data_3M67
# 
_entry.id   3M67 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.380 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   3M67         pdb_00003m67 10.2210/pdb3m67/pdb 
RCSB  RCSB058158   ?            ?                   
WWPDB D_1000058158 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3m2n 'the same protein with another ligand' unspecified 
PDB 3m3x 'the same protein with another ligand' unspecified 
PDB 3m40 'the same protein with another ligand' unspecified 
PDB 3m5e 'the same protein with another ligand' unspecified 
# 
_pdbx_database_status.entry_id                        3M67 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2010-03-15 
_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            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'  1 
'Manakova, E.'  2 
'Golovenko, D.' 3 
# 
_citation.id                        primary 
_citation.title                     'Indapamide-like benzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, and XIII' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            18 
_citation.page_first                7357 
_citation.page_last                 7364 
_citation.year                      2010 
_citation.journal_id_ASTM           BMECEP 
_citation.country                   UK 
_citation.journal_id_ISSN           0968-0896 
_citation.journal_id_CSD            1200 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20926301 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2010.09.016 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1 ? 
primary 'Baranauskiene, L.' 2 ? 
primary 'Golovenko, D.'     3 ? 
primary 'Manakova, E.'      4 ? 
primary 'Grazulis, S.'      5 ? 
primary 'Tumkevicius, S.'   6 ? 
primary 'Matulis, D.'       7 ? 
# 
_cell.entry_id           3M67 
_cell.length_a           41.972 
_cell.length_b           41.007 
_cell.length_c           71.681 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.430 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              2 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3M67 
_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 '2-chloro-5-[(6,7-dihydro-1H-[1,4]dioxino[2,3-f]benzimidazol-2-ylsulfanyl)acetyl]benzenesulfonamide' 439.893   1 
?       ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                                           65.409    1 
?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                 78.133    2 
?       ? ? ? 
5 water       nat water                                                                                                18.015    
158 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonic anhydrase II, CA-II, Carbonate dehydratase II, Carbonic anhydrase C, CAC' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3M67 
_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  
E36 non-polymer         . '2-chloro-5-[(6,7-dihydro-1H-[1,4]dioxino[2,3-f]benzimidazol-2-ylsulfanyl)acetyl]benzenesulfonamide' ? 
'C17 H14 Cl N3 O5 S2' 439.893 
GLN 'L-peptide linking' y GLUTAMINE                                                                                            ? 
'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                      ? 
'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                                                              ? 
'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                            ? 
'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                                                                ? 
'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                           ? 
'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                              ? 
'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                                               ? 
'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                                           ? 
'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                                        ? 
'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                                                              ? 
'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                                                               ? 
'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                                                                            ? 
'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                           ? 
'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                             ? 
'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                                                                               ? 
'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                                                                           ? 
'Zn 2'                65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3M67 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.880 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.04 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   39.70 
_exptl_crystal.size_max              ? 
_exptl_crystal.size_mid              ? 
_exptl_crystal.size_min              ? 
_exptl_crystal.size_rad              ? 
_exptl_crystal.description           'The data was collected by EMBL X13 beamline at the DORIS storage ring.' 
_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            293 
_exptl_crystal_grow.pdbx_details    '0.1M Na-bicine pH 9.0, 2M Na-Malonate pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2009-12-17 
_diffrn_detector.details                'Bent, vertically focussing mirror' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si [111], horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8120 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.pdbx_wavelength_list        0.8120 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
# 
_reflns.entry_id                     3M67 
_reflns.d_resolution_high            1.80 
_reflns.d_resolution_low             40.656 
_reflns.number_all                   22174 
_reflns.number_obs                   22019 
_reflns.pdbx_Rmerge_I_obs            0.052 
_reflns.pdbx_netI_over_sigmaI        31.500 
_reflns.pdbx_Rsym_value              0.052 
_reflns.pdbx_redundancy              7.500 
_reflns.percent_possible_obs         99.300 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   ? 
_reflns.B_iso_Wilson_estimate        19.3 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.80 
_reflns_shell.d_res_low              1.90 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    24150 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.222 
_reflns_shell.meanI_over_sigI_obs    7.0 
_reflns_shell.pdbx_Rsym_value        0.222 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_redundancy        7.60 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      3191 
_reflns_shell.percent_possible_all   99.00 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3M67 
_refine.ls_d_res_high                            1.800 
_refine.ls_d_res_low                             25.130 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.320 
_refine.ls_number_reflns_obs                     22008 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.181 
_refine.ls_R_factor_R_work                       0.176 
_refine.ls_wR_factor_R_work                      0.169 
_refine.ls_R_factor_R_free                       0.228 
_refine.ls_wR_factor_R_free                      0.216 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  2209 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.913 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.040 
_refine.aniso_B[2][2]                            -1.000 
_refine.aniso_B[3][3]                            1.100 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.110 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.954 
_refine.correlation_coeff_Fo_to_Fc_free          0.926 
_refine.overall_SU_R_Cruickshank_DPI             0.153 
_refine.overall_SU_R_free                        0.145 
_refine.pdbx_overall_ESU_R                       0.153 
_refine.pdbx_overall_ESU_R_Free                  0.145 
_refine.overall_SU_ML                            0.094 
_refine.overall_SU_B                             2.949 
_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                   0.852 
_refine.B_iso_max                                50.06 
_refine.B_iso_min                                5.16 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 2NNO' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.number_atoms_solvent             158 
_refine_hist.number_atoms_total               2244 
_refine_hist.d_res_high                       1.800 
_refine_hist.d_res_low                        25.130 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         2207 0.027  0.022  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      3009 2.061  1.965  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   271  6.984  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   102  37.827 24.706 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   363  14.909 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   7    17.316 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           310  0.158  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     1716 0.012  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            953  0.222  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          1404 0.309  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    132  0.164  0.200  ? 'X-RAY DIFFRACTION' ? 
r_metal_ion_refined      3    0.062  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   78   0.242  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 27   0.244  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              1374 1.439  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             2132 2.032  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              1020 3.017  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             872  4.208  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               99.380 
_refine_ls_shell.number_reflns_R_work             1455 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.224 
_refine_ls_shell.R_factor_R_free                  0.355 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             148 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1603 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3M67 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 2-chloro-5-[(6,7-dihydro-1H-[1,4]dioxino[2,3-f]benzimidazol-2-ylsulfanyl)acetyl]benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3M67 
_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 4 ? 
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  ? TRP A 16  ? GLY A 12  TRP A 16  5 ? 5 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 1.82 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 2.17 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N TRP A 191 ? N TRP A 192 O VAL A 210 ? O VAL A 211 
B 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A E36 262 ? 16 'BINDING SITE FOR RESIDUE E36 A 262' 
AC2 Software A ZN  263 ? 4  'BINDING SITE FOR RESIDUE ZN A 263'  
AC3 Software A DMS 264 ? 5  'BINDING SITE FOR RESIDUE DMS A 264' 
AC4 Software A DMS 265 ? 3  'BINDING SITE FOR RESIDUE DMS A 265' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 16 ASN A 62  ? ASN A 62  . ? 1_555 ? 
2  AC1 16 ASN A 67  ? ASN A 67  . ? 1_555 ? 
3  AC1 16 GLN A 92  ? GLN A 92  . ? 1_555 ? 
4  AC1 16 HIS A 94  ? HIS A 94  . ? 1_555 ? 
5  AC1 16 HIS A 96  ? HIS A 96  . ? 1_555 ? 
6  AC1 16 HIS A 119 ? HIS A 119 . ? 1_555 ? 
7  AC1 16 LEU A 140 ? LEU A 141 . ? 1_555 ? 
8  AC1 16 VAL A 142 ? VAL A 143 . ? 1_555 ? 
9  AC1 16 LEU A 197 ? LEU A 198 . ? 1_555 ? 
10 AC1 16 THR A 198 ? THR A 199 . ? 1_555 ? 
11 AC1 16 THR A 199 ? THR A 200 . ? 1_555 ? 
12 AC1 16 PRO A 201 ? PRO A 202 . ? 1_555 ? 
13 AC1 16 TRP A 208 ? TRP A 209 . ? 1_555 ? 
14 AC1 16 ZN  C .   ? ZN  A 263 . ? 1_555 ? 
15 AC1 16 DMS E .   ? DMS A 265 . ? 1_555 ? 
16 AC1 16 HOH F .   ? HOH A 408 . ? 1_555 ? 
17 AC2 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
18 AC2 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
19 AC2 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
20 AC2 4  E36 B .   ? E36 A 262 . ? 1_555 ? 
21 AC3 5  TYR A 7   ? TYR A 7   . ? 1_555 ? 
22 AC3 5  ASP A 242 ? ASP A 243 . ? 1_555 ? 
23 AC3 5  TRP A 244 ? TRP A 245 . ? 1_555 ? 
24 AC3 5  PRO A 246 ? PRO A 247 . ? 1_555 ? 
25 AC3 5  HOH F .   ? HOH A 373 . ? 1_555 ? 
26 AC4 3  ASN A 67  ? ASN A 67  . ? 1_555 ? 
27 AC4 3  GLN A 92  ? GLN A 92  . ? 1_555 ? 
28 AC4 3  E36 B .   ? E36 A 262 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3M67 
_atom_sites.fract_transf_matrix[1][1]   0.023825 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006131 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024386 
_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]   0.014405 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . HIS A 1 4   ? 9.114   1.376   8.045   1.00 27.82 ? 4   HIS A N    1 
ATOM   2    C  CA   . HIS A 1 4   ? 9.966   0.214   8.508   1.00 28.54 ? 4   HIS A CA   1 
ATOM   3    C  C    . HIS A 1 4   ? 9.333   -0.753  9.529   1.00 26.14 ? 4   HIS A C    1 
ATOM   4    O  O    . HIS A 1 4   ? 9.567   -1.946  9.437   1.00 26.06 ? 4   HIS A O    1 
ATOM   5    C  CB   . HIS A 1 4   ? 11.295  0.650   9.056   1.00 30.84 ? 4   HIS A CB   1 
ATOM   6    C  CG   . HIS A 1 4   ? 12.398  -0.327  8.806   1.00 32.90 ? 4   HIS A CG   1 
ATOM   7    N  ND1  . HIS A 1 4   ? 12.855  -1.183  9.785   1.00 39.32 ? 4   HIS A ND1  1 
ATOM   8    C  CD2  . HIS A 1 4   ? 13.143  -0.582  7.689   1.00 37.56 ? 4   HIS A CD2  1 
ATOM   9    C  CE1  . HIS A 1 4   ? 13.842  -1.920  9.286   1.00 41.81 ? 4   HIS A CE1  1 
ATOM   10   N  NE2  . HIS A 1 4   ? 14.034  -1.572  8.020   1.00 40.57 ? 4   HIS A NE2  1 
ATOM   11   N  N    . TRP A 1 5   ? 8.564   -0.263  10.494  1.00 23.28 ? 5   TRP A N    1 
ATOM   12   C  CA   . TRP A 1 5   ? 7.754   -1.207  11.289  1.00 19.27 ? 5   TRP A CA   1 
ATOM   13   C  C    . TRP A 1 5   ? 6.813   -2.045  10.443  1.00 17.99 ? 5   TRP A C    1 
ATOM   14   O  O    . TRP A 1 5   ? 6.315   -1.620  9.358   1.00 16.34 ? 5   TRP A O    1 
ATOM   15   C  CB   . TRP A 1 5   ? 7.026   -0.511  12.490  1.00 17.52 ? 5   TRP A CB   1 
ATOM   16   C  CG   . TRP A 1 5   ? 5.864   0.262   12.115  1.00 18.49 ? 5   TRP A CG   1 
ATOM   17   C  CD1  . TRP A 1 5   ? 5.784   1.582   11.737  1.00 21.07 ? 5   TRP A CD1  1 
ATOM   18   C  CD2  . TRP A 1 5   ? 4.541   -0.245  12.084  1.00 15.76 ? 5   TRP A CD2  1 
ATOM   19   N  NE1  . TRP A 1 5   ? 4.459   1.911   11.462  1.00 20.72 ? 5   TRP A NE1  1 
ATOM   20   C  CE2  . TRP A 1 5   ? 3.686   0.799   11.650  1.00 19.62 ? 5   TRP A CE2  1 
ATOM   21   C  CE3  . TRP A 1 5   ? 4.016   -1.492  12.334  1.00 13.07 ? 5   TRP A CE3  1 
ATOM   22   C  CZ2  . TRP A 1 5   ? 2.312   0.637   11.531  1.00 18.75 ? 5   TRP A CZ2  1 
ATOM   23   C  CZ3  . TRP A 1 5   ? 2.603   -1.662  12.168  1.00 17.48 ? 5   TRP A CZ3  1 
ATOM   24   C  CH2  . TRP A 1 5   ? 1.797   -0.600  11.777  1.00 19.43 ? 5   TRP A CH2  1 
ATOM   25   N  N    . GLY A 1 6   ? 6.589   -3.278  10.936  1.00 17.07 ? 6   GLY A N    1 
ATOM   26   C  CA   . GLY A 1 6   ? 5.628   -4.142  10.280  1.00 16.33 ? 6   GLY A CA   1 
ATOM   27   C  C    . GLY A 1 6   ? 5.203   -5.249  11.212  1.00 16.34 ? 6   GLY A C    1 
ATOM   28   O  O    . GLY A 1 6   ? 5.227   -5.105  12.448  1.00 15.45 ? 6   GLY A O    1 
ATOM   29   N  N    . TYR A 1 7   ? 4.836   -6.391  10.637  1.00 16.25 ? 7   TYR A N    1 
ATOM   30   C  CA   . TYR A 1 7   ? 4.446   -7.551  11.475  1.00 17.07 ? 7   TYR A CA   1 
ATOM   31   C  C    . TYR A 1 7   ? 5.364   -8.803  11.376  1.00 20.31 ? 7   TYR A C    1 
ATOM   32   O  O    . TYR A 1 7   ? 5.105   -9.847  12.021  1.00 20.01 ? 7   TYR A O    1 
ATOM   33   C  CB   . TYR A 1 7   ? 2.959   -7.921  11.228  1.00 14.31 ? 7   TYR A CB   1 
ATOM   34   C  CG   . TYR A 1 7   ? 2.053   -6.861  11.813  1.00 11.45 ? 7   TYR A CG   1 
ATOM   35   C  CD1  . TYR A 1 7   ? 1.699   -6.875  13.184  1.00 14.12 ? 7   TYR A CD1  1 
ATOM   36   C  CD2  . TYR A 1 7   ? 1.549   -5.868  10.978  1.00 11.61 ? 7   TYR A CD2  1 
ATOM   37   C  CE1  . TYR A 1 7   ? 0.812   -5.838  13.686  1.00 10.62 ? 7   TYR A CE1  1 
ATOM   38   C  CE2  . TYR A 1 7   ? 0.751   -4.859  11.452  1.00 9.21  ? 7   TYR A CE2  1 
ATOM   39   C  CZ   . TYR A 1 7   ? 0.359   -4.897  12.800  1.00 11.82 ? 7   TYR A CZ   1 
ATOM   40   O  OH   . TYR A 1 7   ? -0.440  -3.839  13.235  1.00 11.76 ? 7   TYR A OH   1 
ATOM   41   N  N    . GLY A 1 8   ? 6.476   -8.670  10.646  1.00 22.78 ? 8   GLY A N    1 
ATOM   42   C  CA   . GLY A 1 8   ? 7.495   -9.800  10.598  1.00 23.24 ? 8   GLY A CA   1 
ATOM   43   C  C    . GLY A 1 8   ? 8.505   -10.073 11.697  1.00 24.71 ? 8   GLY A C    1 
ATOM   44   O  O    . GLY A 1 8   ? 8.572   -9.398  12.775  1.00 24.43 ? 8   GLY A O    1 
ATOM   45   N  N    . LYS A 1 9   ? 9.331   -11.118 11.419  1.00 24.24 ? 9   LYS A N    1 
ATOM   46   C  CA   . LYS A 1 9   ? 10.334  -11.632 12.353  1.00 23.26 ? 9   LYS A CA   1 
ATOM   47   C  C    . LYS A 1 9   ? 11.305  -10.520 12.780  1.00 21.72 ? 9   LYS A C    1 
ATOM   48   O  O    . LYS A 1 9   ? 11.664  -10.429 13.988  1.00 22.56 ? 9   LYS A O    1 
ATOM   49   C  CB   . LYS A 1 9   ? 11.122  -12.759 11.677  1.00 24.14 ? 9   LYS A CB   1 
ATOM   50   C  CG   . LYS A 1 9   ? 12.226  -13.336 12.532  1.00 25.78 ? 9   LYS A CG   1 
ATOM   51   C  CD   . LYS A 1 9   ? 12.832  -14.592 11.913  0.01 25.19 ? 9   LYS A CD   1 
ATOM   52   C  CE   . LYS A 1 9   ? 11.986  -15.829 12.194  0.01 25.29 ? 9   LYS A CE   1 
ATOM   53   N  NZ   . LYS A 1 9   ? 12.579  -17.059 11.600  0.01 25.15 ? 9   LYS A NZ   1 
ATOM   54   N  N    A HIS A 1 10  ? 11.596  -9.673  11.800  0.50 21.28 ? 10  HIS A N    1 
ATOM   55   N  N    B HIS A 1 10  ? 11.667  -9.660  11.825  0.50 21.05 ? 10  HIS A N    1 
ATOM   56   C  CA   A HIS A 1 10  ? 12.643  -8.663  11.841  0.50 20.46 ? 10  HIS A CA   1 
ATOM   57   C  CA   B HIS A 1 10  ? 12.700  -8.602  12.000  0.50 19.78 ? 10  HIS A CA   1 
ATOM   58   C  C    A HIS A 1 10  ? 12.120  -7.265  12.223  0.50 20.28 ? 10  HIS A C    1 
ATOM   59   C  C    B HIS A 1 10  ? 12.157  -7.151  12.016  0.50 19.85 ? 10  HIS A C    1 
ATOM   60   O  O    A HIS A 1 10  ? 12.876  -6.462  12.767  0.50 19.13 ? 10  HIS A O    1 
ATOM   61   O  O    B HIS A 1 10  ? 12.932  -6.181  12.056  0.50 18.18 ? 10  HIS A O    1 
ATOM   62   C  CB   A HIS A 1 10  ? 13.361  -8.647  10.474  0.50 19.69 ? 10  HIS A CB   1 
ATOM   63   C  CB   B HIS A 1 10  ? 13.781  -8.723  10.905  0.50 19.25 ? 10  HIS A CB   1 
ATOM   64   C  CG   A HIS A 1 10  ? 13.849  -9.999  10.031  0.50 19.82 ? 10  HIS A CG   1 
ATOM   65   C  CG   B HIS A 1 10  ? 14.397  -10.088 10.793  0.50 17.54 ? 10  HIS A CG   1 
ATOM   66   N  ND1  A HIS A 1 10  ? 14.884  -10.664 10.660  0.50 17.99 ? 10  HIS A ND1  1 
ATOM   67   N  ND1  B HIS A 1 10  ? 15.407  -10.521 11.624  0.50 14.55 ? 10  HIS A ND1  1 
ATOM   68   C  CD2  A HIS A 1 10  ? 13.447  -10.805 9.013   0.50 20.78 ? 10  HIS A CD2  1 
ATOM   69   C  CD2  B HIS A 1 10  ? 14.162  -11.101 9.928   0.50 18.91 ? 10  HIS A CD2  1 
ATOM   70   C  CE1  A HIS A 1 10  ? 15.069  -11.836 10.076  0.50 20.33 ? 10  HIS A CE1  1 
ATOM   71   C  CE1  B HIS A 1 10  ? 15.765  -11.739 11.273  0.50 13.72 ? 10  HIS A CE1  1 
ATOM   72   N  NE2  A HIS A 1 10  ? 14.220  -11.943 9.068   0.50 16.97 ? 10  HIS A NE2  1 
ATOM   73   N  NE2  B HIS A 1 10  ? 14.999  -12.132 10.270  0.50 17.38 ? 10  HIS A NE2  1 
ATOM   74   N  N    . ASN A 1 11  ? 10.833  -6.981  11.952  1.00 19.61 ? 11  ASN A N    1 
ATOM   75   C  CA   . ASN A 1 11  ? 10.271  -5.631  12.185  1.00 19.17 ? 11  ASN A CA   1 
ATOM   76   C  C    . ASN A 1 11  ? 8.922   -5.608  12.954  1.00 20.75 ? 11  ASN A C    1 
ATOM   77   O  O    . ASN A 1 11  ? 8.214   -4.543  12.948  1.00 19.50 ? 11  ASN A O    1 
ATOM   78   C  CB   . ASN A 1 11  ? 10.082  -4.913  10.856  1.00 19.18 ? 11  ASN A CB   1 
ATOM   79   C  CG   . ASN A 1 11  ? 9.020   -5.547  9.977   1.00 22.32 ? 11  ASN A CG   1 
ATOM   80   O  OD1  . ASN A 1 11  ? 8.512   -6.655  10.270  1.00 25.01 ? 11  ASN A OD1  1 
ATOM   81   N  ND2  . ASN A 1 11  ? 8.710   -4.896  8.861   1.00 18.43 ? 11  ASN A ND2  1 
ATOM   82   N  N    . GLY A 1 12  ? 8.575   -6.776  13.534  1.00 20.75 ? 12  GLY A N    1 
ATOM   83   C  CA   . GLY A 1 12  ? 7.225   -7.007  14.136  1.00 18.42 ? 12  GLY A CA   1 
ATOM   84   C  C    . GLY A 1 12  ? 7.173   -6.456  15.537  1.00 19.38 ? 12  GLY A C    1 
ATOM   85   O  O    . GLY A 1 12  ? 8.062   -5.718  16.007  1.00 19.67 ? 12  GLY A O    1 
ATOM   86   N  N    . PRO A 1 13  ? 6.106   -6.804  16.281  1.00 18.67 ? 13  PRO A N    1 
ATOM   87   C  CA   . PRO A 1 13  ? 5.904   -6.228  17.600  1.00 18.86 ? 13  PRO A CA   1 
ATOM   88   C  C    . PRO A 1 13  ? 7.044   -6.211  18.571  1.00 19.78 ? 13  PRO A C    1 
ATOM   89   O  O    . PRO A 1 13  ? 7.160   -5.232  19.313  1.00 18.14 ? 13  PRO A O    1 
ATOM   90   C  CB   . PRO A 1 13  ? 4.746   -7.074  18.165  1.00 19.83 ? 13  PRO A CB   1 
ATOM   91   C  CG   . PRO A 1 13  ? 3.937   -7.324  16.921  1.00 16.17 ? 13  PRO A CG   1 
ATOM   92   C  CD   . PRO A 1 13  ? 4.975   -7.643  15.870  1.00 20.16 ? 13  PRO A CD   1 
ATOM   93   N  N    . GLU A 1 14  ? 7.870   -7.273  18.588  1.00 19.35 ? 14  GLU A N    1 
ATOM   94   C  CA   . GLU A 1 14  ? 8.956   -7.373  19.546  1.00 19.87 ? 14  GLU A CA   1 
ATOM   95   C  C    . GLU A 1 14  ? 10.096  -6.344  19.269  1.00 18.83 ? 14  GLU A C    1 
ATOM   96   O  O    . GLU A 1 14  ? 10.875  -6.051  20.169  1.00 19.98 ? 14  GLU A O    1 
ATOM   97   C  CB   . GLU A 1 14  ? 9.486   -8.828  19.585  1.00 21.17 ? 14  GLU A CB   1 
ATOM   98   C  CG   . GLU A 1 14  ? 8.386   -9.882  20.019  1.00 21.46 ? 14  GLU A CG   1 
ATOM   99   C  CD   . GLU A 1 14  ? 7.510   -9.535  21.197  0.50 22.42 ? 14  GLU A CD   1 
ATOM   100  O  OE1  . GLU A 1 14  ? 8.042   -9.035  22.207  0.50 24.51 ? 14  GLU A OE1  1 
ATOM   101  O  OE2  . GLU A 1 14  ? 6.271   -9.818  21.123  0.50 19.82 ? 14  GLU A OE2  1 
ATOM   102  N  N    . HIS A 1 15  ? 10.117  -5.820  18.049  1.00 19.58 ? 15  HIS A N    1 
ATOM   103  C  CA   . HIS A 1 15  ? 11.020  -4.757  17.530  1.00 17.91 ? 15  HIS A CA   1 
ATOM   104  C  C    . HIS A 1 15  ? 10.568  -3.293  17.745  1.00 19.39 ? 15  HIS A C    1 
ATOM   105  O  O    . HIS A 1 15  ? 11.389  -2.352  17.711  1.00 17.34 ? 15  HIS A O    1 
ATOM   106  C  CB   . HIS A 1 15  ? 11.300  -4.984  16.041  1.00 20.25 ? 15  HIS A CB   1 
ATOM   107  C  CG   . HIS A 1 15  ? 12.092  -6.235  15.777  1.00 23.35 ? 15  HIS A CG   1 
ATOM   108  N  ND1  . HIS A 1 15  ? 13.450  -6.323  16.027  1.00 22.28 ? 15  HIS A ND1  1 
ATOM   109  C  CD2  . HIS A 1 15  ? 11.707  -7.471  15.364  1.00 23.39 ? 15  HIS A CD2  1 
ATOM   110  C  CE1  . HIS A 1 15  ? 13.869  -7.545  15.757  1.00 21.59 ? 15  HIS A CE1  1 
ATOM   111  N  NE2  . HIS A 1 15  ? 12.837  -8.269  15.362  1.00 20.99 ? 15  HIS A NE2  1 
ATOM   112  N  N    . TRP A 1 16  ? 9.281   -3.072  17.972  1.00 16.34 ? 16  TRP A N    1 
ATOM   113  C  CA   . TRP A 1 16  ? 8.733   -1.704  17.946  1.00 16.58 ? 16  TRP A CA   1 
ATOM   114  C  C    . TRP A 1 16  ? 9.313   -0.711  18.958  1.00 14.25 ? 16  TRP A C    1 
ATOM   115  O  O    . TRP A 1 16  ? 9.380   0.505   18.654  1.00 17.16 ? 16  TRP A O    1 
ATOM   116  C  CB   . TRP A 1 16  ? 7.164   -1.728  17.999  1.00 13.84 ? 16  TRP A CB   1 
ATOM   117  C  CG   . TRP A 1 16  ? 6.504   -2.400  16.857  1.00 14.90 ? 16  TRP A CG   1 
ATOM   118  C  CD1  . TRP A 1 16  ? 7.046   -2.804  15.636  1.00 13.58 ? 16  TRP A CD1  1 
ATOM   119  C  CD2  . TRP A 1 16  ? 5.085   -2.727  16.777  1.00 13.97 ? 16  TRP A CD2  1 
ATOM   120  N  NE1  . TRP A 1 16  ? 6.071   -3.423  14.861  1.00 14.78 ? 16  TRP A NE1  1 
ATOM   121  C  CE2  . TRP A 1 16  ? 4.863   -3.353  15.516  1.00 16.24 ? 16  TRP A CE2  1 
ATOM   122  C  CE3  . TRP A 1 16  ? 4.009   -2.548  17.657  1.00 15.12 ? 16  TRP A CE3  1 
ATOM   123  C  CZ2  . TRP A 1 16  ? 3.599   -3.810  15.111  1.00 15.80 ? 16  TRP A CZ2  1 
ATOM   124  C  CZ3  . TRP A 1 16  ? 2.736   -3.102  17.287  1.00 9.75  ? 16  TRP A CZ3  1 
ATOM   125  C  CH2  . TRP A 1 16  ? 2.548   -3.656  16.018  1.00 13.96 ? 16  TRP A CH2  1 
ATOM   126  N  N    . HIS A 1 17  ? 9.750   -1.194  20.099  1.00 14.64 ? 17  HIS A N    1 
ATOM   127  C  CA   . HIS A 1 17  ? 10.141  -0.329  21.179  1.00 17.55 ? 17  HIS A CA   1 
ATOM   128  C  C    . HIS A 1 17  ? 11.400  0.473   20.767  1.00 17.30 ? 17  HIS A C    1 
ATOM   129  O  O    . HIS A 1 17  ? 11.669  1.501   21.375  1.00 19.78 ? 17  HIS A O    1 
ATOM   130  C  CB   . HIS A 1 17  ? 10.387  -1.089  22.450  1.00 16.29 ? 17  HIS A CB   1 
ATOM   131  C  CG   . HIS A 1 17  ? 11.599  -1.986  22.367  1.00 19.49 ? 17  HIS A CG   1 
ATOM   132  N  ND1  . HIS A 1 17  ? 12.846  -1.597  22.830  1.00 25.01 ? 17  HIS A ND1  1 
ATOM   133  C  CD2  . HIS A 1 17  ? 11.762  -3.221  21.840  1.00 21.22 ? 17  HIS A CD2  1 
ATOM   134  C  CE1  . HIS A 1 17  ? 13.729  -2.544  22.565  1.00 24.88 ? 17  HIS A CE1  1 
ATOM   135  N  NE2  . HIS A 1 17  ? 13.106  -3.546  21.972  1.00 23.17 ? 17  HIS A NE2  1 
ATOM   136  N  N    . LYS A 1 18  ? 12.156  -0.012  19.796  1.00 18.59 ? 18  LYS A N    1 
ATOM   137  C  CA   . LYS A 1 18  ? 13.421  0.691   19.418  1.00 20.29 ? 18  LYS A CA   1 
ATOM   138  C  C    . LYS A 1 18  ? 13.067  2.048   18.757  1.00 21.19 ? 18  LYS A C    1 
ATOM   139  O  O    . LYS A 1 18  ? 13.601  3.097   19.171  1.00 23.44 ? 18  LYS A O    1 
ATOM   140  C  CB   . LYS A 1 18  ? 14.233  -0.184  18.474  1.00 19.86 ? 18  LYS A CB   1 
ATOM   141  C  CG   . LYS A 1 18  ? 15.004  -1.354  19.153  1.00 20.16 ? 18  LYS A CG   1 
ATOM   142  C  CD   . LYS A 1 18  ? 15.616  -2.235  18.076  1.00 19.73 ? 18  LYS A CD   1 
ATOM   143  C  CE   . LYS A 1 18  ? 14.694  -3.363  17.647  1.00 25.32 ? 18  LYS A CE   1 
ATOM   144  N  NZ   . LYS A 1 18  ? 15.300  -4.130  16.485  1.00 20.76 ? 18  LYS A NZ   1 
ATOM   145  N  N    . ASP A 1 19  ? 12.114  2.038   17.813  1.00 21.20 ? 19  ASP A N    1 
ATOM   146  C  CA   . ASP A 1 19  ? 11.608  3.298   17.218  1.00 22.03 ? 19  ASP A CA   1 
ATOM   147  C  C    . ASP A 1 19  ? 10.615  4.061   18.100  1.00 23.42 ? 19  ASP A C    1 
ATOM   148  O  O    . ASP A 1 19  ? 10.490  5.299   17.961  1.00 22.07 ? 19  ASP A O    1 
ATOM   149  C  CB   . ASP A 1 19  ? 11.017  3.090   15.818  1.00 22.81 ? 19  ASP A CB   1 
ATOM   150  C  CG   . ASP A 1 19  ? 12.035  3.226   14.707  1.00 24.22 ? 19  ASP A CG   1 
ATOM   151  O  OD1  . ASP A 1 19  ? 13.131  3.739   14.902  1.00 30.09 ? 19  ASP A OD1  1 
ATOM   152  O  OD2  . ASP A 1 19  ? 11.721  2.808   13.596  1.00 32.22 ? 19  ASP A OD2  1 
ATOM   153  N  N    . PHE A 1 20  ? 9.917   3.333   19.000  1.00 21.37 ? 20  PHE A N    1 
ATOM   154  C  CA   . PHE A 1 20  ? 8.763   3.859   19.761  1.00 20.82 ? 20  PHE A CA   1 
ATOM   155  C  C    . PHE A 1 20  ? 8.859   3.336   21.168  1.00 20.68 ? 20  PHE A C    1 
ATOM   156  O  O    . PHE A 1 20  ? 8.245   2.336   21.518  1.00 18.88 ? 20  PHE A O    1 
ATOM   157  C  CB   . PHE A 1 20  ? 7.408   3.467   19.045  1.00 19.95 ? 20  PHE A CB   1 
ATOM   158  C  CG   . PHE A 1 20  ? 7.343   3.881   17.591  1.00 20.51 ? 20  PHE A CG   1 
ATOM   159  C  CD1  . PHE A 1 20  ? 6.994   5.192   17.233  1.00 18.08 ? 20  PHE A CD1  1 
ATOM   160  C  CD2  . PHE A 1 20  ? 7.641   2.955   16.556  1.00 21.70 ? 20  PHE A CD2  1 
ATOM   161  C  CE1  . PHE A 1 20  ? 6.931   5.548   15.891  1.00 20.74 ? 20  PHE A CE1  1 
ATOM   162  C  CE2  . PHE A 1 20  ? 7.601   3.318   15.201  1.00 19.89 ? 20  PHE A CE2  1 
ATOM   163  C  CZ   . PHE A 1 20  ? 7.246   4.628   14.885  1.00 23.77 ? 20  PHE A CZ   1 
ATOM   164  N  N    . PRO A 1 21  ? 9.725   3.953   22.006  1.00 20.41 ? 21  PRO A N    1 
ATOM   165  C  CA   . PRO A 1 21  ? 9.967   3.481   23.350  1.00 20.46 ? 21  PRO A CA   1 
ATOM   166  C  C    . PRO A 1 21  ? 8.745   3.389   24.274  1.00 20.17 ? 21  PRO A C    1 
ATOM   167  O  O    . PRO A 1 21  ? 8.747   2.599   25.188  1.00 18.17 ? 21  PRO A O    1 
ATOM   168  C  CB   . PRO A 1 21  ? 11.007  4.484   23.893  1.00 22.14 ? 21  PRO A CB   1 
ATOM   169  C  CG   . PRO A 1 21  ? 11.610  5.042   22.696  1.00 22.58 ? 21  PRO A CG   1 
ATOM   170  C  CD   . PRO A 1 21  ? 10.591  5.103   21.654  1.00 21.33 ? 21  PRO A CD   1 
ATOM   171  N  N    . ILE A 1 22  ? 7.709   4.206   24.024  1.00 19.12 ? 22  ILE A N    1 
ATOM   172  C  CA   . ILE A 1 22  ? 6.423   4.035   24.733  1.00 18.27 ? 22  ILE A CA   1 
ATOM   173  C  C    . ILE A 1 22  ? 5.807   2.602   24.592  1.00 17.77 ? 22  ILE A C    1 
ATOM   174  O  O    . ILE A 1 22  ? 4.922   2.215   25.378  1.00 15.73 ? 22  ILE A O    1 
ATOM   175  C  CB   . ILE A 1 22  ? 5.395   5.161   24.300  1.00 15.98 ? 22  ILE A CB   1 
ATOM   176  C  CG1  . ILE A 1 22  ? 4.241   5.335   25.288  1.00 15.41 ? 22  ILE A CG1  1 
ATOM   177  C  CG2  . ILE A 1 22  ? 4.824   4.829   22.954  1.00 18.38 ? 22  ILE A CG2  1 
ATOM   178  C  CD1  . ILE A 1 22  ? 4.562   5.846   26.618  1.00 17.41 ? 22  ILE A CD1  1 
ATOM   179  N  N    . ALA A 1 23  ? 6.324   1.805   23.640  1.00 18.17 ? 23  ALA A N    1 
ATOM   180  C  CA   . ALA A 1 23  ? 5.995   0.302   23.573  1.00 18.07 ? 23  ALA A CA   1 
ATOM   181  C  C    . ALA A 1 23  ? 6.059   -0.434  24.926  1.00 20.08 ? 23  ALA A C    1 
ATOM   182  O  O    . ALA A 1 23  ? 5.304   -1.440  25.223  1.00 19.56 ? 23  ALA A O    1 
ATOM   183  C  CB   . ALA A 1 23  ? 6.920   -0.398  22.547  1.00 17.48 ? 23  ALA A CB   1 
ATOM   184  N  N    . LYS A 1 24  ? 6.958   0.043   25.789  1.00 20.73 ? 24  LYS A N    1 
ATOM   185  C  CA   . LYS A 1 24  ? 7.132   -0.578  27.078  1.00 22.26 ? 24  LYS A CA   1 
ATOM   186  C  C    . LYS A 1 24  ? 6.510   0.273   28.187  1.00 22.65 ? 24  LYS A C    1 
ATOM   187  O  O    . LYS A 1 24  ? 6.898   0.101   29.353  1.00 21.39 ? 24  LYS A O    1 
ATOM   188  C  CB   . LYS A 1 24  ? 8.629   -0.774  27.393  1.00 23.40 ? 24  LYS A CB   1 
ATOM   189  C  CG   . LYS A 1 24  ? 9.283   -1.799  26.532  1.00 23.92 ? 24  LYS A CG   1 
ATOM   190  C  CD   . LYS A 1 24  ? 10.737  -2.066  27.004  1.00 23.96 ? 24  LYS A CD   1 
ATOM   191  C  CE   . LYS A 1 24  ? 11.390  -3.096  26.049  1.00 29.52 ? 24  LYS A CE   1 
ATOM   192  N  NZ   . LYS A 1 24  ? 10.836  -4.509  26.171  1.00 26.30 ? 24  LYS A NZ   1 
ATOM   193  N  N    . GLY A 1 25  ? 5.527   1.137   27.841  1.00 22.68 ? 25  GLY A N    1 
ATOM   194  C  CA   . GLY A 1 25  ? 4.964   2.076   28.833  1.00 21.79 ? 25  GLY A CA   1 
ATOM   195  C  C    . GLY A 1 25  ? 3.924   1.507   29.774  1.00 21.43 ? 25  GLY A C    1 
ATOM   196  O  O    . GLY A 1 25  ? 3.712   0.283   29.842  1.00 24.21 ? 25  GLY A O    1 
ATOM   197  N  N    . GLU A 1 26  ? 3.256   2.384   30.518  1.00 20.84 ? 26  GLU A N    1 
ATOM   198  C  CA   . GLU A 1 26  ? 2.431   1.952   31.613  1.00 20.72 ? 26  GLU A CA   1 
ATOM   199  C  C    . GLU A 1 26  ? 1.000   1.708   31.185  1.00 17.51 ? 26  GLU A C    1 
ATOM   200  O  O    . GLU A 1 26  ? 0.217   1.196   31.960  1.00 17.24 ? 26  GLU A O    1 
ATOM   201  C  CB   . GLU A 1 26  ? 2.393   3.022   32.750  1.00 23.03 ? 26  GLU A CB   1 
ATOM   202  C  CG   . GLU A 1 26  ? 3.782   3.269   33.440  1.00 28.61 ? 26  GLU A CG   1 
ATOM   203  C  CD   . GLU A 1 26  ? 4.460   1.959   33.907  1.00 33.86 ? 26  GLU A CD   1 
ATOM   204  O  OE1  . GLU A 1 26  ? 3.876   1.229   34.770  1.00 36.38 ? 26  GLU A OE1  1 
