIS A CB   1 
ATOM   771  C  CG   . HIS A 1 96  ? -5.788  -5.642  14.150  1.00 5.84  ? 96  HIS A CG   1 
ATOM   772  N  ND1  . HIS A 1 96  ? -4.530  -5.094  13.926  1.00 7.88  ? 96  HIS A ND1  1 
ATOM   773  C  CD2  . HIS A 1 96  ? -6.622  -4.622  14.514  1.00 8.39  ? 96  HIS A CD2  1 
ATOM   774  C  CE1  . HIS A 1 96  ? -4.607  -3.804  14.289  1.00 9.83  ? 96  HIS A CE1  1 
ATOM   775  N  NE2  . HIS A 1 96  ? -5.866  -3.510  14.566  1.00 7.80  ? 96  HIS A NE2  1 
ATOM   776  N  N    . TRP A 1 97  ? -6.347  -9.559  11.698  1.00 6.93  ? 97  TRP A N    1 
ATOM   777  C  CA   . TRP A 1 97  ? -6.776  -10.951 11.522  1.00 7.52  ? 97  TRP A CA   1 
ATOM   778  C  C    . TRP A 1 97  ? -5.587  -11.926 11.378  1.00 7.42  ? 97  TRP A C    1 
ATOM   779  O  O    . TRP A 1 97  ? -4.402  -11.493 11.268  1.00 8.62  ? 97  TRP A O    1 
ATOM   780  C  CB   . TRP A 1 97  ? -7.687  -11.081 10.257  1.00 8.05  ? 97  TRP A CB   1 
ATOM   781  C  CG   . TRP A 1 97  ? -7.055  -10.704 8.968   1.00 8.03  ? 97  TRP A CG   1 
ATOM   782  C  CD1  . TRP A 1 97  ? -6.325  -11.522 8.138   1.00 9.04  ? 97  TRP A CD1  1 
ATOM   783  C  CD2  . TRP A 1 97  ? -6.998  -9.386  8.416   1.00 7.69  ? 97  TRP A CD2  1 
ATOM   784  N  NE1  . TRP A 1 97  ? -5.909  -10.808 7.015   1.00 9.31  ? 97  TRP A NE1  1 
ATOM   785  C  CE2  . TRP A 1 97  ? -6.255  -9.466  7.193   1.00 7.86  ? 97  TRP A CE2  1 
ATOM   786  C  CE3  . TRP A 1 97  ? -7.509  -8.118  8.830   1.00 8.77  ? 97  TRP A CE3  1 
ATOM   787  C  CZ2  . TRP A 1 97  ? -6.053  -8.367  6.386   1.00 9.26  ? 97  TRP A CZ2  1 
ATOM   788  C  CZ3  . TRP A 1 97  ? -7.264  -7.030  8.015   1.00 9.46  ? 97  TRP A CZ3  1 
ATOM   789  C  CH2  . TRP A 1 97  ? -6.555  -7.162  6.786   1.00 8.60  ? 97  TRP A CH2  1 
ATOM   790  N  N    . GLY A 1 98  ? -5.866  -13.200 11.394  1.00 7.74  ? 98  GLY A N    1 
ATOM   791  C  CA   . GLY A 1 98  ? -4.810  -14.135 11.412  1.00 8.21  ? 98  GLY A CA   1 
ATOM   792  C  C    . GLY A 1 98  ? -4.617  -14.908 10.092  1.00 8.55  ? 98  GLY A C    1 
ATOM   793  O  O    . GLY A 1 98  ? -5.371  -14.722 9.144   1.00 9.34  ? 98  GLY A O    1 
ATOM   794  N  N    . SER A 1 99  ? -3.592  -15.758 10.111  1.00 9.99  ? 99  SER A N    1 
ATOM   795  C  CA   . SER A 1 99  ? -3.382  -16.752 9.026   1.00 9.84  ? 99  SER A CA   1 
ATOM   796  C  C    . SER A 1 99  ? -4.251  -17.936 9.156   1.00 12.19 ? 99  SER A C    1 
ATOM   797  O  O    . SER A 1 99  ? -4.382  -18.626 8.144   1.00 14.57 ? 99  SER A O    1 
ATOM   798  C  CB   . SER A 1 99  ? -1.912  -17.135 9.033   1.00 12.39 ? 99  SER A CB   1 
ATOM   799  O  OG   . SER A 1 99  ? -1.469  -17.586 10.244  1.00 12.97 ? 99  SER A OG   1 
ATOM   800  N  N    . LEU A 1 100 ? -4.861  -18.161 10.321  1.00 10.21 ? 100 LEU A N    1 
ATOM   801  C  CA   . LEU A 1 100 ? -5.628  -19.299 10.621  1.00 12.87 ? 100 LEU A CA   1 
ATOM   802  C  C    . LEU A 1 100 ? -6.811  -18.808 11.454  1.00 12.98 ? 100 LEU A C    1 
ATOM   803  O  O    . LEU A 1 100 ? -6.643  -17.821 12.210  1.00 11.96 ? 100 LEU A O    1 
ATOM   804  C  CB   . LEU A 1 100 ? -4.764  -20.222 11.541  1.00 15.84 ? 100 LEU A CB   1 
ATOM   805  C  CG   . LEU A 1 100 ? -3.437  -20.626 10.993  1.00 19.29 ? 100 LEU A CG   1 
ATOM   806  C  CD1  . LEU A 1 100 ? -2.407  -20.788 12.161  1.00 22.78 ? 100 LEU A CD1  1 
ATOM   807  C  CD2  . LEU A 1 100 ? -3.627  -21.869 10.109  1.00 23.83 ? 100 LEU A CD2  1 
ATOM   808  N  N    . ASP A 1 101 ? -7.912  -19.573 11.509  1.00 11.48 ? 101 ASP A N    1 
ATOM   809  C  CA   . ASP A 1 101 ? -9.088  -19.083 12.279  1.00 12.20 ? 101 ASP A CA   1 
ATOM   810  C  C    . ASP A 1 101 ? -8.777  -19.003 13.759  1.00 11.18 ? 101 ASP A C    1 
ATOM   811  O  O    . ASP A 1 101 ? -9.505  -18.326 14.456  1.00 12.84 ? 101 ASP A O    1 
ATOM   812  C  CB   . ASP A 1 101 ? -10.323 -19.975 12.024  1.00 10.74 ? 101 ASP A CB   1 
ATOM   813  C  CG   . ASP A 1 101 ? -10.763 -19.964 10.609  1.00 17.78 ? 101 ASP A CG   1 
ATOM   814  O  OD1  . ASP A 1 101 ? -10.396 -19.149 9.725   1.00 15.35 ? 101 ASP A OD1  1 
ATOM   815  O  OD2  . ASP A 1 101 ? -11.633 -20.811 10.350  1.00 19.76 ? 101 ASP A OD2  1 
ATOM   816  N  N    . GLY A 1 102 ? -7.783  -19.767 14.268  1.00 10.89 ? 102 GLY A N    1 
ATOM   817  C  CA   . GLY A 1 102 ? -7.442  -19.764 15.684  1.00 10.96 ? 102 GLY A CA   1 
ATOM   818  C  C    . GLY A 1 102 ? -6.639  -18.597 16.236  1.00 10.25 ? 102 GLY A C    1 
ATOM   819  O  O    . GLY A 1 102 ? -6.319  -18.574 17.421  1.00 11.99 ? 102 GLY A O    1 
ATOM   820  N  N    . GLN A 1 103 ? -6.383  -17.587 15.406  1.00 10.07 ? 103 GLN A N    1 
ATOM   821  C  CA   . GLN A 1 103 ? -5.654  -16.404 15.898  1.00 8.41  ? 103 GLN A CA   1 
ATOM   822  C  C    . GLN A 1 103 ? -6.053  -15.264 15.036  1.00 5.83  ? 103 GLN A C    1 
ATOM   823  O  O    . GLN A 1 103 ? -6.584  -15.462 13.982  1.00 9.33  ? 103 GLN A O    1 
ATOM   824  C  CB   . GLN A 1 103 ? -4.118  -16.652 15.933  1.00 10.03 ? 103 GLN A CB   1 
ATOM   825  C  CG   . GLN A 1 103 ? -3.597  -16.900 14.484  1.00 12.21 ? 103 GLN A CG   1 
ATOM   826  C  CD   . GLN A 1 103 ? -2.113  -17.353 14.586  1.00 16.85 ? 103 GLN A CD   1 
ATOM   827  O  OE1  . GLN A 1 103 ? -1.838  -18.172 15.479  1.00 22.34 ? 103 GLN A OE1  1 
ATOM   828  N  NE2  . GLN A 1 103 ? -1.221  -16.904 13.754  1.00 16.15 ? 103 GLN A NE2  1 
ATOM   829  N  N    . GLY A 1 104 ? -5.728  -14.017 15.492  1.00 7.62  ? 104 GLY A N    1 
ATOM   830  C  CA   . GLY A 1 104 ? -5.991  -12.836 14.679  1.00 7.46  ? 104 GLY A CA   1 
ATOM   831  C  C    . GLY A 1 104 ? -6.444  -11.672 15.523  1.00 7.43  ? 104 GLY A C    1 
ATOM   832  O  O    . GLY A 1 104 ? -6.167  -10.526 15.189  1.00 8.16  ? 104 GLY A O    1 
ATOM   833  N  N    . SER A 1 105 ? -7.183  -11.944 16.627  1.00 6.09  ? 105 SER A N    1 
ATOM   834  C  CA   . SER A 1 105 ? -7.587  -10.820 17.454  1.00 7.22  ? 105 SER A CA   1 
ATOM   835  C  C    . SER A 1 105 ? -6.347  -10.247 18.180  1.00 6.46  ? 105 SER A C    1 
ATOM   836  O  O    . SER A 1 105 ? -5.309  -10.988 18.411  1.00 7.70  ? 105 SER A O    1 
ATOM   837  C  CB   . SER A 1 105 ? -8.700  -11.172 18.417  1.00 7.82  ? 105 SER A CB   1 
ATOM   838  O  OG   . SER A 1 105 ? -8.290  -12.108 19.346  1.00 7.73  ? 105 SER A OG   1 
ATOM   839  N  N    . GLU A 1 106 ? -6.488  -9.020  18.569  1.00 6.18  ? 106 GLU A N    1 
ATOM   840  C  CA   . GLU A 1 106 ? -5.416  -8.371  19.421  1.00 6.50  ? 106 GLU A CA   1 
ATOM   841  C  C    . GLU A 1 106 ? -5.783  -8.504  20.893  1.00 7.68  ? 106 GLU A C    1 
ATOM   842  O  O    . GLU A 1 106 ? -5.004  -9.079  21.689  1.00 7.13  ? 106 GLU A O    1 
ATOM   843  C  CB   . GLU A 1 106 ? -5.396  -6.862  19.016  1.00 7.22  ? 106 GLU A CB   1 
ATOM   844  C  CG   . GLU A 1 106 ? -4.904  -6.764  17.580  1.00 9.03  ? 106 GLU A CG   1 
ATOM   845  C  CD   . GLU A 1 106 ? -4.278  -5.433  17.259  1.00 9.36  ? 106 GLU A CD   1 
ATOM   846  O  OE1  . GLU A 1 106 ? -4.871  -4.396  17.536  1.00 8.41  ? 106 GLU A OE1  1 
ATOM   847  O  OE2  . GLU A 1 106 ? -3.112  -5.488  16.789  1.00 10.02 ? 106 GLU A OE2  1 
ATOM   848  N  N    . HIS A 1 107 ? -7.007  -8.109  21.295  1.00 6.11  ? 107 HIS A N    1 
ATOM   849  C  CA   . HIS A 1 107 ? -7.447  -8.431  22.638  1.00 5.56  ? 107 HIS A CA   1 
ATOM   850  C  C    . HIS A 1 107 ? -7.763  -9.945  22.630  1.00 6.08  ? 107 HIS A C    1 
ATOM   851  O  O    . HIS A 1 107 ? -8.067  -10.577 21.605  1.00 6.65  ? 107 HIS A O    1 
ATOM   852  C  CB   . HIS A 1 107 ? -8.669  -7.651  23.071  1.00 6.68  ? 107 HIS A CB   1 
ATOM   853  C  CG   . HIS A 1 107 ? -8.351  -6.218  23.189  1.00 5.78  ? 107 HIS A CG   1 
ATOM   854  N  ND1  . HIS A 1 107 ? -8.418  -5.328  22.137  1.00 7.70  ? 107 HIS A ND1  1 
ATOM   855  C  CD2  . HIS A 1 107 ? -7.920  -5.506  24.230  1.00 6.02  ? 107 HIS A CD2  1 
ATOM   856  C  CE1  . HIS A 1 107 ? -7.970  -4.123  22.527  1.00 6.76  ? 107 HIS A CE1  1 
ATOM   857  N  NE2  . HIS A 1 107 ? -7.705  -4.213  23.827  1.00 7.34  ? 107 HIS A NE2  1 
ATOM   858  N  N    . THR A 1 108 ? -7.602  -10.480 23.817  1.00 7.04  ? 108 THR A N    1 
ATOM   859  C  CA   . THR A 1 108 ? -7.975  -11.859 24.081  1.00 7.04  ? 108 THR A CA   1 
ATOM   860  C  C    . THR A 1 108 ? -8.904  -11.884 25.280  1.00 7.14  ? 108 THR A C    1 
ATOM   861  O  O    . THR A 1 108 ? -8.986  -10.927 26.037  1.00 8.69  ? 108 THR A O    1 
ATOM   862  C  CB   . THR A 1 108 ? -6.771  -12.805 24.280  1.00 8.19  ? 108 THR A CB   1 
ATOM   863  O  OG1  . THR A 1 108 ? -5.895  -12.315 25.341  1.00 8.54  ? 108 THR A OG1  1 
ATOM   864  C  CG2  . THR A 1 108 ? -5.946  -12.832 23.067  1.00 7.64  ? 108 THR A CG2  1 
ATOM   865  N  N    . VAL A 1 109 ? -9.669  -12.950 25.383  1.00 7.37  ? 109 VAL A N    1 
ATOM   866  C  CA   . VAL A 1 109 ? -10.696 -13.049 26.513  1.00 7.66  ? 109 VAL A CA   1 
ATOM   867  C  C    . VAL A 1 109 ? -10.365 -14.382 27.218  1.00 9.99  ? 109 VAL A C    1 
ATOM   868  O  O    . VAL A 1 109 ? -10.505 -15.436 26.635  1.00 9.13  ? 109 VAL A O    1 
ATOM   869  C  CB   . VAL A 1 109 ? -12.112 -13.089 25.894  1.00 11.59 ? 109 VAL A CB   1 
ATOM   870  C  CG1  . VAL A 1 109 ? -13.233 -13.190 27.004  1.00 11.51 ? 109 VAL A CG1  1 
ATOM   871  C  CG2  . VAL A 1 109 ? -12.439 -11.817 25.054  1.00 10.56 ? 109 VAL A CG2  1 
ATOM   872  N  N    . ASP A 1 110 ? -9.916  -14.209 28.453  1.00 9.28  ? 110 ASP A N    1 
ATOM   873  C  CA   . ASP A 1 110 ? -9.387  -15.428 29.125  1.00 10.85 ? 110 ASP A CA   1 
ATOM   874  C  C    . ASP A 1 110 ? -8.487  -16.254 28.263  1.00 10.29 ? 110 ASP A C    1 
ATOM   875  O  O    . ASP A 1 110 ? -8.511  -17.472 28.226  1.00 11.81 ? 110 ASP A O    1 
ATOM   876  C  CB   . ASP A 1 110 ? -10.571 -16.249 29.640  1.00 11.85 ? 110 ASP A CB   1 
ATOM   877  C  CG   . ASP A 1 110 ? -11.467 -15.420 30.690  1.00 12.61 ? 110 ASP A CG   1 
ATOM   878  O  OD1  . ASP A 1 110 ? -10.852 -14.609 31.360  1.00 15.11 ? 110 ASP A OD1  1 
ATOM   879  O  OD2  . ASP A 1 110 ? -12.661 -15.730 30.738  1.00 17.59 ? 110 ASP A OD2  1 
ATOM   880  N  N    . LYS A 1 111 ? -7.560  -15.532 27.629  1.00 9.39  ? 111 LYS A N    1 
ATOM   881  C  CA   . LYS A 1 111 ? -6.522  -16.041 26.715  1.00 11.73 ? 111 LYS A CA   1 
ATOM   882  C  C    . LYS A 1 111 ? -7.074  -16.590 25.401  1.00 10.84 ? 111 LYS A C    1 
ATOM   883  O  O    . LYS A 1 111 ? -6.311  -17.008 24.524  1.00 10.09 ? 111 LYS A O    1 
ATOM   884  C  CB   . LYS A 1 111 ? -5.623  -17.087 27.372  1.00 13.62 ? 111 LYS A CB   1 
ATOM   885  C  CG   . LYS A 1 111 ? -4.906  -16.611 28.657  1.00 15.13 ? 111 LYS A CG   1 
ATOM   886  C  CD   . LYS A 1 111 ? -4.024  -15.494 28.330  1.00 19.02 ? 111 LYS A CD   1 
ATOM   887  C  CE   . LYS A 1 111 ? -3.205  -14.817 29.509  1.00 20.10 ? 111 LYS A CE   1 
ATOM   888  N  NZ   . LYS A 1 111 ? -1.995  -15.617 29.619  1.00 26.22 ? 111 LYS A NZ   1 
ATOM   889  N  N    . LYS A 1 112 ? -8.374  -16.484 25.200  1.00 8.62  ? 112 LYS A N    1 
ATOM   890  C  CA   . LYS A 1 112 ? -8.955  -16.952 23.944  1.00 10.69 ? 112 LYS A CA   1 
ATOM   891  C  C    . LYS A 1 112 ? -8.652  -15.860 22.863  1.00 10.13 ? 112 LYS A C    1 
ATOM   892  O  O    . LYS A 1 112 ? -8.903  -14.651 23.029  1.00 9.33  ? 112 LYS A O    1 
ATOM   893  C  CB   . LYS A 1 112 ? -10.532 -17.066 24.034  1.00 11.86 ? 112 LYS A CB   1 
ATOM   894  C  CG   . LYS A 1 112 ? -11.168 -17.420 22.651  1.00 11.65 ? 112 LYS A CG   1 
ATOM   895  C  CD   . LYS A 1 112 ? -12.692 -17.483 22.817  1.00 16.04 ? 112 LYS A CD   1 
ATOM   896  C  CE   . LYS A 1 112 ? -13.246 -17.556 21.388  1.00 18.16 ? 112 LYS A CE   1 
ATOM   897  N  NZ   . LYS A 1 112 ? -13.145 -18.837 20.950  1.00 18.15 ? 112 LYS A NZ   1 
ATOM   898  N  N    . LYS A 1 113 ? -8.141  -16.358 21.744  1.00 9.05  ? 113 LYS A N    1 
ATOM   899  C  CA   . LYS A 1 113 ? -7.991  -15.562 20.509  1.00 9.13  ? 113 LYS A CA   1 
ATOM   900  C  C    . LYS A 1 113 ? -9.124  -15.771 19.543  1.00 8.61  ? 113 LYS A C    1 
ATOM   901  O  O    . LYS A 1 113 ? -9.451  -16.922 19.267  1.00 10.49 ? 113 LYS A O    1 
ATOM   902  C  CB   . LYS A 1 113 ? -6.647  -15.968 19.842  1.00 9.49  ? 113 LYS A CB   1 
ATOM   903  C  CG   . LYS A 1 113 ? -5.397  -15.663 20.657  1.00 10.07 ? 113 LYS A CG   1 
ATOM   904  C  CD   . LYS A 1 113 ? -4.142  -16.247 20.035  1.00 12.76 ? 113 LYS A CD   1 
ATOM   905  C  CE   . LYS A 1 113 ? -2.935  -15.579 20.752  1.00 14.89 ? 113 LYS A CE   1 
ATOM   906  N  NZ   . LYS A 1 113 ? -1.838  -16.426 20.906  1.00 24.92 ? 113 LYS A NZ   1 
ATOM   907  N  N    . TYR A 1 114 ? -9.708  -14.686 19.063  1.00 7.77  ? 114 TYR A N    1 
ATOM   908  C  CA   . TYR A 1 114 ? -10.649 -14.787 18.012  1.00 7.17  ? 114 TYR A CA   1 
ATOM   909  C  C    . TYR A 1 114 ? -10.034 -14.751 16.667  1.00 7.25  ? 114 TYR A C    1 
ATOM   910  O  O    . TYR A 1 114 ? -8.837  -14.426 16.527  1.00 7.63  ? 114 TYR A O    1 
ATOM   911  C  CB   . TYR A 1 114 ? -11.742 -13.684 18.135  1.00 8.56  ? 114 TYR A CB   1 
ATOM   912  C  CG   . TYR A 1 114 ? -12.685 -13.862 19.281  1.00 9.10  ? 114 TYR A CG   1 
ATOM   913  C  CD1  . TYR A 1 114 ? -12.368 -13.521 20.591  1.00 10.23 ? 114 TYR A CD1  1 
ATOM   914  C  CD2  . TYR A 1 114 ? -13.893 -14.504 19.039  1.00 10.24 ? 114 TYR A CD2  1 
ATOM   915  C  CE1  . TYR A 1 114 ? -13.260 -13.755 21.600  1.00 11.61 ? 114 TYR A CE1  1 
ATOM   916  C  CE2  . TYR A 1 114 ? -14.844 -14.664 20.054  1.00 11.19 ? 114 TYR A CE2  1 
ATOM   917  C  CZ   . TYR A 1 114 ? -14.478 -14.303 21.313  1.00 11.72 ? 114 TYR A CZ   1 
ATOM   918  O  OH   . TYR A 1 114 ? -15.374 -14.475 22.412  1.00 15.95 ? 114 TYR A OH   1 
ATOM   919  N  N    . ALA A 1 115 ? -10.774 -15.019 15.600  1.00 6.55  ? 115 ALA A N    1 
ATOM   920  C  CA   . ALA A 1 115 ? -10.221 -15.008 14.266  1.00 7.07  ? 115 ALA A CA   1 
ATOM   921  C  C    . ALA A 1 115 ? -9.814  -13.647 13.761  1.00 6.75  ? 115 ALA A C    1 
ATOM   922  O  O    . ALA A 1 115 ? -8.983  -13.501 12.867  1.00 7.80  ? 115 ALA A O    1 
ATOM   923  C  CB   . ALA A 1 115 ? -11.247 -15.686 13.274  1.00 8.90  ? 115 ALA A CB   1 
ATOM   924  N  N    . ALA A 1 116 ? -10.503 -12.633 14.302  1.00 6.24  ? 116 ALA A N    1 
ATOM   925  C  CA   . ALA A 1 116 ? -10.147 -11.290 13.848  1.00 7.09  ? 116 ALA A CA   1 
ATOM   926  C  C    . ALA A 1 116 ? -10.791 -10.365 14.852  1.00 6.64  ? 116 ALA A C    1 
ATOM   927  O  O    . ALA A 1 116 ? -11.532 -10.725 15.769  1.00 6.82  ? 116 ALA A O    1 
ATOM   928  C  CB   . ALA A 1 116 ? -10.731 -10.977 12.403  1.00 7.95  ? 116 ALA A CB   1 
ATOM   929  N  N    . GLU A 1 117 ? -10.448 -9.069  14.674  1.00 6.47  ? 117 GLU A N    1 
ATOM   930  C  CA   . GLU A 1 117 ? -11.003 -8.019  15.566  1.00 6.06  ? 117 GLU A CA   1 
ATOM   931  C  C    . GLU A 1 117 ? -11.177 -6.736  14.743  1.00 7.74  ? 117 GLU A C    1 
ATOM   932  O  O    . GLU A 1 117 ? -10.274 -6.374  13.993  1.00 8.17  ? 117 GLU A O    1 
ATOM   933  C  CB   . GLU A 1 117 ? -10.005 -7.731  16.702  1.00 8.42  ? 117 GLU A CB   1 
ATOM   934  C  CG   . GLU A 1 117 ? -10.518 -6.779  17.823  1.00 8.74  ? 117 GLU A CG   1 
ATOM   935  C  CD   . GLU A 1 117 ? -9.563  -6.714  19.064  1.00 8.16  ? 117 GLU A CD   1 
ATOM   936  O  OE1  . GLU A 1 117 ? -8.927  -7.751  19.277  1.00 8.31  ? 117 GLU A OE1  1 
ATOM   937  O  OE2  . GLU A 1 117 ? -9.554  -5.665  19.679  1.00 8.64  ? 117 GLU A OE2  1 
ATOM   938  N  N    . LEU A 1 118 ? -12.372 -6.156  14.822  1.00 7.50  ? 118 LEU A N    1 
ATOM   939  C  CA   . LEU A 1 118 ? -12.689 -4.888  14.182  1.00 6.71  ? 118 LEU A CA   1 
ATOM   940  C  C    . LEU A 1 118 ? -12.467 -3.752  15.208  1.00 5.56  ? 118 LEU A C    1 
ATOM   941  O  O    . LEU A 1 118 ? -12.914 -3.856  16.357  1.00 6.41  ? 118 LEU A O    1 
ATOM   942  C  CB   . LEU A 1 118 ? -14.197 -4.974  13.854  1.00 7.64  ? 118 LEU A CB   1 
ATOM   943  C  CG   . LEU A 1 118 ? -14.966 -3.671  13.528  1.00 8.60  ? 118 LEU A CG   1 
ATOM   944  C  CD1  . LEU A 1 118 ? -14.387 -3.086  12.253  1.00 9.31  ? 118 LEU A CD1  1 
ATOM   945  C  CD2  . LEU A 1 118 ? -16.437 -4.056  13.206  1.00 8.73  ? 118 LEU A CD2  1 
ATOM   946  N  N    . HIS A 1 119 ? -11.852 -2.646  14.705  1.00 5.65  ? 119 HIS A N    1 
ATOM   947  C  CA   . HIS A 1 119 ? -11.659 -1.477  15.473  1.00 5.98  ? 119 HIS A CA   1 
ATOM   948  C  C    . HIS A 1 119 ? -12.324 -0.322  14.779  1.00 6.89  ? 119 HIS A C    1 
ATOM   949  O  O    . HIS A 1 119 ? -11.945 0.029   13.662  1.00 7.01  ? 119 HIS A O    1 
ATOM   950  C  CB   . HIS A 1 119 ? -10.150 -1.214  15.565  1.00 5.97  ? 119 HIS A CB   1 
ATOM   951  C  CG   . HIS A 1 119 ? -9.473  -2.202  16.459  1.00 6.11  ? 119 HIS A CG   1 
ATOM   952  N  ND1  . HIS A 1 119 ? -8.119  -2.424  16.462  1.00 7.25  ? 119 HIS A ND1  1 
ATOM   953  C  CD2  . HIS A 1 119 ? -9.992  -3.027  17.362  1.00 6.73  ? 119 HIS A CD2  1 
ATOM   954  C  CE1  . HIS A 1 119 ? -7.775  -3.386  17.296  1.00 6.21  ? 119 HIS A CE1  1 
ATOM   955  N  NE2  . HIS A 1 119 ? -8.905  -3.742  17.937  1.00 7.20  ? 119 HIS A NE2  1 
ATOM   956  N  N    . LEU A 1 120 ? -13.296 0.251   15.500  1.00 6.39  ? 120 LEU A N    1 
ATOM   957  C  CA   . LEU A 1 120 ? -13.955 1.505   15.023  1.00 8.04  ? 120 LEU A CA   1 
ATOM   958  C  C    . LEU A 1 120 ? -13.348 2.639   15.813  1.00 6.36  ? 120 LEU A C    1 
ATOM   959  O  O    . LEU A 1 120 ? -13.479 2.658   17.005  1.00 6.49  ? 120 LEU A O    1 
ATOM   960  C  CB   . LEU A 1 120 ? -15.435 1.389   15.219  1.00 7.77  ? 120 LEU A CB   1 
ATOM   961  C  CG   . LEU A 1 120 ? -16.155 0.308   14.352  1.00 8.46  ? 120 LEU A CG   1 
ATOM   962  C  CD1  . LEU A 1 120 ? -17.100 -0.527  15.189  1.00 11.46 ? 120 LEU A CD1  1 
ATOM   963  C  CD2  . LEU A 1 120 ? -16.966 1.016   13.248  1.00 9.85  ? 120 LEU A CD2  1 
ATOM   964  N  N    . VAL A 1 121 ? -12.577 3.474   15.107  1.00 6.86  ? 121 VAL A N    1 
ATOM   965  C  CA   . VAL A 1 121 ? -11.744 4.522   15.739  1.00 7.20  ? 121 VAL A CA   1 
ATOM   966  C  C    . VAL A 1 121 ? -12.447 5.819   15.770  1.00 8.56  ? 121 VAL A C    1 
ATOM   967  O  O    . VAL A 1 121 ? -12.898 6.289   14.719  1.00 7.38  ? 121 VAL A O    1 
ATOM   968  C  CB   . VAL A 1 121 ? -10.421 4.616   14.935  1.00 8.20  ? 121 VAL A CB   1 
ATOM   969  C  CG1  . VAL A 1 121 ? -9.509  5.684   15.552  1.00 9.67  ? 121 VAL A CG1  1 
ATOM   970  C  CG2  . VAL A 1 121 ? -9.663  3.274   14.857  1.00 7.92  ? 121 VAL A CG2  1 
ATOM   971  N  N    . HIS A 1 122 ? -12.555 6.438   16.952  1.00 6.82  ? 122 HIS A N    1 
ATOM   972  C  CA   . HIS A 1 122 ? -13.253 7.683   17.105  1.00 6.76  ? 122 HIS A CA   1 
ATOM   973  C  C    . HIS A 1 122 ? -12.297 8.676   17.819  1.00 8.42  ? 122 HIS A C    1 
ATOM   974  O  O    . HIS A 1 122 ? -11.604 8.306   18.770  1.00 8.12  ? 122 HIS A O    1 
ATOM   975  C  CB   . HIS A 1 122 ? -14.500 7.561   17.961  1.00 7.61  ? 122 HIS A CB   1 
ATOM   976  C  CG   . HIS A 1 122 ? -15.430 6.444   17.542  1.00 8.59  ? 122 HIS A CG   1 
ATOM   977  N  ND1  . HIS A 1 122 ? -15.084 5.121   17.756  1.00 7.80  ? 122 HIS A ND1  1 
ATOM   978  C  CD2  . HIS A 1 122 ? -16.646 6.407   16.896  1.00 10.28 ? 122 HIS A CD2  1 
ATOM   979  C  CE1  . HIS A 1 122 ? -16.054 4.310   17.333  1.00 9.30  ? 122 HIS A CE1  1 
ATOM   980  N  NE2  . HIS A 1 122 ? -17.024 5.067   16.786  1.00 9.26  ? 122 HIS A NE2  1 
ATOM   981  N  N    . TRP A 1 123 ? -12.460 9.938   17.511  1.00 7.91  ? 123 TRP A N    1 
ATOM   982  C  CA   . TRP A 1 123 ? -11.658 10.994  18.204  1.00 8.79  ? 123 TRP A CA   1 
ATOM   983  C  C    . TRP A 1 123 ? -12.544 11.947  18.919  1.00 8.84  ? 123 TRP A C    1 
ATOM   984  O  O    . TRP A 1 123 ? -13.664 12.315  18.512  1.00 8.93  ? 123 TRP A O    1 
ATOM   985  C  CB   . TRP A 1 123 ? -10.762 11.733  17.241  1.00 9.10  ? 123 TRP A CB   1 
ATOM   986  C  CG   . TRP A 1 123 ? -11.416 12.340  16.078  1.00 10.48 ? 123 TRP A CG   1 
ATOM   987  C  CD1  . TRP A 1 123 ? -11.583 11.751  14.865  1.00 9.39  ? 123 TRP A CD1  1 
ATOM   988  C  CD2  . TRP A 1 123 ? -11.949 13.655  15.983  1.00 9.56  ? 123 TRP A CD2  1 
ATOM   989  N  NE1  . TRP A 1 123 ? -12.260 12.577  14.028  1.00 11.59 ? 123 TRP A NE1  1 
ATOM   990  C  CE2  . TRP A 1 123 ? -12.430 13.817  14.628  1.00 13.47 ? 123 TRP A CE2  1 
ATOM   991  C  CE3  . TRP A 1 123 ? -11.934 14.744  16.830  1.00 10.55 ? 123 TRP A CE3  1 
ATOM   992  C  CZ2  . TRP A 1 123 ? -13.043 14.970  14.166  1.00 14.37 ? 123 TRP A CZ2  1 
ATOM   993  C  CZ3  . TRP A 1 123 ? -12.549 15.937  16.366  1.00 12.72 ? 123 TRP A CZ3  1 
ATOM   994  C  CH2  . TRP A 1 123 ? -13.120 16.042  15.042  1.00 12.85 ? 123 TRP A CH2  1 
ATOM   995  N  N    . ASN A 1 124 ? -12.015 12.425  20.037  1.00 8.33  ? 124 ASN A N    1 
ATOM   996  C  CA   . ASN A 1 124 ? -12.754 13.302  20.956  1.00 8.68  ? 124 ASN A CA   1 
ATOM   997  C  C    . ASN A 1 124 ? -12.919 14.653  20.375  1.00 9.47  ? 124 ASN A C    1 
ATOM   998  O  O    . ASN A 1 124 ? -11.916 15.343  20.083  1.00 9.31  ? 124 ASN A O    1 
ATOM   999  C  CB   . ASN A 1 124 ? -11.912 13.359  22.257  1.00 8.33  ? 124 ASN A CB   1 
