data_4LHI
# 
_entry.id   4LHI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.381 
_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   4LHI         pdb_00004lhi 10.2210/pdb4lhi/pdb 
RCSB  RCSB080636   ?            ?                   
WWPDB D_1000080636 ?            ?                   
# 
_pdbx_database_status.entry_id                        4LHI 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2013-07-01 
_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.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Crystal structure of human carbonic anhydrase isozyme II with 5-(phenylsulfonyl)thiophene-2-sulfonamide' 
_citation.journal_abbrev            'To be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnov, A.'  1 ? 
primary 'Manakova, E.' 2 ? 
primary 'Grazulis, S.' 3 ? 
primary 'Matulis, D.'  4 ? 
# 
_cell.entry_id           4LHI 
_cell.length_a           41.957 
_cell.length_b           41.227 
_cell.length_c           71.278 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.250 
_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                         4LHI 
_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-(phenylsulfonyl)thiophene-2-sulfonamide' 303.378   1   ?       ? ? ? 
5 water       nat water                                       18.015    233 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     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              4LHI 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                     ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                    ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                  ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                             ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                    ? 'C3 H7 N O2 S'   121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                        ? 'C2 H6 O S'      78.133  
GLN 'L-peptide linking' y GLUTAMINE                                   ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                             ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                     ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                   ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                       ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                  ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                     ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                      ? 'C6 H15 N2 O2 1' 147.195 
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 
WWL non-polymer         . '5-(phenylsulfonyl)thiophene-2-sulfonamide' ? 'C10 H9 N O4 S3' 303.378 
ZN  non-polymer         . 'ZINC ION'                                  ? 'Zn 2'           65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4LHI 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   40.0 
_exptl_crystal.density_Matthews      2.1 
_exptl_crystal.pdbx_mosaicity        0.80 
_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              8 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
'0.1M sodium BICINE (pH 9), 2M sodium malonate (pH 7), VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS IV++' 
_diffrn_detector.pdbx_collection_date   2013-03-07 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'VARIMAX-HF MIRROR' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
# 
_reflns.entry_id                     4LHI 
_reflns.d_resolution_high            1.600 
_reflns.d_resolution_low             22.561 
_reflns.number_all                   ? 
_reflns.number_obs                   30936 
_reflns.pdbx_netI_over_sigmaI        13.900 
_reflns.pdbx_Rsym_value              0.052 
_reflns.pdbx_redundancy              5.700 
_reflns.percent_possible_obs         98.500 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            0.052 
_reflns.B_iso_Wilson_estimate        22.456 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.60 1.69  ? 21036 ? ? 0.391 1.4  0.391 ? 5.00 ? 2.00  ? 4244 ? ? 0.516 ? 93.30  0.52 0.23 1  1 
1.69 1.79  ? 23379 ? ? 0.293 2.0  0.293 ? 5.50 ? 3.90  ? 4227 ? ? 0.359 ? 98.10  0.36 0.15 2  1 
1.79 1.91  ? 22478 ? ? 0.178 3.3  0.178 ? 5.60 ? 7.10  ? 3980 ? ? 0.203 ? 98.70  0.20 0.08 3  1 
1.91 2.07  ? 21563 ? ? 0.102 5.7  0.102 ? 5.80 ? 11.60 ? 3749 ? ? 0.116 ? 99.70  0.12 0.05 4  1 
2.07 2.26  ? 20249 ? ? 0.073 8.2  0.073 ? 5.80 ? 15.80 ? 3489 ? ? 0.084 ? 99.90  0.08 0.03 5  1 
2.26 2.53  ? 18600 ? ? 0.059 10.6 0.059 ? 5.90 ? 18.90 ? 3163 ? ? 0.068 ? 100.00 0.07 0.03 6  1 
2.53 2.92  ? 16635 ? ? 0.048 12.9 0.048 ? 5.90 ? 22.50 ? 2807 ? ? 0.055 ? 100.00 0.05 0.02 7  1 
2.92 3.58  ? 14160 ? ? 0.043 14.0 0.043 ? 6.00 ? 27.80 ? 2373 ? ? 0.049 ? 100.00 0.05 0.02 8  1 
3.58 5.06  ? 11042 ? ? 0.032 19.0 0.032 ? 6.00 ? 31.50 ? 1855 ? ? 0.037 ? 100.00 0.04 0.01 9  1 
5.06 22.56 ? 5934  ? ? 0.034 15.8 0.034 ? 5.70 ? 29.20 ? 1049 ? ? 0.039 ? 98.90  0.04 0.02 10 1 
# 
_refine.entry_id                                 4LHI 
_refine.ls_d_res_high                            1.600 
_refine.ls_d_res_low                             22.560 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    98.340 
_refine.ls_number_reflns_obs                     30923 
_refine.ls_number_reflns_all                     30936 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES: REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          0.189 
_refine.ls_R_factor_obs                          0.189 
_refine.ls_R_factor_R_work                       0.185 
_refine.ls_wR_factor_R_work                      0.189 
_refine.ls_R_factor_R_free                       0.225 
_refine.ls_wR_factor_R_free                      0.232 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  3105 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.562 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.010 
_refine.aniso_B[2][2]                            -0.640 
_refine.aniso_B[3][3]                            0.640 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.030 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.overall_SU_R_Cruickshank_DPI             0.114 
_refine.overall_SU_R_free                        0.111 
_refine.pdbx_overall_ESU_R                       0.114 
_refine.pdbx_overall_ESU_R_Free                  0.111 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.845 
_refine.B_iso_max                                68.37 
_refine.B_iso_min                                8.69 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      3HLJ 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_refine_hist.number_atoms_solvent             233 
_refine_hist.number_atoms_total               2309 
_refine_hist.d_res_high                       1.600 
_refine_hist.d_res_low                        22.560 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       2290 0.021  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3132 2.158  1.960  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 287  6.974  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 105  36.689 24.762 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 383  15.179 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 8    14.814 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         324  0.159  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1795 0.012  0.021  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.600 
_refine_ls_shell.d_res_low                        1.641 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               89.800 
_refine_ls_shell.number_reflns_R_work             1855 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.765 
_refine_ls_shell.R_factor_R_free                  0.776 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             215 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                2070 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  4LHI 
_struct.title                     
'Crystal structure of human carbonic anhydrase isozyme II with 5-(phenylsulfonyl)thiophene-2-sulfonamide' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4LHI 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, LYASE-LYASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.986 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E WWL . N4 ? ? A ZN  301 A WWL 304 1_555 ? ? ? ? ? ? ? 1.987 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -0.84 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 4.98  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O ILE A 91  ? O ILE A 91  N PHE A 70  ? N PHE A 70  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A DMS 302 ? 4  'BINDING SITE FOR RESIDUE DMS A 302' 
AC3 Software A DMS 303 ? 8  'BINDING SITE FOR RESIDUE DMS A 303' 
AC4 Software A WWL 304 ? 12 'BINDING SITE FOR RESIDUE WWL A 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  WWL E .   ? WWL A 304 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  HOH F .   ? HOH A 540 . ? 1_555 ? 
9  AC3 8  ASN A 62  ? ASN A 62  . ? 1_555 ? 
10 AC3 8  HIS A 64  ? HIS A 64  . ? 1_555 ? 
11 AC3 8  ASN A 67  ? ASN A 67  . ? 1_555 ? 
12 AC3 8  GLN A 92  ? GLN A 92  . ? 1_555 ? 
13 AC3 8  HIS A 94  ? HIS A 94  . ? 1_555 ? 
14 AC3 8  THR A 199 ? THR A 200 . ? 1_555 ? 
15 AC3 8  WWL E .   ? WWL A 304 . ? 1_555 ? 
16 AC3 8  HOH F .   ? HOH A 537 . ? 1_555 ? 
17 AC4 12 GLN A 92  ? GLN A 92  . ? 1_555 ? 
18 AC4 12 HIS A 94  ? HIS A 94  . ? 1_555 ? 
19 AC4 12 HIS A 96  ? HIS A 96  . ? 1_555 ? 
20 AC4 12 HIS A 119 ? HIS A 119 . ? 1_555 ? 
21 AC4 12 PHE A 130 ? PHE A 131 . ? 1_555 ? 
22 AC4 12 VAL A 142 ? VAL A 143 . ? 1_555 ? 
23 AC4 12 LEU A 197 ? LEU A 198 . ? 1_555 ? 
24 AC4 12 THR A 198 ? THR A 199 . ? 1_555 ? 
25 AC4 12 THR A 199 ? THR A 200 . ? 1_555 ? 
26 AC4 12 TRP A 208 ? TRP A 209 . ? 1_555 ? 
27 AC4 12 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
28 AC4 12 DMS D .   ? DMS A 303 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4LHI 
_atom_sites.fract_transf_matrix[1][1]   0.023834 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006053 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024256 
_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]   0.014475 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   A HIS A 1 4   ? 30.742 3.313   9.053   0.50 26.42 ? 4   HIS A N   1 
ATOM   2    N  N   B HIS A 1 4   ? 30.010 3.165   7.904   0.50 26.68 ? 4   HIS A N   1 
ATOM   3    C  CA  A HIS A 1 4   ? 31.452 2.021   9.059   0.50 24.75 ? 4   HIS A CA  1 
ATOM   4    C  CA  B HIS A 1 4   ? 30.671 1.851   8.067   0.50 26.35 ? 4   HIS A CA  1 
ATOM   5    C  C   A HIS A 1 4   ? 30.544 0.976   9.633   0.50 23.74 ? 4   HIS A C   1 
ATOM   6    C  C   B HIS A 1 4   ? 30.037 0.920   9.091   0.50 24.89 ? 4   HIS A C   1 
ATOM   7    O  O   A HIS A 1 4   ? 30.792 -0.211  9.499   0.50 23.16 ? 4   HIS A O   1 
ATOM   8    O  O   B HIS A 1 4   ? 30.095 -0.270  8.839   0.50 20.82 ? 4   HIS A O   1 
ATOM   9    C  CB  A HIS A 1 4   ? 32.759 2.115   9.867   0.50 27.01 ? 4   HIS A CB  1 
ATOM   10   C  CB  B HIS A 1 4   ? 32.203 1.931   8.259   0.50 26.79 ? 4   HIS A CB  1 
ATOM   11   C  CG  A HIS A 1 4   ? 33.793 1.105   9.477   0.50 26.21 ? 4   HIS A CG  1 
ATOM   12   C  CG  B HIS A 1 4   ? 33.013 2.042   6.961   0.50 31.67 ? 4   HIS A CG  1 
ATOM   13   N  ND1 A HIS A 1 4   ? 34.140 0.070   10.284  0.50 29.84 ? 4   HIS A ND1 1 
ATOM   14   N  ND1 B HIS A 1 4   ? 34.289 1.550   6.852   0.50 27.57 ? 4   HIS A ND1 1 
ATOM   15   C  CD2 A HIS A 1 4   ? 34.557 0.967   8.310   0.50 25.85 ? 4   HIS A CD2 1 
ATOM   16   C  CD2 B HIS A 1 4   ? 32.709 2.621   5.711   0.50 30.24 ? 4   HIS A CD2 1 
ATOM   17   C  CE1 A HIS A 1 4   ? 35.071 -0.689  9.675   0.50 24.80 ? 4   HIS A CE1 1 
ATOM   18   C  CE1 B HIS A 1 4   ? 34.759 1.786   5.613   0.50 27.64 ? 4   HIS A CE1 1 
ATOM   19   N  NE2 A HIS A 1 4   ? 35.349 -0.128  8.474   0.50 26.33 ? 4   HIS A NE2 1 
ATOM   20   N  NE2 B HIS A 1 4   ? 33.801 2.443   4.913   0.50 33.50 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 29.425 1.399   10.210  1.00 23.09 ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 28.684 0.477   11.116  1.00 19.46 ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 27.703 -0.340  10.347  1.00 19.33 ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 27.165 0.077   9.310   1.00 21.13 ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 28.055 1.215   12.325  1.00 20.52 ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 26.804 1.970   11.970  1.00 21.62 ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 26.656 3.318   11.624  1.00 22.14 ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 25.453 1.414   11.962  1.00 18.25 ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 25.350 3.601   11.380  1.00 22.28 ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 24.558 2.490   11.569  1.00 20.17 ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 24.924 0.150   12.233  1.00 19.04 ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 23.190 2.294   11.433  1.00 19.84 ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 23.537 -0.037  12.066  1.00 17.32 ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 22.701 1.027   11.725  1.00 18.94 ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 27.477 -1.566  10.834  1.00 19.23 ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 26.432 -2.429  10.236  1.00 18.18 ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 26.085 -3.557  11.202  1.00 17.58 ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 26.123 -3.422  12.417  1.00 16.40 ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 25.820 -4.731  10.640  1.00 18.62 ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 25.419 -5.852  11.489  1.00 20.48 ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 26.305 -7.123  11.387  1.00 25.75 ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 25.956 -8.169  11.974  1.00 27.30 ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 23.958 -6.230  11.251  1.00 17.58 ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 22.990 -5.174  11.767  1.00 14.37 ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 22.641 -5.186  13.128  1.00 14.84 ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 22.493 -4.202  10.912  1.00 13.79 ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 21.745 -4.193  13.633  1.00 13.81 ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 21.641 -3.188  11.386  1.00 13.91 ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 21.283 -3.227  12.750  1.00 14.19 ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? 20.338 -2.229  13.109  1.00 15.40 ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 27.419 -7.030  10.658  1.00 25.44 ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 28.352 -8.207  10.553  1.00 23.00 ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 29.407 -8.379  11.654  1.00 24.60 ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 29.493 -7.608  12.658  1.00 24.11 ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 30.282 -9.382  11.421  1.00 25.18 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 31.294 -9.828  12.383  1.00 26.46 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 32.258 -8.675  12.707  1.00 23.46 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 32.683 -8.522  13.868  1.00 27.45 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 32.109 -11.011 11.815  1.00 30.27 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 33.047 -11.621 12.846  1.00 40.23 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 34.231 -12.392 12.240  1.00 47.07 ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 35.157 -12.902 13.366  1.00 52.56 ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 36.420 -13.558 12.898  1.00 54.81 ? 9   LYS A NZ  1 
ATOM   64   N  N   . HIS A 1 10  ? 32.536 -7.888  11.680  1.00 25.92 ? 10  HIS A N   1 
ATOM   65   C  CA  . HIS A 1 10  ? 33.552 -6.860  11.811  1.00 27.00 ? 10  HIS A CA  1 
ATOM   66   C  C   . HIS A 1 10  ? 33.067 -5.471  12.052  1.00 28.44 ? 10  HIS A C   1 
ATOM   67   O  O   . HIS A 1 10  ? 33.882 -4.634  12.431  1.00 26.01 ? 10  HIS A O   1 
ATOM   68   C  CB  . HIS A 1 10  ? 34.515 -6.903  10.651  1.00 24.89 ? 10  HIS A CB  1 
ATOM   69   C  CG  . HIS A 1 10  ? 35.151 -8.268  10.476  1.00 25.10 ? 10  HIS A CG  1 
ATOM   70   N  ND1 . HIS A 1 10  ? 36.162 -8.703  11.281  1.00 30.00 ? 10  HIS A ND1 1 
ATOM   71   C  CD2 . HIS A 1 10  ? 34.883 -9.278  9.572   1.00 28.63 ? 10  HIS A CD2 1 
ATOM   72   C  CE1 . HIS A 1 10  ? 36.514 -9.949  10.900  1.00 29.34 ? 10  HIS A CE1 1 
ATOM   73   N  NE2 . HIS A 1 10  ? 35.710 -10.308 9.855   1.00 25.81 ? 10  HIS A NE2 1 
ATOM   74   N  N   . ASN A 1 11  ? 31.756 -5.217  11.900  1.00 24.78 ? 11  ASN A N   1 
ATOM   75   C  CA  . ASN A 1 11  ? 31.216 -3.860  12.114  1.00 24.58 ? 11  ASN A CA  1 
ATOM   76   C  C   . ASN A 1 11  ? 29.868 -3.856  12.864  1.00 23.93 ? 11  ASN A C   1 
ATOM   77   O  O   . ASN A 1 11  ? 29.137 -2.839  12.826  1.00 22.78 ? 11  ASN A O   1 
ATOM   78   C  CB  . ASN A 1 11  ? 30.995 -3.187  10.775  1.00 23.46 ? 11  ASN A CB  1 
ATOM   79   C  CG  . ASN A 1 11  ? 29.935 -3.879  9.938   1.00 25.45 ? 11  ASN A CG  1 
ATOM   80   O  OD1 . ASN A 1 11  ? 29.366 -4.896  10.357  1.00 26.23 ? 11  ASN A OD1 1 
ATOM   81   N  ND2 . ASN A 1 11  ? 29.680 -3.363  8.750   1.00 25.40 ? 11  ASN A ND2 1 
ATOM   82   N  N   . GLY A 1 12  ? 29.551 -4.993  13.486  1.00 24.19 ? 12  GLY A N   1 
ATOM   83   C  CA  . GLY A 1 12  ? 28.206 -5.247  14.051  1.00 21.29 ? 12  GLY A CA  1 
ATOM   84   C  C   . GLY A 1 12  ? 28.157 -4.671  15.439  1.00 20.63 ? 12  GLY A C   1 
ATOM   85   O  O   . GLY A 1 12  ? 29.085 -3.980  15.902  1.00 18.27 ? 12  GLY A O   1 
ATOM   86   N  N   . PRO A 1 13  ? 27.073 -4.978  16.196  1.00 20.10 ? 13  PRO A N   1 
ATOM   87   C  CA  . PRO A 1 13  ? 26.848 -4.426  17.536  1.00 20.55 ? 13  PRO A CA  1 
ATOM   88   C  C   . PRO A 1 13  ? 28.013 -4.448  18.534  1.00 21.31 ? 13  PRO A C   1 
ATOM   89   O  O   . PRO A 1 13  ? 28.163 -3.495  19.351  1.00 19.78 ? 13  PRO A O   1 
ATOM   90   C  CB  . PRO A 1 13  ? 25.715 -5.326  18.097  1.00 21.25 ? 13  PRO A CB  1 
ATOM   91   C  CG  . PRO A 1 13  ? 24.962 -5.698  16.866  1.00 19.24 ? 13  PRO A CG  1 
ATOM   92   C  CD  . PRO A 1 13  ? 25.936 -5.792  15.725  1.00 20.01 ? 13  PRO A CD  1 
ATOM   93   N  N   A GLU A 1 14  ? 28.824 -5.497  18.434  0.50 19.53 ? 14  GLU A N   1 
ATOM   94   N  N   B GLU A 1 14  ? 28.855 -5.492  18.536  0.50 20.22 ? 14  GLU A N   1 
ATOM   95   C  CA  A GLU A 1 14  ? 29.971 -5.653  19.295  0.50 19.74 ? 14  GLU A CA  1 
ATOM   96   C  CA  B GLU A 1 14  ? 29.975 -5.470  19.502  0.50 20.98 ? 14  GLU A CA  1 
ATOM   97   C  C   A GLU A 1 14  ? 31.056 -4.580  19.061  0.50 18.35 ? 14  GLU A C   1 
ATOM   98   C  C   B GLU A 1 14  ? 31.092 -4.495  19.095  0.50 19.19 ? 14  GLU A C   1 
ATOM   99   O  O   A GLU A 1 14  ? 31.876 -4.350  19.956  0.50 19.61 ? 14  GLU A O   1 
ATOM   100  O  O   B GLU A 1 14  ? 32.000 -4.260  19.884  0.50 21.66 ? 14  GLU A O   1 
ATOM   101  C  CB  A GLU A 1 14  ? 30.547 -7.045  19.083  0.50 20.92 ? 14  GLU A CB  1 
ATOM   102  C  CB  B GLU A 1 14  ? 30.575 -6.855  19.777  0.50 22.98 ? 14  GLU A CB  1 
ATOM   103  C  CG  A GLU A 1 14  ? 31.118 -7.217  17.702  0.50 20.02 ? 14  GLU A CG  1 
ATOM   104  C  CG  B GLU A 1 14  ? 29.568 -7.998  19.804  0.50 24.59 ? 14  GLU A CG  1 
ATOM   105  C  CD  A GLU A 1 14  ? 30.265 -7.970  16.711  0.50 20.95 ? 14  GLU A CD  1 
ATOM   106  C  CD  B GLU A 1 14  ? 28.591 -7.858  20.947  0.50 28.34 ? 14  GLU A CD  1 
ATOM   107  O  OE1 A GLU A 1 14  ? 29.035 -7.629  16.603  0.50 15.52 ? 14  GLU A OE1 1 
ATOM   108  O  OE1 B GLU A 1 14  ? 29.050 -7.673  22.088  0.50 29.90 ? 14  GLU A OE1 1 
ATOM   109  O  OE2 A GLU A 1 14  ? 30.914 -8.859  16.022  0.50 17.53 ? 14  GLU A OE2 1 
ATOM   110  O  OE2 B GLU A 1 14  ? 27.358 -7.935  20.706  0.50 31.68 ? 14  GLU A OE2 1 
ATOM   111  N  N   . HIS A 1 15  ? 31.005 -3.923  17.897  1.00 18.57 ? 15  HIS A N   1 
ATOM   112  C  CA  . HIS A 1 15  ? 31.988 -2.946  17.449  1.00 17.42 ? 15  HIS A CA  1 
ATOM   113  C  C   . HIS A 1 15  ? 31.540 -1.514  17.628  1.00 20.28 ? 15  HIS A C   1 
ATOM   114  O  O   . HIS A 1 15  ? 32.373 -0.578  17.577  1.00 18.05 ? 15  HIS A O   1 
ATOM   115  C  CB  . HIS A 1 15  ? 32.268 -3.138  15.978  1.00 18.36 ? 15  HIS A CB  1 
ATOM   116  C  CG  . HIS A 1 15  ? 33.053 -4.399  15.714  1.00 22.45 ? 15  HIS A CG  1 
ATOM   117  N  ND1 . HIS A 1 15  ? 34.398 -4.425  15.779  1.00 24.84 ? 15  HIS A ND1 1 
ATOM   118  C  CD2 . HIS A 1 15  ? 32.645 -5.691  15.387  1.00 23.97 ? 15  HIS A CD2 1 
ATOM   119  C  CE1 . HIS A 1 15  ? 34.846 -5.684  15.530  1.00 25.85 ? 15  HIS A CE1 1 
ATOM   120  N  NE2 . HIS A 1 15  ? 33.791 -6.468  15.310  1.00 23.24 ? 15  HIS A NE2 1 
ATOM   121  N  N   . TRP A 1 16  ? 30.242 -1.313  17.832  1.00 18.32 ? 16  TRP A N   1 
ATOM   122  C  CA  . TRP A 1 16  ? 29.712 0.041   17.808  1.00 17.90 ? 16  TRP A CA  1 
ATOM   123  C  C   . TRP A 1 16  ? 30.266 1.005   18.788  1.00 15.84 ? 16  TRP A C   1 
ATOM   124  O  O   . TRP A 1 16  ? 30.301 2.190   18.425  1.00 19.48 ? 16  TRP A O   1 
ATOM   125  C  CB  . TRP A 1 16  ? 28.148 0.010   17.930  1.00 15.24 ? 16  TRP A CB  1 
ATOM   126  C  CG  . TRP A 1 16  ? 27.497 -0.668  16.761  1.00 16.25 ? 16  TRP A CG  1 
ATOM   127  C  CD1 . TRP A 1 16  ? 28.038 -1.085  15.533  1.00 15.66 ? 16  TRP A CD1 1 
ATOM   128  C  CD2 . TRP A 1 16  ? 26.081 -1.029  16.707  1.00 15.66 ? 16  TRP A CD2 1 
ATOM   129  N  NE1 . TRP A 1 16  ? 27.083 -1.681  14.756  1.00 16.41 ? 16  TRP A NE1 1 
ATOM   130  C  CE2 . TRP A 1 16  ? 25.868 -1.651  15.409  1.00 15.50 ? 16  TRP A CE2 1 
ATOM   131  C  CE3 . TRP A 1 16  ? 25.027 -0.873  17.579  1.00 16.58 ? 16  TRP A CE3 1 
ATOM   132  C  CZ2 . TRP A 1 16  ? 24.630 -2.131  15.023  1.00 15.54 ? 16  TRP A CZ2 1 
ATOM   133  C  CZ3 . TRP A 1 16  ? 23.782 -1.376  17.200  1.00 15.91 ? 16  TRP A CZ3 1 
ATOM   134  C  CH2 . TRP A 1 16  ? 23.581 -1.942  15.943  1.00 16.54 ? 16  TRP A CH2 1 
ATOM   135  N  N   . HIS A 1 17  ? 30.712 0.546   19.949  1.00 15.74 ? 17  HIS A N   1 
ATOM   136  C  CA  . HIS A 1 17  ? 31.202 1.389   21.028  1.00 16.86 ? 17  HIS A CA  1 
ATOM   137  C  C   . HIS A 1 17  ? 32.402 2.208   20.615  1.00 17.06 ? 17  HIS A C   1 
ATOM   138  O  O   . HIS A 1 17  ? 32.628 3.265   21.235  1.00 17.58 ? 17  HIS A O   1 
ATOM   139  C  CB  . HIS A 1 17  ? 31.481 0.643   22.332  1.00 16.60 ? 17  HIS A CB  1 
ATOM   140  C  CG  . HIS A 1 17  ? 32.678 -0.263  22.246  1.00 19.70 ? 17  HIS A CG  1 
ATOM   141  N  ND1 . HIS A 1 17  ? 33.884 0.058   22.789  1.00 23.22 ? 17  HIS A ND1 1 
ATOM   142  C  CD2 . HIS A 1 17  ? 32.855 -1.417  21.534  1.00 19.57 ? 17  HIS A CD2 1 
ATOM   143  C  CE1 . HIS A 1 17  ? 34.766 -0.895  22.457  1.00 20.14 ? 17  HIS A CE1 1 
ATOM   144  N  NE2 . HIS A 1 17  ? 34.140 -1.797  21.697  1.00 23.39 ? 17  HIS A NE2 1 
ATOM   145  N  N   A LYS A 1 18  ? 33.160 1.737   19.595  0.50 16.48 ? 18  LYS A N   1 
ATOM   146  N  N   B LYS A 1 18  ? 33.176 1.755   19.643  0.50 17.45 ? 18  LYS A N   1 
ATOM   147  C  CA  A LYS A 1 18  ? 34.413 2.404   19.119  0.50 16.77 ? 18  LYS A CA  1 
ATOM   148  C  CA  B LYS A 1 18  ? 34.362 2.524   19.355  0.50 17.74 ? 18  LYS A CA  1 
ATOM   149  C  C   A LYS A 1 18  ? 34.164 3.719   18.363  0.50 18.37 ? 18  LYS A C   1 
ATOM   150  C  C   B LYS A 1 18  ? 33.952 3.869   18.708  0.50 19.29 ? 18  LYS A C   1 
ATOM   151  O  O   A LYS A 1 18  ? 34.993 4.603   18.333  0.50 20.72 ? 18  LYS A O   1 
ATOM   152  O  O   B LYS A 1 18  ? 34.429 4.936   19.173  0.50 17.78 ? 18  LYS A O   1 
ATOM   153  C  CB  A LYS A 1 18  ? 35.196 1.486   18.178  0.50 15.56 ? 18  LYS A CB  1 
ATOM   154  C  CB  B LYS A 1 18  ? 35.321 1.658   18.561  0.50 18.35 ? 18  LYS A CB  1 
ATOM   155  C  CG  A LYS A 1 18  ? 36.058 0.424   18.846  0.50 15.89 ? 18  LYS A CG  1 
ATOM   156  C  CG  B LYS A 1 18  ? 35.433 0.288   19.246  0.50 20.33 ? 18  LYS A CG  1 
ATOM   157  C  CD  A LYS A 1 18  ? 36.634 -0.494  17.803  0.50 14.07 ? 18  LYS A CD  1 
ATOM   158  C  CD  B LYS A 1 18  ? 36.625 -0.518  18.786  0.50 19.38 ? 18  LYS A CD  1 
ATOM   159  C  CE  A LYS A 1 18  ? 35.777 -1.727  17.513  0.50 13.99 ? 18  LYS A CE  1 
ATOM   160  C  CE  B LYS A 1 18  ? 36.600 -0.704  17.280  0.50 21.69 ? 18  LYS A CE  1 
ATOM   161  N  NZ  A LYS A 1 18  ? 36.228 -2.343  16.206  0.50 11.27 ? 18  LYS A NZ  1 
ATOM   162  N  NZ  B LYS A 1 18  ? 35.981 -1.979  16.809  0.50 23.36 ? 18  LYS A NZ  1 
ATOM   163  N  N   . ASP A 1 19  ? 33.008 3.842   17.751  1.00 19.64 ? 19  ASP A N   1 
ATOM   164  C  CA  . ASP A 1 19  ? 32.587 5.094   17.107  1.00 21.51 ? 19  ASP A CA  1 
ATOM   165  C  C   . ASP A 1 19  ? 31.562 5.847   17.970  1.00 24.13 ? 19  ASP A C   1 
ATOM   166  O  O   . ASP A 1 19  ? 31.480 7.076   17.902  1.00 23.35 ? 19  ASP A O   1 
ATOM   167  C  CB  . ASP A 1 19  ? 32.053 4.840   15.704  1.00 26.23 ? 19  ASP A CB  1 
ATOM   168  C  CG  . ASP A 1 19  ? 33.105 4.950   14.621  1.00 30.09 ? 19  ASP A CG  1 
ATOM   169  O  OD1 . ASP A 1 19  ? 34.176 5.489   14.868  1.00 35.67 ? 19  ASP A OD1 1 
ATOM   170  O  OD2 . ASP A 1 19  ? 32.847 4.501   13.491  1.00 40.74 ? 19  ASP A OD2 1 
ATOM   171  N  N   . PHE A 1 20  ? 30.806 5.105   18.808  1.00 19.63 ? 20  PHE A N   1 
ATOM   172  C  CA  . PHE A 1 20  ? 29.678 5.612   19.617  1.00 19.35 ? 20  PHE A CA  1 
ATOM   173  C  C   . PHE A 1 20  ? 29.818 5.071   20.977  1.00 20.21 ? 20  PHE A C   1 
ATOM   174  O  O   . PHE A 1 20  ? 29.212 4.061   21.303  1.00 16.65 ? 20  PHE A O   1 
ATOM   175  C  CB  . PHE A 1 20  ? 28.324 5.189   18.957  1.00 20.74 ? 20  PHE A CB  1 
ATOM   176  C  CG  . PHE A 1 20  ? 28.254 5.574   17.518  1.00 19.16 ? 20  PHE A CG  1 
ATOM   177  C  CD1 . PHE A 1 20  ? 27.859 6.858   17.174  1.00 20.43 ? 20  PHE A CD1 1 
ATOM   178  C  CD2 . PHE A 1 20  ? 28.638 4.672   16.493  1.00 20.14 ? 20  PHE A CD2 1 
ATOM   179  C  CE1 . PHE A 1 20  ? 27.817 7.208   15.856  1.00 19.37 ? 20  PHE A CE1 1 
ATOM   180  C  CE2 . PHE A 1 20  ? 28.625 5.027   15.180  1.00 20.36 ? 20  PHE A CE2 1 
ATOM   181  C  CZ  . PHE A 1 20  ? 28.207 6.320   14.847  1.00 22.12 ? 20  PHE A CZ  1 
ATOM   182  N  N   . PRO A 1 21  ? 30.695 5.692   21.809  1.00 19.85 ? 21  PRO A N   1 
ATOM   183  C  CA  . PRO A 1 21  ? 30.955 5.177   23.136  1.00 19.34 ? 21  PRO A CA  1 
ATOM   184  C  C   . PRO A 1 21  ? 29.738 5.049   24.097  1.00 19.40 ? 21  PRO A C   1 
ATOM   185  O  O   . PRO A 1 21  ? 29.791 4.262   25.062  1.00 19.60 ? 21  PRO A O   1 
ATOM   186  C  CB  . PRO A 1 21  ? 32.158 6.042   23.666  1.00 22.17 ? 21  PRO A CB  1 
ATOM   187  C  CG  . PRO A 1 21  ? 32.184 7.200   22.738  1.00 24.37 ? 21  PRO A CG  1 
ATOM   188  C  CD  . PRO A 1 21  ? 31.617 6.775   21.419  1.00 21.08 ? 21  PRO A CD  1 
ATOM   189  N  N   A ILE A 1 22  ? 28.678 5.776   23.736  0.50 18.77 ? 22  ILE A N   1 
ATOM   190  N  N   B ILE A 1 22  ? 28.624 5.769   23.865  0.50 18.97 ? 22  ILE A N   1 
ATOM   191  C  CA  A ILE A 1 22  ? 27.415 5.756   24.412  0.50 17.59 ? 22  ILE A CA  1 
ATOM   192  C  CA  B ILE A 1 22  ? 27.415 5.629   24.715  0.50 18.52 ? 22  ILE A CA  1 
ATOM   193  C  C   A ILE A 1 22  ? 26.832 4.346   24.367  0.50 17.54 ? 22  ILE A C   1 
ATOM   194  C  C   B ILE A 1 22  ? 26.803 4.260   24.432  0.50 17.89 ? 22  ILE A C   1 
ATOM   195  O  O   A ILE A 1 22  ? 26.003 4.003   25.197  0.50 18.29 ? 22  ILE A O   1 
ATOM   196  O  O   B ILE A 1 22  ? 25.861 3.870   25.119  0.50 19.00 ? 22  ILE A O   1 
ATOM   197  C  CB  A ILE A 1 22  ? 26.452 6.833   23.839  0.50 14.97 ? 22  ILE A CB  1 
ATOM   198  C  CB  B ILE A 1 22  ? 26.345 6.749   24.487  0.50 16.66 ? 22  ILE A CB  1 
ATOM   199  C  CG1 A ILE A 1 22  ? 25.427 7.225   24.899  0.50 12.77 ? 22  ILE A CG1 1 
ATOM   200  C  CG1 B ILE A 1 22  ? 25.308 6.799   25.630  0.50 15.77 ? 22  ILE A CG1 1 
ATOM   201  C  CG2 A ILE A 1 22  ? 25.884 6.425   22.478  0.50 13.95 ? 22  ILE A CG2 1 
ATOM   202  C  CG2 B ILE A 1 22  ? 25.675 6.591   23.142  0.50 16.36 ? 22  ILE A CG2 1 
ATOM   203  C  CD1 A ILE A 1 22  ? 24.425 8.253   24.491  0.50 13.45 ? 22  ILE A CD1 1 
ATOM   204  C  CD1 B ILE A 1 22  ? 25.604 7.771   26.718  0.50 14.91 ? 22  ILE A CD1 1 
ATOM   205  N  N   . ALA A 1 23  ? 27.338 3.534   23.433  1.00 16.20 ? 23  ALA A N   1 
ATOM   206  C  CA  . ALA A 1 23  ? 26.935 2.070   23.318  1.00 18.54 ? 23  ALA A CA  1 
ATOM   207  C  C   . ALA A 1 23  ? 27.012 1.359   24.686  1.00 19.31 ? 23  ALA A C   1 
ATOM   208  O  O   . ALA A 1 23  ? 26.310 0.350   24.930  1.00 16.99 ? 23  ALA A O   1 
ATOM   209  C  CB  . ALA A 1 23  ? 27.708 1.259   22.253  1.00 18.18 ? 23  ALA A CB  1 
ATOM   210  N  N   . LYS A 1 24  ? 27.862 1.842   25.612  1.00 20.03 ? 24  LYS A N   1 
ATOM   211  C  CA  . LYS A 1 24  ? 28.089 1.176   26.890  1.00 20.65 ? 24  LYS A CA  1 
ATOM   212  C  C   . LYS A 1 24  ? 27.492 2.073   27.972  1.00 23.23 ? 24  LYS A C   1 
ATOM   213  O  O   . LYS A 1 24  ? 27.882 1.982   29.145  1.00 23.34 ? 24  LYS A O   1 
ATOM   214  C  CB  . LYS A 1 24  ? 29.612 1.042   27.149  1.00 23.23 ? 24  LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 24  ? 30.266 -0.001  26.263  1.00 22.60 ? 24  LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 24  ? 31.732 -0.170  26.660  1.00 24.38 ? 24  LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 24  ? 32.460 -1.015  25.635  1.00 25.89 ? 24  LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 24  ? 32.151 -2.426  25.993  1.00 32.33 ? 24  LYS A NZ  1 
ATOM   219  N  N   . GLY A 1 25  ? 26.533 2.919   27.566  1.00 20.39 ? 25  GLY A N   1 
ATOM   220  C  CA  . GLY A 1 25  ? 25.847 3.820   28.517  1.00 19.80 ? 25  GLY A CA  1 
ATOM   221  C  C   . GLY A 1 25  ? 24.899 3.217   29.508  1.00 19.62 ? 25  GLY A C   1 
ATOM   222  O  O   . GLY A 1 25  ? 24.734 1.982   29.646  1.00 21.08 ? 25  GLY A O   1 
