data_3M3X
# 
_entry.id   3M3X 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.380 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   3M3X         pdb_00003m3x 10.2210/pdb3m3x/pdb 
RCSB  RCSB058076   ?            ?                   
WWPDB D_1000058076 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3M2N 'The same protein with other ligand' unspecified 
PDB 3M40 'The same protein with other ligand' unspecified 
PDB 3M5E 'The same protein with other ligand' unspecified 
PDB 3MHI 'The same protein with other ligand' unspecified 
PDB 3MHL 'The same protein with other ligand' unspecified 
PDB 3MHM 'The same protein with other ligand' unspecified 
PDB 3MHO 'The same protein with other ligand' unspecified 
# 
_pdbx_database_status.entry_id                        3M3X 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2010-03-10 
_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.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'  1 
'Manakova, E.'  2 
'Golovenko, D.' 3 
# 
_citation.id                        primary 
_citation.title                     
'4-[N-(Substituted 4-pyrimidinyl)amino]benzenesulfonamides as inhibitors of carbonic anhydrase isozymes I, II, VII, and XIII' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            18 
_citation.page_first                7413 
_citation.page_last                 7421 
_citation.year                      2010 
_citation.journal_id_ASTM           BMECEP 
_citation.country                   UK 
_citation.journal_id_ISSN           0968-0896 
_citation.journal_id_CSD            1200 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20889345 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2010.09.011 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sudzius, J.'       1  ? 
primary 'Baranauskiene, L.' 2  ? 
primary 'Golovenko, D.'     3  ? 
primary 'Matuliene, J.'     4  ? 
primary 'Michailoviene, V.' 5  ? 
primary 'Torresan, J.'      6  ? 
primary 'Jachno, J.'        7  ? 
primary 'Sukackaite, R.'    8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Tumkevicius, S.'   11 ? 
primary 'Matulis, D.'       12 ? 
# 
_cell.entry_id           3M3X 
_cell.length_a           42.035 
_cell.length_b           41.051 
_cell.length_c           71.805 
_cell.angle_alpha        90.00 
_cell.angle_beta         104.39 
_cell.angle_gamma        90.00 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3M3X 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                  29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                              65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                    78.133    1   ?       ? ? ? 
4 non-polymer syn '4-{2-[(6-methoxy-5-nitropyrimidin-4-yl)amino]ethyl}benzenesulfonamide' 353.354   1   ?       ? ? ? 
5 water       nat water                                                                   18.015    287 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonic anhydrase II, CA-II, Carbonate dehydratase II, Carbonic anhydrase C, CAC' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3M3X 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                 ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                                                ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                              ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                         ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                ? 'C3 H7 N O2 S'    121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                    ? 'C2 H6 O S'       78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                               ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                         ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                                                 ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                                                               ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                                                                   ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                              ? 'C6 H13 N O2'     131.173 
JS7 non-polymer         . '4-{2-[(6-methoxy-5-nitropyrimidin-4-yl)amino]ethyl}benzenesulfonamide' ? 'C13 H15 N5 O5 S' 353.354 
LEU 'L-peptide linking' y LEUCINE                                                                 ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                                                                  ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                                                              ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                           ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                                                                 ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                                                                  ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                                                               ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                              ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                                                                ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                                                                  ? 'C5 H11 N O2'     117.146 
ZN  non-polymer         . 'ZINC ION'                                                              ? 'Zn 2'            65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3M3X 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   39.97 
_exptl_crystal.density_Matthews      2.05 
_exptl_crystal.pdbx_mosaicity        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              8 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.pdbx_details    '0.1M Na-bicine pH 9.0, 2M Na-Malonate pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2009-12-16 
_diffrn_detector.details                'Bent, vertically focussing mirror' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8120 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.pdbx_wavelength_list        0.8120 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
# 
_reflns.entry_id                     3M3X 
_reflns.d_resolution_high            1.68 
_reflns.d_resolution_low             41.07 
_reflns.number_all                   27211 
_reflns.number_obs                   26749 
_reflns.pdbx_Rmerge_I_obs            0.039 
_reflns.pdbx_netI_over_sigmaI        50.500 
_reflns.pdbx_Rsym_value              0.039 
_reflns.pdbx_redundancy              11.200 
_reflns.percent_possible_obs         98.300 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        16.2 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.68 
_reflns_shell.d_res_low              1.77 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    29134 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.079 
_reflns_shell.meanI_over_sigI_obs    17.8 
_reflns_shell.pdbx_Rsym_value        0.079 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_redundancy        7.60 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      3813 
_reflns_shell.percent_possible_all   97.60 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 3M3X 
_refine.ls_d_res_high                            1.680 
_refine.ls_d_res_low                             31.860 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    97.950 
_refine.ls_number_reflns_obs                     26728 
_refine.ls_number_reflns_all                     27211 
_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_obs                          0.16845 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.16268 
_refine.ls_R_factor_R_free                       0.22167 
_refine.ls_percent_reflns_R_free                 9.900 
_refine.ls_number_reflns_R_free                  2652 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               16.154 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             Isotropic 
_refine.aniso_B[1][1]                            0.20 
_refine.aniso_B[2][2]                            -0.57 
_refine.aniso_B[3][3]                            0.43 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.11 
_refine.aniso_B[2][3]                            0.00 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.927 
_refine.overall_SU_R_Cruickshank_DPI             0.120 
_refine.overall_SU_R_free                        0.125 
_refine.pdbx_overall_ESU_R                       0.120 
_refine.pdbx_overall_ESU_R_Free                  0.125 
_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                   ? 
_refine.B_iso_max                                52.99 
_refine.B_iso_min                                3.22 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.pdbx_ls_sigma_I                          0 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 2NNO' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_phase_error                 ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2059 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             287 
_refine_hist.number_atoms_total               2375 
_refine_hist.d_res_high                       1.680 
_refine_hist.d_res_low                        31.860 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.027  0.021  ? 2291 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.187  1.956  ? 3126 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.035  5.000  ? 285  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       35.602 24.815 ? 108  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.540 15.000 ? 380  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       20.855 15.000 ? 8    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.166  0.200  ? 319  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.013  0.020  ? 1809 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.233  0.200  ? 1146 'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.314  0.200  ? 1490 'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.170  0.200  ? 243  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          0.082  0.200  ? 3    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.252  0.200  ? 86   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.194  0.200  ? 44   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  1.471  1.500  ? 1378 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.208  2.000  ? 2240 'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.123  3.000  ? 913  'X-RAY DIFFRACTION' ? 
r_scangle_it                 4.633  4.500  ? 886  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.680 
_refine_ls_shell.d_res_low                        1.724 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               97.510 
_refine_ls_shell.number_reflns_R_work             1713 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.204 
_refine_ls_shell.R_factor_R_free                  0.323 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             206 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1919 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3M3X 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 4-{2-[N-(6-methoxy-5-nitropyrimidin-4-yl)amino]ethyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3M3X 
_struct_keywords.text            'DRUG DESIGN, CARBONIC ANHYDRASE, SULFONAMIDE, 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 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 12  ? TRP A 16  ? GLY A 12  TRP A 16  5 ? 5 
HELX_P HELX_P2 2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -3.27 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 8.51  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O TRP A 123 ? O TRP A 123 N ARG A 89  ? N ARG A 89  
B 7 8  O ILE A 91  ? O ILE A 91  N PHE A 70  ? N PHE A 70  
B 8 9  O GLU A 69  ? O GLU A 69  N ARG A 58  ? N ARG A 58  
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 ARG A 89  ? N ARG A 89  O TRP A 123 ? O TRP A 123 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  262 ? 4  'BINDING SITE FOR RESIDUE ZN A 262'  
AC2 Software A DMS 263 ? 5  'BINDING SITE FOR RESIDUE DMS A 263' 
AC3 Software A JS7 264 ? 16 'BINDING SITE FOR RESIDUE JS7 A 264' 
# 
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  JS7 D .   ? JS7 A 264 . ? 1_555 ? 
5  AC2 5  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 5  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 5  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 5  HOH E .   ? HOH A 280 . ? 1_555 ? 
9  AC2 5  HOH E .   ? HOH A 514 . ? 1_555 ? 
10 AC3 16 GLN A 92  ? GLN A 92  . ? 1_555 ? 
11 AC3 16 HIS A 94  ? HIS A 94  . ? 1_555 ? 
12 AC3 16 HIS A 96  ? HIS A 96  . ? 1_555 ? 
13 AC3 16 HIS A 119 ? HIS A 119 . ? 1_555 ? 
14 AC3 16 PHE A 130 ? PHE A 131 . ? 1_555 ? 
15 AC3 16 VAL A 134 ? VAL A 135 . ? 1_555 ? 
16 AC3 16 LEU A 197 ? LEU A 198 . ? 1_555 ? 
17 AC3 16 THR A 198 ? THR A 199 . ? 1_555 ? 
18 AC3 16 THR A 199 ? THR A 200 . ? 1_555 ? 
19 AC3 16 PRO A 201 ? PRO A 202 . ? 1_555 ? 
20 AC3 16 LEU A 203 ? LEU A 204 . ? 1_555 ? 
21 AC3 16 TRP A 208 ? TRP A 209 . ? 1_555 ? 
22 AC3 16 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
23 AC3 16 HOH E .   ? HOH A 405 . ? 1_555 ? 
24 AC3 16 HOH E .   ? HOH A 447 . ? 1_555 ? 
25 AC3 16 HOH E .   ? HOH A 486 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3M3X 
_atom_sites.fract_transf_matrix[1][1]   0.023790 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006104 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024360 
_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]   0.014378 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 3   ? 13.752  0.012   6.327   1.00 25.77 ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 3   ? 13.408  -1.001  7.376   1.00 26.90 ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 3   ? 12.329  -0.515  8.408   1.00 27.52 ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 3   ? 12.602  -0.366  9.633   1.00 28.17 ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 3   ? 14.665  -1.434  8.129   1.00 27.88 ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 3   ? 14.407  -2.532  9.106   1.00 30.51 ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 3   ? 14.423  -3.864  8.732   1.00 33.33 ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 3   ? 14.071  -2.503  10.422  1.00 30.57 ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 3   ? 14.152  -4.611  9.795   1.00 31.64 ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 3   ? 13.940  -3.809  10.827  1.00 32.42 ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 4   ? 11.107  -0.259  7.935   1.00 25.14 ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 4   ? 10.143  0.290   8.866   1.00 24.51 ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 4   ? 9.320   -0.842  9.547   1.00 21.20 ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 4   ? 9.428   -2.008  9.200   1.00 18.16 ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 4   ? 9.267   1.364   8.201   1.00 26.79 ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 4   ? 9.820   2.751   8.349   1.00 32.64 ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 4   ? 9.712   3.470   9.526   1.00 36.78 ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 4   ? 10.508  3.546   7.480   1.00 33.54 ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 4   ? 10.304  4.648   9.375   1.00 37.93 ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 4   ? 10.796  4.719   8.144   1.00 31.99 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.446   -0.448  10.450  1.00 19.86 ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 7.782   -1.426  11.316  1.00 15.28 ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 6.825   -2.202  10.480  1.00 13.43 ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.283   -1.732  9.456   1.00 14.29 ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.065   -0.769  12.545  1.00 13.96 ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 5.916   0.075   12.142  1.00 15.60 ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 5.917   1.417   11.814  1.00 16.49 ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.543   -0.363  12.071  1.00 12.69 ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.632   1.811   11.484  1.00 16.51 ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.774   0.740   11.633  1.00 13.12 ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 3.916   -1.594  12.301  1.00 13.05 ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.404   0.673   11.424  1.00 14.96 ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.531   -1.661  12.074  1.00 12.47 ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 1.800   -0.527  11.643  1.00 12.52 ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.534   -3.402  10.988  1.00 13.81 ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.532   -4.243  10.322  1.00 12.50 ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.172   -5.368  11.269  1.00 12.84 ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.225   -5.227  12.487  1.00 12.02 ? 6   GLY A O   1 
ATOM   39   N  N   . TYR A 1 7   ? 4.900   -6.539  10.695  1.00 15.56 ? 7   TYR A N   1 
ATOM   40   C  CA  . TYR A 1 7   ? 4.508   -7.666  11.528  1.00 16.17 ? 7   TYR A CA  1 
ATOM   41   C  C   . TYR A 1 7   ? 5.416   -8.919  11.462  1.00 19.91 ? 7   TYR A C   1 
ATOM   42   O  O   . TYR A 1 7   ? 5.119   -9.967  12.154  1.00 20.03 ? 7   TYR A O   1 
ATOM   43   C  CB  . TYR A 1 7   ? 3.054   -8.015  11.232  1.00 14.86 ? 7   TYR A CB  1 
ATOM   44   C  CG  . TYR A 1 7   ? 2.095   -6.952  11.756  1.00 12.30 ? 7   TYR A CG  1 
ATOM   45   C  CD1 . TYR A 1 7   ? 1.685   -6.986  13.116  1.00 13.28 ? 7   TYR A CD1 1 
ATOM   46   C  CD2 . TYR A 1 7   ? 1.633   -5.935  10.923  1.00 7.75  ? 7   TYR A CD2 1 
ATOM   47   C  CE1 . TYR A 1 7   ? 0.770   -5.988  13.612  1.00 8.30  ? 7   TYR A CE1 1 
ATOM   48   C  CE2 . TYR A 1 7   ? 0.724   -4.929  11.392  1.00 8.53  ? 7   TYR A CE2 1 
ATOM   49   C  CZ  . TYR A 1 7   ? 0.278   -5.012  12.751  1.00 11.75 ? 7   TYR A CZ  1 
ATOM   50   O  OH  . TYR A 1 7   ? -0.597  -4.045  13.231  1.00 10.06 ? 7   TYR A OH  1 
ATOM   51   N  N   . GLY A 1 8   ? 6.490   -8.807  10.676  1.00 19.65 ? 8   GLY A N   1 
ATOM   52   C  CA  . GLY A 1 8   ? 7.456   -9.964  10.486  1.00 21.25 ? 8   GLY A CA  1 
ATOM   53   C  C   . GLY A 1 8   ? 8.465   -10.212 11.598  1.00 21.73 ? 8   GLY A C   1 
ATOM   54   O  O   . GLY A 1 8   ? 8.525   -9.494  12.628  1.00 24.59 ? 8   GLY A O   1 
ATOM   55   N  N   . LYS A 1 9   ? 9.323   -11.242 11.428  1.00 23.94 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 10.328  -11.667 12.467  1.00 22.64 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 11.289  -10.537 12.830  1.00 21.35 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 11.711  -10.422 14.000  1.00 22.95 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 11.209  -12.813 11.944  1.00 23.81 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 12.236  -13.244 12.950  1.00 24.79 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 11.977  -14.514 13.664  0.00 13.03 ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 10.789  -14.403 14.612  0.00 12.89 ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 11.130  -14.870 15.984  0.00 12.75 ? 9   LYS A NZ  1 
ATOM   64   N  N   . HIS A 1 10  ? 11.568  -9.729  11.811  1.00 20.52 ? 10  HIS A N   1 
ATOM   65   C  CA  . HIS A 1 10  ? 12.601  -8.720  11.847  1.00 20.90 ? 10  HIS A CA  1 
ATOM   66   C  C   . HIS A 1 10  ? 12.071  -7.340  12.027  1.00 19.57 ? 10  HIS A C   1 
ATOM   67   O  O   . HIS A 1 10  ? 12.847  -6.473  12.333  1.00 18.86 ? 10  HIS A O   1 
ATOM   68   C  CB  . HIS A 1 10  ? 13.501  -8.802  10.602  1.00 20.59 ? 10  HIS A CB  1 
ATOM   69   C  CG  . HIS A 1 10  ? 14.250  -10.120 10.524  1.00 22.78 ? 10  HIS A CG  1 
ATOM   70   N  ND1 . HIS A 1 10  ? 15.296  -10.428 11.372  1.00 23.89 ? 10  HIS A ND1 1 
ATOM   71   C  CD2 . HIS A 1 10  ? 14.049  -11.210 9.758   1.00 23.38 ? 10  HIS A CD2 1 
ATOM   72   C  CE1 . HIS A 1 10  ? 15.735  -11.639 11.099  1.00 21.62 ? 10  HIS A CE1 1 
ATOM   73   N  NE2 . HIS A 1 10  ? 14.981  -12.143 10.132  1.00 24.37 ? 10  HIS A NE2 1 
ATOM   74   N  N   . ASN A 1 11  ? 10.764  -7.128  11.874  1.00 18.22 ? 11  ASN A N   1 
ATOM   75   C  CA  . ASN A 1 11  ? 10.252  -5.755  12.117  1.00 16.30 ? 11  ASN A CA  1 
ATOM   76   C  C   . ASN A 1 11  ? 8.904   -5.750  12.890  1.00 16.18 ? 11  ASN A C   1 
ATOM   77   O  O   . ASN A 1 11  ? 8.221   -4.718  12.912  1.00 15.55 ? 11  ASN A O   1 
ATOM   78   C  CB  . ASN A 1 11  ? 10.048  -5.022  10.811  1.00 15.17 ? 11  ASN A CB  1 
ATOM   79   C  CG  . ASN A 1 11  ? 8.999   -5.649  9.910   1.00 16.40 ? 11  ASN A CG  1 
ATOM   80   O  OD1 . ASN A 1 11  ? 8.425   -6.736  10.177  1.00 17.66 ? 11  ASN A OD1 1 
ATOM   81   N  ND2 . ASN A 1 11  ? 8.785   -5.018  8.789   1.00 19.86 ? 11  ASN A ND2 1 
ATOM   82   N  N   . GLY A 1 12  ? 8.560   -6.903  13.453  1.00 15.15 ? 12  GLY A N   1 
ATOM   83   C  CA  . GLY A 1 12  ? 7.202   -7.102  14.074  1.00 15.33 ? 12  GLY A CA  1 
ATOM   84   C  C   . GLY A 1 12  ? 7.175   -6.559  15.484  1.00 14.40 ? 12  GLY A C   1 
ATOM   85   O  O   . GLY A 1 12  ? 8.085   -5.835  15.991  1.00 13.93 ? 12  GLY A O   1 
ATOM   86   N  N   . PRO A 1 13  ? 6.073   -6.856  16.183  1.00 14.85 ? 13  PRO A N   1 
ATOM   87   C  CA  . PRO A 1 13  ? 5.837   -6.240  17.477  1.00 14.48 ? 13  PRO A CA  1 
ATOM   88   C  C   . PRO A 1 13  ? 6.970   -6.285  18.501  1.00 12.61 ? 13  PRO A C   1 
ATOM   89   O  O   . PRO A 1 13  ? 7.126   -5.291  19.187  1.00 14.17 ? 13  PRO A O   1 
ATOM   90   C  CB  . PRO A 1 13  ? 4.573   -7.009  17.993  1.00 13.91 ? 13  PRO A CB  1 
ATOM   91   C  CG  . PRO A 1 13  ? 3.910   -7.454  16.818  1.00 13.61 ? 13  PRO A CG  1 
ATOM   92   C  CD  . PRO A 1 13  ? 4.923   -7.636  15.708  1.00 15.09 ? 13  PRO A CD  1 
ATOM   93   N  N   . GLU A 1 14  ? 7.777   -7.360  18.543  1.00 12.06 ? 14  GLU A N   1 
ATOM   94   C  CA  . GLU A 1 14  ? 8.922   -7.508  19.508  1.00 15.19 ? 14  GLU A CA  1 
ATOM   95   C  C   . GLU A 1 14  ? 10.040  -6.431  19.246  1.00 14.05 ? 14  GLU A C   1 
ATOM   96   O  O   . GLU A 1 14  ? 10.873  -6.173  20.120  1.00 16.01 ? 14  GLU A O   1 
ATOM   97   C  CB  . GLU A 1 14  ? 9.517   -8.939  19.381  1.00 17.85 ? 14  GLU A CB  1 
ATOM   98   C  CG  . GLU A 1 14  ? 8.467   -10.045 19.862  1.00 21.89 ? 14  GLU A CG  1 
ATOM   99   C  CD  . GLU A 1 14  ? 7.676   -9.611  21.107  1.00 28.66 ? 14  GLU A CD  1 
ATOM   100  O  OE1 . GLU A 1 14  ? 8.325   -9.070  22.023  1.00 34.06 ? 14  GLU A OE1 1 
ATOM   101  O  OE2 . GLU A 1 14  ? 6.396   -9.763  21.172  1.00 33.01 ? 14  GLU A OE2 1 
ATOM   102  N  N   . HIS A 1 15  ? 9.982   -5.816  18.072  1.00 12.50 ? 15  HIS A N   1 
ATOM   103  C  CA  . HIS A 1 15  ? 10.984  -4.849  17.578  1.00 11.77 ? 15  HIS A CA  1 
ATOM   104  C  C   . HIS A 1 15  ? 10.521  -3.413  17.740  1.00 14.80 ? 15  HIS A C   1 
ATOM   105  O  O   . HIS A 1 15  ? 11.339  -2.465  17.694  1.00 13.49 ? 15  HIS A O   1 
ATOM   106  C  CB  . HIS A 1 15  ? 11.288  -5.055  16.081  1.00 13.62 ? 15  HIS A CB  1 
ATOM   107  C  CG  . HIS A 1 15  ? 12.007  -6.344  15.811  1.00 15.17 ? 15  HIS A CG  1 
ATOM   108  N  ND1 . HIS A 1 15  ? 13.374  -6.477  15.977  1.00 19.46 ? 15  HIS A ND1 1 
ATOM   109  C  CD2 . HIS A 1 15  ? 11.555  -7.545  15.359  1.00 18.38 ? 15  HIS A CD2 1 
ATOM   110  C  CE1 . HIS A 1 15  ? 13.722  -7.729  15.714  1.00 21.01 ? 15  HIS A CE1 1 
ATOM   111  N  NE2 . HIS A 1 15  ? 12.655  -8.394  15.308  1.00 18.18 ? 15  HIS A NE2 1 
ATOM   112  N  N   . TRP A 1 16  ? 9.214   -3.209  17.899  1.00 11.03 ? 16  TRP A N   1 
ATOM   113  C  CA  . TRP A 1 16  ? 8.699   -1.855  17.891  1.00 12.37 ? 16  TRP A CA  1 
ATOM   114  C  C   . TRP A 1 16  ? 9.276   -0.844  18.890  1.00 10.23 ? 16  TRP A C   1 
ATOM   115  O  O   . TRP A 1 16  ? 9.298   0.357   18.553  1.00 13.13 ? 16  TRP A O   1 
ATOM   116  C  CB  . TRP A 1 16  ? 7.124   -1.893  17.991  1.00 8.35  ? 16  TRP A CB  1 
ATOM   117  C  CG  . TRP A 1 16  ? 6.490   -2.546  16.818  1.00 10.30 ? 16  TRP A CG  1 
ATOM   118  C  CD1 . TRP A 1 16  ? 7.058   -2.989  15.621  1.00 9.27  ? 16  TRP A CD1 1 
ATOM   119  C  CD2 . TRP A 1 16  ? 5.080   -2.862  16.733  1.00 8.83  ? 16  TRP A CD2 1 
ATOM   120  N  NE1 . TRP A 1 16  ? 6.079   -3.564  14.816  1.00 11.08 ? 16  TRP A NE1 1 
ATOM   121  C  CE2 . TRP A 1 16  ? 4.858   -3.458  15.457  1.00 11.78 ? 16  TRP A CE2 1 
ATOM   122  C  CE3 . TRP A 1 16  ? 4.001   -2.626  17.605  1.00 12.56 ? 16  TRP A CE3 1 
ATOM   123  C  CZ2 . TRP A 1 16  ? 3.602   -3.892  15.041  1.00 12.84 ? 16  TRP A CZ2 1 
ATOM   124  C  CZ3 . TRP A 1 16  ? 2.756   -3.084  17.235  1.00 10.34 ? 16  TRP A CZ3 1 
ATOM   125  C  CH2 . TRP A 1 16  ? 2.543   -3.648  15.945  1.00 11.11 ? 16  TRP A CH2 1 
ATOM   126  N  N   . HIS A 1 17  ? 9.686   -1.290  20.058  1.00 11.32 ? 17  HIS A N   1 
ATOM   127  C  CA  . HIS A 1 17  ? 10.143  -0.440  21.142  1.00 12.87 ? 17  HIS A CA  1 
ATOM   128  C  C   . HIS A 1 17  ? 11.419  0.333   20.690  1.00 12.84 ? 17  HIS A C   1 
ATOM   129  O  O   . HIS A 1 17  ? 11.636  1.391   21.277  1.00 14.27 ? 17  HIS A O   1 
ATOM   130  C  CB  . HIS A 1 17  ? 10.416  -1.167  22.432  1.00 11.65 ? 17  HIS A CB  1 
ATOM   131  C  CG  . HIS A 1 17  ? 11.641  -2.049  22.360  1.00 13.21 ? 17  HIS A CG  1 
ATOM   132  N  ND1 . HIS A 1 17  ? 12.886  -1.624  22.805  1.00 19.18 ? 17  HIS A ND1 1 
ATOM   133  C  CD2 . HIS A 1 17  ? 11.823  -3.276  21.822  1.00 15.60 ? 17  HIS A CD2 1 
ATOM   134  C  CE1 . HIS A 1 17  ? 13.782  -2.568  22.538  1.00 14.27 ? 17  HIS A CE1 1 
ATOM   135  N  NE2 . HIS A 1 17  ? 13.163  -3.577  21.952  1.00 16.98 ? 17  HIS A NE2 1 
ATOM   136  N  N   . LYS A 1 18  ? 12.181  -0.208  19.714  1.00 14.93 ? 18  LYS A N   1 
ATOM   137  C  CA  . LYS A 1 18  ? 13.437  0.498   19.205  1.00 15.44 ? 18  LYS A CA  1 
ATOM   138  C  C   . LYS A 1 18  ? 13.096  1.833   18.561  1.00 16.87 ? 18  LYS A C   1 
ATOM   139  O  O   . LYS A 1 18  ? 13.662  2.849   18.961  1.00 20.39 ? 18  LYS A O   1 
ATOM   140  C  CB  . LYS A 1 18  ? 14.194  -0.388  18.229  1.00 16.43 ? 18  LYS A CB  1 
ATOM   141  C  CG  . LYS A 1 18  ? 14.917  -1.597  18.966  1.00 17.62 ? 18  LYS A CG  1 
ATOM   142  C  CD  . LYS A 1 18  ? 15.551  -2.567  17.984  1.00 17.17 ? 18  LYS A CD  1 
ATOM   143  C  CE  . LYS A 1 18  ? 14.534  -3.500  17.314  1.00 17.32 ? 18  LYS A CE  1 
ATOM   144  N  NZ  . LYS A 1 18  ? 15.204  -4.447  16.271  1.00 15.18 ? 18  LYS A NZ  1 
ATOM   145  N  N   . ASP A 1 19  ? 12.048  1.878   17.709  1.00 17.53 ? 19  ASP A N   1 
ATOM   146  C  CA  . ASP A 1 19  ? 11.598  3.152   17.126  1.00 18.32 ? 19  ASP A CA  1 
ATOM   147  C  C   . ASP A 1 19  ? 10.624  3.921   18.008  1.00 19.33 ? 19  ASP A C   1 
ATOM   148  O  O   . ASP A 1 19  ? 10.543  5.147   17.894  1.00 19.18 ? 19  ASP A O   1 
ATOM   149  C  CB  . ASP A 1 19  ? 11.009  2.960   15.727  1.00 19.94 ? 19  ASP A CB  1 
ATOM   150  C  CG  . ASP A 1 19  ? 12.051  2.974   14.652  1.00 25.57 ? 19  ASP A CG  1 
ATOM   151  O  OD1 . ASP A 1 19  ? 13.181  3.400   14.937  1.00 28.27 ? 19  ASP A OD1 1 
ATOM   152  O  OD2 . ASP A 1 19  ? 11.740  2.562   13.511  1.00 34.62 ? 19  ASP A OD2 1 
ATOM   153  N  N   . PHE A 1 20  ? 9.904   3.202   18.895  1.00 16.20 ? 20  PHE A N   1 
ATOM   154  C  CA  . PHE A 1 20  ? 8.720   3.737   19.595  1.00 16.13 ? 20  PHE A CA  1 
ATOM   155  C  C   . PHE A 1 20  ? 8.801   3.261   20.993  1.00 15.29 ? 20  PHE A C   1 
ATOM   156  O  O   . PHE A 1 20  ? 8.148   2.245   21.388  1.00 12.88 ? 20  PHE A O   1 
ATOM   157  C  CB  . PHE A 1 20  ? 7.418   3.242   18.897  1.00 16.03 ? 20  PHE A CB  1 
ATOM   158  C  CG  . PHE A 1 20  ? 7.328   3.664   17.473  1.00 13.50 ? 20  PHE A CG  1 
ATOM   159  C  CD1 . PHE A 1 20  ? 6.955   4.964   17.143  1.00 13.46 ? 20  PHE A CD1 1 
ATOM   160  C  CD2 . PHE A 1 20  ? 7.659   2.741   16.413  1.00 13.16 ? 20  PHE A CD2 1 
ATOM   161  C  CE1 . PHE A 1 20  ? 6.865   5.304   15.788  1.00 17.98 ? 20  PHE A CE1 1 
ATOM   162  C  CE2 . PHE A 1 20  ? 7.637   3.106   15.046  1.00 17.22 ? 20  PHE A CE2 1 
ATOM   163  C  CZ  . PHE A 1 20  ? 7.257   4.401   14.756  1.00 20.48 ? 20  PHE A CZ  1 
ATOM   164  N  N   . PRO A 1 21  ? 9.688   3.889   21.806  1.00 15.24 ? 21  PRO A N   1 
ATOM   165  C  CA  . PRO A 1 21  ? 9.934   3.406   23.165  1.00 14.45 ? 21  PRO A CA  1 
ATOM   166  C  C   . PRO A 1 21  ? 8.727   3.251   24.118  1.00 14.33 ? 21  PRO A C   1 
ATOM   167  O  O   . PRO A 1 21  ? 8.786   2.478   25.062  1.00 14.63 ? 21  PRO A O   1 
ATOM   168  C  CB  . PRO A 1 21  ? 10.924  4.454   23.776  1.00 17.81 ? 21  PRO A CB  1 
ATOM   169  C  CG  . PRO A 1 21  ? 11.501  5.118   22.662  1.00 18.34 ? 21  PRO A CG  1 
ATOM   170  C  CD  . PRO A 1 21  ? 10.552  5.050   21.459  1.00 16.72 ? 21  PRO A CD  1 
ATOM   171  N  N   A ILE A 1 22  ? 7.654   4.025   23.886  0.50 13.25 ? 22  ILE A N   1 
ATOM   172  N  N   B ILE A 1 22  ? 7.674   4.025   23.828  0.50 12.99 ? 22  ILE A N   1 
ATOM   173  C  CA  A ILE A 1 22  ? 6.428   3.919   24.675  0.50 13.24 ? 22  ILE A CA  1 
ATOM   174  C  CA  B ILE A 1 22  ? 6.414   3.969   24.527  0.50 12.43 ? 22  ILE A CA  1 
ATOM   175  C  C   A ILE A 1 22  ? 5.804   2.511   24.500  0.50 12.82 ? 22  ILE A C   1 
ATOM   176  C  C   B ILE A 1 22  ? 5.794   2.555   24.450  0.50 12.44 ? 22  ILE A C   1 
ATOM   177  O  O   A ILE A 1 22  ? 4.897   2.139   25.258  0.50 12.59 ? 22  ILE A O   1 
ATOM   178  O  O   B ILE A 1 22  ? 4.896   2.220   25.230  0.50 12.13 ? 22  ILE A O   1 
ATOM   179  C  CB  A ILE A 1 22  ? 5.374   5.009   24.293  0.50 11.18 ? 22  ILE A CB  1 
ATOM   180  C  CB  B ILE A 1 22  ? 5.419   4.998   23.939  0.50 10.58 ? 22  ILE A CB  1 
ATOM   181  C  CG1 A ILE A 1 22  ? 4.286   5.125   25.369  0.50 11.78 ? 22  ILE A CG1 1 
ATOM   182  C  CG1 B ILE A 1 22  ? 4.355   5.320   24.973  0.50 10.51 ? 22  ILE A CG1 1 
ATOM   183  C  CG2 A ILE A 1 22  ? 4.785   4.733   22.884  0.50 13.84 ? 22  ILE A CG2 1 
ATOM   184  C  CG2 B ILE A 1 22  ? 4.915   4.566   22.461  0.50 9.53  ? 22  ILE A CG2 1 
ATOM   185  C  CD1 A ILE A 1 22  ? 4.690   5.806   26.596  0.50 10.05 ? 22  ILE A CD1 1 
ATOM   186  C  CD1 B ILE A 1 22  ? 3.419   6.387   24.514  0.50 7.60  ? 22  ILE A CD1 1 
ATOM   187  N  N   . ALA A 1 23  ? 6.298   1.744   23.523  1.00 12.33 ? 23  ALA A N   1 
ATOM   188  C  CA  . ALA A 1 23  ? 5.899   0.279   23.425  1.00 13.12 ? 23  ALA A CA  1 
ATOM   189  C  C   . ALA A 1 23  ? 5.981   -0.469  24.756  1.00 14.35 ? 23  ALA A C   1 
ATOM   190  O  O   . ALA A 1 23  ? 5.236   -1.458  24.985  1.00 13.18 ? 23  ALA A O   1 
ATOM   191  C  CB  . ALA A 1 23  ? 6.772   -0.472  22.382  1.00 13.32 ? 23  ALA A CB  1 
ATOM   192  N  N   . LYS A 1 24  ? 6.877   -0.043  25.668  1.00 15.89 ? 24  LYS A N   1 
ATOM   193  C  CA  . LYS A 1 24  ? 7.048   -0.746  26.941  1.00 16.71 ? 24  LYS A CA  1 
ATOM   194  C  C   . LYS A 1 24  ? 6.435   0.130   28.054  1.00 17.30 ? 24  LYS A C   1 
ATOM   195  O  O   . LYS A 1 24  ? 6.850   0.043   29.225  1.00 19.40 ? 24  LYS A O   1 
ATOM   196  C  CB  . LYS A 1 24  ? 8.544   -0.947  27.246  1.00 18.45 ? 24  LYS A CB  1 
ATOM   197  C  CG  . LYS A 1 24  ? 9.288   -1.782  26.227  1.00 19.17 ? 24  LYS A CG  1 
ATOM   198  C  CD  . LYS A 1 24  ? 10.717  -1.966  26.740  1.00 21.53 ? 24  LYS A CD  1 
ATOM   199  C  CE  . LYS A 1 24  ? 11.485  -2.992  25.865  1.00 22.18 ? 24  LYS A CE  1 
ATOM   200  N  NZ  . LYS A 1 24  ? 11.050  -4.396  26.104  1.00 24.62 ? 24  LYS A NZ  1 
ATOM   201  N  N   . GLY A 1 25  ? 5.470   0.984   27.667  1.00 15.13 ? 25  GLY A N   1 
ATOM   202  C  CA  . GLY A 1 25  ? 4.886   1.998   28.580  1.00 15.74 ? 25  GLY A CA  1 
ATOM   203  C  C   . GLY A 1 25  ? 3.935   1.430   29.584  1.00 13.48 ? 25  GLY A C   1 
ATOM   204  O  O   . GLY A 1 25  ? 3.743   0.178   29.684  1.00 15.75 ? 25  GLY A O   1 
ATOM   205  N  N   . GLU A 1 26  ? 3.274   2.339   30.303  1.00 13.28 ? 26  GLU A N   1 
ATOM   206  C  CA  . GLU A 1 26  ? 2.453   1.937   31.405  1.00 13.56 ? 26  GLU A CA  1 
ATOM   207  C  C   . GLU A 1 26  ? 0.994   1.663   31.058  1.00 10.61 ? 26  GLU A C   1 
ATOM   208  O  O   . GLU A 1 26  ? 0.229   1.150   31.910  1.00 12.21 ? 26  GLU A O   1 
ATOM   209  C  CB  . GLU A 1 26  ? 2.467   3.019   32.536  1.00 16.93 ? 26  GLU A CB  1 
ATOM   210  C  CG  . GLU A 1 26  ? 3.805   3.322   33.203  1.00 20.81 ? 26  GLU A CG  1 
ATOM   211  C  CD  . GLU A 1 26  ? 4.455   2.043   33.732  1.00 29.30 ? 26  GLU A CD  1 
ATOM   212  O  OE1 . GLU A 1 26  ? 3.806   1.282   34.522  1.00 32.85 ? 26  GLU A OE1 1 
ATOM   213  O  OE2 . GLU A 1 26  ? 5.608   1.777   33.306  1.00 30.74 ? 26  GLU A OE2 1 
ATOM   214  N  N   . ARG A 1 27  ? 0.589   1.995   29.811  1.00 10.48 ? 27  ARG A N   1 
ATOM   215  C  CA  . ARG A 1 27  ? -0.843  1.782   29.477  1.00 9.86  ? 27  ARG A CA  1 
ATOM   216  C  C   . ARG A 1 27  ? -0.922  1.296   27.991  1.00 8.84  ? 27  ARG A C   1 
ATOM   217  O  O   . ARG A 1 27  ? -1.631  1.897   27.166  1.00 8.94  ? 27  ARG A O   1 
ATOM   218  C  CB  . ARG A 1 27  ? -1.745  2.994   29.844  1.00 9.81  ? 27  ARG A CB  1 
ATOM   219  C  CG  . ARG A 1 27  ? -1.444  4.248   29.015  1.00 14.24 ? 27  ARG A CG  1 
ATOM   220  C  CD  . ARG A 1 27  ? -2.388  5.542   29.266  1.00 17.74 ? 27  ARG A CD  1 
ATOM   221  N  NE  . ARG A 1 27  ? -3.630  5.449   28.467  1.00 19.00 ? 27  ARG A NE  1 
ATOM   222  C  CZ  . ARG A 1 27  ? -4.566  6.396   28.362  1.00 18.56 ? 27  ARG A CZ  1 
ATOM   223  N  NH1 . ARG A 1 27  ? -4.425  7.689   28.805  1.00 12.63 ? 27  ARG A NH1 1 
ATOM   224  N  NH2 . ARG A 1 27  ? -5.538  6.106   27.583  1.00 15.58 ? 27  ARG A NH2 1 
ATOM   225  N  N   . GLN A 1 28  ? -0.199  0.199   27.708  1.00 9.69  ? 28  GLN A N   1 
