data_4PYY
# 
_entry.id   4PYY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_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   4PYY         pdb_00004pyy 10.2210/pdb4pyy/pdb 
RCSB  RCSB085394   ?            ?                   
WWPDB D_1000085394 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4PYX . unspecified 
PDB 4PZH . unspecified 
PDB 4Q06 . unspecified 
PDB 4Q07 . unspecified 
PDB 4Q08 . unspecified 
PDB 4Q09 . unspecified 
PDB 4Q0L . unspecified 
# 
_pdbx_database_status.entry_id                        4PYY 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2014-03-28 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     'Discovery and characterization of novel selective inhibitors of carbonic anhydrase IX.' 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_volume            57 
_citation.page_first                9435 
_citation.page_last                 9446 
_citation.year                      2014 
_citation.journal_id_ASTM           JMCMAR 
_citation.country                   US 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_id_CSD            0151 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25358084 
_citation.pdbx_database_id_DOI      10.1021/jm501003k 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dudutiene, V.'      1  ? 
primary 'Matuliene, J.'      2  ? 
primary 'Smirnov, A.'        3  ? 
primary 'Timm, D.D.'         4  ? 
primary 'Zubriene, A.'       5  ? 
primary 'Baranauskiene, L.'  6  ? 
primary 'Morkunaite, V.'     7  ? 
primary 'Smirnoviene, J.'    8  ? 
primary 'Michailoviene, V.'  9  ? 
primary 'Juozapaitiene, V.'  10 ? 
primary 'Mickeviciute, A.'   11 ? 
primary 'Kazokaite, J.'      12 ? 
primary 'Baksyte, S.'        13 ? 
primary 'Kasiliauskaite, A.' 14 ? 
primary 'Jachno, J.'         15 ? 
primary 'Revuckiene, J.'     16 ? 
primary 'Kisonaite, M.'      17 ? 
primary 'Pilipuityte, V.'    18 ? 
primary 'Ivanauskaite, E.'   19 ? 
primary 'Milinaviciute, G.'  20 ? 
primary 'Smirnovas, V.'      21 ? 
primary 'Petrikaite, V.'     22 ? 
primary 'Kairys, V.'         23 ? 
primary 'Petrauskas, V.'     24 ? 
primary 'Norvaisas, P.'      25 ? 
primary 'Linge, D.'          26 ? 
primary 'Gibieza, P.'        27 ? 
primary 'Capkauskaite, E.'   28 ? 
primary 'Zaksauskas, A.'     29 ? 
primary 'Kazlauskas, E.'     30 ? 
primary 'Manakova, E.'       31 ? 
primary 'Grazulis, S.'       32 ? 
primary 'Ladbury, J.E.'      33 ? 
primary 'Matulis, D.'        34 ? 
# 
_cell.entry_id           4PYY 
_cell.length_a           42.240 
_cell.length_b           41.519 
_cell.length_c           71.936 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.420 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              2 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4PYY 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                               29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                           65.409    1   ?       ? ? ? 
3 non-polymer syn '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 444.489   1   ?       ? ? ? 
4 water       nat water                                                                                18.015    296 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     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              4PYY 
_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 
GLN 'L-peptide linking' y GLUTAMINE                                                                            ? 'C5 H10 N2 O3' 
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                      ? 'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                                              ? 'C2 H5 N O2' 
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                            ? 'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                                                                ? 'H2 O' 18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                           ? 'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                              ? 'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking' y LYSINE                                                                               ? 'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking' y METHIONINE                                                                           ? 'C5 H11 N O2 S' 
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                        ? 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                              ? 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                               ? 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                                            ? 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                           ? 'C11 H12 N2 O2' 
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                             ? 'C9 H11 N O3' 
181.189 
V14 non-polymer         . '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 
'C16 H23 F3 N2 O5 S2' 444.489 
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          4PYY 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   39.2 
_exptl_crystal.density_Matthews      2.04 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate, VAPOR DIFFUSION, SITTING DROP, temperature 291K
;
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS IV++' 
_diffrn_detector.pdbx_collection_date   2012-08-03 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'VARIMAX-HF MIRROR' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
# 
_reflns.entry_id                     4PYY 
_reflns.d_resolution_high            1.750 
_reflns.d_resolution_low             24.602 
_reflns.number_all                   ? 
_reflns.number_obs                   24612 
_reflns.pdbx_netI_over_sigmaI        10.800 
_reflns.pdbx_Rsym_value              0.060 
_reflns.pdbx_redundancy              3.600 
_reflns.percent_possible_obs         99.900 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        15.182 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.75 1.84  ? 12573 ? 0.133 4.6  0.133 ? 3.50 ? 3589 99.80  1  1 
1.84 1.96  ? 11780 ? 0.087 6.8  0.087 ? 3.50 ? 3337 99.90  2  1 
1.96 2.09  ? 11295 ? 0.069 8.9  0.069 ? 3.60 ? 3178 100.00 3  1 
2.09 2.26  ? 10584 ? 0.062 8.9  0.062 ? 3.60 ? 2956 100.00 4  1 
2.26 2.47  ? 9976  ? 0.057 9.9  0.057 ? 3.60 ? 2756 100.00 5  1 
2.47 2.77  ? 8978  ? 0.054 10.6 0.054 ? 3.60 ? 2472 100.00 6  1 
2.77 3.20  ? 7976  ? 0.052 8.5  0.052 ? 3.70 ? 2181 100.00 7  1 
3.20 3.91  ? 6826  ? 0.055 9.5  0.055 ? 3.70 ? 1863 100.00 8  1 
3.91 5.53  ? 5313  ? 0.055 9.0  0.055 ? 3.60 ? 1464 100.00 9  1 
5.53 24.60 ? 2803  ? 0.068 5.6  0.068 ? 3.40 ? 816  98.80  10 1 
# 
_refine.entry_id                                 4PYY 
_refine.ls_d_res_high                            1.750 
_refine.ls_d_res_low                             23.760 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.860 
_refine.ls_number_reflns_obs                     24599 
_refine.ls_number_reflns_all                     24599 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          0.154 
_refine.ls_R_factor_obs                          0.154 
_refine.ls_R_factor_R_work                       0.149 
_refine.ls_wR_factor_R_work                      0.164 
_refine.ls_R_factor_R_free                       0.200 
_refine.ls_wR_factor_R_free                      0.222 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  2487 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               15.231 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.110 
_refine.aniso_B[2][2]                            -0.180 
_refine.aniso_B[3][3]                            0.130 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.110 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_refine.overall_SU_R_Cruickshank_DPI             0.121 
_refine.overall_SU_R_free                        0.121 
_refine.pdbx_overall_ESU_R                       0.121 
_refine.pdbx_overall_ESU_R_Free                  0.121 
_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          MR 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.888 
_refine.B_iso_max                                60.77 
_refine.B_iso_min                                5.19 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 3HLJ' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             296 
_refine_hist.number_atoms_total               2374 
_refine_hist.d_res_high                       1.750 
_refine_hist.d_res_low                        23.760 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       2238 0.020  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    3054 2.138  1.981  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 270  6.976  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 101  35.785 24.851 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 366  13.501 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 7    23.027 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         314  0.156  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   1723 0.013  0.021  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.750 
_refine_ls_shell.d_res_low                        1.795 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               99.500 
_refine_ls_shell.number_reflns_R_work             1610 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.253 
_refine_ls_shell.R_factor_R_free                  0.353 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             191 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                1801 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4PYY 
_struct.title                     'Crystal structure of human carbonic anhydrase isozyme II with inhibitor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4PYY 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_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 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P2 2 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P3 3 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P4 4 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P5 5 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P6 6 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P7 7 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P8 8 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V14 . N10 A ? A ZN  301 A V14 302 1_555 ? ? ? ? ? ? ? 1.900 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V14 . N10 B ? A ZN  301 A V14 302 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -4.86 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 11.03 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A V14 302 ? 27 'BINDING SITE FOR RESIDUE V14 A 302' 
# 
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  V14 C .   ? V14 A 302 . ? 1_555 ? 
5  AC2 27 TRP A 5   ? TRP A 5   . ? 1_555 ? 
6  AC2 27 ASN A 62  ? ASN A 62  . ? 1_555 ? 
7  AC2 27 HIS A 64  ? HIS A 64  . ? 1_555 ? 
8  AC2 27 ALA A 65  ? ALA A 65  . ? 1_555 ? 
9  AC2 27 ASN A 67  ? ASN A 67  . ? 1_555 ? 
10 AC2 27 ILE A 91  ? ILE A 91  . ? 1_555 ? 
11 AC2 27 GLN A 92  ? GLN A 92  . ? 1_555 ? 
12 AC2 27 HIS A 94  ? HIS A 94  . ? 1_555 ? 
13 AC2 27 HIS A 96  ? HIS A 96  . ? 1_555 ? 
14 AC2 27 HIS A 119 ? HIS A 119 . ? 1_555 ? 
15 AC2 27 VAL A 121 ? VAL A 121 . ? 1_555 ? 
16 AC2 27 PHE A 130 ? PHE A 131 . ? 1_555 ? 
17 AC2 27 VAL A 134 ? VAL A 135 . ? 1_555 ? 
18 AC2 27 LEU A 140 ? LEU A 141 . ? 1_555 ? 
19 AC2 27 VAL A 142 ? VAL A 143 . ? 1_555 ? 
20 AC2 27 LEU A 197 ? LEU A 198 . ? 1_555 ? 
21 AC2 27 THR A 198 ? THR A 199 . ? 1_555 ? 
22 AC2 27 THR A 199 ? THR A 200 . ? 1_555 ? 
23 AC2 27 PRO A 200 ? PRO A 201 . ? 1_555 ? 
24 AC2 27 PRO A 201 ? PRO A 202 . ? 1_555 ? 
25 AC2 27 TRP A 208 ? TRP A 209 . ? 1_555 ? 
26 AC2 27 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
27 AC2 27 HOH D .   ? HOH A 466 . ? 1_555 ? 
28 AC2 27 HOH D .   ? HOH A 571 . ? 1_555 ? 
29 AC2 27 HOH D .   ? HOH A 572 . ? 1_555 ? 
30 AC2 27 HOH D .   ? HOH A 573 . ? 1_555 ? 
31 AC2 27 HOH D .   ? HOH A 693 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4PYY 
_atom_sites.fract_transf_matrix[1][1]   0.023674 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006089 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024085 
_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]   0.014354 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 30.193  2.924   8.037   1.00 31.93 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 31.086  1.798   8.471   1.00 34.24 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.336  0.791   9.335   1.00 26.08 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.568  -0.415  9.201   1.00 25.20 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 32.335  2.326   9.204   1.00 45.76 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 33.416  1.288   9.399   1.00 53.33 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 33.684  0.741   10.599  1.00 59.94 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 34.308  0.713   8.495   1.00 58.64 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 34.692  -0.142  10.471  1.00 58.16 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 35.072  -0.161  9.183   1.00 60.77 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.460  1.255   10.237  1.00 18.79 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 28.839  0.320   11.186  1.00 15.75 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 27.859  -0.522  10.466  1.00 14.60 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.273  -0.077  9.474   1.00 15.11 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.183  1.030   12.388  1.00 15.08 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 26.992  1.857   12.017  1.00 15.25 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 26.925  3.233   11.737  1.00 15.76 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.639  1.388   11.999  1.00 14.40 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.627  3.601   11.477  1.00 13.97 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.806  2.516   11.593  1.00 14.32 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 25.044  0.134   12.205  1.00 14.76 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.427  2.410   11.517  1.00 14.67 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.659  0.037   12.036  1.00 13.99 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 22.871  1.147   11.738  1.00 14.57 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.574  -1.696  11.003  1.00 12.40 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.585  -2.545  10.396  1.00 13.69 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.222  -3.667  11.327  1.00 13.40 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.160  -3.494  12.551  1.00 13.38 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 25.945  -4.829  10.740  1.00 14.43 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.520  -5.989  11.541  1.00 16.61 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.405  -7.242  11.413  1.00 20.85 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 26.201  -8.249  12.171  1.00 21.48 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 24.036  -6.287  11.269  1.00 15.13 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.150  -5.227  11.834  1.00 11.89 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.715  -5.298  13.181  1.00 11.94 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.689  -4.199  11.036  1.00 12.12 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.879  -4.294  13.698  1.00 10.40 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.861  -3.192  11.541  1.00 12.11 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.484  -3.263  12.907  1.00 10.64 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.621  -2.277  13.302  1.00 10.59 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.395  -7.196  10.511  1.00 22.54 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.345  -8.361  10.382  1.00 23.09 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.339  -8.552  11.502  1.00 21.68 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.426  -7.749  12.458  1.00 26.67 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.202  -9.578  11.355  1.00 26.21 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.254  -9.929  12.353  1.00 26.19 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.216  -8.790  12.552  1.00 26.02 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.708  -8.528  13.687  1.00 23.08 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 32.015  -11.189 11.919  1.00 32.21 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 33.106  -11.684 12.872  1.00 39.50 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 34.088  -12.620 12.157  1.00 43.15 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 35.059  -13.291 13.130  1.00 49.95 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 36.295  -13.796 12.447  1.00 53.64 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 32.430  -8.040  11.486  1.00 22.27 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 33.477  -7.083  11.583  1.00 24.37 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 33.023  -5.733  11.940  1.00 18.40 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 33.848  -4.891  12.284  1.00 18.39 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 34.309  -7.132  10.282  1.00 25.88 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 34.871  -8.519  9.974   1.00 27.00 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 35.830  -9.093  10.724  1.00 28.05 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 34.544  -9.446  8.980   1.00 30.62 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 36.112  -10.321 10.236  1.00 27.16 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 35.327  -10.534 9.171   1.00 32.06 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 31.699  -5.475  11.871  1.00 17.69 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 31.226  -4.098  12.084  1.00 14.85 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 29.893  -4.034  12.881  1.00 13.56 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 29.290  -2.958  12.952  1.00 12.02 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 31.024  -3.342  10.741  1.00 15.13 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 29.958  -3.990  9.892   1.00 18.10 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 29.364  -5.008  10.286  1.00 17.38 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 29.697  -3.414  8.724   1.00 20.75 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 29.600  -5.133  13.571  1.00 12.57 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 28.319  -5.341  14.219  1.00 11.77 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 28.287  -4.735  15.579  1.00 11.65 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 29.160  -3.996  15.985  1.00 12.21 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 27.247  -5.067  16.338  1.00 12.43 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 27.009  -4.459  17.645  1.00 12.40 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 28.170  -4.504  18.638  1.00 12.02 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 28.310  -3.588  19.446  1.00 12.60 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 25.803  -5.273  18.142  1.00 12.18 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 25.000  -5.416  16.900  1.00 12.26 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 26.085  -5.853  15.904  1.00 12.57 ? 13  PRO A CD  1 
ATOM   83   N  N   A GLU A 1 14  ? 28.984  -5.552  18.562  0.50 12.13 ? 14  GLU A N   1 
ATOM   84   N  N   B GLU A 1 14  ? 29.006  -5.547  18.604  0.50 12.95 ? 14  GLU A N   1 
ATOM   85   C  CA  A GLU A 1 14  ? 30.112  -5.693  19.463  0.50 12.74 ? 14  GLU A CA  1 
ATOM   86   C  CA  B GLU A 1 14  ? 30.137  -5.614  19.551  0.50 14.08 ? 14  GLU A CA  1 
ATOM   87   C  C   A GLU A 1 14  ? 31.189  -4.629  19.203  0.50 12.06 ? 14  GLU A C   1 
ATOM   88   C  C   B GLU A 1 14  ? 31.232  -4.599  19.210  0.50 12.92 ? 14  GLU A C   1 
ATOM   89   O  O   A GLU A 1 14  ? 32.034  -4.363  20.076  0.50 13.48 ? 14  GLU A O   1 
ATOM   90   O  O   B GLU A 1 14  ? 32.142  -4.334  20.022  0.50 14.21 ? 14  GLU A O   1 
ATOM   91   C  CB  A GLU A 1 14  ? 30.668  -7.122  19.319  0.50 13.75 ? 14  GLU A CB  1 
ATOM   92   C  CB  B GLU A 1 14  ? 30.692  -7.056  19.628  0.50 17.17 ? 14  GLU A CB  1 
ATOM   93   C  CG  A GLU A 1 14  ? 31.366  -7.378  18.017  0.50 12.85 ? 14  GLU A CG  1 
ATOM   94   C  CG  B GLU A 1 14  ? 29.624  -8.104  19.983  0.50 17.16 ? 14  GLU A CG  1 
ATOM   95   C  CD  A GLU A 1 14  ? 30.561  -8.044  16.892  0.50 13.86 ? 14  GLU A CD  1 
ATOM   96   C  CD  B GLU A 1 14  ? 28.911  -7.749  21.265  0.50 20.47 ? 14  GLU A CD  1 
ATOM   97   O  OE1 A GLU A 1 14  ? 29.361  -7.626  16.593  0.50 10.94 ? 14  GLU A OE1 1 
ATOM   98   O  OE1 B GLU A 1 14  ? 29.652  -7.329  22.187  0.50 22.52 ? 14  GLU A OE1 1 
ATOM   99   O  OE2 A GLU A 1 14  ? 31.254  -8.935  16.247  0.50 10.35 ? 14  GLU A OE2 1 
ATOM   100  O  OE2 B GLU A 1 14  ? 27.637  -7.848  21.342  0.50 20.09 ? 14  GLU A OE2 1 
ATOM   101  N  N   . HIS A 1 15  ? 31.159  -4.009  18.024  1.00 12.69 ? 15  HIS A N   1 
ATOM   102  C  CA  . HIS A 1 15  ? 32.123  -3.037  17.599  1.00 11.37 ? 15  HIS A CA  1 
ATOM   103  C  C   . HIS A 1 15  ? 31.682  -1.598  17.763  1.00 12.34 ? 15  HIS A C   1 
ATOM   104  O  O   . HIS A 1 15  ? 32.506  -0.659  17.670  1.00 10.74 ? 15  HIS A O   1 
ATOM   105  C  CB  . HIS A 1 15  ? 32.479  -3.218  16.112  1.00 12.41 ? 15  HIS A CB  1 
ATOM   106  C  CG  . HIS A 1 15  ? 33.241  -4.504  15.819  1.00 15.24 ? 15  HIS A CG  1 
ATOM   107  N  ND1 . HIS A 1 15  ? 34.616  -4.581  15.901  1.00 15.34 ? 15  HIS A ND1 1 
ATOM   108  C  CD2 . HIS A 1 15  ? 32.796  -5.755  15.444  1.00 15.04 ? 15  HIS A CD2 1 
ATOM   109  C  CE1 . HIS A 1 15  ? 34.993  -5.829  15.584  1.00 16.39 ? 15  HIS A CE1 1 
ATOM   110  N  NE2 . HIS A 1 15  ? 33.882  -6.564  15.347  1.00 16.49 ? 15  HIS A NE2 1 
ATOM   111  N  N   . TRP A 1 16  ? 30.371  -1.383  17.896  1.00 10.05 ? 16  TRP A N   1 
ATOM   112  C  CA  . TRP A 1 16  ? 29.870  -0.006  17.902  1.00 10.40 ? 16  TRP A CA  1 
ATOM   113  C  C   . TRP A 1 16  ? 30.437  0.934   18.910  1.00 9.07  ? 16  TRP A C   1 
ATOM   114  O  O   . TRP A 1 16  ? 30.497  2.164   18.661  1.00 9.94  ? 16  TRP A O   1 
ATOM   115  C  CB  . TRP A 1 16  ? 28.317  0.016   17.989  1.00 8.86  ? 16  TRP A CB  1 
ATOM   116  C  CG  . TRP A 1 16  ? 27.608  -0.671  16.861  1.00 10.08 ? 16  TRP A CG  1 
ATOM   117  C  CD1 . TRP A 1 16  ? 28.136  -1.111  15.652  1.00 10.10 ? 16  TRP A CD1 1 
ATOM   118  C  CD2 . TRP A 1 16  ? 26.196  -1.029  16.816  1.00 8.95  ? 16  TRP A CD2 1 
ATOM   119  N  NE1 . TRP A 1 16  ? 27.165  -1.703  14.885  1.00 9.52  ? 16  TRP A NE1 1 
ATOM   120  C  CE2 . TRP A 1 16  ? 25.978  -1.685  15.527  1.00 10.12 ? 16  TRP A CE2 1 
ATOM   121  C  CE3 . TRP A 1 16  ? 25.131  -0.876  17.684  1.00 8.96  ? 16  TRP A CE3 1 
ATOM   122  C  CZ2 . TRP A 1 16  ? 24.737  -2.158  15.150  1.00 11.10 ? 16  TRP A CZ2 1 
ATOM   123  C  CZ3 . TRP A 1 16  ? 23.887  -1.357  17.293  1.00 8.87  ? 16  TRP A CZ3 1 
ATOM   124  C  CH2 . TRP A 1 16  ? 23.696  -1.982  16.057  1.00 9.96  ? 16  TRP A CH2 1 
ATOM   125  N  N   . HIS A 1 17  ? 30.866  0.410   20.052  1.00 11.16 ? 17  HIS A N   1 
ATOM   126  C  CA  . HIS A 1 17  ? 31.290  1.311   21.109  1.00 11.48 ? 17  HIS A CA  1 
ATOM   127  C  C   . HIS A 1 17  ? 32.535  2.110   20.722  1.00 12.15 ? 17  HIS A C   1 
ATOM   128  O  O   . HIS A 1 17  ? 32.764  3.136   21.315  1.00 10.75 ? 17  HIS A O   1 
ATOM   129  C  CB  . HIS A 1 17  ? 31.531  0.550   22.404  1.00 11.69 ? 17  HIS A CB  1 
ATOM   130  C  CG  . HIS A 1 17  ? 32.720  -0.360  22.310  1.00 12.19 ? 17  HIS A CG  1 
ATOM   131  N  ND1 . HIS A 1 17  ? 33.927  -0.034  22.833  1.00 12.80 ? 17  HIS A ND1 1 
ATOM   132  C  CD2 . HIS A 1 17  ? 32.883  -1.535  21.640  1.00 12.89 ? 17  HIS A CD2 1 
ATOM   133  C  CE1 . HIS A 1 17  ? 34.823  -1.006  22.549  1.00 12.29 ? 17  HIS A CE1 1 
ATOM   134  N  NE2 . HIS A 1 17  ? 34.208  -1.934  21.844  1.00 13.56 ? 17  HIS A NE2 1 
ATOM   135  N  N   . LYS A 1 18  ? 33.290  1.644   19.727  1.00 12.67 ? 18  LYS A N   1 
ATOM   136  C  CA  . LYS A 1 18  ? 34.589  2.343   19.413  1.00 13.16 ? 18  LYS A CA  1 
ATOM   137  C  C   . LYS A 1 18  ? 34.291  3.656   18.716  1.00 14.70 ? 18  LYS A C   1 
ATOM   138  O  O   . LYS A 1 18  ? 34.897  4.655   19.003  1.00 15.82 ? 18  LYS A O   1 
ATOM   139  C  CB  . LYS A 1 18  ? 35.449  1.462   18.522  1.00 12.03 ? 18  LYS A CB  1 
ATOM   140  C  CG  . LYS A 1 18  ? 36.017  0.205   19.225  1.00 12.92 ? 18  LYS A CG  1 
ATOM   141  C  CD  . LYS A 1 18  ? 36.737  -0.719  18.238  1.00 12.37 ? 18  LYS A CD  1 
ATOM   142  C  CE  . LYS A 1 18  ? 35.825  -1.789  17.642  1.00 11.80 ? 18  LYS A CE  1 
ATOM   143  N  NZ  . LYS A 1 18  ? 36.541  -2.519  16.536  1.00 11.19 ? 18  LYS A NZ  1 
ATOM   144  N  N   . ASP A 1 19  ? 33.302  3.657   17.824  1.00 13.97 ? 19  ASP A N   1 
ATOM   145  C  CA  . ASP A 1 19  ? 32.823  4.945   17.320  1.00 14.91 ? 19  ASP A CA  1 
ATOM   146  C  C   . ASP A 1 19  ? 31.808  5.684   18.160  1.00 15.49 ? 19  ASP A C   1 
ATOM   147  O  O   . ASP A 1 19  ? 31.698  6.931   18.030  1.00 15.04 ? 19  ASP A O   1 
ATOM   148  C  CB  . ASP A 1 19  ? 32.319  4.821   15.883  1.00 17.84 ? 19  ASP A CB  1 
ATOM   149  C  CG  . ASP A 1 19  ? 33.450  4.603   14.913  1.00 24.68 ? 19  ASP A CG  1 
ATOM   150  O  OD1 . ASP A 1 19  ? 34.446  5.337   15.003  1.00 24.45 ? 19  ASP A OD1 1 
ATOM   151  O  OD2 . ASP A 1 19  ? 33.384  3.618   14.167  1.00 36.97 ? 19  ASP A OD2 1 
ATOM   152  N  N   . PHE A 1 20  ? 31.043  4.948   18.979  1.00 12.79 ? 20  PHE A N   1 
ATOM   153  C  CA  . PHE A 1 20  ? 29.887  5.492   19.712  1.00 12.80 ? 20  PHE A CA  1 
ATOM   154  C  C   . PHE A 1 20  ? 30.000  5.012   21.131  1.00 12.36 ? 20  PHE A C   1 
ATOM   155  O  O   . PHE A 1 20  ? 29.357  4.045   21.488  1.00 11.85 ? 20  PHE A O   1 
ATOM   156  C  CB  . PHE A 1 20  ? 28.564  5.033   19.045  1.00 12.22 ? 20  PHE A CB  1 
ATOM   157  C  CG  . PHE A 1 20  ? 28.457  5.487   17.640  1.00 12.59 ? 20  PHE A CG  1 
ATOM   158  C  CD1 . PHE A 1 20  ? 28.053  6.784   17.359  1.00 14.13 ? 20  PHE A CD1 1 
ATOM   159  C  CD2 . PHE A 1 20  ? 28.823  4.623   16.587  1.00 14.12 ? 20  PHE A CD2 1 
ATOM   160  C  CE1 . PHE A 1 20  ? 27.973  7.187   16.054  1.00 15.17 ? 20  PHE A CE1 1 
ATOM   161  C  CE2 . PHE A 1 20  ? 28.777  5.053   15.268  1.00 14.90 ? 20  PHE A CE2 1 
ATOM   162  C  CZ  . PHE A 1 20  ? 28.361  6.329   15.023  1.00 14.03 ? 20  PHE A CZ  1 
ATOM   163  N  N   A PRO A 1 21  ? 30.821  5.687   21.967  0.50 11.60 ? 21  PRO A N   1 
ATOM   164  N  N   B PRO A 1 21  ? 30.828  5.689   21.978  0.50 12.09 ? 21  PRO A N   1 
ATOM   165  C  CA  A PRO A 1 21  ? 31.080  5.219   23.326  0.50 11.24 ? 21  PRO A CA  1 
ATOM   166  C  CA  B PRO A 1 21  ? 31.076  5.152   23.322  0.50 11.76 ? 21  PRO A CA  1 
ATOM   167  C  C   A PRO A 1 21  ? 29.829  5.006   24.170  0.50 11.44 ? 21  PRO A C   1 
ATOM   168  C  C   B PRO A 1 21  ? 29.825  4.991   24.192  0.50 11.68 ? 21  PRO A C   1 
ATOM   169  O  O   A PRO A 1 21  ? 29.848  4.246   25.120  0.50 11.45 ? 21  PRO A O   1 
ATOM   170  O  O   B PRO A 1 21  ? 29.843  4.263   25.167  0.50 11.71 ? 21  PRO A O   1 
ATOM   171  C  CB  A PRO A 1 21  ? 31.923  6.361   23.948  0.50 12.27 ? 21  PRO A CB  1 
ATOM   172  C  CB  B PRO A 1 21  ? 32.037  6.188   23.957  0.50 13.36 ? 21  PRO A CB  1 
ATOM   173  C  CG  A PRO A 1 21  ? 31.929  7.449   22.933  0.50 10.82 ? 21  PRO A CG  1 
ATOM   174  C  CG  B PRO A 1 21  ? 32.713  6.824   22.799  0.50 12.44 ? 21  PRO A CG  1 
ATOM   175  C  CD  A PRO A 1 21  ? 31.693  6.810   21.606  0.50 11.72 ? 21  PRO A CD  1 
ATOM   176  C  CD  B PRO A 1 21  ? 31.724  6.817   21.659  0.50 12.57 ? 21  PRO A CD  1 
ATOM   177  N  N   A ILE A 1 22  ? 28.745  5.700   23.813  0.50 10.53 ? 22  ILE A N   1 
ATOM   178  N  N   B ILE A 1 22  ? 28.743  5.684   23.820  0.50 10.48 ? 22  ILE A N   1 
ATOM   179  C  CA  A ILE A 1 22  ? 27.517  5.667   24.579  0.50 10.00 ? 22  ILE A CA  1 
ATOM   180  C  CA  B ILE A 1 22  ? 27.491  5.675   24.562  0.50 9.74  ? 22  ILE A CA  1 
ATOM   181  C  C   A ILE A 1 22  ? 26.912  4.274   24.506  0.50 9.61  ? 22  ILE A C   1 
ATOM   182  C  C   B ILE A 1 22  ? 26.812  4.323   24.384  0.50 9.33  ? 22  ILE A C   1 
ATOM   183  O  O   A ILE A 1 22  ? 26.096  3.932   25.378  0.50 9.27  ? 22  ILE A O   1 
ATOM   184  O  O   B ILE A 1 22  ? 25.812  4.070   25.024  0.50 8.97  ? 22  ILE A O   1 
ATOM   185  C  CB  A ILE A 1 22  ? 26.518  6.733   24.089  0.50 10.12 ? 22  ILE A CB  1 
ATOM   186  C  CB  B ILE A 1 22  ? 26.556  6.796   24.069  0.50 9.65  ? 22  ILE A CB  1 
ATOM   187  C  CG1 A ILE A 1 22  ? 25.483  7.055   25.167  0.50 10.64 ? 22  ILE A CG1 1 
ATOM   188  C  CG1 B ILE A 1 22  ? 25.437  7.113   25.062  0.50 9.79  ? 22  ILE A CG1 1 
ATOM   189  C  CG2 A ILE A 1 22  ? 25.908  6.288   22.757  0.50 10.35 ? 22  ILE A CG2 1 
ATOM   190  C  CG2 B ILE A 1 22  ? 25.987  6.412   22.701  0.50 9.98  ? 22  ILE A CG2 1 
ATOM   191  C  CD1 A ILE A 1 22  ? 24.512  8.165   24.822  0.50 10.61 ? 22  ILE A CD1 1 
ATOM   192  C  CD1 B ILE A 1 22  ? 25.880  7.636   26.419  0.50 9.34  ? 22  ILE A CD1 1 
ATOM   193  N  N   . ALA A 1 23  ? 27.396  3.461   23.544  1.00 8.95  ? 23  ALA A N   1 
ATOM   194  C  CA  . ALA A 1 23  ? 27.005  2.063   23.434  1.00 9.37  ? 23  ALA A CA  1 
ATOM   195  C  C   . ALA A 1 23  ? 27.048  1.364   24.754  1.00 10.36 ? 23  ALA A C   1 
ATOM   196  O  O   . ALA A 1 23  ? 26.310  0.400   24.961  1.00 9.45  ? 23  ALA A O   1 
ATOM   197  C  CB  . ALA A 1 23  ? 27.851  1.309   22.436  1.00 9.76  ? 23  ALA A CB  1 
ATOM   198  N  N   . LYS A 1 24  ? 27.952  1.799   25.637  1.00 10.87 ? 24  LYS A N   1 
ATOM   199  C  CA  . LYS A 1 24  ? 28.081  1.139   26.977  1.00 12.72 ? 24  LYS A CA  1 
ATOM   200  C  C   . LYS A 1 24  ? 27.505  2.065   28.056  1.00 12.83 ? 24  LYS A C   1 
ATOM   201  O  O   . LYS A 1 24  ? 27.983  2.048   29.236  1.00 12.35 ? 24  LYS A O   1 
ATOM   202  C  CB  . LYS A 1 24  ? 29.562  0.924   27.235  1.00 14.34 ? 24  LYS A CB  1 
ATOM   203  C  CG  . LYS A 1 24  ? 30.205  -0.082  26.283  1.00 17.03 ? 24  LYS A CG  1 
ATOM   204  C  CD  . LYS A 1 24  ? 31.691  -0.206  26.605  1.00 18.96 ? 24  LYS A CD  1 
ATOM   205  C  CE  . LYS A 1 24  ? 32.381  -1.177  25.671  1.00 20.44 ? 24  LYS A CE  1 
ATOM   206  N  NZ  . LYS A 1 24  ? 32.130  -2.584  26.010  1.00 23.16 ? 24  LYS A NZ  1 
ATOM   207  N  N   . GLY A 1 25  ? 26.517  2.896   27.687  1.00 10.61 ? 25  GLY A N   1 
ATOM   208  C  CA  . GLY A 1 25  ? 26.038  3.890   28.648  1.00 10.57 ? 25  GLY A CA  1 
ATOM   209  C  C   . GLY A 1 25  ? 24.979  3.337   29.594  1.00 10.53 ? 25  GLY A C   1 
ATOM   210  O  O   . GLY A 1 25  ? 24.755  2.134   29.676  1.00 11.02 ? 25  GLY A O   1 
ATOM   211  N  N   . GLU A 1 26  ? 24.254  4.243   30.254  1.00 11.48 ? 26  GLU A N   1 
ATOM   212  C  CA  . GLU A 1 26  ? 23.427  3.825   31.383  1.00 11.90 ? 26  GLU A CA  1 
ATOM   213  C  C   . GLU A 1 26  ? 22.011  3.528   31.021  1.00 11.05 ? 26  GLU A C   1 
