data_4KNJ
# 
_entry.id   4KNJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.381 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4KNJ         pdb_00004knj 10.2210/pdb4knj/pdb 
RCSB  RCSB079560   ?            ?                   
WWPDB D_1000079560 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4KNI . unspecified 
PDB 4KNM . unspecified 
PDB 4KNN . unspecified 
PDB 4KP5 . unspecified 
PDB 4KP8 . unspecified 
# 
_pdbx_database_status.entry_id                        4KNJ 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2013-05-10 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Benzenesulfonamides with pyrimidine moiety as inhibitors of human carbonic anhydrases I, II, VI, VII, XII, and XIII' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            21 
_citation.page_first                6937 
_citation.page_last                 6947 
_citation.year                      2013 
_citation.journal_id_ASTM           BMECEP 
_citation.country                   UK 
_citation.journal_id_ISSN           0968-0896 
_citation.journal_id_CSD            1200 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   24103428 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2013.09.029 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1  ? 
primary 'Zubriene, A.'      2  ? 
primary 'Smirnov, A.'       3  ? 
primary 'Torresan, J.'      4  ? 
primary 'Kisonaite, M.'     5  ? 
primary 'Kazokaite, J.'     6  ? 
primary 'Gylyte, J.'        7  ? 
primary 'Michailoviene, V.' 8  ? 
primary 'Jogaite, V.'       9  ? 
primary 'Manakova, E.'      10 ? 
primary 'Grazulis, S.'      11 ? 
primary 'Tumkevicius, S.'   12 ? 
primary 'Matulis, D.'       13 ? 
# 
_cell.entry_id           4KNJ 
_cell.length_a           41.988 
_cell.length_b           40.914 
_cell.length_c           71.339 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.140 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              2 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4KNJ 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                          29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                      65.409    1   ?       ? ? ? 
3 non-polymer syn '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' 343.809   1   ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                            78.133    1   ?       ? ? ? 
5 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                          195.237   1   ?       ? ? ? 
6 water       nat water                                                           18.015    156 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              4KNJ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                         ? 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE                                                        ? 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                      ? 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                 ? 'C4 H7 N O4'          133.103 
CYS 'L-peptide linking' y CYSTEINE                                                        ? 'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                            ? 'C2 H6 O S'           78.133  
E1F non-polymer         . '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' ? 'C12 H10 Cl N3 O3 S2' 343.809 
GLN 'L-peptide linking' y GLUTAMINE                                                       ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                 ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                         ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                       ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                           ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                      ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                         ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                          ? 'C6 H15 N2 O2 1'      147.195 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                          ? 'C6 H13 N O4 S'       195.237 
MET 'L-peptide linking' y METHIONINE                                                      ? 'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                   ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                         ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                          ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                                       ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                      ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                        ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                                          ? 'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                                      ? 'Zn 2'                65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4KNJ 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   39.7 
_exptl_crystal.density_Matthews      2.1 
_exptl_crystal.pdbx_mosaicity        0.9 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    '2.2M sodium malonate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR555 FLAT PANEL' 
_diffrn_detector.pdbx_collection_date   2011-11-21 
_diffrn_detector.details                'Detector swing-out angle up to 30 degrees' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.815 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X11' 
_diffrn_source.pdbx_wavelength_list        0.815 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X11 
# 
_reflns.entry_id                     4KNJ 
_reflns.d_resolution_high            2.000 
_reflns.d_resolution_low             30.260 
_reflns.number_all                   ? 
_reflns.number_obs                   15098 
_reflns.pdbx_netI_over_sigmaI        6.700 
_reflns.pdbx_Rsym_value              0.110 
_reflns.pdbx_redundancy              3.900 
_reflns.percent_possible_obs         94.300 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        21.207 
_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.pdbx_CC_half                 ? 
_reflns.pdbx_Rpim_I_all              ? 
_reflns.pdbx_Rrim_I_all              ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
2.00 2.11  ? 8009 ? ? 0.317 1.4 0.317 ? 3.80 ? 3.70 ? 2135 ? ? 0.388 ? 92.50 0.39 0.19 1  1 ? 
2.11 2.24  ? 7689 ? ? 0.243 2.1 0.243 ? 3.70 ? 4.60 ? 2065 ? ? 0.296 ? 94.30 0.30 0.14 2  1 ? 
2.24 2.39  ? 7362 ? ? 0.195 2.7 0.195 ? 3.80 ? 5.40 ? 1957 ? ? 0.236 ? 94.90 0.24 0.11 3  1 ? 
2.39 2.58  ? 6916 ? ? 0.170 3.3 0.170 ? 3.80 ? 5.90 ? 1816 ? ? 0.204 ? 94.30 0.20 0.10 4  1 ? 
2.58 2.83  ? 6930 ? ? 0.135 4.5 0.135 ? 4.10 ? 7.10 ? 1709 ? ? 0.164 ? 95.20 0.16 0.08 5  1 ? 
2.83 3.16  ? 6470 ? ? 0.110 5.5 0.110 ? 4.20 ? 8.30 ? 1533 ? ? 0.137 ? 95.30 0.14 0.06 6  1 ? 
3.16 3.65  ? 5716 ? ? 0.094 6.1 0.094 ? 4.20 ? 9.30 ? 1358 ? ? 0.117 ? 95.30 0.12 0.05 7  1 ? 
3.65 4.47  ? 4830 ? ? 0.081 6.7 0.081 ? 4.20 ? 9.90 ? 1154 ? ? 0.100 ? 95.00 0.10 0.05 8  1 ? 
4.47 6.32  ? 3670 ? ? 0.068 8.6 0.068 ? 4.10 ? 9.70 ? 886  ? ? 0.084 ? 94.80 0.08 0.04 9  1 ? 
6.32 30.26 ? 1835 ? ? 0.084 5.0 0.084 ? 3.80 ? 9.20 ? 485  ? ? 0.108 ? 89.70 0.11 0.05 10 1 ? 
# 
_refine.entry_id                                 4KNJ 
_refine.ls_d_res_high                            2.000 
_refine.ls_d_res_low                             30.260 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    93.630 
_refine.ls_number_reflns_obs                     15077 
_refine.ls_number_reflns_all                     15077 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          0.171 
_refine.ls_R_factor_obs                          0.171 
_refine.ls_R_factor_R_work                       0.164 
_refine.ls_wR_factor_R_work                      0.184 
_refine.ls_R_factor_R_free                       0.228 
_refine.ls_wR_factor_R_free                      0.252 
_refine.ls_percent_reflns_R_free                 9.700 
_refine.ls_number_reflns_R_free                  1465 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.888 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.180 
_refine.aniso_B[2][2]                            -1.240 
_refine.aniso_B[3][3]                            1.380 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.070 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.917 
_refine.overall_SU_R_Cruickshank_DPI             0.247 
_refine.overall_SU_R_free                        0.197 
_refine.pdbx_overall_ESU_R                       0.247 
_refine.pdbx_overall_ESU_R_Free                  0.197 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.844 
_refine.B_iso_max                                46.83 
_refine.B_iso_min                                5.38 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      3HLJ 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_refine_hist.number_atoms_solvent             156 
_refine_hist.number_atoms_total               2238 
_refine_hist.d_res_high                       2.000 
_refine_hist.d_res_low                        30.260 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d         2181 0.023  0.022  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      2960 1.940  1.962  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   262  7.767  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   100  35.104 24.700 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   362  16.409 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   7    18.919 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr           306  0.138  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     1681 0.010  0.020  ? ? 'X-RAY DIFFRACTION' 
r_nbd_refined            1072 0.225  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          1417 0.313  0.200  ? ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    175  0.160  0.200  ? ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      2    0.067  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   56   0.253  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 23   0.251  0.200  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_it              1303 1.119  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcangle_it             2105 1.833  2.000  ? ? 'X-RAY DIFFRACTION' 
r_scbond_it              878  2.872  3.000  ? ? 'X-RAY DIFFRACTION' 
r_scangle_it             855  4.243  4.500  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.052 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               92.210 
_refine_ls_shell.number_reflns_R_work             949 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.204 
_refine_ls_shell.R_factor_R_free                  0.326 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             105 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1054 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  4KNJ 
_struct.title                     
'Crystal structure of human carbonic anhydrase isozyme II with 2-Chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4KNJ 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, LYASE-LYASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
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 ? ASP A 161 ? LEU A 157 ASP A 162 1 ? 6 
HELX_P HELX_P7 7 VAL A 162 ? LYS A 167 ? VAL A 163 LYS A 168 5 ? 6 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 1.973 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C E1F . N19 ? ? A ZN  301 A E1F 302 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -0.07 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 4.44  
# 
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 HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O ASN A 67  ? O ASN A 67  N LEU A 60  ? N LEU A 60  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N LYS A 148 ? N LYS A 149 O VAL A 217 ? O VAL A 218 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A E1F 302 ? 14 'BINDING SITE FOR RESIDUE E1F A 302' 
AC3 Software A DMS 303 ? 4  'BINDING SITE FOR RESIDUE DMS A 303' 
AC4 Software A MES 304 ? 5  'BINDING SITE FOR RESIDUE MES A 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  E1F C .   ? E1F A 302 . ? 1_555 ? 
5  AC2 14 HIS A 94  ? HIS A 94  . ? 1_555 ? 
6  AC2 14 HIS A 96  ? HIS A 96  . ? 1_555 ? 
7  AC2 14 HIS A 119 ? HIS A 119 . ? 1_555 ? 
8  AC2 14 VAL A 121 ? VAL A 121 . ? 1_555 ? 
9  AC2 14 PHE A 130 ? PHE A 131 . ? 1_555 ? 
10 AC2 14 LEU A 140 ? LEU A 141 . ? 1_555 ? 
11 AC2 14 VAL A 142 ? VAL A 143 . ? 1_555 ? 
12 AC2 14 LEU A 197 ? LEU A 198 . ? 1_555 ? 
13 AC2 14 THR A 198 ? THR A 199 . ? 1_555 ? 
14 AC2 14 THR A 199 ? THR A 200 . ? 1_555 ? 
15 AC2 14 PRO A 201 ? PRO A 202 . ? 1_555 ? 
16 AC2 14 TRP A 208 ? TRP A 209 . ? 1_555 ? 
17 AC2 14 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
18 AC2 14 HOH F .   ? HOH A 503 . ? 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  PRO A 246 ? PRO A 247 . ? 1_555 ? 
23 AC4 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
24 AC4 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
25 AC4 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
26 AC4 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
27 AC4 5  HOH F .   ? HOH A 474 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4KNJ 
_atom_sites.fract_transf_matrix[1][1]   0.023816 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024441 
_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]   0.014456 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
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   A HIS A 1 4   ? 9.248   1.501   8.098   0.50 29.24 ? 4   HIS A N   1 
ATOM   2    N  N   B HIS A 1 4   ? 9.058   1.341   8.020   0.50 29.24 ? 4   HIS A N   1 
ATOM   3    C  CA  A HIS A 1 4   ? 9.879   0.123   8.350   0.50 29.20 ? 4   HIS A CA  1 
ATOM   4    C  CA  B HIS A 1 4   ? 9.799   0.134   8.368   0.50 29.20 ? 4   HIS A CA  1 
ATOM   5    C  C   A HIS A 1 4   ? 9.241   -0.870  9.295   0.50 26.61 ? 4   HIS A C   1 
ATOM   6    C  C   B HIS A 1 4   ? 9.198   -0.874  9.293   0.50 26.61 ? 4   HIS A C   1 
ATOM   7    O  O   A HIS A 1 4   ? 9.471   -2.053  9.111   0.50 26.99 ? 4   HIS A O   1 
ATOM   8    O  O   B HIS A 1 4   ? 9.435   -2.024  9.114   0.50 26.99 ? 4   HIS A O   1 
ATOM   9    C  CB  A HIS A 1 4   ? 11.348  0.191   8.744   0.50 30.70 ? 4   HIS A CB  1 
ATOM   10   C  CB  B HIS A 1 4   ? 11.084  0.458   9.008   0.50 30.70 ? 4   HIS A CB  1 
ATOM   11   C  CG  A HIS A 1 4   ? 12.279  -0.262  7.666   0.50 37.72 ? 4   HIS A CG  1 
ATOM   12   C  CG  B HIS A 1 4   ? 12.159  -0.466  8.624   0.50 37.72 ? 4   HIS A CG  1 
ATOM   13   N  ND1 A HIS A 1 4   ? 13.084  -1.377  7.800   0.50 41.06 ? 4   HIS A ND1 1 
ATOM   14   N  ND1 B HIS A 1 4   ? 12.537  -0.630  7.317   0.50 41.06 ? 4   HIS A ND1 1 
ATOM   15   C  CD2 A HIS A 1 4   ? 12.558  0.264   6.441   0.50 42.95 ? 4   HIS A CD2 1 
ATOM   16   C  CD2 B HIS A 1 4   ? 12.931  -1.287  9.357   0.50 42.95 ? 4   HIS A CD2 1 
ATOM   17   C  CE1 A HIS A 1 4   ? 13.808  -1.524  6.700   0.50 43.64 ? 4   HIS A CE1 1 
ATOM   18   C  CE1 B HIS A 1 4   ? 13.522  -1.497  7.258   0.50 43.64 ? 4   HIS A CE1 1 
ATOM   19   N  NE2 A HIS A 1 4   ? 13.515  -0.539  5.864   0.50 44.42 ? 4   HIS A NE2 1 
ATOM   20   N  NE2 B HIS A 1 4   ? 13.783  -1.908  8.483   0.50 44.42 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.492   -0.448  10.311  1.00 23.53 ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 7.837   -1.449  11.164  1.00 20.77 ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 6.855   -2.269  10.369  1.00 19.11 ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.292   -1.811  9.366   1.00 16.81 ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.135   -0.819  12.361  1.00 18.76 ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 5.867   -0.018  11.986  1.00 19.64 ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 5.797   1.304   11.643  1.00 18.10 ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.520   -0.510  11.952  1.00 16.25 ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.483   1.663   11.406  1.00 17.05 ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.682   0.575   11.601  1.00 17.02 ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 3.947   -1.757  12.177  1.00 15.89 ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.289   0.454   11.476  1.00 14.70 ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.531   -1.879  12.053  1.00 17.67 ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 1.740   -0.776  11.697  1.00 15.83 ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.627   -3.493  10.824  1.00 18.86 ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.623   -4.297  10.179  1.00 19.28 ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.188   -5.411  11.101  1.00 19.80 ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.175   -5.247  12.318  1.00 18.01 ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 4.787   -6.530  10.494  1.00 20.36 ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 4.393   -7.715  11.266  1.00 20.70 ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 5.251   -8.973  11.007  1.00 23.71 ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 4.813   -10.073 11.351  1.00 25.14 ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 2.897   -8.002  11.064  1.00 18.50 ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 1.979   -6.915  11.654  1.00 16.76 ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 1.616   -6.925  13.028  1.00 12.95 ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 1.485   -5.904  10.840  1.00 13.68 ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 0.773   -5.951  13.545  1.00 12.92 ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 0.647   -4.926  11.324  1.00 13.51 ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 0.286   -4.960  12.686  1.00 15.51 ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? -0.524  -3.975  13.176  1.00 15.42 ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 6.452   -8.838  10.434  1.00 25.78 ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 7.351   -10.018 10.225  1.00 26.66 ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 8.382   -10.356 11.297  1.00 28.82 ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 8.433   -9.727  12.381  1.00 29.52 ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 9.268   -11.342 11.008  1.00 30.43 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 10.305  -11.749 12.006  1.00 30.05 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 11.298  -10.646 12.374  1.00 29.45 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 11.807  -10.585 13.530  1.00 29.27 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 11.066  -12.985 11.540  1.00 32.20 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 11.959  -13.560 12.622  1.00 33.44 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 13.039  -14.469 12.089  1.00 37.84 ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 14.275  -14.415 13.027  1.00 40.35 ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 13.993  -14.643 14.535  1.00 41.14 ? 9   LYS A NZ  1 
ATOM   64   N  N   . HIS A 1 10  ? 11.515  -9.733  11.418  1.00 27.70 ? 10  HIS A N   1 
ATOM   65   C  CA  . HIS A 1 10  ? 12.566  -8.737  11.540  1.00 26.32 ? 10  HIS A CA  1 
ATOM   66   C  C   . HIS A 1 10  ? 12.074  -7.334  11.894  1.00 24.44 ? 10  HIS A C   1 
ATOM   67   O  O   . HIS A 1 10  ? 12.844  -6.496  12.319  1.00 26.36 ? 10  HIS A O   1 
ATOM   68   C  CB  . HIS A 1 10  ? 13.440  -8.792  10.266  1.00 25.28 ? 10  HIS A CB  1 
ATOM   69   C  CG  . HIS A 1 10  ? 14.107  -10.136 10.097  1.00 27.38 ? 10  HIS A CG  1 
ATOM   70   N  ND1 . HIS A 1 10  ? 15.149  -10.557 10.902  1.00 29.24 ? 10  HIS A ND1 1 
ATOM   71   C  CD2 . HIS A 1 10  ? 13.811  -11.182 9.292   1.00 30.73 ? 10  HIS A CD2 1 
ATOM   72   C  CE1 . HIS A 1 10  ? 15.483  -11.790 10.581  1.00 29.62 ? 10  HIS A CE1 1 
ATOM   73   N  NE2 . HIS A 1 10  ? 14.686  -12.197 9.606   1.00 30.40 ? 10  HIS A NE2 1 
ATOM   74   N  N   . ASN A 1 11  ? 10.778  -7.107  11.767  1.00 23.36 ? 11  ASN A N   1 
ATOM   75   C  CA  . ASN A 1 11  ? 10.183  -5.792  12.004  1.00 21.52 ? 11  ASN A CA  1 
ATOM   76   C  C   . ASN A 1 11  ? 8.823   -5.838  12.708  1.00 21.09 ? 11  ASN A C   1 
ATOM   77   O  O   . ASN A 1 11  ? 8.184   -4.802  12.760  1.00 18.84 ? 11  ASN A O   1 
ATOM   78   C  CB  . ASN A 1 11  ? 9.996   -5.040  10.685  1.00 20.29 ? 11  ASN A CB  1 
ATOM   79   C  CG  . ASN A 1 11  ? 9.004   -5.711  9.764   1.00 22.97 ? 11  ASN A CG  1 
ATOM   80   O  OD1 . ASN A 1 11  ? 8.571   -6.854  10.009  1.00 22.72 ? 11  ASN A OD1 1 
ATOM   81   N  ND2 . ASN A 1 11  ? 8.651   -5.026  8.673   1.00 19.48 ? 11  ASN A ND2 1 
ATOM   82   N  N   . GLY A 1 12  ? 8.424   -7.020  13.238  1.00 20.72 ? 12  GLY A N   1 
ATOM   83   C  CA  . GLY A 1 12  ? 7.150   -7.239  13.947  1.00 19.01 ? 12  GLY A CA  1 
ATOM   84   C  C   . GLY A 1 12  ? 7.103   -6.668  15.377  1.00 19.99 ? 12  GLY A C   1 
ATOM   85   O  O   . GLY A 1 12  ? 8.026   -5.964  15.800  1.00 19.00 ? 12  GLY A O   1 
ATOM   86   N  N   . PRO A 1 13  ? 6.006   -6.924  16.116  1.00 18.77 ? 13  PRO A N   1 
ATOM   87   C  CA  . PRO A 1 13  ? 5.780   -6.255  17.398  1.00 20.06 ? 13  PRO A CA  1 
ATOM   88   C  C   . PRO A 1 13  ? 6.935   -6.271  18.429  1.00 19.48 ? 13  PRO A C   1 
ATOM   89   O  O   . PRO A 1 13  ? 7.102   -5.287  19.157  1.00 18.95 ? 13  PRO A O   1 
ATOM   90   C  CB  . PRO A 1 13  ? 4.553   -7.006  17.971  1.00 19.41 ? 13  PRO A CB  1 
ATOM   91   C  CG  . PRO A 1 13  ? 3.799   -7.438  16.743  1.00 19.07 ? 13  PRO A CG  1 
ATOM   92   C  CD  . PRO A 1 13  ? 4.875   -7.815  15.753  1.00 20.67 ? 13  PRO A CD  1 
ATOM   93   N  N   . GLU A 1 14  ? 7.698   -7.370  18.512  1.00 18.51 ? 14  GLU A N   1 
ATOM   94   C  CA  . GLU A 1 14  ? 8.841   -7.450  19.417  1.00 18.28 ? 14  GLU A CA  1 
ATOM   95   C  C   . GLU A 1 14  ? 9.968   -6.440  19.099  1.00 17.00 ? 14  GLU A C   1 
ATOM   96   O  O   . GLU A 1 14  ? 10.816  -6.216  19.900  1.00 17.96 ? 14  GLU A O   1 
ATOM   97   C  CB  . GLU A 1 14  ? 9.398   -8.851  19.335  1.00 21.08 ? 14  GLU A CB  1 
ATOM   98   C  CG  . GLU A 1 14  ? 9.979   -9.197  17.930  1.00 23.68 ? 14  GLU A CG  1 
ATOM   99   C  CD  . GLU A 1 14  ? 9.068   -10.053 16.996  1.00 35.39 ? 14  GLU A CD  1 
ATOM   100  O  OE1 . GLU A 1 14  ? 7.876   -9.667  16.666  1.00 30.56 ? 14  GLU A OE1 1 
ATOM   101  O  OE2 . GLU A 1 14  ? 9.603   -11.118 16.560  1.00 37.47 ? 14  GLU A OE2 1 
ATOM   102  N  N   . HIS A 1 15  ? 9.992   -5.909  17.891  1.00 16.69 ? 15  HIS A N   1 
ATOM   103  C  CA  . HIS A 1 15  ? 10.994  -4.969  17.464  1.00 17.91 ? 15  HIS A CA  1 
ATOM   104  C  C   . HIS A 1 15  ? 10.519  -3.529  17.560  1.00 18.08 ? 15  HIS A C   1 
ATOM   105  O  O   . HIS A 1 15  ? 11.318  -2.634  17.350  1.00 19.16 ? 15  HIS A O   1 
ATOM   106  C  CB  . HIS A 1 15  ? 11.364  -5.247  15.979  1.00 17.86 ? 15  HIS A CB  1 
ATOM   107  C  CG  . HIS A 1 15  ? 12.133  -6.503  15.774  1.00 18.84 ? 15  HIS A CG  1 
ATOM   108  N  ND1 . HIS A 1 15  ? 13.498  -6.568  15.946  1.00 17.87 ? 15  HIS A ND1 1 
ATOM   109  C  CD2 . HIS A 1 15  ? 11.739  -7.752  15.414  1.00 20.26 ? 15  HIS A CD2 1 
ATOM   110  C  CE1 . HIS A 1 15  ? 13.913  -7.796  15.679  1.00 19.87 ? 15  HIS A CE1 1 
ATOM   111  N  NE2 . HIS A 1 15  ? 12.866  -8.547  15.403  1.00 16.49 ? 15  HIS A NE2 1 
ATOM   112  N  N   . TRP A 1 16  ? 9.211   -3.286  17.735  1.00 17.53 ? 16  TRP A N   1 
ATOM   113  C  CA  . TRP A 1 16  ? 8.701   -1.899  17.646  1.00 16.71 ? 16  TRP A CA  1 
ATOM   114  C  C   . TRP A 1 16  ? 9.295   -0.926  18.683  1.00 15.94 ? 16  TRP A C   1 
ATOM   115  O  O   . TRP A 1 16  ? 9.350   0.252   18.426  1.00 16.66 ? 16  TRP A O   1 
ATOM   116  C  CB  . TRP A 1 16  ? 7.180   -1.841  17.786  1.00 13.41 ? 16  TRP A CB  1 
ATOM   117  C  CG  . TRP A 1 16  ? 6.468   -2.556  16.659  1.00 15.71 ? 16  TRP A CG  1 
ATOM   118  C  CD1 . TRP A 1 16  ? 6.983   -2.973  15.424  1.00 11.97 ? 16  TRP A CD1 1 
ATOM   119  C  CD2 . TRP A 1 16  ? 5.082   -2.852  16.624  1.00 13.13 ? 16  TRP A CD2 1 
ATOM   120  N  NE1 . TRP A 1 16  ? 6.011   -3.595  14.707  1.00 15.23 ? 16  TRP A NE1 1 
ATOM   121  C  CE2 . TRP A 1 16  ? 4.823   -3.505  15.388  1.00 11.85 ? 16  TRP A CE2 1 
ATOM   122  C  CE3 . TRP A 1 16  ? 4.039   -2.659  17.532  1.00 9.59  ? 16  TRP A CE3 1 
ATOM   123  C  CZ2 . TRP A 1 16  ? 3.567   -3.964  15.041  1.00 13.15 ? 16  TRP A CZ2 1 
ATOM   124  C  CZ3 . TRP A 1 16  ? 2.802   -3.128  17.190  1.00 10.67 ? 16  TRP A CZ3 1 
ATOM   125  C  CH2 . TRP A 1 16  ? 2.571   -3.773  15.962  1.00 12.01 ? 16  TRP A CH2 1 
ATOM   126  N  N   . HIS A 1 17  ? 9.724   -1.422  19.835  1.00 17.63 ? 17  HIS A N   1 
ATOM   127  C  CA  . HIS A 1 17  ? 10.170  -0.551  20.900  1.00 17.67 ? 17  HIS A CA  1 
ATOM   128  C  C   . HIS A 1 17  ? 11.447  0.256   20.514  1.00 18.53 ? 17  HIS A C   1 
ATOM   129  O  O   . HIS A 1 17  ? 11.691  1.286   21.100  1.00 17.30 ? 17  HIS A O   1 
ATOM   130  C  CB  . HIS A 1 17  ? 10.416  -1.337  22.186  1.00 18.42 ? 17  HIS A CB  1 
ATOM   131  C  CG  . HIS A 1 17  ? 11.639  -2.219  22.095  1.00 21.57 ? 17  HIS A CG  1 
ATOM   132  N  ND1 . HIS A 1 17  ? 12.894  -1.809  22.519  1.00 24.75 ? 17  HIS A ND1 1 
ATOM   133  C  CD2 . HIS A 1 17  ? 11.816  -3.430  21.527  1.00 17.03 ? 17  HIS A CD2 1 
ATOM   134  C  CE1 . HIS A 1 17  ? 13.774  -2.764  22.277  1.00 17.65 ? 17  HIS A CE1 1 
ATOM   135  N  NE2 . HIS A 1 17  ? 13.146  -3.757  21.671  1.00 17.35 ? 17  HIS A NE2 1 
ATOM   136  N  N   . LYS A 1 18  ? 12.213  -0.215  19.527  1.00 18.04 ? 18  LYS A N   1 
ATOM   137  C  CA  . LYS A 1 18  ? 13.424  0.468   19.105  1.00 19.01 ? 18  LYS A CA  1 
ATOM   138  C  C   . LYS A 1 18  ? 13.077  1.802   18.418  1.00 20.45 ? 18  LYS A C   1 
ATOM   139  O  O   . LYS A 1 18  ? 13.584  2.841   18.795  1.00 20.60 ? 18  LYS A O   1 
ATOM   140  C  CB  . LYS A 1 18  ? 14.244  -0.448  18.198  1.00 18.59 ? 18  LYS A CB  1 
ATOM   141  C  CG  . LYS A 1 18  ? 14.814  -1.722  18.949  1.00 20.44 ? 18  LYS A CG  1 
ATOM   142  C  CD  . LYS A 1 18  ? 15.468  -2.659  17.991  1.00 20.56 ? 18  LYS A CD  1 
ATOM   143  C  CE  . LYS A 1 18  ? 14.501  -3.687  17.522  1.00 19.49 ? 18  LYS A CE  1 
ATOM   144  N  NZ  . LYS A 1 18  ? 15.182  -4.399  16.333  1.00 13.74 ? 18  LYS A NZ  1 
ATOM   145  N  N   . ASP A 1 19  ? 12.121  1.811   17.496  1.00 20.38 ? 19  ASP A N   1 
ATOM   146  C  CA  . ASP A 1 19  ? 11.608  3.107   16.979  1.00 21.50 ? 19  ASP A CA  1 
ATOM   147  C  C   . ASP A 1 19  ? 10.599  3.857   17.829  1.00 21.21 ? 19  ASP A C   1 
ATOM   148  O  O   . ASP A 1 19  ? 10.427  5.045   17.663  1.00 20.53 ? 19  ASP A O   1 
ATOM   149  C  CB  . ASP A 1 19  ? 10.984  2.914   15.611  1.00 21.76 ? 19  ASP A CB  1 
ATOM   150  C  CG  . ASP A 1 19  ? 11.992  2.965   14.492  1.00 25.36 ? 19  ASP A CG  1 
ATOM   151  O  OD1 . ASP A 1 19  ? 13.038  3.592   14.630  1.00 29.66 ? 19  ASP A OD1 1 
ATOM   152  O  OD2 . ASP A 1 19  ? 11.709  2.361   13.452  1.00 33.10 ? 19  ASP A OD2 1 
ATOM   153  N  N   . PHE A 1 20  ? 9.904   3.152   18.711  1.00 21.32 ? 20  PHE A N   1 
ATOM   154  C  CA  . PHE A 1 20  ? 8.791   3.709   19.477  1.00 20.80 ? 20  PHE A CA  1 
ATOM   155  C  C   . PHE A 1 20  ? 8.909   3.168   20.869  1.00 20.59 ? 20  PHE A C   1 
ATOM   156  O  O   . PHE A 1 20  ? 8.313   2.142   21.199  1.00 19.80 ? 20  PHE A O   1 
ATOM   157  C  CB  . PHE A 1 20  ? 7.444   3.356   18.829  1.00 19.95 ? 20  PHE A CB  1 
ATOM   158  C  CG  . PHE A 1 20  ? 7.403   3.674   17.359  1.00 19.00 ? 20  PHE A CG  1 
ATOM   159  C  CD1 . PHE A 1 20  ? 7.079   4.966   16.923  1.00 18.90 ? 20  PHE A CD1 1 
ATOM   160  C  CD2 . PHE A 1 20  ? 7.783   2.705   16.421  1.00 17.35 ? 20  PHE A CD2 1 
ATOM   161  C  CE1 . PHE A 1 20  ? 7.083   5.278   15.560  1.00 16.60 ? 20  PHE A CE1 1 
ATOM   162  C  CE2 . PHE A 1 20  ? 7.796   2.987   15.048  1.00 18.68 ? 20  PHE A CE2 1 
ATOM   163  C  CZ  . PHE A 1 20  ? 7.466   4.303   14.625  1.00 21.67 ? 20  PHE A CZ  1 
ATOM   164  N  N   . PRO A 1 21  ? 9.782   3.790   21.666  1.00 20.81 ? 21  PRO A N   1 
ATOM   165  C  CA  . PRO A 1 21  ? 10.018  3.310   23.016  1.00 19.12 ? 21  PRO A CA  1 
ATOM   166  C  C   . PRO A 1 21  ? 8.796   3.190   23.940  1.00 18.92 ? 21  PRO A C   1 
ATOM   167  O  O   . PRO A 1 21  ? 8.832   2.410   24.933  1.00 18.78 ? 21  PRO A O   1 
ATOM   168  C  CB  . PRO A 1 21  ? 11.057  4.322   23.572  1.00 20.74 ? 21  PRO A CB  1 
ATOM   169  C  CG  . PRO A 1 21  ? 11.741  4.833   22.424  1.00 21.10 ? 21  PRO A CG  1 
ATOM   170  C  CD  . PRO A 1 21  ? 10.714  4.886   21.298  1.00 21.61 ? 21  PRO A CD  1 
ATOM   171  N  N   . ILE A 1 22  ? 7.766   3.999   23.683  1.00 16.94 ? 22  ILE A N   1 
ATOM   172  C  CA  . ILE A 1 22  ? 6.481   3.853   24.361  1.00 17.44 ? 22  ILE A CA  1 
ATOM   173  C  C   . ILE A 1 22  ? 5.880   2.412   24.237  1.00 16.07 ? 22  ILE A C   1 
ATOM   174  O  O   . ILE A 1 22  ? 5.020   2.053   25.025  1.00 15.33 ? 22  ILE A O   1 
ATOM   175  C  CB  . ILE A 1 22  ? 5.425   4.926   23.874  1.00 16.66 ? 22  ILE A CB  1 
ATOM   176  C  CG1 . ILE A 1 22  ? 4.254   5.041   24.847  1.00 20.39 ? 22  ILE A CG1 1 
ATOM   177  C  CG2 . ILE A 1 22  ? 4.820   4.484   22.486  1.00 16.92 ? 22  ILE A CG2 1 
ATOM   178  C  CD1 . ILE A 1 22  ? 4.552   5.804   26.140  1.00 24.67 ? 22  ILE A CD1 1 
ATOM   179  N  N   . ALA A 1 23  ? 6.393   1.578   23.313  1.00 17.05 ? 23  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 23  ? 5.985   0.135   23.176  1.00 17.75 ? 23  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 23  ? 6.011   -0.599  24.504  1.00 18.28 ? 23  ALA A C   1 
ATOM   182  O  O   . ALA A 1 23  ? 5.247   -1.602  24.737  1.00 17.39 ? 23  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 23  ? 6.917   -0.642  22.135  1.00 16.63 ? 23  ALA A CB  1 
ATOM   184  N  N   . LYS A 1 24  ? 6.889   -0.102  25.391  1.00 19.12 ? 24  LYS A N   1 
ATOM   185  C  CA  . LYS A 1 24  ? 7.105   -0.708  26.689  1.00 19.72 ? 24  LYS A CA  1 
ATOM   186  C  C   . LYS A 1 24  ? 6.506   0.133   27.782  1.00 19.80 ? 24  LYS A C   1 
ATOM   187  O  O   . LYS A 1 24  ? 6.923   0.031   28.936  1.00 19.94 ? 24  LYS A O   1 
ATOM   188  C  CB  . LYS A 1 24  ? 8.615   -0.868  26.946  1.00 21.46 ? 24  LYS A CB  1 
ATOM   189  C  CG  . LYS A 1 24  ? 9.296   -1.922  26.054  1.00 21.86 ? 24  LYS A CG  1 
ATOM   190  C  CD  . LYS A 1 24  ? 10.763  -2.002  26.325  1.00 25.78 ? 24  LYS A CD  1 
ATOM   191  C  CE  . LYS A 1 24  ? 11.436  -3.102  25.447  1.00 26.98 ? 24  LYS A CE  1 
ATOM   192  N  NZ  . LYS A 1 24  ? 11.368  -4.532  26.042  1.00 30.93 ? 24  LYS A NZ  1 
ATOM   193  N  N   . GLY A 1 25  ? 5.515   0.964   27.448  1.00 18.76 ? 25  GLY A N   1 
ATOM   194  C  CA  . GLY A 1 25  ? 5.031   1.931   28.402  1.00 17.61 ? 25  GLY A CA  1 
