data_3M2N
# 
_entry.id   3M2N 
# 
_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   3M2N         pdb_00003m2n 10.2210/pdb3m2n/pdb 
RCSB  RCSB058030   ?            ?                   
WWPDB D_1000058030 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3M3X 'The same protein with other ligand' unspecified 
PDB 3M40 'The same protein with other ligand' unspecified 
PDB 3M5E 'The same protein with other ligand' unspecified 
PDB 3MHI 'The same protein with other ligand' unspecified 
PDB 3MHL 'The same protein with other ligand' unspecified 
PDB 3MHM 'The same protein with other ligand' unspecified 
PDB 3MHO 'The same protein with other ligand' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3M2N 
_pdbx_database_status.recvd_initial_deposition_date   2010-03-08 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'  1 
'Manakova, E.'  2 
'Golovenko, D.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            51 
_citation.page_first                259 
_citation.page_last                 270 
_citation.year                      2012 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22440859 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2012.02.050 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1 ? 
primary 'Zubriene, A.'      2 ? 
primary 'Baranauskiene, L.' 3 ? 
primary 'Tamulaitiene, G.'  4 ? 
primary 'Manakova, E.'      5 ? 
primary 'Kairys, V.'        6 ? 
primary 'Grazulis, S.'      7 ? 
primary 'Tumkevicius, S.'   8 ? 
primary 'Matulis, D.'       9 ? 
# 
_cell.entry_id           3M2N 
_cell.length_a           42.041 
_cell.length_b           41.253 
_cell.length_c           71.858 
_cell.angle_alpha        90.00 
_cell.angle_beta         104.74 
_cell.angle_gamma        90.00 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
_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                         3M2N 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_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 '4-{2-[(6-chloro-5-nitropyrimidin-4-yl)amino]ethyl}benzenesulfonamide' 357.773   1   ?       ? ? ? 
3 non-polymer syn 'ZINC ION'                                                             65.409    1   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                   78.133    2   ?       ? ? ? 
5 non-polymer syn BICINE                                                                 163.172   1   ?       ? ? ? 
6 water       nat water                                                                  18.015    370 ?       ? ? ? 
# 
_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              3M2N 
_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 
BCN non-polymer         . BICINE                                                                 ? 'C6 H13 N O4'        163.172 
CYS 'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'       121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                   ? 'C2 H6 O S'          78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'       146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'         147.129 
GLY 'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'         75.067  
HIS 'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1'     156.162 
HOH non-polymer         . WATER                                                                  ? 'H2 O'               18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'        131.173 
J74 non-polymer         . '4-{2-[(6-chloro-5-nitropyrimidin-4-yl)amino]ethyl}benzenesulfonamide' ? 'C12 H12 Cl N5 O4 S' 357.773 
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.entry_id          3M2N 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.06 
_exptl_crystal.density_percent_sol   40.22 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pdbx_details    '0.1M Na-Bicine pH 9, 2M Na-Malonate pH7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   7-9 
# 
_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   2009-12-20 
_diffrn_detector.details                'Bent, vertically focussing mirror' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_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_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.8120 
# 
_reflns.entry_id                     3M2N 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             41.24 
_reflns.d_resolution_high            1.65 
_reflns.number_obs                   28936 
_reflns.number_all                   28936 
_reflns.percent_possible_obs         100 
_reflns.pdbx_Rmerge_I_obs            0.076 
_reflns.pdbx_Rsym_value              0.076 
_reflns.pdbx_netI_over_sigmaI        26.3 
_reflns.B_iso_Wilson_estimate        13.8 
_reflns.pdbx_redundancy              9.6 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.65 
_reflns_shell.d_res_low              1.74 
_reflns_shell.percent_possible_all   100.0 
_reflns_shell.Rmerge_I_obs           0.211 
_reflns_shell.pdbx_Rsym_value        0.211 
_reflns_shell.meanI_over_sigI_obs    8.6 
_reflns_shell.pdbx_redundancy        6.6 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      4178 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3M2N 
_refine.ls_number_reflns_obs                     25992 
_refine.ls_number_reflns_all                     25992 
_refine.pdbx_ls_sigma_I                          0 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             39.78 
_refine.ls_d_res_high                            1.65 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_R_factor_obs                          0.15951 
_refine.ls_R_factor_all                          0.15951 
_refine.ls_R_factor_R_work                       0.15453 
_refine.ls_R_factor_R_free                       0.20304 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 10.1 
_refine.ls_number_reflns_R_free                  2928 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_refine.B_iso_mean                               14.049 
_refine.aniso_B[1][1]                            0.64 
_refine.aniso_B[2][2]                            -0.69 
_refine.aniso_B[3][3]                            0.11 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.13 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      'PDB ENTRY 2NNO' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             isotropic 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.109 
_refine.pdbx_overall_ESU_R_Free                  0.110 
_refine.overall_SU_ML                            0.066 
_refine.overall_SU_B                             1.867 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_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        2059 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.number_atoms_solvent             370 
_refine_hist.number_atoms_total               2472 
_refine_hist.d_res_high                       1.65 
_refine_hist.d_res_low                        39.78 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         0.029  0.021  ? 2341 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      2.443  1.956  ? 3200 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   7.273  5.000  ? 295  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   34.274 24.818 ? 110  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   14.348 15.000 ? 383  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   22.789 15.000 ? 7    'X-RAY DIFFRACTION' ? 
r_chiral_restr           0.163  0.200  ? 328  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     0.014  0.020  ? 1854 'X-RAY DIFFRACTION' ? 
r_nbd_refined            0.237  0.200  ? 1198 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          0.316  0.200  ? 1538 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    0.182  0.200  ? 294  'X-RAY DIFFRACTION' ? 
r_metal_ion_refined      0.099  0.200  ? 3    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   0.266  0.200  ? 113  'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 0.172  0.200  ? 84   'X-RAY DIFFRACTION' ? 
r_mcbond_it              1.521  1.500  ? 1439 'X-RAY DIFFRACTION' ? 
r_mcangle_it             2.156  2.000  ? 2276 'X-RAY DIFFRACTION' ? 
r_scbond_it              3.478  3.000  ? 1063 'X-RAY DIFFRACTION' ? 
r_scangle_it             4.790  4.500  ? 919  'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.650 
_refine_ls_shell.d_res_low                        1.693 
_refine_ls_shell.number_reflns_R_work             1891 
_refine_ls_shell.R_factor_R_work                  0.203 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.R_factor_R_free                  0.258 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             195 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3M2N 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 4-{2-[N-(6-chloro-5-nitropyrimidin-4-yl)amino]ethyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3M2N 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
_struct_keywords.text            
'drug design, carbonic anhydrase, sulfonamide, Lyase, Metal-binding, LYASE-LYASE INHIBITOR complex' 
# 
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 ? 
G N N 6 ? 
# 
_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 ? ILE A 166 ? ASP A 165 ILE A 167 5 ? 3 
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 -0.99 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 8.03  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N 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 TRP A 123 ? O TRP A 123 N ARG A 89  ? N ARG A 89  
B 7 8  O ILE A 91  ? O ILE A 91  N PHE A 70  ? N PHE A 70  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N ARG A 89  ? N ARG A 89  O TRP A 123 ? O TRP A 123 
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 J74 262 ? 14 'BINDING SITE FOR RESIDUE J74 A 262' 
AC2 Software A ZN  263 ? 4  'BINDING SITE FOR RESIDUE ZN A 263'  
AC3 Software A DMS 264 ? 4  'BINDING SITE FOR RESIDUE DMS A 264' 
AC4 Software A DMS 265 ? 8  'BINDING SITE FOR RESIDUE DMS A 265' 
AC5 Software A BCN 266 ? 9  'BINDING SITE FOR RESIDUE BCN A 266' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 14 HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 14 HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 14 HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 14 VAL A 134 ? VAL A 135 . ? 1_555 ? 
5  AC1 14 VAL A 142 ? VAL A 143 . ? 1_555 ? 
6  AC1 14 LEU A 197 ? LEU A 198 . ? 1_555 ? 
7  AC1 14 THR A 198 ? THR A 199 . ? 1_555 ? 
8  AC1 14 THR A 199 ? THR A 200 . ? 1_555 ? 
9  AC1 14 PRO A 201 ? PRO A 202 . ? 1_555 ? 
10 AC1 14 TRP A 208 ? TRP A 209 . ? 1_555 ? 
11 AC1 14 ZN  C .   ? ZN  A 263 . ? 1_555 ? 
12 AC1 14 DMS E .   ? DMS A 265 . ? 1_555 ? 
13 AC1 14 HOH G .   ? HOH A 449 . ? 1_555 ? 
14 AC1 14 HOH G .   ? HOH A 634 . ? 1_555 ? 
15 AC2 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
16 AC2 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
17 AC2 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
18 AC2 4  J74 B .   ? J74 A 262 . ? 1_555 ? 
19 AC3 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
20 AC3 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
21 AC3 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
22 AC3 4  HOH G .   ? HOH A 340 . ? 1_555 ? 
23 AC4 8  ILE A 91  ? ILE A 91  . ? 1_555 ? 
24 AC4 8  GLN A 92  ? GLN A 92  . ? 1_555 ? 
25 AC4 8  PHE A 130 ? PHE A 131 . ? 1_555 ? 
26 AC4 8  J74 B .   ? J74 A 262 . ? 1_555 ? 
27 AC4 8  HOH G .   ? HOH A 356 . ? 1_555 ? 
28 AC4 8  HOH G .   ? HOH A 475 . ? 1_555 ? 
29 AC4 8  HOH G .   ? HOH A 522 . ? 1_555 ? 
30 AC4 8  HOH G .   ? HOH A 541 . ? 1_555 ? 
31 AC5 9  LYS A 148 ? LYS A 149 . ? 1_555 ? 
32 AC5 9  LYS A 212 ? LYS A 213 . ? 1_555 ? 
33 AC5 9  GLU A 213 ? GLU A 214 . ? 1_555 ? 
34 AC5 9  PRO A 214 ? PRO A 215 . ? 1_555 ? 
35 AC5 9  HOH G .   ? HOH A 276 . ? 1_555 ? 
36 AC5 9  HOH G .   ? HOH A 312 . ? 1_555 ? 
37 AC5 9  HOH G .   ? HOH A 411 . ? 1_555 ? 
38 AC5 9  HOH G .   ? HOH A 464 . ? 1_555 ? 
39 AC5 9  HOH G .   ? HOH A 631 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3M2N 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3M2N 
_atom_sites.fract_transf_matrix[1][1]   0.023786 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006258 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024241 
_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]   0.014390 
_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 3   ? 13.620  -0.025  6.440   1.00 21.73 ? 3   HIS A N    1 
ATOM   2    C  CA   . HIS A 1 3   ? 13.292  -1.040  7.491   1.00 22.75 ? 3   HIS A CA   1 
ATOM   3    C  C    . HIS A 1 3   ? 12.216  -0.539  8.516   1.00 23.14 ? 3   HIS A C    1 
ATOM   4    O  O    . HIS A 1 3   ? 12.477  -0.392  9.766   1.00 24.62 ? 3   HIS A O    1 
ATOM   5    C  CB   . HIS A 1 3   ? 14.540  -1.479  8.234   1.00 23.25 ? 3   HIS A CB   1 
ATOM   6    C  CG   . HIS A 1 3   ? 14.343  -2.758  8.977   1.00 27.24 ? 3   HIS A CG   1 
ATOM   7    N  ND1  . HIS A 1 3   ? 14.488  -3.993  8.371   1.00 27.59 ? 3   HIS A ND1  1 
ATOM   8    C  CD2  . HIS A 1 3   ? 13.971  -3.003  10.262  1.00 27.96 ? 3   HIS A CD2  1 
ATOM   9    C  CE1  . HIS A 1 3   ? 14.257  -4.943  9.261   1.00 32.14 ? 3   HIS A CE1  1 
ATOM   10   N  NE2  . HIS A 1 3   ? 13.954  -4.374  10.415  1.00 31.82 ? 3   HIS A NE2  1 
ATOM   11   N  N    A HIS A 1 4   ? 11.026  -0.162  8.067   0.50 20.74 ? 4   HIS A N    1 
ATOM   12   N  N    B HIS A 1 4   ? 11.027  -0.364  7.932   0.50 20.52 ? 4   HIS A N    1 
ATOM   13   C  CA   A HIS A 1 4   ? 10.078  0.207   9.119   0.50 17.92 ? 4   HIS A CA   1 
ATOM   14   C  CA   B HIS A 1 4   ? 9.767   0.083   8.540   0.50 17.81 ? 4   HIS A CA   1 
ATOM   15   C  C    A HIS A 1 4   ? 9.114   -0.929  9.494   0.50 15.92 ? 4   HIS A C    1 
ATOM   16   C  C    B HIS A 1 4   ? 9.170   -0.985  9.532   0.50 15.82 ? 4   HIS A C    1 
ATOM   17   O  O    A HIS A 1 4   ? 9.084   -2.027  8.935   0.50 13.34 ? 4   HIS A O    1 
ATOM   18   O  O    B HIS A 1 4   ? 9.552   -2.147  9.503   0.50 13.85 ? 4   HIS A O    1 
ATOM   19   C  CB   A HIS A 1 4   ? 9.313   1.514   8.858   0.50 17.62 ? 4   HIS A CB   1 
ATOM   20   C  CB   B HIS A 1 4   ? 8.819   0.400   7.363   0.50 17.47 ? 4   HIS A CB   1 
ATOM   21   C  CG   A HIS A 1 4   ? 9.073   2.367   10.097  0.50 18.36 ? 4   HIS A CG   1 
ATOM   22   C  CG   B HIS A 1 4   ? 7.522   1.018   7.764   0.50 17.95 ? 4   HIS A CG   1 
ATOM   23   N  ND1  A HIS A 1 4   ? 9.184   1.901   11.400  0.50 16.46 ? 4   HIS A ND1  1 
ATOM   24   N  ND1  B HIS A 1 4   ? 7.406   2.350   8.102   0.50 19.56 ? 4   HIS A ND1  1 
ATOM   25   C  CD2  A HIS A 1 4   ? 8.734   3.676   10.203  0.50 21.32 ? 4   HIS A CD2  1 
ATOM   26   C  CD2  B HIS A 1 4   ? 6.290   0.479   7.919   0.50 18.40 ? 4   HIS A CD2  1 
ATOM   27   C  CE1  A HIS A 1 4   ? 8.922   2.880   12.241  0.50 22.56 ? 4   HIS A CE1  1 
ATOM   28   C  CE1  B HIS A 1 4   ? 6.145   2.607   8.424   0.50 19.66 ? 4   HIS A CE1  1 
ATOM   29   N  NE2  A HIS A 1 4   ? 8.643   3.970   11.544  0.50 23.64 ? 4   HIS A NE2  1 
ATOM   30   N  NE2  B HIS A 1 4   ? 5.456   1.477   8.346   0.50 17.21 ? 4   HIS A NE2  1 
ATOM   31   N  N    . TRP A 1 5   ? 8.267   -0.568  10.422  1.00 15.26 ? 5   TRP A N    1 
ATOM   32   C  CA   . TRP A 1 5   ? 7.579   -1.518  11.281  1.00 12.07 ? 5   TRP A CA   1 
ATOM   33   C  C    . TRP A 1 5   ? 6.643   -2.290  10.414  1.00 10.17 ? 5   TRP A C    1 
ATOM   34   O  O    . TRP A 1 5   ? 6.138   -1.806  9.370   1.00 10.83 ? 5   TRP A O    1 
ATOM   35   C  CB   . TRP A 1 5   ? 6.856   -0.805  12.482  1.00 11.43 ? 5   TRP A CB   1 
ATOM   36   C  CG   . TRP A 1 5   ? 5.745   0.011   12.071  1.00 12.24 ? 5   TRP A CG   1 
ATOM   37   C  CD1  . TRP A 1 5   ? 5.734   1.372   11.748  1.00 15.35 ? 5   TRP A CD1  1 
ATOM   38   C  CD2  . TRP A 1 5   ? 4.390   -0.429  11.986  1.00 11.06 ? 5   TRP A CD2  1 
ATOM   39   N  NE1  . TRP A 1 5   ? 4.456   1.772   11.435  1.00 13.52 ? 5   TRP A NE1  1 
ATOM   40   C  CE2  . TRP A 1 5   ? 3.611   0.692   11.568  1.00 13.54 ? 5   TRP A CE2  1 
ATOM   41   C  CE3  . TRP A 1 5   ? 3.761   -1.683  12.220  1.00 11.46 ? 5   TRP A CE3  1 
ATOM   42   C  CZ2  . TRP A 1 5   ? 2.236   0.618   11.367  1.00 10.94 ? 5   TRP A CZ2  1 
ATOM   43   C  CZ3  . TRP A 1 5   ? 2.397   -1.761  11.986  1.00 10.82 ? 5   TRP A CZ3  1 
ATOM   44   C  CH2  . TRP A 1 5   ? 1.651   -0.595  11.577  1.00 10.30 ? 5   TRP A CH2  1 
ATOM   45   N  N    . GLY A 1 6   ? 6.397   -3.517  10.872  1.00 9.97  ? 6   GLY A N    1 
ATOM   46   C  CA   . GLY A 1 6   ? 5.366   -4.329  10.280  1.00 9.90  ? 6   GLY A CA   1 
ATOM   47   C  C    . GLY A 1 6   ? 4.987   -5.457  11.228  1.00 10.73 ? 6   GLY A C    1 
ATOM   48   O  O    . GLY A 1 6   ? 4.947   -5.316  12.457  1.00 11.27 ? 6   GLY A O    1 
ATOM   49   N  N    A TYR A 1 7   ? 4.748   -6.651  10.726  0.50 12.29 ? 7   TYR A N    1 
ATOM   50   N  N    B TYR A 1 7   ? 4.560   -6.528  10.538  0.50 12.04 ? 7   TYR A N    1 
ATOM   51   C  CA   A TYR A 1 7   ? 4.443   -7.733  11.663  0.50 11.60 ? 7   TYR A CA   1 
ATOM   52   C  CA   B TYR A 1 7   ? 4.104   -7.767  11.169  0.50 12.31 ? 7   TYR A CA   1 
ATOM   53   C  C    A TYR A 1 7   ? 5.306   -8.917  11.368  0.50 13.94 ? 7   TYR A C    1 
ATOM   54   C  C    B TYR A 1 7   ? 4.991   -9.012  10.799  0.50 14.81 ? 7   TYR A C    1 
ATOM   55   O  O    A TYR A 1 7   ? 5.226   -9.913  12.115  0.50 12.77 ? 7   TYR A O    1 
ATOM   56   O  O    B TYR A 1 7   ? 4.452   -10.052 10.367  0.50 14.56 ? 7   TYR A O    1 
ATOM   57   C  CB   A TYR A 1 7   ? 3.003   -8.169  11.471  0.50 10.81 ? 7   TYR A CB   1 
ATOM   58   C  CB   B TYR A 1 7   ? 2.608   -7.974  10.836  0.50 10.48 ? 7   TYR A CB   1 
ATOM   59   C  CG   A TYR A 1 7   ? 2.048   -7.133  11.955  0.50 7.50  ? 7   TYR A CG   1 
ATOM   60   C  CG   B TYR A 1 7   ? 1.674   -6.881  11.417  0.50 5.68  ? 7   TYR A CG   1 
ATOM   61   C  CD1  A TYR A 1 7   ? 1.605   -7.160  13.283  0.50 6.62  ? 7   TYR A CD1  1 
ATOM   62   C  CD1  B TYR A 1 7   ? 1.293   -6.878  12.754  0.50 3.47  ? 7   TYR A CD1  1 
ATOM   63   C  CD2  A TYR A 1 7   ? 1.595   -6.103  11.101  0.50 4.67  ? 7   TYR A CD2  1 
ATOM   64   C  CD2  B TYR A 1 7   ? 1.209   -5.838  10.625  0.50 3.91  ? 7   TYR A CD2  1 
ATOM   65   C  CE1  A TYR A 1 7   ? 0.721   -6.152  13.764  0.50 8.73  ? 7   TYR A CE1  1 
ATOM   66   C  CE1  B TYR A 1 7   ? 0.438   -5.865  13.300  0.50 6.05  ? 7   TYR A CE1  1 
ATOM   67   C  CE2  A TYR A 1 7   ? 0.754   -5.103  11.561  0.50 4.79  ? 7   TYR A CE2  1 
ATOM   68   C  CE2  B TYR A 1 7   ? 0.319   -4.823  11.136  0.50 4.78  ? 7   TYR A CE2  1 
ATOM   69   C  CZ   A TYR A 1 7   ? 0.303   -5.150  12.905  0.50 7.92  ? 7   TYR A CZ   1 
ATOM   70   C  CZ   B TYR A 1 7   ? -0.082  -4.875  12.477  0.50 7.36  ? 7   TYR A CZ   1 
ATOM   71   O  OH   A TYR A 1 7   ? -0.560  -4.203  13.356  0.50 6.58  ? 7   TYR A OH   1 
ATOM   72   O  OH   B TYR A 1 7   ? -0.907  -3.910  12.987  0.50 5.31  ? 7   TYR A OH   1 
ATOM   73   N  N    A GLY A 1 8   ? 6.005   -8.832  10.186  0.50 14.07 ? 8   GLY A N    1 
ATOM   74   N  N    B GLY A 1 8   ? 6.336   -8.923  11.035  0.50 15.77 ? 8   GLY A N    1 
ATOM   75   C  CA   A GLY A 1 8   ? 6.772   -9.964  9.603   0.50 16.08 ? 8   GLY A CA   1 
ATOM   76   C  CA   B GLY A 1 8   ? 7.274   -10.082 10.845  0.50 13.55 ? 8   GLY A CA   1 
ATOM   77   C  C    A GLY A 1 8   ? 7.853   -10.465 10.519  0.50 17.35 ? 8   GLY A C    1 
ATOM   78   C  C    B GLY A 1 8   ? 8.407   -10.367 11.866  0.50 13.78 ? 8   GLY A C    1 
ATOM   79   O  O    A GLY A 1 8   ? 7.956   -9.993  11.647  0.50 17.71 ? 8   GLY A O    1 
ATOM   80   O  O    B GLY A 1 8   ? 8.572   -9.680  12.929  0.50 13.34 ? 8   GLY A O    1 
ATOM   81   N  N    A LYS A 1 9   ? 8.728   -11.372 10.074  0.50 19.09 ? 9   LYS A N    1 
ATOM   82   N  N    B LYS A 1 9   ? 9.185   -11.419 11.605  0.50 13.00 ? 9   LYS A N    1 
ATOM   83   C  CA   A LYS A 1 9   ? 9.936   -11.492 10.899  0.50 19.65 ? 9   LYS A CA   1 
ATOM   84   C  CA   B LYS A 1 9   ? 10.301  -11.802 12.528  0.50 13.75 ? 9   LYS A CA   1 
ATOM   85   C  C    A LYS A 1 9   ? 10.703  -10.203 10.610  0.50 18.11 ? 9   LYS A C    1 
ATOM   86   C  C    B LYS A 1 9   ? 11.186  -10.640 12.887  0.50 13.75 ? 9   LYS A C    1 
ATOM   87   O  O    A LYS A 1 9   ? 10.623  -9.629  9.531   0.50 19.62 ? 9   LYS A O    1 
ATOM   88   O  O    B LYS A 1 9   ? 11.631  -10.519 14.030  0.50 14.20 ? 9   LYS A O    1 
ATOM   89   C  CB   A LYS A 1 9   ? 10.794  -12.706 10.556  0.50 20.84 ? 9   LYS A CB   1 
ATOM   90   C  CB   B LYS A 1 9   ? 11.234  -12.853 11.900  0.50 14.07 ? 9   LYS A CB   1 
ATOM   91   C  CG   A LYS A 1 9   ? 11.240  -13.521 11.790  0.50 22.18 ? 9   LYS A CG   1 
ATOM   92   C  CG   B LYS A 1 9   ? 12.559  -13.057 12.691  0.50 14.08 ? 9   LYS A CG   1 
ATOM   93   C  CD   A LYS A 1 9   ? 12.484  -14.375 11.555  0.50 20.72 ? 9   LYS A CD   1 
ATOM   94   C  CD   B LYS A 1 9   ? 13.459  -14.247 12.287  0.50 13.36 ? 9   LYS A CD   1 
ATOM   95   C  CE   A LYS A 1 9   ? 12.220  -15.727 10.845  0.50 26.10 ? 9   LYS A CE   1 
ATOM   96   C  CE   B LYS A 1 9   ? 13.803  -14.479 10.778  0.50 19.62 ? 9   LYS A CE   1 
ATOM   97   N  NZ   A LYS A 1 9   ? 13.496  -16.559 10.800  0.50 25.00 ? 9   LYS A NZ   1 
ATOM   98   N  NZ   B LYS A 1 9   ? 14.801  -15.618 10.699  0.50 17.68 ? 9   LYS A NZ   1 
ATOM   99   N  N    A HIS A 1 10  ? 11.422  -9.728  11.581  0.50 18.21 ? 10  HIS A N    1 
ATOM   100  N  N    B HIS A 1 10  ? 11.512  -9.855  11.869  0.50 15.70 ? 10  HIS A N    1 
ATOM   101  C  CA   A HIS A 1 10  ? 12.410  -8.736  11.301  0.50 16.67 ? 10  HIS A CA   1 
ATOM   102  C  CA   B HIS A 1 10  ? 12.517  -8.817  12.008  0.50 14.38 ? 10  HIS A CA   1 
ATOM   103  C  C    A HIS A 1 10  ? 11.912  -7.379  11.678  0.50 14.92 ? 10  HIS A C    1 
ATOM   104  C  C    B HIS A 1 10  ? 11.888  -7.463  12.156  0.50 13.04 ? 10  HIS A C    1 
ATOM   105  O  O    A HIS A 1 10  ? 12.687  -6.477  11.913  0.50 15.19 ? 10  HIS A O    1 
ATOM   106  O  O    B HIS A 1 10  ? 12.585  -6.611  12.645  0.50 12.88 ? 10  HIS A O    1 
ATOM   107  C  CB   A HIS A 1 10  ? 12.903  -8.867  9.838   0.50 14.20 ? 10  HIS A CB   1 
ATOM   108  C  CB   B HIS A 1 10  ? 13.557  -8.821  10.827  0.50 12.63 ? 10  HIS A CB   1 
ATOM   109  C  CG   A HIS A 1 10  ? 13.454  -10.228 9.523   0.50 14.07 ? 10  HIS A CG   1 
ATOM   110  C  CG   B HIS A 1 10  ? 14.186  -10.167 10.586  0.50 14.40 ? 10  HIS A CG   1 
ATOM   111  N  ND1  A HIS A 1 10  ? 14.396  -10.846 10.326  0.50 14.51 ? 10  HIS A ND1  1 
ATOM   112  N  ND1  B HIS A 1 10  ? 15.182  -10.674 11.393  0.50 14.20 ? 10  HIS A ND1  1 
ATOM   113  C  CD2  A HIS A 1 10  ? 13.190  -11.099 8.513   0.50 11.16 ? 10  HIS A CD2  1 
ATOM   114  C  CD2  B HIS A 1 10  ? 13.950  -11.112 9.643   0.50 15.17 ? 10  HIS A CD2  1 
ATOM   115  C  CE1  A HIS A 1 10  ? 14.661  -12.048 9.843   0.50 14.00 ? 10  HIS A CE1  1 
ATOM   116  C  CE1  B HIS A 1 10  ? 15.526  -11.873 10.963  0.50 11.92 ? 10  HIS A CE1  1 
ATOM   117  N  NE2  A HIS A 1 10  ? 13.942  -12.223 8.749   0.50 9.82  ? 10  HIS A NE2  1 
ATOM   118  N  NE2  B HIS A 1 10  ? 14.780  -12.174 9.916   0.50 14.68 ? 10  HIS A NE2  1 
ATOM   119  N  N    . ASN A 1 11  ? 10.592  -7.234  11.782  1.00 15.38 ? 11  ASN A N    1 
ATOM   120  C  CA   . ASN A 1 11  ? 10.015  -5.887  12.044  1.00 13.95 ? 11  ASN A CA   1 
ATOM   121  C  C    . ASN A 1 11  ? 8.635   -5.904  12.799  1.00 13.54 ? 11  ASN A C    1 
ATOM   122  O  O    . ASN A 1 11  ? 7.977   -4.877  12.842  1.00 14.16 ? 11  ASN A O    1 
ATOM   123  C  CB   . ASN A 1 11  ? 9.833   -5.126  10.734  1.00 12.17 ? 11  ASN A CB   1 
ATOM   124  C  CG   . ASN A 1 11  ? 8.757   -5.731  9.844   1.00 14.44 ? 11  ASN A CG   1 
ATOM   125  O  OD1  . ASN A 1 11  ? 8.204   -6.803  10.154  1.00 16.36 ? 11  ASN A OD1  1 
ATOM   126  N  ND2  . ASN A 1 11  ? 8.422   -5.056  8.740   1.00 14.86 ? 11  ASN A ND2  1 
ATOM   127  N  N    . GLY A 1 12  ? 8.298   -7.048  13.365  1.00 12.78 ? 12  GLY A N    1 
ATOM   128  C  CA   . GLY A 1 12  ? 6.925   -7.224  14.002  1.00 11.60 ? 12  GLY A CA   1 
ATOM   129  C  C    . GLY A 1 12  ? 6.936   -6.647  15.404  1.00 11.90 ? 12  GLY A C    1 
ATOM   130  O  O    . GLY A 1 12  ? 7.832   -5.931  15.936  1.00 10.99 ? 12  GLY A O    1 
ATOM   131  N  N    . PRO A 1 13  ? 5.847   -6.934  16.125  1.00 11.75 ? 13  PRO A N    1 
ATOM   132  C  CA   . PRO A 1 13  ? 5.588   -6.304  17.401  1.00 12.38 ? 13  PRO A CA   1 
ATOM   133  C  C    . PRO A 1 13  ? 6.715   -6.315  18.413  1.00 11.73 ? 13  PRO A C    1 
ATOM   134  O  O    . PRO A 1 13  ? 6.858   -5.328  19.166  1.00 11.52 ? 13  PRO A O    1 
ATOM   135  C  CB   . PRO A 1 13  ? 4.367   -7.108  17.917  1.00 11.29 ? 13  PRO A CB   1 
ATOM   136  C  CG   . PRO A 1 13  ? 3.676   -7.467  16.824  1.00 8.88  ? 13  PRO A CG   1 
ATOM   137  C  CD   . PRO A 1 13  ? 4.741   -7.777  15.690  1.00 12.48 ? 13  PRO A CD   1 
ATOM   138  N  N    A GLU A 1 14  ? 7.531   -7.379  18.508  0.50 11.66 ? 14  GLU A N    1 
ATOM   139  N  N    B GLU A 1 14  ? 7.495   -7.399  18.406  0.50 11.38 ? 14  GLU A N    1 
ATOM   140  C  CA   A GLU A 1 14  ? 8.619   -7.347  19.521  0.50 12.04 ? 14  GLU A CA   1 
ATOM   141  C  CA   B GLU A 1 14  ? 8.616   -7.558  19.315  0.50 11.51 ? 14  GLU A CA   1 
ATOM   142  C  C    A GLU A 1 14  ? 9.773   -6.379  19.149  0.50 10.47 ? 14  GLU A C    1 
ATOM   143  C  C    B GLU A 1 14  ? 9.772   -6.521  19.081  0.50 10.26 ? 14  GLU A C    1 
ATOM   144  O  O    A GLU A 1 14  ? 10.654  -6.094  19.977  0.50 11.57 ? 14  GLU A O    1 
ATOM   145  O  O    B GLU A 1 14  ? 10.637  -6.332  19.940  0.50 11.11 ? 14  GLU A O    1 
ATOM   146  C  CB   A GLU A 1 14  ? 9.198   -8.730  19.817  0.50 13.27 ? 14  GLU A CB   1 
ATOM   147  C  CB   B GLU A 1 14  ? 9.144   -8.994  19.211  0.50 12.93 ? 14  GLU A CB   1 
ATOM   148  C  CG   A GLU A 1 14  ? 8.130   -9.819  20.089  0.50 13.71 ? 14  GLU A CG   1 
ATOM   149  C  CG   B GLU A 1 14  ? 9.860   -9.300  17.936  0.50 12.17 ? 14  GLU A CG   1 
ATOM   150  C  CD   A GLU A 1 14  ? 7.182   -9.449  21.242  0.50 20.74 ? 14  GLU A CD   1 
ATOM   151  C  CD   B GLU A 1 14  ? 9.084   -9.994  16.852  0.50 16.35 ? 14  GLU A CD   1 
ATOM   152  O  OE1  A GLU A 1 14  ? 7.704   -9.145  22.341  0.50 25.87 ? 14  GLU A OE1  1 
ATOM   153  O  OE1  B GLU A 1 14  ? 7.842   -9.661  16.692  0.50 7.03  ? 14  GLU A OE1  1 
ATOM   154  O  OE2  A GLU A 1 14  ? 5.921   -9.500  21.065  0.50 19.84 ? 14  GLU A OE2  1 
ATOM   155  O  OE2  B GLU A 1 14  ? 9.828   -10.800 16.139  0.50 7.17  ? 14  GLU A OE2  1 
ATOM   156  N  N    . HIS A 1 15  ? 9.741   -5.858  17.923  1.00 10.81 ? 15  HIS A N    1 
ATOM   157  C  CA   . HIS A 1 15  ? 10.718  -4.895  17.507  1.00 10.30 ? 15  HIS A CA   1 
ATOM   158  C  C    . HIS A 1 15  ? 10.269  -3.421  17.624  1.00 12.54 ? 15  HIS A C    1 
ATOM   159  O  O    . HIS A 1 15  ? 11.115  -2.495  17.612  1.00 11.33 ? 15  HIS A O    1 
ATOM   160  C  CB   . HIS A 1 15  ? 11.114  -5.111  16.029  1.00 12.09 ? 15  HIS A CB   1 
ATOM   161  C  CG   . HIS A 1 15  ? 11.829  -6.405  15.806  1.00 13.99 ? 15  HIS A CG   1 
ATOM   162  N  ND1  . HIS A 1 15  ? 13.209  -6.491  15.911  1.00 15.83 ? 15  HIS A ND1  1 
ATOM   163  C  CD2  . HIS A 1 15  ? 11.392  -7.640  15.450  1.00 16.72 ? 15  HIS A CD2  1 
ATOM   164  C  CE1  . HIS A 1 15  ? 13.584  -7.740  15.678  1.00 19.16 ? 15  HIS A CE1  1 
ATOM   165  N  NE2  . HIS A 1 15  ? 12.509  -8.469  15.452  1.00 16.13 ? 15  HIS A NE2  1 
ATOM   166  N  N    . TRP A 1 16  ? 8.959   -3.194  17.816  1.00 8.75  ? 16  TRP A N    1 
ATOM   167  C  CA   . TRP A 1 16  ? 8.510   -1.833  17.723  1.00 9.53  ? 16  TRP A CA   1 
ATOM   168  C  C    . TRP A 1 16  ? 9.082   -0.852  18.739  1.00 6.94  ? 16  TRP A C    1 
ATOM   169  O  O    . TRP A 1 16  ? 9.148   0.355   18.404  1.00 9.70  ? 16  TRP A O    1 
ATOM   170  C  CB   . TRP A 1 16  ? 6.968   -1.847  17.851  1.00 7.41  ? 16  TRP A CB   1 
ATOM   171  C  CG   . TRP A 1 16  ? 6.310   -2.584  16.739  1.00 7.75  ? 16  TRP A CG   1 
ATOM   172  C  CD1  . TRP A 1 16  ? 6.856   -2.984  15.540  1.00 5.30  ? 16  TRP A CD1  1 
ATOM   173  C  CD2  . TRP A 1 16  ? 4.894   -2.888  16.667  1.00 6.08  ? 16  TRP A CD2  1 
ATOM   174  N  NE1  . TRP A 1 16  ? 5.908   -3.653  14.787  1.00 6.88  ? 16  TRP A NE1  1 
ATOM   175  C  CE2  . TRP A 1 16  ? 4.671   -3.506  15.393  1.00 7.71  ? 16  TRP A CE2  1 
ATOM   176  C  CE3  . TRP A 1 16  ? 3.822   -2.630  17.529  1.00 9.25  ? 16  TRP A CE3  1 
ATOM   177  C  CZ2  . TRP A 1 16  ? 3.388   -3.965  14.966  1.00 11.02 ? 16  TRP A CZ2  1 
ATOM   178  C  CZ3  . TRP A 1 16  ? 2.598   -3.087  17.147  1.00 6.82  ? 16  TRP A CZ3  1 
ATOM   179  C  CH2  . TRP A 1 16  ? 2.345   -3.679  15.873  1.00 6.93  ? 16  TRP A CH2  1 
ATOM   180  N  N    . HIS A 1 17  ? 9.418   -1.335  19.932  1.00 7.63  ? 17  HIS A N    1 
ATOM   181  C  CA   . HIS A 1 17  ? 9.946   -0.512  21.018  1.00 9.83  ? 17  HIS A CA   1 
ATOM   182  C  C    . HIS A 1 17  ? 11.189  0.293   20.603  1.00 9.65  ? 17  HIS A C    1 
ATOM   183  O  O    . HIS A 1 17  ? 11.404  1.316   21.192  1.00 11.37 ? 17  HIS A O    1 
ATOM   184  C  CB   . HIS A 1 17  ? 10.207  -1.302  22.275  1.00 9.47  ? 17  HIS A CB   1 
ATOM   185  C  CG   . HIS A 1 17  ? 11.422  -2.203  22.184  1.00 11.03 ? 17  HIS A CG   1 
ATOM   186  N  ND1  . HIS A 1 17  ? 12.658  -1.788  22.625  1.00 17.23 ? 17  HIS A ND1  1 
ATOM   187  C  CD2  . HIS A 1 17  ? 11.598  -3.431  21.638  1.00 13.53 ? 17  HIS A CD2  1 
ATOM   188  C  CE1  . HIS A 1 17  ? 13.551  -2.728  22.374  1.00 10.51 ? 17  HIS A CE1  1 
ATOM   189  N  NE2  . HIS A 1 17  ? 12.951  -3.731  21.769  1.00 12.08 ? 17  HIS A NE2  1 
ATOM   190  N  N    . LYS A 1 18  ? 11.940  -0.220  19.630  1.00 12.17 ? 18  LYS A N    1 
ATOM   191  C  CA   . LYS A 1 18  ? 13.225  0.456   19.191  1.00 13.62 ? 18  LYS A CA   1 
ATOM   192  C  C    . LYS A 1 18  ? 12.926  1.789   18.508  1.00 14.14 ? 18  LYS A C    1 
ATOM   193  O  O    . LYS A 1 18  ? 13.487  2.790   18.902  1.00 17.32 ? 18  LYS A O    1 
ATOM   194  C  CB   . LYS A 1 18  ? 13.982  -0.463  18.252  1.00 14.37 ? 18  LYS A CB   1 
ATOM   195  C  CG   . LYS A 1 18  ? 14.725  -1.550  19.021  1.00 13.45 ? 18  LYS A CG   1 
ATOM   196  C  CD   . LYS A 1 18  ? 15.390  -2.619  18.126  1.00 13.27 ? 18  LYS A CD   1 
ATOM   197  C  CE   . LYS A 1 18  ? 14.448  -3.646  17.480  1.00 15.37 ? 18  LYS A CE   1 
ATOM   198  N  NZ   . LYS A 1 18  ? 15.047  -4.443  16.326  1.00 10.28 ? 18  LYS A NZ   1 
ATOM   199  N  N    . ASP A 1 19  ? 11.905  1.844   17.635  1.00 13.96 ? 19  ASP A N    1 
ATOM   200  C  CA   . ASP A 1 19  ? 11.465  3.161   17.136  1.00 13.98 ? 19  ASP A CA   1 
ATOM   201  C  C    . ASP A 1 19  ? 10.397  3.869   17.977  1.00 13.80 ? 19  ASP A C    1 
ATOM   202  O  O    . ASP A 1 19  ? 10.267  5.083   17.853  1.00 12.92 ? 19  ASP A O    1 
ATOM   203  C  CB   . ASP A 1 19  ? 11.001  3.103   15.695  1.00 15.13 ? 19  ASP A CB   1 
ATOM   204  C  CG   . ASP A 1 19  ? 12.150  3.002   14.666  1.00 22.34 ? 19  ASP A CG   1 
ATOM   205  O  OD1  . ASP A 1 19  ? 13.192  3.621   14.843  1.00 29.18 ? 19  ASP A OD1  1 
ATOM   206  O  OD2  . ASP A 1 19  ? 11.949  2.309   13.652  1.00 32.43 ? 19  ASP A OD2  1 
ATOM   207  N  N    . PHE A 1 20  ? 9.680   3.107   18.843  1.00 11.78 ? 20  PHE A N    1 
ATOM   208  C  CA   . PHE A 1 20  ? 8.510   3.631   19.550  1.00 11.25 ? 20  PHE A CA   1 
ATOM   209  C  C    . PHE A 1 20  ? 8.592   3.173   20.962  1.00 11.34 ? 20  PHE A C    1 
ATOM   210  O  O    . PHE A 1 20  ? 7.978   2.174   21.366  1.00 10.11 ? 20  PHE A O    1 
ATOM   211  C  CB   . PHE A 1 20  ? 7.206   3.164   18.865  1.00 10.44 ? 20  PHE A CB   1 
ATOM   212  C  CG   . PHE A 1 20  ? 7.109   3.649   17.470  1.00 8.20  ? 20  PHE A CG   1 
ATOM   213  C  CD1  . PHE A 1 20  ? 6.760   4.978   17.194  1.00 12.94 ? 20  PHE A CD1  1 
ATOM   214  C  CD2  . PHE A 1 20  ? 7.421   2.775   16.416  1.00 9.41  ? 20  PHE A CD2  1 
ATOM   215  C  CE1  . PHE A 1 20  ? 6.726   5.349   15.870  1.00 13.27 ? 20  PHE A CE1  1 
ATOM   216  C  CE2  . PHE A 1 20  ? 7.426   3.165   15.080  1.00 11.67 ? 20  PHE A CE2  1 
ATOM   217  C  CZ   . PHE A 1 20  ? 7.118   4.437   14.817  1.00 11.44 ? 20  PHE A CZ   1 
ATOM   218  N  N    . PRO A 1 21  ? 9.454   3.821   21.756  1.00 11.62 ? 21  PRO A N    1 
ATOM   219  C  CA   . PRO A 1 21  ? 9.738   3.305   23.100  1.00 10.82 ? 21  PRO A CA   1 
ATOM   220  C  C    . PRO A 1 21  ? 8.479   3.156   24.009  1.00 10.02 ? 21  PRO A C    1 
ATOM   221  O  O    . PRO A 1 21  ? 8.495   2.394   24.963  1.00 10.33 ? 21  PRO A O    1 
ATOM   222  C  CB   . PRO A 1 21  ? 10.777  4.312   23.684  1.00 13.19 ? 21  PRO A CB   1 
ATOM   223  C  CG   . PRO A 1 21  ? 10.835  5.414   22.603  1.00 14.82 ? 21  PRO A CG   1 
ATOM   224  C  CD   . PRO A 1 21  ? 10.394  4.883   21.324  1.00 11.61 ? 21  PRO A CD   1 
ATOM   225  N  N    . ILE A 1 22  ? 7.460   3.972   23.712  1.00 8.29  ? 22  ILE A N    1 
ATOM   226  C  CA   A ILE A 1 22  ? 6.196   3.894   24.485  0.50 9.42  ? 22  ILE A CA   1 
ATOM   227  C  CA   B ILE A 1 22  ? 6.161   3.934   24.398  0.50 8.34  ? 22  ILE A CA   1 
ATOM   228  C  C    . ILE A 1 22  ? 5.557   2.497   24.319  1.00 7.89  ? 22  ILE A C    1 
ATOM   229  O  O    . ILE A 1 22  ? 4.615   2.132   25.080  1.00 8.92  ? 22  ILE A O    1 
ATOM   230  C  CB   A ILE A 1 22  ? 5.179   4.990   24.130  0.50 8.05  ? 22  ILE A CB   1 
ATOM   231  C  CB   B ILE A 1 22  ? 5.216   5.024   23.817  0.50 6.77  ? 22  ILE A CB   1 
ATOM   232  C  CG1  A ILE A 1 22  ? 4.155   5.191   25.271  0.50 9.64  ? 22  ILE A CG1  1 
ATOM   233  C  CG1  B ILE A 1 22  ? 4.139   5.384   24.846  0.50 4.91  ? 22  ILE A CG1  1 
ATOM   234  C  CG2  A ILE A 1 22  ? 4.503   4.590   22.854  0.50 10.15 ? 22  ILE A CG2  1 
ATOM   235  C  CG2  B ILE A 1 22  ? 4.769   4.574   22.393  0.50 5.96  ? 22  ILE A CG2  1 
ATOM   236  C  CD1  A ILE A 1 22  ? 4.687   5.815   26.536  0.50 11.38 ? 22  ILE A CD1  1 
ATOM   237  C  CD1  B ILE A 1 22  ? 3.168   6.417   24.505  0.50 5.28  ? 22  ILE A CD1  1 
ATOM   238  N  N    . ALA A 1 23  ? 6.069   1.678   23.405  1.00 7.54  ? 23  ALA A N    1 
ATOM   239  C  CA   . ALA A 1 23  ? 5.657   0.223   23.310  1.00 9.05  ? 23  ALA A CA   1 
ATOM   240  C  C    . ALA A 1 23  ? 5.739   -0.516  24.645  1.00 9.74  ? 23  ALA A C    1 
ATOM   241  O  O    . ALA A 1 23  ? 5.003   -1.543  24.840  1.00 9.44  ? 23  ALA A O    1 
ATOM   242  C  CB   . ALA A 1 23  ? 6.453   -0.582  22.253  1.00 10.09 ? 23  ALA A CB   1 
ATOM   243  N  N    . LYS A 1 24  ? 6.616   -0.088  25.571  1.00 10.27 ? 24  LYS A N    1 
ATOM   244  C  CA   . LYS A 1 24  ? 6.796   -0.795  26.864  1.00 11.37 ? 24  LYS A CA   1 
ATOM   245  C  C    . LYS A 1 24  ? 6.191   0.128   27.958  1.00 12.09 ? 24  LYS A C    1 
ATOM   246  O  O    . LYS A 1 24  ? 6.564   0.020   29.139  1.00 13.34 ? 24  LYS A O    1 
ATOM   247  C  CB   . LYS A 1 24  ? 8.324   -0.984  27.145  1.00 12.14 ? 24  LYS A CB   1 
ATOM   248  C  CG   . LYS A 1 24  ? 8.967   -1.867  26.166  1.00 14.77 ? 24  LYS A CG   1 
ATOM   249  C  CD   . LYS A 1 24  ? 10.435  -2.066  26.640  1.00 18.77 ? 24  LYS A CD   1 
ATOM   250  C  CE   . LYS A 1 24  ? 11.154  -3.057  25.668  1.00 19.33 ? 24  LYS A CE   1 
ATOM   251  N  NZ   . LYS A 1 24  ? 10.782  -4.446  25.961  1.00 21.71 ? 24  LYS A NZ   1 
ATOM   252  N  N    . GLY A 1 25  ? 5.208   0.982   27.582  1.00 10.88 ? 25  GLY A N    1 
ATOM   253  C  CA   . GLY A 1 25  ? 4.613   1.948   28.523  1.00 11.41 ? 25  GLY A CA   1 
ATOM   254  C  C    . GLY A 1 25  ? 3.573   1.350   29.470  1.00 10.27 ? 25  GLY A C    1 
ATOM   255  O  O    . GLY A 1 25  ? 3.452   0.080   29.619  1.00 11.74 ? 25  GLY A O    1 
ATOM   256  N  N    . GLU A 1 26  ? 2.914   2.281   30.165  1.00 9.99  ? 26  GLU A N    1 
ATOM   257  C  CA   . GLU A 1 26  ? 2.037   1.891   31.281  1.00 10.28 ? 26  GLU A CA   1 
ATOM   258  C  C    . GLU A 1 26  ? 0.628   1.646   30.897  1.00 9.30  ? 26  GLU A C    1 
ATOM   259  O  O    . GLU A 1 26  ? -0.163  1.116   31.731  1.00 9.89  ? 26  GLU A O    1 
ATOM   260  C  CB   . GLU A 1 26  ? 2.018   3.051   32.350  1.00 13.61 ? 26  GLU A CB   1 