ATOM   1000 C  CG   . ASN A 1 124 ? -12.709 13.951  23.411  1.00 11.40 ? 124 ASN A CG   1 
ATOM   1001 O  OD1  . ASN A 1 124 ? -13.539 14.817  23.166  1.00 11.98 ? 124 ASN A OD1  1 
ATOM   1002 N  ND2  . ASN A 1 124 ? -12.475 13.442  24.657  1.00 12.00 ? 124 ASN A ND2  1 
ATOM   1003 N  N    . THR A 1 125 ? -14.192 15.048  20.174  1.00 10.31 ? 125 THR A N    1 
ATOM   1004 C  CA   . THR A 1 125 ? -14.428 16.338  19.458  1.00 11.37 ? 125 THR A CA   1 
ATOM   1005 C  C    . THR A 1 125 ? -13.850 17.582  20.193  1.00 12.33 ? 125 THR A C    1 
ATOM   1006 O  O    . THR A 1 125 ? -13.680 18.633  19.621  1.00 13.30 ? 125 THR A O    1 
ATOM   1007 C  CB   . THR A 1 125 ? -15.917 16.503  19.168  1.00 14.85 ? 125 THR A CB   1 
ATOM   1008 O  OG1  . THR A 1 125 ? -16.640 16.501  20.425  1.00 17.15 ? 125 THR A OG1  1 
ATOM   1009 C  CG2  . THR A 1 125 ? -16.438 15.363  18.221  1.00 14.99 ? 125 THR A CG2  1 
ATOM   1010 N  N    . LYS A 1 126 ? -13.558 17.343  21.578  1.00 11.19 ? 127 LYS A N    1 
ATOM   1011 C  CA   . LYS A 1 126 ? -12.993 18.532  22.264  1.00 12.79 ? 127 LYS A CA   1 
ATOM   1012 C  C    . LYS A 1 126 ? -11.618 18.869  21.745  1.00 14.35 ? 127 LYS A C    1 
ATOM   1013 O  O    . LYS A 1 126 ? -11.043 19.956  22.051  1.00 16.06 ? 127 LYS A O    1 
ATOM   1014 C  CB   . LYS A 1 126 ? -12.969 18.302  23.752  1.00 14.67 ? 127 LYS A CB   1 
ATOM   1015 C  CG   . LYS A 1 126 ? -11.942 17.369  24.299  1.00 15.43 ? 127 LYS A CG   1 
ATOM   1016 C  CD   . LYS A 1 126 ? -12.253 16.991  25.835  1.00 17.94 ? 127 LYS A CD   1 
ATOM   1017 C  CE   . LYS A 1 126 ? -11.495 17.881  26.778  1.00 29.10 ? 127 LYS A CE   1 
ATOM   1018 N  NZ   . LYS A 1 126 ? -11.182 17.094  28.043  1.00 34.02 ? 127 LYS A NZ   1 
ATOM   1019 N  N    . TYR A 1 127 ? -10.981 17.975  20.998  1.00 11.22 ? 128 TYR A N    1 
ATOM   1020 C  CA   . TYR A 1 127 ? -9.620  18.290  20.474  1.00 11.24 ? 128 TYR A CA   1 
ATOM   1021 C  C    . TYR A 1 127 ? -9.541  18.674  18.995  1.00 11.44 ? 128 TYR A C    1 
ATOM   1022 O  O    . TYR A 1 127 ? -8.447  18.907  18.426  1.00 11.90 ? 128 TYR A O    1 
ATOM   1023 C  CB   . TYR A 1 127 ? -8.653  17.149  20.722  1.00 10.07 ? 128 TYR A CB   1 
ATOM   1024 C  CG   . TYR A 1 127 ? -8.531  16.823  22.171  1.00 9.93  ? 128 TYR A CG   1 
ATOM   1025 C  CD1  . TYR A 1 127 ? -8.083  17.815  23.090  1.00 11.82 ? 128 TYR A CD1  1 
ATOM   1026 C  CD2  . TYR A 1 127 ? -8.840  15.553  22.736  1.00 9.87  ? 128 TYR A CD2  1 
ATOM   1027 C  CE1  . TYR A 1 127 ? -8.012  17.547  24.422  1.00 12.61 ? 128 TYR A CE1  1 
ATOM   1028 C  CE2  . TYR A 1 127 ? -8.744  15.287  24.102  1.00 9.91  ? 128 TYR A CE2  1 
ATOM   1029 C  CZ   . TYR A 1 127 ? -8.331  16.334  24.940  1.00 12.44 ? 128 TYR A CZ   1 
ATOM   1030 O  OH   . TYR A 1 127 ? -8.214  16.097  26.260  1.00 13.92 ? 128 TYR A OH   1 
ATOM   1031 N  N    . GLY A 1 128 ? -10.750 18.768  18.426  1.00 12.68 ? 129 GLY A N    1 
ATOM   1032 C  CA   . GLY A 1 128 ? -10.875 19.419  17.104  1.00 12.07 ? 129 GLY A CA   1 
ATOM   1033 C  C    . GLY A 1 128 ? -10.532 18.553  15.927  1.00 11.88 ? 129 GLY A C    1 
ATOM   1034 O  O    . GLY A 1 128 ? -11.161 18.710  14.835  1.00 14.38 ? 129 GLY A O    1 
ATOM   1035 N  N    . ASP A 1 129 ? -9.484  17.732  16.009  1.00 12.55 ? 130 ASP A N    1 
ATOM   1036 C  CA   . ASP A 1 129 ? -9.254  16.726  14.970  1.00 13.34 ? 130 ASP A CA   1 
ATOM   1037 C  C    . ASP A 1 129 ? -8.444  15.539  15.494  1.00 14.29 ? 130 ASP A C    1 
ATOM   1038 O  O    . ASP A 1 129 ? -7.972  15.565  16.651  1.00 12.73 ? 130 ASP A O    1 
ATOM   1039 C  CB   . ASP A 1 129 ? -8.677  17.318  13.694  1.00 14.74 ? 130 ASP A CB   1 
ATOM   1040 C  CG   . ASP A 1 129 ? -7.343  17.802  13.880  1.00 18.06 ? 130 ASP A CG   1 
ATOM   1041 O  OD1  . ASP A 1 129 ? -6.692  17.635  14.946  1.00 25.11 ? 130 ASP A OD1  1 
ATOM   1042 O  OD2  . ASP A 1 129 ? -6.801  18.437  12.931  1.00 20.36 ? 130 ASP A OD2  1 
ATOM   1043 N  N    . PHE A 1 130 ? -8.293  14.532  14.630  1.00 11.65 ? 131 PHE A N    1 
ATOM   1044 C  CA   . PHE A 1 130 ? -7.685  13.283  15.026  1.00 12.83 ? 131 PHE A CA   1 
ATOM   1045 C  C    . PHE A 1 130 ? -6.243  13.563  15.387  1.00 11.08 ? 131 PHE A C    1 
ATOM   1046 O  O    . PHE A 1 130 ? -5.774  13.053  16.395  1.00 10.85 ? 131 PHE A O    1 
ATOM   1047 C  CB   . PHE A 1 130 ? -7.814  12.262  13.885  1.00 11.11 ? 131 PHE A CB   1 
ATOM   1048 C  CG   . PHE A 1 130 ? -7.049  10.988  14.117  1.00 11.76 ? 131 PHE A CG   1 
ATOM   1049 C  CD1  . PHE A 1 130 ? -7.633  9.901   14.815  1.00 9.61  ? 131 PHE A CD1  1 
ATOM   1050 C  CD2  . PHE A 1 130 ? -5.721  10.910  13.769  1.00 12.08 ? 131 PHE A CD2  1 
ATOM   1051 C  CE1  . PHE A 1 130 ? -6.905  8.793   14.982  1.00 10.33 ? 131 PHE A CE1  1 
ATOM   1052 C  CE2  . PHE A 1 130 ? -4.968  9.803   13.948  1.00 12.94 ? 131 PHE A CE2  1 
ATOM   1053 C  CZ   . PHE A 1 130 ? -5.611  8.700   14.561  1.00 12.39 ? 131 PHE A CZ   1 
ATOM   1054 N  N    . GLY A 1 131 ? -5.486  14.370  14.574  1.00 12.27 ? 132 GLY A N    1 
ATOM   1055 C  CA   . GLY A 1 131 ? -4.073  14.537  14.872  1.00 12.09 ? 132 GLY A CA   1 
ATOM   1056 C  C    . GLY A 1 131 ? -3.777  15.181  16.224  1.00 12.00 ? 132 GLY A C    1 
ATOM   1057 O  O    . GLY A 1 131 ? -2.739  14.867  16.856  1.00 13.88 ? 132 GLY A O    1 
ATOM   1058 N  N    . LYS A 1 132 ? -4.654  16.104  16.598  1.00 11.66 ? 133 LYS A N    1 
ATOM   1059 C  CA   . LYS A 1 132 ? -4.434  16.671  17.923  1.00 12.71 ? 133 LYS A CA   1 
ATOM   1060 C  C    . LYS A 1 132 ? -4.893  15.734  19.047  1.00 11.60 ? 133 LYS A C    1 
ATOM   1061 O  O    . LYS A 1 132 ? -4.373  15.655  20.166  1.00 12.04 ? 133 LYS A O    1 
ATOM   1062 C  CB   . LYS A 1 132 ? -5.195  17.973  18.047  1.00 14.10 ? 133 LYS A CB   1 
ATOM   1063 C  CG   . LYS A 1 132 ? -4.554  19.150  17.236  1.00 20.16 ? 133 LYS A CG   1 
ATOM   1064 C  CD   . LYS A 1 132 ? -3.116  19.472  17.742  1.00 27.39 ? 133 LYS A CD   1 
ATOM   1065 C  CE   . LYS A 1 132 ? -3.168  20.722  18.761  1.00 30.96 ? 133 LYS A CE   1 
ATOM   1066 N  NZ   . LYS A 1 132 ? -1.780  21.337  18.894  1.00 33.54 ? 133 LYS A NZ   1 
ATOM   1067 N  N    . ALA A 1 133 ? -5.997  14.993  18.746  1.00 10.80 ? 134 ALA A N    1 
ATOM   1068 C  CA   . ALA A 1 133 ? -6.557  14.110  19.779  1.00 10.13 ? 134 ALA A CA   1 
ATOM   1069 C  C    . ALA A 1 133 ? -5.570  13.005  20.136  1.00 9.60  ? 134 ALA A C    1 
ATOM   1070 O  O    . ALA A 1 133 ? -5.522  12.622  21.328  1.00 9.16  ? 134 ALA A O    1 
ATOM   1071 C  CB   . ALA A 1 133 ? -7.848  13.431  19.189  1.00 9.91  ? 134 ALA A CB   1 
ATOM   1072 N  N    . VAL A 1 134 ? -4.769  12.500  19.203  1.00 9.75  ? 135 VAL A N    1 
ATOM   1073 C  CA   . VAL A 1 134 ? -3.854  11.460  19.609  1.00 10.25 ? 135 VAL A CA   1 
ATOM   1074 C  C    . VAL A 1 134 ? -2.757  11.857  20.568  1.00 10.24 ? 135 VAL A C    1 
ATOM   1075 O  O    . VAL A 1 134 ? -2.080  11.000  21.115  1.00 10.64 ? 135 VAL A O    1 
ATOM   1076 C  CB   . VAL A 1 134 ? -3.223  10.709  18.404  1.00 11.99 ? 135 VAL A CB   1 
ATOM   1077 C  CG1  . VAL A 1 134 ? -4.327  10.005  17.600  1.00 12.19 ? 135 VAL A CG1  1 
ATOM   1078 C  CG2  . VAL A 1 134 ? -2.326  11.586  17.555  1.00 12.02 ? 135 VAL A CG2  1 
ATOM   1079 N  N    . GLN A 1 135 ? -2.611  13.167  20.765  1.00 10.30 ? 136 GLN A N    1 
ATOM   1080 C  CA   . GLN A 1 135 ? -1.610  13.690  21.752  1.00 13.91 ? 136 GLN A CA   1 
ATOM   1081 C  C    . GLN A 1 135 ? -2.168  13.817  23.091  1.00 14.31 ? 136 GLN A C    1 
ATOM   1082 O  O    . GLN A 1 135 ? -1.536  14.404  24.004  1.00 14.42 ? 136 GLN A O    1 
ATOM   1083 C  CB   . GLN A 1 135 ? -1.072  15.067  21.185  1.00 14.74 ? 136 GLN A CB   1 
ATOM   1084 C  CG   . GLN A 1 135 ? -0.372  14.909  19.872  1.00 15.73 ? 136 GLN A CG   1 
ATOM   1085 C  CD   . GLN A 1 135 ? 0.061   16.290  19.357  1.00 23.23 ? 136 GLN A CD   1 
ATOM   1086 O  OE1  . GLN A 1 135 ? 0.823   17.004  20.063  1.00 32.04 ? 136 GLN A OE1  1 
ATOM   1087 N  NE2  . GLN A 1 135 ? -0.448  16.688  18.180  1.00 23.90 ? 136 GLN A NE2  1 
ATOM   1088 N  N    . GLN A 1 136 ? -3.371  13.336  23.284  1.00 9.84  ? 137 GLN A N    1 
ATOM   1089 C  CA   . GLN A 1 136 ? -4.060  13.498  24.595  1.00 10.85 ? 137 GLN A CA   1 
ATOM   1090 C  C    . GLN A 1 136 ? -4.450  12.166  25.193  1.00 10.97 ? 137 GLN A C    1 
ATOM   1091 O  O    . GLN A 1 136 ? -4.758  11.217  24.470  1.00 10.50 ? 137 GLN A O    1 
ATOM   1092 C  CB   . GLN A 1 136 ? -5.337  14.294  24.464  1.00 10.28 ? 137 GLN A CB   1 
ATOM   1093 C  CG   . GLN A 1 136 ? -5.196  15.602  23.611  1.00 13.29 ? 137 GLN A CG   1 
ATOM   1094 C  CD   . GLN A 1 136 ? -4.264  16.569  24.187  1.00 16.61 ? 137 GLN A CD   1 
ATOM   1095 O  OE1  . GLN A 1 136 ? -4.019  16.557  25.362  1.00 17.31 ? 137 GLN A OE1  1 
ATOM   1096 N  NE2  . GLN A 1 136 ? -3.599  17.333  23.302  1.00 30.57 ? 137 GLN A NE2  1 
ATOM   1097 N  N    . PRO A 1 137 ? -4.459  12.088  26.521  1.00 10.17 ? 138 PRO A N    1 
ATOM   1098 C  CA   . PRO A 1 137 ? -4.709  10.802  27.161  1.00 10.72 ? 138 PRO A CA   1 
ATOM   1099 C  C    . PRO A 1 137 ? -6.147  10.316  26.986  1.00 10.23 ? 138 PRO A C    1 
ATOM   1100 O  O    . PRO A 1 137 ? -6.360  9.097   27.088  1.00 12.14 ? 138 PRO A O    1 
ATOM   1101 C  CB   . PRO A 1 137 ? -4.404  10.992  28.652  1.00 12.92 ? 138 PRO A CB   1 
ATOM   1102 C  CG   . PRO A 1 137 ? -4.359  12.385  28.848  1.00 16.38 ? 138 PRO A CG   1 
ATOM   1103 C  CD   . PRO A 1 137 ? -4.037  13.106  27.510  1.00 12.82 ? 138 PRO A CD   1 
ATOM   1104 N  N    . ASP A 1 138 ? -7.069  11.228  26.663  1.00 8.66  ? 139 ASP A N    1 
ATOM   1105 C  CA   . ASP A 1 138 ? -8.479  10.849  26.393  1.00 9.24  ? 139 ASP A CA   1 
ATOM   1106 C  C    . ASP A 1 138 ? -8.810  11.229  24.961  1.00 8.95  ? 139 ASP A C    1 
ATOM   1107 O  O    . ASP A 1 138 ? -9.973  11.641  24.704  1.00 10.04 ? 139 ASP A O    1 
ATOM   1108 C  CB   . ASP A 1 138 ? -9.471  11.477  27.367  1.00 10.68 ? 139 ASP A CB   1 
ATOM   1109 C  CG   . ASP A 1 138 ? -9.331  12.973  27.397  1.00 12.51 ? 139 ASP A CG   1 
ATOM   1110 O  OD1  . ASP A 1 138 ? -8.389  13.608  26.821  1.00 13.12 ? 139 ASP A OD1  1 
ATOM   1111 O  OD2  . ASP A 1 138 ? -10.142 13.615  28.119  1.00 16.90 ? 139 ASP A OD2  1 
ATOM   1112 N  N    . GLY A 1 139 ? -7.851  11.131  24.046  1.00 8.89  ? 140 GLY A N    1 
ATOM   1113 C  CA   . GLY A 1 139 ? -8.118  11.605  22.719  1.00 8.47  ? 140 GLY A CA   1 
ATOM   1114 C  C    . GLY A 1 139 ? -8.984  10.685  21.883  1.00 8.25  ? 140 GLY A C    1 
ATOM   1115 O  O    . GLY A 1 139 ? -9.622  11.202  20.984  1.00 7.94  ? 140 GLY A O    1 
ATOM   1116 N  N    . LEU A 1 140 ? -8.840  9.349   22.022  1.00 6.76  ? 141 LEU A N    1 
ATOM   1117 C  CA   . LEU A 1 140 ? -9.516  8.447   21.138  1.00 5.47  ? 141 LEU A CA   1 
ATOM   1118 C  C    . LEU A 1 140 ? -10.365 7.498   21.958  1.00 7.60  ? 141 LEU A C    1 
ATOM   1119 O  O    . LEU A 1 140 ? -10.096 7.225   23.128  1.00 7.37  ? 141 LEU A O    1 
ATOM   1120 C  CB   . LEU A 1 140 ? -8.499  7.596   20.378  1.00 7.57  ? 141 LEU A CB   1 
ATOM   1121 C  CG   . LEU A 1 140 ? -7.592  8.346   19.437  1.00 7.89  ? 141 LEU A CG   1 
ATOM   1122 C  CD1  . LEU A 1 140 ? -6.850  7.250   18.544  1.00 9.15  ? 141 LEU A CD1  1 
ATOM   1123 C  CD2  . LEU A 1 140 ? -8.271  9.292   18.476  1.00 9.61  ? 141 LEU A CD2  1 
ATOM   1124 N  N    . ALA A 1 141 ? -11.434 6.979   21.280  1.00 7.68  ? 142 ALA A N    1 
ATOM   1125 C  CA   . ALA A 1 141 ? -12.169 5.859   21.822  1.00 7.19  ? 142 ALA A CA   1 
ATOM   1126 C  C    . ALA A 1 141 ? -12.311 4.863   20.721  1.00 7.35  ? 142 ALA A C    1 
ATOM   1127 O  O    . ALA A 1 141 ? -12.662 5.233   19.597  1.00 8.11  ? 142 ALA A O    1 
ATOM   1128 C  CB   . ALA A 1 141 ? -13.564 6.306   22.305  1.00 8.20  ? 142 ALA A CB   1 
ATOM   1129 N  N    . VAL A 1 142 ? -11.839 3.640   20.997  1.00 7.82  ? 143 VAL A N    1 
ATOM   1130 C  CA   . VAL A 1 142 ? -11.911 2.631   19.948  1.00 8.48  ? 143 VAL A CA   1 
ATOM   1131 C  C    . VAL A 1 142 ? -12.907 1.570   20.419  1.00 8.80  ? 143 VAL A C    1 
ATOM   1132 O  O    . VAL A 1 142 ? -12.794 1.049   21.534  1.00 7.79  ? 143 VAL A O    1 
ATOM   1133 C  CB   . VAL A 1 142 ? -10.537 1.981   19.640  1.00 8.08  ? 143 VAL A CB   1 
ATOM   1134 C  CG1  . VAL A 1 142 ? -10.748 0.943   18.549  1.00 9.44  ? 143 VAL A CG1  1 
ATOM   1135 C  CG2  . VAL A 1 142 ? -9.564  3.016   19.192  1.00 9.37  ? 143 VAL A CG2  1 
ATOM   1136 N  N    . LEU A 1 143 ? -13.892 1.287   19.563  1.00 6.93  ? 144 LEU A N    1 
ATOM   1137 C  CA   . LEU A 1 143 ? -14.852 0.241   19.813  1.00 7.67  ? 144 LEU A CA   1 
ATOM   1138 C  C    . LEU A 1 143 ? -14.305 -0.999  19.120  1.00 7.76  ? 144 LEU A C    1 
ATOM   1139 O  O    . LEU A 1 143 ? -14.156 -1.036  17.908  1.00 8.78  ? 144 LEU A O    1 
ATOM   1140 C  CB   . LEU A 1 143 ? -16.264 0.698   19.305  1.00 8.32  ? 144 LEU A CB   1 
ATOM   1141 C  CG   . LEU A 1 143 ? -17.355 -0.361  19.398  1.00 9.40  ? 144 LEU A CG   1 
ATOM   1142 C  CD1  . LEU A 1 143 ? -17.630 -0.607  20.859  1.00 11.37 ? 144 LEU A CD1  1 
ATOM   1143 C  CD2  . LEU A 1 143 ? -18.605 0.243   18.723  1.00 12.06 ? 144 LEU A CD2  1 
ATOM   1144 N  N    . GLY A 1 144 ? -14.017 -2.000  19.942  1.00 6.76  ? 145 GLY A N    1 
ATOM   1145 C  CA   . GLY A 1 144 ? -13.400 -3.243  19.464  1.00 6.37  ? 145 GLY A CA   1 
ATOM   1146 C  C    . GLY A 1 144 ? -14.441 -4.407  19.485  1.00 5.70  ? 145 GLY A C    1 
ATOM   1147 O  O    . GLY A 1 144 ? -15.191 -4.537  20.458  1.00 7.51  ? 145 GLY A O    1 
ATOM   1148 N  N    . ILE A 1 145 ? -14.514 -5.107  18.368  1.00 5.56  ? 146 ILE A N    1 
ATOM   1149 C  CA   . ILE A 1 145 ? -15.561 -6.140  18.233  1.00 6.53  ? 146 ILE A CA   1 
ATOM   1150 C  C    . ILE A 1 145 ? -14.796 -7.372  17.696  1.00 6.45  ? 146 ILE A C    1 
ATOM   1151 O  O    . ILE A 1 145 ? -14.120 -7.333  16.681  1.00 6.69  ? 146 ILE A O    1 
ATOM   1152 C  CB   . ILE A 1 145 ? -16.609 -5.637  17.222  1.00 6.80  ? 146 ILE A CB   1 
ATOM   1153 C  CG1  . ILE A 1 145 ? -17.273 -4.406  17.738  1.00 10.09 ? 146 ILE A CG1  1 
ATOM   1154 C  CG2  . ILE A 1 145 ? -17.650 -6.749  16.933  1.00 10.53 ? 146 ILE A CG2  1 
ATOM   1155 C  CD1  . ILE A 1 145 ? -18.354 -3.789  16.719  1.00 9.40  ? 146 ILE A CD1  1 
ATOM   1156 N  N    . PHE A 1 146 ? -15.035 -8.472  18.390  1.00 5.78  ? 147 PHE A N    1 
ATOM   1157 C  CA   . PHE A 1 146 ? -14.422 -9.723  17.950  1.00 6.96  ? 147 PHE A CA   1 
ATOM   1158 C  C    . PHE A 1 146 ? -15.174 -10.354 16.790  1.00 8.81  ? 147 PHE A C    1 
ATOM   1159 O  O    . PHE A 1 146 ? -16.414 -10.210 16.741  1.00 8.66  ? 147 PHE A O    1 
ATOM   1160 C  CB   . PHE A 1 146 ? -14.387 -10.710 19.115  1.00 7.58  ? 147 PHE A CB   1 
ATOM   1161 C  CG   . PHE A 1 146 ? -13.534 -10.210 20.273  1.00 5.24  ? 147 PHE A CG   1 
ATOM   1162 C  CD1  . PHE A 1 146 ? -12.189 -10.080 20.051  1.00 6.93  ? 147 PHE A CD1  1 
ATOM   1163 C  CD2  . PHE A 1 146 ? -14.008 -9.949  21.483  1.00 7.26  ? 147 PHE A CD2  1 
ATOM   1164 C  CE1  . PHE A 1 146 ? -11.334 -9.706  21.155  1.00 6.33  ? 147 PHE A CE1  1 
ATOM   1165 C  CE2  . PHE A 1 146 ? -13.253 -9.565  22.544  1.00 7.93  ? 147 PHE A CE2  1 
ATOM   1166 C  CZ   . PHE A 1 146 ? -11.866 -9.485  22.379  1.00 8.22  ? 147 PHE A CZ   1 
ATOM   1167 N  N    . LEU A 1 147 ? -14.426 -11.075 15.968  1.00 7.36  ? 148 LEU A N    1 
ATOM   1168 C  CA   . LEU A 1 147 ? -15.044 -11.826 14.814  1.00 7.46  ? 148 LEU A CA   1 
ATOM   1169 C  C    . LEU A 1 147 ? -14.685 -13.304 15.076  1.00 8.06  ? 148 LEU A C    1 
ATOM   1170 O  O    . LEU A 1 147 ? -13.509 -13.656 15.296  1.00 8.96  ? 148 LEU A O    1 
ATOM   1171 C  CB   . LEU A 1 147 ? -14.415 -11.437 13.462  1.00 8.03  ? 148 LEU A CB   1 
ATOM   1172 C  CG   . LEU A 1 147 ? -14.997 -10.173 12.838  1.00 7.95  ? 148 LEU A CG   1 
ATOM   1173 C  CD1  . LEU A 1 147 ? -14.706 -8.926  13.663  1.00 10.08 ? 148 LEU A CD1  1 
ATOM   1174 C  CD2  . LEU A 1 147 ? -14.377 -10.047 11.494  1.00 9.66  ? 148 LEU A CD2  1 
ATOM   1175 N  N    . LYS A 1 148 ? -15.713 -14.144 14.987  1.00 8.41  ? 149 LYS A N    1 
ATOM   1176 C  CA   . LYS A 1 148 ? -15.536 -15.598 14.961  1.00 9.90  ? 149 LYS A CA   1 
ATOM   1177 C  C    . LYS A 1 148 ? -16.058 -16.082 13.608  1.00 10.41 ? 149 LYS A C    1 
ATOM   1178 O  O    . LYS A 1 148 ? -16.884 -15.485 12.932  1.00 10.56 ? 149 LYS A O    1 
ATOM   1179 C  CB   . LYS A 1 148 ? -16.314 -16.320 16.094  1.00 10.44 ? 149 LYS A CB   1 
ATOM   1180 C  CG   . LYS A 1 148 ? -17.874 -16.199 15.938  1.00 13.15 ? 149 LYS A CG   1 
ATOM   1181 C  CD   . LYS A 1 148 ? -18.469 -16.752 17.323  1.00 19.60 ? 149 LYS A CD   1 
ATOM   1182 C  CE   . LYS A 1 148 ? -19.952 -17.160 17.171  1.00 28.37 ? 149 LYS A CE   1 
ATOM   1183 N  NZ   . LYS A 1 148 ? -20.174 -18.339 18.163  1.00 33.77 ? 149 LYS A NZ   1 
ATOM   1184 N  N    . VAL A 1 149 ? -15.564 -17.233 13.236  1.00 9.97  ? 150 VAL A N    1 
ATOM   1185 C  CA   . VAL A 1 149 ? -15.951 -17.785 11.946  1.00 10.20 ? 150 VAL A CA   1 
ATOM   1186 C  C    . VAL A 1 149 ? -17.169 -18.721 12.100  1.00 12.40 ? 150 VAL A C    1 
ATOM   1187 O  O    . VAL A 1 149 ? -17.142 -19.661 12.922  1.00 11.99 ? 150 VAL A O    1 
ATOM   1188 C  CB   . VAL A 1 149 ? -14.716 -18.583 11.363  1.00 9.59  ? 150 VAL A CB   1 
ATOM   1189 C  CG1  . VAL A 1 149 ? -15.099 -19.306 10.062  1.00 10.72 ? 150 VAL A CG1  1 
ATOM   1190 C  CG2  . VAL A 1 149 ? -13.679 -17.610 11.063  1.00 13.03 ? 150 VAL A CG2  1 
ATOM   1191 N  N    . GLY A 1 150 ? -18.199 -18.459 11.315  1.00 9.96  ? 151 GLY A N    1 
ATOM   1192 C  CA   . GLY A 1 150 ? -19.450 -19.291 11.388  1.00 10.73 ? 151 GLY A CA   1 
ATOM   1193 C  C    . GLY A 1 150 ? -20.307 -18.793 10.283  1.00 10.59 ? 151 GLY A C    1 
ATOM   1194 O  O    . GLY A 1 150 ? -19.928 -18.887 9.135   1.00 11.98 ? 151 GLY A O    1 
ATOM   1195 N  N    A SER A 1 151 ? -21.471 -18.277 10.673  0.50 12.42 ? 152 SER A N    1 
ATOM   1196 N  N    B SER A 1 151 ? -21.502 -18.322 10.682  0.50 11.83 ? 152 SER A N    1 
ATOM   1197 C  CA   A SER A 1 151 ? -22.330 -17.697 9.618   0.50 13.26 ? 152 SER A CA   1 
ATOM   1198 C  CA   B SER A 1 151 ? -22.489 -17.731 9.700   0.50 12.29 ? 152 SER A CA   1 
ATOM   1199 C  C    A SER A 1 151 ? -21.710 -16.440 9.019   0.50 13.45 ? 152 SER A C    1 
ATOM   1200 C  C    B SER A 1 151 ? -21.925 -16.435 9.133   0.50 12.32 ? 152 SER A C    1 
ATOM   1201 O  O    A SER A 1 151 ? -20.826 -15.766 9.582   0.50 11.68 ? 152 SER A O    1 
ATOM   1202 O  O    B SER A 1 151 ? -21.232 -15.748 9.921   0.50 11.25 ? 152 SER A O    1 
ATOM   1203 C  CB   A SER A 1 151 ? -23.727 -17.378 10.124  0.50 15.16 ? 152 SER A CB   1 
ATOM   1204 C  CB   B SER A 1 151 ? -23.759 -17.357 10.424  0.50 14.80 ? 152 SER A CB   1 
ATOM   1205 O  OG   A SER A 1 151 ? -23.737 -16.313 11.071  0.50 19.46 ? 152 SER A OG   1 
ATOM   1206 O  OG   B SER A 1 151 ? -24.385 -18.483 10.931  0.50 16.19 ? 152 SER A OG   1 
ATOM   1207 N  N    . ALA A 1 152 ? -22.152 -16.118 7.822   1.00 12.98 ? 153 ALA A N    1 
ATOM   1208 C  CA   . ALA A 1 152 ? -21.723 -14.891 7.210   1.00 11.93 ? 153 ALA A CA   1 
ATOM   1209 C  C    . ALA A 1 152 ? -22.344 -13.674 7.867   1.00 11.05 ? 153 ALA A C    1 
ATOM   1210 O  O    . ALA A 1 152 ? -23.415 -13.739 8.426   1.00 13.65 ? 153 ALA A O    1 
ATOM   1211 C  CB   . ALA A 1 152 ? -22.068 -14.856 5.677   1.00 14.51 ? 153 ALA A CB   1 
ATOM   1212 N  N    . LYS A 1 153 ? -21.592 -12.568 7.833   1.00 11.63 ? 154 LYS A N    1 
ATOM   1213 C  CA   . LYS A 1 153 ? -22.140 -11.297 8.200   1.00 11.94 ? 154 LYS A CA   1 
ATOM   1214 C  C    . LYS A 1 153 ? -22.530 -10.510 6.950   1.00 12.08 ? 154 LYS A C    1 
ATOM   1215 O  O    . LYS A 1 153 ? -21.702 -10.026 6.236   1.00 11.82 ? 154 LYS A O    1 
ATOM   1216 C  CB   . LYS A 1 153 ? -21.071 -10.538 9.025   1.00 12.59 ? 154 LYS A CB   1 
ATOM   1217 C  CG   . LYS A 1 153 ? -21.591 -9.329  9.777   1.00 15.37 ? 154 LYS A CG   1 
ATOM   1218 C  CD   . LYS A 1 153 ? -22.406 -9.666  10.957  1.00 14.78 ? 154 LYS A CD   1 
ATOM   1219 C  CE   . LYS A 1 153 ? -22.764 -8.444  11.873  1.00 18.58 ? 154 LYS A CE   1 
ATOM   1220 N  NZ   . LYS A 1 153 ? -23.540 -8.954  12.933  1.00 23.48 ? 154 LYS A NZ   1 
ATOM   1221 N  N    . PRO A 1 154 ? -23.902 -10.429 6.724   1.00 13.61 ? 155 PRO A N    1 
ATOM   1222 C  CA   . PRO A 1 154 ? -24.253 -9.826  5.405   1.00 15.64 ? 155 PRO A CA   1 
ATOM   1223 C  C    . PRO A 1 154 ? -23.767 -8.373  5.264   1.00 13.15 ? 155 PRO A C    1 
ATOM   1224 O  O    . PRO A 1 154 ? -23.314 -7.935  4.203   1.00 16.05 ? 155 PRO A O    1 
ATOM   1225 C  CB   . PRO A 1 154 ? -25.825 -9.952  5.366   1.00 16.22 ? 155 PRO A CB   1 
ATOM   1226 C  CG   . PRO A 1 154 ? -26.121 -11.108 6.342   1.00 17.55 ? 155 PRO A CG   1 
ATOM   1227 C  CD   . PRO A 1 154 ? -25.060 -10.976 7.465   1.00 13.90 ? 155 PRO A CD   1 
ATOM   1228 N  N    . GLY A 1 155 ? -23.693 -7.692  6.422   1.00 12.66 ? 156 GLY A N    1 