ATOM   195  C  C   . GLY A 1 25  ? 4.005   1.410   29.361  1.00 16.50 ? 25  GLY A C   1 
ATOM   196  O  O   . GLY A 1 25  ? 3.749   0.229   29.408  1.00 16.21 ? 25  GLY A O   1 
ATOM   197  N  N   . GLU A 1 26  ? 3.400   2.318   30.125  1.00 18.12 ? 26  GLU A N   1 
ATOM   198  C  CA  . GLU A 1 26  ? 2.517   1.941   31.235  1.00 18.22 ? 26  GLU A CA  1 
ATOM   199  C  C   . GLU A 1 26  ? 1.089   1.617   30.829  1.00 16.46 ? 26  GLU A C   1 
ATOM   200  O  O   . GLU A 1 26  ? 0.329   1.092   31.645  1.00 15.25 ? 26  GLU A O   1 
ATOM   201  C  CB  . GLU A 1 26  ? 2.499   3.035   32.382  1.00 20.36 ? 26  GLU A CB  1 
ATOM   202  C  CG  . GLU A 1 26  ? 3.844   3.292   33.136  1.00 26.95 ? 26  GLU A CG  1 
ATOM   203  C  CD  . GLU A 1 26  ? 4.541   1.998   33.632  1.00 34.88 ? 26  GLU A CD  1 
ATOM   204  O  OE1 . GLU A 1 26  ? 4.030   1.348   34.599  1.00 41.16 ? 26  GLU A OE1 1 
ATOM   205  O  OE2 . GLU A 1 26  ? 5.582   1.616   33.045  1.00 33.78 ? 26  GLU A OE2 1 
ATOM   206  N  N   . ARG A 1 27  ? 0.691   1.922   29.593  1.00 14.41 ? 27  ARG A N   1 
ATOM   207  C  CA  . ARG A 1 27  ? -0.725  1.678   29.211  1.00 14.00 ? 27  ARG A CA  1 
ATOM   208  C  C   . ARG A 1 27  ? -0.883  1.277   27.686  1.00 12.33 ? 27  ARG A C   1 
ATOM   209  O  O   . ARG A 1 27  ? -1.641  1.893   26.931  1.00 11.90 ? 27  ARG A O   1 
ATOM   210  C  CB  . ARG A 1 27  ? -1.634  2.862   29.592  1.00 12.48 ? 27  ARG A CB  1 
ATOM   211  C  CG  . ARG A 1 27  ? -1.378  4.176   28.823  1.00 15.58 ? 27  ARG A CG  1 
ATOM   212  C  CD  . ARG A 1 27  ? -2.381  5.384   29.144  1.00 17.26 ? 27  ARG A CD  1 
ATOM   213  N  NE  . ARG A 1 27  ? -3.608  5.327   28.345  1.00 17.55 ? 27  ARG A NE  1 
ATOM   214  C  CZ  . ARG A 1 27  ? -4.471  6.324   28.162  1.00 16.99 ? 27  ARG A CZ  1 
ATOM   215  N  NH1 . ARG A 1 27  ? -4.329  7.521   28.727  1.00 17.22 ? 27  ARG A NH1 1 
ATOM   216  N  NH2 . ARG A 1 27  ? -5.484  6.113   27.381  1.00 16.75 ? 27  ARG A NH2 1 
ATOM   217  N  N   . GLN A 1 28  ? -0.195  0.199   27.324  1.00 10.79 ? 28  GLN A N   1 
ATOM   218  C  CA  . GLN A 1 28  ? -0.132  -0.369  26.004  1.00 9.17  ? 28  GLN A CA  1 
ATOM   219  C  C   . GLN A 1 28  ? -1.267  -1.383  25.814  1.00 9.75  ? 28  GLN A C   1 
ATOM   220  O  O   . GLN A 1 28  ? -1.784  -2.016  26.763  1.00 10.01 ? 28  GLN A O   1 
ATOM   221  C  CB  . GLN A 1 28  ? 1.215   -1.074  25.845  1.00 11.63 ? 28  GLN A CB  1 
ATOM   222  C  CG  . GLN A 1 28  ? 2.396   -0.049  25.707  1.00 8.77  ? 28  GLN A CG  1 
ATOM   223  C  CD  . GLN A 1 28  ? 2.243   0.777   24.403  1.00 12.95 ? 28  GLN A CD  1 
ATOM   224  O  OE1 . GLN A 1 28  ? 2.458   0.255   23.328  1.00 12.59 ? 28  GLN A OE1 1 
ATOM   225  N  NE2 . GLN A 1 28  ? 1.860   2.050   24.512  1.00 11.45 ? 28  GLN A NE2 1 
ATOM   226  N  N   . SER A 1 29  ? -1.625  -1.507  24.554  1.00 10.79 ? 29  SER A N   1 
ATOM   227  C  CA  . SER A 1 29  ? -2.708  -2.321  24.109  1.00 11.28 ? 29  SER A CA  1 
ATOM   228  C  C   . SER A 1 29  ? -2.173  -3.169  22.954  1.00 10.74 ? 29  SER A C   1 
ATOM   229  O  O   . SER A 1 29  ? -1.237  -2.731  22.242  1.00 11.08 ? 29  SER A O   1 
ATOM   230  C  CB  . SER A 1 29  ? -3.846  -1.433  23.598  1.00 9.80  ? 29  SER A CB  1 
ATOM   231  O  OG  . SER A 1 29  ? -4.542  -0.828  24.662  1.00 12.57 ? 29  SER A OG  1 
ATOM   232  N  N   . PRO A 1 30  ? -2.831  -4.326  22.702  1.00 11.12 ? 30  PRO A N   1 
ATOM   233  C  CA  . PRO A 1 30  ? -3.992  -4.815  23.440  1.00 12.05 ? 30  PRO A CA  1 
ATOM   234  C  C   . PRO A 1 30  ? -3.566  -5.455  24.756  1.00 11.61 ? 30  PRO A C   1 
ATOM   235  O  O   . PRO A 1 30  ? -2.376  -5.467  25.063  1.00 10.10 ? 30  PRO A O   1 
ATOM   236  C  CB  . PRO A 1 30  ? -4.535  -5.919  22.524  1.00 11.49 ? 30  PRO A CB  1 
ATOM   237  C  CG  . PRO A 1 30  ? -3.290  -6.483  21.958  1.00 12.54 ? 30  PRO A CG  1 
ATOM   238  C  CD  . PRO A 1 30  ? -2.455  -5.265  21.619  1.00 11.19 ? 30  PRO A CD  1 
ATOM   239  N  N   . VAL A 1 31  ? -4.556  -5.995  25.474  1.00 11.93 ? 31  VAL A N   1 
ATOM   240  C  CA  . VAL A 1 31  ? -4.396  -6.746  26.706  1.00 12.00 ? 31  VAL A CA  1 
ATOM   241  C  C   . VAL A 1 31  ? -5.260  -8.035  26.671  1.00 13.07 ? 31  VAL A C   1 
ATOM   242  O  O   . VAL A 1 31  ? -6.219  -8.200  25.903  1.00 12.33 ? 31  VAL A O   1 
ATOM   243  C  CB  . VAL A 1 31  ? -4.766  -5.910  27.972  1.00 13.16 ? 31  VAL A CB  1 
ATOM   244  C  CG1 . VAL A 1 31  ? -3.786  -4.720  28.141  1.00 12.02 ? 31  VAL A CG1 1 
ATOM   245  C  CG2 . VAL A 1 31  ? -6.285  -5.503  28.009  1.00 10.34 ? 31  VAL A CG2 1 
ATOM   246  N  N   . ASP A 1 32  ? -4.951  -8.941  27.569  1.00 13.48 ? 32  ASP A N   1 
ATOM   247  C  CA  . ASP A 1 32  ? -5.807  -10.051 27.741  1.00 13.65 ? 32  ASP A CA  1 
ATOM   248  C  C   . ASP A 1 32  ? -6.878  -9.618  28.676  1.00 13.80 ? 32  ASP A C   1 
ATOM   249  O  O   . ASP A 1 32  ? -6.588  -8.980  29.677  1.00 13.18 ? 32  ASP A O   1 
ATOM   250  C  CB  . ASP A 1 32  ? -5.071  -11.262 28.288  1.00 13.44 ? 32  ASP A CB  1 
ATOM   251  C  CG  . ASP A 1 32  ? -6.021  -12.379 28.634  1.00 15.81 ? 32  ASP A CG  1 
ATOM   252  O  OD1 . ASP A 1 32  ? -6.694  -12.766 27.682  1.00 11.57 ? 32  ASP A OD1 1 
ATOM   253  O  OD2 . ASP A 1 32  ? -6.094  -12.854 29.822  1.00 14.54 ? 32  ASP A OD2 1 
ATOM   254  N  N   . ILE A 1 33  ? -8.135  -9.941  28.352  1.00 14.67 ? 33  ILE A N   1 
ATOM   255  C  CA  . ILE A 1 33  ? -9.241  -9.595  29.255  1.00 15.41 ? 33  ILE A CA  1 
ATOM   256  C  C   . ILE A 1 33  ? -9.583  -10.833 30.120  1.00 16.40 ? 33  ILE A C   1 
ATOM   257  O  O   . ILE A 1 33  ? -10.179 -11.814 29.643  1.00 16.38 ? 33  ILE A O   1 
ATOM   258  C  CB  . ILE A 1 33  ? -10.502 -9.084  28.481  1.00 16.35 ? 33  ILE A CB  1 
ATOM   259  C  CG1 . ILE A 1 33  ? -10.148 -7.843  27.615  1.00 15.76 ? 33  ILE A CG1 1 
ATOM   260  C  CG2 . ILE A 1 33  ? -11.636 -8.764  29.466  1.00 13.86 ? 33  ILE A CG2 1 
ATOM   261  C  CD1 . ILE A 1 33  ? -11.201 -7.553  26.502  1.00 14.69 ? 33  ILE A CD1 1 
ATOM   262  N  N   . ASP A 1 34  ? -9.163  -10.777 31.386  1.00 17.54 ? 34  ASP A N   1 
ATOM   263  C  CA  . ASP A 1 34  ? -9.466  -11.809 32.399  1.00 19.52 ? 34  ASP A CA  1 
ATOM   264  C  C   . ASP A 1 34  ? -10.925 -11.515 32.885  1.00 18.83 ? 34  ASP A C   1 
ATOM   265  O  O   . ASP A 1 34  ? -11.161 -10.619 33.684  1.00 21.24 ? 34  ASP A O   1 
ATOM   266  C  CB  . ASP A 1 34  ? -8.372  -11.704 33.490  1.00 19.80 ? 34  ASP A CB  1 
ATOM   267  C  CG  . ASP A 1 34  ? -8.535  -12.723 34.692  1.00 25.31 ? 34  ASP A CG  1 
ATOM   268  O  OD1 . ASP A 1 34  ? -9.568  -13.398 34.858  1.00 23.43 ? 34  ASP A OD1 1 
ATOM   269  O  OD2 . ASP A 1 34  ? -7.578  -12.787 35.523  1.00 31.67 ? 34  ASP A OD2 1 
ATOM   270  N  N   . THR A 1 35  ? -11.900 -12.258 32.379  1.00 19.68 ? 35  THR A N   1 
ATOM   271  C  CA  . THR A 1 35  ? -13.315 -11.909 32.523  1.00 20.97 ? 35  THR A CA  1 
ATOM   272  C  C   . THR A 1 35  ? -13.741 -12.054 33.971  1.00 22.26 ? 35  THR A C   1 
ATOM   273  O  O   . THR A 1 35  ? -14.734 -11.431 34.410  1.00 22.65 ? 35  THR A O   1 
ATOM   274  C  CB  . THR A 1 35  ? -14.250 -12.812 31.694  1.00 21.57 ? 35  THR A CB  1 
ATOM   275  O  OG1 . THR A 1 35  ? -14.094 -14.154 32.163  1.00 22.36 ? 35  THR A OG1 1 
ATOM   276  C  CG2 . THR A 1 35  ? -13.959 -12.745 30.163  1.00 18.51 ? 35  THR A CG2 1 
ATOM   277  N  N   . HIS A 1 36  ? -12.984 -12.870 34.694  1.00 22.11 ? 36  HIS A N   1 
ATOM   278  C  CA  . HIS A 1 36  ? -13.204 -13.075 36.090  1.00 22.85 ? 36  HIS A CA  1 
ATOM   279  C  C   . HIS A 1 36  ? -12.723 -11.966 36.978  1.00 22.96 ? 36  HIS A C   1 
ATOM   280  O  O   . HIS A 1 36  ? -13.431 -11.667 37.912  1.00 23.64 ? 36  HIS A O   1 
ATOM   281  C  CB  . HIS A 1 36  ? -12.728 -14.464 36.517  1.00 23.42 ? 36  HIS A CB  1 
ATOM   282  C  CG  . HIS A 1 36  ? -13.614 -15.551 35.991  1.00 24.26 ? 36  HIS A CG  1 
ATOM   283  N  ND1 . HIS A 1 36  ? -13.197 -16.452 35.041  1.00 25.82 ? 36  HIS A ND1 1 
ATOM   284  C  CD2 . HIS A 1 36  ? -14.926 -15.813 36.216  1.00 24.81 ? 36  HIS A CD2 1 
ATOM   285  C  CE1 . HIS A 1 36  ? -14.199 -17.256 34.738  1.00 27.81 ? 36  HIS A CE1 1 
ATOM   286  N  NE2 . HIS A 1 36  ? -15.265 -16.881 35.423  1.00 29.35 ? 36  HIS A NE2 1 
ATOM   287  N  N   . THR A 1 37  ? -11.601 -11.311 36.652  1.00 22.92 ? 37  THR A N   1 
ATOM   288  C  CA  . THR A 1 37  ? -11.096 -10.185 37.432  1.00 23.87 ? 37  THR A CA  1 
ATOM   289  C  C   . THR A 1 37  ? -11.515 -8.783  36.927  1.00 22.88 ? 37  THR A C   1 
ATOM   290  O  O   . THR A 1 37  ? -11.183 -7.764  37.552  1.00 22.49 ? 37  THR A O   1 
ATOM   291  C  CB  . THR A 1 37  ? -9.555  -10.206 37.595  1.00 24.58 ? 37  THR A CB  1 
ATOM   292  O  OG1 . THR A 1 37  ? -8.954  -10.088 36.321  1.00 28.73 ? 37  THR A OG1 1 
ATOM   293  C  CG2 . THR A 1 37  ? -9.060  -11.472 38.269  1.00 26.90 ? 37  THR A CG2 1 
ATOM   294  N  N   . ALA A 1 38  ? -12.185 -8.719  35.775  1.00 21.78 ? 38  ALA A N   1 
ATOM   295  C  CA  . ALA A 1 38  ? -12.722 -7.443  35.312  1.00 22.66 ? 38  ALA A CA  1 
ATOM   296  C  C   . ALA A 1 38  ? -13.784 -7.009  36.327  1.00 23.36 ? 38  ALA A C   1 
ATOM   297  O  O   . ALA A 1 38  ? -14.628 -7.789  36.745  1.00 24.99 ? 38  ALA A O   1 
ATOM   298  C  CB  . ALA A 1 38  ? -13.338 -7.600  33.926  1.00 20.89 ? 38  ALA A CB  1 
ATOM   299  N  N   . LYS A 1 39  ? -13.772 -5.750  36.688  1.00 23.69 ? 39  LYS A N   1 
ATOM   300  C  CA  . LYS A 1 39  ? -14.703 -5.266  37.670  1.00 24.41 ? 39  LYS A CA  1 
ATOM   301  C  C   . LYS A 1 39  ? -16.044 -4.775  37.068  1.00 24.72 ? 39  LYS A C   1 
ATOM   302  O  O   . LYS A 1 39  ? -16.089 -3.740  36.346  1.00 22.94 ? 39  LYS A O   1 
ATOM   303  C  CB  . LYS A 1 39  ? -14.008 -4.166  38.465  1.00 24.96 ? 39  LYS A CB  1 
ATOM   304  C  CG  . LYS A 1 39  ? -14.920 -3.405  39.411  1.00 26.36 ? 39  LYS A CG  1 
ATOM   305  C  CD  . LYS A 1 39  ? -14.936 -4.033  40.794  1.00 24.65 ? 39  LYS A CD  1 
ATOM   306  C  CE  . LYS A 1 39  ? -15.806 -3.168  41.742  1.00 29.01 ? 39  LYS A CE  1 
ATOM   307  N  NZ  . LYS A 1 39  ? -16.530 -3.974  42.739  1.00 30.29 ? 39  LYS A NZ  1 
ATOM   308  N  N   . TYR A 1 40  ? -17.136 -5.466  37.403  1.00 24.28 ? 40  TYR A N   1 
ATOM   309  C  CA  . TYR A 1 40  ? -18.463 -4.872  37.149  1.00 26.97 ? 40  TYR A CA  1 
ATOM   310  C  C   . TYR A 1 40  ? -18.671 -3.461  37.776  1.00 27.86 ? 40  TYR A C   1 
ATOM   311  O  O   . TYR A 1 40  ? -18.489 -3.238  39.016  1.00 26.81 ? 40  TYR A O   1 
ATOM   312  C  CB  . TYR A 1 40  ? -19.617 -5.812  37.510  1.00 26.63 ? 40  TYR A CB  1 
ATOM   313  C  CG  . TYR A 1 40  ? -20.957 -5.144  37.350  1.00 28.96 ? 40  TYR A CG  1 
ATOM   314  C  CD1 . TYR A 1 40  ? -21.422 -4.764  36.077  1.00 28.92 ? 40  TYR A CD1 1 
ATOM   315  C  CD2 . TYR A 1 40  ? -21.761 -4.854  38.470  1.00 32.00 ? 40  TYR A CD2 1 
ATOM   316  C  CE1 . TYR A 1 40  ? -22.620 -4.149  35.899  1.00 27.55 ? 40  TYR A CE1 1 
ATOM   317  C  CE2 . TYR A 1 40  ? -23.004 -4.224  38.302  1.00 31.87 ? 40  TYR A CE2 1 
ATOM   318  C  CZ  . TYR A 1 40  ? -23.419 -3.880  37.006  1.00 31.28 ? 40  TYR A CZ  1 
ATOM   319  O  OH  . TYR A 1 40  ? -24.629 -3.265  36.808  1.00 30.23 ? 40  TYR A OH  1 
ATOM   320  N  N   . ASP A 1 41  ? -19.053 -2.526  36.894  1.00 28.19 ? 41  ASP A N   1 
ATOM   321  C  CA  . ASP A 1 41  ? -19.318 -1.163  37.292  1.00 29.96 ? 41  ASP A CA  1 
ATOM   322  C  C   . ASP A 1 41  ? -20.747 -0.723  36.929  1.00 30.91 ? 41  ASP A C   1 
ATOM   323  O  O   . ASP A 1 41  ? -21.009 -0.287  35.794  1.00 31.49 ? 41  ASP A O   1 
ATOM   324  C  CB  . ASP A 1 41  ? -18.229 -0.205  36.789  1.00 29.64 ? 41  ASP A CB  1 
ATOM   325  C  CG  . ASP A 1 41  ? -18.435 1.220   37.273  1.00 32.87 ? 41  ASP A CG  1 
ATOM   326  O  OD1 . ASP A 1 41  ? -19.444 1.431   38.002  1.00 35.98 ? 41  ASP A OD1 1 
ATOM   327  O  OD2 . ASP A 1 41  ? -17.619 2.113   36.919  1.00 31.82 ? 41  ASP A OD2 1 
ATOM   328  N  N   . PRO A 1 42  ? -21.684 -0.833  37.906  1.00 31.97 ? 42  PRO A N   1 
ATOM   329  C  CA  . PRO A 1 42  ? -23.091 -0.402  37.759  1.00 32.16 ? 42  PRO A CA  1 
ATOM   330  C  C   . PRO A 1 42  ? -23.256 1.089   37.399  1.00 31.73 ? 42  PRO A C   1 
ATOM   331  O  O   . PRO A 1 42  ? -24.317 1.484   36.905  1.00 32.39 ? 42  PRO A O   1 
ATOM   332  C  CB  . PRO A 1 42  ? -23.695 -0.716  39.154  1.00 32.05 ? 42  PRO A CB  1 
ATOM   333  C  CG  . PRO A 1 42  ? -22.524 -0.728  40.061  1.00 32.24 ? 42  PRO A CG  1 
ATOM   334  C  CD  . PRO A 1 42  ? -21.452 -1.381  39.255  1.00 31.66 ? 42  PRO A CD  1 
ATOM   335  N  N   . SER A 1 43  ? -22.228 1.902   37.628  1.00 31.69 ? 43  SER A N   1 
ATOM   336  C  CA  . SER A 1 43  ? -22.268 3.288   37.179  1.00 31.99 ? 43  SER A CA  1 
ATOM   337  C  C   . SER A 1 43  ? -21.838 3.533   35.702  1.00 31.82 ? 43  SER A C   1 
ATOM   338  O  O   . SER A 1 43  ? -21.946 4.665   35.190  1.00 32.35 ? 43  SER A O   1 
ATOM   339  C  CB  . SER A 1 43  ? -21.481 4.178   38.137  1.00 32.70 ? 43  SER A CB  1 
ATOM   340  O  OG  . SER A 1 43  ? -20.093 4.174   37.828  1.00 35.86 ? 43  SER A OG  1 
ATOM   341  N  N   . LEU A 1 44  ? -21.368 2.492   35.007  1.00 30.55 ? 44  LEU A N   1 
ATOM   342  C  CA  . LEU A 1 44  ? -21.057 2.630   33.578  1.00 29.01 ? 44  LEU A CA  1 
ATOM   343  C  C   . LEU A 1 44  ? -22.332 2.802   32.789  1.00 28.89 ? 44  LEU A C   1 
ATOM   344  O  O   . LEU A 1 44  ? -23.301 2.078   33.007  1.00 29.26 ? 44  LEU A O   1 
ATOM   345  C  CB  . LEU A 1 44  ? -20.287 1.395   33.056  1.00 29.14 ? 44  LEU A CB  1 
ATOM   346  C  CG  . LEU A 1 44  ? -18.803 1.365   33.396  1.00 25.29 ? 44  LEU A CG  1 
ATOM   347  C  CD1 . LEU A 1 44  ? -18.232 0.022   32.972  1.00 26.20 ? 44  LEU A CD1 1 
ATOM   348  C  CD2 . LEU A 1 44  ? -18.071 2.446   32.717  1.00 23.89 ? 44  LEU A CD2 1 
ATOM   349  N  N   . LYS A 1 45  ? -22.364 3.768   31.886  1.00 28.80 ? 45  LYS A N   1 
ATOM   350  C  CA  . LYS A 1 45  ? -23.606 4.012   31.127  1.00 28.59 ? 45  LYS A CA  1 
ATOM   351  C  C   . LYS A 1 45  ? -23.707 3.064   29.938  1.00 27.63 ? 45  LYS A C   1 
ATOM   352  O  O   . LYS A 1 45  ? -22.670 2.461   29.549  1.00 26.69 ? 45  LYS A O   1 
ATOM   353  C  CB  . LYS A 1 45  ? -23.734 5.473   30.745  1.00 28.57 ? 45  LYS A CB  1 
ATOM   354  C  CG  . LYS A 1 45  ? -23.857 6.329   32.014  1.00 31.55 ? 45  LYS A CG  1 
ATOM   355  C  CD  . LYS A 1 45  ? -24.477 7.716   31.821  1.00 37.02 ? 45  LYS A CD  1 
ATOM   356  C  CE  . LYS A 1 45  ? -23.450 8.757   31.407  1.00 41.83 ? 45  LYS A CE  1 
ATOM   357  N  NZ  . LYS A 1 45  ? -22.225 8.824   32.303  1.00 41.65 ? 45  LYS A NZ  1 
ATOM   358  N  N   . PRO A 1 46  ? -24.948 2.875   29.386  1.00 26.81 ? 46  PRO A N   1 
ATOM   359  C  CA  . PRO A 1 46  ? -25.000 2.222   28.075  1.00 25.95 ? 46  PRO A CA  1 
ATOM   360  C  C   . PRO A 1 46  ? -24.168 3.004   27.058  1.00 24.21 ? 46  PRO A C   1 
ATOM   361  O  O   . PRO A 1 46  ? -24.083 4.214   27.109  1.00 22.98 ? 46  PRO A O   1 
ATOM   362  C  CB  . PRO A 1 46  ? -26.497 2.301   27.668  1.00 26.27 ? 46  PRO A CB  1 
ATOM   363  C  CG  . PRO A 1 46  ? -27.211 2.508   28.871  1.00 26.16 ? 46  PRO A CG  1 
ATOM   364  C  CD  . PRO A 1 46  ? -26.298 3.250   29.840  1.00 26.94 ? 46  PRO A CD  1 
ATOM   365  N  N   . LEU A 1 47  ? -23.570 2.270   26.138  1.00 23.36 ? 47  LEU A N   1 
ATOM   366  C  CA  . LEU A 1 47  ? -22.805 2.803   25.087  1.00 22.64 ? 47  LEU A CA  1 
ATOM   367  C  C   . LEU A 1 47  ? -23.815 3.329   24.069  1.00 23.27 ? 47  LEU A C   1 
ATOM   368  O  O   . LEU A 1 47  ? -24.843 2.682   23.845  1.00 22.69 ? 47  LEU A O   1 
ATOM   369  C  CB  . LEU A 1 47  ? -21.982 1.666   24.504  1.00 22.60 ? 47  LEU A CB  1 
ATOM   370  C  CG  . LEU A 1 47  ? -20.916 2.031   23.502  1.00 26.16 ? 47  LEU A CG  1 
ATOM   371  C  CD1 . LEU A 1 47  ? -20.015 3.186   24.043  1.00 29.29 ? 47  LEU A CD1 1 
ATOM   372  C  CD2 . LEU A 1 47  ? -20.176 0.742   23.347  1.00 26.24 ? 47  LEU A CD2 1 
ATOM   373  N  N   . SER A 1 48  ? -23.532 4.508   23.507  1.00 21.84 ? 48  SER A N   1 
ATOM   374  C  CA  . SER A 1 48  ? -24.382 5.154   22.512  1.00 23.49 ? 48  SER A CA  1 
ATOM   375  C  C   . SER A 1 48  ? -23.637 5.225   21.194  1.00 22.74 ? 48  SER A C   1 
ATOM   376  O  O   . SER A 1 48  ? -22.627 5.873   21.068  1.00 21.88 ? 48  SER A O   1 
ATOM   377  C  CB  . SER A 1 48  ? -24.811 6.566   22.981  1.00 23.18 ? 48  SER A CB  1 
ATOM   378  O  OG  . SER A 1 48  ? -25.549 7.254   21.984  1.00 26.79 ? 48  SER A OG  1 
ATOM   379  N  N   . VAL A 1 49  ? -24.150 4.507   20.221  1.00 23.33 ? 49  VAL A N   1 
ATOM   380  C  CA  . VAL A 1 49  ? -23.583 4.443   18.899  1.00 24.67 ? 49  VAL A CA  1 
ATOM   381  C  C   . VAL A 1 49  ? -24.597 5.110   17.952  1.00 25.68 ? 49  VAL A C   1 
ATOM   382  O  O   . VAL A 1 49  ? -25.682 4.578   17.686  1.00 26.32 ? 49  VAL A O   1 
ATOM   383  C  CB  . VAL A 1 49  ? -23.396 2.972   18.518  1.00 24.15 ? 49  VAL A CB  1 
ATOM   384  C  CG1 . VAL A 1 49  ? -22.656 2.848   17.216  1.00 25.63 ? 49  VAL A CG1 1 
ATOM   385  C  CG2 . VAL A 1 49  ? -22.630 2.240   19.618  1.00 23.50 ? 49  VAL A CG2 1 
ATOM   386  N  N   . SER A 1 50  ? -24.290 6.321   17.507  1.00 25.32 ? 50  SER A N   1 
ATOM   387  C  CA  . SER A 1 50  ? -25.093 6.942   16.488  1.00 24.19 ? 50  SER A CA  1 
ATOM   388  C  C   . SER A 1 50  ? -24.371 6.955   15.170  1.00 22.60 ? 50  SER A C   1 
ATOM   389  O  O   . SER A 1 50  ? -23.565 7.868   14.894  1.00 21.35 ? 50  SER A O   1 
ATOM   390  C  CB  . SER A 1 50  ? -25.530 8.331   16.916  1.00 24.32 ? 50  SER A CB  1 
ATOM   391  O  OG  . SER A 1 50  ? -26.105 8.152   18.164  1.00 29.04 ? 50  SER A OG  1 
ATOM   392  N  N   . TYR A 1 51  ? -24.679 5.930   14.374  1.00 20.63 ? 51  TYR A N   1 
ATOM   393  C  CA  . TYR A 1 51  ? -24.099 5.723   13.060  1.00 21.08 ? 51  TYR A CA  1 
ATOM   394  C  C   . TYR A 1 51  ? -25.140 5.919   11.921  1.00 22.18 ? 51  TYR A C   1 
ATOM   395  O  O   . TYR A 1 51  ? -24.799 5.778   10.748  1.00 20.62 ? 51  TYR A O   1 
ATOM   396  C  CB  . TYR A 1 51  ? -23.429 4.332   12.949  1.00 19.73 ? 51  TYR A CB  1 
ATOM   397  C  CG  . TYR A 1 51  ? -22.143 4.060   13.752  1.00 19.73 ? 51  TYR A CG  1 
ATOM   398  C  CD1 . TYR A 1 51  ? -21.412 5.093   14.371  1.00 20.63 ? 51  TYR A CD1 1 
ATOM   399  C  CD2 . TYR A 1 51  ? -21.638 2.765   13.832  1.00 17.77 ? 51  TYR A CD2 1 
ATOM   400  C  CE1 . TYR A 1 51  ? -20.223 4.805   15.118  1.00 17.88 ? 51  TYR A CE1 1 
ATOM   401  C  CE2 . TYR A 1 51  ? -20.485 2.469   14.512  1.00 17.31 ? 51  TYR A CE2 1 
ATOM   402  C  CZ  . TYR A 1 51  ? -19.761 3.494   15.157  1.00 19.13 ? 51  TYR A CZ  1 
ATOM   403  O  OH  . TYR A 1 51  ? -18.586 3.155   15.813  1.00 17.21 ? 51  TYR A OH  1 
ATOM   404  N  N   . ASP A 1 52  ? -26.377 6.300   12.264  1.00 24.42 ? 52  ASP A N   1 
ATOM   405  C  CA  . ASP A 1 52  ? -27.391 6.652   11.209  1.00 26.76 ? 52  ASP A CA  1 
ATOM   406  C  C   . ASP A 1 52  ? -26.913 7.560   10.056  1.00 26.48 ? 52  ASP A C   1 
ATOM   407  O  O   . ASP A 1 52  ? -27.276 7.331   8.894   1.00 27.55 ? 52  ASP A O   1 
ATOM   408  C  CB  . ASP A 1 52  ? -28.732 7.154   11.808  1.00 27.64 ? 52  ASP A CB  1 
ATOM   409  C  CG  . ASP A 1 52  ? -28.601 8.444   12.585  1.00 33.40 ? 52  ASP A CG  1 
ATOM   410  O  OD1 . ASP A 1 52  ? -28.280 8.395   13.823  1.00 37.85 ? 52  ASP A OD1 1 
ATOM   411  O  OD2 . ASP A 1 52  ? -28.875 9.518   11.968  1.00 39.91 ? 52  ASP A OD2 1 
ATOM   412  N  N   . GLN A 1 53  ? -26.071 8.545   10.354  1.00 26.45 ? 53  GLN A N   1 
ATOM   413  C  CA  . GLN A 1 53  ? -25.655 9.535   9.327   1.00 26.51 ? 53  GLN A CA  1 
ATOM   414  C  C   . GLN A 1 53  ? -24.218 9.387   8.825   1.00 24.85 ? 53  GLN A C   1 
ATOM   415  O  O   . GLN A 1 53  ? -23.635 10.341  8.254   1.00 23.78 ? 53  GLN A O   1 
ATOM   416  C  CB  . GLN A 1 53  ? -25.910 10.971  9.856   1.00 27.63 ? 53  GLN A CB  1 
ATOM   417  C  CG  . GLN A 1 53  ? -27.442 11.383  9.913   1.00 31.34 ? 53  GLN A CG  1 
ATOM   418  C  CD  . GLN A 1 53  ? -28.266 10.768  8.788   1.00 37.82 ? 53  GLN A CD  1 
ATOM   419  O  OE1 . GLN A 1 53  ? -27.926 10.880  7.587   1.00 39.91 ? 53  GLN A OE1 1 
ATOM   420  N  NE2 . GLN A 1 53  ? -29.353 10.077  9.167   1.00 40.73 ? 53  GLN A NE2 1 
ATOM   421  N  N   . ALA A 1 54  ? -23.645 8.189   9.045   1.00 21.94 ? 54  ALA A N   1 
ATOM   422  C  CA  . ALA A 1 54  ? -22.299 7.895   8.663   1.00 20.41 ? 54  ALA A CA  1 
ATOM   423  C  C   . ALA A 1 54  ? -22.088 8.103   7.150   1.00 20.96 ? 54  ALA A C   1 
ATOM   424  O  O   . ALA A 1 54  ? -22.920 7.680   6.325   1.00 19.92 ? 54  ALA A O   1 
ATOM   425  C  CB  . ALA A 1 54  ? -21.888 6.451   9.094   1.00 19.13 ? 54  ALA A CB  1 
ATOM   426  N  N   . THR A 1 55  ? -20.961 8.719   6.813   1.00 20.17 ? 55  THR A N   1 
ATOM   427  C  CA  . THR A 1 55  ? -20.551 8.921   5.419   1.00 20.84 ? 55  THR A CA  1 
ATOM   428  C  C   . THR A 1 55  ? -19.224 8.285   5.188   1.00 20.10 ? 55  THR A C   1 
ATOM   429  O  O   . THR A 1 55  ? -18.193 8.900   5.471   1.00 20.71 ? 55  THR A O   1 
ATOM   430  C  CB  . THR A 1 55  ? -20.427 10.440  5.044   1.00 21.07 ? 55  THR A CB  1 
ATOM   431  O  OG1 . THR A 1 55  ? -21.714 11.040  5.175   1.00 23.69 ? 55  THR A OG1 1 
ATOM   432  C  CG2 . THR A 1 55  ? -19.953 10.624  3.549   1.00 22.10 ? 55  THR A CG2 1 
ATOM   433  N  N   . SER A 1 56  ? -19.232 7.052   4.686   1.00 20.07 ? 56  SER A N   1 
ATOM   434  C  CA  . SER A 1 56  ? -17.984 6.410   4.251   1.00 20.54 ? 56  SER A CA  1 
ATOM   435  C  C   . SER A 1 56  ? -17.560 7.152   2.966   1.00 20.91 ? 56  SER A C   1 
ATOM   436  O  O   . SER A 1 56  ? -18.423 7.660   2.198   1.00 19.79 ? 56  SER A O   1 
ATOM   437  C  CB  . SER A 1 56  ? -18.143 4.855   4.055   1.00 20.53 ? 56  SER A CB  1 
ATOM   438  O  OG  . SER A 1 56  ? -19.142 4.523   3.065   1.00 21.47 ? 56  SER A OG  1 
ATOM   439  N  N   . LEU A 1 57  ? -16.248 7.240   2.779   1.00 19.50 ? 57  LEU A N   1 
ATOM   440  C  CA  . LEU A 1 57  ? -15.665 7.929   1.673   1.00 21.63 ? 57  LEU A CA  1 
ATOM   441  C  C   . LEU A 1 57  ? -14.852 6.976   0.814   1.00 20.97 ? 57  LEU A C   1 
ATOM   442  O  O   . LEU A 1 57  ? -14.948 6.963   -0.427  1.00 20.85 ? 57  LEU A O   1 
ATOM   443  C  CB  . LEU A 1 57  ? -14.722 9.037   2.178   1.00 20.09 ? 57  LEU A CB  1 
ATOM   444  C  CG  . LEU A 1 57  ? -15.503 10.140  2.940   1.00 23.86 ? 57  LEU A CG  1 
ATOM   445  C  CD1 . LEU A 1 57  ? -14.518 11.149  3.646   1.00 24.62 ? 57  LEU A CD1 1 
ATOM   446  C  CD2 . LEU A 1 57  ? -16.526 10.834  2.030   1.00 23.07 ? 57  LEU A CD2 1 
ATOM   447  N  N   . ARG A 1 58  ? -14.006 6.217   1.492   1.00 19.83 ? 58  ARG A N   1 
ATOM   448  C  CA  . ARG A 1 58  ? -12.914 5.566   0.845   1.00 19.06 ? 58  ARG A CA  1 
ATOM   449  C  C   . ARG A 1 58  ? -12.359 4.334   1.633   1.00 17.85 ? 58  ARG A C   1 
ATOM   450  O  O   . ARG A 1 58  ? -12.475 4.253   2.867   1.00 15.08 ? 58  ARG A O   1 
ATOM   451  C  CB  . ARG A 1 58  ? -11.828 6.618   0.662   1.00 21.01 ? 58  ARG A CB  1 
ATOM   452  C  CG  . ARG A 1 58  ? -10.994 6.349   -0.532  1.00 26.75 ? 58  ARG A CG  1 
ATOM   453  C  CD  . ARG A 1 58  ? -9.881  7.359   -0.675  1.00 32.10 ? 58  ARG A CD  1 
ATOM   454  N  NE  . ARG A 1 58  ? -9.078  7.187   0.512   1.00 32.15 ? 58  ARG A NE  1 
ATOM   455  C  CZ  . ARG A 1 58  ? -7.774  7.370   0.552   1.00 32.72 ? 58  ARG A CZ  1 
ATOM   456  N  NH1 . ARG A 1 58  ? -7.125  7.716   -0.544  1.00 30.77 ? 58  ARG A NH1 1 
ATOM   457  N  NH2 . ARG A 1 58  ? -7.131  7.187   1.698   1.00 31.07 ? 58  ARG A NH2 1 
ATOM   458  N  N   . ILE A 1 59  ? -11.838 3.360   0.898   1.00 14.83 ? 59  ILE A N   1 
ATOM   459  C  CA  . ILE A 1 59  ? -11.194 2.216   1.527   1.00 16.08 ? 59  ILE A CA  1 
ATOM   460  C  C   . ILE A 1 59  ? -9.744  2.193   1.062   1.00 16.14 ? 59  ILE A C   1 
ATOM   461  O  O   . ILE A 1 59  ? -9.440  2.304   -0.178  1.00 15.20 ? 59  ILE A O   1 
ATOM   462  C  CB  . ILE A 1 59  ? -11.910 0.862   1.225   1.00 14.39 ? 59  ILE A CB  1 
ATOM   463  C  CG1 . ILE A 1 59  ? -11.317 -0.271  2.109   1.00 17.82 ? 59  ILE A CG1 1 
ATOM   464  C  CG2 . ILE A 1 59  ? -11.841 0.517   -0.277  1.00 14.10 ? 59  ILE A CG2 1 
ATOM   465  C  CD1 . ILE A 1 59  ? -12.019 -1.621  2.031   1.00 16.46 ? 59  ILE A CD1 1 
ATOM   466  N  N   . LEU A 1 60  ? -8.849  2.013   2.033   1.00 16.65 ? 60  LEU A N   1 
ATOM   467  C  CA  . LEU A 1 60  ? -7.414  2.056   1.733   1.00 16.82 ? 60  LEU A CA  1 
ATOM   468  C  C   . LEU A 1 60  ? -6.620  0.863   2.238   1.00 16.25 ? 60  LEU A C   1 
ATOM   469  O  O   . LEU A 1 60  ? -6.767  0.462   3.391   1.00 13.33 ? 60  LEU A O   1 
ATOM   470  C  CB  . LEU A 1 60  ? -6.817  3.355   2.357   1.00 17.52 ? 60  LEU A CB  1 
ATOM   471  C  CG  . LEU A 1 60  ? -5.310  3.562   2.470   1.00 16.98 ? 60  LEU A CG  1 
ATOM   472  C  CD1 . LEU A 1 60  ? -4.738  3.952   1.085   1.00 21.25 ? 60  LEU A CD1 1 
ATOM   473  C  CD2 . LEU A 1 60  ? -4.921  4.647   3.492   1.00 17.35 ? 60  LEU A CD2 1 
ATOM   474  N  N   . ASN A 1 61  ? -5.740  0.328   1.388   1.00 15.80 ? 61  ASN A N   1 
ATOM   475  C  CA  . ASN A 1 61  ? -4.644  -0.542  1.898   1.00 16.76 ? 61  ASN A CA  1 
ATOM   476  C  C   . ASN A 1 61  ? -3.391  0.315   2.261   1.00 17.60 ? 61  ASN A C   1 
ATOM   477  O  O   . ASN A 1 61  ? -2.705  0.868   1.386   1.00 16.82 ? 61  ASN A O   1 
ATOM   478  C  CB  . ASN A 1 61  ? -4.365  -1.684  0.899   1.00 16.97 ? 61  ASN A CB  1 
ATOM   479  C  CG  . ASN A 1 61  ? -3.219  -2.608  1.276   1.00 14.96 ? 61  ASN A CG  1 
ATOM   480  O  OD1 . ASN A 1 61  ? -2.432  -2.349  2.158   1.00 18.88 ? 61  ASN A OD1 1 
ATOM   481  N  ND2 . ASN A 1 61  ? -3.124  -3.741  0.561   1.00 15.28 ? 61  ASN A ND2 1 
ATOM   482  N  N   . ASN A 1 62  ? -3.088  0.360   3.564   1.00 17.41 ? 62  ASN A N   1 
ATOM   483  C  CA  . ASN A 1 62  ? -2.035  1.198   4.126   1.00 16.90 ? 62  ASN A CA  1 
ATOM   484  C  C   . ASN A 1 62  ? -0.765  0.330   4.329   1.00 18.37 ? 62  ASN A C   1 
ATOM   485  O  O   . ASN A 1 62  ? 0.198   0.773   4.956   1.00 20.52 ? 62  ASN A O   1 
ATOM   486  C  CB  . ASN A 1 62  ? -2.547  1.888   5.411   1.00 17.93 ? 62  ASN A CB  1 
ATOM   487  C  CG  . ASN A 1 62  ? -2.534  0.974   6.663   1.00 15.93 ? 62  ASN A CG  1 
ATOM   488  O  OD1 . ASN A 1 62  ? -2.417  -0.243  6.561   1.00 15.26 ? 62  ASN A OD1 1 
ATOM   489  N  ND2 . ASN A 1 62  ? -2.629  1.587   7.871   1.00 15.82 ? 62  ASN A ND2 1 
ATOM   490  N  N   . GLY A 1 63  ? -0.781  -0.900  3.786   1.00 15.91 ? 63  GLY A N   1 
ATOM   491  C  CA  . GLY A 1 63  ? 0.268   -1.858  3.936   1.00 15.87 ? 63  GLY A CA  1 
ATOM   492  C  C   . GLY A 1 63  ? 0.351   -2.544  5.290   1.00 17.07 ? 63  GLY A C   1 
ATOM   493  O  O   . GLY A 1 63  ? 1.219   -3.355  5.499   1.00 16.33 ? 63  GLY A O   1 
ATOM   494  N  N   . HIS A 1 64  ? -0.541  -2.211  6.229   1.00 16.02 ? 64  HIS A N   1 
ATOM   495  C  CA  . HIS A 1 64  ? -0.574  -2.918  7.521   1.00 16.55 ? 64  HIS A CA  1 
ATOM   496  C  C   . HIS A 1 64  ? -1.975  -3.574  7.692   1.00 16.49 ? 64  HIS A C   1 
ATOM   497  O  O   . HIS A 1 64  ? -2.095  -4.623  8.301   1.00 18.36 ? 64  HIS A O   1 
ATOM   498  C  CB  . HIS A 1 64  ? -0.292  -1.947  8.638   1.00 16.66 ? 64  HIS A CB  1 
ATOM   499  C  CG  . HIS A 1 64  ? 1.013   -1.211  8.480   1.00 18.72 ? 64  HIS A CG  1 
ATOM   500  N  ND1 . HIS A 1 64  ? 2.240   -1.837  8.588   1.00 19.55 ? 64  HIS A ND1 1 
ATOM   501  C  CD2 . HIS A 1 64  ? 1.279   0.089   8.233   1.00 19.85 ? 64  HIS A CD2 1 
ATOM   502  C  CE1 . HIS A 1 64  ? 3.208   -0.952  8.445   1.00 18.57 ? 64  HIS A CE1 1 
ATOM   503  N  NE2 . HIS A 1 64  ? 2.654   0.221   8.214   1.00 19.68 ? 64  HIS A NE2 1 
ATOM   504  N  N   . ALA A 1 65  ? -2.990  -2.981  7.075   1.00 15.06 ? 65  ALA A N   1 
ATOM   505  C  CA  . ALA A 1 65  ? -4.371  -3.413  7.201   1.00 15.17 ? 65  ALA A CA  1 
ATOM   506  C  C   . ALA A 1 65  ? -5.123  -2.700  6.088   1.00 14.76 ? 65  ALA A C   1 
ATOM   507  O  O   . ALA A 1 65  ? -4.505  -2.080  5.217   1.00 16.38 ? 65  ALA A O   1 
ATOM   508  C  CB  . ALA A 1 65  ? -4.931  -3.001  8.600   1.00 13.74 ? 65  ALA A CB  1 
ATOM   509  N  N   . PHE A 1 66  ? -6.448  -2.798  6.087   1.00 14.05 ? 66  PHE A N   1 
ATOM   510  C  CA  . PHE A 1 66  ? -7.221  -1.860  5.324   1.00 14.32 ? 66  PHE A CA  1 
ATOM   511  C  C   . PHE A 1 66  ? -8.086  -0.978  6.162   1.00 13.62 ? 66  PHE A C   1 
ATOM   512  O  O   . PHE A 1 66  ? -8.756  -1.435  7.111   1.00 13.37 ? 66  PHE A O   1 
ATOM   513  C  CB  . PHE A 1 66  ? -8.071  -2.510  4.187   1.00 13.05 ? 66  PHE A CB  1 
ATOM   514  C  CG  . PHE A 1 66  ? -9.152  -3.459  4.696   1.00 15.10 ? 66  PHE A CG  1 
ATOM   515  C  CD1 . PHE A 1 66  ? -10.437 -2.978  4.960   1.00 12.86 ? 66  PHE A CD1 1 
ATOM   516  C  CD2 . PHE A 1 66  ? -8.878  -4.832  4.858   1.00 14.49 ? 66  PHE A CD2 1 
ATOM   517  C  CE1 . PHE A 1 66  ? -11.436 -3.858  5.418   1.00 14.67 ? 66  PHE A CE1 1 
ATOM   518  C  CE2 . PHE A 1 66  ? -9.858  -5.720  5.312   1.00 13.77 ? 66  PHE A CE2 1 
ATOM   519  C  CZ  . PHE A 1 66  ? -11.134 -5.255  5.584   1.00 13.05 ? 66  PHE A CZ  1 
ATOM   520  N  N   . ASN A 1 67  ? -8.181  0.266   5.721   1.00 13.79 ? 67  ASN A N   1 
ATOM   521  C  CA  . ASN A 1 67  ? -9.016  1.217   6.414   1.00 14.36 ? 67  ASN A CA  1 
ATOM   522  C  C   . ASN A 1 67  ? -10.157 1.619   5.595   1.00 14.63 ? 67  ASN A C   1 
ATOM   523  O  O   . ASN A 1 67  ? -10.006 2.079   4.453   1.00 15.04 ? 67  ASN A O   1 
ATOM   524  C  CB  . ASN A 1 67  ? -8.280  2.527   6.742   1.00 14.71 ? 67  ASN A CB  1 
ATOM   525  C  CG  . ASN A 1 67  ? -7.243  2.347   7.767   1.00 15.46 ? 67  ASN A CG  1 
ATOM   526  O  OD1 . ASN A 1 67  ? -7.212  1.309   8.409   1.00 15.75 ? 67  ASN A OD1 1 
ATOM   527  N  ND2 . ASN A 1 67  ? -6.339  3.326   7.903   1.00 18.69 ? 67  ASN A ND2 1 
ATOM   528  N  N   . VAL A 1 68  ? -11.309 1.543   6.210   1.00 14.99 ? 68  VAL A N   1 
ATOM   529  C  CA  . VAL A 1 68  ? -12.465 2.236   5.627   1.00 14.79 ? 68  VAL A CA  1 
ATOM   530  C  C   . VAL A 1 68  ? -12.609 3.572   6.363   1.00 16.41 ? 68  VAL A C   1 
ATOM   531  O  O   . VAL A 1 68  ? -12.837 3.580   7.585   1.00 15.92 ? 68  VAL A O   1 
ATOM   532  C  CB  . VAL A 1 68  ? -13.747 1.405   5.806   1.00 13.87 ? 68  VAL A CB  1 
ATOM   533  C  CG1 . VAL A 1 68  ? -15.051 2.278   5.450   1.00 13.54 ? 68  VAL A CG1 1 
ATOM   534  C  CG2 . VAL A 1 68  ? -13.673 0.153   4.966   1.00 11.71 ? 68  VAL A CG2 1 
ATOM   535  N  N   . GLU A 1 69  ? -12.510 4.671   5.625   1.00 16.71 ? 69  GLU A N   1 
ATOM   536  C  CA  . GLU A 1 69  ? -12.502 6.030   6.186   1.00 19.16 ? 69  GLU A CA  1 
ATOM   537  C  C   . GLU A 1 69  ? -13.820 6.745   5.978   1.00 19.98 ? 69  GLU A C   1 
ATOM   538  O  O   . GLU A 1 69  ? -14.487 6.552   4.946   1.00 20.43 ? 69  GLU A O   1 
ATOM   539  C  CB  . GLU A 1 69  ? -11.454 6.840   5.472   1.00 19.52 ? 69  GLU A CB  1 
ATOM   540  C  CG  . GLU A 1 69  ? -10.179 6.094   5.328   1.00 20.55 ? 69  GLU A CG  1 
ATOM   541  C  CD  . GLU A 1 69  ? -9.399  6.509   4.090   1.00 25.75 ? 69  GLU A CD  1 
