data_4QSJ
# 
_entry.id   4QSJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.381 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4QSJ         pdb_00004qsj 10.2210/pdb4qsj/pdb 
RCSB  RCSB086458   ?            ?                   
WWPDB D_1000086458 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4QSA . unspecified 
PDB 4QSB . unspecified 
PDB 4QSI . unspecified 
# 
_pdbx_database_status.entry_id                        4QSJ 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2014-07-04 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
;Intrinsic Thermodynamics and Structure Correlation of Benzenesulfonamides with a Pyrimidine Moiety Binding to Carbonic Anhydrases I, II, VII, XII, and XIII
;
_citation.journal_abbrev            'Plos One' 
_citation.journal_volume            9 
_citation.page_first                e114106 
_citation.page_last                 e114106 
_citation.year                      2014 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25493428 
_citation.pdbx_database_id_DOI      10.1371/journal.pone.0114106 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kisonaite, M.'     1  ? 
primary 'Zubriene, A.'      2  ? 
primary 'Capkauskaite, E.'  3  ? 
primary 'Smirnov, A.'       4  ? 
primary 'Smirnoviene, J.'   5  ? 
primary 'Kairys, V.'        6  ? 
primary 'Michailoviene, V.' 7  ? 
primary 'Manakova, E.'      8  ? 
primary 'Grazulis, S.'      9  ? 
primary 'Matulis, D.'       10 ? 
# 
_cell.entry_id           4QSJ 
_cell.length_a           56.660 
_cell.length_b           57.780 
_cell.length_c           160.077 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4QSJ 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_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 13'                                                                     29613.318 2   
4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                                  65.409    2   ? ? ? 
? 
3 non-polymer syn '2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' 373.835   2   ? ? ? 
? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                                     106.120   2   ? ? ? 
? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                        78.133    1   ? ? ? 
? 
6 non-polymer syn 'CITRIC ACID'                                                                               192.124   2   ? ? ? 
? 
7 non-polymer syn 1,2-ETHANEDIOL                                                                              62.068    2   ? ? ? 
? 
8 non-polymer syn 'NICKEL (II) ION'                                                                           58.693    1   ? ? ? 
? 
9 water       nat water                                                                                       18.015    543 ? ? ? 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XIII, Carbonic anhydrase XIII, CA-XIII' 
# 
_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       
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_strand_id                 B,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   MET n 
1 3   SER n 
1 4   ARG n 
1 5   LEU n 
1 6   SER n 
1 7   TRP n 
1 8   GLY n 
1 9   TYR n 
1 10  ARG n 
1 11  GLU n 
1 12  HIS n 
1 13  ASN n 
1 14  GLY n 
1 15  PRO n 
1 16  ILE n 
1 17  HIS n 
1 18  TRP n 
1 19  LYS n 
1 20  GLU n 
1 21  PHE n 
1 22  PHE n 
1 23  PRO n 
1 24  ILE n 
1 25  ALA n 
1 26  ASP n 
1 27  GLY n 
1 28  ASP n 
1 29  GLN n 
1 30  GLN n 
1 31  SER n 
1 32  PRO n 
1 33  ILE n 
1 34  GLU n 
1 35  ILE n 
1 36  LYS n 
1 37  THR n 
1 38  LYS n 
1 39  GLU n 
1 40  VAL n 
1 41  LYS n 
1 42  TYR n 
1 43  ASP n 
1 44  SER n 
1 45  SER n 
1 46  LEU n 
1 47  ARG n 
1 48  PRO n 
1 49  LEU n 
1 50  SER n 
1 51  ILE n 
1 52  LYS n 
1 53  TYR n 
1 54  ASP n 
1 55  PRO n 
1 56  SER n 
1 57  SER n 
1 58  ALA n 
1 59  LYS n 
1 60  ILE n 
1 61  ILE n 
1 62  SER n 
1 63  ASN n 
1 64  SER n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  PHE n 
1 69  ASN n 
1 70  VAL n 
1 71  ASP n 
1 72  PHE n 
1 73  ASP n 
1 74  ASP n 
1 75  THR n 
1 76  GLU n 
1 77  ASN n 
1 78  LYS n 
1 79  SER n 
1 80  VAL n 
1 81  LEU n 
1 82  ARG n 
1 83  GLY n 
1 84  GLY n 
1 85  PRO n 
1 86  LEU n 
1 87  THR n 
1 88  GLY n 
1 89  SER n 
1 90  TYR n 
1 91  ARG n 
1 92  LEU n 
1 93  ARG n 
1 94  GLN n 
1 95  VAL n 
1 96  HIS n 
1 97  LEU n 
1 98  HIS n 
1 99  TRP n 
1 100 GLY n 
1 101 SER n 
1 102 ALA n 
1 103 ASP n 
1 104 ASP n 
1 105 HIS n 
1 106 GLY n 
1 107 SER n 
1 108 GLU n 
1 109 HIS n 
1 110 ILE n 
1 111 VAL n 
1 112 ASP n 
1 113 GLY n 
1 114 VAL n 
1 115 SER n 
1 116 TYR n 
1 117 ALA n 
1 118 ALA n 
1 119 GLU n 
1 120 LEU n 
1 121 HIS n 
1 122 VAL n 
1 123 VAL n 
1 124 HIS n 
1 125 TRP n 
1 126 ASN n 
1 127 SER n 
1 128 ASP n 
1 129 LYS n 
1 130 TYR n 
1 131 PRO n 
1 132 SER n 
1 133 PHE n 
1 134 VAL n 
1 135 GLU n 
1 136 ALA n 
1 137 ALA n 
1 138 HIS n 
1 139 GLU n 
1 140 PRO n 
1 141 ASP n 
1 142 GLY n 
1 143 LEU n 
1 144 ALA n 
1 145 VAL n 
1 146 LEU n 
1 147 GLY n 
1 148 VAL n 
1 149 PHE n 
1 150 LEU n 
1 151 GLN n 
1 152 ILE n 
1 153 GLY n 
1 154 GLU n 
1 155 PRO n 
1 156 ASN n 
1 157 SER n 
1 158 GLN n 
1 159 LEU n 
1 160 GLN n 
1 161 LYS n 
1 162 ILE n 
1 163 THR n 
1 164 ASP n 
1 165 THR n 
1 166 LEU n 
1 167 ASP n 
1 168 SER n 
1 169 ILE n 
1 170 LYS n 
1 171 GLU n 
1 172 LYS n 
1 173 GLY n 
1 174 LYS n 
1 175 GLN n 
1 176 THR n 
1 177 ARG n 
1 178 PHE n 
1 179 THR n 
1 180 ASN n 
1 181 PHE n 
1 182 ASP n 
1 183 LEU n 
1 184 LEU n 
1 185 SER n 
1 186 LEU n 
1 187 LEU n 
1 188 PRO n 
1 189 PRO n 
1 190 SER n 
1 191 TRP n 
1 192 ASP n 
1 193 TYR n 
1 194 TRP n 
1 195 THR n 
1 196 TYR n 
1 197 PRO n 
1 198 GLY n 
1 199 SER n 
1 200 LEU n 
1 201 THR n 
1 202 VAL n 
1 203 PRO n 
1 204 PRO n 
1 205 LEU n 
1 206 LEU n 
1 207 GLU n 
1 208 SER n 
1 209 VAL n 
1 210 THR n 
1 211 TRP n 
1 212 ILE n 
1 213 VAL n 
1 214 LEU n 
1 215 LYS n 
1 216 GLN n 
1 217 PRO n 
1 218 ILE n 
1 219 ASN n 
1 220 ILE n 
1 221 SER n 
1 222 SER n 
1 223 GLN n 
1 224 GLN n 
1 225 LEU n 
1 226 ALA n 
1 227 LYS n 
1 228 PHE n 
1 229 ARG n 
1 230 SER n 
1 231 LEU n 
1 232 LEU n 
1 233 CYS n 
1 234 THR n 
1 235 ALA n 
1 236 GLU n 
1 237 GLY n 
1 238 GLU n 
1 239 ALA n 
1 240 ALA n 
1 241 ALA n 
1 242 PHE n 
1 243 LEU n 
1 244 VAL n 
1 245 SER n 
1 246 ASN n 
1 247 HIS n 
1 248 ARG n 
1 249 PRO n 
1 250 PRO n 
1 251 GLN n 
1 252 PRO n 
1 253 LEU n 
1 254 LYS n 
1 255 GLY n 
1 256 ARG n 
1 257 LYS n 
1 258 VAL n 
1 259 ARG n 
1 260 ALA n 
1 261 SER n 
1 262 PHE n 
1 263 HIS 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                 CA13 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH13_HUMAN 
_struct_ref.pdbx_db_accession          Q8N1Q1 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSVL
RGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQK
ITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAAA
FLVSNHRPPQPLKGRKVRASFH
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 4QSJ B 2 ? 263 ? Q8N1Q1 1 ? 262 ? 0 261 
2 1 4QSJ A 2 ? 263 ? Q8N1Q1 1 ? 262 ? 0 261 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4QSJ MET B 1 ? UNP Q8N1Q1 ? ? 'expression tag' -1 1 
2 4QSJ MET A 1 ? UNP Q8N1Q1 ? ? 'expression tag' -1 2 
# 
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 
CIT non-polymer         . 'CITRIC ACID'                                                                               ? 'C6 H8 O7' 
192.124 
CYS 'L-peptide linking' y CYSTEINE                                                                                    ? 
'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                                        ? 
'C2 H6 O S'           78.133  
EDO non-polymer         . 1,2-ETHANEDIOL                                                                              
'ETHYLENE GLYCOL' 'C2 H6 O2'            62.068  
EWW non-polymer         . '2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' ? 
'C13 H12 Cl N3 O4 S2' 373.835 
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 
NI  non-polymer         . 'NICKEL (II) ION'                                                                           ? 'Ni 2' 
58.693  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                                     ? 
'C4 H10 O3'           106.120 
PHE 'L-peptide linking' y PHENYLALANINE                                                                               ? 
'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                                                     ? 
'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                                                      ? 
'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                                                                   ? 
'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                  ? 
'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                    ? 
'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                                                                      ? 
'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                                                                  ? 'Zn 2' 
65.409  
# 
_exptl.entry_id          4QSJ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.21 
_exptl_crystal.density_percent_sol   44.40 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
'0.1M sodium citrate (pH 5.5), 0.2M sodium acetate (pH 4.5), 28% PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2011-11-18 
_diffrn_detector.details                'Mirror Bent, vertically focussing' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8123 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.8123 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4QSJ 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             39.112 
_reflns.d_resolution_high            1.629 
_reflns.number_obs                   57690 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.200 
_reflns.pdbx_Rmerge_I_obs            0.060 
_reflns.pdbx_Rsym_value              0.060 
_reflns.pdbx_netI_over_sigmaI        18.100 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              5.200 
_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         ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_chi_squared 
1 1  1.70 1.79  99.30 0.377 0.377 2.0  5.20 ? ? ? ? ? ? 
1 2  1.79 1.90  99.50 0.252 0.252 2.8  5.20 ? ? ? ? ? ? 
1 3  1.90 2.03  99.60 0.163 0.163 4.5  5.20 ? ? ? ? ? ? 
1 4  2.03 2.19  99.60 0.110 0.110 6.8  5.20 ? ? ? ? ? ? 
1 5  2.19 2.40  99.90 0.080 0.080 9.4  5.20 ? ? ? ? ? ? 
1 6  2.40 2.69  99.80 0.062 0.062 12.1 5.20 ? ? ? ? ? ? 
1 7  2.69 3.10  99.50 0.044 0.044 16.6 5.20 ? ? ? ? ? ? 
1 8  3.10 3.80  98.80 0.030 0.030 22.7 5.20 ? ? ? ? ? ? 
1 9  3.80 5.38  97.70 0.025 0.025 25.3 5.20 ? ? ? ? ? ? 
1 10 5.38 39.11 93.10 0.028 0.028 23.4 5.00 ? ? ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4QSJ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     52172 
_refine.ls_number_reflns_all                     57640 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             27.87 
_refine.ls_d_res_high                            1.70 
_refine.ls_percent_reflns_obs                    98.79 
_refine.ls_R_factor_obs                          0.16781 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.16370 
_refine.ls_R_factor_R_free                       0.20422 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 10.1 
_refine.ls_number_reflns_R_free                  5865 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            0.01 
_refine.occupancy_max                            1.00 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.942 
_refine.B_iso_mean                               17.402 
_refine.aniso_B[1][1]                            0.26 
_refine.aniso_B[2][2]                            0.24 
_refine.aniso_B[3][3]                            -0.50 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.pdbx_starting_model                      2NNO 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.113 
_refine.pdbx_overall_ESU_R_Free                  0.111 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.116 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4127 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         101 
_refine_hist.number_atoms_solvent             543 
_refine_hist.number_atoms_total               4771 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        27.87 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.025  0.020  ? 4535 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.278  1.969  ? 6199 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.771  5.000  ? 551  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.936 24.135 ? 208  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.045 15.000 ? 713  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       12.763 15.000 ? 22   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.192  0.200  ? 644  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.013  0.021  ? 3576 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.700 
_refine_ls_shell.d_res_low                        1.744 
_refine_ls_shell.number_reflns_R_work             3806 
_refine_ls_shell.R_factor_R_work                  0.275 
_refine_ls_shell.percent_reflns_obs               99.18 
_refine_ls_shell.R_factor_R_free                  0.322 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             420 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  4QSJ 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme XIII with 2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)thio]acetyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4QSJ 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 4 ? 
I N N 7 ? 
J N N 6 ? 
K N N 7 ? 
L N N 2 ? 
M N N 3 ? 
N N N 8 ? 
O N N 9 ? 
P N N 9 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  GLY A 14  ? ILE A 16  ? GLY B 12  ILE B 14  5 ? 3 
HELX_P HELX_P2  2  HIS A 17  ? PHE A 22  ? HIS B 15  PHE B 20  1 ? 6 
HELX_P HELX_P3  3  PRO A 23  ? GLY A 27  ? PRO B 21  GLY B 25  5 ? 5 
HELX_P HELX_P4  4  LYS A 36  ? VAL A 40  ? LYS B 34  VAL B 38  5 ? 5 
HELX_P HELX_P5  5  SER A 132 ? ALA A 137 ? SER B 130 ALA B 135 1 ? 6 
HELX_P HELX_P6  6  ASN A 156 ? ASP A 164 ? ASN B 154 ASP B 162 1 ? 9 
HELX_P HELX_P7  7  THR A 165 ? LYS A 170 ? THR B 163 LYS B 168 5 ? 6 
HELX_P HELX_P8  8  ASP A 182 ? LEU A 187 ? ASP B 180 LEU B 185 1 ? 6 
HELX_P HELX_P9  9  SER A 221 ? ARG A 229 ? SER B 219 ARG B 227 1 ? 9 
HELX_P HELX_P10 10 GLY B 14  ? PHE B 21  ? GLY A 12  PHE A 19  5 ? 8 
HELX_P HELX_P11 11 PHE B 22  ? GLY B 27  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P12 12 LYS B 36  ? VAL B 40  ? LYS A 34  VAL A 38  5 ? 5 
HELX_P HELX_P13 13 ASP B 54  ? SER B 56  ? ASP A 52  SER A 54  5 ? 3 
HELX_P HELX_P14 14 SER B 132 ? ALA B 137 ? SER A 130 ALA A 135 1 ? 6 
HELX_P HELX_P15 15 ASN B 156 ? GLN B 158 ? ASN A 154 GLN A 156 5 ? 3 
HELX_P HELX_P16 16 LEU B 159 ? ASP B 164 ? LEU A 157 ASP A 162 1 ? 6 
HELX_P HELX_P17 17 THR B 165 ? LYS B 170 ? THR A 163 LYS A 168 5 ? 6 
HELX_P HELX_P18 18 LEU B 183 ? LEU B 187 ? LEU A 181 LEU A 185 5 ? 5 
HELX_P HELX_P19 19 SER B 221 ? ARG B 229 ? 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 96  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 94  B ZN  301 1_555 ? ? ? ? ? ? ? 1.956 ? ? 
metalc2  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 2.122 ? ? 
metalc3  metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 119 B ZN  301 1_555 ? ? ? ? ? ? ? 2.074 ? ? 
metalc4  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D EWW . N11 B ? B ZN  301 B EWW 302 1_555 ? ? ? ? ? ? ? 1.718 ? ? 
metalc5  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D EWW . N11 A ? B ZN  301 B EWW 302 1_555 ? ? ? ? ? ? ? 1.865 ? ? 
metalc6  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D EWW . O8  A ? B ZN  301 B EWW 302 1_555 ? ? ? ? ? ? ? 2.655 ? ? 
metalc7  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D EWW . S6  A ? B ZN  301 B EWW 302 1_555 ? ? ? ? ? ? ? 2.975 ? ? 
metalc8  metalc ? ? B HIS 96  NE2 ? ? ? 1_555 L ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc9  metalc ? ? B HIS 98  NE2 ? ? ? 1_555 L ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc10 metalc ? ? B HIS 121 ND1 ? ? ? 1_555 L ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc11 metalc ? ? L ZN  .   ZN  ? ? ? 1_555 M EWW . N11 ? ? A ZN  301 A EWW 302 1_555 ? ? ? ? ? ? ? 1.841 ? ? 
# 
_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 31  A . ? SER 29  B PRO 32  A ? PRO 30  B 1 0.65  
2 PRO 203 A . ? PRO 201 B PRO 204 A ? PRO 202 B 1 12.89 
3 SER 31  B . ? SER 29  A PRO 32  B ? PRO 30  A 1 -1.39 
4 PRO 203 B . ? PRO 201 A PRO 204 B ? PRO 202 A 1 12.86 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
D ? 2  ? 
E ? 10 ? 
F ? 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      
D 1 2  ? parallel      
E 1 2  ? parallel      
E 2 3  ? anti-parallel 
E 3 4  ? anti-parallel 
E 4 5  ? parallel      
E 5 6  ? anti-parallel 
E 6 7  ? anti-parallel 
E 7 8  ? anti-parallel 
E 8 9  ? anti-parallel 
E 9 10 ? anti-parallel 
F 1 2  ? anti-parallel 
F 2 3  ? anti-parallel 
F 3 4  ? anti-parallel 
F 4 5  ? anti-parallel 
F 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  GLU A 34  ? ILE A 35  ? GLU B 32  ILE B 33  
A 2  ILE A 110 ? VAL A 111 ? ILE B 108 VAL B 109 
B 1  LYS A 41  ? TYR A 42  ? LYS B 39  TYR B 40  
B 2  ARG A 259 ? ALA A 260 ? ARG B 257 ALA B 258 
B 3  TYR A 193 ? GLY A 198 ? TYR B 191 GLY B 196 
B 4  VAL A 209 ? LEU A 214 ? VAL B 207 LEU B 212 
B 5  LEU A 143 ? ILE A 152 ? LEU B 141 ILE B 150 
B 6  ALA A 118 ? ASN A 126 ? ALA B 116 ASN B 124 
B 7  TYR A 90  ? TRP A 99  ? TYR B 88  TRP B 97  
B 8  PHE A 68  ? PHE A 72  ? PHE B 66  PHE B 70  
B 9  ALA A 58  ? ASN A 63  ? ALA B 56  ASN B 61  
B 10 GLN A 175 ? ARG A 177 ? GLN B 173 ARG B 175 
C 1  LEU A 49  ? LYS A 52  ? LEU B 47  LYS B 50  
C 2  VAL A 80  ? GLY A 83  ? VAL B 78  GLY B 81  
C 3  TYR A 90  ? TRP A 99  ? TYR B 88  TRP B 97  
C 4  ALA A 118 ? ASN A 126 ? ALA B 116 ASN B 124 
C 5  LEU A 143 ? ILE A 152 ? LEU B 141 ILE B 150 
C 6  ILE A 218 ? ILE A 220 ? ILE B 216 ILE B 218 
D 1  GLU B 34  ? ILE B 35  ? GLU A 32  ILE A 33  
D 2  ILE B 110 ? VAL B 111 ? ILE A 108 VAL A 109 
E 1  LYS B 41  ? TYR B 42  ? LYS A 39  TYR A 40  
E 2  ARG B 259 ? ALA B 260 ? ARG A 257 ALA A 258 
E 3  TYR B 193 ? GLY B 198 ? TYR A 191 GLY A 196 
E 4  VAL B 209 ? LEU B 214 ? VAL A 207 LEU A 212 
E 5  LEU B 143 ? ILE B 152 ? LEU A 141 ILE A 150 
E 6  ALA B 118 ? ASN B 126 ? ALA A 116 ASN A 124 
E 7  TYR B 90  ? TRP B 99  ? TYR A 88  TRP A 97  
E 8  PHE B 68  ? PHE B 72  ? PHE A 66  PHE A 70  
E 9  ALA B 58  ? ASN B 63  ? ALA A 56  ASN A 61  
E 10 GLN B 175 ? ARG B 177 ? GLN A 173 ARG A 175 
F 1  ARG B 47  ? LYS B 52  ? ARG A 45  LYS A 50  
F 2  VAL B 80  ? GLY B 84  ? VAL A 78  GLY A 82  
F 3  TYR B 90  ? TRP B 99  ? TYR A 88  TRP A 97  
F 4  ALA B 118 ? ASN B 126 ? ALA A 116 ASN A 124 
F 5  LEU B 143 ? ILE B 152 ? LEU A 141 ILE A 150 
F 6  ILE B 218 ? ILE B 220 ? ILE A 216 ILE 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 35  ? N ILE B 33  O ILE A 110 ? O ILE B 108 
B 1 2  N LYS A 41  ? N LYS B 39  O ALA A 260 ? O ALA B 258 
B 2 3  O ARG A 259 ? O ARG B 257 N THR A 195 ? N THR B 193 
B 3 4  N GLY A 198 ? N GLY B 196 O VAL A 209 ? O VAL B 207 
B 4 5  O ILE A 212 ? O ILE B 210 N GLY A 147 ? N GLY B 145 
B 5 6  O VAL A 148 ? O VAL B 146 N LEU A 120 ? N LEU B 118 
B 6 7  O TRP A 125 ? O TRP B 123 N ARG A 91  ? N ARG B 89  
B 7 8  O VAL A 95  ? O VAL B 93  N VAL A 70  ? N VAL B 68  
B 8 9  O ASP A 71  ? O ASP B 69  N ILE A 60  ? N ILE B 58  
B 9 10 N ILE A 61  ? N ILE B 59  O THR A 176 ? O THR B 174 
C 1 2  N SER A 50  ? N SER B 48  O ARG A 82  ? O ARG B 80  
C 2 3  N LEU A 81  ? N LEU B 79  O TYR A 90  ? O TYR B 88  
C 3 4  N ARG A 91  ? N ARG B 89  O TRP A 125 ? O TRP B 123 
C 4 5  N LEU A 120 ? N LEU B 118 O VAL A 148 ? O VAL B 146 
C 5 6  N GLN A 151 ? N GLN B 149 O ILE A 218 ? O ILE B 216 
D 1 2  N ILE B 35  ? N ILE A 33  O ILE B 110 ? O ILE A 108 
E 1 2  N LYS B 41  ? N LYS A 39  O ALA B 260 ? O ALA A 258 
E 2 3  O ARG B 259 ? O ARG A 257 N THR B 195 ? N THR A 193 
E 3 4  N GLY B 198 ? N GLY A 196 O VAL B 209 ? O VAL A 207 
E 4 5  O LEU B 214 ? O LEU A 212 N GLY B 147 ? N GLY A 145 
E 5 6  O VAL B 148 ? O VAL A 146 N LEU B 120 ? N LEU A 118 
E 6 7  O TRP B 125 ? O TRP A 123 N ARG B 91  ? N ARG A 89  
E 7 8  O VAL B 95  ? O VAL A 93  N VAL B 70  ? N VAL A 68  
E 8 9  O ASP B 71  ? O ASP A 69  N LYS B 59  ? N LYS A 57  
E 9 10 N ILE B 61  ? N ILE A 59  O THR B 176 ? O THR A 174 
F 1 2  N SER B 50  ? N SER A 48  O ARG B 82  ? O ARG A 80  
F 2 3  N LEU B 81  ? N LEU A 79  O TYR B 90  ? O TYR A 88  
F 3 4  N ARG B 91  ? N ARG A 89  O TRP B 125 ? O TRP A 123 
F 4 5  N LEU B 120 ? N LEU A 118 O VAL B 148 ? O VAL A 146 
F 5 6  N GLN B 151 ? N GLN A 149 O ILE B 218 ? 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 B ZN  301 ? 5  'BINDING SITE FOR RESIDUE ZN B 301'  
AC2 Software B EWW 302 ? 19 'BINDING SITE FOR RESIDUE EWW B 302' 
AC3 Software B PEG 303 ? 6  'BINDING SITE FOR RESIDUE PEG B 303' 
AC4 Software B DMS 304 ? 1  'BINDING SITE FOR RESIDUE DMS B 304' 
AC5 Software B CIT 305 ? 9  'BINDING SITE FOR RESIDUE CIT B 305' 
AC6 Software B PEG 306 ? 9  'BINDING SITE FOR RESIDUE PEG B 306' 
AC7 Software B EDO 307 ? 4  'BINDING SITE FOR RESIDUE EDO B 307' 
AC8 Software B CIT 308 ? 14 'BINDING SITE FOR RESIDUE CIT B 308' 
AC9 Software B EDO 309 ? 7  'BINDING SITE FOR RESIDUE EDO B 309' 
BC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
BC2 Software A EWW 302 ? 15 'BINDING SITE FOR RESIDUE EWW A 302' 
BC3 Software A NI  303 ? 4  'BINDING SITE FOR RESIDUE NI A 303'  
# 
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 5  HIS A 96  ? HIS B 94  . ? 1_555 ? 