ATOM   1229 C  CA   . GLY A 1 155 ? -23.345 -6.275  6.398   1.00 13.91 ? 156 GLY A CA   1 
ATOM   1230 C  C    . GLY A 1 155 ? -21.889 -6.042  6.195   1.00 14.02 ? 156 GLY A C    1 
ATOM   1231 O  O    . GLY A 1 155 ? -21.424 -4.898  5.981   1.00 16.40 ? 156 GLY A O    1 
ATOM   1232 N  N    . LEU A 1 156 ? -21.079 -7.107  6.276   1.00 12.47 ? 157 LEU A N    1 
ATOM   1233 C  CA   . LEU A 1 156 ? -19.681 -7.113  5.860   1.00 12.01 ? 157 LEU A CA   1 
ATOM   1234 C  C    . LEU A 1 156 ? -19.356 -7.289  4.405   1.00 11.98 ? 157 LEU A C    1 
ATOM   1235 O  O    . LEU A 1 156 ? -18.243 -7.045  3.926   1.00 11.44 ? 157 LEU A O    1 
ATOM   1236 C  CB   . LEU A 1 156 ? -18.874 -8.126  6.723   1.00 13.65 ? 157 LEU A CB   1 
ATOM   1237 C  CG   . LEU A 1 156 ? -17.361 -8.238  6.548   1.00 12.78 ? 157 LEU A CG   1 
ATOM   1238 C  CD1  . LEU A 1 156 ? -16.635 -6.945  6.945   1.00 12.20 ? 157 LEU A CD1  1 
ATOM   1239 C  CD2  . LEU A 1 156 ? -16.729 -9.374  7.399   1.00 12.92 ? 157 LEU A CD2  1 
ATOM   1240 N  N    . GLN A 1 157 ? -20.394 -7.824  3.660   1.00 12.61 ? 158 GLN A N    1 
ATOM   1241 C  CA   . GLN A 1 157 ? -20.036 -8.304  2.354   1.00 14.93 ? 158 GLN A CA   1 
ATOM   1242 C  C    . GLN A 1 157 ? -19.597 -7.215  1.382   1.00 12.26 ? 158 GLN A C    1 
ATOM   1243 O  O    . GLN A 1 157 ? -18.669 -7.419  0.587   1.00 13.74 ? 158 GLN A O    1 
ATOM   1244 C  CB   . GLN A 1 157 ? -21.189 -9.163  1.800   1.00 15.43 ? 158 GLN A CB   1 
ATOM   1245 C  CG   . GLN A 1 157 ? -20.782 -9.898  0.468   1.00 16.03 ? 158 GLN A CG   1 
ATOM   1246 C  CD   . GLN A 1 157 ? -19.593 -10.888 0.688   1.00 13.45 ? 158 GLN A CD   1 
ATOM   1247 O  OE1  . GLN A 1 157 ? -19.481 -11.426 1.819   1.00 14.77 ? 158 GLN A OE1  1 
ATOM   1248 N  NE2  . GLN A 1 157 ? -18.766 -11.135 -0.296  1.00 17.29 ? 158 GLN A NE2  1 
ATOM   1249 N  N    . LYS A 1 158 ? -20.195 -5.990  1.536   1.00 15.11 ? 159 LYS A N    1 
ATOM   1250 C  CA   . LYS A 1 158 ? -19.738 -4.906  0.724   1.00 14.46 ? 159 LYS A CA   1 
ATOM   1251 C  C    . LYS A 1 158 ? -18.259 -4.545  0.849   1.00 14.46 ? 159 LYS A C    1 
ATOM   1252 O  O    . LYS A 1 158 ? -17.578 -4.200  -0.030  1.00 15.01 ? 159 LYS A O    1 
ATOM   1253 C  CB   . LYS A 1 158 ? -20.702 -3.701  0.924   1.00 16.66 ? 159 LYS A CB   1 
ATOM   1254 C  CG   . LYS A 1 158 ? -22.057 -3.970  0.199   1.00 20.57 ? 159 LYS A CG   1 
ATOM   1255 C  CD   . LYS A 1 158 ? -22.999 -2.788  0.360   0.01 15.79 ? 159 LYS A CD   1 
ATOM   1256 C  CE   . LYS A 1 158 ? -24.359 -3.076  -0.254  0.01 16.27 ? 159 LYS A CE   1 
ATOM   1257 N  NZ   . LYS A 1 158 ? -25.275 -1.907  -0.137  0.01 15.66 ? 159 LYS A NZ   1 
ATOM   1258 N  N    . VAL A 1 159 ? -17.755 -4.732  2.072   1.00 14.91 ? 160 VAL A N    1 
ATOM   1259 C  CA   . VAL A 1 159 ? -16.306 -4.525  2.271   1.00 14.06 ? 160 VAL A CA   1 
ATOM   1260 C  C    . VAL A 1 159 ? -15.451 -5.636  1.626   1.00 11.92 ? 160 VAL A C    1 
ATOM   1261 O  O    . VAL A 1 159 ? -14.482 -5.447  0.913   1.00 13.61 ? 160 VAL A O    1 
ATOM   1262 C  CB   . VAL A 1 159 ? -15.983 -4.601  3.789   1.00 15.32 ? 160 VAL A CB   1 
ATOM   1263 C  CG1  . VAL A 1 159 ? -14.468 -4.660  4.087   1.00 14.95 ? 160 VAL A CG1  1 
ATOM   1264 C  CG2  . VAL A 1 159 ? -16.616 -3.387  4.494   1.00 17.02 ? 160 VAL A CG2  1 
ATOM   1265 N  N    . VAL A 1 160 ? -15.965 -6.864  1.864   1.00 12.65 ? 161 VAL A N    1 
ATOM   1266 C  CA   . VAL A 1 160 ? -15.229 -8.023  1.307   1.00 15.60 ? 161 VAL A CA   1 
ATOM   1267 C  C    . VAL A 1 160 ? -15.162 -7.935  -0.233  1.00 14.34 ? 161 VAL A C    1 
ATOM   1268 O  O    . VAL A 1 160 ? -14.151 -8.213  -0.811  1.00 15.71 ? 161 VAL A O    1 
ATOM   1269 C  CB   . VAL A 1 160 ? -15.949 -9.398  1.716   1.00 15.94 ? 161 VAL A CB   1 
ATOM   1270 C  CG1  . VAL A 1 160 ? -15.486 -10.528 0.775   1.00 20.88 ? 161 VAL A CG1  1 
ATOM   1271 C  CG2  . VAL A 1 160 ? -15.547 -9.675  3.182   1.00 17.97 ? 161 VAL A CG2  1 
ATOM   1272 N  N    . ASP A 1 161 ? -16.277 -7.479  -0.839  1.00 15.04 ? 162 ASP A N    1 
ATOM   1273 C  CA   . ASP A 1 161 ? -16.296 -7.457  -2.289  1.00 19.21 ? 162 ASP A CA   1 
ATOM   1274 C  C    . ASP A 1 161 ? -15.341 -6.458  -2.959  1.00 20.32 ? 162 ASP A C    1 
ATOM   1275 O  O    . ASP A 1 161 ? -14.931 -6.613  -4.152  1.00 24.11 ? 162 ASP A O    1 
ATOM   1276 C  CB   . ASP A 1 161 ? -17.730 -7.331  -2.729  1.00 20.42 ? 162 ASP A CB   1 
ATOM   1277 C  CG   . ASP A 1 161 ? -18.435 -8.706  -2.677  1.00 19.00 ? 162 ASP A CG   1 
ATOM   1278 O  OD1  . ASP A 1 161 ? -17.719 -9.756  -2.737  1.00 25.54 ? 162 ASP A OD1  1 
ATOM   1279 O  OD2  . ASP A 1 161 ? -19.649 -8.735  -2.465  1.00 24.61 ? 162 ASP A OD2  1 
ATOM   1280 N  N    . VAL A 1 162 ? -14.948 -5.420  -2.204  1.00 18.19 ? 163 VAL A N    1 
ATOM   1281 C  CA   . VAL A 1 162 ? -14.114 -4.349  -2.765  1.00 18.77 ? 163 VAL A CA   1 
ATOM   1282 C  C    . VAL A 1 162 ? -12.608 -4.668  -2.612  1.00 16.06 ? 163 VAL A C    1 
ATOM   1283 O  O    . VAL A 1 162 ? -11.704 -4.005  -3.130  1.00 17.96 ? 163 VAL A O    1 
ATOM   1284 C  CB   . VAL A 1 162 ? -14.533 -2.970  -2.121  1.00 20.55 ? 163 VAL A CB   1 
ATOM   1285 C  CG1  . VAL A 1 162 ? -13.786 -2.684  -0.851  1.00 21.22 ? 163 VAL A CG1  1 
ATOM   1286 C  CG2  . VAL A 1 162 ? -14.418 -1.767  -3.108  1.00 20.78 ? 163 VAL A CG2  1 
ATOM   1287 N  N    . LEU A 1 163 ? -12.288 -5.707  -1.797  1.00 16.23 ? 164 LEU A N    1 
ATOM   1288 C  CA   . LEU A 1 163 ? -10.906 -5.932  -1.424  1.00 14.29 ? 164 LEU A CA   1 
ATOM   1289 C  C    . LEU A 1 163 ? -9.985  -6.280  -2.569  1.00 14.50 ? 164 LEU A C    1 
ATOM   1290 O  O    . LEU A 1 163 ? -8.750  -6.042  -2.564  1.00 15.09 ? 164 LEU A O    1 
ATOM   1291 C  CB   . LEU A 1 163 ? -10.676 -6.937  -0.286  1.00 14.90 ? 164 LEU A CB   1 
ATOM   1292 C  CG   . LEU A 1 163 ? -11.376 -6.638  1.049   1.00 13.52 ? 164 LEU A CG   1 
ATOM   1293 C  CD1  . LEU A 1 163 ? -11.174 -7.885  2.006   1.00 15.03 ? 164 LEU A CD1  1 
ATOM   1294 C  CD2  . LEU A 1 163 ? -10.783 -5.354  1.625   1.00 14.58 ? 164 LEU A CD2  1 
ATOM   1295 N  N    . ASP A 1 164 ? -10.680 -6.866  -3.581  1.00 19.02 ? 165 ASP A N    1 
ATOM   1296 C  CA   . ASP A 1 164 ? -9.829  -7.271  -4.688  1.00 21.02 ? 165 ASP A CA   1 
ATOM   1297 C  C    . ASP A 1 164 ? -9.337  -6.006  -5.484  1.00 21.03 ? 165 ASP A C    1 
ATOM   1298 O  O    . ASP A 1 164 ? -8.327  -6.139  -6.219  1.00 22.24 ? 165 ASP A O    1 
ATOM   1299 C  CB   . ASP A 1 164 ? -10.591 -8.227  -5.647  1.00 23.50 ? 165 ASP A CB   1 
ATOM   1300 C  CG   . ASP A 1 164 ? -11.484 -7.459  -6.515  1.00 29.81 ? 165 ASP A CG   1 
ATOM   1301 O  OD1  . ASP A 1 164 ? -12.475 -6.893  -5.957  1.00 35.93 ? 165 ASP A OD1  1 
ATOM   1302 O  OD2  . ASP A 1 164 ? -11.157 -7.334  -7.748  1.00 37.69 ? 165 ASP A OD2  1 
ATOM   1303 N  N    . SER A 1 165 ? -9.992  -4.849  -5.284  1.00 19.95 ? 166 SER A N    1 
ATOM   1304 C  CA   . SER A 1 165 ? -9.566  -3.563  -5.906  1.00 20.56 ? 166 SER A CA   1 
ATOM   1305 C  C    . SER A 1 165 ? -8.448  -2.840  -5.125  1.00 20.47 ? 166 SER A C    1 
ATOM   1306 O  O    . SER A 1 165 ? -7.845  -1.849  -5.589  1.00 20.81 ? 166 SER A O    1 
ATOM   1307 C  CB   . SER A 1 165 ? -10.737 -2.678  -6.131  1.00 24.19 ? 166 SER A CB   1 
ATOM   1308 O  OG   . SER A 1 165 ? -11.255 -2.221  -4.921  1.00 24.13 ? 166 SER A OG   1 
ATOM   1309 N  N    . ILE A 1 166 ? -8.085  -3.382  -3.927  1.00 17.49 ? 167 ILE A N    1 
ATOM   1310 C  CA   . ILE A 1 166 ? -7.108  -2.716  -3.091  1.00 15.22 ? 167 ILE A CA   1 
ATOM   1311 C  C    . ILE A 1 166 ? -6.140  -3.719  -2.574  1.00 14.45 ? 167 ILE A C    1 
ATOM   1312 O  O    . ILE A 1 166 ? -5.717  -3.758  -1.391  1.00 13.19 ? 167 ILE A O    1 
ATOM   1313 C  CB   . ILE A 1 166 ? -7.722  -1.874  -1.928  1.00 14.42 ? 167 ILE A CB   1 
ATOM   1314 C  CG1  . ILE A 1 166 ? -8.593  -2.739  -1.063  1.00 14.76 ? 167 ILE A CG1  1 
ATOM   1315 C  CG2  . ILE A 1 166 ? -8.504  -0.675  -2.466  1.00 15.88 ? 167 ILE A CG2  1 
ATOM   1316 C  CD1  . ILE A 1 166 ? -8.531  -2.218  0.352   1.00 15.60 ? 167 ILE A CD1  1 
ATOM   1317 N  N    . LYS A 1 167 ? -5.766  -4.649  -3.445  1.00 13.81 ? 168 LYS A N    1 
ATOM   1318 C  CA   . LYS A 1 167 ? -4.971  -5.748  -3.004  1.00 15.28 ? 168 LYS A CA   1 
ATOM   1319 C  C    . LYS A 1 167 ? -3.662  -5.382  -2.337  1.00 15.36 ? 168 LYS A C    1 
ATOM   1320 O  O    . LYS A 1 167 ? -3.197  -6.065  -1.452  1.00 15.26 ? 168 LYS A O    1 
ATOM   1321 C  CB   . LYS A 1 167 ? -4.741  -6.669  -4.213  1.00 15.44 ? 168 LYS A CB   1 
ATOM   1322 C  CG   . LYS A 1 167 ? -3.914  -7.878  -3.852  1.00 17.52 ? 168 LYS A CG   1 
ATOM   1323 C  CD   . LYS A 1 167 ? -3.677  -8.787  -5.094  1.00 21.83 ? 168 LYS A CD   1 
ATOM   1324 C  CE   . LYS A 1 167 ? -3.420  -10.187 -4.563  1.00 29.75 ? 168 LYS A CE   1 
ATOM   1325 N  NZ   . LYS A 1 167 ? -2.744  -11.064 -5.635  1.00 35.52 ? 168 LYS A NZ   1 
ATOM   1326 N  N    . THR A 1 168 ? -3.047  -4.315  -2.868  1.00 14.79 ? 169 THR A N    1 
ATOM   1327 C  CA   . THR A 1 168 ? -1.685  -3.979  -2.531  1.00 13.99 ? 169 THR A CA   1 
ATOM   1328 C  C    . THR A 1 168 ? -1.593  -2.564  -1.828  1.00 10.01 ? 169 THR A C    1 
ATOM   1329 O  O    . THR A 1 168 ? -2.492  -1.760  -1.938  1.00 15.45 ? 169 THR A O    1 
ATOM   1330 C  CB   . THR A 1 168 ? -0.703  -4.049  -3.799  1.00 16.63 ? 169 THR A CB   1 
ATOM   1331 O  OG1  . THR A 1 168 ? -1.396  -3.311  -4.796  1.00 19.41 ? 169 THR A OG1  1 
ATOM   1332 C  CG2  . THR A 1 168 ? -0.484  -5.558  -4.147  1.00 14.55 ? 169 THR A CG2  1 
ATOM   1333 N  N    . LYS A 1 169 ? -0.528  -2.493  -1.087  1.00 15.48 ? 170 LYS A N    1 
ATOM   1334 C  CA   . LYS A 1 169 ? -0.197  -1.270  -0.315  1.00 15.43 ? 170 LYS A CA   1 
ATOM   1335 C  C    . LYS A 1 169 ? -0.310  0.018   -1.077  1.00 15.96 ? 170 LYS A C    1 
ATOM   1336 O  O    . LYS A 1 169 ? 0.170   0.097   -2.258  1.00 19.92 ? 170 LYS A O    1 
ATOM   1337 C  CB   . LYS A 1 169 ? 1.167   -1.468  0.285   1.00 15.80 ? 170 LYS A CB   1 
ATOM   1338 C  CG   . LYS A 1 169 ? 1.722   -0.229  1.148   1.00 17.21 ? 170 LYS A CG   1 
ATOM   1339 C  CD   . LYS A 1 169 ? 3.109   -0.519  1.689   1.00 18.87 ? 170 LYS A CD   1 
ATOM   1340 C  CE   . LYS A 1 169 ? 3.723   0.663   2.519   1.00 25.05 ? 170 LYS A CE   1 
ATOM   1341 N  NZ   . LYS A 1 169 ? 5.251   0.815   2.289   1.00 35.04 ? 170 LYS A NZ   1 
ATOM   1342 N  N    . GLY A 1 170 ? -1.031  0.967   -0.560  1.00 17.88 ? 171 GLY A N    1 
ATOM   1343 C  CA   . GLY A 1 170 ? -1.225  2.246   -1.329  1.00 18.40 ? 171 GLY A CA   1 
ATOM   1344 C  C    . GLY A 1 170 ? -2.388  2.285   -2.251  1.00 21.99 ? 171 GLY A C    1 
ATOM   1345 O  O    . GLY A 1 170 ? -2.787  3.404   -2.743  1.00 20.37 ? 171 GLY A O    1 
ATOM   1346 N  N    . LYS A 1 171 ? -3.040  1.131   -2.523  1.00 17.42 ? 172 LYS A N    1 
ATOM   1347 C  CA   . LYS A 1 171 ? -4.282  1.253   -3.247  1.00 19.49 ? 172 LYS A CA   1 
ATOM   1348 C  C    . LYS A 1 171 ? -5.484  1.735   -2.505  1.00 18.02 ? 172 LYS A C    1 
ATOM   1349 O  O    . LYS A 1 171 ? -5.638  1.301   -1.331  1.00 17.44 ? 172 LYS A O    1 
ATOM   1350 C  CB   . LYS A 1 171 ? -4.598  -0.060  -4.026  1.00 19.37 ? 172 LYS A CB   1 
ATOM   1351 C  CG   . LYS A 1 171 ? -3.434  -0.526  -4.829  1.00 21.63 ? 172 LYS A CG   1 
ATOM   1352 C  CD   . LYS A 1 171 ? -3.772  -1.575  -5.985  1.00 24.26 ? 172 LYS A CD   1 
ATOM   1353 C  CE   . LYS A 1 171 ? -4.634  -0.966  -7.086  0.01 23.08 ? 172 LYS A CE   1 
ATOM   1354 N  NZ   . LYS A 1 171 ? -5.118  -1.996  -8.048  0.01 22.55 ? 172 LYS A NZ   1 
ATOM   1355 N  N    . SER A 1 172 ? -6.369  2.532   -3.068  1.00 16.97 ? 173 SER A N    1 
ATOM   1356 C  CA   . SER A 1 172 ? -7.650  2.886   -2.529  1.00 16.65 ? 173 SER A CA   1 
ATOM   1357 C  C    . SER A 1 172 ? -8.846  2.825   -3.454  1.00 14.81 ? 173 SER A C    1 
ATOM   1358 O  O    . SER A 1 172 ? -8.665  2.717   -4.755  1.00 18.19 ? 173 SER A O    1 
ATOM   1359 C  CB   . SER A 1 172 ? -7.664  4.311   -1.895  1.00 16.30 ? 173 SER A CB   1 
ATOM   1360 O  OG   . SER A 1 172 ? -7.444  5.270   -2.953  1.00 22.19 ? 173 SER A OG   1 
ATOM   1361 N  N    . ALA A 1 173 ? -10.034 2.772   -2.954  1.00 20.10 ? 174 ALA A N    1 
ATOM   1362 C  CA   . ALA A 1 173 ? -11.183 2.715   -3.825  1.00 20.19 ? 174 ALA A CA   1 
ATOM   1363 C  C    . ALA A 1 173 ? -12.321 3.562   -3.205  1.00 21.91 ? 174 ALA A C    1 
ATOM   1364 O  O    . ALA A 1 173 ? -12.556 3.603   -1.956  1.00 16.45 ? 174 ALA A O    1 
ATOM   1365 C  CB   . ALA A 1 173 ? -11.619 1.326   -4.035  1.00 21.39 ? 174 ALA A CB   1 
ATOM   1366 N  N    . ASP A 1 174 ? -13.088 4.272   -4.014  1.00 22.91 ? 175 ASP A N    1 
ATOM   1367 C  CA   . ASP A 1 174 ? -14.293 4.907   -3.483  1.00 23.41 ? 175 ASP A CA   1 
ATOM   1368 C  C    . ASP A 1 174 ? -15.097 3.916   -2.726  1.00 23.24 ? 175 ASP A C    1 
ATOM   1369 O  O    . ASP A 1 174 ? -15.294 2.764   -3.163  1.00 23.06 ? 175 ASP A O    1 
ATOM   1370 C  CB   . ASP A 1 174 ? -15.199 5.495   -4.619  1.00 24.26 ? 175 ASP A CB   1 
ATOM   1371 C  CG   . ASP A 1 174 ? -14.484 6.570   -5.346  1.00 30.48 ? 175 ASP A CG   1 
ATOM   1372 O  OD1  . ASP A 1 174 ? -13.763 7.376   -4.721  1.00 33.54 ? 175 ASP A OD1  1 
ATOM   1373 O  OD2  . ASP A 1 174 ? -14.575 6.606   -6.588  1.00 30.84 ? 175 ASP A OD2  1 
ATOM   1374 N  N    . PHE A 1 175 ? -15.635 4.387   -1.583  1.00 18.15 ? 176 PHE A N    1 
ATOM   1375 C  CA   . PHE A 1 175 ? -16.342 3.474   -0.772  1.00 17.50 ? 176 PHE A CA   1 
ATOM   1376 C  C    . PHE A 1 175 ? -17.390 4.200   -0.065  1.00 18.50 ? 176 PHE A C    1 
ATOM   1377 O  O    . PHE A 1 175 ? -17.301 4.410   1.154   1.00 18.87 ? 176 PHE A O    1 
ATOM   1378 C  CB   . PHE A 1 175 ? -15.378 2.610   0.157   1.00 15.13 ? 176 PHE A CB   1 
ATOM   1379 C  CG   . PHE A 1 175 ? -16.006 1.399   0.661   1.00 17.50 ? 176 PHE A CG   1 
ATOM   1380 C  CD1  . PHE A 1 175 ? -16.387 0.339   -0.191  1.00 18.99 ? 176 PHE A CD1  1 
ATOM   1381 C  CD2  . PHE A 1 175 ? -16.292 1.273   2.001   1.00 17.23 ? 176 PHE A CD2  1 
ATOM   1382 C  CE1  . PHE A 1 175 ? -16.969 -0.819  0.345   1.00 19.92 ? 176 PHE A CE1  1 
ATOM   1383 C  CE2  . PHE A 1 175 ? -16.891 0.116   2.531   1.00 20.79 ? 176 PHE A CE2  1 
ATOM   1384 C  CZ   . PHE A 1 175 ? -17.276 -0.891  1.704   1.00 16.53 ? 176 PHE A CZ   1 
ATOM   1385 N  N    . THR A 1 176 ? -18.384 4.685   -0.779  1.00 15.23 ? 177 THR A N    1 
ATOM   1386 C  CA   . THR A 1 176 ? -19.494 5.428   -0.191  1.00 16.32 ? 177 THR A CA   1 
ATOM   1387 C  C    . THR A 1 176 ? -20.681 4.676   0.288   1.00 13.00 ? 177 THR A C    1 
ATOM   1388 O  O    . THR A 1 176 ? -20.891 3.534   -0.199  1.00 14.67 ? 177 THR A O    1 
ATOM   1389 C  CB   . THR A 1 176 ? -19.966 6.539   -1.173  1.00 16.11 ? 177 THR A CB   1 
ATOM   1390 O  OG1  . THR A 1 176 ? -20.313 5.887   -2.412  1.00 20.88 ? 177 THR A OG1  1 
ATOM   1391 C  CG2  . THR A 1 176 ? -18.812 7.472   -1.440  1.00 20.45 ? 177 THR A CG2  1 
ATOM   1392 N  N    . ASN A 1 177 ? -21.499 5.229   1.155   1.00 12.81 ? 178 ASN A N    1 
ATOM   1393 C  CA   . ASN A 1 177 ? -22.734 4.704   1.528   1.00 14.67 ? 178 ASN A CA   1 
ATOM   1394 C  C    . ASN A 1 177 ? -22.609 3.346   2.270   1.00 16.08 ? 178 ASN A C    1 
ATOM   1395 O  O    . ASN A 1 177 ? -23.524 2.566   2.261   1.00 18.86 ? 178 ASN A O    1 
ATOM   1396 C  CB   . ASN A 1 177 ? -23.537 4.548   0.256   1.00 14.37 ? 178 ASN A CB   1 
ATOM   1397 C  CG   . ASN A 1 177 ? -23.889 5.953   -0.304  1.00 16.39 ? 178 ASN A CG   1 
ATOM   1398 O  OD1  . ASN A 1 177 ? -24.584 6.731   0.326   1.00 18.32 ? 178 ASN A OD1  1 
ATOM   1399 N  ND2  . ASN A 1 177 ? -23.268 6.239   -1.435  1.00 15.86 ? 178 ASN A ND2  1 
ATOM   1400 N  N    . PHE A 1 178 ? -21.454 3.155   2.918   1.00 15.61 ? 179 PHE A N    1 
ATOM   1401 C  CA   . PHE A 1 178 ? -21.310 1.862   3.697   1.00 14.69 ? 179 PHE A CA   1 
ATOM   1402 C  C    . PHE A 1 178 ? -21.843 2.138   5.056   1.00 12.98 ? 179 PHE A C    1 
ATOM   1403 O  O    . PHE A 1 178 ? -21.355 3.124   5.694   1.00 15.02 ? 179 PHE A O    1 
ATOM   1404 C  CB   . PHE A 1 178 ? -19.930 1.456   3.828   1.00 14.23 ? 179 PHE A CB   1 
ATOM   1405 C  CG   . PHE A 1 178 ? -19.810 0.227   4.676   1.00 13.94 ? 179 PHE A CG   1 
ATOM   1406 C  CD1  . PHE A 1 178 ? -20.267 -0.993  4.132   1.00 18.22 ? 179 PHE A CD1  1 
ATOM   1407 C  CD2  . PHE A 1 178 ? -19.360 0.280   6.013   1.00 12.27 ? 179 PHE A CD2  1 
ATOM   1408 C  CE1  . PHE A 1 178 ? -20.240 -2.178  4.857   1.00 17.24 ? 179 PHE A CE1  1 
ATOM   1409 C  CE2  . PHE A 1 178 ? -19.337 -0.927  6.740   1.00 12.81 ? 179 PHE A CE2  1 
ATOM   1410 C  CZ   . PHE A 1 178 ? -19.796 -2.113  6.214   1.00 13.90 ? 179 PHE A CZ   1 
ATOM   1411 N  N    . ASP A 1 179 ? -22.727 1.326   5.604   1.00 14.14 ? 180 ASP A N    1 
ATOM   1412 C  CA   . ASP A 1 179 ? -23.365 1.537   6.870   1.00 13.99 ? 180 ASP A CA   1 
ATOM   1413 C  C    . ASP A 1 179 ? -22.690 0.641   7.913   1.00 12.39 ? 180 ASP A C    1 
ATOM   1414 O  O    . ASP A 1 179 ? -22.907 -0.549  7.982   1.00 13.58 ? 180 ASP A O    1 
ATOM   1415 C  CB   . ASP A 1 179 ? -24.810 1.119   6.761   1.00 15.36 ? 180 ASP A CB   1 
ATOM   1416 C  CG   . ASP A 1 179 ? -25.637 1.569   7.935   1.00 18.36 ? 180 ASP A CG   1 
ATOM   1417 O  OD1  . ASP A 1 179 ? -25.113 1.789   9.058   1.00 14.58 ? 180 ASP A OD1  1 
ATOM   1418 O  OD2  . ASP A 1 179 ? -26.879 1.779   7.799   1.00 24.45 ? 180 ASP A OD2  1 
ATOM   1419 N  N    . PRO A 1 180 ? -21.957 1.261   8.850   1.00 11.71 ? 181 PRO A N    1 
ATOM   1420 C  CA   . PRO A 1 180 ? -21.209 0.456   9.845   1.00 10.04 ? 181 PRO A CA   1 
ATOM   1421 C  C    . PRO A 1 180 ? -22.144 -0.102  10.864  1.00 11.11 ? 181 PRO A C    1 
ATOM   1422 O  O    . PRO A 1 180 ? -21.688 -1.052  11.586  1.00 10.75 ? 181 PRO A O    1 
ATOM   1423 C  CB   . PRO A 1 180 ? -20.185 1.466   10.411  1.00 12.90 ? 181 PRO A CB   1 
ATOM   1424 C  CG   . PRO A 1 180 ? -20.854 2.816   10.380  1.00 12.46 ? 181 PRO A CG   1 
ATOM   1425 C  CD   . PRO A 1 180 ? -21.664 2.725   8.976   1.00 13.03 ? 181 PRO A CD   1 
ATOM   1426 N  N    . ARG A 1 181 ? -23.422 0.238   10.885  1.00 11.15 ? 182 ARG A N    1 
ATOM   1427 C  CA   . ARG A 1 181 ? -24.331 -0.461  11.821  1.00 12.54 ? 182 ARG A CA   1 
ATOM   1428 C  C    . ARG A 1 181 ? -24.432 -1.988  11.487  1.00 11.88 ? 182 ARG A C    1 
ATOM   1429 O  O    . ARG A 1 181 ? -24.854 -2.757  12.331  1.00 13.31 ? 182 ARG A O    1 
ATOM   1430 C  CB   . ARG A 1 181 ? -25.791 0.126   11.785  1.00 10.72 ? 182 ARG A CB   1 
ATOM   1431 C  CG   . ARG A 1 181 ? -25.714 1.586   12.309  1.00 15.95 ? 182 ARG A CG   1 
ATOM   1432 C  CD   . ARG A 1 181 ? -27.066 2.366   12.238  1.00 17.50 ? 182 ARG A CD   1 
ATOM   1433 N  NE   . ARG A 1 181 ? -27.374 2.570   10.850  1.00 17.19 ? 182 ARG A NE   1 
ATOM   1434 C  CZ   . ARG A 1 181 ? -28.505 3.157   10.422  1.00 21.66 ? 182 ARG A CZ   1 
ATOM   1435 N  NH1  . ARG A 1 181 ? -29.410 3.496   11.319  1.00 22.80 ? 182 ARG A NH1  1 
ATOM   1436 N  NH2  . ARG A 1 181 ? -28.757 3.240   9.108   1.00 22.24 ? 182 ARG A NH2  1 
ATOM   1437 N  N    . GLY A 1 182 ? -24.261 -2.297  10.207  1.00 12.06 ? 183 GLY A N    1 
ATOM   1438 C  CA   . GLY A 1 182 ? -24.359 -3.689  9.817   1.00 12.77 ? 183 GLY A CA   1 
ATOM   1439 C  C    . GLY A 1 182 ? -23.186 -4.555  10.373  1.00 13.54 ? 183 GLY A C    1 
ATOM   1440 O  O    . GLY A 1 182 ? -23.126 -5.779  10.068  1.00 15.60 ? 183 GLY A O    1 
ATOM   1441 N  N    . LEU A 1 183 ? -22.187 -3.943  11.067  1.00 13.59 ? 184 LEU A N    1 
ATOM   1442 C  CA   . LEU A 1 183 ? -21.023 -4.754  11.624  1.00 12.30 ? 184 LEU A CA   1 
ATOM   1443 C  C    . LEU A 1 183 ? -21.227 -4.891  13.094  1.00 9.78  ? 184 LEU A C    1 
ATOM   1444 O  O    . LEU A 1 183 ? -20.303 -5.458  13.767  1.00 12.55 ? 184 LEU A O    1 
ATOM   1445 C  CB   . LEU A 1 183 ? -19.736 -4.010  11.376  1.00 11.56 ? 184 LEU A CB   1 
ATOM   1446 C  CG   . LEU A 1 183 ? -19.372 -3.857  9.883   1.00 13.17 ? 184 LEU A CG   1 
ATOM   1447 C  CD1  . LEU A 1 183 ? -18.148 -3.043  9.686   1.00 15.68 ? 184 LEU A CD1  1 
ATOM   1448 C  CD2  . LEU A 1 183 ? -19.312 -5.171  9.139   1.00 16.93 ? 184 LEU A CD2  1 
ATOM   1449 N  N    . LEU A 1 184 ? -22.309 -4.484  13.736  1.00 10.76 ? 185 LEU A N    1 
ATOM   1450 C  CA   . LEU A 1 184 ? -22.397 -4.498  15.215  1.00 9.45  ? 185 LEU A CA   1 
ATOM   1451 C  C    . LEU A 1 184 ? -23.226 -5.714  15.715  1.00 13.71 ? 185 LEU A C    1 
ATOM   1452 O  O    . LEU A 1 184 ? -24.326 -6.070  15.172  1.00 15.20 ? 185 LEU A O    1 
ATOM   1453 C  CB   . LEU A 1 184 ? -23.183 -3.239  15.690  1.00 9.36  ? 185 LEU A CB   1 
ATOM   1454 C  CG   . LEU A 1 184 ? -22.639 -1.900  15.295  1.00 10.35 ? 185 LEU A CG   1 
ATOM   1455 C  CD1  . LEU A 1 184 ? -23.454 -0.742  15.759  1.00 13.91 ? 185 LEU A CD1  1 
ATOM   1456 C  CD2  . LEU A 1 184 ? -21.129 -1.763  15.799  1.00 14.69 ? 185 LEU A CD2  1 
ATOM   1457 N  N    . PRO A 1 185 ? -22.820 -6.356  16.787  1.00 11.18 ? 186 PRO A N    1 
ATOM   1458 C  CA   . PRO A 1 185 ? -23.585 -7.466  17.306  1.00 11.85 ? 186 PRO A CA   1 