ATOM   542  O  OE1 . GLU A 1 69  ? -9.995  7.249   3.266   1.00 27.79 ? 69  GLU A OE1 1 
ATOM   543  O  OE2 . GLU A 1 69  ? -8.207  6.070   3.925   1.00 23.19 ? 69  GLU A OE2 1 
ATOM   544  N  N   . PHE A 1 70  ? -14.140 7.604   6.948   1.00 18.65 ? 70  PHE A N   1 
ATOM   545  C  CA  . PHE A 1 70  ? -15.420 8.280   7.093   1.00 16.99 ? 70  PHE A CA  1 
ATOM   546  C  C   . PHE A 1 70  ? -15.208 9.798   7.043   1.00 17.58 ? 70  PHE A C   1 
ATOM   547  O  O   . PHE A 1 70  ? -14.126 10.276  7.320   1.00 15.34 ? 70  PHE A O   1 
ATOM   548  C  CB  . PHE A 1 70  ? -16.099 7.855   8.424   1.00 15.12 ? 70  PHE A CB  1 
ATOM   549  C  CG  . PHE A 1 70  ? -16.718 6.475   8.338   1.00 15.07 ? 70  PHE A CG  1 
ATOM   550  C  CD1 . PHE A 1 70  ? -15.944 5.334   8.536   1.00 17.15 ? 70  PHE A CD1 1 
ATOM   551  C  CD2 . PHE A 1 70  ? -18.007 6.320   7.872   1.00 15.59 ? 70  PHE A CD2 1 
ATOM   552  C  CE1 . PHE A 1 70  ? -16.483 4.036   8.391   1.00 14.86 ? 70  PHE A CE1 1 
ATOM   553  C  CE2 . PHE A 1 70  ? -18.580 5.041   7.726   1.00 12.08 ? 70  PHE A CE2 1 
ATOM   554  C  CZ  . PHE A 1 70  ? -17.784 3.887   7.970   1.00 17.90 ? 70  PHE A CZ  1 
ATOM   555  N  N   . ASP A 1 71  ? -16.235 10.535  6.623   1.00 18.08 ? 71  ASP A N   1 
ATOM   556  C  CA  . ASP A 1 71  ? -16.196 11.981  6.774   1.00 18.79 ? 71  ASP A CA  1 
ATOM   557  C  C   . ASP A 1 71  ? -16.461 12.331  8.201   1.00 18.50 ? 71  ASP A C   1 
ATOM   558  O  O   . ASP A 1 71  ? -17.579 12.087  8.732   1.00 19.54 ? 71  ASP A O   1 
ATOM   559  C  CB  . ASP A 1 71  ? -17.236 12.640  5.907   1.00 19.44 ? 71  ASP A CB  1 
ATOM   560  C  CG  . ASP A 1 71  ? -17.372 14.136  6.206   1.00 23.63 ? 71  ASP A CG  1 
ATOM   561  O  OD1 . ASP A 1 71  ? -16.342 14.796  6.513   1.00 22.17 ? 71  ASP A OD1 1 
ATOM   562  O  OD2 . ASP A 1 71  ? -18.527 14.630  6.184   1.00 27.71 ? 71  ASP A OD2 1 
ATOM   563  N  N   . ASP A 1 72  ? -15.447 12.905  8.830   1.00 17.06 ? 72  ASP A N   1 
ATOM   564  C  CA  . ASP A 1 72  ? -15.492 13.256  10.246  1.00 18.19 ? 72  ASP A CA  1 
ATOM   565  C  C   . ASP A 1 72  ? -15.479 14.770  10.429  1.00 18.76 ? 72  ASP A C   1 
ATOM   566  O  O   . ASP A 1 72  ? -15.160 15.249  11.502  1.00 18.25 ? 72  ASP A O   1 
ATOM   567  C  CB  . ASP A 1 72  ? -14.323 12.617  11.010  1.00 17.38 ? 72  ASP A CB  1 
ATOM   568  C  CG  . ASP A 1 72  ? -12.923 13.149  10.594  1.00 18.40 ? 72  ASP A CG  1 
ATOM   569  O  OD1 . ASP A 1 72  ? -12.738 13.805  9.546   1.00 19.25 ? 72  ASP A OD1 1 
ATOM   570  O  OD2 . ASP A 1 72  ? -11.955 12.846  11.332  1.00 19.05 ? 72  ASP A OD2 1 
ATOM   571  N  N   . SER A 1 73  ? -15.887 15.501  9.387   1.00 19.34 ? 73  SER A N   1 
ATOM   572  C  CA  . SER A 1 73  ? -15.901 16.978  9.411   1.00 21.27 ? 73  SER A CA  1 
ATOM   573  C  C   . SER A 1 73  ? -17.151 17.576  10.078  1.00 23.18 ? 73  SER A C   1 
ATOM   574  O  O   . SER A 1 73  ? -17.225 18.808  10.278  1.00 23.41 ? 73  SER A O   1 
ATOM   575  C  CB  . SER A 1 73  ? -15.674 17.537  7.992   1.00 20.76 ? 73  SER A CB  1 
ATOM   576  O  OG  . SER A 1 73  ? -16.786 17.227  7.138   1.00 21.32 ? 73  SER A OG  1 
ATOM   577  N  N   . GLN A 1 74  ? -18.138 16.723  10.422  1.00 22.72 ? 74  GLN A N   1 
ATOM   578  C  CA  . GLN A 1 74  ? -19.263 17.154  11.257  1.00 25.07 ? 74  GLN A CA  1 
ATOM   579  C  C   . GLN A 1 74  ? -19.649 15.931  12.022  1.00 25.93 ? 74  GLN A C   1 
ATOM   580  O  O   . GLN A 1 74  ? -19.184 14.845  11.682  1.00 26.82 ? 74  GLN A O   1 
ATOM   581  C  CB  . GLN A 1 74  ? -20.481 17.654  10.461  1.00 24.87 ? 74  GLN A CB  1 
ATOM   582  C  CG  . GLN A 1 74  ? -20.189 18.037  9.077   1.00 28.03 ? 74  GLN A CG  1 
ATOM   583  C  CD  . GLN A 1 74  ? -21.433 18.192  8.246   1.00 31.60 ? 74  GLN A CD  1 
ATOM   584  O  OE1 . GLN A 1 74  ? -22.471 18.620  8.742   1.00 34.53 ? 74  GLN A OE1 1 
ATOM   585  N  NE2 . GLN A 1 74  ? -21.336 17.839  6.980   1.00 32.56 ? 74  GLN A NE2 1 
ATOM   586  N  N   . ASP A 1 75  ? -20.481 16.118  13.055  1.00 27.99 ? 75  ASP A N   1 
ATOM   587  C  CA  . ASP A 1 75  ? -20.913 15.050  13.944  1.00 29.66 ? 75  ASP A CA  1 
ATOM   588  C  C   . ASP A 1 75  ? -21.960 14.288  13.199  1.00 30.03 ? 75  ASP A C   1 
ATOM   589  O  O   . ASP A 1 75  ? -23.139 14.669  13.196  1.00 31.02 ? 75  ASP A O   1 
ATOM   590  C  CB  . ASP A 1 75  ? -21.550 15.565  15.248  1.00 31.01 ? 75  ASP A CB  1 
ATOM   591  C  CG  . ASP A 1 75  ? -20.532 16.080  16.238  1.00 33.86 ? 75  ASP A CG  1 
ATOM   592  O  OD1 . ASP A 1 75  ? -19.332 16.058  15.917  1.00 38.94 ? 75  ASP A OD1 1 
ATOM   593  O  OD2 . ASP A 1 75  ? -20.938 16.516  17.336  1.00 37.02 ? 75  ASP A OD2 1 
ATOM   594  N  N   . LYS A 1 76  ? -21.512 13.244  12.528  1.00 29.08 ? 76  LYS A N   1 
ATOM   595  C  CA  . LYS A 1 76  ? -22.383 12.377  11.780  1.00 27.82 ? 76  LYS A CA  1 
ATOM   596  C  C   . LYS A 1 76  ? -22.437 11.055  12.575  1.00 27.94 ? 76  LYS A C   1 
ATOM   597  O  O   . LYS A 1 76  ? -23.411 10.827  13.317  1.00 29.43 ? 76  LYS A O   1 
ATOM   598  C  CB  . LYS A 1 76  ? -21.815 12.232  10.371  1.00 27.70 ? 76  LYS A CB  1 
ATOM   599  C  CG  . LYS A 1 76  ? -22.270 13.364  9.421   1.00 26.34 ? 76  LYS A CG  1 
ATOM   600  C  CD  . LYS A 1 76  ? -21.609 13.186  8.101   1.00 26.01 ? 76  LYS A CD  1 
ATOM   601  C  CE  . LYS A 1 76  ? -22.122 14.186  7.088   1.00 26.64 ? 76  LYS A CE  1 
ATOM   602  N  NZ  . LYS A 1 76  ? -21.510 13.788  5.791   1.00 22.27 ? 76  LYS A NZ  1 
ATOM   603  N  N   . ALA A 1 77  ? -21.349 10.278  12.538  1.00 25.18 ? 77  ALA A N   1 
ATOM   604  C  CA  . ALA A 1 77  ? -21.246 8.960   13.222  1.00 23.10 ? 77  ALA A CA  1 
ATOM   605  C  C   . ALA A 1 77  ? -20.475 9.159   14.497  1.00 21.21 ? 77  ALA A C   1 
ATOM   606  O  O   . ALA A 1 77  ? -19.244 9.436   14.445  1.00 21.40 ? 77  ALA A O   1 
ATOM   607  C  CB  . ALA A 1 77  ? -20.485 8.012   12.378  1.00 22.16 ? 77  ALA A CB  1 
ATOM   608  N  N   . VAL A 1 78  ? -21.163 9.058   15.625  1.00 19.85 ? 78  VAL A N   1 
ATOM   609  C  CA  . VAL A 1 78  ? -20.528 9.349   16.898  1.00 20.31 ? 78  VAL A CA  1 
ATOM   610  C  C   . VAL A 1 78  ? -20.723 8.276   17.944  1.00 18.94 ? 78  VAL A C   1 
ATOM   611  O  O   . VAL A 1 78  ? -21.778 7.602   18.029  1.00 16.17 ? 78  VAL A O   1 
ATOM   612  C  CB  . VAL A 1 78  ? -20.914 10.757  17.500  1.00 21.39 ? 78  VAL A CB  1 
ATOM   613  C  CG1 . VAL A 1 78  ? -20.625 11.928  16.478  1.00 22.31 ? 78  VAL A CG1 1 
ATOM   614  C  CG2 . VAL A 1 78  ? -22.374 10.788  18.030  1.00 22.49 ? 78  VAL A CG2 1 
ATOM   615  N  N   . LEU A 1 79  ? -19.685 8.136   18.748  1.00 17.47 ? 79  LEU A N   1 
ATOM   616  C  CA  . LEU A 1 79  ? -19.746 7.317   19.928  1.00 18.93 ? 79  LEU A CA  1 
ATOM   617  C  C   . LEU A 1 79  ? -19.836 8.219   21.169  1.00 18.27 ? 79  LEU A C   1 
ATOM   618  O  O   . LEU A 1 79  ? -19.132 9.239   21.283  1.00 17.57 ? 79  LEU A O   1 
ATOM   619  C  CB  . LEU A 1 79  ? -18.452 6.509   20.016  1.00 19.09 ? 79  LEU A CB  1 
ATOM   620  C  CG  . LEU A 1 79  ? -18.492 5.301   20.933  1.00 21.09 ? 79  LEU A CG  1 
ATOM   621  C  CD1 . LEU A 1 79  ? -19.531 4.290   20.506  1.00 20.99 ? 79  LEU A CD1 1 
ATOM   622  C  CD2 . LEU A 1 79  ? -17.091 4.664   20.930  1.00 20.57 ? 79  LEU A CD2 1 
ATOM   623  N  N   . LYS A 1 80  ? -20.722 7.874   22.077  1.00 18.74 ? 80  LYS A N   1 
ATOM   624  C  CA  . LYS A 1 80  ? -20.738 8.584   23.344  1.00 20.35 ? 80  LYS A CA  1 
ATOM   625  C  C   . LYS A 1 80  ? -21.291 7.693   24.452  1.00 19.92 ? 80  LYS A C   1 
ATOM   626  O  O   . LYS A 1 80  ? -21.466 6.521   24.208  1.00 18.34 ? 80  LYS A O   1 
ATOM   627  C  CB  . LYS A 1 80  ? -21.447 9.925   23.205  1.00 20.90 ? 80  LYS A CB  1 
ATOM   628  C  CG  . LYS A 1 80  ? -22.884 9.834   22.721  1.00 24.53 ? 80  LYS A CG  1 
ATOM   629  C  CD  . LYS A 1 80  ? -23.440 11.280  22.630  1.00 28.98 ? 80  LYS A CD  1 
ATOM   630  C  CE  . LYS A 1 80  ? -22.906 11.960  21.408  1.00 25.51 ? 80  LYS A CE  1 
ATOM   631  N  NZ  . LYS A 1 80  ? -23.483 13.322  21.229  0.01 26.60 ? 80  LYS A NZ  1 
ATOM   632  N  N   . GLY A 1 81  ? -21.509 8.235   25.656  1.00 20.83 ? 81  GLY A N   1 
ATOM   633  C  CA  . GLY A 1 81  ? -21.983 7.420   26.747  1.00 22.40 ? 81  GLY A CA  1 
ATOM   634  C  C   . GLY A 1 81  ? -20.953 6.325   27.055  1.00 22.34 ? 81  GLY A C   1 
ATOM   635  O  O   . GLY A 1 81  ? -19.777 6.572   26.940  1.00 21.70 ? 81  GLY A O   1 
ATOM   636  N  N   . GLY A 1 82  ? -21.408 5.143   27.456  1.00 22.14 ? 82  GLY A N   1 
ATOM   637  C  CA  . GLY A 1 82  ? -20.505 4.127   27.988  1.00 22.28 ? 82  GLY A CA  1 
ATOM   638  C  C   . GLY A 1 82  ? -19.585 4.737   29.042  1.00 22.01 ? 82  GLY A C   1 
ATOM   639  O  O   . GLY A 1 82  ? -20.078 5.411   29.967  1.00 22.66 ? 82  GLY A O   1 
ATOM   640  N  N   . PRO A 1 83  ? -18.244 4.517   28.928  1.00 20.34 ? 83  PRO A N   1 
ATOM   641  C  CA  . PRO A 1 83  ? -17.378 5.112   29.933  1.00 20.18 ? 83  PRO A CA  1 
ATOM   642  C  C   . PRO A 1 83  ? -16.977 6.545   29.563  1.00 20.92 ? 83  PRO A C   1 
ATOM   643  O  O   . PRO A 1 83  ? -16.225 7.190   30.295  1.00 21.45 ? 83  PRO A O   1 
ATOM   644  C  CB  . PRO A 1 83  ? -16.150 4.194   29.890  1.00 20.50 ? 83  PRO A CB  1 
ATOM   645  C  CG  . PRO A 1 83  ? -16.048 3.843   28.394  1.00 17.90 ? 83  PRO A CG  1 
ATOM   646  C  CD  . PRO A 1 83  ? -17.477 3.701   27.951  1.00 20.07 ? 83  PRO A CD  1 
ATOM   647  N  N   . LEU A 1 84  ? -17.470 7.041   28.438  1.00 21.84 ? 84  LEU A N   1 
ATOM   648  C  CA  . LEU A 1 84  ? -16.884 8.241   27.828  1.00 23.63 ? 84  LEU A CA  1 
ATOM   649  C  C   . LEU A 1 84  ? -17.510 9.471   28.406  1.00 25.55 ? 84  LEU A C   1 
ATOM   650  O  O   . LEU A 1 84  ? -18.683 9.446   28.733  1.00 25.46 ? 84  LEU A O   1 
ATOM   651  C  CB  . LEU A 1 84  ? -17.068 8.277   26.313  1.00 22.37 ? 84  LEU A CB  1 
ATOM   652  C  CG  . LEU A 1 84  ? -16.467 7.064   25.600  1.00 22.10 ? 84  LEU A CG  1 
ATOM   653  C  CD1 . LEU A 1 84  ? -16.835 7.105   24.103  1.00 18.42 ? 84  LEU A CD1 1 
ATOM   654  C  CD2 . LEU A 1 84  ? -14.955 7.013   25.787  1.00 18.07 ? 84  LEU A CD2 1 
ATOM   655  N  N   . ASP A 1 85  ? -16.717 10.551  28.462  1.00 27.03 ? 85  ASP A N   1 
ATOM   656  C  CA  . ASP A 1 85  ? -17.227 11.859  28.858  1.00 29.46 ? 85  ASP A CA  1 
ATOM   657  C  C   . ASP A 1 85  ? -17.553 12.807  27.707  1.00 29.32 ? 85  ASP A C   1 
ATOM   658  O  O   . ASP A 1 85  ? -18.428 13.640  27.848  1.00 32.29 ? 85  ASP A O   1 
ATOM   659  C  CB  . ASP A 1 85  ? -16.363 12.514  29.931  1.00 29.31 ? 85  ASP A CB  1 
ATOM   660  C  CG  . ASP A 1 85  ? -16.680 11.985  31.338  1.00 33.33 ? 85  ASP A CG  1 
ATOM   661  O  OD1 . ASP A 1 85  ? -17.843 11.544  31.602  1.00 36.32 ? 85  ASP A OD1 1 
ATOM   662  O  OD2 . ASP A 1 85  ? -15.768 12.014  32.192  0.01 33.07 ? 85  ASP A OD2 1 
ATOM   663  N  N   . GLY A 1 86  ? -16.950 12.676  26.545  1.00 28.97 ? 86  GLY A N   1 
ATOM   664  C  CA  . GLY A 1 86  ? -17.473 13.491  25.461  1.00 27.52 ? 86  GLY A CA  1 
ATOM   665  C  C   . GLY A 1 86  ? -18.011 12.715  24.259  1.00 27.01 ? 86  GLY A C   1 
ATOM   666  O  O   . GLY A 1 86  ? -18.441 11.557  24.377  1.00 27.34 ? 86  GLY A O   1 
ATOM   667  N  N   . THR A 1 87  ? -18.007 13.396  23.124  1.00 24.47 ? 87  THR A N   1 
ATOM   668  C  CA  . THR A 1 87  ? -18.462 12.920  21.839  1.00 22.26 ? 87  THR A CA  1 
ATOM   669  C  C   . THR A 1 87  ? -17.228 12.638  21.053  1.00 19.89 ? 87  THR A C   1 
ATOM   670  O  O   . THR A 1 87  ? -16.314 13.441  21.019  1.00 18.90 ? 87  THR A O   1 
ATOM   671  C  CB  . THR A 1 87  ? -19.222 14.056  21.110  1.00 23.59 ? 87  THR A CB  1 
ATOM   672  O  OG1 . THR A 1 87  ? -20.394 14.381  21.866  1.00 29.03 ? 87  THR A OG1 1 
ATOM   673  C  CG2 . THR A 1 87  ? -19.640 13.644  19.697  1.00 19.57 ? 87  THR A CG2 1 
ATOM   674  N  N   . TYR A 1 88  ? -17.201 11.461  20.449  1.00 18.84 ? 88  TYR A N   1 
ATOM   675  C  CA  . TYR A 1 88  ? -16.099 11.002  19.650  1.00 17.48 ? 88  TYR A CA  1 
ATOM   676  C  C   . TYR A 1 88  ? -16.638 10.700  18.240  1.00 17.74 ? 88  TYR A C   1 
ATOM   677  O  O   . TYR A 1 88  ? -17.579 9.947   18.100  1.00 20.09 ? 88  TYR A O   1 
ATOM   678  C  CB  . TYR A 1 88  ? -15.487 9.745   20.298  1.00 15.73 ? 88  TYR A CB  1 
ATOM   679  C  CG  . TYR A 1 88  ? -14.740 9.939   21.633  1.00 14.18 ? 88  TYR A CG  1 
ATOM   680  C  CD1 . TYR A 1 88  ? -15.437 10.143  22.804  1.00 10.83 ? 88  TYR A CD1 1 
ATOM   681  C  CD2 . TYR A 1 88  ? -13.320 9.843   21.702  1.00 9.43  ? 88  TYR A CD2 1 
ATOM   682  C  CE1 . TYR A 1 88  ? -14.771 10.342  24.000  1.00 14.32 ? 88  TYR A CE1 1 
ATOM   683  C  CE2 . TYR A 1 88  ? -12.631 10.024  22.907  1.00 7.66  ? 88  TYR A CE2 1 
ATOM   684  C  CZ  . TYR A 1 88  ? -13.365 10.264  24.043  1.00 11.62 ? 88  TYR A CZ  1 
ATOM   685  O  OH  . TYR A 1 88  ? -12.785 10.415  25.254  1.00 15.02 ? 88  TYR A OH  1 
ATOM   686  N  N   . ARG A 1 89  ? -16.078 11.329  17.214  1.00 16.82 ? 89  ARG A N   1 
ATOM   687  C  CA  . ARG A 1 89  ? -16.453 11.073  15.829  1.00 16.40 ? 89  ARG A CA  1 
ATOM   688  C  C   . ARG A 1 89  ? -15.655 9.904   15.233  1.00 14.44 ? 89  ARG A C   1 
ATOM   689  O  O   . ARG A 1 89  ? -14.411 9.874   15.309  1.00 13.39 ? 89  ARG A O   1 
ATOM   690  C  CB  . ARG A 1 89  ? -16.180 12.299  14.941  1.00 16.45 ? 89  ARG A CB  1 
ATOM   691  C  CG  . ARG A 1 89  ? -17.064 13.487  15.158  1.00 17.60 ? 89  ARG A CG  1 
ATOM   692  C  CD  . ARG A 1 89  ? -16.537 14.619  14.311  1.00 22.76 ? 89  ARG A CD  1 
ATOM   693  N  NE  . ARG A 1 89  ? -17.353 15.798  14.534  1.00 25.51 ? 89  ARG A NE  1 
ATOM   694  C  CZ  . ARG A 1 89  ? -17.059 17.008  14.091  1.00 25.97 ? 89  ARG A CZ  1 
ATOM   695  N  NH1 . ARG A 1 89  ? -15.954 17.228  13.405  1.00 27.81 ? 89  ARG A NH1 1 
ATOM   696  N  NH2 . ARG A 1 89  ? -17.896 18.004  14.348  1.00 29.99 ? 89  ARG A NH2 1 
ATOM   697  N  N   . LEU A 1 90  ? -16.389 8.985   14.594  1.00 14.09 ? 90  LEU A N   1 
ATOM   698  C  CA  . LEU A 1 90  ? -15.814 7.939   13.763  1.00 13.34 ? 90  LEU A CA  1 
ATOM   699  C  C   . LEU A 1 90  ? -14.956 8.517   12.632  1.00 13.05 ? 90  LEU A C   1 
ATOM   700  O  O   . LEU A 1 90  ? -15.397 9.306   11.785  1.00 13.47 ? 90  LEU A O   1 
ATOM   701  C  CB  . LEU A 1 90  ? -16.927 7.053   13.150  1.00 12.41 ? 90  LEU A CB  1 
ATOM   702  C  CG  . LEU A 1 90  ? -16.440 5.792   12.407  1.00 14.18 ? 90  LEU A CG  1 
ATOM   703  C  CD1 . LEU A 1 90  ? -15.781 4.724   13.289  1.00 14.72 ? 90  LEU A CD1 1 
ATOM   704  C  CD2 . LEU A 1 90  ? -17.670 5.167   11.678  1.00 13.50 ? 90  LEU A CD2 1 
ATOM   705  N  N   . ILE A 1 91  ? -13.716 8.082   12.594  1.00 13.23 ? 91  ILE A N   1 
ATOM   706  C  CA  . ILE A 1 91  ? -12.830 8.486   11.541  1.00 13.22 ? 91  ILE A CA  1 
ATOM   707  C  C   . ILE A 1 91  ? -12.533 7.336   10.553  1.00 13.15 ? 91  ILE A C   1 
ATOM   708  O  O   . ILE A 1 91  ? -12.523 7.548   9.347   1.00 12.78 ? 91  ILE A O   1 
ATOM   709  C  CB  . ILE A 1 91  ? -11.509 9.089   12.053  1.00 13.28 ? 91  ILE A CB  1 
ATOM   710  C  CG1 . ILE A 1 91  ? -10.586 9.419   10.836  1.00 13.00 ? 91  ILE A CG1 1 
ATOM   711  C  CG2 . ILE A 1 91  ? -10.804 8.163   13.047  1.00 14.06 ? 91  ILE A CG2 1 
ATOM   712  C  CD1 . ILE A 1 91  ? -9.485  10.377  11.182  1.00 12.85 ? 91  ILE A CD1 1 
ATOM   713  N  N   . GLN A 1 92  ? -12.293 6.135   11.092  1.00 13.54 ? 92  GLN A N   1 
ATOM   714  C  CA  . GLN A 1 92  ? -12.018 4.967   10.259  1.00 12.60 ? 92  GLN A CA  1 
ATOM   715  C  C   . GLN A 1 92  ? -12.370 3.718   11.005  1.00 12.33 ? 92  GLN A C   1 
ATOM   716  O  O   . GLN A 1 92  ? -12.380 3.742   12.238  1.00 11.93 ? 92  GLN A O   1 
ATOM   717  C  CB  . GLN A 1 92  ? -10.542 4.942   9.751   1.00 13.71 ? 92  GLN A CB  1 
ATOM   718  C  CG  . GLN A 1 92  ? -9.449  5.048   10.888  1.00 12.84 ? 92  GLN A CG  1 
ATOM   719  C  CD  . GLN A 1 92  ? -8.753  3.734   11.118  1.00 14.55 ? 92  GLN A CD  1 
ATOM   720  O  OE1 . GLN A 1 92  ? -9.387  2.662   11.175  1.00 11.43 ? 92  GLN A OE1 1 
ATOM   721  N  NE2 . GLN A 1 92  ? -7.438  3.805   11.380  1.00 15.55 ? 92  GLN A NE2 1 
ATOM   722  N  N   . PHE A 1 93  ? -12.688 2.639   10.275  1.00 11.88 ? 93  PHE A N   1 
ATOM   723  C  CA  . PHE A 1 93  ? -12.499 1.289   10.810  1.00 12.25 ? 93  PHE A CA  1 
ATOM   724  C  C   . PHE A 1 93  ? -11.477 0.381   10.059  1.00 11.70 ? 93  PHE A C   1 
ATOM   725  O  O   . PHE A 1 93  ? -11.212 0.545   8.907   1.00 11.58 ? 93  PHE A O   1 
ATOM   726  C  CB  . PHE A 1 93  ? -13.822 0.566   11.137  1.00 10.87 ? 93  PHE A CB  1 
ATOM   727  C  CG  . PHE A 1 93  ? -14.572 0.088   9.935   1.00 14.60 ? 93  PHE A CG  1 
ATOM   728  C  CD1 . PHE A 1 93  ? -14.151 -1.060  9.220   1.00 16.61 ? 93  PHE A CD1 1 
ATOM   729  C  CD2 . PHE A 1 93  ? -15.707 0.790   9.484   1.00 14.42 ? 93  PHE A CD2 1 
ATOM   730  C  CE1 . PHE A 1 93  ? -14.852 -1.497  8.054   1.00 13.43 ? 93  PHE A CE1 1 
ATOM   731  C  CE2 . PHE A 1 93  ? -16.422 0.356   8.334   1.00 13.51 ? 93  PHE A CE2 1 
ATOM   732  C  CZ  . PHE A 1 93  ? -15.993 -0.806  7.632   1.00 13.67 ? 93  PHE A CZ  1 
ATOM   733  N  N   . HIS A 1 94  ? -10.893 -0.580  10.759  1.00 11.03 ? 94  HIS A N   1 
ATOM   734  C  CA  . HIS A 1 94  ? -10.016 -1.557  10.138  1.00 9.83  ? 94  HIS A CA  1 
ATOM   735  C  C   . HIS A 1 94  ? -10.085 -2.820  10.999  1.00 10.03 ? 94  HIS A C   1 
ATOM   736  O  O   . HIS A 1 94  ? -10.794 -2.885  12.052  1.00 11.03 ? 94  HIS A O   1 
ATOM   737  C  CB  . HIS A 1 94  ? -8.564  -1.004  10.103  1.00 9.94  ? 94  HIS A CB  1 
ATOM   738  C  CG  . HIS A 1 94  ? -8.041  -0.726  11.498  1.00 8.76  ? 94  HIS A CG  1 
ATOM   739  N  ND1 . HIS A 1 94  ? -8.319  0.441   12.183  1.00 9.11  ? 94  HIS A ND1 1 
ATOM   740  C  CD2 . HIS A 1 94  ? -7.385  -1.529  12.370  1.00 10.39 ? 94  HIS A CD2 1 
ATOM   741  C  CE1 . HIS A 1 94  ? -7.812  0.362   13.408  1.00 7.58  ? 94  HIS A CE1 1 
ATOM   742  N  NE2 . HIS A 1 94  ? -7.233  -0.828  13.538  1.00 6.86  ? 94  HIS A NE2 1 
ATOM   743  N  N   . PHE A 1 95  ? -9.377  -3.836  10.530  1.00 9.66  ? 95  PHE A N   1 
ATOM   744  C  CA  . PHE A 1 95  ? -9.377  -5.169  11.172  1.00 10.04 ? 95  PHE A CA  1 
ATOM   745  C  C   . PHE A 1 95  ? -7.957  -5.613  11.360  1.00 8.84  ? 95  PHE A C   1 
ATOM   746  O  O   . PHE A 1 95  ? -6.999  -5.073  10.735  1.00 8.96  ? 95  PHE A O   1 
ATOM   747  C  CB  . PHE A 1 95  ? -10.155 -6.256  10.330  1.00 8.26  ? 95  PHE A CB  1 
ATOM   748  C  CG  . PHE A 1 95  ? -11.650 -5.931  10.027  1.00 11.41 ? 95  PHE A CG  1 
ATOM   749  C  CD1 . PHE A 1 95  ? -11.982 -5.092  8.958   1.00 14.01 ? 95  PHE A CD1 1 
ATOM   750  C  CD2 . PHE A 1 95  ? -12.687 -6.574  10.699  1.00 10.54 ? 95  PHE A CD2 1 
ATOM   751  C  CE1 . PHE A 1 95  ? -13.294 -4.847  8.582   1.00 11.87 ? 95  PHE A CE1 1 
ATOM   752  C  CE2 . PHE A 1 95  ? -14.027 -6.338  10.356  1.00 13.19 ? 95  PHE A CE2 1 
ATOM   753  C  CZ  . PHE A 1 95  ? -14.335 -5.457  9.264   1.00 11.81 ? 95  PHE A CZ  1 
ATOM   754  N  N   . HIS A 1 96  ? -7.807  -6.540  12.302  1.00 8.66  ? 96  HIS A N   1 
ATOM   755  C  CA  . HIS A 1 96  ? -6.581  -7.387  12.434  1.00 9.24  ? 96  HIS A CA  1 
ATOM   756  C  C   . HIS A 1 96  ? -7.053  -8.820  12.319  1.00 10.44 ? 96  HIS A C   1 
ATOM   757  O  O   . HIS A 1 96  ? -8.117  -9.130  12.819  1.00 12.18 ? 96  HIS A O   1 
ATOM   758  C  CB  . HIS A 1 96  ? -5.922  -7.175  13.821  1.00 9.97  ? 96  HIS A CB  1 
ATOM   759  C  CG  . HIS A 1 96  ? -5.663  -5.738  14.121  1.00 10.00 ? 96  HIS A CG  1 
ATOM   760  N  ND1 . HIS A 1 96  ? -4.468  -5.136  13.816  1.00 9.42  ? 96  HIS A ND1 1 
ATOM   761  C  CD2 . HIS A 1 96  ? -6.498  -4.746  14.514  1.00 10.56 ? 96  HIS A CD2 1 
ATOM   762  C  CE1 . HIS A 1 96  ? -4.535  -3.852  14.115  1.00 11.75 ? 96  HIS A CE1 1 
ATOM   763  N  NE2 . HIS A 1 96  ? -5.755  -3.585  14.545  1.00 12.73 ? 96  HIS A NE2 1 
ATOM   764  N  N   . TRP A 1 97  ? -6.276  -9.692  11.666  1.00 11.19 ? 97  TRP A N   1 
ATOM   765  C  CA  . TRP A 1 97  ? -6.708  -11.083 11.492  1.00 11.05 ? 97  TRP A CA  1 
ATOM   766  C  C   . TRP A 1 97  ? -5.546  -12.004 11.358  1.00 11.53 ? 97  TRP A C   1 
ATOM   767  O  O   . TRP A 1 97  ? -4.397  -11.551 11.159  1.00 12.82 ? 97  TRP A O   1 
ATOM   768  C  CB  . TRP A 1 97  ? -7.618  -11.246 10.265  1.00 11.06 ? 97  TRP A CB  1 
ATOM   769  C  CG  . TRP A 1 97  ? -6.916  -10.843 8.973   1.00 12.16 ? 97  TRP A CG  1 
ATOM   770  C  CD1 . TRP A 1 97  ? -6.223  -11.661 8.091   1.00 12.53 ? 97  TRP A CD1 1 
ATOM   771  C  CD2 . TRP A 1 97  ? -6.882  -9.543  8.434   1.00 13.41 ? 97  TRP A CD2 1 
ATOM   772  N  NE1 . TRP A 1 97  ? -5.735  -10.901 7.028   1.00 14.75 ? 97  TRP A NE1 1 
ATOM   773  C  CE2 . TRP A 1 97  ? -6.141  -9.599  7.219   1.00 15.16 ? 97  TRP A CE2 1 
ATOM   774  C  CE3 . TRP A 1 97  ? -7.402  -8.298  8.856   1.00 12.93 ? 97  TRP A CE3 1 
ATOM   775  C  CZ2 . TRP A 1 97  ? -5.913  -8.461  6.441   1.00 12.48 ? 97  TRP A CZ2 1 
ATOM   776  C  CZ3 . TRP A 1 97  ? -7.156  -7.165  8.076   1.00 14.40 ? 97  TRP A CZ3 1 
ATOM   777  C  CH2 . TRP A 1 97  ? -6.433  -7.255  6.870   1.00 11.26 ? 97  TRP A CH2 1 
ATOM   778  N  N   . GLY A 1 98  ? -5.852  -13.306 11.374  1.00 11.08 ? 98  GLY A N   1 
ATOM   779  C  CA  . GLY A 1 98  ? -4.847  -14.333 11.452  1.00 11.64 ? 98  GLY A CA  1 
ATOM   780  C  C   . GLY A 1 98  ? -4.530  -14.996 10.110  1.00 12.56 ? 98  GLY A C   1 
ATOM   781  O  O   . GLY A 1 98  ? -5.148  -14.715 9.102   1.00 12.07 ? 98  GLY A O   1 
ATOM   782  N  N   . SER A 1 99  ? -3.518  -15.856 10.121  1.00 13.01 ? 99  SER A N   1 
ATOM   783  C  CA  . SER A 1 99  ? -3.190  -16.720 8.972   1.00 14.15 ? 99  SER A CA  1 
ATOM   784  C  C   . SER A 1 99  ? -4.117  -17.934 9.054   1.00 15.92 ? 99  SER A C   1 
ATOM   785  O  O   . SER A 1 99  ? -4.369  -18.587 8.057   1.00 16.22 ? 99  SER A O   1 
ATOM   786  C  CB  . SER A 1 99  ? -1.695  -17.098 9.036   1.00 13.38 ? 99  SER A CB  1 
ATOM   787  O  OG  . SER A 1 99  ? -1.352  -17.578 10.374  1.00 14.50 ? 99  SER A OG  1 
ATOM   788  N  N   . LEU A 1 100 ? -4.700  -18.168 10.251  1.00 16.98 ? 100 LEU A N   1 
ATOM   789  C  CA  . LEU A 1 100 ? -5.551  -19.317 10.552  1.00 18.32 ? 100 LEU A CA  1 
ATOM   790  C  C   . LEU A 1 100 ? -6.706  -18.848 11.416  1.00 18.24 ? 100 LEU A C   1 
ATOM   791  O  O   . LEU A 1 100 ? -6.602  -17.784 12.036  1.00 16.11 ? 100 LEU A O   1 
ATOM   792  C  CB  . LEU A 1 100 ? -4.775  -20.318 11.410  1.00 19.07 ? 100 LEU A CB  1 
ATOM   793  C  CG  . LEU A 1 100 ? -3.433  -20.787 10.908  1.00 21.64 ? 100 LEU A CG  1 
ATOM   794  C  CD1 . LEU A 1 100 ? -2.418  -20.952 12.013  1.00 27.68 ? 100 LEU A CD1 1 
ATOM   795  C  CD2 . LEU A 1 100 ? -3.649  -22.075 10.162  1.00 27.18 ? 100 LEU A CD2 1 
ATOM   796  N  N   . ASP A 1 101 ? -7.807  -19.614 11.467  1.00 17.15 ? 101 ASP A N   1 
ATOM   797  C  CA  . ASP A 1 101 ? -8.999  -19.079 12.192  1.00 16.64 ? 101 ASP A CA  1 
ATOM   798  C  C   . ASP A 1 101 ? -8.741  -19.106 13.689  1.00 16.21 ? 101 ASP A C   1 
ATOM   799  O  O   . ASP A 1 101 ? -9.442  -18.437 14.411  1.00 16.70 ? 101 ASP A O   1 
ATOM   800  C  CB  . ASP A 1 101 ? -10.278 -19.878 11.977  1.00 17.09 ? 101 ASP A CB  1 
ATOM   801  C  CG  . ASP A 1 101 ? -10.673 -19.991 10.560  1.00 20.22 ? 101 ASP A CG  1 
ATOM   802  O  OD1 . ASP A 1 101 ? -10.374 -19.104 9.764   1.00 18.33 ? 101 ASP A OD1 1 
ATOM   803  O  OD2 . ASP A 1 101 ? -11.319 -21.005 10.267  1.00 23.93 ? 101 ASP A OD2 1 
ATOM   804  N  N   . GLY A 1 102 ? -7.773  -19.922 14.152  1.00 15.12 ? 102 GLY A N   1 
ATOM   805  C  CA  . GLY A 1 102 ? -7.402  -19.964 15.553  1.00 14.86 ? 102 GLY A CA  1 
ATOM   806  C  C   . GLY A 1 102 ? -6.677  -18.727 16.136  1.00 12.96 ? 102 GLY A C   1 
ATOM   807  O  O   . GLY A 1 102 ? -6.379  -18.683 17.300  1.00 12.49 ? 102 GLY A O   1 
ATOM   808  N  N   . GLN A 1 103 ? -6.419  -17.714 15.341  1.00 12.97 ? 103 GLN A N   1 
ATOM   809  C  CA  . GLN A 1 103 ? -5.730  -16.523 15.858  1.00 14.15 ? 103 GLN A CA  1 
ATOM   810  C  C   . GLN A 1 103 ? -6.045  -15.357 15.012  1.00 14.60 ? 103 GLN A C   1 
ATOM   811  O  O   . GLN A 1 103 ? -6.693  -15.515 13.972  1.00 16.85 ? 103 GLN A O   1 
ATOM   812  C  CB  . GLN A 1 103 ? -4.202  -16.719 15.907  1.00 12.81 ? 103 GLN A CB  1 
ATOM   813  C  CG  . GLN A 1 103 ? -3.543  -16.825 14.548  1.00 15.52 ? 103 GLN A CG  1 
ATOM   814  C  CD  . GLN A 1 103 ? -2.161  -17.465 14.673  1.00 23.72 ? 103 GLN A CD  1 
ATOM   815  O  OE1 . GLN A 1 103 ? -1.913  -18.226 15.606  1.00 25.39 ? 103 GLN A OE1 1 
ATOM   816  N  NE2 . GLN A 1 103 ? -1.273  -17.166 13.752  1.00 18.65 ? 103 GLN A NE2 1 
ATOM   817  N  N   . GLY A 1 104 ? -5.592  -14.182 15.430  1.00 14.29 ? 104 GLY A N   1 
ATOM   818  C  CA  . GLY A 1 104 ? -5.915  -12.964 14.663  1.00 12.54 ? 104 GLY A CA  1 
ATOM   819  C  C   . GLY A 1 104 ? -6.383  -11.807 15.523  1.00 13.20 ? 104 GLY A C   1 
ATOM   820  O  O   . GLY A 1 104 ? -6.061  -10.652 15.235  1.00 13.49 ? 104 GLY A O   1 
ATOM   821  N  N   . SER A 1 105 ? -7.154  -12.076 16.583  1.00 12.00 ? 105 SER A N   1 
ATOM   822  C  CA  . SER A 1 105 ? -7.548  -10.934 17.448  1.00 11.81 ? 105 SER A CA  1 
ATOM   823  C  C   . SER A 1 105 ? -6.352  -10.324 18.234  1.00 10.30 ? 105 SER A C   1 
ATOM   824  O  O   . SER A 1 105 ? -5.360  -10.986 18.535  1.00 10.66 ? 105 SER A O   1 
ATOM   825  C  CB  . SER A 1 105 ? -8.634  -11.315 18.431  1.00 9.33  ? 105 SER A CB  1 
ATOM   826  O  OG  . SER A 1 105 ? -8.110  -12.129 19.445  1.00 13.90 ? 105 SER A OG  1 
ATOM   827  N  N   . GLU A 1 106 ? -6.468  -9.053  18.586  1.00 11.14 ? 106 GLU A N   1 
ATOM   828  C  CA  . GLU A 1 106 ? -5.397  -8.376  19.394  1.00 10.28 ? 106 GLU A CA  1 
ATOM   829  C  C   . GLU A 1 106 ? -5.733  -8.546  20.898  1.00 10.18 ? 106 GLU A C   1 
ATOM   830  O  O   . GLU A 1 106 ? -4.949  -9.134  21.689  1.00 11.77 ? 106 GLU A O   1 
ATOM   831  C  CB  . GLU A 1 106 ? -5.335  -6.895  18.985  1.00 8.80  ? 106 GLU A CB  1 
ATOM   832  C  CG  . GLU A 1 106 ? -4.964  -6.737  17.471  1.00 10.59 ? 106 GLU A CG  1 
ATOM   833  C  CD  . GLU A 1 106 ? -4.189  -5.489  17.238  1.00 10.42 ? 106 GLU A CD  1 
ATOM   834  O  OE1 . GLU A 1 106 ? -4.805  -4.420  17.443  1.00 9.48  ? 106 GLU A OE1 1 
ATOM   835  O  OE2 . GLU A 1 106 ? -2.986  -5.584  16.848  1.00 12.87 ? 106 GLU A OE2 1 
ATOM   836  N  N   . HIS A 1 107 ? -6.936  -8.119  21.288  1.00 10.84 ? 107 HIS A N   1 
ATOM   837  C  CA  . HIS A 1 107 ? -7.434  -8.419  22.607  1.00 11.17 ? 107 HIS A CA  1 
ATOM   838  C  C   . HIS A 1 107 ? -7.752  -9.897  22.640  1.00 11.47 ? 107 HIS A C   1 
ATOM   839  O  O   . HIS A 1 107 ? -8.043  -10.519 21.586  1.00 10.24 ? 107 HIS A O   1 
ATOM   840  C  CB  . HIS A 1 107 ? -8.689  -7.591  22.946  1.00 10.96 ? 107 HIS A CB  1 
ATOM   841  C  CG  . HIS A 1 107 ? -8.385  -6.123  23.122  1.00 10.78 ? 107 HIS A CG  1 
ATOM   842  N  ND1 . HIS A 1 107 ? -8.412  -5.231  22.076  1.00 11.53 ? 107 HIS A ND1 1 
ATOM   843  C  CD2 . HIS A 1 107 ? -7.944  -5.428  24.197  1.00 5.99  ? 107 HIS A CD2 1 
ATOM   844  C  CE1 . HIS A 1 107 ? -8.003  -4.047  22.494  1.00 9.60  ? 107 HIS A CE1 1 
ATOM   845  N  NE2 . HIS A 1 107 ? -7.745  -4.132  23.784  1.00 9.47  ? 107 HIS A NE2 1 
ATOM   846  N  N   . THR A 1 108 ? -7.608  -10.477 23.821  1.00 10.60 ? 108 THR A N   1 
ATOM   847  C  CA  . THR A 1 108 ? -7.996  -11.892 24.051  1.00 11.79 ? 108 THR A CA  1 
ATOM   848  C  C   . THR A 1 108 ? -8.933  -11.900 25.275  1.00 13.04 ? 108 THR A C   1 
ATOM   849  O  O   . THR A 1 108 ? -8.915  -10.953 26.076  1.00 12.25 ? 108 THR A O   1 
ATOM   850  C  CB  . THR A 1 108 ? -6.753  -12.841 24.266  1.00 10.32 ? 108 THR A CB  1 
ATOM   851  O  OG1 . THR A 1 108 ? -5.890  -12.312 25.282  1.00 12.08 ? 108 THR A OG1 1 
ATOM   852  C  CG2 . THR A 1 108 ? -5.934  -13.016 22.921  1.00 7.53  ? 108 THR A CG2 1 
ATOM   853  N  N   . VAL A 1 109 ? -9.730  -12.955 25.418  1.00 14.00 ? 109 VAL A N   1 
ATOM   854  C  CA  . VAL A 1 109 ? -10.766 -13.090 26.482  1.00 14.40 ? 109 VAL A CA  1 
ATOM   855  C  C   . VAL A 1 109 ? -10.452 -14.369 27.241  1.00 13.72 ? 109 VAL A C   1 
ATOM   856  O  O   . VAL A 1 109 ? -10.612 -15.439 26.724  1.00 15.18 ? 109 VAL A O   1 
ATOM   857  C  CB  . VAL A 1 109 ? -12.199 -13.106 25.898  1.00 14.91 ? 109 VAL A CB  1 
ATOM   858  C  CG1 . VAL A 1 109 ? -13.302 -13.269 27.034  1.00 16.31 ? 109 VAL A CG1 1 
ATOM   859  C  CG2 . VAL A 1 109 ? -12.453 -11.791 25.086  1.00 12.95 ? 109 VAL A CG2 1 
ATOM   860  N  N   . ASP A 1 110 ? -9.912  -14.252 28.433  1.00 12.58 ? 110 ASP A N   1 
ATOM   861  C  CA  . ASP A 1 110 ? -9.395  -15.428 29.133  1.00 15.10 ? 110 ASP A CA  1 
ATOM   862  C  C   . ASP A 1 110 ? -8.422  -16.226 28.276  1.00 15.54 ? 110 ASP A C   1 
ATOM   863  O  O   . ASP A 1 110 ? -8.540  -17.477 28.223  1.00 13.97 ? 110 ASP A O   1 
ATOM   864  C  CB  . ASP A 1 110 ? -10.584 -16.306 29.650  1.00 15.79 ? 110 ASP A CB  1 
ATOM   865  C  CG  . ASP A 1 110 ? -11.427 -15.567 30.644  1.00 16.57 ? 110 ASP A CG  1 
ATOM   866  O  OD1 . ASP A 1 110 ? -10.808 -14.774 31.360  1.00 15.31 ? 110 ASP A OD1 1 
ATOM   867  O  OD2 . ASP A 1 110 ? -12.680 -15.766 30.675  1.00 17.78 ? 110 ASP A OD2 1 
ATOM   868  N  N   A LYS A 1 111 ? -7.461  -15.518 27.644  0.50 14.68 ? 111 LYS A N   1 
ATOM   869  N  N   B LYS A 1 111 ? -7.523  -15.492 27.596  0.50 14.95 ? 111 LYS A N   1 
ATOM   870  C  CA  A LYS A 1 111 ? -6.433  -16.037 26.682  0.50 15.03 ? 111 LYS A CA  1 
ATOM   871  C  CA  B LYS A 1 111 ? -6.458  -16.025 26.731  0.50 15.56 ? 111 LYS A CA  1 
ATOM   872  C  C   A LYS A 1 111 ? -6.968  -16.543 25.355  0.50 15.05 ? 111 LYS A C   1 
ATOM   873  C  C   B LYS A 1 111 ? -6.968  -16.578 25.400  0.50 15.37 ? 111 LYS A C   1 
ATOM   874  O  O   A LYS A 1 111 ? -6.199  -16.979 24.514  0.50 14.34 ? 111 LYS A O   1 
ATOM   875  O  O   B LYS A 1 111 ? -6.184  -17.055 24.595  0.50 14.61 ? 111 LYS A O   1 
ATOM   876  C  CB  A LYS A 1 111 ? -5.498  -17.117 27.275  0.50 15.69 ? 111 LYS A CB  1 
ATOM   877  C  CB  B LYS A 1 111 ? -5.601  -17.070 27.476  0.50 16.56 ? 111 LYS A CB  1 
ATOM   878  C  CG  A LYS A 1 111 ? -4.624  -16.688 28.439  0.50 14.46 ? 111 LYS A CG  1 
ATOM   879  C  CG  B LYS A 1 111 ? -5.219  -16.684 28.919  0.50 16.21 ? 111 LYS A CG  1 
ATOM   880  C  CD  A LYS A 1 111 ? -3.703  -15.570 28.115  0.50 13.82 ? 111 LYS A CD  1 
ATOM   881  C  CD  B LYS A 1 111 ? -3.907  -15.900 28.954  0.50 16.37 ? 111 LYS A CD  1 
ATOM   882  C  CE  A LYS A 1 111 ? -2.951  -15.121 29.394  0.50 14.39 ? 111 LYS A CE  1 
ATOM   883  C  CE  B LYS A 1 111 ? -3.047  -16.283 30.182  0.50 17.43 ? 111 LYS A CE  1 
ATOM   884  N  NZ  A LYS A 1 111 ? -1.573  -15.722 29.361  0.50 15.68 ? 111 LYS A NZ  1 
ATOM   885  N  NZ  B LYS A 1 111 ? -3.057  -15.337 31.344  0.50 18.47 ? 111 LYS A NZ  1 
ATOM   886  N  N   . LYS A 1 112 ? -8.280  -16.506 25.176  1.00 15.23 ? 112 LYS A N   1 
ATOM   887  C  CA  . LYS A 1 112 ? -8.841  -16.926 23.941  1.00 16.11 ? 112 LYS A CA  1 
ATOM   888  C  C   . LYS A 1 112 ? -8.599  -15.897 22.805  1.00 16.21 ? 112 LYS A C   1 