2  AC1 5  HIS A 98  ? HIS B 96  . ? 1_555 ? 
3  AC1 5  HIS A 121 ? HIS B 119 . ? 1_555 ? 
4  AC1 5  THR A 201 ? THR B 199 . ? 1_555 ? 
5  AC1 5  EWW D .   ? EWW B 302 . ? 1_555 ? 
6  AC2 19 ARG A 93  ? ARG B 91  . ? 1_555 ? 
7  AC2 19 GLN A 94  ? GLN B 92  . ? 1_555 ? 
8  AC2 19 HIS A 96  ? HIS B 94  . ? 1_555 ? 
9  AC2 19 HIS A 98  ? HIS B 96  . ? 1_555 ? 
10 AC2 19 HIS A 121 ? HIS B 119 . ? 1_555 ? 
11 AC2 19 VAL A 123 ? VAL B 121 . ? 1_555 ? 
12 AC2 19 PHE A 133 ? PHE B 131 . ? 1_555 ? 
13 AC2 19 VAL A 134 ? VAL B 132 . ? 1_555 ? 
14 AC2 19 VAL A 145 ? VAL B 143 . ? 1_555 ? 
15 AC2 19 SER A 199 ? SER B 197 . ? 1_555 ? 
16 AC2 19 LEU A 200 ? LEU B 198 . ? 1_555 ? 
17 AC2 19 THR A 201 ? THR B 199 . ? 1_555 ? 
18 AC2 19 VAL A 202 ? VAL B 200 . ? 1_555 ? 
19 AC2 19 PRO A 204 ? PRO B 202 . ? 1_555 ? 
20 AC2 19 VAL A 209 ? VAL B 207 . ? 1_555 ? 
21 AC2 19 TRP A 211 ? TRP B 209 . ? 1_555 ? 
22 AC2 19 ZN  C .   ? ZN  B 301 . ? 1_555 ? 
23 AC2 19 HOH O .   ? HOH B 640 . ? 1_555 ? 
24 AC2 19 HOH O .   ? HOH B 667 . ? 1_555 ? 
25 AC3 6  ASP B 28  ? ASP A 26  . ? 1_565 ? 
26 AC3 6  GLN B 29  ? GLN A 27  . ? 1_565 ? 
27 AC3 6  LYS B 254 ? LYS A 252 . ? 1_565 ? 
28 AC3 6  ARG B 256 ? ARG A 254 . ? 1_565 ? 
29 AC3 6  LYS A 59  ? LYS B 57  . ? 1_555 ? 
30 AC3 6  ARG A 177 ? ARG B 175 . ? 1_555 ? 
31 AC4 1  ASP A 141 ? ASP B 139 . ? 1_555 ? 
32 AC5 9  ASP B 128 ? ASP A 126 . ? 4_545 ? 
33 AC5 9  HOH P .   ? HOH A 602 . ? 4_545 ? 
34 AC5 9  GLY A 100 ? GLY B 98  . ? 1_555 ? 
35 AC5 9  SER A 101 ? SER B 99  . ? 1_555 ? 
36 AC5 9  HIS A 105 ? HIS B 103 . ? 1_555 ? 
37 AC5 9  SER A 245 ? SER B 243 . ? 1_555 ? 
38 AC5 9  HIS A 247 ? HIS B 245 . ? 1_555 ? 
39 AC5 9  HOH O .   ? HOH B 437 . ? 1_555 ? 
40 AC5 9  HOH O .   ? HOH B 534 . ? 1_555 ? 
41 AC6 9  THR B 75  ? THR A 73  . ? 4_545 ? 
42 AC6 9  GLU B 76  ? GLU A 74  . ? 4_545 ? 
43 AC6 9  ASP A 103 ? ASP B 101 . ? 1_555 ? 
44 AC6 9  ASP A 104 ? ASP B 102 . ? 1_555 ? 
45 AC6 9  ILE A 152 ? ILE B 150 . ? 1_555 ? 
46 AC6 9  SER A 222 ? SER B 220 . ? 1_555 ? 
47 AC6 9  HOH O .   ? HOH B 536 . ? 1_555 ? 
48 AC6 9  HOH O .   ? HOH B 631 . ? 1_555 ? 
49 AC6 9  HOH O .   ? HOH B 678 . ? 1_555 ? 
50 AC7 4  ARG B 82  ? ARG A 80  . ? 1_555 ? 
51 AC7 4  PRO A 189 ? PRO B 187 . ? 1_555 ? 
52 AC7 4  SER A 190 ? SER B 188 . ? 1_555 ? 
53 AC7 4  HOH O .   ? HOH B 603 . ? 1_555 ? 
54 AC8 14 LYS A 38  ? LYS B 36  . ? 1_555 ? 
55 AC8 14 GLU A 39  ? GLU B 37  . ? 1_555 ? 
56 AC8 14 ASP A 112 ? ASP B 110 . ? 1_555 ? 
57 AC8 14 GLN A 160 ? GLN B 158 . ? 4_545 ? 
58 AC8 14 THR A 163 ? THR B 161 . ? 4_545 ? 
59 AC8 14 ASP A 164 ? ASP B 162 . ? 4_545 ? 
60 AC8 14 GLN A 223 ? GLN B 221 . ? 4_545 ? 
61 AC8 14 GLN A 224 ? GLN B 222 . ? 4_545 ? 
62 AC8 14 LYS A 227 ? LYS B 225 . ? 4_545 ? 
63 AC8 14 HOH O .   ? HOH B 449 . ? 1_555 ? 
64 AC8 14 HOH O .   ? HOH B 471 . ? 1_555 ? 
65 AC8 14 HOH O .   ? HOH B 549 . ? 4_545 ? 
66 AC8 14 HOH O .   ? HOH B 589 . ? 1_555 ? 
67 AC8 14 HOH O .   ? HOH B 608 . ? 4_545 ? 
68 AC9 7  ASN A 156 ? ASN B 154 . ? 1_555 ? 
69 AC9 7  SER A 157 ? SER B 155 . ? 1_555 ? 
70 AC9 7  GLN A 158 ? GLN B 156 . ? 1_555 ? 
71 AC9 7  SER A 185 ? SER B 183 . ? 1_555 ? 
72 AC9 7  HOH O .   ? HOH B 432 . ? 1_555 ? 
73 AC9 7  HOH O .   ? HOH B 452 . ? 4_445 ? 
74 AC9 7  HOH O .   ? HOH B 680 . ? 1_555 ? 
75 BC1 4  HIS B 96  ? HIS A 94  . ? 1_555 ? 
76 BC1 4  HIS B 98  ? HIS A 96  . ? 1_555 ? 
77 BC1 4  HIS B 121 ? HIS A 119 . ? 1_555 ? 
78 BC1 4  EWW M .   ? EWW A 302 . ? 1_555 ? 
79 BC2 15 HIS B 96  ? HIS A 94  . ? 1_555 ? 
80 BC2 15 HIS B 98  ? HIS A 96  . ? 1_555 ? 
81 BC2 15 HIS B 121 ? HIS A 119 . ? 1_555 ? 
82 BC2 15 PHE B 133 ? PHE A 131 . ? 1_555 ? 
83 BC2 15 VAL B 134 ? VAL A 132 . ? 1_555 ? 
84 BC2 15 HIS B 138 ? HIS A 136 . ? 1_555 ? 
85 BC2 15 VAL B 145 ? VAL A 143 . ? 1_555 ? 
86 BC2 15 LEU B 200 ? LEU A 198 . ? 1_555 ? 
87 BC2 15 THR B 201 ? THR A 199 . ? 1_555 ? 
88 BC2 15 VAL B 202 ? VAL A 200 . ? 1_555 ? 
89 BC2 15 TRP B 211 ? TRP A 209 . ? 1_555 ? 
90 BC2 15 ZN  L .   ? ZN  A 301 . ? 1_555 ? 
91 BC2 15 HOH P .   ? HOH A 597 . ? 1_555 ? 
92 BC2 15 HOH P .   ? HOH A 637 . ? 1_555 ? 
93 BC2 15 HOH P .   ? HOH A 638 . ? 1_555 ? 
94 BC3 4  SER B 101 ? SER A 99  . ? 1_555 ? 
95 BC3 4  HIS B 105 ? HIS A 103 . ? 1_555 ? 
96 BC3 4  SER B 245 ? SER A 243 . ? 1_555 ? 
97 BC3 4  HIS B 247 ? HIS A 245 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4QSJ 
_atom_sites.fract_transf_matrix[1][1]   0.017649 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017307 
_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]   0.006247 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
NI 
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   . SER A 1 6   ? 1.329   12.763  12.038  1.00  34.43 ? 4   SER B N   1 
ATOM   2    C  CA  . SER A 1 6   ? 0.686   11.563  12.720  1.00  31.15 ? 4   SER B CA  1 
ATOM   3    C  C   . SER A 1 6   ? 0.801   10.257  11.935  1.00  28.98 ? 4   SER B C   1 
ATOM   4    O  O   . SER A 1 6   ? 0.921   10.251  10.711  1.00  26.28 ? 4   SER B O   1 
ATOM   5    C  CB  . SER A 1 6   ? -0.732  11.837  13.192  1.00  39.15 ? 4   SER B CB  1 
ATOM   6    O  OG  . SER A 1 6   ? -0.862  11.352  14.537  1.00  45.37 ? 4   SER B OG  1 
ATOM   7    N  N   . TRP A 1 7   ? 0.817   9.147   12.656  1.00  21.46 ? 5   TRP B N   1 
ATOM   8    C  CA  . TRP A 1 7   ? 0.998   7.815   12.009  1.00  16.90 ? 5   TRP B CA  1 
ATOM   9    C  C   . TRP A 1 7   ? -0.017  7.506   10.948  1.00  16.22 ? 5   TRP B C   1 
ATOM   10   O  O   . TRP A 1 7   ? -1.146  7.948   11.042  1.00  17.73 ? 5   TRP B O   1 
ATOM   11   C  CB  . TRP A 1 7   ? 1.063   6.721   13.112  1.00  16.68 ? 5   TRP B CB  1 
ATOM   12   C  CG  . TRP A 1 7   ? -0.271  6.342   13.719  1.00  18.05 ? 5   TRP B CG  1 
ATOM   13   C  CD1 . TRP A 1 7   ? -0.875  6.875   14.857  1.00  16.93 ? 5   TRP B CD1 1 
ATOM   14   C  CD2 . TRP A 1 7   ? -1.206  5.313   13.246  1.00  16.96 ? 5   TRP B CD2 1 
ATOM   15   N  NE1 . TRP A 1 7   ? -2.084  6.272   15.101  1.00  19.43 ? 5   TRP B NE1 1 
ATOM   16   C  CE2 . TRP A 1 7   ? -2.342  5.328   14.173  1.00  17.89 ? 5   TRP B CE2 1 
ATOM   17   C  CE3 . TRP A 1 7   ? -1.216  4.423   12.186  1.00  17.49 ? 5   TRP B CE3 1 
ATOM   18   C  CZ2 . TRP A 1 7   ? -3.424  4.479   14.021  1.00  18.64 ? 5   TRP B CZ2 1 
ATOM   19   C  CZ3 . TRP A 1 7   ? -2.313  3.572   12.044  1.00  17.07 ? 5   TRP B CZ3 1 
ATOM   20   C  CH2 . TRP A 1 7   ? -3.389  3.601   12.940  1.00  17.88 ? 5   TRP B CH2 1 
ATOM   21   N  N   . GLY A 1 8   ? 0.379   6.731   9.938   1.00  15.86 ? 6   GLY B N   1 
ATOM   22   C  CA  . GLY A 1 8   ? -0.558  6.258   8.912   1.00  14.67 ? 6   GLY B CA  1 
ATOM   23   C  C   . GLY A 1 8   ? 0.039   5.106   8.156   1.00  14.13 ? 6   GLY B C   1 
ATOM   24   O  O   . GLY A 1 8   ? 0.778   4.282   8.739   1.00  13.76 ? 6   GLY B O   1 
ATOM   25   N  N   . TYR A 1 9   ? -0.264  5.051   6.856   1.00  13.57 ? 7   TYR B N   1 
ATOM   26   C  CA  . TYR A 1 9   ? 0.266   4.003   5.987   1.00  13.45 ? 7   TYR B CA  1 
ATOM   27   C  C   . TYR A 1 9   ? 0.932   4.545   4.742   1.00  17.26 ? 7   TYR B C   1 
ATOM   28   O  O   . TYR A 1 9   ? 1.201   3.779   3.801   1.00  19.44 ? 7   TYR B O   1 
ATOM   29   C  CB  . TYR A 1 9   ? -0.922  3.105   5.567   1.00  13.72 ? 7   TYR B CB  1 
ATOM   30   C  CG  . TYR A 1 9   ? -1.461  2.381   6.786   1.00  10.99 ? 7   TYR B CG  1 
ATOM   31   C  CD1 . TYR A 1 9   ? -0.876  1.174   7.189   1.00  11.05 ? 7   TYR B CD1 1 
ATOM   32   C  CD2 . TYR A 1 9   ? -2.563  2.853   7.494   1.00  11.84 ? 7   TYR B CD2 1 
ATOM   33   C  CE1 . TYR A 1 9   ? -1.379  0.449   8.287   1.00  10.23 ? 7   TYR B CE1 1 
ATOM   34   C  CE2 . TYR A 1 9   ? -3.105  2.141   8.578   1.00  11.37 ? 7   TYR B CE2 1 
ATOM   35   C  CZ  . TYR A 1 9   ? -2.508  0.962   8.949   1.00  11.15 ? 7   TYR B CZ  1 
ATOM   36   O  OH  . TYR A 1 9   ? -3.031  0.197   10.015  1.00  11.27 ? 7   TYR B OH  1 
ATOM   37   N  N   . ARG A 1 10  ? 1.254   5.846   4.811   1.00  18.83 ? 8   ARG B N   1 
ATOM   38   C  CA  . ARG A 1 10  ? 1.895   6.525   3.676   1.00  20.47 ? 8   ARG B CA  1 
ATOM   39   C  C   . ARG A 1 10  ? 3.397   6.420   3.822   1.00  20.39 ? 8   ARG B C   1 
ATOM   40   O  O   . ARG A 1 10  ? 3.920   5.796   4.758   1.00  19.56 ? 8   ARG B O   1 
ATOM   41   C  CB  . ARG A 1 10  ? 1.404   7.957   3.575   1.00  22.78 ? 8   ARG B CB  1 
ATOM   42   C  CG  . ARG A 1 10  ? 0.007   8.028   2.951   1.00  27.37 ? 8   ARG B CG  1 
ATOM   43   C  CD  . ARG A 1 10  ? -0.658  9.332   3.373   1.00  28.03 ? 8   ARG B CD  1 
ATOM   44   N  NE  . ARG A 1 10  ? -0.401  10.378  2.396   1.00  36.08 ? 8   ARG B NE  1 
ATOM   45   C  CZ  . ARG A 1 10  ? -0.815  11.638  2.494   1.00  33.80 ? 8   ARG B CZ  1 
ATOM   46   N  NH1 . ARG A 1 10  ? -1.465  12.052  3.574   1.00  38.16 ? 8   ARG B NH1 1 
ATOM   47   N  NH2 . ARG A 1 10  ? -0.538  12.486  1.521   1.00  36.92 ? 8   ARG B NH2 1 
ATOM   48   N  N   . GLU A 1 11  ? 4.134   6.932   2.841   1.00  23.35 ? 9   GLU B N   1 
ATOM   49   C  CA  . GLU A 1 11  ? 5.602   6.732   2.832   1.00  26.66 ? 9   GLU B CA  1 
ATOM   50   C  C   . GLU A 1 11  ? 6.328   7.243   4.092   1.00  22.64 ? 9   GLU B C   1 
ATOM   51   O  O   . GLU A 1 11  ? 7.215   6.547   4.653   1.00  26.24 ? 9   GLU B O   1 
ATOM   52   C  CB  . GLU A 1 11  ? 6.201   7.351   1.555   1.00  33.93 ? 9   GLU B CB  1 
ATOM   53   C  CG  . GLU A 1 11  ? 7.723   7.562   1.604   1.00  38.29 ? 9   GLU B CG  1 
ATOM   54   C  CD  . GLU A 1 11  ? 8.287   8.062   0.278   1.00  49.18 ? 9   GLU B CD  1 
ATOM   55   O  OE1 . GLU A 1 11  ? 7.826   9.123   -0.215  1.00  52.17 ? 9   GLU B OE1 1 
ATOM   56   O  OE2 . GLU A 1 11  ? 9.199   7.391   -0.263  1.00  55.12 ? 9   GLU B OE2 1 
ATOM   57   N  N   A HIS A 1 12  ? 5.891   8.410   4.538   0.50  25.30 ? 10  HIS B N   1 
ATOM   58   N  N   B HIS A 1 12  ? 5.988   8.429   4.588   0.50  24.94 ? 10  HIS B N   1 
ATOM   59   C  CA  A HIS A 1 12  ? 6.554   9.149   5.608   0.50  25.85 ? 10  HIS B CA  1 
ATOM   60   C  CA  B HIS A 1 12  ? 6.752   9.020   5.732   0.50  24.43 ? 10  HIS B CA  1 
ATOM   61   C  C   A HIS A 1 12  ? 6.192   8.662   6.989   0.50  23.86 ? 10  HIS B C   1 
ATOM   62   C  C   B HIS A 1 12  ? 6.081   8.881   7.083   0.50  22.55 ? 10  HIS B C   1 
ATOM   63   O  O   A HIS A 1 12  ? 7.033   8.675   7.923   0.50  21.96 ? 10  HIS B O   1 
ATOM   64   O  O   B HIS A 1 12  ? 6.563   9.402   8.110   0.50  19.74 ? 10  HIS B O   1 
ATOM   65   C  CB  A HIS A 1 12  ? 6.230   10.641  5.462   0.50  28.57 ? 10  HIS B CB  1 
ATOM   66   C  CB  B HIS A 1 12  ? 7.007   10.503  5.515   0.50  27.28 ? 10  HIS B CB  1 
ATOM   67   C  CG  A HIS A 1 12  ? 4.750   10.964  5.298   0.50  30.94 ? 10  HIS B CG  1 
ATOM   68   C  CG  B HIS A 1 12  ? 7.675   10.835  4.205   0.50  28.17 ? 10  HIS B CG  1 
ATOM   69   N  ND1 A HIS A 1 12  ? 4.066   10.746  4.136   0.50  30.01 ? 10  HIS B ND1 1 
ATOM   70   N  ND1 B HIS A 1 12  ? 8.929   10.443  3.912   0.50  28.35 ? 10  HIS B ND1 1 
ATOM   71   C  CD2 A HIS A 1 12  ? 3.844   11.573  6.183   0.50  30.78 ? 10  HIS B CD2 1 
ATOM   72   C  CD2 B HIS A 1 12  ? 7.247   11.621  3.134   0.50  27.89 ? 10  HIS B CD2 1 
ATOM   73   C  CE1 A HIS A 1 12  ? 2.798   11.200  4.287   0.50  30.02 ? 10  HIS B CE1 1 
ATOM   74   C  CE1 B HIS A 1 12  ? 9.265   10.902  2.695   0.50  26.63 ? 10  HIS B CE1 1 
ATOM   75   N  NE2 A HIS A 1 12  ? 2.665   11.692  5.540   0.50  31.21 ? 10  HIS B NE2 1 
ATOM   76   N  NE2 B HIS A 1 12  ? 8.235   11.618  2.218   0.50  27.01 ? 10  HIS B NE2 1 
ATOM   77   N  N   . ASN A 1 13  ? 4.934   8.211   7.111   1.00  19.56 ? 11  ASN B N   1 
ATOM   78   C  CA  . ASN A 1 13  ? 4.340   7.907   8.396   1.00  17.76 ? 11  ASN B CA  1 
ATOM   79   C  C   . ASN A 1 13  ? 3.905   6.462   8.539   1.00  15.12 ? 11  ASN B C   1 
ATOM   80   O  O   . ASN A 1 13  ? 3.184   6.153   9.515   1.00  15.66 ? 11  ASN B O   1 
ATOM   81   C  CB  . ASN A 1 13  ? 3.149   8.856   8.663   1.00  18.68 ? 11  ASN B CB  1 
ATOM   82   C  CG  . ASN A 1 13  ? 1.934   8.629   7.726   1.00  17.04 ? 11  ASN B CG  1 
ATOM   83   O  OD1 . ASN A 1 13  ? 1.938   7.758   6.821   1.00  19.01 ? 11  ASN B OD1 1 
ATOM   84   N  ND2 . ASN A 1 13  ? 0.926   9.439   7.898   1.00  14.95 ? 11  ASN B ND2 1 
ATOM   85   N  N   . GLY A 1 14  ? 4.345   5.606   7.628   1.00  15.04 ? 12  GLY B N   1 
ATOM   86   C  CA  . GLY A 1 14  ? 3.817   4.194   7.543   1.00  14.90 ? 12  GLY B CA  1 
ATOM   87   C  C   . GLY A 1 14  ? 4.558   3.243   8.456   1.00  15.64 ? 12  GLY B C   1 
ATOM   88   O  O   . GLY A 1 14  ? 5.451   3.659   9.177   1.00  16.01 ? 12  GLY B O   1 
ATOM   89   N  N   . PRO A 1 15  ? 4.180   1.962   8.462   1.00  12.86 ? 13  PRO B N   1 
ATOM   90   C  CA  . PRO A 1 15  ? 4.667   0.933   9.380   1.00  13.78 ? 13  PRO B CA  1 
ATOM   91   C  C   . PRO A 1 15  ? 6.166   0.920   9.657   1.00  16.16 ? 13  PRO B C   1 
ATOM   92   O  O   . PRO A 1 15  ? 6.585   0.723   10.820  1.00  17.82 ? 13  PRO B O   1 
ATOM   93   C  CB  . PRO A 1 15  ? 4.132   -0.395  8.723   1.00  12.88 ? 13  PRO B CB  1 
ATOM   94   C  CG  . PRO A 1 15  ? 2.836   0.048   8.150   1.00  12.21 ? 13  PRO B CG  1 
ATOM   95   C  CD  . PRO A 1 15  ? 3.099   1.435   7.571   1.00  14.20 ? 13  PRO B CD  1 
ATOM   96   N  N   . ILE A 1 16  ? 6.995   1.103   8.616   1.00  17.81 ? 14  ILE B N   1 
ATOM   97   C  CA  . ILE A 1 16  ? 8.459   1.182   8.794   1.00  22.40 ? 14  ILE B CA  1 
ATOM   98   C  C   . ILE A 1 16  ? 8.928   2.310   9.736   1.00  18.93 ? 14  ILE B C   1 
ATOM   99   O  O   . ILE A 1 16  ? 10.003  2.188   10.372  1.00  19.90 ? 14  ILE B O   1 
ATOM   100  C  CB  . ILE A 1 16  ? 9.130   1.248   7.355   1.00  24.59 ? 14  ILE B CB  1 
ATOM   101  C  CG1 . ILE A 1 16  ? 8.886   -0.120  6.678   1.00  31.17 ? 14  ILE B CG1 1 
ATOM   102  C  CG2 . ILE A 1 16  ? 10.585  1.680   7.384   1.00  33.28 ? 14  ILE B CG2 1 
ATOM   103  C  CD1 . ILE A 1 16  ? 8.793   -0.093  5.159   1.00  43.88 ? 14  ILE B CD1 1 
ATOM   104  N  N   . HIS A 1 17  ? 8.154   3.360   9.845   1.00  17.72 ? 15  HIS B N   1 
ATOM   105  C  CA  . HIS A 1 17  ? 8.513   4.519   10.644  1.00  22.10 ? 15  HIS B CA  1 
ATOM   106  C  C   . HIS A 1 17  ? 7.840   4.520   11.989  1.00  19.20 ? 15  HIS B C   1 
ATOM   107  O  O   . HIS A 1 17  ? 8.111   5.398   12.805  1.00  20.07 ? 15  HIS B O   1 
ATOM   108  C  CB  . HIS A 1 17  ? 8.159   5.786   9.957   1.00  21.80 ? 15  HIS B CB  1 
ATOM   109  C  CG  . HIS A 1 17  ? 8.838   5.973   8.647   1.00  25.33 ? 15  HIS B CG  1 
ATOM   110  N  ND1 . HIS A 1 17  ? 10.197  6.171   8.555   1.00  29.54 ? 15  HIS B ND1 1 
ATOM   111  C  CD2 . HIS A 1 17  ? 8.347   6.014   7.356   1.00  29.12 ? 15  HIS B CD2 1 
ATOM   112  C  CE1 . HIS A 1 17  ? 10.543  6.307   7.242   1.00  31.59 ? 15  HIS B CE1 1 
ATOM   113  N  NE2 . HIS A 1 17  ? 9.432   6.214   6.504   1.00  26.01 ? 15  HIS B NE2 1 
ATOM   114  N  N   . TRP A 1 18  ? 6.951   3.567   12.275  1.00  17.00 ? 16  TRP B N   1 
ATOM   115  C  CA  . TRP A 1 18  ? 6.218   3.676   13.554  1.00  15.99 ? 16  TRP B CA  1 
ATOM   116  C  C   . TRP A 1 18  ? 7.092   3.582   14.777  1.00  16.25 ? 16  TRP B C   1 
ATOM   117  O  O   . TRP A 1 18  ? 6.715   4.128   15.826  1.00  19.43 ? 16  TRP B O   1 
ATOM   118  C  CB  . TRP A 1 18  ? 5.105   2.575   13.650  1.00  15.78 ? 16  TRP B CB  1 
ATOM   119  C  CG  . TRP A 1 18  ? 3.956   2.748   12.637  1.00  13.99 ? 16  TRP B CG  1 
ATOM   120  C  CD1 . TRP A 1 18  ? 3.629   3.858   11.876  1.00  14.22 ? 16  TRP B CD1 1 
ATOM   121  C  CD2 . TRP A 1 18  ? 2.896   1.757   12.371  1.00  12.81 ? 16  TRP B CD2 1 
ATOM   122  N  NE1 . TRP A 1 18  ? 2.479   3.657   11.127  1.00  14.24 ? 16  TRP B NE1 1 
ATOM   123  C  CE2 . TRP A 1 18  ? 2.020   2.351   11.370  1.00  13.49 ? 16  TRP B CE2 1 
ATOM   124  C  CE3 . TRP A 1 18  ? 2.617   0.457   12.864  1.00  11.92 ? 16  TRP B CE3 1 