ATOM   226  C  CA  . GLN A 1 28  ? -0.180  -0.318  26.304  1.00 7.53  ? 28  GLN A CA  1 
ATOM   227  C  C   . GLN A 1 28  ? -1.334  -1.300  26.044  1.00 7.02  ? 28  GLN A C   1 
ATOM   228  O  O   . GLN A 1 28  ? -1.813  -2.014  26.944  1.00 8.06  ? 28  GLN A O   1 
ATOM   229  C  CB  . GLN A 1 28  ? 1.174   -1.019  26.050  1.00 8.11  ? 28  GLN A CB  1 
ATOM   230  C  CG  . GLN A 1 28  ? 2.310   0.022   25.952  1.00 6.74  ? 28  GLN A CG  1 
ATOM   231  C  CD  . GLN A 1 28  ? 2.151   0.882   24.643  1.00 8.41  ? 28  GLN A CD  1 
ATOM   232  O  OE1 . GLN A 1 28  ? 2.346   0.359   23.542  1.00 9.26  ? 28  GLN A OE1 1 
ATOM   233  N  NE2 . GLN A 1 28  ? 1.812   2.212   24.774  1.00 7.36  ? 28  GLN A NE2 1 
ATOM   234  N  N   . SER A 1 29  ? -1.708  -1.359  24.763  1.00 6.67  ? 29  SER A N   1 
ATOM   235  C  CA  . SER A 1 29  ? -2.800  -2.219  24.284  1.00 5.71  ? 29  SER A CA  1 
ATOM   236  C  C   . SER A 1 29  ? -2.250  -3.115  23.157  1.00 6.40  ? 29  SER A C   1 
ATOM   237  O  O   . SER A 1 29  ? -1.299  -2.728  22.479  1.00 8.52  ? 29  SER A O   1 
ATOM   238  C  CB  . SER A 1 29  ? -3.940  -1.392  23.674  1.00 5.69  ? 29  SER A CB  1 
ATOM   239  O  OG  . SER A 1 29  ? -4.546  -0.733  24.849  1.00 6.28  ? 29  SER A OG  1 
ATOM   240  N  N   . PRO A 1 30  ? -2.888  -4.265  22.914  1.00 7.45  ? 30  PRO A N   1 
ATOM   241  C  CA  . PRO A 1 30  ? -4.036  -4.836  23.638  1.00 6.22  ? 30  PRO A CA  1 
ATOM   242  C  C   . PRO A 1 30  ? -3.662  -5.506  24.946  1.00 6.25  ? 30  PRO A C   1 
ATOM   243  O  O   . PRO A 1 30  ? -2.455  -5.507  25.301  1.00 7.53  ? 30  PRO A O   1 
ATOM   244  C  CB  . PRO A 1 30  ? -4.563  -5.890  22.612  1.00 6.51  ? 30  PRO A CB  1 
ATOM   245  C  CG  . PRO A 1 30  ? -3.246  -6.475  21.945  1.00 8.97  ? 30  PRO A CG  1 
ATOM   246  C  CD  . PRO A 1 30  ? -2.375  -5.144  21.842  1.00 7.73  ? 30  PRO A CD  1 
ATOM   247  N  N   . VAL A 1 31  ? -4.670  -6.073  25.609  1.00 6.66  ? 31  VAL A N   1 
ATOM   248  C  CA  . VAL A 1 31  ? -4.476  -6.808  26.888  1.00 7.59  ? 31  VAL A CA  1 
ATOM   249  C  C   . VAL A 1 31  ? -5.391  -8.022  26.892  1.00 8.38  ? 31  VAL A C   1 
ATOM   250  O  O   . VAL A 1 31  ? -6.380  -8.095  26.117  1.00 7.96  ? 31  VAL A O   1 
ATOM   251  C  CB  . VAL A 1 31  ? -4.744  -5.935  28.187  1.00 9.32  ? 31  VAL A CB  1 
ATOM   252  C  CG1 . VAL A 1 31  ? -3.765  -4.755  28.261  1.00 7.61  ? 31  VAL A CG1 1 
ATOM   253  C  CG2 . VAL A 1 31  ? -6.306  -5.456  28.237  1.00 9.58  ? 31  VAL A CG2 1 
ATOM   254  N  N   . ASP A 1 32  ? -5.032  -9.007  27.747  1.00 7.85  ? 32  ASP A N   1 
ATOM   255  C  CA  . ASP A 1 32  ? -5.914  -10.106 27.983  1.00 7.01  ? 32  ASP A CA  1 
ATOM   256  C  C   . ASP A 1 32  ? -7.013  -9.635  28.947  1.00 8.52  ? 32  ASP A C   1 
ATOM   257  O  O   . ASP A 1 32  ? -6.675  -8.963  29.973  1.00 10.16 ? 32  ASP A O   1 
ATOM   258  C  CB  . ASP A 1 32  ? -5.158  -11.271 28.615  1.00 9.34  ? 32  ASP A CB  1 
ATOM   259  C  CG  . ASP A 1 32  ? -6.102  -12.389 28.919  1.00 13.46 ? 32  ASP A CG  1 
ATOM   260  O  OD1 . ASP A 1 32  ? -6.764  -12.842 27.941  1.00 9.90  ? 32  ASP A OD1 1 
ATOM   261  O  OD2 . ASP A 1 32  ? -6.211  -12.840 30.144  1.00 15.22 ? 32  ASP A OD2 1 
ATOM   262  N  N   . ILE A 1 33  ? -8.267  -9.893  28.589  1.00 8.07  ? 33  ILE A N   1 
ATOM   263  C  CA  . ILE A 1 33  ? -9.402  -9.514  29.435  1.00 10.18 ? 33  ILE A CA  1 
ATOM   264  C  C   . ILE A 1 33  ? -9.764  -10.719 30.310  1.00 11.24 ? 33  ILE A C   1 
ATOM   265  O  O   . ILE A 1 33  ? -10.353 -11.700 29.833  1.00 12.12 ? 33  ILE A O   1 
ATOM   266  C  CB  . ILE A 1 33  ? -10.640 -9.024  28.634  1.00 9.51  ? 33  ILE A CB  1 
ATOM   267  C  CG1 . ILE A 1 33  ? -10.298 -7.703  27.924  1.00 9.47  ? 33  ILE A CG1 1 
ATOM   268  C  CG2 . ILE A 1 33  ? -11.799 -8.701  29.611  1.00 10.45 ? 33  ILE A CG2 1 
ATOM   269  C  CD1 . ILE A 1 33  ? -11.167 -7.475  26.687  1.00 12.73 ? 33  ILE A CD1 1 
ATOM   270  N  N   . ASP A 1 34  ? -9.324  -10.625 31.570  1.00 12.09 ? 34  ASP A N   1 
ATOM   271  C  CA  . ASP A 1 34  ? -9.598  -11.708 32.606  1.00 11.86 ? 34  ASP A CA  1 
ATOM   272  C  C   . ASP A 1 34  ? -11.045 -11.413 33.133  1.00 13.50 ? 34  ASP A C   1 
ATOM   273  O  O   . ASP A 1 34  ? -11.261 -10.448 33.866  1.00 13.39 ? 34  ASP A O   1 
ATOM   274  C  CB  . ASP A 1 34  ? -8.506  -11.575 33.696  1.00 14.57 ? 34  ASP A CB  1 
ATOM   275  C  CG  . ASP A 1 34  ? -8.678  -12.569 34.861  1.00 20.75 ? 34  ASP A CG  1 
ATOM   276  O  OD1 . ASP A 1 34  ? -9.785  -13.033 35.085  1.00 18.13 ? 34  ASP A OD1 1 
ATOM   277  O  OD2 . ASP A 1 34  ? -7.664  -12.911 35.550  1.00 27.82 ? 34  ASP A OD2 1 
ATOM   278  N  N   . THR A 1 35  ? -12.026 -12.148 32.661  1.00 14.29 ? 35  THR A N   1 
ATOM   279  C  CA  . THR A 1 35  ? -13.442 -11.789 32.823  1.00 15.96 ? 35  THR A CA  1 
ATOM   280  C  C   . THR A 1 35  ? -13.856 -11.965 34.274  1.00 16.99 ? 35  THR A C   1 
ATOM   281  O  O   . THR A 1 35  ? -14.870 -11.381 34.762  1.00 18.10 ? 35  THR A O   1 
ATOM   282  C  CB  . THR A 1 35  ? -14.373 -12.731 32.030  1.00 17.26 ? 35  THR A CB  1 
ATOM   283  O  OG1 . THR A 1 35  ? -14.154 -14.082 32.431  1.00 16.52 ? 35  THR A OG1 1 
ATOM   284  C  CG2 . THR A 1 35  ? -14.178 -12.660 30.522  1.00 13.75 ? 35  THR A CG2 1 
ATOM   285  N  N   . HIS A 1 36  ? -13.073 -12.774 34.986  1.00 18.01 ? 36  HIS A N   1 
ATOM   286  C  CA  . HIS A 1 36  ? -13.427 -13.013 36.392  1.00 19.07 ? 36  HIS A CA  1 
ATOM   287  C  C   . HIS A 1 36  ? -12.914 -11.856 37.274  1.00 21.13 ? 36  HIS A C   1 
ATOM   288  O  O   . HIS A 1 36  ? -13.540 -11.578 38.318  1.00 24.89 ? 36  HIS A O   1 
ATOM   289  C  CB  . HIS A 1 36  ? -13.052 -14.482 36.799  1.00 20.17 ? 36  HIS A CB  1 
ATOM   290  C  CG  . HIS A 1 36  ? -13.967 -15.527 36.199  1.00 18.17 ? 36  HIS A CG  1 
ATOM   291  N  ND1 . HIS A 1 36  ? -15.305 -15.617 36.563  1.00 20.71 ? 36  HIS A ND1 1 
ATOM   292  C  CD2 . HIS A 1 36  ? -13.767 -16.489 35.260  1.00 18.97 ? 36  HIS A CD2 1 
ATOM   293  C  CE1 . HIS A 1 36  ? -15.877 -16.601 35.884  1.00 26.19 ? 36  HIS A CE1 1 
ATOM   294  N  NE2 . HIS A 1 36  ? -14.969 -17.130 35.072  1.00 22.52 ? 36  HIS A NE2 1 
ATOM   295  N  N   . THR A 1 37  ? -11.845 -11.165 36.861  1.00 21.32 ? 37  THR A N   1 
ATOM   296  C  CA  . THR A 1 37  ? -11.148 -10.108 37.606  1.00 20.52 ? 37  THR A CA  1 
ATOM   297  C  C   . THR A 1 37  ? -11.662 -8.672  37.203  1.00 18.45 ? 37  THR A C   1 
ATOM   298  O  O   . THR A 1 37  ? -11.366 -7.649  37.896  1.00 19.10 ? 37  THR A O   1 
ATOM   299  C  CB  . THR A 1 37  ? -9.615  -10.274 37.472  1.00 23.61 ? 37  THR A CB  1 
ATOM   300  O  OG1 . THR A 1 37  ? -9.202  -11.336 38.351  1.00 27.44 ? 37  THR A OG1 1 
ATOM   301  C  CG2 . THR A 1 37  ? -8.846  -9.038  37.897  1.00 24.24 ? 37  THR A CG2 1 
ATOM   302  N  N   . ALA A 1 38  ? -12.461 -8.632  36.131  1.00 17.64 ? 38  ALA A N   1 
ATOM   303  C  CA  . ALA A 1 38  ? -12.995 -7.344  35.618  1.00 16.07 ? 38  ALA A CA  1 
ATOM   304  C  C   . ALA A 1 38  ? -14.101 -6.988  36.640  1.00 17.99 ? 38  ALA A C   1 
ATOM   305  O  O   . ALA A 1 38  ? -14.863 -7.859  37.092  1.00 19.58 ? 38  ALA A O   1 
ATOM   306  C  CB  . ALA A 1 38  ? -13.556 -7.499  34.263  1.00 16.62 ? 38  ALA A CB  1 
ATOM   307  N  N   . LYS A 1 39  ? -14.176 -5.730  37.007  1.00 18.08 ? 39  LYS A N   1 
ATOM   308  C  CA  . LYS A 1 39  ? -15.146 -5.321  38.011  1.00 18.54 ? 39  LYS A CA  1 
ATOM   309  C  C   . LYS A 1 39  ? -16.432 -4.817  37.343  1.00 18.42 ? 39  LYS A C   1 
ATOM   310  O  O   . LYS A 1 39  ? -16.388 -3.851  36.601  1.00 17.74 ? 39  LYS A O   1 
ATOM   311  C  CB  . LYS A 1 39  ? -14.474 -4.217  38.789  1.00 17.62 ? 39  LYS A CB  1 
ATOM   312  C  CG  . LYS A 1 39  ? -15.343 -3.367  39.712  1.00 21.94 ? 39  LYS A CG  1 
ATOM   313  C  CD  . LYS A 1 39  ? -15.422 -3.992  41.072  1.00 23.27 ? 39  LYS A CD  1 
ATOM   314  C  CE  . LYS A 1 39  ? -16.266 -3.102  42.007  1.00 25.10 ? 39  LYS A CE  1 
ATOM   315  N  NZ  . LYS A 1 39  ? -16.672 -3.762  43.313  1.00 25.06 ? 39  LYS A NZ  1 
ATOM   316  N  N   . TYR A 1 40  ? -17.575 -5.383  37.721  1.00 19.84 ? 40  TYR A N   1 
ATOM   317  C  CA  . TYR A 1 40  ? -18.853 -4.792  37.328  1.00 20.96 ? 40  TYR A CA  1 
ATOM   318  C  C   . TYR A 1 40  ? -18.997 -3.368  37.917  1.00 21.27 ? 40  TYR A C   1 
ATOM   319  O  O   . TYR A 1 40  ? -18.807 -3.126  39.159  1.00 18.91 ? 40  TYR A O   1 
ATOM   320  C  CB  . TYR A 1 40  ? -19.999 -5.728  37.689  1.00 23.71 ? 40  TYR A CB  1 
ATOM   321  C  CG  . TYR A 1 40  ? -21.336 -5.092  37.546  1.00 22.76 ? 40  TYR A CG  1 
ATOM   322  C  CD1 . TYR A 1 40  ? -21.770 -4.588  36.327  1.00 23.28 ? 40  TYR A CD1 1 
ATOM   323  C  CD2 . TYR A 1 40  ? -22.177 -4.974  38.658  1.00 29.45 ? 40  TYR A CD2 1 
ATOM   324  C  CE1 . TYR A 1 40  ? -22.970 -4.005  36.192  1.00 24.27 ? 40  TYR A CE1 1 
ATOM   325  C  CE2 . TYR A 1 40  ? -23.398 -4.364  38.539  1.00 26.17 ? 40  TYR A CE2 1 
ATOM   326  C  CZ  . TYR A 1 40  ? -23.790 -3.903  37.314  1.00 28.17 ? 40  TYR A CZ  1 
ATOM   327  O  OH  . TYR A 1 40  ? -25.003 -3.325  37.208  1.00 29.36 ? 40  TYR A OH  1 
ATOM   328  N  N   . ASP A 1 41  ? -19.313 -2.399  37.052  1.00 19.67 ? 41  ASP A N   1 
ATOM   329  C  CA  . ASP A 1 41  ? -19.371 -1.013  37.522  1.00 20.97 ? 41  ASP A CA  1 
ATOM   330  C  C   . ASP A 1 41  ? -20.785 -0.479  37.264  1.00 22.49 ? 41  ASP A C   1 
ATOM   331  O  O   . ASP A 1 41  ? -21.097 -0.031  36.156  1.00 19.80 ? 41  ASP A O   1 
ATOM   332  C  CB  . ASP A 1 41  ? -18.339 -0.128  36.882  1.00 22.40 ? 41  ASP A CB  1 
ATOM   333  C  CG  . ASP A 1 41  ? -18.379 1.279   37.463  1.00 26.30 ? 41  ASP A CG  1 
ATOM   334  O  OD1 . ASP A 1 41  ? -19.330 1.543   38.256  1.00 28.39 ? 41  ASP A OD1 1 
ATOM   335  O  OD2 . ASP A 1 41  ? -17.489 2.105   37.151  1.00 25.06 ? 41  ASP A OD2 1 
ATOM   336  N  N   . PRO A 1 42  ? -21.695 -0.646  38.246  1.00 23.94 ? 42  PRO A N   1 
ATOM   337  C  CA  . PRO A 1 42  ? -23.033 -0.131  37.969  1.00 25.45 ? 42  PRO A CA  1 
ATOM   338  C  C   . PRO A 1 42  ? -23.141 1.373   37.682  1.00 25.83 ? 42  PRO A C   1 
ATOM   339  O  O   . PRO A 1 42  ? -24.220 1.797   37.230  1.00 29.01 ? 42  PRO A O   1 
ATOM   340  C  CB  . PRO A 1 42  ? -23.857 -0.546  39.229  1.00 25.00 ? 42  PRO A CB  1 
ATOM   341  C  CG  . PRO A 1 42  ? -22.815 -0.816  40.300  1.00 26.64 ? 42  PRO A CG  1 
ATOM   342  C  CD  . PRO A 1 42  ? -21.658 -1.390  39.526  1.00 24.93 ? 42  PRO A CD  1 
ATOM   343  N  N   . SER A 1 43  ? -22.097 2.191   37.874  1.00 26.07 ? 43  SER A N   1 
ATOM   344  C  CA  . SER A 1 43  ? -22.203 3.589   37.362  1.00 26.80 ? 43  SER A CA  1 
ATOM   345  C  C   . SER A 1 43  ? -21.896 3.768   35.854  1.00 25.73 ? 43  SER A C   1 
ATOM   346  O  O   . SER A 1 43  ? -22.037 4.883   35.303  1.00 27.10 ? 43  SER A O   1 
ATOM   347  C  CB  . SER A 1 43  ? -21.362 4.598   38.161  1.00 26.23 ? 43  SER A CB  1 
ATOM   348  O  OG  . SER A 1 43  ? -19.998 4.245   38.090  1.00 28.71 ? 43  SER A OG  1 
ATOM   349  N  N   . LEU A 1 44  ? -21.396 2.722   35.188  1.00 25.54 ? 44  LEU A N   1 
ATOM   350  C  CA  . LEU A 1 44  ? -21.160 2.833   33.739  1.00 23.82 ? 44  LEU A CA  1 
ATOM   351  C  C   . LEU A 1 44  ? -22.504 2.977   33.057  1.00 25.73 ? 44  LEU A C   1 
ATOM   352  O  O   . LEU A 1 44  ? -23.449 2.257   33.403  1.00 26.67 ? 44  LEU A O   1 
ATOM   353  C  CB  . LEU A 1 44  ? -20.482 1.575   33.184  1.00 23.18 ? 44  LEU A CB  1 
ATOM   354  C  CG  . LEU A 1 44  ? -19.005 1.521   33.532  1.00 20.35 ? 44  LEU A CG  1 
ATOM   355  C  CD1 . LEU A 1 44  ? -18.491 0.101   33.182  1.00 19.12 ? 44  LEU A CD1 1 
ATOM   356  C  CD2 . LEU A 1 44  ? -18.294 2.639   32.798  1.00 17.88 ? 44  LEU A CD2 1 
ATOM   357  N  N   . LYS A 1 45  ? -22.583 3.913   32.120  1.00 24.58 ? 45  LYS A N   1 
ATOM   358  C  CA  . LYS A 1 45  ? -23.807 4.123   31.289  1.00 24.56 ? 45  LYS A CA  1 
ATOM   359  C  C   . LYS A 1 45  ? -23.840 3.198   30.120  1.00 24.04 ? 45  LYS A C   1 
ATOM   360  O  O   . LYS A 1 45  ? -22.772 2.634   29.740  1.00 24.30 ? 45  LYS A O   1 
ATOM   361  C  CB  . LYS A 1 45  ? -23.810 5.514   30.787  1.00 24.66 ? 45  LYS A CB  1 
ATOM   362  C  CG  . LYS A 1 45  ? -23.623 6.475   31.942  1.00 27.29 ? 45  LYS A CG  1 
ATOM   363  C  CD  . LYS A 1 45  ? -23.500 7.893   31.419  1.00 36.55 ? 45  LYS A CD  1 
ATOM   364  C  CE  . LYS A 1 45  ? -24.735 8.721   31.689  1.00 39.24 ? 45  LYS A CE  1 
ATOM   365  N  NZ  . LYS A 1 45  ? -25.077 9.646   30.554  1.00 42.02 ? 45  LYS A NZ  1 
ATOM   366  N  N   . PRO A 1 46  ? -25.064 2.996   29.527  1.00 21.60 ? 46  PRO A N   1 
ATOM   367  C  CA  . PRO A 1 46  ? -25.140 2.298   28.232  1.00 21.88 ? 46  PRO A CA  1 
ATOM   368  C  C   . PRO A 1 46  ? -24.251 3.075   27.263  1.00 20.23 ? 46  PRO A C   1 
ATOM   369  O  O   . PRO A 1 46  ? -24.202 4.305   27.337  1.00 21.46 ? 46  PRO A O   1 
ATOM   370  C  CB  . PRO A 1 46  ? -26.607 2.453   27.812  1.00 20.38 ? 46  PRO A CB  1 
ATOM   371  C  CG  . PRO A 1 46  ? -27.375 2.749   29.085  1.00 21.95 ? 46  PRO A CG  1 
ATOM   372  C  CD  . PRO A 1 46  ? -26.394 3.367   30.072  1.00 23.00 ? 46  PRO A CD  1 
ATOM   373  N  N   . LEU A 1 47  ? -23.580 2.349   26.370  1.00 21.29 ? 47  LEU A N   1 
ATOM   374  C  CA  . LEU A 1 47  ? -22.890 2.956   25.268  1.00 19.33 ? 47  LEU A CA  1 
ATOM   375  C  C   . LEU A 1 47  ? -23.919 3.570   24.292  1.00 20.88 ? 47  LEU A C   1 
ATOM   376  O  O   . LEU A 1 47  ? -24.933 2.947   23.983  1.00 21.29 ? 47  LEU A O   1 
ATOM   377  C  CB  . LEU A 1 47  ? -22.135 1.856   24.532  1.00 20.41 ? 47  LEU A CB  1 
ATOM   378  C  CG  . LEU A 1 47  ? -20.956 2.226   23.693  1.00 24.04 ? 47  LEU A CG  1 
ATOM   379  C  CD1 . LEU A 1 47  ? -19.947 3.059   24.479  1.00 23.81 ? 47  LEU A CD1 1 
ATOM   380  C  CD2 . LEU A 1 47  ? -20.351 0.926   23.234  1.00 24.94 ? 47  LEU A CD2 1 
ATOM   381  N  N   . SER A 1 48  ? -23.638 4.761   23.793  1.00 16.71 ? 48  SER A N   1 
ATOM   382  C  CA  . SER A 1 48  ? -24.447 5.381   22.784  1.00 17.08 ? 48  SER A CA  1 
ATOM   383  C  C   . SER A 1 48  ? -23.702 5.373   21.490  1.00 16.51 ? 48  SER A C   1 
ATOM   384  O  O   . SER A 1 48  ? -22.750 6.114   21.291  1.00 15.02 ? 48  SER A O   1 
ATOM   385  C  CB  . SER A 1 48  ? -24.824 6.826   23.168  1.00 17.26 ? 48  SER A CB  1 
ATOM   386  O  OG  . SER A 1 48  ? -25.482 7.457   22.094  1.00 18.31 ? 48  SER A OG  1 
ATOM   387  N  N   . VAL A 1 49  ? -24.205 4.575   20.577  1.00 16.08 ? 49  VAL A N   1 
ATOM   388  C  CA  . VAL A 1 49  ? -23.644 4.507   19.244  1.00 18.03 ? 49  VAL A CA  1 
ATOM   389  C  C   . VAL A 1 49  ? -24.609 5.130   18.235  1.00 19.30 ? 49  VAL A C   1 
ATOM   390  O  O   . VAL A 1 49  ? -25.665 4.586   17.959  1.00 21.85 ? 49  VAL A O   1 
ATOM   391  C  CB  . VAL A 1 49  ? -23.283 3.051   18.852  1.00 18.30 ? 49  VAL A CB  1 
ATOM   392  C  CG1 . VAL A 1 49  ? -22.527 3.070   17.480  1.00 22.26 ? 49  VAL A CG1 1 
ATOM   393  C  CG2 . VAL A 1 49  ? -22.532 2.312   20.018  1.00 18.84 ? 49  VAL A CG2 1 
ATOM   394  N  N   . SER A 1 50  ? -24.275 6.288   17.696  1.00 16.88 ? 50  SER A N   1 
ATOM   395  C  CA  . SER A 1 50  ? -25.197 7.003   16.803  1.00 19.16 ? 50  SER A CA  1 
ATOM   396  C  C   . SER A 1 50  ? -24.638 7.058   15.389  1.00 17.99 ? 50  SER A C   1 
ATOM   397  O  O   . SER A 1 50  ? -23.928 7.978   15.016  1.00 19.00 ? 50  SER A O   1 
ATOM   398  C  CB  . SER A 1 50  ? -25.590 8.374   17.367  1.00 18.41 ? 50  SER A CB  1 
ATOM   399  O  OG  . SER A 1 50  ? -26.121 8.167   18.675  1.00 27.47 ? 50  SER A OG  1 
ATOM   400  N  N   . TYR A 1 51  ? -24.885 5.979   14.636  1.00 17.99 ? 51  TYR A N   1 
ATOM   401  C  CA  . TYR A 1 51  ? -24.314 5.795   13.271  1.00 17.45 ? 51  TYR A CA  1 
ATOM   402  C  C   . TYR A 1 51  ? -25.257 6.063   12.073  1.00 19.47 ? 51  TYR A C   1 
ATOM   403  O  O   . TYR A 1 51  ? -24.821 5.898   10.933  1.00 19.28 ? 51  TYR A O   1 
ATOM   404  C  CB  . TYR A 1 51  ? -23.577 4.432   13.064  1.00 15.86 ? 51  TYR A CB  1 
ATOM   405  C  CG  . TYR A 1 51  ? -22.261 4.197   13.823  1.00 14.62 ? 51  TYR A CG  1 
ATOM   406  C  CD1 . TYR A 1 51  ? -21.551 5.263   14.447  1.00 14.16 ? 51  TYR A CD1 1 
ATOM   407  C  CD2 . TYR A 1 51  ? -21.745 2.909   13.930  1.00 13.13 ? 51  TYR A CD2 1 
ATOM   408  C  CE1 . TYR A 1 51  ? -20.327 4.979   15.197  1.00 12.78 ? 51  TYR A CE1 1 
ATOM   409  C  CE2 . TYR A 1 51  ? -20.600 2.616   14.609  1.00 15.58 ? 51  TYR A CE2 1 
ATOM   410  C  CZ  . TYR A 1 51  ? -19.857 3.657   15.219  1.00 14.00 ? 51  TYR A CZ  1 
ATOM   411  O  OH  . TYR A 1 51  ? -18.721 3.302   15.899  1.00 12.08 ? 51  TYR A OH  1 
ATOM   412  N  N   A ASP A 1 52  ? -26.486 6.532   12.380  0.50 20.01 ? 52  ASP A N   1 
ATOM   413  N  N   B ASP A 1 52  ? -26.503 6.463   12.343  0.50 20.27 ? 52  ASP A N   1 
ATOM   414  C  CA  A ASP A 1 52  ? -27.532 6.864   11.370  0.50 20.68 ? 52  ASP A CA  1 
ATOM   415  C  CA  B ASP A 1 52  ? -27.475 6.781   11.277  0.50 21.11 ? 52  ASP A CA  1 
ATOM   416  C  C   A ASP A 1 52  ? -27.086 7.759   10.193  0.50 21.04 ? 52  ASP A C   1 
ATOM   417  C  C   B ASP A 1 52  ? -26.866 7.603   10.105  0.50 21.18 ? 52  ASP A C   1 
ATOM   418  O  O   A ASP A 1 52  ? -27.536 7.574   9.065   0.50 21.83 ? 52  ASP A O   1 
ATOM   419  O  O   B ASP A 1 52  ? -26.974 7.217   8.917   0.50 20.71 ? 52  ASP A O   1 
ATOM   420  C  CB  A ASP A 1 52  ? -28.826 7.396   12.043  0.50 20.96 ? 52  ASP A CB  1 
ATOM   421  C  CB  B ASP A 1 52  ? -28.686 7.481   11.911  0.50 21.57 ? 52  ASP A CB  1 
ATOM   422  C  CG  A ASP A 1 52  ? -28.553 8.352   13.216  0.50 19.75 ? 52  ASP A CG  1 
ATOM   423  C  CG  B ASP A 1 52  ? -29.698 7.890   10.914  0.50 23.25 ? 52  ASP A CG  1 
ATOM   424  O  OD1 A ASP A 1 52  ? -28.101 7.937   14.316  0.50 26.22 ? 52  ASP A OD1 1 
ATOM   425  O  OD1 B ASP A 1 52  ? -30.308 7.004   10.274  0.50 28.06 ? 52  ASP A OD1 1 
ATOM   426  O  OD2 A ASP A 1 52  ? -28.823 9.551   13.046  0.50 27.76 ? 52  ASP A OD2 1 
ATOM   427  O  OD2 B ASP A 1 52  ? -29.876 9.114   10.749  0.50 26.43 ? 52  ASP A OD2 1 
ATOM   428  N  N   . GLN A 1 53  ? -26.166 8.679   10.445  1.00 20.67 ? 53  GLN A N   1 
ATOM   429  C  CA  . GLN A 1 53  ? -25.687 9.606   9.399   1.00 21.65 ? 53  GLN A CA  1 
ATOM   430  C  C   . GLN A 1 53  ? -24.237 9.380   8.942   1.00 19.72 ? 53  GLN A C   1 
ATOM   431  O  O   . GLN A 1 53  ? -23.698 10.236  8.287   1.00 18.97 ? 53  GLN A O   1 
ATOM   432  C  CB  . GLN A 1 53  ? -25.861 11.039  9.891   1.00 22.40 ? 53  GLN A CB  1 
ATOM   433  C  CG  . GLN A 1 53  ? -27.205 11.350  10.452  1.00 27.71 ? 53  GLN A CG  1 
ATOM   434  C  CD  . GLN A 1 53  ? -28.168 11.634  9.338   1.00 32.94 ? 53  GLN A CD  1 
ATOM   435  O  OE1 . GLN A 1 53  ? -28.161 12.735  8.757   1.00 41.06 ? 53  GLN A OE1 1 
ATOM   436  N  NE2 . GLN A 1 53  ? -28.994 10.648  9.007   1.00 34.07 ? 53  GLN A NE2 1 
ATOM   437  N  N   . ALA A 1 54  ? -23.587 8.253   9.317   1.00 17.66 ? 54  ALA A N   1 
ATOM   438  C  CA  . ALA A 1 54  ? -22.260 7.964   8.878   1.00 17.06 ? 54  ALA A CA  1 
ATOM   439  C  C   . ALA A 1 54  ? -22.103 8.115   7.379   1.00 17.67 ? 54  ALA A C   1 
ATOM   440  O  O   . ALA A 1 54  ? -22.966 7.660   6.605   1.00 17.81 ? 54  ALA A O   1 
ATOM   441  C  CB  . ALA A 1 54  ? -21.774 6.519   9.387   1.00 16.71 ? 54  ALA A CB  1 
ATOM   442  N  N   . THR A 1 55  ? -21.046 8.799   6.975   1.00 15.91 ? 55  THR A N   1 
ATOM   443  C  CA  . THR A 1 55  ? -20.658 8.983   5.580   1.00 16.52 ? 55  THR A CA  1 
ATOM   444  C  C   . THR A 1 55  ? -19.318 8.390   5.267   1.00 15.27 ? 55  THR A C   1 
ATOM   445  O  O   . THR A 1 55  ? -18.298 8.998   5.513   1.00 12.44 ? 55  THR A O   1 
ATOM   446  C  CB  . THR A 1 55  ? -20.580 10.501  5.199   1.00 18.28 ? 55  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 55  ? -21.832 11.073  5.469   1.00 23.92 ? 55  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 55  ? -20.311 10.561  3.686   1.00 18.52 ? 55  THR A CG2 1 
ATOM   449  N  N   . SER A 1 56  ? -19.293 7.156   4.783   1.00 16.05 ? 56  SER A N   1 
ATOM   450  C  CA  . SER A 1 56  ? -18.035 6.600   4.352   1.00 16.26 ? 56  SER A CA  1 
ATOM   451  C  C   . SER A 1 56  ? -17.485 7.300   3.064   1.00 16.63 ? 56  SER A C   1 
ATOM   452  O  O   . SER A 1 56  ? -18.218 7.870   2.216   1.00 19.88 ? 56  SER A O   1 
ATOM   453  C  CB  . SER A 1 56  ? -18.106 5.043   4.154   1.00 17.06 ? 56  SER A CB  1 
ATOM   454  O  OG  . SER A 1 56  ? -19.063 4.663   3.119   1.00 19.50 ? 56  SER A OG  1 
ATOM   455  N  N   . LEU A 1 57  ? -16.202 7.333   2.930   1.00 16.56 ? 57  LEU A N   1 
ATOM   456  C  CA  . LEU A 1 57  ? -15.638 7.948   1.682   1.00 18.11 ? 57  LEU A CA  1 
ATOM   457  C  C   . LEU A 1 57  ? -14.842 6.993   0.817   1.00 18.26 ? 57  LEU A C   1 
ATOM   458  O  O   . LEU A 1 57  ? -14.880 7.064   -0.442  1.00 18.40 ? 57  LEU A O   1 
ATOM   459  C  CB  . LEU A 1 57  ? -14.757 9.130   2.018   1.00 17.57 ? 57  LEU A CB  1 
ATOM   460  C  CG  . LEU A 1 57  ? -15.560 10.301  2.690   1.00 21.02 ? 57  LEU A CG  1 
ATOM   461  C  CD1 . LEU A 1 57  ? -14.521 11.287  3.224   1.00 25.13 ? 57  LEU A CD1 1 
ATOM   462  C  CD2 . LEU A 1 57  ? -16.576 10.988  1.754   1.00 24.97 ? 57  LEU A CD2 1 
ATOM   463  N  N   . ARG A 1 58  ? -14.029 6.185   1.482   1.00 16.57 ? 58  ARG A N   1 
ATOM   464  C  CA  . ARG A 1 58  ? -12.938 5.567   0.826   1.00 15.52 ? 58  ARG A CA  1 
ATOM   465  C  C   . ARG A 1 58  ? -12.427 4.394   1.613   1.00 15.15 ? 58  ARG A C   1 
ATOM   466  O  O   . ARG A 1 58  ? -12.486 4.398   2.858   1.00 14.41 ? 58  ARG A O   1 
ATOM   467  C  CB  . ARG A 1 58  ? -11.781 6.541   0.733   1.00 15.17 ? 58  ARG A CB  1 
ATOM   468  C  CG  . ARG A 1 58  ? -10.840 6.215   -0.291  1.00 21.19 ? 58  ARG A CG  1 
ATOM   469  C  CD  . ARG A 1 58  ? -9.881  7.380   -0.392  1.00 29.45 ? 58  ARG A CD  1 
ATOM   470  N  NE  . ARG A 1 58  ? -9.022  7.315   0.793   1.00 28.03 ? 58  ARG A NE  1 
ATOM   471  C  CZ  . ARG A 1 58  ? -7.701  7.418   0.752   1.00 26.26 ? 58  ARG A CZ  1 
ATOM   472  N  NH1 . ARG A 1 58  ? -7.115  7.662   -0.420  1.00 28.04 ? 58  ARG A NH1 1 
ATOM   473  N  NH2 . ARG A 1 58  ? -6.985  7.386   1.897   1.00 24.01 ? 58  ARG A NH2 1 
ATOM   474  N  N   . ILE A 1 59  ? -11.834 3.485   0.865   1.00 13.86 ? 59  ILE A N   1 
ATOM   475  C  CA  . ILE A 1 59  ? -11.160 2.335   1.534   1.00 13.54 ? 59  ILE A CA  1 
ATOM   476  C  C   . ILE A 1 59  ? -9.724  2.290   1.036   1.00 13.61 ? 59  ILE A C   1 
ATOM   477  O  O   . ILE A 1 59  ? -9.420  2.446   -0.173  1.00 14.83 ? 59  ILE A O   1 
ATOM   478  C  CB  . ILE A 1 59  ? -12.006 1.035   1.323   1.00 11.18 ? 59  ILE A CB  1 
ATOM   479  C  CG1 . ILE A 1 59  ? -11.385 -0.134  2.125   1.00 12.93 ? 59  ILE A CG1 1 
ATOM   480  C  CG2 . ILE A 1 59  ? -11.978 0.678   -0.255  1.00 12.61 ? 59  ILE A CG2 1 
ATOM   481  C  CD1 . ILE A 1 59  ? -12.059 -1.559  1.795   1.00 11.83 ? 59  ILE A CD1 1 
ATOM   482  N  N   . LEU A 1 60  ? -8.776  2.025   1.944   1.00 14.44 ? 60  LEU A N   1 
ATOM   483  C  CA  . LEU A 1 60  ? -7.397  2.101   1.670   1.00 13.09 ? 60  LEU A CA  1 
ATOM   484  C  C   . LEU A 1 60  ? -6.563  0.957   2.244   1.00 14.76 ? 60  LEU A C   1 
ATOM   485  O  O   . LEU A 1 60  ? -6.758  0.602   3.422   1.00 15.24 ? 60  LEU A O   1 
ATOM   486  C  CB  . LEU A 1 60  ? -6.954  3.448   2.307   1.00 14.75 ? 60  LEU A CB  1 
ATOM   487  C  CG  . LEU A 1 60  ? -5.467  3.632   2.387   1.00 16.67 ? 60  LEU A CG  1 
ATOM   488  C  CD1 . LEU A 1 60  ? -4.801  3.813   0.972   1.00 21.65 ? 60  LEU A CD1 1 
ATOM   489  C  CD2 . LEU A 1 60  ? -5.146  4.762   3.364   1.00 15.12 ? 60  LEU A CD2 1 
ATOM   490  N  N   . ASN A 1 61  ? -5.732  0.329   1.412   1.00 14.80 ? 61  ASN A N   1 
ATOM   491  C  CA  . ASN A 1 61  ? -4.685  -0.584  1.899   1.00 14.71 ? 61  ASN A CA  1 
ATOM   492  C  C   . ASN A 1 61  ? -3.440  0.227   2.288   1.00 15.65 ? 61  ASN A C   1 
ATOM   493  O  O   . ASN A 1 61  ? -2.747  0.808   1.410   1.00 16.09 ? 61  ASN A O   1 
ATOM   494  C  CB  . ASN A 1 61  ? -4.302  -1.675  0.850   1.00 13.95 ? 61  ASN A CB  1 
ATOM   495  C  CG  . ASN A 1 61  ? -3.190  -2.632  1.279   1.00 17.00 ? 61  ASN A CG  1 
ATOM   496  O  OD1 . ASN A 1 61  ? -2.326  -2.390  2.133   1.00 14.63 ? 61  ASN A OD1 1 
ATOM   497  N  ND2 . ASN A 1 61  ? -3.221  -3.846  0.635   1.00 15.65 ? 61  ASN A ND2 1 
ATOM   498  N  N   . ASN A 1 62  ? -3.132  0.286   3.582   1.00 14.74 ? 62  ASN A N   1 
ATOM   499  C  CA  . ASN A 1 62  ? -1.937  1.071   4.029   1.00 15.55 ? 62  ASN A CA  1 
ATOM   500  C  C   . ASN A 1 62  ? -0.671  0.268   4.267   1.00 16.94 ? 62  ASN A C   1 
ATOM   501  O  O   . ASN A 1 62  ? 0.352   0.786   4.829   1.00 18.77 ? 62  ASN A O   1 
ATOM   502  C  CB  . ASN A 1 62  ? -2.350  1.980   5.243   1.00 15.85 ? 62  ASN A CB  1 
ATOM   503  C  CG  . ASN A 1 62  ? -2.774  1.149   6.432   1.00 16.11 ? 62  ASN A CG  1 
ATOM   504  O  OD1 . ASN A 1 62  ? -2.424  -0.044  6.536   1.00 13.96 ? 62  ASN A OD1 1 
ATOM   505  N  ND2 . ASN A 1 62  ? -3.436  1.804   7.381   1.00 19.44 ? 62  ASN A ND2 1 
ATOM   506  N  N   . GLY A 1 63  ? -0.654  -1.020  3.854   1.00 12.00 ? 63  GLY A N   1 
ATOM   507  C  CA  . GLY A 1 63  ? 0.467   -1.849  4.076   1.00 13.48 ? 63  GLY A CA  1 
ATOM   508  C  C   . GLY A 1 63  ? 0.453   -2.612  5.393   1.00 12.20 ? 63  GLY A C   1 
ATOM   509  O  O   . GLY A 1 63  ? 1.245   -3.506  5.540   1.00 15.90 ? 63  GLY A O   1 
ATOM   510  N  N   A HIS A 1 64  ? -0.485  -2.265  6.261   0.50 13.20 ? 64  HIS A N   1 
ATOM   511  N  N   B HIS A 1 64  ? -0.423  -2.219  6.341   0.50 12.89 ? 64  HIS A N   1 
ATOM   512  C  CA  A HIS A 1 64  ? -0.594  -2.924  7.556   0.50 12.57 ? 64  HIS A CA  1 
ATOM   513  C  CA  B HIS A 1 64  ? -0.630  -2.962  7.641   0.50 12.04 ? 64  HIS A CA  1 
ATOM   514  C  C   A HIS A 1 64  ? -1.969  -3.599  7.641   0.50 12.50 ? 64  HIS A C   1 
ATOM   515  C  C   B HIS A 1 64  ? -2.063  -3.416  7.933   0.50 11.19 ? 64  HIS A C   1 
ATOM   516  O  O   A HIS A 1 64  ? -2.036  -4.801  8.028   0.50 12.61 ? 64  HIS A O   1 
ATOM   517  O  O   B HIS A 1 64  ? -2.294  -4.265  8.790   0.50 10.46 ? 64  HIS A O   1 
ATOM   518  C  CB  A HIS A 1 64  ? -0.332  -1.928  8.691   0.50 12.06 ? 64  HIS A CB  1 
ATOM   519  C  CB  B HIS A 1 64  ? -0.097  -2.258  8.902   0.50 11.57 ? 64  HIS A CB  1 
ATOM   520  C  CG  A HIS A 1 64  ? 0.967   -1.175  8.537   0.50 11.18 ? 64  HIS A CG  1 
ATOM   521  C  CG  B HIS A 1 64  ? -0.608  -0.865  9.130   0.50 12.27 ? 64  HIS A CG  1 
ATOM   522  N  ND1 A HIS A 1 64  ? 2.196   -1.804  8.587   0.50 14.05 ? 64  HIS A ND1 1 
ATOM   523  N  ND1 B HIS A 1 64  ? 0.001   0.232   8.561   0.50 14.55 ? 64  HIS A ND1 1 
ATOM   524  C  CD2 A HIS A 1 64  ? 1.219   0.132   8.302   0.50 12.18 ? 64  HIS A CD2 1 
ATOM   525  C  CD2 B HIS A 1 64  ? -1.564  -0.375  9.965   0.50 14.16 ? 64  HIS A CD2 1 
ATOM   526  C  CE1 A HIS A 1 64  ? 3.154   -0.903  8.447   0.50 12.48 ? 64  HIS A CE1 1 
ATOM   527  C  CE1 B HIS A 1 64  ? -0.588  1.334   8.996   0.50 16.84 ? 64  HIS A CE1 1 
ATOM   528  N  NE2 A HIS A 1 64  ? 2.583   0.279   8.258   0.50 10.24 ? 64  HIS A NE2 1 
ATOM   529  N  NE2 B HIS A 1 64  ? -1.540  0.992   9.848   0.50 17.67 ? 64  HIS A NE2 1 
ATOM   530  N  N   . ALA A 1 65  ? -3.024  -2.873  7.216   1.00 11.50 ? 65  ALA A N   1 
ATOM   531  C  CA  . ALA A 1 65  ? -4.448  -3.348  7.287   1.00 10.54 ? 65  ALA A CA  1 
ATOM   532  C  C   . ALA A 1 65  ? -5.185  -2.620  6.152   1.00 10.03 ? 65  ALA A C   1 
ATOM   533  O  O   . ALA A 1 65  ? -4.512  -1.974  5.257   1.00 11.57 ? 65  ALA A O   1 
ATOM   534  C  CB  . ALA A 1 65  ? -5.072  -3.116  8.691   1.00 9.11  ? 65  ALA A CB  1 
ATOM   535  N  N   . PHE A 1 66  ? -6.514  -2.647  6.153   1.00 8.49  ? 66  PHE A N   1 
ATOM   536  C  CA  . PHE A 1 66  ? -7.273  -1.745  5.287   1.00 10.95 ? 66  PHE A CA  1 
ATOM   537  C  C   . PHE A 1 66  ? -8.220  -0.860  6.090   1.00 12.35 ? 66  PHE A C   1 
ATOM   538  O  O   . PHE A 1 66  ? -8.927  -1.349  6.970   1.00 10.21 ? 66  PHE A O   1 
ATOM   539  C  CB  . PHE A 1 66  ? -8.055  -2.539  4.239   1.00 9.71  ? 66  PHE A CB  1 
ATOM   540  C  CG  . PHE A 1 66  ? -9.135  -3.408  4.819   1.00 12.10 ? 66  PHE A CG  1 
ATOM   541  C  CD1 . PHE A 1 66  ? -10.355 -2.866  5.186   1.00 12.24 ? 66  PHE A CD1 1 
ATOM   542  C  CD2 . PHE A 1 66  ? -8.929  -4.766  4.996   1.00 12.65 ? 66  PHE A CD2 1 
ATOM   543  C  CE1 . PHE A 1 66  ? -11.351 -3.663  5.719   1.00 12.23 ? 66  PHE A CE1 1 
ATOM   544  C  CE2 . PHE A 1 66  ? -9.921  -5.567  5.528   1.00 9.34  ? 66  PHE A CE2 1 
ATOM   545  C  CZ  . PHE A 1 66  ? -11.133 -5.015  5.890   1.00 10.79 ? 66  PHE A CZ  1 
ATOM   546  N  N   . ASN A 1 67  ? -8.239  0.439   5.795   1.00 10.83 ? 67  ASN A N   1 
ATOM   547  C  CA  . ASN A 1 67  ? -9.093  1.339   6.567   1.00 12.49 ? 67  ASN A CA  1 
ATOM   548  C  C   . ASN A 1 67  ? -10.322 1.743   5.763   1.00 11.83 ? 67  ASN A C   1 
ATOM   549  O  O   . ASN A 1 67  ? -10.138 2.146   4.584   1.00 15.82 ? 67  ASN A O   1 
ATOM   550  C  CB  . ASN A 1 67  ? -8.393  2.659   6.936   1.00 12.87 ? 67  ASN A CB  1 
ATOM   551  C  CG  . ASN A 1 67  ? -7.249  2.516   7.910   1.00 17.32 ? 67  ASN A CG  1 
ATOM   552  O  OD1 . ASN A 1 67  ? -6.523  3.528   8.150   1.00 21.99 ? 67  ASN A OD1 1 
ATOM   553  N  ND2 . ASN A 1 67  ? -7.030  1.328   8.456   1.00 11.65 ? 67  ASN A ND2 1 
ATOM   554  N  N   . VAL A 1 68  ? -11.505 1.637   6.337   1.00 13.82 ? 68  VAL A N   1 
ATOM   555  C  CA  . VAL A 1 68  ? -12.689 2.255   5.758   1.00 12.59 ? 68  VAL A CA  1 
ATOM   556  C  C   . VAL A 1 68  ? -12.759 3.663   6.422   1.00 16.35 ? 68  VAL A C   1 
ATOM   557  O  O   . VAL A 1 68  ? -12.907 3.763   7.662   1.00 13.45 ? 68  VAL A O   1 
ATOM   558  C  CB  . VAL A 1 68  ? -13.944 1.421   5.905   1.00 15.83 ? 68  VAL A CB  1 
ATOM   559  C  CG1 . VAL A 1 68  ? -15.227 2.249   5.492   1.00 15.98 ? 68  VAL A CG1 1 
ATOM   560  C  CG2 . VAL A 1 68  ? -13.789 0.153   5.022   1.00 13.79 ? 68  VAL A CG2 1 
ATOM   561  N  N   . GLU A 1 69  ? -12.627 4.733   5.616   1.00 16.57 ? 69  GLU A N   1 
ATOM   562  C  CA  . GLU A 1 69  ? -12.511 6.105   6.180   1.00 17.99 ? 69  GLU A CA  1 
ATOM   563  C  C   . GLU A 1 69  ? -13.824 6.837   6.036   1.00 17.27 ? 69  GLU A C   1 
ATOM   564  O  O   . GLU A 1 69  ? -14.574 6.602   5.052   1.00 19.12 ? 69  GLU A O   1 
ATOM   565  C  CB  . GLU A 1 69  ? -11.462 6.872   5.449   1.00 19.95 ? 69  GLU A CB  1 
ATOM   566  C  CG  . GLU A 1 69  ? -10.098 6.201   5.419   1.00 22.51 ? 69  GLU A CG  1 
ATOM   567  C  CD  . GLU A 1 69  ? -9.365  6.694   4.244   1.00 27.01 ? 69  GLU A CD  1 
ATOM   568  O  OE1 . GLU A 1 69  ? -10.072 7.305   3.402   1.00 25.63 ? 69  GLU A OE1 1 
ATOM   569  O  OE2 . GLU A 1 69  ? -8.125  6.481   4.159   1.00 26.98 ? 69  GLU A OE2 1 
ATOM   570  N  N   . PHE A 1 70  ? -14.104 7.732   6.980   1.00 12.87 ? 70  PHE A N   1 
ATOM   571  C  CA  . PHE A 1 70  ? -15.389 8.441   7.013   1.00 12.08 ? 70  PHE A CA  1 
ATOM   572  C  C   . PHE A 1 70  ? -15.149 9.940   6.988   1.00 12.51 ? 70  PHE A C   1 
ATOM   573  O  O   . PHE A 1 70  ? -14.106 10.402  7.343   1.00 12.36 ? 70  PHE A O   1 
ATOM   574  C  CB  . PHE A 1 70  ? -16.145 8.111   8.258   1.00 12.25 ? 70  PHE A CB  1 
ATOM   575  C  CG  . PHE A 1 70  ? -16.679 6.717   8.242   1.00 10.43 ? 70  PHE A CG  1 
ATOM   576  C  CD1 . PHE A 1 70  ? -15.846 5.615   8.477   1.00 13.91 ? 70  PHE A CD1 1 
ATOM   577  C  CD2 . PHE A 1 70  ? -18.015 6.479   8.010   1.00 11.33 ? 70  PHE A CD2 1 
ATOM   578  C  CE1 . PHE A 1 70  ? -16.404 4.297   8.412   1.00 11.76 ? 70  PHE A CE1 1 
ATOM   579  C  CE2 . PHE A 1 70  ? -18.540 5.183   7.928   1.00 11.31 ? 70  PHE A CE2 1 
ATOM   580  C  CZ  . PHE A 1 70  ? -17.689 4.079   8.101   1.00 13.84 ? 70  PHE A CZ  1 
ATOM   581  N  N   A ASP A 1 71  ? -16.226 10.650  6.636   0.50 13.27 ? 71  ASP A N   1 
ATOM   582  N  N   B ASP A 1 71  ? -16.080 10.684  6.444   0.50 13.45 ? 71  ASP A N   1 
ATOM   583  C  CA  A ASP A 1 71  ? -16.267 12.112  6.737   0.50 11.49 ? 71  ASP A CA  1 
ATOM   584  C  CA  B ASP A 1 71  ? -15.934 12.130  6.507   0.50 11.53 ? 71  ASP A CA  1 
ATOM   585  C  C   A ASP A 1 71  ? -16.490 12.416  8.175   0.50 11.48 ? 71  ASP A C   1 
ATOM   586  C  C   B ASP A 1 71  ? -16.419 12.555  7.896   0.50 11.39 ? 71  ASP A C   1 
ATOM   587  O  O   A ASP A 1 71  ? -17.544 12.129  8.786   0.50 13.74 ? 71  ASP A O   1 
ATOM   588  O  O   B ASP A 1 71  ? -17.615 12.476  8.159   0.50 13.23 ? 71  ASP A O   1 
ATOM   589  C  CB  A ASP A 1 71  ? -17.401 12.695  5.903   0.50 10.84 ? 71  ASP A CB  1 
ATOM   590  C  CB  B ASP A 1 71  ? -16.760 12.678  5.355   0.50 10.96 ? 71  ASP A CB  1 
ATOM   591  C  CG  A ASP A 1 71  ? -17.658 14.179  6.176   0.50 8.49  ? 71  ASP A CG  1 
ATOM   592  C  CG  B ASP A 1 71  ? -16.976 14.148  5.416   0.50 10.56 ? 71  ASP A CG  1 
ATOM   593  O  OD1 A ASP A 1 71  ? -16.948 14.851  6.891   0.50 13.73 ? 71  ASP A OD1 1 
ATOM   594  O  OD1 B ASP A 1 71  ? -16.345 14.815  6.214   0.50 9.80  ? 71  ASP A OD1 1 
ATOM   595  O  OD2 A ASP A 1 71  ? -18.660 14.670  5.667   0.50 13.15 ? 71  ASP A OD2 1 
ATOM   596  O  OD2 B ASP A 1 71  ? -17.789 14.632  4.600   0.50 16.86 ? 71  ASP A OD2 1 
ATOM   597  N  N   . ASP A 1 72  ? -15.476 13.005  8.746   1.00 11.44 ? 72  ASP A N   1 
ATOM   598  C  CA  . ASP A 1 72  ? -15.619 13.359  10.170  1.00 11.62 ? 72  ASP A CA  1 
ATOM   599  C  C   . ASP A 1 72  ? -15.586 14.871  10.315  1.00 15.46 ? 72  ASP A C   1 
ATOM   600  O  O   . ASP A 1 72  ? -15.088 15.373  11.335  1.00 14.51 ? 72  ASP A O   1 
ATOM   601  C  CB  . ASP A 1 72  ? -14.458 12.720  10.986  1.00 13.86 ? 72  ASP A CB  1 
ATOM   602  C  CG  . ASP A 1 72  ? -13.074 13.254  10.592  1.00 16.63 ? 72  ASP A CG  1 
ATOM   603  O  OD1 . ASP A 1 72  ? -12.899 13.975  9.564   1.00 14.61 ? 72  ASP A OD1 1 
ATOM   604  O  OD2 . ASP A 1 72  ? -12.082 12.925  11.285  1.00 17.59 ? 72  ASP A OD2 1 
ATOM   605  N  N   . SER A 1 73  ? -16.110 15.566  9.299   1.00 15.24 ? 73  SER A N   1 