ATOM   1459 C  C    . PRO A 1 185 ? -24.859 -6.921  17.950  1.00 12.22 ? 186 PRO A C    1 
ATOM   1460 O  O    . PRO A 1 185 ? -24.995 -5.724  18.098  1.00 12.93 ? 186 PRO A O    1 
ATOM   1461 C  CB   . PRO A 1 185 ? -22.631 -8.067  18.335  1.00 11.74 ? 186 PRO A CB   1 
ATOM   1462 C  CG   . PRO A 1 185 ? -21.852 -6.834  18.873  1.00 9.67  ? 186 PRO A CG   1 
ATOM   1463 C  CD   . PRO A 1 185 ? -21.645 -5.934  17.611  1.00 11.43 ? 186 PRO A CD   1 
ATOM   1464 N  N    . GLU A 1 186 ? -25.725 -7.802  18.463  1.00 13.62 ? 187 GLU A N    1 
ATOM   1465 C  CA   . GLU A 1 186 ? -26.966 -7.362  19.095  1.00 12.90 ? 187 GLU A CA   1 
ATOM   1466 C  C    . GLU A 1 186 ? -26.688 -6.625  20.351  1.00 14.08 ? 187 GLU A C    1 
ATOM   1467 O  O    . GLU A 1 186 ? -27.325 -5.590  20.617  1.00 16.58 ? 187 GLU A O    1 
ATOM   1468 C  CB   . GLU A 1 186 ? -27.852 -8.547  19.482  1.00 15.48 ? 187 GLU A CB   1 
ATOM   1469 C  CG   . GLU A 1 186 ? -28.593 -9.275  18.417  1.00 22.59 ? 187 GLU A CG   1 
ATOM   1470 C  CD   . GLU A 1 186 ? -29.232 -10.619 18.984  1.00 17.46 ? 187 GLU A CD   1 
ATOM   1471 O  OE1  . GLU A 1 186 ? -29.278 -10.830 20.190  1.00 21.72 ? 187 GLU A OE1  1 
ATOM   1472 O  OE2  . GLU A 1 186 ? -29.716 -11.392 18.143  1.00 30.61 ? 187 GLU A OE2  1 
ATOM   1473 N  N    . SER A 1 187 ? -25.821 -7.204  21.237  1.00 12.88 ? 188 SER A N    1 
ATOM   1474 C  CA   . SER A 1 187 ? -25.649 -6.612  22.504  1.00 13.95 ? 188 SER A CA   1 
ATOM   1475 C  C    . SER A 1 187 ? -24.473 -5.561  22.484  1.00 12.07 ? 188 SER A C    1 
ATOM   1476 O  O    . SER A 1 187 ? -23.450 -5.829  21.803  1.00 14.00 ? 188 SER A O    1 
ATOM   1477 C  CB   . SER A 1 187 ? -25.156 -7.622  23.502  1.00 13.91 ? 188 SER A CB   1 
ATOM   1478 O  OG   . SER A 1 187 ? -24.981 -7.061  24.791  1.00 16.12 ? 188 SER A OG   1 
ATOM   1479 N  N    . LEU A 1 188 ? -24.602 -4.508  23.251  1.00 11.09 ? 189 LEU A N    1 
ATOM   1480 C  CA   . LEU A 1 188 ? -23.520 -3.480  23.430  1.00 11.85 ? 189 LEU A CA   1 
ATOM   1481 C  C    . LEU A 1 188 ? -22.939 -3.626  24.829  1.00 10.82 ? 189 LEU A C    1 
ATOM   1482 O  O    . LEU A 1 188 ? -22.198 -2.729  25.293  1.00 13.60 ? 189 LEU A O    1 
ATOM   1483 C  CB   . LEU A 1 188 ? -24.036 -2.017  23.145  1.00 11.42 ? 189 LEU A CB   1 
ATOM   1484 C  CG   . LEU A 1 188 ? -24.507 -1.765  21.714  1.00 16.08 ? 189 LEU A CG   1 
ATOM   1485 C  CD1  . LEU A 1 188 ? -25.000 -0.308  21.610  1.00 17.55 ? 189 LEU A CD1  1 
ATOM   1486 C  CD2  . LEU A 1 188 ? -23.324 -1.942  20.759  1.00 14.93 ? 189 LEU A CD2  1 
ATOM   1487 N  N    . ASP A 1 189 ? -23.015 -4.755  25.484  1.00 12.15 ? 190 ASP A N    1 
ATOM   1488 C  CA   . ASP A 1 189 ? -22.278 -5.025  26.750  1.00 12.63 ? 190 ASP A CA   1 
ATOM   1489 C  C    . ASP A 1 189 ? -20.758 -5.011  26.408  1.00 10.42 ? 190 ASP A C    1 
ATOM   1490 O  O    . ASP A 1 189 ? -20.390 -5.474  25.340  1.00 9.76  ? 190 ASP A O    1 
ATOM   1491 C  CB   . ASP A 1 189 ? -22.612 -6.447  27.314  1.00 13.09 ? 190 ASP A CB   1 
ATOM   1492 C  CG   . ASP A 1 189 ? -24.038 -6.563  28.003  1.00 17.91 ? 190 ASP A CG   1 
ATOM   1493 O  OD1  . ASP A 1 189 ? -24.637 -5.557  28.267  1.00 22.53 ? 190 ASP A OD1  1 
ATOM   1494 O  OD2  . ASP A 1 189 ? -24.382 -7.719  28.222  1.00 25.78 ? 190 ASP A OD2  1 
ATOM   1495 N  N    . TYR A 1 190 ? -19.967 -4.389  27.334  1.00 9.04  ? 191 TYR A N    1 
ATOM   1496 C  CA   . TYR A 1 190 ? -18.557 -4.188  26.965  1.00 9.16  ? 191 TYR A CA   1 
ATOM   1497 C  C    . TYR A 1 190 ? -17.681 -4.260  28.206  1.00 9.93  ? 191 TYR A C    1 
ATOM   1498 O  O    . TYR A 1 190 ? -18.081 -4.104  29.407  1.00 9.85  ? 191 TYR A O    1 
ATOM   1499 C  CB   . TYR A 1 190 ? -18.417 -2.774  26.342  1.00 10.89 ? 191 TYR A CB   1 
ATOM   1500 C  CG   . TYR A 1 190 ? -18.842 -1.639  27.184  1.00 9.81  ? 191 TYR A CG   1 
ATOM   1501 C  CD1  . TYR A 1 190 ? -17.920 -1.003  28.091  1.00 9.83  ? 191 TYR A CD1  1 
ATOM   1502 C  CD2  . TYR A 1 190 ? -20.150 -1.128  27.149  1.00 11.63 ? 191 TYR A CD2  1 
ATOM   1503 C  CE1  . TYR A 1 190 ? -18.334 -0.006  28.896  1.00 9.93  ? 191 TYR A CE1  1 
ATOM   1504 C  CE2  . TYR A 1 190 ? -20.554 -0.025  27.958  1.00 11.77 ? 191 TYR A CE2  1 
ATOM   1505 C  CZ   . TYR A 1 190 ? -19.624 0.552   28.848  1.00 12.75 ? 191 TYR A CZ   1 
ATOM   1506 O  OH   . TYR A 1 190 ? -19.987 1.557   29.709  1.00 12.54 ? 191 TYR A OH   1 
ATOM   1507 N  N    . TRP A 1 191 ? -16.379 -4.396  27.929  1.00 7.98  ? 192 TRP A N    1 
ATOM   1508 C  CA   . TRP A 1 191 ? -15.303 -4.140  28.917  1.00 7.22  ? 192 TRP A CA   1 
ATOM   1509 C  C    . TRP A 1 191 ? -14.618 -2.848  28.451  1.00 9.33  ? 192 TRP A C    1 
ATOM   1510 O  O    . TRP A 1 191 ? -14.615 -2.496  27.265  1.00 8.58  ? 192 TRP A O    1 
ATOM   1511 C  CB   . TRP A 1 191 ? -14.291 -5.243  28.799  1.00 8.90  ? 192 TRP A CB   1 
ATOM   1512 C  CG   . TRP A 1 191 ? -14.805 -6.567  29.238  1.00 7.79  ? 192 TRP A CG   1 
ATOM   1513 C  CD1  . TRP A 1 191 ? -15.054 -7.013  30.554  1.00 10.31 ? 192 TRP A CD1  1 
ATOM   1514 C  CD2  . TRP A 1 191 ? -15.064 -7.720  28.383  1.00 8.76  ? 192 TRP A CD2  1 
ATOM   1515 N  NE1  . TRP A 1 191 ? -15.464 -8.335  30.494  1.00 10.14 ? 192 TRP A NE1  1 
ATOM   1516 C  CE2  . TRP A 1 191 ? -15.522 -8.775  29.199  1.00 8.84  ? 192 TRP A CE2  1 
ATOM   1517 C  CE3  . TRP A 1 191 ? -14.995 -7.906  27.000  1.00 8.47  ? 192 TRP A CE3  1 
ATOM   1518 C  CZ2  . TRP A 1 191 ? -15.792 -10.049 28.646  1.00 10.68 ? 192 TRP A CZ2  1 
ATOM   1519 C  CZ3  . TRP A 1 191 ? -15.249 -9.149  26.470  1.00 8.82  ? 192 TRP A CZ3  1 
ATOM   1520 C  CH2  . TRP A 1 191 ? -15.663 -10.192 27.299  1.00 11.20 ? 192 TRP A CH2  1 
ATOM   1521 N  N    . THR A 1 192 ? -13.997 -2.158  29.383  1.00 7.24  ? 193 THR A N    1 
ATOM   1522 C  CA   . THR A 1 192 ? -13.290 -0.937  29.023  1.00 7.44  ? 193 THR A CA   1 
ATOM   1523 C  C    . THR A 1 192 ? -12.067 -0.723  29.914  1.00 7.59  ? 193 THR A C    1 
ATOM   1524 O  O    . THR A 1 192 ? -12.031 -1.139  31.081  1.00 8.35  ? 193 THR A O    1 
ATOM   1525 C  CB   . THR A 1 192 ? -14.250 0.284   29.131  1.00 7.15  ? 193 THR A CB   1 
ATOM   1526 O  OG1  . THR A 1 192 ? -13.588 1.503   28.751  1.00 8.48  ? 193 THR A OG1  1 
ATOM   1527 C  CG2  . THR A 1 192 ? -14.723 0.522   30.561  1.00 9.92  ? 193 THR A CG2  1 
ATOM   1528 N  N    . TYR A 1 193 ? -11.007 -0.126  29.341  1.00 8.63  ? 194 TYR A N    1 
ATOM   1529 C  CA   . TYR A 1 193 ? -9.779  0.138   30.101  1.00 7.52  ? 194 TYR A CA   1 
ATOM   1530 C  C    . TYR A 1 193 ? -9.003  1.140   29.296  1.00 8.79  ? 194 TYR A C    1 
ATOM   1531 O  O    . TYR A 1 193 ? -9.250  1.337   28.110  1.00 7.46  ? 194 TYR A O    1 
ATOM   1532 C  CB   . TYR A 1 193 ? -8.942  -1.116  30.246  1.00 8.28  ? 194 TYR A CB   1 
ATOM   1533 C  CG   . TYR A 1 193 ? -8.243  -1.604  29.000  1.00 5.75  ? 194 TYR A CG   1 
ATOM   1534 C  CD1  . TYR A 1 193 ? -8.926  -2.391  28.023  1.00 7.63  ? 194 TYR A CD1  1 
ATOM   1535 C  CD2  . TYR A 1 193 ? -6.925  -1.275  28.758  1.00 8.86  ? 194 TYR A CD2  1 
ATOM   1536 C  CE1  . TYR A 1 193 ? -8.301  -2.668  26.856  1.00 5.95  ? 194 TYR A CE1  1 
ATOM   1537 C  CE2  . TYR A 1 193 ? -6.281  -1.603  27.602  1.00 6.57  ? 194 TYR A CE2  1 
ATOM   1538 C  CZ   . TYR A 1 193 ? -6.966  -2.303  26.627  1.00 7.05  ? 194 TYR A CZ   1 
ATOM   1539 O  OH   . TYR A 1 193 ? -6.358  -2.639  25.446  1.00 6.98  ? 194 TYR A OH   1 
ATOM   1540 N  N    . PRO A 1 194 ? -8.088  1.910   29.920  1.00 7.96  ? 195 PRO A N    1 
ATOM   1541 C  CA   . PRO A 1 194 ? -7.282  2.888   29.276  1.00 7.99  ? 195 PRO A CA   1 
ATOM   1542 C  C    . PRO A 1 194 ? -6.049  2.304   28.588  1.00 6.60  ? 195 PRO A C    1 
ATOM   1543 O  O    . PRO A 1 194 ? -5.303  1.506   29.261  1.00 8.80  ? 195 PRO A O    1 
ATOM   1544 C  CB   . PRO A 1 194 ? -6.761  3.758   30.465  1.00 9.80  ? 195 PRO A CB   1 
ATOM   1545 C  CG   . PRO A 1 194 ? -6.744  2.819   31.650  1.00 8.77  ? 195 PRO A CG   1 
ATOM   1546 C  CD   . PRO A 1 194 ? -7.925  1.883   31.408  1.00 10.03 ? 195 PRO A CD   1 
ATOM   1547 N  N    . GLY A 1 195 ? -5.814  2.597   27.346  1.00 6.29  ? 196 GLY A N    1 
ATOM   1548 C  CA   . GLY A 1 195 ? -4.726  1.903   26.605  1.00 8.19  ? 196 GLY A CA   1 
ATOM   1549 C  C    . GLY A 1 195 ? -4.190  2.800   25.557  1.00 6.29  ? 196 GLY A C    1 
ATOM   1550 O  O    . GLY A 1 195 ? -4.084  4.007   25.675  1.00 6.94  ? 196 GLY A O    1 
ATOM   1551 N  N    . SER A 1 196 ? -3.793  2.132   24.490  1.00 6.47  ? 197 SER A N    1 
ATOM   1552 C  CA   . SER A 1 196 ? -2.991  2.816   23.466  1.00 6.35  ? 197 SER A CA   1 
ATOM   1553 C  C    . SER A 1 196 ? -3.423  2.402   22.049  1.00 6.20  ? 197 SER A C    1 
ATOM   1554 O  O    . SER A 1 196 ? -4.125  1.407   21.888  1.00 6.78  ? 197 SER A O    1 
ATOM   1555 C  CB   . SER A 1 196 ? -1.460  2.413   23.589  1.00 9.43  ? 197 SER A CB   1 
ATOM   1556 O  OG   . SER A 1 196 ? -1.237  1.050   23.204  1.00 6.72  ? 197 SER A OG   1 
ATOM   1557 N  N    . LEU A 1 197 ? -2.848  3.054   21.063  1.00 6.47  ? 198 LEU A N    1 
ATOM   1558 C  CA   . LEU A 1 197 ? -2.873  2.427   19.704  1.00 7.12  ? 198 LEU A CA   1 
ATOM   1559 C  C    . LEU A 1 197 ? -2.213  1.123   19.786  1.00 7.12  ? 198 LEU A C    1 
ATOM   1560 O  O    . LEU A 1 197 ? -1.150  0.957   20.524  1.00 7.81  ? 198 LEU A O    1 
ATOM   1561 C  CB   . LEU A 1 197 ? -2.055  3.242   18.748  1.00 9.01  ? 198 LEU A CB   1 
ATOM   1562 C  CG   . LEU A 1 197 ? -2.391  4.698   18.661  1.00 15.02 ? 198 LEU A CG   1 
ATOM   1563 C  CD1  . LEU A 1 197 ? -1.535  5.331   17.467  1.00 15.02 ? 198 LEU A CD1  1 
ATOM   1564 C  CD2  . LEU A 1 197 ? -3.711  5.252   18.680  1.00 13.75 ? 198 LEU A CD2  1 
ATOM   1565 N  N    . THR A 1 198 ? -2.643  0.153   19.002  1.00 6.05  ? 199 THR A N    1 
ATOM   1566 C  CA   . THR A 1 198 ? -1.979  -1.128  18.983  1.00 8.08  ? 199 THR A CA   1 
ATOM   1567 C  C    . THR A 1 198 ? -0.952  -1.160  17.860  1.00 7.21  ? 199 THR A C    1 
ATOM   1568 O  O    . THR A 1 198 ? -0.351  -2.175  17.671  1.00 8.11  ? 199 THR A O    1 
ATOM   1569 C  CB   . THR A 1 198 ? -2.999  -2.277  18.817  1.00 6.76  ? 199 THR A CB   1 
ATOM   1570 O  OG1  . THR A 1 198 ? -3.562  -2.162  17.496  1.00 6.97  ? 199 THR A OG1  1 
ATOM   1571 C  CG2  . THR A 1 198 ? -3.960  -2.245  19.868  1.00 7.35  ? 199 THR A CG2  1 
ATOM   1572 N  N    . THR A 1 199 ? -0.848  -0.094  17.081  1.00 8.09  ? 200 THR A N    1 
ATOM   1573 C  CA   . THR A 1 199 ? 0.167   -0.006  16.026  1.00 10.16 ? 200 THR A CA   1 
ATOM   1574 C  C    . THR A 1 199 ? 1.025   1.196   16.317  1.00 10.93 ? 200 THR A C    1 
ATOM   1575 O  O    . THR A 1 199 ? 0.602   2.157   16.919  1.00 10.11 ? 200 THR A O    1 
ATOM   1576 C  CB   . THR A 1 199 ? -0.456  0.256   14.664  1.00 11.27 ? 200 THR A CB   1 
ATOM   1577 O  OG1  . THR A 1 199 ? -1.209  1.461   14.726  1.00 14.27 ? 200 THR A OG1  1 
ATOM   1578 C  CG2  . THR A 1 199 ? -1.373  -0.837  14.295  1.00 12.29 ? 200 THR A CG2  1 
ATOM   1579 N  N    . PRO A 1 200 ? 2.325   1.151   15.892  1.00 10.22 ? 201 PRO A N    1 
ATOM   1580 C  CA   . PRO A 1 200 ? 3.116   2.404   15.975  1.00 10.22 ? 201 PRO A CA   1 
ATOM   1581 C  C    . PRO A 1 200 ? 2.253   3.556   15.439  1.00 10.16 ? 201 PRO A C    1 
ATOM   1582 O  O    . PRO A 1 200 ? 1.566   3.397   14.368  1.00 11.40 ? 201 PRO A O    1 
ATOM   1583 C  CB   . PRO A 1 200 ? 4.320   2.073   15.062  1.00 10.31 ? 201 PRO A CB   1 
ATOM   1584 C  CG   . PRO A 1 200 ? 4.521   0.628   15.231  1.00 10.03 ? 201 PRO A CG   1 
ATOM   1585 C  CD   . PRO A 1 200 ? 3.032   0.061   15.204  1.00 11.14 ? 201 PRO A CD   1 
ATOM   1586 N  N    . PRO A 1 201 ? 2.327   4.770   15.975  1.00 9.57  ? 202 PRO A N    1 
ATOM   1587 C  CA   . PRO A 1 201 ? 3.266   5.098   17.062  1.00 11.27 ? 202 PRO A CA   1 
ATOM   1588 C  C    . PRO A 1 201 ? 2.897   4.760   18.501  1.00 10.45 ? 202 PRO A C    1 
ATOM   1589 O  O    . PRO A 1 201 ? 3.560   5.139   19.434  1.00 10.92 ? 202 PRO A O    1 
ATOM   1590 C  CB   . PRO A 1 201 ? 3.356   6.618   16.914  1.00 11.54 ? 202 PRO A CB   1 
ATOM   1591 C  CG   . PRO A 1 201 ? 1.915   7.042   16.407  1.00 13.93 ? 202 PRO A CG   1 
ATOM   1592 C  CD   . PRO A 1 201 ? 1.560   5.923   15.435  1.00 10.37 ? 202 PRO A CD   1 
ATOM   1593 N  N    . LEU A 1 202 ? 1.887   3.874   18.700  1.00 9.17  ? 203 LEU A N    1 
ATOM   1594 C  CA   . LEU A 1 202 ? 1.667   3.298   19.992  1.00 8.18  ? 203 LEU A CA   1 
ATOM   1595 C  C    . LEU A 1 202 ? 1.310   4.326   21.096  1.00 7.54  ? 203 LEU A C    1 
ATOM   1596 O  O    . LEU A 1 202 ? 1.441   4.026   22.237  1.00 8.23  ? 203 LEU A O    1 
ATOM   1597 C  CB   . LEU A 1 202 ? 2.835   2.429   20.442  1.00 8.46  ? 203 LEU A CB   1 
ATOM   1598 C  CG   . LEU A 1 202 ? 3.107   1.233   19.479  1.00 8.72  ? 203 LEU A CG   1 
ATOM   1599 C  CD1  . LEU A 1 202 ? 4.416   0.563   19.938  1.00 11.77 ? 203 LEU A CD1  1 
ATOM   1600 C  CD2  . LEU A 1 202 ? 2.012   0.140   19.501  1.00 11.05 ? 203 LEU A CD2  1 
ATOM   1601 N  N    . LEU A 1 203 ? 0.701   5.428   20.627  1.00 8.03  ? 204 LEU A N    1 
ATOM   1602 C  CA   . LEU A 1 203 ? 0.418   6.521   21.553  1.00 7.98  ? 204 LEU A CA   1 
ATOM   1603 C  C    . LEU A 1 203 ? -0.606  6.136   22.577  1.00 7.41  ? 204 LEU A C    1 
ATOM   1604 O  O    . LEU A 1 203 ? -1.605  5.359   22.317  1.00 9.04  ? 204 LEU A O    1 
ATOM   1605 C  CB   . LEU A 1 203 ? -0.088  7.737   20.822  1.00 11.28 ? 204 LEU A CB   1 
ATOM   1606 C  CG   . LEU A 1 203 ? 0.937   8.287   19.799  1.00 10.70 ? 204 LEU A CG   1 
ATOM   1607 C  CD1  . LEU A 1 203 ? 0.373   9.340   18.900  1.00 11.93 ? 204 LEU A CD1  1 
ATOM   1608 C  CD2  . LEU A 1 203 ? 2.145   8.960   20.506  1.00 15.98 ? 204 LEU A CD2  1 
ATOM   1609 N  N    . GLU A 1 204 ? -0.448  6.579   23.796  1.00 9.50  ? 205 GLU A N    1 
ATOM   1610 C  CA   . GLU A 1 204 ? -1.245  6.192   24.926  1.00 9.23  ? 205 GLU A CA   1 
ATOM   1611 C  C    . GLU A 1 204 ? -2.408  7.191   25.078  1.00 10.54 ? 205 GLU A C    1 
ATOM   1612 O  O    . GLU A 1 204 ? -2.555  7.918   26.065  1.00 12.01 ? 205 GLU A O    1 
ATOM   1613 C  CB   . GLU A 1 204 ? -0.403  6.088   26.234  1.00 9.58  ? 205 GLU A CB   1 
ATOM   1614 C  CG   . GLU A 1 204 ? 0.492   4.873   26.095  1.00 11.54 ? 205 GLU A CG   1 
ATOM   1615 C  CD   . GLU A 1 204 ? 1.404   4.586   27.259  1.00 14.46 ? 205 GLU A CD   1 
ATOM   1616 O  OE1  . GLU A 1 204 ? 1.687   5.550   28.018  1.00 15.57 ? 205 GLU A OE1  1 
ATOM   1617 O  OE2  . GLU A 1 204 ? 1.786   3.410   27.401  1.00 11.39 ? 205 GLU A OE2  1 
ATOM   1618 N  N    . CYS A 1 205 ? -3.331  7.081   24.135  1.00 9.73  ? 206 CYS A N    1 
ATOM   1619 C  CA   . CYS A 1 205 ? -4.419  8.048   23.930  1.00 7.94  ? 206 CYS A CA   1 
ATOM   1620 C  C    . CYS A 1 205 ? -5.748  7.355   23.810  1.00 7.17  ? 206 CYS A C    1 
ATOM   1621 O  O    . CYS A 1 205 ? -6.729  8.124   23.477  1.00 9.04  ? 206 CYS A O    1 
ATOM   1622 C  CB   . CYS A 1 205 ? -4.171  8.933   22.723  1.00 9.41  ? 206 CYS A CB   1 
ATOM   1623 S  SG   . CYS A 1 205 ? -4.088  7.961   21.184  1.00 10.47 ? 206 CYS A SG   1 
ATOM   1624 N  N    . VAL A 1 206 ? -5.915  6.093   24.105  1.00 6.67  ? 207 VAL A N    1 
ATOM   1625 C  CA   . VAL A 1 206 ? -7.191  5.424   23.751  1.00 6.35  ? 207 VAL A CA   1 
ATOM   1626 C  C    . VAL A 1 206 ? -7.955  4.956   24.969  1.00 7.44  ? 207 VAL A C    1 
ATOM   1627 O  O    . VAL A 1 206 ? -7.388  4.325   25.834  1.00 8.00  ? 207 VAL A O    1 
ATOM   1628 C  CB   . VAL A 1 206 ? -6.871  4.156   22.967  1.00 7.12  ? 207 VAL A CB   1 
ATOM   1629 C  CG1  . VAL A 1 206 ? -8.194  3.415   22.550  1.00 7.37  ? 207 VAL A CG1  1 
ATOM   1630 C  CG2  . VAL A 1 206 ? -6.177  4.500   21.652  1.00 9.62  ? 207 VAL A CG2  1 
ATOM   1631 N  N    . THR A 1 207 ? -9.273  5.246   25.029  1.00 7.45  ? 208 THR A N    1 
ATOM   1632 C  CA   . THR A 1 207 ? -10.181 4.532   25.871  1.00 6.81  ? 208 THR A CA   1 
ATOM   1633 C  C    . THR A 1 207 ? -10.706 3.363   25.069  1.00 7.79  ? 208 THR A C    1 
ATOM   1634 O  O    . THR A 1 207 ? -11.382 3.560   24.029  1.00 6.75  ? 208 THR A O    1 
ATOM   1635 C  CB   . THR A 1 207 ? -11.393 5.392   26.330  1.00 7.88  ? 208 THR A CB   1 
ATOM   1636 O  OG1  . THR A 1 207 ? -10.826 6.525   27.035  1.00 9.07  ? 208 THR A OG1  1 
ATOM   1637 C  CG2  . THR A 1 207 ? -12.317 4.638   27.272  1.00 9.51  ? 208 THR A CG2  1 
ATOM   1638 N  N    . TRP A 1 208 ? -10.336 2.141   25.421  1.00 6.71  ? 209 TRP A N    1 
ATOM   1639 C  CA   . TRP A 1 208 ? -10.794 0.941   24.730  1.00 7.22  ? 209 TRP A CA   1 
ATOM   1640 C  C    . TRP A 1 208 ? -12.150 0.529   25.276  1.00 6.90  ? 209 TRP A C    1 
ATOM   1641 O  O    . TRP A 1 208 ? -12.373 0.453   26.463  1.00 6.26  ? 209 TRP A O    1 
ATOM   1642 C  CB   . TRP A 1 208 ? -9.787  -0.213  24.964  1.00 6.89  ? 209 TRP A CB   1 
ATOM   1643 C  CG   . TRP A 1 208 ? -8.680  -0.102  24.005  1.00 6.10  ? 209 TRP A CG   1 
ATOM   1644 C  CD1  . TRP A 1 208 ? -7.428  0.542   24.203  1.00 6.58  ? 209 TRP A CD1  1 
ATOM   1645 C  CD2  . TRP A 1 208 ? -8.710  -0.471  22.637  1.00 6.82  ? 209 TRP A CD2  1 
ATOM   1646 N  NE1  . TRP A 1 208 ? -6.757  0.519   23.031  1.00 7.65  ? 209 TRP A NE1  1 
ATOM   1647 C  CE2  . TRP A 1 208 ? -7.461  -0.120  22.036  1.00 6.37  ? 209 TRP A CE2  1 
ATOM   1648 C  CE3  . TRP A 1 208 ? -9.696  -1.134  21.837  1.00 5.36  ? 209 TRP A CE3  1 
ATOM   1649 C  CZ2  . TRP A 1 208 ? -7.180  -0.313  20.701  1.00 7.29  ? 209 TRP A CZ2  1 
ATOM   1650 C  CZ3  . TRP A 1 208 ? -9.438  -1.351  20.574  1.00 8.15  ? 209 TRP A CZ3  1 
ATOM   1651 C  CH2  . TRP A 1 208 ? -8.189  -0.923  19.997  1.00 7.59  ? 209 TRP A CH2  1 
ATOM   1652 N  N    . ILE A 1 209 ? -13.047 0.203   24.325  1.00 7.06  ? 210 ILE A N    1 
ATOM   1653 C  CA   . ILE A 1 209 ? -14.389 -0.321  24.683  1.00 6.80  ? 210 ILE A CA   1 
ATOM   1654 C  C    . ILE A 1 209 ? -14.518 -1.581  23.874  1.00 7.38  ? 210 ILE A C    1 
ATOM   1655 O  O    . ILE A 1 209 ? -14.633 -1.488  22.641  1.00 7.21  ? 210 ILE A O    1 
ATOM   1656 C  CB   . ILE A 1 209 ? -15.424 0.718   24.290  1.00 7.94  ? 210 ILE A CB   1 
ATOM   1657 C  CG1  . ILE A 1 209 ? -15.150 1.981   25.121  1.00 8.06  ? 210 ILE A CG1  1 
ATOM   1658 C  CG2  . ILE A 1 209 ? -16.879 0.099   24.518  1.00 10.54 ? 210 ILE A CG2  1 
ATOM   1659 C  CD1  . ILE A 1 209 ? -16.013 3.181   24.693  1.00 12.55 ? 210 ILE A CD1  1 
ATOM   1660 N  N    . VAL A 1 210 ? -14.443 -2.748  24.492  1.00 7.60  ? 211 VAL A N    1 
ATOM   1661 C  CA   . VAL A 1 210 ? -14.386 -4.047  23.749  1.00 7.28  ? 211 VAL A CA   1 
ATOM   1662 C  C    . VAL A 1 210 ? -15.738 -4.742  24.032  1.00 8.08  ? 211 VAL A C    1 
ATOM   1663 O  O    . VAL A 1 210 ? -16.050 -4.973  25.149  1.00 7.94  ? 211 VAL A O    1 
ATOM   1664 C  CB   . VAL A 1 210 ? -13.197 -4.870  24.216  1.00 7.20  ? 211 VAL A CB   1 
ATOM   1665 C  CG1  . VAL A 1 210 ? -13.194 -6.245  23.494  1.00 8.46  ? 211 VAL A CG1  1 
ATOM   1666 C  CG2  . VAL A 1 210 ? -11.886 -4.071  23.907  1.00 7.99  ? 211 VAL A CG2  1 
ATOM   1667 N  N    . LEU A 1 211 ? -16.469 -4.992  22.960  1.00 7.47  ? 212 LEU A N    1 
ATOM   1668 C  CA   . LEU A 1 211 ? -17.780 -5.672  23.107  1.00 7.30  ? 212 LEU A CA   1 
ATOM   1669 C  C    . LEU A 1 211 ? -17.604 -7.113  23.506  1.00 7.32  ? 212 LEU A C    1 
ATOM   1670 O  O    . LEU A 1 211 ? -16.778 -7.809  22.951  1.00 8.46  ? 212 LEU A O    1 
ATOM   1671 C  CB   . LEU A 1 211 ? -18.526 -5.519  21.793  1.00 7.76  ? 212 LEU A CB   1 
ATOM   1672 C  CG   . LEU A 1 211 ? -18.949 -4.085  21.485  1.00 8.73  ? 212 LEU A CG   1 
ATOM   1673 C  CD1  . LEU A 1 211 ? -20.049 -4.137  20.305  1.00 11.51 ? 212 LEU A CD1  1 
ATOM   1674 C  CD2  . LEU A 1 211 ? -19.463 -3.258  22.669  1.00 10.98 ? 212 LEU A CD2  1 
ATOM   1675 N  N    . LYS A 1 212 ? -18.465 -7.572  24.453  1.00 8.71  ? 213 LYS A N    1 
ATOM   1676 C  CA   . LYS A 1 212 ? -18.397 -8.990  24.820  1.00 9.22  ? 213 LYS A CA   1 
ATOM   1677 C  C    . LYS A 1 212 ? -18.899 -9.937  23.723  1.00 10.26 ? 213 LYS A C    1 
ATOM   1678 O  O    . LYS A 1 212 ? -18.391 -11.017 23.542  1.00 12.31 ? 213 LYS A O    1 
ATOM   1679 C  CB   . LYS A 1 212 ? -19.208 -9.213  26.104  1.00 12.55 ? 213 LYS A CB   1 
ATOM   1680 C  CG   . LYS A 1 212 ? -19.448 -10.718 26.557  1.00 16.35 ? 213 LYS A CG   1 
ATOM   1681 C  CD   . LYS A 1 212 ? -20.679 -10.696 27.549  1.00 21.59 ? 213 LYS A CD   1 
ATOM   1682 C  CE   . LYS A 1 212 ? -22.015 -9.852  27.012  1.00 25.40 ? 213 LYS A CE   1 
ATOM   1683 N  NZ   . LYS A 1 212 ? -22.631 -9.788  25.458  1.00 24.12 ? 213 LYS A NZ   1 
ATOM   1684 N  N    . GLU A 1 213 ? -19.896 -9.513  22.935  1.00 7.58  ? 214 GLU A N    1 
ATOM   1685 C  CA   . GLU A 1 213 ? -20.514 -10.411 21.970  1.00 9.36  ? 214 GLU A CA   1 
ATOM   1686 C  C    . GLU A 1 213 ? -19.783 -10.290 20.622  1.00 8.43  ? 214 GLU A C    1 
ATOM   1687 O  O    . GLU A 1 213 ? -19.684 -9.183  20.049  1.00 8.14  ? 214 GLU A O    1 