ATOM   125  C  CZ2 . TRP A 1 18  ? 0.859   1.725   10.936  1.00  12.78 ? 16  TRP B CZ2 1 
ATOM   126  C  CZ3 . TRP A 1 18  ? 1.502   -0.227  12.331  1.00  11.88 ? 16  TRP B CZ3 1 
ATOM   127  C  CH2 . TRP A 1 18  ? 0.614   0.402   11.424  1.00  12.33 ? 16  TRP B CH2 1 
ATOM   128  N  N   . LYS A 1 19  ? 8.146   2.790   14.710  1.00  17.25 ? 17  LYS B N   1 
ATOM   129  C  CA  . LYS A 1 19  ? 9.120   2.676   15.793  1.00  23.32 ? 17  LYS B CA  1 
ATOM   130  C  C   . LYS A 1 19  ? 9.625   4.115   16.191  1.00  27.49 ? 17  LYS B C   1 
ATOM   131  O  O   . LYS A 1 19  ? 9.876   4.396   17.373  1.00  27.84 ? 17  LYS B O   1 
ATOM   132  C  CB  . LYS A 1 19  ? 10.270  1.778   15.384  1.00  25.01 ? 17  LYS B CB  1 
ATOM   133  C  CG  . LYS A 1 19  ? 11.324  2.503   14.525  1.00  27.98 ? 17  LYS B CG  1 
ATOM   134  C  CD  . LYS A 1 19  ? 11.921  1.680   13.405  1.00  34.57 ? 17  LYS B CD  1 
ATOM   135  C  CE  . LYS A 1 19  ? 12.342  0.280   13.787  1.00  41.53 ? 17  LYS B CE  1 
ATOM   136  N  NZ  . LYS A 1 19  ? 13.728  0.076   14.315  1.00  44.99 ? 17  LYS B NZ  1 
ATOM   137  N  N   . GLU A 1 20  ? 9.614   5.055   15.252  1.00  30.62 ? 18  GLU B N   1 
ATOM   138  C  CA  . GLU A 1 20  ? 9.980   6.449   15.590  1.00  33.52 ? 18  GLU B CA  1 
ATOM   139  C  C   . GLU A 1 20  ? 9.082   7.147   16.654  1.00  35.86 ? 18  GLU B C   1 
ATOM   140  O  O   . GLU A 1 20  ? 9.596   7.902   17.503  1.00  45.19 ? 18  GLU B O   1 
ATOM   141  C  CB  . GLU A 1 20  ? 10.217  7.316   14.299  1.00  27.76 ? 18  GLU B CB  1 
ATOM   142  C  CG  . GLU A 1 20  ? 11.259  6.681   13.362  1.00  30.81 ? 18  GLU B CG  1 
ATOM   143  C  CD  . GLU A 1 20  ? 11.062  7.060   11.887  1.00  27.16 ? 18  GLU B CD  1 
ATOM   144  O  OE1 . GLU A 1 20  ? 10.433  8.079   11.578  1.00  31.99 ? 18  GLU B OE1 1 
ATOM   145  O  OE2 . GLU A 1 20  ? 11.507  6.300   10.991  1.00  31.64 ? 18  GLU B OE2 1 
ATOM   146  N  N   . PHE A 1 21  ? 7.769   6.924   16.640  1.00  32.11 ? 19  PHE B N   1 
ATOM   147  C  CA  . PHE A 1 21  ? 6.893   7.441   17.677  1.00  30.32 ? 19  PHE B CA  1 
ATOM   148  C  C   . PHE A 1 21  ? 6.535   6.404   18.799  1.00  30.98 ? 19  PHE B C   1 
ATOM   149  O  O   . PHE A 1 21  ? 6.124   6.792   19.893  1.00  27.78 ? 19  PHE B O   1 
ATOM   150  C  CB  . PHE A 1 21  ? 5.636   8.070   17.066  0.010 30.81 ? 19  PHE B CB  1 
ATOM   151  C  CG  . PHE A 1 21  ? 5.898   9.351   16.323  0.010 30.89 ? 19  PHE B CG  1 
ATOM   152  C  CD1 . PHE A 1 21  ? 5.876   10.568  16.984  0.010 30.87 ? 19  PHE B CD1 1 
ATOM   153  C  CD2 . PHE A 1 21  ? 6.164   9.339   14.963  0.010 31.01 ? 19  PHE B CD2 1 
ATOM   154  C  CE1 . PHE A 1 21  ? 6.117   11.748  16.306  0.010 30.90 ? 19  PHE B CE1 1 
ATOM   155  C  CE2 . PHE A 1 21  ? 6.406   10.515  14.278  0.010 30.95 ? 19  PHE B CE2 1 
ATOM   156  C  CZ  . PHE A 1 21  ? 6.382   11.721  14.950  0.010 30.95 ? 19  PHE B CZ  1 
ATOM   157  N  N   . PHE A 1 22  ? 6.672   5.105   18.512  1.00  26.07 ? 20  PHE B N   1 
ATOM   158  C  CA  . PHE A 1 22  ? 6.218   4.020   19.414  1.00  24.24 ? 20  PHE B CA  1 
ATOM   159  C  C   . PHE A 1 22  ? 7.241   2.879   19.422  1.00  20.96 ? 20  PHE B C   1 
ATOM   160  O  O   . PHE A 1 22  ? 7.183   1.931   18.627  1.00  19.10 ? 20  PHE B O   1 
ATOM   161  C  CB  . PHE A 1 22  ? 4.850   3.479   18.940  1.00  25.08 ? 20  PHE B CB  1 
ATOM   162  C  CG  . PHE A 1 22  ? 3.814   4.526   18.728  1.00  25.43 ? 20  PHE B CG  1 
ATOM   163  C  CD1 . PHE A 1 22  ? 2.993   4.892   19.755  1.00  25.13 ? 20  PHE B CD1 1 
ATOM   164  C  CD2 . PHE A 1 22  ? 3.693   5.180   17.494  1.00  26.33 ? 20  PHE B CD2 1 
ATOM   165  C  CE1 . PHE A 1 22  ? 2.005   5.873   19.596  1.00  26.56 ? 20  PHE B CE1 1 
ATOM   166  C  CE2 . PHE A 1 22  ? 2.731   6.174   17.312  1.00  31.04 ? 20  PHE B CE2 1 
ATOM   167  C  CZ  . PHE A 1 22  ? 1.863   6.519   18.375  1.00  28.79 ? 20  PHE B CZ  1 
ATOM   168  N  N   . PRO A 1 23  ? 8.250   2.941   20.305  1.00  19.14 ? 21  PRO B N   1 
ATOM   169  C  CA  . PRO A 1 23  ? 9.377   1.991   20.243  1.00  17.79 ? 21  PRO B CA  1 
ATOM   170  C  C   . PRO A 1 23  ? 9.037   0.513   20.441  1.00  18.01 ? 21  PRO B C   1 
ATOM   171  O  O   . PRO A 1 23  ? 9.818   -0.371  20.059  1.00  18.04 ? 21  PRO B O   1 
ATOM   172  C  CB  . PRO A 1 23  ? 10.252  2.481   21.401  1.00  18.30 ? 21  PRO B CB  1 
ATOM   173  C  CG  . PRO A 1 23  ? 10.117  3.952   21.268  1.00  20.04 ? 21  PRO B CG  1 
ATOM   174  C  CD  . PRO A 1 23  ? 8.620   4.150   21.113  1.00  19.52 ? 21  PRO B CD  1 
ATOM   175  N  N   . ILE A 1 24  ? 7.888   0.236   21.081  1.00  16.45 ? 22  ILE B N   1 
ATOM   176  C  CA  . ILE A 1 24  ? 7.473   -1.164  21.278  1.00  16.84 ? 22  ILE B CA  1 
ATOM   177  C  C   . ILE A 1 24  ? 7.169   -1.852  19.894  1.00  14.34 ? 22  ILE B C   1 
ATOM   178  O  O   . ILE A 1 24  ? 7.076   -3.084  19.819  1.00  16.06 ? 22  ILE B O   1 
ATOM   179  C  CB  . ILE A 1 24  ? 6.172   -1.267  22.181  1.00  14.82 ? 22  ILE B CB  1 
ATOM   180  C  CG1 . ILE A 1 24  ? 6.008   -2.662  22.772  1.00  17.23 ? 22  ILE B CG1 1 
ATOM   181  C  CG2 . ILE A 1 24  ? 4.950   -0.750  21.430  1.00  13.90 ? 22  ILE B CG2 1 
ATOM   182  C  CD1 . ILE A 1 24  ? 7.182   -3.155  23.648  1.00  19.96 ? 22  ILE B CD1 1 
ATOM   183  N  N   . ALA A 1 25  ? 7.176   -1.054  18.822  1.00  15.95 ? 23  ALA B N   1 
ATOM   184  C  CA  . ALA A 1 25  ? 7.026   -1.584  17.455  1.00  15.53 ? 23  ALA B CA  1 
ATOM   185  C  C   . ALA A 1 25  ? 8.072   -2.639  17.210  1.00  15.47 ? 23  ALA B C   1 
ATOM   186  O  O   . ALA A 1 25  ? 7.875   -3.564  16.368  1.00  14.75 ? 23  ALA B O   1 
ATOM   187  C  CB  . ALA A 1 25  ? 7.146   -0.498  16.443  1.00  15.25 ? 23  ALA B CB  1 
ATOM   188  N  N   . ASP A 1 26  ? 9.235   -2.510  17.914  1.00  17.10 ? 24  ASP B N   1 
ATOM   189  C  CA  . ASP A 1 26  ? 10.294  -3.508  17.858  1.00  19.64 ? 24  ASP B CA  1 
ATOM   190  C  C   . ASP A 1 26  ? 10.340  -4.517  19.022  1.00  19.49 ? 24  ASP B C   1 
ATOM   191  O  O   . ASP A 1 26  ? 11.385  -5.195  19.249  1.00  18.68 ? 24  ASP B O   1 
ATOM   192  C  CB  . ASP A 1 26  ? 11.657  -2.783  17.747  1.00  25.34 ? 24  ASP B CB  1 
ATOM   193  C  CG  . ASP A 1 26  ? 11.800  -2.015  16.421  1.00  26.95 ? 24  ASP B CG  1 
ATOM   194  O  OD1 . ASP A 1 26  ? 11.496  -2.553  15.324  1.00  24.35 ? 24  ASP B OD1 1 
ATOM   195  O  OD2 . ASP A 1 26  ? 12.235  -0.869  16.471  1.00  31.76 ? 24  ASP B OD2 1 
ATOM   196  N  N   . GLY A 1 27  ? 9.213   -4.591  19.752  1.00  20.44 ? 25  GLY B N   1 
ATOM   197  C  CA  . GLY A 1 27  ? 9.035   -5.558  20.831  1.00  17.85 ? 25  GLY B CA  1 
ATOM   198  C  C   . GLY A 1 27  ? 9.068   -7.029  20.503  1.00  18.98 ? 25  GLY B C   1 
ATOM   199  O  O   . GLY A 1 27  ? 9.162   -7.420  19.312  1.00  20.64 ? 25  GLY B O   1 
ATOM   200  N  N   . ASP A 1 28  ? 8.954   -7.879  21.542  1.00  17.88 ? 26  ASP B N   1 
ATOM   201  C  CA  . ASP A 1 28  ? 9.125   -9.303  21.414  1.00  16.90 ? 26  ASP B CA  1 
ATOM   202  C  C   . ASP A 1 28  ? 7.752   -9.993  21.187  1.00  15.19 ? 26  ASP B C   1 
ATOM   203  O  O   . ASP A 1 28  ? 7.748   -11.180 20.899  1.00  18.12 ? 26  ASP B O   1 
ATOM   204  C  CB  . ASP A 1 28  ? 9.723   -9.848  22.731  1.00  21.70 ? 26  ASP B CB  1 
ATOM   205  C  CG  . ASP A 1 28  ? 11.281  -9.592  22.823  1.00  26.47 ? 26  ASP B CG  1 
ATOM   206  O  OD1 . ASP A 1 28  ? 11.865  -9.185  21.792  1.00  29.82 ? 26  ASP B OD1 1 
ATOM   207  O  OD2 . ASP A 1 28  ? 11.824  -9.811  23.901  1.00  33.28 ? 26  ASP B OD2 1 
ATOM   208  N  N   . GLN A 1 29  ? 6.643   -9.243  21.277  1.00  13.59 ? 27  GLN B N   1 
ATOM   209  C  CA  . GLN A 1 29  ? 5.290   -9.891  21.061  1.00  14.04 ? 27  GLN B CA  1 
ATOM   210  C  C   . GLN A 1 29  ? 4.423   -9.091  20.094  1.00  12.34 ? 27  GLN B C   1 
ATOM   211  O  O   . GLN A 1 29  ? 3.273   -8.676  20.416  1.00  11.74 ? 27  GLN B O   1 
ATOM   212  C  CB  . GLN A 1 29  ? 4.563   -10.168 22.398  1.00  15.92 ? 27  GLN B CB  1 
ATOM   213  C  CG  . GLN A 1 29  ? 5.451   -11.049 23.331  1.00  17.85 ? 27  GLN B CG  1 
ATOM   214  C  CD  . GLN A 1 29  ? 4.626   -12.001 24.244  1.00  20.93 ? 27  GLN B CD  1 
ATOM   215  O  OE1 . GLN A 1 29  ? 3.517   -11.646 24.634  1.00  24.58 ? 27  GLN B OE1 1 
ATOM   216  N  NE2 . GLN A 1 29  ? 5.212   -13.184 24.609  1.00  20.04 ? 27  GLN B NE2 1 
ATOM   217  N  N   . GLN A 1 30  ? 5.034   -8.728  18.958  1.00  12.37 ? 28  GLN B N   1 
ATOM   218  C  CA  . GLN A 1 30  ? 4.361   -7.924  17.957  1.00  11.05 ? 28  GLN B CA  1 
ATOM   219  C  C   . GLN A 1 30  ? 3.572   -8.746  16.935  1.00  9.52  ? 28  GLN B C   1 
ATOM   220  O  O   . GLN A 1 30  ? 3.898   -9.836  16.660  1.00  10.77 ? 28  GLN B O   1 
ATOM   221  C  CB  . GLN A 1 30  ? 5.402   -7.038  17.226  1.00  10.62 ? 28  GLN B CB  1 
ATOM   222  C  CG  . GLN A 1 30  ? 5.938   -5.919  18.206  1.00  11.12 ? 28  GLN B CG  1 
ATOM   223  C  CD  . GLN A 1 30  ? 4.844   -4.920  18.492  1.00  10.40 ? 28  GLN B CD  1 
ATOM   224  O  OE1 . GLN A 1 30  ? 4.347   -4.143  17.603  1.00  11.51 ? 28  GLN B OE1 1 
ATOM   225  N  NE2 . GLN A 1 30  ? 4.443   -4.841  19.819  1.00  10.05 ? 28  GLN B NE2 1 
ATOM   226  N  N   . SER A 1 31  ? 2.516   -8.086  16.431  1.00  9.87  ? 29  SER B N   1 
ATOM   227  C  CA  . SER A 1 31  ? 1.582   -8.619  15.446  1.00  9.50  ? 29  SER B CA  1 
ATOM   228  C  C   . SER A 1 31  ? 1.448   -7.732  14.255  1.00  9.53  ? 29  SER B C   1 
ATOM   229  O  O   . SER A 1 31  ? 1.670   -6.540  14.338  1.00  9.97  ? 29  SER B O   1 
ATOM   230  C  CB  . SER A 1 31  ? 0.186   -8.795  16.074  1.00  8.66  ? 29  SER B CB  1 
ATOM   231  O  OG  . SER A 1 31  ? 0.277   -9.801  17.136  1.00  9.51  ? 29  SER B OG  1 
ATOM   232  N  N   . PRO A 1 32  ? 1.062   -8.312  13.082  1.00  9.99  ? 30  PRO B N   1 
ATOM   233  C  CA  . PRO A 1 32  ? 0.735   -9.676  12.770  1.00  9.60  ? 30  PRO B CA  1 
ATOM   234  C  C   . PRO A 1 32  ? 2.025   -10.509 12.520  1.00  9.72  ? 30  PRO B C   1 
ATOM   235  O  O   . PRO A 1 32  ? 3.190   -10.023 12.733  1.00  9.82  ? 30  PRO B O   1 
ATOM   236  C  CB  . PRO A 1 32  ? -0.095  -9.521  11.472  1.00  8.83  ? 30  PRO B CB  1 
ATOM   237  C  CG  . PRO A 1 32  ? 0.696   -8.377  10.754  1.00  9.36  ? 30  PRO B CG  1 
ATOM   238  C  CD  . PRO A 1 32  ? 1.014   -7.406  11.874  1.00  10.40 ? 30  PRO B CD  1 
ATOM   239  N  N   . ILE A 1 33  ? 1.793   -11.756 12.170  1.00  10.43 ? 31  ILE B N   1 
ATOM   240  C  CA  . ILE A 1 33  ? 2.880   -12.745 11.951  1.00  10.11 ? 31  ILE B CA  1 
ATOM   241  C  C   . ILE A 1 33  ? 2.567   -13.618 10.739  1.00  10.18 ? 31  ILE B C   1 
ATOM   242  O  O   . ILE A 1 33  ? 1.442   -13.717 10.268  1.00  10.67 ? 31  ILE B O   1 
ATOM   243  C  CB  . ILE A 1 33  ? 3.099   -13.712 13.187  1.00  10.57 ? 31  ILE B CB  1 
ATOM   244  C  CG1 . ILE A 1 33  ? 1.862   -14.599 13.360  1.00  9.51  ? 31  ILE B CG1 1 
ATOM   245  C  CG2 . ILE A 1 33  ? 3.482   -12.912 14.476  1.00  11.89 ? 31  ILE B CG2 1 
ATOM   246  C  CD1 . ILE A 1 33  ? 2.107   -15.688 14.406  1.00  11.39 ? 31  ILE B CD1 1 
ATOM   247  N  N   . GLU A 1 34  ? 3.623   -14.288 10.285  1.00  11.61 ? 32  GLU B N   1 
ATOM   248  C  CA  . GLU A 1 34  ? 3.553   -15.323 9.303   1.00  11.45 ? 32  GLU B CA  1 
ATOM   249  C  C   . GLU A 1 34  ? 3.145   -16.611 10.126  1.00  12.08 ? 32  GLU B C   1 
ATOM   250  O  O   . GLU A 1 34  ? 3.841   -16.993 11.152  1.00  12.37 ? 32  GLU B O   1 
ATOM   251  C  CB  . GLU A 1 34  ? 4.954   -15.567 8.675   1.00  14.15 ? 32  GLU B CB  1 
ATOM   252  C  CG  . GLU A 1 34  ? 5.014   -14.820 7.321   1.00  19.78 ? 32  GLU B CG  1 
ATOM   253  C  CD  . GLU A 1 34  ? 4.405   -15.493 6.089   1.00  15.38 ? 32  GLU B CD  1 
ATOM   254  O  OE1 . GLU A 1 34  ? 3.854   -16.608 6.139   1.00  16.89 ? 32  GLU B OE1 1 
ATOM   255  O  OE2 . GLU A 1 34  ? 4.471   -14.860 5.025   1.00  23.04 ? 32  GLU B OE2 1 
ATOM   256  N  N   . ILE A 1 35  ? 2.078   -17.260 9.661   1.00  11.12 ? 33  ILE B N   1 
ATOM   257  C  CA  . ILE A 1 35  ? 1.681   -18.533 10.246  1.00  11.99 ? 33  ILE B CA  1 
ATOM   258  C  C   . ILE A 1 35  ? 2.217   -19.668 9.346   1.00  11.99 ? 33  ILE B C   1 
ATOM   259  O  O   . ILE A 1 35  ? 1.765   -19.822 8.236   1.00  11.47 ? 33  ILE B O   1 
ATOM   260  C  CB  . ILE A 1 35  ? 0.158   -18.601 10.394  1.00  12.77 ? 33  ILE B CB  1 
ATOM   261  C  CG1 . ILE A 1 35  ? -0.281  -17.511 11.392  1.00  12.86 ? 33  ILE B CG1 1 
ATOM   262  C  CG2 . ILE A 1 35  ? -0.204  -20.005 10.958  1.00  13.73 ? 33  ILE B CG2 1 
ATOM   263  C  CD1 . ILE A 1 35  ? -1.815  -17.350 11.475  1.00  14.43 ? 33  ILE B CD1 1 
ATOM   264  N  N   . LYS A 1 36  ? 3.193   -20.422 9.867   1.00  14.22 ? 34  LYS B N   1 
ATOM   265  C  CA  . LYS A 1 36  ? 3.869   -21.524 9.106   1.00  14.32 ? 34  LYS B CA  1 
ATOM   266  C  C   . LYS A 1 36  ? 3.267   -22.820 9.716   1.00  14.71 ? 34  LYS B C   1 
ATOM   267  O  O   . LYS A 1 36  ? 3.581   -23.176 10.877  1.00  16.53 ? 34  LYS B O   1 
ATOM   268  C  CB  . LYS A 1 36  ? 5.390   -21.505 9.344   1.00  13.27 ? 34  LYS B CB  1 
ATOM   269  C  CG  . LYS A 1 36  ? 6.113   -20.268 8.786   1.00  13.72 ? 34  LYS B CG  1 
ATOM   270  C  CD  . LYS A 1 36  ? 7.573   -20.415 9.117   1.00  16.74 ? 34  LYS B CD  1 
ATOM   271  C  CE  . LYS A 1 36  ? 8.470   -19.315 8.601   1.00  18.79 ? 34  LYS B CE  1 
ATOM   272  N  NZ  . LYS A 1 36  ? 9.933   -19.463 8.962   1.00  18.86 ? 34  LYS B NZ  1 
ATOM   273  N  N   . THR A 1 37  ? 2.387   -23.415 8.959   1.00  15.74 ? 35  THR B N   1 
ATOM   274  C  CA  . THR A 1 37  ? 1.522   -24.493 9.447   1.00  18.97 ? 35  THR B CA  1 
ATOM   275  C  C   . THR A 1 37  ? 2.320   -25.747 9.906   1.00  20.12 ? 35  THR B C   1 
ATOM   276  O  O   . THR A 1 37  ? 1.881   -26.444 10.831  1.00  23.03 ? 35  THR B O   1 
ATOM   277  C  CB  . THR A 1 37  ? 0.426   -24.867 8.455   1.00  19.99 ? 35  THR B CB  1 
ATOM   278  O  OG1 . THR A 1 37  ? 0.953   -25.329 7.183   1.00  21.24 ? 35  THR B OG1 1 
ATOM   279  C  CG2 . THR A 1 37  ? -0.584  -23.759 8.263   1.00  17.72 ? 35  THR B CG2 1 
ATOM   280  N  N   . LYS A 1 38  ? 3.518   -25.984 9.341   1.00  18.75 ? 36  LYS B N   1 
ATOM   281  C  CA  . LYS A 1 38  ? 4.327   -27.090 9.854   1.00  20.91 ? 36  LYS B CA  1 
ATOM   282  C  C   . LYS A 1 38  ? 5.017   -26.826 11.160  1.00  21.34 ? 36  LYS B C   1 
ATOM   283  O  O   . LYS A 1 38  ? 5.578   -27.795 11.739  1.00  23.69 ? 36  LYS B O   1 
ATOM   284  C  CB  . LYS A 1 38  ? 5.404   -27.533 8.863   1.00  22.65 ? 36  LYS B CB  1 
ATOM   285  C  CG  . LYS A 1 38  ? 4.786   -28.070 7.610   1.00  27.26 ? 36  LYS B CG  1 
ATOM   286  C  CD  . LYS A 1 38  ? 5.323   -29.451 7.360   1.00  39.31 ? 36  LYS B CD  1 
ATOM   287  C  CE  . LYS A 1 38  ? 4.212   -30.480 7.321   1.00  43.46 ? 36  LYS B CE  1 
ATOM   288  N  NZ  . LYS A 1 38  ? 4.869   -31.758 7.718   1.00  48.97 ? 36  LYS B NZ  1 
ATOM   289  N  N   . GLU A 1 39  ? 5.043   -25.557 11.590  1.00  18.35 ? 37  GLU B N   1 
ATOM   290  C  CA  . GLU A 1 39  ? 5.603   -25.164 12.863  1.00  18.94 ? 37  GLU B CA  1 
ATOM   291  C  C   . GLU A 1 39  ? 4.560   -24.993 13.986  1.00  18.30 ? 37  GLU B C   1 
ATOM   292  O  O   . GLU A 1 39  ? 4.952   -24.759 15.123  1.00  18.78 ? 37  GLU B O   1 
ATOM   293  C  CB  . GLU A 1 39  ? 6.356   -23.837 12.779  1.00  20.12 ? 37  GLU B CB  1 
ATOM   294  C  CG  . GLU A 1 39  ? 7.359   -23.757 11.613  1.00  22.93 ? 37  GLU B CG  1 
ATOM   295  C  CD  . GLU A 1 39  ? 8.260   -24.919 11.618  1.00  26.80 ? 37  GLU B CD  1 
ATOM   296  O  OE1 . GLU A 1 39  ? 8.843   -25.195 12.731  1.00  29.37 ? 37  GLU B OE1 1 
ATOM   297  O  OE2 . GLU A 1 39  ? 8.353   -25.535 10.517  1.00  28.91 ? 37  GLU B OE2 1 
ATOM   298  N  N   . VAL A 1 40  ? 3.264   -25.035 13.626  1.00  16.57 ? 38  VAL B N   1 
ATOM   299  C  CA  . VAL A 1 40  ? 2.237   -24.809 14.614  1.00  17.40 ? 38  VAL B CA  1 