ATOM   205  O  OE2  . GLU A 1 26  ? 5.569   1.673   33.384  1.00 35.90 ? 26  GLU A OE2  1 
ATOM   206  N  N    . ARG A 1 27  ? 0.635   2.123   29.970  1.00 16.08 ? 27  ARG A N    1 
ATOM   207  C  CA   . ARG A 1 27  ? -0.807  1.924   29.574  1.00 14.88 ? 27  ARG A CA   1 
ATOM   208  C  C    . ARG A 1 27  ? -0.921  1.379   28.111  1.00 13.13 ? 27  ARG A C    1 
ATOM   209  O  O    . ARG A 1 27  ? -1.588  1.996   27.230  1.00 12.47 ? 27  ARG A O    1 
ATOM   210  C  CB   . ARG A 1 27  ? -1.645  3.193   29.855  1.00 15.78 ? 27  ARG A CB   1 
ATOM   211  C  CG   . ARG A 1 27  ? -1.258  4.496   29.034  1.00 18.39 ? 27  ARG A CG   1 
ATOM   212  C  CD   . ARG A 1 27  ? -2.236  5.821   29.187  1.00 20.96 ? 27  ARG A CD   1 
ATOM   213  N  NE   . ARG A 1 27  ? -3.537  5.613   28.519  1.00 21.46 ? 27  ARG A NE   1 
ATOM   214  C  CZ   . ARG A 1 27  ? -4.507  6.516   28.334  1.00 21.40 ? 27  ARG A CZ   1 
ATOM   215  N  NH1  . ARG A 1 27  ? -4.413  7.828   28.649  1.00 12.86 ? 27  ARG A NH1  1 
ATOM   216  N  NH2  . ARG A 1 27  ? -5.537  6.107   27.708  1.00 18.47 ? 27  ARG A NH2  1 
ATOM   217  N  N    . GLN A 1 28  ? -0.242  0.262   27.830  1.00 12.33 ? 28  GLN A N    1 
ATOM   218  C  CA   . GLN A 1 28  ? -0.206  -0.277  26.428  1.00 12.18 ? 28  GLN A CA   1 
ATOM   219  C  C    . GLN A 1 28  ? -1.343  -1.255  26.141  1.00 11.22 ? 28  GLN A C    1 
ATOM   220  O  O    . GLN A 1 28  ? -1.828  -1.975  27.050  1.00 11.07 ? 28  GLN A O    1 
ATOM   221  C  CB   . GLN A 1 28  ? 1.148   -0.995  26.176  1.00 14.72 ? 28  GLN A CB   1 
ATOM   222  C  CG   . GLN A 1 28  ? 2.310   0.077   26.028  1.00 14.23 ? 28  GLN A CG   1 
ATOM   223  C  CD   . GLN A 1 28  ? 2.179   0.894   24.718  1.00 14.44 ? 28  GLN A CD   1 
ATOM   224  O  OE1  . GLN A 1 28  ? 2.385   0.383   23.634  1.00 12.76 ? 28  GLN A OE1  1 
ATOM   225  N  NE2  . GLN A 1 28  ? 1.872   2.194   24.836  1.00 16.24 ? 28  GLN A NE2  1 
ATOM   226  N  N    . SER A 1 29  ? -1.691  -1.320  24.842  1.00 10.18 ? 29  SER A N    1 
ATOM   227  C  CA   . SER A 1 29  ? -2.766  -2.194  24.341  1.00 10.06 ? 29  SER A CA   1 
ATOM   228  C  C    . SER A 1 29  ? -2.179  -3.048  23.203  1.00 9.57  ? 29  SER A C    1 
ATOM   229  O  O    . SER A 1 29  ? -1.272  -2.566  22.533  1.00 11.03 ? 29  SER A O    1 
ATOM   230  C  CB   . SER A 1 29  ? -3.879  -1.314  23.785  1.00 9.48  ? 29  SER A CB   1 
ATOM   231  O  OG   . SER A 1 29  ? -4.486  -0.573  24.875  1.00 10.10 ? 29  SER A OG   1 
ATOM   232  N  N    . PRO A 1 30  ? -2.776  -4.246  22.938  1.00 10.23 ? 30  PRO A N    1 
ATOM   233  C  CA   . PRO A 1 30  ? -3.991  -4.750  23.669  1.00 11.08 ? 30  PRO A CA   1 
ATOM   234  C  C    . PRO A 1 30  ? -3.633  -5.437  25.006  1.00 11.68 ? 30  PRO A C    1 
ATOM   235  O  O    . PRO A 1 30  ? -2.443  -5.457  25.360  1.00 10.78 ? 30  PRO A O    1 
ATOM   236  C  CB   . PRO A 1 30  ? -4.545  -5.810  22.697  1.00 10.16 ? 30  PRO A CB   1 
ATOM   237  C  CG   . PRO A 1 30  ? -3.209  -6.431  22.084  1.00 9.60  ? 30  PRO A CG   1 
ATOM   238  C  CD   . PRO A 1 30  ? -2.337  -5.172  21.866  1.00 10.69 ? 30  PRO A CD   1 
ATOM   239  N  N    . VAL A 1 31  ? -4.630  -6.010  25.697  1.00 11.98 ? 31  VAL A N    1 
ATOM   240  C  CA   . VAL A 1 31  ? -4.457  -6.739  26.939  1.00 10.30 ? 31  VAL A CA   1 
ATOM   241  C  C    . VAL A 1 31  ? -5.379  -7.952  26.908  1.00 11.54 ? 31  VAL A C    1 
ATOM   242  O  O    . VAL A 1 31  ? -6.374  -8.048  26.114  1.00 8.78  ? 31  VAL A O    1 
ATOM   243  C  CB   . VAL A 1 31  ? -4.765  -5.884  28.234  1.00 11.31 ? 31  VAL A CB   1 
ATOM   244  C  CG1  . VAL A 1 31  ? -3.798  -4.706  28.287  1.00 9.50  ? 31  VAL A CG1  1 
ATOM   245  C  CG2  . VAL A 1 31  ? -6.313  -5.451  28.285  1.00 8.78  ? 31  VAL A CG2  1 
ATOM   246  N  N    . ASP A 1 32  ? -5.061  -8.919  27.784  1.00 12.51 ? 32  ASP A N    1 
ATOM   247  C  CA   . ASP A 1 32  ? -5.949  -10.022 27.964  1.00 13.39 ? 32  ASP A CA   1 
ATOM   248  C  C    . ASP A 1 32  ? -7.023  -9.528  28.921  1.00 14.31 ? 32  ASP A C    1 
ATOM   249  O  O    . ASP A 1 32  ? -6.679  -8.846  29.884  1.00 15.40 ? 32  ASP A O    1 
ATOM   250  C  CB   . ASP A 1 32  ? -5.216  -11.224 28.522  1.00 14.53 ? 32  ASP A CB   1 
ATOM   251  C  CG   . ASP A 1 32  ? -6.172  -12.388 28.846  1.00 17.88 ? 32  ASP A CG   1 
ATOM   252  O  OD1  . ASP A 1 32  ? -6.863  -12.870 27.904  1.00 13.51 ? 32  ASP A OD1  1 
ATOM   253  O  OD2  . ASP A 1 32  ? -6.229  -12.801 30.041  1.00 17.51 ? 32  ASP A OD2  1 
ATOM   254  N  N    . ILE A 1 33  ? -8.299  -9.855  28.661  1.00 14.73 ? 33  ILE A N    1 
ATOM   255  C  CA   . ILE A 1 33  ? -9.403  -9.404  29.511  1.00 15.85 ? 33  ILE A CA   1 
ATOM   256  C  C    . ILE A 1 33  ? -9.752  -10.610 30.328  1.00 16.46 ? 33  ILE A C    1 
ATOM   257  O  O    . ILE A 1 33  ? -10.291 -11.624 29.827  1.00 18.38 ? 33  ILE A O    1 
ATOM   258  C  CB   . ILE A 1 33  ? -10.614 -8.930  28.694  1.00 16.69 ? 33  ILE A CB   1 
ATOM   259  C  CG1  . ILE A 1 33  ? -10.193 -7.679  27.908  1.00 13.16 ? 33  ILE A CG1  1 
ATOM   260  C  CG2  . ILE A 1 33  ? -11.885 -8.628  29.635  1.00 14.77 ? 33  ILE A CG2  1 
ATOM   261  C  CD1  . ILE A 1 33  ? -11.120 -7.420  26.746  1.00 12.81 ? 33  ILE A CD1  1 
ATOM   262  N  N    . ASP A 1 34  ? -9.316  -10.545 31.562  1.00 17.85 ? 34  ASP A N    1 
ATOM   263  C  CA   . ASP A 1 34  ? -9.671  -11.625 32.490  1.00 19.27 ? 34  ASP A CA   1 
ATOM   264  C  C    . ASP A 1 34  ? -11.065 -11.371 33.102  1.00 20.50 ? 34  ASP A C    1 
ATOM   265  O  O    . ASP A 1 34  ? -11.241 -10.482 33.972  1.00 22.65 ? 34  ASP A O    1 
ATOM   266  C  CB   . ASP A 1 34  ? -8.616  -11.868 33.532  1.00 20.90 ? 34  ASP A CB   1 
ATOM   267  C  CG   . ASP A 1 34  ? -8.945  -13.129 34.341  1.00 25.17 ? 34  ASP A CG   1 
ATOM   268  O  OD1  . ASP A 1 34  ? -9.725  -12.939 35.261  1.00 22.83 ? 34  ASP A OD1  1 
ATOM   269  O  OD2  . ASP A 1 34  ? -8.607  -14.297 33.902  1.00 29.61 ? 34  ASP A OD2  1 
ATOM   270  N  N    . THR A 1 35  ? -12.043 -12.109 32.590  1.00 20.73 ? 35  THR A N    1 
ATOM   271  C  CA   . THR A 1 35  ? -13.466 -11.806 32.780  1.00 21.76 ? 35  THR A CA   1 
ATOM   272  C  C    . THR A 1 35  ? -13.867 -11.905 34.288  1.00 24.12 ? 35  THR A C    1 
ATOM   273  O  O    . THR A 1 35  ? -14.883 -11.355 34.726  1.00 23.20 ? 35  THR A O    1 
ATOM   274  C  CB   . THR A 1 35  ? -14.325 -12.758 31.992  1.00 22.63 ? 35  THR A CB   1 
ATOM   275  O  OG1  . THR A 1 35  ? -14.083 -14.115 32.436  1.00 23.63 ? 35  THR A OG1  1 
ATOM   276  C  CG2  . THR A 1 35  ? -14.063 -12.612 30.436  1.00 20.68 ? 35  THR A CG2  1 
ATOM   277  N  N    . HIS A 1 36  ? -13.039 -12.591 35.072  1.00 25.93 ? 36  HIS A N    1 
ATOM   278  C  CA   A HIS A 1 36  ? -13.359 -12.751 36.502  0.50 27.25 ? 36  HIS A CA   1 
ATOM   279  C  CA   B HIS A 1 36  ? -13.285 -12.832 36.504  0.50 26.33 ? 36  HIS A CA   1 
ATOM   280  C  C    . HIS A 1 36  ? -12.596 -11.790 37.420  1.00 27.33 ? 36  HIS A C    1 
ATOM   281  O  O    . HIS A 1 36  ? -12.837 -11.719 38.639  1.00 29.99 ? 36  HIS A O    1 
ATOM   282  C  CB   A HIS A 1 36  ? -13.197 -14.226 36.921  0.50 27.79 ? 36  HIS A CB   1 
ATOM   283  C  CB   B HIS A 1 36  ? -12.852 -14.287 36.844  0.50 25.90 ? 36  HIS A CB   1 
ATOM   284  C  CG   A HIS A 1 36  ? -14.293 -15.119 36.416  0.50 28.32 ? 36  HIS A CG   1 
ATOM   285  C  CG   B HIS A 1 36  ? -13.502 -15.339 35.981  0.50 22.41 ? 36  HIS A CG   1 
ATOM   286  N  ND1  A HIS A 1 36  ? -15.591 -15.032 36.872  0.50 30.24 ? 36  HIS A ND1  1 
ATOM   287  N  ND1  B HIS A 1 36  ? -12.782 -16.195 35.177  0.50 22.60 ? 36  HIS A ND1  1 
ATOM   288  C  CD2  A HIS A 1 36  ? -14.283 -16.112 35.494  0.50 28.17 ? 36  HIS A CD2  1 
ATOM   289  C  CD2  B HIS A 1 36  ? -14.805 -15.663 35.791  0.50 19.68 ? 36  HIS A CD2  1 
ATOM   290  C  CE1  A HIS A 1 36  ? -16.333 -15.939 36.260  0.50 28.44 ? 36  HIS A CE1  1 
ATOM   291  C  CE1  B HIS A 1 36  ? -13.603 -17.002 34.533  0.50 18.92 ? 36  HIS A CE1  1 
ATOM   292  N  NE2  A HIS A 1 36  ? -15.566 -16.604 35.414  0.50 30.25 ? 36  HIS A NE2  1 
ATOM   293  N  NE2  B HIS A 1 36  ? -14.838 -16.701 34.882  0.50 19.60 ? 36  HIS A NE2  1 
ATOM   294  N  N    . THR A 1 37  ? -11.703 -11.003 36.866  1.00 27.55 ? 37  THR A N    1 
ATOM   295  C  CA   . THR A 1 37  ? -10.981 -10.022 37.617  1.00 27.15 ? 37  THR A CA   1 
ATOM   296  C  C    . THR A 1 37  ? -11.515 -8.584  37.261  1.00 24.80 ? 37  THR A C    1 
ATOM   297  O  O    . THR A 1 37  ? -11.236 -7.603  37.966  1.00 23.49 ? 37  THR A O    1 
ATOM   298  C  CB   . THR A 1 37  ? -9.504  -10.261 37.387  1.00 28.89 ? 37  THR A CB   1 
ATOM   299  O  OG1  . THR A 1 37  ? -9.052  -11.155 38.427  1.00 34.08 ? 37  THR A OG1  1 
ATOM   300  C  CG2  . THR A 1 37  ? -8.707  -8.993  37.498  1.00 30.74 ? 37  THR A CG2  1 
ATOM   301  N  N    . ALA A 1 38  ? -12.298 -8.523  36.176  1.00 22.48 ? 38  ALA A N    1 
ATOM   302  C  CA   . ALA A 1 38  ? -12.983 -7.278  35.703  1.00 21.60 ? 38  ALA A CA   1 
ATOM   303  C  C    . ALA A 1 38  ? -14.056 -6.857  36.714  1.00 21.62 ? 38  ALA A C    1 
ATOM   304  O  O    . ALA A 1 38  ? -14.779 -7.690  37.206  1.00 21.51 ? 38  ALA A O    1 
ATOM   305  C  CB   . ALA A 1 38  ? -13.627 -7.502  34.347  1.00 18.51 ? 38  ALA A CB   1 
ATOM   306  N  N    . LYS A 1 39  ? -14.116 -5.578  37.041  1.00 22.12 ? 39  LYS A N    1 
ATOM   307  C  CA   . LYS A 1 39  ? -15.073 -5.118  38.028  1.00 23.12 ? 39  LYS A CA   1 
ATOM   308  C  C    . LYS A 1 39  ? -16.352 -4.596  37.407  1.00 24.57 ? 39  LYS A C    1 
ATOM   309  O  O    . LYS A 1 39  ? -16.342 -3.616  36.624  1.00 23.26 ? 39  LYS A O    1 
ATOM   310  C  CB   . LYS A 1 39  ? -14.481 -4.084  38.962  1.00 24.45 ? 39  LYS A CB   1 
ATOM   311  C  CG   . LYS A 1 39  ? -15.118 -4.267  40.410  1.00 26.60 ? 39  LYS A CG   1 
ATOM   312  C  CD   . LYS A 1 39  ? -15.369 -3.037  41.145  1.00 29.72 ? 39  LYS A CD   1 
ATOM   313  C  CE   . LYS A 1 39  ? -16.720 -3.129  41.874  1.00 27.40 ? 39  LYS A CE   1 
ATOM   314  N  NZ   . LYS A 1 39  ? -16.547 -3.375  43.342  1.00 22.52 ? 39  LYS A NZ   1 
ATOM   315  N  N    . TYR A 1 40  ? -17.457 -5.219  37.804  1.00 25.41 ? 40  TYR A N    1 
ATOM   316  C  CA   . TYR A 1 40  ? -18.766 -4.738  37.418  1.00 28.33 ? 40  TYR A CA   1 
ATOM   317  C  C    . TYR A 1 40  ? -19.024 -3.347  38.004  1.00 29.03 ? 40  TYR A C    1 
ATOM   318  O  O    . TYR A 1 40  ? -18.926 -3.139  39.228  1.00 28.34 ? 40  TYR A O    1 
ATOM   319  C  CB   . TYR A 1 40  ? -19.892 -5.762  37.712  1.00 29.86 ? 40  TYR A CB   1 
ATOM   320  C  CG   . TYR A 1 40  ? -21.269 -5.122  37.628  1.00 32.34 ? 40  TYR A CG   1 
ATOM   321  C  CD1  . TYR A 1 40  ? -21.793 -4.659  36.396  1.00 32.20 ? 40  TYR A CD1  1 
ATOM   322  C  CD2  . TYR A 1 40  ? -22.038 -4.934  38.803  1.00 35.53 ? 40  TYR A CD2  1 
ATOM   323  C  CE1  . TYR A 1 40  ? -23.040 -4.022  36.331  1.00 33.64 ? 40  TYR A CE1  1 
ATOM   324  C  CE2  . TYR A 1 40  ? -23.306 -4.322  38.746  1.00 37.55 ? 40  TYR A CE2  1 
ATOM   325  C  CZ   . TYR A 1 40  ? -23.792 -3.859  37.529  1.00 35.41 ? 40  TYR A CZ   1 
ATOM   326  O  OH   . TYR A 1 40  ? -25.033 -3.261  37.541  1.00 36.46 ? 40  TYR A OH   1 
ATOM   327  N  N    . ASP A 1 41  ? -19.355 -2.385  37.127  1.00 29.29 ? 41  ASP A N    1 
ATOM   328  C  CA   . ASP A 1 41  ? -19.578 -1.021  37.590  1.00 31.67 ? 41  ASP A CA   1 
ATOM   329  C  C    . ASP A 1 41  ? -21.002 -0.519  37.287  1.00 32.04 ? 41  ASP A C    1 
ATOM   330  O  O    . ASP A 1 41  ? -21.230 0.020   36.198  1.00 31.43 ? 41  ASP A O    1 
ATOM   331  C  CB   . ASP A 1 41  ? -18.505 -0.057  37.057  1.00 30.91 ? 41  ASP A CB   1 
ATOM   332  C  CG   . ASP A 1 41  ? -18.629 1.363   37.652  1.00 34.20 ? 41  ASP A CG   1 
ATOM   333  O  OD1  . ASP A 1 41  ? -19.537 1.562   38.525  1.00 34.75 ? 41  ASP A OD1  1 
ATOM   334  O  OD2  . ASP A 1 41  ? -17.805 2.260   37.262  1.00 32.98 ? 41  ASP A OD2  1 
ATOM   335  N  N    . PRO A 1 42  ? -21.988 -0.734  38.223  1.00 33.24 ? 42  PRO A N    1 
ATOM   336  C  CA   . PRO A 1 42  ? -23.368 -0.209  38.028  1.00 34.04 ? 42  PRO A CA   1 
ATOM   337  C  C    . PRO A 1 42  ? -23.490 1.306   37.739  1.00 35.03 ? 42  PRO A C    1 
ATOM   338  O  O    . PRO A 1 42  ? -24.569 1.758   37.309  1.00 36.45 ? 42  PRO A O    1 
ATOM   339  C  CB   . PRO A 1 42  ? -24.070 -0.524  39.370  1.00 34.03 ? 42  PRO A CB   1 
ATOM   340  C  CG   . PRO A 1 42  ? -22.927 -0.808  40.368  1.00 34.07 ? 42  PRO A CG   1 
ATOM   341  C  CD   . PRO A 1 42  ? -21.919 -1.518  39.479  1.00 33.69 ? 42  PRO A CD   1 
ATOM   342  N  N    . SER A 1 43  ? -22.427 2.086   37.966  1.00 35.48 ? 43  SER A N    1 
ATOM   343  C  CA   . SER A 1 43  ? -22.476 3.511   37.642  1.00 36.17 ? 43  SER A CA   1 
ATOM   344  C  C    . SER A 1 43  ? -22.152 3.879   36.149  1.00 36.86 ? 43  SER A C    1 
ATOM   345  O  O    . SER A 1 43  ? -22.335 5.038   35.732  1.00 37.58 ? 43  SER A O    1 
ATOM   346  C  CB   . SER A 1 43  ? -21.550 4.268   38.573  1.00 36.39 ? 43  SER A CB   1 
ATOM   347  O  OG   . SER A 1 43  ? -20.281 4.458   37.972  1.00 38.30 ? 43  SER A OG   1 
ATOM   348  N  N    . LEU A 1 44  ? -21.625 2.917   35.368  1.00 36.42 ? 44  LEU A N    1 
ATOM   349  C  CA   . LEU A 1 44  ? -21.298 3.156   33.955  1.00 35.45 ? 44  LEU A CA   1 
ATOM   350  C  C    . LEU A 1 44  ? -22.598 3.279   33.133  1.00 35.46 ? 44  LEU A C    1 
ATOM   351  O  O    . LEU A 1 44  ? -23.544 2.499   33.327  1.00 35.09 ? 44  LEU A O    1 
ATOM   352  C  CB   . LEU A 1 44  ? -20.473 2.001   33.387  1.00 35.12 ? 44  LEU A CB   1 
ATOM   353  C  CG   . LEU A 1 44  ? -19.006 1.849   33.744  1.00 33.66 ? 44  LEU A CG   1 
ATOM   354  C  CD1  . LEU A 1 44  ? -18.603 0.409   33.432  1.00 31.81 ? 44  LEU A CD1  1 
ATOM   355  C  CD2  . LEU A 1 44  ? -18.234 2.765   32.891  1.00 30.46 ? 44  LEU A CD2  1 
ATOM   356  N  N    . LYS A 1 45  ? -22.624 4.233   32.199  1.00 34.90 ? 45  LYS A N    1 
ATOM   357  C  CA   . LYS A 1 45  ? -23.818 4.494   31.382  1.00 34.14 ? 45  LYS A CA   1 
ATOM   358  C  C    . LYS A 1 45  ? -23.903 3.556   30.183  1.00 33.77 ? 45  LYS A C    1 
ATOM   359  O  O    . LYS A 1 45  ? -22.890 2.916   29.809  1.00 34.29 ? 45  LYS A O    1 
ATOM   360  C  CB   . LYS A 1 45  ? -23.819 5.934   30.942  1.00 34.72 ? 45  LYS A CB   1 
ATOM   361  C  CG   . LYS A 1 45  ? -23.362 6.902   32.053  1.00 34.69 ? 45  LYS A CG   1 
ATOM   362  C  CD   . LYS A 1 45  ? -23.996 8.273   31.885  1.00 38.86 ? 45  LYS A CD   1 
ATOM   363  C  CE   . LYS A 1 45  ? -23.502 9.241   32.948  0.01 37.77 ? 45  LYS A CE   1 
ATOM   364  N  NZ   . LYS A 1 45  ? -24.070 10.605  32.764  0.01 38.05 ? 45  LYS A NZ   1 
ATOM   365  N  N    . PRO A 1 46  ? -25.111 3.425   29.581  1.00 32.26 ? 46  PRO A N    1 
ATOM   366  C  CA   . PRO A 1 46  ? -25.096 2.582   28.380  1.00 31.46 ? 46  PRO A CA   1 
ATOM   367  C  C    . PRO A 1 46  ? -24.226 3.327   27.371  1.00 29.34 ? 46  PRO A C    1 
ATOM   368  O  O    . PRO A 1 46  ? -24.074 4.549   27.452  1.00 29.76 ? 46  PRO A O    1 
ATOM   369  C  CB   . PRO A 1 46  ? -26.577 2.563   27.937  1.00 31.88 ? 46  PRO A CB   1 
ATOM   370  C  CG   . PRO A 1 46  ? -27.343 2.918   29.217  1.00 32.28 ? 46  PRO A CG   1 
ATOM   371  C  CD   . PRO A 1 46  ? -26.459 3.955   29.862  1.00 31.85 ? 46  PRO A CD   1 
ATOM   372  N  N    . LEU A 1 47  ? -23.618 2.575   26.476  1.00 28.63 ? 47  LEU A N    1 
ATOM   373  C  CA   . LEU A 1 47  ? -22.849 3.123   25.426  1.00 26.41 ? 47  LEU A CA   1 
ATOM   374  C  C    . LEU A 1 47  ? -23.869 3.757   24.515  1.00 26.34 ? 47  LEU A C    1 
ATOM   375  O  O    . LEU A 1 47  ? -24.938 3.170   24.299  1.00 25.03 ? 47  LEU A O    1 
ATOM   376  C  CB   . LEU A 1 47  ? -22.237 1.981   24.652  1.00 27.03 ? 47  LEU A CB   1 
ATOM   377  C  CG   . LEU A 1 47  ? -20.755 1.930   24.468  1.00 29.68 ? 47  LEU A CG   1 
ATOM   378  C  CD1  . LEU A 1 47  ? -20.468 1.499   23.044  1.00 31.46 ? 47  LEU A CD1  1 
ATOM   379  C  CD2  . LEU A 1 47  ? -20.136 3.332   24.815  1.00 30.66 ? 47  LEU A CD2  1 
ATOM   380  N  N    . SER A 1 48  ? -23.549 4.923   23.965  1.00 22.49 ? 48  SER A N    1 
ATOM   381  C  CA   . SER A 1 48  ? -24.369 5.494   22.946  1.00 21.95 ? 48  SER A CA   1 
ATOM   382  C  C    . SER A 1 48  ? -23.668 5.503   21.574  1.00 21.78 ? 48  SER A C    1 
ATOM   383  O  O    . SER A 1 48  ? -22.757 6.303   21.353  1.00 19.03 ? 48  SER A O    1 
ATOM   384  C  CB   . SER A 1 48  ? -24.816 6.929   23.336  1.00 20.63 ? 48  SER A CB   1 
ATOM   385  O  OG   . SER A 1 48  ? -25.407 7.543   22.199  1.00 21.00 ? 48  SER A OG   1 
ATOM   386  N  N    . VAL A 1 49  ? -24.173 4.696   20.656  1.00 20.43 ? 49  VAL A N    1 
ATOM   387  C  CA   . VAL A 1 49  ? -23.626 4.619   19.299  1.00 22.29 ? 49  VAL A CA   1 
ATOM   388  C  C    . VAL A 1 49  ? -24.611 5.188   18.308  1.00 23.21 ? 49  VAL A C    1 
ATOM   389  O  O    . VAL A 1 49  ? -25.620 4.576   18.014  1.00 25.97 ? 49  VAL A O    1 
ATOM   390  C  CB   . VAL A 1 49  ? -23.310 3.168   18.883  1.00 21.45 ? 49  VAL A CB   1 
ATOM   391  C  CG1  . VAL A 1 49  ? -22.522 3.130   17.569  1.00 23.03 ? 49  VAL A CG1  1 
ATOM   392  C  CG2  . VAL A 1 49  ? -22.595 2.428   19.972  1.00 20.92 ? 49  VAL A CG2  1 
ATOM   393  N  N    . SER A 1 50  ? -24.327 6.370   17.802  1.00 22.73 ? 50  SER A N    1 
ATOM   394  C  CA   . SER A 1 50  ? -25.196 7.037   16.814  1.00 22.98 ? 50  SER A CA   1 
ATOM   395  C  C    . SER A 1 50  ? -24.581 7.091   15.448  1.00 20.87 ? 50  SER A C    1 
ATOM   396  O  O    . SER A 1 50  ? -23.899 8.036   15.096  1.00 21.55 ? 50  SER A O    1 
ATOM   397  C  CB   . SER A 1 50  ? -25.614 8.432   17.276  1.00 22.29 ? 50  SER A CB   1 
ATOM   398  O  OG   . SER A 1 50  ? -25.944 8.345   18.652  1.00 27.41 ? 50  SER A OG   1 
ATOM   399  N  N    . TYR A 1 51  ? -24.840 6.050   14.657  1.00 20.70 ? 51  TYR A N    1 
ATOM   400  C  CA   . TYR A 1 51  ? -24.290 5.888   13.305  1.00 20.53 ? 51  TYR A CA   1 
ATOM   401  C  C    . TYR A 1 51  ? -25.273 6.174   12.133  1.00 20.96 ? 51  TYR A C    1 
ATOM   402  O  O    . TYR A 1 51  ? -24.925 6.010   10.930  1.00 20.11 ? 51  TYR A O    1 
ATOM   403  C  CB   . TYR A 1 51  ? -23.602 4.487   13.127  1.00 17.84 ? 51  TYR A CB   1 
ATOM   404  C  CG   . TYR A 1 51  ? -22.274 4.259   13.910  1.00 19.30 ? 51  TYR A CG   1 
ATOM   405  C  CD1  . TYR A 1 51  ? -21.550 5.321   14.495  1.00 16.45 ? 51  TYR A CD1  1 
ATOM   406  C  CD2  . TYR A 1 51  ? -21.758 2.976   14.020  1.00 12.09 ? 51  TYR A CD2  1 
ATOM   407  C  CE1  . TYR A 1 51  ? -20.354 5.054   15.243  1.00 15.74 ? 51  TYR A CE1  1 
ATOM   408  C  CE2  . TYR A 1 51  ? -20.612 2.691   14.673  1.00 16.08 ? 51  TYR A CE2  1 
ATOM   409  C  CZ   . TYR A 1 51  ? -19.879 3.740   15.294  1.00 16.85 ? 51  TYR A CZ   1 
ATOM   410  O  OH   . TYR A 1 51  ? -18.724 3.348   15.947  1.00 13.73 ? 51  TYR A OH   1 
ATOM   411  N  N    . ASP A 1 52  ? -26.481 6.636   12.482  1.00 24.13 ? 52  ASP A N    1 
ATOM   412  C  CA   . ASP A 1 52  ? -27.525 6.948   11.437  1.00 26.44 ? 52  ASP A CA   1 
ATOM   413  C  C    . ASP A 1 52  ? -27.008 7.800   10.266  1.00 26.46 ? 52  ASP A C    1 
ATOM   414  O  O    . ASP A 1 52  ? -27.288 7.510   9.088   1.00 27.54 ? 52  ASP A O    1 
ATOM   415  C  CB   . ASP A 1 52  ? -28.821 7.550   12.025  1.00 27.35 ? 52  ASP A CB   1 
ATOM   416  C  CG   . ASP A 1 52  ? -28.583 8.535   13.202  1.00 31.30 ? 52  ASP A CG   1 
ATOM   417  O  OD1  . ASP A 1 52  ? -28.146 8.146   14.337  1.00 38.02 ? 52  ASP A OD1  1 
ATOM   418  O  OD2  . ASP A 1 52  ? -28.926 9.724   13.015  1.00 37.57 ? 52  ASP A OD2  1 
ATOM   419  N  N    . GLN A 1 53  ? -26.205 8.810   10.569  1.00 26.17 ? 53  GLN A N    1 
ATOM   420  C  CA   . GLN A 1 53  ? -25.756 9.718   9.482   1.00 24.96 ? 53  GLN A CA   1 
ATOM   421  C  C    . GLN A 1 53  ? -24.308 9.530   9.041   1.00 23.75 ? 53  GLN A C    1 
ATOM   422  O  O    . GLN A 1 53  ? -23.749 10.420  8.399   1.00 22.54 ? 53  GLN A O    1 
ATOM   423  C  CB   . GLN A 1 53  ? -25.989 11.165  9.904   1.00 25.72 ? 53  GLN A CB   1 
ATOM   424  C  CG   . GLN A 1 53  ? -27.462 11.589  10.031  1.00 31.35 ? 53  GLN A CG   1 
ATOM   425  C  CD   . GLN A 1 53  ? -27.972 12.055  8.677   1.00 38.02 ? 53  GLN A CD   1 
ATOM   426  O  OE1  . GLN A 1 53  ? -27.970 13.266  8.383   1.00 43.62 ? 53  GLN A OE1  1 
ATOM   427  N  NE2  . GLN A 1 53  ? -28.334 11.099  7.804   1.00 42.05 ? 53  GLN A NE2  1 
ATOM   428  N  N    . ALA A 1 54  ? -23.690 8.374   9.359   1.00 21.99 ? 54  ALA A N    1 
ATOM   429  C  CA   . ALA A 1 54  ? -22.332 8.097   8.899   1.00 20.72 ? 54  ALA A CA   1 
ATOM   430  C  C    . ALA A 1 54  ? -22.092 8.221   7.394   1.00 21.21 ? 54  ALA A C    1 
ATOM   431  O  O    . ALA A 1 54  ? -22.838 7.659   6.549   1.00 21.97 ? 54  ALA A O    1 
ATOM   432  C  CB   . ALA A 1 54  ? -21.820 6.718   9.422   1.00 20.80 ? 54  ALA A CB   1 
ATOM   433  N  N    . THR A 1 55  ? -21.029 8.926   7.053   1.00 18.53 ? 55  THR A N    1 
ATOM   434  C  CA   . THR A 1 55  ? -20.590 9.023   5.655   1.00 20.42 ? 55  THR A CA   1 
ATOM   435  C  C    . THR A 1 55  ? -19.225 8.459   5.319   1.00 20.57 ? 55  THR A C    1 
ATOM   436  O  O    . THR A 1 55  ? -18.239 9.139   5.555   1.00 19.07 ? 55  THR A O    1 
ATOM   437  C  CB   . THR A 1 55  ? -20.501 10.537  5.225   1.00 21.26 ? 55  THR A CB   1 
ATOM   438  O  OG1  . THR A 1 55  ? -21.727 11.166  5.497   1.00 26.32 ? 55  THR A OG1  1 
ATOM   439  C  CG2  . THR A 1 55  ? -20.307 10.601  3.714   1.00 24.93 ? 55  THR A CG2  1 
ATOM   440  N  N    . SER A 1 56  ? -19.140 7.277   4.697   1.00 20.86 ? 56  SER A N    1 
ATOM   441  C  CA   . SER A 1 56  ? -17.862 6.743   4.297   1.00 21.61 ? 56  SER A CA   1 
ATOM   442  C  C    . SER A 1 56  ? -17.369 7.433   3.017   1.00 22.26 ? 56  SER A C    1 
ATOM   443  O  O    . SER A 1 56  ? -18.166 7.962   2.218   1.00 22.44 ? 56  SER A O    1 
ATOM   444  C  CB   . SER A 1 56  ? -17.885 5.195   4.143   1.00 21.91 ? 56  SER A CB   1 
ATOM   445  O  OG   . SER A 1 56  ? -18.861 4.786   3.190   1.00 20.42 ? 56  SER A OG   1 
ATOM   446  N  N    . LEU A 1 57  ? -16.061 7.477   2.868   1.00 22.48 ? 57  LEU A N    1 
ATOM   447  C  CA   . LEU A 1 57  ? -15.465 8.116   1.718   1.00 23.39 ? 57  LEU A CA   1 
ATOM   448  C  C    . LEU A 1 57  ? -14.641 7.183   0.823   1.00 23.56 ? 57  LEU A C    1 
ATOM   449  O  O    . LEU A 1 57  ? -14.737 7.251   -0.402  1.00 21.23 ? 57  LEU A O    1 
ATOM   450  C  CB   . LEU A 1 57  ? -14.570 9.255   2.188   1.00 24.48 ? 57  LEU A CB   1 
ATOM   451  C  CG   . LEU A 1 57  ? -15.353 10.395  2.900   1.00 25.57 ? 57  LEU A CG   1 
ATOM   452  C  CD1  . LEU A 1 57  ? -14.372 11.402  3.482   1.00 25.15 ? 57  LEU A CD1  1 
ATOM   453  C  CD2  . LEU A 1 57  ? -16.347 11.046  1.969   1.00 27.41 ? 57  LEU A CD2  1 
ATOM   454  N  N    . ARG A 1 58  ? -13.745 6.411   1.442   1.00 22.29 ? 58  ARG A N    1 
ATOM   455  C  CA   . ARG A 1 58  ? -12.716 5.718   0.711   1.00 22.54 ? 58  ARG A CA   1 
ATOM   456  C  C    . ARG A 1 58  ? -12.273 4.541   1.555   1.00 21.69 ? 58  ARG A C    1 
ATOM   457  O  O    . ARG A 1 58  ? -12.430 4.515   2.820   1.00 20.11 ? 58  ARG A O    1 
ATOM   458  C  CB   . ARG A 1 58  ? -11.416 6.529   0.498   1.00 22.85 ? 58  ARG A CB   1 
ATOM   459  C  CG   . ARG A 1 58  ? -11.359 7.622   -0.626  1.00 25.17 ? 58  ARG A CG   1 
ATOM   460  C  CD   . ARG A 1 58  ? -9.915  8.026   -0.813  1.00 27.02 ? 58  ARG A CD   1 
ATOM   461  N  NE   . ARG A 1 58  ? -9.229  7.643   0.441   1.00 33.51 ? 58  ARG A NE   1 
ATOM   462  C  CZ   . ARG A 1 58  ? -7.921  7.459   0.516   1.00 31.39 ? 58  ARG A CZ   1 
ATOM   463  N  NH1  . ARG A 1 58  ? -7.219  7.634   -0.565  1.00 31.66 ? 58  ARG A NH1  1 
ATOM   464  N  NH2  . ARG A 1 58  ? -7.316  7.164   1.654   1.00 34.72 ? 58  ARG A NH2  1 
ATOM   465  N  N    . ILE A 1 59  ? -11.657 3.628   0.839   1.00 19.48 ? 59  ILE A N    1 
ATOM   466  C  CA   . ILE A 1 59  ? -10.970 2.512   1.489   1.00 18.98 ? 59  ILE A CA   1 
ATOM   467  C  C    . ILE A 1 59  ? -9.544  2.412   0.977   1.00 19.88 ? 59  ILE A C    1 
ATOM   468  O  O    . ILE A 1 59  ? -9.262  2.580   -0.236  1.00 19.67 ? 59  ILE A O    1 
ATOM   469  C  CB   . ILE A 1 59  ? -11.826 1.204   1.334   1.00 17.48 ? 59  ILE A CB   1 
ATOM   470  C  CG1  . ILE A 1 59  ? -11.152 0.044   2.073   1.00 16.06 ? 59  ILE A CG1  1 
ATOM   471  C  CG2  . ILE A 1 59  ? -11.921 0.736   -0.173  1.00 19.19 ? 59  ILE A CG2  1 
ATOM   472  C  CD1  . ILE A 1 59  ? -11.965 -1.342  2.022   1.00 17.04 ? 59  ILE A CD1  1 
ATOM   473  N  N    . LEU A 1 60  ? -8.625  2.124   1.899   1.00 18.66 ? 60  LEU A N    1 
ATOM   474  C  CA   . LEU A 1 60  ? -7.228  2.204   1.655   1.00 19.39 ? 60  LEU A CA   1 
ATOM   475  C  C    . LEU A 1 60  ? -6.412  1.027   2.257   1.00 19.13 ? 60  LEU A C    1 
ATOM   476  O  O    . LEU A 1 60  ? -6.574  0.702   3.433   1.00 19.24 ? 60  LEU A O    1 
ATOM   477  C  CB   . LEU A 1 60  ? -6.743  3.578   2.226   1.00 19.10 ? 60  LEU A CB   1 
ATOM   478  C  CG   . LEU A 1 60  ? -5.240  3.686   2.429   1.00 20.87 ? 60  LEU A CG   1 
ATOM   479  C  CD1  . LEU A 1 60  ? -4.539  3.847   1.058   1.00 24.00 ? 60  LEU A CD1  1 
ATOM   480  C  CD2  . LEU A 1 60  ? -4.895  4.852   3.401   1.00 20.51 ? 60  LEU A CD2  1 
ATOM   481  N  N    . ASN A 1 61  ? -5.567  0.385   1.462   1.00 17.50 ? 61  ASN A N    1 
ATOM   482  C  CA   . ASN A 1 61  ? -4.561  -0.538  1.972   1.00 19.14 ? 61  ASN A CA   1 
ATOM   483  C  C    . ASN A 1 61  ? -3.314  0.311   2.279   1.00 17.80 ? 61  ASN A C    1 
ATOM   484  O  O    . ASN A 1 61  ? -2.718  0.919   1.353   1.00 18.53 ? 61  ASN A O    1 
ATOM   485  C  CB   . ASN A 1 61  ? -4.271  -1.646  0.932   1.00 17.05 ? 61  ASN A CB   1 
ATOM   486  C  CG   . ASN A 1 61  ? -3.158  -2.567  1.305   1.00 18.90 ? 61  ASN A CG   1 
ATOM   487  O  OD1  . ASN A 1 61  ? -2.279  -2.306  2.153   1.00 18.29 ? 61  ASN A OD1  1 
ATOM   488  N  ND2  . ASN A 1 61  ? -3.163  -3.715  0.649   1.00 21.31 ? 61  ASN A ND2  1 
ATOM   489  N  N    . ASN A 1 62  ? -2.925  0.363   3.563   1.00 16.88 ? 62  ASN A N    1 
ATOM   490  C  CA   . ASN A 1 62  ? -1.714  1.166   4.025   1.00 18.62 ? 62  ASN A CA   1 
ATOM   491  C  C    . ASN A 1 62  ? -0.461  0.310   4.285   1.00 19.76 ? 62  ASN A C    1 
ATOM   492  O  O    . ASN A 1 62  ? 0.575   0.739   4.903   1.00 22.43 ? 62  ASN A O    1 
ATOM   493  C  CB   . ASN A 1 62  ? -2.098  2.034   5.253   1.00 19.75 ? 62  ASN A CB   1 
ATOM   494  C  CG   . ASN A 1 62  ? -2.525  1.184   6.480   1.00 20.16 ? 62  ASN A CG   1 
ATOM   495  O  OD1  . ASN A 1 62  ? -2.399  -0.036  6.486   1.00 17.53 ? 62  ASN A OD1  1 
ATOM   496  N  ND2  . ASN A 1 62  ? -2.956  1.857   7.539   1.00 23.12 ? 62  ASN A ND2  1 
ATOM   497  N  N    . GLY A 1 63  ? -0.534  -0.936  3.833   1.00 16.28 ? 63  GLY A N    1 
ATOM   498  C  CA   . GLY A 1 63  ? 0.536   -1.850  4.033   1.00 17.22 ? 63  GLY A CA   1 
ATOM   499  C  C    . GLY A 1 63  ? 0.520   -2.532  5.385   1.00 15.74 ? 63  GLY A C    1 
ATOM   500  O  O    . GLY A 1 63  ? 1.310   -3.407  5.604   1.00 17.95 ? 63  GLY A O    1 
ATOM   501  N  N    . HIS A 1 64  ? -0.429  -2.165  6.264   1.00 14.94 ? 64  HIS A N    1 
ATOM   502  C  CA   . HIS A 1 64  ? -0.576  -2.813  7.634   1.00 16.96 ? 64  HIS A CA   1 
ATOM   503  C  C    . HIS A 1 64  ? -1.972  -3.462  7.758   1.00 15.47 ? 64  HIS A C    1 
ATOM   504  O  O    . HIS A 1 64  ? -2.121  -4.551  8.397   1.00 17.10 ? 64  HIS A O    1 
ATOM   505  C  CB   . HIS A 1 64  ? -0.437  -1.758  8.763   1.00 16.38 ? 64  HIS A CB   1 
ATOM   506  C  CG   . HIS A 1 64  ? 0.788   -0.889  8.630   1.00 20.88 ? 64  HIS A CG   1 
ATOM   507  N  ND1  . HIS A 1 64  ? 2.081   -1.389  8.725   1.00 23.17 ? 64  HIS A ND1  1 
ATOM   508  C  CD2  . HIS A 1 64  ? 0.918   0.447   8.441   1.00 25.13 ? 64  HIS A CD2  1 
ATOM   509  C  CE1  . HIS A 1 64  ? 2.957   -0.407  8.587   1.00 24.12 ? 64  HIS A CE1  1 
ATOM   510  N  NE2  . HIS A 1 64  ? 2.284   0.719   8.400   1.00 24.53 ? 64  HIS A NE2  1 
ATOM   511  N  N    . ALA A 1 65  ? -2.982  -2.752  7.260   1.00 14.15 ? 65  ALA A N    1 
ATOM   512  C  CA   . ALA A 1 65  ? -4.374  -3.225  7.222   1.00 14.86 ? 65  ALA A CA   1 
ATOM   513  C  C    . ALA A 1 65  ? -5.149  -2.485  6.095   1.00 14.29 ? 65  ALA A C    1 
ATOM   514  O  O    . ALA A 1 65  ? -4.497  -1.895  5.208   1.00 15.92 ? 65  ALA A O    1 
ATOM   515  C  CB   . ALA A 1 65  ? -5.062  -3.063  8.661   1.00 13.33 ? 65  ALA A CB   1 
ATOM   516  N  N    . PHE A 1 66  ? -6.497  -2.536  6.069   1.00 13.95 ? 66  PHE A N    1 
ATOM   517  C  CA   . PHE A 1 66  ? -7.279  -1.666  5.193   1.00 14.89 ? 66  PHE A CA   1 
ATOM   518  C  C    . PHE A 1 66  ? -8.118  -0.786  6.066   1.00 16.18 ? 66  PHE A C    1 
ATOM   519  O  O    . PHE A 1 66  ? -8.679  -1.262  7.043   1.00 14.56 ? 66  PHE A O    1 
ATOM   520  C  CB   . PHE A 1 66  ? -8.135  -2.410  4.111   1.00 16.53 ? 66  PHE A CB   1 
ATOM   521  C  CG   . PHE A 1 66  ? -9.186  -3.345  4.680   1.00 13.32 ? 66  PHE A CG   1 
ATOM   522  C  CD1  . PHE A 1 66  ? -8.879  -4.734  4.836   1.00 16.34 ? 66  PHE A CD1  1 
ATOM   523  C  CD2  . PHE A 1 66  ? -10.470 -2.877  5.027   1.00 14.98 ? 66  PHE A CD2  1 
ATOM   524  C  CE1  . PHE A 1 66  ? -9.785  -5.628  5.383   1.00 16.45 ? 66  PHE A CE1  1 
ATOM   525  C  CE2  . PHE A 1 66  ? -11.378 -3.745  5.578   1.00 13.06 ? 66  PHE A CE2  1 
ATOM   526  C  CZ   . PHE A 1 66  ? -11.047 -5.166  5.738   1.00 14.49 ? 66  PHE A CZ   1 
ATOM   527  N  N    . ASN A 1 67  ? -8.184  0.513   5.751   1.00 16.40 ? 67  ASN A N    1 
ATOM   528  C  CA   . ASN A 1 67  ? -8.934  1.450   6.561   1.00 17.99 ? 67  ASN A CA   1 
ATOM   529  C  C    . ASN A 1 67  ? -10.115 1.882   5.765   1.00 17.01 ? 67  ASN A C    1 
ATOM   530  O  O    . ASN A 1 67  ? -9.942  2.295   4.620   1.00 20.01 ? 67  ASN A O    1 
ATOM   531  C  CB   . ASN A 1 67  ? -8.134  2.768   6.869   1.00 18.43 ? 67  ASN A CB   1 
ATOM   532  C  CG   . ASN A 1 67  ? -7.020  2.632   7.879   1.00 23.76 ? 67  ASN A CG   1 
ATOM   533  O  OD1  . ASN A 1 67  ? -6.231  3.637   8.052   1.00 26.08 ? 67  ASN A OD1  1 
ATOM   534  N  ND2  . ASN A 1 67  ? -6.904  1.484   8.575   1.00 15.68 ? 67  ASN A ND2  1 
ATOM   535  N  N    . VAL A 1 68  ? -11.309 1.812   6.336   1.00 16.11 ? 68  VAL A N    1 
ATOM   536  C  CA   . VAL A 1 68  ? -12.469 2.472   5.716   1.00 17.61 ? 68  VAL A CA   1 
ATOM   537  C  C    . VAL A 1 68  ? -12.614 3.828   6.430   1.00 19.07 ? 68  VAL A C    1 
ATOM   538  O  O    . VAL A 1 68  ? -12.802 3.893   7.652   1.00 17.07 ? 68  VAL A O    1 
ATOM   539  C  CB   . VAL A 1 68  ? -13.730 1.643   5.800   1.00 18.07 ? 68  VAL A CB   1 
ATOM   540  C  CG1  . VAL A 1 68  ? -15.002 2.492   5.289   1.00 16.56 ? 68  VAL A CG1  1 
ATOM   541  C  CG2  . VAL A 1 68  ? -13.570 0.313   4.972   1.00 14.65 ? 68  VAL A CG2  1 
ATOM   542  N  N    . GLU A 1 69  ? -12.500 4.897   5.665   1.00 20.57 ? 69  GLU A N    1 
ATOM   543  C  CA   . GLU A 1 69  ? -12.491 6.252   6.234   1.00 21.67 ? 69  GLU A CA   1 
ATOM   544  C  C    . GLU A 1 69  ? -13.771 7.018   5.980   1.00 21.70 ? 69  GLU A C    1 
ATOM   545  O  O    . GLU A 1 69  ? -14.411 6.845   4.917   1.00 23.46 ? 69  GLU A O    1 
ATOM   546  C  CB   . GLU A 1 69  ? -11.376 7.055   5.614   1.00 23.47 ? 69  GLU A CB   1 
ATOM   547  C  CG   . GLU A 1 69  ? -10.097 6.355   5.451   1.00 26.60 ? 69  GLU A CG   1 
ATOM   548  C  CD   . GLU A 1 69  ? -9.504  6.769   4.159   1.00 32.53 ? 69  GLU A CD   1 
ATOM   549  O  OE1  . GLU A 1 69  ? -10.301 7.395   3.402   1.00 33.14 ? 69  GLU A OE1  1 
ATOM   550  O  OE2  . GLU A 1 69  ? -8.293  6.496   3.917   1.00 35.36 ? 69  GLU A OE2  1 
ATOM   551  N  N    . PHE A 1 70  ? -14.154 7.830   6.969   1.00 17.78 ? 70  PHE A N    1 
ATOM   552  C  CA   . PHE A 1 70  ? -15.439 8.511   7.055   1.00 16.29 ? 70  PHE A CA   1 
ATOM   553  C  C    . PHE A 1 70  ? -15.213 10.033  6.988   1.00 16.79 ? 70  PHE A C    1 