ATOM   261  C  CG   . GLU A 1 26  ? 3.430   3.315   32.919  1.00 15.36 ? 26  GLU A CG   1 
ATOM   262  C  CD   . GLU A 1 26  ? 4.026   2.046   33.582  1.00 23.62 ? 26  GLU A CD   1 
ATOM   263  O  OE1  . GLU A 1 26  ? 3.364   1.350   34.440  1.00 28.86 ? 26  GLU A OE1  1 
ATOM   264  O  OE2  . GLU A 1 26  ? 5.180   1.703   33.205  1.00 28.36 ? 26  GLU A OE2  1 
ATOM   265  N  N    . ARG A 1 27  ? 0.261   1.974   29.648  1.00 7.98  ? 27  ARG A N    1 
ATOM   266  C  CA   . ARG A 1 27  ? -1.181  1.775   29.314  1.00 8.04  ? 27  ARG A CA   1 
ATOM   267  C  C    . ARG A 1 27  ? -1.231  1.309   27.836  1.00 6.42  ? 27  ARG A C    1 
ATOM   268  O  O    . ARG A 1 27  ? -1.954  1.900   26.969  1.00 5.90  ? 27  ARG A O    1 
ATOM   269  C  CB   . ARG A 1 27  ? -2.085  3.008   29.640  1.00 7.24  ? 27  ARG A CB   1 
ATOM   270  C  CG   . ARG A 1 27  ? -1.683  4.280   28.940  1.00 12.81 ? 27  ARG A CG   1 
ATOM   271  C  CD   . ARG A 1 27  ? -2.726  5.414   29.258  1.00 15.12 ? 27  ARG A CD   1 
ATOM   272  N  NE   . ARG A 1 27  ? -3.879  5.339   28.326  1.00 13.11 ? 27  ARG A NE   1 
ATOM   273  C  CZ   . ARG A 1 27  ? -4.796  6.284   28.225  1.00 11.66 ? 27  ARG A CZ   1 
ATOM   274  N  NH1  . ARG A 1 27  ? -4.717  7.444   28.931  1.00 15.07 ? 27  ARG A NH1  1 
ATOM   275  N  NH2  . ARG A 1 27  ? -5.758  6.124   27.366  1.00 13.45 ? 27  ARG A NH2  1 
ATOM   276  N  N    . GLN A 1 28  ? -0.475  0.199   27.544  1.00 5.96  ? 28  GLN A N    1 
ATOM   277  C  CA   . GLN A 1 28  ? -0.440  -0.317  26.165  1.00 4.11  ? 28  GLN A CA   1 
ATOM   278  C  C    . GLN A 1 28  ? -1.619  -1.289  25.902  1.00 5.33  ? 28  GLN A C    1 
ATOM   279  O  O    . GLN A 1 28  ? -2.105  -1.991  26.803  1.00 5.59  ? 28  GLN A O    1 
ATOM   280  C  CB   . GLN A 1 28  ? 0.903   -1.071  25.874  1.00 6.00  ? 28  GLN A CB   1 
ATOM   281  C  CG   . GLN A 1 28  ? 2.011   0.058   25.812  1.00 5.84  ? 28  GLN A CG   1 
ATOM   282  C  CD   . GLN A 1 28  ? 1.925   0.854   24.521  1.00 4.13  ? 28  GLN A CD   1 
ATOM   283  O  OE1  . GLN A 1 28  ? 2.119   0.314   23.465  1.00 7.86  ? 28  GLN A OE1  1 
ATOM   284  N  NE2  . GLN A 1 28  ? 1.553   2.167   24.616  1.00 6.72  ? 28  GLN A NE2  1 
ATOM   285  N  N    . SER A 1 29  ? -1.941  -1.386  24.617  1.00 4.56  ? 29  SER A N    1 
ATOM   286  C  CA   . SER A 1 29  ? -3.042  -2.239  24.136  1.00 4.21  ? 29  SER A CA   1 
ATOM   287  C  C    . SER A 1 29  ? -2.511  -3.145  23.036  1.00 5.41  ? 29  SER A C    1 
ATOM   288  O  O    . SER A 1 29  ? -1.560  -2.769  22.318  1.00 7.49  ? 29  SER A O    1 
ATOM   289  C  CB   . SER A 1 29  ? -4.194  -1.432  23.585  1.00 4.37  ? 29  SER A CB   1 
ATOM   290  O  OG   . SER A 1 29  ? -4.803  -0.711  24.713  1.00 5.45  ? 29  SER A OG   1 
ATOM   291  N  N    . PRO A 1 30  ? -3.177  -4.274  22.822  1.00 4.97  ? 30  PRO A N    1 
ATOM   292  C  CA   . PRO A 1 30  ? -4.370  -4.836  23.495  1.00 5.33  ? 30  PRO A CA   1 
ATOM   293  C  C    . PRO A 1 30  ? -3.921  -5.501  24.834  1.00 3.90  ? 30  PRO A C    1 
ATOM   294  O  O    . PRO A 1 30  ? -2.720  -5.485  25.149  1.00 6.31  ? 30  PRO A O    1 
ATOM   295  C  CB   . PRO A 1 30  ? -4.851  -5.868  22.461  1.00 5.45  ? 30  PRO A CB   1 
ATOM   296  C  CG   . PRO A 1 30  ? -3.511  -6.475  21.891  1.00 6.47  ? 30  PRO A CG   1 
ATOM   297  C  CD   . PRO A 1 30  ? -2.709  -5.117  21.701  1.00 4.62  ? 30  PRO A CD   1 
ATOM   298  N  N    . VAL A 1 31  ? -4.900  -6.059  25.515  1.00 4.97  ? 31  VAL A N    1 
ATOM   299  C  CA   . VAL A 1 31  ? -4.731  -6.809  26.751  1.00 5.49  ? 31  VAL A CA   1 
ATOM   300  C  C    . VAL A 1 31  ? -5.653  -8.011  26.726  1.00 6.55  ? 31  VAL A C    1 
ATOM   301  O  O    . VAL A 1 31  ? -6.652  -8.086  25.985  1.00 6.95  ? 31  VAL A O    1 
ATOM   302  C  CB   . VAL A 1 31  ? -5.026  -5.943  28.042  1.00 7.29  ? 31  VAL A CB   1 
ATOM   303  C  CG1  . VAL A 1 31  ? -4.074  -4.724  28.136  1.00 5.16  ? 31  VAL A CG1  1 
ATOM   304  C  CG2  . VAL A 1 31  ? -6.537  -5.496  28.143  1.00 6.53  ? 31  VAL A CG2  1 
ATOM   305  N  N    . ASP A 1 32  ? -5.289  -8.981  27.596  1.00 5.88  ? 32  ASP A N    1 
ATOM   306  C  CA   . ASP A 1 32  ? -6.188  -10.128 27.798  1.00 7.03  ? 32  ASP A CA   1 
ATOM   307  C  C    . ASP A 1 32  ? -7.247  -9.607  28.814  1.00 7.84  ? 32  ASP A C    1 
ATOM   308  O  O    . ASP A 1 32  ? -6.898  -8.931  29.827  1.00 6.77  ? 32  ASP A O    1 
ATOM   309  C  CB   . ASP A 1 32  ? -5.434  -11.252 28.453  1.00 7.97  ? 32  ASP A CB   1 
ATOM   310  C  CG   . ASP A 1 32  ? -6.359  -12.430 28.748  1.00 9.30  ? 32  ASP A CG   1 
ATOM   311  O  OD1  . ASP A 1 32  ? -7.050  -12.910 27.830  1.00 8.30  ? 32  ASP A OD1  1 
ATOM   312  O  OD2  . ASP A 1 32  ? -6.402  -12.865 29.999  1.00 11.10 ? 32  ASP A OD2  1 
ATOM   313  N  N    . ILE A 1 33  ? -8.497  -9.923  28.552  1.00 6.37  ? 33  ILE A N    1 
ATOM   314  C  CA   . ILE A 1 33  ? -9.596  -9.550  29.398  1.00 6.39  ? 33  ILE A CA   1 
ATOM   315  C  C    . ILE A 1 33  ? -9.919  -10.779 30.253  1.00 7.48  ? 33  ILE A C    1 
ATOM   316  O  O    . ILE A 1 33  ? -10.445 -11.785 29.774  1.00 8.05  ? 33  ILE A O    1 
ATOM   317  C  CB   . ILE A 1 33  ? -10.830 -9.114  28.602  1.00 7.87  ? 33  ILE A CB   1 
ATOM   318  C  CG1  . ILE A 1 33  ? -10.506 -7.806  27.823  1.00 6.25  ? 33  ILE A CG1  1 
ATOM   319  C  CG2  . ILE A 1 33  ? -12.038 -8.906  29.559  1.00 7.70  ? 33  ILE A CG2  1 
ATOM   320  C  CD1  . ILE A 1 33  ? -11.504 -7.541  26.660  1.00 7.78  ? 33  ILE A CD1  1 
ATOM   321  N  N    . ASP A 1 34  ? -9.564  -10.653 31.517  1.00 9.12  ? 34  ASP A N    1 
ATOM   322  C  CA   . ASP A 1 34  ? -9.850  -11.737 32.515  1.00 9.26  ? 34  ASP A CA   1 
ATOM   323  C  C    . ASP A 1 34  ? -11.286 -11.491 33.067  1.00 9.99  ? 34  ASP A C    1 
ATOM   324  O  O    . ASP A 1 34  ? -11.497 -10.488 33.793  1.00 11.64 ? 34  ASP A O    1 
ATOM   325  C  CB   . ASP A 1 34  ? -8.755  -11.695 33.584  1.00 9.33  ? 34  ASP A CB   1 
ATOM   326  C  CG   . ASP A 1 34  ? -9.014  -12.644 34.767  1.00 15.07 ? 34  ASP A CG   1 
ATOM   327  O  OD1  . ASP A 1 34  ? -10.137 -13.031 35.032  1.00 16.00 ? 34  ASP A OD1  1 
ATOM   328  O  OD2  . ASP A 1 34  ? -8.034  -13.017 35.454  1.00 25.67 ? 34  ASP A OD2  1 
ATOM   329  N  N    . THR A 1 35  ? -12.250 -12.227 32.570  1.00 10.29 ? 35  THR A N    1 
ATOM   330  C  CA   . THR A 1 35  ? -13.652 -11.927 32.773  1.00 12.41 ? 35  THR A CA   1 
ATOM   331  C  C    . THR A 1 35  ? -14.031 -12.075 34.243  1.00 13.26 ? 35  THR A C    1 
ATOM   332  O  O    . THR A 1 35  ? -15.040 -11.452 34.762  1.00 13.29 ? 35  THR A O    1 
ATOM   333  C  CB   . THR A 1 35  ? -14.533 -12.875 31.958  1.00 13.83 ? 35  THR A CB   1 
ATOM   334  O  OG1  . THR A 1 35  ? -14.348 -14.238 32.390  1.00 12.01 ? 35  THR A OG1  1 
ATOM   335  C  CG2  . THR A 1 35  ? -14.199 -12.815 30.469  1.00 9.20  ? 35  THR A CG2  1 
ATOM   336  N  N    . HIS A 1 36  ? -13.277 -12.944 34.945  1.00 12.03 ? 36  HIS A N    1 
ATOM   337  C  CA   . HIS A 1 36  ? -13.590 -13.133 36.359  1.00 14.10 ? 36  HIS A CA   1 
ATOM   338  C  C    . HIS A 1 36  ? -13.112 -11.965 37.257  1.00 16.56 ? 36  HIS A C    1 
ATOM   339  O  O    . HIS A 1 36  ? -13.779 -11.687 38.292  1.00 19.10 ? 36  HIS A O    1 
ATOM   340  C  CB   . HIS A 1 36  ? -13.171 -14.581 36.779  1.00 15.28 ? 36  HIS A CB   1 
ATOM   341  C  CG   . HIS A 1 36  ? -14.081 -15.636 36.203  1.00 15.49 ? 36  HIS A CG   1 
ATOM   342  N  ND1  . HIS A 1 36  ? -15.425 -15.675 36.542  1.00 22.10 ? 36  HIS A ND1  1 
ATOM   343  C  CD2  . HIS A 1 36  ? -13.878 -16.649 35.315  1.00 13.50 ? 36  HIS A CD2  1 
ATOM   344  C  CE1  . HIS A 1 36  ? -16.010 -16.666 35.883  1.00 25.00 ? 36  HIS A CE1  1 
ATOM   345  N  NE2  . HIS A 1 36  ? -15.091 -17.264 35.131  1.00 19.33 ? 36  HIS A NE2  1 
ATOM   346  N  N    . THR A 1 37  ? -12.038 -11.261 36.846  1.00 12.77 ? 37  THR A N    1 
ATOM   347  C  CA   . THR A 1 37  ? -11.428 -10.117 37.527  1.00 15.11 ? 37  THR A CA   1 
ATOM   348  C  C    . THR A 1 37  ? -12.037 -8.739  37.071  1.00 14.49 ? 37  THR A C    1 
ATOM   349  O  O    . THR A 1 37  ? -11.907 -7.735  37.786  1.00 16.78 ? 37  THR A O    1 
ATOM   350  C  CB   . THR A 1 37  ? -9.910  -10.154 37.346  1.00 17.63 ? 37  THR A CB   1 
ATOM   351  O  OG1  . THR A 1 37  ? -9.461  -11.315 38.062  1.00 22.90 ? 37  THR A OG1  1 
ATOM   352  C  CG2  . THR A 1 37  ? -9.234  -8.926  37.979  1.00 18.66 ? 37  THR A CG2  1 
ATOM   353  N  N    . ALA A 1 38  ? -12.710 -8.709  35.926  1.00 13.72 ? 38  ALA A N    1 
ATOM   354  C  CA   . ALA A 1 38  ? -13.264 -7.378  35.475  1.00 13.37 ? 38  ALA A CA   1 
ATOM   355  C  C    . ALA A 1 38  ? -14.387 -7.107  36.490  1.00 14.61 ? 38  ALA A C    1 
ATOM   356  O  O    . ALA A 1 38  ? -15.196 -7.970  36.753  1.00 18.69 ? 38  ALA A O    1 
ATOM   357  C  CB   . ALA A 1 38  ? -13.814 -7.465  34.111  1.00 14.89 ? 38  ALA A CB   1 
ATOM   358  N  N    . LYS A 1 39  ? -14.456 -5.892  36.987  1.00 15.04 ? 39  LYS A N    1 
ATOM   359  C  CA   . LYS A 1 39  ? -15.477 -5.569  37.990  1.00 16.81 ? 39  LYS A CA   1 
ATOM   360  C  C    . LYS A 1 39  ? -16.706 -5.026  37.274  1.00 13.65 ? 39  LYS A C    1 
ATOM   361  O  O    . LYS A 1 39  ? -16.584 -4.044  36.539  1.00 12.49 ? 39  LYS A O    1 
ATOM   362  C  CB   . LYS A 1 39  ? -14.795 -4.418  38.708  1.00 18.45 ? 39  LYS A CB   1 
ATOM   363  C  CG   . LYS A 1 39  ? -15.548 -3.649  39.717  1.00 24.90 ? 39  LYS A CG   1 
ATOM   364  C  CD   . LYS A 1 39  ? -15.623 -4.328  41.085  1.00 25.50 ? 39  LYS A CD   1 
ATOM   365  C  CE   . LYS A 1 39  ? -16.356 -3.376  41.990  1.00 30.25 ? 39  LYS A CE   1 
ATOM   366  N  NZ   . LYS A 1 39  ? -16.597 -3.851  43.388  1.00 29.36 ? 39  LYS A NZ   1 
ATOM   367  N  N    . TYR A 1 40  ? -17.914 -5.532  37.592  1.00 14.94 ? 40  TYR A N    1 
ATOM   368  C  CA   . TYR A 1 40  ? -19.108 -4.830  37.163  1.00 15.37 ? 40  TYR A CA   1 
ATOM   369  C  C    . TYR A 1 40  ? -19.158 -3.416  37.754  1.00 13.59 ? 40  TYR A C    1 
ATOM   370  O  O    . TYR A 1 40  ? -18.914 -3.225  39.004  1.00 13.23 ? 40  TYR A O    1 
ATOM   371  C  CB   . TYR A 1 40  ? -20.350 -5.640  37.534  1.00 17.80 ? 40  TYR A CB   1 
ATOM   372  C  CG   . TYR A 1 40  ? -21.619 -4.904  37.389  1.00 21.30 ? 40  TYR A CG   1 
ATOM   373  C  CD1  . TYR A 1 40  ? -22.025 -4.376  36.142  1.00 21.19 ? 40  TYR A CD1  1 
ATOM   374  C  CD2  . TYR A 1 40  ? -22.451 -4.719  38.503  1.00 28.39 ? 40  TYR A CD2  1 
ATOM   375  C  CE1  . TYR A 1 40  ? -23.212 -3.712  35.994  1.00 22.60 ? 40  TYR A CE1  1 
ATOM   376  C  CE2  . TYR A 1 40  ? -23.610 -4.029  38.390  1.00 23.32 ? 40  TYR A CE2  1 
ATOM   377  C  CZ   . TYR A 1 40  ? -23.992 -3.521  37.150  1.00 26.00 ? 40  TYR A CZ   1 
ATOM   378  O  OH   . TYR A 1 40  ? -25.167 -2.850  37.052  1.00 26.23 ? 40  TYR A OH   1 
ATOM   379  N  N    . ASP A 1 41  ? -19.512 -2.427  36.924  1.00 12.12 ? 41  ASP A N    1 
ATOM   380  C  CA   . ASP A 1 41  ? -19.485 -1.019  37.412  1.00 14.46 ? 41  ASP A CA   1 
ATOM   381  C  C    . ASP A 1 41  ? -20.849 -0.417  37.172  1.00 16.62 ? 41  ASP A C    1 
ATOM   382  O  O    . ASP A 1 41  ? -21.190 -0.060  36.040  1.00 14.34 ? 41  ASP A O    1 
ATOM   383  C  CB   . ASP A 1 41  ? -18.365 -0.202  36.758  1.00 16.66 ? 41  ASP A CB   1 
ATOM   384  C  CG   . ASP A 1 41  ? -18.347 1.218   37.248  1.00 19.73 ? 41  ASP A CG   1 
ATOM   385  O  OD1  . ASP A 1 41  ? -19.230 1.613   37.994  1.00 17.64 ? 41  ASP A OD1  1 
ATOM   386  O  OD2  . ASP A 1 41  ? -17.441 1.959   36.892  1.00 18.68 ? 41  ASP A OD2  1 
ATOM   387  N  N    . PRO A 1 42  ? -21.680 -0.423  38.239  1.00 17.39 ? 42  PRO A N    1 
ATOM   388  C  CA   . PRO A 1 42  ? -23.063 -0.067  37.992  1.00 20.10 ? 42  PRO A CA   1 
ATOM   389  C  C    . PRO A 1 42  ? -23.178 1.452   37.669  1.00 19.63 ? 42  PRO A C    1 
ATOM   390  O  O    . PRO A 1 42  ? -24.265 1.857   37.243  1.00 23.11 ? 42  PRO A O    1 
ATOM   391  C  CB   . PRO A 1 42  ? -23.763 -0.493  39.324  1.00 18.98 ? 42  PRO A CB   1 
ATOM   392  C  CG   . PRO A 1 42  ? -22.721 -0.137  40.385  1.00 21.17 ? 42  PRO A CG   1 
ATOM   393  C  CD   . PRO A 1 42  ? -21.421 -0.741  39.665  1.00 18.41 ? 42  PRO A CD   1 
ATOM   394  N  N    . SER A 1 43  ? -22.109 2.255   37.796  1.00 18.74 ? 43  SER A N    1 
ATOM   395  C  CA   . SER A 1 43  ? -22.099 3.658   37.328  1.00 20.55 ? 43  SER A CA   1 
ATOM   396  C  C    . SER A 1 43  ? -21.806 3.808   35.822  1.00 19.66 ? 43  SER A C    1 
ATOM   397  O  O    . SER A 1 43  ? -21.936 4.916   35.273  1.00 21.73 ? 43  SER A O    1 
ATOM   398  C  CB   . SER A 1 43  ? -21.087 4.531   38.093  1.00 21.17 ? 43  SER A CB   1 
ATOM   399  O  OG   . SER A 1 43  ? -19.743 4.205   37.718  1.00 24.59 ? 43  SER A OG   1 
ATOM   400  N  N    . LEU A 1 44  ? -21.327 2.749   35.160  1.00 19.65 ? 44  LEU A N    1 
ATOM   401  C  CA   . LEU A 1 44  ? -21.216 2.806   33.666  1.00 19.08 ? 44  LEU A CA   1 
ATOM   402  C  C    . LEU A 1 44  ? -22.573 2.980   33.009  1.00 20.90 ? 44  LEU A C    1 
ATOM   403  O  O    . LEU A 1 44  ? -23.550 2.373   33.423  1.00 21.81 ? 44  LEU A O    1 
ATOM   404  C  CB   . LEU A 1 44  ? -20.572 1.522   33.116  1.00 18.40 ? 44  LEU A CB   1 
ATOM   405  C  CG   . LEU A 1 44  ? -19.095 1.445   33.429  1.00 13.22 ? 44  LEU A CG   1 
ATOM   406  C  CD1  . LEU A 1 44  ? -18.548 0.000   33.084  1.00 12.57 ? 44  LEU A CD1  1 
ATOM   407  C  CD2  . LEU A 1 44  ? -18.232 2.589   32.813  1.00 14.30 ? 44  LEU A CD2  1 
ATOM   408  N  N    . LYS A 1 45  ? -22.617 3.748   31.937  1.00 20.18 ? 45  LYS A N    1 
ATOM   409  C  CA   . LYS A 1 45  ? -23.889 3.947   31.182  1.00 20.10 ? 45  LYS A CA   1 
ATOM   410  C  C    . LYS A 1 45  ? -23.934 3.038   30.014  1.00 19.56 ? 45  LYS A C    1 
ATOM   411  O  O    . LYS A 1 45  ? -22.892 2.499   29.572  1.00 19.77 ? 45  LYS A O    1 
ATOM   412  C  CB   . LYS A 1 45  ? -23.947 5.358   30.676  1.00 20.03 ? 45  LYS A CB   1 
ATOM   413  C  CG   . LYS A 1 45  ? -23.975 6.298   31.815  1.00 22.72 ? 45  LYS A CG   1 
ATOM   414  C  CD   . LYS A 1 45  ? -24.069 7.694   31.353  1.00 27.52 ? 45  LYS A CD   1 
ATOM   415  C  CE   . LYS A 1 45  ? -24.404 8.584   32.548  1.00 37.09 ? 45  LYS A CE   1 
ATOM   416  N  NZ   . LYS A 1 45  ? -23.339 8.672   33.589  1.00 39.27 ? 45  LYS A NZ   1 
ATOM   417  N  N    . PRO A 1 46  ? -25.174 2.819   29.485  1.00 17.78 ? 46  PRO A N    1 
ATOM   418  C  CA   . PRO A 1 46  ? -25.297 2.162   28.204  1.00 17.21 ? 46  PRO A CA   1 
ATOM   419  C  C    . PRO A 1 46  ? -24.449 2.951   27.186  1.00 13.64 ? 46  PRO A C    1 
ATOM   420  O  O    . PRO A 1 46  ? -24.415 4.190   27.244  1.00 14.77 ? 46  PRO A O    1 
ATOM   421  C  CB   . PRO A 1 46  ? -26.788 2.318   27.882  1.00 17.17 ? 46  PRO A CB   1 
ATOM   422  C  CG   . PRO A 1 46  ? -27.478 2.411   29.239  1.00 18.17 ? 46  PRO A CG   1 
ATOM   423  C  CD   . PRO A 1 46  ? -26.475 3.147   30.112  1.00 18.26 ? 46  PRO A CD   1 
ATOM   424  N  N    . LEU A 1 47  ? -23.787 2.201   26.306  1.00 17.58 ? 47  LEU A N    1 
ATOM   425  C  CA   . LEU A 1 47  ? -23.059 2.821   25.181  1.00 14.92 ? 47  LEU A CA   1 
ATOM   426  C  C    . LEU A 1 47  ? -24.117 3.416   24.277  1.00 17.89 ? 47  LEU A C    1 
ATOM   427  O  O    . LEU A 1 47  ? -25.179 2.754   24.033  1.00 18.20 ? 47  LEU A O    1 
ATOM   428  C  CB   . LEU A 1 47  ? -22.377 1.791   24.306  1.00 17.76 ? 47  LEU A CB   1 
ATOM   429  C  CG   . LEU A 1 47  ? -20.937 1.521   24.194  1.00 20.61 ? 47  LEU A CG   1 
ATOM   430  C  CD1  . LEU A 1 47  ? -20.599 0.837   22.906  1.00 19.59 ? 47  LEU A CD1  1 
ATOM   431  C  CD2  . LEU A 1 47  ? -20.258 2.928   24.367  1.00 21.03 ? 47  LEU A CD2  1 
ATOM   432  N  N    . SER A 1 48  ? -23.816 4.583   23.706  1.00 13.08 ? 48  SER A N    1 
ATOM   433  C  CA   . SER A 1 48  ? -24.642 5.216   22.664  1.00 12.17 ? 48  SER A CA   1 
ATOM   434  C  C    . SER A 1 48  ? -23.891 5.245   21.372  1.00 12.12 ? 48  SER A C    1 
ATOM   435  O  O    . SER A 1 48  ? -22.878 5.938   21.196  1.00 10.85 ? 48  SER A O    1 
ATOM   436  C  CB   . SER A 1 48  ? -25.095 6.620   23.115  1.00 13.91 ? 48  SER A CB   1 
ATOM   437  O  OG   . SER A 1 48  ? -25.675 7.386   22.094  1.00 14.00 ? 48  SER A OG   1 
ATOM   438  N  N    . VAL A 1 49  ? -24.410 4.509   20.429  1.00 11.18 ? 49  VAL A N    1 
ATOM   439  C  CA   . VAL A 1 49  ? -23.778 4.393   19.116  1.00 14.60 ? 49  VAL A CA   1 
ATOM   440  C  C    . VAL A 1 49  ? -24.747 4.966   18.084  1.00 14.95 ? 49  VAL A C    1 
ATOM   441  O  O    . VAL A 1 49  ? -25.795 4.401   17.829  1.00 17.23 ? 49  VAL A O    1 
ATOM   442  C  CB   . VAL A 1 49  ? -23.455 2.896   18.770  1.00 14.66 ? 49  VAL A CB   1 
ATOM   443  C  CG1  . VAL A 1 49  ? -22.574 2.796   17.498  1.00 19.84 ? 49  VAL A CG1  1 
ATOM   444  C  CG2  . VAL A 1 49  ? -22.766 2.128   20.002  1.00 18.96 ? 49  VAL A CG2  1 
ATOM   445  N  N    . SER A 1 50  ? -24.436 6.130   17.568  1.00 13.12 ? 50  SER A N    1 
ATOM   446  C  CA   . SER A 1 50  ? -25.359 6.855   16.673  1.00 15.26 ? 50  SER A CA   1 
ATOM   447  C  C    . SER A 1 50  ? -24.731 6.895   15.295  1.00 14.60 ? 50  SER A C    1 
ATOM   448  O  O    . SER A 1 50  ? -24.031 7.823   14.943  1.00 14.24 ? 50  SER A O    1 
ATOM   449  C  CB   . SER A 1 50  ? -25.747 8.226   17.207  1.00 15.71 ? 50  SER A CB   1 
ATOM   450  O  OG   . SER A 1 50  ? -26.427 8.063   18.427  1.00 23.14 ? 50  SER A OG   1 
ATOM   451  N  N    . TYR A 1 51  ? -24.927 5.832   14.516  1.00 14.71 ? 51  TYR A N    1 
ATOM   452  C  CA   . TYR A 1 51  ? -24.335 5.717   13.183  1.00 11.83 ? 51  TYR A CA   1 
ATOM   453  C  C    . TYR A 1 51  ? -25.300 5.957   11.957  1.00 14.65 ? 51  TYR A C    1 
ATOM   454  O  O    . TYR A 1 51  ? -24.832 5.834   10.804  1.00 14.57 ? 51  TYR A O    1 
ATOM   455  C  CB   . TYR A 1 51  ? -23.642 4.342   12.954  1.00 12.02 ? 51  TYR A CB   1 
ATOM   456  C  CG   . TYR A 1 51  ? -22.358 4.089   13.693  1.00 9.79  ? 51  TYR A CG   1 
ATOM   457  C  CD1  . TYR A 1 51  ? -21.640 5.137   14.347  1.00 12.29 ? 51  TYR A CD1  1 
ATOM   458  C  CD2  . TYR A 1 51  ? -21.896 2.782   13.789  1.00 9.69  ? 51  TYR A CD2  1 
ATOM   459  C  CE1  . TYR A 1 51  ? -20.459 4.819   15.119  1.00 6.46  ? 51  TYR A CE1  1 
ATOM   460  C  CE2  . TYR A 1 51  ? -20.712 2.429   14.485  1.00 8.76  ? 51  TYR A CE2  1 
ATOM   461  C  CZ   . TYR A 1 51  ? -20.007 3.481   15.162  1.00 10.52 ? 51  TYR A CZ   1 
ATOM   462  O  OH   . TYR A 1 51  ? -18.863 3.179   15.850  1.00 9.46  ? 51  TYR A OH   1 
ATOM   463  N  N    . ASP A 1 52  ? -26.552 6.344   12.258  1.00 17.48 ? 52  ASP A N    1 
ATOM   464  C  CA   A ASP A 1 52  ? -27.557 6.634   11.215  0.50 18.80 ? 52  ASP A CA   1 
ATOM   465  C  CA   B ASP A 1 52  ? -27.565 6.651   11.216  0.50 19.29 ? 52  ASP A CA   1 
ATOM   466  C  C    . ASP A 1 52  ? -27.070 7.583   10.097  1.00 19.68 ? 52  ASP A C    1 
ATOM   467  O  O    . ASP A 1 52  ? -27.344 7.350   8.906   1.00 20.27 ? 52  ASP A O    1 
ATOM   468  C  CB   A ASP A 1 52  ? -28.879 7.096   11.855  0.50 18.88 ? 52  ASP A CB   1 
ATOM   469  C  CB   B ASP A 1 52  ? -28.834 7.220   11.859  0.50 19.45 ? 52  ASP A CB   1 
ATOM   470  C  CG   A ASP A 1 52  ? -28.681 8.133   12.962  0.50 18.19 ? 52  ASP A CG   1 
ATOM   471  C  CG   B ASP A 1 52  ? -29.945 7.431   10.862  0.50 21.91 ? 52  ASP A CG   1 
ATOM   472  O  OD1  A ASP A 1 52  ? -28.170 7.826   14.079  0.50 24.80 ? 52  ASP A OD1  1 
ATOM   473  O  OD1  B ASP A 1 52  ? -30.536 6.430   10.385  0.50 26.72 ? 52  ASP A OD1  1 
ATOM   474  O  OD2  A ASP A 1 52  ? -29.029 9.292   12.703  0.50 27.24 ? 52  ASP A OD2  1 
ATOM   475  O  OD2  B ASP A 1 52  ? -30.229 8.609   10.555  0.50 26.11 ? 52  ASP A OD2  1 
ATOM   476  N  N    . GLN A 1 53  ? -26.298 8.595   10.445  1.00 18.22 ? 53  GLN A N    1 
ATOM   477  C  CA   . GLN A 1 53  ? -25.823 9.550   9.422   1.00 19.89 ? 53  GLN A CA   1 
ATOM   478  C  C    . GLN A 1 53  ? -24.361 9.349   8.975   1.00 16.59 ? 53  GLN A C    1 
ATOM   479  O  O    . GLN A 1 53  ? -23.807 10.203  8.320   1.00 16.33 ? 53  GLN A O    1 
ATOM   480  C  CB   . GLN A 1 53  ? -26.008 10.993  9.927   1.00 19.45 ? 53  GLN A CB   1 
ATOM   481  C  CG   . GLN A 1 53  ? -27.470 11.406  10.226  1.00 26.99 ? 53  GLN A CG   1 
ATOM   482  C  CD   . GLN A 1 53  ? -28.361 11.215  9.045   1.00 30.42 ? 53  GLN A CD   1 
ATOM   483  O  OE1  . GLN A 1 53  ? -29.510 10.790  9.197   1.00 38.71 ? 53  GLN A OE1  1 
ATOM   484  N  NE2  . GLN A 1 53  ? -27.840 11.495  7.823   1.00 37.15 ? 53  GLN A NE2  1 
ATOM   485  N  N    . ALA A 1 54  ? -23.712 8.244   9.379   1.00 15.35 ? 54  ALA A N    1 
ATOM   486  C  CA   . ALA A 1 54  ? -22.375 7.935   8.922   1.00 12.22 ? 54  ALA A CA   1 
ATOM   487  C  C    . ALA A 1 54  ? -22.182 8.030   7.409   1.00 14.87 ? 54  ALA A C    1 
ATOM   488  O  O    . ALA A 1 54  ? -23.001 7.522   6.658   1.00 15.68 ? 54  ALA A O    1 
ATOM   489  C  CB   . ALA A 1 54  ? -21.933 6.472   9.461   1.00 13.35 ? 54  ALA A CB   1 
ATOM   490  N  N    A THR A 1 55  ? -21.111 8.718   7.006   0.50 13.53 ? 55  THR A N    1 
ATOM   491  N  N    B THR A 1 55  ? -21.143 8.716   6.967   0.50 13.64 ? 55  THR A N    1 
ATOM   492  C  CA   A THR A 1 55  ? -20.712 8.919   5.607   0.50 13.21 ? 55  THR A CA   1 
ATOM   493  C  CA   B THR A 1 55  ? -20.867 8.798   5.544   0.50 13.29 ? 55  THR A CA   1 
ATOM   494  C  C    A THR A 1 55  ? -19.373 8.340   5.281   0.50 12.38 ? 55  THR A C    1 
ATOM   495  C  C    B THR A 1 55  ? -19.461 8.363   5.207   0.50 12.47 ? 55  THR A C    1 
ATOM   496  O  O    A THR A 1 55  ? -18.351 8.978   5.556   0.50 11.33 ? 55  THR A O    1 
ATOM   497  O  O    B THR A 1 55  ? -18.496 9.086   5.436   0.50 10.93 ? 55  THR A O    1 
ATOM   498  C  CB   A THR A 1 55  ? -20.682 10.428  5.229   0.50 13.10 ? 55  THR A CB   1 
ATOM   499  C  CB   B THR A 1 55  ? -21.308 10.182  4.936   0.50 14.25 ? 55  THR A CB   1 
ATOM   500  O  OG1  A THR A 1 55  ? -22.025 10.917  5.253   0.50 16.59 ? 55  THR A OG1  1 
ATOM   501  O  OG1  B THR A 1 55  ? -21.088 10.194  3.516   0.50 13.40 ? 55  THR A OG1  1 
ATOM   502  C  CG2  A THR A 1 55  ? -20.115 10.601  3.823   0.50 13.03 ? 55  THR A CG2  1 
ATOM   503  C  CG2  B THR A 1 55  ? -20.631 11.348  5.642   0.50 10.77 ? 55  THR A CG2  1 
ATOM   504  N  N    . SER A 1 56  ? -19.358 7.141   4.682   1.00 13.13 ? 56  SER A N    1 
ATOM   505  C  CA   . SER A 1 56  ? -18.075 6.591   4.306   1.00 13.83 ? 56  SER A CA   1 
ATOM   506  C  C    . SER A 1 56  ? -17.538 7.281   3.024   1.00 14.97 ? 56  SER A C    1 
ATOM   507  O  O    . SER A 1 56  ? -18.330 7.772   2.171   1.00 17.91 ? 56  SER A O    1 
ATOM   508  C  CB   . SER A 1 56  ? -18.126 5.051   4.110   1.00 16.41 ? 56  SER A CB   1 
ATOM   509  O  OG   . SER A 1 56  ? -18.975 4.665   2.989   1.00 17.07 ? 56  SER A OG   1 
ATOM   510  N  N    . LEU A 1 57  ? -16.255 7.329   2.875   1.00 13.74 ? 57  LEU A N    1 
ATOM   511  C  CA   . LEU A 1 57  ? -15.683 7.996   1.665   1.00 16.02 ? 57  LEU A CA   1 
ATOM   512  C  C    . LEU A 1 57  ? -14.896 7.016   0.806   1.00 15.35 ? 57  LEU A C    1 
ATOM   513  O  O    . LEU A 1 57  ? -14.952 7.028   -0.463  1.00 14.33 ? 57  LEU A O    1 
ATOM   514  C  CB   . LEU A 1 57  ? -14.737 9.081   2.060   1.00 17.64 ? 57  LEU A CB   1 
ATOM   515  C  CG   . LEU A 1 57  ? -15.297 10.466  2.518   1.00 24.66 ? 57  LEU A CG   1 
ATOM   516  C  CD1  . LEU A 1 57  ? -14.246 11.221  3.298   1.00 25.28 ? 57  LEU A CD1  1 
ATOM   517  C  CD2  . LEU A 1 57  ? -15.772 11.308  1.316   1.00 28.92 ? 57  LEU A CD2  1 
ATOM   518  N  N    . ARG A 1 58  ? -14.074 6.218   1.487   1.00 13.21 ? 58  ARG A N    1 
ATOM   519  C  CA   . ARG A 1 58  ? -12.966 5.569   0.818   1.00 12.51 ? 58  ARG A CA   1 
ATOM   520  C  C    . ARG A 1 58  ? -12.510 4.372   1.597   1.00 13.58 ? 58  ARG A C    1 
ATOM   521  O  O    . ARG A 1 58  ? -12.643 4.362   2.831   1.00 13.80 ? 58  ARG A O    1 
ATOM   522  C  CB   . ARG A 1 58  ? -11.774 6.528   0.691   1.00 12.91 ? 58  ARG A CB   1 
ATOM   523  C  CG   . ARG A 1 58  ? -10.926 6.159   -0.404  1.00 15.55 ? 58  ARG A CG   1 
ATOM   524  C  CD   . ARG A 1 58  ? -9.879  7.252   -0.604  1.00 21.41 ? 58  ARG A CD   1 
ATOM   525  N  NE   . ARG A 1 58  ? -9.086  7.247   0.642   1.00 18.04 ? 58  ARG A NE   1 
ATOM   526  C  CZ   . ARG A 1 58  ? -7.750  7.352   0.650   1.00 14.29 ? 58  ARG A CZ   1 
ATOM   527  N  NH1  . ARG A 1 58  ? -7.141  7.547   -0.515  1.00 17.22 ? 58  ARG A NH1  1 
ATOM   528  N  NH2  . ARG A 1 58  ? -7.045  7.362   1.811   1.00 15.89 ? 58  ARG A NH2  1 
ATOM   529  N  N    . ILE A 1 59  ? -11.913 3.433   0.858   1.00 12.54 ? 59  ILE A N    1 
ATOM   530  C  CA   . ILE A 1 59  ? -11.218 2.283   1.551   1.00 12.95 ? 59  ILE A CA   1 
ATOM   531  C  C    . ILE A 1 59  ? -9.771  2.242   1.058   1.00 12.06 ? 59  ILE A C    1 
ATOM   532  O  O    . ILE A 1 59  ? -9.499  2.398   -0.139  1.00 12.16 ? 59  ILE A O    1 
ATOM   533  C  CB   . ILE A 1 59  ? -11.986 0.958   1.364   1.00 11.79 ? 59  ILE A CB   1 
ATOM   534  C  CG1  . ILE A 1 59  ? -11.312 -0.212  2.104   1.00 13.57 ? 59  ILE A CG1  1 
ATOM   535  C  CG2  . ILE A 1 59  ? -12.095 0.593   -0.218  1.00 13.55 ? 59  ILE A CG2  1 
ATOM   536  C  CD1  . ILE A 1 59  ? -12.240 -1.492  1.973   1.00 14.04 ? 59  ILE A CD1  1 
ATOM   537  N  N    . LEU A 1 60  ? -8.817  2.010   1.969   1.00 12.75 ? 60  LEU A N    1 
ATOM   538  C  CA   . LEU A 1 60  ? -7.451  2.084   1.694   1.00 9.37  ? 60  LEU A CA   1 
ATOM   539  C  C    . LEU A 1 60  ? -6.626  0.904   2.267   1.00 11.71 ? 60  LEU A C    1 
ATOM   540  O  O    . LEU A 1 60  ? -6.769  0.552   3.458   1.00 11.01 ? 60  LEU A O    1 
ATOM   541  C  CB   . LEU A 1 60  ? -6.919  3.411   2.344   1.00 11.58 ? 60  LEU A CB   1 
ATOM   542  C  CG   . LEU A 1 60  ? -5.413  3.568   2.305   1.00 9.58  ? 60  LEU A CG   1 
ATOM   543  C  CD1  . LEU A 1 60  ? -4.815  3.701   0.864   1.00 12.30 ? 60  LEU A CD1  1 
ATOM   544  C  CD2  . LEU A 1 60  ? -4.899  4.703   3.298   1.00 9.55  ? 60  LEU A CD2  1 
ATOM   545  N  N    . ASN A 1 61  ? -5.817  0.307   1.420   1.00 9.90  ? 61  ASN A N    1 
ATOM   546  C  CA   . ASN A 1 61  ? -4.869  -0.641  1.897   1.00 9.93  ? 61  ASN A CA   1 
ATOM   547  C  C    . ASN A 1 61  ? -3.607  0.137   2.261   1.00 12.20 ? 61  ASN A C    1 
ATOM   548  O  O    . ASN A 1 61  ? -2.966  0.731   1.400   1.00 11.98 ? 61  ASN A O    1 
ATOM   549  C  CB   . ASN A 1 61  ? -4.578  -1.736  0.875   1.00 11.77 ? 61  ASN A CB   1 
ATOM   550  C  CG   . ASN A 1 61  ? -3.463  -2.668  1.280   1.00 12.55 ? 61  ASN A CG   1 
ATOM   551  O  OD1  . ASN A 1 61  ? -2.546  -2.420  2.101   1.00 12.92 ? 61  ASN A OD1  1 
ATOM   552  N  ND2  . ASN A 1 61  ? -3.527  -3.896  0.648   1.00 12.32 ? 61  ASN A ND2  1 
ATOM   553  N  N    . ASN A 1 62  ? -3.314  0.239   3.559   1.00 11.82 ? 62  ASN A N    1 
ATOM   554  C  CA   . ASN A 1 62  ? -2.186  1.088   3.987   1.00 12.46 ? 62  ASN A CA   1 
ATOM   555  C  C    . ASN A 1 62  ? -0.940  0.285   4.257   1.00 12.61 ? 62  ASN A C    1 
ATOM   556  O  O    . ASN A 1 62  ? 0.099   0.753   4.834   1.00 16.55 ? 62  ASN A O    1 
ATOM   557  C  CB   . ASN A 1 62  ? -2.590  1.922   5.222   1.00 11.99 ? 62  ASN A CB   1 
ATOM   558  C  CG   . ASN A 1 62  ? -2.866  1.039   6.421   1.00 16.07 ? 62  ASN A CG   1 
ATOM   559  O  OD1  . ASN A 1 62  ? -2.567  -0.201  6.419   1.00 12.45 ? 62  ASN A OD1  1 
ATOM   560  N  ND2  . ASN A 1 62  ? -3.371  1.691   7.477   1.00 20.93 ? 62  ASN A ND2  1 
ATOM   561  N  N    . GLY A 1 63  ? -0.931  -0.977  3.778   1.00 10.62 ? 63  GLY A N    1 
ATOM   562  C  CA   . GLY A 1 63  ? 0.097   -1.854  3.978   1.00 9.58  ? 63  GLY A CA   1 
ATOM   563  C  C    . GLY A 1 63  ? 0.208   -2.642  5.318   1.00 10.76 ? 63  GLY A C    1 
ATOM   564  O  O    . GLY A 1 63  ? 1.060   -3.483  5.480   1.00 12.82 ? 63  GLY A O    1 
ATOM   565  N  N    A HIS A 1 64  ? -0.722  -2.378  6.188   0.50 9.90  ? 64  HIS A N    1 
ATOM   566  N  N    B HIS A 1 64  ? -0.577  -2.244  6.330   0.50 10.45 ? 64  HIS A N    1 
ATOM   567  C  CA   A HIS A 1 64  ? -0.807  -3.070  7.466   0.50 9.97  ? 64  HIS A CA   1 
ATOM   568  C  CA   B HIS A 1 64  ? -0.827  -3.047  7.620   0.50 10.70 ? 64  HIS A CA   1 
ATOM   569  C  C    A HIS A 1 64  ? -2.159  -3.744  7.528   0.50 9.51  ? 64  HIS A C    1 
ATOM   570  C  C    B HIS A 1 64  ? -2.253  -3.541  7.848   0.50 9.17  ? 64  HIS A C    1 
ATOM   571  O  O    A HIS A 1 64  ? -2.229  -4.975  7.883   0.50 8.15  ? 64  HIS A O    1 
ATOM   572  O  O    B HIS A 1 64  ? -2.510  -4.410  8.695   0.50 6.95  ? 64  HIS A O    1 
ATOM   573  C  CB   A HIS A 1 64  ? -0.630  -2.062  8.565   0.50 8.21  ? 64  HIS A CB   1 
ATOM   574  C  CB   B HIS A 1 64  ? -0.423  -2.399  8.950   0.50 11.05 ? 64  HIS A CB   1 
ATOM   575  C  CG   A HIS A 1 64  ? 0.690   -1.341  8.462   0.50 8.53  ? 64  HIS A CG   1 
ATOM   576  C  CG   B HIS A 1 64  ? -0.804  -0.964  9.125   0.50 15.77 ? 64  HIS A CG   1 
ATOM   577  N  ND1  A HIS A 1 64  ? 1.891   -1.994  8.625   0.50 10.37 ? 64  HIS A ND1  1 
ATOM   578  N  ND1  B HIS A 1 64  ? -1.863  -0.548  9.920   0.50 17.03 ? 64  HIS A ND1  1 
ATOM   579  C  CD2  A HIS A 1 64  ? 0.990   -0.051  8.193   0.50 6.51  ? 64  HIS A CD2  1 
ATOM   580  C  CD2  B HIS A 1 64  ? -0.169  0.165   8.713   0.50 16.29 ? 64  HIS A CD2  1 
ATOM   581  C  CE1  A HIS A 1 64  ? 2.887   -1.138  8.472   0.50 7.08  ? 64  HIS A CE1  1 
ATOM   582  C  CE1  B HIS A 1 64  ? -1.894  0.770   9.933   0.50 17.76 ? 64  HIS A CE1  1 
ATOM   583  N  NE2  A HIS A 1 64  ? 2.371   0.042   8.167   0.50 5.26  ? 64  HIS A NE2  1 
ATOM   584  N  NE2  B HIS A 1 64  ? -0.873  1.228   9.225   0.50 19.94 ? 64  HIS A NE2  1 
ATOM   585  N  N    . ALA A 1 65  ? -3.190  -2.971  7.139   1.00 9.94  ? 65  ALA A N    1 
ATOM   586  C  CA   . ALA A 1 65  ? -4.615  -3.365  7.210   1.00 10.29 ? 65  ALA A CA   1 
ATOM   587  C  C    . ALA A 1 65  ? -5.372  -2.638  6.098   1.00 8.83  ? 65  ALA A C    1 
ATOM   588  O  O    . ALA A 1 65  ? -4.703  -2.018  5.208   1.00 10.48 ? 65  ALA A O    1 
ATOM   589  C  CB   . ALA A 1 65  ? -5.270  -3.179  8.642   1.00 10.42 ? 65  ALA A CB   1 
ATOM   590  N  N    . PHE A 1 66  ? -6.684  -2.680  6.104   1.00 7.51  ? 66  PHE A N    1 
ATOM   591  C  CA   . PHE A 1 66  ? -7.409  -1.751  5.201   1.00 9.04  ? 66  PHE A CA   1 
ATOM   592  C  C    . PHE A 1 66  ? -8.258  -0.873  6.109   1.00 10.43 ? 66  PHE A C    1 
ATOM   593  O  O    . PHE A 1 66  ? -8.924  -1.358  7.094   1.00 9.83  ? 66  PHE A O    1 
ATOM   594  C  CB   . PHE A 1 66  ? -8.217  -2.485  4.116   1.00 9.51  ? 66  PHE A CB   1 
ATOM   595  C  CG   . PHE A 1 66  ? -9.278  -3.415  4.652   1.00 8.85  ? 66  PHE A CG   1 
ATOM   596  C  CD1  . PHE A 1 66  ? -10.546 -2.938  5.039   1.00 8.53  ? 66  PHE A CD1  1 
ATOM   597  C  CD2  . PHE A 1 66  ? -8.991  -4.812  4.777   1.00 8.86  ? 66  PHE A CD2  1 
ATOM   598  C  CE1  . PHE A 1 66  ? -11.532 -3.780  5.522   1.00 11.75 ? 66  PHE A CE1  1 
ATOM   599  C  CE2  . PHE A 1 66  ? -9.995  -5.670  5.330   1.00 9.45  ? 66  PHE A CE2  1 
ATOM   600  C  CZ   . PHE A 1 66  ? -11.235 -5.191  5.663   1.00 10.31 ? 66  PHE A CZ   1 
ATOM   601  N  N    . ASN A 1 67  ? -8.280  0.437   5.805   1.00 10.08 ? 67  ASN A N    1 
ATOM   602  C  CA   . ASN A 1 67  ? -9.183  1.308   6.545   1.00 11.02 ? 67  ASN A CA   1 
ATOM   603  C  C    . ASN A 1 67  ? -10.384 1.756   5.736   1.00 11.24 ? 67  ASN A C    1 
ATOM   604  O  O    . ASN A 1 67  ? -10.184 2.189   4.594   1.00 12.57 ? 67  ASN A O    1 
ATOM   605  C  CB   . ASN A 1 67  ? -8.463  2.622   6.908   1.00 12.43 ? 67  ASN A CB   1 
ATOM   606  C  CG   . ASN A 1 67  ? -7.306  2.463   7.831   1.00 13.49 ? 67  ASN A CG   1 
ATOM   607  O  OD1  . ASN A 1 67  ? -6.574  3.462   8.003   1.00 17.06 ? 67  ASN A OD1  1 
ATOM   608  N  ND2  . ASN A 1 67  ? -7.127  1.334   8.478   1.00 9.19  ? 67  ASN A ND2  1 
ATOM   609  N  N    . VAL A 1 68  ? -11.569 1.640   6.300   1.00 8.87  ? 68  VAL A N    1 
ATOM   610  C  CA   . VAL A 1 68  ? -12.769 2.234   5.730   1.00 10.00 ? 68  VAL A CA   1 
ATOM   611  C  C    . VAL A 1 68  ? -12.936 3.648   6.360   1.00 13.53 ? 68  VAL A C    1 
ATOM   612  O  O    . VAL A 1 68  ? -13.066 3.750   7.608   1.00 9.67  ? 68  VAL A O    1 
ATOM   613  C  CB   . VAL A 1 68  ? -13.997 1.390   5.928   1.00 11.29 ? 68  VAL A CB   1 
ATOM   614  C  CG1  . VAL A 1 68  ? -15.241 2.196   5.385   1.00 10.87 ? 68  VAL A CG1  1 
ATOM   615  C  CG2  . VAL A 1 68  ? -13.826 0.089   5.116   1.00 13.05 ? 68  VAL A CG2  1 
ATOM   616  N  N    . GLU A 1 69  ? -12.854 4.721   5.521   1.00 12.13 ? 69  GLU A N    1 
ATOM   617  C  CA   . GLU A 1 69  ? -12.616 6.064   6.045   1.00 13.51 ? 69  GLU A CA   1 
ATOM   618  C  C    . GLU A 1 69  ? -13.977 6.786   5.938   1.00 14.24 ? 69  GLU A C    1 
ATOM   619  O  O    . GLU A 1 69  ? -14.761 6.539   4.956   1.00 14.75 ? 69  GLU A O    1 
ATOM   620  C  CB   . GLU A 1 69  ? -11.636 6.778   5.139   1.00 15.53 ? 69  GLU A CB   1 
ATOM   621  C  CG   . GLU A 1 69  ? -10.233 6.282   5.283   1.00 12.90 ? 69  GLU A CG   1 
ATOM   622  C  CD   . GLU A 1 69  ? -9.470  6.659   4.080   1.00 18.43 ? 69  GLU A CD   1 
ATOM   623  O  OE1  . GLU A 1 69  ? -10.086 7.362   3.245   1.00 18.00 ? 69  GLU A OE1  1 
ATOM   624  O  OE2  . GLU A 1 69  ? -8.288  6.322   3.964   1.00 16.28 ? 69  GLU A OE2  1 
ATOM   625  N  N    . PHE A 1 70  ? -14.246 7.659   6.927   1.00 12.10 ? 70  PHE A N    1 
ATOM   626  C  CA   . PHE A 1 70  ? -15.499 8.418   6.996   1.00 10.64 ? 70  PHE A CA   1 
ATOM   627  C  C    . PHE A 1 70  ? -15.242 9.898   6.854   1.00 10.38 ? 70  PHE A C    1 
ATOM   628  O  O    . PHE A 1 70  ? -14.216 10.367  7.254   1.00 10.22 ? 70  PHE A O    1 
ATOM   629  C  CB   . PHE A 1 70  ? -16.231 8.094   8.290   1.00 11.76 ? 70  PHE A CB   1 
ATOM   630  C  CG   . PHE A 1 70  ? -16.805 6.701   8.267   1.00 9.50  ? 70  PHE A CG   1 
ATOM   631  C  CD1  . PHE A 1 70  ? -15.990 5.572   8.489   1.00 13.33 ? 70  PHE A CD1  1 
ATOM   632  C  CD2  . PHE A 1 70  ? -18.130 6.499   7.952   1.00 10.32 ? 70  PHE A CD2  1 
ATOM   633  C  CE1  . PHE A 1 70  ? -16.543 4.258   8.390   1.00 11.38 ? 70  PHE A CE1  1 
ATOM   634  C  CE2  . PHE A 1 70  ? -18.656 5.239   7.837   1.00 10.42 ? 70  PHE A CE2  1 
ATOM   635  C  CZ   . PHE A 1 70  ? -17.807 4.092   8.053   1.00 12.57 ? 70  PHE A CZ   1 
ATOM   636  N  N    . ASP A 1 71  ? -16.232 10.611  6.315   1.00 12.44 ? 71  ASP A N    1 
ATOM   637  C  CA   . ASP A 1 71  ? -16.178 12.084  6.402   1.00 13.78 ? 71  ASP A CA   1 
ATOM   638  C  C    . ASP A 1 71  ? -16.553 12.467  7.802   1.00 13.56 ? 71  ASP A C    1 
ATOM   639  O  O    . ASP A 1 71  ? -17.701 12.320  8.208   1.00 14.20 ? 71  ASP A O    1 
ATOM   640  C  CB   . ASP A 1 71  ? -17.264 12.581  5.494   1.00 15.86 ? 71  ASP A CB   1 
ATOM   641  C  CG   . ASP A 1 71  ? -17.369 14.111  5.454   1.00 19.93 ? 71  ASP A CG   1 
ATOM   642  O  OD1  . ASP A 1 71  ? -16.708 14.778  6.243   1.00 17.48 ? 71  ASP A OD1  1 
ATOM   643  O  OD2  . ASP A 1 71  ? -18.124 14.576  4.547   1.00 30.82 ? 71  ASP A OD2  1 
ATOM   644  N  N    . ASP A 1 72  ? -15.601 13.005  8.540   1.00 10.75 ? 72  ASP A N    1 
ATOM   645  C  CA   . ASP A 1 72  ? -15.817 13.405  9.946   1.00 10.54 ? 72  ASP A CA   1 
ATOM   646  C  C    . ASP A 1 72  ? -15.829 14.936  10.069  1.00 14.46 ? 72  ASP A C    1 
ATOM   647  O  O    . ASP A 1 72  ? -15.453 15.426  11.148  1.00 13.80 ? 72  ASP A O    1 
ATOM   648  C  CB   . ASP A 1 72  ? -14.722 12.847  10.860  1.00 13.22 ? 72  ASP A CB   1 
ATOM   649  C  CG   . ASP A 1 72  ? -13.311 13.376  10.533  1.00 11.23 ? 72  ASP A CG   1 
ATOM   650  O  OD1  . ASP A 1 72  ? -13.044 14.004  9.457   1.00 13.14 ? 72  ASP A OD1  1 
ATOM   651  O  OD2  . ASP A 1 72  ? -12.402 13.115  11.326  1.00 15.55 ? 72  ASP A OD2  1 
ATOM   652  N  N    . SER A 1 73  ? -16.243 15.611  8.994   1.00 14.91 ? 73  SER A N    1 
ATOM   653  C  CA   . SER A 1 73  ? -16.257 17.117  9.017   1.00 15.73 ? 73  SER A CA   1 
ATOM   654  C  C    . SER A 1 73  ? -17.523 17.706  9.633   1.00 17.25 ? 73  SER A C    1 
ATOM   655  O  O    . SER A 1 73  ? -17.616 18.938  9.879   1.00 15.42 ? 73  SER A O    1 
ATOM   656  C  CB   . SER A 1 73  ? -15.965 17.708  7.666   1.00 16.27 ? 73  SER A CB   1 