ATOM   889  O  O   . LYS A 1 112 ? -8.992  -14.679 22.904  1.00 16.69 ? 112 LYS A O   1 
ATOM   890  C  CB  . LYS A 1 112 ? -10.333 -17.235 24.080  1.00 16.19 ? 112 LYS A CB  1 
ATOM   891  C  CG  . LYS A 1 112 ? -10.956 -17.628 22.741  1.00 15.15 ? 112 LYS A CG  1 
ATOM   892  C  CD  . LYS A 1 112 ? -12.494 -17.510 22.674  1.00 19.73 ? 112 LYS A CD  1 
ATOM   893  C  CE  . LYS A 1 112 ? -12.961 -18.137 21.273  1.00 19.93 ? 112 LYS A CE  1 
ATOM   894  N  NZ  . LYS A 1 112 ? -14.422 -18.452 21.296  1.00 25.01 ? 112 LYS A NZ  1 
ATOM   895  N  N   . LYS A 1 113 ? -7.964  -16.386 21.746  1.00 14.87 ? 113 LYS A N   1 
ATOM   896  C  CA  . LYS A 1 113 ? -7.885  -15.641 20.451  1.00 14.50 ? 113 LYS A CA  1 
ATOM   897  C  C   . LYS A 1 113 ? -9.060  -15.874 19.464  1.00 13.81 ? 113 LYS A C   1 
ATOM   898  O  O   . LYS A 1 113 ? -9.447  -17.035 19.162  1.00 11.65 ? 113 LYS A O   1 
ATOM   899  C  CB  . LYS A 1 113 ? -6.581  -15.914 19.704  1.00 14.33 ? 113 LYS A CB  1 
ATOM   900  C  CG  . LYS A 1 113 ? -5.344  -15.696 20.499  1.00 16.19 ? 113 LYS A CG  1 
ATOM   901  C  CD  . LYS A 1 113 ? -4.125  -16.239 19.777  1.00 14.11 ? 113 LYS A CD  1 
ATOM   902  C  CE  . LYS A 1 113 ? -2.768  -15.611 20.314  1.00 16.57 ? 113 LYS A CE  1 
ATOM   903  N  NZ  . LYS A 1 113 ? -2.145  -16.436 21.365  1.00 19.56 ? 113 LYS A NZ  1 
ATOM   904  N  N   . TYR A 1 114 ? -9.580  -14.755 18.912  1.00 12.27 ? 114 TYR A N   1 
ATOM   905  C  CA  . TYR A 1 114 ? -10.638 -14.812 17.957  1.00 12.09 ? 114 TYR A CA  1 
ATOM   906  C  C   . TYR A 1 114 ? -10.018 -14.754 16.582  1.00 10.94 ? 114 TYR A C   1 
ATOM   907  O  O   . TYR A 1 114 ? -8.882  -14.436 16.475  1.00 12.35 ? 114 TYR A O   1 
ATOM   908  C  CB  . TYR A 1 114 ? -11.682 -13.715 18.185  1.00 11.94 ? 114 TYR A CB  1 
ATOM   909  C  CG  . TYR A 1 114 ? -12.645 -13.981 19.308  1.00 15.48 ? 114 TYR A CG  1 
ATOM   910  C  CD1 . TYR A 1 114 ? -12.354 -13.604 20.629  1.00 14.85 ? 114 TYR A CD1 1 
ATOM   911  C  CD2 . TYR A 1 114 ? -13.867 -14.577 19.052  1.00 18.08 ? 114 TYR A CD2 1 
ATOM   912  C  CE1 . TYR A 1 114 ? -13.240 -13.815 21.637  1.00 16.42 ? 114 TYR A CE1 1 
ATOM   913  C  CE2 . TYR A 1 114 ? -14.775 -14.741 20.048  1.00 17.79 ? 114 TYR A CE2 1 
ATOM   914  C  CZ  . TYR A 1 114 ? -14.444 -14.407 21.343  1.00 18.45 ? 114 TYR A CZ  1 
ATOM   915  O  OH  . TYR A 1 114 ? -15.375 -14.651 22.331  1.00 18.23 ? 114 TYR A OH  1 
ATOM   916  N  N   . ALA A 1 115 ? -10.755 -15.135 15.541  1.00 12.57 ? 115 ALA A N   1 
ATOM   917  C  CA  . ALA A 1 115 ? -10.230 -15.174 14.181  1.00 12.52 ? 115 ALA A CA  1 
ATOM   918  C  C   . ALA A 1 115 ? -9.769  -13.783 13.734  1.00 12.59 ? 115 ALA A C   1 
ATOM   919  O  O   . ALA A 1 115 ? -8.921  -13.646 12.870  1.00 14.23 ? 115 ALA A O   1 
ATOM   920  C  CB  . ALA A 1 115 ? -11.268 -15.731 13.247  1.00 12.58 ? 115 ALA A CB  1 
ATOM   921  N  N   . ALA A 1 116 ? -10.388 -12.740 14.312  1.00 12.89 ? 116 ALA A N   1 
ATOM   922  C  CA  . ALA A 1 116 ? -10.176 -11.352 13.903  1.00 11.80 ? 116 ALA A CA  1 
ATOM   923  C  C   . ALA A 1 116 ? -10.725 -10.384 14.898  1.00 10.25 ? 116 ALA A C   1 
ATOM   924  O  O   . ALA A 1 116 ? -11.455 -10.756 15.832  1.00 10.86 ? 116 ALA A O   1 
ATOM   925  C  CB  . ALA A 1 116 ? -10.801 -11.041 12.445  1.00 9.92  ? 116 ALA A CB  1 
ATOM   926  N  N   . GLU A 1 117 ? -10.299 -9.136  14.728  1.00 11.47 ? 117 GLU A N   1 
ATOM   927  C  CA  . GLU A 1 117 ? -10.748 -8.032  15.547  1.00 10.40 ? 117 GLU A CA  1 
ATOM   928  C  C   . GLU A 1 117 ? -11.007 -6.778  14.727  1.00 11.20 ? 117 GLU A C   1 
ATOM   929  O  O   . GLU A 1 117 ? -10.140 -6.343  13.993  1.00 12.31 ? 117 GLU A O   1 
ATOM   930  C  CB  . GLU A 1 117 ? -9.805  -7.781  16.714  1.00 10.95 ? 117 GLU A CB  1 
ATOM   931  C  CG  . GLU A 1 117 ? -10.404 -6.865  17.764  1.00 10.69 ? 117 GLU A CG  1 
ATOM   932  C  CD  . GLU A 1 117 ? -9.547  -6.806  18.990  1.00 10.27 ? 117 GLU A CD  1 
ATOM   933  O  OE1 . GLU A 1 117 ? -8.933  -7.866  19.264  1.00 10.78 ? 117 GLU A OE1 1 
ATOM   934  O  OE2 . GLU A 1 117 ? -9.497  -5.705  19.654  1.00 10.84 ? 117 GLU A OE2 1 
ATOM   935  N  N   . LEU A 1 118 ? -12.247 -6.268  14.825  1.00 9.94  ? 118 LEU A N   1 
ATOM   936  C  CA  . LEU A 1 118 ? -12.668 -4.959  14.247  1.00 9.66  ? 118 LEU A CA  1 
ATOM   937  C  C   . LEU A 1 118 ? -12.438 -3.815  15.225  1.00 9.70  ? 118 LEU A C   1 
ATOM   938  O  O   . LEU A 1 118 ? -12.871 -3.889  16.346  1.00 9.42  ? 118 LEU A O   1 
ATOM   939  C  CB  . LEU A 1 118 ? -14.136 -5.004  13.794  1.00 8.50  ? 118 LEU A CB  1 
ATOM   940  C  CG  . LEU A 1 118 ? -15.013 -3.782  13.453  1.00 9.16  ? 118 LEU A CG  1 
ATOM   941  C  CD1 . LEU A 1 118 ? -14.470 -3.076  12.231  1.00 7.78  ? 118 LEU A CD1 1 
ATOM   942  C  CD2 . LEU A 1 118 ? -16.464 -4.281  13.197  1.00 8.86  ? 118 LEU A CD2 1 
ATOM   943  N  N   . HIS A 1 119 ? -11.779 -2.752  14.740  1.00 10.52 ? 119 HIS A N   1 
ATOM   944  C  CA  . HIS A 1 119 ? -11.540 -1.513  15.465  1.00 9.66  ? 119 HIS A CA  1 
ATOM   945  C  C   . HIS A 1 119 ? -12.255 -0.355  14.748  1.00 9.71  ? 119 HIS A C   1 
ATOM   946  O  O   . HIS A 1 119 ? -11.921 -0.002  13.578  1.00 10.06 ? 119 HIS A O   1 
ATOM   947  C  CB  . HIS A 1 119 ? -10.001 -1.287  15.557  1.00 7.31  ? 119 HIS A CB  1 
ATOM   948  C  CG  . HIS A 1 119 ? -9.307  -2.292  16.441  1.00 12.05 ? 119 HIS A CG  1 
ATOM   949  N  ND1 . HIS A 1 119 ? -7.943  -2.533  16.430  1.00 12.03 ? 119 HIS A ND1 1 
ATOM   950  C  CD2 . HIS A 1 119 ? -9.812  -3.107  17.404  1.00 10.99 ? 119 HIS A CD2 1 
ATOM   951  C  CE1 . HIS A 1 119 ? -7.646  -3.445  17.342  1.00 12.41 ? 119 HIS A CE1 1 
ATOM   952  N  NE2 . HIS A 1 119 ? -8.765  -3.831  17.917  1.00 10.39 ? 119 HIS A NE2 1 
ATOM   953  N  N   . LEU A 1 120 ? -13.244 0.228   15.432  1.00 10.13 ? 120 LEU A N   1 
ATOM   954  C  CA  . LEU A 1 120 ? -13.925 1.475   14.988  1.00 9.82  ? 120 LEU A CA  1 
ATOM   955  C  C   . LEU A 1 120 ? -13.300 2.627   15.771  1.00 10.14 ? 120 LEU A C   1 
ATOM   956  O  O   . LEU A 1 120 ? -13.483 2.691   16.988  1.00 10.83 ? 120 LEU A O   1 
ATOM   957  C  CB  . LEU A 1 120 ? -15.437 1.358   15.213  1.00 9.71  ? 120 LEU A CB  1 
ATOM   958  C  CG  . LEU A 1 120 ? -16.133 0.254   14.332  1.00 12.53 ? 120 LEU A CG  1 
ATOM   959  C  CD1 . LEU A 1 120 ? -16.941 -0.684  15.228  1.00 12.61 ? 120 LEU A CD1 1 
ATOM   960  C  CD2 . LEU A 1 120 ? -17.033 0.907   13.183  1.00 13.63 ? 120 LEU A CD2 1 
ATOM   961  N  N   . VAL A 1 121 ? -12.487 3.442   15.096  1.00 10.45 ? 121 VAL A N   1 
ATOM   962  C  CA  . VAL A 1 121 ? -11.617 4.422   15.730  1.00 11.20 ? 121 VAL A CA  1 
ATOM   963  C  C   . VAL A 1 121 ? -12.367 5.774   15.765  1.00 11.93 ? 121 VAL A C   1 
ATOM   964  O  O   . VAL A 1 121 ? -12.865 6.251   14.715  1.00 11.51 ? 121 VAL A O   1 
ATOM   965  C  CB  . VAL A 1 121 ? -10.251 4.566   14.933  1.00 12.21 ? 121 VAL A CB  1 
ATOM   966  C  CG1 . VAL A 1 121 ? -9.322  5.703   15.507  1.00 10.16 ? 121 VAL A CG1 1 
ATOM   967  C  CG2 . VAL A 1 121 ? -9.484  3.201   14.833  1.00 9.04  ? 121 VAL A CG2 1 
ATOM   968  N  N   . HIS A 1 122 ? -12.466 6.379   16.958  1.00 10.04 ? 122 HIS A N   1 
ATOM   969  C  CA  . HIS A 1 122 ? -13.188 7.633   17.097  1.00 11.10 ? 122 HIS A CA  1 
ATOM   970  C  C   . HIS A 1 122 ? -12.310 8.612   17.889  1.00 12.49 ? 122 HIS A C   1 
ATOM   971  O  O   . HIS A 1 122 ? -11.507 8.218   18.749  1.00 11.42 ? 122 HIS A O   1 
ATOM   972  C  CB  . HIS A 1 122 ? -14.518 7.518   17.853  1.00 10.15 ? 122 HIS A CB  1 
ATOM   973  C  CG  . HIS A 1 122 ? -15.362 6.321   17.479  1.00 9.73  ? 122 HIS A CG  1 
ATOM   974  N  ND1 . HIS A 1 122 ? -15.019 5.017   17.790  1.00 7.74  ? 122 HIS A ND1 1 
ATOM   975  C  CD2 . HIS A 1 122 ? -16.574 6.263   16.895  1.00 11.15 ? 122 HIS A CD2 1 
ATOM   976  C  CE1 . HIS A 1 122 ? -15.988 4.211   17.391  1.00 13.28 ? 122 HIS A CE1 1 
ATOM   977  N  NE2 . HIS A 1 122 ? -16.919 4.936   16.796  1.00 12.40 ? 122 HIS A NE2 1 
ATOM   978  N  N   . TRP A 1 123 ? -12.482 9.891   17.584  1.00 11.99 ? 123 TRP A N   1 
ATOM   979  C  CA  . TRP A 1 123 ? -11.689 10.924  18.246  1.00 12.08 ? 123 TRP A CA  1 
ATOM   980  C  C   . TRP A 1 123 ? -12.549 11.996  18.920  1.00 12.11 ? 123 TRP A C   1 
ATOM   981  O  O   . TRP A 1 123 ? -13.612 12.386  18.428  1.00 12.26 ? 123 TRP A O   1 
ATOM   982  C  CB  . TRP A 1 123 ? -10.688 11.548  17.298  1.00 12.24 ? 123 TRP A CB  1 
ATOM   983  C  CG  . TRP A 1 123 ? -11.274 12.154  16.055  1.00 14.34 ? 123 TRP A CG  1 
ATOM   984  C  CD1 . TRP A 1 123 ? -11.433 11.544  14.804  1.00 14.77 ? 123 TRP A CD1 1 
ATOM   985  C  CD2 . TRP A 1 123 ? -11.707 13.508  15.897  1.00 15.71 ? 123 TRP A CD2 1 
ATOM   986  N  NE1 . TRP A 1 123 ? -11.969 12.436  13.914  1.00 13.26 ? 123 TRP A NE1 1 
ATOM   987  C  CE2 . TRP A 1 123 ? -12.148 13.650  14.545  1.00 15.55 ? 123 TRP A CE2 1 
ATOM   988  C  CE3 . TRP A 1 123 ? -11.805 14.613  16.777  1.00 14.14 ? 123 TRP A CE3 1 
ATOM   989  C  CZ2 . TRP A 1 123 ? -12.659 14.878  14.040  1.00 14.10 ? 123 TRP A CZ2 1 
ATOM   990  C  CZ3 . TRP A 1 123 ? -12.343 15.802  16.308  1.00 15.20 ? 123 TRP A CZ3 1 
ATOM   991  C  CH2 . TRP A 1 123 ? -12.733 15.939  14.914  1.00 15.40 ? 123 TRP A CH2 1 
ATOM   992  N  N   . ASN A 1 124 ? -12.058 12.455  20.056  1.00 13.79 ? 124 ASN A N   1 
ATOM   993  C  CA  . ASN A 1 124 ? -12.791 13.320  20.958  1.00 14.20 ? 124 ASN A CA  1 
ATOM   994  C  C   . ASN A 1 124 ? -13.011 14.711  20.266  1.00 14.87 ? 124 ASN A C   1 
ATOM   995  O  O   . ASN A 1 124 ? -12.057 15.384  19.869  1.00 12.65 ? 124 ASN A O   1 
ATOM   996  C  CB  . ASN A 1 124 ? -12.014 13.399  22.286  1.00 14.17 ? 124 ASN A CB  1 
ATOM   997  C  CG  . ASN A 1 124 ? -12.810 14.031  23.397  1.00 13.59 ? 124 ASN A CG  1 
ATOM   998  O  OD1 . ASN A 1 124 ? -13.482 15.027  23.174  1.00 15.57 ? 124 ASN A OD1 1 
ATOM   999  N  ND2 . ASN A 1 124 ? -12.705 13.465  24.621  1.00 14.38 ? 124 ASN A ND2 1 
ATOM   1000 N  N   . THR A 1 125 ? -14.272 15.111  20.142  1.00 16.15 ? 125 THR A N   1 
ATOM   1001 C  CA  . THR A 1 125 ? -14.625 16.355  19.462  1.00 16.78 ? 125 THR A CA  1 
ATOM   1002 C  C   . THR A 1 125 ? -13.967 17.590  20.078  1.00 16.91 ? 125 THR A C   1 
ATOM   1003 O  O   . THR A 1 125 ? -13.800 18.609  19.408  1.00 18.36 ? 125 THR A O   1 
ATOM   1004 C  CB  . THR A 1 125 ? -16.151 16.565  19.433  1.00 16.89 ? 125 THR A CB  1 
ATOM   1005 O  OG1 . THR A 1 125 ? -16.703 16.261  20.719  1.00 20.28 ? 125 THR A OG1 1 
ATOM   1006 C  CG2 . THR A 1 125 ? -16.793 15.668  18.385  1.00 18.16 ? 125 THR A CG2 1 
ATOM   1007 N  N   . LYS A 1 126 ? -13.601 17.498  21.352  1.00 18.11 ? 127 LYS A N   1 
ATOM   1008 C  CA  . LYS A 1 126 ? -13.012 18.629  22.064  1.00 20.52 ? 127 LYS A CA  1 
ATOM   1009 C  C   . LYS A 1 126 ? -11.661 19.048  21.487  1.00 20.95 ? 127 LYS A C   1 
ATOM   1010 O  O   . LYS A 1 126 ? -11.278 20.216  21.566  1.00 23.53 ? 127 LYS A O   1 
ATOM   1011 C  CB  . LYS A 1 126 ? -12.867 18.306  23.553  1.00 21.08 ? 127 LYS A CB  1 
ATOM   1012 C  CG  . LYS A 1 126 ? -12.141 17.001  23.837  1.00 21.22 ? 127 LYS A CG  1 
ATOM   1013 C  CD  . LYS A 1 126 ? -12.482 16.468  25.218  1.00 25.63 ? 127 LYS A CD  1 
ATOM   1014 C  CE  . LYS A 1 126 ? -11.342 16.698  26.196  1.00 26.28 ? 127 LYS A CE  1 
ATOM   1015 N  NZ  . LYS A 1 126 ? -11.697 16.264  27.576  1.00 29.96 ? 127 LYS A NZ  1 
ATOM   1016 N  N   . TYR A 1 127 ? -10.945 18.089  20.912  1.00 19.09 ? 128 TYR A N   1 
ATOM   1017 C  CA  . TYR A 1 127 ? -9.612  18.338  20.352  1.00 17.49 ? 128 TYR A CA  1 
ATOM   1018 C  C   . TYR A 1 127 ? -9.580  18.748  18.915  1.00 18.26 ? 128 TYR A C   1 
ATOM   1019 O  O   . TYR A 1 127 ? -8.491  18.965  18.342  1.00 18.58 ? 128 TYR A O   1 
ATOM   1020 C  CB  . TYR A 1 127 ? -8.696  17.152  20.586  1.00 16.82 ? 128 TYR A CB  1 
ATOM   1021 C  CG  . TYR A 1 127 ? -8.601  16.876  22.053  1.00 15.90 ? 128 TYR A CG  1 
ATOM   1022 C  CD1 . TYR A 1 127 ? -8.242  17.910  22.943  1.00 16.89 ? 128 TYR A CD1 1 
ATOM   1023 C  CD2 . TYR A 1 127 ? -8.885  15.621  22.565  1.00 16.07 ? 128 TYR A CD2 1 
ATOM   1024 C  CE1 . TYR A 1 127 ? -8.169  17.663  24.321  1.00 16.01 ? 128 TYR A CE1 1 
ATOM   1025 C  CE2 . TYR A 1 127 ? -8.793  15.362  23.896  1.00 14.08 ? 128 TYR A CE2 1 
ATOM   1026 C  CZ  . TYR A 1 127 ? -8.427  16.427  24.771  1.00 14.12 ? 128 TYR A CZ  1 
ATOM   1027 O  OH  . TYR A 1 127 ? -8.353  16.218  26.082  1.00 15.70 ? 128 TYR A OH  1 
ATOM   1028 N  N   . GLY A 1 128 ? -10.764 18.797  18.316  1.00 17.94 ? 129 GLY A N   1 
ATOM   1029 C  CA  . GLY A 1 128 ? -10.937 19.459  17.055  1.00 19.10 ? 129 GLY A CA  1 
ATOM   1030 C  C   . GLY A 1 128 ? -10.517 18.606  15.877  1.00 20.12 ? 129 GLY A C   1 
ATOM   1031 O  O   . GLY A 1 128 ? -11.066 18.745  14.792  1.00 18.41 ? 129 GLY A O   1 
ATOM   1032 N  N   . ASP A 1 129 ? -9.517  17.746  16.044  1.00 20.03 ? 130 ASP A N   1 
ATOM   1033 C  CA  . ASP A 1 129 ? -9.216  16.853  14.931  1.00 20.27 ? 130 ASP A CA  1 
ATOM   1034 C  C   . ASP A 1 129 ? -8.465  15.629  15.435  1.00 19.90 ? 130 ASP A C   1 
ATOM   1035 O  O   . ASP A 1 129 ? -8.025  15.619  16.596  1.00 18.97 ? 130 ASP A O   1 
ATOM   1036 C  CB  . ASP A 1 129 ? -8.616  17.534  13.681  1.00 21.25 ? 130 ASP A CB  1 
ATOM   1037 C  CG  . ASP A 1 129 ? -7.121  17.866  13.796  1.00 23.61 ? 130 ASP A CG  1 
ATOM   1038 O  OD1 . ASP A 1 129 ? -6.509  17.748  14.880  1.00 27.82 ? 130 ASP A OD1 1 
ATOM   1039 O  OD2 . ASP A 1 129 ? -6.552  18.274  12.759  1.00 29.40 ? 130 ASP A OD2 1 
ATOM   1040 N  N   . PHE A 1 130 ? -8.326  14.626  14.573  1.00 18.67 ? 131 PHE A N   1 
ATOM   1041 C  CA  . PHE A 1 130 ? -7.638  13.360  14.947  1.00 18.22 ? 131 PHE A CA  1 
ATOM   1042 C  C   . PHE A 1 130 ? -6.171  13.603  15.329  1.00 17.62 ? 131 PHE A C   1 
ATOM   1043 O  O   . PHE A 1 130 ? -5.689  13.040  16.337  1.00 15.66 ? 131 PHE A O   1 
ATOM   1044 C  CB  . PHE A 1 130 ? -7.780  12.303  13.833  1.00 14.82 ? 131 PHE A CB  1 
ATOM   1045 C  CG  . PHE A 1 130 ? -7.050  11.036  14.090  1.00 18.84 ? 131 PHE A CG  1 
ATOM   1046 C  CD1 . PHE A 1 130 ? -7.686  9.966   14.748  1.00 15.42 ? 131 PHE A CD1 1 
ATOM   1047 C  CD2 . PHE A 1 130 ? -5.715  10.873  13.651  1.00 18.10 ? 131 PHE A CD2 1 
ATOM   1048 C  CE1 . PHE A 1 130 ? -7.020  8.767   14.985  1.00 18.39 ? 131 PHE A CE1 1 
ATOM   1049 C  CE2 . PHE A 1 130 ? -5.027  9.648   13.890  1.00 19.75 ? 131 PHE A CE2 1 
ATOM   1050 C  CZ  . PHE A 1 130 ? -5.680  8.601   14.564  1.00 18.25 ? 131 PHE A CZ  1 
ATOM   1051 N  N   . GLY A 1 131 ? -5.476  14.417  14.532  1.00 16.25 ? 132 GLY A N   1 
ATOM   1052 C  CA  . GLY A 1 131 ? -4.018  14.687  14.806  1.00 17.18 ? 132 GLY A CA  1 
ATOM   1053 C  C   . GLY A 1 131 ? -3.719  15.252  16.195  1.00 16.47 ? 132 GLY A C   1 
ATOM   1054 O  O   . GLY A 1 131 ? -2.763  14.853  16.902  1.00 17.70 ? 132 GLY A O   1 
ATOM   1055 N  N   . LYS A 1 132 ? -4.537  16.194  16.620  1.00 16.74 ? 133 LYS A N   1 
ATOM   1056 C  CA  . LYS A 1 132 ? -4.437  16.725  17.993  1.00 16.44 ? 133 LYS A CA  1 
ATOM   1057 C  C   . LYS A 1 132 ? -4.954  15.801  19.069  1.00 15.78 ? 133 LYS A C   1 
ATOM   1058 O  O   . LYS A 1 132 ? -4.379  15.707  20.164  1.00 14.30 ? 133 LYS A O   1 
ATOM   1059 C  CB  . LYS A 1 132 ? -5.150  18.088  18.042  1.00 18.80 ? 133 LYS A CB  1 
ATOM   1060 C  CG  . LYS A 1 132 ? -4.395  19.160  17.261  1.00 24.09 ? 133 LYS A CG  1 
ATOM   1061 C  CD  . LYS A 1 132 ? -3.219  19.746  18.058  1.00 33.52 ? 133 LYS A CD  1 
ATOM   1062 C  CE  . LYS A 1 132 ? -3.677  20.887  18.988  1.00 35.19 ? 133 LYS A CE  1 
ATOM   1063 N  NZ  . LYS A 1 132 ? -2.630  21.334  20.000  1.00 35.20 ? 133 LYS A NZ  1 
ATOM   1064 N  N   . ALA A 1 133 ? -6.070  15.108  18.779  1.00 14.18 ? 134 ALA A N   1 
ATOM   1065 C  CA  . ALA A 1 133 ? -6.653  14.141  19.704  1.00 14.40 ? 134 ALA A CA  1 
ATOM   1066 C  C   . ALA A 1 133 ? -5.651  13.040  20.183  1.00 13.98 ? 134 ALA A C   1 
ATOM   1067 O  O   . ALA A 1 133 ? -5.651  12.649  21.396  1.00 12.53 ? 134 ALA A O   1 
ATOM   1068 C  CB  . ALA A 1 133 ? -7.910  13.472  19.030  1.00 12.60 ? 134 ALA A CB  1 
ATOM   1069 N  N   . VAL A 1 134 ? -4.813  12.541  19.249  1.00 13.68 ? 135 VAL A N   1 
ATOM   1070 C  CA  . VAL A 1 134 ? -3.867  11.446  19.581  1.00 13.72 ? 135 VAL A CA  1 
ATOM   1071 C  C   . VAL A 1 134 ? -2.768  11.869  20.538  1.00 14.49 ? 135 VAL A C   1 
ATOM   1072 O  O   . VAL A 1 134 ? -2.091  11.023  21.115  1.00 14.69 ? 135 VAL A O   1 
ATOM   1073 C  CB  . VAL A 1 134 ? -3.241  10.667  18.342  1.00 14.23 ? 135 VAL A CB  1 
ATOM   1074 C  CG1 . VAL A 1 134 ? -4.376  10.001  17.540  1.00 14.50 ? 135 VAL A CG1 1 
ATOM   1075 C  CG2 . VAL A 1 134 ? -2.382  11.541  17.472  1.00 11.93 ? 135 VAL A CG2 1 
ATOM   1076 N  N   . GLN A 1 135 ? -2.586  13.165  20.703  1.00 14.19 ? 136 GLN A N   1 
ATOM   1077 C  CA  . GLN A 1 135 ? -1.611  13.675  21.628  1.00 16.13 ? 136 GLN A CA  1 
ATOM   1078 C  C   . GLN A 1 135 ? -2.203  13.852  23.049  1.00 16.55 ? 136 GLN A C   1 
ATOM   1079 O  O   . GLN A 1 135 ? -1.528  14.369  23.980  1.00 17.87 ? 136 GLN A O   1 
ATOM   1080 C  CB  . GLN A 1 135 ? -1.040  15.014  21.083  1.00 16.70 ? 136 GLN A CB  1 
ATOM   1081 C  CG  . GLN A 1 135 ? -0.321  14.874  19.713  1.00 23.71 ? 136 GLN A CG  1 
ATOM   1082 C  CD  . GLN A 1 135 ? 0.916   13.926  19.763  1.00 34.86 ? 136 GLN A CD  1 
ATOM   1083 O  OE1 . GLN A 1 135 ? 1.529   13.729  20.845  1.00 39.47 ? 136 GLN A OE1 1 
ATOM   1084 N  NE2 . GLN A 1 135 ? 1.307   13.354  18.580  1.00 33.04 ? 136 GLN A NE2 1 
ATOM   1085 N  N   . GLN A 1 136 ? -3.444  13.444  23.230  1.00 15.66 ? 137 GLN A N   1 
ATOM   1086 C  CA  . GLN A 1 136 ? -4.136  13.599  24.521  1.00 14.45 ? 137 GLN A CA  1 
ATOM   1087 C  C   . GLN A 1 136 ? -4.472  12.275  25.140  1.00 14.25 ? 137 GLN A C   1 
ATOM   1088 O  O   . GLN A 1 136 ? -4.766  11.316  24.433  1.00 12.71 ? 137 GLN A O   1 
ATOM   1089 C  CB  . GLN A 1 136 ? -5.432  14.379  24.367  1.00 15.16 ? 137 GLN A CB  1 
ATOM   1090 C  CG  . GLN A 1 136 ? -5.320  15.625  23.494  1.00 17.82 ? 137 GLN A CG  1 
ATOM   1091 C  CD  . GLN A 1 136 ? -4.375  16.688  24.088  1.00 24.38 ? 137 GLN A CD  1 
ATOM   1092 O  OE1 . GLN A 1 136 ? -4.282  16.858  25.311  1.00 24.55 ? 137 GLN A OE1 1 
ATOM   1093 N  NE2 . GLN A 1 136 ? -3.699  17.408  23.207  1.00 25.34 ? 137 GLN A NE2 1 
ATOM   1094 N  N   . PRO A 1 137 ? -4.492  12.226  26.495  1.00 13.58 ? 138 PRO A N   1 
ATOM   1095 C  CA  . PRO A 1 137 ? -4.719  10.950  27.149  1.00 13.57 ? 138 PRO A CA  1 
ATOM   1096 C  C   . PRO A 1 137 ? -6.150  10.410  26.958  1.00 14.28 ? 138 PRO A C   1 
ATOM   1097 O  O   . PRO A 1 137 ? -6.387  9.203   27.079  1.00 13.24 ? 138 PRO A O   1 
ATOM   1098 C  CB  . PRO A 1 137 ? -4.364  11.188  28.621  1.00 15.19 ? 138 PRO A CB  1 
ATOM   1099 C  CG  . PRO A 1 137 ? -4.189  12.731  28.790  1.00 16.38 ? 138 PRO A CG  1 
ATOM   1100 C  CD  . PRO A 1 137 ? -4.230  13.372  27.386  1.00 13.14 ? 138 PRO A CD  1 
ATOM   1101 N  N   . ASP A 1 138 ? -7.098  11.300  26.677  1.00 13.55 ? 139 ASP A N   1 
ATOM   1102 C  CA  . ASP A 1 138 ? -8.451  10.858  26.373  1.00 14.83 ? 139 ASP A CA  1 
ATOM   1103 C  C   . ASP A 1 138 ? -8.806  11.230  24.926  1.00 13.86 ? 139 ASP A C   1 
ATOM   1104 O  O   . ASP A 1 138 ? -9.933  11.594  24.632  1.00 13.05 ? 139 ASP A O   1 
ATOM   1105 C  CB  . ASP A 1 138 ? -9.478  11.534  27.303  1.00 14.85 ? 139 ASP A CB  1 
ATOM   1106 C  CG  . ASP A 1 138 ? -9.315  13.039  27.347  1.00 17.37 ? 139 ASP A CG  1 
ATOM   1107 O  OD1 . ASP A 1 138 ? -8.355  13.578  26.729  1.00 21.00 ? 139 ASP A OD1 1 
ATOM   1108 O  OD2 . ASP A 1 138 ? -10.145 13.698  27.989  1.00 18.87 ? 139 ASP A OD2 1 
ATOM   1109 N  N   . GLY A 1 139 ? -7.849  11.157  24.031  1.00 13.11 ? 140 GLY A N   1 
ATOM   1110 C  CA  . GLY A 1 139 ? -8.109  11.684  22.711  1.00 13.25 ? 140 GLY A CA  1 
ATOM   1111 C  C   . GLY A 1 139 ? -8.922  10.796  21.809  1.00 12.01 ? 140 GLY A C   1 
ATOM   1112 O  O   . GLY A 1 139 ? -9.654  11.309  20.952  1.00 12.28 ? 140 GLY A O   1 
ATOM   1113 N  N   . LEU A 1 140 ? -8.770  9.479   21.988  1.00 12.89 ? 141 LEU A N   1 
ATOM   1114 C  CA  . LEU A 1 140 ? -9.434  8.490   21.159  1.00 12.89 ? 141 LEU A CA  1 
ATOM   1115 C  C   . LEU A 1 140 ? -10.375 7.571   21.930  1.00 13.35 ? 141 LEU A C   1 
ATOM   1116 O  O   . LEU A 1 140 ? -10.209 7.323   23.143  1.00 14.05 ? 141 LEU A O   1 
ATOM   1117 C  CB  . LEU A 1 140 ? -8.396  7.626   20.430  1.00 12.78 ? 141 LEU A CB  1 
ATOM   1118 C  CG  . LEU A 1 140 ? -7.477  8.295   19.359  1.00 15.58 ? 141 LEU A CG  1 
ATOM   1119 C  CD1 . LEU A 1 140 ? -6.808  7.241   18.475  1.00 14.19 ? 141 LEU A CD1 1 
ATOM   1120 C  CD2 . LEU A 1 140 ? -8.135  9.403   18.478  1.00 13.83 ? 141 LEU A CD2 1 
ATOM   1121 N  N   . ALA A 1 141 ? -11.395 7.087   21.232  1.00 12.50 ? 142 ALA A N   1 
ATOM   1122 C  CA  . ALA A 1 141 ? -12.213 5.964   21.750  1.00 10.40 ? 142 ALA A CA  1 
ATOM   1123 C  C   . ALA A 1 141 ? -12.261 4.898   20.648  1.00 11.75 ? 142 ALA A C   1 
ATOM   1124 O  O   . ALA A 1 141 ? -12.640 5.156   19.527  1.00 10.31 ? 142 ALA A O   1 
ATOM   1125 C  CB  . ALA A 1 141 ? -13.578 6.430   22.168  1.00 11.06 ? 142 ALA A CB  1 
ATOM   1126 N  N   . VAL A 1 142 ? -11.784 3.694   20.962  1.00 12.43 ? 143 VAL A N   1 
ATOM   1127 C  CA  . VAL A 1 142 ? -11.811 2.659   19.914  1.00 12.42 ? 143 VAL A CA  1 
ATOM   1128 C  C   . VAL A 1 142 ? -12.749 1.549   20.375  1.00 11.84 ? 143 VAL A C   1 
ATOM   1129 O  O   . VAL A 1 142 ? -12.599 0.999   21.499  1.00 11.61 ? 143 VAL A O   1 
ATOM   1130 C  CB  . VAL A 1 142 ? -10.393 2.115   19.578  1.00 12.64 ? 143 VAL A CB  1 
ATOM   1131 C  CG1 . VAL A 1 142 ? -10.435 1.105   18.419  1.00 10.51 ? 143 VAL A CG1 1 
ATOM   1132 C  CG2 . VAL A 1 142 ? -9.397  3.282   19.257  1.00 11.79 ? 143 VAL A CG2 1 
ATOM   1133 N  N   . LEU A 1 143 ? -13.751 1.296   19.544  1.00 11.28 ? 144 LEU A N   1 
ATOM   1134 C  CA  . LEU A 1 143 ? -14.724 0.229   19.755  1.00 11.19 ? 144 LEU A CA  1 
ATOM   1135 C  C   . LEU A 1 143 ? -14.203 -1.039  19.096  1.00 11.05 ? 144 LEU A C   1 
ATOM   1136 O  O   . LEU A 1 143 ? -14.171 -1.084  17.901  1.00 10.37 ? 144 LEU A O   1 
ATOM   1137 C  CB  . LEU A 1 143 ? -16.092 0.609   19.168  1.00 10.90 ? 144 LEU A CB  1 
ATOM   1138 C  CG  . LEU A 1 143 ? -17.291 -0.315  19.378  1.00 12.65 ? 144 LEU A CG  1 
ATOM   1139 C  CD1 . LEU A 1 143 ? -17.577 -0.503  20.911  1.00 16.99 ? 144 LEU A CD1 1 
ATOM   1140 C  CD2 . LEU A 1 143 ? -18.563 0.154   18.602  1.00 12.41 ? 144 LEU A CD2 1 
ATOM   1141 N  N   . GLY A 1 144 ? -13.836 -2.050  19.911  1.00 10.17 ? 145 GLY A N   1 
ATOM   1142 C  CA  . GLY A 1 144 ? -13.236 -3.329  19.452  1.00 10.50 ? 145 GLY A CA  1 
ATOM   1143 C  C   . GLY A 1 144 ? -14.342 -4.403  19.415  1.00 10.04 ? 145 GLY A C   1 
ATOM   1144 O  O   . GLY A 1 144 ? -15.072 -4.611  20.377  1.00 8.95  ? 145 GLY A O   1 
ATOM   1145 N  N   . ILE A 1 145 ? -14.466 -5.090  18.296  1.00 10.55 ? 146 ILE A N   1 
ATOM   1146 C  CA  . ILE A 1 145 ? -15.502 -6.145  18.164  1.00 11.11 ? 146 ILE A CA  1 
ATOM   1147 C  C   . ILE A 1 145 ? -14.754 -7.418  17.654  1.00 12.39 ? 146 ILE A C   1 
ATOM   1148 O  O   . ILE A 1 145 ? -14.002 -7.354  16.681  1.00 13.31 ? 146 ILE A O   1 
ATOM   1149 C  CB  . ILE A 1 145 ? -16.636 -5.689  17.202  1.00 10.62 ? 146 ILE A CB  1 
ATOM   1150 C  CG1 . ILE A 1 145 ? -17.292 -4.369  17.677  1.00 10.15 ? 146 ILE A CG1 1 
ATOM   1151 C  CG2 . ILE A 1 145 ? -17.637 -6.901  16.857  1.00 9.71  ? 146 ILE A CG2 1 
ATOM   1152 C  CD1 . ILE A 1 145 ? -18.329 -3.682  16.680  1.00 9.54  ? 146 ILE A CD1 1 
ATOM   1153 N  N   . PHE A 1 146 ? -14.943 -8.550  18.319  1.00 12.45 ? 147 PHE A N   1 
ATOM   1154 C  CA  . PHE A 1 146 ? -14.257 -9.816  17.883  1.00 12.31 ? 147 PHE A CA  1 
ATOM   1155 C  C   . PHE A 1 146 ? -15.048 -10.458 16.770  1.00 12.92 ? 147 PHE A C   1 
ATOM   1156 O  O   . PHE A 1 146 ? -16.267 -10.286 16.717  1.00 11.71 ? 147 PHE A O   1 
ATOM   1157 C  CB  . PHE A 1 146 ? -14.209 -10.806 19.032  1.00 12.07 ? 147 PHE A CB  1 
ATOM   1158 C  CG  . PHE A 1 146 ? -13.415 -10.319 20.228  1.00 11.68 ? 147 PHE A CG  1 
ATOM   1159 C  CD1 . PHE A 1 146 ? -12.019 -10.166 20.129  1.00 13.26 ? 147 PHE A CD1 1 
ATOM   1160 C  CD2 . PHE A 1 146 ? -14.035 -10.081 21.428  1.00 12.73 ? 147 PHE A CD2 1 
ATOM   1161 C  CE1 . PHE A 1 146 ? -11.242 -9.785  21.223  1.00 12.27 ? 147 PHE A CE1 1 
ATOM   1162 C  CE2 . PHE A 1 146 ? -13.288 -9.690  22.564  1.00 11.01 ? 147 PHE A CE2 1 
ATOM   1163 C  CZ  . PHE A 1 146 ? -11.886 -9.548  22.463  1.00 10.82 ? 147 PHE A CZ  1 
ATOM   1164 N  N   . LEU A 1 147 ? -14.346 -11.136 15.870  1.00 11.82 ? 148 LEU A N   1 
ATOM   1165 C  CA  . LEU A 1 147 ? -14.932 -11.933 14.813  1.00 12.28 ? 148 LEU A CA  1 
ATOM   1166 C  C   . LEU A 1 147 ? -14.614 -13.407 15.068  1.00 13.42 ? 148 LEU A C   1 
ATOM   1167 O  O   . LEU A 1 147 ? -13.447 -13.801 15.297  1.00 13.49 ? 148 LEU A O   1 
ATOM   1168 C  CB  . LEU A 1 147 ? -14.408 -11.493 13.400  1.00 11.68 ? 148 LEU A CB  1 
ATOM   1169 C  CG  . LEU A 1 147 ? -14.934 -10.156 12.755  1.00 9.83  ? 148 LEU A CG  1 
ATOM   1170 C  CD1 . LEU A 1 147 ? -14.739 -8.864  13.673  1.00 7.97  ? 148 LEU A CD1 1 
ATOM   1171 C  CD2 . LEU A 1 147 ? -14.317 -9.910  11.418  1.00 11.91 ? 148 LEU A CD2 1 
ATOM   1172 N  N   . LYS A 1 148 ? -15.663 -14.219 15.049  1.00 14.28 ? 149 LYS A N   1 
ATOM   1173 C  CA  . LYS A 1 148 ? -15.475 -15.650 14.919  1.00 16.52 ? 149 LYS A CA  1 
ATOM   1174 C  C   . LYS A 1 148 ? -15.997 -16.106 13.550  1.00 15.14 ? 149 LYS A C   1 
ATOM   1175 O  O   . LYS A 1 148 ? -16.810 -15.461 12.897  1.00 14.32 ? 149 LYS A O   1 
ATOM   1176 C  CB  . LYS A 1 148 ? -16.128 -16.437 16.082  1.00 14.87 ? 149 LYS A CB  1 
ATOM   1177 C  CG  . LYS A 1 148 ? -17.610 -16.195 16.231  1.00 19.50 ? 149 LYS A CG  1 
ATOM   1178 C  CD  . LYS A 1 148 ? -18.184 -17.111 17.369  1.00 20.00 ? 149 LYS A CD  1 
ATOM   1179 C  CE  . LYS A 1 148 ? -19.697 -16.974 17.442  1.00 28.65 ? 149 LYS A CE  1 
ATOM   1180 N  NZ  . LYS A 1 148 ? -20.264 -18.050 18.372  1.00 35.54 ? 149 LYS A NZ  1 
ATOM   1181 N  N   . VAL A 1 149 ? -15.543 -17.275 13.165  1.00 16.20 ? 150 VAL A N   1 
ATOM   1182 C  CA  . VAL A 1 149 ? -15.868 -17.850 11.888  1.00 15.89 ? 150 VAL A CA  1 
ATOM   1183 C  C   . VAL A 1 149 ? -17.065 -18.816 12.156  1.00 16.34 ? 150 VAL A C   1 
ATOM   1184 O  O   . VAL A 1 149 ? -17.009 -19.670 13.087  1.00 15.85 ? 150 VAL A O   1 
ATOM   1185 C  CB  . VAL A 1 149 ? -14.650 -18.575 11.314  1.00 15.76 ? 150 VAL A CB  1 
ATOM   1186 C  CG1 . VAL A 1 149 ? -15.040 -19.390 10.041  1.00 14.33 ? 150 VAL A CG1 1 
ATOM   1187 C  CG2 . VAL A 1 149 ? -13.523 -17.551 11.003  1.00 15.10 ? 150 VAL A CG2 1 
ATOM   1188 N  N   . GLY A 1 150 ? -18.161 -18.556 11.424  1.00 15.09 ? 151 GLY A N   1 
ATOM   1189 C  CA  . GLY A 1 150 ? -19.336 -19.494 11.296  1.00 15.53 ? 151 GLY A CA  1 
ATOM   1190 C  C   . GLY A 1 150 ? -20.219 -18.972 10.188  1.00 13.58 ? 151 GLY A C   1 
ATOM   1191 O  O   . GLY A 1 150 ? -19.828 -18.953 9.025   1.00 14.16 ? 151 GLY A O   1 
ATOM   1192 N  N   . SER A 1 151 ? -21.408 -18.508 10.551  1.00 16.68 ? 152 SER A N   1 
ATOM   1193 C  CA  . SER A 1 151 ? -22.288 -17.748 9.599   1.00 17.82 ? 152 SER A CA  1 
ATOM   1194 C  C   . SER A 1 151 ? -21.628 -16.480 9.020   1.00 16.92 ? 152 SER A C   1 
ATOM   1195 O  O   . SER A 1 151 ? -20.959 -15.792 9.736   1.00 15.39 ? 152 SER A O   1 
ATOM   1196 C  CB  . SER A 1 151 ? -23.548 -17.299 10.316  1.00 18.68 ? 152 SER A CB  1 
ATOM   1197 O  OG  . SER A 1 151 ? -24.266 -18.438 10.706  1.00 25.91 ? 152 SER A OG  1 
ATOM   1198 N  N   . ALA A 1 152 ? -21.816 -16.194 7.721   1.00 15.63 ? 153 ALA A N   1 
ATOM   1199 C  CA  . ALA A 1 152 ? -21.511 -14.913 7.142   1.00 14.29 ? 153 ALA A CA  1 
ATOM   1200 C  C   . ALA A 1 152 ? -22.155 -13.702 7.865   1.00 15.71 ? 153 ALA A C   1 
ATOM   1201 O  O   . ALA A 1 152 ? -23.246 -13.782 8.433   1.00 15.94 ? 153 ALA A O   1 
ATOM   1202 C  CB  . ALA A 1 152 ? -21.856 -14.886 5.595   1.00 14.82 ? 153 ALA A CB  1 
ATOM   1203 N  N   . LYS A 1 153 ? -21.444 -12.567 7.858   1.00 15.54 ? 154 LYS A N   1 
ATOM   1204 C  CA  . LYS A 1 153 ? -22.039 -11.313 8.299   1.00 16.07 ? 154 LYS A CA  1 
ATOM   1205 C  C   . LYS A 1 153 ? -22.447 -10.546 7.043   1.00 16.28 ? 154 LYS A C   1 
ATOM   1206 O  O   . LYS A 1 153 ? -21.554 -10.083 6.293   1.00 15.66 ? 154 LYS A O   1 
ATOM   1207 C  CB  . LYS A 1 153 ? -20.989 -10.489 9.034   1.00 16.45 ? 154 LYS A CB  1 
ATOM   1208 C  CG  . LYS A 1 153 ? -21.564 -9.355  9.782   1.00 16.41 ? 154 LYS A CG  1 
ATOM   1209 C  CD  . LYS A 1 153 ? -22.188 -9.837  11.056  1.00 18.49 ? 154 LYS A CD  1 
ATOM   1210 C  CE  . LYS A 1 153 ? -22.909 -8.728  11.823  1.00 20.09 ? 154 LYS A CE  1 
ATOM   1211 N  NZ  . LYS A 1 153 ? -23.867 -9.216  12.862  1.00 21.16 ? 154 LYS A NZ  1 
ATOM   1212 N  N   . PRO A 1 154 ? -23.782 -10.468 6.763   1.00 17.68 ? 155 PRO A N   1 
ATOM   1213 C  CA  . PRO A 1 154 ? -24.210 -9.870  5.490   1.00 18.28 ? 155 PRO A CA  1 
ATOM   1214 C  C   . PRO A 1 154 ? -23.684 -8.451  5.354   1.00 17.70 ? 155 PRO A C   1 
ATOM   1215 O  O   . PRO A 1 154 ? -23.294 -8.068  4.268   1.00 19.17 ? 155 PRO A O   1 
ATOM   1216 C  CB  . PRO A 1 154 ? -25.754 -9.853  5.618   1.00 18.67 ? 155 PRO A CB  1 
ATOM   1217 C  CG  . PRO A 1 154 ? -26.024 -11.070 6.500   1.00 17.99 ? 155 PRO A CG  1 
ATOM   1218 C  CD  . PRO A 1 154 ? -24.953 -10.946 7.547   1.00 17.55 ? 155 PRO A CD  1 
ATOM   1219 N  N   . GLY A 1 155 ? -23.665 -7.708  6.451   1.00 16.99 ? 156 GLY A N   1 
ATOM   1220 C  CA  . GLY A 1 155 ? -23.182 -6.321  6.455   1.00 16.52 ? 156 GLY A CA  1 
ATOM   1221 C  C   . GLY A 1 155 ? -21.711 -6.108  6.182   1.00 16.49 ? 156 GLY A C   1 
ATOM   1222 O  O   . GLY A 1 155 ? -21.305 -4.973  5.923   1.00 18.10 ? 156 GLY A O   1 
ATOM   1223 N  N   . LEU A 1 156 ? -20.918 -7.192  6.240   1.00 13.85 ? 157 LEU A N   1 
ATOM   1224 C  CA  . LEU A 1 156 ? -19.508 -7.149  5.912   1.00 13.85 ? 157 LEU A CA  1 
ATOM   1225 C  C   . LEU A 1 156 ? -19.228 -7.378  4.453   1.00 13.05 ? 157 LEU A C   1 
ATOM   1226 O  O   . LEU A 1 156 ? -18.182 -7.074  4.014   1.00 13.87 ? 157 LEU A O   1 
ATOM   1227 C  CB  . LEU A 1 156 ? -18.735 -8.215  6.740   1.00 14.09 ? 157 LEU A CB  1 
ATOM   1228 C  CG  . LEU A 1 156 ? -17.200 -8.332  6.559   1.00 14.36 ? 157 LEU A CG  1 
ATOM   1229 C  CD1 . LEU A 1 156 ? -16.578 -6.988  6.931   1.00 11.27 ? 157 LEU A CD1 1 
ATOM   1230 C  CD2 . LEU A 1 156 ? -16.571 -9.482  7.411   1.00 10.99 ? 157 LEU A CD2 1 
ATOM   1231 N  N   . GLN A 1 157 ? -20.159 -7.965  3.697   1.00 16.35 ? 158 GLN A N   1 
ATOM   1232 C  CA  . GLN A 1 157 ? -19.879 -8.408  2.307   1.00 16.33 ? 158 GLN A CA  1 
ATOM   1233 C  C   . GLN A 1 157 ? -19.470 -7.319  1.371   1.00 16.11 ? 158 GLN A C   1 
ATOM   1234 O  O   . GLN A 1 157 ? -18.570 -7.529  0.534   1.00 16.94 ? 158 GLN A O   1 