ATOM   606  C  CA  . SER A 1 73  ? -16.068 17.057  9.342   1.00 16.72 ? 73  SER A CA  1 
ATOM   607  C  C   . SER A 1 73  ? -17.329 17.617  9.937   1.00 17.34 ? 73  SER A C   1 
ATOM   608  O  O   . SER A 1 73  ? -17.472 18.856  10.096  1.00 15.93 ? 73  SER A O   1 
ATOM   609  C  CB  . SER A 1 73  ? -15.747 17.647  7.952   1.00 16.17 ? 73  SER A CB  1 
ATOM   610  O  OG  . SER A 1 73  ? -16.841 17.428  7.040   1.00 16.09 ? 73  SER A OG  1 
ATOM   611  N  N   . GLN A 1 74  ? -18.265 16.724  10.290  1.00 17.30 ? 74  GLN A N   1 
ATOM   612  C  CA  . GLN A 1 74  ? -19.450 17.132  11.015  1.00 20.77 ? 74  GLN A CA  1 
ATOM   613  C  C   . GLN A 1 74  ? -19.786 16.076  12.000  1.00 20.73 ? 74  GLN A C   1 
ATOM   614  O  O   . GLN A 1 74  ? -19.258 15.004  11.941  1.00 19.30 ? 74  GLN A O   1 
ATOM   615  C  CB  . GLN A 1 74  ? -20.691 17.287  10.102  1.00 20.27 ? 74  GLN A CB  1 
ATOM   616  C  CG  . GLN A 1 74  ? -20.620 18.342  9.027   1.00 24.35 ? 74  GLN A CG  1 
ATOM   617  C  CD  . GLN A 1 74  ? -21.940 18.435  8.288   1.00 24.91 ? 74  GLN A CD  1 
ATOM   618  O  OE1 . GLN A 1 74  ? -22.924 18.937  8.836   1.00 35.37 ? 74  GLN A OE1 1 
ATOM   619  N  NE2 . GLN A 1 74  ? -21.990 17.896  7.079   1.00 24.78 ? 74  GLN A NE2 1 
ATOM   620  N  N   A ASP A 1 75  ? -20.582 16.428  13.015  0.50 21.63 ? 75  ASP A N   1 
ATOM   621  N  N   B ASP A 1 75  ? -20.811 16.411  12.771  0.50 21.72 ? 75  ASP A N   1 
ATOM   622  C  CA  A ASP A 1 75  ? -21.019 15.431  13.993  0.50 21.40 ? 75  ASP A CA  1 
ATOM   623  C  CA  B ASP A 1 75  ? -21.324 15.673  13.892  0.50 21.94 ? 75  ASP A CA  1 
ATOM   624  C  C   A ASP A 1 75  ? -22.076 14.605  13.239  0.50 22.01 ? 75  ASP A C   1 
ATOM   625  C  C   B ASP A 1 75  ? -22.168 14.415  13.471  0.50 22.44 ? 75  ASP A C   1 
ATOM   626  O  O   A ASP A 1 75  ? -23.256 15.013  13.127  0.50 21.60 ? 75  ASP A O   1 
ATOM   627  O  O   B ASP A 1 75  ? -23.310 14.285  13.899  0.50 22.52 ? 75  ASP A O   1 
ATOM   628  C  CB  A ASP A 1 75  ? -21.611 16.070  15.275  0.50 21.87 ? 75  ASP A CB  1 
ATOM   629  C  CB  B ASP A 1 75  ? -22.161 16.745  14.633  0.50 22.22 ? 75  ASP A CB  1 
ATOM   630  C  CG  A ASP A 1 75  ? -20.631 16.100  16.485  0.50 22.88 ? 75  ASP A CG  1 
ATOM   631  C  CG  B ASP A 1 75  ? -22.843 16.250  15.859  0.50 22.53 ? 75  ASP A CG  1 
ATOM   632  O  OD1 A ASP A 1 75  ? -19.723 15.247  16.612  0.50 22.93 ? 75  ASP A OD1 1 
ATOM   633  O  OD1 B ASP A 1 75  ? -23.944 16.786  16.133  0.50 21.79 ? 75  ASP A OD1 1 
ATOM   634  O  OD2 A ASP A 1 75  ? -20.834 16.958  17.382  0.50 23.68 ? 75  ASP A OD2 1 
ATOM   635  O  OD2 B ASP A 1 75  ? -22.290 15.384  16.558  0.50 18.54 ? 75  ASP A OD2 1 
ATOM   636  N  N   . LYS A 1 76  ? -21.617 13.489  12.684  1.00 21.57 ? 76  LYS A N   1 
ATOM   637  C  CA  . LYS A 1 76  ? -22.495 12.479  11.951  1.00 23.11 ? 76  LYS A CA  1 
ATOM   638  C  C   . LYS A 1 76  ? -22.576 11.006  12.442  1.00 25.07 ? 76  LYS A C   1 
ATOM   639  O  O   . LYS A 1 76  ? -23.592 10.263  12.202  1.00 28.21 ? 76  LYS A O   1 
ATOM   640  C  CB  . LYS A 1 76  ? -22.129 12.431  10.468  1.00 23.98 ? 76  LYS A CB  1 
ATOM   641  C  CG  . LYS A 1 76  ? -22.809 13.505  9.592   1.00 26.54 ? 76  LYS A CG  1 
ATOM   642  C  CD  . LYS A 1 76  ? -21.823 13.811  8.488   1.00 30.78 ? 76  LYS A CD  1 
ATOM   643  C  CE  . LYS A 1 76  ? -22.428 14.370  7.196   1.00 33.98 ? 76  LYS A CE  1 
ATOM   644  N  NZ  . LYS A 1 76  ? -21.391 14.261  6.121   1.00 27.97 ? 76  LYS A NZ  1 
ATOM   645  N  N   . ALA A 1 77  ? -21.480 10.528  12.965  1.00 22.42 ? 77  ALA A N   1 
ATOM   646  C  CA  . ALA A 1 77  ? -21.346 9.125   13.442  1.00 18.68 ? 77  ALA A CA  1 
ATOM   647  C  C   . ALA A 1 77  ? -20.615 9.268   14.759  1.00 18.88 ? 77  ALA A C   1 
ATOM   648  O  O   . ALA A 1 77  ? -19.384 9.331   14.748  1.00 21.32 ? 77  ALA A O   1 
ATOM   649  C  CB  . ALA A 1 77  ? -20.487 8.377   12.502  1.00 18.78 ? 77  ALA A CB  1 
ATOM   650  N  N   . VAL A 1 78  ? -21.344 9.336   15.845  1.00 17.66 ? 78  VAL A N   1 
ATOM   651  C  CA  . VAL A 1 78  ? -20.702 9.609   17.149  1.00 17.07 ? 78  VAL A CA  1 
ATOM   652  C  C   . VAL A 1 78  ? -20.909 8.485   18.186  1.00 15.20 ? 78  VAL A C   1 
ATOM   653  O  O   . VAL A 1 78  ? -21.977 7.809   18.242  1.00 15.39 ? 78  VAL A O   1 
ATOM   654  C  CB  . VAL A 1 78  ? -21.133 10.974  17.775  1.00 19.36 ? 78  VAL A CB  1 
ATOM   655  C  CG1 . VAL A 1 78  ? -20.788 12.161  16.846  1.00 21.20 ? 78  VAL A CG1 1 
ATOM   656  C  CG2 . VAL A 1 78  ? -22.561 10.902  18.159  1.00 20.90 ? 78  VAL A CG2 1 
ATOM   657  N  N   . LEU A 1 79  ? -19.865 8.329   19.027  1.00 12.29 ? 79  LEU A N   1 
ATOM   658  C  CA  . LEU A 1 79  ? -19.885 7.463   20.143  1.00 13.37 ? 79  LEU A CA  1 
ATOM   659  C  C   . LEU A 1 79  ? -19.870 8.347   21.378  1.00 14.78 ? 79  LEU A C   1 
ATOM   660  O  O   . LEU A 1 79  ? -19.112 9.325   21.446  1.00 14.59 ? 79  LEU A O   1 
ATOM   661  C  CB  . LEU A 1 79  ? -18.611 6.524   20.038  1.00 13.06 ? 79  LEU A CB  1 
ATOM   662  C  CG  . LEU A 1 79  ? -18.507 5.462   21.101  1.00 15.51 ? 79  LEU A CG  1 
ATOM   663  C  CD1 . LEU A 1 79  ? -19.568 4.393   20.887  1.00 19.56 ? 79  LEU A CD1 1 
ATOM   664  C  CD2 . LEU A 1 79  ? -17.151 4.783   20.967  1.00 12.56 ? 79  LEU A CD2 1 
ATOM   665  N  N   . LYS A 1 80  ? -20.736 8.024   22.330  1.00 13.44 ? 80  LYS A N   1 
ATOM   666  C  CA  . LYS A 1 80  ? -20.739 8.700   23.632  1.00 16.54 ? 80  LYS A CA  1 
ATOM   667  C  C   . LYS A 1 80  ? -21.392 7.808   24.716  1.00 16.04 ? 80  LYS A C   1 
ATOM   668  O  O   . LYS A 1 80  ? -21.726 6.666   24.426  1.00 12.20 ? 80  LYS A O   1 
ATOM   669  C  CB  . LYS A 1 80  ? -21.367 10.121  23.500  1.00 17.43 ? 80  LYS A CB  1 
ATOM   670  C  CG  . LYS A 1 80  ? -22.841 10.020  23.231  1.00 22.61 ? 80  LYS A CG  1 
ATOM   671  C  CD  . LYS A 1 80  ? -23.577 11.369  23.288  1.00 22.61 ? 80  LYS A CD  1 
ATOM   672  C  CE  . LYS A 1 80  ? -25.001 11.036  23.783  1.00 27.57 ? 80  LYS A CE  1 
ATOM   673  N  NZ  . LYS A 1 80  ? -26.044 12.060  23.457  1.00 37.63 ? 80  LYS A NZ  1 
ATOM   674  N  N   . GLY A 1 81  ? -21.538 8.351   25.933  1.00 15.29 ? 81  GLY A N   1 
ATOM   675  C  CA  . GLY A 1 81  ? -21.994 7.638   27.106  1.00 16.87 ? 81  GLY A CA  1 
ATOM   676  C  C   . GLY A 1 81  ? -21.029 6.533   27.386  1.00 18.18 ? 81  GLY A C   1 
ATOM   677  O  O   . GLY A 1 81  ? -19.816 6.707   27.209  1.00 15.90 ? 81  GLY A O   1 
ATOM   678  N  N   . GLY A 1 82  ? -21.546 5.382   27.799  1.00 19.29 ? 82  GLY A N   1 
ATOM   679  C  CA  . GLY A 1 82  ? -20.622 4.356   28.315  1.00 19.66 ? 82  GLY A CA  1 
ATOM   680  C  C   . GLY A 1 82  ? -19.680 4.977   29.341  1.00 18.10 ? 82  GLY A C   1 
ATOM   681  O  O   . GLY A 1 82  ? -20.116 5.720   30.273  1.00 19.30 ? 82  GLY A O   1 
ATOM   682  N  N   . PRO A 1 83  ? -18.343 4.723   29.215  1.00 16.32 ? 83  PRO A N   1 
ATOM   683  C  CA  . PRO A 1 83  ? -17.385 5.318   30.122  1.00 14.50 ? 83  PRO A CA  1 
ATOM   684  C  C   . PRO A 1 83  ? -16.947 6.750   29.714  1.00 16.11 ? 83  PRO A C   1 
ATOM   685  O  O   . PRO A 1 83  ? -16.169 7.369   30.415  1.00 18.03 ? 83  PRO A O   1 
ATOM   686  C  CB  . PRO A 1 83  ? -16.139 4.398   29.975  1.00 18.12 ? 83  PRO A CB  1 
ATOM   687  C  CG  . PRO A 1 83  ? -16.226 3.997   28.563  1.00 14.17 ? 83  PRO A CG  1 
ATOM   688  C  CD  . PRO A 1 83  ? -17.670 3.856   28.194  1.00 14.58 ? 83  PRO A CD  1 
ATOM   689  N  N   . LEU A 1 84  ? -17.492 7.293   28.646  1.00 15.62 ? 84  LEU A N   1 
ATOM   690  C  CA  . LEU A 1 84  ? -16.864 8.494   28.018  1.00 15.01 ? 84  LEU A CA  1 
ATOM   691  C  C   . LEU A 1 84  ? -17.512 9.740   28.604  1.00 18.29 ? 84  LEU A C   1 
ATOM   692  O  O   . LEU A 1 84  ? -18.703 9.730   28.862  1.00 18.84 ? 84  LEU A O   1 
ATOM   693  C  CB  . LEU A 1 84  ? -17.089 8.475   26.532  1.00 13.64 ? 84  LEU A CB  1 
ATOM   694  C  CG  . LEU A 1 84  ? -16.616 7.145   25.855  1.00 12.26 ? 84  LEU A CG  1 
ATOM   695  C  CD1 . LEU A 1 84  ? -17.113 6.999   24.461  1.00 13.28 ? 84  LEU A CD1 1 
ATOM   696  C  CD2 . LEU A 1 84  ? -15.000 7.023   25.899  1.00 13.04 ? 84  LEU A CD2 1 
ATOM   697  N  N   . ASP A 1 85  ? -16.691 10.771  28.735  1.00 19.70 ? 85  ASP A N   1 
ATOM   698  C  CA  . ASP A 1 85  ? -17.177 12.123  28.933  1.00 22.71 ? 85  ASP A CA  1 
ATOM   699  C  C   . ASP A 1 85  ? -17.179 12.778  27.543  1.00 23.80 ? 85  ASP A C   1 
ATOM   700  O  O   . ASP A 1 85  ? -16.204 12.672  26.751  1.00 23.99 ? 85  ASP A O   1 
ATOM   701  C  CB  . ASP A 1 85  ? -16.230 12.827  29.924  1.00 22.98 ? 85  ASP A CB  1 
ATOM   702  C  CG  . ASP A 1 85  ? -16.396 12.298  31.367  1.00 30.23 ? 85  ASP A CG  1 
ATOM   703  O  OD1 . ASP A 1 85  ? -17.522 11.845  31.674  1.00 35.29 ? 85  ASP A OD1 1 
ATOM   704  O  OD2 . ASP A 1 85  ? -15.432 12.338  32.191  1.00 30.52 ? 85  ASP A OD2 1 
ATOM   705  N  N   . GLY A 1 86  ? -18.259 13.462  27.204  1.00 24.67 ? 86  GLY A N   1 
ATOM   706  C  CA  . GLY A 1 86  ? -18.314 14.063  25.890  1.00 23.14 ? 86  GLY A CA  1 
ATOM   707  C  C   . GLY A 1 86  ? -18.526 13.164  24.677  1.00 24.06 ? 86  GLY A C   1 
ATOM   708  O  O   . GLY A 1 86  ? -19.102 12.100  24.765  1.00 25.62 ? 86  GLY A O   1 
ATOM   709  N  N   . THR A 1 87  ? -18.077 13.631  23.522  1.00 20.57 ? 87  THR A N   1 
ATOM   710  C  CA  . THR A 1 87  ? -18.560 13.130  22.245  1.00 18.60 ? 87  THR A CA  1 
ATOM   711  C  C   . THR A 1 87  ? -17.366 12.762  21.408  1.00 16.43 ? 87  THR A C   1 
ATOM   712  O  O   . THR A 1 87  ? -16.415 13.541  21.302  1.00 14.92 ? 87  THR A O   1 
ATOM   713  C  CB  . THR A 1 87  ? -19.420 14.260  21.509  1.00 21.03 ? 87  THR A CB  1 
ATOM   714  O  OG1 . THR A 1 87  ? -20.709 14.301  22.194  1.00 24.98 ? 87  THR A OG1 1 
ATOM   715  C  CG2 . THR A 1 87  ? -19.598 13.921  19.990  1.00 24.39 ? 87  THR A CG2 1 
ATOM   716  N  N   . TYR A 1 88  ? -17.376 11.540  20.856  1.00 12.55 ? 88  TYR A N   1 
ATOM   717  C  CA  . TYR A 1 88  ? -16.269 11.108  19.977  1.00 12.02 ? 88  TYR A CA  1 
ATOM   718  C  C   . TYR A 1 88  ? -16.729 10.797  18.552  1.00 12.24 ? 88  TYR A C   1 
ATOM   719  O  O   . TYR A 1 88  ? -17.757 10.099  18.360  1.00 15.52 ? 88  TYR A O   1 
ATOM   720  C  CB  . TYR A 1 88  ? -15.635 9.856   20.559  1.00 10.49 ? 88  TYR A CB  1 
ATOM   721  C  CG  . TYR A 1 88  ? -14.867 10.058  21.889  1.00 8.96  ? 88  TYR A CG  1 
ATOM   722  C  CD1 . TYR A 1 88  ? -15.518 10.359  23.101  1.00 10.54 ? 88  TYR A CD1 1 
ATOM   723  C  CD2 . TYR A 1 88  ? -13.454 9.902   21.896  1.00 10.56 ? 88  TYR A CD2 1 
ATOM   724  C  CE1 . TYR A 1 88  ? -14.806 10.524  24.295  1.00 10.09 ? 88  TYR A CE1 1 
ATOM   725  C  CE2 . TYR A 1 88  ? -12.689 10.099  23.097  1.00 8.01  ? 88  TYR A CE2 1 
ATOM   726  C  CZ  . TYR A 1 88  ? -13.381 10.333  24.303  1.00 9.10  ? 88  TYR A CZ  1 
ATOM   727  O  OH  . TYR A 1 88  ? -12.693 10.501  25.455  1.00 11.02 ? 88  TYR A OH  1 
ATOM   728  N  N   . ARG A 1 89  ? -16.022 11.334  17.586  1.00 10.66 ? 89  ARG A N   1 
ATOM   729  C  CA  . ARG A 1 89  ? -16.456 11.234  16.185  1.00 10.26 ? 89  ARG A CA  1 
ATOM   730  C  C   . ARG A 1 89  ? -15.777 10.063  15.436  1.00 8.35  ? 89  ARG A C   1 
ATOM   731  O  O   . ARG A 1 89  ? -14.558 9.954   15.499  1.00 9.16  ? 89  ARG A O   1 
ATOM   732  C  CB  . ARG A 1 89  ? -16.173 12.542  15.471  1.00 14.43 ? 89  ARG A CB  1 
ATOM   733  C  CG  . ARG A 1 89  ? -17.067 12.731  14.343  1.00 21.21 ? 89  ARG A CG  1 
ATOM   734  C  CD  . ARG A 1 89  ? -16.955 14.103  13.767  1.00 22.37 ? 89  ARG A CD  1 
ATOM   735  N  NE  . ARG A 1 89  ? -17.565 15.087  14.648  1.00 21.96 ? 89  ARG A NE  1 
ATOM   736  C  CZ  . ARG A 1 89  ? -17.495 16.390  14.444  1.00 20.08 ? 89  ARG A CZ  1 
ATOM   737  N  NH1 . ARG A 1 89  ? -16.868 16.873  13.413  1.00 19.31 ? 89  ARG A NH1 1 
ATOM   738  N  NH2 . ARG A 1 89  ? -18.087 17.229  15.285  1.00 22.28 ? 89  ARG A NH2 1 
ATOM   739  N  N   . LEU A 1 90  ? -16.547 9.203   14.711  1.00 7.83  ? 90  LEU A N   1 
ATOM   740  C  CA  . LEU A 1 90  ? -15.933 8.108   13.885  1.00 7.64  ? 90  LEU A CA  1 
ATOM   741  C  C   . LEU A 1 90  ? -15.093 8.678   12.747  1.00 8.55  ? 90  LEU A C   1 
ATOM   742  O  O   . LEU A 1 90  ? -15.607 9.488   11.918  1.00 10.46 ? 90  LEU A O   1 
ATOM   743  C  CB  . LEU A 1 90  ? -17.083 7.244   13.252  1.00 9.27  ? 90  LEU A CB  1 
ATOM   744  C  CG  . LEU A 1 90  ? -16.558 6.119   12.402  1.00 10.63 ? 90  LEU A CG  1 
ATOM   745  C  CD1 . LEU A 1 90  ? -15.676 5.072   13.198  1.00 12.09 ? 90  LEU A CD1 1 
ATOM   746  C  CD2 . LEU A 1 90  ? -17.776 5.392   11.774  1.00 10.63 ? 90  LEU A CD2 1 
ATOM   747  N  N   . ILE A 1 91  ? -13.845 8.244   12.701  1.00 7.73  ? 91  ILE A N   1 
ATOM   748  C  CA  . ILE A 1 91  ? -12.914 8.590   11.572  1.00 8.71  ? 91  ILE A CA  1 
ATOM   749  C  C   . ILE A 1 91  ? -12.640 7.407   10.631  1.00 9.14  ? 91  ILE A C   1 
ATOM   750  O  O   . ILE A 1 91  ? -12.614 7.563   9.399   1.00 10.47 ? 91  ILE A O   1 
ATOM   751  C  CB  . ILE A 1 91  ? -11.633 9.301   12.047  1.00 7.94  ? 91  ILE A CB  1 
ATOM   752  C  CG1 . ILE A 1 91  ? -10.708 9.558   10.842  1.00 11.94 ? 91  ILE A CG1 1 
ATOM   753  C  CG2 . ILE A 1 91  ? -10.930 8.485   13.110  1.00 8.82  ? 91  ILE A CG2 1 
ATOM   754  C  CD1 . ILE A 1 91  ? -9.518  10.466  11.265  1.00 15.42 ? 91  ILE A CD1 1 
ATOM   755  N  N   . GLN A 1 92  ? -12.428 6.195   11.194  1.00 9.59  ? 92  GLN A N   1 
ATOM   756  C  CA  . GLN A 1 92  ? -12.157 5.038   10.281  1.00 7.66  ? 92  GLN A CA  1 
ATOM   757  C  C   . GLN A 1 92  ? -12.397 3.781   11.067  1.00 7.82  ? 92  GLN A C   1 
ATOM   758  O  O   . GLN A 1 92  ? -12.504 3.839   12.260  1.00 6.78  ? 92  GLN A O   1 
ATOM   759  C  CB  . GLN A 1 92  ? -10.712 5.012   9.738   1.00 8.67  ? 92  GLN A CB  1 
ATOM   760  C  CG  . GLN A 1 92  ? -9.612  5.193   10.812  1.00 11.32 ? 92  GLN A CG  1 
ATOM   761  C  CD  . GLN A 1 92  ? -8.903  3.904   11.237  1.00 11.78 ? 92  GLN A CD  1 
ATOM   762  O  OE1 . GLN A 1 92  ? -9.460  2.815   11.138  1.00 9.09  ? 92  GLN A OE1 1 
ATOM   763  N  NE2 . GLN A 1 92  ? -7.710  4.065   11.797  1.00 14.74 ? 92  GLN A NE2 1 
ATOM   764  N  N   . PHE A 1 93  ? -12.606 2.684   10.349  1.00 7.26  ? 93  PHE A N   1 
ATOM   765  C  CA  . PHE A 1 93  ? -12.513 1.394   10.950  1.00 7.45  ? 93  PHE A CA  1 
ATOM   766  C  C   . PHE A 1 93  ? -11.543 0.518   10.168  1.00 9.53  ? 93  PHE A C   1 
ATOM   767  O  O   . PHE A 1 93  ? -11.308 0.694   9.004   1.00 9.37  ? 93  PHE A O   1 
ATOM   768  C  CB  . PHE A 1 93  ? -13.848 0.742   11.213  1.00 7.37  ? 93  PHE A CB  1 
ATOM   769  C  CG  . PHE A 1 93  ? -14.552 0.256   9.957   1.00 8.41  ? 93  PHE A CG  1 
ATOM   770  C  CD1 . PHE A 1 93  ? -14.173 -0.928  9.312   1.00 8.62  ? 93  PHE A CD1 1 
ATOM   771  C  CD2 . PHE A 1 93  ? -15.677 0.988   9.483   1.00 9.93  ? 93  PHE A CD2 1 
ATOM   772  C  CE1 . PHE A 1 93  ? -14.834 -1.394  8.136   1.00 13.64 ? 93  PHE A CE1 1 
ATOM   773  C  CE2 . PHE A 1 93  ? -16.370 0.491   8.344   1.00 11.55 ? 93  PHE A CE2 1 
ATOM   774  C  CZ  . PHE A 1 93  ? -15.964 -0.666  7.711   1.00 11.45 ? 93  PHE A CZ  1 
ATOM   775  N  N   . HIS A 1 94  ? -11.044 -0.506  10.824  1.00 7.72  ? 94  HIS A N   1 
ATOM   776  C  CA  . HIS A 1 94  ? -10.140 -1.435  10.219  1.00 7.07  ? 94  HIS A CA  1 
ATOM   777  C  C   . HIS A 1 94  ? -10.240 -2.737  11.062  1.00 7.27  ? 94  HIS A C   1 
ATOM   778  O  O   . HIS A 1 94  ? -10.927 -2.779  12.101  1.00 5.98  ? 94  HIS A O   1 
ATOM   779  C  CB  . HIS A 1 94  ? -8.677  -0.950  10.170  1.00 8.10  ? 94  HIS A CB  1 
ATOM   780  C  CG  . HIS A 1 94  ? -8.145  -0.680  11.542  1.00 8.57  ? 94  HIS A CG  1 
ATOM   781  N  ND1 . HIS A 1 94  ? -8.307  0.553   12.159  1.00 10.34 ? 94  HIS A ND1 1 
ATOM   782  C  CD2 . HIS A 1 94  ? -7.613  -1.500  12.456  1.00 6.64  ? 94  HIS A CD2 1 
ATOM   783  C  CE1 . HIS A 1 94  ? -7.825  0.468   13.403  1.00 8.29  ? 94  HIS A CE1 1 
ATOM   784  N  NE2 . HIS A 1 94  ? -7.371  -0.766  13.601  1.00 6.82  ? 94  HIS A NE2 1 
ATOM   785  N  N   . PHE A 1 95  ? -9.542  -3.760  10.593  1.00 6.94  ? 95  PHE A N   1 
ATOM   786  C  CA  . PHE A 1 95  ? -9.518  -5.080  11.265  1.00 6.90  ? 95  PHE A CA  1 
ATOM   787  C  C   . PHE A 1 95  ? -8.035  -5.515  11.454  1.00 5.64  ? 95  PHE A C   1 
ATOM   788  O  O   . PHE A 1 95  ? -7.109  -5.040  10.771  1.00 8.11  ? 95  PHE A O   1 
ATOM   789  C  CB  . PHE A 1 95  ? -10.223 -6.184  10.379  1.00 6.69  ? 95  PHE A CB  1 
ATOM   790  C  CG  . PHE A 1 95  ? -11.677 -5.900  10.085  1.00 7.36  ? 95  PHE A CG  1 
ATOM   791  C  CD1 . PHE A 1 95  ? -11.984 -5.027  9.037   1.00 9.05  ? 95  PHE A CD1 1 
ATOM   792  C  CD2 . PHE A 1 95  ? -12.730 -6.520  10.800  1.00 9.31  ? 95  PHE A CD2 1 
ATOM   793  C  CE1 . PHE A 1 95  ? -13.318 -4.776  8.699   1.00 7.33  ? 95  PHE A CE1 1 
ATOM   794  C  CE2 . PHE A 1 95  ? -14.066 -6.277  10.465  1.00 8.44  ? 95  PHE A CE2 1 
ATOM   795  C  CZ  . PHE A 1 95  ? -14.335 -5.385  9.372   1.00 7.91  ? 95  PHE A CZ  1 
ATOM   796  N  N   . HIS A 1 96  ? -7.886  -6.492  12.354  1.00 6.16  ? 96  HIS A N   1 
ATOM   797  C  CA  . HIS A 1 96  ? -6.704  -7.291  12.571  1.00 5.79  ? 96  HIS A CA  1 
ATOM   798  C  C   . HIS A 1 96  ? -7.077  -8.749  12.456  1.00 6.10  ? 96  HIS A C   1 
ATOM   799  O  O   . HIS A 1 96  ? -8.155  -9.108  12.975  1.00 6.80  ? 96  HIS A O   1 
ATOM   800  C  CB  . HIS A 1 96  ? -6.077  -7.044  13.982  1.00 7.89  ? 96  HIS A CB  1 
ATOM   801  C  CG  . HIS A 1 96  ? -5.779  -5.598  14.255  1.00 8.39  ? 96  HIS A CG  1 
ATOM   802  N  ND1 . HIS A 1 96  ? -4.517  -5.050  14.087  1.00 8.26  ? 96  HIS A ND1 1 
ATOM   803  C  CD2 . HIS A 1 96  ? -6.604  -4.571  14.607  1.00 9.20  ? 96  HIS A CD2 1 
ATOM   804  C  CE1 . HIS A 1 96  ? -4.562  -3.764  14.452  1.00 7.58  ? 96  HIS A CE1 1 
ATOM   805  N  NE2 . HIS A 1 96  ? -5.828  -3.440  14.693  1.00 8.56  ? 96  HIS A NE2 1 
ATOM   806  N  N   . TRP A 1 97  ? -6.286  -9.557  11.729  1.00 4.98  ? 97  TRP A N   1 
ATOM   807  C  CA  . TRP A 1 97  ? -6.706  -10.983 11.587  1.00 8.31  ? 97  TRP A CA  1 
ATOM   808  C  C   . TRP A 1 97  ? -5.554  -11.914 11.447  1.00 6.14  ? 97  TRP A C   1 
ATOM   809  O  O   . TRP A 1 97  ? -4.367  -11.435 11.317  1.00 8.04  ? 97  TRP A O   1 
ATOM   810  C  CB  . TRP A 1 97  ? -7.626  -11.157 10.371  1.00 8.24  ? 97  TRP A CB  1 
ATOM   811  C  CG  . TRP A 1 97  ? -6.986  -10.746 9.059   1.00 7.77  ? 97  TRP A CG  1 
ATOM   812  C  CD1 . TRP A 1 97  ? -6.315  -11.544 8.195   1.00 8.63  ? 97  TRP A CD1 1 
ATOM   813  C  CD2 . TRP A 1 97  ? -6.929  -9.408  8.510   1.00 9.95  ? 97  TRP A CD2 1 
ATOM   814  N  NE1 . TRP A 1 97  ? -5.921  -10.815 7.058   1.00 11.18 ? 97  TRP A NE1 1 
ATOM   815  C  CE2 . TRP A 1 97  ? -6.241  -9.497  7.259   1.00 10.66 ? 97  TRP A CE2 1 
ATOM   816  C  CE3 . TRP A 1 97  ? -7.438  -8.149  8.931   1.00 8.31  ? 97  TRP A CE3 1 
ATOM   817  C  CZ2 . TRP A 1 97  ? -6.056  -8.403  6.430   1.00 10.05 ? 97  TRP A CZ2 1 
ATOM   818  C  CZ3 . TRP A 1 97  ? -7.182  -6.988  8.088   1.00 7.93  ? 97  TRP A CZ3 1 
ATOM   819  C  CH2 . TRP A 1 97  ? -6.496  -7.140  6.878   1.00 8.16  ? 97  TRP A CH2 1 
ATOM   820  N  N   . GLY A 1 98  ? -5.882  -13.207 11.491  1.00 6.17  ? 98  GLY A N   1 
ATOM   821  C  CA  . GLY A 1 98  ? -4.797  -14.209 11.478  1.00 5.84  ? 98  GLY A CA  1 
ATOM   822  C  C   . GLY A 1 98  ? -4.612  -14.942 10.142  1.00 6.95  ? 98  GLY A C   1 
ATOM   823  O  O   . GLY A 1 98  ? -5.298  -14.722 9.148   1.00 8.81  ? 98  GLY A O   1 
ATOM   824  N  N   . SER A 1 99  ? -3.588  -15.780 10.162  1.00 7.84  ? 99  SER A N   1 
ATOM   825  C  CA  . SER A 1 99  ? -3.325  -16.684 9.037   1.00 11.31 ? 99  SER A CA  1 
ATOM   826  C  C   . SER A 1 99  ? -4.183  -17.934 9.155   1.00 11.73 ? 99  SER A C   1 
ATOM   827  O  O   . SER A 1 99  ? -4.270  -18.677 8.171   1.00 13.33 ? 99  SER A O   1 
ATOM   828  C  CB  . SER A 1 99  ? -1.828  -17.113 9.075   1.00 9.13  ? 99  SER A CB  1 
ATOM   829  O  OG  . SER A 1 99  ? -1.422  -17.663 10.318  1.00 12.68 ? 99  SER A OG  1 
ATOM   830  N  N   . LEU A 1 100 ? -4.840  -18.134 10.303  1.00 11.54 ? 100 LEU A N   1 
ATOM   831  C  CA  . LEU A 1 100 ? -5.623  -19.346 10.621  1.00 14.18 ? 100 LEU A CA  1 
ATOM   832  C  C   . LEU A 1 100 ? -6.759  -18.838 11.488  1.00 12.39 ? 100 LEU A C   1 
ATOM   833  O  O   . LEU A 1 100 ? -6.597  -17.824 12.188  1.00 12.96 ? 100 LEU A O   1 
ATOM   834  C  CB  . LEU A 1 100 ? -4.847  -20.326 11.547  1.00 16.45 ? 100 LEU A CB  1 
ATOM   835  C  CG  . LEU A 1 100 ? -3.503  -20.683 10.957  1.00 20.45 ? 100 LEU A CG  1 
ATOM   836  C  CD1 . LEU A 1 100 ? -2.554  -20.929 12.054  1.00 26.35 ? 100 LEU A CD1 1 
ATOM   837  C  CD2 . LEU A 1 100 ? -3.723  -21.894 10.048  1.00 25.72 ? 100 LEU A CD2 1 
ATOM   838  N  N   . ASP A 1 101 ? -7.880  -19.591 11.543  1.00 10.93 ? 101 ASP A N   1 
ATOM   839  C  CA  . ASP A 1 101 ? -9.047  -19.071 12.343  1.00 9.14  ? 101 ASP A CA  1 
ATOM   840  C  C   . ASP A 1 101 ? -8.789  -19.051 13.828  1.00 9.81  ? 101 ASP A C   1 
ATOM   841  O  O   . ASP A 1 101 ? -9.437  -18.311 14.586  1.00 12.18 ? 101 ASP A O   1 
ATOM   842  C  CB  . ASP A 1 101 ? -10.314 -19.918 12.070  1.00 9.04  ? 101 ASP A CB  1 
ATOM   843  C  CG  . ASP A 1 101 ? -10.742 -19.925 10.611  1.00 16.40 ? 101 ASP A CG  1 
ATOM   844  O  OD1 . ASP A 1 101 ? -10.356 -19.108 9.716   1.00 14.48 ? 101 ASP A OD1 1 
ATOM   845  O  OD2 . ASP A 1 101 ? -11.514 -20.859 10.331  1.00 20.67 ? 101 ASP A OD2 1 
ATOM   846  N  N   . GLY A 1 102 ? -7.752  -19.838 14.272  1.00 11.40 ? 102 GLY A N   1 
ATOM   847  C  CA  . GLY A 1 102 ? -7.389  -19.851 15.703  1.00 10.17 ? 102 GLY A CA  1 
ATOM   848  C  C   . GLY A 1 102 ? -6.668  -18.650 16.302  1.00 8.97  ? 102 GLY A C   1 
ATOM   849  O  O   . GLY A 1 102 ? -6.333  -18.636 17.492  1.00 10.36 ? 102 GLY A O   1 
ATOM   850  N  N   . GLN A 1 103 ? -6.361  -17.657 15.473  1.00 9.33  ? 103 GLN A N   1 
ATOM   851  C  CA  . GLN A 1 103 ? -5.714  -16.452 16.026  1.00 9.28  ? 103 GLN A CA  1 
ATOM   852  C  C   . GLN A 1 103 ? -6.074  -15.279 15.114  1.00 8.67  ? 103 GLN A C   1 
ATOM   853  O  O   . GLN A 1 103 ? -6.584  -15.480 14.017  1.00 8.76  ? 103 GLN A O   1 
ATOM   854  C  CB  . GLN A 1 103 ? -4.196  -16.653 16.047  1.00 9.28  ? 103 GLN A CB  1 
ATOM   855  C  CG  . GLN A 1 103 ? -3.587  -16.815 14.583  1.00 10.64 ? 103 GLN A CG  1 
ATOM   856  C  CD  . GLN A 1 103 ? -2.224  -17.419 14.645  1.00 14.21 ? 103 GLN A CD  1 
ATOM   857  O  OE1 . GLN A 1 103 ? -2.020  -18.368 15.406  1.00 20.13 ? 103 GLN A OE1 1 
ATOM   858  N  NE2 . GLN A 1 103 ? -1.302  -16.943 13.849  1.00 11.68 ? 103 GLN A NE2 1 
ATOM   859  N  N   . GLY A 1 104 ? -5.730  -14.076 15.584  1.00 7.97  ? 104 GLY A N   1 
ATOM   860  C  CA  . GLY A 1 104 ? -6.052  -12.879 14.763  1.00 6.96  ? 104 GLY A CA  1 
ATOM   861  C  C   . GLY A 1 104 ? -6.507  -11.711 15.629  1.00 6.22  ? 104 GLY A C   1 
ATOM   862  O  O   . GLY A 1 104 ? -6.199  -10.529 15.282  1.00 7.91  ? 104 GLY A O   1 
ATOM   863  N  N   . SER A 1 105 ? -7.215  -11.982 16.747  1.00 6.55  ? 105 SER A N   1 
ATOM   864  C  CA  . SER A 1 105 ? -7.622  -10.803 17.583  1.00 6.55  ? 105 SER A CA  1 
ATOM   865  C  C   . SER A 1 105 ? -6.387  -10.271 18.345  1.00 6.56  ? 105 SER A C   1 
ATOM   866  O  O   . SER A 1 105 ? -5.321  -11.000 18.559  1.00 6.54  ? 105 SER A O   1 
ATOM   867  C  CB  . SER A 1 105 ? -8.745  -11.174 18.576  1.00 5.45  ? 105 SER A CB  1 
ATOM   868  O  OG  . SER A 1 105 ? -8.298  -12.147 19.493  1.00 7.26  ? 105 SER A OG  1 
ATOM   869  N  N   . GLU A 1 106 ? -6.496  -9.010  18.729  1.00 6.12  ? 106 GLU A N   1 
ATOM   870  C  CA  . GLU A 1 106 ? -5.424  -8.315  19.532  1.00 5.79  ? 106 GLU A CA  1 
ATOM   871  C  C   . GLU A 1 106 ? -5.830  -8.515  21.036  1.00 6.66  ? 106 GLU A C   1 
ATOM   872  O  O   . GLU A 1 106 ? -5.117  -9.162  21.817  1.00 7.44  ? 106 GLU A O   1 
ATOM   873  C  CB  . GLU A 1 106 ? -5.428  -6.830  19.142  1.00 4.96  ? 106 GLU A CB  1 
ATOM   874  C  CG  . GLU A 1 106 ? -4.878  -6.756  17.686  1.00 8.63  ? 106 GLU A CG  1 
ATOM   875  C  CD  . GLU A 1 106 ? -4.330  -5.400  17.309  1.00 8.14  ? 106 GLU A CD  1 
ATOM   876  O  OE1 . GLU A 1 106 ? -5.002  -4.372  17.614  1.00 6.76  ? 106 GLU A OE1 1 
ATOM   877  O  OE2 . GLU A 1 106 ? -3.142  -5.413  16.907  1.00 10.33 ? 106 GLU A OE2 1 
ATOM   878  N  N   . HIS A 1 107 ? -7.038  -8.067  21.431  1.00 7.12  ? 107 HIS A N   1 
ATOM   879  C  CA  . HIS A 1 107 ? -7.452  -8.436  22.777  1.00 5.26  ? 107 HIS A CA  1 
ATOM   880  C  C   . HIS A 1 107 ? -7.785  -9.903  22.809  1.00 6.93  ? 107 HIS A C   1 
ATOM   881  O  O   . HIS A 1 107 ? -8.145  -10.493 21.759  1.00 6.66  ? 107 HIS A O   1 
ATOM   882  C  CB  . HIS A 1 107 ? -8.701  -7.648  23.180  1.00 5.31  ? 107 HIS A CB  1 
ATOM   883  C  CG  . HIS A 1 107 ? -8.412  -6.197  23.344  1.00 6.70  ? 107 HIS A CG  1 
ATOM   884  N  ND1 . HIS A 1 107 ? -8.473  -5.308  22.272  1.00 6.29  ? 107 HIS A ND1 1 
ATOM   885  C  CD2 . HIS A 1 107 ? -7.932  -5.499  24.408  1.00 8.60  ? 107 HIS A CD2 1 
ATOM   886  C  CE1 . HIS A 1 107 ? -8.081  -4.108  22.696  1.00 7.53  ? 107 HIS A CE1 1 
ATOM   887  N  NE2 . HIS A 1 107 ? -7.720  -4.207  23.972  1.00 7.00  ? 107 HIS A NE2 1 
ATOM   888  N  N   . THR A 1 108 ? -7.654  -10.485 24.005  1.00 7.49  ? 108 THR A N   1 
ATOM   889  C  CA  . THR A 1 108 ? -8.050  -11.879 24.229  1.00 4.74  ? 108 THR A CA  1 
ATOM   890  C  C   . THR A 1 108 ? -9.031  -11.906 25.413  1.00 8.01  ? 108 THR A C   1 
ATOM   891  O  O   . THR A 1 108 ? -9.082  -10.974 26.206  1.00 8.49  ? 108 THR A O   1 
ATOM   892  C  CB  . THR A 1 108 ? -6.836  -12.769 24.455  1.00 5.85  ? 108 THR A CB  1 
ATOM   893  O  OG1 . THR A 1 108 ? -6.064  -12.288 25.570  1.00 9.09  ? 108 THR A OG1 1 
ATOM   894  C  CG2 . THR A 1 108 ? -5.922  -12.841 23.155  1.00 5.89  ? 108 THR A CG2 1 
ATOM   895  N  N   . VAL A 1 109 ? -9.821  -12.975 25.503  1.00 8.03  ? 109 VAL A N   1 
ATOM   896  C  CA  . VAL A 1 109 ? -10.808 -13.033 26.643  1.00 8.31  ? 109 VAL A CA  1 
ATOM   897  C  C   . VAL A 1 109 ? -10.492 -14.343 27.424  1.00 9.24  ? 109 VAL A C   1 
ATOM   898  O  O   . VAL A 1 109 ? -10.592 -15.425 26.826  1.00 8.19  ? 109 VAL A O   1 
ATOM   899  C  CB  . VAL A 1 109 ? -12.201 -13.102 26.100  1.00 10.59 ? 109 VAL A CB  1 
ATOM   900  C  CG1 . VAL A 1 109 ? -13.259 -13.222 27.281  1.00 9.69  ? 109 VAL A CG1 1 
ATOM   901  C  CG2 . VAL A 1 109 ? -12.540 -11.807 25.258  1.00 10.05 ? 109 VAL A CG2 1 
ATOM   902  N  N   . ASP A 1 110 ? -10.021 -14.215 28.643  1.00 9.10  ? 110 ASP A N   1 
ATOM   903  C  CA  . ASP A 1 110 ? -9.487  -15.413 29.392  1.00 11.55 ? 110 ASP A CA  1 
ATOM   904  C  C   . ASP A 1 110 ? -8.570  -16.248 28.485  1.00 9.76  ? 110 ASP A C   1 
ATOM   905  O  O   . ASP A 1 110 ? -8.688  -17.535 28.446  1.00 11.52 ? 110 ASP A O   1 
ATOM   906  C  CB  . ASP A 1 110 ? -10.689 -16.248 29.863  1.00 12.68 ? 110 ASP A CB  1 
ATOM   907  C  CG  . ASP A 1 110 ? -11.611 -15.441 30.833  1.00 11.57 ? 110 ASP A CG  1 
ATOM   908  O  OD1 . ASP A 1 110 ? -11.033 -14.628 31.529  1.00 13.37 ? 110 ASP A OD1 1 
ATOM   909  O  OD2 . ASP A 1 110 ? -12.804 -15.699 30.852  1.00 17.99 ? 110 ASP A OD2 1 
ATOM   910  N  N   . LYS A 1 111 ? -7.657  -15.529 27.794  1.00 8.86  ? 111 LYS A N   1 
ATOM   911  C  CA  . LYS A 1 111 ? -6.598  -16.057 26.895  1.00 9.75  ? 111 LYS A CA  1 
ATOM   912  C  C   . LYS A 1 111 ? -7.129  -16.589 25.560  1.00 9.16  ? 111 LYS A C   1 
ATOM   913  O  O   . LYS A 1 111 ? -6.369  -17.017 24.718  1.00 8.78  ? 111 LYS A O   1 
ATOM   914  C  CB  . LYS A 1 111 ? -5.690  -17.100 27.625  1.00 12.78 ? 111 LYS A CB  1 
ATOM   915  C  CG  . LYS A 1 111 ? -5.034  -16.519 28.910  1.00 14.26 ? 111 LYS A CG  1 
ATOM   916  C  CD  . LYS A 1 111 ? -4.123  -15.355 28.526  1.00 21.71 ? 111 LYS A CD  1 
ATOM   917  C  CE  . LYS A 1 111 ? -3.253  -14.783 29.731  1.00 18.17 ? 111 LYS A CE  1 
ATOM   918  N  NZ  . LYS A 1 111 ? -2.016  -15.507 29.493  1.00 21.96 ? 111 LYS A NZ  1 
ATOM   919  N  N   . LYS A 1 112 ? -8.455  -16.514 25.343  1.00 8.00  ? 112 LYS A N   1 
ATOM   920  C  CA  . LYS A 1 112 ? -9.045  -16.990 24.079  1.00 9.26  ? 112 LYS A CA  1 
ATOM   921  C  C   . LYS A 1 112 ? -8.720  -15.920 22.983  1.00 10.22 ? 112 LYS A C   1 
ATOM   922  O  O   . LYS A 1 112 ? -9.019  -14.701 23.164  1.00 10.04 ? 112 LYS A O   1 
ATOM   923  C  CB  . LYS A 1 112 ? -10.600 -17.093 24.202  1.00 10.16 ? 112 LYS A CB  1 
ATOM   924  C  CG  . LYS A 1 112 ? -11.259 -17.377 22.803  1.00 11.36 ? 112 LYS A CG  1 
ATOM   925  C  CD  . LYS A 1 112 ? -12.757 -17.432 23.028  1.00 14.64 ? 112 LYS A CD  1 
ATOM   926  C  CE  . LYS A 1 112 ? -13.384 -17.431 21.642  1.00 19.20 ? 112 LYS A CE  1 
ATOM   927  N  NZ  . LYS A 1 112 ? -13.176 -18.694 20.910  1.00 19.49 ? 112 LYS A NZ  1 
ATOM   928  N  N   A LYS A 1 113 ? -8.129  -16.364 21.880  0.50 8.95  ? 113 LYS A N   1 
ATOM   929  N  N   B LYS A 1 113 ? -8.214  -16.411 21.851  0.50 9.18  ? 113 LYS A N   1 
ATOM   930  C  CA  A LYS A 1 113 ? -8.004  -15.532 20.687  0.50 8.44  ? 113 LYS A CA  1 
ATOM   931  C  CA  B LYS A 1 113 ? -7.957  -15.623 20.639  0.50 8.89  ? 113 LYS A CA  1 
ATOM   932  C  C   A LYS A 1 113 ? -9.207  -15.776 19.772  0.50 8.02  ? 113 LYS A C   1 
ATOM   933  C  C   B LYS A 1 113 ? -9.077  -15.804 19.582  0.50 7.86  ? 113 LYS A C   1 
ATOM   934  O  O   A LYS A 1 113 ? -9.699  -16.911 19.635  0.50 7.08  ? 113 LYS A O   1 
ATOM   935  O  O   B LYS A 1 113 ? -9.395  -16.934 19.156  0.50 7.05  ? 113 LYS A O   1 
ATOM   936  C  CB  A LYS A 1 113 ? -6.709  -15.866 19.937  0.50 8.25  ? 113 LYS A CB  1 
ATOM   937  C  CB  B LYS A 1 113 ? -6.604  -16.055 20.049  0.50 8.48  ? 113 LYS A CB  1 
ATOM   938  C  CG  A LYS A 1 113 ? -5.456  -15.448 20.664  0.50 7.37  ? 113 LYS A CG  1 
ATOM   939  C  CG  B LYS A 1 113 ? -5.431  -15.719 20.943  0.50 10.11 ? 113 LYS A CG  1 
ATOM   940  C  CD  A LYS A 1 113 ? -4.283  -16.037 19.899  0.50 5.35  ? 113 LYS A CD  1 
ATOM   941  C  CD  B LYS A 1 113 ? -4.176  -16.445 20.459  0.50 12.18 ? 113 LYS A CD  1 
ATOM   942  C  CE  A LYS A 1 113 ? -2.956  -15.638 20.547  0.50 7.28  ? 113 LYS A CE  1 
ATOM   943  C  CE  B LYS A 1 113 ? -2.944  -15.835 21.155  0.50 16.11 ? 113 LYS A CE  1 
ATOM   944  N  NZ  A LYS A 1 113 ? -2.628  -16.465 21.794  0.50 8.31  ? 113 LYS A NZ  1 
ATOM   945  N  NZ  B LYS A 1 113 ? -1.652  -16.236 20.539  0.50 16.43 ? 113 LYS A NZ  1 
ATOM   946  N  N   . TYR A 1 114 ? -9.695  -14.699 19.177  1.00 7.94  ? 114 TYR A N   1 
ATOM   947  C  CA  . TYR A 1 114 ? -10.687 -14.789 18.147  1.00 6.98  ? 114 TYR A CA  1 
ATOM   948  C  C   . TYR A 1 114 ? -10.054 -14.734 16.748  1.00 6.68  ? 114 TYR A C   1 
ATOM   949  O  O   . TYR A 1 114 ? -8.874  -14.407 16.626  1.00 8.21  ? 114 TYR A O   1 
ATOM   950  C  CB  . TYR A 1 114 ? -11.758 -13.648 18.278  1.00 6.24  ? 114 TYR A CB  1 
ATOM   951  C  CG  . TYR A 1 114 ? -12.784 -13.869 19.429  1.00 6.48  ? 114 TYR A CG  1 
ATOM   952  C  CD1 . TYR A 1 114 ? -12.480 -13.485 20.721  1.00 11.31 ? 114 TYR A CD1 1 
ATOM   953  C  CD2 . TYR A 1 114 ? -13.965 -14.556 19.181  1.00 9.58  ? 114 TYR A CD2 1 
ATOM   954  C  CE1 . TYR A 1 114 ? -13.371 -13.728 21.764  1.00 12.86 ? 114 TYR A CE1 1 
ATOM   955  C  CE2 . TYR A 1 114 ? -14.908 -14.708 20.172  1.00 11.74 ? 114 TYR A CE2 1 
ATOM   956  C  CZ  . TYR A 1 114 ? -14.579 -14.325 21.468  1.00 12.39 ? 114 TYR A CZ  1 
ATOM   957  O  OH  . TYR A 1 114 ? -15.463 -14.550 22.526  1.00 14.92 ? 114 TYR A OH  1 
ATOM   958  N  N   . ALA A 1 115 ? -10.835 -15.046 15.676  1.00 6.85  ? 115 ALA A N   1 
ATOM   959  C  CA  . ALA A 1 115 ? -10.301 -15.050 14.284  1.00 8.72  ? 115 ALA A CA  1 
ATOM   960  C  C   . ALA A 1 115 ? -9.818  -13.655 13.780  1.00 8.01  ? 115 ALA A C   1 
ATOM   961  O  O   . ALA A 1 115 ? -9.002  -13.512 12.824  1.00 8.77  ? 115 ALA A O   1 
ATOM   962  C  CB  . ALA A 1 115 ? -11.392 -15.613 13.320  1.00 8.69  ? 115 ALA A CB  1 
ATOM   963  N  N   . ALA A 1 116 ? -10.507 -12.653 14.349  1.00 6.36  ? 116 ALA A N   1 
ATOM   964  C  CA  . ALA A 1 116 ? -10.217 -11.253 13.924  1.00 4.64  ? 116 ALA A CA  1 
ATOM   965  C  C   . ALA A 1 116 ? -10.790 -10.281 14.933  1.00 5.32  ? 116 ALA A C   1 
ATOM   966  O  O   . ALA A 1 116 ? -11.523 -10.667 15.876  1.00 5.73  ? 116 ALA A O   1 
ATOM   967  C  CB  . ALA A 1 116 ? -10.687 -10.972 12.498  1.00 6.66  ? 116 ALA A CB  1 
ATOM   968  N  N   . GLU A 1 117 ? -10.411 -9.013  14.776  1.00 6.46  ? 117 GLU A N   1 
ATOM   969  C  CA  . GLU A 1 117 ? -10.993 -7.998  15.668  1.00 6.28  ? 117 GLU A CA  1 
ATOM   970  C  C   . GLU A 1 117 ? -11.159 -6.701  14.863  1.00 8.04  ? 117 GLU A C   1 
ATOM   971  O  O   . GLU A 1 117 ? -10.277 -6.339  14.142  1.00 8.16  ? 117 GLU A O   1 
ATOM   972  C  CB  . GLU A 1 117 ? -10.016 -7.786  16.843  1.00 6.82  ? 117 GLU A CB  1 
ATOM   973  C  CG  . GLU A 1 117 ? -10.526 -6.709  17.900  1.00 3.54  ? 117 GLU A CG  1 
ATOM   974  C  CD  . GLU A 1 117 ? -9.601  -6.700  19.117  1.00 7.58  ? 117 GLU A CD  1 
ATOM   975  O  OE1 . GLU A 1 117 ? -8.916  -7.736  19.395  1.00 8.70  ? 117 GLU A OE1 1 
ATOM   976  O  OE2 . GLU A 1 117 ? -9.574  -5.640  19.813  1.00 8.75  ? 117 GLU A OE2 1 
ATOM   977  N  N   . LEU A 1 118 ? -12.341 -6.127  14.958  1.00 6.75  ? 118 LEU A N   1 
ATOM   978  C  CA  . LEU A 1 118 ? -12.720 -4.880  14.327  1.00 6.62  ? 118 LEU A CA  1 
ATOM   979  C  C   . LEU A 1 118 ? -12.511 -3.702  15.304  1.00 5.66  ? 118 LEU A C   1 
ATOM   980  O  O   . LEU A 1 118 ? -12.886 -3.779  16.444  1.00 5.75  ? 118 LEU A O   1 
ATOM   981  C  CB  . LEU A 1 118 ? -14.215 -4.981  13.920  1.00 5.65  ? 118 LEU A CB  1 
ATOM   982  C  CG  . LEU A 1 118 ? -15.001 -3.687  13.588  1.00 7.44  ? 118 LEU A CG  1 
ATOM   983  C  CD1 . LEU A 1 118 ? -14.458 -3.164  12.326  1.00 7.49  ? 118 LEU A CD1 1 
ATOM   984  C  CD2 . LEU A 1 118 ? -16.500 -4.047  13.326  1.00 7.77  ? 118 LEU A CD2 1 
ATOM   985  N  N   . HIS A 1 119 ? -11.881 -2.635  14.795  1.00 5.39  ? 119 HIS A N   1 