ATOM   223  N  N   . GLU A 1 26  ? 24.242 4.133   30.221  1.00 19.15 ? 26  GLU A N   1 
ATOM   224  C  CA  . GLU A 1 26  ? 23.439 3.777   31.323  1.00 20.89 ? 26  GLU A CA  1 
ATOM   225  C  C   . GLU A 1 26  ? 21.985 3.490   30.959  1.00 15.54 ? 26  GLU A C   1 
ATOM   226  O  O   . GLU A 1 26  ? 21.247 2.906   31.733  1.00 16.50 ? 26  GLU A O   1 
ATOM   227  C  CB  . GLU A 1 26  ? 23.467 4.944   32.380  1.00 25.11 ? 26  GLU A CB  1 
ATOM   228  C  CG  . GLU A 1 26  ? 24.744 5.041   33.254  1.00 34.98 ? 26  GLU A CG  1 
ATOM   229  C  CD  . GLU A 1 26  ? 25.454 3.689   33.598  1.00 38.77 ? 26  GLU A CD  1 
ATOM   230  O  OE1 . GLU A 1 26  ? 24.944 2.863   34.428  1.00 43.63 ? 26  GLU A OE1 1 
ATOM   231  O  OE2 . GLU A 1 26  ? 26.571 3.457   33.038  1.00 41.73 ? 26  GLU A OE2 1 
ATOM   232  N  N   . ARG A 1 27  ? 21.567 3.887   29.761  1.00 15.03 ? 27  ARG A N   1 
ATOM   233  C  CA  . ARG A 1 27  ? 20.189 3.599   29.376  1.00 13.94 ? 27  ARG A CA  1 
ATOM   234  C  C   . ARG A 1 27  ? 20.122 3.092   27.911  1.00 13.20 ? 27  ARG A C   1 
ATOM   235  O  O   . ARG A 1 27  ? 19.455 3.676   27.035  1.00 13.97 ? 27  ARG A O   1 
ATOM   236  C  CB  . ARG A 1 27  ? 19.282 4.824   29.630  1.00 15.32 ? 27  ARG A CB  1 
ATOM   237  C  CG  . ARG A 1 27  ? 19.765 6.132   28.978  1.00 22.90 ? 27  ARG A CG  1 
ATOM   238  C  CD  . ARG A 1 27  ? 18.857 7.417   29.164  1.00 28.04 ? 27  ARG A CD  1 
ATOM   239  N  NE  . ARG A 1 27  ? 17.601 7.249   28.435  1.00 26.77 ? 27  ARG A NE  1 
ATOM   240  C  CZ  . ARG A 1 27  ? 16.737 8.226   28.179  1.00 24.78 ? 27  ARG A CZ  1 
ATOM   241  N  NH1 . ARG A 1 27  ? 16.982 9.460   28.595  1.00 16.38 ? 27  ARG A NH1 1 
ATOM   242  N  NH2 . ARG A 1 27  ? 15.624 7.965   27.507  1.00 20.05 ? 27  ARG A NH2 1 
ATOM   243  N  N   . GLN A 1 28  ? 20.825 1.997   27.628  1.00 13.67 ? 28  GLN A N   1 
ATOM   244  C  CA  . GLN A 1 28  ? 20.860 1.526   26.240  1.00 11.15 ? 28  GLN A CA  1 
ATOM   245  C  C   . GLN A 1 28  ? 19.711 0.504   25.960  1.00 10.96 ? 28  GLN A C   1 
ATOM   246  O  O   . GLN A 1 28  ? 19.211 -0.176  26.853  1.00 13.32 ? 28  GLN A O   1 
ATOM   247  C  CB  . GLN A 1 28  ? 22.201 0.820   25.993  1.00 13.08 ? 28  GLN A CB  1 
ATOM   248  C  CG  . GLN A 1 28  ? 23.309 1.857   25.843  1.00 12.23 ? 28  GLN A CG  1 
ATOM   249  C  CD  . GLN A 1 28  ? 23.169 2.607   24.533  1.00 13.85 ? 28  GLN A CD  1 
ATOM   250  O  OE1 . GLN A 1 28  ? 23.364 2.058   23.478  1.00 14.75 ? 28  GLN A OE1 1 
ATOM   251  N  NE2 . GLN A 1 28  ? 22.868 3.907   24.605  1.00 14.74 ? 28  GLN A NE2 1 
ATOM   252  N  N   . SER A 1 29  ? 19.330 0.438   24.679  1.00 11.92 ? 29  SER A N   1 
ATOM   253  C  CA  . SER A 1 29  ? 18.240 -0.463  24.192  1.00 10.60 ? 29  SER A CA  1 
ATOM   254  C  C   . SER A 1 29  ? 18.777 -1.319  23.079  1.00 11.15 ? 29  SER A C   1 
ATOM   255  O  O   . SER A 1 29  ? 19.719 -0.937  22.374  1.00 13.62 ? 29  SER A O   1 
ATOM   256  C  CB  . SER A 1 29  ? 17.057 0.375   23.653  1.00 10.51 ? 29  SER A CB  1 
ATOM   257  O  OG  . SER A 1 29  ? 16.555 1.101   24.784  1.00 11.38 ? 29  SER A OG  1 
ATOM   258  N  N   . PRO A 1 30  ? 18.121 -2.440  22.856  1.00 10.84 ? 30  PRO A N   1 
ATOM   259  C  CA  . PRO A 1 30  ? 16.949 -2.969  23.560  1.00 11.84 ? 30  PRO A CA  1 
ATOM   260  C  C   . PRO A 1 30  ? 17.342 -3.677  24.858  1.00 12.42 ? 30  PRO A C   1 
ATOM   261  O  O   . PRO A 1 30  ? 18.558 -3.732  25.168  1.00 12.31 ? 30  PRO A O   1 
ATOM   262  C  CB  . PRO A 1 30  ? 16.405 -3.939  22.524  1.00 10.46 ? 30  PRO A CB  1 
ATOM   263  C  CG  . PRO A 1 30  ? 17.696 -4.579  21.907  1.00 10.62 ? 30  PRO A CG  1 
ATOM   264  C  CD  . PRO A 1 30  ? 18.623 -3.377  21.816  1.00 10.90 ? 30  PRO A CD  1 
ATOM   265  N  N   . VAL A 1 31  ? 16.348 -4.225  25.562  1.00 12.45 ? 31  VAL A N   1 
ATOM   266  C  CA  . VAL A 1 31  ? 16.608 -5.000  26.769  1.00 11.37 ? 31  VAL A CA  1 
ATOM   267  C  C   . VAL A 1 31  ? 15.678 -6.210  26.748  1.00 12.96 ? 31  VAL A C   1 
ATOM   268  O  O   . VAL A 1 31  ? 14.663 -6.270  26.012  1.00 11.64 ? 31  VAL A O   1 
ATOM   269  C  CB  . VAL A 1 31  ? 16.317 -4.154  28.061  1.00 13.02 ? 31  VAL A CB  1 
ATOM   270  C  CG1 . VAL A 1 31  ? 17.254 -2.943  28.197  1.00 13.73 ? 31  VAL A CG1 1 
ATOM   271  C  CG2 . VAL A 1 31  ? 14.841 -3.696  28.125  1.00 12.33 ? 31  VAL A CG2 1 
ATOM   272  N  N   . ASP A 1 32  ? 16.002 -7.196  27.609  1.00 12.92 ? 32  ASP A N   1 
ATOM   273  C  CA  . ASP A 1 32  ? 15.087 -8.250  27.872  1.00 12.56 ? 32  ASP A CA  1 
ATOM   274  C  C   . ASP A 1 32  ? 13.986 -7.710  28.817  1.00 14.02 ? 32  ASP A C   1 
ATOM   275  O  O   . ASP A 1 32  ? 14.279 -7.075  29.846  1.00 14.73 ? 32  ASP A O   1 
ATOM   276  C  CB  . ASP A 1 32  ? 15.802 -9.437  28.535  1.00 15.15 ? 32  ASP A CB  1 
ATOM   277  C  CG  . ASP A 1 32  ? 14.811 -10.582 28.823  1.00 15.56 ? 32  ASP A CG  1 
ATOM   278  O  OD1 . ASP A 1 32  ? 14.163 -11.059 27.837  1.00 15.15 ? 32  ASP A OD1 1 
ATOM   279  O  OD2 . ASP A 1 32  ? 14.737 -11.064 30.004  1.00 18.42 ? 32  ASP A OD2 1 
ATOM   280  N  N   . ILE A 1 33  ? 12.751 -8.011  28.493  1.00 13.12 ? 33  ILE A N   1 
ATOM   281  C  CA  . ILE A 1 33  ? 11.683 -7.659  29.362  1.00 13.15 ? 33  ILE A CA  1 
ATOM   282  C  C   . ILE A 1 33  ? 11.336 -8.829  30.258  1.00 14.10 ? 33  ILE A C   1 
ATOM   283  O  O   . ILE A 1 33  ? 10.734 -9.764  29.817  1.00 14.54 ? 33  ILE A O   1 
ATOM   284  C  CB  . ILE A 1 33  ? 10.452 -7.180  28.582  1.00 12.70 ? 33  ILE A CB  1 
ATOM   285  C  CG1 . ILE A 1 33  ? 10.801 -5.919  27.816  1.00 10.66 ? 33  ILE A CG1 1 
ATOM   286  C  CG2 . ILE A 1 33  ? 9.301  -6.897  29.520  1.00 11.89 ? 33  ILE A CG2 1 
ATOM   287  C  CD1 . ILE A 1 33  ? 9.852  -5.599  26.721  1.00 8.93  ? 33  ILE A CD1 1 
ATOM   288  N  N   . ASP A 1 34  ? 11.785 -8.745  31.497  1.00 15.54 ? 34  ASP A N   1 
ATOM   289  C  CA  . ASP A 1 34  ? 11.505 -9.807  32.523  1.00 17.97 ? 34  ASP A CA  1 
ATOM   290  C  C   . ASP A 1 34  ? 10.045 -9.561  33.073  1.00 18.94 ? 34  ASP A C   1 
ATOM   291  O  O   . ASP A 1 34  ? 9.821  -8.624  33.812  1.00 21.59 ? 34  ASP A O   1 
ATOM   292  C  CB  . ASP A 1 34  ? 12.620 -9.763  33.586  1.00 21.53 ? 34  ASP A CB  1 
ATOM   293  C  CG  . ASP A 1 34  ? 12.346 -10.690 34.780  1.00 26.07 ? 34  ASP A CG  1 
ATOM   294  O  OD1 . ASP A 1 34  ? 11.217 -11.204 34.894  1.00 24.61 ? 34  ASP A OD1 1 
ATOM   295  O  OD2 . ASP A 1 34  ? 13.294 -10.906 35.588  1.00 35.88 ? 34  ASP A OD2 1 
ATOM   296  N  N   . THR A 1 35  ? 9.063  -10.316 32.614  1.00 19.06 ? 35  THR A N   1 
ATOM   297  C  CA  . THR A 1 35  ? 7.631  -9.975  32.788  1.00 21.09 ? 35  THR A CA  1 
ATOM   298  C  C   . THR A 1 35  ? 7.222  -10.129 34.242  1.00 24.60 ? 35  THR A C   1 
ATOM   299  O  O   . THR A 1 35  ? 6.243  -9.506  34.713  1.00 23.21 ? 35  THR A O   1 
ATOM   300  C  CB  . THR A 1 35  ? 6.735  -10.860 31.981  1.00 26.40 ? 35  THR A CB  1 
ATOM   301  O  OG1 . THR A 1 35  ? 6.963  -12.226 32.363  1.00 24.68 ? 35  THR A OG1 1 
ATOM   302  C  CG2 . THR A 1 35  ? 7.012  -10.686 30.475  1.00 23.17 ? 35  THR A CG2 1 
ATOM   303  N  N   . HIS A 1 36  ? 8.050  -10.893 34.944  1.00 24.32 ? 36  HIS A N   1 
ATOM   304  C  CA  . HIS A 1 36  ? 7.912  -11.095 36.379  1.00 26.06 ? 36  HIS A CA  1 
ATOM   305  C  C   . HIS A 1 36  ? 8.481  -10.004 37.258  1.00 29.17 ? 36  HIS A C   1 
ATOM   306  O  O   . HIS A 1 36  ? 7.992  -9.828  38.377  1.00 38.02 ? 36  HIS A O   1 
ATOM   307  C  CB  . HIS A 1 36  ? 8.408  -12.526 36.737  1.00 28.36 ? 36  HIS A CB  1 
ATOM   308  C  CG  . HIS A 1 36  ? 7.638  -13.638 35.981  1.00 27.37 ? 36  HIS A CG  1 
ATOM   309  N  ND1 . HIS A 1 36  ? 8.225  -14.438 35.040  1.00 34.98 ? 36  HIS A ND1 1 
ATOM   310  C  CD2 . HIS A 1 36  ? 6.292  -13.997 36.007  1.00 27.99 ? 36  HIS A CD2 1 
ATOM   311  C  CE1 . HIS A 1 36  ? 7.320  -15.289 34.539  1.00 32.16 ? 36  HIS A CE1 1 
ATOM   312  N  NE2 . HIS A 1 36  ? 6.127  -15.015 35.101  1.00 32.22 ? 36  HIS A NE2 1 
ATOM   313  N  N   . THR A 1 37  ? 9.485  -9.260  36.823  1.00 24.22 ? 37  THR A N   1 
ATOM   314  C  CA  . THR A 1 37  ? 10.022 -8.153  37.610  1.00 25.21 ? 37  THR A CA  1 
ATOM   315  C  C   . THR A 1 37  ? 9.583  -6.751  37.084  1.00 23.95 ? 37  THR A C   1 
ATOM   316  O  O   . THR A 1 37  ? 9.927  -5.702  37.713  1.00 26.20 ? 37  THR A O   1 
ATOM   317  C  CB  . THR A 1 37  ? 11.550 -8.251  37.894  1.00 29.98 ? 37  THR A CB  1 
ATOM   318  O  OG1 . THR A 1 37  ? 12.309 -7.930  36.730  1.00 37.30 ? 37  THR A OG1 1 
ATOM   319  C  CG2 . THR A 1 37  ? 11.917 -9.654  38.317  1.00 29.49 ? 37  THR A CG2 1 
ATOM   320  N  N   . ALA A 1 38  ? 8.842  -6.754  35.972  1.00 21.93 ? 38  ALA A N   1 
ATOM   321  C  CA  . ALA A 1 38  ? 8.194  -5.507  35.493  1.00 21.85 ? 38  ALA A CA  1 
ATOM   322  C  C   . ALA A 1 38  ? 7.088  -5.144  36.493  1.00 23.69 ? 38  ALA A C   1 
ATOM   323  O  O   . ALA A 1 38  ? 6.297  -5.998  36.891  1.00 27.21 ? 38  ALA A O   1 
ATOM   324  C  CB  . ALA A 1 38  ? 7.600  -5.656  34.112  1.00 18.94 ? 38  ALA A CB  1 
ATOM   325  N  N   . LYS A 1 39  ? 7.052  -3.869  36.879  1.00 23.07 ? 39  LYS A N   1 
ATOM   326  C  CA  . LYS A 1 39  ? 6.050  -3.373  37.829  1.00 25.68 ? 39  LYS A CA  1 
ATOM   327  C  C   . LYS A 1 39  ? 4.733  -2.899  37.181  1.00 23.93 ? 39  LYS A C   1 
ATOM   328  O  O   . LYS A 1 39  ? 4.704  -1.927  36.411  1.00 21.30 ? 39  LYS A O   1 
ATOM   329  C  CB  . LYS A 1 39  ? 6.692  -2.244  38.631  1.00 26.28 ? 39  LYS A CB  1 
ATOM   330  C  CG  . LYS A 1 39  ? 5.790  -1.517  39.633  1.00 32.88 ? 39  LYS A CG  1 
ATOM   331  C  CD  . LYS A 1 39  ? 5.696  -2.157  41.024  1.00 28.78 ? 39  LYS A CD  1 
ATOM   332  C  CE  . LYS A 1 39  ? 4.928  -1.215  41.949  1.00 33.06 ? 39  LYS A CE  1 
ATOM   333  N  NZ  . LYS A 1 39  ? 4.763  -1.698  43.359  1.00 33.15 ? 39  LYS A NZ  1 
ATOM   334  N  N   . TYR A 1 40  ? 3.628  -3.503  37.582  1.00 24.39 ? 40  TYR A N   1 
ATOM   335  C  CA  . TYR A 1 40  ? 2.364  -2.936  37.224  1.00 25.37 ? 40  TYR A CA  1 
ATOM   336  C  C   . TYR A 1 40  ? 2.198  -1.551  37.841  1.00 25.28 ? 40  TYR A C   1 
ATOM   337  O  O   . TYR A 1 40  ? 2.424  -1.356  39.060  1.00 25.57 ? 40  TYR A O   1 
ATOM   338  C  CB  . TYR A 1 40  ? 1.225  -3.869  37.570  1.00 29.10 ? 40  TYR A CB  1 
ATOM   339  C  CG  . TYR A 1 40  ? -0.106 -3.198  37.437  1.00 31.45 ? 40  TYR A CG  1 
ATOM   340  C  CD1 . TYR A 1 40  ? -0.554 -2.721  36.201  1.00 31.95 ? 40  TYR A CD1 1 
ATOM   341  C  CD2 . TYR A 1 40  ? -0.931 -3.029  38.556  1.00 36.84 ? 40  TYR A CD2 1 
ATOM   342  C  CE1 . TYR A 1 40  ? -1.755 -2.084  36.070  1.00 33.48 ? 40  TYR A CE1 1 
ATOM   343  C  CE2 . TYR A 1 40  ? -2.167 -2.400  38.430  1.00 34.53 ? 40  TYR A CE2 1 
ATOM   344  C  CZ  . TYR A 1 40  ? -2.570 -1.931  37.199  1.00 39.34 ? 40  TYR A CZ  1 
ATOM   345  O  OH  . TYR A 1 40  ? -3.777 -1.308  37.082  1.00 40.21 ? 40  TYR A OH  1 
ATOM   346  N  N   . ASP A 1 41  ? 1.804  -0.592  36.995  1.00 25.88 ? 41  ASP A N   1 
ATOM   347  C  CA  . ASP A 1 41  ? 1.698  0.777   37.475  1.00 26.99 ? 41  ASP A CA  1 
ATOM   348  C  C   . ASP A 1 41  ? 0.325  1.347   37.189  1.00 30.43 ? 41  ASP A C   1 
ATOM   349  O  O   . ASP A 1 41  ? 0.051  1.760   36.045  1.00 25.45 ? 41  ASP A O   1 
ATOM   350  C  CB  . ASP A 1 41  ? 2.773  1.691   36.895  1.00 30.09 ? 41  ASP A CB  1 
ATOM   351  C  CG  . ASP A 1 41  ? 2.694  3.121   37.476  1.00 33.14 ? 41  ASP A CG  1 
ATOM   352  O  OD1 . ASP A 1 41  ? 1.746  3.421   38.229  1.00 35.01 ? 41  ASP A OD1 1 
ATOM   353  O  OD2 . ASP A 1 41  ? 3.590  3.928   37.195  1.00 35.05 ? 41  ASP A OD2 1 
ATOM   354  N  N   . PRO A 1 42  ? -0.544 1.412   38.233  1.00 33.74 ? 42  PRO A N   1 
ATOM   355  C  CA  . PRO A 1 42  ? -1.958 1.741   37.982  1.00 35.78 ? 42  PRO A CA  1 
ATOM   356  C  C   . PRO A 1 42  ? -2.144 3.227   37.641  1.00 34.25 ? 42  PRO A C   1 
ATOM   357  O  O   . PRO A 1 42  ? -3.236 3.638   37.195  1.00 37.89 ? 42  PRO A O   1 
ATOM   358  C  CB  . PRO A 1 42  ? -2.656 1.393   39.325  1.00 37.13 ? 42  PRO A CB  1 
ATOM   359  C  CG  . PRO A 1 42  ? -1.614 0.685   40.161  1.00 38.99 ? 42  PRO A CG  1 
ATOM   360  C  CD  . PRO A 1 42  ? -0.282 1.191   39.670  1.00 34.73 ? 42  PRO A CD  1 
ATOM   361  N  N   . SER A 1 43  ? -1.094 4.020   37.831  1.00 33.74 ? 43  SER A N   1 
ATOM   362  C  CA  . SER A 1 43  ? -1.129 5.418   37.423  1.00 36.23 ? 43  SER A CA  1 
ATOM   363  C  C   . SER A 1 43  ? -0.817 5.632   35.925  1.00 36.87 ? 43  SER A C   1 
ATOM   364  O  O   . SER A 1 43  ? -1.000 6.736   35.407  1.00 41.10 ? 43  SER A O   1 
ATOM   365  C  CB  . SER A 1 43  ? -0.235 6.289   38.320  1.00 39.50 ? 43  SER A CB  1 
ATOM   366  O  OG  . SER A 1 43  ? 1.124  6.258   37.919  1.00 38.58 ? 43  SER A OG  1 
ATOM   367  N  N   . LEU A 1 44  ? -0.349 4.598   35.213  1.00 33.34 ? 44  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 44  ? -0.136 4.728   33.770  1.00 30.96 ? 44  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 44  ? -1.484 4.876   33.069  1.00 36.04 ? 44  LEU A C   1 
ATOM   370  O  O   . LEU A 1 44  ? -2.433 4.136   33.359  1.00 35.00 ? 44  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 44  ? 0.583  3.495   33.210  1.00 28.85 ? 44  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 44  ? 2.087  3.414   33.480  1.00 25.06 ? 44  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 44  ? 2.583  2.018   33.089  1.00 25.22 ? 44  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 44  ? 2.846  4.505   32.737  1.00 23.62 ? 44  LEU A CD2 1 
ATOM   375  N  N   . LYS A 1 45  ? -1.562 5.819   32.143  1.00 34.74 ? 45  LYS A N   1 
ATOM   376  C  CA  . LYS A 1 45  ? -2.782 6.016   31.335  1.00 32.95 ? 45  LYS A CA  1 
ATOM   377  C  C   . LYS A 1 45  ? -2.808 5.067   30.151  1.00 30.89 ? 45  LYS A C   1 
ATOM   378  O  O   . LYS A 1 45  ? -1.746 4.509   29.768  1.00 29.82 ? 45  LYS A O   1 
ATOM   379  C  CB  . LYS A 1 45  ? -2.811 7.423   30.811  1.00 34.20 ? 45  LYS A CB  1 
ATOM   380  C  CG  . LYS A 1 45  ? -2.823 8.459   31.907  1.00 38.23 ? 45  LYS A CG  1 
ATOM   381  C  CD  . LYS A 1 45  ? -2.902 9.866   31.343  1.00 45.14 ? 45  LYS A CD  1 
ATOM   382  C  CE  . LYS A 1 45  ? -2.506 10.879  32.416  1.00 50.83 ? 45  LYS A CE  1 
ATOM   383  N  NZ  . LYS A 1 45  ? -1.125 10.556  32.894  1.00 49.82 ? 45  LYS A NZ  1 
ATOM   384  N  N   . PRO A 1 46  ? -4.021 4.850   29.554  1.00 26.13 ? 46  PRO A N   1 
ATOM   385  C  CA  . PRO A 1 46  ? -4.050 4.141   28.284  1.00 23.31 ? 46  PRO A CA  1 
ATOM   386  C  C   . PRO A 1 46  ? -3.182 4.977   27.307  1.00 21.17 ? 46  PRO A C   1 
ATOM   387  O  O   . PRO A 1 46  ? -3.128 6.218   27.383  1.00 22.34 ? 46  PRO A O   1 
ATOM   388  C  CB  . PRO A 1 46  ? -5.561 4.100   27.904  1.00 26.31 ? 46  PRO A CB  1 
ATOM   389  C  CG  . PRO A 1 46  ? -6.288 4.393   29.184  1.00 27.11 ? 46  PRO A CG  1 
ATOM   390  C  CD  . PRO A 1 46  ? -5.374 5.278   29.983  1.00 28.57 ? 46  PRO A CD  1 
ATOM   391  N  N   . LEU A 1 47  ? -2.527 4.261   26.412  1.00 23.74 ? 47  LEU A N   1 
ATOM   392  C  CA  . LEU A 1 47  ? -1.793 4.828   25.311  1.00 21.78 ? 47  LEU A CA  1 
ATOM   393  C  C   . LEU A 1 47  ? -2.825 5.346   24.330  1.00 24.33 ? 47  LEU A C   1 
ATOM   394  O  O   . LEU A 1 47  ? -3.806 4.650   24.030  1.00 25.01 ? 47  LEU A O   1 
ATOM   395  C  CB  . LEU A 1 47  ? -1.055 3.686   24.644  1.00 24.29 ? 47  LEU A CB  1 
ATOM   396  C  CG  . LEU A 1 47  ? 0.044  4.035   23.717  1.00 25.29 ? 47  LEU A CG  1 
ATOM   397  C  CD1 . LEU A 1 47  ? 1.054  4.917   24.463  1.00 24.49 ? 47  LEU A CD1 1 
ATOM   398  C  CD2 . LEU A 1 47  ? 0.652  2.724   23.218  1.00 25.44 ? 47  LEU A CD2 1 
ATOM   399  N  N   . SER A 1 48  ? -2.578 6.536   23.797  1.00 19.16 ? 48  SER A N   1 
ATOM   400  C  CA  . SER A 1 48  ? -3.397 7.098   22.777  1.00 21.48 ? 48  SER A CA  1 
ATOM   401  C  C   . SER A 1 48  ? -2.677 7.138   21.470  1.00 21.07 ? 48  SER A C   1 
ATOM   402  O  O   . SER A 1 48  ? -1.690 7.864   21.331  1.00 17.35 ? 48  SER A O   1 
ATOM   403  C  CB  . SER A 1 48  ? -3.776 8.504   23.209  1.00 20.12 ? 48  SER A CB  1 
ATOM   404  O  OG  . SER A 1 48  ? -4.332 9.271   22.158  1.00 22.40 ? 48  SER A OG  1 
ATOM   405  N  N   . VAL A 1 49  ? -3.148 6.354   20.520  1.00 18.45 ? 49  VAL A N   1 
ATOM   406  C  CA  . VAL A 1 49  ? -2.520 6.259   19.184  1.00 21.11 ? 49  VAL A CA  1 
ATOM   407  C  C   . VAL A 1 49  ? -3.534 6.816   18.215  1.00 23.40 ? 49  VAL A C   1 
ATOM   408  O  O   . VAL A 1 49  ? -4.630 6.267   18.047  1.00 25.26 ? 49  VAL A O   1 
ATOM   409  C  CB  . VAL A 1 49  ? -2.169 4.794   18.826  1.00 23.07 ? 49  VAL A CB  1 
ATOM   410  C  CG1 . VAL A 1 49  ? -1.496 4.693   17.440  1.00 25.18 ? 49  VAL A CG1 1 
ATOM   411  C  CG2 . VAL A 1 49  ? -1.320 4.146   19.914  1.00 24.34 ? 49  VAL A CG2 1 
ATOM   412  N  N   . SER A 1 50  ? -3.231 7.970   17.644  1.00 18.58 ? 50  SER A N   1 
ATOM   413  C  CA  . SER A 1 50  ? -4.164 8.663   16.736  1.00 21.47 ? 50  SER A CA  1 
ATOM   414  C  C   . SER A 1 50  ? -3.546 8.757   15.363  1.00 20.00 ? 50  SER A C   1 
ATOM   415  O  O   . SER A 1 50  ? -2.958 9.751   14.987  1.00 19.61 ? 50  SER A O   1 
ATOM   416  C  CB  . SER A 1 50  ? -4.599 10.023  17.306  1.00 21.81 ? 50  SER A CB  1 
ATOM   417  O  OG  . SER A 1 50  ? -5.132 9.832   18.623  1.00 30.04 ? 50  SER A OG  1 
ATOM   418  N  N   . TYR A 1 51  ? -3.755 7.712   14.569  1.00 19.94 ? 51  TYR A N   1 
ATOM   419  C  CA  . TYR A 1 51  ? -3.192 7.594   13.222  1.00 18.78 ? 51  TYR A CA  1 
ATOM   420  C  C   . TYR A 1 51  ? -4.164 7.865   12.032  1.00 19.77 ? 51  TYR A C   1 
ATOM   421  O  O   . TYR A 1 51  ? -3.765 7.705   10.873  1.00 21.71 ? 51  TYR A O   1 
ATOM   422  C  CB  . TYR A 1 51  ? -2.453 6.245   13.005  1.00 18.45 ? 51  TYR A CB  1 
ATOM   423  C  CG  . TYR A 1 51  ? -1.154 5.990   13.816  1.00 17.63 ? 51  TYR A CG  1 
ATOM   424  C  CD1 . TYR A 1 51  ? -0.415 7.045   14.460  1.00 18.05 ? 51  TYR A CD1 1 
ATOM   425  C  CD2 . TYR A 1 51  ? -0.662 4.699   13.885  1.00 16.85 ? 51  TYR A CD2 1 
ATOM   426  C  CE1 . TYR A 1 51  ? 0.760  6.752   15.215  1.00 15.96 ? 51  TYR A CE1 1 
ATOM   427  C  CE2 . TYR A 1 51  ? 0.499  4.404   14.563  1.00 17.03 ? 51  TYR A CE2 1 
ATOM   428  C  CZ  . TYR A 1 51  ? 1.204  5.444   15.224  1.00 16.43 ? 51  TYR A CZ  1 
ATOM   429  O  OH  . TYR A 1 51  ? 2.348  5.086   15.877  1.00 16.22 ? 51  TYR A OH  1 
ATOM   430  N  N   . ASP A 1 52  ? -5.400 8.302   12.333  1.00 24.64 ? 52  ASP A N   1 
ATOM   431  C  CA  . ASP A 1 52  ? -6.431 8.577   11.287  1.00 28.15 ? 52  ASP A CA  1 
ATOM   432  C  C   . ASP A 1 52  ? -5.940 9.451   10.127  1.00 28.52 ? 52  ASP A C   1 
ATOM   433  O  O   . ASP A 1 52  ? -6.211 9.178   8.956   1.00 29.62 ? 52  ASP A O   1 
ATOM   434  C  CB  . ASP A 1 52  ? -7.786 9.076   11.852  1.00 31.38 ? 52  ASP A CB  1 
ATOM   435  C  CG  . ASP A 1 52  ? -7.650 10.155  12.944  1.00 37.43 ? 52  ASP A CG  1 
ATOM   436  O  OD1 . ASP A 1 52  ? -7.311 9.845   14.121  1.00 43.06 ? 52  ASP A OD1 1 
ATOM   437  O  OD2 . ASP A 1 52  ? -7.925 11.343  12.630  1.00 48.79 ? 52  ASP A OD2 1 
ATOM   438  N  N   A GLN A 1 53  ? -5.161 10.458  10.465  0.50 25.65 ? 53  GLN A N   1 
ATOM   439  N  N   B GLN A 1 53  ? -5.190 10.496  10.432  0.50 26.20 ? 53  GLN A N   1 
ATOM   440  C  CA  A GLN A 1 53  ? -4.710 11.375  9.433   0.50 24.43 ? 53  GLN A CA  1 
ATOM   441  C  CA  B GLN A 1 53  ? -4.733 11.370  9.338   0.50 24.90 ? 53  GLN A CA  1 
ATOM   442  C  C   A GLN A 1 53  ? -3.249 11.199  9.069   0.50 21.58 ? 53  GLN A C   1 
ATOM   443  C  C   B GLN A 1 53  ? -3.298 11.104  8.882   0.50 21.63 ? 53  GLN A C   1 
ATOM   444  O  O   A GLN A 1 53  ? -2.654 12.133  8.544   0.50 20.76 ? 53  GLN A O   1 
ATOM   445  O  O   B GLN A 1 53  ? -2.758 11.880  8.104   0.50 20.36 ? 53  GLN A O   1 
ATOM   446  C  CB  A GLN A 1 53  ? -5.004 12.812  9.871   0.50 25.90 ? 53  GLN A CB  1 
ATOM   447  C  CB  B GLN A 1 53  ? -4.925 12.858  9.694   0.50 27.48 ? 53  GLN A CB  1 
ATOM   448  C  CG  A GLN A 1 53  ? -6.444 13.020  10.320  0.50 28.38 ? 53  GLN A CG  1 
ATOM   449  C  CG  B GLN A 1 53  ? -6.348 13.418  9.593   0.50 31.49 ? 53  GLN A CG  1 
ATOM   450  C  CD  A GLN A 1 53  ? -7.404 12.821  9.168   0.50 29.70 ? 53  GLN A CD  1 
ATOM   451  C  CD  B GLN A 1 53  ? -6.465 14.846  10.146  0.50 33.78 ? 53  GLN A CD  1 
ATOM   452  O  OE1 A GLN A 1 53  ? -7.120 13.232  8.040   0.50 35.24 ? 53  GLN A OE1 1 
ATOM   453  O  OE1 B GLN A 1 53  ? -6.371 15.068  11.355  0.50 30.39 ? 53  GLN A OE1 1 
ATOM   454  N  NE2 A GLN A 1 53  ? -8.538 12.163  9.434   0.50 30.84 ? 53  GLN A NE2 1 
ATOM   455  N  NE2 B GLN A 1 53  ? -6.685 15.819  9.257   0.50 34.53 ? 53  GLN A NE2 1 
ATOM   456  N  N   . ALA A 1 54  ? -2.651 10.024  9.339   1.00 20.62 ? 54  ALA A N   1 
ATOM   457  C  CA  . ALA A 1 54  ? -1.264 9.784   8.912   1.00 16.98 ? 54  ALA A CA  1 
ATOM   458  C  C   . ALA A 1 54  ? -1.060 9.927   7.408   1.00 19.67 ? 54  ALA A C   1 
ATOM   459  O  O   . ALA A 1 54  ? -1.908 9.448   6.632   1.00 21.61 ? 54  ALA A O   1 
ATOM   460  C  CB  . ALA A 1 54  ? -0.702 8.408   9.384   1.00 16.65 ? 54  ALA A CB  1 
ATOM   461  N  N   . THR A 1 55  ? 0.029  10.602  7.006   1.00 17.83 ? 55  THR A N   1 
ATOM   462  C  CA  . THR A 1 55  ? 0.384  10.739  5.568   1.00 18.91 ? 55  THR A CA  1 
ATOM   463  C  C   . THR A 1 55  ? 1.746  10.237  5.238   1.00 18.85 ? 55  THR A C   1 
ATOM   464  O  O   . THR A 1 55  ? 2.729  10.944  5.462   1.00 18.38 ? 55  THR A O   1 
ATOM   465  C  CB  . THR A 1 55  ? 0.405  12.200  5.064   1.00 25.80 ? 55  THR A CB  1 
ATOM   466  O  OG1 . THR A 1 55  ? -0.680 12.902  5.620   1.00 30.87 ? 55  THR A OG1 1 
ATOM   467  C  CG2 . THR A 1 55  ? 0.266  12.163  3.512   1.00 24.57 ? 55  THR A CG2 1 
ATOM   468  N  N   . SER A 1 56  ? 1.838  9.032   4.693   1.00 18.61 ? 56  SER A N   1 
ATOM   469  C  CA  . SER A 1 56  ? 3.123  8.529   4.309   1.00 19.17 ? 56  SER A CA  1 
ATOM   470  C  C   . SER A 1 56  ? 3.696  9.202   3.014   1.00 19.11 ? 56  SER A C   1 
ATOM   471  O  O   . SER A 1 56  ? 2.950  9.760   2.143   1.00 23.01 ? 56  SER A O   1 
ATOM   472  C  CB  . SER A 1 56  ? 3.055  6.999   4.181   1.00 20.57 ? 56  SER A CB  1 
ATOM   473  O  OG  . SER A 1 56  ? 2.171  6.635   3.111   1.00 21.27 ? 56  SER A OG  1 
ATOM   474  N  N   . LEU A 1 57  ? 4.989  9.268   2.932   1.00 19.24 ? 57  LEU A N   1 
ATOM   475  C  CA  . LEU A 1 57  ? 5.588  9.922   1.749   1.00 21.85 ? 57  LEU A CA  1 
ATOM   476  C  C   . LEU A 1 57  ? 6.401  8.953   0.850   1.00 22.43 ? 57  LEU A C   1 
ATOM   477  O  O   . LEU A 1 57  ? 6.242  8.904   -0.394  1.00 21.21 ? 57  LEU A O   1 
ATOM   478  C  CB  . LEU A 1 57  ? 6.500  11.066  2.174   1.00 25.51 ? 57  LEU A CB  1 
ATOM   479  C  CG  . LEU A 1 57  ? 5.849  12.308  2.810   1.00 28.99 ? 57  LEU A CG  1 
ATOM   480  C  CD1 . LEU A 1 57  ? 6.962  13.226  3.293   1.00 28.40 ? 57  LEU A CD1 1 
ATOM   481  C  CD2 . LEU A 1 57  ? 4.936  13.023  1.809   1.00 32.89 ? 57  LEU A CD2 1 
ATOM   482  N  N   A ARG A 1 58  ? 7.213  8.132   1.469   0.50 20.29 ? 58  ARG A N   1 
ATOM   483  N  N   B ARG A 1 58  ? 7.358  8.288   1.500   0.50 21.83 ? 58  ARG A N   1 
ATOM   484  C  CA  A ARG A 1 58  ? 8.205  7.430   0.709   0.50 18.04 ? 58  ARG A CA  1 
ATOM   485  C  CA  B ARG A 1 58  ? 8.471  7.616   0.834   0.50 18.99 ? 58  ARG A CA  1 
ATOM   486  C  C   A ARG A 1 58  ? 8.517  6.194   1.484   0.50 17.97 ? 58  ARG A C   1 
ATOM   487  C  C   B ARG A 1 58  ? 8.949  6.379   1.599   0.50 19.17 ? 58  ARG A C   1 
ATOM   488  O  O   A ARG A 1 58  ? 8.127  6.084   2.654   0.50 14.95 ? 58  ARG A O   1 
ATOM   489  O  O   B ARG A 1 58  ? 8.961  6.347   2.842   0.50 14.85 ? 58  ARG A O   1 
ATOM   490  C  CB  A ARG A 1 58  ? 9.501  8.240   0.655   0.50 17.88 ? 58  ARG A CB  1 
ATOM   491  C  CB  B ARG A 1 58  ? 9.657  8.564   0.616   0.50 20.15 ? 58  ARG A CB  1 
ATOM   492  C  CG  A ARG A 1 58  ? 9.590  9.383   -0.363  0.50 19.01 ? 58  ARG A CG  1 
ATOM   493  C  CG  B ARG A 1 58  ? 10.813 7.930   -0.142  0.50 20.76 ? 58  ARG A CG  1 
ATOM   494  C  CD  A ARG A 1 58  ? 11.051 9.695   -0.571  0.50 18.18 ? 58  ARG A CD  1 
ATOM   495  C  CD  B ARG A 1 58  ? 11.855 8.891   -0.750  0.50 22.76 ? 58  ARG A CD  1 
ATOM   496  N  NE  A ARG A 1 58  ? 11.871 9.346   0.615   0.50 18.30 ? 58  ARG A NE  1 
ATOM   497  N  NE  B ARG A 1 58  ? 11.234 9.612   -1.842  0.50 20.33 ? 58  ARG A NE  1 
ATOM   498  C  CZ  A ARG A 1 58  ? 13.208 9.243   0.600   0.50 17.61 ? 58  ARG A CZ  1 
ATOM   499  C  CZ  B ARG A 1 58  ? 11.374 9.347   -3.136  0.50 19.07 ? 58  ARG A CZ  1 
ATOM   500  N  NH1 A ARG A 1 58  ? 13.866 9.431   -0.513  0.50 18.39 ? 58  ARG A NH1 1 
ATOM   501  N  NH1 B ARG A 1 58  ? 12.234 8.435   -3.591  0.50 19.37 ? 58  ARG A NH1 1 
ATOM   502  N  NH2 A ARG A 1 58  ? 13.896 9.029   1.707   0.50 18.95 ? 58  ARG A NH2 1 
ATOM   503  N  NH2 B ARG A 1 58  ? 10.677 10.062  -3.984  0.50 17.98 ? 58  ARG A NH2 1 
ATOM   504  N  N   . ILE A 1 59  ? 9.315  5.356   0.833   1.00 18.72 ? 59  ILE A N   1 
ATOM   505  C  CA  . ILE A 1 59  ? 9.962  4.194   1.461   1.00 18.47 ? 59  ILE A CA  1 
ATOM   506  C  C   . ILE A 1 59  ? 11.402 4.111   0.955   1.00 18.25 ? 59  ILE A C   1 
ATOM   507  O  O   . ILE A 1 59  ? 11.700 4.280   -0.250  1.00 18.14 ? 59  ILE A O   1 
ATOM   508  C  CB  . ILE A 1 59  ? 9.106  2.918   1.293   1.00 20.05 ? 59  ILE A CB  1 
ATOM   509  C  CG1 . ILE A 1 59  ? 9.724  1.777   2.120   1.00 19.07 ? 59  ILE A CG1 1 
ATOM   510  C  CG2 . ILE A 1 59  ? 9.021  2.473   -0.173  1.00 19.04 ? 59  ILE A CG2 1 
ATOM   511  C  CD1 . ILE A 1 59  ? 8.882  0.491   2.056   1.00 20.79 ? 59  ILE A CD1 1 
ATOM   512  N  N   . LEU A 1 60  ? 12.320 3.860   1.873   1.00 17.10 ? 60  LEU A N   1 
ATOM   513  C  CA  . LEU A 1 60  ? 13.693 3.931   1.666   1.00 15.84 ? 60  LEU A CA  1 
ATOM   514  C  C   . LEU A 1 60  ? 14.481 2.744   2.232   1.00 18.45 ? 60  LEU A C   1 
ATOM   515  O  O   . LEU A 1 60  ? 14.349 2.423   3.426   1.00 17.58 ? 60  LEU A O   1 
ATOM   516  C  CB  . LEU A 1 60  ? 14.169 5.225   2.363   1.00 20.92 ? 60  LEU A CB  1 
ATOM   517  C  CG  . LEU A 1 60  ? 15.662 5.419   2.271   1.00 21.24 ? 60  LEU A CG  1 
ATOM   518  C  CD1 . LEU A 1 60  ? 16.230 5.664   0.858   1.00 24.30 ? 60  LEU A CD1 1 
ATOM   519  C  CD2 . LEU A 1 60  ? 16.077 6.550   3.226   1.00 20.89 ? 60  LEU A CD2 1 
ATOM   520  N  N   . ASN A 1 61  ? 15.333 2.120   1.420   1.00 17.64 ? 61  ASN A N   1 
ATOM   521  C  CA  . ASN A 1 61  ? 16.311 1.181   1.899   1.00 17.74 ? 61  ASN A CA  1 
ATOM   522  C  C   . ASN A 1 61  ? 17.562 1.981   2.267   1.00 21.75 ? 61  ASN A C   1 
ATOM   523  O  O   . ASN A 1 61  ? 18.168 2.565   1.364   1.00 21.22 ? 61  ASN A O   1 
ATOM   524  C  CB  . ASN A 1 61  ? 16.648 0.098   0.829   1.00 18.14 ? 61  ASN A CB  1 
ATOM   525  C  CG  . ASN A 1 61  ? 17.690 -0.901  1.279   1.00 20.26 ? 61  ASN A CG  1 
ATOM   526  O  OD1 . ASN A 1 61  ? 18.513 -0.648  2.148   1.00 22.43 ? 61  ASN A OD1 1 
ATOM   527  N  ND2 . ASN A 1 61  ? 17.692 -2.114  0.629   1.00 19.53 ? 61  ASN A ND2 1 
ATOM   528  N  N   . ASN A 1 62  ? 17.946 2.034   3.557   1.00 20.87 ? 62  ASN A N   1 
ATOM   529  C  CA  . ASN A 1 62  ? 19.106 2.871   4.006   1.00 21.08 ? 62  ASN A CA  1 
ATOM   530  C  C   . ASN A 1 62  ? 20.348 2.036   4.287   1.00 22.10 ? 62  ASN A C   1 
ATOM   531  O  O   . ASN A 1 62  ? 21.409 2.470   4.859   1.00 23.14 ? 62  ASN A O   1 
ATOM   532  C  CB  . ASN A 1 62  ? 18.697 3.768   5.217   1.00 22.37 ? 62  ASN A CB  1 
ATOM   533  C  CG  . ASN A 1 62  ? 18.430 2.932   6.493   1.00 25.25 ? 62  ASN A CG  1 
ATOM   534  O  OD1 . ASN A 1 62  ? 18.557 1.700   6.479   1.00 19.48 ? 62  ASN A OD1 1 
ATOM   535  N  ND2 . ASN A 1 62  ? 18.083 3.605   7.591   1.00 27.60 ? 62  ASN A ND2 1 
ATOM   536  N  N   . GLY A 1 63  ? 20.262 0.779   3.846   1.00 19.95 ? 63  GLY A N   1 
ATOM   537  C  CA  . GLY A 1 63  ? 21.286 -0.155  3.977   1.00 18.35 ? 63  GLY A CA  1 
ATOM   538  C  C   . GLY A 1 63  ? 21.352 -0.857  5.336   1.00 19.12 ? 63  GLY A C   1 
ATOM   539  O  O   . GLY A 1 63  ? 22.229 -1.713  5.524   1.00 19.50 ? 63  GLY A O   1 
ATOM   540  N  N   . HIS A 1 64  ? 20.426 -0.490  6.245   1.00 18.82 ? 64  HIS A N   1 
ATOM   541  C  CA  . HIS A 1 64  ? 20.327 -1.158  7.588   1.00 16.97 ? 64  HIS A CA  1 
ATOM   542  C  C   . HIS A 1 64  ? 18.950 -1.775  7.721   1.00 17.97 ? 64  HIS A C   1 
ATOM   543  O  O   . HIS A 1 64  ? 18.777 -2.872  8.302   1.00 19.34 ? 64  HIS A O   1 
ATOM   544  C  CB  . HIS A 1 64  ? 20.531 -0.115  8.683   1.00 18.25 ? 64  HIS A CB  1 
ATOM   545  C  CG  . HIS A 1 64  ? 21.840 0.659   8.523   1.00 21.97 ? 64  HIS A CG  1 
ATOM   546  N  ND1 . HIS A 1 64  ? 23.052 0.058   8.616   1.00 23.35 ? 64  HIS A ND1 1 
ATOM   547  C  CD2 . HIS A 1 64  ? 22.078 2.009   8.233   1.00 24.89 ? 64  HIS A CD2 1 
ATOM   548  C  CE1 . HIS A 1 64  ? 24.039 0.997   8.458   1.00 23.16 ? 64  HIS A CE1 1 
ATOM   549  N  NE2 . HIS A 1 64  ? 23.441 2.190   8.209   1.00 22.58 ? 64  HIS A NE2 1 
ATOM   550  N  N   . ALA A 1 65  ? 17.967 -1.085  7.206   1.00 15.60 ? 65  ALA A N   1 
ATOM   551  C  CA  . ALA A 1 65  ? 16.564 -1.507  7.222   1.00 16.96 ? 65  ALA A CA  1 
ATOM   552  C  C   . ALA A 1 65  ? 15.795 -0.808  6.082   1.00 15.22 ? 65  ALA A C   1 
ATOM   553  O  O   . ALA A 1 65  ? 16.434 -0.103  5.240   1.00 17.14 ? 65  ALA A O   1 
ATOM   554  C  CB  . ALA A 1 65  ? 15.915 -1.237  8.596   1.00 15.03 ? 65  ALA A CB  1 
ATOM   555  N  N   . PHE A 1 66  ? 14.457 -0.941  6.033   1.00 14.91 ? 66  PHE A N   1 
ATOM   556  C  CA  . PHE A 1 66  ? 13.723 -0.028  5.198   1.00 16.16 ? 66  PHE A CA  1 
ATOM   557  C  C   . PHE A 1 66  ? 12.870 0.893   6.064   1.00 16.98 ? 66  PHE A C   1 
ATOM   558  O  O   . PHE A 1 66  ? 12.311 0.467   7.091   1.00 16.40 ? 66  PHE A O   1 
ATOM   559  C  CB  . PHE A 1 66  ? 12.877 -0.776  4.112   1.00 16.94 ? 66  PHE A CB  1 
ATOM   560  C  CG  . PHE A 1 66  ? 11.829 -1.684  4.676   1.00 16.38 ? 66  PHE A CG  1 