ATOM   214  O  O   . GLU A 1 26  ? 21.262  3.012   31.838  1.00 11.54 ? 26  GLU A O   1 
ATOM   215  C  CB  . GLU A 1 26  ? 23.407  4.918   32.452  1.00 16.62 ? 26  GLU A CB  1 
ATOM   216  C  CG  . GLU A 1 26  ? 24.791  5.109   33.054  1.00 18.55 ? 26  GLU A CG  1 
ATOM   217  C  CD  . GLU A 1 26  ? 25.338  3.858   33.711  1.00 22.47 ? 26  GLU A CD  1 
ATOM   218  O  OE1 . GLU A 1 26  ? 24.682  3.172   34.555  1.00 27.78 ? 26  GLU A OE1 1 
ATOM   219  O  OE2 . GLU A 1 26  ? 26.476  3.548   33.388  1.00 27.35 ? 26  GLU A OE2 1 
ATOM   220  N  N   . ARG A 1 27  ? 21.615  3.834   29.811  1.00 8.43  ? 27  ARG A N   1 
ATOM   221  C  CA  . ARG A 1 27  ? 20.185  3.635   29.441  1.00 8.26  ? 27  ARG A CA  1 
ATOM   222  C  C   . ARG A 1 27  ? 20.098  3.156   27.961  1.00 7.79  ? 27  ARG A C   1 
ATOM   223  O  O   . ARG A 1 27  ? 19.353  3.708   27.096  1.00 7.31  ? 27  ARG A O   1 
ATOM   224  C  CB  . ARG A 1 27  ? 19.284  4.895   29.729  1.00 8.91  ? 27  ARG A CB  1 
ATOM   225  C  CG  . ARG A 1 27  ? 19.732  6.156   29.058  1.00 10.31 ? 27  ARG A CG  1 
ATOM   226  C  CD  . ARG A 1 27  ? 18.763  7.360   29.222  1.00 12.50 ? 27  ARG A CD  1 
ATOM   227  N  NE  . ARG A 1 27  ? 17.571  7.274   28.340  1.00 11.65 ? 27  ARG A NE  1 
ATOM   228  C  CZ  . ARG A 1 27  ? 16.618  8.174   28.314  1.00 12.48 ? 27  ARG A CZ  1 
ATOM   229  N  NH1 . ARG A 1 27  ? 16.695  9.257   29.133  1.00 12.91 ? 27  ARG A NH1 1 
ATOM   230  N  NH2 . ARG A 1 27  ? 15.619  8.012   27.482  1.00 13.26 ? 27  ARG A NH2 1 
ATOM   231  N  N   . GLN A 1 28  ? 20.845  2.082   27.696  1.00 7.87  ? 28  GLN A N   1 
ATOM   232  C  CA  . GLN A 1 28  ? 20.872  1.520   26.290  1.00 7.22  ? 28  GLN A CA  1 
ATOM   233  C  C   . GLN A 1 28  ? 19.731  0.545   26.044  1.00 7.10  ? 28  GLN A C   1 
ATOM   234  O  O   . GLN A 1 28  ? 19.210  -0.118  26.924  1.00 7.81  ? 28  GLN A O   1 
ATOM   235  C  CB  . GLN A 1 28  ? 22.233  0.825   26.016  1.00 7.85  ? 28  GLN A CB  1 
ATOM   236  C  CG  . GLN A 1 28  ? 23.343  1.903   25.928  1.00 7.61  ? 28  GLN A CG  1 
ATOM   237  C  CD  . GLN A 1 28  ? 23.239  2.714   24.610  1.00 7.16  ? 28  GLN A CD  1 
ATOM   238  O  OE1 . GLN A 1 28  ? 23.443  2.177   23.518  1.00 7.89  ? 28  GLN A OE1 1 
ATOM   239  N  NE2 . GLN A 1 28  ? 22.922  4.019   24.711  1.00 7.40  ? 28  GLN A NE2 1 
ATOM   240  N  N   . SER A 1 29  ? 19.335  0.502   24.773  1.00 6.78  ? 29  SER A N   1 
ATOM   241  C  CA  . SER A 1 29  ? 18.265  -0.360  24.247  1.00 5.96  ? 29  SER A CA  1 
ATOM   242  C  C   . SER A 1 29  ? 18.824  -1.222  23.130  1.00 6.13  ? 29  SER A C   1 
ATOM   243  O  O   . SER A 1 29  ? 19.787  -0.916  22.461  1.00 6.87  ? 29  SER A O   1 
ATOM   244  C  CB  . SER A 1 29  ? 17.161  0.504   23.672  1.00 5.49  ? 29  SER A CB  1 
ATOM   245  O  OG  . SER A 1 29  ? 16.548  1.179   24.774  1.00 5.44  ? 29  SER A OG  1 
ATOM   246  N  N   . PRO A 1 30  ? 18.178  -2.327  22.890  1.00 6.02  ? 30  PRO A N   1 
ATOM   247  C  CA  . PRO A 1 30  ? 17.069  -2.875  23.605  1.00 6.08  ? 30  PRO A CA  1 
ATOM   248  C  C   . PRO A 1 30  ? 17.456  -3.581  24.915  1.00 6.44  ? 30  PRO A C   1 
ATOM   249  O  O   . PRO A 1 30  ? 18.642  -3.612  25.278  1.00 6.59  ? 30  PRO A O   1 
ATOM   250  C  CB  . PRO A 1 30  ? 16.518  -3.904  22.582  1.00 5.73  ? 30  PRO A CB  1 
ATOM   251  C  CG  . PRO A 1 30  ? 17.822  -4.453  21.978  1.00 5.68  ? 30  PRO A CG  1 
ATOM   252  C  CD  . PRO A 1 30  ? 18.686  -3.215  21.829  1.00 5.52  ? 30  PRO A CD  1 
ATOM   253  N  N   . VAL A 1 31  ? 16.435  -4.103  25.616  1.00 6.85  ? 31  VAL A N   1 
ATOM   254  C  CA  . VAL A 1 31  ? 16.602  -4.841  26.879  1.00 6.90  ? 31  VAL A CA  1 
ATOM   255  C  C   . VAL A 1 31  ? 15.718  -6.085  26.843  1.00 7.27  ? 31  VAL A C   1 
ATOM   256  O  O   . VAL A 1 31  ? 14.744  -6.213  26.037  1.00 7.46  ? 31  VAL A O   1 
ATOM   257  C  CB  . VAL A 1 31  ? 16.273  -4.011  28.155  1.00 7.17  ? 31  VAL A CB  1 
ATOM   258  C  CG1 . VAL A 1 31  ? 17.248  -2.818  28.266  1.00 6.70  ? 31  VAL A CG1 1 
ATOM   259  C  CG2 . VAL A 1 31  ? 14.772  -3.541  28.183  1.00 7.08  ? 31  VAL A CG2 1 
ATOM   260  N  N   . ASP A 1 32  ? 16.065  -7.047  27.702  1.00 7.03  ? 32  ASP A N   1 
ATOM   261  C  CA  . ASP A 1 32  ? 15.157  -8.135  27.944  1.00 7.33  ? 32  ASP A CA  1 
ATOM   262  C  C   . ASP A 1 32  ? 14.096  -7.638  28.900  1.00 7.81  ? 32  ASP A C   1 
ATOM   263  O  O   . ASP A 1 32  ? 14.414  -6.966  29.902  1.00 8.01  ? 32  ASP A O   1 
ATOM   264  C  CB  . ASP A 1 32  ? 15.897  -9.323  28.548  1.00 7.85  ? 32  ASP A CB  1 
ATOM   265  C  CG  . ASP A 1 32  ? 14.924  -10.479 28.888  1.00 8.99  ? 32  ASP A CG  1 
ATOM   266  O  OD1 . ASP A 1 32  ? 14.234  -10.991 27.972  1.00 8.19  ? 32  ASP A OD1 1 
ATOM   267  O  OD2 . ASP A 1 32  ? 14.942  -10.923 30.094  1.00 9.17  ? 32  ASP A OD2 1 
ATOM   268  N  N   . ILE A 1 33  ? 12.843  -7.983  28.628  1.00 8.25  ? 33  ILE A N   1 
ATOM   269  C  CA  . ILE A 1 33  ? 11.713  -7.593  29.474  1.00 8.33  ? 33  ILE A CA  1 
ATOM   270  C  C   . ILE A 1 33  ? 11.409  -8.834  30.316  1.00 8.81  ? 33  ILE A C   1 
ATOM   271  O  O   . ILE A 1 33  ? 10.856  -9.843  29.845  1.00 9.56  ? 33  ILE A O   1 
ATOM   272  C  CB  . ILE A 1 33  ? 10.498  -7.220  28.668  1.00 7.76  ? 33  ILE A CB  1 
ATOM   273  C  CG1 . ILE A 1 33  ? 10.822  -5.922  27.890  1.00 8.14  ? 33  ILE A CG1 1 
ATOM   274  C  CG2 . ILE A 1 33  ? 9.334   -6.956  29.667  1.00 8.13  ? 33  ILE A CG2 1 
ATOM   275  C  CD1 . ILE A 1 33  ? 9.828   -5.582  26.700  1.00 7.17  ? 33  ILE A CD1 1 
ATOM   276  N  N   . ASP A 1 34  ? 11.826  -8.756  31.574  1.00 10.17 ? 34  ASP A N   1 
ATOM   277  C  CA  . ASP A 1 34  ? 11.501  -9.868  32.532  1.00 11.37 ? 34  ASP A CA  1 
ATOM   278  C  C   . ASP A 1 34  ? 10.105  -9.632  33.105  1.00 12.88 ? 34  ASP A C   1 
ATOM   279  O  O   . ASP A 1 34  ? 9.907   -8.669  33.867  1.00 13.36 ? 34  ASP A O   1 
ATOM   280  C  CB  . ASP A 1 34  ? 12.566  -9.901  33.626  1.00 13.80 ? 34  ASP A CB  1 
ATOM   281  C  CG  . ASP A 1 34  ? 12.434  -11.151 34.489  1.00 18.86 ? 34  ASP A CG  1 
ATOM   282  O  OD1 . ASP A 1 34  ? 11.810  -11.010 35.508  1.00 21.11 ? 34  ASP A OD1 1 
ATOM   283  O  OD2 . ASP A 1 34  ? 12.921  -12.234 34.083  1.00 21.79 ? 34  ASP A OD2 1 
ATOM   284  N  N   . THR A 1 35  ? 9.150   -10.458 32.707  1.00 12.58 ? 35  THR A N   1 
ATOM   285  C  CA  . THR A 1 35  ? 7.722   -10.174 32.895  1.00 13.12 ? 35  THR A CA  1 
ATOM   286  C  C   . THR A 1 35  ? 7.380   -10.334 34.355  1.00 15.08 ? 35  THR A C   1 
ATOM   287  O  O   . THR A 1 35  ? 6.427   -9.729  34.837  1.00 14.86 ? 35  THR A O   1 
ATOM   288  C  CB  . THR A 1 35  ? 6.815   -11.091 32.096  1.00 15.10 ? 35  THR A CB  1 
ATOM   289  O  OG1 . THR A 1 35  ? 7.001   -12.471 32.475  1.00 14.62 ? 35  THR A OG1 1 
ATOM   290  C  CG2 . THR A 1 35  ? 7.069   -10.907 30.588  1.00 11.67 ? 35  THR A CG2 1 
ATOM   291  N  N   . HIS A 1 36  ? 8.214   -11.099 35.107  1.00 15.59 ? 36  HIS A N   1 
ATOM   292  C  CA  . HIS A 1 36  ? 7.988   -11.218 36.536  1.00 16.37 ? 36  HIS A CA  1 
ATOM   293  C  C   . HIS A 1 36  ? 8.686   -10.137 37.401  1.00 19.71 ? 36  HIS A C   1 
ATOM   294  O  O   . HIS A 1 36  ? 8.564   -10.107 38.646  1.00 26.89 ? 36  HIS A O   1 
ATOM   295  C  CB  . HIS A 1 36  ? 8.368   -12.668 36.943  1.00 16.92 ? 36  HIS A CB  1 
ATOM   296  C  CG  . HIS A 1 36  ? 7.484   -13.739 36.321  1.00 18.99 ? 36  HIS A CG  1 
ATOM   297  N  ND1 . HIS A 1 36  ? 7.932   -14.617 35.385  1.00 19.96 ? 36  HIS A ND1 1 
ATOM   298  C  CD2 . HIS A 1 36  ? 6.153   -14.063 36.537  1.00 21.00 ? 36  HIS A CD2 1 
ATOM   299  C  CE1 . HIS A 1 36  ? 6.967   -15.431 35.044  1.00 19.70 ? 36  HIS A CE1 1 
ATOM   300  N  NE2 . HIS A 1 36  ? 5.870   -15.093 35.719  1.00 23.31 ? 36  HIS A NE2 1 
ATOM   301  N  N   . THR A 1 37  ? 9.438   -9.223  36.813  1.00 17.42 ? 37  THR A N   1 
ATOM   302  C  CA  . THR A 1 37  ? 10.119  -8.188  37.580  1.00 17.34 ? 37  THR A CA  1 
ATOM   303  C  C   . THR A 1 37  ? 9.418   -6.857  37.189  1.00 16.86 ? 37  THR A C   1 
ATOM   304  O  O   . THR A 1 37  ? 9.493   -5.892  37.926  1.00 17.23 ? 37  THR A O   1 
ATOM   305  C  CB  . THR A 1 37  ? 11.620  -8.124  37.217  1.00 19.93 ? 37  THR A CB  1 
ATOM   306  O  OG1 . THR A 1 37  ? 12.194  -9.386  37.523  1.00 23.58 ? 37  THR A OG1 1 
ATOM   307  C  CG2 . THR A 1 37  ? 12.400  -7.046  37.985  1.00 22.05 ? 37  THR A CG2 1 
ATOM   308  N  N   . ALA A 1 38  ? 8.781   -6.817  36.029  1.00 15.59 ? 38  ALA A N   1 
ATOM   309  C  CA  . ALA A 1 38  ? 8.125   -5.526  35.579  1.00 15.07 ? 38  ALA A CA  1 
ATOM   310  C  C   . ALA A 1 38  ? 6.986   -5.257  36.544  1.00 16.83 ? 38  ALA A C   1 
ATOM   311  O  O   . ALA A 1 38  ? 6.299   -6.157  36.926  1.00 20.60 ? 38  ALA A O   1 
ATOM   312  C  CB  . ALA A 1 38  ? 7.635   -5.661  34.170  1.00 15.73 ? 38  ALA A CB  1 
ATOM   313  N  N   . LYS A 1 39  ? 6.810   -4.044  36.996  1.00 16.64 ? 39  LYS A N   1 
ATOM   314  C  CA  . LYS A 1 39  ? 5.686   -3.827  37.904  1.00 16.49 ? 39  LYS A CA  1 
ATOM   315  C  C   . LYS A 1 39  ? 4.554   -3.018  37.275  1.00 14.90 ? 39  LYS A C   1 
ATOM   316  O  O   . LYS A 1 39  ? 4.758   -1.970  36.579  1.00 12.55 ? 39  LYS A O   1 
ATOM   317  C  CB  . LYS A 1 39  ? 6.177   -3.090  39.109  1.00 18.36 ? 39  LYS A CB  1 
ATOM   318  C  CG  . LYS A 1 39  ? 5.202   -3.188  40.302  1.00 22.91 ? 39  LYS A CG  1 
ATOM   319  C  CD  . LYS A 1 39  ? 5.730   -2.143  41.278  1.00 25.82 ? 39  LYS A CD  1 
ATOM   320  C  CE  . LYS A 1 39  ? 4.682   -1.527  42.190  1.00 28.00 ? 39  LYS A CE  1 
ATOM   321  N  NZ  . LYS A 1 39  ? 4.384   -2.464  43.302  1.00 30.75 ? 39  LYS A NZ  1 
ATOM   322  N  N   . TYR A 1 40  ? 3.344   -3.471  37.583  1.00 15.64 ? 40  TYR A N   1 
ATOM   323  C  CA  . TYR A 1 40  ? 2.150   -2.777  37.099  1.00 16.83 ? 40  TYR A CA  1 
ATOM   324  C  C   . TYR A 1 40  ? 2.171   -1.377  37.701  1.00 16.63 ? 40  TYR A C   1 
ATOM   325  O  O   . TYR A 1 40  ? 2.392   -1.211  38.927  1.00 16.89 ? 40  TYR A O   1 
ATOM   326  C  CB  . TYR A 1 40  ? 0.873   -3.569  37.488  1.00 19.21 ? 40  TYR A CB  1 
ATOM   327  C  CG  . TYR A 1 40  ? -0.370  -2.748  37.402  1.00 23.21 ? 40  TYR A CG  1 
ATOM   328  C  CD1 . TYR A 1 40  ? -0.807  -2.258  36.177  1.00 23.73 ? 40  TYR A CD1 1 
ATOM   329  C  CD2 . TYR A 1 40  ? -1.109  -2.408  38.553  1.00 29.17 ? 40  TYR A CD2 1 
ATOM   330  C  CE1 . TYR A 1 40  ? -1.924  -1.468  36.068  1.00 27.39 ? 40  TYR A CE1 1 
ATOM   331  C  CE2 . TYR A 1 40  ? -2.250  -1.613  38.452  1.00 31.07 ? 40  TYR A CE2 1 
ATOM   332  C  CZ  . TYR A 1 40  ? -2.657  -1.154  37.195  1.00 31.20 ? 40  TYR A CZ  1 
ATOM   333  O  OH  . TYR A 1 40  ? -3.760  -0.347  36.989  1.00 35.37 ? 40  TYR A OH  1 
ATOM   334  N  N   . ASP A 1 41  ? 1.924   -0.338  36.898  1.00 16.66 ? 41  ASP A N   1 
ATOM   335  C  CA  . ASP A 1 41  ? 1.998   1.029   37.424  1.00 17.63 ? 41  ASP A CA  1 
ATOM   336  C  C   . ASP A 1 41  ? 0.578   1.651   37.239  1.00 22.52 ? 41  ASP A C   1 
ATOM   337  O  O   . ASP A 1 41  ? 0.155   1.954   36.107  1.00 20.54 ? 41  ASP A O   1 
ATOM   338  C  CB  . ASP A 1 41  ? 3.073   1.833   36.654  1.00 20.18 ? 41  ASP A CB  1 
ATOM   339  C  CG  . ASP A 1 41  ? 3.273   3.249   37.193  1.00 22.70 ? 41  ASP A CG  1 
ATOM   340  O  OD1 . ASP A 1 41  ? 2.441   3.685   37.998  1.00 24.50 ? 41  ASP A OD1 1 
ATOM   341  O  OD2 . ASP A 1 41  ? 4.244   3.912   36.765  1.00 22.43 ? 41  ASP A OD2 1 
ATOM   342  N  N   . PRO A 1 42  ? -0.168  1.853   38.346  1.00 27.23 ? 42  PRO A N   1 
ATOM   343  C  CA  . PRO A 1 42  ? -1.559  2.257   38.158  1.00 28.83 ? 42  PRO A CA  1 
ATOM   344  C  C   . PRO A 1 42  ? -1.689  3.720   37.790  1.00 29.34 ? 42  PRO A C   1 
ATOM   345  O  O   . PRO A 1 42  ? -2.781  4.134   37.390  1.00 32.69 ? 42  PRO A O   1 
ATOM   346  C  CB  . PRO A 1 42  ? -2.188  1.972   39.544  1.00 32.53 ? 42  PRO A CB  1 
ATOM   347  C  CG  . PRO A 1 42  ? -1.070  2.238   40.506  1.00 30.19 ? 42  PRO A CG  1 
ATOM   348  C  CD  . PRO A 1 42  ? 0.149   1.653   39.786  1.00 30.33 ? 42  PRO A CD  1 
ATOM   349  N  N   . SER A 1 43  ? -0.608  4.495   37.943  1.00 27.87 ? 43  SER A N   1 
ATOM   350  C  CA  . SER A 1 43  ? -0.582  5.890   37.522  1.00 31.96 ? 43  SER A CA  1 
ATOM   351  C  C   . SER A 1 43  ? -0.368  6.080   35.990  1.00 31.74 ? 43  SER A C   1 
ATOM   352  O  O   . SER A 1 43  ? -0.494  7.192   35.474  1.00 33.49 ? 43  SER A O   1 
ATOM   353  C  CB  . SER A 1 43  ? 0.500   6.662   38.259  1.00 31.02 ? 43  SER A CB  1 
ATOM   354  O  OG  . SER A 1 43  ? 1.779   6.194   37.898  1.00 35.94 ? 43  SER A OG  1 
ATOM   355  N  N   . LEU A 1 44  ? -0.004  5.026   35.264  1.00 28.54 ? 44  LEU A N   1 
ATOM   356  C  CA  . LEU A 1 44  ? 0.137   5.190   33.806  1.00 27.05 ? 44  LEU A CA  1 
ATOM   357  C  C   . LEU A 1 44  ? -1.235  5.542   33.218  1.00 30.28 ? 44  LEU A C   1 
ATOM   358  O  O   . LEU A 1 44  ? -2.214  4.827   33.451  1.00 32.09 ? 44  LEU A O   1 
ATOM   359  C  CB  . LEU A 1 44  ? 0.697   3.932   33.156  1.00 19.75 ? 44  LEU A CB  1 
ATOM   360  C  CG  . LEU A 1 44  ? 2.190   3.689   33.396  1.00 16.48 ? 44  LEU A CG  1 
ATOM   361  C  CD1 . LEU A 1 44  ? 2.549   2.249   32.929  1.00 15.76 ? 44  LEU A CD1 1 
ATOM   362  C  CD2 . LEU A 1 44  ? 3.044   4.686   32.634  1.00 17.26 ? 44  LEU A CD2 1 
ATOM   363  N  N   . LYS A 1 45  ? -1.289  6.648   32.472  1.00 31.27 ? 45  LYS A N   1 
ATOM   364  C  CA  . LYS A 1 45  ? -2.526  7.092   31.803  1.00 30.90 ? 45  LYS A CA  1 
ATOM   365  C  C   . LYS A 1 45  ? -2.818  6.160   30.625  1.00 27.54 ? 45  LYS A C   1 
ATOM   366  O  O   . LYS A 1 45  ? -1.914  5.552   30.067  1.00 25.04 ? 45  LYS A O   1 
ATOM   367  C  CB  . LYS A 1 45  ? -2.320  8.523   31.314  1.00 35.00 ? 45  LYS A CB  1 
ATOM   368  C  CG  . LYS A 1 45  ? -2.731  9.587   32.285  1.00 41.86 ? 45  LYS A CG  1 
ATOM   369  C  CD  . LYS A 1 45  ? -4.128  10.059  31.886  1.00 45.18 ? 45  LYS A CD  1 
ATOM   370  C  CE  . LYS A 1 45  ? -4.900  10.647  33.057  1.00 47.23 ? 45  LYS A CE  1 
ATOM   371  N  NZ  . LYS A 1 45  ? -6.360  10.410  32.878  1.00 45.17 ? 45  LYS A NZ  1 
ATOM   372  N  N   . PRO A 1 46  ? -4.079  6.019   30.188  1.00 30.74 ? 46  PRO A N   1 
ATOM   373  C  CA  . PRO A 1 46  ? -4.154  5.143   28.978  1.00 26.46 ? 46  PRO A CA  1 
ATOM   374  C  C   . PRO A 1 46  ? -3.320  5.653   27.743  1.00 20.93 ? 46  PRO A C   1 
ATOM   375  O  O   . PRO A 1 46  ? -3.122  6.861   27.591  1.00 22.60 ? 46  PRO A O   1 
ATOM   376  C  CB  . PRO A 1 46  ? -5.662  5.122   28.636  1.00 30.28 ? 46  PRO A CB  1 
ATOM   377  C  CG  . PRO A 1 46  ? -6.249  6.246   29.448  1.00 32.50 ? 46  PRO A CG  1 
ATOM   378  C  CD  . PRO A 1 46  ? -5.412  6.419   30.686  1.00 31.94 ? 46  PRO A CD  1 
ATOM   379  N  N   . LEU A 1 47  ? -2.840  4.746   26.906  1.00 18.14 ? 47  LEU A N   1 
ATOM   380  C  CA  . LEU A 1 47  ? -2.097  5.187   25.695  1.00 17.59 ? 47  LEU A CA  1 
ATOM   381  C  C   . LEU A 1 47  ? -3.051  5.637   24.612  1.00 17.61 ? 47  LEU A C   1 
ATOM   382  O  O   . LEU A 1 47  ? -4.128  5.038   24.475  1.00 18.67 ? 47  LEU A O   1 
ATOM   383  C  CB  . LEU A 1 47  ? -1.374  4.029   25.129  1.00 19.47 ? 47  LEU A CB  1 
ATOM   384  C  CG  . LEU A 1 47  ? -0.276  4.134   24.104  1.00 17.45 ? 47  LEU A CG  1 
ATOM   385  C  CD1 . LEU A 1 47  ? 0.884   4.942   24.729  1.00 18.23 ? 47  LEU A CD1 1 
ATOM   386  C  CD2 . LEU A 1 47  ? 0.219   2.731   23.755  1.00 19.25 ? 47  LEU A CD2 1 
ATOM   387  N  N   . SER A 1 48  ? -2.656  6.635   23.833  1.00 13.38 ? 48  SER A N   1 
ATOM   388  C  CA  . SER A 1 48  ? -3.469  7.224   22.780  1.00 14.19 ? 48  SER A CA  1 
ATOM   389  C  C   . SER A 1 48  ? -2.656  7.231   21.492  1.00 13.35 ? 48  SER A C   1 
ATOM   390  O  O   . SER A 1 48  ? -1.716  7.967   21.360  1.00 12.39 ? 48  SER A O   1 
ATOM   391  C  CB  . SER A 1 48  ? -3.802  8.668   23.178  1.00 15.41 ? 48  SER A CB  1 
ATOM   392  O  OG  . SER A 1 48  ? -4.501  9.337   22.142  1.00 13.99 ? 48  SER A OG  1 
ATOM   393  N  N   . VAL A 1 49  ? -3.022  6.358   20.595  1.00 13.35 ? 49  VAL A N   1 
ATOM   394  C  CA  . VAL A 1 49  ? -2.420  6.254   19.278  1.00 14.32 ? 49  VAL A CA  1 
ATOM   395  C  C   . VAL A 1 49  ? -3.449  6.821   18.301  1.00 15.76 ? 49  VAL A C   1 
ATOM   396  O  O   . VAL A 1 49  ? -4.506  6.215   18.051  1.00 18.36 ? 49  VAL A O   1 
ATOM   397  C  CB  . VAL A 1 49  ? -2.105  4.785   18.985  1.00 15.41 ? 49  VAL A CB  1 
ATOM   398  C  CG1 . VAL A 1 49  ? -1.264  4.655   17.708  1.00 17.52 ? 49  VAL A CG1 1 
ATOM   399  C  CG2 . VAL A 1 49  ? -1.406  4.161   20.162  1.00 16.57 ? 49  VAL A CG2 1 
ATOM   400  N  N   . SER A 1 50  ? -3.176  7.987   17.755  1.00 14.34 ? 50  SER A N   1 
ATOM   401  C  CA  . SER A 1 50  ? -4.105  8.649   16.820  1.00 16.82 ? 50  SER A CA  1 
ATOM   402  C  C   . SER A 1 50  ? -3.491  8.704   15.450  1.00 15.14 ? 50  SER A C   1 
ATOM   403  O  O   . SER A 1 50  ? -2.805  9.656   15.121  1.00 15.23 ? 50  SER A O   1 
ATOM   404  C  CB  . SER A 1 50  ? -4.483  10.042  17.288  1.00 20.64 ? 50  SER A CB  1 
ATOM   405  O  OG  . SER A 1 50  ? -4.996  9.988   18.582  1.00 28.30 ? 50  SER A OG  1 
ATOM   406  N  N   . TYR A 1 51  ? -3.735  7.681   14.651  1.00 14.93 ? 51  TYR A N   1 
ATOM   407  C  CA  . TYR A 1 51  ? -3.157  7.580   13.313  1.00 14.96 ? 51  TYR A CA  1 
ATOM   408  C  C   . TYR A 1 51  ? -4.139  7.841   12.143  1.00 17.83 ? 51  TYR A C   1 
ATOM   409  O  O   . TYR A 1 51  ? -3.748  7.668   11.005  1.00 18.00 ? 51  TYR A O   1 
ATOM   410  C  CB  . TYR A 1 51  ? -2.513  6.200   13.101  1.00 13.09 ? 51  TYR A CB  1 
ATOM   411  C  CG  . TYR A 1 51  ? -1.206  5.937   13.882  1.00 12.04 ? 51  TYR A CG  1 
ATOM   412  C  CD1 . TYR A 1 51  ? -0.525  6.982   14.542  1.00 11.27 ? 51  TYR A CD1 1 
ATOM   413  C  CD2 . TYR A 1 51  ? -0.715  4.634   13.972  1.00 10.93 ? 51  TYR A CD2 1 
ATOM   414  C  CE1 . TYR A 1 51  ? 0.681   6.742   15.273  1.00 10.18 ? 51  TYR A CE1 1 
ATOM   415  C  CE2 . TYR A 1 51  ? 0.479   4.362   14.660  1.00 10.51 ? 51  TYR A CE2 1 
ATOM   416  C  CZ  . TYR A 1 51  ? 1.161   5.419   15.309  1.00 9.64  ? 51  TYR A CZ  1 
ATOM   417  O  OH  . TYR A 1 51  ? 2.322   4.992   15.948  1.00 8.34  ? 51  TYR A OH  1 
ATOM   418  N  N   . ASP A 1 52  ? -5.402  8.196   12.413  1.00 20.07 ? 52  ASP A N   1 
ATOM   419  C  CA  . ASP A 1 52  ? -6.410  8.437   11.327  1.00 23.29 ? 52  ASP A CA  1 
ATOM   420  C  C   . ASP A 1 52  ? -5.971  9.430   10.215  1.00 24.39 ? 52  ASP A C   1 
ATOM   421  O  O   . ASP A 1 52  ? -6.262  9.219   9.029   1.00 24.84 ? 52  ASP A O   1 
ATOM   422  C  CB  . ASP A 1 52  ? -7.775  8.871   11.914  1.00 24.90 ? 52  ASP A CB  1 
ATOM   423  C  CG  . ASP A 1 52  ? -7.641  9.934   12.952  1.00 31.24 ? 52  ASP A CG  1 
ATOM   424  O  OD1 . ASP A 1 52  ? -7.077  9.653   14.049  1.00 41.78 ? 52  ASP A OD1 1 
ATOM   425  O  OD2 . ASP A 1 52  ? -8.115  11.060  12.703  1.00 39.51 ? 52  ASP A OD2 1 
ATOM   426  N  N   . GLN A 1 53  ? -5.234  10.468  10.589  1.00 22.25 ? 53  GLN A N   1 
ATOM   427  C  CA  . GLN A 1 53  ? -4.744  11.438  9.597   1.00 22.60 ? 53  GLN A CA  1 
ATOM   428  C  C   . GLN A 1 53  ? -3.318  11.184  9.096   1.00 19.20 ? 53  GLN A C   1 
ATOM   429  O  O   . GLN A 1 53  ? -2.726  12.078  8.475   1.00 18.30 ? 53  GLN A O   1 
ATOM   430  C  CB  . GLN A 1 53  ? -4.760  12.846  10.192  1.00 26.68 ? 53  GLN A CB  1 
ATOM   431  C  CG  . GLN A 1 53  ? -6.140  13.339  10.554  1.00 33.79 ? 53  GLN A CG  1 
ATOM   432  C  CD  . GLN A 1 53  ? -6.906  13.589  9.293   1.00 41.27 ? 53  GLN A CD  1 
ATOM   433  O  OE1 . GLN A 1 53  ? -6.589  14.531  8.544   1.00 45.51 ? 53  GLN A OE1 1 
ATOM   434  N  NE2 . GLN A 1 53  ? -7.872  12.711  8.998   1.00 39.22 ? 53  GLN A NE2 1 
ATOM   435  N  N   . ALA A 1 54  ? -2.764  10.000  9.353   1.00 17.63 ? 54  ALA A N   1 
ATOM   436  C  CA  . ALA A 1 54  ? -1.372  9.735   8.988   1.00 14.87 ? 54  ALA A CA  1 
ATOM   437  C  C   . ALA A 1 54  ? -1.197  9.850   7.459   1.00 17.51 ? 54  ALA A C   1 
ATOM   438  O  O   . ALA A 1 54  ? -2.036  9.342   6.672   1.00 19.91 ? 54  ALA A O   1 
ATOM   439  C  CB  . ALA A 1 54  ? -0.931  8.363   9.499   1.00 14.53 ? 54  ALA A CB  1 
ATOM   440  N  N   . THR A 1 55  ? -0.149  10.559  7.044   1.00 14.98 ? 55  THR A N   1 
ATOM   441  C  CA  . THR A 1 55  ? 0.161   10.662  5.589   1.00 16.43 ? 55  THR A CA  1 
ATOM   442  C  C   . THR A 1 55  ? 1.553   10.102  5.295   1.00 13.49 ? 55  THR A C   1 
ATOM   443  O  O   . THR A 1 55  ? 2.535   10.777  5.525   1.00 12.97 ? 55  THR A O   1 
ATOM   444  C  CB  . THR A 1 55  ? 0.315   12.129  5.111   1.00 19.41 ? 55  THR A CB  1 
ATOM   445  O  OG1 . THR A 1 55  ? -0.785  12.895  5.577   1.00 24.60 ? 55  THR A OG1 1 
ATOM   446  C  CG2 . THR A 1 55  ? 0.315   12.099  3.588   1.00 20.47 ? 55  THR A CG2 1 
ATOM   447  N  N   . SER A 1 56  ? 1.596   8.913   4.746   1.00 14.00 ? 56  SER A N   1 
ATOM   448  C  CA  . SER A 1 56  ? 2.878   8.316   4.394   1.00 14.56 ? 56  SER A CA  1 
ATOM   449  C  C   . SER A 1 56  ? 3.347   8.950   3.074   1.00 14.63 ? 56  SER A C   1 
ATOM   450  O  O   . SER A 1 56  ? 2.517   9.384   2.239   1.00 15.93 ? 56  SER A O   1 
ATOM   451  C  CB  . SER A 1 56  ? 2.798   6.798   4.276   1.00 14.43 ? 56  SER A CB  1 
ATOM   452  O  OG  . SER A 1 56  ? 1.913   6.409   3.210   1.00 16.67 ? 56  SER A OG  1 
ATOM   453  N  N   . LEU A 1 57  ? 4.648   9.003   2.890   1.00 13.52 ? 57  LEU A N   1 
ATOM   454  C  CA  . LEU A 1 57  ? 5.196   9.583   1.645   1.00 15.30 ? 57  LEU A CA  1 
ATOM   455  C  C   . LEU A 1 57  ? 6.052   8.633   0.822   1.00 13.52 ? 57  LEU A C   1 
ATOM   456  O  O   . LEU A 1 57  ? 6.014   8.671   -0.430  1.00 11.95 ? 57  LEU A O   1 
ATOM   457  C  CB  . LEU A 1 57  ? 6.039   10.772  2.050   1.00 16.90 ? 57  LEU A CB  1 
ATOM   458  C  CG  . LEU A 1 57  ? 5.181   11.898  2.658   1.00 23.36 ? 57  LEU A CG  1 
ATOM   459  C  CD1 . LEU A 1 57  ? 6.121   13.011  3.097   1.00 24.21 ? 57  LEU A CD1 1 
ATOM   460  C  CD2 . LEU A 1 57  ? 4.158   12.422  1.660   1.00 23.68 ? 57  LEU A CD2 1 
ATOM   461  N  N   . ARG A 1 58  ? 6.919   7.845   1.485   1.00 11.59 ? 58  ARG A N   1 
ATOM   462  C  CA  . ARG A 1 58  ? 8.021   7.269   0.739   1.00 10.81 ? 58  ARG A CA  1 
ATOM   463  C  C   . ARG A 1 58  ? 8.519   6.109   1.571   1.00 10.58 ? 58  ARG A C   1 
ATOM   464  O  O   . ARG A 1 58  ? 8.401   6.123   2.824   1.00 9.75  ? 58  ARG A O   1 
ATOM   465  C  CB  . ARG A 1 58  ? 9.145   8.305   0.612   1.00 12.49 ? 58  ARG A CB  1 
ATOM   466  C  CG  . ARG A 1 58  ? 10.184  7.924   -0.380  1.00 14.75 ? 58  ARG A CG  1 
ATOM   467  C  CD  . ARG A 1 58  ? 11.222  9.028   -0.561  1.00 15.94 ? 58  ARG A CD  1 
ATOM   468  N  NE  . ARG A 1 58  ? 12.020  9.107   0.664   1.00 15.15 ? 58  ARG A NE  1 
ATOM   469  C  CZ  . ARG A 1 58  ? 13.336  9.298   0.633   1.00 15.40 ? 58  ARG A CZ  1 
ATOM   470  N  NH1 . ARG A 1 58  ? 13.939  9.517   -0.544  1.00 15.40 ? 58  ARG A NH1 1 
ATOM   471  N  NH2 . ARG A 1 58  ? 14.001  9.337   1.761   1.00 16.75 ? 58  ARG A NH2 1 
ATOM   472  N  N   . ILE A 1 59  ? 9.109   5.159   0.882   1.00 10.06 ? 59  ILE A N   1 
ATOM   473  C  CA  . ILE A 1 59  ? 9.796   4.044   1.549   1.00 9.79  ? 59  ILE A CA  1 
ATOM   474  C  C   . ILE A 1 59  ? 11.232  4.007   1.033   1.00 10.82 ? 59  ILE A C   1 
ATOM   475  O  O   . ILE A 1 59  ? 11.510  4.185   -0.198  1.00 9.66  ? 59  ILE A O   1 
ATOM   476  C  CB  . ILE A 1 59  ? 8.999   2.715   1.304   1.00 9.20  ? 59  ILE A CB  1 
ATOM   477  C  CG1 . ILE A 1 59  ? 9.561   1.591   2.196   1.00 9.24  ? 59  ILE A CG1 1 
ATOM   478  C  CG2 . ILE A 1 59  ? 8.970   2.262   -0.198  1.00 8.85  ? 59  ILE A CG2 1 
ATOM   479  C  CD1 . ILE A 1 59  ? 8.703   0.312   2.157   1.00 10.06 ? 59  ILE A CD1 1 
ATOM   480  N  N   . LEU A 1 60  ? 12.200  3.767   1.946   1.00 10.46 ? 60  LEU A N   1 
ATOM   481  C  CA  . LEU A 1 60  ? 13.606  3.968   1.620   1.00 9.77  ? 60  LEU A CA  1 
ATOM   482  C  C   . LEU A 1 60  ? 14.410  2.767   2.198   1.00 10.53 ? 60  LEU A C   1 
ATOM   483  O  O   . LEU A 1 60  ? 14.206  2.437   3.366   1.00 10.38 ? 60  LEU A O   1 
ATOM   484  C  CB  . LEU A 1 60  ? 14.088  5.262   2.353   1.00 10.42 ? 60  LEU A CB  1 
ATOM   485  C  CG  . LEU A 1 60  ? 15.614  5.389   2.242   1.00 9.91  ? 60  LEU A CG  1 
ATOM   486  C  CD1 . LEU A 1 60  ? 16.176  5.628   0.871   1.00 10.41 ? 60  LEU A CD1 1 
ATOM   487  C  CD2 . LEU A 1 60  ? 16.130  6.512   3.153   1.00 10.83 ? 60  LEU A CD2 1 
ATOM   488  N  N   . ASN A 1 61  ? 15.235  2.102   1.391   1.00 9.68  ? 61  ASN A N   1 
ATOM   489  C  CA  . ASN A 1 61  ? 16.197  1.125   1.934   1.00 9.90  ? 61  ASN A CA  1 
ATOM   490  C  C   . ASN A 1 61  ? 17.423  1.991   2.333   1.00 9.94  ? 61  ASN A C   1 
ATOM   491  O  O   . ASN A 1 61  ? 18.045  2.581   1.445   1.00 10.81 ? 61  ASN A O   1 
ATOM   492  C  CB  . ASN A 1 61  ? 16.596  0.164   0.797   1.00 9.83  ? 61  ASN A CB  1 
ATOM   493  C  CG  . ASN A 1 61  ? 17.620  -0.839  1.193   1.00 10.56 ? 61  ASN A CG  1 
ATOM   494  O  OD1 . ASN A 1 61  ? 18.467  -0.589  2.068   1.00 11.55 ? 61  ASN A OD1 1 
ATOM   495  N  ND2 . ASN A 1 61  ? 17.541  -2.023  0.605   1.00 10.32 ? 61  ASN A ND2 1 
ATOM   496  N  N   . ASN A 1 62  ? 17.764  2.041   3.620   1.00 10.08 ? 62  ASN A N   1 
ATOM   497  C  CA  . ASN A 1 62  ? 18.864  2.915   4.069   1.00 11.38 ? 62  ASN A CA  1 
ATOM   498  C  C   . ASN A 1 62  ? 20.128  2.112   4.283   1.00 12.13 ? 62  ASN A C   1 
ATOM   499  O  O   . ASN A 1 62  ? 21.121  2.623   4.842   1.00 13.01 ? 62  ASN A O   1 
ATOM   500  C  CB  . ASN A 1 62  ? 18.467  3.676   5.317   1.00 12.29 ? 62  ASN A CB  1 
ATOM   501  C  CG  . ASN A 1 62  ? 18.201  2.778   6.495   1.00 12.37 ? 62  ASN A CG  1 
ATOM   502  O  OD1 . ASN A 1 62  ? 18.472  1.565   6.478   1.00 12.91 ? 62  ASN A OD1 1 
ATOM   503  N  ND2 . ASN A 1 62  ? 17.774  3.395   7.572   1.00 15.46 ? 62  ASN A ND2 1 
ATOM   504  N  N   . GLY A 1 63  ? 20.146  0.863   3.819   1.00 10.94 ? 63  GLY A N   1 
ATOM   505  C  CA  . GLY A 1 63  ? 21.344  0.029   3.947   1.00 10.47 ? 63  GLY A CA  1 
ATOM   506  C  C   . GLY A 1 63  ? 21.382  -0.769  5.246   1.00 10.93 ? 63  GLY A C   1 
ATOM   507  O  O   . GLY A 1 63  ? 22.277  -1.630  5.425   1.00 11.82 ? 63  GLY A O   1 
ATOM   508  N  N   . HIS A 1 64  ? 20.426  -0.488  6.129   1.00 10.44 ? 64  HIS A N   1 
ATOM   509  C  CA  . HIS A 1 64  ? 20.331  -1.143  7.469   1.00 12.01 ? 64  HIS A CA  1 
ATOM   510  C  C   . HIS A 1 64  ? 19.001  -1.793  7.614   1.00 11.58 ? 64  HIS A C   1 
ATOM   511  O  O   . HIS A 1 64  ? 18.933  -2.961  8.058   1.00 13.97 ? 64  HIS A O   1 
ATOM   512  C  CB  . HIS A 1 64  ? 20.508  -0.127  8.607   1.00 13.84 ? 64  HIS A CB  1 
ATOM   513  C  CG  . HIS A 1 64  ? 21.777  0.687   8.456   1.00 15.80 ? 64  HIS A CG  1 
ATOM   514  N  ND1 . HIS A 1 64  ? 22.997  0.101   8.474   1.00 18.62 ? 64  HIS A ND1 1 
ATOM   515  C  CD2 . HIS A 1 64  ? 21.988  2.036   8.316   1.00 17.60 ? 64  HIS A CD2 1 
ATOM   516  C  CE1 . HIS A 1 64  ? 23.955  1.022   8.319   1.00 17.43 ? 64  HIS A CE1 1 
ATOM   517  N  NE2 . HIS A 1 64  ? 23.361  2.208   8.185   1.00 18.14 ? 64  HIS A NE2 1 
ATOM   518  N  N   . ALA A 1 65  ? 17.960  -1.096  7.171   1.00 9.32  ? 65  ALA A N   1 
ATOM   519  C  CA  . ALA A 1 65  ? 16.594  -1.591  7.256   1.00 8.69  ? 65  ALA A CA  1 
ATOM   520  C  C   . ALA A 1 65  ? 15.841  -0.843  6.146   1.00 8.53  ? 65  ALA A C   1 
ATOM   521  O  O   . ALA A 1 65  ? 16.520  -0.315  5.239   1.00 9.19  ? 65  ALA A O   1 
ATOM   522  C  CB  . ALA A 1 65  ? 16.014  -1.321  8.641   1.00 8.41  ? 65  ALA A CB  1 
ATOM   523  N  N   . PHE A 1 66  ? 14.514  -0.884  6.134   1.00 8.57  ? 66  PHE A N   1 
ATOM   524  C  CA  . PHE A 1 66  ? 13.749  0.050   5.245   1.00 9.48  ? 66  PHE A CA  1 
ATOM   525  C  C   . PHE A 1 66  ? 12.880  0.948   6.118   1.00 9.90  ? 66  PHE A C   1 
ATOM   526  O  O   . PHE A 1 66  ? 12.301  0.484   7.158   1.00 10.38 ? 66  PHE A O   1 
ATOM   527  C  CB  . PHE A 1 66  ? 12.944  -0.666  4.160   1.00 9.53  ? 66  PHE A CB  1 
ATOM   528  C  CG  . PHE A 1 66  ? 11.887  -1.593  4.690   1.00 10.12 ? 66  PHE A CG  1 
ATOM   529  C  CD1 . PHE A 1 66  ? 10.611  -1.116  5.007   1.00 10.23 ? 66  PHE A CD1 1 
ATOM   530  C  CD2 . PHE A 1 66  ? 12.167  -3.011  4.874   1.00 10.34 ? 66  PHE A CD2 1 
ATOM   531  C  CE1 . PHE A 1 66  ? 9.632   -1.989  5.512   1.00 12.33 ? 66  PHE A CE1 1 
ATOM   532  C  CE2 . PHE A 1 66  ? 11.164  -3.871  5.420   1.00 11.07 ? 66  PHE A CE2 1 
ATOM   533  C  CZ  . PHE A 1 66  ? 9.910   -3.360  5.728   1.00 11.24 ? 66  PHE A CZ  1 
ATOM   534  N  N   . ASN A 1 67  ? 12.785  2.239   5.746   1.00 9.66  ? 67  ASN A N   1 
ATOM   535  C  CA  . ASN A 1 67  ? 11.981  3.170   6.521   1.00 9.45  ? 67  ASN A CA  1 
ATOM   536  C  C   . ASN A 1 67  ? 10.760  3.570   5.707   1.00 9.42  ? 67  ASN A C   1 
ATOM   537  O  O   . ASN A 1 67  ? 10.908  3.993   4.578   1.00 9.39  ? 67  ASN A O   1 
ATOM   538  C  CB  . ASN A 1 67  ? 12.744  4.450   6.784   1.00 11.12 ? 67  ASN A CB  1 
ATOM   539  C  CG  . ASN A 1 67  ? 13.925  4.259   7.711   1.00 12.32 ? 67  ASN A CG  1 
ATOM   540  O  OD1 . ASN A 1 67  ? 13.955  3.306   8.513   1.00 11.66 ? 67  ASN A OD1 1 
ATOM   541  N  ND2 . ASN A 1 67  ? 14.927  5.185   7.624   1.00 14.06 ? 67  ASN A ND2 1 
ATOM   542  N  N   . VAL A 1 68  ? 9.587   3.522   6.308   1.00 8.44  ? 68  VAL A N   1 
ATOM   543  C  CA  . VAL A 1 68  ? 8.405   4.153   5.708   1.00 8.86  ? 68  VAL A CA  1 
ATOM   544  C  C   . VAL A 1 68  ? 8.244   5.521   6.404   1.00 9.63  ? 68  VAL A C   1 
ATOM   545  O  O   . VAL A 1 68  ? 8.110   5.618   7.681   1.00 8.36  ? 68  VAL A O   1 
ATOM   546  C  CB  . VAL A 1 68  ? 7.144   3.319   5.915   1.00 8.39  ? 68  VAL A CB  1 
ATOM   547  C  CG1 . VAL A 1 68  ? 5.919   4.138   5.409   1.00 8.69  ? 68  VAL A CG1 1 
ATOM   548  C  CG2 . VAL A 1 68  ? 7.233   2.007   5.137   1.00 9.12  ? 68  VAL A CG2 1 
ATOM   549  N  N   . GLU A 1 69  ? 8.316   6.580   5.604   1.00 10.43 ? 69  GLU A N   1 
ATOM   550  C  CA  . GLU A 1 69  ? 8.400   7.935   6.145   1.00 11.75 ? 69  GLU A CA  1 
ATOM   551  C  C   . GLU A 1 69  ? 7.035   8.634   5.978   1.00 11.97 ? 69  GLU A C   1 
ATOM   552  O  O   . GLU A 1 69  ? 6.280   8.351   5.030   1.00 12.86 ? 69  GLU A O   1 
ATOM   553  C  CB  . GLU A 1 69  ? 9.387   8.720   5.303   1.00 12.18 ? 69  GLU A CB  1 
ATOM   554  C  CG  . GLU A 1 69  ? 10.820  8.183   5.337   1.00 14.16 ? 69  GLU A CG  1 
ATOM   555  C  CD  . GLU A 1 69  ? 11.617  8.660   4.123   1.00 15.61 ? 69  GLU A CD  1 
ATOM   556  O  OE1 . GLU A 1 69  ? 11.019  9.325   3.225   1.00 18.15 ? 69  GLU A OE1 1 
ATOM   557  O  OE2 . GLU A 1 69  ? 12.779  8.247   3.960   1.00 16.29 ? 69  GLU A OE2 1 
ATOM   558  N  N   . PHE A 1 70  ? 6.759   9.514   6.933   1.00 11.36 ? 70  PHE A N   1 
ATOM   559  C  CA  . PHE A 1 70  ? 5.468   10.221  7.016   1.00 12.03 ? 70  PHE A CA  1 
ATOM   560  C  C   . PHE A 1 70  ? 5.710   11.676  6.922   1.00 12.88 ? 70  PHE A C   1 
ATOM   561  O  O   . PHE A 1 70  ? 6.780   12.148  7.217   1.00 12.43 ? 70  PHE A O   1 
ATOM   562  C  CB  . PHE A 1 70  ? 4.745   9.887   8.354   1.00 11.20 ? 70  PHE A CB  1 
ATOM   563  C  CG  . PHE A 1 70  ? 4.200   8.502   8.336   1.00 10.57 ? 70  PHE A CG  1 
ATOM   564  C  CD1 . PHE A 1 70  ? 5.004   7.405   8.601   1.00 11.01 ? 70  PHE A CD1 1 
ATOM   565  C  CD2 . PHE A 1 70  ? 2.879   8.279   8.013   1.00 11.33 ? 70  PHE A CD2 1 