ATOM   986  C  CA  . HIS A 1 119 ? -11.610 -1.434  15.547  1.00 5.31  ? 119 HIS A CA  1 
ATOM   987  C  C   . HIS A 1 119 ? -12.306 -0.247  14.883  1.00 5.97  ? 119 HIS A C   1 
ATOM   988  O  O   . HIS A 1 119 ? -11.953 0.044   13.734  1.00 7.91  ? 119 HIS A O   1 
ATOM   989  C  CB  . HIS A 1 119 ? -10.093 -1.196  15.614  1.00 5.09  ? 119 HIS A CB  1 
ATOM   990  C  CG  . HIS A 1 119 ? -9.445  -2.169  16.569  1.00 4.07  ? 119 HIS A CG  1 
ATOM   991  N  ND1 . HIS A 1 119 ? -8.092  -2.483  16.554  1.00 8.26  ? 119 HIS A ND1 1 
ATOM   992  C  CD2 . HIS A 1 119 ? -10.010 -2.931  17.533  1.00 4.79  ? 119 HIS A CD2 1 
ATOM   993  C  CE1 . HIS A 1 119 ? -7.844  -3.379  17.498  1.00 7.62  ? 119 HIS A CE1 1 
ATOM   994  N  NE2 . HIS A 1 119 ? -9.005  -3.697  18.083  1.00 5.21  ? 119 HIS A NE2 1 
ATOM   995  N  N   . LEU A 1 120 ? -13.329 0.326   15.543  1.00 5.59  ? 120 LEU A N   1 
ATOM   996  C  CA  . LEU A 1 120 ? -13.992 1.576   15.054  1.00 5.76  ? 120 LEU A CA  1 
ATOM   997  C  C   . LEU A 1 120 ? -13.367 2.705   15.851  1.00 7.09  ? 120 LEU A C   1 
ATOM   998  O  O   . LEU A 1 120 ? -13.484 2.741   17.080  1.00 6.08  ? 120 LEU A O   1 
ATOM   999  C  CB  . LEU A 1 120 ? -15.496 1.545   15.280  1.00 5.94  ? 120 LEU A CB  1 
ATOM   1000 C  CG  . LEU A 1 120 ? -16.118 0.376   14.443  1.00 8.49  ? 120 LEU A CG  1 
ATOM   1001 C  CD1 . LEU A 1 120 ? -16.928 -0.501  15.333  1.00 11.56 ? 120 LEU A CD1 1 
ATOM   1002 C  CD2 . LEU A 1 120 ? -16.957 0.988   13.310  1.00 9.63  ? 120 LEU A CD2 1 
ATOM   1003 N  N   . VAL A 1 121 ? -12.606 3.545   15.127  1.00 6.01  ? 121 VAL A N   1 
ATOM   1004 C  CA  . VAL A 1 121 ? -11.783 4.547   15.803  1.00 6.01  ? 121 VAL A CA  1 
ATOM   1005 C  C   . VAL A 1 121 ? -12.495 5.890   15.832  1.00 7.26  ? 121 VAL A C   1 
ATOM   1006 O  O   . VAL A 1 121 ? -12.882 6.385   14.755  1.00 6.50  ? 121 VAL A O   1 
ATOM   1007 C  CB  . VAL A 1 121 ? -10.442 4.694   15.003  1.00 6.45  ? 121 VAL A CB  1 
ATOM   1008 C  CG1 . VAL A 1 121 ? -9.449  5.668   15.699  1.00 6.97  ? 121 VAL A CG1 1 
ATOM   1009 C  CG2 . VAL A 1 121 ? -9.770  3.324   14.783  1.00 7.43  ? 121 VAL A CG2 1 
ATOM   1010 N  N   . HIS A 1 122 ? -12.576 6.507   17.037  1.00 5.46  ? 122 HIS A N   1 
ATOM   1011 C  CA  . HIS A 1 122 ? -13.286 7.743   17.186  1.00 5.94  ? 122 HIS A CA  1 
ATOM   1012 C  C   . HIS A 1 122 ? -12.399 8.730   17.915  1.00 6.64  ? 122 HIS A C   1 
ATOM   1013 O  O   . HIS A 1 122 ? -11.626 8.347   18.809  1.00 6.55  ? 122 HIS A O   1 
ATOM   1014 C  CB  . HIS A 1 122 ? -14.569 7.600   18.006  1.00 7.85  ? 122 HIS A CB  1 
ATOM   1015 C  CG  . HIS A 1 122 ? -15.455 6.454   17.611  1.00 7.08  ? 122 HIS A CG  1 
ATOM   1016 N  ND1 . HIS A 1 122 ? -15.138 5.138   17.894  1.00 6.71  ? 122 HIS A ND1 1 
ATOM   1017 C  CD2 . HIS A 1 122 ? -16.652 6.423   16.952  1.00 11.07 ? 122 HIS A CD2 1 
ATOM   1018 C  CE1 . HIS A 1 122 ? -16.118 4.345   17.443  1.00 10.62 ? 122 HIS A CE1 1 
ATOM   1019 N  NE2 . HIS A 1 122 ? -17.042 5.103   16.851  1.00 9.55  ? 122 HIS A NE2 1 
ATOM   1020 N  N   . TRP A 1 123 ? -12.531 10.010  17.582  1.00 6.69  ? 123 TRP A N   1 
ATOM   1021 C  CA  . TRP A 1 123 ? -11.708 11.050  18.306  1.00 6.09  ? 123 TRP A CA  1 
ATOM   1022 C  C   . TRP A 1 123 ? -12.561 12.062  19.034  1.00 8.57  ? 123 TRP A C   1 
ATOM   1023 O  O   . TRP A 1 123 ? -13.636 12.444  18.531  1.00 9.57  ? 123 TRP A O   1 
ATOM   1024 C  CB  . TRP A 1 123 ? -10.699 11.729  17.312  1.00 7.87  ? 123 TRP A CB  1 
ATOM   1025 C  CG  . TRP A 1 123 ? -11.364 12.367  16.132  1.00 10.34 ? 123 TRP A CG  1 
ATOM   1026 C  CD1 . TRP A 1 123 ? -11.593 11.777  14.879  1.00 10.70 ? 123 TRP A CD1 1 
ATOM   1027 C  CD2 . TRP A 1 123 ? -11.865 13.709  16.034  1.00 11.68 ? 123 TRP A CD2 1 
ATOM   1028 N  NE1 . TRP A 1 123 ? -12.284 12.645  14.055  1.00 12.04 ? 123 TRP A NE1 1 
ATOM   1029 C  CE2 . TRP A 1 123 ? -12.427 13.855  14.701  1.00 13.71 ? 123 TRP A CE2 1 
ATOM   1030 C  CE3 . TRP A 1 123 ? -11.906 14.803  16.914  1.00 10.26 ? 123 TRP A CE3 1 
ATOM   1031 C  CZ2 . TRP A 1 123 ? -12.976 15.046  14.244  1.00 15.14 ? 123 TRP A CZ2 1 
ATOM   1032 C  CZ3 . TRP A 1 123 ? -12.501 15.996  16.449  1.00 13.48 ? 123 TRP A CZ3 1 
ATOM   1033 C  CH2 . TRP A 1 123 ? -12.988 16.118  15.121  1.00 12.74 ? 123 TRP A CH2 1 
ATOM   1034 N  N   . ASN A 1 124 ? -12.041 12.496  20.178  1.00 8.64  ? 124 ASN A N   1 
ATOM   1035 C  CA  . ASN A 1 124 ? -12.750 13.410  21.071  1.00 8.57  ? 124 ASN A CA  1 
ATOM   1036 C  C   . ASN A 1 124 ? -12.947 14.801  20.403  1.00 8.84  ? 124 ASN A C   1 
ATOM   1037 O  O   . ASN A 1 124 ? -11.958 15.491  20.115  1.00 7.76  ? 124 ASN A O   1 
ATOM   1038 C  CB  . ASN A 1 124 ? -11.896 13.548  22.344  1.00 8.93  ? 124 ASN A CB  1 
ATOM   1039 C  CG  . ASN A 1 124 ? -12.701 14.099  23.532  1.00 9.50  ? 124 ASN A CG  1 
ATOM   1040 O  OD1 . ASN A 1 124 ? -13.581 14.950  23.337  1.00 11.96 ? 124 ASN A OD1 1 
ATOM   1041 N  ND2 . ASN A 1 124 ? -12.435 13.588  24.734  1.00 12.56 ? 124 ASN A ND2 1 
ATOM   1042 N  N   . THR A 1 125 ? -14.225 15.233  20.276  1.00 11.77 ? 125 THR A N   1 
ATOM   1043 C  CA  . THR A 1 125 ? -14.509 16.483  19.550  1.00 13.46 ? 125 THR A CA  1 
ATOM   1044 C  C   . THR A 1 125 ? -13.911 17.711  20.305  1.00 14.02 ? 125 THR A C   1 
ATOM   1045 O  O   . THR A 1 125 ? -13.711 18.748  19.709  1.00 14.86 ? 125 THR A O   1 
ATOM   1046 C  CB  . THR A 1 125 ? -16.020 16.656  19.285  1.00 14.01 ? 125 THR A CB  1 
ATOM   1047 O  OG1 . THR A 1 125 ? -16.730 16.576  20.512  1.00 17.18 ? 125 THR A OG1 1 
ATOM   1048 C  CG2 . THR A 1 125 ? -16.498 15.560  18.372  1.00 15.04 ? 125 THR A CG2 1 
ATOM   1049 N  N   . LYS A 1 126 ? -13.622 17.533  21.596  1.00 14.16 ? 127 LYS A N   1 
ATOM   1050 C  CA  . LYS A 1 126 ? -13.053 18.678  22.350  1.00 15.07 ? 127 LYS A CA  1 
ATOM   1051 C  C   . LYS A 1 126 ? -11.669 19.061  21.799  1.00 14.67 ? 127 LYS A C   1 
ATOM   1052 O  O   . LYS A 1 126 ? -11.167 20.183  22.076  1.00 16.84 ? 127 LYS A O   1 
ATOM   1053 C  CB  . LYS A 1 126 ? -13.105 18.430  23.850  1.00 16.06 ? 127 LYS A CB  1 
ATOM   1054 C  CG  . LYS A 1 126 ? -12.010 17.608  24.421  1.00 17.68 ? 127 LYS A CG  1 
ATOM   1055 C  CD  . LYS A 1 126 ? -12.260 17.381  25.969  1.00 17.52 ? 127 LYS A CD  1 
ATOM   1056 C  CE  . LYS A 1 126 ? -11.444 16.350  26.540  1.00 25.26 ? 127 LYS A CE  1 
ATOM   1057 N  NZ  . LYS A 1 126 ? -11.002 16.845  27.928  1.00 28.81 ? 127 LYS A NZ  1 
ATOM   1058 N  N   . TYR A 1 127 ? -11.022 18.131  21.061  1.00 10.46 ? 128 TYR A N   1 
ATOM   1059 C  CA  . TYR A 1 127 ? -9.673  18.359  20.498  1.00 10.87 ? 128 TYR A CA  1 
ATOM   1060 C  C   . TYR A 1 127 ? -9.600  18.823  19.034  1.00 10.84 ? 128 TYR A C   1 
ATOM   1061 O  O   . TYR A 1 127 ? -8.469  19.029  18.472  1.00 11.13 ? 128 TYR A O   1 
ATOM   1062 C  CB  . TYR A 1 127 ? -8.668  17.216  20.774  1.00 11.41 ? 128 TYR A CB  1 
ATOM   1063 C  CG  . TYR A 1 127 ? -8.578  16.940  22.252  1.00 8.71  ? 128 TYR A CG  1 
ATOM   1064 C  CD1 . TYR A 1 127 ? -8.197  17.961  23.145  1.00 14.93 ? 128 TYR A CD1 1 
ATOM   1065 C  CD2 . TYR A 1 127 ? -8.794  15.669  22.742  1.00 9.39  ? 128 TYR A CD2 1 
ATOM   1066 C  CE1 . TYR A 1 127 ? -8.093  17.700  24.502  1.00 8.62  ? 128 TYR A CE1 1 
ATOM   1067 C  CE2 . TYR A 1 127 ? -8.743  15.377  24.078  1.00 11.83 ? 128 TYR A CE2 1 
ATOM   1068 C  CZ  . TYR A 1 127 ? -8.369  16.441  24.973  1.00 12.65 ? 128 TYR A CZ  1 
ATOM   1069 O  OH  . TYR A 1 127 ? -8.341  16.130  26.307  1.00 13.24 ? 128 TYR A OH  1 
ATOM   1070 N  N   . GLY A 1 128 ? -10.795 18.935  18.438  1.00 11.89 ? 129 GLY A N   1 
ATOM   1071 C  CA  . GLY A 1 128 ? -10.962 19.584  17.114  1.00 13.46 ? 129 GLY A CA  1 
ATOM   1072 C  C   . GLY A 1 128 ? -10.561 18.683  15.922  1.00 14.27 ? 129 GLY A C   1 
ATOM   1073 O  O   . GLY A 1 128 ? -11.152 18.770  14.813  1.00 15.76 ? 129 GLY A O   1 
ATOM   1074 N  N   . ASP A 1 129 ? -9.559  17.803  16.101  1.00 12.57 ? 130 ASP A N   1 
ATOM   1075 C  CA  . ASP A 1 129 ? -9.322  16.838  15.059  1.00 14.44 ? 130 ASP A CA  1 
ATOM   1076 C  C   . ASP A 1 129 ? -8.517  15.646  15.543  1.00 15.33 ? 130 ASP A C   1 
ATOM   1077 O  O   . ASP A 1 129 ? -7.960  15.664  16.649  1.00 13.44 ? 130 ASP A O   1 
ATOM   1078 C  CB  . ASP A 1 129 ? -8.674  17.463  13.778  1.00 14.68 ? 130 ASP A CB  1 
ATOM   1079 C  CG  . ASP A 1 129 ? -7.242  17.983  13.965  1.00 17.48 ? 130 ASP A CG  1 
ATOM   1080 O  OD1 . ASP A 1 129 ? -6.511  17.715  14.923  1.00 22.46 ? 130 ASP A OD1 1 
ATOM   1081 O  OD2 . ASP A 1 129 ? -6.713  18.635  13.048  1.00 20.17 ? 130 ASP A OD2 1 
ATOM   1082 N  N   . PHE A 1 130 ? -8.375  14.674  14.635  1.00 13.70 ? 131 PHE A N   1 
ATOM   1083 C  CA  . PHE A 1 130 ? -7.664  13.445  14.963  1.00 14.21 ? 131 PHE A CA  1 
ATOM   1084 C  C   . PHE A 1 130 ? -6.231  13.698  15.345  1.00 11.93 ? 131 PHE A C   1 
ATOM   1085 O  O   . PHE A 1 130 ? -5.720  13.120  16.345  1.00 10.21 ? 131 PHE A O   1 
ATOM   1086 C  CB  . PHE A 1 130 ? -7.800  12.396  13.847  1.00 12.14 ? 131 PHE A CB  1 
ATOM   1087 C  CG  . PHE A 1 130 ? -7.111  11.113  14.126  1.00 12.01 ? 131 PHE A CG  1 
ATOM   1088 C  CD1 . PHE A 1 130 ? -7.767  10.065  14.890  1.00 7.04  ? 131 PHE A CD1 1 
ATOM   1089 C  CD2 . PHE A 1 130 ? -5.796  10.915  13.710  1.00 13.18 ? 131 PHE A CD2 1 
ATOM   1090 C  CE1 . PHE A 1 130 ? -7.111  8.889   15.146  1.00 11.75 ? 131 PHE A CE1 1 
ATOM   1091 C  CE2 . PHE A 1 130 ? -5.161  9.690   13.952  1.00 14.32 ? 131 PHE A CE2 1 
ATOM   1092 C  CZ  . PHE A 1 130 ? -5.838  8.708   14.705  1.00 13.91 ? 131 PHE A CZ  1 
ATOM   1093 N  N   . GLY A 1 131 ? -5.507  14.484  14.532  1.00 10.83 ? 132 GLY A N   1 
ATOM   1094 C  CA  . GLY A 1 131 ? -4.101  14.639  14.851  1.00 12.68 ? 132 GLY A CA  1 
ATOM   1095 C  C   . GLY A 1 131 ? -3.804  15.246  16.217  1.00 12.97 ? 132 GLY A C   1 
ATOM   1096 O  O   . GLY A 1 131 ? -2.777  14.933  16.838  1.00 12.91 ? 132 GLY A O   1 
ATOM   1097 N  N   . LYS A 1 132 ? -4.630  16.185  16.626  1.00 12.15 ? 133 LYS A N   1 
ATOM   1098 C  CA  . LYS A 1 132 ? -4.467  16.774  17.989  1.00 12.07 ? 133 LYS A CA  1 
ATOM   1099 C  C   . LYS A 1 132 ? -4.909  15.778  19.101  1.00 12.76 ? 133 LYS A C   1 
ATOM   1100 O  O   . LYS A 1 132 ? -4.336  15.694  20.178  1.00 11.59 ? 133 LYS A O   1 
ATOM   1101 C  CB  . LYS A 1 132 ? -5.268  18.048  18.113  1.00 14.59 ? 133 LYS A CB  1 
ATOM   1102 C  CG  . LYS A 1 132 ? -4.711  19.252  17.330  1.00 18.86 ? 133 LYS A CG  1 
ATOM   1103 C  CD  . LYS A 1 132 ? -3.225  19.088  17.026  1.00 27.00 ? 133 LYS A CD  1 
ATOM   1104 C  CE  . LYS A 1 132 ? -2.865  19.624  15.632  1.00 35.73 ? 133 LYS A CE  1 
ATOM   1105 N  NZ  . LYS A 1 132 ? -4.035  19.706  14.676  1.00 40.38 ? 133 LYS A NZ  1 
ATOM   1106 N  N   . ALA A 1 133 ? -6.028  15.122  18.830  1.00 11.73 ? 134 ALA A N   1 
ATOM   1107 C  CA  . ALA A 1 133 ? -6.581  14.137  19.770  1.00 11.26 ? 134 ALA A CA  1 
ATOM   1108 C  C   . ALA A 1 133 ? -5.594  13.055  20.186  1.00 8.97  ? 134 ALA A C   1 
ATOM   1109 O  O   . ALA A 1 133 ? -5.549  12.679  21.362  1.00 10.16 ? 134 ALA A O   1 
ATOM   1110 C  CB  . ALA A 1 133 ? -7.898  13.453  19.145  1.00 9.54  ? 134 ALA A CB  1 
ATOM   1111 N  N   . VAL A 1 134 ? -4.833  12.497  19.242  1.00 9.43  ? 135 VAL A N   1 
ATOM   1112 C  CA  . VAL A 1 134 ? -3.870  11.405  19.613  1.00 11.68 ? 135 VAL A CA  1 
ATOM   1113 C  C   . VAL A 1 134 ? -2.762  11.839  20.587  1.00 10.79 ? 135 VAL A C   1 
ATOM   1114 O  O   . VAL A 1 134 ? -2.107  11.016  21.171  1.00 11.87 ? 135 VAL A O   1 
ATOM   1115 C  CB  . VAL A 1 134 ? -3.295  10.642  18.350  1.00 11.75 ? 135 VAL A CB  1 
ATOM   1116 C  CG1 . VAL A 1 134 ? -4.433  10.120  17.519  1.00 13.08 ? 135 VAL A CG1 1 
ATOM   1117 C  CG2 . VAL A 1 134 ? -2.318  11.548  17.565  1.00 13.49 ? 135 VAL A CG2 1 
ATOM   1118 N  N   A GLN A 1 135 ? -2.610  13.162  20.766  0.50 10.55 ? 136 GLN A N   1 
ATOM   1119 N  N   B GLN A 1 135 ? -2.582  13.151  20.757  0.50 11.01 ? 136 GLN A N   1 
ATOM   1120 C  CA  A GLN A 1 135 ? -1.613  13.706  21.686  0.50 12.13 ? 136 GLN A CA  1 
ATOM   1121 C  CA  B GLN A 1 135 ? -1.553  13.611  21.667  0.50 12.91 ? 136 GLN A CA  1 
ATOM   1122 C  C   A GLN A 1 135 ? -2.211  13.960  23.064  0.50 12.47 ? 136 GLN A C   1 
ATOM   1123 C  C   B GLN A 1 135 ? -2.126  13.766  23.098  0.50 12.70 ? 136 GLN A C   1 
ATOM   1124 O  O   A GLN A 1 135 ? -1.614  14.685  23.927  0.50 11.98 ? 136 GLN A O   1 
ATOM   1125 O  O   B GLN A 1 135 ? -1.409  14.209  24.039  0.50 12.63 ? 136 GLN A O   1 
ATOM   1126 C  CB  A GLN A 1 135 ? -1.135  15.048  21.121  0.50 11.63 ? 136 GLN A CB  1 
ATOM   1127 C  CB  B GLN A 1 135 ? -0.955  14.928  21.091  0.50 13.04 ? 136 GLN A CB  1 
ATOM   1128 C  CG  A GLN A 1 135 ? -0.816  14.968  19.701  0.50 11.50 ? 136 GLN A CG  1 
ATOM   1129 C  CG  B GLN A 1 135 ? -0.200  14.720  19.758  0.50 16.35 ? 136 GLN A CG  1 
ATOM   1130 C  CD  A GLN A 1 135 ? -0.169  16.242  19.239  0.50 16.23 ? 136 GLN A CD  1 
ATOM   1131 C  CD  B GLN A 1 135 ? 1.027   13.783  19.878  0.50 19.23 ? 136 GLN A CD  1 
ATOM   1132 O  OE1 A GLN A 1 135 ? -0.409  16.666  18.137  0.50 16.70 ? 136 GLN A OE1 1 
ATOM   1133 O  OE1 B GLN A 1 135 ? 1.698   13.739  20.918  0.50 21.98 ? 136 GLN A OE1 1 
ATOM   1134 N  NE2 A GLN A 1 135 ? 0.624   16.880  20.114  0.50 16.38 ? 136 GLN A NE2 1 
ATOM   1135 N  NE2 B GLN A 1 135 ? 1.332   13.054  18.798  0.50 21.27 ? 136 GLN A NE2 1 
ATOM   1136 N  N   . GLN A 1 136 ? -3.416  13.442  23.277  1.00 12.07 ? 137 GLN A N   1 
ATOM   1137 C  CA  . GLN A 1 136 ? -4.101  13.654  24.595  1.00 10.82 ? 137 GLN A CA  1 
ATOM   1138 C  C   . GLN A 1 136 ? -4.492  12.312  25.260  1.00 11.92 ? 137 GLN A C   1 
ATOM   1139 O  O   . GLN A 1 136 ? -4.836  11.344  24.566  1.00 9.35  ? 137 GLN A O   1 
ATOM   1140 C  CB  . GLN A 1 136 ? -5.365  14.464  24.449  1.00 11.74 ? 137 GLN A CB  1 
ATOM   1141 C  CG  . GLN A 1 136 ? -5.199  15.763  23.543  1.00 14.02 ? 137 GLN A CG  1 
ATOM   1142 C  CD  . GLN A 1 136 ? -4.116  16.696  24.009  1.00 22.64 ? 137 GLN A CD  1 
ATOM   1143 O  OE1 . GLN A 1 136 ? -3.357  17.299  23.174  1.00 29.43 ? 137 GLN A OE1 1 
ATOM   1144 N  NE2 . GLN A 1 136 ? -3.976  16.798  25.311  1.00 17.91 ? 137 GLN A NE2 1 
ATOM   1145 N  N   . PRO A 1 137 ? -4.510  12.251  26.593  1.00 11.61 ? 138 PRO A N   1 
ATOM   1146 C  CA  . PRO A 1 137 ? -4.726  10.931  27.221  1.00 12.65 ? 138 PRO A CA  1 
ATOM   1147 C  C   . PRO A 1 137 ? -6.167  10.421  27.086  1.00 9.88  ? 138 PRO A C   1 
ATOM   1148 O  O   . PRO A 1 137 ? -6.398  9.197   27.176  1.00 12.93 ? 138 PRO A O   1 
ATOM   1149 C  CB  . PRO A 1 137 ? -4.360  11.152  28.716  1.00 14.77 ? 138 PRO A CB  1 
ATOM   1150 C  CG  . PRO A 1 137 ? -4.408  12.594  28.919  1.00 16.80 ? 138 PRO A CG  1 
ATOM   1151 C  CD  . PRO A 1 137 ? -4.110  13.290  27.588  1.00 14.57 ? 138 PRO A CD  1 
ATOM   1152 N  N   . ASP A 1 138 ? -7.116  11.323  26.782  1.00 8.01  ? 139 ASP A N   1 
ATOM   1153 C  CA  . ASP A 1 138 ? -8.494  10.905  26.536  1.00 8.58  ? 139 ASP A CA  1 
ATOM   1154 C  C   . ASP A 1 138 ? -8.894  11.302  25.080  1.00 8.12  ? 139 ASP A C   1 
ATOM   1155 O  O   . ASP A 1 138 ? -10.031 11.727  24.860  1.00 9.73  ? 139 ASP A O   1 
ATOM   1156 C  CB  . ASP A 1 138 ? -9.485  11.566  27.496  1.00 10.14 ? 139 ASP A CB  1 
ATOM   1157 C  CG  . ASP A 1 138 ? -9.362  13.085  27.500  1.00 10.87 ? 139 ASP A CG  1 
ATOM   1158 O  OD1 . ASP A 1 138 ? -8.408  13.660  26.936  1.00 14.49 ? 139 ASP A OD1 1 
ATOM   1159 O  OD2 . ASP A 1 138 ? -10.270 13.696  28.122  1.00 14.49 ? 139 ASP A OD2 1 
ATOM   1160 N  N   . GLY A 1 139 ? -7.940  11.203  24.115  1.00 7.22  ? 140 GLY A N   1 
ATOM   1161 C  CA  . GLY A 1 139 ? -8.211  11.705  22.790  1.00 6.40  ? 140 GLY A CA  1 
ATOM   1162 C  C   . GLY A 1 139 ? -9.050  10.800  21.917  1.00 7.51  ? 140 GLY A C   1 
ATOM   1163 O  O   . GLY A 1 139 ? -9.763  11.302  21.032  1.00 7.51  ? 140 GLY A O   1 
ATOM   1164 N  N   . LEU A 1 140 ? -8.893  9.472   22.102  1.00 7.14  ? 141 LEU A N   1 
ATOM   1165 C  CA  . LEU A 1 140 ? -9.621  8.545   21.231  1.00 4.18  ? 141 LEU A CA  1 
ATOM   1166 C  C   . LEU A 1 140 ? -10.484 7.578   22.056  1.00 5.80  ? 141 LEU A C   1 
ATOM   1167 O  O   . LEU A 1 140 ? -10.207 7.325   23.206  1.00 6.50  ? 141 LEU A O   1 
ATOM   1168 C  CB  . LEU A 1 140 ? -8.667  7.653   20.416  1.00 6.34  ? 141 LEU A CB  1 
ATOM   1169 C  CG  . LEU A 1 140 ? -7.584  8.327   19.574  1.00 10.91 ? 141 LEU A CG  1 
ATOM   1170 C  CD1 . LEU A 1 140 ? -6.876  7.275   18.701  1.00 9.55  ? 141 LEU A CD1 1 
ATOM   1171 C  CD2 . LEU A 1 140 ? -8.097  9.453   18.657  1.00 14.15 ? 141 LEU A CD2 1 
ATOM   1172 N  N   . ALA A 1 141 ? -11.531 7.074   21.391  1.00 6.09  ? 142 ALA A N   1 
ATOM   1173 C  CA  . ALA A 1 141 ? -12.302 5.956   21.966  1.00 5.70  ? 142 ALA A CA  1 
ATOM   1174 C  C   . ALA A 1 141 ? -12.342 4.955   20.846  1.00 6.30  ? 142 ALA A C   1 
ATOM   1175 O  O   . ALA A 1 141 ? -12.713 5.309   19.717  1.00 7.17  ? 142 ALA A O   1 
ATOM   1176 C  CB  . ALA A 1 141 ? -13.708 6.391   22.367  1.00 6.89  ? 142 ALA A CB  1 
ATOM   1177 N  N   . VAL A 1 142 ? -11.837 3.751   21.138  1.00 7.18  ? 143 VAL A N   1 
ATOM   1178 C  CA  . VAL A 1 142 ? -11.888 2.788   20.051  1.00 7.11  ? 143 VAL A CA  1 
ATOM   1179 C  C   . VAL A 1 142 ? -12.846 1.675   20.492  1.00 6.24  ? 143 VAL A C   1 
ATOM   1180 O  O   . VAL A 1 142 ? -12.708 1.127   21.604  1.00 6.79  ? 143 VAL A O   1 
ATOM   1181 C  CB  . VAL A 1 142 ? -10.524 2.145   19.723  1.00 7.14  ? 143 VAL A CB  1 
ATOM   1182 C  CG1 . VAL A 1 142 ? -10.636 1.061   18.554  1.00 8.19  ? 143 VAL A CG1 1 
ATOM   1183 C  CG2 . VAL A 1 142 ? -9.524  3.216   19.350  1.00 6.59  ? 143 VAL A CG2 1 
ATOM   1184 N  N   . LEU A 1 143 ? -13.818 1.372   19.637  1.00 5.30  ? 144 LEU A N   1 
ATOM   1185 C  CA  . LEU A 1 143 ? -14.774 0.323   19.924  1.00 6.57  ? 144 LEU A CA  1 
ATOM   1186 C  C   . LEU A 1 143 ? -14.264 -0.948  19.268  1.00 6.36  ? 144 LEU A C   1 
ATOM   1187 O  O   . LEU A 1 143 ? -14.177 -0.997  18.031  1.00 6.90  ? 144 LEU A O   1 
ATOM   1188 C  CB  . LEU A 1 143 ? -16.174 0.734   19.361  1.00 7.17  ? 144 LEU A CB  1 
ATOM   1189 C  CG  . LEU A 1 143 ? -17.325 -0.231  19.438  1.00 7.37  ? 144 LEU A CG  1 
ATOM   1190 C  CD1 . LEU A 1 143 ? -17.544 -0.607  20.892  1.00 9.90  ? 144 LEU A CD1 1 
ATOM   1191 C  CD2 . LEU A 1 143 ? -18.579 0.366   18.820  1.00 9.44  ? 144 LEU A CD2 1 
ATOM   1192 N  N   . GLY A 1 144 ? -14.017 -1.979  20.090  1.00 5.99  ? 145 GLY A N   1 
ATOM   1193 C  CA  . GLY A 1 144 ? -13.453 -3.233  19.563  1.00 4.88  ? 145 GLY A CA  1 
ATOM   1194 C  C   . GLY A 1 144 ? -14.506 -4.348  19.580  1.00 5.14  ? 145 GLY A C   1 
ATOM   1195 O  O   . GLY A 1 144 ? -15.228 -4.485  20.550  1.00 6.90  ? 145 GLY A O   1 
ATOM   1196 N  N   . ILE A 1 145 ? -14.587 -5.099  18.500  1.00 6.58  ? 146 ILE A N   1 
ATOM   1197 C  CA  . ILE A 1 145 ? -15.640 -6.130  18.309  1.00 4.19  ? 146 ILE A CA  1 
ATOM   1198 C  C   . ILE A 1 145 ? -14.911 -7.390  17.791  1.00 6.42  ? 146 ILE A C   1 
ATOM   1199 O  O   . ILE A 1 145 ? -14.270 -7.365  16.784  1.00 7.31  ? 146 ILE A O   1 
ATOM   1200 C  CB  . ILE A 1 145 ? -16.717 -5.629  17.269  1.00 5.49  ? 146 ILE A CB  1 
ATOM   1201 C  CG1 . ILE A 1 145 ? -17.311 -4.338  17.760  1.00 5.80  ? 146 ILE A CG1 1 
ATOM   1202 C  CG2 . ILE A 1 145 ? -17.738 -6.756  17.067  1.00 7.73  ? 146 ILE A CG2 1 
ATOM   1203 C  CD1 . ILE A 1 145 ? -18.379 -3.757  16.775  1.00 6.22  ? 146 ILE A CD1 1 
ATOM   1204 N  N   . PHE A 1 146 ? -15.119 -8.495  18.473  1.00 6.48  ? 147 PHE A N   1 
ATOM   1205 C  CA  . PHE A 1 146 ? -14.439 -9.744  18.057  1.00 5.52  ? 147 PHE A CA  1 
ATOM   1206 C  C   . PHE A 1 146 ? -15.236 -10.388 16.909  1.00 7.01  ? 147 PHE A C   1 
ATOM   1207 O  O   . PHE A 1 146 ? -16.479 -10.292 16.838  1.00 8.10  ? 147 PHE A O   1 
ATOM   1208 C  CB  . PHE A 1 146 ? -14.445 -10.689 19.251  1.00 5.49  ? 147 PHE A CB  1 
ATOM   1209 C  CG  . PHE A 1 146 ? -13.627 -10.196 20.350  1.00 3.22  ? 147 PHE A CG  1 
ATOM   1210 C  CD1 . PHE A 1 146 ? -12.257 -10.073 20.157  1.00 5.39  ? 147 PHE A CD1 1 
ATOM   1211 C  CD2 . PHE A 1 146 ? -14.166 -10.007 21.600  1.00 5.45  ? 147 PHE A CD2 1 
ATOM   1212 C  CE1 . PHE A 1 146 ? -11.374 -9.621  21.229  1.00 5.85  ? 147 PHE A CE1 1 
ATOM   1213 C  CE2 . PHE A 1 146 ? -13.382 -9.555  22.721  1.00 7.44  ? 147 PHE A CE2 1 
ATOM   1214 C  CZ  . PHE A 1 146 ? -11.937 -9.432  22.526  1.00 5.87  ? 147 PHE A CZ  1 
ATOM   1215 N  N   . LEU A 1 147 ? -14.480 -11.058 16.054  1.00 7.30  ? 148 LEU A N   1 
ATOM   1216 C  CA  . LEU A 1 147 ? -15.071 -11.874 14.957  1.00 5.10  ? 148 LEU A CA  1 
ATOM   1217 C  C   . LEU A 1 147 ? -14.710 -13.343 15.193  1.00 8.03  ? 148 LEU A C   1 
ATOM   1218 O  O   . LEU A 1 147 ? -13.529 -13.697 15.328  1.00 6.68  ? 148 LEU A O   1 
ATOM   1219 C  CB  . LEU A 1 147 ? -14.435 -11.461 13.552  1.00 6.95  ? 148 LEU A CB  1 
ATOM   1220 C  CG  . LEU A 1 147 ? -15.030 -10.232 12.913  1.00 8.97  ? 148 LEU A CG  1 
ATOM   1221 C  CD1 . LEU A 1 147 ? -14.869 -8.939  13.825  1.00 11.36 ? 148 LEU A CD1 1 
ATOM   1222 C  CD2 . LEU A 1 147 ? -14.381 -10.005 11.603  1.00 9.37  ? 148 LEU A CD2 1 
ATOM   1223 N  N   . LYS A 1 148 ? -15.754 -14.189 15.156  1.00 8.94  ? 149 LYS A N   1 
ATOM   1224 C  CA  . LYS A 1 148 ? -15.557 -15.635 15.046  1.00 9.48  ? 149 LYS A CA  1 
ATOM   1225 C  C   . LYS A 1 148 ? -16.047 -16.125 13.666  1.00 9.84  ? 149 LYS A C   1 
ATOM   1226 O  O   . LYS A 1 148 ? -16.892 -15.527 13.023  1.00 10.78 ? 149 LYS A O   1 
ATOM   1227 C  CB  . LYS A 1 148 ? -16.321 -16.373 16.167  1.00 10.59 ? 149 LYS A CB  1 
ATOM   1228 C  CG  . LYS A 1 148 ? -17.826 -16.147 16.095  1.00 12.36 ? 149 LYS A CG  1 
ATOM   1229 C  CD  . LYS A 1 148 ? -18.518 -16.717 17.375  1.00 17.03 ? 149 LYS A CD  1 
ATOM   1230 C  CE  . LYS A 1 148 ? -19.942 -16.931 17.077  1.00 26.82 ? 149 LYS A CE  1 
ATOM   1231 N  NZ  . LYS A 1 148 ? -20.635 -17.600 18.247  1.00 33.70 ? 149 LYS A NZ  1 
ATOM   1232 N  N   . VAL A 1 149 ? -15.573 -17.290 13.258  1.00 9.64  ? 150 VAL A N   1 
ATOM   1233 C  CA  . VAL A 1 149 ? -15.999 -17.814 11.964  1.00 11.44 ? 150 VAL A CA  1 
ATOM   1234 C  C   . VAL A 1 149 ? -17.198 -18.747 12.187  1.00 9.60  ? 150 VAL A C   1 
ATOM   1235 O  O   . VAL A 1 149 ? -17.152 -19.719 13.020  1.00 10.88 ? 150 VAL A O   1 
ATOM   1236 C  CB  . VAL A 1 149 ? -14.820 -18.571 11.353  1.00 11.36 ? 150 VAL A CB  1 
ATOM   1237 C  CG1 . VAL A 1 149 ? -15.197 -19.326 10.070  1.00 12.47 ? 150 VAL A CG1 1 
ATOM   1238 C  CG2 . VAL A 1 149 ? -13.686 -17.585 11.074  1.00 15.63 ? 150 VAL A CG2 1 
ATOM   1239 N  N   . GLY A 1 150 ? -18.216 -18.513 11.406  1.00 9.37  ? 151 GLY A N   1 
ATOM   1240 C  CA  . GLY A 1 150 ? -19.419 -19.372 11.410  1.00 12.64 ? 151 GLY A CA  1 
ATOM   1241 C  C   . GLY A 1 150 ? -20.319 -18.855 10.320  1.00 11.39 ? 151 GLY A C   1 
ATOM   1242 O  O   . GLY A 1 150 ? -19.961 -18.921 9.167   1.00 13.02 ? 151 GLY A O   1 
ATOM   1243 N  N   A SER A 1 151 ? -21.500 -18.340 10.682  0.50 13.37 ? 152 SER A N   1 
ATOM   1244 N  N   B SER A 1 151 ? -21.489 -18.328 10.711  0.50 12.86 ? 152 SER A N   1 
ATOM   1245 C  CA  A SER A 1 151 ? -22.367 -17.772 9.643   0.50 14.19 ? 152 SER A CA  1 
ATOM   1246 C  CA  B SER A 1 151 ? -22.422 -17.712 9.751   0.50 13.32 ? 152 SER A CA  1 
ATOM   1247 C  C   A SER A 1 151 ? -21.753 -16.473 9.080   0.50 14.69 ? 152 SER A C   1 
ATOM   1248 C  C   B SER A 1 151 ? -21.827 -16.420 9.129   0.50 14.17 ? 152 SER A C   1 
ATOM   1249 O  O   A SER A 1 151 ? -20.929 -15.784 9.750   0.50 13.54 ? 152 SER A O   1 
ATOM   1250 O  O   B SER A 1 151 ? -21.057 -15.684 9.816   0.50 13.13 ? 152 SER A O   1 
ATOM   1251 C  CB  A SER A 1 151 ? -23.779 -17.525 10.173  0.50 16.02 ? 152 SER A CB  1 
ATOM   1252 C  CB  B SER A 1 151 ? -23.748 -17.412 10.461  0.50 14.75 ? 152 SER A CB  1 
ATOM   1253 O  OG  A SER A 1 151 ? -23.841 -16.276 10.853  0.50 19.00 ? 152 SER A OG  1 
ATOM   1254 O  OG  B SER A 1 151 ? -24.306 -18.565 11.061  0.50 14.87 ? 152 SER A OG  1 
ATOM   1255 N  N   . ALA A 1 152 ? -22.117 -16.158 7.836   1.00 13.27 ? 153 ALA A N   1 
ATOM   1256 C  CA  . ALA A 1 152 ? -21.714 -14.883 7.201   1.00 11.88 ? 153 ALA A CA  1 
ATOM   1257 C  C   . ALA A 1 152 ? -22.364 -13.677 7.918   1.00 12.01 ? 153 ALA A C   1 
ATOM   1258 O  O   . ALA A 1 152 ? -23.486 -13.773 8.402   1.00 14.43 ? 153 ALA A O   1 
ATOM   1259 C  CB  . ALA A 1 152 ? -22.111 -14.799 5.665   1.00 14.63 ? 153 ALA A CB  1 
ATOM   1260 N  N   . LYS A 1 153 ? -21.634 -12.561 7.899   1.00 11.61 ? 154 LYS A N   1 
ATOM   1261 C  CA  . LYS A 1 153 ? -22.163 -11.259 8.326   1.00 12.36 ? 154 LYS A CA  1 
ATOM   1262 C  C   . LYS A 1 153 ? -22.517 -10.517 7.005   1.00 10.76 ? 154 LYS A C   1 
ATOM   1263 O  O   . LYS A 1 153 ? -21.632 -10.031 6.237   1.00 11.74 ? 154 LYS A O   1 
ATOM   1264 C  CB  . LYS A 1 153 ? -21.099 -10.461 9.119   1.00 12.54 ? 154 LYS A CB  1 
ATOM   1265 C  CG  . LYS A 1 153 ? -21.673 -9.273  9.866   1.00 15.45 ? 154 LYS A CG  1 
ATOM   1266 C  CD  . LYS A 1 153 ? -22.531 -9.731  11.039  1.00 15.73 ? 154 LYS A CD  1 
ATOM   1267 C  CE  . LYS A 1 153 ? -23.054 -8.579  11.893  1.00 19.99 ? 154 LYS A CE  1 
ATOM   1268 N  NZ  . LYS A 1 153 ? -24.070 -8.941  12.869  1.00 23.92 ? 154 LYS A NZ  1 
ATOM   1269 N  N   . PRO A 1 154 ? -23.838 -10.439 6.695   1.00 14.07 ? 155 PRO A N   1 
ATOM   1270 C  CA  . PRO A 1 154 ? -24.271 -9.819  5.408   1.00 13.59 ? 155 PRO A CA  1 
ATOM   1271 C  C   . PRO A 1 154 ? -23.799 -8.412  5.303   1.00 13.91 ? 155 PRO A C   1 
ATOM   1272 O  O   . PRO A 1 154 ? -23.287 -8.035  4.233   1.00 15.86 ? 155 PRO A O   1 
ATOM   1273 C  CB  . PRO A 1 154 ? -25.818 -9.859  5.470   1.00 14.52 ? 155 PRO A CB  1 
ATOM   1274 C  CG  . PRO A 1 154 ? -26.101 -11.058 6.431   1.00 17.50 ? 155 PRO A CG  1 
ATOM   1275 C  CD  . PRO A 1 154 ? -24.978 -10.934 7.469   1.00 12.79 ? 155 PRO A CD  1 
ATOM   1276 N  N   . GLY A 1 155 ? -23.798 -7.696  6.440   1.00 14.39 ? 156 GLY A N   1 
ATOM   1277 C  CA  . GLY A 1 155 ? -23.387 -6.300  6.377   1.00 15.49 ? 156 GLY A CA  1 
ATOM   1278 C  C   . GLY A 1 155 ? -21.899 -6.062  6.121   1.00 15.38 ? 156 GLY A C   1 
ATOM   1279 O  O   . GLY A 1 155 ? -21.460 -4.933  5.924   1.00 17.91 ? 156 GLY A O   1 
ATOM   1280 N  N   . LEU A 1 156 ? -21.083 -7.131  6.181   1.00 13.48 ? 157 LEU A N   1 
ATOM   1281 C  CA  . LEU A 1 156 ? -19.642 -7.079  5.841   1.00 11.22 ? 157 LEU A CA  1 
ATOM   1282 C  C   . LEU A 1 156 ? -19.321 -7.274  4.381   1.00 12.37 ? 157 LEU A C   1 
ATOM   1283 O  O   . LEU A 1 156 ? -18.213 -6.994  3.878   1.00 13.42 ? 157 LEU A O   1 
ATOM   1284 C  CB  . LEU A 1 156 ? -18.815 -8.087  6.724   1.00 12.90 ? 157 LEU A CB  1 
ATOM   1285 C  CG  . LEU A 1 156 ? -17.287 -8.277  6.508   1.00 11.37 ? 157 LEU A CG  1 
ATOM   1286 C  CD1 . LEU A 1 156 ? -16.527 -6.924  6.859   1.00 13.19 ? 157 LEU A CD1 1 
ATOM   1287 C  CD2 . LEU A 1 156 ? -16.740 -9.406  7.360   1.00 9.58  ? 157 LEU A CD2 1 
ATOM   1288 N  N   . GLN A 1 157 ? -20.286 -7.847  3.652   1.00 12.44 ? 158 GLN A N   1 
ATOM   1289 C  CA  . GLN A 1 157 ? -19.945 -8.306  2.316   1.00 13.35 ? 158 GLN A CA  1 
ATOM   1290 C  C   . GLN A 1 157 ? -19.499 -7.186  1.378   1.00 12.91 ? 158 GLN A C   1 
ATOM   1291 O  O   . GLN A 1 157 ? -18.593 -7.379  0.575   1.00 13.83 ? 158 GLN A O   1 
ATOM   1292 C  CB  . GLN A 1 157 ? -21.085 -9.148  1.709   1.00 15.32 ? 158 GLN A CB  1 
ATOM   1293 C  CG  . GLN A 1 157 ? -20.650 -9.904  0.407   1.00 13.73 ? 158 GLN A CG  1 
ATOM   1294 C  CD  . GLN A 1 157 ? -19.567 -10.946 0.710   1.00 14.92 ? 158 GLN A CD  1 
ATOM   1295 O  OE1 . GLN A 1 157 ? -19.557 -11.481 1.833   1.00 15.98 ? 158 GLN A OE1 1 
ATOM   1296 N  NE2 . GLN A 1 157 ? -18.648 -11.196 -0.229  1.00 15.66 ? 158 GLN A NE2 1 
ATOM   1297 N  N   . LYS A 1 158 ? -20.085 -5.995  1.527   1.00 14.51 ? 159 LYS A N   1 
ATOM   1298 C  CA  . LYS A 1 158 ? -19.679 -4.908  0.656   1.00 14.58 ? 159 LYS A CA  1 
ATOM   1299 C  C   . LYS A 1 158 ? -18.182 -4.582  0.819   1.00 14.89 ? 159 LYS A C   1 
ATOM   1300 O  O   . LYS A 1 158 ? -17.463 -4.278  -0.137  1.00 15.30 ? 159 LYS A O   1 
ATOM   1301 C  CB  . LYS A 1 158 ? -20.636 -3.713  0.826   1.00 16.63 ? 159 LYS A CB  1 
ATOM   1302 C  CG  . LYS A 1 158 ? -22.094 -4.063  0.462   1.00 22.97 ? 159 LYS A CG  1 
ATOM   1303 C  CD  . LYS A 1 158 ? -22.416 -3.720  -1.037  1.00 34.50 ? 159 LYS A CD  1 
ATOM   1304 C  CE  . LYS A 1 158 ? -23.466 -4.735  -1.775  1.00 33.06 ? 159 LYS A CE  1 
ATOM   1305 N  NZ  . LYS A 1 158 ? -23.019 -6.135  -2.445  1.00 33.02 ? 159 LYS A NZ  1 
ATOM   1306 N  N   . VAL A 1 159 ? -17.703 -4.713  2.081   1.00 13.29 ? 160 VAL A N   1 
ATOM   1307 C  CA  . VAL A 1 159 ? -16.263 -4.504  2.318   1.00 12.41 ? 160 VAL A CA  1 
ATOM   1308 C  C   . VAL A 1 159 ? -15.474 -5.648  1.639   1.00 12.55 ? 160 VAL A C   1 
ATOM   1309 O  O   . VAL A 1 159 ? -14.515 -5.405  0.934   1.00 11.31 ? 160 VAL A O   1 
ATOM   1310 C  CB  . VAL A 1 159 ? -15.984 -4.506  3.804   1.00 12.65 ? 160 VAL A CB  1 
ATOM   1311 C  CG1 . VAL A 1 159 ? -14.445 -4.494  4.073   1.00 13.31 ? 160 VAL A CG1 1 
ATOM   1312 C  CG2 . VAL A 1 159 ? -16.797 -3.371  4.486   1.00 17.05 ? 160 VAL A CG2 1 
ATOM   1313 N  N   . VAL A 1 160 ? -15.864 -6.897  1.864   1.00 13.02 ? 161 VAL A N   1 
ATOM   1314 C  CA  . VAL A 1 160 ? -15.116 -8.013  1.292   1.00 14.85 ? 161 VAL A CA  1 
ATOM   1315 C  C   . VAL A 1 160 ? -15.070 -7.929  -0.247  1.00 14.71 ? 161 VAL A C   1 
ATOM   1316 O  O   . VAL A 1 160 ? -14.043 -8.110  -0.838  1.00 15.22 ? 161 VAL A O   1 
ATOM   1317 C  CB  . VAL A 1 160 ? -15.826 -9.375  1.756   1.00 16.82 ? 161 VAL A CB  1 
ATOM   1318 C  CG1 . VAL A 1 160 ? -15.421 -10.574 0.899   1.00 20.24 ? 161 VAL A CG1 1 
ATOM   1319 C  CG2 . VAL A 1 160 ? -15.621 -9.584  3.223   1.00 19.41 ? 161 VAL A CG2 1 
ATOM   1320 N  N   . ASP A 1 161 ? -16.153 -7.503  -0.861  1.00 17.09 ? 162 ASP A N   1 
ATOM   1321 C  CA  . ASP A 1 161 ? -16.156 -7.513  -2.313  1.00 18.21 ? 162 ASP A CA  1 
ATOM   1322 C  C   . ASP A 1 161 ? -15.213 -6.474  -2.966  1.00 19.37 ? 162 ASP A C   1 
ATOM   1323 O  O   . ASP A 1 161 ? -14.785 -6.668  -4.125  1.00 21.44 ? 162 ASP A O   1 
ATOM   1324 C  CB  . ASP A 1 161 ? -17.559 -7.395  -2.798  1.00 19.81 ? 162 ASP A CB  1 
ATOM   1325 C  CG  . ASP A 1 161 ? -18.288 -8.758  -2.828  1.00 20.41 ? 162 ASP A CG  1 
ATOM   1326 O  OD1 . ASP A 1 161 ? -17.631 -9.816  -2.959  1.00 26.27 ? 162 ASP A OD1 1 
ATOM   1327 O  OD2 . ASP A 1 161 ? -19.531 -8.752  -2.645  1.00 24.89 ? 162 ASP A OD2 1 
ATOM   1328 N  N   . VAL A 1 162 ? -14.877 -5.366  -2.256  1.00 16.89 ? 163 VAL A N   1 
ATOM   1329 C  CA  . VAL A 1 162 ? -13.971 -4.338  -2.844  1.00 18.25 ? 163 VAL A CA  1 
ATOM   1330 C  C   . VAL A 1 162 ? -12.455 -4.639  -2.627  1.00 15.65 ? 163 VAL A C   1 
ATOM   1331 O  O   . VAL A 1 162 ? -11.538 -3.985  -3.170  1.00 15.13 ? 163 VAL A O   1 
ATOM   1332 C  CB  . VAL A 1 162 ? -14.435 -2.927  -2.309  1.00 19.65 ? 163 VAL A CB  1 
ATOM   1333 C  CG1 . VAL A 1 162 ? -13.967 -2.661  -0.888  1.00 20.51 ? 163 VAL A CG1 1 
ATOM   1334 C  CG2 . VAL A 1 162 ? -14.014 -1.781  -3.241  1.00 20.25 ? 163 VAL A CG2 1 
ATOM   1335 N  N   . LEU A 1 163 ? -12.118 -5.636  -1.783  1.00 14.60 ? 164 LEU A N   1 
ATOM   1336 C  CA  . LEU A 1 163 ? -10.692 -5.914  -1.463  1.00 13.08 ? 164 LEU A CA  1 
ATOM   1337 C  C   . LEU A 1 163 ? -9.786  -6.288  -2.643  1.00 14.06 ? 164 LEU A C   1 
ATOM   1338 O  O   . LEU A 1 163 ? -8.590  -6.022  -2.632  1.00 14.55 ? 164 LEU A O   1 
ATOM   1339 C  CB  . LEU A 1 163 ? -10.558 -6.920  -0.293  1.00 12.56 ? 164 LEU A CB  1 
ATOM   1340 C  CG  . LEU A 1 163 ? -11.310 -6.621  1.006   1.00 12.83 ? 164 LEU A CG  1 
ATOM   1341 C  CD1 . LEU A 1 163 ? -10.950 -7.877  1.912   1.00 13.41 ? 164 LEU A CD1 1 
ATOM   1342 C  CD2 . LEU A 1 163 ? -10.818 -5.302  1.585   1.00 13.38 ? 164 LEU A CD2 1 
ATOM   1343 N  N   . ASP A 1 164 ? -10.352 -6.955  -3.660  1.00 18.02 ? 165 ASP A N   1 
ATOM   1344 C  CA  . ASP A 1 164 ? -9.505  -7.319  -4.768  1.00 20.59 ? 165 ASP A CA  1 
ATOM   1345 C  C   . ASP A 1 164 ? -9.079  -6.042  -5.555  1.00 20.76 ? 165 ASP A C   1 
ATOM   1346 O  O   . ASP A 1 164 ? -8.060  -6.101  -6.239  1.00 22.48 ? 165 ASP A O   1 
ATOM   1347 C  CB  . ASP A 1 164 ? -10.275 -8.278  -5.656  1.00 23.45 ? 165 ASP A CB  1 
ATOM   1348 C  CG  . ASP A 1 164 ? -11.227 -7.540  -6.501  1.00 27.73 ? 165 ASP A CG  1 
ATOM   1349 O  OD1 . ASP A 1 164 ? -12.196 -6.990  -5.923  1.00 35.53 ? 165 ASP A OD1 1 
ATOM   1350 O  OD2 . ASP A 1 164 ? -10.930 -7.369  -7.716  1.00 35.40 ? 165 ASP A OD2 1 
ATOM   1351 N  N   . SER A 1 165 ? -9.796  -4.911  -5.385  1.00 20.20 ? 166 SER A N   1 
ATOM   1352 C  CA  . SER A 1 165 ? -9.428  -3.611  -5.984  1.00 19.36 ? 166 SER A CA  1 
ATOM   1353 C  C   . SER A 1 165 ? -8.310  -2.815  -5.199  1.00 19.95 ? 166 SER A C   1 
ATOM   1354 O  O   . SER A 1 165 ? -7.735  -1.799  -5.679  1.00 18.10 ? 166 SER A O   1 
ATOM   1355 C  CB  . SER A 1 165 ? -10.690 -2.775  -6.164  1.00 20.14 ? 166 SER A CB  1 
ATOM   1356 O  OG  . SER A 1 165 ? -11.014 -2.080  -4.973  1.00 22.63 ? 166 SER A OG  1 
ATOM   1357 N  N   . ILE A 1 166 ? -8.031  -3.242  -3.952  1.00 16.47 ? 167 ILE A N   1 
ATOM   1358 C  CA  . ILE A 1 166 ? -6.944  -2.658  -3.129  1.00 16.44 ? 167 ILE A CA  1 
ATOM   1359 C  C   . ILE A 1 166 ? -6.015  -3.755  -2.600  1.00 15.33 ? 167 ILE A C   1 
ATOM   1360 O  O   . ILE A 1 166 ? -5.634  -3.801  -1.423  1.00 15.68 ? 167 ILE A O   1 
ATOM   1361 C  CB  . ILE A 1 166 ? -7.533  -1.805  -1.938  1.00 17.24 ? 167 ILE A CB  1 
ATOM   1362 C  CG1 . ILE A 1 166 ? -8.522  -2.631  -1.085  1.00 13.80 ? 167 ILE A CG1 1 
ATOM   1363 C  CG2 . ILE A 1 166 ? -8.320  -0.589  -2.471  1.00 16.63 ? 167 ILE A CG2 1 
ATOM   1364 C  CD1 . ILE A 1 166 ? -8.648  -2.086  0.391   1.00 16.10 ? 167 ILE A CD1 1 
ATOM   1365 N  N   . LYS A 1 167 ? -5.633  -4.686  -3.475  1.00 15.95 ? 168 LYS A N   1 
ATOM   1366 C  CA  . LYS A 1 167 ? -4.789  -5.767  -3.049  1.00 15.63 ? 168 LYS A CA  1 