ATOM   561  C  CD1 . PHE A 1 66  ? 10.564 -1.167  5.028   1.00 16.29 ? 66  PHE A CD1 1 
ATOM   562  C  CD2 . PHE A 1 66  ? 12.052 -3.080  4.827   1.00 17.95 ? 66  PHE A CD2 1 
ATOM   563  C  CE1 . PHE A 1 66  ? 9.590  -1.959  5.609   1.00 18.22 ? 66  PHE A CE1 1 
ATOM   564  C  CE2 . PHE A 1 66  ? 11.049 -3.887  5.414   1.00 16.95 ? 66  PHE A CE2 1 
ATOM   565  C  CZ  . PHE A 1 66  ? 9.812  -3.334  5.760   1.00 16.11 ? 66  PHE A CZ  1 
ATOM   566  N  N   . ASN A 1 67  ? 12.753 2.163   5.668   1.00 17.02 ? 67  ASN A N   1 
ATOM   567  C  CA  . ASN A 1 67  ? 12.013 3.101   6.466   1.00 18.59 ? 67  ASN A CA  1 
ATOM   568  C  C   . ASN A 1 67  ? 10.834 3.613   5.671   1.00 16.42 ? 67  ASN A C   1 
ATOM   569  O  O   . ASN A 1 67  ? 11.037 4.061   4.484   1.00 21.24 ? 67  ASN A O   1 
ATOM   570  C  CB  . ASN A 1 67  ? 12.874 4.350   6.807   1.00 21.23 ? 67  ASN A CB  1 
ATOM   571  C  CG  . ASN A 1 67  ? 14.026 4.110   7.758   1.00 25.54 ? 67  ASN A CG  1 
ATOM   572  O  OD1 . ASN A 1 67  ? 14.115 3.134   8.509   1.00 21.17 ? 67  ASN A OD1 1 
ATOM   573  N  ND2 . ASN A 1 67  ? 14.938 5.101   7.767   1.00 27.69 ? 67  ASN A ND2 1 
ATOM   574  N  N   . VAL A 1 68  ? 9.644  3.544   6.253   1.00 16.03 ? 68  VAL A N   1 
ATOM   575  C  CA  . VAL A 1 68  ? 8.470  4.217   5.690   1.00 15.78 ? 68  VAL A CA  1 
ATOM   576  C  C   . VAL A 1 68  ? 8.399  5.600   6.388   1.00 18.01 ? 68  VAL A C   1 
ATOM   577  O  O   . VAL A 1 68  ? 8.161  5.660   7.607   1.00 15.17 ? 68  VAL A O   1 
ATOM   578  C  CB  . VAL A 1 68  ? 7.187  3.413   5.824   1.00 16.98 ? 68  VAL A CB  1 
ATOM   579  C  CG1 . VAL A 1 68  ? 6.021  4.286   5.343   1.00 16.92 ? 68  VAL A CG1 1 
ATOM   580  C  CG2 . VAL A 1 68  ? 7.227  2.116   4.980   1.00 17.61 ? 68  VAL A CG2 1 
ATOM   581  N  N   . GLU A 1 69  ? 8.556  6.689   5.638   1.00 19.60 ? 69  GLU A N   1 
ATOM   582  C  CA  . GLU A 1 69  ? 8.546  8.040   6.172   1.00 20.61 ? 69  GLU A CA  1 
ATOM   583  C  C   . GLU A 1 69  ? 7.244  8.734   5.983   1.00 21.43 ? 69  GLU A C   1 
ATOM   584  O  O   . GLU A 1 69  ? 6.537  8.528   4.966   1.00 25.65 ? 69  GLU A O   1 
ATOM   585  C  CB  . GLU A 1 69  ? 9.537  8.866   5.430   1.00 27.87 ? 69  GLU A CB  1 
ATOM   586  C  CG  . GLU A 1 69  ? 10.925 8.296   5.479   1.00 30.36 ? 69  GLU A CG  1 
ATOM   587  C  CD  . GLU A 1 69  ? 11.704 8.619   4.220   1.00 38.69 ? 69  GLU A CD  1 
ATOM   588  O  OE1 . GLU A 1 69  ? 11.046 9.169   3.258   1.00 38.23 ? 69  GLU A OE1 1 
ATOM   589  O  OE2 . GLU A 1 69  ? 12.946 8.329   4.180   1.00 40.96 ? 69  GLU A OE2 1 
ATOM   590  N  N   . PHE A 1 70  ? 6.949  9.599   6.950   1.00 16.48 ? 70  PHE A N   1 
ATOM   591  C  CA  . PHE A 1 70  ? 5.702  10.339  6.988   1.00 16.08 ? 70  PHE A CA  1 
ATOM   592  C  C   . PHE A 1 70  ? 5.970  11.825  6.866   1.00 17.31 ? 70  PHE A C   1 
ATOM   593  O  O   . PHE A 1 70  ? 6.988  12.277  7.233   1.00 17.30 ? 70  PHE A O   1 
ATOM   594  C  CB  . PHE A 1 70  ? 4.907  10.019  8.290   1.00 15.31 ? 70  PHE A CB  1 
ATOM   595  C  CG  . PHE A 1 70  ? 4.289  8.621   8.250   1.00 14.73 ? 70  PHE A CG  1 
ATOM   596  C  CD1 . PHE A 1 70  ? 5.091  7.510   8.513   1.00 16.35 ? 70  PHE A CD1 1 
ATOM   597  C  CD2 . PHE A 1 70  ? 2.968  8.415   7.899   1.00 14.47 ? 70  PHE A CD2 1 
ATOM   598  C  CE1 . PHE A 1 70  ? 4.582  6.229   8.379   1.00 15.89 ? 70  PHE A CE1 1 
ATOM   599  C  CE2 . PHE A 1 70  ? 2.404  7.132   7.814   1.00 15.27 ? 70  PHE A CE2 1 
ATOM   600  C  CZ  . PHE A 1 70  ? 3.259  6.032   8.049   1.00 15.64 ? 70  PHE A CZ  1 
ATOM   601  N  N   . ASP A 1 71  ? 4.982  12.529  6.320   1.00 19.10 ? 71  ASP A N   1 
ATOM   602  C  CA  . ASP A 1 71  ? 4.935  13.994  6.396   1.00 18.50 ? 71  ASP A CA  1 
ATOM   603  C  C   . ASP A 1 71  ? 4.475  14.363  7.821   1.00 17.32 ? 71  ASP A C   1 
ATOM   604  O  O   . ASP A 1 71  ? 3.300  14.127  8.222   1.00 18.90 ? 71  ASP A O   1 
ATOM   605  C  CB  . ASP A 1 71  ? 3.985  14.466  5.340   1.00 21.22 ? 71  ASP A CB  1 
ATOM   606  C  CG  . ASP A 1 71  ? 3.712  15.979  5.416   1.00 27.14 ? 71  ASP A CG  1 
ATOM   607  O  OD1 . ASP A 1 71  ? 4.261  16.671  6.272   1.00 21.92 ? 71  ASP A OD1 1 
ATOM   608  O  OD2 . ASP A 1 71  ? 2.927  16.465  4.575   1.00 34.03 ? 71  ASP A OD2 1 
ATOM   609  N  N   . ASP A 1 72  ? 5.424  14.907  8.598   1.00 16.48 ? 72  ASP A N   1 
ATOM   610  C  CA  . ASP A 1 72  ? 5.264  15.307  9.995   1.00 16.00 ? 72  ASP A CA  1 
ATOM   611  C  C   . ASP A 1 72  ? 5.306  16.830  10.126  1.00 17.29 ? 72  ASP A C   1 
ATOM   612  O  O   . ASP A 1 72  ? 5.759  17.335  11.149  1.00 17.76 ? 72  ASP A O   1 
ATOM   613  C  CB  . ASP A 1 72  ? 6.383  14.648  10.841  1.00 17.87 ? 72  ASP A CB  1 
ATOM   614  C  CG  . ASP A 1 72  ? 7.776  15.151  10.507  1.00 19.87 ? 72  ASP A CG  1 
ATOM   615  O  OD1 . ASP A 1 72  ? 8.036  15.784  9.437   1.00 19.06 ? 72  ASP A OD1 1 
ATOM   616  O  OD2 . ASP A 1 72  ? 8.702  14.888  11.278  1.00 19.62 ? 72  ASP A OD2 1 
ATOM   617  N  N   . SER A 1 73  ? 4.897  17.520  9.064   1.00 18.21 ? 73  SER A N   1 
ATOM   618  C  CA  . SER A 1 73  ? 4.871  19.008  9.080   1.00 21.00 ? 73  SER A CA  1 
ATOM   619  C  C   . SER A 1 73  ? 3.591  19.580  9.704   1.00 23.24 ? 73  SER A C   1 
ATOM   620  O  O   . SER A 1 73  ? 3.501  20.804  9.964   1.00 18.08 ? 73  SER A O   1 
ATOM   621  C  CB  . SER A 1 73  ? 5.140  19.566  7.678   1.00 20.79 ? 73  SER A CB  1 
ATOM   622  O  OG  . SER A 1 73  ? 4.023  19.355  6.815   1.00 22.35 ? 73  SER A OG  1 
ATOM   623  N  N   . GLN A 1 74  ? 2.599  18.725  9.965   1.00 22.58 ? 74  GLN A N   1 
ATOM   624  C  CA  . GLN A 1 74  ? 1.359  19.178  10.622  1.00 26.43 ? 74  GLN A CA  1 
ATOM   625  C  C   . GLN A 1 74  ? 1.081  18.237  11.762  1.00 26.69 ? 74  GLN A C   1 
ATOM   626  O  O   . GLN A 1 74  ? 1.675  17.144  11.853  1.00 20.61 ? 74  GLN A O   1 
ATOM   627  C  CB  . GLN A 1 74  ? 0.165  19.179  9.646   1.00 25.12 ? 74  GLN A CB  1 
ATOM   628  C  CG  . GLN A 1 74  ? 0.225  20.277  8.566   1.00 33.70 ? 74  GLN A CG  1 
ATOM   629  C  CD  . GLN A 1 74  ? -0.725 19.998  7.403   1.00 35.59 ? 74  GLN A CD  1 
ATOM   630  O  OE1 . GLN A 1 74  ? -1.893 19.678  7.618   1.00 40.42 ? 74  GLN A OE1 1 
ATOM   631  N  NE2 . GLN A 1 74  ? -0.225 20.102  6.174   1.00 39.87 ? 74  GLN A NE2 1 
ATOM   632  N  N   . ASP A 1 75  ? 0.139  18.647  12.597  1.00 25.26 ? 75  ASP A N   1 
ATOM   633  C  CA  . ASP A 1 75  ? -0.263 17.893  13.754  1.00 27.58 ? 75  ASP A CA  1 
ATOM   634  C  C   . ASP A 1 75  ? -1.194 16.739  13.286  1.00 28.59 ? 75  ASP A C   1 
ATOM   635  O  O   . ASP A 1 75  ? -2.422 16.851  13.322  1.00 30.05 ? 75  ASP A O   1 
ATOM   636  C  CB  . ASP A 1 75  ? -0.919 18.915  14.703  1.00 31.33 ? 75  ASP A CB  1 
ATOM   637  C  CG  . ASP A 1 75  ? -1.663 18.294  15.852  1.00 38.83 ? 75  ASP A CG  1 
ATOM   638  O  OD1 . ASP A 1 75  ? -1.294 17.166  16.283  1.00 37.83 ? 75  ASP A OD1 1 
ATOM   639  O  OD2 . ASP A 1 75  ? -2.626 18.970  16.319  1.00 36.02 ? 75  ASP A OD2 1 
ATOM   640  N  N   . LYS A 1 76  ? -0.588 15.655  12.818  1.00 24.04 ? 76  LYS A N   1 
ATOM   641  C  CA  . LYS A 1 76  ? -1.283 14.453  12.327  1.00 27.01 ? 76  LYS A CA  1 
ATOM   642  C  C   . LYS A 1 76  ? -0.510 13.255  12.863  1.00 28.47 ? 76  LYS A C   1 
ATOM   643  O  O   . LYS A 1 76  ? 0.721  13.350  13.083  1.00 31.20 ? 76  LYS A O   1 
ATOM   644  C  CB  . LYS A 1 76  ? -1.188 14.365  10.816  1.00 26.43 ? 76  LYS A CB  1 
ATOM   645  C  CG  . LYS A 1 76  ? -2.146 15.309  10.127  1.00 30.02 ? 76  LYS A CG  1 
ATOM   646  C  CD  . LYS A 1 76  ? -1.709 15.549  8.718   1.00 32.07 ? 76  LYS A CD  1 
ATOM   647  C  CE  . LYS A 1 76  ? -2.866 16.180  7.955   1.00 36.57 ? 76  LYS A CE  1 
ATOM   648  N  NZ  . LYS A 1 76  ? -2.423 16.282  6.541   1.00 36.28 ? 76  LYS A NZ  1 
ATOM   649  N  N   . ALA A 1 77  ? -1.175 12.140  13.059  1.00 25.44 ? 77  ALA A N   1 
ATOM   650  C  CA  . ALA A 1 77  ? -0.478 10.917  13.554  1.00 23.24 ? 77  ALA A CA  1 
ATOM   651  C  C   . ALA A 1 77  ? 0.283  11.154  14.852  1.00 21.65 ? 77  ALA A C   1 
ATOM   652  O  O   . ALA A 1 77  ? 1.512  11.325  14.819  1.00 24.19 ? 77  ALA A O   1 
ATOM   653  C  CB  . ALA A 1 77  ? 0.447  10.307  12.490  1.00 23.39 ? 77  ALA A CB  1 
ATOM   654  N  N   . VAL A 1 78  ? -0.420 11.155  15.965  1.00 19.53 ? 78  VAL A N   1 
ATOM   655  C  CA  . VAL A 1 78  ? 0.214  11.476  17.262  1.00 20.82 ? 78  VAL A CA  1 
ATOM   656  C  C   . VAL A 1 78  ? 0.095  10.295  18.243  1.00 19.43 ? 78  VAL A C   1 
ATOM   657  O  O   . VAL A 1 78  ? -0.911 9.556   18.253  1.00 18.93 ? 78  VAL A O   1 
ATOM   658  C  CB  . VAL A 1 78  ? -0.368 12.778  17.874  1.00 25.00 ? 78  VAL A CB  1 
ATOM   659  C  CG1 . VAL A 1 78  ? -0.061 13.967  16.959  1.00 24.72 ? 78  VAL A CG1 1 
ATOM   660  C  CG2 . VAL A 1 78  ? -1.840 12.636  18.005  1.00 26.41 ? 78  VAL A CG2 1 
ATOM   661  N  N   . LEU A 1 79  ? 1.155  10.126  19.046  1.00 17.30 ? 79  LEU A N   1 
ATOM   662  C  CA  . LEU A 1 79  ? 1.126  9.258   20.180  1.00 16.44 ? 79  LEU A CA  1 
ATOM   663  C  C   . LEU A 1 79  ? 1.154  10.131  21.415  1.00 17.70 ? 79  LEU A C   1 
ATOM   664  O  O   . LEU A 1 79  ? 1.898  11.131  21.472  1.00 18.33 ? 79  LEU A O   1 
ATOM   665  C  CB  . LEU A 1 79  ? 2.341  8.346   20.096  1.00 15.43 ? 79  LEU A CB  1 
ATOM   666  C  CG  . LEU A 1 79  ? 2.533  7.321   21.161  1.00 17.73 ? 79  LEU A CG  1 
ATOM   667  C  CD1 . LEU A 1 79  ? 1.505  6.226   20.946  1.00 22.50 ? 79  LEU A CD1 1 
ATOM   668  C  CD2 . LEU A 1 79  ? 3.928  6.811   20.951  1.00 15.45 ? 79  LEU A CD2 1 
ATOM   669  N  N   . LYS A 1 80  ? 0.287  9.845   22.374  1.00 16.03 ? 80  LYS A N   1 
ATOM   670  C  CA  . LYS A 1 80  ? 0.319  10.525  23.645  1.00 17.97 ? 80  LYS A CA  1 
ATOM   671  C  C   . LYS A 1 80  ? -0.262 9.587   24.729  1.00 18.15 ? 80  LYS A C   1 
ATOM   672  O  O   . LYS A 1 80  ? -0.614 8.456   24.408  1.00 17.44 ? 80  LYS A O   1 
ATOM   673  C  CB  . LYS A 1 80  ? -0.455 11.881  23.573  1.00 21.40 ? 80  LYS A CB  1 
ATOM   674  C  CG  . LYS A 1 80  ? -1.981 11.704  23.505  1.00 26.82 ? 80  LYS A CG  1 
ATOM   675  C  CD  . LYS A 1 80  ? -2.746 13.026  23.332  1.00 30.09 ? 80  LYS A CD  1 
ATOM   676  C  CE  . LYS A 1 80  ? -2.549 13.537  21.923  1.00 38.79 ? 80  LYS A CE  1 
ATOM   677  N  NZ  . LYS A 1 80  ? -3.608 13.126  20.928  1.00 48.47 ? 80  LYS A NZ  1 
ATOM   678  N  N   . GLY A 1 81  ? -0.442 10.074  25.955  1.00 18.83 ? 81  GLY A N   1 
ATOM   679  C  CA  . GLY A 1 81  ? -0.976 9.251   27.033  1.00 21.16 ? 81  GLY A CA  1 
ATOM   680  C  C   . GLY A 1 81  ? 0.058  8.219   27.407  1.00 23.62 ? 81  GLY A C   1 
ATOM   681  O  O   . GLY A 1 81  ? 1.248  8.452   27.244  1.00 19.71 ? 81  GLY A O   1 
ATOM   682  N  N   . GLY A 1 82  ? -0.385 7.098   27.966  1.00 25.17 ? 82  GLY A N   1 
ATOM   683  C  CA  . GLY A 1 82  ? 0.571  6.157   28.533  1.00 25.00 ? 82  GLY A CA  1 
ATOM   684  C  C   . GLY A 1 82  ? 1.529  6.799   29.490  1.00 23.55 ? 82  GLY A C   1 
ATOM   685  O  O   . GLY A 1 82  ? 1.130  7.570   30.390  1.00 23.02 ? 82  GLY A O   1 
ATOM   686  N  N   . PRO A 1 83  ? 2.866  6.574   29.284  1.00 19.44 ? 83  PRO A N   1 
ATOM   687  C  CA  . PRO A 1 83  ? 3.815  7.189   30.151  1.00 18.31 ? 83  PRO A CA  1 
ATOM   688  C  C   . PRO A 1 83  ? 4.270  8.586   29.695  1.00 20.86 ? 83  PRO A C   1 
ATOM   689  O  O   . PRO A 1 83  ? 5.107  9.196   30.334  1.00 23.56 ? 83  PRO A O   1 
ATOM   690  C  CB  . PRO A 1 83  ? 5.058  6.274   29.988  1.00 21.47 ? 83  PRO A CB  1 
ATOM   691  C  CG  . PRO A 1 83  ? 4.998  5.942   28.479  1.00 19.00 ? 83  PRO A CG  1 
ATOM   692  C  CD  . PRO A 1 83  ? 3.499  5.698   28.249  1.00 18.99 ? 83  PRO A CD  1 
ATOM   693  N  N   . LEU A 1 84  ? 3.684  9.111   28.643  1.00 19.73 ? 84  LEU A N   1 
ATOM   694  C  CA  . LEU A 1 84  ? 4.285  10.302  27.991  1.00 18.41 ? 84  LEU A CA  1 
ATOM   695  C  C   . LEU A 1 84  ? 3.667  11.562  28.542  1.00 20.83 ? 84  LEU A C   1 
ATOM   696  O  O   . LEU A 1 84  ? 2.482  11.554  28.841  1.00 19.85 ? 84  LEU A O   1 
ATOM   697  C  CB  . LEU A 1 84  ? 3.989  10.245  26.523  1.00 17.08 ? 84  LEU A CB  1 
ATOM   698  C  CG  . LEU A 1 84  ? 4.528  8.975   25.832  1.00 17.33 ? 84  LEU A CG  1 
ATOM   699  C  CD1 . LEU A 1 84  ? 4.101  8.875   24.379  1.00 14.46 ? 84  LEU A CD1 1 
ATOM   700  C  CD2 . LEU A 1 84  ? 6.046  8.935   25.877  1.00 14.99 ? 84  LEU A CD2 1 
ATOM   701  N  N   A ASP A 1 85  ? 4.431  12.644  28.643  0.50 24.57 ? 85  ASP A N   1 
ATOM   702  N  N   B ASP A 1 85  ? 4.483  12.615  28.578  0.50 20.12 ? 85  ASP A N   1 
ATOM   703  C  CA  A ASP A 1 85  ? 3.822  13.877  29.196  0.50 27.76 ? 85  ASP A CA  1 
ATOM   704  C  CA  B ASP A 1 85  ? 4.006  13.970  28.902  0.50 20.63 ? 85  ASP A CA  1 
ATOM   705  C  C   A ASP A 1 85  ? 3.436  14.837  28.099  0.50 28.84 ? 85  ASP A C   1 
ATOM   706  C  C   B ASP A 1 85  ? 3.955  14.689  27.573  0.50 20.52 ? 85  ASP A C   1 
ATOM   707  O  O   A ASP A 1 85  ? 2.878  15.896  28.374  0.50 30.31 ? 85  ASP A O   1 
ATOM   708  O  O   B ASP A 1 85  ? 4.903  14.641  26.764  0.50 19.81 ? 85  ASP A O   1 
ATOM   709  C  CB  A ASP A 1 85  ? 4.711  14.579  30.227  0.50 33.02 ? 85  ASP A CB  1 
ATOM   710  C  CB  B ASP A 1 85  ? 4.938  14.687  29.899  0.50 22.39 ? 85  ASP A CB  1 
ATOM   711  C  CG  A ASP A 1 85  ? 3.935  14.956  31.502  0.50 38.41 ? 85  ASP A CG  1 
ATOM   712  C  CG  B ASP A 1 85  ? 4.902  14.051  31.316  0.50 24.35 ? 85  ASP A CG  1 
ATOM   713  O  OD1 A ASP A 1 85  ? 2.855  14.350  31.730  0.50 37.82 ? 85  ASP A OD1 1 
ATOM   714  O  OD1 B ASP A 1 85  ? 3.851  13.471  31.712  0.50 26.35 ? 85  ASP A OD1 1 
ATOM   715  O  OD2 A ASP A 1 85  ? 4.401  15.844  32.266  0.50 40.33 ? 85  ASP A OD2 1 
ATOM   716  O  OD2 B ASP A 1 85  ? 5.934  14.112  32.022  0.50 24.15 ? 85  ASP A OD2 1 
ATOM   717  N  N   A GLY A 1 86  ? 3.738  14.490  26.853  0.50 29.62 ? 86  GLY A N   1 
ATOM   718  N  N   B GLY A 1 86  ? 2.831  15.351  27.314  0.50 19.01 ? 86  GLY A N   1 
ATOM   719  C  CA  A GLY A 1 86  ? 3.399  15.389  25.767  0.50 26.67 ? 86  GLY A CA  1 
ATOM   720  C  CA  B GLY A 1 86  ? 2.702  16.083  26.072  0.50 17.46 ? 86  GLY A CA  1 
ATOM   721  C  C   A GLY A 1 86  ? 2.891  14.685  24.522  0.50 27.12 ? 86  GLY A C   1 
ATOM   722  C  C   B GLY A 1 86  ? 2.410  15.130  24.930  0.50 18.85 ? 86  GLY A C   1 
ATOM   723  O  O   A GLY A 1 86  ? 2.595  13.487  24.552  0.50 26.85 ? 86  GLY A O   1 
ATOM   724  O  O   B GLY A 1 86  ? 1.679  14.140  25.081  0.50 17.23 ? 86  GLY A O   1 
ATOM   725  N  N   A THR A 1 87  ? 2.756  15.462  23.443  0.50 24.60 ? 87  THR A N   1 
ATOM   726  N  N   B THR A 1 87  ? 3.007  15.412  23.770  0.50 18.29 ? 87  THR A N   1 
ATOM   727  C  CA  A THR A 1 87  ? 2.361  14.954  22.142  0.50 20.86 ? 87  THR A CA  1 
ATOM   728  C  CA  B THR A 1 87  ? 2.582  14.746  22.542  0.50 16.53 ? 87  THR A CA  1 
ATOM   729  C  C   A THR A 1 87  ? 3.595  14.609  21.319  0.50 18.62 ? 87  THR A C   1 
ATOM   730  C  C   B THR A 1 87  ? 3.734  14.504  21.570  0.50 16.38 ? 87  THR A C   1 
ATOM   731  O  O   A THR A 1 87  ? 4.464  15.439  21.104  0.50 17.38 ? 87  THR A O   1 
ATOM   732  O  O   B THR A 1 87  ? 4.642  15.316  21.451  0.50 14.43 ? 87  THR A O   1 
ATOM   733  C  CB  A THR A 1 87  ? 1.515  15.985  21.351  0.50 24.56 ? 87  THR A CB  1 
ATOM   734  C  CB  B THR A 1 87  ? 1.486  15.552  21.857  0.50 18.85 ? 87  THR A CB  1 
ATOM   735  O  OG1 A THR A 1 87  ? 0.228  16.151  21.979  0.50 25.58 ? 87  THR A OG1 1 
ATOM   736  O  OG1 B THR A 1 87  ? 2.032  16.803  21.396  0.50 16.77 ? 87  THR A OG1 1 
ATOM   737  C  CG2 A THR A 1 87  ? 1.325  15.504  19.921  0.50 23.67 ? 87  THR A CG2 1 
ATOM   738  C  CG2 B THR A 1 87  ? 0.333  15.792  22.856  0.50 17.20 ? 87  THR A CG2 1 
ATOM   739  N  N   . TYR A 1 88  ? 3.702  13.352  20.909  1.00 15.27 ? 88  TYR A N   1 
ATOM   740  C  CA  . TYR A 1 88  ? 4.803  12.940  20.033  1.00 13.90 ? 88  TYR A CA  1 
ATOM   741  C  C   . TYR A 1 88  ? 4.263  12.637  18.608  1.00 15.33 ? 88  TYR A C   1 
ATOM   742  O  O   . TYR A 1 88  ? 3.169  11.999  18.469  1.00 18.59 ? 88  TYR A O   1 
ATOM   743  C  CB  . TYR A 1 88  ? 5.446  11.689  20.584  1.00 12.36 ? 88  TYR A CB  1 
ATOM   744  C  CG  . TYR A 1 88  ? 6.208  11.864  21.905  1.00 12.79 ? 88  TYR A CG  1 
ATOM   745  C  CD1 . TYR A 1 88  ? 5.575  12.258  23.099  1.00 12.65 ? 88  TYR A CD1 1 
ATOM   746  C  CD2 . TYR A 1 88  ? 7.629  11.710  21.914  1.00 12.55 ? 88  TYR A CD2 1 
ATOM   747  C  CE1 . TYR A 1 88  ? 6.337  12.417  24.307  1.00 11.98 ? 88  TYR A CE1 1 
ATOM   748  C  CE2 . TYR A 1 88  ? 8.355  11.857  23.082  1.00 12.27 ? 88  TYR A CE2 1 
ATOM   749  C  CZ  . TYR A 1 88  ? 7.726  12.183  24.267  1.00 12.86 ? 88  TYR A CZ  1 
ATOM   750  O  OH  . TYR A 1 88  ? 8.451  12.268  25.394  1.00 14.15 ? 88  TYR A OH  1 
ATOM   751  N  N   . ARG A 1 89  ? 4.947  13.123  17.590  1.00 11.99 ? 89  ARG A N   1 
ATOM   752  C  CA  . ARG A 1 89  ? 4.444  13.090  16.226  1.00 12.25 ? 89  ARG A CA  1 
ATOM   753  C  C   . ARG A 1 89  ? 5.139  11.947  15.430  1.00 11.13 ? 89  ARG A C   1 
ATOM   754  O  O   . ARG A 1 89  ? 6.367  11.816  15.447  1.00 10.93 ? 89  ARG A O   1 
ATOM   755  C  CB  . ARG A 1 89  ? 4.554  14.485  15.598  1.00 15.46 ? 89  ARG A CB  1 
ATOM   756  C  CG  . ARG A 1 89  ? 3.949  14.552  14.203  1.00 17.13 ? 89  ARG A CG  1 
ATOM   757  C  CD  . ARG A 1 89  ? 4.089  15.990  13.691  1.00 18.77 ? 89  ARG A CD  1 
ATOM   758  N  NE  . ARG A 1 89  ? 3.403  16.942  14.558  1.00 19.99 ? 89  ARG A NE  1 
ATOM   759  C  CZ  . ARG A 1 89  ? 3.514  18.260  14.353  1.00 22.70 ? 89  ARG A CZ  1 
ATOM   760  N  NH1 . ARG A 1 89  ? 4.260  18.695  13.323  1.00 21.91 ? 89  ARG A NH1 1 
ATOM   761  N  NH2 . ARG A 1 89  ? 2.927  19.139  15.171  1.00 21.59 ? 89  ARG A NH2 1 
ATOM   762  N  N   . LEU A 1 90  ? 4.353  11.083  14.741  1.00 12.12 ? 90  LEU A N   1 
ATOM   763  C  CA  . LEU A 1 90  ? 4.997  10.029  13.905  1.00 11.32 ? 90  LEU A CA  1 
ATOM   764  C  C   . LEU A 1 90  ? 5.874  10.573  12.778  1.00 12.22 ? 90  LEU A C   1 
ATOM   765  O  O   . LEU A 1 90  ? 5.407  11.433  11.963  1.00 12.70 ? 90  LEU A O   1 
ATOM   766  C  CB  . LEU A 1 90  ? 3.866  9.126   13.308  1.00 12.84 ? 90  LEU A CB  1 
ATOM   767  C  CG  . LEU A 1 90  ? 4.326  7.994   12.401  1.00 13.02 ? 90  LEU A CG  1 
ATOM   768  C  CD1 . LEU A 1 90  ? 5.081  6.918   13.170  1.00 13.50 ? 90  LEU A CD1 1 
ATOM   769  C  CD2 . LEU A 1 90  ? 3.088  7.311   11.824  1.00 14.09 ? 90  LEU A CD2 1 
ATOM   770  N  N   . ILE A 1 91  ? 7.098  10.072  12.665  1.00 12.78 ? 91  ILE A N   1 
ATOM   771  C  CA  . ILE A 1 91  ? 7.967  10.486  11.551  1.00 13.01 ? 91  ILE A CA  1 
ATOM   772  C  C   . ILE A 1 91  ? 8.304  9.318   10.645  1.00 12.65 ? 91  ILE A C   1 
ATOM   773  O  O   . ILE A 1 91  ? 8.321  9.459   9.428   1.00 11.45 ? 91  ILE A O   1 
ATOM   774  C  CB  . ILE A 1 91  ? 9.274  11.221  11.990  1.00 15.10 ? 91  ILE A CB  1 
ATOM   775  C  CG1 . ILE A 1 91  ? 10.099 11.561  10.732  1.00 15.65 ? 91  ILE A CG1 1 
ATOM   776  C  CG2 . ILE A 1 91  ? 10.092 10.379  12.964  1.00 12.58 ? 91  ILE A CG2 1 
ATOM   777  C  CD1 . ILE A 1 91  ? 11.262 12.528  11.060  1.00 18.55 ? 91  ILE A CD1 1 
ATOM   778  N  N   . GLN A 1 92  ? 8.448  8.096   11.188  1.00 12.28 ? 92  GLN A N   1 
ATOM   779  C  CA  . GLN A 1 92  ? 8.828  6.965   10.269  1.00 11.83 ? 92  GLN A CA  1 
ATOM   780  C  C   . GLN A 1 92  ? 8.565  5.684   11.024  1.00 12.21 ? 92  GLN A C   1 
ATOM   781  O  O   . GLN A 1 92  ? 8.417  5.696   12.232  1.00 12.23 ? 92  GLN A O   1 
ATOM   782  C  CB  . GLN A 1 92  ? 10.302 6.976   9.796   1.00 14.42 ? 92  GLN A CB  1 
ATOM   783  C  CG  . GLN A 1 92  ? 11.295 6.952   10.956  1.00 15.04 ? 92  GLN A CG  1 
ATOM   784  C  CD  . GLN A 1 92  ? 12.039 5.632   11.002  1.00 18.69 ? 92  GLN A CD  1 
ATOM   785  O  OE1 . GLN A 1 92  ? 11.456 4.626   11.208  1.00 15.33 ? 92  GLN A OE1 1 
ATOM   786  N  NE2 . GLN A 1 92  ? 13.329 5.681   10.955  1.00 25.14 ? 92  GLN A NE2 1 
ATOM   787  N  N   . PHE A 1 93  ? 8.411  4.581   10.283  1.00 11.93 ? 93  PHE A N   1 
ATOM   788  C  CA  . PHE A 1 93  ? 8.519  3.264   10.919  1.00 11.03 ? 93  PHE A CA  1 
ATOM   789  C  C   . PHE A 1 93  ? 9.498  2.377   10.131  1.00 11.12 ? 93  PHE A C   1 
ATOM   790  O  O   . PHE A 1 93  ? 9.748  2.575   8.943   1.00 11.64 ? 93  PHE A O   1 
ATOM   791  C  CB  . PHE A 1 93  ? 7.178  2.572   11.150  1.00 10.95 ? 93  PHE A CB  1 
ATOM   792  C  CG  . PHE A 1 93  ? 6.496  2.126   9.865   1.00 13.13 ? 93  PHE A CG  1 
ATOM   793  C  CD1 . PHE A 1 93  ? 6.878  0.959   9.171   1.00 13.61 ? 93  PHE A CD1 1 
ATOM   794  C  CD2 . PHE A 1 93  ? 5.377  2.854   9.422   1.00 14.17 ? 93  PHE A CD2 1 
ATOM   795  C  CE1 . PHE A 1 93  ? 6.183  0.543   8.010   1.00 15.39 ? 93  PHE A CE1 1 
ATOM   796  C  CE2 . PHE A 1 93  ? 4.653  2.402   8.301   1.00 16.69 ? 93  PHE A CE2 1 
ATOM   797  C  CZ  . PHE A 1 93  ? 5.061  1.279   7.589   1.00 15.70 ? 93  PHE A CZ  1 
ATOM   798  N  N   . HIS A 1 94  ? 9.976  1.308   10.783  1.00 10.18 ? 94  HIS A N   1 
ATOM   799  C  CA  . HIS A 1 94  ? 10.888 0.346   10.191  1.00 10.51 ? 94  HIS A CA  1 
ATOM   800  C  C   . HIS A 1 94  ? 10.821 -0.888  11.046  1.00 11.14 ? 94  HIS A C   1 
ATOM   801  O  O   . HIS A 1 94  ? 10.102 -0.908  12.061  1.00 10.59 ? 94  HIS A O   1 
ATOM   802  C  CB  . HIS A 1 94  ? 12.312 0.868   10.173  1.00 10.76 ? 94  HIS A CB  1 
ATOM   803  C  CG  . HIS A 1 94  ? 12.840 1.137   11.556  1.00 11.18 ? 94  HIS A CG  1 
ATOM   804  N  ND1 . HIS A 1 94  ? 12.714 2.362   12.204  1.00 11.40 ? 94  HIS A ND1 1 
ATOM   805  C  CD2 . HIS A 1 94  ? 13.395 0.277   12.450  1.00 11.27 ? 94  HIS A CD2 1 
ATOM   806  C  CE1 . HIS A 1 94  ? 13.197 2.260   13.424  1.00 11.88 ? 94  HIS A CE1 1 
ATOM   807  N  NE2 . HIS A 1 94  ? 13.660 0.987   13.602  1.00 10.99 ? 94  HIS A NE2 1 
ATOM   808  N  N   . PHE A 1 95  ? 11.494 -1.937  10.556  1.00 10.10 ? 95  PHE A N   1 
ATOM   809  C  CA  . PHE A 1 95  ? 11.460 -3.209  11.223  1.00 9.48  ? 95  PHE A CA  1 
ATOM   810  C  C   . PHE A 1 95  ? 12.903 -3.660  11.364  1.00 8.88  ? 95  PHE A C   1 
ATOM   811  O  O   . PHE A 1 95  ? 13.862 -3.200  10.724  1.00 10.58 ? 95  PHE A O   1 
ATOM   812  C  CB  . PHE A 1 95  ? 10.785 -4.306  10.372  1.00 9.72  ? 95  PHE A CB  1 
ATOM   813  C  CG  . PHE A 1 95  ? 9.325  -4.030  10.070  1.00 9.76  ? 95  PHE A CG  1 
ATOM   814  C  CD1 . PHE A 1 95  ? 8.999  -3.126  9.045   1.00 11.29 ? 95  PHE A CD1 1 
ATOM   815  C  CD2 . PHE A 1 95  ? 8.313  -4.652  10.737  1.00 11.56 ? 95  PHE A CD2 1 
ATOM   816  C  CE1 . PHE A 1 95  ? 7.695  -2.863  8.679   1.00 11.12 ? 95  PHE A CE1 1 
ATOM   817  C  CE2 . PHE A 1 95  ? 6.969  -4.417  10.396  1.00 11.83 ? 95  PHE A CE2 1 
ATOM   818  C  CZ  . PHE A 1 95  ? 6.666  -3.506  9.321   1.00 12.33 ? 95  PHE A CZ  1 
ATOM   819  N  N   . HIS A 1 96  ? 13.025 -4.606  12.306  1.00 9.54  ? 96  HIS A N   1 
ATOM   820  C  CA  . HIS A 1 96  ? 14.206 -5.472  12.468  1.00 10.08 ? 96  HIS A CA  1 
ATOM   821  C  C   . HIS A 1 96  ? 13.822 -6.917  12.358  1.00 11.15 ? 96  HIS A C   1 
ATOM   822  O  O   . HIS A 1 96  ? 12.802 -7.264  12.877  1.00 11.87 ? 96  HIS A O   1 
ATOM   823  C  CB  . HIS A 1 96  ? 14.873 -5.222  13.841  1.00 10.40 ? 96  HIS A CB  1 
ATOM   824  C  CG  . HIS A 1 96  ? 15.213 -3.765  14.109  1.00 9.65  ? 96  HIS A CG  1 
ATOM   825  N  ND1 . HIS A 1 96  ? 16.467 -3.278  13.946  1.00 10.11 ? 96  HIS A ND1 1 
ATOM   826  C  CD2 . HIS A 1 96  ? 14.423 -2.726  14.518  1.00 10.70 ? 96  HIS A CD2 1 
ATOM   827  C  CE1 . HIS A 1 96  ? 16.475 -1.940  14.280  1.00 9.97  ? 96  HIS A CE1 1 
ATOM   828  N  NE2 . HIS A 1 96  ? 15.199 -1.608  14.596  1.00 9.71  ? 96  HIS A NE2 1 
ATOM   829  N  N   . TRP A 1 97  ? 14.623 -7.771  11.706  1.00 9.99  ? 97  TRP A N   1 
ATOM   830  C  CA  . TRP A 1 97  ? 14.190 -9.197  11.523  1.00 10.77 ? 97  TRP A CA  1 
ATOM   831  C  C   . TRP A 1 97  ? 15.342 -10.086 11.416  1.00 10.89 ? 97  TRP A C   1 
ATOM   832  O  O   . TRP A 1 97  ? 16.513 -9.640  11.274  1.00 11.31 ? 97  TRP A O   1 
ATOM   833  C  CB  . TRP A 1 97  ? 13.311 -9.332  10.271  1.00 11.22 ? 97  TRP A CB  1 
ATOM   834  C  CG  . TRP A 1 97  ? 13.957 -8.927  8.979   1.00 12.21 ? 97  TRP A CG  1 
ATOM   835  C  CD1 . TRP A 1 97  ? 14.665 -9.729  8.100   1.00 12.12 ? 97  TRP A CD1 1 
ATOM   836  C  CD2 . TRP A 1 97  ? 14.014 -7.579  8.409   1.00 11.79 ? 97  TRP A CD2 1 
ATOM   837  N  NE1 . TRP A 1 97  ? 15.084 -9.002  6.990   1.00 13.60 ? 97  TRP A NE1 1 
ATOM   838  C  CE2 . TRP A 1 97  ? 14.713 -7.683  7.140   1.00 13.13 ? 97  TRP A CE2 1 
ATOM   839  C  CE3 . TRP A 1 97  ? 13.541 -6.327  8.826   1.00 13.04 ? 97  TRP A CE3 1 
ATOM   840  C  CZ2 . TRP A 1 97  ? 14.921 -6.589  6.330   1.00 12.89 ? 97  TRP A CZ2 1 
ATOM   841  C  CZ3 . TRP A 1 97  ? 13.777 -5.201  7.947   1.00 13.20 ? 97  TRP A CZ3 1 
ATOM   842  C  CH2 . TRP A 1 97  ? 14.449 -5.341  6.756   1.00 13.94 ? 97  TRP A CH2 1 
ATOM   843  N  N   . GLY A 1 98  ? 15.062 -11.374 11.447  1.00 10.48 ? 98  GLY A N   1 
ATOM   844  C  CA  . GLY A 1 98  ? 16.132 -12.394 11.423  1.00 10.66 ? 98  GLY A CA  1 
ATOM   845  C  C   . GLY A 1 98  ? 16.309 -13.110 10.106  1.00 11.43 ? 98  GLY A C   1 
ATOM   846  O  O   . GLY A 1 98  ? 15.564 -12.899 9.149   1.00 12.50 ? 98  GLY A O   1 
ATOM   847  N  N   . SER A 1 99  ? 17.347 -13.935 10.120  1.00 12.42 ? 99  SER A N   1 
ATOM   848  C  CA  . SER A 1 99  ? 17.600 -14.909 9.020   1.00 13.49 ? 99  SER A CA  1 
ATOM   849  C  C   . SER A 1 99  ? 16.663 -16.145 9.121   1.00 16.12 ? 99  SER A C   1 
ATOM   850  O  O   . SER A 1 99  ? 16.577 -16.898 8.122   1.00 17.72 ? 99  SER A O   1 
ATOM   851  C  CB  . SER A 1 99  ? 19.069 -15.337 9.070   1.00 13.87 ? 99  SER A CB  1 
ATOM   852  O  OG  . SER A 1 99  ? 19.418 -15.943 10.301  1.00 15.37 ? 99  SER A OG  1 
ATOM   853  N  N   . LEU A 1 100 ? 16.039 -16.353 10.280  1.00 14.61 ? 100 LEU A N   1 
ATOM   854  C  CA  . LEU A 1 100 ? 15.189 -17.507 10.564  1.00 17.29 ? 100 LEU A CA  1 
ATOM   855  C  C   . LEU A 1 100 ? 14.060 -16.971 11.393  1.00 16.60 ? 100 LEU A C   1 
ATOM   856  O  O   . LEU A 1 100 ? 14.196 -15.984 12.122  1.00 16.66 ? 100 LEU A O   1 
ATOM   857  C  CB  . LEU A 1 100 ? 15.964 -18.498 11.511  1.00 20.77 ? 100 LEU A CB  1 
ATOM   858  C  CG  . LEU A 1 100 ? 17.335 -18.992 11.054  1.00 24.53 ? 100 LEU A CG  1 
ATOM   859  C  CD1 . LEU A 1 100 ? 18.071 -19.798 12.116  1.00 29.56 ? 100 LEU A CD1 1 
ATOM   860  C  CD2 . LEU A 1 100 ? 17.030 -19.888 9.855   1.00 24.88 ? 100 LEU A CD2 1 
ATOM   861  N  N   . ASP A 1 101 ? 12.922 -17.633 11.360  1.00 15.24 ? 101 ASP A N   1 
ATOM   862  C  CA  . ASP A 1 101 ? 11.815 -17.198 12.221  1.00 14.43 ? 101 ASP A CA  1 
ATOM   863  C  C   . ASP A 1 101 ? 12.102 -17.174 13.741  1.00 14.72 ? 101 ASP A C   1 
ATOM   864  O  O   . ASP A 1 101 ? 11.465 -16.445 14.458  1.00 16.55 ? 101 ASP A O   1 
ATOM   865  C  CB  . ASP A 1 101 ? 10.578 -18.095 12.015  1.00 14.13 ? 101 ASP A CB  1 
ATOM   866  C  CG  . ASP A 1 101 ? 10.090 -18.128 10.575  1.00 18.27 ? 101 ASP A CG  1 
ATOM   867  O  OD1 . ASP A 1 101 ? 10.525 -17.286 9.763   1.00 17.04 ? 101 ASP A OD1 1 
ATOM   868  O  OD2 . ASP A 1 101 ? 9.258  -19.006 10.256  1.00 21.59 ? 101 ASP A OD2 1 
ATOM   869  N  N   . GLY A 1 102 ? 13.062 -17.972 14.238  1.00 15.48 ? 102 GLY A N   1 
ATOM   870  C  CA  . GLY A 1 102 ? 13.344 -17.994 15.696  1.00 13.46 ? 102 GLY A CA  1 
ATOM   871  C  C   . GLY A 1 102 ? 14.148 -16.823 16.244  1.00 11.95 ? 102 GLY A C   1 
ATOM   872  O  O   . GLY A 1 102 ? 14.475 -16.800 17.433  1.00 14.79 ? 102 GLY A O   1 
ATOM   873  N  N   . GLN A 1 103 ? 14.425 -15.821 15.419  1.00 12.62 ? 103 GLN A N   1 
ATOM   874  C  CA  . GLN A 1 103 ? 15.125 -14.608 15.934  1.00 11.86 ? 103 GLN A CA  1 
ATOM   875  C  C   . GLN A 1 103 ? 14.805 -13.446 15.029  1.00 13.42 ? 103 GLN A C   1 
ATOM   876  O  O   . GLN A 1 103 ? 14.309 -13.621 13.922  1.00 13.24 ? 103 GLN A O   1 
ATOM   877  C  CB  . GLN A 1 103 ? 16.653 -14.872 15.935  1.00 13.00 ? 103 GLN A CB  1 
ATOM   878  C  CG  . GLN A 1 103 ? 17.251 -15.065 14.529  1.00 15.25 ? 103 GLN A CG  1 
ATOM   879  C  CD  . GLN A 1 103 ? 18.637 -15.651 14.629  1.00 18.42 ? 103 GLN A CD  1 
ATOM   880  O  OE1 . GLN A 1 103 ? 18.811 -16.583 15.415  1.00 24.35 ? 103 GLN A OE1 1 
ATOM   881  N  NE2 . GLN A 1 103 ? 19.609 -15.149 13.859  1.00 17.21 ? 103 GLN A NE2 1 
ATOM   882  N  N   . GLY A 1 104 ? 15.086 -12.233 15.514  1.00 13.86 ? 104 GLY A N   1 
ATOM   883  C  CA  . GLY A 1 104 ? 14.898 -11.052 14.689  1.00 11.54 ? 104 GLY A CA  1 
ATOM   884  C  C   . GLY A 1 104 ? 14.468 -9.895  15.547  1.00 11.89 ? 104 GLY A C   1 
ATOM   885  O  O   . GLY A 1 104 ? 14.720 -8.729  15.195  1.00 12.72 ? 104 GLY A O   1 
ATOM   886  N  N   . SER A 1 105 ? 13.829 -10.162 16.675  1.00 10.65 ? 105 SER A N   1 
ATOM   887  C  CA  . SER A 1 105 ? 13.349 -8.996  17.517  1.00 11.50 ? 105 SER A CA  1 
ATOM   888  C  C   . SER A 1 105 ? 14.547 -8.482  18.308  1.00 12.45 ? 105 SER A C   1 
ATOM   889  O  O   . SER A 1 105 ? 15.577 -9.187  18.503  1.00 11.32 ? 105 SER A O   1 
ATOM   890  C  CB  . SER A 1 105 ? 12.214 -9.391  18.394  1.00 12.33 ? 105 SER A CB  1 
ATOM   891  O  OG  . SER A 1 105 ? 12.600 -10.283 19.369  1.00 11.82 ? 105 SER A OG  1 
ATOM   892  N  N   . GLU A 1 106 ? 14.451 -7.207  18.639  1.00 11.67 ? 106 GLU A N   1 
ATOM   893  C  CA  . GLU A 1 106 ? 15.512 -6.548  19.449  1.00 12.78 ? 106 GLU A CA  1 
ATOM   894  C  C   . GLU A 1 106 ? 15.153 -6.721  20.936  1.00 11.45 ? 106 GLU A C   1 
ATOM   895  O  O   . GLU A 1 106 ? 15.902 -7.317  21.693  1.00 11.86 ? 106 GLU A O   1 
ATOM   896  C  CB  . GLU A 1 106 ? 15.619 -5.075  19.019  1.00 11.18 ? 106 GLU A CB  1 
ATOM   897  C  CG  . GLU A 1 106 ? 15.896 -4.956  17.523  1.00 13.57 ? 106 GLU A CG  1 
ATOM   898  C  CD  . GLU A 1 106 ? 16.663 -3.701  17.229  1.00 11.95 ? 106 GLU A CD  1 