ATOM   300  C  C   . VAL A 1 40  ? 2.094   -26.068 15.443  1.00  18.40 ? 38  VAL B C   1 
ATOM   301  O  O   . VAL A 1 40  ? 2.254   -27.163 14.913  1.00  23.23 ? 38  VAL B O   1 
ATOM   302  C  CB  . VAL A 1 40  ? 0.922   -24.484 13.899  1.00  19.73 ? 38  VAL B CB  1 
ATOM   303  C  CG1 . VAL A 1 40  ? -0.206  -24.381 14.891  1.00  22.39 ? 38  VAL B CG1 1 
ATOM   304  C  CG2 . VAL A 1 40  ? 1.067   -23.112 13.222  1.00  18.64 ? 38  VAL B CG2 1 
ATOM   305  N  N   . LYS A 1 41  ? 1.899   -25.907 16.736  1.00  17.55 ? 39  LYS B N   1 
ATOM   306  C  CA  . LYS A 1 41  ? 1.650   -27.059 17.637  1.00  20.94 ? 39  LYS B CA  1 
ATOM   307  C  C   . LYS A 1 41  ? 0.146   -27.255 17.868  1.00  20.08 ? 39  LYS B C   1 
ATOM   308  O  O   . LYS A 1 41  ? -0.509  -26.380 18.481  1.00  18.03 ? 39  LYS B O   1 
ATOM   309  C  CB  . LYS A 1 41  ? 2.319   -26.784 19.003  1.00  23.89 ? 39  LYS B CB  1 
ATOM   310  C  CG  . LYS A 1 41  ? 3.845   -27.014 19.044  1.00  33.75 ? 39  LYS B CG  1 
ATOM   311  C  CD  . LYS A 1 41  ? 4.710   -26.183 18.119  1.00  41.85 ? 39  LYS B CD  1 
ATOM   312  C  CE  . LYS A 1 41  ? 6.085   -26.823 17.854  1.00  44.08 ? 39  LYS B CE  1 
ATOM   313  N  NZ  . LYS A 1 41  ? 6.709   -26.370 16.546  1.00  42.88 ? 39  LYS B NZ  1 
ATOM   314  N  N   . TYR A 1 42  ? -0.376  -28.435 17.495  1.00  17.14 ? 40  TYR B N   1 
ATOM   315  C  CA  . TYR A 1 42  ? -1.730  -28.801 17.878  1.00  18.46 ? 40  TYR B CA  1 
ATOM   316  C  C   . TYR A 1 42  ? -1.780  -28.856 19.416  1.00  17.91 ? 40  TYR B C   1 
ATOM   317  O  O   . TYR A 1 42  ? -0.866  -29.428 20.044  1.00  18.86 ? 40  TYR B O   1 
ATOM   318  C  CB  . TYR A 1 42  ? -2.131  -30.165 17.292  1.00  18.69 ? 40  TYR B CB  1 
ATOM   319  C  CG  . TYR A 1 42  ? -3.433  -30.666 17.902  1.00  19.29 ? 40  TYR B CG  1 
ATOM   320  C  CD1 . TYR A 1 42  ? -4.653  -29.988 17.691  1.00  17.32 ? 40  TYR B CD1 1 
ATOM   321  C  CD2 . TYR A 1 42  ? -3.462  -31.827 18.721  1.00  19.35 ? 40  TYR B CD2 1 
ATOM   322  C  CE1 . TYR A 1 42  ? -5.864  -30.428 18.291  1.00  19.53 ? 40  TYR B CE1 1 
ATOM   323  C  CE2 . TYR A 1 42  ? -4.640  -32.288 19.290  1.00  21.76 ? 40  TYR B CE2 1 
ATOM   324  C  CZ  . TYR A 1 42  ? -5.832  -31.616 19.094  1.00  23.32 ? 40  TYR B CZ  1 
ATOM   325  O  OH  . TYR A 1 42  ? -6.966  -32.102 19.707  1.00  25.21 ? 40  TYR B OH  1 
ATOM   326  N  N   . ASP A 1 43  ? -2.746  -28.205 20.059  1.00  16.11 ? 41  ASP B N   1 
ATOM   327  C  CA  . ASP A 1 43  ? -2.860  -28.241 21.494  1.00  15.46 ? 41  ASP B CA  1 
ATOM   328  C  C   . ASP A 1 43  ? -4.264  -28.759 21.882  1.00  17.53 ? 41  ASP B C   1 
ATOM   329  O  O   . ASP A 1 43  ? -5.286  -28.051 21.691  1.00  16.47 ? 41  ASP B O   1 
ATOM   330  C  CB  . ASP A 1 43  ? -2.598  -26.840 22.111  1.00  16.57 ? 41  ASP B CB  1 
ATOM   331  C  CG  . ASP A 1 43  ? -2.542  -26.862 23.653  1.00  17.08 ? 41  ASP B CG  1 
ATOM   332  O  OD1 . ASP A 1 43  ? -3.069  -27.841 24.292  1.00  16.40 ? 41  ASP B OD1 1 
ATOM   333  O  OD2 . ASP A 1 43  ? -2.026  -25.888 24.214  1.00  19.34 ? 41  ASP B OD2 1 
ATOM   334  N  N   . SER A 1 44  ? -4.347  -30.009 22.404  1.00  15.94 ? 42  SER B N   1 
ATOM   335  C  CA  . SER A 1 44  ? -5.668  -30.538 22.782  1.00  18.85 ? 42  SER B CA  1 
ATOM   336  C  C   . SER A 1 44  ? -6.347  -29.817 23.973  1.00  19.11 ? 42  SER B C   1 
ATOM   337  O  O   . SER A 1 44  ? -7.509  -30.057 24.241  1.00  17.71 ? 42  SER B O   1 
ATOM   338  C  CB  . SER A 1 44  ? -5.645  -32.102 22.953  1.00  19.65 ? 42  SER B CB  1 
ATOM   339  O  OG  . SER A 1 44  ? -4.786  -32.352 24.033  1.00  21.34 ? 42  SER B OG  1 
ATOM   340  N  N   . SER A 1 45  ? -5.650  -28.951 24.705  1.00  17.89 ? 43  SER B N   1 
ATOM   341  C  CA  . SER A 1 45  ? -6.301  -28.248 25.822  1.00  17.04 ? 43  SER B CA  1 
ATOM   342  C  C   . SER A 1 45  ? -7.072  -26.995 25.316  1.00  16.56 ? 43  SER B C   1 
ATOM   343  O  O   . SER A 1 45  ? -7.833  -26.381 26.083  1.00  17.80 ? 43  SER B O   1 
ATOM   344  C  CB  . SER A 1 45  ? -5.315  -27.881 26.905  1.00  20.54 ? 43  SER B CB  1 
ATOM   345  O  OG  . SER A 1 45  ? -4.353  -26.883 26.447  1.00  21.84 ? 43  SER B OG  1 
ATOM   346  N  N   . LEU A 1 46  ? -6.849  -26.622 24.055  1.00  14.24 ? 44  LEU B N   1 
ATOM   347  C  CA  . LEU A 1 46  ? -7.577  -25.451 23.494  1.00  13.06 ? 44  LEU B CA  1 
ATOM   348  C  C   . LEU A 1 46  ? -9.049  -25.848 23.356  1.00  14.21 ? 44  LEU B C   1 
ATOM   349  O  O   . LEU A 1 46  ? -9.346  -26.985 22.948  1.00  18.51 ? 44  LEU B O   1 
ATOM   350  C  CB  . LEU A 1 46  ? -7.027  -25.184 22.111  1.00  13.22 ? 44  LEU B CB  1 
ATOM   351  C  CG  . LEU A 1 46  ? -5.747  -24.352 22.154  1.00  11.00 ? 44  LEU B CG  1 
ATOM   352  C  CD1 . LEU A 1 46  ? -5.175  -24.244 20.715  1.00  10.94 ? 44  LEU B CD1 1 
ATOM   353  C  CD2 . LEU A 1 46  ? -5.782  -22.990 22.937  1.00  12.84 ? 44  LEU B CD2 1 
ATOM   354  N  N   . ARG A 1 47  ? -9.949  -24.913 23.602  1.00  13.53 ? 45  ARG B N   1 
ATOM   355  C  CA  . ARG A 1 47  ? -11.370 -25.202 23.500  1.00  13.11 ? 45  ARG B CA  1 
ATOM   356  C  C   . ARG A 1 47  ? -11.978 -24.638 22.212  1.00  13.65 ? 45  ARG B C   1 
ATOM   357  O  O   . ARG A 1 47  ? -11.385 -23.776 21.631  1.00  14.85 ? 45  ARG B O   1 
ATOM   358  C  CB  . ARG A 1 47  ? -12.115 -24.582 24.667  1.00  14.39 ? 45  ARG B CB  1 
ATOM   359  C  CG  . ARG A 1 47  ? -11.784 -25.341 25.942  1.00  15.49 ? 45  ARG B CG  1 
ATOM   360  C  CD  . ARG A 1 47  ? -12.390 -24.648 27.091  1.00  17.49 ? 45  ARG B CD  1 
ATOM   361  N  NE  . ARG A 1 47  ? -12.141 -25.422 28.292  1.00  19.96 ? 45  ARG B NE  1 
ATOM   362  C  CZ  . ARG A 1 47  ? -12.446 -24.988 29.522  1.00  20.52 ? 45  ARG B CZ  1 
ATOM   363  N  NH1 . ARG A 1 47  ? -13.044 -23.795 29.692  1.00  24.41 ? 45  ARG B NH1 1 
ATOM   364  N  NH2 . ARG A 1 47  ? -12.143 -25.751 30.567  1.00  23.99 ? 45  ARG B NH2 1 
ATOM   365  N  N   . PRO A 1 48  ? -13.130 -25.192 21.749  1.00  12.53 ? 46  PRO B N   1 
ATOM   366  C  CA  . PRO A 1 48  ? -13.838 -24.505 20.631  1.00  11.46 ? 46  PRO B CA  1 
ATOM   367  C  C   . PRO A 1 48  ? -14.256 -23.092 21.049  1.00  11.15 ? 46  PRO B C   1 
ATOM   368  O  O   . PRO A 1 48  ? -14.411 -22.808 22.238  1.00  10.25 ? 46  PRO B O   1 
ATOM   369  C  CB  . PRO A 1 48  ? -15.127 -25.347 20.448  1.00  11.77 ? 46  PRO B CB  1 
ATOM   370  C  CG  . PRO A 1 48  ? -14.738 -26.757 20.964  1.00  11.52 ? 46  PRO B CG  1 
ATOM   371  C  CD  . PRO A 1 48  ? -13.898 -26.375 22.188  1.00  12.36 ? 46  PRO B CD  1 
ATOM   372  N  N   . LEU A 1 49  ? -14.396 -22.249 20.053  1.00  10.93 ? 47  LEU B N   1 
ATOM   373  C  CA  . LEU A 1 49  ? -14.860 -20.870 20.391  1.00  11.42 ? 47  LEU B CA  1 
ATOM   374  C  C   . LEU A 1 49  ? -16.364 -20.935 20.826  1.00  11.74 ? 47  LEU B C   1 
ATOM   375  O  O   . LEU A 1 49  ? -17.177 -21.607 20.172  1.00  11.66 ? 47  LEU B O   1 
ATOM   376  C  CB  . LEU A 1 49  ? -14.765 -20.039 19.140  1.00  10.87 ? 47  LEU B CB  1 
ATOM   377  C  CG  . LEU A 1 49  ? -13.273 -19.879 18.684  1.00  11.28 ? 47  LEU B CG  1 
ATOM   378  C  CD1 . LEU A 1 49  ? -13.275 -18.950 17.463  1.00  12.11 ? 47  LEU B CD1 1 
ATOM   379  C  CD2 . LEU A 1 49  ? -12.405 -19.329 19.845  1.00  10.95 ? 47  LEU B CD2 1 
ATOM   380  N  N   . SER A 1 50  ? -16.695 -20.211 21.895  1.00  10.37 ? 48  SER B N   1 
ATOM   381  C  CA  . SER A 1 50  ? -18.062 -19.977 22.370  1.00  10.73 ? 48  SER B CA  1 
ATOM   382  C  C   . SER A 1 50  ? -18.438 -18.489 22.050  1.00  11.24 ? 48  SER B C   1 
ATOM   383  O  O   . SER A 1 50  ? -17.920 -17.541 22.684  1.00  10.47 ? 48  SER B O   1 
ATOM   384  C  CB  . SER A 1 50  ? -18.122 -20.233 23.900  1.00  13.37 ? 48  SER B CB  1 
ATOM   385  O  OG  . SER A 1 50  ? -19.289 -19.649 24.458  1.00  16.39 ? 48  SER B OG  1 
ATOM   386  N  N   . ILE A 1 51  ? -19.330 -18.319 21.064  1.00  9.45  ? 49  ILE B N   1 
ATOM   387  C  CA  . ILE A 1 51  ? -19.481 -16.967 20.510  1.00  10.00 ? 49  ILE B CA  1 
ATOM   388  C  C   . ILE A 1 51  ? -20.928 -16.496 20.655  1.00  10.62 ? 49  ILE B C   1 
ATOM   389  O  O   . ILE A 1 51  ? -21.811 -17.239 20.239  1.00  11.46 ? 49  ILE B O   1 
ATOM   390  C  CB  . ILE A 1 51  ? -19.110 -16.971 19.022  1.00  10.53 ? 49  ILE B CB  1 
ATOM   391  C  CG1 . ILE A 1 51  ? -17.710 -17.625 18.827  1.00  10.42 ? 49  ILE B CG1 1 
ATOM   392  C  CG2 . ILE A 1 51  ? -19.116 -15.514 18.571  1.00  11.24 ? 49  ILE B CG2 1 
ATOM   393  C  CD1 . ILE A 1 51  ? -17.271 -17.535 17.343  1.00  12.33 ? 49  ILE B CD1 1 
ATOM   394  N  N   . LYS A 1 52  ? -21.167 -15.311 21.262  1.00  10.19 ? 50  LYS B N   1 
ATOM   395  C  CA  . LYS A 1 52  ? -22.538 -14.757 21.353  1.00  10.48 ? 50  LYS B CA  1 
ATOM   396  C  C   . LYS A 1 52  ? -22.456 -13.309 20.969  1.00  11.13 ? 50  LYS B C   1 
ATOM   397  O  O   . LYS A 1 52  ? -21.804 -12.545 21.674  1.00  10.45 ? 50  LYS B O   1 
ATOM   398  C  CB  . LYS A 1 52  ? -23.028 -14.850 22.769  1.00  11.72 ? 50  LYS B CB  1 
ATOM   399  C  CG  . LYS A 1 52  ? -24.452 -14.334 22.958  1.00  12.81 ? 50  LYS B CG  1 
ATOM   400  C  CD  . LYS A 1 52  ? -24.758 -14.285 24.453  1.00  13.07 ? 50  LYS B CD  1 
ATOM   401  C  CE  . LYS A 1 52  ? -26.220 -13.733 24.547  1.00  13.01 ? 50  LYS B CE  1 
ATOM   402  N  NZ  . LYS A 1 52  ? -26.668 -12.448 23.826  1.00  13.43 ? 50  LYS B NZ  1 
ATOM   403  N  N   . TYR A 1 53  ? -23.087 -12.973 19.855  1.00  9.91  ? 51  TYR B N   1 
ATOM   404  C  CA  . TYR A 1 53  ? -23.088 -11.586 19.332  1.00  10.64 ? 51  TYR B CA  1 
ATOM   405  C  C   . TYR A 1 53  ? -24.553 -11.195 19.063  1.00  9.84  ? 51  TYR B C   1 
ATOM   406  O  O   . TYR A 1 53  ? -25.237 -11.794 18.204  1.00  11.98 ? 51  TYR B O   1 
ATOM   407  C  CB  . TYR A 1 53  ? -22.219 -11.482 18.027  1.00  9.49  ? 51  TYR B CB  1 
ATOM   408  C  CG  . TYR A 1 53  ? -20.726 -11.734 18.156  1.00  9.18  ? 51  TYR B CG  1 
ATOM   409  C  CD1 . TYR A 1 53  ? -20.012 -11.364 19.284  1.00  9.76  ? 51  TYR B CD1 1 
ATOM   410  C  CD2 . TYR A 1 53  ? -20.057 -12.330 17.074  1.00  9.94  ? 51  TYR B CD2 1 
ATOM   411  C  CE1 . TYR A 1 53  ? -18.655 -11.582 19.352  1.00  9.24  ? 51  TYR B CE1 1 
ATOM   412  C  CE2 . TYR A 1 53  ? -18.684 -12.526 17.105  1.00  9.81  ? 51  TYR B CE2 1 
ATOM   413  C  CZ  . TYR A 1 53  ? -17.990 -12.140 18.227  1.00  8.88  ? 51  TYR B CZ  1 
ATOM   414  O  OH  . TYR A 1 53  ? -16.633 -12.350 18.274  1.00  8.70  ? 51  TYR B OH  1 
ATOM   415  N  N   . ASP A 1 54  ? -25.008 -10.167 19.802  1.00  11.55 ? 52  ASP B N   1 
ATOM   416  C  CA  . ASP A 1 54  ? -26.368 -9.601  19.684  1.00  13.27 ? 52  ASP B CA  1 
ATOM   417  C  C   . ASP A 1 54  ? -26.379 -8.563  18.539  1.00  13.21 ? 52  ASP B C   1 
ATOM   418  O  O   . ASP A 1 54  ? -25.624 -7.604  18.559  1.00  13.91 ? 52  ASP B O   1 
ATOM   419  C  CB  . ASP A 1 54  ? -26.740 -8.959  21.048  1.00  14.27 ? 52  ASP B CB  1 
ATOM   420  C  CG  . ASP A 1 54  ? -28.213 -8.476  21.146  1.00  19.09 ? 52  ASP B CG  1 
ATOM   421  O  OD1 . ASP A 1 54  ? -28.825 -8.021  20.139  1.00  16.14 ? 52  ASP B OD1 1 
ATOM   422  O  OD2 . ASP A 1 54  ? -28.722 -8.498  22.292  1.00  20.69 ? 52  ASP B OD2 1 
ATOM   423  N  N   . PRO A 1 55  ? -27.123 -8.818  17.456  1.00  15.24 ? 53  PRO B N   1 
ATOM   424  C  CA  . PRO A 1 55  ? -27.140 -7.842  16.283  1.00  13.85 ? 53  PRO B CA  1 
ATOM   425  C  C   . PRO A 1 55  ? -27.501 -6.367  16.691  1.00  14.39 ? 53  PRO B C   1 
ATOM   426  O  O   . PRO A 1 55  ? -27.171 -5.412  15.939  1.00  16.58 ? 53  PRO B O   1 
ATOM   427  C  CB  . PRO A 1 55  ? -28.270 -8.414  15.379  1.00  15.01 ? 53  PRO B CB  1 
ATOM   428  C  CG  . PRO A 1 55  ? -28.226 -9.930  15.758  1.00  17.70 ? 53  PRO B CG  1 
ATOM   429  C  CD  . PRO A 1 55  ? -27.999 -9.981  17.261  1.00  14.61 ? 53  PRO B CD  1 
ATOM   430  N  N   . SER A 1 56  ? -28.168 -6.214  17.831  1.00  14.43 ? 54  SER B N   1 
ATOM   431  C  CA  . SER A 1 56  ? -28.574 -4.897  18.337  1.00  16.92 ? 54  SER B CA  1 
ATOM   432  C  C   . SER A 1 56  ? -27.422 -4.172  19.067  1.00  17.30 ? 54  SER B C   1 
ATOM   433  O  O   . SER A 1 56  ? -27.499 -2.966  19.280  1.00  18.95 ? 54  SER B O   1 
ATOM   434  C  CB  . SER A 1 56  ? -29.802 -5.004  19.244  1.00  17.70 ? 54  SER B CB  1 
ATOM   435  O  OG  . SER A 1 56  ? -29.400 -5.269  20.614  1.00  25.96 ? 54  SER B OG  1 
ATOM   436  N  N   . SER A 1 57  ? -26.321 -4.907  19.345  1.00  12.92 ? 55  SER B N   1 
ATOM   437  C  CA  . SER A 1 57  ? -25.113 -4.349  19.985  1.00  13.31 ? 55  SER B CA  1 
ATOM   438  C  C   . SER A 1 57  ? -24.437 -3.316  19.034  1.00  13.24 ? 55  SER B C   1 
ATOM   439  O  O   . SER A 1 57  ? -23.827 -2.385  19.512  1.00  14.06 ? 55  SER B O   1 
ATOM   440  C  CB  . SER A 1 57  ? -24.069 -5.475  20.303  1.00  13.40 ? 55  SER B CB  1 
ATOM   441  O  OG  . SER A 1 57  ? -24.544 -6.195  21.393  1.00  14.61 ? 55  SER B OG  1 
ATOM   442  N  N   . ALA A 1 58  ? -24.510 -3.514  17.701  1.00  12.32 ? 56  ALA B N   1 
ATOM   443  C  CA  . ALA A 1 58  ? -23.891 -2.547  16.827  1.00  11.97 ? 56  ALA B CA  1 
ATOM   444  C  C   . ALA A 1 58  ? -24.615 -1.216  16.880  1.00  12.62 ? 56  ALA B C   1 
ATOM   445  O  O   . ALA A 1 58  ? -25.844 -1.212  16.853  1.00  12.56 ? 56  ALA B O   1 
ATOM   446  C  CB  . ALA A 1 58  ? -23.883 -3.069  15.377  1.00  11.28 ? 56  ALA B CB  1 
ATOM   447  N  N   . LYS A 1 59  ? -23.833 -0.109  17.008  1.00  11.86 ? 57  LYS B N   1 
ATOM   448  C  CA  . LYS A 1 59  ? -24.521 1.203   17.028  1.00  13.11 ? 57  LYS B CA  1 
ATOM   449  C  C   . LYS A 1 59  ? -24.100 2.244   16.012  1.00  14.02 ? 57  LYS B C   1 
ATOM   450  O  O   . LYS A 1 59  ? -24.970 3.012   15.573  1.00  13.91 ? 57  LYS B O   1 
ATOM   451  C  CB  . LYS A 1 59  ? -24.319 1.840   18.384  1.00  11.21 ? 57  LYS B CB  1 
ATOM   452  C  CG  . LYS A 1 59  ? -24.841 0.949   19.534  1.00  11.47 ? 57  LYS B CG  1 
ATOM   453  C  CD  . LYS A 1 59  ? -26.373 0.765   19.565  1.00  11.89 ? 57  LYS B CD  1 
ATOM   454  C  CE  . LYS A 1 59  ? -26.858 -0.033  20.813  1.00  13.92 ? 57  LYS B CE  1 
ATOM   455  N  NZ  . LYS A 1 59  ? -28.251 -0.519  20.634  1.00  16.87 ? 57  LYS B NZ  1 
ATOM   456  N  N   . ILE A 1 60  ? -22.790 2.326   15.716  1.00  14.91 ? 58  ILE B N   1 
ATOM   457  C  CA  . ILE A 1 60  ? -22.241 3.419   14.902  1.00  17.67 ? 58  ILE B CA  1 
ATOM   458  C  C   . ILE A 1 60  ? -21.162 2.874   14.012  1.00  15.24 ? 58  ILE B C   1 
ATOM   459  O  O   . ILE A 1 60  ? -20.423 1.956   14.431  1.00  15.62 ? 58  ILE B O   1 
ATOM   460  C  CB  . ILE A 1 60  ? -21.586 4.449   15.886  1.00  17.39 ? 58  ILE B CB  1 
ATOM   461  C  CG1 . ILE A 1 60  ? -22.691 5.051   16.780  1.00  22.73 ? 58  ILE B CG1 1 
ATOM   462  C  CG2 . ILE A 1 60  ? -20.922 5.605   15.142  1.00  22.55 ? 58  ILE B CG2 1 
ATOM   463  C  CD1 . ILE A 1 60  ? -22.257 5.619   18.105  1.00  28.62 ? 58  ILE B CD1 1 
ATOM   464  N  N   . ILE A 1 61  ? -21.056 3.424   12.801  1.00  13.18 ? 59  ILE B N   1 
ATOM   465  C  CA  . ILE A 1 61  ? -19.872 3.125   11.957  1.00  12.69 ? 59  ILE B CA  1 
ATOM   466  C  C   . ILE A 1 61  ? -19.157 4.470   11.640  1.00  13.20 ? 59  ILE B C   1 
ATOM   467  O  O   . ILE A 1 61  ? -19.857 5.453   11.426  1.00  14.63 ? 59  ILE B O   1 
ATOM   468  C  CB  . ILE A 1 61  ? -20.270 2.375   10.678  1.00  12.88 ? 59  ILE B CB  1 
ATOM   469  C  CG1 . ILE A 1 61  ? -18.995 1.870   9.964   1.00  13.13 ? 59  ILE B CG1 1 
ATOM   470  C  CG2 . ILE A 1 61  ? -21.136 3.205   9.692   1.00  13.28 ? 59  ILE B CG2 1 
ATOM   471  C  CD1 . ILE A 1 61  ? -19.270 0.938   8.794   1.00  14.98 ? 59  ILE B CD1 1 
ATOM   472  N  N   . SER A 1 62  ? -17.850 4.499   11.773  1.00  13.89 ? 60  SER B N   1 
ATOM   473  C  CA  . SER A 1 62  ? -17.094 5.779   11.630  1.00  12.61 ? 60  SER B CA  1 
ATOM   474  C  C   . SER A 1 62  ? -15.854 5.523   10.745  1.00  13.96 ? 60  SER B C   1 