ATOM   566  C  CE1 . PHE A 1 70  ? 4.510   6.108   8.520   1.00 10.22 ? 70  PHE A CE1 1 
ATOM   567  C  CE2 . PHE A 1 70  ? 2.362   6.984   7.929   1.00 10.77 ? 70  PHE A CE2 1 
ATOM   568  C  CZ  . PHE A 1 70  ? 3.186   5.884   8.182   1.00 10.87 ? 70  PHE A CZ  1 
ATOM   569  N  N   . ASP A 1 71  ? 4.676   12.408  6.519   1.00 15.63 ? 71  ASP A N   1 
ATOM   570  C  CA  . ASP A 1 71  ? 4.756   13.854  6.613   1.00 19.51 ? 71  ASP A CA  1 
ATOM   571  C  C   . ASP A 1 71  ? 4.520   14.293  8.059   1.00 19.93 ? 71  ASP A C   1 
ATOM   572  O  O   . ASP A 1 71  ? 3.419   14.112  8.577   1.00 25.07 ? 71  ASP A O   1 
ATOM   573  C  CB  . ASP A 1 71  ? 3.689   14.456  5.747   1.00 23.73 ? 71  ASP A CB  1 
ATOM   574  C  CG  . ASP A 1 71  ? 3.651   16.002  5.881   1.00 26.57 ? 71  ASP A CG  1 
ATOM   575  O  OD1 . ASP A 1 71  ? 4.604   16.615  6.369   1.00 29.56 ? 71  ASP A OD1 1 
ATOM   576  O  OD2 . ASP A 1 71  ? 2.644   16.563  5.551   1.00 29.03 ? 71  ASP A OD2 1 
ATOM   577  N  N   . ASP A 1 72  ? 5.500   14.897  8.693   1.00 21.04 ? 72  ASP A N   1 
ATOM   578  C  CA  . ASP A 1 72  ? 5.366   15.306  10.098  1.00 24.46 ? 72  ASP A CA  1 
ATOM   579  C  C   . ASP A 1 72  ? 5.425   16.855  10.235  1.00 28.09 ? 72  ASP A C   1 
ATOM   580  O  O   . ASP A 1 72  ? 5.772   17.366  11.333  1.00 30.28 ? 72  ASP A O   1 
ATOM   581  C  CB  . ASP A 1 72  ? 6.470   14.648  10.959  1.00 26.96 ? 72  ASP A CB  1 
ATOM   582  C  CG  . ASP A 1 72  ? 7.872   15.166  10.615  1.00 26.42 ? 72  ASP A CG  1 
ATOM   583  O  OD1 . ASP A 1 72  ? 8.090   15.714  9.494   1.00 27.50 ? 72  ASP A OD1 1 
ATOM   584  O  OD2 . ASP A 1 72  ? 8.783   15.010  11.438  1.00 30.39 ? 72  ASP A OD2 1 
ATOM   585  N  N   . SER A 1 73  ? 5.172   17.564  9.116   1.00 27.87 ? 73  SER A N   1 
ATOM   586  C  CA  . SER A 1 73  ? 5.127   19.047  9.084   1.00 33.20 ? 73  SER A CA  1 
ATOM   587  C  C   . SER A 1 73  ? 3.878   19.673  9.754   1.00 32.38 ? 73  SER A C   1 
ATOM   588  O  O   . SER A 1 73  ? 3.728   20.907  9.799   1.00 29.20 ? 73  SER A O   1 
ATOM   589  C  CB  . SER A 1 73  ? 5.283   19.580  7.658   1.00 32.48 ? 73  SER A CB  1 
ATOM   590  O  OG  . SER A 1 73  ? 4.124   19.333  6.879   1.00 32.79 ? 73  SER A OG  1 
ATOM   591  N  N   . GLN A 1 74  ? 2.988   18.826  10.260  1.00 29.87 ? 74  GLN A N   1 
ATOM   592  C  CA  . GLN A 1 74  ? 1.973   19.251  11.222  1.00 30.61 ? 74  GLN A CA  1 
ATOM   593  C  C   . GLN A 1 74  ? 1.447   18.057  11.967  1.00 29.97 ? 74  GLN A C   1 
ATOM   594  O  O   . GLN A 1 74  ? 1.769   16.941  11.582  1.00 25.63 ? 74  GLN A O   1 
ATOM   595  C  CB  . GLN A 1 74  ? 0.843   20.039  10.545  1.00 36.66 ? 74  GLN A CB  1 
ATOM   596  C  CG  . GLN A 1 74  ? 0.070   19.320  9.446   1.00 41.04 ? 74  GLN A CG  1 
ATOM   597  C  CD  . GLN A 1 74  ? -0.891  20.279  8.753   1.00 44.61 ? 74  GLN A CD  1 
ATOM   598  O  OE1 . GLN A 1 74  ? -1.465  21.182  9.388   1.00 46.72 ? 74  GLN A OE1 1 
ATOM   599  N  NE2 . GLN A 1 74  ? -1.063  20.097  7.455   1.00 41.91 ? 74  GLN A NE2 1 
ATOM   600  N  N   . ASP A 1 75  ? 0.657   18.320  13.017  1.00 31.20 ? 75  ASP A N   1 
ATOM   601  C  CA  . ASP A 1 75  ? 0.149   17.331  13.964  1.00 33.89 ? 75  ASP A CA  1 
ATOM   602  C  C   . ASP A 1 75  ? -1.014  16.597  13.363  1.00 35.77 ? 75  ASP A C   1 
ATOM   603  O  O   . ASP A 1 75  ? -2.174  17.033  13.458  1.00 36.55 ? 75  ASP A O   1 
ATOM   604  C  CB  . ASP A 1 75  ? -0.321  17.968  15.260  1.00 39.01 ? 75  ASP A CB  1 
ATOM   605  C  CG  . ASP A 1 75  ? 0.743   17.957  16.336  1.00 40.00 ? 75  ASP A CG  1 
ATOM   606  O  OD1 . ASP A 1 75  ? 1.710   17.161  16.232  1.00 40.28 ? 75  ASP A OD1 1 
ATOM   607  O  OD2 . ASP A 1 75  ? 0.597   18.751  17.290  1.00 43.23 ? 75  ASP A OD2 1 
ATOM   608  N  N   . LYS A 1 76  ? -0.690  15.479  12.749  1.00 29.07 ? 76  LYS A N   1 
ATOM   609  C  CA  . LYS A 1 76  ? -1.682  14.646  12.051  1.00 32.74 ? 76  LYS A CA  1 
ATOM   610  C  C   . LYS A 1 76  ? -1.790  13.250  12.667  1.00 32.63 ? 76  LYS A C   1 
ATOM   611  O  O   . LYS A 1 76  ? -2.893  12.711  12.782  1.00 43.26 ? 76  LYS A O   1 
ATOM   612  C  CB  . LYS A 1 76  ? -1.282  14.470  10.601  1.00 32.62 ? 76  LYS A CB  1 
ATOM   613  C  CG  . LYS A 1 76  ? -1.801  15.555  9.675   1.00 37.32 ? 76  LYS A CG  1 
ATOM   614  C  CD  . LYS A 1 76  ? -0.952  15.515  8.421   1.00 38.93 ? 76  LYS A CD  1 
ATOM   615  C  CE  . LYS A 1 76  ? -1.451  16.500  7.380   1.00 40.17 ? 76  LYS A CE  1 
ATOM   616  N  NZ  . LYS A 1 76  ? -0.372  16.652  6.376   1.00 38.09 ? 76  LYS A NZ  1 
ATOM   617  N  N   . ALA A 1 77  ? -0.648  12.666  13.015  1.00 24.27 ? 77  ALA A N   1 
ATOM   618  C  CA  . ALA A 1 77  ? -0.580  11.256  13.489  1.00 19.85 ? 77  ALA A CA  1 
ATOM   619  C  C   . ALA A 1 77  ? 0.284   11.396  14.731  1.00 17.66 ? 77  ALA A C   1 
ATOM   620  O  O   . ALA A 1 77  ? 1.467   11.762  14.596  1.00 16.75 ? 77  ALA A O   1 
ATOM   621  C  CB  . ALA A 1 77  ? 0.131   10.399  12.442  1.00 19.15 ? 77  ALA A CB  1 
ATOM   622  N  N   . VAL A 1 78  ? -0.283  11.166  15.911  1.00 13.95 ? 78  VAL A N   1 
ATOM   623  C  CA  . VAL A 1 78  ? 0.442   11.413  17.143  1.00 14.49 ? 78  VAL A CA  1 
ATOM   624  C  C   . VAL A 1 78  ? 0.221   10.301  18.162  1.00 12.56 ? 78  VAL A C   1 
ATOM   625  O  O   . VAL A 1 78  ? -0.854  9.649   18.225  1.00 13.19 ? 78  VAL A O   1 
ATOM   626  C  CB  . VAL A 1 78  ? 0.025   12.746  17.807  1.00 15.40 ? 78  VAL A CB  1 
ATOM   627  C  CG1 . VAL A 1 78  ? 0.346   13.939  16.892  1.00 16.41 ? 78  VAL A CG1 1 
ATOM   628  C  CG2 . VAL A 1 78  ? -1.459  12.721  18.124  1.00 16.63 ? 78  VAL A CG2 1 
ATOM   629  N  N   . LEU A 1 79  ? 1.211   10.200  19.030  1.00 10.97 ? 79  LEU A N   1 
ATOM   630  C  CA  . LEU A 1 79  ? 1.173   9.276   20.174  1.00 10.75 ? 79  LEU A CA  1 
ATOM   631  C  C   . LEU A 1 79  ? 1.185   10.153  21.422  1.00 11.14 ? 79  LEU A C   1 
ATOM   632  O  O   . LEU A 1 79  ? 2.003   11.085  21.539  1.00 10.59 ? 79  LEU A O   1 
ATOM   633  C  CB  . LEU A 1 79  ? 2.398   8.332   20.073  1.00 10.20 ? 79  LEU A CB  1 
ATOM   634  C  CG  . LEU A 1 79  ? 2.526   7.300   21.159  1.00 10.20 ? 79  LEU A CG  1 
ATOM   635  C  CD1 . LEU A 1 79  ? 1.434   6.225   21.102  1.00 11.01 ? 79  LEU A CD1 1 
ATOM   636  C  CD2 . LEU A 1 79  ? 3.921   6.655   21.096  1.00 9.18  ? 79  LEU A CD2 1 
ATOM   637  N  N   . LYS A 1 80  ? 0.309   9.855   22.365  1.00 10.54 ? 80  LYS A N   1 
ATOM   638  C  CA  . LYS A 1 80  ? 0.174   10.643  23.601  1.00 13.35 ? 80  LYS A CA  1 
ATOM   639  C  C   . LYS A 1 80  ? -0.199  9.660   24.740  1.00 12.22 ? 80  LYS A C   1 
ATOM   640  O  O   . LYS A 1 80  ? -0.519  8.514   24.464  1.00 11.51 ? 80  LYS A O   1 
ATOM   641  C  CB  . LYS A 1 80  ? -1.043  11.604  23.496  1.00 17.65 ? 80  LYS A CB  1 
ATOM   642  C  CG  . LYS A 1 80  ? -1.039  12.701  22.447  1.00 24.90 ? 80  LYS A CG  1 
ATOM   643  C  CD  . LYS A 1 80  ? -2.310  13.531  22.769  1.00 23.92 ? 80  LYS A CD  1 
ATOM   644  C  CE  . LYS A 1 80  ? -3.448  13.465  21.736  1.00 34.22 ? 80  LYS A CE  1 
ATOM   645  N  NZ  . LYS A 1 80  ? -3.480  14.731  20.870  1.00 37.90 ? 80  LYS A NZ  1 
ATOM   646  N  N   . GLY A 1 81  ? -0.141  10.084  25.999  1.00 12.09 ? 81  GLY A N   1 
ATOM   647  C  CA  . GLY A 1 81  ? -0.741  9.260   27.032  1.00 12.57 ? 81  GLY A CA  1 
ATOM   648  C  C   . GLY A 1 81  ? 0.267   8.240   27.468  1.00 13.77 ? 81  GLY A C   1 
ATOM   649  O  O   . GLY A 1 81  ? 1.464   8.391   27.139  1.00 12.22 ? 81  GLY A O   1 
ATOM   650  N  N   . GLY A 1 82  ? -0.184  7.206   28.188  1.00 13.75 ? 82  GLY A N   1 
ATOM   651  C  CA  . GLY A 1 82  ? 0.777   6.250   28.745  1.00 14.36 ? 82  GLY A CA  1 
ATOM   652  C  C   . GLY A 1 82  ? 1.788   6.968   29.608  1.00 14.82 ? 82  GLY A C   1 
ATOM   653  O  O   . GLY A 1 82  ? 1.400   7.768   30.502  1.00 15.06 ? 82  GLY A O   1 
ATOM   654  N  N   . PRO A 1 83  ? 3.102   6.717   29.394  1.00 12.26 ? 83  PRO A N   1 
ATOM   655  C  CA  . PRO A 1 83  ? 4.066   7.346   30.246  1.00 12.49 ? 83  PRO A CA  1 
ATOM   656  C  C   . PRO A 1 83  ? 4.420   8.752   29.749  1.00 12.16 ? 83  PRO A C   1 
ATOM   657  O  O   . PRO A 1 83  ? 5.267   9.424   30.333  1.00 14.66 ? 83  PRO A O   1 
ATOM   658  C  CB  . PRO A 1 83  ? 5.306   6.426   30.116  1.00 12.12 ? 83  PRO A CB  1 
ATOM   659  C  CG  . PRO A 1 83  ? 5.222   5.920   28.662  1.00 12.34 ? 83  PRO A CG  1 
ATOM   660  C  CD  . PRO A 1 83  ? 3.728   5.799   28.394  1.00 12.10 ? 83  PRO A CD  1 
ATOM   661  N  N   . LEU A 1 84  ? 3.851   9.169   28.633  1.00 11.94 ? 84  LEU A N   1 
ATOM   662  C  CA  . LEU A 1 84  ? 4.370   10.324  27.957  1.00 10.98 ? 84  LEU A CA  1 
ATOM   663  C  C   . LEU A 1 84  ? 3.715   11.620  28.473  1.00 13.52 ? 84  LEU A C   1 
ATOM   664  O  O   . LEU A 1 84  ? 2.507   11.637  28.731  1.00 13.19 ? 84  LEU A O   1 
ATOM   665  C  CB  . LEU A 1 84  ? 4.058   10.219  26.493  1.00 10.14 ? 84  LEU A CB  1 
ATOM   666  C  CG  . LEU A 1 84  ? 4.616   8.975   25.739  1.00 10.03 ? 84  LEU A CG  1 
ATOM   667  C  CD1 . LEU A 1 84  ? 4.109   8.954   24.325  1.00 9.20  ? 84  LEU A CD1 1 
ATOM   668  C  CD2 . LEU A 1 84  ? 6.186   9.001   25.791  1.00 9.43  ? 84  LEU A CD2 1 
ATOM   669  N  N   . ASP A 1 85  ? 4.527   12.665  28.538  1.00 14.27 ? 85  ASP A N   1 
ATOM   670  C  CA  . ASP A 1 85  ? 4.039   14.020  28.772  1.00 17.42 ? 85  ASP A CA  1 
ATOM   671  C  C   . ASP A 1 85  ? 4.059   14.708  27.443  1.00 18.60 ? 85  ASP A C   1 
ATOM   672  O  O   . ASP A 1 85  ? 5.083   14.748  26.773  1.00 18.92 ? 85  ASP A O   1 
ATOM   673  C  CB  . ASP A 1 85  ? 4.963   14.723  29.755  1.00 21.20 ? 85  ASP A CB  1 
ATOM   674  C  CG  . ASP A 1 85  ? 4.738   14.233  31.182  1.00 30.92 ? 85  ASP A CG  1 
ATOM   675  O  OD1 . ASP A 1 85  ? 3.643   13.655  31.507  1.00 34.40 ? 85  ASP A OD1 1 
ATOM   676  O  OD2 . ASP A 1 85  ? 5.665   14.412  32.002  1.00 33.45 ? 85  ASP A OD2 1 
ATOM   677  N  N   . GLY A 1 86  ? 2.930   15.243  27.026  1.00 17.27 ? 86  GLY A N   1 
ATOM   678  C  CA  . GLY A 1 86  ? 2.944   16.037  25.806  1.00 15.96 ? 86  GLY A CA  1 
ATOM   679  C  C   . GLY A 1 86  ? 2.639   15.201  24.555  1.00 16.68 ? 86  GLY A C   1 
ATOM   680  O  O   . GLY A 1 86  ? 1.996   14.170  24.650  1.00 17.71 ? 86  GLY A O   1 
ATOM   681  N  N   . THR A 1 87  ? 3.101   15.647  23.393  1.00 14.25 ? 87  THR A N   1 
ATOM   682  C  CA  . THR A 1 87  ? 2.562   15.120  22.151  1.00 14.95 ? 87  THR A CA  1 
ATOM   683  C  C   . THR A 1 87  ? 3.726   14.695  21.310  1.00 13.56 ? 87  THR A C   1 
ATOM   684  O  O   . THR A 1 87  ? 4.695   15.478  21.159  1.00 12.77 ? 87  THR A O   1 
ATOM   685  C  CB  . THR A 1 87  ? 1.884   16.263  21.343  1.00 17.24 ? 87  THR A CB  1 
ATOM   686  O  OG1 . THR A 1 87  ? 0.688   16.606  22.025  1.00 20.42 ? 87  THR A OG1 1 
ATOM   687  C  CG2 . THR A 1 87  ? 1.483   15.758  19.916  1.00 17.65 ? 87  THR A CG2 1 
ATOM   688  N  N   . TYR A 1 88  ? 3.664   13.438  20.855  1.00 10.42 ? 88  TYR A N   1 
ATOM   689  C  CA  . TYR A 1 88  ? 4.727   12.968  19.971  1.00 10.05 ? 88  TYR A CA  1 
ATOM   690  C  C   . TYR A 1 88  ? 4.228   12.683  18.574  1.00 10.36 ? 88  TYR A C   1 
ATOM   691  O  O   . TYR A 1 88  ? 3.305   11.913  18.414  1.00 11.80 ? 88  TYR A O   1 
ATOM   692  C  CB  . TYR A 1 88  ? 5.405   11.714  20.572  1.00 8.67  ? 88  TYR A CB  1 
ATOM   693  C  CG  . TYR A 1 88  ? 6.188   11.907  21.866  1.00 8.52  ? 88  TYR A CG  1 
ATOM   694  C  CD1 . TYR A 1 88  ? 5.551   12.319  23.079  1.00 7.50  ? 88  TYR A CD1 1 
ATOM   695  C  CD2 . TYR A 1 88  ? 7.600   11.752  21.875  1.00 7.80  ? 88  TYR A CD2 1 
ATOM   696  C  CE1 . TYR A 1 88  ? 6.302   12.551  24.236  1.00 8.21  ? 88  TYR A CE1 1 
ATOM   697  C  CE2 . TYR A 1 88  ? 8.352   11.900  23.068  1.00 7.91  ? 88  TYR A CE2 1 
ATOM   698  C  CZ  . TYR A 1 88  ? 7.713   12.317  24.230  1.00 8.14  ? 88  TYR A CZ  1 
ATOM   699  O  OH  . TYR A 1 88  ? 8.430   12.430  25.380  1.00 8.44  ? 88  TYR A OH  1 
ATOM   700  N  N   . ARG A 1 89  ? 4.917   13.194  17.547  1.00 9.69  ? 89  ARG A N   1 
ATOM   701  C  CA  . ARG A 1 89  ? 4.494   13.073  16.154  1.00 10.20 ? 89  ARG A CA  1 
ATOM   702  C  C   . ARG A 1 89  ? 5.150   11.912  15.432  1.00 10.05 ? 89  ARG A C   1 
ATOM   703  O  O   . ARG A 1 89  ? 6.375   11.788  15.496  1.00 9.87  ? 89  ARG A O   1 
ATOM   704  C  CB  . ARG A 1 89  ? 4.800   14.391  15.435  1.00 13.01 ? 89  ARG A CB  1 
ATOM   705  C  CG  . ARG A 1 89  ? 4.203   14.605  14.061  1.00 18.68 ? 89  ARG A CG  1 
ATOM   706  C  CD  . ARG A 1 89  ? 4.526   16.094  13.643  1.00 18.51 ? 89  ARG A CD  1 
ATOM   707  N  NE  . ARG A 1 89  ? 3.872   17.051  14.525  1.00 21.14 ? 89  ARG A NE  1 
ATOM   708  C  CZ  . ARG A 1 89  ? 3.957   18.386  14.386  1.00 23.84 ? 89  ARG A CZ  1 
ATOM   709  N  NH1 . ARG A 1 89  ? 4.677   18.905  13.412  1.00 19.01 ? 89  ARG A NH1 1 
ATOM   710  N  NH2 . ARG A 1 89  ? 3.310   19.206  15.231  1.00 24.29 ? 89  ARG A NH2 1 
ATOM   711  N  N   . LEU A 1 90  ? 4.351   11.072  14.755  1.00 10.04 ? 90  LEU A N   1 
ATOM   712  C  CA  . LEU A 1 90  ? 4.902   9.912   14.003  1.00 10.22 ? 90  LEU A CA  1 
ATOM   713  C  C   . LEU A 1 90  ? 5.734   10.499  12.865  1.00 10.46 ? 90  LEU A C   1 
ATOM   714  O  O   . LEU A 1 90  ? 5.235   11.344  12.094  1.00 11.86 ? 90  LEU A O   1 
ATOM   715  C  CB  . LEU A 1 90  ? 3.753   9.077   13.431  1.00 11.77 ? 90  LEU A CB  1 
ATOM   716  C  CG  . LEU A 1 90  ? 4.242   7.943   12.497  1.00 11.53 ? 90  LEU A CG  1 
ATOM   717  C  CD1 . LEU A 1 90  ? 5.004   6.854   13.241  1.00 12.15 ? 90  LEU A CD1 1 
ATOM   718  C  CD2 . LEU A 1 90  ? 3.035   7.298   11.858  1.00 12.98 ? 90  LEU A CD2 1 
ATOM   719  N  N   . ILE A 1 91  ? 6.953   10.022  12.721  1.00 10.04 ? 91  ILE A N   1 
ATOM   720  C  CA  . ILE A 1 91  ? 7.822   10.424  11.621  1.00 10.38 ? 91  ILE A CA  1 
ATOM   721  C  C   . ILE A 1 91  ? 8.140   9.282   10.659  1.00 9.84  ? 91  ILE A C   1 
ATOM   722  O  O   . ILE A 1 91  ? 8.229   9.481   9.435   1.00 9.72  ? 91  ILE A O   1 
ATOM   723  C  CB  . ILE A 1 91  ? 9.091   11.160  12.114  1.00 10.75 ? 91  ILE A CB  1 
ATOM   724  C  CG1 . ILE A 1 91  ? 9.990   11.474  10.901  1.00 13.45 ? 91  ILE A CG1 1 
ATOM   725  C  CG2 . ILE A 1 91  ? 9.898   10.365  13.140  1.00 10.65 ? 91  ILE A CG2 1 
ATOM   726  C  CD1 . ILE A 1 91  ? 11.032  12.461  11.311  1.00 14.93 ? 91  ILE A CD1 1 
ATOM   727  N  N   . GLN A 1 92  ? 8.292   8.055   11.199  1.00 8.42  ? 92  GLN A N   1 
ATOM   728  C  CA  . GLN A 1 92  ? 8.600   6.940   10.315  1.00 8.14  ? 92  GLN A CA  1 
ATOM   729  C  C   . GLN A 1 92  ? 8.398   5.646   11.084  1.00 7.50  ? 92  GLN A C   1 
ATOM   730  O  O   . GLN A 1 92  ? 8.267   5.686   12.278  1.00 7.41  ? 92  GLN A O   1 
ATOM   731  C  CB  . GLN A 1 92  ? 10.084  6.992   9.840   1.00 8.47  ? 92  GLN A CB  1 
ATOM   732  C  CG  . GLN A 1 92  ? 11.199  6.997   10.950  1.00 9.45  ? 92  GLN A CG  1 
ATOM   733  C  CD  . GLN A 1 92  ? 11.894  5.644   10.956  1.00 11.08 ? 92  GLN A CD  1 
ATOM   734  O  OE1 . GLN A 1 92  ? 11.331  4.647   11.340  1.00 10.12 ? 92  GLN A OE1 1 
ATOM   735  N  NE2 . GLN A 1 92  ? 13.091  5.604   10.390  1.00 11.59 ? 92  GLN A NE2 1 
ATOM   736  N  N   . PHE A 1 93  ? 8.284   4.537   10.361  1.00 7.15  ? 93  PHE A N   1 
ATOM   737  C  CA  . PHE A 1 93  ? 8.452   3.223   10.986  1.00 7.16  ? 93  PHE A CA  1 
ATOM   738  C  C   . PHE A 1 93  ? 9.419   2.343   10.194  1.00 7.17  ? 93  PHE A C   1 
ATOM   739  O  O   . PHE A 1 93  ? 9.728   2.561   9.023   1.00 7.09  ? 93  PHE A O   1 
ATOM   740  C  CB  . PHE A 1 93  ? 7.103   2.486   11.251  1.00 6.91  ? 93  PHE A CB  1 
ATOM   741  C  CG  . PHE A 1 93  ? 6.366   2.026   10.004  1.00 7.72  ? 93  PHE A CG  1 
ATOM   742  C  CD1 . PHE A 1 93  ? 6.775   0.908   9.275   1.00 7.42  ? 93  PHE A CD1 1 
ATOM   743  C  CD2 . PHE A 1 93  ? 5.221   2.765   9.571   1.00 7.30  ? 93  PHE A CD2 1 
ATOM   744  C  CE1 . PHE A 1 93  ? 6.114   0.480   8.126   1.00 7.75  ? 93  PHE A CE1 1 
ATOM   745  C  CE2 . PHE A 1 93  ? 4.502   2.294   8.438   1.00 7.62  ? 93  PHE A CE2 1 
ATOM   746  C  CZ  . PHE A 1 93  ? 4.952   1.184   7.725   1.00 7.60  ? 93  PHE A CZ  1 
ATOM   747  N  N   . HIS A 1 94  ? 9.943   1.317   10.873  1.00 6.57  ? 94  HIS A N   1 
ATOM   748  C  CA  . HIS A 1 94  ? 10.816  0.366   10.217  1.00 6.53  ? 94  HIS A CA  1 
ATOM   749  C  C   . HIS A 1 94  ? 10.755  -0.879  11.049  1.00 6.46  ? 94  HIS A C   1 
ATOM   750  O  O   . HIS A 1 94  ? 10.076  -0.913  12.109  1.00 7.14  ? 94  HIS A O   1 
ATOM   751  C  CB  . HIS A 1 94  ? 12.277  0.854   10.196  1.00 6.44  ? 94  HIS A CB  1 
ATOM   752  C  CG  . HIS A 1 94  ? 12.775  1.151   11.576  1.00 6.27  ? 94  HIS A CG  1 
ATOM   753  N  ND1 . HIS A 1 94  ? 12.531  2.322   12.193  1.00 6.00  ? 94  HIS A ND1 1 
ATOM   754  C  CD2 . HIS A 1 94  ? 13.460  0.361   12.469  1.00 6.45  ? 94  HIS A CD2 1 
ATOM   755  C  CE1 . HIS A 1 94  ? 13.086  2.304   13.426  1.00 6.32  ? 94  HIS A CE1 1 
ATOM   756  N  NE2 . HIS A 1 94  ? 13.641  1.080   13.614  1.00 6.46  ? 94  HIS A NE2 1 
ATOM   757  N  N   . PHE A 1 95  ? 11.420  -1.915  10.572  1.00 5.91  ? 95  PHE A N   1 
ATOM   758  C  CA  . PHE A 1 95  ? 11.489  -3.200  11.290  1.00 6.18  ? 95  PHE A CA  1 
ATOM   759  C  C   . PHE A 1 95  ? 12.955  -3.634  11.495  1.00 6.03  ? 95  PHE A C   1 
ATOM   760  O  O   . PHE A 1 95  ? 13.901  -3.182  10.806  1.00 6.34  ? 95  PHE A O   1 
ATOM   761  C  CB  . PHE A 1 95  ? 10.827  -4.328  10.472  1.00 6.12  ? 95  PHE A CB  1 
ATOM   762  C  CG  . PHE A 1 95  ? 9.392   -4.057  10.159  1.00 6.73  ? 95  PHE A CG  1 
ATOM   763  C  CD1 . PHE A 1 95  ? 9.068   -3.187  9.113   1.00 7.28  ? 95  PHE A CD1 1 
ATOM   764  C  CD2 . PHE A 1 95  ? 8.376   -4.746  10.868  1.00 7.37  ? 95  PHE A CD2 1 
ATOM   765  C  CE1 . PHE A 1 95  ? 7.725   -2.977  8.740   1.00 7.18  ? 95  PHE A CE1 1 
ATOM   766  C  CE2 . PHE A 1 95  ? 7.035   -4.534  10.501  1.00 7.43  ? 95  PHE A CE2 1 
ATOM   767  C  CZ  . PHE A 1 95  ? 6.729   -3.636  9.436   1.00 7.54  ? 95  PHE A CZ  1 
ATOM   768  N  N   . HIS A 1 96  ? 13.081  -4.623  12.381  1.00 5.86  ? 96  HIS A N   1 
ATOM   769  C  CA  . HIS A 1 96  ? 14.318  -5.420  12.510  1.00 5.87  ? 96  HIS A CA  1 
ATOM   770  C  C   . HIS A 1 96  ? 13.908  -6.878  12.396  1.00 5.94  ? 96  HIS A C   1 
ATOM   771  O  O   . HIS A 1 96  ? 12.819  -7.240  12.948  1.00 6.09  ? 96  HIS A O   1 
ATOM   772  C  CB  . HIS A 1 96  ? 14.965  -5.195  13.879  1.00 5.87  ? 96  HIS A CB  1 
ATOM   773  C  CG  . HIS A 1 96  ? 15.266  -3.738  14.167  1.00 6.07  ? 96  HIS A CG  1 
ATOM   774  N  ND1 . HIS A 1 96  ? 16.506  -3.198  13.954  1.00 5.99  ? 96  HIS A ND1 1 
ATOM   775  C  CD2 . HIS A 1 96  ? 14.418  -2.694  14.542  1.00 6.29  ? 96  HIS A CD2 1 
ATOM   776  C  CE1 . HIS A 1 96  ? 16.466  -1.874  14.318  1.00 6.11  ? 96  HIS A CE1 1 
ATOM   777  N  NE2 . HIS A 1 96  ? 15.169  -1.557  14.594  1.00 6.49  ? 96  HIS A NE2 1 
ATOM   778  N  N   . TRP A 1 97  ? 14.692  -7.710  11.702  1.00 6.21  ? 97  TRP A N   1 
ATOM   779  C  CA  . TRP A 1 97  ? 14.272  -9.088  11.574  1.00 6.74  ? 97  TRP A CA  1 
ATOM   780  C  C   . TRP A 1 97  ? 15.407  -10.018 11.454  1.00 6.91  ? 97  TRP A C   1 
ATOM   781  O  O   . TRP A 1 97  ? 16.567  -9.588  11.356  1.00 6.82  ? 97  TRP A O   1 
ATOM   782  C  CB  . TRP A 1 97  ? 13.307  -9.216  10.384  1.00 7.23  ? 97  TRP A CB  1 
ATOM   783  C  CG  . TRP A 1 97  ? 13.939  -8.823  9.078   1.00 7.03  ? 97  TRP A CG  1 
ATOM   784  C  CD1 . TRP A 1 97  ? 14.602  -9.642  8.165   1.00 7.44  ? 97  TRP A CD1 1 
ATOM   785  C  CD2 . TRP A 1 97  ? 13.999  -7.480  8.499   1.00 7.71  ? 97  TRP A CD2 1 
ATOM   786  N  NE1 . TRP A 1 97  ? 15.048  -8.913  7.092   1.00 7.89  ? 97  TRP A NE1 1 
ATOM   787  C  CE2 . TRP A 1 97  ? 14.718  -7.609  7.231   1.00 7.42  ? 97  TRP A CE2 1 
ATOM   788  C  CE3 . TRP A 1 97  ? 13.542  -6.232  8.890   1.00 6.63  ? 97  TRP A CE3 1 
ATOM   789  C  CZ2 . TRP A 1 97  ? 14.955  -6.521  6.410   1.00 7.57  ? 97  TRP A CZ2 1 
ATOM   790  C  CZ3 . TRP A 1 97  ? 13.788  -5.144  8.054   1.00 7.06  ? 97  TRP A CZ3 1 
ATOM   791  C  CH2 . TRP A 1 97  ? 14.476  -5.286  6.846   1.00 7.05  ? 97  TRP A CH2 1 
ATOM   792  N  N   . GLY A 1 98  ? 15.067  -11.309 11.447  1.00 7.28  ? 98  GLY A N   1 
ATOM   793  C  CA  . GLY A 1 98  ? 16.135  -12.349 11.512  1.00 7.37  ? 98  GLY A CA  1 
ATOM   794  C  C   . GLY A 1 98  ? 16.340  -13.093 10.186  1.00 8.10  ? 98  GLY A C   1 
ATOM   795  O  O   . GLY A 1 98  ? 15.657  -12.867 9.175   1.00 8.55  ? 98  GLY A O   1 
ATOM   796  N  N   . SER A 1 99  ? 17.312  -13.971 10.230  1.00 9.53  ? 99  SER A N   1 
ATOM   797  C  CA  . SER A 1 99  ? 17.521  -14.893 9.076   1.00 9.20  ? 99  SER A CA  1 
ATOM   798  C  C   . SER A 1 99  ? 16.664  -16.140 9.223   1.00 10.84 ? 99  SER A C   1 
ATOM   799  O  O   . SER A 1 99  ? 16.564  -16.934 8.280   1.00 10.38 ? 99  SER A O   1 
ATOM   800  C  CB  . SER A 1 99  ? 18.998  -15.286 9.040   1.00 10.37 ? 99  SER A CB  1 
ATOM   801  O  OG  . SER A 1 99  ? 19.448  -15.806 10.295  1.00 10.69 ? 99  SER A OG  1 
ATOM   802  N  N   . LEU A 1 100 ? 16.148  -16.371 10.427  1.00 10.14 ? 100 LEU A N   1 
ATOM   803  C  CA  . LEU A 1 100 ? 15.288  -17.500 10.765  1.00 11.17 ? 100 LEU A CA  1 
ATOM   804  C  C   . LEU A 1 100 ? 14.173  -16.975 11.675  1.00 11.25 ? 100 LEU A C   1 
ATOM   805  O  O   . LEU A 1 100 ? 14.363  -16.010 12.401  1.00 10.19 ? 100 LEU A O   1 
ATOM   806  C  CB  . LEU A 1 100 ? 16.046  -18.602 11.539  1.00 12.54 ? 100 LEU A CB  1 
ATOM   807  C  CG  . LEU A 1 100 ? 17.420  -19.076 10.979  1.00 15.90 ? 100 LEU A CG  1 
ATOM   808  C  CD1 . LEU A 1 100 ? 18.253  -19.720 12.088  1.00 17.95 ? 100 LEU A CD1 1 
ATOM   809  C  CD2 . LEU A 1 100 ? 17.033  -20.099 9.939   1.00 16.79 ? 100 LEU A CD2 1 
ATOM   810  N  N   . ASP A 1 101 ? 13.092  -17.711 11.770  1.00 10.57 ? 101 ASP A N   1 
ATOM   811  C  CA  . ASP A 1 101 ? 11.937  -17.215 12.543  1.00 12.07 ? 101 ASP A CA  1 
ATOM   812  C  C   . ASP A 1 101 ? 12.168  -17.115 14.020  1.00 11.86 ? 101 ASP A C   1 
ATOM   813  O  O   . ASP A 1 101 ? 11.424  -16.429 14.699  1.00 13.60 ? 101 ASP A O   1 
ATOM   814  C  CB  . ASP A 1 101 ? 10.708  -18.129 12.336  1.00 13.29 ? 101 ASP A CB  1 
ATOM   815  C  CG  . ASP A 1 101 ? 10.241  -18.221 10.875  1.00 16.54 ? 101 ASP A CG  1 
ATOM   816  O  OD1 . ASP A 1 101 ? 10.633  -17.373 9.982   1.00 14.81 ? 101 ASP A OD1 1 
ATOM   817  O  OD2 . ASP A 1 101 ? 9.467   -19.195 10.603  1.00 19.27 ? 101 ASP A OD2 1 
ATOM   818  N  N   . GLY A 1 102 ? 13.131  -17.887 14.525  1.00 11.58 ? 102 GLY A N   1 
ATOM   819  C  CA  . GLY A 1 102 ? 13.480  -17.853 15.956  1.00 12.45 ? 102 GLY A CA  1 
ATOM   820  C  C   . GLY A 1 102 ? 14.349  -16.692 16.445  1.00 11.70 ? 102 GLY A C   1 
ATOM   821  O  O   . GLY A 1 102 ? 14.727  -16.677 17.615  1.00 11.31 ? 102 GLY A O   1 
ATOM   822  N  N   . GLN A 1 103 ? 14.602  -15.680 15.607  1.00 9.87  ? 103 GLN A N   1 
ATOM   823  C  CA  . GLN A 1 103 ? 15.393  -14.530 16.054  1.00 9.45  ? 103 GLN A CA  1 
ATOM   824  C  C   . GLN A 1 103 ? 15.021  -13.382 15.117  1.00 8.61  ? 103 GLN A C   1 
ATOM   825  O  O   . GLN A 1 103 ? 14.436  -13.595 14.060  1.00 8.32  ? 103 GLN A O   1 
ATOM   826  C  CB  . GLN A 1 103 ? 16.891  -14.834 15.942  1.00 11.00 ? 103 GLN A CB  1 
ATOM   827  C  CG  . GLN A 1 103 ? 17.373  -15.054 14.485  1.00 12.51 ? 103 GLN A CG  1 
ATOM   828  C  CD  . GLN A 1 103 ? 18.699  -15.775 14.441  1.00 16.41 ? 103 GLN A CD  1 
ATOM   829  O  OE1 . GLN A 1 103 ? 18.765  -16.933 14.883  1.00 20.52 ? 103 GLN A OE1 1 
ATOM   830  N  NE2 . GLN A 1 103 ? 19.730  -15.160 13.813  1.00 14.37 ? 103 GLN A NE2 1 
ATOM   831  N  N   . GLY A 1 104 ? 15.308  -12.164 15.569  1.00 7.69  ? 104 GLY A N   1 
ATOM   832  C  CA  . GLY A 1 104 ? 15.059  -11.008 14.754  1.00 7.61  ? 104 GLY A CA  1 
ATOM   833  C  C   . GLY A 1 104 ? 14.581  -9.832  15.584  1.00 8.70  ? 104 GLY A C   1 
ATOM   834  O  O   . GLY A 1 104 ? 14.821  -8.683  15.214  1.00 8.82  ? 104 GLY A O   1 
ATOM   835  N  N   . SER A 1 105 ? 13.875  -10.094 16.689  1.00 7.75  ? 105 SER A N   1 
ATOM   836  C  CA  . SER A 1 105 ? 13.414  -8.918  17.499  1.00 7.01  ? 105 SER A CA  1 
ATOM   837  C  C   . SER A 1 105 ? 14.663  -8.388  18.311  1.00 6.12  ? 105 SER A C   1 
ATOM   838  O  O   . SER A 1 105 ? 15.679  -9.072  18.545  1.00 6.84  ? 105 SER A O   1 
ATOM   839  C  CB  . SER A 1 105 ? 12.269  -9.256  18.415  1.00 6.54  ? 105 SER A CB  1 
ATOM   840  O  OG  . SER A 1 105 ? 12.749  -10.191 19.414  1.00 7.91  ? 105 SER A OG  1 
ATOM   841  N  N   . GLU A 1 106 ? 14.536  -7.141  18.713  1.00 6.08  ? 106 GLU A N   1 
ATOM   842  C  CA  . GLU A 1 106 ? 15.527  -6.460  19.517  1.00 6.28  ? 106 GLU A CA  1 
ATOM   843  C  C   . GLU A 1 106 ? 15.202  -6.650  21.004  1.00 6.11  ? 106 GLU A C   1 
ATOM   844  O  O   . GLU A 1 106 ? 15.990  -7.216  21.741  1.00 5.35  ? 106 GLU A O   1 
ATOM   845  C  CB  . GLU A 1 106 ? 15.579  -4.954  19.126  1.00 6.35  ? 106 GLU A CB  1 
ATOM   846  C  CG  . GLU A 1 106 ? 15.987  -4.843  17.637  1.00 6.66  ? 106 GLU A CG  1 
ATOM   847  C  CD  . GLU A 1 106 ? 16.725  -3.585  17.334  1.00 7.03  ? 106 GLU A CD  1 
ATOM   848  O  OE1 . GLU A 1 106 ? 16.119  -2.481  17.548  1.00 6.55  ? 106 GLU A OE1 1 
ATOM   849  O  OE2 . GLU A 1 106 ? 17.935  -3.646  16.973  1.00 7.79  ? 106 GLU A OE2 1 
ATOM   850  N  N   . HIS A 1 107 ? 14.018  -6.200  21.443  1.00 6.01  ? 107 HIS A N   1 
ATOM   851  C  CA  . HIS A 1 107 ? 13.543  -6.560  22.781  1.00 5.98  ? 107 HIS A CA  1 
ATOM   852  C  C   . HIS A 1 107 ? 13.288  -8.024  22.820  1.00 6.44  ? 107 HIS A C   1 
ATOM   853  O  O   . HIS A 1 107 ? 12.989  -8.642  21.764  1.00 5.85  ? 107 HIS A O   1 
ATOM   854  C  CB  . HIS A 1 107 ? 12.321  -5.757  23.158  1.00 6.25  ? 107 HIS A CB  1 
ATOM   855  C  CG  . HIS A 1 107 ? 12.639  -4.319  23.289  1.00 6.26  ? 107 HIS A CG  1 
ATOM   856  N  ND1 . HIS A 1 107 ? 12.553  -3.472  22.234  1.00 6.39  ? 107 HIS A ND1 1 
ATOM   857  C  CD2 . HIS A 1 107 ? 13.144  -3.582  24.360  1.00 6.12  ? 107 HIS A CD2 1 
ATOM   858  C  CE1 . HIS A 1 107 ? 13.033  -2.253  22.635  1.00 6.08  ? 107 HIS A CE1 1 
ATOM   859  N  NE2 . HIS A 1 107 ? 13.317  -2.320  23.934  1.00 6.08  ? 107 HIS A NE2 1 
ATOM   860  N  N   . THR A 1 108 ? 13.461  -8.597  23.994  1.00 6.44  ? 108 THR A N   1 
ATOM   861  C  CA  . THR A 1 108 ? 13.053  -10.002 24.217  1.00 6.73  ? 108 THR A CA  1 
ATOM   862  C  C   . THR A 1 108 ? 12.125  -10.038 25.401  1.00 7.06  ? 108 THR A C   1 
ATOM   863  O  O   . THR A 1 108 ? 12.082  -9.050  26.163  1.00 7.32  ? 108 THR A O   1 
ATOM   864  C  CB  . THR A 1 108 ? 14.290  -10.893 24.452  1.00 6.07  ? 108 THR A CB  1 
ATOM   865  O  OG1 . THR A 1 108 ? 15.156  -10.351 25.506  1.00 6.81  ? 108 THR A OG1 1 
ATOM   866  C  CG2 . THR A 1 108 ? 15.140  -11.008 23.179  1.00 6.64  ? 108 THR A CG2 1 
ATOM   867  N  N   . VAL A 1 109 ? 11.342  -11.122 25.518  1.00 7.19  ? 109 VAL A N   1 
ATOM   868  C  CA  . VAL A 1 109 ? 10.346  -11.199 26.635  1.00 7.57  ? 109 VAL A CA  1 
ATOM   869  C  C   . VAL A 1 109 ? 10.688  -12.472 27.369  1.00 8.00  ? 109 VAL A C   1 
ATOM   870  O  O   . VAL A 1 109 ? 10.508  -13.559 26.790  1.00 7.85  ? 109 VAL A O   1 
ATOM   871  C  CB  . VAL A 1 109 ? 8.907   -11.225 26.084  1.00 8.13  ? 109 VAL A CB  1 
ATOM   872  C  CG1 . VAL A 1 109 ? 7.839   -11.360 27.153  1.00 8.31  ? 109 VAL A CG1 1 
ATOM   873  C  CG2 . VAL A 1 109 ? 8.592   -9.926  25.315  1.00 8.02  ? 109 VAL A CG2 1 
ATOM   874  N  N   . ASP A 1 110 ? 11.102  -12.361 28.623  1.00 8.61  ? 110 ASP A N   1 
ATOM   875  C  CA  . ASP A 1 110 ? 11.647  -13.541 29.316  1.00 10.16 ? 110 ASP A CA  1 
ATOM   876  C  C   . ASP A 1 110 ? 12.626  -14.367 28.438  1.00 10.86 ? 110 ASP A C   1 
ATOM   877  O  O   . ASP A 1 110 ? 12.559  -15.645 28.399  1.00 10.68 ? 110 ASP A O   1 
ATOM   878  C  CB  . ASP A 1 110 ? 10.455  -14.404 29.767  1.00 11.56 ? 110 ASP A CB  1 
ATOM   879  C  CG  . ASP A 1 110 ? 9.602   -13.701 30.795  1.00 12.08 ? 110 ASP A CG  1 
ATOM   880  O  OD1 . ASP A 1 110 ? 10.178  -12.841 31.490  1.00 12.40 ? 110 ASP A OD1 1 
ATOM   881  O  OD2 . ASP A 1 110 ? 8.409   -14.065 30.959  1.00 15.04 ? 110 ASP A OD2 1 
ATOM   882  N  N   . LYS A 1 111 ? 13.534  -13.624 27.796  1.00 9.89  ? 111 LYS A N   1 
ATOM   883  C  CA  . LYS A 1 111 ? 14.577  -14.088 26.861  1.00 10.51 ? 111 LYS A CA  1 
ATOM   884  C  C   . LYS A 1 111 ? 14.047  -14.651 25.560  1.00 10.49 ? 111 LYS A C   1 
ATOM   885  O  O   . LYS A 1 111 ? 14.862  -14.986 24.676  1.00 11.81 ? 111 LYS A O   1 
ATOM   886  C  CB  . LYS A 1 111 ? 15.611  -15.042 27.537  1.00 12.48 ? 111 LYS A CB  1 
ATOM   887  C  CG  . LYS A 1 111 ? 16.187  -14.489 28.819  1.00 14.53 ? 111 LYS A CG  1 
ATOM   888  C  CD  . LYS A 1 111 ? 17.229  -13.416 28.534  1.00 15.38 ? 111 LYS A CD  1 
ATOM   889  C  CE  . LYS A 1 111 ? 17.827  -12.850 29.829  1.00 19.01 ? 111 LYS A CE  1 
ATOM   890  N  NZ  . LYS A 1 111 ? 18.931  -13.702 30.327  1.00 22.17 ? 111 LYS A NZ  1 
ATOM   891  N  N   . LYS A 1 112 ? 12.713  -14.674 25.357  1.00 9.68  ? 112 LYS A N   1 
ATOM   892  C  CA  . LYS A 1 112 ? 12.167  -15.103 24.085  1.00 10.45 ? 112 LYS A CA  1 
ATOM   893  C  C   . LYS A 1 112 ? 12.447  -14.060 22.979  1.00 10.64 ? 112 LYS A C   1 
ATOM   894  O  O   . LYS A 1 112 ? 12.107  -12.883 23.173  1.00 9.00  ? 112 LYS A O   1 
ATOM   895  C  CB  . LYS A 1 112 ? 10.638  -15.297 24.194  1.00 11.24 ? 112 LYS A CB  1 
ATOM   896  C  CG  . LYS A 1 112 ? 9.990   -15.710 22.852  1.00 12.90 ? 112 LYS A CG  1 
ATOM   897  C  CD  . LYS A 1 112 ? 8.454   -15.666 23.000  1.00 16.69 ? 112 LYS A CD  1 
ATOM   898  C  CE  . LYS A 1 112 ? 7.712   -15.874 21.660  1.00 18.91 ? 112 LYS A CE  1 
ATOM   899  N  NZ  . LYS A 1 112 ? 8.184   -17.096 20.989  1.00 18.67 ? 112 LYS A NZ  1 
ATOM   900  N  N   . LYS A 1 113 ? 13.026  -14.502 21.842  1.00 9.22  ? 113 LYS A N   1 
ATOM   901  C  CA  . LYS A 1 113 ? 13.155  -13.644 20.658  1.00 10.20 ? 113 LYS A CA  1 
ATOM   902  C  C   . LYS A 1 113 ? 12.017  -13.881 19.697  1.00 9.55  ? 113 LYS A C   1 
ATOM   903  O  O   . LYS A 1 113 ? 11.632  -15.038 19.476  1.00 10.42 ? 113 LYS A O   1 
ATOM   904  C  CB  . LYS A 1 113 ? 14.493  -13.944 19.934  1.00 9.84  ? 113 LYS A CB  1 
ATOM   905  C  CG  . LYS A 1 113 ? 15.705  -13.641 20.796  1.00 11.23 ? 113 LYS A CG  1 
ATOM   906  C  CD  . LYS A 1 113 ? 16.937  -14.206 20.106  1.00 12.64 ? 113 LYS A CD  1 
ATOM   907  C  CE  . LYS A 1 113 ? 18.155  -13.618 20.769  1.00 15.08 ? 113 LYS A CE  1 
ATOM   908  N  NZ  . LYS A 1 113 ? 19.209  -14.617 21.009  1.00 20.79 ? 113 LYS A NZ  1 
ATOM   909  N  N   . TYR A 1 114 ? 11.406  -12.816 19.151  1.00 8.00  ? 114 TYR A N   1 
ATOM   910  C  CA  . TYR A 1 114 ? 10.400  -12.939 18.102  1.00 7.67  ? 114 TYR A CA  1 
ATOM   911  C  C   . TYR A 1 114 ? 11.046  -12.858 16.715  1.00 7.79  ? 114 TYR A C   1 
ATOM   912  O  O   . TYR A 1 114 ? 12.244  -12.560 16.597  1.00 7.65  ? 114 TYR A O   1 
ATOM   913  C  CB  . TYR A 1 114 ? 9.367   -11.811 18.251  1.00 8.08  ? 114 TYR A CB  1 
ATOM   914  C  CG  . TYR A 1 114 ? 8.413   -12.058 19.414  1.00 8.93  ? 114 TYR A CG  1 
ATOM   915  C  CD1 . TYR A 1 114 ? 8.698   -11.598 20.697  1.00 9.42  ? 114 TYR A CD1 1 
ATOM   916  C  CD2 . TYR A 1 114 ? 7.228   -12.741 19.202  1.00 10.00 ? 114 TYR A CD2 1 
ATOM   917  C  CE1 . TYR A 1 114 ? 7.809   -11.806 21.756  1.00 10.08 ? 114 TYR A CE1 1 