ATOM   1367 C  C   . LYS A 1 167 ? -3.452  -5.418  -2.358  1.00 15.65 ? 168 LYS A C   1 
ATOM   1368 O  O   . LYS A 1 167 ? -3.075  -6.096  -1.423  1.00 14.88 ? 168 LYS A O   1 
ATOM   1369 C  CB  . LYS A 1 167 ? -4.511  -6.720  -4.231  1.00 13.89 ? 168 LYS A CB  1 
ATOM   1370 C  CG  . LYS A 1 167 ? -3.793  -7.925  -3.806  1.00 17.47 ? 168 LYS A CG  1 
ATOM   1371 C  CD  . LYS A 1 167 ? -3.343  -8.788  -5.021  1.00 22.93 ? 168 LYS A CD  1 
ATOM   1372 C  CE  . LYS A 1 167 ? -3.023  -10.157 -4.500  1.00 28.42 ? 168 LYS A CE  1 
ATOM   1373 N  NZ  . LYS A 1 167 ? -2.580  -11.065 -5.608  1.00 33.21 ? 168 LYS A NZ  1 
ATOM   1374 N  N   . THR A 1 168 ? -2.752  -4.357  -2.824  1.00 12.31 ? 169 THR A N   1 
ATOM   1375 C  CA  . THR A 1 168 ? -1.385  -4.046  -2.396  1.00 14.90 ? 169 THR A CA  1 
ATOM   1376 C  C   . THR A 1 168 ? -1.295  -2.668  -1.752  1.00 13.51 ? 169 THR A C   1 
ATOM   1377 O  O   . THR A 1 168 ? -2.179  -1.846  -1.935  1.00 16.38 ? 169 THR A O   1 
ATOM   1378 C  CB  . THR A 1 168 ? -0.363  -4.130  -3.584  1.00 15.97 ? 169 THR A CB  1 
ATOM   1379 O  OG1 . THR A 1 168 ? -0.873  -3.337  -4.667  1.00 20.32 ? 169 THR A OG1 1 
ATOM   1380 C  CG2 . THR A 1 168 ? -0.159  -5.643  -4.017  1.00 17.01 ? 169 THR A CG2 1 
ATOM   1381 N  N   A LYS A 1 169 ? -0.283  -2.502  -0.922  0.50 15.04 ? 170 LYS A N   1 
ATOM   1382 N  N   B LYS A 1 169 ? -0.270  -2.508  -0.933  0.50 15.43 ? 170 LYS A N   1 
ATOM   1383 C  CA  A LYS A 1 169 ? -0.005  -1.274  -0.174  0.50 15.72 ? 170 LYS A CA  1 
ATOM   1384 C  CA  B LYS A 1 169 ? 0.110   -1.237  -0.328  0.50 16.52 ? 170 LYS A CA  1 
ATOM   1385 C  C   A LYS A 1 169 ? 0.025   0.000   -0.997  0.50 16.67 ? 170 LYS A C   1 
ATOM   1386 C  C   B LYS A 1 169 ? -0.214  -0.028  -1.216  0.50 17.11 ? 170 LYS A C   1 
ATOM   1387 O  O   A LYS A 1 169 ? 0.868   0.076   -1.928  0.50 17.69 ? 170 LYS A O   1 
ATOM   1388 O  O   B LYS A 1 169 ? 0.043   -0.019  -2.442  0.50 18.41 ? 170 LYS A O   1 
ATOM   1389 C  CB  A LYS A 1 169 ? 1.331   -1.432  0.508   0.50 15.76 ? 170 LYS A CB  1 
ATOM   1390 C  CB  B LYS A 1 169 ? 1.587   -1.267  0.037   0.50 16.72 ? 170 LYS A CB  1 
ATOM   1391 C  CG  A LYS A 1 169 ? 1.799   -0.131  1.232   0.50 14.15 ? 170 LYS A CG  1 
ATOM   1392 C  CG  B LYS A 1 169 ? 2.014   -0.151  1.043   0.50 15.67 ? 170 LYS A CG  1 
ATOM   1393 C  CD  A LYS A 1 169 ? 2.966   -0.454  2.097   0.50 16.24 ? 170 LYS A CD  1 
ATOM   1394 C  CD  B LYS A 1 169 ? 3.433   -0.392  1.543   0.50 18.42 ? 170 LYS A CD  1 
ATOM   1395 C  CE  A LYS A 1 169 ? 4.218   -0.567  1.239   0.50 17.99 ? 170 LYS A CE  1 
ATOM   1396 C  CE  B LYS A 1 169 ? 3.862   0.699   2.542   0.50 18.72 ? 170 LYS A CE  1 
ATOM   1397 N  NZ  A LYS A 1 169 ? 5.267   -1.386  1.886   0.50 25.42 ? 170 LYS A NZ  1 
ATOM   1398 N  NZ  B LYS A 1 169 ? 5.276   1.030   2.248   0.50 23.38 ? 170 LYS A NZ  1 
ATOM   1399 N  N   . GLY A 1 170 ? -0.829  0.968   -0.609  1.00 17.85 ? 171 GLY A N   1 
ATOM   1400 C  CA  . GLY A 1 170 ? -0.984  2.274   -1.266  1.00 19.15 ? 171 GLY A CA  1 
ATOM   1401 C  C   . GLY A 1 170 ? -2.126  2.350   -2.196  1.00 19.53 ? 171 GLY A C   1 
ATOM   1402 O  O   . GLY A 1 170 ? -2.500  3.463   -2.654  1.00 21.81 ? 171 GLY A O   1 
ATOM   1403 N  N   . LYS A 1 171 ? -2.778  1.217   -2.501  1.00 17.88 ? 172 LYS A N   1 
ATOM   1404 C  CA  . LYS A 1 171 ? -4.059  1.306   -3.227  1.00 17.90 ? 172 LYS A CA  1 
ATOM   1405 C  C   . LYS A 1 171 ? -5.334  1.755   -2.479  1.00 19.01 ? 172 LYS A C   1 
ATOM   1406 O  O   . LYS A 1 171 ? -5.610  1.323   -1.337  1.00 18.65 ? 172 LYS A O   1 
ATOM   1407 C  CB  . LYS A 1 171 ? -4.396  -0.025  -3.916  1.00 18.23 ? 172 LYS A CB  1 
ATOM   1408 C  CG  . LYS A 1 171 ? -3.322  -0.501  -4.783  1.00 20.69 ? 172 LYS A CG  1 
ATOM   1409 C  CD  . LYS A 1 171 ? -3.965  -1.189  -5.957  1.00 31.61 ? 172 LYS A CD  1 
ATOM   1410 C  CE  . LYS A 1 171 ? -2.940  -1.711  -6.880  1.00 35.68 ? 172 LYS A CE  1 
ATOM   1411 N  NZ  . LYS A 1 171 ? -3.549  -2.810  -7.691  1.00 39.14 ? 172 LYS A NZ  1 
ATOM   1412 N  N   . SER A 1 172 ? -6.151  2.580   -3.106  1.00 18.53 ? 173 SER A N   1 
ATOM   1413 C  CA  . SER A 1 172 ? -7.348  2.998   -2.515  1.00 20.61 ? 173 SER A CA  1 
ATOM   1414 C  C   . SER A 1 172 ? -8.480  2.949   -3.526  1.00 21.42 ? 173 SER A C   1 
ATOM   1415 O  O   . SER A 1 172 ? -8.258  2.835   -4.782  1.00 21.95 ? 173 SER A O   1 
ATOM   1416 C  CB  . SER A 1 172 ? -7.194  4.419   -1.911  1.00 22.21 ? 173 SER A CB  1 
ATOM   1417 O  OG  . SER A 1 172 ? -7.191  5.418   -2.931  1.00 23.55 ? 173 SER A OG  1 
ATOM   1418 N  N   . ALA A 1 173 ? -9.664  2.999   -3.014  1.00 21.54 ? 174 ALA A N   1 
ATOM   1419 C  CA  . ALA A 1 173 ? -10.888 2.995   -3.825  1.00 22.04 ? 174 ALA A CA  1 
ATOM   1420 C  C   . ALA A 1 173 ? -11.977 3.827   -3.184  1.00 23.17 ? 174 ALA A C   1 
ATOM   1421 O  O   . ALA A 1 173 ? -12.070 3.904   -1.929  1.00 22.10 ? 174 ALA A O   1 
ATOM   1422 C  CB  . ALA A 1 173 ? -11.346 1.581   -4.056  1.00 21.69 ? 174 ALA A CB  1 
ATOM   1423 N  N   A ASP A 1 174 ? -12.947 4.177   -4.042  0.50 21.87 ? 175 ASP A N   1 
ATOM   1424 N  N   B ASP A 1 174 ? -12.667 4.669   -3.952  0.50 21.40 ? 175 ASP A N   1 
ATOM   1425 C  CA  A ASP A 1 174 ? -14.195 4.807   -3.661  0.50 20.66 ? 175 ASP A CA  1 
ATOM   1426 C  CA  B ASP A 1 174 ? -13.768 5.362   -3.287  0.50 20.52 ? 175 ASP A CA  1 
ATOM   1427 C  C   A ASP A 1 174 ? -15.127 3.972   -2.811  0.50 20.02 ? 175 ASP A C   1 
ATOM   1428 C  C   B ASP A 1 174 ? -14.672 4.204   -2.733  0.50 20.58 ? 175 ASP A C   1 
ATOM   1429 O  O   A ASP A 1 174 ? -15.585 2.864   -3.162  0.50 17.91 ? 175 ASP A O   1 
ATOM   1430 O  O   B ASP A 1 174 ? -14.566 3.054   -3.229  0.50 18.37 ? 175 ASP A O   1 
ATOM   1431 C  CB  A ASP A 1 174 ? -14.962 5.313   -4.885  0.50 20.74 ? 175 ASP A CB  1 
ATOM   1432 C  CB  B ASP A 1 174 ? -14.446 6.446   -4.169  0.50 20.84 ? 175 ASP A CB  1 
ATOM   1433 C  CG  A ASP A 1 174 ? -14.320 6.499   -5.488  0.50 22.44 ? 175 ASP A CG  1 
ATOM   1434 C  CG  B ASP A 1 174 ? -15.876 6.149   -4.452  0.50 21.71 ? 175 ASP A CG  1 
ATOM   1435 O  OD1 A ASP A 1 174 ? -13.673 7.257   -4.735  0.50 23.30 ? 175 ASP A OD1 1 
ATOM   1436 O  OD1 B ASP A 1 174 ? -16.093 5.099   -5.064  0.50 20.00 ? 175 ASP A OD1 1 
ATOM   1437 O  OD2 A ASP A 1 174 ? -14.480 6.692   -6.712  0.50 22.98 ? 175 ASP A OD2 1 
ATOM   1438 O  OD2 B ASP A 1 174 ? -16.788 6.959   -4.073  0.50 23.99 ? 175 ASP A OD2 1 
ATOM   1439 N  N   . PHE A 1 175 ? -15.426 4.501   -1.652  1.00 18.79 ? 176 PHE A N   1 
ATOM   1440 C  CA  . PHE A 1 175 ? -16.194 3.590   -0.806  1.00 19.83 ? 176 PHE A CA  1 
ATOM   1441 C  C   . PHE A 1 175 ? -17.257 4.339   -0.027  1.00 20.14 ? 176 PHE A C   1 
ATOM   1442 O  O   . PHE A 1 175 ? -17.045 4.701   1.132   1.00 20.67 ? 176 PHE A O   1 
ATOM   1443 C  CB  . PHE A 1 175 ? -15.248 2.768   0.119   1.00 17.68 ? 176 PHE A CB  1 
ATOM   1444 C  CG  . PHE A 1 175 ? -15.888 1.517   0.650   1.00 17.21 ? 176 PHE A CG  1 
ATOM   1445 C  CD1 . PHE A 1 175 ? -16.185 0.449   -0.204  1.00 17.81 ? 176 PHE A CD1 1 
ATOM   1446 C  CD2 . PHE A 1 175 ? -16.223 1.373   1.999   1.00 17.09 ? 176 PHE A CD2 1 
ATOM   1447 C  CE1 . PHE A 1 175 ? -16.790 -0.724  0.314   1.00 19.96 ? 176 PHE A CE1 1 
ATOM   1448 C  CE2 . PHE A 1 175 ? -16.861 0.200   2.500   1.00 19.81 ? 176 PHE A CE2 1 
ATOM   1449 C  CZ  . PHE A 1 175 ? -17.124 -0.850  1.659   1.00 20.95 ? 176 PHE A CZ  1 
ATOM   1450 N  N   . THR A 1 176 ? -18.347 4.655   -0.712  1.00 16.49 ? 177 THR A N   1 
ATOM   1451 C  CA  . THR A 1 176 ? -19.404 5.502   -0.220  1.00 16.80 ? 177 THR A CA  1 
ATOM   1452 C  C   . THR A 1 176 ? -20.604 4.670   0.208   1.00 15.48 ? 177 THR A C   1 
ATOM   1453 O  O   . THR A 1 176 ? -20.778 3.526   -0.278  1.00 16.82 ? 177 THR A O   1 
ATOM   1454 C  CB  . THR A 1 176 ? -19.790 6.591   -1.338  1.00 17.07 ? 177 THR A CB  1 
ATOM   1455 O  OG1 . THR A 1 176 ? -20.265 5.905   -2.517  1.00 21.28 ? 177 THR A OG1 1 
ATOM   1456 C  CG2 . THR A 1 176 ? -18.594 7.488   -1.651  1.00 19.61 ? 177 THR A CG2 1 
ATOM   1457 N  N   . ASN A 1 177 ? -21.432 5.242   1.066   1.00 14.97 ? 178 ASN A N   1 
ATOM   1458 C  CA  . ASN A 1 177 ? -22.705 4.738   1.520   1.00 15.49 ? 178 ASN A CA  1 
ATOM   1459 C  C   . ASN A 1 177 ? -22.564 3.366   2.232   1.00 17.22 ? 178 ASN A C   1 
ATOM   1460 O  O   . ASN A 1 177 ? -23.495 2.624   2.268   1.00 18.81 ? 178 ASN A O   1 
ATOM   1461 C  CB  . ASN A 1 177 ? -23.721 4.615   0.388   1.00 15.63 ? 178 ASN A CB  1 
ATOM   1462 C  CG  . ASN A 1 177 ? -23.953 5.994   -0.285  1.00 17.10 ? 178 ASN A CG  1 
ATOM   1463 O  OD1 . ASN A 1 177 ? -24.640 6.835   0.289   1.00 17.42 ? 178 ASN A OD1 1 
ATOM   1464 N  ND2 . ASN A 1 177 ? -23.283 6.239   -1.406  1.00 16.85 ? 178 ASN A ND2 1 
ATOM   1465 N  N   . PHE A 1 178 ? -21.401 3.131   2.840   1.00 15.40 ? 179 PHE A N   1 
ATOM   1466 C  CA  . PHE A 1 178 ? -21.272 1.887   3.687   1.00 15.13 ? 179 PHE A CA  1 
ATOM   1467 C  C   . PHE A 1 178 ? -21.808 2.168   5.065   1.00 13.87 ? 179 PHE A C   1 
ATOM   1468 O  O   . PHE A 1 178 ? -21.387 3.155   5.712   1.00 14.94 ? 179 PHE A O   1 
ATOM   1469 C  CB  . PHE A 1 178 ? -19.853 1.477   3.799   1.00 13.83 ? 179 PHE A CB  1 
ATOM   1470 C  CG  . PHE A 1 178 ? -19.726 0.223   4.582   1.00 14.54 ? 179 PHE A CG  1 
ATOM   1471 C  CD1 . PHE A 1 178 ? -20.058 -0.999  4.008   1.00 18.36 ? 179 PHE A CD1 1 
ATOM   1472 C  CD2 . PHE A 1 178 ? -19.431 0.301   5.951   1.00 12.22 ? 179 PHE A CD2 1 
ATOM   1473 C  CE1 . PHE A 1 178 ? -20.022 -2.125  4.783   1.00 14.09 ? 179 PHE A CE1 1 
ATOM   1474 C  CE2 . PHE A 1 178 ? -19.421 -0.835  6.717   1.00 13.08 ? 179 PHE A CE2 1 
ATOM   1475 C  CZ  . PHE A 1 178 ? -19.667 -2.017  6.159   1.00 12.97 ? 179 PHE A CZ  1 
ATOM   1476 N  N   . ASP A 1 179 ? -22.681 1.301   5.556   1.00 15.20 ? 180 ASP A N   1 
ATOM   1477 C  CA  . ASP A 1 179 ? -23.327 1.517   6.826   1.00 14.98 ? 180 ASP A CA  1 
ATOM   1478 C  C   . ASP A 1 179 ? -22.672 0.714   7.946   1.00 12.26 ? 180 ASP A C   1 
ATOM   1479 O  O   . ASP A 1 179 ? -22.840 -0.531  7.984   1.00 10.66 ? 180 ASP A O   1 
ATOM   1480 C  CB  . ASP A 1 179 ? -24.776 1.090   6.749   1.00 17.99 ? 180 ASP A CB  1 
ATOM   1481 C  CG  . ASP A 1 179 ? -25.598 1.563   7.924   1.00 18.77 ? 180 ASP A CG  1 
ATOM   1482 O  OD1 . ASP A 1 179 ? -25.092 1.813   9.078   1.00 14.70 ? 180 ASP A OD1 1 
ATOM   1483 O  OD2 . ASP A 1 179 ? -26.821 1.745   7.690   1.00 22.63 ? 180 ASP A OD2 1 
ATOM   1484 N  N   . PRO A 1 180 ? -21.937 1.372   8.866   1.00 11.26 ? 181 PRO A N   1 
ATOM   1485 C  CA  . PRO A 1 180 ? -21.229 0.484   9.855   1.00 11.73 ? 181 PRO A CA  1 
ATOM   1486 C  C   . PRO A 1 180 ? -22.162 -0.150  10.911  1.00 11.70 ? 181 PRO A C   1 
ATOM   1487 O  O   . PRO A 1 180 ? -21.729 -1.059  11.683  1.00 10.42 ? 181 PRO A O   1 
ATOM   1488 C  CB  . PRO A 1 180 ? -20.189 1.439   10.451  1.00 13.11 ? 181 PRO A CB  1 
ATOM   1489 C  CG  . PRO A 1 180 ? -20.968 2.781   10.519  1.00 13.81 ? 181 PRO A CG  1 
ATOM   1490 C  CD  . PRO A 1 180 ? -21.582 2.790   9.074   1.00 13.74 ? 181 PRO A CD  1 
ATOM   1491 N  N   . ARG A 1 181 ? -23.464 0.230   10.931  1.00 10.74 ? 182 ARG A N   1 
ATOM   1492 C  CA  . ARG A 1 181 ? -24.411 -0.439  11.847  1.00 10.90 ? 182 ARG A CA  1 
ATOM   1493 C  C   . ARG A 1 181 ? -24.530 -1.940  11.542  1.00 13.05 ? 182 ARG A C   1 
ATOM   1494 O  O   . ARG A 1 181 ? -24.932 -2.731  12.419  1.00 13.74 ? 182 ARG A O   1 
ATOM   1495 C  CB  . ARG A 1 181 ? -25.795 0.250   11.794  1.00 12.52 ? 182 ARG A CB  1 
ATOM   1496 C  CG  . ARG A 1 181 ? -25.673 1.705   12.351  1.00 12.15 ? 182 ARG A CG  1 
ATOM   1497 C  CD  . ARG A 1 181 ? -27.045 2.355   12.226  1.00 13.41 ? 182 ARG A CD  1 
ATOM   1498 N  NE  . ARG A 1 181 ? -27.346 2.533   10.839  1.00 15.62 ? 182 ARG A NE  1 
ATOM   1499 C  CZ  . ARG A 1 181 ? -28.454 3.168   10.431  1.00 21.79 ? 182 ARG A CZ  1 
ATOM   1500 N  NH1 . ARG A 1 181 ? -29.290 3.642   11.337  1.00 20.11 ? 182 ARG A NH1 1 
ATOM   1501 N  NH2 . ARG A 1 181 ? -28.723 3.310   9.145   1.00 18.35 ? 182 ARG A NH2 1 
ATOM   1502 N  N   . GLY A 1 182 ? -24.208 -2.274  10.306  1.00 11.77 ? 183 GLY A N   1 
ATOM   1503 C  CA  . GLY A 1 182 ? -24.291 -3.686  9.856   1.00 12.88 ? 183 GLY A CA  1 
ATOM   1504 C  C   . GLY A 1 182 ? -23.194 -4.565  10.405  1.00 13.62 ? 183 GLY A C   1 
ATOM   1505 O  O   . GLY A 1 182 ? -23.220 -5.782  10.139  1.00 15.34 ? 183 GLY A O   1 
ATOM   1506 N  N   . LEU A 1 183 ? -22.218 -3.954  11.090  1.00 11.00 ? 184 LEU A N   1 
ATOM   1507 C  CA  . LEU A 1 183 ? -21.064 -4.705  11.681  1.00 12.31 ? 184 LEU A CA  1 
ATOM   1508 C  C   . LEU A 1 183 ? -21.255 -4.898  13.189  1.00 11.44 ? 184 LEU A C   1 
ATOM   1509 O  O   . LEU A 1 183 ? -20.328 -5.503  13.828  1.00 14.31 ? 184 LEU A O   1 
ATOM   1510 C  CB  . LEU A 1 183 ? -19.741 -3.975  11.430  1.00 11.42 ? 184 LEU A CB  1 
ATOM   1511 C  CG  . LEU A 1 183 ? -19.333 -3.774  9.928   1.00 12.04 ? 184 LEU A CG  1 
ATOM   1512 C  CD1 . LEU A 1 183 ? -18.099 -2.964  9.749   1.00 13.30 ? 184 LEU A CD1 1 
ATOM   1513 C  CD2 . LEU A 1 183 ? -19.241 -5.059  9.139   1.00 17.36 ? 184 LEU A CD2 1 
ATOM   1514 N  N   . LEU A 1 184 ? -22.383 -4.487  13.780  1.00 10.66 ? 185 LEU A N   1 
ATOM   1515 C  CA  . LEU A 1 184 ? -22.513 -4.492  15.279  1.00 10.09 ? 185 LEU A CA  1 
ATOM   1516 C  C   . LEU A 1 184 ? -23.267 -5.733  15.752  1.00 12.70 ? 185 LEU A C   1 
ATOM   1517 O  O   . LEU A 1 184 ? -24.348 -6.073  15.199  1.00 14.29 ? 185 LEU A O   1 
ATOM   1518 C  CB  . LEU A 1 184 ? -23.269 -3.217  15.818  1.00 9.01  ? 185 LEU A CB  1 
ATOM   1519 C  CG  . LEU A 1 184 ? -22.667 -1.878  15.399  1.00 9.31  ? 185 LEU A CG  1 
ATOM   1520 C  CD1 . LEU A 1 184 ? -23.493 -0.618  15.852  1.00 10.73 ? 185 LEU A CD1 1 
ATOM   1521 C  CD2 . LEU A 1 184 ? -21.185 -1.796  15.946  1.00 11.44 ? 185 LEU A CD2 1 
ATOM   1522 N  N   . PRO A 1 185 ? -22.825 -6.319  16.868  1.00 12.83 ? 186 PRO A N   1 
ATOM   1523 C  CA  . PRO A 1 185 ? -23.587 -7.445  17.385  1.00 13.13 ? 186 PRO A CA  1 
ATOM   1524 C  C   . PRO A 1 185 ? -24.944 -6.958  18.013  1.00 13.98 ? 186 PRO A C   1 
ATOM   1525 O  O   . PRO A 1 185 ? -25.138 -5.722  18.114  1.00 14.27 ? 186 PRO A O   1 
ATOM   1526 C  CB  . PRO A 1 185 ? -22.644 -8.044  18.447  1.00 13.88 ? 186 PRO A CB  1 
ATOM   1527 C  CG  . PRO A 1 185 ? -21.880 -6.829  18.973  1.00 10.42 ? 186 PRO A CG  1 
ATOM   1528 C  CD  . PRO A 1 185 ? -21.696 -5.899  17.718  1.00 10.46 ? 186 PRO A CD  1 
ATOM   1529 N  N   . GLU A 1 186 ? -25.806 -7.876  18.550  1.00 12.16 ? 187 GLU A N   1 
ATOM   1530 C  CA  . GLU A 1 186 ? -27.038 -7.409  19.238  1.00 14.46 ? 187 GLU A CA  1 
ATOM   1531 C  C   . GLU A 1 186 ? -26.769 -6.643  20.519  1.00 13.57 ? 187 GLU A C   1 
ATOM   1532 O  O   . GLU A 1 186 ? -27.368 -5.587  20.749  1.00 16.67 ? 187 GLU A O   1 
ATOM   1533 C  CB  . GLU A 1 186 ? -27.914 -8.627  19.629  1.00 14.78 ? 187 GLU A CB  1 
ATOM   1534 C  CG  . GLU A 1 186 ? -28.496 -9.353  18.528  1.00 20.29 ? 187 GLU A CG  1 
ATOM   1535 C  CD  . GLU A 1 186 ? -29.263 -10.627 19.085  1.00 16.77 ? 187 GLU A CD  1 
ATOM   1536 O  OE1 . GLU A 1 186 ? -29.391 -10.773 20.321  1.00 20.29 ? 187 GLU A OE1 1 
ATOM   1537 O  OE2 . GLU A 1 186 ? -29.643 -11.472 18.280  1.00 28.52 ? 187 GLU A OE2 1 
ATOM   1538 N  N   . SER A 1 187 ? -25.881 -7.146  21.402  1.00 13.56 ? 188 SER A N   1 
ATOM   1539 C  CA  . SER A 1 187 ? -25.710 -6.571  22.711  1.00 14.03 ? 188 SER A CA  1 
ATOM   1540 C  C   . SER A 1 187 ? -24.590 -5.530  22.649  1.00 13.30 ? 188 SER A C   1 
ATOM   1541 O  O   . SER A 1 187 ? -23.575 -5.803  21.983  1.00 14.58 ? 188 SER A O   1 
ATOM   1542 C  CB  . SER A 1 187 ? -25.329 -7.641  23.730  1.00 13.42 ? 188 SER A CB  1 
ATOM   1543 O  OG  . SER A 1 187 ? -25.080 -7.076  24.995  1.00 14.29 ? 188 SER A OG  1 
ATOM   1544 N  N   . LEU A 1 188 ? -24.762 -4.433  23.359  1.00 12.19 ? 189 LEU A N   1 
ATOM   1545 C  CA  . LEU A 1 188 ? -23.633 -3.437  23.584  1.00 13.92 ? 189 LEU A CA  1 
ATOM   1546 C  C   . LEU A 1 188 ? -22.980 -3.571  24.966  1.00 13.09 ? 189 LEU A C   1 
ATOM   1547 O  O   . LEU A 1 188 ? -22.349 -2.600  25.460  1.00 15.14 ? 189 LEU A O   1 
ATOM   1548 C  CB  . LEU A 1 188 ? -24.115 -1.987  23.264  1.00 12.69 ? 189 LEU A CB  1 
ATOM   1549 C  CG  . LEU A 1 188 ? -24.547 -1.621  21.856  1.00 16.61 ? 189 LEU A CG  1 
ATOM   1550 C  CD1 . LEU A 1 188 ? -25.003 -0.163  21.839  1.00 17.99 ? 189 LEU A CD1 1 
ATOM   1551 C  CD2 . LEU A 1 188 ? -23.436 -1.897  20.756  1.00 13.53 ? 189 LEU A CD2 1 
ATOM   1552 N  N   . ASP A 1 189 ? -23.158 -4.722  25.622  1.00 13.88 ? 190 ASP A N   1 
ATOM   1553 C  CA  . ASP A 1 189 ? -22.457 -5.042  26.881  1.00 12.46 ? 190 ASP A CA  1 
ATOM   1554 C  C   . ASP A 1 189 ? -20.939 -4.972  26.548  1.00 11.89 ? 190 ASP A C   1 
ATOM   1555 O  O   . ASP A 1 189 ? -20.500 -5.401  25.439  1.00 11.85 ? 190 ASP A O   1 
ATOM   1556 C  CB  . ASP A 1 189 ? -22.782 -6.432  27.368  1.00 13.61 ? 190 ASP A CB  1 
ATOM   1557 C  CG  . ASP A 1 189 ? -24.137 -6.511  28.120  1.00 18.25 ? 190 ASP A CG  1 
ATOM   1558 O  OD1 . ASP A 1 189 ? -24.769 -5.468  28.311  1.00 22.59 ? 190 ASP A OD1 1 
ATOM   1559 O  OD2 . ASP A 1 189 ? -24.493 -7.629  28.451  1.00 26.60 ? 190 ASP A OD2 1 
ATOM   1560 N  N   . TYR A 1 190 ? -20.195 -4.318  27.450  1.00 9.81  ? 191 TYR A N   1 
ATOM   1561 C  CA  . TYR A 1 190 ? -18.751 -4.067  27.117  1.00 10.01 ? 191 TYR A CA  1 
ATOM   1562 C  C   . TYR A 1 190 ? -17.843 -4.159  28.337  1.00 9.72  ? 191 TYR A C   1 
ATOM   1563 O  O   . TYR A 1 190 ? -18.276 -4.011  29.518  1.00 9.19  ? 191 TYR A O   1 
ATOM   1564 C  CB  . TYR A 1 190 ? -18.574 -2.696  26.397  1.00 10.45 ? 191 TYR A CB  1 
ATOM   1565 C  CG  . TYR A 1 190 ? -18.955 -1.533  27.285  1.00 8.62  ? 191 TYR A CG  1 
ATOM   1566 C  CD1 . TYR A 1 190 ? -18.006 -0.956  28.173  1.00 8.19  ? 191 TYR A CD1 1 
ATOM   1567 C  CD2 . TYR A 1 190 ? -20.287 -1.022  27.235  1.00 8.23  ? 191 TYR A CD2 1 
ATOM   1568 C  CE1 . TYR A 1 190 ? -18.409 0.098   29.083  1.00 12.23 ? 191 TYR A CE1 1 
ATOM   1569 C  CE2 . TYR A 1 190 ? -20.678 0.015   28.099  1.00 12.21 ? 191 TYR A CE2 1 
ATOM   1570 C  CZ  . TYR A 1 190 ? -19.707 0.586   29.017  1.00 11.88 ? 191 TYR A CZ  1 
ATOM   1571 O  OH  . TYR A 1 190 ? -20.011 1.627   29.863  1.00 13.36 ? 191 TYR A OH  1 
ATOM   1572 N  N   . TRP A 1 191 ? -16.537 -4.341  28.059  1.00 7.05  ? 192 TRP A N   1 
ATOM   1573 C  CA  . TRP A 1 191 ? -15.455 -4.069  29.021  1.00 6.93  ? 192 TRP A CA  1 
ATOM   1574 C  C   . TRP A 1 191 ? -14.706 -2.796  28.613  1.00 7.82  ? 192 TRP A C   1 
ATOM   1575 O  O   . TRP A 1 191 ? -14.698 -2.422  27.423  1.00 8.27  ? 192 TRP A O   1 
ATOM   1576 C  CB  . TRP A 1 191 ? -14.410 -5.188  28.957  1.00 8.83  ? 192 TRP A CB  1 
ATOM   1577 C  CG  . TRP A 1 191 ? -14.965 -6.527  29.412  1.00 7.60  ? 192 TRP A CG  1 
ATOM   1578 C  CD1 . TRP A 1 191 ? -15.210 -6.966  30.709  1.00 9.95  ? 192 TRP A CD1 1 
ATOM   1579 C  CD2 . TRP A 1 191 ? -15.189 -7.634  28.567  1.00 7.33  ? 192 TRP A CD2 1 
ATOM   1580 N  NE1 . TRP A 1 191 ? -15.656 -8.302  30.659  1.00 12.55 ? 192 TRP A NE1 1 
ATOM   1581 C  CE2 . TRP A 1 191 ? -15.688 -8.712  29.361  1.00 11.82 ? 192 TRP A CE2 1 
ATOM   1582 C  CE3 . TRP A 1 191 ? -15.095 -7.812  27.179  1.00 9.01  ? 192 TRP A CE3 1 
ATOM   1583 C  CZ2 . TRP A 1 191 ? -15.976 -10.004 28.806  1.00 10.66 ? 192 TRP A CZ2 1 
ATOM   1584 C  CZ3 . TRP A 1 191 ? -15.423 -9.059  26.637  1.00 8.40  ? 192 TRP A CZ3 1 
ATOM   1585 C  CH2 . TRP A 1 191 ? -15.840 -10.149 27.448  1.00 11.50 ? 192 TRP A CH2 1 
ATOM   1586 N  N   . THR A 1 192 ? -14.148 -2.116  29.606  1.00 6.11  ? 193 THR A N   1 
ATOM   1587 C  CA  . THR A 1 192 ? -13.449 -0.810  29.280  1.00 8.18  ? 193 THR A CA  1 
ATOM   1588 C  C   . THR A 1 192 ? -12.233 -0.628  30.149  1.00 8.95  ? 193 THR A C   1 
ATOM   1589 O  O   . THR A 1 192 ? -12.205 -1.051  31.305  1.00 9.78  ? 193 THR A O   1 
ATOM   1590 C  CB  . THR A 1 192 ? -14.386 0.450   29.335  1.00 9.50  ? 193 THR A CB  1 
ATOM   1591 O  OG1 . THR A 1 192 ? -13.674 1.641   28.926  1.00 9.45  ? 193 THR A OG1 1 
ATOM   1592 C  CG2 . THR A 1 192 ? -14.886 0.714   30.825  1.00 10.48 ? 193 THR A CG2 1 
ATOM   1593 N  N   . TYR A 1 193 ? -11.153 -0.077  29.552  1.00 7.84  ? 194 TYR A N   1 
ATOM   1594 C  CA  . TYR A 1 193 ? -9.877  0.119   30.264  1.00 7.66  ? 194 TYR A CA  1 
ATOM   1595 C  C   . TYR A 1 193 ? -9.122  1.190   29.480  1.00 8.57  ? 194 TYR A C   1 
ATOM   1596 O  O   . TYR A 1 193 ? -9.405  1.386   28.281  1.00 7.24  ? 194 TYR A O   1 
ATOM   1597 C  CB  . TYR A 1 193 ? -9.054  -1.193  30.463  1.00 7.48  ? 194 TYR A CB  1 
ATOM   1598 C  CG  . TYR A 1 193 ? -8.369  -1.645  29.196  1.00 8.13  ? 194 TYR A CG  1 
ATOM   1599 C  CD1 . TYR A 1 193 ? -9.085  -2.331  28.200  1.00 7.38  ? 194 TYR A CD1 1 
ATOM   1600 C  CD2 . TYR A 1 193 ? -7.031  -1.286  28.967  1.00 7.82  ? 194 TYR A CD2 1 
ATOM   1601 C  CE1 . TYR A 1 193 ? -8.425  -2.717  26.990  1.00 6.81  ? 194 TYR A CE1 1 
ATOM   1602 C  CE2 . TYR A 1 193 ? -6.360  -1.619  27.747  1.00 7.98  ? 194 TYR A CE2 1 
ATOM   1603 C  CZ  . TYR A 1 193 ? -7.074  -2.305  26.791  1.00 6.62  ? 194 TYR A CZ  1 
ATOM   1604 O  OH  . TYR A 1 193 ? -6.384  -2.580  25.669  1.00 6.82  ? 194 TYR A OH  1 
ATOM   1605 N  N   . PRO A 1 194 ? -8.242  1.925   30.150  1.00 8.35  ? 195 PRO A N   1 
ATOM   1606 C  CA  . PRO A 1 194 ? -7.401  2.928   29.490  1.00 8.28  ? 195 PRO A CA  1 
ATOM   1607 C  C   . PRO A 1 194 ? -6.166  2.278   28.804  1.00 7.36  ? 195 PRO A C   1 
ATOM   1608 O  O   . PRO A 1 194 ? -5.468  1.501   29.489  1.00 8.10  ? 195 PRO A O   1 
ATOM   1609 C  CB  . PRO A 1 194 ? -6.915  3.821   30.659  1.00 10.89 ? 195 PRO A CB  1 
ATOM   1610 C  CG  . PRO A 1 194 ? -6.985  2.950   31.827  1.00 11.11 ? 195 PRO A CG  1 
ATOM   1611 C  CD  . PRO A 1 194 ? -8.031  1.933   31.624  1.00 9.25  ? 195 PRO A CD  1 
ATOM   1612 N  N   . GLY A 1 195 ? -5.923  2.595   27.538  1.00 5.96  ? 196 GLY A N   1 
ATOM   1613 C  CA  . GLY A 1 195 ? -4.792  1.946   26.803  1.00 7.23  ? 196 GLY A CA  1 
ATOM   1614 C  C   . GLY A 1 195 ? -4.246  2.796   25.700  1.00 8.27  ? 196 GLY A C   1 
ATOM   1615 O  O   . GLY A 1 195 ? -4.191  4.055   25.848  1.00 7.51  ? 196 GLY A O   1 
ATOM   1616 N  N   . SER A 1 196 ? -3.815  2.130   24.617  1.00 7.91  ? 197 SER A N   1 
ATOM   1617 C  CA  . SER A 1 196 ? -3.067  2.832   23.564  1.00 6.66  ? 197 SER A CA  1 
ATOM   1618 C  C   . SER A 1 196 ? -3.540  2.431   22.167  1.00 6.94  ? 197 SER A C   1 
ATOM   1619 O  O   . SER A 1 196 ? -4.230  1.411   22.038  1.00 6.67  ? 197 SER A O   1 
ATOM   1620 C  CB  . SER A 1 196 ? -1.583  2.461   23.592  1.00 9.24  ? 197 SER A CB  1 
ATOM   1621 O  OG  . SER A 1 196 ? -1.363  1.062   23.313  1.00 6.49  ? 197 SER A OG  1 
ATOM   1622 N  N   . LEU A 1 197 ? -3.006  3.129   21.162  1.00 6.68  ? 198 LEU A N   1 
ATOM   1623 C  CA  . LEU A 1 197 ? -3.021  2.553   19.773  1.00 7.09  ? 198 LEU A CA  1 
ATOM   1624 C  C   . LEU A 1 197 ? -2.224  1.230   19.830  1.00 6.83  ? 198 LEU A C   1 
ATOM   1625 O  O   . LEU A 1 197 ? -1.175  1.083   20.569  1.00 7.60  ? 198 LEU A O   1 
ATOM   1626 C  CB  . LEU A 1 197 ? -2.383  3.550   18.823  1.00 9.05  ? 198 LEU A CB  1 
ATOM   1627 C  CG  . LEU A 1 197 ? -3.009  4.937   18.714  1.00 11.03 ? 198 LEU A CG  1 
ATOM   1628 C  CD1 . LEU A 1 197 ? -2.179  5.781   17.709  1.00 15.09 ? 198 LEU A CD1 1 
ATOM   1629 C  CD2 . LEU A 1 197 ? -4.382  4.836   18.205  1.00 16.08 ? 198 LEU A CD2 1 
ATOM   1630 N  N   . THR A 1 198 ? -2.720  0.266   19.070  1.00 6.10  ? 199 THR A N   1 
ATOM   1631 C  CA  . THR A 1 198 ? -1.991  -1.029  19.019  1.00 6.35  ? 199 THR A CA  1 
ATOM   1632 C  C   . THR A 1 198 ? -0.947  -1.089  17.874  1.00 7.11  ? 199 THR A C   1 
ATOM   1633 O  O   . THR A 1 198 ? -0.363  -2.150  17.662  1.00 7.83  ? 199 THR A O   1 
ATOM   1634 C  CB  . THR A 1 198 ? -3.008  -2.167  18.858  1.00 6.34  ? 199 THR A CB  1 
ATOM   1635 O  OG1 . THR A 1 198 ? -3.623  -2.129  17.586  1.00 7.49  ? 199 THR A OG1 1 
ATOM   1636 C  CG2 . THR A 1 198 ? -3.985  -2.180  19.992  1.00 7.01  ? 199 THR A CG2 1 
ATOM   1637 N  N   . THR A 1 199 ? -0.873  -0.045  17.047  1.00 7.48  ? 200 THR A N   1 
ATOM   1638 C  CA  . THR A 1 199 ? 0.209   0.071   16.024  1.00 9.92  ? 200 THR A CA  1 
ATOM   1639 C  C   . THR A 1 199 ? 1.050   1.284   16.373  1.00 9.86  ? 200 THR A C   1 
ATOM   1640 O  O   . THR A 1 199 ? 0.533   2.271   16.935  1.00 8.58  ? 200 THR A O   1 
ATOM   1641 C  CB  . THR A 1 199 ? -0.372  0.275   14.627  1.00 11.09 ? 200 THR A CB  1 
ATOM   1642 O  OG1 . THR A 1 199 ? -1.302  1.394   14.632  1.00 14.60 ? 200 THR A OG1 1 
ATOM   1643 C  CG2 . THR A 1 199 ? -1.167  -1.026  14.199  1.00 9.50  ? 200 THR A CG2 1 
ATOM   1644 N  N   . PRO A 1 200 ? 2.317   1.262   15.922  1.00 10.78 ? 201 PRO A N   1 
ATOM   1645 C  CA  . PRO A 1 200 ? 3.069   2.523   15.955  1.00 10.68 ? 201 PRO A CA  1 
ATOM   1646 C  C   . PRO A 1 200 ? 2.201   3.711   15.388  1.00 9.58  ? 201 PRO A C   1 
ATOM   1647 O  O   . PRO A 1 200 ? 1.503   3.576   14.311  1.00 11.46 ? 201 PRO A O   1 
ATOM   1648 C  CB  . PRO A 1 200 ? 4.315   2.179   15.059  1.00 9.20  ? 201 PRO A CB  1 
ATOM   1649 C  CG  . PRO A 1 200 ? 4.555   0.692   15.284  1.00 11.05 ? 201 PRO A CG  1 
ATOM   1650 C  CD  . PRO A 1 200 ? 3.068   0.126   15.301  1.00 11.85 ? 201 PRO A CD  1 
ATOM   1651 N  N   . PRO A 1 201 ? 2.259   4.903   16.065  1.00 11.26 ? 202 PRO A N   1 
ATOM   1652 C  CA  . PRO A 1 201 ? 3.156   5.307   17.174  1.00 11.48 ? 202 PRO A CA  1 
ATOM   1653 C  C   . PRO A 1 201 ? 2.847   4.854   18.607  1.00 7.72  ? 202 PRO A C   1 
ATOM   1654 O  O   . PRO A 1 201 ? 3.499   5.273   19.611  1.00 11.03 ? 202 PRO A O   1 
ATOM   1655 C  CB  . PRO A 1 201 ? 3.157   6.846   17.062  1.00 10.29 ? 202 PRO A CB  1 
ATOM   1656 C  CG  . PRO A 1 201 ? 1.732   7.164   16.591  1.00 12.94 ? 202 PRO A CG  1 
ATOM   1657 C  CD  . PRO A 1 201 ? 1.470   6.056   15.551  1.00 11.93 ? 202 PRO A CD  1 
ATOM   1658 N  N   . LEU A 1 202 ? 1.828   3.947   18.743  1.00 8.65  ? 203 LEU A N   1 
ATOM   1659 C  CA  . LEU A 1 202 ? 1.585   3.340   20.047  1.00 7.13  ? 203 LEU A CA  1 
ATOM   1660 C  C   . LEU A 1 202 ? 1.184   4.353   21.173  1.00 6.71  ? 203 LEU A C   1 
ATOM   1661 O  O   . LEU A 1 202 ? 1.332   4.073   22.375  1.00 8.59  ? 203 LEU A O   1 
ATOM   1662 C  CB  . LEU A 1 202 ? 2.733   2.396   20.551  1.00 8.42  ? 203 LEU A CB  1 
ATOM   1663 C  CG  . LEU A 1 202 ? 3.107   1.250   19.580  1.00 7.74  ? 203 LEU A CG  1 
ATOM   1664 C  CD1 . LEU A 1 202 ? 4.286   0.512   20.267  1.00 8.74  ? 203 LEU A CD1 1 
ATOM   1665 C  CD2 . LEU A 1 202 ? 1.902   0.253   19.437  1.00 10.50 ? 203 LEU A CD2 1 
ATOM   1666 N  N   . LEU A 1 203 ? 0.592   5.472   20.745  1.00 8.39  ? 204 LEU A N   1 
ATOM   1667 C  CA  . LEU A 1 203 ? 0.310   6.589   21.694  1.00 9.33  ? 204 LEU A CA  1 
ATOM   1668 C  C   . LEU A 1 203 ? -0.713  6.150   22.741  1.00 9.29  ? 204 LEU A C   1 
ATOM   1669 O  O   . LEU A 1 203 ? -1.694  5.423   22.394  1.00 7.85  ? 204 LEU A O   1 
ATOM   1670 C  CB  . LEU A 1 203 ? -0.147  7.832   20.905  1.00 9.17  ? 204 LEU A CB  1 
ATOM   1671 C  CG  . LEU A 1 203 ? 0.927   8.382   19.948  1.00 11.59 ? 204 LEU A CG  1 
ATOM   1672 C  CD1 . LEU A 1 203 ? 0.313   9.442   18.996  1.00 15.28 ? 204 LEU A CD1 1 
ATOM   1673 C  CD2 . LEU A 1 203 ? 2.075   8.953   20.828  1.00 16.07 ? 204 LEU A CD2 1 
ATOM   1674 N  N   . GLU A 1 204 ? -0.502  6.551   24.004  1.00 8.84  ? 205 GLU A N   1 
ATOM   1675 C  CA  . GLU A 1 204 ? -1.361  6.213   25.092  1.00 9.76  ? 205 GLU A CA  1 
ATOM   1676 C  C   . GLU A 1 204 ? -2.549  7.184   25.215  1.00 11.54 ? 205 GLU A C   1 
ATOM   1677 O  O   . GLU A 1 204 ? -2.646  7.983   26.167  1.00 11.19 ? 205 GLU A O   1 
ATOM   1678 C  CB  . GLU A 1 204 ? -0.543  6.126   26.394  1.00 12.14 ? 205 GLU A CB  1 
ATOM   1679 C  CG  . GLU A 1 204 ? 0.346   4.853   26.254  1.00 13.53 ? 205 GLU A CG  1 
ATOM   1680 C  CD  . GLU A 1 204 ? 1.309   4.640   27.375  1.00 15.94 ? 205 GLU A CD  1 
ATOM   1681 O  OE1 . GLU A 1 204 ? 1.584   5.613   28.097  1.00 15.21 ? 205 GLU A OE1 1 
ATOM   1682 O  OE2 . GLU A 1 204 ? 1.738   3.475   27.552  1.00 12.12 ? 205 GLU A OE2 1 
ATOM   1683 N  N   . CYS A 1 205 ? -3.420  7.111   24.213  1.00 6.47  ? 206 CYS A N   1 
ATOM   1684 C  CA  . CYS A 1 205 ? -4.508  8.125   24.069  1.00 7.21  ? 206 CYS A CA  1 
ATOM   1685 C  C   . CYS A 1 205 ? -5.899  7.504   23.942  1.00 7.09  ? 206 CYS A C   1 
ATOM   1686 O  O   . CYS A 1 205 ? -6.838  8.202   23.562  1.00 8.10  ? 206 CYS A O   1 
ATOM   1687 C  CB  . CYS A 1 205 ? -4.230  8.962   22.858  1.00 5.22  ? 206 CYS A CB  1 
ATOM   1688 S  SG  . CYS A 1 205 ? -4.191  7.961   21.283  1.00 9.73  ? 206 CYS A SG  1 
ATOM   1689 N  N   . VAL A 1 206 ? -6.007  6.225   24.274  1.00 5.89  ? 207 VAL A N   1 
ATOM   1690 C  CA  . VAL A 1 206 ? -7.256  5.435   23.919  1.00 4.72  ? 207 VAL A CA  1 
ATOM   1691 C  C   . VAL A 1 206 ? -8.050  4.998   25.138  1.00 5.49  ? 207 VAL A C   1 
ATOM   1692 O  O   . VAL A 1 206 ? -7.512  4.349   26.053  1.00 7.80  ? 207 VAL A O   1 
ATOM   1693 C  CB  . VAL A 1 206 ? -6.931  4.130   23.093  1.00 5.48  ? 207 VAL A CB  1 
ATOM   1694 C  CG1 . VAL A 1 206 ? -8.303  3.478   22.717  1.00 5.66  ? 207 VAL A CG1 1 
ATOM   1695 C  CG2 . VAL A 1 206 ? -6.142  4.523   21.750  1.00 8.56  ? 207 VAL A CG2 1 
ATOM   1696 N  N   . THR A 1 207 ? -9.346  5.297   25.155  1.00 6.42  ? 208 THR A N   1 
ATOM   1697 C  CA  . THR A 1 207 ? -10.256 4.608   26.084  1.00 6.27  ? 208 THR A CA  1 
ATOM   1698 C  C   . THR A 1 207 ? -10.799 3.438   25.288  1.00 6.39  ? 208 THR A C   1 
ATOM   1699 O  O   . THR A 1 207 ? -11.462 3.641   24.258  1.00 5.82  ? 208 THR A O   1 
ATOM   1700 C  CB  . THR A 1 207 ? -11.454 5.537   26.593  1.00 8.50  ? 208 THR A CB  1 
ATOM   1701 O  OG1 . THR A 1 207 ? -10.887 6.670   27.286  1.00 7.57  ? 208 THR A OG1 1 
ATOM   1702 C  CG2 . THR A 1 207 ? -12.353 4.716   27.469  1.00 7.22  ? 208 THR A CG2 1 
ATOM   1703 N  N   . TRP A 1 208 ? -10.445 2.249   25.686  1.00 5.64  ? 209 TRP A N   1 
ATOM   1704 C  CA  . TRP A 1 208 ? -10.883 1.042   24.945  1.00 5.39  ? 209 TRP A CA  1 
ATOM   1705 C  C   . TRP A 1 208 ? -12.279 0.595   25.434  1.00 7.92  ? 209 TRP A C   1 
ATOM   1706 O  O   . TRP A 1 208 ? -12.519 0.560   26.651  1.00 7.72  ? 209 TRP A O   1 
ATOM   1707 C  CB  . TRP A 1 208 ? -9.871  -0.116  25.190  1.00 7.13  ? 209 TRP A CB  1 
ATOM   1708 C  CG  . TRP A 1 208 ? -8.771  0.022   24.211  1.00 7.46  ? 209 TRP A CG  1 
ATOM   1709 C  CD1 . TRP A 1 208 ? -7.473  0.603   24.394  1.00 6.01  ? 209 TRP A CD1 1 
ATOM   1710 C  CD2 . TRP A 1 208 ? -8.821  -0.413  22.841  1.00 7.78  ? 209 TRP A CD2 1 
ATOM   1711 N  NE1 . TRP A 1 208 ? -6.792  0.576   23.187  1.00 6.11  ? 209 TRP A NE1 1 
ATOM   1712 C  CE2 . TRP A 1 208 ? -7.537  -0.081  22.239  1.00 6.92  ? 209 TRP A CE2 1 
ATOM   1713 C  CE3 . TRP A 1 208 ? -9.817  -1.027  22.038  1.00 6.49  ? 209 TRP A CE3 1 
ATOM   1714 C  CZ2 . TRP A 1 208 ? -7.257  -0.259  20.883  1.00 7.51  ? 209 TRP A CZ2 1 
ATOM   1715 C  CZ3 . TRP A 1 208 ? -9.501  -1.324  20.671  1.00 6.43  ? 209 TRP A CZ3 1 
ATOM   1716 C  CH2 . TRP A 1 208 ? -8.212  -0.932  20.086  1.00 6.99  ? 209 TRP A CH2 1 
ATOM   1717 N  N   . ILE A 1 209 ? -13.130 0.323   24.458  1.00 6.76  ? 210 ILE A N   1 
ATOM   1718 C  CA  . ILE A 1 209 ? -14.468 -0.199  24.775  1.00 7.03  ? 210 ILE A CA  1 
ATOM   1719 C  C   . ILE A 1 209 ? -14.533 -1.512  23.960  1.00 8.02  ? 210 ILE A C   1 
ATOM   1720 O  O   . ILE A 1 209 ? -14.687 -1.424  22.774  1.00 5.79  ? 210 ILE A O   1 
ATOM   1721 C  CB  . ILE A 1 209 ? -15.561 0.846   24.404  1.00 6.94  ? 210 ILE A CB  1 
ATOM   1722 C  CG1 . ILE A 1 209 ? -15.289 2.128   25.221  1.00 9.54  ? 210 ILE A CG1 1 
ATOM   1723 C  CG2 . ILE A 1 209 ? -17.034 0.217   24.674  1.00 8.10  ? 210 ILE A CG2 1 
ATOM   1724 C  CD1 . ILE A 1 209 ? -16.077 3.340   24.736  1.00 13.83 ? 210 ILE A CD1 1 
ATOM   1725 N  N   . VAL A 1 210 ? -14.420 -2.669  24.602  1.00 6.14  ? 211 VAL A N   1 
ATOM   1726 C  CA  . VAL A 1 210 ? -14.486 -3.937  23.882  1.00 5.87  ? 211 VAL A CA  1 
ATOM   1727 C  C   . VAL A 1 210 ? -15.808 -4.653  24.143  1.00 5.51  ? 211 VAL A C   1 
ATOM   1728 O  O   . VAL A 1 210 ? -16.137 -4.958  25.289  1.00 7.10  ? 211 VAL A O   1 
ATOM   1729 C  CB  . VAL A 1 210 ? -13.324 -4.869  24.272  1.00 5.97  ? 211 VAL A CB  1 
ATOM   1730 C  CG1 . VAL A 1 210 ? -13.409 -6.176  23.498  1.00 6.48  ? 211 VAL A CG1 1 
ATOM   1731 C  CG2 . VAL A 1 210 ? -11.989 -4.182  24.027  1.00 6.39  ? 211 VAL A CG2 1 
ATOM   1732 N  N   . LEU A 1 211 ? -16.565 -4.920  23.082  1.00 7.00  ? 212 LEU A N   1 
ATOM   1733 C  CA  . LEU A 1 211 ? -17.859 -5.585  23.241  1.00 6.65  ? 212 LEU A CA  1 
ATOM   1734 C  C   . LEU A 1 211 ? -17.674 -7.060  23.626  1.00 7.19  ? 212 LEU A C   1 
ATOM   1735 O  O   . LEU A 1 211 ? -16.833 -7.787  23.068  1.00 9.30  ? 212 LEU A O   1 
ATOM   1736 C  CB  . LEU A 1 211 ? -18.645 -5.470  21.930  1.00 7.25  ? 212 LEU A CB  1 
ATOM   1737 C  CG  . LEU A 1 211 ? -19.057 -4.065  21.487  1.00 8.57  ? 212 LEU A CG  1 
ATOM   1738 C  CD1 . LEU A 1 211 ? -20.163 -4.123  20.331  1.00 9.34  ? 212 LEU A CD1 1 
ATOM   1739 C  CD2 . LEU A 1 211 ? -19.535 -3.163  22.698  1.00 6.58  ? 212 LEU A CD2 1 
ATOM   1740 N  N   . LYS A 1 212 ? -18.556 -7.509  24.551  1.00 7.86  ? 213 LYS A N   1 
ATOM   1741 C  CA  . LYS A 1 212 ? -18.520 -8.942  24.945  1.00 7.31  ? 213 LYS A CA  1 
ATOM   1742 C  C   . LYS A 1 212 ? -19.002 -9.908  23.887  1.00 8.17  ? 213 LYS A C   1 
ATOM   1743 O  O   . LYS A 1 212 ? -18.491 -11.043 23.780  1.00 11.03 ? 213 LYS A O   1 
ATOM   1744 C  CB  . LYS A 1 212 ? -19.283 -9.110  26.283  1.00 9.81  ? 213 LYS A CB  1 
ATOM   1745 C  CG  . LYS A 1 212 ? -19.530 -10.608 26.606  1.00 14.76 ? 213 LYS A CG  1 
ATOM   1746 C  CD  . LYS A 1 212 ? -19.861 -10.956 28.002  1.00 21.83 ? 213 LYS A CD  1 
ATOM   1747 C  CE  . LYS A 1 212 ? -21.366 -11.110 28.215  1.00 32.07 ? 213 LYS A CE  1 