ATOM   554  O  O    . PHE A 1 70  ? -14.193 10.487  7.361   1.00 17.22 ? 70  PHE A O    1 
ATOM   555  C  CB   . PHE A 1 70  ? -16.188 8.160   8.344   1.00 15.64 ? 70  PHE A CB   1 
ATOM   556  C  CG   . PHE A 1 70  ? -16.754 6.752   8.329   1.00 15.18 ? 70  PHE A CG   1 
ATOM   557  C  CD1  . PHE A 1 70  ? -15.908 5.657   8.529   1.00 15.88 ? 70  PHE A CD1  1 
ATOM   558  C  CD2  . PHE A 1 70  ? -18.091 6.516   8.045   1.00 17.70 ? 70  PHE A CD2  1 
ATOM   559  C  CE1  . PHE A 1 70  ? -16.406 4.323   8.456   1.00 17.91 ? 70  PHE A CE1  1 
ATOM   560  C  CE2  . PHE A 1 70  ? -18.616 5.163   7.998   1.00 16.76 ? 70  PHE A CE2  1 
ATOM   561  C  CZ   . PHE A 1 70  ? -17.756 4.089   8.206   1.00 15.93 ? 70  PHE A CZ   1 
ATOM   562  N  N    . ASP A 1 71  ? -16.202 10.789  6.522   1.00 16.91 ? 71  ASP A N    1 
ATOM   563  C  CA   . ASP A 1 71  ? -16.108 12.262  6.597   1.00 18.13 ? 71  ASP A CA   1 
ATOM   564  C  C    . ASP A 1 71  ? -16.463 12.636  8.033   1.00 16.57 ? 71  ASP A C    1 
ATOM   565  O  O    . ASP A 1 71  ? -17.578 12.372  8.543   1.00 19.45 ? 71  ASP A O    1 
ATOM   566  C  CB   . ASP A 1 71  ? -17.012 12.901  5.567   1.00 20.41 ? 71  ASP A CB   1 
ATOM   567  C  CG   . ASP A 1 71  ? -17.395 14.334  5.911   1.00 23.69 ? 71  ASP A CG   1 
ATOM   568  O  OD1  . ASP A 1 71  ? -16.670 15.008  6.645   1.00 26.68 ? 71  ASP A OD1  1 
ATOM   569  O  OD2  . ASP A 1 71  ? -18.461 14.787  5.442   1.00 31.58 ? 71  ASP A OD2  1 
ATOM   570  N  N    . ASP A 1 72  ? -15.476 13.142  8.747   1.00 14.71 ? 72  ASP A N    1 
ATOM   571  C  CA   . ASP A 1 72  ? -15.626 13.466  10.188  1.00 15.81 ? 72  ASP A CA   1 
ATOM   572  C  C    . ASP A 1 72  ? -15.627 14.977  10.364  1.00 17.59 ? 72  ASP A C    1 
ATOM   573  O  O    . ASP A 1 72  ? -15.197 15.485  11.411  1.00 17.81 ? 72  ASP A O    1 
ATOM   574  C  CB   . ASP A 1 72  ? -14.458 12.866  11.007  1.00 16.45 ? 72  ASP A CB   1 
ATOM   575  C  CG   . ASP A 1 72  ? -13.092 13.347  10.547  1.00 16.83 ? 72  ASP A CG   1 
ATOM   576  O  OD1  . ASP A 1 72  ? -12.939 13.962  9.465   1.00 15.13 ? 72  ASP A OD1  1 
ATOM   577  O  OD2  . ASP A 1 72  ? -12.113 13.098  11.253  1.00 15.76 ? 72  ASP A OD2  1 
ATOM   578  N  N    . SER A 1 73  ? -16.087 15.690  9.336   1.00 18.08 ? 73  SER A N    1 
ATOM   579  C  CA   . SER A 1 73  ? -16.090 17.191  9.397   1.00 20.02 ? 73  SER A CA   1 
ATOM   580  C  C    . SER A 1 73  ? -17.409 17.746  10.001  1.00 21.37 ? 73  SER A C    1 
ATOM   581  O  O    . SER A 1 73  ? -17.585 18.974  10.167  1.00 19.69 ? 73  SER A O    1 
ATOM   582  C  CB   . SER A 1 73  ? -15.736 17.793  8.020   1.00 18.69 ? 73  SER A CB   1 
ATOM   583  O  OG   . SER A 1 73  ? -16.848 17.543  7.129   1.00 19.40 ? 73  SER A OG   1 
ATOM   584  N  N    . GLN A 1 74  ? -18.339 16.862  10.372  1.00 22.16 ? 74  GLN A N    1 
ATOM   585  C  CA   . GLN A 1 74  ? -19.504 17.304  11.160  1.00 25.51 ? 74  GLN A CA   1 
ATOM   586  C  C    . GLN A 1 74  ? -19.834 16.185  12.129  1.00 25.68 ? 74  GLN A C    1 
ATOM   587  O  O    . GLN A 1 74  ? -19.285 15.103  11.992  1.00 25.16 ? 74  GLN A O    1 
ATOM   588  C  CB   . GLN A 1 74  ? -20.732 17.536  10.265  1.00 25.03 ? 74  GLN A CB   1 
ATOM   589  C  CG   . GLN A 1 74  ? -20.655 18.659  9.230   1.00 29.77 ? 74  GLN A CG   1 
ATOM   590  C  CD   . GLN A 1 74  ? -21.703 18.494  8.141   1.00 29.75 ? 74  GLN A CD   1 
ATOM   591  O  OE1  . GLN A 1 74  ? -22.891 18.750  8.374   1.00 39.57 ? 74  GLN A OE1  1 
ATOM   592  N  NE2  . GLN A 1 74  ? -21.279 18.052  6.941   1.00 36.69 ? 74  GLN A NE2  1 
ATOM   593  N  N    . ASP A 1 75  ? -20.769 16.444  13.045  1.00 27.14 ? 75  ASP A N    1 
ATOM   594  C  CA   . ASP A 1 75  ? -21.155 15.525  14.113  1.00 29.25 ? 75  ASP A CA   1 
ATOM   595  C  C    . ASP A 1 75  ? -22.141 14.514  13.531  1.00 29.06 ? 75  ASP A C    1 
ATOM   596  O  O    . ASP A 1 75  ? -23.332 14.575  13.834  1.00 29.94 ? 75  ASP A O    1 
ATOM   597  C  CB   . ASP A 1 75  ? -21.837 16.275  15.289  1.00 31.62 ? 75  ASP A CB   1 
ATOM   598  C  CG   . ASP A 1 75  ? -20.902 16.452  16.554  1.00 36.17 ? 75  ASP A CG   1 
ATOM   599  O  OD1  . ASP A 1 75  ? -19.753 15.930  16.609  1.00 36.69 ? 75  ASP A OD1  1 
ATOM   600  O  OD2  . ASP A 1 75  ? -21.374 17.069  17.539  1.00 41.46 ? 75  ASP A OD2  1 
ATOM   601  N  N    . LYS A 1 76  ? -21.644 13.597  12.719  1.00 26.91 ? 76  LYS A N    1 
ATOM   602  C  CA   . LYS A 1 76  ? -22.484 12.633  11.992  1.00 26.49 ? 76  LYS A CA   1 
ATOM   603  C  C    . LYS A 1 76  ? -22.517 11.164  12.484  1.00 27.87 ? 76  LYS A C    1 
ATOM   604  O  O    . LYS A 1 76  ? -23.479 10.416  12.197  1.00 29.57 ? 76  LYS A O    1 
ATOM   605  C  CB   . LYS A 1 76  ? -22.078 12.603  10.541  1.00 25.53 ? 76  LYS A CB   1 
ATOM   606  C  CG   . LYS A 1 76  ? -22.625 13.739  9.680   1.00 27.12 ? 76  LYS A CG   1 
ATOM   607  C  CD   . LYS A 1 76  ? -22.050 13.517  8.282   1.00 31.78 ? 76  LYS A CD   1 
ATOM   608  C  CE   . LYS A 1 76  ? -22.170 14.694  7.307   1.00 35.33 ? 76  LYS A CE   1 
ATOM   609  N  NZ   . LYS A 1 76  ? -21.512 14.236  6.059   1.00 30.64 ? 76  LYS A NZ   1 
ATOM   610  N  N    . ALA A 1 77  ? -21.442 10.687  13.063  1.00 25.90 ? 77  ALA A N    1 
ATOM   611  C  CA   . ALA A 1 77  ? -21.388 9.267   13.507  1.00 23.68 ? 77  ALA A CA   1 
ATOM   612  C  C    . ALA A 1 77  ? -20.671 9.382   14.826  1.00 23.07 ? 77  ALA A C    1 
ATOM   613  O  O    . ALA A 1 77  ? -19.431 9.511   14.854  1.00 23.93 ? 77  ALA A O    1 
ATOM   614  C  CB   . ALA A 1 77  ? -20.576 8.435   12.540  1.00 22.86 ? 77  ALA A CB   1 
ATOM   615  N  N    . VAL A 1 78  ? -21.409 9.441   15.918  1.00 20.95 ? 78  VAL A N    1 
ATOM   616  C  CA   . VAL A 1 78  ? -20.739 9.717   17.193  1.00 20.61 ? 78  VAL A CA   1 
ATOM   617  C  C    . VAL A 1 78  ? -20.904 8.617   18.268  1.00 18.72 ? 78  VAL A C    1 
ATOM   618  O  O    . VAL A 1 78  ? -21.955 7.950   18.393  1.00 18.06 ? 78  VAL A O    1 
ATOM   619  C  CB   . VAL A 1 78  ? -21.179 11.127  17.766  1.00 22.04 ? 78  VAL A CB   1 
ATOM   620  C  CG1  . VAL A 1 78  ? -21.115 12.221  16.693  1.00 24.62 ? 78  VAL A CG1  1 
ATOM   621  C  CG2  . VAL A 1 78  ? -22.565 11.036  18.262  1.00 22.32 ? 78  VAL A CG2  1 
ATOM   622  N  N    . LEU A 1 79  ? -19.834 8.443   19.044  1.00 18.11 ? 79  LEU A N    1 
ATOM   623  C  CA   . LEU A 1 79  ? -19.874 7.681   20.282  1.00 18.05 ? 79  LEU A CA   1 
ATOM   624  C  C    . LEU A 1 79  ? -19.870 8.556   21.526  1.00 19.56 ? 79  LEU A C    1 
ATOM   625  O  O    . LEU A 1 79  ? -19.159 9.583   21.619  1.00 18.84 ? 79  LEU A O    1 
ATOM   626  C  CB   . LEU A 1 79  ? -18.649 6.758   20.311  1.00 18.17 ? 79  LEU A CB   1 
ATOM   627  C  CG   . LEU A 1 79  ? -18.548 5.638   21.287  1.00 19.75 ? 79  LEU A CG   1 
ATOM   628  C  CD1  . LEU A 1 79  ? -19.650 4.613   21.023  1.00 19.71 ? 79  LEU A CD1  1 
ATOM   629  C  CD2  . LEU A 1 79  ? -17.150 5.000   21.121  1.00 14.54 ? 79  LEU A CD2  1 
ATOM   630  N  N    . LYS A 1 80  ? -20.687 8.165   22.475  1.00 18.04 ? 80  LYS A N    1 
ATOM   631  C  CA   . LYS A 1 80  ? -20.709 8.861   23.756  1.00 20.85 ? 80  LYS A CA   1 
ATOM   632  C  C    . LYS A 1 80  ? -21.275 7.953   24.859  1.00 20.78 ? 80  LYS A C    1 
ATOM   633  O  O    . LYS A 1 80  ? -21.627 6.778   24.586  1.00 19.83 ? 80  LYS A O    1 
ATOM   634  C  CB   . LYS A 1 80  ? -21.376 10.246  23.647  1.00 21.01 ? 80  LYS A CB   1 
ATOM   635  C  CG   . LYS A 1 80  ? -22.858 10.231  23.519  1.00 24.45 ? 80  LYS A CG   1 
ATOM   636  C  CD   . LYS A 1 80  ? -23.427 11.634  23.315  0.01 21.61 ? 80  LYS A CD   1 
ATOM   637  C  CE   . LYS A 1 80  ? -23.271 12.109  21.875  0.01 22.15 ? 80  LYS A CE   1 
ATOM   638  N  NZ   . LYS A 1 80  ? -23.780 13.494  21.679  0.01 21.82 ? 80  LYS A NZ   1 
ATOM   639  N  N    . GLY A 1 81  ? -21.367 8.470   26.080  1.00 20.81 ? 81  GLY A N    1 
ATOM   640  C  CA   . GLY A 1 81  ? -21.952 7.722   27.162  1.00 21.67 ? 81  GLY A CA   1 
ATOM   641  C  C    . GLY A 1 81  ? -20.953 6.649   27.561  1.00 23.10 ? 81  GLY A C    1 
ATOM   642  O  O    . GLY A 1 81  ? -19.757 6.831   27.409  1.00 22.12 ? 81  GLY A O    1 
ATOM   643  N  N    . GLY A 1 82  ? -21.431 5.509   28.045  1.00 24.00 ? 82  GLY A N    1 
ATOM   644  C  CA   . GLY A 1 82  ? -20.471 4.508   28.566  1.00 23.55 ? 82  GLY A CA   1 
ATOM   645  C  C    . GLY A 1 82  ? -19.563 5.091   29.602  1.00 22.49 ? 82  GLY A C    1 
ATOM   646  O  O    . GLY A 1 82  ? -20.015 5.826   30.511  1.00 23.65 ? 82  GLY A O    1 
ATOM   647  N  N    . PRO A 1 83  ? -18.239 4.827   29.478  1.00 19.94 ? 83  PRO A N    1 
ATOM   648  C  CA   . PRO A 1 83  ? -17.254 5.425   30.359  1.00 18.47 ? 83  PRO A CA   1 
ATOM   649  C  C    . PRO A 1 83  ? -16.823 6.874   29.897  1.00 19.22 ? 83  PRO A C    1 
ATOM   650  O  O    . PRO A 1 83  ? -15.940 7.474   30.481  1.00 21.38 ? 83  PRO A O    1 
ATOM   651  C  CB   . PRO A 1 83  ? -16.052 4.472   30.207  1.00 19.35 ? 83  PRO A CB   1 
ATOM   652  C  CG   . PRO A 1 83  ? -16.141 4.093   28.723  1.00 16.17 ? 83  PRO A CG   1 
ATOM   653  C  CD   . PRO A 1 83  ? -17.624 3.965   28.414  1.00 18.52 ? 83  PRO A CD   1 
ATOM   654  N  N    . LEU A 1 84  ? -17.457 7.437   28.886  1.00 19.14 ? 84  LEU A N    1 
ATOM   655  C  CA   . LEU A 1 84  ? -16.834 8.622   28.263  1.00 18.86 ? 84  LEU A CA   1 
ATOM   656  C  C    . LEU A 1 84  ? -17.467 9.890   28.814  1.00 21.00 ? 84  LEU A C    1 
ATOM   657  O  O    . LEU A 1 84  ? -18.656 9.866   29.176  1.00 21.01 ? 84  LEU A O    1 
ATOM   658  C  CB   . LEU A 1 84  ? -16.967 8.577   26.749  1.00 16.40 ? 84  LEU A CB   1 
ATOM   659  C  CG   . LEU A 1 84  ? -16.462 7.270   26.104  1.00 16.56 ? 84  LEU A CG   1 
ATOM   660  C  CD1  . LEU A 1 84  ? -17.065 7.135   24.694  1.00 14.31 ? 84  LEU A CD1  1 
ATOM   661  C  CD2  . LEU A 1 84  ? -14.844 7.200   26.073  1.00 14.67 ? 84  LEU A CD2  1 
ATOM   662  N  N    . ASP A 1 85  ? -16.666 10.950  28.850  1.00 24.05 ? 85  ASP A N    1 
ATOM   663  C  CA   . ASP A 1 85  ? -17.129 12.317  29.129  1.00 26.24 ? 85  ASP A CA   1 
ATOM   664  C  C    . ASP A 1 85  ? -17.129 12.981  27.781  1.00 26.88 ? 85  ASP A C    1 
ATOM   665  O  O    . ASP A 1 85  ? -16.220 12.794  26.953  1.00 27.51 ? 85  ASP A O    1 
ATOM   666  C  CB   . ASP A 1 85  ? -16.156 13.029  30.086  1.00 26.46 ? 85  ASP A CB   1 
ATOM   667  C  CG   . ASP A 1 85  ? -16.278 12.549  31.537  1.00 33.24 ? 85  ASP A CG   1 
ATOM   668  O  OD1  . ASP A 1 85  ? -17.435 12.306  32.021  1.00 34.00 ? 85  ASP A OD1  1 
ATOM   669  O  OD2  . ASP A 1 85  ? -15.203 12.472  32.200  1.00 33.20 ? 85  ASP A OD2  1 
ATOM   670  N  N    . GLY A 1 86  ? -18.166 13.723  27.472  1.00 27.44 ? 86  GLY A N    1 
ATOM   671  C  CA   . GLY A 1 86  ? -18.209 14.268  26.128  1.00 26.48 ? 86  GLY A CA   1 
ATOM   672  C  C    . GLY A 1 86  ? -18.469 13.364  24.915  1.00 27.30 ? 86  GLY A C    1 
ATOM   673  O  O    . GLY A 1 86  ? -19.159 12.338  25.040  1.00 28.20 ? 86  GLY A O    1 
ATOM   674  N  N    . THR A 1 87  ? -17.934 13.768  23.737  1.00 24.03 ? 87  THR A N    1 
ATOM   675  C  CA   . THR A 1 87  ? -18.422 13.304  22.437  1.00 21.58 ? 87  THR A CA   1 
ATOM   676  C  C    . THR A 1 87  ? -17.240 12.900  21.560  1.00 19.33 ? 87  THR A C    1 
ATOM   677  O  O    . THR A 1 87  ? -16.258 13.645  21.439  1.00 16.06 ? 87  THR A O    1 
ATOM   678  C  CB   . THR A 1 87  ? -19.226 14.474  21.673  1.00 22.75 ? 87  THR A CB   1 
ATOM   679  O  OG1  . THR A 1 87  ? -20.506 14.648  22.346  1.00 26.84 ? 87  THR A OG1  1 
ATOM   680  C  CG2  . THR A 1 87  ? -19.483 14.108  20.208  1.00 24.12 ? 87  THR A CG2  1 
ATOM   681  N  N    . TYR A 1 88  ? -17.332 11.715  20.967  1.00 17.88 ? 88  TYR A N    1 
ATOM   682  C  CA   . TYR A 1 88  ? -16.268 11.234  20.089  1.00 16.63 ? 88  TYR A CA   1 
ATOM   683  C  C    . TYR A 1 88  ? -16.735 10.930  18.677  1.00 16.31 ? 88  TYR A C    1 
ATOM   684  O  O    . TYR A 1 88  ? -17.772 10.245  18.463  1.00 19.23 ? 88  TYR A O    1 
ATOM   685  C  CB   . TYR A 1 88  ? -15.598 10.006  20.692  1.00 14.02 ? 88  TYR A CB   1 
ATOM   686  C  CG   . TYR A 1 88  ? -14.832 10.218  21.988  1.00 13.05 ? 88  TYR A CG   1 
ATOM   687  C  CD1  . TYR A 1 88  ? -15.507 10.526  23.215  1.00 12.66 ? 88  TYR A CD1  1 
ATOM   688  C  CD2  . TYR A 1 88  ? -13.435 10.044  22.008  1.00 13.33 ? 88  TYR A CD2  1 
ATOM   689  C  CE1  . TYR A 1 88  ? -14.775 10.698  24.414  1.00 15.46 ? 88  TYR A CE1  1 
ATOM   690  C  CE2  . TYR A 1 88  ? -12.693 10.183  23.233  1.00 9.78  ? 88  TYR A CE2  1 
ATOM   691  C  CZ   . TYR A 1 88  ? -13.373 10.488  24.416  1.00 14.35 ? 88  TYR A CZ   1 
ATOM   692  O  OH   . TYR A 1 88  ? -12.629 10.595  25.574  1.00 14.45 ? 88  TYR A OH   1 
ATOM   693  N  N    . ARG A 1 89  ? -16.031 11.469  17.687  1.00 14.67 ? 89  ARG A N    1 
ATOM   694  C  CA   . ARG A 1 89  ? -16.516 11.365  16.296  1.00 15.22 ? 89  ARG A CA   1 
ATOM   695  C  C    . ARG A 1 89  ? -15.817 10.209  15.521  1.00 13.83 ? 89  ARG A C    1 
ATOM   696  O  O    . ARG A 1 89  ? -14.602 10.114  15.557  1.00 13.11 ? 89  ARG A O    1 
ATOM   697  C  CB   . ARG A 1 89  ? -16.273 12.680  15.575  1.00 16.58 ? 89  ARG A CB   1 
ATOM   698  C  CG   . ARG A 1 89  ? -17.179 12.950  14.416  1.00 23.00 ? 89  ARG A CG   1 
ATOM   699  C  CD   . ARG A 1 89  ? -16.878 14.339  13.921  1.00 22.48 ? 89  ARG A CD   1 
ATOM   700  N  NE   . ARG A 1 89  ? -17.566 15.369  14.719  1.00 27.27 ? 89  ARG A NE   1 
ATOM   701  C  CZ   . ARG A 1 89  ? -17.385 16.670  14.555  1.00 27.95 ? 89  ARG A CZ   1 
ATOM   702  N  NH1  . ARG A 1 89  ? -16.517 17.126  13.652  1.00 27.03 ? 89  ARG A NH1  1 
ATOM   703  N  NH2  . ARG A 1 89  ? -18.031 17.513  15.341  1.00 26.20 ? 89  ARG A NH2  1 
ATOM   704  N  N    . LEU A 1 90  ? -16.573 9.357   14.815  1.00 13.45 ? 90  LEU A N    1 
ATOM   705  C  CA   . LEU A 1 90  ? -15.995 8.272   13.991  1.00 12.66 ? 90  LEU A CA   1 
ATOM   706  C  C    . LEU A 1 90  ? -15.136 8.795   12.852  1.00 13.19 ? 90  LEU A C    1 
ATOM   707  O  O    . LEU A 1 90  ? -15.614 9.532   12.011  1.00 14.67 ? 90  LEU A O    1 
ATOM   708  C  CB   . LEU A 1 90  ? -17.110 7.388   13.403  1.00 12.88 ? 90  LEU A CB   1 
ATOM   709  C  CG   . LEU A 1 90  ? -16.717 6.273   12.440  1.00 13.74 ? 90  LEU A CG   1 
ATOM   710  C  CD1  . LEU A 1 90  ? -15.777 5.226   13.096  1.00 14.04 ? 90  LEU A CD1  1 
ATOM   711  C  CD2  . LEU A 1 90  ? -17.963 5.570   11.983  1.00 11.71 ? 90  LEU A CD2  1 
ATOM   712  N  N    . ILE A 1 91  ? -13.870 8.393   12.817  1.00 11.84 ? 91  ILE A N    1 
ATOM   713  C  CA   . ILE A 1 91  ? -12.990 8.713   11.679  1.00 12.26 ? 91  ILE A CA   1 
ATOM   714  C  C    . ILE A 1 91  ? -12.744 7.545   10.704  1.00 11.05 ? 91  ILE A C    1 
ATOM   715  O  O    . ILE A 1 91  ? -12.676 7.724   9.478   1.00 10.76 ? 91  ILE A O    1 
ATOM   716  C  CB   . ILE A 1 91  ? -11.632 9.345   12.135  1.00 10.87 ? 91  ILE A CB   1 
ATOM   717  C  CG1  . ILE A 1 91  ? -10.760 9.667   10.899  1.00 12.59 ? 91  ILE A CG1  1 
ATOM   718  C  CG2  . ILE A 1 91  ? -10.876 8.425   13.164  1.00 12.36 ? 91  ILE A CG2  1 
ATOM   719  C  CD1  . ILE A 1 91  ? -9.574  10.630  11.249  1.00 16.15 ? 91  ILE A CD1  1 
ATOM   720  N  N    . GLN A 1 92  ? -12.499 6.347   11.238  1.00 10.82 ? 92  GLN A N    1 
ATOM   721  C  CA   . GLN A 1 92  ? -12.247 5.192   10.343  1.00 10.86 ? 92  GLN A CA   1 
ATOM   722  C  C    . GLN A 1 92  ? -12.498 3.882   11.090  1.00 10.71 ? 92  GLN A C    1 
ATOM   723  O  O    . GLN A 1 92  ? -12.594 3.912   12.322  1.00 8.50  ? 92  GLN A O    1 
ATOM   724  C  CB   . GLN A 1 92  ? -10.787 5.244   9.825   1.00 12.67 ? 92  GLN A CB   1 
ATOM   725  C  CG   . GLN A 1 92  ? -9.704  5.149   10.966  1.00 12.09 ? 92  GLN A CG   1 
ATOM   726  C  CD   . GLN A 1 92  ? -8.963  3.807   11.005  1.00 14.63 ? 92  GLN A CD   1 
ATOM   727  O  OE1  . GLN A 1 92  ? -9.541  2.777   11.198  1.00 15.30 ? 92  GLN A OE1  1 
ATOM   728  N  NE2  . GLN A 1 92  ? -7.702  3.850   10.778  1.00 21.49 ? 92  GLN A NE2  1 
ATOM   729  N  N    . PHE A 1 93  ? -12.662 2.783   10.350  1.00 11.11 ? 93  PHE A N    1 
ATOM   730  C  CA   . PHE A 1 93  ? -12.513 1.458   10.988  1.00 11.14 ? 93  PHE A CA   1 
ATOM   731  C  C    . PHE A 1 93  ? -11.515 0.576   10.182  1.00 12.48 ? 93  PHE A C    1 
ATOM   732  O  O    . PHE A 1 93  ? -11.263 0.794   8.991   1.00 12.72 ? 93  PHE A O    1 
ATOM   733  C  CB   . PHE A 1 93  ? -13.882 0.798   11.244  1.00 10.09 ? 93  PHE A CB   1 
ATOM   734  C  CG   . PHE A 1 93  ? -14.565 0.323   9.977   1.00 13.21 ? 93  PHE A CG   1 
ATOM   735  C  CD1  . PHE A 1 93  ? -14.145 -0.840  9.317   1.00 15.42 ? 93  PHE A CD1  1 
ATOM   736  C  CD2  . PHE A 1 93  ? -15.648 1.044   9.464   1.00 12.36 ? 93  PHE A CD2  1 
ATOM   737  C  CE1  . PHE A 1 93  ? -14.783 -1.264  8.138   1.00 17.80 ? 93  PHE A CE1  1 
ATOM   738  C  CE2  . PHE A 1 93  ? -16.311 0.620   8.308   1.00 13.81 ? 93  PHE A CE2  1 
ATOM   739  C  CZ   . PHE A 1 93  ? -15.860 -0.525  7.649   1.00 13.15 ? 93  PHE A CZ   1 
ATOM   740  N  N    . HIS A 1 94  ? -10.930 -0.415  10.856  1.00 12.03 ? 94  HIS A N    1 
ATOM   741  C  CA   . HIS A 1 94  ? -10.040 -1.383  10.241  1.00 11.19 ? 94  HIS A CA   1 
ATOM   742  C  C    . HIS A 1 94  ? -10.197 -2.674  11.078  1.00 9.97  ? 94  HIS A C    1 
ATOM   743  O  O    . HIS A 1 94  ? -10.867 -2.676  12.129  1.00 8.18  ? 94  HIS A O    1 
ATOM   744  C  CB   . HIS A 1 94  ? -8.569  -0.852  10.248  1.00 10.56 ? 94  HIS A CB   1 
ATOM   745  C  CG   . HIS A 1 94  ? -8.051  -0.596  11.639  1.00 13.47 ? 94  HIS A CG   1 
ATOM   746  N  ND1  . HIS A 1 94  ? -8.256  0.597   12.299  1.00 11.49 ? 94  HIS A ND1  1 
ATOM   747  C  CD2  . HIS A 1 94  ? -7.479  -1.427  12.530  1.00 9.07  ? 94  HIS A CD2  1 
ATOM   748  C  CE1  . HIS A 1 94  ? -7.745  0.512   13.522  1.00 14.08 ? 94  HIS A CE1  1 
ATOM   749  N  NE2  . HIS A 1 94  ? -7.302  -0.719  13.715  1.00 8.49  ? 94  HIS A NE2  1 
ATOM   750  N  N    . PHE A 1 95  ? -9.493  -3.709  10.646  1.00 10.47 ? 95  PHE A N    1 
ATOM   751  C  CA   . PHE A 1 95  ? -9.487  -5.024  11.295  1.00 10.09 ? 95  PHE A CA   1 
ATOM   752  C  C    . PHE A 1 95  ? -8.029  -5.490  11.465  1.00 8.44  ? 95  PHE A C    1 
ATOM   753  O  O    . PHE A 1 95  ? -7.063  -4.981  10.818  1.00 10.08 ? 95  PHE A O    1 
ATOM   754  C  CB   . PHE A 1 95  ? -10.217 -6.109  10.441  1.00 9.48  ? 95  PHE A CB   1 
ATOM   755  C  CG   . PHE A 1 95  ? -11.666 -5.798  10.099  1.00 10.48 ? 95  PHE A CG   1 
ATOM   756  C  CD1  . PHE A 1 95  ? -11.976 -4.934  9.023   1.00 9.90  ? 95  PHE A CD1  1 
ATOM   757  C  CD2  . PHE A 1 95  ? -12.702 -6.439  10.748  1.00 12.54 ? 95  PHE A CD2  1 
ATOM   758  C  CE1  . PHE A 1 95  ? -13.313 -4.694  8.637   1.00 11.73 ? 95  PHE A CE1  1 
ATOM   759  C  CE2  . PHE A 1 95  ? -14.039 -6.213  10.365  1.00 12.76 ? 95  PHE A CE2  1 
ATOM   760  C  CZ   . PHE A 1 95  ? -14.337 -5.345  9.301   1.00 13.47 ? 95  PHE A CZ   1 
ATOM   761  N  N    . HIS A 1 96  ? -7.875  -6.452  12.368  1.00 8.26  ? 96  HIS A N    1 
ATOM   762  C  CA   . HIS A 1 96  ? -6.608  -7.225  12.552  1.00 7.86  ? 96  HIS A CA   1 
ATOM   763  C  C    . HIS A 1 96  ? -7.032  -8.660  12.436  1.00 7.38  ? 96  HIS A C    1 
ATOM   764  O  O    . HIS A 1 96  ? -8.093  -9.016  12.971  1.00 9.29  ? 96  HIS A O    1 
ATOM   765  C  CB   . HIS A 1 96  ? -6.080  -6.991  13.993  1.00 8.92  ? 96  HIS A CB   1 
ATOM   766  C  CG   . HIS A 1 96  ? -5.748  -5.532  14.253  1.00 8.88  ? 96  HIS A CG   1 
ATOM   767  N  ND1  . HIS A 1 96  ? -4.481  -5.007  14.019  1.00 11.26 ? 96  HIS A ND1  1 
ATOM   768  C  CD2  . HIS A 1 96  ? -6.541  -4.483  14.603  1.00 12.16 ? 96  HIS A CD2  1 
ATOM   769  C  CE1  . HIS A 1 96  ? -4.501  -3.708  14.313  1.00 14.19 ? 96  HIS A CE1  1 
ATOM   770  N  NE2  . HIS A 1 96  ? -5.749  -3.361  14.633  1.00 13.05 ? 96  HIS A NE2  1 
ATOM   771  N  N    . TRP A 1 97  ? -6.250  -9.507  11.760  1.00 6.67  ? 97  TRP A N    1 
ATOM   772  C  CA   . TRP A 1 97  ? -6.702  -10.930 11.548  1.00 9.29  ? 97  TRP A CA   1 
ATOM   773  C  C    . TRP A 1 97  ? -5.512  -11.867 11.442  1.00 8.39  ? 97  TRP A C    1 
ATOM   774  O  O    . TRP A 1 97  ? -4.338  -11.398 11.357  1.00 10.69 ? 97  TRP A O    1 
ATOM   775  C  CB   . TRP A 1 97  ? -7.620  -11.095 10.334  1.00 9.95  ? 97  TRP A CB   1 
ATOM   776  C  CG   . TRP A 1 97  ? -6.976  -10.642 9.035   1.00 11.63 ? 97  TRP A CG   1 
ATOM   777  C  CD1  . TRP A 1 97  ? -6.283  -11.437 8.136   1.00 12.15 ? 97  TRP A CD1  1 
ATOM   778  C  CD2  . TRP A 1 97  ? -6.961  -9.313  8.483   1.00 13.66 ? 97  TRP A CD2  1 
ATOM   779  N  NE1  . TRP A 1 97  ? -5.841  -10.697 7.092   1.00 14.60 ? 97  TRP A NE1  1 
ATOM   780  C  CE2  . TRP A 1 97  ? -6.196  -9.379  7.284   1.00 14.12 ? 97  TRP A CE2  1 
ATOM   781  C  CE3  . TRP A 1 97  ? -7.443  -8.060  8.923   1.00 13.25 ? 97  TRP A CE3  1 
ATOM   782  C  CZ2  . TRP A 1 97  ? -5.973  -8.274  6.474   1.00 13.57 ? 97  TRP A CZ2  1 
ATOM   783  C  CZ3  . TRP A 1 97  ? -7.187  -6.870  8.046   1.00 10.65 ? 97  TRP A CZ3  1 
ATOM   784  C  CH2  . TRP A 1 97  ? -6.468  -7.033  6.855   1.00 11.86 ? 97  TRP A CH2  1 
ATOM   785  N  N    . GLY A 1 98  ? -5.817  -13.164 11.434  1.00 8.27  ? 98  GLY A N    1 
ATOM   786  C  CA   . GLY A 1 98  ? -4.807  -14.219 11.475  1.00 8.15  ? 98  GLY A CA   1 
ATOM   787  C  C    . GLY A 1 98  ? -4.543  -14.913 10.120  1.00 9.15  ? 98  GLY A C    1 
ATOM   788  O  O    . GLY A 1 98  ? -5.233  -14.682 9.111   1.00 9.72  ? 98  GLY A O    1 
ATOM   789  N  N    . SER A 1 99  ? -3.486  -15.726 10.137  1.00 12.69 ? 99  SER A N    1 
ATOM   790  C  CA   . SER A 1 99  ? -3.171  -16.684 9.063   1.00 13.55 ? 99  SER A CA   1 
ATOM   791  C  C    . SER A 1 99  ? -4.078  -17.923 9.133   1.00 14.94 ? 99  SER A C    1 
ATOM   792  O  O    . SER A 1 99  ? -4.164  -18.677 8.152   1.00 17.24 ? 99  SER A O    1 
ATOM   793  C  CB   . SER A 1 99  ? -1.687  -17.127 9.181   1.00 12.29 ? 99  SER A CB   1 
ATOM   794  O  OG   . SER A 1 99  ? -1.421  -17.733 10.449  1.00 14.48 ? 99  SER A OG   1 
ATOM   795  N  N    . LEU A 1 100 ? -4.745  -18.131 10.273  1.00 13.90 ? 100 LEU A N    1 
ATOM   796  C  CA   . LEU A 1 100 ? -5.612  -19.286 10.535  1.00 17.02 ? 100 LEU A CA   1 
ATOM   797  C  C    . LEU A 1 100 ? -6.739  -18.772 11.430  1.00 16.84 ? 100 LEU A C    1 
ATOM   798  O  O    . LEU A 1 100 ? -6.557  -17.770 12.142  1.00 16.61 ? 100 LEU A O    1 
ATOM   799  C  CB   . LEU A 1 100 ? -4.869  -20.316 11.416  1.00 19.66 ? 100 LEU A CB   1 
ATOM   800  C  CG   . LEU A 1 100 ? -3.506  -20.733 10.922  1.00 21.97 ? 100 LEU A CG   1 
ATOM   801  C  CD1  . LEU A 1 100 ? -2.490  -20.656 12.048  1.00 27.84 ? 100 LEU A CD1  1 
ATOM   802  C  CD2  . LEU A 1 100 ? -3.655  -22.119 10.268  1.00 29.43 ? 100 LEU A CD2  1 
ATOM   803  N  N    . ASP A 1 101 ? -7.856  -19.520 11.473  1.00 15.85 ? 101 ASP A N    1 
ATOM   804  C  CA   . ASP A 1 101 ? -9.007  -19.066 12.285  1.00 13.47 ? 101 ASP A CA   1 
ATOM   805  C  C    . ASP A 1 101 ? -8.740  -18.987 13.769  1.00 14.26 ? 101 ASP A C    1 
ATOM   806  O  O    . ASP A 1 101 ? -9.400  -18.232 14.492  1.00 13.68 ? 101 ASP A O    1 
ATOM   807  C  CB   . ASP A 1 101 ? -10.254 -19.928 12.046  1.00 12.91 ? 101 ASP A CB   1 
ATOM   808  C  CG   . ASP A 1 101 ? -10.732 -19.934 10.619  1.00 16.41 ? 101 ASP A CG   1 
ATOM   809  O  OD1  . ASP A 1 101 ? -10.383 -19.070 9.776   1.00 16.10 ? 101 ASP A OD1  1 
ATOM   810  O  OD2  . ASP A 1 101 ? -11.533 -20.841 10.361  1.00 16.74 ? 101 ASP A OD2  1 
ATOM   811  N  N    . GLY A 1 102 ? -7.754  -19.766 14.255  1.00 12.53 ? 102 GLY A N    1 
ATOM   812  C  CA   . GLY A 1 102 ? -7.480  -19.847 15.704  1.00 12.51 ? 102 GLY A CA   1 
ATOM   813  C  C    . GLY A 1 102 ? -6.677  -18.670 16.286  1.00 10.67 ? 102 GLY A C    1 
ATOM   814  O  O    . GLY A 1 102 ? -6.339  -18.656 17.445  1.00 13.09 ? 102 GLY A O    1 
ATOM   815  N  N    . GLN A 1 103 ? -6.365  -17.652 15.482  1.00 11.67 ? 103 GLN A N    1 
ATOM   816  C  CA   . GLN A 1 103 ? -5.688  -16.434 16.002  1.00 11.57 ? 103 GLN A CA   1 
ATOM   817  C  C    . GLN A 1 103 ? -6.025  -15.241 15.105  1.00 10.96 ? 103 GLN A C    1 
ATOM   818  O  O    . GLN A 1 103 ? -6.498  -15.439 14.018  1.00 11.26 ? 103 GLN A O    1 
ATOM   819  C  CB   . GLN A 1 103 ? -4.164  -16.655 16.021  1.00 11.13 ? 103 GLN A CB   1 
ATOM   820  C  CG   . GLN A 1 103 ? -3.491  -16.749 14.642  1.00 12.62 ? 103 GLN A CG   1 
ATOM   821  C  CD   . GLN A 1 103 ? -2.044  -17.289 14.762  1.00 14.28 ? 103 GLN A CD   1 
ATOM   822  O  OE1  . GLN A 1 103 ? -1.741  -18.079 15.649  0.50 9.97  ? 103 GLN A OE1  1 
ATOM   823  N  NE2  . GLN A 1 103 ? -1.165  -16.864 13.839  1.00 13.08 ? 103 GLN A NE2  1 
ATOM   824  N  N    . GLY A 1 104 ? -5.702  -14.020 15.534  1.00 9.76  ? 104 GLY A N    1 
ATOM   825  C  CA   . GLY A 1 104 ? -6.068  -12.849 14.746  1.00 9.16  ? 104 GLY A CA   1 
ATOM   826  C  C    . GLY A 1 104 ? -6.445  -11.662 15.594  1.00 9.63  ? 104 GLY A C    1 
ATOM   827  O  O    . GLY A 1 104 ? -6.095  -10.488 15.289  1.00 9.76  ? 104 GLY A O    1 
ATOM   828  N  N    . SER A 1 105 ? -7.157  -11.916 16.700  1.00 8.55  ? 105 SER A N    1 
ATOM   829  C  CA   . SER A 1 105 ? -7.501  -10.786 17.585  1.00 9.20  ? 105 SER A CA   1 
ATOM   830  C  C    . SER A 1 105 ? -6.300  -10.244 18.371  1.00 8.66  ? 105 SER A C    1 
ATOM   831  O  O    . SER A 1 105 ? -5.299  -10.906 18.586  1.00 9.20  ? 105 SER A O    1 
ATOM   832  C  CB   . SER A 1 105 ? -8.663  -11.148 18.556  1.00 8.48  ? 105 SER A CB   1 
ATOM   833  O  OG   . SER A 1 105 ? -8.234  -12.145 19.483  1.00 10.96 ? 105 SER A OG   1 
ATOM   834  N  N    . GLU A 1 106 ? -6.398  -8.952  18.719  1.00 7.41  ? 106 GLU A N    1 
ATOM   835  C  CA   . GLU A 1 106 ? -5.392  -8.304  19.549  1.00 8.38  ? 106 GLU A CA   1 
ATOM   836  C  C    . GLU A 1 106 ? -5.802  -8.463  21.040  1.00 9.31  ? 106 GLU A C    1 
ATOM   837  O  O    . GLU A 1 106 ? -5.061  -9.036  21.841  1.00 8.89  ? 106 GLU A O    1 
ATOM   838  C  CB   . GLU A 1 106 ? -5.308  -6.801  19.087  1.00 5.79  ? 106 GLU A CB   1 
ATOM   839  C  CG   . GLU A 1 106 ? -4.824  -6.683  17.615  1.00 8.73  ? 106 GLU A CG   1 
ATOM   840  C  CD   . GLU A 1 106 ? -4.225  -5.356  17.336  1.00 9.69  ? 106 GLU A CD   1 
ATOM   841  O  OE1  . GLU A 1 106 ? -4.910  -4.344  17.561  1.00 9.80  ? 106 GLU A OE1  1 
ATOM   842  O  OE2  . GLU A 1 106 ? -3.050  -5.355  16.913  1.00 10.10 ? 106 GLU A OE2  1 
ATOM   843  N  N    . HIS A 1 107 ? -7.002  -8.025  21.440  1.00 8.16  ? 107 HIS A N    1 
ATOM   844  C  CA   . HIS A 1 107 ? -7.437  -8.361  22.770  1.00 7.99  ? 107 HIS A CA   1 
ATOM   845  C  C    . HIS A 1 107 ? -7.768  -9.862  22.875  1.00 8.80  ? 107 HIS A C    1 
ATOM   846  O  O    . HIS A 1 107 ? -8.105  -10.487 21.863  1.00 8.79  ? 107 HIS A O    1 
ATOM   847  C  CB   . HIS A 1 107 ? -8.688  -7.532  23.147  1.00 9.40  ? 107 HIS A CB   1 
ATOM   848  C  CG   . HIS A 1 107 ? -8.384  -6.087  23.311  1.00 8.55  ? 107 HIS A CG   1 
ATOM   849  N  ND1  . HIS A 1 107 ? -8.336  -5.220  22.241  1.00 10.51 ? 107 HIS A ND1  1 
ATOM   850  C  CD2  . HIS A 1 107 ? -7.975  -5.388  24.402  1.00 11.51 ? 107 HIS A CD2  1 
ATOM   851  C  CE1  . HIS A 1 107 ? -7.954  -4.030  22.670  1.00 10.92 ? 107 HIS A CE1  1 
ATOM   852  N  NE2  . HIS A 1 107 ? -7.740  -4.110  23.982  1.00 8.95  ? 107 HIS A NE2  1 
ATOM   853  N  N    . THR A 1 108 ? -7.615  -10.432 24.054  1.00 9.97  ? 108 THR A N    1 
ATOM   854  C  CA   . THR A 1 108 ? -8.026  -11.834 24.262  1.00 11.22 ? 108 THR A CA   1 
ATOM   855  C  C    . THR A 1 108 ? -9.032  -11.850 25.444  1.00 11.60 ? 108 THR A C    1 
ATOM   856  O  O    . THR A 1 108 ? -9.105  -10.900 26.224  1.00 13.96 ? 108 THR A O    1 
ATOM   857  C  CB   . THR A 1 108 ? -6.819  -12.761 24.507  1.00 9.32  ? 108 THR A CB   1 
ATOM   858  O  OG1  . THR A 1 108 ? -5.987  -12.239 25.553  1.00 12.60 ? 108 THR A OG1  1 
ATOM   859  C  CG2  . THR A 1 108 ? -5.944  -12.844 23.181  1.00 8.01  ? 108 THR A CG2  1 
ATOM   860  N  N    . VAL A 1 109 ? -9.816  -12.915 25.554  1.00 12.24 ? 109 VAL A N    1 
ATOM   861  C  CA   . VAL A 1 109 ? -10.808 -13.000 26.681  1.00 11.96 ? 109 VAL A CA   1 
ATOM   862  C  C    . VAL A 1 109 ? -10.507 -14.320 27.384  1.00 11.71 ? 109 VAL A C    1 
ATOM   863  O  O    . VAL A 1 109 ? -10.640 -15.404 26.768  1.00 11.75 ? 109 VAL A O    1 
ATOM   864  C  CB   . VAL A 1 109 ? -12.233 -12.976 26.107  1.00 13.06 ? 109 VAL A CB   1 
ATOM   865  C  CG1  . VAL A 1 109 ? -13.280 -13.044 27.267  1.00 14.85 ? 109 VAL A CG1  1 
ATOM   866  C  CG2  . VAL A 1 109 ? -12.433 -11.721 25.201  1.00 11.90 ? 109 VAL A CG2  1 
ATOM   867  N  N    . ASP A 1 110 ? -10.029 -14.211 28.595  1.00 13.28 ? 110 ASP A N    1 
ATOM   868  C  CA   . ASP A 1 110 ? -9.491  -15.398 29.394  1.00 14.69 ? 110 ASP A CA   1 
ATOM   869  C  C    . ASP A 1 110 ? -8.585  -16.219 28.478  1.00 15.19 ? 110 ASP A C    1 
ATOM   870  O  O    . ASP A 1 110 ? -8.665  -17.477 28.415  1.00 14.68 ? 110 ASP A O    1 
ATOM   871  C  CB   . ASP A 1 110 ? -10.685 -16.253 29.973  1.00 14.80 ? 110 ASP A CB   1 
ATOM   872  C  CG   . ASP A 1 110 ? -11.643 -15.407 30.855  1.00 14.76 ? 110 ASP A CG   1 
ATOM   873  O  OD1  . ASP A 1 110 ? -11.145 -14.564 31.572  1.00 17.98 ? 110 ASP A OD1  1 
ATOM   874  O  OD2  . ASP A 1 110 ? -12.873 -15.592 30.757  1.00 20.43 ? 110 ASP A OD2  1 
ATOM   875  N  N    . LYS A 1 111 ? -7.678  -15.483 27.823  1.00 13.57 ? 111 LYS A N    1 
ATOM   876  C  CA   . LYS A 1 111 ? -6.605  -16.025 26.939  1.00 14.31 ? 111 LYS A CA   1 
ATOM   877  C  C    . LYS A 1 111 ? -7.146  -16.532 25.620  1.00 13.22 ? 111 LYS A C    1 
ATOM   878  O  O    . LYS A 1 111 ? -6.362  -16.963 24.783  1.00 12.28 ? 111 LYS A O    1 
ATOM   879  C  CB   . LYS A 1 111 ? -5.786  -17.110 27.663  1.00 16.03 ? 111 LYS A CB   1 
ATOM   880  C  CG   . LYS A 1 111 ? -5.243  -16.653 28.978  1.00 16.83 ? 111 LYS A CG   1 
ATOM   881  C  CD   . LYS A 1 111 ? -3.974  -15.931 28.602  1.00 19.43 ? 111 LYS A CD   1 
ATOM   882  C  CE   . LYS A 1 111 ? -3.372  -15.187 29.815  1.00 25.42 ? 111 LYS A CE   1 
ATOM   883  N  NZ   . LYS A 1 111 ? -1.950  -15.264 29.502  1.00 27.25 ? 111 LYS A NZ   1 
ATOM   884  N  N    . LYS A 1 112 ? -8.470  -16.459 25.391  1.00 13.18 ? 112 LYS A N    1 
ATOM   885  C  CA   . LYS A 1 112 ? -9.049  -16.919 24.097  1.00 14.52 ? 112 LYS A CA   1 
ATOM   886  C  C    . LYS A 1 112 ? -8.767  -15.870 22.982  1.00 13.75 ? 112 LYS A C    1 
ATOM   887  O  O    . LYS A 1 112 ? -9.009  -14.680 23.191  1.00 12.28 ? 112 LYS A O    1 
ATOM   888  C  CB   . LYS A 1 112 ? -10.560 -17.175 24.191  1.00 16.29 ? 112 LYS A CB   1 
ATOM   889  C  CG   . LYS A 1 112 ? -11.272 -17.398 22.808  1.00 15.81 ? 112 LYS A CG   1 
ATOM   890  C  CD   . LYS A 1 112 ? -12.839 -17.433 23.030  1.00 20.18 ? 112 LYS A CD   1 
ATOM   891  C  CE   . LYS A 1 112 ? -13.651 -17.592 21.669  1.00 24.87 ? 112 LYS A CE   1 
ATOM   892  N  NZ   . LYS A 1 112 ? -12.863 -18.311 20.675  1.00 25.59 ? 112 LYS A NZ   1 
ATOM   893  N  N    . LYS A 1 113 ? -8.199  -16.336 21.876  1.00 11.62 ? 113 LYS A N    1 
ATOM   894  C  CA   A LYS A 1 113 ? -7.975  -15.509 20.643  0.50 11.81 ? 113 LYS A CA   1 
ATOM   895  C  CA   B LYS A 1 113 ? -7.971  -15.498 20.661  0.50 11.55 ? 113 LYS A CA   1 
ATOM   896  C  C    . LYS A 1 113 ? -9.119  -15.747 19.662  1.00 11.54 ? 113 LYS A C    1 
ATOM   897  O  O    . LYS A 1 113 ? -9.490  -16.904 19.394  1.00 12.02 ? 113 LYS A O    1 
ATOM   898  C  CB   A LYS A 1 113 ? -6.682  -15.898 19.913  0.50 9.74  ? 113 LYS A CB   1 
ATOM   899  C  CB   B LYS A 1 113 ? -6.597  -15.796 20.011  0.50 9.87  ? 113 LYS A CB   1 
ATOM   900  C  CG   A LYS A 1 113 ? -5.401  -15.654 20.666  0.50 12.49 ? 113 LYS A CG   1 
ATOM   901  C  CG   B LYS A 1 113 ? -5.369  -15.338 20.869  0.50 10.14 ? 113 LYS A CG   1 