ATOM   918  C  CE2 . TYR A 1 114 ? 6.326   -12.955 20.252  1.00 11.58 ? 114 TYR A CE2 1 
ATOM   919  C  CZ  . TYR A 1 114 ? 6.651   -12.501 21.515  1.00 12.63 ? 114 TYR A CZ  1 
ATOM   920  O  OH  . TYR A 1 114 ? 5.719   -12.681 22.524  1.00 16.63 ? 114 TYR A OH  1 
ATOM   921  N  N   . ALA A 1 115 ? 10.252  -13.123 15.669  1.00 7.51  ? 115 ALA A N   1 
ATOM   922  C  CA  . ALA A 1 115 ? 10.806  -13.159 14.313  1.00 7.26  ? 115 ALA A CA  1 
ATOM   923  C  C   . ALA A 1 115 ? 11.207  -11.776 13.829  1.00 7.23  ? 115 ALA A C   1 
ATOM   924  O  O   . ALA A 1 115 ? 12.064  -11.631 12.939  1.00 6.42  ? 115 ALA A O   1 
ATOM   925  C  CB  . ALA A 1 115 ? 9.832   -13.819 13.335  1.00 8.67  ? 115 ALA A CB  1 
ATOM   926  N  N   . ALA A 1 116 ? 10.533  -10.767 14.343  1.00 6.72  ? 116 ALA A N   1 
ATOM   927  C  CA  . ALA A 1 116 ? 10.862  -9.391  13.956  1.00 6.41  ? 116 ALA A CA  1 
ATOM   928  C  C   . ALA A 1 116 ? 10.226  -8.441  14.981  1.00 6.57  ? 116 ALA A C   1 
ATOM   929  O  O   . ALA A 1 116 ? 9.494   -8.880  15.888  1.00 6.88  ? 116 ALA A O   1 
ATOM   930  C  CB  . ALA A 1 116 ? 10.298  -9.042  12.528  1.00 6.31  ? 116 ALA A CB  1 
ATOM   931  N  N   . GLU A 1 117 ? 10.595  -7.189  14.837  1.00 6.51  ? 117 GLU A N   1 
ATOM   932  C  CA  . GLU A 1 117 ? 10.032  -6.098  15.688  1.00 6.35  ? 117 GLU A CA  1 
ATOM   933  C  C   . GLU A 1 117 ? 9.856   -4.866  14.860  1.00 6.93  ? 117 GLU A C   1 
ATOM   934  O  O   . GLU A 1 117 ? 10.783  -4.434  14.156  1.00 7.19  ? 117 GLU A O   1 
ATOM   935  C  CB  . GLU A 1 117 ? 11.022  -5.859  16.862  1.00 6.82  ? 117 GLU A CB  1 
ATOM   936  C  CG  . GLU A 1 117 ? 10.439  -4.932  17.943  1.00 6.30  ? 117 GLU A CG  1 
ATOM   937  C  CD  . GLU A 1 117 ? 11.454  -4.825  19.071  1.00 7.26  ? 117 GLU A CD  1 
ATOM   938  O  OE1 . GLU A 1 117 ? 12.036  -5.868  19.420  1.00 7.49  ? 117 GLU A OE1 1 
ATOM   939  O  OE2 . GLU A 1 117 ? 11.538  -3.759  19.702  1.00 8.98  ? 117 GLU A OE2 1 
ATOM   940  N  N   . LEU A 1 118 ? 8.628   -4.346  14.914  1.00 6.38  ? 118 LEU A N   1 
ATOM   941  C  CA  . LEU A 1 118 ? 8.261   -3.066  14.290  1.00 5.82  ? 118 LEU A CA  1 
ATOM   942  C  C   . LEU A 1 118 ? 8.490   -1.903  15.248  1.00 5.94  ? 118 LEU A C   1 
ATOM   943  O  O   . LEU A 1 118 ? 8.094   -1.986  16.418  1.00 6.17  ? 118 LEU A O   1 
ATOM   944  C  CB  . LEU A 1 118 ? 6.776   -3.127  13.855  1.00 6.28  ? 118 LEU A CB  1 
ATOM   945  C  CG  . LEU A 1 118 ? 6.012   -1.818  13.558  1.00 6.62  ? 118 LEU A CG  1 
ATOM   946  C  CD1 . LEU A 1 118 ? 6.572   -1.243  12.268  1.00 6.99  ? 118 LEU A CD1 1 
ATOM   947  C  CD2 . LEU A 1 118 ? 4.531   -2.204  13.407  1.00 6.87  ? 118 LEU A CD2 1 
ATOM   948  N  N   . HIS A 1 119 ? 9.143   -0.834  14.737  1.00 5.47  ? 119 HIS A N   1 
ATOM   949  C  CA  . HIS A 1 119 ? 9.345   0.375   15.535  1.00 5.38  ? 119 HIS A CA  1 
ATOM   950  C  C   . HIS A 1 119 ? 8.652   1.526   14.886  1.00 5.70  ? 119 HIS A C   1 
ATOM   951  O  O   . HIS A 1 119 ? 8.999   1.889   13.724  1.00 5.97  ? 119 HIS A O   1 
ATOM   952  C  CB  . HIS A 1 119 ? 10.864  0.674   15.645  1.00 5.38  ? 119 HIS A CB  1 
ATOM   953  C  CG  . HIS A 1 119 ? 11.553  -0.321  16.539  1.00 5.19  ? 119 HIS A CG  1 
ATOM   954  N  ND1 . HIS A 1 119 ? 12.931  -0.562  16.523  1.00 5.54  ? 119 HIS A ND1 1 
ATOM   955  C  CD2 . HIS A 1 119 ? 11.010  -1.146  17.498  1.00 5.38  ? 119 HIS A CD2 1 
ATOM   956  C  CE1 . HIS A 1 119 ? 13.205  -1.519  17.463  1.00 5.22  ? 119 HIS A CE1 1 
ATOM   957  N  NE2 . HIS A 1 119 ? 12.050  -1.875  18.067  1.00 5.43  ? 119 HIS A NE2 1 
ATOM   958  N  N   . LEU A 1 120 ? 7.640   2.091   15.578  1.00 6.09  ? 120 LEU A N   1 
ATOM   959  C  CA  . LEU A 1 120 ? 6.952   3.300   15.059  1.00 6.91  ? 120 LEU A CA  1 
ATOM   960  C  C   . LEU A 1 120 ? 7.588   4.482   15.839  1.00 7.11  ? 120 LEU A C   1 
ATOM   961  O  O   . LEU A 1 120 ? 7.460   4.534   17.089  1.00 6.74  ? 120 LEU A O   1 
ATOM   962  C  CB  . LEU A 1 120 ? 5.474   3.242   15.293  1.00 7.43  ? 120 LEU A CB  1 
ATOM   963  C  CG  . LEU A 1 120 ? 4.778   2.194   14.387  1.00 7.63  ? 120 LEU A CG  1 
ATOM   964  C  CD1 . LEU A 1 120 ? 3.888   1.269   15.179  1.00 8.31  ? 120 LEU A CD1 1 
ATOM   965  C  CD2 . LEU A 1 120 ? 3.920   2.932   13.312  1.00 8.24  ? 120 LEU A CD2 1 
ATOM   966  N  N   . VAL A 1 121 ? 8.268   5.369   15.112  1.00 7.10  ? 121 VAL A N   1 
ATOM   967  C  CA  . VAL A 1 121 ? 9.141   6.365   15.770  1.00 7.45  ? 121 VAL A CA  1 
ATOM   968  C  C   . VAL A 1 121 ? 8.425   7.722   15.835  1.00 7.81  ? 121 VAL A C   1 
ATOM   969  O  O   . VAL A 1 121 ? 7.889   8.141   14.818  1.00 7.88  ? 121 VAL A O   1 
ATOM   970  C  CB  . VAL A 1 121 ? 10.493  6.494   14.983  1.00 7.72  ? 121 VAL A CB  1 
ATOM   971  C  CG1 . VAL A 1 121 ? 11.460  7.506   15.596  1.00 7.60  ? 121 VAL A CG1 1 
ATOM   972  C  CG2 . VAL A 1 121 ? 11.175  5.122   14.880  1.00 7.34  ? 121 VAL A CG2 1 
ATOM   973  N  N   . HIS A 1 122 ? 8.400   8.343   17.020  1.00 7.76  ? 122 HIS A N   1 
ATOM   974  C  CA  . HIS A 1 122 ? 7.682   9.622   17.154  1.00 8.40  ? 122 HIS A CA  1 
ATOM   975  C  C   . HIS A 1 122 ? 8.547   10.609  17.882  1.00 8.71  ? 122 HIS A C   1 
ATOM   976  O  O   . HIS A 1 122 ? 9.318   10.264  18.792  1.00 8.12  ? 122 HIS A O   1 
ATOM   977  C  CB  . HIS A 1 122 ? 6.397   9.448   18.007  1.00 8.57  ? 122 HIS A CB  1 
ATOM   978  C  CG  . HIS A 1 122 ? 5.521   8.278   17.618  1.00 9.25  ? 122 HIS A CG  1 
ATOM   979  N  ND1 . HIS A 1 122 ? 5.855   7.001   17.875  1.00 8.72  ? 122 HIS A ND1 1 
ATOM   980  C  CD2 . HIS A 1 122 ? 4.255   8.242   17.033  1.00 8.59  ? 122 HIS A CD2 1 
ATOM   981  C  CE1 . HIS A 1 122 ? 4.869   6.186   17.452  1.00 9.01  ? 122 HIS A CE1 1 
ATOM   982  N  NE2 . HIS A 1 122 ? 3.891   6.947   16.937  1.00 8.14  ? 122 HIS A NE2 1 
ATOM   983  N  N   . TRP A 1 123 ? 8.486   11.889  17.491  1.00 8.25  ? 123 TRP A N   1 
ATOM   984  C  CA  . TRP A 1 123 ? 9.300   12.883  18.181  1.00 9.44  ? 123 TRP A CA  1 
ATOM   985  C  C   . TRP A 1 123 ? 8.477   13.898  18.928  1.00 9.31  ? 123 TRP A C   1 
ATOM   986  O  O   . TRP A 1 123 ? 7.360   14.242  18.537  1.00 8.91  ? 123 TRP A O   1 
ATOM   987  C  CB  . TRP A 1 123 ? 10.280  13.567  17.188  1.00 9.73  ? 123 TRP A CB  1 
ATOM   988  C  CG  . TRP A 1 123 ? 9.632   14.273  16.057  1.00 11.33 ? 123 TRP A CG  1 
ATOM   989  C  CD1 . TRP A 1 123 ? 9.214   13.749  14.829  1.00 11.82 ? 123 TRP A CD1 1 
ATOM   990  C  CD2 . TRP A 1 123 ? 9.319   15.699  15.991  1.00 11.52 ? 123 TRP A CD2 1 
ATOM   991  N  NE1 . TRP A 1 123 ? 8.663   14.737  14.028  1.00 13.07 ? 123 TRP A NE1 1 
ATOM   992  C  CE2 . TRP A 1 123 ? 8.713   15.936  14.696  1.00 12.46 ? 123 TRP A CE2 1 
ATOM   993  C  CE3 . TRP A 1 123 ? 9.479   16.763  16.875  1.00 12.93 ? 123 TRP A CE3 1 
ATOM   994  C  CZ2 . TRP A 1 123 ? 8.259   17.207  14.306  1.00 12.94 ? 123 TRP A CZ2 1 
ATOM   995  C  CZ3 . TRP A 1 123 ? 9.051   18.043  16.449  1.00 13.05 ? 123 TRP A CZ3 1 
ATOM   996  C  CH2 . TRP A 1 123 ? 8.452   18.243  15.229  1.00 13.65 ? 123 TRP A CH2 1 
ATOM   997  N  N   . ASN A 1 124 ? 9.028   14.342  20.043  1.00 9.41  ? 124 ASN A N   1 
ATOM   998  C  CA  . ASN A 1 124 ? 8.371   15.264  21.010  1.00 10.07 ? 124 ASN A CA  1 
ATOM   999  C  C   . ASN A 1 124 ? 8.240   16.683  20.405  1.00 9.61  ? 124 ASN A C   1 
ATOM   1000 O  O   . ASN A 1 124 ? 9.273   17.356  20.176  1.00 8.36  ? 124 ASN A O   1 
ATOM   1001 C  CB  . ASN A 1 124 ? 9.213   15.286  22.320  1.00 10.15 ? 124 ASN A CB  1 
ATOM   1002 C  CG  . ASN A 1 124 ? 8.482   15.971  23.460  1.00 11.76 ? 124 ASN A CG  1 
ATOM   1003 O  OD1 . ASN A 1 124 ? 7.596   16.831  23.204  1.00 9.84  ? 124 ASN A OD1 1 
ATOM   1004 N  ND2 . ASN A 1 124 ? 8.738   15.528  24.712  1.00 12.40 ? 124 ASN A ND2 1 
ATOM   1005 N  N   . THR A 1 125 ? 6.982   17.135  20.143  1.00 10.57 ? 125 THR A N   1 
ATOM   1006 C  CA  . THR A 1 125 ? 6.836   18.349  19.311  1.00 11.84 ? 125 THR A CA  1 
ATOM   1007 C  C   . THR A 1 125 ? 7.282   19.592  20.092  1.00 13.58 ? 125 THR A C   1 
ATOM   1008 O  O   . THR A 1 125 ? 7.464   20.653  19.498  1.00 13.08 ? 125 THR A O   1 
ATOM   1009 C  CB  . THR A 1 125 ? 5.427   18.520  18.791  1.00 12.87 ? 125 THR A CB  1 
ATOM   1010 O  OG1 . THR A 1 125 ? 4.537   18.530  19.905  1.00 15.92 ? 125 THR A OG1 1 
ATOM   1011 C  CG2 . THR A 1 125 ? 5.090   17.338  17.805  1.00 15.55 ? 125 THR A CG2 1 
ATOM   1012 N  N   . LYS A 1 126 ? 7.472   19.419  21.524  1.00 11.06 ? 127 LYS A N   1 
ATOM   1013 C  CA  . LYS A 1 126 ? 7.968   20.659  22.128  1.00 12.97 ? 127 LYS A CA  1 
ATOM   1014 C  C   . LYS A 1 126 ? 9.372   21.058  21.759  1.00 13.15 ? 127 LYS A C   1 
ATOM   1015 O  O   . LYS A 1 126 ? 9.796   22.195  22.075  1.00 12.81 ? 127 LYS A O   1 
ATOM   1016 C  CB  . LYS A 1 126 ? 7.803   20.595  23.593  1.00 14.17 ? 127 LYS A CB  1 
ATOM   1017 C  CG  . LYS A 1 126 ? 8.914   19.887  24.287  1.00 15.89 ? 127 LYS A CG  1 
ATOM   1018 C  CD  . LYS A 1 126 ? 8.387   19.500  25.649  1.00 19.65 ? 127 LYS A CD  1 
ATOM   1019 C  CE  . LYS A 1 126 ? 9.485   18.719  26.282  1.00 20.67 ? 127 LYS A CE  1 
ATOM   1020 N  NZ  . LYS A 1 126 ? 9.182   18.693  27.729  1.00 27.60 ? 127 LYS A NZ  1 
ATOM   1021 N  N   . TYR A 1 127 ? 10.098  20.181  21.066  1.00 10.52 ? 128 TYR A N   1 
ATOM   1022 C  CA  . TYR A 1 127 ? 11.481  20.448  20.609  1.00 10.06 ? 128 TYR A CA  1 
ATOM   1023 C  C   . TYR A 1 127 ? 11.560  20.939  19.172  1.00 11.23 ? 128 TYR A C   1 
ATOM   1024 O  O   . TYR A 1 127 ? 12.676  21.251  18.653  1.00 13.13 ? 128 TYR A O   1 
ATOM   1025 C  CB  . TYR A 1 127 ? 12.418  19.241  20.840  1.00 10.30 ? 128 TYR A CB  1 
ATOM   1026 C  CG  . TYR A 1 127 ? 12.500  18.914  22.302  1.00 10.03 ? 128 TYR A CG  1 
ATOM   1027 C  CD1 . TYR A 1 127 ? 12.898  19.889  23.248  1.00 11.96 ? 128 TYR A CD1 1 
ATOM   1028 C  CD2 . TYR A 1 127 ? 12.205  17.640  22.769  1.00 10.33 ? 128 TYR A CD2 1 
ATOM   1029 C  CE1 . TYR A 1 127 ? 12.939  19.582  24.635  1.00 10.90 ? 128 TYR A CE1 1 
ATOM   1030 C  CE2 . TYR A 1 127 ? 12.230  17.348  24.110  1.00 11.06 ? 128 TYR A CE2 1 
ATOM   1031 C  CZ  . TYR A 1 127 ? 12.652  18.302  25.039  1.00 11.10 ? 128 TYR A CZ  1 
ATOM   1032 O  OH  . TYR A 1 127 ? 12.702  17.969  26.413  1.00 10.53 ? 128 TYR A OH  1 
ATOM   1033 N  N   . GLY A 1 128 ? 10.377  21.061  18.554  1.00 10.19 ? 129 GLY A N   1 
ATOM   1034 C  CA  . GLY A 1 128 ? 10.247  21.780  17.273  1.00 10.60 ? 129 GLY A CA  1 
ATOM   1035 C  C   . GLY A 1 128 ? 10.684  21.009  16.028  1.00 11.22 ? 129 GLY A C   1 
ATOM   1036 O  O   . GLY A 1 128 ? 10.028  21.169  14.974  1.00 12.39 ? 129 GLY A O   1 
ATOM   1037 N  N   . ASP A 1 129 ? 11.783  20.224  16.105  1.00 11.81 ? 130 ASP A N   1 
ATOM   1038 C  CA  . ASP A 1 129 ? 12.158  19.312  15.003  1.00 12.78 ? 130 ASP A CA  1 
ATOM   1039 C  C   . ASP A 1 129 ? 12.823  18.085  15.557  1.00 12.92 ? 130 ASP A C   1 
ATOM   1040 O  O   . ASP A 1 129 ? 13.290  18.023  16.717  1.00 10.93 ? 130 ASP A O   1 
ATOM   1041 C  CB  . ASP A 1 129 ? 13.019  19.988  13.877  1.00 13.82 ? 130 ASP A CB  1 
ATOM   1042 C  CG  . ASP A 1 129 ? 14.436  20.422  14.321  1.00 18.58 ? 130 ASP A CG  1 
ATOM   1043 O  OD1 . ASP A 1 129 ? 15.334  19.617  14.654  1.00 17.99 ? 130 ASP A OD1 1 
ATOM   1044 O  OD2 . ASP A 1 129 ? 14.756  21.624  14.337  1.00 21.97 ? 130 ASP A OD2 1 
ATOM   1045 N  N   . PHE A 1 130 ? 12.869  17.051  14.737  1.00 12.23 ? 131 PHE A N   1 
ATOM   1046 C  CA  . PHE A 1 130 ? 13.387  15.833  15.306  1.00 13.08 ? 131 PHE A CA  1 
ATOM   1047 C  C   . PHE A 1 130 ? 14.888  15.870  15.569  1.00 12.67 ? 131 PHE A C   1 
ATOM   1048 O  O   . PHE A 1 130 ? 15.388  15.194  16.483  1.00 10.73 ? 131 PHE A O   1 
ATOM   1049 C  CB  . PHE A 1 130 ? 13.031  14.642  14.424  1.00 14.18 ? 131 PHE A CB  1 
ATOM   1050 C  CG  . PHE A 1 130 ? 13.741  14.624  13.091  1.00 19.56 ? 131 PHE A CG  1 
ATOM   1051 C  CD1 . PHE A 1 130 ? 15.094  14.316  12.989  1.00 20.96 ? 131 PHE A CD1 1 
ATOM   1052 C  CD2 . PHE A 1 130 ? 13.019  14.855  11.904  1.00 22.28 ? 131 PHE A CD2 1 
ATOM   1053 C  CE1 . PHE A 1 130 ? 15.714  14.285  11.721  1.00 25.09 ? 131 PHE A CE1 1 
ATOM   1054 C  CE2 . PHE A 1 130 ? 13.646  14.831  10.659  1.00 22.29 ? 131 PHE A CE2 1 
ATOM   1055 C  CZ  . PHE A 1 130 ? 14.976  14.540  10.589  1.00 23.83 ? 131 PHE A CZ  1 
ATOM   1056 N  N   . GLY A 1 131 ? 15.638  16.660  14.779  1.00 12.02 ? 132 GLY A N   1 
ATOM   1057 C  CA  . GLY A 1 131 ? 17.058  16.782  15.090  1.00 11.97 ? 132 GLY A CA  1 
ATOM   1058 C  C   . GLY A 1 131 ? 17.323  17.395  16.478  1.00 12.21 ? 132 GLY A C   1 
ATOM   1059 O  O   . GLY A 1 131 ? 18.286  17.016  17.133  1.00 13.31 ? 132 GLY A O   1 
ATOM   1060 N  N   A LYS A 1 132 ? 16.481  18.333  16.901  0.50 11.31 ? 133 LYS A N   1 
ATOM   1061 N  N   B LYS A 1 132 ? 16.503  18.346  16.934  0.50 11.86 ? 133 LYS A N   1 
ATOM   1062 C  CA  A LYS A 1 132 ? 16.581  18.897  18.254  0.50 10.53 ? 133 LYS A CA  1 
ATOM   1063 C  CA  B LYS A 1 132 ? 16.662  18.851  18.322  0.50 11.30 ? 133 LYS A CA  1 
ATOM   1064 C  C   A LYS A 1 132 ? 16.121  17.878  19.316  0.50 10.63 ? 133 LYS A C   1 
ATOM   1065 C  C   B LYS A 1 132 ? 16.159  17.815  19.332  0.50 11.07 ? 133 LYS A C   1 
ATOM   1066 O  O   A LYS A 1 132 ? 16.707  17.775  20.395  0.50 9.83  ? 133 LYS A O   1 
ATOM   1067 O  O   B LYS A 1 132 ? 16.723  17.671  20.414  0.50 10.15 ? 133 LYS A O   1 
ATOM   1068 C  CB  A LYS A 1 132 ? 15.727  20.164  18.327  0.50 10.68 ? 133 LYS A CB  1 
ATOM   1069 C  CB  B LYS A 1 132 ? 15.869  20.136  18.560  0.50 12.52 ? 133 LYS A CB  1 
ATOM   1070 C  CG  A LYS A 1 132 ? 16.411  21.371  17.681  0.50 10.51 ? 133 LYS A CG  1 
ATOM   1071 C  CG  B LYS A 1 132 ? 15.955  20.650  20.004  0.50 13.17 ? 133 LYS A CG  1 
ATOM   1072 C  CD  A LYS A 1 132 ? 17.805  21.620  18.288  0.50 10.94 ? 133 LYS A CD  1 
ATOM   1073 C  CD  B LYS A 1 132 ? 17.294  21.309  20.345  0.50 14.76 ? 133 LYS A CD  1 
ATOM   1074 C  CE  A LYS A 1 132 ? 17.849  22.924  19.078  0.50 11.88 ? 133 LYS A CE  1 
ATOM   1075 C  CE  B LYS A 1 132 ? 18.159  20.358  21.175  0.50 16.77 ? 133 LYS A CE  1 
ATOM   1076 N  NZ  A LYS A 1 132 ? 16.914  23.926  18.467  0.50 11.06 ? 133 LYS A NZ  1 
ATOM   1077 N  NZ  B LYS A 1 132 ? 19.636  20.683  21.231  0.50 20.37 ? 133 LYS A NZ  1 
ATOM   1078 N  N   . ALA A 1 133 ? 15.063  17.142  18.986  1.00 9.24  ? 134 ALA A N   1 
ATOM   1079 C  CA  . ALA A 1 133 ? 14.455  16.159  19.921  1.00 9.70  ? 134 ALA A CA  1 
ATOM   1080 C  C   . ALA A 1 133 ? 15.455  15.061  20.304  1.00 8.84  ? 134 ALA A C   1 
ATOM   1081 O  O   . ALA A 1 133 ? 15.512  14.714  21.452  1.00 8.18  ? 134 ALA A O   1 
ATOM   1082 C  CB  . ALA A 1 133 ? 13.211  15.562  19.281  1.00 8.84  ? 134 ALA A CB  1 
ATOM   1083 N  N   . VAL A 1 134 ? 16.261  14.560  19.360  1.00 9.45  ? 135 VAL A N   1 
ATOM   1084 C  CA  . VAL A 1 134 ? 17.225  13.461  19.670  1.00 10.57 ? 135 VAL A CA  1 
ATOM   1085 C  C   . VAL A 1 134 ? 18.326  13.868  20.638  1.00 10.26 ? 135 VAL A C   1 
ATOM   1086 O  O   . VAL A 1 134 ? 18.967  13.005  21.204  1.00 10.78 ? 135 VAL A O   1 
ATOM   1087 C  CB  . VAL A 1 134 ? 17.840  12.759  18.420  1.00 10.92 ? 135 VAL A CB  1 
ATOM   1088 C  CG1 . VAL A 1 134 ? 16.716  12.175  17.570  1.00 11.42 ? 135 VAL A CG1 1 
ATOM   1089 C  CG2 . VAL A 1 134 ? 18.699  13.691  17.577  1.00 11.53 ? 135 VAL A CG2 1 
ATOM   1090 N  N   . GLN A 1 135 ? 18.532  15.187  20.818  1.00 10.11 ? 136 GLN A N   1 
ATOM   1091 C  CA  . GLN A 1 135 ? 19.479  15.668  21.813  1.00 11.74 ? 136 GLN A CA  1 
ATOM   1092 C  C   . GLN A 1 135 ? 18.883  15.707  23.217  1.00 11.01 ? 136 GLN A C   1 
ATOM   1093 O  O   . GLN A 1 135 ? 19.518  16.224  24.137  1.00 12.18 ? 136 GLN A O   1 
ATOM   1094 C  CB  . GLN A 1 135 ? 19.900  17.110  21.400  1.00 12.99 ? 136 GLN A CB  1 
ATOM   1095 C  CG  . GLN A 1 135 ? 20.522  17.037  20.015  1.00 16.19 ? 136 GLN A CG  1 
ATOM   1096 C  CD  . GLN A 1 135 ? 21.023  18.360  19.476  1.00 22.64 ? 136 GLN A CD  1 
ATOM   1097 O  OE1 . GLN A 1 135 ? 21.833  19.028  20.111  1.00 27.94 ? 136 GLN A OE1 1 
ATOM   1098 N  NE2 . GLN A 1 135 ? 20.513  18.757  18.295  1.00 22.57 ? 136 GLN A NE2 1 
ATOM   1099 N  N   . GLN A 1 136 ? 17.660  15.232  23.372  1.00 10.81 ? 137 GLN A N   1 
ATOM   1100 C  CA  . GLN A 1 136 ? 16.963  15.432  24.696  1.00 10.78 ? 137 GLN A CA  1 
ATOM   1101 C  C   . GLN A 1 136 ? 16.590  14.072  25.253  1.00 10.81 ? 137 GLN A C   1 
ATOM   1102 O  O   . GLN A 1 136 ? 16.251  13.133  24.481  1.00 9.69  ? 137 GLN A O   1 
ATOM   1103 C  CB  . GLN A 1 136 ? 15.642  16.182  24.548  1.00 10.51 ? 137 GLN A CB  1 
ATOM   1104 C  CG  . GLN A 1 136 ? 15.688  17.501  23.741  1.00 12.24 ? 137 GLN A CG  1 
ATOM   1105 C  CD  . GLN A 1 136 ? 16.769  18.468  24.147  1.00 14.92 ? 137 GLN A CD  1 
ATOM   1106 O  OE1 . GLN A 1 136 ? 17.025  18.681  25.347  1.00 15.08 ? 137 GLN A OE1 1 
ATOM   1107 N  NE2 . GLN A 1 136 ? 17.406  19.097  23.128  1.00 15.85 ? 137 GLN A NE2 1 
ATOM   1108 N  N   . PRO A 1 137 ? 16.598  13.955  26.608  1.00 11.04 ? 138 PRO A N   1 
ATOM   1109 C  CA  . PRO A 1 137 ? 16.338  12.651  27.215  1.00 10.47 ? 138 PRO A CA  1 
ATOM   1110 C  C   . PRO A 1 137 ? 14.906  12.185  26.951  1.00 10.88 ? 138 PRO A C   1 
ATOM   1111 O  O   . PRO A 1 137 ? 14.668  10.974  26.960  1.00 10.76 ? 138 PRO A O   1 
ATOM   1112 C  CB  . PRO A 1 137 ? 16.617  12.869  28.735  1.00 11.99 ? 138 PRO A CB  1 
ATOM   1113 C  CG  . PRO A 1 137 ? 16.614  14.346  28.896  1.00 14.15 ? 138 PRO A CG  1 
ATOM   1114 C  CD  . PRO A 1 137 ? 17.102  14.935  27.587  1.00 11.97 ? 138 PRO A CD  1 
ATOM   1115 N  N   . ASP A 1 138 ? 13.971  13.118  26.687  1.00 9.99  ? 139 ASP A N   1 
ATOM   1116 C  CA  . ASP A 1 138 ? 12.565  12.755  26.370  1.00 9.88  ? 139 ASP A CA  1 
ATOM   1117 C  C   . ASP A 1 138 ? 12.216  13.160  24.970  1.00 8.37  ? 139 ASP A C   1 
ATOM   1118 O  O   . ASP A 1 138 ? 11.090  13.545  24.687  1.00 8.05  ? 139 ASP A O   1 
ATOM   1119 C  CB  . ASP A 1 138 ? 11.618  13.381  27.416  1.00 11.40 ? 139 ASP A CB  1 
ATOM   1120 C  CG  . ASP A 1 138 ? 11.734  14.898  27.491  1.00 11.77 ? 139 ASP A CG  1 
ATOM   1121 O  OD1 . ASP A 1 138 ? 12.654  15.492  26.851  1.00 11.48 ? 139 ASP A OD1 1 
ATOM   1122 O  OD2 . ASP A 1 138 ? 10.830  15.499  28.168  1.00 13.14 ? 139 ASP A OD2 1 
ATOM   1123 N  N   . GLY A 1 139 ? 13.180  13.072  24.040  1.00 7.66  ? 140 GLY A N   1 
ATOM   1124 C  CA  . GLY A 1 139 ? 12.921  13.602  22.739  1.00 6.89  ? 140 GLY A CA  1 
ATOM   1125 C  C   . GLY A 1 139 ? 12.089  12.686  21.852  1.00 7.25  ? 140 GLY A C   1 
ATOM   1126 O  O   . GLY A 1 139 ? 11.423  13.208  20.930  1.00 7.13  ? 140 GLY A O   1 
ATOM   1127 N  N   . LEU A 1 140 ? 12.201  11.342  22.038  1.00 6.73  ? 141 LEU A N   1 
ATOM   1128 C  CA  . LEU A 1 140 ? 11.512  10.425  21.135  1.00 6.60  ? 141 LEU A CA  1 
ATOM   1129 C  C   . LEU A 1 140 ? 10.655  9.444   21.953  1.00 6.75  ? 141 LEU A C   1 
ATOM   1130 O  O   . LEU A 1 140 ? 10.933  9.148   23.125  1.00 6.78  ? 141 LEU A O   1 
ATOM   1131 C  CB  . LEU A 1 140 ? 12.546  9.588   20.348  1.00 8.12  ? 141 LEU A CB  1 
ATOM   1132 C  CG  . LEU A 1 140 ? 13.438  10.286  19.312  1.00 8.99  ? 141 LEU A CG  1 
ATOM   1133 C  CD1 . LEU A 1 140 ? 14.204  9.229   18.482  1.00 9.27  ? 141 LEU A CD1 1 
ATOM   1134 C  CD2 . LEU A 1 140 ? 12.764  11.223  18.327  1.00 9.02  ? 141 LEU A CD2 1 
ATOM   1135 N  N   . ALA A 1 141 ? 9.627   8.934   21.289  1.00 6.74  ? 142 ALA A N   1 
ATOM   1136 C  CA  . ALA A 1 141 ? 8.814   7.799   21.853  1.00 6.60  ? 142 ALA A CA  1 
ATOM   1137 C  C   . ALA A 1 141 ? 8.742   6.779   20.731  1.00 6.78  ? 142 ALA A C   1 
ATOM   1138 O  O   . ALA A 1 141 ? 8.413   7.117   19.575  1.00 6.90  ? 142 ALA A O   1 
ATOM   1139 C  CB  . ALA A 1 141 ? 7.449   8.250   22.317  1.00 6.62  ? 142 ALA A CB  1 
ATOM   1140 N  N   . VAL A 1 142 ? 9.239   5.576   21.013  1.00 6.06  ? 143 VAL A N   1 
ATOM   1141 C  CA  . VAL A 1 142 ? 9.206   4.506   19.973  1.00 6.47  ? 143 VAL A CA  1 
ATOM   1142 C  C   . VAL A 1 142 ? 8.225   3.438   20.443  1.00 6.49  ? 143 VAL A C   1 
ATOM   1143 O  O   . VAL A 1 142 ? 8.367   2.894   21.589  1.00 6.77  ? 143 VAL A O   1 
ATOM   1144 C  CB  . VAL A 1 142 ? 10.602  3.918   19.647  1.00 6.34  ? 143 VAL A CB  1 
ATOM   1145 C  CG1 . VAL A 1 142 ? 10.451  2.948   18.454  1.00 6.43  ? 143 VAL A CG1 1 
ATOM   1146 C  CG2 . VAL A 1 142 ? 11.492  5.055   19.189  1.00 6.84  ? 143 VAL A CG2 1 
ATOM   1147 N  N   . LEU A 1 143 ? 7.223   3.122   19.611  1.00 6.21  ? 144 LEU A N   1 
ATOM   1148 C  CA  . LEU A 1 143 ? 6.244   2.144   19.937  1.00 6.42  ? 144 LEU A CA  1 
ATOM   1149 C  C   . LEU A 1 143 ? 6.781   0.848   19.273  1.00 6.86  ? 144 LEU A C   1 
ATOM   1150 O  O   . LEU A 1 143 ? 6.954   0.823   18.036  1.00 7.58  ? 144 LEU A O   1 
ATOM   1151 C  CB  . LEU A 1 143 ? 4.852   2.617   19.342  1.00 7.56  ? 144 LEU A CB  1 
ATOM   1152 C  CG  . LEU A 1 143 ? 3.683   1.675   19.519  1.00 8.07  ? 144 LEU A CG  1 
ATOM   1153 C  CD1 . LEU A 1 143 ? 3.553   1.423   21.011  1.00 9.65  ? 144 LEU A CD1 1 
ATOM   1154 C  CD2 . LEU A 1 143 ? 2.422   2.318   18.869  1.00 7.56  ? 144 LEU A CD2 1 
ATOM   1155 N  N   . GLY A 1 144 ? 7.050   -0.216  20.084  1.00 5.86  ? 145 GLY A N   1 
ATOM   1156 C  CA  . GLY A 1 144 ? 7.687   -1.387  19.510  1.00 6.22  ? 145 GLY A CA  1 
ATOM   1157 C  C   . GLY A 1 144 ? 6.572   -2.454  19.483  1.00 5.98  ? 145 GLY A C   1 
ATOM   1158 O  O   . GLY A 1 144 ? 5.814   -2.586  20.482  1.00 6.23  ? 145 GLY A O   1 
ATOM   1159 N  N   . ILE A 1 145 ? 6.538   -3.253  18.439  1.00 5.94  ? 146 ILE A N   1 
ATOM   1160 C  CA  . ILE A 1 145 ? 5.480   -4.292  18.289  1.00 6.53  ? 146 ILE A CA  1 
ATOM   1161 C  C   . ILE A 1 145 ? 6.172   -5.541  17.766  1.00 6.79  ? 146 ILE A C   1 
ATOM   1162 O  O   . ILE A 1 145 ? 6.898   -5.510  16.788  1.00 7.65  ? 146 ILE A O   1 
ATOM   1163 C  CB  . ILE A 1 145 ? 4.404   -3.833  17.282  1.00 7.08  ? 146 ILE A CB  1 
ATOM   1164 C  CG1 . ILE A 1 145 ? 3.698   -2.539  17.826  1.00 7.40  ? 146 ILE A CG1 1 
ATOM   1165 C  CG2 . ILE A 1 145 ? 3.375   -4.949  16.984  1.00 8.09  ? 146 ILE A CG2 1 
ATOM   1166 C  CD1 . ILE A 1 145 ? 2.576   -2.052  16.899  1.00 8.42  ? 146 ILE A CD1 1 
ATOM   1167 N  N   . PHE A 1 146 ? 5.977   -6.638  18.464  1.00 7.54  ? 147 PHE A N   1 
ATOM   1168 C  CA  . PHE A 1 146 ? 6.640   -7.893  18.047  1.00 6.52  ? 147 PHE A CA  1 
ATOM   1169 C  C   . PHE A 1 146 ? 5.885   -8.568  16.923  1.00 7.10  ? 147 PHE A C   1 
ATOM   1170 O  O   . PHE A 1 146 ? 4.670   -8.465  16.887  1.00 7.10  ? 147 PHE A O   1 
ATOM   1171 C  CB  . PHE A 1 146 ? 6.684   -8.876  19.219  1.00 6.58  ? 147 PHE A CB  1 
ATOM   1172 C  CG  . PHE A 1 146 ? 7.529   -8.397  20.372  1.00 5.91  ? 147 PHE A CG  1 
ATOM   1173 C  CD1 . PHE A 1 146 ? 8.913   -8.213  20.194  1.00 6.10  ? 147 PHE A CD1 1 
ATOM   1174 C  CD2 . PHE A 1 146 ? 6.965   -8.148  21.624  1.00 6.11  ? 147 PHE A CD2 1 
ATOM   1175 C  CE1 . PHE A 1 146 ? 9.747   -7.832  21.278  1.00 6.22  ? 147 PHE A CE1 1 
ATOM   1176 C  CE2 . PHE A 1 146 ? 7.757   -7.737  22.702  1.00 6.26  ? 147 PHE A CE2 1 
ATOM   1177 C  CZ  . PHE A 1 146 ? 9.147   -7.597  22.545  1.00 6.37  ? 147 PHE A CZ  1 
ATOM   1178 N  N   . LEU A 1 147 ? 6.629   -9.223  16.025  1.00 6.73  ? 148 LEU A N   1 
ATOM   1179 C  CA  . LEU A 1 147 ? 6.028   -10.049 14.966  1.00 6.84  ? 148 LEU A CA  1 
ATOM   1180 C  C   . LEU A 1 147 ? 6.347   -11.498 15.182  1.00 7.85  ? 148 LEU A C   1 
ATOM   1181 O  O   . LEU A 1 147 ? 7.515   -11.858 15.413  1.00 7.07  ? 148 LEU A O   1 
ATOM   1182 C  CB  . LEU A 1 147 ? 6.578   -9.618  13.578  1.00 7.32  ? 148 LEU A CB  1 
ATOM   1183 C  CG  . LEU A 1 147 ? 5.950   -8.376  12.884  1.00 7.82  ? 148 LEU A CG  1 
ATOM   1184 C  CD1 . LEU A 1 147 ? 6.262   -7.128  13.729  1.00 8.29  ? 148 LEU A CD1 1 
ATOM   1185 C  CD2 . LEU A 1 147 ? 6.592   -8.148  11.505  1.00 7.52  ? 148 LEU A CD2 1 
ATOM   1186 N  N   . LYS A 1 148 ? 5.312   -12.341 15.133  1.00 8.79  ? 149 LYS A N   1 
ATOM   1187 C  CA  . LYS A 1 148 ? 5.559   -13.769 15.083  1.00 10.48 ? 149 LYS A CA  1 
ATOM   1188 C  C   . LYS A 1 148 ? 5.021   -14.299 13.757  1.00 11.77 ? 149 LYS A C   1 
ATOM   1189 O  O   . LYS A 1 148 ? 4.208   -13.674 13.106  1.00 11.40 ? 149 LYS A O   1 
ATOM   1190 C  CB  . LYS A 1 148 ? 4.841   -14.507 16.227  1.00 12.25 ? 149 LYS A CB  1 
ATOM   1191 C  CG  . LYS A 1 148 ? 3.351   -14.328 16.220  1.00 15.34 ? 149 LYS A CG  1 
ATOM   1192 C  CD  . LYS A 1 148 ? 2.732   -15.007 17.426  1.00 19.70 ? 149 LYS A CD  1 
ATOM   1193 C  CE  . LYS A 1 148 ? 1.238   -14.934 17.294  1.00 22.58 ? 149 LYS A CE  1 
ATOM   1194 N  NZ  . LYS A 1 148 ? 0.541   -15.600 18.458  1.00 25.65 ? 149 LYS A NZ  1 
ATOM   1195 N  N   . VAL A 1 149 ? 5.460   -15.498 13.405  1.00 12.22 ? 150 VAL A N   1 
ATOM   1196 C  CA  . VAL A 1 149 ? 5.106   -16.035 12.093  1.00 11.84 ? 150 VAL A CA  1 
ATOM   1197 C  C   . VAL A 1 149 ? 3.859   -16.935 12.285  1.00 12.52 ? 150 VAL A C   1 
ATOM   1198 O  O   . VAL A 1 149 ? 3.813   -17.808 13.186  1.00 12.73 ? 150 VAL A O   1 
ATOM   1199 C  CB  . VAL A 1 149 ? 6.328   -16.794 11.528  1.00 13.71 ? 150 VAL A CB  1 
ATOM   1200 C  CG1 . VAL A 1 149 ? 5.942   -17.576 10.264  1.00 13.74 ? 150 VAL A CG1 1 
ATOM   1201 C  CG2 . VAL A 1 149 ? 7.474   -15.831 11.169  1.00 12.37 ? 150 VAL A CG2 1 
ATOM   1202 N  N   . GLY A 1 150 ? 2.834   -16.729 11.491  1.00 11.13 ? 151 GLY A N   1 
ATOM   1203 C  CA  . GLY A 1 150 ? 1.624   -17.597 11.613  1.00 13.12 ? 151 GLY A CA  1 
ATOM   1204 C  C   . GLY A 1 150 ? 0.724   -17.126 10.486  1.00 11.98 ? 151 GLY A C   1 
ATOM   1205 O  O   . GLY A 1 150 ? 1.098   -17.232 9.338   1.00 13.25 ? 151 GLY A O   1 
ATOM   1206 N  N   A SER A 1 151 ? -0.443  -16.575 10.816  0.50 12.78 ? 152 SER A N   1 
ATOM   1207 N  N   B SER A 1 151 ? -0.423  -16.572 10.827  0.50 12.39 ? 152 SER A N   1 
ATOM   1208 C  CA  A SER A 1 151 ? -1.350  -16.033 9.773   0.50 13.75 ? 152 SER A CA  1 
ATOM   1209 C  CA  B SER A 1 151 ? -1.312  -16.015 9.812   0.50 13.13 ? 152 SER A CA  1 
ATOM   1210 C  C   A SER A 1 151 ? -0.846  -14.689 9.235   0.50 13.36 ? 152 SER A C   1 
ATOM   1211 C  C   B SER A 1 151 ? -0.690  -14.754 9.191   0.50 12.89 ? 152 SER A C   1 
ATOM   1212 O  O   A SER A 1 151 ? -0.251  -13.905 9.979   0.50 12.35 ? 152 SER A O   1 
ATOM   1213 O  O   B SER A 1 151 ? 0.150   -14.103 9.834   0.50 11.40 ? 152 SER A O   1 
ATOM   1214 C  CB  A SER A 1 151 ? -2.786  -15.892 10.282  0.50 15.26 ? 152 SER A CB  1 
ATOM   1215 C  CB  B SER A 1 151 ? -2.643  -15.707 10.462  0.50 14.03 ? 152 SER A CB  1 
ATOM   1216 O  OG  A SER A 1 151 ? -2.923  -14.863 11.255  0.50 15.26 ? 152 SER A OG  1 
ATOM   1217 O  OG  B SER A 1 151 ? -3.228  -16.914 10.931  0.50 13.50 ? 152 SER A OG  1 
ATOM   1218 N  N   . ALA A 1 152 ? -1.059  -14.444 7.941   1.00 12.01 ? 153 ALA A N   1 
ATOM   1219 C  CA  . ALA A 1 152 ? -0.690  -13.180 7.312   1.00 12.57 ? 153 ALA A CA  1 
ATOM   1220 C  C   . ALA A 1 152 ? -1.314  -11.968 7.999   1.00 12.53 ? 153 ALA A C   1 
ATOM   1221 O  O   . ALA A 1 152 ? -2.416  -12.043 8.569   1.00 13.89 ? 153 ALA A O   1 
ATOM   1222 C  CB  . ALA A 1 152 ? -1.055  -13.168 5.824   1.00 13.17 ? 153 ALA A CB  1 
ATOM   1223 N  N   . LYS A 1 153 ? -0.591  -10.850 7.945   1.00 12.49 ? 154 LYS A N   1 
ATOM   1224 C  CA  . LYS A 1 153 ? -1.121  -9.561  8.387   1.00 12.79 ? 154 LYS A CA  1 
ATOM   1225 C  C   . LYS A 1 153 ? -1.530  -8.761  7.127   1.00 13.20 ? 154 LYS A C   1 
ATOM   1226 O  O   . LYS A 1 153 ? -0.675  -8.296  6.327   1.00 11.89 ? 154 LYS A O   1 
ATOM   1227 C  CB  . LYS A 1 153 ? -0.054  -8.817  9.206   1.00 11.60 ? 154 LYS A CB  1 
ATOM   1228 C  CG  . LYS A 1 153 ? -0.573  -7.535  9.857   1.00 13.16 ? 154 LYS A CG  1 
ATOM   1229 C  CD  . LYS A 1 153 ? -1.473  -7.907  11.038  1.00 14.52 ? 154 LYS A CD  1 
ATOM   1230 C  CE  . LYS A 1 153 ? -1.727  -6.725  11.942  1.00 18.25 ? 154 LYS A CE  1 
ATOM   1231 N  NZ  . LYS A 1 153 ? -2.637  -7.205  13.012  1.00 19.08 ? 154 LYS A NZ  1 
ATOM   1232 N  N   . PRO A 1 154 ? -2.852  -8.648  6.891   1.00 15.13 ? 155 PRO A N   1 
ATOM   1233 C  CA  . PRO A 1 154 ? -3.307  -7.999  5.618   1.00 15.02 ? 155 PRO A CA  1 
ATOM   1234 C  C   . PRO A 1 154 ? -2.751  -6.586  5.499   1.00 14.11 ? 155 PRO A C   1 
ATOM   1235 O  O   . PRO A 1 154 ? -2.359  -6.163  4.398   1.00 15.48 ? 155 PRO A O   1 
ATOM   1236 C  CB  . PRO A 1 154 ? -4.847  -7.973  5.779   1.00 16.06 ? 155 PRO A CB  1 
ATOM   1237 C  CG  . PRO A 1 154 ? -5.075  -9.231  6.579   1.00 17.48 ? 155 PRO A CG  1 
ATOM   1238 C  CD  . PRO A 1 154 ? -4.003  -9.192  7.645   1.00 17.11 ? 155 PRO A CD  1 
ATOM   1239 N  N   . GLY A 1 155 ? -2.681  -5.896  6.623   1.00 12.85 ? 156 GLY A N   1 
ATOM   1240 C  CA  . GLY A 1 155 ? -2.228  -4.518  6.656   1.00 14.06 ? 156 GLY A CA  1 
ATOM   1241 C  C   . GLY A 1 155 ? -0.758  -4.331  6.341   1.00 13.69 ? 156 GLY A C   1 
ATOM   1242 O  O   . GLY A 1 155 ? -0.367  -3.235  6.021   1.00 14.50 ? 156 GLY A O   1 
ATOM   1243 N  N   . LEU A 1 156 ? 0.018   -5.404  6.355   1.00 11.52 ? 157 LEU A N   1 
ATOM   1244 C  CA  . LEU A 1 156 ? 1.422   -5.360  5.979   1.00 10.94 ? 157 LEU A CA  1 
ATOM   1245 C  C   . LEU A 1 156 ? 1.673   -5.604  4.514   1.00 11.40 ? 157 LEU A C   1 
ATOM   1246 O  O   . LEU A 1 156 ? 2.778   -5.346  4.031   1.00 11.11 ? 157 LEU A O   1 
ATOM   1247 C  CB  . LEU A 1 156 ? 2.181   -6.441  6.783   1.00 9.94  ? 157 LEU A CB  1 
ATOM   1248 C  CG  . LEU A 1 156 ? 3.702   -6.528  6.576   1.00 9.54  ? 157 LEU A CG  1 
ATOM   1249 C  CD1 . LEU A 1 156 ? 4.383   -5.187  6.989   1.00 10.10 ? 157 LEU A CD1 1 
ATOM   1250 C  CD2 . LEU A 1 156 ? 4.315   -7.672  7.387   1.00 9.45  ? 157 LEU A CD2 1 
ATOM   1251 N  N   . GLN A 1 157 ? 0.704   -6.169  3.790   1.00 12.97 ? 158 GLN A N   1 
ATOM   1252 C  CA  . GLN A 1 157 ? 1.009   -6.684  2.440   1.00 12.53 ? 158 GLN A CA  1 
ATOM   1253 C  C   . GLN A 1 157 ? 1.412   -5.534  1.499   1.00 12.63 ? 158 GLN A C   1 
ATOM   1254 O  O   . GLN A 1 157 ? 2.287   -5.694  0.704   1.00 12.83 ? 158 GLN A O   1 
ATOM   1255 C  CB  . GLN A 1 157 ? -0.139  -7.522  1.875   1.00 15.98 ? 158 GLN A CB  1 
ATOM   1256 C  CG  . GLN A 1 157 ? 0.248   -8.281  0.592   1.00 15.45 ? 158 GLN A CG  1 
ATOM   1257 C  CD  . GLN A 1 157 ? 1.368   -9.285  0.821   1.00 15.66 ? 158 GLN A CD  1 
ATOM   1258 O  OE1 . GLN A 1 157 ? 1.511   -9.880  1.918   1.00 13.90 ? 158 GLN A OE1 1 
ATOM   1259 N  NE2 . GLN A 1 157 ? 2.189   -9.482  -0.195  1.00 17.50 ? 158 GLN A NE2 1 
ATOM   1260 N  N   . LYS A 1 158 ? 0.848   -4.348  1.651   1.00 14.11 ? 159 LYS A N   1 
ATOM   1261 C  CA  . LYS A 1 158 ? 1.305   -3.265  0.792   1.00 14.28 ? 159 LYS A CA  1 
ATOM   1262 C  C   . LYS A 1 158 ? 2.806   -2.913  0.951   1.00 14.49 ? 159 LYS A C   1 
ATOM   1263 O  O   . LYS A 1 158 ? 3.492   -2.571  -0.015  1.00 12.83 ? 159 LYS A O   1 
ATOM   1264 C  CB  . LYS A 1 158 ? 0.426   -2.041  0.980   1.00 19.24 ? 159 LYS A CB  1 
ATOM   1265 C  CG  . LYS A 1 158 ? -0.921  -2.248  0.305   1.00 26.78 ? 159 LYS A CG  1 
ATOM   1266 C  CD  . LYS A 1 158 ? -1.693  -0.942  0.093   1.00 33.60 ? 159 LYS A CD  1 
ATOM   1267 C  CE  . LYS A 1 158 ? -3.138  -1.205  -0.412  1.00 37.12 ? 159 LYS A CE  1 
ATOM   1268 N  NZ  . LYS A 1 158 ? -4.156  -0.186  0.066   1.00 33.42 ? 159 LYS A NZ  1 
ATOM   1269 N  N   . VAL A 1 159 ? 3.286   -3.012  2.191   1.00 11.90 ? 160 VAL A N   1 
ATOM   1270 C  CA  . VAL A 1 159 ? 4.722   -2.911  2.441   1.00 11.52 ? 160 VAL A CA  1 