ATOM   1748 N  NZ  . LYS A 1 212 ? -21.580 -11.900 29.534  1.00 32.69 ? 213 LYS A NZ  1 
ATOM   1749 N  N   . GLU A 1 213 ? -19.964 -9.484  23.088  1.00 9.21  ? 214 GLU A N   1 
ATOM   1750 C  CA  . GLU A 1 213 ? -20.561 -10.360 22.081  1.00 10.54 ? 214 GLU A CA  1 
ATOM   1751 C  C   . GLU A 1 213 ? -19.817 -10.252 20.760  1.00 8.21  ? 214 GLU A C   1 
ATOM   1752 O  O   . GLU A 1 213 ? -19.770 -9.172  20.194  1.00 8.46  ? 214 GLU A O   1 
ATOM   1753 C  CB  . GLU A 1 213 ? -22.026 -10.002 21.870  1.00 11.21 ? 214 GLU A CB  1 
ATOM   1754 C  CG  . GLU A 1 213 ? -22.701 -10.949 20.828  1.00 12.69 ? 214 GLU A CG  1 
ATOM   1755 C  CD  . GLU A 1 213 ? -24.230 -10.714 20.664  1.00 16.98 ? 214 GLU A CD  1 
ATOM   1756 O  OE1 . GLU A 1 213 ? -24.810 -9.970  21.460  1.00 16.45 ? 214 GLU A OE1 1 
ATOM   1757 O  OE2 . GLU A 1 213 ? -24.790 -11.303 19.713  1.00 28.06 ? 214 GLU A OE2 1 
ATOM   1758 N  N   . PRO A 1 214 ? -19.267 -11.362 20.263  1.00 9.36  ? 215 PRO A N   1 
ATOM   1759 C  CA  . PRO A 1 214 ? -18.587 -11.314 18.965  1.00 9.27  ? 215 PRO A CA  1 
ATOM   1760 C  C   . PRO A 1 214 ? -19.632 -11.338 17.836  1.00 10.39 ? 215 PRO A C   1 
ATOM   1761 O  O   . PRO A 1 214 ? -20.852 -11.683 18.089  1.00 12.89 ? 215 PRO A O   1 
ATOM   1762 C  CB  . PRO A 1 214 ? -17.850 -12.677 18.847  1.00 9.92  ? 215 PRO A CB  1 
ATOM   1763 C  CG  . PRO A 1 214 ? -18.746 -13.604 19.725  1.00 14.58 ? 215 PRO A CG  1 
ATOM   1764 C  CD  . PRO A 1 214 ? -19.275 -12.719 20.879  1.00 10.35 ? 215 PRO A CD  1 
ATOM   1765 N  N   . ILE A 1 215 ? -19.196 -10.862 16.694  1.00 8.63  ? 216 ILE A N   1 
ATOM   1766 C  CA  . ILE A 1 215 ? -19.990 -11.107 15.483  1.00 9.45  ? 216 ILE A CA  1 
ATOM   1767 C  C   . ILE A 1 215 ? -19.480 -12.370 14.781  1.00 10.13 ? 216 ILE A C   1 
ATOM   1768 O  O   . ILE A 1 215 ? -18.292 -12.724 14.909  1.00 10.71 ? 216 ILE A O   1 
ATOM   1769 C  CB  . ILE A 1 215 ? -20.036 -9.891  14.535  1.00 9.94  ? 216 ILE A CB  1 
ATOM   1770 C  CG1 . ILE A 1 215 ? -18.604 -9.518  14.033  1.00 8.54  ? 216 ILE A CG1 1 
ATOM   1771 C  CG2 . ILE A 1 215 ? -20.826 -8.665  15.191  1.00 11.77 ? 216 ILE A CG2 1 
ATOM   1772 C  CD1 . ILE A 1 215 ? -18.651 -8.490  12.800  1.00 8.15  ? 216 ILE A CD1 1 
ATOM   1773 N  N   A SER A 1 216 ? -20.382 -13.003 14.001  0.50 10.46 ? 217 SER A N   1 
ATOM   1774 N  N   B SER A 1 216 ? -20.357 -13.045 14.025  0.50 10.48 ? 217 SER A N   1 
ATOM   1775 C  CA  A SER A 1 216 ? -20.037 -14.195 13.176  0.50 10.35 ? 217 SER A CA  1 
ATOM   1776 C  CA  B SER A 1 216 ? -19.890 -14.215 13.242  0.50 9.58  ? 217 SER A CA  1 
ATOM   1777 C  C   A SER A 1 216 ? -19.753 -13.734 11.755  0.50 9.94  ? 217 SER A C   1 
ATOM   1778 C  C   B SER A 1 216 ? -19.735 -13.765 11.808  0.50 9.75  ? 217 SER A C   1 
ATOM   1779 O  O   A SER A 1 216 ? -20.523 -12.958 11.161  0.50 11.24 ? 217 SER A O   1 
ATOM   1780 O  O   B SER A 1 216 ? -20.577 -13.038 11.269  0.50 11.07 ? 217 SER A O   1 
ATOM   1781 C  CB  A SER A 1 216 ? -21.244 -15.189 13.116  0.50 11.77 ? 217 SER A CB  1 
ATOM   1782 C  CB  B SER A 1 216 ? -20.918 -15.352 13.260  0.50 11.99 ? 217 SER A CB  1 
ATOM   1783 O  OG  A SER A 1 216 ? -20.867 -16.367 12.419  0.50 14.08 ? 217 SER A OG  1 
ATOM   1784 O  OG  B SER A 1 216 ? -20.998 -15.991 14.505  0.50 11.60 ? 217 SER A OG  1 
ATOM   1785 N  N   . VAL A 1 217 ? -18.653 -14.220 11.192  1.00 9.16  ? 218 VAL A N   1 
ATOM   1786 C  CA  . VAL A 1 217 ? -18.343 -13.975 9.787   1.00 9.40  ? 218 VAL A CA  1 
ATOM   1787 C  C   . VAL A 1 217 ? -18.057 -15.329 9.132   1.00 8.81  ? 218 VAL A C   1 
ATOM   1788 O  O   . VAL A 1 217 ? -17.617 -16.286 9.820   1.00 11.33 ? 218 VAL A O   1 
ATOM   1789 C  CB  . VAL A 1 217 ? -17.121 -13.006 9.577   1.00 9.86  ? 218 VAL A CB  1 
ATOM   1790 C  CG1 . VAL A 1 217 ? -17.493 -11.681 10.215  1.00 10.48 ? 218 VAL A CG1 1 
ATOM   1791 C  CG2 . VAL A 1 217 ? -15.802 -13.592 10.103  1.00 10.00 ? 218 VAL A CG2 1 
ATOM   1792 N  N   . SER A 1 218 ? -18.297 -15.464 7.841   1.00 9.34  ? 219 SER A N   1 
ATOM   1793 C  CA  . SER A 1 218 ? -18.044 -16.781 7.266   1.00 10.10 ? 219 SER A CA  1 
ATOM   1794 C  C   . SER A 1 218 ? -16.548 -17.032 7.002   1.00 8.82  ? 219 SER A C   1 
ATOM   1795 O  O   . SER A 1 218 ? -15.716 -16.123 6.884   1.00 8.02  ? 219 SER A O   1 
ATOM   1796 C  CB  . SER A 1 218 ? -18.842 -16.936 5.959   1.00 10.35 ? 219 SER A CB  1 
ATOM   1797 O  OG  . SER A 1 218 ? -18.288 -16.117 4.953   1.00 12.75 ? 219 SER A OG  1 
ATOM   1798 N  N   A SER A 1 219 ? -16.213 -18.306 6.854   0.50 8.28  ? 220 SER A N   1 
ATOM   1799 N  N   B SER A 1 219 ? -16.201 -18.301 6.843   0.50 8.95  ? 220 SER A N   1 
ATOM   1800 C  CA  A SER A 1 219 ? -14.896 -18.734 6.418   0.50 10.26 ? 220 SER A CA  1 
ATOM   1801 C  CA  B SER A 1 219 ? -14.866 -18.685 6.419   0.50 11.43 ? 220 SER A CA  1 
ATOM   1802 C  C   A SER A 1 219 ? -14.475 -18.035 5.100   0.50 11.63 ? 220 SER A C   1 
ATOM   1803 C  C   B SER A 1 219 ? -14.473 -17.990 5.098   0.50 12.27 ? 220 SER A C   1 
ATOM   1804 O  O   A SER A 1 219 ? -13.329 -17.558 5.008   0.50 11.56 ? 220 SER A O   1 
ATOM   1805 O  O   B SER A 1 219 ? -13.342 -17.486 4.993   0.50 12.25 ? 220 SER A O   1 
ATOM   1806 C  CB  A SER A 1 219 ? -14.869 -20.293 6.313   0.50 11.08 ? 220 SER A CB  1 
ATOM   1807 C  CB  B SER A 1 219 ? -14.775 -20.223 6.289   0.50 12.93 ? 220 SER A CB  1 
ATOM   1808 O  OG  A SER A 1 219 ? -15.715 -20.784 5.295   0.50 9.84  ? 220 SER A OG  1 
ATOM   1809 O  OG  B SER A 1 219 ? -13.415 -20.612 6.270   0.50 15.37 ? 220 SER A OG  1 
ATOM   1810 N  N   . GLU A 1 220 ? -15.396 -17.963 4.110   1.00 11.39 ? 221 GLU A N   1 
ATOM   1811 C  CA  . GLU A 1 220 ? -15.162 -17.287 2.809   1.00 12.39 ? 221 GLU A CA  1 
ATOM   1812 C  C   . GLU A 1 220 ? -14.819 -15.758 3.013   1.00 11.15 ? 221 GLU A C   1 
ATOM   1813 O  O   . GLU A 1 220 ? -13.950 -15.228 2.323   1.00 10.49 ? 221 GLU A O   1 
ATOM   1814 C  CB  . GLU A 1 220 ? -16.358 -17.379 1.874   1.00 13.28 ? 221 GLU A CB  1 
ATOM   1815 C  CG  . GLU A 1 220 ? -16.666 -18.874 1.426   1.00 19.43 ? 221 GLU A CG  1 
ATOM   1816 C  CD  . GLU A 1 220 ? -17.449 -19.685 2.468   1.00 26.18 ? 221 GLU A CD  1 
ATOM   1817 O  OE1 . GLU A 1 220 ? -18.100 -19.155 3.431   1.00 20.53 ? 221 GLU A OE1 1 
ATOM   1818 O  OE2 . GLU A 1 220 ? -17.401 -20.943 2.308   1.00 28.94 ? 221 GLU A OE2 1 
ATOM   1819 N  N   . GLN A 1 221 ? -15.538 -15.111 3.929   1.00 11.51 ? 222 GLN A N   1 
ATOM   1820 C  CA  . GLN A 1 221 ? -15.321 -13.661 4.175   1.00 11.49 ? 222 GLN A CA  1 
ATOM   1821 C  C   . GLN A 1 221 ? -13.893 -13.452 4.703   1.00 12.04 ? 222 GLN A C   1 
ATOM   1822 O  O   . GLN A 1 221 ? -13.135 -12.633 4.209   1.00 10.07 ? 222 GLN A O   1 
ATOM   1823 C  CB  . GLN A 1 221 ? -16.366 -13.172 5.167   1.00 12.31 ? 222 GLN A CB  1 
ATOM   1824 C  CG  . GLN A 1 221 ? -17.719 -12.920 4.404   1.00 12.28 ? 222 GLN A CG  1 
ATOM   1825 C  CD  . GLN A 1 221 ? -18.819 -12.394 5.322   1.00 10.11 ? 222 GLN A CD  1 
ATOM   1826 O  OE1 . GLN A 1 221 ? -18.955 -12.844 6.453   1.00 10.67 ? 222 GLN A OE1 1 
ATOM   1827 N  NE2 . GLN A 1 221 ? -19.693 -11.555 4.779   1.00 10.45 ? 222 GLN A NE2 1 
ATOM   1828 N  N   . VAL A 1 222 ? -13.486 -14.225 5.739   1.00 10.63 ? 223 VAL A N   1 
ATOM   1829 C  CA  . VAL A 1 222 ? -12.113 -14.041 6.293   1.00 12.52 ? 223 VAL A CA  1 
ATOM   1830 C  C   . VAL A 1 222 ? -10.989 -14.545 5.341   1.00 11.54 ? 223 VAL A C   1 
ATOM   1831 O  O   . VAL A 1 222 ? -9.968  -13.901 5.225   1.00 11.66 ? 223 VAL A O   1 
ATOM   1832 C  CB  . VAL A 1 222 ? -12.064 -14.583 7.745   1.00 14.65 ? 223 VAL A CB  1 
ATOM   1833 C  CG1 . VAL A 1 222 ? -12.258 -16.029 7.706   1.00 17.03 ? 223 VAL A CG1 1 
ATOM   1834 C  CG2 . VAL A 1 222 ? -10.743 -14.085 8.454   1.00 13.57 ? 223 VAL A CG2 1 
ATOM   1835 N  N   . LEU A 1 223 ? -11.305 -15.542 4.516   1.00 13.41 ? 224 LEU A N   1 
ATOM   1836 C  CA  . LEU A 1 223 ? -10.385 -15.930 3.473   1.00 14.12 ? 224 LEU A CA  1 
ATOM   1837 C  C   . LEU A 1 223 ? -10.070 -14.783 2.517   1.00 15.38 ? 224 LEU A C   1 
ATOM   1838 O  O   . LEU A 1 223 ? -8.913  -14.647 2.129   1.00 15.57 ? 224 LEU A O   1 
ATOM   1839 C  CB  . LEU A 1 223 ? -10.818 -17.184 2.750   1.00 16.34 ? 224 LEU A CB  1 
ATOM   1840 C  CG  . LEU A 1 223 ? -9.536  -17.954 2.372   1.00 21.68 ? 224 LEU A CG  1 
ATOM   1841 C  CD1 . LEU A 1 223 ? -8.975  -18.722 3.524   1.00 23.43 ? 224 LEU A CD1 1 
ATOM   1842 C  CD2 . LEU A 1 223 ? -10.054 -19.001 1.302   1.00 26.24 ? 224 LEU A CD2 1 
ATOM   1843 N  N   . LYS A 1 224 ? -11.081 -13.989 2.172   1.00 12.81 ? 225 LYS A N   1 
ATOM   1844 C  CA  . LYS A 1 224 ? -10.833 -12.832 1.339   1.00 15.16 ? 225 LYS A CA  1 
ATOM   1845 C  C   . LYS A 1 224 ? -9.930  -11.775 2.015   1.00 13.62 ? 225 LYS A C   1 
ATOM   1846 O  O   . LYS A 1 224 ? -9.106  -11.153 1.324   1.00 12.11 ? 225 LYS A O   1 
ATOM   1847 C  CB  . LYS A 1 224 ? -12.144 -12.285 0.751   1.00 13.20 ? 225 LYS A CB  1 
ATOM   1848 C  CG  . LYS A 1 224 ? -12.787 -13.417 -0.180  1.00 18.59 ? 225 LYS A CG  1 
ATOM   1849 C  CD  . LYS A 1 224 ? -14.061 -12.994 -0.899  1.00 21.24 ? 225 LYS A CD  1 
ATOM   1850 C  CE  . LYS A 1 224 ? -14.748 -14.248 -1.627  1.00 26.55 ? 225 LYS A CE  1 
ATOM   1851 N  NZ  . LYS A 1 224 ? -15.935 -13.823 -2.437  1.00 31.04 ? 225 LYS A NZ  1 
ATOM   1852 N  N   . PHE A 1 225 ? -10.062 -11.550 3.346   1.00 10.86 ? 226 PHE A N   1 
ATOM   1853 C  CA  . PHE A 1 225 ? -9.080  -10.716 4.031   1.00 9.68  ? 226 PHE A CA  1 
ATOM   1854 C  C   . PHE A 1 225 ? -7.690  -11.206 3.815   1.00 9.73  ? 226 PHE A C   1 
ATOM   1855 O  O   . PHE A 1 225 ? -6.760  -10.407 3.642   1.00 9.84  ? 226 PHE A O   1 
ATOM   1856 C  CB  . PHE A 1 225 ? -9.265  -10.723 5.594   1.00 8.46  ? 226 PHE A CB  1 
ATOM   1857 C  CG  . PHE A 1 225 ? -10.489 -9.924  6.111   1.00 10.07 ? 226 PHE A CG  1 
ATOM   1858 C  CD1 . PHE A 1 225 ? -11.546 -9.487  5.300   1.00 12.92 ? 226 PHE A CD1 1 
ATOM   1859 C  CD2 . PHE A 1 225 ? -10.582 -9.708  7.530   1.00 13.15 ? 226 PHE A CD2 1 
ATOM   1860 C  CE1 . PHE A 1 225 ? -12.612 -8.782  5.865   1.00 13.17 ? 226 PHE A CE1 1 
ATOM   1861 C  CE2 . PHE A 1 225 ? -11.668 -9.066  8.110   1.00 13.90 ? 226 PHE A CE2 1 
ATOM   1862 C  CZ  . PHE A 1 225 ? -12.676 -8.567  7.278   1.00 13.57 ? 226 PHE A CZ  1 
ATOM   1863 N  N   . ARG A 1 226 ? -7.511  -12.527 3.857   1.00 9.11  ? 227 ARG A N   1 
ATOM   1864 C  CA  . ARG A 1 226 ? -6.143  -13.123 3.776   1.00 10.99 ? 227 ARG A CA  1 
ATOM   1865 C  C   . ARG A 1 226 ? -5.510  -13.140 2.385   1.00 10.73 ? 227 ARG A C   1 
ATOM   1866 O  O   . ARG A 1 226 ? -4.349  -13.529 2.231   1.00 13.23 ? 227 ARG A O   1 
ATOM   1867 C  CB  . ARG A 1 226 ? -6.124  -14.571 4.340   1.00 10.36 ? 227 ARG A CB  1 
ATOM   1868 C  CG  . ARG A 1 226 ? -6.637  -14.681 5.767   1.00 9.09  ? 227 ARG A CG  1 
ATOM   1869 C  CD  . ARG A 1 226 ? -6.537  -16.170 6.270   1.00 12.20 ? 227 ARG A CD  1 
ATOM   1870 N  NE  . ARG A 1 226 ? -7.116  -16.276 7.650   1.00 10.51 ? 227 ARG A NE  1 
ATOM   1871 C  CZ  . ARG A 1 226 ? -8.068  -17.148 8.042   1.00 12.83 ? 227 ARG A CZ  1 
ATOM   1872 N  NH1 . ARG A 1 226 ? -8.535  -18.108 7.168   1.00 12.57 ? 227 ARG A NH1 1 
ATOM   1873 N  NH2 . ARG A 1 226 ? -8.516  -17.092 9.304   1.00 15.03 ? 227 ARG A NH2 1 
ATOM   1874 N  N   . LYS A 1 227 ? -6.230  -12.612 1.433   1.00 12.38 ? 228 LYS A N   1 
ATOM   1875 C  CA  . LYS A 1 227 ? -5.746  -12.548 0.034   1.00 13.30 ? 228 LYS A CA  1 
ATOM   1876 C  C   . LYS A 1 227 ? -5.090  -11.193 -0.220  1.00 13.87 ? 228 LYS A C   1 
ATOM   1877 O  O   . LYS A 1 227 ? -4.328  -10.998 -1.196  1.00 13.89 ? 228 LYS A O   1 
ATOM   1878 C  CB  . LYS A 1 227 ? -6.943  -12.721 -0.919  1.00 15.06 ? 228 LYS A CB  1 
ATOM   1879 C  CG  . LYS A 1 227 ? -7.446  -14.168 -1.026  1.00 19.55 ? 228 LYS A CG  1 
ATOM   1880 C  CD  . LYS A 1 227 ? -8.247  -14.290 -2.287  1.00 27.57 ? 228 LYS A CD  1 
ATOM   1881 C  CE  . LYS A 1 227 ? -8.033  -15.677 -2.858  1.00 34.48 ? 228 LYS A CE  1 
ATOM   1882 N  NZ  . LYS A 1 227 ? -9.238  -16.559 -2.509  1.00 34.76 ? 228 LYS A NZ  1 
ATOM   1883 N  N   . LEU A 1 228 ? -5.339  -10.264 0.709   1.00 13.33 ? 229 LEU A N   1 
ATOM   1884 C  CA  . LEU A 1 228 ? -4.587  -8.985  0.638   1.00 12.70 ? 229 LEU A CA  1 
ATOM   1885 C  C   . LEU A 1 228 ? -3.082  -9.132  0.776   1.00 12.11 ? 229 LEU A C   1 
ATOM   1886 O  O   . LEU A 1 228 ? -2.578  -10.108 1.274   1.00 11.13 ? 229 LEU A O   1 
ATOM   1887 C  CB  . LEU A 1 228 ? -5.024  -8.080  1.784   1.00 10.14 ? 229 LEU A CB  1 
ATOM   1888 C  CG  . LEU A 1 228 ? -6.451  -7.604  1.591   1.00 9.67  ? 229 LEU A CG  1 
ATOM   1889 C  CD1 . LEU A 1 228 ? -6.923  -6.966  2.915   1.00 13.00 ? 229 LEU A CD1 1 
ATOM   1890 C  CD2 . LEU A 1 228 ? -6.524  -6.504  0.478   1.00 13.28 ? 229 LEU A CD2 1 
ATOM   1891 N  N   . ASN A 1 229 ? -2.388  -8.046  0.451   1.00 13.83 ? 230 ASN A N   1 
ATOM   1892 C  CA  . ASN A 1 229 ? -0.947  -8.059  0.436   1.00 13.52 ? 230 ASN A CA  1 
ATOM   1893 C  C   . ASN A 1 229 ? -0.402  -6.898  1.346   1.00 13.38 ? 230 ASN A C   1 
ATOM   1894 O  O   . ASN A 1 229 ? -0.922  -5.761  1.272   1.00 12.33 ? 230 ASN A O   1 
ATOM   1895 C  CB  . ASN A 1 229 ? -0.419  -7.823  -1.007  1.00 14.54 ? 230 ASN A CB  1 
ATOM   1896 C  CG  . ASN A 1 229 ? -0.496  -9.091  -1.925  1.00 16.78 ? 230 ASN A CG  1 
ATOM   1897 O  OD1 . ASN A 1 229 ? 0.056   -9.050  -3.034  1.00 20.47 ? 230 ASN A OD1 1 
ATOM   1898 N  ND2 . ASN A 1 229 ? -1.134  -10.169 -1.489  1.00 15.66 ? 230 ASN A ND2 1 
ATOM   1899 N  N   . PHE A 1 230 ? 0.683   -7.209  2.054   1.00 13.50 ? 231 PHE A N   1 
ATOM   1900 C  CA  . PHE A 1 230 ? 1.507   -6.195  2.864   1.00 14.82 ? 231 PHE A CA  1 
ATOM   1901 C  C   . PHE A 1 230 ? 2.378   -5.402  1.874   1.00 17.06 ? 231 PHE A C   1 
ATOM   1902 O  O   . PHE A 1 230 ? 2.685   -4.220  2.129   1.00 16.21 ? 231 PHE A O   1 
ATOM   1903 C  CB  . PHE A 1 230 ? 2.480   -6.828  3.784   1.00 15.61 ? 231 PHE A CB  1 
ATOM   1904 C  CG  . PHE A 1 230 ? 1.877   -7.390  5.086   1.00 14.46 ? 231 PHE A CG  1 
ATOM   1905 C  CD1 . PHE A 1 230 ? 1.057   -6.580  5.890   1.00 15.06 ? 231 PHE A CD1 1 
ATOM   1906 C  CD2 . PHE A 1 230 ? 2.209   -8.681  5.489   1.00 16.26 ? 231 PHE A CD2 1 
ATOM   1907 C  CE1 . PHE A 1 230 ? 0.560   -7.090  7.104   1.00 12.23 ? 231 PHE A CE1 1 
ATOM   1908 C  CE2 . PHE A 1 230 ? 1.727   -9.233  6.689   1.00 17.58 ? 231 PHE A CE2 1 
ATOM   1909 C  CZ  . PHE A 1 230 ? 0.898   -8.403  7.488   1.00 11.59 ? 231 PHE A CZ  1 
ATOM   1910 N  N   . ASN A 1 231 ? 2.819   -6.097  0.830   1.00 18.20 ? 232 ASN A N   1 
ATOM   1911 C  CA  . ASN A 1 231 ? 3.773   -5.458  -0.107  1.00 18.35 ? 232 ASN A CA  1 
ATOM   1912 C  C   . ASN A 1 231 ? 3.061   -4.528  -1.101  1.00 18.33 ? 232 ASN A C   1 
ATOM   1913 O  O   . ASN A 1 231 ? 1.823   -4.637  -1.349  1.00 15.59 ? 232 ASN A O   1 
ATOM   1914 C  CB  . ASN A 1 231 ? 4.473   -6.566  -0.853  1.00 18.85 ? 232 ASN A CB  1 
ATOM   1915 C  CG  . ASN A 1 231 ? 3.459   -7.438  -1.547  1.00 18.59 ? 232 ASN A CG  1 
ATOM   1916 O  OD1 . ASN A 1 231 ? 2.963   -8.373  -0.927  1.00 22.11 ? 232 ASN A OD1 1 
ATOM   1917 N  ND2 . ASN A 1 231 ? 3.133   -7.139  -2.843  1.00 20.84 ? 232 ASN A ND2 1 
ATOM   1918 N  N   . GLY A 1 232 ? 3.815   -3.620  -1.741  1.00 17.25 ? 233 GLY A N   1 
ATOM   1919 C  CA  . GLY A 1 232 ? 3.221   -2.839  -2.848  1.00 21.03 ? 233 GLY A CA  1 
ATOM   1920 C  C   . GLY A 1 232 ? 3.178   -3.604  -4.187  1.00 21.59 ? 233 GLY A C   1 
ATOM   1921 O  O   . GLY A 1 232 ? 3.897   -4.593  -4.354  1.00 23.65 ? 233 GLY A O   1 
ATOM   1922 N  N   . GLU A 1 233 ? 2.358   -3.117  -5.110  1.00 23.29 ? 234 GLU A N   1 
ATOM   1923 C  CA  . GLU A 1 233 ? 2.282   -3.636  -6.505  1.00 24.38 ? 234 GLU A CA  1 
ATOM   1924 C  C   . GLU A 1 233 ? 3.666   -3.741  -7.187  1.00 25.27 ? 234 GLU A C   1 
ATOM   1925 O  O   . GLU A 1 233 ? 4.469   -2.822  -7.153  1.00 24.31 ? 234 GLU A O   1 
ATOM   1926 C  CB  . GLU A 1 233 ? 1.334   -2.799  -7.357  1.00 23.51 ? 234 GLU A CB  1 
ATOM   1927 C  CG  . GLU A 1 233 ? 1.019   -3.416  -8.692  1.00 25.61 ? 234 GLU A CG  1 
ATOM   1928 C  CD  . GLU A 1 233 ? 0.130   -2.548  -9.520  1.00 29.26 ? 234 GLU A CD  1 
ATOM   1929 O  OE1 . GLU A 1 233 ? -0.186  -1.394  -9.086  1.00 28.98 ? 234 GLU A OE1 1 
ATOM   1930 O  OE2 . GLU A 1 233 ? -0.209  -2.996  -10.632 1.00 32.98 ? 234 GLU A OE2 1 
ATOM   1931 N  N   . GLY A 1 234 ? 3.936   -4.914  -7.746  1.00 26.25 ? 235 GLY A N   1 
ATOM   1932 C  CA  . GLY A 1 234 ? 5.225   -5.221  -8.327  1.00 28.01 ? 235 GLY A CA  1 
ATOM   1933 C  C   . GLY A 1 234 ? 6.357   -5.482  -7.370  1.00 29.18 ? 235 GLY A C   1 
ATOM   1934 O  O   . GLY A 1 234 ? 7.518   -5.292  -7.748  1.00 29.25 ? 235 GLY A O   1 
ATOM   1935 N  N   . GLU A 1 235 ? 6.052   -5.891  -6.118  1.00 28.87 ? 236 GLU A N   1 
ATOM   1936 C  CA  . GLU A 1 235 ? 7.056   -6.411  -5.150  1.00 29.42 ? 236 GLU A CA  1 
ATOM   1937 C  C   . GLU A 1 235 ? 6.673   -7.878  -4.837  1.00 28.16 ? 236 GLU A C   1 
ATOM   1938 O  O   . GLU A 1 235 ? 5.548   -8.275  -5.189  1.00 30.15 ? 236 GLU A O   1 
ATOM   1939 C  CB  . GLU A 1 235 ? 7.056   -5.580  -3.836  1.00 30.21 ? 236 GLU A CB  1 
ATOM   1940 C  CG  . GLU A 1 235 ? 7.593   -4.171  -3.993  1.00 31.36 ? 236 GLU A CG  1 
ATOM   1941 C  CD  . GLU A 1 235 ? 7.156   -3.214  -2.903  1.00 34.46 ? 236 GLU A CD  1 
ATOM   1942 O  OE1 . GLU A 1 235 ? 6.772   -3.665  -1.770  1.00 41.72 ? 236 GLU A OE1 1 
ATOM   1943 O  OE2 . GLU A 1 235 ? 7.211   -1.992  -3.173  1.00 37.29 ? 236 GLU A OE2 1 
ATOM   1944 N  N   . PRO A 1 236 ? 7.597   -8.685  -4.266  1.00 26.97 ? 237 PRO A N   1 
ATOM   1945 C  CA  . PRO A 1 236 ? 7.351   -10.102 -3.915  1.00 27.11 ? 237 PRO A CA  1 
ATOM   1946 C  C   . PRO A 1 236 ? 6.116   -10.158 -3.017  1.00 25.61 ? 237 PRO A C   1 
ATOM   1947 O  O   . PRO A 1 236 ? 5.906   -9.235  -2.203  1.00 24.92 ? 237 PRO A O   1 
ATOM   1948 C  CB  . PRO A 1 236 ? 8.631   -10.522 -3.168  1.00 26.97 ? 237 PRO A CB  1 
ATOM   1949 C  CG  . PRO A 1 236 ? 9.673   -9.623  -3.744  1.00 28.46 ? 237 PRO A CG  1 
ATOM   1950 C  CD  . PRO A 1 236 ? 8.991   -8.300  -3.942  1.00 27.60 ? 237 PRO A CD  1 
ATOM   1951 N  N   . GLU A 1 237 ? 5.259   -11.151 -3.266  1.00 23.10 ? 238 GLU A N   1 
ATOM   1952 C  CA  . GLU A 1 237 ? 3.981   -11.199 -2.555  1.00 20.58 ? 238 GLU A CA  1 
ATOM   1953 C  C   . GLU A 1 237 ? 4.227   -11.703 -1.132  1.00 18.78 ? 238 GLU A C   1 
ATOM   1954 O  O   . GLU A 1 237 ? 4.778   -12.746 -0.913  1.00 17.47 ? 238 GLU A O   1 
ATOM   1955 C  CB  . GLU A 1 237 ? 2.904   -12.064 -3.267  1.00 20.88 ? 238 GLU A CB  1 
ATOM   1956 C  CG  . GLU A 1 237 ? 1.504   -11.922 -2.645  1.00 20.39 ? 238 GLU A CG  1 
ATOM   1957 C  CD  . GLU A 1 237 ? 0.399   -12.747 -3.300  1.00 21.90 ? 238 GLU A CD  1 
ATOM   1958 O  OE1 . GLU A 1 237 ? 0.696   -13.814 -3.913  1.00 25.97 ? 238 GLU A OE1 1 
ATOM   1959 O  OE2 . GLU A 1 237 ? -0.778  -12.329 -3.245  1.00 17.29 ? 238 GLU A OE2 1 
ATOM   1960 N  N   . GLU A 1 238 ? 3.680   -10.940 -0.186  1.00 19.17 ? 239 GLU A N   1 
ATOM   1961 C  CA  . GLU A 1 238 ? 3.689   -11.257 1.231   1.00 19.65 ? 239 GLU A CA  1 
ATOM   1962 C  C   . GLU A 1 238 ? 2.211   -11.117 1.645   1.00 15.77 ? 239 GLU A C   1 
ATOM   1963 O  O   . GLU A 1 238 ? 1.670   -10.047 1.556   1.00 15.53 ? 239 GLU A O   1 
ATOM   1964 C  CB  . GLU A 1 238 ? 4.523   -10.227 2.000   1.00 18.76 ? 239 GLU A CB  1 
ATOM   1965 C  CG  . GLU A 1 238 ? 5.686   -9.645  1.266   1.00 25.66 ? 239 GLU A CG  1 
ATOM   1966 C  CD  . GLU A 1 238 ? 6.494   -8.670  2.153   1.00 27.92 ? 239 GLU A CD  1 
ATOM   1967 O  OE1 . GLU A 1 238 ? 5.868   -7.685  2.684   1.00 33.99 ? 239 GLU A OE1 1 
ATOM   1968 O  OE2 . GLU A 1 238 ? 7.754   -8.918  2.305   1.00 29.46 ? 239 GLU A OE2 1 
ATOM   1969 N  N   . LEU A 1 239 ? 1.521   -12.229 1.940   1.00 13.32 ? 240 LEU A N   1 
ATOM   1970 C  CA  . LEU A 1 239 ? 0.096   -12.111 2.231   1.00 12.53 ? 240 LEU A CA  1 
ATOM   1971 C  C   . LEU A 1 239 ? -0.073  -11.276 3.542   1.00 8.52  ? 240 LEU A C   1 
ATOM   1972 O  O   . LEU A 1 239 ? 0.685   -11.449 4.526   1.00 12.27 ? 240 LEU A O   1 
ATOM   1973 C  CB  . LEU A 1 239 ? -0.446  -13.506 2.496   1.00 11.95 ? 240 LEU A CB  1 
ATOM   1974 C  CG  . LEU A 1 239 ? -0.629  -14.411 1.249   1.00 10.75 ? 240 LEU A CG  1 
ATOM   1975 C  CD1 . LEU A 1 239 ? -1.349  -15.691 1.639   1.00 17.74 ? 240 LEU A CD1 1 
ATOM   1976 C  CD2 . LEU A 1 239 ? -1.357  -13.597 0.162   1.00 13.60 ? 240 LEU A CD2 1 
ATOM   1977 N  N   . MET A 1 240 ? -1.128  -10.483 3.548   1.00 11.83 ? 241 MET A N   1 
ATOM   1978 C  CA  . MET A 1 240 ? -1.506  -9.662  4.747   1.00 11.06 ? 241 MET A CA  1 
ATOM   1979 C  C   . MET A 1 240 ? -2.271  -10.586 5.721   1.00 10.71 ? 241 MET A C   1 
ATOM   1980 O  O   . MET A 1 240 ? -3.434  -10.757 5.565   1.00 10.29 ? 241 MET A O   1 
ATOM   1981 C  CB  . MET A 1 240 ? -2.306  -8.439  4.341   1.00 11.57 ? 241 MET A CB  1 
ATOM   1982 C  CG  . MET A 1 240 ? -2.710  -7.474  5.557   1.00 11.53 ? 241 MET A CG  1 
ATOM   1983 S  SD  . MET A 1 240 ? -3.616  -6.091  4.974   1.00 16.33 ? 241 MET A SD  1 
ATOM   1984 C  CE  . MET A 1 240 ? -2.351  -4.953  4.330   1.00 15.71 ? 241 MET A CE  1 
ATOM   1985 N  N   . VAL A 1 241 ? -1.501  -11.215 6.604   1.00 9.94  ? 242 VAL A N   1 
ATOM   1986 C  CA  . VAL A 1 241 ? -2.097  -12.061 7.646   1.00 10.01 ? 242 VAL A CA  1 
ATOM   1987 C  C   . VAL A 1 241 ? -1.303  -11.829 8.914   1.00 9.89  ? 242 VAL A C   1 
ATOM   1988 O  O   . VAL A 1 241 ? -0.073  -11.426 8.856   1.00 9.68  ? 242 VAL A O   1 
ATOM   1989 C  CB  . VAL A 1 241 ? -2.083  -13.605 7.280   1.00 9.66  ? 242 VAL A CB  1 
ATOM   1990 C  CG1 . VAL A 1 241 ? -2.944  -13.868 5.932   1.00 9.43  ? 242 VAL A CG1 1 
ATOM   1991 C  CG2 . VAL A 1 241 ? -0.627  -14.090 7.159   1.00 9.71  ? 242 VAL A CG2 1 
ATOM   1992 N  N   . ASP A 1 242 ? -1.942  -12.145 10.062  1.00 6.94  ? 243 ASP A N   1 
ATOM   1993 C  CA  . ASP A 1 242 ? -1.246  -11.984 11.328  1.00 8.13  ? 243 ASP A CA  1 
ATOM   1994 C  C   . ASP A 1 242 ? -0.723  -10.549 11.524  1.00 6.32  ? 243 ASP A C   1 
ATOM   1995 O  O   . ASP A 1 242 ? 0.387   -10.376 12.102  1.00 9.84  ? 243 ASP A O   1 
ATOM   1996 C  CB  . ASP A 1 242 ? -0.166  -13.020 11.637  1.00 9.28  ? 243 ASP A CB  1 
ATOM   1997 C  CG  . ASP A 1 242 ? -0.701  -14.449 11.692  1.00 12.23 ? 243 ASP A CG  1 
ATOM   1998 O  OD1 . ASP A 1 242 ? -1.754  -14.648 12.332  1.00 8.59  ? 243 ASP A OD1 1 
ATOM   1999 O  OD2 . ASP A 1 242 ? -0.108  -15.368 11.022  1.00 10.80 ? 243 ASP A OD2 1 
ATOM   2000 N  N   . ASN A 1 243 ? -1.619  -9.596  11.280  1.00 7.59  ? 244 ASN A N   1 
ATOM   2001 C  CA  . ASN A 1 243 ? -1.296  -8.173  11.515  1.00 6.06  ? 244 ASN A CA  1 
ATOM   2002 C  C   . ASN A 1 243 ? -1.916  -7.748  12.878  1.00 8.08  ? 244 ASN A C   1 
ATOM   2003 O  O   . ASN A 1 243 ? -2.601  -6.697  12.911  1.00 8.42  ? 244 ASN A O   1 
ATOM   2004 C  CB  . ASN A 1 243 ? -1.868  -7.296  10.391  1.00 9.13  ? 244 ASN A CB  1 
ATOM   2005 C  CG  . ASN A 1 243 ? -3.388  -7.473  10.149  1.00 9.79  ? 244 ASN A CG  1 
ATOM   2006 O  OD1 . ASN A 1 243 ? -4.024  -8.341  10.741  1.00 11.68 ? 244 ASN A OD1 1 
ATOM   2007 N  ND2 . ASN A 1 243 ? -4.008  -6.540  9.343   1.00 13.76 ? 244 ASN A ND2 1 
ATOM   2008 N  N   . TRP A 1 244 ? -1.686  -8.527  13.920  1.00 6.75  ? 245 TRP A N   1 
ATOM   2009 C  CA  . TRP A 1 244 ? -2.162  -8.268  15.301  1.00 7.82  ? 245 TRP A CA  1 
ATOM   2010 C  C   . TRP A 1 244 ? -0.958  -8.176  16.232  1.00 8.27  ? 245 TRP A C   1 
ATOM   2011 O  O   . TRP A 1 244 ? 0.082   -8.898  16.038  1.00 8.62  ? 245 TRP A O   1 
ATOM   2012 C  CB  . TRP A 1 244 ? -3.089  -9.426  15.766  1.00 7.49  ? 245 TRP A CB  1 
ATOM   2013 C  CG  . TRP A 1 244 ? -2.579  -10.797 15.583  1.00 6.91  ? 245 TRP A CG  1 
ATOM   2014 C  CD1 . TRP A 1 244 ? -2.764  -11.549 14.477  1.00 7.99  ? 245 TRP A CD1 1 
ATOM   2015 C  CD2 . TRP A 1 244 ? -2.073  -11.667 16.585  1.00 7.51  ? 245 TRP A CD2 1 
ATOM   2016 N  NE1 . TRP A 1 244 ? -2.243  -12.832 14.665  1.00 9.07  ? 245 TRP A NE1 1 
ATOM   2017 C  CE2 . TRP A 1 244 ? -1.832  -12.914 15.966  1.00 8.35  ? 245 TRP A CE2 1 
ATOM   2018 C  CE3 . TRP A 1 244 ? -1.757  -11.518 17.950  1.00 10.59 ? 245 TRP A CE3 1 
ATOM   2019 C  CZ2 . TRP A 1 244 ? -1.214  -13.997 16.650  1.00 8.69  ? 245 TRP A CZ2 1 
ATOM   2020 C  CZ3 . TRP A 1 244 ? -1.159  -12.614 18.630  1.00 7.42  ? 245 TRP A CZ3 1 
ATOM   2021 C  CH2 . TRP A 1 244 ? -0.952  -13.844 17.949  1.00 7.78  ? 245 TRP A CH2 1 
ATOM   2022 N  N   . ARG A 1 245 ? -1.036  -7.247  17.195  1.00 7.03  ? 246 ARG A N   1 
ATOM   2023 C  CA  . ARG A 1 245 ? -0.071  -7.180  18.317  1.00 7.64  ? 246 ARG A CA  1 
ATOM   2024 C  C   . ARG A 1 245 ? -0.593  -8.069  19.419  1.00 6.59  ? 246 ARG A C   1 
ATOM   2025 O  O   . ARG A 1 245 ? -1.777  -8.102  19.688  1.00 11.21 ? 246 ARG A O   1 
ATOM   2026 C  CB  . ARG A 1 245 ? -0.056  -5.719  18.812  1.00 8.01  ? 246 ARG A CB  1 
ATOM   2027 C  CG  . ARG A 1 245 ? 1.079   -5.551  19.794  1.00 6.92  ? 246 ARG A CG  1 
ATOM   2028 C  CD  . ARG A 1 245 ? 1.069   -4.145  20.380  1.00 10.76 ? 246 ARG A CD  1 
ATOM   2029 N  NE  . ARG A 1 245 ? 2.302   -3.870  21.200  1.00 9.82  ? 246 ARG A NE  1 
ATOM   2030 C  CZ  . ARG A 1 245 ? 2.483   -2.818  21.990  1.00 12.64 ? 246 ARG A CZ  1 
ATOM   2031 N  NH1 . ARG A 1 245 ? 1.464   -1.969  22.305  1.00 9.74  ? 246 ARG A NH1 1 
ATOM   2032 N  NH2 . ARG A 1 245 ? 3.687   -2.651  22.528  1.00 13.22 ? 246 ARG A NH2 1 
ATOM   2033 N  N   . PRO A 1 246 ? 0.281   -8.857  20.091  1.00 8.98  ? 247 PRO A N   1 
ATOM   2034 C  CA  . PRO A 1 246 ? -0.149  -9.717  21.174  1.00 8.01  ? 247 PRO A CA  1 
ATOM   2035 C  C   . PRO A 1 246 ? -0.414  -8.945  22.408  1.00 8.69  ? 247 PRO A C   1 
ATOM   2036 O  O   . PRO A 1 246 ? -0.030  -7.781  22.521  1.00 9.61  ? 247 PRO A O   1 
ATOM   2037 C  CB  . PRO A 1 246 ? 1.038   -10.636 21.401  1.00 11.30 ? 247 PRO A CB  1 
ATOM   2038 C  CG  . PRO A 1 246 ? 2.128   -10.009 20.612  1.00 13.24 ? 247 PRO A CG  1 
ATOM   2039 C  CD  . PRO A 1 246 ? 1.717   -8.977  19.771  1.00 10.86 ? 247 PRO A CD  1 
ATOM   2040 N  N   . ALA A 1 247 ? -1.113  -9.587  23.329  1.00 9.54  ? 248 ALA A N   1 
ATOM   2041 C  CA  . ALA A 1 247 ? -1.454  -8.979  24.604  1.00 7.18  ? 248 ALA A CA  1 
ATOM   2042 C  C   . ALA A 1 247 ? -0.213  -8.442  25.360  1.00 9.36  ? 248 ALA A C   1 
ATOM   2043 O  O   . ALA A 1 247 ? 0.877   -9.091  25.348  1.00 9.89  ? 248 ALA A O   1 
ATOM   2044 C  CB  . ALA A 1 247 ? -2.244  -10.042 25.467  1.00 10.66 ? 248 ALA A CB  1 
ATOM   2045 N  N   . GLN A 1 248 ? -0.366  -7.268  25.965  1.00 7.69  ? 249 GLN A N   1 
ATOM   2046 C  CA  . GLN A 1 248 ? 0.683   -6.562  26.689  1.00 9.81  ? 249 GLN A CA  1 
ATOM   2047 C  C   . GLN A 1 248 ? 0.351   -6.518  28.155  1.00 11.39 ? 249 GLN A C   1 
ATOM   2048 O  O   . GLN A 1 248 ? -0.792  -6.692  28.563  1.00 10.04 ? 249 GLN A O   1 
ATOM   2049 C  CB  . GLN A 1 248 ? 0.764   -5.117  26.189  1.00 11.39 ? 249 GLN A CB  1 
ATOM   2050 C  CG  . GLN A 1 248 ? 1.075   -4.992  24.645  1.00 7.89  ? 249 GLN A CG  1 
ATOM   2051 C  CD  . GLN A 1 248 ? 2.396   -5.620  24.302  1.00 12.54 ? 249 GLN A CD  1 
ATOM   2052 O  OE1 . GLN A 1 248 ? 3.454   -5.204  24.783  1.00 14.52 ? 249 GLN A OE1 1 
ATOM   2053 N  NE2 . GLN A 1 248 ? 2.353   -6.646  23.447  1.00 11.05 ? 249 GLN A NE2 1 
ATOM   2054 N  N   . PRO A 1 249 ? 1.359   -6.217  29.003  1.00 12.48 ? 250 PRO A N   1 
ATOM   2055 C  CA  . PRO A 1 249 ? 1.111   -6.279  30.455  1.00 12.44 ? 250 PRO A CA  1 
ATOM   2056 C  C   . PRO A 1 249 ? 0.069   -5.293  30.923  1.00 9.90  ? 250 PRO A C   1 
ATOM   2057 O  O   . PRO A 1 249 ? 0.111   -4.132  30.519  1.00 12.24 ? 250 PRO A O   1 
ATOM   2058 C  CB  . PRO A 1 249 ? 2.479   -5.850  31.030  1.00 14.17 ? 250 PRO A CB  1 
ATOM   2059 C  CG  . PRO A 1 249 ? 3.446   -6.206  29.961  1.00 15.04 ? 250 PRO A CG  1 
ATOM   2060 C  CD  . PRO A 1 249 ? 2.746   -5.893  28.660  1.00 12.23 ? 250 PRO A CD  1 
ATOM   2061 N  N   . LEU A 1 250 ? -0.827  -5.751  31.781  1.00 11.67 ? 251 LEU A N   1 
ATOM   2062 C  CA  . LEU A 1 250 ? -1.876  -4.887  32.326  1.00 12.45 ? 251 LEU A CA  1 
ATOM   2063 C  C   . LEU A 1 250 ? -1.284  -3.811  33.241  1.00 12.30 ? 251 LEU A C   1 
ATOM   2064 O  O   . LEU A 1 250 ? -1.849  -2.703  33.314  1.00 10.43 ? 251 LEU A O   1 
ATOM   2065 C  CB  . LEU A 1 250 ? -2.969  -5.703  33.053  1.00 12.44 ? 251 LEU A CB  1 
ATOM   2066 C  CG  . LEU A 1 250 ? -4.324  -5.028  33.444  1.00 10.80 ? 251 LEU A CG  1 
ATOM   2067 C  CD1 . LEU A 1 250 ? -5.037  -4.378  32.215  1.00 12.28 ? 251 LEU A CD1 1 
ATOM   2068 C  CD2 . LEU A 1 250 ? -5.268  -6.086  34.187  1.00 16.06 ? 251 LEU A CD2 1 
ATOM   2069 N  N   A LYS A 1 251 ? -0.103  -4.049  33.865  0.50 11.73 ? 252 LYS A N   1 
ATOM   2070 N  N   B LYS A 1 251 ? -0.263  -4.256  33.996  0.50 13.78 ? 252 LYS A N   1 
ATOM   2071 C  CA  A LYS A 1 251 ? 0.562   -2.994  34.731  0.50 10.93 ? 252 LYS A CA  1 
ATOM   2072 C  CA  B LYS A 1 251 ? 0.345   -3.445  35.036  0.50 15.37 ? 252 LYS A CA  1 
ATOM   2073 C  C   A LYS A 1 251 ? -0.421  -2.407  35.750  0.50 10.75 ? 252 LYS A C   1 
ATOM   2074 C  C   B LYS A 1 251 ? -0.782  -3.006  35.971  0.50 15.33 ? 252 LYS A C   1 
ATOM   2075 O  O   A LYS A 1 251 ? -1.214  -3.150  36.367  0.50 12.84 ? 252 LYS A O   1 
ATOM   2076 O  O   B LYS A 1 251 ? -1.612  -3.838  36.323  0.50 15.71 ? 252 LYS A O   1 
ATOM   2077 C  CB  A LYS A 1 251 ? 1.272   -1.885  33.907  0.50 9.41  ? 252 LYS A CB  1 
ATOM   2078 C  CB  B LYS A 1 251 ? 1.236   -2.384  34.412  0.50 15.83 ? 252 LYS A CB  1 
ATOM   2079 C  CG  A LYS A 1 251 ? 2.454   -2.483  33.117  0.50 10.10 ? 252 LYS A CG  1 
ATOM   2080 C  CG  B LYS A 1 251 ? 2.462   -3.124  33.830  0.50 16.41 ? 252 LYS A CG  1 
ATOM   2081 C  CD  A LYS A 1 251 ? 3.314   -1.435  32.448  0.50 11.98 ? 252 LYS A CD  1 
ATOM   2082 C  CD  B LYS A 1 251 ? 3.500   -2.254  33.263  0.50 18.55 ? 252 LYS A CD  1 
ATOM   2083 C  CE  A LYS A 1 251 ? 4.367   -2.093  31.634  0.50 14.82 ? 252 LYS A CE  1 
ATOM   2084 C  CE  B LYS A 1 251 ? 4.621   -3.076  32.652  0.50 20.47 ? 252 LYS A CE  1 
ATOM   2085 N  NZ  A LYS A 1 251 ? 5.361   -1.174  31.076  0.50 16.14 ? 252 LYS A NZ  1 
ATOM   2086 N  NZ  B LYS A 1 251 ? 5.147   -2.286  31.485  0.50 25.06 ? 252 LYS A NZ  1 
ATOM   2087 N  N   A ASN A 1 252 ? -0.430  -1.093  35.892  0.50 10.41 ? 253 ASN A N   1 
ATOM   2088 N  N   B ASN A 1 252 ? -0.883  -1.753  36.370  0.50 14.37 ? 253 ASN A N   1 
ATOM   2089 C  CA  A ASN A 1 252 ? -1.288  -0.499  36.884  0.50 13.43 ? 253 ASN A CA  1 
ATOM   2090 C  CA  B ASN A 1 252 ? -1.796  -1.532  37.512  0.50 15.34 ? 253 ASN A CA  1 
ATOM   2091 C  C   A ASN A 1 252 ? -2.668  -0.076  36.390  0.50 13.91 ? 253 ASN A C   1 
ATOM   2092 C  C   B ASN A 1 252 ? -3.341  -1.524  37.167  0.50 13.53 ? 253 ASN A C   1 
ATOM   2093 O  O   A ASN A 1 252 ? -2.940  1.155   36.415  0.50 13.98 ? 253 ASN A O   1 
ATOM   2094 O  O   B ASN A 1 252 ? -4.217  -1.367  38.049  0.50 14.77 ? 253 ASN A O   1 
ATOM   2095 C  CB  A ASN A 1 252 ? -0.634  0.747   37.453  0.50 13.84 ? 253 ASN A CB  1 
ATOM   2096 C  CB  B ASN A 1 252 ? -1.362  -0.269  38.264  0.50 16.55 ? 253 ASN A CB  1 
ATOM   2097 C  CG  A ASN A 1 252 ? -1.229  1.142   38.795  0.50 12.97 ? 253 ASN A CG  1 
ATOM   2098 C  CG  B ASN A 1 252 ? -2.116  -0.078  39.550  0.50 19.05 ? 253 ASN A CG  1 
ATOM   2099 O  OD1 A ASN A 1 252 ? -1.199  0.344   39.739  0.50 23.42 ? 253 ASN A OD1 1 
ATOM   2100 O  OD1 B ASN A 1 252 ? -2.460  -1.054  40.219  0.50 22.81 ? 253 ASN A OD1 1 
ATOM   2101 N  ND2 A ASN A 1 252 ? -1.726  2.365   38.899  0.50 20.11 ? 253 ASN A ND2 1 
ATOM   2102 N  ND2 B ASN A 1 252 ? -2.395  1.186   39.908  0.50 24.12 ? 253 ASN A ND2 1 
ATOM   2103 N  N   A ARG A 1 253 ? -3.490  -1.049  35.941  0.50 12.57 ? 254 ARG A N   1 
ATOM   2104 N  N   B ARG A 1 253 ? -3.678  -1.767  35.902  0.50 10.50 ? 254 ARG A N   1 
ATOM   2105 C  CA  A ARG A 1 253 ? -4.842  -0.753  35.438  0.50 11.53 ? 254 ARG A CA  1 
ATOM   2106 C  CA  B ARG A 1 253 ? -4.930  -1.240  35.376  0.50 10.41 ? 254 ARG A CA  1 
ATOM   2107 C  C   A ARG A 1 253 ? -5.940  -1.756  35.815  0.50 12.66 ? 254 ARG A C   1 
ATOM   2108 C  C   B ARG A 1 253 ? -6.100  -2.133  35.737  0.50 12.35 ? 254 ARG A C   1 
ATOM   2109 O  O   A ARG A 1 253 ? -5.647  -2.944  36.053  0.50 13.64 ? 254 ARG A O   1 
ATOM   2110 O  O   B ARG A 1 253 ? -5.939  -3.348  35.764  0.50 13.33 ? 254 ARG A O   1 
ATOM   2111 C  CB  A ARG A 1 253 ? -4.819  -0.561  33.912  0.50 11.04 ? 254 ARG A CB  1 
ATOM   2112 C  CB  B ARG A 1 253 ? -4.860  -1.087  33.830  0.50 10.48 ? 254 ARG A CB  1 
ATOM   2113 C  CG  A ARG A 1 253 ? -3.591  0.204   33.440  0.50 6.10  ? 254 ARG A CG  1 
ATOM   2114 C  CG  B ARG A 1 253 ? -4.280  0.220   33.251  0.50 7.43  ? 254 ARG A CG  1 
ATOM   2115 C  CD  A ARG A 1 253 ? -3.558  0.300   31.954  0.50 5.60  ? 254 ARG A CD  1 
ATOM   2116 C  CD  B ARG A 1 253 ? -4.240  0.054   31.719  0.50 8.49  ? 254 ARG A CD  1 
ATOM   2117 N  NE  A ARG A 1 253 ? -2.686  -0.751  31.390  0.50 6.07  ? 254 ARG A NE  1 
ATOM   2118 N  NE  B ARG A 1 253 ? -3.303  -1.045  31.335  0.50 9.15  ? 254 ARG A NE  1 
ATOM   2119 C  CZ  A ARG A 1 253 ? -2.558  -1.012  30.085  0.50 4.04  ? 254 ARG A CZ  1 
ATOM   2120 C  CZ  B ARG A 1 253 ? -2.959  -1.346  30.076  0.50 8.72  ? 254 ARG A CZ  1 
ATOM   2121 N  NH1 A ARG A 1 253 ? -3.267  -0.274  29.203  0.50 4.22  ? 254 ARG A NH1 1 
ATOM   2122 N  NH1 B ARG A 1 253 ? -3.501  -0.675  29.037  0.50 5.62  ? 254 ARG A NH1 1 
ATOM   2123 N  NH2 A ARG A 1 253 ? -1.740  -1.989  29.638  0.50 5.68  ? 254 ARG A NH2 1 
ATOM   2124 N  NH2 B ARG A 1 253 ? -2.091  -2.317  29.846  0.50 8.43  ? 254 ARG A NH2 1 
ATOM   2125 N  N   A GLN A 1 254 ? -7.197  -1.258  35.848  0.50 12.53 ? 255 GLN A N   1 
ATOM   2126 N  N   B GLN A 1 254 ? -7.264  -1.534  36.022  0.50 12.67 ? 255 GLN A N   1 
ATOM   2127 C  CA  A GLN A 1 254 ? -8.390  -2.067  36.058  0.50 14.67 ? 255 GLN A CA  1 