ATOM   1235 C  CB  . GLN A 1 157 ? -21.041 -9.226  1.706   1.00 17.32 ? 158 GLN A CB  1 
ATOM   1236 C  CG  . GLN A 1 157 ? -20.657 -10.014 0.439   1.00 18.97 ? 158 GLN A CG  1 
ATOM   1237 C  CD  . GLN A 1 157 ? -19.513 -10.985 0.704   1.00 15.61 ? 158 GLN A CD  1 
ATOM   1238 O  OE1 . GLN A 1 157 ? -19.343 -11.514 1.823   1.00 20.58 ? 158 GLN A OE1 1 
ATOM   1239 N  NE2 . GLN A 1 157 ? -18.699 -11.202 -0.308  1.00 17.64 ? 158 GLN A NE2 1 
ATOM   1240 N  N   A LYS A 1 158 ? -20.120 -6.152  1.501   0.50 16.51 ? 159 LYS A N   1 
ATOM   1241 N  N   B LYS A 1 158 ? -20.085 -6.148  1.456   0.50 15.52 ? 159 LYS A N   1 
ATOM   1242 C  CA  A LYS A 1 158 ? -19.771 -4.917  0.754   0.50 15.85 ? 159 LYS A CA  1 
ATOM   1243 C  CA  B LYS A 1 158 ? -19.594 -5.081  0.595   0.50 14.74 ? 159 LYS A CA  1 
ATOM   1244 C  C   A LYS A 1 158 ? -18.265 -4.557  0.893   0.50 15.61 ? 159 LYS A C   1 
ATOM   1245 C  C   B LYS A 1 158 ? -18.105 -4.801  0.819   0.50 14.60 ? 159 LYS A C   1 
ATOM   1246 O  O   A LYS A 1 158 ? -17.637 -4.163  -0.078  0.50 14.63 ? 159 LYS A O   1 
ATOM   1247 O  O   B LYS A 1 158 ? -17.343 -4.607  -0.135  0.50 12.84 ? 159 LYS A O   1 
ATOM   1248 C  CB  A LYS A 1 158 ? -20.733 -3.756  1.129   0.50 16.56 ? 159 LYS A CB  1 
ATOM   1249 C  CB  B LYS A 1 158 ? -20.368 -3.799  0.749   0.50 14.66 ? 159 LYS A CB  1 
ATOM   1250 C  CG  A LYS A 1 158 ? -20.562 -2.356  0.407   0.50 18.09 ? 159 LYS A CG  1 
ATOM   1251 C  CG  B LYS A 1 158 ? -19.699 -2.679  -0.036  0.50 15.68 ? 159 LYS A CG  1 
ATOM   1252 C  CD  A LYS A 1 158 ? -20.887 -2.385  -1.136  0.50 21.72 ? 159 LYS A CD  1 
ATOM   1253 C  CD  B LYS A 1 158 ? -20.084 -2.665  -1.526  0.50 15.48 ? 159 LYS A CD  1 
ATOM   1254 C  CE  A LYS A 1 158 ? -20.880 -0.988  -1.834  0.50 19.49 ? 159 LYS A CE  1 
ATOM   1255 C  CE  B LYS A 1 158 ? -18.884 -2.636  -2.436  0.50 12.72 ? 159 LYS A CE  1 
ATOM   1256 N  NZ  A LYS A 1 158 ? -19.570 -0.612  -2.437  0.50 15.01 ? 159 LYS A NZ  1 
ATOM   1257 N  NZ  B LYS A 1 158 ? -18.335 -4.032  -2.526  0.50 6.65  ? 159 LYS A NZ  1 
ATOM   1258 N  N   . VAL A 1 159 ? -17.685 -4.764  2.085   1.00 15.19 ? 160 VAL A N   1 
ATOM   1259 C  CA  . VAL A 1 159 ? -16.241 -4.563  2.354   1.00 13.90 ? 160 VAL A CA  1 
ATOM   1260 C  C   . VAL A 1 159 ? -15.394 -5.675  1.697   1.00 13.41 ? 160 VAL A C   1 
ATOM   1261 O  O   . VAL A 1 159 ? -14.395 -5.404  1.027   1.00 14.05 ? 160 VAL A O   1 
ATOM   1262 C  CB  . VAL A 1 159 ? -15.955 -4.544  3.871   1.00 13.40 ? 160 VAL A CB  1 
ATOM   1263 C  CG1 . VAL A 1 159 ? -14.441 -4.681  4.111   1.00 16.63 ? 160 VAL A CG1 1 
ATOM   1264 C  CG2 . VAL A 1 159 ? -16.573 -3.321  4.488   1.00 15.14 ? 160 VAL A CG2 1 
ATOM   1265 N  N   . VAL A 1 160 ? -15.818 -6.927  1.856   1.00 13.51 ? 161 VAL A N   1 
ATOM   1266 C  CA  . VAL A 1 160 ? -15.052 -8.098  1.341   1.00 16.37 ? 161 VAL A CA  1 
ATOM   1267 C  C   . VAL A 1 160 ? -14.946 -8.055  -0.221  1.00 16.59 ? 161 VAL A C   1 
ATOM   1268 O  O   . VAL A 1 160 ? -13.878 -8.257  -0.781  1.00 16.23 ? 161 VAL A O   1 
ATOM   1269 C  CB  . VAL A 1 160 ? -15.689 -9.478  1.880   1.00 16.62 ? 161 VAL A CB  1 
ATOM   1270 C  CG1 . VAL A 1 160 ? -15.394 -10.622 0.990   1.00 20.21 ? 161 VAL A CG1 1 
ATOM   1271 C  CG2 . VAL A 1 160 ? -15.256 -9.734  3.291   1.00 14.61 ? 161 VAL A CG2 1 
ATOM   1272 N  N   . ASP A 1 161 ? -16.035 -7.658  -0.874  1.00 19.53 ? 162 ASP A N   1 
ATOM   1273 C  CA  . ASP A 1 161 ? -16.066 -7.598  -2.344  1.00 22.44 ? 162 ASP A CA  1 
ATOM   1274 C  C   . ASP A 1 161 ? -15.229 -6.520  -3.022  1.00 22.88 ? 162 ASP A C   1 
ATOM   1275 O  O   . ASP A 1 161 ? -15.028 -6.606  -4.229  1.00 25.82 ? 162 ASP A O   1 
ATOM   1276 C  CB  . ASP A 1 161 ? -17.495 -7.441  -2.833  1.00 24.47 ? 162 ASP A CB  1 
ATOM   1277 C  CG  . ASP A 1 161 ? -18.280 -8.717  -2.725  1.00 26.83 ? 162 ASP A CG  1 
ATOM   1278 O  OD1 . ASP A 1 161 ? -17.670 -9.797  -2.855  1.00 30.39 ? 162 ASP A OD1 1 
ATOM   1279 O  OD2 . ASP A 1 161 ? -19.516 -8.621  -2.521  1.00 34.14 ? 162 ASP A OD2 1 
ATOM   1280 N  N   . VAL A 1 162 ? -14.778 -5.505  -2.293  1.00 21.17 ? 163 VAL A N   1 
ATOM   1281 C  CA  . VAL A 1 162 ? -13.957 -4.444  -2.858  1.00 19.88 ? 163 VAL A CA  1 
ATOM   1282 C  C   . VAL A 1 162 ? -12.469 -4.728  -2.650  1.00 19.21 ? 163 VAL A C   1 
ATOM   1283 O  O   . VAL A 1 162 ? -11.624 -4.106  -3.273  1.00 19.90 ? 163 VAL A O   1 
ATOM   1284 C  CB  . VAL A 1 162 ? -14.424 -3.110  -2.221  1.00 20.25 ? 163 VAL A CB  1 
ATOM   1285 C  CG1 . VAL A 1 162 ? -13.662 -2.767  -0.941  1.00 18.38 ? 163 VAL A CG1 1 
ATOM   1286 C  CG2 . VAL A 1 162 ? -14.374 -1.970  -3.185  1.00 23.16 ? 163 VAL A CG2 1 
ATOM   1287 N  N   . LEU A 1 163 ? -12.113 -5.666  -1.753  1.00 19.50 ? 164 LEU A N   1 
ATOM   1288 C  CA  . LEU A 1 163 ? -10.690 -5.937  -1.390  1.00 18.43 ? 164 LEU A CA  1 
ATOM   1289 C  C   . LEU A 1 163 ? -9.766  -6.303  -2.558  1.00 19.46 ? 164 LEU A C   1 
ATOM   1290 O  O   . LEU A 1 163 ? -8.532  -6.034  -2.524  1.00 17.10 ? 164 LEU A O   1 
ATOM   1291 C  CB  . LEU A 1 163 ? -10.579 -7.030  -0.335  1.00 17.90 ? 164 LEU A CB  1 
ATOM   1292 C  CG  . LEU A 1 163 ? -11.164 -6.724  1.043   1.00 17.70 ? 164 LEU A CG  1 
ATOM   1293 C  CD1 . LEU A 1 163 ? -10.940 -7.947  1.930   1.00 18.25 ? 164 LEU A CD1 1 
ATOM   1294 C  CD2 . LEU A 1 163 ? -10.696 -5.396  1.685   1.00 20.68 ? 164 LEU A CD2 1 
ATOM   1295 N  N   . ASP A 1 164 ? -10.372 -6.936  -3.572  1.00 21.67 ? 165 ASP A N   1 
ATOM   1296 C  CA  . ASP A 1 164 ? -9.673  -7.261  -4.830  1.00 23.06 ? 165 ASP A CA  1 
ATOM   1297 C  C   . ASP A 1 164 ? -9.092  -5.980  -5.485  1.00 22.48 ? 165 ASP A C   1 
ATOM   1298 O  O   . ASP A 1 164 ? -7.975  -6.009  -6.008  1.00 23.27 ? 165 ASP A O   1 
ATOM   1299 C  CB  . ASP A 1 164 ? -10.585 -8.102  -5.785  1.00 24.29 ? 165 ASP A CB  1 
ATOM   1300 C  CG  . ASP A 1 164 ? -11.478 -7.249  -6.675  1.00 28.15 ? 165 ASP A CG  1 
ATOM   1301 O  OD1 . ASP A 1 164 ? -12.567 -6.766  -6.213  1.00 31.57 ? 165 ASP A OD1 1 
ATOM   1302 O  OD2 . ASP A 1 164 ? -11.094 -7.051  -7.861  1.00 30.35 ? 165 ASP A OD2 1 
ATOM   1303 N  N   . SER A 1 165 ? -9.834  -4.874  -5.383  1.00 21.72 ? 166 SER A N   1 
ATOM   1304 C  CA  . SER A 1 165 ? -9.432  -3.546  -5.897  1.00 23.27 ? 166 SER A CA  1 
ATOM   1305 C  C   . SER A 1 165 ? -8.319  -2.789  -5.113  1.00 21.95 ? 166 SER A C   1 
ATOM   1306 O  O   . SER A 1 165 ? -7.740  -1.810  -5.618  1.00 20.36 ? 166 SER A O   1 
ATOM   1307 C  CB  . SER A 1 165 ? -10.670 -2.669  -6.103  1.00 22.47 ? 166 SER A CB  1 
ATOM   1308 O  OG  . SER A 1 165 ? -11.003 -2.038  -4.882  1.00 28.35 ? 166 SER A OG  1 
ATOM   1309 N  N   . ILE A 1 166 ? -8.031  -3.238  -3.877  1.00 19.22 ? 167 ILE A N   1 
ATOM   1310 C  CA  . ILE A 1 166 ? -7.005  -2.614  -3.054  1.00 18.64 ? 167 ILE A CA  1 
ATOM   1311 C  C   . ILE A 1 166 ? -6.021  -3.688  -2.578  1.00 18.23 ? 167 ILE A C   1 
ATOM   1312 O  O   . ILE A 1 166 ? -5.650  -3.780  -1.373  1.00 17.09 ? 167 ILE A O   1 
ATOM   1313 C  CB  . ILE A 1 166 ? -7.650  -1.836  -1.877  1.00 18.68 ? 167 ILE A CB  1 
ATOM   1314 C  CG1 . ILE A 1 166 ? -8.524  -2.761  -0.995  1.00 18.09 ? 167 ILE A CG1 1 
ATOM   1315 C  CG2 . ILE A 1 166 ? -8.525  -0.640  -2.407  1.00 17.63 ? 167 ILE A CG2 1 
ATOM   1316 C  CD1 . ILE A 1 166 ? -8.615  -2.306  0.485   1.00 18.31 ? 167 ILE A CD1 1 
ATOM   1317 N  N   . LYS A 1 167 ? -5.655  -4.583  -3.487  1.00 19.58 ? 168 LYS A N   1 
ATOM   1318 C  CA  . LYS A 1 167 ? -4.839  -5.721  -3.057  1.00 19.95 ? 168 LYS A CA  1 
ATOM   1319 C  C   . LYS A 1 167 ? -3.539  -5.343  -2.356  1.00 20.06 ? 168 LYS A C   1 
ATOM   1320 O  O   . LYS A 1 167 ? -3.150  -5.969  -1.382  1.00 20.27 ? 168 LYS A O   1 
ATOM   1321 C  CB  . LYS A 1 167 ? -4.516  -6.658  -4.231  1.00 20.22 ? 168 LYS A CB  1 
ATOM   1322 C  CG  . LYS A 1 167 ? -3.709  -7.914  -3.844  1.00 17.34 ? 168 LYS A CG  1 
ATOM   1323 C  CD  . LYS A 1 167 ? -3.519  -8.870  -5.092  1.00 20.92 ? 168 LYS A CD  1 
ATOM   1324 C  CE  . LYS A 1 167 ? -2.887  -10.202 -4.688  1.00 25.36 ? 168 LYS A CE  1 
ATOM   1325 N  NZ  . LYS A 1 167 ? -3.862  -11.302 -4.341  1.00 33.01 ? 168 LYS A NZ  1 
ATOM   1326 N  N   . THR A 1 168 ? -2.855  -4.332  -2.867  1.00 20.12 ? 169 THR A N   1 
ATOM   1327 C  CA  . THR A 1 168 ? -1.479  -4.089  -2.448  1.00 19.60 ? 169 THR A CA  1 
ATOM   1328 C  C   . THR A 1 168 ? -1.372  -2.740  -1.743  1.00 19.83 ? 169 THR A C   1 
ATOM   1329 O  O   . THR A 1 168 ? -2.293  -1.900  -1.824  1.00 20.60 ? 169 THR A O   1 
ATOM   1330 C  CB  . THR A 1 168 ? -0.496  -4.098  -3.687  1.00 19.51 ? 169 THR A CB  1 
ATOM   1331 O  OG1 . THR A 1 168 ? -1.059  -3.338  -4.744  1.00 20.68 ? 169 THR A OG1 1 
ATOM   1332 C  CG2 . THR A 1 168 ? -0.206  -5.512  -4.209  1.00 19.31 ? 169 THR A CG2 1 
ATOM   1333 N  N   . LYS A 1 169 ? -0.274  -2.565  -1.006  1.00 21.09 ? 170 LYS A N   1 
ATOM   1334 C  CA  . LYS A 1 169 ? 0.045   -1.322  -0.276  1.00 20.56 ? 170 LYS A CA  1 
ATOM   1335 C  C   . LYS A 1 169 ? -0.138  -0.036  -1.052  1.00 21.69 ? 170 LYS A C   1 
ATOM   1336 O  O   . LYS A 1 169 ? 0.301   0.078   -2.238  1.00 22.95 ? 170 LYS A O   1 
ATOM   1337 C  CB  . LYS A 1 169 ? 1.463   -1.392  0.197   1.00 21.10 ? 170 LYS A CB  1 
ATOM   1338 C  CG  . LYS A 1 169 ? 1.868   -0.192  1.075   1.00 22.85 ? 170 LYS A CG  1 
ATOM   1339 C  CD  . LYS A 1 169 ? 3.135   -0.490  1.829   1.00 25.35 ? 170 LYS A CD  1 
ATOM   1340 C  CE  . LYS A 1 169 ? 4.353   -0.278  0.941   1.00 33.02 ? 170 LYS A CE  1 
ATOM   1341 N  NZ  . LYS A 1 169 ? 5.573   -0.833  1.640   1.00 35.80 ? 170 LYS A NZ  1 
ATOM   1342 N  N   . GLY A 1 170 ? -0.828  0.918   -0.430  1.00 21.58 ? 171 GLY A N   1 
ATOM   1343 C  CA  . GLY A 1 170 ? -1.101  2.207   -1.058  1.00 21.15 ? 171 GLY A CA  1 
ATOM   1344 C  C   . GLY A 1 170 ? -2.272  2.313   -2.001  1.00 22.55 ? 171 GLY A C   1 
ATOM   1345 O  O   . GLY A 1 170 ? -2.618  3.458   -2.413  1.00 22.62 ? 171 GLY A O   1 
ATOM   1346 N  N   . LYS A 1 171 ? -2.928  1.178   -2.358  1.00 21.33 ? 172 LYS A N   1 
ATOM   1347 C  CA  . LYS A 1 171 ? -4.158  1.268   -3.170  1.00 20.02 ? 172 LYS A CA  1 
ATOM   1348 C  C   . LYS A 1 171 ? -5.377  1.753   -2.401  1.00 20.68 ? 172 LYS A C   1 
ATOM   1349 O  O   . LYS A 1 171 ? -5.554  1.412   -1.243  1.00 19.65 ? 172 LYS A O   1 
ATOM   1350 C  CB  . LYS A 1 171 ? -4.507  -0.051  -3.907  1.00 21.27 ? 172 LYS A CB  1 
ATOM   1351 C  CG  . LYS A 1 171 ? -3.419  -0.605  -4.831  1.00 21.92 ? 172 LYS A CG  1 
ATOM   1352 C  CD  . LYS A 1 171 ? -4.022  -0.948  -6.174  1.00 30.36 ? 172 LYS A CD  1 
ATOM   1353 C  CE  . LYS A 1 171 ? -3.004  -1.574  -7.124  1.00 32.63 ? 172 LYS A CE  1 
ATOM   1354 N  NZ  . LYS A 1 171 ? -3.683  -2.507  -8.109  1.00 34.00 ? 172 LYS A NZ  1 
ATOM   1355 N  N   . SER A 1 172 ? -6.219  2.545   -3.059  1.00 19.82 ? 173 SER A N   1 
ATOM   1356 C  CA  . SER A 1 172 ? -7.461  3.029   -2.495  1.00 21.72 ? 173 SER A CA  1 
ATOM   1357 C  C   . SER A 1 172 ? -8.573  2.877   -3.509  1.00 22.60 ? 173 SER A C   1 
ATOM   1358 O  O   . SER A 1 172 ? -8.330  2.854   -4.733  1.00 22.07 ? 173 SER A O   1 
ATOM   1359 C  CB  . SER A 1 172 ? -7.391  4.513   -2.055  1.00 22.16 ? 173 SER A CB  1 
ATOM   1360 O  OG  . SER A 1 172 ? -6.721  5.355   -2.981  1.00 23.85 ? 173 SER A OG  1 
ATOM   1361 N  N   . ALA A 1 173 ? -9.788  2.775   -2.998  1.00 22.38 ? 174 ALA A N   1 
ATOM   1362 C  CA  . ALA A 1 173 ? -10.961 2.795   -3.824  1.00 23.56 ? 174 ALA A CA  1 
ATOM   1363 C  C   . ALA A 1 173 ? -12.019 3.624   -3.123  1.00 24.79 ? 174 ALA A C   1 
ATOM   1364 O  O   . ALA A 1 173 ? -12.104 3.637   -1.862  1.00 23.32 ? 174 ALA A O   1 
ATOM   1365 C  CB  . ALA A 1 173 ? -11.484 1.383   -4.047  1.00 23.05 ? 174 ALA A CB  1 
ATOM   1366 N  N   . ASP A 1 174 ? -12.844 4.289   -3.928  1.00 24.08 ? 175 ASP A N   1 
ATOM   1367 C  CA  . ASP A 1 174 ? -14.025 4.945   -3.401  1.00 24.99 ? 175 ASP A CA  1 
ATOM   1368 C  C   . ASP A 1 174 ? -14.865 3.923   -2.668  1.00 24.12 ? 175 ASP A C   1 
ATOM   1369 O  O   . ASP A 1 174 ? -14.968 2.740   -3.075  1.00 22.01 ? 175 ASP A O   1 
ATOM   1370 C  CB  . ASP A 1 174 ? -14.893 5.603   -4.499  1.00 26.82 ? 175 ASP A CB  1 
ATOM   1371 C  CG  . ASP A 1 174 ? -14.140 6.604   -5.281  1.00 29.57 ? 175 ASP A CG  1 
ATOM   1372 O  OD1 . ASP A 1 174 ? -13.606 7.520   -4.626  1.00 33.94 ? 175 ASP A OD1 1 
ATOM   1373 O  OD2 . ASP A 1 174 ? -14.074 6.467   -6.545  1.00 37.35 ? 175 ASP A OD2 1 
ATOM   1374 N  N   . PHE A 1 175 ? -15.482 4.374   -1.583  1.00 21.10 ? 176 PHE A N   1 
ATOM   1375 C  CA  . PHE A 1 175 ? -16.230 3.430   -0.809  1.00 20.90 ? 176 PHE A CA  1 
ATOM   1376 C  C   . PHE A 1 175 ? -17.309 4.185   -0.073  1.00 20.65 ? 176 PHE A C   1 
ATOM   1377 O  O   . PHE A 1 175 ? -17.187 4.451   1.111   1.00 22.58 ? 176 PHE A O   1 
ATOM   1378 C  CB  . PHE A 1 175 ? -15.280 2.609   0.101   1.00 19.05 ? 176 PHE A CB  1 
ATOM   1379 C  CG  . PHE A 1 175 ? -15.895 1.337   0.586   1.00 19.49 ? 176 PHE A CG  1 
ATOM   1380 C  CD1 . PHE A 1 175 ? -16.252 0.307   -0.334  1.00 16.65 ? 176 PHE A CD1 1 
ATOM   1381 C  CD2 . PHE A 1 175 ? -16.194 1.178   1.938   1.00 19.84 ? 176 PHE A CD2 1 
ATOM   1382 C  CE1 . PHE A 1 175 ? -16.857 -0.853  0.111   1.00 20.92 ? 176 PHE A CE1 1 
ATOM   1383 C  CE2 . PHE A 1 175 ? -16.797 0.003   2.398   1.00 21.12 ? 176 PHE A CE2 1 
ATOM   1384 C  CZ  . PHE A 1 175 ? -17.143 -1.009  1.468   1.00 19.09 ? 176 PHE A CZ  1 
ATOM   1385 N  N   . THR A 1 176 ? -18.338 4.589   -0.805  1.00 19.06 ? 177 THR A N   1 
ATOM   1386 C  CA  . THR A 1 176 ? -19.412 5.381   -0.251  1.00 17.65 ? 177 THR A CA  1 
ATOM   1387 C  C   . THR A 1 176 ? -20.585 4.512   0.168   1.00 17.06 ? 177 THR A C   1 
ATOM   1388 O  O   . THR A 1 176 ? -20.714 3.306   -0.263  1.00 17.80 ? 177 THR A O   1 
ATOM   1389 C  CB  . THR A 1 176 ? -19.895 6.518   -1.240  1.00 18.84 ? 177 THR A CB  1 
ATOM   1390 O  OG1 . THR A 1 176 ? -20.325 5.921   -2.469  1.00 20.99 ? 177 THR A OG1 1 
ATOM   1391 C  CG2 . THR A 1 176 ? -18.817 7.533   -1.527  1.00 18.25 ? 177 THR A CG2 1 
ATOM   1392 N  N   . ASN A 1 177 ? -21.387 5.110   1.048   1.00 15.95 ? 178 ASN A N   1 
ATOM   1393 C  CA  . ASN A 1 177 ? -22.674 4.594   1.522   1.00 17.21 ? 178 ASN A CA  1 
ATOM   1394 C  C   . ASN A 1 177 ? -22.522 3.221   2.237   1.00 17.80 ? 178 ASN A C   1 
ATOM   1395 O  O   . ASN A 1 177 ? -23.449 2.415   2.202   1.00 19.60 ? 178 ASN A O   1 
ATOM   1396 C  CB  . ASN A 1 177 ? -23.679 4.481   0.353   1.00 17.67 ? 178 ASN A CB  1 
ATOM   1397 C  CG  . ASN A 1 177 ? -23.992 5.817   -0.279  1.00 18.49 ? 178 ASN A CG  1 
ATOM   1398 O  OD1 . ASN A 1 177 ? -24.808 6.593   0.248   1.00 20.96 ? 178 ASN A OD1 1 
ATOM   1399 N  ND2 . ASN A 1 177 ? -23.350 6.104   -1.385  1.00 17.81 ? 178 ASN A ND2 1 
ATOM   1400 N  N   . PHE A 1 178 ? -21.349 2.928   2.803   1.00 16.70 ? 179 PHE A N   1 
ATOM   1401 C  CA  . PHE A 1 178 ? -21.243 1.762   3.656   1.00 16.17 ? 179 PHE A CA  1 
ATOM   1402 C  C   . PHE A 1 178 ? -21.788 2.071   5.056   1.00 15.95 ? 179 PHE A C   1 
ATOM   1403 O  O   . PHE A 1 178 ? -21.366 3.049   5.649   1.00 16.40 ? 179 PHE A O   1 
ATOM   1404 C  CB  . PHE A 1 178 ? -19.794 1.202   3.724   1.00 16.26 ? 179 PHE A CB  1 
ATOM   1405 C  CG  . PHE A 1 178 ? -19.674 -0.020  4.626   1.00 15.89 ? 179 PHE A CG  1 
ATOM   1406 C  CD1 . PHE A 1 178 ? -20.015 -1.280  4.156   1.00 13.59 ? 179 PHE A CD1 1 
ATOM   1407 C  CD2 . PHE A 1 178 ? -19.327 0.121   5.982   1.00 16.20 ? 179 PHE A CD2 1 
ATOM   1408 C  CE1 . PHE A 1 178 ? -19.947 -2.380  4.977   1.00 15.38 ? 179 PHE A CE1 1 
ATOM   1409 C  CE2 . PHE A 1 178 ? -19.280 -1.008  6.809   1.00 18.33 ? 179 PHE A CE2 1 
ATOM   1410 C  CZ  . PHE A 1 178 ? -19.590 -2.234  6.325   1.00 13.33 ? 179 PHE A CZ  1 
ATOM   1411 N  N   . ASP A 1 179 ? -22.686 1.236   5.569   1.00 15.76 ? 180 ASP A N   1 
ATOM   1412 C  CA  . ASP A 1 179 ? -23.340 1.439   6.862   1.00 16.39 ? 180 ASP A CA  1 
ATOM   1413 C  C   . ASP A 1 179 ? -22.648 0.583   7.926   1.00 15.92 ? 180 ASP A C   1 
ATOM   1414 O  O   . ASP A 1 179 ? -22.804 -0.657  7.933   1.00 14.97 ? 180 ASP A O   1 
ATOM   1415 C  CB  . ASP A 1 179 ? -24.814 1.061   6.775   1.00 17.94 ? 180 ASP A CB  1 
ATOM   1416 C  CG  . ASP A 1 179 ? -25.614 1.491   7.987   1.00 20.08 ? 180 ASP A CG  1 
ATOM   1417 O  OD1 . ASP A 1 179 ? -25.057 1.607   9.094   1.00 23.70 ? 180 ASP A OD1 1 
ATOM   1418 O  OD2 . ASP A 1 179 ? -26.819 1.806   7.828   1.00 25.72 ? 180 ASP A OD2 1 
ATOM   1419 N  N   . PRO A 1 180 ? -21.827 1.214   8.784   1.00 16.21 ? 181 PRO A N   1 
ATOM   1420 C  CA  . PRO A 1 180 ? -21.059 0.352   9.745   1.00 16.67 ? 181 PRO A CA  1 
ATOM   1421 C  C   . PRO A 1 180 ? -21.955 -0.267  10.822  1.00 15.81 ? 181 PRO A C   1 
ATOM   1422 O  O   . PRO A 1 180 ? -21.497 -1.091  11.584  1.00 16.65 ? 181 PRO A O   1 
ATOM   1423 C  CB  . PRO A 1 180 ? -20.068 1.339   10.361  1.00 15.89 ? 181 PRO A CB  1 
ATOM   1424 C  CG  . PRO A 1 180 ? -20.846 2.673   10.294  1.00 17.07 ? 181 PRO A CG  1 
ATOM   1425 C  CD  . PRO A 1 180 ? -21.468 2.642   8.932   1.00 15.78 ? 181 PRO A CD  1 
ATOM   1426 N  N   . ARG A 1 181 ? -23.230 0.084   10.855  1.00 16.23 ? 182 ARG A N   1 
ATOM   1427 C  CA  . ARG A 1 181 ? -24.161 -0.543  11.828  1.00 16.46 ? 182 ARG A CA  1 
ATOM   1428 C  C   . ARG A 1 181 ? -24.346 -2.039  11.514  1.00 16.88 ? 182 ARG A C   1 
ATOM   1429 O  O   . ARG A 1 181 ? -24.691 -2.809  12.375  1.00 16.17 ? 182 ARG A O   1 
ATOM   1430 C  CB  . ARG A 1 181 ? -25.554 0.148   11.804  1.00 15.68 ? 182 ARG A CB  1 
ATOM   1431 C  CG  . ARG A 1 181 ? -25.541 1.619   12.223  1.00 16.70 ? 182 ARG A CG  1 
ATOM   1432 C  CD  . ARG A 1 181 ? -26.946 2.203   12.155  1.00 17.00 ? 182 ARG A CD  1 
ATOM   1433 N  NE  . ARG A 1 181 ? -27.340 2.356   10.754  1.00 16.17 ? 182 ARG A NE  1 
ATOM   1434 C  CZ  . ARG A 1 181 ? -28.402 3.059   10.359  1.00 20.98 ? 182 ARG A CZ  1 
ATOM   1435 N  NH1 . ARG A 1 181 ? -29.136 3.650   11.266  1.00 22.40 ? 182 ARG A NH1 1 
ATOM   1436 N  NH2 . ARG A 1 181 ? -28.744 3.135   9.066   1.00 20.02 ? 182 ARG A NH2 1 
ATOM   1437 N  N   . GLY A 1 182 ? -24.138 -2.421  10.255  1.00 17.24 ? 183 GLY A N   1 
ATOM   1438 C  CA  . GLY A 1 182 ? -24.172 -3.810  9.844   1.00 17.15 ? 183 GLY A CA  1 
ATOM   1439 C  C   . GLY A 1 182 ? -22.998 -4.651  10.347  1.00 17.75 ? 183 GLY A C   1 
ATOM   1440 O  O   . GLY A 1 182 ? -22.897 -5.831  10.056  1.00 18.41 ? 183 GLY A O   1 
ATOM   1441 N  N   . LEU A 1 183 ? -22.104 -4.042  11.108  1.00 18.05 ? 184 LEU A N   1 
ATOM   1442 C  CA  . LEU A 1 183 ? -20.978 -4.756  11.646  1.00 17.03 ? 184 LEU A CA  1 
ATOM   1443 C  C   . LEU A 1 183 ? -21.148 -4.994  13.133  1.00 17.11 ? 184 LEU A C   1 
ATOM   1444 O  O   . LEU A 1 183 ? -20.275 -5.605  13.760  1.00 17.61 ? 184 LEU A O   1 
ATOM   1445 C  CB  . LEU A 1 183 ? -19.670 -4.015  11.352  1.00 17.20 ? 184 LEU A CB  1 
ATOM   1446 C  CG  . LEU A 1 183 ? -19.353 -3.813  9.859   1.00 15.25 ? 184 LEU A CG  1 
ATOM   1447 C  CD1 . LEU A 1 183 ? -18.138 -3.030  9.782   1.00 15.37 ? 184 LEU A CD1 1 
ATOM   1448 C  CD2 . LEU A 1 183 ? -19.149 -5.115  9.108   1.00 14.39 ? 184 LEU A CD2 1 
ATOM   1449 N  N   . LEU A 1 184 ? -22.258 -4.527  13.709  1.00 16.59 ? 185 LEU A N   1 
ATOM   1450 C  CA  . LEU A 1 184 ? -22.410 -4.553  15.197  1.00 15.33 ? 185 LEU A CA  1 
ATOM   1451 C  C   . LEU A 1 184 ? -23.038 -5.863  15.623  1.00 17.51 ? 185 LEU A C   1 
ATOM   1452 O  O   . LEU A 1 184 ? -23.884 -6.450  14.897  1.00 19.00 ? 185 LEU A O   1 
ATOM   1453 C  CB  . LEU A 1 184 ? -23.265 -3.361  15.704  1.00 13.97 ? 185 LEU A CB  1 
ATOM   1454 C  CG  . LEU A 1 184 ? -22.678 -1.996  15.302  1.00 17.04 ? 185 LEU A CG  1 
ATOM   1455 C  CD1 . LEU A 1 184 ? -23.537 -0.783  15.801  1.00 17.74 ? 185 LEU A CD1 1 
ATOM   1456 C  CD2 . LEU A 1 184 ? -21.213 -1.870  15.701  1.00 14.18 ? 185 LEU A CD2 1 
ATOM   1457 N  N   . PRO A 1 185 ? -22.646 -6.346  16.792  1.00 15.44 ? 186 PRO A N   1 
ATOM   1458 C  CA  . PRO A 1 185 ? -23.422 -7.479  17.270  1.00 15.60 ? 186 PRO A CA  1 
ATOM   1459 C  C   . PRO A 1 185 ? -24.700 -6.925  17.900  1.00 16.53 ? 186 PRO A C   1 
ATOM   1460 O  O   . PRO A 1 185 ? -24.907 -5.722  17.968  1.00 15.12 ? 186 PRO A O   1 
ATOM   1461 C  CB  . PRO A 1 185 ? -22.529 -8.066  18.363  1.00 14.51 ? 186 PRO A CB  1 
ATOM   1462 C  CG  . PRO A 1 185 ? -21.860 -6.869  18.947  1.00 14.35 ? 186 PRO A CG  1 
ATOM   1463 C  CD  . PRO A 1 185 ? -21.615 -5.921  17.739  1.00 13.49 ? 186 PRO A CD  1 
ATOM   1464 N  N   . GLU A 1 186 ? -25.501 -7.836  18.436  1.00 17.74 ? 187 GLU A N   1 
ATOM   1465 C  CA  . GLU A 1 186 ? -26.743 -7.530  19.101  1.00 18.13 ? 187 GLU A CA  1 
ATOM   1466 C  C   . GLU A 1 186 ? -26.532 -6.804  20.392  1.00 17.69 ? 187 GLU A C   1 
ATOM   1467 O  O   . GLU A 1 186 ? -27.164 -5.770  20.643  1.00 18.41 ? 187 GLU A O   1 
ATOM   1468 C  CB  . GLU A 1 186 ? -27.419 -8.876  19.370  1.00 18.48 ? 187 GLU A CB  1 
ATOM   1469 C  CG  . GLU A 1 186 ? -28.775 -8.825  19.816  1.00 22.77 ? 187 GLU A CG  1 
ATOM   1470 C  CD  . GLU A 1 186 ? -29.354 -10.229 20.000  1.00 24.94 ? 187 GLU A CD  1 
ATOM   1471 O  OE1 . GLU A 1 186 ? -29.284 -11.076 19.046  1.00 23.70 ? 187 GLU A OE1 1 
ATOM   1472 O  OE2 . GLU A 1 186 ? -29.886 -10.429 21.121  1.00 26.13 ? 187 GLU A OE2 1 
ATOM   1473 N  N   . SER A 1 187 ? -25.675 -7.328  21.262  1.00 16.36 ? 188 SER A N   1 
ATOM   1474 C  CA  . SER A 1 187 ? -25.555 -6.701  22.591  1.00 16.35 ? 188 SER A CA  1 
ATOM   1475 C  C   . SER A 1 187 ? -24.481 -5.623  22.531  1.00 16.81 ? 188 SER A C   1 
ATOM   1476 O  O   . SER A 1 187 ? -23.542 -5.780  21.786  1.00 17.09 ? 188 SER A O   1 
ATOM   1477 C  CB  . SER A 1 187 ? -25.166 -7.756  23.635  1.00 15.39 ? 188 SER A CB  1 
ATOM   1478 O  OG  . SER A 1 187 ? -24.979 -7.204  24.937  1.00 15.72 ? 188 SER A OG  1 
ATOM   1479 N  N   . LEU A 1 188 ? -24.609 -4.550  23.313  1.00 16.39 ? 189 LEU A N   1 
ATOM   1480 C  CA  . LEU A 1 188 ? -23.516 -3.568  23.452  1.00 16.25 ? 189 LEU A CA  1 
ATOM   1481 C  C   . LEU A 1 188 ? -22.817 -3.655  24.822  1.00 16.12 ? 189 LEU A C   1 
ATOM   1482 O  O   . LEU A 1 188 ? -22.171 -2.689  25.251  1.00 18.28 ? 189 LEU A O   1 
ATOM   1483 C  CB  . LEU A 1 188 ? -24.049 -2.134  23.177  1.00 16.62 ? 189 LEU A CB  1 
ATOM   1484 C  CG  . LEU A 1 188 ? -24.485 -1.748  21.759  1.00 14.43 ? 189 LEU A CG  1 
ATOM   1485 C  CD1 . LEU A 1 188 ? -24.912 -0.291  21.664  1.00 17.56 ? 189 LEU A CD1 1 
ATOM   1486 C  CD2 . LEU A 1 188 ? -23.417 -2.035  20.703  1.00 19.02 ? 189 LEU A CD2 1 
ATOM   1487 N  N   . ASP A 1 189 ? -22.971 -4.771  25.534  1.00 15.43 ? 190 ASP A N   1 
ATOM   1488 C  CA  . ASP A 1 189 ? -22.221 -4.961  26.773  1.00 15.32 ? 190 ASP A CA  1 
ATOM   1489 C  C   . ASP A 1 189 ? -20.742 -4.936  26.395  1.00 14.86 ? 190 ASP A C   1 
ATOM   1490 O  O   . ASP A 1 189 ? -20.384 -5.385  25.291  1.00 13.94 ? 190 ASP A O   1 
ATOM   1491 C  CB  . ASP A 1 189 ? -22.557 -6.280  27.425  1.00 14.96 ? 190 ASP A CB  1 
ATOM   1492 C  CG  . ASP A 1 189 ? -23.958 -6.296  28.022  1.00 20.87 ? 190 ASP A CG  1 
ATOM   1493 O  OD1 . ASP A 1 189 ? -24.542 -5.229  28.291  1.00 21.08 ? 190 ASP A OD1 1 
ATOM   1494 O  OD2 . ASP A 1 189 ? -24.473 -7.406  28.196  1.00 24.35 ? 190 ASP A OD2 1 
ATOM   1495 N  N   . TYR A 1 190 ? -19.906 -4.358  27.271  1.00 14.66 ? 191 TYR A N   1 
ATOM   1496 C  CA  . TYR A 1 190 ? -18.518 -4.091  26.925  1.00 14.13 ? 191 TYR A CA  1 
ATOM   1497 C  C   . TYR A 1 190 ? -17.593 -4.180  28.161  1.00 14.28 ? 191 TYR A C   1 
ATOM   1498 O  O   . TYR A 1 190 ? -18.087 -4.178  29.294  1.00 14.80 ? 191 TYR A O   1 
ATOM   1499 C  CB  . TYR A 1 190 ? -18.442 -2.696  26.227  1.00 13.30 ? 191 TYR A CB  1 
ATOM   1500 C  CG  . TYR A 1 190 ? -18.854 -1.526  27.159  1.00 14.17 ? 191 TYR A CG  1 
ATOM   1501 C  CD1 . TYR A 1 190 ? -17.925 -0.969  28.069  1.00 14.67 ? 191 TYR A CD1 1 
ATOM   1502 C  CD2 . TYR A 1 190 ? -20.150 -0.997  27.120  1.00 13.19 ? 191 TYR A CD2 1 
ATOM   1503 C  CE1 . TYR A 1 190 ? -18.281 0.047   28.936  1.00 17.29 ? 191 TYR A CE1 1 
ATOM   1504 C  CE2 . TYR A 1 190 ? -20.530 0.076   27.996  1.00 19.68 ? 191 TYR A CE2 1 
ATOM   1505 C  CZ  . TYR A 1 190 ? -19.576 0.569   28.892  1.00 18.76 ? 191 TYR A CZ  1 
ATOM   1506 O  OH  . TYR A 1 190 ? -19.894 1.575   29.711  1.00 13.20 ? 191 TYR A OH  1 
ATOM   1507 N  N   . TRP A 1 191 ? -16.283 -4.315  27.909  1.00 12.79 ? 192 TRP A N   1 
ATOM   1508 C  CA  . TRP A 1 191 ? -15.213 -4.118  28.857  1.00 12.36 ? 192 TRP A CA  1 
ATOM   1509 C  C   . TRP A 1 191 ? -14.563 -2.798  28.424  1.00 12.48 ? 192 TRP A C   1 
ATOM   1510 O  O   . TRP A 1 191 ? -14.630 -2.400  27.244  1.00 12.76 ? 192 TRP A O   1 
ATOM   1511 C  CB  . TRP A 1 191 ? -14.144 -5.266  28.791  1.00 12.66 ? 192 TRP A CB  1 
ATOM   1512 C  CG  . TRP A 1 191 ? -14.684 -6.659  29.137  1.00 13.47 ? 192 TRP A CG  1 
ATOM   1513 C  CD1 . TRP A 1 191 ? -14.968 -7.131  30.395  1.00 12.66 ? 192 TRP A CD1 1 
ATOM   1514 C  CD2 . TRP A 1 191 ? -14.942 -7.750  28.233  1.00 12.87 ? 192 TRP A CD2 1 
ATOM   1515 N  NE1 . TRP A 1 191 ? -15.422 -8.431  30.315  1.00 13.62 ? 192 TRP A NE1 1 
ATOM   1516 C  CE2 . TRP A 1 191 ? -15.454 -8.818  29.006  1.00 15.41 ? 192 TRP A CE2 1 
ATOM   1517 C  CE3 . TRP A 1 191 ? -14.871 -7.896  26.832  1.00 14.55 ? 192 TRP A CE3 1 
ATOM   1518 C  CZ2 . TRP A 1 191 ? -15.809 -10.048 28.449  1.00 12.94 ? 192 TRP A CZ2 1 
ATOM   1519 C  CZ3 . TRP A 1 191 ? -15.245 -9.129  26.268  1.00 12.46 ? 192 TRP A CZ3 1 
ATOM   1520 C  CH2 . TRP A 1 191 ? -15.674 -10.192 27.086  1.00 13.17 ? 192 TRP A CH2 1 
ATOM   1521 N  N   . THR A 1 192 ? -13.943 -2.109  29.367  1.00 11.28 ? 193 THR A N   1 
ATOM   1522 C  CA  . THR A 1 192 ? -13.309 -0.862  29.070  1.00 12.29 ? 193 THR A CA  1 
ATOM   1523 C  C   . THR A 1 192 ? -12.074 -0.735  29.941  1.00 11.99 ? 193 THR A C   1 
ATOM   1524 O  O   . THR A 1 192 ? -12.070 -1.186  31.067  1.00 12.35 ? 193 THR A O   1 
ATOM   1525 C  CB  . THR A 1 192 ? -14.310 0.385   29.103  1.00 10.75 ? 193 THR A CB  1 
ATOM   1526 O  OG1 . THR A 1 192 ? -13.656 1.594   28.642  1.00 9.90  ? 193 THR A OG1 1 
ATOM   1527 C  CG2 . THR A 1 192 ? -14.903 0.615   30.470  1.00 12.21 ? 193 THR A CG2 1 
ATOM   1528 N  N   . TYR A 1 193 ? -11.011 -0.217  29.350  1.00 12.46 ? 194 TYR A N   1 
ATOM   1529 C  CA  . TYR A 1 193 ? -9.758  0.093   30.069  1.00 11.65 ? 194 TYR A CA  1 
ATOM   1530 C  C   . TYR A 1 193 ? -9.019  1.174   29.260  1.00 11.71 ? 194 TYR A C   1 
ATOM   1531 O  O   . TYR A 1 193 ? -9.295  1.303   28.036  1.00 12.69 ? 194 TYR A O   1 
ATOM   1532 C  CB  . TYR A 1 193 ? -8.935  -1.231  30.256  1.00 12.56 ? 194 TYR A CB  1 
ATOM   1533 C  CG  . TYR A 1 193 ? -8.219  -1.641  28.979  1.00 9.85  ? 194 TYR A CG  1 
ATOM   1534 C  CD1 . TYR A 1 193 ? -8.884  -2.354  27.971  1.00 8.83  ? 194 TYR A CD1 1 
ATOM   1535 C  CD2 . TYR A 1 193 ? -6.934  -1.245  28.761  1.00 12.33 ? 194 TYR A CD2 1 
ATOM   1536 C  CE1 . TYR A 1 193 ? -8.268  -2.681  26.775  1.00 6.04  ? 194 TYR A CE1 1 
ATOM   1537 C  CE2 . TYR A 1 193 ? -6.265  -1.586  27.560  1.00 10.39 ? 194 TYR A CE2 1 
ATOM   1538 C  CZ  . TYR A 1 193 ? -6.939  -2.335  26.615  1.00 7.64  ? 194 TYR A CZ  1 
ATOM   1539 O  OH  . TYR A 1 193 ? -6.272  -2.611  25.476  1.00 11.18 ? 194 TYR A OH  1 
ATOM   1540 N  N   . PRO A 1 194 ? -8.102  1.966   29.898  1.00 10.57 ? 195 PRO A N   1 
ATOM   1541 C  CA  . PRO A 1 194 ? -7.253  2.944   29.245  1.00 11.34 ? 195 PRO A CA  1 
ATOM   1542 C  C   . PRO A 1 194 ? -6.014  2.316   28.563  1.00 11.01 ? 195 PRO A C   1 
ATOM   1543 O  O   . PRO A 1 194 ? -5.279  1.558   29.193  1.00 10.59 ? 195 PRO A O   1 
ATOM   1544 C  CB  . PRO A 1 194 ? -6.779  3.866   30.407  1.00 11.85 ? 195 PRO A CB  1 
ATOM   1545 C  CG  . PRO A 1 194 ? -6.846  3.041   31.653  1.00 12.22 ? 195 PRO A CG  1 
ATOM   1546 C  CD  . PRO A 1 194 ? -7.830  1.872   31.360  1.00 11.16 ? 195 PRO A CD  1 
ATOM   1547 N  N   . GLY A 1 195 ? -5.784  2.624   27.300  1.00 10.41 ? 196 GLY A N   1 
ATOM   1548 C  CA  . GLY A 1 195 ? -4.685  1.956   26.621  1.00 11.04 ? 196 GLY A CA  1 
ATOM   1549 C  C   . GLY A 1 195 ? -4.125  2.822   25.511  1.00 11.67 ? 196 GLY A C   1 
ATOM   1550 O  O   . GLY A 1 195 ? -4.054  4.030   25.670  1.00 9.93  ? 196 GLY A O   1 
ATOM   1551 N  N   . SER A 1 196 ? -3.703  2.171   24.424  1.00 10.35 ? 197 SER A N   1 
ATOM   1552 C  CA  . SER A 1 196 ? -2.864  2.765   23.400  1.00 9.59  ? 197 SER A CA  1 
ATOM   1553 C  C   . SER A 1 196 ? -3.344  2.413   21.984  1.00 10.60 ? 197 SER A C   1 
ATOM   1554 O  O   . SER A 1 196 ? -4.183  1.503   21.824  1.00 10.17 ? 197 SER A O   1 
ATOM   1555 C  CB  . SER A 1 196 ? -1.416  2.294   23.570  1.00 11.20 ? 197 SER A CB  1 
ATOM   1556 O  OG  . SER A 1 196 ? -1.199  0.976   23.032  1.00 10.81 ? 197 SER A OG  1 
ATOM   1557 N  N   . LEU A 1 197 ? -2.801  3.091   20.958  1.00 10.25 ? 198 LEU A N   1 
ATOM   1558 C  CA  . LEU A 1 197 ? -2.829  2.484   19.646  1.00 11.36 ? 198 LEU A CA  1 
ATOM   1559 C  C   . LEU A 1 197 ? -2.097  1.126   19.724  1.00 11.62 ? 198 LEU A C   1 
ATOM   1560 O  O   . LEU A 1 197 ? -1.107  0.962   20.485  1.00 11.44 ? 198 LEU A O   1 
ATOM   1561 C  CB  . LEU A 1 197 ? -2.138  3.352   18.610  1.00 11.44 ? 198 LEU A CB  1 
ATOM   1562 C  CG  . LEU A 1 197 ? -2.442  4.809   18.244  1.00 15.69 ? 198 LEU A CG  1 
ATOM   1563 C  CD1 . LEU A 1 197 ? -2.092  5.009   16.794  1.00 18.06 ? 198 LEU A CD1 1 
ATOM   1564 C  CD2 . LEU A 1 197 ? -3.803  5.391   18.617  1.00 11.76 ? 198 LEU A CD2 1 
ATOM   1565 N  N   . THR A 1 198 ? -2.531  0.170   18.911  1.00 8.40  ? 199 THR A N   1 
ATOM   1566 C  CA  . THR A 1 198 ? -1.882  -1.112  18.905  1.00 10.13 ? 199 THR A CA  1 
ATOM   1567 C  C   . THR A 1 198 ? -0.863  -1.208  17.786  1.00 10.34 ? 199 THR A C   1 
ATOM   1568 O  O   . THR A 1 198 ? -0.188  -2.237  17.656  1.00 12.62 ? 199 THR A O   1 
ATOM   1569 C  CB  . THR A 1 198 ? -2.873  -2.269  18.707  1.00 9.60  ? 199 THR A CB  1 
ATOM   1570 O  OG1 . THR A 1 198 ? -3.525  -2.138  17.429  1.00 8.90  ? 199 THR A OG1 1 
ATOM   1571 C  CG2 . THR A 1 198 ? -3.864  -2.273  19.830  1.00 8.29  ? 199 THR A CG2 1 
ATOM   1572 N  N   . THR A 1 199 ? -0.780  -0.185  16.963  1.00 9.44  ? 200 THR A N   1 
ATOM   1573 C  CA  . THR A 1 199 ? 0.308   -0.078  16.029  1.00 10.78 ? 200 THR A CA  1 
ATOM   1574 C  C   . THR A 1 199 ? 1.146   1.170   16.341  1.00 11.47 ? 200 THR A C   1 
ATOM   1575 O  O   . THR A 1 199 ? 0.628   2.160   16.904  1.00 10.33 ? 200 THR A O   1 
ATOM   1576 C  CB  . THR A 1 199 ? -0.169  0.066   14.536  1.00 12.20 ? 200 THR A CB  1 
ATOM   1577 O  OG1 . THR A 1 199 ? -0.670  1.396   14.298  1.00 13.06 ? 200 THR A OG1 1 
ATOM   1578 C  CG2 . THR A 1 199 ? -1.171  -0.960  14.170  1.00 9.30  ? 200 THR A CG2 1 
ATOM   1579 N  N   . PRO A 1 200 ? 2.406   1.176   15.846  1.00 13.30 ? 201 PRO A N   1 
ATOM   1580 C  CA  . PRO A 1 200 ? 3.161   2.446   15.959  1.00 13.49 ? 201 PRO A CA  1 
ATOM   1581 C  C   . PRO A 1 200 ? 2.257   3.558   15.407  1.00 13.53 ? 201 PRO A C   1 