ATOM   899  O  OE1 . GLU A 1 106 ? 16.076 -2.573  17.478  1.00 12.86 ? 106 GLU A OE1 1 
ATOM   900  O  OE2 . GLU A 1 106 ? 17.866 -3.797  16.888  1.00 14.46 ? 106 GLU A OE2 1 
ATOM   901  N  N   . HIS A 1 107 ? 13.954 -6.285  21.358  1.00 11.32 ? 107 HIS A N   1 
ATOM   902  C  CA  . HIS A 1 107 ? 13.507 -6.636  22.697  1.00 10.27 ? 107 HIS A CA  1 
ATOM   903  C  C   . HIS A 1 107 ? 13.186 -8.093  22.724  1.00 10.79 ? 107 HIS A C   1 
ATOM   904  O  O   . HIS A 1 107 ? 12.801 -8.678  21.708  1.00 11.33 ? 107 HIS A O   1 
ATOM   905  C  CB  . HIS A 1 107 ? 12.270 -5.824  23.074  1.00 10.42 ? 107 HIS A CB  1 
ATOM   906  C  CG  . HIS A 1 107 ? 12.595 -4.365  23.221  1.00 10.54 ? 107 HIS A CG  1 
ATOM   907  N  ND1 . HIS A 1 107 ? 12.538 -3.503  22.166  1.00 9.38  ? 107 HIS A ND1 1 
ATOM   908  C  CD2 . HIS A 1 107 ? 13.049 -3.645  24.310  1.00 11.79 ? 107 HIS A CD2 1 
ATOM   909  C  CE1 . HIS A 1 107 ? 12.999 -2.293  22.579  1.00 10.07 ? 107 HIS A CE1 1 
ATOM   910  N  NE2 . HIS A 1 107 ? 13.249 -2.362  23.876  1.00 10.24 ? 107 HIS A NE2 1 
ATOM   911  N  N   . THR A 1 108 ? 13.386 -8.697  23.894  1.00 10.82 ? 108 THR A N   1 
ATOM   912  C  CA  . THR A 1 108 ? 12.911 -10.054 24.139  1.00 11.40 ? 108 THR A CA  1 
ATOM   913  C  C   . THR A 1 108 ? 11.976 -10.072 25.358  1.00 12.83 ? 108 THR A C   1 
ATOM   914  O  O   . THR A 1 108 ? 11.914 -9.126  26.143  1.00 11.81 ? 108 THR A O   1 
ATOM   915  C  CB  . THR A 1 108 ? 14.122 -10.991 24.341  1.00 11.22 ? 108 THR A CB  1 
ATOM   916  O  OG1 . THR A 1 108 ? 14.988 -10.469 25.362  1.00 12.31 ? 108 THR A OG1 1 
ATOM   917  C  CG2 . THR A 1 108 ? 15.025 -11.028 23.106  1.00 11.31 ? 108 THR A CG2 1 
ATOM   918  N  N   . VAL A 1 109 ? 11.164 -11.133 25.488  1.00 13.29 ? 109 VAL A N   1 
ATOM   919  C  CA  . VAL A 1 109 ? 10.182 -11.181 26.576  1.00 12.88 ? 109 VAL A CA  1 
ATOM   920  C  C   . VAL A 1 109 ? 10.511 -12.468 27.363  1.00 12.50 ? 109 VAL A C   1 
ATOM   921  O  O   . VAL A 1 109 ? 10.400 -13.534 26.771  1.00 14.58 ? 109 VAL A O   1 
ATOM   922  C  CB  . VAL A 1 109 ? 8.753  -11.246 25.996  1.00 13.77 ? 109 VAL A CB  1 
ATOM   923  C  CG1 . VAL A 1 109 ? 7.714  -11.348 27.124  1.00 15.53 ? 109 VAL A CG1 1 
ATOM   924  C  CG2 . VAL A 1 109 ? 8.398  -10.005 25.146  1.00 12.37 ? 109 VAL A CG2 1 
ATOM   925  N  N   . ASP A 1 110 ? 10.982 -12.347 28.576  1.00 14.11 ? 110 ASP A N   1 
ATOM   926  C  CA  . ASP A 1 110 ? 11.547 -13.532 29.334  1.00 16.84 ? 110 ASP A CA  1 
ATOM   927  C  C   . ASP A 1 110 ? 12.452 -14.364 28.399  1.00 14.67 ? 110 ASP A C   1 
ATOM   928  O  O   . ASP A 1 110 ? 12.331 -15.623 28.320  1.00 17.03 ? 110 ASP A O   1 
ATOM   929  C  CB  . ASP A 1 110 ? 10.378 -14.334 29.894  1.00 18.47 ? 110 ASP A CB  1 
ATOM   930  C  CG  . ASP A 1 110 ? 9.512  -13.484 30.850  1.00 17.09 ? 110 ASP A CG  1 
ATOM   931  O  OD1 . ASP A 1 110 ? 10.099 -12.720 31.567  1.00 19.67 ? 110 ASP A OD1 1 
ATOM   932  O  OD2 . ASP A 1 110 ? 8.294  -13.652 30.872  1.00 20.16 ? 110 ASP A OD2 1 
ATOM   933  N  N   . LYS A 1 111 ? 13.384 -13.653 27.729  1.00 14.54 ? 111 LYS A N   1 
ATOM   934  C  CA  . LYS A 1 111 ? 14.419 -14.178 26.793  1.00 14.57 ? 111 LYS A CA  1 
ATOM   935  C  C   . LYS A 1 111 ? 13.862 -14.706 25.462  1.00 13.76 ? 111 LYS A C   1 
ATOM   936  O  O   . LYS A 1 111 ? 14.622 -15.148 24.605  1.00 14.57 ? 111 LYS A O   1 
ATOM   937  C  CB  . LYS A 1 111 ? 15.272 -15.250 27.497  1.00 17.81 ? 111 LYS A CB  1 
ATOM   938  C  CG  . LYS A 1 111 ? 15.830 -14.759 28.836  1.00 21.50 ? 111 LYS A CG  1 
ATOM   939  C  CD  . LYS A 1 111 ? 16.830 -13.651 28.562  1.00 26.32 ? 111 LYS A CD  1 
ATOM   940  C  CE  . LYS A 1 111 ? 17.651 -13.259 29.771  1.00 28.40 ? 111 LYS A CE  1 
ATOM   941  N  NZ  . LYS A 1 111 ? 19.038 -13.683 29.406  1.00 35.16 ? 111 LYS A NZ  1 
ATOM   942  N  N   . LYS A 1 112 ? 12.542 -14.680 25.294  1.00 12.79 ? 112 LYS A N   1 
ATOM   943  C  CA  . LYS A 1 112 ? 11.921 -15.078 24.027  1.00 14.21 ? 112 LYS A CA  1 
ATOM   944  C  C   . LYS A 1 112 ? 12.222 -14.029 22.931  1.00 14.86 ? 112 LYS A C   1 
ATOM   945  O  O   . LYS A 1 112 ? 11.962 -12.832 23.133  1.00 13.49 ? 112 LYS A O   1 
ATOM   946  C  CB  . LYS A 1 112 ? 10.383 -15.219 24.135  1.00 14.95 ? 112 LYS A CB  1 
ATOM   947  C  CG  . LYS A 1 112 ? 9.759  -15.524 22.764  1.00 16.27 ? 112 LYS A CG  1 
ATOM   948  C  CD  . LYS A 1 112 ? 8.225  -15.437 22.889  1.00 18.20 ? 112 LYS A CD  1 
ATOM   949  C  CE  . LYS A 1 112 ? 7.613  -15.601 21.489  1.00 20.84 ? 112 LYS A CE  1 
ATOM   950  N  NZ  . LYS A 1 112 ? 7.713  -17.010 21.044  1.00 20.09 ? 112 LYS A NZ  1 
ATOM   951  N  N   . LYS A 1 113 ? 12.767 -14.504 21.821  1.00 13.10 ? 113 LYS A N   1 
ATOM   952  C  CA  . LYS A 1 113 ? 12.998 -13.733 20.584  1.00 13.64 ? 113 LYS A CA  1 
ATOM   953  C  C   . LYS A 1 113 ? 11.846 -13.961 19.609  1.00 14.24 ? 113 LYS A C   1 
ATOM   954  O  O   . LYS A 1 113 ? 11.451 -15.097 19.299  1.00 13.95 ? 113 LYS A O   1 
ATOM   955  C  CB  . LYS A 1 113 ? 14.323 -14.152 19.903  1.00 13.94 ? 113 LYS A CB  1 
ATOM   956  C  CG  . LYS A 1 113 ? 15.534 -13.727 20.672  1.00 15.35 ? 113 LYS A CG  1 
ATOM   957  C  CD  . LYS A 1 113 ? 16.761 -14.338 20.009  1.00 16.86 ? 113 LYS A CD  1 
ATOM   958  C  CE  . LYS A 1 113 ? 17.956 -13.796 20.750  1.00 19.75 ? 113 LYS A CE  1 
ATOM   959  N  NZ  . LYS A 1 113 ? 19.144 -14.640 20.455  1.00 27.30 ? 113 LYS A NZ  1 
ATOM   960  N  N   . TYR A 1 114 ? 11.214 -12.878 19.154  1.00 14.22 ? 114 TYR A N   1 
ATOM   961  C  CA  . TYR A 1 114 ? 10.221 -12.975 18.121  1.00 11.56 ? 114 TYR A CA  1 
ATOM   962  C  C   . TYR A 1 114 ? 10.875 -12.860 16.694  1.00 10.87 ? 114 TYR A C   1 
ATOM   963  O  O   . TYR A 1 114 ? 12.122 -12.595 16.564  1.00 12.90 ? 114 TYR A O   1 
ATOM   964  C  CB  . TYR A 1 114 ? 9.185  -11.852 18.238  1.00 12.71 ? 114 TYR A CB  1 
ATOM   965  C  CG  . TYR A 1 114 ? 8.212  -12.047 19.390  1.00 11.37 ? 114 TYR A CG  1 
ATOM   966  C  CD1 . TYR A 1 114 ? 8.539  -11.652 20.681  1.00 13.89 ? 114 TYR A CD1 1 
ATOM   967  C  CD2 . TYR A 1 114 ? 6.974  -12.686 19.147  1.00 14.91 ? 114 TYR A CD2 1 
ATOM   968  C  CE1 . TYR A 1 114 ? 7.630  -11.829 21.736  1.00 16.60 ? 114 TYR A CE1 1 
ATOM   969  C  CE2 . TYR A 1 114 ? 6.079  -12.881 20.156  1.00 16.45 ? 114 TYR A CE2 1 
ATOM   970  C  CZ  . TYR A 1 114 ? 6.421  -12.461 21.450  1.00 16.76 ? 114 TYR A CZ  1 
ATOM   971  O  OH  . TYR A 1 114 ? 5.530  -12.655 22.484  1.00 21.46 ? 114 TYR A OH  1 
ATOM   972  N  N   . ALA A 1 115 ? 10.093 -13.148 15.618  1.00 11.44 ? 115 ALA A N   1 
ATOM   973  C  CA  . ALA A 1 115 ? 10.606 -13.217 14.231  1.00 11.86 ? 115 ALA A CA  1 
ATOM   974  C  C   . ALA A 1 115 ? 11.055 -11.833 13.737  1.00 11.59 ? 115 ALA A C   1 
ATOM   975  O  O   . ALA A 1 115 ? 11.908 -11.699 12.873  1.00 13.16 ? 115 ALA A O   1 
ATOM   976  C  CB  . ALA A 1 115 ? 9.519  -13.775 13.306  1.00 12.41 ? 115 ALA A CB  1 
ATOM   977  N  N   . ALA A 1 116 ? 10.431 -10.805 14.341  1.00 11.90 ? 116 ALA A N   1 
ATOM   978  C  CA  . ALA A 1 116 ? 10.723 -9.423  13.857  1.00 11.57 ? 116 ALA A CA  1 
ATOM   979  C  C   . ALA A 1 116 ? 10.165 -8.391  14.846  1.00 12.33 ? 116 ALA A C   1 
ATOM   980  O  O   . ALA A 1 116 ? 9.487  -8.811  15.778  1.00 10.96 ? 116 ALA A O   1 
ATOM   981  C  CB  . ALA A 1 116 ? 10.180 -9.161  12.436  1.00 11.67 ? 116 ALA A CB  1 
ATOM   982  N  N   . GLU A 1 117 ? 10.543 -7.112  14.732  1.00 11.62 ? 117 GLU A N   1 
ATOM   983  C  CA  . GLU A 1 117 ? 9.957  -6.107  15.629  1.00 10.96 ? 117 GLU A CA  1 
ATOM   984  C  C   . GLU A 1 117 ? 9.792  -4.901  14.763  1.00 11.51 ? 117 GLU A C   1 
ATOM   985  O  O   . GLU A 1 117 ? 10.720 -4.524  14.039  1.00 11.15 ? 117 GLU A O   1 
ATOM   986  C  CB  . GLU A 1 117 ? 10.890 -5.822  16.802  1.00 12.08 ? 117 GLU A CB  1 
ATOM   987  C  CG  . GLU A 1 117 ? 10.359 -4.932  17.931  1.00 11.81 ? 117 GLU A CG  1 
ATOM   988  C  CD  . GLU A 1 117 ? 11.346 -4.866  19.080  1.00 13.57 ? 117 GLU A CD  1 
ATOM   989  O  OE1 . GLU A 1 117 ? 12.008 -5.921  19.400  1.00 11.97 ? 117 GLU A OE1 1 
ATOM   990  O  OE2 . GLU A 1 117 ? 11.445 -3.758  19.678  1.00 14.09 ? 117 GLU A OE2 1 
ATOM   991  N  N   . LEU A 1 118 ? 8.616  -4.312  14.869  1.00 10.17 ? 118 LEU A N   1 
ATOM   992  C  CA  . LEU A 1 118 ? 8.224  -3.041  14.207  1.00 9.72  ? 118 LEU A CA  1 
ATOM   993  C  C   . LEU A 1 118 ? 8.459  -1.867  15.189  1.00 9.24  ? 118 LEU A C   1 
ATOM   994  O  O   . LEU A 1 118 ? 8.114  -1.977  16.343  1.00 9.25  ? 118 LEU A O   1 
ATOM   995  C  CB  . LEU A 1 118 ? 6.726  -3.093  13.843  1.00 9.20  ? 118 LEU A CB  1 
ATOM   996  C  CG  . LEU A 1 118 ? 6.024  -1.749  13.520  1.00 9.64  ? 118 LEU A CG  1 
ATOM   997  C  CD1 . LEU A 1 118 ? 6.595  -1.209  12.206  1.00 11.34 ? 118 LEU A CD1 1 
ATOM   998  C  CD2 . LEU A 1 118 ? 4.485  -2.100  13.395  1.00 10.16 ? 118 LEU A CD2 1 
ATOM   999  N  N   . HIS A 1 119 ? 9.096  -0.788  14.705  1.00 8.90  ? 119 HIS A N   1 
ATOM   1000 C  CA  . HIS A 1 119 ? 9.371  0.428   15.460  1.00 9.89  ? 119 HIS A CA  1 
ATOM   1001 C  C   . HIS A 1 119 ? 8.676  1.566   14.797  1.00 10.37 ? 119 HIS A C   1 
ATOM   1002 O  O   . HIS A 1 119 ? 8.999  1.853   13.617  1.00 11.01 ? 119 HIS A O   1 
ATOM   1003 C  CB  . HIS A 1 119 ? 10.897 0.693   15.516  1.00 9.37  ? 119 HIS A CB  1 
ATOM   1004 C  CG  . HIS A 1 119 ? 11.571 -0.319  16.474  1.00 9.25  ? 119 HIS A CG  1 
ATOM   1005 N  ND1 . HIS A 1 119 ? 12.887 -0.647  16.466  1.00 10.50 ? 119 HIS A ND1 1 
ATOM   1006 C  CD2 . HIS A 1 119 ? 10.973 -1.074  17.466  1.00 9.34  ? 119 HIS A CD2 1 
ATOM   1007 C  CE1 . HIS A 1 119 ? 13.133 -1.551  17.440  1.00 9.98  ? 119 HIS A CE1 1 
ATOM   1008 N  NE2 . HIS A 1 119 ? 11.949 -1.898  17.990  1.00 8.95  ? 119 HIS A NE2 1 
ATOM   1009 N  N   . LEU A 1 120 ? 7.683  2.200   15.491  1.00 10.29 ? 120 LEU A N   1 
ATOM   1010 C  CA  . LEU A 1 120 ? 7.013  3.446   15.008  1.00 10.13 ? 120 LEU A CA  1 
ATOM   1011 C  C   . LEU A 1 120 ? 7.611  4.588   15.797  1.00 9.62  ? 120 LEU A C   1 
ATOM   1012 O  O   . LEU A 1 120 ? 7.532  4.593   16.990  1.00 10.08 ? 120 LEU A O   1 
ATOM   1013 C  CB  . LEU A 1 120 ? 5.508  3.297   15.240  1.00 9.90  ? 120 LEU A CB  1 
ATOM   1014 C  CG  . LEU A 1 120 ? 4.915  2.224   14.317  1.00 12.54 ? 120 LEU A CG  1 
ATOM   1015 C  CD1 . LEU A 1 120 ? 4.013  1.330   15.155  1.00 14.85 ? 120 LEU A CD1 1 
ATOM   1016 C  CD2 . LEU A 1 120 ? 4.119  2.873   13.184  1.00 14.26 ? 120 LEU A CD2 1 
ATOM   1017 N  N   . VAL A 1 121 ? 8.354  5.442   15.077  1.00 10.56 ? 121 VAL A N   1 
ATOM   1018 C  CA  . VAL A 1 121 ? 9.226  6.442   15.746  1.00 9.77  ? 121 VAL A CA  1 
ATOM   1019 C  C   . VAL A 1 121 ? 8.491  7.785   15.776  1.00 9.27  ? 121 VAL A C   1 
ATOM   1020 O  O   . VAL A 1 121 ? 8.140  8.240   14.721  1.00 9.63  ? 121 VAL A O   1 
ATOM   1021 C  CB  . VAL A 1 121 ? 10.556 6.567   14.958  1.00 10.77 ? 121 VAL A CB  1 
ATOM   1022 C  CG1 . VAL A 1 121 ? 11.536 7.541   15.643  1.00 12.37 ? 121 VAL A CG1 1 
ATOM   1023 C  CG2 . VAL A 1 121 ? 11.253 5.186   14.781  1.00 10.48 ? 121 VAL A CG2 1 
ATOM   1024 N  N   . HIS A 1 122 ? 8.418  8.394   16.948  1.00 9.19  ? 122 HIS A N   1 
ATOM   1025 C  CA  . HIS A 1 122 ? 7.703  9.660   17.131  1.00 10.52 ? 122 HIS A CA  1 
ATOM   1026 C  C   . HIS A 1 122 ? 8.593  10.624  17.859  1.00 11.86 ? 122 HIS A C   1 
ATOM   1027 O  O   . HIS A 1 122 ? 9.302  10.248  18.756  1.00 11.10 ? 122 HIS A O   1 
ATOM   1028 C  CB  . HIS A 1 122 ? 6.423  9.493   17.956  1.00 12.57 ? 122 HIS A CB  1 
ATOM   1029 C  CG  . HIS A 1 122 ? 5.579  8.317   17.560  1.00 12.23 ? 122 HIS A CG  1 
ATOM   1030 N  ND1 . HIS A 1 122 ? 5.944  7.016   17.849  1.00 12.02 ? 122 HIS A ND1 1 
ATOM   1031 C  CD2 . HIS A 1 122 ? 4.314  8.251   16.984  1.00 13.25 ? 122 HIS A CD2 1 
ATOM   1032 C  CE1 . HIS A 1 122 ? 4.954  6.177   17.416  1.00 13.24 ? 122 HIS A CE1 1 
ATOM   1033 N  NE2 . HIS A 1 122 ? 3.959  6.924   16.877  1.00 13.01 ? 122 HIS A NE2 1 
ATOM   1034 N  N   . TRP A 1 123 ? 8.482  11.879  17.494  1.00 10.68 ? 123 TRP A N   1 
ATOM   1035 C  CA  . TRP A 1 123 ? 9.262  12.901  18.223  1.00 11.40 ? 123 TRP A CA  1 
ATOM   1036 C  C   . TRP A 1 123 ? 8.381  13.865  19.022  1.00 12.11 ? 123 TRP A C   1 
ATOM   1037 O  O   . TRP A 1 123 ? 7.258  14.225  18.658  1.00 13.61 ? 123 TRP A O   1 
ATOM   1038 C  CB  . TRP A 1 123 ? 10.173 13.683  17.296  1.00 12.17 ? 123 TRP A CB  1 
ATOM   1039 C  CG  . TRP A 1 123 ? 9.471  14.318  16.113  1.00 12.31 ? 123 TRP A CG  1 
ATOM   1040 C  CD1 . TRP A 1 123 ? 9.188  13.740  14.876  1.00 12.10 ? 123 TRP A CD1 1 
ATOM   1041 C  CD2 . TRP A 1 123 ? 8.943  15.691  16.021  1.00 13.86 ? 123 TRP A CD2 1 
ATOM   1042 N  NE1 . TRP A 1 123 ? 8.539  14.632  14.057  1.00 14.18 ? 123 TRP A NE1 1 
ATOM   1043 C  CE2 . TRP A 1 123 ? 8.362  15.820  14.682  1.00 14.37 ? 123 TRP A CE2 1 
ATOM   1044 C  CE3 . TRP A 1 123 ? 8.897  16.779  16.882  1.00 12.77 ? 123 TRP A CE3 1 
ATOM   1045 C  CZ2 . TRP A 1 123 ? 7.767  16.997  14.252  1.00 16.87 ? 123 TRP A CZ2 1 
ATOM   1046 C  CZ3 . TRP A 1 123 ? 8.295  17.959  16.438  1.00 14.24 ? 123 TRP A CZ3 1 
ATOM   1047 C  CH2 . TRP A 1 123 ? 7.744  18.064  15.155  1.00 14.78 ? 123 TRP A CH2 1 
ATOM   1048 N  N   . ASN A 1 124 ? 8.943  14.334  20.131  1.00 12.90 ? 124 ASN A N   1 
ATOM   1049 C  CA  . ASN A 1 124 ? 8.229  15.221  21.032  1.00 12.00 ? 124 ASN A CA  1 
ATOM   1050 C  C   . ASN A 1 124 ? 8.016  16.630  20.416  1.00 12.91 ? 124 ASN A C   1 
ATOM   1051 O  O   . ASN A 1 124 ? 8.986  17.339  20.119  1.00 14.05 ? 124 ASN A O   1 
ATOM   1052 C  CB  . ASN A 1 124 ? 9.059  15.284  22.312  1.00 13.75 ? 124 ASN A CB  1 
ATOM   1053 C  CG  . ASN A 1 124 ? 8.283  15.865  23.502  1.00 14.49 ? 124 ASN A CG  1 
ATOM   1054 O  OD1 . ASN A 1 124 ? 7.405  16.709  23.339  1.00 14.62 ? 124 ASN A OD1 1 
ATOM   1055 N  ND2 . ASN A 1 124 ? 8.604  15.397  24.703  1.00 16.02 ? 124 ASN A ND2 1 
ATOM   1056 N  N   . THR A 1 125 ? 6.740  17.024  20.281  1.00 15.36 ? 125 THR A N   1 
ATOM   1057 C  CA  . THR A 1 125 ? 6.431  18.253  19.524  1.00 17.50 ? 125 THR A CA  1 
ATOM   1058 C  C   . THR A 1 125 ? 7.009  19.462  20.296  1.00 17.41 ? 125 THR A C   1 
ATOM   1059 O  O   . THR A 1 125 ? 7.189  20.539  19.725  1.00 16.97 ? 125 THR A O   1 
ATOM   1060 C  CB  . THR A 1 125 ? 4.922  18.368  19.264  1.00 16.83 ? 125 THR A CB  1 
ATOM   1061 O  OG1 . THR A 1 125 ? 4.195  18.281  20.461  1.00 19.89 ? 125 THR A OG1 1 
ATOM   1062 C  CG2 . THR A 1 125 ? 4.460  17.196  18.415  1.00 19.68 ? 125 THR A CG2 1 
ATOM   1063 N  N   . LYS A 1 126 ? 7.244  19.248  21.694  1.00 14.94 ? 127 LYS A N   1 
ATOM   1064 C  CA  . LYS A 1 126 ? 7.836  20.435  22.409  1.00 16.37 ? 127 LYS A CA  1 
ATOM   1065 C  C   . LYS A 1 126 ? 9.185  20.911  21.862  1.00 17.63 ? 127 LYS A C   1 
ATOM   1066 O  O   . LYS A 1 126 ? 9.635  22.033  22.216  1.00 19.05 ? 127 LYS A O   1 
ATOM   1067 C  CB  . LYS A 1 126 ? 7.904  20.200  23.926  1.00 17.77 ? 127 LYS A CB  1 
ATOM   1068 C  CG  . LYS A 1 126 ? 9.086  19.397  24.396  1.00 19.49 ? 127 LYS A CG  1 
ATOM   1069 C  CD  . LYS A 1 126 ? 8.956  18.970  25.884  1.00 23.03 ? 127 LYS A CD  1 
ATOM   1070 C  CE  . LYS A 1 126 ? 9.616  19.988  26.823  1.00 29.69 ? 127 LYS A CE  1 
ATOM   1071 N  NZ  . LYS A 1 126 ? 9.301  19.745  28.279  1.00 32.55 ? 127 LYS A NZ  1 
ATOM   1072 N  N   . TYR A 1 127 ? 9.862  20.092  21.045  1.00 14.46 ? 128 TYR A N   1 
ATOM   1073 C  CA  . TYR A 1 127 ? 11.200 20.417  20.502  1.00 13.69 ? 128 TYR A CA  1 
ATOM   1074 C  C   . TYR A 1 127 ? 11.228 20.851  19.064  1.00 16.06 ? 128 TYR A C   1 
ATOM   1075 O  O   . TYR A 1 127 ? 12.328 21.032  18.526  1.00 15.64 ? 128 TYR A O   1 
ATOM   1076 C  CB  . TYR A 1 127 ? 12.192 19.287  20.702  1.00 13.89 ? 128 TYR A CB  1 
ATOM   1077 C  CG  . TYR A 1 127 ? 12.304 18.943  22.149  1.00 13.08 ? 128 TYR A CG  1 
ATOM   1078 C  CD1 . TYR A 1 127 ? 12.675 19.926  23.077  1.00 16.13 ? 128 TYR A CD1 1 
ATOM   1079 C  CD2 . TYR A 1 127 ? 12.070 17.682  22.617  1.00 14.68 ? 128 TYR A CD2 1 
ATOM   1080 C  CE1 . TYR A 1 127 ? 12.805 19.623  24.423  1.00 15.23 ? 128 TYR A CE1 1 
ATOM   1081 C  CE2 . TYR A 1 127 ? 12.183 17.365  23.953  1.00 15.08 ? 128 TYR A CE2 1 
ATOM   1082 C  CZ  . TYR A 1 127 ? 12.574 18.380  24.863  1.00 15.91 ? 128 TYR A CZ  1 
ATOM   1083 O  OH  . TYR A 1 127 ? 12.689 18.027  26.162  1.00 16.31 ? 128 TYR A OH  1 
ATOM   1084 N  N   . GLY A 1 128 ? 10.056 20.934  18.466  1.00 15.58 ? 129 GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 128 ? 9.849  21.661  17.196  1.00 15.82 ? 129 GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 128 ? 10.135 20.825  15.983  1.00 17.67 ? 129 GLY A C   1 
ATOM   1087 O  O   . GLY A 1 128 ? 9.417  20.960  14.990  1.00 19.01 ? 129 GLY A O   1 
ATOM   1088 N  N   . ASP A 1 129 ? 11.128 19.941  16.072  1.00 16.41 ? 130 ASP A N   1 
ATOM   1089 C  CA  . ASP A 1 129 ? 11.303 19.011  14.962  1.00 17.71 ? 130 ASP A CA  1 
ATOM   1090 C  C   . ASP A 1 129 ? 12.070 17.800  15.440  1.00 18.70 ? 130 ASP A C   1 
ATOM   1091 O  O   . ASP A 1 129 ? 12.557 17.755  16.580  1.00 16.04 ? 130 ASP A O   1 
ATOM   1092 C  CB  . ASP A 1 129 ? 11.866 19.638  13.684  1.00 20.97 ? 130 ASP A CB  1 
ATOM   1093 C  CG  . ASP A 1 129 ? 13.322 20.058  13.799  1.00 23.30 ? 130 ASP A CG  1 
ATOM   1094 O  OD1 . ASP A 1 129 ? 13.965 19.873  14.858  1.00 25.75 ? 130 ASP A OD1 1 
ATOM   1095 O  OD2 . ASP A 1 129 ? 13.819 20.593  12.788  1.00 23.59 ? 130 ASP A OD2 1 
ATOM   1096 N  N   . PHE A 1 130 ? 12.190 16.831  14.551  1.00 17.52 ? 131 PHE A N   1 
ATOM   1097 C  CA  . PHE A 1 130 ? 12.874 15.619  14.897  1.00 18.34 ? 131 PHE A CA  1 
ATOM   1098 C  C   . PHE A 1 130 ? 14.350 15.839  15.231  1.00 16.53 ? 131 PHE A C   1 
ATOM   1099 O  O   . PHE A 1 130 ? 14.910 15.242  16.181  1.00 16.18 ? 131 PHE A O   1 
ATOM   1100 C  CB  . PHE A 1 130 ? 12.766 14.633  13.700  1.00 15.61 ? 131 PHE A CB  1 
ATOM   1101 C  CG  . PHE A 1 130 ? 13.567 13.365  13.880  1.00 18.38 ? 131 PHE A CG  1 
ATOM   1102 C  CD1 . PHE A 1 130 ? 13.006 12.285  14.523  1.00 18.27 ? 131 PHE A CD1 1 
ATOM   1103 C  CD2 . PHE A 1 130 ? 14.865 13.289  13.413  1.00 21.19 ? 131 PHE A CD2 1 
ATOM   1104 C  CE1 . PHE A 1 130 ? 13.741 11.121  14.718  1.00 20.55 ? 131 PHE A CE1 1 
ATOM   1105 C  CE2 . PHE A 1 130 ? 15.624 12.116  13.570  1.00 20.77 ? 131 PHE A CE2 1 
ATOM   1106 C  CZ  . PHE A 1 130 ? 15.047 11.058  14.235  1.00 21.35 ? 131 PHE A CZ  1 
ATOM   1107 N  N   . GLY A 1 131 ? 15.009 16.641  14.408  1.00 17.68 ? 132 GLY A N   1 
ATOM   1108 C  CA  . GLY A 1 131 ? 16.467 16.816  14.605  1.00 17.77 ? 132 GLY A CA  1 
ATOM   1109 C  C   . GLY A 1 131 ? 16.855 17.426  15.958  1.00 16.79 ? 132 GLY A C   1 
ATOM   1110 O  O   . GLY A 1 131 ? 17.866 17.046  16.540  1.00 22.48 ? 132 GLY A O   1 
ATOM   1111 N  N   . LYS A 1 132 ? 16.075 18.397  16.436  1.00 17.10 ? 133 LYS A N   1 
ATOM   1112 C  CA  . LYS A 1 132 ? 16.258 18.887  17.808  1.00 19.08 ? 133 LYS A CA  1 
ATOM   1113 C  C   . LYS A 1 132 ? 15.816 17.896  18.872  1.00 19.35 ? 133 LYS A C   1 
ATOM   1114 O  O   . LYS A 1 132 ? 16.485 17.751  19.909  1.00 20.34 ? 133 LYS A O   1 
ATOM   1115 C  CB  . LYS A 1 132 ? 15.510 20.186  17.985  1.00 22.87 ? 133 LYS A CB  1 
ATOM   1116 C  CG  . LYS A 1 132 ? 16.070 21.340  17.165  1.00 27.87 ? 133 LYS A CG  1 
ATOM   1117 C  CD  . LYS A 1 132 ? 17.601 21.415  17.202  1.00 32.74 ? 133 LYS A CD  1 
ATOM   1118 C  CE  . LYS A 1 132 ? 18.095 21.613  18.646  1.00 36.22 ? 133 LYS A CE  1 
ATOM   1119 N  NZ  . LYS A 1 132 ? 18.301 23.026  19.048  1.00 38.48 ? 133 LYS A NZ  1 
ATOM   1120 N  N   . ALA A 1 133 ? 14.675 17.222  18.621  1.00 16.19 ? 134 ALA A N   1 
ATOM   1121 C  CA  . ALA A 1 133 ? 14.177 16.287  19.629  1.00 16.40 ? 134 ALA A CA  1 
ATOM   1122 C  C   . ALA A 1 133 ? 15.212 15.171  19.950  1.00 15.26 ? 134 ALA A C   1 
ATOM   1123 O  O   . ALA A 1 133 ? 15.332 14.756  21.117  1.00 15.29 ? 134 ALA A O   1 
ATOM   1124 C  CB  . ALA A 1 133 ? 12.823 15.662  19.171  1.00 14.13 ? 134 ALA A CB  1 
ATOM   1125 N  N   . VAL A 1 134 ? 15.956 14.650  18.953  1.00 15.01 ? 135 VAL A N   1 
ATOM   1126 C  CA  . VAL A 1 134 ? 16.870 13.523  19.239  1.00 18.69 ? 135 VAL A CA  1 
ATOM   1127 C  C   . VAL A 1 134 ? 18.043 13.921  20.141  1.00 17.49 ? 135 VAL A C   1 
ATOM   1128 O  O   . VAL A 1 134 ? 18.757 13.066  20.640  1.00 16.75 ? 135 VAL A O   1 
ATOM   1129 C  CB  . VAL A 1 134 ? 17.409 12.791  17.969  1.00 19.65 ? 135 VAL A CB  1 
ATOM   1130 C  CG1 . VAL A 1 134 ? 16.228 12.279  17.181  1.00 22.09 ? 135 VAL A CG1 1 
ATOM   1131 C  CG2 . VAL A 1 134 ? 18.383 13.650  17.137  1.00 20.22 ? 135 VAL A CG2 1 
ATOM   1132 N  N   A GLN A 1 135 ? 18.227 15.220  20.355  0.50 17.10 ? 136 GLN A N   1 
ATOM   1133 N  N   B GLN A 1 135 ? 18.163 15.220  20.403  0.50 16.60 ? 136 GLN A N   1 
ATOM   1134 C  CA  A GLN A 1 135 ? 19.309 15.637  21.232  0.50 18.19 ? 136 GLN A CA  1 
ATOM   1135 C  CA  B GLN A 1 135 ? 19.233 15.732  21.250  0.50 17.54 ? 136 GLN A CA  1 
ATOM   1136 C  C   A GLN A 1 135 ? 18.762 15.944  22.660  0.50 17.63 ? 136 GLN A C   1 
ATOM   1137 C  C   B GLN A 1 135 ? 18.817 15.743  22.733  0.50 17.17 ? 136 GLN A C   1 
ATOM   1138 O  O   A GLN A 1 135 ? 19.412 16.632  23.468  0.50 17.83 ? 136 GLN A O   1 
ATOM   1139 O  O   B GLN A 1 135 ? 19.591 16.021  23.648  0.50 18.52 ? 136 GLN A O   1 
ATOM   1140 C  CB  A GLN A 1 135 ? 20.174 16.772  20.601  0.50 18.74 ? 136 GLN A CB  1 
ATOM   1141 C  CB  B GLN A 1 135 ? 19.662 17.109  20.735  0.50 17.61 ? 136 GLN A CB  1 
ATOM   1142 C  CG  A GLN A 1 135 ? 20.739 16.562  19.165  0.50 22.22 ? 136 GLN A CG  1 
ATOM   1143 C  CG  B GLN A 1 135 ? 20.075 17.047  19.279  0.50 21.02 ? 136 GLN A CG  1 
ATOM   1144 C  CD  A GLN A 1 135 ? 21.739 15.391  18.925  0.50 24.04 ? 136 GLN A CD  1 
ATOM   1145 C  CD  B GLN A 1 135 ? 20.582 18.353  18.745  0.50 22.29 ? 136 GLN A CD  1 
ATOM   1146 O  OE1 A GLN A 1 135 ? 22.651 15.120  19.719  0.50 26.90 ? 136 GLN A OE1 1 
ATOM   1147 O  OE1 B GLN A 1 135 ? 21.505 18.922  19.292  0.50 26.44 ? 136 GLN A OE1 1 
ATOM   1148 N  NE2 A GLN A 1 135 ? 21.584 14.721  17.786  0.50 23.95 ? 136 GLN A NE2 1 
ATOM   1149 N  NE2 B GLN A 1 135 ? 19.994 18.822  17.663  0.50 27.73 ? 136 GLN A NE2 1 
ATOM   1150 N  N   . GLN A 1 136 ? 17.555 15.438  22.966  1.00 17.17 ? 137 GLN A N   1 
ATOM   1151 C  CA  . GLN A 1 136 ? 16.968 15.595  24.321  1.00 16.24 ? 137 GLN A CA  1 
ATOM   1152 C  C   . GLN A 1 136 ? 16.647 14.300  24.950  1.00 15.56 ? 137 GLN A C   1 
ATOM   1153 O  O   . GLN A 1 136 ? 16.200 13.348  24.290  1.00 13.94 ? 137 GLN A O   1 
ATOM   1154 C  CB  . GLN A 1 136 ? 15.664 16.389  24.219  1.00 17.97 ? 137 GLN A CB  1 
ATOM   1155 C  CG  . GLN A 1 136 ? 15.707 17.610  23.302  1.00 19.91 ? 137 GLN A CG  1 
ATOM   1156 C  CD  . GLN A 1 136 ? 16.716 18.646  23.764  1.00 24.95 ? 137 GLN A CD  1 
ATOM   1157 O  OE1 . GLN A 1 136 ? 17.020 18.731  24.953  1.00 23.32 ? 137 GLN A OE1 1 
ATOM   1158 N  NE2 . GLN A 1 136 ? 17.282 19.409  22.801  1.00 29.08 ? 137 GLN A NE2 1 
ATOM   1159 N  N   . PRO A 1 137 ? 16.665 14.230  26.270  1.00 15.37 ? 138 PRO A N   1 
ATOM   1160 C  CA  . PRO A 1 137 ? 16.480 12.927  26.934  1.00 18.29 ? 138 PRO A CA  1 
ATOM   1161 C  C   . PRO A 1 137 ? 15.065 12.347  26.807  1.00 17.04 ? 138 PRO A C   1 
ATOM   1162 O  O   . PRO A 1 137 ? 14.885 11.117  26.951  1.00 16.82 ? 138 PRO A O   1 
ATOM   1163 C  CB  . PRO A 1 137 ? 16.755 13.233  28.391  1.00 19.78 ? 138 PRO A CB  1 
ATOM   1164 C  CG  . PRO A 1 137 ? 17.512 14.504  28.364  1.00 22.67 ? 138 PRO A CG  1 
ATOM   1165 C  CD  . PRO A 1 137 ? 17.010 15.307  27.218  1.00 20.52 ? 138 PRO A CD  1 
ATOM   1166 N  N   . ASP A 1 138 ? 14.073 13.213  26.551  1.00 15.70 ? 139 ASP A N   1 
ATOM   1167 C  CA  . ASP A 1 138 ? 12.673 12.784  26.320  1.00 15.29 ? 139 ASP A CA  1 
ATOM   1168 C  C   . ASP A 1 138 ? 12.235 13.140  24.878  1.00 14.13 ? 139 ASP A C   1 
ATOM   1169 O  O   . ASP A 1 138 ? 11.085 13.551  24.680  1.00 14.41 ? 139 ASP A O   1 
ATOM   1170 C  CB  . ASP A 1 138 ? 11.721 13.417  27.306  1.00 16.61 ? 139 ASP A CB  1 
ATOM   1171 C  CG  . ASP A 1 138 ? 11.838 14.939  27.341  1.00 15.05 ? 139 ASP A CG  1 
ATOM   1172 O  OD1 . ASP A 1 138 ? 12.796 15.538  26.752  1.00 18.22 ? 139 ASP A OD1 1 
ATOM   1173 O  OD2 . ASP A 1 138 ? 10.912 15.536  27.953  1.00 18.56 ? 139 ASP A OD2 1 
ATOM   1174 N  N   . GLY A 1 139 ? 13.171 13.121  23.926  1.00 13.74 ? 140 GLY A N   1 
ATOM   1175 C  CA  . GLY A 1 139 ? 12.903 13.649  22.582  1.00 12.03 ? 140 GLY A CA  1 
ATOM   1176 C  C   . GLY A 1 139 ? 12.071 12.678  21.746  1.00 11.27 ? 140 GLY A C   1 
ATOM   1177 O  O   . GLY A 1 139 ? 11.311 13.135  20.943  1.00 11.30 ? 140 GLY A O   1 
ATOM   1178 N  N   . LEU A 1 140 ? 12.259 11.352  21.956  1.00 10.55 ? 141 LEU A N   1 
ATOM   1179 C  CA  . LEU A 1 140 ? 11.542 10.401  21.117  1.00 10.01 ? 141 LEU A CA  1 
ATOM   1180 C  C   . LEU A 1 140 ? 10.665 9.446   21.951  1.00 10.44 ? 141 LEU A C   1 
ATOM   1181 O  O   . LEU A 1 140 ? 10.947 9.143   23.117  1.00 11.16 ? 141 LEU A O   1 
ATOM   1182 C  CB  . LEU A 1 140 ? 12.531 9.498   20.331  1.00 11.54 ? 141 LEU A CB  1 
ATOM   1183 C  CG  . LEU A 1 140 ? 13.397 10.180  19.322  1.00 13.28 ? 141 LEU A CG  1 
ATOM   1184 C  CD1 . LEU A 1 140 ? 14.101 9.131   18.428  1.00 14.59 ? 141 LEU A CD1 1 
ATOM   1185 C  CD2 . LEU A 1 140 ? 12.665 11.142  18.371  1.00 15.66 ? 141 LEU A CD2 1 
ATOM   1186 N  N   . ALA A 1 141 ? 9.632  8.949   21.294  1.00 11.18 ? 142 ALA A N   1 
ATOM   1187 C  CA  . ALA A 1 141 ? 8.879  7.821   21.847  1.00 9.85  ? 142 ALA A CA  1 
ATOM   1188 C  C   . ALA A 1 141 ? 8.812  6.827   20.710  1.00 10.39 ? 142 ALA A C   1 
ATOM   1189 O  O   . ALA A 1 141 ? 8.374  7.124   19.616  1.00 11.65 ? 142 ALA A O   1 
ATOM   1190 C  CB  . ALA A 1 141 ? 7.487  8.184   22.356  1.00 10.61 ? 142 ALA A CB  1 
ATOM   1191 N  N   . VAL A 1 142 ? 9.313  5.613   20.989  1.00 10.43 ? 143 VAL A N   1 
ATOM   1192 C  CA  . VAL A 1 142 ? 9.264  4.577   19.963  1.00 10.19 ? 143 VAL A CA  1 
ATOM   1193 C  C   . VAL A 1 142 ? 8.284  3.485   20.399  1.00 10.30 ? 143 VAL A C   1 
ATOM   1194 O  O   . VAL A 1 142 ? 8.414  2.921   21.489  1.00 10.27 ? 143 VAL A O   1 
ATOM   1195 C  CB  . VAL A 1 142 ? 10.654 4.009   19.620  1.00 11.29 ? 143 VAL A CB  1 
ATOM   1196 C  CG1 . VAL A 1 142 ? 10.544 2.955   18.486  1.00 13.10 ? 143 VAL A CG1 1 
ATOM   1197 C  CG2 . VAL A 1 142 ? 11.525 5.161   19.138  1.00 11.51 ? 143 VAL A CG2 1 
ATOM   1198 N  N   . LEU A 1 143 ? 7.293  3.190   19.556  1.00 10.36 ? 144 LEU A N   1 
ATOM   1199 C  CA  . LEU A 1 143 ? 6.293  2.147   19.876  1.00 9.93  ? 144 LEU A CA  1 
ATOM   1200 C  C   . LEU A 1 143 ? 6.848  0.898   19.206  1.00 10.21 ? 144 LEU A C   1 
ATOM   1201 O  O   . LEU A 1 143 ? 6.976  0.884   17.968  1.00 9.85  ? 144 LEU A O   1 
ATOM   1202 C  CB  . LEU A 1 143 ? 4.904  2.589   19.321  1.00 12.17 ? 144 LEU A CB  1 
ATOM   1203 C  CG  . LEU A 1 143 ? 3.749  1.617   19.425  1.00 12.13 ? 144 LEU A CG  1 
ATOM   1204 C  CD1 . LEU A 1 143 ? 3.509  1.249   20.879  1.00 11.83 ? 144 LEU A CD1 1 
ATOM   1205 C  CD2 . LEU A 1 143 ? 2.497  2.270   18.834  1.00 13.89 ? 144 LEU A CD2 1 
ATOM   1206 N  N   . GLY A 1 144 ? 7.090  -0.154  19.999  1.00 10.24 ? 145 GLY A N   1 
ATOM   1207 C  CA  . GLY A 1 144 ? 7.586  -1.401  19.413  1.00 8.69  ? 145 GLY A CA  1 
ATOM   1208 C  C   . GLY A 1 144 ? 6.527  -2.477  19.479  1.00 8.83  ? 145 GLY A C   1 
ATOM   1209 O  O   . GLY A 1 144 ? 5.825  -2.579  20.464  1.00 10.35 ? 145 GLY A O   1 
ATOM   1210 N  N   . ILE A 1 145 ? 6.457  -3.225  18.404  1.00 9.47  ? 146 ILE A N   1 
ATOM   1211 C  CA  . ILE A 1 145 ? 5.417  -4.265  18.251  1.00 9.42  ? 146 ILE A CA  1 
ATOM   1212 C  C   . ILE A 1 145 ? 6.135  -5.497  17.741  1.00 9.65  ? 146 ILE A C   1 
ATOM   1213 O  O   . ILE A 1 145 ? 6.743  -5.450  16.694  1.00 10.56 ? 146 ILE A O   1 
ATOM   1214 C  CB  . ILE A 1 145 ? 4.352  -3.788  17.232  1.00 9.79  ? 146 ILE A CB  1 
ATOM   1215 C  CG1 . ILE A 1 145 ? 3.775  -2.488  17.725  1.00 11.00 ? 146 ILE A CG1 1 
ATOM   1216 C  CG2 . ILE A 1 145 ? 3.298  -4.894  17.061  1.00 11.02 ? 146 ILE A CG2 1 
ATOM   1217 C  CD1 . ILE A 1 145 ? 2.723  -1.911  16.773  1.00 11.04 ? 146 ILE A CD1 1 
ATOM   1218 N  N   . PHE A 1 146 ? 5.905  -6.622  18.426  1.00 10.94 ? 147 PHE A N   1 
ATOM   1219 C  CA  . PHE A 1 146 ? 6.566  -7.875  17.977  1.00 11.11 ? 147 PHE A CA  1 
ATOM   1220 C  C   . PHE A 1 146 ? 5.791  -8.521  16.832  1.00 11.56 ? 147 PHE A C   1 
ATOM   1221 O  O   . PHE A 1 146 ? 4.539  -8.409  16.802  1.00 11.94 ? 147 PHE A O   1 
ATOM   1222 C  CB  . PHE A 1 146 ? 6.576  -8.808  19.156  1.00 11.56 ? 147 PHE A CB  1 
ATOM   1223 C  CG  . PHE A 1 146 ? 7.410  -8.349  20.300  1.00 9.93  ? 147 PHE A CG  1 
ATOM   1224 C  CD1 . PHE A 1 146 ? 8.805  -8.226  20.129  1.00 11.52 ? 147 PHE A CD1 1 
ATOM   1225 C  CD2 . PHE A 1 146 ? 6.864  -8.128  21.563  1.00 13.00 ? 147 PHE A CD2 1 
ATOM   1226 C  CE1 . PHE A 1 146 ? 9.610  -7.872  21.201  1.00 10.79 ? 147 PHE A CE1 1 
ATOM   1227 C  CE2 . PHE A 1 146 ? 7.657  -7.721  22.631  1.00 11.97 ? 147 PHE A CE2 1 
ATOM   1228 C  CZ  . PHE A 1 146 ? 9.049  -7.611  22.453  1.00 11.88 ? 147 PHE A CZ  1 
ATOM   1229 N  N   . LEU A 1 147 ? 6.521  -9.182  15.959  1.00 11.01 ? 148 LEU A N   1 
ATOM   1230 C  CA  . LEU A 1 147 ? 5.919  -9.997  14.908  1.00 10.88 ? 148 LEU A CA  1 
ATOM   1231 C  C   . LEU A 1 147 ? 6.194  -11.451 15.161  1.00 11.56 ? 148 LEU A C   1 
ATOM   1232 O  O   . LEU A 1 147 ? 7.349  -11.839 15.311  1.00 12.57 ? 148 LEU A O   1 
ATOM   1233 C  CB  . LEU A 1 147 ? 6.465  -9.640  13.528  1.00 11.18 ? 148 LEU A CB  1 
ATOM   1234 C  CG  . LEU A 1 147 ? 5.963  -8.317  12.857  1.00 11.29 ? 148 LEU A CG  1 
ATOM   1235 C  CD1 . LEU A 1 147 ? 6.175  -7.004  13.718  1.00 13.55 ? 148 LEU A CD1 1 
ATOM   1236 C  CD2 . LEU A 1 147 ? 6.453  -8.150  11.434  1.00 12.23 ? 148 LEU A CD2 1 
ATOM   1237 N  N   . LYS A 1 148 ? 5.151  -12.283 15.049  1.00 12.41 ? 149 LYS A N   1 