ATOM   1271 C  C   . VAL A 1 159 ? 5.510   -4.024  1.750   1.00 11.39 ? 160 VAL A C   1 
ATOM   1272 O  O   . VAL A 1 159 ? 6.508   -3.774  1.089   1.00 13.44 ? 160 VAL A O   1 
ATOM   1273 C  CB  . VAL A 1 159 ? 4.992   -2.912  3.962   1.00 11.44 ? 160 VAL A CB  1 
ATOM   1274 C  CG1 . VAL A 1 159 ? 6.514   -2.964  4.187   1.00 11.05 ? 160 VAL A CG1 1 
ATOM   1275 C  CG2 . VAL A 1 159 ? 4.338   -1.674  4.611   1.00 12.61 ? 160 VAL A CG2 1 
ATOM   1276 N  N   . VAL A 1 160 ? 5.102   -5.266  1.948   1.00 11.21 ? 161 VAL A N   1 
ATOM   1277 C  CA  . VAL A 1 160 ? 5.813   -6.418  1.402   1.00 14.03 ? 161 VAL A CA  1 
ATOM   1278 C  C   . VAL A 1 160 ? 5.868   -6.282  -0.114  1.00 12.61 ? 161 VAL A C   1 
ATOM   1279 O  O   . VAL A 1 160 ? 6.900   -6.560  -0.721  1.00 12.77 ? 161 VAL A O   1 
ATOM   1280 C  CB  . VAL A 1 160 ? 5.067   -7.723  1.849   1.00 15.17 ? 161 VAL A CB  1 
ATOM   1281 C  CG1 . VAL A 1 160 ? 5.485   -8.931  1.001   1.00 18.28 ? 161 VAL A CG1 1 
ATOM   1282 C  CG2 . VAL A 1 160 ? 5.428   -7.932  3.287   1.00 17.63 ? 161 VAL A CG2 1 
ATOM   1283 N  N   . ASP A 1 161 ? 4.786   -5.788  -0.705  1.00 14.75 ? 162 ASP A N   1 
ATOM   1284 C  CA  . ASP A 1 161 ? 4.657   -5.734  -2.163  1.00 17.98 ? 162 ASP A CA  1 
ATOM   1285 C  C   . ASP A 1 161 ? 5.714   -4.781  -2.751  1.00 17.78 ? 162 ASP A C   1 
ATOM   1286 O  O   . ASP A 1 161 ? 6.194   -5.025  -3.835  1.00 22.47 ? 162 ASP A O   1 
ATOM   1287 C  CB  . ASP A 1 161 ? 3.270   -5.201  -2.622  1.00 20.95 ? 162 ASP A CB  1 
ATOM   1288 C  CG  . ASP A 1 161 ? 2.081   -6.206  -2.468  1.00 26.54 ? 162 ASP A CG  1 
ATOM   1289 O  OD1 . ASP A 1 161 ? 2.306   -7.436  -2.419  1.00 24.14 ? 162 ASP A OD1 1 
ATOM   1290 O  OD2 . ASP A 1 161 ? 0.878   -5.717  -2.403  1.00 29.26 ? 162 ASP A OD2 1 
ATOM   1291 N  N   . VAL A 1 162 ? 6.058   -3.686  -2.084  1.00 14.20 ? 163 VAL A N   1 
ATOM   1292 C  CA  . VAL A 1 162 ? 6.865   -2.667  -2.723  1.00 14.34 ? 163 VAL A CA  1 
ATOM   1293 C  C   . VAL A 1 162 ? 8.372   -2.963  -2.554  1.00 12.89 ? 163 VAL A C   1 
ATOM   1294 O  O   . VAL A 1 162 ? 9.249   -2.262  -3.103  1.00 12.52 ? 163 VAL A O   1 
ATOM   1295 C  CB  . VAL A 1 162 ? 6.464   -1.293  -2.143  1.00 15.29 ? 163 VAL A CB  1 
ATOM   1296 C  CG1 . VAL A 1 162 ? 7.035   -1.065  -0.752  1.00 15.47 ? 163 VAL A CG1 1 
ATOM   1297 C  CG2 . VAL A 1 162 ? 6.850   -0.180  -3.099  1.00 18.78 ? 163 VAL A CG2 1 
ATOM   1298 N  N   . LEU A 1 163 ? 8.685   -3.983  -1.749  1.00 13.22 ? 164 LEU A N   1 
ATOM   1299 C  CA  . LEU A 1 163 ? 10.110  -4.223  -1.337  1.00 13.06 ? 164 LEU A CA  1 
ATOM   1300 C  C   . LEU A 1 163 ? 11.026  -4.575  -2.502  1.00 13.26 ? 164 LEU A C   1 
ATOM   1301 O  O   . LEU A 1 163 ? 12.211  -4.216  -2.533  1.00 11.55 ? 164 LEU A O   1 
ATOM   1302 C  CB  . LEU A 1 163 ? 10.236  -5.304  -0.272  1.00 13.14 ? 164 LEU A CB  1 
ATOM   1303 C  CG  . LEU A 1 163 ? 9.609   -4.969  1.090   1.00 13.94 ? 164 LEU A CG  1 
ATOM   1304 C  CD1 . LEU A 1 163 ? 9.941   -6.100  2.070   1.00 14.53 ? 164 LEU A CD1 1 
ATOM   1305 C  CD2 . LEU A 1 163 ? 10.004  -3.616  1.652   1.00 12.99 ? 164 LEU A CD2 1 
ATOM   1306 N  N   . ASP A 1 164 ? 10.471  -5.247  -3.480  1.00 15.56 ? 165 ASP A N   1 
ATOM   1307 C  CA  . ASP A 1 164 ? 11.352  -5.552  -4.570  1.00 20.52 ? 165 ASP A CA  1 
ATOM   1308 C  C   . ASP A 1 164 ? 11.675  -4.313  -5.436  1.00 18.87 ? 165 ASP A C   1 
ATOM   1309 O  O   . ASP A 1 164 ? 12.655  -4.356  -6.155  1.00 22.80 ? 165 ASP A O   1 
ATOM   1310 C  CB  . ASP A 1 164 ? 10.945  -6.842  -5.319  1.00 32.74 ? 165 ASP A CB  1 
ATOM   1311 C  CG  . ASP A 1 164 ? 9.723   -6.667  -6.116  1.00 37.62 ? 165 ASP A CG  1 
ATOM   1312 O  OD1 . ASP A 1 164 ? 9.680   -5.686  -6.883  1.00 48.17 ? 165 ASP A OD1 1 
ATOM   1313 O  OD2 . ASP A 1 164 ? 8.809   -7.527  -6.028  1.00 49.42 ? 165 ASP A OD2 1 
ATOM   1314 N  N   . SER A 1 165 ? 10.955  -3.205  -5.299  1.00 15.98 ? 166 SER A N   1 
ATOM   1315 C  CA  . SER A 1 165 ? 11.420  -1.896  -5.895  1.00 15.39 ? 166 SER A CA  1 
ATOM   1316 C  C   . SER A 1 165 ? 12.462  -1.088  -5.095  1.00 14.48 ? 166 SER A C   1 
ATOM   1317 O  O   . SER A 1 165 ? 12.968  -0.035  -5.561  1.00 13.75 ? 166 SER A O   1 
ATOM   1318 C  CB  . SER A 1 165 ? 10.245  -0.994  -6.203  1.00 16.59 ? 166 SER A CB  1 
ATOM   1319 O  OG  . SER A 1 165 ? 9.770   -0.404  -5.004  1.00 18.87 ? 166 SER A OG  1 
ATOM   1320 N  N   . ILE A 1 166 ? 12.785  -1.550  -3.878  1.00 11.54 ? 167 ILE A N   1 
ATOM   1321 C  CA  . ILE A 1 166 ? 13.844  -0.915  -3.104  1.00 11.48 ? 167 ILE A CA  1 
ATOM   1322 C  C   . ILE A 1 166 ? 14.825  -1.961  -2.596  1.00 11.83 ? 167 ILE A C   1 
ATOM   1323 O  O   . ILE A 1 166 ? 15.217  -1.972  -1.412  1.00 11.65 ? 167 ILE A O   1 
ATOM   1324 C  CB  . ILE A 1 166 ? 13.294  -0.056  -1.922  1.00 10.82 ? 167 ILE A CB  1 
ATOM   1325 C  CG1 . ILE A 1 166 ? 12.440  -0.869  -0.985  1.00 10.43 ? 167 ILE A CG1 1 
ATOM   1326 C  CG2 . ILE A 1 166 ? 12.466  1.143   -2.444  1.00 11.83 ? 167 ILE A CG2 1 
ATOM   1327 C  CD1 . ILE A 1 166 ? 12.385  -0.294  0.477   1.00 11.26 ? 167 ILE A CD1 1 
ATOM   1328 N  N   . LYS A 1 167 ? 15.234  -2.850  -3.518  1.00 11.99 ? 168 LYS A N   1 
ATOM   1329 C  CA  . LYS A 1 167 ? 16.031  -3.970  -3.088  1.00 13.59 ? 168 LYS A CA  1 
ATOM   1330 C  C   . LYS A 1 167 ? 17.340  -3.594  -2.431  1.00 12.34 ? 168 LYS A C   1 
ATOM   1331 O  O   . LYS A 1 167 ? 17.760  -4.311  -1.518  1.00 10.50 ? 168 LYS A O   1 
ATOM   1332 C  CB  . LYS A 1 167 ? 16.269  -4.930  -4.262  1.00 14.24 ? 168 LYS A CB  1 
ATOM   1333 C  CG  . LYS A 1 167 ? 17.010  -6.187  -3.862  1.00 17.10 ? 168 LYS A CG  1 
ATOM   1334 C  CD  . LYS A 1 167 ? 17.235  -7.082  -5.097  1.00 19.64 ? 168 LYS A CD  1 
ATOM   1335 C  CE  . LYS A 1 167 ? 18.237  -8.153  -4.735  1.00 24.69 ? 168 LYS A CE  1 
ATOM   1336 N  NZ  . LYS A 1 167 ? 18.131  -9.377  -5.602  1.00 29.97 ? 168 LYS A NZ  1 
ATOM   1337 N  N   . THR A 1 168 ? 17.995  -2.514  -2.896  1.00 10.65 ? 169 THR A N   1 
ATOM   1338 C  CA  . THR A 1 168 ? 19.356  -2.225  -2.510  1.00 10.52 ? 169 THR A CA  1 
ATOM   1339 C  C   . THR A 1 168 ? 19.471  -0.831  -1.847  1.00 10.39 ? 169 THR A C   1 
ATOM   1340 O  O   . THR A 1 168 ? 18.597  0.021   -1.980  1.00 10.68 ? 169 THR A O   1 
ATOM   1341 C  CB  . THR A 1 168 ? 20.312  -2.251  -3.720  1.00 11.67 ? 169 THR A CB  1 
ATOM   1342 O  OG1 . THR A 1 168 ? 19.744  -1.475  -4.771  1.00 11.48 ? 169 THR A OG1 1 
ATOM   1343 C  CG2 . THR A 1 168 ? 20.501  -3.725  -4.216  1.00 12.20 ? 169 THR A CG2 1 
ATOM   1344 N  N   . LYS A 1 169 ? 20.533  -0.695  -1.085  1.00 11.12 ? 170 LYS A N   1 
ATOM   1345 C  CA  . LYS A 1 169 ? 20.884  0.532   -0.332  1.00 12.88 ? 170 LYS A CA  1 
ATOM   1346 C  C   . LYS A 1 169 ? 20.698  1.785   -1.160  1.00 13.66 ? 170 LYS A C   1 
ATOM   1347 O  O   . LYS A 1 169 ? 21.230  1.867   -2.287  1.00 15.36 ? 170 LYS A O   1 
ATOM   1348 C  CB  . LYS A 1 169 ? 22.323  0.419   0.198   1.00 13.65 ? 170 LYS A CB  1 
ATOM   1349 C  CG  . LYS A 1 169 ? 22.725  1.666   1.038   1.00 13.69 ? 170 LYS A CG  1 
ATOM   1350 C  CD  . LYS A 1 169 ? 24.092  1.563   1.710   1.00 19.34 ? 170 LYS A CD  1 
ATOM   1351 C  CE  . LYS A 1 169 ? 25.140  1.051   0.711   1.00 23.41 ? 170 LYS A CE  1 
ATOM   1352 N  NZ  . LYS A 1 169 ? 26.477  0.606   1.253   1.00 28.65 ? 170 LYS A NZ  1 
ATOM   1353 N  N   . GLY A 1 170 ? 19.903  2.745   -0.651  1.00 12.68 ? 171 GLY A N   1 
ATOM   1354 C  CA  . GLY A 1 170 ? 19.759  4.073   -1.289  1.00 12.25 ? 171 GLY A CA  1 
ATOM   1355 C  C   . GLY A 1 170 ? 18.602  4.139   -2.263  1.00 13.26 ? 171 GLY A C   1 
ATOM   1356 O  O   . GLY A 1 170 ? 18.279  5.237   -2.775  1.00 14.77 ? 171 GLY A O   1 
ATOM   1357 N  N   . LYS A 1 171 ? 17.945  3.016   -2.532  1.00 11.45 ? 172 LYS A N   1 
ATOM   1358 C  CA  . LYS A 1 171 ? 16.729  3.041   -3.349  1.00 13.42 ? 172 LYS A CA  1 
ATOM   1359 C  C   . LYS A 1 171 ? 15.520  3.449   -2.524  1.00 12.32 ? 172 LYS A C   1 
ATOM   1360 O  O   . LYS A 1 171 ? 15.361  3.039   -1.385  1.00 12.91 ? 172 LYS A O   1 
ATOM   1361 C  CB  . LYS A 1 171 ? 16.408  1.685   -3.998  1.00 15.23 ? 172 LYS A CB  1 
ATOM   1362 C  CG  . LYS A 1 171 ? 17.453  1.234   -5.004  1.00 19.30 ? 172 LYS A CG  1 
ATOM   1363 C  CD  . LYS A 1 171 ? 16.929  0.196   -6.005  1.00 24.34 ? 172 LYS A CD  1 
ATOM   1364 C  CE  . LYS A 1 171 ? 15.881  0.737   -7.020  1.00 27.76 ? 172 LYS A CE  1 
ATOM   1365 N  NZ  . LYS A 1 171 ? 15.221  -0.316  -7.898  1.00 27.50 ? 172 LYS A NZ  1 
ATOM   1366 N  N   . SER A 1 172 ? 14.673  4.251   -3.128  1.00 13.63 ? 173 SER A N   1 
ATOM   1367 C  CA  . SER A 1 172 ? 13.447  4.705   -2.515  1.00 12.93 ? 173 SER A CA  1 
ATOM   1368 C  C   . SER A 1 172 ? 12.287  4.561   -3.505  1.00 13.58 ? 173 SER A C   1 
ATOM   1369 O  O   . SER A 1 172 ? 12.475  4.484   -4.764  1.00 13.29 ? 173 SER A O   1 
ATOM   1370 C  CB  . SER A 1 172 ? 13.592  6.147   -1.989  1.00 13.12 ? 173 SER A CB  1 
ATOM   1371 O  OG  . SER A 1 172 ? 13.718  7.119   -3.047  1.00 14.05 ? 173 SER A OG  1 
ATOM   1372 N  N   . ALA A 1 173 ? 11.077  4.522   -2.968  1.00 14.68 ? 174 ALA A N   1 
ATOM   1373 C  CA  . ALA A 1 173 ? 9.870   4.520   -3.781  1.00 13.69 ? 174 ALA A CA  1 
ATOM   1374 C  C   . ALA A 1 173 ? 8.737   5.290   -3.138  1.00 15.11 ? 174 ALA A C   1 
ATOM   1375 O  O   . ALA A 1 173 ? 8.635   5.375   -1.925  1.00 13.07 ? 174 ALA A O   1 
ATOM   1376 C  CB  . ALA A 1 173 ? 9.445   3.102   -4.122  1.00 13.11 ? 174 ALA A CB  1 
ATOM   1377 N  N   . ASP A 1 174 ? 7.916   5.916   -3.987  1.00 14.68 ? 175 ASP A N   1 
ATOM   1378 C  CA  . ASP A 1 174 ? 6.713   6.553   -3.507  1.00 16.54 ? 175 ASP A CA  1 
ATOM   1379 C  C   . ASP A 1 174 ? 5.889   5.565   -2.714  1.00 15.89 ? 175 ASP A C   1 
ATOM   1380 O  O   . ASP A 1 174 ? 5.739   4.396   -3.098  1.00 16.92 ? 175 ASP A O   1 
ATOM   1381 C  CB  . ASP A 1 174 ? 5.851   7.136   -4.671  1.00 20.26 ? 175 ASP A CB  1 
ATOM   1382 C  CG  . ASP A 1 174 ? 6.587   8.243   -5.425  1.00 26.53 ? 175 ASP A CG  1 
ATOM   1383 O  OD1 . ASP A 1 174 ? 7.150   9.163   -4.759  1.00 29.38 ? 175 ASP A OD1 1 
ATOM   1384 O  OD2 . ASP A 1 174 ? 6.656   8.199   -6.692  1.00 32.63 ? 175 ASP A OD2 1 
ATOM   1385 N  N   . PHE A 1 175 ? 5.337   6.046   -1.597  1.00 13.71 ? 176 PHE A N   1 
ATOM   1386 C  CA  . PHE A 1 175 ? 4.632   5.123   -0.703  1.00 14.31 ? 176 PHE A CA  1 
ATOM   1387 C  C   . PHE A 1 175 ? 3.586   5.922   0.014   1.00 15.11 ? 176 PHE A C   1 
ATOM   1388 O  O   . PHE A 1 175 ? 3.622   6.139   1.231   1.00 16.92 ? 176 PHE A O   1 
ATOM   1389 C  CB  . PHE A 1 175 ? 5.592   4.306   0.230   1.00 13.07 ? 176 PHE A CB  1 
ATOM   1390 C  CG  . PHE A 1 175 ? 4.949   3.038   0.769   1.00 12.53 ? 176 PHE A CG  1 
ATOM   1391 C  CD1 . PHE A 1 175 ? 4.660   1.958   -0.081  1.00 13.77 ? 176 PHE A CD1 1 
ATOM   1392 C  CD2 . PHE A 1 175 ? 4.585   2.947   2.124   1.00 12.91 ? 176 PHE A CD2 1 
ATOM   1393 C  CE1 . PHE A 1 175 ? 4.028   0.789   0.406   1.00 13.75 ? 176 PHE A CE1 1 
ATOM   1394 C  CE2 . PHE A 1 175 ? 3.958   1.793   2.610   1.00 12.71 ? 176 PHE A CE2 1 
ATOM   1395 C  CZ  . PHE A 1 175 ? 3.685   0.733   1.763   1.00 13.68 ? 176 PHE A CZ  1 
ATOM   1396 N  N   . THR A 1 176 ? 2.597   6.407   -0.763  1.00 14.01 ? 177 THR A N   1 
ATOM   1397 C  CA  . THR A 1 176 ? 1.570   7.228   -0.155  1.00 14.29 ? 177 THR A CA  1 
ATOM   1398 C  C   . THR A 1 176 ? 0.344   6.414   0.223   1.00 12.83 ? 177 THR A C   1 
ATOM   1399 O  O   . THR A 1 176 ? 0.111   5.301   -0.317  1.00 13.00 ? 177 THR A O   1 
ATOM   1400 C  CB  . THR A 1 176 ? 1.118   8.374   -1.101  1.00 17.44 ? 177 THR A CB  1 
ATOM   1401 O  OG1 . THR A 1 176 ? 0.918   7.810   -2.376  1.00 20.47 ? 177 THR A OG1 1 
ATOM   1402 C  CG2 . THR A 1 176 ? 2.144   9.453   -1.201  1.00 19.78 ? 177 THR A CG2 1 
ATOM   1403 N  N   . ASN A 1 177 ? -0.430  7.028   1.118   1.00 12.48 ? 178 ASN A N   1 
ATOM   1404 C  CA  . ASN A 1 177 ? -1.729  6.512   1.571   1.00 12.91 ? 178 ASN A CA  1 
ATOM   1405 C  C   . ASN A 1 177 ? -1.577  5.170   2.255   1.00 12.89 ? 178 ASN A C   1 
ATOM   1406 O  O   . ASN A 1 177 ? -2.475  4.367   2.203   1.00 13.57 ? 178 ASN A O   1 
ATOM   1407 C  CB  . ASN A 1 177 ? -2.687  6.444   0.387   1.00 14.84 ? 178 ASN A CB  1 
ATOM   1408 C  CG  . ASN A 1 177 ? -2.876  7.817   -0.253  1.00 18.13 ? 178 ASN A CG  1 
ATOM   1409 O  OD1 . ASN A 1 177 ? -3.528  8.677   0.337   1.00 19.05 ? 178 ASN A OD1 1 
ATOM   1410 N  ND2 . ASN A 1 177 ? -2.265  8.046   -1.432  1.00 15.70 ? 178 ASN A ND2 1 
ATOM   1411 N  N   . PHE A 1 178 ? -0.460  4.945   2.940   1.00 11.13 ? 179 PHE A N   1 
ATOM   1412 C  CA  . PHE A 1 178 ? -0.397  3.686   3.701   1.00 11.29 ? 179 PHE A CA  1 
ATOM   1413 C  C   . PHE A 1 178 ? -0.946  3.965   5.113   1.00 11.45 ? 179 PHE A C   1 
ATOM   1414 O  O   . PHE A 1 178 ? -0.491  4.887   5.703   1.00 13.97 ? 179 PHE A O   1 
ATOM   1415 C  CB  . PHE A 1 178 ? 1.014   3.159   3.755   1.00 11.07 ? 179 PHE A CB  1 
ATOM   1416 C  CG  . PHE A 1 178 ? 1.136   1.932   4.600   1.00 10.77 ? 179 PHE A CG  1 
ATOM   1417 C  CD1 . PHE A 1 178 ? 0.753   0.693   4.127   1.00 10.85 ? 179 PHE A CD1 1 
ATOM   1418 C  CD2 . PHE A 1 178 ? 1.496   2.060   5.929   1.00 10.53 ? 179 PHE A CD2 1 
ATOM   1419 C  CE1 . PHE A 1 178 ? 0.778   -0.427  4.970   1.00 13.27 ? 179 PHE A CE1 1 
ATOM   1420 C  CE2 . PHE A 1 178 ? 1.568   0.950   6.756   1.00 10.37 ? 179 PHE A CE2 1 
ATOM   1421 C  CZ  . PHE A 1 178 ? 1.240   -0.307  6.306   1.00 10.70 ? 179 PHE A CZ  1 
ATOM   1422 N  N   . ASP A 1 179 ? -1.761  3.073   5.679   1.00 11.52 ? 180 ASP A N   1 
ATOM   1423 C  CA  . ASP A 1 179 ? -2.403  3.344   6.960   1.00 11.73 ? 180 ASP A CA  1 
ATOM   1424 C  C   . ASP A 1 179 ? -1.707  2.469   8.037   1.00 10.78 ? 180 ASP A C   1 
ATOM   1425 O  O   . ASP A 1 179 ? -1.879  1.223   8.057   1.00 10.77 ? 180 ASP A O   1 
ATOM   1426 C  CB  . ASP A 1 179 ? -3.873  2.923   6.834   1.00 14.41 ? 180 ASP A CB  1 
ATOM   1427 C  CG  . ASP A 1 179 ? -4.659  3.255   8.066   1.00 17.34 ? 180 ASP A CG  1 
ATOM   1428 O  OD1 . ASP A 1 179 ? -4.062  3.591   9.106   1.00 13.61 ? 180 ASP A OD1 1 
ATOM   1429 O  OD2 . ASP A 1 179 ? -5.904  3.187   7.999   1.00 18.59 ? 180 ASP A OD2 1 
ATOM   1430 N  N   . PRO A 1 180 ? -0.959  3.102   8.940   1.00 11.31 ? 181 PRO A N   1 
ATOM   1431 C  CA  . PRO A 1 180 ? -0.157  2.253   9.862   1.00 11.71 ? 181 PRO A CA  1 
ATOM   1432 C  C   . PRO A 1 180 ? -1.053  1.600   10.937  1.00 11.68 ? 181 PRO A C   1 
ATOM   1433 O  O   . PRO A 1 180 ? -0.613  0.687   11.685  1.00 10.71 ? 181 PRO A O   1 
ATOM   1434 C  CB  . PRO A 1 180 ? 0.832   3.267   10.454  1.00 12.24 ? 181 PRO A CB  1 
ATOM   1435 C  CG  . PRO A 1 180 ? 0.099   4.575   10.404  1.00 11.77 ? 181 PRO A CG  1 
ATOM   1436 C  CD  . PRO A 1 180 ? -0.528  4.506   9.048   1.00 11.72 ? 181 PRO A CD  1 
ATOM   1437 N  N   . ARG A 1 181 ? -2.314  2.027   11.003  1.00 10.25 ? 182 ARG A N   1 
ATOM   1438 C  CA  . ARG A 1 181 ? -3.270  1.332   11.941  1.00 11.44 ? 182 ARG A CA  1 
ATOM   1439 C  C   . ARG A 1 181 ? -3.414  -0.162  11.619  1.00 11.56 ? 182 ARG A C   1 
ATOM   1440 O  O   . ARG A 1 181 ? -3.785  -0.958  12.480  1.00 12.54 ? 182 ARG A O   1 
ATOM   1441 C  CB  . ARG A 1 181 ? -4.648  2.036   11.880  1.00 11.99 ? 182 ARG A CB  1 
ATOM   1442 C  CG  . ARG A 1 181 ? -4.629  3.434   12.473  1.00 12.99 ? 182 ARG A CG  1 
ATOM   1443 C  CD  . ARG A 1 181 ? -6.010  4.088   12.300  1.00 13.92 ? 182 ARG A CD  1 
ATOM   1444 N  NE  . ARG A 1 181 ? -6.315  4.271   10.899  1.00 16.31 ? 182 ARG A NE  1 
ATOM   1445 C  CZ  . ARG A 1 181 ? -7.353  5.014   10.536  1.00 19.97 ? 182 ARG A CZ  1 
ATOM   1446 N  NH1 . ARG A 1 181 ? -8.107  5.557   11.487  1.00 17.38 ? 182 ARG A NH1 1 
ATOM   1447 N  NH2 . ARG A 1 181 ? -7.627  5.215   9.270   1.00 20.00 ? 182 ARG A NH2 1 
ATOM   1448 N  N   . GLY A 1 182 ? -3.130  -0.545  10.359  1.00 10.80 ? 183 GLY A N   1 
ATOM   1449 C  CA  . GLY A 1 182 ? -3.217  -1.916  9.928   1.00 10.74 ? 183 GLY A CA  1 
ATOM   1450 C  C   . GLY A 1 182 ? -2.063  -2.763  10.411  1.00 11.95 ? 183 GLY A C   1 
ATOM   1451 O  O   . GLY A 1 182 ? -2.082  -3.963  10.176  1.00 13.61 ? 183 GLY A O   1 
ATOM   1452 N  N   . LEU A 1 183 ? -1.097  -2.163  11.136  1.00 10.82 ? 184 LEU A N   1 
ATOM   1453 C  CA  . LEU A 1 183 ? 0.029   -2.929  11.714  1.00 10.17 ? 184 LEU A CA  1 
ATOM   1454 C  C   . LEU A 1 183 ? -0.133  -3.138  13.230  1.00 10.99 ? 184 LEU A C   1 
ATOM   1455 O  O   . LEU A 1 183 ? 0.785   -3.732  13.847  1.00 11.35 ? 184 LEU A O   1 
ATOM   1456 C  CB  . LEU A 1 183 ? 1.340   -2.167  11.455  1.00 10.11 ? 184 LEU A CB  1 
ATOM   1457 C  CG  . LEU A 1 183 ? 1.635   -2.061  9.937   1.00 11.59 ? 184 LEU A CG  1 
ATOM   1458 C  CD1 . LEU A 1 183 ? 2.812   -1.124  9.762   1.00 11.77 ? 184 LEU A CD1 1 
ATOM   1459 C  CD2 . LEU A 1 183 ? 1.796   -3.399  9.212   1.00 13.07 ? 184 LEU A CD2 1 
ATOM   1460 N  N   . LEU A 1 184 ? -1.253  -2.657  13.842  1.00 10.12 ? 185 LEU A N   1 
ATOM   1461 C  CA  . LEU A 1 184 ? -1.387  -2.733  15.331  1.00 9.84  ? 185 LEU A CA  1 
ATOM   1462 C  C   . LEU A 1 184 ? -2.080  -4.049  15.770  1.00 11.37 ? 185 LEU A C   1 
ATOM   1463 O  O   . LEU A 1 184 ? -3.013  -4.573  15.074  1.00 13.45 ? 185 LEU A O   1 
ATOM   1464 C  CB  . LEU A 1 184 ? -2.211  -1.547  15.904  1.00 9.83  ? 185 LEU A CB  1 
ATOM   1465 C  CG  . LEU A 1 184 ? -1.658  -0.178  15.537  1.00 10.02 ? 185 LEU A CG  1 
ATOM   1466 C  CD1 . LEU A 1 184 ? -2.456  1.067   15.904  1.00 11.65 ? 185 LEU A CD1 1 
ATOM   1467 C  CD2 . LEU A 1 184 ? -0.214  -0.108  16.075  1.00 10.80 ? 185 LEU A CD2 1 
ATOM   1468 N  N   . PRO A 1 185 ? -1.689  -4.562  16.948  1.00 10.37 ? 186 PRO A N   1 
ATOM   1469 C  CA  . PRO A 1 185 ? -2.462  -5.636  17.494  1.00 11.17 ? 186 PRO A CA  1 
ATOM   1470 C  C   . PRO A 1 185 ? -3.791  -5.098  18.118  1.00 11.63 ? 186 PRO A C   1 
ATOM   1471 O  O   . PRO A 1 185 ? -4.042  -3.888  18.180  1.00 12.28 ? 186 PRO A O   1 
ATOM   1472 C  CB  . PRO A 1 185 ? -1.556  -6.187  18.605  1.00 9.73  ? 186 PRO A CB  1 
ATOM   1473 C  CG  . PRO A 1 185 ? -0.841  -4.954  19.098  1.00 8.49  ? 186 PRO A CG  1 
ATOM   1474 C  CD  . PRO A 1 185 ? -0.584  -4.096  17.820  1.00 8.99  ? 186 PRO A CD  1 
ATOM   1475 N  N   A GLU A 1 186 ? -4.590  -6.023  18.617  0.50 12.13 ? 187 GLU A N   1 
ATOM   1476 N  N   B GLU A 1 186 ? -4.647  -6.000  18.617  0.50 11.56 ? 187 GLU A N   1 
ATOM   1477 C  CA  A GLU A 1 186 ? -5.849  -5.665  19.193  0.50 12.63 ? 187 GLU A CA  1 
ATOM   1478 C  CA  B GLU A 1 186 ? -5.894  -5.546  19.250  0.50 11.64 ? 187 GLU A CA  1 
ATOM   1479 C  C   A GLU A 1 186 ? -5.689  -4.896  20.517  0.50 12.10 ? 187 GLU A C   1 
ATOM   1480 C  C   B GLU A 1 186 ? -5.608  -4.764  20.510  0.50 11.44 ? 187 GLU A C   1 
ATOM   1481 O  O   A GLU A 1 186 ? -6.372  -3.897  20.763  0.50 11.59 ? 187 GLU A O   1 
ATOM   1482 O  O   B GLU A 1 186 ? -6.129  -3.643  20.717  0.50 10.68 ? 187 GLU A O   1 
ATOM   1483 C  CB  A GLU A 1 186 ? -6.628  -6.962  19.397  0.50 14.22 ? 187 GLU A CB  1 
ATOM   1484 C  CB  B GLU A 1 186 ? -6.820  -6.729  19.629  0.50 12.12 ? 187 GLU A CB  1 
ATOM   1485 C  CG  A GLU A 1 186 ? -7.827  -6.843  20.262  0.50 15.86 ? 187 GLU A CG  1 
ATOM   1486 C  CG  B GLU A 1 186 ? -7.244  -7.550  18.437  0.50 13.40 ? 187 GLU A CG  1 
ATOM   1487 C  CD  A GLU A 1 186 ? -8.422  -8.189  20.591  0.50 17.49 ? 187 GLU A CD  1 
ATOM   1488 C  CD  B GLU A 1 186 ? -8.131  -8.716  18.816  0.50 13.24 ? 187 GLU A CD  1 
ATOM   1489 O  OE1 A GLU A 1 186 ? -8.310  -9.094  19.725  0.50 18.82 ? 187 GLU A OE1 1 
ATOM   1490 O  OE1 B GLU A 1 186 ? -8.264  -9.021  20.037  0.50 14.95 ? 187 GLU A OE1 1 
ATOM   1491 O  OE2 A GLU A 1 186 ? -9.012  -8.313  21.690  0.50 19.39 ? 187 GLU A OE2 1 
ATOM   1492 O  OE2 B GLU A 1 186 ? -8.653  -9.346  17.876  0.50 15.56 ? 187 GLU A OE2 1 
ATOM   1493 N  N   . SER A 1 187 ? -4.770  -5.350  21.367  1.00 11.06 ? 188 SER A N   1 
ATOM   1494 C  CA  . SER A 1 187 ? -4.568  -4.742  22.695  1.00 11.00 ? 188 SER A CA  1 
ATOM   1495 C  C   . SER A 1 187 ? -3.411  -3.752  22.657  1.00 11.14 ? 188 SER A C   1 
ATOM   1496 O  O   . SER A 1 187 ? -2.397  -3.993  21.973  1.00 11.56 ? 188 SER A O   1 
ATOM   1497 C  CB  . SER A 1 187 ? -4.170  -5.816  23.702  1.00 11.36 ? 188 SER A CB  1 
ATOM   1498 O  OG  . SER A 1 187 ? -3.976  -5.253  25.010  1.00 12.00 ? 188 SER A OG  1 
ATOM   1499 N  N   . LEU A 1 188 ? -3.568  -2.689  23.413  1.00 10.66 ? 189 LEU A N   1 
ATOM   1500 C  CA  . LEU A 1 188 ? -2.464  -1.713  23.641  1.00 10.79 ? 189 LEU A CA  1 
ATOM   1501 C  C   . LEU A 1 188 ? -1.795  -1.857  25.011  1.00 10.37 ? 189 LEU A C   1 
ATOM   1502 O  O   . LEU A 1 188 ? -1.056  -0.934  25.436  1.00 12.26 ? 189 LEU A O   1 
ATOM   1503 C  CB  . LEU A 1 188 ? -2.990  -0.274  23.476  1.00 13.06 ? 189 LEU A CB  1 
ATOM   1504 C  CG  . LEU A 1 188 ? -3.521  0.129   22.078  1.00 14.26 ? 189 LEU A CG  1 
ATOM   1505 C  CD1 . LEU A 1 188 ? -3.988  1.594   22.102  1.00 16.86 ? 189 LEU A CD1 1 
ATOM   1506 C  CD2 . LEU A 1 188 ? -2.399  -0.070  21.070  1.00 16.42 ? 189 LEU A CD2 1 
ATOM   1507 N  N   . ASP A 1 189 ? -2.019  -2.970  25.729  1.00 10.27 ? 190 ASP A N   1 
ATOM   1508 C  CA  . ASP A 1 189 ? -1.248  -3.256  26.931  1.00 10.06 ? 190 ASP A CA  1 
ATOM   1509 C  C   . ASP A 1 189 ? 0.260   -3.210  26.583  1.00 8.85  ? 190 ASP A C   1 
ATOM   1510 O  O   . ASP A 1 189 ? 0.664   -3.654  25.477  1.00 7.96  ? 190 ASP A O   1 
ATOM   1511 C  CB  . ASP A 1 189 ? -1.527  -4.638  27.463  1.00 11.96 ? 190 ASP A CB  1 
ATOM   1512 C  CG  . ASP A 1 189 ? -2.940  -4.791  28.086  1.00 12.90 ? 190 ASP A CG  1 
ATOM   1513 O  OD1 . ASP A 1 189 ? -3.654  -3.805  28.311  1.00 16.01 ? 190 ASP A OD1 1 
ATOM   1514 O  OD2 . ASP A 1 189 ? -3.290  -5.963  28.323  1.00 17.59 ? 190 ASP A OD2 1 
ATOM   1515 N  N   . TYR A 1 190 ? 1.059   -2.596  27.467  1.00 7.83  ? 191 TYR A N   1 
ATOM   1516 C  CA  . TYR A 1 190 ? 2.450   -2.389  27.100  1.00 7.91  ? 191 TYR A CA  1 
ATOM   1517 C  C   . TYR A 1 190 ? 3.396   -2.404  28.317  1.00 7.56  ? 191 TYR A C   1 
ATOM   1518 O  O   . TYR A 1 190 ? 2.965   -2.278  29.509  1.00 7.08  ? 191 TYR A O   1 
ATOM   1519 C  CB  . TYR A 1 190 ? 2.629   -1.005  26.371  1.00 7.56  ? 191 TYR A CB  1 
ATOM   1520 C  CG  . TYR A 1 190 ? 2.238   0.181   27.264  1.00 7.91  ? 191 TYR A CG  1 
ATOM   1521 C  CD1 . TYR A 1 190 ? 3.175   0.803   28.080  1.00 8.25  ? 191 TYR A CD1 1 
ATOM   1522 C  CD2 . TYR A 1 190 ? 0.946   0.729   27.236  1.00 8.30  ? 191 TYR A CD2 1 
ATOM   1523 C  CE1 . TYR A 1 190 ? 2.819   1.848   28.921  1.00 8.53  ? 191 TYR A CE1 1 
ATOM   1524 C  CE2 . TYR A 1 190 ? 0.600   1.818   28.028  1.00 8.80  ? 191 TYR A CE2 1 
ATOM   1525 C  CZ  . TYR A 1 190 ? 1.542   2.362   28.885  1.00 8.43  ? 191 TYR A CZ  1 
ATOM   1526 O  OH  . TYR A 1 190 ? 1.209   3.393   29.721  1.00 8.95  ? 191 TYR A OH  1 
ATOM   1527 N  N   . TRP A 1 191 ? 4.675   -2.574  28.010  1.00 7.85  ? 192 TRP A N   1 
ATOM   1528 C  CA  . TRP A 1 191 ? 5.741   -2.277  28.969  1.00 7.23  ? 192 TRP A CA  1 
ATOM   1529 C  C   . TRP A 1 191 ? 6.427   -1.009  28.602  1.00 7.47  ? 192 TRP A C   1 
ATOM   1530 O  O   . TRP A 1 191 ? 6.505   -0.672  27.413  1.00 7.22  ? 192 TRP A O   1 
ATOM   1531 C  CB  . TRP A 1 191 ? 6.763   -3.390  28.968  1.00 7.75  ? 192 TRP A CB  1 
ATOM   1532 C  CG  . TRP A 1 191 ? 6.238   -4.707  29.423  1.00 7.46  ? 192 TRP A CG  1 
ATOM   1533 C  CD1 . TRP A 1 191 ? 5.957   -5.132  30.713  1.00 7.75  ? 192 TRP A CD1 1 
ATOM   1534 C  CD2 . TRP A 1 191 ? 5.976   -5.850  28.572  1.00 8.42  ? 192 TRP A CD2 1 
ATOM   1535 N  NE1 . TRP A 1 191 ? 5.531   -6.471  30.703  1.00 9.06  ? 192 TRP A NE1 1 
ATOM   1536 C  CE2 . TRP A 1 191 ? 5.529   -6.931  29.431  1.00 8.36  ? 192 TRP A CE2 1 
ATOM   1537 C  CE3 . TRP A 1 191 ? 6.040   -6.052  27.213  1.00 8.09  ? 192 TRP A CE3 1 
ATOM   1538 C  CZ2 . TRP A 1 191 ? 5.173   -8.169  28.925  1.00 8.71  ? 192 TRP A CZ2 1 
ATOM   1539 C  CZ3 . TRP A 1 191 ? 5.708   -7.327  26.722  1.00 8.38  ? 192 TRP A CZ3 1 
ATOM   1540 C  CH2 . TRP A 1 191 ? 5.302   -8.341  27.570  1.00 8.38  ? 192 TRP A CH2 1 
ATOM   1541 N  N   . THR A 1 192 ? 6.935   -0.261  29.595  1.00 6.59  ? 193 THR A N   1 
ATOM   1542 C  CA  . THR A 1 192 ? 7.683   0.956   29.237  1.00 6.82  ? 193 THR A CA  1 
ATOM   1543 C  C   . THR A 1 192 ? 8.922   1.210   30.078  1.00 7.17  ? 193 THR A C   1 
ATOM   1544 O  O   . THR A 1 192 ? 8.937   0.841   31.245  1.00 8.03  ? 193 THR A O   1 
ATOM   1545 C  CB  . THR A 1 192 ? 6.746   2.180   29.247  1.00 6.71  ? 193 THR A CB  1 
ATOM   1546 O  OG1 . THR A 1 192 ? 7.463   3.351   28.855  1.00 6.70  ? 193 THR A OG1 1 
ATOM   1547 C  CG2 . THR A 1 192 ? 6.152   2.447   30.644  1.00 7.40  ? 193 THR A CG2 1 
ATOM   1548 N  N   . TYR A 1 193 ? 9.986   1.783   29.466  1.00 6.49  ? 194 TYR A N   1 
ATOM   1549 C  CA  . TYR A 1 193 ? 11.195  2.057   30.209  1.00 6.78  ? 194 TYR A CA  1 
ATOM   1550 C  C   . TYR A 1 193 ? 11.974  3.094   29.407  1.00 6.80  ? 194 TYR A C   1 
ATOM   1551 O  O   . TYR A 1 193 ? 11.678  3.323   28.173  1.00 6.56  ? 194 TYR A O   1 
ATOM   1552 C  CB  . TYR A 1 193 ? 12.047  0.712   30.387  1.00 6.57  ? 194 TYR A CB  1 
ATOM   1553 C  CG  . TYR A 1 193 ? 12.736  0.297   29.120  1.00 6.38  ? 194 TYR A CG  1 
ATOM   1554 C  CD1 . TYR A 1 193 ? 12.037  -0.441  28.146  1.00 6.03  ? 194 TYR A CD1 1 
ATOM   1555 C  CD2 . TYR A 1 193 ? 14.054  0.660   28.895  1.00 6.41  ? 194 TYR A CD2 1 
ATOM   1556 C  CE1 . TYR A 1 193 ? 12.687  -0.786  26.964  1.00 6.09  ? 194 TYR A CE1 1 
ATOM   1557 C  CE2 . TYR A 1 193 ? 14.707  0.338   27.666  1.00 6.49  ? 194 TYR A CE2 1 
ATOM   1558 C  CZ  . TYR A 1 193 ? 14.001  -0.405  26.745  1.00 6.24  ? 194 TYR A CZ  1 
ATOM   1559 O  OH  . TYR A 1 193 ? 14.638  -0.687  25.540  1.00 7.10  ? 194 TYR A OH  1 
ATOM   1560 N  N   . PRO A 1 194 ? 12.859  3.835   30.093  1.00 6.93  ? 195 PRO A N   1 
ATOM   1561 C  CA  . PRO A 1 194 ? 13.693  4.801   29.369  1.00 7.07  ? 195 PRO A CA  1 
ATOM   1562 C  C   . PRO A 1 194 ? 14.912  4.179   28.681  1.00 7.01  ? 195 PRO A C   1 
ATOM   1563 O  O   . PRO A 1 194 ? 15.667  3.443   29.362  1.00 7.07  ? 195 PRO A O   1 
ATOM   1564 C  CB  . PRO A 1 194 ? 14.228  5.743   30.511  1.00 7.70  ? 195 PRO A CB  1 
ATOM   1565 C  CG  . PRO A 1 194 ? 14.216  4.849   31.731  1.00 7.40  ? 195 PRO A CG  1 
ATOM   1566 C  CD  . PRO A 1 194 ? 13.019  3.936   31.566  1.00 7.23  ? 195 PRO A CD  1 
ATOM   1567 N  N   . GLY A 1 195 ? 15.149  4.507   27.392  1.00 6.63  ? 196 GLY A N   1 
ATOM   1568 C  CA  . GLY A 1 195 ? 16.295  3.845   26.720  1.00 7.21  ? 196 GLY A CA  1 
ATOM   1569 C  C   . GLY A 1 195 ? 16.805  4.715   25.608  1.00 6.95  ? 196 GLY A C   1 
ATOM   1570 O  O   . GLY A 1 195 ? 16.906  5.935   25.778  1.00 7.04  ? 196 GLY A O   1 
ATOM   1571 N  N   . SER A 1 196 ? 17.231  4.067   24.539  1.00 6.74  ? 197 SER A N   1 
ATOM   1572 C  CA  . SER A 1 196 ? 18.096  4.758   23.551  1.00 6.24  ? 197 SER A CA  1 
ATOM   1573 C  C   . SER A 1 196 ? 17.703  4.324   22.160  1.00 6.19  ? 197 SER A C   1 
ATOM   1574 O  O   . SER A 1 196 ? 16.910  3.406   21.988  1.00 6.27  ? 197 SER A O   1 
ATOM   1575 C  CB  . SER A 1 196 ? 19.582  4.330   23.763  1.00 6.19  ? 197 SER A CB  1 
ATOM   1576 O  OG  . SER A 1 196 ? 19.697  2.961   23.269  1.00 6.09  ? 197 SER A OG  1 
ATOM   1577 N  N   . LEU A 1 197 ? 18.255  4.985   21.138  1.00 6.30  ? 198 LEU A N   1 
ATOM   1578 C  CA  . LEU A 1 197 ? 18.169  4.432   19.777  1.00 6.99  ? 198 LEU A CA  1 
ATOM   1579 C  C   . LEU A 1 197 ? 18.909  3.082   19.837  1.00 7.00  ? 198 LEU A C   1 
ATOM   1580 O  O   . LEU A 1 197 ? 19.899  2.901   20.559  1.00 7.22  ? 198 LEU A O   1 
ATOM   1581 C  CB  . LEU A 1 197 ? 18.871  5.435   18.851  1.00 7.92  ? 198 LEU A CB  1 
ATOM   1582 C  CG  . LEU A 1 197 ? 18.285  6.826   18.770  1.00 8.31  ? 198 LEU A CG  1 
ATOM   1583 C  CD1 . LEU A 1 197 ? 19.165  7.574   17.826  1.00 9.66  ? 198 LEU A CD1 1 
ATOM   1584 C  CD2 . LEU A 1 197 ? 16.893  6.703   18.153  1.00 9.18  ? 198 LEU A CD2 1 
ATOM   1585 N  N   . THR A 1 198 ? 18.425  2.078   19.099  1.00 5.80  ? 199 THR A N   1 
ATOM   1586 C  CA  . THR A 1 198 ? 19.126  0.789   19.077  1.00 6.20  ? 199 THR A CA  1 
ATOM   1587 C  C   . THR A 1 198 ? 20.167  0.631   17.962  1.00 6.86  ? 199 THR A C   1 
ATOM   1588 O  O   . THR A 1 198 ? 20.750  -0.463  17.816  1.00 7.62  ? 199 THR A O   1 
ATOM   1589 C  CB  . THR A 1 198 ? 18.129  -0.376  18.887  1.00 5.84  ? 199 THR A CB  1 
ATOM   1590 O  OG1 . THR A 1 198 ? 17.558  -0.270  17.564  1.00 5.78  ? 199 THR A OG1 1 
ATOM   1591 C  CG2 . THR A 1 198 ? 17.041  -0.362  19.980  1.00 5.77  ? 199 THR A CG2 1 
ATOM   1592 N  N   . THR A 1 199 ? 20.345  1.673   17.139  1.00 7.89  ? 200 THR A N   1 
ATOM   1593 C  CA  . THR A 1 199 ? 21.489  1.685   16.202  1.00 8.97  ? 200 THR A CA  1 
ATOM   1594 C  C   . THR A 1 199 ? 22.278  2.951   16.441  1.00 8.94  ? 200 THR A C   1 
ATOM   1595 O  O   . THR A 1 199 ? 21.773  3.937   17.016  1.00 8.72  ? 200 THR A O   1 
ATOM   1596 C  CB  . THR A 1 199 ? 21.132  1.618   14.729  1.00 10.89 ? 200 THR A CB  1 
ATOM   1597 O  OG1 . THR A 1 199 ? 20.725  2.886   14.278  1.00 15.02 ? 200 THR A OG1 1 
ATOM   1598 C  CG2 . THR A 1 199 ? 19.945  0.672   14.505  1.00 11.46 ? 200 THR A CG2 1 
ATOM   1599 N  N   . PRO A 1 200 ? 23.541  2.934   15.961  1.00 9.14  ? 201 PRO A N   1 
ATOM   1600 C  CA  . PRO A 1 200 ? 24.311  4.213   16.035  1.00 9.33  ? 201 PRO A CA  1 
ATOM   1601 C  C   . PRO A 1 200 ? 23.430  5.319   15.476  1.00 10.38 ? 201 PRO A C   1 
ATOM   1602 O  O   . PRO A 1 200 ? 22.797  5.092   14.402  1.00 12.90 ? 201 PRO A O   1 
ATOM   1603 C  CB  . PRO A 1 200 ? 25.489  3.901   15.100  1.00 9.33  ? 201 PRO A CB  1 
ATOM   1604 C  CG  . PRO A 1 200 ? 25.756  2.414   15.386  1.00 9.28  ? 201 PRO A CG  1 
ATOM   1605 C  CD  . PRO A 1 200 ? 24.316  1.836   15.366  1.00 8.69  ? 201 PRO A CD  1 
ATOM   1606 N  N   . PRO A 1 201 ? 23.424  6.496   16.075  1.00 10.12 ? 202 PRO A N   1 
ATOM   1607 C  CA  . PRO A 1 201 ? 24.340  6.974   17.116  1.00 10.73 ? 202 PRO A CA  1 
ATOM   1608 C  C   . PRO A 1 201 ? 23.988  6.614   18.573  1.00 9.09  ? 202 PRO A C   1 
ATOM   1609 O  O   . PRO A 1 201 ? 24.622  7.111   19.497  1.00 9.82  ? 202 PRO A O   1 
ATOM   1610 C  CB  . PRO A 1 201 ? 24.327  8.487   16.908  1.00 11.30 ? 202 PRO A CB  1 
ATOM   1611 C  CG  . PRO A 1 201 ? 23.020  8.801   16.287  1.00 12.78 ? 202 PRO A CG  1 
ATOM   1612 C  CD  . PRO A 1 201 ? 22.625  7.625   15.482  1.00 12.09 ? 202 PRO A CD  1 
ATOM   1613 N  N   . LEU A 1 202 ? 23.014  5.714   18.751  1.00 8.71  ? 203 LEU A N   1 
ATOM   1614 C  CA  . LEU A 1 202 ? 22.706  5.110   20.084  1.00 8.09  ? 203 LEU A CA  1 
ATOM   1615 C  C   . LEU A 1 202 ? 22.312  6.141   21.143  1.00 7.94  ? 203 LEU A C   1 
ATOM   1616 O  O   . LEU A 1 202 ? 22.445  5.889   22.339  1.00 7.23  ? 203 LEU A O   1 
ATOM   1617 C  CB  . LEU A 1 202 ? 23.869  4.192   20.597  1.00 7.59  ? 203 LEU A CB  1 
ATOM   1618 C  CG  . LEU A 1 202 ? 24.168  3.071   19.606  1.00 7.72  ? 203 LEU A CG  1 
ATOM   1619 C  CD1 . LEU A 1 202 ? 25.513  2.442   20.066  1.00 8.75  ? 203 LEU A CD1 1 
ATOM   1620 C  CD2 . LEU A 1 202 ? 23.109  1.946   19.644  1.00 7.64  ? 203 LEU A CD2 1 
ATOM   1621 N  N   . LEU A 1 203 ? 21.780  7.261   20.663  1.00 8.03  ? 204 LEU A N   1 
ATOM   1622 C  CA  . LEU A 1 203 ? 21.440  8.388   21.541  1.00 8.82  ? 204 LEU A CA  1 