ATOM   1582 O  O   . PRO A 1 200 ? 1.538   3.298   14.434  1.00 16.52 ? 201 PRO A O   1 
ATOM   1583 C  CB  . PRO A 1 200 ? 4.352   2.197   15.048  1.00 11.89 ? 201 PRO A CB  1 
ATOM   1584 C  CG  . PRO A 1 200 ? 4.621   0.704   15.200  1.00 16.24 ? 201 PRO A CG  1 
ATOM   1585 C  CD  . PRO A 1 200 ? 3.180   0.122   15.166  1.00 11.41 ? 201 PRO A CD  1 
ATOM   1586 N  N   . PRO A 1 201 ? 2.300   4.791   15.948  1.00 13.90 ? 202 PRO A N   1 
ATOM   1587 C  CA  . PRO A 1 201 ? 3.207   5.286   17.007  1.00 14.00 ? 202 PRO A CA  1 
ATOM   1588 C  C   . PRO A 1 201 ? 2.861   4.835   18.441  1.00 12.85 ? 202 PRO A C   1 
ATOM   1589 O  O   . PRO A 1 201 ? 3.577   5.208   19.385  1.00 11.13 ? 202 PRO A O   1 
ATOM   1590 C  CB  . PRO A 1 201 ? 3.143   6.809   16.828  1.00 15.16 ? 202 PRO A CB  1 
ATOM   1591 C  CG  . PRO A 1 201 ? 1.744   7.063   16.321  1.00 15.01 ? 202 PRO A CG  1 
ATOM   1592 C  CD  . PRO A 1 201 ? 1.436   5.868   15.419  1.00 12.53 ? 202 PRO A CD  1 
ATOM   1593 N  N   . LEU A 1 202 ? 1.870   3.929   18.601  1.00 13.24 ? 203 LEU A N   1 
ATOM   1594 C  CA  . LEU A 1 202 ? 1.605   3.308   19.951  1.00 13.59 ? 203 LEU A CA  1 
ATOM   1595 C  C   . LEU A 1 202 ? 1.249   4.323   21.040  1.00 12.94 ? 203 LEU A C   1 
ATOM   1596 O  O   . LEU A 1 202 ? 1.432   4.073   22.279  1.00 12.86 ? 203 LEU A O   1 
ATOM   1597 C  CB  . LEU A 1 202 ? 2.785   2.408   20.415  1.00 13.35 ? 203 LEU A CB  1 
ATOM   1598 C  CG  . LEU A 1 202 ? 3.060   1.182   19.526  1.00 15.46 ? 203 LEU A CG  1 
ATOM   1599 C  CD1 . LEU A 1 202 ? 4.337   0.590   19.905  1.00 13.84 ? 203 LEU A CD1 1 
ATOM   1600 C  CD2 . LEU A 1 202 ? 1.947   0.083   19.558  1.00 13.25 ? 203 LEU A CD2 1 
ATOM   1601 N  N   . LEU A 1 203 ? 0.660   5.429   20.591  1.00 12.78 ? 204 LEU A N   1 
ATOM   1602 C  CA  . LEU A 1 203 ? 0.385   6.597   21.464  1.00 14.28 ? 204 LEU A CA  1 
ATOM   1603 C  C   . LEU A 1 203 ? -0.642  6.208   22.515  1.00 13.92 ? 204 LEU A C   1 
ATOM   1604 O  O   . LEU A 1 203 ? -1.632  5.473   22.240  1.00 13.38 ? 204 LEU A O   1 
ATOM   1605 C  CB  . LEU A 1 203 ? -0.069  7.835   20.645  1.00 14.40 ? 204 LEU A CB  1 
ATOM   1606 C  CG  . LEU A 1 203 ? 0.949   8.426   19.672  1.00 15.66 ? 204 LEU A CG  1 
ATOM   1607 C  CD1 . LEU A 1 203 ? 0.389   9.617   18.872  1.00 18.87 ? 204 LEU A CD1 1 
ATOM   1608 C  CD2 . LEU A 1 203 ? 2.223   8.842   20.397  1.00 18.81 ? 204 LEU A CD2 1 
ATOM   1609 N  N   . GLU A 1 204 ? -0.406  6.658   23.734  1.00 12.63 ? 205 GLU A N   1 
ATOM   1610 C  CA  . GLU A 1 204 ? -1.213  6.223   24.817  1.00 13.08 ? 205 GLU A CA  1 
ATOM   1611 C  C   . GLU A 1 204 ? -2.437  7.148   25.010  1.00 12.96 ? 205 GLU A C   1 
ATOM   1612 O  O   . GLU A 1 204 ? -2.602  7.823   26.047  1.00 12.49 ? 205 GLU A O   1 
ATOM   1613 C  CB  . GLU A 1 204 ? -0.329  6.114   26.089  1.00 13.71 ? 205 GLU A CB  1 
ATOM   1614 C  CG  . GLU A 1 204 ? 0.579   4.857   25.940  1.00 14.94 ? 205 GLU A CG  1 
ATOM   1615 C  CD  . GLU A 1 204 ? 1.392   4.505   27.182  1.00 15.47 ? 205 GLU A CD  1 
ATOM   1616 O  OE1 . GLU A 1 204 ? 1.709   5.416   27.920  1.00 16.90 ? 205 GLU A OE1 1 
ATOM   1617 O  OE2 . GLU A 1 204 ? 1.746   3.332   27.393  1.00 14.88 ? 205 GLU A OE2 1 
ATOM   1618 N  N   . CYS A 1 205 ? -3.351  7.100   24.057  1.00 11.16 ? 206 CYS A N   1 
ATOM   1619 C  CA  . CYS A 1 205 ? -4.400  8.112   23.953  1.00 10.26 ? 206 CYS A CA  1 
ATOM   1620 C  C   . CYS A 1 205 ? -5.779  7.445   23.839  1.00 10.32 ? 206 CYS A C   1 
ATOM   1621 O  O   . CYS A 1 205 ? -6.744  8.119   23.515  1.00 10.37 ? 206 CYS A O   1 
ATOM   1622 C  CB  . CYS A 1 205 ? -4.197  8.955   22.710  1.00 10.68 ? 206 CYS A CB  1 
ATOM   1623 S  SG  . CYS A 1 205 ? -4.092  7.984   21.098  1.00 12.92 ? 206 CYS A SG  1 
ATOM   1624 N  N   . VAL A 1 206 ? -5.856  6.139   24.075  1.00 10.85 ? 207 VAL A N   1 
ATOM   1625 C  CA  . VAL A 1 206 ? -7.102  5.401   23.768  1.00 11.22 ? 207 VAL A CA  1 
ATOM   1626 C  C   . VAL A 1 206 ? -7.933  4.983   24.972  1.00 11.27 ? 207 VAL A C   1 
ATOM   1627 O  O   . VAL A 1 206 ? -7.424  4.312   25.832  1.00 12.35 ? 207 VAL A O   1 
ATOM   1628 C  CB  . VAL A 1 206 ? -6.864  4.114   22.978  1.00 10.51 ? 207 VAL A CB  1 
ATOM   1629 C  CG1 . VAL A 1 206 ? -8.302  3.484   22.586  1.00 9.79  ? 207 VAL A CG1 1 
ATOM   1630 C  CG2 . VAL A 1 206 ? -6.064  4.392   21.662  1.00 11.94 ? 207 VAL A CG2 1 
ATOM   1631 N  N   . THR A 1 207 ? -9.246  5.252   24.948  1.00 10.87 ? 208 THR A N   1 
ATOM   1632 C  CA  . THR A 1 207 ? -10.175 4.506   25.797  1.00 11.27 ? 208 THR A CA  1 
ATOM   1633 C  C   . THR A 1 207 ? -10.731 3.328   24.977  1.00 11.06 ? 208 THR A C   1 
ATOM   1634 O  O   . THR A 1 207 ? -11.442 3.545   23.992  1.00 10.78 ? 208 THR A O   1 
ATOM   1635 C  CB  . THR A 1 207 ? -11.379 5.440   26.332  1.00 10.73 ? 208 THR A CB  1 
ATOM   1636 O  OG1 . THR A 1 207 ? -10.864 6.432   27.217  1.00 13.17 ? 208 THR A OG1 1 
ATOM   1637 C  CG2 . THR A 1 207 ? -12.491 4.636   27.010  1.00 11.13 ? 208 THR A CG2 1 
ATOM   1638 N  N   . TRP A 1 208 ? -10.402 2.104   25.400  1.00 9.84  ? 209 TRP A N   1 
ATOM   1639 C  CA  . TRP A 1 208 ? -10.714 0.889   24.697  1.00 10.75 ? 209 TRP A CA  1 
ATOM   1640 C  C   . TRP A 1 208 ? -12.081 0.455   25.187  1.00 10.50 ? 209 TRP A C   1 
ATOM   1641 O  O   . TRP A 1 208 ? -12.358 0.495   26.370  1.00 10.69 ? 209 TRP A O   1 
ATOM   1642 C  CB  . TRP A 1 208 ? -9.672  -0.275  24.944  1.00 7.89  ? 209 TRP A CB  1 
ATOM   1643 C  CG  . TRP A 1 208 ? -8.623  -0.139  23.978  1.00 8.55  ? 209 TRP A CG  1 
ATOM   1644 C  CD1 . TRP A 1 208 ? -7.409  0.503   24.154  1.00 7.99  ? 209 TRP A CD1 1 
ATOM   1645 C  CD2 . TRP A 1 208 ? -8.710  -0.481  22.570  1.00 10.71 ? 209 TRP A CD2 1 
ATOM   1646 N  NE1 . TRP A 1 208 ? -6.730  0.522   22.935  1.00 10.21 ? 209 TRP A NE1 1 
ATOM   1647 C  CE2 . TRP A 1 208 ? -7.473  -0.136  21.980  1.00 7.51  ? 209 TRP A CE2 1 
ATOM   1648 C  CE3 . TRP A 1 208 ? -9.689  -1.110  21.777  1.00 6.75  ? 209 TRP A CE3 1 
ATOM   1649 C  CZ2 . TRP A 1 208 ? -7.220  -0.314  20.618  1.00 5.52  ? 209 TRP A CZ2 1 
ATOM   1650 C  CZ3 . TRP A 1 208 ? -9.371  -1.392  20.416  1.00 7.14  ? 209 TRP A CZ3 1 
ATOM   1651 C  CH2 . TRP A 1 208 ? -8.146  -0.987  19.863  1.00 5.38  ? 209 TRP A CH2 1 
ATOM   1652 N  N   . ILE A 1 209 ? -12.954 0.204   24.239  1.00 11.45 ? 210 ILE A N   1 
ATOM   1653 C  CA  . ILE A 1 209 ? -14.328 -0.244  24.558  1.00 11.04 ? 210 ILE A CA  1 
ATOM   1654 C  C   . ILE A 1 209 ? -14.412 -1.528  23.734  1.00 11.12 ? 210 ILE A C   1 
ATOM   1655 O  O   . ILE A 1 209 ? -14.428 -1.483  22.542  1.00 12.42 ? 210 ILE A O   1 
ATOM   1656 C  CB  . ILE A 1 209 ? -15.428 0.812   24.217  1.00 10.04 ? 210 ILE A CB  1 
ATOM   1657 C  CG1 . ILE A 1 209 ? -15.175 2.108   25.008  1.00 13.31 ? 210 ILE A CG1 1 
ATOM   1658 C  CG2 . ILE A 1 209 ? -16.884 0.222   24.595  1.00 11.75 ? 210 ILE A CG2 1 
ATOM   1659 C  CD1 . ILE A 1 209 ? -16.021 3.311   24.587  1.00 11.74 ? 210 ILE A CD1 1 
ATOM   1660 N  N   . VAL A 1 210 ? -14.308 -2.666  24.391  1.00 11.46 ? 211 VAL A N   1 
ATOM   1661 C  CA  . VAL A 1 210 ? -14.269 -3.982  23.701  1.00 11.64 ? 211 VAL A CA  1 
ATOM   1662 C  C   . VAL A 1 210 ? -15.639 -4.667  23.960  1.00 11.49 ? 211 VAL A C   1 
ATOM   1663 O  O   . VAL A 1 210 ? -15.981 -4.897  25.090  1.00 10.29 ? 211 VAL A O   1 
ATOM   1664 C  CB  . VAL A 1 210 ? -13.078 -4.874  24.167  1.00 12.80 ? 211 VAL A CB  1 
ATOM   1665 C  CG1 . VAL A 1 210 ? -13.031 -6.236  23.415  1.00 11.06 ? 211 VAL A CG1 1 
ATOM   1666 C  CG2 . VAL A 1 210 ? -11.701 -4.140  23.927  1.00 8.71  ? 211 VAL A CG2 1 
ATOM   1667 N  N   . LEU A 1 211 ? -16.391 -4.972  22.888  1.00 11.58 ? 212 LEU A N   1 
ATOM   1668 C  CA  . LEU A 1 211 ? -17.674 -5.732  23.014  1.00 12.70 ? 212 LEU A CA  1 
ATOM   1669 C  C   . LEU A 1 211 ? -17.523 -7.191  23.422  1.00 12.77 ? 212 LEU A C   1 
ATOM   1670 O  O   . LEU A 1 211 ? -16.764 -7.924  22.865  1.00 12.79 ? 212 LEU A O   1 
ATOM   1671 C  CB  . LEU A 1 211 ? -18.544 -5.615  21.769  1.00 10.71 ? 212 LEU A CB  1 
ATOM   1672 C  CG  . LEU A 1 211 ? -18.971 -4.175  21.356  1.00 14.15 ? 212 LEU A CG  1 
ATOM   1673 C  CD1 . LEU A 1 211 ? -19.949 -4.218  20.223  1.00 15.88 ? 212 LEU A CD1 1 
ATOM   1674 C  CD2 . LEU A 1 211 ? -19.568 -3.279  22.481  1.00 10.50 ? 212 LEU A CD2 1 
ATOM   1675 N  N   . LYS A 1 212 ? -18.335 -7.595  24.394  1.00 14.62 ? 213 LYS A N   1 
ATOM   1676 C  CA  . LYS A 1 212 ? -18.398 -8.999  24.872  1.00 15.86 ? 213 LYS A CA  1 
ATOM   1677 C  C   . LYS A 1 212 ? -18.852 -9.927  23.784  1.00 14.96 ? 213 LYS A C   1 
ATOM   1678 O  O   . LYS A 1 212 ? -18.313 -11.042 23.617  1.00 14.51 ? 213 LYS A O   1 
ATOM   1679 C  CB  . LYS A 1 212 ? -19.317 -9.056  26.118  1.00 16.28 ? 213 LYS A CB  1 
ATOM   1680 C  CG  . LYS A 1 212 ? -19.963 -10.376 26.361  1.00 22.56 ? 213 LYS A CG  1 
ATOM   1681 C  CD  . LYS A 1 212 ? -20.732 -10.327 27.666  1.00 26.54 ? 213 LYS A CD  1 
ATOM   1682 C  CE  . LYS A 1 212 ? -22.238 -10.453 27.444  1.00 33.42 ? 213 LYS A CE  1 
ATOM   1683 N  NZ  . LYS A 1 212 ? -22.695 -9.728  26.217  1.00 36.33 ? 213 LYS A NZ  1 
ATOM   1684 N  N   . GLU A 1 213 ? -19.823 -9.489  23.006  1.00 14.86 ? 214 GLU A N   1 
ATOM   1685 C  CA  . GLU A 1 213 ? -20.405 -10.407 22.006  1.00 16.31 ? 214 GLU A CA  1 
ATOM   1686 C  C   . GLU A 1 213 ? -19.723 -10.283 20.638  1.00 15.26 ? 214 GLU A C   1 
ATOM   1687 O  O   . GLU A 1 213 ? -19.741 -9.170  20.046  1.00 15.11 ? 214 GLU A O   1 
ATOM   1688 C  CB  . GLU A 1 213 ? -21.923 -10.235 21.890  1.00 16.09 ? 214 GLU A CB  1 
ATOM   1689 C  CG  . GLU A 1 213 ? -22.517 -10.972 20.675  1.00 18.56 ? 214 GLU A CG  1 
ATOM   1690 C  CD  . GLU A 1 213 ? -24.036 -10.767 20.547  1.00 20.92 ? 214 GLU A CD  1 
ATOM   1691 O  OE1 . GLU A 1 213 ? -24.580 -9.988  21.332  1.00 18.78 ? 214 GLU A OE1 1 
ATOM   1692 O  OE2 . GLU A 1 213 ? -24.661 -11.409 19.663  1.00 27.35 ? 214 GLU A OE2 1 
ATOM   1693 N  N   . PRO A 1 214 ? -19.124 -11.407 20.142  1.00 13.60 ? 215 PRO A N   1 
ATOM   1694 C  CA  . PRO A 1 214 ? -18.441 -11.419 18.869  1.00 13.59 ? 215 PRO A CA  1 
ATOM   1695 C  C   . PRO A 1 214 ? -19.448 -11.406 17.732  1.00 13.30 ? 215 PRO A C   1 
ATOM   1696 O  O   . PRO A 1 214 ? -20.620 -11.791 17.932  1.00 13.07 ? 215 PRO A O   1 
ATOM   1697 C  CB  . PRO A 1 214 ? -17.605 -12.724 18.904  1.00 14.48 ? 215 PRO A CB  1 
ATOM   1698 C  CG  . PRO A 1 214 ? -18.386 -13.657 19.804  1.00 16.27 ? 215 PRO A CG  1 
ATOM   1699 C  CD  . PRO A 1 214 ? -19.144 -12.746 20.789  1.00 15.58 ? 215 PRO A CD  1 
ATOM   1700 N  N   . ILE A 1 215 ? -19.062 -10.882 16.573  1.00 11.25 ? 216 ILE A N   1 
ATOM   1701 C  CA  . ILE A 1 215 ? -19.861 -11.137 15.399  1.00 12.94 ? 216 ILE A CA  1 
ATOM   1702 C  C   . ILE A 1 215 ? -19.377 -12.420 14.729  1.00 12.77 ? 216 ILE A C   1 
ATOM   1703 O  O   . ILE A 1 215 ? -18.223 -12.784 14.910  1.00 13.54 ? 216 ILE A O   1 
ATOM   1704 C  CB  . ILE A 1 215 ? -19.890 -9.903  14.466  1.00 13.26 ? 216 ILE A CB  1 
ATOM   1705 C  CG1 . ILE A 1 215 ? -18.504 -9.526  13.966  1.00 13.05 ? 216 ILE A CG1 1 
ATOM   1706 C  CG2 . ILE A 1 215 ? -20.587 -8.668  15.271  1.00 13.95 ? 216 ILE A CG2 1 
ATOM   1707 C  CD1 . ILE A 1 215 ? -18.528 -8.557  12.656  1.00 11.81 ? 216 ILE A CD1 1 
ATOM   1708 N  N   . SER A 1 216 ? -20.251 -13.121 14.011  1.00 14.63 ? 217 SER A N   1 
ATOM   1709 C  CA  . SER A 1 216 ? -19.820 -14.237 13.131  1.00 16.36 ? 217 SER A CA  1 
ATOM   1710 C  C   . SER A 1 216 ? -19.582 -13.804 11.700  1.00 15.10 ? 217 SER A C   1 
ATOM   1711 O  O   . SER A 1 216 ? -20.373 -13.069 11.152  1.00 16.98 ? 217 SER A O   1 
ATOM   1712 C  CB  . SER A 1 216 ? -20.849 -15.385 13.076  1.00 15.75 ? 217 SER A CB  1 
ATOM   1713 O  OG  . SER A 1 216 ? -20.875 -15.976 14.347  1.00 26.02 ? 217 SER A OG  1 
ATOM   1714 N  N   . VAL A 1 217 ? -18.490 -14.271 11.105  1.00 14.89 ? 218 VAL A N   1 
ATOM   1715 C  CA  . VAL A 1 217 ? -18.194 -14.047 9.671   1.00 16.24 ? 218 VAL A CA  1 
ATOM   1716 C  C   . VAL A 1 217 ? -17.917 -15.450 9.087   1.00 14.81 ? 218 VAL A C   1 
ATOM   1717 O  O   . VAL A 1 217 ? -17.548 -16.350 9.823   1.00 15.84 ? 218 VAL A O   1 
ATOM   1718 C  CB  . VAL A 1 217 ? -17.011 -13.057 9.430   1.00 14.23 ? 218 VAL A CB  1 
ATOM   1719 C  CG1 . VAL A 1 217 ? -17.327 -11.678 10.105  1.00 16.26 ? 218 VAL A CG1 1 
ATOM   1720 C  CG2 . VAL A 1 217 ? -15.709 -13.664 9.999   1.00 16.57 ? 218 VAL A CG2 1 
ATOM   1721 N  N   . SER A 1 218 ? -18.089 -15.623 7.780   1.00 14.84 ? 219 SER A N   1 
ATOM   1722 C  CA  . SER A 1 218 ? -17.859 -16.890 7.173   1.00 14.04 ? 219 SER A CA  1 
ATOM   1723 C  C   . SER A 1 218 ? -16.390 -17.103 6.889   1.00 14.49 ? 219 SER A C   1 
ATOM   1724 O  O   . SER A 1 218 ? -15.589 -16.142 6.836   1.00 14.50 ? 219 SER A O   1 
ATOM   1725 C  CB  . SER A 1 218 ? -18.663 -17.044 5.869   1.00 14.24 ? 219 SER A CB  1 
ATOM   1726 O  OG  . SER A 1 218 ? -18.186 -16.124 4.925   1.00 11.95 ? 219 SER A OG  1 
ATOM   1727 N  N   . SER A 1 219 ? -16.052 -18.376 6.777   1.00 15.39 ? 220 SER A N   1 
ATOM   1728 C  CA  . SER A 1 219 ? -14.737 -18.786 6.418   1.00 16.74 ? 220 SER A CA  1 
ATOM   1729 C  C   . SER A 1 219 ? -14.404 -18.084 5.103   1.00 17.67 ? 220 SER A C   1 
ATOM   1730 O  O   . SER A 1 219 ? -13.248 -17.644 4.935   1.00 16.72 ? 220 SER A O   1 
ATOM   1731 C  CB  . SER A 1 219 ? -14.653 -20.316 6.260   1.00 18.29 ? 220 SER A CB  1 
ATOM   1732 O  OG  . SER A 1 219 ? -15.666 -20.808 5.357   1.00 22.58 ? 220 SER A OG  1 
ATOM   1733 N  N   . GLU A 1 220 ? -15.376 -17.958 4.167   1.00 18.13 ? 221 GLU A N   1 
ATOM   1734 C  CA  . GLU A 1 220 ? -15.048 -17.328 2.872   1.00 17.92 ? 221 GLU A CA  1 
ATOM   1735 C  C   . GLU A 1 220 ? -14.773 -15.807 2.987   1.00 17.73 ? 221 GLU A C   1 
ATOM   1736 O  O   . GLU A 1 220 ? -13.913 -15.284 2.296   1.00 17.20 ? 221 GLU A O   1 
ATOM   1737 C  CB  . GLU A 1 220 ? -16.154 -17.515 1.840   1.00 19.12 ? 221 GLU A CB  1 
ATOM   1738 C  CG  . GLU A 1 220 ? -16.417 -18.968 1.439   1.00 17.63 ? 221 GLU A CG  1 
ATOM   1739 C  CD  . GLU A 1 220 ? -17.481 -19.596 2.305   1.00 22.67 ? 221 GLU A CD  1 
ATOM   1740 O  OE1 . GLU A 1 220 ? -17.830 -19.002 3.358   1.00 20.34 ? 221 GLU A OE1 1 
ATOM   1741 O  OE2 . GLU A 1 220 ? -17.946 -20.715 1.952   1.00 26.52 ? 221 GLU A OE2 1 
ATOM   1742 N  N   . GLN A 1 221 ? -15.542 -15.111 3.826   1.00 16.19 ? 222 GLN A N   1 
ATOM   1743 C  CA  . GLN A 1 221 ? -15.224 -13.710 4.147   1.00 15.97 ? 222 GLN A CA  1 
ATOM   1744 C  C   . GLN A 1 221 ? -13.810 -13.483 4.706   1.00 16.57 ? 222 GLN A C   1 
ATOM   1745 O  O   . GLN A 1 221 ? -13.086 -12.585 4.225   1.00 13.04 ? 222 GLN A O   1 
ATOM   1746 C  CB  . GLN A 1 221 ? -16.262 -13.142 5.093   1.00 15.36 ? 222 GLN A CB  1 
ATOM   1747 C  CG  . GLN A 1 221 ? -17.599 -12.926 4.376   1.00 16.32 ? 222 GLN A CG  1 
ATOM   1748 C  CD  . GLN A 1 221 ? -18.730 -12.394 5.285   1.00 15.80 ? 222 GLN A CD  1 
ATOM   1749 O  OE1 . GLN A 1 221 ? -18.872 -12.850 6.424   1.00 19.94 ? 222 GLN A OE1 1 
ATOM   1750 N  NE2 . GLN A 1 221 ? -19.598 -11.505 4.738   1.00 12.46 ? 222 GLN A NE2 1 
ATOM   1751 N  N   . VAL A 1 222 ? -13.404 -14.280 5.702   1.00 17.07 ? 223 VAL A N   1 
ATOM   1752 C  CA  . VAL A 1 222 ? -12.089 -14.054 6.320   1.00 19.12 ? 223 VAL A CA  1 
ATOM   1753 C  C   . VAL A 1 222 ? -10.988 -14.507 5.335   1.00 19.45 ? 223 VAL A C   1 
ATOM   1754 O  O   . VAL A 1 222 ? -9.894  -13.955 5.310   1.00 17.39 ? 223 VAL A O   1 
ATOM   1755 C  CB  . VAL A 1 222 ? -11.928 -14.711 7.756   1.00 20.43 ? 223 VAL A CB  1 
ATOM   1756 C  CG1 . VAL A 1 222 ? -11.812 -16.212 7.635   1.00 20.28 ? 223 VAL A CG1 1 
ATOM   1757 C  CG2 . VAL A 1 222 ? -10.653 -14.132 8.501   1.00 18.66 ? 223 VAL A CG2 1 
ATOM   1758 N  N   . LEU A 1 223 ? -11.302 -15.513 4.513   1.00 20.31 ? 224 LEU A N   1 
ATOM   1759 C  CA  . LEU A 1 223 ? -10.359 -15.954 3.485   1.00 21.48 ? 224 LEU A CA  1 
ATOM   1760 C  C   . LEU A 1 223 ? -9.990  -14.821 2.518   1.00 19.63 ? 224 LEU A C   1 
ATOM   1761 O  O   . LEU A 1 223 ? -8.850  -14.673 2.092   1.00 18.73 ? 224 LEU A O   1 
ATOM   1762 C  CB  . LEU A 1 223 ? -10.882 -17.205 2.734   1.00 22.62 ? 224 LEU A CB  1 
ATOM   1763 C  CG  . LEU A 1 223 ? -10.292 -18.535 3.253   1.00 25.72 ? 224 LEU A CG  1 
ATOM   1764 C  CD1 . LEU A 1 223 ? -11.037 -19.798 2.631   1.00 27.28 ? 224 LEU A CD1 1 
ATOM   1765 C  CD2 . LEU A 1 223 ? -8.796  -18.582 2.918   1.00 31.71 ? 224 LEU A CD2 1 
ATOM   1766 N  N   . LYS A 1 224 ? -10.964 -14.016 2.165   1.00 19.20 ? 225 LYS A N   1 
ATOM   1767 C  CA  . LYS A 1 224 ? -10.674 -12.874 1.288   1.00 19.66 ? 225 LYS A CA  1 
ATOM   1768 C  C   . LYS A 1 224 ? -9.784  -11.783 1.914   1.00 18.59 ? 225 LYS A C   1 
ATOM   1769 O  O   . LYS A 1 224 ? -8.971  -11.159 1.181   1.00 17.34 ? 225 LYS A O   1 
ATOM   1770 C  CB  . LYS A 1 224 ? -11.980 -12.356 0.660   1.00 21.20 ? 225 LYS A CB  1 
ATOM   1771 C  CG  . LYS A 1 224 ? -12.579 -13.412 -0.367  1.00 22.47 ? 225 LYS A CG  1 
ATOM   1772 C  CD  . LYS A 1 224 ? -13.957 -13.067 -0.931  1.00 22.75 ? 225 LYS A CD  1 
ATOM   1773 C  CE  . LYS A 1 224 ? -14.710 -14.307 -1.535  1.00 23.92 ? 225 LYS A CE  1 
ATOM   1774 N  NZ  . LYS A 1 224 ? -16.059 -13.878 -2.157  1.00 26.91 ? 225 LYS A NZ  1 
ATOM   1775 N  N   . PHE A 1 225 ? -9.936  -11.538 3.243   1.00 16.56 ? 226 PHE A N   1 
ATOM   1776 C  CA  . PHE A 1 225 ? -8.996  -10.705 4.042   1.00 15.11 ? 226 PHE A CA  1 
ATOM   1777 C  C   . PHE A 1 225 ? -7.557  -11.153 3.819   1.00 14.42 ? 226 PHE A C   1 
ATOM   1778 O  O   . PHE A 1 225 ? -6.645  -10.343 3.666   1.00 15.46 ? 226 PHE A O   1 
ATOM   1779 C  CB  . PHE A 1 225 ? -9.263  -10.816 5.583   1.00 14.97 ? 226 PHE A CB  1 
ATOM   1780 C  CG  . PHE A 1 225 ? -10.425 -9.975  6.145   1.00 16.91 ? 226 PHE A CG  1 
ATOM   1781 C  CD1 . PHE A 1 225 ? -11.449 -9.473  5.356   1.00 14.35 ? 226 PHE A CD1 1 
ATOM   1782 C  CD2 . PHE A 1 225 ? -10.517 -9.792  7.538   1.00 17.13 ? 226 PHE A CD2 1 
ATOM   1783 C  CE1 . PHE A 1 225 ? -12.514 -8.738  5.938   1.00 17.61 ? 226 PHE A CE1 1 
ATOM   1784 C  CE2 . PHE A 1 225 ? -11.546 -9.119  8.110   1.00 17.24 ? 226 PHE A CE2 1 
ATOM   1785 C  CZ  . PHE A 1 225 ? -12.553 -8.547  7.304   1.00 17.20 ? 226 PHE A CZ  1 
ATOM   1786 N  N   . ARG A 1 226 ? -7.366  -12.451 3.872   1.00 14.24 ? 227 ARG A N   1 
ATOM   1787 C  CA  . ARG A 1 226 ? -6.044  -13.157 3.735   1.00 15.14 ? 227 ARG A CA  1 
ATOM   1788 C  C   . ARG A 1 226 ? -5.393  -13.163 2.314   1.00 15.85 ? 227 ARG A C   1 
ATOM   1789 O  O   . ARG A 1 226 ? -4.234  -13.500 2.147   1.00 17.34 ? 227 ARG A O   1 
ATOM   1790 C  CB  . ARG A 1 226 ? -6.194  -14.602 4.256   1.00 15.91 ? 227 ARG A CB  1 
ATOM   1791 C  CG  . ARG A 1 226 ? -6.518  -14.757 5.806   1.00 15.46 ? 227 ARG A CG  1 
ATOM   1792 C  CD  . ARG A 1 226 ? -6.419  -16.245 6.316   1.00 14.50 ? 227 ARG A CD  1 
ATOM   1793 N  NE  . ARG A 1 226 ? -7.027  -16.352 7.656   1.00 19.37 ? 227 ARG A NE  1 
ATOM   1794 C  CZ  . ARG A 1 226 ? -8.073  -17.115 7.959   1.00 20.70 ? 227 ARG A CZ  1 
ATOM   1795 N  NH1 . ARG A 1 226 ? -8.593  -17.951 7.046   1.00 21.32 ? 227 ARG A NH1 1 
ATOM   1796 N  NH2 . ARG A 1 226 ? -8.586  -17.078 9.175   1.00 16.82 ? 227 ARG A NH2 1 
ATOM   1797 N  N   . LYS A 1 227 ? -6.115  -12.696 1.333   1.00 15.62 ? 228 LYS A N   1 
ATOM   1798 C  CA  . LYS A 1 227 ? -5.626  -12.551 -0.015  1.00 16.40 ? 228 LYS A CA  1 
ATOM   1799 C  C   . LYS A 1 227 ? -5.028  -11.181 -0.254  1.00 15.49 ? 228 LYS A C   1 
ATOM   1800 O  O   . LYS A 1 227 ? -4.469  -10.909 -1.310  1.00 16.64 ? 228 LYS A O   1 
ATOM   1801 C  CB  . LYS A 1 227 ? -6.814  -12.816 -0.958  1.00 14.71 ? 228 LYS A CB  1 
ATOM   1802 C  CG  . LYS A 1 227 ? -7.115  -14.375 -1.123  1.00 16.93 ? 228 LYS A CG  1 
ATOM   1803 C  CD  . LYS A 1 227 ? -8.501  -14.553 -1.787  1.00 19.40 ? 228 LYS A CD  1 
ATOM   1804 C  CE  . LYS A 1 227 ? -8.561  -13.923 -3.201  1.00 29.62 ? 228 LYS A CE  1 
ATOM   1805 N  NZ  . LYS A 1 227 ? -8.765  -14.865 -4.367  1.00 31.48 ? 228 LYS A NZ  1 
ATOM   1806 N  N   . LEU A 1 228 ? -5.132  -10.309 0.740   1.00 16.84 ? 229 LEU A N   1 
ATOM   1807 C  CA  . LEU A 1 228 ? -4.573  -8.969  0.605   1.00 16.47 ? 229 LEU A CA  1 
ATOM   1808 C  C   . LEU A 1 228 ? -3.064  -9.083  0.779   1.00 17.01 ? 229 LEU A C   1 
ATOM   1809 O  O   . LEU A 1 228 ? -2.570  -10.134 1.191   1.00 14.78 ? 229 LEU A O   1 
ATOM   1810 C  CB  . LEU A 1 228 ? -5.202  -7.987  1.617   1.00 15.49 ? 229 LEU A CB  1 
ATOM   1811 C  CG  . LEU A 1 228 ? -6.675  -7.614  1.414   1.00 14.79 ? 229 LEU A CG  1 
ATOM   1812 C  CD1 . LEU A 1 228 ? -7.134  -7.183  2.714   1.00 10.58 ? 229 LEU A CD1 1 
ATOM   1813 C  CD2 . LEU A 1 228 ? -6.889  -6.462  0.383   1.00 12.79 ? 229 LEU A CD2 1 
ATOM   1814 N  N   . ASN A 1 229 ? -2.343  -7.991  0.467   1.00 18.19 ? 230 ASN A N   1 
ATOM   1815 C  CA  . ASN A 1 229 ? -0.882  -8.002  0.503   1.00 20.80 ? 230 ASN A CA  1 
ATOM   1816 C  C   . ASN A 1 229 ? -0.347  -6.846  1.338   1.00 20.80 ? 230 ASN A C   1 
ATOM   1817 O  O   . ASN A 1 229 ? -0.811  -5.735  1.236   1.00 21.54 ? 230 ASN A O   1 
ATOM   1818 C  CB  . ASN A 1 229 ? -0.281  -7.817  -0.908  1.00 20.43 ? 230 ASN A CB  1 
ATOM   1819 C  CG  . ASN A 1 229 ? -0.430  -9.046  -1.846  1.00 22.20 ? 230 ASN A CG  1 
ATOM   1820 O  OD1 . ASN A 1 229 ? -0.103  -8.934  -3.028  1.00 19.04 ? 230 ASN A OD1 1 
ATOM   1821 N  ND2 . ASN A 1 229 ? -0.857  -10.193 -1.325  1.00 20.05 ? 230 ASN A ND2 1 
ATOM   1822 N  N   . PHE A 1 230 ? 0.681   -7.144  2.119   1.00 22.71 ? 231 PHE A N   1 
ATOM   1823 C  CA  . PHE A 1 230 ? 1.522   -6.157  2.772   1.00 23.59 ? 231 PHE A CA  1 
ATOM   1824 C  C   . PHE A 1 230 ? 2.367   -5.372  1.734   1.00 24.89 ? 231 PHE A C   1 
ATOM   1825 O  O   . PHE A 1 230 ? 2.510   -4.126  1.825   1.00 25.09 ? 231 PHE A O   1 
ATOM   1826 C  CB  . PHE A 1 230 ? 2.480   -6.859  3.724   1.00 23.52 ? 231 PHE A CB  1 
ATOM   1827 C  CG  . PHE A 1 230 ? 1.851   -7.359  5.006   1.00 23.41 ? 231 PHE A CG  1 
ATOM   1828 C  CD1 . PHE A 1 230 ? 1.015   -6.544  5.763   1.00 20.60 ? 231 PHE A CD1 1 
ATOM   1829 C  CD2 . PHE A 1 230 ? 2.185   -8.652  5.494   1.00 23.15 ? 231 PHE A CD2 1 
ATOM   1830 C  CE1 . PHE A 1 230 ? 0.474   -7.033  7.006   1.00 20.28 ? 231 PHE A CE1 1 
ATOM   1831 C  CE2 . PHE A 1 230 ? 1.647   -9.140  6.716   1.00 21.54 ? 231 PHE A CE2 1 
ATOM   1832 C  CZ  . PHE A 1 230 ? 0.802   -8.324  7.448   1.00 20.07 ? 231 PHE A CZ  1 
ATOM   1833 N  N   . ASN A 1 231 ? 2.922   -6.095  0.762   1.00 24.68 ? 232 ASN A N   1 
ATOM   1834 C  CA  . ASN A 1 231 ? 3.736   -5.437  -0.303  1.00 25.38 ? 232 ASN A CA  1 
ATOM   1835 C  C   . ASN A 1 231 ? 2.939   -4.520  -1.202  1.00 25.88 ? 232 ASN A C   1 
ATOM   1836 O  O   . ASN A 1 231 ? 1.691   -4.626  -1.316  1.00 24.70 ? 232 ASN A O   1 
ATOM   1837 C  CB  . ASN A 1 231 ? 4.377   -6.468  -1.212  1.00 24.78 ? 232 ASN A CB  1 
ATOM   1838 C  CG  . ASN A 1 231 ? 3.365   -7.395  -1.779  1.00 24.90 ? 232 ASN A CG  1 
ATOM   1839 O  OD1 . ASN A 1 231 ? 2.924   -8.314  -1.092  1.00 23.49 ? 232 ASN A OD1 1 
ATOM   1840 N  ND2 . ASN A 1 231 ? 2.959   -7.155  -3.038  1.00 25.91 ? 232 ASN A ND2 1 
ATOM   1841 N  N   . GLY A 1 232 ? 3.671   -3.630  -1.869  1.00 25.83 ? 233 GLY A N   1 
ATOM   1842 C  CA  . GLY A 1 232 ? 3.091   -2.816  -2.913  1.00 27.25 ? 233 GLY A CA  1 
ATOM   1843 C  C   . GLY A 1 232 ? 3.081   -3.490  -4.282  1.00 27.53 ? 233 GLY A C   1 
ATOM   1844 O  O   . GLY A 1 232 ? 3.730   -4.483  -4.488  1.00 27.92 ? 233 GLY A O   1 
ATOM   1845 N  N   . GLU A 1 233 ? 2.346   -2.914  -5.216  1.00 29.95 ? 234 GLU A N   1 
ATOM   1846 C  CA  . GLU A 1 233 ? 2.105   -3.561  -6.525  1.00 32.38 ? 234 GLU A CA  1 
ATOM   1847 C  C   . GLU A 1 233 ? 3.335   -4.031  -7.318  1.00 32.81 ? 234 GLU A C   1 
ATOM   1848 O  O   . GLU A 1 233 ? 3.252   -5.005  -8.094  1.00 33.92 ? 234 GLU A O   1 
ATOM   1849 C  CB  . GLU A 1 233 ? 1.136   -2.749  -7.406  1.00 31.82 ? 234 GLU A CB  1 
ATOM   1850 C  CG  . GLU A 1 233 ? 0.723   -3.491  -8.657  1.00 35.48 ? 234 GLU A CG  1 
ATOM   1851 C  CD  . GLU A 1 233 ? -0.018  -2.646  -9.662  1.00 38.60 ? 234 GLU A CD  1 
ATOM   1852 O  OE1 . GLU A 1 233 ? -0.359  -1.459  -9.383  1.00 40.71 ? 234 GLU A OE1 1 
ATOM   1853 O  OE2 . GLU A 1 233 ? -0.254  -3.198  -10.754 1.00 40.94 ? 234 GLU A OE2 1 
ATOM   1854 N  N   . GLY A 1 234 ? 4.469   -3.379  -7.145  1.00 32.51 ? 235 GLY A N   1 
ATOM   1855 C  CA  . GLY A 1 234 ? 5.668   -3.872  -7.878  1.00 35.01 ? 235 GLY A CA  1 
ATOM   1856 C  C   . GLY A 1 234 ? 6.466   -5.078  -7.340  1.00 34.82 ? 235 GLY A C   1 
ATOM   1857 O  O   . GLY A 1 234 ? 7.560   -5.383  -7.821  1.00 34.62 ? 235 GLY A O   1 
ATOM   1858 N  N   . GLU A 1 235 ? 5.925   -5.754  -6.329  1.00 34.50 ? 236 GLU A N   1 
ATOM   1859 C  CA  . GLU A 1 235 ? 6.759   -6.446  -5.352  1.00 33.35 ? 236 GLU A CA  1 
ATOM   1860 C  C   . GLU A 1 235 ? 6.321   -7.897  -5.157  1.00 32.06 ? 236 GLU A C   1 
ATOM   1861 O  O   . GLU A 1 235 ? 5.195   -8.281  -5.553  1.00 31.32 ? 236 GLU A O   1 
ATOM   1862 C  CB  . GLU A 1 235 ? 6.740   -5.690  -4.004  1.00 34.42 ? 236 GLU A CB  1 
ATOM   1863 C  CG  . GLU A 1 235 ? 7.469   -4.329  -4.002  1.00 36.35 ? 236 GLU A CG  1 
ATOM   1864 C  CD  . GLU A 1 235 ? 7.072   -3.417  -2.849  1.00 37.51 ? 236 GLU A CD  1 
ATOM   1865 O  OE1 . GLU A 1 235 ? 6.385   -3.850  -1.873  1.00 42.90 ? 236 GLU A OE1 1 
ATOM   1866 O  OE2 . GLU A 1 235 ? 7.472   -2.227  -2.906  1.00 45.17 ? 236 GLU A OE2 1 
ATOM   1867 N  N   . PRO A 1 236 ? 7.224   -8.714  -4.589  1.00 29.96 ? 237 PRO A N   1 
ATOM   1868 C  CA  . PRO A 1 236 ? 6.962   -10.124 -4.308  1.00 29.65 ? 237 PRO A CA  1 
ATOM   1869 C  C   . PRO A 1 236 ? 5.831   -10.245 -3.245  1.00 28.34 ? 237 PRO A C   1 
ATOM   1870 O  O   . PRO A 1 236 ? 5.776   -9.441  -2.331  1.00 26.97 ? 237 PRO A O   1 
ATOM   1871 C  CB  . PRO A 1 236 ? 8.301   -10.624 -3.753  1.00 29.83 ? 237 PRO A CB  1 
ATOM   1872 C  CG  . PRO A 1 236 ? 9.321   -9.549  -4.035  1.00 30.44 ? 237 PRO A CG  1 
ATOM   1873 C  CD  . PRO A 1 236 ? 8.575   -8.285  -4.175  1.00 29.99 ? 237 PRO A CD  1 
ATOM   1874 N  N   . GLU A 1 237 ? 4.948   -11.231 -3.400  1.00 27.38 ? 238 GLU A N   1 
ATOM   1875 C  CA  . GLU A 1 237 ? 3.765   -11.315 -2.571  1.00 26.33 ? 238 GLU A CA  1 
ATOM   1876 C  C   . GLU A 1 237 ? 4.085   -11.756 -1.137  1.00 24.64 ? 238 GLU A C   1 
ATOM   1877 O  O   . GLU A 1 237 ? 4.740   -12.739 -0.904  1.00 24.40 ? 238 GLU A O   1 
ATOM   1878 C  CB  . GLU A 1 237 ? 2.710   -12.211 -3.195  1.00 26.94 ? 238 GLU A CB  1 
ATOM   1879 C  CG  . GLU A 1 237 ? 1.348   -11.964 -2.630  1.00 28.95 ? 238 GLU A CG  1 
ATOM   1880 C  CD  . GLU A 1 237 ? 0.259   -12.756 -3.294  1.00 30.07 ? 238 GLU A CD  1 
ATOM   1881 O  OE1 . GLU A 1 237 ? 0.573   -13.816 -3.824  1.00 38.79 ? 238 GLU A OE1 1 
ATOM   1882 O  OE2 . GLU A 1 237 ? -0.921  -12.342 -3.278  1.00 29.48 ? 238 GLU A OE2 1 
ATOM   1883 N  N   . GLU A 1 238 ? 3.559   -11.005 -0.194  1.00 23.28 ? 239 GLU A N   1 
ATOM   1884 C  CA  . GLU A 1 238 ? 3.655   -11.324 1.215   1.00 22.22 ? 239 GLU A CA  1 
ATOM   1885 C  C   . GLU A 1 238 ? 2.170   -11.178 1.623   1.00 20.23 ? 239 GLU A C   1 
ATOM   1886 O  O   . GLU A 1 238 ? 1.650   -10.088 1.582   1.00 19.32 ? 239 GLU A O   1 
ATOM   1887 C  CB  . GLU A 1 238 ? 4.554   -10.372 1.939   1.00 21.95 ? 239 GLU A CB  1 
ATOM   1888 C  CG  . GLU A 1 238 ? 5.905   -11.062 2.337   1.00 23.70 ? 239 GLU A CG  1 
ATOM   1889 C  CD  . GLU A 1 238 ? 6.993   -10.047 2.779   0.01 22.56 ? 239 GLU A CD  1 
ATOM   1890 O  OE1 . GLU A 1 238 ? 7.511   -10.168 3.911   0.01 22.63 ? 239 GLU A OE1 1 
ATOM   1891 O  OE2 . GLU A 1 238 ? 7.361   -9.151  1.984   0.01 22.87 ? 239 GLU A OE2 1 
ATOM   1892 N  N   . LEU A 1 239 ? 1.494   -12.275 1.936   1.00 18.63 ? 240 LEU A N   1 
ATOM   1893 C  CA  . LEU A 1 239 ? 0.086   -12.138 2.276   1.00 16.93 ? 240 LEU A CA  1 
ATOM   1894 C  C   . LEU A 1 239 ? -0.044  -11.285 3.557   1.00 15.46 ? 240 LEU A C   1 
ATOM   1895 O  O   . LEU A 1 239 ? 0.706   -11.464 4.504   1.00 13.07 ? 240 LEU A O   1 
ATOM   1896 C  CB  . LEU A 1 239 ? -0.556  -13.485 2.503   1.00 17.06 ? 240 LEU A CB  1 
ATOM   1897 C  CG  . LEU A 1 239 ? -0.510  -14.423 1.282   1.00 19.59 ? 240 LEU A CG  1 
ATOM   1898 C  CD1 . LEU A 1 239 ? -1.221  -15.734 1.662   1.00 16.85 ? 240 LEU A CD1 1 
ATOM   1899 C  CD2 . LEU A 1 239 ? -1.212  -13.786 0.085   1.00 17.63 ? 240 LEU A CD2 1 
ATOM   1900 N  N   . MET A 1 240 ? -1.010  -10.373 3.528   1.00 15.28 ? 241 MET A N   1 
ATOM   1901 C  CA  . MET A 1 240 ? -1.427  -9.641  4.708   1.00 14.83 ? 241 MET A CA  1 
ATOM   1902 C  C   . MET A 1 240 ? -2.174  -10.594 5.618   1.00 14.14 ? 241 MET A C   1 
ATOM   1903 O  O   . MET A 1 240 ? -3.377  -10.791 5.421   1.00 11.40 ? 241 MET A O   1 
ATOM   1904 C  CB  . MET A 1 240 ? -2.347  -8.472  4.315   1.00 13.97 ? 241 MET A CB  1 
ATOM   1905 C  CG  . MET A 1 240 ? -2.586  -7.491  5.477   1.00 11.92 ? 241 MET A CG  1 
ATOM   1906 S  SD  . MET A 1 240 ? -3.638  -6.179  4.905   1.00 18.19 ? 241 MET A SD  1 
ATOM   1907 C  CE  . MET A 1 240 ? -2.396  -5.042  4.292   1.00 14.94 ? 241 MET A CE  1 
ATOM   1908 N  N   . VAL A 1 241 ? -1.419  -11.224 6.532   1.00 13.56 ? 242 VAL A N   1 
ATOM   1909 C  CA  . VAL A 1 241 ? -1.950  -12.136 7.546   1.00 14.30 ? 242 VAL A CA  1 
ATOM   1910 C  C   . VAL A 1 241 ? -1.165  -11.910 8.833   1.00 14.86 ? 242 VAL A C   1 
ATOM   1911 O  O   . VAL A 1 241 ? 0.007   -11.518 8.804   1.00 15.20 ? 242 VAL A O   1 
ATOM   1912 C  CB  . VAL A 1 241 ? -1.858  -13.665 7.213   1.00 13.83 ? 242 VAL A CB  1 
ATOM   1913 C  CG1 . VAL A 1 241 ? -2.807  -14.038 6.044   1.00 13.65 ? 242 VAL A CG1 1 
ATOM   1914 C  CG2 . VAL A 1 241 ? -0.405  -14.109 6.883   1.00 16.17 ? 242 VAL A CG2 1 
ATOM   1915 N  N   . ASP A 1 242 ? -1.803  -12.233 9.938   1.00 12.51 ? 243 ASP A N   1 
ATOM   1916 C  CA  . ASP A 1 242 ? -1.181  -12.044 11.234  1.00 13.25 ? 243 ASP A CA  1 
ATOM   1917 C  C   . ASP A 1 242 ? -0.720  -10.609 11.488  1.00 12.05 ? 243 ASP A C   1 
ATOM   1918 O  O   . ASP A 1 242 ? 0.364   -10.436 12.007  1.00 13.07 ? 243 ASP A O   1 
ATOM   1919 C  CB  . ASP A 1 242 ? -0.039  -13.099 11.518  1.00 12.49 ? 243 ASP A CB  1 
ATOM   1920 C  CG  . ASP A 1 242 ? -0.566  -14.510 11.576  1.00 13.57 ? 243 ASP A CG  1 
ATOM   1921 O  OD1 . ASP A 1 242 ? -1.661  -14.682 12.155  1.00 13.95 ? 243 ASP A OD1 1 
ATOM   1922 O  OD2 . ASP A 1 242 ? 0.064   -15.466 11.026  1.00 15.07 ? 243 ASP A OD2 1 
ATOM   1923 N  N   . ASN A 1 243 ? -1.567  -9.610  11.166  1.00 12.19 ? 244 ASN A N   1 
ATOM   1924 C  CA  . ASN A 1 243 ? -1.263  -8.215  11.423  1.00 11.35 ? 244 ASN A CA  1 
ATOM   1925 C  C   . ASN A 1 243 ? -1.880  -7.827  12.808  1.00 12.78 ? 244 ASN A C   1 
ATOM   1926 O  O   . ASN A 1 243 ? -2.612  -6.826  12.956  1.00 12.53 ? 244 ASN A O   1 
ATOM   1927 C  CB  . ASN A 1 243 ? -1.800  -7.345  10.299  1.00 11.45 ? 244 ASN A CB  1 
ATOM   1928 C  CG  . ASN A 1 243 ? -3.328  -7.537  10.037  1.00 13.40 ? 244 ASN A CG  1 