ATOM   475  O  O   . SER A 1 62  ? -15.442 4.357   10.556  1.00  12.62 ? 60  SER B O   1 
ATOM   476  C  CB  . SER A 1 62  ? -16.779 6.360   12.994  1.00  14.24 ? 60  SER B CB  1 
ATOM   477  O  OG  . SER A 1 62  ? -15.919 5.521   13.688  1.00  18.70 ? 60  SER B OG  1 
ATOM   478  N  N   . ASN A 1 63  ? -15.339 6.582   10.099  1.00  13.02 ? 61  ASN B N   1 
ATOM   479  C  CA  . ASN A 1 63  ? -14.035 6.569   9.504   1.00  12.86 ? 61  ASN B CA  1 
ATOM   480  C  C   . ASN A 1 63  ? -13.026 7.160   10.485  1.00  13.30 ? 61  ASN B C   1 
ATOM   481  O  O   . ASN A 1 63  ? -13.066 8.385   10.806  1.00  14.45 ? 61  ASN B O   1 
ATOM   482  C  CB  . ASN A 1 63  ? -14.089 7.365   8.152   1.00  13.66 ? 61  ASN B CB  1 
ATOM   483  C  CG  . ASN A 1 63  ? -12.763 7.435   7.455   1.00  14.86 ? 61  ASN B CG  1 
ATOM   484  O  OD1 . ASN A 1 63  ? -11.775 6.882   7.941   1.00  13.81 ? 61  ASN B OD1 1 
ATOM   485  N  ND2 . ASN A 1 63  ? -12.724 8.126   6.270   1.00  13.85 ? 61  ASN B ND2 1 
ATOM   486  N  N   . SER A 1 64  ? -12.135 6.307   10.992  1.00  11.99 ? 62  SER B N   1 
ATOM   487  C  CA  . SER A 1 64  ? -11.040 6.771   11.936  1.00  13.08 ? 62  SER B CA  1 
ATOM   488  C  C   . SER A 1 64  ? -9.875  7.495   11.180  1.00  14.60 ? 62  SER B C   1 
ATOM   489  O  O   . SER A 1 64  ? -8.944  8.021   11.820  1.00  18.89 ? 62  SER B O   1 
ATOM   490  C  CB  . SER A 1 64  ? -10.446 5.592   12.714  1.00  13.56 ? 62  SER B CB  1 
ATOM   491  O  OG  . SER A 1 64  ? -9.680  4.708   11.826  1.00  12.72 ? 62  SER B OG  1 
ATOM   492  N  N   . GLY A 1 65  ? -9.876  7.455   9.841   1.00  12.65 ? 63  GLY B N   1 
ATOM   493  C  CA  . GLY A 1 65  ? -8.673  7.790   9.101   1.00  13.39 ? 63  GLY B CA  1 
ATOM   494  C  C   . GLY A 1 65  ? -7.764  6.597   8.825   1.00  13.34 ? 63  GLY B C   1 
ATOM   495  O  O   . GLY A 1 65  ? -6.980  6.643   7.871   1.00  15.25 ? 63  GLY B O   1 
ATOM   496  N  N   . HIS A 1 66  ? -7.920  5.493   9.608   1.00  13.85 ? 64  HIS B N   1 
ATOM   497  C  CA  . HIS A 1 66  ? -7.068  4.276   9.551   1.00  12.25 ? 64  HIS B CA  1 
ATOM   498  C  C   . HIS A 1 66  ? -7.800  3.012   9.090   1.00  12.03 ? 64  HIS B C   1 
ATOM   499  O  O   . HIS A 1 66  ? -7.135  2.047   8.745   1.00  12.73 ? 64  HIS B O   1 
ATOM   500  C  CB  . HIS A 1 66  ? -6.454  3.973   10.898  1.00  14.18 ? 64  HIS B CB  1 
ATOM   501  C  CG  . HIS A 1 66  ? -5.863  5.197   11.547  1.00  18.35 ? 64  HIS B CG  1 
ATOM   502  N  ND1 . HIS A 1 66  ? -6.383  5.761   12.723  1.00  18.82 ? 64  HIS B ND1 1 
ATOM   503  C  CD2 . HIS A 1 66  ? -4.871  6.050   11.088  1.00  17.31 ? 64  HIS B CD2 1 
ATOM   504  C  CE1 . HIS A 1 66  ? -5.652  6.896   13.007  1.00  18.43 ? 64  HIS B CE1 1 
ATOM   505  N  NE2 . HIS A 1 66  ? -4.775  7.099   12.008  1.00  18.90 ? 64  HIS B NE2 1 
ATOM   506  N  N   . SER A 1 67  ? -9.139  3.032   9.219   1.00  12.94 ? 65  SER B N   1 
ATOM   507  C  CA  . SER A 1 67  ? -10.040 1.937   8.759   1.00  12.91 ? 65  SER B CA  1 
ATOM   508  C  C   . SER A 1 67  ? -11.435 2.498   8.985   1.00  12.36 ? 65  SER B C   1 
ATOM   509  O  O   . SER A 1 67  ? -11.561 3.681   9.453   1.00  12.52 ? 65  SER B O   1 
ATOM   510  C  CB  . SER A 1 67  ? -9.888  0.653   9.625   1.00  12.63 ? 65  SER B CB  1 
ATOM   511  O  OG  . SER A 1 67  ? -10.649 -0.435  9.044   1.00  12.32 ? 65  SER B OG  1 
ATOM   512  N  N   . PHE A 1 68  ? -12.485 1.701   8.706   1.00  12.11 ? 66  PHE B N   1 
ATOM   513  C  CA  . PHE A 1 68  ? -13.809 2.039   9.330   1.00  12.83 ? 66  PHE B CA  1 
ATOM   514  C  C   . PHE A 1 68  ? -13.852 1.294   10.683  1.00  13.14 ? 66  PHE B C   1 
ATOM   515  O  O   . PHE A 1 68  ? -13.125 0.345   10.886  1.00  13.50 ? 66  PHE B O   1 
ATOM   516  C  CB  . PHE A 1 68  ? -15.032 1.547   8.512   1.00  12.75 ? 66  PHE B CB  1 
ATOM   517  C  CG  . PHE A 1 68  ? -15.175 0.043   8.485   1.00  12.99 ? 66  PHE B CG  1 
ATOM   518  C  CD1 . PHE A 1 68  ? -14.560 -0.678  7.447   1.00  13.94 ? 66  PHE B CD1 1 
ATOM   519  C  CD2 . PHE A 1 68  ? -15.882 -0.685  9.526   1.00  11.79 ? 66  PHE B CD2 1 
ATOM   520  C  CE1 . PHE A 1 68  ? -14.721 -2.061  7.363   1.00  13.03 ? 66  PHE B CE1 1 
ATOM   521  C  CE2 . PHE A 1 68  ? -15.969 -2.053  9.462   1.00  13.96 ? 66  PHE B CE2 1 
ATOM   522  C  CZ  . PHE A 1 68  ? -15.390 -2.752  8.408   1.00  13.75 ? 66  PHE B CZ  1 
ATOM   523  N  N   . ASN A 1 69  ? -14.654 1.808   11.624  1.00  12.90 ? 67  ASN B N   1 
ATOM   524  C  CA  . ASN A 1 69  ? -14.887 1.124   12.896  1.00  12.79 ? 67  ASN B CA  1 
ATOM   525  C  C   . ASN A 1 69  ? -16.392 0.983   13.064  1.00  14.46 ? 67  ASN B C   1 
ATOM   526  O  O   . ASN A 1 69  ? -17.133 2.004   13.065  1.00  14.03 ? 67  ASN B O   1 
ATOM   527  C  CB  . ASN A 1 69  ? -14.416 2.000   14.070  1.00  14.84 ? 67  ASN B CB  1 
ATOM   528  C  CG  . ASN A 1 69  ? -12.918 2.276   14.069  1.00  16.24 ? 67  ASN B CG  1 
ATOM   529  O  OD1 . ASN A 1 69  ? -12.148 1.567   13.480  1.00  22.65 ? 67  ASN B OD1 1 
ATOM   530  N  ND2 . ASN A 1 69  ? -12.507 3.313   14.784  1.00  20.90 ? 67  ASN B ND2 1 
ATOM   531  N  N   . VAL A 1 70  ? -16.869 -0.248  13.295  1.00  13.00 ? 68  VAL B N   1 
ATOM   532  C  CA  . VAL A 1 70  ? -18.213 -0.466  13.788  1.00  12.43 ? 68  VAL B CA  1 
ATOM   533  C  C   . VAL A 1 70  ? -18.008 -0.538  15.317  1.00  13.22 ? 68  VAL B C   1 
ATOM   534  O  O   . VAL A 1 70  ? -17.252 -1.402  15.850  1.00  12.40 ? 68  VAL B O   1 
ATOM   535  C  CB  . VAL A 1 70  ? -18.880 -1.766  13.182  1.00  14.22 ? 68  VAL B CB  1 
ATOM   536  C  CG1 . VAL A 1 70  ? -20.286 -2.050  13.786  1.00  13.91 ? 68  VAL B CG1 1 
ATOM   537  C  CG2 . VAL A 1 70  ? -19.098 -1.602  11.663  1.00  15.02 ? 68  VAL B CG2 1 
ATOM   538  N  N   . ASP A 1 71  ? -18.634 0.388   16.055  1.00  12.05 ? 69  ASP B N   1 
ATOM   539  C  CA  . ASP A 1 71  ? -18.531 0.354   17.464  1.00  12.64 ? 69  ASP B CA  1 
ATOM   540  C  C   . ASP A 1 71  ? -19.813 -0.254  18.078  1.00  12.07 ? 69  ASP B C   1 
ATOM   541  O  O   . ASP A 1 71  ? -20.936 0.009   17.619  1.00  11.44 ? 69  ASP B O   1 
ATOM   542  C  CB  . ASP A 1 71  ? -18.411 1.755   18.011  1.00  15.24 ? 69  ASP B CB  1 
ATOM   543  C  CG  . ASP A 1 71  ? -17.102 2.422   17.591  1.00  20.30 ? 69  ASP B CG  1 
ATOM   544  O  OD1 . ASP A 1 71  ? -16.100 1.683   17.373  1.00  25.44 ? 69  ASP B OD1 1 
ATOM   545  O  OD2 . ASP A 1 71  ? -17.089 3.672   17.563  1.00  24.71 ? 69  ASP B OD2 1 
ATOM   546  N  N   . PHE A 1 72  ? -19.579 -1.076  19.081  1.00  11.96 ? 70  PHE B N   1 
ATOM   547  C  CA  . PHE A 1 72  ? -20.679 -1.835  19.783  1.00  12.63 ? 70  PHE B CA  1 
ATOM   548  C  C   . PHE A 1 72  ? -20.826 -1.242  21.162  1.00  11.78 ? 70  PHE B C   1 
ATOM   549  O  O   . PHE A 1 72  ? -19.844 -0.857  21.832  1.00  16.09 ? 70  PHE B O   1 
ATOM   550  C  CB  . PHE A 1 72  ? -20.350 -3.336  19.888  1.00  11.86 ? 70  PHE B CB  1 
ATOM   551  C  CG  . PHE A 1 72  ? -20.219 -3.989  18.508  1.00  12.51 ? 70  PHE B CG  1 
ATOM   552  C  CD1 . PHE A 1 72  ? -19.051 -3.781  17.747  1.00  15.34 ? 70  PHE B CD1 1 
ATOM   553  C  CD2 . PHE A 1 72  ? -21.217 -4.706  17.989  1.00  11.89 ? 70  PHE B CD2 1 
ATOM   554  C  CE1 . PHE A 1 72  ? -18.952 -4.315  16.463  1.00  13.15 ? 70  PHE B CE1 1 
ATOM   555  C  CE2 . PHE A 1 72  ? -21.141 -5.276  16.722  1.00  14.61 ? 70  PHE B CE2 1 
ATOM   556  C  CZ  . PHE A 1 72  ? -19.959 -5.081  15.983  1.00  13.57 ? 70  PHE B CZ  1 
ATOM   557  N  N   . ASP A 1 73  ? -22.071 -1.232  21.610  1.00  12.52 ? 71  ASP B N   1 
ATOM   558  C  CA  . ASP A 1 73  ? -22.367 -0.844  22.987  1.00  11.72 ? 71  ASP B CA  1 
ATOM   559  C  C   . ASP A 1 73  ? -21.875 -1.942  23.880  1.00  13.26 ? 71  ASP B C   1 
ATOM   560  O  O   . ASP A 1 73  ? -22.423 -3.062  23.823  1.00  15.34 ? 71  ASP B O   1 
ATOM   561  C  CB  . ASP A 1 73  ? -23.870 -0.715  23.093  1.00  12.54 ? 71  ASP B CB  1 
ATOM   562  C  CG  . ASP A 1 73  ? -24.285 -0.433  24.552  1.00  13.16 ? 71  ASP B CG  1 
ATOM   563  O  OD1 . ASP A 1 73  ? -23.414 -0.146  25.362  1.00  16.04 ? 71  ASP B OD1 1 
ATOM   564  O  OD2 . ASP A 1 73  ? -25.470 -0.396  24.836  1.00  16.95 ? 71  ASP B OD2 1 
ATOM   565  N  N   . ASP A 1 74  ? -20.822 -1.649  24.633  1.00  11.49 ? 72  ASP B N   1 
ATOM   566  C  CA  . ASP A 1 74  ? -20.175 -2.612  25.553  1.00  13.86 ? 72  ASP B CA  1 
ATOM   567  C  C   . ASP A 1 74  ? -20.421 -2.213  27.032  1.00  14.16 ? 72  ASP B C   1 
ATOM   568  O  O   . ASP A 1 74  ? -19.544 -2.377  27.891  1.00  14.71 ? 72  ASP B O   1 
ATOM   569  C  CB  . ASP A 1 74  ? -18.654 -2.746  25.301  1.00  14.69 ? 72  ASP B CB  1 
ATOM   570  C  CG  . ASP A 1 74  ? -17.823 -1.505  25.746  1.00  16.70 ? 72  ASP B CG  1 
ATOM   571  O  OD1 . ASP A 1 74  ? -18.452 -0.425  25.984  1.00  19.29 ? 72  ASP B OD1 1 
ATOM   572  O  OD2 . ASP A 1 74  ? -16.572 -1.516  25.839  1.00  17.77 ? 72  ASP B OD2 1 
ATOM   573  N  N   . THR A 1 75  ? -21.595 -1.646  27.260  1.00  14.99 ? 73  THR B N   1 
ATOM   574  C  CA  . THR A 1 75  ? -22.093 -1.273  28.623  1.00  15.07 ? 73  THR B CA  1 
ATOM   575  C  C   . THR A 1 75  ? -22.292 -2.572  29.417  1.00  15.76 ? 73  THR B C   1 
ATOM   576  O  O   . THR A 1 75  ? -22.126 -2.561  30.638  1.00  16.96 ? 73  THR B O   1 
ATOM   577  C  CB  . THR A 1 75  ? -23.523 -0.650  28.539  1.00  15.98 ? 73  THR B CB  1 
ATOM   578  O  OG1 . THR A 1 75  ? -23.452 0.578   27.791  1.00  14.97 ? 73  THR B OG1 1 
ATOM   579  C  CG2 . THR A 1 75  ? -24.076 -0.295  29.966  1.00  17.68 ? 73  THR B CG2 1 
ATOM   580  N  N   . GLU A 1 76  ? -22.783 -3.628  28.795  1.00  18.22 ? 74  GLU B N   1 
ATOM   581  C  CA  . GLU A 1 76  ? -22.874 -4.900  29.574  1.00  20.59 ? 74  GLU B CA  1 
ATOM   582  C  C   . GLU A 1 76  ? -22.568 -6.126  28.707  1.00  20.00 ? 74  GLU B C   1 
ATOM   583  O  O   . GLU A 1 76  ? -21.882 -5.948  27.701  1.00  18.15 ? 74  GLU B O   1 
ATOM   584  C  CB  . GLU A 1 76  ? -24.180 -5.008  30.332  1.00  24.27 ? 74  GLU B CB  1 
ATOM   585  C  CG  . GLU A 1 76  ? -25.399 -5.268  29.457  1.00  26.23 ? 74  GLU B CG  1 
ATOM   586  C  CD  . GLU A 1 76  ? -26.665 -5.445  30.286  1.00  34.82 ? 74  GLU B CD  1 
ATOM   587  O  OE1 . GLU A 1 76  ? -27.803 -5.378  29.724  1.00  39.07 ? 74  GLU B OE1 1 
ATOM   588  O  OE2 . GLU A 1 76  ? -26.504 -5.682  31.509  1.00  35.83 ? 74  GLU B OE2 1 
ATOM   589  N  N   . ASN A 1 77  ? -22.876 -7.331  29.192  1.00  17.97 ? 75  ASN B N   1 
ATOM   590  C  CA  . ASN A 1 77  ? -22.363 -8.566  28.599  1.00  17.55 ? 75  ASN B CA  1 
ATOM   591  C  C   . ASN A 1 77  ? -23.303 -9.182  27.630  1.00  16.31 ? 75  ASN B C   1 
ATOM   592  O  O   . ASN A 1 77  ? -23.501 -10.389 27.675  1.00  19.32 ? 75  ASN B O   1 
ATOM   593  C  CB  . ASN A 1 77  ? -22.037 -9.611  29.684  1.00  17.83 ? 75  ASN B CB  1 
ATOM   594  C  CG  . ASN A 1 77  ? -20.611 -9.530  30.151  1.00  17.02 ? 75  ASN B CG  1 
ATOM   595  O  OD1 . ASN A 1 77  ? -19.711 -8.933  29.502  1.00  14.02 ? 75  ASN B OD1 1 
ATOM   596  N  ND2 . ASN A 1 77  ? -20.352 -10.181 31.295  1.00  17.95 ? 75  ASN B ND2 1 
ATOM   597  N  N   . LYS A 1 78  ? -23.944 -8.415  26.757  1.00  13.12 ? 76  LYS B N   1 
ATOM   598  C  CA  . LYS A 1 78  ? -24.833 -9.018  25.711  1.00  14.65 ? 76  LYS B CA  1 
ATOM   599  C  C   . LYS A 1 78  ? -24.033 -9.735  24.553  1.00  13.88 ? 76  LYS B C   1 
ATOM   600  O  O   . LYS A 1 78  ? -24.513 -10.753 24.011  1.00  13.40 ? 76  LYS B O   1 
ATOM   601  C  CB  . LYS A 1 78  ? -25.735 -7.979  25.059  1.00  19.89 ? 76  LYS B CB  1 
ATOM   602  C  CG  . LYS A 1 78  ? -26.814 -7.403  26.021  1.00  22.46 ? 76  LYS B CG  1 
ATOM   603  C  CD  . LYS A 1 78  ? -27.523 -6.218  25.338  1.00  28.82 ? 76  LYS B CD  1 
ATOM   604  C  CE  . LYS A 1 78  ? -28.437 -5.458  26.335  1.00  32.86 ? 76  LYS B CE  1 
ATOM   605  N  NZ  . LYS A 1 78  ? -28.769 -4.028  25.945  1.00  30.32 ? 76  LYS B NZ  1 
ATOM   606  N  N   . SER A 1 79  ? -22.829 -9.253  24.254  1.00  12.63 ? 77  SER B N   1 
ATOM   607  C  CA  . SER A 1 79  ? -22.062 -9.827  23.115  1.00  11.18 ? 77  SER B CA  1 
ATOM   608  C  C   . SER A 1 79  ? -20.673 -10.169 23.713  1.00  10.49 ? 77  SER B C   1 
ATOM   609  O  O   . SER A 1 79  ? -19.911 -9.240  24.161  1.00  10.49 ? 77  SER B O   1 
ATOM   610  C  CB  . SER A 1 79  ? -21.943 -8.786  21.991  1.00  10.59 ? 77  SER B CB  1 
ATOM   611  O  OG  . SER A 1 79  ? -23.237 -8.631  21.456  1.00  11.33 ? 77  SER B OG  1 
ATOM   612  N  N   . VAL A 1 80  ? -20.360 -11.486 23.786  1.00  9.77  ? 78  VAL B N   1 
ATOM   613  C  CA  . VAL A 1 80  ? -19.113 -11.907 24.456  1.00  9.64  ? 78  VAL B CA  1 
ATOM   614  C  C   . VAL A 1 80  ? -18.484 -13.102 23.716  1.00  9.80  ? 78  VAL B C   1 
ATOM   615  O  O   . VAL A 1 80  ? -19.225 -13.948 23.058  1.00  10.45 ? 78  VAL B O   1 
ATOM   616  C  CB  . VAL A 1 80  ? -19.358 -12.358 25.921  1.00  10.76 ? 78  VAL B CB  1 
ATOM   617  C  CG1 . VAL A 1 80  ? -19.793 -11.180 26.836  1.00  11.14 ? 78  VAL B CG1 1 
ATOM   618  C  CG2 . VAL A 1 80  ? -20.425 -13.440 25.939  1.00  12.92 ? 78  VAL B CG2 1 
ATOM   619  N  N   . LEU A 1 81  ? -17.155 -13.214 23.873  1.00  8.69  ? 79  LEU B N   1 
ATOM   620  C  CA  . LEU A 1 81  ? -16.411 -14.368 23.336  1.00  8.86  ? 79  LEU B CA  1 
ATOM   621  C  C   . LEU A 1 81  ? -15.814 -15.095 24.526  1.00  9.65  ? 79  LEU B C   1 
ATOM   622  O  O   . LEU A 1 81  ? -15.179 -14.442 25.403  1.00  9.15  ? 79  LEU B O   1 
ATOM   623  C  CB  . LEU A 1 81  ? -15.264 -13.796 22.435  1.00  9.30  ? 79  LEU B CB  1 
ATOM   624  C  CG  . LEU A 1 81  ? -14.230 -14.833 21.896  1.00  8.78  ? 79  LEU B CG  1 
ATOM   625  C  CD1 . LEU A 1 81  ? -14.974 -15.792 20.975  1.00  9.87  ? 79  LEU B CD1 1 
ATOM   626  C  CD2 . LEU A 1 81  ? -13.104 -14.082 21.132  1.00  9.57  ? 79  LEU B CD2 1 
ATOM   627  N  N   . ARG A 1 82  ? -15.973 -16.443 24.508  1.00  9.54  ? 80  ARG B N   1 
ATOM   628  C  CA  . ARG A 1 82  ? -15.370 -17.319 25.575  1.00  9.73  ? 80  ARG B CA  1 
ATOM   629  C  C   . ARG A 1 82  ? -14.822 -18.544 24.885  1.00  10.30 ? 80  ARG B C   1 
ATOM   630  O  O   . ARG A 1 82  ? -14.923 -18.651 23.650  1.00  10.38 ? 80  ARG B O   1 
ATOM   631  C  CB  . ARG A 1 82  ? -16.471 -17.701 26.575  1.00  10.12 ? 80  ARG B CB  1 
ATOM   632  C  CG  . ARG A 1 82  ? -16.975 -16.519 27.404  1.00  11.37 ? 80  ARG B CG  1 
ATOM   633  C  CD  . ARG A 1 82  ? -18.255 -16.860 28.162  1.00  13.51 ? 80  ARG B CD  1 
ATOM   634  N  NE  . ARG A 1 82  ? -19.405 -16.928 27.238  1.00  15.15 ? 80  ARG B NE  1 
ATOM   635  C  CZ  . ARG A 1 82  ? -20.650 -17.207 27.604  1.00  20.59 ? 80  ARG B CZ  1 
ATOM   636  N  NH1 . ARG A 1 82  ? -20.900 -17.344 28.909  1.00  21.25 ? 80  ARG B NH1 1 
ATOM   637  N  NH2 . ARG A 1 82  ? -21.641 -17.304 26.688  1.00  19.46 ? 80  ARG B NH2 1 
ATOM   638  N  N   . GLY A 1 83  ? -14.257 -19.464 25.686  1.00  10.21 ? 81  GLY B N   1 
ATOM   639  C  CA  . GLY A 1 83  ? -13.600 -20.652 25.151  1.00  10.27 ? 81  GLY B CA  1 
ATOM   640  C  C   . GLY A 1 83  ? -12.344 -20.311 24.400  1.00  10.65 ? 81  GLY B C   1 
ATOM   641  O  O   . GLY A 1 83  ? -11.684 -19.310 24.690  1.00  11.12 ? 81  GLY B O   1 
ATOM   642  N  N   . GLY A 1 84  ? -12.094 -21.098 23.350  1.00  11.67 ? 82  GLY B N   1 
ATOM   643  C  CA  . GLY A 1 84  ? -10.797 -20.929 22.589  1.00  10.72 ? 82  GLY B CA  1 
ATOM   644  C  C   . GLY A 1 84  ? -9.681  -21.044 23.593  1.00  10.18 ? 82  GLY B C   1 
ATOM   645  O  O   . GLY A 1 84  ? -9.748  -21.893 24.471  1.00  10.40 ? 82  GLY B O   1 
ATOM   646  N  N   . PRO A 1 85  ? -8.617  -20.190 23.494  1.00  10.10 ? 83  PRO B N   1 
ATOM   647  C  CA  . PRO A 1 85  ? -7.515  -20.158 24.516  1.00  10.18 ? 83  PRO B CA  1 
ATOM   648  C  C   . PRO A 1 85  ? -7.800  -19.294 25.786  1.00  10.24 ? 83  PRO B C   1 
ATOM   649  O  O   . PRO A 1 85  ? -6.917  -19.117 26.606  1.00  13.32 ? 83  PRO B O   1 
ATOM   650  C  CB  . PRO A 1 85  ? -6.335  -19.472 23.714  1.00  10.96 ? 83  PRO B CB  1 