ATOM   902  C  CD   A LYS A 1 113 ? -4.238  -16.300 19.866  0.50 11.01 ? 113 LYS A CD   1 
ATOM   903  C  CD   B LYS A 1 113 ? -4.056  -16.066 20.432  0.50 11.31 ? 113 LYS A CD   1 
ATOM   904  C  CE   A LYS A 1 113 ? -2.898  -15.786 20.318  0.50 10.61 ? 113 LYS A CE   1 
ATOM   905  C  CE   B LYS A 1 113 ? -2.798  -15.370 20.947  0.50 11.67 ? 113 LYS A CE   1 
ATOM   906  N  NZ   A LYS A 1 113 ? -2.464  -16.374 21.627  0.50 6.55  ? 113 LYS A NZ   1 
ATOM   907  N  NZ   B LYS A 1 113 ? -1.526  -16.158 20.591  0.50 9.13  ? 113 LYS A NZ   1 
ATOM   908  N  N    . TYR A 1 114 ? -9.672  -14.674 19.106  1.00 9.84  ? 114 TYR A N    1 
ATOM   909  C  CA   . TYR A 1 114 ? -10.713 -14.750 18.099  1.00 10.29 ? 114 TYR A CA   1 
ATOM   910  C  C    . TYR A 1 114 ? -10.069 -14.669 16.718  1.00 10.02 ? 114 TYR A C    1 
ATOM   911  O  O    . TYR A 1 114 ? -8.854  -14.371 16.644  1.00 10.85 ? 114 TYR A O    1 
ATOM   912  C  CB   . TYR A 1 114 ? -11.701 -13.578 18.284  1.00 9.45  ? 114 TYR A CB   1 
ATOM   913  C  CG   . TYR A 1 114 ? -12.706 -13.817 19.396  1.00 13.20 ? 114 TYR A CG   1 
ATOM   914  C  CD1  . TYR A 1 114 ? -13.901 -14.491 19.131  1.00 14.93 ? 114 TYR A CD1  1 
ATOM   915  C  CD2  . TYR A 1 114 ? -12.455 -13.420 20.727  1.00 13.12 ? 114 TYR A CD2  1 
ATOM   916  C  CE1  . TYR A 1 114 ? -14.845 -14.705 20.166  1.00 17.34 ? 114 TYR A CE1  1 
ATOM   917  C  CE2  . TYR A 1 114 ? -13.371 -13.693 21.747  1.00 15.81 ? 114 TYR A CE2  1 
ATOM   918  C  CZ   . TYR A 1 114 ? -14.566 -14.313 21.441  1.00 18.14 ? 114 TYR A CZ   1 
ATOM   919  O  OH   . TYR A 1 114 ? -15.499 -14.522 22.449  1.00 17.40 ? 114 TYR A OH   1 
ATOM   920  N  N    . ALA A 1 115 ? -10.809 -15.015 15.649  1.00 10.62 ? 115 ALA A N    1 
ATOM   921  C  CA   . ALA A 1 115 ? -10.273 -15.049 14.267  1.00 10.50 ? 115 ALA A CA   1 
ATOM   922  C  C    . ALA A 1 115 ? -9.814  -13.629 13.816  1.00 10.84 ? 115 ALA A C    1 
ATOM   923  O  O    . ALA A 1 115 ? -8.959  -13.455 12.916  1.00 10.49 ? 115 ALA A O    1 
ATOM   924  C  CB   . ALA A 1 115 ? -11.342 -15.592 13.301  1.00 12.87 ? 115 ALA A CB   1 
ATOM   925  N  N    . ALA A 1 116 ? -10.494 -12.613 14.340  1.00 9.94  ? 116 ALA A N    1 
ATOM   926  C  CA   . ALA A 1 116 ? -10.216 -11.253 13.912  1.00 9.47  ? 116 ALA A CA   1 
ATOM   927  C  C    . ALA A 1 116 ? -10.771 -10.238 14.941  1.00 9.06  ? 116 ALA A C    1 
ATOM   928  O  O    . ALA A 1 116 ? -11.438 -10.633 15.908  1.00 9.19  ? 116 ALA A O    1 
ATOM   929  C  CB   . ALA A 1 116 ? -10.719 -10.981 12.496  1.00 8.67  ? 116 ALA A CB   1 
ATOM   930  N  N    . GLU A 1 117 ? -10.421 -8.952  14.772  1.00 10.80 ? 117 GLU A N    1 
ATOM   931  C  CA   . GLU A 1 117 ? -10.977 -7.923  15.649  1.00 8.86  ? 117 GLU A CA   1 
ATOM   932  C  C    . GLU A 1 117 ? -11.131 -6.661  14.843  1.00 10.32 ? 117 GLU A C    1 
ATOM   933  O  O    . GLU A 1 117 ? -10.257 -6.266  14.112  1.00 9.70  ? 117 GLU A O    1 
ATOM   934  C  CB   . GLU A 1 117 ? -9.999  -7.699  16.835  1.00 11.01 ? 117 GLU A CB   1 
ATOM   935  C  CG   . GLU A 1 117 ? -10.511 -6.678  17.970  1.00 7.13  ? 117 GLU A CG   1 
ATOM   936  C  CD   . GLU A 1 117 ? -9.552  -6.648  19.168  1.00 11.01 ? 117 GLU A CD   1 
ATOM   937  O  OE1  . GLU A 1 117 ? -8.835  -7.696  19.444  1.00 9.85  ? 117 GLU A OE1  1 
ATOM   938  O  OE2  . GLU A 1 117 ? -9.530  -5.595  19.846  1.00 11.62 ? 117 GLU A OE2  1 
ATOM   939  N  N    . LEU A 1 118 ? -12.296 -6.062  15.014  1.00 9.87  ? 118 LEU A N    1 
ATOM   940  C  CA   . LEU A 1 118 ? -12.701 -4.795  14.380  1.00 8.20  ? 118 LEU A CA   1 
ATOM   941  C  C    . LEU A 1 118 ? -12.485 -3.636  15.328  1.00 6.95  ? 118 LEU A C    1 
ATOM   942  O  O    . LEU A 1 118 ? -12.894 -3.673  16.492  1.00 7.80  ? 118 LEU A O    1 
ATOM   943  C  CB   . LEU A 1 118 ? -14.180 -4.901  13.897  1.00 7.69  ? 118 LEU A CB   1 
ATOM   944  C  CG   . LEU A 1 118 ? -14.962 -3.595  13.599  1.00 11.45 ? 118 LEU A CG   1 
ATOM   945  C  CD1  . LEU A 1 118 ? -14.456 -2.938  12.285  1.00 12.33 ? 118 LEU A CD1  1 
ATOM   946  C  CD2  . LEU A 1 118 ? -16.534 -3.994  13.507  1.00 9.10  ? 118 LEU A CD2  1 
ATOM   947  N  N    . HIS A 1 119 ? -11.879 -2.552  14.782  1.00 6.37  ? 119 HIS A N    1 
ATOM   948  C  CA   . HIS A 1 119 ? -11.603 -1.339  15.538  1.00 8.04  ? 119 HIS A CA   1 
ATOM   949  C  C    . HIS A 1 119 ? -12.305 -0.166  14.878  1.00 8.78  ? 119 HIS A C    1 
ATOM   950  O  O    . HIS A 1 119 ? -11.961 0.193   13.714  1.00 9.62  ? 119 HIS A O    1 
ATOM   951  C  CB   . HIS A 1 119 ? -10.062 -1.154  15.662  1.00 7.83  ? 119 HIS A CB   1 
ATOM   952  C  CG   . HIS A 1 119 ? -9.423  -2.117  16.616  1.00 7.70  ? 119 HIS A CG   1 
ATOM   953  N  ND1  . HIS A 1 119 ? -8.072  -2.430  16.601  1.00 9.04  ? 119 HIS A ND1  1 
ATOM   954  C  CD2  . HIS A 1 119 ? -9.961  -2.876  17.595  1.00 5.16  ? 119 HIS A CD2  1 
ATOM   955  C  CE1  . HIS A 1 119 ? -7.805  -3.304  17.566  1.00 6.68  ? 119 HIS A CE1  1 
ATOM   956  N  NE2  . HIS A 1 119 ? -8.948  -3.628  18.139  1.00 8.79  ? 119 HIS A NE2  1 
ATOM   957  N  N    . LEU A 1 120 ? -13.310 0.382   15.581  1.00 8.49  ? 120 LEU A N    1 
ATOM   958  C  CA   . LEU A 1 120 ? -14.020 1.586   15.116  1.00 7.82  ? 120 LEU A CA   1 
ATOM   959  C  C    . LEU A 1 120 ? -13.405 2.731   15.957  1.00 6.67  ? 120 LEU A C    1 
ATOM   960  O  O    . LEU A 1 120 ? -13.553 2.776   17.190  1.00 8.12  ? 120 LEU A O    1 
ATOM   961  C  CB   . LEU A 1 120 ? -15.511 1.453   15.327  1.00 8.64  ? 120 LEU A CB   1 
ATOM   962  C  CG   . LEU A 1 120 ? -16.105 0.399   14.339  1.00 10.76 ? 120 LEU A CG   1 
ATOM   963  C  CD1  . LEU A 1 120 ? -16.939 -0.512  15.189  1.00 14.56 ? 120 LEU A CD1  1 
ATOM   964  C  CD2  . LEU A 1 120 ? -16.910 1.119   13.274  1.00 12.35 ? 120 LEU A CD2  1 
ATOM   965  N  N    . VAL A 1 121 ? -12.610 3.510   15.262  1.00 8.90  ? 121 VAL A N    1 
ATOM   966  C  CA   . VAL A 1 121 ? -11.752 4.612   15.824  1.00 9.94  ? 121 VAL A CA   1 
ATOM   967  C  C    . VAL A 1 121 ? -12.504 5.964   15.868  1.00 10.16 ? 121 VAL A C    1 
ATOM   968  O  O    . VAL A 1 121 ? -12.899 6.463   14.820  1.00 9.68  ? 121 VAL A O    1 
ATOM   969  C  CB   . VAL A 1 121 ? -10.434 4.766   15.004  1.00 10.68 ? 121 VAL A CB   1 
ATOM   970  C  CG1  . VAL A 1 121 ? -9.484  5.884   15.604  1.00 10.80 ? 121 VAL A CG1  1 
ATOM   971  C  CG2  . VAL A 1 121 ? -9.665  3.424   14.896  1.00 8.55  ? 121 VAL A CG2  1 
ATOM   972  N  N    . HIS A 1 122 ? -12.573 6.577   17.065  1.00 9.26  ? 122 HIS A N    1 
ATOM   973  C  CA   . HIS A 1 122 ? -13.289 7.859   17.243  1.00 9.94  ? 122 HIS A CA   1 
ATOM   974  C  C    . HIS A 1 122 ? -12.363 8.814   17.959  1.00 9.84  ? 122 HIS A C    1 
ATOM   975  O  O    . HIS A 1 122 ? -11.607 8.409   18.844  1.00 10.30 ? 122 HIS A O    1 
ATOM   976  C  CB   . HIS A 1 122 ? -14.626 7.710   18.054  1.00 9.81  ? 122 HIS A CB   1 
ATOM   977  C  CG   . HIS A 1 122 ? -15.495 6.533   17.683  1.00 9.24  ? 122 HIS A CG   1 
ATOM   978  N  ND1  . HIS A 1 122 ? -15.130 5.225   17.892  1.00 10.35 ? 122 HIS A ND1  1 
ATOM   979  C  CD2  . HIS A 1 122 ? -16.742 6.489   17.122  1.00 12.38 ? 122 HIS A CD2  1 
ATOM   980  C  CE1  . HIS A 1 122 ? -16.116 4.416   17.526  1.00 11.40 ? 122 HIS A CE1  1 
ATOM   981  N  NE2  . HIS A 1 122 ? -17.099 5.151   17.003  1.00 9.02  ? 122 HIS A NE2  1 
ATOM   982  N  N    . TRP A 1 123 ? -12.462 10.102  17.639  1.00 11.14 ? 123 TRP A N    1 
ATOM   983  C  CA   . TRP A 1 123 ? -11.672 11.140  18.341  1.00 11.42 ? 123 TRP A CA   1 
ATOM   984  C  C    . TRP A 1 123 ? -12.521 12.167  19.108  1.00 11.94 ? 123 TRP A C    1 
ATOM   985  O  O    . TRP A 1 123 ? -13.607 12.555  18.660  1.00 10.84 ? 123 TRP A O    1 
ATOM   986  C  CB   . TRP A 1 123 ? -10.700 11.820  17.410  1.00 12.11 ? 123 TRP A CB   1 
ATOM   987  C  CG   . TRP A 1 123 ? -11.324 12.432  16.109  1.00 14.41 ? 123 TRP A CG   1 
ATOM   988  C  CD1  . TRP A 1 123 ? -11.486 11.804  14.878  1.00 14.33 ? 123 TRP A CD1  1 
ATOM   989  C  CD2  . TRP A 1 123 ? -11.843 13.753  15.966  1.00 15.31 ? 123 TRP A CD2  1 
ATOM   990  N  NE1  . TRP A 1 123 ? -12.106 12.674  13.984  1.00 16.77 ? 123 TRP A NE1  1 
ATOM   991  C  CE2  . TRP A 1 123 ? -12.308 13.889  14.620  1.00 17.14 ? 123 TRP A CE2  1 
ATOM   992  C  CE3  . TRP A 1 123 ? -11.938 14.857  16.845  1.00 14.12 ? 123 TRP A CE3  1 
ATOM   993  C  CZ2  . TRP A 1 123 ? -12.911 15.099  14.138  1.00 16.57 ? 123 TRP A CZ2  1 
ATOM   994  C  CZ3  . TRP A 1 123 ? -12.516 16.036  16.396  1.00 14.12 ? 123 TRP A CZ3  1 
ATOM   995  C  CH2  . TRP A 1 123 ? -12.993 16.166  15.019  1.00 15.25 ? 123 TRP A CH2  1 
ATOM   996  N  N    . ASN A 1 124 ? -12.002 12.613  20.252  1.00 13.53 ? 124 ASN A N    1 
ATOM   997  C  CA   . ASN A 1 124 ? -12.687 13.506  21.177  1.00 13.46 ? 124 ASN A CA   1 
ATOM   998  C  C    . ASN A 1 124 ? -12.907 14.873  20.492  1.00 14.45 ? 124 ASN A C    1 
ATOM   999  O  O    . ASN A 1 124 ? -11.913 15.596  20.123  1.00 12.12 ? 124 ASN A O    1 
ATOM   1000 C  CB   . ASN A 1 124 ? -11.828 13.600  22.454  1.00 13.28 ? 124 ASN A CB   1 
ATOM   1001 C  CG   . ASN A 1 124 ? -12.608 14.144  23.644  1.00 17.35 ? 124 ASN A CG   1 
ATOM   1002 O  OD1  . ASN A 1 124 ? -13.453 15.022  23.467  1.00 14.20 ? 124 ASN A OD1  1 
ATOM   1003 N  ND2  . ASN A 1 124 ? -12.281 13.663  24.869  1.00 17.90 ? 124 ASN A ND2  1 
ATOM   1004 N  N    . THR A 1 125 ? -14.197 15.295  20.376  1.00 15.72 ? 125 THR A N    1 
ATOM   1005 C  CA   . THR A 1 125 ? -14.519 16.532  19.596  1.00 17.45 ? 125 THR A CA   1 
ATOM   1006 C  C    . THR A 1 125 ? -13.956 17.749  20.375  1.00 18.57 ? 125 THR A C    1 
ATOM   1007 O  O    . THR A 1 125 ? -13.653 18.806  19.828  1.00 19.48 ? 125 THR A O    1 
ATOM   1008 C  CB   . THR A 1 125 ? -16.027 16.718  19.408  1.00 18.45 ? 125 THR A CB   1 
ATOM   1009 O  OG1  . THR A 1 125 ? -16.669 16.708  20.697  1.00 19.66 ? 125 THR A OG1  1 
ATOM   1010 C  CG2  . THR A 1 125 ? -16.560 15.535  18.656  1.00 16.50 ? 125 THR A CG2  1 
ATOM   1011 N  N    . LYS A 1 126 ? -13.487 17.697  21.765  1.00 18.72 ? 127 LYS A N    1 
ATOM   1012 C  CA   . LYS A 1 126 ? -12.885 18.871  22.376  1.00 20.84 ? 127 LYS A CA   1 
ATOM   1013 C  C    . LYS A 1 126 ? -11.513 19.220  21.779  1.00 20.81 ? 127 LYS A C    1 
ATOM   1014 O  O    . LYS A 1 126 ? -11.018 20.313  22.038  1.00 22.32 ? 127 LYS A O    1 
ATOM   1015 C  CB   . LYS A 1 126 ? -12.764 18.635  23.895  1.00 21.55 ? 127 LYS A CB   1 
ATOM   1016 C  CG   . LYS A 1 126 ? -11.761 17.632  24.310  1.00 24.96 ? 127 LYS A CG   1 
ATOM   1017 C  CD   . LYS A 1 126 ? -11.316 17.888  25.752  1.00 32.59 ? 127 LYS A CD   1 
ATOM   1018 C  CE   . LYS A 1 126 ? -12.083 17.090  26.749  1.00 32.47 ? 127 LYS A CE   1 
ATOM   1019 N  NZ   . LYS A 1 126 ? -11.288 17.002  28.027  1.00 37.59 ? 127 LYS A NZ   1 
ATOM   1020 N  N    . TYR A 1 127 ? -10.891 18.286  21.026  1.00 18.46 ? 128 TYR A N    1 
ATOM   1021 C  CA   . TYR A 1 127 ? -9.535  18.507  20.446  1.00 18.32 ? 128 TYR A CA   1 
ATOM   1022 C  C    . TYR A 1 127 ? -9.540  18.884  18.963  1.00 17.83 ? 128 TYR A C    1 
ATOM   1023 O  O    . TYR A 1 127 ? -8.469  19.075  18.362  1.00 18.77 ? 128 TYR A O    1 
ATOM   1024 C  CB   . TYR A 1 127 ? -8.614  17.296  20.724  1.00 17.83 ? 128 TYR A CB   1 
ATOM   1025 C  CG   . TYR A 1 127 ? -8.516  17.007  22.235  1.00 16.70 ? 128 TYR A CG   1 
ATOM   1026 C  CD1  . TYR A 1 127 ? -8.170  18.035  23.149  1.00 16.85 ? 128 TYR A CD1  1 
ATOM   1027 C  CD2  . TYR A 1 127 ? -8.766  15.734  22.747  1.00 13.93 ? 128 TYR A CD2  1 
ATOM   1028 C  CE1  . TYR A 1 127 ? -8.086  17.800  24.508  1.00 17.50 ? 128 TYR A CE1  1 
ATOM   1029 C  CE2  . TYR A 1 127 ? -8.705  15.478  24.108  1.00 16.23 ? 128 TYR A CE2  1 
ATOM   1030 C  CZ   . TYR A 1 127 ? -8.349  16.559  24.984  1.00 16.06 ? 128 TYR A CZ   1 
ATOM   1031 O  OH   . TYR A 1 127 ? -8.250  16.366  26.338  1.00 18.30 ? 128 TYR A OH   1 
ATOM   1032 N  N    . GLY A 1 128 ? -10.742 18.985  18.393  1.00 15.98 ? 129 GLY A N    1 
ATOM   1033 C  CA   . GLY A 1 128 ? -10.969 19.582  17.066  1.00 17.79 ? 129 GLY A CA   1 
ATOM   1034 C  C    . GLY A 1 128 ? -10.586 18.711  15.846  1.00 17.97 ? 129 GLY A C    1 
ATOM   1035 O  O    . GLY A 1 128 ? -11.195 18.818  14.782  1.00 18.68 ? 129 GLY A O    1 
ATOM   1036 N  N    . ASP A 1 129 ? -9.577  17.849  15.961  1.00 17.82 ? 130 ASP A N    1 
ATOM   1037 C  CA   . ASP A 1 129 ? -9.383  16.804  14.949  1.00 18.39 ? 130 ASP A CA   1 
ATOM   1038 C  C    . ASP A 1 129 ? -8.580  15.605  15.469  1.00 20.16 ? 130 ASP A C    1 
ATOM   1039 O  O    . ASP A 1 129 ? -8.150  15.599  16.612  1.00 17.65 ? 130 ASP A O    1 
ATOM   1040 C  CB   . ASP A 1 129 ? -8.703  17.344  13.674  1.00 20.10 ? 130 ASP A CB   1 
ATOM   1041 C  CG   . ASP A 1 129 ? -7.334  17.968  13.919  1.00 20.37 ? 130 ASP A CG   1 
ATOM   1042 O  OD1  . ASP A 1 129 ? -6.743  17.871  14.999  1.00 27.95 ? 130 ASP A OD1  1 
ATOM   1043 O  OD2  . ASP A 1 129 ? -6.741  18.511  12.956  1.00 19.90 ? 130 ASP A OD2  1 
ATOM   1044 N  N    . PHE A 1 130 ? -8.398  14.595  14.606  1.00 18.90 ? 131 PHE A N    1 
ATOM   1045 C  CA   . PHE A 1 130 ? -7.681  13.374  15.009  1.00 19.09 ? 131 PHE A CA   1 
ATOM   1046 C  C    . PHE A 1 130 ? -6.210  13.652  15.393  1.00 17.56 ? 131 PHE A C    1 
ATOM   1047 O  O    . PHE A 1 130 ? -5.722  13.164  16.400  1.00 15.29 ? 131 PHE A O    1 
ATOM   1048 C  CB   . PHE A 1 130 ? -7.768  12.339  13.877  1.00 16.40 ? 131 PHE A CB   1 
ATOM   1049 C  CG   . PHE A 1 130 ? -6.998  11.083  14.142  1.00 15.95 ? 131 PHE A CG   1 
ATOM   1050 C  CD1  . PHE A 1 130 ? -7.596  10.021  14.871  1.00 12.58 ? 131 PHE A CD1  1 
ATOM   1051 C  CD2  . PHE A 1 130 ? -5.690  10.929  13.674  1.00 16.28 ? 131 PHE A CD2  1 
ATOM   1052 C  CE1  . PHE A 1 130 ? -6.871  8.856   15.134  1.00 13.93 ? 131 PHE A CE1  1 
ATOM   1053 C  CE2  . PHE A 1 130 ? -4.967  9.778   13.915  1.00 16.89 ? 131 PHE A CE2  1 
ATOM   1054 C  CZ   . PHE A 1 130 ? -5.547  8.739   14.623  1.00 18.91 ? 131 PHE A CZ   1 
ATOM   1055 N  N    . GLY A 1 131 ? -5.499  14.414  14.545  1.00 17.55 ? 132 GLY A N    1 
ATOM   1056 C  CA   . GLY A 1 131 ? -4.089  14.678  14.810  1.00 17.11 ? 132 GLY A CA   1 
ATOM   1057 C  C    . GLY A 1 131 ? -3.775  15.328  16.128  1.00 17.10 ? 132 GLY A C    1 
ATOM   1058 O  O    . GLY A 1 131 ? -2.756  15.060  16.749  1.00 17.73 ? 132 GLY A O    1 
ATOM   1059 N  N    . LYS A 1 132 ? -4.643  16.222  16.550  1.00 17.55 ? 133 LYS A N    1 
ATOM   1060 C  CA   . LYS A 1 132 ? -4.460  16.865  17.882  1.00 16.49 ? 133 LYS A CA   1 
ATOM   1061 C  C    . LYS A 1 132 ? -4.906  15.934  19.004  1.00 16.24 ? 133 LYS A C    1 
ATOM   1062 O  O    . LYS A 1 132 ? -4.303  15.903  20.073  1.00 14.67 ? 133 LYS A O    1 
ATOM   1063 C  CB   . LYS A 1 132 ? -5.103  18.249  17.922  1.00 17.69 ? 133 LYS A CB   1 
ATOM   1064 C  CG   . LYS A 1 132 ? -4.396  19.303  16.947  1.00 20.12 ? 133 LYS A CG   1 
ATOM   1065 C  CD   . LYS A 1 132 ? -2.974  19.631  17.385  0.01 18.98 ? 133 LYS A CD   1 
ATOM   1066 C  CE   . LYS A 1 132 ? -2.230  20.402  16.307  0.01 18.62 ? 133 LYS A CE   1 
ATOM   1067 N  NZ   . LYS A 1 132 ? -0.798  20.607  16.658  0.01 18.62 ? 133 LYS A NZ   1 
ATOM   1068 N  N    . ALA A 1 133 ? -5.980  15.192  18.766  1.00 15.42 ? 134 ALA A N    1 
ATOM   1069 C  CA   . ALA A 1 133 ? -6.490  14.224  19.760  1.00 15.05 ? 134 ALA A CA   1 
ATOM   1070 C  C    . ALA A 1 133 ? -5.454  13.182  20.186  1.00 14.31 ? 134 ALA A C    1 
ATOM   1071 O  O    . ALA A 1 133 ? -5.415  12.789  21.384  1.00 14.35 ? 134 ALA A O    1 
ATOM   1072 C  CB   . ALA A 1 133 ? -7.831  13.509  19.252  1.00 13.81 ? 134 ALA A CB   1 
ATOM   1073 N  N    . VAL A 1 134 ? -4.727  12.600  19.224  1.00 14.07 ? 135 VAL A N    1 
ATOM   1074 C  CA   . VAL A 1 134 ? -3.751  11.496  19.591  1.00 15.83 ? 135 VAL A CA   1 
ATOM   1075 C  C    . VAL A 1 134 ? -2.651  11.939  20.523  1.00 16.66 ? 135 VAL A C    1 
ATOM   1076 O  O    . VAL A 1 134 ? -1.963  11.123  21.148  1.00 17.08 ? 135 VAL A O    1 
ATOM   1077 C  CB   . VAL A 1 134 ? -3.164  10.755  18.339  1.00 16.42 ? 135 VAL A CB   1 
ATOM   1078 C  CG1  . VAL A 1 134 ? -4.306  10.112  17.598  1.00 14.98 ? 135 VAL A CG1  1 
ATOM   1079 C  CG2  . VAL A 1 134 ? -2.260  11.686  17.496  1.00 15.43 ? 135 VAL A CG2  1 
ATOM   1080 N  N    A GLN A 1 135 ? -2.555  13.261  20.671  0.50 16.35 ? 136 GLN A N    1 
ATOM   1081 N  N    B GLN A 1 135 ? -2.494  13.252  20.673  0.50 16.80 ? 136 GLN A N    1 
ATOM   1082 C  CA   A GLN A 1 135 ? -1.556  13.869  21.524  0.50 16.96 ? 136 GLN A CA   1 
ATOM   1083 C  CA   B GLN A 1 135 ? -1.468  13.732  21.582  0.50 17.38 ? 136 GLN A CA   1 
ATOM   1084 C  C    A GLN A 1 135 ? -2.141  14.111  22.939  0.50 17.10 ? 136 GLN A C    1 
ATOM   1085 C  C    B GLN A 1 135 ? -2.076  13.957  22.996  0.50 17.45 ? 136 GLN A C    1 
ATOM   1086 O  O    A GLN A 1 135 ? -1.526  14.757  23.822  0.50 17.69 ? 136 GLN A O    1 
ATOM   1087 O  O    B GLN A 1 135 ? -1.415  14.444  23.936  0.50 18.12 ? 136 GLN A O    1 
ATOM   1088 C  CB   A GLN A 1 135 ? -1.092  15.178  20.857  0.50 16.24 ? 136 GLN A CB   1 
ATOM   1089 C  CB   B GLN A 1 135 ? -0.790  14.998  21.002  0.50 17.78 ? 136 GLN A CB   1 
ATOM   1090 C  CG   A GLN A 1 135 ? -0.550  14.998  19.431  0.50 18.63 ? 136 GLN A CG   1 
ATOM   1091 C  CG   B GLN A 1 135 ? -0.133  14.868  19.586  0.50 21.15 ? 136 GLN A CG   1 
ATOM   1092 C  CD   A GLN A 1 135 ? -0.166  16.295  18.753  0.50 17.64 ? 136 GLN A CD   1 
ATOM   1093 C  CD   B GLN A 1 135 ? 0.980   13.799  19.479  0.50 24.67 ? 136 GLN A CD   1 
ATOM   1094 O  OE1  A GLN A 1 135 ? -0.079  16.365  17.525  0.50 23.60 ? 136 GLN A OE1  1 
ATOM   1095 O  OE1  B GLN A 1 135 ? 1.775   13.582  20.407  0.50 28.07 ? 136 GLN A OE1  1 
ATOM   1096 N  NE2  A GLN A 1 135 ? 0.079   17.328  19.542  0.50 22.05 ? 136 GLN A NE2  1 
ATOM   1097 N  NE2  B GLN A 1 135 ? 1.043   13.155  18.337  0.50 23.24 ? 136 GLN A NE2  1 
ATOM   1098 N  N    . GLN A 1 136 ? -3.345  13.610  23.170  1.00 16.13 ? 137 GLN A N    1 
ATOM   1099 C  CA   . GLN A 1 136 ? -3.959  13.741  24.515  1.00 15.61 ? 137 GLN A CA   1 
ATOM   1100 C  C    . GLN A 1 136 ? -4.382  12.429  25.187  1.00 15.18 ? 137 GLN A C    1 
ATOM   1101 O  O    . GLN A 1 136 ? -4.712  11.460  24.502  1.00 15.71 ? 137 GLN A O    1 
ATOM   1102 C  CB   . GLN A 1 136 ? -5.187  14.638  24.398  1.00 15.41 ? 137 GLN A CB   1 
ATOM   1103 C  CG   . GLN A 1 136 ? -5.117  15.786  23.389  1.00 20.42 ? 137 GLN A CG   1 
ATOM   1104 C  CD   . GLN A 1 136 ? -4.087  16.856  23.781  1.00 28.61 ? 137 GLN A CD   1 
ATOM   1105 O  OE1  . GLN A 1 136 ? -3.360  17.423  22.918  1.00 32.45 ? 137 GLN A OE1  1 
ATOM   1106 N  NE2  . GLN A 1 136 ? -3.998  17.107  25.071  1.00 23.50 ? 137 GLN A NE2  1 
ATOM   1107 N  N    . PRO A 1 137 ? -4.417  12.371  26.560  1.00 14.75 ? 138 PRO A N    1 
ATOM   1108 C  CA   . PRO A 1 137 ? -4.577  11.078  27.263  1.00 14.93 ? 138 PRO A CA   1 
ATOM   1109 C  C    . PRO A 1 137 ? -6.013  10.572  27.114  1.00 13.82 ? 138 PRO A C    1 
ATOM   1110 O  O    . PRO A 1 137 ? -6.274  9.369   27.260  1.00 13.62 ? 138 PRO A O    1 
ATOM   1111 C  CB   . PRO A 1 137 ? -4.215  11.407  28.727  1.00 16.05 ? 138 PRO A CB   1 
ATOM   1112 C  CG   . PRO A 1 137 ? -4.584  12.910  28.849  1.00 15.41 ? 138 PRO A CG   1 
ATOM   1113 C  CD   . PRO A 1 137 ? -4.230  13.505  27.493  1.00 16.76 ? 138 PRO A CD   1 
ATOM   1114 N  N    . ASP A 1 138 ? -6.951  11.473  26.809  1.00 11.97 ? 139 ASP A N    1 
ATOM   1115 C  CA   . ASP A 1 138 ? -8.293  11.057  26.487  1.00 14.08 ? 139 ASP A CA   1 
ATOM   1116 C  C    . ASP A 1 138 ? -8.694  11.455  25.041  1.00 12.32 ? 139 ASP A C    1 
ATOM   1117 O  O    . ASP A 1 138 ? -9.834  11.861  24.802  1.00 13.27 ? 139 ASP A O    1 
ATOM   1118 C  CB   . ASP A 1 138 ? -9.298  11.688  27.450  1.00 14.76 ? 139 ASP A CB   1 
ATOM   1119 C  CG   . ASP A 1 138 ? -9.193  13.176  27.513  1.00 16.04 ? 139 ASP A CG   1 
ATOM   1120 O  OD1  . ASP A 1 138 ? -8.196  13.791  26.974  1.00 19.93 ? 139 ASP A OD1  1 
ATOM   1121 O  OD2  . ASP A 1 138 ? -10.118 13.767  28.122  1.00 17.97 ? 139 ASP A OD2  1 
ATOM   1122 N  N    . GLY A 1 139 ? -7.743  11.373  24.122  1.00 13.07 ? 140 GLY A N    1 
ATOM   1123 C  CA   . GLY A 1 139 ? -8.005  11.815  22.768  1.00 10.68 ? 140 GLY A CA   1 
ATOM   1124 C  C    . GLY A 1 139 ? -8.914  10.896  21.921  1.00 9.89  ? 140 GLY A C    1 
ATOM   1125 O  O    . GLY A 1 139 ? -9.631  11.402  21.069  1.00 9.89  ? 140 GLY A O    1 
ATOM   1126 N  N    . LEU A 1 140 ? -8.821  9.581   22.141  1.00 7.55  ? 141 LEU A N    1 
ATOM   1127 C  CA   . LEU A 1 140 ? -9.514  8.609   21.295  1.00 8.14  ? 141 LEU A CA   1 
ATOM   1128 C  C    . LEU A 1 140 ? -10.401 7.652   22.146  1.00 9.65  ? 141 LEU A C    1 
ATOM   1129 O  O    . LEU A 1 140 ? -10.118 7.389   23.336  1.00 9.18  ? 141 LEU A O    1 
ATOM   1130 C  CB   . LEU A 1 140 ? -8.531  7.733   20.501  1.00 9.75  ? 141 LEU A CB   1 
ATOM   1131 C  CG   . LEU A 1 140 ? -7.550  8.472   19.554  1.00 10.65 ? 141 LEU A CG   1 
ATOM   1132 C  CD1  . LEU A 1 140 ? -6.850  7.446   18.671  1.00 13.55 ? 141 LEU A CD1  1 
ATOM   1133 C  CD2  . LEU A 1 140 ? -8.219  9.524   18.557  1.00 12.71 ? 141 LEU A CD2  1 
ATOM   1134 N  N    . ALA A 1 141 ? -11.469 7.173   21.502  1.00 11.20 ? 142 ALA A N    1 
ATOM   1135 C  CA   . ALA A 1 141 ? -12.305 6.052   22.012  1.00 9.95  ? 142 ALA A CA   1 
ATOM   1136 C  C    . ALA A 1 141 ? -12.351 5.027   20.885  1.00 10.30 ? 142 ALA A C    1 
ATOM   1137 O  O    . ALA A 1 141 ? -12.715 5.389   19.740  1.00 10.72 ? 142 ALA A O    1 
ATOM   1138 C  CB   . ALA A 1 141 ? -13.720 6.531   22.394  1.00 10.60 ? 142 ALA A CB   1 
ATOM   1139 N  N    . VAL A 1 142 ? -11.945 3.777   21.161  1.00 11.22 ? 143 VAL A N    1 
ATOM   1140 C  CA   . VAL A 1 142 ? -11.982 2.758   20.116  1.00 10.24 ? 143 VAL A CA   1 
ATOM   1141 C  C    . VAL A 1 142 ? -12.993 1.734   20.553  1.00 11.08 ? 143 VAL A C    1 
ATOM   1142 O  O    . VAL A 1 142 ? -12.869 1.148   21.679  1.00 12.70 ? 143 VAL A O    1 
ATOM   1143 C  CB   . VAL A 1 142 ? -10.637 2.072   19.829  1.00 10.03 ? 143 VAL A CB   1 
ATOM   1144 C  CG1  . VAL A 1 142 ? -10.819 0.946   18.694  1.00 10.44 ? 143 VAL A CG1  1 
ATOM   1145 C  CG2  . VAL A 1 142 ? -9.615  3.144   19.427  1.00 12.07 ? 143 VAL A CG2  1 
ATOM   1146 N  N    . LEU A 1 143 ? -13.978 1.479   19.691  1.00 10.04 ? 144 LEU A N    1 
ATOM   1147 C  CA   . LEU A 1 143 ? -14.923 0.398   19.979  1.00 10.59 ? 144 LEU A CA   1 
ATOM   1148 C  C    . LEU A 1 143 ? -14.335 -0.872  19.314  1.00 9.22  ? 144 LEU A C    1 
ATOM   1149 O  O    . LEU A 1 143 ? -14.198 -0.922  18.068  1.00 10.56 ? 144 LEU A O    1 
ATOM   1150 C  CB   . LEU A 1 143 ? -16.345 0.773   19.409  1.00 10.12 ? 144 LEU A CB   1 
ATOM   1151 C  CG   . LEU A 1 143 ? -17.455 -0.216  19.501  1.00 13.07 ? 144 LEU A CG   1 
ATOM   1152 C  CD1  . LEU A 1 143 ? -17.612 -0.529  21.076  1.00 12.96 ? 144 LEU A CD1  1 
ATOM   1153 C  CD2  . LEU A 1 143 ? -18.763 0.368   18.903  1.00 14.58 ? 144 LEU A CD2  1 
ATOM   1154 N  N    . GLY A 1 144 ? -13.991 -1.871  20.137  1.00 7.95  ? 145 GLY A N    1 
ATOM   1155 C  CA   . GLY A 1 144 ? -13.435 -3.145  19.633  1.00 7.00  ? 145 GLY A CA   1 
ATOM   1156 C  C    . GLY A 1 144 ? -14.504 -4.254  19.630  1.00 8.69  ? 145 GLY A C    1 
ATOM   1157 O  O    . GLY A 1 144 ? -15.225 -4.474  20.611  1.00 10.38 ? 145 GLY A O    1 
ATOM   1158 N  N    . ILE A 1 145 ? -14.556 -4.994  18.540  1.00 8.13  ? 146 ILE A N    1 
ATOM   1159 C  CA   . ILE A 1 145 ? -15.602 -6.043  18.368  1.00 8.94  ? 146 ILE A CA   1 
ATOM   1160 C  C    . ILE A 1 145 ? -14.870 -7.294  17.839  1.00 10.07 ? 146 ILE A C    1 
ATOM   1161 O  O    . ILE A 1 145 ? -14.215 -7.272  16.804  1.00 11.40 ? 146 ILE A O    1 
ATOM   1162 C  CB   . ILE A 1 145 ? -16.650 -5.534  17.321  1.00 9.11  ? 146 ILE A CB   1 
ATOM   1163 C  CG1  . ILE A 1 145 ? -17.315 -4.311  17.893  1.00 8.71  ? 146 ILE A CG1  1 
ATOM   1164 C  CG2  . ILE A 1 145 ? -17.656 -6.644  16.988  1.00 9.58  ? 146 ILE A CG2  1 
ATOM   1165 C  CD1  . ILE A 1 145 ? -18.449 -3.691  16.930  1.00 8.84  ? 146 ILE A CD1  1 
ATOM   1166 N  N    . PHE A 1 146 ? -15.059 -8.420  18.508  1.00 10.75 ? 147 PHE A N    1 
ATOM   1167 C  CA   . PHE A 1 146 ? -14.384 -9.676  18.048  1.00 10.19 ? 147 PHE A CA   1 
ATOM   1168 C  C    . PHE A 1 146 ? -15.167 -10.332 16.902  1.00 10.67 ? 147 PHE A C    1 
ATOM   1169 O  O    . PHE A 1 146 ? -16.380 -10.213 16.826  1.00 11.16 ? 147 PHE A O    1 
ATOM   1170 C  CB   . PHE A 1 146 ? -14.359 -10.632 19.229  1.00 10.43 ? 147 PHE A CB   1 
ATOM   1171 C  CG   . PHE A 1 146 ? -13.545 -10.148 20.367  1.00 7.51  ? 147 PHE A CG   1 
ATOM   1172 C  CD1  . PHE A 1 146 ? -12.153 -9.986  20.219  1.00 11.18 ? 147 PHE A CD1  1 
ATOM   1173 C  CD2  . PHE A 1 146 ? -14.100 -9.898  21.619  1.00 11.78 ? 147 PHE A CD2  1 
ATOM   1174 C  CE1  . PHE A 1 146 ? -11.326 -9.563  21.256  1.00 13.16 ? 147 PHE A CE1  1 
ATOM   1175 C  CE2  . PHE A 1 146 ? -13.281 -9.487  22.667  1.00 14.38 ? 147 PHE A CE2  1 
ATOM   1176 C  CZ   . PHE A 1 146 ? -11.903 -9.342  22.472  1.00 10.53 ? 147 PHE A CZ   1 
ATOM   1177 N  N    . LEU A 1 147 ? -14.453 -10.997 15.998  1.00 10.64 ? 148 LEU A N    1 
ATOM   1178 C  CA   . LEU A 1 147 ? -15.062 -11.807 14.958  1.00 9.06  ? 148 LEU A CA   1 
ATOM   1179 C  C    . LEU A 1 147 ? -14.723 -13.285 15.162  1.00 11.26 ? 148 LEU A C    1 
ATOM   1180 O  O    . LEU A 1 147 ? -13.580 -13.636 15.382  1.00 10.35 ? 148 LEU A O    1 
ATOM   1181 C  CB   . LEU A 1 147 ? -14.574 -11.365 13.580  1.00 10.29 ? 148 LEU A CB   1 
ATOM   1182 C  CG   . LEU A 1 147 ? -15.112 -10.065 12.950  1.00 10.65 ? 148 LEU A CG   1 
ATOM   1183 C  CD1  . LEU A 1 147 ? -14.918 -8.766  13.807  1.00 12.58 ? 148 LEU A CD1  1 
ATOM   1184 C  CD2  . LEU A 1 147 ? -14.351 -9.894  11.588  1.00 12.44 ? 148 LEU A CD2  1 
ATOM   1185 N  N    . LYS A 1 148 ? -15.761 -14.129 15.150  1.00 11.97 ? 149 LYS A N    1 
ATOM   1186 C  CA   . LYS A 1 148 ? -15.515 -15.560 15.038  1.00 13.39 ? 149 LYS A CA   1 
ATOM   1187 C  C    . LYS A 1 148 ? -16.045 -16.058 13.711  1.00 13.36 ? 149 LYS A C    1 
ATOM   1188 O  O    . LYS A 1 148 ? -16.901 -15.470 13.092  1.00 13.99 ? 149 LYS A O    1 
ATOM   1189 C  CB   . LYS A 1 148 ? -16.167 -16.299 16.182  1.00 14.53 ? 149 LYS A CB   1 
ATOM   1190 C  CG   . LYS A 1 148 ? -17.705 -16.161 16.173  1.00 16.21 ? 149 LYS A CG   1 
ATOM   1191 C  CD   . LYS A 1 148 ? -18.219 -16.757 17.481  1.00 25.55 ? 149 LYS A CD   1 
ATOM   1192 C  CE   . LYS A 1 148 ? -19.744 -16.892 17.466  1.00 28.84 ? 149 LYS A CE   1 
ATOM   1193 N  NZ   . LYS A 1 148 ? -20.190 -18.044 18.338  1.00 35.55 ? 149 LYS A NZ   1 
ATOM   1194 N  N    . VAL A 1 149 ? -15.577 -17.226 13.302  1.00 14.26 ? 150 VAL A N    1 
ATOM   1195 C  CA   . VAL A 1 149 ? -15.955 -17.785 12.018  1.00 14.44 ? 150 VAL A CA   1 
ATOM   1196 C  C    . VAL A 1 149 ? -17.144 -18.735 12.240  1.00 13.86 ? 150 VAL A C    1 
ATOM   1197 O  O    . VAL A 1 149 ? -17.119 -19.665 13.097  1.00 13.35 ? 150 VAL A O    1 
ATOM   1198 C  CB   . VAL A 1 149 ? -14.793 -18.590 11.344  1.00 13.72 ? 150 VAL A CB   1 
ATOM   1199 C  CG1  . VAL A 1 149 ? -15.254 -19.318 10.084  1.00 13.35 ? 150 VAL A CG1  1 
ATOM   1200 C  CG2  . VAL A 1 149 ? -13.592 -17.636 11.075  1.00 15.89 ? 150 VAL A CG2  1 
ATOM   1201 N  N    . GLY A 1 150 ? -18.174 -18.488 11.445  1.00 12.42 ? 151 GLY A N    1 
ATOM   1202 C  CA   . GLY A 1 150 ? -19.424 -19.308 11.468  1.00 15.28 ? 151 GLY A CA   1 
ATOM   1203 C  C    . GLY A 1 150 ? -20.331 -18.801 10.348  1.00 14.43 ? 151 GLY A C    1 
ATOM   1204 O  O    . GLY A 1 150 ? -19.963 -18.859 9.180   1.00 14.92 ? 151 GLY A O    1 
ATOM   1205 N  N    . SER A 1 151 ? -21.510 -18.271 10.709  1.00 16.74 ? 152 SER A N    1 
ATOM   1206 C  CA   A SER A 1 151 ? -22.425 -17.676 9.726   0.50 16.69 ? 152 SER A CA   1 
ATOM   1207 C  CA   B SER A 1 151 ? -22.413 -17.694 9.699   0.50 16.58 ? 152 SER A CA   1 
ATOM   1208 C  C    . SER A 1 151 ? -21.817 -16.390 9.159   1.00 16.81 ? 152 SER A C    1 
ATOM   1209 O  O    . SER A 1 151 ? -21.011 -15.737 9.835   1.00 14.14 ? 152 SER A O    1 
ATOM   1210 C  CB   A SER A 1 151 ? -23.780 -17.391 10.365  0.50 17.41 ? 152 SER A CB   1 
ATOM   1211 C  CB   B SER A 1 151 ? -23.838 -17.477 10.229  0.50 17.38 ? 152 SER A CB   1 
ATOM   1212 O  OG   A SER A 1 151 ? -24.267 -18.576 10.969  0.50 18.96 ? 152 SER A OG   1 
ATOM   1213 O  OG   B SER A 1 151 ? -23.860 -16.662 11.382  0.50 18.02 ? 152 SER A OG   1 
ATOM   1214 N  N    . ALA A 1 152 ? -22.145 -16.085 7.894   1.00 17.84 ? 153 ALA A N    1 
ATOM   1215 C  CA   . ALA A 1 152 ? -21.763 -14.800 7.237   1.00 16.04 ? 153 ALA A CA   1 
ATOM   1216 C  C    . ALA A 1 152 ? -22.372 -13.588 7.928   1.00 15.79 ? 153 ALA A C    1 
ATOM   1217 O  O    . ALA A 1 152 ? -23.455 -13.676 8.468   1.00 16.56 ? 153 ALA A O    1 
ATOM   1218 C  CB   . ALA A 1 152 ? -22.142 -14.816 5.748   1.00 16.49 ? 153 ALA A CB   1 
ATOM   1219 N  N    . LYS A 1 153 ? -21.646 -12.455 7.944   1.00 14.98 ? 154 LYS A N    1 
ATOM   1220 C  CA   . LYS A 1 153 ? -22.189 -11.159 8.363   1.00 14.23 ? 154 LYS A CA   1 
ATOM   1221 C  C    . LYS A 1 153 ? -22.551 -10.412 7.055   1.00 14.94 ? 154 LYS A C    1 
ATOM   1222 O  O    . LYS A 1 153 ? -21.677 -9.980  6.277   1.00 12.62 ? 154 LYS A O    1 
ATOM   1223 C  CB   . LYS A 1 153 ? -21.136 -10.352 9.187   1.00 15.51 ? 154 LYS A CB   1 
ATOM   1224 C  CG   . LYS A 1 153 ? -21.706 -9.170  9.953   1.00 17.23 ? 154 LYS A CG   1 
ATOM   1225 C  CD   . LYS A 1 153 ? -22.724 -9.647  11.033  1.00 16.63 ? 154 LYS A CD   1 
ATOM   1226 C  CE   . LYS A 1 153 ? -22.983 -8.606  12.152  1.00 18.76 ? 154 LYS A CE   1 
ATOM   1227 N  NZ   . LYS A 1 153 ? -24.269 -8.855  12.881  1.00 20.38 ? 154 LYS A NZ   1 
ATOM   1228 N  N    . PRO A 1 154 ? -23.885 -10.326 6.739   1.00 15.54 ? 155 PRO A N    1 
ATOM   1229 C  CA   . PRO A 1 154 ? -24.224 -9.711  5.436   1.00 16.21 ? 155 PRO A CA   1 
ATOM   1230 C  C    . PRO A 1 154 ? -23.699 -8.285  5.304   1.00 15.30 ? 155 PRO A C    1 
ATOM   1231 O  O    . PRO A 1 154 ? -23.244 -7.880  4.223   1.00 16.33 ? 155 PRO A O    1 
ATOM   1232 C  CB   . PRO A 1 154 ? -25.804 -9.784  5.404   1.00 16.17 ? 155 PRO A CB   1 
ATOM   1233 C  CG   . PRO A 1 154 ? -26.153 -10.883 6.498   1.00 16.21 ? 155 PRO A CG   1 
ATOM   1234 C  CD   . PRO A 1 154 ? -25.073 -10.710 7.530   1.00 15.75 ? 155 PRO A CD   1 
ATOM   1235 N  N    . GLY A 1 155 ? -23.675 -7.577  6.421   1.00 16.58 ? 156 GLY A N    1 
ATOM   1236 C  CA   . GLY A 1 155 ? -23.295 -6.147  6.475   1.00 17.68 ? 156 GLY A CA   1 
ATOM   1237 C  C    . GLY A 1 155 ? -21.828 -5.925  6.216   1.00 18.24 ? 156 GLY A C    1 
ATOM   1238 O  O    . GLY A 1 155 ? -21.410 -4.808  5.994   1.00 19.68 ? 156 GLY A O    1 
ATOM   1239 N  N    . LEU A 1 156 ? -21.033 -7.010  6.265   1.00 17.07 ? 157 LEU A N    1 
ATOM   1240 C  CA   . LEU A 1 156 ? -19.617 -6.966  5.912   1.00 15.51 ? 157 LEU A CA   1 
ATOM   1241 C  C    . LEU A 1 156 ? -19.305 -7.259  4.446   1.00 16.17 ? 157 LEU A C    1 
ATOM   1242 O  O    . LEU A 1 156 ? -18.177 -7.000  3.942   1.00 15.43 ? 157 LEU A O    1 
ATOM   1243 C  CB   . LEU A 1 156 ? -18.847 -7.991  6.794   1.00 15.36 ? 157 LEU A CB   1 
ATOM   1244 C  CG   . LEU A 1 156 ? -17.304 -8.137  6.610   1.00 16.42 ? 157 LEU A CG   1 
ATOM   1245 C  CD1  . LEU A 1 156 ? -16.599 -6.786  6.961   1.00 14.22 ? 157 LEU A CD1  1 
ATOM   1246 C  CD2  . LEU A 1 156 ? -16.789 -9.274  7.428   1.00 13.65 ? 157 LEU A CD2  1 
ATOM   1247 N  N    . GLN A 1 157 ? -20.242 -7.867  3.713   1.00 16.78 ? 158 GLN A N    1 
ATOM   1248 C  CA   . GLN A 1 157 ? -19.879 -8.259  2.336   1.00 16.69 ? 158 GLN A CA   1 
ATOM   1249 C  C    . GLN A 1 157 ? -19.454 -7.103  1.442   1.00 16.55 ? 158 GLN A C    1 
ATOM   1250 O  O    . GLN A 1 157 ? -18.614 -7.269  0.584   1.00 16.33 ? 158 GLN A O    1 