ATOM   657  O  OG   . SER A 1 73  ? -17.009 17.481  6.782   1.00 15.37 ? 73  SER A OG   1 
ATOM   658  N  N    . GLN A 1 74  ? -18.495 16.838  9.912   1.00 17.52 ? 74  GLN A N    1 
ATOM   659  C  CA   . GLN A 1 74  ? -19.678 17.283  10.618  1.00 19.53 ? 74  GLN A CA   1 
ATOM   660  C  C    . GLN A 1 74  ? -19.997 16.311  11.704  1.00 18.81 ? 74  GLN A C    1 
ATOM   661  O  O    . GLN A 1 74  ? -19.445 15.208  11.756  1.00 15.77 ? 74  GLN A O    1 
ATOM   662  C  CB   . GLN A 1 74  ? -20.852 17.291  9.684   1.00 19.79 ? 74  GLN A CB   1 
ATOM   663  C  CG   . GLN A 1 74  ? -20.758 18.372  8.601   1.00 25.50 ? 74  GLN A CG   1 
ATOM   664  C  CD   . GLN A 1 74  ? -21.913 18.285  7.675   1.00 26.64 ? 74  GLN A CD   1 
ATOM   665  O  OE1  . GLN A 1 74  ? -23.060 18.387  8.113   1.00 35.86 ? 74  GLN A OE1  1 
ATOM   666  N  NE2  . GLN A 1 74  ? -21.646 18.125  6.391   1.00 29.85 ? 74  GLN A NE2  1 
ATOM   667  N  N    . ASP A 1 75  ? -20.983 16.713  12.504  1.00 19.37 ? 75  ASP A N    1 
ATOM   668  C  CA   . ASP A 1 75  ? -21.376 15.992  13.669  1.00 20.44 ? 75  ASP A CA   1 
ATOM   669  C  C    . ASP A 1 75  ? -22.315 14.823  13.243  1.00 19.66 ? 75  ASP A C    1 
ATOM   670  O  O    . ASP A 1 75  ? -23.571 14.947  13.300  1.00 21.80 ? 75  ASP A O    1 
ATOM   671  C  CB   . ASP A 1 75  ? -22.050 17.054  14.562  1.00 22.35 ? 75  ASP A CB   1 
ATOM   672  C  CG   . ASP A 1 75  ? -22.786 16.471  15.749  1.00 27.93 ? 75  ASP A CG   1 
ATOM   673  O  OD1  . ASP A 1 75  ? -22.443 15.338  16.180  1.00 27.48 ? 75  ASP A OD1  1 
ATOM   674  O  OD2  . ASP A 1 75  ? -23.724 17.181  16.237  1.00 31.58 ? 75  ASP A OD2  1 
ATOM   675  N  N    A LYS A 1 76  ? -21.745 13.713  12.779  0.50 18.12 ? 76  LYS A N    1 
ATOM   676  N  N    B LYS A 1 76  ? -21.722 13.721  12.823  0.50 16.94 ? 76  LYS A N    1 
ATOM   677  C  CA   A LYS A 1 76  ? -22.550 12.618  12.175  0.50 17.95 ? 76  LYS A CA   1 
ATOM   678  C  CA   B LYS A 1 76  ? -22.466 12.525  12.443  0.50 16.10 ? 76  LYS A CA   1 
ATOM   679  C  C    A LYS A 1 76  ? -22.478 11.318  12.985  0.50 17.17 ? 76  LYS A C    1 
ATOM   680  C  C    B LYS A 1 76  ? -21.628 11.343  12.964  0.50 13.82 ? 76  LYS A C    1 
ATOM   681  O  O    A LYS A 1 76  ? -23.238 11.177  13.965  0.50 18.74 ? 76  LYS A O    1 
ATOM   682  O  O    B LYS A 1 76  ? -20.410 11.493  13.165  0.50 12.49 ? 76  LYS A O    1 
ATOM   683  C  CB   A LYS A 1 76  ? -22.180 12.398  10.695  0.50 17.43 ? 76  LYS A CB   1 
ATOM   684  C  CB   B LYS A 1 76  ? -22.661 12.474  10.923  0.50 15.85 ? 76  LYS A CB   1 
ATOM   685  C  CG   A LYS A 1 76  ? -22.468 13.645  9.905   0.50 17.25 ? 76  LYS A CG   1 
ATOM   686  C  CG   B LYS A 1 76  ? -23.516 13.657  10.398  0.50 16.00 ? 76  LYS A CG   1 
ATOM   687  C  CD   A LYS A 1 76  ? -22.875 13.351  8.512   0.50 19.36 ? 76  LYS A CD   1 
ATOM   688  C  CD   B LYS A 1 76  ? -23.541 13.705  8.910   0.50 17.57 ? 76  LYS A CD   1 
ATOM   689  C  CE   A LYS A 1 76  ? -24.099 14.227  8.101   0.50 17.46 ? 76  LYS A CE   1 
ATOM   690  C  CE   B LYS A 1 76  ? -22.125 13.949  8.313   0.50 13.60 ? 76  LYS A CE   1 
ATOM   691  N  NZ   A LYS A 1 76  ? -23.938 14.578  6.678   0.50 14.99 ? 76  LYS A NZ   1 
ATOM   692  N  NZ   B LYS A 1 76  ? -22.118 14.200  6.796   0.50 16.84 ? 76  LYS A NZ   1 
ATOM   693  N  N    A ALA A 1 77  ? -21.570 10.417  12.595  0.50 15.59 ? 77  ALA A N    1 
ATOM   694  N  N    B ALA A 1 77  ? -22.288 10.226  13.243  0.50 12.72 ? 77  ALA A N    1 
ATOM   695  C  CA   A ALA A 1 77  ? -21.385 9.085   13.260  0.50 12.85 ? 77  ALA A CA   1 
ATOM   696  C  CA   B ALA A 1 77  ? -21.598 9.007   13.560  0.50 11.28 ? 77  ALA A CA   1 
ATOM   697  C  C    A ALA A 1 77  ? -20.680 9.163   14.644  0.50 12.41 ? 77  ALA A C    1 
ATOM   698  C  C    B ALA A 1 77  ? -20.836 9.420   14.820  0.50 11.38 ? 77  ALA A C    1 
ATOM   699  O  O    A ALA A 1 77  ? -19.472 9.091   14.735  0.50 11.82 ? 77  ALA A O    1 
ATOM   700  O  O    B ALA A 1 77  ? -19.710 10.008  14.755  0.50 11.62 ? 77  ALA A O    1 
ATOM   701  C  CB   A ALA A 1 77  ? -20.628 8.128   12.325  0.50 13.11 ? 77  ALA A CB   1 
ATOM   702  C  CB   B ALA A 1 77  ? -20.678 8.634   12.432  0.50 10.75 ? 77  ALA A CB   1 
ATOM   703  N  N    A VAL A 1 78  ? -21.424 9.364   15.714  0.50 9.92  ? 78  VAL A N    1 
ATOM   704  N  N    B VAL A 1 78  ? -21.521 9.181   15.926  0.50 10.37 ? 78  VAL A N    1 
ATOM   705  C  CA   A VAL A 1 78  ? -20.731 9.541   17.024  0.50 10.05 ? 78  VAL A CA   1 
ATOM   706  C  CA   B VAL A 1 78  ? -21.107 9.649   17.256  0.50 10.54 ? 78  VAL A CA   1 
ATOM   707  C  C    A VAL A 1 78  ? -20.960 8.388   18.012  0.50 10.18 ? 78  VAL A C    1 
ATOM   708  C  C    B VAL A 1 78  ? -21.162 8.504   18.274  0.50 10.47 ? 78  VAL A C    1 
ATOM   709  O  O    A VAL A 1 78  ? -21.926 7.629   17.898  0.50 8.80  ? 78  VAL A O    1 
ATOM   710  O  O    B VAL A 1 78  ? -22.211 7.843   18.423  0.50 8.91  ? 78  VAL A O    1 
ATOM   711  C  CB   A VAL A 1 78  ? -21.093 10.876  17.734  0.50 9.93  ? 78  VAL A CB   1 
ATOM   712  C  CB   B VAL A 1 78  ? -22.049 10.812  17.753  0.50 12.05 ? 78  VAL A CB   1 
ATOM   713  C  CG1  A VAL A 1 78  ? -20.559 12.098  16.990  0.50 9.72  ? 78  VAL A CG1  1 
ATOM   714  C  CG1  B VAL A 1 78  ? -21.834 11.127  19.203  0.50 11.46 ? 78  VAL A CG1  1 
ATOM   715  C  CG2  A VAL A 1 78  ? -22.593 10.921  18.042  0.50 12.29 ? 78  VAL A CG2  1 
ATOM   716  C  CG2  B VAL A 1 78  ? -21.844 12.068  16.927  0.50 12.92 ? 78  VAL A CG2  1 
ATOM   717  N  N    . LEU A 1 79  ? -20.043 8.311   18.977  1.00 8.88  ? 79  LEU A N    1 
ATOM   718  C  CA   . LEU A 1 79  ? -20.055 7.391   20.092  1.00 10.10 ? 79  LEU A CA   1 
ATOM   719  C  C    . LEU A 1 79  ? -20.042 8.264   21.330  1.00 11.08 ? 79  LEU A C    1 
ATOM   720  O  O    . LEU A 1 79  ? -19.213 9.190   21.462  1.00 11.75 ? 79  LEU A O    1 
ATOM   721  C  CB   . LEU A 1 79  ? -18.806 6.436   19.940  1.00 9.35  ? 79  LEU A CB   1 
ATOM   722  C  CG   . LEU A 1 79  ? -18.681 5.425   21.050  1.00 9.71  ? 79  LEU A CG   1 
ATOM   723  C  CD1  . LEU A 1 79  ? -19.741 4.371   20.996  1.00 15.21 ? 79  LEU A CD1  1 
ATOM   724  C  CD2  . LEU A 1 79  ? -17.285 4.756   21.009  1.00 9.46  ? 79  LEU A CD2  1 
ATOM   725  N  N    . LYS A 1 80  ? -20.902 7.928   22.300  1.00 9.77  ? 80  LYS A N    1 
ATOM   726  C  CA   . LYS A 1 80  ? -20.920 8.623   23.561  1.00 10.49 ? 80  LYS A CA   1 
ATOM   727  C  C    . LYS A 1 80  ? -21.510 7.688   24.623  1.00 9.69  ? 80  LYS A C    1 
ATOM   728  O  O    . LYS A 1 80  ? -21.871 6.547   24.323  1.00 9.61  ? 80  LYS A O    1 
ATOM   729  C  CB   . LYS A 1 80  ? -21.729 9.947   23.426  1.00 13.77 ? 80  LYS A CB   1 
ATOM   730  C  CG   . LYS A 1 80  ? -23.173 9.768   23.174  1.00 15.72 ? 80  LYS A CG   1 
ATOM   731  C  CD   . LYS A 1 80  ? -23.769 11.190  22.946  1.00 20.73 ? 80  LYS A CD   1 
ATOM   732  C  CE   . LYS A 1 80  ? -25.332 11.171  22.766  1.00 29.22 ? 80  LYS A CE   1 
ATOM   733  N  NZ   . LYS A 1 80  ? -26.019 11.282  24.104  1.00 35.87 ? 80  LYS A NZ   1 
ATOM   734  N  N    . GLY A 1 81  ? -21.651 8.192   25.835  1.00 9.95  ? 81  GLY A N    1 
ATOM   735  C  CA   . GLY A 1 81  ? -22.202 7.404   26.935  1.00 12.76 ? 81  GLY A CA   1 
ATOM   736  C  C    . GLY A 1 81  ? -21.199 6.318   27.232  1.00 13.85 ? 81  GLY A C    1 
ATOM   737  O  O    . GLY A 1 81  ? -19.986 6.507   27.010  1.00 12.61 ? 81  GLY A O    1 
ATOM   738  N  N    . GLY A 1 82  ? -21.680 5.179   27.697  1.00 15.28 ? 82  GLY A N    1 
ATOM   739  C  CA   . GLY A 1 82  ? -20.710 4.182   28.164  1.00 15.89 ? 82  GLY A CA   1 
ATOM   740  C  C    . GLY A 1 82  ? -19.832 4.797   29.251  1.00 14.75 ? 82  GLY A C    1 
ATOM   741  O  O    . GLY A 1 82  ? -20.273 5.515   30.177  1.00 16.52 ? 82  GLY A O    1 
ATOM   742  N  N    . PRO A 1 83  ? -18.477 4.599   29.134  1.00 12.16 ? 83  PRO A N    1 
ATOM   743  C  CA   . PRO A 1 83  ? -17.579 5.218   30.056  1.00 12.07 ? 83  PRO A CA   1 
ATOM   744  C  C    . PRO A 1 83  ? -17.138 6.637   29.667  1.00 12.34 ? 83  PRO A C    1 
ATOM   745  O  O    . PRO A 1 83  ? -16.341 7.266   30.379  1.00 13.93 ? 83  PRO A O    1 
ATOM   746  C  CB   . PRO A 1 83  ? -16.315 4.318   29.888  1.00 13.57 ? 83  PRO A CB   1 
ATOM   747  C  CG   . PRO A 1 83  ? -16.349 3.943   28.459  1.00 10.32 ? 83  PRO A CG   1 
ATOM   748  C  CD   . PRO A 1 83  ? -17.771 3.727   28.121  1.00 10.67 ? 83  PRO A CD   1 
ATOM   749  N  N    . LEU A 1 84  ? -17.667 7.150   28.578  1.00 11.36 ? 84  LEU A N    1 
ATOM   750  C  CA   . LEU A 1 84  ? -17.110 8.396   27.973  1.00 11.51 ? 84  LEU A CA   1 
ATOM   751  C  C    . LEU A 1 84  ? -17.808 9.663   28.519  1.00 13.82 ? 84  LEU A C    1 
ATOM   752  O  O    . LEU A 1 84  ? -19.004 9.652   28.794  1.00 13.09 ? 84  LEU A O    1 
ATOM   753  C  CB   . LEU A 1 84  ? -17.233 8.383   26.509  1.00 10.09 ? 84  LEU A CB   1 
ATOM   754  C  CG   . LEU A 1 84  ? -16.754 7.113   25.787  1.00 8.79  ? 84  LEU A CG   1 
ATOM   755  C  CD1  . LEU A 1 84  ? -17.331 6.972   24.333  1.00 9.35  ? 84  LEU A CD1  1 
ATOM   756  C  CD2  . LEU A 1 84  ? -15.134 7.084   25.858  1.00 8.91  ? 84  LEU A CD2  1 
ATOM   757  N  N    . ASP A 1 85  ? -17.017 10.710  28.620  1.00 15.04 ? 85  ASP A N    1 
ATOM   758  C  CA   . ASP A 1 85  ? -17.510 12.043  28.891  1.00 18.23 ? 85  ASP A CA   1 
ATOM   759  C  C    . ASP A 1 85  ? -17.503 12.648  27.521  1.00 18.29 ? 85  ASP A C    1 
ATOM   760  O  O    . ASP A 1 85  ? -16.525 12.566  26.760  1.00 20.40 ? 85  ASP A O    1 
ATOM   761  C  CB   . ASP A 1 85  ? -16.538 12.798  29.827  1.00 18.98 ? 85  ASP A CB   1 
ATOM   762  C  CG   . ASP A 1 85  ? -16.603 12.300  31.203  1.00 28.58 ? 85  ASP A CG   1 
ATOM   763  O  OD1  . ASP A 1 85  ? -17.734 11.861  31.567  1.00 31.84 ? 85  ASP A OD1  1 
ATOM   764  O  OD2  . ASP A 1 85  ? -15.546 12.339  31.915  1.00 33.73 ? 85  ASP A OD2  1 
ATOM   765  N  N    . GLY A 1 86  ? -18.546 13.364  27.177  1.00 20.75 ? 86  GLY A N    1 
ATOM   766  C  CA   . GLY A 1 86  ? -18.482 13.981  25.885  1.00 17.17 ? 86  GLY A CA   1 
ATOM   767  C  C    . GLY A 1 86  ? -18.696 13.040  24.671  1.00 16.51 ? 86  GLY A C    1 
ATOM   768  O  O    . GLY A 1 86  ? -19.163 11.912  24.789  1.00 18.13 ? 86  GLY A O    1 
ATOM   769  N  N    A THR A 1 87  ? -18.381 13.556  23.494  0.50 14.56 ? 87  THR A N    1 
ATOM   770  N  N    B THR A 1 87  ? -18.359 13.550  23.490  0.50 14.07 ? 87  THR A N    1 
ATOM   771  C  CA   A THR A 1 87  ? -18.818 12.941  22.256  0.50 12.30 ? 87  THR A CA   1 
ATOM   772  C  CA   B THR A 1 87  ? -18.774 12.922  22.238  0.50 11.35 ? 87  THR A CA   1 
ATOM   773  C  C    A THR A 1 87  ? -17.573 12.676  21.424  0.50 11.31 ? 87  THR A C    1 
ATOM   774  C  C    B THR A 1 87  ? -17.616 12.714  21.268  0.50 10.77 ? 87  THR A C    1 
ATOM   775  O  O    A THR A 1 87  ? -16.631 13.492  21.432  0.50 8.66  ? 87  THR A O    1 
ATOM   776  O  O    B THR A 1 87  ? -16.814 13.588  20.955  0.50 8.41  ? 87  THR A O    1 
ATOM   777  C  CB   A THR A 1 87  ? -19.804 13.894  21.478  0.50 14.47 ? 87  THR A CB   1 
ATOM   778  C  CB   B THR A 1 87  ? -19.783 13.780  21.454  0.50 13.29 ? 87  THR A CB   1 
ATOM   779  O  OG1  A THR A 1 87  ? -20.898 14.266  22.353  0.50 13.55 ? 87  THR A OG1  1 
ATOM   780  O  OG1  B THR A 1 87  ? -19.300 15.121  21.456  0.50 9.70  ? 87  THR A OG1  1 
ATOM   781  C  CG2  A THR A 1 87  ? -20.340 13.243  20.172  0.50 13.72 ? 87  THR A CG2  1 
ATOM   782  C  CG2  B THR A 1 87  ? -21.206 13.722  22.087  0.50 12.06 ? 87  THR A CG2  1 
ATOM   783  N  N    . TYR A 1 88  ? -17.567 11.506  20.766  1.00 9.08  ? 88  TYR A N    1 
ATOM   784  C  CA   . TYR A 1 88  ? -16.453 11.116  19.951  1.00 8.43  ? 88  TYR A CA   1 
ATOM   785  C  C    . TYR A 1 88  ? -16.926 10.791  18.565  1.00 8.60  ? 88  TYR A C    1 
ATOM   786  O  O    . TYR A 1 88  ? -17.927 10.061  18.401  1.00 11.37 ? 88  TYR A O    1 
ATOM   787  C  CB   . TYR A 1 88  ? -15.831 9.836   20.497  1.00 6.85  ? 88  TYR A CB   1 
ATOM   788  C  CG   . TYR A 1 88  ? -15.084 10.023  21.787  1.00 7.28  ? 88  TYR A CG   1 
ATOM   789  C  CD1  . TYR A 1 88  ? -15.787 10.360  22.977  1.00 7.89  ? 88  TYR A CD1  1 
ATOM   790  C  CD2  . TYR A 1 88  ? -13.657 9.867   21.818  1.00 7.41  ? 88  TYR A CD2  1 
ATOM   791  C  CE1  . TYR A 1 88  ? -15.088 10.553  24.207  1.00 7.04  ? 88  TYR A CE1  1 
ATOM   792  C  CE2  . TYR A 1 88  ? -12.981 10.059  23.040  1.00 7.81  ? 88  TYR A CE2  1 
ATOM   793  C  CZ   . TYR A 1 88  ? -13.671 10.347  24.220  1.00 8.92  ? 88  TYR A CZ   1 
ATOM   794  O  OH   . TYR A 1 88  ? -12.980 10.444  25.368  1.00 8.40  ? 88  TYR A OH   1 
ATOM   795  N  N    . ARG A 1 89  ? -16.183 11.273  17.580  1.00 7.64  ? 89  ARG A N    1 
ATOM   796  C  CA   . ARG A 1 89  ? -16.642 11.214  16.213  1.00 8.17  ? 89  ARG A CA   1 
ATOM   797  C  C    . ARG A 1 89  ? -15.968 10.070  15.411  1.00 6.80  ? 89  ARG A C    1 
ATOM   798  O  O    . ARG A 1 89  ? -14.752 9.958   15.451  1.00 7.83  ? 89  ARG A O    1 
ATOM   799  C  CB   . ARG A 1 89  ? -16.533 12.599  15.545  1.00 11.66 ? 89  ARG A CB   1 
ATOM   800  C  CG   . ARG A 1 89  ? -17.214 12.634  14.284  1.00 12.09 ? 89  ARG A CG   1 
ATOM   801  C  CD   . ARG A 1 89  ? -17.113 14.070  13.682  1.00 13.00 ? 89  ARG A CD   1 
ATOM   802  N  NE   . ARG A 1 89  ? -17.759 15.080  14.524  1.00 14.57 ? 89  ARG A NE   1 
ATOM   803  C  CZ   . ARG A 1 89  ? -17.648 16.402  14.289  1.00 16.32 ? 89  ARG A CZ   1 
ATOM   804  N  NH1  . ARG A 1 89  ? -16.916 16.870  13.261  1.00 13.85 ? 89  ARG A NH1  1 
ATOM   805  N  NH2  . ARG A 1 89  ? -18.262 17.275  15.071  1.00 15.64 ? 89  ARG A NH2  1 
ATOM   806  N  N    . LEU A 1 90  ? -16.761 9.232   14.704  1.00 7.82  ? 90  LEU A N    1 
ATOM   807  C  CA   . LEU A 1 90  ? -16.141 8.154   13.879  1.00 6.42  ? 90  LEU A CA   1 
ATOM   808  C  C    . LEU A 1 90  ? -15.303 8.720   12.746  1.00 5.90  ? 90  LEU A C    1 
ATOM   809  O  O    . LEU A 1 90  ? -15.789 9.605   11.971  1.00 7.97  ? 90  LEU A O    1 
ATOM   810  C  CB   . LEU A 1 90  ? -17.267 7.317   13.252  1.00 7.66  ? 90  LEU A CB   1 
ATOM   811  C  CG   . LEU A 1 90  ? -16.815 6.123   12.417  1.00 7.17  ? 90  LEU A CG   1 
ATOM   812  C  CD1  . LEU A 1 90  ? -16.051 5.040   13.213  1.00 10.19 ? 90  LEU A CD1  1 
ATOM   813  C  CD2  . LEU A 1 90  ? -18.036 5.449   11.775  1.00 8.83  ? 90  LEU A CD2  1 
ATOM   814  N  N    . ILE A 1 91  ? -14.083 8.221   12.620  1.00 5.49  ? 91  ILE A N    1 
ATOM   815  C  CA   . ILE A 1 91  ? -13.151 8.610   11.512  1.00 6.65  ? 91  ILE A CA   1 
ATOM   816  C  C    . ILE A 1 91  ? -12.811 7.432   10.596  1.00 7.35  ? 91  ILE A C    1 
ATOM   817  O  O    . ILE A 1 91  ? -12.790 7.580   9.371   1.00 8.15  ? 91  ILE A O    1 
ATOM   818  C  CB   . ILE A 1 91  ? -11.860 9.318   12.037  1.00 7.73  ? 91  ILE A CB   1 
ATOM   819  C  CG1  . ILE A 1 91  ? -10.937 9.613   10.843  1.00 8.11  ? 91  ILE A CG1  1 
ATOM   820  C  CG2  . ILE A 1 91  ? -11.207 8.515   13.126  1.00 7.44  ? 91  ILE A CG2  1 
ATOM   821  C  CD1  . ILE A 1 91  ? -9.794  10.608  11.229  1.00 10.63 ? 91  ILE A CD1  1 
ATOM   822  N  N    . GLN A 1 92  ? -12.652 6.212   11.186  1.00 6.80  ? 92  GLN A N    1 
ATOM   823  C  CA   . GLN A 1 92  ? -12.365 5.062   10.279  1.00 5.01  ? 92  GLN A CA   1 
ATOM   824  C  C    . GLN A 1 92  ? -12.629 3.806   11.074  1.00 5.62  ? 92  GLN A C    1 
ATOM   825  O  O    . GLN A 1 92  ? -12.684 3.817   12.302  1.00 6.39  ? 92  GLN A O    1 
ATOM   826  C  CB   . GLN A 1 92  ? -10.874 5.034   9.807   1.00 6.88  ? 92  GLN A CB   1 
ATOM   827  C  CG   . GLN A 1 92  ? -9.880  5.189   10.974  1.00 8.99  ? 92  GLN A CG   1 
ATOM   828  C  CD   . GLN A 1 92  ? -9.079  3.881   11.270  1.00 10.05 ? 92  GLN A CD   1 
ATOM   829  O  OE1  . GLN A 1 92  ? -9.622  2.781   11.114  1.00 8.43  ? 92  GLN A OE1  1 
ATOM   830  N  NE2  . GLN A 1 92  ? -7.805  4.045   11.570  1.00 11.00 ? 92  GLN A NE2  1 
ATOM   831  N  N    . PHE A 1 93  ? -12.731 2.710   10.326  1.00 5.43  ? 93  PHE A N    1 
ATOM   832  C  CA   . PHE A 1 93  ? -12.648 1.372   10.926  1.00 7.00  ? 93  PHE A CA   1 
ATOM   833  C  C    . PHE A 1 93  ? -11.703 0.490   10.162  1.00 6.92  ? 93  PHE A C    1 
ATOM   834  O  O    . PHE A 1 93  ? -11.485 0.684   9.014   1.00 7.70  ? 93  PHE A O    1 
ATOM   835  C  CB   . PHE A 1 93  ? -13.978 0.701   11.168  1.00 4.42  ? 93  PHE A CB   1 
ATOM   836  C  CG   . PHE A 1 93  ? -14.694 0.208   9.937   1.00 7.49  ? 93  PHE A CG   1 
ATOM   837  C  CD1  . PHE A 1 93  ? -14.284 -0.956  9.272   1.00 9.51  ? 93  PHE A CD1  1 
ATOM   838  C  CD2  . PHE A 1 93  ? -15.832 0.896   9.491   1.00 10.82 ? 93  PHE A CD2  1 
ATOM   839  C  CE1  . PHE A 1 93  ? -14.978 -1.440  8.138   1.00 10.25 ? 93  PHE A CE1  1 
ATOM   840  C  CE2  . PHE A 1 93  ? -16.549 0.415   8.409   1.00 9.77  ? 93  PHE A CE2  1 
ATOM   841  C  CZ   . PHE A 1 93  ? -16.091 -0.723  7.713   1.00 10.49 ? 93  PHE A CZ   1 
ATOM   842  N  N    . HIS A 1 94  ? -11.214 -0.576  10.818  1.00 5.50  ? 94  HIS A N    1 
ATOM   843  C  CA   . HIS A 1 94  ? -10.286 -1.508  10.183  1.00 5.38  ? 94  HIS A CA   1 
ATOM   844  C  C    . HIS A 1 94  ? -10.385 -2.789  11.025  1.00 6.25  ? 94  HIS A C    1 
ATOM   845  O  O    . HIS A 1 94  ? -11.046 -2.798  12.072  1.00 5.79  ? 94  HIS A O    1 
ATOM   846  C  CB   . HIS A 1 94  ? -8.857  -1.027  10.155  1.00 7.77  ? 94  HIS A CB   1 
ATOM   847  C  CG   . HIS A 1 94  ? -8.363  -0.732  11.543  1.00 6.29  ? 94  HIS A CG   1 
ATOM   848  N  ND1  . HIS A 1 94  ? -8.564  0.498   12.160  1.00 6.23  ? 94  HIS A ND1  1 
ATOM   849  C  CD2  . HIS A 1 94  ? -7.795  -1.526  12.467  1.00 7.09  ? 94  HIS A CD2  1 
ATOM   850  C  CE1  . HIS A 1 94  ? -8.059  0.451   13.391  1.00 4.55  ? 94  HIS A CE1  1 
ATOM   851  N  NE2  . HIS A 1 94  ? -7.561  -0.758  13.603  1.00 6.48  ? 94  HIS A NE2  1 
ATOM   852  N  N    . PHE A 1 95  ? -9.666  -3.821  10.560  1.00 4.04  ? 95  PHE A N    1 
ATOM   853  C  CA   . PHE A 1 95  ? -9.665  -5.128  11.230  1.00 5.04  ? 95  PHE A CA   1 
ATOM   854  C  C    . PHE A 1 95  ? -8.220  -5.522  11.449  1.00 4.92  ? 95  PHE A C    1 
ATOM   855  O  O    . PHE A 1 95  ? -7.295  -5.071  10.739  1.00 6.88  ? 95  PHE A O    1 
ATOM   856  C  CB   . PHE A 1 95  ? -10.356 -6.239  10.347  1.00 3.80  ? 95  PHE A CB   1 
ATOM   857  C  CG   . PHE A 1 95  ? -11.756 -5.925  10.057  1.00 4.22  ? 95  PHE A CG   1 
ATOM   858  C  CD1  . PHE A 1 95  ? -12.079 -5.079  8.968   1.00 7.42  ? 95  PHE A CD1  1 
ATOM   859  C  CD2  . PHE A 1 95  ? -12.790 -6.549  10.756  1.00 7.83  ? 95  PHE A CD2  1 
ATOM   860  C  CE1  . PHE A 1 95  ? -13.418 -4.848  8.668   1.00 4.27  ? 95  PHE A CE1  1 
ATOM   861  C  CE2  . PHE A 1 95  ? -14.144 -6.299  10.470  1.00 4.97  ? 95  PHE A CE2  1 
ATOM   862  C  CZ   . PHE A 1 95  ? -14.434 -5.458  9.372   1.00 5.14  ? 95  PHE A CZ   1 
ATOM   863  N  N    . HIS A 1 96  ? -8.111  -6.508  12.326  1.00 3.78  ? 96  HIS A N    1 
ATOM   864  C  CA   . HIS A 1 96  ? -6.861  -7.340  12.558  1.00 5.24  ? 96  HIS A CA   1 
ATOM   865  C  C    . HIS A 1 96  ? -7.273  -8.805  12.439  1.00 5.88  ? 96  HIS A C    1 
ATOM   866  O  O    . HIS A 1 96  ? -8.370  -9.159  12.901  1.00 7.15  ? 96  HIS A O    1 
ATOM   867  C  CB   . HIS A 1 96  ? -6.261  -7.082  13.933  1.00 7.52  ? 96  HIS A CB   1 
ATOM   868  C  CG   . HIS A 1 96  ? -5.987  -5.636  14.183  1.00 6.22  ? 96  HIS A CG   1 
ATOM   869  N  ND1  . HIS A 1 96  ? -4.719  -5.067  13.996  1.00 7.19  ? 96  HIS A ND1  1 
ATOM   870  C  CD2  . HIS A 1 96  ? -6.818  -4.637  14.582  1.00 7.67  ? 96  HIS A CD2  1 
ATOM   871  C  CE1  . HIS A 1 96  ? -4.790  -3.782  14.380  1.00 8.21  ? 96  HIS A CE1  1 
ATOM   872  N  NE2  . HIS A 1 96  ? -6.065  -3.492  14.644  1.00 6.93  ? 96  HIS A NE2  1 
ATOM   873  N  N    . TRP A 1 97  ? -6.510  -9.601  11.690  1.00 4.19  ? 97  TRP A N    1 
ATOM   874  C  CA   . TRP A 1 97  ? -6.907  -11.022 11.538  1.00 7.43  ? 97  TRP A CA   1 
ATOM   875  C  C    . TRP A 1 97  ? -5.706  -11.925 11.440  1.00 5.51  ? 97  TRP A C    1 
ATOM   876  O  O    . TRP A 1 97  ? -4.552  -11.480 11.297  1.00 6.39  ? 97  TRP A O    1 
ATOM   877  C  CB   . TRP A 1 97  ? -7.796  -11.202 10.334  1.00 7.02  ? 97  TRP A CB   1 
ATOM   878  C  CG   . TRP A 1 97  ? -7.150  -10.759 9.037   1.00 7.56  ? 97  TRP A CG   1 
ATOM   879  C  CD1  . TRP A 1 97  ? -6.444  -11.567 8.193   1.00 8.62  ? 97  TRP A CD1  1 
ATOM   880  C  CD2  . TRP A 1 97  ? -7.127  -9.427  8.454   1.00 8.88  ? 97  TRP A CD2  1 
ATOM   881  N  NE1  . TRP A 1 97  ? -6.031  -10.838 7.068   1.00 8.25  ? 97  TRP A NE1  1 
ATOM   882  C  CE2  . TRP A 1 97  ? -6.389  -9.516  7.234   1.00 8.06  ? 97  TRP A CE2  1 
ATOM   883  C  CE3  . TRP A 1 97  ? -7.622  -8.140  8.873   1.00 7.17  ? 97  TRP A CE3  1 
ATOM   884  C  CZ2  . TRP A 1 97  ? -6.216  -8.444  6.392   1.00 9.62  ? 97  TRP A CZ2  1 
ATOM   885  C  CZ3  . TRP A 1 97  ? -7.413  -7.004  7.986   1.00 8.16  ? 97  TRP A CZ3  1 
ATOM   886  C  CH2  . TRP A 1 97  ? -6.686  -7.191  6.771   1.00 7.54  ? 97  TRP A CH2  1 
ATOM   887  N  N    . GLY A 1 98  ? -6.049  -13.226 11.460  1.00 5.77  ? 98  GLY A N    1 
ATOM   888  C  CA   . GLY A 1 98  ? -5.088  -14.305 11.467  1.00 5.89  ? 98  GLY A CA   1 
ATOM   889  C  C    . GLY A 1 98  ? -4.807  -14.956 10.102  1.00 7.37  ? 98  GLY A C    1 
ATOM   890  O  O    . GLY A 1 98  ? -5.499  -14.765 9.108   1.00 6.96  ? 98  GLY A O    1 
ATOM   891  N  N    . SER A 1 99  ? -3.758  -15.785 10.121  1.00 5.63  ? 99  SER A N    1 
ATOM   892  C  CA   . SER A 1 99  ? -3.577  -16.714 9.011   1.00 8.67  ? 99  SER A CA   1 
ATOM   893  C  C    . SER A 1 99  ? -4.441  -17.966 9.123   1.00 9.35  ? 99  SER A C    1 
ATOM   894  O  O    . SER A 1 99  ? -4.527  -18.746 8.139   1.00 10.28 ? 99  SER A O    1 
ATOM   895  C  CB   . SER A 1 99  ? -2.085  -17.115 9.008   1.00 8.55  ? 99  SER A CB   1 
ATOM   896  O  OG   . SER A 1 99  ? -1.635  -17.706 10.183  1.00 10.28 ? 99  SER A OG   1 
ATOM   897  N  N    . LEU A 1 100 ? -4.999  -18.196 10.316  1.00 8.98  ? 100 LEU A N    1 
ATOM   898  C  CA   . LEU A 1 100 ? -5.787  -19.343 10.621  1.00 10.93 ? 100 LEU A CA   1 
ATOM   899  C  C    . LEU A 1 100 ? -6.988  -18.889 11.450  1.00 9.29  ? 100 LEU A C    1 
ATOM   900  O  O    . LEU A 1 100 ? -6.911  -17.903 12.160  1.00 8.85  ? 100 LEU A O    1 
ATOM   901  C  CB   . LEU A 1 100 ? -4.923  -20.265 11.498  1.00 12.98 ? 100 LEU A CB   1 
ATOM   902  C  CG   . LEU A 1 100 ? -3.587  -20.652 10.886  1.00 15.94 ? 100 LEU A CG   1 
ATOM   903  C  CD1  . LEU A 1 100 ? -2.709  -21.143 11.966  1.00 22.79 ? 100 LEU A CD1  1 
ATOM   904  C  CD2  . LEU A 1 100 ? -3.927  -21.763 9.904   1.00 16.59 ? 100 LEU A CD2  1 
ATOM   905  N  N    . ASP A 1 101 ? -8.051  -19.663 11.499  1.00 7.80  ? 101 ASP A N    1 
ATOM   906  C  CA   . ASP A 1 101 ? -9.192  -19.126 12.299  1.00 7.90  ? 101 ASP A CA   1 
ATOM   907  C  C    . ASP A 1 101 ? -8.964  -19.091 13.786  1.00 8.49  ? 101 ASP A C    1 
ATOM   908  O  O    . ASP A 1 101 ? -9.680  -18.394 14.475  1.00 11.47 ? 101 ASP A O    1 
ATOM   909  C  CB   . ASP A 1 101 ? -10.428 -19.951 12.066  1.00 9.11  ? 101 ASP A CB   1 
ATOM   910  C  CG   . ASP A 1 101 ? -10.842 -20.035 10.623  1.00 12.26 ? 101 ASP A CG   1 
ATOM   911  O  OD1  . ASP A 1 101 ? -10.537 -19.222 9.699   1.00 11.60 ? 101 ASP A OD1  1 
ATOM   912  O  OD2  . ASP A 1 101 ? -11.597 -20.992 10.408  1.00 19.48 ? 101 ASP A OD2  1 
ATOM   913  N  N    . GLY A 1 102 ? -7.974  -19.903 14.286  1.00 9.49  ? 102 GLY A N    1 
ATOM   914  C  CA   . GLY A 1 102 ? -7.640  -19.912 15.693  1.00 7.97  ? 102 GLY A CA   1 
ATOM   915  C  C    . GLY A 1 102 ? -6.879  -18.715 16.245  1.00 6.57  ? 102 GLY A C    1 
ATOM   916  O  O    . GLY A 1 102 ? -6.567  -18.674 17.451  1.00 8.15  ? 102 GLY A O    1 
ATOM   917  N  N    . GLN A 1 103 ? -6.640  -17.702 15.393  1.00 6.67  ? 103 GLN A N    1 
ATOM   918  C  CA   . GLN A 1 103 ? -5.944  -16.513 15.946  1.00 5.86  ? 103 GLN A CA   1 
ATOM   919  C  C    . GLN A 1 103 ? -6.300  -15.344 15.067  1.00 6.75  ? 103 GLN A C    1 
ATOM   920  O  O    . GLN A 1 103 ? -6.815  -15.535 13.972  1.00 6.94  ? 103 GLN A O    1 
ATOM   921  C  CB   . GLN A 1 103 ? -4.406  -16.709 15.930  1.00 8.16  ? 103 GLN A CB   1 
ATOM   922  C  CG   . GLN A 1 103 ? -3.838  -16.949 14.535  1.00 9.31  ? 103 GLN A CG   1 
ATOM   923  C  CD   . GLN A 1 103 ? -2.404  -17.456 14.616  1.00 13.47 ? 103 GLN A CD   1 
ATOM   924  O  OE1  . GLN A 1 103 ? -2.102  -18.336 15.420  1.00 19.86 ? 103 GLN A OE1  1 
ATOM   925  N  NE2  . GLN A 1 103 ? -1.551  -16.981 13.733  1.00 13.22 ? 103 GLN A NE2  1 
ATOM   926  N  N    . GLY A 1 104 ? -5.978  -14.151 15.560  1.00 7.10  ? 104 GLY A N    1 
ATOM   927  C  CA   . GLY A 1 104 ? -6.225  -12.949 14.742  1.00 6.32  ? 104 GLY A CA   1 
ATOM   928  C  C    . GLY A 1 104 ? -6.655  -11.775 15.590  1.00 6.48  ? 104 GLY A C    1 
ATOM   929  O  O    . GLY A 1 104 ? -6.442  -10.600 15.186  1.00 6.73  ? 104 GLY A O    1 
ATOM   930  N  N    . SER A 1 105 ? -7.362  -12.049 16.683  1.00 4.21  ? 105 SER A N    1 
ATOM   931  C  CA   . SER A 1 105 ? -7.794  -10.861 17.480  1.00 5.57  ? 105 SER A CA   1 
ATOM   932  C  C    . SER A 1 105 ? -6.584  -10.297 18.242  1.00 4.94  ? 105 SER A C    1 
ATOM   933  O  O    . SER A 1 105 ? -5.543  -11.000 18.426  1.00 6.52  ? 105 SER A O    1 
ATOM   934  C  CB   . SER A 1 105 ? -8.939  -11.181 18.441  1.00 5.68  ? 105 SER A CB   1 
ATOM   935  O  OG   . SER A 1 105 ? -8.566  -12.181 19.410  1.00 5.54  ? 105 SER A OG   1 
ATOM   936  N  N    . GLU A 1 106 ? -6.745  -9.051  18.654  1.00 5.67  ? 106 GLU A N    1 
ATOM   937  C  CA   . GLU A 1 106 ? -5.673  -8.347  19.448  1.00 5.03  ? 106 GLU A CA   1 
ATOM   938  C  C    . GLU A 1 106 ? -6.079  -8.547  20.950  1.00 5.84  ? 106 GLU A C    1 
ATOM   939  O  O    . GLU A 1 106 ? -5.379  -9.153  21.705  1.00 6.08  ? 106 GLU A O    1 
ATOM   940  C  CB   . GLU A 1 106 ? -5.695  -6.865  19.089  1.00 2.56  ? 106 GLU A CB   1 
ATOM   941  C  CG   . GLU A 1 106 ? -5.240  -6.765  17.593  1.00 8.14  ? 106 GLU A CG   1 
ATOM   942  C  CD   . GLU A 1 106 ? -4.571  -5.447  17.233  1.00 9.16  ? 106 GLU A CD   1 
ATOM   943  O  OE1  . GLU A 1 106 ? -5.131  -4.387  17.540  1.00 6.33  ? 106 GLU A OE1  1 
ATOM   944  O  OE2  . GLU A 1 106 ? -3.369  -5.532  16.824  1.00 7.07  ? 106 GLU A OE2  1 
ATOM   945  N  N    . HIS A 1 107 ? -7.306  -8.118  21.346  1.00 4.75  ? 107 HIS A N    1 
ATOM   946  C  CA   . HIS A 1 107 ? -7.712  -8.444  22.691  1.00 4.46  ? 107 HIS A CA   1 
ATOM   947  C  C    . HIS A 1 107 ? -8.035  -9.923  22.711  1.00 4.76  ? 107 HIS A C    1 
ATOM   948  O  O    . HIS A 1 107 ? -8.334  -10.512 21.663  1.00 5.20  ? 107 HIS A O    1 
ATOM   949  C  CB   . HIS A 1 107 ? -8.975  -7.648  23.046  1.00 4.70  ? 107 HIS A CB   1 
ATOM   950  C  CG   . HIS A 1 107 ? -8.674  -6.185  23.220  1.00 3.62  ? 107 HIS A CG   1 
ATOM   951  N  ND1  . HIS A 1 107 ? -8.633  -5.319  22.156  1.00 4.36  ? 107 HIS A ND1  1 
ATOM   952  C  CD2  . HIS A 1 107 ? -8.256  -5.484  24.299  1.00 6.91  ? 107 HIS A CD2  1 
ATOM   953  C  CE1  . HIS A 1 107 ? -8.247  -4.108  22.580  1.00 6.19  ? 107 HIS A CE1  1 
ATOM   954  N  NE2  . HIS A 1 107 ? -8.041  -4.182  23.877  1.00 4.95  ? 107 HIS A NE2  1 
ATOM   955  N  N    . THR A 1 108 ? -7.852  -10.502 23.896  1.00 5.33  ? 108 THR A N    1 
ATOM   956  C  CA   . THR A 1 108 ? -8.276  -11.899 24.160  1.00 4.36  ? 108 THR A CA   1 
ATOM   957  C  C    . THR A 1 108 ? -9.202  -11.939 25.366  1.00 6.39  ? 108 THR A C    1 
ATOM   958  O  O    . THR A 1 108 ? -9.324  -10.969 26.137  1.00 7.81  ? 108 THR A O    1 
ATOM   959  C  CB   . THR A 1 108 ? -7.053  -12.774 24.321  1.00 4.20  ? 108 THR A CB   1 
ATOM   960  O  OG1  . THR A 1 108 ? -6.250  -12.320 25.425  1.00 6.52  ? 108 THR A OG1  1 
ATOM   961  C  CG2  . THR A 1 108 ? -6.223  -12.786 23.010  1.00 5.68  ? 108 THR A CG2  1 
ATOM   962  N  N    . VAL A 1 109 ? -9.987  -13.007 25.443  1.00 6.80  ? 109 VAL A N    1 
ATOM   963  C  CA   . VAL A 1 109 ? -11.004 -13.101 26.577  1.00 6.20  ? 109 VAL A CA   1 
ATOM   964  C  C    . VAL A 1 109 ? -10.656 -14.393 27.295  1.00 7.83  ? 109 VAL A C    1 
ATOM   965  O  O    . VAL A 1 109 ? -10.840 -15.482 26.750  1.00 6.70  ? 109 VAL A O    1 
ATOM   966  C  CB   . VAL A 1 109 ? -12.415 -13.175 26.041  1.00 8.63  ? 109 VAL A CB   1 
ATOM   967  C  CG1  . VAL A 1 109 ? -13.466 -13.332 27.216  1.00 7.66  ? 109 VAL A CG1  1 
ATOM   968  C  CG2  . VAL A 1 109 ? -12.748 -11.837 25.208  1.00 7.47  ? 109 VAL A CG2  1 
ATOM   969  N  N    . ASP A 1 110 ? -10.178 -14.255 28.513  1.00 7.41  ? 110 ASP A N    1 
ATOM   970  C  CA   . ASP A 1 110 ? -9.651  -15.437 29.275  1.00 9.77  ? 110 ASP A CA   1 
ATOM   971  C  C    . ASP A 1 110 ? -8.716  -16.255 28.364  1.00 8.02  ? 110 ASP A C    1 
ATOM   972  O  O    . ASP A 1 110 ? -8.816  -17.522 28.302  1.00 10.47 ? 110 ASP A O    1 
ATOM   973  C  CB   . ASP A 1 110 ? -10.876 -16.273 29.759  1.00 10.29 ? 110 ASP A CB   1 
ATOM   974  C  CG   . ASP A 1 110 ? -11.734 -15.460 30.837  1.00 5.68  ? 110 ASP A CG   1 
ATOM   975  O  OD1  . ASP A 1 110 ? -11.067 -14.636 31.497  1.00 11.50 ? 110 ASP A OD1  1 
ATOM   976  O  OD2  . ASP A 1 110 ? -12.912 -15.785 30.963  1.00 14.75 ? 110 ASP A OD2  1 
ATOM   977  N  N    . LYS A 1 111 ? -7.819  -15.523 27.628  1.00 7.76  ? 111 LYS A N    1 
ATOM   978  C  CA   . LYS A 1 111 ? -6.767  -16.075 26.700  1.00 7.37  ? 111 LYS A CA   1 
ATOM   979  C  C    . LYS A 1 111 ? -7.322  -16.599 25.383  1.00 7.04  ? 111 LYS A C    1 
ATOM   980  O  O    . LYS A 1 111 ? -6.548  -16.982 24.498  1.00 7.93  ? 111 LYS A O    1 
ATOM   981  C  CB   . LYS A 1 111 ? -5.895  -17.139 27.448  1.00 8.43  ? 111 LYS A CB   1 
ATOM   982  C  CG   . LYS A 1 111 ? -5.193  -16.521 28.701  1.00 10.11 ? 111 LYS A CG   1 
ATOM   983  C  CD   . LYS A 1 111 ? -4.251  -15.406 28.189  1.00 15.65 ? 111 LYS A CD   1 
ATOM   984  C  CE   . LYS A 1 111 ? -3.363  -14.768 29.399  1.00 14.52 ? 111 LYS A CE   1 
ATOM   985  N  NZ   . LYS A 1 111 ? -2.260  -15.638 29.605  1.00 18.72 ? 111 LYS A NZ   1 
ATOM   986  N  N    . LYS A 1 112 ? -8.658  -16.573 25.208  1.00 4.76  ? 112 LYS A N    1 
ATOM   987  C  CA   . LYS A 1 112 ? -9.274  -17.021 23.970  1.00 6.29  ? 112 LYS A CA   1 
ATOM   988  C  C    . LYS A 1 112 ? -8.939  -15.945 22.886  1.00 8.22  ? 112 LYS A C    1 
ATOM   989  O  O    . LYS A 1 112 ? -9.185  -14.732 23.105  1.00 7.08  ? 112 LYS A O    1 
ATOM   990  C  CB   . LYS A 1 112 ? -10.833 -17.054 24.086  1.00 6.61  ? 112 LYS A CB   1 
ATOM   991  C  CG   . LYS A 1 112 ? -11.426 -17.408 22.696  1.00 7.55  ? 112 LYS A CG   1 
ATOM   992  C  CD   . LYS A 1 112 ? -12.953 -17.333 22.848  1.00 7.49  ? 112 LYS A CD   1 
ATOM   993  C  CE   . LYS A 1 112 ? -13.551 -17.530 21.436  1.00 14.26 ? 112 LYS A CE   1 
ATOM   994  N  NZ   . LYS A 1 112 ? -13.447 -18.970 21.052  1.00 9.28  ? 112 LYS A NZ   1 
ATOM   995  N  N    . LYS A 1 113 ? -8.429  -16.428 21.744  1.00 7.06  ? 113 LYS A N    1 
ATOM   996  C  CA   . LYS A 1 113 ? -8.196  -15.603 20.541  1.00 8.53  ? 113 LYS A CA   1 
ATOM   997  C  C    . LYS A 1 113 ? -9.311  -15.817 19.564  1.00 8.76  ? 113 LYS A C    1 
ATOM   998  O  O    . LYS A 1 113 ? -9.673  -16.995 19.279  1.00 7.53  ? 113 LYS A O    1 
ATOM   999  C  CB   . LYS A 1 113 ? -6.845  -16.022 19.902  1.00 8.29  ? 113 LYS A CB   1 
ATOM   1000 C  CG   . LYS A 1 113 ? -5.666  -15.645 20.731  1.00 8.94  ? 113 LYS A CG   1 
ATOM   1001 C  CD   . LYS A 1 113 ? -4.438  -16.262 19.994  1.00 10.53 ? 113 LYS A CD   1 
ATOM   1002 C  CE   . LYS A 1 113 ? -3.128  -15.704 20.588  1.00 14.02 ? 113 LYS A CE   1 
ATOM   1003 N  NZ   . LYS A 1 113 ? -2.783  -16.564 21.745  1.00 21.44 ? 113 LYS A NZ   1 
ATOM   1004 N  N    . TYR A 1 114 ? -9.931  -14.715 19.089  1.00 8.19  ? 114 TYR A N    1 
ATOM   1005 C  CA   . TYR A 1 114 ? -10.893 -14.844 18.068  1.00 6.43  ? 114 TYR A CA   1 
ATOM   1006 C  C    . TYR A 1 114 ? -10.264 -14.789 16.677  1.00 6.28  ? 114 TYR A C    1 
ATOM   1007 O  O    . TYR A 1 114 ? -9.063  -14.487 16.574  1.00 5.83  ? 114 TYR A O    1 
ATOM   1008 C  CB   . TYR A 1 114 ? -11.954 -13.716 18.189  1.00 7.23  ? 114 TYR A CB   1 
ATOM   1009 C  CG   . TYR A 1 114 ? -12.909 -13.934 19.333  1.00 3.92  ? 114 TYR A CG   1 
ATOM   1010 C  CD1  . TYR A 1 114 ? -12.577 -13.526 20.660  1.00 5.90  ? 114 TYR A CD1  1 
ATOM   1011 C  CD2  . TYR A 1 114 ? -14.171 -14.528 19.081  1.00 8.02  ? 114 TYR A CD2  1 
ATOM   1012 C  CE1  . TYR A 1 114 ? -13.479 -13.712 21.714  1.00 8.46  ? 114 TYR A CE1  1 
ATOM   1013 C  CE2  . TYR A 1 114 ? -15.118 -14.684 20.116  1.00 7.79  ? 114 TYR A CE2  1 
ATOM   1014 C  CZ   . TYR A 1 114 ? -14.735 -14.268 21.447  1.00 8.17  ? 114 TYR A CZ   1 
ATOM   1015 O  OH   . TYR A 1 114 ? -15.598 -14.450 22.537  1.00 13.04 ? 114 TYR A OH   1 
ATOM   1016 N  N    . ALA A 1 115 ? -11.034 -15.065 15.610  1.00 6.55  ? 115 ALA A N    1 
ATOM   1017 C  CA   . ALA A 1 115 ? -10.472 -15.139 14.262  1.00 7.25  ? 115 ALA A CA   1 
ATOM   1018 C  C    . ALA A 1 115 ? -10.017 -13.717 13.753  1.00 7.16  ? 115 ALA A C    1 
ATOM   1019 O  O    . ALA A 1 115 ? -9.135  -13.557 12.896  1.00 7.64  ? 115 ALA A O    1 
ATOM   1020 C  CB   . ALA A 1 115 ? -11.544 -15.768 13.304  1.00 8.70  ? 115 ALA A CB   1 
ATOM   1021 N  N    . ALA A 1 116 ? -10.663 -12.707 14.348  1.00 6.39  ? 116 ALA A N    1 
ATOM   1022 C  CA   . ALA A 1 116 ? -10.372 -11.318 13.926  1.00 5.08  ? 116 ALA A CA   1 
ATOM   1023 C  C    . ALA A 1 116 ? -11.001 -10.346 14.870  1.00 6.29  ? 116 ALA A C    1 
ATOM   1024 O  O    . ALA A 1 116 ? -11.721 -10.733 15.801  1.00 5.12  ? 116 ALA A O    1 
ATOM   1025 C  CB   . ALA A 1 116 ? -10.879 -11.048 12.461  1.00 7.10  ? 116 ALA A CB   1 
ATOM   1026 N  N    . GLU A 1 117 ? -10.603 -9.078  14.729  1.00 5.90  ? 117 GLU A N    1 
ATOM   1027 C  CA   . GLU A 1 117 ? -11.146 -8.053  15.581  1.00 5.71  ? 117 GLU A CA   1 
ATOM   1028 C  C    . GLU A 1 117 ? -11.341 -6.742  14.810  1.00 7.09  ? 117 GLU A C    1 
ATOM   1029 O  O    . GLU A 1 117 ? -10.471 -6.344  14.066  1.00 5.48  ? 117 GLU A O    1 
ATOM   1030 C  CB   . GLU A 1 117 ? -10.180 -7.781  16.726  1.00 6.70  ? 117 GLU A CB   1 
ATOM   1031 C  CG   . GLU A 1 117 ? -10.773 -6.801  17.800  1.00 5.05  ? 117 GLU A CG   1 
ATOM   1032 C  CD   . GLU A 1 117 ? -9.878  -6.729  18.997  1.00 6.22  ? 117 GLU A CD   1 
ATOM   1033 O  OE1  . GLU A 1 117 ? -9.182  -7.756  19.367  1.00 6.30  ? 117 GLU A OE1  1 
ATOM   1034 O  OE2  . GLU A 1 117 ? -9.891  -5.673  19.723  1.00 6.84  ? 117 GLU A OE2  1 
ATOM   1035 N  N    . LEU A 1 118 ? -12.514 -6.181  14.956  1.00 4.25  ? 118 LEU A N    1 
ATOM   1036 C  CA   . LEU A 1 118 ? -12.906 -4.921  14.246  1.00 3.14  ? 118 LEU A CA   1 
ATOM   1037 C  C    . LEU A 1 118 ? -12.719 -3.712  15.196  1.00 3.33  ? 118 LEU A C    1 
ATOM   1038 O  O    . LEU A 1 118 ? -13.092 -3.821  16.392  1.00 3.84  ? 118 LEU A O    1 
ATOM   1039 C  CB   . LEU A 1 118 ? -14.411 -4.989  13.883  1.00 3.27  ? 118 LEU A CB   1 
ATOM   1040 C  CG   . LEU A 1 118 ? -15.130 -3.651  13.544  1.00 5.32  ? 118 LEU A CG   1 
ATOM   1041 C  CD1  . LEU A 1 118 ? -14.476 -3.130  12.226  1.00 6.50  ? 118 LEU A CD1  1 
ATOM   1042 C  CD2  . LEU A 1 118 ? -16.614 -4.036  13.330  1.00 5.49  ? 118 LEU A CD2  1 
ATOM   1043 N  N    . HIS A 1 119 ? -12.050 -2.655  14.705  1.00 3.47  ? 119 HIS A N    1 
ATOM   1044 C  CA   . HIS A 1 119 ? -11.839 -1.460  15.512  1.00 2.94  ? 119 HIS A CA   1 
ATOM   1045 C  C    . HIS A 1 119 ? -12.508 -0.287  14.869  1.00 5.35  ? 119 HIS A C    1 
ATOM   1046 O  O    . HIS A 1 119 ? -12.152 0.014   13.687  1.00 5.37  ? 119 HIS A O    1 
ATOM   1047 C  CB   . HIS A 1 119 ? -10.342 -1.236  15.552  1.00 3.91  ? 119 HIS A CB   1 
ATOM   1048 C  CG   . HIS A 1 119 ? -9.710  -2.214  16.502  1.00 3.01  ? 119 HIS A CG   1 
ATOM   1049 N  ND1  . HIS A 1 119 ? -8.369  -2.491  16.468  1.00 4.40  ? 119 HIS A ND1  1 
ATOM   1050 C  CD2  . HIS A 1 119 ? -10.245 -3.027  17.446  1.00 2.81  ? 119 HIS A CD2  1 
ATOM   1051 C  CE1  . HIS A 1 119 ? -8.072  -3.386  17.385  1.00 3.54  ? 119 HIS A CE1  1 