ATOM   651  C  CG  . PRO A 1 85  ? -7.121  -18.401 22.864  1.00  9.73  ? 83  PRO B CG  1 
ATOM   652  C  CD  . PRO A 1 85  ? -8.398  -19.165 22.399  1.00  9.72  ? 83  PRO B CD  1 
ATOM   653  N  N   . LEU A 1 86  ? -9.002  -18.732 25.892  1.00  10.38 ? 84  LEU B N   1 
ATOM   654  C  CA  . LEU A 1 86  ? -9.299  -17.685 26.847  1.00  10.11 ? 84  LEU B CA  1 
ATOM   655  C  C   . LEU A 1 86  ? -9.719  -18.162 28.195  1.00  11.34 ? 84  LEU B C   1 
ATOM   656  O  O   . LEU A 1 86  ? -10.465 -19.101 28.302  1.00  13.49 ? 84  LEU B O   1 
ATOM   657  C  CB  . LEU A 1 86  ? -10.424 -16.797 26.303  1.00  10.24 ? 84  LEU B CB  1 
ATOM   658  C  CG  . LEU A 1 86  ? -10.161 -16.088 24.922  1.00  8.73  ? 84  LEU B CG  1 
ATOM   659  C  CD1 . LEU A 1 86  ? -11.416 -15.354 24.364  1.00  9.50  ? 84  LEU B CD1 1 
ATOM   660  C  CD2 . LEU A 1 86  ? -8.930  -15.128 24.939  1.00  8.98  ? 84  LEU B CD2 1 
ATOM   661  N  N   . THR A 1 87  ? -9.270  -17.452 29.200  1.00  11.77 ? 85  THR B N   1 
ATOM   662  C  CA  . THR A 1 87  ? -9.805  -17.666 30.546  1.00  13.16 ? 85  THR B CA  1 
ATOM   663  C  C   . THR A 1 87  ? -10.825 -16.566 30.739  1.00  14.60 ? 85  THR B C   1 
ATOM   664  O  O   . THR A 1 87  ? -10.467 -15.365 30.652  1.00  14.81 ? 85  THR B O   1 
ATOM   665  C  CB  . THR A 1 87  ? -8.686  -17.507 31.540  1.00  14.19 ? 85  THR B CB  1 
ATOM   666  O  OG1 . THR A 1 87  ? -7.812  -18.647 31.371  1.00  18.90 ? 85  THR B OG1 1 
ATOM   667  C  CG2 . THR A 1 87  ? -9.269  -17.565 33.031  1.00  17.83 ? 85  THR B CG2 1 
ATOM   668  N  N   . GLY A 1 88  ? -12.072 -16.951 31.029  1.00  12.80 ? 86  GLY B N   1 
ATOM   669  C  CA  . GLY A 1 88  ? -13.091 -15.931 31.359  1.00  14.20 ? 86  GLY B CA  1 
ATOM   670  C  C   . GLY A 1 88  ? -13.733 -15.286 30.114  1.00  13.83 ? 86  GLY B C   1 
ATOM   671  O  O   . GLY A 1 88  ? -13.585 -15.815 28.960  1.00  15.38 ? 86  GLY B O   1 
ATOM   672  N  N   . SER A 1 89  ? -14.376 -14.138 30.317  1.00  12.10 ? 87  SER B N   1 
ATOM   673  C  CA  . SER A 1 89  ? -15.349 -13.669 29.315  1.00  11.43 ? 87  SER B CA  1 
ATOM   674  C  C   . SER A 1 89  ? -14.827 -12.407 28.756  1.00  11.16 ? 87  SER B C   1 
ATOM   675  O  O   . SER A 1 89  ? -14.504 -11.445 29.536  1.00  11.39 ? 87  SER B O   1 
ATOM   676  C  CB  . SER A 1 89  ? -16.750 -13.413 30.013  1.00  11.64 ? 87  SER B CB  1 
ATOM   677  O  OG  . SER A 1 89  ? -17.712 -13.067 29.040  1.00  13.45 ? 87  SER B OG  1 
ATOM   678  N  N   . TYR A 1 90  ? -14.787 -12.328 27.409  1.00  10.94 ? 88  TYR B N   1 
ATOM   679  C  CA  . TYR A 1 90  ? -14.251 -11.111 26.680  1.00  8.85  ? 88  TYR B CA  1 
ATOM   680  C  C   . TYR A 1 90  ? -15.340 -10.404 25.918  1.00  9.60  ? 88  TYR B C   1 
ATOM   681  O  O   . TYR A 1 90  ? -16.060 -11.017 25.105  1.00  11.01 ? 88  TYR B O   1 
ATOM   682  C  CB  . TYR A 1 90  ? -13.069 -11.566 25.735  1.00  8.82  ? 88  TYR B CB  1 
ATOM   683  C  CG  . TYR A 1 90  ? -11.787 -11.873 26.473  1.00  8.62  ? 88  TYR B CG  1 
ATOM   684  C  CD1 . TYR A 1 90  ? -11.686 -13.022 27.294  1.00  8.24  ? 88  TYR B CD1 1 
ATOM   685  C  CD2 . TYR A 1 90  ? -10.650 -11.018 26.356  1.00  8.51  ? 88  TYR B CD2 1 
ATOM   686  C  CE1 . TYR A 1 90  ? -10.509 -13.295 27.982  1.00  9.34  ? 88  TYR B CE1 1 
ATOM   687  C  CE2 . TYR A 1 90  ? -9.444  -11.299 26.998  1.00  8.30  ? 88  TYR B CE2 1 
ATOM   688  C  CZ  . TYR A 1 90  ? -9.406  -12.463 27.820  1.00  9.23  ? 88  TYR B CZ  1 
ATOM   689  O  OH  . TYR A 1 90  ? -8.233  -12.709 28.434  1.00  10.22 ? 88  TYR B OH  1 
ATOM   690  N  N   . ARG A 1 91  ? -15.548 -9.150  26.240  1.00  8.27  ? 89  ARG B N   1 
ATOM   691  C  CA  . ARG A 1 91  ? -16.742 -8.399  25.779  1.00  8.12  ? 89  ARG B CA  1 
ATOM   692  C  C   . ARG A 1 91  ? -16.458 -7.716  24.422  1.00  8.33  ? 89  ARG B C   1 
ATOM   693  O  O   . ARG A 1 91  ? -15.453 -7.038  24.244  1.00  8.16  ? 89  ARG B O   1 
ATOM   694  C  CB  . ARG A 1 91  ? -17.095 -7.370  26.863  1.00  8.85  ? 89  ARG B CB  1 
ATOM   695  C  CG  . ARG A 1 91  ? -18.362 -6.627  26.535  1.00  10.15 ? 89  ARG B CG  1 
ATOM   696  C  CD  . ARG A 1 91  ? -18.679 -5.593  27.618  1.00  10.60 ? 89  ARG B CD  1 
ATOM   697  N  NE  . ARG A 1 91  ? -18.874 -6.301  28.916  1.00  11.90 ? 89  ARG B NE  1 
ATOM   698  C  CZ  . ARG A 1 91  ? -18.951 -5.651  30.104  1.00  12.91 ? 89  ARG B CZ  1 
ATOM   699  N  NH1 . ARG A 1 91  ? -19.051 -4.293  30.097  1.00  11.43 ? 89  ARG B NH1 1 
ATOM   700  N  NH2 . ARG A 1 91  ? -19.049 -6.354  31.278  1.00  11.31 ? 89  ARG B NH2 1 
ATOM   701  N  N   . LEU A 1 92  ? -17.397 -7.859  23.486  1.00  8.20  ? 90  LEU B N   1 
ATOM   702  C  CA  . LEU A 1 92  ? -17.255 -7.259  22.138  1.00  8.52  ? 90  LEU B CA  1 
ATOM   703  C  C   . LEU A 1 92  ? -17.175 -5.734  22.219  1.00  8.74  ? 90  LEU B C   1 
ATOM   704  O  O   . LEU A 1 92  ? -18.032 -5.121  22.844  1.00  10.14 ? 90  LEU B O   1 
ATOM   705  C  CB  . LEU A 1 92  ? -18.414 -7.693  21.250  1.00  8.92  ? 90  LEU B CB  1 
ATOM   706  C  CG  . LEU A 1 92  ? -18.441 -7.048  19.845  1.00  8.41  ? 90  LEU B CG  1 
ATOM   707  C  CD1 . LEU A 1 92  ? -17.162 -7.477  19.039  1.00  10.25 ? 90  LEU B CD1 1 
ATOM   708  C  CD2 . LEU A 1 92  ? -19.761 -7.496  19.147  1.00  9.06  ? 90  LEU B CD2 1 
ATOM   709  N  N   . ARG A 1 93  ? -16.199 -5.110  21.570  1.00  9.28  ? 91  ARG B N   1 
ATOM   710  C  CA  . ARG A 1 93  ? -16.091 -3.664  21.528  1.00  10.11 ? 91  ARG B CA  1 
ATOM   711  C  C   . ARG A 1 93  ? -16.173 -3.071  20.127  1.00  10.46 ? 91  ARG B C   1 
ATOM   712  O  O   . ARG A 1 93  ? -16.939 -2.097  19.941  1.00  10.52 ? 91  ARG B O   1 
ATOM   713  C  CB  . ARG A 1 93  ? -14.739 -3.252  22.148  1.00  11.08 ? 91  ARG B CB  1 
ATOM   714  C  CG  . ARG A 1 93  ? -14.380 -1.772  21.981  1.00  15.40 ? 91  ARG B CG  1 
ATOM   715  C  CD  . ARG A 1 93  ? -14.586 -1.061  23.270  1.00  17.82 ? 91  ARG B CD  1 
ATOM   716  N  NE  . ARG A 1 93  ? -14.121 0.328   23.176  1.00  19.30 ? 91  ARG B NE  1 
ATOM   717  C  CZ  . ARG A 1 93  ? -14.423 1.250   24.087  1.00  19.32 ? 91  ARG B CZ  1 
ATOM   718  N  NH1 . ARG A 1 93  ? -15.187 0.928   25.159  1.00  20.72 ? 91  ARG B NH1 1 
ATOM   719  N  NH2 . ARG A 1 93  ? -13.946 2.485   23.915  1.00  19.48 ? 91  ARG B NH2 1 
ATOM   720  N  N   A GLN A 1 94  ? -15.526 -3.658  19.110  0.50  10.68 ? 92  GLN B N   1 
ATOM   721  N  N   B GLN A 1 94  ? -15.401 -3.595  19.167  0.50  10.13 ? 92  GLN B N   1 
ATOM   722  C  CA  A GLN A 1 94  ? -15.237 -2.889  17.893  0.50  9.83  ? 92  GLN B CA  1 
ATOM   723  C  CA  B GLN A 1 94  ? -15.426 -3.008  17.834  0.50  9.12  ? 92  GLN B CA  1 
ATOM   724  C  C   A GLN A 1 94  ? -14.878 -3.848  16.776  0.50  9.42  ? 92  GLN B C   1 
ATOM   725  C  C   B GLN A 1 94  ? -15.095 -4.008  16.755  0.50  9.10  ? 92  GLN B C   1 
ATOM   726  O  O   A GLN A 1 94  ? -14.127 -4.802  17.083  0.50  8.06  ? 92  GLN B O   1 
ATOM   727  O  O   B GLN A 1 94  ? -14.580 -5.095  17.006  0.50  7.96  ? 92  GLN B O   1 
ATOM   728  C  CB  A GLN A 1 94  ? -13.993 -2.066  18.303  0.50  11.10 ? 92  GLN B CB  1 
ATOM   729  C  CB  B GLN A 1 94  ? -14.391 -1.883  17.794  0.50  9.89  ? 92  GLN B CB  1 
ATOM   730  C  CG  A GLN A 1 94  ? -13.360 -1.045  17.429  0.50  13.69 ? 92  GLN B CG  1 
ATOM   731  C  CG  B GLN A 1 94  ? -14.122 -1.305  16.428  0.50  11.21 ? 92  GLN B CG  1 
ATOM   732  C  CD  A GLN A 1 94  ? -12.250 -1.704  16.703  0.50  12.42 ? 92  GLN B CD  1 
ATOM   733  C  CD  B GLN A 1 94  ? -12.937 -0.370  16.506  0.50  11.94 ? 92  GLN B CD  1 
ATOM   734  O  OE1 A GLN A 1 94  ? -12.521 -2.476  15.796  0.50  12.74 ? 92  GLN B OE1 1 
ATOM   735  O  OE1 B GLN A 1 94  ? -11.824 -0.714  16.081  0.50  14.42 ? 92  GLN B OE1 1 
ATOM   736  N  NE2 A GLN A 1 94  ? -11.018 -1.439  17.090  0.50  13.81 ? 92  GLN B NE2 1 
ATOM   737  N  NE2 B GLN A 1 94  ? -13.157 0.800   17.115  0.50  14.48 ? 92  GLN B NE2 1 
ATOM   738  N  N   . VAL A 1 95  ? -15.394 -3.620  15.532  1.00  9.42  ? 93  VAL B N   1 
ATOM   739  C  CA  . VAL A 1 95  ? -15.013 -4.422  14.344  1.00  9.77  ? 93  VAL B CA  1 
ATOM   740  C  C   . VAL A 1 95  ? -14.344 -3.422  13.337  1.00  10.12 ? 93  VAL B C   1 
ATOM   741  O  O   . VAL A 1 95  ? -14.845 -2.289  13.168  1.00  9.90  ? 93  VAL B O   1 
ATOM   742  C  CB  . VAL A 1 95  ? -16.165 -5.141  13.698  1.00  9.24  ? 93  VAL B CB  1 
ATOM   743  C  CG1 . VAL A 1 95  ? -15.760 -5.629  12.276  1.00  10.64 ? 93  VAL B CG1 1 
ATOM   744  C  CG2 . VAL A 1 95  ? -16.720 -6.336  14.592  1.00  9.96  ? 93  VAL B CG2 1 
ATOM   745  N  N   . HIS A 1 96  ? -13.245 -3.864  12.717  1.00  8.54  ? 94  HIS B N   1 
ATOM   746  C  CA  . HIS A 1 96  ? -12.656 -3.065  11.644  1.00  8.78  ? 94  HIS B CA  1 
ATOM   747  C  C   . HIS A 1 96  ? -11.970 -3.972  10.650  1.00  8.57  ? 94  HIS B C   1 
ATOM   748  O  O   . HIS A 1 96  ? -12.045 -5.126  10.798  1.00  8.53  ? 94  HIS B O   1 
ATOM   749  C  CB  . HIS A 1 96  ? -11.698 -2.037  12.230  1.00  9.16  ? 94  HIS B CB  1 
ATOM   750  C  CG  . HIS A 1 96  ? -10.513 -2.627  12.877  1.00  9.10  ? 94  HIS B CG  1 
ATOM   751  N  ND1 . HIS A 1 96  ? -10.443 -2.858  14.264  1.00  10.86 ? 94  HIS B ND1 1 
ATOM   752  C  CD2 . HIS A 1 96  ? -9.347  -3.082  12.364  1.00  8.56  ? 94  HIS B CD2 1 
ATOM   753  C  CE1 . HIS A 1 96  ? -9.264  -3.409  14.559  1.00  10.12 ? 94  HIS B CE1 1 
ATOM   754  N  NE2 . HIS A 1 96  ? -8.582  -3.617  13.429  1.00  9.86  ? 94  HIS B NE2 1 
ATOM   755  N  N   . LEU A 1 97  ? -11.430 -3.413  9.588   1.00  7.32  ? 95  LEU B N   1 
ATOM   756  C  CA  . LEU A 1 97  ? -10.932 -4.181  8.445   1.00  7.47  ? 95  LEU B CA  1 
ATOM   757  C  C   . LEU A 1 97  ? -9.590  -3.681  7.980   1.00  7.87  ? 95  LEU B C   1 
ATOM   758  O  O   . LEU A 1 97  ? -9.359  -2.454  7.962   1.00  8.03  ? 95  LEU B O   1 
ATOM   759  C  CB  . LEU A 1 97  ? -12.000 -4.112  7.234   1.00  7.07  ? 95  LEU B CB  1 
ATOM   760  C  CG  . LEU A 1 97  ? -11.745 -5.029  6.023   1.00  7.47  ? 95  LEU B CG  1 
ATOM   761  C  CD1 . LEU A 1 97  ? -11.953 -6.504  6.435   1.00  7.08  ? 95  LEU B CD1 1 
ATOM   762  C  CD2 . LEU A 1 97  ? -12.712 -4.555  4.923   1.00  8.08  ? 95  LEU B CD2 1 
ATOM   763  N  N   . HIS A 1 98  ? -8.747  -4.612  7.507   1.00  6.53  ? 96  HIS B N   1 
ATOM   764  C  CA  . HIS A 1 98  ? -7.487  -4.238  6.851   1.00  7.25  ? 96  HIS B CA  1 
ATOM   765  C  C   . HIS A 1 98  ? -7.462  -4.767  5.406   1.00  7.69  ? 96  HIS B C   1 
ATOM   766  O  O   . HIS A 1 98  ? -7.955  -5.862  5.146   1.00  8.35  ? 96  HIS B O   1 
ATOM   767  C  CB  . HIS A 1 98  ? -6.248  -4.797  7.597   1.00  8.22  ? 96  HIS B CB  1 
ATOM   768  C  CG  . HIS A 1 98  ? -6.159  -4.292  9.061   1.00  8.81  ? 96  HIS B CG  1 
ATOM   769  N  ND1 . HIS A 1 98  ? -5.517  -3.154  9.404   1.00  9.30  ? 96  HIS B ND1 1 
ATOM   770  C  CD2 . HIS A 1 98  ? -6.691  -4.796  10.257  1.00  9.75  ? 96  HIS B CD2 1 
ATOM   771  C  CE1 . HIS A 1 98  ? -5.612  -2.948  10.733  1.00  10.07 ? 96  HIS B CE1 1 
ATOM   772  N  NE2 . HIS A 1 98  ? -6.332  -3.953  11.253  1.00  7.77  ? 96  HIS B NE2 1 
ATOM   773  N  N   . TRP A 1 99  ? -6.894  -3.963  4.477   1.00  7.20  ? 97  TRP B N   1 
ATOM   774  C  CA  . TRP A 1 99  ? -6.838  -4.340  3.076   1.00  7.52  ? 97  TRP B CA  1 
ATOM   775  C  C   . TRP A 1 99  ? -5.579  -3.741  2.491   1.00  7.74  ? 97  TRP B C   1 
ATOM   776  O  O   . TRP A 1 99  ? -4.702  -3.172  3.187   1.00  7.35  ? 97  TRP B O   1 
ATOM   777  C  CB  . TRP A 1 99  ? -8.057  -3.863  2.321   1.00  7.41  ? 97  TRP B CB  1 
ATOM   778  C  CG  . TRP A 1 99  ? -8.224  -2.335  2.435   1.00  6.54  ? 97  TRP B CG  1 
ATOM   779  C  CD1 . TRP A 1 99  ? -7.571  -1.366  1.658   1.00  7.27  ? 97  TRP B CD1 1 
ATOM   780  C  CD2 . TRP A 1 99  ? -9.070  -1.613  3.382   1.00  7.19  ? 97  TRP B CD2 1 
ATOM   781  N  NE1 . TRP A 1 99  ? -8.023  -0.103  1.994   1.00  6.32  ? 97  TRP B NE1 1 
ATOM   782  C  CE2 . TRP A 1 99  ? -8.874  -0.197  3.115   1.00  7.21  ? 97  TRP B CE2 1 
ATOM   783  C  CE3 . TRP A 1 99  ? -9.892  -2.010  4.507   1.00  7.19  ? 97  TRP B CE3 1 
ATOM   784  C  CZ2 . TRP A 1 99  ? -9.538  0.813   3.876   1.00  7.46  ? 97  TRP B CZ2 1 
ATOM   785  C  CZ3 . TRP A 1 99  ? -10.578 -1.006  5.250   1.00  7.92  ? 97  TRP B CZ3 1 
ATOM   786  C  CH2 . TRP A 1 99  ? -10.431 0.368   4.940   1.00  7.73  ? 97  TRP B CH2 1 
ATOM   787  N  N   . GLY A 1 100 ? -5.421  -4.016  1.191   1.00  8.70  ? 98  GLY B N   1 
ATOM   788  C  CA  . GLY A 1 100 ? -4.204  -3.543  0.483   1.00  9.05  ? 98  GLY B CA  1 
ATOM   789  C  C   . GLY A 1 100 ? -4.652  -2.873  -0.795  1.00  9.06  ? 98  GLY B C   1 
ATOM   790  O  O   . GLY A 1 100 ? -5.836  -2.836  -1.069  1.00  9.96  ? 98  GLY B O   1 
ATOM   791  N  N   . SER A 1 101 ? -3.665  -2.365  -1.583  1.00  9.77  ? 99  SER B N   1 
ATOM   792  C  CA  . SER A 1 101 ? -4.093  -1.755  -2.865  1.00  9.75  ? 99  SER B CA  1 
ATOM   793  C  C   . SER A 1 101 ? -4.467  -2.777  -3.964  1.00  10.92 ? 99  SER B C   1 
ATOM   794  O  O   . SER A 1 101 ? -5.153  -2.365  -4.943  1.00  13.54 ? 99  SER B O   1 
ATOM   795  C  CB  . SER A 1 101 ? -3.043  -0.711  -3.333  1.00  11.70 ? 99  SER B CB  1 
ATOM   796  O  OG  . SER A 1 101 ? -1.910  -1.432  -3.781  1.00  14.65 ? 99  SER B OG  1 
ATOM   797  N  N   . ALA A 1 102 ? -4.127  -4.031  -3.775  1.00  10.89 ? 100 ALA B N   1 
ATOM   798  C  CA  . ALA A 1 102 ? -4.352  -5.075  -4.779  1.00  12.28 ? 100 ALA B CA  1 
ATOM   799  C  C   . ALA A 1 102 ? -5.055  -6.216  -4.034  1.00  11.96 ? 100 ALA B C   1 
ATOM   800  O  O   . ALA A 1 102 ? -4.759  -6.470  -2.865  1.00  11.98 ? 100 ALA B O   1 
ATOM   801  C  CB  . ALA A 1 102 ? -3.028  -5.609  -5.286  1.00  14.02 ? 100 ALA B CB  1 
ATOM   802  N  N   . ASP A 1 103 ? -5.918  -6.937  -4.742  1.00  12.37 ? 101 ASP B N   1 
ATOM   803  C  CA  . ASP A 1 103 ? -6.680  -8.071  -4.120  1.00  14.13 ? 101 ASP B CA  1 
ATOM   804  C  C   . ASP A 1 103 ? -5.851  -9.271  -3.656  1.00  20.11 ? 101 ASP B C   1 
ATOM   805  O  O   . ASP A 1 103 ? -6.350  -10.074 -2.894  1.00  23.17 ? 101 ASP B O   1 
ATOM   806  C  CB  . ASP A 1 103 ? -7.811  -8.544  -5.078  1.00  15.11 ? 101 ASP B CB  1 
ATOM   807  C  CG  . ASP A 1 103 ? -8.961  -7.571  -5.204  1.00  17.50 ? 101 ASP B CG  1 
ATOM   808  O  OD1 . ASP A 1 103 ? -8.988  -6.495  -4.597  1.00  18.02 ? 101 ASP B OD1 1 
ATOM   809  O  OD2 . ASP A 1 103 ? -9.856  -7.811  -6.050  1.00  22.58 ? 101 ASP B OD2 1 
ATOM   810  N  N   . ASP A 1 104 ? -4.615  -9.398  -4.116  1.00  20.20 ? 102 ASP B N   1 
ATOM   811  C  CA  . ASP A 1 104 ? -3.807  -10.578 -3.825  1.00  22.62 ? 102 ASP B CA  1 
ATOM   812  C  C   . ASP A 1 104 ? -2.946  -10.331 -2.574  1.00  20.75 ? 102 ASP B C   1 
ATOM   813  O  O   . ASP A 1 104 ? -2.196  -11.243 -2.227  1.00  19.16 ? 102 ASP B O   1 
ATOM   814  C  CB  . ASP A 1 104 ? -2.854  -10.736 -5.015  1.00  25.40 ? 102 ASP B CB  1 
ATOM   815  C  CG  . ASP A 1 104 ? -2.467  -9.415  -5.569  1.00  25.97 ? 102 ASP B CG  1 
ATOM   816  O  OD1 . ASP A 1 104 ? -3.062  -8.890  -6.631  1.00  34.91 ? 102 ASP B OD1 1 
ATOM   817  O  OD2 . ASP A 1 104 ? -1.568  -8.792  -4.938  1.00  36.62 ? 102 ASP B OD2 1 
ATOM   818  N  N   . HIS A 1 105 ? -2.955  -9.099  -1.958  1.00  16.57 ? 103 HIS B N   1 
ATOM   819  C  CA  . HIS A 1 105 ? -2.072  -8.844  -0.857  1.00  15.34 ? 103 HIS B CA  1 
ATOM   820  C  C   . HIS A 1 105 ? -2.655  -7.796  0.075   1.00  13.02 ? 103 HIS B C   1 
ATOM   821  O  O   . HIS A 1 105 ? -2.196  -6.620  0.134   1.00  14.30 ? 103 HIS B O   1 
ATOM   822  C  CB  . HIS A 1 105 ? -0.705  -8.404  -1.473  1.00  20.54 ? 103 HIS B CB  1 
ATOM   823  C  CG  . HIS A 1 105 ? 0.436   -8.566  -0.581  1.00  29.02 ? 103 HIS B CG  1 
ATOM   824  N  ND1 . HIS A 1 105 ? 1.092   -9.759  -0.438  1.00  34.42 ? 103 HIS B ND1 1 
ATOM   825  C  CD2 . HIS A 1 105 ? 1.092   -7.651  0.246   1.00  31.88 ? 103 HIS B CD2 1 