ATOM   1251 C  CB   . GLN A 1 157 ? -21.023 -9.102  1.702   1.00 17.98 ? 158 GLN A CB   1 
ATOM   1252 C  CG   . GLN A 1 157 ? -20.598 -9.800  0.408   1.00 19.11 ? 158 GLN A CG   1 
ATOM   1253 C  CD   . GLN A 1 157 ? -19.508 -10.822 0.663   1.00 17.68 ? 158 GLN A CD   1 
ATOM   1254 O  OE1  . GLN A 1 157 ? -19.445 -11.410 1.750   1.00 18.42 ? 158 GLN A OE1  1 
ATOM   1255 N  NE2  . GLN A 1 157 ? -18.695 -11.085 -0.321  1.00 20.08 ? 158 GLN A NE2  1 
ATOM   1256 N  N    . LYS A 1 158 ? -20.066 -5.917  1.565   1.00 17.21 ? 159 LYS A N    1 
ATOM   1257 C  CA   . LYS A 1 158 ? -19.630 -4.817  0.705   1.00 17.77 ? 159 LYS A CA   1 
ATOM   1258 C  C    . LYS A 1 158 ? -18.121 -4.450  0.852   1.00 17.57 ? 159 LYS A C    1 
ATOM   1259 O  O    . LYS A 1 158 ? -17.431 -4.157  -0.122  1.00 17.36 ? 159 LYS A O    1 
ATOM   1260 C  CB   . LYS A 1 158 ? -20.566 -3.591  0.833   1.00 18.25 ? 159 LYS A CB   1 
ATOM   1261 C  CG   . LYS A 1 158 ? -21.991 -3.856  0.362   1.00 21.65 ? 159 LYS A CG   1 
ATOM   1262 C  CD   . LYS A 1 158 ? -22.881 -2.638  0.551   0.01 18.59 ? 159 LYS A CD   1 
ATOM   1263 C  CE   . LYS A 1 158 ? -24.304 -2.922  0.096   0.01 19.20 ? 159 LYS A CE   1 
ATOM   1264 N  NZ   . LYS A 1 158 ? -25.203 -1.751  0.291   0.01 18.82 ? 159 LYS A NZ   1 
ATOM   1265 N  N    . VAL A 1 159 ? -17.605 -4.539  2.095   1.00 17.12 ? 160 VAL A N    1 
ATOM   1266 C  CA   . VAL A 1 159 ? -16.178 -4.419  2.361   1.00 14.62 ? 160 VAL A CA   1 
ATOM   1267 C  C    . VAL A 1 159 ? -15.410 -5.578  1.688   1.00 14.57 ? 160 VAL A C    1 
ATOM   1268 O  O    . VAL A 1 159 ? -14.448 -5.370  0.935   1.00 13.68 ? 160 VAL A O    1 
ATOM   1269 C  CB   . VAL A 1 159 ? -15.960 -4.424  3.882   1.00 14.91 ? 160 VAL A CB   1 
ATOM   1270 C  CG1  . VAL A 1 159 ? -14.483 -4.495  4.212   1.00 14.14 ? 160 VAL A CG1  1 
ATOM   1271 C  CG2  . VAL A 1 159 ? -16.576 -3.172  4.491   1.00 16.32 ? 160 VAL A CG2  1 
ATOM   1272 N  N    . VAL A 1 160 ? -15.856 -6.813  1.899   1.00 14.01 ? 161 VAL A N    1 
ATOM   1273 C  CA   . VAL A 1 160 ? -15.091 -7.961  1.354   1.00 15.58 ? 161 VAL A CA   1 
ATOM   1274 C  C    . VAL A 1 160 ? -15.017 -7.850  -0.195  1.00 15.77 ? 161 VAL A C    1 
ATOM   1275 O  O    . VAL A 1 160 ? -13.953 -8.084  -0.833  1.00 15.98 ? 161 VAL A O    1 
ATOM   1276 C  CB   . VAL A 1 160 ? -15.838 -9.299  1.819   1.00 17.47 ? 161 VAL A CB   1 
ATOM   1277 C  CG1  . VAL A 1 160 ? -15.505 -10.498 0.976   1.00 17.48 ? 161 VAL A CG1  1 
ATOM   1278 C  CG2  . VAL A 1 160 ? -15.625 -9.521  3.277   1.00 15.87 ? 161 VAL A CG2  1 
ATOM   1279 N  N    . ASP A 1 161 ? -16.111 -7.404  -0.815  1.00 18.80 ? 162 ASP A N    1 
ATOM   1280 C  CA   . ASP A 1 161 ? -16.100 -7.355  -2.283  1.00 21.84 ? 162 ASP A CA   1 
ATOM   1281 C  C    . ASP A 1 161 ? -15.097 -6.379  -2.940  1.00 22.79 ? 162 ASP A C    1 
ATOM   1282 O  O    . ASP A 1 161 ? -14.608 -6.648  -4.049  1.00 25.25 ? 162 ASP A O    1 
ATOM   1283 C  CB   . ASP A 1 161 ? -17.503 -7.191  -2.795  1.00 21.82 ? 162 ASP A CB   1 
ATOM   1284 C  CG   . ASP A 1 161 ? -18.277 -8.527  -2.733  1.00 23.39 ? 162 ASP A CG   1 
ATOM   1285 O  OD1  . ASP A 1 161 ? -17.619 -9.577  -2.895  1.00 25.94 ? 162 ASP A OD1  1 
ATOM   1286 O  OD2  . ASP A 1 161 ? -19.511 -8.530  -2.489  1.00 27.53 ? 162 ASP A OD2  1 
ATOM   1287 N  N    . VAL A 1 162 ? -14.775 -5.269  -2.257  1.00 21.14 ? 163 VAL A N    1 
ATOM   1288 C  CA   . VAL A 1 162 ? -13.932 -4.211  -2.842  1.00 20.81 ? 163 VAL A CA   1 
ATOM   1289 C  C    . VAL A 1 162 ? -12.453 -4.502  -2.650  1.00 19.64 ? 163 VAL A C    1 
ATOM   1290 O  O    . VAL A 1 162 ? -11.562 -3.833  -3.230  1.00 19.02 ? 163 VAL A O    1 
ATOM   1291 C  CB   . VAL A 1 162 ? -14.404 -2.827  -2.233  1.00 20.66 ? 163 VAL A CB   1 
ATOM   1292 C  CG1  . VAL A 1 162 ? -13.847 -2.589  -0.861  1.00 19.70 ? 163 VAL A CG1  1 
ATOM   1293 C  CG2  . VAL A 1 162 ? -14.027 -1.672  -3.107  1.00 24.14 ? 163 VAL A CG2  1 
ATOM   1294 N  N    . LEU A 1 163 ? -12.124 -5.516  -1.809  1.00 18.62 ? 164 LEU A N    1 
ATOM   1295 C  CA   . LEU A 1 163 ? -10.708 -5.749  -1.418  1.00 16.60 ? 164 LEU A CA   1 
ATOM   1296 C  C    . LEU A 1 163 ? -9.778  -6.110  -2.592  1.00 17.99 ? 164 LEU A C    1 
ATOM   1297 O  O    . LEU A 1 163 ? -8.555  -5.828  -2.584  1.00 17.79 ? 164 LEU A O    1 
ATOM   1298 C  CB   . LEU A 1 163 ? -10.579 -6.823  -0.319  1.00 15.76 ? 164 LEU A CB   1 
ATOM   1299 C  CG   . LEU A 1 163 ? -11.220 -6.519  1.042   1.00 13.59 ? 164 LEU A CG   1 
ATOM   1300 C  CD1  . LEU A 1 163 ? -11.048 -7.751  1.980   1.00 16.11 ? 164 LEU A CD1  1 
ATOM   1301 C  CD2  . LEU A 1 163 ? -10.567 -5.312  1.639   1.00 13.50 ? 164 LEU A CD2  1 
ATOM   1302 N  N    . ASP A 1 164 ? -10.331 -6.821  -3.563  1.00 21.22 ? 165 ASP A N    1 
ATOM   1303 C  CA   . ASP A 1 164 ? -9.491  -7.197  -4.719  1.00 24.79 ? 165 ASP A CA   1 
ATOM   1304 C  C    . ASP A 1 164 ? -9.052  -5.933  -5.543  1.00 25.23 ? 165 ASP A C    1 
ATOM   1305 O  O    . ASP A 1 164 ? -8.011  -5.963  -6.185  1.00 26.61 ? 165 ASP A O    1 
ATOM   1306 C  CB   . ASP A 1 164 ? -10.262 -8.198  -5.584  1.00 27.21 ? 165 ASP A CB   1 
ATOM   1307 C  CG   . ASP A 1 164 ? -11.134 -7.493  -6.623  1.00 33.69 ? 165 ASP A CG   1 
ATOM   1308 O  OD1  . ASP A 1 164 ? -10.639 -7.325  -7.784  1.00 38.60 ? 165 ASP A OD1  1 
ATOM   1309 O  OD2  . ASP A 1 164 ? -12.278 -7.058  -6.281  1.00 39.61 ? 165 ASP A OD2  1 
ATOM   1310 N  N    . SER A 1 165 ? -9.810  -4.834  -5.460  1.00 24.63 ? 166 SER A N    1 
ATOM   1311 C  CA   . SER A 1 165 ? -9.398  -3.507  -6.008  1.00 24.80 ? 166 SER A CA   1 
ATOM   1312 C  C    . SER A 1 165 ? -8.331  -2.718  -5.211  1.00 23.11 ? 166 SER A C    1 
ATOM   1313 O  O    . SER A 1 165 ? -7.782  -1.694  -5.698  1.00 21.03 ? 166 SER A O    1 
ATOM   1314 C  CB   . SER A 1 165 ? -10.641 -2.629  -6.213  1.00 26.48 ? 166 SER A CB   1 
ATOM   1315 O  OG   . SER A 1 165 ? -11.148 -2.089  -4.988  1.00 29.07 ? 166 SER A OG   1 
ATOM   1316 N  N    . ILE A 1 166 ? -8.069  -3.123  -3.964  1.00 19.75 ? 167 ILE A N    1 
ATOM   1317 C  CA   . ILE A 1 166 ? -6.937  -2.552  -3.177  1.00 18.67 ? 167 ILE A CA   1 
ATOM   1318 C  C    . ILE A 1 166 ? -5.977  -3.638  -2.677  1.00 18.72 ? 167 ILE A C    1 
ATOM   1319 O  O    . ILE A 1 166 ? -5.596  -3.685  -1.495  1.00 16.07 ? 167 ILE A O    1 
ATOM   1320 C  CB   . ILE A 1 166 ? -7.456  -1.702  -1.938  1.00 19.48 ? 167 ILE A CB   1 
ATOM   1321 C  CG1  . ILE A 1 166 ? -8.422  -2.538  -1.066  1.00 18.99 ? 167 ILE A CG1  1 
ATOM   1322 C  CG2  . ILE A 1 166 ? -8.289  -0.468  -2.403  1.00 20.57 ? 167 ILE A CG2  1 
ATOM   1323 C  CD1  . ILE A 1 166 ? -8.535  -2.055  0.437   1.00 18.13 ? 167 ILE A CD1  1 
ATOM   1324 N  N    . LYS A 1 167 ? -5.570  -4.531  -3.567  1.00 18.37 ? 168 LYS A N    1 
ATOM   1325 C  CA   . LYS A 1 167 ? -4.732  -5.624  -3.117  1.00 19.36 ? 168 LYS A CA   1 
ATOM   1326 C  C    . LYS A 1 167 ? -3.402  -5.265  -2.390  1.00 18.27 ? 168 LYS A C    1 
ATOM   1327 O  O    . LYS A 1 167 ? -3.078  -5.900  -1.397  1.00 16.49 ? 168 LYS A O    1 
ATOM   1328 C  CB   . LYS A 1 167 ? -4.499  -6.623  -4.286  1.00 18.13 ? 168 LYS A CB   1 
ATOM   1329 C  CG   . LYS A 1 167 ? -3.623  -7.808  -3.927  1.00 20.46 ? 168 LYS A CG   1 
ATOM   1330 C  CD   . LYS A 1 167 ? -3.494  -8.786  -5.180  1.00 21.27 ? 168 LYS A CD   1 
ATOM   1331 C  CE   . LYS A 1 167 ? -2.691  -10.009 -4.762  1.00 27.16 ? 168 LYS A CE   1 
ATOM   1332 N  NZ   . LYS A 1 167 ? -2.624  -11.141 -5.756  1.00 29.91 ? 168 LYS A NZ   1 
ATOM   1333 N  N    . THR A 1 168 ? -2.656  -4.258  -2.885  1.00 17.85 ? 169 THR A N    1 
ATOM   1334 C  CA   . THR A 1 168 ? -1.288  -3.970  -2.436  1.00 18.78 ? 169 THR A CA   1 
ATOM   1335 C  C    . THR A 1 168 ? -1.163  -2.608  -1.725  1.00 18.17 ? 169 THR A C    1 
ATOM   1336 O  O    . THR A 1 168 ? -1.961  -1.718  -1.982  1.00 20.22 ? 169 THR A O    1 
ATOM   1337 C  CB   . THR A 1 168 ? -0.322  -4.015  -3.678  1.00 18.54 ? 169 THR A CB   1 
ATOM   1338 O  OG1  . THR A 1 168 ? -0.942  -3.244  -4.703  1.00 19.68 ? 169 THR A OG1  1 
ATOM   1339 C  CG2  . THR A 1 168 ? -0.136  -5.496  -4.160  1.00 20.38 ? 169 THR A CG2  1 
ATOM   1340 N  N    . LYS A 1 169 ? -0.169  -2.497  -0.832  1.00 21.00 ? 170 LYS A N    1 
ATOM   1341 C  CA   . LYS A 1 169 ? 0.218   -1.246  -0.140  1.00 22.03 ? 170 LYS A CA   1 
ATOM   1342 C  C    . LYS A 1 169 ? 0.057   -0.010  -1.032  1.00 22.20 ? 170 LYS A C    1 
ATOM   1343 O  O    . LYS A 1 169 ? 0.618   0.043   -2.172  1.00 24.80 ? 170 LYS A O    1 
ATOM   1344 C  CB   . LYS A 1 169 ? 1.629   -1.342  0.421   1.00 22.04 ? 170 LYS A CB   1 
ATOM   1345 C  CG   . LYS A 1 169 ? 2.101   -0.073  1.214   1.00 21.77 ? 170 LYS A CG   1 
ATOM   1346 C  CD   . LYS A 1 169 ? 3.348   -0.313  2.075   1.00 25.04 ? 170 LYS A CD   1 
ATOM   1347 C  CE   . LYS A 1 169 ? 4.697   -0.231  1.302   1.00 31.06 ? 170 LYS A CE   1 
ATOM   1348 N  NZ   . LYS A 1 169 ? 5.850   -1.023  1.983   1.00 32.99 ? 170 LYS A NZ   1 
ATOM   1349 N  N    . GLY A 1 170 ? -0.718  0.944   -0.542  1.00 22.62 ? 171 GLY A N    1 
ATOM   1350 C  CA   . GLY A 1 170 ? -0.896  2.239   -1.200  1.00 21.87 ? 171 GLY A CA   1 
ATOM   1351 C  C    . GLY A 1 170 ? -2.068  2.358   -2.090  1.00 22.65 ? 171 GLY A C    1 
ATOM   1352 O  O    . GLY A 1 170 ? -2.463  3.483   -2.464  1.00 24.86 ? 171 GLY A O    1 
ATOM   1353 N  N    . LYS A 1 171 ? -2.692  1.232   -2.470  1.00 20.64 ? 172 LYS A N    1 
ATOM   1354 C  CA   . LYS A 1 171 ? -3.913  1.347   -3.259  1.00 20.48 ? 172 LYS A CA   1 
ATOM   1355 C  C    . LYS A 1 171 ? -5.095  1.788   -2.454  1.00 21.22 ? 172 LYS A C    1 
ATOM   1356 O  O    . LYS A 1 171 ? -5.257  1.372   -1.302  1.00 22.70 ? 172 LYS A O    1 
ATOM   1357 C  CB   . LYS A 1 171 ? -4.287  0.046   -4.040  1.00 20.52 ? 172 LYS A CB   1 
ATOM   1358 C  CG   . LYS A 1 171 ? -3.199  -0.475  -4.985  1.00 21.01 ? 172 LYS A CG   1 
ATOM   1359 C  CD   . LYS A 1 171 ? -3.726  -1.564  -5.914  0.01 20.48 ? 172 LYS A CD   1 
ATOM   1360 C  CE   . LYS A 1 171 ? -4.553  -0.983  -7.057  0.01 20.44 ? 172 LYS A CE   1 
ATOM   1361 N  NZ   . LYS A 1 171 ? -5.125  -2.044  -7.930  0.01 20.16 ? 172 LYS A NZ   1 
ATOM   1362 N  N    . SER A 1 172 ? -5.972  2.566   -3.087  1.00 21.59 ? 173 SER A N    1 
ATOM   1363 C  CA   . SER A 1 172 ? -7.178  3.071   -2.489  1.00 23.84 ? 173 SER A CA   1 
ATOM   1364 C  C    . SER A 1 172 ? -8.301  3.100   -3.521  1.00 26.22 ? 173 SER A C    1 
ATOM   1365 O  O    . SER A 1 172 ? -8.027  3.088   -4.757  1.00 26.00 ? 173 SER A O    1 
ATOM   1366 C  CB   . SER A 1 172 ? -6.917  4.455   -1.810  1.00 25.67 ? 173 SER A CB   1 
ATOM   1367 O  OG   . SER A 1 172 ? -6.519  5.438   -2.766  1.00 25.46 ? 173 SER A OG   1 
ATOM   1368 N  N    . ALA A 1 173 ? -9.543  3.079   -3.049  1.00 24.63 ? 174 ALA A N    1 
ATOM   1369 C  CA   . ALA A 1 173 ? -10.736 3.111   -3.905  1.00 25.39 ? 174 ALA A CA   1 
ATOM   1370 C  C    . ALA A 1 173 ? -11.783 3.937   -3.241  1.00 25.88 ? 174 ALA A C    1 
ATOM   1371 O  O    . ALA A 1 173 ? -11.849 3.965   -1.996  1.00 25.65 ? 174 ALA A O    1 
ATOM   1372 C  CB   . ALA A 1 173 ? -11.288 1.751   -4.109  1.00 23.47 ? 174 ALA A CB   1 
ATOM   1373 N  N    A ASP A 1 174 ? -12.568 4.719   -3.986  0.50 24.36 ? 175 ASP A N    1 
ATOM   1374 N  N    B ASP A 1 174 ? -12.723 4.406   -4.066  0.50 24.97 ? 175 ASP A N    1 
ATOM   1375 C  CA   A ASP A 1 174 ? -13.630 5.425   -3.258  0.50 23.91 ? 175 ASP A CA   1 
ATOM   1376 C  CA   B ASP A 1 174 ? -13.929 5.042   -3.577  0.50 25.05 ? 175 ASP A CA   1 
ATOM   1377 C  C    A ASP A 1 174 ? -14.545 4.306   -2.713  0.50 23.81 ? 175 ASP A C    1 
ATOM   1378 C  C    B ASP A 1 174 ? -14.921 4.134   -2.833  0.50 24.38 ? 175 ASP A C    1 
ATOM   1379 O  O    A ASP A 1 174 ? -14.411 3.175   -3.198  0.50 23.41 ? 175 ASP A O    1 
ATOM   1380 O  O    B ASP A 1 174 ? -15.257 3.004   -3.236  0.50 23.86 ? 175 ASP A O    1 
ATOM   1381 C  CB   A ASP A 1 174 ? -14.319 6.552   -4.067  0.50 23.83 ? 175 ASP A CB   1 
ATOM   1382 C  CB   B ASP A 1 174 ? -14.582 5.909   -4.675  0.50 25.94 ? 175 ASP A CB   1 
ATOM   1383 C  CG   A ASP A 1 174 ? -15.017 6.051   -5.294  0.50 23.95 ? 175 ASP A CG   1 
ATOM   1384 C  CG   B ASP A 1 174 ? -13.749 7.138   -4.987  0.50 26.76 ? 175 ASP A CG   1 
ATOM   1385 O  OD1  A ASP A 1 174 ? -14.763 6.628   -6.376  0.50 25.07 ? 175 ASP A OD1  1 
ATOM   1386 O  OD1  B ASP A 1 174 ? -13.679 7.997   -4.112  0.50 31.55 ? 175 ASP A OD1  1 
ATOM   1387 O  OD2  A ASP A 1 174 ? -15.809 5.097   -5.188  0.50 22.67 ? 175 ASP A OD2  1 
ATOM   1388 O  OD2  B ASP A 1 174 ? -13.155 7.264   -6.082  0.50 29.49 ? 175 ASP A OD2  1 
ATOM   1389 N  N    . PHE A 1 175 ? -15.373 4.607   -1.690  1.00 22.69 ? 176 PHE A N    1 
ATOM   1390 C  CA   . PHE A 1 175 ? -16.141 3.648   -0.845  1.00 22.46 ? 176 PHE A CA   1 
ATOM   1391 C  C    . PHE A 1 175 ? -17.163 4.395   -0.079  1.00 22.93 ? 176 PHE A C    1 
ATOM   1392 O  O    . PHE A 1 175 ? -16.957 4.812   1.067   1.00 23.22 ? 176 PHE A O    1 
ATOM   1393 C  CB   . PHE A 1 175 ? -15.223 2.810   0.098   1.00 20.84 ? 176 PHE A CB   1 
ATOM   1394 C  CG   . PHE A 1 175 ? -15.875 1.558   0.628   1.00 20.01 ? 176 PHE A CG   1 
ATOM   1395 C  CD1  . PHE A 1 175 ? -16.110 0.461   -0.215  1.00 22.81 ? 176 PHE A CD1  1 
ATOM   1396 C  CD2  . PHE A 1 175 ? -16.232 1.452   1.980   1.00 19.59 ? 176 PHE A CD2  1 
ATOM   1397 C  CE1  . PHE A 1 175 ? -16.688 -0.720  0.299   1.00 22.86 ? 176 PHE A CE1  1 
ATOM   1398 C  CE2  . PHE A 1 175 ? -16.802 0.276   2.498   1.00 21.07 ? 176 PHE A CE2  1 
ATOM   1399 C  CZ   . PHE A 1 175 ? -17.049 -0.806  1.649   1.00 20.01 ? 176 PHE A CZ   1 
ATOM   1400 N  N    . THR A 1 176 ? -18.294 4.555   -0.728  1.00 21.49 ? 177 THR A N    1 
ATOM   1401 C  CA   . THR A 1 176 ? -19.316 5.465   -0.372  1.00 21.45 ? 177 THR A CA   1 
ATOM   1402 C  C    . THR A 1 176 ? -20.546 4.692   0.078   1.00 20.46 ? 177 THR A C    1 
ATOM   1403 O  O    . THR A 1 176 ? -20.730 3.509   -0.342  1.00 20.94 ? 177 THR A O    1 
ATOM   1404 C  CB   . THR A 1 176 ? -19.480 6.366   -1.682  1.00 23.31 ? 177 THR A CB   1 
ATOM   1405 O  OG1  . THR A 1 176 ? -19.089 7.717   -1.408  1.00 27.10 ? 177 THR A OG1  1 
ATOM   1406 C  CG2  . THR A 1 176 ? -20.771 6.195   -2.385  1.00 25.28 ? 177 THR A CG2  1 
ATOM   1407 N  N    . ASN A 1 177 ? -21.314 5.308   0.980   1.00 17.85 ? 178 ASN A N    1 
ATOM   1408 C  CA   . ASN A 1 177 ? -22.589 4.819   1.568   1.00 18.51 ? 178 ASN A CA   1 
ATOM   1409 C  C    . ASN A 1 177 ? -22.438 3.446   2.282   1.00 19.22 ? 178 ASN A C    1 
ATOM   1410 O  O    . ASN A 1 177 ? -23.323 2.631   2.221   1.00 20.44 ? 178 ASN A O    1 
ATOM   1411 C  CB   . ASN A 1 177 ? -23.758 4.770   0.554   1.00 19.92 ? 178 ASN A CB   1 
ATOM   1412 C  CG   . ASN A 1 177 ? -23.914 6.113   -0.261  1.00 19.59 ? 178 ASN A CG   1 
ATOM   1413 O  OD1  . ASN A 1 177 ? -24.601 6.992   0.175   1.00 24.35 ? 178 ASN A OD1  1 
ATOM   1414 N  ND2  . ASN A 1 177 ? -23.325 6.184   -1.447  1.00 18.63 ? 178 ASN A ND2  1 
ATOM   1415 N  N    . PHE A 1 178 ? -21.288 3.209   2.890   1.00 18.99 ? 179 PHE A N    1 
ATOM   1416 C  CA   . PHE A 1 178 ? -21.156 2.007   3.755   1.00 18.08 ? 179 PHE A CA   1 
ATOM   1417 C  C    . PHE A 1 178 ? -21.678 2.331   5.142   1.00 17.82 ? 179 PHE A C    1 
ATOM   1418 O  O    . PHE A 1 178 ? -21.205 3.291   5.772   1.00 18.07 ? 179 PHE A O    1 
ATOM   1419 C  CB   . PHE A 1 178 ? -19.735 1.500   3.799   1.00 18.21 ? 179 PHE A CB   1 
ATOM   1420 C  CG   . PHE A 1 178 ? -19.617 0.241   4.618   1.00 20.80 ? 179 PHE A CG   1 
ATOM   1421 C  CD1  . PHE A 1 178 ? -20.132 -0.976  4.100   1.00 19.32 ? 179 PHE A CD1  1 
ATOM   1422 C  CD2  . PHE A 1 178 ? -19.205 0.312   5.961   1.00 18.49 ? 179 PHE A CD2  1 
ATOM   1423 C  CE1  . PHE A 1 178 ? -20.110 -2.121  4.863   1.00 17.55 ? 179 PHE A CE1  1 
ATOM   1424 C  CE2  . PHE A 1 178 ? -19.206 -0.851  6.768   1.00 18.87 ? 179 PHE A CE2  1 
ATOM   1425 C  CZ   . PHE A 1 178 ? -19.654 -2.054  6.239   1.00 15.91 ? 179 PHE A CZ   1 
ATOM   1426 N  N    . ASP A 1 179 ? -22.597 1.503   5.624   1.00 17.79 ? 180 ASP A N    1 
ATOM   1427 C  CA   . ASP A 1 179 ? -23.271 1.649   6.912   1.00 18.36 ? 180 ASP A CA   1 
ATOM   1428 C  C    . ASP A 1 179 ? -22.662 0.787   7.994   1.00 16.43 ? 180 ASP A C    1 
ATOM   1429 O  O    . ASP A 1 179 ? -22.909 -0.455  8.002   1.00 15.01 ? 180 ASP A O    1 
ATOM   1430 C  CB   . ASP A 1 179 ? -24.688 1.161   6.812   1.00 19.95 ? 180 ASP A CB   1 
ATOM   1431 C  CG   . ASP A 1 179 ? -25.544 1.643   7.936   1.00 20.36 ? 180 ASP A CG   1 
ATOM   1432 O  OD1  . ASP A 1 179 ? -25.096 1.936   9.092   1.00 20.75 ? 180 ASP A OD1  1 
ATOM   1433 O  OD2  . ASP A 1 179 ? -26.750 1.781   7.681   1.00 29.88 ? 180 ASP A OD2  1 
ATOM   1434 N  N    . PRO A 1 180 ? -21.912 1.411   8.920   1.00 15.30 ? 181 PRO A N    1 
ATOM   1435 C  CA   . PRO A 1 180 ? -21.224 0.569   9.981   1.00 14.07 ? 181 PRO A CA   1 
ATOM   1436 C  C    . PRO A 1 180 ? -22.141 -0.068  11.001  1.00 14.72 ? 181 PRO A C    1 
ATOM   1437 O  O    . PRO A 1 180 ? -21.749 -1.008  11.708  1.00 12.59 ? 181 PRO A O    1 
ATOM   1438 C  CB   . PRO A 1 180 ? -20.227 1.597   10.589  1.00 16.49 ? 181 PRO A CB   1 
ATOM   1439 C  CG   . PRO A 1 180 ? -20.923 2.915   10.442  1.00 15.01 ? 181 PRO A CG   1 
ATOM   1440 C  CD   . PRO A 1 180 ? -21.593 2.854   9.090   1.00 14.83 ? 181 PRO A CD   1 
ATOM   1441 N  N    . ARG A 1 181 ? -23.430 0.311   11.030  1.00 14.78 ? 182 ARG A N    1 
ATOM   1442 C  CA   . ARG A 1 181 ? -24.377 -0.393  11.949  1.00 14.84 ? 182 ARG A CA   1 
ATOM   1443 C  C    . ARG A 1 181 ? -24.526 -1.872  11.567  1.00 15.38 ? 182 ARG A C    1 
ATOM   1444 O  O    . ARG A 1 181 ? -24.880 -2.652  12.428  1.00 16.36 ? 182 ARG A O    1 
ATOM   1445 C  CB   . ARG A 1 181 ? -25.779 0.297   12.010  1.00 15.11 ? 182 ARG A CB   1 
ATOM   1446 C  CG   . ARG A 1 181 ? -25.657 1.816   12.413  1.00 14.41 ? 182 ARG A CG   1 
ATOM   1447 C  CD   . ARG A 1 181 ? -27.040 2.451   12.294  1.00 18.16 ? 182 ARG A CD   1 
ATOM   1448 N  NE   . ARG A 1 181 ? -27.348 2.695   10.903  1.00 18.55 ? 182 ARG A NE   1 
ATOM   1449 C  CZ   . ARG A 1 181 ? -28.457 3.349   10.506  1.00 25.70 ? 182 ARG A CZ   1 
ATOM   1450 N  NH1  . ARG A 1 181 ? -29.298 3.793   11.413  1.00 22.71 ? 182 ARG A NH1  1 
ATOM   1451 N  NH2  . ARG A 1 181 ? -28.709 3.568   9.222   1.00 24.70 ? 182 ARG A NH2  1 
ATOM   1452 N  N    . GLY A 1 182 ? -24.191 -2.232  10.322  1.00 14.88 ? 183 GLY A N    1 
ATOM   1453 C  CA   . GLY A 1 182 ? -24.276 -3.608  9.845   1.00 16.50 ? 183 GLY A CA   1 
ATOM   1454 C  C    . GLY A 1 182 ? -23.107 -4.471  10.366  1.00 16.97 ? 183 GLY A C    1 
ATOM   1455 O  O    . GLY A 1 182 ? -23.027 -5.649  10.041  1.00 17.32 ? 183 GLY A O    1 
ATOM   1456 N  N    . LEU A 1 183 ? -22.199 -3.896  11.170  1.00 16.16 ? 184 LEU A N    1 
ATOM   1457 C  CA   . LEU A 1 183 ? -21.016 -4.670  11.723  1.00 14.81 ? 184 LEU A CA   1 
ATOM   1458 C  C    . LEU A 1 183 ? -21.194 -4.841  13.224  1.00 14.02 ? 184 LEU A C    1 
ATOM   1459 O  O    . LEU A 1 183 ? -20.355 -5.451  13.920  1.00 16.85 ? 184 LEU A O    1 
ATOM   1460 C  CB   . LEU A 1 183 ? -19.681 -3.985  11.401  1.00 11.91 ? 184 LEU A CB   1 
ATOM   1461 C  CG   . LEU A 1 183 ? -19.301 -3.704  9.946   1.00 13.61 ? 184 LEU A CG   1 
ATOM   1462 C  CD1  . LEU A 1 183 ? -18.234 -2.761  9.874   1.00 16.10 ? 184 LEU A CD1  1 
ATOM   1463 C  CD2  . LEU A 1 183 ? -19.100 -4.944  9.081   1.00 17.58 ? 184 LEU A CD2  1 
ATOM   1464 N  N    . LEU A 1 184 ? -22.310 -4.373  13.772  1.00 14.60 ? 185 LEU A N    1 
ATOM   1465 C  CA   . LEU A 1 184 ? -22.492 -4.409  15.265  1.00 13.69 ? 185 LEU A CA   1 
ATOM   1466 C  C    . LEU A 1 184 ? -23.263 -5.635  15.765  1.00 15.87 ? 185 LEU A C    1 
ATOM   1467 O  O    . LEU A 1 184 ? -24.349 -5.967  15.201  1.00 19.57 ? 185 LEU A O    1 
ATOM   1468 C  CB   . LEU A 1 184 ? -23.178 -3.156  15.831  1.00 12.15 ? 185 LEU A CB   1 
ATOM   1469 C  CG   . LEU A 1 184 ? -22.571 -1.816  15.376  1.00 11.58 ? 185 LEU A CG   1 
ATOM   1470 C  CD1  . LEU A 1 184 ? -23.402 -0.586  15.800  1.00 18.66 ? 185 LEU A CD1  1 
ATOM   1471 C  CD2  . LEU A 1 184 ? -21.076 -1.635  15.827  1.00 13.21 ? 185 LEU A CD2  1 
ATOM   1472 N  N    . PRO A 1 185 ? -22.791 -6.269  16.874  1.00 14.15 ? 186 PRO A N    1 
ATOM   1473 C  CA   . PRO A 1 185 ? -23.565 -7.424  17.381  1.00 13.59 ? 186 PRO A CA   1 
ATOM   1474 C  C    . PRO A 1 185 ? -24.884 -6.908  18.062  1.00 15.39 ? 186 PRO A C    1 
ATOM   1475 O  O    . PRO A 1 185 ? -25.091 -5.707  18.154  1.00 14.98 ? 186 PRO A O    1 
ATOM   1476 C  CB   . PRO A 1 185 ? -22.651 -8.043  18.430  1.00 12.96 ? 186 PRO A CB   1 
ATOM   1477 C  CG   . PRO A 1 185 ? -21.841 -6.835  18.991  1.00 10.80 ? 186 PRO A CG   1 
ATOM   1478 C  CD   . PRO A 1 185 ? -21.645 -5.879  17.741  1.00 13.61 ? 186 PRO A CD   1 
ATOM   1479 N  N    . GLU A 1 186 ? -25.758 -7.797  18.554  1.00 16.13 ? 187 GLU A N    1 
ATOM   1480 C  CA   . GLU A 1 186 ? -26.949 -7.370  19.312  1.00 19.26 ? 187 GLU A CA   1 
ATOM   1481 C  C    . GLU A 1 186 ? -26.718 -6.562  20.567  1.00 19.67 ? 187 GLU A C    1 
ATOM   1482 O  O    . GLU A 1 186 ? -27.302 -5.487  20.751  1.00 22.26 ? 187 GLU A O    1 
ATOM   1483 C  CB   . GLU A 1 186 ? -27.717 -8.629  19.741  1.00 18.15 ? 187 GLU A CB   1 
ATOM   1484 C  CG   . GLU A 1 186 ? -28.392 -9.355  18.652  1.00 20.82 ? 187 GLU A CG   1 
ATOM   1485 C  CD   . GLU A 1 186 ? -29.174 -10.597 19.254  1.00 20.76 ? 187 GLU A CD   1 
ATOM   1486 O  OE1  . GLU A 1 186 ? -29.205 -10.778 20.497  1.00 26.03 ? 187 GLU A OE1  1 
ATOM   1487 O  OE2  . GLU A 1 186 ? -29.745 -11.356 18.488  1.00 28.22 ? 187 GLU A OE2  1 
ATOM   1488 N  N    . SER A 1 187 ? -25.910 -7.095  21.488  1.00 18.41 ? 188 SER A N    1 
ATOM   1489 C  CA   . SER A 1 187 ? -25.687 -6.475  22.768  1.00 18.77 ? 188 SER A CA   1 
ATOM   1490 C  C    . SER A 1 187 ? -24.556 -5.447  22.682  1.00 18.30 ? 188 SER A C    1 
ATOM   1491 O  O    . SER A 1 187 ? -23.617 -5.666  21.948  1.00 16.91 ? 188 SER A O    1 
ATOM   1492 C  CB   . SER A 1 187 ? -25.352 -7.556  23.793  1.00 18.93 ? 188 SER A CB   1 
ATOM   1493 O  OG   . SER A 1 187 ? -25.078 -7.047  25.051  1.00 18.54 ? 188 SER A OG   1 
ATOM   1494 N  N    . LEU A 1 188 ? -24.704 -4.361  23.446  1.00 16.91 ? 189 LEU A N    1 
ATOM   1495 C  CA   . LEU A 1 188 ? -23.640 -3.350  23.675  1.00 17.92 ? 189 LEU A CA   1 
ATOM   1496 C  C    . LEU A 1 188 ? -22.980 -3.509  25.051  1.00 16.83 ? 189 LEU A C    1 
ATOM   1497 O  O    . LEU A 1 188 ? -22.343 -2.562  25.549  1.00 21.12 ? 189 LEU A O    1 
ATOM   1498 C  CB   . LEU A 1 188 ? -24.150 -1.883  23.413  1.00 14.95 ? 189 LEU A CB   1 
ATOM   1499 C  CG   . LEU A 1 188 ? -24.489 -1.390  22.017  1.00 17.19 ? 189 LEU A CG   1 
ATOM   1500 C  CD1  . LEU A 1 188 ? -25.033 0.052   22.014  1.00 17.88 ? 189 LEU A CD1  1 
ATOM   1501 C  CD2  . LEU A 1 188 ? -23.306 -1.525  20.960  1.00 19.25 ? 189 LEU A CD2  1 
ATOM   1502 N  N    . ASP A 1 189 ? -23.097 -4.689  25.697  1.00 17.58 ? 190 ASP A N    1 
ATOM   1503 C  CA   . ASP A 1 189 ? -22.400 -4.947  26.970  1.00 17.94 ? 190 ASP A CA   1 
ATOM   1504 C  C    . ASP A 1 189 ? -20.904 -4.956  26.637  1.00 16.72 ? 190 ASP A C    1 
ATOM   1505 O  O    . ASP A 1 189 ? -20.503 -5.453  25.539  1.00 17.39 ? 190 ASP A O    1 
ATOM   1506 C  CB   . ASP A 1 189 ? -22.770 -6.281  27.577  1.00 17.42 ? 190 ASP A CB   1 
ATOM   1507 C  CG   . ASP A 1 189 ? -24.169 -6.277  28.228  1.00 23.30 ? 190 ASP A CG   1 
ATOM   1508 O  OD1  . ASP A 1 189 ? -24.856 -5.228  28.215  1.00 27.17 ? 190 ASP A OD1  1 
ATOM   1509 O  OD2  . ASP A 1 189 ? -24.562 -7.369  28.628  1.00 28.36 ? 190 ASP A OD2  1 
ATOM   1510 N  N    . TYR A 1 190 ? -20.135 -4.289  27.500  1.00 16.24 ? 191 TYR A N    1 
ATOM   1511 C  CA   . TYR A 1 190 ? -18.718 -3.992  27.170  1.00 15.74 ? 191 TYR A CA   1 
ATOM   1512 C  C    . TYR A 1 190 ? -17.784 -4.090  28.414  1.00 15.24 ? 191 TYR A C    1 
ATOM   1513 O  O    . TYR A 1 190 ? -18.220 -3.962  29.573  1.00 13.13 ? 191 TYR A O    1 
ATOM   1514 C  CB   . TYR A 1 190 ? -18.644 -2.603  26.470  1.00 15.25 ? 191 TYR A CB   1 
ATOM   1515 C  CG   . TYR A 1 190 ? -19.019 -1.446  27.404  1.00 16.45 ? 191 TYR A CG   1 
ATOM   1516 C  CD1  . TYR A 1 190 ? -18.066 -0.870  28.249  1.00 14.83 ? 191 TYR A CD1  1 
ATOM   1517 C  CD2  . TYR A 1 190 ? -20.329 -0.875  27.353  1.00 15.05 ? 191 TYR A CD2  1 
ATOM   1518 C  CE1  . TYR A 1 190 ? -18.414 0.238   29.133  1.00 14.77 ? 191 TYR A CE1  1 
ATOM   1519 C  CE2  . TYR A 1 190 ? -20.687 0.213   28.203  1.00 18.43 ? 191 TYR A CE2  1 
ATOM   1520 C  CZ   . TYR A 1 190 ? -19.736 0.743   29.085  1.00 15.83 ? 191 TYR A CZ   1 
ATOM   1521 O  OH   . TYR A 1 190 ? -20.043 1.779   29.922  1.00 14.65 ? 191 TYR A OH   1 
ATOM   1522 N  N    . TRP A 1 191 ? -16.497 -4.349  28.195  1.00 12.35 ? 192 TRP A N    1 
ATOM   1523 C  CA   . TRP A 1 191 ? -15.431 -4.030  29.099  1.00 11.96 ? 192 TRP A CA   1 
ATOM   1524 C  C    . TRP A 1 191 ? -14.722 -2.722  28.639  1.00 13.41 ? 192 TRP A C    1 
ATOM   1525 O  O    . TRP A 1 191 ? -14.756 -2.354  27.424  1.00 12.85 ? 192 TRP A O    1 
ATOM   1526 C  CB   . TRP A 1 191 ? -14.371 -5.147  29.124  1.00 13.04 ? 192 TRP A CB   1 
ATOM   1527 C  CG   . TRP A 1 191 ? -14.908 -6.533  29.492  1.00 13.51 ? 192 TRP A CG   1 
ATOM   1528 C  CD1  . TRP A 1 191 ? -15.211 -6.969  30.735  1.00 15.22 ? 192 TRP A CD1  1 
ATOM   1529 C  CD2  . TRP A 1 191 ? -15.153 -7.595  28.606  1.00 11.04 ? 192 TRP A CD2  1 
ATOM   1530 N  NE1  . TRP A 1 191 ? -15.711 -8.270  30.680  1.00 15.55 ? 192 TRP A NE1  1 
ATOM   1531 C  CE2  . TRP A 1 191 ? -15.684 -8.663  29.358  1.00 15.81 ? 192 TRP A CE2  1 
ATOM   1532 C  CE3  . TRP A 1 191 ? -15.019 -7.747  27.191  1.00 8.89  ? 192 TRP A CE3  1 
ATOM   1533 C  CZ2  . TRP A 1 191 ? -15.986 -9.892  28.780  1.00 15.23 ? 192 TRP A CZ2  1 
ATOM   1534 C  CZ3  . TRP A 1 191 ? -15.300 -8.948  26.630  1.00 13.95 ? 192 TRP A CZ3  1 
ATOM   1535 C  CH2  . TRP A 1 191 ? -15.801 -10.022 27.405  1.00 15.71 ? 192 TRP A CH2  1 
ATOM   1536 N  N    . THR A 1 192 ? -14.138 -2.016  29.605  1.00 11.58 ? 193 THR A N    1 
ATOM   1537 C  CA   . THR A 1 192 ? -13.415 -0.758  29.315  1.00 12.63 ? 193 THR A CA   1 
ATOM   1538 C  C    . THR A 1 192 ? -12.164 -0.548  30.219  1.00 12.51 ? 193 THR A C    1 
ATOM   1539 O  O    . THR A 1 192 ? -12.139 -0.957  31.401  1.00 13.78 ? 193 THR A O    1 
ATOM   1540 C  CB   . THR A 1 192 ? -14.374 0.497   29.365  1.00 12.71 ? 193 THR A CB   1 
ATOM   1541 O  OG1  . THR A 1 192 ? -13.713 1.695   28.907  1.00 12.31 ? 193 THR A OG1  1 
ATOM   1542 C  CG2  . THR A 1 192 ? -14.850 0.742   30.821  1.00 13.34 ? 193 THR A CG2  1 
ATOM   1543 N  N    . TYR A 1 193 ? -11.062 -0.027  29.628  1.00 11.57 ? 194 TYR A N    1 
ATOM   1544 C  CA   . TYR A 1 193 ? -9.817  0.180   30.353  1.00 11.76 ? 194 TYR A CA   1 
ATOM   1545 C  C    . TYR A 1 193 ? -9.073  1.264   29.530  1.00 12.56 ? 194 TYR A C    1 
ATOM   1546 O  O    . TYR A 1 193 ? -9.458  1.450   28.325  1.00 12.09 ? 194 TYR A O    1 
ATOM   1547 C  CB   . TYR A 1 193 ? -9.031  -1.162  30.512  1.00 11.46 ? 194 TYR A CB   1 
ATOM   1548 C  CG   . TYR A 1 193 ? -8.317  -1.602  29.219  1.00 10.08 ? 194 TYR A CG   1 
ATOM   1549 C  CD1  . TYR A 1 193 ? -9.000  -2.347  28.208  1.00 8.90  ? 194 TYR A CD1  1 
ATOM   1550 C  CD2  . TYR A 1 193 ? -6.998  -1.222  29.030  1.00 10.38 ? 194 TYR A CD2  1 
ATOM   1551 C  CE1  . TYR A 1 193 ? -8.354  -2.652  26.976  1.00 8.37  ? 194 TYR A CE1  1 
ATOM   1552 C  CE2  . TYR A 1 193 ? -6.306  -1.509  27.809  1.00 9.27  ? 194 TYR A CE2  1 
ATOM   1553 C  CZ   . TYR A 1 193 ? -7.000  -2.272  26.824  1.00 7.30  ? 194 TYR A CZ   1 
ATOM   1554 O  OH   . TYR A 1 193 ? -6.342  -2.512  25.673  1.00 11.42 ? 194 TYR A OH   1 
ATOM   1555 N  N    . PRO A 1 194 ? -8.159  2.035   30.179  1.00 12.67 ? 195 PRO A N    1 
ATOM   1556 C  CA   . PRO A 1 194 ? -7.333  3.030   29.520  1.00 13.31 ? 195 PRO A CA   1 
ATOM   1557 C  C    . PRO A 1 194 ? -6.131  2.342   28.861  1.00 11.32 ? 195 PRO A C    1 
ATOM   1558 O  O    . PRO A 1 194 ? -5.450  1.546   29.548  1.00 10.94 ? 195 PRO A O    1 
ATOM   1559 C  CB   . PRO A 1 194 ? -6.882  3.950   30.702  1.00 14.79 ? 195 PRO A CB   1 
ATOM   1560 C  CG   . PRO A 1 194 ? -6.919  3.042   31.907  1.00 15.20 ? 195 PRO A CG   1 
ATOM   1561 C  CD   . PRO A 1 194 ? -8.014  2.093   31.659  1.00 14.29 ? 195 PRO A CD   1 
ATOM   1562 N  N    . GLY A 1 195 ? -5.869  2.615   27.582  1.00 11.19 ? 196 GLY A N    1 
ATOM   1563 C  CA   . GLY A 1 195 ? -4.677  2.027   26.882  1.00 10.69 ? 196 GLY A CA   1 
ATOM   1564 C  C    . GLY A 1 195 ? -4.174  2.946   25.780  1.00 11.56 ? 196 GLY A C    1 
ATOM   1565 O  O    . GLY A 1 195 ? -4.153  4.227   25.928  1.00 12.11 ? 196 GLY A O    1 
ATOM   1566 N  N    . SER A 1 196 ? -3.748  2.310   24.687  1.00 12.63 ? 197 SER A N    1 
ATOM   1567 C  CA   . SER A 1 196 ? -2.982  2.967   23.594  1.00 12.09 ? 197 SER A CA   1 
ATOM   1568 C  C    . SER A 1 196 ? -3.426  2.535   22.217  1.00 11.92 ? 197 SER A C    1 
ATOM   1569 O  O    . SER A 1 196 ? -4.184  1.568   22.063  1.00 11.26 ? 197 SER A O    1 
ATOM   1570 C  CB   . SER A 1 196 ? -1.505  2.545   23.689  1.00 13.16 ? 197 SER A CB   1 
ATOM   1571 O  OG   . SER A 1 196 ? -1.299  1.106   23.391  1.00 10.65 ? 197 SER A OG   1 
ATOM   1572 N  N    . LEU A 1 197 ? -2.871  3.195   21.173  1.00 10.21 ? 198 LEU A N    1 
ATOM   1573 C  CA   . LEU A 1 197 ? -2.898  2.636   19.852  1.00 11.22 ? 198 LEU A CA   1 
ATOM   1574 C  C    . LEU A 1 197 ? -2.205  1.301   19.910  1.00 11.49 ? 198 LEU A C    1 
ATOM   1575 O  O    . LEU A 1 197 ? -1.249  1.164   20.664  1.00 13.69 ? 198 LEU A O    1 
ATOM   1576 C  CB   . LEU A 1 197 ? -2.082  3.518   18.913  1.00 12.51 ? 198 LEU A CB   1 
ATOM   1577 C  CG   . LEU A 1 197 ? -2.434  4.997   18.738  1.00 15.26 ? 198 LEU A CG   1 
ATOM   1578 C  CD1  . LEU A 1 197 ? -1.611  5.523   17.515  1.00 19.97 ? 198 LEU A CD1  1 
ATOM   1579 C  CD2  . LEU A 1 197 ? -3.864  5.335   18.583  1.00 12.62 ? 198 LEU A CD2  1 
ATOM   1580 N  N    . THR A 1 198 ? -2.664  0.317   19.126  1.00 10.15 ? 199 THR A N    1 
ATOM   1581 C  CA   . THR A 1 198 ? -1.941  -0.950  19.145  1.00 10.82 ? 199 THR A CA   1 
ATOM   1582 C  C    . THR A 1 198 ? -0.930  -1.035  17.987  1.00 11.02 ? 199 THR A C    1 
ATOM   1583 O  O    . THR A 1 198 ? -0.340  -2.132  17.757  1.00 11.34 ? 199 THR A O    1 
ATOM   1584 C  CB   . THR A 1 198 ? -2.921  -2.157  18.937  1.00 8.17  ? 199 THR A CB   1 
ATOM   1585 O  OG1  . THR A 1 198 ? -3.493  -2.066  17.644  1.00 11.26 ? 199 THR A OG1  1 
ATOM   1586 C  CG2  . THR A 1 198 ? -3.999  -2.191  20.042  1.00 8.01  ? 199 THR A CG2  1 
ATOM   1587 N  N    . THR A 1 199 ? -0.839  0.036   17.186  1.00 12.25 ? 200 THR A N    1 
ATOM   1588 C  CA   . THR A 1 199 ? 0.185   0.123   16.118  1.00 11.98 ? 200 THR A CA   1 
ATOM   1589 C  C    . THR A 1 199 ? 1.103   1.267   16.516  1.00 13.47 ? 200 THR A C    1 
ATOM   1590 O  O    . THR A 1 199 ? 0.677   2.187   17.209  1.00 11.45 ? 200 THR A O    1 
ATOM   1591 C  CB   . THR A 1 199 ? -0.421  0.457   14.734  1.00 13.82 ? 200 THR A CB   1 
ATOM   1592 O  OG1  . THR A 1 199 ? -1.170  1.698   14.762  1.00 14.41 ? 200 THR A OG1  1 
ATOM   1593 C  CG2  . THR A 1 199 ? -1.399  -0.631  14.302  1.00 12.43 ? 200 THR A CG2  1 
ATOM   1594 N  N    . PRO A 1 200 ? 2.337   1.277   15.980  1.00 14.48 ? 201 PRO A N    1 
ATOM   1595 C  CA   . PRO A 1 200 ? 3.129   2.535   16.055  1.00 14.80 ? 201 PRO A CA   1 
ATOM   1596 C  C    . PRO A 1 200 ? 2.281   3.713   15.549  1.00 13.97 ? 201 PRO A C    1 
ATOM   1597 O  O    . PRO A 1 200 ? 1.547   3.608   14.555  1.00 16.49 ? 201 PRO A O    1 
ATOM   1598 C  CB   . PRO A 1 200 ? 4.305   2.240   15.078  1.00 11.61 ? 201 PRO A CB   1 