ATOM   1929 O  OD1 . ASN A 1 243 ? -3.968  -8.466  10.520  1.00 16.02 ? 244 ASN A OD1 1 
ATOM   1930 N  ND2 . ASN A 1 243 ? -3.896  -6.614  9.280   1.00 15.68 ? 244 ASN A ND2 1 
ATOM   1931 N  N   . TRP A 1 244 ? -1.535  -8.611  13.815  1.00 11.77 ? 245 TRP A N   1 
ATOM   1932 C  CA  . TRP A 1 244 ? -2.013  -8.334  15.163  1.00 11.60 ? 245 TRP A CA  1 
ATOM   1933 C  C   . TRP A 1 244 ? -0.820  -8.223  16.066  1.00 11.77 ? 245 TRP A C   1 
ATOM   1934 O  O   . TRP A 1 244 ? 0.199   -8.875  15.842  1.00 11.95 ? 245 TRP A O   1 
ATOM   1935 C  CB  . TRP A 1 244 ? -2.978  -9.433  15.658  1.00 10.79 ? 245 TRP A CB  1 
ATOM   1936 C  CG  . TRP A 1 244 ? -2.475  -10.861 15.451  1.00 10.35 ? 245 TRP A CG  1 
ATOM   1937 C  CD1 . TRP A 1 244 ? -2.536  -11.604 14.302  1.00 13.39 ? 245 TRP A CD1 1 
ATOM   1938 C  CD2 . TRP A 1 244 ? -1.938  -11.729 16.457  1.00 6.95  ? 245 TRP A CD2 1 
ATOM   1939 N  NE1 . TRP A 1 244 ? -2.049  -12.870 14.524  1.00 8.75  ? 245 TRP A NE1 1 
ATOM   1940 C  CE2 . TRP A 1 244 ? -1.677  -12.967 15.845  1.00 10.92 ? 245 TRP A CE2 1 
ATOM   1941 C  CE3 . TRP A 1 244 ? -1.695  -11.583 17.832  1.00 9.24  ? 245 TRP A CE3 1 
ATOM   1942 C  CZ2 . TRP A 1 244 ? -1.086  -14.045 16.538  1.00 10.08 ? 245 TRP A CZ2 1 
ATOM   1943 C  CZ3 . TRP A 1 244 ? -1.107  -12.666 18.538  1.00 11.69 ? 245 TRP A CZ3 1 
ATOM   1944 C  CH2 . TRP A 1 244 ? -0.842  -13.883 17.886  1.00 13.30 ? 245 TRP A CH2 1 
ATOM   1945 N  N   . ARG A 1 245 ? -0.967  -7.382  17.079  1.00 11.40 ? 246 ARG A N   1 
ATOM   1946 C  CA  . ARG A 1 245 ? -0.023  -7.240  18.188  1.00 11.99 ? 246 ARG A CA  1 
ATOM   1947 C  C   . ARG A 1 245 ? -0.534  -8.132  19.318  1.00 12.62 ? 246 ARG A C   1 
ATOM   1948 O  O   . ARG A 1 245 ? -1.739  -8.140  19.609  1.00 13.83 ? 246 ARG A O   1 
ATOM   1949 C  CB  . ARG A 1 245 ? 0.046   -5.779  18.652  1.00 10.90 ? 246 ARG A CB  1 
ATOM   1950 C  CG  . ARG A 1 245 ? 1.068   -5.560  19.783  1.00 8.58  ? 246 ARG A CG  1 
ATOM   1951 C  CD  . ARG A 1 245 ? 1.060   -4.115  20.323  1.00 10.20 ? 246 ARG A CD  1 
ATOM   1952 N  NE  . ARG A 1 245 ? 2.309   -3.828  21.088  1.00 10.81 ? 246 ARG A NE  1 
ATOM   1953 C  CZ  . ARG A 1 245 ? 2.509   -2.743  21.833  1.00 15.41 ? 246 ARG A CZ  1 
ATOM   1954 N  NH1 . ARG A 1 245 ? 1.505   -1.866  22.104  1.00 12.86 ? 246 ARG A NH1 1 
ATOM   1955 N  NH2 . ARG A 1 245 ? 3.686   -2.589  22.401  1.00 15.07 ? 246 ARG A NH2 1 
ATOM   1956 N  N   . PRO A 1 246 ? 0.369   -8.939  19.932  1.00 14.79 ? 247 PRO A N   1 
ATOM   1957 C  CA  . PRO A 1 246 ? -0.029  -9.720  21.066  1.00 14.67 ? 247 PRO A CA  1 
ATOM   1958 C  C   . PRO A 1 246 ? -0.340  -8.879  22.311  1.00 13.96 ? 247 PRO A C   1 
ATOM   1959 O  O   . PRO A 1 246 ? 0.067   -7.710  22.416  1.00 12.45 ? 247 PRO A O   1 
ATOM   1960 C  CB  . PRO A 1 246 ? 1.183   -10.617 21.309  1.00 16.46 ? 247 PRO A CB  1 
ATOM   1961 C  CG  . PRO A 1 246 ? 2.021   -10.497 20.041  1.00 17.79 ? 247 PRO A CG  1 
ATOM   1962 C  CD  . PRO A 1 246 ? 1.788   -9.139  19.605  1.00 14.98 ? 247 PRO A CD  1 
ATOM   1963 N  N   . ALA A 1 247 ? -1.028  -9.529  23.248  1.00 14.72 ? 248 ALA A N   1 
ATOM   1964 C  CA  . ALA A 1 247 ? -1.446  -8.940  24.529  1.00 13.98 ? 248 ALA A CA  1 
ATOM   1965 C  C   . ALA A 1 247 ? -0.210  -8.430  25.228  1.00 15.00 ? 248 ALA A C   1 
ATOM   1966 O  O   . ALA A 1 247 ? 0.846   -9.085  25.232  1.00 13.30 ? 248 ALA A O   1 
ATOM   1967 C  CB  . ALA A 1 247 ? -2.101  -9.981  25.386  1.00 13.16 ? 248 ALA A CB  1 
ATOM   1968 N  N   . GLN A 1 248 ? -0.366  -7.257  25.831  1.00 13.88 ? 249 GLN A N   1 
ATOM   1969 C  CA  . GLN A 1 248 ? 0.723   -6.543  26.463  1.00 13.73 ? 249 GLN A CA  1 
ATOM   1970 C  C   . GLN A 1 248 ? 0.482   -6.597  27.970  1.00 14.46 ? 249 GLN A C   1 
ATOM   1971 O  O   . GLN A 1 248 ? -0.659  -6.853  28.396  1.00 12.83 ? 249 GLN A O   1 
ATOM   1972 C  CB  . GLN A 1 248 ? 0.734   -5.090  25.959  1.00 13.68 ? 249 GLN A CB  1 
ATOM   1973 C  CG  . GLN A 1 248 ? 1.097   -4.945  24.443  1.00 11.67 ? 249 GLN A CG  1 
ATOM   1974 C  CD  . GLN A 1 248 ? 2.374   -5.687  24.138  1.00 12.05 ? 249 GLN A CD  1 
ATOM   1975 O  OE1 . GLN A 1 248 ? 3.411   -5.334  24.689  1.00 17.78 ? 249 GLN A OE1 1 
ATOM   1976 N  NE2 . GLN A 1 248 ? 2.323   -6.738  23.295  1.00 12.33 ? 249 GLN A NE2 1 
ATOM   1977 N  N   . PRO A 1 249 ? 1.537   -6.347  28.794  1.00 15.56 ? 250 PRO A N   1 
ATOM   1978 C  CA  . PRO A 1 249 ? 1.310   -6.335  30.247  1.00 15.60 ? 250 PRO A CA  1 
ATOM   1979 C  C   . PRO A 1 249 ? 0.190   -5.366  30.678  1.00 15.86 ? 250 PRO A C   1 
ATOM   1980 O  O   . PRO A 1 249 ? 0.246   -4.162  30.337  1.00 17.23 ? 250 PRO A O   1 
ATOM   1981 C  CB  . PRO A 1 249 ? 2.671   -5.778  30.794  1.00 14.51 ? 250 PRO A CB  1 
ATOM   1982 C  CG  . PRO A 1 249 ? 3.684   -6.300  29.810  1.00 16.51 ? 250 PRO A CG  1 
ATOM   1983 C  CD  . PRO A 1 249 ? 2.933   -5.968  28.486  1.00 14.94 ? 250 PRO A CD  1 
ATOM   1984 N  N   . LEU A 1 250 ? -0.764  -5.846  31.464  1.00 16.24 ? 251 LEU A N   1 
ATOM   1985 C  CA  . LEU A 1 250 ? -1.814  -4.954  32.057  1.00 17.70 ? 251 LEU A CA  1 
ATOM   1986 C  C   . LEU A 1 250 ? -1.218  -3.864  32.964  1.00 18.96 ? 251 LEU A C   1 
ATOM   1987 O  O   . LEU A 1 250 ? -1.651  -2.703  32.910  1.00 17.27 ? 251 LEU A O   1 
ATOM   1988 C  CB  . LEU A 1 250 ? -2.881  -5.752  32.837  1.00 17.99 ? 251 LEU A CB  1 
ATOM   1989 C  CG  . LEU A 1 250 ? -4.210  -5.045  33.167  1.00 18.00 ? 251 LEU A CG  1 
ATOM   1990 C  CD1 . LEU A 1 250 ? -4.842  -4.429  31.950  1.00 19.19 ? 251 LEU A CD1 1 
ATOM   1991 C  CD2 . LEU A 1 250 ? -5.203  -6.014  33.906  1.00 18.35 ? 251 LEU A CD2 1 
ATOM   1992 N  N   . LYS A 1 251 ? -0.177  -4.221  33.737  1.00 19.90 ? 252 LYS A N   1 
ATOM   1993 C  CA  . LYS A 1 251 ? 0.485   -3.257  34.665  1.00 22.12 ? 252 LYS A CA  1 
ATOM   1994 C  C   . LYS A 1 251 ? -0.552  -2.704  35.694  1.00 22.08 ? 252 LYS A C   1 
ATOM   1995 O  O   . LYS A 1 251 ? -1.351  -3.469  36.191  1.00 22.81 ? 252 LYS A O   1 
ATOM   1996 C  CB  . LYS A 1 251 ? 1.253   -2.174  33.910  1.00 21.31 ? 252 LYS A CB  1 
ATOM   1997 C  CG  . LYS A 1 251 ? 2.388   -2.767  33.062  1.00 24.79 ? 252 LYS A CG  1 
ATOM   1998 C  CD  . LYS A 1 251 ? 3.382   -1.721  32.581  1.00 28.33 ? 252 LYS A CD  1 
ATOM   1999 C  CE  . LYS A 1 251 ? 4.589   -2.414  31.947  1.00 26.86 ? 252 LYS A CE  1 
ATOM   2000 N  NZ  . LYS A 1 251 ? 5.373   -1.450  31.133  1.00 26.00 ? 252 LYS A NZ  1 
ATOM   2001 N  N   A ASN A 1 252 ? -0.572  -1.426  36.049  0.50 22.98 ? 253 ASN A N   1 
ATOM   2002 N  N   B ASN A 1 252 ? -0.533  -1.397  35.929  0.50 22.52 ? 253 ASN A N   1 
ATOM   2003 C  CA  A ASN A 1 252 ? -1.536  -1.031  37.135  0.50 24.29 ? 253 ASN A CA  1 
ATOM   2004 C  CA  B ASN A 1 252 ? -1.371  -0.822  36.995  0.50 23.87 ? 253 ASN A CA  1 
ATOM   2005 C  C   A ASN A 1 252 ? -3.021  -1.460  36.895  0.50 23.78 ? 253 ASN A C   1 
ATOM   2006 C  C   B ASN A 1 252 ? -2.909  -0.709  36.716  0.50 23.48 ? 253 ASN A C   1 
ATOM   2007 O  O   A ASN A 1 252 ? -3.770  -1.864  37.815  0.50 23.35 ? 253 ASN A O   1 
ATOM   2008 O  O   B ASN A 1 252 ? -3.654  -0.172  37.560  0.50 24.39 ? 253 ASN A O   1 
ATOM   2009 C  CB  A ASN A 1 252 ? -1.534  0.489   37.373  0.50 25.25 ? 253 ASN A CB  1 
ATOM   2010 C  CB  B ASN A 1 252 ? -0.759  0.488   37.543  0.50 24.15 ? 253 ASN A CB  1 
ATOM   2011 C  CG  A ASN A 1 252 ? -2.702  1.187   36.680  0.50 24.61 ? 253 ASN A CG  1 
ATOM   2012 C  CG  B ASN A 1 252 ? -1.398  0.941   38.867  0.50 23.64 ? 253 ASN A CG  1 
ATOM   2013 O  OD1 A ASN A 1 252 ? -2.730  1.248   35.486  0.50 28.81 ? 253 ASN A OD1 1 
ATOM   2014 O  OD1 B ASN A 1 252 ? -2.329  0.320   39.388  0.50 21.87 ? 253 ASN A OD1 1 
ATOM   2015 N  ND2 A ASN A 1 252 ? -3.669  1.699   37.444  0.50 30.46 ? 253 ASN A ND2 1 
ATOM   2016 N  ND2 B ASN A 1 252 ? -0.900  2.043   39.399  0.50 27.71 ? 253 ASN A ND2 1 
ATOM   2017 N  N   . ARG A 1 253 ? -3.393  -1.320  35.630  1.00 22.38 ? 254 ARG A N   1 
ATOM   2018 C  CA  . ARG A 1 253 ? -4.743  -1.058  35.161  1.00 21.60 ? 254 ARG A CA  1 
ATOM   2019 C  C   . ARG A 1 253 ? -5.832  -2.006  35.556  1.00 21.23 ? 254 ARG A C   1 
ATOM   2020 O  O   . ARG A 1 253 ? -5.608  -3.207  35.679  1.00 22.90 ? 254 ARG A O   1 
ATOM   2021 C  CB  . ARG A 1 253 ? -4.721  -0.906  33.619  1.00 20.57 ? 254 ARG A CB  1 
ATOM   2022 C  CG  . ARG A 1 253 ? -3.775  0.135   33.152  1.00 20.25 ? 254 ARG A CG  1 
ATOM   2023 C  CD  . ARG A 1 253 ? -3.757  0.093   31.620  1.00 17.02 ? 254 ARG A CD  1 
ATOM   2024 N  NE  . ARG A 1 253 ? -2.800  -0.923  31.132  1.00 15.17 ? 254 ARG A NE  1 
ATOM   2025 C  CZ  . ARG A 1 253 ? -2.611  -1.199  29.847  1.00 11.99 ? 254 ARG A CZ  1 
ATOM   2026 N  NH1 . ARG A 1 253 ? -3.356  -0.532  28.923  1.00 8.54  ? 254 ARG A NH1 1 
ATOM   2027 N  NH2 . ARG A 1 253 ? -1.710  -2.136  29.494  1.00 11.55 ? 254 ARG A NH2 1 
ATOM   2028 N  N   . GLN A 1 254 ? -7.021  -1.451  35.689  1.00 20.56 ? 255 GLN A N   1 
ATOM   2029 C  CA  . GLN A 1 254 ? -8.218  -2.234  35.928  1.00 22.32 ? 255 GLN A CA  1 
ATOM   2030 C  C   . GLN A 1 254 ? -9.130  -2.216  34.680  1.00 21.04 ? 255 GLN A C   1 
ATOM   2031 O  O   . GLN A 1 254 ? -9.371  -1.152  34.073  1.00 21.64 ? 255 GLN A O   1 
ATOM   2032 C  CB  . GLN A 1 254 ? -8.971  -1.730  37.164  1.00 22.74 ? 255 GLN A CB  1 
ATOM   2033 C  CG  . GLN A 1 254 ? -9.326  -2.915  38.027  1.00 30.42 ? 255 GLN A CG  1 
ATOM   2034 C  CD  . GLN A 1 254 ? -10.481 -2.668  38.985  1.00 40.75 ? 255 GLN A CD  1 
ATOM   2035 O  OE1 . GLN A 1 254 ? -11.374 -1.823  38.735  1.00 44.24 ? 255 GLN A OE1 1 
ATOM   2036 N  NE2 . GLN A 1 254 ? -10.489 -3.427  40.085  1.00 42.38 ? 255 GLN A NE2 1 
ATOM   2037 N  N   . ILE A 1 255 ? -9.596  -3.383  34.280  1.00 18.91 ? 256 ILE A N   1 
ATOM   2038 C  CA  . ILE A 1 255 ? -10.556 -3.485  33.163  1.00 18.57 ? 256 ILE A CA  1 
ATOM   2039 C  C   . ILE A 1 255 ? -11.917 -3.514  33.852  1.00 17.70 ? 256 ILE A C   1 
ATOM   2040 O  O   . ILE A 1 255 ? -12.094 -4.289  34.781  1.00 16.97 ? 256 ILE A O   1 
ATOM   2041 C  CB  . ILE A 1 255 ? -10.394 -4.796  32.361  1.00 18.54 ? 256 ILE A CB  1 
ATOM   2042 C  CG1 . ILE A 1 255 ? -8.976  -4.919  31.759  1.00 18.69 ? 256 ILE A CG1 1 
ATOM   2043 C  CG2 . ILE A 1 255 ? -11.496 -4.914  31.282  1.00 15.67 ? 256 ILE A CG2 1 
ATOM   2044 C  CD1 . ILE A 1 255 ? -8.746  -6.293  31.037  1.00 18.64 ? 256 ILE A CD1 1 
ATOM   2045 N  N   . LYS A 1 256 ? -12.815 -2.606  33.468  1.00 15.81 ? 257 LYS A N   1 
ATOM   2046 C  CA  . LYS A 1 256 ? -14.172 -2.585  34.010  1.00 16.00 ? 257 LYS A CA  1 
ATOM   2047 C  C   . LYS A 1 256 ? -15.162 -3.252  33.095  1.00 15.61 ? 257 LYS A C   1 
ATOM   2048 O  O   . LYS A 1 256 ? -14.992 -3.257  31.867  1.00 15.62 ? 257 LYS A O   1 
ATOM   2049 C  CB  . LYS A 1 256 ? -14.576 -1.130  34.363  1.00 17.78 ? 257 LYS A CB  1 
ATOM   2050 C  CG  . LYS A 1 256 ? -13.785 -0.670  35.627  1.00 21.21 ? 257 LYS A CG  1 
ATOM   2051 C  CD  . LYS A 1 256 ? -14.066 0.767   35.967  1.00 30.69 ? 257 LYS A CD  1 
ATOM   2052 C  CE  . LYS A 1 256 ? -12.969 1.384   36.880  1.00 31.21 ? 257 LYS A CE  1 
ATOM   2053 N  NZ  . LYS A 1 256 ? -11.575 1.502   36.276  1.00 34.69 ? 257 LYS A NZ  1 
ATOM   2054 N  N   . ALA A 1 257 ? -16.181 -3.853  33.660  1.00 16.42 ? 258 ALA A N   1 
ATOM   2055 C  CA  . ALA A 1 257 ? -17.219 -4.458  32.821  1.00 17.96 ? 258 ALA A CA  1 
ATOM   2056 C  C   . ALA A 1 257 ? -18.507 -3.702  33.018  1.00 17.79 ? 258 ALA A C   1 
ATOM   2057 O  O   . ALA A 1 257 ? -18.829 -3.235  34.132  1.00 18.63 ? 258 ALA A O   1 
ATOM   2058 C  CB  . ALA A 1 257 ? -17.391 -5.968  33.064  1.00 17.52 ? 258 ALA A CB  1 
ATOM   2059 N  N   . SER A 1 258 ? -19.236 -3.531  31.917  1.00 18.82 ? 259 SER A N   1 
ATOM   2060 C  CA  . SER A 1 258 ? -20.529 -2.818  31.936  1.00 19.97 ? 259 SER A CA  1 
ATOM   2061 C  C   . SER A 1 258 ? -21.672 -3.766  32.350  1.00 21.20 ? 259 SER A C   1 
ATOM   2062 O  O   . SER A 1 258 ? -22.832 -3.367  32.386  1.00 22.86 ? 259 SER A O   1 
ATOM   2063 C  CB  . SER A 1 258 ? -20.823 -2.221  30.555  1.00 19.09 ? 259 SER A CB  1 
ATOM   2064 O  OG  . SER A 1 258 ? -21.289 -3.223  29.658  1.00 18.93 ? 259 SER A OG  1 
ATOM   2065 N  N   . PHE A 1 259 ? -21.334 -5.016  32.657  1.00 22.37 ? 260 PHE A N   1 
ATOM   2066 C  CA  . PHE A 1 259 ? -22.293 -6.130  32.819  1.00 23.21 ? 260 PHE A CA  1 
ATOM   2067 C  C   . PHE A 1 259 ? -21.738 -7.167  33.813  1.00 25.68 ? 260 PHE A C   1 
ATOM   2068 O  O   . PHE A 1 259 ? -20.517 -7.168  34.093  1.00 25.09 ? 260 PHE A O   1 
ATOM   2069 C  CB  . PHE A 1 259 ? -22.540 -6.808  31.478  1.00 23.17 ? 260 PHE A CB  1 
ATOM   2070 C  CG  . PHE A 1 259 ? -21.318 -7.547  30.927  1.00 21.18 ? 260 PHE A CG  1 
ATOM   2071 C  CD1 . PHE A 1 259 ? -20.314 -6.839  30.228  1.00 19.46 ? 260 PHE A CD1 1 
ATOM   2072 C  CD2 . PHE A 1 259 ? -21.158 -8.926  31.152  1.00 20.56 ? 260 PHE A CD2 1 
ATOM   2073 C  CE1 . PHE A 1 259 ? -19.185 -7.507  29.745  1.00 21.08 ? 260 PHE A CE1 1 
ATOM   2074 C  CE2 . PHE A 1 259 ? -20.039 -9.599  30.710  1.00 20.78 ? 260 PHE A CE2 1 
ATOM   2075 C  CZ  . PHE A 1 259 ? -19.043 -8.873  29.965  1.00 21.30 ? 260 PHE A CZ  1 
ATOM   2076 N  N   . LYS A 1 260 ? -22.611 -8.044  34.351  1.00 28.16 ? 261 LYS A N   1 
ATOM   2077 C  CA  . LYS A 1 260 ? -22.151 -9.275  35.095  1.00 31.12 ? 261 LYS A CA  1 
ATOM   2078 C  C   . LYS A 1 260 ? -22.535 -10.520 34.291  1.00 31.86 ? 261 LYS A C   1 
ATOM   2079 O  O   . LYS A 1 260 ? -23.570 -10.509 33.598  1.00 33.20 ? 261 LYS A O   1 
ATOM   2080 C  CB  . LYS A 1 260 ? -22.708 -9.409  36.520  1.00 30.92 ? 261 LYS A CB  1 
ATOM   2081 C  CG  . LYS A 1 260 ? -21.897 -8.652  37.605  1.00 32.81 ? 261 LYS A CG  1 
ATOM   2082 C  CD  . LYS A 1 260 ? -22.226 -9.105  39.036  1.00 32.38 ? 261 LYS A CD  1 
ATOM   2083 C  CE  . LYS A 1 260 ? -23.546 -8.519  39.526  0.01 32.51 ? 261 LYS A CE  1 
ATOM   2084 N  NZ  . LYS A 1 260 ? -23.879 -8.973  40.904  0.01 32.49 ? 261 LYS A NZ  1 
ATOM   2085 O  OXT . LYS A 1 260 ? -21.833 -11.531 34.321  1.00 30.00 ? 261 LYS A OXT 1 
HETATM 2086 ZN ZN  . ZN  B 2 .   ? -6.593  -1.797  15.194  1.00 11.61 ? 301 ZN  A ZN  1 
HETATM 2087 O  O18 . E1F C 3 .   ? -5.281  0.999   18.223  1.00 11.42 ? 302 E1F A O18 1 
HETATM 2088 C  C13 . E1F C 3 .   ? -1.154  8.334   15.024  1.00 21.93 ? 302 E1F A C13 1 
HETATM 2089 C  C1  . E1F C 3 .   ? -4.177  4.032   14.012  1.00 16.44 ? 302 E1F A C1  1 
HETATM 2090 C  C2  . E1F C 3 .   ? -5.592  3.400   15.816  1.00 13.30 ? 302 E1F A C2  1 
HETATM 2091 CL CL1 . E1F C 3 .   ? -6.664  3.865   17.111  1.00 12.91 ? 302 E1F A CL1 1 
HETATM 2092 C  C21 . E1F C 3 .   ? -5.094  4.410   14.997  1.00 14.07 ? 302 E1F A C21 1 
HETATM 2093 C  C5  . E1F C 3 .   ? -3.788  2.684   13.784  1.00 12.16 ? 302 E1F A C5  1 
HETATM 2094 C  C4  . E1F C 3 .   ? -4.297  1.663   14.607  1.00 14.12 ? 302 E1F A C4  1 
HETATM 2095 C  C3  . E1F C 3 .   ? -5.181  2.052   15.615  1.00 13.05 ? 302 E1F A C3  1 
HETATM 2096 S  S16 . E1F C 3 .   ? -5.806  0.742   16.681  1.00 12.75 ? 302 E1F A S16 1 
HETATM 2097 N  N19 . E1F C 3 .   ? -5.016  -0.701  16.116  1.00 12.53 ? 302 E1F A N19 1 
HETATM 2098 O  O17 . E1F C 3 .   ? -7.350  0.813   16.603  1.00 9.86  ? 302 E1F A O17 1 
HETATM 2099 C  C6  . E1F C 3 .   ? -3.626  5.121   13.182  1.00 17.99 ? 302 E1F A C6  1 
HETATM 2100 O  O12 . E1F C 3 .   ? -4.321  6.105   12.900  1.00 20.77 ? 302 E1F A O12 1 
HETATM 2101 C  C7  . E1F C 3 .   ? -2.190  4.996   12.794  1.00 23.20 ? 302 E1F A C7  1 
HETATM 2102 S  S8  . E1F C 3 .   ? -1.894  6.325   11.590  1.00 25.43 ? 302 E1F A S8  1 
HETATM 2103 C  C9  . E1F C 3 .   ? -1.518  7.583   12.789  1.00 27.20 ? 302 E1F A C9  1 
HETATM 2104 N  N11 . E1F C 3 .   ? -1.310  8.832   12.259  1.00 27.64 ? 302 E1F A N11 1 
HETATM 2105 C  C14 . E1F C 3 .   ? -1.034  9.854   13.140  1.00 27.11 ? 302 E1F A C14 1 
HETATM 2106 C  C15 . E1F C 3 .   ? -0.945  9.607   14.530  1.00 23.91 ? 302 E1F A C15 1 
HETATM 2107 N  N10 . E1F C 3 .   ? -1.461  7.329   14.149  1.00 20.13 ? 302 E1F A N10 1 
HETATM 2108 S  S   . DMS D 4 .   ? 1.502   -11.795 14.907  1.00 26.68 ? 303 DMS A S   1 
HETATM 2109 O  O   . DMS D 4 .   ? 2.567   -10.572 14.075  1.00 25.68 ? 303 DMS A O   1 
HETATM 2110 C  C1  . DMS D 4 .   ? 1.988   -13.467 14.472  1.00 22.79 ? 303 DMS A C1  1 
HETATM 2111 C  C2  . DMS D 4 .   ? 2.010   -11.731 16.650  1.00 25.53 ? 303 DMS A C2  1 
HETATM 2112 O  O1  . MES E 5 .   ? -7.212  -9.186  -2.616  1.00 26.42 ? 304 MES A O1  1 
HETATM 2113 C  C2  . MES E 5 .   ? -7.475  -9.861  -3.925  1.00 25.23 ? 304 MES A C2  1 
HETATM 2114 C  C3  . MES E 5 .   ? -8.745  -10.781 -4.057  1.00 29.42 ? 304 MES A C3  1 
HETATM 2115 N  N4  . MES E 5 .   ? -9.832  -10.687 -3.086  1.00 29.28 ? 304 MES A N4  1 
HETATM 2116 C  C5  . MES E 5 .   ? -9.463  -10.085 -1.767  1.00 26.98 ? 304 MES A C5  1 
HETATM 2117 C  C6  . MES E 5 .   ? -8.196  -9.445  -1.580  1.00 22.52 ? 304 MES A C6  1 
HETATM 2118 C  C7  . MES E 5 .   ? -11.269 -11.216 -3.279  1.00 29.15 ? 304 MES A C7  1 
HETATM 2119 O  O   . HOH F 6 .   ? -4.501  -13.458 17.827  1.00 9.32  ? 401 HOH A O   1 
HETATM 2120 O  O   . HOH F 6 .   ? -2.411  -8.655  28.964  1.00 9.72  ? 402 HOH A O   1 
HETATM 2121 O  O   . HOH F 6 .   ? -16.888 -8.417  20.384  1.00 8.42  ? 403 HOH A O   1 
HETATM 2122 O  O   . HOH F 6 .   ? -14.048 10.352  27.617  1.00 14.87 ? 404 HOH A O   1 
HETATM 2123 O  O   . HOH F 6 .   ? -10.624 8.739   25.461  1.00 17.11 ? 405 HOH A O   1 
HETATM 2124 O  O   . HOH F 6 .   ? -1.246  -4.114  15.597  1.00 7.88  ? 406 HOH A O   1 
HETATM 2125 O  O   . HOH F 6 .   ? -5.233  1.431   10.548  1.00 17.25 ? 407 HOH A O   1 
HETATM 2126 O  O   . HOH F 6 .   ? -21.514 -7.157  23.466  1.00 13.28 ? 408 HOH A O   1 
HETATM 2127 O  O   . HOH F 6 .   ? 3.870   5.002   29.475  1.00 17.48 ? 409 HOH A O   1 
HETATM 2128 O  O   . HOH F 6 .   ? -3.376  -13.272 25.160  1.00 14.04 ? 410 HOH A O   1 
HETATM 2129 O  O   . HOH F 6 .   ? -17.868 -20.601 8.056   1.00 14.89 ? 411 HOH A O   1 
HETATM 2130 O  O   . HOH F 6 .   ? -21.665 5.546   4.661   1.00 17.76 ? 412 HOH A O   1 
HETATM 2131 O  O   . HOH F 6 .   ? 7.626   6.182   21.533  1.00 18.96 ? 413 HOH A O   1 
HETATM 2132 O  O   . HOH F 6 .   ? -16.314 -9.919  32.824  1.00 17.95 ? 414 HOH A O   1 
HETATM 2133 O  O   . HOH F 6 .   ? -2.378  -2.947  11.315  1.00 17.46 ? 415 HOH A O   1 
HETATM 2134 O  O   . HOH F 6 .   ? 4.914   -5.066  20.812  1.00 16.96 ? 416 HOH A O   1 
HETATM 2135 O  O   . HOH F 6 .   ? -3.683  -15.917 24.293  1.00 14.67 ? 417 HOH A O   1 
HETATM 2136 O  O   . HOH F 6 .   ? 1.370   -1.737  29.281  1.00 16.90 ? 418 HOH A O   1 
HETATM 2137 O  O   . HOH F 6 .   ? 8.531   -3.669  20.922  1.00 21.98 ? 419 HOH A O   1 
HETATM 2138 O  O   . HOH F 6 .   ? -21.998 -18.421 13.763  1.00 27.44 ? 420 HOH A O   1 
HETATM 2139 O  O   . HOH F 6 .   ? -21.075 -12.614 -1.876  1.00 22.66 ? 421 HOH A O   1 
HETATM 2140 O  O   . HOH F 6 .   ? -17.789 10.378  11.363  1.00 21.14 ? 422 HOH A O   1 
HETATM 2141 O  O   . HOH F 6 .   ? -28.709 -5.987  24.551  1.00 21.49 ? 423 HOH A O   1 
HETATM 2142 O  O   . HOH F 6 .   ? -2.039  -12.469 22.871  1.00 15.19 ? 424 HOH A O   1 
HETATM 2143 O  O   . HOH F 6 .   ? 8.201   -5.694  -10.610 1.00 19.92 ? 425 HOH A O   1 
HETATM 2144 O  O   . HOH F 6 .   ? -3.476  -11.056 20.833  1.00 13.62 ? 426 HOH A O   1 
HETATM 2145 O  O   . HOH F 6 .   ? -12.694 -17.352 16.901  1.00 19.95 ? 427 HOH A O   1 
HETATM 2146 O  O   . HOH F 6 .   ? -13.365 -18.679 14.765  1.00 17.72 ? 428 HOH A O   1 
HETATM 2147 O  O   . HOH F 6 .   ? -23.957 -0.875  26.354  1.00 18.13 ? 429 HOH A O   1 
HETATM 2148 O  O   . HOH F 6 .   ? -10.275 -18.207 16.970  1.00 16.31 ? 430 HOH A O   1 
HETATM 2149 O  O   . HOH F 6 .   ? 2.570   -12.992 5.117   1.00 25.75 ? 431 HOH A O   1 
HETATM 2150 O  O   . HOH F 6 .   ? -14.259 -16.589 28.851  1.00 28.86 ? 432 HOH A O   1 
HETATM 2151 O  O   . HOH F 6 .   ? -9.624  -7.993  33.954  1.00 20.76 ? 433 HOH A O   1 
HETATM 2152 O  O   . HOH F 6 .   ? -17.728 -21.242 17.651  1.00 23.43 ? 434 HOH A O   1 
HETATM 2153 O  O   . HOH F 6 .   ? -7.839  -15.420 11.232  1.00 14.39 ? 435 HOH A O   1 
HETATM 2154 O  O   . HOH F 6 .   ? -7.882  -19.378 21.554  1.00 19.84 ? 436 HOH A O   1 
HETATM 2155 O  O   . HOH F 6 .   ? 2.659   -11.349 9.631   1.00 22.66 ? 437 HOH A O   1 
HETATM 2156 O  O   . HOH F 6 .   ? -8.759  -3.884  7.817   1.00 18.75 ? 438 HOH A O   1 
HETATM 2157 O  O   . HOH F 6 .   ? -24.621 -7.727  8.960   1.00 17.71 ? 439 HOH A O   1 
HETATM 2158 O  O   . HOH F 6 .   ? -16.268 -12.477 24.199  1.00 24.65 ? 440 HOH A O   1 
HETATM 2159 O  O   . HOH F 6 .   ? -4.556  -15.891 0.896   1.00 28.64 ? 441 HOH A O   1 
HETATM 2160 O  O   . HOH F 6 .   ? -18.544 -9.152  34.396  1.00 21.40 ? 442 HOH A O   1 
HETATM 2161 O  O   . HOH F 6 .   ? -25.750 -6.034  12.991  1.00 26.10 ? 443 HOH A O   1 
HETATM 2162 O  O   . HOH F 6 .   ? -11.831 2.989   30.677  1.00 21.05 ? 444 HOH A O   1 
HETATM 2163 O  O   . HOH F 6 .   ? 4.410   -3.347  26.245  1.00 20.11 ? 445 HOH A O   1 
HETATM 2164 O  O   . HOH F 6 .   ? -20.230 10.893  26.630  1.00 19.82 ? 446 HOH A O   1 
HETATM 2165 O  O   . HOH F 6 .   ? 5.348   7.183   19.799  1.00 21.02 ? 447 HOH A O   1 
HETATM 2166 O  O   . HOH F 6 .   ? -0.218  -11.230 28.555  1.00 31.85 ? 448 HOH A O   1 
HETATM 2167 O  O   . HOH F 6 .   ? -7.176  -8.856  32.549  1.00 21.19 ? 449 HOH A O   1 
HETATM 2168 O  O   . HOH F 6 .   ? -27.592 2.543   23.303  1.00 46.83 ? 450 HOH A O   1 
HETATM 2169 O  O   . HOH F 6 .   ? -23.828 -0.863  3.937   1.00 16.60 ? 451 HOH A O   1 
HETATM 2170 O  O   . HOH F 6 .   ? -3.009  -0.236  10.647  1.00 21.63 ? 452 HOH A O   1 
HETATM 2171 O  O   . HOH F 6 .   ? -8.085  -22.224 10.214  1.00 19.91 ? 453 HOH A O   1 
HETATM 2172 O  O   . HOH F 6 .   ? -22.711 -5.753  2.844   1.00 19.60 ? 454 HOH A O   1 
HETATM 2173 O  O   . HOH F 6 .   ? 4.348   -2.522  28.567  1.00 30.17 ? 455 HOH A O   1 
HETATM 2174 O  O   . HOH F 6 .   ? -23.404 -0.849  34.071  1.00 21.87 ? 456 HOH A O   1 
HETATM 2175 O  O   . HOH F 6 .   ? 0.018   0.967   34.258  1.00 27.00 ? 457 HOH A O   1 
HETATM 2176 O  O   . HOH F 6 .   ? -1.425  -13.253 27.254  1.00 30.08 ? 458 HOH A O   1 
HETATM 2177 O  O   . HOH F 6 .   ? -1.837  -17.569 25.522  1.00 30.55 ? 459 HOH A O   1 
HETATM 2178 O  O   . HOH F 6 .   ? -26.747 -2.834  14.203  1.00 22.03 ? 460 HOH A O   1 
HETATM 2179 O  O   . HOH F 6 .   ? -21.678 -13.868 23.182  1.00 26.05 ? 461 HOH A O   1 
HETATM 2180 O  O   . HOH F 6 .   ? 1.699   -17.414 6.702   1.00 31.83 ? 462 HOH A O   1 
HETATM 2181 O  O   . HOH F 6 .   ? 1.447   -11.910 24.943  1.00 20.76 ? 463 HOH A O   1 
HETATM 2182 O  O   . HOH F 6 .   ? -5.811  -4.570  -6.562  1.00 22.83 ? 464 HOH A O   1 
HETATM 2183 O  O   . HOH F 6 .   ? -3.457  -13.117 -2.822  1.00 27.68 ? 465 HOH A O   1 
HETATM 2184 O  O   . HOH F 6 .   ? -8.916  -6.157  35.595  1.00 19.46 ? 466 HOH A O   1 
HETATM 2185 O  O   . HOH F 6 .   ? -31.145 4.123   7.784   1.00 26.62 ? 467 HOH A O   1 
HETATM 2186 O  O   . HOH F 6 .   ? -23.936 8.697   19.832  1.00 26.83 ? 468 HOH A O   1 
HETATM 2187 O  O   . HOH F 6 .   ? -17.896 19.035  5.841   1.00 18.92 ? 469 HOH A O   1 
HETATM 2188 O  O   . HOH F 6 .   ? 0.428   -1.114  -4.462  1.00 28.40 ? 470 HOH A O   1 
HETATM 2189 O  O   . HOH F 6 .   ? 1.372   -6.475  34.297  1.00 22.34 ? 471 HOH A O   1 
HETATM 2190 O  O   . HOH F 6 .   ? 2.906   -4.308  7.640   1.00 20.70 ? 472 HOH A O   1 
HETATM 2191 O  O   . HOH F 6 .   ? -10.930 -19.468 7.086   1.00 27.64 ? 473 HOH A O   1 
HETATM 2192 O  O   . HOH F 6 .   ? -13.029 -8.885  -3.126  1.00 32.47 ? 474 HOH A O   1 
HETATM 2193 O  O   . HOH F 6 .   ? -22.988 -2.963  6.591   1.00 19.30 ? 475 HOH A O   1 
HETATM 2194 O  O   . HOH F 6 .   ? -18.136 3.599   -3.773  1.00 30.36 ? 476 HOH A O   1 
HETATM 2195 O  O   . HOH F 6 .   ? -16.325 5.202   -7.819  1.00 25.54 ? 477 HOH A O   1 
HETATM 2196 O  O   . HOH F 6 .   ? -23.419 -13.500 11.498  1.00 32.77 ? 478 HOH A O   1 
HETATM 2197 O  O   . HOH F 6 .   ? -17.097 -16.509 21.546  1.00 28.47 ? 479 HOH A O   1 
HETATM 2198 O  O   . HOH F 6 .   ? 6.144   -5.227  3.655   1.00 32.29 ? 480 HOH A O   1 
HETATM 2199 O  O   . HOH F 6 .   ? -5.119  3.479   -5.792  1.00 30.44 ? 481 HOH A O   1 
HETATM 2200 O  O   . HOH F 6 .   ? -30.913 -6.788  22.157  1.00 30.97 ? 482 HOH A O   1 
HETATM 2201 O  O   . HOH F 6 .   ? -12.163 12.783  29.029  1.00 26.24 ? 483 HOH A O   1 
HETATM 2202 O  O   . HOH F 6 .   ? 3.689   9.772   23.563  1.00 26.71 ? 484 HOH A O   1 
HETATM 2203 O  O   . HOH F 6 .   ? 0.138   3.339   9.931   1.00 23.78 ? 485 HOH A O   1 
HETATM 2204 O  O   . HOH F 6 .   ? -1.289  1.672   11.325  1.00 21.54 ? 486 HOH A O   1 
HETATM 2205 O  O   . HOH F 6 .   ? -4.344  3.980   10.086  1.00 20.34 ? 487 HOH A O   1 
HETATM 2206 O  O   . HOH F 6 .   ? -2.457  4.368   8.425   1.00 24.19 ? 488 HOH A O   1 
HETATM 2207 O  O   . HOH F 6 .   ? 1.140   2.913   2.337   1.00 24.74 ? 489 HOH A O   1 
HETATM 2208 O  O   . HOH F 6 .   ? 4.422   -6.581  7.796   1.00 23.20 ? 490 HOH A O   1 
HETATM 2209 O  O   . HOH F 6 .   ? 8.487   -4.825  23.935  1.00 34.72 ? 491 HOH A O   1 
HETATM 2210 O  O   . HOH F 6 .   ? 15.527  3.240   20.340  1.00 34.91 ? 492 HOH A O   1 
HETATM 2211 O  O   . HOH F 6 .   ? -0.264  10.913  23.130  1.00 21.13 ? 493 HOH A O   1 
HETATM 2212 O  O   . HOH F 6 .   ? -1.306  11.329  25.511  1.00 31.37 ? 494 HOH A O   1 
HETATM 2213 O  O   . HOH F 6 .   ? -0.484  -8.514  32.195  1.00 22.19 ? 495 HOH A O   1 
HETATM 2214 O  O   . HOH F 6 .   ? -27.792 4.806   24.824  1.00 28.86 ? 496 HOH A O   1 
HETATM 2215 O  O   . HOH F 6 .   ? -24.806 4.608   8.166   1.00 27.83 ? 497 HOH A O   1 
HETATM 2216 O  O   . HOH F 6 .   ? -19.204 10.098  8.714   1.00 18.54 ? 498 HOH A O   1 
HETATM 2217 O  O   . HOH F 6 .   ? -13.145 18.692  11.734  1.00 29.89 ? 499 HOH A O   1 
HETATM 2218 O  O   . HOH F 6 .   ? -10.017 14.651  12.050  1.00 17.74 ? 500 HOH A O   1 
HETATM 2219 O  O   . HOH F 6 .   ? -24.704 -9.345  2.188   1.00 23.93 ? 501 HOH A O   1 
HETATM 2220 O  O   . HOH F 6 .   ? -17.251 -8.392  -6.321  1.00 35.70 ? 502 HOH A O   1 
HETATM 2221 O  O   . HOH F 6 .   ? -0.808  9.208   9.579   1.00 35.45 ? 503 HOH A O   1 
HETATM 2222 O  O   . HOH F 6 .   ? -0.467  8.117   7.075   1.00 32.11 ? 504 HOH A O   1 
HETATM 2223 O  O   . HOH F 6 .   ? -6.343  6.581   10.444  1.00 30.93 ? 505 HOH A O   1 
HETATM 2224 O  O   . HOH F 6 .   ? -23.888 -6.716  0.191   1.00 31.50 ? 506 HOH A O   1 
HETATM 2225 O  O   . HOH F 6 .   ? 1.285   8.847   24.094  1.00 17.40 ? 507 HOH A O   1 
HETATM 2226 O  O   . HOH F 6 .   ? -1.117  9.187   27.897  1.00 24.95 ? 508 HOH A O   1 
HETATM 2227 O  O   . HOH F 6 .   ? -6.921  -14.798 31.513  1.00 22.92 ? 509 HOH A O   1 
HETATM 2228 O  O   . HOH F 6 .   ? -24.659 0.041   1.951   1.00 36.48 ? 510 HOH A O   1 
HETATM 2229 O  O   . HOH F 6 .   ? -13.767 14.348  27.066  1.00 34.58 ? 511 HOH A O   1 
HETATM 2230 O  O   . HOH F 6 .   ? -16.244 15.709  23.551  1.00 33.24 ? 512 HOH A O   1 
HETATM 2231 O  O   . HOH F 6 .   ? 9.127   2.085   11.947  1.00 29.39 ? 513 HOH A O   1 
HETATM 2232 O  O   . HOH F 6 .   ? -4.197  -15.490 -2.248  1.00 29.50 ? 514 HOH A O   1 
HETATM 2233 O  O   . HOH F 6 .   ? -7.093  -19.963 19.335  1.00 22.49 ? 515 HOH A O   1 
HETATM 2234 O  O   . HOH F 6 .   ? 13.922  -3.877  10.474  1.00 35.37 ? 516 HOH A O   1 
HETATM 2235 O  O   . HOH F 6 .   ? 6.205   -6.839  22.884  1.00 33.88 ? 517 HOH A O   1 
HETATM 2236 O  O   . HOH F 6 .   ? -15.976 -10.226 36.671  1.00 30.92 ? 518 HOH A O   1 
HETATM 2237 O  O   . HOH F 6 .   ? -15.450 9.208   -1.910  1.00 27.46 ? 519 HOH A O   1 
HETATM 2238 O  O   . HOH F 6 .   ? 2.190   -9.903  29.989  1.00 27.73 ? 520 HOH A O   1 
HETATM 2239 O  O   . HOH F 6 .   ? -23.105 -11.740 14.231  1.00 26.32 ? 521 HOH A O   1 
HETATM 2240 O  O   . HOH F 6 .   ? -25.135 -10.508 17.370  1.00 28.27 ? 522 HOH A O   1 
HETATM 2241 O  O   . HOH F 6 .   ? 0.277   0.850   -6.503  1.00 31.56 ? 523 HOH A O   1 
HETATM 2242 O  O   . HOH F 6 .   ? -26.600 -3.942  25.040  1.00 23.94 ? 524 HOH A O   1 
HETATM 2243 O  O   . HOH F 6 .   ? 13.381  0.364   24.331  1.00 23.22 ? 525 HOH A O   1 
HETATM 2244 O  O   . HOH F 6 .   ? 11.367  1.316   25.627  1.00 25.19 ? 526 HOH A O   1 
HETATM 2245 O  O   . HOH F 6 .   ? 8.473   2.963   27.550  1.00 22.35 ? 527 HOH A O   1 
HETATM 2246 O  O   . HOH F 6 .   ? 6.569   5.421   28.510  1.00 37.92 ? 528 HOH A O   1 
HETATM 2247 O  O   . HOH F 6 .   ? 0.991   -19.130 10.357  1.00 29.93 ? 529 HOH A O   1 
HETATM 2248 O  O   . HOH F 6 .   ? -1.236  -17.675 4.885   1.00 31.59 ? 530 HOH A O   1 
HETATM 2249 O  O   . HOH F 6 .   ? 13.078  -3.802  13.340  1.00 25.54 ? 531 HOH A O   1 
HETATM 2250 O  O   . HOH F 6 .   ? -10.763 -15.591 33.977  1.00 28.65 ? 532 HOH A O   1 
HETATM 2251 O  O   . HOH F 6 .   ? -20.768 8.275   30.001  1.00 26.18 ? 533 HOH A O   1 
HETATM 2252 O  O   . HOH F 6 .   ? -25.482 9.617   13.120  1.00 30.20 ? 534 HOH A O   1 
HETATM 2253 O  O   . HOH F 6 .   ? -13.779 14.758  6.110   1.00 36.54 ? 535 HOH A O   1 
HETATM 2254 O  O   . HOH F 6 .   ? -13.803 19.873  14.816  1.00 31.50 ? 536 HOH A O   1 
HETATM 2255 O  O   . HOH F 6 .   ? -14.541 -18.649 18.816  1.00 27.83 ? 537 HOH A O   1 
HETATM 2256 O  O   . HOH F 6 .   ? -6.193  -19.739 23.968  1.00 25.92 ? 538 HOH A O   1 
HETATM 2257 O  O   . HOH F 6 .   ? -12.919 -16.861 26.586  1.00 25.66 ? 539 HOH A O   1 
HETATM 2258 O  O   . HOH F 6 .   ? -16.437 -15.265 32.575  1.00 36.12 ? 540 HOH A O   1 
HETATM 2259 O  O   . HOH F 6 .   ? 1.697   12.546  22.765  1.00 32.30 ? 541 HOH A O   1 
HETATM 2260 O  O   . HOH F 6 .   ? -19.618 -17.209 3.087   1.00 26.09 ? 542 HOH A O   1 
HETATM 2261 O  O   . HOH F 6 .   ? -7.844  7.073   27.458  1.00 33.94 ? 543 HOH A O   1 
HETATM 2262 O  O   . HOH F 6 .   ? -17.248 -23.127 3.802   1.00 33.65 ? 544 HOH A O   1 
HETATM 2263 O  O   . HOH F 6 .   ? 1.977   -15.638 9.132   1.00 26.98 ? 545 HOH A O   1 
HETATM 2264 O  O   . HOH F 6 .   ? -5.003  -12.088 31.980  1.00 29.20 ? 546 HOH A O   1 
HETATM 2265 O  O   . HOH F 6 .   ? -27.839 11.900  5.328   1.00 36.99 ? 547 HOH A O   1 
HETATM 2266 O  O   . HOH F 6 .   ? -16.989 -13.896 26.252  1.00 22.16 ? 548 HOH A O   1 
HETATM 2267 O  O   . HOH F 6 .   ? -14.944 -16.461 25.206  1.00 30.04 ? 549 HOH A O   1 
HETATM 2268 O  O   . HOH F 6 .   ? 10.069  -4.920  -7.736  1.00 32.20 ? 550 HOH A O   1 
HETATM 2269 O  O   . HOH F 6 .   ? -18.750 -12.108 -3.328  1.00 24.83 ? 551 HOH A O   1 
HETATM 2270 O  O   . HOH F 6 .   ? -1.361  -17.785 17.695  1.00 21.85 ? 552 HOH A O   1 
HETATM 2271 O  O   . HOH F 6 .   ? -14.912 19.768  17.492  1.00 33.16 ? 553 HOH A O   1 
HETATM 2272 O  O   . HOH F 6 .   ? -7.022  5.991   6.359   1.00 31.18 ? 554 HOH A O   1 
HETATM 2273 O  O   . HOH F 6 .   ? -21.341 18.820  13.526  1.00 40.18 ? 555 HOH A O   1 
HETATM 2274 O  O   . HOH F 6 .   ? -8.101  -15.184 36.712  1.00 26.27 ? 556 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 E1F 1   302 1   E1F E18 A . 