ATOM   826  C  CE1 . HIS A 1 105 ? 2.088   -9.606  0.464   1.00  33.23 ? 103 HIS B CE1 1 
ATOM   827  N  NE2 . HIS A 1 105 ? 2.097   -8.333  0.875   1.00  33.81 ? 103 HIS B NE2 1 
ATOM   828  N  N   . GLY A 1 106 ? -3.651  -8.198  0.882   1.00  10.82 ? 104 GLY B N   1 
ATOM   829  C  CA  . GLY A 1 106 ? -4.360  -7.253  1.759   1.00  9.49  ? 104 GLY B CA  1 
ATOM   830  C  C   . GLY A 1 106 ? -4.462  -7.608  3.234   1.00  10.65 ? 104 GLY B C   1 
ATOM   831  O  O   . GLY A 1 106 ? -4.711  -6.741  4.083   1.00  11.39 ? 104 GLY B O   1 
ATOM   832  N  N   . SER A 1 107 ? -4.210  -8.859  3.557   1.00  9.42  ? 105 SER B N   1 
ATOM   833  C  CA  . SER A 1 107 ? -4.342  -9.326  4.952   1.00  9.37  ? 105 SER B CA  1 
ATOM   834  C  C   . SER A 1 107 ? -3.101  -8.970  5.786   1.00  8.96  ? 105 SER B C   1 
ATOM   835  O  O   . SER A 1 107 ? -2.035  -8.572  5.248   1.00  9.11  ? 105 SER B O   1 
ATOM   836  C  CB  . SER A 1 107 ? -4.664  -10.819 4.974   1.00  8.95  ? 105 SER B CB  1 
ATOM   837  O  OG  . SER A 1 107 ? -3.557  -11.607 4.540   1.00  8.68  ? 105 SER B OG  1 
ATOM   838  N  N   . GLU A 1 108 ? -3.268  -9.006  7.120   1.00  8.56  ? 106 GLU B N   1 
ATOM   839  C  CA  . GLU A 1 108 ? -2.127  -8.747  8.026   1.00  8.74  ? 106 GLU B CA  1 
ATOM   840  C  C   . GLU A 1 108 ? -1.395  -10.045 8.369   1.00  9.36  ? 106 GLU B C   1 
ATOM   841  O  O   . GLU A 1 108 ? -0.198  -10.196 8.120   1.00  9.29  ? 106 GLU B O   1 
ATOM   842  C  CB  . GLU A 1 108 ? -2.694  -8.086  9.308   1.00  8.65  ? 106 GLU B CB  1 
ATOM   843  C  CG  . GLU A 1 108 ? -3.232  -6.657  8.905   1.00  10.69 ? 106 GLU B CG  1 
ATOM   844  C  CD  . GLU A 1 108 ? -3.132  -5.613  10.032  1.00  11.22 ? 106 GLU B CD  1 
ATOM   845  O  OE1 . GLU A 1 108 ? -3.553  -5.913  11.154  1.00  11.05 ? 106 GLU B OE1 1 
ATOM   846  O  OE2 . GLU A 1 108 ? -2.555  -4.529  9.786   1.00  10.93 ? 106 GLU B OE2 1 
ATOM   847  N  N   . HIS A 1 109 ? -2.104  -11.031 8.910   1.00  8.28  ? 107 HIS B N   1 
ATOM   848  C  CA  . HIS A 1 109 ? -1.555  -12.394 9.010   1.00  8.71  ? 107 HIS B CA  1 
ATOM   849  C  C   . HIS A 1 109 ? -1.435  -13.052 7.641   1.00  7.71  ? 107 HIS B C   1 
ATOM   850  O  O   . HIS A 1 109 ? -2.212  -12.710 6.735   1.00  8.04  ? 107 HIS B O   1 
ATOM   851  C  CB  . HIS A 1 109 ? -2.416  -13.270 9.926   1.00  8.09  ? 107 HIS B CB  1 
ATOM   852  C  CG  . HIS A 1 109 ? -2.423  -12.719 11.333  1.00  8.21  ? 107 HIS B CG  1 
ATOM   853  N  ND1 . HIS A 1 109 ? -3.338  -11.790 11.776  1.00  7.81  ? 107 HIS B ND1 1 
ATOM   854  C  CD2 . HIS A 1 109 ? -1.576  -12.999 12.390  1.00  8.14  ? 107 HIS B CD2 1 
ATOM   855  C  CE1 . HIS A 1 109 ? -3.025  -11.469 13.080  1.00  8.40  ? 107 HIS B CE1 1 
ATOM   856  N  NE2 . HIS A 1 109 ? -1.934  -12.140 13.421  1.00  8.12  ? 107 HIS B NE2 1 
ATOM   857  N  N   . ILE A 1 110 ? -0.397  -13.881 7.494   1.00  8.72  ? 108 ILE B N   1 
ATOM   858  C  CA  . ILE A 1 110 ? -0.059  -14.523 6.188   1.00  9.22  ? 108 ILE B CA  1 
ATOM   859  C  C   . ILE A 1 110 ? 0.110   -16.020 6.529   1.00  9.62  ? 108 ILE B C   1 
ATOM   860  O  O   . ILE A 1 110 ? 0.655   -16.323 7.589   1.00  11.46 ? 108 ILE B O   1 
ATOM   861  C  CB  . ILE A 1 110 ? 1.248   -13.900 5.609   1.00  11.78 ? 108 ILE B CB  1 
ATOM   862  C  CG1 . ILE A 1 110 ? 1.145   -12.315 5.567   1.00  15.18 ? 108 ILE B CG1 1 
ATOM   863  C  CG2 . ILE A 1 110 ? 1.499   -14.499 4.169   1.00  9.61  ? 108 ILE B CG2 1 
ATOM   864  C  CD1 . ILE A 1 110 ? 2.456   -11.731 5.121   1.00  18.97 ? 108 ILE B CD1 1 
ATOM   865  N  N   . VAL A 1 111 ? -0.428  -16.936 5.713   1.00  9.07  ? 109 VAL B N   1 
ATOM   866  C  CA  . VAL A 1 111 ? -0.406  -18.363 6.076   1.00  9.20  ? 109 VAL B CA  1 
ATOM   867  C  C   . VAL A 1 111 ? 0.419   -19.120 5.012   1.00  10.11 ? 109 VAL B C   1 
ATOM   868  O  O   . VAL A 1 111 ? 0.003   -19.179 3.853   1.00  10.75 ? 109 VAL B O   1 
ATOM   869  C  CB  . VAL A 1 111 ? -1.851  -18.950 6.032   1.00  9.59  ? 109 VAL B CB  1 
ATOM   870  C  CG1 . VAL A 1 111 ? -1.788  -20.442 6.390   1.00  9.98  ? 109 VAL B CG1 1 
ATOM   871  C  CG2 . VAL A 1 111 ? -2.766  -18.213 7.019   1.00  10.40 ? 109 VAL B CG2 1 
ATOM   872  N  N   . ASP A 1 112 ? 1.626   -19.538 5.403   1.00  10.47 ? 110 ASP B N   1 
ATOM   873  C  CA  . ASP A 1 112 ? 2.564   -20.182 4.480   1.00  10.99 ? 110 ASP B CA  1 
ATOM   874  C  C   . ASP A 1 112 ? 2.744   -19.344 3.223   1.00  11.10 ? 110 ASP B C   1 
ATOM   875  O  O   . ASP A 1 112 ? 2.747   -19.842 2.085   1.00  11.74 ? 110 ASP B O   1 
ATOM   876  C  CB  . ASP A 1 112 ? 2.114   -21.638 4.215   1.00  13.03 ? 110 ASP B CB  1 
ATOM   877  C  CG  . ASP A 1 112 ? 2.322   -22.526 5.436   1.00  14.47 ? 110 ASP B CG  1 
ATOM   878  O  OD1 . ASP A 1 112 ? 3.456   -22.535 5.953   1.00  15.31 ? 110 ASP B OD1 1 
ATOM   879  O  OD2 . ASP A 1 112 ? 1.366   -23.254 5.800   1.00  19.64 ? 110 ASP B OD2 1 
ATOM   880  N  N   . GLY A 1 113 ? 2.876   -18.041 3.426   1.00  9.58  ? 111 GLY B N   1 
ATOM   881  C  CA  . GLY A 1 113 ? 3.104   -17.130 2.280   1.00  11.15 ? 111 GLY B CA  1 
ATOM   882  C  C   . GLY A 1 113 ? 1.867   -16.635 1.585   1.00  11.23 ? 111 GLY B C   1 
ATOM   883  O  O   . GLY A 1 113 ? 1.988   -15.740 0.702   1.00  12.04 ? 111 GLY B O   1 
ATOM   884  N  N   . VAL A 1 114 ? 0.657   -17.135 1.951   1.00  11.90 ? 112 VAL B N   1 
ATOM   885  C  CA  . VAL A 1 114 ? -0.591  -16.755 1.279   1.00  13.20 ? 112 VAL B CA  1 
ATOM   886  C  C   . VAL A 1 114 ? -1.118  -15.525 2.024   1.00  13.77 ? 112 VAL B C   1 
ATOM   887  O  O   . VAL A 1 114 ? -1.376  -15.600 3.235   1.00  12.72 ? 112 VAL B O   1 
ATOM   888  C  CB  . VAL A 1 114 ? -1.606  -17.915 1.230   1.00  15.12 ? 112 VAL B CB  1 
ATOM   889  C  CG1 . VAL A 1 114 ? -2.947  -17.428 0.684   1.00  16.61 ? 112 VAL B CG1 1 
ATOM   890  C  CG2 . VAL A 1 114 ? -0.970  -19.044 0.364   1.00  16.61 ? 112 VAL B CG2 1 
ATOM   891  N  N   A SER A 1 115 ? -1.172  -14.406 1.324   0.50  11.74 ? 113 SER B N   1 
ATOM   892  N  N   B SER A 1 115 ? -1.175  -14.375 1.330   0.50  12.11 ? 113 SER B N   1 
ATOM   893  C  CA  A SER A 1 115 ? -1.929  -13.271 1.849   0.50  11.71 ? 113 SER B CA  1 
ATOM   894  C  CA  B SER A 1 115 ? -1.857  -13.127 1.857   0.50  12.14 ? 113 SER B CA  1 
ATOM   895  C  C   A SER A 1 115 ? -3.322  -13.454 1.316   0.50  10.46 ? 113 SER B C   1 
ATOM   896  C  C   B SER A 1 115 ? -3.236  -13.000 1.213   0.50  11.22 ? 113 SER B C   1 
ATOM   897  O  O   A SER A 1 115 ? -3.539  -14.013 0.215   0.50  9.38  ? 113 SER B O   1 
ATOM   898  O  O   B SER A 1 115 ? -3.364  -12.958 -0.054  0.50  9.70  ? 113 SER B O   1 
ATOM   899  C  CB  A SER A 1 115 ? -1.335  -11.968 1.327   0.50  12.81 ? 113 SER B CB  1 
ATOM   900  C  CB  B SER A 1 115 ? -1.009  -11.847 1.590   0.50  13.53 ? 113 SER B CB  1 
ATOM   901  O  OG  A SER A 1 115 ? -0.096  -11.688 1.956   0.50  12.22 ? 113 SER B OG  1 
ATOM   902  O  OG  B SER A 1 115 ? -1.719  -10.608 1.852   0.50  13.52 ? 113 SER B OG  1 
ATOM   903  N  N   . TYR A 1 116 ? -4.292  -12.925 2.063   1.00  10.18 ? 114 TYR B N   1 
ATOM   904  C  CA  . TYR A 1 116 ? -5.640  -12.819 1.602   1.00  10.81 ? 114 TYR B CA  1 
ATOM   905  C  C   . TYR A 1 116 ? -6.029  -11.430 1.108   1.00  8.76  ? 114 TYR B C   1 
ATOM   906  O  O   . TYR A 1 116 ? -5.232  -10.502 1.256   1.00  10.16 ? 114 TYR B O   1 
ATOM   907  C  CB  . TYR A 1 116 ? -6.606  -13.336 2.725   1.00  10.87 ? 114 TYR B CB  1 
ATOM   908  C  CG  . TYR A 1 116 ? -6.348  -14.807 2.944   1.00  11.58 ? 114 TYR B CG  1 
ATOM   909  C  CD1 . TYR A 1 116 ? -7.100  -15.818 2.233   1.00  12.84 ? 114 TYR B CD1 1 
ATOM   910  C  CD2 . TYR A 1 116 ? -5.400  -15.215 3.889   1.00  11.81 ? 114 TYR B CD2 1 
ATOM   911  C  CE1 . TYR A 1 116 ? -6.825  -17.180 2.479   1.00  12.92 ? 114 TYR B CE1 1 
ATOM   912  C  CE2 . TYR A 1 116 ? -5.146  -16.569 4.120   1.00  11.99 ? 114 TYR B CE2 1 
ATOM   913  C  CZ  . TYR A 1 116 ? -5.864  -17.498 3.377   1.00  14.26 ? 114 TYR B CZ  1 
ATOM   914  O  OH  . TYR A 1 116 ? -5.656  -18.900 3.532   1.00  18.09 ? 114 TYR B OH  1 
ATOM   915  N  N   . ALA A 1 117 ? -7.265  -11.248 0.563   1.00  8.42  ? 115 ALA B N   1 
ATOM   916  C  CA  . ALA A 1 117 ? -7.597  -9.936  0.018   1.00  8.06  ? 115 ALA B CA  1 
ATOM   917  C  C   . ALA A 1 117 ? -7.775  -8.938  1.160   1.00  8.33  ? 115 ALA B C   1 
ATOM   918  O  O   . ALA A 1 117 ? -7.564  -7.780  0.946   1.00  9.37  ? 115 ALA B O   1 
ATOM   919  C  CB  . ALA A 1 117 ? -8.881  -9.968  -0.816  1.00  8.53  ? 115 ALA B CB  1 
ATOM   920  N  N   . ALA A 1 118 ? -8.261  -9.376  2.342   1.00  7.58  ? 116 ALA B N   1 
ATOM   921  C  CA  . ALA A 1 118 ? -8.422  -8.391  3.433   1.00  7.10  ? 116 ALA B CA  1 
ATOM   922  C  C   . ALA A 1 118 ? -8.487  -9.198  4.715   1.00  7.64  ? 116 ALA B C   1 
ATOM   923  O  O   . ALA A 1 118 ? -8.485  -10.449 4.648   1.00  7.28  ? 116 ALA B O   1 
ATOM   924  C  CB  . ALA A 1 118 ? -9.755  -7.590  3.212   1.00  7.80  ? 116 ALA B CB  1 
ATOM   925  N  N   . GLU A 1 119 ? -8.622  -8.531  5.875   1.00  6.95  ? 117 GLU B N   1 
ATOM   926  C  CA  . GLU A 1 119 ? -8.689  -9.291  7.123   1.00  7.66  ? 117 GLU B CA  1 
ATOM   927  C  C   . GLU A 1 119 ? -9.523  -8.441  8.096   1.00  7.46  ? 117 GLU B C   1 
ATOM   928  O  O   . GLU A 1 119 ? -9.191  -7.259  8.395   1.00  7.55  ? 117 GLU B O   1 
ATOM   929  C  CB  . GLU A 1 119 ? -7.233  -9.569  7.658   1.00  7.63  ? 117 GLU B CB  1 
ATOM   930  C  CG  . GLU A 1 119 ? -7.193  -10.248 8.999   1.00  8.16  ? 117 GLU B CG  1 
ATOM   931  C  CD  . GLU A 1 119 ? -5.785  -10.622 9.432   1.00  8.53  ? 117 GLU B CD  1 
ATOM   932  O  OE1 . GLU A 1 119 ? -4.909  -10.795 8.545   1.00  7.76  ? 117 GLU B OE1 1 
ATOM   933  O  OE2 . GLU A 1 119 ? -5.550  -10.768 10.677  1.00  9.63  ? 117 GLU B OE2 1 
ATOM   934  N  N   . LEU A 1 120 ? -10.571 -9.098  8.629   1.00  6.88  ? 118 LEU B N   1 
ATOM   935  C  CA  . LEU A 1 120 ? -11.472 -8.427  9.548   1.00  7.07  ? 118 LEU B CA  1 
ATOM   936  C  C   . LEU A 1 120 ? -10.952 -8.705  10.973  1.00  7.84  ? 118 LEU B C   1 
ATOM   937  O  O   . LEU A 1 120 ? -10.586 -9.845  11.311  1.00  7.47  ? 118 LEU B O   1 
ATOM   938  C  CB  . LEU A 1 120 ? -12.857 -9.038  9.402   1.00  8.58  ? 118 LEU B CB  1 
ATOM   939  C  CG  . LEU A 1 120 ? -13.983 -8.338  10.190  1.00  9.69  ? 118 LEU B CG  1 
ATOM   940  C  CD1 . LEU A 1 120 ? -14.539 -7.222  9.327   1.00  10.58 ? 118 LEU B CD1 1 
ATOM   941  C  CD2 . LEU A 1 120 ? -15.132 -9.269  10.483  1.00  12.65 ? 118 LEU B CD2 1 
ATOM   942  N  N   . HIS A 1 121 ? -10.981 -7.659  11.826  1.00  6.91  ? 119 HIS B N   1 
ATOM   943  C  CA  . HIS A 1 121 ? -10.646 -7.858  13.261  1.00  8.13  ? 119 HIS B CA  1 
ATOM   944  C  C   . HIS A 1 121 ? -11.814 -7.541  14.145  1.00  8.29  ? 119 HIS B C   1 
ATOM   945  O  O   . HIS A 1 121 ? -12.444 -6.517  14.012  1.00  8.89  ? 119 HIS B O   1 
ATOM   946  C  CB  . HIS A 1 121 ? -9.453  -6.971  13.657  1.00  7.30  ? 119 HIS B CB  1 
ATOM   947  C  CG  . HIS A 1 121 ? -8.122  -7.430  13.005  1.00  7.03  ? 119 HIS B CG  1 
ATOM   948  N  ND1 . HIS A 1 121 ? -7.049  -6.591  12.835  1.00  8.25  ? 119 HIS B ND1 1 
ATOM   949  C  CD2 . HIS A 1 121 ? -7.784  -8.628  12.435  1.00  7.44  ? 119 HIS B CD2 1 
ATOM   950  C  CE1 . HIS A 1 121 ? -6.024  -7.317  12.273  1.00  7.23  ? 119 HIS B CE1 1 
ATOM   951  N  NE2 . HIS A 1 121 ? -6.495  -8.545  12.023  1.00  7.48  ? 119 HIS B NE2 1 
ATOM   952  N  N   . VAL A 1 122 ? -12.085 -8.454  15.071  1.00  6.99  ? 120 VAL B N   1 
ATOM   953  C  CA  . VAL A 1 122 ? -13.193 -8.330  16.013  1.00  7.25  ? 120 VAL B CA  1 
ATOM   954  C  C   . VAL A 1 122 ? -12.525 -8.223  17.400  1.00  7.93  ? 120 VAL B C   1 
ATOM   955  O  O   . VAL A 1 122 ? -11.887 -9.187  17.901  1.00  8.29  ? 120 VAL B O   1 
ATOM   956  C  CB  . VAL A 1 122 ? -14.116 -9.565  16.018  1.00  7.53  ? 120 VAL B CB  1 
ATOM   957  C  CG1 . VAL A 1 122 ? -15.346 -9.231  16.890  1.00  8.37  ? 120 VAL B CG1 1 
ATOM   958  C  CG2 . VAL A 1 122 ? -14.578 -9.958  14.539  1.00  8.28  ? 120 VAL B CG2 1 
ATOM   959  N  N   . VAL A 1 123 ? -12.660 -7.037  18.030  1.00  7.50  ? 121 VAL B N   1 
ATOM   960  C  CA  . VAL A 1 123 ? -11.843 -6.735  19.233  1.00  7.59  ? 121 VAL B CA  1 
ATOM   961  C  C   . VAL A 1 123 ? -12.679 -6.829  20.499  1.00  7.34  ? 121 VAL B C   1 
ATOM   962  O  O   . VAL A 1 123 ? -13.799 -6.335  20.528  1.00  8.53  ? 121 VAL B O   1 
ATOM   963  C  CB  . VAL A 1 123 ? -11.337 -5.280  19.131  1.00  7.81  ? 121 VAL B CB  1 
ATOM   964  C  CG1 . VAL A 1 123 ? -10.528 -4.904  20.365  1.00  8.50  ? 121 VAL B CG1 1 
ATOM   965  C  CG2 . VAL A 1 123 ? -10.508 -5.021  17.851  1.00  8.52  ? 121 VAL B CG2 1 
ATOM   966  N  N   . HIS A 1 124 ? -12.137 -7.533  21.502  1.00  8.22  ? 122 HIS B N   1 
ATOM   967  C  CA  . HIS A 1 124 ? -12.935 -7.800  22.716  1.00  7.98  ? 122 HIS B CA  1 
ATOM   968  C  C   . HIS A 1 124 ? -12.055 -7.500  23.917  1.00  7.44  ? 122 HIS B C   1 
ATOM   969  O  O   . HIS A 1 124 ? -10.806 -7.606  23.846  1.00  8.87  ? 122 HIS B O   1 
ATOM   970  C  CB  . HIS A 1 124 ? -13.294 -9.289  22.819  1.00  8.28  ? 122 HIS B CB  1 
ATOM   971  C  CG  . HIS A 1 124 ? -13.915 -9.891  21.584  1.00  8.51  ? 122 HIS B CG  1 
ATOM   972  N  ND1 . HIS A 1 124 ? -13.173 -10.230 20.498  1.00  8.89  ? 122 HIS B ND1 1 
ATOM   973  C  CD2 . HIS A 1 124 ? -15.207 -10.375 21.331  1.00  8.97  ? 122 HIS B CD2 1 
ATOM   974  C  CE1 . HIS A 1 124 ? -13.929 -10.836 19.596  1.00  8.35  ? 122 HIS B CE1 1 
ATOM   975  N  NE2 . HIS A 1 124 ? -15.188 -10.958 20.118  1.00  8.19  ? 122 HIS B NE2 1 
ATOM   976  N  N   . TRP A 1 125 ? -12.667 -7.258  25.070  1.00  8.80  ? 123 TRP B N   1 
ATOM   977  C  CA  . TRP A 1 125 ? -11.857 -7.005  26.270  1.00  9.13  ? 123 TRP B CA  1 
ATOM   978  C  C   . TRP A 1 125 ? -12.307 -7.793  27.508  1.00  8.98  ? 123 TRP B C   1 
ATOM   979  O  O   . TRP A 1 125 ? -13.509 -8.023  27.692  1.00  9.52  ? 123 TRP B O   1 
ATOM   980  C  CB  . TRP A 1 125 ? -11.741 -5.486  26.578  1.00  9.36  ? 123 TRP B CB  1 
ATOM   981  C  CG  . TRP A 1 125 ? -13.070 -4.827  26.819  1.00  9.91  ? 123 TRP B CG  1 
ATOM   982  C  CD1 . TRP A 1 125 ? -13.950 -4.284  25.857  1.00  10.89 ? 123 TRP B CD1 1 
ATOM   983  C  CD2 . TRP A 1 125 ? -13.662 -4.500  28.115  1.00  10.40 ? 123 TRP B CD2 1 
ATOM   984  N  NE1 . TRP A 1 125 ? -15.005 -3.662  26.461  1.00  10.66 ? 123 TRP B NE1 1 
ATOM   985  C  CE2 . TRP A 1 125 ? -14.872 -3.776  27.849  1.00  11.17 ? 123 TRP B CE2 1 
ATOM   986  C  CE3 . TRP A 1 125 ? -13.256 -4.700  29.431  1.00  12.30 ? 123 TRP B CE3 1 
ATOM   987  C  CZ2 . TRP A 1 125 ? -15.738 -3.338  28.890  1.00  11.55 ? 123 TRP B CZ2 1 
ATOM   988  C  CZ3 . TRP A 1 125 ? -14.059 -4.190  30.483  1.00  11.82 ? 123 TRP B CZ3 1 
ATOM   989  C  CH2 . TRP A 1 125 ? -15.274 -3.535  30.227  1.00  12.02 ? 123 TRP B CH2 1 
ATOM   990  N  N   . ASN A 1 126 ? -11.356 -8.088  28.401  1.00  11.26 ? 124 ASN B N   1 
ATOM   991  C  CA  . ASN A 1 126 ? -11.597 -9.010  29.543  1.00  10.75 ? 124 ASN B CA  1 
ATOM   992  C  C   . ASN A 1 126 ? -12.288 -8.195  30.653  1.00  10.98 ? 124 ASN B C   1 
ATOM   993  O  O   . ASN A 1 126 ? -11.627 -7.588  31.473  1.00  10.64 ? 124 ASN B O   1 
ATOM   994  C  CB  . ASN A 1 126 ? -10.221 -9.478  30.025  1.00  10.84 ? 124 ASN B CB  1 
ATOM   995  C  CG  . ASN A 1 126 ? -10.335 -10.563 31.105  1.00  12.49 ? 124 ASN B CG  1 
ATOM   996  O  OD1 . ASN A 1 126 ? -11.412 -10.718 31.721  1.00  12.98 ? 124 ASN B OD1 1 
ATOM   997  N  ND2 . ASN A 1 126 ? -9.295  -11.309 31.304  1.00  13.79 ? 124 ASN B ND2 1 
ATOM   998  N  N   . SER A 1 127 ? -13.602 -8.274  30.730  1.00  11.03 ? 125 SER B N   1 
ATOM   999  C  CA  . SER A 1 127 ? -14.364 -7.546  31.780  1.00  11.66 ? 125 SER B CA  1 
ATOM   1000 C  C   . SER A 1 127 ? -14.472 -8.411  33.033  1.00  12.85 ? 125 SER B C   1 