ATOM   1688 C  CB   . GLU A 1 213 ? -21.961 -10.006 21.784  1.00 10.15 ? 214 GLU A CB   1 
ATOM   1689 C  CG   . GLU A 1 213 ? -22.679 -10.975 20.869  1.00 13.46 ? 214 GLU A CG   1 
ATOM   1690 C  CD   . GLU A 1 213 ? -24.187 -10.666 20.648  1.00 16.93 ? 214 GLU A CD   1 
ATOM   1691 O  OE1  . GLU A 1 213 ? -24.777 -9.844  21.291  1.00 15.45 ? 214 GLU A OE1  1 
ATOM   1692 O  OE2  . GLU A 1 213 ? -24.741 -11.364 19.735  1.00 28.39 ? 214 GLU A OE2  1 
ATOM   1693 N  N    . PRO A 1 214 ? -19.197 -11.394 20.132  1.00 8.04  ? 215 PRO A N    1 
ATOM   1694 C  CA   . PRO A 1 214 ? -18.581 -11.325 18.823  1.00 8.98  ? 215 PRO A CA   1 
ATOM   1695 C  C    . PRO A 1 214 ? -19.569 -11.288 17.721  1.00 9.85  ? 215 PRO A C    1 
ATOM   1696 O  O    . PRO A 1 214 ? -20.807 -11.621 17.965  1.00 11.37 ? 215 PRO A O    1 
ATOM   1697 C  CB   . PRO A 1 214 ? -17.768 -12.674 18.761  1.00 8.28  ? 215 PRO A CB   1 
ATOM   1698 C  CG   . PRO A 1 214 ? -18.685 -13.590 19.574  1.00 14.73 ? 215 PRO A CG   1 
ATOM   1699 C  CD   . PRO A 1 214 ? -19.207 -12.756 20.717  1.00 9.81  ? 215 PRO A CD   1 
ATOM   1700 N  N    . ILE A 1 215 ? -19.139 -10.912 16.546  1.00 8.43  ? 216 ILE A N    1 
ATOM   1701 C  CA   . ILE A 1 215 ? -19.979 -11.079 15.347  1.00 9.59  ? 216 ILE A CA   1 
ATOM   1702 C  C    . ILE A 1 215 ? -19.463 -12.310 14.671  1.00 10.26 ? 216 ILE A C    1 
ATOM   1703 O  O    . ILE A 1 215 ? -18.282 -12.690 14.832  1.00 10.21 ? 216 ILE A O    1 
ATOM   1704 C  CB   . ILE A 1 215 ? -20.002 -9.925  14.416  1.00 10.79 ? 216 ILE A CB   1 
ATOM   1705 C  CG1  . ILE A 1 215 ? -18.575 -9.559  13.974  1.00 11.08 ? 216 ILE A CG1  1 
ATOM   1706 C  CG2  . ILE A 1 215 ? -20.662 -8.669  15.071  1.00 13.03 ? 216 ILE A CG2  1 
ATOM   1707 C  CD1  . ILE A 1 215 ? -18.558 -8.532  12.762  1.00 13.70 ? 216 ILE A CD1  1 
ATOM   1708 N  N    A SER A 1 216 ? -20.341 -12.907 13.861  0.50 10.29 ? 217 SER A N    1 
ATOM   1709 N  N    B SER A 1 216 ? -20.321 -13.120 14.038  0.50 9.32  ? 217 SER A N    1 
ATOM   1710 C  CA   A SER A 1 216 ? -20.061 -14.066 13.055  0.50 10.63 ? 217 SER A CA   1 
ATOM   1711 C  CA   B SER A 1 216 ? -19.778 -14.214 13.156  0.50 9.93  ? 217 SER A CA   1 
ATOM   1712 C  C    A SER A 1 216 ? -19.697 -13.617 11.616  0.50 9.50  ? 217 SER A C    1 
ATOM   1713 C  C    B SER A 1 216 ? -19.706 -13.749 11.746  0.50 9.10  ? 217 SER A C    1 
ATOM   1714 O  O    A SER A 1 216 ? -20.372 -12.732 11.031  0.50 10.48 ? 217 SER A O    1 
ATOM   1715 O  O    B SER A 1 216 ? -20.666 -13.093 11.292  0.50 8.43  ? 217 SER A O    1 
ATOM   1716 C  CB   A SER A 1 216 ? -21.349 -14.995 13.117  0.50 9.24  ? 217 SER A CB   1 
ATOM   1717 C  CB   B SER A 1 216 ? -20.671 -15.444 13.102  0.50 11.82 ? 217 SER A CB   1 
ATOM   1718 O  OG   A SER A 1 216 ? -21.999 -14.996 11.861  0.50 22.86 ? 217 SER A OG   1 
ATOM   1719 O  OG   B SER A 1 216 ? -20.963 -15.813 14.392  0.50 11.01 ? 217 SER A OG   1 
ATOM   1720 N  N    . VAL A 1 217 ? -18.621 -14.141 11.087  1.00 9.29  ? 218 VAL A N    1 
ATOM   1721 C  CA   . VAL A 1 217 ? -18.362 -13.946 9.708   1.00 9.16  ? 218 VAL A CA   1 
ATOM   1722 C  C    . VAL A 1 217 ? -18.105 -15.317 9.072   1.00 9.96  ? 218 VAL A C    1 
ATOM   1723 O  O    . VAL A 1 217 ? -17.755 -16.274 9.807   1.00 10.32 ? 218 VAL A O    1 
ATOM   1724 C  CB   . VAL A 1 217 ? -17.117 -13.004 9.500   1.00 10.69 ? 218 VAL A CB   1 
ATOM   1725 C  CG1  . VAL A 1 217 ? -17.390 -11.606 10.127  1.00 11.83 ? 218 VAL A CG1  1 
ATOM   1726 C  CG2  . VAL A 1 217 ? -15.798 -13.621 9.983   1.00 11.57 ? 218 VAL A CG2  1 
ATOM   1727 N  N    . SER A 1 218 ? -18.251 -15.452 7.751   1.00 9.74  ? 219 SER A N    1 
ATOM   1728 C  CA   . SER A 1 218 ? -18.032 -16.771 7.241   1.00 10.32 ? 219 SER A CA   1 
ATOM   1729 C  C    . SER A 1 218 ? -16.573 -17.007 6.931   1.00 10.32 ? 219 SER A C    1 
ATOM   1730 O  O    . SER A 1 218 ? -15.729 -16.106 6.797   1.00 10.06 ? 219 SER A O    1 
ATOM   1731 C  CB   . SER A 1 218 ? -18.813 -16.956 5.932   1.00 11.38 ? 219 SER A CB   1 
ATOM   1732 O  OG   . SER A 1 218 ? -18.367 -16.081 4.934   1.00 13.29 ? 219 SER A OG   1 
ATOM   1733 N  N    A SER A 1 219 ? -16.254 -18.287 6.784   0.50 10.08 ? 220 SER A N    1 
ATOM   1734 N  N    B SER A 1 219 ? -16.181 -18.260 6.750   0.50 10.22 ? 220 SER A N    1 
ATOM   1735 C  CA   A SER A 1 219 ? -14.934 -18.681 6.449   0.50 11.61 ? 220 SER A CA   1 
ATOM   1736 C  CA   B SER A 1 219 ? -14.805 -18.588 6.382   0.50 11.85 ? 220 SER A CA   1 
ATOM   1737 C  C    A SER A 1 219 ? -14.549 -17.982 5.170   0.50 12.72 ? 220 SER A C    1 
ATOM   1738 C  C    B SER A 1 219 ? -14.451 -17.964 5.019   0.50 13.23 ? 220 SER A C    1 
ATOM   1739 O  O    A SER A 1 219 ? -13.453 -17.444 5.155   0.50 12.21 ? 220 SER A O    1 
ATOM   1740 O  O    B SER A 1 219 ? -13.285 -17.549 4.707   0.50 12.27 ? 220 SER A O    1 
ATOM   1741 C  CB   A SER A 1 219 ? -14.865 -20.234 6.334   0.50 12.37 ? 220 SER A CB   1 
ATOM   1742 C  CB   B SER A 1 219 ? -14.745 -20.143 6.317   0.50 13.70 ? 220 SER A CB   1 
ATOM   1743 O  OG   A SER A 1 219 ? -15.786 -20.738 5.397   0.50 11.50 ? 220 SER A OG   1 
ATOM   1744 O  OG   B SER A 1 219 ? -13.451 -20.595 6.031   0.50 17.13 ? 220 SER A OG   1 
ATOM   1745 N  N    . GLU A 1 220 ? -15.462 -17.880 4.166   1.00 12.60 ? 221 GLU A N    1 
ATOM   1746 C  CA   . GLU A 1 220 ? -15.160 -17.276 2.850   1.00 12.92 ? 221 GLU A CA   1 
ATOM   1747 C  C    . GLU A 1 220 ? -14.898 -15.739 2.996   1.00 12.69 ? 221 GLU A C    1 
ATOM   1748 O  O    . GLU A 1 220 ? -13.988 -15.204 2.334   1.00 13.22 ? 221 GLU A O    1 
ATOM   1749 C  CB   . GLU A 1 220 ? -16.282 -17.416 1.856   1.00 15.32 ? 221 GLU A CB   1 
ATOM   1750 C  CG   . GLU A 1 220 ? -16.537 -18.907 1.461   1.00 19.41 ? 221 GLU A CG   1 
ATOM   1751 C  CD   . GLU A 1 220 ? -17.621 -19.550 2.308   1.00 25.04 ? 221 GLU A CD   1 
ATOM   1752 O  OE1  . GLU A 1 220 ? -17.964 -19.103 3.408   1.00 19.90 ? 221 GLU A OE1  1 
ATOM   1753 O  OE2  . GLU A 1 220 ? -18.151 -20.618 1.883   1.00 32.52 ? 221 GLU A OE2  1 
ATOM   1754 N  N    . GLN A 1 221 ? -15.601 -15.116 3.934   1.00 10.76 ? 222 GLN A N    1 
ATOM   1755 C  CA   . GLN A 1 221 ? -15.309 -13.693 4.162   1.00 10.99 ? 222 GLN A CA   1 
ATOM   1756 C  C    . GLN A 1 221 ? -13.866 -13.449 4.716   1.00 12.68 ? 222 GLN A C    1 
ATOM   1757 O  O    . GLN A 1 221 ? -13.121 -12.633 4.219   1.00 11.56 ? 222 GLN A O    1 
ATOM   1758 C  CB   . GLN A 1 221 ? -16.327 -13.189 5.151   1.00 12.92 ? 222 GLN A CB   1 
ATOM   1759 C  CG   . GLN A 1 221 ? -17.719 -13.016 4.411   1.00 10.86 ? 222 GLN A CG   1 
ATOM   1760 C  CD   . GLN A 1 221 ? -18.790 -12.454 5.291   1.00 10.01 ? 222 GLN A CD   1 
ATOM   1761 O  OE1  . GLN A 1 221 ? -18.927 -12.781 6.423   1.00 10.51 ? 222 GLN A OE1  1 
ATOM   1762 N  NE2  . GLN A 1 221 ? -19.590 -11.537 4.750   1.00 9.46  ? 222 GLN A NE2  1 
ATOM   1763 N  N    . VAL A 1 222 ? -13.501 -14.239 5.708   1.00 12.32 ? 223 VAL A N    1 
ATOM   1764 C  CA   . VAL A 1 222 ? -12.146 -14.040 6.246   1.00 11.95 ? 223 VAL A CA   1 
ATOM   1765 C  C    . VAL A 1 222 ? -11.026 -14.519 5.277   1.00 13.53 ? 223 VAL A C    1 
ATOM   1766 O  O    . VAL A 1 222 ? -9.908  -13.949 5.213   1.00 11.99 ? 223 VAL A O    1 
ATOM   1767 C  CB   . VAL A 1 222 ? -11.983 -14.619 7.660   1.00 15.87 ? 223 VAL A CB   1 
ATOM   1768 C  CG1  . VAL A 1 222 ? -12.064 -16.091 7.608   1.00 15.54 ? 223 VAL A CG1  1 
ATOM   1769 C  CG2  . VAL A 1 222 ? -10.644 -14.079 8.309   1.00 14.77 ? 223 VAL A CG2  1 
ATOM   1770 N  N    . LEU A 1 223 ? -11.363 -15.528 4.468   1.00 12.75 ? 224 LEU A N    1 
ATOM   1771 C  CA   . LEU A 1 223 ? -10.392 -15.931 3.429   1.00 13.86 ? 224 LEU A CA   1 
ATOM   1772 C  C    . LEU A 1 223 ? -10.051 -14.760 2.501   1.00 15.12 ? 224 LEU A C    1 
ATOM   1773 O  O    . LEU A 1 223 ? -8.923  -14.632 2.058   1.00 15.35 ? 224 LEU A O    1 
ATOM   1774 C  CB   . LEU A 1 223 ? -10.845 -17.221 2.703   1.00 16.23 ? 224 LEU A CB   1 
ATOM   1775 C  CG   . LEU A 1 223 ? -10.686 -18.447 3.594   1.00 22.97 ? 224 LEU A CG   1 
ATOM   1776 C  CD1  . LEU A 1 223 ? -11.587 -19.672 3.095   1.00 27.26 ? 224 LEU A CD1  1 
ATOM   1777 C  CD2  . LEU A 1 223 ? -9.177  -18.826 3.629   1.00 25.11 ? 224 LEU A CD2  1 
ATOM   1778 N  N    . LYS A 1 224 ? -11.058 -13.974 2.214   1.00 12.67 ? 225 LYS A N    1 
ATOM   1779 C  CA   . LYS A 1 224 ? -10.830 -12.824 1.338   1.00 14.10 ? 225 LYS A CA   1 
ATOM   1780 C  C    . LYS A 1 224 ? -9.937  -11.768 2.003   1.00 12.53 ? 225 LYS A C    1 
ATOM   1781 O  O    . LYS A 1 224 ? -9.135  -11.169 1.352   1.00 13.37 ? 225 LYS A O    1 
ATOM   1782 C  CB   . LYS A 1 224 ? -12.144 -12.235 0.791   1.00 14.95 ? 225 LYS A CB   1 
ATOM   1783 C  CG   . LYS A 1 224 ? -12.716 -13.341 -0.331  1.00 17.44 ? 225 LYS A CG   1 
ATOM   1784 C  CD   . LYS A 1 224 ? -13.858 -12.922 -1.197  1.00 21.50 ? 225 LYS A CD   1 
ATOM   1785 C  CE   . LYS A 1 224 ? -14.593 -14.215 -1.788  1.00 26.23 ? 225 LYS A CE   1 
ATOM   1786 N  NZ   . LYS A 1 224 ? -15.927 -13.861 -2.432  1.00 31.73 ? 225 LYS A NZ   1 
ATOM   1787 N  N    . PHE A 1 225 ? -10.043 -11.552 3.326   1.00 10.77 ? 226 PHE A N    1 
ATOM   1788 C  CA   . PHE A 1 225 ? -9.080  -10.677 3.957   1.00 9.79  ? 226 PHE A CA   1 
ATOM   1789 C  C    . PHE A 1 225 ? -7.672  -11.165 3.798   1.00 10.42 ? 226 PHE A C    1 
ATOM   1790 O  O    . PHE A 1 225 ? -6.714  -10.423 3.630   1.00 11.70 ? 226 PHE A O    1 
ATOM   1791 C  CB   . PHE A 1 225 ? -9.326  -10.727 5.514   1.00 11.09 ? 226 PHE A CB   1 
ATOM   1792 C  CG   . PHE A 1 225 ? -10.497 -9.918  5.990   1.00 10.38 ? 226 PHE A CG   1 
ATOM   1793 C  CD1  . PHE A 1 225 ? -11.596 -9.512  5.231   1.00 14.11 ? 226 PHE A CD1  1 
ATOM   1794 C  CD2  . PHE A 1 225 ? -10.575 -9.697  7.399   1.00 16.72 ? 226 PHE A CD2  1 
ATOM   1795 C  CE1  . PHE A 1 225 ? -12.674 -8.814  5.819   1.00 16.22 ? 226 PHE A CE1  1 
ATOM   1796 C  CE2  . PHE A 1 225 ? -11.661 -8.982  7.957   1.00 19.99 ? 226 PHE A CE2  1 
ATOM   1797 C  CZ   . PHE A 1 225 ? -12.627 -8.454  7.111   1.00 14.84 ? 226 PHE A CZ   1 
ATOM   1798 N  N    . ARG A 1 226 ? -7.527  -12.494 3.888   1.00 11.35 ? 227 ARG A N    1 
ATOM   1799 C  CA   . ARG A 1 226 ? -6.196  -13.109 3.752   1.00 11.14 ? 227 ARG A CA   1 
ATOM   1800 C  C    . ARG A 1 226 ? -5.602  -13.132 2.360   1.00 12.80 ? 227 ARG A C    1 
ATOM   1801 O  O    . ARG A 1 226 ? -4.433  -13.563 2.227   1.00 12.73 ? 227 ARG A O    1 
ATOM   1802 C  CB   . ARG A 1 226 ? -6.201  -14.585 4.285   1.00 12.09 ? 227 ARG A CB   1 
ATOM   1803 C  CG   . ARG A 1 226 ? -6.689  -14.686 5.752   1.00 10.69 ? 227 ARG A CG   1 
ATOM   1804 C  CD   . ARG A 1 226 ? -6.667  -16.198 6.192   1.00 12.05 ? 227 ARG A CD   1 
ATOM   1805 N  NE   . ARG A 1 226 ? -7.141  -16.267 7.577   1.00 11.50 ? 227 ARG A NE   1 
ATOM   1806 C  CZ   . ARG A 1 226 ? -8.084  -17.114 8.007   1.00 13.98 ? 227 ARG A CZ   1 
ATOM   1807 N  NH1  . ARG A 1 226 ? -8.589  -18.035 7.109   1.00 17.39 ? 227 ARG A NH1  1 
ATOM   1808 N  NH2  . ARG A 1 226 ? -8.521  -17.114 9.234   1.00 13.97 ? 227 ARG A NH2  1 
ATOM   1809 N  N    . LYS A 1 227 ? -6.374  -12.634 1.394   1.00 11.95 ? 228 LYS A N    1 
ATOM   1810 C  CA   . LYS A 1 227 ? -5.771  -12.531 0.096   1.00 14.32 ? 228 LYS A CA   1 
ATOM   1811 C  C    . LYS A 1 227 ? -5.139  -11.169 -0.172  1.00 14.69 ? 228 LYS A C    1 
ATOM   1812 O  O    . LYS A 1 227 ? -4.524  -10.945 -1.207  1.00 14.15 ? 228 LYS A O    1 
ATOM   1813 C  CB   . LYS A 1 227 ? -6.899  -12.770 -0.933  1.00 14.09 ? 228 LYS A CB   1 
ATOM   1814 C  CG   . LYS A 1 227 ? -7.268  -14.196 -1.086  1.00 17.00 ? 228 LYS A CG   1 
ATOM   1815 C  CD   . LYS A 1 227 ? -8.599  -14.379 -1.878  1.00 23.23 ? 228 LYS A CD   1 
ATOM   1816 C  CE   . LYS A 1 227 ? -8.500  -13.767 -3.283  1.00 34.91 ? 228 LYS A CE   1 
ATOM   1817 N  NZ   . LYS A 1 227 ? -8.301  -14.686 -4.499  1.00 37.70 ? 228 LYS A NZ   1 
ATOM   1818 N  N    . LEU A 1 228 ? -5.366  -10.225 0.744   1.00 12.43 ? 229 LEU A N    1 
ATOM   1819 C  CA   . LEU A 1 228 ? -4.688  -8.948  0.648   1.00 11.74 ? 229 LEU A CA   1 
ATOM   1820 C  C    . LEU A 1 228 ? -3.208  -9.120  0.839   1.00 12.47 ? 229 LEU A C    1 
ATOM   1821 O  O    . LEU A 1 228 ? -2.638  -10.133 1.231   1.00 12.60 ? 229 LEU A O    1 
ATOM   1822 C  CB   . LEU A 1 228 ? -5.251  -8.041  1.749   1.00 11.46 ? 229 LEU A CB   1 
ATOM   1823 C  CG   . LEU A 1 228 ? -6.654  -7.580  1.562   1.00 13.33 ? 229 LEU A CG   1 
ATOM   1824 C  CD1  . LEU A 1 228 ? -7.172  -6.944  2.827   1.00 13.57 ? 229 LEU A CD1  1 
ATOM   1825 C  CD2  . LEU A 1 228 ? -6.706  -6.557  0.397   1.00 13.56 ? 229 LEU A CD2  1 
ATOM   1826 N  N    . ASN A 1 229 ? -2.541  -8.026  0.452   1.00 14.57 ? 230 ASN A N    1 
ATOM   1827 C  CA   . ASN A 1 229 ? -1.117  -8.011  0.451   1.00 13.99 ? 230 ASN A CA   1 
ATOM   1828 C  C    . ASN A 1 229 ? -0.507  -6.879  1.348   1.00 14.49 ? 230 ASN A C    1 
ATOM   1829 O  O    . ASN A 1 229 ? -1.013  -5.807  1.267   1.00 14.62 ? 230 ASN A O    1 
ATOM   1830 C  CB   . ASN A 1 229 ? -0.572  -7.784  -1.021  1.00 15.05 ? 230 ASN A CB   1 
ATOM   1831 C  CG   . ASN A 1 229 ? -0.534  -9.050  -1.913  1.00 18.01 ? 230 ASN A CG   1 
ATOM   1832 O  OD1  . ASN A 1 229 ? 0.128   -8.990  -2.974  1.00 19.43 ? 230 ASN A OD1  1 
ATOM   1833 N  ND2  . ASN A 1 229 ? -1.164  -10.156 -1.521  1.00 16.80 ? 230 ASN A ND2  1 
ATOM   1834 N  N    . PHE A 1 230 ? 0.559   -7.232  2.048   1.00 13.55 ? 231 PHE A N    1 
ATOM   1835 C  CA   . PHE A 1 230 ? 1.334   -6.163  2.763   1.00 13.01 ? 231 PHE A CA   1 
ATOM   1836 C  C    . PHE A 1 230 ? 2.205   -5.387  1.760   1.00 17.50 ? 231 PHE A C    1 
ATOM   1837 O  O    . PHE A 1 230 ? 2.397   -4.189  2.009   1.00 15.94 ? 231 PHE A O    1 
ATOM   1838 C  CB   . PHE A 1 230 ? 2.304   -6.694  3.718   1.00 12.83 ? 231 PHE A CB   1 
ATOM   1839 C  CG   . PHE A 1 230 ? 1.703   -7.287  5.016   1.00 13.73 ? 231 PHE A CG   1 
ATOM   1840 C  CD1  . PHE A 1 230 ? 0.899   -6.527  5.875   1.00 11.98 ? 231 PHE A CD1  1 
ATOM   1841 C  CD2  . PHE A 1 230 ? 2.072   -8.584  5.346   1.00 13.88 ? 231 PHE A CD2  1 
ATOM   1842 C  CE1  . PHE A 1 230 ? 0.457   -7.114  7.116   1.00 13.12 ? 231 PHE A CE1  1 
ATOM   1843 C  CE2  . PHE A 1 230 ? 1.627   -9.179  6.579   1.00 14.79 ? 231 PHE A CE2  1 
ATOM   1844 C  CZ   . PHE A 1 230 ? 0.847   -8.405  7.469   1.00 10.73 ? 231 PHE A CZ   1 
ATOM   1845 N  N    . ASN A 1 231 ? 2.775   -6.082  0.769   1.00 16.37 ? 232 ASN A N    1 
ATOM   1846 C  CA   . ASN A 1 231 ? 3.621   -5.445  -0.247  1.00 17.83 ? 232 ASN A CA   1 
ATOM   1847 C  C    . ASN A 1 231 ? 2.836   -4.551  -1.170  1.00 16.63 ? 232 ASN A C    1 
ATOM   1848 O  O    . ASN A 1 231 ? 1.622   -4.679  -1.336  1.00 18.15 ? 232 ASN A O    1 
ATOM   1849 C  CB   . ASN A 1 231 ? 4.231   -6.513  -1.055  1.00 18.48 ? 232 ASN A CB   1 
ATOM   1850 C  CG   . ASN A 1 231 ? 3.190   -7.379  -1.680  1.00 18.44 ? 232 ASN A CG   1 
ATOM   1851 O  OD1  . ASN A 1 231 ? 2.661   -8.267  -0.989  1.00 20.51 ? 232 ASN A OD1  1 
ATOM   1852 N  ND2  . ASN A 1 231 ? 2.860   -7.175  -3.005  1.00 19.16 ? 232 ASN A ND2  1 
ATOM   1853 N  N    . GLY A 1 232 ? 3.590   -3.621  -1.878  1.00 19.03 ? 233 GLY A N    1 
ATOM   1854 C  CA   . GLY A 1 232 ? 2.975   -2.804  -2.988  1.00 18.75 ? 233 GLY A CA   1 
ATOM   1855 C  C    . GLY A 1 232 ? 2.975   -3.590  -4.293  1.00 18.25 ? 233 GLY A C    1 
ATOM   1856 O  O    . GLY A 1 232 ? 3.638   -4.616  -4.348  1.00 19.48 ? 233 GLY A O    1 
ATOM   1857 N  N    . GLU A 1 233 ? 2.154   -3.142  -5.255  1.00 19.87 ? 234 GLU A N    1 
ATOM   1858 C  CA   . GLU A 1 233 ? 2.118   -3.702  -6.616  1.00 20.25 ? 234 GLU A CA   1 
ATOM   1859 C  C    . GLU A 1 233 ? 3.502   -3.698  -7.246  1.00 20.89 ? 234 GLU A C    1 
ATOM   1860 O  O    . GLU A 1 233 ? 4.300   -2.772  -7.061  1.00 21.39 ? 234 GLU A O    1 
ATOM   1861 C  CB   . GLU A 1 233 ? 1.146   -2.878  -7.430  1.00 18.08 ? 234 GLU A CB   1 
ATOM   1862 C  CG   . GLU A 1 233 ? 0.844   -3.448  -8.801  1.00 20.96 ? 234 GLU A CG   1 
ATOM   1863 C  CD   . GLU A 1 233 ? 0.047   -2.518  -9.630  1.00 33.25 ? 234 GLU A CD   1 
ATOM   1864 O  OE1  . GLU A 1 233 ? -0.219  -2.916  -10.790 1.00 35.42 ? 234 GLU A OE1  1 
ATOM   1865 O  OE2  . GLU A 1 233 ? -0.291  -1.377  -9.163  1.00 35.18 ? 234 GLU A OE2  1 
ATOM   1866 N  N    . GLY A 1 234 ? 3.824   -4.843  -7.848  1.00 20.33 ? 235 GLY A N    1 
ATOM   1867 C  CA   . GLY A 1 234 ? 5.145   -4.999  -8.454  1.00 23.42 ? 235 GLY A CA   1 
ATOM   1868 C  C    . GLY A 1 234 ? 6.159   -5.396  -7.460  1.00 24.49 ? 235 GLY A C    1 
ATOM   1869 O  O    . GLY A 1 234 ? 7.344   -5.440  -7.773  1.00 25.64 ? 235 GLY A O    1 
ATOM   1870 N  N    . GLU A 1 235 ? 5.706   -5.729  -6.240  1.00 23.98 ? 236 GLU A N    1 
ATOM   1871 C  CA   . GLU A 1 235 ? 6.677   -6.309  -5.264  1.00 24.73 ? 236 GLU A CA   1 
ATOM   1872 C  C    . GLU A 1 235 ? 6.268   -7.746  -4.969  1.00 25.05 ? 236 GLU A C    1 
ATOM   1873 O  O    . GLU A 1 235 ? 5.102   -8.152  -5.276  1.00 26.28 ? 236 GLU A O    1 
ATOM   1874 C  CB   . GLU A 1 235 ? 6.725   -5.535  -3.902  1.00 24.77 ? 236 GLU A CB   1 
ATOM   1875 C  CG   . GLU A 1 235 ? 7.101   -4.047  -4.065  1.00 26.17 ? 236 GLU A CG   1 
ATOM   1876 C  CD   . GLU A 1 235 ? 6.979   -3.247  -2.789  1.00 31.71 ? 236 GLU A CD   1 
ATOM   1877 O  OE1  . GLU A 1 235 ? 7.622   -2.190  -2.757  1.00 36.64 ? 236 GLU A OE1  1 
ATOM   1878 O  OE2  . GLU A 1 235 ? 6.300   -3.682  -1.778  1.00 33.77 ? 236 GLU A OE2  1 
ATOM   1879 N  N    . PRO A 1 236 ? 7.220   -8.522  -4.426  1.00 22.44 ? 237 PRO A N    1 
ATOM   1880 C  CA   . PRO A 1 236 ? 7.038   -9.957  -4.126  1.00 23.62 ? 237 PRO A CA   1 
ATOM   1881 C  C    . PRO A 1 236 ? 5.869   -10.046 -3.125  1.00 22.91 ? 237 PRO A C    1 
ATOM   1882 O  O    . PRO A 1 236 ? 5.712   -9.168  -2.252  1.00 20.82 ? 237 PRO A O    1 
ATOM   1883 C  CB   . PRO A 1 236 ? 8.306   -10.374 -3.423  1.00 25.18 ? 237 PRO A CB   1 
ATOM   1884 C  CG   . PRO A 1 236 ? 9.326   -9.219  -3.658  1.00 25.80 ? 237 PRO A CG   1 
ATOM   1885 C  CD   . PRO A 1 236 ? 8.566   -8.015  -4.080  1.00 26.10 ? 237 PRO A CD   1 
ATOM   1886 N  N    . GLU A 1 237 ? 5.103   -11.112 -3.250  1.00 21.83 ? 238 GLU A N    1 
ATOM   1887 C  CA   . GLU A 1 237 ? 3.861   -11.164 -2.558  1.00 19.91 ? 238 GLU A CA   1 
ATOM   1888 C  C    . GLU A 1 237 ? 4.092   -11.644 -1.142  1.00 19.19 ? 238 GLU A C    1 
ATOM   1889 O  O    . GLU A 1 237 ? 4.665   -12.650 -0.899  1.00 18.01 ? 238 GLU A O    1 
ATOM   1890 C  CB   . GLU A 1 237 ? 2.868   -12.060 -3.290  1.00 20.74 ? 238 GLU A CB   1 
ATOM   1891 C  CG   . GLU A 1 237 ? 1.558   -12.090 -2.581  1.00 21.42 ? 238 GLU A CG   1 
ATOM   1892 C  CD   . GLU A 1 237 ? 0.447   -12.823 -3.311  1.00 25.13 ? 238 GLU A CD   1 
ATOM   1893 O  OE1  . GLU A 1 237 ? 0.791   -13.832 -4.014  1.00 31.47 ? 238 GLU A OE1  1 
ATOM   1894 O  OE2  . GLU A 1 237 ? -0.739  -12.374 -3.213  1.00 22.94 ? 238 GLU A OE2  1 
ATOM   1895 N  N    . GLU A 1 238 ? 3.573   -10.833 -0.204  1.00 15.52 ? 239 GLU A N    1 
ATOM   1896 C  CA   . GLU A 1 238 ? 3.551   -11.159 1.230   1.00 19.06 ? 239 GLU A CA   1 
ATOM   1897 C  C    . GLU A 1 238 ? 2.083   -10.989 1.698   1.00 12.25 ? 239 GLU A C    1 
ATOM   1898 O  O    . GLU A 1 238 ? 1.536   -9.872  1.655   1.00 14.21 ? 239 GLU A O    1 
ATOM   1899 C  CB   . GLU A 1 238 ? 4.463   -10.199 2.044   1.00 17.83 ? 239 GLU A CB   1 
ATOM   1900 C  CG   . GLU A 1 238 ? 5.744   -9.681  1.361   1.00 24.18 ? 239 GLU A CG   1 
ATOM   1901 C  CD   . GLU A 1 238 ? 6.468   -8.530  2.184   1.00 29.79 ? 239 GLU A CD   1 
ATOM   1902 O  OE1  . GLU A 1 238 ? 5.821   -7.488  2.569   1.00 36.94 ? 239 GLU A OE1  1 
ATOM   1903 O  OE2  . GLU A 1 238 ? 7.708   -8.740  2.430   1.00 36.19 ? 239 GLU A OE2  1 
ATOM   1904 N  N    . LEU A 1 239 ? 1.467   -12.151 1.959   1.00 13.46 ? 240 LEU A N    1 
ATOM   1905 C  CA   . LEU A 1 239 ? 0.040   -12.087 2.248   1.00 12.01 ? 240 LEU A CA   1 
ATOM   1906 C  C    . LEU A 1 239 ? -0.162  -11.268 3.556   1.00 11.29 ? 240 LEU A C    1 
ATOM   1907 O  O    . LEU A 1 239 ? 0.568   -11.466 4.557   1.00 12.38 ? 240 LEU A O    1 
ATOM   1908 C  CB   . LEU A 1 239 ? -0.563  -13.497 2.460   1.00 12.78 ? 240 LEU A CB   1 
ATOM   1909 C  CG   . LEU A 1 239 ? -0.610  -14.298 1.175   1.00 14.04 ? 240 LEU A CG   1 
ATOM   1910 C  CD1  . LEU A 1 239 ? -1.295  -15.675 1.585   1.00 19.67 ? 240 LEU A CD1  1 
ATOM   1911 C  CD2  . LEU A 1 239 ? -1.427  -13.622 0.080   1.00 12.81 ? 240 LEU A CD2  1 
ATOM   1912 N  N    . MET A 1 240 ? -1.218  -10.485 3.519   1.00 11.04 ? 241 MET A N    1 
ATOM   1913 C  CA   . MET A 1 240 ? -1.590  -9.692  4.705   1.00 12.21 ? 241 MET A CA   1 
ATOM   1914 C  C    . MET A 1 240 ? -2.372  -10.607 5.644   1.00 11.29 ? 241 MET A C    1 
ATOM   1915 O  O    . MET A 1 240 ? -3.590  -10.721 5.545   1.00 11.83 ? 241 MET A O    1 
ATOM   1916 C  CB   . MET A 1 240 ? -2.369  -8.500  4.270   1.00 12.77 ? 241 MET A CB   1 