ATOM   1238 C  CA  . LYS A 1 148 ? 5.383  -13.732 15.003  1.00 13.79 ? 149 LYS A CA  1 
ATOM   1239 C  C   . LYS A 1 148 ? 4.902  -14.244 13.644  1.00 13.03 ? 149 LYS A C   1 
ATOM   1240 O  O   . LYS A 1 148 ? 4.107  -13.587 12.961  1.00 13.92 ? 149 LYS A O   1 
ATOM   1241 C  CB  . LYS A 1 148 ? 4.606  -14.442 16.139  1.00 16.81 ? 149 LYS A CB  1 
ATOM   1242 C  CG  . LYS A 1 148 ? 3.104  -14.416 15.999  1.00 19.20 ? 149 LYS A CG  1 
ATOM   1243 C  CD  . LYS A 1 148 ? 2.580  -15.138 17.240  1.00 26.89 ? 149 LYS A CD  1 
ATOM   1244 C  CE  . LYS A 1 148 ? 1.083  -14.965 17.354  1.00 32.18 ? 149 LYS A CE  1 
ATOM   1245 N  NZ  . LYS A 1 148 ? 0.498  -16.198 17.972  1.00 43.72 ? 149 LYS A NZ  1 
ATOM   1246 N  N   . VAL A 1 149 ? 5.359  -15.428 13.234  1.00 12.78 ? 150 VAL A N   1 
ATOM   1247 C  CA  . VAL A 1 149 ? 4.966  -15.969 11.928  1.00 13.12 ? 150 VAL A CA  1 
ATOM   1248 C  C   . VAL A 1 149 ? 3.784  -16.888 12.102  1.00 14.11 ? 150 VAL A C   1 
ATOM   1249 O  O   . VAL A 1 149 ? 3.814  -17.822 12.956  1.00 16.07 ? 150 VAL A O   1 
ATOM   1250 C  CB  . VAL A 1 149 ? 6.137  -16.783 11.363  1.00 14.72 ? 150 VAL A CB  1 
ATOM   1251 C  CG1 . VAL A 1 149 ? 5.721  -17.644 10.138  1.00 14.74 ? 150 VAL A CG1 1 
ATOM   1252 C  CG2 . VAL A 1 149 ? 7.206  -15.814 10.978  1.00 13.11 ? 150 VAL A CG2 1 
ATOM   1253 N  N   . GLY A 1 150 ? 2.746  -16.635 11.314  1.00 13.98 ? 151 GLY A N   1 
ATOM   1254 C  CA  . GLY A 1 150 ? 1.478  -17.351 11.490  1.00 16.24 ? 151 GLY A CA  1 
ATOM   1255 C  C   . GLY A 1 150 ? 0.607  -16.921 10.348  1.00 16.19 ? 151 GLY A C   1 
ATOM   1256 O  O   . GLY A 1 150 ? 1.007  -17.041 9.205   1.00 17.08 ? 151 GLY A O   1 
ATOM   1257 N  N   A SER A 1 151 ? -0.581 -16.405 10.669  0.50 17.23 ? 152 SER A N   1 
ATOM   1258 N  N   B SER A 1 151 ? -0.573 -16.397 10.677  0.50 16.96 ? 152 SER A N   1 
ATOM   1259 C  CA  A SER A 1 151 ? -1.463 -15.863 9.636   0.50 17.63 ? 152 SER A CA  1 
ATOM   1260 C  CA  B SER A 1 151 ? -1.493 -15.852 9.679   0.50 17.20 ? 152 SER A CA  1 
ATOM   1261 C  C   A SER A 1 151 ? -0.827 -14.594 9.075   0.50 17.88 ? 152 SER A C   1 
ATOM   1262 C  C   B SER A 1 151 ? -0.919 -14.547 9.121   0.50 17.52 ? 152 SER A C   1 
ATOM   1263 O  O   A SER A 1 151 ? -0.008 -13.948 9.736   0.50 17.62 ? 152 SER A O   1 
ATOM   1264 O  O   B SER A 1 151 ? -0.233 -13.817 9.854   0.50 17.26 ? 152 SER A O   1 
ATOM   1265 C  CB  A SER A 1 151 ? -2.862 -15.556 10.169  0.50 20.01 ? 152 SER A CB  1 
ATOM   1266 C  CB  B SER A 1 151 ? -2.834 -15.563 10.323  0.50 19.26 ? 152 SER A CB  1 
ATOM   1267 O  OG  A SER A 1 151 ? -2.908 -14.350 10.913  0.50 20.85 ? 152 SER A OG  1 
ATOM   1268 O  OG  B SER A 1 151 ? -3.385 -16.740 10.893  0.50 19.42 ? 152 SER A OG  1 
ATOM   1269 N  N   . ALA A 1 152 ? -1.181 -14.276 7.836   1.00 17.58 ? 153 ALA A N   1 
ATOM   1270 C  CA  . ALA A 1 152 ? -0.758 -13.027 7.197   1.00 15.37 ? 153 ALA A CA  1 
ATOM   1271 C  C   . ALA A 1 152 ? -1.367 -11.820 7.888   1.00 15.12 ? 153 ALA A C   1 
ATOM   1272 O  O   . ALA A 1 152 ? -2.460 -11.921 8.430   1.00 17.71 ? 153 ALA A O   1 
ATOM   1273 C  CB  . ALA A 1 152 ? -1.115 -13.012 5.711   1.00 17.22 ? 153 ALA A CB  1 
ATOM   1274 N  N   . LYS A 1 153 ? -0.641 -10.702 7.836   1.00 15.43 ? 154 LYS A N   1 
ATOM   1275 C  CA  . LYS A 1 153 ? -1.179 -9.415  8.275   1.00 15.69 ? 154 LYS A CA  1 
ATOM   1276 C  C   . LYS A 1 153 ? -1.556 -8.649  6.975   1.00 15.65 ? 154 LYS A C   1 
ATOM   1277 O  O   . LYS A 1 153 ? -0.669 -8.183  6.231   1.00 15.28 ? 154 LYS A O   1 
ATOM   1278 C  CB  . LYS A 1 153 ? -0.104 -8.649  9.079   1.00 14.79 ? 154 LYS A CB  1 
ATOM   1279 C  CG  . LYS A 1 153 ? -0.719 -7.442  9.804   1.00 17.60 ? 154 LYS A CG  1 
ATOM   1280 C  CD  . LYS A 1 153 ? -1.692 -7.846  10.902  1.00 18.69 ? 154 LYS A CD  1 
ATOM   1281 C  CE  . LYS A 1 153 ? -1.887 -6.694  11.898  1.00 22.15 ? 154 LYS A CE  1 
ATOM   1282 N  NZ  . LYS A 1 153 ? -3.011 -7.032  12.768  1.00 24.75 ? 154 LYS A NZ  1 
ATOM   1283 N  N   . PRO A 1 154 ? -2.899 -8.502  6.718   1.00 16.10 ? 155 PRO A N   1 
ATOM   1284 C  CA  . PRO A 1 154 ? -3.346 -7.922  5.433   1.00 15.73 ? 155 PRO A CA  1 
ATOM   1285 C  C   . PRO A 1 154 ? -2.827 -6.533  5.273   1.00 15.64 ? 155 PRO A C   1 
ATOM   1286 O  O   . PRO A 1 154 ? -2.366 -6.167  4.206   1.00 17.50 ? 155 PRO A O   1 
ATOM   1287 C  CB  . PRO A 1 154 ? -4.907 -7.955  5.560   1.00 17.38 ? 155 PRO A CB  1 
ATOM   1288 C  CG  . PRO A 1 154 ? -5.181 -9.131  6.474   1.00 19.43 ? 155 PRO A CG  1 
ATOM   1289 C  CD  . PRO A 1 154 ? -4.041 -9.061  7.485   1.00 16.98 ? 155 PRO A CD  1 
ATOM   1290 N  N   . GLY A 1 155 ? -2.797 -5.803  6.379   1.00 16.58 ? 156 GLY A N   1 
ATOM   1291 C  CA  . GLY A 1 155 ? -2.326 -4.403  6.345   1.00 17.75 ? 156 GLY A CA  1 
ATOM   1292 C  C   . GLY A 1 155 ? -0.871 -4.176  6.108   1.00 19.25 ? 156 GLY A C   1 
ATOM   1293 O  O   . GLY A 1 155 ? -0.434 -3.037  5.840   1.00 23.47 ? 156 GLY A O   1 
ATOM   1294 N  N   . LEU A 1 156 ? -0.089 -5.256  6.199   1.00 15.02 ? 157 LEU A N   1 
ATOM   1295 C  CA  . LEU A 1 156 ? 1.357  -5.240  5.867   1.00 14.77 ? 157 LEU A CA  1 
ATOM   1296 C  C   . LEU A 1 156 ? 1.664  -5.438  4.384   1.00 13.82 ? 157 LEU A C   1 
ATOM   1297 O  O   . LEU A 1 156 ? 2.787  -5.204  3.890   1.00 14.33 ? 157 LEU A O   1 
ATOM   1298 C  CB  . LEU A 1 156 ? 2.115  -6.271  6.716   1.00 14.46 ? 157 LEU A CB  1 
ATOM   1299 C  CG  . LEU A 1 156 ? 3.671  -6.418  6.545   1.00 13.99 ? 157 LEU A CG  1 
ATOM   1300 C  CD1 . LEU A 1 156 ? 4.397  -5.062  6.832   1.00 14.98 ? 157 LEU A CD1 1 
ATOM   1301 C  CD2 . LEU A 1 156 ? 4.271  -7.543  7.430   1.00 12.94 ? 157 LEU A CD2 1 
ATOM   1302 N  N   . GLN A 1 157 ? 0.703  -6.005  3.646   1.00 16.05 ? 158 GLN A N   1 
ATOM   1303 C  CA  . GLN A 1 157 ? 0.988  -6.443  2.272   1.00 17.30 ? 158 GLN A CA  1 
ATOM   1304 C  C   . GLN A 1 157 ? 1.455  -5.334  1.335   1.00 17.13 ? 158 GLN A C   1 
ATOM   1305 O  O   . GLN A 1 157 ? 2.366  -5.550  0.522   1.00 16.83 ? 158 GLN A O   1 
ATOM   1306 C  CB  . GLN A 1 157 ? -0.190 -7.277  1.747   1.00 20.78 ? 158 GLN A CB  1 
ATOM   1307 C  CG  . GLN A 1 157 ? 0.182  -8.009  0.493   1.00 19.68 ? 158 GLN A CG  1 
ATOM   1308 C  CD  . GLN A 1 157 ? 1.277  -9.027  0.740   1.00 19.78 ? 158 GLN A CD  1 
ATOM   1309 O  OE1 . GLN A 1 157 ? 1.351  -9.624  1.827   1.00 20.49 ? 158 GLN A OE1 1 
ATOM   1310 N  NE2 . GLN A 1 157 ? 2.152  -9.228  -0.252  1.00 21.39 ? 158 GLN A NE2 1 
ATOM   1311 N  N   A LYS A 1 158 ? 0.915  -4.110  1.466   0.50 17.73 ? 159 LYS A N   1 
ATOM   1312 N  N   B LYS A 1 158 ? 0.896  -4.135  1.509   0.50 17.92 ? 159 LYS A N   1 
ATOM   1313 C  CA  A LYS A 1 158 ? 1.360  -2.999  0.599   0.50 17.70 ? 159 LYS A CA  1 
ATOM   1314 C  CA  B LYS A 1 158 ? 1.275  -3.021  0.661   0.50 18.02 ? 159 LYS A CA  1 
ATOM   1315 C  C   A LYS A 1 158 ? 2.838  -2.758  0.785   0.50 17.36 ? 159 LYS A C   1 
ATOM   1316 C  C   B LYS A 1 158 ? 2.740  -2.649  0.827   0.50 17.69 ? 159 LYS A C   1 
ATOM   1317 O  O   A LYS A 1 158 ? 3.585  -2.518  -0.153  0.50 17.55 ? 159 LYS A O   1 
ATOM   1318 O  O   B LYS A 1 158 ? 3.376  -2.212  -0.107  0.50 17.97 ? 159 LYS A O   1 
ATOM   1319 C  CB  A LYS A 1 158 ? 0.530  -1.705  0.862   0.50 19.90 ? 159 LYS A CB  1 
ATOM   1320 C  CB  B LYS A 1 158 ? 0.295  -1.833  0.861   0.50 20.03 ? 159 LYS A CB  1 
ATOM   1321 C  CG  A LYS A 1 158 ? 0.907  -0.480  0.018   0.50 21.61 ? 159 LYS A CG  1 
ATOM   1322 C  CG  B LYS A 1 158 ? -1.056 -2.071  0.199   0.50 21.81 ? 159 LYS A CG  1 
ATOM   1323 C  CD  A LYS A 1 158 ? 0.052  0.740   0.404   0.50 23.21 ? 159 LYS A CD  1 
ATOM   1324 C  CD  B LYS A 1 158 ? -1.969 -0.873  0.360   0.50 24.74 ? 159 LYS A CD  1 
ATOM   1325 C  CE  A LYS A 1 158 ? 0.480  2.054   -0.266  0.50 21.74 ? 159 LYS A CE  1 
ATOM   1326 C  CE  B LYS A 1 158 ? -3.407 -1.153  -0.093  0.50 25.59 ? 159 LYS A CE  1 
ATOM   1327 N  NZ  A LYS A 1 158 ? 0.111  2.027   -1.721  0.50 22.03 ? 159 LYS A NZ  1 
ATOM   1328 N  NZ  B LYS A 1 158 ? -4.260 0.081   -0.118  0.50 25.36 ? 159 LYS A NZ  1 
ATOM   1329 N  N   . VAL A 1 159 ? 3.281  -2.851  2.041   1.00 16.72 ? 160 VAL A N   1 
ATOM   1330 C  CA  . VAL A 1 159 ? 4.711  -2.686  2.293   1.00 14.77 ? 160 VAL A CA  1 
ATOM   1331 C  C   . VAL A 1 159 ? 5.486  -3.830  1.615   1.00 16.61 ? 160 VAL A C   1 
ATOM   1332 O  O   . VAL A 1 159 ? 6.458  -3.591  0.950   1.00 15.48 ? 160 VAL A O   1 
ATOM   1333 C  CB  . VAL A 1 159 ? 5.013  -2.670  3.819   1.00 15.68 ? 160 VAL A CB  1 
ATOM   1334 C  CG1 . VAL A 1 159 ? 6.517  -2.769  4.085   1.00 18.11 ? 160 VAL A CG1 1 
ATOM   1335 C  CG2 . VAL A 1 159 ? 4.443  -1.382  4.434   1.00 17.75 ? 160 VAL A CG2 1 
ATOM   1336 N  N   . VAL A 1 160 ? 5.064  -5.082  1.823   1.00 16.66 ? 161 VAL A N   1 
ATOM   1337 C  CA  . VAL A 1 160 ? 5.846  -6.194  1.292   1.00 17.65 ? 161 VAL A CA  1 
ATOM   1338 C  C   . VAL A 1 160 ? 5.857  -6.113  -0.243  1.00 16.93 ? 161 VAL A C   1 
ATOM   1339 O  O   . VAL A 1 160 ? 6.873  -6.289  -0.843  1.00 16.79 ? 161 VAL A O   1 
ATOM   1340 C  CB  . VAL A 1 160 ? 5.194  -7.567  1.692   1.00 18.37 ? 161 VAL A CB  1 
ATOM   1341 C  CG1 . VAL A 1 160 ? 5.701  -8.695  0.780   1.00 20.02 ? 161 VAL A CG1 1 
ATOM   1342 C  CG2 . VAL A 1 160 ? 5.417  -7.850  3.174   1.00 18.97 ? 161 VAL A CG2 1 
ATOM   1343 N  N   . ASP A 1 161 ? 4.753  -5.698  -0.845  1.00 18.05 ? 162 ASP A N   1 
ATOM   1344 C  CA  . ASP A 1 161 ? 4.746  -5.586  -2.304  1.00 21.89 ? 162 ASP A CA  1 
ATOM   1345 C  C   . ASP A 1 161 ? 5.713  -4.544  -2.936  1.00 21.73 ? 162 ASP A C   1 
ATOM   1346 O  O   . ASP A 1 161 ? 6.164  -4.703  -4.054  1.00 24.50 ? 162 ASP A O   1 
ATOM   1347 C  CB  . ASP A 1 161 ? 3.291  -5.399  -2.733  1.00 26.38 ? 162 ASP A CB  1 
ATOM   1348 C  CG  . ASP A 1 161 ? 2.546  -6.744  -2.751  1.00 27.38 ? 162 ASP A CG  1 
ATOM   1349 O  OD1 . ASP A 1 161 ? 3.206  -7.798  -2.872  1.00 29.15 ? 162 ASP A OD1 1 
ATOM   1350 O  OD2 . ASP A 1 161 ? 1.308  -6.745  -2.639  1.00 32.47 ? 162 ASP A OD2 1 
ATOM   1351 N  N   . VAL A 1 162 ? 6.032  -3.468  -2.220  1.00 19.51 ? 163 VAL A N   1 
ATOM   1352 C  CA  . VAL A 1 162 ? 6.944  -2.461  -2.794  1.00 21.19 ? 163 VAL A CA  1 
ATOM   1353 C  C   . VAL A 1 162 ? 8.417  -2.806  -2.595  1.00 18.63 ? 163 VAL A C   1 
ATOM   1354 O  O   . VAL A 1 162 ? 9.301  -2.175  -3.136  1.00 19.19 ? 163 VAL A O   1 
ATOM   1355 C  CB  . VAL A 1 162 ? 6.580  -1.090  -2.152  1.00 21.25 ? 163 VAL A CB  1 
ATOM   1356 C  CG1 . VAL A 1 162 ? 7.389  -0.825  -0.905  1.00 21.71 ? 163 VAL A CG1 1 
ATOM   1357 C  CG2 . VAL A 1 162 ? 6.812  0.067   -3.108  1.00 24.59 ? 163 VAL A CG2 1 
ATOM   1358 N  N   . LEU A 1 163 ? 8.762  -3.808  -1.760  1.00 18.32 ? 164 LEU A N   1 
ATOM   1359 C  CA  . LEU A 1 163 ? 10.187 -4.103  -1.456  1.00 17.25 ? 164 LEU A CA  1 
ATOM   1360 C  C   . LEU A 1 163 ? 11.101 -4.435  -2.656  1.00 20.80 ? 164 LEU A C   1 
ATOM   1361 O  O   . LEU A 1 163 ? 12.298 -4.149  -2.623  1.00 18.17 ? 164 LEU A O   1 
ATOM   1362 C  CB  . LEU A 1 163 ? 10.330 -5.165  -0.334  1.00 15.36 ? 164 LEU A CB  1 
ATOM   1363 C  CG  . LEU A 1 163 ? 9.649  -4.892  1.018   1.00 16.11 ? 164 LEU A CG  1 
ATOM   1364 C  CD1 . LEU A 1 163 ? 10.066 -5.997  2.002   1.00 15.16 ? 164 LEU A CD1 1 
ATOM   1365 C  CD2 . LEU A 1 163 ? 10.085 -3.534  1.543   1.00 17.55 ? 164 LEU A CD2 1 
ATOM   1366 N  N   . ASP A 1 164 ? 10.515 -5.058  -3.692  1.00 24.98 ? 165 ASP A N   1 
ATOM   1367 C  CA  . ASP A 1 164 ? 11.331 -5.428  -4.830  1.00 29.78 ? 165 ASP A CA  1 
ATOM   1368 C  C   . ASP A 1 164 ? 11.817 -4.166  -5.596  1.00 29.02 ? 165 ASP A C   1 
ATOM   1369 O  O   . ASP A 1 164 ? 12.868 -4.218  -6.232  1.00 30.61 ? 165 ASP A O   1 
ATOM   1370 C  CB  . ASP A 1 164 ? 10.582 -6.418  -5.724  1.00 37.42 ? 165 ASP A CB  1 
ATOM   1371 C  CG  . ASP A 1 164 ? 9.604  -5.734  -6.644  1.00 47.20 ? 165 ASP A CG  1 
ATOM   1372 O  OD1 . ASP A 1 164 ? 8.517  -5.293  -6.187  1.00 50.67 ? 165 ASP A OD1 1 
ATOM   1373 O  OD2 . ASP A 1 164 ? 9.946  -5.596  -7.848  1.00 54.52 ? 165 ASP A OD2 1 
ATOM   1374 N  N   . SER A 1 165 ? 11.094 -3.052  -5.446  1.00 25.54 ? 166 SER A N   1 
ATOM   1375 C  CA  . SER A 1 165 ? 11.521 -1.765  -6.003  1.00 25.84 ? 166 SER A CA  1 
ATOM   1376 C  C   . SER A 1 165 ? 12.604 -1.020  -5.177  1.00 24.19 ? 166 SER A C   1 
ATOM   1377 O  O   . SER A 1 165 ? 13.206 -0.028  -5.659  1.00 23.15 ? 166 SER A O   1 
ATOM   1378 C  CB  . SER A 1 165 ? 10.289 -0.887  -6.174  1.00 25.73 ? 166 SER A CB  1 
ATOM   1379 O  OG  . SER A 1 165 ? 9.910  -0.351  -4.915  1.00 26.79 ? 166 SER A OG  1 
ATOM   1380 N  N   . ILE A 1 166 ? 12.886 -1.469  -3.931  1.00 18.76 ? 167 ILE A N   1 
ATOM   1381 C  CA  . ILE A 1 166 ? 13.960 -0.872  -3.144  1.00 18.95 ? 167 ILE A CA  1 
ATOM   1382 C  C   . ILE A 1 166 ? 14.932 -1.917  -2.642  1.00 18.39 ? 167 ILE A C   1 
ATOM   1383 O  O   . ILE A 1 166 ? 15.294 -1.931  -1.463  1.00 20.47 ? 167 ILE A O   1 
ATOM   1384 C  CB  . ILE A 1 166 ? 13.410 -0.029  -1.941  1.00 18.48 ? 167 ILE A CB  1 
ATOM   1385 C  CG1 . ILE A 1 166 ? 12.444 -0.862  -1.060  1.00 17.95 ? 167 ILE A CG1 1 
ATOM   1386 C  CG2 . ILE A 1 166 ? 12.658 1.225   -2.464  1.00 19.96 ? 167 ILE A CG2 1 
ATOM   1387 C  CD1 . ILE A 1 166 ? 12.187 -0.251  0.319   1.00 20.18 ? 167 ILE A CD1 1 
ATOM   1388 N  N   . LYS A 1 167 ? 15.346 -2.835  -3.517  1.00 19.44 ? 168 LYS A N   1 
ATOM   1389 C  CA  . LYS A 1 167 ? 16.179 -3.941  -3.054  1.00 22.14 ? 168 LYS A CA  1 
ATOM   1390 C  C   . LYS A 1 167 ? 17.527 -3.595  -2.371  1.00 21.90 ? 168 LYS A C   1 
ATOM   1391 O  O   . LYS A 1 167 ? 17.929 -4.250  -1.414  1.00 19.43 ? 168 LYS A O   1 
ATOM   1392 C  CB  . LYS A 1 167 ? 16.426 -4.906  -4.233  1.00 20.22 ? 168 LYS A CB  1 
ATOM   1393 C  CG  . LYS A 1 167 ? 17.151 -6.184  -3.814  1.00 25.06 ? 168 LYS A CG  1 
ATOM   1394 C  CD  . LYS A 1 167 ? 17.196 -7.131  -5.016  1.00 29.21 ? 168 LYS A CD  1 
ATOM   1395 C  CE  . LYS A 1 167 ? 18.367 -8.093  -4.893  1.00 34.82 ? 168 LYS A CE  1 
ATOM   1396 N  NZ  . LYS A 1 167 ? 18.480 -9.074  -6.036  1.00 36.29 ? 168 LYS A NZ  1 
ATOM   1397 N  N   . THR A 1 168 ? 18.208 -2.521  -2.825  1.00 17.64 ? 169 THR A N   1 
ATOM   1398 C  CA  . THR A 1 168 ? 19.601 -2.275  -2.464  1.00 19.37 ? 169 THR A CA  1 
ATOM   1399 C  C   . THR A 1 168 ? 19.721 -0.928  -1.766  1.00 17.35 ? 169 THR A C   1 
ATOM   1400 O  O   . THR A 1 168 ? 18.815 -0.119  -1.912  1.00 18.82 ? 169 THR A O   1 
ATOM   1401 C  CB  . THR A 1 168 ? 20.533 -2.301  -3.716  1.00 20.69 ? 169 THR A CB  1 
ATOM   1402 O  OG1 . THR A 1 168 ? 19.948 -1.503  -4.741  1.00 22.55 ? 169 THR A OG1 1 
ATOM   1403 C  CG2 . THR A 1 168 ? 20.763 -3.771  -4.180  1.00 20.44 ? 169 THR A CG2 1 
ATOM   1404 N  N   A LYS A 1 169 ? 20.795 -0.768  -0.987  0.50 19.64 ? 170 LYS A N   1 
ATOM   1405 N  N   B LYS A 1 169 ? 20.813 -0.773  -1.022  0.50 19.82 ? 170 LYS A N   1 
ATOM   1406 C  CA  A LYS A 1 169 ? 21.090 0.399   -0.150  0.50 20.48 ? 170 LYS A CA  1 
ATOM   1407 C  CA  B LYS A 1 169 ? 21.160 0.424   -0.291  0.50 20.77 ? 170 LYS A CA  1 
ATOM   1408 C  C   A LYS A 1 169 ? 21.181 1.640   -0.992  0.50 21.31 ? 170 LYS A C   1 
ATOM   1409 C  C   B LYS A 1 169 ? 20.957 1.633   -1.188  0.50 21.63 ? 170 LYS A C   1 
ATOM   1410 O  O   A LYS A 1 169 ? 21.997 1.652   -1.951  0.50 22.03 ? 170 LYS A O   1 
ATOM   1411 O  O   B LYS A 1 169 ? 21.269 1.641   -2.399  0.50 22.79 ? 170 LYS A O   1 
ATOM   1412 C  CB  A LYS A 1 169 ? 22.413 0.215   0.580   0.50 20.03 ? 170 LYS A CB  1 
ATOM   1413 C  CB  B LYS A 1 169 ? 22.585 0.329   0.256   0.50 20.59 ? 170 LYS A CB  1 
ATOM   1414 C  CG  A LYS A 1 169 ? 22.970 1.482   1.287   0.50 19.90 ? 170 LYS A CG  1 
ATOM   1415 C  CG  B LYS A 1 169 ? 23.102 1.513   1.118   0.50 20.27 ? 170 LYS A CG  1 
ATOM   1416 C  CD  A LYS A 1 169 ? 24.413 1.257   1.722   0.50 22.45 ? 170 LYS A CD  1 
ATOM   1417 C  CD  B LYS A 1 169 ? 24.405 1.116   1.814   0.50 22.23 ? 170 LYS A CD  1 
ATOM   1418 C  CE  A LYS A 1 169 ? 24.926 2.402   2.593   0.50 22.53 ? 170 LYS A CE  1 
ATOM   1419 C  CE  B LYS A 1 169 ? 25.501 0.777   0.816   0.50 22.32 ? 170 LYS A CE  1 
ATOM   1420 N  NZ  A LYS A 1 169 ? 26.321 2.689   2.177   0.50 25.21 ? 170 LYS A NZ  1 
ATOM   1421 N  NZ  B LYS A 1 169 ? 26.785 0.353   1.445   0.50 24.52 ? 170 LYS A NZ  1 
ATOM   1422 N  N   . GLY A 1 170 ? 20.381 2.643   -0.592  1.00 21.38 ? 171 GLY A N   1 
ATOM   1423 C  CA  . GLY A 1 170 ? 20.128 3.913   -1.314  1.00 25.24 ? 171 GLY A CA  1 
ATOM   1424 C  C   . GLY A 1 170 ? 18.923 4.014   -2.213  1.00 26.10 ? 171 GLY A C   1 
ATOM   1425 O  O   . GLY A 1 170 ? 18.644 5.126   -2.738  1.00 28.04 ? 171 GLY A O   1 
ATOM   1426 N  N   . LYS A 1 171 ? 18.195 2.905   -2.484  1.00 21.33 ? 172 LYS A N   1 
ATOM   1427 C  CA  . LYS A 1 171 ? 16.989 2.983   -3.296  1.00 21.94 ? 172 LYS A CA  1 
ATOM   1428 C  C   . LYS A 1 171 ? 15.738 3.482   -2.550  1.00 23.50 ? 172 LYS A C   1 
ATOM   1429 O  O   . LYS A 1 171 ? 15.470 3.082   -1.405  1.00 25.33 ? 172 LYS A O   1 
ATOM   1430 C  CB  . LYS A 1 171 ? 16.694 1.635   -4.043  1.00 22.61 ? 172 LYS A CB  1 
ATOM   1431 C  CG  . LYS A 1 171 ? 17.772 1.303   -5.090  1.00 29.14 ? 172 LYS A CG  1 
ATOM   1432 C  CD  . LYS A 1 171 ? 17.412 0.151   -6.064  1.00 29.89 ? 172 LYS A CD  1 
ATOM   1433 C  CE  . LYS A 1 171 ? 16.770 0.609   -7.376  1.00 38.56 ? 172 LYS A CE  1 
ATOM   1434 N  NZ  . LYS A 1 171 ? 15.408 -0.003  -7.676  1.00 36.96 ? 172 LYS A NZ  1 
ATOM   1435 N  N   A SER A 1 172 ? 14.917 4.259   -3.253  0.50 22.79 ? 173 SER A N   1 
ATOM   1436 N  N   B SER A 1 172 ? 15.009 4.404   -3.128  0.50 22.64 ? 173 SER A N   1 
ATOM   1437 C  CA  A SER A 1 172 ? 13.654 4.763   -2.710  0.50 21.38 ? 173 SER A CA  1 
ATOM   1438 C  CA  B SER A 1 172 ? 13.812 4.869   -2.484  0.50 22.37 ? 173 SER A CA  1 
ATOM   1439 C  C   A SER A 1 172 ? 12.357 4.628   -3.575  0.50 22.54 ? 173 SER A C   1 
ATOM   1440 C  C   B SER A 1 172 ? 12.810 4.919   -3.573  0.50 24.58 ? 173 SER A C   1 
ATOM   1441 O  O   A SER A 1 172 ? 12.378 4.557   -4.834  0.50 20.28 ? 173 SER A O   1 
ATOM   1442 O  O   B SER A 1 172 ? 13.221 4.967   -4.752  0.50 22.73 ? 173 SER A O   1 
ATOM   1443 C  CB  A SER A 1 172 ? 13.843 6.214   -2.165  0.50 24.93 ? 173 SER A CB  1 
ATOM   1444 C  CB  B SER A 1 172 ? 13.975 6.310   -1.989  0.50 24.19 ? 173 SER A CB  1 
ATOM   1445 O  OG  A SER A 1 172 ? 14.878 6.965   -2.834  0.50 18.71 ? 173 SER A OG  1 
ATOM   1446 O  OG  B SER A 1 172 ? 14.030 7.200   -3.123  0.50 17.57 ? 173 SER A OG  1 
ATOM   1447 N  N   A ALA A 1 173 ? 11.207 4.591   -2.924  0.50 22.40 ? 174 ALA A N   1 
ATOM   1448 N  N   B ALA A 1 173 ? 11.522 4.997   -3.200  0.50 22.89 ? 174 ALA A N   1 
ATOM   1449 C  CA  A ALA A 1 173 ? 9.970  4.538   -3.681  0.50 23.19 ? 174 ALA A CA  1 
ATOM   1450 C  CA  B ALA A 1 173 ? 10.381 5.110   -4.154  0.50 25.96 ? 174 ALA A CA  1 
ATOM   1451 C  C   A ALA A 1 173 ? 8.913  5.426   -3.086  0.50 24.24 ? 174 ALA A C   1 
ATOM   1452 C  C   B ALA A 1 173 ? 9.362  6.291   -3.975  0.50 25.72 ? 174 ALA A C   1 
ATOM   1453 O  O   A ALA A 1 173 ? 8.864  5.631   -1.885  0.50 17.47 ? 174 ALA A O   1 
ATOM   1454 O  O   B ALA A 1 173 ? 9.759  7.455   -3.941  0.50 30.59 ? 174 ALA A O   1 
ATOM   1455 C  CB  A ALA A 1 173 ? 9.461  3.116   -3.839  0.50 24.08 ? 174 ALA A CB  1 
ATOM   1456 C  CB  B ALA A 1 173 ? 9.629  3.781   -4.219  0.50 23.10 ? 174 ALA A CB  1 
ATOM   1457 N  N   . ASP A 1 174 ? 8.061  5.956   -3.962  1.00 27.12 ? 175 ASP A N   1 
ATOM   1458 C  CA  . ASP A 1 174 ? 6.956  6.805   -3.537  1.00 30.33 ? 175 ASP A CA  1 
ATOM   1459 C  C   . ASP A 1 174 ? 6.059  5.884   -2.786  1.00 29.86 ? 175 ASP A C   1 
ATOM   1460 O  O   . ASP A 1 174 ? 5.800  4.741   -3.232  1.00 29.22 ? 175 ASP A O   1 
ATOM   1461 C  CB  . ASP A 1 174 ? 6.160  7.390   -4.716  1.00 35.18 ? 175 ASP A CB  1 
ATOM   1462 C  CG  . ASP A 1 174 ? 6.904  8.483   -5.367  1.00 43.74 ? 175 ASP A CG  1 
ATOM   1463 O  OD1 . ASP A 1 174 ? 7.418  9.330   -4.608  1.00 42.84 ? 175 ASP A OD1 1 
ATOM   1464 O  OD2 . ASP A 1 174 ? 7.021  8.489   -6.617  1.00 55.07 ? 175 ASP A OD2 1 
ATOM   1465 N  N   . PHE A 1 175 ? 5.551  6.350   -1.651  1.00 23.91 ? 176 PHE A N   1 
ATOM   1466 C  CA  . PHE A 1 175 ? 4.811  5.429   -0.827  1.00 24.75 ? 176 PHE A CA  1 
ATOM   1467 C  C   . PHE A 1 175 ? 3.818  6.223   -0.054  1.00 25.64 ? 176 PHE A C   1 
ATOM   1468 O  O   . PHE A 1 175 ? 4.051  6.553   1.128   1.00 23.32 ? 176 PHE A O   1 
ATOM   1469 C  CB  . PHE A 1 175 ? 5.784  4.583   0.052   1.00 21.73 ? 176 PHE A CB  1 
ATOM   1470 C  CG  . PHE A 1 175 ? 5.142  3.326   0.596   1.00 21.33 ? 176 PHE A CG  1 
ATOM   1471 C  CD1 . PHE A 1 175 ? 4.844  2.261   -0.252  1.00 23.43 ? 176 PHE A CD1 1 
ATOM   1472 C  CD2 . PHE A 1 175 ? 4.800  3.201   1.944   1.00 22.24 ? 176 PHE A CD2 1 
ATOM   1473 C  CE1 . PHE A 1 175 ? 4.214  1.123   0.249   1.00 23.97 ? 176 PHE A CE1 1 
ATOM   1474 C  CE2 . PHE A 1 175 ? 4.202  2.061   2.465   1.00 21.63 ? 176 PHE A CE2 1 
ATOM   1475 C  CZ  . PHE A 1 175 ? 3.903  1.014   1.611   1.00 24.62 ? 176 PHE A CZ  1 
ATOM   1476 N  N   . THR A 1 176 ? 2.745  6.577   -0.760  1.00 20.98 ? 177 THR A N   1 
ATOM   1477 C  CA  . THR A 1 176 ? 1.706  7.428   -0.240  1.00 20.71 ? 177 THR A CA  1 
ATOM   1478 C  C   . THR A 1 176 ? 0.501  6.606   0.188   1.00 18.20 ? 177 THR A C   1 
ATOM   1479 O  O   . THR A 1 176 ? 0.281  5.448   -0.284  1.00 20.84 ? 177 THR A O   1 
ATOM   1480 C  CB  . THR A 1 176 ? 1.278  8.538   -1.257  1.00 22.07 ? 177 THR A CB  1 
ATOM   1481 O  OG1 . THR A 1 176 ? 0.621  7.908   -2.370  1.00 26.10 ? 177 THR A OG1 1 
ATOM   1482 C  CG2 . THR A 1 176 ? 2.492  9.368   -1.749  1.00 27.82 ? 177 THR A CG2 1 
ATOM   1483 N  N   . ASN A 1 177 ? -0.289 7.196   1.090   1.00 19.47 ? 178 ASN A N   1 
ATOM   1484 C  CA  . ASN A 1 177 ? -1.537 6.675   1.564   1.00 18.82 ? 178 ASN A CA  1 
ATOM   1485 C  C   . ASN A 1 177 ? -1.405 5.311   2.264   1.00 20.12 ? 178 ASN A C   1 
ATOM   1486 O  O   . ASN A 1 177 ? -2.344 4.585   2.275   1.00 24.16 ? 178 ASN A O   1 
ATOM   1487 C  CB  . ASN A 1 177 ? -2.550 6.564   0.415   1.00 20.42 ? 178 ASN A CB  1 
ATOM   1488 C  CG  . ASN A 1 177 ? -2.816 7.933   -0.228  1.00 21.75 ? 178 ASN A CG  1 
ATOM   1489 O  OD1 . ASN A 1 177 ? -3.565 8.714   0.341   1.00 22.18 ? 178 ASN A OD1 1 
ATOM   1490 N  ND2 . ASN A 1 177 ? -2.153 8.219   -1.371  1.00 19.10 ? 178 ASN A ND2 1 
ATOM   1491 N  N   . PHE A 1 178 ? -0.243 5.029   2.844   1.00 18.79 ? 179 PHE A N   1 
ATOM   1492 C  CA  . PHE A 1 178 ? -0.120 3.759   3.675   1.00 17.75 ? 179 PHE A CA  1 
ATOM   1493 C  C   . PHE A 1 178 ? -0.662 4.036   5.062   1.00 18.19 ? 179 PHE A C   1 
ATOM   1494 O  O   . PHE A 1 178 ? -0.253 5.027   5.684   1.00 20.42 ? 179 PHE A O   1 
ATOM   1495 C  CB  . PHE A 1 178 ? 1.287  3.278   3.734   1.00 17.91 ? 179 PHE A CB  1 
ATOM   1496 C  CG  . PHE A 1 178 ? 1.405  2.038   4.540   1.00 16.82 ? 179 PHE A CG  1 
ATOM   1497 C  CD1 . PHE A 1 178 ? 0.997  0.833   4.003   1.00 19.01 ? 179 PHE A CD1 1 
ATOM   1498 C  CD2 . PHE A 1 178 ? 1.709  2.123   5.885   1.00 17.04 ? 179 PHE A CD2 1 
ATOM   1499 C  CE1 . PHE A 1 178 ? 1.001  -0.293  4.793   1.00 18.52 ? 179 PHE A CE1 1 
ATOM   1500 C  CE2 . PHE A 1 178 ? 1.702  0.989   6.685   1.00 17.20 ? 179 PHE A CE2 1 
ATOM   1501 C  CZ  . PHE A 1 178 ? 1.377  -0.206  6.126   1.00 18.09 ? 179 PHE A CZ  1 
ATOM   1502 N  N   . ASP A 1 179 ? -1.592 3.205   5.528   1.00 18.06 ? 180 ASP A N   1 
ATOM   1503 C  CA  . ASP A 1 179 ? -2.229 3.390   6.807   1.00 18.22 ? 180 ASP A CA  1 
ATOM   1504 C  C   . ASP A 1 179 ? -1.604 2.558   7.876   1.00 16.96 ? 180 ASP A C   1 
ATOM   1505 O  O   . ASP A 1 179 ? -1.806 1.315   7.880   1.00 14.60 ? 180 ASP A O   1 
ATOM   1506 C  CB  . ASP A 1 179 ? -3.712 2.990   6.676   1.00 21.10 ? 180 ASP A CB  1 
ATOM   1507 C  CG  . ASP A 1 179 ? -4.567 3.466   7.846   1.00 23.38 ? 180 ASP A CG  1 
ATOM   1508 O  OD1 . ASP A 1 179 ? -4.029 3.612   8.962   1.00 20.47 ? 180 ASP A OD1 1 
ATOM   1509 O  OD2 . ASP A 1 179 ? -5.782 3.697   7.648   1.00 28.23 ? 180 ASP A OD2 1 
ATOM   1510 N  N   . PRO A 1 180 ? -0.857 3.189   8.817   1.00 15.30 ? 181 PRO A N   1 
ATOM   1511 C  CA  . PRO A 1 180 ? -0.184 2.367   9.839   1.00 15.67 ? 181 PRO A CA  1 
ATOM   1512 C  C   . PRO A 1 180 ? -1.114 1.750   10.855  1.00 14.20 ? 181 PRO A C   1 
ATOM   1513 O  O   . PRO A 1 180 ? -0.686 0.826   11.609  1.00 13.56 ? 181 PRO A O   1 
ATOM   1514 C  CB  . PRO A 1 180 ? 0.778  3.391   10.488  1.00 17.14 ? 181 PRO A CB  1 
ATOM   1515 C  CG  . PRO A 1 180 ? 0.046  4.675   10.370  1.00 16.79 ? 181 PRO A CG  1 
ATOM   1516 C  CD  . PRO A 1 180 ? -0.425 4.601   8.933   1.00 16.61 ? 181 PRO A CD  1 
ATOM   1517 N  N   . ARG A 1 181 ? -2.412 2.133   10.881  1.00 13.95 ? 182 ARG A N   1 
ATOM   1518 C  CA  . ARG A 1 181 ? -3.340 1.426   11.813  1.00 15.58 ? 182 ARG A CA  1 
ATOM   1519 C  C   . ARG A 1 181 ? -3.433 -0.079  11.461  1.00 15.61 ? 182 ARG A C   1 
ATOM   1520 O  O   . ARG A 1 181 ? -3.757 -0.880  12.319  1.00 16.49 ? 182 ARG A O   1 
ATOM   1521 C  CB  . ARG A 1 181 ? -4.757 2.080   11.820  1.00 16.48 ? 182 ARG A CB  1 
ATOM   1522 C  CG  . ARG A 1 181 ? -4.659 3.544   12.298  1.00 16.96 ? 182 ARG A CG  1 
ATOM   1523 C  CD  . ARG A 1 181 ? -5.979 4.306   12.083  1.00 17.90 ? 182 ARG A CD  1 
ATOM   1524 N  NE  . ARG A 1 181 ? -6.306 4.410   10.698  1.00 18.49 ? 182 ARG A NE  1 
ATOM   1525 C  CZ  . ARG A 1 181 ? -7.423 5.041   10.313  1.00 25.42 ? 182 ARG A CZ  1 
ATOM   1526 N  NH1 . ARG A 1 181 ? -8.190 5.568   11.259  1.00 27.88 ? 182 ARG A NH1 1 
ATOM   1527 N  NH2 . ARG A 1 181 ? -7.775 5.101   9.044   1.00 24.36 ? 182 ARG A NH2 1 
ATOM   1528 N  N   . GLY A 1 182 ? -3.198 -0.390  10.206  1.00 15.50 ? 183 GLY A N   1 
ATOM   1529 C  CA  . GLY A 1 182 ? -3.207 -1.795  9.715   1.00 17.39 ? 183 GLY A CA  1 
ATOM   1530 C  C   . GLY A 1 182 ? -2.093 -2.667  10.261  1.00 20.43 ? 183 GLY A C   1 
ATOM   1531 O  O   . GLY A 1 182 ? -2.129 -3.878  10.028  1.00 22.14 ? 183 GLY A O   1 
ATOM   1532 N  N   . LEU A 1 183 ? -1.142 -2.081  11.010  1.00 16.76 ? 184 LEU A N   1 
ATOM   1533 C  CA  . LEU A 1 183 ? -0.019 -2.849  11.586  1.00 16.12 ? 184 LEU A CA  1 
ATOM   1534 C  C   . LEU A 1 183 ? -0.205 -3.041  13.116  1.00 15.90 ? 184 LEU A C   1 
ATOM   1535 O  O   . LEU A 1 183 ? 0.671  -3.610  13.780  1.00 18.89 ? 184 LEU A O   1 
ATOM   1536 C  CB  . LEU A 1 183 ? 1.299  -2.115  11.325  1.00 15.54 ? 184 LEU A CB  1 
ATOM   1537 C  CG  . LEU A 1 183 ? 1.661  -1.881  9.825   1.00 16.06 ? 184 LEU A CG  1 
ATOM   1538 C  CD1 . LEU A 1 183 ? 2.940  -1.113  9.620   1.00 17.98 ? 184 LEU A CD1 1 
ATOM   1539 C  CD2 . LEU A 1 183 ? 1.828  -3.165  9.012   1.00 19.28 ? 184 LEU A CD2 1 
ATOM   1540 N  N   . LEU A 1 184 ? -1.334 -2.640  13.697  1.00 14.77 ? 185 LEU A N   1 
ATOM   1541 C  CA  . LEU A 1 184 ? -1.455 -2.626  15.169  1.00 14.14 ? 185 LEU A CA  1 
ATOM   1542 C  C   . LEU A 1 184 ? -2.187 -3.884  15.646  1.00 16.38 ? 185 LEU A C   1 
ATOM   1543 O  O   . LEU A 1 184 ? -3.196 -4.278  15.011  1.00 19.88 ? 185 LEU A O   1 
ATOM   1544 C  CB  . LEU A 1 184 ? -2.183 -1.360  15.708  1.00 13.61 ? 185 LEU A CB  1 
ATOM   1545 C  CG  . LEU A 1 184 ? -1.572 -0.024  15.348  1.00 15.14 ? 185 LEU A CG  1 
ATOM   1546 C  CD1 . LEU A 1 184 ? -2.369 1.207   15.832  1.00 16.66 ? 185 LEU A CD1 1 
ATOM   1547 C  CD2 . LEU A 1 184 ? -0.131 0.090   15.844  1.00 16.32 ? 185 LEU A CD2 1 
ATOM   1548 N  N   . PRO A 1 185 ? -1.771 -4.459  16.778  1.00 16.21 ? 186 PRO A N   1 
ATOM   1549 C  CA  . PRO A 1 185 ? -2.563 -5.565  17.286  1.00 16.51 ? 186 PRO A CA  1 
ATOM   1550 C  C   . PRO A 1 185 ? -3.871 -5.062  17.968  1.00 17.73 ? 186 PRO A C   1 
ATOM   1551 O  O   . PRO A 1 185 ? -4.024 -3.892  18.172  1.00 18.40 ? 186 PRO A O   1 
ATOM   1552 C  CB  . PRO A 1 185 ? -1.631 -6.194  18.345  1.00 15.59 ? 186 PRO A CB  1 
ATOM   1553 C  CG  . PRO A 1 185 ? -0.876 -4.992  18.920  1.00 13.60 ? 186 PRO A CG  1 
ATOM   1554 C  CD  . PRO A 1 185 ? -0.685 -4.052  17.706  1.00 15.16 ? 186 PRO A CD  1 
ATOM   1555 N  N   . GLU A 1 186 ? -4.733 -5.948  18.457  1.00 18.53 ? 187 GLU A N   1 
ATOM   1556 C  CA  . GLU A 1 186 ? -5.966 -5.483  19.190  1.00 18.72 ? 187 GLU A CA  1 
ATOM   1557 C  C   . GLU A 1 186 ? -5.689 -4.711  20.448  1.00 17.97 ? 187 GLU A C   1 
ATOM   1558 O  O   . GLU A 1 186 ? -6.286 -3.662  20.650  1.00 21.03 ? 187 GLU A O   1 
ATOM   1559 C  CB  . GLU A 1 186 ? -6.816 -6.676  19.626  1.00 20.12 ? 187 GLU A CB  1 
ATOM   1560 C  CG  . GLU A 1 186 ? -7.407 -7.488  18.490  1.00 24.38 ? 187 GLU A CG  1 
ATOM   1561 C  CD  . GLU A 1 186 ? -8.140 -8.768  19.005  1.00 24.29 ? 187 GLU A CD  1 
ATOM   1562 O  OE1 . GLU A 1 186 ? -8.644 -9.518  18.190  1.00 32.37 ? 187 GLU A OE1 1 
ATOM   1563 O  OE2 . GLU A 1 186 ? -8.203 -9.017  20.226  1.00 26.32 ? 187 GLU A OE2 1 
ATOM   1564 N  N   . SER A 1 187 ? -4.811 -5.214  21.322  1.00 17.54 ? 188 SER A N   1 
ATOM   1565 C  CA  . SER A 1 187 ? -4.633 -4.615  22.630  1.00 17.87 ? 188 SER A CA  1 
ATOM   1566 C  C   . SER A 1 187 ? -3.506 -3.613  22.557  1.00 17.13 ? 188 SER A C   1 
ATOM   1567 O  O   . SER A 1 187 ? -2.529 -3.890  21.887  1.00 17.62 ? 188 SER A O   1 
ATOM   1568 C  CB  . SER A 1 187 ? -4.198 -5.654  23.626  1.00 17.56 ? 188 SER A CB  1 
ATOM   1569 O  OG  . SER A 1 187 ? -4.021 -5.157  24.922  1.00 17.42 ? 188 SER A OG  1 
ATOM   1570 N  N   . LEU A 1 188 ? -3.649 -2.525  23.294  1.00 15.96 ? 189 LEU A N   1 
ATOM   1571 C  CA  . LEU A 1 188 ? -2.562 -1.551  23.526  1.00 17.03 ? 189 LEU A CA  1 
ATOM   1572 C  C   . LEU A 1 188 ? -1.889 -1.696  24.915  1.00 17.90 ? 189 LEU A C   1 
ATOM   1573 O  O   . LEU A 1 188 ? -1.250 -0.751  25.395  1.00 19.98 ? 189 LEU A O   1 
ATOM   1574 C  CB  . LEU A 1 188 ? -3.100 -0.102  23.283  1.00 16.44 ? 189 LEU A CB  1 
ATOM   1575 C  CG  . LEU A 1 188 ? -3.414 0.242   21.813  1.00 18.81 ? 189 LEU A CG  1 
ATOM   1576 C  CD1 . LEU A 1 188 ? -3.924 1.697   21.690  1.00 19.91 ? 189 LEU A CD1 1 