ATOM   1052 N  NE2  . HIS A 1 119 ? -9.192  -3.719  18.009  1.00 4.02  ? 119 HIS A NE2  1 
ATOM   1053 N  N    . LEU A 1 120 ? -13.547 0.267   15.516  1.00 4.85  ? 120 LEU A N    1 
ATOM   1054 C  CA   . LEU A 1 120 ? -14.216 1.516   15.024  1.00 5.17  ? 120 LEU A CA   1 
ATOM   1055 C  C    . LEU A 1 120 ? -13.629 2.653   15.806  1.00 3.92  ? 120 LEU A C    1 
ATOM   1056 O  O    . LEU A 1 120 ? -13.730 2.696   17.057  1.00 3.94  ? 120 LEU A O    1 
ATOM   1057 C  CB   . LEU A 1 120 ? -15.728 1.480   15.278  1.00 3.65  ? 120 LEU A CB   1 
ATOM   1058 C  CG   . LEU A 1 120 ? -16.319 0.341   14.379  1.00 6.05  ? 120 LEU A CG   1 
ATOM   1059 C  CD1  . LEU A 1 120 ? -17.197 -0.536  15.155  1.00 10.77 ? 120 LEU A CD1  1 
ATOM   1060 C  CD2  . LEU A 1 120 ? -17.119 1.008   13.203  1.00 8.77  ? 120 LEU A CD2  1 
ATOM   1061 N  N    . VAL A 1 121 ? -12.932 3.509   15.058  1.00 4.61  ? 121 VAL A N    1 
ATOM   1062 C  CA   . VAL A 1 121 ? -12.071 4.530   15.773  1.00 3.88  ? 121 VAL A CA   1 
ATOM   1063 C  C    . VAL A 1 121 ? -12.777 5.861   15.808  1.00 5.46  ? 121 VAL A C    1 
ATOM   1064 O  O    . VAL A 1 121 ? -13.108 6.365   14.734  1.00 5.64  ? 121 VAL A O    1 
ATOM   1065 C  CB   . VAL A 1 121 ? -10.776 4.677   14.923  1.00 5.16  ? 121 VAL A CB   1 
ATOM   1066 C  CG1  . VAL A 1 121 ? -9.677  5.624   15.606  1.00 4.96  ? 121 VAL A CG1  1 
ATOM   1067 C  CG2  . VAL A 1 121 ? -10.024 3.287   14.658  1.00 4.97  ? 121 VAL A CG2  1 
ATOM   1068 N  N    . HIS A 1 122 ? -12.796 6.503   16.990  1.00 4.88  ? 122 HIS A N    1 
ATOM   1069 C  CA   . HIS A 1 122 ? -13.528 7.766   17.167  1.00 4.59  ? 122 HIS A CA   1 
ATOM   1070 C  C    . HIS A 1 122 ? -12.637 8.749   17.881  1.00 6.58  ? 122 HIS A C    1 
ATOM   1071 O  O    . HIS A 1 122 ? -11.890 8.374   18.756  1.00 5.52  ? 122 HIS A O    1 
ATOM   1072 C  CB   . HIS A 1 122 ? -14.816 7.607   17.971  1.00 6.93  ? 122 HIS A CB   1 
ATOM   1073 C  CG   . HIS A 1 122 ? -15.667 6.448   17.578  1.00 5.43  ? 122 HIS A CG   1 
ATOM   1074 N  ND1  . HIS A 1 122 ? -15.289 5.139   17.807  1.00 4.79  ? 122 HIS A ND1  1 
ATOM   1075 C  CD2  . HIS A 1 122 ? -16.873 6.382   16.918  1.00 6.36  ? 122 HIS A CD2  1 
ATOM   1076 C  CE1  . HIS A 1 122 ? -16.270 4.325   17.356  1.00 9.10  ? 122 HIS A CE1  1 
ATOM   1077 N  NE2  . HIS A 1 122 ? -17.218 5.056   16.793  1.00 7.67  ? 122 HIS A NE2  1 
ATOM   1078 N  N    . TRP A 1 123 ? -12.715 10.032  17.482  1.00 4.81  ? 123 TRP A N    1 
ATOM   1079 C  CA   . TRP A 1 123 ? -11.946 11.041  18.215  1.00 5.63  ? 123 TRP A CA   1 
ATOM   1080 C  C    . TRP A 1 123 ? -12.818 12.059  18.969  1.00 6.53  ? 123 TRP A C    1 
ATOM   1081 O  O    . TRP A 1 123 ? -13.957 12.407  18.535  1.00 6.83  ? 123 TRP A O    1 
ATOM   1082 C  CB   . TRP A 1 123 ? -10.963 11.793  17.265  1.00 6.76  ? 123 TRP A CB   1 
ATOM   1083 C  CG   . TRP A 1 123 ? -11.632 12.427  16.102  1.00 6.67  ? 123 TRP A CG   1 
ATOM   1084 C  CD1  . TRP A 1 123 ? -11.862 11.831  14.853  1.00 7.58  ? 123 TRP A CD1  1 
ATOM   1085 C  CD2  . TRP A 1 123 ? -12.147 13.794  15.984  1.00 7.61  ? 123 TRP A CD2  1 
ATOM   1086 N  NE1  . TRP A 1 123 ? -12.548 12.737  14.025  1.00 9.19  ? 123 TRP A NE1  1 
ATOM   1087 C  CE2  . TRP A 1 123 ? -12.695 13.941  14.683  1.00 11.39 ? 123 TRP A CE2  1 
ATOM   1088 C  CE3  . TRP A 1 123 ? -12.211 14.907  16.870  1.00 9.78  ? 123 TRP A CE3  1 
ATOM   1089 C  CZ2  . TRP A 1 123 ? -13.291 15.144  14.247  1.00 11.80 ? 123 TRP A CZ2  1 
ATOM   1090 C  CZ3  . TRP A 1 123 ? -12.812 16.106  16.405  1.00 9.86  ? 123 TRP A CZ3  1 
ATOM   1091 C  CH2  . TRP A 1 123 ? -13.319 16.219  15.143  1.00 10.08 ? 123 TRP A CH2  1 
ATOM   1092 N  N    . ASN A 1 124 ? -12.305 12.448  20.141  1.00 6.34  ? 124 ASN A N    1 
ATOM   1093 C  CA   . ASN A 1 124 ? -12.996 13.401  21.061  1.00 6.66  ? 124 ASN A CA   1 
ATOM   1094 C  C    . ASN A 1 124 ? -13.180 14.786  20.418  1.00 6.96  ? 124 ASN A C    1 
ATOM   1095 O  O    . ASN A 1 124 ? -12.181 15.458  20.096  1.00 6.25  ? 124 ASN A O    1 
ATOM   1096 C  CB   . ASN A 1 124 ? -12.182 13.480  22.339  1.00 8.00  ? 124 ASN A CB   1 
ATOM   1097 C  CG   . ASN A 1 124 ? -12.981 14.052  23.475  1.00 9.37  ? 124 ASN A CG   1 
ATOM   1098 O  OD1  . ASN A 1 124 ? -13.843 14.873  23.221  1.00 9.43  ? 124 ASN A OD1  1 
ATOM   1099 N  ND2  . ASN A 1 124 ? -12.787 13.535  24.693  1.00 9.69  ? 124 ASN A ND2  1 
ATOM   1100 N  N    . THR A 1 125 ? -14.445 15.206  20.241  1.00 8.88  ? 125 THR A N    1 
ATOM   1101 C  CA   . THR A 1 125 ? -14.686 16.432  19.469  1.00 10.19 ? 125 THR A CA   1 
ATOM   1102 C  C    . THR A 1 125 ? -14.136 17.673  20.247  1.00 11.04 ? 125 THR A C    1 
ATOM   1103 O  O    . THR A 1 125 ? -13.997 18.730  19.625  1.00 10.74 ? 125 THR A O    1 
ATOM   1104 C  CB   . THR A 1 125 ? -16.192 16.609  19.169  1.00 11.45 ? 125 THR A CB   1 
ATOM   1105 O  OG1  . THR A 1 125 ? -16.969 16.570  20.375  1.00 12.74 ? 125 THR A OG1  1 
ATOM   1106 C  CG2  . THR A 1 125 ? -16.648 15.486  18.227  1.00 11.91 ? 125 THR A CG2  1 
ATOM   1107 N  N    . LYS A 1 126 ? -13.894 17.418  21.615  1.00 6.51  ? 127 LYS A N    1 
ATOM   1108 C  CA   . LYS A 1 126 ? -13.384 18.636  22.328  1.00 7.29  ? 127 LYS A CA   1 
ATOM   1109 C  C    . LYS A 1 126 ? -11.970 19.072  21.787  1.00 9.17  ? 127 LYS A C    1 
ATOM   1110 O  O    . LYS A 1 126 ? -11.473 20.139  22.147  1.00 12.10 ? 127 LYS A O    1 
ATOM   1111 C  CB   . LYS A 1 126 ? -13.386 18.456  23.863  1.00 8.94  ? 127 LYS A CB   1 
ATOM   1112 C  CG   . LYS A 1 126 ? -12.354 17.573  24.357  1.00 10.74 ? 127 LYS A CG   1 
ATOM   1113 C  CD   . LYS A 1 126 ? -12.601 17.330  25.904  1.00 14.88 ? 127 LYS A CD   1 
ATOM   1114 C  CE   . LYS A 1 126 ? -11.663 16.342  26.395  1.00 22.92 ? 127 LYS A CE   1 
ATOM   1115 N  NZ   . LYS A 1 126 ? -12.123 15.809  27.704  0.01 20.16 ? 127 LYS A NZ   1 
ATOM   1116 N  N    . TYR A 1 127 ? -11.292 18.202  21.019  1.00 5.98  ? 128 TYR A N    1 
ATOM   1117 C  CA   . TYR A 1 127 ? -9.914  18.476  20.561  1.00 7.03  ? 128 TYR A CA   1 
ATOM   1118 C  C    . TYR A 1 127 ? -9.904  18.881  19.098  1.00 9.03  ? 128 TYR A C    1 
ATOM   1119 O  O    . TYR A 1 127 ? -8.808  19.061  18.513  1.00 10.07 ? 128 TYR A O    1 
ATOM   1120 C  CB   . TYR A 1 127 ? -8.977  17.254  20.834  1.00 8.51  ? 128 TYR A CB   1 
ATOM   1121 C  CG   . TYR A 1 127 ? -8.910  16.977  22.296  1.00 6.01  ? 128 TYR A CG   1 
ATOM   1122 C  CD1  . TYR A 1 127 ? -8.501  17.970  23.213  1.00 11.04 ? 128 TYR A CD1  1 
ATOM   1123 C  CD2  . TYR A 1 127 ? -9.188  15.740  22.744  1.00 4.80  ? 128 TYR A CD2  1 
ATOM   1124 C  CE1  . TYR A 1 127 ? -8.444  17.682  24.581  1.00 8.41  ? 128 TYR A CE1  1 
ATOM   1125 C  CE2  . TYR A 1 127 ? -9.132  15.390  24.097  1.00 6.28  ? 128 TYR A CE2  1 
ATOM   1126 C  CZ   . TYR A 1 127 ? -8.812  16.462  25.017  1.00 11.76 ? 128 TYR A CZ   1 
ATOM   1127 O  OH   . TYR A 1 127 ? -8.696  16.161  26.333  1.00 13.58 ? 128 TYR A OH   1 
ATOM   1128 N  N    . GLY A 1 128 ? -11.101 18.948  18.482  1.00 8.77  ? 129 GLY A N    1 
ATOM   1129 C  CA   . GLY A 1 128 ? -11.222 19.683  17.189  1.00 9.30  ? 129 GLY A CA   1 
ATOM   1130 C  C    . GLY A 1 128 ? -10.830 18.822  15.993  1.00 9.78  ? 129 GLY A C    1 
ATOM   1131 O  O    . GLY A 1 128 ? -11.476 18.945  14.953  1.00 12.25 ? 129 GLY A O    1 
ATOM   1132 N  N    . ASP A 1 129 ? -9.792  17.931  16.113  1.00 9.85  ? 130 ASP A N    1 
ATOM   1133 C  CA   . ASP A 1 129 ? -9.596  16.976  15.001  1.00 11.76 ? 130 ASP A CA   1 
ATOM   1134 C  C    . ASP A 1 129 ? -8.858  15.764  15.480  1.00 12.51 ? 130 ASP A C    1 
ATOM   1135 O  O    . ASP A 1 129 ? -8.401  15.714  16.635  1.00 11.46 ? 130 ASP A O    1 
ATOM   1136 C  CB   . ASP A 1 129 ? -8.923  17.602  13.740  1.00 13.20 ? 130 ASP A CB   1 
ATOM   1137 C  CG   . ASP A 1 129 ? -7.554  18.092  13.974  1.00 12.94 ? 130 ASP A CG   1 
ATOM   1138 O  OD1  . ASP A 1 129 ? -6.871  17.816  14.986  1.00 20.30 ? 130 ASP A OD1  1 
ATOM   1139 O  OD2  . ASP A 1 129 ? -6.967  18.726  13.083  1.00 16.19 ? 130 ASP A OD2  1 
ATOM   1140 N  N    . PHE A 1 130 ? -8.701  14.800  14.569  1.00 12.12 ? 131 PHE A N    1 
ATOM   1141 C  CA   . PHE A 1 130 ? -8.012  13.573  14.918  1.00 13.04 ? 131 PHE A CA   1 
ATOM   1142 C  C    . PHE A 1 130 ? -6.553  13.780  15.305  1.00 10.98 ? 131 PHE A C    1 
ATOM   1143 O  O    . PHE A 1 130 ? -6.051  13.162  16.318  1.00 9.38  ? 131 PHE A O    1 
ATOM   1144 C  CB   . PHE A 1 130 ? -8.115  12.566  13.778  1.00 11.52 ? 131 PHE A CB   1 
ATOM   1145 C  CG   . PHE A 1 130 ? -7.392  11.259  14.062  1.00 12.81 ? 131 PHE A CG   1 
ATOM   1146 C  CD1  . PHE A 1 130 ? -8.062  10.229  14.772  1.00 7.14  ? 131 PHE A CD1  1 
ATOM   1147 C  CD2  . PHE A 1 130 ? -6.014  11.109  13.798  1.00 14.89 ? 131 PHE A CD2  1 
ATOM   1148 C  CE1  . PHE A 1 130 ? -7.456  9.007   15.032  1.00 10.83 ? 131 PHE A CE1  1 
ATOM   1149 C  CE2  . PHE A 1 130 ? -5.322  9.856   14.084  1.00 16.82 ? 131 PHE A CE2  1 
ATOM   1150 C  CZ   . PHE A 1 130 ? -6.051  8.806   14.743  1.00 13.31 ? 131 PHE A CZ   1 
ATOM   1151 N  N    . GLY A 1 131 ? -5.837  14.608  14.520  1.00 10.33 ? 132 GLY A N    1 
ATOM   1152 C  CA   . GLY A 1 131 ? -4.454  14.751  14.829  1.00 12.36 ? 132 GLY A CA   1 
ATOM   1153 C  C    . GLY A 1 131 ? -4.128  15.348  16.204  1.00 11.69 ? 132 GLY A C    1 
ATOM   1154 O  O    . GLY A 1 131 ? -3.111  15.008  16.830  1.00 13.99 ? 132 GLY A O    1 
ATOM   1155 N  N    . LYS A 1 132 ? -4.959  16.311  16.652  1.00 10.37 ? 133 LYS A N    1 
ATOM   1156 C  CA   . LYS A 1 132 ? -4.796  16.846  17.999  1.00 10.21 ? 133 LYS A CA   1 
ATOM   1157 C  C    . LYS A 1 132 ? -5.311  15.887  19.089  1.00 10.74 ? 133 LYS A C    1 
ATOM   1158 O  O    . LYS A 1 132 ? -4.753  15.798  20.154  1.00 11.22 ? 133 LYS A O    1 
ATOM   1159 C  CB   . LYS A 1 132 ? -5.560  18.118  18.201  1.00 11.02 ? 133 LYS A CB   1 
ATOM   1160 C  CG   . LYS A 1 132 ? -5.036  19.368  17.427  1.00 17.10 ? 133 LYS A CG   1 
ATOM   1161 C  CD   . LYS A 1 132 ? -3.616  19.338  16.940  1.00 22.79 ? 133 LYS A CD   1 
ATOM   1162 C  CE   . LYS A 1 132 ? -3.171  20.806  16.740  1.00 26.03 ? 133 LYS A CE   1 
ATOM   1163 N  NZ   . LYS A 1 132 ? -2.869  21.405  18.143  1.00 34.40 ? 133 LYS A NZ   1 
ATOM   1164 N  N    . ALA A 1 133 ? -6.403  15.220  18.769  1.00 10.20 ? 134 ALA A N    1 
ATOM   1165 C  CA   . ALA A 1 133 ? -6.901  14.225  19.729  1.00 9.80  ? 134 ALA A CA   1 
ATOM   1166 C  C    . ALA A 1 133 ? -5.905  13.140  20.168  1.00 6.39  ? 134 ALA A C    1 
ATOM   1167 O  O    . ALA A 1 133 ? -5.901  12.731  21.349  1.00 8.17  ? 134 ALA A O    1 
ATOM   1168 C  CB   . ALA A 1 133 ? -8.144  13.507  19.114  1.00 6.88  ? 134 ALA A CB   1 
ATOM   1169 N  N    . VAL A 1 134 ? -5.143  12.584  19.202  1.00 7.85  ? 135 VAL A N    1 
ATOM   1170 C  CA   . VAL A 1 134 ? -4.212  11.450  19.563  1.00 10.36 ? 135 VAL A CA   1 
ATOM   1171 C  C    . VAL A 1 134 ? -3.103  11.899  20.519  1.00 9.02  ? 135 VAL A C    1 
ATOM   1172 O  O    . VAL A 1 134 ? -2.422  11.086  21.099  1.00 9.47  ? 135 VAL A O    1 
ATOM   1173 C  CB   . VAL A 1 134 ? -3.545  10.734  18.357  1.00 10.35 ? 135 VAL A CB   1 
ATOM   1174 C  CG1  . VAL A 1 134 ? -4.614  10.050  17.563  1.00 10.93 ? 135 VAL A CG1  1 
ATOM   1175 C  CG2  . VAL A 1 134 ? -2.601  11.653  17.439  1.00 12.62 ? 135 VAL A CG2  1 
ATOM   1176 N  N    A GLN A 1 135 ? -2.990  13.225  20.683  0.50 9.03  ? 136 GLN A N    1 
ATOM   1177 N  N    B GLN A 1 135 ? -2.936  13.213  20.690  0.50 9.37  ? 136 GLN A N    1 
ATOM   1178 C  CA   A GLN A 1 135 ? -2.043  13.800  21.633  0.50 10.59 ? 136 GLN A CA   1 
ATOM   1179 C  CA   B GLN A 1 135 ? -1.934  13.645  21.657  0.50 11.15 ? 136 GLN A CA   1 
ATOM   1180 C  C    A GLN A 1 135 ? -2.573  13.935  23.049  0.50 10.24 ? 136 GLN A C    1 
ATOM   1181 C  C    B GLN A 1 135 ? -2.492  13.751  23.084  0.50 10.14 ? 136 GLN A C    1 
ATOM   1182 O  O    A GLN A 1 135 ? -1.947  14.564  23.935  0.50 10.98 ? 136 GLN A O    1 
ATOM   1183 O  O    B GLN A 1 135 ? -1.777  14.139  24.018  0.50 11.62 ? 136 GLN A O    1 
ATOM   1184 C  CB   A GLN A 1 135 ? -1.631  15.178  21.117  0.50 10.41 ? 136 GLN A CB   1 
ATOM   1185 C  CB   B GLN A 1 135 ? -1.251  14.951  21.162  0.50 11.44 ? 136 GLN A CB   1 
ATOM   1186 C  CG   A GLN A 1 135 ? -1.129  15.094  19.721  0.50 11.21 ? 136 GLN A CG   1 
ATOM   1187 C  CG   B GLN A 1 135 ? -0.702  14.826  19.724  0.50 14.78 ? 136 GLN A CG   1 
ATOM   1188 C  CD   A GLN A 1 135 ? -0.461  16.381  19.331  0.50 15.02 ? 136 GLN A CD   1 
ATOM   1189 C  CD   B GLN A 1 135 ? 0.521   13.894  19.629  0.50 17.56 ? 136 GLN A CD   1 
ATOM   1190 O  OE1  A GLN A 1 135 ? -0.618  16.855  18.204  0.50 18.00 ? 136 GLN A OE1  1 
ATOM   1191 O  OE1  B GLN A 1 135 ? 1.263   13.733  20.608  0.50 23.72 ? 136 GLN A OE1  1 
ATOM   1192 N  NE2  A GLN A 1 135 ? 0.270   16.983  20.283  0.50 14.04 ? 136 GLN A NE2  1 
ATOM   1193 N  NE2  B GLN A 1 135 ? 0.762   13.322  18.440  0.50 18.73 ? 136 GLN A NE2  1 
ATOM   1194 N  N    . GLN A 1 136 ? -3.788  13.430  23.263  1.00 9.00  ? 137 GLN A N    1 
ATOM   1195 C  CA   . GLN A 1 136 ? -4.427  13.604  24.589  1.00 9.08  ? 137 GLN A CA   1 
ATOM   1196 C  C    . GLN A 1 136 ? -4.802  12.228  25.168  1.00 9.47  ? 137 GLN A C    1 
ATOM   1197 O  O    . GLN A 1 136 ? -5.143  11.311  24.433  1.00 6.88  ? 137 GLN A O    1 
ATOM   1198 C  CB   . GLN A 1 136 ? -5.679  14.448  24.496  1.00 9.94  ? 137 GLN A CB   1 
ATOM   1199 C  CG   . GLN A 1 136 ? -5.514  15.733  23.585  1.00 13.62 ? 137 GLN A CG   1 
ATOM   1200 C  CD   . GLN A 1 136 ? -4.548  16.727  24.129  1.00 19.42 ? 137 GLN A CD   1 
ATOM   1201 O  OE1  . GLN A 1 136 ? -3.915  17.476  23.373  1.00 27.55 ? 137 GLN A OE1  1 
ATOM   1202 N  NE2  . GLN A 1 136 ? -4.403  16.734  25.398  1.00 14.23 ? 137 GLN A NE2  1 
ATOM   1203 N  N    . PRO A 1 137 ? -4.849  12.094  26.478  1.00 9.78  ? 138 PRO A N    1 
ATOM   1204 C  CA   . PRO A 1 137 ? -5.071  10.803  27.110  1.00 9.86  ? 138 PRO A CA   1 
ATOM   1205 C  C    . PRO A 1 137 ? -6.480  10.329  26.968  1.00 9.09  ? 138 PRO A C    1 
ATOM   1206 O  O    . PRO A 1 137 ? -6.734  9.110   27.087  1.00 9.77  ? 138 PRO A O    1 
ATOM   1207 C  CB   . PRO A 1 137 ? -4.804  11.067  28.608  1.00 11.30 ? 138 PRO A CB   1 
ATOM   1208 C  CG   . PRO A 1 137 ? -4.416  12.442  28.719  1.00 15.06 ? 138 PRO A CG   1 
ATOM   1209 C  CD   . PRO A 1 137 ? -4.492  13.153  27.437  1.00 12.11 ? 138 PRO A CD   1 
ATOM   1210 N  N    . ASP A 1 138 ? -7.383  11.268  26.682  1.00 7.07  ? 139 ASP A N    1 
ATOM   1211 C  CA   . ASP A 1 138 ? -8.769  10.879  26.483  1.00 6.52  ? 139 ASP A CA   1 
ATOM   1212 C  C    . ASP A 1 138 ? -9.138  11.273  25.025  1.00 6.81  ? 139 ASP A C    1 
ATOM   1213 O  O    . ASP A 1 138 ? -10.283 11.687  24.757  1.00 6.92  ? 139 ASP A O    1 
ATOM   1214 C  CB   . ASP A 1 138 ? -9.741  11.520  27.488  1.00 8.59  ? 139 ASP A CB   1 
ATOM   1215 C  CG   . ASP A 1 138 ? -9.650  13.035  27.501  1.00 6.47  ? 139 ASP A CG   1 
ATOM   1216 O  OD1  . ASP A 1 138 ? -8.699  13.627  26.913  1.00 10.41 ? 139 ASP A OD1  1 
ATOM   1217 O  OD2  . ASP A 1 138 ? -10.586 13.610  28.146  1.00 12.29 ? 139 ASP A OD2  1 
ATOM   1218 N  N    . GLY A 1 139 ? -8.194  11.154  24.076  1.00 4.52  ? 140 GLY A N    1 
ATOM   1219 C  CA   . GLY A 1 139 ? -8.428  11.679  22.746  1.00 5.61  ? 140 GLY A CA   1 
ATOM   1220 C  C    . GLY A 1 139 ? -9.299  10.789  21.827  1.00 4.90  ? 140 GLY A C    1 
ATOM   1221 O  O    . GLY A 1 139 ? -10.033 11.295  20.985  1.00 5.47  ? 140 GLY A O    1 
ATOM   1222 N  N    . LEU A 1 140 ? -9.162  9.447   22.011  1.00 5.03  ? 141 LEU A N    1 
ATOM   1223 C  CA   . LEU A 1 140 ? -9.818  8.520   21.140  1.00 4.10  ? 141 LEU A CA   1 
ATOM   1224 C  C    . LEU A 1 140 ? -10.694 7.566   21.940  1.00 4.83  ? 141 LEU A C    1 
ATOM   1225 O  O    . LEU A 1 140 ? -10.377 7.303   23.111  1.00 5.65  ? 141 LEU A O    1 
ATOM   1226 C  CB   . LEU A 1 140 ? -8.821  7.657   20.372  1.00 4.91  ? 141 LEU A CB   1 
ATOM   1227 C  CG   . LEU A 1 140 ? -7.931  8.344   19.322  1.00 8.93  ? 141 LEU A CG   1 
ATOM   1228 C  CD1  . LEU A 1 140 ? -7.229  7.247   18.448  1.00 9.13  ? 141 LEU A CD1  1 
ATOM   1229 C  CD2  . LEU A 1 140 ? -8.470  9.390   18.444  1.00 11.76 ? 141 LEU A CD2  1 
ATOM   1230 N  N    . ALA A 1 141 ? -11.778 7.071   21.282  1.00 5.72  ? 142 ALA A N    1 
ATOM   1231 C  CA   . ALA A 1 141 ? -12.517 5.928   21.829  1.00 4.71  ? 142 ALA A CA   1 
ATOM   1232 C  C    . ALA A 1 141 ? -12.570 4.926   20.702  1.00 5.32  ? 142 ALA A C    1 
ATOM   1233 O  O    . ALA A 1 141 ? -12.919 5.294   19.619  1.00 6.02  ? 142 ALA A O    1 
ATOM   1234 C  CB   . ALA A 1 141 ? -13.886 6.394   22.291  1.00 5.33  ? 142 ALA A CB   1 
ATOM   1235 N  N    . VAL A 1 142 ? -12.047 3.715   20.951  1.00 4.96  ? 143 VAL A N    1 
ATOM   1236 C  CA   . VAL A 1 142 ? -12.079 2.684   19.905  1.00 5.03  ? 143 VAL A CA   1 
ATOM   1237 C  C    . VAL A 1 142 ? -13.034 1.626   20.445  1.00 5.35  ? 143 VAL A C    1 
ATOM   1238 O  O    . VAL A 1 142 ? -12.894 1.067   21.553  1.00 4.59  ? 143 VAL A O    1 
ATOM   1239 C  CB   . VAL A 1 142 ? -10.674 2.070   19.569  1.00 6.06  ? 143 VAL A CB   1 
ATOM   1240 C  CG1  . VAL A 1 142 ? -10.806 1.083   18.396  1.00 8.15  ? 143 VAL A CG1  1 
ATOM   1241 C  CG2  . VAL A 1 142 ? -9.713  3.188   19.212  1.00 5.11  ? 143 VAL A CG2  1 
ATOM   1242 N  N    . LEU A 1 143 ? -13.983 1.286   19.617  1.00 5.29  ? 144 LEU A N    1 
ATOM   1243 C  CA   . LEU A 1 143 ? -14.960 0.255   19.950  1.00 5.16  ? 144 LEU A CA   1 
ATOM   1244 C  C    . LEU A 1 143 ? -14.454 -0.993  19.243  1.00 5.84  ? 144 LEU A C    1 
ATOM   1245 O  O    . LEU A 1 143 ? -14.337 -1.027  17.983  1.00 5.84  ? 144 LEU A O    1 
ATOM   1246 C  CB   . LEU A 1 143 ? -16.345 0.735   19.403  1.00 6.40  ? 144 LEU A CB   1 
ATOM   1247 C  CG   . LEU A 1 143 ? -17.464 -0.282  19.385  1.00 4.73  ? 144 LEU A CG   1 
ATOM   1248 C  CD1  . LEU A 1 143 ? -17.757 -0.639  20.871  1.00 9.52  ? 144 LEU A CD1  1 
ATOM   1249 C  CD2  . LEU A 1 143 ? -18.749 0.341   18.812  1.00 5.58  ? 144 LEU A CD2  1 
ATOM   1250 N  N    . GLY A 1 144 ? -14.168 -2.045  20.034  1.00 4.29  ? 145 GLY A N    1 
ATOM   1251 C  CA   . GLY A 1 144 ? -13.580 -3.278  19.500  1.00 3.46  ? 145 GLY A CA   1 
ATOM   1252 C  C    . GLY A 1 144 ? -14.660 -4.388  19.506  1.00 4.05  ? 145 GLY A C    1 
ATOM   1253 O  O    . GLY A 1 144 ? -15.394 -4.483  20.433  1.00 5.15  ? 145 GLY A O    1 
ATOM   1254 N  N    . ILE A 1 145 ? -14.753 -5.126  18.427  1.00 4.28  ? 146 ILE A N    1 
ATOM   1255 C  CA   . ILE A 1 145 ? -15.845 -6.146  18.254  1.00 3.58  ? 146 ILE A CA   1 
ATOM   1256 C  C    . ILE A 1 145 ? -15.098 -7.401  17.752  1.00 5.64  ? 146 ILE A C    1 
ATOM   1257 O  O    . ILE A 1 145 ? -14.411 -7.364  16.726  1.00 6.43  ? 146 ILE A O    1 
ATOM   1258 C  CB   . ILE A 1 145 ? -16.854 -5.645  17.262  1.00 5.25  ? 146 ILE A CB   1 
ATOM   1259 C  CG1  . ILE A 1 145 ? -17.458 -4.361  17.750  1.00 5.63  ? 146 ILE A CG1  1 
ATOM   1260 C  CG2  . ILE A 1 145 ? -17.946 -6.754  17.015  1.00 6.71  ? 146 ILE A CG2  1 
ATOM   1261 C  CD1  . ILE A 1 145 ? -18.563 -3.774  16.817  1.00 6.33  ? 146 ILE A CD1  1 
ATOM   1262 N  N    . PHE A 1 146 ? -15.295 -8.508  18.436  1.00 6.05  ? 147 PHE A N    1 
ATOM   1263 C  CA   . PHE A 1 146 ? -14.600 -9.769  17.968  1.00 5.33  ? 147 PHE A CA   1 
ATOM   1264 C  C    . PHE A 1 146 ? -15.377 -10.421 16.816  1.00 7.50  ? 147 PHE A C    1 
ATOM   1265 O  O    . PHE A 1 146 ? -16.617 -10.267 16.762  1.00 6.87  ? 147 PHE A O    1 
ATOM   1266 C  CB   . PHE A 1 146 ? -14.610 -10.749 19.148  1.00 3.87  ? 147 PHE A CB   1 
ATOM   1267 C  CG   . PHE A 1 146 ? -13.780 -10.280 20.293  1.00 3.61  ? 147 PHE A CG   1 
ATOM   1268 C  CD1  . PHE A 1 146 ? -12.355 -10.085 20.118  1.00 4.09  ? 147 PHE A CD1  1 
ATOM   1269 C  CD2  . PHE A 1 146 ? -14.333 -10.086 21.534  1.00 7.19  ? 147 PHE A CD2  1 
ATOM   1270 C  CE1  . PHE A 1 146 ? -11.586 -9.636  21.177  1.00 3.70  ? 147 PHE A CE1  1 
ATOM   1271 C  CE2  . PHE A 1 146 ? -13.586 -9.599  22.602  1.00 6.24  ? 147 PHE A CE2  1 
ATOM   1272 C  CZ   . PHE A 1 146 ? -12.151 -9.478  22.458  1.00 5.25  ? 147 PHE A CZ   1 
ATOM   1273 N  N    . LEU A 1 147 ? -14.648 -11.103 15.930  1.00 5.79  ? 148 LEU A N    1 
ATOM   1274 C  CA   . LEU A 1 147 ? -15.235 -11.887 14.858  1.00 5.85  ? 148 LEU A CA   1 
ATOM   1275 C  C    . LEU A 1 147 ? -14.896 -13.354 15.096  1.00 7.91  ? 148 LEU A C    1 
ATOM   1276 O  O    . LEU A 1 147 ? -13.740 -13.675 15.319  1.00 6.55  ? 148 LEU A O    1 
ATOM   1277 C  CB   . LEU A 1 147 ? -14.620 -11.501 13.516  1.00 6.97  ? 148 LEU A CB   1 
ATOM   1278 C  CG   . LEU A 1 147 ? -15.221 -10.237 12.788  1.00 7.34  ? 148 LEU A CG   1 
ATOM   1279 C  CD1  . LEU A 1 147 ? -15.085 -8.907  13.694  1.00 7.96  ? 148 LEU A CD1  1 
ATOM   1280 C  CD2  . LEU A 1 147 ? -14.517 -10.037 11.475  1.00 8.11  ? 148 LEU A CD2  1 
ATOM   1281 N  N    . LYS A 1 148 ? -15.923 -14.210 15.001  1.00 5.68  ? 149 LYS A N    1 
ATOM   1282 C  CA   . LYS A 1 148 ? -15.739 -15.665 14.964  1.00 8.06  ? 149 LYS A CA   1 
ATOM   1283 C  C    . LYS A 1 148 ? -16.248 -16.154 13.597  1.00 7.71  ? 149 LYS A C    1 
ATOM   1284 O  O    . LYS A 1 148 ? -17.099 -15.510 12.955  1.00 8.68  ? 149 LYS A O    1 
ATOM   1285 C  CB   . LYS A 1 148 ? -16.502 -16.401 16.127  1.00 9.79  ? 149 LYS A CB   1 
ATOM   1286 C  CG   . LYS A 1 148 ? -18.021 -16.256 16.023  1.00 10.96 ? 149 LYS A CG   1 
ATOM   1287 C  CD   . LYS A 1 148 ? -18.677 -17.001 17.189  1.00 15.55 ? 149 LYS A CD   1 
ATOM   1288 C  CE   . LYS A 1 148 ? -20.128 -16.781 17.125  1.00 24.62 ? 149 LYS A CE   1 
ATOM   1289 N  NZ   . LYS A 1 148 ? -20.858 -17.717 18.101  1.00 33.50 ? 149 LYS A NZ   1 
ATOM   1290 N  N    . VAL A 1 149 ? -15.757 -17.325 13.198  1.00 7.53  ? 150 VAL A N    1 
ATOM   1291 C  CA   . VAL A 1 149 ? -16.095 -17.886 11.884  1.00 7.02  ? 150 VAL A CA   1 
ATOM   1292 C  C    . VAL A 1 149 ? -17.310 -18.818 12.088  1.00 7.03  ? 150 VAL A C    1 
ATOM   1293 O  O    . VAL A 1 149 ? -17.287 -19.785 12.904  1.00 9.58  ? 150 VAL A O    1 
ATOM   1294 C  CB   . VAL A 1 149 ? -14.934 -18.721 11.370  1.00 9.64  ? 150 VAL A CB   1 
ATOM   1295 C  CG1  . VAL A 1 149 ? -15.306 -19.491 10.103  1.00 9.22  ? 150 VAL A CG1  1 
ATOM   1296 C  CG2  . VAL A 1 149 ? -13.755 -17.754 11.005  1.00 9.90  ? 150 VAL A CG2  1 
ATOM   1297 N  N    . GLY A 1 150 ? -18.347 -18.537 11.356  1.00 8.55  ? 151 GLY A N    1 
ATOM   1298 C  CA   . GLY A 1 150 ? -19.572 -19.348 11.393  1.00 10.63 ? 151 GLY A CA   1 
ATOM   1299 C  C    . GLY A 1 150 ? -20.450 -18.869 10.291  1.00 8.70  ? 151 GLY A C    1 
ATOM   1300 O  O    . GLY A 1 150 ? -20.066 -18.955 9.153   1.00 10.44 ? 151 GLY A O    1 
ATOM   1301 N  N    . SER A 1 151 ? -21.652 -18.385 10.646  1.00 10.36 ? 152 SER A N    1 
ATOM   1302 C  CA   A SER A 1 151 ? -22.533 -17.788 9.634   0.50 11.71 ? 152 SER A CA   1 
ATOM   1303 C  CA   B SER A 1 151 ? -22.542 -17.760 9.647   0.50 11.03 ? 152 SER A CA   1 
ATOM   1304 C  C    . SER A 1 151 ? -21.926 -16.497 9.064   1.00 11.68 ? 152 SER A C    1 
ATOM   1305 O  O    . SER A 1 151 ? -21.150 -15.785 9.751   1.00 11.42 ? 152 SER A O    1 
ATOM   1306 C  CB   A SER A 1 151 ? -23.947 -17.558 10.190  0.50 13.51 ? 152 SER A CB   1 
ATOM   1307 C  CB   B SER A 1 151 ? -23.883 -17.393 10.267  0.50 12.70 ? 152 SER A CB   1 
ATOM   1308 O  OG   A SER A 1 151 ? -23.964 -16.581 11.224  0.50 16.84 ? 152 SER A OG   1 
ATOM   1309 O  OG   B SER A 1 151 ? -24.451 -18.500 10.921  0.50 11.88 ? 152 SER A OG   1 
ATOM   1310 N  N    . ALA A 1 152 ? -22.213 -16.204 7.781   1.00 9.88  ? 153 ALA A N    1 
ATOM   1311 C  CA   . ALA A 1 152 ? -21.736 -14.952 7.197   1.00 9.28  ? 153 ALA A CA   1 
ATOM   1312 C  C    . ALA A 1 152 ? -22.397 -13.708 7.888   1.00 8.45  ? 153 ALA A C    1 
ATOM   1313 O  O    . ALA A 1 152 ? -23.497 -13.797 8.410   1.00 10.83 ? 153 ALA A O    1 
ATOM   1314 C  CB   . ALA A 1 152 ? -22.010 -14.898 5.662   1.00 10.49 ? 153 ALA A CB   1 
ATOM   1315 N  N    . LYS A 1 153 ? -21.684 -12.575 7.790   1.00 10.10 ? 154 LYS A N    1 
ATOM   1316 C  CA   . LYS A 1 153 ? -22.253 -11.324 8.217   1.00 11.97 ? 154 LYS A CA   1 
ATOM   1317 C  C    . LYS A 1 153 ? -22.631 -10.538 6.951   1.00 9.98  ? 154 LYS A C    1 
ATOM   1318 O  O    . LYS A 1 153 ? -21.771 -10.063 6.215   1.00 9.82  ? 154 LYS A O    1 
ATOM   1319 C  CB   . LYS A 1 153 ? -21.236 -10.561 9.072   1.00 10.92 ? 154 LYS A CB   1 
ATOM   1320 C  CG   . LYS A 1 153 ? -21.823 -9.289  9.759   1.00 14.08 ? 154 LYS A CG   1 
ATOM   1321 C  CD   . LYS A 1 153 ? -22.618 -9.731  11.006  1.00 11.01 ? 154 LYS A CD   1 
ATOM   1322 C  CE   . LYS A 1 153 ? -22.852 -8.549  11.905  1.00 16.78 ? 154 LYS A CE   1 
ATOM   1323 N  NZ   . LYS A 1 153 ? -23.766 -8.974  12.939  1.00 20.05 ? 154 LYS A NZ   1 
ATOM   1324 N  N    . PRO A 1 154 ? -23.957 -10.505 6.632   1.00 12.53 ? 155 PRO A N    1 
ATOM   1325 C  CA   . PRO A 1 154 ? -24.329 -9.860  5.350   1.00 11.79 ? 155 PRO A CA   1 
ATOM   1326 C  C    . PRO A 1 154 ? -23.840 -8.438  5.299   1.00 10.95 ? 155 PRO A C    1 
ATOM   1327 O  O    . PRO A 1 154 ? -23.335 -7.993  4.239   1.00 12.13 ? 155 PRO A O    1 
ATOM   1328 C  CB   . PRO A 1 154 ? -25.885 -9.932  5.340   1.00 12.88 ? 155 PRO A CB   1 
ATOM   1329 C  CG   . PRO A 1 154 ? -26.237 -11.025 6.325   1.00 17.37 ? 155 PRO A CG   1 
ATOM   1330 C  CD   . PRO A 1 154 ? -25.104 -11.067 7.350   1.00 12.61 ? 155 PRO A CD   1 
ATOM   1331 N  N    . GLY A 1 155 ? -23.815 -7.746  6.430   1.00 11.76 ? 156 GLY A N    1 
ATOM   1332 C  CA   . GLY A 1 155 ? -23.369 -6.331  6.405   1.00 11.41 ? 156 GLY A CA   1 
ATOM   1333 C  C    . GLY A 1 155 ? -21.903 -6.089  6.116   1.00 12.90 ? 156 GLY A C    1 
ATOM   1334 O  O    . GLY A 1 155 ? -21.444 -4.941  5.884   1.00 14.08 ? 156 GLY A O    1 
ATOM   1335 N  N    . LEU A 1 156 ? -21.141 -7.178  6.176   1.00 10.99 ? 157 LEU A N    1 
ATOM   1336 C  CA   . LEU A 1 156 ? -19.698 -7.162  5.822   1.00 8.62  ? 157 LEU A CA   1 
ATOM   1337 C  C    . LEU A 1 156 ? -19.402 -7.329  4.356   1.00 9.46  ? 157 LEU A C    1 
ATOM   1338 O  O    . LEU A 1 156 ? -18.320 -7.112  3.897   1.00 10.23 ? 157 LEU A O    1 
ATOM   1339 C  CB   . LEU A 1 156 ? -18.941 -8.181  6.690   1.00 8.11  ? 157 LEU A CB   1 
ATOM   1340 C  CG   . LEU A 1 156 ? -17.391 -8.269  6.558   1.00 9.80  ? 157 LEU A CG   1 
ATOM   1341 C  CD1  . LEU A 1 156 ? -16.681 -6.906  6.890   1.00 10.92 ? 157 LEU A CD1  1 
ATOM   1342 C  CD2  . LEU A 1 156 ? -16.800 -9.491  7.366   1.00 9.90  ? 157 LEU A CD2  1 
ATOM   1343 N  N    . GLN A 1 157 ? -20.366 -7.881  3.619   1.00 9.86  ? 158 GLN A N    1 
ATOM   1344 C  CA   . GLN A 1 157 ? -20.054 -8.360  2.254   1.00 12.24 ? 158 GLN A CA   1 
ATOM   1345 C  C    . GLN A 1 157 ? -19.595 -7.247  1.343   1.00 10.01 ? 158 GLN A C    1 
ATOM   1346 O  O    . GLN A 1 157 ? -18.627 -7.426  0.621   1.00 12.45 ? 158 GLN A O    1 
ATOM   1347 C  CB   . GLN A 1 157 ? -21.203 -9.221  1.686   1.00 14.55 ? 158 GLN A CB   1 
ATOM   1348 C  CG   . GLN A 1 157 ? -20.735 -10.009 0.424   1.00 14.01 ? 158 GLN A CG   1 
ATOM   1349 C  CD   . GLN A 1 157 ? -19.603 -10.996 0.724   1.00 13.84 ? 158 GLN A CD   1 
ATOM   1350 O  OE1  . GLN A 1 157 ? -19.558 -11.561 1.827   1.00 14.40 ? 158 GLN A OE1  1 
ATOM   1351 N  NE2  . GLN A 1 157 ? -18.722 -11.260 -0.277  1.00 14.41 ? 158 GLN A NE2  1 
ATOM   1352 N  N    . LYS A 1 158 ? -20.188 -6.036  1.428   1.00 13.15 ? 159 LYS A N    1 
ATOM   1353 C  CA   . LYS A 1 158 ? -19.696 -4.947  0.577   1.00 12.92 ? 159 LYS A CA   1 
ATOM   1354 C  C    . LYS A 1 158 ? -18.208 -4.648  0.806   1.00 12.55 ? 159 LYS A C    1 
ATOM   1355 O  O    . LYS A 1 158 ? -17.454 -4.351  -0.091  1.00 13.62 ? 159 LYS A O    1 
ATOM   1356 C  CB   . LYS A 1 158 ? -20.515 -3.656  0.798   1.00 14.02 ? 159 LYS A CB   1 
ATOM   1357 C  CG   . LYS A 1 158 ? -21.997 -3.849  0.400   1.00 18.74 ? 159 LYS A CG   1 
ATOM   1358 C  CD   . LYS A 1 158 ? -22.326 -3.564  -1.123  1.00 24.21 ? 159 LYS A CD   1 
ATOM   1359 C  CE   . LYS A 1 158 ? -23.810 -3.734  -1.420  0.01 19.50 ? 159 LYS A CE   1 
ATOM   1360 N  NZ   . LYS A 1 158 ? -24.651 -2.700  -0.751  0.01 20.84 ? 159 LYS A NZ   1 
ATOM   1361 N  N    . VAL A 1 159 ? -17.763 -4.757  2.058   1.00 11.76 ? 160 VAL A N    1 
ATOM   1362 C  CA   . VAL A 1 159 ? -16.366 -4.552  2.306   1.00 9.79  ? 160 VAL A CA   1 
ATOM   1363 C  C    . VAL A 1 159 ? -15.540 -5.705  1.648   1.00 12.96 ? 160 VAL A C    1 
ATOM   1364 O  O    . VAL A 1 159 ? -14.520 -5.470  0.988   1.00 11.05 ? 160 VAL A O    1 
ATOM   1365 C  CB   . VAL A 1 159 ? -16.097 -4.534  3.848   1.00 12.11 ? 160 VAL A CB   1 
ATOM   1366 C  CG1  . VAL A 1 159 ? -14.608 -4.558  4.122   1.00 11.02 ? 160 VAL A CG1  1 
ATOM   1367 C  CG2  . VAL A 1 159 ? -16.861 -3.424  4.528   1.00 12.28 ? 160 VAL A CG2  1 
ATOM   1368 N  N    . VAL A 1 160 ? -15.961 -6.960  1.880   1.00 11.77 ? 161 VAL A N    1 
ATOM   1369 C  CA   . VAL A 1 160 ? -15.229 -8.111  1.325   1.00 13.82 ? 161 VAL A CA   1 
ATOM   1370 C  C    . VAL A 1 160 ? -15.096 -8.010  -0.203  1.00 12.46 ? 161 VAL A C    1 
ATOM   1371 O  O    . VAL A 1 160 ? -14.057 -8.200  -0.770  1.00 14.06 ? 161 VAL A O    1 
ATOM   1372 C  CB   . VAL A 1 160 ? -16.007 -9.462  1.696   1.00 14.38 ? 161 VAL A CB   1 
ATOM   1373 C  CG1  . VAL A 1 160 ? -15.591 -10.607 0.756   1.00 17.08 ? 161 VAL A CG1  1 
ATOM   1374 C  CG2  . VAL A 1 160 ? -15.815 -9.729  3.175   1.00 15.98 ? 161 VAL A CG2  1 
ATOM   1375 N  N    . ASP A 1 161 ? -16.176 -7.565  -0.827  1.00 14.49 ? 162 ASP A N    1 
ATOM   1376 C  CA   . ASP A 1 161 ? -16.160 -7.546  -2.289  1.00 15.94 ? 162 ASP A CA   1 
ATOM   1377 C  C    . ASP A 1 161 ? -15.217 -6.494  -2.916  1.00 16.04 ? 162 ASP A C    1 
ATOM   1378 O  O    . ASP A 1 161 ? -14.666 -6.721  -4.031  1.00 18.80 ? 162 ASP A O    1 
ATOM   1379 C  CB   . ASP A 1 161 ? -17.583 -7.434  -2.741  1.00 17.03 ? 162 ASP A CB   1 
ATOM   1380 C  CG   . ASP A 1 161 ? -18.313 -8.807  -2.737  1.00 14.85 ? 162 ASP A CG   1 
ATOM   1381 O  OD1  . ASP A 1 161 ? -17.674 -9.866  -2.764  1.00 20.50 ? 162 ASP A OD1  1 
ATOM   1382 O  OD2  . ASP A 1 161 ? -19.540 -8.777  -2.681  1.00 21.85 ? 162 ASP A OD2  1 
ATOM   1383 N  N    . VAL A 1 162 ? -14.929 -5.377  -2.223  1.00 13.39 ? 163 VAL A N    1 
ATOM   1384 C  CA   . VAL A 1 162 ? -14.116 -4.323  -2.809  1.00 15.66 ? 163 VAL A CA   1 
ATOM   1385 C  C    . VAL A 1 162 ? -12.629 -4.660  -2.615  1.00 12.26 ? 163 VAL A C    1 
ATOM   1386 O  O    . VAL A 1 162 ? -11.748 -4.023  -3.142  1.00 13.56 ? 163 VAL A O    1 
ATOM   1387 C  CB   . VAL A 1 162 ? -14.525 -2.941  -2.178  1.00 16.98 ? 163 VAL A CB   1 
ATOM   1388 C  CG1  . VAL A 1 162 ? -13.999 -2.817  -0.820  1.00 17.05 ? 163 VAL A CG1  1 
ATOM   1389 C  CG2  . VAL A 1 162 ? -14.090 -1.752  -3.005  1.00 16.35 ? 163 VAL A CG2  1 
ATOM   1390 N  N    . LEU A 1 163 ? -12.285 -5.640  -1.715  1.00 13.25 ? 164 LEU A N    1 
ATOM   1391 C  CA   . LEU A 1 163 ? -10.876 -5.965  -1.446  1.00 11.81 ? 164 LEU A CA   1 
ATOM   1392 C  C    . LEU A 1 163 ? -9.972  -6.352  -2.634  1.00 12.41 ? 164 LEU A C    1 
ATOM   1393 O  O    . LEU A 1 163 ? -8.794  -6.091  -2.629  1.00 11.97 ? 164 LEU A O    1 
ATOM   1394 C  CB   . LEU A 1 163 ? -10.724 -7.000  -0.305  1.00 11.15 ? 164 LEU A CB   1 
ATOM   1395 C  CG   . LEU A 1 163 ? -11.374 -6.675  1.046   1.00 11.84 ? 164 LEU A CG   1 
ATOM   1396 C  CD1  . LEU A 1 163 ? -11.111 -7.859  1.965   1.00 14.72 ? 164 LEU A CD1  1 
ATOM   1397 C  CD2  . LEU A 1 163 ? -10.762 -5.396  1.607   1.00 11.04 ? 164 LEU A CD2  1 
ATOM   1398 N  N    A ASP A 1 164 ? -10.529 -7.020  -3.648  0.50 14.74 ? 165 ASP A N    1 
ATOM   1399 N  N    B ASP A 1 164 ? -10.615 -6.988  -3.618  0.50 15.13 ? 165 ASP A N    1 
ATOM   1400 C  CA   A ASP A 1 164 ? -9.695  -7.333  -4.820  0.50 16.64 ? 165 ASP A CA   1 
ATOM   1401 C  CA   B ASP A 1 164 ? -9.975  -7.262  -4.891  0.50 17.74 ? 165 ASP A CA   1 
ATOM   1402 C  C    A ASP A 1 164 ? -9.275  -6.040  -5.591  0.50 16.55 ? 165 ASP A C    1 
ATOM   1403 C  C    B ASP A 1 164 ? -9.228  -6.028  -5.420  0.50 17.07 ? 165 ASP A C    1 
ATOM   1404 O  O    A ASP A 1 164 ? -8.437  -6.141  -6.492  0.50 18.02 ? 165 ASP A O    1 
ATOM   1405 O  O    B ASP A 1 164 ? -8.063  -6.134  -5.849  0.50 18.95 ? 165 ASP A O    1 
ATOM   1406 C  CB   A ASP A 1 164 ? -10.470 -8.226  -5.801  0.50 16.61 ? 165 ASP A CB   1 
ATOM   1407 C  CB   B ASP A 1 164 ? -11.064 -7.711  -5.881  0.50 17.70 ? 165 ASP A CB   1 
ATOM   1408 C  CG   A ASP A 1 164 ? -11.421 -7.415  -6.671  0.50 19.46 ? 165 ASP A CG   1 
ATOM   1409 C  CG   B ASP A 1 164 ? -11.654 -9.016  -5.496  0.50 22.88 ? 165 ASP A CG   1 
ATOM   1410 O  OD1  A ASP A 1 164 ? -12.420 -6.886  -6.161  0.50 18.14 ? 165 ASP A OD1  1 
ATOM   1411 O  OD1  B ASP A 1 164 ? -10.838 -9.943  -5.275  0.50 26.32 ? 165 ASP A OD1  1 
ATOM   1412 O  OD2  A ASP A 1 164 ? -11.143 -7.235  -7.871  0.50 23.16 ? 165 ASP A OD2  1 
ATOM   1413 O  OD2  B ASP A 1 164 ? -12.914 -9.124  -5.390  0.50 28.48 ? 165 ASP A OD2  1 
ATOM   1414 N  N    . SER A 1 165 ? -9.913  -4.887  -5.321  1.00 17.26 ? 166 SER A N    1 
ATOM   1415 C  CA   . SER A 1 165 ? -9.492  -3.629  -5.935  1.00 17.30 ? 166 SER A CA   1 
ATOM   1416 C  C    . SER A 1 165 ? -8.389  -2.883  -5.175  1.00 18.02 ? 166 SER A C    1 
ATOM   1417 O  O    . SER A 1 165 ? -7.804  -1.887  -5.697  1.00 17.71 ? 166 SER A O    1 
ATOM   1418 C  CB   . SER A 1 165 ? -10.683 -2.705  -6.181  1.00 17.81 ? 166 SER A CB   1 
ATOM   1419 O  OG   . SER A 1 165 ? -11.155 -2.138  -4.965  1.00 18.57 ? 166 SER A OG   1 
ATOM   1420 N  N    . ILE A 1 166 ? -8.097  -3.315  -3.924  1.00 14.70 ? 167 ILE A N    1 
ATOM   1421 C  CA   . ILE A 1 166 ? -7.041  -2.723  -3.097  1.00 12.94 ? 167 ILE A CA   1 
ATOM   1422 C  C    . ILE A 1 166 ? -6.083  -3.799  -2.565  1.00 13.52 ? 167 ILE A C    1 
ATOM   1423 O  O    . ILE A 1 166 ? -5.685  -3.813  -1.398  1.00 12.49 ? 167 ILE A O    1 
ATOM   1424 C  CB   . ILE A 1 166 ? -7.654  -1.859  -1.931  1.00 12.30 ? 167 ILE A CB   1 
ATOM   1425 C  CG1  . ILE A 1 166 ? -8.618  -2.690  -1.125  1.00 10.87 ? 167 ILE A CG1  1 
ATOM   1426 C  CG2  . ILE A 1 166 ? -8.381  -0.600  -2.520  1.00 12.88 ? 167 ILE A CG2  1 
ATOM   1427 C  CD1  . ILE A 1 166 ? -8.731  -2.221  0.373   1.00 16.54 ? 167 ILE A CD1  1 
ATOM   1428 N  N    . LYS A 1 167 ? -5.710  -4.736  -3.435  1.00 12.67 ? 168 LYS A N    1 
ATOM   1429 C  CA   . LYS A 1 167 ? -4.943  -5.843  -2.970  1.00 13.31 ? 168 LYS A CA   1 
ATOM   1430 C  C    . LYS A 1 167 ? -3.634  -5.451  -2.318  1.00 13.55 ? 168 LYS A C    1 
ATOM   1431 O  O    . LYS A 1 167 ? -3.197  -6.108  -1.393  1.00 11.12 ? 168 LYS A O    1 
ATOM   1432 C  CB   . LYS A 1 167 ? -4.603  -6.741  -4.151  1.00 13.17 ? 168 LYS A CB   1 
ATOM   1433 C  CG   . LYS A 1 167 ? -4.003  -7.994  -3.720  1.00 17.70 ? 168 LYS A CG   1 
ATOM   1434 C  CD   . LYS A 1 167 ? -4.134  -8.943  -4.931  1.00 24.21 ? 168 LYS A CD   1 
ATOM   1435 C  CE   . LYS A 1 167 ? -2.789  -9.209  -5.447  1.00 29.92 ? 168 LYS A CE   1 
ATOM   1436 N  NZ   . LYS A 1 167 ? -2.456  -10.585 -4.870  1.00 35.34 ? 168 LYS A NZ   1 
ATOM   1437 N  N    . THR A 1 168 ? -2.964  -4.375  -2.846  1.00 12.10 ? 169 THR A N    1 
ATOM   1438 C  CA   . THR A 1 168 ? -1.613  -4.088  -2.507  1.00 11.12 ? 169 THR A CA   1 
ATOM   1439 C  C    . THR A 1 168 ? -1.505  -2.732  -1.820  1.00 10.98 ? 169 THR A C    1 
ATOM   1440 O  O    . THR A 1 168 ? -2.413  -1.906  -1.942  1.00 12.66 ? 169 THR A O    1 
ATOM   1441 C  CB   . THR A 1 168 ? -0.639  -4.094  -3.736  1.00 13.57 ? 169 THR A CB   1 
ATOM   1442 O  OG1  . THR A 1 168 ? -1.281  -3.317  -4.774  1.00 15.07 ? 169 THR A OG1  1 
ATOM   1443 C  CG2  . THR A 1 168 ? -0.400  -5.570  -4.102  1.00 13.16 ? 169 THR A CG2  1 
ATOM   1444 N  N    . LYS A 1 169 ? -0.481  -2.612  -1.014  1.00 12.87 ? 170 LYS A N    1 
ATOM   1445 C  CA   . LYS A 1 169 ? -0.153  -1.435  -0.243  1.00 13.99 ? 170 LYS A CA   1 
ATOM   1446 C  C    . LYS A 1 169 ? -0.266  -0.161  -1.041  1.00 14.15 ? 170 LYS A C    1 
ATOM   1447 O  O    . LYS A 1 169 ? 0.223   -0.105  -2.206  1.00 18.19 ? 170 LYS A O    1 