ATOM   1917 C  CG   . MET A 1 240 ? -2.787  -7.459  5.456   1.00 13.07 ? 241 MET A CG   1 
ATOM   1918 S  SD   . MET A 1 240 ? -3.691  -6.120  4.898   1.00 14.32 ? 241 MET A SD   1 
ATOM   1919 C  CE   . MET A 1 240 ? -2.356  -5.046  4.248   1.00 12.60 ? 241 MET A CE   1 
ATOM   1920 N  N    . VAL A 1 241 ? -1.568  -11.212 6.528   1.00 9.95  ? 242 VAL A N    1 
ATOM   1921 C  CA   . VAL A 1 241 ? -2.149  -12.050 7.583   1.00 10.82 ? 242 VAL A CA   1 
ATOM   1922 C  C    . VAL A 1 241 ? -1.347  -11.836 8.854   1.00 11.36 ? 242 VAL A C    1 
ATOM   1923 O  O    . VAL A 1 241 ? -0.147  -11.386 8.793   1.00 10.67 ? 242 VAL A O    1 
ATOM   1924 C  CB   . VAL A 1 241 ? -2.069  -13.557 7.233   1.00 10.16 ? 242 VAL A CB   1 
ATOM   1925 C  CG1  . VAL A 1 241 ? -2.992  -13.890 5.999   1.00 12.22 ? 242 VAL A CG1  1 
ATOM   1926 C  CG2  . VAL A 1 241 ? -0.630  -14.053 7.060   1.00 12.51 ? 242 VAL A CG2  1 
ATOM   1927 N  N    . ASP A 1 242 ? -1.943  -12.134 10.003  1.00 8.93  ? 243 ASP A N    1 
ATOM   1928 C  CA   . ASP A 1 242 ? -1.222  -11.984 11.233  1.00 10.01 ? 243 ASP A CA   1 
ATOM   1929 C  C    . ASP A 1 242 ? -0.788  -10.580 11.508  1.00 9.08  ? 243 ASP A C    1 
ATOM   1930 O  O    . ASP A 1 242 ? 0.332   -10.316 12.015  1.00 10.17 ? 243 ASP A O    1 
ATOM   1931 C  CB   . ASP A 1 242 ? -0.101  -13.038 11.474  1.00 8.58  ? 243 ASP A CB   1 
ATOM   1932 C  CG   . ASP A 1 242 ? -0.699  -14.420 11.637  1.00 11.98 ? 243 ASP A CG   1 
ATOM   1933 O  OD1  . ASP A 1 242 ? -1.780  -14.636 12.239  1.00 9.83  ? 243 ASP A OD1  1 
ATOM   1934 O  OD2  . ASP A 1 242 ? -0.084  -15.343 11.033  1.00 12.80 ? 243 ASP A OD2  1 
ATOM   1935 N  N    . ASN A 1 243 ? -1.672  -9.661  11.223  1.00 7.35  ? 244 ASN A N    1 
ATOM   1936 C  CA   . ASN A 1 243 ? -1.360  -8.226  11.444  1.00 8.73  ? 244 ASN A CA   1 
ATOM   1937 C  C    . ASN A 1 243 ? -1.943  -7.818  12.811  1.00 7.69  ? 244 ASN A C    1 
ATOM   1938 O  O    . ASN A 1 243 ? -2.579  -6.733  12.906  1.00 8.28  ? 244 ASN A O    1 
ATOM   1939 C  CB   . ASN A 1 243 ? -1.940  -7.330  10.303  1.00 8.73  ? 244 ASN A CB   1 
ATOM   1940 C  CG   . ASN A 1 243 ? -3.401  -7.572  10.047  1.00 9.38  ? 244 ASN A CG   1 
ATOM   1941 O  OD1  . ASN A 1 243 ? -4.062  -8.373  10.662  1.00 10.00 ? 244 ASN A OD1  1 
ATOM   1942 N  ND2  . ASN A 1 243 ? -3.946  -6.736  9.181   1.00 12.28 ? 244 ASN A ND2  1 
ATOM   1943 N  N    . TRP A 1 244 ? -1.620  -8.564  13.846  1.00 6.91  ? 245 TRP A N    1 
ATOM   1944 C  CA   . TRP A 1 244 ? -2.086  -8.281  15.192  1.00 6.56  ? 245 TRP A CA   1 
ATOM   1945 C  C    . TRP A 1 244 ? -0.900  -8.181  16.118  1.00 8.28  ? 245 TRP A C    1 
ATOM   1946 O  O    . TRP A 1 244 ? 0.116   -8.903  15.980  1.00 9.10  ? 245 TRP A O    1 
ATOM   1947 C  CB   . TRP A 1 244 ? -3.055  -9.371  15.721  1.00 7.28  ? 245 TRP A CB   1 
ATOM   1948 C  CG   . TRP A 1 244 ? -2.562  -10.752 15.526  1.00 7.14  ? 245 TRP A CG   1 
ATOM   1949 C  CD1  . TRP A 1 244 ? -2.751  -11.549 14.386  1.00 8.74  ? 245 TRP A CD1  1 
ATOM   1950 C  CD2  . TRP A 1 244 ? -2.016  -11.632 16.501  1.00 7.71  ? 245 TRP A CD2  1 
ATOM   1951 N  NE1  . TRP A 1 244 ? -2.204  -12.815 14.560  1.00 8.06  ? 245 TRP A NE1  1 
ATOM   1952 C  CE2  . TRP A 1 244 ? -1.778  -12.886 15.880  1.00 8.78  ? 245 TRP A CE2  1 
ATOM   1953 C  CE3  . TRP A 1 244 ? -1.735  -11.508 17.893  1.00 9.24  ? 245 TRP A CE3  1 
ATOM   1954 C  CZ2  . TRP A 1 244 ? -1.188  -13.961 16.611  1.00 7.70  ? 245 TRP A CZ2  1 
ATOM   1955 C  CZ3  . TRP A 1 244 ? -1.126  -12.583 18.566  1.00 10.24 ? 245 TRP A CZ3  1 
ATOM   1956 C  CH2  . TRP A 1 244 ? -0.926  -13.802 17.912  1.00 9.04  ? 245 TRP A CH2  1 
ATOM   1957 N  N    . ARG A 1 245 ? -0.996  -7.274  17.074  1.00 6.94  ? 246 ARG A N    1 
ATOM   1958 C  CA   . ARG A 1 245 ? -0.021  -7.162  18.199  1.00 8.54  ? 246 ARG A CA   1 
ATOM   1959 C  C    . ARG A 1 245 ? -0.496  -8.068  19.287  1.00 8.47  ? 246 ARG A C    1 
ATOM   1960 O  O    . ARG A 1 245 ? -1.718  -8.089  19.573  1.00 8.85  ? 246 ARG A O    1 
ATOM   1961 C  CB   . ARG A 1 245 ? 0.003   -5.712  18.735  1.00 8.32  ? 246 ARG A CB   1 
ATOM   1962 C  CG   . ARG A 1 245 ? 1.126   -5.494  19.713  1.00 8.81  ? 246 ARG A CG   1 
ATOM   1963 C  CD   . ARG A 1 245 ? 1.028   -4.120  20.318  1.00 9.92  ? 246 ARG A CD   1 
ATOM   1964 N  NE   . ARG A 1 245 ? 2.305   -3.855  21.032  1.00 10.25 ? 246 ARG A NE   1 
ATOM   1965 C  CZ   . ARG A 1 245 ? 2.468   -2.858  21.844  1.00 9.34  ? 246 ARG A CZ   1 
ATOM   1966 N  NH1  . ARG A 1 245 ? 1.489   -2.013  22.237  1.00 9.61  ? 246 ARG A NH1  1 
ATOM   1967 N  NH2  . ARG A 1 245 ? 3.745   -2.630  22.316  1.00 10.95 ? 246 ARG A NH2  1 
ATOM   1968 N  N    . PRO A 1 246 ? 0.351   -8.892  19.951  1.00 9.06  ? 247 PRO A N    1 
ATOM   1969 C  CA   . PRO A 1 246 ? -0.075  -9.739  21.010  1.00 8.41  ? 247 PRO A CA   1 
ATOM   1970 C  C    . PRO A 1 246 ? -0.368  -8.910  22.264  1.00 8.53  ? 247 PRO A C    1 
ATOM   1971 O  O    . PRO A 1 246 ? -0.031  -7.731  22.409  1.00 8.42  ? 247 PRO A O    1 
ATOM   1972 C  CB   . PRO A 1 246 ? 1.146   -10.598 21.333  1.00 12.16 ? 247 PRO A CB   1 
ATOM   1973 C  CG   . PRO A 1 246 ? 2.141   -10.264 20.307  1.00 15.57 ? 247 PRO A CG   1 
ATOM   1974 C  CD   . PRO A 1 246 ? 1.815   -9.018  19.620  1.00 10.28 ? 247 PRO A CD   1 
ATOM   1975 N  N    . ALA A 1 247 ? -1.042  -9.580  23.200  1.00 9.21  ? 248 ALA A N    1 
ATOM   1976 C  CA   . ALA A 1 247 ? -1.387  -8.942  24.471  1.00 8.62  ? 248 ALA A CA   1 
ATOM   1977 C  C    . ALA A 1 247 ? -0.175  -8.457  25.231  1.00 9.81  ? 248 ALA A C    1 
ATOM   1978 O  O    . ALA A 1 247 ? 0.890   -9.112  25.214  1.00 11.49 ? 248 ALA A O    1 
ATOM   1979 C  CB   . ALA A 1 247 ? -2.145  -9.933  25.390  1.00 11.09 ? 248 ALA A CB   1 
ATOM   1980 N  N    . GLN A 1 248 ? -0.325  -7.293  25.855  1.00 8.58  ? 249 GLN A N    1 
ATOM   1981 C  CA   . GLN A 1 248 ? 0.775   -6.535  26.518  1.00 9.92  ? 249 GLN A CA   1 
ATOM   1982 C  C    . GLN A 1 248 ? 0.468   -6.547  27.958  1.00 10.42 ? 249 GLN A C    1 
ATOM   1983 O  O    . GLN A 1 248 ? -0.665  -6.751  28.427  1.00 9.47  ? 249 GLN A O    1 
ATOM   1984 C  CB   . GLN A 1 248 ? 0.797   -5.128  26.025  1.00 9.47  ? 249 GLN A CB   1 
ATOM   1985 C  CG   . GLN A 1 248 ? 1.098   -4.996  24.543  1.00 10.86 ? 249 GLN A CG   1 
ATOM   1986 C  CD   . GLN A 1 248 ? 2.437   -5.668  24.146  1.00 12.95 ? 249 GLN A CD   1 
ATOM   1987 O  OE1  . GLN A 1 248 ? 3.486   -5.349  24.756  1.00 15.56 ? 249 GLN A OE1  1 
ATOM   1988 N  NE2  . GLN A 1 248 ? 2.433   -6.603  23.236  1.00 10.72 ? 249 GLN A NE2  1 
ATOM   1989 N  N    . PRO A 1 249 ? 1.482   -6.282  28.798  1.00 12.39 ? 250 PRO A N    1 
ATOM   1990 C  CA   . PRO A 1 249 ? 1.212   -6.365  30.212  1.00 12.30 ? 250 PRO A CA   1 
ATOM   1991 C  C    . PRO A 1 249 ? 0.137   -5.340  30.716  1.00 10.52 ? 250 PRO A C    1 
ATOM   1992 O  O    . PRO A 1 249 ? 0.189   -4.172  30.322  1.00 12.10 ? 250 PRO A O    1 
ATOM   1993 C  CB   . PRO A 1 249 ? 2.633   -6.041  30.851  1.00 15.53 ? 250 PRO A CB   1 
ATOM   1994 C  CG   . PRO A 1 249 ? 3.576   -6.239  29.825  1.00 16.24 ? 250 PRO A CG   1 
ATOM   1995 C  CD   . PRO A 1 249 ? 2.890   -5.959  28.457  1.00 13.15 ? 250 PRO A CD   1 
ATOM   1996 N  N    . LEU A 1 250 ? -0.725  -5.794  31.621  1.00 12.40 ? 251 LEU A N    1 
ATOM   1997 C  CA   . LEU A 1 250 ? -1.777  -4.889  32.092  1.00 11.54 ? 251 LEU A CA   1 
ATOM   1998 C  C    . LEU A 1 250 ? -1.209  -3.836  33.013  1.00 13.04 ? 251 LEU A C    1 
ATOM   1999 O  O    . LEU A 1 250 ? -1.706  -2.711  33.049  1.00 12.38 ? 251 LEU A O    1 
ATOM   2000 C  CB   . LEU A 1 250 ? -2.775  -5.724  32.854  1.00 15.66 ? 251 LEU A CB   1 
ATOM   2001 C  CG   . LEU A 1 250 ? -4.042  -5.021  33.257  1.00 13.74 ? 251 LEU A CG   1 
ATOM   2002 C  CD1  . LEU A 1 250 ? -4.879  -4.498  32.045  1.00 12.91 ? 251 LEU A CD1  1 
ATOM   2003 C  CD2  . LEU A 1 250 ? -4.929  -6.054  34.065  1.00 18.46 ? 251 LEU A CD2  1 
ATOM   2004 N  N    . LYS A 1 251 ? -0.130  -4.169  33.725  1.00 13.30 ? 252 LYS A N    1 
ATOM   2005 C  CA   . LYS A 1 251 ? 0.573   -3.118  34.626  1.00 12.50 ? 252 LYS A CA   1 
ATOM   2006 C  C    . LYS A 1 251 ? -0.462  -2.574  35.619  1.00 12.78 ? 252 LYS A C    1 
ATOM   2007 O  O    . LYS A 1 251 ? -1.267  -3.367  36.124  1.00 15.53 ? 252 LYS A O    1 
ATOM   2008 C  CB   . LYS A 1 251 ? 1.318   -2.024  33.825  1.00 15.56 ? 252 LYS A CB   1 
ATOM   2009 C  CG   . LYS A 1 251 ? 2.432   -2.709  33.057  1.00 17.33 ? 252 LYS A CG   1 
ATOM   2010 C  CD   . LYS A 1 251 ? 3.284   -1.761  32.315  1.00 21.55 ? 252 LYS A CD   1 
ATOM   2011 C  CE   . LYS A 1 251 ? 4.511   -2.461  31.850  1.00 22.94 ? 252 LYS A CE   1 
ATOM   2012 N  NZ   . LYS A 1 251 ? 5.500   -1.583  31.180  1.00 27.29 ? 252 LYS A NZ   1 
ATOM   2013 N  N    . ASN A 1 252 ? -0.446  -1.298  35.768  1.00 14.12 ? 253 ASN A N    1 
ATOM   2014 C  CA   . ASN A 1 252 ? -1.306  -0.809  36.800  1.00 19.33 ? 253 ASN A CA   1 
ATOM   2015 C  C    . ASN A 1 252 ? -2.673  -0.361  36.253  1.00 18.17 ? 253 ASN A C    1 
ATOM   2016 O  O    . ASN A 1 252 ? -2.850  0.942   36.208  1.00 21.48 ? 253 ASN A O    1 
ATOM   2017 C  CB   . ASN A 1 252 ? -0.581  0.367   37.553  1.00 21.11 ? 253 ASN A CB   1 
ATOM   2018 C  CG   . ASN A 1 252 ? -1.340  0.807   38.804  1.00 28.19 ? 253 ASN A CG   1 
ATOM   2019 O  OD1  . ASN A 1 252 ? -1.919  -0.045  39.546  1.00 38.35 ? 253 ASN A OD1  1 
ATOM   2020 N  ND2  . ASN A 1 252 ? -1.371  2.116   39.055  1.00 36.52 ? 253 ASN A ND2  1 
ATOM   2021 N  N    . ARG A 1 253 ? -3.455  -1.362  35.688  1.00 15.13 ? 254 ARG A N    1 
ATOM   2022 C  CA   . ARG A 1 253 ? -4.742  -1.009  35.190  1.00 11.55 ? 254 ARG A CA   1 
ATOM   2023 C  C    . ARG A 1 253 ? -5.817  -1.945  35.629  1.00 13.16 ? 254 ARG A C    1 
ATOM   2024 O  O    . ARG A 1 253 ? -5.545  -3.095  35.862  1.00 15.42 ? 254 ARG A O    1 
ATOM   2025 C  CB   . ARG A 1 253 ? -4.743  -0.922  33.604  1.00 12.06 ? 254 ARG A CB   1 
ATOM   2026 C  CG   . ARG A 1 253 ? -3.837  0.183   33.133  1.00 8.67  ? 254 ARG A CG   1 
ATOM   2027 C  CD   . ARG A 1 253 ? -3.758  0.152   31.606  1.00 9.78  ? 254 ARG A CD   1 
ATOM   2028 N  NE   . ARG A 1 253 ? -2.872  -0.962  31.171  1.00 10.17 ? 254 ARG A NE   1 
ATOM   2029 C  CZ   . ARG A 1 253 ? -2.625  -1.239  29.887  1.00 8.63  ? 254 ARG A CZ   1 
ATOM   2030 N  NH1  . ARG A 1 253 ? -3.281  -0.541  28.925  1.00 8.73  ? 254 ARG A NH1  1 
ATOM   2031 N  NH2  . ARG A 1 253 ? -1.831  -2.243  29.536  1.00 9.38  ? 254 ARG A NH2  1 
ATOM   2032 N  N    . GLN A 1 254 ? -7.071  -1.483  35.634  1.00 12.93 ? 255 GLN A N    1 
ATOM   2033 C  CA   . GLN A 1 254 ? -8.247  -2.243  35.928  1.00 13.94 ? 255 GLN A CA   1 
ATOM   2034 C  C    . GLN A 1 254 ? -9.099  -2.214  34.671  1.00 13.33 ? 255 GLN A C    1 
ATOM   2035 O  O    . GLN A 1 254 ? -9.300  -1.144  34.040  1.00 15.45 ? 255 GLN A O    1 
ATOM   2036 C  CB   . GLN A 1 254 ? -9.085  -1.574  37.070  1.00 15.42 ? 255 GLN A CB   1 
ATOM   2037 C  CG   . GLN A 1 254 ? -10.214 -2.447  37.693  1.00 25.20 ? 255 GLN A CG   1 
ATOM   2038 C  CD   . GLN A 1 254 ? -9.714  -3.726  38.350  1.00 27.92 ? 255 GLN A CD   1 
ATOM   2039 O  OE1  . GLN A 1 254 ? -8.674  -3.737  39.012  0.01 26.99 ? 255 GLN A OE1  1 
ATOM   2040 N  NE2  . GLN A 1 254 ? -10.461 -4.810  38.174  0.01 26.92 ? 255 GLN A NE2  1 
ATOM   2041 N  N    . ILE A 1 255 ? -9.590  -3.369  34.282  1.00 11.35 ? 256 ILE A N    1 
ATOM   2042 C  CA   . ILE A 1 255 ? -10.622 -3.521  33.262  1.00 11.91 ? 256 ILE A CA   1 
ATOM   2043 C  C    . ILE A 1 255 ? -11.992 -3.608  33.945  1.00 10.88 ? 256 ILE A C    1 
ATOM   2044 O  O    . ILE A 1 255 ? -12.172 -4.262  34.956  1.00 11.68 ? 256 ILE A O    1 
ATOM   2045 C  CB   . ILE A 1 255 ? -10.336 -4.742  32.462  1.00 11.13 ? 256 ILE A CB   1 
ATOM   2046 C  CG1  . ILE A 1 255 ? -8.890  -4.695  31.841  1.00 11.43 ? 256 ILE A CG1  1 
ATOM   2047 C  CG2  . ILE A 1 255 ? -11.462 -4.986  31.375  1.00 11.96 ? 256 ILE A CG2  1 
ATOM   2048 C  CD1  . ILE A 1 255 ? -8.680  -5.921  31.013  1.00 16.67 ? 256 ILE A CD1  1 
ATOM   2049 N  N    . LYS A 1 256 ? -12.879 -2.723  33.461  1.00 9.47  ? 257 LYS A N    1 
ATOM   2050 C  CA   . LYS A 1 256 ? -14.221 -2.588  34.019  1.00 11.34 ? 257 LYS A CA   1 
ATOM   2051 C  C    . LYS A 1 256 ? -15.225 -3.203  33.058  1.00 10.29 ? 257 LYS A C    1 
ATOM   2052 O  O    . LYS A 1 256 ? -15.055 -3.095  31.812  1.00 11.55 ? 257 LYS A O    1 
ATOM   2053 C  CB   . LYS A 1 256 ? -14.566 -1.111  34.227  1.00 11.32 ? 257 LYS A CB   1 
ATOM   2054 C  CG   . LYS A 1 256 ? -13.674 -0.406  35.367  1.00 18.32 ? 257 LYS A CG   1 
ATOM   2055 C  CD   . LYS A 1 256 ? -14.167 -0.758  36.766  0.01 14.97 ? 257 LYS A CD   1 
ATOM   2056 C  CE   . LYS A 1 256 ? -13.700 0.257   37.800  0.01 13.86 ? 257 LYS A CE   1 
ATOM   2057 N  NZ   . LYS A 1 256 ? -14.470 1.533   37.724  0.01 13.92 ? 257 LYS A NZ   1 
ATOM   2058 N  N    . ALA A 1 257 ? -16.225 -3.849  33.558  1.00 11.12 ? 258 ALA A N    1 
ATOM   2059 C  CA   . ALA A 1 257 ? -17.294 -4.455  32.756  1.00 10.96 ? 258 ALA A CA   1 
ATOM   2060 C  C    . ALA A 1 257 ? -18.587 -3.654  32.907  1.00 11.50 ? 258 ALA A C    1 
ATOM   2061 O  O    . ALA A 1 257 ? -18.962 -3.193  34.054  1.00 11.92 ? 258 ALA A O    1 
ATOM   2062 C  CB   . ALA A 1 257 ? -17.485 -5.995  33.166  1.00 12.94 ? 258 ALA A CB   1 
ATOM   2063 N  N    . SER A 1 258 ? -19.344 -3.548  31.843  1.00 11.65 ? 259 SER A N    1 
ATOM   2064 C  CA   . SER A 1 258 ? -20.605 -2.854  31.895  1.00 13.45 ? 259 SER A CA   1 
ATOM   2065 C  C    . SER A 1 258 ? -21.736 -3.799  32.298  1.00 13.74 ? 259 SER A C    1 
ATOM   2066 O  O    . SER A 1 258 ? -22.879 -3.271  32.448  1.00 17.45 ? 259 SER A O    1 
ATOM   2067 C  CB   . SER A 1 258 ? -20.892 -2.276  30.514  1.00 12.50 ? 259 SER A CB   1 
ATOM   2068 O  OG   . SER A 1 258 ? -21.379 -3.268  29.606  1.00 12.79 ? 259 SER A OG   1 
ATOM   2069 N  N    . PHE A 1 259 ? -21.469 -5.053  32.527  1.00 14.05 ? 260 PHE A N    1 
ATOM   2070 C  CA   . PHE A 1 259 ? -22.511 -6.038  32.686  1.00 15.86 ? 260 PHE A CA   1 
ATOM   2071 C  C    . PHE A 1 259 ? -22.070 -7.001  33.767  1.00 19.86 ? 260 PHE A C    1 
ATOM   2072 O  O    . PHE A 1 259 ? -20.876 -7.051  34.155  1.00 20.09 ? 260 PHE A O    1 
ATOM   2073 C  CB   . PHE A 1 259 ? -22.728 -6.780  31.383  1.00 16.67 ? 260 PHE A CB   1 
ATOM   2074 C  CG   . PHE A 1 259 ? -21.438 -7.527  30.916  1.00 16.29 ? 260 PHE A CG   1 
ATOM   2075 C  CD1  . PHE A 1 259 ? -20.406 -6.861  30.237  1.00 13.54 ? 260 PHE A CD1  1 
ATOM   2076 C  CD2  . PHE A 1 259 ? -21.212 -8.852  31.336  1.00 18.00 ? 260 PHE A CD2  1 
ATOM   2077 C  CE1  . PHE A 1 259 ? -19.240 -7.523  29.888  1.00 15.72 ? 260 PHE A CE1  1 
ATOM   2078 C  CE2  . PHE A 1 259 ? -19.993 -9.528  30.989  1.00 17.74 ? 260 PHE A CE2  1 
ATOM   2079 C  CZ   . PHE A 1 259 ? -19.021 -8.830  30.263  1.00 18.56 ? 260 PHE A CZ   1 
ATOM   2080 N  N    . LYS A 1 260 ? -23.105 -7.748  34.234  1.00 25.99 ? 261 LYS A N    1 
ATOM   2081 C  CA   . LYS A 1 260 ? -23.109 -8.912  35.148  1.00 32.23 ? 261 LYS A CA   1 
ATOM   2082 C  C    . LYS A 1 260 ? -22.516 -8.737  36.541  1.00 34.82 ? 261 LYS A C    1 
ATOM   2083 O  O    . LYS A 1 260 ? -22.754 -9.573  37.425  1.00 36.62 ? 261 LYS A O    1 
ATOM   2084 C  CB   . LYS A 1 260 ? -22.676 -10.247 34.472  1.00 32.91 ? 261 LYS A CB   1 
ATOM   2085 C  CG   . LYS A 1 260 ? -23.634 -10.698 33.339  1.00 32.72 ? 261 LYS A CG   1 
ATOM   2086 C  CD   . LYS A 1 260 ? -23.167 -12.026 32.595  1.00 32.33 ? 261 LYS A CD   1 
ATOM   2087 C  CE   . LYS A 1 260 ? -21.580 -12.258 32.727  1.00 34.46 ? 261 LYS A CE   1 
ATOM   2088 N  NZ   . LYS A 1 260 ? -20.947 -13.352 31.939  1.00 35.27 ? 261 LYS A NZ   1 
ATOM   2089 O  OXT  . LYS A 1 260 ? -21.860 -7.728  36.859  1.00 38.16 ? 261 LYS A OXT  1 
HETATM 2090 ZN ZN   . ZN  B 2 .   ? -6.616  -1.717  15.214  1.00 7.21  ? 262 ZN  A ZN   1 
HETATM 2091 S  S    . DMS C 3 .   ? 1.380   -11.709 14.878  1.00 19.38 ? 263 DMS A S    1 
HETATM 2092 O  O    . DMS C 3 .   ? 2.388   -10.409 14.390  1.00 23.21 ? 263 DMS A O    1 
HETATM 2093 C  C1   . DMS C 3 .   ? 1.836   -11.642 16.592  1.00 18.28 ? 263 DMS A C1   1 
HETATM 2094 C  C2   . DMS C 3 .   ? 2.121   -13.203 14.381  1.00 20.22 ? 263 DMS A C2   1 
HETATM 2095 S  S    . DMS D 3 .   ? -5.495  7.168   11.029  1.00 30.60 ? 264 DMS A S    1 
HETATM 2096 O  O    . DMS D 3 .   ? -6.853  6.423   10.318  1.00 29.73 ? 264 DMS A O    1 
HETATM 2097 C  C1   . DMS D 3 .   ? -5.660  8.878   10.380  1.00 31.77 ? 264 DMS A C1   1 
HETATM 2098 C  C2   . DMS D 3 .   ? -4.207  6.533   9.928   1.00 31.94 ? 264 DMS A C2   1 
HETATM 2099 N  N1   . E38 E 4 .   ? -0.271  4.625   11.030  1.00 34.70 ? 265 E38 A N1   1 
HETATM 2100 C  C2   . E38 E 4 .   ? -1.194  3.784   11.527  1.00 32.94 ? 265 E38 A C2   1 
HETATM 2101 N  N3   . E38 E 4 .   ? -1.817  4.303   12.613  1.00 34.67 ? 265 E38 A N3   1 
HETATM 2102 C  C4   . E38 E 4 .   ? -1.288  5.504   12.780  1.00 33.56 ? 265 E38 A C4   1 
HETATM 2103 C  C5   . E38 E 4 .   ? -0.313  5.700   11.820  1.00 32.95 ? 265 E38 A C5   1 
HETATM 2104 C  C6   . E38 E 4 .   ? 0.466   6.874   11.748  1.00 33.75 ? 265 E38 A C6   1 
HETATM 2105 C  C7   . E38 E 4 .   ? 0.204   7.852   12.721  1.00 33.53 ? 265 E38 A C7   1 
HETATM 2106 C  C8   . E38 E 4 .   ? -0.823  7.576   13.676  1.00 32.27 ? 265 E38 A C8   1 
HETATM 2107 C  C9   . E38 E 4 .   ? -1.608  6.448   13.731  1.00 31.48 ? 265 E38 A C9   1 
HETATM 2108 S  S10  . E38 E 4 .   ? -1.617  2.179   10.866  1.00 30.53 ? 265 E38 A S10  1 
HETATM 2109 C  C11  . E38 E 4 .   ? -3.000  1.760   12.034  1.00 17.43 ? 265 E38 A C11  1 
HETATM 2110 C  C12  . E38 E 4 .   ? -4.165  2.750   12.114  1.00 18.61 ? 265 E38 A C12  1 
HETATM 2111 O  O13  . E38 E 4 .   ? -4.632  3.346   11.077  1.00 24.13 ? 265 E38 A O13  1 
HETATM 2112 BR BR14 . E38 E 4 .   ? -1.297  8.770   15.077  1.00 33.19 ? 265 E38 A BR14 1 
HETATM 2113 C  C15  . E38 E 4 .   ? -4.767  3.055   13.523  1.00 14.39 ? 265 E38 A C15  1 
HETATM 2114 C  C16  . E38 E 4 .   ? -5.000  1.987   14.421  1.00 10.42 ? 265 E38 A C16  1 
HETATM 2115 C  C17  . E38 E 4 .   ? -5.545  2.198   15.629  1.00 9.49  ? 265 E38 A C17  1 
HETATM 2116 C  C18  . E38 E 4 .   ? -5.972  3.466   16.013  1.00 11.58 ? 265 E38 A C18  1 
HETATM 2117 C  C19  . E38 E 4 .   ? -5.752  4.541   15.132  1.00 12.01 ? 265 E38 A C19  1 
HETATM 2118 C  C20  . E38 E 4 .   ? -5.190  4.326   13.926  1.00 14.36 ? 265 E38 A C20  1 
HETATM 2119 S  S21  . E38 E 4 .   ? -5.894  0.773   16.687  1.00 8.62  ? 265 E38 A S21  1 
HETATM 2120 O  O22  . E38 E 4 .   ? -7.393  0.687   16.694  1.00 9.07  ? 265 E38 A O22  1 
HETATM 2121 CL CL23 . E38 E 4 .   ? -6.703  3.798   17.464  1.00 13.17 ? 265 E38 A CL23 1 
HETATM 2122 O  O24  . E38 E 4 .   ? -5.265  1.042   17.969  1.00 7.89  ? 265 E38 A O24  1 
HETATM 2123 N  N25  . E38 E 4 .   ? -5.285  -0.560  16.000  1.00 6.38  ? 265 E38 A N25  1 
HETATM 2124 O  O    . HOH F 5 .   ? 0.082   1.020   34.382  1.00 25.42 ? 126 HOH A O    1 
HETATM 2125 O  O    . HOH F 5 .   ? -1.177  -4.001  15.685  1.00 8.40  ? 266 HOH A O    1 
HETATM 2126 O  O    . HOH F 5 .   ? 10.119  -5.896  -12.214 1.00 16.11 ? 267 HOH A O    1 
HETATM 2127 O  O    . HOH F 5 .   ? -4.506  -13.495 17.991  1.00 8.97  ? 268 HOH A O    1 
HETATM 2128 O  O    . HOH F 5 .   ? 4.477   -6.522  7.907   1.00 21.04 ? 269 HOH A O    1 
HETATM 2129 O  O    . HOH F 5 .   ? -16.995 -8.377  20.326  1.00 8.24  ? 270 HOH A O    1 
HETATM 2130 O  O    . HOH F 5 .   ? -6.163  -19.682 23.766  1.00 21.07 ? 271 HOH A O    1 
HETATM 2131 O  O    . HOH F 5 .   ? -18.191 3.890   -3.686  1.00 27.73 ? 272 HOH A O    1 
HETATM 2132 O  O    . HOH F 5 .   ? -24.868 -7.756  8.991   1.00 16.64 ? 273 HOH A O    1 
HETATM 2133 O  O    . HOH F 5 .   ? -21.563 -7.144  23.480  1.00 12.51 ? 274 HOH A O    1 
HETATM 2134 O  O    . HOH F 5 .   ? -0.394  10.832  23.356  1.00 16.82 ? 275 HOH A O    1 
HETATM 2135 O  O    . HOH F 5 .   ? -21.766 5.658   4.777   1.00 16.82 ? 276 HOH A O    1 
HETATM 2136 O  O    . HOH F 5 .   ? -34.006 -9.435  16.510  1.00 18.53 ? 277 HOH A O    1 
HETATM 2137 O  O    . HOH F 5 .   ? -8.415  -19.806 26.574  1.00 19.86 ? 278 HOH A O    1 
HETATM 2138 O  O    . HOH F 5 .   ? -6.699  -20.131 19.496  1.00 13.51 ? 279 HOH A O    1 
HETATM 2139 O  O    . HOH F 5 .   ? -3.378  -13.249 25.060  1.00 13.08 ? 280 HOH A O    1 
HETATM 2140 O  O    . HOH F 5 .   ? -1.267  -13.118 26.865  1.00 21.48 ? 281 HOH A O    1 
HETATM 2141 O  O    . HOH F 5 .   ? -22.782 -5.779  2.735   1.00 23.50 ? 282 HOH A O    1 
HETATM 2142 O  O    . HOH F 5 .   ? 1.320   8.868   24.253  1.00 18.10 ? 283 HOH A O    1 
HETATM 2143 O  O    . HOH F 5 .   ? -17.987 -20.379 7.928   1.00 12.65 ? 284 HOH A O    1 
HETATM 2144 O  O    . HOH F 5 .   ? -1.115  -17.593 17.846  1.00 27.95 ? 285 HOH A O    1 
HETATM 2145 O  O    . HOH F 5 .   ? -2.304  4.345   7.962   1.00 32.19 ? 286 HOH A O    1 