D 4 DMS 1   303 1   DMS DMS A . 
E 5 MES 1   304 2   MES MES A . 
F 6 HOH 1   401 1   HOH HOH A . 
F 6 HOH 2   402 2   HOH HOH A . 
F 6 HOH 3   403 3   HOH HOH A . 
F 6 HOH 4   404 4   HOH HOH A . 
F 6 HOH 5   405 5   HOH HOH A . 
F 6 HOH 6   406 6   HOH HOH A . 
F 6 HOH 7   407 7   HOH HOH A . 
F 6 HOH 8   408 8   HOH HOH A . 
F 6 HOH 9   409 9   HOH HOH A . 
F 6 HOH 10  410 10  HOH HOH A . 
F 6 HOH 11  411 11  HOH HOH A . 
F 6 HOH 12  412 12  HOH HOH A . 
F 6 HOH 13  413 13  HOH HOH A . 
F 6 HOH 14  414 14  HOH HOH A . 
F 6 HOH 15  415 15  HOH HOH A . 
F 6 HOH 16  416 16  HOH HOH A . 
F 6 HOH 17  417 17  HOH HOH A . 
F 6 HOH 18  418 18  HOH HOH A . 
F 6 HOH 19  419 19  HOH HOH A . 
F 6 HOH 20  420 20  HOH HOH A . 
F 6 HOH 21  421 21  HOH HOH A . 
F 6 HOH 22  422 22  HOH HOH A . 
F 6 HOH 23  423 23  HOH HOH A . 
F 6 HOH 24  424 24  HOH HOH A . 
F 6 HOH 25  425 25  HOH HOH A . 
F 6 HOH 26  426 26  HOH HOH A . 
F 6 HOH 27  427 27  HOH HOH A . 
F 6 HOH 28  428 28  HOH HOH A . 
F 6 HOH 29  429 29  HOH HOH A . 
F 6 HOH 30  430 30  HOH HOH A . 
F 6 HOH 31  431 31  HOH HOH A . 
F 6 HOH 32  432 32  HOH HOH A . 
F 6 HOH 33  433 33  HOH HOH A . 
F 6 HOH 34  434 34  HOH HOH A . 
F 6 HOH 35  435 35  HOH HOH A . 
F 6 HOH 36  436 36  HOH HOH A . 
F 6 HOH 37  437 37  HOH HOH A . 
F 6 HOH 38  438 38  HOH HOH A . 
F 6 HOH 39  439 39  HOH HOH A . 
F 6 HOH 40  440 40  HOH HOH A . 
F 6 HOH 41  441 41  HOH HOH A . 
F 6 HOH 42  442 42  HOH HOH A . 
F 6 HOH 43  443 43  HOH HOH A . 
F 6 HOH 44  444 44  HOH HOH A . 
F 6 HOH 45  445 45  HOH HOH A . 
F 6 HOH 46  446 46  HOH HOH A . 
F 6 HOH 47  447 47  HOH HOH A . 
F 6 HOH 48  448 48  HOH HOH A . 
F 6 HOH 49  449 49  HOH HOH A . 
F 6 HOH 50  450 50  HOH HOH A . 
F 6 HOH 51  451 51  HOH HOH A . 
F 6 HOH 52  452 52  HOH HOH A . 
F 6 HOH 53  453 53  HOH HOH A . 
F 6 HOH 54  454 54  HOH HOH A . 
F 6 HOH 55  455 55  HOH HOH A . 
F 6 HOH 56  456 56  HOH HOH A . 
F 6 HOH 57  457 57  HOH HOH A . 
F 6 HOH 58  458 58  HOH HOH A . 
F 6 HOH 59  459 59  HOH HOH A . 
F 6 HOH 60  460 60  HOH HOH A . 
F 6 HOH 61  461 61  HOH HOH A . 
F 6 HOH 62  462 62  HOH HOH A . 
F 6 HOH 63  463 63  HOH HOH A . 
F 6 HOH 64  464 64  HOH HOH A . 
F 6 HOH 65  465 65  HOH HOH A . 
F 6 HOH 66  466 66  HOH HOH A . 
F 6 HOH 67  467 67  HOH HOH A . 
F 6 HOH 68  468 68  HOH HOH A . 
F 6 HOH 69  469 69  HOH HOH A . 
F 6 HOH 70  470 70  HOH HOH A . 
F 6 HOH 71  471 71  HOH HOH A . 
F 6 HOH 72  472 72  HOH HOH A . 
F 6 HOH 73  473 73  HOH HOH A . 
F 6 HOH 74  474 74  HOH HOH A . 
F 6 HOH 75  475 75  HOH HOH A . 
F 6 HOH 76  476 76  HOH HOH A . 
F 6 HOH 77  477 77  HOH HOH A . 
F 6 HOH 78  478 78  HOH HOH A . 
F 6 HOH 79  479 79  HOH HOH A . 
F 6 HOH 80  480 80  HOH HOH A . 
F 6 HOH 81  481 81  HOH HOH A . 
F 6 HOH 82  482 82  HOH HOH A . 
F 6 HOH 83  483 83  HOH HOH A . 
F 6 HOH 84  484 84  HOH HOH A . 
F 6 HOH 85  485 85  HOH HOH A . 
F 6 HOH 86  486 86  HOH HOH A . 
F 6 HOH 87  487 87  HOH HOH A . 
F 6 HOH 88  488 88  HOH HOH A . 
F 6 HOH 89  489 89  HOH HOH A . 
F 6 HOH 90  490 90  HOH HOH A . 
F 6 HOH 91  491 91  HOH HOH A . 
F 6 HOH 92  492 92  HOH HOH A . 
F 6 HOH 93  493 93  HOH HOH A . 
F 6 HOH 94  494 94  HOH HOH A . 
F 6 HOH 95  495 95  HOH HOH A . 
F 6 HOH 96  496 96  HOH HOH A . 
F 6 HOH 97  497 97  HOH HOH A . 
F 6 HOH 98  498 98  HOH HOH A . 
F 6 HOH 99  499 99  HOH HOH A . 
F 6 HOH 100 500 100 HOH HOH A . 
F 6 HOH 101 501 101 HOH HOH A . 
F 6 HOH 102 502 102 HOH HOH A . 
F 6 HOH 103 503 103 HOH HOH A . 
F 6 HOH 104 504 104 HOH HOH A . 
F 6 HOH 105 505 105 HOH HOH A . 
F 6 HOH 106 506 106 HOH HOH A . 
F 6 HOH 107 507 107 HOH HOH A . 
F 6 HOH 108 508 108 HOH HOH A . 
F 6 HOH 109 509 109 HOH HOH A . 
F 6 HOH 110 510 110 HOH HOH A . 
F 6 HOH 111 511 111 HOH HOH A . 
F 6 HOH 112 512 112 HOH HOH A . 
F 6 HOH 113 513 113 HOH HOH A . 
F 6 HOH 114 514 114 HOH HOH A . 
F 6 HOH 115 515 115 HOH HOH A . 
F 6 HOH 116 516 116 HOH HOH A . 
F 6 HOH 117 517 117 HOH HOH A . 
F 6 HOH 118 518 118 HOH HOH A . 
F 6 HOH 119 519 119 HOH HOH A . 
F 6 HOH 120 520 120 HOH HOH A . 
F 6 HOH 121 521 121 HOH HOH A . 
F 6 HOH 122 522 122 HOH HOH A . 
F 6 HOH 123 523 123 HOH HOH A . 
F 6 HOH 124 524 124 HOH HOH A . 
F 6 HOH 125 525 125 HOH HOH A . 
F 6 HOH 126 526 126 HOH HOH A . 
F 6 HOH 127 527 127 HOH HOH A . 
F 6 HOH 128 528 128 HOH HOH A . 
F 6 HOH 129 529 129 HOH HOH A . 
F 6 HOH 130 530 130 HOH HOH A . 
F 6 HOH 131 531 131 HOH HOH A . 
F 6 HOH 132 532 132 HOH HOH A . 
F 6 HOH 133 533 133 HOH HOH A . 
F 6 HOH 134 534 134 HOH HOH A . 
F 6 HOH 135 535 135 HOH HOH A . 
F 6 HOH 136 536 136 HOH HOH A . 
F 6 HOH 137 537 137 HOH HOH A . 
F 6 HOH 138 538 138 HOH HOH A . 
F 6 HOH 139 539 139 HOH HOH A . 
F 6 HOH 140 540 140 HOH HOH A . 
F 6 HOH 141 541 141 HOH HOH A . 
F 6 HOH 142 542 142 HOH HOH A . 
F 6 HOH 143 543 143 HOH HOH A . 
F 6 HOH 144 544 144 HOH HOH A . 
F 6 HOH 145 545 145 HOH HOH A . 
F 6 HOH 146 546 146 HOH HOH A . 
F 6 HOH 147 547 147 HOH HOH A . 
F 6 HOH 148 548 148 HOH HOH A . 
F 6 HOH 149 549 149 HOH HOH A . 
F 6 HOH 150 550 150 HOH HOH A . 
F 6 HOH 151 551 151 HOH HOH A . 
F 6 HOH 152 552 152 HOH HOH A . 
F 6 HOH 153 553 153 HOH HOH A . 
F 6 HOH 154 554 154 HOH HOH A . 
F 6 HOH 155 555 155 HOH HOH A . 
F 6 HOH 156 556 156 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 106.5 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 118.4 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.7  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N19 ? C E1F .   ? A E1F 302 ? 1_555 110.0 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N19 ? C E1F .   ? A E1F 302 ? 1_555 106.2 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N19 ? C E1F .   ? A E1F 302 ? 1_555 115.3 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2013-11-06 
2 'Structure model' 1 1 2017-10-04 
3 'Structure model' 1 2 2023-11-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Refinement description' 
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Database references'    
5 3 'Structure model' 'Derived calculations'   
6 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  2 'Structure model' diffrn_detector               
2  2 'Structure model' software                      
3  3 'Structure model' chem_comp_atom                
4  3 'Structure model' chem_comp_bond                
5  3 'Structure model' database_2                    
6  3 'Structure model' diffrn_source                 
7  3 'Structure model' pdbx_initial_refinement_model 
8  3 'Structure model' pdbx_struct_conn_angle        
9  3 'Structure model' struct_conn                   
10 3 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_diffrn_detector.detector'                   
2  2 'Structure model' '_software.version'                           
3  3 'Structure model' '_database_2.pdbx_DOI'                        
4  3 'Structure model' '_database_2.pdbx_database_accession'         
5  3 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
12 3 'Structure model' '_pdbx_struct_conn_angle.value'               
13 3 'Structure model' '_struct_conn.pdbx_dist_value'                
14 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
15 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
16 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
17 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
18 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
19 3 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      5.2.0019 ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .        ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.3.20   2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006    'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
DNA         .        ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .        ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -141.39 11.16   
2 1 ARG A 27  ? ? -147.03 57.65   
3 1 LYS A 76  ? ? -108.61 -73.01  
4 1 LYS A 111 ? A 67.01   -1.25   
5 1 PHE A 176 ? ? -154.11 74.50   
6 1 ASN A 244 ? ? -93.70  53.37   
7 1 LYS A 252 ? ? 58.94   -138.82 
8 1 LYS A 252 ? ? 58.94   -135.40 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 A MES 304 ? C8  ? E MES 1 C8  
2 1 N 1 A MES 304 ? S   ? E MES 1 S   
3 1 N 1 A MES 304 ? O1S ? E MES 1 O1S 
4 1 N 1 A MES 304 ? O2S ? E MES 1 O2S 
5 1 N 1 A MES 304 ? O3S ? E MES 1 O3S 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
E1F O18  O  N N 98  
E1F C13  C  Y N 99  
E1F C1   C  Y N 100 
E1F C2   C  Y N 101 
E1F CL1  CL N N 102 
E1F C21  C  Y N 103 
E1F C5   C  Y N 104 
E1F C4   C  Y N 105 
E1F C3   C  Y N 106 
E1F S16  S  N N 107 
E1F N19  N  N N 108 
E1F O17  O  N N 109 
E1F C6   C  N N 110 
E1F O12  O  N N 111 
E1F C7   C  N N 112 
E1F S8   S  N N 113 
E1F C9   C  Y N 114 
E1F N11  N  Y N 115 
E1F C14  C  Y N 116 
E1F C15  C  Y N 117 
E1F N10  N  Y N 118 
E1F H1   H  N N 119 
E1F H2   H  N N 120 
E1F H3   H  N N 121 
E1F H4   H  N N 122 
E1F H5   H  N N 123 
E1F H6   H  N N 124 
E1F H7   H  N N 125 
E1F H8   H  N N 126 
E1F H9   H  N N 127 
E1F H10  H  N N 128 
GLN N    N  N N 129 
GLN CA   C  N S 130 
GLN C    C  N N 131 
GLN O    O  N N 132 
GLN CB   C  N N 133 
GLN CG   C  N N 134 
GLN CD   C  N N 135 
GLN OE1  O  N N 136 
GLN NE2  N  N N 137 
GLN OXT  O  N N 138 
GLN H    H  N N 139 
GLN H2   H  N N 140 
GLN HA   H  N N 141 
GLN HB2  H  N N 142 
GLN HB3  H  N N 143 
GLN HG2  H  N N 144 
GLN HG3  H  N N 145 
GLN HE21 H  N N 146 
GLN HE22 H  N N 147 
GLN HXT  H  N N 148 
GLU N    N  N N 149 
GLU CA   C  N S 150 
GLU C    C  N N 151 
GLU O    O  N N 152 
GLU CB   C  N N 153 
GLU CG   C  N N 154 
GLU CD   C  N N 155 
GLU OE1  O  N N 156 
GLU OE2  O  N N 157 
GLU OXT  O  N N 158 
GLU H    H  N N 159 
GLU H2   H  N N 160 
GLU HA   H  N N 161 
GLU HB2  H  N N 162 
GLU HB3  H  N N 163 
GLU HG2  H  N N 164 
GLU HG3  H  N N 165 
GLU HE2  H  N N 166 
GLU HXT  H  N N 167 
GLY N    N  N N 168 
GLY CA   C  N N 169 
GLY C    C  N N 170 
GLY O    O  N N 171 
GLY OXT  O  N N 172 
GLY H    H  N N 173 
GLY H2   H  N N 174 
GLY HA2  H  N N 175 
GLY HA3  H  N N 176 
GLY HXT  H  N N 177 
HIS N    N  N N 178 
HIS CA   C  N S 179 
HIS C    C  N N 180 
HIS O    O  N N 181 
HIS CB   C  N N 182 
HIS CG   C  Y N 183 
HIS ND1  N  Y N 184 
HIS CD2  C  Y N 185 
HIS CE1  C  Y N 186 
HIS NE2  N  Y N 187 
HIS OXT  O  N N 188 
HIS H    H  N N 189 
HIS H2   H  N N 190 
HIS HA   H  N N 191 
HIS HB2  H  N N 192 
HIS HB3  H  N N 193 
HIS HD1  H  N N 194 
HIS HD2  H  N N 195 
HIS HE1  H  N N 196 
HIS HE2  H  N N 197 
HIS HXT  H  N N 198 
HOH O    O  N N 199 
HOH H1   H  N N 200 
HOH H2   H  N N 201 
ILE N    N  N N 202 
ILE CA   C  N S 203 
ILE C    C  N N 204 
ILE O    O  N N 205 
ILE CB   C  N S 206 
ILE CG1  C  N N 207 
ILE CG2  C  N N 208 
ILE CD1  C  N N 209 
ILE OXT  O  N N 210 
ILE H    H  N N 211 
ILE H2   H  N N 212 
ILE HA   H  N N 213 
ILE HB   H  N N 214 
ILE HG12 H  N N 215 
ILE HG13 H  N N 216 
ILE HG21 H  N N 217 
ILE HG22 H  N N 218 
ILE HG23 H  N N 219 
ILE HD11 H  N N 220 
ILE HD12 H  N N 221 
ILE HD13 H  N N 222 
ILE HXT  H  N N 223 
LEU N    N  N N 224 
LEU CA   C  N S 225 
LEU C    C  N N 226 
LEU O    O  N N 227 
LEU CB   C  N N 228 
LEU CG   C  N N 229 
LEU CD1  C  N N 230 
LEU CD2  C  N N 231 
LEU OXT  O  N N 232 
LEU H    H  N N 233 
LEU H2   H  N N 234 
LEU HA   H  N N 235 
LEU HB2  H  N N 236 
LEU HB3  H  N N 237 
LEU HG   H  N N 238 
LEU HD11 H  N N 239 
LEU HD12 H  N N 240 
LEU HD13 H  N N 241 
LEU HD21 H  N N 242 
LEU HD22 H  N N 243 
LEU HD23 H  N N 244 
LEU HXT  H  N N 245 
LYS N    N  N N 246 
LYS CA   C  N S 247 
LYS C    C  N N 248 
LYS O    O  N N 249 
LYS CB   C  N N 250 
LYS CG   C  N N 251 
LYS CD   C  N N 252 
LYS CE   C  N N 253 
LYS NZ   N  N N 254 
LYS OXT  O  N N 255 
LYS H    H  N N 256 
LYS H2   H  N N 257 
LYS HA   H  N N 258 
LYS HB2  H  N N 259 
LYS HB3  H  N N 260 
LYS HG2  H  N N 261 
LYS HG3  H  N N 262 
LYS HD2  H  N N 263 
LYS HD3  H  N N 264 
LYS HE2  H  N N 265 
LYS HE3  H  N N 266 
LYS HZ1  H  N N 267 
LYS HZ2  H  N N 268 
LYS HZ3  H  N N 269 
LYS HXT  H  N N 270 
MES O1   O  N N 271 
MES C2   C  N N 272 
MES C3   C  N N 273 
MES N4   N  N N 274 
MES C5   C  N N 275 
MES C6   C  N N 276 
MES C7   C  N N 277 
MES C8   C  N N 278 
MES S    S  N N 279 
MES O1S  O  N N 280 
MES O2S  O  N N 281 
MES O3S  O  N N 282 
MES H21  H  N N 283 
MES H22  H  N N 284 
MES H31  H  N N 285 
MES H32  H  N N 286 
MES HN4  H  N N 287 
MES H51  H  N N 288 
MES H52  H  N N 289 
MES H61  H  N N 290 
MES H62  H  N N 291 
MES H71  H  N N 292 
MES H72  H  N N 293 
MES H81  H  N N 294 
MES H82  H  N N 295 
MET N    N  N N 296 
MET CA   C  N S 297 
MET C    C  N N 298 
MET O    O  N N 299 
MET CB   C  N N 300 
MET CG   C  N N 301 
MET SD   S  N N 302 
MET CE   C  N N 303 
MET OXT  O  N N 304 
MET H    H  N N 305 
MET H2   H  N N 306 
MET HA   H  N N 307 
MET HB2  H  N N 308 
MET HB3  H  N N 309 
MET HG2  H  N N 310 
MET HG3  H  N N 311 
MET HE1  H  N N 312 
MET HE2  H  N N 313 
MET HE3  H  N N 314 
MET HXT  H  N N 315 
PHE N    N  N N 316 
PHE CA   C  N S 317 
PHE C    C  N N 318 
PHE O    O  N N 319 
PHE CB   C  N N 320 
PHE CG   C  Y N 321 
PHE CD1  C  Y N 322 
PHE CD2  C  Y N 323 
PHE CE1  C  Y N 324 
PHE CE2  C  Y N 325 
PHE CZ   C  Y N 326 
PHE OXT  O  N N 327 
PHE H    H  N N 328 
PHE H2   H  N N 329 
PHE HA   H  N N 330 
PHE HB2  H  N N 331 
PHE HB3  H  N N 332 
PHE HD1  H  N N 333 
PHE HD2  H  N N 334 
PHE HE1  H  N N 335 
PHE HE2  H  N N 336 
PHE HZ   H  N N 337 
PHE HXT  H  N N 338 
PRO N    N  N N 339 
PRO CA   C  N S 340 
PRO C    C  N N 341 
PRO O    O  N N 342 
PRO CB   C  N N 343 
PRO CG   C  N N 344 
PRO CD   C  N N 345 
PRO OXT  O  N N 346 
PRO H    H  N N 347 
PRO HA   H  N N 348 
PRO HB2  H  N N 349 
PRO HB3  H  N N 350 
PRO HG2  H  N N 351 
PRO HG3  H  N N 352 
PRO HD2  H  N N 353 
PRO HD3  H  N N 354 
PRO HXT  H  N N 355 
SER N    N  N N 356 
SER CA   C  N S 357 
SER C    C  N N 358 
SER O    O  N N 359 
SER CB   C  N N 360 
SER OG   O  N N 361 
SER OXT  O  N N 362 
SER H    H  N N 363 
SER H2   H  N N 364 
SER HA   H  N N 365 
SER HB2  H  N N 366 
SER HB3  H  N N 367 
SER HG   H  N N 368 
SER HXT  H  N N 369 
THR N    N  N N 370 
THR CA   C  N S 371 
THR C    C  N N 372 
THR O    O  N N 373 
THR CB   C  N R 374 
THR OG1  O  N N 375 
THR CG2  C  N N 376 
THR OXT  O  N N 377 
THR H    H  N N 378 
THR H2   H  N N 379 
THR HA   H  N N 380 
THR HB   H  N N 381 
THR HG1  H  N N 382 
THR HG21 H  N N 383 
THR HG22 H  N N 384 
THR HG23 H  N N 385 
THR HXT  H  N N 386 
TRP N    N  N N 387 
TRP CA   C  N S 388 
TRP C    C  N N 389 
TRP O    O  N N 390 
TRP CB   C  N N 391 
TRP CG   C  Y N 392 
TRP CD1  C  Y N 393 
TRP CD2  C  Y N 394 
TRP NE1  N  Y N 395 
TRP CE2  C  Y N 396 
TRP CE3  C  Y N 397 
TRP CZ2  C  Y N 398 
TRP CZ3  C  Y N 399 
TRP CH2  C  Y N 400 
TRP OXT  O  N N 401 
TRP H    H  N N 402 
TRP H2   H  N N 403 
TRP HA   H  N N 404 
TRP HB2  H  N N 405 
TRP HB3  H  N N 406 
TRP HD1  H  N N 407 
TRP HE1  H  N N 408 
TRP HE3  H  N N 409 
TRP HZ2  H  N N 410 
TRP HZ3  H  N N 411 
TRP HH2  H  N N 412 
TRP HXT  H  N N 413 
TYR N    N  N N 414 
TYR CA   C  N S 415 
TYR C    C  N N 416 
TYR O    O  N N 417 
TYR CB   C  N N 418 
TYR CG   C  Y N 419 
TYR CD1  C  Y N 420 
TYR CD2  C  Y N 421 
TYR CE1  C  Y N 422 
TYR CE2  C  Y N 423 
TYR CZ   C  Y N 424 
TYR OH   O  N N 425 
TYR OXT  O  N N 426 
TYR H    H  N N 427 
TYR H2   H  N N 428 
TYR HA   H  N N 429 
TYR HB2  H  N N 430 
TYR HB3  H  N N 431 
TYR HD1  H  N N 432 
TYR HD2  H  N N 433 
TYR HE1  H  N N 434 
TYR HE2  H  N N 435 
TYR HH   H  N N 436 
TYR HXT  H  N N 437 
VAL N    N  N N 438 
VAL CA   C  N S 439 
VAL C    C  N N 440 
VAL O    O  N N 441 
VAL CB   C  N N 442 
VAL CG1  C  N N 443 
VAL CG2  C  N N 444 
VAL OXT  O  N N 445 
VAL H    H  N N 446 
VAL H2   H  N N 447 
VAL HA   H  N N 448 
VAL HB   H  N N 449 
VAL HG11 H  N N 450 
VAL HG12 H  N N 451 
VAL HG13 H  N N 452 
VAL HG21 H  N N 453 
VAL HG22 H  N N 454 
VAL HG23 H  N N 455 
VAL HXT  H  N N 456 
ZN  ZN   ZN N N 457 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
E1F S8  C9   sing N N 92  
E1F S8  C7   sing N N 93  
E1F N11 C9   doub Y N 94  
E1F N11 C14  sing Y N 95  
E1F C9  N10  sing Y N 96  
E1F C7  C6   sing N N 97  
E1F O12 C6   doub N N 98  
E1F C14 C15  doub Y N 99  
E1F C6  C1   sing N N 100 
E1F C5  C1   doub Y N 101 
E1F C5  C4   sing Y N 102 
E1F C1  C21  sing Y N 103 
E1F N10 C13  doub Y N 104 
E1F C15 C13  sing Y N 105 
E1F C4  C3   doub Y N 106 
E1F C21 C2   doub Y N 107 
E1F C3  C2   sing Y N 108 
E1F C3  S16  sing N N 109 
E1F C2  CL1  sing N N 110 
E1F N19 S16  sing N N 111 
E1F O17 S16  doub N N 112 
E1F S16 O18  doub N N 113 
E1F C13 H1   sing N N 114 
E1F C21 H2   sing N N 115 
E1F C5  H3   sing N N 116 
E1F C4  H4   sing N N 117 
E1F N19 H5   sing N N 118 
E1F N19 H6   sing N N 119 
E1F C7  H7   sing N N 120 
E1F C7  H8   sing N N 121 
E1F C14 H9   sing N N 122 
E1F C15 H10  sing N N 123 
GLN N   CA   sing N N 124 
GLN N   H    sing N N 125 
GLN N   H2   sing N N 126 
GLN CA  C    sing N N 127 
GLN CA  CB   sing N N 128 
GLN CA  HA   sing N N 129 
GLN C   O    doub N N 130 
GLN C   OXT  sing N N 131 
GLN CB  CG   sing N N 132 
GLN CB  HB2  sing N N 133 
GLN CB  HB3  sing N N 134 
GLN CG  CD   sing N N 135 
GLN CG  HG2  sing N N 136 
GLN CG  HG3  sing N N 137 
GLN CD  OE1  doub N N 138 
GLN CD  NE2  sing N N 139 
GLN NE2 HE21 sing N N 140 
GLN NE2 HE22 sing N N 141 
GLN OXT HXT  sing N N 142 
GLU N   CA   sing N N 143 
GLU N   H    sing N N 144 
GLU N   H2   sing N N 145 
GLU CA  C    sing N N 146 
GLU CA  CB   sing N N 147 
GLU CA  HA   sing N N 148 
GLU C   O    doub N N 149 
GLU C   OXT  sing N N 150 
GLU CB  CG   sing N N 151 
GLU CB  HB2  sing N N 152 
GLU CB  HB3  sing N N 153 
GLU CG  CD   sing N N 154 
GLU CG  HG2  sing N N 155 
GLU CG  HG3  sing N N 156 
GLU CD  OE1  doub N N 157 
GLU CD  OE2  sing N N 158 
GLU OE2 HE2  sing N N 159 
GLU OXT HXT  sing N N 160 
GLY N   CA   sing N N 161 
GLY N   H    sing N N 162 
GLY N   H2   sing N N 163 
GLY CA  C    sing N N 164 
GLY CA  HA2  sing N N 165 
GLY CA  HA3  sing N N 166 
GLY C   O    doub N N 167 
GLY C   OXT  sing N N 168 
GLY OXT HXT  sing N N 169 
HIS N   CA   sing N N 170 
HIS N   H    sing N N 171 
HIS N   H2   sing N N 172 
HIS CA  C    sing N N 173 
HIS CA  CB   sing N N 174 
HIS CA  HA   sing N N 175 
HIS C   O    doub N N 176 
HIS C   OXT  sing N N 177 
HIS CB  CG   sing N N 178 
HIS CB  HB2  sing N N 179 
HIS CB  HB3  sing N N 180 
HIS CG  ND1  sing Y N 181 
HIS CG  CD2  doub Y N 182 
HIS ND1 CE1  doub Y N 183 
HIS ND1 HD1  sing N N 184 
HIS CD2 NE2  sing Y N 185 
HIS CD2 HD2  sing N N 186 
HIS CE1 NE2  sing Y N 187 
HIS CE1 HE1  sing N N 188 
HIS NE2 HE2  sing N N 189 
HIS OXT HXT  sing N N 190 
HOH O   H1   sing N N 191 
HOH O   H2   sing N N 192 
ILE N   CA   sing N N 193 
ILE N   H    sing N N 194 
ILE N   H2   sing N N 195 
ILE CA  C    sing N N 196 
ILE CA  CB   sing N N 197 
ILE CA  HA   sing N N 198 
ILE C   O    doub N N 199 
ILE C   OXT  sing N N 200 
ILE CB  CG1  sing N N 201 
ILE CB  CG2  sing N N 202 
ILE CB  HB   sing N N 203 
ILE CG1 CD1  sing N N 204 
ILE CG1 HG12 sing N N 205 
ILE CG1 HG13 sing N N 206 
ILE CG2 HG21 sing N N 207 
ILE CG2 HG22 sing N N 208 
ILE CG2 HG23 sing N N 209 
ILE CD1 HD11 sing N N 210 
ILE CD1 HD12 sing N N 211 
ILE CD1 HD13 sing N N 212 
ILE OXT HXT  sing N N 213 
LEU N   CA   sing N N 214 
LEU N   H    sing N N 215 
LEU N   H2   sing N N 216 
LEU CA  C    sing N N 217 
LEU CA  CB   sing N N 218 
LEU CA  HA   sing N N 219 
LEU C   O    doub N N 220 
LEU C   OXT  sing N N 221 
LEU CB  CG   sing N N 222 
LEU CB  HB2  sing N N 223 
LEU CB  HB3  sing N N 224 
LEU CG  CD1  sing N N 225 
LEU CG  CD2  sing N N 226 
LEU CG  HG   sing N N 227 
LEU CD1 HD11 sing N N 228 
LEU CD1 HD12 sing N N 229 
LEU CD1 HD13 sing N N 230 
LEU CD2 HD21 sing N N 231 
LEU CD2 HD22 sing N N 232 
LEU CD2 HD23 sing N N 233 
LEU OXT HXT  sing N N 234 
LYS N   CA   sing N N 235 
LYS N   H    sing N N 236 
LYS N   H2   sing N N 237 
LYS CA  C    sing N N 238 
LYS CA  CB   sing N N 239 
LYS CA  HA   sing N N 240 
LYS C   O    doub N N 241 
LYS C   OXT  sing N N 242 
LYS CB  CG   sing N N 243 
LYS CB  HB2  sing N N 244 
LYS CB  HB3  sing N N 245 
LYS CG  CD   sing N N 246 
LYS CG  HG2  sing N N 247 
LYS CG  HG3  sing N N 248 
LYS CD  CE   sing N N 249 
LYS CD  HD2  sing N N 250 
LYS CD  HD3  sing N N 251 
LYS CE  NZ   sing N N 252 
LYS CE  HE2  sing N N 253 
LYS CE  HE3  sing N N 254 
LYS NZ  HZ1  sing N N 255 
LYS NZ  HZ2  sing N N 256 
LYS NZ  HZ3  sing N N 257 
LYS OXT HXT  sing N N 258 
MES O1  C2   sing N N 259 
MES O1  C6   sing N N 260 
MES C2  C3   sing N N 261 
MES C2  H21  sing N N 262 
MES C2  H22  sing N N 263 
MES C3  N4   sing N N 264 
MES C3  H31  sing N N 265 
MES C3  H32  sing N N 266 
MES N4  C5   sing N N 267 
MES N4  C7   sing N N 268 
MES N4  HN4  sing N N 269 
MES C5  C6   sing N N 270 
MES C5  H51  sing N N 271 
MES C5  H52  sing N N 272 
MES C6  H61  sing N N 273 
MES C6  H62  sing N N 274 
MES C7  C8   sing N N 275 
MES C7  H71  sing N N 276 
MES C7  H72  sing N N 277 
MES C8  S    sing N N 278 
MES C8  H81  sing N N 279 
MES C8  H82  sing N N 280 
MES S   O1S  doub N N 281 
MES S   O2S  doub N N 282 
MES S   O3S  sing N N 283 
MET N   CA   sing N N 284 
MET N   H    sing N N 285 
MET N   H2   sing N N 286 
MET CA  C    sing N N 287 
MET CA  CB   sing N N 288 
MET CA  HA   sing N N 289 
MET C   O    doub N N 290 
MET C   OXT  sing N N 291 
MET CB  CG   sing N N 292 
MET CB  HB2  sing N N 293 
MET CB  HB3  sing N N 294 
MET CG  SD   sing N N 295 
MET CG  HG2  sing N N 296 
MET CG  HG3  sing N N 297 
MET SD  CE   sing N N 298 
MET CE  HE1  sing N N 299 
MET CE  HE2  sing N N 300 
MET CE  HE3  sing N N 301 
MET OXT HXT  sing N N 302 
PHE N   CA   sing N N 303 
PHE N   H    sing N N 304 
PHE N   H2   sing N N 305 
PHE CA  C    sing N N 306 
PHE CA  CB   sing N N 307 
PHE CA  HA   sing N N 308 
PHE C   O    doub N N 309 
PHE C   OXT  sing N N 310 
PHE CB  CG   sing N N 311 
PHE CB  HB2  sing N N 312 
PHE CB  HB3  sing N N 313 
PHE CG  CD1  doub Y N 314 
PHE CG  CD2  sing Y N 315 
PHE CD1 CE1  sing Y N 316 
PHE CD1 HD1  sing N N 317 
PHE CD2 CE2  doub Y N 318 
PHE CD2 HD2  sing N N 319 
PHE CE1 CZ   doub Y N 320 
PHE CE1 HE1  sing N N 321 
PHE CE2 CZ   sing Y N 322 
PHE CE2 HE2  sing N N 323 
PHE CZ  HZ   sing N N 324 
PHE OXT HXT  sing N N 325 
PRO N   CA   sing N N 326 
PRO N   CD   sing N N 327 
PRO N   H    sing N N 328 
PRO CA  C    sing N N 329 
PRO CA  CB   sing N N 330 
PRO CA  HA   sing N N 331 
PRO C   O    doub N N 332 
PRO C   OXT  sing N N 333 
PRO CB  CG   sing N N 334 
PRO CB  HB2  sing N N 335 
PRO CB  HB3  sing N N 336 
PRO CG  CD   sing N N 337 
PRO CG  HG2  sing N N 338 
PRO CG  HG3  sing N N 339 
PRO CD  HD2  sing N N 340 
PRO CD  HD3  sing N N 341 
PRO OXT HXT  sing N N 342 
SER N   CA   sing N N 343 
SER N   H    sing N N 344 
SER N   H2   sing N N 345 
SER CA  C    sing N N 346 
SER CA  CB   sing N N 347 
SER CA  HA   sing N N 348 
SER C   O    doub N N 349 
SER C   OXT  sing N N 350 
SER CB  OG   sing N N 351 
SER CB  HB2  sing N N 352 
SER CB  HB3  sing N N 353 
SER OG  HG   sing N N 354 
SER OXT HXT  sing N N 355 
THR N   CA   sing N N 356 
THR N   H    sing N N 357 
THR N   H2   sing N N 358 
THR CA  C    sing N N 359 
THR CA  CB   sing N N 360 
THR CA  HA   sing N N 361 
THR C   O    doub N N 362 
THR C   OXT  sing N N 363 
THR CB  OG1  sing N N 364 
THR CB  CG2  sing N N 365 
THR CB  HB   sing N N 366 
THR OG1 HG1  sing N N 367 
THR CG2 HG21 sing N N 368 
THR CG2 HG22 sing N N 369 
THR CG2 HG23 sing N N 370 
THR OXT HXT  sing N N 371 
TRP N   CA   sing N N 372 
TRP N   H    sing N N 373 
TRP N   H2   sing N N 374 
TRP CA  C    sing N N 375 
TRP CA  CB   sing N N 376 
TRP CA  HA   sing N N 377 
TRP C   O    doub N N 378 
TRP C   OXT  sing N N 379 
TRP CB  CG   sing N N 380 
TRP CB  HB2  sing N N 381 
TRP CB  HB3  sing N N 382 
TRP CG  CD1  doub Y N 383 
TRP CG  CD2  sing Y N 384 
TRP CD1 NE1  sing Y N 385 
TRP CD1 HD1  sing N N 386 
TRP CD2 CE2  doub Y N 387 
TRP CD2 CE3  sing Y N 388 
TRP NE1 CE2  sing Y N 389 
TRP NE1 HE1  sing N N 390 
TRP CE2 CZ2  sing Y N 391 
TRP CE3 CZ3  doub Y N 392 
TRP CE3 HE3  sing N N 393 
TRP CZ2 CH2  doub Y N 394 
TRP CZ2 HZ2  sing N N 395 
TRP CZ3 CH2  sing Y N 396 
TRP CZ3 HZ3  sing N N 397 
TRP CH2 HH2  sing N N 398 
TRP OXT HXT  sing N N 399 
TYR N   CA   sing N N 400 
TYR N   H    sing N N 401 
TYR N   H2   sing N N 402 
TYR CA  C    sing N N 403 
TYR CA  CB   sing N N 404 
TYR CA  HA   sing N N 405 
TYR C   O    doub N N 406 
TYR C   OXT  sing N N 407 
TYR CB  CG   sing N N 408 
TYR CB  HB2  sing N N 409 
TYR CB  HB3  sing N N 410 
TYR CG  CD1  doub Y N 411 
TYR CG  CD2  sing Y N 412 
TYR CD1 CE1  sing Y N 413 
TYR CD1 HD1  sing N N 414 
TYR CD2 CE2  doub Y N 415 
TYR CD2 HD2  sing N N 416 
TYR CE1 CZ   doub Y N 417 
TYR CE1 HE1  sing N N 418 
TYR CE2 CZ   sing Y N 419 
TYR CE2 HE2  sing N N 420 
TYR CZ  OH   sing N N 421 
TYR OH  HH   sing N N 422 
TYR OXT HXT  sing N N 423 
VAL N   CA   sing N N 424 
VAL N   H    sing N N 425 
VAL N   H2   sing N N 426 
VAL CA  C    sing N N 427 
VAL CA  CB   sing N N 428 
VAL CA  HA   sing N N 429 
VAL C   O    doub N N 430 
VAL C   OXT  sing N N 431 
VAL CB  CG1  sing N N 432 
VAL CB  CG2  sing N N 433 
VAL CB  HB   sing N N 434 
VAL CG1 HG11 sing N N 435 
VAL CG1 HG12 sing N N 436 
VAL CG1 HG13 sing N N 437 
VAL CG2 HG21 sing N N 438 
VAL CG2 HG22 sing N N 439 
VAL CG2 HG23 sing N N 440 
VAL OXT HXT  sing N N 441 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                      ZN  
3 '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' E1F 
4 'DIMETHYL SULFOXIDE'                                            DMS 
5 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                          MES 
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   3HLJ 
_pdbx_initial_refinement_model.details          ? 
# 