ATOM   1623 C  C   . LEU A 1 203 ? 20.414  7.993   22.624  1.00 8.12  ? 204 LEU A C   1 
ATOM   1624 O  O   . LEU A 1 203 ? 19.438  7.274   22.363  1.00 8.59  ? 204 LEU A O   1 
ATOM   1625 C  CB  . LEU A 1 203 ? 20.929  9.614   20.700  1.00 9.11  ? 204 LEU A CB  1 
ATOM   1626 C  CG  . LEU A 1 203 ? 22.022  10.207  19.744  1.00 10.29 ? 204 LEU A CG  1 
ATOM   1627 C  CD1 . LEU A 1 203 ? 21.337  11.193  18.764  1.00 11.81 ? 204 LEU A CD1 1 
ATOM   1628 C  CD2 . LEU A 1 203 ? 23.141  10.845  20.558  1.00 11.31 ? 204 LEU A CD2 1 
ATOM   1629 N  N   . GLU A 1 204 ? 20.607  8.529   23.820  1.00 8.80  ? 205 GLU A N   1 
ATOM   1630 C  CA  . GLU A 1 204 ? 19.783  8.118   24.966  1.00 8.39  ? 205 GLU A CA  1 
ATOM   1631 C  C   . GLU A 1 204 ? 18.586  9.051   25.090  1.00 8.50  ? 205 GLU A C   1 
ATOM   1632 O  O   . GLU A 1 204 ? 18.458  9.793   26.089  1.00 9.36  ? 205 GLU A O   1 
ATOM   1633 C  CB  . GLU A 1 204 ? 20.620  8.005   26.284  1.00 8.74  ? 205 GLU A CB  1 
ATOM   1634 C  CG  . GLU A 1 204 ? 21.485  6.750   26.105  1.00 8.59  ? 205 GLU A CG  1 
ATOM   1635 C  CD  . GLU A 1 204 ? 22.400  6.452   27.297  1.00 9.24  ? 205 GLU A CD  1 
ATOM   1636 O  OE1 . GLU A 1 204 ? 22.663  7.370   28.101  1.00 10.00 ? 205 GLU A OE1 1 
ATOM   1637 O  OE2 . GLU A 1 204 ? 22.833  5.301   27.442  1.00 8.97  ? 205 GLU A OE2 1 
ATOM   1638 N  N   . CYS A 1 205 ? 17.686  8.952   24.100  1.00 7.76  ? 206 CYS A N   1 
ATOM   1639 C  CA  . CYS A 1 205 ? 16.633  9.986   23.933  1.00 7.49  ? 206 CYS A CA  1 
ATOM   1640 C  C   . CYS A 1 205 ? 15.266  9.384   23.773  1.00 7.39  ? 206 CYS A C   1 
ATOM   1641 O  O   . CYS A 1 205 ? 14.336  10.074  23.395  1.00 7.94  ? 206 CYS A O   1 
ATOM   1642 C  CB  . CYS A 1 205 ? 16.941  10.824  22.700  1.00 8.64  ? 206 CYS A CB  1 
ATOM   1643 S  SG  . CYS A 1 205 ? 17.015  9.886   21.138  1.00 10.39 ? 206 CYS A SG  1 
ATOM   1644 N  N   . VAL A 1 206 ? 15.144  8.092   24.123  1.00 6.67  ? 207 VAL A N   1 
ATOM   1645 C  CA  . VAL A 1 206 ? 13.900  7.332   23.796  1.00 6.63  ? 207 VAL A CA  1 
ATOM   1646 C  C   . VAL A 1 206 ? 13.125  6.908   25.037  1.00 6.61  ? 207 VAL A C   1 
ATOM   1647 O  O   . VAL A 1 206 ? 13.686  6.209   25.913  1.00 7.91  ? 207 VAL A O   1 
ATOM   1648 C  CB  . VAL A 1 206 ? 14.215  6.066   22.938  1.00 6.54  ? 207 VAL A CB  1 
ATOM   1649 C  CG1 . VAL A 1 206 ? 12.866  5.412   22.506  1.00 6.83  ? 207 VAL A CG1 1 
ATOM   1650 C  CG2 . VAL A 1 206 ? 14.956  6.517   21.657  1.00 6.78  ? 207 VAL A CG2 1 
ATOM   1651 N  N   . THR A 1 207 ? 11.806  7.177   25.020  1.00 6.14  ? 208 THR A N   1 
ATOM   1652 C  CA  . THR A 1 207 ? 10.873  6.465   25.924  1.00 6.37  ? 208 THR A CA  1 
ATOM   1653 C  C   . THR A 1 207 ? 10.355  5.301   25.128  1.00 5.98  ? 208 THR A C   1 
ATOM   1654 O  O   . THR A 1 207 ? 9.696   5.482   24.086  1.00 6.17  ? 208 THR A O   1 
ATOM   1655 C  CB  . THR A 1 207 ? 9.703   7.350   26.387  1.00 7.30  ? 208 THR A CB  1 
ATOM   1656 O  OG1 . THR A 1 207 ? 10.195  8.453   27.151  1.00 7.77  ? 208 THR A OG1 1 
ATOM   1657 C  CG2 . THR A 1 207 ? 8.754   6.537   27.258  1.00 6.65  ? 208 THR A CG2 1 
ATOM   1658 N  N   . TRP A 1 208 ? 10.671  4.100   25.589  1.00 5.88  ? 209 TRP A N   1 
ATOM   1659 C  CA  . TRP A 1 208 ? 10.232  2.902   24.854  1.00 5.59  ? 209 TRP A CA  1 
ATOM   1660 C  C   . TRP A 1 208 ? 8.887   2.473   25.355  1.00 5.54  ? 209 TRP A C   1 
ATOM   1661 O  O   . TRP A 1 208 ? 8.677   2.388   26.550  1.00 5.48  ? 209 TRP A O   1 
ATOM   1662 C  CB  . TRP A 1 208 ? 11.238  1.733   25.094  1.00 5.72  ? 209 TRP A CB  1 
ATOM   1663 C  CG  . TRP A 1 208 ? 12.378  1.901   24.116  1.00 5.39  ? 209 TRP A CG  1 
ATOM   1664 C  CD1 . TRP A 1 208 ? 13.652  2.471   24.276  1.00 5.54  ? 209 TRP A CD1 1 
ATOM   1665 C  CD2 . TRP A 1 208 ? 12.299  1.516   22.718  1.00 5.70  ? 209 TRP A CD2 1 
ATOM   1666 N  NE1 . TRP A 1 208 ? 14.308  2.446   23.063  1.00 5.57  ? 209 TRP A NE1 1 
ATOM   1667 C  CE2 . TRP A 1 208 ? 13.590  1.840   22.136  1.00 5.23  ? 209 TRP A CE2 1 
ATOM   1668 C  CE3 . TRP A 1 208 ? 11.311  0.863   21.944  1.00 5.42  ? 209 TRP A CE3 1 
ATOM   1669 C  CZ2 . TRP A 1 208 ? 13.879  1.593   20.814  1.00 5.55  ? 209 TRP A CZ2 1 
ATOM   1670 C  CZ3 . TRP A 1 208 ? 11.610  0.575   20.608  1.00 5.95  ? 209 TRP A CZ3 1 
ATOM   1671 C  CH2 . TRP A 1 208 ? 12.857  0.930   20.060  1.00 5.54  ? 209 TRP A CH2 1 
ATOM   1672 N  N   . ILE A 1 209 ? 7.986   2.173   24.434  1.00 5.94  ? 210 ILE A N   1 
ATOM   1673 C  CA  . ILE A 1 209 ? 6.650   1.653   24.784  1.00 6.00  ? 210 ILE A CA  1 
ATOM   1674 C  C   . ILE A 1 209 ? 6.500   0.378   23.928  1.00 6.08  ? 210 ILE A C   1 
ATOM   1675 O  O   . ILE A 1 209 ? 6.449   0.469   22.727  1.00 5.86  ? 210 ILE A O   1 
ATOM   1676 C  CB  . ILE A 1 209 ? 5.550   2.659   24.417  1.00 6.67  ? 210 ILE A CB  1 
ATOM   1677 C  CG1 . ILE A 1 209 ? 5.750   3.917   25.265  1.00 6.87  ? 210 ILE A CG1 1 
ATOM   1678 C  CG2 . ILE A 1 209 ? 4.164   2.068   24.702  1.00 6.99  ? 210 ILE A CG2 1 
ATOM   1679 C  CD1 . ILE A 1 209 ? 4.962   5.104   24.693  1.00 7.57  ? 210 ILE A CD1 1 
ATOM   1680 N  N   . VAL A 1 210 ? 6.599   -0.813  24.559  1.00 5.88  ? 211 VAL A N   1 
ATOM   1681 C  CA  . VAL A 1 210 ? 6.642   -2.109  23.846  1.00 5.81  ? 211 VAL A CA  1 
ATOM   1682 C  C   . VAL A 1 210 ? 5.360   -2.884  24.096  1.00 5.96  ? 211 VAL A C   1 
ATOM   1683 O  O   . VAL A 1 210 ? 5.017   -3.166  25.260  1.00 6.02  ? 211 VAL A O   1 
ATOM   1684 C  CB  . VAL A 1 210 ? 7.875   -2.991  24.303  1.00 5.32  ? 211 VAL A CB  1 
ATOM   1685 C  CG1 . VAL A 1 210 ? 7.858   -4.330  23.521  1.00 5.35  ? 211 VAL A CG1 1 
ATOM   1686 C  CG2 . VAL A 1 210 ? 9.176   -2.247  23.964  1.00 5.79  ? 211 VAL A CG2 1 
ATOM   1687 N  N   . LEU A 1 211 ? 4.583   -3.107  23.041  1.00 6.40  ? 212 LEU A N   1 
ATOM   1688 C  CA  . LEU A 1 211 ? 3.275   -3.753  23.227  1.00 6.64  ? 212 LEU A CA  1 
ATOM   1689 C  C   . LEU A 1 211 ? 3.485   -5.217  23.588  1.00 7.01  ? 212 LEU A C   1 
ATOM   1690 O  O   . LEU A 1 211 ? 4.367   -5.921  23.044  1.00 7.71  ? 212 LEU A O   1 
ATOM   1691 C  CB  . LEU A 1 211 ? 2.403   -3.653  21.978  1.00 6.72  ? 212 LEU A CB  1 
ATOM   1692 C  CG  . LEU A 1 211 ? 2.070   -2.215  21.557  1.00 7.39  ? 212 LEU A CG  1 
ATOM   1693 C  CD1 . LEU A 1 211 ? 1.070   -2.212  20.383  1.00 7.22  ? 212 LEU A CD1 1 
ATOM   1694 C  CD2 . LEU A 1 211 ? 1.516   -1.378  22.720  1.00 7.84  ? 212 LEU A CD2 1 
ATOM   1695 N  N   . LYS A 1 212 ? 2.614   -5.678  24.486  1.00 7.70  ? 213 LYS A N   1 
ATOM   1696 C  CA  . LYS A 1 212 ? 2.640   -7.081  24.923  1.00 9.23  ? 213 LYS A CA  1 
ATOM   1697 C  C   . LYS A 1 212 ? 2.155   -8.051  23.848  1.00 9.46  ? 213 LYS A C   1 
ATOM   1698 O  O   . LYS A 1 212 ? 2.701   -9.134  23.660  1.00 9.43  ? 213 LYS A O   1 
ATOM   1699 C  CB  . LYS A 1 212 ? 1.825   -7.228  26.257  1.00 12.09 ? 213 LYS A CB  1 
ATOM   1700 C  CG  . LYS A 1 212 ? 1.580   -8.727  26.669  1.00 15.62 ? 213 LYS A CG  1 
ATOM   1701 C  CD  . LYS A 1 212 ? 0.851   -8.902  27.993  1.00 20.94 ? 213 LYS A CD  1 
ATOM   1702 C  CE  . LYS A 1 212 ? 0.680   -10.391 28.377  1.00 24.91 ? 213 LYS A CE  1 
ATOM   1703 N  NZ  . LYS A 1 212 ? -0.283  -10.464 29.535  1.00 32.41 ? 213 LYS A NZ  1 
ATOM   1704 N  N   . GLU A 1 213 ? 1.147   -7.647  23.120  1.00 8.68  ? 214 GLU A N   1 
ATOM   1705 C  CA  . GLU A 1 213 ? 0.535   -8.557  22.136  1.00 10.42 ? 214 GLU A CA  1 
ATOM   1706 C  C   . GLU A 1 213 ? 1.284   -8.504  20.810  1.00 9.44  ? 214 GLU A C   1 
ATOM   1707 O  O   . GLU A 1 213 ? 1.339   -7.446  20.177  1.00 8.63  ? 214 GLU A O   1 
ATOM   1708 C  CB  . GLU A 1 213 ? -0.932  -8.171  21.890  1.00 11.30 ? 214 GLU A CB  1 
ATOM   1709 C  CG  . GLU A 1 213 ? -1.636  -9.186  20.962  1.00 14.02 ? 214 GLU A CG  1 
ATOM   1710 C  CD  . GLU A 1 213 ? -3.071  -8.779  20.686  1.00 17.39 ? 214 GLU A CD  1 
ATOM   1711 O  OE1 . GLU A 1 213 ? -3.637  -7.994  21.429  1.00 14.69 ? 214 GLU A OE1 1 
ATOM   1712 O  OE2 . GLU A 1 213 ? -3.631  -9.309  19.688  1.00 27.14 ? 214 GLU A OE2 1 
ATOM   1713 N  N   . PRO A 1 214 ? 1.841   -9.639  20.369  1.00 10.63 ? 215 PRO A N   1 
ATOM   1714 C  CA  . PRO A 1 214 ? 2.532   -9.561  19.049  1.00 10.02 ? 215 PRO A CA  1 
ATOM   1715 C  C   . PRO A 1 214 ? 1.501   -9.521  17.914  1.00 10.79 ? 215 PRO A C   1 
ATOM   1716 O  O   . PRO A 1 214 ? 0.311   -9.931  18.133  1.00 11.75 ? 215 PRO A O   1 
ATOM   1717 C  CB  . PRO A 1 214 ? 3.350   -10.856 18.973  1.00 11.07 ? 215 PRO A CB  1 
ATOM   1718 C  CG  . PRO A 1 214 ? 2.699   -11.794 19.934  1.00 14.24 ? 215 PRO A CG  1 
ATOM   1719 C  CD  . PRO A 1 214 ? 1.918   -10.990 20.964  1.00 11.51 ? 215 PRO A CD  1 
ATOM   1720 N  N   . ILE A 1 215 ? 1.910   -9.037  16.727  1.00 9.74  ? 216 ILE A N   1 
ATOM   1721 C  CA  . ILE A 1 215 ? 1.065   -9.274  15.552  1.00 9.35  ? 216 ILE A CA  1 
ATOM   1722 C  C   . ILE A 1 215 ? 1.548   -10.523 14.849  1.00 9.09  ? 216 ILE A C   1 
ATOM   1723 O  O   . ILE A 1 215 ? 2.695   -10.874 14.983  1.00 8.59  ? 216 ILE A O   1 
ATOM   1724 C  CB  . ILE A 1 215 ? 1.055   -8.070  14.564  1.00 9.41  ? 216 ILE A CB  1 
ATOM   1725 C  CG1 . ILE A 1 215 ? 2.488   -7.652  14.125  1.00 9.57  ? 216 ILE A CG1 1 
ATOM   1726 C  CG2 . ILE A 1 215 ? 0.382   -6.871  15.255  1.00 11.58 ? 216 ILE A CG2 1 
ATOM   1727 C  CD1 . ILE A 1 215 ? 2.439   -6.714  12.828  1.00 9.30  ? 216 ILE A CD1 1 
ATOM   1728 N  N   A SER A 1 216 ? 0.657   -11.224 14.128  0.50 9.59  ? 217 SER A N   1 
ATOM   1729 N  N   B SER A 1 216 ? 0.673   -11.241 14.133  0.50 9.85  ? 217 SER A N   1 
ATOM   1730 C  CA  A SER A 1 216 ? 1.144   -12.348 13.287  0.50 10.07 ? 217 SER A CA  1 
ATOM   1731 C  CA  B SER A 1 216 ? 1.208   -12.350 13.304  0.50 10.43 ? 217 SER A CA  1 
ATOM   1732 C  C   A SER A 1 216 ? 1.344   -11.941 11.830  0.50 9.72  ? 217 SER A C   1 
ATOM   1733 C  C   B SER A 1 216 ? 1.362   -11.936 11.850  0.50 9.94  ? 217 SER A C   1 
ATOM   1734 O  O   A SER A 1 216 ? 0.525   -11.205 11.287  0.50 10.74 ? 217 SER A O   1 
ATOM   1735 O  O   B SER A 1 216 ? 0.529   -11.200 11.330  0.50 10.89 ? 217 SER A O   1 
ATOM   1736 C  CB  A SER A 1 216 ? 0.209   -13.576 13.326  0.50 10.42 ? 217 SER A CB  1 
ATOM   1737 C  CB  B SER A 1 216 ? 0.323   -13.607 13.349  0.50 11.20 ? 217 SER A CB  1 
ATOM   1738 O  OG  A SER A 1 216 ? 0.092   -14.063 14.655  0.50 10.93 ? 217 SER A OG  1 
ATOM   1739 O  OG  B SER A 1 216 ? -1.023  -13.209 13.407  0.50 12.60 ? 217 SER A OG  1 
ATOM   1740 N  N   . VAL A 1 217 ? 2.428   -12.411 11.228  1.00 9.81  ? 218 VAL A N   1 
ATOM   1741 C  CA  . VAL A 1 217 ? 2.692   -12.167 9.816   1.00 9.76  ? 218 VAL A CA  1 
ATOM   1742 C  C   . VAL A 1 217 ? 2.929   -13.555 9.245   1.00 9.77  ? 218 VAL A C   1 
ATOM   1743 O  O   . VAL A 1 217 ? 3.326   -14.505 9.975   1.00 10.54 ? 218 VAL A O   1 
ATOM   1744 C  CB  . VAL A 1 217 ? 3.925   -11.267 9.560   1.00 9.70  ? 218 VAL A CB  1 
ATOM   1745 C  CG1 . VAL A 1 217 ? 3.705   -9.899  10.214  1.00 9.18  ? 218 VAL A CG1 1 
ATOM   1746 C  CG2 . VAL A 1 217 ? 5.177   -11.892 10.133  1.00 11.10 ? 218 VAL A CG2 1 
ATOM   1747 N  N   . SER A 1 218 ? 2.806   -13.679 7.935   1.00 10.09 ? 219 SER A N   1 
ATOM   1748 C  CA  . SER A 1 218 ? 2.982   -15.021 7.354   1.00 11.27 ? 219 SER A CA  1 
ATOM   1749 C  C   . SER A 1 218 ? 4.474   -15.326 7.052   1.00 11.43 ? 219 SER A C   1 
ATOM   1750 O  O   . SER A 1 218 ? 5.328   -14.436 6.948   1.00 9.92  ? 219 SER A O   1 
ATOM   1751 C  CB  . SER A 1 218 ? 2.109   -15.231 6.111   1.00 11.45 ? 219 SER A CB  1 
ATOM   1752 O  OG  . SER A 1 218 ? 2.573   -14.389 5.073   1.00 12.83 ? 219 SER A OG  1 
ATOM   1753 N  N   . SER A 1 219 ? 4.786   -16.608 6.858   1.00 11.98 ? 220 SER A N   1 
ATOM   1754 C  CA  . SER A 1 219 ? 6.130   -16.968 6.548   1.00 12.78 ? 220 SER A CA  1 
ATOM   1755 C  C   . SER A 1 219 ? 6.476   -16.311 5.217   1.00 13.42 ? 220 SER A C   1 
ATOM   1756 O  O   . SER A 1 219 ? 7.625   -15.842 5.049   1.00 13.96 ? 220 SER A O   1 
ATOM   1757 C  CB  . SER A 1 219 ? 6.314   -18.503 6.475   1.00 15.32 ? 220 SER A CB  1 
ATOM   1758 O  OG  . SER A 1 219 ? 5.516   -18.913 5.410   1.00 22.99 ? 220 SER A OG  1 
ATOM   1759 N  N   . GLU A 1 220 ? 5.522   -16.232 4.266   1.00 15.12 ? 221 GLU A N   1 
ATOM   1760 C  CA  . GLU A 1 220 ? 5.843   -15.635 2.934   1.00 14.43 ? 221 GLU A CA  1 
ATOM   1761 C  C   . GLU A 1 220 ? 6.181   -14.108 3.084   1.00 14.11 ? 221 GLU A C   1 
ATOM   1762 O  O   . GLU A 1 220 ? 7.073   -13.562 2.383   1.00 14.67 ? 221 GLU A O   1 
ATOM   1763 C  CB  . GLU A 1 220 ? 4.714   -15.824 1.921   1.00 17.21 ? 221 GLU A CB  1 
ATOM   1764 C  CG  . GLU A 1 220 ? 4.491   -17.295 1.503   1.00 21.13 ? 221 GLU A CG  1 
ATOM   1765 C  CD  . GLU A 1 220 ? 3.558   -18.035 2.456   1.00 24.24 ? 221 GLU A CD  1 
ATOM   1766 O  OE1 . GLU A 1 220 ? 3.227   -17.555 3.561   1.00 21.76 ? 221 GLU A OE1 1 
ATOM   1767 O  OE2 . GLU A 1 220 ? 3.127   -19.155 2.107   1.00 29.28 ? 221 GLU A OE2 1 
ATOM   1768 N  N   . GLN A 1 221 ? 5.458   -13.453 3.983   1.00 12.25 ? 222 GLN A N   1 
ATOM   1769 C  CA  . GLN A 1 221 ? 5.658   -12.006 4.229   1.00 11.46 ? 222 GLN A CA  1 
ATOM   1770 C  C   . GLN A 1 221 ? 7.069   -11.768 4.784   1.00 11.85 ? 222 GLN A C   1 
ATOM   1771 O  O   . GLN A 1 221 ? 7.849   -10.917 4.301   1.00 10.02 ? 222 GLN A O   1 
ATOM   1772 C  CB  . GLN A 1 221 ? 4.573   -11.472 5.185   1.00 11.51 ? 222 GLN A CB  1 
ATOM   1773 C  CG  . GLN A 1 221 ? 3.239   -11.257 4.467   1.00 11.22 ? 222 GLN A CG  1 
ATOM   1774 C  CD  . GLN A 1 221 ? 2.126   -10.722 5.346   1.00 11.22 ? 222 GLN A CD  1 
ATOM   1775 O  OE1 . GLN A 1 221 ? 2.021   -11.093 6.497   1.00 11.35 ? 222 GLN A OE1 1 
ATOM   1776 N  NE2 . GLN A 1 221 ? 1.290   -9.841  4.792   1.00 11.15 ? 222 GLN A NE2 1 
ATOM   1777 N  N   . VAL A 1 222 ? 7.457   -12.565 5.783   1.00 11.72 ? 223 VAL A N   1 
ATOM   1778 C  CA  . VAL A 1 222 ? 8.792   -12.336 6.407   1.00 13.68 ? 223 VAL A CA  1 
ATOM   1779 C  C   . VAL A 1 222 ? 9.925   -12.781 5.437   1.00 15.01 ? 223 VAL A C   1 
ATOM   1780 O  O   . VAL A 1 222 ? 10.996  -12.142 5.354   1.00 13.88 ? 223 VAL A O   1 
ATOM   1781 C  CB  . VAL A 1 222 ? 8.915   -12.959 7.825   1.00 16.01 ? 223 VAL A CB  1 
ATOM   1782 C  CG1 . VAL A 1 222 ? 9.086   -14.457 7.783   1.00 16.86 ? 223 VAL A CG1 1 
ATOM   1783 C  CG2 . VAL A 1 222 ? 10.137  -12.347 8.508   1.00 17.01 ? 223 VAL A CG2 1 
ATOM   1784 N  N   . LEU A 1 223 ? 9.628   -13.800 4.616   1.00 13.96 ? 224 LEU A N   1 
ATOM   1785 C  CA  . LEU A 1 223 ? 10.598  -14.211 3.595   1.00 16.39 ? 224 LEU A CA  1 
ATOM   1786 C  C   . LEU A 1 223 ? 10.941  -13.090 2.633   1.00 15.52 ? 224 LEU A C   1 
ATOM   1787 O  O   . LEU A 1 223 ? 12.127  -12.993 2.212   1.00 15.89 ? 224 LEU A O   1 
ATOM   1788 C  CB  . LEU A 1 223 ? 10.112  -15.439 2.814   1.00 17.66 ? 224 LEU A CB  1 
ATOM   1789 C  CG  . LEU A 1 223 ? 10.286  -16.755 3.595   1.00 21.28 ? 224 LEU A CG  1 
ATOM   1790 C  CD1 . LEU A 1 223 ? 9.297   -17.827 3.079   1.00 24.67 ? 224 LEU A CD1 1 
ATOM   1791 C  CD2 . LEU A 1 223 ? 11.738  -17.226 3.601   1.00 23.06 ? 224 LEU A CD2 1 
ATOM   1792 N  N   . LYS A 1 224 ? 9.944   -12.266 2.282   1.00 15.43 ? 225 LYS A N   1 
ATOM   1793 C  CA  . LYS A 1 224 ? 10.187  -11.106 1.421   1.00 16.02 ? 225 LYS A CA  1 
ATOM   1794 C  C   . LYS A 1 224 ? 11.039  -10.020 2.100   1.00 13.31 ? 225 LYS A C   1 
ATOM   1795 O  O   . LYS A 1 224 ? 11.882  -9.425  1.384   1.00 13.02 ? 225 LYS A O   1 
ATOM   1796 C  CB  . LYS A 1 224 ? 8.911   -10.566 0.824   1.00 18.55 ? 225 LYS A CB  1 
ATOM   1797 C  CG  . LYS A 1 224 ? 8.385   -11.585 -0.230  1.00 23.06 ? 225 LYS A CG  1 
ATOM   1798 C  CD  . LYS A 1 224 ? 7.001   -11.311 -0.749  1.00 28.17 ? 225 LYS A CD  1 
ATOM   1799 C  CE  . LYS A 1 224 ? 6.573   -12.430 -1.711  1.00 30.64 ? 225 LYS A CE  1 
ATOM   1800 N  NZ  . LYS A 1 224 ? 5.214   -12.221 -2.328  1.00 32.74 ? 225 LYS A NZ  1 
ATOM   1801 N  N   . PHE A 1 225 ? 10.942  -9.821  3.437   1.00 10.36 ? 226 PHE A N   1 
ATOM   1802 C  CA  . PHE A 1 225 ? 11.893  -8.929  4.106   1.00 10.28 ? 226 PHE A CA  1 
ATOM   1803 C  C   . PHE A 1 225 ? 13.305  -9.470  3.911   1.00 10.24 ? 226 PHE A C   1 
ATOM   1804 O  O   . PHE A 1 225 ? 14.202  -8.725  3.662   1.00 9.72  ? 226 PHE A O   1 
ATOM   1805 C  CB  . PHE A 1 225 ? 11.689  -8.952  5.654   1.00 10.90 ? 226 PHE A CB  1 
ATOM   1806 C  CG  . PHE A 1 225 ? 10.506  -8.138  6.143   1.00 12.74 ? 226 PHE A CG  1 
ATOM   1807 C  CD1 . PHE A 1 225 ? 9.441   -7.801  5.333   1.00 15.11 ? 226 PHE A CD1 1 
ATOM   1808 C  CD2 . PHE A 1 225 ? 10.451  -7.809  7.497   1.00 15.98 ? 226 PHE A CD2 1 
ATOM   1809 C  CE1 . PHE A 1 225 ? 8.373   -7.056  5.806   1.00 16.49 ? 226 PHE A CE1 1 
ATOM   1810 C  CE2 . PHE A 1 225 ? 9.378   -7.070  7.994   1.00 18.91 ? 226 PHE A CE2 1 
ATOM   1811 C  CZ  . PHE A 1 225 ? 8.341   -6.678  7.140   1.00 17.85 ? 226 PHE A CZ  1 
ATOM   1812 N  N   . ARG A 1 226 ? 13.476  -10.779 3.999   1.00 9.84  ? 227 ARG A N   1 
ATOM   1813 C  CA  . ARG A 1 226 ? 14.824  -11.358 3.908   1.00 10.82 ? 227 ARG A CA  1 
ATOM   1814 C  C   . ARG A 1 226 ? 15.418  -11.397 2.496   1.00 12.08 ? 227 ARG A C   1 
ATOM   1815 O  O   . ARG A 1 226 ? 16.587  -11.797 2.359   1.00 12.89 ? 227 ARG A O   1 
ATOM   1816 C  CB  . ARG A 1 226 ? 14.827  -12.802 4.474   1.00 9.73  ? 227 ARG A CB  1 
ATOM   1817 C  CG  . ARG A 1 226 ? 14.312  -12.899 5.908   1.00 9.08  ? 227 ARG A CG  1 
ATOM   1818 C  CD  . ARG A 1 226 ? 14.362  -14.368 6.356   1.00 10.85 ? 227 ARG A CD  1 
ATOM   1819 N  NE  . ARG A 1 226 ? 13.791  -14.481 7.737   1.00 10.37 ? 227 ARG A NE  1 
ATOM   1820 C  CZ  . ARG A 1 226 ? 12.880  -15.377 8.115   1.00 12.09 ? 227 ARG A CZ  1 
ATOM   1821 N  NH1 . ARG A 1 226 ? 12.488  -16.404 7.271   1.00 12.17 ? 227 ARG A NH1 1 
ATOM   1822 N  NH2 . ARG A 1 226 ? 12.410  -15.316 9.350   1.00 12.39 ? 227 ARG A NH2 1 
ATOM   1823 N  N   . LYS A 1 227 ? 14.658  -10.929 1.486   1.00 12.25 ? 228 LYS A N   1 
ATOM   1824 C  CA  . LYS A 1 227 ? 15.198  -10.788 0.120   1.00 13.39 ? 228 LYS A CA  1 
ATOM   1825 C  C   . LYS A 1 227 ? 15.857  -9.441  -0.140  1.00 12.94 ? 228 LYS A C   1 
ATOM   1826 O  O   . LYS A 1 227 ? 16.549  -9.225  -1.172  1.00 12.30 ? 228 LYS A O   1 
ATOM   1827 C  CB  . LYS A 1 227 ? 14.084  -11.051 -0.905  1.00 16.14 ? 228 LYS A CB  1 
ATOM   1828 C  CG  . LYS A 1 227 ? 13.817  -12.558 -1.005  1.00 23.39 ? 228 LYS A CG  1 
ATOM   1829 C  CD  . LYS A 1 227 ? 12.609  -12.924 -1.848  1.00 29.94 ? 228 LYS A CD  1 
ATOM   1830 C  CE  . LYS A 1 227 ? 12.896  -12.889 -3.357  1.00 37.04 ? 228 LYS A CE  1 
ATOM   1831 N  NZ  . LYS A 1 227 ? 11.624  -12.661 -4.138  1.00 41.10 ? 228 LYS A NZ  1 
ATOM   1832 N  N   . LEU A 1 228 ? 15.663  -8.524  0.810   1.00 11.31 ? 229 LEU A N   1 
ATOM   1833 C  CA  . LEU A 1 228 ? 16.263  -7.214  0.688   1.00 10.63 ? 229 LEU A CA  1 
ATOM   1834 C  C   . LEU A 1 228 ? 17.775  -7.333  0.809   1.00 10.14 ? 229 LEU A C   1 
ATOM   1835 O  O   . LEU A 1 228 ? 18.314  -8.339  1.316   1.00 9.84  ? 229 LEU A O   1 
ATOM   1836 C  CB  . LEU A 1 228 ? 15.724  -6.351  1.811   1.00 9.93  ? 229 LEU A CB  1 
ATOM   1837 C  CG  . LEU A 1 228 ? 14.352  -5.788  1.531   1.00 9.55  ? 229 LEU A CG  1 
ATOM   1838 C  CD1 . LEU A 1 228 ? 13.923  -5.148  2.835   1.00 10.41 ? 229 LEU A CD1 1 
ATOM   1839 C  CD2 . LEU A 1 228 ? 14.353  -4.738  0.409   1.00 11.21 ? 229 LEU A CD2 1 
ATOM   1840 N  N   . ASN A 1 229 ? 18.477  -6.311  0.348   1.00 10.56 ? 230 ASN A N   1 
ATOM   1841 C  CA  . ASN A 1 229 ? 19.923  -6.289  0.371   1.00 11.03 ? 230 ASN A CA  1 
ATOM   1842 C  C   . ASN A 1 229 ? 20.484  -5.134  1.273   1.00 10.83 ? 230 ASN A C   1 
ATOM   1843 O  O   . ASN A 1 229 ? 19.974  -3.991  1.192   1.00 10.42 ? 230 ASN A O   1 
ATOM   1844 C  CB  . ASN A 1 229 ? 20.451  -6.020  -1.058  1.00 12.96 ? 230 ASN A CB  1 
ATOM   1845 C  CG  . ASN A 1 229 ? 20.453  -7.237  -1.962  1.00 14.53 ? 230 ASN A CG  1 
ATOM   1846 O  OD1 . ASN A 1 229 ? 20.952  -7.102  -3.101  1.00 15.01 ? 230 ASN A OD1 1 
ATOM   1847 N  ND2 . ASN A 1 229 ? 19.824  -8.356  -1.572  1.00 13.95 ? 230 ASN A ND2 1 
ATOM   1848 N  N   . PHE A 1 230 ? 21.572  -5.405  2.026   1.00 10.82 ? 231 PHE A N   1 
ATOM   1849 C  CA  . PHE A 1 230 ? 22.344  -4.350  2.740   1.00 11.24 ? 231 PHE A CA  1 
ATOM   1850 C  C   . PHE A 1 230 ? 23.192  -3.558  1.743   1.00 13.36 ? 231 PHE A C   1 
ATOM   1851 O  O   . PHE A 1 230 ? 23.446  -2.347  1.945   1.00 12.49 ? 231 PHE A O   1 
ATOM   1852 C  CB  . PHE A 1 230 ? 23.355  -4.958  3.662   1.00 12.17 ? 231 PHE A CB  1 
ATOM   1853 C  CG  . PHE A 1 230 ? 22.783  -5.539  4.959   1.00 12.28 ? 231 PHE A CG  1 
ATOM   1854 C  CD1 . PHE A 1 230 ? 21.995  -4.721  5.844   1.00 11.50 ? 231 PHE A CD1 1 
ATOM   1855 C  CD2 . PHE A 1 230 ? 23.102  -6.851  5.330   1.00 11.32 ? 231 PHE A CD2 1 
ATOM   1856 C  CE1 . PHE A 1 230 ? 21.565  -5.222  7.102   1.00 11.48 ? 231 PHE A CE1 1 
ATOM   1857 C  CE2 . PHE A 1 230 ? 22.671  -7.353  6.566   1.00 10.33 ? 231 PHE A CE2 1 
ATOM   1858 C  CZ  . PHE A 1 230 ? 21.917  -6.570  7.463   1.00 10.39 ? 231 PHE A CZ  1 
ATOM   1859 N  N   . ASN A 1 231 ? 23.642  -4.256  0.703   1.00 12.53 ? 232 ASN A N   1 
ATOM   1860 C  CA  . ASN A 1 231 ? 24.563  -3.583  -0.271  1.00 13.69 ? 232 ASN A CA  1 
ATOM   1861 C  C   . ASN A 1 231 ? 23.816  -2.667  -1.229  1.00 14.65 ? 232 ASN A C   1 
ATOM   1862 O  O   . ASN A 1 231 ? 22.604  -2.786  -1.413  1.00 13.46 ? 232 ASN A O   1 
ATOM   1863 C  CB  . ASN A 1 231 ? 25.255  -4.660  -1.109  1.00 13.78 ? 232 ASN A CB  1 
ATOM   1864 C  CG  . ASN A 1 231 ? 24.254  -5.587  -1.740  1.00 14.02 ? 232 ASN A CG  1 
ATOM   1865 O  OD1 . ASN A 1 231 ? 23.682  -6.425  -1.045  1.00 15.74 ? 232 ASN A OD1 1 
ATOM   1866 N  ND2 . ASN A 1 231 ? 23.995  -5.429  -3.054  1.00 16.82 ? 232 ASN A ND2 1 
ATOM   1867 N  N   . GLY A 1 232 ? 24.567  -1.767  -1.890  1.00 14.98 ? 233 GLY A N   1 
ATOM   1868 C  CA  . GLY A 1 232 ? 24.040  -0.978  -3.010  1.00 14.97 ? 233 GLY A CA  1 
ATOM   1869 C  C   . GLY A 1 232 ? 23.974  -1.774  -4.307  1.00 16.10 ? 233 GLY A C   1 
ATOM   1870 O  O   . GLY A 1 232 ? 24.557  -2.839  -4.454  1.00 16.44 ? 233 GLY A O   1 
ATOM   1871 N  N   . GLU A 1 233 ? 23.254  -1.239  -5.277  1.00 15.77 ? 234 GLU A N   1 
ATOM   1872 C  CA  . GLU A 1 233 ? 23.152  -1.842  -6.601  1.00 16.73 ? 234 GLU A CA  1 
ATOM   1873 C  C   . GLU A 1 233 ? 24.543  -1.984  -7.230  1.00 16.47 ? 234 GLU A C   1 
ATOM   1874 O  O   . GLU A 1 233 ? 25.358  -1.114  -7.125  1.00 15.52 ? 234 GLU A O   1 
ATOM   1875 C  CB  . GLU A 1 233 ? 22.316  -0.891  -7.479  1.00 16.66 ? 234 GLU A CB  1 
ATOM   1876 C  CG  . GLU A 1 233 ? 22.019  -1.368  -8.894  1.00 18.72 ? 234 GLU A CG  1 
ATOM   1877 C  CD  . GLU A 1 233 ? 21.094  -0.433  -9.655  1.00 24.31 ? 234 GLU A CD  1 
ATOM   1878 O  OE1 . GLU A 1 233 ? 20.799  0.726   -9.214  1.00 24.85 ? 234 GLU A OE1 1 
ATOM   1879 O  OE2 . GLU A 1 233 ? 20.646  -0.863  -10.724 1.00 23.90 ? 234 GLU A OE2 1 
ATOM   1880 N  N   . GLY A 1 234 ? 24.768  -3.078  -7.918  1.00 18.30 ? 235 GLY A N   1 
ATOM   1881 C  CA  . GLY A 1 234 ? 26.086  -3.277  -8.510  1.00 22.02 ? 235 GLY A CA  1 
ATOM   1882 C  C   . GLY A 1 234 ? 27.217  -3.644  -7.576  1.00 23.84 ? 235 GLY A C   1 
ATOM   1883 O  O   . GLY A 1 234 ? 28.406  -3.558  -7.972  1.00 22.34 ? 235 GLY A O   1 
ATOM   1884 N  N   . GLU A 1 235 ? 26.848  -4.057  -6.354  1.00 21.18 ? 236 GLU A N   1 
ATOM   1885 C  CA  . GLU A 1 235 ? 27.754  -4.620  -5.357  1.00 20.71 ? 236 GLU A CA  1 
ATOM   1886 C  C   . GLU A 1 235 ? 27.384  -6.063  -5.025  1.00 20.39 ? 236 GLU A C   1 
ATOM   1887 O  O   . GLU A 1 235 ? 26.235  -6.519  -5.346  1.00 20.36 ? 236 GLU A O   1 
ATOM   1888 C  CB  . GLU A 1 235 ? 27.730  -3.770  -4.073  1.00 22.77 ? 236 GLU A CB  1 
ATOM   1889 C  CG  . GLU A 1 235 ? 28.317  -2.384  -4.207  1.00 22.93 ? 236 GLU A CG  1 
ATOM   1890 C  CD  . GLU A 1 235 ? 27.925  -1.462  -3.048  1.00 30.13 ? 236 GLU A CD  1 
ATOM   1891 O  OE1 . GLU A 1 235 ? 27.369  -1.930  -1.986  1.00 23.83 ? 236 GLU A OE1 1 
ATOM   1892 O  OE2 . GLU A 1 235 ? 28.149  -0.230  -3.177  1.00 31.26 ? 236 GLU A OE2 1 
ATOM   1893 N  N   . PRO A 1 236 ? 28.348  -6.822  -4.445  1.00 20.31 ? 237 PRO A N   1 
ATOM   1894 C  CA  . PRO A 1 236 ? 28.122  -8.231  -4.093  1.00 22.31 ? 237 PRO A CA  1 
ATOM   1895 C  C   . PRO A 1 236 ? 26.894  -8.271  -3.160  1.00 20.07 ? 237 PRO A C   1 
ATOM   1896 O  O   . PRO A 1 236 ? 26.744  -7.397  -2.333  1.00 20.78 ? 237 PRO A O   1 
ATOM   1897 C  CB  . PRO A 1 236 ? 29.401  -8.629  -3.329  1.00 25.09 ? 237 PRO A CB  1 
ATOM   1898 C  CG  . PRO A 1 236 ? 30.453  -7.699  -3.873  1.00 26.74 ? 237 PRO A CG  1 
ATOM   1899 C  CD  . PRO A 1 236 ? 29.745  -6.400  -4.203  1.00 23.93 ? 237 PRO A CD  1 
ATOM   1900 N  N   . GLU A 1 237 ? 26.047  -9.265  -3.345  1.00 19.80 ? 238 GLU A N   1 
ATOM   1901 C  CA  . GLU A 1 237 ? 24.800  -9.317  -2.644  1.00 17.75 ? 238 GLU A CA  1 
ATOM   1902 C  C   . GLU A 1 237 ? 25.047  -9.788  -1.230  1.00 17.35 ? 238 GLU A C   1 
ATOM   1903 O  O   . GLU A 1 237 ? 25.635  -10.844 -1.016  1.00 15.35 ? 238 GLU A O   1 
ATOM   1904 C  CB  . GLU A 1 237 ? 23.804  -10.270 -3.336  1.00 18.67 ? 238 GLU A CB  1 
ATOM   1905 C  CG  . GLU A 1 237 ? 22.458  -10.268 -2.631  1.00 21.66 ? 238 GLU A CG  1 
ATOM   1906 C  CD  . GLU A 1 237 ? 21.387  -11.034 -3.349  1.00 25.72 ? 238 GLU A CD  1 
ATOM   1907 O  OE1 . GLU A 1 237 ? 21.765  -12.024 -4.026  1.00 31.00 ? 238 GLU A OE1 1 
ATOM   1908 O  OE2 . GLU A 1 237 ? 20.189  -10.674 -3.241  1.00 18.17 ? 238 GLU A OE2 1 
ATOM   1909 N  N   A GLU A 1 238 ? 24.575  -8.988  -0.269  0.50 16.11 ? 239 GLU A N   1 
ATOM   1910 N  N   B GLU A 1 238 ? 24.580  -8.999  -0.257  0.50 16.28 ? 239 GLU A N   1 
ATOM   1911 C  CA  A GLU A 1 238 ? 24.510  -9.390  1.109   0.50 16.30 ? 239 GLU A CA  1 
ATOM   1912 C  CA  B GLU A 1 238 ? 24.533  -9.431  1.118   0.50 16.64 ? 239 GLU A CA  1 
ATOM   1913 C  C   A GLU A 1 238 ? 23.067  -9.214  1.557   0.50 14.82 ? 239 GLU A C   1 
ATOM   1914 C  C   B GLU A 1 238 ? 23.115  -9.219  1.631   0.50 14.94 ? 239 GLU A C   1 
ATOM   1915 O  O   A GLU A 1 238 ? 22.482  -8.114  1.507   0.50 14.17 ? 239 GLU A O   1 
ATOM   1916 O  O   B GLU A 1 238 ? 22.592  -8.096  1.691   0.50 14.57 ? 239 GLU A O   1 
ATOM   1917 C  CB  A GLU A 1 238 ? 25.485  -8.632  2.007   0.50 18.40 ? 239 GLU A CB  1 
ATOM   1918 C  CB  B GLU A 1 238 ? 25.593  -8.771  2.004   0.50 19.31 ? 239 GLU A CB  1 
ATOM   1919 C  CG  A GLU A 1 238 ? 25.617  -9.224  3.418   0.50 20.02 ? 239 GLU A CG  1 
ATOM   1920 C  CG  B GLU A 1 238 ? 25.459  -7.298  2.162   0.50 20.45 ? 239 GLU A CG  1 
ATOM   1921 C  CD  A GLU A 1 238 ? 26.036  -10.715 3.587   0.50 21.75 ? 239 GLU A CD  1 
ATOM   1922 C  CD  B GLU A 1 238 ? 26.720  -6.640  2.752   0.50 22.93 ? 239 GLU A CD  1 
ATOM   1923 O  OE1 A GLU A 1 238 ? 26.106  -11.570 2.665   0.50 21.96 ? 239 GLU A OE1 1 
ATOM   1924 O  OE1 B GLU A 1 238 ? 27.119  -6.945  3.907   0.50 23.95 ? 239 GLU A OE1 1 
ATOM   1925 O  OE2 A GLU A 1 238 ? 26.288  -11.063 4.750   0.50 23.81 ? 239 GLU A OE2 1 
ATOM   1926 O  OE2 B GLU A 1 238 ? 27.275  -5.788  2.066   0.50 20.96 ? 239 GLU A OE2 1 
ATOM   1927 N  N   . LEU A 1 239 ? 22.458  -10.345 1.887   1.00 13.20 ? 240 LEU A N   1 
ATOM   1928 C  CA  . LEU A 1 239 ? 21.065  -10.295 2.253   1.00 11.40 ? 240 LEU A CA  1 
ATOM   1929 C  C   . LEU A 1 239 ? 20.886  -9.458  3.512   1.00 9.71  ? 240 LEU A C   1 
ATOM   1930 O  O   . LEU A 1 239 ? 21.617  -9.615  4.493   1.00 9.47  ? 240 LEU A O   1 
ATOM   1931 C  CB  . LEU A 1 239 ? 20.527  -11.719 2.478   1.00 12.06 ? 240 LEU A CB  1 
ATOM   1932 C  CG  . LEU A 1 239 ? 20.506  -12.632 1.236   1.00 13.59 ? 240 LEU A CG  1 
ATOM   1933 C  CD1 . LEU A 1 239 ? 20.004  -14.028 1.676   1.00 15.33 ? 240 LEU A CD1 1 
ATOM   1934 C  CD2 . LEU A 1 239 ? 19.613  -12.018 0.155   1.00 14.44 ? 240 LEU A CD2 1 
ATOM   1935 N  N   . MET A 1 240 ? 19.788  -8.683  3.508   1.00 9.29  ? 241 MET A N   1 
ATOM   1936 C  CA  . MET A 1 240 ? 19.442  -7.852  4.717   1.00 9.27  ? 241 MET A CA  1 
ATOM   1937 C  C   . MET A 1 240 ? 18.699  -8.774  5.684   1.00 8.61  ? 241 MET A C   1 
ATOM   1938 O  O   . MET A 1 240 ? 17.496  -8.910  5.584   1.00 8.96  ? 241 MET A O   1 
ATOM   1939 C  CB  . MET A 1 240 ? 18.639  -6.573  4.324   1.00 10.21 ? 241 MET A CB  1 
ATOM   1940 C  CG  . MET A 1 240 ? 18.307  -5.625  5.570   1.00 8.96  ? 241 MET A CG  1 
ATOM   1941 S  SD  . MET A 1 240 ? 17.317  -4.264  4.937   1.00 11.36 ? 241 MET A SD  1 
ATOM   1942 C  CE  . MET A 1 240 ? 18.651  -3.234  4.264   1.00 9.19  ? 241 MET A CE  1 
ATOM   1943 N  N   . VAL A 1 241 ? 19.462  -9.416  6.592   1.00 7.98  ? 242 VAL A N   1 
ATOM   1944 C  CA  . VAL A 1 241 ? 18.865  -10.243 7.663   1.00 8.80  ? 242 VAL A CA  1 
ATOM   1945 C  C   . VAL A 1 241 ? 19.655  -9.972  8.942   1.00 9.04  ? 242 VAL A C   1 
ATOM   1946 O  O   . VAL A 1 241 ? 20.833  -9.535  8.884   1.00 8.70  ? 242 VAL A O   1 
ATOM   1947 C  CB  . VAL A 1 241 ? 18.898  -11.759 7.325   1.00 8.35  ? 242 VAL A CB  1 
ATOM   1948 C  CG1 . VAL A 1 241 ? 18.010  -12.029 6.098   1.00 9.29  ? 242 VAL A CG1 1 
ATOM   1949 C  CG2 . VAL A 1 241 ? 20.337  -12.242 7.177   1.00 7.92  ? 242 VAL A CG2 1 
ATOM   1950 N  N   . ASP A 1 242 ? 19.032  -10.292 10.075  1.00 8.44  ? 243 ASP A N   1 
ATOM   1951 C  CA  . ASP A 1 242 ? 19.720  -10.142 11.351  1.00 8.88  ? 243 ASP A CA  1 
ATOM   1952 C  C   . ASP A 1 242 ? 20.207  -8.710  11.605  1.00 8.20  ? 243 ASP A C   1 
ATOM   1953 O  O   . ASP A 1 242 ? 21.330  -8.493  12.129  1.00 9.50  ? 243 ASP A O   1 
ATOM   1954 C  CB  . ASP A 1 242 ? 20.812  -11.247 11.633  1.00 10.00 ? 243 ASP A CB  1 
ATOM   1955 C  CG  . ASP A 1 242 ? 20.224  -12.620 11.655  1.00 10.17 ? 243 ASP A CG  1 
ATOM   1956 O  OD1 . ASP A 1 242 ? 19.189  -12.839 12.345  1.00 11.11 ? 243 ASP A OD1 1 
ATOM   1957 O  OD2 . ASP A 1 242 ? 20.781  -13.546 10.976  1.00 10.65 ? 243 ASP A OD2 1 
ATOM   1958 N  N   . ASN A 1 243 ? 19.327  -7.748  11.324  1.00 7.47  ? 244 ASN A N   1 
ATOM   1959 C  CA  . ASN A 1 243 ? 19.699  -6.353  11.558  1.00 7.57  ? 244 ASN A CA  1 
ATOM   1960 C  C   . ASN A 1 243 ? 19.140  -5.889  12.934  1.00 7.72  ? 244 ASN A C   1 
ATOM   1961 O  O   . ASN A 1 243 ? 18.427  -4.873  13.023  1.00 8.86  ? 244 ASN A O   1 
ATOM   1962 C  CB  . ASN A 1 243 ? 19.174  -5.484  10.392  1.00 7.32  ? 244 ASN A CB  1 
ATOM   1963 C  CG  . ASN A 1 243 ? 17.697  -5.670  10.144  1.00 8.39  ? 244 ASN A CG  1 
ATOM   1964 O  OD1 . ASN A 1 243 ? 17.035  -6.473  10.804  1.00 8.04  ? 244 ASN A OD1 1 
ATOM   1965 N  ND2 . ASN A 1 243 ? 17.143  -4.846  9.210   1.00 8.45  ? 244 ASN A ND2 1 
ATOM   1966 N  N   . TRP A 1 244 ? 19.405  -6.690  13.943  1.00 7.57  ? 245 TRP A N   1 
ATOM   1967 C  CA  . TRP A 1 244 ? 18.889  -6.421  15.310  1.00 7.16  ? 245 TRP A CA  1 
ATOM   1968 C  C   . TRP A 1 244 ? 20.074  -6.356  16.232  1.00 7.43  ? 245 TRP A C   1 
ATOM   1969 O  O   . TRP A 1 244 ? 21.089  -7.056  16.082  1.00 7.97  ? 245 TRP A O   1 
ATOM   1970 C  CB  . TRP A 1 244 ? 17.914  -7.524  15.804  1.00 7.05  ? 245 TRP A CB  1 
ATOM   1971 C  CG  . TRP A 1 244 ? 18.393  -8.930  15.612  1.00 7.25  ? 245 TRP A CG  1 
ATOM   1972 C  CD1 . TRP A 1 244 ? 18.309  -9.710  14.444  1.00 6.99  ? 245 TRP A CD1 1 
ATOM   1973 C  CD2 . TRP A 1 244 ? 19.027  -9.792  16.613  1.00 7.52  ? 245 TRP A CD2 1 
ATOM   1974 N  NE1 . TRP A 1 244 ? 18.862  -10.965 14.665  1.00 7.53  ? 245 TRP A NE1 1 