ATOM   1448 C  CB   . LYS A 1 169 ? 1.259   -1.564  0.298   1.00 13.16 ? 170 LYS A CB   1 
ATOM   1449 C  CG   . LYS A 1 169 ? 1.806   -0.244  1.107   1.00 13.03 ? 170 LYS A CG   1 
ATOM   1450 C  CD   . LYS A 1 169 ? 3.065   -0.571  1.798   1.00 15.92 ? 170 LYS A CD   1 
ATOM   1451 C  CE   . LYS A 1 169 ? 4.120   -1.062  0.854   1.00 22.79 ? 170 LYS A CE   1 
ATOM   1452 N  NZ   . LYS A 1 169 ? 5.478   -1.234  1.492   1.00 29.13 ? 170 LYS A NZ   1 
ATOM   1453 N  N    . GLY A 1 170 ? -0.931  0.822   -0.488  1.00 14.47 ? 171 GLY A N    1 
ATOM   1454 C  CA   . GLY A 1 170 ? -1.136  2.135   -1.242  1.00 15.96 ? 171 GLY A CA   1 
ATOM   1455 C  C    . GLY A 1 170 ? -2.259  2.243   -2.260  1.00 17.34 ? 171 GLY A C    1 
ATOM   1456 O  O    . GLY A 1 170 ? -2.564  3.380   -2.786  1.00 16.70 ? 171 GLY A O    1 
ATOM   1457 N  N    . LYS A 1 171 ? -2.940  1.129   -2.570  1.00 12.85 ? 172 LYS A N    1 
ATOM   1458 C  CA   . LYS A 1 171 ? -4.190  1.216   -3.263  1.00 14.40 ? 172 LYS A CA   1 
ATOM   1459 C  C    . LYS A 1 171 ? -5.411  1.659   -2.470  1.00 14.33 ? 172 LYS A C    1 
ATOM   1460 O  O    . LYS A 1 171 ? -5.594  1.223   -1.316  1.00 15.99 ? 172 LYS A O    1 
ATOM   1461 C  CB   . LYS A 1 171 ? -4.455  -0.141  -3.871  1.00 14.74 ? 172 LYS A CB   1 
ATOM   1462 C  CG   . LYS A 1 171 ? -3.399  -0.468  -4.858  1.00 16.74 ? 172 LYS A CG   1 
ATOM   1463 C  CD   . LYS A 1 171 ? -4.164  -1.252  -5.967  1.00 26.76 ? 172 LYS A CD   1 
ATOM   1464 C  CE   . LYS A 1 171 ? -3.348  -1.494  -7.236  1.00 29.17 ? 172 LYS A CE   1 
ATOM   1465 N  NZ   . LYS A 1 171 ? -3.119  -0.264  -8.060  1.00 32.42 ? 172 LYS A NZ   1 
ATOM   1466 N  N    . SER A 1 172 ? -6.219  2.521   -3.055  1.00 15.40 ? 173 SER A N    1 
ATOM   1467 C  CA   . SER A 1 172 ? -7.473  2.976   -2.502  1.00 14.29 ? 173 SER A CA   1 
ATOM   1468 C  C    . SER A 1 172 ? -8.621  2.919   -3.489  1.00 16.28 ? 173 SER A C    1 
ATOM   1469 O  O    . SER A 1 172 ? -8.403  2.718   -4.735  1.00 16.29 ? 173 SER A O    1 
ATOM   1470 C  CB   . SER A 1 172 ? -7.352  4.401   -1.931  1.00 16.11 ? 173 SER A CB   1 
ATOM   1471 O  OG   . SER A 1 172 ? -7.100  5.346   -2.934  1.00 17.10 ? 173 SER A OG   1 
ATOM   1472 N  N    . ALA A 1 173 ? -9.823  2.920   -2.962  1.00 17.90 ? 174 ALA A N    1 
ATOM   1473 C  CA   . ALA A 1 173 ? -11.019 2.823   -3.812  1.00 17.48 ? 174 ALA A CA   1 
ATOM   1474 C  C    . ALA A 1 173 ? -12.107 3.639   -3.165  1.00 18.80 ? 174 ALA A C    1 
ATOM   1475 O  O    . ALA A 1 173 ? -12.276 3.659   -1.906  1.00 16.27 ? 174 ALA A O    1 
ATOM   1476 C  CB   . ALA A 1 173 ? -11.461 1.351   -4.059  1.00 18.20 ? 174 ALA A CB   1 
ATOM   1477 N  N    A ASP A 1 174 ? -12.964 4.170   -4.037  0.50 16.56 ? 175 ASP A N    1 
ATOM   1478 N  N    B ASP A 1 174 ? -12.714 4.529   -3.930  0.50 16.58 ? 175 ASP A N    1 
ATOM   1479 C  CA   A ASP A 1 174 ? -14.200 4.799   -3.633  0.50 16.07 ? 175 ASP A CA   1 
ATOM   1480 C  CA   B ASP A 1 174 ? -13.824 5.228   -3.305  0.50 16.88 ? 175 ASP A CA   1 
ATOM   1481 C  C    A ASP A 1 174 ? -15.125 3.903   -2.816  0.50 16.15 ? 175 ASP A C    1 
ATOM   1482 C  C    B ASP A 1 174 ? -14.782 4.112   -2.738  0.50 17.03 ? 175 ASP A C    1 
ATOM   1483 O  O    A ASP A 1 174 ? -15.445 2.753   -3.173  0.50 16.14 ? 175 ASP A O    1 
ATOM   1484 O  O    B ASP A 1 174 ? -14.679 2.966   -3.167  0.50 15.79 ? 175 ASP A O    1 
ATOM   1485 C  CB   A ASP A 1 174 ? -14.950 5.378   -4.852  0.50 16.05 ? 175 ASP A CB   1 
ATOM   1486 C  CB   B ASP A 1 174 ? -14.392 6.331   -4.223  0.50 18.31 ? 175 ASP A CB   1 
ATOM   1487 C  CG   A ASP A 1 174 ? -14.119 6.392   -5.608  0.50 17.76 ? 175 ASP A CG   1 
ATOM   1488 C  CG   B ASP A 1 174 ? -15.813 6.148   -4.501  0.50 19.30 ? 175 ASP A CG   1 
ATOM   1489 O  OD1  A ASP A 1 174 ? -13.411 7.190   -4.970  0.50 17.91 ? 175 ASP A OD1  1 
ATOM   1490 O  OD1  B ASP A 1 174 ? -16.094 5.110   -5.098  0.50 20.02 ? 175 ASP A OD1  1 
ATOM   1491 O  OD2  A ASP A 1 174 ? -14.207 6.435   -6.846  0.50 21.34 ? 175 ASP A OD2  1 
ATOM   1492 O  OD2  B ASP A 1 174 ? -16.636 7.022   -4.135  0.50 26.93 ? 175 ASP A OD2  1 
ATOM   1493 N  N    . PHE A 1 175 ? -15.564 4.428   -1.686  1.00 15.46 ? 176 PHE A N    1 
ATOM   1494 C  CA   . PHE A 1 175 ? -16.329 3.481   -0.829  1.00 16.59 ? 176 PHE A CA   1 
ATOM   1495 C  C    . PHE A 1 175 ? -17.324 4.296   -0.071  1.00 16.81 ? 176 PHE A C    1 
ATOM   1496 O  O    . PHE A 1 175 ? -17.116 4.654   1.110   1.00 14.75 ? 176 PHE A O    1 
ATOM   1497 C  CB   . PHE A 1 175 ? -15.415 2.667   0.113   1.00 16.44 ? 176 PHE A CB   1 
ATOM   1498 C  CG   . PHE A 1 175 ? -16.063 1.423   0.627   1.00 15.44 ? 176 PHE A CG   1 
ATOM   1499 C  CD1  . PHE A 1 175 ? -16.309 0.311   -0.201  1.00 16.48 ? 176 PHE A CD1  1 
ATOM   1500 C  CD2  . PHE A 1 175 ? -16.406 1.310   1.979   1.00 15.30 ? 176 PHE A CD2  1 
ATOM   1501 C  CE1  . PHE A 1 175 ? -16.909 -0.863  0.304   1.00 19.75 ? 176 PHE A CE1  1 
ATOM   1502 C  CE2  . PHE A 1 175 ? -17.037 0.140   2.491   1.00 15.33 ? 176 PHE A CE2  1 
ATOM   1503 C  CZ   . PHE A 1 175 ? -17.290 -0.937  1.677   1.00 18.58 ? 176 PHE A CZ   1 
ATOM   1504 N  N    . THR A 1 176 ? -18.402 4.634   -0.762  1.00 13.63 ? 177 THR A N    1 
ATOM   1505 C  CA   . THR A 1 176 ? -19.441 5.452   -0.184  1.00 13.58 ? 177 THR A CA   1 
ATOM   1506 C  C    . THR A 1 176 ? -20.628 4.639   0.250   1.00 13.49 ? 177 THR A C    1 
ATOM   1507 O  O    . THR A 1 176 ? -20.829 3.506   -0.234  1.00 15.16 ? 177 THR A O    1 
ATOM   1508 C  CB   . THR A 1 176 ? -19.857 6.573   -1.238  1.00 15.27 ? 177 THR A CB   1 
ATOM   1509 O  OG1  . THR A 1 176 ? -20.452 5.931   -2.352  1.00 18.64 ? 177 THR A OG1  1 
ATOM   1510 C  CG2  . THR A 1 176 ? -18.659 7.329   -1.662  1.00 19.41 ? 177 THR A CG2  1 
ATOM   1511 N  N    . ASN A 1 177 ? -21.449 5.220   1.135   1.00 11.61 ? 178 ASN A N    1 
ATOM   1512 C  CA   . ASN A 1 177 ? -22.750 4.697   1.583   1.00 11.90 ? 178 ASN A CA   1 
ATOM   1513 C  C    . ASN A 1 177 ? -22.637 3.358   2.337   1.00 12.56 ? 178 ASN A C    1 
ATOM   1514 O  O    . ASN A 1 177 ? -23.621 2.684   2.450   1.00 15.72 ? 178 ASN A O    1 
ATOM   1515 C  CB   . ASN A 1 177 ? -23.715 4.599   0.406   1.00 12.69 ? 178 ASN A CB   1 
ATOM   1516 C  CG   . ASN A 1 177 ? -23.906 6.015   -0.252  1.00 14.30 ? 178 ASN A CG   1 
ATOM   1517 O  OD1  . ASN A 1 177 ? -24.601 6.842   0.299   1.00 17.55 ? 178 ASN A OD1  1 
ATOM   1518 N  ND2  . ASN A 1 177 ? -23.187 6.272   -1.343  1.00 11.26 ? 178 ASN A ND2  1 
ATOM   1519 N  N    . PHE A 1 178 ? -21.470 3.129   2.906   1.00 10.76 ? 179 PHE A N    1 
ATOM   1520 C  CA   . PHE A 1 178 ? -21.289 1.873   3.708   1.00 10.61 ? 179 PHE A CA   1 
ATOM   1521 C  C    . PHE A 1 178 ? -21.817 2.154   5.078   1.00 10.52 ? 179 PHE A C    1 
ATOM   1522 O  O    . PHE A 1 178 ? -21.350 3.106   5.704   1.00 11.73 ? 179 PHE A O    1 
ATOM   1523 C  CB   . PHE A 1 178 ? -19.863 1.412   3.770   1.00 11.06 ? 179 PHE A CB   1 
ATOM   1524 C  CG   . PHE A 1 178 ? -19.737 0.166   4.588   1.00 10.84 ? 179 PHE A CG   1 
ATOM   1525 C  CD1  . PHE A 1 178 ? -20.229 -1.034  4.072   1.00 13.65 ? 179 PHE A CD1  1 
ATOM   1526 C  CD2  . PHE A 1 178 ? -19.357 0.256   5.922   1.00 11.54 ? 179 PHE A CD2  1 
ATOM   1527 C  CE1  . PHE A 1 178 ? -20.236 -2.189  4.848   1.00 13.82 ? 179 PHE A CE1  1 
ATOM   1528 C  CE2  . PHE A 1 178 ? -19.396 -0.901  6.727   1.00 8.59  ? 179 PHE A CE2  1 
ATOM   1529 C  CZ   . PHE A 1 178 ? -19.803 -2.100  6.197   1.00 11.93 ? 179 PHE A CZ   1 
ATOM   1530 N  N    . ASP A 1 179 ? -22.757 1.334   5.551   1.00 12.02 ? 180 ASP A N    1 
ATOM   1531 C  CA   . ASP A 1 179 ? -23.419 1.553   6.831   1.00 11.34 ? 180 ASP A CA   1 
ATOM   1532 C  C    . ASP A 1 179 ? -22.776 0.691   7.907   1.00 8.62  ? 180 ASP A C    1 
ATOM   1533 O  O    . ASP A 1 179 ? -22.974 -0.548  7.904   1.00 9.08  ? 180 ASP A O    1 
ATOM   1534 C  CB   . ASP A 1 179 ? -24.895 1.183   6.736   1.00 12.92 ? 180 ASP A CB   1 
ATOM   1535 C  CG   . ASP A 1 179 ? -25.686 1.612   7.961   1.00 15.79 ? 180 ASP A CG   1 
ATOM   1536 O  OD1  . ASP A 1 179 ? -25.118 1.761   9.095   1.00 11.97 ? 180 ASP A OD1  1 
ATOM   1537 O  OD2  . ASP A 1 179 ? -26.933 1.855   7.806   1.00 19.49 ? 180 ASP A OD2  1 
ATOM   1538 N  N    . PRO A 1 180 ? -22.010 1.287   8.834   1.00 8.98  ? 181 PRO A N    1 
ATOM   1539 C  CA   . PRO A 1 180 ? -21.321 0.387   9.834   1.00 9.88  ? 181 PRO A CA   1 
ATOM   1540 C  C    . PRO A 1 180 ? -22.258 -0.242  10.899  1.00 8.85  ? 181 PRO A C    1 
ATOM   1541 O  O    . PRO A 1 180 ? -21.821 -1.181  11.615  1.00 8.90  ? 181 PRO A O    1 
ATOM   1542 C  CB   . PRO A 1 180 ? -20.280 1.338   10.453  1.00 11.34 ? 181 PRO A CB   1 
ATOM   1543 C  CG   . PRO A 1 180 ? -21.044 2.653   10.519  1.00 10.45 ? 181 PRO A CG   1 
ATOM   1544 C  CD   . PRO A 1 180 ? -21.642 2.693   9.090   1.00 8.64  ? 181 PRO A CD   1 
ATOM   1545 N  N    . ARG A 1 181 ? -23.530 0.171   10.919  1.00 8.65  ? 182 ARG A N    1 
ATOM   1546 C  CA   . ARG A 1 181 ? -24.469 -0.470  11.858  1.00 8.87  ? 182 ARG A CA   1 
ATOM   1547 C  C    . ARG A 1 181 ? -24.575 -1.978  11.475  1.00 10.54 ? 182 ARG A C    1 
ATOM   1548 O  O    . ARG A 1 181 ? -24.972 -2.800  12.307  1.00 13.47 ? 182 ARG A O    1 
ATOM   1549 C  CB   . ARG A 1 181 ? -25.828 0.192   11.762  1.00 8.87  ? 182 ARG A CB   1 
ATOM   1550 C  CG   . ARG A 1 181 ? -25.786 1.664   12.261  1.00 7.74  ? 182 ARG A CG   1 
ATOM   1551 C  CD   . ARG A 1 181 ? -27.165 2.341   12.217  1.00 8.46  ? 182 ARG A CD   1 
ATOM   1552 N  NE   . ARG A 1 181 ? -27.521 2.487   10.832  1.00 12.77 ? 182 ARG A NE   1 
ATOM   1553 C  CZ   . ARG A 1 181 ? -28.644 3.098   10.436  1.00 19.55 ? 182 ARG A CZ   1 
ATOM   1554 N  NH1  . ARG A 1 181 ? -29.428 3.608   11.355  1.00 20.10 ? 182 ARG A NH1  1 
ATOM   1555 N  NH2  . ARG A 1 181 ? -28.940 3.211   9.156   1.00 18.62 ? 182 ARG A NH2  1 
ATOM   1556 N  N    . GLY A 1 182 ? -24.297 -2.297  10.220  1.00 10.56 ? 183 GLY A N    1 
ATOM   1557 C  CA   . GLY A 1 182 ? -24.288 -3.706  9.749   1.00 12.18 ? 183 GLY A CA   1 
ATOM   1558 C  C    . GLY A 1 182 ? -23.239 -4.603  10.371  1.00 12.75 ? 183 GLY A C    1 
ATOM   1559 O  O    . GLY A 1 182 ? -23.317 -5.832  10.197  1.00 14.17 ? 183 GLY A O    1 
ATOM   1560 N  N    . LEU A 1 183 ? -22.267 -4.014  11.086  1.00 10.36 ? 184 LEU A N    1 
ATOM   1561 C  CA   . LEU A 1 183 ? -21.195 -4.792  11.627  1.00 10.16 ? 184 LEU A CA   1 
ATOM   1562 C  C    . LEU A 1 183 ? -21.414 -4.972  13.141  1.00 9.77  ? 184 LEU A C    1 
ATOM   1563 O  O    . LEU A 1 183 ? -20.484 -5.532  13.806  1.00 12.35 ? 184 LEU A O    1 
ATOM   1564 C  CB   . LEU A 1 183 ? -19.849 -4.101  11.423  1.00 9.96  ? 184 LEU A CB   1 
ATOM   1565 C  CG   . LEU A 1 183 ? -19.521 -4.024  9.880   1.00 12.18 ? 184 LEU A CG   1 
ATOM   1566 C  CD1  . LEU A 1 183 ? -18.304 -3.178  9.695   1.00 12.90 ? 184 LEU A CD1  1 
ATOM   1567 C  CD2  . LEU A 1 183 ? -19.342 -5.337  9.140   1.00 15.85 ? 184 LEU A CD2  1 
ATOM   1568 N  N    . LEU A 1 184 ? -22.529 -4.499  13.742  1.00 8.99  ? 185 LEU A N    1 
ATOM   1569 C  CA   . LEU A 1 184 ? -22.624 -4.499  15.267  1.00 8.39  ? 185 LEU A CA   1 
ATOM   1570 C  C    . LEU A 1 184 ? -23.385 -5.778  15.720  1.00 10.97 ? 185 LEU A C    1 
ATOM   1571 O  O    . LEU A 1 184 ? -24.495 -6.094  15.174  1.00 15.88 ? 185 LEU A O    1 
ATOM   1572 C  CB   . LEU A 1 184 ? -23.381 -3.252  15.859  1.00 7.73  ? 185 LEU A CB   1 
ATOM   1573 C  CG   . LEU A 1 184 ? -22.916 -1.908  15.448  1.00 7.35  ? 185 LEU A CG   1 
ATOM   1574 C  CD1  . LEU A 1 184 ? -23.782 -0.667  15.797  1.00 10.44 ? 185 LEU A CD1  1 
ATOM   1575 C  CD2  . LEU A 1 184 ? -21.397 -1.833  15.977  1.00 9.84  ? 185 LEU A CD2  1 
ATOM   1576 N  N    . PRO A 1 185 ? -22.946 -6.366  16.849  1.00 10.63 ? 186 PRO A N    1 
ATOM   1577 C  CA   . PRO A 1 185 ? -23.730 -7.486  17.354  1.00 11.45 ? 186 PRO A CA   1 
ATOM   1578 C  C    . PRO A 1 185 ? -25.045 -6.975  17.973  1.00 11.20 ? 186 PRO A C    1 
ATOM   1579 O  O    . PRO A 1 185 ? -25.256 -5.743  18.080  1.00 11.94 ? 186 PRO A O    1 
ATOM   1580 C  CB   . PRO A 1 185 ? -22.835 -8.068  18.462  1.00 11.31 ? 186 PRO A CB   1 
ATOM   1581 C  CG   . PRO A 1 185 ? -21.974 -6.876  18.985  1.00 6.04  ? 186 PRO A CG   1 
ATOM   1582 C  CD   . PRO A 1 185 ? -21.785 -5.956  17.712  1.00 8.77  ? 186 PRO A CD   1 
ATOM   1583 N  N    . GLU A 1 186 ? -25.869 -7.895  18.517  1.00 11.81 ? 187 GLU A N    1 
ATOM   1584 C  CA   . GLU A 1 186 ? -27.145 -7.452  19.119  1.00 11.64 ? 187 GLU A CA   1 
ATOM   1585 C  C    . GLU A 1 186 ? -26.874 -6.747  20.436  1.00 11.15 ? 187 GLU A C    1 
ATOM   1586 O  O    . GLU A 1 186 ? -27.510 -5.726  20.712  1.00 12.92 ? 187 GLU A O    1 
ATOM   1587 C  CB   . GLU A 1 186 ? -28.046 -8.655  19.515  1.00 12.47 ? 187 GLU A CB   1 
ATOM   1588 C  CG   . GLU A 1 186 ? -28.524 -9.477  18.413  1.00 20.08 ? 187 GLU A CG   1 
ATOM   1589 C  CD   . GLU A 1 186 ? -29.409 -10.676 18.958  1.00 16.38 ? 187 GLU A CD   1 
ATOM   1590 O  OE1  . GLU A 1 186 ? -29.521 -10.846 20.190  1.00 18.74 ? 187 GLU A OE1  1 
ATOM   1591 O  OE2  . GLU A 1 186 ? -29.957 -11.420 18.109  1.00 31.47 ? 187 GLU A OE2  1 
ATOM   1592 N  N    . SER A 1 187 ? -25.983 -7.271  21.299  1.00 10.04 ? 188 SER A N    1 
ATOM   1593 C  CA   . SER A 1 187 ? -25.847 -6.653  22.597  1.00 9.91  ? 188 SER A CA   1 
ATOM   1594 C  C    . SER A 1 187 ? -24.706 -5.645  22.594  1.00 9.70  ? 188 SER A C    1 
ATOM   1595 O  O    . SER A 1 187 ? -23.693 -5.942  21.987  1.00 11.12 ? 188 SER A O    1 
ATOM   1596 C  CB   . SER A 1 187 ? -25.530 -7.704  23.670  1.00 10.48 ? 188 SER A CB   1 
ATOM   1597 O  OG   . SER A 1 187 ? -25.320 -7.127  24.939  1.00 12.05 ? 188 SER A OG   1 
ATOM   1598 N  N    . LEU A 1 188 ? -24.880 -4.563  23.306  1.00 9.01  ? 189 LEU A N    1 
ATOM   1599 C  CA   . LEU A 1 188 ? -23.762 -3.584  23.536  1.00 11.20 ? 189 LEU A CA   1 
ATOM   1600 C  C    . LEU A 1 188 ? -23.155 -3.705  24.917  1.00 8.99  ? 189 LEU A C    1 
ATOM   1601 O  O    . LEU A 1 188 ? -22.482 -2.734  25.386  1.00 10.23 ? 189 LEU A O    1 
ATOM   1602 C  CB   . LEU A 1 188 ? -24.274 -2.148  23.221  1.00 10.42 ? 189 LEU A CB   1 
ATOM   1603 C  CG   . LEU A 1 188 ? -24.744 -1.869  21.802  1.00 11.91 ? 189 LEU A CG   1 
ATOM   1604 C  CD1  . LEU A 1 188 ? -25.212 -0.377  21.821  1.00 14.14 ? 189 LEU A CD1  1 
ATOM   1605 C  CD2  . LEU A 1 188 ? -23.571 -1.953  20.785  1.00 11.86 ? 189 LEU A CD2  1 
ATOM   1606 N  N    . ASP A 1 189 ? -23.333 -4.858  25.599  1.00 8.56  ? 190 ASP A N    1 
ATOM   1607 C  CA   . ASP A 1 189 ? -22.564 -5.157  26.797  1.00 8.68  ? 190 ASP A CA   1 
ATOM   1608 C  C    . ASP A 1 189 ? -21.075 -5.090  26.425  1.00 7.01  ? 190 ASP A C    1 
ATOM   1609 O  O    . ASP A 1 189 ? -20.637 -5.526  25.377  1.00 7.40  ? 190 ASP A O    1 
ATOM   1610 C  CB   . ASP A 1 189 ? -22.869 -6.517  27.376  1.00 9.87  ? 190 ASP A CB   1 
ATOM   1611 C  CG   . ASP A 1 189 ? -24.341 -6.592  28.021  1.00 12.80 ? 190 ASP A CG   1 
ATOM   1612 O  OD1  . ASP A 1 189 ? -24.915 -5.545  28.254  1.00 17.69 ? 190 ASP A OD1  1 
ATOM   1613 O  OD2  . ASP A 1 189 ? -24.762 -7.734  28.254  1.00 22.00 ? 190 ASP A OD2  1 
ATOM   1614 N  N    . TYR A 1 190 ? -20.346 -4.461  27.339  1.00 5.50  ? 191 TYR A N    1 
ATOM   1615 C  CA   . TYR A 1 190 ? -18.913 -4.188  27.047  1.00 5.71  ? 191 TYR A CA   1 
ATOM   1616 C  C    . TYR A 1 190 ? -18.005 -4.250  28.264  1.00 6.48  ? 191 TYR A C    1 
ATOM   1617 O  O    . TYR A 1 190 ? -18.460 -4.159  29.440  1.00 6.52  ? 191 TYR A O    1 
ATOM   1618 C  CB   . TYR A 1 190 ? -18.745 -2.824  26.321  1.00 5.80  ? 191 TYR A CB   1 
ATOM   1619 C  CG   . TYR A 1 190 ? -19.115 -1.632  27.205  1.00 4.48  ? 191 TYR A CG   1 
ATOM   1620 C  CD1  . TYR A 1 190 ? -18.191 -1.017  28.088  1.00 6.12  ? 191 TYR A CD1  1 
ATOM   1621 C  CD2  . TYR A 1 190 ? -20.436 -1.129  27.177  1.00 6.62  ? 191 TYR A CD2  1 
ATOM   1622 C  CE1  . TYR A 1 190 ? -18.611 0.050   28.994  1.00 7.40  ? 191 TYR A CE1  1 
ATOM   1623 C  CE2  . TYR A 1 190 ? -20.856 -0.069  28.009  1.00 9.51  ? 191 TYR A CE2  1 
ATOM   1624 C  CZ   . TYR A 1 190 ? -19.924 0.534   28.923  1.00 10.12 ? 191 TYR A CZ   1 
ATOM   1625 O  OH   . TYR A 1 190 ? -20.299 1.550   29.752  1.00 9.62  ? 191 TYR A OH   1 
ATOM   1626 N  N    . TRP A 1 191 ? -16.703 -4.418  27.996  1.00 4.95  ? 192 TRP A N    1 
ATOM   1627 C  CA   . TRP A 1 191 ? -15.640 -4.168  29.004  1.00 4.92  ? 192 TRP A CA   1 
ATOM   1628 C  C    . TRP A 1 191 ? -14.894 -2.874  28.525  1.00 4.37  ? 192 TRP A C    1 
ATOM   1629 O  O    . TRP A 1 191 ? -14.950 -2.514  27.353  1.00 5.17  ? 192 TRP A O    1 
ATOM   1630 C  CB   . TRP A 1 191 ? -14.614 -5.238  28.912  1.00 7.43  ? 192 TRP A CB   1 
ATOM   1631 C  CG   . TRP A 1 191 ? -15.151 -6.609  29.324  1.00 5.93  ? 192 TRP A CG   1 
ATOM   1632 C  CD1  . TRP A 1 191 ? -15.419 -7.006  30.597  1.00 6.68  ? 192 TRP A CD1  1 
ATOM   1633 C  CD2  . TRP A 1 191 ? -15.431 -7.715  28.459  1.00 6.68  ? 192 TRP A CD2  1 
ATOM   1634 N  NE1  . TRP A 1 191 ? -15.825 -8.322  30.571  1.00 8.27  ? 192 TRP A NE1  1 
ATOM   1635 C  CE2  . TRP A 1 191 ? -15.856 -8.771  29.273  1.00 7.44  ? 192 TRP A CE2  1 
ATOM   1636 C  CE3  . TRP A 1 191 ? -15.303 -7.929  27.083  1.00 7.66  ? 192 TRP A CE3  1 
ATOM   1637 C  CZ2  . TRP A 1 191 ? -16.148 -10.067 28.751  1.00 7.26  ? 192 TRP A CZ2  1 
ATOM   1638 C  CZ3  . TRP A 1 191 ? -15.630 -9.202  26.557  1.00 6.61  ? 192 TRP A CZ3  1 
ATOM   1639 C  CH2  . TRP A 1 191 ? -16.046 -10.248 27.403  1.00 8.27  ? 192 TRP A CH2  1 
ATOM   1640 N  N    . THR A 1 192 ? -14.351 -2.153  29.483  1.00 3.87  ? 193 THR A N    1 
ATOM   1641 C  CA   . THR A 1 192 ? -13.633 -0.909  29.129  1.00 5.80  ? 193 THR A CA   1 
ATOM   1642 C  C    . THR A 1 192 ? -12.400 -0.687  29.990  1.00 6.19  ? 193 THR A C    1 
ATOM   1643 O  O    . THR A 1 192 ? -12.386 -1.083  31.145  1.00 6.97  ? 193 THR A O    1 
ATOM   1644 C  CB   . THR A 1 192 ? -14.538 0.333   29.217  1.00 6.80  ? 193 THR A CB   1 
ATOM   1645 O  OG1  . THR A 1 192 ? -13.833 1.544   28.834  1.00 6.25  ? 193 THR A OG1  1 
ATOM   1646 C  CG2  . THR A 1 192 ? -15.117 0.585   30.685  1.00 5.71  ? 193 THR A CG2  1 
ATOM   1647 N  N    . TYR A 1 193 ? -11.324 -0.138  29.407  1.00 5.90  ? 194 TYR A N    1 
ATOM   1648 C  CA   . TYR A 1 193 ? -10.091 0.125   30.173  1.00 6.21  ? 194 TYR A CA   1 
ATOM   1649 C  C    . TYR A 1 193 ? -9.316  1.152   29.358  1.00 6.31  ? 194 TYR A C    1 
ATOM   1650 O  O    . TYR A 1 193 ? -9.632  1.392   28.144  1.00 5.24  ? 194 TYR A O    1 
ATOM   1651 C  CB   . TYR A 1 193 ? -9.266  -1.173  30.331  1.00 6.15  ? 194 TYR A CB   1 
ATOM   1652 C  CG   . TYR A 1 193 ? -8.601  -1.614  29.063  1.00 7.08  ? 194 TYR A CG   1 
ATOM   1653 C  CD1  . TYR A 1 193 ? -9.313  -2.315  28.050  1.00 3.68  ? 194 TYR A CD1  1 
ATOM   1654 C  CD2  . TYR A 1 193 ? -7.246  -1.281  28.863  1.00 5.22  ? 194 TYR A CD2  1 
ATOM   1655 C  CE1  . TYR A 1 193 ? -8.660  -2.673  26.831  1.00 3.85  ? 194 TYR A CE1  1 
ATOM   1656 C  CE2  . TYR A 1 193 ? -6.607  -1.579  27.658  1.00 5.70  ? 194 TYR A CE2  1 
ATOM   1657 C  CZ   . TYR A 1 193 ? -7.284  -2.304  26.689  1.00 4.79  ? 194 TYR A CZ   1 
ATOM   1658 O  OH   . TYR A 1 193 ? -6.638  -2.574  25.494  1.00 5.63  ? 194 TYR A OH   1 
ATOM   1659 N  N    . PRO A 1 194 ? -8.414  1.845   30.051  1.00 6.03  ? 195 PRO A N    1 
ATOM   1660 C  CA   . PRO A 1 194 ? -7.624  2.878   29.325  1.00 5.62  ? 195 PRO A CA   1 
ATOM   1661 C  C    . PRO A 1 194 ? -6.383  2.272   28.667  1.00 7.22  ? 195 PRO A C    1 
ATOM   1662 O  O    . PRO A 1 194 ? -5.696  1.481   29.315  1.00 6.42  ? 195 PRO A O    1 
ATOM   1663 C  CB   . PRO A 1 194 ? -7.193  3.809   30.475  1.00 5.79  ? 195 PRO A CB   1 
ATOM   1664 C  CG   . PRO A 1 194 ? -7.138  2.946   31.710  1.00 8.95  ? 195 PRO A CG   1 
ATOM   1665 C  CD   . PRO A 1 194 ? -8.241  1.894   31.524  1.00 6.38  ? 195 PRO A CD   1 
ATOM   1666 N  N    . GLY A 1 195 ? -6.180  2.568   27.378  1.00 5.17  ? 196 GLY A N    1 
ATOM   1667 C  CA   . GLY A 1 195 ? -4.988  1.943   26.685  1.00 6.41  ? 196 GLY A CA   1 
ATOM   1668 C  C    . GLY A 1 195 ? -4.467  2.771   25.557  1.00 5.25  ? 196 GLY A C    1 
ATOM   1669 O  O    . GLY A 1 195 ? -4.408  3.997   25.682  1.00 5.73  ? 196 GLY A O    1 
ATOM   1670 N  N    . SER A 1 196 ? -4.105  2.150   24.447  1.00 5.71  ? 197 SER A N    1 
ATOM   1671 C  CA   . SER A 1 196 ? -3.283  2.857   23.448  1.00 4.60  ? 197 SER A CA   1 
ATOM   1672 C  C    . SER A 1 196 ? -3.711  2.461   22.049  1.00 4.27  ? 197 SER A C    1 
ATOM   1673 O  O    . SER A 1 196 ? -4.439  1.465   21.869  1.00 6.14  ? 197 SER A O    1 
ATOM   1674 C  CB   . SER A 1 196 ? -1.816  2.407   23.596  1.00 5.95  ? 197 SER A CB   1 
ATOM   1675 O  OG   . SER A 1 196 ? -1.614  1.072   23.190  1.00 3.90  ? 197 SER A OG   1 
ATOM   1676 N  N    . LEU A 1 197 ? -3.125  3.113   21.047  1.00 3.68  ? 198 LEU A N    1 
ATOM   1677 C  CA   . LEU A 1 197 ? -3.169  2.593   19.702  1.00 6.05  ? 198 LEU A CA   1 
ATOM   1678 C  C    . LEU A 1 197 ? -2.413  1.252   19.733  1.00 5.23  ? 198 LEU A C    1 
ATOM   1679 O  O    . LEU A 1 197 ? -1.346  1.081   20.415  1.00 4.86  ? 198 LEU A O    1 
ATOM   1680 C  CB   . LEU A 1 197 ? -2.442  3.562   18.775  1.00 5.97  ? 198 LEU A CB   1 
ATOM   1681 C  CG   . LEU A 1 197 ? -2.909  4.979   18.713  1.00 7.10  ? 198 LEU A CG   1 
ATOM   1682 C  CD1  . LEU A 1 197 ? -2.028  5.728   17.735  1.00 9.71  ? 198 LEU A CD1  1 
ATOM   1683 C  CD2  . LEU A 1 197 ? -4.357  5.096   18.340  1.00 8.09  ? 198 LEU A CD2  1 
ATOM   1684 N  N    . THR A 1 198 ? -2.888  0.288   18.969  1.00 5.69  ? 199 THR A N    1 
ATOM   1685 C  CA   . THR A 1 198 ? -2.184  -1.029  18.927  1.00 4.29  ? 199 THR A CA   1 
ATOM   1686 C  C    . THR A 1 198 ? -1.158  -1.108  17.779  1.00 5.72  ? 199 THR A C    1 
ATOM   1687 O  O    . THR A 1 198 ? -0.558  -2.207  17.578  1.00 6.36  ? 199 THR A O    1 
ATOM   1688 C  CB   . THR A 1 198 ? -3.240  -2.183  18.748  1.00 4.94  ? 199 THR A CB   1 
ATOM   1689 O  OG1  . THR A 1 198 ? -3.769  -2.151  17.458  1.00 5.80  ? 199 THR A OG1  1 
ATOM   1690 C  CG2  . THR A 1 198 ? -4.247  -2.131  19.888  1.00 5.18  ? 199 THR A CG2  1 
ATOM   1691 N  N    . THR A 1 199 ? -1.037  -0.028  16.972  1.00 5.07  ? 200 THR A N    1 
ATOM   1692 C  CA   . THR A 1 199 ? 0.037   0.053   15.997  1.00 7.16  ? 200 THR A CA   1 
ATOM   1693 C  C    . THR A 1 199 ? 0.886   1.273   16.262  1.00 6.05  ? 200 THR A C    1 
ATOM   1694 O  O    . THR A 1 199 ? 0.441   2.214   16.896  1.00 6.47  ? 200 THR A O    1 
ATOM   1695 C  CB   . THR A 1 199 ? -0.457  0.142   14.563  1.00 7.90  ? 200 THR A CB   1 
ATOM   1696 O  OG1  . THR A 1 199 ? -1.328  1.304   14.317  1.00 9.36  ? 200 THR A OG1  1 
ATOM   1697 C  CG2  . THR A 1 199 ? -1.245  -1.101  14.220  1.00 8.08  ? 200 THR A CG2  1 
ATOM   1698 N  N    . PRO A 1 200 ? 2.154   1.207   15.780  1.00 7.37  ? 201 PRO A N    1 
ATOM   1699 C  CA   . PRO A 1 200 ? 2.867   2.511   15.900  1.00 7.36  ? 201 PRO A CA   1 
ATOM   1700 C  C    . PRO A 1 200 ? 2.007   3.691   15.341  1.00 7.30  ? 201 PRO A C    1 
ATOM   1701 O  O    . PRO A 1 200 ? 1.395   3.562   14.237  1.00 9.19  ? 201 PRO A O    1 
ATOM   1702 C  CB   . PRO A 1 200 ? 4.116   2.241   15.012  1.00 6.86  ? 201 PRO A CB   1 
ATOM   1703 C  CG   . PRO A 1 200 ? 4.372   0.722   15.146  1.00 8.53  ? 201 PRO A CG   1 
ATOM   1704 C  CD   . PRO A 1 200 ? 2.947   0.118   15.170  1.00 8.54  ? 201 PRO A CD   1 
ATOM   1705 N  N    . PRO A 1 201 ? 2.065   4.903   15.997  1.00 8.38  ? 202 PRO A N    1 
ATOM   1706 C  CA   . PRO A 1 201 ? 2.972   5.283   17.085  1.00 9.75  ? 202 PRO A CA   1 
ATOM   1707 C  C    . PRO A 1 201 ? 2.617   4.858   18.523  1.00 7.43  ? 202 PRO A C    1 
ATOM   1708 O  O    . PRO A 1 201 ? 3.195   5.322   19.495  1.00 7.62  ? 202 PRO A O    1 
ATOM   1709 C  CB   . PRO A 1 201 ? 3.070   6.829   16.893  1.00 9.00  ? 202 PRO A CB   1 
ATOM   1710 C  CG   . PRO A 1 201 ? 1.673   7.200   16.501  1.00 9.66  ? 202 PRO A CG   1 
ATOM   1711 C  CD   . PRO A 1 201 ? 1.340   6.091   15.445  1.00 8.72  ? 202 PRO A CD   1 
ATOM   1712 N  N    . LEU A 1 202 ? 1.591   3.956   18.646  1.00 5.36  ? 203 LEU A N    1 
ATOM   1713 C  CA   . LEU A 1 202 ? 1.340   3.310   19.946  1.00 4.42  ? 203 LEU A CA   1 
ATOM   1714 C  C    . LEU A 1 202 ? 0.958   4.344   21.088  1.00 4.94  ? 203 LEU A C    1 
ATOM   1715 O  O    . LEU A 1 202 ? 1.131   4.080   22.273  1.00 6.62  ? 203 LEU A O    1 
ATOM   1716 C  CB   . LEU A 1 202 ? 2.487   2.423   20.465  1.00 5.61  ? 203 LEU A CB   1 
ATOM   1717 C  CG   . LEU A 1 202 ? 2.839   1.286   19.510  1.00 4.94  ? 203 LEU A CG   1 
ATOM   1718 C  CD1  . LEU A 1 202 ? 4.121   0.652   20.093  1.00 8.44  ? 203 LEU A CD1  1 
ATOM   1719 C  CD2  . LEU A 1 202 ? 1.723   0.214   19.421  1.00 9.31  ? 203 LEU A CD2  1 
ATOM   1720 N  N    . LEU A 1 203 ? 0.347   5.459   20.647  1.00 5.71  ? 204 LEU A N    1 
ATOM   1721 C  CA   . LEU A 1 203 ? 0.135   6.596   21.598  1.00 6.67  ? 204 LEU A CA   1 
ATOM   1722 C  C    . LEU A 1 203 ? -0.910  6.166   22.641  1.00 6.88  ? 204 LEU A C    1 
ATOM   1723 O  O    . LEU A 1 203 ? -1.901  5.437   22.320  1.00 5.76  ? 204 LEU A O    1 
ATOM   1724 C  CB   . LEU A 1 203 ? -0.378  7.845   20.831  1.00 7.07  ? 204 LEU A CB   1 
ATOM   1725 C  CG   . LEU A 1 203 ? 0.711   8.363   19.859  1.00 7.71  ? 204 LEU A CG   1 
ATOM   1726 C  CD1  . LEU A 1 203 ? 0.079   9.372   18.891  1.00 11.36 ? 204 LEU A CD1  1 
ATOM   1727 C  CD2  . LEU A 1 203 ? 1.905   8.968   20.714  1.00 13.58 ? 204 LEU A CD2  1 
ATOM   1728 N  N    . GLU A 1 204 ? -0.738  6.657   23.850  1.00 6.59  ? 205 GLU A N    1 
ATOM   1729 C  CA   . GLU A 1 204 ? -1.590  6.238   24.984  1.00 6.39  ? 205 GLU A CA   1 
ATOM   1730 C  C    . GLU A 1 204 ? -2.791  7.192   25.086  1.00 7.37  ? 205 GLU A C    1 
ATOM   1731 O  O    . GLU A 1 204 ? -2.909  8.026   26.046  1.00 8.07  ? 205 GLU A O    1 
ATOM   1732 C  CB   . GLU A 1 204 ? -0.777  6.142   26.256  1.00 7.36  ? 205 GLU A CB   1 
ATOM   1733 C  CG   . GLU A 1 204 ? 0.050   4.766   26.142  1.00 8.24  ? 205 GLU A CG   1 
ATOM   1734 C  CD   . GLU A 1 204 ? 1.038   4.573   27.265  1.00 12.30 ? 205 GLU A CD   1 
ATOM   1735 O  OE1  . GLU A 1 204 ? 1.348   5.544   28.005  1.00 10.20 ? 205 GLU A OE1  1 
ATOM   1736 O  OE2  . GLU A 1 204 ? 1.451   3.426   27.395  1.00 9.26  ? 205 GLU A OE2  1 
ATOM   1737 N  N    . CYS A 1 205 ? -3.667  7.086   24.093  1.00 6.77  ? 206 CYS A N    1 
ATOM   1738 C  CA   . CYS A 1 205 ? -4.726  8.121   23.941  1.00 5.38  ? 206 CYS A CA   1 
ATOM   1739 C  C    . CYS A 1 205 ? -6.082  7.512   23.815  1.00 5.78  ? 206 CYS A C    1 
ATOM   1740 O  O    . CYS A 1 205 ? -7.005  8.216   23.355  1.00 7.74  ? 206 CYS A O    1 
ATOM   1741 C  CB   . CYS A 1 205 ? -4.485  8.952   22.695  1.00 5.34  ? 206 CYS A CB   1 
ATOM   1742 S  SG   . CYS A 1 205 ? -4.339  7.972   21.174  1.00 8.05  ? 206 CYS A SG   1 
ATOM   1743 N  N    . VAL A 1 206 ? -6.208  6.225   24.155  1.00 3.94  ? 207 VAL A N    1 
ATOM   1744 C  CA   . VAL A 1 206 ? -7.470  5.474   23.782  1.00 3.35  ? 207 VAL A CA   1 
ATOM   1745 C  C    . VAL A 1 206 ? -8.257  4.983   24.989  1.00 4.07  ? 207 VAL A C    1 
ATOM   1746 O  O    . VAL A 1 206 ? -7.705  4.365   25.872  1.00 6.26  ? 207 VAL A O    1 
ATOM   1747 C  CB   . VAL A 1 206 ? -7.153  4.193   22.933  1.00 4.73  ? 207 VAL A CB   1 
ATOM   1748 C  CG1  . VAL A 1 206 ? -8.485  3.502   22.540  1.00 6.24  ? 207 VAL A CG1  1 
ATOM   1749 C  CG2  . VAL A 1 206 ? -6.458  4.554   21.585  1.00 6.47  ? 207 VAL A CG2  1 
ATOM   1750 N  N    . THR A 1 207 ? -9.578  5.285   25.008  1.00 4.55  ? 208 THR A N    1 
ATOM   1751 C  CA   . THR A 1 207 ? -10.491 4.603   25.968  1.00 4.16  ? 208 THR A CA   1 
ATOM   1752 C  C    . THR A 1 207 ? -11.020 3.433   25.158  1.00 4.49  ? 208 THR A C    1 
ATOM   1753 O  O    . THR A 1 207 ? -11.656 3.651   24.106  1.00 5.75  ? 208 THR A O    1 
ATOM   1754 C  CB   . THR A 1 207 ? -11.721 5.479   26.358  1.00 5.15  ? 208 THR A CB   1 
ATOM   1755 O  OG1  . THR A 1 207 ? -11.191 6.580   27.088  1.00 5.78  ? 208 THR A OG1  1 
ATOM   1756 C  CG2  . THR A 1 207 ? -12.633 4.697   27.237  1.00 6.45  ? 208 THR A CG2  1 
ATOM   1757 N  N    . TRP A 1 208 ? -10.674 2.241   25.572  1.00 3.39  ? 209 TRP A N    1 
ATOM   1758 C  CA   . TRP A 1 208 ? -11.057 1.055   24.820  1.00 3.22  ? 209 TRP A CA   1 
ATOM   1759 C  C    . TRP A 1 208 ? -12.462 0.584   25.331  1.00 4.26  ? 209 TRP A C    1 
ATOM   1760 O  O    . TRP A 1 208 ? -12.686 0.526   26.535  1.00 5.08  ? 209 TRP A O    1 
ATOM   1761 C  CB   . TRP A 1 208 ? -10.009 -0.115  25.034  1.00 4.78  ? 209 TRP A CB   1 
ATOM   1762 C  CG   . TRP A 1 208 ? -8.946  0.044   24.049  1.00 4.65  ? 209 TRP A CG   1 
ATOM   1763 C  CD1  . TRP A 1 208 ? -7.622  0.599   24.235  1.00 4.66  ? 209 TRP A CD1  1 
ATOM   1764 C  CD2  . TRP A 1 208 ? -9.025  -0.396  22.674  1.00 4.51  ? 209 TRP A CD2  1 
ATOM   1765 N  NE1  . TRP A 1 208 ? -6.998  0.606   22.994  1.00 3.50  ? 209 TRP A NE1  1 
ATOM   1766 C  CE2  . TRP A 1 208 ? -7.750  -0.088  22.060  1.00 4.04  ? 209 TRP A CE2  1 
ATOM   1767 C  CE3  . TRP A 1 208 ? -10.027 -1.046  21.914  1.00 5.23  ? 209 TRP A CE3  1 
ATOM   1768 C  CZ2  . TRP A 1 208 ? -7.515  -0.289  20.698  1.00 5.91  ? 209 TRP A CZ2  1 
ATOM   1769 C  CZ3  . TRP A 1 208 ? -9.763  -1.343  20.591  1.00 4.88  ? 209 TRP A CZ3  1 
ATOM   1770 C  CH2  . TRP A 1 208 ? -8.498  -0.985  19.975  1.00 4.25  ? 209 TRP A CH2  1 
ATOM   1771 N  N    . ILE A 1 209 ? -13.319 0.309   24.374  1.00 4.27  ? 210 ILE A N    1 
ATOM   1772 C  CA   . ILE A 1 209 ? -14.632 -0.261  24.726  1.00 4.26  ? 210 ILE A CA   1 
ATOM   1773 C  C    . ILE A 1 209 ? -14.735 -1.560  23.879  1.00 5.65  ? 210 ILE A C    1 
ATOM   1774 O  O    . ILE A 1 209 ? -14.816 -1.473  22.694  1.00 5.42  ? 210 ILE A O    1 
ATOM   1775 C  CB   . ILE A 1 209 ? -15.674 0.775   24.356  1.00 5.95  ? 210 ILE A CB   1 
ATOM   1776 C  CG1  . ILE A 1 209 ? -15.446 2.043   25.185  1.00 7.10  ? 210 ILE A CG1  1 
ATOM   1777 C  CG2  . ILE A 1 209 ? -17.155 0.185   24.609  1.00 5.86  ? 210 ILE A CG2  1 
ATOM   1778 C  CD1  . ILE A 1 209 ? -16.307 3.183   24.620  1.00 10.32 ? 210 ILE A CD1  1 
ATOM   1779 N  N    . VAL A 1 210 ? -14.673 -2.718  24.522  1.00 4.47  ? 211 VAL A N    1 
ATOM   1780 C  CA   . VAL A 1 210 ? -14.695 -4.025  23.789  1.00 3.27  ? 211 VAL A CA   1 
ATOM   1781 C  C    . VAL A 1 210 ? -16.023 -4.746  24.108  1.00 4.94  ? 211 VAL A C    1 
ATOM   1782 O  O    . VAL A 1 210 ? -16.366 -5.001  25.241  1.00 5.05  ? 211 VAL A O    1 
ATOM   1783 C  CB   . VAL A 1 210 ? -13.505 -4.886  24.210  1.00 4.95  ? 211 VAL A CB   1 
ATOM   1784 C  CG1  . VAL A 1 210 ? -13.527 -6.303  23.510  1.00 5.22  ? 211 VAL A CG1  1 
ATOM   1785 C  CG2  . VAL A 1 210 ? -12.074 -4.122  23.923  1.00 2.92  ? 211 VAL A CG2  1 
ATOM   1786 N  N    . LEU A 1 211 ? -16.730 -4.991  23.024  1.00 4.76  ? 212 LEU A N    1 
ATOM   1787 C  CA   . LEU A 1 211 ? -18.003 -5.696  23.163  1.00 5.51  ? 212 LEU A CA   1 
ATOM   1788 C  C    . LEU A 1 211 ? -17.772 -7.143  23.507  1.00 4.74  ? 212 LEU A C    1 
ATOM   1789 O  O    . LEU A 1 211 ? -16.921 -7.848  23.007  1.00 6.20  ? 212 LEU A O    1 
ATOM   1790 C  CB   . LEU A 1 211 ? -18.794 -5.558  21.863  1.00 5.83  ? 212 LEU A CB   1 
ATOM   1791 C  CG   . LEU A 1 211 ? -19.144 -4.131  21.394  1.00 7.89  ? 212 LEU A CG   1 
ATOM   1792 C  CD1  . LEU A 1 211 ? -20.212 -4.117  20.228  1.00 8.35  ? 212 LEU A CD1  1 
ATOM   1793 C  CD2  . LEU A 1 211 ? -19.610 -3.261  22.598  1.00 6.61  ? 212 LEU A CD2  1 
ATOM   1794 N  N    . LYS A 1 212 ? -18.689 -7.595  24.384  1.00 5.32  ? 213 LYS A N    1 
ATOM   1795 C  CA   . LYS A 1 212 ? -18.625 -9.000  24.811  1.00 5.80  ? 213 LYS A CA   1 
ATOM   1796 C  C    . LYS A 1 212 ? -19.137 -9.946  23.722  1.00 6.75  ? 213 LYS A C    1 
ATOM   1797 O  O    . LYS A 1 212 ? -18.640 -11.087 23.609  1.00 8.31  ? 213 LYS A O    1 
ATOM   1798 C  CB   . LYS A 1 212 ? -19.420 -9.165  26.149  1.00 9.22  ? 213 LYS A CB   1 
ATOM   1799 C  CG   . LYS A 1 212 ? -19.630 -10.689 26.479  1.00 10.28 ? 213 LYS A CG   1 
ATOM   1800 C  CD   . LYS A 1 212 ? -20.088 -10.886 27.879  1.00 16.90 ? 213 LYS A CD   1 
ATOM   1801 C  CE   . LYS A 1 212 ? -20.349 -12.293 28.310  1.00 20.29 ? 213 LYS A CE   1 
ATOM   1802 N  NZ   . LYS A 1 212 ? -21.397 -12.192 29.475  1.00 25.06 ? 213 LYS A NZ   1 
ATOM   1803 N  N    . GLU A 1 213 ? -20.164 -9.534  22.982  1.00 4.54  ? 214 GLU A N    1 
ATOM   1804 C  CA   . GLU A 1 213 ? -20.727 -10.384 21.922  1.00 5.79  ? 214 GLU A CA   1 
ATOM   1805 C  C    . GLU A 1 213 ? -19.985 -10.310 20.672  1.00 4.92  ? 214 GLU A C    1 
ATOM   1806 O  O    . GLU A 1 213 ? -19.959 -9.218  20.054  1.00 6.06  ? 214 GLU A O    1 
ATOM   1807 C  CB   . GLU A 1 213 ? -22.225 -10.000 21.745  1.00 5.06  ? 214 GLU A CB   1 
ATOM   1808 C  CG   . GLU A 1 213 ? -22.848 -11.021 20.801  1.00 8.96  ? 214 GLU A CG   1 
ATOM   1809 C  CD   . GLU A 1 213 ? -24.331 -10.871 20.588  1.00 18.39 ? 214 GLU A CD   1 
ATOM   1810 O  OE1  . GLU A 1 213 ? -24.925 -10.006 21.201  1.00 14.24 ? 214 GLU A OE1  1 
ATOM   1811 O  OE2  . GLU A 1 213 ? -24.893 -11.732 19.842  1.00 23.96 ? 214 GLU A OE2  1 
ATOM   1812 N  N    . PRO A 1 214 ? -19.398 -11.415 20.226  1.00 7.98  ? 215 PRO A N    1 
ATOM   1813 C  CA   . PRO A 1 214 ? -18.769 -11.360 18.885  1.00 7.28  ? 215 PRO A CA   1 
ATOM   1814 C  C    . PRO A 1 214 ? -19.740 -11.329 17.771  1.00 9.00  ? 215 PRO A C    1 
ATOM   1815 O  O    . PRO A 1 214 ? -20.954 -11.741 17.974  1.00 10.34 ? 215 PRO A O    1 
ATOM   1816 C  CB   . PRO A 1 214 ? -18.018 -12.684 18.789  1.00 6.90  ? 215 PRO A CB   1 
ATOM   1817 C  CG   . PRO A 1 214 ? -18.822 -13.655 19.632  1.00 11.97 ? 215 PRO A CG   1 
ATOM   1818 C  CD   . PRO A 1 214 ? -19.374 -12.790 20.794  1.00 9.23  ? 215 PRO A CD   1 
ATOM   1819 N  N    . ILE A 1 215 ? -19.296 -10.846 16.608  1.00 7.15  ? 216 ILE A N    1 
ATOM   1820 C  CA   . ILE A 1 215 ? -20.103 -11.114 15.443  1.00 8.22  ? 216 ILE A CA   1 
ATOM   1821 C  C    . ILE A 1 215 ? -19.602 -12.368 14.723  1.00 7.12  ? 216 ILE A C    1 
ATOM   1822 O  O    . ILE A 1 215 ? -18.414 -12.705 14.810  1.00 8.06  ? 216 ILE A O    1 
ATOM   1823 C  CB   . ILE A 1 215 ? -20.134 -9.942  14.417  1.00 7.35  ? 216 ILE A CB   1 
ATOM   1824 C  CG1  . ILE A 1 215 ? -18.655 -9.548  14.014  1.00 6.40  ? 216 ILE A CG1  1 
ATOM   1825 C  CG2  . ILE A 1 215 ? -20.952 -8.705  14.979  1.00 10.75 ? 216 ILE A CG2  1 
ATOM   1826 C  CD1  . ILE A 1 215 ? -18.683 -8.534  12.697  1.00 8.64  ? 216 ILE A CD1  1 
ATOM   1827 N  N    . SER A 1 216 ? -20.501 -13.028 13.999  1.00 7.23  ? 217 SER A N    1 
ATOM   1828 C  CA   A SER A 1 216 ? -20.114 -14.194 13.168  0.50 7.42  ? 217 SER A CA   1 
ATOM   1829 C  CA   B SER A 1 216 ? -20.066 -14.182 13.171  0.50 6.72  ? 217 SER A CA   1 
ATOM   1830 C  C    . SER A 1 216 ? -19.875 -13.721 11.732  1.00 7.17  ? 217 SER A C    1 
ATOM   1831 O  O    . SER A 1 216 ? -20.698 -12.960 11.170  1.00 9.76  ? 217 SER A O    1 
ATOM   1832 C  CB   A SER A 1 216 ? -21.261 -15.225 13.115  0.50 8.49  ? 217 SER A CB   1 
ATOM   1833 C  CB   B SER A 1 216 ? -21.118 -15.295 13.155  0.50 8.01  ? 217 SER A CB   1 
ATOM   1834 O  OG   A SER A 1 216 ? -20.855 -16.354 12.373  0.50 10.61 ? 217 SER A OG   1 
ATOM   1835 O  OG   B SER A 1 216 ? -21.206 -15.924 14.404  0.50 6.44  ? 217 SER A OG   1 
ATOM   1836 N  N    . VAL A 1 217 ? -18.778 -14.179 11.137  1.00 7.21  ? 218 VAL A N    1 
ATOM   1837 C  CA   . VAL A 1 217 ? -18.481 -13.959 9.746   1.00 7.29  ? 218 VAL A CA   1 
ATOM   1838 C  C    . VAL A 1 217 ? -18.211 -15.346 9.113   1.00 7.51  ? 218 VAL A C    1 
ATOM   1839 O  O    . VAL A 1 217 ? -17.874 -16.312 9.816   1.00 8.44  ? 218 VAL A O    1 
ATOM   1840 C  CB   . VAL A 1 217 ? -17.263 -13.051 9.534   1.00 9.19  ? 218 VAL A CB   1 
ATOM   1841 C  CG1  . VAL A 1 217 ? -17.541 -11.715 10.188  1.00 7.82  ? 218 VAL A CG1  1 
ATOM   1842 C  CG2  . VAL A 1 217 ? -15.967 -13.699 10.017  1.00 8.58  ? 218 VAL A CG2  1 
ATOM   1843 N  N    . SER A 1 218 ? -18.413 -15.474 7.813   1.00 8.06  ? 219 SER A N    1 