ATOM   1577 C  CD2 . LEU A 1 188 ? -2.281 -0.050  20.799  1.00 19.07 ? 189 LEU A CD2 1 
ATOM   1578 N  N   . ASP A 1 189 ? -2.058 -2.832  25.597  1.00 17.97 ? 190 ASP A N   1 
ATOM   1579 C  CA  . ASP A 1 189 ? -1.294 -3.142  26.811  1.00 17.90 ? 190 ASP A CA  1 
ATOM   1580 C  C   . ASP A 1 189 ? 0.195  -3.123  26.447  1.00 15.37 ? 190 ASP A C   1 
ATOM   1581 O  O   . ASP A 1 189 ? 0.606  -3.583  25.354  1.00 15.90 ? 190 ASP A O   1 
ATOM   1582 C  CB  . ASP A 1 189 ? -1.637 -4.517  27.345  1.00 20.80 ? 190 ASP A CB  1 
ATOM   1583 C  CG  . ASP A 1 189 ? -3.040 -4.555  28.026  1.00 25.55 ? 190 ASP A CG  1 
ATOM   1584 O  OD1 . ASP A 1 189 ? -3.715 -3.510  28.144  1.00 29.10 ? 190 ASP A OD1 1 
ATOM   1585 O  OD2 . ASP A 1 189 ? -3.401 -5.661  28.423  1.00 30.10 ? 190 ASP A OD2 1 
ATOM   1586 N  N   . TYR A 1 190 ? 0.947  -2.479  27.310  1.00 15.31 ? 191 TYR A N   1 
ATOM   1587 C  CA  . TYR A 1 190 ? 2.370  -2.250  27.025  1.00 14.76 ? 191 TYR A CA  1 
ATOM   1588 C  C   . TYR A 1 190 ? 3.271  -2.345  28.238  1.00 14.28 ? 191 TYR A C   1 
ATOM   1589 O  O   . TYR A 1 190 ? 2.824  -2.214  29.402  1.00 13.34 ? 191 TYR A O   1 
ATOM   1590 C  CB  . TYR A 1 190 ? 2.537  -0.865  26.349  1.00 15.07 ? 191 TYR A CB  1 
ATOM   1591 C  CG  . TYR A 1 190 ? 2.156  0.285   27.279  1.00 15.98 ? 191 TYR A CG  1 
ATOM   1592 C  CD1 . TYR A 1 190 ? 3.104  0.852   28.128  1.00 16.66 ? 191 TYR A CD1 1 
ATOM   1593 C  CD2 . TYR A 1 190 ? 0.872  0.847   27.227  1.00 15.60 ? 191 TYR A CD2 1 
ATOM   1594 C  CE1 . TYR A 1 190 ? 2.719  1.899   29.024  1.00 18.72 ? 191 TYR A CE1 1 
ATOM   1595 C  CE2 . TYR A 1 190 ? 0.494  1.893   28.068  1.00 19.09 ? 191 TYR A CE2 1 
ATOM   1596 C  CZ  . TYR A 1 190 ? 1.429  2.410   28.956  1.00 17.90 ? 191 TYR A CZ  1 
ATOM   1597 O  OH  . TYR A 1 190 ? 1.052  3.438   29.796  1.00 18.14 ? 191 TYR A OH  1 
ATOM   1598 N  N   . TRP A 1 191 ? 4.576  -2.490  27.995  1.00 12.19 ? 192 TRP A N   1 
ATOM   1599 C  CA  . TRP A 1 191 ? 5.617  -2.225  28.955  1.00 11.29 ? 192 TRP A CA  1 
ATOM   1600 C  C   . TRP A 1 191 ? 6.346  -0.947  28.497  1.00 11.17 ? 192 TRP A C   1 
ATOM   1601 O  O   . TRP A 1 191 ? 6.317  -0.600  27.315  1.00 11.17 ? 192 TRP A O   1 
ATOM   1602 C  CB  . TRP A 1 191 ? 6.660  -3.302  28.920  1.00 13.28 ? 192 TRP A CB  1 
ATOM   1603 C  CG  . TRP A 1 191 ? 6.148  -4.661  29.323  1.00 13.59 ? 192 TRP A CG  1 
ATOM   1604 C  CD1 . TRP A 1 191 ? 5.877  -5.122  30.609  1.00 14.09 ? 192 TRP A CD1 1 
ATOM   1605 C  CD2 . TRP A 1 191 ? 5.873  -5.786  28.433  1.00 14.27 ? 192 TRP A CD2 1 
ATOM   1606 N  NE1 . TRP A 1 191 ? 5.458  -6.428  30.564  1.00 17.59 ? 192 TRP A NE1 1 
ATOM   1607 C  CE2 . TRP A 1 191 ? 5.433  -6.890  29.289  1.00 14.46 ? 192 TRP A CE2 1 
ATOM   1608 C  CE3 . TRP A 1 191 ? 5.944  -5.986  27.061  1.00 13.36 ? 192 TRP A CE3 1 
ATOM   1609 C  CZ2 . TRP A 1 191 ? 5.088  -8.130  28.773  1.00 17.09 ? 192 TRP A CZ2 1 
ATOM   1610 C  CZ3 . TRP A 1 191 ? 5.595  -7.237  26.544  1.00 14.80 ? 192 TRP A CZ3 1 
ATOM   1611 C  CH2 . TRP A 1 191 ? 5.177  -8.280  27.381  1.00 16.10 ? 192 TRP A CH2 1 
ATOM   1612 N  N   . THR A 1 192 ? 6.902  -0.250  29.442  1.00 11.26 ? 193 THR A N   1 
ATOM   1613 C  CA  . THR A 1 192 ? 7.646  0.991   29.120  1.00 12.81 ? 193 THR A CA  1 
ATOM   1614 C  C   . THR A 1 192 ? 8.873  1.169   30.009  1.00 13.39 ? 193 THR A C   1 
ATOM   1615 O  O   . THR A 1 192 ? 8.881  0.764   31.174  1.00 13.69 ? 193 THR A O   1 
ATOM   1616 C  CB  . THR A 1 192 ? 6.717  2.226   29.181  1.00 13.08 ? 193 THR A CB  1 
ATOM   1617 O  OG1 . THR A 1 192 ? 7.424  3.408   28.736  1.00 13.15 ? 193 THR A OG1 1 
ATOM   1618 C  CG2 . THR A 1 192 ? 6.137  2.423   30.639  1.00 13.03 ? 193 THR A CG2 1 
ATOM   1619 N  N   . TYR A 1 193 ? 9.929  1.773   29.445  1.00 13.97 ? 194 TYR A N   1 
ATOM   1620 C  CA  . TYR A 1 193 ? 11.158 2.020   30.145  1.00 12.82 ? 194 TYR A CA  1 
ATOM   1621 C  C   . TYR A 1 193 ? 11.937 3.064   29.336  1.00 12.78 ? 194 TYR A C   1 
ATOM   1622 O  O   . TYR A 1 193 ? 11.670 3.289   28.126  1.00 11.80 ? 194 TYR A O   1 
ATOM   1623 C  CB  . TYR A 1 193 ? 11.965 0.667   30.393  1.00 12.65 ? 194 TYR A CB  1 
ATOM   1624 C  CG  . TYR A 1 193 ? 12.673 0.246   29.096  1.00 11.09 ? 194 TYR A CG  1 
ATOM   1625 C  CD1 . TYR A 1 193 ? 11.973 -0.471  28.114  1.00 10.77 ? 194 TYR A CD1 1 
ATOM   1626 C  CD2 . TYR A 1 193 ? 14.054 0.570   28.849  1.00 12.28 ? 194 TYR A CD2 1 
ATOM   1627 C  CE1 . TYR A 1 193 ? 12.608 -0.814  26.890  1.00 10.36 ? 194 TYR A CE1 1 
ATOM   1628 C  CE2 . TYR A 1 193 ? 14.680 0.235   27.650  1.00 12.29 ? 194 TYR A CE2 1 
ATOM   1629 C  CZ  . TYR A 1 193 ? 13.967 -0.460  26.678  1.00 10.03 ? 194 TYR A CZ  1 
ATOM   1630 O  OH  . TYR A 1 193 ? 14.675 -0.741  25.521  1.00 11.57 ? 194 TYR A OH  1 
ATOM   1631 N  N   . PRO A 1 194 ? 12.894 3.741   29.980  1.00 12.33 ? 195 PRO A N   1 
ATOM   1632 C  CA  . PRO A 1 194 ? 13.708 4.754   29.312  1.00 13.37 ? 195 PRO A CA  1 
ATOM   1633 C  C   . PRO A 1 194 ? 14.935 4.132   28.643  1.00 12.21 ? 195 PRO A C   1 
ATOM   1634 O  O   . PRO A 1 194 ? 15.637 3.358   29.318  1.00 12.54 ? 195 PRO A O   1 
ATOM   1635 C  CB  . PRO A 1 194 ? 14.202 5.633   30.496  1.00 14.58 ? 195 PRO A CB  1 
ATOM   1636 C  CG  . PRO A 1 194 ? 14.146 4.735   31.694  1.00 14.40 ? 195 PRO A CG  1 
ATOM   1637 C  CD  . PRO A 1 194 ? 13.069 3.710   31.443  1.00 13.83 ? 195 PRO A CD  1 
ATOM   1638 N  N   . GLY A 1 195 ? 15.195 4.429   27.373  1.00 11.08 ? 196 GLY A N   1 
ATOM   1639 C  CA  . GLY A 1 195 ? 16.376 3.815   26.738  1.00 13.15 ? 196 GLY A CA  1 
ATOM   1640 C  C   . GLY A 1 195 ? 16.853 4.670   25.609  1.00 13.27 ? 196 GLY A C   1 
ATOM   1641 O  O   . GLY A 1 195 ? 16.903 5.896   25.751  1.00 12.49 ? 196 GLY A O   1 
ATOM   1642 N  N   . SER A 1 196 ? 17.274 3.998   24.513  1.00 12.86 ? 197 SER A N   1 
ATOM   1643 C  CA  . SER A 1 196 ? 18.030 4.638   23.451  1.00 12.34 ? 197 SER A CA  1 
ATOM   1644 C  C   . SER A 1 196 ? 17.606 4.208   22.092  1.00 12.61 ? 197 SER A C   1 
ATOM   1645 O  O   . SER A 1 196 ? 16.860 3.234   21.942  1.00 12.78 ? 197 SER A O   1 
ATOM   1646 C  CB  . SER A 1 196 ? 19.531 4.284   23.576  1.00 13.65 ? 197 SER A CB  1 
ATOM   1647 O  OG  . SER A 1 196 ? 19.785 2.891   23.292  1.00 11.88 ? 197 SER A OG  1 
ATOM   1648 N  N   . LEU A 1 197 ? 18.164 4.864   21.092  1.00 10.96 ? 198 LEU A N   1 
ATOM   1649 C  CA  . LEU A 1 197 ? 18.124 4.285   19.744  1.00 11.07 ? 198 LEU A CA  1 
ATOM   1650 C  C   . LEU A 1 197 ? 18.838 2.968   19.825  1.00 10.91 ? 198 LEU A C   1 
ATOM   1651 O  O   . LEU A 1 197 ? 19.856 2.804   20.528  1.00 12.43 ? 198 LEU A O   1 
ATOM   1652 C  CB  . LEU A 1 197 ? 18.868 5.161   18.703  1.00 13.52 ? 198 LEU A CB  1 
ATOM   1653 C  CG  . LEU A 1 197 ? 18.438 6.607   18.723  1.00 14.95 ? 198 LEU A CG  1 
ATOM   1654 C  CD1 . LEU A 1 197 ? 19.328 7.390   17.755  1.00 15.49 ? 198 LEU A CD1 1 
ATOM   1655 C  CD2 . LEU A 1 197 ? 17.015 6.829   18.333  1.00 15.72 ? 198 LEU A CD2 1 
ATOM   1656 N  N   . THR A 1 198 ? 18.347 2.001   19.065  1.00 11.69 ? 199 THR A N   1 
ATOM   1657 C  CA  . THR A 1 198 ? 19.043 0.722   19.013  1.00 10.87 ? 199 THR A CA  1 
ATOM   1658 C  C   . THR A 1 198 ? 20.063 0.631   17.854  1.00 12.82 ? 199 THR A C   1 
ATOM   1659 O  O   . THR A 1 198 ? 20.625 -0.476  17.624  1.00 13.17 ? 199 THR A O   1 
ATOM   1660 C  CB  . THR A 1 198 ? 17.999 -0.421  18.842  1.00 10.96 ? 199 THR A CB  1 
ATOM   1661 O  OG1 . THR A 1 198 ? 17.480 -0.423  17.503  1.00 12.14 ? 199 THR A OG1 1 
ATOM   1662 C  CG2 . THR A 1 198 ? 16.934 -0.330  19.951  1.00 11.92 ? 199 THR A CG2 1 
ATOM   1663 N  N   . THR A 1 199 ? 20.250 1.703   17.083  1.00 14.00 ? 200 THR A N   1 
ATOM   1664 C  CA  . THR A 1 199 ? 21.366 1.724   16.119  1.00 14.62 ? 200 THR A CA  1 
ATOM   1665 C  C   . THR A 1 199 ? 22.188 2.957   16.431  1.00 14.91 ? 200 THR A C   1 
ATOM   1666 O  O   . THR A 1 199 ? 21.648 3.918   17.033  1.00 13.25 ? 200 THR A O   1 
ATOM   1667 C  CB  . THR A 1 199 ? 20.928 1.874   14.641  1.00 15.14 ? 200 THR A CB  1 
ATOM   1668 O  OG1 . THR A 1 199 ? 20.280 3.163   14.434  1.00 16.84 ? 200 THR A OG1 1 
ATOM   1669 C  CG2 . THR A 1 199 ? 19.963 0.779   14.204  1.00 16.34 ? 200 THR A CG2 1 
ATOM   1670 N  N   . PRO A 1 200 ? 23.462 2.943   15.989  1.00 15.45 ? 201 PRO A N   1 
ATOM   1671 C  CA  . PRO A 1 200 ? 24.196 4.240   15.935  1.00 14.89 ? 201 PRO A CA  1 
ATOM   1672 C  C   . PRO A 1 200 ? 23.250 5.340   15.409  1.00 14.81 ? 201 PRO A C   1 
ATOM   1673 O  O   . PRO A 1 200 ? 22.574 5.143   14.387  1.00 15.70 ? 201 PRO A O   1 
ATOM   1674 C  CB  . PRO A 1 200 ? 25.305 3.921   14.922  1.00 14.68 ? 201 PRO A CB  1 
ATOM   1675 C  CG  . PRO A 1 200 ? 25.620 2.491   15.171  1.00 16.54 ? 201 PRO A CG  1 
ATOM   1676 C  CD  . PRO A 1 200 ? 24.215 1.852   15.277  1.00 15.74 ? 201 PRO A CD  1 
ATOM   1677 N  N   . PRO A 1 201 ? 23.290 6.567   16.005  1.00 16.39 ? 202 PRO A N   1 
ATOM   1678 C  CA  . PRO A 1 201 ? 24.202 7.039   17.049  1.00 17.26 ? 202 PRO A CA  1 
ATOM   1679 C  C   . PRO A 1 201 ? 23.868 6.649   18.484  1.00 14.17 ? 202 PRO A C   1 
ATOM   1680 O  O   . PRO A 1 201 ? 24.504 7.079   19.451  1.00 16.13 ? 202 PRO A O   1 
ATOM   1681 C  CB  . PRO A 1 201 ? 24.266 8.557   16.770  1.00 15.34 ? 202 PRO A CB  1 
ATOM   1682 C  CG  . PRO A 1 201 ? 22.843 8.850   16.374  1.00 17.04 ? 202 PRO A CG  1 
ATOM   1683 C  CD  . PRO A 1 201 ? 22.463 7.659   15.461  1.00 15.55 ? 202 PRO A CD  1 
ATOM   1684 N  N   . LEU A 1 202 ? 22.876 5.729   18.652  1.00 13.43 ? 203 LEU A N   1 
ATOM   1685 C  CA  . LEU A 1 202 ? 22.646 5.146   20.012  1.00 12.38 ? 203 LEU A CA  1 
ATOM   1686 C  C   . LEU A 1 202 ? 22.277 6.162   21.120  1.00 11.34 ? 203 LEU A C   1 
ATOM   1687 O  O   . LEU A 1 202 ? 22.396 5.904   22.313  1.00 13.77 ? 203 LEU A O   1 
ATOM   1688 C  CB  . LEU A 1 202 ? 23.743 4.199   20.539  1.00 13.67 ? 203 LEU A CB  1 
ATOM   1689 C  CG  . LEU A 1 202 ? 24.114 3.055   19.574  1.00 14.59 ? 203 LEU A CG  1 
ATOM   1690 C  CD1 . LEU A 1 202 ? 25.364 2.437   20.188  1.00 16.89 ? 203 LEU A CD1 1 
ATOM   1691 C  CD2 . LEU A 1 202 ? 22.961 2.008   19.556  1.00 14.37 ? 203 LEU A CD2 1 
ATOM   1692 N  N   . LEU A 1 203 ? 21.705 7.266   20.672  1.00 13.25 ? 204 LEU A N   1 
ATOM   1693 C  CA  . LEU A 1 203 ? 21.305 8.386   21.574  1.00 15.61 ? 204 LEU A CA  1 
ATOM   1694 C  C   . LEU A 1 203 ? 20.307 7.983   22.624  1.00 15.45 ? 204 LEU A C   1 
ATOM   1695 O  O   . LEU A 1 203 ? 19.324 7.248   22.339  1.00 14.26 ? 204 LEU A O   1 
ATOM   1696 C  CB  . LEU A 1 203 ? 20.748 9.524   20.698  1.00 15.81 ? 204 LEU A CB  1 
ATOM   1697 C  CG  . LEU A 1 203 ? 21.811 10.144  19.768  1.00 18.18 ? 204 LEU A CG  1 
ATOM   1698 C  CD1 . LEU A 1 203 ? 21.194 11.117  18.785  1.00 21.68 ? 204 LEU A CD1 1 
ATOM   1699 C  CD2 . LEU A 1 203 ? 22.994 10.786  20.568  1.00 21.04 ? 204 LEU A CD2 1 
ATOM   1700 N  N   . GLU A 1 204 ? 20.531 8.455   23.861  1.00 15.80 ? 205 GLU A N   1 
ATOM   1701 C  CA  . GLU A 1 204 ? 19.730 8.064   24.984  1.00 15.59 ? 205 GLU A CA  1 
ATOM   1702 C  C   . GLU A 1 204 ? 18.543 9.030   25.109  1.00 17.82 ? 205 GLU A C   1 
ATOM   1703 O  O   . GLU A 1 204 ? 18.442 9.784   26.104  1.00 18.53 ? 205 GLU A O   1 
ATOM   1704 C  CB  . GLU A 1 204 ? 20.590 7.943   26.251  1.00 18.25 ? 205 GLU A CB  1 
ATOM   1705 C  CG  . GLU A 1 204 ? 21.372 6.607   26.176  1.00 15.55 ? 205 GLU A CG  1 
ATOM   1706 C  CD  . GLU A 1 204 ? 22.371 6.389   27.285  1.00 19.59 ? 205 GLU A CD  1 
ATOM   1707 O  OE1 . GLU A 1 204 ? 22.639 7.346   28.058  1.00 21.58 ? 205 GLU A OE1 1 
ATOM   1708 O  OE2 . GLU A 1 204 ? 22.844 5.239   27.414  1.00 16.52 ? 205 GLU A OE2 1 
ATOM   1709 N  N   . CYS A 1 205 ? 17.634 8.968   24.115  1.00 14.26 ? 206 CYS A N   1 
ATOM   1710 C  CA  . CYS A 1 205 ? 16.587 9.976   23.938  1.00 13.49 ? 206 CYS A CA  1 
ATOM   1711 C  C   . CYS A 1 205 ? 15.222 9.330   23.788  1.00 13.49 ? 206 CYS A C   1 
ATOM   1712 O  O   . CYS A 1 205 ? 14.297 10.010  23.374  1.00 12.43 ? 206 CYS A O   1 
ATOM   1713 C  CB  . CYS A 1 205 ? 16.885 10.780  22.661  1.00 12.74 ? 206 CYS A CB  1 
ATOM   1714 S  SG  . CYS A 1 205 ? 16.909 9.821   21.101  1.00 14.85 ? 206 CYS A SG  1 
ATOM   1715 N  N   . VAL A 1 206 ? 15.109 8.026   24.060  1.00 11.33 ? 207 VAL A N   1 
ATOM   1716 C  CA  . VAL A 1 206 ? 13.834 7.302   23.738  1.00 11.42 ? 207 VAL A CA  1 
ATOM   1717 C  C   . VAL A 1 206 ? 13.054 6.858   24.971  1.00 11.64 ? 207 VAL A C   1 
ATOM   1718 O  O   . VAL A 1 206 ? 13.589 6.228   25.918  1.00 14.01 ? 207 VAL A O   1 
ATOM   1719 C  CB  . VAL A 1 206 ? 14.155 6.033   22.866  1.00 10.96 ? 207 VAL A CB  1 
ATOM   1720 C  CG1 . VAL A 1 206 ? 12.784 5.351   22.597  1.00 12.84 ? 207 VAL A CG1 1 
ATOM   1721 C  CG2 . VAL A 1 206 ? 14.939 6.381   21.565  1.00 11.35 ? 207 VAL A CG2 1 
ATOM   1722 N  N   . THR A 1 207 ? 11.763 7.164   25.013  1.00 10.54 ? 208 THR A N   1 
ATOM   1723 C  CA  . THR A 1 207 ? 10.867 6.471   25.889  1.00 10.34 ? 208 THR A CA  1 
ATOM   1724 C  C   . THR A 1 207 ? 10.322 5.290   25.103  1.00 10.89 ? 208 THR A C   1 
ATOM   1725 O  O   . THR A 1 207 ? 9.668  5.502   24.078  1.00 10.34 ? 208 THR A O   1 
ATOM   1726 C  CB  . THR A 1 207 ? 9.667  7.363   26.341  1.00 12.13 ? 208 THR A CB  1 
ATOM   1727 O  OG1 . THR A 1 207 ? 10.156 8.430   27.155  1.00 12.70 ? 208 THR A OG1 1 
ATOM   1728 C  CG2 . THR A 1 207 ? 8.751  6.531   27.218  1.00 11.51 ? 208 THR A CG2 1 
ATOM   1729 N  N   . TRP A 1 208 ? 10.626 4.072   25.551  1.00 11.02 ? 209 TRP A N   1 
ATOM   1730 C  CA  . TRP A 1 208 ? 10.194 2.884   24.805  1.00 10.09 ? 209 TRP A CA  1 
ATOM   1731 C  C   . TRP A 1 208 ? 8.841  2.411   25.296  1.00 11.13 ? 209 TRP A C   1 
ATOM   1732 O  O   . TRP A 1 208 ? 8.634  2.380   26.507  1.00 12.00 ? 209 TRP A O   1 
ATOM   1733 C  CB  . TRP A 1 208 ? 11.218 1.703   24.986  1.00 10.84 ? 209 TRP A CB  1 
ATOM   1734 C  CG  . TRP A 1 208 ? 12.332 1.833   24.048  1.00 10.68 ? 209 TRP A CG  1 
ATOM   1735 C  CD1 . TRP A 1 208 ? 13.626 2.361   24.240  1.00 10.46 ? 209 TRP A CD1 1 
ATOM   1736 C  CD2 . TRP A 1 208 ? 12.277 1.441   22.651  1.00 10.85 ? 209 TRP A CD2 1 
ATOM   1737 N  NE1 . TRP A 1 208 ? 14.292 2.389   23.061  1.00 10.51 ? 209 TRP A NE1 1 
ATOM   1738 C  CE2 . TRP A 1 208 ? 13.575 1.764   22.084  1.00 10.80 ? 209 TRP A CE2 1 
ATOM   1739 C  CE3 . TRP A 1 208 ? 11.287 0.800   21.844  1.00 10.51 ? 209 TRP A CE3 1 
ATOM   1740 C  CZ2 . TRP A 1 208 ? 13.853 1.573   20.743  1.00 10.42 ? 209 TRP A CZ2 1 
ATOM   1741 C  CZ3 . TRP A 1 208 ? 11.580 0.560   20.524  1.00 11.40 ? 209 TRP A CZ3 1 
ATOM   1742 C  CH2 . TRP A 1 208 ? 12.865 0.896   19.976  1.00 10.76 ? 209 TRP A CH2 1 
ATOM   1743 N  N   . ILE A 1 209 ? 7.957  2.124   24.367  1.00 11.24 ? 210 ILE A N   1 
ATOM   1744 C  CA  . ILE A 1 209 ? 6.586  1.595   24.725  1.00 10.48 ? 210 ILE A CA  1 
ATOM   1745 C  C   . ILE A 1 209 ? 6.522  0.336   23.874  1.00 9.69  ? 210 ILE A C   1 
ATOM   1746 O  O   . ILE A 1 209 ? 6.420  0.447   22.675  1.00 10.39 ? 210 ILE A O   1 
ATOM   1747 C  CB  . ILE A 1 209 ? 5.495  2.611   24.371  1.00 11.53 ? 210 ILE A CB  1 
ATOM   1748 C  CG1 . ILE A 1 209 ? 5.755  3.939   25.166  1.00 13.50 ? 210 ILE A CG1 1 
ATOM   1749 C  CG2 . ILE A 1 209 ? 4.106  2.011   24.701  1.00 12.16 ? 210 ILE A CG2 1 
ATOM   1750 C  CD1 . ILE A 1 209 ? 4.995  5.195   24.642  1.00 14.99 ? 210 ILE A CD1 1 
ATOM   1751 N  N   . VAL A 1 210 ? 6.543  -0.838  24.480  1.00 10.59 ? 211 VAL A N   1 
ATOM   1752 C  CA  . VAL A 1 210 ? 6.551  -2.112  23.752  1.00 10.05 ? 211 VAL A CA  1 
ATOM   1753 C  C   . VAL A 1 210 ? 5.211  -2.810  24.040  1.00 9.93  ? 211 VAL A C   1 
ATOM   1754 O  O   . VAL A 1 210 ? 4.893  -3.061  25.196  1.00 12.32 ? 211 VAL A O   1 
ATOM   1755 C  CB  . VAL A 1 210 ? 7.732  -2.985  24.227  1.00 9.24  ? 211 VAL A CB  1 
ATOM   1756 C  CG1 . VAL A 1 210 ? 7.743  -4.305  23.427  1.00 10.00 ? 211 VAL A CG1 1 
ATOM   1757 C  CG2 . VAL A 1 210 ? 9.073  -2.250  23.934  1.00 9.66  ? 211 VAL A CG2 1 
ATOM   1758 N  N   . LEU A 1 211 ? 4.473  -3.100  22.993  1.00 10.83 ? 212 LEU A N   1 
ATOM   1759 C  CA  . LEU A 1 211 ? 3.139  -3.749  23.150  1.00 11.06 ? 212 LEU A CA  1 
ATOM   1760 C  C   . LEU A 1 211 ? 3.357  -5.196  23.537  1.00 12.17 ? 212 LEU A C   1 
ATOM   1761 O  O   . LEU A 1 211 ? 4.253  -5.851  23.014  1.00 14.05 ? 212 LEU A O   1 
ATOM   1762 C  CB  . LEU A 1 211 ? 2.368  -3.674  21.845  1.00 11.00 ? 212 LEU A CB  1 
ATOM   1763 C  CG  . LEU A 1 211 ? 1.961  -2.220  21.427  1.00 13.48 ? 212 LEU A CG  1 
ATOM   1764 C  CD1 . LEU A 1 211 ? 0.855  -2.268  20.349  1.00 15.10 ? 212 LEU A CD1 1 
ATOM   1765 C  CD2 . LEU A 1 211 ? 1.628  -1.319  22.639  1.00 12.03 ? 212 LEU A CD2 1 
ATOM   1766 N  N   . LYS A 1 212 ? 2.487  -5.680  24.466  1.00 13.07 ? 213 LYS A N   1 
ATOM   1767 C  CA  . LYS A 1 212 ? 2.538  -7.084  24.907  1.00 14.39 ? 213 LYS A CA  1 
ATOM   1768 C  C   . LYS A 1 212 ? 2.050  -8.015  23.817  1.00 13.77 ? 213 LYS A C   1 
ATOM   1769 O  O   . LYS A 1 212 ? 2.554  -9.113  23.633  1.00 14.59 ? 213 LYS A O   1 
ATOM   1770 C  CB  . LYS A 1 212 ? 1.738  -7.252  26.224  1.00 17.60 ? 213 LYS A CB  1 
ATOM   1771 C  CG  . LYS A 1 212 ? 1.429  -8.712  26.656  1.00 22.02 ? 213 LYS A CG  1 
ATOM   1772 C  CD  . LYS A 1 212 ? 0.305  -8.750  27.719  1.00 29.45 ? 213 LYS A CD  1 
ATOM   1773 C  CE  . LYS A 1 212 ? -1.164 -8.570  27.216  1.00 33.73 ? 213 LYS A CE  1 
ATOM   1774 N  NZ  . LYS A 1 212 ? -1.556 -7.744  25.994  1.00 35.09 ? 213 LYS A NZ  1 
ATOM   1775 N  N   . GLU A 1 213 ? 1.072  -7.578  23.065  1.00 13.73 ? 214 GLU A N   1 
ATOM   1776 C  CA  . GLU A 1 213 ? 0.450  -8.475  22.052  1.00 14.41 ? 214 GLU A CA  1 
ATOM   1777 C  C   . GLU A 1 213 ? 1.162  -8.387  20.720  1.00 13.82 ? 214 GLU A C   1 
ATOM   1778 O  O   . GLU A 1 213 ? 1.190  -7.323  20.107  1.00 12.38 ? 214 GLU A O   1 
ATOM   1779 C  CB  . GLU A 1 213 ? -1.009 -8.080  21.821  1.00 13.97 ? 214 GLU A CB  1 
ATOM   1780 C  CG  . GLU A 1 213 ? -1.713 -9.032  20.858  1.00 16.86 ? 214 GLU A CG  1 
ATOM   1781 C  CD  . GLU A 1 213 ? -3.202 -8.652  20.648  1.00 23.44 ? 214 GLU A CD  1 
ATOM   1782 O  OE1 . GLU A 1 213 ? -3.758 -8.029  21.537  1.00 23.74 ? 214 GLU A OE1 1 
ATOM   1783 O  OE2 . GLU A 1 213 ? -3.797 -8.985  19.595  1.00 33.36 ? 214 GLU A OE2 1 
ATOM   1784 N  N   . PRO A 1 214 ? 1.793  -9.481  20.243  1.00 12.77 ? 215 PRO A N   1 
ATOM   1785 C  CA  . PRO A 1 214 ? 2.418  -9.440  18.913  1.00 13.24 ? 215 PRO A CA  1 
ATOM   1786 C  C   . PRO A 1 214 ? 1.371  -9.434  17.790  1.00 14.46 ? 215 PRO A C   1 
ATOM   1787 O  O   . PRO A 1 214 ? 0.145  -9.791  18.034  1.00 14.99 ? 215 PRO A O   1 
ATOM   1788 C  CB  . PRO A 1 214 ? 3.243  -10.773 18.825  1.00 13.77 ? 215 PRO A CB  1 
ATOM   1789 C  CG  . PRO A 1 214 ? 2.465  -11.710 19.751  1.00 16.86 ? 215 PRO A CG  1 
ATOM   1790 C  CD  . PRO A 1 214 ? 1.805  -10.850 20.852  1.00 14.44 ? 215 PRO A CD  1 
ATOM   1791 N  N   . ILE A 1 215 ? 1.811  -9.017  16.624  1.00 13.59 ? 216 ILE A N   1 
ATOM   1792 C  CA  . ILE A 1 215 ? 1.001  -9.213  15.443  1.00 14.68 ? 216 ILE A CA  1 
ATOM   1793 C  C   . ILE A 1 215 ? 1.535  -10.473 14.761  1.00 14.41 ? 216 ILE A C   1 
ATOM   1794 O  O   . ILE A 1 215 ? 2.727  -10.814 14.847  1.00 15.56 ? 216 ILE A O   1 
ATOM   1795 C  CB  . ILE A 1 215 ? 1.016  -7.993  14.459  1.00 14.10 ? 216 ILE A CB  1 
ATOM   1796 C  CG1 . ILE A 1 215 ? 2.435  -7.633  13.931  1.00 15.02 ? 216 ILE A CG1 1 
ATOM   1797 C  CG2 . ILE A 1 215 ? 0.253  -6.775  15.103  1.00 15.49 ? 216 ILE A CG2 1 
ATOM   1798 C  CD1 . ILE A 1 215 ? 2.475  -6.679  12.684  1.00 13.84 ? 216 ILE A CD1 1 
ATOM   1799 N  N   A SER A 1 216 ? 0.622  -11.118 14.020  0.50 14.01 ? 217 SER A N   1 
ATOM   1800 N  N   B SER A 1 216 ? 0.661  -11.149 14.046  0.50 14.59 ? 217 SER A N   1 
ATOM   1801 C  CA  A SER A 1 216 ? 0.925  -12.269 13.136  0.50 13.73 ? 217 SER A CA  1 
ATOM   1802 C  CA  B SER A 1 216 ? 1.160  -12.250 13.257  0.50 14.42 ? 217 SER A CA  1 
ATOM   1803 C  C   A SER A 1 216 ? 1.209  -11.817 11.682  0.50 14.40 ? 217 SER A C   1 
ATOM   1804 C  C   B SER A 1 216 ? 1.223  -11.865 11.773  0.50 15.09 ? 217 SER A C   1 
ATOM   1805 O  O   A SER A 1 216 ? 0.468  -11.003 11.075  0.50 15.02 ? 217 SER A O   1 
ATOM   1806 O  O   B SER A 1 216 ? 0.350  -11.113 11.264  0.50 16.36 ? 217 SER A O   1 
ATOM   1807 C  CB  A SER A 1 216 ? -0.228 -13.299 13.212  0.50 13.87 ? 217 SER A CB  1 
ATOM   1808 C  CB  B SER A 1 216 ? 0.370  -13.490 13.557  0.50 15.77 ? 217 SER A CB  1 
ATOM   1809 O  OG  A SER A 1 216 ? -0.127 -14.030 14.464  0.50 15.40 ? 217 SER A OG  1 
ATOM   1810 O  OG  B SER A 1 216 ? 0.062  -14.181 12.402  0.50 17.33 ? 217 SER A OG  1 
ATOM   1811 N  N   . VAL A 1 217 ? 2.300  -12.300 11.133  1.00 14.08 ? 218 VAL A N   1 
ATOM   1812 C  CA  . VAL A 1 217 ? 2.570  -12.061 9.727   1.00 13.15 ? 218 VAL A CA  1 
ATOM   1813 C  C   . VAL A 1 217 ? 2.835  -13.434 9.121   1.00 13.06 ? 218 VAL A C   1 
ATOM   1814 O  O   . VAL A 1 217 ? 3.175  -14.361 9.838   1.00 14.58 ? 218 VAL A O   1 
ATOM   1815 C  CB  . VAL A 1 217 ? 3.778  -11.132 9.470   1.00 13.58 ? 218 VAL A CB  1 
ATOM   1816 C  CG1 . VAL A 1 217 ? 3.513  -9.829  10.155  1.00 13.69 ? 218 VAL A CG1 1 
ATOM   1817 C  CG2 . VAL A 1 217 ? 5.080  -11.770 9.950   1.00 13.28 ? 218 VAL A CG2 1 
ATOM   1818 N  N   . SER A 1 218 ? 2.627  -13.586 7.831   1.00 13.36 ? 219 SER A N   1 
ATOM   1819 C  CA  . SER A 1 218 ? 2.886  -14.897 7.243   1.00 14.09 ? 219 SER A CA  1 
ATOM   1820 C  C   . SER A 1 218 ? 4.361  -15.180 6.958   1.00 13.56 ? 219 SER A C   1 
ATOM   1821 O  O   . SER A 1 218 ? 5.210  -14.285 6.856   1.00 13.94 ? 219 SER A O   1 
ATOM   1822 C  CB  . SER A 1 218 ? 2.103  -15.109 5.967   1.00 14.23 ? 219 SER A CB  1 
ATOM   1823 O  OG  . SER A 1 218 ? 2.629  -14.321 4.915   1.00 17.58 ? 219 SER A OG  1 
ATOM   1824 N  N   A SER A 1 219 ? 4.697  -16.454 6.823   0.50 13.81 ? 220 SER A N   1 
ATOM   1825 N  N   B SER A 1 219 ? 4.664  -16.457 6.823   0.50 13.41 ? 220 SER A N   1 
ATOM   1826 C  CA  A SER A 1 219 ? 6.068  -16.786 6.490   0.50 14.75 ? 220 SER A CA  1 
ATOM   1827 C  CA  B SER A 1 219 ? 5.998  -16.855 6.471   0.50 14.28 ? 220 SER A CA  1 
ATOM   1828 C  C   A SER A 1 219 ? 6.439  -16.143 5.133   0.50 15.97 ? 220 SER A C   1 
ATOM   1829 C  C   B SER A 1 219 ? 6.416  -16.169 5.152   0.50 15.54 ? 220 SER A C   1 
ATOM   1830 O  O   A SER A 1 219 ? 7.592  -15.683 4.978   0.50 16.24 ? 220 SER A O   1 
ATOM   1831 O  O   B SER A 1 219 ? 7.576  -15.705 5.045   0.50 15.92 ? 220 SER A O   1 
ATOM   1832 C  CB  A SER A 1 219 ? 6.278  -18.318 6.493   0.50 16.06 ? 220 SER A CB  1 
ATOM   1833 C  CB  B SER A 1 219 ? 6.045  -18.395 6.363   0.50 14.39 ? 220 SER A CB  1 
ATOM   1834 O  OG  A SER A 1 219 ? 5.403  -18.950 5.583   0.50 16.42 ? 220 SER A OG  1 
ATOM   1835 O  OG  B SER A 1 219 ? 7.369  -18.815 6.134   0.50 14.52 ? 220 SER A OG  1 
ATOM   1836 N  N   . GLU A 1 220 ? 5.500  -16.097 4.165   1.00 15.40 ? 221 GLU A N   1 
ATOM   1837 C  CA  . GLU A 1 220 ? 5.780  -15.479 2.832   1.00 17.19 ? 221 GLU A CA  1 
ATOM   1838 C  C   . GLU A 1 220 ? 6.099  -13.956 2.997   1.00 15.23 ? 221 GLU A C   1 
ATOM   1839 O  O   . GLU A 1 220 ? 6.984  -13.428 2.313   1.00 15.10 ? 221 GLU A O   1 
ATOM   1840 C  CB  . GLU A 1 220 ? 4.647  -15.629 1.877   1.00 19.58 ? 221 GLU A CB  1 
ATOM   1841 C  CG  . GLU A 1 220 ? 4.487  -17.083 1.474   1.00 23.90 ? 221 GLU A CG  1 
ATOM   1842 C  CD  . GLU A 1 220 ? 3.495  -17.818 2.343   1.00 30.22 ? 221 GLU A CD  1 
ATOM   1843 O  OE1 . GLU A 1 220 ? 3.118  -17.392 3.475   1.00 25.98 ? 221 GLU A OE1 1 
ATOM   1844 O  OE2 . GLU A 1 220 ? 3.042  -18.880 1.858   1.00 35.66 ? 221 GLU A OE2 1 
ATOM   1845 N  N   . GLN A 1 221 ? 5.375  -13.309 3.916   1.00 15.39 ? 222 GLN A N   1 
ATOM   1846 C  CA  . GLN A 1 221 ? 5.639  -11.855 4.174   1.00 14.60 ? 222 GLN A CA  1 
ATOM   1847 C  C   . GLN A 1 221 ? 7.050  -11.624 4.716   1.00 15.54 ? 222 GLN A C   1 
ATOM   1848 O  O   . GLN A 1 221 ? 7.810  -10.813 4.199   1.00 14.77 ? 222 GLN A O   1 
ATOM   1849 C  CB  . GLN A 1 221 ? 4.585  -11.268 5.097   1.00 15.80 ? 222 GLN A CB  1 
ATOM   1850 C  CG  . GLN A 1 221 ? 3.236  -11.129 4.384   1.00 15.17 ? 222 GLN A CG  1 
ATOM   1851 C  CD  . GLN A 1 221 ? 2.131  -10.601 5.248   1.00 15.50 ? 222 GLN A CD  1 
ATOM   1852 O  OE1 . GLN A 1 221 ? 2.009  -10.951 6.409   1.00 14.41 ? 222 GLN A OE1 1 
ATOM   1853 N  NE2 . GLN A 1 221 ? 1.331  -9.691  4.691   1.00 14.62 ? 222 GLN A NE2 1 
ATOM   1854 N  N   . VAL A 1 222 ? 7.446  -12.422 5.730   1.00 14.60 ? 223 VAL A N   1 
ATOM   1855 C  CA  . VAL A 1 222 ? 8.781  -12.181 6.308   1.00 15.25 ? 223 VAL A CA  1 
ATOM   1856 C  C   . VAL A 1 222 ? 9.909  -12.657 5.353   1.00 15.12 ? 223 VAL A C   1 
ATOM   1857 O  O   . VAL A 1 222 ? 11.020 -12.072 5.256   1.00 14.38 ? 223 VAL A O   1 
ATOM   1858 C  CB  . VAL A 1 222 ? 8.900  -12.757 7.732   1.00 17.25 ? 223 VAL A CB  1 
ATOM   1859 C  CG1 . VAL A 1 222 ? 9.014  -14.272 7.739   1.00 18.68 ? 223 VAL A CG1 1 
ATOM   1860 C  CG2 . VAL A 1 222 ? 10.118 -12.133 8.437   1.00 17.13 ? 223 VAL A CG2 1 
ATOM   1861 N  N   . LEU A 1 223 ? 9.631  -13.705 4.565   1.00 16.07 ? 224 LEU A N   1 
ATOM   1862 C  CA  . LEU A 1 223 ? 10.585 -14.129 3.536   1.00 16.87 ? 224 LEU A CA  1 
ATOM   1863 C  C   . LEU A 1 223 ? 10.894 -13.007 2.538   1.00 17.20 ? 224 LEU A C   1 
ATOM   1864 O  O   . LEU A 1 223 ? 12.037 -12.900 2.078   1.00 18.32 ? 224 LEU A O   1 
ATOM   1865 C  CB  . LEU A 1 223 ? 10.051 -15.360 2.796   1.00 18.17 ? 224 LEU A CB  1 
ATOM   1866 C  CG  . LEU A 1 223 ? 10.429 -16.640 3.522   1.00 23.60 ? 224 LEU A CG  1 
ATOM   1867 C  CD1 . LEU A 1 223 ? 9.376  -17.724 3.162   1.00 29.10 ? 224 LEU A CD1 1 
ATOM   1868 C  CD2 . LEU A 1 223 ? 11.804 -16.970 2.944   1.00 27.52 ? 224 LEU A CD2 1 
ATOM   1869 N  N   . LYS A 1 224 ? 9.884  -12.198 2.210   1.00 17.23 ? 225 LYS A N   1 
ATOM   1870 C  CA  . LYS A 1 224 ? 10.140 -11.081 1.329   1.00 17.86 ? 225 LYS A CA  1 
ATOM   1871 C  C   . LYS A 1 224 ? 11.023 -9.981  1.991   1.00 15.35 ? 225 LYS A C   1 
ATOM   1872 O  O   . LYS A 1 224 ? 11.843 -9.389  1.302   1.00 18.23 ? 225 LYS A O   1 
ATOM   1873 C  CB  . LYS A 1 224 ? 8.819  -10.574 0.774   1.00 17.06 ? 225 LYS A CB  1 
ATOM   1874 C  CG  . LYS A 1 224 ? 8.234  -11.662 -0.141  1.00 21.81 ? 225 LYS A CG  1 
ATOM   1875 C  CD  . LYS A 1 224 ? 7.321  -11.106 -1.213  1.00 28.17 ? 225 LYS A CD  1 
ATOM   1876 C  CE  . LYS A 1 224 ? 6.520  -12.249 -1.860  1.00 31.92 ? 225 LYS A CE  1 
ATOM   1877 N  NZ  . LYS A 1 224 ? 5.154  -11.843 -2.329  1.00 36.69 ? 225 LYS A NZ  1 
ATOM   1878 N  N   . PHE A 1 225 ? 10.889 -9.710  3.299   1.00 13.13 ? 226 PHE A N   1 
ATOM   1879 C  CA  . PHE A 1 225 ? 11.879 -8.847  3.990   1.00 13.94 ? 226 PHE A CA  1 
ATOM   1880 C  C   . PHE A 1 225 ? 13.278 -9.335  3.804   1.00 13.00 ? 226 PHE A C   1 
ATOM   1881 O  O   . PHE A 1 225 ? 14.221 -8.567  3.592   1.00 13.36 ? 226 PHE A O   1 
ATOM   1882 C  CB  . PHE A 1 225 ? 11.670 -8.871  5.537   1.00 13.72 ? 226 PHE A CB  1 
ATOM   1883 C  CG  . PHE A 1 225 ? 10.456 -8.073  6.050   1.00 14.51 ? 226 PHE A CG  1 
ATOM   1884 C  CD1 . PHE A 1 225 ? 9.378  -7.677  5.247   1.00 15.93 ? 226 PHE A CD1 1 
ATOM   1885 C  CD2 . PHE A 1 225 ? 10.404 -7.805  7.426   1.00 18.11 ? 226 PHE A CD2 1 
ATOM   1886 C  CE1 . PHE A 1 225 ? 8.322  -6.957  5.832   1.00 16.49 ? 226 PHE A CE1 1 
ATOM   1887 C  CE2 . PHE A 1 225 ? 9.370  -7.093  8.023   1.00 18.12 ? 226 PHE A CE2 1 
ATOM   1888 C  CZ  . PHE A 1 225 ? 8.333  -6.643  7.201   1.00 18.01 ? 226 PHE A CZ  1 
ATOM   1889 N  N   . ARG A 1 226 ? 13.452 -10.666 3.874   1.00 14.39 ? 227 ARG A N   1 
ATOM   1890 C  CA  . ARG A 1 226 ? 14.767 -11.287 3.782   1.00 14.80 ? 227 ARG A CA  1 
ATOM   1891 C  C   . ARG A 1 226 ? 15.425 -11.292 2.383   1.00 15.16 ? 227 ARG A C   1 
ATOM   1892 O  O   . ARG A 1 226 ? 16.563 -11.663 2.275   1.00 16.98 ? 227 ARG A O   1 
ATOM   1893 C  CB  . ARG A 1 226 ? 14.683 -12.776 4.307   1.00 13.59 ? 227 ARG A CB  1 
ATOM   1894 C  CG  . ARG A 1 226 ? 14.284 -12.900 5.759   1.00 14.05 ? 227 ARG A CG  1 
ATOM   1895 C  CD  . ARG A 1 226 ? 14.438 -14.337 6.258   1.00 13.75 ? 227 ARG A CD  1 
ATOM   1896 N  NE  . ARG A 1 226 ? 13.802 -14.441 7.594   1.00 16.14 ? 227 ARG A NE  1 
ATOM   1897 C  CZ  . ARG A 1 226 ? 12.796 -15.288 7.898   1.00 16.82 ? 227 ARG A CZ  1 
ATOM   1898 N  NH1 . ARG A 1 226 ? 12.408 -16.211 6.975   1.00 16.78 ? 227 ARG A NH1 1 
ATOM   1899 N  NH2 . ARG A 1 226 ? 12.235 -15.277 9.112   1.00 16.85 ? 227 ARG A NH2 1 
ATOM   1900 N  N   . LYS A 1 227 ? 14.695 -10.840 1.374   1.00 17.34 ? 228 LYS A N   1 
ATOM   1901 C  CA  . LYS A 1 227 ? 15.205 -10.752 0.010   1.00 18.56 ? 228 LYS A CA  1 
ATOM   1902 C  C   . LYS A 1 227 ? 15.835 -9.370  -0.230  1.00 17.42 ? 228 LYS A C   1 
ATOM   1903 O  O   . LYS A 1 227 ? 16.476 -9.156  -1.255  1.00 19.05 ? 228 LYS A O   1 
ATOM   1904 C  CB  . LYS A 1 227 ? 14.085 -10.968 -0.988  1.00 19.88 ? 228 LYS A CB  1 
ATOM   1905 C  CG  . LYS A 1 227 ? 13.642 -12.417 -1.130  1.00 22.69 ? 228 LYS A CG  1 
ATOM   1906 C  CD  . LYS A 1 227 ? 12.430 -12.466 -2.082  1.00 33.34 ? 228 LYS A CD  1 
ATOM   1907 C  CE  . LYS A 1 227 ? 12.728 -11.934 -3.502  1.00 40.76 ? 228 LYS A CE  1 
ATOM   1908 N  NZ  . LYS A 1 227 ? 13.134 -12.940 -4.548  1.00 45.47 ? 228 LYS A NZ  1 
ATOM   1909 N  N   . LEU A 1 228 ? 15.611 -8.443  0.696   1.00 16.60 ? 229 LEU A N   1 
ATOM   1910 C  CA  . LEU A 1 228 ? 16.312 -7.146  0.575   1.00 15.73 ? 229 LEU A CA  1 
ATOM   1911 C  C   . LEU A 1 228 ? 17.796 -7.332  0.731   1.00 15.55 ? 229 LEU A C   1 
ATOM   1912 O  O   . LEU A 1 228 ? 18.272 -8.338  1.209   1.00 14.65 ? 229 LEU A O   1 
ATOM   1913 C  CB  . LEU A 1 228 ? 15.825 -6.219  1.707   1.00 14.17 ? 229 LEU A CB  1 
ATOM   1914 C  CG  . LEU A 1 228 ? 14.399 -5.757  1.557   1.00 16.16 ? 229 LEU A CG  1 
ATOM   1915 C  CD1 . LEU A 1 228 ? 13.934 -5.052  2.828   1.00 15.01 ? 229 LEU A CD1 1 