ATOM   1599 C  CG   . PRO A 1 200 ? 4.576   0.794   15.339  1.00 16.21 ? 201 PRO A CG   1 
ATOM   1600 C  CD   . PRO A 1 200 ? 3.079   0.182   15.287  1.00 15.07 ? 201 PRO A CD   1 
ATOM   1601 N  N    . PRO A 1 201 ? 2.416   4.887   16.167  1.00 15.64 ? 202 PRO A N    1 
ATOM   1602 C  CA   . PRO A 1 201 ? 3.308   5.277   17.275  1.00 16.00 ? 202 PRO A CA   1 
ATOM   1603 C  C    . PRO A 1 201 ? 2.928   4.909   18.715  1.00 14.61 ? 202 PRO A C    1 
ATOM   1604 O  O    . PRO A 1 201 ? 3.606   5.379   19.664  1.00 16.58 ? 202 PRO A O    1 
ATOM   1605 C  CB   . PRO A 1 201 ? 3.446   6.800   17.074  1.00 16.42 ? 202 PRO A CB   1 
ATOM   1606 C  CG   . PRO A 1 201 ? 2.190   7.200   16.444  1.00 16.47 ? 202 PRO A CG   1 
ATOM   1607 C  CD   . PRO A 1 201 ? 1.697   6.033   15.601  1.00 14.89 ? 202 PRO A CD   1 
ATOM   1608 N  N    . LEU A 1 202 ? 1.931   3.990   18.870  1.00 13.95 ? 203 LEU A N    1 
ATOM   1609 C  CA   . LEU A 1 202 ? 1.647   3.389   20.165  1.00 11.60 ? 203 LEU A CA   1 
ATOM   1610 C  C    . LEU A 1 202 ? 1.284   4.450   21.295  1.00 12.60 ? 203 LEU A C    1 
ATOM   1611 O  O    . LEU A 1 202 ? 1.419   4.191   22.492  1.00 15.02 ? 203 LEU A O    1 
ATOM   1612 C  CB   . LEU A 1 202 ? 2.803   2.465   20.645  1.00 13.55 ? 203 LEU A CB   1 
ATOM   1613 C  CG   . LEU A 1 202 ? 3.180   1.257   19.777  1.00 15.49 ? 203 LEU A CG   1 
ATOM   1614 C  CD1  . LEU A 1 202 ? 4.361   0.489   20.472  1.00 12.61 ? 203 LEU A CD1  1 
ATOM   1615 C  CD2  . LEU A 1 202 ? 1.942   0.279   19.553  1.00 12.37 ? 203 LEU A CD2  1 
ATOM   1616 N  N    . LEU A 1 203 ? 0.760   5.597   20.873  1.00 12.05 ? 204 LEU A N    1 
ATOM   1617 C  CA   . LEU A 1 203 ? 0.448   6.721   21.792  1.00 12.39 ? 204 LEU A CA   1 
ATOM   1618 C  C    . LEU A 1 203 ? -0.610  6.272   22.797  1.00 12.81 ? 204 LEU A C    1 
ATOM   1619 O  O    . LEU A 1 203 ? -1.545  5.508   22.449  1.00 12.46 ? 204 LEU A O    1 
ATOM   1620 C  CB   . LEU A 1 203 ? -0.005  7.952   20.925  1.00 12.45 ? 204 LEU A CB   1 
ATOM   1621 C  CG   . LEU A 1 203 ? 1.086   8.516   19.970  1.00 12.28 ? 204 LEU A CG   1 
ATOM   1622 C  CD1  . LEU A 1 203 ? 0.619   9.566   18.928  1.00 16.64 ? 204 LEU A CD1  1 
ATOM   1623 C  CD2  . LEU A 1 203 ? 2.259   9.092   20.804  1.00 20.68 ? 204 LEU A CD2  1 
ATOM   1624 N  N    . GLU A 1 204 ? -0.423  6.680   24.056  1.00 11.43 ? 205 GLU A N    1 
ATOM   1625 C  CA   . GLU A 1 204 ? -1.278  6.314   25.158  1.00 14.09 ? 205 GLU A CA   1 
ATOM   1626 C  C    . GLU A 1 204 ? -2.478  7.280   25.323  1.00 15.17 ? 205 GLU A C    1 
ATOM   1627 O  O    . GLU A 1 204 ? -2.621  7.990   26.361  1.00 15.81 ? 205 GLU A O    1 
ATOM   1628 C  CB   . GLU A 1 204 ? -0.433  6.177   26.463  1.00 12.75 ? 205 GLU A CB   1 
ATOM   1629 C  CG   . GLU A 1 204 ? 0.430   4.896   26.343  1.00 14.64 ? 205 GLU A CG   1 
ATOM   1630 C  CD   . GLU A 1 204 ? 1.326   4.668   27.517  1.00 17.35 ? 205 GLU A CD   1 
ATOM   1631 O  OE1  . GLU A 1 204 ? 1.601   5.646   28.247  1.00 21.86 ? 205 GLU A OE1  1 
ATOM   1632 O  OE2  . GLU A 1 204 ? 1.768   3.546   27.725  1.00 13.55 ? 205 GLU A OE2  1 
ATOM   1633 N  N    . CYS A 1 205 ? -3.358  7.231   24.300  1.00 12.92 ? 206 CYS A N    1 
ATOM   1634 C  CA   . CYS A 1 205 ? -4.430  8.223   24.109  1.00 13.22 ? 206 CYS A CA   1 
ATOM   1635 C  C    . CYS A 1 205 ? -5.832  7.588   24.006  1.00 12.58 ? 206 CYS A C    1 
ATOM   1636 O  O    . CYS A 1 205 ? -6.801  8.276   23.676  1.00 11.63 ? 206 CYS A O    1 
ATOM   1637 C  CB   . CYS A 1 205 ? -4.141  9.004   22.835  1.00 14.49 ? 206 CYS A CB   1 
ATOM   1638 S  SG   . CYS A 1 205 ? -4.093  8.021   21.278  1.00 14.39 ? 206 CYS A SG   1 
ATOM   1639 N  N    . VAL A 1 206 ? -5.943  6.262   24.243  1.00 10.32 ? 207 VAL A N    1 
ATOM   1640 C  CA   . VAL A 1 206 ? -7.191  5.515   23.979  1.00 10.76 ? 207 VAL A CA   1 
ATOM   1641 C  C    . VAL A 1 206 ? -8.006  5.072   25.203  1.00 9.32  ? 207 VAL A C    1 
ATOM   1642 O  O    . VAL A 1 206 ? -7.516  4.441   26.105  1.00 13.32 ? 207 VAL A O    1 
ATOM   1643 C  CB   . VAL A 1 206 ? -6.918  4.248   23.055  1.00 9.88  ? 207 VAL A CB   1 
ATOM   1644 C  CG1  . VAL A 1 206 ? -8.315  3.559   22.726  1.00 9.83  ? 207 VAL A CG1  1 
ATOM   1645 C  CG2  . VAL A 1 206 ? -6.096  4.682   21.740  1.00 11.47 ? 207 VAL A CG2  1 
ATOM   1646 N  N    . THR A 1 207 ? -9.281  5.383   25.205  1.00 12.18 ? 208 THR A N    1 
ATOM   1647 C  CA   . THR A 1 207 ? -10.223 4.683   26.083  1.00 10.99 ? 208 THR A CA   1 
ATOM   1648 C  C    . THR A 1 207 ? -10.744 3.473   25.263  1.00 11.59 ? 208 THR A C    1 
ATOM   1649 O  O    . THR A 1 207 ? -11.430 3.657   24.254  1.00 11.50 ? 208 THR A O    1 
ATOM   1650 C  CB   . THR A 1 207 ? -11.371 5.616   26.562  1.00 12.20 ? 208 THR A CB   1 
ATOM   1651 O  OG1  . THR A 1 207 ? -10.807 6.661   27.398  1.00 10.10 ? 208 THR A OG1  1 
ATOM   1652 C  CG2  . THR A 1 207 ? -12.411 4.805   27.341  1.00 10.68 ? 208 THR A CG2  1 
ATOM   1653 N  N    . TRP A 1 208 ? -10.375 2.259   25.666  1.00 10.59 ? 209 TRP A N    1 
ATOM   1654 C  CA   . TRP A 1 208 ? -10.808 1.069   24.944  1.00 11.05 ? 209 TRP A CA   1 
ATOM   1655 C  C    . TRP A 1 208 ? -12.182 0.633   25.452  1.00 12.49 ? 209 TRP A C    1 
ATOM   1656 O  O    . TRP A 1 208 ? -12.406 0.613   26.675  1.00 12.26 ? 209 TRP A O    1 
ATOM   1657 C  CB   . TRP A 1 208 ? -9.800  -0.102  25.190  1.00 10.98 ? 209 TRP A CB   1 
ATOM   1658 C  CG   . TRP A 1 208 ? -8.699  0.080   24.190  1.00 8.74  ? 209 TRP A CG   1 
ATOM   1659 C  CD1  . TRP A 1 208 ? -7.464  0.691   24.376  1.00 10.04 ? 209 TRP A CD1  1 
ATOM   1660 C  CD2  . TRP A 1 208 ? -8.760  -0.325  22.826  1.00 12.54 ? 209 TRP A CD2  1 
ATOM   1661 N  NE1  . TRP A 1 208 ? -6.775  0.694   23.183  1.00 10.24 ? 209 TRP A NE1  1 
ATOM   1662 C  CE2  . TRP A 1 208 ? -7.533  0.044   22.227  1.00 9.33  ? 209 TRP A CE2  1 
ATOM   1663 C  CE3  . TRP A 1 208 ? -9.741  -0.977  22.054  1.00 8.31  ? 209 TRP A CE3  1 
ATOM   1664 C  CZ2  . TRP A 1 208 ? -7.258  -0.177  20.855  1.00 8.87  ? 209 TRP A CZ2  1 
ATOM   1665 C  CZ3  . TRP A 1 208 ? -9.467  -1.278  20.703  1.00 9.20  ? 209 TRP A CZ3  1 
ATOM   1666 C  CH2  . TRP A 1 208 ? -8.208  -0.890  20.107  1.00 8.98  ? 209 TRP A CH2  1 
ATOM   1667 N  N    . ILE A 1 209 ? -13.060 0.395   24.515  1.00 12.08 ? 210 ILE A N    1 
ATOM   1668 C  CA   . ILE A 1 209 ? -14.460 -0.127  24.791  1.00 11.69 ? 210 ILE A CA   1 
ATOM   1669 C  C    . ILE A 1 209 ? -14.648 -1.440  23.996  1.00 10.94 ? 210 ILE A C    1 
ATOM   1670 O  O    . ILE A 1 209 ? -14.760 -1.383  22.816  1.00 11.14 ? 210 ILE A O    1 
ATOM   1671 C  CB   . ILE A 1 209 ? -15.552 0.932   24.469  1.00 11.38 ? 210 ILE A CB   1 
ATOM   1672 C  CG1  . ILE A 1 209 ? -15.324 2.192   25.296  1.00 13.96 ? 210 ILE A CG1  1 
ATOM   1673 C  CG2  . ILE A 1 209 ? -17.046 0.301   24.812  1.00 12.66 ? 210 ILE A CG2  1 
ATOM   1674 C  CD1  . ILE A 1 209 ? -15.919 3.463   24.688  1.00 15.04 ? 210 ILE A CD1  1 
ATOM   1675 N  N    . VAL A 1 210 ? -14.533 -2.608  24.653  1.00 11.71 ? 211 VAL A N    1 
ATOM   1676 C  CA   . VAL A 1 210 ? -14.457 -3.897  23.954  1.00 10.09 ? 211 VAL A CA   1 
ATOM   1677 C  C    . VAL A 1 210 ? -15.810 -4.600  24.200  1.00 11.26 ? 211 VAL A C    1 
ATOM   1678 O  O    . VAL A 1 210 ? -16.170 -4.808  25.395  1.00 11.81 ? 211 VAL A O    1 
ATOM   1679 C  CB   . VAL A 1 210 ? -13.219 -4.723  24.411  1.00 11.70 ? 211 VAL A CB   1 
ATOM   1680 C  CG1  . VAL A 1 210 ? -13.206 -6.069  23.709  1.00 10.26 ? 211 VAL A CG1  1 
ATOM   1681 C  CG2  . VAL A 1 210 ? -11.901 -3.940  24.025  1.00 8.44  ? 211 VAL A CG2  1 
ATOM   1682 N  N    . LEU A 1 211 ? -16.535 -4.871  23.111  1.00 11.24 ? 212 LEU A N    1 
ATOM   1683 C  CA   . LEU A 1 211 ? -17.838 -5.571  23.226  1.00 11.39 ? 212 LEU A CA   1 
ATOM   1684 C  C    . LEU A 1 211 ? -17.679 -7.028  23.662  1.00 12.45 ? 212 LEU A C    1 
ATOM   1685 O  O    . LEU A 1 211 ? -16.844 -7.728  23.124  1.00 12.95 ? 212 LEU A O    1 
ATOM   1686 C  CB   . LEU A 1 211 ? -18.655 -5.473  21.926  1.00 10.99 ? 212 LEU A CB   1 
ATOM   1687 C  CG   . LEU A 1 211 ? -19.060 -4.036  21.491  1.00 11.00 ? 212 LEU A CG   1 
ATOM   1688 C  CD1  . LEU A 1 211 ? -20.156 -4.194  20.349  1.00 14.25 ? 212 LEU A CD1  1 
ATOM   1689 C  CD2  . LEU A 1 211 ? -19.607 -3.140  22.681  1.00 10.62 ? 212 LEU A CD2  1 
ATOM   1690 N  N    . LYS A 1 212 ? -18.489 -7.469  24.642  1.00 12.70 ? 213 LYS A N    1 
ATOM   1691 C  CA   . LYS A 1 212 ? -18.464 -8.904  25.051  1.00 15.24 ? 213 LYS A CA   1 
ATOM   1692 C  C    . LYS A 1 212 ? -18.958 -9.879  23.972  1.00 12.73 ? 213 LYS A C    1 
ATOM   1693 O  O    . LYS A 1 212 ? -18.502 -11.052 23.864  1.00 14.11 ? 213 LYS A O    1 
ATOM   1694 C  CB   . LYS A 1 212 ? -19.217 -9.094  26.412  1.00 17.14 ? 213 LYS A CB   1 
ATOM   1695 C  CG   . LYS A 1 212 ? -19.463 -10.582 26.757  1.00 20.64 ? 213 LYS A CG   1 
ATOM   1696 C  CD   . LYS A 1 212 ? -20.730 -10.859 27.567  1.00 23.56 ? 213 LYS A CD   1 
ATOM   1697 C  CE   . LYS A 1 212 ? -20.740 -12.361 28.045  1.00 29.80 ? 213 LYS A CE   1 
ATOM   1698 N  NZ   . LYS A 1 212 ? -21.902 -12.549 29.034  1.00 35.06 ? 213 LYS A NZ   1 
ATOM   1699 N  N    . GLU A 1 213 ? -19.921 -9.435  23.178  1.00 13.87 ? 214 GLU A N    1 
ATOM   1700 C  CA   . GLU A 1 213 ? -20.533 -10.299 22.154  1.00 14.00 ? 214 GLU A CA   1 
ATOM   1701 C  C    . GLU A 1 213 ? -19.786 -10.190 20.799  1.00 12.58 ? 214 GLU A C    1 
ATOM   1702 O  O    . GLU A 1 213 ? -19.780 -9.096  20.174  1.00 13.83 ? 214 GLU A O    1 
ATOM   1703 C  CB   . GLU A 1 213 ? -21.987 -9.896  21.940  1.00 14.08 ? 214 GLU A CB   1 
ATOM   1704 C  CG   . GLU A 1 213 ? -22.707 -10.819 20.935  1.00 17.16 ? 214 GLU A CG   1 
ATOM   1705 C  CD   . GLU A 1 213 ? -24.269 -10.434 20.789  1.00 18.21 ? 214 GLU A CD   1 
ATOM   1706 O  OE1  . GLU A 1 213 ? -24.897 -10.733 19.755  1.00 28.49 ? 214 GLU A OE1  1 
ATOM   1707 O  OE2  . GLU A 1 213 ? -24.761 -9.774  21.673  1.00 19.50 ? 214 GLU A OE2  1 
ATOM   1708 N  N    . PRO A 1 214 ? -19.206 -11.325 20.307  1.00 12.10 ? 215 PRO A N    1 
ATOM   1709 C  CA   . PRO A 1 214 ? -18.578 -11.281 18.964  1.00 12.51 ? 215 PRO A CA   1 
ATOM   1710 C  C    . PRO A 1 214 ? -19.623 -11.242 17.855  1.00 14.18 ? 215 PRO A C    1 
ATOM   1711 O  O    . PRO A 1 214 ? -20.824 -11.596 18.096  1.00 16.14 ? 215 PRO A O    1 
ATOM   1712 C  CB   . PRO A 1 214 ? -17.718 -12.562 18.883  1.00 14.23 ? 215 PRO A CB   1 
ATOM   1713 C  CG   . PRO A 1 214 ? -18.477 -13.586 19.829  1.00 15.32 ? 215 PRO A CG   1 
ATOM   1714 C  CD   . PRO A 1 214 ? -19.245 -12.683 20.909  1.00 12.10 ? 215 PRO A CD   1 
ATOM   1715 N  N    . ILE A 1 215 ? -19.210 -10.821 16.660  1.00 11.91 ? 216 ILE A N    1 
ATOM   1716 C  CA   . ILE A 1 215 ? -20.014 -11.094 15.494  1.00 13.30 ? 216 ILE A CA   1 
ATOM   1717 C  C    . ILE A 1 215 ? -19.467 -12.309 14.799  1.00 13.72 ? 216 ILE A C    1 
ATOM   1718 O  O    . ILE A 1 215 ? -18.285 -12.675 14.970  1.00 13.63 ? 216 ILE A O    1 
ATOM   1719 C  CB   . ILE A 1 215 ? -20.030 -9.874  14.523  1.00 12.12 ? 216 ILE A CB   1 
ATOM   1720 C  CG1  . ILE A 1 215 ? -18.594 -9.505  14.062  1.00 12.56 ? 216 ILE A CG1  1 
ATOM   1721 C  CG2  . ILE A 1 215 ? -20.737 -8.516  15.220  1.00 14.20 ? 216 ILE A CG2  1 
ATOM   1722 C  CD1  . ILE A 1 215 ? -18.635 -8.416  12.863  1.00 12.62 ? 216 ILE A CD1  1 
ATOM   1723 N  N    . SER A 1 216 ? -20.310 -12.998 14.027  1.00 14.93 ? 217 SER A N    1 
ATOM   1724 C  CA   A SER A 1 216 ? -19.833 -14.111 13.191  0.50 14.34 ? 217 SER A CA   1 
ATOM   1725 C  CA   B SER A 1 216 ? -19.740 -14.060 13.193  0.50 14.69 ? 217 SER A CA   1 
ATOM   1726 C  C    . SER A 1 216 ? -19.677 -13.659 11.737  1.00 14.40 ? 217 SER A C    1 
ATOM   1727 O  O    . SER A 1 216 ? -20.569 -12.892 11.182  1.00 14.04 ? 217 SER A O    1 
ATOM   1728 C  CB   A SER A 1 216 ? -20.766 -15.329 13.276  0.50 15.85 ? 217 SER A CB   1 
ATOM   1729 C  CB   B SER A 1 216 ? -20.437 -15.397 13.347  0.50 16.17 ? 217 SER A CB   1 
ATOM   1730 O  OG   A SER A 1 216 ? -20.925 -15.761 14.632  0.50 14.73 ? 217 SER A OG   1 
ATOM   1731 O  OG   B SER A 1 216 ? -21.814 -15.217 13.161  0.50 17.43 ? 217 SER A OG   1 
ATOM   1732 N  N    . VAL A 1 217 ? -18.596 -14.121 11.139  1.00 13.78 ? 218 VAL A N    1 
ATOM   1733 C  CA   . VAL A 1 217 ? -18.269 -13.914 9.750   1.00 13.63 ? 218 VAL A CA   1 
ATOM   1734 C  C    . VAL A 1 217 ? -18.016 -15.300 9.170   1.00 14.09 ? 218 VAL A C    1 
ATOM   1735 O  O    . VAL A 1 217 ? -17.652 -16.250 9.922   1.00 15.06 ? 218 VAL A O    1 
ATOM   1736 C  CB   . VAL A 1 217 ? -16.993 -13.016 9.490   1.00 15.59 ? 218 VAL A CB   1 
ATOM   1737 C  CG1  . VAL A 1 217 ? -17.212 -11.607 9.947   1.00 14.07 ? 218 VAL A CG1  1 
ATOM   1738 C  CG2  . VAL A 1 217 ? -15.710 -13.621 10.183  1.00 13.19 ? 218 VAL A CG2  1 
ATOM   1739 N  N    . SER A 1 218 ? -18.230 -15.445 7.871   1.00 13.67 ? 219 SER A N    1 
ATOM   1740 C  CA   . SER A 1 218 ? -18.058 -16.779 7.246   1.00 13.30 ? 219 SER A CA   1 
ATOM   1741 C  C    . SER A 1 218 ? -16.581 -17.038 6.956   1.00 12.91 ? 219 SER A C    1 
ATOM   1742 O  O    . SER A 1 218 ? -15.760 -16.118 6.908   1.00 9.62  ? 219 SER A O    1 
ATOM   1743 C  CB   . SER A 1 218 ? -18.852 -16.946 5.967   1.00 12.73 ? 219 SER A CB   1 
ATOM   1744 O  OG   . SER A 1 218 ? -18.346 -16.109 4.949   1.00 13.43 ? 219 SER A OG   1 
ATOM   1745 N  N    . SER A 1 219 ? -16.223 -18.305 6.817   1.00 13.13 ? 220 SER A N    1 
ATOM   1746 C  CA   . SER A 1 219 ? -14.843 -18.643 6.461   1.00 13.76 ? 220 SER A CA   1 
ATOM   1747 C  C    . SER A 1 219 ? -14.436 -17.926 5.133   1.00 15.85 ? 220 SER A C    1 
ATOM   1748 O  O    . SER A 1 219 ? -13.290 -17.488 4.964   1.00 14.21 ? 220 SER A O    1 
ATOM   1749 C  CB   . SER A 1 219 ? -14.689 -20.198 6.406   1.00 15.25 ? 220 SER A CB   1 
ATOM   1750 O  OG   . SER A 1 219 ? -15.636 -20.764 5.459   1.00 18.35 ? 220 SER A OG   1 
ATOM   1751 N  N    . GLU A 1 220 ? -15.374 -17.813 4.164   1.00 15.21 ? 221 GLU A N    1 
ATOM   1752 C  CA   . GLU A 1 220 ? -15.061 -17.170 2.858   1.00 16.11 ? 221 GLU A CA   1 
ATOM   1753 C  C    . GLU A 1 220 ? -14.799 -15.689 3.031   1.00 14.26 ? 221 GLU A C    1 
ATOM   1754 O  O    . GLU A 1 220 ? -13.959 -15.138 2.296   1.00 13.82 ? 221 GLU A O    1 
ATOM   1755 C  CB   . GLU A 1 220 ? -16.224 -17.302 1.868   1.00 17.32 ? 221 GLU A CB   1 
ATOM   1756 C  CG   . GLU A 1 220 ? -16.467 -18.755 1.391   1.00 21.82 ? 221 GLU A CG   1 
ATOM   1757 C  CD   . GLU A 1 220 ? -17.368 -19.521 2.310   1.00 25.23 ? 221 GLU A CD   1 
ATOM   1758 O  OE1  . GLU A 1 220 ? -17.961 -18.996 3.283   1.00 21.33 ? 221 GLU A OE1  1 
ATOM   1759 O  OE2  . GLU A 1 220 ? -17.511 -20.739 2.041   1.00 34.39 ? 221 GLU A OE2  1 
ATOM   1760 N  N    . GLN A 1 221 ? -15.533 -15.049 3.938   1.00 13.06 ? 222 GLN A N    1 
ATOM   1761 C  CA   . GLN A 1 221 ? -15.312 -13.581 4.183   1.00 13.94 ? 222 GLN A CA   1 
ATOM   1762 C  C    . GLN A 1 221 ? -13.864 -13.332 4.738   1.00 15.41 ? 222 GLN A C    1 
ATOM   1763 O  O    . GLN A 1 221 ? -13.116 -12.483 4.235   1.00 11.38 ? 222 GLN A O    1 
ATOM   1764 C  CB   . GLN A 1 221 ? -16.377 -13.072 5.141   1.00 14.21 ? 222 GLN A CB   1 
ATOM   1765 C  CG   . GLN A 1 221 ? -17.721 -12.795 4.408   1.00 13.45 ? 222 GLN A CG   1 
ATOM   1766 C  CD   . GLN A 1 221 ? -18.828 -12.310 5.314   1.00 14.39 ? 222 GLN A CD   1 
ATOM   1767 O  OE1  . GLN A 1 221 ? -18.915 -12.733 6.479   1.00 14.72 ? 222 GLN A OE1  1 
ATOM   1768 N  NE2  . GLN A 1 221 ? -19.779 -11.501 4.745   1.00 12.63 ? 222 GLN A NE2  1 
ATOM   1769 N  N    . VAL A 1 222 ? -13.443 -14.174 5.700   1.00 14.25 ? 223 VAL A N    1 
ATOM   1770 C  CA   . VAL A 1 222 ? -12.108 -13.971 6.328   1.00 16.21 ? 223 VAL A CA   1 
ATOM   1771 C  C    . VAL A 1 222 ? -10.991 -14.414 5.369   1.00 16.09 ? 223 VAL A C    1 
ATOM   1772 O  O    . VAL A 1 222 ? -9.957  -13.796 5.283   1.00 14.72 ? 223 VAL A O    1 
ATOM   1773 C  CB   . VAL A 1 222 ? -12.028 -14.555 7.766   1.00 18.31 ? 223 VAL A CB   1 
ATOM   1774 C  CG1  . VAL A 1 222 ? -12.097 -16.029 7.787   1.00 17.59 ? 223 VAL A CG1  1 
ATOM   1775 C  CG2  . VAL A 1 222 ? -10.751 -14.021 8.515   1.00 19.83 ? 223 VAL A CG2  1 
ATOM   1776 N  N    . LEU A 1 223 ? -11.275 -15.425 4.560   1.00 16.14 ? 224 LEU A N    1 
ATOM   1777 C  CA   . LEU A 1 223 ? -10.354 -15.857 3.537   1.00 17.32 ? 224 LEU A CA   1 
ATOM   1778 C  C    . LEU A 1 223 ? -10.019 -14.734 2.536   1.00 17.72 ? 224 LEU A C    1 
ATOM   1779 O  O    . LEU A 1 223 ? -8.880  -14.632 2.094   1.00 18.14 ? 224 LEU A O    1 
ATOM   1780 C  CB   . LEU A 1 223 ? -10.933 -17.062 2.778   1.00 18.54 ? 224 LEU A CB   1 
ATOM   1781 C  CG   . LEU A 1 223 ? -9.878  -17.666 1.882   1.00 25.05 ? 224 LEU A CG   1 
ATOM   1782 C  CD1  . LEU A 1 223 ? -8.936  -18.481 2.784   1.00 28.39 ? 224 LEU A CD1  1 
ATOM   1783 C  CD2  . LEU A 1 223 ? -10.591 -18.555 0.822   1.00 29.72 ? 224 LEU A CD2  1 
ATOM   1784 N  N    . LYS A 1 224 ? -11.024 -13.904 2.187   1.00 14.93 ? 225 LYS A N    1 
ATOM   1785 C  CA   . LYS A 1 224 ? -10.795 -12.742 1.373   1.00 16.18 ? 225 LYS A CA   1 
ATOM   1786 C  C    . LYS A 1 224 ? -9.894  -11.662 2.041   1.00 14.56 ? 225 LYS A C    1 
ATOM   1787 O  O    . LYS A 1 224 ? -9.095  -11.042 1.329   1.00 13.78 ? 225 LYS A O    1 
ATOM   1788 C  CB   . LYS A 1 224 ? -12.098 -12.222 0.783   1.00 15.62 ? 225 LYS A CB   1 
ATOM   1789 C  CG   . LYS A 1 224 ? -12.604 -13.236 -0.308  1.00 21.70 ? 225 LYS A CG   1 
ATOM   1790 C  CD   . LYS A 1 224 ? -13.999 -12.929 -0.796  1.00 29.86 ? 225 LYS A CD   1 
ATOM   1791 C  CE   . LYS A 1 224 ? -14.526 -14.031 -1.798  1.00 28.04 ? 225 LYS A CE   1 
ATOM   1792 N  NZ   . LYS A 1 224 ? -15.703 -13.391 -2.552  1.00 33.79 ? 225 LYS A NZ   1 
ATOM   1793 N  N    . PHE A 1 225 ? -10.006 -11.439 3.365   1.00 12.42 ? 226 PHE A N    1 
ATOM   1794 C  CA   . PHE A 1 225 ? -9.011  -10.590 4.089   1.00 12.38 ? 226 PHE A CA   1 
ATOM   1795 C  C    . PHE A 1 225 ? -7.596  -11.076 3.857   1.00 12.93 ? 226 PHE A C    1 
ATOM   1796 O  O    . PHE A 1 225 ? -6.645  -10.279 3.677   1.00 11.12 ? 226 PHE A O    1 
ATOM   1797 C  CB   . PHE A 1 225 ? -9.215  -10.628 5.644   1.00 11.33 ? 226 PHE A CB   1 
ATOM   1798 C  CG   . PHE A 1 225 ? -10.449 -9.854  6.142   1.00 12.57 ? 226 PHE A CG   1 
ATOM   1799 C  CD1  . PHE A 1 225 ? -11.471 -9.459  5.294   1.00 14.75 ? 226 PHE A CD1  1 
ATOM   1800 C  CD2  . PHE A 1 225 ? -10.594 -9.643  7.542   1.00 12.83 ? 226 PHE A CD2  1 
ATOM   1801 C  CE1  . PHE A 1 225 ? -12.595 -8.790  5.824   1.00 18.66 ? 226 PHE A CE1  1 
ATOM   1802 C  CE2  . PHE A 1 225 ? -11.681 -8.973  8.050   1.00 18.61 ? 226 PHE A CE2  1 
ATOM   1803 C  CZ   . PHE A 1 225 ? -12.675 -8.536  7.176   1.00 16.68 ? 226 PHE A CZ   1 
ATOM   1804 N  N    . ARG A 1 226 ? -7.428  -12.408 3.924   1.00 13.33 ? 227 ARG A N    1 
ATOM   1805 C  CA   . ARG A 1 226 ? -6.079  -13.064 3.749   1.00 13.91 ? 227 ARG A CA   1 
ATOM   1806 C  C    . ARG A 1 226 ? -5.403  -13.053 2.341   1.00 14.05 ? 227 ARG A C    1 
ATOM   1807 O  O    . ARG A 1 226 ? -4.228  -13.439 2.240   1.00 17.78 ? 227 ARG A O    1 
ATOM   1808 C  CB   . ARG A 1 226 ? -6.088  -14.502 4.287   1.00 12.75 ? 227 ARG A CB   1 
ATOM   1809 C  CG   . ARG A 1 226 ? -6.599  -14.624 5.735   1.00 12.67 ? 227 ARG A CG   1 
ATOM   1810 C  CD   . ARG A 1 226 ? -6.515  -16.070 6.244   1.00 14.74 ? 227 ARG A CD   1 
ATOM   1811 N  NE   . ARG A 1 226 ? -7.054  -16.187 7.619   1.00 16.20 ? 227 ARG A NE   1 
ATOM   1812 C  CZ   . ARG A 1 226 ? -7.981  -17.087 7.939   1.00 18.31 ? 227 ARG A CZ   1 
ATOM   1813 N  NH1  . ARG A 1 226 ? -8.395  -17.991 7.014   1.00 19.15 ? 227 ARG A NH1  1 
ATOM   1814 N  NH2  . ARG A 1 226 ? -8.446  -17.146 9.160   1.00 14.14 ? 227 ARG A NH2  1 
ATOM   1815 N  N    . LYS A 1 227 ? -6.125  -12.579 1.331   1.00 14.99 ? 228 LYS A N    1 
ATOM   1816 C  CA   . LYS A 1 227 ? -5.645  -12.455 -0.028  1.00 16.01 ? 228 LYS A CA   1 
ATOM   1817 C  C    . LYS A 1 227 ? -4.997  -11.098 -0.266  1.00 15.38 ? 228 LYS A C    1 
ATOM   1818 O  O    . LYS A 1 227 ? -4.262  -10.923 -1.220  1.00 14.48 ? 228 LYS A O    1 
ATOM   1819 C  CB   . LYS A 1 227 ? -6.832  -12.699 -1.019  1.00 14.70 ? 228 LYS A CB   1 
ATOM   1820 C  CG   . LYS A 1 227 ? -7.118  -14.171 -1.170  1.00 21.99 ? 228 LYS A CG   1 
ATOM   1821 C  CD   . LYS A 1 227 ? -8.378  -14.321 -2.091  1.00 31.95 ? 228 LYS A CD   1 
ATOM   1822 C  CE   . LYS A 1 227 ? -8.536  -15.710 -2.815  1.00 36.59 ? 228 LYS A CE   1 
ATOM   1823 N  NZ   . LYS A 1 227 ? -8.951  -16.894 -1.954  1.00 40.49 ? 228 LYS A NZ   1 
ATOM   1824 N  N    . LEU A 1 228 ? -5.186  -10.167 0.669   1.00 15.97 ? 229 LEU A N    1 
ATOM   1825 C  CA   . LEU A 1 228 ? -4.538  -8.856  0.567   1.00 15.30 ? 229 LEU A CA   1 
ATOM   1826 C  C    . LEU A 1 228 ? -3.043  -9.000  0.770   1.00 14.35 ? 229 LEU A C    1 
ATOM   1827 O  O    . LEU A 1 228 ? -2.566  -10.022 1.290   1.00 13.07 ? 229 LEU A O    1 
ATOM   1828 C  CB   . LEU A 1 228 ? -5.067  -7.969  1.682   1.00 16.40 ? 229 LEU A CB   1 
ATOM   1829 C  CG   . LEU A 1 228 ? -6.465  -7.396  1.532   1.00 15.05 ? 229 LEU A CG   1 
ATOM   1830 C  CD1  . LEU A 1 228 ? -6.916  -6.755  2.842   1.00 12.80 ? 229 LEU A CD1  1 
ATOM   1831 C  CD2  . LEU A 1 228 ? -6.477  -6.379  0.432   1.00 15.38 ? 229 LEU A CD2  1 
ATOM   1832 N  N    . ASN A 1 229 ? -2.313  -7.928  0.429   1.00 16.43 ? 230 ASN A N    1 
ATOM   1833 C  CA   . ASN A 1 229 ? -0.835  -7.897  0.454   1.00 16.10 ? 230 ASN A CA   1 
ATOM   1834 C  C    . ASN A 1 229 ? -0.309  -6.702  1.351   1.00 16.47 ? 230 ASN A C    1 
ATOM   1835 O  O    . ASN A 1 229 ? -0.822  -5.588  1.240   1.00 17.32 ? 230 ASN A O    1 
ATOM   1836 C  CB   . ASN A 1 229 ? -0.318  -7.632  -0.987  1.00 16.93 ? 230 ASN A CB   1 
ATOM   1837 C  CG   . ASN A 1 229 ? -0.396  -8.884  -1.933  1.00 20.05 ? 230 ASN A CG   1 
ATOM   1838 O  OD1  . ASN A 1 229 ? 0.148   -8.824  -3.044  1.00 21.47 ? 230 ASN A OD1  1 
ATOM   1839 N  ND2  . ASN A 1 229 ? -1.001  -9.998  -1.482  1.00 16.94 ? 230 ASN A ND2  1 
ATOM   1840 N  N    . PHE A 1 230 ? 0.745   -6.983  2.104   1.00 17.51 ? 231 PHE A N    1 
ATOM   1841 C  CA   . PHE A 1 230 ? 1.575   -6.025  2.915   1.00 17.77 ? 231 PHE A CA   1 
ATOM   1842 C  C    . PHE A 1 230 ? 2.468   -5.273  1.906   1.00 20.67 ? 231 PHE A C    1 
ATOM   1843 O  O    . PHE A 1 230 ? 2.802   -4.097  2.126   1.00 20.64 ? 231 PHE A O    1 
ATOM   1844 C  CB   . PHE A 1 230 ? 2.548   -6.750  3.811   1.00 18.89 ? 231 PHE A CB   1 
ATOM   1845 C  CG   . PHE A 1 230 ? 1.942   -7.315  5.156   1.00 16.10 ? 231 PHE A CG   1 
ATOM   1846 C  CD1  . PHE A 1 230 ? 1.125   -6.530  5.954   1.00 17.82 ? 231 PHE A CD1  1 
ATOM   1847 C  CD2  . PHE A 1 230 ? 2.282   -8.625  5.570   1.00 16.33 ? 231 PHE A CD2  1 
ATOM   1848 C  CE1  . PHE A 1 230 ? 0.635   -7.078  7.204   1.00 18.98 ? 231 PHE A CE1  1 
ATOM   1849 C  CE2  . PHE A 1 230 ? 1.841   -9.167  6.765   1.00 16.85 ? 231 PHE A CE2  1 
ATOM   1850 C  CZ   . PHE A 1 230 ? 1.016   -8.395  7.577   1.00 13.72 ? 231 PHE A CZ   1 
ATOM   1851 N  N    . ASN A 1 231 ? 2.891   -5.960  0.837   1.00 19.57 ? 232 ASN A N    1 
ATOM   1852 C  CA   . ASN A 1 231 ? 3.826   -5.290  -0.150  1.00 20.97 ? 232 ASN A CA   1 
ATOM   1853 C  C    . ASN A 1 231 ? 3.141   -4.357  -1.101  1.00 21.03 ? 232 ASN A C    1 
ATOM   1854 O  O    . ASN A 1 231 ? 1.901   -4.434  -1.308  1.00 19.72 ? 232 ASN A O    1 
ATOM   1855 C  CB   . ASN A 1 231 ? 4.502   -6.369  -0.989  1.00 20.91 ? 232 ASN A CB   1 
ATOM   1856 C  CG   . ASN A 1 231 ? 3.500   -7.276  -1.597  1.00 20.65 ? 232 ASN A CG   1 
ATOM   1857 O  OD1  . ASN A 1 231 ? 3.084   -8.240  -0.949  1.00 22.43 ? 232 ASN A OD1  1 
ATOM   1858 N  ND2  . ASN A 1 231 ? 3.107   -6.999  -2.872  1.00 20.73 ? 232 ASN A ND2  1 
ATOM   1859 N  N    . GLY A 1 232 ? 3.918   -3.477  -1.746  1.00 22.24 ? 233 GLY A N    1 
ATOM   1860 C  CA   . GLY A 1 232 ? 3.393   -2.716  -2.865  1.00 25.25 ? 233 GLY A CA   1 
ATOM   1861 C  C    . GLY A 1 232 ? 3.392   -3.499  -4.194  1.00 27.75 ? 233 GLY A C    1 
ATOM   1862 O  O    . GLY A 1 232 ? 4.169   -4.457  -4.368  1.00 28.35 ? 233 GLY A O    1 
ATOM   1863 N  N    . GLU A 1 233 ? 2.525   -3.076  -5.109  1.00 30.25 ? 234 GLU A N    1 
ATOM   1864 C  CA   . GLU A 1 233 ? 2.461   -3.600  -6.486  1.00 33.29 ? 234 GLU A CA   1 
ATOM   1865 C  C    . GLU A 1 233 ? 3.846   -3.753  -7.105  1.00 33.25 ? 234 GLU A C    1 
ATOM   1866 O  O    . GLU A 1 233 ? 4.700   -2.867  -6.988  1.00 32.85 ? 234 GLU A O    1 
ATOM   1867 C  CB   . GLU A 1 233 ? 1.580   -2.732  -7.381  1.00 33.00 ? 234 GLU A CB   1 
ATOM   1868 C  CG   . GLU A 1 233 ? 0.963   -3.516  -8.567  1.00 35.36 ? 234 GLU A CG   1 
ATOM   1869 C  CD   . GLU A 1 233 ? 0.269   -2.655  -9.610  1.00 35.99 ? 234 GLU A CD   1 
ATOM   1870 O  OE1  . GLU A 1 233 ? -0.230  -1.549  -9.300  1.00 39.17 ? 234 GLU A OE1  1 
ATOM   1871 O  OE2  . GLU A 1 233 ? 0.240   -3.077  -10.784 1.00 40.73 ? 234 GLU A OE2  1 
ATOM   1872 N  N    . GLY A 1 234 ? 4.100   -4.919  -7.687  1.00 32.65 ? 235 GLY A N    1 
ATOM   1873 C  CA   . GLY A 1 234 ? 5.406   -5.168  -8.244  1.00 33.18 ? 235 GLY A CA   1 
ATOM   1874 C  C    . GLY A 1 234 ? 6.552   -5.491  -7.329  1.00 33.23 ? 235 GLY A C    1 
ATOM   1875 O  O    . GLY A 1 234 ? 7.695   -5.432  -7.790  1.00 32.79 ? 235 GLY A O    1 
ATOM   1876 N  N    . GLU A 1 235 ? 6.297   -5.801  -6.033  1.00 33.32 ? 236 GLU A N    1 
ATOM   1877 C  CA   . GLU A 1 235 ? 7.350   -6.347  -5.099  1.00 33.76 ? 236 GLU A CA   1 
ATOM   1878 C  C    . GLU A 1 235 ? 6.954   -7.794  -4.724  1.00 31.23 ? 236 GLU A C    1 
ATOM   1879 O  O    . GLU A 1 235 ? 5.794   -8.156  -4.996  1.00 32.57 ? 236 GLU A O    1 
ATOM   1880 C  CB   . GLU A 1 235 ? 7.501   -5.507  -3.798  1.00 33.98 ? 236 GLU A CB   1 
ATOM   1881 C  CG   . GLU A 1 235 ? 7.232   -4.010  -3.975  1.00 36.23 ? 236 GLU A CG   1 
ATOM   1882 C  CD   . GLU A 1 235 ? 7.239   -3.266  -2.652  1.00 38.31 ? 236 GLU A CD   1 
ATOM   1883 O  OE1  . GLU A 1 235 ? 6.663   -3.798  -1.665  1.00 43.35 ? 236 GLU A OE1  1 
ATOM   1884 O  OE2  . GLU A 1 235 ? 7.827   -2.160  -2.586  1.00 42.60 ? 236 GLU A OE2  1 
ATOM   1885 N  N    . PRO A 1 236 ? 7.891   -8.625  -4.165  1.00 30.13 ? 237 PRO A N    1 
ATOM   1886 C  CA   . PRO A 1 236 ? 7.539   -10.017 -3.809  1.00 28.30 ? 237 PRO A CA   1 
ATOM   1887 C  C    . PRO A 1 236 ? 6.265   -10.070 -2.942  1.00 27.61 ? 237 PRO A C    1 
ATOM   1888 O  O    . PRO A 1 236 ? 6.090   -9.234  -2.014  1.00 26.95 ? 237 PRO A O    1 
ATOM   1889 C  CB   . PRO A 1 236 ? 8.749   -10.491 -3.016  1.00 29.66 ? 237 PRO A CB   1 
ATOM   1890 C  CG   . PRO A 1 236 ? 9.906   -9.701  -3.558  1.00 29.46 ? 237 PRO A CG   1 
ATOM   1891 C  CD   . PRO A 1 236 ? 9.321   -8.342  -3.859  1.00 29.99 ? 237 PRO A CD   1 
ATOM   1892 N  N    . GLU A 1 237 ? 5.344   -10.973 -3.283  1.00 25.26 ? 238 GLU A N    1 
ATOM   1893 C  CA   . GLU A 1 237 ? 4.102   -11.056 -2.544  1.00 22.93 ? 238 GLU A CA   1 
ATOM   1894 C  C    . GLU A 1 237 ? 4.321   -11.552 -1.101  1.00 21.34 ? 238 GLU A C    1 
ATOM   1895 O  O    . GLU A 1 237 ? 4.861   -12.608 -0.881  1.00 20.91 ? 238 GLU A O    1 
ATOM   1896 C  CB   . GLU A 1 237 ? 3.057   -11.925 -3.317  1.00 23.60 ? 238 GLU A CB   1 
ATOM   1897 C  CG   . GLU A 1 237 ? 1.752   -12.069 -2.574  1.00 22.52 ? 238 GLU A CG   1 
ATOM   1898 C  CD   . GLU A 1 237 ? 0.589   -12.765 -3.310  1.00 23.82 ? 238 GLU A CD   1 
ATOM   1899 O  OE1  . GLU A 1 237 ? 0.806   -13.809 -3.966  1.00 26.97 ? 238 GLU A OE1  1 
ATOM   1900 O  OE2  . GLU A 1 237 ? -0.573  -12.274 -3.220  1.00 18.87 ? 238 GLU A OE2  1 
ATOM   1901 N  N    . GLU A 1 238 ? 3.834   -10.779 -0.123  1.00 20.85 ? 239 GLU A N    1 
ATOM   1902 C  CA   . GLU A 1 238 ? 3.781   -11.153 1.262   1.00 21.25 ? 239 GLU A CA   1 
ATOM   1903 C  C    . GLU A 1 238 ? 2.298   -10.996 1.682   1.00 17.99 ? 239 GLU A C    1 
ATOM   1904 O  O    . GLU A 1 238 ? 1.711   -9.887  1.646   1.00 17.59 ? 239 GLU A O    1 
ATOM   1905 C  CB   . GLU A 1 238 ? 4.719   -10.270 2.125   1.00 20.30 ? 239 GLU A CB   1 
ATOM   1906 C  CG   . GLU A 1 238 ? 6.215   -10.909 2.279   1.00 26.55 ? 239 GLU A CG   1 
ATOM   1907 C  CD   . GLU A 1 238 ? 7.200   -10.095 3.155   1.00 28.48 ? 239 GLU A CD   1 
ATOM   1908 O  OE1  . GLU A 1 238 ? 7.187   -10.261 4.436   1.00 29.08 ? 239 GLU A OE1  1 
ATOM   1909 O  OE2  . GLU A 1 238 ? 7.967   -9.257  2.559   1.00 29.74 ? 239 GLU A OE2  1 
ATOM   1910 N  N    . LEU A 1 239 ? 1.641   -12.119 1.958   1.00 16.74 ? 240 LEU A N    1 
ATOM   1911 C  CA   . LEU A 1 239 ? 0.190   -11.997 2.250   1.00 15.42 ? 240 LEU A CA   1 
ATOM   1912 C  C    . LEU A 1 239 ? -0.035  -11.215 3.559   1.00 14.07 ? 240 LEU A C    1 
ATOM   1913 O  O    . LEU A 1 239 ? 0.693   -11.396 4.540   1.00 14.92 ? 240 LEU A O    1 
ATOM   1914 C  CB   . LEU A 1 239 ? -0.410  -13.384 2.419   1.00 15.42 ? 240 LEU A CB   1 
ATOM   1915 C  CG   . LEU A 1 239 ? -0.462  -14.267 1.175   1.00 16.42 ? 240 LEU A CG   1 
ATOM   1916 C  CD1  . LEU A 1 239 ? -1.225  -15.563 1.538   1.00 21.21 ? 240 LEU A CD1  1 
ATOM   1917 C  CD2  . LEU A 1 239 ? -1.155  -13.534 0.075   1.00 13.75 ? 240 LEU A CD2  1 
ATOM   1918 N  N    . MET A 1 240 ? -1.084  -10.393 3.547   1.00 14.25 ? 241 MET A N    1 
ATOM   1919 C  CA   . MET A 1 240 ? -1.522  -9.580  4.716   1.00 13.73 ? 241 MET A CA   1 
ATOM   1920 C  C    . MET A 1 240 ? -2.278  -10.477 5.684   1.00 12.09 ? 241 MET A C    1 
ATOM   1921 O  O    . MET A 1 240 ? -3.517  -10.602 5.598   1.00 12.95 ? 241 MET A O    1 
ATOM   1922 C  CB   . MET A 1 240 ? -2.349  -8.356  4.312   1.00 14.11 ? 241 MET A CB   1 
ATOM   1923 C  CG   . MET A 1 240 ? -2.642  -7.383  5.579   1.00 13.00 ? 241 MET A CG   1 
ATOM   1924 S  SD   . MET A 1 240 ? -3.548  -5.993  5.017   1.00 18.30 ? 241 MET A SD   1 
ATOM   1925 C  CE   . MET A 1 240 ? -2.254  -4.965  4.286   1.00 22.11 ? 241 MET A CE   1 
ATOM   1926 N  N    . VAL A 1 241 ? -1.503  -11.102 6.558   1.00 12.53 ? 242 VAL A N    1 
ATOM   1927 C  CA   . VAL A 1 241 ? -2.021  -11.994 7.622   1.00 12.07 ? 242 VAL A CA   1 
ATOM   1928 C  C    . VAL A 1 241 ? -1.205  -11.796 8.907   1.00 12.73 ? 242 VAL A C    1 
ATOM   1929 O  O    . VAL A 1 241 ? 0.005   -11.454 8.856   1.00 12.22 ? 242 VAL A O    1 
ATOM   1930 C  CB   . VAL A 1 241 ? -1.989  -13.542 7.241   1.00 11.21 ? 242 VAL A CB   1 
ATOM   1931 C  CG1  . VAL A 1 241 ? -3.012  -13.824 6.053   1.00 14.87 ? 242 VAL A CG1  1 
ATOM   1932 C  CG2  . VAL A 1 241 ? -0.522  -13.996 6.952   1.00 14.51 ? 242 VAL A CG2  1 
ATOM   1933 N  N    . ASP A 1 242 ? -1.835  -12.090 10.055  1.00 9.53  ? 243 ASP A N    1 
ATOM   1934 C  CA   . ASP A 1 242 ? -1.196  -11.950 11.372  1.00 9.64  ? 243 ASP A CA   1 
ATOM   1935 C  C    . ASP A 1 242 ? -0.697  -10.515 11.584  1.00 9.69  ? 243 ASP A C    1 
ATOM   1936 O  O    . ASP A 1 242 ? 0.417   -10.338 12.037  1.00 13.10 ? 243 ASP A O    1 
ATOM   1937 C  CB   . ASP A 1 242 ? -0.060  -13.013 11.689  1.00 10.36 ? 243 ASP A CB   1 
ATOM   1938 C  CG   . ASP A 1 242 ? -0.578  -14.385 11.684  1.00 12.43 ? 243 ASP A CG   1 
ATOM   1939 O  OD1  . ASP A 1 242 ? -1.647  -14.627 12.307  1.00 10.30 ? 243 ASP A OD1  1 
ATOM   1940 O  OD2  . ASP A 1 242 ? 0.035   -15.273 11.061  1.00 14.30 ? 243 ASP A OD2  1 
ATOM   1941 N  N    . ASN A 1 243 ? -1.557  -9.536  11.328  1.00 9.81  ? 244 ASN A N    1 
ATOM   1942 C  CA   . ASN A 1 243 ? -1.236  -8.058  11.532  1.00 8.62  ? 244 ASN A CA   1 
ATOM   1943 C  C    . ASN A 1 243 ? -1.857  -7.691  12.927  1.00 10.57 ? 244 ASN A C    1 
ATOM   1944 O  O    . ASN A 1 243 ? -2.544  -6.689  13.035  1.00 11.18 ? 244 ASN A O    1 
ATOM   1945 C  CB   . ASN A 1 243 ? -1.809  -7.177  10.398  1.00 11.21 ? 244 ASN A CB   1 
ATOM   1946 C  CG   . ASN A 1 243 ? -3.318  -7.430  10.117  1.00 13.53 ? 244 ASN A CG   1 