ATOM   1844 C  CA   . SER A 1 218 ? -18.136 -16.795 7.208   1.00 8.90  ? 219 SER A CA   1 
ATOM   1845 C  C    . SER A 1 218 ? -16.672 -17.081 6.974   1.00 7.70  ? 219 SER A C    1 
ATOM   1846 O  O    . SER A 1 218 ? -15.835 -16.176 6.817   1.00 7.72  ? 219 SER A O    1 
ATOM   1847 C  CB   . SER A 1 218 ? -18.959 -17.022 5.927   1.00 9.78  ? 219 SER A CB   1 
ATOM   1848 O  OG   . SER A 1 218 ? -18.458 -16.150 4.956   1.00 9.55  ? 219 SER A OG   1 
ATOM   1849 N  N    . SER A 1 219 ? -16.338 -18.362 6.838   1.00 7.82  ? 220 SER A N    1 
ATOM   1850 C  CA   A SER A 1 219 ? -15.004 -18.753 6.447   0.50 9.57  ? 220 SER A CA   1 
ATOM   1851 C  CA   B SER A 1 219 ? -14.995 -18.756 6.440   0.50 9.36  ? 220 SER A CA   1 
ATOM   1852 C  C    . SER A 1 219 ? -14.605 -18.061 5.099   1.00 9.54  ? 220 SER A C    1 
ATOM   1853 O  O    . SER A 1 219 ? -13.456 -17.561 4.967   1.00 10.32 ? 220 SER A O    1 
ATOM   1854 C  CB   A SER A 1 219 ? -14.917 -20.294 6.428   0.50 9.17  ? 220 SER A CB   1 
ATOM   1855 C  CB   B SER A 1 219 ? -14.856 -20.302 6.414   0.50 9.27  ? 220 SER A CB   1 
ATOM   1856 O  OG   A SER A 1 219 ? -15.830 -20.828 5.496   0.50 9.52  ? 220 SER A OG   1 
ATOM   1857 O  OG   B SER A 1 219 ? -13.501 -20.693 6.171   0.50 9.89  ? 220 SER A OG   1 
ATOM   1858 N  N    . GLU A 1 220 ? -15.548 -17.974 4.111   1.00 10.12 ? 221 GLU A N    1 
ATOM   1859 C  CA   . GLU A 1 220 ? -15.225 -17.366 2.804   1.00 11.04 ? 221 GLU A CA   1 
ATOM   1860 C  C    . GLU A 1 220 ? -14.935 -15.844 2.990   1.00 9.26  ? 221 GLU A C    1 
ATOM   1861 O  O    . GLU A 1 220 ? -13.988 -15.308 2.386   1.00 9.88  ? 221 GLU A O    1 
ATOM   1862 C  CB   . GLU A 1 220 ? -16.371 -17.521 1.886   1.00 14.12 ? 221 GLU A CB   1 
ATOM   1863 C  CG   . GLU A 1 220 ? -16.563 -19.056 1.576   1.00 17.94 ? 221 GLU A CG   1 
ATOM   1864 C  CD   . GLU A 1 220 ? -17.607 -19.783 2.450   1.00 25.91 ? 221 GLU A CD   1 
ATOM   1865 O  OE1  . GLU A 1 220 ? -18.103 -19.290 3.474   1.00 19.46 ? 221 GLU A OE1  1 
ATOM   1866 O  OE2  . GLU A 1 220 ? -17.910 -20.954 2.136   1.00 30.50 ? 221 GLU A OE2  1 
ATOM   1867 N  N    . GLN A 1 221 ? -15.662 -15.224 3.908   1.00 8.21  ? 222 GLN A N    1 
ATOM   1868 C  CA   . GLN A 1 221 ? -15.434 -13.779 4.178   1.00 8.04  ? 222 GLN A CA   1 
ATOM   1869 C  C    . GLN A 1 221 ? -13.999 -13.563 4.689   1.00 9.47  ? 222 GLN A C    1 
ATOM   1870 O  O    . GLN A 1 221 ? -13.233 -12.710 4.181   1.00 8.49  ? 222 GLN A O    1 
ATOM   1871 C  CB   . GLN A 1 221 ? -16.473 -13.241 5.182   1.00 9.51  ? 222 GLN A CB   1 
ATOM   1872 C  CG   . GLN A 1 221 ? -17.747 -12.967 4.417   1.00 10.41 ? 222 GLN A CG   1 
ATOM   1873 C  CD   . GLN A 1 221 ? -18.910 -12.504 5.274   1.00 7.55  ? 222 GLN A CD   1 
ATOM   1874 O  OE1  . GLN A 1 221 ? -19.054 -12.922 6.424   1.00 8.51  ? 222 GLN A OE1  1 
ATOM   1875 N  NE2  . GLN A 1 221 ? -19.750 -11.588 4.708   1.00 9.28  ? 222 GLN A NE2  1 
ATOM   1876 N  N    . VAL A 1 222 ? -13.600 -14.318 5.734   1.00 8.44  ? 223 VAL A N    1 
ATOM   1877 C  CA   . VAL A 1 222 ? -12.264 -14.076 6.315   1.00 9.98  ? 223 VAL A CA   1 
ATOM   1878 C  C    . VAL A 1 222 ? -11.098 -14.544 5.347   1.00 9.19  ? 223 VAL A C    1 
ATOM   1879 O  O    . VAL A 1 222 ? -10.014 -13.930 5.224   1.00 10.16 ? 223 VAL A O    1 
ATOM   1880 C  CB   . VAL A 1 222 ? -12.148 -14.646 7.757   1.00 11.67 ? 223 VAL A CB   1 
ATOM   1881 C  CG1  . VAL A 1 222 ? -12.197 -16.170 7.716   1.00 12.70 ? 223 VAL A CG1  1 
ATOM   1882 C  CG2  . VAL A 1 222 ? -10.848 -14.044 8.378   1.00 13.19 ? 223 VAL A CG2  1 
ATOM   1883 N  N    . LEU A 1 223 ? -11.452 -15.549 4.526   1.00 9.58  ? 224 LEU A N    1 
ATOM   1884 C  CA   . LEU A 1 223 ? -10.512 -16.012 3.496   1.00 11.30 ? 224 LEU A CA   1 
ATOM   1885 C  C    . LEU A 1 223 ? -10.141 -14.895 2.519   1.00 12.57 ? 224 LEU A C    1 
ATOM   1886 O  O    . LEU A 1 223 ? -8.979  -14.828 2.107   1.00 10.84 ? 224 LEU A O    1 
ATOM   1887 C  CB   . LEU A 1 223 ? -11.061 -17.242 2.764   1.00 12.11 ? 224 LEU A CB   1 
ATOM   1888 C  CG   . LEU A 1 223 ? -10.850 -18.464 3.654   1.00 15.34 ? 224 LEU A CG   1 
ATOM   1889 C  CD1  . LEU A 1 223 ? -11.813 -19.654 3.161   1.00 18.29 ? 224 LEU A CD1  1 
ATOM   1890 C  CD2  . LEU A 1 223 ? -9.389  -18.902 3.713   1.00 19.98 ? 224 LEU A CD2  1 
ATOM   1891 N  N    . LYS A 1 224 ? -11.111 -14.077 2.175   1.00 11.48 ? 225 LYS A N    1 
ATOM   1892 C  CA   . LYS A 1 224 ? -10.912 -12.919 1.319   1.00 12.40 ? 225 LYS A CA   1 
ATOM   1893 C  C    . LYS A 1 224 ? -10.027 -11.875 2.030   1.00 10.36 ? 225 LYS A C    1 
ATOM   1894 O  O    . LYS A 1 224 ? -9.251  -11.205 1.326   1.00 11.23 ? 225 LYS A O    1 
ATOM   1895 C  CB   . LYS A 1 224 ? -12.251 -12.373 0.782   1.00 10.94 ? 225 LYS A CB   1 
ATOM   1896 C  CG   . LYS A 1 224 ? -12.825 -13.463 -0.319  1.00 12.16 ? 225 LYS A CG   1 
ATOM   1897 C  CD   . LYS A 1 224 ? -14.161 -13.100 -0.927  1.00 19.07 ? 225 LYS A CD   1 
ATOM   1898 C  CE   . LYS A 1 224 ? -14.740 -14.248 -1.913  1.00 17.60 ? 225 LYS A CE   1 
ATOM   1899 N  NZ   . LYS A 1 224 ? -16.015 -13.849 -2.653  1.00 20.67 ? 225 LYS A NZ   1 
ATOM   1900 N  N    . PHE A 1 225 ? -10.168 -11.680 3.363   1.00 8.06  ? 226 PHE A N    1 
ATOM   1901 C  CA   . PHE A 1 225 ? -9.193  -10.783 4.041   1.00 7.43  ? 226 PHE A CA   1 
ATOM   1902 C  C    . PHE A 1 225 ? -7.800  -11.252 3.823   1.00 7.74  ? 226 PHE A C    1 
ATOM   1903 O  O    . PHE A 1 225 ? -6.848  -10.469 3.594   1.00 8.25  ? 226 PHE A O    1 
ATOM   1904 C  CB   . PHE A 1 225 ? -9.420  -10.760 5.580   1.00 7.00  ? 226 PHE A CB   1 
ATOM   1905 C  CG   . PHE A 1 225 ? -10.638 -9.962  6.061   1.00 8.46  ? 226 PHE A CG   1 
ATOM   1906 C  CD1  . PHE A 1 225 ? -11.660 -9.499  5.265   1.00 10.87 ? 226 PHE A CD1  1 
ATOM   1907 C  CD2  . PHE A 1 225 ? -10.734 -9.802  7.458   1.00 14.89 ? 226 PHE A CD2  1 
ATOM   1908 C  CE1  . PHE A 1 225 ? -12.716 -8.775  5.826   1.00 13.54 ? 226 PHE A CE1  1 
ATOM   1909 C  CE2  . PHE A 1 225 ? -11.766 -9.112  8.030   1.00 12.62 ? 226 PHE A CE2  1 
ATOM   1910 C  CZ   . PHE A 1 225 ? -12.762 -8.570  7.183   1.00 11.62 ? 226 PHE A CZ   1 
ATOM   1911 N  N    . ARG A 1 226 ? -7.614  -12.581 3.870   1.00 7.39  ? 227 ARG A N    1 
ATOM   1912 C  CA   . ARG A 1 226 ? -6.303  -13.170 3.787   1.00 10.25 ? 227 ARG A CA   1 
ATOM   1913 C  C    . ARG A 1 226 ? -5.665  -13.210 2.384   1.00 9.42  ? 227 ARG A C    1 
ATOM   1914 O  O    . ARG A 1 226 ? -4.497  -13.609 2.243   1.00 11.22 ? 227 ARG A O    1 
ATOM   1915 C  CB   . ARG A 1 226 ? -6.365  -14.602 4.343   1.00 10.56 ? 227 ARG A CB   1 
ATOM   1916 C  CG   . ARG A 1 226 ? -6.810  -14.709 5.840   1.00 7.62  ? 227 ARG A CG   1 
ATOM   1917 C  CD   . ARG A 1 226 ? -6.714  -16.224 6.324   1.00 8.48  ? 227 ARG A CD   1 
ATOM   1918 N  NE   . ARG A 1 226 ? -7.335  -16.319 7.664   1.00 7.91  ? 227 ARG A NE   1 
ATOM   1919 C  CZ   . ARG A 1 226 ? -8.295  -17.182 8.017   1.00 10.57 ? 227 ARG A CZ   1 
ATOM   1920 N  NH1  . ARG A 1 226 ? -8.636  -18.171 7.149   1.00 9.87  ? 227 ARG A NH1  1 
ATOM   1921 N  NH2  . ARG A 1 226 ? -8.763  -17.194 9.255   1.00 13.48 ? 227 ARG A NH2  1 
ATOM   1922 N  N    . LYS A 1 227 ? -6.395  -12.710 1.394   1.00 9.86  ? 228 LYS A N    1 
ATOM   1923 C  CA   . LYS A 1 227 ? -5.870  -12.628 0.046   1.00 11.42 ? 228 LYS A CA   1 
ATOM   1924 C  C    . LYS A 1 227 ? -5.228  -11.246 -0.174  1.00 11.60 ? 228 LYS A C    1 
ATOM   1925 O  O    . LYS A 1 227 ? -4.498  -11.020 -1.166  1.00 11.74 ? 228 LYS A O    1 
ATOM   1926 C  CB   . LYS A 1 227 ? -6.948  -12.843 -0.969  1.00 11.84 ? 228 LYS A CB   1 
ATOM   1927 C  CG   . LYS A 1 227 ? -7.322  -14.297 -1.137  1.00 15.80 ? 228 LYS A CG   1 
ATOM   1928 C  CD   . LYS A 1 227 ? -8.512  -14.485 -2.073  1.00 21.61 ? 228 LYS A CD   1 
ATOM   1929 C  CE   . LYS A 1 227 ? -8.155  -13.860 -3.443  1.00 25.53 ? 228 LYS A CE   1 
ATOM   1930 N  NZ   . LYS A 1 227 ? -8.603  -14.678 -4.602  1.00 32.05 ? 228 LYS A NZ   1 
ATOM   1931 N  N    . LEU A 1 228 ? -5.501  -10.325 0.735   1.00 11.54 ? 229 LEU A N    1 
ATOM   1932 C  CA   . LEU A 1 228 ? -4.780  -9.053  0.662   1.00 10.71 ? 229 LEU A CA   1 
ATOM   1933 C  C    . LEU A 1 228 ? -3.270  -9.181  0.811   1.00 10.49 ? 229 LEU A C    1 
ATOM   1934 O  O    . LEU A 1 228 ? -2.714  -10.203 1.264   1.00 9.13  ? 229 LEU A O    1 
ATOM   1935 C  CB   . LEU A 1 228 ? -5.280  -8.108  1.766   1.00 7.26  ? 229 LEU A CB   1 
ATOM   1936 C  CG   . LEU A 1 228 ? -6.702  -7.658  1.583   1.00 10.02 ? 229 LEU A CG   1 
ATOM   1937 C  CD1  . LEU A 1 228 ? -7.193  -7.075  2.878   1.00 12.67 ? 229 LEU A CD1  1 
ATOM   1938 C  CD2  . LEU A 1 228 ? -6.763  -6.570  0.469   1.00 10.35 ? 229 LEU A CD2  1 
ATOM   1939 N  N    . ASN A 1 229 ? -2.573  -8.097  0.431   1.00 12.85 ? 230 ASN A N    1 
ATOM   1940 C  CA   . ASN A 1 229 ? -1.130  -8.153  0.392   1.00 10.66 ? 230 ASN A CA   1 
ATOM   1941 C  C    . ASN A 1 229 ? -0.525  -7.021  1.286   1.00 11.26 ? 230 ASN A C    1 
ATOM   1942 O  O    . ASN A 1 229 ? -1.066  -5.923  1.222   1.00 9.67  ? 230 ASN A O    1 
ATOM   1943 C  CB   . ASN A 1 229 ? -0.644  -7.863  -1.046  1.00 13.10 ? 230 ASN A CB   1 
ATOM   1944 C  CG   . ASN A 1 229 ? -0.638  -9.082  -1.964  1.00 17.24 ? 230 ASN A CG   1 
ATOM   1945 O  OD1  . ASN A 1 229 ? -0.048  -8.970  -3.061  1.00 15.49 ? 230 ASN A OD1  1 
ATOM   1946 N  ND2  . ASN A 1 229 ? -1.227  -10.225 -1.552  1.00 12.88 ? 230 ASN A ND2  1 
ATOM   1947 N  N    . PHE A 1 230 ? 0.532   -7.348  2.065   1.00 11.17 ? 231 PHE A N    1 
ATOM   1948 C  CA   . PHE A 1 230 ? 1.366   -6.321  2.765   1.00 10.14 ? 231 PHE A CA   1 
ATOM   1949 C  C    . PHE A 1 230 ? 2.226   -5.509  1.787   1.00 14.36 ? 231 PHE A C    1 
ATOM   1950 O  O    . PHE A 1 230 ? 2.481   -4.293  2.043   1.00 13.64 ? 231 PHE A O    1 
ATOM   1951 C  CB   . PHE A 1 230 ? 2.326   -6.904  3.729   1.00 12.79 ? 231 PHE A CB   1 
ATOM   1952 C  CG   . PHE A 1 230 ? 1.715   -7.427  5.030   1.00 11.72 ? 231 PHE A CG   1 
ATOM   1953 C  CD1  . PHE A 1 230 ? 0.853   -6.611  5.835   1.00 10.07 ? 231 PHE A CD1  1 
ATOM   1954 C  CD2  . PHE A 1 230 ? 2.036   -8.726  5.425   1.00 11.86 ? 231 PHE A CD2  1 
ATOM   1955 C  CE1  . PHE A 1 230 ? 0.312   -7.171  7.094   1.00 12.28 ? 231 PHE A CE1  1 
ATOM   1956 C  CE2  . PHE A 1 230 ? 1.600   -9.281  6.646   1.00 12.88 ? 231 PHE A CE2  1 
ATOM   1957 C  CZ   . PHE A 1 230 ? 0.717   -8.488  7.496   1.00 10.72 ? 231 PHE A CZ   1 
ATOM   1958 N  N    . ASN A 1 231 ? 2.631   -6.175  0.715   1.00 14.47 ? 232 ASN A N    1 
ATOM   1959 C  CA   . ASN A 1 231 ? 3.542   -5.528  -0.274  1.00 15.83 ? 232 ASN A CA   1 
ATOM   1960 C  C    . ASN A 1 231 ? 2.798   -4.577  -1.213  1.00 14.57 ? 232 ASN A C    1 
ATOM   1961 O  O    . ASN A 1 231 ? 1.556   -4.666  -1.435  1.00 12.74 ? 232 ASN A O    1 
ATOM   1962 C  CB   . ASN A 1 231 ? 4.195   -6.659  -1.074  1.00 15.63 ? 232 ASN A CB   1 
ATOM   1963 C  CG   . ASN A 1 231 ? 3.162   -7.534  -1.704  1.00 14.31 ? 232 ASN A CG   1 
ATOM   1964 O  OD1  . ASN A 1 231 ? 2.528   -8.329  -1.019  1.00 18.69 ? 232 ASN A OD1  1 
ATOM   1965 N  ND2  . ASN A 1 231 ? 2.944   -7.392  -3.015  1.00 17.29 ? 232 ASN A ND2  1 
ATOM   1966 N  N    . GLY A 1 232 ? 3.555   -3.653  -1.840  1.00 14.88 ? 233 GLY A N    1 
ATOM   1967 C  CA   . GLY A 1 232 ? 3.050   -2.887  -3.001  1.00 16.96 ? 233 GLY A CA   1 
ATOM   1968 C  C    . GLY A 1 232 ? 3.025   -3.688  -4.286  1.00 17.71 ? 233 GLY A C    1 
ATOM   1969 O  O    . GLY A 1 232 ? 3.714   -4.691  -4.363  1.00 18.16 ? 233 GLY A O    1 
ATOM   1970 N  N    . GLU A 1 233 ? 2.215   -3.213  -5.251  1.00 19.21 ? 234 GLU A N    1 
ATOM   1971 C  CA   . GLU A 1 233 ? 2.136   -3.731  -6.619  1.00 18.26 ? 234 GLU A CA   1 
ATOM   1972 C  C    . GLU A 1 233 ? 3.547   -3.831  -7.234  1.00 19.27 ? 234 GLU A C    1 
ATOM   1973 O  O    . GLU A 1 233 ? 4.399   -2.926  -7.113  1.00 18.74 ? 234 GLU A O    1 
ATOM   1974 C  CB   . GLU A 1 233 ? 1.278   -2.839  -7.499  1.00 17.86 ? 234 GLU A CB   1 
ATOM   1975 C  CG   . GLU A 1 233 ? 1.027   -3.436  -8.868  1.00 18.16 ? 234 GLU A CG   1 
ATOM   1976 C  CD   . GLU A 1 233 ? 0.177   -2.551  -9.679  1.00 25.18 ? 234 GLU A CD   1 
ATOM   1977 O  OE1  . GLU A 1 233 ? -0.137  -1.385  -9.215  1.00 26.85 ? 234 GLU A OE1  1 
ATOM   1978 O  OE2  . GLU A 1 233 ? -0.113  -2.980  -10.825 1.00 25.51 ? 234 GLU A OE2  1 
ATOM   1979 N  N    . GLY A 1 234 ? 3.752   -4.943  -7.938  1.00 20.05 ? 235 GLY A N    1 
ATOM   1980 C  CA   . GLY A 1 234 ? 5.054   -5.252  -8.473  1.00 23.14 ? 235 GLY A CA   1 
ATOM   1981 C  C    . GLY A 1 234 ? 6.143   -5.629  -7.510  1.00 22.93 ? 235 GLY A C    1 
ATOM   1982 O  O    . GLY A 1 234 ? 7.329   -5.625  -7.895  1.00 25.28 ? 235 GLY A O    1 
ATOM   1983 N  N    . GLU A 1 235 ? 5.789   -5.937  -6.250  1.00 23.04 ? 236 GLU A N    1 
ATOM   1984 C  CA   . GLU A 1 235 ? 6.745   -6.519  -5.264  1.00 22.37 ? 236 GLU A CA   1 
ATOM   1985 C  C    . GLU A 1 235 ? 6.335   -7.965  -4.972  1.00 23.54 ? 236 GLU A C    1 
ATOM   1986 O  O    . GLU A 1 235 ? 5.239   -8.360  -5.373  1.00 23.87 ? 236 GLU A O    1 
ATOM   1987 C  CB   . GLU A 1 235 ? 6.774   -5.713  -3.943  1.00 23.61 ? 236 GLU A CB   1 
ATOM   1988 C  CG   . GLU A 1 235 ? 7.162   -4.277  -4.187  1.00 24.18 ? 236 GLU A CG   1 
ATOM   1989 C  CD   . GLU A 1 235 ? 6.889   -3.383  -3.024  1.00 30.24 ? 236 GLU A CD   1 
ATOM   1990 O  OE1  . GLU A 1 235 ? 6.240   -3.830  -2.036  1.00 28.45 ? 236 GLU A OE1  1 
ATOM   1991 O  OE2  . GLU A 1 235 ? 7.311   -2.216  -3.093  1.00 27.99 ? 236 GLU A OE2  1 
ATOM   1992 N  N    . PRO A 1 236 ? 7.240   -8.750  -4.368  1.00 23.31 ? 237 PRO A N    1 
ATOM   1993 C  CA   . PRO A 1 236 ? 7.006   -10.187 -4.131  1.00 23.47 ? 237 PRO A CA   1 
ATOM   1994 C  C    . PRO A 1 236 ? 5.850   -10.260 -3.115  1.00 22.12 ? 237 PRO A C    1 
ATOM   1995 O  O    . PRO A 1 236 ? 5.746   -9.375  -2.234  1.00 19.40 ? 237 PRO A O    1 
ATOM   1996 C  CB   . PRO A 1 236 ? 8.317   -10.671 -3.518  1.00 23.88 ? 237 PRO A CB   1 
ATOM   1997 C  CG   . PRO A 1 236 ? 9.370   -9.577  -3.964  1.00 25.62 ? 237 PRO A CG   1 
ATOM   1998 C  CD   . PRO A 1 236 ? 8.563   -8.326  -3.850  1.00 25.15 ? 237 PRO A CD   1 
ATOM   1999 N  N    . GLU A 1 237 ? 4.993   -11.260 -3.328  1.00 20.92 ? 238 GLU A N    1 
ATOM   2000 C  CA   . GLU A 1 237 ? 3.765   -11.312 -2.585  1.00 18.63 ? 238 GLU A CA   1 
ATOM   2001 C  C    . GLU A 1 237 ? 4.034   -11.759 -1.146  1.00 18.30 ? 238 GLU A C    1 
ATOM   2002 O  O    . GLU A 1 237 ? 4.620   -12.826 -0.879  1.00 17.47 ? 238 GLU A O    1 
ATOM   2003 C  CB   . GLU A 1 237 ? 2.730   -12.211 -3.251  1.00 19.29 ? 238 GLU A CB   1 
ATOM   2004 C  CG   . GLU A 1 237 ? 1.421   -12.089 -2.615  1.00 18.94 ? 238 GLU A CG   1 
ATOM   2005 C  CD   . GLU A 1 237 ? 0.364   -12.875 -3.307  1.00 21.80 ? 238 GLU A CD   1 
ATOM   2006 O  OE1  . GLU A 1 237 ? 0.784   -13.890 -3.940  1.00 28.01 ? 238 GLU A OE1  1 
ATOM   2007 O  OE2  . GLU A 1 237 ? -0.836  -12.464 -3.314  1.00 17.55 ? 238 GLU A OE2  1 
ATOM   2008 N  N    . GLU A 1 238 ? 3.478   -10.948 -0.237  1.00 17.00 ? 239 GLU A N    1 
ATOM   2009 C  CA   . GLU A 1 238 ? 3.481   -11.225 1.196   1.00 18.19 ? 239 GLU A CA   1 
ATOM   2010 C  C    . GLU A 1 238 ? 2.019   -11.132 1.610   1.00 13.30 ? 239 GLU A C    1 
ATOM   2011 O  O    . GLU A 1 238 ? 1.463   -10.050 1.602   1.00 13.70 ? 239 GLU A O    1 
ATOM   2012 C  CB   . GLU A 1 238 ? 4.276   -10.143 1.972   1.00 15.65 ? 239 GLU A CB   1 
ATOM   2013 C  CG   . GLU A 1 238 ? 5.473   -9.620  1.258   1.00 22.83 ? 239 GLU A CG   1 
ATOM   2014 C  CD   . GLU A 1 238 ? 6.267   -8.550  2.033   1.00 24.48 ? 239 GLU A CD   1 
ATOM   2015 O  OE1  . GLU A 1 238 ? 5.675   -7.628  2.635   1.00 31.60 ? 239 GLU A OE1  1 
ATOM   2016 O  OE2  . GLU A 1 238 ? 7.527   -8.675  2.037   1.00 35.16 ? 239 GLU A OE2  1 
ATOM   2017 N  N    . LEU A 1 239 ? 1.363   -12.269 1.896   1.00 10.67 ? 240 LEU A N    1 
ATOM   2018 C  CA   . LEU A 1 239 ? -0.042  -12.155 2.264   1.00 8.17  ? 240 LEU A CA   1 
ATOM   2019 C  C    . LEU A 1 239 ? -0.218  -11.319 3.554   1.00 6.84  ? 240 LEU A C    1 
ATOM   2020 O  O    . LEU A 1 239 ? 0.525   -11.525 4.534   1.00 10.01 ? 240 LEU A O    1 
ATOM   2021 C  CB   . LEU A 1 239 ? -0.629  -13.573 2.538   1.00 9.57  ? 240 LEU A CB   1 
ATOM   2022 C  CG   . LEU A 1 239 ? -0.766  -14.434 1.275   1.00 8.77  ? 240 LEU A CG   1 
ATOM   2023 C  CD1  . LEU A 1 239 ? -1.341  -15.819 1.693   1.00 16.20 ? 240 LEU A CD1  1 
ATOM   2024 C  CD2  . LEU A 1 239 ? -1.496  -13.796 0.096   1.00 11.77 ? 240 LEU A CD2  1 
ATOM   2025 N  N    . MET A 1 240 ? -1.323  -10.580 3.535   1.00 9.79  ? 241 MET A N    1 
ATOM   2026 C  CA   . MET A 1 240 ? -1.761  -9.752  4.688   1.00 9.56  ? 241 MET A CA   1 
ATOM   2027 C  C    . MET A 1 240 ? -2.523  -10.661 5.632   1.00 7.84  ? 241 MET A C    1 
ATOM   2028 O  O    . MET A 1 240 ? -3.716  -10.812 5.534   1.00 9.71  ? 241 MET A O    1 
ATOM   2029 C  CB   . MET A 1 240 ? -2.563  -8.548  4.271   1.00 11.01 ? 241 MET A CB   1 
ATOM   2030 C  CG   . MET A 1 240 ? -2.835  -7.486  5.489   1.00 10.20 ? 241 MET A CG   1 
ATOM   2031 S  SD   . MET A 1 240 ? -3.826  -6.137  4.923   1.00 13.29 ? 241 MET A SD   1 
ATOM   2032 C  CE   . MET A 1 240 ? -2.580  -4.999  4.193   1.00 14.32 ? 241 MET A CE   1 
ATOM   2033 N  N    . VAL A 1 241 ? -1.705  -11.290 6.484   1.00 7.43  ? 242 VAL A N    1 
ATOM   2034 C  CA   . VAL A 1 241 ? -2.256  -12.197 7.587   1.00 6.75  ? 242 VAL A CA   1 
ATOM   2035 C  C    . VAL A 1 241 ? -1.489  -11.931 8.866   1.00 8.44  ? 242 VAL A C    1 
ATOM   2036 O  O    . VAL A 1 241 ? -0.292  -11.455 8.811   1.00 8.79  ? 242 VAL A O    1 
ATOM   2037 C  CB   . VAL A 1 241 ? -2.182  -13.700 7.189   1.00 5.68  ? 242 VAL A CB   1 
ATOM   2038 C  CG1  . VAL A 1 241 ? -3.012  -13.944 5.908   1.00 8.20  ? 242 VAL A CG1  1 
ATOM   2039 C  CG2  . VAL A 1 241 ? -0.715  -14.137 7.143   1.00 8.26  ? 242 VAL A CG2  1 
ATOM   2040 N  N    . ASP A 1 242 ? -2.130  -12.206 10.028  1.00 5.60  ? 243 ASP A N    1 
ATOM   2041 C  CA   . ASP A 1 242 ? -1.444  -12.029 11.294  1.00 6.61  ? 243 ASP A CA   1 
ATOM   2042 C  C    . ASP A 1 242 ? -0.956  -10.604 11.488  1.00 5.81  ? 243 ASP A C    1 
ATOM   2043 O  O    . ASP A 1 242 ? 0.163   -10.367 12.025  1.00 9.89  ? 243 ASP A O    1 
ATOM   2044 C  CB   . ASP A 1 242 ? -0.347  -13.088 11.608  1.00 5.99  ? 243 ASP A CB   1 
ATOM   2045 C  CG   . ASP A 1 242 ? -0.911  -14.502 11.637  1.00 9.16  ? 243 ASP A CG   1 
ATOM   2046 O  OD1  . ASP A 1 242 ? -2.004  -14.678 12.220  1.00 7.99  ? 243 ASP A OD1  1 
ATOM   2047 O  OD2  . ASP A 1 242 ? -0.312  -15.458 11.005  1.00 9.17  ? 243 ASP A OD2  1 
ATOM   2048 N  N    . ASN A 1 243 ? -1.849  -9.670  11.193  1.00 6.65  ? 244 ASN A N    1 
ATOM   2049 C  CA   . ASN A 1 243 ? -1.563  -8.274  11.455  1.00 7.13  ? 244 ASN A CA   1 
ATOM   2050 C  C    . ASN A 1 243 ? -2.171  -7.838  12.832  1.00 6.28  ? 244 ASN A C    1 
ATOM   2051 O  O    . ASN A 1 243 ? -2.841  -6.740  12.875  1.00 6.67  ? 244 ASN A O    1 
ATOM   2052 C  CB   . ASN A 1 243 ? -2.084  -7.400  10.275  1.00 7.59  ? 244 ASN A CB   1 
ATOM   2053 C  CG   . ASN A 1 243 ? -3.580  -7.507  10.038  1.00 7.55  ? 244 ASN A CG   1 
ATOM   2054 O  OD1  . ASN A 1 243 ? -4.252  -8.338  10.720  1.00 8.43  ? 244 ASN A OD1  1 
ATOM   2055 N  ND2  . ASN A 1 243 ? -4.143  -6.627  9.164   1.00 10.52 ? 244 ASN A ND2  1 
ATOM   2056 N  N    . TRP A 1 244 ? -1.925  -8.631  13.858  1.00 5.99  ? 245 TRP A N    1 
ATOM   2057 C  CA   . TRP A 1 244 ? -2.373  -8.357  15.219  1.00 5.26  ? 245 TRP A CA   1 
ATOM   2058 C  C    . TRP A 1 244 ? -1.187  -8.217  16.136  1.00 7.48  ? 245 TRP A C    1 
ATOM   2059 O  O    . TRP A 1 244 ? -0.141  -8.920  15.955  1.00 6.30  ? 245 TRP A O    1 
ATOM   2060 C  CB   . TRP A 1 244 ? -3.348  -9.464  15.692  1.00 5.81  ? 245 TRP A CB   1 
ATOM   2061 C  CG   . TRP A 1 244 ? -2.829  -10.849 15.505  1.00 4.87  ? 245 TRP A CG   1 
ATOM   2062 C  CD1  . TRP A 1 244 ? -2.963  -11.610 14.366  1.00 5.94  ? 245 TRP A CD1  1 
ATOM   2063 C  CD2  . TRP A 1 244 ? -2.303  -11.706 16.511  1.00 6.84  ? 245 TRP A CD2  1 
ATOM   2064 N  NE1  . TRP A 1 244 ? -2.437  -12.892 14.609  1.00 6.02  ? 245 TRP A NE1  1 
ATOM   2065 C  CE2  . TRP A 1 244 ? -2.049  -12.951 15.912  1.00 6.99  ? 245 TRP A CE2  1 
ATOM   2066 C  CE3  . TRP A 1 244 ? -2.027  -11.545 17.881  1.00 8.48  ? 245 TRP A CE3  1 
ATOM   2067 C  CZ2  . TRP A 1 244 ? -1.431  -14.015 16.623  1.00 7.58  ? 245 TRP A CZ2  1 
ATOM   2068 C  CZ3  . TRP A 1 244 ? -1.411  -12.634 18.593  1.00 8.05  ? 245 TRP A CZ3  1 
ATOM   2069 C  CH2  . TRP A 1 244 ? -1.182  -13.813 17.960  1.00 7.61  ? 245 TRP A CH2  1 
ATOM   2070 N  N    . ARG A 1 245 ? -1.297  -7.281  17.118  1.00 5.28  ? 246 ARG A N    1 
ATOM   2071 C  CA   . ARG A 1 245 ? -0.373  -7.185  18.209  1.00 6.79  ? 246 ARG A CA   1 
ATOM   2072 C  C    . ARG A 1 245 ? -0.883  -8.128  19.339  1.00 6.02  ? 246 ARG A C    1 
ATOM   2073 O  O    . ARG A 1 245 ? -2.062  -8.171  19.688  1.00 7.91  ? 246 ARG A O    1 
ATOM   2074 C  CB   . ARG A 1 245 ? -0.406  -5.739  18.693  1.00 6.05  ? 246 ARG A CB   1 
ATOM   2075 C  CG   . ARG A 1 245 ? 0.719   -5.513  19.735  1.00 3.69  ? 246 ARG A CG   1 
ATOM   2076 C  CD   . ARG A 1 245 ? 0.731   -4.104  20.334  1.00 7.03  ? 246 ARG A CD   1 
ATOM   2077 N  NE   . ARG A 1 245 ? 2.046   -3.822  21.047  1.00 9.43  ? 246 ARG A NE   1 
ATOM   2078 C  CZ   . ARG A 1 245 ? 2.247   -2.802  21.902  1.00 10.06 ? 246 ARG A CZ   1 
ATOM   2079 N  NH1  . ARG A 1 245 ? 1.214   -1.984  22.267  1.00 6.05  ? 246 ARG A NH1  1 
ATOM   2080 N  NH2  . ARG A 1 245 ? 3.471   -2.583  22.379  1.00 10.08 ? 246 ARG A NH2  1 
ATOM   2081 N  N    . PRO A 1 246 ? 0.003   -8.887  19.974  1.00 7.35  ? 247 PRO A N    1 
ATOM   2082 C  CA   . PRO A 1 246 ? -0.393  -9.758  21.082  1.00 7.12  ? 247 PRO A CA   1 
ATOM   2083 C  C    . PRO A 1 246 ? -0.698  -8.931  22.312  1.00 5.77  ? 247 PRO A C    1 
ATOM   2084 O  O    . PRO A 1 246 ? -0.300  -7.751  22.418  1.00 7.64  ? 247 PRO A O    1 
ATOM   2085 C  CB   . PRO A 1 246 ? 0.879   -10.587 21.393  1.00 8.43  ? 247 PRO A CB   1 
ATOM   2086 C  CG   . PRO A 1 246 ? 1.861   -10.101 20.445  1.00 12.07 ? 247 PRO A CG   1 
ATOM   2087 C  CD   . PRO A 1 246 ? 1.464   -8.963  19.672  1.00 8.47  ? 247 PRO A CD   1 
ATOM   2088 N  N    . ALA A 1 247 ? -1.365  -9.595  23.244  1.00 6.41  ? 248 ALA A N    1 
ATOM   2089 C  CA   . ALA A 1 247 ? -1.730  -8.989  24.538  1.00 5.74  ? 248 ALA A CA   1 
ATOM   2090 C  C    . ALA A 1 247 ? -0.478  -8.395  25.237  1.00 5.51  ? 248 ALA A C    1 
ATOM   2091 O  O    . ALA A 1 247 ? 0.576   -9.103  25.295  1.00 7.64  ? 248 ALA A O    1 
ATOM   2092 C  CB   . ALA A 1 247 ? -2.490  -10.069 25.401  1.00 9.05  ? 248 ALA A CB   1 
ATOM   2093 N  N    . GLN A 1 248 ? -0.635  -7.217  25.829  1.00 5.50  ? 249 GLN A N    1 
ATOM   2094 C  CA   . GLN A 1 248 ? 0.451   -6.514  26.527  1.00 6.80  ? 249 GLN A CA   1 
ATOM   2095 C  C    . GLN A 1 248 ? 0.128   -6.481  28.024  1.00 8.51  ? 249 GLN A C    1 
ATOM   2096 O  O    . GLN A 1 248 ? -1.040  -6.681  28.451  1.00 7.69  ? 249 GLN A O    1 
ATOM   2097 C  CB   . GLN A 1 248 ? 0.449   -5.105  26.004  1.00 8.20  ? 249 GLN A CB   1 
ATOM   2098 C  CG   . GLN A 1 248 ? 0.765   -5.073  24.518  1.00 4.95  ? 249 GLN A CG   1 
ATOM   2099 C  CD   . GLN A 1 248 ? 2.128   -5.658  24.183  1.00 10.83 ? 249 GLN A CD   1 
ATOM   2100 O  OE1  . GLN A 1 248 ? 3.154   -5.301  24.781  1.00 12.67 ? 249 GLN A OE1  1 
ATOM   2101 N  NE2  . GLN A 1 248 ? 2.120   -6.652  23.273  1.00 10.96 ? 249 GLN A NE2  1 
ATOM   2102 N  N    . PRO A 1 249 ? 1.109   -6.192  28.866  1.00 9.39  ? 250 PRO A N    1 
ATOM   2103 C  CA   . PRO A 1 249 ? 0.903   -6.222  30.318  1.00 10.36 ? 250 PRO A CA   1 
ATOM   2104 C  C    . PRO A 1 249 ? -0.190  -5.239  30.753  1.00 8.66  ? 250 PRO A C    1 
ATOM   2105 O  O    . PRO A 1 249 ? -0.176  -4.040  30.346  1.00 9.43  ? 250 PRO A O    1 
ATOM   2106 C  CB   . PRO A 1 249 ? 2.301   -5.761  30.872  1.00 11.64 ? 250 PRO A CB   1 
ATOM   2107 C  CG   . PRO A 1 249 ? 3.266   -6.141  29.823  1.00 13.89 ? 250 PRO A CG   1 
ATOM   2108 C  CD   . PRO A 1 249 ? 2.545   -6.017  28.471  1.00 9.57  ? 250 PRO A CD   1 
ATOM   2109 N  N    . LEU A 1 250 ? -1.061  -5.743  31.643  1.00 9.37  ? 251 LEU A N    1 
ATOM   2110 C  CA   . LEU A 1 250 ? -2.199  -4.923  32.120  1.00 9.76  ? 251 LEU A CA   1 
ATOM   2111 C  C    . LEU A 1 250 ? -1.623  -3.803  33.066  1.00 9.44  ? 251 LEU A C    1 
ATOM   2112 O  O    . LEU A 1 250 ? -2.196  -2.668  33.142  1.00 8.19  ? 251 LEU A O    1 
ATOM   2113 C  CB   . LEU A 1 250 ? -3.177  -5.774  32.881  1.00 9.36  ? 251 LEU A CB   1 
ATOM   2114 C  CG   . LEU A 1 250 ? -4.463  -5.018  33.348  1.00 10.37 ? 251 LEU A CG   1 
ATOM   2115 C  CD1  . LEU A 1 250 ? -5.213  -4.416  32.153  1.00 9.73  ? 251 LEU A CD1  1 
ATOM   2116 C  CD2  . LEU A 1 250 ? -5.403  -5.995  34.206  1.00 14.52 ? 251 LEU A CD2  1 
ATOM   2117 N  N    . LYS A 1 251 ? -0.524  -4.141  33.792  1.00 11.17 ? 252 LYS A N    1 
ATOM   2118 C  CA   . LYS A 1 251 ? 0.117   -3.065  34.685  1.00 10.65 ? 252 LYS A CA   1 
ATOM   2119 C  C    . LYS A 1 251 ? -0.969  -2.584  35.686  1.00 11.77 ? 252 LYS A C    1 
ATOM   2120 O  O    . LYS A 1 251 ? -1.738  -3.421  36.166  1.00 14.01 ? 252 LYS A O    1 
ATOM   2121 C  CB   . LYS A 1 251 ? 0.804   -1.989  33.829  1.00 11.88 ? 252 LYS A CB   1 
ATOM   2122 C  CG   . LYS A 1 251 ? 2.093   -2.681  33.236  1.00 14.77 ? 252 LYS A CG   1 
ATOM   2123 C  CD   . LYS A 1 251 ? 2.937   -1.776  32.488  1.00 19.75 ? 252 LYS A CD   1 
ATOM   2124 C  CE   . LYS A 1 251 ? 4.038   -2.578  31.912  1.00 22.14 ? 252 LYS A CE   1 
ATOM   2125 N  NZ   . LYS A 1 251 ? 4.755   -1.688  31.027  1.00 25.00 ? 252 LYS A NZ   1 
ATOM   2126 N  N    A ASN A 1 252 ? -1.130  -1.336  36.083  0.50 12.97 ? 253 ASN A N    1 
ATOM   2127 N  N    B ASN A 1 252 ? -0.988  -1.257  35.822  0.50 11.31 ? 253 ASN A N    1 
ATOM   2128 C  CA   A ASN A 1 252 ? -2.008  -1.201  37.322  0.50 14.86 ? 253 ASN A CA   1 
ATOM   2129 C  CA   B ASN A 1 252 ? -1.767  -0.589  36.821  0.50 12.93 ? 253 ASN A CA   1 
ATOM   2130 C  C    A ASN A 1 252 ? -3.580  -1.256  37.060  0.50 14.05 ? 253 ASN A C    1 
ATOM   2131 C  C    B ASN A 1 252 ? -3.102  -0.225  36.265  0.50 13.72 ? 253 ASN A C    1 
ATOM   2132 O  O    A ASN A 1 252 ? -4.479  -1.370  37.952  0.50 14.86 ? 253 ASN A O    1 
ATOM   2133 O  O    B ASN A 1 252 ? -3.356  1.026   36.227  0.50 14.23 ? 253 ASN A O    1 
ATOM   2134 C  CB   A ASN A 1 252 ? -1.530  -0.005  38.182  0.50 15.82 ? 253 ASN A CB   1 
ATOM   2135 C  CB   B ASN A 1 252 ? -1.063  0.717   37.235  0.50 13.55 ? 253 ASN A CB   1 
ATOM   2136 C  CG   A ASN A 1 252 ? -2.423  0.259   39.368  0.50 19.02 ? 253 ASN A CG   1 
ATOM   2137 C  CG   B ASN A 1 252 ? -1.483  1.195   38.618  0.50 14.71 ? 253 ASN A CG   1 
ATOM   2138 O  OD1  A ASN A 1 252 ? -2.710  1.414   39.698  0.50 25.66 ? 253 ASN A OD1  1 
ATOM   2139 O  OD1  B ASN A 1 252 ? -1.938  2.334   38.776  0.50 26.14 ? 253 ASN A OD1  1 
ATOM   2140 N  ND2  A ASN A 1 252 ? -2.857  -0.809  40.038  0.50 22.00 ? 253 ASN A ND2  1 
ATOM   2141 N  ND2  B ASN A 1 252 ? -1.290  0.346   39.634  0.50 23.96 ? 253 ASN A ND2  1 
ATOM   2142 N  N    . ARG A 1 253 ? -3.885  -1.252  35.772  1.00 13.28 ? 254 ARG A N    1 
ATOM   2143 C  CA   . ARG A 1 253 ? -5.187  -0.944  35.256  1.00 10.58 ? 254 ARG A CA   1 
ATOM   2144 C  C    . ARG A 1 253 ? -6.285  -1.907  35.616  1.00 10.70 ? 254 ARG A C    1 
ATOM   2145 O  O    . ARG A 1 253 ? -6.056  -3.091  35.784  1.00 12.82 ? 254 ARG A O    1 
ATOM   2146 C  CB   . ARG A 1 253 ? -5.160  -0.823  33.700  1.00 10.20 ? 254 ARG A CB   1 
ATOM   2147 C  CG   . ARG A 1 253 ? -4.164  0.274   33.201  1.00 7.19  ? 254 ARG A CG   1 
ATOM   2148 C  CD   . ARG A 1 253 ? -4.052  0.213   31.668  1.00 9.45  ? 254 ARG A CD   1 
ATOM   2149 N  NE   . ARG A 1 253 ? -3.205  -0.959  31.230  1.00 7.38  ? 254 ARG A NE   1 
ATOM   2150 C  CZ   . ARG A 1 253 ? -3.032  -1.270  29.930  1.00 5.34  ? 254 ARG A CZ   1 
ATOM   2151 N  NH1  . ARG A 1 253 ? -3.611  -0.504  28.962  1.00 5.35  ? 254 ARG A NH1  1 
ATOM   2152 N  NH2  . ARG A 1 253 ? -2.177  -2.259  29.602  1.00 6.71  ? 254 ARG A NH2  1 
ATOM   2153 N  N    A GLN A 1 254 ? -7.476  -1.357  35.661  0.50 9.95  ? 255 GLN A N    1 
ATOM   2154 N  N    B GLN A 1 254 ? -7.495  -1.388  35.729  0.50 10.17 ? 255 GLN A N    1 
ATOM   2155 C  CA   A GLN A 1 254 ? -8.677  -2.096  35.929  0.50 10.72 ? 255 GLN A CA   1 
ATOM   2156 C  CA   B GLN A 1 254 ? -8.674  -2.199  36.032  0.50 11.27 ? 255 GLN A CA   1 
ATOM   2157 C  C    A GLN A 1 254 ? -9.437  -2.179  34.597  0.50 9.33  ? 255 GLN A C    1 
ATOM   2158 C  C    B GLN A 1 254 ? -9.607  -2.192  34.801  0.50 9.97  ? 255 GLN A C    1 
ATOM   2159 O  O    A GLN A 1 254 ? -9.541  -1.143  33.822  0.50 9.04  ? 255 GLN A O    1 
ATOM   2160 O  O    B GLN A 1 254 ? -10.008 -1.119  34.299  0.50 11.04 ? 255 GLN A O    1 
ATOM   2161 C  CB   A GLN A 1 254 ? -9.504  -1.373  36.979  0.50 11.40 ? 255 GLN A CB   1 
ATOM   2162 C  CB   B GLN A 1 254 ? -9.445  -1.664  37.232  0.50 10.97 ? 255 GLN A CB   1 
ATOM   2163 C  CG   A GLN A 1 254 ? -9.100  -1.707  38.432  0.50 15.14 ? 255 GLN A CG   1 
ATOM   2164 C  CG   B GLN A 1 254 ? -8.593  -1.193  38.467  0.50 12.68 ? 255 GLN A CG   1 
ATOM   2165 C  CD   A GLN A 1 254 ? -9.851  -2.891  38.966  0.50 20.55 ? 255 GLN A CD   1 
ATOM   2166 C  CD   B GLN A 1 254 ? -9.452  -1.129  39.771  0.50 15.44 ? 255 GLN A CD   1 
ATOM   2167 O  OE1  A GLN A 1 254 ? -10.400 -3.673  38.183  0.50 23.70 ? 255 GLN A OE1  1 
ATOM   2168 O  OE1  B GLN A 1 254 ? -10.694 -1.051  39.705  0.50 22.71 ? 255 GLN A OE1  1 
ATOM   2169 N  NE2  A GLN A 1 254 ? -9.885  -3.052  40.318  0.50 22.57 ? 255 GLN A NE2  1 
ATOM   2170 N  NE2  B GLN A 1 254 ? -8.793  -1.175  40.944  0.50 18.40 ? 255 GLN A NE2  1 
ATOM   2171 N  N    . ILE A 1 255 ? -9.950  -3.394  34.329  1.00 8.48  ? 256 ILE A N    1 
ATOM   2172 C  CA   . ILE A 1 255 ? -10.956 -3.561  33.289  1.00 7.98  ? 256 ILE A CA   1 
ATOM   2173 C  C    . ILE A 1 255 ? -12.366 -3.584  33.936  1.00 6.92  ? 256 ILE A C    1 
ATOM   2174 O  O    . ILE A 1 255 ? -12.549 -4.283  34.922  1.00 9.31  ? 256 ILE A O    1 
ATOM   2175 C  CB   . ILE A 1 255 ? -10.723 -4.864  32.497  1.00 8.39  ? 256 ILE A CB   1 
ATOM   2176 C  CG1  . ILE A 1 255 ? -9.298  -4.790  31.890  1.00 10.58 ? 256 ILE A CG1  1 
ATOM   2177 C  CG2  . ILE A 1 255 ? -11.759 -4.978  31.386  1.00 9.30  ? 256 ILE A CG2  1 
ATOM   2178 C  CD1  . ILE A 1 255 ? -8.932  -6.109  31.121  1.00 11.64 ? 256 ILE A CD1  1 
ATOM   2179 N  N    . LYS A 1 256 ? -13.227 -2.667  33.511  1.00 7.16  ? 257 LYS A N    1 
ATOM   2180 C  CA   . LYS A 1 256 ? -14.620 -2.555  34.086  1.00 6.45  ? 257 LYS A CA   1 
ATOM   2181 C  C    . LYS A 1 256 ? -15.563 -3.196  33.161  1.00 9.24  ? 257 LYS A C    1 
ATOM   2182 O  O    . LYS A 1 256 ? -15.439 -3.041  31.909  1.00 9.64  ? 257 LYS A O    1 
ATOM   2183 C  CB   . LYS A 1 256 ? -14.953 -1.074  34.325  1.00 7.10  ? 257 LYS A CB   1 
ATOM   2184 C  CG   . LYS A 1 256 ? -14.012 -0.514  35.395  1.00 15.15 ? 257 LYS A CG   1 
ATOM   2185 C  CD   . LYS A 1 256 ? -14.261 0.890   35.693  1.00 21.52 ? 257 LYS A CD   1 
ATOM   2186 C  CE   . LYS A 1 256 ? -13.056 1.348   36.609  1.00 27.23 ? 257 LYS A CE   1 
ATOM   2187 N  NZ   . LYS A 1 256 ? -13.059 2.833   36.936  1.00 32.30 ? 257 LYS A NZ   1 
ATOM   2188 N  N    . ALA A 1 257 ? -16.582 -3.876  33.695  1.00 9.52  ? 258 ALA A N    1 
ATOM   2189 C  CA   . ALA A 1 257 ? -17.701 -4.444  32.886  1.00 8.77  ? 258 ALA A CA   1 
ATOM   2190 C  C    . ALA A 1 257 ? -18.980 -3.672  33.027  1.00 9.60  ? 258 ALA A C    1 
ATOM   2191 O  O    . ALA A 1 257 ? -19.357 -3.254  34.130  1.00 8.78  ? 258 ALA A O    1 
ATOM   2192 C  CB   . ALA A 1 257 ? -17.979 -5.922  33.263  1.00 10.10 ? 258 ALA A CB   1 
ATOM   2193 N  N    . SER A 1 258 ? -19.650 -3.494  31.916  1.00 8.29  ? 259 SER A N    1 
ATOM   2194 C  CA   . SER A 1 258 ? -20.941 -2.777  31.923  1.00 10.14 ? 259 SER A CA   1 
ATOM   2195 C  C    . SER A 1 258 ? -22.085 -3.701  32.363  1.00 11.26 ? 259 SER A C    1 
ATOM   2196 O  O    . SER A 1 258 ? -23.212 -3.187  32.510  1.00 14.05 ? 259 SER A O    1 
ATOM   2197 C  CB   . SER A 1 258 ? -21.250 -2.227  30.550  1.00 11.13 ? 259 SER A CB   1 
ATOM   2198 O  OG   . SER A 1 258 ? -21.673 -3.281  29.657  1.00 9.88  ? 259 SER A OG   1 
ATOM   2199 N  N    . PHE A 1 259 ? -21.809 -4.951  32.649  1.00 9.90  ? 260 PHE A N    1 
ATOM   2200 C  CA   . PHE A 1 259 ? -22.883 -5.992  32.792  1.00 12.71 ? 260 PHE A CA   1 
ATOM   2201 C  C    . PHE A 1 259 ? -22.516 -6.893  33.957  1.00 16.21 ? 260 PHE A C    1 
ATOM   2202 O  O    . PHE A 1 259 ? -21.299 -7.117  34.306  1.00 15.02 ? 260 PHE A O    1 
ATOM   2203 C  CB   . PHE A 1 259 ? -23.071 -6.822  31.498  1.00 11.95 ? 260 PHE A CB   1 
ATOM   2204 C  CG   . PHE A 1 259 ? -21.806 -7.566  31.097  1.00 12.65 ? 260 PHE A CG   1 
ATOM   2205 C  CD1  . PHE A 1 259 ? -20.849 -6.909  30.354  1.00 11.51 ? 260 PHE A CD1  1 
ATOM   2206 C  CD2  . PHE A 1 259 ? -21.536 -8.851  31.590  1.00 16.07 ? 260 PHE A CD2  1 
ATOM   2207 C  CE1  . PHE A 1 259 ? -19.619 -7.547  30.048  1.00 14.61 ? 260 PHE A CE1  1 
ATOM   2208 C  CE2  . PHE A 1 259 ? -20.372 -9.475  31.317  1.00 14.81 ? 260 PHE A CE2  1 
ATOM   2209 C  CZ   . PHE A 1 259 ? -19.380 -8.825  30.522  1.00 16.39 ? 260 PHE A CZ   1 
ATOM   2210 N  N    . LYS A 1 260 ? -23.587 -7.467  34.518  1.00 23.51 ? 261 LYS A N    1 
ATOM   2211 C  CA   . LYS A 1 260 ? -23.433 -8.508  35.536  1.00 29.68 ? 261 LYS A CA   1 
ATOM   2212 C  C    . LYS A 1 260 ? -23.202 -9.937  34.969  1.00 32.00 ? 261 LYS A C    1 
ATOM   2213 O  O    . LYS A 1 260 ? -23.905 -10.514 34.071  1.00 33.23 ? 261 LYS A O    1 
ATOM   2214 C  CB   . LYS A 1 260 ? -24.547 -8.420  36.589  1.00 30.34 ? 261 LYS A CB   1 
ATOM   2215 C  CG   . LYS A 1 260 ? -24.108 -7.612  37.798  1.00 33.62 ? 261 LYS A CG   1 
ATOM   2216 C  CD   . LYS A 1 260 ? -25.076 -7.699  39.018  1.00 33.08 ? 261 LYS A CD   1 
ATOM   2217 C  CE   . LYS A 1 260 ? -24.204 -7.770  40.354  1.00 37.74 ? 261 LYS A CE   1 
ATOM   2218 N  NZ   . LYS A 1 260 ? -24.406 -6.701  41.417  1.00 37.66 ? 261 LYS A NZ   1 
ATOM   2219 O  OXT  . LYS A 1 260 ? -22.186 -10.519 35.418  1.00 33.52 ? 261 LYS A OXT  1 
HETATM 2220 N  N1   . J74 B 2 .   ? -0.916  10.025  14.622  1.00 22.78 ? 262 J74 A N1   1 
HETATM 2221 C  C2   . J74 B 2 .   ? -1.198  8.884   15.241  1.00 23.41 ? 262 J74 A C2   1 
HETATM 2222 N  N3   . J74 B 2 .   ? -1.694  7.881   14.547  1.00 21.24 ? 262 J74 A N3   1 
HETATM 2223 C  C4   . J74 B 2 .   ? -1.892  7.919   13.218  1.00 27.81 ? 262 J74 A C4   1 
HETATM 2224 C  C5   . J74 B 2 .   ? -1.674  9.125   12.500  1.00 31.15 ? 262 J74 A C5   1 
HETATM 2225 C  C6   . J74 B 2 .   ? -1.197  10.179  13.337  1.00 29.51 ? 262 J74 A C6   1 
HETATM 2226 N  N7   . J74 B 2 .   ? -2.318  6.807   12.505  1.00 25.60 ? 262 J74 A N7   1 
HETATM 2227 C  C8   . J74 B 2 .   ? -4.578  4.521   14.468  1.00 8.72  ? 262 J74 A C8   1 
HETATM 2228 C  C9   . J74 B 2 .   ? -3.715  3.470   14.751  1.00 8.79  ? 262 J74 A C9   1 
HETATM 2229 C  C10  . J74 B 2 .   ? -4.146  2.313   15.477  1.00 6.85  ? 262 J74 A C10  1 
HETATM 2230 C  C11  . J74 B 2 .   ? -5.512  2.297   15.849  1.00 4.82  ? 262 J74 A C11  1 
HETATM 2231 C  C12  . J74 B 2 .   ? -6.376  3.322   15.508  1.00 6.74  ? 262 J74 A C12  1 
HETATM 2232 C  C13  . J74 B 2 .   ? -5.933  4.459   14.807  1.00 8.22  ? 262 J74 A C13  1 
HETATM 2233 S  S14  . J74 B 2 .   ? -6.107  0.835   16.744  1.00 6.40  ? 262 J74 A S14  1 
HETATM 2234 O  O15  . J74 B 2 .   ? -5.555  0.959   18.166  1.00 5.18  ? 262 J74 A O15  1 
HETATM 2235 O  O16  . J74 B 2 .   ? -7.657  0.871   16.569  1.00 4.41  ? 262 J74 A O16  1 
HETATM 2236 N  N17  . J74 B 2 .   ? -5.532  -0.495  15.930  1.00 6.12  ? 262 J74 A N17  1 
HETATM 2237 N  N18  . J74 B 2 .   ? -1.904  9.214   11.050  1.00 29.79 ? 262 J74 A N18  1 
HETATM 2238 O  O19  . J74 B 2 .   ? -2.058  8.180   10.282  1.00 34.24 ? 262 J74 A O19  1 
HETATM 2239 O  O20  . J74 B 2 .   ? -1.921  10.336  10.411  1.00 38.41 ? 262 J74 A O20  1 