ATOM   1916 C  CD2 . LEU A 1 228 ? 14.355 -4.731  0.415   1.00 17.69 ? 229 LEU A CD2 1 
ATOM   1917 N  N   . ASN A 1 229 ? 18.584 -6.307  0.400   1.00 18.12 ? 230 ASN A N   1 
ATOM   1918 C  CA  . ASN A 1 229 ? 20.027 -6.384  0.471   1.00 17.10 ? 230 ASN A CA  1 
ATOM   1919 C  C   . ASN A 1 229 ? 20.587 -5.203  1.360   1.00 18.37 ? 230 ASN A C   1 
ATOM   1920 O  O   . ASN A 1 229 ? 20.071 -4.040  1.233   1.00 17.97 ? 230 ASN A O   1 
ATOM   1921 C  CB  . ASN A 1 229 ? 20.674 -6.116  -0.925  1.00 20.98 ? 230 ASN A CB  1 
ATOM   1922 C  CG  . ASN A 1 229 ? 20.504 -7.251  -1.923  1.00 23.21 ? 230 ASN A CG  1 
ATOM   1923 O  OD1 . ASN A 1 229 ? 21.015 -7.138  -3.048  1.00 22.50 ? 230 ASN A OD1 1 
ATOM   1924 N  ND2 . ASN A 1 229 ? 19.849 -8.361  -1.526  1.00 20.91 ? 230 ASN A ND2 1 
ATOM   1925 N  N   . PHE A 1 230 ? 21.637 -5.536  2.127   1.00 18.45 ? 231 PHE A N   1 
ATOM   1926 C  CA  . PHE A 1 230 ? 22.484 -4.507  2.864   1.00 18.85 ? 231 PHE A CA  1 
ATOM   1927 C  C   . PHE A 1 230 ? 23.321 -3.712  1.860   1.00 23.35 ? 231 PHE A C   1 
ATOM   1928 O  O   . PHE A 1 230 ? 23.594 -2.513  2.074   1.00 23.15 ? 231 PHE A O   1 
ATOM   1929 C  CB  . PHE A 1 230 ? 23.442 -5.175  3.763   1.00 21.83 ? 231 PHE A CB  1 
ATOM   1930 C  CG  . PHE A 1 230 ? 22.838 -5.696  5.061   1.00 21.48 ? 231 PHE A CG  1 
ATOM   1931 C  CD1 . PHE A 1 230 ? 22.005 -4.859  5.848   1.00 18.89 ? 231 PHE A CD1 1 
ATOM   1932 C  CD2 . PHE A 1 230 ? 23.151 -6.977  5.500   1.00 22.48 ? 231 PHE A CD2 1 
ATOM   1933 C  CE1 . PHE A 1 230 ? 21.493 -5.334  7.083   1.00 19.80 ? 231 PHE A CE1 1 
ATOM   1934 C  CE2 . PHE A 1 230 ? 22.671 -7.473  6.705   1.00 18.62 ? 231 PHE A CE2 1 
ATOM   1935 C  CZ  . PHE A 1 230 ? 21.814 -6.646  7.481   1.00 17.96 ? 231 PHE A CZ  1 
ATOM   1936 N  N   . ASN A 1 231 ? 23.767 -4.384  0.812   1.00 22.21 ? 232 ASN A N   1 
ATOM   1937 C  CA  . ASN A 1 231 ? 24.685 -3.730  -0.147  1.00 24.57 ? 232 ASN A CA  1 
ATOM   1938 C  C   . ASN A 1 231 ? 23.976 -2.812  -1.115  1.00 22.99 ? 232 ASN A C   1 
ATOM   1939 O  O   . ASN A 1 231 ? 22.757 -2.890  -1.317  1.00 23.47 ? 232 ASN A O   1 
ATOM   1940 C  CB  . ASN A 1 231 ? 25.392 -4.810  -0.922  1.00 24.10 ? 232 ASN A CB  1 
ATOM   1941 C  CG  . ASN A 1 231 ? 24.400 -5.732  -1.585  1.00 25.33 ? 232 ASN A CG  1 
ATOM   1942 O  OD1 . ASN A 1 231 ? 23.945 -6.683  -0.963  1.00 26.25 ? 232 ASN A OD1 1 
ATOM   1943 N  ND2 . ASN A 1 231 ? 24.049 -5.451  -2.843  1.00 25.92 ? 232 ASN A ND2 1 
ATOM   1944 N  N   . GLY A 1 232 ? 24.732 -1.900  -1.741  1.00 24.23 ? 233 GLY A N   1 
ATOM   1945 C  CA  . GLY A 1 232 ? 24.182 -1.111  -2.825  1.00 26.03 ? 233 GLY A CA  1 
ATOM   1946 C  C   . GLY A 1 232 ? 24.261 -1.875  -4.143  1.00 27.50 ? 233 GLY A C   1 
ATOM   1947 O  O   . GLY A 1 232 ? 25.039 -2.850  -4.244  1.00 25.47 ? 233 GLY A O   1 
ATOM   1948 N  N   . GLU A 1 233 ? 23.449 -1.401  -5.101  1.00 28.86 ? 234 GLU A N   1 
ATOM   1949 C  CA  . GLU A 1 233 ? 23.327 -1.903  -6.471  1.00 31.77 ? 234 GLU A CA  1 
ATOM   1950 C  C   . GLU A 1 233 ? 24.703 -1.992  -7.075  1.00 32.99 ? 234 GLU A C   1 
ATOM   1951 O  O   . GLU A 1 233 ? 25.468 -1.040  -7.013  1.00 30.49 ? 234 GLU A O   1 
ATOM   1952 C  CB  . GLU A 1 233 ? 22.426 -1.005  -7.313  1.00 30.32 ? 234 GLU A CB  1 
ATOM   1953 C  CG  . GLU A 1 233 ? 22.135 -1.569  -8.711  1.00 37.76 ? 234 GLU A CG  1 
ATOM   1954 C  CD  . GLU A 1 233 ? 21.274 -0.664  -9.581  1.00 41.59 ? 234 GLU A CD  1 
ATOM   1955 O  OE1 . GLU A 1 233 ? 20.855 0.415   -9.106  1.00 48.27 ? 234 GLU A OE1 1 
ATOM   1956 O  OE2 . GLU A 1 233 ? 21.043 -1.004  -10.769 1.00 44.51 ? 234 GLU A OE2 1 
ATOM   1957 N  N   . GLY A 1 234 ? 25.038 -3.183  -7.558  1.00 33.13 ? 235 GLY A N   1 
ATOM   1958 C  CA  . GLY A 1 234 ? 26.340 -3.448  -8.139  1.00 36.30 ? 235 GLY A CA  1 
ATOM   1959 C  C   . GLY A 1 234 ? 27.464 -3.830  -7.208  1.00 40.89 ? 235 GLY A C   1 
ATOM   1960 O  O   . GLY A 1 234 ? 28.616 -3.742  -7.631  1.00 40.22 ? 235 GLY A O   1 
ATOM   1961 N  N   . GLU A 1 235 ? 27.169 -4.236  -5.948  1.00 36.40 ? 236 GLU A N   1 
ATOM   1962 C  CA  . GLU A 1 235 ? 28.190 -4.785  -5.022  1.00 35.07 ? 236 GLU A CA  1 
ATOM   1963 C  C   . GLU A 1 235 ? 27.886 -6.263  -4.715  1.00 31.00 ? 236 GLU A C   1 
ATOM   1964 O  O   . GLU A 1 235 ? 26.783 -6.705  -5.049  1.00 35.79 ? 236 GLU A O   1 
ATOM   1965 C  CB  . GLU A 1 235 ? 28.208 -3.992  -3.714  1.00 43.26 ? 236 GLU A CB  1 
ATOM   1966 C  CG  . GLU A 1 235 ? 28.849 -2.615  -3.812  1.00 48.32 ? 236 GLU A CG  1 
ATOM   1967 C  CD  . GLU A 1 235 ? 28.451 -1.698  -2.661  1.00 58.15 ? 236 GLU A CD  1 
ATOM   1968 O  OE1 . GLU A 1 235 ? 27.773 -2.145  -1.693  1.00 57.32 ? 236 GLU A OE1 1 
ATOM   1969 O  OE2 . GLU A 1 235 ? 28.833 -0.509  -2.726  1.00 59.81 ? 236 GLU A OE2 1 
ATOM   1970 N  N   . PRO A 1 236 ? 28.844 -7.024  -4.115  1.00 31.68 ? 237 PRO A N   1 
ATOM   1971 C  CA  . PRO A 1 236 ? 28.505 -8.428  -3.810  1.00 28.76 ? 237 PRO A CA  1 
ATOM   1972 C  C   . PRO A 1 236 ? 27.170 -8.483  -2.989  1.00 31.11 ? 237 PRO A C   1 
ATOM   1973 O  O   . PRO A 1 236 ? 26.954 -7.622  -2.115  1.00 29.65 ? 237 PRO A O   1 
ATOM   1974 C  CB  . PRO A 1 236 ? 29.697 -8.906  -2.980  1.00 29.81 ? 237 PRO A CB  1 
ATOM   1975 C  CG  . PRO A 1 236 ? 30.852 -8.019  -3.377  1.00 32.28 ? 237 PRO A CG  1 
ATOM   1976 C  CD  . PRO A 1 236 ? 30.206 -6.680  -3.651  1.00 34.11 ? 237 PRO A CD  1 
ATOM   1977 N  N   . GLU A 1 237 ? 26.291 -9.438  -3.303  1.00 27.58 ? 238 GLU A N   1 
ATOM   1978 C  CA  . GLU A 1 237 ? 24.985 -9.465  -2.648  1.00 24.88 ? 238 GLU A CA  1 
ATOM   1979 C  C   . GLU A 1 237 ? 25.130 -9.927  -1.174  1.00 22.15 ? 238 GLU A C   1 
ATOM   1980 O  O   . GLU A 1 237 ? 25.673 -10.955 -0.896  1.00 21.45 ? 238 GLU A O   1 
ATOM   1981 C  CB  . GLU A 1 237 ? 23.949 -10.335 -3.380  1.00 25.70 ? 238 GLU A CB  1 
ATOM   1982 C  CG  . GLU A 1 237 ? 22.597 -10.252 -2.675  1.00 26.93 ? 238 GLU A CG  1 
ATOM   1983 C  CD  . GLU A 1 237 ? 21.475 -11.032 -3.319  1.00 29.43 ? 238 GLU A CD  1 
ATOM   1984 O  OE1 . GLU A 1 237 ? 21.782 -12.120 -3.868  1.00 34.34 ? 238 GLU A OE1 1 
ATOM   1985 O  OE2 . GLU A 1 237 ? 20.288 -10.569 -3.289  1.00 24.38 ? 238 GLU A OE2 1 
ATOM   1986 N  N   . GLU A 1 238 ? 24.594 -9.131  -0.248  1.00 20.14 ? 239 GLU A N   1 
ATOM   1987 C  CA  . GLU A 1 238 ? 24.611 -9.412  1.174   1.00 23.18 ? 239 GLU A CA  1 
ATOM   1988 C  C   . GLU A 1 238 ? 23.148 -9.329  1.621   1.00 18.86 ? 239 GLU A C   1 
ATOM   1989 O  O   . GLU A 1 238 ? 22.541 -8.237  1.602   1.00 18.98 ? 239 GLU A O   1 
ATOM   1990 C  CB  . GLU A 1 238 ? 25.328 -8.253  1.866   1.00 25.83 ? 239 GLU A CB  1 
ATOM   1991 C  CG  . GLU A 1 238 ? 26.079 -8.596  3.108   1.00 41.08 ? 239 GLU A CG  1 
ATOM   1992 C  CD  . GLU A 1 238 ? 27.549 -8.970  2.815   1.00 47.72 ? 239 GLU A CD  1 
ATOM   1993 O  OE1 . GLU A 1 238 ? 28.463 -8.109  2.929   1.00 53.63 ? 239 GLU A OE1 1 
ATOM   1994 O  OE2 . GLU A 1 238 ? 27.780 -10.144 2.462   1.00 57.47 ? 239 GLU A OE2 1 
ATOM   1995 N  N   . LEU A 1 239 ? 22.494 -10.464 1.898   1.00 18.95 ? 240 LEU A N   1 
ATOM   1996 C  CA  . LEU A 1 239 ? 21.073 -10.323 2.221   1.00 15.63 ? 240 LEU A CA  1 
ATOM   1997 C  C   . LEU A 1 239 ? 20.880 -9.492  3.538   1.00 14.46 ? 240 LEU A C   1 
ATOM   1998 O  O   . LEU A 1 239 ? 21.618 -9.730  4.522   1.00 16.27 ? 240 LEU A O   1 
ATOM   1999 C  CB  . LEU A 1 239 ? 20.463 -11.713 2.430   1.00 16.78 ? 240 LEU A CB  1 
ATOM   2000 C  CG  . LEU A 1 239 ? 20.421 -12.575 1.144   1.00 17.15 ? 240 LEU A CG  1 
ATOM   2001 C  CD1 . LEU A 1 239 ? 19.742 -13.853 1.585   1.00 21.72 ? 240 LEU A CD1 1 
ATOM   2002 C  CD2 . LEU A 1 239 ? 19.577 -11.870 0.118   1.00 17.37 ? 240 LEU A CD2 1 
ATOM   2003 N  N   . MET A 1 240 ? 19.802 -8.675  3.530   1.00 14.87 ? 241 MET A N   1 
ATOM   2004 C  CA  . MET A 1 240 ? 19.380 -7.871  4.722   1.00 15.08 ? 241 MET A CA  1 
ATOM   2005 C  C   . MET A 1 240 ? 18.641 -8.853  5.654   1.00 14.93 ? 241 MET A C   1 
ATOM   2006 O  O   . MET A 1 240 ? 17.436 -8.985  5.555   1.00 16.15 ? 241 MET A O   1 
ATOM   2007 C  CB  . MET A 1 240 ? 18.424 -6.742  4.366   1.00 17.57 ? 241 MET A CB  1 
ATOM   2008 C  CG  . MET A 1 240 ? 18.238 -5.729  5.525   1.00 16.76 ? 241 MET A CG  1 
ATOM   2009 S  SD  . MET A 1 240 ? 17.334 -4.335  4.941   1.00 20.02 ? 241 MET A SD  1 
ATOM   2010 C  CE  . MET A 1 240 ? 18.645 -3.207  4.331   1.00 16.13 ? 241 MET A CE  1 
ATOM   2011 N  N   . VAL A 1 241 ? 19.406 -9.495  6.539   1.00 15.45 ? 242 VAL A N   1 
ATOM   2012 C  CA  . VAL A 1 241 ? 18.832 -10.345 7.583   1.00 15.62 ? 242 VAL A CA  1 
ATOM   2013 C  C   . VAL A 1 241 ? 19.644 -10.101 8.859   1.00 16.18 ? 242 VAL A C   1 
ATOM   2014 O  O   . VAL A 1 241 ? 20.836 -9.672  8.800   1.00 14.98 ? 242 VAL A O   1 
ATOM   2015 C  CB  . VAL A 1 241 ? 18.872 -11.849 7.206   1.00 15.49 ? 242 VAL A CB  1 
ATOM   2016 C  CG1 . VAL A 1 241 ? 17.981 -12.145 5.979   1.00 17.88 ? 242 VAL A CG1 1 
ATOM   2017 C  CG2 . VAL A 1 241 ? 20.310 -12.335 7.102   1.00 15.05 ? 242 VAL A CG2 1 
ATOM   2018 N  N   . ASP A 1 242 ? 19.036 -10.390 10.005  1.00 12.70 ? 243 ASP A N   1 
ATOM   2019 C  CA  . ASP A 1 242 ? 19.703 -10.257 11.315  1.00 12.14 ? 243 ASP A CA  1 
ATOM   2020 C  C   . ASP A 1 242 ? 20.189 -8.811  11.506  1.00 12.67 ? 243 ASP A C   1 
ATOM   2021 O  O   . ASP A 1 242 ? 21.290 -8.582  12.054  1.00 13.24 ? 243 ASP A O   1 
ATOM   2022 C  CB  . ASP A 1 242 ? 20.828 -11.327 11.595  1.00 12.79 ? 243 ASP A CB  1 
ATOM   2023 C  CG  . ASP A 1 242 ? 20.263 -12.703 11.665  1.00 16.04 ? 243 ASP A CG  1 
ATOM   2024 O  OD1 . ASP A 1 242 ? 19.187 -12.848 12.290  1.00 13.82 ? 243 ASP A OD1 1 
ATOM   2025 O  OD2 . ASP A 1 242 ? 20.868 -13.626 11.015  1.00 16.62 ? 243 ASP A OD2 1 
ATOM   2026 N  N   . ASN A 1 243 ? 19.290 -7.888  11.198  1.00 12.31 ? 244 ASN A N   1 
ATOM   2027 C  CA  . ASN A 1 243 ? 19.577 -6.460  11.493  1.00 12.64 ? 244 ASN A CA  1 
ATOM   2028 C  C   . ASN A 1 243 ? 19.042 -6.012  12.854  1.00 12.61 ? 244 ASN A C   1 
ATOM   2029 O  O   . ASN A 1 243 ? 18.332 -5.015  12.910  1.00 12.27 ? 244 ASN A O   1 
ATOM   2030 C  CB  . ASN A 1 243 ? 19.114 -5.593  10.327  1.00 14.88 ? 244 ASN A CB  1 
ATOM   2031 C  CG  . ASN A 1 243 ? 17.575 -5.668  10.060  1.00 12.82 ? 244 ASN A CG  1 
ATOM   2032 O  OD1 . ASN A 1 243 ? 16.912 -6.519  10.670  1.00 15.82 ? 244 ASN A OD1 1 
ATOM   2033 N  ND2 . ASN A 1 243 ? 16.999 -4.776  9.181   1.00 14.16 ? 244 ASN A ND2 1 
ATOM   2034 N  N   . TRP A 1 244 ? 19.345 -6.761  13.892  1.00 11.92 ? 245 TRP A N   1 
ATOM   2035 C  CA  . TRP A 1 244 ? 18.901 -6.480  15.241  1.00 13.28 ? 245 TRP A CA  1 
ATOM   2036 C  C   . TRP A 1 244 ? 20.061 -6.380  16.146  1.00 13.39 ? 245 TRP A C   1 
ATOM   2037 O  O   . TRP A 1 244 ? 21.084 -7.074  15.961  1.00 13.08 ? 245 TRP A O   1 
ATOM   2038 C  CB  . TRP A 1 244 ? 17.896 -7.529  15.733  1.00 12.84 ? 245 TRP A CB  1 
ATOM   2039 C  CG  . TRP A 1 244 ? 18.328 -8.974  15.552  1.00 12.08 ? 245 TRP A CG  1 
ATOM   2040 C  CD1 . TRP A 1 244 ? 18.201 -9.753  14.434  1.00 12.14 ? 245 TRP A CD1 1 
ATOM   2041 C  CD2 . TRP A 1 244 ? 18.868 -9.846  16.552  1.00 11.84 ? 245 TRP A CD2 1 
ATOM   2042 N  NE1 . TRP A 1 244 ? 18.715 -11.030 14.672  1.00 12.67 ? 245 TRP A NE1 1 
ATOM   2043 C  CE2 . TRP A 1 244 ? 19.132 -11.111 15.910  1.00 12.49 ? 245 TRP A CE2 1 
ATOM   2044 C  CE3 . TRP A 1 244 ? 19.188 -9.696  17.903  1.00 13.37 ? 245 TRP A CE3 1 
ATOM   2045 C  CZ2 . TRP A 1 244 ? 19.728 -12.188 16.602  1.00 12.78 ? 245 TRP A CZ2 1 
ATOM   2046 C  CZ3 . TRP A 1 244 ? 19.752 -10.776 18.586  1.00 13.32 ? 245 TRP A CZ3 1 
ATOM   2047 C  CH2 . TRP A 1 244 ? 20.004 -11.987 17.933  1.00 12.55 ? 245 TRP A CH2 1 
ATOM   2048 N  N   . ARG A 1 245 ? 19.936 -5.501  17.141  1.00 11.82 ? 246 ARG A N   1 
ATOM   2049 C  CA  . ARG A 1 245 ? 20.871 -5.386  18.257  1.00 12.92 ? 246 ARG A CA  1 
ATOM   2050 C  C   . ARG A 1 245 ? 20.400 -6.299  19.394  1.00 13.96 ? 246 ARG A C   1 
ATOM   2051 O  O   . ARG A 1 245 ? 19.224 -6.344  19.743  1.00 15.65 ? 246 ARG A O   1 
ATOM   2052 C  CB  . ARG A 1 245 ? 20.985 -3.958  18.764  1.00 13.89 ? 246 ARG A CB  1 
ATOM   2053 C  CG  . ARG A 1 245 ? 22.054 -3.793  19.854  1.00 12.94 ? 246 ARG A CG  1 
ATOM   2054 C  CD  . ARG A 1 245 ? 22.012 -2.396  20.485  1.00 13.64 ? 246 ARG A CD  1 
ATOM   2055 N  NE  . ARG A 1 245 ? 23.289 -2.034  21.103  1.00 15.33 ? 246 ARG A NE  1 
ATOM   2056 C  CZ  . ARG A 1 245 ? 23.479 -1.017  21.943  1.00 15.22 ? 246 ARG A CZ  1 
ATOM   2057 N  NH1 . ARG A 1 245 ? 22.478 -0.214  22.286  1.00 15.38 ? 246 ARG A NH1 1 
ATOM   2058 N  NH2 . ARG A 1 245 ? 24.689 -0.803  22.441  1.00 16.10 ? 246 ARG A NH2 1 
ATOM   2059 N  N   . PRO A 1 246 ? 21.306 -7.094  19.983  1.00 15.94 ? 247 PRO A N   1 
ATOM   2060 C  CA  . PRO A 1 246 ? 20.862 -7.924  21.096  1.00 15.63 ? 247 PRO A CA  1 
ATOM   2061 C  C   . PRO A 1 246 ? 20.577 -7.126  22.372  1.00 14.68 ? 247 PRO A C   1 
ATOM   2062 O  O   . PRO A 1 246 ? 20.991 -5.956  22.486  1.00 15.85 ? 247 PRO A O   1 
ATOM   2063 C  CB  . PRO A 1 246 ? 22.057 -8.853  21.356  1.00 17.95 ? 247 PRO A CB  1 
ATOM   2064 C  CG  . PRO A 1 246 ? 23.211 -8.158  20.692  1.00 20.64 ? 247 PRO A CG  1 
ATOM   2065 C  CD  . PRO A 1 246 ? 22.718 -7.295  19.618  1.00 17.28 ? 247 PRO A CD  1 
ATOM   2066 N  N   . ALA A 1 247 ? 19.893 -7.760  23.315  1.00 15.44 ? 248 ALA A N   1 
ATOM   2067 C  CA  . ALA A 1 247 ? 19.531 -7.138  24.615  1.00 13.58 ? 248 ALA A CA  1 
ATOM   2068 C  C   . ALA A 1 247 ? 20.811 -6.597  25.320  1.00 16.32 ? 248 ALA A C   1 
ATOM   2069 O  O   . ALA A 1 247 ? 21.910 -7.205  25.362  1.00 14.88 ? 248 ALA A O   1 
ATOM   2070 C  CB  . ALA A 1 247 ? 18.740 -8.145  25.479  1.00 16.74 ? 248 ALA A CB  1 
ATOM   2071 N  N   . GLN A 1 248 ? 20.661 -5.443  25.905  1.00 14.56 ? 249 GLN A N   1 
ATOM   2072 C  CA  . GLN A 1 248 ? 21.762 -4.744  26.589  1.00 15.72 ? 249 GLN A CA  1 
ATOM   2073 C  C   . GLN A 1 248 ? 21.385 -4.743  28.054  1.00 17.46 ? 249 GLN A C   1 
ATOM   2074 O  O   . GLN A 1 248 ? 20.230 -4.904  28.424  1.00 15.38 ? 249 GLN A O   1 
ATOM   2075 C  CB  . GLN A 1 248 ? 21.807 -3.325  26.078  1.00 16.55 ? 249 GLN A CB  1 
ATOM   2076 C  CG  . GLN A 1 248 ? 22.000 -3.226  24.569  1.00 14.66 ? 249 GLN A CG  1 
ATOM   2077 C  CD  . GLN A 1 248 ? 23.335 -3.802  24.201  1.00 18.64 ? 249 GLN A CD  1 
ATOM   2078 O  OE1 . GLN A 1 248 ? 24.382 -3.406  24.769  1.00 20.50 ? 249 GLN A OE1 1 
ATOM   2079 N  NE2 . GLN A 1 248 ? 23.319 -4.816  23.321  1.00 18.11 ? 249 GLN A NE2 1 
ATOM   2080 N  N   . PRO A 1 249 ? 22.354 -4.488  28.936  1.00 18.67 ? 250 PRO A N   1 
ATOM   2081 C  CA  . PRO A 1 249 ? 22.188 -4.473  30.360  1.00 18.72 ? 250 PRO A CA  1 
ATOM   2082 C  C   . PRO A 1 249 ? 21.123 -3.466  30.852  1.00 17.13 ? 250 PRO A C   1 
ATOM   2083 O  O   . PRO A 1 249 ? 21.149 -2.277  30.462  1.00 20.50 ? 250 PRO A O   1 
ATOM   2084 C  CB  . PRO A 1 249 ? 23.580 -4.001  30.826  1.00 21.52 ? 250 PRO A CB  1 
ATOM   2085 C  CG  . PRO A 1 249 ? 24.487 -4.600  29.826  1.00 24.15 ? 250 PRO A CG  1 
ATOM   2086 C  CD  . PRO A 1 249 ? 23.751 -4.220  28.557  1.00 20.50 ? 250 PRO A CD  1 
ATOM   2087 N  N   . LEU A 1 250 ? 20.229 -3.963  31.689  1.00 17.41 ? 251 LEU A N   1 
ATOM   2088 C  CA  . LEU A 1 250 ? 19.173 -3.086  32.233  1.00 17.40 ? 251 LEU A CA  1 
ATOM   2089 C  C   . LEU A 1 250 ? 19.770 -2.024  33.133  1.00 19.05 ? 251 LEU A C   1 
ATOM   2090 O  O   . LEU A 1 250 ? 19.270 -0.889  33.209  1.00 17.36 ? 251 LEU A O   1 
ATOM   2091 C  CB  . LEU A 1 250 ? 18.084 -3.882  32.950  1.00 19.00 ? 251 LEU A CB  1 
ATOM   2092 C  CG  . LEU A 1 250 ? 16.776 -3.219  33.364  1.00 17.99 ? 251 LEU A CG  1 
ATOM   2093 C  CD1 . LEU A 1 250 ? 16.031 -2.557  32.204  1.00 18.28 ? 251 LEU A CD1 1 
ATOM   2094 C  CD2 . LEU A 1 250 ? 15.934 -4.242  34.142  1.00 20.32 ? 251 LEU A CD2 1 
ATOM   2095 N  N   . LYS A 1 251 ? 20.833 -2.369  33.864  1.00 21.08 ? 252 LYS A N   1 
ATOM   2096 C  CA  . LYS A 1 251 ? 21.468 -1.341  34.760  1.00 23.19 ? 252 LYS A CA  1 
ATOM   2097 C  C   . LYS A 1 251 ? 20.448 -0.858  35.795  1.00 24.70 ? 252 LYS A C   1 
ATOM   2098 O  O   . LYS A 1 251 ? 19.638 -1.646  36.293  1.00 28.92 ? 252 LYS A O   1 
ATOM   2099 C  CB  . LYS A 1 251 ? 22.253 -0.256  33.969  1.00 22.63 ? 252 LYS A CB  1 
ATOM   2100 C  CG  . LYS A 1 251 ? 23.401 -0.918  33.188  1.00 24.58 ? 252 LYS A CG  1 
ATOM   2101 C  CD  . LYS A 1 251 ? 24.555 -0.035  32.860  1.00 30.13 ? 252 LYS A CD  1 
ATOM   2102 C  CE  . LYS A 1 251 ? 25.475 -0.722  31.876  1.00 30.16 ? 252 LYS A CE  1 
ATOM   2103 N  NZ  . LYS A 1 251 ? 26.194 0.286   31.044  1.00 30.21 ? 252 LYS A NZ  1 
ATOM   2104 N  N   A ASN A 1 252 ? 20.401 0.396   36.206  0.50 25.81 ? 253 ASN A N   1 
ATOM   2105 N  N   B ASN A 1 252 ? 20.533 0.445   36.021  0.50 25.56 ? 253 ASN A N   1 
ATOM   2106 C  CA  A ASN A 1 252 ? 19.517 0.696   37.389  0.50 27.21 ? 253 ASN A CA  1 
ATOM   2107 C  CA  B ASN A 1 252 ? 19.734 1.140   36.989  0.50 29.10 ? 253 ASN A CA  1 
ATOM   2108 C  C   A ASN A 1 252 ? 17.956 0.611   37.097  0.50 24.95 ? 253 ASN A C   1 
ATOM   2109 C  C   B ASN A 1 252 ? 18.372 1.493   36.370  0.50 26.10 ? 253 ASN A C   1 
ATOM   2110 O  O   A ASN A 1 252 ? 17.090 0.582   37.992  0.50 23.94 ? 253 ASN A O   1 
ATOM   2111 O  O   B ASN A 1 252 ? 18.044 2.703   36.364  0.50 25.29 ? 253 ASN A O   1 
ATOM   2112 C  CB  A ASN A 1 252 ? 19.967 2.048   38.010  0.50 30.72 ? 253 ASN A CB  1 
ATOM   2113 C  CB  B ASN A 1 252 ? 20.453 2.455   37.403  0.50 31.43 ? 253 ASN A CB  1 
ATOM   2114 C  CG  A ASN A 1 252 ? 19.294 2.368   39.322  0.50 32.57 ? 253 ASN A CG  1 
ATOM   2115 C  CG  B ASN A 1 252 ? 21.656 2.236   38.329  0.50 35.79 ? 253 ASN A CG  1 
ATOM   2116 O  OD1 A ASN A 1 252 ? 19.636 1.825   40.377  0.50 36.20 ? 253 ASN A OD1 1 
ATOM   2117 O  OD1 B ASN A 1 252 ? 22.046 1.106   38.644  0.50 40.90 ? 253 ASN A OD1 1 
ATOM   2118 N  ND2 A ASN A 1 252 ? 18.353 3.295   39.275  0.50 34.64 ? 253 ASN A ND2 1 
ATOM   2119 N  ND2 B ASN A 1 252 ? 22.236 3.338   38.785  0.50 35.26 ? 253 ASN A ND2 1 
ATOM   2120 N  N   . ARG A 1 253 ? 17.625 0.493   35.812  1.00 22.19 ? 254 ARG A N   1 
ATOM   2121 C  CA  . ARG A 1 253 ? 16.255 0.773   35.306  1.00 19.36 ? 254 ARG A CA  1 
ATOM   2122 C  C   . ARG A 1 253 ? 15.117 -0.168  35.722  1.00 20.37 ? 254 ARG A C   1 
ATOM   2123 O  O   . ARG A 1 253 ? 15.313 -1.375  35.918  1.00 24.31 ? 254 ARG A O   1 
ATOM   2124 C  CB  . ARG A 1 253 ? 16.272 0.956   33.755  1.00 15.79 ? 254 ARG A CB  1 
ATOM   2125 C  CG  . ARG A 1 253 ? 17.240 2.080   33.275  1.00 14.58 ? 254 ARG A CG  1 
ATOM   2126 C  CD  . ARG A 1 253 ? 17.295 2.058   31.746  1.00 14.59 ? 254 ARG A CD  1 
ATOM   2127 N  NE  . ARG A 1 253 ? 18.119 0.891   31.300  1.00 12.89 ? 254 ARG A NE  1 
ATOM   2128 C  CZ  . ARG A 1 253 ? 18.336 0.583   30.021  1.00 11.86 ? 254 ARG A CZ  1 
ATOM   2129 N  NH1 . ARG A 1 253 ? 17.748 1.298   29.062  1.00 11.82 ? 254 ARG A NH1 1 
ATOM   2130 N  NH2 . ARG A 1 253 ? 19.160 -0.408  29.668  1.00 12.38 ? 254 ARG A NH2 1 
ATOM   2131 N  N   . GLN A 1 254 ? 13.910 0.385   35.793  1.00 20.22 ? 255 GLN A N   1 
ATOM   2132 C  CA  . GLN A 1 254 ? 12.701 -0.376  35.993  1.00 21.26 ? 255 GLN A CA  1 
ATOM   2133 C  C   . GLN A 1 254 ? 11.878 -0.334  34.733  1.00 20.15 ? 255 GLN A C   1 
ATOM   2134 O  O   . GLN A 1 254 ? 11.709 0.735   34.101  1.00 22.44 ? 255 GLN A O   1 
ATOM   2135 C  CB  . GLN A 1 254 ? 11.850 0.244   37.119  1.00 27.82 ? 255 GLN A CB  1 
ATOM   2136 C  CG  . GLN A 1 254 ? 11.110 -0.828  37.928  1.00 38.81 ? 255 GLN A CG  1 
ATOM   2137 C  CD  . GLN A 1 254 ? 11.852 -1.178  39.228  1.00 51.42 ? 255 GLN A CD  1 
ATOM   2138 O  OE1 . GLN A 1 254 ? 11.837 -0.385  40.192  1.00 60.21 ? 255 GLN A OE1 1 
ATOM   2139 N  NE2 . GLN A 1 254 ? 12.512 -2.364  39.267  1.00 51.19 ? 255 GLN A NE2 1 
ATOM   2140 N  N   . ILE A 1 255 ? 11.395 -1.504  34.355  1.00 17.64 ? 256 ILE A N   1 
ATOM   2141 C  CA  . ILE A 1 255 ? 10.394 -1.610  33.356  1.00 17.93 ? 256 ILE A CA  1 
ATOM   2142 C  C   . ILE A 1 255 ? 9.016  -1.627  34.032  1.00 16.82 ? 256 ILE A C   1 
ATOM   2143 O  O   . ILE A 1 255 ? 8.766  -2.357  35.002  1.00 16.72 ? 256 ILE A O   1 
ATOM   2144 C  CB  . ILE A 1 255 ? 10.605 -2.875  32.465  1.00 16.83 ? 256 ILE A CB  1 
ATOM   2145 C  CG1 . ILE A 1 255 ? 12.018 -2.854  31.922  1.00 17.23 ? 256 ILE A CG1 1 
ATOM   2146 C  CG2 . ILE A 1 255 ? 9.536  -2.982  31.392  1.00 16.93 ? 256 ILE A CG2 1 
ATOM   2147 C  CD1 . ILE A 1 255 ? 12.331 -4.125  31.119  1.00 18.62 ? 256 ILE A CD1 1 
ATOM   2148 N  N   . LYS A 1 256 ? 8.151  -0.711  33.577  1.00 17.38 ? 257 LYS A N   1 
ATOM   2149 C  CA  . LYS A 1 256 ? 6.759  -0.618  34.047  1.00 16.90 ? 257 LYS A CA  1 
ATOM   2150 C  C   . LYS A 1 256 ? 5.779  -1.284  33.118  1.00 17.77 ? 257 LYS A C   1 
ATOM   2151 O  O   . LYS A 1 256 ? 5.954  -1.247  31.913  1.00 16.72 ? 257 LYS A O   1 
ATOM   2152 C  CB  . LYS A 1 256 ? 6.353  0.893   34.234  1.00 17.92 ? 257 LYS A CB  1 
ATOM   2153 C  CG  . LYS A 1 256 ? 7.174  1.753   35.213  1.00 27.03 ? 257 LYS A CG  1 
ATOM   2154 C  CD  . LYS A 1 256 ? 7.244  1.159   36.602  1.00 34.75 ? 257 LYS A CD  1 
ATOM   2155 C  CE  . LYS A 1 256 ? 7.413  2.250   37.684  1.00 42.72 ? 257 LYS A CE  1 
ATOM   2156 N  NZ  . LYS A 1 256 ? 6.446  3.390   37.551  1.00 46.24 ? 257 LYS A NZ  1 
ATOM   2157 N  N   . ALA A 1 257 ? 4.741  -1.915  33.644  1.00 17.31 ? 258 ALA A N   1 
ATOM   2158 C  CA  . ALA A 1 257 ? 3.679  -2.505  32.863  1.00 17.61 ? 258 ALA A CA  1 
ATOM   2159 C  C   . ALA A 1 257 ? 2.343  -1.771  33.022  1.00 17.24 ? 258 ALA A C   1 
ATOM   2160 O  O   . ALA A 1 257 ? 1.963  -1.338  34.129  1.00 17.27 ? 258 ALA A O   1 
ATOM   2161 C  CB  . ALA A 1 257 ? 3.506  -3.983  33.218  1.00 20.04 ? 258 ALA A CB  1 
ATOM   2162 N  N   . SER A 1 258 ? 1.598  -1.668  31.936  1.00 14.37 ? 259 SER A N   1 
ATOM   2163 C  CA  . SER A 1 258 ? 0.344  -0.908  31.977  1.00 18.94 ? 259 SER A CA  1 
ATOM   2164 C  C   . SER A 1 258 ? -0.779 -1.815  32.414  1.00 19.50 ? 259 SER A C   1 
ATOM   2165 O  O   . SER A 1 258 ? -1.931 -1.368  32.426  1.00 26.46 ? 259 SER A O   1 
ATOM   2166 C  CB  . SER A 1 258 ? -0.016 -0.391  30.596  1.00 17.69 ? 259 SER A CB  1 
ATOM   2167 O  OG  . SER A 1 258 ? -0.427 -1.426  29.688  1.00 18.65 ? 259 SER A OG  1 
ATOM   2168 N  N   . PHE A 1 259 ? -0.489 -3.070  32.669  1.00 19.78 ? 260 PHE A N   1 
ATOM   2169 C  CA  . PHE A 1 259 ? -1.481 -4.121  32.792  1.00 22.51 ? 260 PHE A CA  1 
ATOM   2170 C  C   . PHE A 1 259 ? -1.072 -5.061  33.908  1.00 27.19 ? 260 PHE A C   1 
ATOM   2171 O  O   . PHE A 1 259 ? 0.144  -5.270  34.199  1.00 24.00 ? 260 PHE A O   1 
ATOM   2172 C  CB  . PHE A 1 259 ? -1.671 -4.953  31.529  1.00 23.22 ? 260 PHE A CB  1 
ATOM   2173 C  CG  . PHE A 1 259 ? -0.391 -5.638  31.054  1.00 22.97 ? 260 PHE A CG  1 
ATOM   2174 C  CD1 . PHE A 1 259 ? 0.524  -4.918  30.315  1.00 23.38 ? 260 PHE A CD1 1 
ATOM   2175 C  CD2 . PHE A 1 259 ? -0.106 -6.959  31.405  1.00 25.59 ? 260 PHE A CD2 1 
ATOM   2176 C  CE1 . PHE A 1 259 ? 1.720  -5.512  29.931  1.00 23.53 ? 260 PHE A CE1 1 
ATOM   2177 C  CE2 . PHE A 1 259 ? 1.076  -7.564  31.010  1.00 25.95 ? 260 PHE A CE2 1 
ATOM   2178 C  CZ  . PHE A 1 259 ? 1.984  -6.825  30.267  1.00 26.66 ? 260 PHE A CZ  1 
ATOM   2179 N  N   . LYS A 1 260 ? -2.163 -5.587  34.506  1.00 38.94 ? 261 LYS A N   1 
ATOM   2180 C  CA  . LYS A 1 260 ? -2.286 -6.809  35.313  1.00 49.99 ? 261 LYS A CA  1 
ATOM   2181 C  C   . LYS A 1 260 ? -1.497 -6.842  36.609  1.00 57.60 ? 261 LYS A C   1 
ATOM   2182 O  O   . LYS A 1 260 ? -0.286 -7.038  36.603  1.00 68.37 ? 261 LYS A O   1 
ATOM   2183 C  CB  . LYS A 1 260 ? -2.111 -8.080  34.453  1.00 50.38 ? 261 LYS A CB  1 
ATOM   2184 C  CG  . LYS A 1 260 ? -3.184 -8.195  33.358  1.00 53.86 ? 261 LYS A CG  1 
ATOM   2185 C  CD  . LYS A 1 260 ? -3.241 -9.596  32.777  1.00 53.96 ? 261 LYS A CD  1 
ATOM   2186 C  CE  . LYS A 1 260 ? -2.242 -9.788  31.657  1.00 50.79 ? 261 LYS A CE  1 
ATOM   2187 N  NZ  . LYS A 1 260 ? -1.316 -10.921 31.965  1.00 49.13 ? 261 LYS A NZ  1 
ATOM   2188 O  OXT . LYS A 1 260 ? -2.084 -6.629  37.683  1.00 60.11 ? 261 LYS A OXT 1 
HETATM 2189 ZN ZN  . ZN  B 2 .   ? 14.348 0.098   15.239  1.00 11.38 ? 301 ZN  A ZN  1 
HETATM 2190 S  S   . DMS C 3 .   ? 22.337 -9.889  14.932  1.00 27.53 ? 302 DMS A S   1 
HETATM 2191 O  O   . DMS C 3 .   ? 23.023 -11.214 14.601  1.00 27.07 ? 302 DMS A O   1 
HETATM 2192 C  C1  . DMS C 3 .   ? 22.625 -9.816  16.598  1.00 23.45 ? 302 DMS A C1  1 
HETATM 2193 C  C2  . DMS C 3 .   ? 23.437 -8.633  14.527  1.00 27.37 ? 302 DMS A C2  1 
HETATM 2194 S  S   . DMS D 3 .   ? 16.689 1.906   10.979  1.00 55.43 ? 303 DMS A S   1 
HETATM 2195 O  O   . DMS D 3 .   ? 18.056 1.961   10.355  1.00 37.54 ? 303 DMS A O   1 
HETATM 2196 C  C1  . DMS D 3 .   ? 16.865 1.521   12.655  1.00 39.70 ? 303 DMS A C1  1 
HETATM 2197 C  C2  . DMS D 3 .   ? 15.915 3.445   11.151  1.00 40.08 ? 303 DMS A C2  1 
HETATM 2198 O  O12 . WWL E 4 .   ? 14.880 7.857   13.656  1.00 27.44 ? 304 WWL A O12 1 
HETATM 2199 S  S10 . WWL E 4 .   ? 16.246 7.288   13.561  1.00 24.63 ? 304 WWL A S10 1 
HETATM 2200 O  O11 . WWL E 4 .   ? 16.427 6.887   12.085  1.00 24.61 ? 304 WWL A O11 1 
HETATM 2201 C  C7  . WWL E 4 .   ? 16.301 5.772   14.449  1.00 17.34 ? 304 WWL A C7  1 
HETATM 2202 S  S8  . WWL E 4 .   ? 15.042 5.220   15.280  1.00 17.13 ? 304 WWL A S8  1 
HETATM 2203 C  C5  . WWL E 4 .   ? 17.273 3.910   15.324  1.00 15.35 ? 304 WWL A C5  1 
HETATM 2204 C  C6  . WWL E 4 .   ? 17.476 5.079   14.533  1.00 17.14 ? 304 WWL A C6  1 
HETATM 2205 C  C9  . WWL E 4 .   ? 15.911 3.894   15.734  1.00 12.72 ? 304 WWL A C9  1 
HETATM 2206 S  S2  . WWL E 4 .   ? 15.161 2.690   16.733  1.00 12.68 ? 304 WWL A S2  1 
HETATM 2207 O  O3  . WWL E 4 .   ? 13.678 2.838   16.638  1.00 12.75 ? 304 WWL A O3  1 
HETATM 2208 N  N4  . WWL E 4 .   ? 15.727 1.239   16.102  1.00 11.54 ? 304 WWL A N4  1 
HETATM 2209 O  O1  . WWL E 4 .   ? 15.667 2.768   18.132  1.00 10.78 ? 304 WWL A O1  1 
HETATM 2210 C  C13 . WWL E 4 .   ? 17.592 8.400   13.980  1.00 25.29 ? 304 WWL A C13 1 
HETATM 2211 C  C18 . WWL E 4 .   ? 18.703 8.420   13.124  1.00 30.66 ? 304 WWL A C18 1 
HETATM 2212 C  C17 . WWL E 4 .   ? 19.801 9.256   13.411  1.00 30.78 ? 304 WWL A C17 1 
HETATM 2213 C  C16 . WWL E 4 .   ? 19.762 10.065  14.561  1.00 29.33 ? 304 WWL A C16 1 
HETATM 2214 C  C15 . WWL E 4 .   ? 18.659 10.029  15.422  1.00 31.71 ? 304 WWL A C15 1 
HETATM 2215 C  C14 . WWL E 4 .   ? 17.542 9.171   15.141  1.00 31.67 ? 304 WWL A C14 1 
HETATM 2216 O  O   . HOH F 5 .   ? 19.733 -2.305  15.711  1.00 15.40 ? 401 HOH A O   1 
HETATM 2217 O  O   . HOH F 5 .   ? -0.596 7.526   4.642   1.00 19.28 ? 402 HOH A O   1 
HETATM 2218 O  O   . HOH F 5 .   ? 3.986  -6.507  20.412  1.00 13.45 ? 403 HOH A O   1 
HETATM 2219 O  O   . HOH F 5 .   ? 16.329 -11.631 18.027  1.00 13.53 ? 404 HOH A O   1 
HETATM 2220 O  O   . HOH F 5 .   ? 2.966  -18.548 7.867   1.00 17.69 ? 405 HOH A O   1 
HETATM 2221 O  O   . HOH F 5 .   ? 22.247 0.274   29.443  1.00 19.47 ? 406 HOH A O   1 
HETATM 2222 O  O   . HOH F 5 .   ? 18.590 -6.924  29.053  1.00 16.12 ? 407 HOH A O   1 
HETATM 2223 O  O   . HOH F 5 .   ? 12.959 -13.570 11.286  1.00 15.08 ? 408 HOH A O   1 
HETATM 2224 O  O   . HOH F 5 .   ? -0.569 -5.240  23.633  1.00 17.10 ? 409 HOH A O   1 
HETATM 2225 O  O   . HOH F 5 .   ? 10.540 10.535  25.500  1.00 13.73 ? 410 HOH A O   1 
HETATM 2226 O  O   . HOH F 5 .   ? 17.084 -14.096 24.381  1.00 17.27 ? 411 HOH A O   1 
HETATM 2227 O  O   . HOH F 5 .   ? 24.651 6.884   29.680  1.00 23.66 ? 412 HOH A O   1 
HETATM 2228 O  O   . HOH F 5 .   ? 17.417 -9.340  20.931  1.00 15.99 ? 413 HOH A O   1 
HETATM 2229 O  O   . HOH F 5 .   ? -3.134 10.363  20.104  1.00 22.06 ? 414 HOH A O   1 
HETATM 2230 O  O   . HOH F 5 .   ? 7.174  16.075  27.205  1.00 24.92 ? 415 HOH A O   1 
HETATM 2231 O  O   . HOH F 5 .   ? 17.325 -11.175 -2.874  1.00 28.43 ? 416 HOH A O   1 
HETATM 2232 O  O   . HOH F 5 .   ? 4.542  -8.010  32.877  1.00 24.69 ? 417 HOH A O   1 
HETATM 2233 O  O   . HOH F 5 .   ? 18.868 -10.565 22.744  1.00 15.21 ? 418 HOH A O   1 
HETATM 2234 O  O   . HOH F 5 .   ? 12.356 -2.081  7.842   1.00 16.46 ? 419 HOH A O   1 
HETATM 2235 O  O   . HOH F 5 .   ? -1.773 -3.934  2.664   1.00 23.97 ? 420 HOH A O   1 
HETATM 2236 O  O   . HOH F 5 .   ? 3.028  12.549  11.333  1.00 17.52 ? 421 HOH A O   1 
HETATM 2237 O  O   . HOH F 5 .   ? -3.067 1.153   26.504  1.00 21.41 ? 422 HOH A O   1 
HETATM 2238 O  O   . HOH F 5 .   ? 12.767 -17.537 21.664  1.00 20.93 ? 423 HOH A O   1 
HETATM 2239 O  O   . HOH F 5 .   ? 7.145  12.364  27.847  1.00 21.24 ? 424 HOH A O   1 
HETATM 2240 O  O   . HOH F 5 .   ? 9.110  4.873   30.637  1.00 24.88 ? 425 HOH A O   1 
HETATM 2241 O  O   . HOH F 5 .   ? -0.148 -10.840 -1.759  1.00 21.19 ? 426 HOH A O   1 
HETATM 2242 O  O   . HOH F 5 .   ? 11.677 -8.268  -1.422  1.00 23.22 ? 427 HOH A O   1 
HETATM 2243 O  O   . HOH F 5 .   ? 6.760  21.902  15.340  1.00 21.84 ? 428 HOH A O   1 
HETATM 2244 O  O   . HOH F 5 .   ? 32.254 3.330   26.002  1.00 27.53 ? 429 HOH A O   1 
HETATM 2245 O  O   . HOH F 5 .   ? 1.814  11.979  8.845   1.00 17.04 ? 430 HOH A O   1 
HETATM 2246 O  O   . HOH F 5 .   ? 12.819 -20.234 10.061  1.00 22.39 ? 431 HOH A O   1 
HETATM 2247 O  O   . HOH F 5 .   ? -1.184 -16.429 13.550  1.00 25.62 ? 432 HOH A O   1 
HETATM 2248 O  O   . HOH F 5 .   ? 29.231 -3.936  -10.524 1.00 29.93 ? 433 HOH A O   1 
HETATM 2249 O  O   . HOH F 5 .   ? 25.559 -4.788  7.887   1.00 24.73 ? 434 HOH A O   1 
HETATM 2250 O  O   . HOH F 5 .   ? 10.568 -16.327 17.006  1.00 19.70 ? 435 HOH A O   1 
HETATM 2251 O  O   . HOH F 5 .   ? 4.789  -10.490 24.348  1.00 22.93 ? 436 HOH A O   1 
HETATM 2252 O  O   . HOH F 5 .   ? 17.540 -11.408 25.214  1.00 15.37 ? 437 HOH A O   1 
HETATM 2253 O  O   . HOH F 5 .   ? 5.689  22.013  17.802  1.00 22.08 ? 438 HOH A O   1 