ATOM   1947 O  OD1  . ASN A 1 243 ? -3.891  -8.387  10.637  1.00 12.39 ? 244 ASN A OD1  1 
ATOM   1948 N  ND2  . ASN A 1 243 ? -3.958  -6.533  9.357   1.00 14.36 ? 244 ASN A ND2  1 
ATOM   1949 N  N    . TRP A 1 244 ? -1.557  -8.480  13.936  1.00 9.09  ? 245 TRP A N    1 
ATOM   1950 C  CA   . TRP A 1 244 ? -2.022  -8.218  15.319  1.00 10.06 ? 245 TRP A CA   1 
ATOM   1951 C  C    . TRP A 1 244 ? -0.836  -8.128  16.251  1.00 12.23 ? 245 TRP A C    1 
ATOM   1952 O  O    . TRP A 1 244 ? 0.222   -8.831  16.077  1.00 12.17 ? 245 TRP A O    1 
ATOM   1953 C  CB   . TRP A 1 244 ? -3.044  -9.308  15.742  1.00 9.98  ? 245 TRP A CB   1 
ATOM   1954 C  CG   . TRP A 1 244 ? -2.559  -10.746 15.557  1.00 8.91  ? 245 TRP A CG   1 
ATOM   1955 C  CD1  . TRP A 1 244 ? -2.691  -11.504 14.434  1.00 7.33  ? 245 TRP A CD1  1 
ATOM   1956 C  CD2  . TRP A 1 244 ? -2.012  -11.599 16.564  1.00 9.70  ? 245 TRP A CD2  1 
ATOM   1957 N  NE1  . TRP A 1 244 ? -2.192  -12.781 14.655  1.00 11.52 ? 245 TRP A NE1  1 
ATOM   1958 C  CE2  . TRP A 1 244 ? -1.745  -12.846 15.952  1.00 11.82 ? 245 TRP A CE2  1 
ATOM   1959 C  CE3  . TRP A 1 244 ? -1.743  -11.447 17.953  1.00 10.50 ? 245 TRP A CE3  1 
ATOM   1960 C  CZ2  . TRP A 1 244 ? -1.195  -13.958 16.673  1.00 9.69  ? 245 TRP A CZ2  1 
ATOM   1961 C  CZ3  . TRP A 1 244 ? -1.119  -12.542 18.652  1.00 9.94  ? 245 TRP A CZ3  1 
ATOM   1962 C  CH2  . TRP A 1 244 ? -0.931  -13.784 18.000  1.00 10.10 ? 245 TRP A CH2  1 
ATOM   1963 N  N    . ARG A 1 245 ? -0.967  -7.221  17.229  1.00 10.95 ? 246 ARG A N    1 
ATOM   1964 C  CA   . ARG A 1 245 ? -0.084  -7.113  18.365  1.00 11.83 ? 246 ARG A CA   1 
ATOM   1965 C  C    . ARG A 1 245 ? -0.577  -7.992  19.502  1.00 11.32 ? 246 ARG A C    1 
ATOM   1966 O  O    . ARG A 1 245 ? -1.753  -7.962  19.834  1.00 13.05 ? 246 ARG A O    1 
ATOM   1967 C  CB   . ARG A 1 245 ? -0.008  -5.642  18.906  1.00 11.81 ? 246 ARG A CB   1 
ATOM   1968 C  CG   . ARG A 1 245 ? 1.134   -5.431  19.875  1.00 13.50 ? 246 ARG A CG   1 
ATOM   1969 C  CD   . ARG A 1 245 ? 1.119   -4.056  20.552  1.00 13.16 ? 246 ARG A CD   1 
ATOM   1970 N  NE   . ARG A 1 245 ? 2.363   -3.785  21.330  1.00 12.29 ? 246 ARG A NE   1 
ATOM   1971 C  CZ   . ARG A 1 245 ? 2.558   -2.765  22.159  1.00 17.16 ? 246 ARG A CZ   1 
ATOM   1972 N  NH1  . ARG A 1 245 ? 1.569   -1.925  22.462  1.00 11.19 ? 246 ARG A NH1  1 
ATOM   1973 N  NH2  . ARG A 1 245 ? 3.756   -2.583  22.714  1.00 17.32 ? 246 ARG A NH2  1 
ATOM   1974 N  N    . PRO A 1 246 ? 0.310   -8.821  20.082  1.00 11.83 ? 247 PRO A N    1 
ATOM   1975 C  CA   A PRO A 1 246 ? -0.093  -9.677  21.210  0.50 12.15 ? 247 PRO A CA   1 
ATOM   1976 C  CA   B PRO A 1 246 ? -0.080  -9.681  21.204  0.50 12.03 ? 247 PRO A CA   1 
ATOM   1977 C  C    . PRO A 1 246 ? -0.384  -8.883  22.497  1.00 12.53 ? 247 PRO A C    1 
ATOM   1978 O  O    . PRO A 1 246 ? -0.002  -7.700  22.641  1.00 12.47 ? 247 PRO A O    1 
ATOM   1979 C  CB   A PRO A 1 246 ? 1.128   -10.566 21.426  0.50 13.33 ? 247 PRO A CB   1 
ATOM   1980 C  CB   B PRO A 1 246 ? 1.136   -10.602 21.380  0.50 13.26 ? 247 PRO A CB   1 
ATOM   1981 C  CG   A PRO A 1 246 ? 2.255   -9.719  20.949  0.50 12.50 ? 247 PRO A CG   1 
ATOM   1982 C  CG   B PRO A 1 246 ? 1.970   -10.409 20.069  0.50 11.58 ? 247 PRO A CG   1 
ATOM   1983 C  CD   A PRO A 1 246 ? 1.740   -8.985  19.763  0.50 12.58 ? 247 PRO A CD   1 
ATOM   1984 C  CD   B PRO A 1 246 ? 1.731   -8.992  19.728  0.50 12.49 ? 247 PRO A CD   1 
ATOM   1985 N  N    . ALA A 1 247 ? -1.083  -9.532  23.428  1.00 12.17 ? 248 ALA A N    1 
ATOM   1986 C  CA   . ALA A 1 247 ? -1.391  -8.958  24.719  1.00 11.15 ? 248 ALA A CA   1 
ATOM   1987 C  C    . ALA A 1 247 ? -0.177  -8.426  25.481  1.00 13.31 ? 248 ALA A C    1 
ATOM   1988 O  O    . ALA A 1 247 ? 0.911   -9.074  25.518  1.00 11.33 ? 248 ALA A O    1 
ATOM   1989 C  CB   . ALA A 1 247 ? -2.143  -10.070 25.590  1.00 13.08 ? 248 ALA A CB   1 
ATOM   1990 N  N    . GLN A 1 248 ? -0.356  -7.245  26.074  1.00 12.48 ? 249 GLN A N    1 
ATOM   1991 C  CA   . GLN A 1 248 ? 0.716   -6.526  26.736  1.00 15.40 ? 249 GLN A CA   1 
ATOM   1992 C  C    . GLN A 1 248 ? 0.425   -6.542  28.212  1.00 16.63 ? 249 GLN A C    1 
ATOM   1993 O  O    . GLN A 1 248 ? -0.700  -6.795  28.632  1.00 16.82 ? 249 GLN A O    1 
ATOM   1994 C  CB   . GLN A 1 248 ? 0.724   -5.079  26.250  1.00 14.40 ? 249 GLN A CB   1 
ATOM   1995 C  CG   . GLN A 1 248 ? 1.110   -4.881  24.736  1.00 13.19 ? 249 GLN A CG   1 
ATOM   1996 C  CD   . GLN A 1 248 ? 2.408   -5.596  24.392  1.00 16.44 ? 249 GLN A CD   1 
ATOM   1997 O  OE1  . GLN A 1 248 ? 3.535   -5.233  24.928  1.00 17.17 ? 249 GLN A OE1  1 
ATOM   1998 N  NE2  . GLN A 1 248 ? 2.316   -6.604  23.458  1.00 14.09 ? 249 GLN A NE2  1 
ATOM   1999 N  N    . PRO A 1 249 ? 1.447   -6.254  29.036  1.00 18.35 ? 250 PRO A N    1 
ATOM   2000 C  CA   . PRO A 1 249 ? 1.222   -6.281  30.465  1.00 17.98 ? 250 PRO A CA   1 
ATOM   2001 C  C    . PRO A 1 249 ? 0.113   -5.318  30.960  1.00 17.07 ? 250 PRO A C    1 
ATOM   2002 O  O    . PRO A 1 249 ? 0.165   -4.143  30.598  1.00 18.58 ? 250 PRO A O    1 
ATOM   2003 C  CB   . PRO A 1 249 ? 2.569   -5.790  31.011  1.00 19.01 ? 250 PRO A CB   1 
ATOM   2004 C  CG   . PRO A 1 249 ? 3.564   -6.147  29.947  1.00 19.12 ? 250 PRO A CG   1 
ATOM   2005 C  CD   . PRO A 1 249 ? 2.849   -5.947  28.676  1.00 17.59 ? 250 PRO A CD   1 
ATOM   2006 N  N    . LEU A 1 250 ? -0.807  -5.784  31.800  1.00 16.30 ? 251 LEU A N    1 
ATOM   2007 C  CA   . LEU A 1 250 ? -1.834  -4.906  32.415  1.00 18.52 ? 251 LEU A CA   1 
ATOM   2008 C  C    . LEU A 1 250 ? -1.259  -3.826  33.354  1.00 19.20 ? 251 LEU A C    1 
ATOM   2009 O  O    . LEU A 1 250 ? -1.759  -2.682  33.370  1.00 17.26 ? 251 LEU A O    1 
ATOM   2010 C  CB   . LEU A 1 250 ? -2.934  -5.696  33.116  1.00 19.67 ? 251 LEU A CB   1 
ATOM   2011 C  CG   . LEU A 1 250 ? -4.234  -4.998  33.503  1.00 16.68 ? 251 LEU A CG   1 
ATOM   2012 C  CD1  . LEU A 1 250 ? -5.019  -4.370  32.346  1.00 17.49 ? 251 LEU A CD1  1 
ATOM   2013 C  CD2  . LEU A 1 250 ? -5.146  -5.976  34.320  1.00 21.32 ? 251 LEU A CD2  1 
ATOM   2014 N  N    . LYS A 1 251 ? -0.165  -4.157  34.060  1.00 19.17 ? 252 LYS A N    1 
ATOM   2015 C  CA   . LYS A 1 251 ? 0.488   -3.159  34.991  1.00 20.98 ? 252 LYS A CA   1 
ATOM   2016 C  C    . LYS A 1 251 ? -0.529  -2.569  35.992  1.00 22.05 ? 252 LYS A C    1 
ATOM   2017 O  O    . LYS A 1 251 ? -1.340  -3.291  36.566  1.00 24.99 ? 252 LYS A O    1 
ATOM   2018 C  CB   . LYS A 1 251 ? 1.297   -2.102  34.207  1.00 20.81 ? 252 LYS A CB   1 
ATOM   2019 C  CG   . LYS A 1 251 ? 2.406   -2.764  33.366  1.00 24.11 ? 252 LYS A CG   1 
ATOM   2020 C  CD   . LYS A 1 251 ? 3.422   -1.836  32.855  1.00 27.10 ? 252 LYS A CD   1 
ATOM   2021 C  CE   . LYS A 1 251 ? 4.546   -2.601  32.221  1.00 29.64 ? 252 LYS A CE   1 
ATOM   2022 N  NZ   . LYS A 1 251 ? 5.420   -1.621  31.477  1.00 29.63 ? 252 LYS A NZ   1 
ATOM   2023 N  N    . ASN A 1 252 ? -0.525  -1.276  36.218  1.00 23.59 ? 253 ASN A N    1 
ATOM   2024 C  CA   . ASN A 1 252 ? -1.429  -0.782  37.249  0.01 25.68 ? 253 ASN A CA   1 
ATOM   2025 C  C    . ASN A 1 252 ? -2.769  -0.358  36.663  1.00 27.77 ? 253 ASN A C    1 
ATOM   2026 O  O    . ASN A 1 252 ? -3.027  0.888   36.616  1.00 29.81 ? 253 ASN A O    1 
ATOM   2027 C  CB   . ASN A 1 252 ? -0.781  0.364   38.038  0.01 25.65 ? 253 ASN A CB   1 
ATOM   2028 C  CG   . ASN A 1 252 ? 0.470   -0.070  38.788  0.01 25.60 ? 253 ASN A CG   1 
ATOM   2029 O  OD1  . ASN A 1 252 ? 0.556   -1.193  39.288  0.01 25.52 ? 253 ASN A OD1  1 
ATOM   2030 N  ND2  . ASN A 1 252 ? 1.444   0.829   38.877  0.01 25.48 ? 253 ASN A ND2  1 
ATOM   2031 N  N    . ARG A 1 253 ? -3.562  -1.334  36.122  1.00 25.36 ? 254 ARG A N    1 
ATOM   2032 C  CA   . ARG A 1 253 ? -4.887  -0.997  35.542  1.00 21.10 ? 254 ARG A CA   1 
ATOM   2033 C  C    . ARG A 1 253 ? -5.978  -1.973  35.923  1.00 22.08 ? 254 ARG A C    1 
ATOM   2034 O  O    . ARG A 1 253 ? -5.703  -3.180  36.008  1.00 24.30 ? 254 ARG A O    1 
ATOM   2035 C  CB   . ARG A 1 253 ? -4.824  -0.889  33.984  1.00 21.28 ? 254 ARG A CB   1 
ATOM   2036 C  CG   . ARG A 1 253 ? -3.885  0.179   33.471  1.00 14.92 ? 254 ARG A CG   1 
ATOM   2037 C  CD   . ARG A 1 253 ? -3.861  0.169   31.942  1.00 17.27 ? 254 ARG A CD   1 
ATOM   2038 N  NE   . ARG A 1 253 ? -2.954  -0.918  31.455  1.00 16.97 ? 254 ARG A NE   1 
ATOM   2039 C  CZ   . ARG A 1 253 ? -2.700  -1.129  30.158  1.00 15.59 ? 254 ARG A CZ   1 
ATOM   2040 N  NH1  . ARG A 1 253 ? -3.346  -0.376  29.286  1.00 9.07  ? 254 ARG A NH1  1 
ATOM   2041 N  NH2  . ARG A 1 253 ? -1.890  -2.128  29.758  1.00 12.24 ? 254 ARG A NH2  1 
ATOM   2042 N  N    . GLN A 1 254 ? -7.208  -1.452  36.106  1.00 22.19 ? 255 GLN A N    1 
ATOM   2043 C  CA   . GLN A 1 254 ? -8.455  -2.174  36.326  1.00 24.17 ? 255 GLN A CA   1 
ATOM   2044 C  C    . GLN A 1 254 ? -9.300  -2.131  35.034  1.00 23.02 ? 255 GLN A C    1 
ATOM   2045 O  O    . GLN A 1 254 ? -9.527  -1.054  34.445  1.00 22.28 ? 255 GLN A O    1 
ATOM   2046 C  CB   . GLN A 1 254 ? -9.272  -1.570  37.543  1.00 24.11 ? 255 GLN A CB   1 
ATOM   2047 C  CG   . GLN A 1 254 ? -10.131 -0.322  37.159  1.00 28.11 ? 255 GLN A CG   1 
ATOM   2048 C  CD   . GLN A 1 254 ? -10.787 0.485   38.332  1.00 30.60 ? 255 GLN A CD   1 
ATOM   2049 O  OE1  . GLN A 1 254 ? -10.286 1.596   38.710  1.00 30.66 ? 255 GLN A OE1  1 
ATOM   2050 N  NE2  . GLN A 1 254 ? -11.921 -0.052  38.884  1.00 33.31 ? 255 GLN A NE2  1 
ATOM   2051 N  N    . ILE A 1 255 ? -9.718  -3.303  34.572  1.00 20.96 ? 256 ILE A N    1 
ATOM   2052 C  CA   . ILE A 1 255 ? -10.665 -3.368  33.510  1.00 19.42 ? 256 ILE A CA   1 
ATOM   2053 C  C    . ILE A 1 255 ? -12.052 -3.370  34.209  1.00 20.41 ? 256 ILE A C    1 
ATOM   2054 O  O    . ILE A 1 255 ? -12.295 -4.153  35.157  1.00 18.91 ? 256 ILE A O    1 
ATOM   2055 C  CB   . ILE A 1 255 ? -10.457 -4.654  32.650  1.00 19.75 ? 256 ILE A CB   1 
ATOM   2056 C  CG1  . ILE A 1 255 ? -9.016  -4.653  32.074  1.00 17.17 ? 256 ILE A CG1  1 
ATOM   2057 C  CG2  . ILE A 1 255 ? -11.618 -4.866  31.597  1.00 17.24 ? 256 ILE A CG2  1 
ATOM   2058 C  CD1  . ILE A 1 255 ? -8.792  -5.964  31.261  1.00 18.61 ? 256 ILE A CD1  1 
ATOM   2059 N  N    . LYS A 1 256 ? -12.916 -2.444  33.768  1.00 18.26 ? 257 LYS A N    1 
ATOM   2060 C  CA   . LYS A 1 256 ? -14.296 -2.357  34.264  1.00 19.51 ? 257 LYS A CA   1 
ATOM   2061 C  C    . LYS A 1 256 ? -15.277 -3.059  33.324  1.00 20.24 ? 257 LYS A C    1 
ATOM   2062 O  O    . LYS A 1 256 ? -15.085 -3.048  32.093  1.00 20.25 ? 257 LYS A O    1 
ATOM   2063 C  CB   . LYS A 1 256 ? -14.695 -0.845  34.477  1.00 18.19 ? 257 LYS A CB   1 
ATOM   2064 C  CG   . LYS A 1 256 ? -13.860 -0.128  35.618  1.00 21.56 ? 257 LYS A CG   1 
ATOM   2065 C  CD   . LYS A 1 256 ? -13.722 1.373   35.369  0.01 19.82 ? 257 LYS A CD   1 
ATOM   2066 C  CE   . LYS A 1 256 ? -15.046 2.112   35.506  0.01 20.17 ? 257 LYS A CE   1 
ATOM   2067 N  NZ   . LYS A 1 256 ? -14.916 3.549   35.140  0.01 19.88 ? 257 LYS A NZ   1 
ATOM   2068 N  N    . ALA A 1 257 ? -16.351 -3.649  33.846  1.00 19.91 ? 258 ALA A N    1 
ATOM   2069 C  CA   . ALA A 1 257 ? -17.431 -4.175  33.008  1.00 19.89 ? 258 ALA A CA   1 
ATOM   2070 C  C    . ALA A 1 257 ? -18.753 -3.405  33.166  1.00 21.10 ? 258 ALA A C    1 
ATOM   2071 O  O    . ALA A 1 257 ? -19.114 -2.960  34.296  1.00 20.26 ? 258 ALA A O    1 
ATOM   2072 C  CB   . ALA A 1 257 ? -17.665 -5.674  33.267  1.00 21.54 ? 258 ALA A CB   1 
ATOM   2073 N  N    . SER A 1 258 ? -19.497 -3.307  32.070  1.00 19.84 ? 259 SER A N    1 
ATOM   2074 C  CA   . SER A 1 258 ? -20.855 -2.640  32.087  1.00 21.93 ? 259 SER A CA   1 
ATOM   2075 C  C    . SER A 1 258 ? -21.988 -3.577  32.512  1.00 22.51 ? 259 SER A C    1 
ATOM   2076 O  O    . SER A 1 258 ? -23.172 -3.185  32.439  1.00 24.09 ? 259 SER A O    1 
ATOM   2077 C  CB   . SER A 1 258 ? -21.205 -2.092  30.709  1.00 21.04 ? 259 SER A CB   1 
ATOM   2078 O  OG   . SER A 1 258 ? -21.558 -3.139  29.858  1.00 19.98 ? 259 SER A OG   1 
ATOM   2079 N  N    . PHE A 1 259 ? -21.635 -4.816  32.863  1.00 23.07 ? 260 PHE A N    1 
ATOM   2080 C  CA   . PHE A 1 259 ? -22.581 -5.987  32.984  1.00 24.27 ? 260 PHE A CA   1 
ATOM   2081 C  C    . PHE A 1 259 ? -22.076 -7.001  34.046  1.00 25.34 ? 260 PHE A C    1 
ATOM   2082 O  O    . PHE A 1 259 ? -20.873 -7.021  34.349  1.00 23.52 ? 260 PHE A O    1 
ATOM   2083 C  CB   . PHE A 1 259 ? -22.796 -6.710  31.625  1.00 24.73 ? 260 PHE A CB   1 
ATOM   2084 C  CG   . PHE A 1 259 ? -21.555 -7.497  31.126  1.00 24.95 ? 260 PHE A CG   1 
ATOM   2085 C  CD1  . PHE A 1 259 ? -20.595 -6.855  30.349  1.00 25.03 ? 260 PHE A CD1  1 
ATOM   2086 C  CD2  . PHE A 1 259 ? -21.337 -8.848  31.515  1.00 26.75 ? 260 PHE A CD2  1 
ATOM   2087 C  CE1  . PHE A 1 259 ? -19.415 -7.551  29.932  1.00 24.19 ? 260 PHE A CE1  1 
ATOM   2088 C  CE2  . PHE A 1 259 ? -20.185 -9.556  31.116  1.00 25.42 ? 260 PHE A CE2  1 
ATOM   2089 C  CZ   . PHE A 1 259 ? -19.226 -8.904  30.290  1.00 26.97 ? 260 PHE A CZ   1 
ATOM   2090 N  N    . LYS A 1 260 ? -23.031 -7.785  34.627  1.00 27.03 ? 261 LYS A N    1 
ATOM   2091 C  CA   . LYS A 1 260 ? -22.782 -8.865  35.621  1.00 27.14 ? 261 LYS A CA   1 
ATOM   2092 C  C    . LYS A 1 260 ? -22.886 -10.213 34.872  1.00 27.37 ? 261 LYS A C    1 
ATOM   2093 O  O    . LYS A 1 260 ? -23.610 -10.352 33.874  0.50 27.27 ? 261 LYS A O    1 
ATOM   2094 C  CB   . LYS A 1 260 ? -23.824 -8.831  36.736  0.01 27.15 ? 261 LYS A CB   1 
ATOM   2095 C  CG   . LYS A 1 260 ? -23.496 -7.897  37.885  0.01 27.10 ? 261 LYS A CG   1 
ATOM   2096 C  CD   . LYS A 1 260 ? -24.627 -7.831  38.912  0.01 27.07 ? 261 LYS A CD   1 
ATOM   2097 C  CE   . LYS A 1 260 ? -24.702 -9.085  39.781  0.01 26.95 ? 261 LYS A CE   1 
ATOM   2098 N  NZ   . LYS A 1 260 ? -23.526 -9.231  40.686  0.01 26.91 ? 261 LYS A NZ   1 
ATOM   2099 O  OXT  . LYS A 1 260 ? -22.244 -11.192 35.252  0.01 27.30 ? 261 LYS A OXT  1 
HETATM 2100 O  O1   . E36 B 2 .   ? -0.927  10.103  12.631  1.00 48.79 ? 262 E36 A O1   1 
HETATM 2101 C  C2   . E36 B 2 .   ? -0.093  10.655  13.650  1.00 49.04 ? 262 E36 A C2   1 
HETATM 2102 C  C3   . E36 B 2 .   ? -0.227  9.852   14.991  1.00 49.08 ? 262 E36 A C3   1 
HETATM 2103 O  O4   . E36 B 2 .   ? -1.362  9.005   15.023  1.00 46.31 ? 262 E36 A O4   1 
HETATM 2104 C  C5   . E36 B 2 .   ? -1.400  8.126   13.974  1.00 46.83 ? 262 E36 A C5   1 
HETATM 2105 C  C6   . E36 B 2 .   ? -1.138  8.725   12.627  1.00 47.26 ? 262 E36 A C6   1 
HETATM 2106 C  C7   . E36 B 2 .   ? -1.111  7.958   11.516  1.00 47.17 ? 262 E36 A C7   1 
HETATM 2107 C  C8   . E36 B 2 .   ? -1.332  6.511   11.728  1.00 47.79 ? 262 E36 A C8   1 
HETATM 2108 N  N9   . E36 B 2 .   ? -1.329  5.438   10.757  1.00 50.06 ? 262 E36 A N9   1 
HETATM 2109 C  C10  . E36 B 2 .   ? -1.548  4.362   11.453  1.00 47.51 ? 262 E36 A C10  1 
HETATM 2110 N  N11  . E36 B 2 .   ? -1.721  4.676   12.849  1.00 47.16 ? 262 E36 A N11  1 
HETATM 2111 C  C12  . E36 B 2 .   ? -1.562  6.027   12.932  1.00 46.42 ? 262 E36 A C12  1 
HETATM 2112 C  C13  . E36 B 2 .   ? -1.609  6.834   14.151  1.00 45.35 ? 262 E36 A C13  1 
HETATM 2113 S  S14  . E36 B 2 .   ? -1.700  2.664   10.859  1.00 43.34 ? 262 E36 A S14  1 
HETATM 2114 C  C15  . E36 B 2 .   ? -2.838  2.091   12.203  1.00 26.43 ? 262 E36 A C15  1 
HETATM 2115 C  C16  . E36 B 2 .   ? -4.081  3.048   12.307  1.00 19.76 ? 262 E36 A C16  1 
HETATM 2116 O  O17  . E36 B 2 .   ? -4.505  3.623   11.221  1.00 28.02 ? 262 E36 A O17  1 
HETATM 2117 C  C18  . E36 B 2 .   ? -4.775  3.260   13.659  1.00 15.17 ? 262 E36 A C18  1 
HETATM 2118 C  C19  . E36 B 2 .   ? -4.980  2.146   14.602  1.00 15.15 ? 262 E36 A C19  1 
HETATM 2119 C  C20  . E36 B 2 .   ? -5.586  2.366   15.788  1.00 11.37 ? 262 E36 A C20  1 
HETATM 2120 C  C21  . E36 B 2 .   ? -6.025  3.732   16.069  1.00 12.39 ? 262 E36 A C21  1 
HETATM 2121 C  C22  . E36 B 2 .   ? -5.882  4.760   15.219  1.00 12.95 ? 262 E36 A C22  1 
HETATM 2122 C  C23  . E36 B 2 .   ? -5.235  4.505   13.951  1.00 14.38 ? 262 E36 A C23  1 
HETATM 2123 S  S24  . E36 B 2 .   ? -5.886  0.930   16.856  1.00 12.26 ? 262 E36 A S24  1 
HETATM 2124 O  O25  . E36 B 2 .   ? -7.441  0.899   16.855  1.00 11.74 ? 262 E36 A O25  1 
HETATM 2125 CL CL26 . E36 B 2 .   ? -6.794  3.929   17.581  1.00 16.27 ? 262 E36 A CL26 1 
HETATM 2126 O  O27  . E36 B 2 .   ? -5.270  1.143   18.233  1.00 13.05 ? 262 E36 A O27  1 
HETATM 2127 N  N28  . E36 B 2 .   ? -5.190  -0.377  16.007  1.00 12.95 ? 262 E36 A N28  1 
HETATM 2128 ZN ZN   . ZN  C 3 .   ? -6.596  -1.616  15.328  1.00 10.01 ? 263 ZN  A ZN   1 
HETATM 2129 S  S    . DMS D 4 .   ? 1.442   -11.723 15.055  1.00 25.24 ? 264 DMS A S    1 
HETATM 2130 O  O    . DMS D 4 .   ? 1.875   -11.495 16.790  1.00 26.39 ? 264 DMS A O    1 
HETATM 2131 C  C1   . DMS D 4 .   ? 2.340   -10.534 14.017  1.00 29.45 ? 264 DMS A C1   1 
HETATM 2132 C  C2   . DMS D 4 .   ? 2.193   -13.256 14.583  1.00 19.87 ? 264 DMS A C2   1 
HETATM 2133 S  S    . DMS E 4 .   ? -5.626  7.354   10.982  1.00 36.04 ? 265 DMS A S    1 
HETATM 2134 O  O    . DMS E 4 .   ? -6.914  6.304   10.400  1.00 35.44 ? 265 DMS A O    1 
HETATM 2135 C  C1   . DMS E 4 .   ? -4.189  6.951   9.937   1.00 37.21 ? 265 DMS A C1   1 
HETATM 2136 C  C2   . DMS E 4 .   ? -5.831  9.049   10.370  1.00 35.68 ? 265 DMS A C2   1 
HETATM 2137 O  O    . HOH F 5 .   ? 2.212   -15.409 9.407   1.00 24.77 ? 126 HOH A O    1 
HETATM 2138 O  O    . HOH F 5 .   ? -16.992 -8.238  20.504  1.00 12.70 ? 266 HOH A O    1 
HETATM 2139 O  O    . HOH F 5 .   ? -3.375  -13.200 25.277  1.00 11.95 ? 267 HOH A O    1 
HETATM 2140 O  O    . HOH F 5 .   ? -1.209  -3.980  15.719  1.00 10.55 ? 268 HOH A O    1 
HETATM 2141 O  O    . HOH F 5 .   ? -4.454  -13.537 18.093  1.00 9.43  ? 269 HOH A O    1 
HETATM 2142 O  O    . HOH F 5 .   ? -21.653 -7.085  23.765  1.00 16.06 ? 270 HOH A O    1 
HETATM 2143 O  O    . HOH F 5 .   ? -10.552 8.881   25.725  1.00 13.83 ? 271 HOH A O    1 
HETATM 2144 O  O    . HOH F 5 .   ? -3.747  -15.878 24.461  1.00 15.68 ? 272 HOH A O    1 
HETATM 2145 O  O    . HOH F 5 .   ? -21.649 5.802   4.709   1.00 16.90 ? 273 HOH A O    1 
HETATM 2146 O  O    . HOH F 5 .   ? 1.215   -1.526  29.554  1.00 20.68 ? 274 HOH A O    1 
HETATM 2147 O  O    . HOH F 5 .   ? -17.924 10.719  11.454  1.00 17.66 ? 275 HOH A O    1 
HETATM 2148 O  O    . HOH F 5 .   ? 3.688   5.129   29.886  1.00 20.22 ? 276 HOH A O    1 
HETATM 2149 O  O    . HOH F 5 .   ? -24.121 8.966   20.213  1.00 22.02 ? 277 HOH A O    1 
HETATM 2150 O  O    . HOH F 5 .   ? -1.961  -12.322 22.965  1.00 12.63 ? 278 HOH A O    1 
HETATM 2151 O  O    . HOH F 5 .   ? -8.118  -19.293 21.643  1.00 18.16 ? 279 HOH A O    1 
HETATM 2152 O  O    . HOH F 5 .   ? -3.515  -11.091 20.926  1.00 9.82  ? 280 HOH A O    1 
HETATM 2153 O  O    . HOH F 5 .   ? -18.057 -20.351 7.989   1.00 14.14 ? 281 HOH A O    1 
HETATM 2154 O  O    . HOH F 5 .   ? -20.718 7.978   1.844   1.00 20.92 ? 282 HOH A O    1 
HETATM 2155 O  O    . HOH F 5 .   ? -16.135 -12.406 24.546  1.00 18.32 ? 283 HOH A O    1 
HETATM 2156 O  O    . HOH F 5 .   ? -16.599 -9.913  32.915  1.00 18.91 ? 284 HOH A O    1 
HETATM 2157 O  O    . HOH F 5 .   ? 4.914   -4.837  21.071  1.00 15.38 ? 285 HOH A O    1 
HETATM 2158 O  O    . HOH F 5 .   ? -10.349 -18.221 17.060  1.00 17.45 ? 286 HOH A O    1 
HETATM 2159 O  O    . HOH F 5 .   ? -2.489  -8.681  29.248  1.00 15.47 ? 287 HOH A O    1 
HETATM 2160 O  O    . HOH F 5 .   ? -7.851  -15.321 11.254  1.00 9.51  ? 288 HOH A O    1 
HETATM 2161 O  O    . HOH F 5 .   ? -19.266 10.253  8.784   1.00 17.73 ? 289 HOH A O    1 
HETATM 2162 O  O    . HOH F 5 .   ? -13.894 10.699  27.926  1.00 29.62 ? 290 HOH A O    1 
HETATM 2163 O  O    . HOH F 5 .   ? 2.597   -11.258 9.602   1.00 23.80 ? 291 HOH A O    1 
HETATM 2164 O  O    . HOH F 5 .   ? -8.593  -3.777  7.910   1.00 15.13 ? 292 HOH A O    1 
HETATM 2165 O  O    . HOH F 5 .   ? -2.453  -2.920  11.387  1.00 19.79 ? 293 HOH A O    1 
HETATM 2166 O  O    . HOH F 5 .   ? -8.044  -22.117 10.418  1.00 19.51 ? 294 HOH A O    1 
HETATM 2167 O  O    . HOH F 5 .   ? 8.008   -9.375  16.636  1.00 17.64 ? 295 HOH A O    1 
HETATM 2168 O  O    . HOH F 5 .   ? -25.808 -6.078  13.151  1.00 22.40 ? 296 HOH A O    1 
HETATM 2169 O  O    . HOH F 5 .   ? -15.572 9.255   -2.029  1.00 22.17 ? 297 HOH A O    1 
HETATM 2170 O  O    . HOH F 5 .   ? 7.583   6.445   21.779  1.00 20.47 ? 298 HOH A O    1 
HETATM 2171 O  O    . HOH F 5 .   ? -11.940 3.049   30.867  1.00 26.13 ? 299 HOH A O    1 
HETATM 2172 O  O    . HOH F 5 .   ? 2.703   -13.037 5.175   1.00 23.04 ? 300 HOH A O    1 
HETATM 2173 O  O    . HOH F 5 .   ? 13.366  0.396   24.724  1.00 26.81 ? 301 HOH A O    1 
HETATM 2174 O  O    . HOH F 5 .   ? -10.104 14.696  12.211  1.00 22.84 ? 302 HOH A O    1 
HETATM 2175 O  O    . HOH F 5 .   ? -9.838  -7.877  34.025  1.00 24.15 ? 303 HOH A O    1 
HETATM 2176 O  O    . HOH F 5 .   ? -13.442 -18.605 14.791  1.00 20.09 ? 304 HOH A O    1 
HETATM 2177 O  O    . HOH F 5 .   ? 8.580   -3.658  21.315  1.00 25.12 ? 305 HOH A O    1 
HETATM 2178 O  O    . HOH F 5 .   ? -15.978 16.132  23.887  1.00 17.48 ? 306 HOH A O    1 
HETATM 2179 O  O    . HOH F 5 .   ? -9.018  -9.967  -1.413  1.00 23.39 ? 307 HOH A O    1 
HETATM 2180 O  O    . HOH F 5 .   ? -23.702 -0.731  3.957   1.00 21.14 ? 308 HOH A O    1 
HETATM 2181 O  O    . HOH F 5 .   ? -22.159 -18.269 13.507  1.00 26.40 ? 309 HOH A O    1 
HETATM 2182 O  O    . HOH F 5 .   ? 1.227   -11.751 25.351  1.00 22.10 ? 310 HOH A O    1 
HETATM 2183 O  O    . HOH F 5 .   ? -20.318 11.081  26.963  1.00 19.39 ? 311 HOH A O    1 
HETATM 2184 O  O    . HOH F 5 .   ? -23.103 -2.775  6.594   1.00 23.39 ? 312 HOH A O    1 
HETATM 2185 O  O    . HOH F 5 .   ? 2.937   -4.014  7.862   1.00 24.21 ? 313 HOH A O    1 
HETATM 2186 O  O    . HOH F 5 .   ? -25.355 9.788   12.976  1.00 28.57 ? 314 HOH A O    1 
HETATM 2187 O  O    . HOH F 5 .   ? -13.668 14.210  27.462  1.00 22.83 ? 315 HOH A O    1 
HETATM 2188 O  O    . HOH F 5 .   ? -5.680  -4.428  -6.601  1.00 24.65 ? 316 HOH A O    1 
HETATM 2189 O  O    . HOH F 5 .   ? -6.834  -15.004 31.704  1.00 23.32 ? 317 HOH A O    1 
HETATM 2190 O  O    . HOH F 5 .   ? -8.212  14.689  10.475  1.00 28.03 ? 318 HOH A O    1 
HETATM 2191 O  O    . HOH F 5 .   ? -24.957 -7.632  9.013   1.00 22.08 ? 319 HOH A O    1 
HETATM 2192 O  O    . HOH F 5 .   ? 4.638   -6.578  7.992   1.00 22.26 ? 320 HOH A O    1 
HETATM 2193 O  O    . HOH F 5 .   ? -7.222  -8.583  -2.389  1.00 27.48 ? 321 HOH A O    1 
HETATM 2194 O  O    . HOH F 5 .   ? -22.798 -5.945  2.788   1.00 25.62 ? 322 HOH A O    1 
HETATM 2195 O  O    . HOH F 5 .   ? -3.614  -12.758 -3.009  1.00 30.07 ? 323 HOH A O    1 
HETATM 2196 O  O    . HOH F 5 .   ? -12.767 -17.218 16.812  1.00 24.49 ? 324 HOH A O    1 
HETATM 2197 O  O    . HOH F 5 .   ? -26.172 3.558   15.668  1.00 36.04 ? 325 HOH A O    1 
HETATM 2198 O  O    . HOH F 5 .   ? -7.070  -16.795 1.253   1.00 29.41 ? 326 HOH A O    1 
HETATM 2199 O  O    . HOH F 5 .   ? -11.091 -19.236 7.025   1.00 29.69 ? 327 HOH A O    1 
HETATM 2200 O  O    . HOH F 5 .   ? 4.318   -3.419  26.659  1.00 21.74 ? 328 HOH A O    1 
HETATM 2201 O  O    . HOH F 5 .   ? -17.727 -21.170 17.602  1.00 25.29 ? 329 HOH A O    1 
HETATM 2202 O  O    . HOH F 5 .   ? 1.581   12.786  22.576  1.00 28.79 ? 330 HOH A O    1 
HETATM 2203 O  O    . HOH F 5 .   ? -1.545  -13.145 27.378  1.00 23.18 ? 331 HOH A O    1 
HETATM 2204 O  O    . HOH F 5 .   ? -1.039  -11.079 29.033  1.00 22.84 ? 332 HOH A O    1 
HETATM 2205 O  O    . HOH F 5 .   ? -8.616  -15.233 36.675  1.00 34.83 ? 333 HOH A O    1 
HETATM 2206 O  O    . HOH F 5 .   ? -4.722  -12.000 32.165  1.00 26.92 ? 334 HOH A O    1 
HETATM 2207 O  O    . HOH F 5 .   ? -14.309 -16.383 29.266  1.00 28.75 ? 335 HOH A O    1 
HETATM 2208 O  O    . HOH F 5 .   ? -6.671  -20.171 19.552  1.00 19.85 ? 336 HOH A O    1 
HETATM 2209 O  O    . HOH F 5 .   ? -6.132  -19.811 23.973  1.00 25.01 ? 337 HOH A O    1 
HETATM 2210 O  O    . HOH F 5 .   ? -23.415 -11.212 17.420  1.00 22.94 ? 338 HOH A O    1 
HETATM 2211 O  O    . HOH F 5 .   ? -27.797 5.224   25.261  1.00 31.37 ? 339 HOH A O    1 
HETATM 2212 O  O    . HOH F 5 .   ? -1.196  9.352   28.057  1.00 25.66 ? 340 HOH A O    1 
HETATM 2213 O  O    . HOH F 5 .   ? -23.118 -11.728 14.054  1.00 26.21 ? 341 HOH A O    1 
HETATM 2214 O  O    . HOH F 5 .   ? -24.912 12.149  6.467   1.00 30.60 ? 342 HOH A O    1 
HETATM 2215 O  O    . HOH F 5 .   ? -1.218  -17.783 17.912  1.00 29.56 ? 343 HOH A O    1 
HETATM 2216 O  O    . HOH F 5 .   ? -0.399  11.035  23.386  1.00 27.83 ? 344 HOH A O    1 
HETATM 2217 O  O    . HOH F 5 .   ? -17.308 11.205  -2.012  1.00 26.10 ? 345 HOH A O    1 
HETATM 2218 O  O    . HOH F 5 .   ? -1.943  -17.376 25.279  1.00 27.64 ? 346 HOH A O    1 
HETATM 2219 O  O    . HOH F 5 .   ? 11.333  1.450   26.158  1.00 29.22 ? 347 HOH A O    1 
HETATM 2220 O  O    . HOH F 5 .   ? -1.052  11.898  25.698  1.00 38.27 ? 348 HOH A O    1 
HETATM 2221 O  O    . HOH F 5 .   ? -24.082 -0.632  26.630  1.00 24.24 ? 349 HOH A O    1 
HETATM 2222 O  O    . HOH F 5 .   ? -10.358 13.410  8.814   1.00 23.69 ? 350 HOH A O    1 
HETATM 2223 O  O    . HOH F 5 .   ? -26.759 -2.321  14.344  1.00 19.00 ? 351 HOH A O    1 
HETATM 2224 O  O    . HOH F 5 .   ? -20.913 -20.346 1.817   1.00 32.26 ? 352 HOH A O    1 
HETATM 2225 O  O    . HOH F 5 .   ? -17.890 -21.893 5.830   1.00 21.68 ? 353 HOH A O    1 
HETATM 2226 O  O    . HOH F 5 .   ? -13.177 -16.749 26.524  1.00 25.45 ? 354 HOH A O    1 
HETATM 2227 O  O    . HOH F 5 .   ? -18.800 -8.897  34.437  1.00 27.87 ? 355 HOH A O    1 
HETATM 2228 O  O    . HOH F 5 .   ? 9.104   2.483   11.682  1.00 29.43 ? 356 HOH A O    1 
HETATM 2229 O  O    . HOH F 5 .   ? 9.816   -4.499  -7.606  1.00 28.20 ? 357 HOH A O    1 
HETATM 2230 O  O    . HOH F 5 .   ? -11.371 -15.436 34.036  1.00 25.92 ? 358 HOH A O    1 
HETATM 2231 O  O    . HOH F 5 .   ? 0.662   0.615   -6.625  1.00 27.06 ? 359 HOH A O    1 
HETATM 2232 O  O    . HOH F 5 .   ? -10.701 1.277   34.124  1.00 28.26 ? 360 HOH A O    1 
HETATM 2233 O  O    . HOH F 5 .   ? -24.078 -6.699  0.374   1.00 32.48 ? 361 HOH A O    1 
HETATM 2234 O  O    . HOH F 5 .   ? -5.591  -7.644  40.316  1.00 27.14 ? 362 HOH A O    1 
HETATM 2235 O  O    . HOH F 5 .   ? -18.356 -3.557  -2.561  1.00 23.78 ? 363 HOH A O    1 
HETATM 2236 O  O    . HOH F 5 .   ? 5.554   7.305   20.286  1.00 21.26 ? 364 HOH A O    1 
HETATM 2237 O  O    . HOH F 5 .   ? -19.810 -16.796 3.040   1.00 26.49 ? 365 HOH A O    1 
HETATM 2238 O  O    . HOH F 5 .   ? -6.231  15.327  11.762  1.00 26.90 ? 366 HOH A O    1 
HETATM 2239 O  O    . HOH F 5 .   ? -26.684 -3.893  25.452  1.00 23.64 ? 367 HOH A O    1 
HETATM 2240 O  O    . HOH F 5 .   ? -14.618 -18.433 18.844  1.00 25.33 ? 368 HOH A O    1 
HETATM 2241 O  O    . HOH F 5 .   ? -13.223 -22.326 12.016  1.00 31.49 ? 369 HOH A O    1 
HETATM 2242 O  O    . HOH F 5 .   ? -29.184 -3.569  13.445  1.00 24.92 ? 370 HOH A O    1 
HETATM 2243 O  O    . HOH F 5 .   ? 1.427   8.874   24.585  1.00 21.84 ? 371 HOH A O    1 
HETATM 2244 O  O    . HOH F 5 .   ? -23.504 -13.242 11.285  1.00 27.48 ? 372 HOH A O    1 
HETATM 2245 O  O    . HOH F 5 .   ? 3.603   -13.287 12.093  1.00 28.75 ? 373 HOH A O    1 
HETATM 2246 O  O    . HOH F 5 .   ? -2.468  -9.048  34.737  1.00 33.57 ? 374 HOH A O    1 
HETATM 2247 O  O    . HOH F 5 .   ? -11.760 11.265  0.423   1.00 34.63 ? 375 HOH A O    1 
HETATM 2248 O  O    . HOH F 5 .   ? -25.928 -15.065 8.294   1.00 28.13 ? 376 HOH A O    1 
HETATM 2249 O  O    . HOH F 5 .   ? 2.293   3.182   -5.157  1.00 33.50 ? 377 HOH A O    1 
HETATM 2250 O  O    . HOH F 5 .   ? -2.034  -12.047 31.439  1.00 34.76 ? 378 HOH A O    1 
HETATM 2251 O  O    . HOH F 5 .   ? 5.151   -7.254  22.575  1.00 29.63 ? 379 HOH A O    1 
HETATM 2252 O  O    . HOH F 5 .   ? -0.116  -14.264 22.213  1.00 28.30 ? 380 HOH A O    1 
HETATM 2253 O  O    . HOH F 5 .   ? -15.072 -21.035 17.720  1.00 35.83 ? 381 HOH A O    1 
HETATM 2254 O  O    . HOH F 5 .   ? -2.839  6.361   5.967   1.00 37.82 ? 382 HOH A O    1 
HETATM 2255 O  O    . HOH F 5 .   ? -16.939 -13.802 26.530  1.00 25.49 ? 383 HOH A O    1 
HETATM 2256 O  O    . HOH F 5 .   ? -26.609 3.313   21.144  1.00 33.66 ? 384 HOH A O    1 
HETATM 2257 O  O    . HOH F 5 .   ? 12.212  -4.302  -8.025  1.00 25.21 ? 385 HOH A O    1 
HETATM 2258 O  O    . HOH F 5 .   ? 4.412   -2.386  29.115  1.00 33.16 ? 386 HOH A O    1 
HETATM 2259 O  O    . HOH F 5 .   ? -12.915 -18.281 31.916  1.00 31.71 ? 387 HOH A O    1 
HETATM 2260 O  O    . HOH F 5 .   ? -0.570  -8.430  32.839  1.00 26.24 ? 388 HOH A O    1 
HETATM 2261 O  O    . HOH F 5 .   ? -28.289 6.086   19.607  1.00 32.20 ? 389 HOH A O    1 
HETATM 2262 O  O    . HOH F 5 .   ? -31.706 -10.744 16.091  1.00 23.11 ? 390 HOH A O    1 
HETATM 2263 O  O    . HOH F 5 .   ? -5.099  -7.327  37.717  1.00 30.89 ? 391 HOH A O    1 
HETATM 2264 O  O    . HOH F 5 .   ? -31.850 -2.357  14.016  1.00 29.85 ? 392 HOH A O    1 
HETATM 2265 O  O    . HOH F 5 .   ? 7.916   -7.643  -0.696  1.00 37.40 ? 393 HOH A O    1 
HETATM 2266 O  O    . HOH F 5 .   ? -17.681 2.643   -6.670  1.00 30.07 ? 394 HOH A O    1 
HETATM 2267 O  O    . HOH F 5 .   ? -4.854  -20.796 21.239  1.00 29.20 ? 395 HOH A O    1 
HETATM 2268 O  O    . HOH F 5 .   ? -25.954 6.645   27.081  1.00 26.78 ? 396 HOH A O    1 
HETATM 2269 O  O    . HOH F 5 .   ? 2.148   8.279   27.670  1.00 23.03 ? 397 HOH A O    1 
HETATM 2270 O  O    . HOH F 5 .   ? 0.785   -1.099  -4.769  1.00 27.45 ? 398 HOH A O    1 
HETATM 2271 O  O    . HOH F 5 .   ? -28.995 -5.700  24.515  1.00 27.68 ? 399 HOH A O    1 
HETATM 2272 O  O    . HOH F 5 .   ? -22.079 -13.920 18.713  1.00 33.41 ? 400 HOH A O    1 
HETATM 2273 O  O    . HOH F 5 .   ? -6.433  12.473  10.082  1.00 40.81 ? 401 HOH A O    1 
HETATM 2274 O  O    . HOH F 5 .   ? -7.333  -8.612  32.744  1.00 23.08 ? 402 HOH A O    1 
HETATM 2275 O  O    . HOH F 5 .   ? 1.377   -6.282  34.562  1.00 29.32 ? 403 HOH A O    1 
HETATM 2276 O  O    . HOH F 5 .   ? -9.119  6.740   -3.659  1.00 46.94 ? 404 HOH A O    1 
HETATM 2277 O  O    . HOH F 5 .   ? -8.540  8.518   7.362   1.00 38.16 ? 405 HOH A O    1 
HETATM 2278 O  O    . HOH F 5 .   ? -27.923 -4.072  10.393  1.00 35.98 ? 406 HOH A O    1 
HETATM 2279 O  O    . HOH F 5 .   ? -15.669 -9.964  37.447  1.00 30.34 ? 407 HOH A O    1 
HETATM 2280 O  O    . HOH F 5 .   ? -1.474  4.466   7.940   1.00 35.63 ? 408 HOH A O    1 
HETATM 2281 O  O    . HOH F 5 .   ? -0.293  13.750  15.721  1.00 32.86 ? 409 HOH A O    1 
HETATM 2282 O  O    . HOH F 5 .   ? -21.314 -19.461 6.565   1.00 23.56 ? 410 HOH A O    1 
HETATM 2283 O  O    . HOH F 5 .   ? -10.821 -18.891 33.608  1.00 34.68 ? 411 HOH A O    1 
HETATM 2284 O  O    . HOH F 5 .   ? -21.686 -13.681 23.366  1.00 34.49 ? 412 HOH A O    1 
HETATM 2285 O  O    . HOH F 5 .   ? -17.366 -16.001 22.143  1.00 33.36 ? 413 HOH A O    1 
HETATM 2286 O  O    . HOH F 5 .   ? 11.530  -6.926  22.450  1.00 35.90 ? 414 HOH A O    1 
HETATM 2287 O  O    . HOH F 5 .   ? 8.547   -4.639  24.177  1.00 30.72 ? 415 HOH A O    1 
HETATM 2288 O  O    . HOH F 5 .   ? -9.090  -5.819  35.979  1.00 23.50 ? 416 HOH A O    1 
HETATM 2289 O  O    . HOH F 5 .   ? -7.162  -10.070 -4.706  1.00 24.32 ? 417 HOH A O    1 
HETATM 2290 O  O    . HOH F 5 .   ? -19.754 -15.804 22.391  1.00 33.98 ? 418 HOH A O    1 
HETATM 2291 O  O    . HOH F 5 .   ? -27.675 2.807   23.682  1.00 34.99 ? 419 HOH A O    1 
HETATM 2292 O  O    . HOH F 5 .   ? -4.016  -4.882  37.783  1.00 39.57 ? 420 HOH A O    1 
HETATM 2293 O  O    . HOH F 5 .   ? -17.944 4.041   -3.665  1.00 33.21 ? 421 HOH A O    1 
HETATM 2294 O  O    . HOH F 5 .   ? -0.187  1.155   34.670  1.00 33.21 ? 422 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 E36 1   262 1   E36 E36 A . 