HETATM 2240 CL CL21 . J74 B 2 .   ? -0.831  11.739  12.759  1.00 37.59 ? 262 J74 A CL21 1 
HETATM 2241 C  C22  . J74 B 2 .   ? -2.627  5.553   13.174  1.00 26.35 ? 262 J74 A C22  1 
HETATM 2242 C  C23  . J74 B 2 .   ? -4.083  5.758   13.695  1.00 13.17 ? 262 J74 A C23  1 
HETATM 2243 ZN ZN   . ZN  C 3 .   ? -6.839  -1.684  15.254  1.00 6.28  ? 263 ZN  A ZN   1 
HETATM 2244 S  S    . DMS D 4 .   ? 1.188   -11.564 14.853  1.00 29.96 ? 264 DMS A S    1 
HETATM 2245 O  O    . DMS D 4 .   ? 1.658   -11.037 16.485  1.00 27.19 ? 264 DMS A O    1 
HETATM 2246 C  C1   . DMS D 4 .   ? 2.316   -10.865 13.600  1.00 26.96 ? 264 DMS A C1   1 
HETATM 2247 C  C2   . DMS D 4 .   ? 1.787   -13.275 14.674  1.00 25.13 ? 264 DMS A C2   1 
HETATM 2248 S  S    . DMS E 4 .   ? -5.469  7.875   10.939  1.00 32.88 ? 265 DMS A S    1 
HETATM 2249 O  O    . DMS E 4 .   ? -6.505  6.453   10.670  1.00 27.83 ? 265 DMS A O    1 
HETATM 2250 C  C1   . DMS E 4 .   ? -4.632  8.235   9.350   1.00 31.56 ? 265 DMS A C1   1 
HETATM 2251 C  C2   . DMS E 4 .   ? -6.475  9.377   10.941  1.00 30.25 ? 265 DMS A C2   1 
HETATM 2252 N  N1   . BCN F 5 .   ? -20.749 -14.595 23.141  1.00 28.87 ? 266 BCN A N1   1 
HETATM 2253 C  C1   . BCN F 5 .   ? -20.007 -14.142 24.321  1.00 27.13 ? 266 BCN A C1   1 
HETATM 2254 C  C2   . BCN F 5 .   ? -20.263 -15.036 25.503  1.00 30.27 ? 266 BCN A C2   1 
HETATM 2255 O  O21  . BCN F 5 .   ? -21.269 -15.825 25.562  1.00 34.85 ? 266 BCN A O21  1 
HETATM 2256 O  O22  . BCN F 5 .   ? -19.473 -14.964 26.480  1.00 25.78 ? 266 BCN A O22  1 
HETATM 2257 C  C3   . BCN F 5 .   ? -20.167 -15.676 22.421  1.00 21.15 ? 266 BCN A C3   1 
HETATM 2258 C  C4   . BCN F 5 .   ? -20.583 -16.425 21.151  1.00 31.27 ? 266 BCN A C4   1 
HETATM 2259 O  O4   . BCN F 5 .   ? -21.671 -16.041 20.301  1.00 37.48 ? 266 BCN A O4   1 
HETATM 2260 C  C5   . BCN F 5 .   ? -22.011 -13.921 22.881  1.00 22.27 ? 266 BCN A C5   1 
HETATM 2261 C  C6   . BCN F 5 .   ? -21.960 -12.612 23.685  1.00 33.79 ? 266 BCN A C6   1 
HETATM 2262 O  O6   . BCN F 5 .   ? -22.708 -12.474 24.856  1.00 29.37 ? 266 BCN A O6   1 
HETATM 2263 O  O    . HOH G 6 .   ? -27.043 -3.833  24.944  1.00 17.70 ? 126 HOH A O    1 
HETATM 2264 O  O    . HOH G 6 .   ? -15.489 -20.036 22.979  1.00 25.18 ? 267 HOH A O    1 
HETATM 2265 O  O    . HOH G 6 .   ? -14.763 -8.114  -5.884  1.00 31.74 ? 268 HOH A O    1 
HETATM 2266 O  O    . HOH G 6 .   ? -30.313 -6.581  7.755   1.00 29.24 ? 269 HOH A O    1 
HETATM 2267 O  O    . HOH G 6 .   ? -16.750 -14.750 28.798  1.00 31.33 ? 270 HOH A O    1 
HETATM 2268 O  O    . HOH G 6 .   ? -11.915 9.408   2.921   1.00 24.63 ? 271 HOH A O    1 
HETATM 2269 O  O    . HOH G 6 .   ? -3.024  -17.941 30.972  1.00 25.05 ? 272 HOH A O    1 
HETATM 2270 O  O    . HOH G 6 .   ? 3.521   3.496   -3.432  1.00 42.32 ? 273 HOH A O    1 
HETATM 2271 O  O    . HOH G 6 .   ? 2.147   -7.152  -8.340  1.00 32.28 ? 274 HOH A O    1 
HETATM 2272 O  O    . HOH G 6 .   ? -1.492  -13.237 33.170  1.00 23.57 ? 275 HOH A O    1 
HETATM 2273 O  O    . HOH G 6 .   ? -22.084 -14.074 18.705  1.00 27.07 ? 276 HOH A O    1 
HETATM 2274 O  O    . HOH G 6 .   ? 9.284   -9.394  0.503   1.00 42.11 ? 277 HOH A O    1 
HETATM 2275 O  O    . HOH G 6 .   ? 5.933   5.501   28.912  1.00 27.14 ? 278 HOH A O    1 
HETATM 2276 O  O    . HOH G 6 .   ? 3.455   9.795   23.647  1.00 23.97 ? 279 HOH A O    1 
HETATM 2277 O  O    . HOH G 6 .   ? -5.035  -20.892 21.262  1.00 21.19 ? 280 HOH A O    1 
HETATM 2278 O  O    . HOH G 6 .   ? -9.620  5.423   36.290  1.00 35.90 ? 281 HOH A O    1 
HETATM 2279 O  O    . HOH G 6 .   ? -24.714 -27.062 16.678  1.00 33.83 ? 282 HOH A O    1 
HETATM 2280 O  O    . HOH G 6 .   ? 2.652   6.672   31.901  1.00 28.00 ? 283 HOH A O    1 
HETATM 2281 O  O    . HOH G 6 .   ? -1.490  -6.035  36.337  1.00 29.15 ? 284 HOH A O    1 
HETATM 2282 O  O    . HOH G 6 .   ? -20.854 -6.853  -2.166  1.00 36.18 ? 285 HOH A O    1 
HETATM 2283 O  O    . HOH G 6 .   ? 6.159   -5.490  27.300  1.00 31.13 ? 286 HOH A O    1 
HETATM 2284 O  O    . HOH G 6 .   ? -31.465 4.406   8.130   1.00 35.81 ? 287 HOH A O    1 
HETATM 2285 O  O    . HOH G 6 .   ? -22.004 -21.582 17.210  1.00 31.25 ? 288 HOH A O    1 
HETATM 2286 O  O    . HOH G 6 .   ? -29.467 -9.548  5.284   1.00 27.65 ? 289 HOH A O    1 
HETATM 2287 O  O    . HOH G 6 .   ? -12.367 -24.947 8.124   1.00 31.68 ? 290 HOH A O    1 
HETATM 2288 O  O    . HOH G 6 .   ? 2.453   -4.478  -12.202 1.00 27.56 ? 291 HOH A O    1 
HETATM 2289 O  O    . HOH G 6 .   ? -27.698 -7.580  26.105  1.00 33.12 ? 292 HOH A O    1 
HETATM 2290 O  O    . HOH G 6 .   ? -17.385 -14.239 37.485  1.00 27.57 ? 293 HOH A O    1 
HETATM 2291 O  O    . HOH G 6 .   ? -20.362 -2.212  42.888  1.00 33.68 ? 294 HOH A O    1 
HETATM 2292 O  O    . HOH G 6 .   ? 6.499   -0.484  -1.299  1.00 27.66 ? 295 HOH A O    1 
HETATM 2293 O  O    . HOH G 6 .   ? -30.127 4.133   27.328  1.00 26.27 ? 296 HOH A O    1 
HETATM 2294 O  O    . HOH G 6 .   ? 1.742   8.903   30.888  1.00 36.72 ? 297 HOH A O    1 
HETATM 2295 O  O    . HOH G 6 .   ? 0.924   -9.827  29.134  1.00 38.76 ? 298 HOH A O    1 
HETATM 2296 O  O    . HOH G 6 .   ? -25.143 16.246  5.261   1.00 27.70 ? 299 HOH A O    1 
HETATM 2297 O  O    . HOH G 6 .   ? -24.495 13.567  20.414  1.00 27.76 ? 300 HOH A O    1 
HETATM 2298 O  O    . HOH G 6 .   ? -17.463 -1.126  40.331  1.00 30.72 ? 301 HOH A O    1 
HETATM 2299 O  O    . HOH G 6 .   ? 1.065   4.997   12.094  1.00 30.26 ? 302 HOH A O    1 
HETATM 2300 O  O    . HOH G 6 .   ? -11.250 -5.814  40.621  1.00 24.40 ? 303 HOH A O    1 
HETATM 2301 O  O    . HOH G 6 .   ? -8.110  -15.463 11.303  1.00 8.11  ? 304 HOH A O    1 
HETATM 2302 O  O    . HOH G 6 .   ? -20.121 17.263  23.092  1.00 34.18 ? 305 HOH A O    1 
HETATM 2303 O  O    . HOH G 6 .   ? 10.117  7.049   15.409  1.00 33.17 ? 306 HOH A O    1 
HETATM 2304 O  O    . HOH G 6 .   ? 2.891   1.189   -6.314  1.00 32.02 ? 307 HOH A O    1 
HETATM 2305 O  O    . HOH G 6 .   ? 4.872   -13.117 -5.892  1.00 24.75 ? 308 HOH A O    1 
HETATM 2306 O  O    . HOH G 6 .   ? -15.274 5.651   36.798  1.00 23.79 ? 309 HOH A O    1 
HETATM 2307 O  O    . HOH G 6 .   ? -12.400 -24.800 11.016  1.00 24.21 ? 310 HOH A O    1 
HETATM 2308 O  O    . HOH G 6 .   ? 2.023   8.043   27.694  1.00 25.83 ? 311 HOH A O    1 
HETATM 2309 O  O    . HOH G 6 .   ? -25.070 -11.236 23.748  1.00 30.57 ? 312 HOH A O    1 
HETATM 2310 O  O    . HOH G 6 .   ? -5.930  -2.369  -8.122  1.00 29.33 ? 313 HOH A O    1 
HETATM 2311 O  O    . HOH G 6 .   ? -18.294 -13.212 39.982  1.00 26.50 ? 314 HOH A O    1 
HETATM 2312 O  O    . HOH G 6 .   ? -17.158 -11.386 36.441  1.00 29.03 ? 315 HOH A O    1 
HETATM 2313 O  O    . HOH G 6 .   ? 5.788   2.351   -3.453  1.00 26.88 ? 316 HOH A O    1 
HETATM 2314 O  O    . HOH G 6 .   ? -17.217 -8.389  20.343  1.00 6.93  ? 317 HOH A O    1 
HETATM 2315 O  O    . HOH G 6 .   ? -10.868 8.715   25.440  1.00 7.82  ? 318 HOH A O    1 
HETATM 2316 O  O    . HOH G 6 .   ? -20.187 -25.344 18.868  1.00 23.50 ? 319 HOH A O    1 
HETATM 2317 O  O    . HOH G 6 .   ? -24.176 10.300  27.298  1.00 37.84 ? 320 HOH A O    1 
HETATM 2318 O  O    . HOH G 6 .   ? -27.202 -13.060 20.282  1.00 33.93 ? 321 HOH A O    1 
HETATM 2319 O  O    . HOH G 6 .   ? 6.742   8.503   17.753  1.00 35.51 ? 322 HOH A O    1 
HETATM 2320 O  O    . HOH G 6 .   ? -17.354 -7.534  39.673  1.00 39.58 ? 323 HOH A O    1 
HETATM 2321 O  O    . HOH G 6 .   ? -17.280 -22.144 21.926  1.00 37.75 ? 324 HOH A O    1 
HETATM 2322 O  O    . HOH G 6 .   ? -18.168 10.656  2.120   1.00 31.00 ? 325 HOH A O    1 
HETATM 2323 O  O    . HOH G 6 .   ? -24.011 -9.734  27.604  1.00 39.02 ? 326 HOH A O    1 
HETATM 2324 O  O    . HOH G 6 .   ? -0.616  -16.253 27.356  1.00 39.41 ? 327 HOH A O    1 
HETATM 2325 O  O    . HOH G 6 .   ? -28.113 15.588  6.206   1.00 29.24 ? 328 HOH A O    1 
HETATM 2326 O  O    . HOH G 6 .   ? 9.636   -13.722 9.076   1.00 45.43 ? 329 HOH A O    1 
HETATM 2327 O  O    . HOH G 6 .   ? -0.306  -14.982 34.706  1.00 44.18 ? 330 HOH A O    1 
HETATM 2328 O  O    . HOH G 6 .   ? -19.522 11.088  32.980  1.00 30.65 ? 331 HOH A O    1 
HETATM 2329 O  O    . HOH G 6 .   ? -25.699 -3.518  5.871   1.00 39.04 ? 332 HOH A O    1 
HETATM 2330 O  O    . HOH G 6 .   ? 3.866   -2.700  5.232   1.00 43.00 ? 333 HOH A O    1 
HETATM 2331 O  O    . HOH G 6 .   ? -1.406  -4.143  15.649  1.00 6.39  ? 334 HOH A O    1 
HETATM 2332 O  O    . HOH G 6 .   ? -22.997 -25.882 19.095  1.00 29.91 ? 335 HOH A O    1 
HETATM 2333 O  O    . HOH G 6 .   ? -12.115 -3.073  42.054  1.00 27.72 ? 336 HOH A O    1 
HETATM 2334 O  O    . HOH G 6 .   ? 1.622   -16.351 -1.958  1.00 30.37 ? 337 HOH A O    1 
HETATM 2335 O  O    . HOH G 6 .   ? 3.234   -16.163 -7.167  1.00 35.76 ? 338 HOH A O    1 
HETATM 2336 O  O    . HOH G 6 .   ? -23.737 -21.478 10.312  1.00 29.27 ? 339 HOH A O    1 
HETATM 2337 O  O    . HOH G 6 .   ? 3.315   -13.743 12.543  1.00 31.41 ? 340 HOH A O    1 
HETATM 2338 O  O    . HOH G 6 .   ? 6.806   -1.830  -7.993  1.00 27.24 ? 341 HOH A O    1 
HETATM 2339 O  O    . HOH G 6 .   ? -0.989  -5.637  -10.880 1.00 34.74 ? 342 HOH A O    1 
HETATM 2340 O  O    . HOH G 6 .   ? -12.041 -27.779 4.995   1.00 36.92 ? 343 HOH A O    1 
HETATM 2341 O  O    . HOH G 6 .   ? -8.769  -17.942 -1.034  1.00 43.19 ? 344 HOH A O    1 
HETATM 2342 O  O    . HOH G 6 .   ? -25.956 -3.749  31.821  1.00 37.63 ? 345 HOH A O    1 
HETATM 2343 O  O    . HOH G 6 .   ? -9.784  -25.978 6.523   1.00 45.83 ? 346 HOH A O    1 
HETATM 2344 O  O    . HOH G 6 .   ? 3.565   -0.597  36.472  1.00 41.02 ? 347 HOH A O    1 
HETATM 2345 O  O    . HOH G 6 .   ? 8.814   2.309   29.720  1.00 34.63 ? 348 HOH A O    1 
HETATM 2346 O  O    . HOH G 6 .   ? -14.002 -22.118 3.856   1.00 39.86 ? 349 HOH A O    1 
HETATM 2347 O  O    . HOH G 6 .   ? -24.188 -6.902  0.444   1.00 22.56 ? 350 HOH A O    1 
HETATM 2348 O  O    . HOH G 6 .   ? -26.675 -6.257  4.619   0.50 21.24 ? 351 HOH A O    1 
HETATM 2349 O  O    . HOH G 6 .   ? -6.494  -19.520 5.613   1.00 26.06 ? 352 HOH A O    1 
HETATM 2350 O  O    . HOH G 6 .   ? -30.156 -9.768  22.101  1.00 27.25 ? 353 HOH A O    1 
HETATM 2351 O  O    . HOH G 6 .   ? 2.754   -14.340 -5.784  1.00 30.04 ? 354 HOH A O    1 
HETATM 2352 O  O    . HOH G 6 .   ? -19.895 -23.200 17.535  1.00 27.30 ? 355 HOH A O    1 
HETATM 2353 O  O    . HOH G 6 .   ? -6.913  10.282  8.183   1.00 30.78 ? 356 HOH A O    1 
HETATM 2354 O  O    . HOH G 6 .   ? 7.562   -1.410  -5.465  1.00 39.53 ? 357 HOH A O    1 
HETATM 2355 O  O    . HOH G 6 .   ? -26.001 0.890   32.766  1.00 36.55 ? 358 HOH A O    1 
HETATM 2356 O  O    . HOH G 6 .   ? -26.939 5.195   6.365   1.00 40.92 ? 359 HOH A O    1 
HETATM 2357 O  O    . HOH G 6 .   ? 1.618   -2.537  -14.954 1.00 45.84 ? 360 HOH A O    1 
HETATM 2358 O  O    . HOH G 6 .   ? -11.405 -11.179 -2.708  1.00 33.97 ? 361 HOH A O    1 
HETATM 2359 O  O    . HOH G 6 .   ? -19.026 -5.996  45.229  1.00 34.14 ? 362 HOH A O    1 
HETATM 2360 O  O    . HOH G 6 .   ? 5.466   -12.791 11.299  1.00 34.70 ? 363 HOH A O    1 
HETATM 2361 O  O    . HOH G 6 .   ? -13.467 -2.629  -9.477  1.00 44.40 ? 364 HOH A O    1 
HETATM 2362 O  O    . HOH G 6 .   ? 6.344   8.959   25.030  1.00 41.92 ? 365 HOH A O    1 
HETATM 2363 O  O    . HOH G 6 .   ? 1.218   7.689   12.049  1.00 39.59 ? 366 HOH A O    1 
HETATM 2364 O  O    . HOH G 6 .   ? -3.707  -23.238 21.266  1.00 35.76 ? 367 HOH A O    1 
HETATM 2365 O  O    . HOH G 6 .   ? -7.275  -24.426 10.319  1.00 41.38 ? 368 HOH A O    1 
HETATM 2366 O  O    . HOH G 6 .   ? -17.553 -6.602  42.511  1.00 44.82 ? 369 HOH A O    1 
HETATM 2367 O  O    . HOH G 6 .   ? -8.762  11.731  7.623   1.00 45.65 ? 370 HOH A O    1 
HETATM 2368 O  O    . HOH G 6 .   ? 4.658   -4.909  20.978  1.00 9.43  ? 371 HOH A O    1 
HETATM 2369 O  O    . HOH G 6 .   ? 0.371   -0.077  -15.068 1.00 36.79 ? 372 HOH A O    1 
HETATM 2370 O  O    . HOH G 6 .   ? -26.176 -6.522  33.836  1.00 49.52 ? 373 HOH A O    1 
HETATM 2371 O  O    . HOH G 6 .   ? -14.043 -26.027 5.719   1.00 33.83 ? 374 HOH A O    1 
HETATM 2372 O  O    . HOH G 6 .   ? -10.297 -23.743 9.610   1.00 28.02 ? 375 HOH A O    1 
HETATM 2373 O  O    . HOH G 6 .   ? -25.336 -9.817  31.968  1.00 34.18 ? 376 HOH A O    1 
HETATM 2374 O  O    . HOH G 6 .   ? -26.609 9.347   3.552   1.00 37.51 ? 377 HOH A O    1 
HETATM 2375 O  O    . HOH G 6 .   ? -4.739  -13.535 18.029  1.00 6.91  ? 378 HOH A O    1 
HETATM 2376 O  O    . HOH G 6 .   ? -18.112 -20.451 7.943   1.00 9.95  ? 379 HOH A O    1 
HETATM 2377 O  O    . HOH G 6 .   ? -21.836 -7.319  23.621  1.00 9.57  ? 380 HOH A O    1 
HETATM 2378 O  O    . HOH G 6 .   ? -18.038 10.732  11.206  1.00 14.84 ? 381 HOH A O    1 
HETATM 2379 O  O    . HOH G 6 .   ? 3.342   5.106   29.743  1.00 14.61 ? 382 HOH A O    1 
HETATM 2380 O  O    . HOH G 6 .   ? -8.842  -3.871  7.815   1.00 7.85  ? 383 HOH A O    1 
HETATM 2381 O  O    . HOH G 6 .   ? -2.309  -12.355 22.725  1.00 8.24  ? 384 HOH A O    1 
HETATM 2382 O  O    . HOH G 6 .   ? -3.688  -13.278 25.066  1.00 8.15  ? 385 HOH A O    1 
HETATM 2383 O  O    . HOH G 6 .   ? -2.782  -8.739  29.116  1.00 9.65  ? 386 HOH A O    1 
HETATM 2384 O  O    . HOH G 6 .   ? -13.628 -18.510 14.565  1.00 11.55 ? 387 HOH A O    1 
HETATM 2385 O  O    . HOH G 6 .   ? 0.920   -1.463  29.332  1.00 10.74 ? 388 HOH A O    1 
HETATM 2386 O  O    . HOH G 6 .   ? -14.116 10.286  27.882  1.00 14.96 ? 389 HOH A O    1 
HETATM 2387 O  O    . HOH G 6 .   ? -21.758 5.654   4.713   1.00 12.53 ? 390 HOH A O    1 
HETATM 2388 O  O    . HOH G 6 .   ? -9.960  -7.980  34.038  1.00 16.78 ? 391 HOH A O    1 
HETATM 2389 O  O    . HOH G 6 .   ? -29.289 -5.807  24.340  1.00 17.36 ? 392 HOH A O    1 
HETATM 2390 O  O    . HOH G 6 .   ? 5.174   7.131   20.152  1.00 13.76 ? 393 HOH A O    1 
HETATM 2391 O  O    . HOH G 6 .   ? -24.291 8.540   20.141  1.00 17.75 ? 394 HOH A O    1 
HETATM 2392 O  O    . HOH G 6 .   ? -19.310 10.073  8.864   1.00 11.35 ? 395 HOH A O    1 
HETATM 2393 O  O    . HOH G 6 .   ? -14.537 -16.625 28.995  1.00 18.35 ? 396 HOH A O    1 
HETATM 2394 O  O    . HOH G 6 .   ? -4.049  -15.940 24.268  1.00 8.59  ? 397 HOH A O    1 
HETATM 2395 O  O    . HOH G 6 .   ? -3.764  -11.113 20.842  1.00 7.68  ? 398 HOH A O    1 
HETATM 2396 O  O    . HOH G 6 .   ? -10.621 -18.330 17.004  1.00 10.43 ? 399 HOH A O    1 
HETATM 2397 O  O    . HOH G 6 .   ? -14.944 -18.588 18.707  1.00 12.13 ? 400 HOH A O    1 
HETATM 2398 O  O    . HOH G 6 .   ? -15.151 -21.184 17.708  1.00 12.80 ? 401 HOH A O    1 
HETATM 2399 O  O    . HOH G 6 .   ? -16.326 -12.277 24.344  1.00 11.35 ? 402 HOH A O    1 
HETATM 2400 O  O    . HOH G 6 .   ? 7.332   6.099   21.597  1.00 11.93 ? 403 HOH A O    1 
HETATM 2401 O  O    . HOH G 6 .   ? -21.054 7.958   1.824   1.00 17.70 ? 404 HOH A O    1 
HETATM 2402 O  O    . HOH G 6 .   ? -10.338 14.881  12.137  1.00 16.07 ? 405 HOH A O    1 
HETATM 2403 O  O    . HOH G 6 .   ? 8.287   -3.805  20.999  1.00 13.76 ? 406 HOH A O    1 
HETATM 2404 O  O    . HOH G 6 .   ? -13.069 -17.242 16.913  1.00 10.28 ? 407 HOH A O    1 
HETATM 2405 O  O    . HOH G 6 .   ? -12.370 2.773   30.895  1.00 16.20 ? 408 HOH A O    1 
HETATM 2406 O  O    . HOH G 6 .   ? -17.953 -21.205 17.566  1.00 17.81 ? 409 HOH A O    1 
HETATM 2407 O  O    . HOH G 6 .   ? 1.008   8.888   24.245  1.00 16.04 ? 410 HOH A O    1 
HETATM 2408 O  O    . HOH G 6 .   ? -17.643 -16.158 22.149  1.00 16.20 ? 411 HOH A O    1 
HETATM 2409 O  O    . HOH G 6 .   ? -5.958  -4.629  -6.385  1.00 19.44 ? 412 HOH A O    1 
HETATM 2410 O  O    . HOH G 6 .   ? -13.208 -16.925 26.656  1.00 10.38 ? 413 HOH A O    1 
HETATM 2411 O  O    . HOH G 6 .   ? 4.370   -6.490  7.848   1.00 17.96 ? 414 HOH A O    1 
HETATM 2412 O  O    . HOH G 6 .   ? -8.485  -19.470 21.686  1.00 11.37 ? 415 HOH A O    1 
HETATM 2413 O  O    . HOH G 6 .   ? -5.135  -11.901 32.053  1.00 15.68 ? 416 HOH A O    1 
HETATM 2414 O  O    . HOH G 6 .   ? -2.744  -3.527  11.345  1.00 17.83 ? 417 HOH A O    1 
HETATM 2415 O  O    . HOH G 6 .   ? -9.293  -10.065 -1.250  1.00 17.03 ? 418 HOH A O    1 
HETATM 2416 O  O    . HOH G 6 .   ? -26.996 -2.442  14.332  1.00 17.28 ? 419 HOH A O    1 
HETATM 2417 O  O    . HOH G 6 .   ? -28.877 0.201   24.393  1.00 21.80 ? 420 HOH A O    1 
HETATM 2418 O  O    . HOH G 6 .   ? -14.012 -21.215 15.077  1.00 13.66 ? 421 HOH A O    1 
HETATM 2419 O  O    . HOH G 6 .   ? 1.082   -11.756 25.030  1.00 21.25 ? 422 HOH A O    1 
HETATM 2420 O  O    . HOH G 6 .   ? -17.168 -17.961 20.101  1.00 15.82 ? 423 HOH A O    1 
HETATM 2421 O  O    . HOH G 6 .   ? -18.290 -3.665  -2.694  1.00 23.82 ? 424 HOH A O    1 
HETATM 2422 O  O    . HOH G 6 .   ? 2.651   -4.330  7.651   1.00 16.11 ? 425 HOH A O    1 
HETATM 2423 O  O    . HOH G 6 .   ? -10.809 4.946   30.958  1.00 18.77 ? 426 HOH A O    1 
HETATM 2424 O  O    . HOH G 6 .   ? -20.630 10.787  26.670  1.00 13.27 ? 427 HOH A O    1 
HETATM 2425 O  O    . HOH G 6 .   ? -23.133 -11.778 14.060  1.00 18.12 ? 428 HOH A O    1 
HETATM 2426 O  O    . HOH G 6 .   ? -24.280 -0.799  26.537  1.00 17.94 ? 429 HOH A O    1 
HETATM 2427 O  O    . HOH G 6 .   ? -7.268  -16.909 1.585   1.00 19.34 ? 430 HOH A O    1 
HETATM 2428 O  O    . HOH G 6 .   ? 10.932  1.376   25.834  1.00 19.20 ? 431 HOH A O    1 
HETATM 2429 O  O    . HOH G 6 .   ? -2.229  -17.487 25.536  1.00 17.94 ? 432 HOH A O    1 
HETATM 2430 O  O    . HOH G 6 .   ? -15.650 9.084   -2.091  1.00 21.57 ? 433 HOH A O    1 
HETATM 2431 O  O    . HOH G 6 .   ? -12.560 12.573  29.149  1.00 21.82 ? 434 HOH A O    1 
HETATM 2432 O  O    . HOH G 6 .   ? -14.314 14.208  27.136  1.00 17.00 ? 435 HOH A O    1 
HETATM 2433 O  O    . HOH G 6 .   ? -22.770 -5.822  2.753   1.00 16.14 ? 436 HOH A O    1 
HETATM 2434 O  O    . HOH G 6 .   ? -16.619 -9.989  32.940  1.00 15.07 ? 437 HOH A O    1 
HETATM 2435 O  O    . HOH G 6 .   ? -9.357  -5.885  35.897  1.00 15.12 ? 438 HOH A O    1 
HETATM 2436 O  O    . HOH G 6 .   ? 3.925   -3.406  26.439  1.00 18.37 ? 439 HOH A O    1 
HETATM 2437 O  O    . HOH G 6 .   ? -23.266 -2.990  6.581   1.00 16.35 ? 440 HOH A O    1 
HETATM 2438 O  O    . HOH G 6 .   ? -8.112  -22.272 10.342  1.00 14.69 ? 441 HOH A O    1 
HETATM 2439 O  O    . HOH G 6 .   ? -16.775 -11.366 41.619  1.00 22.23 ? 442 HOH A O    1 
HETATM 2440 O  O    . HOH G 6 .   ? -19.306 14.111  8.956   1.00 26.01 ? 443 HOH A O    1 
HETATM 2441 O  O    . HOH G 6 .   ? 4.217   -2.665  28.887  1.00 18.86 ? 444 HOH A O    1 
HETATM 2442 O  O    . HOH G 6 .   ? -3.706  -13.050 -2.787  1.00 18.37 ? 445 HOH A O    1 
HETATM 2443 O  O    . HOH G 6 .   ? -7.039  -20.236 19.478  1.00 11.37 ? 446 HOH A O    1 
HETATM 2444 O  O    . HOH G 6 .   ? -8.371  0.718   -6.461  1.00 21.63 ? 447 HOH A O    1 
HETATM 2445 O  O    . HOH G 6 .   ? -16.399 15.923  23.722  1.00 15.12 ? 448 HOH A O    1 
HETATM 2446 O  O    . HOH G 6 .   ? -4.093  0.230   13.396  1.00 14.83 ? 449 HOH A O    1 
HETATM 2447 O  O    . HOH G 6 .   ? -1.591  -13.105 26.962  1.00 14.59 ? 450 HOH A O    1 
HETATM 2448 O  O    . HOH G 6 .   ? -13.155 -19.587 26.069  1.00 16.67 ? 451 HOH A O    1 
HETATM 2449 O  O    . HOH G 6 .   ? -11.337 15.436  32.146  1.00 14.86 ? 452 HOH A O    1 
HETATM 2450 O  O    . HOH G 6 .   ? -0.425  -14.217 22.107  1.00 18.81 ? 453 HOH A O    1 
HETATM 2451 O  O    . HOH G 6 .   ? -15.609 -21.868 13.073  1.00 14.18 ? 454 HOH A O    1 
HETATM 2452 O  O    . HOH G 6 .   ? -1.433  -11.129 28.970  1.00 13.69 ? 455 HOH A O    1 
HETATM 2453 O  O    . HOH G 6 .   ? -11.233 -19.613 7.153   1.00 24.33 ? 456 HOH A O    1 
HETATM 2454 O  O    . HOH G 6 .   ? 0.227   -1.110  -4.720  1.00 15.02 ? 457 HOH A O    1 
HETATM 2455 O  O    . HOH G 6 .   ? -18.015 6.175   38.251  1.00 25.48 ? 458 HOH A O    1 
HETATM 2456 O  O    . HOH G 6 .   ? -8.977  -15.401 36.564  1.00 22.29 ? 459 HOH A O    1 
HETATM 2457 O  O    . HOH G 6 .   ? -23.858 -17.073 3.595   1.00 30.44 ? 460 HOH A O    1 
HETATM 2458 O  O    . HOH G 6 .   ? 4.745   -7.407  22.224  1.00 23.09 ? 461 HOH A O    1 
HETATM 2459 O  O    . HOH G 6 .   ? -26.093 -6.206  13.002  1.00 27.60 ? 462 HOH A O    1 
HETATM 2460 O  O    . HOH G 6 .   ? -26.235 3.359   15.325  1.00 20.49 ? 463 HOH A O    1 
HETATM 2461 O  O    . HOH G 6 .   ? -17.073 -13.973 26.304  1.00 17.17 ? 464 HOH A O    1 
HETATM 2462 O  O    . HOH G 6 .   ? -0.747  10.824  23.249  1.00 16.35 ? 465 HOH A O    1 
HETATM 2463 O  O    . HOH G 6 .   ? 1.636   3.114   -4.987  1.00 25.46 ? 466 HOH A O    1 
HETATM 2464 O  O    . HOH G 6 .   ? -23.759 -0.855  3.909   1.00 18.80 ? 467 HOH A O    1 
HETATM 2465 O  O    . HOH G 6 .   ? -19.934 -16.891 2.922   1.00 19.85 ? 468 HOH A O    1 
HETATM 2466 O  O    . HOH G 6 .   ? -27.353 -7.007  7.726   1.00 33.20 ? 469 HOH A O    1 
HETATM 2467 O  O    . HOH G 6 .   ? -7.048  -14.938 31.466  1.00 19.06 ? 470 HOH A O    1 
HETATM 2468 O  O    . HOH G 6 .   ? -9.380  5.909   29.104  1.00 16.14 ? 471 HOH A O    1 
HETATM 2469 O  O    . HOH G 6 .   ? -1.279  -17.651 -1.748  1.00 27.45 ? 472 HOH A O    1 
HETATM 2470 O  O    . HOH G 6 .   ? -6.518  -19.744 23.784  1.00 16.84 ? 473 HOH A O    1 
HETATM 2471 O  O    . HOH G 6 .   ? -10.767 -19.512 19.927  1.00 15.28 ? 474 HOH A O    1 
HETATM 2472 O  O    . HOH G 6 .   ? -4.529  4.198   10.255  1.00 22.91 ? 475 HOH A O    1 
HETATM 2473 O  O    . HOH G 6 .   ? -5.504  2.097   12.039  1.00 13.58 ? 476 HOH A O    1 
HETATM 2474 O  O    . HOH G 6 .   ? -22.275 -18.391 13.650  1.00 18.28 ? 477 HOH A O    1 
HETATM 2475 O  O    . HOH G 6 .   ? -25.404 10.957  19.538  1.00 24.94 ? 478 HOH A O    1 
HETATM 2476 O  O    . HOH G 6 .   ? -7.098  5.942   6.444   1.00 21.42 ? 479 HOH A O    1 
HETATM 2477 O  O    . HOH G 6 .   ? -11.327 1.105   33.426  1.00 15.95 ? 480 HOH A O    1 
HETATM 2478 O  O    . HOH G 6 .   ? -1.281  -17.566 17.938  1.00 30.62 ? 481 HOH A O    1 
HETATM 2479 O  O    . HOH G 6 .   ? -0.796  -8.535  32.517  1.00 20.09 ? 482 HOH A O    1 
HETATM 2480 O  O    . HOH G 6 .   ? -27.828 2.939   23.651  1.00 29.91 ? 483 HOH A O    1 
HETATM 2481 O  O    . HOH G 6 .   ? -29.188 -3.928  13.501  1.00 23.08 ? 484 HOH A O    1 
HETATM 2482 O  O    . HOH G 6 .   ? -24.903 -7.787  9.006   1.00 15.04 ? 485 HOH A O    1 
HETATM 2483 O  O    . HOH G 6 .   ? -4.645  -15.866 0.689   1.00 22.80 ? 486 HOH A O    1 
HETATM 2484 O  O    . HOH G 6 .   ? -7.475  -8.744  -2.494  1.00 22.44 ? 487 HOH A O    1 
HETATM 2485 O  O    . HOH G 6 .   ? -7.644  -8.670  32.510  1.00 15.33 ? 488 HOH A O    1 
HETATM 2486 O  O    . HOH G 6 .   ? 2.591   -13.261 5.328   1.00 21.01 ? 489 HOH A O    1 
HETATM 2487 O  O    . HOH G 6 .   ? -16.952 -17.818 23.988  1.00 30.41 ? 490 HOH A O    1 
HETATM 2488 O  O    . HOH G 6 .   ? 1.416   12.541  22.640  1.00 23.00 ? 491 HOH A O    1 
HETATM 2489 O  O    . HOH G 6 .   ? 2.428   -11.571 9.346   1.00 24.72 ? 492 HOH A O    1 
HETATM 2490 O  O    . HOH G 6 .   ? -18.785 -21.181 14.743  1.00 19.22 ? 493 HOH A O    1 
HETATM 2491 O  O    . HOH G 6 .   ? -10.160 1.521   38.962  1.00 27.24 ? 494 HOH A O    1 
HETATM 2492 O  O    . HOH G 6 .   ? -8.688  -19.991 26.639  1.00 18.70 ? 495 HOH A O    1 
HETATM 2493 O  O    . HOH G 6 .   ? -1.677  -4.747  -6.904  1.00 28.45 ? 496 HOH A O    1 
HETATM 2494 O  O    . HOH G 6 .   ? -19.408 -20.915 5.270   1.00 21.23 ? 497 HOH A O    1 
HETATM 2495 O  O    . HOH G 6 .   ? -10.919 -20.385 24.826  1.00 15.19 ? 498 HOH A O    1 
HETATM 2496 O  O    . HOH G 6 .   ? -30.970 -6.968  22.422  1.00 24.62 ? 499 HOH A O    1 
HETATM 2497 O  O    . HOH G 6 .   ? -24.705 -9.496  1.990   1.00 22.78 ? 500 HOH A O    1 
HETATM 2498 O  O    . HOH G 6 .   ? 8.318   -4.525  23.556  1.00 22.85 ? 501 HOH A O    1 
HETATM 2499 O  O    . HOH G 6 .   ? -17.732 -19.524 35.080  1.00 23.30 ? 502 HOH A O    1 
HETATM 2500 O  O    . HOH G 6 .   ? -7.478  1.676   35.183  1.00 21.68 ? 503 HOH A O    1 
HETATM 2501 O  O    . HOH G 6 .   ? -23.535 -13.254 11.186  1.00 17.09 ? 504 HOH A O    1 
HETATM 2502 O  O    . HOH G 6 .   ? -13.227 -22.160 8.567   1.00 15.31 ? 505 HOH A O    1 
HETATM 2503 O  O    . HOH G 6 .   ? -13.136 7.909   28.793  1.00 18.41 ? 506 HOH A O    1 
HETATM 2504 O  O    . HOH G 6 .   ? -5.201  0.481   9.782   1.00 18.02 ? 507 HOH A O    1 
HETATM 2505 O  O    . HOH G 6 .   ? -21.344 -20.562 14.575  1.00 28.54 ? 508 HOH A O    1 
HETATM 2506 O  O    . HOH G 6 .   ? -9.715  3.031   34.717  1.00 19.12 ? 509 HOH A O    1 
HETATM 2507 O  O    . HOH G 6 .   ? -6.572  -26.126 11.733  1.00 22.34 ? 510 HOH A O    1 
HETATM 2508 O  O    . HOH G 6 .   ? -1.715  11.355  25.832  1.00 26.20 ? 511 HOH A O    1 
HETATM 2509 O  O    . HOH G 6 .   ? 6.617   -3.665  29.817  1.00 30.15 ? 512 HOH A O    1 
HETATM 2510 O  O    . HOH G 6 .   ? -26.160 6.130   26.944  1.00 22.87 ? 513 HOH A O    1 
HETATM 2511 O  O    . HOH G 6 .   ? -26.728 2.793   20.887  1.00 19.49 ? 514 HOH A O    1 
HETATM 2512 O  O    . HOH G 6 .   ? -12.936 -9.206  -3.072  1.00 23.19 ? 515 HOH A O    1 
HETATM 2513 O  O    . HOH G 6 .   ? -20.456 -0.169  -1.937  1.00 41.26 ? 516 HOH A O    1 
HETATM 2514 O  O    . HOH G 6 .   ? -18.810 -8.851  34.640  1.00 31.36 ? 517 HOH A O    1 
HETATM 2515 O  O    . HOH G 6 .   ? -32.014 -2.568  13.813  1.00 27.49 ? 518 HOH A O    1 
HETATM 2516 O  O    . HOH G 6 .   ? -11.286 -15.215 34.191  1.00 26.38 ? 519 HOH A O    1 
HETATM 2517 O  O    . HOH G 6 .   ? 0.524   0.419   -6.827  1.00 25.35 ? 520 HOH A O    1 
HETATM 2518 O  O    . HOH G 6 .   ? -12.050 -0.188  43.449  1.00 24.30 ? 521 HOH A O    1 
HETATM 2519 O  O    . HOH G 6 .   ? -8.217  7.493   8.449   1.00 25.81 ? 522 HOH A O    1 
HETATM 2520 O  O    . HOH G 6 .   ? -23.600 -10.849 17.078  1.00 24.52 ? 523 HOH A O    1 
HETATM 2521 O  O    . HOH G 6 .   ? 6.456   -5.555  3.659   1.00 24.09 ? 524 HOH A O    1 
HETATM 2522 O  O    . HOH G 6 .   ? 1.011   -6.294  34.324  1.00 17.49 ? 525 HOH A O    1 
HETATM 2523 O  O    . HOH G 6 .   ? 0.088   -19.676 10.539  1.00 30.05 ? 526 HOH A O    1 
HETATM 2524 O  O    . HOH G 6 .   ? -18.214 -12.151 31.427  1.00 24.24 ? 527 HOH A O    1 
HETATM 2525 O  O    . HOH G 6 .   ? 1.802   -14.212 20.476  1.00 22.69 ? 528 HOH A O    1 
HETATM 2526 O  O    . HOH G 6 .   ? -15.740 -16.413 25.596  1.00 24.44 ? 529 HOH A O    1 
HETATM 2527 O  O    . HOH G 6 .   ? -16.277 3.645   35.199  1.00 27.77 ? 530 HOH A O    1 
HETATM 2528 O  O    . HOH G 6 .   ? -20.727 13.849  28.807  1.00 30.81 ? 531 HOH A O    1 
HETATM 2529 O  O    . HOH G 6 .   ? -17.361 -8.732  -6.322  1.00 25.50 ? 532 HOH A O    1 
HETATM 2530 O  O    . HOH G 6 .   ? -16.132 5.403   -8.013  1.00 24.59 ? 533 HOH A O    1 
HETATM 2531 O  O    . HOH G 6 .   ? -23.638 -17.906 6.043   1.00 32.80 ? 534 HOH A O    1 
HETATM 2532 O  O    . HOH G 6 .   ? -28.506 -1.085  28.194  1.00 34.00 ? 535 HOH A O    1 
HETATM 2533 O  O    . HOH G 6 .   ? -2.342  -11.743 31.485  1.00 23.42 ? 536 HOH A O    1 
HETATM 2534 O  O    . HOH G 6 .   ? -26.960 -1.269  25.977  1.00 19.94 ? 537 HOH A O    1 
HETATM 2535 O  O    . HOH G 6 .   ? -0.175  -7.257  -7.338  1.00 31.94 ? 538 HOH A O    1 
HETATM 2536 O  O    . HOH G 6 .   ? -4.010  -15.656 -2.227  1.00 26.76 ? 539 HOH A O    1 
HETATM 2537 O  O    . HOH G 6 .   ? -7.130  -10.131 -4.511  1.00 24.40 ? 540 HOH A O    1 
HETATM 2538 O  O    . HOH G 6 .   ? -6.421  12.368  10.486  1.00 30.50 ? 541 HOH A O    1 
HETATM 2539 O  O    . HOH G 6 .   ? 8.007   3.102   27.585  1.00 28.64 ? 542 HOH A O    1 
HETATM 2540 O  O    . HOH G 6 .   ? -12.028 10.598  5.789   1.00 25.77 ? 543 HOH A O    1 
HETATM 2541 O  O    . HOH G 6 .   ? -13.230 13.309  31.771  1.00 26.34 ? 544 HOH A O    1 
HETATM 2542 O  O    . HOH G 6 .   ? -24.756 4.830   7.862   1.00 27.88 ? 545 HOH A O    1 
HETATM 2543 O  O    . HOH G 6 .   ? -28.325 5.259   25.582  1.00 26.75 ? 546 HOH A O    1 
HETATM 2544 O  O    . HOH G 6 .   ? -5.372  3.511   -5.814  1.00 30.87 ? 547 HOH A O    1 
HETATM 2545 O  O    . HOH G 6 .   ? -31.015 -3.637  7.600   1.00 31.69 ? 548 HOH A O    1 
HETATM 2546 O  O    . HOH G 6 .   ? 3.042   -14.775 2.136   1.00 26.34 ? 549 HOH A O    1 
HETATM 2547 O  O    . HOH G 6 .   ? -25.896 -10.644 17.572  1.00 24.31 ? 550 HOH A O    1 
HETATM 2548 O  O    . HOH G 6 .   ? -4.686  -8.480  31.087  1.00 16.77 ? 551 HOH A O    1 
HETATM 2549 O  O    . HOH G 6 .   ? 6.560   -5.881  6.759   1.00 22.35 ? 552 HOH A O    1 
HETATM 2550 O  O    . HOH G 6 .   ? -13.559 -16.800 0.004   1.00 25.64 ? 553 HOH A O    1 
HETATM 2551 O  O    . HOH G 6 .   ? -26.476 -7.688  30.429  1.00 26.59 ? 554 HOH A O    1 
HETATM 2552 O  O    . HOH G 6 .   ? -21.334 -19.691 6.614   1.00 22.35 ? 555 HOH A O    1 
HETATM 2553 O  O    . HOH G 6 .   ? -13.137 -22.431 12.153  1.00 33.99 ? 556 HOH A O    1 
HETATM 2554 O  O    . HOH G 6 .   ? 10.370  5.536   12.981  1.00 34.63 ? 557 HOH A O    1 
HETATM 2555 O  O    . HOH G 6 .   ? -25.169 9.552   12.813  1.00 23.58 ? 558 HOH A O    1 
HETATM 2556 O  O    . HOH G 6 .   ? -20.232 -4.354  41.299  1.00 23.78 ? 559 HOH A O    1 
HETATM 2557 O  O    . HOH G 6 .   ? 4.124   -11.482 23.445  1.00 39.40 ? 560 HOH A O    1 
HETATM 2558 O  O    . HOH G 6 .   ? -23.631 -3.634  3.416   1.00 41.76 ? 561 HOH A O    1 
HETATM 2559 O  O    . HOH G 6 .   ? -16.368 17.242  26.026  1.00 30.63 ? 562 HOH A O    1 
HETATM 2560 O  O    . HOH G 6 .   ? 0.446   -9.739  -5.550  1.00 26.16 ? 563 HOH A O    1 
HETATM 2561 O  O    . HOH G 6 .   ? 1.791   -15.763 9.136   1.00 21.52 ? 564 HOH A O    1 
HETATM 2562 O  O    . HOH G 6 .   ? -12.652 3.545   -6.954  1.00 28.07 ? 565 HOH A O    1 
HETATM 2563 O  O    . HOH G 6 .   ? -20.973 8.283   30.078  1.00 22.20 ? 566 HOH A O    1 
HETATM 2564 O  O    . HOH G 6 .   ? 1.389   -16.352 5.072   1.00 33.65 ? 567 HOH A O    1 
HETATM 2565 O  O    . HOH G 6 .   ? -10.887 8.592   7.547   1.00 23.60 ? 568 HOH A O    1 
HETATM 2566 O  O    . HOH G 6 .   ? 2.775   -13.618 8.128   1.00 20.91 ? 569 HOH A O    1 
HETATM 2567 O  O    . HOH G 6 .   ? 1.454   -17.830 7.302   1.00 28.54 ? 570 HOH A O    1 
HETATM 2568 O  O    . HOH G 6 .   ? -11.651 10.615  0.605   1.00 30.37 ? 571 HOH A O    1 
HETATM 2569 O  O    . HOH G 6 .   ? -23.571 -0.363  34.555  1.00 22.75 ? 572 HOH A O    1 
HETATM 2570 O  O    . HOH G 6 .   ? -9.041  6.552   -3.828  1.00 34.42 ? 573 HOH A O    1 
HETATM 2571 O  O    . HOH G 6 .   ? -12.918 -18.254 32.394  1.00 31.05 ? 574 HOH A O    1 
HETATM 2572 O  O    . HOH G 6 .   ? -13.094 -0.712  -6.037  1.00 34.23 ? 575 HOH A O    1 
HETATM 2573 O  O    . HOH G 6 .   ? 1.147   -9.849  31.591  1.00 25.00 ? 576 HOH A O    1 
HETATM 2574 O  O    . HOH G 6 .   ? -0.799  14.378  16.013  1.00 23.35 ? 577 HOH A O    1 
HETATM 2575 O  O    . HOH G 6 .   ? 10.090  -8.643  8.112   1.00 28.65 ? 578 HOH A O    1 
HETATM 2576 O  O    . HOH G 6 .   ? 2.636   1.406   -2.233  1.00 30.99 ? 579 HOH A O    1 
HETATM 2577 O  O    . HOH G 6 .   ? -25.674 -8.477  11.311  1.00 37.19 ? 580 HOH A O    1 
HETATM 2578 O  O    . HOH G 6 .   ? -24.262 -2.447  28.775  1.00 30.48 ? 581 HOH A O    1 
HETATM 2579 O  O    . HOH G 6 .   ? -24.009 -0.253  1.298   1.00 28.14 ? 582 HOH A O    1 
HETATM 2580 O  O    . HOH G 6 .   ? 4.797   -3.566  3.175   1.00 30.61 ? 583 HOH A O    1 
HETATM 2581 O  O    . HOH G 6 .   ? -25.835 -9.550  14.788  1.00 31.38 ? 584 HOH A O    1 
HETATM 2582 O  O    . HOH G 6 .   ? 4.602   -0.606  -5.567  1.00 31.23 ? 585 HOH A O    1 
HETATM 2583 O  O    . HOH G 6 .   ? -23.676 8.288   3.534   1.00 19.44 ? 586 HOH A O    1 
HETATM 2584 O  O    . HOH G 6 .   ? 2.735   2.934   8.435   1.00 31.31 ? 587 HOH A O    1 
HETATM 2585 O  O    . HOH G 6 .   ? -25.848 8.029   6.050   1.00 29.76 ? 588 HOH A O    1 
HETATM 2586 O  O    . HOH G 6 .   ? -21.454 0.565   0.301   1.00 31.59 ? 589 HOH A O    1 
HETATM 2587 O  O    . HOH G 6 .   ? 3.167   2.910   0.062   1.00 31.41 ? 590 HOH A O    1 
HETATM 2588 O  O    . HOH G 6 .   ? -25.534 4.585   4.192   1.00 28.90 ? 591 HOH A O    1 
HETATM 2589 O  O    . HOH G 6 .   ? 8.988   7.723   18.462  1.00 34.15 ? 592 HOH A O    1 
HETATM 2590 O  O    . HOH G 6 .   ? -15.276 6.007   32.727  1.00 25.29 ? 593 HOH A O    1 
HETATM 2591 O  O    . HOH G 6 .   ? -7.707  8.068   29.601  1.00 36.50 ? 594 HOH A O    1 
HETATM 2592 O  O    . HOH G 6 .   ? 5.192   9.112   21.878  1.00 28.17 ? 595 HOH A O    1 
HETATM 2593 O  O    . HOH G 6 .   ? -16.514 -15.465 32.688  1.00 34.23 ? 596 HOH A O    1 
HETATM 2594 O  O    . HOH G 6 .   ? 1.221   2.347   35.915  1.00 34.89 ? 597 HOH A O    1 
HETATM 2595 O  O    . HOH G 6 .   ? -27.520 -5.491  27.361  1.00 26.92 ? 598 HOH A O    1 
HETATM 2596 O  O    . HOH G 6 .   ? -7.001  -8.539  -7.094  1.00 27.83 ? 599 HOH A O    1 
HETATM 2597 O  O    . HOH G 6 .   ? -10.529 13.561  8.647   1.00 28.04 ? 600 HOH A O    1 
HETATM 2598 O  O    . HOH G 6 .   ? -25.363 8.839   26.065  1.00 27.35 ? 601 HOH A O    1 
HETATM 2599 O  O    . HOH G 6 .   ? 6.321   -2.746  6.743   1.00 31.51 ? 602 HOH A O    1 
HETATM 2600 O  O    . HOH G 6 .   ? -4.401  -5.650  -8.183  1.00 35.33 ? 603 HOH A O    1 
HETATM 2601 O  O    . HOH G 6 .   ? -19.257 2.106   40.840  1.00 32.42 ? 604 HOH A O    1 
HETATM 2602 O  O    . HOH G 6 .   ? -20.618 -4.818  -3.659  1.00 33.38 ? 605 HOH A O    1 
HETATM 2603 O  O    . HOH G 6 .   ? -5.536  -12.525 -5.217  1.00 27.25 ? 606 HOH A O    1 
HETATM 2604 O  O    . HOH G 6 .   ? -10.395 15.812  29.562  1.00 33.00 ? 607 HOH A O    1 
HETATM 2605 O  O    . HOH G 6 .   ? -10.868 -5.848  38.164  1.00 28.55 ? 608 HOH A O    1 
HETATM 2606 O  O    . HOH G 6 .   ? -23.053 -14.978 16.200  1.00 35.80 ? 609 HOH A O    1 
HETATM 2607 O  O    . HOH G 6 .   ? -14.193 3.581   33.233  1.00 22.50 ? 610 HOH A O    1 
HETATM 2608 O  O    . HOH G 6 .   ? -4.792  -8.128  -8.331  1.00 37.48 ? 611 HOH A O    1 
HETATM 2609 O  O    . HOH G 6 .   ? 9.897   0.035   13.966  1.00 35.14 ? 612 HOH A O    1 
HETATM 2610 O  O    . HOH G 6 .   ? 11.389  -0.430  15.946  1.00 23.77 ? 613 HOH A O    1 
HETATM 2611 O  O    . HOH G 6 .   ? 14.462  0.091   15.061  1.00 26.46 ? 614 HOH A O    1 
HETATM 2612 O  O    . HOH G 6 .   ? -11.811 9.064   32.864  1.00 24.79 ? 615 HOH A O    1 
HETATM 2613 O  O    . HOH G 6 .   ? -12.548 6.355   30.972  1.00 27.71 ? 616 HOH A O    1 
HETATM 2614 O  O    . HOH G 6 .   ? -12.651 4.332   35.090  1.00 43.80 ? 617 HOH A O    1 
HETATM 2615 O  O    . HOH G 6 .   ? -24.004 -0.375  31.804  1.00 30.00 ? 618 HOH A O    1 
HETATM 2616 O  O    . HOH G 6 .   ? -25.917 -1.173  35.075  1.00 26.77 ? 619 HOH A O    1 
HETATM 2617 O  O    . HOH G 6 .   ? -14.509 0.417   42.548  1.00 29.10 ? 620 HOH A O    1 
HETATM 2618 O  O    . HOH G 6 .   ? -1.389  1.849   11.674  1.00 37.91 ? 621 HOH A O    1 
HETATM 2619 O  O    . HOH G 6 .   ? 0.205   3.405   10.142  1.00 31.58 ? 622 HOH A O    1 
HETATM 2620 O  O    . HOH G 6 .   ? 3.565   4.361   10.750  1.00 29.54 ? 623 HOH A O    1 
HETATM 2621 O  O    . HOH G 6 .   ? -11.376 0.956   -7.739  1.00 30.05 ? 624 HOH A O    1 
HETATM 2622 O  O    . HOH G 6 .   ? 5.829   -14.043 8.927   1.00 32.91 ? 625 HOH A O    1 
HETATM 2623 O  O    . HOH G 6 .   ? 6.190   -11.003 15.197  1.00 27.21 ? 626 HOH A O    1 
HETATM 2624 O  O    . HOH G 6 .   ? 5.014   -11.184 19.028  1.00 30.71 ? 627 HOH A O    1 
HETATM 2625 O  O    . HOH G 6 .   ? -28.302 5.746   19.200  1.00 22.17 ? 628 HOH A O    1 
HETATM 2626 O  O    . HOH G 6 .   ? -28.076 6.252   21.474  1.00 30.24 ? 629 HOH A O    1 
HETATM 2627 O  O    . HOH G 6 .   ? -21.836 19.522  12.167  1.00 24.85 ? 630 HOH A O    1 
HETATM 2628 O  O    . HOH G 6 .   ? -22.820 -9.747  25.240  1.00 18.97 ? 631 HOH A O    1 
HETATM 2629 O  O    . HOH G 6 .   ? -2.744  -8.944  34.721  1.00 27.60 ? 632 HOH A O    1 
HETATM 2630 O  O    . HOH G 6 .   ? -5.375  -9.736  33.600  1.00 32.43 ? 633 HOH A O    1 
HETATM 2631 O  O    . HOH G 6 .   ? 1.102   11.432  15.793  1.00 32.06 ? 634 HOH A O    1 
HETATM 2632 O  O    . HOH G 6 .   ? -3.935  -1.118  11.385  1.00 24.77 ? 635 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   3   HIS HIS 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 J74 1   262 1   J74 J74 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 BCN 1   266 1   BCN BCN A . 