HETATM 2254 O  O   . HOH F 5 .   ? 29.661 -1.892  21.120  1.00 22.70 ? 439 HOH A O   1 
HETATM 2255 O  O   . HOH F 5 .   ? 9.729  -17.550 6.835   1.00 29.81 ? 440 HOH A O   1 
HETATM 2256 O  O   . HOH F 5 .   ? -5.002 -4.222  13.078  1.00 32.81 ? 441 HOH A O   1 
HETATM 2257 O  O   . HOH F 5 .   ? 31.537 -7.423  9.225   1.00 42.35 ? 442 HOH A O   1 
HETATM 2258 O  O   . HOH F 5 .   ? 5.398  -19.981 13.144  1.00 20.12 ? 443 HOH A O   1 
HETATM 2259 O  O   . HOH F 5 .   ? 7.987  -15.064 26.616  1.00 20.77 ? 444 HOH A O   1 
HETATM 2260 O  O   . HOH F 5 .   ? 25.343 -1.527  26.358  1.00 26.65 ? 445 HOH A O   1 
HETATM 2261 O  O   . HOH F 5 .   ? -3.950 -5.793  8.999   1.00 19.45 ? 446 HOH A O   1 
HETATM 2262 O  O   . HOH F 5 .   ? 14.807 -2.808  -6.479  1.00 23.40 ? 447 HOH A O   1 
HETATM 2263 O  O   . HOH F 5 .   ? -2.179 -0.958  6.507   1.00 24.32 ? 448 HOH A O   1 
HETATM 2264 O  O   . HOH F 5 .   ? 28.578 8.039   21.751  1.00 22.94 ? 449 HOH A O   1 
HETATM 2265 O  O   . HOH F 5 .   ? 36.243 -0.441  14.366  1.00 23.49 ? 450 HOH A O   1 
HETATM 2266 O  O   . HOH F 5 .   ? 23.823 -2.518  7.937   1.00 21.73 ? 451 HOH A O   1 
HETATM 2267 O  O   . HOH F 5 .   ? 3.199  21.782  17.546  1.00 28.92 ? 452 HOH A O   1 
HETATM 2268 O  O   . HOH F 5 .   ? 0.588  12.589  26.770  1.00 19.12 ? 453 HOH A O   1 
HETATM 2269 O  O   . HOH F 5 .   ? 11.373 -6.102  33.929  1.00 27.74 ? 454 HOH A O   1 
HETATM 2270 O  O   . HOH F 5 .   ? 8.090  -17.614 26.359  1.00 25.90 ? 455 HOH A O   1 
HETATM 2271 O  O   . HOH F 5 .   ? 5.855  -17.887 23.294  1.00 34.68 ? 456 HOH A O   1 
HETATM 2272 O  O   . HOH F 5 .   ? 19.959 -9.314  28.898  1.00 28.69 ? 457 HOH A O   1 
HETATM 2273 O  O   . HOH F 5 .   ? 5.694  10.870  -2.189  1.00 26.21 ? 458 HOH A O   1 
HETATM 2274 O  O   . HOH F 5 .   ? 29.660 -2.791  23.507  1.00 34.84 ? 459 HOH A O   1 
HETATM 2275 O  O   . HOH F 5 .   ? 7.976  -15.345 16.889  1.00 16.40 ? 460 HOH A O   1 
HETATM 2276 O  O   . HOH F 5 .   ? -2.024 -9.870  13.932  1.00 25.30 ? 461 HOH A O   1 
HETATM 2277 O  O   . HOH F 5 .   ? 34.336 2.243   24.468  1.00 23.89 ? 462 HOH A O   1 
HETATM 2278 O  O   . HOH F 5 .   ? 26.389 9.042   20.240  1.00 24.18 ? 463 HOH A O   1 
HETATM 2279 O  O   . HOH F 5 .   ? 16.380 4.264   37.053  1.00 30.97 ? 464 HOH A O   1 
HETATM 2280 O  O   . HOH F 5 .   ? 3.054  5.945   -3.778  1.00 34.87 ? 465 HOH A O   1 
HETATM 2281 O  O   . HOH F 5 .   ? -0.330 -17.875 6.691   1.00 30.88 ? 466 HOH A O   1 
HETATM 2282 O  O   . HOH F 5 .   ? 19.816 11.300  27.976  1.00 41.88 ? 467 HOH A O   1 
HETATM 2283 O  O   . HOH F 5 .   ? 10.492 15.526  8.507   1.00 31.28 ? 468 HOH A O   1 
HETATM 2284 O  O   . HOH F 5 .   ? 21.573 0.592   -4.634  1.00 29.40 ? 469 HOH A O   1 
HETATM 2285 O  O   . HOH F 5 .   ? 7.867  -20.513 12.119  1.00 25.70 ? 470 HOH A O   1 
HETATM 2286 O  O   . HOH F 5 .   ? 7.458  -16.757 14.682  1.00 22.05 ? 471 HOH A O   1 
HETATM 2287 O  O   . HOH F 5 .   ? -2.480 -9.293  17.254  1.00 26.33 ? 472 HOH A O   1 
HETATM 2288 O  O   . HOH F 5 .   ? 2.212  -19.350 14.638  1.00 21.35 ? 473 HOH A O   1 
HETATM 2289 O  O   . HOH F 5 .   ? 23.537 -9.569  9.774   1.00 26.96 ? 474 HOH A O   1 
HETATM 2290 O  O   . HOH F 5 .   ? 6.222  -16.739 18.845  1.00 21.19 ? 475 HOH A O   1 
HETATM 2291 O  O   . HOH F 5 .   ? -2.698 1.075   3.857   1.00 26.73 ? 476 HOH A O   1 
HETATM 2292 O  O   . HOH F 5 .   ? 23.664 -11.462 5.229   1.00 24.64 ? 477 HOH A O   1 
HETATM 2293 O  O   . HOH F 5 .   ? 4.418  -12.736 32.775  1.00 34.85 ? 478 HOH A O   1 
HETATM 2294 O  O   . HOH F 5 .   ? 22.300 -9.902  25.112  1.00 28.80 ? 479 HOH A O   1 
HETATM 2295 O  O   . HOH F 5 .   ? 14.509 -3.391  37.247  1.00 20.53 ? 480 HOH A O   1 
HETATM 2296 O  O   . HOH F 5 .   ? 14.149 -18.263 19.403  1.00 21.54 ? 481 HOH A O   1 
HETATM 2297 O  O   . HOH F 5 .   ? 19.438 -11.335 27.206  1.00 29.72 ? 482 HOH A O   1 
HETATM 2298 O  O   . HOH F 5 .   ? -3.937 -7.616  1.943   1.00 27.09 ? 483 HOH A O   1 
HETATM 2299 O  O   . HOH F 5 .   ? -5.683 -2.054  25.229  1.00 24.91 ? 484 HOH A O   1 
HETATM 2300 O  O   . HOH F 5 .   ? 9.488  13.646  6.860   1.00 40.75 ? 485 HOH A O   1 
HETATM 2301 O  O   . HOH F 5 .   ? 36.517 4.797   20.977  1.00 35.12 ? 486 HOH A O   1 
HETATM 2302 O  O   . HOH F 5 .   ? -4.896 8.009   26.900  1.00 30.47 ? 487 HOH A O   1 
HETATM 2303 O  O   . HOH F 5 .   ? 8.243  14.976  31.705  1.00 32.38 ? 488 HOH A O   1 
HETATM 2304 O  O   . HOH F 5 .   ? 25.342 -0.796  28.734  1.00 33.18 ? 489 HOH A O   1 
HETATM 2305 O  O   . HOH F 5 .   ? 18.464 -1.317  11.215  1.00 26.92 ? 490 HOH A O   1 
HETATM 2306 O  O   . HOH F 5 .   ? 20.822 -12.413 22.079  1.00 25.52 ? 491 HOH A O   1 
HETATM 2307 O  O   . HOH F 5 .   ? 12.388 -17.982 26.544  1.00 25.71 ? 492 HOH A O   1 
HETATM 2308 O  O   . HOH F 5 .   ? 13.710 -15.041 1.497   1.00 28.79 ? 493 HOH A O   1 
HETATM 2309 O  O   . HOH F 5 .   ? 1.116  -14.909 2.926   1.00 28.66 ? 494 HOH A O   1 
HETATM 2310 O  O   . HOH F 5 .   ? 33.759 -1.738  13.245  1.00 26.27 ? 495 HOH A O   1 
HETATM 2311 O  O   . HOH F 5 .   ? -1.029 -12.239 18.643  1.00 35.30 ? 496 HOH A O   1 
HETATM 2312 O  O   . HOH F 5 .   ? 4.027  -12.015 26.313  1.00 26.82 ? 497 HOH A O   1 
HETATM 2313 O  O   . HOH F 5 .   ? 29.396 5.035   27.728  1.00 33.13 ? 498 HOH A O   1 
HETATM 2314 O  O   . HOH F 5 .   ? -3.352 -4.934  0.423   1.00 27.44 ? 499 HOH A O   1 
HETATM 2315 O  O   . HOH F 5 .   ? 16.325 -10.080 32.112  1.00 23.57 ? 500 HOH A O   1 
HETATM 2316 O  O   . HOH F 5 .   ? 1.728  15.950  9.103   1.00 30.45 ? 501 HOH A O   1 
HETATM 2317 O  O   . HOH F 5 .   ? 20.363 12.806  23.079  1.00 30.25 ? 502 HOH A O   1 
HETATM 2318 O  O   . HOH F 5 .   ? 23.023 -12.482 20.305  1.00 36.67 ? 503 HOH A O   1 
HETATM 2319 O  O   . HOH F 5 .   ? 14.589 -17.966 23.965  1.00 26.73 ? 504 HOH A O   1 
HETATM 2320 O  O   . HOH F 5 .   ? 23.141 9.823   27.575  1.00 28.68 ? 505 HOH A O   1 
HETATM 2321 O  O   . HOH F 5 .   ? 22.948 -13.872 9.244   1.00 26.53 ? 506 HOH A O   1 
HETATM 2322 O  O   . HOH F 5 .   ? 20.575 -6.703  32.620  1.00 24.09 ? 507 HOH A O   1 
HETATM 2323 O  O   . HOH F 5 .   ? 34.918 7.674   19.145  1.00 31.46 ? 508 HOH A O   1 
HETATM 2324 O  O   . HOH F 5 .   ? 4.766  17.701  23.766  1.00 28.00 ? 509 HOH A O   1 
HETATM 2325 O  O   . HOH F 5 .   ? 6.753  -14.757 29.193  1.00 32.02 ? 510 HOH A O   1 
HETATM 2326 O  O   . HOH F 5 .   ? 14.343 -13.103 31.478  1.00 27.19 ? 511 HOH A O   1 
HETATM 2327 O  O   . HOH F 5 .   ? 8.576  18.335  11.192  1.00 25.40 ? 512 HOH A O   1 
HETATM 2328 O  O   . HOH F 5 .   ? -2.446 -11.370 11.278  1.00 25.36 ? 513 HOH A O   1 
HETATM 2329 O  O   . HOH F 5 .   ? -6.613 4.558   23.625  1.00 34.44 ? 514 HOH A O   1 
HETATM 2330 O  O   . HOH F 5 .   ? -5.240 5.099   15.612  1.00 27.86 ? 515 HOH A O   1 
HETATM 2331 O  O   . HOH F 5 .   ? -5.699 0.650   26.088  1.00 30.72 ? 516 HOH A O   1 
HETATM 2332 O  O   . HOH F 5 .   ? 10.586 16.763  12.017  1.00 21.66 ? 517 HOH A O   1 
HETATM 2333 O  O   . HOH F 5 .   ? 0.562  15.489  28.951  1.00 37.85 ? 518 HOH A O   1 
HETATM 2334 O  O   . HOH F 5 .   ? 27.557 1.165   -1.051  1.00 45.28 ? 519 HOH A O   1 
HETATM 2335 O  O   . HOH F 5 .   ? 12.605 2.428   -6.559  1.00 31.60 ? 520 HOH A O   1 
HETATM 2336 O  O   . HOH F 5 .   ? 32.409 -5.186  22.196  1.00 31.95 ? 521 HOH A O   1 
HETATM 2337 O  O   . HOH F 5 .   ? 17.582 7.535   -2.539  1.00 31.03 ? 522 HOH A O   1 
HETATM 2338 O  O   . HOH F 5 .   ? 20.646 2.840   34.445  1.00 33.54 ? 523 HOH A O   1 
HETATM 2339 O  O   . HOH F 5 .   ? 8.085  -7.033  -3.342  1.00 30.69 ? 524 HOH A O   1 
HETATM 2340 O  O   . HOH F 5 .   ? -6.922 6.959   25.332  1.00 31.85 ? 525 HOH A O   1 
HETATM 2341 O  O   . HOH F 5 .   ? 2.742  -1.586  -2.596  1.00 29.77 ? 526 HOH A O   1 
HETATM 2342 O  O   . HOH F 5 .   ? -7.914 -3.778  24.547  1.00 30.07 ? 527 HOH A O   1 
HETATM 2343 O  O   . HOH F 5 .   ? 25.235 -9.541  23.621  1.00 40.45 ? 528 HOH A O   1 
HETATM 2344 O  O   . HOH F 5 .   ? -8.889 6.146   27.177  1.00 37.64 ? 529 HOH A O   1 
HETATM 2345 O  O   . HOH F 5 .   ? 19.870 -15.955 17.878  1.00 30.49 ? 530 HOH A O   1 
HETATM 2346 O  O   . HOH F 5 .   ? 1.846  -19.043 5.518   1.00 30.60 ? 531 HOH A O   1 
HETATM 2347 O  O   . HOH F 5 .   ? 16.699 -6.739  31.111  1.00 27.41 ? 532 HOH A O   1 
HETATM 2348 O  O   . HOH F 5 .   ? 32.701 1.536   15.911  1.00 27.88 ? 533 HOH A O   1 
HETATM 2349 O  O   . HOH F 5 .   ? 35.385 1.854   14.938  1.00 29.17 ? 534 HOH A O   1 
HETATM 2350 O  O   . HOH F 5 .   ? 26.128 -5.545  22.387  1.00 33.66 ? 535 HOH A O   1 
HETATM 2351 O  O   . HOH F 5 .   ? 25.904 -3.107  20.914  1.00 18.23 ? 536 HOH A O   1 
HETATM 2352 O  O   . HOH F 5 .   ? 19.891 3.631   11.491  1.00 48.27 ? 537 HOH A O   1 
HETATM 2353 O  O   . HOH F 5 .   ? 14.417 9.926   10.763  1.00 42.01 ? 538 HOH A O   1 
HETATM 2354 O  O   . HOH F 5 .   ? 14.387 17.874  11.645  1.00 33.24 ? 539 HOH A O   1 
HETATM 2355 O  O   . HOH F 5 .   ? 24.547 -11.855 12.268  1.00 35.05 ? 540 HOH A O   1 
HETATM 2356 O  O   . HOH F 5 .   ? 37.178 -13.243 8.138   1.00 29.52 ? 541 HOH A O   1 
HETATM 2357 O  O   . HOH F 5 .   ? -6.550 -5.224  7.569   1.00 33.51 ? 542 HOH A O   1 
HETATM 2358 O  O   . HOH F 5 .   ? 22.375 10.676  24.262  1.00 29.27 ? 543 HOH A O   1 
HETATM 2359 O  O   . HOH F 5 .   ? 18.653 12.244  31.796  1.00 28.74 ? 544 HOH A O   1 
HETATM 2360 O  O   . HOH F 5 .   ? 13.767 -6.785  32.649  1.00 23.70 ? 545 HOH A O   1 
HETATM 2361 O  O   . HOH F 5 .   ? 11.909 -3.912  35.937  1.00 26.03 ? 546 HOH A O   1 
HETATM 2362 O  O   . HOH F 5 .   ? 17.706 -2.741  37.405  1.00 41.16 ? 547 HOH A O   1 
HETATM 2363 O  O   . HOH F 5 .   ? 22.187 -4.603  34.318  1.00 33.09 ? 548 HOH A O   1 
HETATM 2364 O  O   . HOH F 5 .   ? 18.431 -7.337  34.438  1.00 34.21 ? 549 HOH A O   1 
HETATM 2365 O  O   . HOH F 5 .   ? 16.134 -7.792  33.569  1.00 39.63 ? 550 HOH A O   1 
HETATM 2366 O  O   . HOH F 5 .   ? 4.090  -12.184 37.146  1.00 31.06 ? 551 HOH A O   1 
HETATM 2367 O  O   . HOH F 5 .   ? 10.094 2.941   33.678  1.00 30.88 ? 552 HOH A O   1 
HETATM 2368 O  O   . HOH F 5 .   ? 10.906 3.402   38.575  1.00 36.30 ? 553 HOH A O   1 
HETATM 2369 O  O   . HOH F 5 .   ? -2.181 1.302   34.355  1.00 32.70 ? 554 HOH A O   1 
HETATM 2370 O  O   . HOH F 5 .   ? -4.112 11.503  12.883  1.00 28.02 ? 555 HOH A O   1 
HETATM 2371 O  O   . HOH F 5 .   ? -3.779 13.963  6.366   1.00 29.76 ? 556 HOH A O   1 
HETATM 2372 O  O   . HOH F 5 .   ? -2.636 10.093  3.447   1.00 27.23 ? 557 HOH A O   1 
HETATM 2373 O  O   . HOH F 5 .   ? -0.531 17.479  3.740   1.00 35.09 ? 558 HOH A O   1 
HETATM 2374 O  O   . HOH F 5 .   ? 16.176 4.923   -5.865  1.00 38.20 ? 559 HOH A O   1 
HETATM 2375 O  O   . HOH F 5 .   ? 21.464 2.483   -6.659  1.00 33.01 ? 560 HOH A O   1 
HETATM 2376 O  O   . HOH F 5 .   ? 8.365  18.022  7.915   1.00 29.83 ? 561 HOH A O   1 
HETATM 2377 O  O   . HOH F 5 .   ? 7.825  20.855  8.476   1.00 24.71 ? 562 HOH A O   1 
HETATM 2378 O  O   . HOH F 5 .   ? 8.060  9.705   29.044  1.00 30.45 ? 563 HOH A O   1 
HETATM 2379 O  O   . HOH F 5 .   ? 6.887  11.221  31.673  1.00 38.07 ? 564 HOH A O   1 
HETATM 2380 O  O   . HOH F 5 .   ? 8.789  14.308  29.092  1.00 25.96 ? 565 HOH A O   1 
HETATM 2381 O  O   . HOH F 5 .   ? 10.412 -17.480 19.882  1.00 28.04 ? 566 HOH A O   1 
HETATM 2382 O  O   . HOH F 5 .   ? 3.690  -14.415 22.044  1.00 27.39 ? 567 HOH A O   1 
HETATM 2383 O  O   . HOH F 5 .   ? 3.962  -16.095 20.163  1.00 26.65 ? 568 HOH A O   1 
HETATM 2384 O  O   . HOH F 5 .   ? 12.440 -13.280 33.144  1.00 38.95 ? 569 HOH A O   1 
HETATM 2385 O  O   . HOH F 5 .   ? 10.462 -17.236 33.540  1.00 38.79 ? 570 HOH A O   1 
HETATM 2386 O  O   . HOH F 5 .   ? 19.019 -15.557 25.290  1.00 28.56 ? 571 HOH A O   1 
HETATM 2387 O  O   . HOH F 5 .   ? 3.842  -2.250  -5.164  1.00 37.39 ? 572 HOH A O   1 
HETATM 2388 O  O   . HOH F 5 .   ? 13.590 -8.304  -4.491  1.00 33.83 ? 573 HOH A O   1 
HETATM 2389 O  O   . HOH F 5 .   ? 16.995 -13.737 -2.212  1.00 33.64 ? 574 HOH A O   1 
HETATM 2390 O  O   . HOH F 5 .   ? 3.314  4.793   -6.631  1.00 34.05 ? 575 HOH A O   1 
HETATM 2391 O  O   . HOH F 5 .   ? 12.092 7.908   29.033  1.00 30.62 ? 576 HOH A O   1 
HETATM 2392 O  O   . HOH F 5 .   ? -0.409 -18.589 14.686  1.00 31.45 ? 577 HOH A O   1 
HETATM 2393 O  O   . HOH F 5 .   ? 29.186 -6.669  -0.191  1.00 34.54 ? 578 HOH A O   1 
HETATM 2394 O  O   . HOH F 5 .   ? 30.137 -8.606  -6.949  1.00 33.21 ? 579 HOH A O   1 
HETATM 2395 O  O   . HOH F 5 .   ? 22.619 -14.641 18.525  1.00 42.37 ? 580 HOH A O   1 
HETATM 2396 O  O   . HOH F 5 .   ? 31.136 -0.514  13.684  1.00 34.17 ? 581 HOH A O   1 
HETATM 2397 O  O   . HOH F 5 .   ? 24.705 6.394   10.409  1.00 41.74 ? 582 HOH A O   1 
HETATM 2398 O  O   . HOH F 5 .   ? 23.751 -11.603 8.122   1.00 30.52 ? 583 HOH A O   1 
HETATM 2399 O  O   . HOH F 5 .   ? 27.355 -13.557 6.060   1.00 37.14 ? 584 HOH A O   1 
HETATM 2400 O  O   . HOH F 5 .   ? 26.543 -10.840 5.503   1.00 30.19 ? 585 HOH A O   1 
HETATM 2401 O  O   . HOH F 5 .   ? 34.934 0.825   28.367  1.00 37.33 ? 586 HOH A O   1 
HETATM 2402 O  O   . HOH F 5 .   ? 11.754 4.806   34.590  1.00 32.84 ? 587 HOH A O   1 
HETATM 2403 O  O   . HOH F 5 .   ? 9.943  -13.427 33.970  1.00 38.65 ? 588 HOH A O   1 
HETATM 2404 O  O   . HOH F 5 .   ? 2.560  -7.130  34.777  1.00 32.85 ? 589 HOH A O   1 
HETATM 2405 O  O   . HOH F 5 .   ? 17.894 8.276   5.860   1.00 42.81 ? 590 HOH A O   1 
HETATM 2406 O  O   . HOH F 5 .   ? 17.022 17.348  11.253  1.00 36.76 ? 591 HOH A O   1 
HETATM 2407 O  O   . HOH F 5 .   ? 11.263 17.855  7.957   1.00 39.98 ? 592 HOH A O   1 
HETATM 2408 O  O   . HOH F 5 .   ? 1.297  18.240  18.903  1.00 34.26 ? 593 HOH A O   1 
HETATM 2409 O  O   . HOH F 5 .   ? 18.231 -15.904 5.280   1.00 35.08 ? 594 HOH A O   1 
HETATM 2410 O  O   . HOH F 5 .   ? 18.898 -10.179 31.376  1.00 46.30 ? 595 HOH A O   1 
HETATM 2411 O  O   . HOH F 5 .   ? 20.215 16.280  15.759  1.00 35.48 ? 596 HOH A O   1 
HETATM 2412 O  O   . HOH F 5 .   ? 10.348 22.730  24.970  1.00 29.31 ? 597 HOH A O   1 
HETATM 2413 O  O   . HOH F 5 .   ? 15.247 19.167  27.078  1.00 38.66 ? 598 HOH A O   1 
HETATM 2414 O  O   . HOH F 5 .   ? 13.558 -6.915  -2.466  1.00 31.11 ? 599 HOH A O   1 
HETATM 2415 O  O   . HOH F 5 .   ? 15.617 -10.775 -5.448  1.00 40.04 ? 600 HOH A O   1 
HETATM 2416 O  O   . HOH F 5 .   ? 8.383  5.504   -6.960  1.00 37.34 ? 601 HOH A O   1 
HETATM 2417 O  O   . HOH F 5 .   ? 16.171 -13.952 0.536   1.00 32.93 ? 602 HOH A O   1 
HETATM 2418 O  O   . HOH F 5 .   ? 26.929 -1.072  6.793   1.00 41.28 ? 603 HOH A O   1 
HETATM 2419 O  O   . HOH F 5 .   ? 27.334 -9.202  14.654  1.00 37.54 ? 604 HOH A O   1 
HETATM 2420 O  O   . HOH F 5 .   ? 31.939 -10.516 21.732  1.00 42.10 ? 605 HOH A O   1 
HETATM 2421 O  O   . HOH F 5 .   ? 4.072  -4.972  39.937  1.00 35.81 ? 606 HOH A O   1 
HETATM 2422 O  O   . HOH F 5 .   ? 1.101  -2.216  41.369  1.00 31.21 ? 607 HOH A O   1 
HETATM 2423 O  O   . HOH F 5 .   ? 0.280  10.245  29.946  1.00 33.13 ? 608 HOH A O   1 
HETATM 2424 O  O   . HOH F 5 .   ? -3.238 -0.069  28.944  1.00 39.20 ? 609 HOH A O   1 
HETATM 2425 O  O   . HOH F 5 .   ? -0.862 21.444  12.246  1.00 32.09 ? 610 HOH A O   1 
HETATM 2426 O  O   . HOH F 5 .   ? 22.650 14.361  22.220  1.00 38.76 ? 611 HOH A O   1 
HETATM 2427 O  O   . HOH F 5 .   ? -0.366 -11.906 23.172  1.00 32.34 ? 612 HOH A O   1 
HETATM 2428 O  O   . HOH F 5 .   ? 1.155  -13.855 22.380  1.00 33.92 ? 613 HOH A O   1 
HETATM 2429 O  O   . HOH F 5 .   ? 25.077 -11.387 22.032  1.00 46.79 ? 614 HOH A O   1 
HETATM 2430 O  O   . HOH F 5 .   ? 17.724 -15.959 -0.117  1.00 36.28 ? 615 HOH A O   1 
HETATM 2431 O  O   . HOH F 5 .   ? 12.581 -13.510 36.573  1.00 35.29 ? 616 HOH A O   1 
HETATM 2432 O  O   . HOH F 5 .   ? 27.741 7.490   28.490  1.00 39.55 ? 617 HOH A O   1 
HETATM 2433 O  O   . HOH F 5 .   ? -0.382 -4.937  -2.009  1.00 45.70 ? 618 HOH A O   1 
HETATM 2434 O  O   . HOH F 5 .   ? 19.407 5.089   -7.012  1.00 37.81 ? 619 HOH A O   1 
HETATM 2435 O  O   . HOH F 5 .   ? -3.129 1.668   1.189   1.00 38.32 ? 620 HOH A O   1 
HETATM 2436 O  O   . HOH F 5 .   ? 30.751 -11.500 9.217   1.00 45.79 ? 621 HOH A O   1 
HETATM 2437 O  O   . HOH F 5 .   ? 31.614 5.487   7.158   1.00 46.34 ? 622 HOH A O   1 
HETATM 2438 O  O   . HOH F 5 .   ? 14.016 7.449   6.468   1.00 37.72 ? 623 HOH A O   1 
HETATM 2439 O  O   . HOH F 5 .   ? 32.728 2.382   28.730  1.00 42.12 ? 624 HOH A O   1 
HETATM 2440 O  O   . HOH F 5 .   ? 29.983 9.494   18.607  1.00 40.33 ? 625 HOH A O   1 
HETATM 2441 O  O   . HOH F 5 .   ? 21.491 4.965   10.108  1.00 40.45 ? 626 HOH A O   1 
HETATM 2442 O  O   . HOH F 5 .   ? 9.645  2.985   -7.736  1.00 44.68 ? 627 HOH A O   1 
HETATM 2443 O  O   . HOH F 5 .   ? 8.447  11.725  -2.818  1.00 34.24 ? 628 HOH A O   1 
HETATM 2444 O  O   . HOH F 5 .   ? -3.999 6.562   8.138   1.00 39.98 ? 629 HOH A O   1 
HETATM 2445 O  O   . HOH F 5 .   ? 30.261 3.865   12.072  1.00 39.11 ? 630 HOH A O   1 
HETATM 2446 O  O   . HOH F 5 .   ? 35.095 -9.936  15.695  1.00 40.75 ? 631 HOH A O   1 
HETATM 2447 O  O   . HOH F 5 .   ? 18.593 -13.015 32.537  1.00 32.89 ? 632 HOH A O   1 
HETATM 2448 O  O   . HOH F 5 .   ? 1.366  17.140  16.591  1.00 29.11 ? 633 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 DMS 1   302 1   DMS DMS A . 
D 3 DMS 1   303 2   DMS DMS A . 
E 4 WWL 1   304 1   WWL WWL A . 
F 5 HOH 1   401 1   HOH HOH A . 
F 5 HOH 2   402 2   HOH HOH A . 
F 5 HOH 3   403 3   HOH HOH A . 
F 5 HOH 4   404 4   HOH HOH A . 
F 5 HOH 5   405 5   HOH HOH A . 
F 5 HOH 6   406 6   HOH HOH A . 
F 5 HOH 7   407 7   HOH HOH A . 
F 5 HOH 8   408 8   HOH HOH A . 
F 5 HOH 9   409 9   HOH HOH A . 
F 5 HOH 10  410 10  HOH HOH A . 
F 5 HOH 11  411 11  HOH HOH A . 
F 5 HOH 12  412 12  HOH HOH A . 
F 5 HOH 13  413 13  HOH HOH A . 
F 5 HOH 14  414 14  HOH HOH A . 
F 5 HOH 15  415 15  HOH HOH A . 
F 5 HOH 16  416 16  HOH HOH A . 
F 5 HOH 17  417 17  HOH HOH A . 
F 5 HOH 18  418 18  HOH HOH A . 
F 5 HOH 19  419 19  HOH HOH A . 
F 5 HOH 20  420 20  HOH HOH A . 
F 5 HOH 21  421 21  HOH HOH A . 
F 5 HOH 22  422 22  HOH HOH A . 
F 5 HOH 23  423 23  HOH HOH A . 
F 5 HOH 24  424 24  HOH HOH A . 
F 5 HOH 25  425 25  HOH HOH A . 
F 5 HOH 26  426 26  HOH HOH A . 
F 5 HOH 27  427 27  HOH HOH A . 
F 5 HOH 28  428 28  HOH HOH A . 
F 5 HOH 29  429 29  HOH HOH A . 
F 5 HOH 30  430 30  HOH HOH A . 
F 5 HOH 31  431 31  HOH HOH A . 
F 5 HOH 32  432 32  HOH HOH A . 
F 5 HOH 33  433 33  HOH HOH A . 
F 5 HOH 34  434 34  HOH HOH A . 
F 5 HOH 35  435 35  HOH HOH A . 
F 5 HOH 36  436 36  HOH HOH A . 
F 5 HOH 37  437 37  HOH HOH A . 
F 5 HOH 38  438 38  HOH HOH A . 
F 5 HOH 39  439 39  HOH HOH A . 
F 5 HOH 40  440 40  HOH HOH A . 
F 5 HOH 41  441 41  HOH HOH A . 
F 5 HOH 42  442 42  HOH HOH A . 
F 5 HOH 43  443 43  HOH HOH A . 
F 5 HOH 44  444 44  HOH HOH A . 
F 5 HOH 45  445 45  HOH HOH A . 
F 5 HOH 46  446 46  HOH HOH A . 
F 5 HOH 47  447 47  HOH HOH A . 
F 5 HOH 48  448 48  HOH HOH A . 
F 5 HOH 49  449 49  HOH HOH A . 
F 5 HOH 50  450 50  HOH HOH A . 
F 5 HOH 51  451 51  HOH HOH A . 
F 5 HOH 52  452 52  HOH HOH A . 
F 5 HOH 53  453 53  HOH HOH A . 
F 5 HOH 54  454 54  HOH HOH A . 
F 5 HOH 55  455 55  HOH HOH A . 
F 5 HOH 56  456 56  HOH HOH A . 
F 5 HOH 57  457 57  HOH HOH A . 
F 5 HOH 58  458 58  HOH HOH A . 
F 5 HOH 59  459 59  HOH HOH A . 
F 5 HOH 60  460 60  HOH HOH A . 
F 5 HOH 61  461 61  HOH HOH A . 
F 5 HOH 62  462 62  HOH HOH A . 
F 5 HOH 63  463 63  HOH HOH A . 
F 5 HOH 64  464 64  HOH HOH A . 
F 5 HOH 65  465 65  HOH HOH A . 
F 5 HOH 66  466 66  HOH HOH A . 
F 5 HOH 67  467 67  HOH HOH A . 
F 5 HOH 68  468 68  HOH HOH A . 
F 5 HOH 69  469 69  HOH HOH A . 
F 5 HOH 70  470 70  HOH HOH A . 
F 5 HOH 71  471 71  HOH HOH A . 
F 5 HOH 72  472 72  HOH HOH A . 
F 5 HOH 73  473 73  HOH HOH A . 
F 5 HOH 74  474 74  HOH HOH A . 
F 5 HOH 75  475 75  HOH HOH A . 
F 5 HOH 76  476 76  HOH HOH A . 
F 5 HOH 77  477 77  HOH HOH A . 
F 5 HOH 78  478 78  HOH HOH A . 
F 5 HOH 79  479 79  HOH HOH A . 
F 5 HOH 80  480 80  HOH HOH A . 
F 5 HOH 81  481 81  HOH HOH A . 
F 5 HOH 82  482 82  HOH HOH A . 
F 5 HOH 83  483 83  HOH HOH A . 
F 5 HOH 84  484 84  HOH HOH A . 
F 5 HOH 85  485 85  HOH HOH A . 
F 5 HOH 86  486 86  HOH HOH A . 
F 5 HOH 87  487 87  HOH HOH A . 
F 5 HOH 88  488 88  HOH HOH A . 
F 5 HOH 89  489 89  HOH HOH A . 
F 5 HOH 90  490 90  HOH HOH A . 
F 5 HOH 91  491 91  HOH HOH A . 
F 5 HOH 92  492 92  HOH HOH A . 
F 5 HOH 93  493 93  HOH HOH A . 
F 5 HOH 94  494 94  HOH HOH A . 
F 5 HOH 95  495 95  HOH HOH A . 
F 5 HOH 96  496 96  HOH HOH A . 
F 5 HOH 97  497 97  HOH HOH A . 
F 5 HOH 98  498 98  HOH HOH A . 
F 5 HOH 99  499 99  HOH HOH A . 
F 5 HOH 100 500 100 HOH HOH A . 
F 5 HOH 101 501 101 HOH HOH A . 
F 5 HOH 102 502 102 HOH HOH A . 
F 5 HOH 103 503 103 HOH HOH A . 
F 5 HOH 104 504 104 HOH HOH A . 
F 5 HOH 105 505 105 HOH HOH A . 
F 5 HOH 106 506 106 HOH HOH A . 
F 5 HOH 107 507 107 HOH HOH A . 
F 5 HOH 108 508 108 HOH HOH A . 
F 5 HOH 109 509 109 HOH HOH A . 
F 5 HOH 110 510 110 HOH HOH A . 
F 5 HOH 111 511 111 HOH HOH A . 
F 5 HOH 112 512 112 HOH HOH A . 
F 5 HOH 113 513 113 HOH HOH A . 
F 5 HOH 114 514 114 HOH HOH A . 
F 5 HOH 115 515 115 HOH HOH A . 
F 5 HOH 116 516 116 HOH HOH A . 
F 5 HOH 117 517 117 HOH HOH A . 
F 5 HOH 118 518 118 HOH HOH A . 
F 5 HOH 119 519 119 HOH HOH A . 
F 5 HOH 120 520 120 HOH HOH A . 
F 5 HOH 121 521 121 HOH HOH A . 
F 5 HOH 122 522 122 HOH HOH A . 
F 5 HOH 123 523 123 HOH HOH A . 
F 5 HOH 124 524 124 HOH HOH A . 
F 5 HOH 125 525 125 HOH HOH A . 
F 5 HOH 126 526 126 HOH HOH A . 
F 5 HOH 127 527 127 HOH HOH A . 
F 5 HOH 128 528 128 HOH HOH A . 
F 5 HOH 129 529 129 HOH HOH A . 
F 5 HOH 130 530 130 HOH HOH A . 
F 5 HOH 131 531 131 HOH HOH A . 
F 5 HOH 132 532 132 HOH HOH A . 
F 5 HOH 133 533 133 HOH HOH A . 
F 5 HOH 134 534 134 HOH HOH A . 
F 5 HOH 135 535 135 HOH HOH A . 
F 5 HOH 136 536 136 HOH HOH A . 
F 5 HOH 137 537 137 HOH HOH A . 
F 5 HOH 138 538 138 HOH HOH A . 
F 5 HOH 139 539 139 HOH HOH A . 
F 5 HOH 140 540 140 HOH HOH A . 
F 5 HOH 141 541 141 HOH HOH A . 
F 5 HOH 142 542 142 HOH HOH A . 
F 5 HOH 143 543 143 HOH HOH A . 
F 5 HOH 144 544 144 HOH HOH A . 
F 5 HOH 145 545 145 HOH HOH A . 
F 5 HOH 146 546 146 HOH HOH A . 
F 5 HOH 147 547 147 HOH HOH A . 
F 5 HOH 148 548 148 HOH HOH A . 
F 5 HOH 149 549 149 HOH HOH A . 
F 5 HOH 150 550 150 HOH HOH A . 
F 5 HOH 151 551 151 HOH HOH A . 
F 5 HOH 152 552 152 HOH HOH A . 
F 5 HOH 153 553 153 HOH HOH A . 
F 5 HOH 154 554 154 HOH HOH A . 
F 5 HOH 155 555 155 HOH HOH A . 
F 5 HOH 156 556 156 HOH HOH A . 
F 5 HOH 157 557 157 HOH HOH A . 
F 5 HOH 158 558 158 HOH HOH A . 
F 5 HOH 159 559 159 HOH HOH A . 
F 5 HOH 160 560 160 HOH HOH A . 
F 5 HOH 161 561 161 HOH HOH A . 
F 5 HOH 162 562 162 HOH HOH A . 
F 5 HOH 163 563 163 HOH HOH A . 
F 5 HOH 164 564 164 HOH HOH A . 
F 5 HOH 165 565 165 HOH HOH A . 
F 5 HOH 166 566 166 HOH HOH A . 
F 5 HOH 167 567 167 HOH HOH A . 
F 5 HOH 168 568 168 HOH HOH A . 
F 5 HOH 169 569 169 HOH HOH A . 
F 5 HOH 170 570 170 HOH HOH A . 
F 5 HOH 171 571 171 HOH HOH A . 
F 5 HOH 172 572 172 HOH HOH A . 
F 5 HOH 173 573 173 HOH HOH A . 
F 5 HOH 174 574 174 HOH HOH A . 
F 5 HOH 175 575 175 HOH HOH A . 
F 5 HOH 176 576 176 HOH HOH A . 
F 5 HOH 177 577 177 HOH HOH A . 
F 5 HOH 178 578 178 HOH HOH A . 
F 5 HOH 179 579 179 HOH HOH A . 
F 5 HOH 180 580 180 HOH HOH A . 
F 5 HOH 181 581 181 HOH HOH A . 
F 5 HOH 182 582 182 HOH HOH A . 
F 5 HOH 183 583 183 HOH HOH A . 
F 5 HOH 184 584 184 HOH HOH A . 
F 5 HOH 185 585 185 HOH HOH A . 
F 5 HOH 186 586 186 HOH HOH A . 
F 5 HOH 187 587 187 HOH HOH A . 
F 5 HOH 188 588 188 HOH HOH A . 
F 5 HOH 189 589 189 HOH HOH A . 
F 5 HOH 190 590 190 HOH HOH A . 
F 5 HOH 191 591 191 HOH HOH A . 
F 5 HOH 192 592 192 HOH HOH A . 
F 5 HOH 193 593 193 HOH HOH A . 
F 5 HOH 194 594 194 HOH HOH A . 
F 5 HOH 195 595 195 HOH HOH A . 
F 5 HOH 196 596 196 HOH HOH A . 
F 5 HOH 197 597 197 HOH HOH A . 
F 5 HOH 198 598 198 HOH HOH A . 
F 5 HOH 199 599 199 HOH HOH A . 
F 5 HOH 200 600 200 HOH HOH A . 
F 5 HOH 201 601 201 HOH HOH A . 
F 5 HOH 202 602 202 HOH HOH A . 
F 5 HOH 203 603 203 HOH HOH A . 
F 5 HOH 204 604 204 HOH HOH A . 
F 5 HOH 205 605 205 HOH HOH A . 
F 5 HOH 206 606 206 HOH HOH A . 
F 5 HOH 207 607 207 HOH HOH A . 
F 5 HOH 208 608 208 HOH HOH A . 
F 5 HOH 209 609 209 HOH HOH A . 
F 5 HOH 210 610 210 HOH HOH A . 
F 5 HOH 211 611 211 HOH HOH A . 
F 5 HOH 212 612 212 HOH HOH A . 
F 5 HOH 213 613 213 HOH HOH A . 
F 5 HOH 214 614 214 HOH HOH A . 
F 5 HOH 215 615 215 HOH HOH A . 
F 5 HOH 216 616 216 HOH HOH A . 
F 5 HOH 217 617 217 HOH HOH A . 
F 5 HOH 218 618 218 HOH HOH A . 
F 5 HOH 219 619 219 HOH HOH A . 
F 5 HOH 220 620 220 HOH HOH A . 
F 5 HOH 221 621 221 HOH HOH A . 
F 5 HOH 222 622 222 HOH HOH A . 
F 5 HOH 223 623 223 HOH HOH A . 
F 5 HOH 224 624 224 HOH HOH A . 
F 5 HOH 225 625 225 HOH HOH A . 
F 5 HOH 226 626 226 HOH HOH A . 
F 5 HOH 227 627 227 HOH HOH A . 
F 5 HOH 228 628 228 HOH HOH A . 
F 5 HOH 229 629 229 HOH HOH A . 
F 5 HOH 230 630 230 HOH HOH A . 
F 5 HOH 231 631 231 HOH HOH A . 
F 5 HOH 232 632 232 HOH HOH A . 
F 5 HOH 233 633 233 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 105.2 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 114.2 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 100.6 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? E WWL .   ? A WWL 304 ? 1_555 110.0 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? E WWL .   ? A WWL 304 ? 1_555 109.4 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? E WWL .   ? A WWL 304 ? 1_555 116.3 ? 
# 
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 2014-07-02 
2 'Structure model' 1 1 2023-11-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' pdbx_initial_refinement_model 
5 2 'Structure model' pdbx_struct_conn_angle        
6 2 'Structure model' struct_conn                   
7 2 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_database_2.pdbx_DOI'                        
2  2 'Structure model' '_database_2.pdbx_database_accession'         
3  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
15 2 'Structure model' '_pdbx_struct_conn_angle.value'               
16 2 'Structure model' '_struct_conn.pdbx_dist_value'                
17 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
18 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
19 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
20 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
21 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
22 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
23 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
24 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
25 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
26 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
27 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
28 2 'Structure model' '_struct_site.pdbx_auth_asym_id'              
29 2 'Structure model' '_struct_site.pdbx_auth_comp_id'              
30 2 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.3.20 2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
DNA         .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             4 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            B 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             4 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            B 
_pdbx_validate_rmsd_bond.bond_value                1.411 
_pdbx_validate_rmsd_bond.bond_target_value         1.354 
_pdbx_validate_rmsd_bond.bond_deviation            0.057 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.009 
_pdbx_validate_rmsd_bond.linker_flag               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 ALA A 77  ? ? 54.93   79.76   
2 1 LYS A 111 ? ? 69.71   -1.86   
3 1 ALA A 174 ? B -126.14 -129.78 
4 1 PHE A 176 ? ? -152.16 78.10   
5 1 ASN A 244 ? ? -93.03  50.30   
6 1 LYS A 252 ? ? 60.50   -143.44 
7 1 LYS A 252 ? ? 60.50   -140.55 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
VAL N    N  N N 382 
VAL CA   C  N S 383 
VAL C    C  N N 384 
VAL O    O  N N 385 
VAL CB   C  N N 386 
VAL CG1  C  N N 387 
VAL CG2  C  N N 388 
VAL OXT  O  N N 389 
VAL H    H  N N 390 
VAL H2   H  N N 391 
VAL HA   H  N N 392 
VAL HB   H  N N 393 
VAL HG11 H  N N 394 
VAL HG12 H  N N 395 
VAL HG13 H  N N 396 
VAL HG21 H  N N 397 
VAL HG22 H  N N 398 
VAL HG23 H  N N 399 
VAL HXT  H  N N 400 
WWL O12  O  N N 401 
WWL S10  S  N N 402 
WWL O11  O  N N 403 
WWL C7   C  Y N 404 
WWL S8   S  Y N 405 
WWL C5   C  Y N 406 
WWL C6   C  Y N 407 
WWL C9   C  Y N 408 
WWL S2   S  N N 409 
WWL O3   O  N N 410 
WWL N4   N  N N 411 
WWL O1   O  N N 412 
WWL C13  C  Y N 413 
WWL C18  C  Y N 414 
WWL C17  C  Y N 415 
WWL C16  C  Y N 416 
WWL C15  C  Y N 417 
WWL C14  C  Y N 418 
WWL H1   H  N N 419 
WWL H2   H  N N 420 
WWL H3   H  N N 421 
WWL H4   H  N N 422 
WWL H5   H  N N 423 
WWL H6   H  N N 424 
WWL H7   H  N N 425 
WWL H8   H  N N 426 
WWL H9   H  N N 427 
ZN  ZN   ZN N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
WWL O11 S10  doub N N 385 
WWL C18 C17  doub Y N 386 
WWL C18 C13  sing Y N 387 
WWL C17 C16  sing Y N 388 
WWL S10 O12  doub N N 389 
WWL S10 C13  sing N N 390 
WWL S10 C7   sing N N 391 
WWL C13 C14  doub Y N 392 
WWL C7  C6   doub Y N 393 
WWL C7  S8   sing Y N 394 
WWL C6  C5   sing Y N 395 
WWL C16 C15  doub Y N 396 
WWL C14 C15  sing Y N 397 
WWL S8  C9   sing Y N 398 
WWL C5  C9   doub Y N 399 
WWL C9  S2   sing N N 400 
WWL N4  S2   sing N N 401 
WWL O3  S2   doub N N 402 
WWL S2  O1   doub N N 403 
WWL C5  H1   sing N N 404 
WWL C6  H2   sing N N 405 
WWL N4  H3   sing N N 406 
WWL N4  H4   sing N N 407 
WWL C18 H5   sing N N 408 
WWL C17 H6   sing N N 409 
WWL C16 H7   sing N N 410 
WWL C15 H8   sing N N 411 
WWL C14 H9   sing N N 412 
# 
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-(phenylsulfonyl)thiophene-2-sulfonamide' WWL 
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          ? 
# 