ATOM   2128 C  CA  B GLN A 1 254 ? -8.486  -2.294  36.248  0.50 15.02 ? 255 GLN A CA  1 
ATOM   2129 C  C   A GLN A 1 254 ? -9.222  -2.148  34.750  0.50 13.14 ? 255 GLN A C   1 
ATOM   2130 C  C   B GLN A 1 254 ? -9.413  -2.194  35.005  0.50 13.75 ? 255 GLN A C   1 
ATOM   2131 O  O   A GLN A 1 254 ? -9.384  -1.124  34.017  0.50 12.29 ? 255 GLN A O   1 
ATOM   2132 O  O   B GLN A 1 254 ? -9.765  -1.113  34.519  0.50 14.09 ? 255 GLN A O   1 
ATOM   2133 C  CB  A GLN A 1 254 ? -9.264  -1.484  37.202  0.50 14.60 ? 255 GLN A CB  1 
ATOM   2134 C  CB  B GLN A 1 254 ? -9.177  -1.853  37.565  0.50 15.85 ? 255 GLN A CB  1 
ATOM   2135 C  CG  A GLN A 1 254 ? -10.443 -2.450  37.595  0.50 17.55 ? 255 GLN A CG  1 
ATOM   2136 C  CG  B GLN A 1 254 ? -8.343  -2.194  38.835  0.50 17.51 ? 255 GLN A CG  1 
ATOM   2137 C  CD  A GLN A 1 254 ? -11.288 -2.080  38.833  0.50 18.91 ? 255 GLN A CD  1 
ATOM   2138 C  CD  B GLN A 1 254 ? -9.114  -2.159  40.180  0.50 20.47 ? 255 GLN A CD  1 
ATOM   2139 O  OE1 A GLN A 1 254 ? -11.572 -2.980  39.653  0.50 18.30 ? 255 GLN A OE1 1 
ATOM   2140 O  OE1 B GLN A 1 254 ? -9.022  -1.177  40.946  0.50 22.09 ? 255 GLN A OE1 1 
ATOM   2141 N  NE2 A GLN A 1 254 ? -11.688 -0.774  38.985  0.50 19.60 ? 255 GLN A NE2 1 
ATOM   2142 N  NE2 B GLN A 1 254 ? -9.804  -3.259  40.500  0.50 21.24 ? 255 GLN A NE2 1 
ATOM   2143 N  N   . ILE A 1 255 ? -9.729  -3.349  34.458  1.00 12.32 ? 256 ILE A N   1 
ATOM   2144 C  CA  . ILE A 1 255 ? -10.759 -3.474  33.449  1.00 12.27 ? 256 ILE A CA  1 
ATOM   2145 C  C   . ILE A 1 255 ? -12.153 -3.515  34.143  1.00 11.99 ? 256 ILE A C   1 
ATOM   2146 O  O   . ILE A 1 255 ? -12.356 -4.229  35.136  1.00 12.44 ? 256 ILE A O   1 
ATOM   2147 C  CB  . ILE A 1 255 ? -10.541 -4.713  32.599  1.00 11.73 ? 256 ILE A CB  1 
ATOM   2148 C  CG1 . ILE A 1 255 ? -9.101  -4.684  32.038  1.00 12.51 ? 256 ILE A CG1 1 
ATOM   2149 C  CG2 . ILE A 1 255 ? -11.666 -4.873  31.540  1.00 12.44 ? 256 ILE A CG2 1 
ATOM   2150 C  CD1 . ILE A 1 255 ? -8.771  -6.066  31.326  1.00 14.67 ? 256 ILE A CD1 1 
ATOM   2151 N  N   . LYS A 1 256 ? -13.031 -2.623  33.692  1.00 11.29 ? 257 LYS A N   1 
ATOM   2152 C  CA  . LYS A 1 256 ? -14.406 -2.508  34.193  1.00 12.17 ? 257 LYS A CA  1 
ATOM   2153 C  C   . LYS A 1 256 ? -15.349 -3.178  33.275  1.00 11.85 ? 257 LYS A C   1 
ATOM   2154 O  O   . LYS A 1 256 ? -15.180 -3.139  32.049  1.00 12.36 ? 257 LYS A O   1 
ATOM   2155 C  CB  . LYS A 1 256 ? -14.755 -0.998  34.388  1.00 13.39 ? 257 LYS A CB  1 
ATOM   2156 C  CG  . LYS A 1 256 ? -13.904 -0.395  35.574  1.00 16.64 ? 257 LYS A CG  1 
ATOM   2157 C  CD  . LYS A 1 256 ? -14.011 1.133   35.538  1.00 20.50 ? 257 LYS A CD  1 
ATOM   2158 C  CE  . LYS A 1 256 ? -13.320 1.802   36.768  1.00 26.34 ? 257 LYS A CE  1 
ATOM   2159 N  NZ  . LYS A 1 256 ? -13.217 3.325   36.690  1.00 26.85 ? 257 LYS A NZ  1 
ATOM   2160 N  N   . ALA A 1 257 ? -16.417 -3.786  33.807  1.00 12.84 ? 258 ALA A N   1 
ATOM   2161 C  CA  . ALA A 1 257 ? -17.467 -4.418  32.990  1.00 12.55 ? 258 ALA A CA  1 
ATOM   2162 C  C   . ALA A 1 257 ? -18.786 -3.650  33.118  1.00 12.87 ? 258 ALA A C   1 
ATOM   2163 O  O   . ALA A 1 257 ? -19.144 -3.169  34.195  1.00 12.07 ? 258 ALA A O   1 
ATOM   2164 C  CB  . ALA A 1 257 ? -17.669 -5.935  33.354  1.00 12.21 ? 258 ALA A CB  1 
ATOM   2165 N  N   . SER A 1 258 ? -19.512 -3.520  32.013  1.00 10.33 ? 259 SER A N   1 
ATOM   2166 C  CA  . SER A 1 258 ? -20.750 -2.722  32.022  1.00 14.12 ? 259 SER A CA  1 
ATOM   2167 C  C   . SER A 1 258 ? -21.893 -3.666  32.444  1.00 16.19 ? 259 SER A C   1 
ATOM   2168 O  O   . SER A 1 258 ? -23.035 -3.223  32.553  1.00 19.73 ? 259 SER A O   1 
ATOM   2169 C  CB  . SER A 1 258 ? -21.031 -2.179  30.623  1.00 14.39 ? 259 SER A CB  1 
ATOM   2170 O  OG  . SER A 1 258 ? -21.571 -3.189  29.762  1.00 13.45 ? 259 SER A OG  1 
ATOM   2171 N  N   . PHE A 1 259 ? -21.574 -4.916  32.722  1.00 18.20 ? 260 PHE A N   1 
ATOM   2172 C  CA  . PHE A 1 259 ? -22.593 -5.968  32.950  1.00 19.20 ? 260 PHE A CA  1 
ATOM   2173 C  C   . PHE A 1 259 ? -22.123 -6.962  34.060  1.00 22.03 ? 260 PHE A C   1 
ATOM   2174 O  O   . PHE A 1 259 ? -20.935 -7.080  34.335  1.00 20.27 ? 260 PHE A O   1 
ATOM   2175 C  CB  . PHE A 1 259 ? -22.860 -6.723  31.651  1.00 17.92 ? 260 PHE A CB  1 
ATOM   2176 C  CG  . PHE A 1 259 ? -21.624 -7.490  31.126  1.00 19.47 ? 260 PHE A CG  1 
ATOM   2177 C  CD1 . PHE A 1 259 ? -20.690 -6.798  30.371  1.00 18.51 ? 260 PHE A CD1 1 
ATOM   2178 C  CD2 . PHE A 1 259 ? -21.333 -8.775  31.542  1.00 19.21 ? 260 PHE A CD2 1 
ATOM   2179 C  CE1 . PHE A 1 259 ? -19.495 -7.412  29.948  1.00 19.60 ? 260 PHE A CE1 1 
ATOM   2180 C  CE2 . PHE A 1 259 ? -20.155 -9.402  31.138  1.00 18.88 ? 260 PHE A CE2 1 
ATOM   2181 C  CZ  . PHE A 1 259 ? -19.237 -8.710  30.312  1.00 18.05 ? 260 PHE A CZ  1 
ATOM   2182 N  N   . LYS A 1 260 ? -23.064 -7.724  34.655  1.00 28.02 ? 261 LYS A N   1 
ATOM   2183 C  CA  . LYS A 1 260 ? -22.691 -8.794  35.624  1.00 33.03 ? 261 LYS A CA  1 
ATOM   2184 C  C   . LYS A 1 260 ? -22.594 -10.167 34.955  1.00 34.31 ? 261 LYS A C   1 
ATOM   2185 O  O   . LYS A 1 260 ? -23.336 -10.540 34.017  1.00 35.52 ? 261 LYS A O   1 
ATOM   2186 C  CB  . LYS A 1 260 ? -23.641 -8.900  36.825  1.00 33.64 ? 261 LYS A CB  1 
ATOM   2187 C  CG  . LYS A 1 260 ? -23.566 -7.713  37.790  1.00 35.84 ? 261 LYS A CG  1 
ATOM   2188 C  CD  . LYS A 1 260 ? -24.566 -7.835  38.941  1.00 37.08 ? 261 LYS A CD  1 
ATOM   2189 C  CE  . LYS A 1 260 ? -25.983 -7.506  38.497  1.00 43.00 ? 261 LYS A CE  1 
ATOM   2190 N  NZ  . LYS A 1 260 ? -26.949 -7.665  39.641  1.00 45.05 ? 261 LYS A NZ  1 
ATOM   2191 O  OXT . LYS A 1 260 ? -21.691 -10.910 35.372  1.00 36.67 ? 261 LYS A OXT 1 
HETATM 2192 ZN ZN  . ZN  B 2 .   ? -6.652  -1.669  15.304  1.00 7.10  ? 262 ZN  A ZN  1 
HETATM 2193 S  S   . DMS C 3 .   ? 1.383   -11.638 14.975  1.00 25.98 ? 263 DMS A S   1 
HETATM 2194 O  O   . DMS C 3 .   ? 2.406   -10.396 14.128  1.00 28.30 ? 263 DMS A O   1 
HETATM 2195 C  C1  . DMS C 3 .   ? 2.186   -13.225 14.695  1.00 23.00 ? 263 DMS A C1  1 
HETATM 2196 C  C2  . DMS C 3 .   ? 1.667   -11.543 16.746  1.00 21.10 ? 263 DMS A C2  1 
HETATM 2197 N  N1  . JS7 D 4 .   ? -0.712  10.154  14.995  1.00 45.28 ? 264 JS7 A N1  1 
HETATM 2198 C  C2  . JS7 D 4 .   ? -0.728  8.931   15.516  1.00 46.90 ? 264 JS7 A C2  1 
HETATM 2199 N  N3  . JS7 D 4 .   ? -1.192  7.902   14.836  1.00 44.42 ? 264 JS7 A N3  1 
HETATM 2200 C  C4  . JS7 D 4 .   ? -1.671  8.064   13.604  1.00 45.48 ? 264 JS7 A C4  1 
HETATM 2201 C  C5  . JS7 D 4 .   ? -1.689  9.358   12.992  1.00 48.73 ? 264 JS7 A C5  1 
HETATM 2202 C  C6  . JS7 D 4 .   ? -1.170  10.447  13.768  1.00 48.13 ? 264 JS7 A C6  1 
HETATM 2203 N  N7  . JS7 D 4 .   ? -2.127  6.908   12.936  1.00 42.38 ? 264 JS7 A N7  1 
HETATM 2204 C  C8  . JS7 D 4 .   ? -4.378  4.592   14.508  1.00 26.08 ? 264 JS7 A C8  1 
HETATM 2205 C  C9  . JS7 D 4 .   ? -5.713  4.452   14.872  1.00 21.65 ? 264 JS7 A C9  1 
HETATM 2206 C  C10 . JS7 D 4 .   ? -6.138  3.297   15.575  1.00 19.31 ? 264 JS7 A C10 1 
HETATM 2207 C  C11 . JS7 D 4 .   ? -5.293  2.254   15.910  1.00 19.53 ? 264 JS7 A C11 1 
HETATM 2208 C  C12 . JS7 D 4 .   ? -3.938  2.395   15.517  1.00 21.70 ? 264 JS7 A C12 1 
HETATM 2209 C  C13 . JS7 D 4 .   ? -3.461  3.554   14.818  1.00 22.89 ? 264 JS7 A C13 1 
HETATM 2210 S  S14 . JS7 D 4 .   ? -5.916  0.767   16.791  1.00 20.06 ? 264 JS7 A S14 1 
HETATM 2211 O  O15 . JS7 D 4 .   ? -5.368  0.837   18.176  1.00 10.89 ? 264 JS7 A O15 1 
HETATM 2212 O  O16 . JS7 D 4 .   ? -7.479  0.865   16.618  1.00 18.20 ? 264 JS7 A O16 1 
HETATM 2213 N  N17 . JS7 D 4 .   ? -5.270  -0.493  15.929  1.00 15.67 ? 264 JS7 A N17 1 
HETATM 2214 N  N18 . JS7 D 4 .   ? -2.266  9.462   11.573  1.00 51.34 ? 264 JS7 A N18 1 
HETATM 2215 O  O19 . JS7 D 4 .   ? -3.178  10.177  11.322  1.00 52.99 ? 264 JS7 A O19 1 
HETATM 2216 O  O20 . JS7 D 4 .   ? -1.731  8.733   10.576  1.00 51.80 ? 264 JS7 A O20 1 
HETATM 2217 O  O21 . JS7 D 4 .   ? -1.060  11.902  13.426  1.00 46.30 ? 264 JS7 A O21 1 
HETATM 2218 C  C22 . JS7 D 4 .   ? 0.158   12.564  13.340  1.00 46.42 ? 264 JS7 A C22 1 
HETATM 2219 C  C23 . JS7 D 4 .   ? -2.477  5.787   13.705  1.00 31.50 ? 264 JS7 A C23 1 
HETATM 2220 C  C24 . JS7 D 4 .   ? -3.996  5.841   13.776  1.00 27.81 ? 264 JS7 A C24 1 
HETATM 2221 O  O   . HOH E 5 .   ? -0.455  10.887  23.421  1.00 19.81 ? 126 HOH A O   1 
HETATM 2222 O  O   . HOH E 5 .   ? -16.764 -22.099 -0.010  1.00 36.82 ? 265 HOH A O   1 
HETATM 2223 O  O   . HOH E 5 .   ? -6.552  -8.407  -7.170  1.00 36.76 ? 266 HOH A O   1 
HETATM 2224 O  O   . HOH E 5 .   ? -15.515 -16.579 25.597  1.00 33.35 ? 267 HOH A O   1 
HETATM 2225 O  O   . HOH E 5 .   ? -1.689  -0.942  -12.469 1.00 42.69 ? 268 HOH A O   1 
HETATM 2226 O  O   . HOH E 5 .   ? -29.680 6.706   7.098   1.00 39.15 ? 269 HOH A O   1 
HETATM 2227 O  O   . HOH E 5 .   ? 2.403   -2.178  37.535  1.00 40.96 ? 270 HOH A O   1 
HETATM 2228 O  O   . HOH E 5 .   ? -6.130  6.496   -8.999  1.00 35.81 ? 271 HOH A O   1 
HETATM 2229 O  O   . HOH E 5 .   ? -21.737 -21.355 17.437  1.00 36.64 ? 272 HOH A O   1 
HETATM 2230 O  O   . HOH E 5 .   ? -17.087 -8.335  20.446  1.00 8.48  ? 273 HOH A O   1 
HETATM 2231 O  O   . HOH E 5 .   ? 9.938   -12.883 9.436   1.00 43.60 ? 274 HOH A O   1 
HETATM 2232 O  O   . HOH E 5 .   ? -18.678 -2.976  45.282  1.00 42.10 ? 275 HOH A O   1 
HETATM 2233 O  O   . HOH E 5 .   ? 5.847   -12.447 11.717  1.00 39.36 ? 276 HOH A O   1 
HETATM 2234 O  O   . HOH E 5 .   ? -20.429 13.561  29.129  1.00 38.64 ? 277 HOH A O   1 
HETATM 2235 O  O   . HOH E 5 .   ? 9.142   1.980   30.425  1.00 50.04 ? 278 HOH A O   1 
HETATM 2236 O  O   . HOH E 5 .   ? 5.090   -10.849 18.634  1.00 32.97 ? 279 HOH A O   1 
HETATM 2237 O  O   . HOH E 5 .   ? 4.990   -13.559 15.535  1.00 37.71 ? 280 HOH A O   1 
HETATM 2238 O  O   . HOH E 5 .   ? -22.037 -13.999 18.690  1.00 28.38 ? 281 HOH A O   1 
HETATM 2239 O  O   . HOH E 5 .   ? 4.385   -0.544  36.253  1.00 40.22 ? 282 HOH A O   1 
HETATM 2240 O  O   . HOH E 5 .   ? 10.435  6.777   15.034  1.00 35.91 ? 283 HOH A O   1 
HETATM 2241 O  O   . HOH E 5 .   ? -21.721 -7.128  23.661  1.00 11.57 ? 284 HOH A O   1 
HETATM 2242 O  O   . HOH E 5 .   ? 5.169   -7.544  25.943  1.00 35.80 ? 285 HOH A O   1 
HETATM 2243 O  O   . HOH E 5 .   ? 4.505   -0.272  -5.985  1.00 35.77 ? 286 HOH A O   1 
HETATM 2244 O  O   . HOH E 5 .   ? -19.591 -15.001 25.732  1.00 43.59 ? 287 HOH A O   1 
HETATM 2245 O  O   . HOH E 5 .   ? -22.311 -14.497 16.271  1.00 39.77 ? 288 HOH A O   1 
HETATM 2246 O  O   . HOH E 5 .   ? -9.755  5.566   -6.516  1.00 37.37 ? 289 HOH A O   1 
HETATM 2247 O  O   . HOH E 5 .   ? -24.051 -7.091  0.559   1.00 30.51 ? 290 HOH A O   1 
HETATM 2248 O  O   . HOH E 5 .   ? 7.891   -9.567  16.799  1.00 18.29 ? 291 HOH A O   1 
HETATM 2249 O  O   . HOH E 5 .   ? 10.177  -10.855 16.149  1.00 17.39 ? 292 HOH A O   1 
HETATM 2250 O  O   . HOH E 5 .   ? -5.704  7.527   11.060  1.00 38.07 ? 293 HOH A O   1 
HETATM 2251 O  O   . HOH E 5 .   ? -12.177 -19.804 3.047   1.00 42.54 ? 294 HOH A O   1 
HETATM 2252 O  O   . HOH E 5 .   ? -16.375 -9.955  32.962  1.00 15.82 ? 295 HOH A O   1 
HETATM 2253 O  O   . HOH E 5 .   ? -21.573 5.672   4.686   1.00 15.07 ? 296 HOH A O   1 
HETATM 2254 O  O   . HOH E 5 .   ? -2.539  -8.701  29.266  1.00 12.22 ? 297 HOH A O   1 
HETATM 2255 O  O   . HOH E 5 .   ? -1.248  -4.081  15.738  1.00 8.14  ? 298 HOH A O   1 
HETATM 2256 O  O   . HOH E 5 .   ? -10.629 8.733   25.591  1.00 9.69  ? 299 HOH A O   1 
HETATM 2257 O  O   . HOH E 5 .   ? -4.553  -13.477 18.097  1.00 8.39  ? 300 HOH A O   1 
HETATM 2258 O  O   . HOH E 5 .   ? -13.887 10.496  27.881  1.00 16.21 ? 301 HOH A O   1 
HETATM 2259 O  O   . HOH E 5 .   ? 3.631   5.102   29.843  1.00 19.74 ? 302 HOH A O   1 
HETATM 2260 O  O   . HOH E 5 .   ? -18.016 -20.434 7.931   1.00 12.89 ? 303 HOH A O   1 
HETATM 2261 O  O   . HOH E 5 .   ? -2.025  -12.310 22.909  1.00 11.37 ? 304 HOH A O   1 
HETATM 2262 O  O   . HOH E 5 .   ? -19.221 10.154  8.940   1.00 14.09 ? 305 HOH A O   1 
HETATM 2263 O  O   . HOH E 5 .   ? -21.012 -12.651 -1.767  1.00 17.80 ? 306 HOH A O   1 
HETATM 2264 O  O   . HOH E 5 .   ? -12.952 -22.358 12.179  1.00 33.50 ? 307 HOH A O   1 
HETATM 2265 O  O   . HOH E 5 .   ? 4.839   -4.978  21.008  1.00 12.16 ? 308 HOH A O   1 
HETATM 2266 O  O   . HOH E 5 .   ? 5.279   7.140   20.093  1.00 19.43 ? 309 HOH A O   1 
HETATM 2267 O  O   . HOH E 5 .   ? -3.410  -13.260 25.275  1.00 11.42 ? 310 HOH A O   1 
HETATM 2268 O  O   . HOH E 5 .   ? -3.832  -15.899 24.485  1.00 11.99 ? 311 HOH A O   1 
HETATM 2269 O  O   . HOH E 5 .   ? 7.481   6.188   21.747  1.00 16.99 ? 312 HOH A O   1 
HETATM 2270 O  O   . HOH E 5 .   ? 1.244   -1.512  29.503  1.00 13.71 ? 313 HOH A O   1 
HETATM 2271 O  O   . HOH E 5 .   ? -24.117 -0.761  26.486  1.00 23.20 ? 314 HOH A O   1 
HETATM 2272 O  O   . HOH E 5 .   ? 8.542   -3.724  21.113  1.00 15.75 ? 315 HOH A O   1 
HETATM 2273 O  O   . HOH E 5 .   ? -7.884  -15.402 11.362  1.00 9.55  ? 316 HOH A O   1 
HETATM 2274 O  O   . HOH E 5 .   ? -10.236 14.770  12.115  1.00 18.54 ? 317 HOH A O   1 
HETATM 2275 O  O   . HOH E 5 .   ? -12.077 2.921   30.913  1.00 24.74 ? 318 HOH A O   1 
HETATM 2276 O  O   . HOH E 5 .   ? -23.507 -0.858  3.931   1.00 20.02 ? 319 HOH A O   1 
HETATM 2277 O  O   . HOH E 5 .   ? -17.895 10.566  11.312  1.00 15.24 ? 320 HOH A O   1 
HETATM 2278 O  O   . HOH E 5 .   ? -8.205  -19.358 21.777  1.00 14.68 ? 321 HOH A O   1 
HETATM 2279 O  O   . HOH E 5 .   ? -9.821  -7.950  34.091  1.00 25.01 ? 322 HOH A O   1 
HETATM 2280 O  O   . HOH E 5 .   ? -3.525  -11.096 20.999  1.00 10.16 ? 323 HOH A O   1 
HETATM 2281 O  O   . HOH E 5 .   ? -22.822 -5.943  2.707   1.00 20.51 ? 324 HOH A O   1 
HETATM 2282 O  O   . HOH E 5 .   ? 2.566   -13.276 5.079   1.00 25.18 ? 325 HOH A O   1 
HETATM 2283 O  O   . HOH E 5 .   ? -26.222 3.517   15.507  1.00 32.70 ? 326 HOH A O   1 
HETATM 2284 O  O   . HOH E 5 .   ? -23.043 -11.795 14.084  1.00 19.27 ? 327 HOH A O   1 
HETATM 2285 O  O   . HOH E 5 .   ? 8.269   -5.791  -10.694 1.00 28.86 ? 328 HOH A O   1 
HETATM 2286 O  O   . HOH E 5 .   ? -5.978  -4.527  -6.490  1.00 21.61 ? 329 HOH A O   1 
HETATM 2287 O  O   . HOH E 5 .   ? -28.930 -5.700  24.620  1.00 24.25 ? 330 HOH A O   1 
HETATM 2288 O  O   . HOH E 5 .   ? -2.210  -17.423 4.886   1.00 28.30 ? 331 HOH A O   1 
HETATM 2289 O  O   . HOH E 5 .   ? -20.409 11.012  26.735  1.00 15.59 ? 332 HOH A O   1 
HETATM 2290 O  O   . HOH E 5 .   ? 4.604   -6.638  8.036   1.00 21.62 ? 333 HOH A O   1 
HETATM 2291 O  O   . HOH E 5 .   ? -24.113 8.761   20.156  1.00 22.78 ? 334 HOH A O   1 
HETATM 2292 O  O   . HOH E 5 .   ? -25.010 -7.740  9.018   1.00 13.59 ? 335 HOH A O   1 
HETATM 2293 O  O   . HOH E 5 .   ? -27.069 3.487   21.080  1.00 31.01 ? 336 HOH A O   1 
HETATM 2294 O  O   . HOH E 5 .   ? -17.835 -21.986 5.899   1.00 19.66 ? 337 HOH A O   1 
HETATM 2295 O  O   . HOH E 5 .   ? -19.494 -23.575 5.979   1.00 24.71 ? 338 HOH A O   1 
HETATM 2296 O  O   . HOH E 5 .   ? -20.474 -6.672  -2.307  1.00 36.95 ? 339 HOH A O   1 
HETATM 2297 O  O   . HOH E 5 .   ? -16.072 15.936  23.783  1.00 16.86 ? 340 HOH A O   1 
HETATM 2298 O  O   . HOH E 5 .   ? -8.688  -3.907  7.848   1.00 9.83  ? 341 HOH A O   1 
HETATM 2299 O  O   . HOH E 5 .   ? -28.644 0.334   24.555  1.00 19.26 ? 342 HOH A O   1 
HETATM 2300 O  O   . HOH E 5 .   ? 4.198   -3.329  26.448  1.00 18.82 ? 343 HOH A O   1 
HETATM 2301 O  O   . HOH E 5 .   ? -8.668  -15.322 36.631  1.00 26.42 ? 344 HOH A O   1 
HETATM 2302 O  O   . HOH E 5 .   ? -15.530 8.999   -2.093  1.00 19.98 ? 345 HOH A O   1 
HETATM 2303 O  O   . HOH E 5 .   ? -10.324 -18.234 17.048  1.00 15.02 ? 346 HOH A O   1 
HETATM 2304 O  O   . HOH E 5 .   ? 5.107   -7.413  22.387  1.00 27.30 ? 347 HOH A O   1 
HETATM 2305 O  O   . HOH E 5 .   ? -4.803  -11.852 32.228  1.00 17.99 ? 348 HOH A O   1 
HETATM 2306 O  O   . HOH E 5 .   ? -8.339  0.692   -6.474  1.00 21.49 ? 349 HOH A O   1 
HETATM 2307 O  O   . HOH E 5 .   ? -22.148 -18.488 13.669  1.00 24.59 ? 350 HOH A O   1 
HETATM 2308 O  O   . HOH E 5 .   ? -3.669  -12.988 -2.848  1.00 21.55 ? 351 HOH A O   1 
HETATM 2309 O  O   . HOH E 5 .   ? 1.390   8.850   24.461  1.00 19.19 ? 352 HOH A O   1 
HETATM 2310 O  O   . HOH E 5 .   ? -23.276 -2.911  6.523   1.00 19.21 ? 353 HOH A O   1 
HETATM 2311 O  O   . HOH E 5 .   ? -16.136 -12.323 24.340  1.00 15.21 ? 354 HOH A O   1 
HETATM 2312 O  O   . HOH E 5 .   ? -14.294 -16.515 29.116  1.00 24.00 ? 355 HOH A O   1 
HETATM 2313 O  O   . HOH E 5 .   ? -0.247  -21.656 4.759   1.00 19.45 ? 356 HOH A O   1 
HETATM 2314 O  O   . HOH E 5 .   ? -11.216 5.583   37.971  1.00 19.65 ? 357 HOH A O   1 
HETATM 2315 O  O   . HOH E 5 .   ? -19.937 -16.751 3.014   1.00 20.39 ? 358 HOH A O   1 
HETATM 2316 O  O   . HOH E 5 .   ? -24.787 12.066  6.442   1.00 24.50 ? 359 HOH A O   1 
HETATM 2317 O  O   . HOH E 5 .   ? 4.477   -2.671  29.055  1.00 27.36 ? 360 HOH A O   1 
HETATM 2318 O  O   . HOH E 5 .   ? 0.110   1.236   34.495  1.00 27.41 ? 361 HOH A O   1 
HETATM 2319 O  O   . HOH E 5 .   ? -8.003  -22.222 10.411  1.00 17.06 ? 362 HOH A O   1 
HETATM 2320 O  O   . HOH E 5 .   ? -13.461 -18.596 14.822  1.00 19.57 ? 363 HOH A O   1 
HETATM 2321 O  O   . HOH E 5 .   ? 0.215   -19.427 10.781  1.00 24.31 ? 364 HOH A O   1 
HETATM 2322 O  O   . HOH E 5 .   ? -9.187  -5.862  35.963  1.00 18.80 ? 365 HOH A O   1 
HETATM 2323 O  O   . HOH E 5 .   ? -18.755 -8.843  34.649  1.00 27.45 ? 366 HOH A O   1 
HETATM 2324 O  O   . HOH E 5 .   ? -24.602 -9.365  2.057   1.00 23.03 ? 367 HOH A O   1 
HETATM 2325 O  O   . HOH E 5 .   ? 1.933   -17.472 7.068   0.50 17.11 ? 368 HOH A O   1 
HETATM 2326 O  O   . HOH E 5 .   ? -27.619 2.737   23.524  1.00 24.08 ? 369 HOH A O   1 
HETATM 2327 O  O   . HOH E 5 .   ? -12.703 -8.869  -3.118  1.00 27.93 ? 370 HOH A O   1 
HETATM 2328 O  O   . HOH E 5 .   ? 8.509   -4.685  23.811  1.00 24.16 ? 371 HOH A O   1 
HETATM 2329 O  O   . HOH E 5 .   ? -12.089 10.600  6.035   1.00 32.20 ? 372 HOH A O   1 
HETATM 2330 O  O   . HOH E 5 .   ? -23.388 -0.571  34.412  1.00 25.60 ? 373 HOH A O   1 
HETATM 2331 O  O   . HOH E 5 .   ? -23.302 -13.242 11.224  1.00 22.02 ? 374 HOH A O   1 
HETATM 2332 O  O   . HOH E 5 .   ? -17.647 2.939   -6.689  1.00 27.68 ? 375 HOH A O   1 
HETATM 2333 O  O   . HOH E 5 .   ? -30.570 -6.831  22.451  1.00 33.30 ? 376 HOH A O   1 
HETATM 2334 O  O   . HOH E 5 .   ? -12.110 -3.260  42.207  1.00 33.50 ? 377 HOH A O   1 
HETATM 2335 O  O   . HOH E 5 .   ? -30.839 1.529   25.886  1.00 26.48 ? 378 HOH A O   1 
HETATM 2336 O  O   . HOH E 5 .   ? -0.200  -14.214 22.305  1.00 23.57 ? 379 HOH A O   1 
HETATM 2337 O  O   . HOH E 5 .   ? -7.111  5.895   6.641   1.00 27.32 ? 380 HOH A O   1 
HETATM 2338 O  O   . HOH E 5 .   ? -1.597  -13.107 27.240  1.00 20.53 ? 381 HOH A O   1 
HETATM 2339 O  O   . HOH E 5 .   ? -15.569 -10.147 37.347  1.00 30.64 ? 382 HOH A O   1 
HETATM 2340 O  O   . HOH E 5 .   ? -7.257  -8.697  -2.422  1.00 24.30 ? 383 HOH A O   1 
HETATM 2341 O  O   . HOH E 5 .   ? -17.092 -14.074 37.442  1.00 27.37 ? 384 HOH A O   1 
HETATM 2342 O  O   . HOH E 5 .   ? -25.927 6.456   27.001  1.00 24.26 ? 385 HOH A O   1 
HETATM 2343 O  O   . HOH E 5 .   ? -1.419  11.600  25.977  1.00 31.25 ? 386 HOH A O   1 
HETATM 2344 O  O   . HOH E 5 .   ? 2.920   -4.158  7.769   1.00 20.88 ? 387 HOH A O   1 
HETATM 2345 O  O   . HOH E 5 .   ? -1.205  9.303   28.044  1.00 27.73 ? 388 HOH A O   1 
HETATM 2346 O  O   . HOH E 5 .   ? -6.217  -19.745 23.920  1.00 19.94 ? 389 HOH A O   1 
HETATM 2347 O  O   . HOH E 5 .   ? -26.827 -2.482  14.336  1.00 16.29 ? 390 HOH A O   1 
HETATM 2348 O  O   . HOH E 5 .   ? -21.256 -24.958 3.442   1.00 38.45 ? 391 HOH A O   1 
HETATM 2349 O  O   . HOH E 5 .   ? 3.552   1.039   -1.647  1.00 38.07 ? 392 HOH A O   1 
HETATM 2350 O  O   . HOH E 5 .   ? -16.330 5.337   -8.134  1.00 28.73 ? 393 HOH A O   1 
HETATM 2351 O  O   . HOH E 5 .   ? 6.147   -5.300  -11.765 1.00 25.72 ? 394 HOH A O   1 
HETATM 2352 O  O   . HOH E 5 .   ? -26.740 -3.844  25.231  1.00 22.56 ? 395 HOH A O   1 
HETATM 2353 O  O   . HOH E 5 .   ? -18.023 4.067   -3.807  1.00 31.42 ? 396 HOH A O   1 
HETATM 2354 O  O   . HOH E 5 .   ? -12.394 -24.835 8.146   1.00 30.72 ? 397 HOH A O   1 
HETATM 2355 O  O   . HOH E 5 .   ? 2.215   -14.004 20.532  1.00 30.60 ? 398 HOH A O   1 
HETATM 2356 O  O   . HOH E 5 .   ? 11.571  -9.714  -0.383  1.00 36.35 ? 399 HOH A O   1 
HETATM 2357 O  O   . HOH E 5 .   ? -4.869  3.266   -5.910  1.00 33.87 ? 400 HOH A O   1 
HETATM 2358 O  O   . HOH E 5 .   ? 2.889   -14.069 -5.801  1.00 34.11 ? 401 HOH A O   1 
HETATM 2359 O  O   . HOH E 5 .   ? 2.881   -13.460 8.222   1.00 29.69 ? 402 HOH A O   1 
HETATM 2360 O  O   . HOH E 5 .   ? 2.640   -11.547 9.454   1.00 22.80 ? 403 HOH A O   1 
HETATM 2361 O  O   . HOH E 5 .   ? -13.044 -16.859 26.644  1.00 16.24 ? 404 HOH A O   1 
HETATM 2362 O  O   . HOH E 5 .   ? 1.666   11.243  15.815  1.00 38.10 ? 405 HOH A O   1 
HETATM 2363 O  O   . HOH E 5 .   ? -0.536  -19.882 6.685   1.00 27.26 ? 406 HOH A O   1 
HETATM 2364 O  O   . HOH E 5 .   ? -7.063  -16.812 1.395   1.00 25.87 ? 407 HOH A O   1 
HETATM 2365 O  O   . HOH E 5 .   ? -9.113  -10.042 -1.252  1.00 20.00 ? 408 HOH A O   1 
HETATM 2366 O  O   . HOH E 5 .   ? -28.023 5.979   19.529  1.00 27.25 ? 409 HOH A O   1 
HETATM 2367 O  O   . HOH E 5 .   ? -7.413  -8.702  32.709  1.00 16.37 ? 410 HOH A O   1 
HETATM 2368 O  O   . HOH E 5 .   ? -6.619  -20.153 19.519  1.00 14.43 ? 411 HOH A O   1 
HETATM 2369 O  O   . HOH E 5 .   ? -13.676 -21.091 14.982  1.00 23.85 ? 412 HOH A O   1 
HETATM 2370 O  O   . HOH E 5 .   ? -27.662 0.133   15.037  1.00 24.96 ? 413 HOH A O   1 
HETATM 2371 O  O   . HOH E 5 .   ? 1.944   8.062   27.742  1.00 29.85 ? 414 HOH A O   1 
HETATM 2372 O  O   . HOH E 5 .   ? -12.951 7.897   28.998  1.00 23.06 ? 415 HOH A O   1 
HETATM 2373 O  O   . HOH E 5 .   ? -12.413 12.664  29.177  1.00 21.32 ? 416 HOH A O   1 
HETATM 2374 O  O   . HOH E 5 .   ? -26.704 -1.261  26.039  1.00 20.56 ? 417 HOH A O   1 
HETATM 2375 O  O   . HOH E 5 .   ? 1.407   -11.692 25.070  1.00 23.57 ? 418 HOH A O   1 
HETATM 2376 O  O   . HOH E 5 .   ? -11.100 -19.423 7.136   1.00 30.97 ? 419 HOH A O   1 
HETATM 2377 O  O   . HOH E 5 .   ? -25.903 -6.224  13.210  1.00 22.43 ? 420 HOH A O   1 
HETATM 2378 O  O   . HOH E 5 .   ? -29.925 4.253   27.386  1.00 28.87 ? 421 HOH A O   1 
HETATM 2379 O  O   . HOH E 5 .   ? 6.418   -8.108  -10.337 1.00 30.77 ? 422 HOH A O   1 
HETATM 2380 O  O   . HOH E 5 .   ? -15.426 -21.709 12.986  1.00 22.27 ? 423 HOH A O   1 
HETATM 2381 O  O   . HOH E 5 .   ? -4.018  3.556   10.272  1.00 33.57 ? 424 HOH A O   1 
HETATM 2382 O  O   . HOH E 5 .   ? -17.112 -7.045  39.946  1.00 35.97 ? 425 HOH A O   1 
HETATM 2383 O  O   . HOH E 5 .   ? 2.105   -15.551 9.255   1.00 20.99 ? 426 HOH A O   1 
HETATM 2384 O  O   . HOH E 5 .   ? -27.951 5.149   25.261  1.00 29.72 ? 427 HOH A O   1 
HETATM 2385 O  O   . HOH E 5 .   ? 4.078   -2.898  4.601   1.00 47.39 ? 428 HOH A O   1 
HETATM 2386 O  O   . HOH E 5 .   ? 1.285   -6.366  34.422  1.00 22.65 ? 429 HOH A O   1 
HETATM 2387 O  O   . HOH E 5 .   ? -4.886  2.232   37.346  1.00 33.37 ? 430 HOH A O   1 
HETATM 2388 O  O   . HOH E 5 .   ? 8.381   -8.580  -0.085  1.00 31.46 ? 431 HOH A O   1 
HETATM 2389 O  O   . HOH E 5 .   ? -1.111  -17.742 18.079  1.00 34.93 ? 432 HOH A O   1 
HETATM 2390 O  O   . HOH E 5 .   ? -0.561  -8.560  32.750  1.00 22.27 ? 433 HOH A O   1 
HETATM 2391 O  O   . HOH E 5 .   ? -21.143 -20.625 1.833   1.00 40.65 ? 434 HOH A O   1 
HETATM 2392 O  O   . HOH E 5 .   ? -25.861 -6.179  34.020  1.00 47.52 ? 435 HOH A O   1 
HETATM 2393 O  O   . HOH E 5 .   ? -10.887 -19.020 34.100  1.00 27.25 ? 436 HOH A O   1 
HETATM 2394 O  O   . HOH E 5 .   ? -1.223  -17.524 -1.850  1.00 33.74 ? 437 HOH A O   1 
HETATM 2395 O  O   . HOH E 5 .   ? -28.115 -1.154  28.451  1.00 31.82 ? 438 HOH A O   1 
HETATM 2396 O  O   . HOH E 5 .   ? -2.035  -12.004 31.397  1.00 30.83 ? 439 HOH A O   1 
HETATM 2397 O  O   . HOH E 5 .   ? -11.143 15.208  32.002  1.00 19.62 ? 440 HOH A O   1 
HETATM 2398 O  O   . HOH E 5 .   ? 5.562   8.844   22.083  1.00 31.88 ? 441 HOH A O   1 
HETATM 2399 O  O   . HOH E 5 .   ? -24.059 -2.270  28.849  1.00 32.59 ? 442 HOH A O   1 
HETATM 2400 O  O   . HOH E 5 .   ? -1.865  -17.364 25.547  1.00 24.41 ? 443 HOH A O   1 
HETATM 2401 O  O   . HOH E 5 .   ? -4.548  -15.814 0.551   1.00 25.73 ? 444 HOH A O   1 
HETATM 2402 O  O   . HOH E 5 .   ? -26.337 -7.498  30.410  1.00 32.19 ? 445 HOH A O   1 
HETATM 2403 O  O   . HOH E 5 .   ? -17.324 -16.184 22.156  1.00 27.41 ? 446 HOH A O   1 
HETATM 2404 O  O   . HOH E 5 .   ? -0.420  14.022  15.910  1.00 35.23 ? 447 HOH A O   1 
HETATM 2405 O  O   . HOH E 5 .   ? -26.013 -5.025  -3.224  1.00 46.54 ? 448 HOH A O   1 
HETATM 2406 O  O   . HOH E 5 .   ? -24.006 -0.029  31.650  1.00 35.23 ? 449 HOH A O   1 
HETATM 2407 O  O   . HOH E 5 .   ? 3.867   9.637   23.694  1.00 33.49 ? 450 HOH A O   1 
HETATM 2408 O  O   . HOH E 5 .   ? 0.174   -6.881  -7.122  1.00 28.91 ? 451 HOH A O   1 
HETATM 2409 O  O   . HOH E 5 .   ? -0.356  -20.609 14.669  1.00 44.86 ? 452 HOH A O   1 
HETATM 2410 O  O   . HOH E 5 .   ? -15.241 11.464  34.741  1.00 24.98 ? 453 HOH A O   1 
HETATM 2411 O  O   . HOH E 5 .   ? -13.037 -19.531 26.231  1.00 22.91 ? 454 HOH A O   1 
HETATM 2412 O  O   . HOH E 5 .   ? -12.392 9.745   -2.754  1.00 41.41 ? 455 HOH A O   1 
HETATM 2413 O  O   . HOH E 5 .   ? 10.432  -7.014  -8.720  1.00 28.11 ? 456 HOH A O   1 
HETATM 2414 O  O   . HOH E 5 .   ? 9.923   -4.483  -7.505  1.00 29.73 ? 457 HOH A O   1 
HETATM 2415 O  O   . HOH E 5 .   ? -23.814 -3.471  3.901   1.00 34.76 ? 458 HOH A O   1 
HETATM 2416 O  O   . HOH E 5 .   ? -14.391 3.549   33.423  1.00 29.57 ? 459 HOH A O   1 
HETATM 2417 O  O   . HOH E 5 .   ? -11.464 -15.287 34.076  1.00 31.99 ? 460 HOH A O   1 
HETATM 2418 O  O   . HOH E 5 .   ? 12.170  -11.089 -2.926  1.00 28.37 ? 461 HOH A O   1 
HETATM 2419 O  O   . HOH E 5 .   ? -24.813 4.788   7.990   1.00 37.85 ? 462 HOH A O   1 
HETATM 2420 O  O   . HOH E 5 .   ? -31.732 5.628   12.964  1.00 35.17 ? 463 HOH A O   1 
HETATM 2421 O  O   . HOH E 5 .   ? 10.473  -8.902  9.017   1.00 31.88 ? 464 HOH A O   1 
HETATM 2422 O  O   . HOH E 5 .   ? 7.063   -7.261  23.677  1.00 30.45 ? 465 HOH A O   1 
HETATM 2423 O  O   . HOH E 5 .   ? -14.147 15.742  31.765  1.00 33.11 ? 466 HOH A O   1 
HETATM 2424 O  O   . HOH E 5 .   ? -25.512 9.725   13.093  1.00 27.01 ? 467 HOH A O   1 
HETATM 2425 O  O   . HOH E 5 .   ? -18.730 20.046  14.784  1.00 26.80 ? 468 HOH A O   1 
HETATM 2426 O  O   . HOH E 5 .   ? -18.543 -3.585  -2.563  1.00 28.63 ? 469 HOH A O   1 
HETATM 2427 O  O   . HOH E 5 .   ? -12.721 3.685   -6.840  1.00 35.97 ? 470 HOH A O   1 
HETATM 2428 O  O   . HOH E 5 .   ? -26.463 -7.749  1.851   1.00 43.82 ? 471 HOH A O   1 
HETATM 2429 O  O   . HOH E 5 .   ? 5.700   9.150   18.714  1.00 32.77 ? 472 HOH A O   1 
HETATM 2430 O  O   . HOH E 5 .   ? -17.835 -12.035 31.793  1.00 33.48 ? 473 HOH A O   1 
HETATM 2431 O  O   . HOH E 5 .   ? -10.881 1.171   33.863  1.00 25.84 ? 474 HOH A O   1 
HETATM 2432 O  O   . HOH E 5 .   ? -12.921 -17.238 16.921  1.00 15.50 ? 475 HOH A O   1 
HETATM 2433 O  O   . HOH E 5 .   ? -25.329 10.989  19.475  1.00 29.99 ? 476 HOH A O   1 
HETATM 2434 O  O   . HOH E 5 .   ? -2.469  -3.198  11.319  1.00 19.62 ? 477 HOH A O   1 
HETATM 2435 O  O   . HOH E 5 .   ? -13.947 14.205  27.286  1.00 22.14 ? 478 HOH A O   1 
HETATM 2436 O  O   . HOH E 5 .   ? -1.693  -4.760  -6.955  1.00 31.92 ? 479 HOH A O   1 
HETATM 2437 O  O   . HOH E 5 .   ? -14.677 -18.513 18.837  1.00 19.02 ? 480 HOH A O   1 
HETATM 2438 O  O   . HOH E 5 .   ? 9.495   2.214   12.111  1.00 28.04 ? 481 HOH A O   1 
HETATM 2439 O  O   . HOH E 5 .   ? 6.141   -11.050 15.427  1.00 37.18 ? 482 HOH A O   1 
HETATM 2440 O  O   . HOH E 5 .   ? -15.019 19.988  17.705  1.00 25.74 ? 483 HOH A O   1 
HETATM 2441 O  O   . HOH E 5 .   ? 6.695   -5.404  3.938   1.00 28.94 ? 484 HOH A O   1 
HETATM 2442 O  O   . HOH E 5 .   ? -5.266  2.409   12.144  1.00 27.25 ? 485 HOH A O   1 
HETATM 2443 O  O   . HOH E 5 .   ? -4.080  0.641   13.741  1.00 18.44 ? 486 HOH A O   1 
HETATM 2444 O  O   . HOH E 5 .   ? -13.035 -22.048 8.508   1.00 20.22 ? 487 HOH A O   1 
HETATM 2445 O  O   . HOH E 5 .   ? -23.751 8.237   3.514   1.00 26.73 ? 488 HOH A O   1 
HETATM 2446 O  O   . HOH E 5 .   ? -16.901 -17.790 20.216  1.00 25.34 ? 489 HOH A O   1 
HETATM 2447 O  O   . HOH E 5 .   ? -14.929 9.328   31.518  1.00 35.09 ? 490 HOH A O   1 
HETATM 2448 O  O   . HOH E 5 .   ? 11.643  -0.374  16.062  1.00 24.39 ? 491 HOH A O   1 
HETATM 2449 O  O   . HOH E 5 .   ? -8.774  -15.005 33.397  1.00 34.75 ? 492 HOH A O   1 
HETATM 2450 O  O   . HOH E 5 .   ? 6.385   -0.389  -1.079  1.00 38.62 ? 493 HOH A O   1 
HETATM 2451 O  O   . HOH E 5 .   ? 12.969  -3.645  13.473  1.00 20.23 ? 494 HOH A O   1 
HETATM 2452 O  O   . HOH E 5 .   ? -7.074  -10.054 -4.645  1.00 25.62 ? 495 HOH A O   1 
HETATM 2453 O  O   . HOH E 5 .   ? -8.423  -18.133 -0.734  1.00 50.34 ? 496 HOH A O   1 
HETATM 2454 O  O   . HOH E 5 .   ? -9.241  5.933   29.297  1.00 27.79 ? 497 HOH A O   1 
HETATM 2455 O  O   . HOH E 5 .   ? 5.727   1.467   8.241   1.00 36.59 ? 498 HOH A O   1 
HETATM 2456 O  O   . HOH E 5 .   ? -23.419 -11.033 17.273  1.00 21.91 ? 499 HOH A O   1 
HETATM 2457 O  O   . HOH E 5 .   ? -21.237 -19.475 6.505   1.00 24.87 ? 500 HOH A O   1 
HETATM 2458 O  O   . HOH E 5 .   ? -27.847 6.453   21.675  1.00 35.83 ? 501 HOH A O   1 
HETATM 2459 O  O   . HOH E 5 .   ? -6.022  -11.134 36.520  1.00 30.97 ? 502 HOH A O   1 
HETATM 2460 O  O   . HOH E 5 .   ? 0.279   -14.330 31.213  1.00 40.21 ? 503 HOH A O   1 
HETATM 2461 O  O   . HOH E 5 .   ? -17.511 19.464  21.149  1.00 40.18 ? 504 HOH A O   1 
HETATM 2462 O  O   . HOH E 5 .   ? -2.591  -14.916 32.754  1.00 28.41 ? 505 HOH A O   1 
HETATM 2463 O  O   . HOH E 5 .   ? 8.125   3.047   27.909  1.00 31.15 ? 506 HOH A O   1 
HETATM 2464 O  O   . HOH E 5 .   ? -16.408 3.737   35.051  1.00 40.72 ? 507 HOH A O   1 
HETATM 2465 O  O   . HOH E 5 .   ? -24.323 13.799  20.479  1.00 41.02 ? 508 HOH A O   1 
HETATM 2466 O  O   . HOH E 5 .   ? -15.246 -19.962 23.055  1.00 34.46 ? 509 HOH A O   1 
HETATM 2467 O  O   . HOH E 5 .   ? -23.998 -0.180  1.333   1.00 30.51 ? 510 HOH A O   1 
HETATM 2468 O  O   . HOH E 5 .   ? -20.610 8.385   30.187  1.00 25.65 ? 511 HOH A O   1 
HETATM 2469 O  O   . HOH E 5 .   ? -15.921 17.340  26.130  1.00 34.06 ? 512 HOH A O   1 
HETATM 2470 O  O   . HOH E 5 .   ? -8.900  6.660   -3.803  1.00 33.37 ? 513 HOH A O   1 
HETATM 2471 O  O   . HOH E 5 .   ? 3.446   -13.565 12.247  1.00 29.65 ? 514 HOH A O   1 
HETATM 2472 O  O   . HOH E 5 .   ? -4.001  -0.838  11.709  1.00 22.27 ? 515 HOH A O   1 
HETATM 2473 O  O   . HOH E 5 .   ? -3.680  -15.603 -2.209  1.00 27.43 ? 516 HOH A O   1 
HETATM 2474 O  O   . HOH E 5 .   ? -10.717 7.897   -3.700  1.00 31.67 ? 517 HOH A O   1 
HETATM 2475 O  O   . HOH E 5 .   ? -14.917 5.825   32.810  1.00 35.79 ? 518 HOH A O   1 
HETATM 2476 O  O   . HOH E 5 .   ? -12.039 9.832   -6.292  1.00 35.29 ? 519 HOH A O   1 
HETATM 2477 O  O   . HOH E 5 .   ? -4.377  -8.545  31.225  1.00 18.91 ? 520 HOH A O   1 
HETATM 2478 O  O   . HOH E 5 .   ? -17.668 19.946  17.589  1.00 20.15 ? 521 HOH A O   1 
HETATM 2479 O  O   . HOH E 5 .   ? -12.805 6.390   31.081  1.00 33.02 ? 522 HOH A O   1 
HETATM 2480 O  O   . HOH E 5 .   ? -8.407  -17.360 34.793  1.00 26.87 ? 523 HOH A O   1 
HETATM 2481 O  O   . HOH E 5 .   ? -8.534  -19.902 26.796  1.00 24.93 ? 524 HOH A O   1 
HETATM 2482 O  O   . HOH E 5 .   ? 11.997  -6.605  7.771   1.00 25.50 ? 525 HOH A O   1 
HETATM 2483 O  O   . HOH E 5 .   ? 14.565  -6.985  7.629   1.00 30.12 ? 526 HOH A O   1 
HETATM 2484 O  O   . HOH E 5 .   ? -1.180  -11.244 29.133  1.00 17.81 ? 527 HOH A O   1 
HETATM 2485 O  O   . HOH E 5 .   ? -5.038  0.822   9.967   1.00 25.47 ? 528 HOH A O   1 
HETATM 2486 O  O   . HOH E 5 .   ? -12.835 13.099  32.046  1.00 27.68 ? 529 HOH A O   1 
HETATM 2487 O  O   . HOH E 5 .   ? 4.304   -11.465 23.547  1.00 34.82 ? 530 HOH A O   1 
HETATM 2488 O  O   . HOH E 5 .   ? 15.584  -6.016  4.681   1.00 42.43 ? 531 HOH A O   1 
HETATM 2489 O  O   . HOH E 5 .   ? -6.538  5.184   -6.198  1.00 29.75 ? 532 HOH A O   1 
HETATM 2490 O  O   . HOH E 5 .   ? -17.000 -13.959 26.433  1.00 19.53 ? 533 HOH A O   1 
HETATM 2491 O  O   . HOH E 5 .   ? -10.533 -19.410 19.873  1.00 22.70 ? 534 HOH A O   1 
HETATM 2492 O  O   . HOH E 5 .   ? -16.659 -14.935 28.673  1.00 38.31 ? 535 HOH A O   1 
HETATM 2493 O  O   . HOH E 5 .   ? 6.461   5.411   28.941  1.00 32.10 ? 536 HOH A O   1 
HETATM 2494 O  O   . HOH E 5 .   ? 1.678   12.579  22.612  1.00 27.08 ? 537 HOH A O   1 
HETATM 2495 O  O   . HOH E 5 .   ? -20.043 -15.717 22.227  1.00 31.91 ? 538 HOH A O   1 
HETATM 2496 O  O   . HOH E 5 .   ? -11.184 1.124   -7.668  1.00 34.00 ? 539 HOH A O   1 
HETATM 2497 O  O   . HOH E 5 .   ? -10.312 -11.188 -3.154  1.00 35.30 ? 540 HOH A O   1 
HETATM 2498 O  O   . HOH E 5 .   ? -3.456  5.594   -2.687  1.00 27.23 ? 541 HOH A O   1 
HETATM 2499 O  O   . HOH E 5 .   ? -21.858 -13.815 23.284  1.00 30.50 ? 542 HOH A O   1 
HETATM 2500 O  O   . HOH E 5 .   ? -4.981  -20.766 21.473  1.00 23.21 ? 543 HOH A O   1 
HETATM 2501 O  O   . HOH E 5 .   ? -10.817 8.732   7.632   1.00 29.11 ? 544 HOH A O   1 
HETATM 2502 O  O   . HOH E 5 .   ? -10.511 -20.232 24.819  1.00 26.73 ? 545 HOH A O   1 
HETATM 2503 O  O   . HOH E 5 .   ? -8.265  7.619   8.564   1.00 33.97 ? 546 HOH A O   1 
HETATM 2504 O  O   . HOH E 5 .   ? 11.177  -3.516  7.727   1.00 38.73 ? 547 HOH A O   1 
HETATM 2505 O  O   . HOH E 5 .   ? 3.835   4.550   10.835  1.00 38.81 ? 548 HOH A O   1 
HETATM 2506 O  O   . HOH E 5 .   ? 6.911   -5.925  6.823   1.00 26.12 ? 549 HOH A O   1 
HETATM 2507 O  O   . HOH E 5 .   ? -21.276 -20.391 14.621  1.00 35.82 ? 550 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   262 262 ZN  ZN  A . 