G 6 HOH 1   126 126 HOH HOH A . 
G 6 HOH 2   267 267 HOH HOH A . 
G 6 HOH 3   268 268 HOH HOH A . 
G 6 HOH 4   269 269 HOH HOH A . 
G 6 HOH 5   270 270 HOH HOH A . 
G 6 HOH 6   271 271 HOH HOH A . 
G 6 HOH 7   272 272 HOH HOH A . 
G 6 HOH 8   273 273 HOH HOH A . 
G 6 HOH 9   274 274 HOH HOH A . 
G 6 HOH 10  275 275 HOH HOH A . 
G 6 HOH 11  276 276 HOH HOH A . 
G 6 HOH 12  277 277 HOH HOH A . 
G 6 HOH 13  278 278 HOH HOH A . 
G 6 HOH 14  279 279 HOH HOH A . 
G 6 HOH 15  280 280 HOH HOH A . 
G 6 HOH 16  281 281 HOH HOH A . 
G 6 HOH 17  282 282 HOH HOH A . 
G 6 HOH 18  283 283 HOH HOH A . 
G 6 HOH 19  284 284 HOH HOH A . 
G 6 HOH 20  285 285 HOH HOH A . 
G 6 HOH 21  286 286 HOH HOH A . 
G 6 HOH 22  287 287 HOH HOH A . 
G 6 HOH 23  288 288 HOH HOH A . 
G 6 HOH 24  289 289 HOH HOH A . 
G 6 HOH 25  290 290 HOH HOH A . 
G 6 HOH 26  291 291 HOH HOH A . 
G 6 HOH 27  292 292 HOH HOH A . 
G 6 HOH 28  293 293 HOH HOH A . 
G 6 HOH 29  294 294 HOH HOH A . 
G 6 HOH 30  295 295 HOH HOH A . 
G 6 HOH 31  296 296 HOH HOH A . 
G 6 HOH 32  297 297 HOH HOH A . 
G 6 HOH 33  298 298 HOH HOH A . 
G 6 HOH 34  299 299 HOH HOH A . 
G 6 HOH 35  300 300 HOH HOH A . 
G 6 HOH 36  301 301 HOH HOH A . 
G 6 HOH 37  302 302 HOH HOH A . 
G 6 HOH 38  303 303 HOH HOH A . 
G 6 HOH 39  304 1   HOH HOH A . 
G 6 HOH 40  305 305 HOH HOH A . 
G 6 HOH 41  306 306 HOH HOH A . 
G 6 HOH 42  307 307 HOH HOH A . 
G 6 HOH 43  308 308 HOH HOH A . 
G 6 HOH 44  309 309 HOH HOH A . 
G 6 HOH 45  310 310 HOH HOH A . 
G 6 HOH 46  311 311 HOH HOH A . 
G 6 HOH 47  312 312 HOH HOH A . 
G 6 HOH 48  313 313 HOH HOH A . 
G 6 HOH 49  314 314 HOH HOH A . 
G 6 HOH 50  315 315 HOH HOH A . 
G 6 HOH 51  316 316 HOH HOH A . 
G 6 HOH 52  317 2   HOH HOH A . 
G 6 HOH 53  318 3   HOH HOH A . 
G 6 HOH 54  319 319 HOH HOH A . 
G 6 HOH 55  320 320 HOH HOH A . 
G 6 HOH 56  321 321 HOH HOH A . 
G 6 HOH 57  322 322 HOH HOH A . 
G 6 HOH 58  323 323 HOH HOH A . 
G 6 HOH 59  324 324 HOH HOH A . 
G 6 HOH 60  325 325 HOH HOH A . 
G 6 HOH 61  326 326 HOH HOH A . 
G 6 HOH 62  327 327 HOH HOH A . 
G 6 HOH 63  328 328 HOH HOH A . 
G 6 HOH 64  329 329 HOH HOH A . 
G 6 HOH 65  330 330 HOH HOH A . 
G 6 HOH 66  331 331 HOH HOH A . 
G 6 HOH 67  332 332 HOH HOH A . 
G 6 HOH 68  333 333 HOH HOH A . 
G 6 HOH 69  334 4   HOH HOH A . 
G 6 HOH 70  335 335 HOH HOH A . 
G 6 HOH 71  336 336 HOH HOH A . 
G 6 HOH 72  337 337 HOH HOH A . 
G 6 HOH 73  338 338 HOH HOH A . 
G 6 HOH 74  339 339 HOH HOH A . 
G 6 HOH 75  340 340 HOH HOH A . 
G 6 HOH 76  341 341 HOH HOH A . 
G 6 HOH 77  342 342 HOH HOH A . 
G 6 HOH 78  343 343 HOH HOH A . 
G 6 HOH 79  344 344 HOH HOH A . 
G 6 HOH 80  345 345 HOH HOH A . 
G 6 HOH 81  346 346 HOH HOH A . 
G 6 HOH 82  347 347 HOH HOH A . 
G 6 HOH 83  348 348 HOH HOH A . 
G 6 HOH 84  349 349 HOH HOH A . 
G 6 HOH 85  350 350 HOH HOH A . 
G 6 HOH 86  351 351 HOH HOH A . 
G 6 HOH 87  352 352 HOH HOH A . 
G 6 HOH 88  353 353 HOH HOH A . 
G 6 HOH 89  354 354 HOH HOH A . 
G 6 HOH 90  355 355 HOH HOH A . 
G 6 HOH 91  356 356 HOH HOH A . 
G 6 HOH 92  357 357 HOH HOH A . 
G 6 HOH 93  358 358 HOH HOH A . 
G 6 HOH 94  359 359 HOH HOH A . 
G 6 HOH 95  360 360 HOH HOH A . 
G 6 HOH 96  361 361 HOH HOH A . 
G 6 HOH 97  362 362 HOH HOH A . 
G 6 HOH 98  363 363 HOH HOH A . 
G 6 HOH 99  364 364 HOH HOH A . 
G 6 HOH 100 365 365 HOH HOH A . 
G 6 HOH 101 366 366 HOH HOH A . 
G 6 HOH 102 367 367 HOH HOH A . 
G 6 HOH 103 368 368 HOH HOH A . 
G 6 HOH 104 369 369 HOH HOH A . 
G 6 HOH 105 370 370 HOH HOH A . 
G 6 HOH 106 371 5   HOH HOH A . 
G 6 HOH 107 372 372 HOH HOH A . 
G 6 HOH 108 373 373 HOH HOH A . 
G 6 HOH 109 374 374 HOH HOH A . 
G 6 HOH 110 375 375 HOH HOH A . 
G 6 HOH 111 376 376 HOH HOH A . 
G 6 HOH 112 377 377 HOH HOH A . 
G 6 HOH 113 378 6   HOH HOH A . 
G 6 HOH 114 379 7   HOH HOH A . 
G 6 HOH 115 380 8   HOH HOH A . 
G 6 HOH 116 381 9   HOH HOH A . 
G 6 HOH 117 382 10  HOH HOH A . 
G 6 HOH 118 383 11  HOH HOH A . 
G 6 HOH 119 384 12  HOH HOH A . 
G 6 HOH 120 385 13  HOH HOH A . 
G 6 HOH 121 386 14  HOH HOH A . 
G 6 HOH 122 387 15  HOH HOH A . 
G 6 HOH 123 388 16  HOH HOH A . 
G 6 HOH 124 389 17  HOH HOH A . 
G 6 HOH 125 390 18  HOH HOH A . 
G 6 HOH 126 391 19  HOH HOH A . 
G 6 HOH 127 392 20  HOH HOH A . 
G 6 HOH 128 393 21  HOH HOH A . 
G 6 HOH 129 394 22  HOH HOH A . 
G 6 HOH 130 395 23  HOH HOH A . 
G 6 HOH 131 396 24  HOH HOH A . 
G 6 HOH 132 397 25  HOH HOH A . 
G 6 HOH 133 398 26  HOH HOH A . 
G 6 HOH 134 399 27  HOH HOH A . 
G 6 HOH 135 400 28  HOH HOH A . 
G 6 HOH 136 401 29  HOH HOH A . 
G 6 HOH 137 402 30  HOH HOH A . 
G 6 HOH 138 403 31  HOH HOH A . 
G 6 HOH 139 404 32  HOH HOH A . 
G 6 HOH 140 405 33  HOH HOH A . 
G 6 HOH 141 406 34  HOH HOH A . 
G 6 HOH 142 407 35  HOH HOH A . 
G 6 HOH 143 408 36  HOH HOH A . 
G 6 HOH 144 409 37  HOH HOH A . 
G 6 HOH 145 410 38  HOH HOH A . 
G 6 HOH 146 411 39  HOH HOH A . 
G 6 HOH 147 412 40  HOH HOH A . 
G 6 HOH 148 413 41  HOH HOH A . 
G 6 HOH 149 414 42  HOH HOH A . 
G 6 HOH 150 415 43  HOH HOH A . 
G 6 HOH 151 416 44  HOH HOH A . 
G 6 HOH 152 417 45  HOH HOH A . 
G 6 HOH 153 418 46  HOH HOH A . 
G 6 HOH 154 419 47  HOH HOH A . 
G 6 HOH 155 420 48  HOH HOH A . 
G 6 HOH 156 421 49  HOH HOH A . 
G 6 HOH 157 422 50  HOH HOH A . 
G 6 HOH 158 423 51  HOH HOH A . 
G 6 HOH 159 424 52  HOH HOH A . 
G 6 HOH 160 425 53  HOH HOH A . 
G 6 HOH 161 426 54  HOH HOH A . 
G 6 HOH 162 427 55  HOH HOH A . 
G 6 HOH 163 428 56  HOH HOH A . 
G 6 HOH 164 429 57  HOH HOH A . 
G 6 HOH 165 430 58  HOH HOH A . 
G 6 HOH 166 431 59  HOH HOH A . 
G 6 HOH 167 432 60  HOH HOH A . 
G 6 HOH 168 433 61  HOH HOH A . 
G 6 HOH 169 434 62  HOH HOH A . 
G 6 HOH 170 435 63  HOH HOH A . 
G 6 HOH 171 436 64  HOH HOH A . 
G 6 HOH 172 437 65  HOH HOH A . 
G 6 HOH 173 438 66  HOH HOH A . 
G 6 HOH 174 439 67  HOH HOH A . 
G 6 HOH 175 440 68  HOH HOH A . 
G 6 HOH 176 441 69  HOH HOH A . 
G 6 HOH 177 442 70  HOH HOH A . 
G 6 HOH 178 443 71  HOH HOH A . 
G 6 HOH 179 444 72  HOH HOH A . 
G 6 HOH 180 445 73  HOH HOH A . 
G 6 HOH 181 446 74  HOH HOH A . 
G 6 HOH 182 447 75  HOH HOH A . 
G 6 HOH 183 448 76  HOH HOH A . 
G 6 HOH 184 449 77  HOH HOH A . 
G 6 HOH 185 450 78  HOH HOH A . 
G 6 HOH 186 451 79  HOH HOH A . 
G 6 HOH 187 452 80  HOH HOH A . 
G 6 HOH 188 453 81  HOH HOH A . 
G 6 HOH 189 454 82  HOH HOH A . 
G 6 HOH 190 455 83  HOH HOH A . 
G 6 HOH 191 456 84  HOH HOH A . 
G 6 HOH 192 457 85  HOH HOH A . 
G 6 HOH 193 458 86  HOH HOH A . 
G 6 HOH 194 459 87  HOH HOH A . 
G 6 HOH 195 460 88  HOH HOH A . 
G 6 HOH 196 461 89  HOH HOH A . 
G 6 HOH 197 462 90  HOH HOH A . 
G 6 HOH 198 463 91  HOH HOH A . 
G 6 HOH 199 464 92  HOH HOH A . 
G 6 HOH 200 465 93  HOH HOH A . 
G 6 HOH 201 466 94  HOH HOH A . 
G 6 HOH 202 467 95  HOH HOH A . 
G 6 HOH 203 468 96  HOH HOH A . 
G 6 HOH 204 469 97  HOH HOH A . 
G 6 HOH 205 470 98  HOH HOH A . 
G 6 HOH 206 471 99  HOH HOH A . 
G 6 HOH 207 472 100 HOH HOH A . 
G 6 HOH 208 473 101 HOH HOH A . 
G 6 HOH 209 474 102 HOH HOH A . 
G 6 HOH 210 475 103 HOH HOH A . 
G 6 HOH 211 476 104 HOH HOH A . 
G 6 HOH 212 477 105 HOH HOH A . 
G 6 HOH 213 478 106 HOH HOH A . 
G 6 HOH 214 479 107 HOH HOH A . 
G 6 HOH 215 480 108 HOH HOH A . 
G 6 HOH 216 481 109 HOH HOH A . 
G 6 HOH 217 482 110 HOH HOH A . 
G 6 HOH 218 483 111 HOH HOH A . 
G 6 HOH 219 484 112 HOH HOH A . 
G 6 HOH 220 485 113 HOH HOH A . 
G 6 HOH 221 486 114 HOH HOH A . 
G 6 HOH 222 487 115 HOH HOH A . 
G 6 HOH 223 488 116 HOH HOH A . 
G 6 HOH 224 489 117 HOH HOH A . 
G 6 HOH 225 490 118 HOH HOH A . 
G 6 HOH 226 491 119 HOH HOH A . 
G 6 HOH 227 492 120 HOH HOH A . 
G 6 HOH 228 493 121 HOH HOH A . 
G 6 HOH 229 494 122 HOH HOH A . 
G 6 HOH 230 495 123 HOH HOH A . 
G 6 HOH 231 496 124 HOH HOH A . 
G 6 HOH 232 497 125 HOH HOH A . 
G 6 HOH 233 498 127 HOH HOH A . 
G 6 HOH 234 499 128 HOH HOH A . 
G 6 HOH 235 500 129 HOH HOH A . 
G 6 HOH 236 501 130 HOH HOH A . 
G 6 HOH 237 502 131 HOH HOH A . 
G 6 HOH 238 503 132 HOH HOH A . 
G 6 HOH 239 504 133 HOH HOH A . 
G 6 HOH 240 505 134 HOH HOH A . 
G 6 HOH 241 506 135 HOH HOH A . 
G 6 HOH 242 507 136 HOH HOH A . 
G 6 HOH 243 508 137 HOH HOH A . 
G 6 HOH 244 509 138 HOH HOH A . 
G 6 HOH 245 510 139 HOH HOH A . 
G 6 HOH 246 511 140 HOH HOH A . 
G 6 HOH 247 512 141 HOH HOH A . 
G 6 HOH 248 513 142 HOH HOH A . 
G 6 HOH 249 514 143 HOH HOH A . 
G 6 HOH 250 515 144 HOH HOH A . 
G 6 HOH 251 516 145 HOH HOH A . 
G 6 HOH 252 517 146 HOH HOH A . 
G 6 HOH 253 518 147 HOH HOH A . 
G 6 HOH 254 519 148 HOH HOH A . 
G 6 HOH 255 520 149 HOH HOH A . 
G 6 HOH 256 521 150 HOH HOH A . 
G 6 HOH 257 522 151 HOH HOH A . 
G 6 HOH 258 523 152 HOH HOH A . 
G 6 HOH 259 524 153 HOH HOH A . 
G 6 HOH 260 525 154 HOH HOH A . 
G 6 HOH 261 526 155 HOH HOH A . 
G 6 HOH 262 527 156 HOH HOH A . 
G 6 HOH 263 528 157 HOH HOH A . 
G 6 HOH 264 529 158 HOH HOH A . 
G 6 HOH 265 530 159 HOH HOH A . 
G 6 HOH 266 531 160 HOH HOH A . 
G 6 HOH 267 532 161 HOH HOH A . 
G 6 HOH 268 533 162 HOH HOH A . 
G 6 HOH 269 534 163 HOH HOH A . 
G 6 HOH 270 535 164 HOH HOH A . 
G 6 HOH 271 536 165 HOH HOH A . 
G 6 HOH 272 537 166 HOH HOH A . 
G 6 HOH 273 538 167 HOH HOH A . 
G 6 HOH 274 539 168 HOH HOH A . 
G 6 HOH 275 540 169 HOH HOH A . 
G 6 HOH 276 541 170 HOH HOH A . 
G 6 HOH 277 542 171 HOH HOH A . 
G 6 HOH 278 543 172 HOH HOH A . 
G 6 HOH 279 544 173 HOH HOH A . 
G 6 HOH 280 545 174 HOH HOH A . 
G 6 HOH 281 546 175 HOH HOH A . 
G 6 HOH 282 547 176 HOH HOH A . 
G 6 HOH 283 548 177 HOH HOH A . 
G 6 HOH 284 549 178 HOH HOH A . 
G 6 HOH 285 550 179 HOH HOH A . 
G 6 HOH 286 551 180 HOH HOH A . 
G 6 HOH 287 552 181 HOH HOH A . 
G 6 HOH 288 553 182 HOH HOH A . 
G 6 HOH 289 554 183 HOH HOH A . 
G 6 HOH 290 555 184 HOH HOH A . 
G 6 HOH 291 556 185 HOH HOH A . 
G 6 HOH 292 557 186 HOH HOH A . 
G 6 HOH 293 558 187 HOH HOH A . 
G 6 HOH 294 559 188 HOH HOH A . 
G 6 HOH 295 560 189 HOH HOH A . 
G 6 HOH 296 561 190 HOH HOH A . 
G 6 HOH 297 562 191 HOH HOH A . 
G 6 HOH 298 563 192 HOH HOH A . 
G 6 HOH 299 564 193 HOH HOH A . 
G 6 HOH 300 565 194 HOH HOH A . 
G 6 HOH 301 566 195 HOH HOH A . 
G 6 HOH 302 567 196 HOH HOH A . 
G 6 HOH 303 568 197 HOH HOH A . 
G 6 HOH 304 569 198 HOH HOH A . 
G 6 HOH 305 570 199 HOH HOH A . 
G 6 HOH 306 571 200 HOH HOH A . 
G 6 HOH 307 572 201 HOH HOH A . 
G 6 HOH 308 573 202 HOH HOH A . 
G 6 HOH 309 574 203 HOH HOH A . 
G 6 HOH 310 575 204 HOH HOH A . 
G 6 HOH 311 576 205 HOH HOH A . 
G 6 HOH 312 577 206 HOH HOH A . 
G 6 HOH 313 578 208 HOH HOH A . 
G 6 HOH 314 579 209 HOH HOH A . 
G 6 HOH 315 580 210 HOH HOH A . 
G 6 HOH 316 581 211 HOH HOH A . 
G 6 HOH 317 582 212 HOH HOH A . 
G 6 HOH 318 583 213 HOH HOH A . 
G 6 HOH 319 584 214 HOH HOH A . 
G 6 HOH 320 585 215 HOH HOH A . 
G 6 HOH 321 586 216 HOH HOH A . 
G 6 HOH 322 587 217 HOH HOH A . 
G 6 HOH 323 588 218 HOH HOH A . 
G 6 HOH 324 589 219 HOH HOH A . 
G 6 HOH 325 590 220 HOH HOH A . 
G 6 HOH 326 591 221 HOH HOH A . 
G 6 HOH 327 592 222 HOH HOH A . 
G 6 HOH 328 593 223 HOH HOH A . 
G 6 HOH 329 594 224 HOH HOH A . 
G 6 HOH 330 595 225 HOH HOH A . 
G 6 HOH 331 596 226 HOH HOH A . 
G 6 HOH 332 597 227 HOH HOH A . 
G 6 HOH 333 598 228 HOH HOH A . 
G 6 HOH 334 599 229 HOH HOH A . 
G 6 HOH 335 600 230 HOH HOH A . 
G 6 HOH 336 601 231 HOH HOH A . 
G 6 HOH 337 602 232 HOH HOH A . 
G 6 HOH 338 603 233 HOH HOH A . 
G 6 HOH 339 604 234 HOH HOH A . 
G 6 HOH 340 605 235 HOH HOH A . 
G 6 HOH 341 606 236 HOH HOH A . 
G 6 HOH 342 607 237 HOH HOH A . 
G 6 HOH 343 608 238 HOH HOH A . 
G 6 HOH 344 609 239 HOH HOH A . 
G 6 HOH 345 610 240 HOH HOH A . 
G 6 HOH 346 611 241 HOH HOH A . 
G 6 HOH 347 612 242 HOH HOH A . 
G 6 HOH 348 613 243 HOH HOH A . 
G 6 HOH 349 614 244 HOH HOH A . 
G 6 HOH 350 615 245 HOH HOH A . 
G 6 HOH 351 616 246 HOH HOH A . 
G 6 HOH 352 617 247 HOH HOH A . 
G 6 HOH 353 618 248 HOH HOH A . 
G 6 HOH 354 619 249 HOH HOH A . 
G 6 HOH 355 620 250 HOH HOH A . 
G 6 HOH 356 621 251 HOH HOH A . 
G 6 HOH 357 622 252 HOH HOH A . 
G 6 HOH 358 623 253 HOH HOH A . 
G 6 HOH 359 624 254 HOH HOH A . 
G 6 HOH 360 625 255 HOH HOH A . 
G 6 HOH 361 626 256 HOH HOH A . 
G 6 HOH 362 627 257 HOH HOH A . 
G 6 HOH 363 628 258 HOH HOH A . 
G 6 HOH 364 629 259 HOH HOH A . 
G 6 HOH 365 630 260 HOH HOH A . 
G 6 HOH 366 631 262 HOH HOH A . 
G 6 HOH 367 632 263 HOH HOH A . 
G 6 HOH 368 633 264 HOH HOH A . 
G 6 HOH 369 634 265 HOH HOH A . 
G 6 HOH 370 635 266 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2011-02-16 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2012-05-16 
4 'Structure model' 1 3 2017-11-08 
5 'Structure model' 1 4 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' 'Database references'       
3 4 'Structure model' 'Refinement description'    
4 5 'Structure model' 'Data collection'           
5 5 'Structure model' 'Database references'       
6 5 'Structure model' 'Derived calculations'      
7 5 '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 4 'Structure model' software                      
2 5 'Structure model' chem_comp_atom                
3 5 'Structure model' chem_comp_bond                
4 5 'Structure model' database_2                    
5 5 'Structure model' diffrn_source                 
6 5 'Structure model' pdbx_initial_refinement_model 
7 5 '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 5 'Structure model' '_database_2.pdbx_DOI'                 
2 5 'Structure model' '_database_2.pdbx_database_accession'  
3 5 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
4 5 'Structure model' '_struct_site.pdbx_auth_asym_id'       
5 5 'Structure model' '_struct_site.pdbx_auth_comp_id'       
6 5 'Structure model' '_struct_site.pdbx_auth_seq_id'        
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MAR345 'data collection' 'v. 0.9.7 on RedHat Linux 8' ? 1 
REFMAC refinement        5.2.0019                     ? 2 
MOSFLM 'data reduction'  .                            ? 3 
SCALA  'data scaling'    .                            ? 4 
# 
_pdbx_entry_details.entry_id                 3M2N 
_pdbx_entry_details.nonpolymer_details       'METAL ION NATURALLY OCCURS IN CARBONIC ANHYDRASES.' 
_pdbx_entry_details.sequence_details         '126 IS SKIPPED IN THE NUMBERING.' 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A LYS 9   ? A O A HOH 578 ? ? 1.81 
2 1 CE1 A HIS 64  ? B O A HOH 621 ? ? 2.11 
3 1 CB  A LYS 9   ? A O A HOH 329 ? ? 2.14 
4 1 OD2 A ASP 165 ? B O A HOH 268 ? ? 2.16 
5 1 O   A THR 37  ? ? O A HOH 608 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE1 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLN 
_pdbx_validate_symm_contact.auth_seq_id_1     137 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     367 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_565 
_pdbx_validate_symm_contact.dist              2.18 
# 
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 N  A GLY 63  ? ? CA  A GLY 63  ? ? 1.366 1.456 -0.090 0.015 N 
2 1 CG A TRP 209 ? ? CD1 A TRP 209 ? ? 1.448 1.363 0.085  0.014 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 101 ? ? CG A ASP 101 ? ? OD1 A ASP 101 ? ? 126.68 118.30 8.38  0.90 N 
2 1 CB A ASP 101 ? ? CG A ASP 101 ? ? OD2 A ASP 101 ? ? 112.20 118.30 -6.10 0.90 N 
3 1 CB A ASP 130 ? ? CG A ASP 130 ? ? OD1 A ASP 130 ? ? 124.22 118.30 5.92  0.90 N 
4 1 CB A PHE 226 ? ? CG A PHE 226 ? ? CD2 A PHE 226 ? ? 115.09 120.80 -5.71 0.70 N 
5 1 CB A PHE 226 ? ? CG A PHE 226 ? ? CD1 A PHE 226 ? ? 125.71 120.80 4.91  0.70 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 TYR A 7   ? B -117.62 54.91   
2  1 HIS A 10  ? A 101.61  -20.65  
3  1 ASN A 11  ? ? -152.36 14.40   
4  1 ARG A 27  ? ? -144.06 54.97   
5  1 ALA A 65  ? ? -171.42 -169.63 
6  1 LYS A 76  ? A -115.75 -95.18  
7  1 ALA A 77  ? B 61.29   91.00   
8  1 LYS A 111 ? ? 74.52   -2.80   
9  1 PHE A 176 ? ? -164.21 79.12   
10 1 ASN A 244 ? ? -96.02  48.43   
11 1 LYS A 252 ? ? 58.48   -141.70 
12 1 LYS A 252 ? ? 58.48   -136.03 
13 1 ASN A 253 ? B -92.37  57.94   
# 
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 
# 
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  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
J74 N1   N  Y N 217 
J74 C2   C  Y N 218 
J74 N3   N  Y N 219 
J74 C4   C  Y N 220 
J74 C5   C  Y N 221 
J74 C6   C  Y N 222 
J74 N7   N  N N 223 
J74 C8   C  Y N 224 
J74 C9   C  Y N 225 
J74 C10  C  Y N 226 
J74 C11  C  Y N 227 
J74 C12  C  Y N 228 
J74 C13  C  Y N 229 
J74 S14  S  N N 230 
J74 O15  O  N N 231 
J74 O16  O  N N 232 
J74 N17  N  N N 233 
J74 N18  N  N N 234 
J74 O19  O  N N 235 
J74 O20  O  N N 236 
J74 CL21 CL N N 237 
J74 C22  C  N N 238 
J74 C23  C  N N 239 
J74 H2   H  N N 240 
J74 HN7  H  N N 241 
J74 H9   H  N N 242 
J74 H10  H  N N 243 
J74 H12  H  N N 244 
J74 H13  H  N N 245 
J74 HN17 H  N N 246 
J74 HN1A H  N N 247 
J74 H22  H  N N 248 
J74 H22A H  N N 249 
J74 H23  H  N N 250 
J74 H23A H  N N 251 
LEU N    N  N N 252 
LEU CA   C  N S 253 
LEU C    C  N N 254 
LEU O    O  N N 255 
LEU CB   C  N N 256 
LEU CG   C  N N 257 
LEU CD1  C  N N 258 
LEU CD2  C  N N 259 
LEU OXT  O  N N 260 
LEU H    H  N N 261 
LEU H2   H  N N 262 
LEU HA   H  N N 263 
LEU HB2  H  N N 264 
LEU HB3  H  N N 265 
LEU HG   H  N N 266 
LEU HD11 H  N N 267 
LEU HD12 H  N N 268 
LEU HD13 H  N N 269 
LEU HD21 H  N N 270 
LEU HD22 H  N N 271 
LEU HD23 H  N N 272 
LEU HXT  H  N N 273 
LYS N    N  N N 274 
LYS CA   C  N S 275 
LYS C    C  N N 276 
LYS O    O  N N 277 
LYS CB   C  N N 278 
LYS CG   C  N N 279 
LYS CD   C  N N 280 
LYS CE   C  N N 281 
LYS NZ   N  N N 282 
LYS OXT  O  N N 283 
LYS H    H  N N 284 
LYS H2   H  N N 285 
LYS HA   H  N N 286 
LYS HB2  H  N N 287 
LYS HB3  H  N N 288 
LYS HG2  H  N N 289 
LYS HG3  H  N N 290 
LYS HD2  H  N N 291 
LYS HD3  H  N N 292 
LYS HE2  H  N N 293 
LYS HE3  H  N N 294 
LYS HZ1  H  N N 295 
LYS HZ2  H  N N 296 
LYS HZ3  H  N N 297 
LYS HXT  H  N N 298 
MET N    N  N N 299 
MET CA   C  N S 300 
MET C    C  N N 301 
MET O    O  N N 302 
MET CB   C  N N 303 
MET CG   C  N N 304 
MET SD   S  N N 305 
MET CE   C  N N 306 
MET OXT  O  N N 307 
MET H    H  N N 308 
MET H2   H  N N 309 
MET HA   H  N N 310 
MET HB2  H  N N 311 
MET HB3  H  N N 312 
MET HG2  H  N N 313 
MET HG3  H  N N 314 
MET HE1  H  N N 315 
MET HE2  H  N N 316 
MET HE3  H  N N 317 
MET HXT  H  N N 318 
PHE N    N  N N 319 
PHE CA   C  N S 320 
PHE C    C  N N 321 
PHE O    O  N N 322 
PHE CB   C  N N 323 
PHE CG   C  Y N 324 
PHE CD1  C  Y N 325 
PHE CD2  C  Y N 326 
PHE CE1  C  Y N 327 
PHE CE2  C  Y N 328 
PHE CZ   C  Y N 329 
PHE OXT  O  N N 330 
PHE H    H  N N 331 
PHE H2   H  N N 332 
PHE HA   H  N N 333 
PHE HB2  H  N N 334 
PHE HB3  H  N N 335 
PHE HD1  H  N N 336 
PHE HD2  H  N N 337 
PHE HE1  H  N N 338 
PHE HE2  H  N N 339 
PHE HZ   H  N N 340 
PHE HXT  H  N N 341 
PRO N    N  N N 342 
PRO CA   C  N S 343 
PRO C    C  N N 344 
PRO O    O  N N 345 
PRO CB   C  N N 346 
PRO CG   C  N N 347 
PRO CD   C  N N 348 
PRO OXT  O  N N 349 
PRO H    H  N N 350 
PRO HA   H  N N 351 
PRO HB2  H  N N 352 
PRO HB3  H  N N 353 
PRO HG2  H  N N 354 
PRO HG3  H  N N 355 
PRO HD2  H  N N 356 
PRO HD3  H  N N 357 
PRO HXT  H  N N 358 
SER N    N  N N 359 
SER CA   C  N S 360 
SER C    C  N N 361 
SER O    O  N N 362 
SER CB   C  N N 363 
SER OG   O  N N 364 
SER OXT  O  N N 365 
SER H    H  N N 366 
SER H2   H  N N 367 
SER HA   H  N N 368 
SER HB2  H  N N 369 
SER HB3  H  N N 370 
SER HG   H  N N 371 
SER HXT  H  N N 372 
THR N    N  N N 373 
THR CA   C  N S 374 
THR C    C  N N 375 
THR O    O  N N 376 
THR CB   C  N R 377 
THR OG1  O  N N 378 
THR CG2  C  N N 379 
THR OXT  O  N N 380 
THR H    H  N N 381 
THR H2   H  N N 382 
THR HA   H  N N 383 
THR HB   H  N N 384 
THR HG1  H  N N 385 
THR HG21 H  N N 386 
THR HG22 H  N N 387 
THR HG23 H  N N 388 
THR HXT  H  N N 389 
TRP N    N  N N 390 
TRP CA   C  N S 391 
TRP C    C  N N 392 
TRP O    O  N N 393 
TRP CB   C  N N 394 
TRP CG   C  Y N 395 
TRP CD1  C  Y N 396 
TRP CD2  C  Y N 397 
TRP NE1  N  Y N 398 
TRP CE2  C  Y N 399 
TRP CE3  C  Y N 400 
TRP CZ2  C  Y N 401 
TRP CZ3  C  Y N 402 
TRP CH2  C  Y N 403 
TRP OXT  O  N N 404 
TRP H    H  N N 405 
TRP H2   H  N N 406 
TRP HA   H  N N 407 
TRP HB2  H  N N 408 
TRP HB3  H  N N 409 
TRP HD1  H  N N 410 
TRP HE1  H  N N 411 
TRP HE3  H  N N 412 
TRP HZ2  H  N N 413 
TRP HZ3  H  N N 414 
TRP HH2  H  N N 415 
TRP HXT  H  N N 416 
TYR N    N  N N 417 
TYR CA   C  N S 418 
TYR C    C  N N 419 
TYR O    O  N N 420 
TYR CB   C  N N 421 
TYR CG   C  Y N 422 
TYR CD1  C  Y N 423 
TYR CD2  C  Y N 424 
TYR CE1  C  Y N 425 
TYR CE2  C  Y N 426 
TYR CZ   C  Y N 427 
TYR OH   O  N N 428 
TYR OXT  O  N N 429 
TYR H    H  N N 430 
TYR H2   H  N N 431 
TYR HA   H  N N 432 
TYR HB2  H  N N 433 
TYR HB3  H  N N 434 
TYR HD1  H  N N 435 
TYR HD2  H  N N 436 
TYR HE1  H  N N 437 
TYR HE2  H  N N 438 
TYR HH   H  N N 439 
TYR HXT  H  N N 440 
VAL N    N  N N 441 
VAL CA   C  N S 442 
VAL C    C  N N 443 
VAL O    O  N N 444 
VAL CB   C  N N 445 
VAL CG1  C  N N 446 
VAL CG2  C  N N 447 
VAL OXT  O  N N 448 
VAL H    H  N N 449 
VAL H2   H  N N 450 
VAL HA   H  N N 451 
VAL HB   H  N N 452 
VAL HG11 H  N N 453 
VAL HG12 H  N N 454 
VAL HG13 H  N N 455 
VAL HG21 H  N N 456 
VAL HG22 H  N N 457 
VAL HG23 H  N N 458 
VAL HXT  H  N N 459 
ZN  ZN   ZN N N 460 
# 
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  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
J74 N1  C2   doub Y N 205 
J74 N1  C6   sing Y N 206 
J74 C2  N3   sing Y N 207 
J74 N3  C4   doub Y N 208 
J74 C4  C5   sing Y N 209 
J74 C4  N7   sing N N 210 
J74 C5  C6   doub Y N 211 
J74 C5  N18  sing N N 212 
J74 C6  CL21 sing N N 213 
J74 N7  C22  sing N N 214 
J74 C8  C9   doub Y N 215 
J74 C8  C13  sing Y N 216 
J74 C8  C23  sing N N 217 
J74 C9  C10  sing Y N 218 
J74 C10 C11  doub Y N 219 
J74 C11 C12  sing Y N 220 
J74 C11 S14  sing N N 221 
J74 C12 C13  doub Y N 222 
J74 S14 O15  doub N N 223 
J74 S14 O16  doub N N 224 
J74 S14 N17  sing N N 225 
J74 N18 O19  sing N N 226 
J74 N18 O20  doub N N 227 
J74 C22 C23  sing N N 228 
J74 C2  H2   sing N N 229 
J74 N7  HN7  sing N N 230 
J74 C9  H9   sing N N 231 
J74 C10 H10  sing N N 232 
J74 C12 H12  sing N N 233 
J74 C13 H13  sing N N 234 
J74 N17 HN17 sing N N 235 
J74 N17 HN1A sing N N 236 
J74 C22 H22  sing N N 237 
J74 C22 H22A sing N N 238 
J74 C23 H23  sing N N 239 
J74 C23 H23A sing N N 240 
LEU N   CA   sing N N 241 
LEU N   H    sing N N 242 
LEU N   H2   sing N N 243 
LEU CA  C    sing N N 244 
LEU CA  CB   sing N N 245 
LEU CA  HA   sing N N 246 
LEU C   O    doub N N 247 
LEU C   OXT  sing N N 248 
LEU CB  CG   sing N N 249 
LEU CB  HB2  sing N N 250 
LEU CB  HB3  sing N N 251 
LEU CG  CD1  sing N N 252 
LEU CG  CD2  sing N N 253 
LEU CG  HG   sing N N 254 
LEU CD1 HD11 sing N N 255 
LEU CD1 HD12 sing N N 256 
LEU CD1 HD13 sing N N 257 
LEU CD2 HD21 sing N N 258 
LEU CD2 HD22 sing N N 259 
LEU CD2 HD23 sing N N 260 
LEU OXT HXT  sing N N 261 
LYS N   CA   sing N N 262 
LYS N   H    sing N N 263 
LYS N   H2   sing N N 264 
LYS CA  C    sing N N 265 
LYS CA  CB   sing N N 266 
LYS CA  HA   sing N N 267 
LYS C   O    doub N N 268 
LYS C   OXT  sing N N 269 
LYS CB  CG   sing N N 270 
LYS CB  HB2  sing N N 271 
LYS CB  HB3  sing N N 272 
LYS CG  CD   sing N N 273 
LYS CG  HG2  sing N N 274 
LYS CG  HG3  sing N N 275 
LYS CD  CE   sing N N 276 
LYS CD  HD2  sing N N 277 
LYS CD  HD3  sing N N 278 
LYS CE  NZ   sing N N 279 
LYS CE  HE2  sing N N 280 
LYS CE  HE3  sing N N 281 
LYS NZ  HZ1  sing N N 282 
LYS NZ  HZ2  sing N N 283 
LYS NZ  HZ3  sing N N 284 
LYS OXT HXT  sing N N 285 
MET N   CA   sing N N 286 
MET N   H    sing N N 287 
MET N   H2   sing N N 288 
MET CA  C    sing N N 289 
MET CA  CB   sing N N 290 
MET CA  HA   sing N N 291 
MET C   O    doub N N 292 
MET C   OXT  sing N N 293 
MET CB  CG   sing N N 294 
MET CB  HB2  sing N N 295 
MET CB  HB3  sing N N 296 
MET CG  SD   sing N N 297 
MET CG  HG2  sing N N 298 
MET CG  HG3  sing N N 299 
MET SD  CE   sing N N 300 
MET CE  HE1  sing N N 301 
MET CE  HE2  sing N N 302 
MET CE  HE3  sing N N 303 
MET OXT HXT  sing N N 304 
PHE N   CA   sing N N 305 
PHE N   H    sing N N 306 
PHE N   H2   sing N N 307 
PHE CA  C    sing N N 308 
PHE CA  CB   sing N N 309 
PHE CA  HA   sing N N 310 
PHE C   O    doub N N 311 
PHE C   OXT  sing N N 312 
PHE CB  CG   sing N N 313 
PHE CB  HB2  sing N N 314 
PHE CB  HB3  sing N N 315 
PHE CG  CD1  doub Y N 316 
PHE CG  CD2  sing Y N 317 
PHE CD1 CE1  sing Y N 318 
PHE CD1 HD1  sing N N 319 
PHE CD2 CE2  doub Y N 320 
PHE CD2 HD2  sing N N 321 
PHE CE1 CZ   doub Y N 322 
PHE CE1 HE1  sing N N 323 
PHE CE2 CZ   sing Y N 324 
PHE CE2 HE2  sing N N 325 
PHE CZ  HZ   sing N N 326 
PHE OXT HXT  sing N N 327 
PRO N   CA   sing N N 328 
PRO N   CD   sing N N 329 
PRO N   H    sing N N 330 
PRO CA  C    sing N N 331 
PRO CA  CB   sing N N 332 
PRO CA  HA   sing N N 333 
PRO C   O    doub N N 334 
PRO C   OXT  sing N N 335 
PRO CB  CG   sing N N 336 
PRO CB  HB2  sing N N 337 
PRO CB  HB3  sing N N 338 
PRO CG  CD   sing N N 339 
PRO CG  HG2  sing N N 340 
PRO CG  HG3  sing N N 341 
PRO CD  HD2  sing N N 342 
PRO CD  HD3  sing N N 343 
PRO OXT HXT  sing N N 344 
SER N   CA   sing N N 345 
SER N   H    sing N N 346 
SER N   H2   sing N N 347 
SER CA  C    sing N N 348 
SER CA  CB   sing N N 349 
SER CA  HA   sing N N 350 
SER C   O    doub N N 351 
SER C   OXT  sing N N 352 
SER CB  OG   sing N N 353 
SER CB  HB2  sing N N 354 
SER CB  HB3  sing N N 355 
SER OG  HG   sing N N 356 
SER OXT HXT  sing N N 357 
THR N   CA   sing N N 358 
THR N   H    sing N N 359 
THR N   H2   sing N N 360 
THR CA  C    sing N N 361 
THR CA  CB   sing N N 362 
THR CA  HA   sing N N 363 
THR C   O    doub N N 364 
THR C   OXT  sing N N 365 
THR CB  OG1  sing N N 366 
THR CB  CG2  sing N N 367 
THR CB  HB   sing N N 368 
THR OG1 HG1  sing N N 369 
THR CG2 HG21 sing N N 370 
THR CG2 HG22 sing N N 371 
THR CG2 HG23 sing N N 372 
THR OXT HXT  sing N N 373 
TRP N   CA   sing N N 374 
TRP N   H    sing N N 375 
TRP N   H2   sing N N 376 
TRP CA  C    sing N N 377 
TRP CA  CB   sing N N 378 
TRP CA  HA   sing N N 379 
TRP C   O    doub N N 380 
TRP C   OXT  sing N N 381 
TRP CB  CG   sing N N 382 
TRP CB  HB2  sing N N 383 
TRP CB  HB3  sing N N 384 
TRP CG  CD1  doub Y N 385 
TRP CG  CD2  sing Y N 386 
TRP CD1 NE1  sing Y N 387 
TRP CD1 HD1  sing N N 388 
TRP CD2 CE2  doub Y N 389 
TRP CD2 CE3  sing Y N 390 
TRP NE1 CE2  sing Y N 391 
TRP NE1 HE1  sing N N 392 
TRP CE2 CZ2  sing Y N 393 
TRP CE3 CZ3  doub Y N 394 
TRP CE3 HE3  sing N N 395 
TRP CZ2 CH2  doub Y N 396 
TRP CZ2 HZ2  sing N N 397 
TRP CZ3 CH2  sing Y N 398 
TRP CZ3 HZ3  sing N N 399 
TRP CH2 HH2  sing N N 400 
TRP OXT HXT  sing N N 401 
TYR N   CA   sing N N 402 
TYR N   H    sing N N 403 
TYR N   H2   sing N N 404 
TYR CA  C    sing N N 405 
TYR CA  CB   sing N N 406 
TYR CA  HA   sing N N 407 
TYR C   O    doub N N 408 
TYR C   OXT  sing N N 409 
TYR CB  CG   sing N N 410 
TYR CB  HB2  sing N N 411 
TYR CB  HB3  sing N N 412 
TYR CG  CD1  doub Y N 413 
TYR CG  CD2  sing Y N 414 
TYR CD1 CE1  sing Y N 415 
TYR CD1 HD1  sing N N 416 
TYR CD2 CE2  doub Y N 417 
TYR CD2 HD2  sing N N 418 
TYR CE1 CZ   doub Y N 419 
TYR CE1 HE1  sing N N 420 
TYR CE2 CZ   sing Y N 421 
TYR CE2 HE2  sing N N 422 
TYR CZ  OH   sing N N 423 
TYR OH  HH   sing N N 424 
TYR OXT HXT  sing N N 425 
VAL N   CA   sing N N 426 
VAL N   H    sing N N 427 
VAL N   H2   sing N N 428 
VAL CA  C    sing N N 429 
VAL CA  CB   sing N N 430 
VAL CA  HA   sing N N 431 
VAL C   O    doub N N 432 
VAL C   OXT  sing N N 433 
VAL CB  CG1  sing N N 434 
VAL CB  CG2  sing N N 435 
VAL CB  HB   sing N N 436 
VAL CG1 HG11 sing N N 437 
VAL CG1 HG12 sing N N 438 
VAL CG1 HG13 sing N N 439 
VAL CG2 HG21 sing N N 440 
VAL CG2 HG22 sing N N 441 
VAL CG2 HG23 sing N N 442 
VAL OXT HXT  sing N N 443 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '4-{2-[(6-chloro-5-nitropyrimidin-4-yl)amino]ethyl}benzenesulfonamide' J74 
3 'ZINC ION'                                                             ZN  
4 'DIMETHYL SULFOXIDE'                                                   DMS 
5 BICINE                                                                 BCN 
6 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' 
# 