HETATM 2146 O  O    . HOH F 5 .   ? -13.739 -21.160 15.076  1.00 16.45 ? 287 HOH A O    1 
HETATM 2147 O  O    . HOH F 5 .   ? -4.600  -11.881 31.909  1.00 19.97 ? 288 HOH A O    1 
HETATM 2148 O  O    . HOH F 5 .   ? -6.870  -14.869 31.441  1.00 21.34 ? 289 HOH A O    1 
HETATM 2149 O  O    . HOH F 5 .   ? 4.956   -4.942  20.927  1.00 12.63 ? 290 HOH A O    1 
HETATM 2150 O  O    . HOH F 5 .   ? 0.225   -1.113  -4.713  1.00 20.47 ? 291 HOH A O    1 
HETATM 2151 O  O    . HOH F 5 .   ? -2.426  -8.716  28.993  1.00 10.39 ? 292 HOH A O    1 
HETATM 2152 O  O    . HOH F 5 .   ? 4.556   -2.538  28.814  1.00 25.33 ? 293 HOH A O    1 
HETATM 2153 O  O    . HOH F 5 .   ? -24.037 8.557   20.081  1.00 19.37 ? 294 HOH A O    1 
HETATM 2154 O  O    . HOH F 5 .   ? -0.385  -8.486  32.359  1.00 22.68 ? 295 HOH A O    1 
HETATM 2155 O  O    . HOH F 5 .   ? -16.780 -13.904 26.264  1.00 20.46 ? 296 HOH A O    1 
HETATM 2156 O  O    . HOH F 5 .   ? 3.748   5.080   29.584  1.00 18.89 ? 297 HOH A O    1 
HETATM 2157 O  O    . HOH F 5 .   ? 5.031   -7.427  22.133  1.00 23.47 ? 298 HOH A O    1 
HETATM 2158 O  O    . HOH F 5 .   ? 1.367   -11.746 25.088  1.00 22.96 ? 299 HOH A O    1 
HETATM 2159 O  O    . HOH F 5 .   ? -14.928 -21.118 17.612  1.00 20.72 ? 300 HOH A O    1 
HETATM 2160 O  O    . HOH F 5 .   ? -10.408 -18.247 16.992  1.00 12.19 ? 301 HOH A O    1 
HETATM 2161 O  O    . HOH F 5 .   ? -6.108  -4.559  -6.365  1.00 26.21 ? 302 HOH A O    1 
HETATM 2162 O  O    . HOH F 5 .   ? -24.035 -6.831  0.334   1.00 32.72 ? 303 HOH A O    1 
HETATM 2163 O  O    . HOH F 5 .   ? -23.067 -11.784 13.910  1.00 21.28 ? 304 HOH A O    1 
HETATM 2164 O  O    . HOH F 5 .   ? -3.745  -15.851 24.230  1.00 12.71 ? 305 HOH A O    1 
HETATM 2165 O  O    . HOH F 5 .   ? 4.256   -3.380  26.447  1.00 18.86 ? 306 HOH A O    1 
HETATM 2166 O  O    . HOH F 5 .   ? -15.391 -21.765 13.051  1.00 16.97 ? 307 HOH A O    1 
HETATM 2167 O  O    . HOH F 5 .   ? -3.493  -11.127 20.811  1.00 9.95  ? 308 HOH A O    1 
HETATM 2168 O  O    . HOH F 5 .   ? -16.042 15.837  23.641  1.00 17.08 ? 309 HOH A O    1 
HETATM 2169 O  O    . HOH F 5 .   ? -8.159  -19.322 21.561  1.00 13.96 ? 310 HOH A O    1 
HETATM 2170 O  O    . HOH F 5 .   ? -26.774 -3.948  25.116  1.00 21.10 ? 311 HOH A O    1 
HETATM 2171 O  O    . HOH F 5 .   ? -23.377 -13.261 11.227  1.00 21.05 ? 312 HOH A O    1 
HETATM 2172 O  O    . HOH F 5 .   ? 7.640   6.156   21.700  1.00 18.05 ? 313 HOH A O    1 
HETATM 2173 O  O    . HOH F 5 .   ? -0.158  -14.297 22.111  1.00 21.60 ? 314 HOH A O    1 
HETATM 2174 O  O    . HOH F 5 .   ? -7.017  5.833   6.292   1.00 25.60 ? 315 HOH A O    1 
HETATM 2175 O  O    . HOH F 5 .   ? -19.866 -16.622 2.899   1.00 23.04 ? 316 HOH A O    1 
HETATM 2176 O  O    . HOH F 5 .   ? -16.106 -12.297 24.248  1.00 14.49 ? 317 HOH A O    1 
HETATM 2177 O  O    . HOH F 5 .   ? -7.389  -8.727  -2.375  1.00 23.25 ? 318 HOH A O    1 
HETATM 2178 O  O    . HOH F 5 .   ? -8.620  -3.811  7.789   1.00 9.46  ? 319 HOH A O    1 
HETATM 2179 O  O    . HOH F 5 .   ? -20.001 -15.521 22.296  1.00 25.95 ? 320 HOH A O    1 
HETATM 2180 O  O    . HOH F 5 .   ? -10.555 8.642   25.440  1.00 9.50  ? 321 HOH A O    1 
HETATM 2181 O  O    . HOH F 5 .   ? -10.400 -18.907 34.306  1.00 25.10 ? 322 HOH A O    1 
HETATM 2182 O  O    . HOH F 5 .   ? -2.012  -12.350 22.772  1.00 10.33 ? 323 HOH A O    1 
HETATM 2183 O  O    . HOH F 5 .   ? -5.537  -12.544 -5.107  1.00 29.59 ? 324 HOH A O    1 
HETATM 2184 O  O    . HOH F 5 .   ? -28.953 -5.700  24.509  1.00 28.91 ? 325 HOH A O    1 
HETATM 2185 O  O    . HOH F 5 .   ? 1.315   -1.577  29.321  1.00 13.60 ? 326 HOH A O    1 
HETATM 2186 O  O    . HOH F 5 .   ? -7.205  -8.689  32.461  1.00 17.55 ? 327 HOH A O    1 
HETATM 2187 O  O    . HOH F 5 .   ? -13.745 10.324  27.769  1.00 18.24 ? 328 HOH A O    1 
HETATM 2188 O  O    . HOH F 5 .   ? -7.250  -16.795 1.447   1.00 22.54 ? 329 HOH A O    1 
HETATM 2189 O  O    . HOH F 5 .   ? -17.870 10.573  11.229  1.00 16.22 ? 330 HOH A O    1 
HETATM 2190 O  O    . HOH F 5 .   ? -9.348  -10.004 -1.161  1.00 22.72 ? 331 HOH A O    1 
HETATM 2191 O  O    . HOH F 5 .   ? 8.615   -3.795  20.996  1.00 14.36 ? 332 HOH A O    1 
HETATM 2192 O  O    . HOH F 5 .   ? 1.763   12.583  22.466  1.00 25.85 ? 333 HOH A O    1 
HETATM 2193 O  O    . HOH F 5 .   ? -9.488  -7.946  33.947  1.00 19.59 ? 334 HOH A O    1 
HETATM 2194 O  O    . HOH F 5 .   ? -25.208 11.092  19.618  1.00 26.48 ? 335 HOH A O    1 
HETATM 2195 O  O    . HOH F 5 .   ? -7.940  -15.429 11.338  1.00 9.49  ? 336 HOH A O    1 
HETATM 2196 O  O    . HOH F 5 .   ? 1.976   -15.570 9.209   1.00 20.71 ? 337 HOH A O    1 
HETATM 2197 O  O    . HOH F 5 .   ? -16.276 -9.898  32.816  1.00 16.97 ? 338 HOH A O    1 
HETATM 2198 O  O    . HOH F 5 .   ? -10.941 -19.399 7.066   1.00 25.78 ? 339 HOH A O    1 
HETATM 2199 O  O    . HOH F 5 .   ? -13.382 -18.491 14.511  1.00 15.45 ? 340 HOH A O    1 
HETATM 2200 O  O    . HOH F 5 .   ? -8.631  0.629   -6.476  1.00 22.37 ? 341 HOH A O    1 
HETATM 2201 O  O    . HOH F 5 .   ? -19.257 9.982   8.865   1.00 13.71 ? 342 HOH A O    1 
HETATM 2202 O  O    . HOH F 5 .   ? -27.217 -6.840  7.631   1.00 28.46 ? 343 HOH A O    1 
HETATM 2203 O  O    . HOH F 5 .   ? -30.696 1.450   26.021  1.00 20.66 ? 344 HOH A O    1 
HETATM 2204 O  O    . HOH F 5 .   ? -8.243  7.662   8.439   1.00 33.24 ? 345 HOH A O    1 
HETATM 2205 O  O    . HOH F 5 .   ? -21.163 -12.594 -1.837  1.00 17.15 ? 346 HOH A O    1 
HETATM 2206 O  O    . HOH F 5 .   ? -17.787 -21.947 5.920   1.00 16.69 ? 347 HOH A O    1 
HETATM 2207 O  O    . HOH F 5 .   ? -28.680 0.322   24.475  1.00 19.26 ? 348 HOH A O    1 
HETATM 2208 O  O    . HOH F 5 .   ? 1.483   -6.343  34.237  1.00 22.96 ? 349 HOH A O    1 
HETATM 2209 O  O    . HOH F 5 .   ? -24.983 9.499   12.755  1.00 28.19 ? 350 HOH A O    1 
HETATM 2210 O  O    . HOH F 5 .   ? -0.986  -11.168 28.853  1.00 19.46 ? 351 HOH A O    1 
HETATM 2211 O  O    . HOH F 5 .   ? -1.182  9.134   27.911  1.00 23.17 ? 352 HOH A O    1 
HETATM 2212 O  O    . HOH F 5 .   ? -28.084 5.723   18.992  1.00 27.29 ? 353 HOH A O    1 
HETATM 2213 O  O    . HOH F 5 .   ? 8.216   -5.766  -10.466 1.00 24.40 ? 354 HOH A O    1 
HETATM 2214 O  O    . HOH F 5 .   ? -13.989 14.056  27.038  1.00 20.43 ? 355 HOH A O    1 
HETATM 2215 O  O    . HOH F 5 .   ? -12.813 -17.152 16.737  1.00 12.31 ? 356 HOH A O    1 
HETATM 2216 O  O    . HOH F 5 .   ? -17.403 -16.194 21.926  1.00 20.94 ? 357 HOH A O    1 
HETATM 2217 O  O    . HOH F 5 .   ? -25.960 -6.353  12.937  1.00 26.80 ? 358 HOH A O    1 
HETATM 2218 O  O    . HOH F 5 .   ? -8.387  -15.331 36.512  1.00 25.55 ? 359 HOH A O    1 
HETATM 2219 O  O    . HOH F 5 .   ? -11.940 2.783   30.726  1.00 19.01 ? 360 HOH A O    1 
HETATM 2220 O  O    . HOH F 5 .   ? -6.140  15.127  11.849  1.00 25.25 ? 361 HOH A O    1 
HETATM 2221 O  O    . HOH F 5 .   ? 2.763   -4.285  7.743   1.00 20.41 ? 362 HOH A O    1 
HETATM 2222 O  O    . HOH F 5 .   ? -9.185  3.051   34.608  1.00 23.63 ? 363 HOH A O    1 
HETATM 2223 O  O    . HOH F 5 .   ? 2.560   -13.181 5.220   1.00 21.46 ? 364 HOH A O    1 
HETATM 2224 O  O    . HOH F 5 .   ? -26.195 3.231   15.456  1.00 24.01 ? 365 HOH A O    1 
HETATM 2225 O  O    . HOH F 5 .   ? -1.939  -17.430 25.492  1.00 23.79 ? 366 HOH A O    1 
HETATM 2226 O  O    . HOH F 5 .   ? 8.561   -4.614  23.653  1.00 27.40 ? 367 HOH A O    1 
HETATM 2227 O  O    . HOH F 5 .   ? 5.390   7.140   20.138  1.00 17.82 ? 368 HOH A O    1 
HETATM 2228 O  O    . HOH F 5 .   ? -17.332 -23.131 4.049   1.00 31.95 ? 369 HOH A O    1 
HETATM 2229 O  O    . HOH F 5 .   ? -2.546  -3.330  11.366  1.00 16.56 ? 370 HOH A O    1 
HETATM 2230 O  O    . HOH F 5 .   ? -7.193  -10.090 -4.596  1.00 29.83 ? 371 HOH A O    1 
HETATM 2231 O  O    . HOH F 5 .   ? -30.528 -6.961  22.233  1.00 24.26 ? 372 HOH A O    1 
HETATM 2232 O  O    . HOH F 5 .   ? -18.506 -3.507  -2.527  1.00 23.93 ? 373 HOH A O    1 
HETATM 2233 O  O    . HOH F 5 .   ? -14.604 -18.494 18.609  1.00 16.61 ? 374 HOH A O    1 
HETATM 2234 O  O    . HOH F 5 .   ? -26.400 2.932   20.952  1.00 26.58 ? 375 HOH A O    1 
HETATM 2235 O  O    . HOH F 5 .   ? -1.314  11.259  25.821  1.00 26.29 ? 376 HOH A O    1 
HETATM 2236 O  O    . HOH F 5 .   ? 2.051   -14.131 20.595  1.00 32.17 ? 377 HOH A O    1 
HETATM 2237 O  O    . HOH F 5 .   ? -23.188 -2.876  6.535   1.00 19.86 ? 378 HOH A O    1 
HETATM 2238 O  O    . HOH F 5 .   ? 2.592   -11.419 9.529   1.00 24.11 ? 379 HOH A O    1 
HETATM 2239 O  O    . HOH F 5 .   ? 2.107   2.956   -5.032  1.00 33.64 ? 380 HOH A O    1 
HETATM 2240 O  O    . HOH F 5 .   ? 6.104   -2.737  6.853   1.00 40.58 ? 381 HOH A O    1 
HETATM 2241 O  O    . HOH F 5 .   ? -26.734 -2.428  14.334  1.00 18.66 ? 382 HOH A O    1 
HETATM 2242 O  O    . HOH F 5 .   ? -26.520 -11.450 2.052   1.00 20.18 ? 383 HOH A O    1 
HETATM 2243 O  O    . HOH F 5 .   ? -20.253 10.762  26.715  1.00 16.78 ? 384 HOH A O    1 
HETATM 2244 O  O    . HOH F 5 .   ? -27.473 2.696   23.606  1.00 29.57 ? 385 HOH A O    1 
HETATM 2245 O  O    . HOH F 5 .   ? -17.690 19.873  17.501  1.00 23.40 ? 386 HOH A O    1 
HETATM 2246 O  O    . HOH F 5 .   ? 10.158  -2.362  13.689  1.00 23.01 ? 387 HOH A O    1 
HETATM 2247 O  O    . HOH F 5 .   ? -23.927 -0.745  26.449  1.00 17.56 ? 388 HOH A O    1 
HETATM 2248 O  O    . HOH F 5 .   ? -8.698  -14.965 33.211  1.00 38.09 ? 389 HOH A O    1 
HETATM 2249 O  O    . HOH F 5 .   ? -23.740 -0.745  3.847   1.00 23.97 ? 390 HOH A O    1 
HETATM 2250 O  O    . HOH F 5 .   ? -7.950  -22.225 10.489  1.00 20.06 ? 391 HOH A O    1 
HETATM 2251 O  O    . HOH F 5 .   ? -22.136 -18.247 13.473  1.00 23.06 ? 392 HOH A O    1 
HETATM 2252 O  O    . HOH F 5 .   ? -12.760 -19.497 26.225  1.00 24.28 ? 393 HOH A O    1 
HETATM 2253 O  O    . HOH F 5 .   ? -28.016 5.224   25.583  1.00 28.08 ? 394 HOH A O    1 
HETATM 2254 O  O    . HOH F 5 .   ? -25.504 -15.218 7.853   1.00 28.02 ? 395 HOH A O    1 
HETATM 2255 O  O    . HOH F 5 .   ? -12.834 18.808  8.457   1.00 26.73 ? 396 HOH A O    1 
HETATM 2256 O  O    . HOH F 5 .   ? 7.620   -7.989  -0.700  1.00 36.89 ? 397 HOH A O    1 
HETATM 2257 O  O    . HOH F 5 .   ? -12.987 -16.803 26.538  1.00 15.63 ? 398 HOH A O    1 
HETATM 2258 O  O    . HOH F 5 .   ? -14.151 -16.536 28.946  1.00 23.55 ? 399 HOH A O    1 
HETATM 2259 O  O    . HOH F 5 .   ? -15.302 -10.324 37.053  1.00 28.86 ? 400 HOH A O    1 
HETATM 2260 O  O    . HOH F 5 .   ? 10.638  -8.940  8.981   1.00 33.10 ? 401 HOH A O    1 
HETATM 2261 O  O    . HOH F 5 .   ? -11.121 -15.104 33.977  1.00 24.23 ? 402 HOH A O    1 
HETATM 2262 O  O    . HOH F 5 .   ? -8.907  -5.881  35.767  1.00 17.62 ? 403 HOH A O    1 
HETATM 2263 O  O    . HOH F 5 .   ? 8.328   3.147   27.609  1.00 28.90 ? 404 HOH A O    1 
HETATM 2264 O  O    . HOH F 5 .   ? -3.564  -12.856 -2.829  1.00 23.27 ? 405 HOH A O    1 
HETATM 2265 O  O    . HOH F 5 .   ? -25.828 6.229   26.916  1.00 23.06 ? 406 HOH A O    1 
HETATM 2266 O  O    . HOH F 5 .   ? -18.612 19.888  14.740  1.00 22.41 ? 407 HOH A O    1 
HETATM 2267 O  O    . HOH F 5 .   ? -19.346 -20.680 5.105   1.00 25.52 ? 408 HOH A O    1 
HETATM 2268 O  O    . HOH F 5 .   ? -10.611 21.582  19.889  1.00 22.67 ? 409 HOH A O    1 
HETATM 2269 O  O    . HOH F 5 .   ? -12.281 12.512  29.011  1.00 24.75 ? 410 HOH A O    1 
HETATM 2270 O  O    . HOH F 5 .   ? -15.722 8.410   38.005  1.00 26.81 ? 411 HOH A O    1 
HETATM 2271 O  O    . HOH F 5 .   ? -5.607  3.801   -5.614  1.00 31.70 ? 412 HOH A O    1 
HETATM 2272 O  O    . HOH F 5 .   ? -12.512 -18.220 32.290  1.00 29.59 ? 413 HOH A O    1 
HETATM 2273 O  O    . HOH F 5 .   ? -21.116 -20.344 1.708   1.00 32.64 ? 414 HOH A O    1 
HETATM 2274 O  O    . HOH F 5 .   ? 3.022   4.427   12.177  1.00 25.04 ? 415 HOH A O    1 
HETATM 2275 O  O    . HOH F 5 .   ? -18.616 -9.016  34.325  1.00 27.14 ? 416 HOH A O    1 
HETATM 2276 O  O    . HOH F 5 .   ? 2.285   8.051   27.467  1.00 30.91 ? 417 HOH A O    1 
HETATM 2277 O  O    . HOH F 5 .   ? -12.761 13.169  31.808  1.00 29.97 ? 418 HOH A O    1 
HETATM 2278 O  O    . HOH F 5 .   ? -25.630 4.072   4.269   1.00 37.85 ? 419 HOH A O    1 
HETATM 2279 O  O    . HOH F 5 .   ? -24.774 4.793   8.088   1.00 32.38 ? 420 HOH A O    1 
HETATM 2280 O  O    . HOH F 5 .   ? -31.755 -10.842 15.985  1.00 24.05 ? 421 HOH A O    1 
HETATM 2281 O  O    . HOH F 5 .   ? -12.700 7.965   28.860  1.00 24.03 ? 422 HOH A O    1 
HETATM 2282 O  O    . HOH F 5 .   ? 11.648  -0.416  15.894  1.00 22.66 ? 423 HOH A O    1 
HETATM 2283 O  O    . HOH F 5 .   ? -23.146 -0.588  34.279  1.00 27.83 ? 424 HOH A O    1 
HETATM 2284 O  O    . HOH F 5 .   ? -13.349 -22.563 11.820  1.00 35.53 ? 425 HOH A O    1 
HETATM 2285 O  O    . HOH F 5 .   ? -10.884 15.102  32.070  1.00 19.44 ? 426 HOH A O    1 
HETATM 2286 O  O    . HOH F 5 .   ? -12.686 3.771   -6.831  1.00 28.31 ? 427 HOH A O    1 
HETATM 2287 O  O    . HOH F 5 .   ? 1.308   14.661  24.249  1.00 31.11 ? 428 HOH A O    1 
HETATM 2288 O  O    . HOH F 5 .   ? 9.176   7.737   18.670  1.00 29.60 ? 429 HOH A O    1 
HETATM 2289 O  O    . HOH F 5 .   ? -9.624  15.659  7.784   1.00 29.12 ? 430 HOH A O    1 
HETATM 2290 O  O    . HOH F 5 .   ? -21.110 20.519  14.629  1.00 26.61 ? 431 HOH A O    1 
HETATM 2291 O  O    . HOH F 5 .   ? -17.069 -13.993 37.327  1.00 27.81 ? 432 HOH A O    1 
HETATM 2292 O  O    . HOH F 5 .   ? -20.535 8.289   30.044  1.00 23.50 ? 433 HOH A O    1 
HETATM 2293 O  O    . HOH F 5 .   ? -11.061 1.167   33.232  1.00 23.64 ? 434 HOH A O    1 
HETATM 2294 O  O    . HOH F 5 .   ? -23.459 -10.981 17.192  1.00 23.40 ? 435 HOH A O    1 
HETATM 2295 O  O    . HOH F 5 .   ? -26.750 -12.850 20.252  1.00 33.89 ? 436 HOH A O    1 
HETATM 2296 O  O    . HOH F 5 .   ? -21.142 -19.558 6.573   1.00 22.83 ? 437 HOH A O    1 
HETATM 2297 O  O    . HOH F 5 .   ? -11.545 1.082   -7.716  1.00 33.63 ? 438 HOH A O    1 
HETATM 2298 O  O    . HOH F 5 .   ? -10.179 14.973  5.624   1.00 36.15 ? 439 HOH A O    1 
HETATM 2299 O  O    . HOH F 5 .   ? -10.332 13.459  8.695   1.00 28.40 ? 440 HOH A O    1 
HETATM 2300 O  O    . HOH F 5 .   ? -5.921  -20.769 26.032  1.00 26.20 ? 441 HOH A O    1 
HETATM 2301 O  O    . HOH F 5 .   ? 2.352   -14.524 -5.815  1.00 32.40 ? 442 HOH A O    1 
HETATM 2302 O  O    . HOH F 5 .   ? -4.674  -15.932 0.658   1.00 25.00 ? 443 HOH A O    1 
HETATM 2303 O  O    . HOH F 5 .   ? 10.156  5.700   13.055  1.00 35.61 ? 444 HOH A O    1 
HETATM 2304 O  O    . HOH F 5 .   ? -24.662 -9.493  1.843   1.00 23.65 ? 445 HOH A O    1 
HETATM 2305 O  O    . HOH F 5 .   ? -12.148 16.130  8.343   1.00 32.10 ? 446 HOH A O    1 
HETATM 2306 O  O    . HOH F 5 .   ? -24.064 -3.377  29.445  1.00 26.48 ? 447 HOH A O    1 
HETATM 2307 O  O    . HOH F 5 .   ? -22.112 -13.957 18.540  1.00 27.92 ? 448 HOH A O    1 
HETATM 2308 O  O    . HOH F 5 .   ? -17.662 5.974   38.166  1.00 36.82 ? 449 HOH A O    1 
HETATM 2309 O  O    . HOH F 5 .   ? -16.928 -7.346  39.571  1.00 32.56 ? 450 HOH A O    1 
HETATM 2310 O  O    . HOH F 5 .   ? 5.249   -11.024 18.874  1.00 45.64 ? 451 HOH A O    1 
HETATM 2311 O  O    . HOH F 5 .   ? -27.764 6.400   21.546  1.00 32.28 ? 452 HOH A O    1 
HETATM 2312 O  O    . HOH F 5 .   ? -13.131 -9.018  -3.152  1.00 27.72 ? 453 HOH A O    1 
HETATM 2313 O  O    . HOH F 5 .   ? -3.381  18.004  21.324  1.00 29.07 ? 454 HOH A O    1 
HETATM 2314 O  O    . HOH F 5 .   ? -25.604 -10.502 17.622  1.00 28.27 ? 455 HOH A O    1 
HETATM 2315 O  O    . HOH F 5 .   ? 5.899   0.742   8.431   1.00 26.59 ? 456 HOH A O    1 
HETATM 2316 O  O    . HOH F 5 .   ? -24.663 11.930  6.222   1.00 28.76 ? 457 HOH A O    1 
HETATM 2317 O  O    . HOH F 5 .   ? -11.179 17.370  12.146  1.00 23.42 ? 458 HOH A O    1 
HETATM 2318 O  O    . HOH F 5 .   ? -35.808 -10.872 15.281  1.00 30.39 ? 459 HOH A O    1 
HETATM 2319 O  O    . HOH F 5 .   ? -4.221  -8.547  31.067  1.00 17.89 ? 460 HOH A O    1 
HETATM 2320 O  O    . HOH F 5 .   ? -26.231 -7.542  30.259  1.00 30.70 ? 461 HOH A O    1 
HETATM 2321 O  O    . HOH F 5 .   ? 12.931  -3.585  13.464  1.00 23.43 ? 462 HOH A O    1 
HETATM 2322 O  O    . HOH F 5 .   ? 3.338   -14.888 2.629   1.00 28.08 ? 463 HOH A O    1 
HETATM 2323 O  O    . HOH F 5 .   ? -18.001 -2.740  44.714  1.00 38.99 ? 464 HOH A O    1 
HETATM 2324 O  O    . HOH F 5 .   ? -7.734  -19.007 30.420  1.00 29.22 ? 465 HOH A O    1 
HETATM 2325 O  O    . HOH F 5 .   ? 7.311   3.634   31.555  1.00 47.97 ? 466 HOH A O    1 
HETATM 2326 O  O    . HOH F 5 .   ? -11.481 -10.988 -2.781  1.00 32.70 ? 467 HOH A O    1 
HETATM 2327 O  O    . HOH F 5 .   ? -16.868 -17.982 19.969  1.00 22.67 ? 468 HOH A O    1 
HETATM 2328 O  O    . HOH F 5 .   ? 3.425   0.768   -1.774  1.00 32.01 ? 469 HOH A O    1 
HETATM 2329 O  O    . HOH F 5 .   ? -26.666 -1.294  25.919  1.00 23.84 ? 470 HOH A O    1 
HETATM 2330 O  O    . HOH F 5 .   ? -27.857 -1.396  28.313  1.00 25.73 ? 471 HOH A O    1 
HETATM 2331 O  O    . HOH F 5 .   ? -10.753 8.688   7.552   1.00 26.41 ? 472 HOH A O    1 
HETATM 2332 O  O    . HOH F 5 .   ? -24.556 -3.364  4.647   1.00 39.24 ? 473 HOH A O    1 
HETATM 2333 O  O    . HOH F 5 .   ? 9.412   2.137   12.074  1.00 34.20 ? 474 HOH A O    1 
HETATM 2334 O  O    . HOH F 5 .   ? -23.934 -17.911 6.280   1.00 41.06 ? 475 HOH A O    1 
HETATM 2335 O  O    . HOH F 5 .   ? -19.405 17.378  6.155   1.00 29.81 ? 476 HOH A O    1 
HETATM 2336 O  O    . HOH F 5 .   ? -23.481 8.311   3.413   1.00 34.71 ? 477 HOH A O    1 
HETATM 2337 O  O    . HOH F 5 .   ? -16.464 -14.811 32.790  1.00 35.14 ? 478 HOH A O    1 
HETATM 2338 O  O    . HOH F 5 .   ? -25.828 -6.593  33.936  1.00 36.87 ? 479 HOH A O    1 
HETATM 2339 O  O    . HOH F 5 .   ? -31.423 4.070   7.722   1.00 38.15 ? 480 HOH A O    1 
HETATM 2340 O  O    . HOH F 5 .   ? -28.498 6.450   15.583  1.00 43.82 ? 481 HOH A O    1 
HETATM 2341 O  O    . HOH F 5 .   ? -9.097  6.623   -3.638  1.00 33.15 ? 482 HOH A O    1 
HETATM 2342 O  O    . HOH F 5 .   ? 0.958   2.959   1.856   1.00 37.71 ? 483 HOH A O    1 
HETATM 2343 O  O    . HOH F 5 .   ? -30.269 0.814   28.389  1.00 38.24 ? 484 HOH A O    1 
HETATM 2344 O  O    . HOH F 5 .   ? -6.406  12.228  10.276  1.00 35.52 ? 485 HOH A O    1 
HETATM 2345 O  O    . HOH F 5 .   ? -4.156  -1.169  11.733  1.00 21.20 ? 486 HOH A O    1 
HETATM 2346 O  O    . HOH F 5 .   ? -17.778 -12.036 31.443  1.00 29.29 ? 487 HOH A O    1 
HETATM 2347 O  O    . HOH F 5 .   ? -27.487 -0.007  14.997  1.00 27.02 ? 488 HOH A O    1 
HETATM 2348 O  O    . HOH F 5 .   ? -15.819 16.976  26.346  1.00 37.83 ? 489 HOH A O    1 
HETATM 2349 O  O    . HOH F 5 .   ? -7.032  -15.529 38.584  1.00 26.55 ? 490 HOH A O    1 
HETATM 2350 O  O    . HOH F 5 .   ? 2.864   -13.466 8.187   1.00 27.99 ? 491 HOH A O    1 
HETATM 2351 O  O    . HOH F 5 .   ? -12.121 10.675  5.758   1.00 27.98 ? 492 HOH A O    1 
HETATM 2352 O  O    . HOH F 5 .   ? -8.387  -14.600 40.327  1.00 25.09 ? 493 HOH A O    1 
HETATM 2353 O  O    . HOH F 5 .   ? -4.839  -9.718  33.376  1.00 32.66 ? 494 HOH A O    1 
HETATM 2354 O  O    . HOH F 5 .   ? 2.011   -6.989  -7.926  1.00 31.61 ? 495 HOH A O    1 
HETATM 2355 O  O    . HOH F 5 .   ? -10.440 20.562  24.847  1.00 23.15 ? 496 HOH A O    1 
HETATM 2356 O  O    . HOH F 5 .   ? 4.875   -13.013 -5.803  1.00 29.48 ? 497 HOH A O    1 
HETATM 2357 O  O    . HOH F 5 .   ? -4.619  -7.718  -8.185  1.00 37.29 ? 498 HOH A O    1 
HETATM 2358 O  O    . HOH F 5 .   ? -21.525 -13.882 22.876  1.00 26.90 ? 499 HOH A O    1 
HETATM 2359 O  O    . HOH F 5 .   ? -2.469  -9.173  34.332  1.00 39.57 ? 500 HOH A O    1 
HETATM 2360 O  O    . HOH F 5 .   ? -0.541  1.178   -10.730 1.00 30.63 ? 501 HOH A O    1 
HETATM 2361 O  O    . HOH F 5 .   ? -22.459 -12.305 24.691  1.00 30.68 ? 502 HOH A O    1 
HETATM 2362 O  O    . HOH F 5 .   ? -0.400  13.935  16.019  1.00 25.55 ? 503 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 E38 1   265 1   E38 E38 A . 
F 5 HOH 1   126 126 HOH HOH A . 
F 5 HOH 2   266 1   HOH HOH A . 
F 5 HOH 3   267 2   HOH HOH A . 
F 5 HOH 4   268 3   HOH HOH A . 
F 5 HOH 5   269 4   HOH HOH A . 
F 5 HOH 6   270 5   HOH HOH A . 
F 5 HOH 7   271 6   HOH HOH A . 
F 5 HOH 8   272 7   HOH HOH A . 
F 5 HOH 9   273 8   HOH HOH A . 
F 5 HOH 10  274 9   HOH HOH A . 
F 5 HOH 11  275 10  HOH HOH A . 
F 5 HOH 12  276 11  HOH HOH A . 
F 5 HOH 13  277 12  HOH HOH A . 
F 5 HOH 14  278 13  HOH HOH A . 
F 5 HOH 15  279 14  HOH HOH A . 
F 5 HOH 16  280 15  HOH HOH A . 
F 5 HOH 17  281 16  HOH HOH A . 
F 5 HOH 18  282 17  HOH HOH A . 
F 5 HOH 19  283 18  HOH HOH A . 
F 5 HOH 20  284 19  HOH HOH A . 
F 5 HOH 21  285 20  HOH HOH A . 
F 5 HOH 22  286 21  HOH HOH A . 
F 5 HOH 23  287 22  HOH HOH A . 
F 5 HOH 24  288 23  HOH HOH A . 
F 5 HOH 25  289 24  HOH HOH A . 
F 5 HOH 26  290 25  HOH HOH A . 
F 5 HOH 27  291 26  HOH HOH A . 
F 5 HOH 28  292 27  HOH HOH A . 
F 5 HOH 29  293 28  HOH HOH A . 
F 5 HOH 30  294 29  HOH HOH A . 
F 5 HOH 31  295 30  HOH HOH A . 
F 5 HOH 32  296 31  HOH HOH A . 
F 5 HOH 33  297 32  HOH HOH A . 