C 3 DMS 1   263 263 DMS DMS A . 
D 4 JS7 1   264 264 JS7 JS7 A . 
E 5 HOH 1   126 126 HOH HOH A . 
E 5 HOH 2   265 265 HOH HOH A . 
E 5 HOH 3   266 266 HOH HOH A . 
E 5 HOH 4   267 267 HOH HOH A . 
E 5 HOH 5   268 268 HOH HOH A . 
E 5 HOH 6   269 269 HOH HOH A . 
E 5 HOH 7   270 270 HOH HOH A . 
E 5 HOH 8   271 271 HOH HOH A . 
E 5 HOH 9   272 272 HOH HOH A . 
E 5 HOH 10  273 273 HOH HOH A . 
E 5 HOH 11  274 274 HOH HOH A . 
E 5 HOH 12  275 275 HOH HOH A . 
E 5 HOH 13  276 276 HOH HOH A . 
E 5 HOH 14  277 277 HOH HOH A . 
E 5 HOH 15  278 278 HOH HOH A . 
E 5 HOH 16  279 279 HOH HOH A . 
E 5 HOH 17  280 280 HOH HOH A . 
E 5 HOH 18  281 281 HOH HOH A . 
E 5 HOH 19  282 282 HOH HOH A . 
E 5 HOH 20  283 283 HOH HOH A . 
E 5 HOH 21  284 284 HOH HOH A . 
E 5 HOH 22  285 285 HOH HOH A . 
E 5 HOH 23  286 286 HOH HOH A . 
E 5 HOH 24  287 287 HOH HOH A . 
E 5 HOH 25  288 288 HOH HOH A . 
E 5 HOH 26  289 289 HOH HOH A . 
E 5 HOH 27  290 290 HOH HOH A . 
E 5 HOH 28  291 291 HOH HOH A . 
E 5 HOH 29  292 292 HOH HOH A . 
E 5 HOH 30  293 293 HOH HOH A . 
E 5 HOH 31  294 294 HOH HOH A . 
E 5 HOH 32  295 295 HOH HOH A . 
E 5 HOH 33  296 296 HOH HOH A . 
E 5 HOH 34  297 297 HOH HOH A . 
E 5 HOH 35  298 298 HOH HOH A . 
E 5 HOH 36  299 299 HOH HOH A . 
E 5 HOH 37  300 300 HOH HOH A . 
E 5 HOH 38  301 301 HOH HOH A . 
E 5 HOH 39  302 302 HOH HOH A . 
E 5 HOH 40  303 303 HOH HOH A . 
E 5 HOH 41  304 304 HOH HOH A . 
E 5 HOH 42  305 305 HOH HOH A . 
E 5 HOH 43  306 306 HOH HOH A . 
E 5 HOH 44  307 307 HOH HOH A . 
E 5 HOH 45  308 308 HOH HOH A . 
E 5 HOH 46  309 309 HOH HOH A . 
E 5 HOH 47  310 310 HOH HOH A . 
E 5 HOH 48  311 311 HOH HOH A . 
E 5 HOH 49  312 312 HOH HOH A . 
E 5 HOH 50  313 313 HOH HOH A . 
E 5 HOH 51  314 314 HOH HOH A . 
E 5 HOH 52  315 315 HOH HOH A . 
E 5 HOH 53  316 316 HOH HOH A . 
E 5 HOH 54  317 317 HOH HOH A . 
E 5 HOH 55  318 318 HOH HOH A . 
E 5 HOH 56  319 319 HOH HOH A . 
E 5 HOH 57  320 320 HOH HOH A . 
E 5 HOH 58  321 321 HOH HOH A . 
E 5 HOH 59  322 322 HOH HOH A . 
E 5 HOH 60  323 323 HOH HOH A . 
E 5 HOH 61  324 324 HOH HOH A . 
E 5 HOH 62  325 325 HOH HOH A . 
E 5 HOH 63  326 326 HOH HOH A . 
E 5 HOH 64  327 327 HOH HOH A . 
E 5 HOH 65  328 328 HOH HOH A . 
E 5 HOH 66  329 329 HOH HOH A . 
E 5 HOH 67  330 330 HOH HOH A . 
E 5 HOH 68  331 331 HOH HOH A . 
E 5 HOH 69  332 332 HOH HOH A . 
E 5 HOH 70  333 333 HOH HOH A . 
E 5 HOH 71  334 334 HOH HOH A . 
E 5 HOH 72  335 335 HOH HOH A . 
E 5 HOH 73  336 336 HOH HOH A . 
E 5 HOH 74  337 337 HOH HOH A . 
E 5 HOH 75  338 338 HOH HOH A . 
E 5 HOH 76  339 339 HOH HOH A . 
E 5 HOH 77  340 340 HOH HOH A . 
E 5 HOH 78  341 341 HOH HOH A . 
E 5 HOH 79  342 342 HOH HOH A . 
E 5 HOH 80  343 343 HOH HOH A . 
E 5 HOH 81  344 344 HOH HOH A . 
E 5 HOH 82  345 345 HOH HOH A . 
E 5 HOH 83  346 346 HOH HOH A . 
E 5 HOH 84  347 347 HOH HOH A . 
E 5 HOH 85  348 348 HOH HOH A . 
E 5 HOH 86  349 349 HOH HOH A . 
E 5 HOH 87  350 350 HOH HOH A . 
E 5 HOH 88  351 351 HOH HOH A . 
E 5 HOH 89  352 352 HOH HOH A . 
E 5 HOH 90  353 353 HOH HOH A . 
E 5 HOH 91  354 354 HOH HOH A . 
E 5 HOH 92  355 355 HOH HOH A . 
E 5 HOH 93  356 356 HOH HOH A . 
E 5 HOH 94  357 357 HOH HOH A . 
E 5 HOH 95  358 358 HOH HOH A . 
E 5 HOH 96  359 359 HOH HOH A . 
E 5 HOH 97  360 360 HOH HOH A . 
E 5 HOH 98  361 361 HOH HOH A . 
E 5 HOH 99  362 362 HOH HOH A . 
E 5 HOH 100 363 363 HOH HOH A . 
E 5 HOH 101 364 364 HOH HOH A . 
E 5 HOH 102 365 365 HOH HOH A . 
E 5 HOH 103 366 366 HOH HOH A . 
E 5 HOH 104 367 367 HOH HOH A . 
E 5 HOH 105 368 368 HOH HOH A . 
E 5 HOH 106 369 369 HOH HOH A . 
E 5 HOH 107 370 370 HOH HOH A . 
E 5 HOH 108 371 371 HOH HOH A . 
E 5 HOH 109 372 372 HOH HOH A . 
E 5 HOH 110 373 373 HOH HOH A . 
E 5 HOH 111 374 374 HOH HOH A . 
E 5 HOH 112 375 375 HOH HOH A . 
E 5 HOH 113 376 376 HOH HOH A . 
E 5 HOH 114 377 377 HOH HOH A . 
E 5 HOH 115 378 378 HOH HOH A . 
E 5 HOH 116 379 379 HOH HOH A . 
E 5 HOH 117 380 380 HOH HOH A . 
E 5 HOH 118 381 381 HOH HOH A . 
E 5 HOH 119 382 382 HOH HOH A . 
E 5 HOH 120 383 383 HOH HOH A . 
E 5 HOH 121 384 384 HOH HOH A . 
E 5 HOH 122 385 385 HOH HOH A . 
E 5 HOH 123 386 386 HOH HOH A . 
E 5 HOH 124 387 387 HOH HOH A . 
E 5 HOH 125 388 388 HOH HOH A . 
E 5 HOH 126 389 389 HOH HOH A . 
E 5 HOH 127 390 390 HOH HOH A . 
E 5 HOH 128 391 391 HOH HOH A . 
E 5 HOH 129 392 392 HOH HOH A . 
E 5 HOH 130 393 393 HOH HOH A . 
E 5 HOH 131 394 394 HOH HOH A . 
E 5 HOH 132 395 395 HOH HOH A . 
E 5 HOH 133 396 396 HOH HOH A . 
E 5 HOH 134 397 397 HOH HOH A . 
E 5 HOH 135 398 398 HOH HOH A . 
E 5 HOH 136 399 399 HOH HOH A . 
E 5 HOH 137 400 400 HOH HOH A . 
E 5 HOH 138 401 401 HOH HOH A . 
E 5 HOH 139 402 402 HOH HOH A . 
E 5 HOH 140 403 403 HOH HOH A . 
E 5 HOH 141 404 404 HOH HOH A . 
E 5 HOH 142 405 405 HOH HOH A . 
E 5 HOH 143 406 406 HOH HOH A . 
E 5 HOH 144 407 407 HOH HOH A . 
E 5 HOH 145 408 408 HOH HOH A . 
E 5 HOH 146 409 409 HOH HOH A . 
E 5 HOH 147 410 410 HOH HOH A . 
E 5 HOH 148 411 411 HOH HOH A . 
E 5 HOH 149 412 412 HOH HOH A . 
E 5 HOH 150 413 413 HOH HOH A . 
E 5 HOH 151 414 414 HOH HOH A . 
E 5 HOH 152 415 415 HOH HOH A . 
E 5 HOH 153 416 416 HOH HOH A . 
E 5 HOH 154 417 417 HOH HOH A . 
E 5 HOH 155 418 418 HOH HOH A . 
E 5 HOH 156 419 419 HOH HOH A . 
E 5 HOH 157 420 420 HOH HOH A . 
E 5 HOH 158 421 421 HOH HOH A . 
E 5 HOH 159 422 422 HOH HOH A . 
E 5 HOH 160 423 423 HOH HOH A . 
E 5 HOH 161 424 424 HOH HOH A . 
E 5 HOH 162 425 425 HOH HOH A . 
E 5 HOH 163 426 426 HOH HOH A . 
E 5 HOH 164 427 427 HOH HOH A . 
E 5 HOH 165 428 428 HOH HOH A . 
E 5 HOH 166 429 429 HOH HOH A . 
E 5 HOH 167 430 430 HOH HOH A . 
E 5 HOH 168 431 431 HOH HOH A . 
E 5 HOH 169 432 432 HOH HOH A . 
E 5 HOH 170 433 433 HOH HOH A . 
E 5 HOH 171 434 434 HOH HOH A . 
E 5 HOH 172 435 435 HOH HOH A . 
E 5 HOH 173 436 436 HOH HOH A . 
E 5 HOH 174 437 437 HOH HOH A . 
E 5 HOH 175 438 438 HOH HOH A . 
E 5 HOH 176 439 439 HOH HOH A . 
E 5 HOH 177 440 440 HOH HOH A . 
E 5 HOH 178 441 441 HOH HOH A . 
E 5 HOH 179 442 442 HOH HOH A . 
E 5 HOH 180 443 443 HOH HOH A . 
E 5 HOH 181 444 444 HOH HOH A . 
E 5 HOH 182 445 445 HOH HOH A . 
E 5 HOH 183 446 446 HOH HOH A . 
E 5 HOH 184 447 447 HOH HOH A . 
E 5 HOH 185 448 448 HOH HOH A . 
E 5 HOH 186 449 449 HOH HOH A . 
E 5 HOH 187 450 450 HOH HOH A . 
E 5 HOH 188 451 451 HOH HOH A . 
E 5 HOH 189 452 452 HOH HOH A . 
E 5 HOH 190 453 453 HOH HOH A . 
E 5 HOH 191 454 454 HOH HOH A . 
E 5 HOH 192 455 455 HOH HOH A . 
E 5 HOH 193 456 456 HOH HOH A . 
E 5 HOH 194 457 457 HOH HOH A . 
E 5 HOH 195 458 458 HOH HOH A . 
E 5 HOH 196 459 459 HOH HOH A . 
E 5 HOH 197 460 460 HOH HOH A . 
E 5 HOH 198 461 461 HOH HOH A . 
E 5 HOH 199 462 462 HOH HOH A . 
E 5 HOH 200 463 463 HOH HOH A . 
E 5 HOH 201 464 464 HOH HOH A . 
E 5 HOH 202 465 465 HOH HOH A . 
E 5 HOH 203 466 466 HOH HOH A . 
E 5 HOH 204 467 467 HOH HOH A . 
E 5 HOH 205 468 468 HOH HOH A . 
E 5 HOH 206 469 469 HOH HOH A . 
E 5 HOH 207 470 470 HOH HOH A . 
E 5 HOH 208 471 471 HOH HOH A . 
E 5 HOH 209 472 472 HOH HOH A . 
E 5 HOH 210 473 473 HOH HOH A . 
E 5 HOH 211 474 474 HOH HOH A . 
E 5 HOH 212 475 475 HOH HOH A . 
E 5 HOH 213 476 476 HOH HOH A . 
E 5 HOH 214 477 477 HOH HOH A . 
E 5 HOH 215 478 478 HOH HOH A . 
E 5 HOH 216 479 479 HOH HOH A . 
E 5 HOH 217 480 480 HOH HOH A . 
E 5 HOH 218 481 481 HOH HOH A . 
E 5 HOH 219 482 482 HOH HOH A . 
E 5 HOH 220 483 483 HOH HOH A . 
E 5 HOH 221 484 484 HOH HOH A . 
E 5 HOH 222 485 485 HOH HOH A . 
E 5 HOH 223 486 486 HOH HOH A . 
E 5 HOH 224 487 487 HOH HOH A . 
E 5 HOH 225 488 488 HOH HOH A . 
E 5 HOH 226 489 489 HOH HOH A . 
E 5 HOH 227 490 490 HOH HOH A . 
E 5 HOH 228 491 491 HOH HOH A . 
E 5 HOH 229 492 492 HOH HOH A . 
E 5 HOH 230 493 493 HOH HOH A . 
E 5 HOH 231 494 494 HOH HOH A . 
E 5 HOH 232 495 495 HOH HOH A . 
E 5 HOH 233 496 496 HOH HOH A . 
E 5 HOH 234 497 497 HOH HOH A . 
E 5 HOH 235 498 498 HOH HOH A . 
E 5 HOH 236 499 499 HOH HOH A . 
E 5 HOH 237 500 500 HOH HOH A . 
E 5 HOH 238 501 501 HOH HOH A . 
E 5 HOH 239 502 502 HOH HOH A . 
E 5 HOH 240 503 503 HOH HOH A . 
E 5 HOH 241 504 504 HOH HOH A . 
E 5 HOH 242 505 505 HOH HOH A . 
E 5 HOH 243 506 506 HOH HOH A . 
E 5 HOH 244 507 507 HOH HOH A . 
E 5 HOH 245 508 508 HOH HOH A . 
E 5 HOH 246 509 509 HOH HOH A . 
E 5 HOH 247 510 510 HOH HOH A . 
E 5 HOH 248 511 511 HOH HOH A . 
E 5 HOH 249 512 512 HOH HOH A . 
E 5 HOH 250 513 513 HOH HOH A . 
E 5 HOH 251 514 514 HOH HOH A . 
E 5 HOH 252 515 515 HOH HOH A . 
E 5 HOH 253 516 516 HOH HOH A . 
E 5 HOH 254 517 517 HOH HOH A . 
E 5 HOH 255 518 518 HOH HOH A . 
E 5 HOH 256 519 519 HOH HOH A . 
E 5 HOH 257 520 520 HOH HOH A . 
E 5 HOH 258 521 521 HOH HOH A . 
E 5 HOH 259 522 522 HOH HOH A . 
E 5 HOH 260 523 523 HOH HOH A . 
E 5 HOH 261 524 524 HOH HOH A . 
E 5 HOH 262 525 525 HOH HOH A . 
E 5 HOH 263 526 526 HOH HOH A . 
E 5 HOH 264 527 527 HOH HOH A . 
E 5 HOH 265 528 528 HOH HOH A . 
E 5 HOH 266 529 529 HOH HOH A . 
E 5 HOH 267 530 530 HOH HOH A . 
E 5 HOH 268 531 531 HOH HOH A . 
E 5 HOH 269 532 532 HOH HOH A . 
E 5 HOH 270 533 533 HOH HOH A . 
E 5 HOH 271 534 534 HOH HOH A . 
E 5 HOH 272 535 535 HOH HOH A . 
E 5 HOH 273 536 536 HOH HOH A . 
E 5 HOH 274 537 537 HOH HOH A . 
E 5 HOH 275 538 538 HOH HOH A . 
E 5 HOH 276 539 539 HOH HOH A . 
E 5 HOH 277 540 540 HOH HOH A . 
E 5 HOH 278 541 541 HOH HOH A . 
E 5 HOH 279 542 542 HOH HOH A . 
E 5 HOH 280 543 543 HOH HOH A . 
E 5 HOH 281 544 544 HOH HOH A . 
E 5 HOH 282 545 545 HOH HOH A . 
E 5 HOH 283 546 546 HOH HOH A . 
E 5 HOH 284 547 547 HOH HOH A . 
E 5 HOH 285 548 548 HOH HOH A . 
E 5 HOH 286 549 549 HOH HOH A . 
E 5 HOH 287 550 550 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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2010-10-20 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-08 
4 'Structure model' 1 3 2023-11-01 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' Advisory                    
3 3 'Structure model' 'Refinement description'    
4 4 'Structure model' Advisory                    
5 4 'Structure model' 'Data collection'           
6 4 'Structure model' 'Database references'       
7 4 'Structure model' 'Derived calculations'      
8 4 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' pdbx_unobs_or_zero_occ_atoms  
2 3 'Structure model' software                      
3 4 'Structure model' chem_comp_atom                
4 4 'Structure model' chem_comp_bond                
5 4 'Structure model' database_2                    
6 4 'Structure model' diffrn_source                 
7 4 'Structure model' pdbx_initial_refinement_model 
8 4 'Structure model' pdbx_unobs_or_zero_occ_atoms  
9 4 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_software.name'                       
2 4 'Structure model' '_database_2.pdbx_DOI'                 
3 4 'Structure model' '_database_2.pdbx_database_accession'  
4 4 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
5 4 'Structure model' '_struct_site.pdbx_auth_asym_id'       
6 4 'Structure model' '_struct_site.pdbx_auth_comp_id'       
7 4 'Structure model' '_struct_site.pdbx_auth_seq_id'        
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .                            ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .                            ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.2.25                       21/9/2006       other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006                        'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345      'v. 0.9.7 on RedHat Linux 8' ?               ?       ?                    ?                        'data collection' ? 
?          ? 5 
O           .                            ?               ?       ?                    ?                        'model building'  ? 
?          ? 6 
# 
_pdbx_entry_details.entry_id                 3M3X 
_pdbx_entry_details.nonpolymer_details       'METAL ION NATURALLY OCCURS IN CARBONIC ANHYDRASES.' 
_pdbx_entry_details.sequence_details         '126 IS SKIPPED IN THE NUMBERING.' 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE1 A GLN 136 ? B O A HOH 537 ? ? 2.05 
2 1 O   A LYS 76  ? ? O A HOH 467 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH1 A ARG 27  ? ? 124.75 120.30 4.45  0.50 N 
2 1 NE A ARG 27  ? ? CZ A ARG 27  ? ? NH2 A ARG 27  ? ? 114.82 120.30 -5.48 0.50 N 
3 1 CB A ASP 101 ? ? CG A ASP 101 ? ? OD1 A ASP 101 ? ? 125.94 118.30 7.64  0.90 N 
4 1 CB A ASP 130 ? ? CG A ASP 130 ? ? OD1 A ASP 130 ? ? 124.99 118.30 6.69  0.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -142.79 55.74   
2 1 PRO A 42  ? ? -59.88  -9.62   
3 1 ALA A 65  ? ? -171.15 -166.62 
4 1 LYS A 170 ? B -31.41  132.37  
5 1 PHE A 176 ? ? -160.14 78.43   
6 1 ASN A 244 ? ? -100.00 49.31   
7 1 LYS A 252 ? A 50.08   -134.70 
8 1 LYS A 252 ? B 54.80   -133.61 
# 
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 Y 0 A LYS 9 ? CD ? A LYS 9 CD 
2 1 Y 0 A LYS 9 ? CE ? A LYS 9 CE 
3 1 Y 0 A LYS 9 ? NZ ? A LYS 9 NZ 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
JS7 N1   N  Y N 193 
JS7 C2   C  Y N 194 
JS7 N3   N  Y N 195 
JS7 C4   C  Y N 196 
JS7 C5   C  Y N 197 
JS7 C6   C  Y N 198 
JS7 N7   N  N N 199 
JS7 C8   C  Y N 200 
JS7 C9   C  Y N 201 
JS7 C10  C  Y N 202 
JS7 C11  C  Y N 203 
JS7 C12  C  Y N 204 
JS7 C13  C  Y N 205 
JS7 S14  S  N N 206 
JS7 O15  O  N N 207 
JS7 O16  O  N N 208 
JS7 N17  N  N N 209 
JS7 N18  N  N N 210 
JS7 O19  O  N N 211 
JS7 O20  O  N N 212 
JS7 O21  O  N N 213 
JS7 C22  C  N N 214 
JS7 C23  C  N N 215 
JS7 C24  C  N N 216 
JS7 H2   H  N N 217 
JS7 HN7  H  N N 218 
JS7 H9   H  N N 219 
JS7 H10  H  N N 220 
JS7 H12  H  N N 221 
JS7 H13  H  N N 222 
JS7 HN17 H  N N 223 
JS7 HN1A H  N N 224 
JS7 H22  H  N N 225 
JS7 H22A H  N N 226 
JS7 H22B H  N N 227 
JS7 H23  H  N N 228 
JS7 H23A H  N N 229 
JS7 H24  H  N N 230 
JS7 H24A H  N N 231 
LEU N    N  N N 232 
LEU CA   C  N S 233 
LEU C    C  N N 234 
LEU O    O  N N 235 
LEU CB   C  N N 236 
LEU CG   C  N N 237 
LEU CD1  C  N N 238 
LEU CD2  C  N N 239 
LEU OXT  O  N N 240 
LEU H    H  N N 241 
LEU H2   H  N N 242 
LEU HA   H  N N 243 
LEU HB2  H  N N 244 
LEU HB3  H  N N 245 
LEU HG   H  N N 246 
LEU HD11 H  N N 247 
LEU HD12 H  N N 248 
LEU HD13 H  N N 249 
LEU HD21 H  N N 250 
LEU HD22 H  N N 251 
LEU HD23 H  N N 252 
LEU HXT  H  N N 253 
LYS N    N  N N 254 
LYS CA   C  N S 255 
LYS C    C  N N 256 
LYS O    O  N N 257 
LYS CB   C  N N 258 
LYS CG   C  N N 259 
LYS CD   C  N N 260 
LYS CE   C  N N 261 
LYS NZ   N  N N 262 
LYS OXT  O  N N 263 
LYS H    H  N N 264 
LYS H2   H  N N 265 
LYS HA   H  N N 266 
LYS HB2  H  N N 267 
LYS HB3  H  N N 268 
LYS HG2  H  N N 269 
LYS HG3  H  N N 270 
LYS HD2  H  N N 271 
LYS HD3  H  N N 272 
LYS HE2  H  N N 273 
LYS HE3  H  N N 274 
LYS HZ1  H  N N 275 
LYS HZ2  H  N N 276 
LYS HZ3  H  N N 277 
LYS HXT  H  N N 278 
MET N    N  N N 279 
MET CA   C  N S 280 
MET C    C  N N 281 
MET O    O  N N 282 
MET CB   C  N N 283 
MET CG   C  N N 284 
MET SD   S  N N 285 
MET CE   C  N N 286 
MET OXT  O  N N 287 
MET H    H  N N 288 
MET H2   H  N N 289 
MET HA   H  N N 290 
MET HB2  H  N N 291 
MET HB3  H  N N 292 
MET HG2  H  N N 293 
MET HG3  H  N N 294 
MET HE1  H  N N 295 
MET HE2  H  N N 296 
MET HE3  H  N N 297 
MET HXT  H  N N 298 
PHE N    N  N N 299 
PHE CA   C  N S 300 
PHE C    C  N N 301 
PHE O    O  N N 302 
PHE CB   C  N N 303 
PHE CG   C  Y N 304 
PHE CD1  C  Y N 305 
PHE CD2  C  Y N 306 
PHE CE1  C  Y N 307 
PHE CE2  C  Y N 308 
PHE CZ   C  Y N 309 
PHE OXT  O  N N 310 
PHE H    H  N N 311 
PHE H2   H  N N 312 
PHE HA   H  N N 313 
PHE HB2  H  N N 314 
PHE HB3  H  N N 315 
PHE HD1  H  N N 316 
PHE HD2  H  N N 317 
PHE HE1  H  N N 318 
PHE HE2  H  N N 319 
PHE HZ   H  N N 320 
PHE HXT  H  N N 321 
PRO N    N  N N 322 
PRO CA   C  N S 323 
PRO C    C  N N 324 
PRO O    O  N N 325 
PRO CB   C  N N 326 
PRO CG   C  N N 327 
PRO CD   C  N N 328 
PRO OXT  O  N N 329 
PRO H    H  N N 330 
PRO HA   H  N N 331 
PRO HB2  H  N N 332 
PRO HB3  H  N N 333 
PRO HG2  H  N N 334 
PRO HG3  H  N N 335 
PRO HD2  H  N N 336 
PRO HD3  H  N N 337 
PRO HXT  H  N N 338 
SER N    N  N N 339 
SER CA   C  N S 340 
SER C    C  N N 341 
SER O    O  N N 342 
SER CB   C  N N 343 
SER OG   O  N N 344 
SER OXT  O  N N 345 
SER H    H  N N 346 
SER H2   H  N N 347 
SER HA   H  N N 348 
SER HB2  H  N N 349 
SER HB3  H  N N 350 
SER HG   H  N N 351 
SER HXT  H  N N 352 
THR N    N  N N 353 
THR CA   C  N S 354 
THR C    C  N N 355 
THR O    O  N N 356 
THR CB   C  N R 357 
THR OG1  O  N N 358 
THR CG2  C  N N 359 
THR OXT  O  N N 360 
THR H    H  N N 361 
THR H2   H  N N 362 
THR HA   H  N N 363 
THR HB   H  N N 364 
THR HG1  H  N N 365 
THR HG21 H  N N 366 
THR HG22 H  N N 367 
THR HG23 H  N N 368 
THR HXT  H  N N 369 
TRP N    N  N N 370 
TRP CA   C  N S 371 
TRP C    C  N N 372 
TRP O    O  N N 373 
TRP CB   C  N N 374 
TRP CG   C  Y N 375 
TRP CD1  C  Y N 376 
TRP CD2  C  Y N 377 
TRP NE1  N  Y N 378 
TRP CE2  C  Y N 379 
TRP CE3  C  Y N 380 
TRP CZ2  C  Y N 381 
TRP CZ3  C  Y N 382 
TRP CH2  C  Y N 383 
TRP OXT  O  N N 384 
TRP H    H  N N 385 
TRP H2   H  N N 386 
TRP HA   H  N N 387 
TRP HB2  H  N N 388 
TRP HB3  H  N N 389 
TRP HD1  H  N N 390 
TRP HE1  H  N N 391 
TRP HE3  H  N N 392 
TRP HZ2  H  N N 393 
TRP HZ3  H  N N 394 
TRP HH2  H  N N 395 
TRP HXT  H  N N 396 
TYR N    N  N N 397 
TYR CA   C  N S 398 
TYR C    C  N N 399 
TYR O    O  N N 400 
TYR CB   C  N N 401 
TYR CG   C  Y N 402 
TYR CD1  C  Y N 403 
TYR CD2  C  Y N 404 
TYR CE1  C  Y N 405 
TYR CE2  C  Y N 406 
TYR CZ   C  Y N 407 
TYR OH   O  N N 408 
TYR OXT  O  N N 409 
TYR H    H  N N 410 
TYR H2   H  N N 411 
TYR HA   H  N N 412 
TYR HB2  H  N N 413 
TYR HB3  H  N N 414 
TYR HD1  H  N N 415 
TYR HD2  H  N N 416 
TYR HE1  H  N N 417 
TYR HE2  H  N N 418 
TYR HH   H  N N 419 
TYR HXT  H  N N 420 
VAL N    N  N N 421 
VAL CA   C  N S 422 
VAL C    C  N N 423 
VAL O    O  N N 424 
VAL CB   C  N N 425 
VAL CG1  C  N N 426 
VAL CG2  C  N N 427 
VAL OXT  O  N N 428 
VAL H    H  N N 429 
VAL H2   H  N N 430 
VAL HA   H  N N 431 
VAL HB   H  N N 432 
VAL HG11 H  N N 433 
VAL HG12 H  N N 434 
VAL HG13 H  N N 435 
VAL HG21 H  N N 436 
VAL HG22 H  N N 437 
VAL HG23 H  N N 438 
VAL HXT  H  N N 439 
ZN  ZN   ZN N N 440 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
JS7 N1  C2   doub Y N 182 
JS7 N1  C6   sing Y N 183 
JS7 C2  N3   sing Y N 184 
JS7 N3  C4   doub Y N 185 
JS7 C4  C5   sing Y N 186 
JS7 C4  N7   sing N N 187 
JS7 C5  C6   doub Y N 188 
JS7 C5  N18  sing N N 189 
JS7 C6  O21  sing N N 190 
JS7 N7  C23  sing N N 191 
JS7 C8  C9   doub Y N 192 
JS7 C8  C13  sing Y N 193 
JS7 C8  C24  sing N N 194 
JS7 C9  C10  sing Y N 195 
JS7 C10 C11  doub Y N 196 
JS7 C11 C12  sing Y N 197 
JS7 C11 S14  sing N N 198 
JS7 C12 C13  doub Y N 199 
JS7 S14 O15  doub N N 200 
JS7 S14 O16  doub N N 201 
JS7 S14 N17  sing N N 202 
JS7 N18 O19  sing N N 203 
JS7 N18 O20  doub N N 204 
JS7 O21 C22  sing N N 205 
JS7 C23 C24  sing N N 206 
JS7 C2  H2   sing N N 207 
JS7 N7  HN7  sing N N 208 
JS7 C9  H9   sing N N 209 
JS7 C10 H10  sing N N 210 
JS7 C12 H12  sing N N 211 
JS7 C13 H13  sing N N 212 
JS7 N17 HN17 sing N N 213 
JS7 N17 HN1A sing N N 214 
JS7 C22 H22  sing N N 215 
JS7 C22 H22A sing N N 216 
JS7 C22 H22B sing N N 217 
JS7 C23 H23  sing N N 218 
JS7 C23 H23A sing N N 219 
JS7 C24 H24  sing N N 220 
JS7 C24 H24A sing N N 221 
LEU N   CA   sing N N 222 
LEU N   H    sing N N 223 
LEU N   H2   sing N N 224 
LEU CA  C    sing N N 225 
LEU CA  CB   sing N N 226 
LEU CA  HA   sing N N 227 
LEU C   O    doub N N 228 
LEU C   OXT  sing N N 229 
LEU CB  CG   sing N N 230 
LEU CB  HB2  sing N N 231 
LEU CB  HB3  sing N N 232 
LEU CG  CD1  sing N N 233 
LEU CG  CD2  sing N N 234 
LEU CG  HG   sing N N 235 
LEU CD1 HD11 sing N N 236 
LEU CD1 HD12 sing N N 237 
LEU CD1 HD13 sing N N 238 
LEU CD2 HD21 sing N N 239 
LEU CD2 HD22 sing N N 240 
LEU CD2 HD23 sing N N 241 
LEU OXT HXT  sing N N 242 
LYS N   CA   sing N N 243 
LYS N   H    sing N N 244 
LYS N   H2   sing N N 245 
LYS CA  C    sing N N 246 
LYS CA  CB   sing N N 247 
LYS CA  HA   sing N N 248 
LYS C   O    doub N N 249 
LYS C   OXT  sing N N 250 
LYS CB  CG   sing N N 251 
LYS CB  HB2  sing N N 252 
LYS CB  HB3  sing N N 253 
LYS CG  CD   sing N N 254 
LYS CG  HG2  sing N N 255 
LYS CG  HG3  sing N N 256 
LYS CD  CE   sing N N 257 
LYS CD  HD2  sing N N 258 
LYS CD  HD3  sing N N 259 
LYS CE  NZ   sing N N 260 
LYS CE  HE2  sing N N 261 
LYS CE  HE3  sing N N 262 
LYS NZ  HZ1  sing N N 263 
LYS NZ  HZ2  sing N N 264 
LYS NZ  HZ3  sing N N 265 
LYS OXT HXT  sing N N 266 
MET N   CA   sing N N 267 
MET N   H    sing N N 268 
MET N   H2   sing N N 269 
MET CA  C    sing N N 270 
MET CA  CB   sing N N 271 
MET CA  HA   sing N N 272 
MET C   O    doub N N 273 
MET C   OXT  sing N N 274 
MET CB  CG   sing N N 275 
MET CB  HB2  sing N N 276 
MET CB  HB3  sing N N 277 
MET CG  SD   sing N N 278 
MET CG  HG2  sing N N 279 
MET CG  HG3  sing N N 280 
MET SD  CE   sing N N 281 
MET CE  HE1  sing N N 282 
MET CE  HE2  sing N N 283 
MET CE  HE3  sing N N 284 
MET OXT HXT  sing N N 285 
PHE N   CA   sing N N 286 
PHE N   H    sing N N 287 
PHE N   H2   sing N N 288 
PHE CA  C    sing N N 289 
PHE CA  CB   sing N N 290 
PHE CA  HA   sing N N 291 
PHE C   O    doub N N 292 
PHE C   OXT  sing N N 293 
PHE CB  CG   sing N N 294 
PHE CB  HB2  sing N N 295 
PHE CB  HB3  sing N N 296 
PHE CG  CD1  doub Y N 297 
PHE CG  CD2  sing Y N 298 
PHE CD1 CE1  sing Y N 299 
PHE CD1 HD1  sing N N 300 
PHE CD2 CE2  doub Y N 301 
PHE CD2 HD2  sing N N 302 
PHE CE1 CZ   doub Y N 303 
PHE CE1 HE1  sing N N 304 
PHE CE2 CZ   sing Y N 305 
PHE CE2 HE2  sing N N 306 
PHE CZ  HZ   sing N N 307 
PHE OXT HXT  sing N N 308 
PRO N   CA   sing N N 309 
PRO N   CD   sing N N 310 
PRO N   H    sing N N 311 
PRO CA  C    sing N N 312 
PRO CA  CB   sing N N 313 
PRO CA  HA   sing N N 314 
PRO C   O    doub N N 315 
PRO C   OXT  sing N N 316 
PRO CB  CG   sing N N 317 
PRO CB  HB2  sing N N 318 
PRO CB  HB3  sing N N 319 
PRO CG  CD   sing N N 320 
PRO CG  HG2  sing N N 321 
PRO CG  HG3  sing N N 322 
PRO CD  HD2  sing N N 323 
PRO CD  HD3  sing N N 324 
PRO OXT HXT  sing N N 325 
SER N   CA   sing N N 326 
SER N   H    sing N N 327 
SER N   H2   sing N N 328 
SER CA  C    sing N N 329 
SER CA  CB   sing N N 330 
SER CA  HA   sing N N 331 
SER C   O    doub N N 332 
SER C   OXT  sing N N 333 
SER CB  OG   sing N N 334 
SER CB  HB2  sing N N 335 
SER CB  HB3  sing N N 336 
SER OG  HG   sing N N 337 
SER OXT HXT  sing N N 338 
THR N   CA   sing N N 339 
THR N   H    sing N N 340 
THR N   H2   sing N N 341 
THR CA  C    sing N N 342 
THR CA  CB   sing N N 343 
THR CA  HA   sing N N 344 
THR C   O    doub N N 345 
THR C   OXT  sing N N 346 
THR CB  OG1  sing N N 347 
THR CB  CG2  sing N N 348 
THR CB  HB   sing N N 349 
THR OG1 HG1  sing N N 350 
THR CG2 HG21 sing N N 351 
THR CG2 HG22 sing N N 352 
THR CG2 HG23 sing N N 353 
THR OXT HXT  sing N N 354 
TRP N   CA   sing N N 355 
TRP N   H    sing N N 356 
TRP N   H2   sing N N 357 
TRP CA  C    sing N N 358 
TRP CA  CB   sing N N 359 
TRP CA  HA   sing N N 360 
TRP C   O    doub N N 361 
TRP C   OXT  sing N N 362 
TRP CB  CG   sing N N 363 
TRP CB  HB2  sing N N 364 
TRP CB  HB3  sing N N 365 
TRP CG  CD1  doub Y N 366 
TRP CG  CD2  sing Y N 367 
TRP CD1 NE1  sing Y N 368 
TRP CD1 HD1  sing N N 369 
TRP CD2 CE2  doub Y N 370 
TRP CD2 CE3  sing Y N 371 
TRP NE1 CE2  sing Y N 372 
TRP NE1 HE1  sing N N 373 
TRP CE2 CZ2  sing Y N 374 
TRP CE3 CZ3  doub Y N 375 
TRP CE3 HE3  sing N N 376 
TRP CZ2 CH2  doub Y N 377 
TRP CZ2 HZ2  sing N N 378 
TRP CZ3 CH2  sing Y N 379 
TRP CZ3 HZ3  sing N N 380 
TRP CH2 HH2  sing N N 381 
TRP OXT HXT  sing N N 382 
TYR N   CA   sing N N 383 
TYR N   H    sing N N 384 
TYR N   H2   sing N N 385 
TYR CA  C    sing N N 386 
TYR CA  CB   sing N N 387 
TYR CA  HA   sing N N 388 
TYR C   O    doub N N 389 
TYR C   OXT  sing N N 390 
TYR CB  CG   sing N N 391 
TYR CB  HB2  sing N N 392 
TYR CB  HB3  sing N N 393 
TYR CG  CD1  doub Y N 394 
TYR CG  CD2  sing Y N 395 
TYR CD1 CE1  sing Y N 396 
TYR CD1 HD1  sing N N 397 
TYR CD2 CE2  doub Y N 398 
TYR CD2 HD2  sing N N 399 
TYR CE1 CZ   doub Y N 400 
TYR CE1 HE1  sing N N 401 
TYR CE2 CZ   sing Y N 402 
TYR CE2 HE2  sing N N 403 
TYR CZ  OH   sing N N 404 
TYR OH  HH   sing N N 405 
TYR OXT HXT  sing N N 406 
VAL N   CA   sing N N 407 
VAL N   H    sing N N 408 
VAL N   H2   sing N N 409 
VAL CA  C    sing N N 410 
VAL CA  CB   sing N N 411 
VAL CA  HA   sing N N 412 
VAL C   O    doub N N 413 
VAL C   OXT  sing N N 414 
VAL CB  CG1  sing N N 415 
VAL CB  CG2  sing N N 416 
VAL CB  HB   sing N N 417 
VAL CG1 HG11 sing N N 418 
VAL CG1 HG12 sing N N 419 
VAL CG1 HG13 sing N N 420 
VAL CG2 HG21 sing N N 421 
VAL CG2 HG22 sing N N 422 
VAL CG2 HG23 sing N N 423 
VAL OXT HXT  sing N N 424 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                              ZN  
3 'DIMETHYL SULFOXIDE'                                                    DMS 
4 '4-{2-[(6-methoxy-5-nitropyrimidin-4-yl)amino]ethyl}benzenesulfonamide' JS7 
5 water                                                                   HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2NNO 
_pdbx_initial_refinement_model.details          'PDB ENTRY 2NNO' 
# 