ATOM   1975 C  CE2 . TRP A 1 244 ? 19.259  -11.078 15.961  1.00 7.82  ? 245 TRP A CE2 1 
ATOM   1976 C  CE3 . TRP A 1 244 ? 19.324  -9.647  17.986  1.00 7.69  ? 245 TRP A CE3 1 
ATOM   1977 C  CZ2 . TRP A 1 244 ? 19.862  -12.148 16.624  1.00 7.72  ? 245 TRP A CZ2 1 
ATOM   1978 C  CZ3 . TRP A 1 244 ? 19.939  -10.731 18.639  1.00 8.57  ? 245 TRP A CZ3 1 
ATOM   1979 C  CH2 . TRP A 1 244 ? 20.171  -11.952 17.977  1.00 8.60  ? 245 TRP A CH2 1 
ATOM   1980 N  N   . ARG A 1 245 ? 19.960  -5.484  17.232  1.00 7.21  ? 246 ARG A N   1 
ATOM   1981 C  CA  . ARG A 1 245 ? 20.954  -5.403  18.312  1.00 7.23  ? 246 ARG A CA  1 
ATOM   1982 C  C   . ARG A 1 245 ? 20.454  -6.282  19.456  1.00 7.85  ? 246 ARG A C   1 
ATOM   1983 O  O   . ARG A 1 245 ? 19.288  -6.262  19.811  1.00 8.49  ? 246 ARG A O   1 
ATOM   1984 C  CB  . ARG A 1 245 ? 21.038  -3.926  18.774  1.00 7.67  ? 246 ARG A CB  1 
ATOM   1985 C  CG  . ARG A 1 245 ? 22.190  -3.708  19.802  1.00 6.91  ? 246 ARG A CG  1 
ATOM   1986 C  CD  . ARG A 1 245 ? 22.078  -2.299  20.415  1.00 7.63  ? 246 ARG A CD  1 
ATOM   1987 N  NE  . ARG A 1 245 ? 23.335  -2.001  21.137  1.00 7.55  ? 246 ARG A NE  1 
ATOM   1988 C  CZ  . ARG A 1 245 ? 23.512  -1.003  22.021  1.00 8.07  ? 246 ARG A CZ  1 
ATOM   1989 N  NH1 . ARG A 1 245 ? 22.502  -0.202  22.432  1.00 7.51  ? 246 ARG A NH1 1 
ATOM   1990 N  NH2 . ARG A 1 245 ? 24.768  -0.805  22.505  1.00 8.18  ? 246 ARG A NH2 1 
ATOM   1991 N  N   . PRO A 1 246 ? 21.334  -7.079  20.049  1.00 8.76  ? 247 PRO A N   1 
ATOM   1992 C  CA  . PRO A 1 246 ? 20.950  -7.888  21.221  1.00 8.83  ? 247 PRO A CA  1 
ATOM   1993 C  C   . PRO A 1 246 ? 20.639  -7.049  22.441  1.00 8.96  ? 247 PRO A C   1 
ATOM   1994 O  O   . PRO A 1 246 ? 21.008  -5.847  22.531  1.00 8.20  ? 247 PRO A O   1 
ATOM   1995 C  CB  . PRO A 1 246 ? 22.209  -8.775  21.499  1.00 9.62  ? 247 PRO A CB  1 
ATOM   1996 C  CG  . PRO A 1 246 ? 23.204  -8.403  20.466  1.00 10.04 ? 247 PRO A CG  1 
ATOM   1997 C  CD  . PRO A 1 246 ? 22.756  -7.176  19.722  1.00 9.46  ? 247 PRO A CD  1 
ATOM   1998 N  N   . ALA A 1 247 ? 19.983  -7.716  23.384  1.00 8.57  ? 248 ALA A N   1 
ATOM   1999 C  CA  . ALA A 1 247 ? 19.639  -7.073  24.654  1.00 8.36  ? 248 ALA A CA  1 
ATOM   2000 C  C   . ALA A 1 247 ? 20.842  -6.548  25.395  1.00 8.41  ? 248 ALA A C   1 
ATOM   2001 O  O   . ALA A 1 247 ? 21.909  -7.217  25.468  1.00 8.30  ? 248 ALA A O   1 
ATOM   2002 C  CB  . ALA A 1 247 ? 18.766  -8.030  25.523  1.00 9.73  ? 248 ALA A CB  1 
ATOM   2003 N  N   . GLN A 1 248 ? 20.674  -5.333  25.940  1.00 7.97  ? 249 GLN A N   1 
ATOM   2004 C  CA  . GLN A 1 248 ? 21.701  -4.645  26.691  1.00 8.59  ? 249 GLN A CA  1 
ATOM   2005 C  C   . GLN A 1 248 ? 21.411  -4.643  28.181  1.00 8.89  ? 249 GLN A C   1 
ATOM   2006 O  O   . GLN A 1 248 ? 20.266  -4.839  28.595  1.00 8.70  ? 249 GLN A O   1 
ATOM   2007 C  CB  . GLN A 1 248 ? 21.824  -3.230  26.199  1.00 9.04  ? 249 GLN A CB  1 
ATOM   2008 C  CG  . GLN A 1 248 ? 22.191  -3.121  24.714  1.00 9.17  ? 249 GLN A CG  1 
ATOM   2009 C  CD  . GLN A 1 248 ? 23.504  -3.810  24.373  1.00 9.81  ? 249 GLN A CD  1 
ATOM   2010 O  OE1 . GLN A 1 248 ? 24.576  -3.470  24.956  1.00 10.66 ? 249 GLN A OE1 1 
ATOM   2011 N  NE2 . GLN A 1 248 ? 23.452  -4.786  23.432  1.00 10.57 ? 249 GLN A NE2 1 
ATOM   2012 N  N   . PRO A 1 249 ? 22.427  -4.287  28.995  1.00 9.83  ? 250 PRO A N   1 
ATOM   2013 C  CA  . PRO A 1 249 ? 22.203  -4.399  30.438  1.00 10.87 ? 250 PRO A CA  1 
ATOM   2014 C  C   . PRO A 1 249 ? 21.169  -3.388  30.952  1.00 9.83  ? 250 PRO A C   1 
ATOM   2015 O  O   . PRO A 1 249 ? 21.193  -2.205  30.518  1.00 9.72  ? 250 PRO A O   1 
ATOM   2016 C  CB  . PRO A 1 249 ? 23.546  -3.988  31.029  1.00 11.05 ? 250 PRO A CB  1 
ATOM   2017 C  CG  . PRO A 1 249 ? 24.550  -4.337  30.011  1.00 13.22 ? 250 PRO A CG  1 
ATOM   2018 C  CD  . PRO A 1 249 ? 23.847  -4.076  28.668  1.00 10.89 ? 250 PRO A CD  1 
ATOM   2019 N  N   . LEU A 1 250 ? 20.267  -3.872  31.833  1.00 10.34 ? 251 LEU A N   1 
ATOM   2020 C  CA  . LEU A 1 250 ? 19.165  -2.985  32.324  1.00 10.98 ? 251 LEU A CA  1 
ATOM   2021 C  C   . LEU A 1 250 ? 19.698  -1.875  33.220  1.00 11.47 ? 251 LEU A C   1 
ATOM   2022 O  O   . LEU A 1 250 ? 19.116  -0.781  33.255  1.00 10.02 ? 251 LEU A O   1 
ATOM   2023 C  CB  . LEU A 1 250 ? 18.090  -3.773  33.078  1.00 12.94 ? 251 LEU A CB  1 
ATOM   2024 C  CG  . LEU A 1 250 ? 16.802  -3.042  33.460  1.00 12.75 ? 251 LEU A CG  1 
ATOM   2025 C  CD1 . LEU A 1 250 ? 16.008  -2.533  32.253  1.00 14.66 ? 251 LEU A CD1 1 
ATOM   2026 C  CD2 . LEU A 1 250 ? 15.896  -3.943  34.321  1.00 16.63 ? 251 LEU A CD2 1 
ATOM   2027 N  N   . LYS A 1 251 ? 20.787  -2.166  33.974  1.00 11.31 ? 252 LYS A N   1 
ATOM   2028 C  CA  . LYS A 1 251 ? 21.414  -1.108  34.831  1.00 12.67 ? 252 LYS A CA  1 
ATOM   2029 C  C   . LYS A 1 251 ? 20.370  -0.587  35.820  1.00 13.14 ? 252 LYS A C   1 
ATOM   2030 O  O   . LYS A 1 251 ? 19.600  -1.402  36.354  1.00 14.20 ? 252 LYS A O   1 
ATOM   2031 C  CB  . LYS A 1 251 ? 22.134  -0.057  34.005  1.00 14.80 ? 252 LYS A CB  1 
ATOM   2032 C  CG  . LYS A 1 251 ? 23.402  -0.766  33.422  1.00 17.63 ? 252 LYS A CG  1 
ATOM   2033 C  CD  . LYS A 1 251 ? 24.269  0.167   32.678  1.00 18.41 ? 252 LYS A CD  1 
ATOM   2034 C  CE  . LYS A 1 251 ? 25.523  -0.601  32.264  1.00 21.60 ? 252 LYS A CE  1 
ATOM   2035 N  NZ  . LYS A 1 251 ? 26.300  0.281   31.338  1.00 20.54 ? 252 LYS A NZ  1 
ATOM   2036 N  N   . ASN A 1 252 ? 20.340  0.708   36.020  1.00 14.60 ? 253 ASN A N   1 
ATOM   2037 C  CA  . ASN A 1 252 ? 19.523  1.255   37.063  1.00 18.33 ? 253 ASN A CA  1 
ATOM   2038 C  C   . ASN A 1 252 ? 18.216  1.690   36.452  1.00 17.56 ? 253 ASN A C   1 
ATOM   2039 O  O   . ASN A 1 252 ? 17.939  2.948   36.493  1.00 21.17 ? 253 ASN A O   1 
ATOM   2040 C  CB  . ASN A 1 252 ? 20.185  2.519   37.646  1.00 20.99 ? 253 ASN A CB  1 
ATOM   2041 C  CG  . ASN A 1 252 ? 19.469  3.020   38.891  1.00 25.80 ? 253 ASN A CG  1 
ATOM   2042 O  OD1 . ASN A 1 252 ? 19.142  2.220   39.777  1.00 24.87 ? 253 ASN A OD1 1 
ATOM   2043 N  ND2 . ASN A 1 252 ? 19.182  4.347   38.951  1.00 29.13 ? 253 ASN A ND2 1 
ATOM   2044 N  N   . ARG A 1 253 ? 17.461  0.711   35.898  1.00 13.30 ? 254 ARG A N   1 
ATOM   2045 C  CA  . ARG A 1 253 ? 16.133  1.001   35.297  1.00 12.06 ? 254 ARG A CA  1 
ATOM   2046 C  C   . ARG A 1 253 ? 15.080  0.040   35.785  1.00 12.72 ? 254 ARG A C   1 
ATOM   2047 O  O   . ARG A 1 253 ? 15.408  -1.102  36.139  1.00 14.58 ? 254 ARG A O   1 
ATOM   2048 C  CB  . ARG A 1 253 ? 16.218  1.028   33.757  1.00 9.22  ? 254 ARG A CB  1 
ATOM   2049 C  CG  . ARG A 1 253 ? 17.086  2.223   33.294  1.00 10.27 ? 254 ARG A CG  1 
ATOM   2050 C  CD  . ARG A 1 253 ? 17.205  2.113   31.777  1.00 9.21  ? 254 ARG A CD  1 
ATOM   2051 N  NE  . ARG A 1 253 ? 18.055  0.942   31.350  1.00 8.42  ? 254 ARG A NE  1 
ATOM   2052 C  CZ  . ARG A 1 253 ? 18.334  0.690   30.078  1.00 7.75  ? 254 ARG A CZ  1 
ATOM   2053 N  NH1 . ARG A 1 253 ? 17.654  1.354   29.086  1.00 7.25  ? 254 ARG A NH1 1 
ATOM   2054 N  NH2 . ARG A 1 253 ? 19.141  -0.339  29.780  1.00 7.11  ? 254 ARG A NH2 1 
ATOM   2055 N  N   . GLN A 1 254 ? 13.838  0.531   35.875  1.00 12.66 ? 255 GLN A N   1 
ATOM   2056 C  CA  . GLN A 1 254 ? 12.663  -0.292  36.142  1.00 14.16 ? 255 GLN A CA  1 
ATOM   2057 C  C   . GLN A 1 254 ? 11.783  -0.305  34.869  1.00 13.16 ? 255 GLN A C   1 
ATOM   2058 O  O   . GLN A 1 254 ? 11.518  0.745   34.269  1.00 14.44 ? 255 GLN A O   1 
ATOM   2059 C  CB  . GLN A 1 254 ? 11.889  0.335   37.334  1.00 19.71 ? 255 GLN A CB  1 
ATOM   2060 C  CG  . GLN A 1 254 ? 12.636  0.076   38.649  1.00 25.85 ? 255 GLN A CG  1 
ATOM   2061 C  CD  . GLN A 1 254 ? 11.740  0.131   39.859  1.00 32.48 ? 255 GLN A CD  1 
ATOM   2062 O  OE1 . GLN A 1 254 ? 11.849  -0.696  40.800  1.00 39.41 ? 255 GLN A OE1 1 
ATOM   2063 N  NE2 . GLN A 1 254 ? 10.828  1.089   39.848  1.00 33.01 ? 255 GLN A NE2 1 
ATOM   2064 N  N   . ILE A 1 255 ? 11.333  -1.471  34.481  1.00 11.73 ? 256 ILE A N   1 
ATOM   2065 C  CA  . ILE A 1 255 ? 10.391  -1.578  33.390  1.00 10.86 ? 256 ILE A CA  1 
ATOM   2066 C  C   . ILE A 1 255 ? 9.004   -1.594  34.043  1.00 10.81 ? 256 ILE A C   1 
ATOM   2067 O  O   . ILE A 1 255 ? 8.746   -2.359  35.008  1.00 11.12 ? 256 ILE A O   1 
ATOM   2068 C  CB  . ILE A 1 255 ? 10.624  -2.866  32.585  1.00 11.34 ? 256 ILE A CB  1 
ATOM   2069 C  CG1 . ILE A 1 255 ? 12.031  -2.841  31.952  1.00 10.79 ? 256 ILE A CG1 1 
ATOM   2070 C  CG2 . ILE A 1 255 ? 9.554   -3.069  31.481  1.00 11.53 ? 256 ILE A CG2 1 
ATOM   2071 C  CD1 . ILE A 1 255 ? 12.281  -4.102  31.095  1.00 12.21 ? 256 ILE A CD1 1 
ATOM   2072 N  N   . LYS A 1 256 ? 8.133   -0.679  33.593  1.00 9.97  ? 257 LYS A N   1 
ATOM   2073 C  CA  . LYS A 1 256 ? 6.742   -0.633  34.129  1.00 10.45 ? 257 LYS A CA  1 
ATOM   2074 C  C   . LYS A 1 256 ? 5.757   -1.295  33.193  1.00 10.69 ? 257 LYS A C   1 
ATOM   2075 O  O   . LYS A 1 256 ? 5.909   -1.236  31.979  1.00 10.64 ? 257 LYS A O   1 
ATOM   2076 C  CB  . LYS A 1 256 ? 6.314   0.810   34.335  1.00 12.82 ? 257 LYS A CB  1 
ATOM   2077 C  CG  . LYS A 1 256 ? 7.325   1.680   35.053  1.00 20.06 ? 257 LYS A CG  1 
ATOM   2078 C  CD  . LYS A 1 256 ? 7.480   1.331   36.499  1.00 27.29 ? 257 LYS A CD  1 
ATOM   2079 C  CE  . LYS A 1 256 ? 7.769   2.634   37.272  1.00 36.41 ? 257 LYS A CE  1 
ATOM   2080 N  NZ  . LYS A 1 256 ? 8.465   2.361   38.580  1.00 41.74 ? 257 LYS A NZ  1 
ATOM   2081 N  N   . ALA A 1 257 ? 4.771   -1.984  33.757  1.00 9.65  ? 258 ALA A N   1 
ATOM   2082 C  CA  . ALA A 1 257 ? 3.644   -2.573  32.978  1.00 9.81  ? 258 ALA A CA  1 
ATOM   2083 C  C   . ALA A 1 257 ? 2.395   -1.711  33.084  1.00 9.99  ? 258 ALA A C   1 
ATOM   2084 O  O   . ALA A 1 257 ? 2.073   -1.205  34.151  1.00 9.88  ? 258 ALA A O   1 
ATOM   2085 C  CB  . ALA A 1 257 ? 3.342   -4.000  33.399  1.00 11.04 ? 258 ALA A CB  1 
ATOM   2086 N  N   . SER A 1 258 ? 1.653   -1.628  31.982  1.00 8.77  ? 259 SER A N   1 
ATOM   2087 C  CA  . SER A 1 258 ? 0.424   -0.840  31.954  1.00 10.83 ? 259 SER A CA  1 
ATOM   2088 C  C   . SER A 1 258 ? -0.739  -1.699  32.403  1.00 11.78 ? 259 SER A C   1 
ATOM   2089 O  O   . SER A 1 258 ? -1.831  -1.147  32.609  1.00 13.87 ? 259 SER A O   1 
ATOM   2090 C  CB  . SER A 1 258 ? 0.166   -0.367  30.524  1.00 10.44 ? 259 SER A CB  1 
ATOM   2091 O  OG  . SER A 1 258 ? -0.288  -1.438  29.713  1.00 10.75 ? 259 SER A OG  1 
ATOM   2092 N  N   . PHE A 1 259 ? -0.483  -2.983  32.675  1.00 13.51 ? 260 PHE A N   1 
ATOM   2093 C  CA  . PHE A 1 259 ? -1.578  -3.967  32.857  1.00 15.34 ? 260 PHE A CA  1 
ATOM   2094 C  C   . PHE A 1 259 ? -1.259  -4.886  34.046  1.00 21.00 ? 260 PHE A C   1 
ATOM   2095 O  O   . PHE A 1 259 ? -0.077  -5.020  34.480  1.00 18.26 ? 260 PHE A O   1 
ATOM   2096 C  CB  . PHE A 1 259 ? -1.761  -4.805  31.565  1.00 16.05 ? 260 PHE A CB  1 
ATOM   2097 C  CG  . PHE A 1 259 ? -0.494  -5.560  31.169  1.00 16.20 ? 260 PHE A CG  1 
ATOM   2098 C  CD1 . PHE A 1 259 ? 0.530   -4.910  30.432  1.00 14.90 ? 260 PHE A CD1 1 
ATOM   2099 C  CD2 . PHE A 1 259 ? -0.243  -6.844  31.672  1.00 17.40 ? 260 PHE A CD2 1 
ATOM   2100 C  CE1 . PHE A 1 259 ? 1.719   -5.571  30.135  1.00 15.74 ? 260 PHE A CE1 1 
ATOM   2101 C  CE2 . PHE A 1 259 ? 0.934   -7.493  31.390  1.00 18.38 ? 260 PHE A CE2 1 
ATOM   2102 C  CZ  . PHE A 1 259 ? 1.944   -6.850  30.626  1.00 18.23 ? 260 PHE A CZ  1 
ATOM   2103 N  N   . LYS A 1 260 ? -2.364  -5.476  34.526  1.00 27.28 ? 261 LYS A N   1 
ATOM   2104 C  CA  . LYS A 1 260 ? -2.533  -6.635  35.480  1.00 35.17 ? 261 LYS A CA  1 
ATOM   2105 C  C   . LYS A 1 260 ? -2.236  -6.419  36.959  1.00 44.85 ? 261 LYS A C   1 
ATOM   2106 O  O   . LYS A 1 260 ? -1.353  -7.050  37.554  1.00 54.92 ? 261 LYS A O   1 
ATOM   2107 C  CB  . LYS A 1 260 ? -1.976  -7.968  34.943  1.00 38.41 ? 261 LYS A CB  1 
ATOM   2108 C  CG  . LYS A 1 260 ? -2.789  -8.544  33.780  1.00 41.34 ? 261 LYS A CG  1 
ATOM   2109 C  CD  . LYS A 1 260 ? -2.211  -9.840  33.209  1.00 45.84 ? 261 LYS A CD  1 
ATOM   2110 C  CE  . LYS A 1 260 ? -0.714  -9.957  33.516  1.00 48.58 ? 261 LYS A CE  1 
ATOM   2111 N  NZ  . LYS A 1 260 ? 0.030   -10.860 32.595  1.00 46.32 ? 261 LYS A NZ  1 
ATOM   2112 O  OXT . LYS A 1 260 ? -2.923  -5.586  37.584  1.00 50.95 ? 261 LYS A OXT 1 
HETATM 2113 ZN ZN  . ZN  B 2 .   ? 14.397  0.189   15.266  1.00 7.26  ? 301 ZN  A ZN  1 
HETATM 2114 F  F20 A V14 C 3 .   ? 14.412  4.917   14.180  0.50 7.99  ? 302 V14 A F20 1 
HETATM 2115 F  F20 B V14 C 3 .   ? 16.726  2.411   14.395  0.50 18.46 ? 302 V14 A F20 1 
HETATM 2116 C  C5  A V14 C 3 .   ? 15.717  5.004   14.398  0.50 7.10  ? 302 V14 A C5  1 
HETATM 2117 C  C5  B V14 C 3 .   ? 16.297  3.704   14.637  0.50 16.56 ? 302 V14 A C5  1 
HETATM 2118 C  C4  A V14 C 3 .   ? 16.320  4.099   15.280  0.50 6.46  ? 302 V14 A C4  1 
HETATM 2119 C  C4  B V14 C 3 .   ? 15.538  4.045   15.744  0.50 14.68 ? 302 V14 A C4  1 
HETATM 2120 S  S7  A V14 C 3 .   ? 15.450  2.888   16.273  0.50 5.65  ? 302 V14 A S7  1 
HETATM 2121 S  S7  B V14 C 3 .   ? 15.118  2.794   16.914  0.50 11.22 ? 302 V14 A S7  1 
HETATM 2122 O  O9  A V14 C 3 .   ? 13.914  3.042   16.315  0.50 5.48  ? 302 V14 A O9  1 
HETATM 2123 O  O9  B V14 C 3 .   ? 13.631  2.749   17.120  0.50 12.64 ? 302 V14 A O9  1 
HETATM 2124 N  N10 A V14 C 3 .   ? 15.840  1.286   15.837  0.50 5.55  ? 302 V14 A N10 1 
HETATM 2125 N  N10 B V14 C 3 .   ? 15.526  1.159   16.610  0.50 10.70 ? 302 V14 A N10 1 
HETATM 2126 O  O8  A V14 C 3 .   ? 16.016  3.126   17.645  0.50 5.30  ? 302 V14 A O8  1 
HETATM 2127 O  O8  B V14 C 3 .   ? 15.722  3.054   18.290  0.50 11.86 ? 302 V14 A O8  1 
HETATM 2128 C  C3  A V14 C 3 .   ? 17.680  4.195   15.456  0.50 6.83  ? 302 V14 A C3  1 
HETATM 2129 C  C3  B V14 C 3 .   ? 15.047  5.332   16.001  0.50 15.26 ? 302 V14 A C3  1 
HETATM 2130 F  F12 A V14 C 3 .   ? 18.317  3.303   16.242  0.50 6.90  ? 302 V14 A F12 1 
HETATM 2131 F  F12 B V14 C 3 .   ? 14.307  5.592   17.119  0.50 17.55 ? 302 V14 A F12 1 
HETATM 2132 C  C2  A V14 C 3 .   ? 18.438  5.139   14.791  0.50 7.54  ? 302 V14 A C2  1 
HETATM 2133 C  C2  B V14 C 3 .   ? 15.333  6.365   15.164  0.50 18.16 ? 302 V14 A C2  1 
HETATM 2134 F  F13 A V14 C 3 .   ? 19.786  5.175   15.024  0.50 7.83  ? 302 V14 A F13 1 
HETATM 2135 F  F13 B V14 C 3 .   ? 14.883  7.642   15.384  0.50 17.57 ? 302 V14 A F13 1 
HETATM 2136 C  C6  A V14 C 3 .   ? 16.453  5.964   13.698  0.50 7.46  ? 302 V14 A C6  1 
HETATM 2137 C  C6  B V14 C 3 .   ? 16.571  4.781   13.777  0.50 18.14 ? 302 V14 A C6  1 
HETATM 2138 C  C1  A V14 C 3 .   ? 17.843  6.033   13.901  0.50 7.72  ? 302 V14 A C1  1 
HETATM 2139 C  C1  B V14 C 3 .   ? 16.095  6.073   14.056  0.50 20.26 ? 302 V14 A C1  1 
HETATM 2140 S  S11 A V14 C 3 .   ? 19.015  7.176   13.143  0.50 9.03  ? 302 V14 A S11 1 
HETATM 2141 S  S11 B V14 C 3 .   ? 16.410  7.502   13.026  0.50 26.36 ? 302 V14 A S11 1 
HETATM 2142 O  O16 A V14 C 3 .   ? 19.521  8.066   14.268  0.50 8.86  ? 302 V14 A O16 1 
HETATM 2143 O  O16 B V14 C 3 .   ? 16.823  7.012   11.632  0.50 26.16 ? 302 V14 A O16 1 
HETATM 2144 O  O17 A V14 C 3 .   ? 18.257  8.113   12.204  0.50 9.01  ? 302 V14 A O17 1 
HETATM 2145 O  O17 B V14 C 3 .   ? 17.787  8.059   13.519  0.50 27.65 ? 302 V14 A O17 1 
HETATM 2146 C  C15 A V14 C 3 .   ? 20.309  6.327   12.203  0.50 9.51  ? 302 V14 A C15 1 
HETATM 2147 C  C15 B V14 C 3 .   ? 15.264  8.915   12.850  0.50 25.73 ? 302 V14 A C15 1 
HETATM 2148 C  C18 A V14 C 3 .   ? 19.692  5.569   10.998  0.50 10.10 ? 302 V14 A C18 1 
HETATM 2149 C  C18 B V14 C 3 .   ? 14.150  8.558   11.896  0.50 24.58 ? 302 V14 A C18 1 
HETATM 2150 O  O21 A V14 C 3 .   ? 18.336  5.187   11.118  0.50 10.75 ? 302 V14 A O21 1 
HETATM 2151 O  O21 B V14 C 3 .   ? 14.482  8.747   10.550  0.50 24.73 ? 302 V14 A O21 1 
HETATM 2152 N  N19 A V14 C 3 .   ? 15.736  6.818   12.785  0.50 7.22  ? 302 V14 A N19 1 
HETATM 2153 N  N19 B V14 C 3 .   ? 17.332  4.610   12.628  0.50 16.39 ? 302 V14 A N19 1 
HETATM 2154 C  C14 A V14 C 3 .   ? 14.693  7.665   13.254  0.50 7.39  ? 302 V14 A C14 1 
HETATM 2155 C  C14 B V14 C 3 .   ? 17.636  3.355   12.017  0.50 14.99 ? 302 V14 A C14 1 
HETATM 2156 C  C28 A V14 C 3 .   ? 14.983  8.124   14.681  0.50 7.76  ? 302 V14 A C28 1 
HETATM 2157 C  C28 B V14 C 3 .   ? 16.341  3.149   11.200  0.50 13.11 ? 302 V14 A C28 1 
HETATM 2158 C  C27 A V14 C 3 .   ? 16.229  9.013   14.814  0.50 8.34  ? 302 V14 A C27 1 
HETATM 2159 C  C27 B V14 C 3 .   ? 16.248  1.935   10.371  0.50 12.71 ? 302 V14 A C27 1 
HETATM 2160 C  C26 A V14 C 3 .   ? 15.946  10.477  14.438  0.50 8.95  ? 302 V14 A C26 1 
HETATM 2161 C  C26 B V14 C 3 .   ? 16.769  0.961   11.412  0.50 11.87 ? 302 V14 A C26 1 
HETATM 2162 C  C25 A V14 C 3 .   ? 14.504  10.974  14.387  0.50 8.64  ? 302 V14 A C25 1 
HETATM 2163 C  C25 B V14 C 3 .   ? 18.245  0.788   11.178  0.50 11.57 ? 302 V14 A C25 1 
HETATM 2164 C  C24 A V14 C 3 .   ? 13.948  11.036  12.975  0.50 8.34  ? 302 V14 A C24 1 
HETATM 2165 C  C24 B V14 C 3 .   ? 18.824  1.837   10.229  0.50 13.25 ? 302 V14 A C24 1 
HETATM 2166 C  C23 A V14 C 3 .   ? 13.345  9.679   12.533  0.50 8.50  ? 302 V14 A C23 1 
HETATM 2167 C  C23 B V14 C 3 .   ? 19.842  2.686   10.998  0.50 12.64 ? 302 V14 A C23 1 
HETATM 2168 C  C22 A V14 C 3 .   ? 14.520  8.766   12.220  0.50 7.54  ? 302 V14 A C22 1 
HETATM 2169 C  C22 B V14 C 3 .   ? 18.962  3.827   11.370  0.50 14.60 ? 302 V14 A C22 1 
HETATM 2170 O  O   . HOH D 4 .   ? 19.870  -2.309  15.841  1.00 6.74  ? 401 HOH A O   1 
HETATM 2171 O  O   . HOH D 4 .   ? 9.124   4.660   30.850  1.00 10.69 ? 402 HOH A O   1 
HETATM 2172 O  O   . HOH D 4 .   ? 16.598  -11.604 18.102  1.00 6.84  ? 403 HOH A O   1 
HETATM 2173 O  O   . HOH D 4 .   ? 17.383  -13.949 24.403  1.00 10.42 ? 404 HOH A O   1 
HETATM 2174 O  O   . HOH D 4 .   ? 4.006   -6.549  20.485  1.00 8.25  ? 405 HOH A O   1 
HETATM 2175 O  O   . HOH D 4 .   ? 10.502  10.553  25.456  1.00 10.15 ? 406 HOH A O   1 
HETATM 2176 O  O   . HOH D 4 .   ? 22.298  0.373   29.432  1.00 10.07 ? 407 HOH A O   1 
HETATM 2177 O  O   . HOH D 4 .   ? 24.609  7.045   29.855  1.00 14.07 ? 408 HOH A O   1 
HETATM 2178 O  O   . HOH D 4 .   ? 26.066  -3.086  21.093  1.00 11.36 ? 409 HOH A O   1 
HETATM 2179 O  O   . HOH D 4 .   ? 17.498  -9.223  20.878  1.00 8.90  ? 410 HOH A O   1 
HETATM 2180 O  O   . HOH D 4 .   ? 19.046  -10.442 22.886  1.00 9.97  ? 411 HOH A O   1 
HETATM 2181 O  O   . HOH D 4 .   ? 17.737  -11.302 25.312  1.00 8.21  ? 412 HOH A O   1 
HETATM 2182 O  O   . HOH D 4 .   ? 11.595  -6.017  34.119  1.00 14.24 ? 413 HOH A O   1 
HETATM 2183 O  O   . HOH D 4 .   ? 29.757  -1.980  21.141  1.00 14.02 ? 414 HOH A O   1 
HETATM 2184 O  O   . HOH D 4 .   ? 21.225  0.740   -4.763  1.00 14.03 ? 415 HOH A O   1 
HETATM 2185 O  O   . HOH D 4 .   ? -2.975  0.945   3.948   1.00 12.02 ? 416 HOH A O   1 
HETATM 2186 O  O   . HOH D 4 .   ? 6.829   -14.758 29.027  1.00 19.33 ? 417 HOH A O   1 
HETATM 2187 O  O   . HOH D 4 .   ? -5.346  4.626   21.014  1.00 21.17 ? 418 HOH A O   1 
HETATM 2188 O  O   . HOH D 4 .   ? 12.425  -1.951  7.857   1.00 10.17 ? 419 HOH A O   1 
HETATM 2189 O  O   . HOH D 4 .   ? 14.232  7.539   6.090   1.00 17.93 ? 420 HOH A O   1 
HETATM 2190 O  O   . HOH D 4 .   ? 26.437  8.943   20.207  1.00 15.18 ? 421 HOH A O   1 
HETATM 2191 O  O   . HOH D 4 .   ? 19.856  -9.370  29.141  1.00 17.98 ? 422 HOH A O   1 
HETATM 2192 O  O   . HOH D 4 .   ? 28.718  8.048   21.656  1.00 12.83 ? 423 HOH A O   1 
HETATM 2193 O  O   . HOH D 4 .   ? 25.372  -0.753  29.029  1.00 21.05 ? 424 HOH A O   1 
HETATM 2194 O  O   . HOH D 4 .   ? 13.108  -13.664 11.386  1.00 7.98  ? 425 HOH A O   1 
HETATM 2195 O  O   . HOH D 4 .   ? -0.646  -5.328  23.667  1.00 10.32 ? 426 HOH A O   1 
HETATM 2196 O  O   . HOH D 4 .   ? 0.250   -11.093 -1.838  1.00 15.95 ? 427 HOH A O   1 
HETATM 2197 O  O   . HOH D 4 .   ? 19.090  -15.558 25.694  1.00 19.27 ? 428 HOH A O   1 
HETATM 2198 O  O   . HOH D 4 .   ? 14.868  -2.804  -6.369  1.00 21.71 ? 429 HOH A O   1 
HETATM 2199 O  O   . HOH D 4 .   ? 18.598  -6.813  29.258  1.00 10.06 ? 430 HOH A O   1 
HETATM 2200 O  O   . HOH D 4 .   ? 11.859  7.866   29.029  1.00 17.43 ? 431 HOH A O   1 
HETATM 2201 O  O   . HOH D 4 .   ? -3.024  10.668  20.265  1.00 19.29 ? 432 HOH A O   1 
HETATM 2202 O  O   . HOH D 4 .   ? 7.393   12.196  27.965  1.00 12.06 ? 433 HOH A O   1 
HETATM 2203 O  O   . HOH D 4 .   ? 8.121   -14.973 26.577  1.00 12.34 ? 434 HOH A O   1 
HETATM 2204 O  O   . HOH D 4 .   ? 11.238  17.504  12.168  1.00 18.42 ? 435 HOH A O   1 
HETATM 2205 O  O   . HOH D 4 .   ? 5.003   17.899  23.593  1.00 19.61 ? 436 HOH A O   1 
HETATM 2206 O  O   . HOH D 4 .   ? 6.294   -19.439 17.516  1.00 14.64 ? 437 HOH A O   1 
HETATM 2207 O  O   . HOH D 4 .   ? 16.361  -10.106 32.136  1.00 17.07 ? 438 HOH A O   1 
HETATM 2208 O  O   . HOH D 4 .   ? 10.657  -16.350 17.277  1.00 19.05 ? 439 HOH A O   1 
HETATM 2209 O  O   . HOH D 4 .   ? -1.391  3.300   30.190  1.00 19.73 ? 440 HOH A O   1 
HETATM 2210 O  O   . HOH D 4 .   ? 0.813   12.665  26.728  1.00 12.65 ? 441 HOH A O   1 
HETATM 2211 O  O   . HOH D 4 .   ? 7.376   16.120  27.217  1.00 18.50 ? 442 HOH A O   1 
HETATM 2212 O  O   . HOH D 4 .   ? -1.973  -9.844  14.012  1.00 18.22 ? 443 HOH A O   1 
HETATM 2213 O  O   . HOH D 4 .   ? 3.457   -19.748 17.409  1.00 23.57 ? 444 HOH A O   1 
HETATM 2214 O  O   . HOH D 4 .   ? -1.128  5.714   -3.038  1.00 22.54 ? 445 HOH A O   1 
HETATM 2215 O  O   . HOH D 4 .   ? 25.402  -1.588  26.591  1.00 18.11 ? 446 HOH A O   1 
HETATM 2216 O  O   . HOH D 4 .   ? -9.539  -5.231  22.476  1.00 23.71 ? 447 HOH A O   1 
HETATM 2217 O  O   . HOH D 4 .   ? 4.164   -12.077 26.270  1.00 17.67 ? 448 HOH A O   1 
HETATM 2218 O  O   . HOH D 4 .   ? 11.963  -3.884  36.007  1.00 15.68 ? 449 HOH A O   1 
HETATM 2219 O  O   . HOH D 4 .   ? 14.075  -18.287 19.571  1.00 22.93 ? 450 HOH A O   1 
HETATM 2220 O  O   . HOH D 4 .   ? 7.324   -20.748 11.280  1.00 33.88 ? 451 HOH A O   1 
HETATM 2221 O  O   . HOH D 4 .   ? 8.193   -15.457 16.961  1.00 13.99 ? 452 HOH A O   1 
HETATM 2222 O  O   . HOH D 4 .   ? -7.994  -4.074  24.562  1.00 23.89 ? 453 HOH A O   1 
HETATM 2223 O  O   . HOH D 4 .   ? 10.118  -17.973 7.340   1.00 29.33 ? 454 HOH A O   1 
HETATM 2224 O  O   . HOH D 4 .   ? 14.205  -12.989 31.642  1.00 17.72 ? 455 HOH A O   1 
HETATM 2225 O  O   . HOH D 4 .   ? 5.681   -20.047 13.163  1.00 22.48 ? 456 HOH A O   1 
HETATM 2226 O  O   . HOH D 4 .   ? -1.742  -4.188  2.838   1.00 19.31 ? 457 HOH A O   1 
HETATM 2227 O  O   . HOH D 4 .   ? 8.788   14.545  29.184  1.00 18.02 ? 458 HOH A O   1 
HETATM 2228 O  O   . HOH D 4 .   ? -6.928  7.515   19.125  1.00 25.97 ? 459 HOH A O   1 
HETATM 2229 O  O   . HOH D 4 .   ? 20.939  -12.393 22.314  1.00 16.40 ? 460 HOH A O   1 
HETATM 2230 O  O   . HOH D 4 .   ? 14.338  -3.346  37.504  1.00 16.43 ? 461 HOH A O   1 
HETATM 2231 O  O   . HOH D 4 .   ? -3.847  -5.985  9.099   1.00 16.07 ? 462 HOH A O   1 
HETATM 2232 O  O   . HOH D 4 .   ? 9.960   -13.335 34.204  1.00 21.10 ? 463 HOH A O   1 
HETATM 2233 O  O   . HOH D 4 .   ? 4.975   -10.471 24.442  1.00 13.99 ? 464 HOH A O   1 
HETATM 2234 O  O   . HOH D 4 .   ? 20.598  12.707  23.408  1.00 20.04 ? 465 HOH A O   1 
HETATM 2235 O  O   . HOH D 4 .   ? 18.581  -1.676  11.520  1.00 18.44 ? 466 HOH A O   1 
HETATM 2236 O  O   . HOH D 4 .   ? 3.042   -18.678 7.986   1.00 13.70 ? 467 HOH A O   1 
HETATM 2237 O  O   . HOH D 4 .   ? 19.708  -11.064 27.105  1.00 18.92 ? 468 HOH A O   1 
HETATM 2238 O  O   . HOH D 4 .   ? 8.488   9.790   28.800  1.00 22.00 ? 469 HOH A O   1 
HETATM 2239 O  O   . HOH D 4 .   ? 22.587  10.574  24.193  1.00 17.37 ? 470 HOH A O   1 
HETATM 2240 O  O   . HOH D 4 .   ? -5.817  -2.151  25.186  1.00 18.30 ? 471 HOH A O   1 
HETATM 2241 O  O   . HOH D 4 .   ? 3.782   -14.563 21.901  1.00 20.08 ? 472 HOH A O   1 
HETATM 2242 O  O   . HOH D 4 .   ? -2.378  1.744   32.194  1.00 22.12 ? 473 HOH A O   1 
HETATM 2243 O  O   . HOH D 4 .   ? 25.632  -5.051  7.817   1.00 27.09 ? 474 HOH A O   1 
HETATM 2244 O  O   . HOH D 4 .   ? 11.678  -8.403  -1.195  1.00 18.98 ? 475 HOH A O   1 
HETATM 2245 O  O   . HOH D 4 .   ? -4.572  11.390  13.471  1.00 26.81 ? 476 HOH A O   1 
HETATM 2246 O  O   . HOH D 4 .   ? -1.155  -16.570 13.619  1.00 20.15 ? 477 HOH A O   1 
HETATM 2247 O  O   . HOH D 4 .   ? -2.124  -1.268  6.813   1.00 16.44 ? 478 HOH A O   1 
HETATM 2248 O  O   . HOH D 4 .   ? 22.996  -12.439 20.462  1.00 22.90 ? 479 HOH A O   1 
HETATM 2249 O  O   . HOH D 4 .   ? -5.624  -0.508  14.570  1.00 20.26 ? 480 HOH A O   1 
HETATM 2250 O  O   . HOH D 4 .   ? 26.110  -5.743  22.374  1.00 22.18 ? 481 HOH A O   1 
HETATM 2251 O  O   . HOH D 4 .   ? 8.332   5.258   -6.786  1.00 19.77 ? 482 HOH A O   1 
HETATM 2252 O  O   . HOH D 4 .   ? 8.086   15.358  31.848  1.00 21.73 ? 483 HOH A O   1 
HETATM 2253 O  O   . HOH D 4 .   ? 13.956  -13.844 38.678  1.00 23.38 ? 484 HOH A O   1 
HETATM 2254 O  O   . HOH D 4 .   ? 13.307  -17.541 21.909  1.00 25.65 ? 485 HOH A O   1 
HETATM 2255 O  O   . HOH D 4 .   ? 22.258  -9.875  25.154  1.00 17.85 ? 486 HOH A O   1 
HETATM 2256 O  O   . HOH D 4 .   ? 13.692  -6.671  32.619  1.00 14.12 ? 487 HOH A O   1 
HETATM 2257 O  O   . HOH D 4 .   ? 5.402   10.684  -2.323  1.00 23.50 ? 488 HOH A O   1 
HETATM 2258 O  O   . HOH D 4 .   ? 21.136  -0.103  39.619  1.00 35.03 ? 489 HOH A O   1 
HETATM 2259 O  O   . HOH D 4 .   ? 6.427   -16.883 18.779  1.00 19.61 ? 490 HOH A O   1 
HETATM 2260 O  O   . HOH D 4 .   ? 16.829  -6.479  31.181  1.00 20.98 ? 491 HOH A O   1 
HETATM 2261 O  O   . HOH D 4 .   ? 13.683  -6.922  -2.336  1.00 23.41 ? 492 HOH A O   1 
HETATM 2262 O  O   . HOH D 4 .   ? 13.040  -20.289 10.343  1.00 18.12 ? 493 HOH A O   1 
HETATM 2263 O  O   . HOH D 4 .   ? 2.763   -1.816  -2.506  1.00 25.25 ? 494 HOH A O   1 
HETATM 2264 O  O   . HOH D 4 .   ? 1.252   -2.142  41.308  1.00 24.31 ? 495 HOH A O   1 
HETATM 2265 O  O   . HOH D 4 .   ? 7.772   -16.757 14.841  1.00 17.07 ? 496 HOH A O   1 
HETATM 2266 O  O   . HOH D 4 .   ? 11.299  3.388   39.064  1.00 25.47 ? 497 HOH A O   1 
HETATM 2267 O  O   . HOH D 4 .   ? 7.480   -19.329 15.084  1.00 17.25 ? 498 HOH A O   1 
HETATM 2268 O  O   . HOH D 4 .   ? 21.391  2.547   -6.810  1.00 23.19 ? 499 HOH A O   1 
HETATM 2269 O  O   . HOH D 4 .   ? 2.984   12.471  11.185  1.00 21.57 ? 500 HOH A O   1 
HETATM 2270 O  O   . HOH D 4 .   ? 2.348   5.246   -3.651  1.00 24.79 ? 501 HOH A O   1 
HETATM 2271 O  O   . HOH D 4 .   ? 1.646   11.992  8.860   1.00 14.66 ? 502 HOH A O   1 
HETATM 2272 O  O   . HOH D 4 .   ? 8.345   -16.453 31.980  1.00 25.51 ? 503 HOH A O   1 
HETATM 2273 O  O   . HOH D 4 .   ? 23.985  -12.870 1.403   1.00 22.60 ? 504 HOH A O   1 
HETATM 2274 O  O   . HOH D 4 .   ? 23.687  -9.575  9.557   1.00 21.80 ? 505 HOH A O   1 
HETATM 2275 O  O   . HOH D 4 .   ? 0.569   10.339  30.019  1.00 18.58 ? 506 HOH A O   1 
HETATM 2276 O  O   . HOH D 4 .   ? 11.235  17.658  29.671  1.00 23.47 ? 507 HOH A O   1 
HETATM 2277 O  O   . HOH D 4 .   ? 18.672  9.364   -5.294  1.00 18.63 ? 508 HOH A O   1 
HETATM 2278 O  O   . HOH D 4 .   ? -2.342  -11.359 11.334  1.00 20.27 ? 509 HOH A O   1 
HETATM 2279 O  O   . HOH D 4 .   ? 23.905  -11.637 8.049   1.00 26.61 ? 510 HOH A O   1 
HETATM 2280 O  O   . HOH D 4 .   ? 25.910  -11.375 -5.689  1.00 26.24 ? 511 HOH A O   1 
HETATM 2281 O  O   . HOH D 4 .   ? 28.498  -6.118  -0.551  1.00 28.66 ? 512 HOH A O   1 
HETATM 2282 O  O   . HOH D 4 .   ? 23.133  14.263  22.665  1.00 24.64 ? 513 HOH A O   1 
HETATM 2283 O  O   . HOH D 4 .   ? 9.478   12.455  0.699   1.00 22.63 ? 514 HOH A O   1 
HETATM 2284 O  O   . HOH D 4 .   ? 2.104   -19.246 5.458   1.00 28.29 ? 515 HOH A O   1 
HETATM 2285 O  O   . HOH D 4 .   ? -5.192  5.376   15.398  1.00 23.16 ? 516 HOH A O   1 
HETATM 2286 O  O   . HOH D 4 .   ? 22.805  -9.384  14.102  1.00 29.67 ? 517 HOH A O   1 
HETATM 2287 O  O   . HOH D 4 .   ? 19.012  -2.651  -7.026  1.00 24.27 ? 518 HOH A O   1 
HETATM 2288 O  O   . HOH D 4 .   ? 10.897  7.853   -4.312  1.00 30.10 ? 519 HOH A O   1 
HETATM 2289 O  O   . HOH D 4 .   ? 24.183  2.803   -1.820  1.00 32.67 ? 520 HOH A O   1 
HETATM 2290 O  O   . HOH D 4 .   ? 5.594   -8.680  37.382  1.00 27.05 ? 521 HOH A O   1 
HETATM 2291 O  O   . HOH D 4 .   ? 22.597  -4.361  34.496  1.00 16.10 ? 522 HOH A O   1 
HETATM 2292 O  O   . HOH D 4 .   ? 23.008  9.947   27.745  1.00 29.65 ? 523 HOH A O   1 
HETATM 2293 O  O   . HOH D 4 .   ? -4.964  -4.573  33.851  1.00 30.19 ? 524 HOH A O   1 
HETATM 2294 O  O   . HOH D 4 .   ? 15.041  18.941  27.494  1.00 31.20 ? 525 HOH A O   1 
HETATM 2295 O  O   . HOH D 4 .   ? 2.308   -19.407 14.799  1.00 22.64 ? 526 HOH A O   1 
HETATM 2296 O  O   . HOH D 4 .   ? -6.217  -5.004  8.027   1.00 33.41 ? 527 HOH A O   1 
HETATM 2297 O  O   . HOH D 4 .   ? -5.238  -5.356  30.443  1.00 30.39 ? 528 HOH A O   1 
HETATM 2298 O  O   . HOH D 4 .   ? 15.474  -10.790 -4.996  1.00 31.31 ? 529 HOH A O   1 
HETATM 2299 O  O   . HOH D 4 .   ? -4.829  8.342   26.796  1.00 32.38 ? 530 HOH A O   1 
HETATM 2300 O  O   . HOH D 4 .   ? 20.297  -6.622  32.749  1.00 20.76 ? 531 HOH A O   1 
HETATM 2301 O  O   . HOH D 4 .   ? 20.945  3.020   34.483  1.00 25.01 ? 532 HOH A O   1 
HETATM 2302 O  O   . HOH D 4 .   ? 29.664  -2.778  23.663  1.00 27.15 ? 533 HOH A O   1 
HETATM 2303 O  O   . HOH D 4 .   ? 32.191  3.216   25.939  1.00 16.98 ? 534 HOH A O   1 
HETATM 2304 O  O   . HOH D 4 .   ? 34.510  2.105   24.527  1.00 17.23 ? 535 HOH A O   1 
HETATM 2305 O  O   . HOH D 4 .   ? 29.423  5.043   27.893  1.00 27.51 ? 536 HOH A O   1 
HETATM 2306 O  O   . HOH D 4 .   ? 34.823  4.008   22.744  1.00 23.75 ? 537 HOH A O   1 
HETATM 2307 O  O   . HOH D 4 .   ? 19.817  11.071  28.031  1.00 18.76 ? 538 HOH A O   1 
HETATM 2308 O  O   . HOH D 4 .   ? 22.278  16.638  24.272  1.00 29.00 ? 539 HOH A O   1 
HETATM 2309 O  O   . HOH D 4 .   ? 16.030  -7.848  33.638  1.00 26.29 ? 540 HOH A O   1 
HETATM 2310 O  O   . HOH D 4 .   ? 15.063  -9.492  36.734  1.00 29.66 ? 541 HOH A O   1 
HETATM 2311 O  O   . HOH D 4 .   ? 12.370  -13.628 36.563  1.00 19.56 ? 542 HOH A O   1 
HETATM 2312 O  O   . HOH D 4 .   ? 4.878   -8.056  33.049  1.00 16.49 ? 543 HOH A O   1 
HETATM 2313 O  O   . HOH D 4 .   ? 3.215   -10.264 31.795  1.00 27.79 ? 544 HOH A O   1 
HETATM 2314 O  O   . HOH D 4 .   ? 4.739   -13.879 32.704  1.00 27.03 ? 545 HOH A O   1 
HETATM 2315 O  O   . HOH D 4 .   ? -2.110  2.265   34.700  1.00 28.26 ? 546 HOH A O   1 
HETATM 2316 O  O   . HOH D 4 .   ? -3.783  6.576   8.375   1.00 28.38 ? 547 HOH A O   1 
HETATM 2317 O  O   . HOH D 4 .   ? -0.989  7.467   4.761   1.00 14.48 ? 548 HOH A O   1 
HETATM 2318 O  O   . HOH D 4 .   ? 8.882   12.697  5.624   1.00 26.74 ? 549 HOH A O   1 
HETATM 2319 O  O   . HOH D 4 .   ? 9.104   11.294  2.973   1.00 21.51 ? 550 HOH A O   1 
HETATM 2320 O  O   . HOH D 4 .   ? 15.649  18.171  12.225  1.00 23.60 ? 551 HOH A O   1 
HETATM 2321 O  O   . HOH D 4 .   ? 13.379  18.514  10.500  1.00 20.21 ? 552 HOH A O   1 
HETATM 2322 O  O   . HOH D 4 .   ? 9.908   19.933  12.308  1.00 23.08 ? 553 HOH A O   1 
HETATM 2323 O  O   . HOH D 4 .   ? 0.923   15.583  28.819  1.00 25.35 ? 554 HOH A O   1 
HETATM 2324 O  O   . HOH D 4 .   ? -0.773  -12.372 18.832  1.00 25.49 ? 555 HOH A O   1 
HETATM 2325 O  O   . HOH D 4 .   ? -2.270  -9.285  17.082  1.00 21.12 ? 556 HOH A O   1 
HETATM 2326 O  O   . HOH D 4 .   ? -4.576  -3.694  13.323  1.00 25.38 ? 557 HOH A O   1 