F 5 HOH 34  298 33  HOH HOH A . 
F 5 HOH 35  299 34  HOH HOH A . 
F 5 HOH 36  300 35  HOH HOH A . 
F 5 HOH 37  301 36  HOH HOH A . 
F 5 HOH 38  302 37  HOH HOH A . 
F 5 HOH 39  303 38  HOH HOH A . 
F 5 HOH 40  304 39  HOH HOH A . 
F 5 HOH 41  305 40  HOH HOH A . 
F 5 HOH 42  306 41  HOH HOH A . 
F 5 HOH 43  307 42  HOH HOH A . 
F 5 HOH 44  308 43  HOH HOH A . 
F 5 HOH 45  309 44  HOH HOH A . 
F 5 HOH 46  310 45  HOH HOH A . 
F 5 HOH 47  311 46  HOH HOH A . 
F 5 HOH 48  312 47  HOH HOH A . 
F 5 HOH 49  313 48  HOH HOH A . 
F 5 HOH 50  314 49  HOH HOH A . 
F 5 HOH 51  315 50  HOH HOH A . 
F 5 HOH 52  316 51  HOH HOH A . 
F 5 HOH 53  317 52  HOH HOH A . 
F 5 HOH 54  318 53  HOH HOH A . 
F 5 HOH 55  319 54  HOH HOH A . 
F 5 HOH 56  320 55  HOH HOH A . 
F 5 HOH 57  321 56  HOH HOH A . 
F 5 HOH 58  322 57  HOH HOH A . 
F 5 HOH 59  323 58  HOH HOH A . 
F 5 HOH 60  324 59  HOH HOH A . 
F 5 HOH 61  325 60  HOH HOH A . 
F 5 HOH 62  326 61  HOH HOH A . 
F 5 HOH 63  327 62  HOH HOH A . 
F 5 HOH 64  328 63  HOH HOH A . 
F 5 HOH 65  329 64  HOH HOH A . 
F 5 HOH 66  330 65  HOH HOH A . 
F 5 HOH 67  331 66  HOH HOH A . 
F 5 HOH 68  332 67  HOH HOH A . 
F 5 HOH 69  333 68  HOH HOH A . 
F 5 HOH 70  334 69  HOH HOH A . 
F 5 HOH 71  335 70  HOH HOH A . 
F 5 HOH 72  336 71  HOH HOH A . 
F 5 HOH 73  337 72  HOH HOH A . 
F 5 HOH 74  338 73  HOH HOH A . 
F 5 HOH 75  339 74  HOH HOH A . 
F 5 HOH 76  340 75  HOH HOH A . 
F 5 HOH 77  341 76  HOH HOH A . 
F 5 HOH 78  342 77  HOH HOH A . 
F 5 HOH 79  343 78  HOH HOH A . 
F 5 HOH 80  344 79  HOH HOH A . 
F 5 HOH 81  345 80  HOH HOH A . 
F 5 HOH 82  346 81  HOH HOH A . 
F 5 HOH 83  347 82  HOH HOH A . 
F 5 HOH 84  348 83  HOH HOH A . 
F 5 HOH 85  349 84  HOH HOH A . 
F 5 HOH 86  350 85  HOH HOH A . 
F 5 HOH 87  351 86  HOH HOH A . 
F 5 HOH 88  352 87  HOH HOH A . 
F 5 HOH 89  353 88  HOH HOH A . 
F 5 HOH 90  354 89  HOH HOH A . 
F 5 HOH 91  355 90  HOH HOH A . 
F 5 HOH 92  356 91  HOH HOH A . 
F 5 HOH 93  357 92  HOH HOH A . 
F 5 HOH 94  358 93  HOH HOH A . 
F 5 HOH 95  359 94  HOH HOH A . 
F 5 HOH 96  360 95  HOH HOH A . 
F 5 HOH 97  361 96  HOH HOH A . 
F 5 HOH 98  362 97  HOH HOH A . 
F 5 HOH 99  363 98  HOH HOH A . 
F 5 HOH 100 364 99  HOH HOH A . 
F 5 HOH 101 365 100 HOH HOH A . 
F 5 HOH 102 366 101 HOH HOH A . 
F 5 HOH 103 367 102 HOH HOH A . 
F 5 HOH 104 368 103 HOH HOH A . 
F 5 HOH 105 369 104 HOH HOH A . 
F 5 HOH 106 370 105 HOH HOH A . 
F 5 HOH 107 371 106 HOH HOH A . 
F 5 HOH 108 372 107 HOH HOH A . 
F 5 HOH 109 373 108 HOH HOH A . 
F 5 HOH 110 374 109 HOH HOH A . 
F 5 HOH 111 375 110 HOH HOH A . 
F 5 HOH 112 376 111 HOH HOH A . 
F 5 HOH 113 377 112 HOH HOH A . 
F 5 HOH 114 378 113 HOH HOH A . 
F 5 HOH 115 379 114 HOH HOH A . 
F 5 HOH 116 380 115 HOH HOH A . 
F 5 HOH 117 381 116 HOH HOH A . 
F 5 HOH 118 382 117 HOH HOH A . 
F 5 HOH 119 383 118 HOH HOH A . 
F 5 HOH 120 384 119 HOH HOH A . 
F 5 HOH 121 385 120 HOH HOH A . 
F 5 HOH 122 386 121 HOH HOH A . 
F 5 HOH 123 387 122 HOH HOH A . 
F 5 HOH 124 388 123 HOH HOH A . 
F 5 HOH 125 389 124 HOH HOH A . 
F 5 HOH 126 390 125 HOH HOH A . 
F 5 HOH 127 391 127 HOH HOH A . 
F 5 HOH 128 392 128 HOH HOH A . 
F 5 HOH 129 393 129 HOH HOH A . 
F 5 HOH 130 394 130 HOH HOH A . 
F 5 HOH 131 395 131 HOH HOH A . 
F 5 HOH 132 396 132 HOH HOH A . 
F 5 HOH 133 397 133 HOH HOH A . 
F 5 HOH 134 398 134 HOH HOH A . 
F 5 HOH 135 399 135 HOH HOH A . 
F 5 HOH 136 400 136 HOH HOH A . 
F 5 HOH 137 401 137 HOH HOH A . 
F 5 HOH 138 402 138 HOH HOH A . 
F 5 HOH 139 403 139 HOH HOH A . 
F 5 HOH 140 404 140 HOH HOH A . 
F 5 HOH 141 405 141 HOH HOH A . 
F 5 HOH 142 406 142 HOH HOH A . 
F 5 HOH 143 407 143 HOH HOH A . 
F 5 HOH 144 408 144 HOH HOH A . 
F 5 HOH 145 409 145 HOH HOH A . 
F 5 HOH 146 410 146 HOH HOH A . 
F 5 HOH 147 411 147 HOH HOH A . 
F 5 HOH 148 412 148 HOH HOH A . 
F 5 HOH 149 413 149 HOH HOH A . 
F 5 HOH 150 414 150 HOH HOH A . 
F 5 HOH 151 415 151 HOH HOH A . 
F 5 HOH 152 416 152 HOH HOH A . 
F 5 HOH 153 417 153 HOH HOH A . 
F 5 HOH 154 418 154 HOH HOH A . 
F 5 HOH 155 419 155 HOH HOH A . 
F 5 HOH 156 420 156 HOH HOH A . 
F 5 HOH 157 421 157 HOH HOH A . 
F 5 HOH 158 422 158 HOH HOH A . 
F 5 HOH 159 423 159 HOH HOH A . 
F 5 HOH 160 424 160 HOH HOH A . 
F 5 HOH 161 425 161 HOH HOH A . 
F 5 HOH 162 426 162 HOH HOH A . 
F 5 HOH 163 427 163 HOH HOH A . 
F 5 HOH 164 428 164 HOH HOH A . 
F 5 HOH 165 429 165 HOH HOH A . 
F 5 HOH 166 430 166 HOH HOH A . 
F 5 HOH 167 431 167 HOH HOH A . 
F 5 HOH 168 432 168 HOH HOH A . 
F 5 HOH 169 433 169 HOH HOH A . 
F 5 HOH 170 434 170 HOH HOH A . 
F 5 HOH 171 435 171 HOH HOH A . 
F 5 HOH 172 436 172 HOH HOH A . 
F 5 HOH 173 437 173 HOH HOH A . 
F 5 HOH 174 438 174 HOH HOH A . 
F 5 HOH 175 439 175 HOH HOH A . 
F 5 HOH 176 440 176 HOH HOH A . 
F 5 HOH 177 441 178 HOH HOH A . 
F 5 HOH 178 442 180 HOH HOH A . 
F 5 HOH 179 443 181 HOH HOH A . 
F 5 HOH 180 444 182 HOH HOH A . 
F 5 HOH 181 445 183 HOH HOH A . 
F 5 HOH 182 446 184 HOH HOH A . 
F 5 HOH 183 447 185 HOH HOH A . 
F 5 HOH 184 448 186 HOH HOH A . 
F 5 HOH 185 449 187 HOH HOH A . 
F 5 HOH 186 450 188 HOH HOH A . 
F 5 HOH 187 451 189 HOH HOH A . 
F 5 HOH 188 452 190 HOH HOH A . 
F 5 HOH 189 453 191 HOH HOH A . 
F 5 HOH 190 454 192 HOH HOH A . 
F 5 HOH 191 455 193 HOH HOH A . 
F 5 HOH 192 456 194 HOH HOH A . 
F 5 HOH 193 457 195 HOH HOH A . 
F 5 HOH 194 458 196 HOH HOH A . 
F 5 HOH 195 459 197 HOH HOH A . 
F 5 HOH 196 460 198 HOH HOH A . 
F 5 HOH 197 461 199 HOH HOH A . 
F 5 HOH 198 462 200 HOH HOH A . 
F 5 HOH 199 463 201 HOH HOH A . 
F 5 HOH 200 464 202 HOH HOH A . 
F 5 HOH 201 465 203 HOH HOH A . 
F 5 HOH 202 466 205 HOH HOH A . 
F 5 HOH 203 467 206 HOH HOH A . 
F 5 HOH 204 468 207 HOH HOH A . 
F 5 HOH 205 469 208 HOH HOH A . 
F 5 HOH 206 470 209 HOH HOH A . 
F 5 HOH 207 471 210 HOH HOH A . 
F 5 HOH 208 472 211 HOH HOH A . 
F 5 HOH 209 473 212 HOH HOH A . 
F 5 HOH 210 474 213 HOH HOH A . 
F 5 HOH 211 475 214 HOH HOH A . 
F 5 HOH 212 476 215 HOH HOH A . 
F 5 HOH 213 477 216 HOH HOH A . 
F 5 HOH 214 478 217 HOH HOH A . 
F 5 HOH 215 479 218 HOH HOH A . 
F 5 HOH 216 480 219 HOH HOH A . 
F 5 HOH 217 481 220 HOH HOH A . 
F 5 HOH 218 482 221 HOH HOH A . 
F 5 HOH 219 483 222 HOH HOH A . 
F 5 HOH 220 484 223 HOH HOH A . 
F 5 HOH 221 485 224 HOH HOH A . 
F 5 HOH 222 486 225 HOH HOH A . 
F 5 HOH 223 487 226 HOH HOH A . 
F 5 HOH 224 488 227 HOH HOH A . 
F 5 HOH 225 489 228 HOH HOH A . 
F 5 HOH 226 490 229 HOH HOH A . 
F 5 HOH 227 491 230 HOH HOH A . 
F 5 HOH 228 492 231 HOH HOH A . 
F 5 HOH 229 493 232 HOH HOH A . 
F 5 HOH 230 494 233 HOH HOH A . 
F 5 HOH 231 495 234 HOH HOH A . 
F 5 HOH 232 496 235 HOH HOH A . 
F 5 HOH 233 497 236 HOH HOH A . 
F 5 HOH 234 498 237 HOH HOH A . 
F 5 HOH 235 499 238 HOH HOH A . 
F 5 HOH 236 500 239 HOH HOH A . 
F 5 HOH 237 501 240 HOH HOH A . 
F 5 HOH 238 502 241 HOH HOH A . 
F 5 HOH 239 503 242 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 2011-02-02 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-08 
4 'Structure model' 1 3 2023-09-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Refinement description'    
3 4 'Structure model' 'Data collection'           
4 4 'Structure model' 'Database references'       
5 4 'Structure model' 'Derived calculations'      
6 4 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' software                      
2 4 'Structure model' chem_comp_atom                
3 4 'Structure model' chem_comp_bond                
4 4 'Structure model' database_2                    
5 4 'Structure model' diffrn_source                 
6 4 'Structure model' pdbx_initial_refinement_model 
7 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       3.2.25 21/9/2006       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      .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NE2 A GLN 137 ? ? O A HOH 454 ? ? 2.10 
2 1 O   A HOH 347 ? ? O A HOH 408 ? ? 2.17 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CZ A ARG 27  ? ? NH2 A ARG 27  ? ? 1.236 1.326 -0.090 0.013 N 
2 1 CZ A TYR 88  ? ? CE2 A TYR 88  ? ? 1.303 1.381 -0.078 0.013 N 
3 1 CD A LYS 213 ? ? CE  A LYS 213 ? ? 1.669 1.508 0.161  0.025 N 
4 1 CE A LYS 213 ? ? NZ  A LYS 213 ? ? 1.673 1.486 0.187  0.025 N 
# 
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 CB A ASP 34  ? ? CG A ASP 34  ? ? OD2 A ASP 34  ? ? 112.63 118.30 -5.67  0.90 N 
2  1 C  A ASP 85  ? ? N  A GLY 86  ? ? CA  A GLY 86  ? ? 107.00 122.30 -15.30 2.10 Y 
3  1 CB A ASP 101 ? ? CG A ASP 101 ? ? OD1 A ASP 101 ? ? 126.13 118.30 7.83   0.90 N 
4  1 CB A ASP 139 ? ? CG A ASP 139 ? ? OD1 A ASP 139 ? ? 123.79 118.30 5.49   0.90 N 
5  1 CB A LEU 198 ? ? CG A LEU 198 ? ? CD2 A LEU 198 ? ? 125.63 111.00 14.63  1.70 N 
6  1 CD A LYS 213 ? ? CE A LYS 213 ? ? NZ  A LYS 213 ? ? 127.81 111.70 16.11  2.30 N 
7  1 CB A PHE 226 ? ? CG A PHE 226 ? ? CD2 A PHE 226 ? ? 116.03 120.80 -4.77  0.70 N 
8  1 CB A PHE 226 ? ? CG A PHE 226 ? ? CD1 A PHE 226 ? ? 126.77 120.80 5.97   0.70 N 
9  1 NE A ARG 246 ? ? CZ A ARG 246 ? ? NH1 A ARG 246 ? ? 124.89 120.30 4.59   0.50 N 
10 1 NE A ARG 246 ? ? CZ A ARG 246 ? ? NH2 A ARG 246 ? ? 117.23 120.30 -3.07  0.50 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 ARG A 27  ? ? -145.71 59.66   
2 1 LYS A 76  ? ? -114.54 -84.50  
3 1 ASN A 244 ? ? -96.50  52.20   
4 1 LYS A 252 ? ? 57.06   -135.46 
# 
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  
E38 N1   N  Y N 98  
E38 C2   C  Y N 99  
E38 N3   N  Y N 100 
E38 C4   C  Y N 101 
E38 C5   C  Y N 102 
E38 C6   C  Y N 103 
E38 C7   C  Y N 104 
E38 C8   C  Y N 105 
E38 C9   C  Y N 106 
E38 S10  S  N N 107 
E38 C11  C  N N 108 
E38 C12  C  N N 109 
E38 O13  O  N N 110 
E38 BR14 BR N N 111 
E38 C15  C  Y N 112 
E38 C16  C  Y N 113 
E38 C17  C  Y N 114 
E38 C18  C  Y N 115 
E38 C19  C  Y N 116 
E38 C20  C  Y N 117 
E38 S21  S  N N 118 
E38 O22  O  N N 119 
E38 CL23 CL N N 120 
E38 O24  O  N N 121 
E38 N25  N  N N 122 
E38 H6   H  N N 123 
E38 H7   H  N N 124 
E38 H9   H  N N 125 
E38 H11  H  N N 126 
E38 H11A H  N N 127 
E38 H16  H  N N 128 
E38 H19  H  N N 129 
E38 H20  H  N N 130 
E38 HN25 H  N N 131 
E38 HN2A H  N N 132 
E38 HN1  H  N N 133 
GLN N    N  N N 134 
GLN CA   C  N S 135 
GLN C    C  N N 136 
GLN O    O  N N 137 
GLN CB   C  N N 138 
GLN CG   C  N N 139 
GLN CD   C  N N 140 
GLN OE1  O  N N 141 
GLN NE2  N  N N 142 
GLN OXT  O  N N 143 
GLN H    H  N N 144 
GLN H2   H  N N 145 
GLN HA   H  N N 146 
GLN HB2  H  N N 147 
GLN HB3  H  N N 148 
GLN HG2  H  N N 149 
GLN HG3  H  N N 150 
GLN HE21 H  N N 151 
GLN HE22 H  N N 152 
GLN HXT  H  N N 153 
GLU N    N  N N 154 
GLU CA   C  N S 155 
GLU C    C  N N 156 
GLU O    O  N N 157 
GLU CB   C  N N 158 
GLU CG   C  N N 159 
GLU CD   C  N N 160 
GLU OE1  O  N N 161 
GLU OE2  O  N N 162 
GLU OXT  O  N N 163 
GLU H    H  N N 164 
GLU H2   H  N N 165 
GLU HA   H  N N 166 
GLU HB2  H  N N 167 
GLU HB3  H  N N 168 
GLU HG2  H  N N 169 
GLU HG3  H  N N 170 
GLU HE2  H  N N 171 
GLU HXT  H  N N 172 
GLY N    N  N N 173 
GLY CA   C  N N 174 
GLY C    C  N N 175 
GLY O    O  N N 176 
GLY OXT  O  N N 177 
GLY H    H  N N 178 
GLY H2   H  N N 179 
GLY HA2  H  N N 180 
GLY HA3  H  N N 181 
GLY HXT  H  N N 182 
HIS N    N  N N 183 
HIS CA   C  N S 184 
HIS C    C  N N 185 
HIS O    O  N N 186 
HIS CB   C  N N 187 
HIS CG   C  Y N 188 
HIS ND1  N  Y N 189 
HIS CD2  C  Y N 190 
HIS CE1  C  Y N 191 
HIS NE2  N  Y N 192 
HIS OXT  O  N N 193 
HIS H    H  N N 194 
HIS H2   H  N N 195 
HIS HA   H  N N 196 
HIS HB2  H  N N 197 
HIS HB3  H  N N 198 
HIS HD1  H  N N 199 
HIS HD2  H  N N 200 
HIS HE1  H  N N 201 
HIS HE2  H  N N 202 
HIS HXT  H  N N 203 
HOH O    O  N N 204 
HOH H1   H  N N 205 
HOH H2   H  N N 206 
ILE N    N  N N 207 
ILE CA   C  N S 208 
ILE C    C  N N 209 
ILE O    O  N N 210 
ILE CB   C  N S 211 
ILE CG1  C  N N 212 
ILE CG2  C  N N 213 
ILE CD1  C  N N 214 
ILE OXT  O  N N 215 
ILE H    H  N N 216 
ILE H2   H  N N 217 
ILE HA   H  N N 218 
ILE HB   H  N N 219 
ILE HG12 H  N N 220 
ILE HG13 H  N N 221 
ILE HG21 H  N N 222 
ILE HG22 H  N N 223 
ILE HG23 H  N N 224 
ILE HD11 H  N N 225 
ILE HD12 H  N N 226 
ILE HD13 H  N N 227 
ILE HXT  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  
E38 N1  C2   sing Y N 92  
E38 N1  C5   sing Y N 93  
E38 S10 C2   sing N N 94  
E38 C2  N3   doub Y N 95  
E38 N3  C4   sing Y N 96  
E38 C5  C4   doub Y N 97  
E38 C4  C9   sing Y N 98  
E38 C6  C5   sing Y N 99  
E38 C6  C7   doub Y N 100 
E38 C6  H6   sing N N 101 
E38 C7  C8   sing Y N 102 
E38 C7  H7   sing N N 103 
E38 C8  C9   doub Y N 104 
E38 C8  BR14 sing N N 105 
E38 C9  H9   sing N N 106 
E38 S10 C11  sing N N 107 
E38 C11 C12  sing N N 108 
E38 C11 H11  sing N N 109 
E38 C11 H11A sing N N 110 
E38 O13 C12  doub N N 111 
E38 C12 C15  sing N N 112 
E38 C15 C20  doub Y N 113 
E38 C15 C16  sing Y N 114 
E38 C16 C17  doub Y N 115 
E38 C16 H16  sing N N 116 
E38 C17 C18  sing Y N 117 
E38 C17 S21  sing N N 118 
E38 C19 C18  doub Y N 119 
E38 C18 CL23 sing N N 120 
E38 C20 C19  sing Y N 121 
E38 C19 H19  sing N N 122 
E38 C20 H20  sing N N 123 
E38 N25 S21  sing N N 124 
E38 S21 O22  doub N N 125 
E38 S21 O24  doub N N 126 
E38 N25 HN25 sing N N 127 
E38 N25 HN2A sing N N 128 
E38 N1  HN1  sing N N 129 
GLN N   CA   sing N N 130 
GLN N   H    sing N N 131 
GLN N   H2   sing N N 132 
GLN CA  C    sing N N 133 
GLN CA  CB   sing N N 134 
GLN CA  HA   sing N N 135 
GLN C   O    doub N N 136 
GLN C   OXT  sing N N 137 
GLN CB  CG   sing N N 138 
GLN CB  HB2  sing N N 139 
GLN CB  HB3  sing N N 140 
GLN CG  CD   sing N N 141 
GLN CG  HG2  sing N N 142 
GLN CG  HG3  sing N N 143 
GLN CD  OE1  doub N N 144 
GLN CD  NE2  sing N N 145 
GLN NE2 HE21 sing N N 146 
GLN NE2 HE22 sing N N 147 
GLN OXT HXT  sing N N 148 
GLU N   CA   sing N N 149 
GLU N   H    sing N N 150 
GLU N   H2   sing N N 151 
GLU CA  C    sing N N 152 
GLU CA  CB   sing N N 153 
GLU CA  HA   sing N N 154 
GLU C   O    doub N N 155 
GLU C   OXT  sing N N 156 
GLU CB  CG   sing N N 157 
GLU CB  HB2  sing N N 158 
GLU CB  HB3  sing N N 159 
GLU CG  CD   sing N N 160 
GLU CG  HG2  sing N N 161 
GLU CG  HG3  sing N N 162 
GLU CD  OE1  doub N N 163 
GLU CD  OE2  sing N N 164 
GLU OE2 HE2  sing N N 165 
GLU OXT HXT  sing N N 166 
GLY N   CA   sing N N 167 
GLY N   H    sing N N 168 
GLY N   H2   sing N N 169 
GLY CA  C    sing N N 170 
GLY CA  HA2  sing N N 171 
GLY CA  HA3  sing N N 172 
GLY C   O    doub N N 173 
GLY C   OXT  sing N N 174 
GLY OXT HXT  sing N N 175 
HIS N   CA   sing N N 176 
HIS N   H    sing N N 177 
HIS N   H2   sing N N 178 
HIS CA  C    sing N N 179 
HIS CA  CB   sing N N 180 
HIS CA  HA   sing N N 181 
HIS C   O    doub N N 182 
HIS C   OXT  sing N N 183 
HIS CB  CG   sing N N 184 
HIS CB  HB2  sing N N 185 
HIS CB  HB3  sing N N 186 
HIS CG  ND1  sing Y N 187 
HIS CG  CD2  doub Y N 188 
HIS ND1 CE1  doub Y N 189 
HIS ND1 HD1  sing N N 190 
HIS CD2 NE2  sing Y N 191 
HIS CD2 HD2  sing N N 192 
HIS CE1 NE2  sing Y N 193 
HIS CE1 HE1  sing N N 194 
HIS NE2 HE2  sing N N 195 
HIS OXT HXT  sing N N 196 
HOH O   H1   sing N N 197 
HOH O   H2   sing N N 198 
ILE N   CA   sing N N 199 
ILE N   H    sing N N 200 
ILE N   H2   sing N N 201 
ILE CA  C    sing N N 202 
ILE CA  CB   sing N N 203 
ILE CA  HA   sing N N 204 
ILE C   O    doub N N 205 
ILE C   OXT  sing N N 206 
ILE CB  CG1  sing N N 207 
ILE CB  CG2  sing N N 208 
ILE CB  HB   sing N N 209 
ILE CG1 CD1  sing N N 210 
ILE CG1 HG12 sing N N 211 
ILE CG1 HG13 sing N N 212 
ILE CG2 HG21 sing N N 213 
ILE CG2 HG22 sing N N 214 
ILE CG2 HG23 sing N N 215 
ILE CD1 HD11 sing N N 216 
ILE CD1 HD12 sing N N 217 
ILE CD1 HD13 sing N N 218 
ILE OXT HXT  sing N N 219 
LEU N   CA   sing N N 220 
LEU N   H    sing N N 221 
LEU N   H2   sing N N 222 
LEU CA  C    sing N N 223 
LEU CA  CB   sing N N 224 
LEU CA  HA   sing N N 225 
LEU C   O    doub N N 226 
LEU C   OXT  sing N N 227 
LEU CB  CG   sing N N 228 
LEU CB  HB2  sing N N 229 
LEU CB  HB3  sing N N 230 
LEU CG  CD1  sing N N 231 
LEU CG  CD2  sing N N 232 
LEU CG  HG   sing N N 233 
LEU CD1 HD11 sing N N 234 
LEU CD1 HD12 sing N N 235 
LEU CD1 HD13 sing N N 236 
LEU CD2 HD21 sing N N 237 
LEU CD2 HD22 sing N N 238 
LEU CD2 HD23 sing N N 239 
LEU OXT HXT  sing N N 240 
LYS N   CA   sing N N 241 
LYS N   H    sing N N 242 
LYS N   H2   sing N N 243 
LYS CA  C    sing N N 244 
LYS CA  CB   sing N N 245 
LYS CA  HA   sing N N 246 
LYS C   O    doub N N 247 
LYS C   OXT  sing N N 248 
LYS CB  CG   sing N N 249 
LYS CB  HB2  sing N N 250 
LYS CB  HB3  sing N N 251 
LYS CG  CD   sing N N 252 
LYS CG  HG2  sing N N 253 
LYS CG  HG3  sing N N 254 
LYS CD  CE   sing N N 255 
LYS CD  HD2  sing N N 256 
LYS CD  HD3  sing N N 257 
LYS CE  NZ   sing N N 258 
LYS CE  HE2  sing N N 259 
LYS CE  HE3  sing N N 260 
LYS NZ  HZ1  sing N N 261 
LYS NZ  HZ2  sing N N 262 
LYS NZ  HZ3  sing N N 263 
LYS OXT HXT  sing N N 264 
MET N   CA   sing N N 265 
MET N   H    sing N N 266 
MET N   H2   sing N N 267 
MET CA  C    sing N N 268 
MET CA  CB   sing N N 269 
MET CA  HA   sing N N 270 
MET C   O    doub N N 271 
MET C   OXT  sing N N 272 
MET CB  CG   sing N N 273 
MET CB  HB2  sing N N 274 
MET CB  HB3  sing N N 275 
MET CG  SD   sing N N 276 
MET CG  HG2  sing N N 277 
MET CG  HG3  sing N N 278 
MET SD  CE   sing N N 279 
MET CE  HE1  sing N N 280 
MET CE  HE2  sing N N 281 
MET CE  HE3  sing N N 282 
MET OXT HXT  sing N N 283 
PHE N   CA   sing N N 284 
PHE N   H    sing N N 285 
PHE N   H2   sing N N 286 
PHE CA  C    sing N N 287 
PHE CA  CB   sing N N 288 
PHE CA  HA   sing N N 289 
PHE C   O    doub N N 290 
PHE C   OXT  sing N N 291 
PHE CB  CG   sing N N 292 
PHE CB  HB2  sing N N 293 
PHE CB  HB3  sing N N 294 
PHE CG  CD1  doub Y N 295 
PHE CG  CD2  sing Y N 296 
PHE CD1 CE1  sing Y N 297 
PHE CD1 HD1  sing N N 298 
PHE CD2 CE2  doub Y N 299 
PHE CD2 HD2  sing N N 300 
PHE CE1 CZ   doub Y N 301 
PHE CE1 HE1  sing N N 302 
PHE CE2 CZ   sing Y N 303 
PHE CE2 HE2  sing N N 304 
PHE CZ  HZ   sing N N 305 
PHE OXT HXT  sing N N 306 
PRO N   CA   sing N N 307 
PRO N   CD   sing N N 308 
PRO N   H    sing N N 309 
PRO CA  C    sing N N 310 
PRO CA  CB   sing N N 311 
PRO CA  HA   sing N N 312 
PRO C   O    doub N N 313 
PRO C   OXT  sing N N 314 
PRO CB  CG   sing N N 315 
PRO CB  HB2  sing N N 316 
PRO CB  HB3  sing N N 317 
PRO CG  CD   sing N N 318 
PRO CG  HG2  sing N N 319 
PRO CG  HG3  sing N N 320 
PRO CD  HD2  sing N N 321 
PRO CD  HD3  sing N N 322 
PRO OXT HXT  sing N N 323 
SER N   CA   sing N N 324 
SER N   H    sing N N 325 
SER N   H2   sing N N 326 
SER CA  C    sing N N 327 
SER CA  CB   sing N N 328 
SER CA  HA   sing N N 329 
SER C   O    doub N N 330 
SER C   OXT  sing N N 331 
SER CB  OG   sing N N 332 
SER CB  HB2  sing N N 333 
SER CB  HB3  sing N N 334 
SER OG  HG   sing N N 335 
SER OXT HXT  sing N N 336 
THR N   CA   sing N N 337 
THR N   H    sing N N 338 
THR N   H2   sing N N 339 
THR CA  C    sing N N 340 
THR CA  CB   sing N N 341 
THR CA  HA   sing N N 342 
THR C   O    doub N N 343 
THR C   OXT  sing N N 344 
THR CB  OG1  sing N N 345 
THR CB  CG2  sing N N 346 
THR CB  HB   sing N N 347 
THR OG1 HG1  sing N N 348 
THR CG2 HG21 sing N N 349 
THR CG2 HG22 sing N N 350 
THR CG2 HG23 sing N N 351 
THR OXT HXT  sing N N 352 
TRP N   CA   sing N N 353 
TRP N   H    sing N N 354 
TRP N   H2   sing N N 355 
TRP CA  C    sing N N 356 
TRP CA  CB   sing N N 357 
TRP CA  HA   sing N N 358 
TRP C   O    doub N N 359 
TRP C   OXT  sing N N 360 
TRP CB  CG   sing N N 361 
TRP CB  HB2  sing N N 362 
TRP CB  HB3  sing N N 363 
TRP CG  CD1  doub Y N 364 
TRP CG  CD2  sing Y N 365 
TRP CD1 NE1  sing Y N 366 
TRP CD1 HD1  sing N N 367 
TRP CD2 CE2  doub Y N 368 
TRP CD2 CE3  sing Y N 369 
TRP NE1 CE2  sing Y N 370 
TRP NE1 HE1  sing N N 371 
TRP CE2 CZ2  sing Y N 372 
TRP CE3 CZ3  doub Y N 373 
TRP CE3 HE3  sing N N 374 
TRP CZ2 CH2  doub Y N 375 
TRP CZ2 HZ2  sing N N 376 
TRP CZ3 CH2  sing Y N 377 
TRP CZ3 HZ3  sing N N 378 
TRP CH2 HH2  sing N N 379 
TRP OXT HXT  sing N N 380 
TYR N   CA   sing N N 381 
TYR N   H    sing N N 382 
TYR N   H2   sing N N 383 
TYR CA  C    sing N N 384 
TYR CA  CB   sing N N 385 
TYR CA  HA   sing N N 386 
TYR C   O    doub N N 387 
TYR C   OXT  sing N N 388 
TYR CB  CG   sing N N 389 
TYR CB  HB2  sing N N 390 
TYR CB  HB3  sing N N 391 
TYR CG  CD1  doub Y N 392 
TYR CG  CD2  sing Y N 393 
TYR CD1 CE1  sing Y N 394 
TYR CD1 HD1  sing N N 395 
TYR CD2 CE2  doub Y N 396 
TYR CD2 HD2  sing N N 397 
TYR CE1 CZ   doub Y N 398 
TYR CE1 HE1  sing N N 399 
TYR CE2 CZ   sing Y N 400 
TYR CE2 HE2  sing N N 401 
TYR CZ  OH   sing N N 402 
TYR OH  HH   sing N N 403 
TYR OXT HXT  sing N N 404 
VAL N   CA   sing N N 405 
VAL N   H    sing N N 406 
VAL N   H2   sing N N 407 
VAL CA  C    sing N N 408 
VAL CA  CB   sing N N 409 
VAL CA  HA   sing N N 410 
VAL C   O    doub N N 411 
VAL C   OXT  sing N N 412 
VAL CB  CG1  sing N N 413 
VAL CB  CG2  sing N N 414 
VAL CB  HB   sing N N 415 
VAL CG1 HG11 sing N N 416 
VAL CG1 HG12 sing N N 417 
VAL CG1 HG13 sing N N 418 
VAL CG2 HG21 sing N N 419 
VAL CG2 HG22 sing N N 420 
VAL CG2 HG23 sing N N 421 
VAL OXT HXT  sing N N 422 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                      ZN  
3 'DIMETHYL SULFOXIDE'                                                            DMS 
4 '5-{[(5-bromo-1H-benzimidazol-2-yl)sulfanyl]acetyl}-2-chlorobenzenesulfonamide' E38 
5 water                                                                           HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HLJ 
_pdbx_initial_refinement_model.details          'PDB entry 3HLJ' 
# 