C 3 ZN  1   263 1   ZN  ZN  A . 
D 4 DMS 1   264 1   DMS DMS A . 
E 4 DMS 1   265 2   DMS DMS A . 
F 5 HOH 1   126 126 HOH HOH A . 
F 5 HOH 2   266 1   HOH HOH A . 
F 5 HOH 3   267 2   HOH HOH A . 
F 5 HOH 4   268 3   HOH HOH A . 
F 5 HOH 5   269 4   HOH HOH A . 
F 5 HOH 6   270 5   HOH HOH A . 
F 5 HOH 7   271 6   HOH HOH A . 
F 5 HOH 8   272 7   HOH HOH A . 
F 5 HOH 9   273 8   HOH HOH A . 
F 5 HOH 10  274 9   HOH HOH A . 
F 5 HOH 11  275 10  HOH HOH A . 
F 5 HOH 12  276 11  HOH HOH A . 
F 5 HOH 13  277 12  HOH HOH A . 
F 5 HOH 14  278 13  HOH HOH A . 
F 5 HOH 15  279 14  HOH HOH A . 
F 5 HOH 16  280 15  HOH HOH A . 
F 5 HOH 17  281 16  HOH HOH A . 
F 5 HOH 18  282 17  HOH HOH A . 
F 5 HOH 19  283 18  HOH HOH A . 
F 5 HOH 20  284 19  HOH HOH A . 
F 5 HOH 21  285 20  HOH HOH A . 
F 5 HOH 22  286 21  HOH HOH A . 
F 5 HOH 23  287 22  HOH HOH A . 
F 5 HOH 24  288 23  HOH HOH A . 
F 5 HOH 25  289 24  HOH HOH A . 
F 5 HOH 26  290 25  HOH HOH A . 
F 5 HOH 27  291 26  HOH HOH A . 
F 5 HOH 28  292 27  HOH HOH A . 
F 5 HOH 29  293 28  HOH HOH A . 
F 5 HOH 30  294 29  HOH HOH A . 
F 5 HOH 31  295 30  HOH HOH A . 
F 5 HOH 32  296 31  HOH HOH A . 
F 5 HOH 33  297 32  HOH HOH A . 
F 5 HOH 34  298 33  HOH HOH A . 
F 5 HOH 35  299 34  HOH HOH A . 
F 5 HOH 36  300 35  HOH HOH A . 
F 5 HOH 37  301 36  HOH HOH A . 
F 5 HOH 38  302 37  HOH HOH A . 
F 5 HOH 39  303 38  HOH HOH A . 
F 5 HOH 40  304 39  HOH HOH A . 
F 5 HOH 41  305 40  HOH HOH A . 
F 5 HOH 42  306 41  HOH HOH A . 
F 5 HOH 43  307 42  HOH HOH A . 
F 5 HOH 44  308 43  HOH HOH A . 
F 5 HOH 45  309 44  HOH HOH A . 
F 5 HOH 46  310 45  HOH HOH A . 
F 5 HOH 47  311 46  HOH HOH A . 
F 5 HOH 48  312 47  HOH HOH A . 
F 5 HOH 49  313 48  HOH HOH A . 
F 5 HOH 50  314 49  HOH HOH A . 
F 5 HOH 51  315 50  HOH HOH A . 
F 5 HOH 52  316 51  HOH HOH A . 
F 5 HOH 53  317 52  HOH HOH A . 
F 5 HOH 54  318 53  HOH HOH A . 
F 5 HOH 55  319 54  HOH HOH A . 
F 5 HOH 56  320 55  HOH HOH A . 
F 5 HOH 57  321 56  HOH HOH A . 
F 5 HOH 58  322 57  HOH HOH A . 
F 5 HOH 59  323 58  HOH HOH A . 
F 5 HOH 60  324 59  HOH HOH A . 
F 5 HOH 61  325 60  HOH HOH A . 
F 5 HOH 62  326 61  HOH HOH A . 
F 5 HOH 63  327 62  HOH HOH A . 
F 5 HOH 64  328 63  HOH HOH A . 
F 5 HOH 65  329 64  HOH HOH A . 
F 5 HOH 66  330 65  HOH HOH A . 
F 5 HOH 67  331 66  HOH HOH A . 
F 5 HOH 68  332 67  HOH HOH A . 
F 5 HOH 69  333 68  HOH HOH A . 
F 5 HOH 70  334 69  HOH HOH A . 
F 5 HOH 71  335 70  HOH HOH A . 
F 5 HOH 72  336 71  HOH HOH A . 
F 5 HOH 73  337 72  HOH HOH A . 
F 5 HOH 74  338 73  HOH HOH A . 
F 5 HOH 75  339 74  HOH HOH A . 
F 5 HOH 76  340 75  HOH HOH A . 
F 5 HOH 77  341 76  HOH HOH A . 
F 5 HOH 78  342 77  HOH HOH A . 
F 5 HOH 79  343 78  HOH HOH A . 
F 5 HOH 80  344 79  HOH HOH A . 
F 5 HOH 81  345 80  HOH HOH A . 
F 5 HOH 82  346 81  HOH HOH A . 
F 5 HOH 83  347 82  HOH HOH A . 
F 5 HOH 84  348 83  HOH HOH A . 
F 5 HOH 85  349 84  HOH HOH A . 
F 5 HOH 86  350 85  HOH HOH A . 
F 5 HOH 87  351 86  HOH HOH A . 
F 5 HOH 88  352 87  HOH HOH A . 
F 5 HOH 89  353 88  HOH HOH A . 
F 5 HOH 90  354 89  HOH HOH A . 
F 5 HOH 91  355 90  HOH HOH A . 
F 5 HOH 92  356 91  HOH HOH A . 
F 5 HOH 93  357 92  HOH HOH A . 
F 5 HOH 94  358 93  HOH HOH A . 
F 5 HOH 95  359 94  HOH HOH A . 
F 5 HOH 96  360 95  HOH HOH A . 
F 5 HOH 97  361 96  HOH HOH A . 
F 5 HOH 98  362 97  HOH HOH A . 
F 5 HOH 99  363 98  HOH HOH A . 
F 5 HOH 100 364 99  HOH HOH A . 
F 5 HOH 101 365 100 HOH HOH A . 
F 5 HOH 102 366 101 HOH HOH A . 
F 5 HOH 103 367 102 HOH HOH A . 
F 5 HOH 104 368 103 HOH HOH A . 
F 5 HOH 105 369 104 HOH HOH A . 
F 5 HOH 106 370 105 HOH HOH A . 
F 5 HOH 107 371 106 HOH HOH A . 
F 5 HOH 108 372 107 HOH HOH A . 
F 5 HOH 109 373 108 HOH HOH A . 
F 5 HOH 110 374 109 HOH HOH A . 
F 5 HOH 111 375 110 HOH HOH A . 
F 5 HOH 112 376 111 HOH HOH A . 
F 5 HOH 113 377 112 HOH HOH A . 
F 5 HOH 114 378 113 HOH HOH A . 
F 5 HOH 115 379 114 HOH HOH A . 
F 5 HOH 116 380 115 HOH HOH A . 
F 5 HOH 117 381 116 HOH HOH A . 
F 5 HOH 118 382 117 HOH HOH A . 
F 5 HOH 119 383 118 HOH HOH A . 
F 5 HOH 120 384 119 HOH HOH A . 
F 5 HOH 121 385 120 HOH HOH A . 
F 5 HOH 122 386 121 HOH HOH A . 
F 5 HOH 123 387 122 HOH HOH A . 
F 5 HOH 124 388 123 HOH HOH A . 
F 5 HOH 125 389 124 HOH HOH A . 
F 5 HOH 126 390 125 HOH HOH A . 
F 5 HOH 127 391 127 HOH HOH A . 
F 5 HOH 128 392 128 HOH HOH A . 
F 5 HOH 129 393 129 HOH HOH A . 
F 5 HOH 130 394 130 HOH HOH A . 
F 5 HOH 131 395 131 HOH HOH A . 
F 5 HOH 132 396 132 HOH HOH A . 
F 5 HOH 133 397 133 HOH HOH A . 
F 5 HOH 134 398 134 HOH HOH A . 
F 5 HOH 135 399 135 HOH HOH A . 
F 5 HOH 136 400 136 HOH HOH A . 
F 5 HOH 137 401 137 HOH HOH A . 
F 5 HOH 138 402 138 HOH HOH A . 
F 5 HOH 139 403 139 HOH HOH A . 
F 5 HOH 140 404 140 HOH HOH A . 
F 5 HOH 141 405 141 HOH HOH A . 
F 5 HOH 142 406 142 HOH HOH A . 
F 5 HOH 143 407 143 HOH HOH A . 
F 5 HOH 144 408 144 HOH HOH A . 
F 5 HOH 145 409 145 HOH HOH A . 
F 5 HOH 146 410 146 HOH HOH A . 
F 5 HOH 147 411 147 HOH HOH A . 
F 5 HOH 148 412 148 HOH HOH A . 
F 5 HOH 149 413 149 HOH HOH A . 
F 5 HOH 150 414 150 HOH HOH A . 
F 5 HOH 151 415 151 HOH HOH A . 
F 5 HOH 152 416 152 HOH HOH A . 
F 5 HOH 153 417 153 HOH HOH A . 
F 5 HOH 154 418 155 HOH HOH A . 
F 5 HOH 155 419 156 HOH HOH A . 
F 5 HOH 156 420 157 HOH HOH A . 
F 5 HOH 157 421 158 HOH HOH A . 
F 5 HOH 158 422 159 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2010-11-03 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2023-11-01 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Data collection'           
3 3 'Structure model' 'Database references'       
4 3 'Structure model' 'Derived calculations'      
5 3 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' chem_comp_atom                
2 3 'Structure model' chem_comp_bond                
3 3 'Structure model' database_2                    
4 3 'Structure model' diffrn_source                 
5 3 'Structure model' pdbx_initial_refinement_model 
6 3 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_database_2.pdbx_DOI'                 
2 3 'Structure model' '_database_2.pdbx_database_accession'  
3 3 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
4 3 'Structure model' '_struct_site.pdbx_auth_asym_id'       
5 3 'Structure model' '_struct_site.pdbx_auth_comp_id'       
6 3 'Structure model' '_struct_site.pdbx_auth_seq_id'        
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.2.19 22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
# 
_pdbx_entry_details.entry_id                 3M67 
_pdbx_entry_details.nonpolymer_details       'METAL ION NATURALLY OCCURS IN CARBONIC ANHYDRASES' 
_pdbx_entry_details.sequence_details         '126 IS SKIPPED IN THE NUMBERING.' 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND1 A HIS 36 ? B O A HOH 358 ? ? 1.97 
2 1 O   A LYS 76 ? ? O A HOH 314 ? ? 2.13 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CE3 A TRP 97  ? ? CZ3 A TRP 97  ? ? 1.500 1.380 0.120 0.017 N 
2 1 CG  A GLU 214 ? ? CD  A GLU 214 ? ? 1.615 1.515 0.100 0.015 N 
3 1 CB  A GLU 239 ? ? CG  A GLU 239 ? ? 1.634 1.517 0.117 0.019 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH1 A ARG 27  ? ? 124.89 120.30 4.59   0.50 N 
2 1 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH2 A ARG 27  ? ? 115.96 120.30 -4.34  0.50 N 
3 1 O  A THR 125 ? ? C  A THR 125 ? ? N   A LYS 127 ? ? 111.93 122.70 -10.77 1.60 Y 
4 1 CB A ASP 180 ? ? CG A ASP 180 ? ? OD1 A ASP 180 ? ? 123.77 118.30 5.47   0.90 N 
5 1 NE A ARG 254 ? ? CZ A ARG 254 ? ? NH1 A ARG 254 ? ? 117.20 120.30 -3.10  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -143.13 12.52   
2 1 LYS A 111 ? ? 73.07   -0.54   
3 1 LYS A 170 ? ? -35.18  123.88  
4 1 PHE A 176 ? ? -166.07 87.04   
5 1 ASN A 244 ? ? -98.04  50.45   
6 1 LYS A 252 ? ? 53.29   -135.39 
# 
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  
E36 O1   O  N N 98  
E36 C2   C  N N 99  
E36 C3   C  N N 100 
E36 O4   O  N N 101 
E36 C5   C  Y N 102 
E36 C6   C  Y N 103 
E36 C7   C  Y N 104 
E36 C8   C  Y N 105 
E36 N9   N  Y N 106 
E36 C10  C  Y N 107 
E36 N11  N  Y N 108 
E36 C12  C  Y N 109 
E36 C13  C  Y N 110 
E36 S14  S  N N 111 
E36 C15  C  N N 112 
E36 C16  C  N N 113 
E36 O17  O  N N 114 
E36 C18  C  Y N 115 
E36 C19  C  Y N 116 
E36 C20  C  Y N 117 
E36 C21  C  Y N 118 
E36 C22  C  Y N 119 
E36 C23  C  Y N 120 
E36 S24  S  N N 121 
E36 O25  O  N N 122 
E36 CL26 CL N N 123 
E36 O27  O  N N 124 
E36 N28  N  N N 125 
E36 H2   H  N N 126 
E36 H2A  H  N N 127 
E36 H3   H  N N 128 
E36 H3A  H  N N 129 
E36 H7   H  N N 130 
E36 HN11 H  N N 131 
E36 H13  H  N N 132 
E36 H15  H  N N 133 
E36 H15A H  N N 134 
E36 H19  H  N N 135 
E36 H22  H  N N 136 
E36 H23  H  N N 137 
E36 HN28 H  N N 138 
E36 HN2A H  N N 139 
GLN N    N  N N 140 
GLN CA   C  N S 141 
GLN C    C  N N 142 
GLN O    O  N N 143 
GLN CB   C  N N 144 
GLN CG   C  N N 145 
GLN CD   C  N N 146 
GLN OE1  O  N N 147 
GLN NE2  N  N N 148 
GLN OXT  O  N N 149 
GLN H    H  N N 150 
GLN H2   H  N N 151 
GLN HA   H  N N 152 
GLN HB2  H  N N 153 
GLN HB3  H  N N 154 
GLN HG2  H  N N 155 
GLN HG3  H  N N 156 
GLN HE21 H  N N 157 
GLN HE22 H  N N 158 
GLN HXT  H  N N 159 
GLU N    N  N N 160 
GLU CA   C  N S 161 
GLU C    C  N N 162 
GLU O    O  N N 163 
GLU CB   C  N N 164 
GLU CG   C  N N 165 
GLU CD   C  N N 166 
GLU OE1  O  N N 167 
GLU OE2  O  N N 168 
GLU OXT  O  N N 169 
GLU H    H  N N 170 
GLU H2   H  N N 171 
GLU HA   H  N N 172 
GLU HB2  H  N N 173 
GLU HB3  H  N N 174 
GLU HG2  H  N N 175 
GLU HG3  H  N N 176 
GLU HE2  H  N N 177 
GLU HXT  H  N N 178 
GLY N    N  N N 179 
GLY CA   C  N N 180 
GLY C    C  N N 181 
GLY O    O  N N 182 
GLY OXT  O  N N 183 
GLY H    H  N N 184 
GLY H2   H  N N 185 
GLY HA2  H  N N 186 
GLY HA3  H  N N 187 
GLY HXT  H  N N 188 
HIS N    N  N N 189 
HIS CA   C  N S 190 
HIS C    C  N N 191 
HIS O    O  N N 192 
HIS CB   C  N N 193 
HIS CG   C  Y N 194 
HIS ND1  N  Y N 195 
HIS CD2  C  Y N 196 
HIS CE1  C  Y N 197 
HIS NE2  N  Y N 198 
HIS OXT  O  N N 199 
HIS H    H  N N 200 
HIS H2   H  N N 201 
HIS HA   H  N N 202 
HIS HB2  H  N N 203 
HIS HB3  H  N N 204 
HIS HD1  H  N N 205 
HIS HD2  H  N N 206 
HIS HE1  H  N N 207 
HIS HE2  H  N N 208 
HIS HXT  H  N N 209 
HOH O    O  N N 210 
HOH H1   H  N N 211 
HOH H2   H  N N 212 
ILE N    N  N N 213 
ILE CA   C  N S 214 
ILE C    C  N N 215 
ILE O    O  N N 216 
ILE CB   C  N S 217 
ILE CG1  C  N N 218 
ILE CG2  C  N N 219 
ILE CD1  C  N N 220 
ILE OXT  O  N N 221 
ILE H    H  N N 222 
ILE H2   H  N N 223 
ILE HA   H  N N 224 
ILE HB   H  N N 225 
ILE HG12 H  N N 226 
ILE HG13 H  N N 227 
ILE HG21 H  N N 228 
ILE HG22 H  N N 229 
ILE HG23 H  N N 230 
ILE HD11 H  N N 231 
ILE HD12 H  N N 232 
ILE HD13 H  N N 233 
ILE HXT  H  N N 234 
LEU N    N  N N 235 
LEU CA   C  N S 236 
LEU C    C  N N 237 
LEU O    O  N N 238 
LEU CB   C  N N 239 
LEU CG   C  N N 240 
LEU CD1  C  N N 241 
LEU CD2  C  N N 242 
LEU OXT  O  N N 243 
LEU H    H  N N 244 
LEU H2   H  N N 245 
LEU HA   H  N N 246 
LEU HB2  H  N N 247 
LEU HB3  H  N N 248 
LEU HG   H  N N 249 
LEU HD11 H  N N 250 
LEU HD12 H  N N 251 
LEU HD13 H  N N 252 
LEU HD21 H  N N 253 
LEU HD22 H  N N 254 
LEU HD23 H  N N 255 
LEU HXT  H  N N 256 
LYS N    N  N N 257 
LYS CA   C  N S 258 
LYS C    C  N N 259 
LYS O    O  N N 260 
LYS CB   C  N N 261 
LYS CG   C  N N 262 
LYS CD   C  N N 263 
LYS CE   C  N N 264 
LYS NZ   N  N N 265 
LYS OXT  O  N N 266 
LYS H    H  N N 267 
LYS H2   H  N N 268 
LYS HA   H  N N 269 
LYS HB2  H  N N 270 
LYS HB3  H  N N 271 
LYS HG2  H  N N 272 
LYS HG3  H  N N 273 
LYS HD2  H  N N 274 
LYS HD3  H  N N 275 
LYS HE2  H  N N 276 
LYS HE3  H  N N 277 
LYS HZ1  H  N N 278 
LYS HZ2  H  N N 279 
LYS HZ3  H  N N 280 
LYS HXT  H  N N 281 
MET N    N  N N 282 
MET CA   C  N S 283 
MET C    C  N N 284 
MET O    O  N N 285 
MET CB   C  N N 286 
MET CG   C  N N 287 
MET SD   S  N N 288 
MET CE   C  N N 289 
MET OXT  O  N N 290 
MET H    H  N N 291 
MET H2   H  N N 292 
MET HA   H  N N 293 
MET HB2  H  N N 294 
MET HB3  H  N N 295 
MET HG2  H  N N 296 
MET HG3  H  N N 297 
MET HE1  H  N N 298 
MET HE2  H  N N 299 
MET HE3  H  N N 300 
MET HXT  H  N N 301 
PHE N    N  N N 302 
PHE CA   C  N S 303 
PHE C    C  N N 304 
PHE O    O  N N 305 
PHE CB   C  N N 306 
PHE CG   C  Y N 307 
PHE CD1  C  Y N 308 
PHE CD2  C  Y N 309 
PHE CE1  C  Y N 310 
PHE CE2  C  Y N 311 
PHE CZ   C  Y N 312 
PHE OXT  O  N N 313 
PHE H    H  N N 314 
PHE H2   H  N N 315 
PHE HA   H  N N 316 
PHE HB2  H  N N 317 
PHE HB3  H  N N 318 
PHE HD1  H  N N 319 
PHE HD2  H  N N 320 
PHE HE1  H  N N 321 
PHE HE2  H  N N 322 
PHE HZ   H  N N 323 
PHE HXT  H  N N 324 
PRO N    N  N N 325 
PRO CA   C  N S 326 
PRO C    C  N N 327 
PRO O    O  N N 328 
PRO CB   C  N N 329 
PRO CG   C  N N 330 
PRO CD   C  N N 331 
PRO OXT  O  N N 332 
PRO H    H  N N 333 
PRO HA   H  N N 334 
PRO HB2  H  N N 335 
PRO HB3  H  N N 336 
PRO HG2  H  N N 337 
PRO HG3  H  N N 338 
PRO HD2  H  N N 339 
PRO HD3  H  N N 340 
PRO HXT  H  N N 341 
SER N    N  N N 342 
SER CA   C  N S 343 
SER C    C  N N 344 
SER O    O  N N 345 
SER CB   C  N N 346 
SER OG   O  N N 347 
SER OXT  O  N N 348 
SER H    H  N N 349 
SER H2   H  N N 350 
SER HA   H  N N 351 
SER HB2  H  N N 352 
SER HB3  H  N N 353 
SER HG   H  N N 354 
SER HXT  H  N N 355 
THR N    N  N N 356 
THR CA   C  N S 357 
THR C    C  N N 358 
THR O    O  N N 359 
THR CB   C  N R 360 
THR OG1  O  N N 361 
THR CG2  C  N N 362 
THR OXT  O  N N 363 
THR H    H  N N 364 
THR H2   H  N N 365 
THR HA   H  N N 366 
THR HB   H  N N 367 
THR HG1  H  N N 368 
THR HG21 H  N N 369 
THR HG22 H  N N 370 
THR HG23 H  N N 371 
THR HXT  H  N N 372 
TRP N    N  N N 373 
TRP CA   C  N S 374 
TRP C    C  N N 375 
TRP O    O  N N 376 
TRP CB   C  N N 377 
TRP CG   C  Y N 378 
TRP CD1  C  Y N 379 
TRP CD2  C  Y N 380 
TRP NE1  N  Y N 381 
TRP CE2  C  Y N 382 
TRP CE3  C  Y N 383 
TRP CZ2  C  Y N 384 
TRP CZ3  C  Y N 385 
TRP CH2  C  Y N 386 
TRP OXT  O  N N 387 
TRP H    H  N N 388 
TRP H2   H  N N 389 
TRP HA   H  N N 390 
TRP HB2  H  N N 391 
TRP HB3  H  N N 392 
TRP HD1  H  N N 393 
TRP HE1  H  N N 394 
TRP HE3  H  N N 395 
TRP HZ2  H  N N 396 
TRP HZ3  H  N N 397 
TRP HH2  H  N N 398 
TRP HXT  H  N N 399 
TYR N    N  N N 400 
TYR CA   C  N S 401 
TYR C    C  N N 402 
TYR O    O  N N 403 
TYR CB   C  N N 404 
TYR CG   C  Y N 405 
TYR CD1  C  Y N 406 
TYR CD2  C  Y N 407 
TYR CE1  C  Y N 408 
TYR CE2  C  Y N 409 
TYR CZ   C  Y N 410 
TYR OH   O  N N 411 
TYR OXT  O  N N 412 
TYR H    H  N N 413 
TYR H2   H  N N 414 
TYR HA   H  N N 415 
TYR HB2  H  N N 416 
TYR HB3  H  N N 417 
TYR HD1  H  N N 418 
TYR HD2  H  N N 419 
TYR HE1  H  N N 420 
TYR HE2  H  N N 421 
TYR HH   H  N N 422 
TYR HXT  H  N N 423 
VAL N    N  N N 424 
VAL CA   C  N S 425 
VAL C    C  N N 426 
VAL O    O  N N 427 
VAL CB   C  N N 428 
VAL CG1  C  N N 429 
VAL CG2  C  N N 430 
VAL OXT  O  N N 431 
VAL H    H  N N 432 
VAL H2   H  N N 433 
VAL HA   H  N N 434 
VAL HB   H  N N 435 
VAL HG11 H  N N 436 
VAL HG12 H  N N 437 
VAL HG13 H  N N 438 
VAL HG21 H  N N 439 
VAL HG22 H  N N 440 
VAL HG23 H  N N 441 
VAL HXT  H  N N 442 
ZN  ZN   ZN N N 443 
# 
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  
E36 O1  C2   sing N N 92  
E36 O1  C6   sing N N 93  
E36 C2  C3   sing N N 94  
E36 C3  O4   sing N N 95  
E36 O4  C5   sing N N 96  
E36 C5  C6   doub Y N 97  
E36 C5  C13  sing Y N 98  
E36 C6  C7   sing Y N 99  
E36 C7  C8   doub Y N 100 
E36 C8  N9   sing Y N 101 
E36 C8  C12  sing Y N 102 
E36 N9  C10  doub Y N 103 
E36 C10 N11  sing Y N 104 
E36 C10 S14  sing N N 105 
E36 N11 C12  sing Y N 106 
E36 C12 C13  doub Y N 107 
E36 S14 C15  sing N N 108 
E36 C15 C16  sing N N 109 
E36 C16 O17  doub N N 110 
E36 C16 C18  sing N N 111 
E36 C18 C19  doub Y N 112 
E36 C18 C23  sing Y N 113 
E36 C19 C20  sing Y N 114 
E36 C20 C21  doub Y N 115 
E36 C20 S24  sing N N 116 
E36 C21 C22  sing Y N 117 
E36 C21 CL26 sing N N 118 
E36 C22 C23  doub Y N 119 
E36 S24 O25  doub N N 120 
E36 S24 O27  doub N N 121 
E36 S24 N28  sing N N 122 
E36 C2  H2   sing N N 123 
E36 C2  H2A  sing N N 124 
E36 C3  H3   sing N N 125 
E36 C3  H3A  sing N N 126 
E36 C7  H7   sing N N 127 
E36 N11 HN11 sing N N 128 
E36 C13 H13  sing N N 129 
E36 C15 H15  sing N N 130 
E36 C15 H15A sing N N 131 
E36 C19 H19  sing N N 132 
E36 C22 H22  sing N N 133 
E36 C23 H23  sing N N 134 
E36 N28 HN28 sing N N 135 
E36 N28 HN2A sing N N 136 
GLN N   CA   sing N N 137 
GLN N   H    sing N N 138 
GLN N   H2   sing N N 139 
GLN CA  C    sing N N 140 
GLN CA  CB   sing N N 141 
GLN CA  HA   sing N N 142 
GLN C   O    doub N N 143 
GLN C   OXT  sing N N 144 
GLN CB  CG   sing N N 145 
GLN CB  HB2  sing N N 146 
GLN CB  HB3  sing N N 147 
GLN CG  CD   sing N N 148 
GLN CG  HG2  sing N N 149 
GLN CG  HG3  sing N N 150 
GLN CD  OE1  doub N N 151 
GLN CD  NE2  sing N N 152 
GLN NE2 HE21 sing N N 153 
GLN NE2 HE22 sing N N 154 
GLN OXT HXT  sing N N 155 
GLU N   CA   sing N N 156 
GLU N   H    sing N N 157 
GLU N   H2   sing N N 158 
GLU CA  C    sing N N 159 
GLU CA  CB   sing N N 160 
GLU CA  HA   sing N N 161 
GLU C   O    doub N N 162 
GLU C   OXT  sing N N 163 
GLU CB  CG   sing N N 164 
GLU CB  HB2  sing N N 165 
GLU CB  HB3  sing N N 166 
GLU CG  CD   sing N N 167 
GLU CG  HG2  sing N N 168 
GLU CG  HG3  sing N N 169 
GLU CD  OE1  doub N N 170 
GLU CD  OE2  sing N N 171 
GLU OE2 HE2  sing N N 172 
GLU OXT HXT  sing N N 173 
GLY N   CA   sing N N 174 
GLY N   H    sing N N 175 
GLY N   H2   sing N N 176 
GLY CA  C    sing N N 177 
GLY CA  HA2  sing N N 178 
GLY CA  HA3  sing N N 179 
GLY C   O    doub N N 180 
GLY C   OXT  sing N N 181 
GLY OXT HXT  sing N N 182 
HIS N   CA   sing N N 183 
HIS N   H    sing N N 184 
HIS N   H2   sing N N 185 
HIS CA  C    sing N N 186 
HIS CA  CB   sing N N 187 
HIS CA  HA   sing N N 188 
HIS C   O    doub N N 189 
HIS C   OXT  sing N N 190 
HIS CB  CG   sing N N 191 
HIS CB  HB2  sing N N 192 
HIS CB  HB3  sing N N 193 
HIS CG  ND1  sing Y N 194 
HIS CG  CD2  doub Y N 195 
HIS ND1 CE1  doub Y N 196 
HIS ND1 HD1  sing N N 197 
HIS CD2 NE2  sing Y N 198 
HIS CD2 HD2  sing N N 199 
HIS CE1 NE2  sing Y N 200 
HIS CE1 HE1  sing N N 201 
HIS NE2 HE2  sing N N 202 
HIS OXT HXT  sing N N 203 
HOH O   H1   sing N N 204 
HOH O   H2   sing N N 205 
ILE N   CA   sing N N 206 
ILE N   H    sing N N 207 
ILE N   H2   sing N N 208 
ILE CA  C    sing N N 209 
ILE CA  CB   sing N N 210 
ILE CA  HA   sing N N 211 
ILE C   O    doub N N 212 
ILE C   OXT  sing N N 213 
ILE CB  CG1  sing N N 214 
ILE CB  CG2  sing N N 215 
ILE CB  HB   sing N N 216 
ILE CG1 CD1  sing N N 217 
ILE CG1 HG12 sing N N 218 
ILE CG1 HG13 sing N N 219 
ILE CG2 HG21 sing N N 220 
ILE CG2 HG22 sing N N 221 
ILE CG2 HG23 sing N N 222 
ILE CD1 HD11 sing N N 223 
ILE CD1 HD12 sing N N 224 
ILE CD1 HD13 sing N N 225 
ILE OXT HXT  sing N N 226 
LEU N   CA   sing N N 227 
LEU N   H    sing N N 228 
LEU N   H2   sing N N 229 
LEU CA  C    sing N N 230 
LEU CA  CB   sing N N 231 
LEU CA  HA   sing N N 232 
LEU C   O    doub N N 233 
LEU C   OXT  sing N N 234 
LEU CB  CG   sing N N 235 
LEU CB  HB2  sing N N 236 
LEU CB  HB3  sing N N 237 
LEU CG  CD1  sing N N 238 
LEU CG  CD2  sing N N 239 
LEU CG  HG   sing N N 240 
LEU CD1 HD11 sing N N 241 
LEU CD1 HD12 sing N N 242 
LEU CD1 HD13 sing N N 243 
LEU CD2 HD21 sing N N 244 
LEU CD2 HD22 sing N N 245 
LEU CD2 HD23 sing N N 246 
LEU OXT HXT  sing N N 247 
LYS N   CA   sing N N 248 
LYS N   H    sing N N 249 
LYS N   H2   sing N N 250 
LYS CA  C    sing N N 251 
LYS CA  CB   sing N N 252 
LYS CA  HA   sing N N 253 
LYS C   O    doub N N 254 
LYS C   OXT  sing N N 255 
LYS CB  CG   sing N N 256 
LYS CB  HB2  sing N N 257 
LYS CB  HB3  sing N N 258 
LYS CG  CD   sing N N 259 
LYS CG  HG2  sing N N 260 
LYS CG  HG3  sing N N 261 
LYS CD  CE   sing N N 262 
LYS CD  HD2  sing N N 263 
LYS CD  HD3  sing N N 264 
LYS CE  NZ   sing N N 265 
LYS CE  HE2  sing N N 266 
LYS CE  HE3  sing N N 267 
LYS NZ  HZ1  sing N N 268 
LYS NZ  HZ2  sing N N 269 
LYS NZ  HZ3  sing N N 270 
LYS OXT HXT  sing N N 271 
MET N   CA   sing N N 272 
MET N   H    sing N N 273 
MET N   H2   sing N N 274 
MET CA  C    sing N N 275 
MET CA  CB   sing N N 276 
MET CA  HA   sing N N 277 
MET C   O    doub N N 278 
MET C   OXT  sing N N 279 
MET CB  CG   sing N N 280 
MET CB  HB2  sing N N 281 
MET CB  HB3  sing N N 282 
MET CG  SD   sing N N 283 
MET CG  HG2  sing N N 284 
MET CG  HG3  sing N N 285 
MET SD  CE   sing N N 286 
MET CE  HE1  sing N N 287 
MET CE  HE2  sing N N 288 
MET CE  HE3  sing N N 289 
MET OXT HXT  sing N N 290 
PHE N   CA   sing N N 291 
PHE N   H    sing N N 292 
PHE N   H2   sing N N 293 
PHE CA  C    sing N N 294 
PHE CA  CB   sing N N 295 
PHE CA  HA   sing N N 296 
PHE C   O    doub N N 297 
PHE C   OXT  sing N N 298 
PHE CB  CG   sing N N 299 
PHE CB  HB2  sing N N 300 
PHE CB  HB3  sing N N 301 
PHE CG  CD1  doub Y N 302 
PHE CG  CD2  sing Y N 303 
PHE CD1 CE1  sing Y N 304 
PHE CD1 HD1  sing N N 305 
PHE CD2 CE2  doub Y N 306 
PHE CD2 HD2  sing N N 307 
PHE CE1 CZ   doub Y N 308 
PHE CE1 HE1  sing N N 309 
PHE CE2 CZ   sing Y N 310 
PHE CE2 HE2  sing N N 311 
PHE CZ  HZ   sing N N 312 
PHE OXT HXT  sing N N 313 
PRO N   CA   sing N N 314 
PRO N   CD   sing N N 315 
PRO N   H    sing N N 316 
PRO CA  C    sing N N 317 
PRO CA  CB   sing N N 318 
PRO CA  HA   sing N N 319 
PRO C   O    doub N N 320 
PRO C   OXT  sing N N 321 
PRO CB  CG   sing N N 322 
PRO CB  HB2  sing N N 323 
PRO CB  HB3  sing N N 324 
PRO CG  CD   sing N N 325 
PRO CG  HG2  sing N N 326 
PRO CG  HG3  sing N N 327 
PRO CD  HD2  sing N N 328 
PRO CD  HD3  sing N N 329 
PRO OXT HXT  sing N N 330 
SER N   CA   sing N N 331 
SER N   H    sing N N 332 
SER N   H2   sing N N 333 
SER CA  C    sing N N 334 
SER CA  CB   sing N N 335 
SER CA  HA   sing N N 336 
SER C   O    doub N N 337 
SER C   OXT  sing N N 338 
SER CB  OG   sing N N 339 
SER CB  HB2  sing N N 340 
SER CB  HB3  sing N N 341 
SER OG  HG   sing N N 342 
SER OXT HXT  sing N N 343 
THR N   CA   sing N N 344 
THR N   H    sing N N 345 
THR N   H2   sing N N 346 
THR CA  C    sing N N 347 
THR CA  CB   sing N N 348 
THR CA  HA   sing N N 349 
THR C   O    doub N N 350 
THR C   OXT  sing N N 351 
THR CB  OG1  sing N N 352 
THR CB  CG2  sing N N 353 
THR CB  HB   sing N N 354 
THR OG1 HG1  sing N N 355 
THR CG2 HG21 sing N N 356 
THR CG2 HG22 sing N N 357 
THR CG2 HG23 sing N N 358 
THR OXT HXT  sing N N 359 
TRP N   CA   sing N N 360 
TRP N   H    sing N N 361 
TRP N   H2   sing N N 362 
TRP CA  C    sing N N 363 
TRP CA  CB   sing N N 364 
TRP CA  HA   sing N N 365 
TRP C   O    doub N N 366 
TRP C   OXT  sing N N 367 
TRP CB  CG   sing N N 368 
TRP CB  HB2  sing N N 369 
TRP CB  HB3  sing N N 370 
TRP CG  CD1  doub Y N 371 
TRP CG  CD2  sing Y N 372 
TRP CD1 NE1  sing Y N 373 
TRP CD1 HD1  sing N N 374 
TRP CD2 CE2  doub Y N 375 
TRP CD2 CE3  sing Y N 376 
TRP NE1 CE2  sing Y N 377 
TRP NE1 HE1  sing N N 378 
TRP CE2 CZ2  sing Y N 379 
TRP CE3 CZ3  doub Y N 380 
TRP CE3 HE3  sing N N 381 
TRP CZ2 CH2  doub Y N 382 
TRP CZ2 HZ2  sing N N 383 
TRP CZ3 CH2  sing Y N 384 
TRP CZ3 HZ3  sing N N 385 
TRP CH2 HH2  sing N N 386 
TRP OXT HXT  sing N N 387 
TYR N   CA   sing N N 388 
TYR N   H    sing N N 389 
TYR N   H2   sing N N 390 
TYR CA  C    sing N N 391 
TYR CA  CB   sing N N 392 
TYR CA  HA   sing N N 393 
TYR C   O    doub N N 394 
TYR C   OXT  sing N N 395 
TYR CB  CG   sing N N 396 
TYR CB  HB2  sing N N 397 
TYR CB  HB3  sing N N 398 
TYR CG  CD1  doub Y N 399 
TYR CG  CD2  sing Y N 400 
TYR CD1 CE1  sing Y N 401 
TYR CD1 HD1  sing N N 402 
TYR CD2 CE2  doub Y N 403 
TYR CD2 HD2  sing N N 404 
TYR CE1 CZ   doub Y N 405 
TYR CE1 HE1  sing N N 406 
TYR CE2 CZ   sing Y N 407 
TYR CE2 HE2  sing N N 408 
TYR CZ  OH   sing N N 409 
TYR OH  HH   sing N N 410 
TYR OXT HXT  sing N N 411 
VAL N   CA   sing N N 412 
VAL N   H    sing N N 413 
VAL N   H2   sing N N 414 
VAL CA  C    sing N N 415 
VAL CA  CB   sing N N 416 
VAL CA  HA   sing N N 417 
VAL C   O    doub N N 418 
VAL C   OXT  sing N N 419 
VAL CB  CG1  sing N N 420 
VAL CB  CG2  sing N N 421 
VAL CB  HB   sing N N 422 
VAL CG1 HG11 sing N N 423 
VAL CG1 HG12 sing N N 424 
VAL CG1 HG13 sing N N 425 
VAL CG2 HG21 sing N N 426 
VAL CG2 HG22 sing N N 427 
VAL CG2 HG23 sing N N 428 
VAL OXT HXT  sing N N 429 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-chloro-5-[(6,7-dihydro-1H-[1,4]dioxino[2,3-f]benzimidazol-2-ylsulfanyl)acetyl]benzenesulfonamide' E36 
3 'ZINC ION'                                                                                           ZN  
4 'DIMETHYL SULFOXIDE'                                                                                 DMS 
5 water                                                                                                HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2NNO 
_pdbx_initial_refinement_model.details          'PDB ENTRY 2NNO' 
# 