HETATM 2327 O  O   . HOH D 4 .   ? -2.668  -16.184 6.411   1.00 23.58 ? 558 HOH A O   1 
HETATM 2328 O  O   . HOH D 4 .   ? 12.186  2.343   -6.626  1.00 21.84 ? 559 HOH A O   1 
HETATM 2329 O  O   . HOH D 4 .   ? 15.569  5.399   -5.725  1.00 28.86 ? 560 HOH A O   1 
HETATM 2330 O  O   . HOH D 4 .   ? 13.960  -6.680  -6.918  1.00 32.99 ? 561 HOH A O   1 
HETATM 2331 O  O   . HOH D 4 .   ? 17.520  -11.318 -2.761  1.00 22.19 ? 562 HOH A O   1 
HETATM 2332 O  O   . HOH D 4 .   ? 13.700  -15.228 1.633   1.00 24.02 ? 563 HOH A O   1 
HETATM 2333 O  O   . HOH D 4 .   ? -6.375  -5.551  26.193  1.00 29.17 ? 564 HOH A O   1 
HETATM 2334 O  O   . HOH D 4 .   ? 10.120  2.999   33.712  1.00 20.17 ? 565 HOH A O   1 
HETATM 2335 O  O   . HOH D 4 .   ? 13.765  3.512   35.243  1.00 23.55 ? 566 HOH A O   1 
HETATM 2336 O  O   . HOH D 4 .   ? 22.881  -9.111  16.393  1.00 23.55 ? 567 HOH A O   1 
HETATM 2337 O  O   . HOH D 4 .   ? -2.906  -1.589  29.521  1.00 23.11 ? 568 HOH A O   1 
HETATM 2338 O  O   . HOH D 4 .   ? 18.114  6.303   7.435   1.00 23.69 ? 569 HOH A O   1 
HETATM 2339 O  O   . HOH D 4 .   ? 18.276  7.967   5.493   1.00 43.66 ? 570 HOH A O   1 
HETATM 2340 O  O   . HOH D 4 .   ? 16.785  8.410   9.127   1.00 33.60 ? 571 HOH A O   1 
HETATM 2341 O  O   . HOH D 4 .   ? 16.366  5.846   9.895   1.00 32.05 ? 572 HOH A O   1 
HETATM 2342 O  O   . HOH D 4 .   ? 13.536  8.056   8.668   1.00 29.16 ? 573 HOH A O   1 
HETATM 2343 O  O   . HOH D 4 .   ? 20.782  16.280  16.271  1.00 22.04 ? 574 HOH A O   1 
HETATM 2344 O  O   . HOH D 4 .   ? 34.768  1.909   5.976   1.00 34.05 ? 575 HOH A O   1 
HETATM 2345 O  O   . HOH D 4 .   ? 31.444  -7.160  8.819   1.00 33.54 ? 576 HOH A O   1 
HETATM 2346 O  O   . HOH D 4 .   ? 32.881  -5.059  7.689   1.00 39.01 ? 577 HOH A O   1 
HETATM 2347 O  O   . HOH D 4 .   ? 23.774  -2.456  7.829   1.00 29.99 ? 578 HOH A O   1 
HETATM 2348 O  O   . HOH D 4 .   ? 31.165  -0.728  13.609  1.00 26.84 ? 579 HOH A O   1 
HETATM 2349 O  O   . HOH D 4 .   ? 32.684  1.374   15.902  1.00 26.25 ? 580 HOH A O   1 
HETATM 2350 O  O   . HOH D 4 .   ? 31.516  7.374   13.079  1.00 30.54 ? 581 HOH A O   1 
HETATM 2351 O  O   . HOH D 4 .   ? 30.731  3.763   12.410  1.00 31.18 ? 582 HOH A O   1 
HETATM 2352 O  O   . HOH D 4 .   ? 37.421  -7.368  11.634  1.00 27.60 ? 583 HOH A O   1 
HETATM 2353 O  O   . HOH D 4 .   ? 26.801  2.363   8.238   1.00 26.39 ? 584 HOH A O   1 
HETATM 2354 O  O   . HOH D 4 .   ? 24.889  -0.935  4.696   1.00 35.56 ? 585 HOH A O   1 
HETATM 2355 O  O   . HOH D 4 .   ? 27.535  1.440   -1.406  1.00 33.67 ? 586 HOH A O   1 
HETATM 2356 O  O   . HOH D 4 .   ? 22.613  -14.340 4.969   1.00 27.96 ? 587 HOH A O   1 
HETATM 2357 O  O   . HOH D 4 .   ? 22.976  -13.787 9.353   1.00 21.65 ? 588 HOH A O   1 
HETATM 2358 O  O   . HOH D 4 .   ? 28.719  -3.418  -0.311  1.00 34.27 ? 589 HOH A O   1 
HETATM 2359 O  O   . HOH D 4 .   ? 27.382  -9.284  15.706  1.00 26.19 ? 590 HOH A O   1 
HETATM 2360 O  O   . HOH D 4 .   ? 27.410  7.390   29.241  1.00 28.78 ? 591 HOH A O   1 
HETATM 2361 O  O   . HOH D 4 .   ? 27.716  1.784   32.720  1.00 30.94 ? 592 HOH A O   1 
HETATM 2362 O  O   . HOH D 4 .   ? 27.804  -1.445  30.188  1.00 28.59 ? 593 HOH A O   1 
HETATM 2363 O  O   . HOH D 4 .   ? 32.196  -2.959  29.451  1.00 39.26 ? 594 HOH A O   1 
HETATM 2364 O  O   . HOH D 4 .   ? 12.546  -15.779 34.849  1.00 24.56 ? 595 HOH A O   1 
HETATM 2365 O  O   . HOH D 4 .   ? 4.504   -13.048 28.759  1.00 27.11 ? 596 HOH A O   1 
HETATM 2366 O  O   . HOH D 4 .   ? 12.212  -18.170 26.576  1.00 34.00 ? 597 HOH A O   1 
HETATM 2367 O  O   . HOH D 4 .   ? 8.388   -17.740 26.339  1.00 18.84 ? 598 HOH A O   1 
HETATM 2368 O  O   . HOH D 4 .   ? 4.282   -16.163 20.342  1.00 28.97 ? 599 HOH A O   1 
HETATM 2369 O  O   . HOH D 4 .   ? 10.412  -3.679  38.417  1.00 31.09 ? 600 HOH A O   1 
HETATM 2370 O  O   . HOH D 4 .   ? 2.801   -6.916  35.011  1.00 32.02 ? 601 HOH A O   1 
HETATM 2371 O  O   . HOH D 4 .   ? -6.882  8.164   21.754  1.00 25.70 ? 602 HOH A O   1 
HETATM 2372 O  O   . HOH D 4 .   ? -6.708  6.350   24.122  1.00 32.94 ? 603 HOH A O   1 
HETATM 2373 O  O   . HOH D 4 .   ? -0.076  23.397  6.542   1.00 32.51 ? 604 HOH A O   1 
HETATM 2374 O  O   . HOH D 4 .   ? 2.260   19.674  18.676  1.00 30.34 ? 605 HOH A O   1 
HETATM 2375 O  O   . HOH D 4 .   ? -0.325  21.757  17.565  1.00 41.61 ? 606 HOH A O   1 
HETATM 2376 O  O   . HOH D 4 .   ? 8.031   21.311  8.648   1.00 26.88 ? 607 HOH A O   1 
HETATM 2377 O  O   . HOH D 4 .   ? 17.121  -18.953 15.676  1.00 27.06 ? 608 HOH A O   1 
HETATM 2378 O  O   . HOH D 4 .   ? 10.499  22.694  25.053  1.00 31.88 ? 609 HOH A O   1 
HETATM 2379 O  O   . HOH D 4 .   ? 19.680  13.295  25.942  1.00 25.68 ? 610 HOH A O   1 
HETATM 2380 O  O   . HOH D 4 .   ? -4.688  -13.440 8.217   1.00 29.80 ? 611 HOH A O   1 
HETATM 2381 O  O   . HOH D 4 .   ? -3.457  -7.990  2.136   1.00 27.70 ? 612 HOH A O   1 
HETATM 2382 O  O   . HOH D 4 .   ? -2.852  -5.386  0.090   1.00 33.90 ? 613 HOH A O   1 
HETATM 2383 O  O   . HOH D 4 .   ? 13.759  -8.179  -4.531  1.00 26.65 ? 614 HOH A O   1 
HETATM 2384 O  O   . HOH D 4 .   ? 7.515   0.899   -6.096  1.00 23.77 ? 615 HOH A O   1 
HETATM 2385 O  O   . HOH D 4 .   ? 21.767  -7.090  -5.318  1.00 35.47 ? 616 HOH A O   1 
HETATM 2386 O  O   . HOH D 4 .   ? 16.447  -14.300 1.258   1.00 26.32 ? 617 HOH A O   1 
HETATM 2387 O  O   . HOH D 4 .   ? -4.540  6.156   4.124   1.00 32.19 ? 618 HOH A O   1 
HETATM 2388 O  O   . HOH D 4 .   ? -2.681  0.204   27.378  1.00 32.00 ? 619 HOH A O   1 
HETATM 2389 O  O   . HOH D 4 .   ? 25.104  -11.486 21.909  1.00 27.70 ? 620 HOH A O   1 
HETATM 2390 O  O   . HOH D 4 .   ? 3.948   -12.398 37.448  1.00 23.48 ? 621 HOH A O   1 
HETATM 2391 O  O   . HOH D 4 .   ? 10.571  -17.622 19.893  1.00 26.07 ? 622 HOH A O   1 
HETATM 2392 O  O   . HOH D 4 .   ? 20.080  -15.681 -1.862  1.00 31.08 ? 623 HOH A O   1 
HETATM 2393 O  O   . HOH D 4 .   ? -2.572  10.265  3.407   1.00 26.99 ? 624 HOH A O   1 
HETATM 2394 O  O   . HOH D 4 .   ? -7.476  7.499   26.147  1.00 34.67 ? 625 HOH A O   1 
HETATM 2395 O  O   . HOH D 4 .   ? 18.706  -6.982  34.816  1.00 35.85 ? 626 HOH A O   1 
HETATM 2396 O  O   . HOH D 4 .   ? 25.342  -9.857  23.493  1.00 32.26 ? 627 HOH A O   1 
HETATM 2397 O  O   . HOH D 4 .   ? 23.449  -12.918 -1.114  1.00 33.94 ? 628 HOH A O   1 
HETATM 2398 O  O   . HOH D 4 .   ? 25.569  7.736   12.686  1.00 34.38 ? 629 HOH A O   1 
HETATM 2399 O  O   . HOH D 4 .   ? 19.005  -10.016 31.656  1.00 35.28 ? 630 HOH A O   1 
HETATM 2400 O  O   . HOH D 4 .   ? 8.865   15.468  2.079   1.00 36.18 ? 631 HOH A O   1 
HETATM 2401 O  O   . HOH D 4 .   ? -4.534  -8.646  17.706  1.00 33.00 ? 632 HOH A O   1 
HETATM 2402 O  O   . HOH D 4 .   ? -0.071  3.662   -3.843  1.00 34.30 ? 633 HOH A O   1 
HETATM 2403 O  O   . HOH D 4 .   ? -6.592  1.971   15.083  1.00 31.79 ? 634 HOH A O   1 
HETATM 2404 O  O   . HOH D 4 .   ? 19.801  -3.844  36.601  1.00 26.97 ? 635 HOH A O   1 
HETATM 2405 O  O   . HOH D 4 .   ? 26.056  -3.872  33.586  1.00 34.14 ? 636 HOH A O   1 
HETATM 2406 O  O   . HOH D 4 .   ? -8.252  -1.504  13.448  1.00 37.14 ? 637 HOH A O   1 
HETATM 2407 O  O   . HOH D 4 .   ? 15.431  2.491   40.656  1.00 40.98 ? 638 HOH A O   1 
HETATM 2408 O  O   . HOH D 4 .   ? 8.328   8.742   31.414  1.00 30.64 ? 639 HOH A O   1 
HETATM 2409 O  O   . HOH D 4 .   ? 16.264  -16.985 22.909  1.00 31.98 ? 640 HOH A O   1 
HETATM 2410 O  O   . HOH D 4 .   ? 6.166   -14.197 25.121  1.00 37.34 ? 641 HOH A O   1 
HETATM 2411 O  O   . HOH D 4 .   ? 10.419  10.473  7.684   1.00 32.38 ? 642 HOH A O   1 
HETATM 2412 O  O   . HOH D 4 .   ? 21.101  -19.926 17.598  1.00 38.20 ? 643 HOH A O   1 
HETATM 2413 O  O   . HOH D 4 .   ? 1.223   -14.193 21.972  1.00 32.93 ? 644 HOH A O   1 
HETATM 2414 O  O   . HOH D 4 .   ? 29.256  9.596   24.004  1.00 38.10 ? 645 HOH A O   1 
HETATM 2415 O  O   . HOH D 4 .   ? 9.312   2.605   -7.818  1.00 35.94 ? 646 HOH A O   1 
HETATM 2416 O  O   . HOH D 4 .   ? -4.028  -7.700  15.325  1.00 39.40 ? 647 HOH A O   1 
HETATM 2417 O  O   . HOH D 4 .   ? 19.692  4.894   -7.277  1.00 34.14 ? 648 HOH A O   1 
HETATM 2418 O  O   . HOH D 4 .   ? 27.591  -3.333  27.733  1.00 32.40 ? 649 HOH A O   1 
HETATM 2419 O  O   . HOH D 4 .   ? 19.917  -5.160  -7.762  1.00 38.51 ? 650 HOH A O   1 
HETATM 2420 O  O   . HOH D 4 .   ? 22.463  -7.819  29.392  1.00 31.41 ? 651 HOH A O   1 
HETATM 2421 O  O   . HOH D 4 .   ? 24.330  -3.646  -11.560 1.00 28.41 ? 652 HOH A O   1 
HETATM 2422 O  O   . HOH D 4 .   ? -1.057  -19.685 12.270  1.00 32.69 ? 653 HOH A O   1 
HETATM 2423 O  O   . HOH D 4 .   ? 22.106  -14.691 -2.232  1.00 38.43 ? 654 HOH A O   1 
HETATM 2424 O  O   . HOH D 4 .   ? -5.453  6.251   6.434   1.00 35.60 ? 655 HOH A O   1 
HETATM 2425 O  O   . HOH D 4 .   ? 23.855  8.431   32.252  1.00 28.46 ? 656 HOH A O   1 
HETATM 2426 O  O   . HOH D 4 .   ? 27.536  -4.150  6.484   1.00 30.67 ? 657 HOH A O   1 
HETATM 2427 O  O   . HOH D 4 .   ? 29.227  8.718   26.447  1.00 39.07 ? 658 HOH A O   1 
HETATM 2428 O  O   . HOH D 4 .   ? 26.907  -12.199 8.700   1.00 33.54 ? 659 HOH A O   1 
HETATM 2429 O  O   . HOH D 4 .   ? 20.913  2.944   -10.692 1.00 34.03 ? 660 HOH A O   1 
HETATM 2430 O  O   . HOH D 4 .   ? -5.057  -4.014  4.841   1.00 36.55 ? 661 HOH A O   1 
HETATM 2431 O  O   . HOH D 4 .   ? -11.754 -5.564  24.151  1.00 37.53 ? 662 HOH A O   1 
HETATM 2432 O  O   . HOH D 4 .   ? 25.873  10.361  22.652  1.00 35.61 ? 663 HOH A O   1 
HETATM 2433 O  O   . HOH D 4 .   ? 2.952   -5.871  39.262  1.00 32.02 ? 664 HOH A O   1 
HETATM 2434 O  O   . HOH D 4 .   ? 8.161   11.672  -1.645  1.00 40.52 ? 665 HOH A O   1 
HETATM 2435 O  O   . HOH D 4 .   ? 15.679  -0.184  40.387  1.00 34.06 ? 666 HOH A O   1 
HETATM 2436 O  O   . HOH D 4 .   ? 17.200  -13.972 -2.030  1.00 31.42 ? 667 HOH A O   1 
HETATM 2437 O  O   . HOH D 4 .   ? 4.868   19.181  26.129  1.00 30.69 ? 668 HOH A O   1 
HETATM 2438 O  O   . HOH D 4 .   ? 22.336  5.184   -5.088  1.00 35.27 ? 669 HOH A O   1 
HETATM 2439 O  O   . HOH D 4 .   ? 14.244  -18.347 24.077  1.00 34.09 ? 670 HOH A O   1 
HETATM 2440 O  O   . HOH D 4 .   ? 32.634  2.336   28.624  1.00 39.62 ? 671 HOH A O   1 
HETATM 2441 O  O   . HOH D 4 .   ? 18.562  -16.899 22.501  1.00 31.88 ? 672 HOH A O   1 
HETATM 2442 O  O   . HOH D 4 .   ? 21.019  -13.418 27.614  1.00 27.71 ? 673 HOH A O   1 
HETATM 2443 O  O   . HOH D 4 .   ? 27.262  -3.438  2.880   1.00 38.88 ? 674 HOH A O   1 
HETATM 2444 O  O   . HOH D 4 .   ? 24.098  -7.194  27.359  1.00 32.20 ? 675 HOH A O   1 
HETATM 2445 O  O   . HOH D 4 .   ? 19.168  11.836  13.417  1.00 46.96 ? 676 HOH A O   1 
HETATM 2446 O  O   . HOH D 4 .   ? 30.603  10.145  21.603  1.00 37.17 ? 677 HOH A O   1 
HETATM 2447 O  O   . HOH D 4 .   ? 15.983  -6.153  -8.554  1.00 41.59 ? 678 HOH A O   1 
HETATM 2448 O  O   . HOH D 4 .   ? 20.055  -15.723 18.156  1.00 31.80 ? 679 HOH A O   1 
HETATM 2449 O  O   . HOH D 4 .   ? -5.954  -11.044 20.326  1.00 39.68 ? 680 HOH A O   1 
HETATM 2450 O  O   . HOH D 4 .   ? 27.610  3.135   -5.359  1.00 32.71 ? 681 HOH A O   1 
HETATM 2451 O  O   . HOH D 4 .   ? -9.813  -11.004 21.370  1.00 35.91 ? 682 HOH A O   1 
HETATM 2452 O  O   . HOH D 4 .   ? 6.422   -18.920 27.562  1.00 36.47 ? 683 HOH A O   1 
HETATM 2453 O  O   . HOH D 4 .   ? 2.869   -0.998  45.301  1.00 31.89 ? 684 HOH A O   1 
HETATM 2454 O  O   . HOH D 4 .   ? 5.295   22.768  22.282  1.00 40.37 ? 685 HOH A O   1 
HETATM 2455 O  O   . HOH D 4 .   ? -0.045  2.358   0.217   1.00 30.78 ? 686 HOH A O   1 
HETATM 2456 O  O   . HOH D 4 .   ? 4.092   -8.720  -2.744  1.00 28.27 ? 687 HOH A O   1 
HETATM 2457 O  O   . HOH D 4 .   ? 36.284  -4.847  11.972  1.00 30.74 ? 688 HOH A O   1 
HETATM 2458 O  O   . HOH D 4 .   ? 35.901  -8.774  14.784  1.00 35.41 ? 689 HOH A O   1 
HETATM 2459 O  O   . HOH D 4 .   ? 15.021  -7.428  35.864  1.00 42.70 ? 690 HOH A O   1 
HETATM 2460 O  O   . HOH D 4 .   ? 11.171  -10.731 40.224  1.00 38.48 ? 691 HOH A O   1 
HETATM 2461 O  O   . HOH D 4 .   ? -3.768  13.987  6.476   1.00 33.32 ? 692 HOH A O   1 
HETATM 2462 O  O   . HOH D 4 .   ? 12.703  10.394  8.668   1.00 39.00 ? 693 HOH A O   1 
HETATM 2463 O  O   . HOH D 4 .   ? 0.320   1.552   -1.900  1.00 39.31 ? 694 HOH A O   1 
HETATM 2464 O  O   . HOH D 4 .   ? -1.534  -7.821  25.616  1.00 24.76 ? 695 HOH A O   1 
HETATM 2465 O  O   . HOH D 4 .   ? -4.674  -1.530  31.695  1.00 38.10 ? 696 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 V14 1   302 1   V14 V14 A . 
D 4 HOH 1   401 1   HOH HOH A . 
D 4 HOH 2   402 2   HOH HOH A . 
D 4 HOH 3   403 3   HOH HOH A . 
D 4 HOH 4   404 4   HOH HOH A . 
D 4 HOH 5   405 5   HOH HOH A . 
D 4 HOH 6   406 6   HOH HOH A . 
D 4 HOH 7   407 7   HOH HOH A . 
D 4 HOH 8   408 8   HOH HOH A . 
D 4 HOH 9   409 9   HOH HOH A . 
D 4 HOH 10  410 10  HOH HOH A . 
D 4 HOH 11  411 11  HOH HOH A . 
D 4 HOH 12  412 12  HOH HOH A . 
D 4 HOH 13  413 13  HOH HOH A . 
D 4 HOH 14  414 14  HOH HOH A . 
D 4 HOH 15  415 15  HOH HOH A . 
D 4 HOH 16  416 16  HOH HOH A . 
D 4 HOH 17  417 17  HOH HOH A . 
D 4 HOH 18  418 18  HOH HOH A . 
D 4 HOH 19  419 19  HOH HOH A . 
D 4 HOH 20  420 20  HOH HOH A . 
D 4 HOH 21  421 21  HOH HOH A . 
D 4 HOH 22  422 22  HOH HOH A . 
D 4 HOH 23  423 23  HOH HOH A . 
D 4 HOH 24  424 24  HOH HOH A . 
D 4 HOH 25  425 25  HOH HOH A . 
D 4 HOH 26  426 26  HOH HOH A . 
D 4 HOH 27  427 27  HOH HOH A . 
D 4 HOH 28  428 28  HOH HOH A . 
D 4 HOH 29  429 29  HOH HOH A . 
D 4 HOH 30  430 30  HOH HOH A . 
D 4 HOH 31  431 31  HOH HOH A . 
D 4 HOH 32  432 32  HOH HOH A . 
D 4 HOH 33  433 33  HOH HOH A . 
D 4 HOH 34  434 34  HOH HOH A . 
D 4 HOH 35  435 35  HOH HOH A . 
D 4 HOH 36  436 36  HOH HOH A . 
D 4 HOH 37  437 37  HOH HOH A . 
D 4 HOH 38  438 38  HOH HOH A . 
D 4 HOH 39  439 39  HOH HOH A . 
D 4 HOH 40  440 40  HOH HOH A . 
D 4 HOH 41  441 41  HOH HOH A . 
D 4 HOH 42  442 42  HOH HOH A . 
D 4 HOH 43  443 43  HOH HOH A . 
D 4 HOH 44  444 44  HOH HOH A . 
D 4 HOH 45  445 45  HOH HOH A . 
D 4 HOH 46  446 46  HOH HOH A . 
D 4 HOH 47  447 47  HOH HOH A . 
D 4 HOH 48  448 48  HOH HOH A . 
D 4 HOH 49  449 49  HOH HOH A . 
D 4 HOH 50  450 50  HOH HOH A . 
D 4 HOH 51  451 51  HOH HOH A . 
D 4 HOH 52  452 52  HOH HOH A . 
D 4 HOH 53  453 53  HOH HOH A . 
D 4 HOH 54  454 54  HOH HOH A . 
D 4 HOH 55  455 55  HOH HOH A . 
D 4 HOH 56  456 56  HOH HOH A . 
D 4 HOH 57  457 57  HOH HOH A . 
D 4 HOH 58  458 58  HOH HOH A . 
D 4 HOH 59  459 59  HOH HOH A . 
D 4 HOH 60  460 60  HOH HOH A . 
D 4 HOH 61  461 61  HOH HOH A . 
D 4 HOH 62  462 62  HOH HOH A . 
D 4 HOH 63  463 63  HOH HOH A . 
D 4 HOH 64  464 64  HOH HOH A . 
D 4 HOH 65  465 65  HOH HOH A . 
D 4 HOH 66  466 66  HOH HOH A . 
D 4 HOH 67  467 67  HOH HOH A . 
D 4 HOH 68  468 68  HOH HOH A . 
D 4 HOH 69  469 69  HOH HOH A . 
D 4 HOH 70  470 70  HOH HOH A . 
D 4 HOH 71  471 71  HOH HOH A . 
D 4 HOH 72  472 72  HOH HOH A . 
D 4 HOH 73  473 73  HOH HOH A . 
D 4 HOH 74  474 74  HOH HOH A . 
D 4 HOH 75  475 75  HOH HOH A . 
D 4 HOH 76  476 76  HOH HOH A . 
D 4 HOH 77  477 77  HOH HOH A . 
D 4 HOH 78  478 78  HOH HOH A . 
D 4 HOH 79  479 79  HOH HOH A . 
D 4 HOH 80  480 80  HOH HOH A . 
D 4 HOH 81  481 81  HOH HOH A . 
D 4 HOH 82  482 82  HOH HOH A . 
D 4 HOH 83  483 83  HOH HOH A . 
D 4 HOH 84  484 84  HOH HOH A . 
D 4 HOH 85  485 85  HOH HOH A . 
D 4 HOH 86  486 86  HOH HOH A . 
D 4 HOH 87  487 87  HOH HOH A . 
D 4 HOH 88  488 88  HOH HOH A . 
D 4 HOH 89  489 89  HOH HOH A . 
D 4 HOH 90  490 90  HOH HOH A . 
D 4 HOH 91  491 91  HOH HOH A . 
D 4 HOH 92  492 92  HOH HOH A . 
D 4 HOH 93  493 93  HOH HOH A . 
D 4 HOH 94  494 94  HOH HOH A . 
D 4 HOH 95  495 95  HOH HOH A . 
D 4 HOH 96  496 96  HOH HOH A . 
D 4 HOH 97  497 97  HOH HOH A . 
D 4 HOH 98  498 98  HOH HOH A . 
D 4 HOH 99  499 99  HOH HOH A . 
D 4 HOH 100 500 100 HOH HOH A . 
D 4 HOH 101 501 101 HOH HOH A . 
D 4 HOH 102 502 102 HOH HOH A . 
D 4 HOH 103 503 103 HOH HOH A . 
D 4 HOH 104 504 104 HOH HOH A . 
D 4 HOH 105 505 105 HOH HOH A . 
D 4 HOH 106 506 106 HOH HOH A . 
D 4 HOH 107 507 107 HOH HOH A . 
D 4 HOH 108 508 108 HOH HOH A . 
D 4 HOH 109 509 109 HOH HOH A . 
D 4 HOH 110 510 110 HOH HOH A . 
D 4 HOH 111 511 111 HOH HOH A . 
D 4 HOH 112 512 112 HOH HOH A . 
D 4 HOH 113 513 113 HOH HOH A . 
D 4 HOH 114 514 114 HOH HOH A . 
D 4 HOH 115 515 115 HOH HOH A . 
D 4 HOH 116 516 116 HOH HOH A . 
D 4 HOH 117 517 117 HOH HOH A . 
D 4 HOH 118 518 118 HOH HOH A . 
D 4 HOH 119 519 119 HOH HOH A . 
D 4 HOH 120 520 120 HOH HOH A . 
D 4 HOH 121 521 121 HOH HOH A . 
D 4 HOH 122 522 122 HOH HOH A . 
D 4 HOH 123 523 123 HOH HOH A . 
D 4 HOH 124 524 124 HOH HOH A . 
D 4 HOH 125 525 125 HOH HOH A . 
D 4 HOH 126 526 126 HOH HOH A . 
D 4 HOH 127 527 127 HOH HOH A . 
D 4 HOH 128 528 128 HOH HOH A . 
D 4 HOH 129 529 129 HOH HOH A . 
D 4 HOH 130 530 130 HOH HOH A . 
D 4 HOH 131 531 131 HOH HOH A . 
D 4 HOH 132 532 132 HOH HOH A . 
D 4 HOH 133 533 133 HOH HOH A . 
D 4 HOH 134 534 134 HOH HOH A . 
D 4 HOH 135 535 135 HOH HOH A . 
D 4 HOH 136 536 136 HOH HOH A . 
D 4 HOH 137 537 137 HOH HOH A . 
D 4 HOH 138 538 138 HOH HOH A . 
D 4 HOH 139 539 139 HOH HOH A . 
D 4 HOH 140 540 140 HOH HOH A . 
D 4 HOH 141 541 141 HOH HOH A . 
D 4 HOH 142 542 142 HOH HOH A . 
D 4 HOH 143 543 143 HOH HOH A . 
D 4 HOH 144 544 144 HOH HOH A . 
D 4 HOH 145 545 145 HOH HOH A . 
D 4 HOH 146 546 146 HOH HOH A . 
D 4 HOH 147 547 147 HOH HOH A . 
D 4 HOH 148 548 148 HOH HOH A . 
D 4 HOH 149 549 149 HOH HOH A . 
D 4 HOH 150 550 150 HOH HOH A . 
D 4 HOH 151 551 151 HOH HOH A . 
D 4 HOH 152 552 152 HOH HOH A . 
D 4 HOH 153 553 153 HOH HOH A . 
D 4 HOH 154 554 154 HOH HOH A . 
D 4 HOH 155 555 155 HOH HOH A . 
D 4 HOH 156 556 156 HOH HOH A . 
D 4 HOH 157 557 157 HOH HOH A . 
D 4 HOH 158 558 158 HOH HOH A . 
D 4 HOH 159 559 159 HOH HOH A . 
D 4 HOH 160 560 160 HOH HOH A . 
D 4 HOH 161 561 161 HOH HOH A . 
D 4 HOH 162 562 162 HOH HOH A . 
D 4 HOH 163 563 163 HOH HOH A . 
D 4 HOH 164 564 164 HOH HOH A . 
D 4 HOH 165 565 165 HOH HOH A . 
D 4 HOH 166 566 166 HOH HOH A . 
D 4 HOH 167 567 167 HOH HOH A . 
D 4 HOH 168 568 168 HOH HOH A . 
D 4 HOH 169 569 169 HOH HOH A . 
D 4 HOH 170 570 170 HOH HOH A . 
D 4 HOH 171 571 171 HOH HOH A . 
D 4 HOH 172 572 172 HOH HOH A . 
D 4 HOH 173 573 173 HOH HOH A . 
D 4 HOH 174 574 174 HOH HOH A . 
D 4 HOH 175 575 175 HOH HOH A . 
D 4 HOH 176 576 176 HOH HOH A . 
D 4 HOH 177 577 177 HOH HOH A . 
D 4 HOH 178 578 178 HOH HOH A . 
D 4 HOH 179 579 179 HOH HOH A . 
D 4 HOH 180 580 180 HOH HOH A . 
D 4 HOH 181 581 181 HOH HOH A . 
D 4 HOH 182 582 182 HOH HOH A . 
D 4 HOH 183 583 183 HOH HOH A . 
D 4 HOH 184 584 184 HOH HOH A . 
D 4 HOH 185 585 185 HOH HOH A . 
D 4 HOH 186 586 186 HOH HOH A . 
D 4 HOH 187 587 187 HOH HOH A . 
D 4 HOH 188 588 188 HOH HOH A . 
D 4 HOH 189 589 189 HOH HOH A . 
D 4 HOH 190 590 190 HOH HOH A . 
D 4 HOH 191 591 191 HOH HOH A . 
D 4 HOH 192 592 192 HOH HOH A . 
D 4 HOH 193 593 193 HOH HOH A . 
D 4 HOH 194 594 194 HOH HOH A . 
D 4 HOH 195 595 195 HOH HOH A . 
D 4 HOH 196 596 196 HOH HOH A . 
D 4 HOH 197 597 197 HOH HOH A . 
D 4 HOH 198 598 198 HOH HOH A . 
D 4 HOH 199 599 199 HOH HOH A . 
D 4 HOH 200 600 200 HOH HOH A . 
D 4 HOH 201 601 201 HOH HOH A . 
D 4 HOH 202 602 202 HOH HOH A . 
D 4 HOH 203 603 203 HOH HOH A . 
D 4 HOH 204 604 204 HOH HOH A . 
D 4 HOH 205 605 205 HOH HOH A . 
D 4 HOH 206 606 206 HOH HOH A . 
D 4 HOH 207 607 207 HOH HOH A . 
D 4 HOH 208 608 208 HOH HOH A . 
D 4 HOH 209 609 209 HOH HOH A . 
D 4 HOH 210 610 210 HOH HOH A . 
D 4 HOH 211 611 211 HOH HOH A . 
D 4 HOH 212 612 212 HOH HOH A . 
D 4 HOH 213 613 213 HOH HOH A . 
D 4 HOH 214 614 214 HOH HOH A . 
D 4 HOH 215 615 215 HOH HOH A . 
D 4 HOH 216 616 216 HOH HOH A . 
D 4 HOH 217 617 217 HOH HOH A . 
D 4 HOH 218 618 218 HOH HOH A . 
D 4 HOH 219 619 219 HOH HOH A . 
D 4 HOH 220 620 220 HOH HOH A . 
D 4 HOH 221 621 221 HOH HOH A . 
D 4 HOH 222 622 222 HOH HOH A . 
D 4 HOH 223 623 223 HOH HOH A . 
D 4 HOH 224 624 224 HOH HOH A . 
D 4 HOH 225 625 225 HOH HOH A . 
D 4 HOH 226 626 226 HOH HOH A . 
D 4 HOH 227 627 227 HOH HOH A . 
D 4 HOH 228 628 228 HOH HOH A . 
D 4 HOH 229 629 229 HOH HOH A . 
D 4 HOH 230 630 230 HOH HOH A . 
D 4 HOH 231 631 231 HOH HOH A . 
D 4 HOH 232 632 232 HOH HOH A . 
D 4 HOH 233 633 233 HOH HOH A . 
D 4 HOH 234 634 234 HOH HOH A . 
D 4 HOH 235 635 235 HOH HOH A . 
D 4 HOH 236 636 236 HOH HOH A . 
D 4 HOH 237 637 237 HOH HOH A . 
D 4 HOH 238 638 238 HOH HOH A . 
D 4 HOH 239 639 239 HOH HOH A . 
D 4 HOH 240 640 240 HOH HOH A . 
D 4 HOH 241 641 241 HOH HOH A . 
D 4 HOH 242 642 242 HOH HOH A . 
D 4 HOH 243 643 243 HOH HOH A . 
D 4 HOH 244 644 244 HOH HOH A . 
D 4 HOH 245 645 245 HOH HOH A . 
D 4 HOH 246 646 246 HOH HOH A . 
D 4 HOH 247 647 247 HOH HOH A . 
D 4 HOH 248 648 248 HOH HOH A . 
D 4 HOH 249 649 249 HOH HOH A . 
D 4 HOH 250 650 250 HOH HOH A . 
D 4 HOH 251 651 251 HOH HOH A . 
D 4 HOH 252 652 252 HOH HOH A . 
D 4 HOH 253 653 253 HOH HOH A . 
D 4 HOH 254 654 254 HOH HOH A . 
D 4 HOH 255 655 255 HOH HOH A . 
D 4 HOH 256 656 256 HOH HOH A . 
D 4 HOH 257 657 257 HOH HOH A . 
D 4 HOH 258 658 258 HOH HOH A . 
D 4 HOH 259 659 259 HOH HOH A . 
D 4 HOH 260 660 260 HOH HOH A . 
D 4 HOH 261 661 261 HOH HOH A . 
D 4 HOH 262 662 262 HOH HOH A . 
D 4 HOH 263 663 263 HOH HOH A . 
D 4 HOH 264 664 264 HOH HOH A . 
D 4 HOH 265 665 265 HOH HOH A . 
D 4 HOH 266 666 266 HOH HOH A . 
D 4 HOH 267 667 267 HOH HOH A . 
D 4 HOH 268 668 268 HOH HOH A . 
D 4 HOH 269 669 269 HOH HOH A . 
D 4 HOH 270 670 270 HOH HOH A . 
D 4 HOH 271 671 271 HOH HOH A . 
D 4 HOH 272 672 272 HOH HOH A . 
D 4 HOH 273 673 273 HOH HOH A . 
D 4 HOH 274 674 274 HOH HOH A . 
D 4 HOH 275 675 275 HOH HOH A . 
D 4 HOH 276 676 276 HOH HOH A . 
D 4 HOH 277 677 277 HOH HOH A . 
D 4 HOH 278 678 278 HOH HOH A . 
D 4 HOH 279 679 279 HOH HOH A . 
D 4 HOH 280 680 280 HOH HOH A . 
D 4 HOH 281 681 281 HOH HOH A . 
D 4 HOH 282 682 282 HOH HOH A . 
D 4 HOH 283 683 283 HOH HOH A . 
D 4 HOH 284 684 284 HOH HOH A . 
D 4 HOH 285 685 285 HOH HOH A . 
D 4 HOH 286 686 286 HOH HOH A . 
D 4 HOH 287 687 287 HOH HOH A . 
D 4 HOH 288 688 288 HOH HOH A . 
D 4 HOH 289 689 289 HOH HOH A . 
D 4 HOH 290 690 290 HOH HOH A . 
D 4 HOH 291 691 291 HOH HOH A . 
D 4 HOH 292 692 292 HOH HOH A . 
D 4 HOH 293 693 293 HOH HOH A . 
D 4 HOH 294 694 294 HOH HOH A . 
D 4 HOH 295 695 295 HOH HOH A . 
D 4 HOH 296 696 296 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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 104.6 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 113.0 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.1  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C V14 .   ? A V14 302 ? 1_555 106.0 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C V14 .   ? A V14 302 ? 1_555 107.9 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 A C V14 .   ? A V14 302 ? 1_555 124.3 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V14 .   ? A V14 302 ? 1_555 123.0 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V14 .   ? A V14 302 ? 1_555 115.2 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V14 .   ? A V14 302 ? 1_555 99.6  ? 
10 N10 A C V14 .   ? A V14 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N10 B C V14 .   ? A V14 302 ? 1_555 24.8  ? 
# 
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 2015-01-28 
2 'Structure model' 1 1 2023-09-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' pdbx_initial_refinement_model 
5 2 'Structure model' pdbx_struct_conn_angle        
6 2 'Structure model' struct_conn                   
7 2 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_database_2.pdbx_DOI'                        
2  2 'Structure model' '_database_2.pdbx_database_accession'         
3  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_alt_id'  
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_alt_id'  
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
15 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
16 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
17 2 'Structure model' '_pdbx_struct_conn_angle.value'               
18 2 'Structure model' '_struct_conn.pdbx_dist_value'                
19 2 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
20 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
21 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
22 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
23 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
24 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
25 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
26 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
27 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
28 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
29 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
30 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
31 2 'Structure model' '_struct_site.pdbx_auth_asym_id'              
32 2 'Structure model' '_struct_site.pdbx_auth_comp_id'              
33 2 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.3.20 2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345dtb   .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O16 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   V14 
_pdbx_validate_close_contact.auth_seq_id_1    302 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    572 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.14 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -141.88 18.95   
2 1 ARG A 27  ? ? -143.43 53.45   
3 1 PHE A 176 ? ? -151.99 66.10   
4 1 ASN A 244 ? ? -97.19  49.97   
5 1 LYS A 252 ? ? 58.71   -138.13 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
PHE N    N  N N 250 
PHE CA   C  N S 251 
PHE C    C  N N 252 
PHE O    O  N N 253 
PHE CB   C  N N 254 
PHE CG   C  Y N 255 
PHE CD1  C  Y N 256 
PHE CD2  C  Y N 257 
PHE CE1  C  Y N 258 
PHE CE2  C  Y N 259 
PHE CZ   C  Y N 260 
PHE OXT  O  N N 261 
PHE H    H  N N 262 
PHE H2   H  N N 263 
PHE HA   H  N N 264 
PHE HB2  H  N N 265 
PHE HB3  H  N N 266 
PHE HD1  H  N N 267 
PHE HD2  H  N N 268 
PHE HE1  H  N N 269 
PHE HE2  H  N N 270 
PHE HZ   H  N N 271 
PHE HXT  H  N N 272 
PRO N    N  N N 273 
PRO CA   C  N S 274 
PRO C    C  N N 275 
PRO O    O  N N 276 
PRO CB   C  N N 277 
PRO CG   C  N N 278 
PRO CD   C  N N 279 
PRO OXT  O  N N 280 
PRO H    H  N N 281 
PRO HA   H  N N 282 
PRO HB2  H  N N 283 
PRO HB3  H  N N 284 
PRO HG2  H  N N 285 
PRO HG3  H  N N 286 
PRO HD2  H  N N 287 
PRO HD3  H  N N 288 
PRO HXT  H  N N 289 
SER N    N  N N 290 
SER CA   C  N S 291 
SER C    C  N N 292 
SER O    O  N N 293 
SER CB   C  N N 294 
SER OG   O  N N 295 
SER OXT  O  N N 296 
SER H    H  N N 297 
SER H2   H  N N 298 
SER HA   H  N N 299 
SER HB2  H  N N 300 
SER HB3  H  N N 301 
SER HG   H  N N 302 
SER HXT  H  N N 303 
THR N    N  N N 304 
THR CA   C  N S 305 
THR C    C  N N 306 
THR O    O  N N 307 
THR CB   C  N R 308 
THR OG1  O  N N 309 
THR CG2  C  N N 310 
THR OXT  O  N N 311 
THR H    H  N N 312 
THR H2   H  N N 313 
THR HA   H  N N 314 
THR HB   H  N N 315 
THR HG1  H  N N 316 
THR HG21 H  N N 317 
THR HG22 H  N N 318 
THR HG23 H  N N 319 
THR HXT  H  N N 320 
TRP N    N  N N 321 
TRP CA   C  N S 322 
TRP C    C  N N 323 
TRP O    O  N N 324 
TRP CB   C  N N 325 
TRP CG   C  Y N 326 
TRP CD1  C  Y N 327 
TRP CD2  C  Y N 328 
TRP NE1  N  Y N 329 
TRP CE2  C  Y N 330 
TRP CE3  C  Y N 331 
TRP CZ2  C  Y N 332 
TRP CZ3  C  Y N 333 
TRP CH2  C  Y N 334 
TRP OXT  O  N N 335 
TRP H    H  N N 336 
TRP H2   H  N N 337 
TRP HA   H  N N 338 
TRP HB2  H  N N 339 
TRP HB3  H  N N 340 
TRP HD1  H  N N 341 
TRP HE1  H  N N 342 
TRP HE3  H  N N 343 
TRP HZ2  H  N N 344 
TRP HZ3  H  N N 345 
TRP HH2  H  N N 346 
TRP HXT  H  N N 347 
TYR N    N  N N 348 
TYR CA   C  N S 349 
TYR C    C  N N 350 
TYR O    O  N N 351 
TYR CB   C  N N 352 
TYR CG   C  Y N 353 
TYR CD1  C  Y N 354 
TYR CD2  C  Y N 355 
TYR CE1  C  Y N 356 
TYR CE2  C  Y N 357 
TYR CZ   C  Y N 358 
TYR OH   O  N N 359 
TYR OXT  O  N N 360 
TYR H    H  N N 361 
TYR H2   H  N N 362 
TYR HA   H  N N 363 
TYR HB2  H  N N 364 
TYR HB3  H  N N 365 
TYR HD1  H  N N 366 
TYR HD2  H  N N 367 
TYR HE1  H  N N 368 
TYR HE2  H  N N 369 
TYR HH   H  N N 370 
TYR HXT  H  N N 371 
V14 F20  F  N N 372 
V14 C5   C  Y N 373 
V14 C4   C  Y N 374 
V14 S7   S  N N 375 
V14 O9   O  N N 376 
V14 N10  N  N N 377 
V14 O8   O  N N 378 
V14 C3   C  Y N 379 
V14 F12  F  N N 380 
V14 C2   C  Y N 381 
V14 F13  F  N N 382 
V14 C6   C  Y N 383 
V14 C1   C  Y N 384 
V14 S11  S  N N 385 
V14 O16  O  N N 386 
V14 O17  O  N N 387 
V14 C15  C  N N 388 
V14 C18  C  N N 389 
V14 O21  O  N N 390 
V14 N19  N  N N 391 
V14 C14  C  N N 392 
V14 C28  C  N N 393 
V14 C27  C  N N 394 
V14 C26  C  N N 395 
V14 C25  C  N N 396 
V14 C24  C  N N 397 
V14 C23  C  N N 398 
V14 C22  C  N N 399 
V14 H1   H  N N 400 
V14 H2   H  N N 401 
V14 H3   H  N N 402 
V14 H4   H  N N 403 
V14 H5   H  N N 404 
V14 H6   H  N N 405 
V14 H7   H  N N 406 
V14 H8   H  N N 407 
V14 H9   H  N N 408 
V14 H10  H  N N 409 
V14 H11  H  N N 410 
V14 H12  H  N N 411 
V14 H13  H  N N 412 
V14 H14  H  N N 413 
V14 H15  H  N N 414 
V14 H16  H  N N 415 
V14 H17  H  N N 416 
V14 H18  H  N N 417 
V14 H19  H  N N 418 
V14 H20  H  N N 419 
V14 H21  H  N N 420 
V14 H22  H  N N 421 
V14 H23  H  N N 422 
VAL N    N  N N 423 
VAL CA   C  N S 424 
VAL C    C  N N 425 
VAL O    O  N N 426 
VAL CB   C  N N 427 
VAL CG1  C  N N 428 
VAL CG2  C  N N 429 
VAL OXT  O  N N 430 
VAL H    H  N N 431 
VAL H2   H  N N 432 
VAL HA   H  N N 433 
VAL HB   H  N N 434 
VAL HG11 H  N N 435 
VAL HG12 H  N N 436 
VAL HG13 H  N N 437 
VAL HG21 H  N N 438 
VAL HG22 H  N N 439 
VAL HG23 H  N N 440 
VAL HXT  H  N N 441 
ZN  ZN   ZN N N 442 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
V14 C18 O21  sing N N 358 
V14 C18 C15  sing N N 359 
V14 C15 S11  sing N N 360 
V14 O17 S11  doub N N 361 
V14 C22 C23  sing N N 362 
V14 C22 C14  sing N N 363 
V14 C23 C24  sing N N 364 
V14 N19 C14  sing N N 365 
V14 N19 C6   sing N N 366 
V14 C24 C25  sing N N 367 
V14 S11 C1   sing N N 368 
V14 S11 O16  doub N N 369 
V14 C14 C28  sing N N 370 
V14 C6  C1   doub Y N 371 
V14 C6  C5   sing Y N 372 
V14 C1  C2   sing Y N 373 
V14 F20 C5   sing N N 374 
V14 C25 C26  sing N N 375 
V14 C5  C4   doub Y N 376 
V14 C26 C27  sing N N 377 
V14 C28 C27  sing N N 378 
V14 C2  F13  sing N N 379 
V14 C2  C3   doub Y N 380 
V14 C4  C3   sing Y N 381 
V14 C4  S7   sing N N 382 
V14 C3  F12  sing N N 383 
V14 N10 S7   sing N N 384 
V14 S7  O9   doub N N 385 
V14 S7  O8   doub N N 386 
V14 N10 H1   sing N N 387 
V14 N10 H2   sing N N 388 
V14 C15 H3   sing N N 389 
V14 C15 H4   sing N N 390 
V14 C18 H5   sing N N 391 
V14 C18 H6   sing N N 392 
V14 O21 H7   sing N N 393 
V14 N19 H8   sing N N 394 
V14 C14 H9   sing N N 395 
V14 C28 H10  sing N N 396 
V14 C28 H11  sing N N 397 
V14 C27 H12  sing N N 398 
V14 C27 H13  sing N N 399 
V14 C26 H14  sing N N 400 
V14 C26 H15  sing N N 401 
V14 C25 H16  sing N N 402 
V14 C25 H17  sing N N 403 
V14 C24 H18  sing N N 404 
V14 C24 H19  sing N N 405 
V14 C23 H20  sing N N 406 
V14 C23 H21  sing N N 407 
V14 C22 H22  sing N N 408 
V14 C22 H23  sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                           ZN  
3 '3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' V14 
4 water                                                                                HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HLJ 
_pdbx_initial_refinement_model.details          'PDB ENTRY 3HLJ' 
# 