ATOM   1001 O  O   . SER A 1 127 ? -14.960 -7.892  34.050  1.00  13.01 ? 125 SER B O   1 
ATOM   1002 C  CB  . SER A 1 127 ? -15.765 -7.170  31.255  1.00  11.61 ? 125 SER B CB  1 
ATOM   1003 O  OG  . SER A 1 127 ? -16.509 -8.348  30.911  1.00  14.38 ? 125 SER B OG  1 
ATOM   1004 N  N   . ASP A 1 128 ? -13.972 -9.665  32.996  1.00  12.09 ? 126 ASP B N   1 
ATOM   1005 C  CA  . ASP A 1 128 ? -13.911 -10.477 34.246  1.00  14.13 ? 126 ASP B CA  1 
ATOM   1006 C  C   . ASP A 1 128 ? -12.740 -10.024 35.154  1.00  15.23 ? 126 ASP B C   1 
ATOM   1007 O  O   . ASP A 1 128 ? -12.760 -10.272 36.366  1.00  17.53 ? 126 ASP B O   1 
ATOM   1008 C  CB  . ASP A 1 128 ? -13.734 -11.957 33.953  1.00  14.07 ? 126 ASP B CB  1 
ATOM   1009 C  CG  . ASP A 1 128 ? -15.012 -12.636 33.472  1.00  14.01 ? 126 ASP B CG  1 
ATOM   1010 O  OD1 . ASP A 1 128 ? -14.899 -13.803 33.031  1.00  15.31 ? 126 ASP B OD1 1 
ATOM   1011 O  OD2 . ASP A 1 128 ? -16.109 -12.030 33.529  1.00  20.28 ? 126 ASP B OD2 1 
ATOM   1012 N  N   . LYS A 1 129 ? -11.731 -9.363  34.599  1.00  13.53 ? 127 LYS B N   1 
ATOM   1013 C  CA  . LYS A 1 129 ? -10.596 -8.938  35.408  1.00  13.89 ? 127 LYS B CA  1 
ATOM   1014 C  C   . LYS A 1 129 ? -10.447 -7.421  35.408  1.00  13.73 ? 127 LYS B C   1 
ATOM   1015 O  O   . LYS A 1 129 ? -9.742  -6.902  36.271  1.00  13.23 ? 127 LYS B O   1 
ATOM   1016 C  CB  . LYS A 1 129 ? -9.297  -9.560  34.904  1.00  15.49 ? 127 LYS B CB  1 
ATOM   1017 C  CG  . LYS A 1 129 ? -9.124  -11.040 35.218  1.00  20.77 ? 127 LYS B CG  1 
ATOM   1018 C  CD  . LYS A 1 129 ? -7.635  -11.472 35.062  1.00  22.06 ? 127 LYS B CD  1 
ATOM   1019 C  CE  . LYS A 1 129 ? -6.550  -10.587 35.730  1.00  26.39 ? 127 LYS B CE  1 
ATOM   1020 N  NZ  . LYS A 1 129 ? -5.100  -10.920 35.448  1.00  23.92 ? 127 LYS B NZ  1 
ATOM   1021 N  N   . TYR A 1 130 ? -10.953 -6.729  34.386  1.00  13.28 ? 128 TYR B N   1 
ATOM   1022 C  CA  . TYR A 1 130 ? -10.715 -5.262  34.217  1.00  12.02 ? 128 TYR B CA  1 
ATOM   1023 C  C   . TYR A 1 130 ? -12.051 -4.475  34.167  1.00  11.75 ? 128 TYR B C   1 
ATOM   1024 O  O   . TYR A 1 130 ? -13.093 -4.979  33.677  1.00  11.54 ? 128 TYR B O   1 
ATOM   1025 C  CB  . TYR A 1 130 ? -9.860  -4.996  32.941  1.00  12.17 ? 128 TYR B CB  1 
ATOM   1026 C  CG  . TYR A 1 130 ? -8.568  -5.732  33.043  1.00  12.49 ? 128 TYR B CG  1 
ATOM   1027 C  CD1 . TYR A 1 130 ? -7.609  -5.393  34.044  1.00  12.94 ? 128 TYR B CD1 1 
ATOM   1028 C  CD2 . TYR A 1 130 ? -8.328  -6.886  32.244  1.00  11.76 ? 128 TYR B CD2 1 
ATOM   1029 C  CE1 . TYR A 1 130 ? -6.477  -6.206  34.247  1.00  15.25 ? 128 TYR B CE1 1 
ATOM   1030 C  CE2 . TYR A 1 130 ? -7.166  -7.659  32.409  1.00  13.46 ? 128 TYR B CE2 1 
ATOM   1031 C  CZ  . TYR A 1 130 ? -6.234  -7.285  33.393  1.00  15.40 ? 128 TYR B CZ  1 
ATOM   1032 O  OH  . TYR A 1 130 ? -5.117  -8.042  33.581  1.00  16.25 ? 128 TYR B OH  1 
ATOM   1033 N  N   . PRO A 1 131 ? -12.036 -3.232  34.663  1.00  11.95 ? 129 PRO B N   1 
ATOM   1034 C  CA  . PRO A 1 131 ? -13.301 -2.509  34.707  1.00  11.71 ? 129 PRO B CA  1 
ATOM   1035 C  C   . PRO A 1 131 ? -13.676 -1.820  33.377  1.00  13.14 ? 129 PRO B C   1 
ATOM   1036 O  O   . PRO A 1 131 ? -14.803 -1.345  33.244  1.00  13.05 ? 129 PRO B O   1 
ATOM   1037 C  CB  . PRO A 1 131 ? -13.036 -1.466  35.804  1.00  12.76 ? 129 PRO B CB  1 
ATOM   1038 C  CG  . PRO A 1 131 ? -11.604 -1.123  35.656  1.00  12.34 ? 129 PRO B CG  1 
ATOM   1039 C  CD  . PRO A 1 131 ? -10.980 -2.539  35.430  1.00  11.37 ? 129 PRO B CD  1 
ATOM   1040 N  N   . SER A 1 132 ? -12.735 -1.765  32.436  1.00  13.52 ? 130 SER B N   1 
ATOM   1041 C  CA  . SER A 1 132 ? -12.992 -0.984  31.179  1.00  13.56 ? 130 SER B CA  1 
ATOM   1042 C  C   . SER A 1 132 ? -11.986 -1.480  30.105  1.00  11.76 ? 130 SER B C   1 
ATOM   1043 O  O   . SER A 1 132 ? -10.919 -2.041  30.419  1.00  12.21 ? 130 SER B O   1 
ATOM   1044 C  CB  . SER A 1 132 ? -12.679 0.515   31.397  1.00  13.79 ? 130 SER B CB  1 
ATOM   1045 O  OG  . SER A 1 132 ? -11.282 0.679   31.683  1.00  14.76 ? 130 SER B OG  1 
ATOM   1046 N  N   . PHE A 1 133 ? -12.387 -1.259  28.864  1.00  12.23 ? 131 PHE B N   1 
ATOM   1047 C  CA  . PHE A 1 133 ? -11.495 -1.473  27.732  1.00  14.26 ? 131 PHE B CA  1 
ATOM   1048 C  C   . PHE A 1 133 ? -10.182 -0.813  27.932  1.00  14.02 ? 131 PHE B C   1 
ATOM   1049 O  O   . PHE A 1 133 ? -9.133  -1.434  27.666  1.00  13.60 ? 131 PHE B O   1 
ATOM   1050 C  CB  . PHE A 1 133 ? -12.193 -0.969  26.463  1.00  13.86 ? 131 PHE B CB  1 
ATOM   1051 C  CG  . PHE A 1 133 ? -11.310 -1.019  25.239  1.00  17.14 ? 131 PHE B CG  1 
ATOM   1052 C  CD1 . PHE A 1 133 ? -11.045 -2.229  24.605  1.00  16.42 ? 131 PHE B CD1 1 
ATOM   1053 C  CD2 . PHE A 1 133 ? -10.729 0.142   24.767  1.00  18.77 ? 131 PHE B CD2 1 
ATOM   1054 C  CE1 . PHE A 1 133 ? -10.173 -2.259  23.507  1.00  18.00 ? 131 PHE B CE1 1 
ATOM   1055 C  CE2 . PHE A 1 133 ? -9.846  0.111   23.684  1.00  18.45 ? 131 PHE B CE2 1 
ATOM   1056 C  CZ  . PHE A 1 133 ? -9.609  -1.093  23.051  1.00  17.95 ? 131 PHE B CZ  1 
ATOM   1057 N  N   A VAL A 1 134 ? -10.232 0.421   28.422  0.50  15.11 ? 132 VAL B N   1 
ATOM   1058 N  N   B VAL A 1 134 ? -10.119 0.453   28.374  0.50  14.59 ? 132 VAL B N   1 
ATOM   1059 C  CA  A VAL A 1 134 ? -9.025  1.210   28.559  0.50  15.92 ? 132 VAL B CA  1 
ATOM   1060 C  CA  B VAL A 1 134 ? -8.771  1.107   28.458  0.50  14.84 ? 132 VAL B CA  1 
ATOM   1061 C  C   A VAL A 1 134 ? -7.994  0.586   29.477  0.50  15.62 ? 132 VAL B C   1 
ATOM   1062 C  C   B VAL A 1 134 ? -7.859  0.408   29.468  0.50  14.52 ? 132 VAL B C   1 
ATOM   1063 O  O   A VAL A 1 134 ? -6.809  0.644   29.188  0.50  16.06 ? 132 VAL B O   1 
ATOM   1064 O  O   B VAL A 1 134 ? -6.629  0.186   29.250  0.50  13.81 ? 132 VAL B O   1 
ATOM   1065 C  CB  A VAL A 1 134 ? -9.350  2.632   28.972  0.50  18.56 ? 132 VAL B CB  1 
ATOM   1066 C  CB  B VAL A 1 134 ? -8.844  2.638   28.665  0.50  15.99 ? 132 VAL B CB  1 
ATOM   1067 C  CG1 A VAL A 1 134 ? -8.189  3.228   29.783  0.50  18.21 ? 132 VAL B CG1 1 
ATOM   1068 C  CG1 B VAL A 1 134 ? -9.574  3.009   29.969  0.50  15.57 ? 132 VAL B CG1 1 
ATOM   1069 C  CG2 A VAL A 1 134 ? -9.687  3.424   27.721  0.50  16.74 ? 132 VAL B CG2 1 
ATOM   1070 C  CG2 B VAL A 1 134 ? -7.462  3.280   28.649  0.50  15.49 ? 132 VAL B CG2 1 
ATOM   1071 N  N   . GLU A 1 135 ? -8.440  -0.003  30.594  1.00  14.22 ? 133 GLU B N   1 
ATOM   1072 C  CA  . GLU A 1 135 ? -7.578  -0.697  31.526  1.00  15.59 ? 133 GLU B CA  1 
ATOM   1073 C  C   . GLU A 1 135 ? -7.081  -2.045  30.961  1.00  15.38 ? 133 GLU B C   1 
ATOM   1074 O  O   . GLU A 1 135 ? -5.905  -2.412  31.106  1.00  14.49 ? 133 GLU B O   1 
ATOM   1075 C  CB  . GLU A 1 135 ? -8.275  -0.935  32.887  1.00  16.84 ? 133 GLU B CB  1 
ATOM   1076 C  CG  . GLU A 1 135 ? -8.534  0.395   33.664  1.00  22.16 ? 133 GLU B CG  1 
ATOM   1077 C  CD  . GLU A 1 135 ? -7.277  1.050   34.227  1.00  22.89 ? 133 GLU B CD  1 
ATOM   1078 O  OE1 . GLU A 1 135 ? -6.193  0.412   34.218  1.00  22.30 ? 133 GLU B OE1 1 
ATOM   1079 O  OE2 . GLU A 1 135 ? -7.391  2.231   34.708  1.00  26.30 ? 133 GLU B OE2 1 
ATOM   1080 N  N   . ALA A 1 136 ? -8.012  -2.754  30.317  1.00  10.89 ? 134 ALA B N   1 
ATOM   1081 C  CA  . ALA A 1 136 ? -7.701  -4.078  29.743  1.00  11.51 ? 134 ALA B CA  1 
ATOM   1082 C  C   . ALA A 1 136 ? -6.589  -3.968  28.646  1.00  11.60 ? 134 ALA B C   1 
ATOM   1083 O  O   . ALA A 1 136 ? -5.775  -4.874  28.515  1.00  14.62 ? 134 ALA B O   1 
ATOM   1084 C  CB  . ALA A 1 136 ? -8.993  -4.661  29.156  1.00  10.82 ? 134 ALA B CB  1 
ATOM   1085 N  N   . ALA A 1 137 ? -6.586  -2.835  27.940  1.00  12.33 ? 135 ALA B N   1 
ATOM   1086 C  CA  . ALA A 1 137 ? -5.733  -2.709  26.749  1.00  13.96 ? 135 ALA B CA  1 
ATOM   1087 C  C   . ALA A 1 137 ? -4.255  -2.622  27.112  1.00  13.52 ? 135 ALA B C   1 
ATOM   1088 O  O   . ALA A 1 137 ? -3.398  -2.805  26.222  1.00  15.46 ? 135 ALA B O   1 
ATOM   1089 C  CB  . ALA A 1 137 ? -6.171  -1.531  25.889  1.00  11.70 ? 135 ALA B CB  1 
ATOM   1090 N  N   . HIS A 1 138 ? -3.967  -2.438  28.406  1.00  16.14 ? 136 HIS B N   1 
ATOM   1091 C  CA  . HIS A 1 138 ? -2.591  -2.328  28.934  1.00  16.85 ? 136 HIS B CA  1 
ATOM   1092 C  C   . HIS A 1 138 ? -2.142  -3.539  29.716  1.00  16.37 ? 136 HIS B C   1 
ATOM   1093 O  O   . HIS A 1 138 ? -1.135  -3.477  30.453  1.00  20.22 ? 136 HIS B O   1 
ATOM   1094 C  CB  . HIS A 1 138 ? -2.562  -1.067  29.830  1.00  21.84 ? 136 HIS B CB  1 
ATOM   1095 C  CG  . HIS A 1 138 ? -2.606  0.180   29.026  1.00  23.45 ? 136 HIS B CG  1 
ATOM   1096 N  ND1 . HIS A 1 138 ? -1.487  0.775   28.549  1.00  26.18 ? 136 HIS B ND1 1 
ATOM   1097 C  CD2 . HIS A 1 138 ? -3.692  0.900   28.528  1.00  24.43 ? 136 HIS B CD2 1 
ATOM   1098 C  CE1 . HIS A 1 138 ? -1.841  1.864   27.812  1.00  29.25 ? 136 HIS B CE1 1 
ATOM   1099 N  NE2 . HIS A 1 138 ? -3.192  1.936   27.800  1.00  27.22 ? 136 HIS B NE2 1 
ATOM   1100 N  N   . GLU A 1 139 ? -2.819  -4.693  29.588  1.00  15.10 ? 137 GLU B N   1 
ATOM   1101 C  CA  . GLU A 1 139 ? -2.408  -5.864  30.279  1.00  14.54 ? 137 GLU B CA  1 
ATOM   1102 C  C   . GLU A 1 139 ? -2.310  -7.104  29.329  1.00  13.90 ? 137 GLU B C   1 
ATOM   1103 O  O   . GLU A 1 139 ? -3.134  -7.178  28.385  1.00  12.80 ? 137 GLU B O   1 
ATOM   1104 C  CB  . GLU A 1 139 ? -3.480  -6.205  31.347  1.00  18.93 ? 137 GLU B CB  1 
ATOM   1105 C  CG  . GLU A 1 139 ? -3.378  -5.397  32.665  1.00  25.64 ? 137 GLU B CG  1 
ATOM   1106 C  CD  . GLU A 1 139 ? -1.949  -5.156  33.152  1.00  29.56 ? 137 GLU B CD  1 
ATOM   1107 O  OE1 . GLU A 1 139 ? -1.157  -6.083  33.349  1.00  32.71 ? 137 GLU B OE1 1 
ATOM   1108 O  OE2 . GLU A 1 139 ? -1.587  -3.966  33.367  1.00  39.92 ? 137 GLU B OE2 1 
ATOM   1109 N  N   . PRO A 1 140 ? -1.381  -8.016  29.590  1.00  13.91 ? 138 PRO B N   1 
ATOM   1110 C  CA  . PRO A 1 140 ? -1.164  -9.135  28.626  1.00  13.78 ? 138 PRO B CA  1 
ATOM   1111 C  C   . PRO A 1 140 ? -2.390  -9.986  28.395  1.00  12.47 ? 138 PRO B C   1 
ATOM   1112 O  O   . PRO A 1 140 ? -2.573  -10.443 27.250  1.00  12.97 ? 138 PRO B O   1 
ATOM   1113 C  CB  . PRO A 1 140 ? -0.030  -9.972  29.273  1.00  13.70 ? 138 PRO B CB  1 
ATOM   1114 C  CG  . PRO A 1 140 ? 0.720   -8.866  30.001  1.00  15.08 ? 138 PRO B CG  1 
ATOM   1115 C  CD  . PRO A 1 140 ? -0.403  -8.173  30.707  1.00  15.13 ? 138 PRO B CD  1 
ATOM   1116 N  N   . ASP A 1 141 ? -3.269  -10.128 29.375  1.00  10.85 ? 139 ASP B N   1 
ATOM   1117 C  CA  . ASP A 1 141 ? -4.490  -10.945 29.206  1.00  11.74 ? 139 ASP B CA  1 
ATOM   1118 C  C   . ASP A 1 141 ? -5.725  -10.039 28.973  1.00  10.37 ? 139 ASP B C   1 
ATOM   1119 O  O   . ASP A 1 141 ? -6.858  -10.476 29.158  1.00  12.36 ? 139 ASP B O   1 
ATOM   1120 C  CB  . ASP A 1 141 ? -4.739  -11.835 30.431  1.00  13.70 ? 139 ASP B CB  1 
ATOM   1121 C  CG  . ASP A 1 141 ? -4.917  -11.011 31.726  1.00  16.08 ? 139 ASP B CG  1 
ATOM   1122 O  OD1 . ASP A 1 141 ? -4.655  -9.758  31.723  1.00  15.89 ? 139 ASP B OD1 1 
ATOM   1123 O  OD2 . ASP A 1 141 ? -5.322  -11.662 32.737  1.00  19.19 ? 139 ASP B OD2 1 
ATOM   1124 N  N   . GLY A 1 142 ? -5.520  -8.766  28.626  1.00  10.49 ? 140 GLY B N   1 
ATOM   1125 C  CA  . GLY A 1 142 ? -6.698  -7.820  28.566  1.00  9.72  ? 140 GLY B CA  1 
ATOM   1126 C  C   . GLY A 1 142 ? -7.554  -7.918  27.295  1.00  8.54  ? 140 GLY B C   1 
ATOM   1127 O  O   . GLY A 1 142 ? -8.770  -7.692  27.380  1.00  9.58  ? 140 GLY B O   1 
ATOM   1128 N  N   . LEU A 1 143 ? -6.930  -8.203  26.132  1.00  8.82  ? 141 LEU B N   1 
ATOM   1129 C  CA  . LEU A 1 143 ? -7.686  -8.117  24.866  1.00  8.36  ? 141 LEU B CA  1 
ATOM   1130 C  C   . LEU A 1 143 ? -7.696  -9.475  24.139  1.00  7.97  ? 141 LEU B C   1 
ATOM   1131 O  O   . LEU A 1 143 ? -6.782  -10.250 24.244  1.00  8.11  ? 141 LEU B O   1 
ATOM   1132 C  CB  . LEU A 1 143 ? -7.021  -7.092  23.877  1.00  8.06  ? 141 LEU B CB  1 
ATOM   1133 C  CG  . LEU A 1 143 ? -7.051  -5.668  24.479  1.00  9.37  ? 141 LEU B CG  1 
ATOM   1134 C  CD1 . LEU A 1 143 ? -6.466  -4.701  23.389  1.00  9.33  ? 141 LEU B CD1 1 
ATOM   1135 C  CD2 . LEU A 1 143 ? -8.413  -5.089  24.950  1.00  11.16 ? 141 LEU B CD2 1 
ATOM   1136 N  N   . ALA A 1 144 ? -8.767  -9.716  23.380  1.00  7.50  ? 142 ALA B N   1 
ATOM   1137 C  CA  . ALA A 1 144 ? -8.770  -10.887 22.490  1.00  8.34  ? 142 ALA B CA  1 
ATOM   1138 C  C   . ALA A 1 144 ? -9.310  -10.417 21.196  1.00  8.33  ? 142 ALA B C   1 
ATOM   1139 O  O   . ALA A 1 144 ? -10.373 -9.716  21.107  1.00  8.31  ? 142 ALA B O   1 
ATOM   1140 C  CB  . ALA A 1 144 ? -9.695  -11.983 23.056  1.00  8.16  ? 142 ALA B CB  1 
ATOM   1141 N  N   . VAL A 1 145 ? -8.570  -10.756 20.130  1.00  8.61  ? 143 VAL B N   1 
ATOM   1142 C  CA  . VAL A 1 145 ? -9.002  -10.340 18.774  1.00  8.24  ? 143 VAL B CA  1 
ATOM   1143 C  C   . VAL A 1 145 ? -9.221  -11.588 17.901  1.00  8.87  ? 143 VAL B C   1 
ATOM   1144 O  O   . VAL A 1 145 ? -8.318  -12.438 17.809  1.00  9.11  ? 143 VAL B O   1 
ATOM   1145 C  CB  . VAL A 1 145 ? -7.997  -9.413  18.108  1.00  8.47  ? 143 VAL B CB  1 
ATOM   1146 C  CG1 . VAL A 1 145 ? -8.609  -8.971  16.718  1.00  8.91  ? 143 VAL B CG1 1 
ATOM   1147 C  CG2 . VAL A 1 145 ? -7.821  -8.185  19.077  1.00  9.88  ? 143 VAL B CG2 1 
ATOM   1148 N  N   . LEU A 1 146 ? -10.415 -11.672 17.317  1.00  8.76  ? 144 LEU B N   1 
ATOM   1149 C  CA  . LEU A 1 146 ? -10.758 -12.690 16.353  1.00  10.16 ? 144 LEU B CA  1 
ATOM   1150 C  C   . LEU A 1 146 ? -10.375 -12.119 14.948  1.00  10.01 ? 144 LEU B C   1 
ATOM   1151 O  O   . LEU A 1 146 ? -10.922 -11.029 14.554  1.00  11.94 ? 144 LEU B O   1 
ATOM   1152 C  CB  . LEU A 1 146 ? -12.278 -13.041 16.550  1.00  11.81 ? 144 LEU B CB  1 
ATOM   1153 C  CG  . LEU A 1 146 ? -12.838 -14.079 15.579  1.00  14.80 ? 144 LEU B CG  1 
ATOM   1154 C  CD1 . LEU A 1 146 ? -12.087 -15.407 15.860  1.00  16.49 ? 144 LEU B CD1 1 
ATOM   1155 C  CD2 . LEU A 1 146 ? -14.366 -14.219 15.868  1.00  14.58 ? 144 LEU B CD2 1 
ATOM   1156 N  N   . GLY A 1 147 ? -9.480  -12.840 14.188  1.00  9.08  ? 145 GLY B N   1 
ATOM   1157 C  CA  . GLY A 1 147 ? -9.057  -12.357 12.840  1.00  8.34  ? 145 GLY B CA  1 
ATOM   1158 C  C   . GLY A 1 147 ? -9.804  -13.242 11.839  1.00  9.18  ? 145 GLY B C   1 
ATOM   1159 O  O   . GLY A 1 147 ? -9.775  -14.475 12.009  1.00  9.23  ? 145 GLY B O   1 
ATOM   1160 N  N   . VAL A 1 148 ? -10.492 -12.639 10.841  1.00  7.17  ? 146 VAL B N   1 
ATOM   1161 C  CA  . VAL A 1 148 ? -11.162 -13.455 9.808   1.00  7.40  ? 146 VAL B CA  1 
ATOM   1162 C  C   . VAL A 1 148 ? -10.637 -12.994 8.471   1.00  7.24  ? 146 VAL B C   1 
ATOM   1163 O  O   . VAL A 1 148 ? -10.797 -11.812 8.117   1.00  7.18  ? 146 VAL B O   1 
ATOM   1164 C  CB  . VAL A 1 148 ? -12.681 -13.194 9.870   1.00  7.86  ? 146 VAL B CB  1 
ATOM   1165 C  CG1 . VAL A 1 148 ? -13.368 -14.143 8.806   1.00  9.15  ? 146 VAL B CG1 1 
ATOM   1166 C  CG2 . VAL A 1 148 ? -13.167 -13.624 11.287  1.00  7.93  ? 146 VAL B CG2 1 
ATOM   1167 N  N   . PHE A 1 149 ? -10.123 -13.941 7.667   1.00  7.24  ? 147 PHE B N   1 
ATOM   1168 C  CA  . PHE A 1 149 ? -9.649  -13.605 6.307   1.00  7.66  ? 147 PHE B CA  1 
ATOM   1169 C  C   . PHE A 1 149 ? -10.803 -13.390 5.377   1.00  9.16  ? 147 PHE B C   1 
ATOM   1170 O  O   . PHE A 1 149 ? -11.858 -14.059 5.499   1.00  9.00  ? 147 PHE B O   1 
ATOM   1171 C  CB  . PHE A 1 149 ? -8.778  -14.790 5.793   1.00  7.89  ? 147 PHE B CB  1 
ATOM   1172 C  CG  . PHE A 1 149 ? -7.481  -14.974 6.598   1.00  7.71  ? 147 PHE B CG  1 
ATOM   1173 C  CD1 . PHE A 1 149 ? -6.564  -13.868 6.728   1.00  7.06  ? 147 PHE B CD1 1 
ATOM   1174 C  CD2 . PHE A 1 149 ? -7.155  -16.208 7.188   1.00  7.52  ? 147 PHE B CD2 1 
ATOM   1175 C  CE1 . PHE A 1 149 ? -5.345  -14.041 7.440   1.00  7.04  ? 147 PHE B CE1 1 
ATOM   1176 C  CE2 . PHE A 1 149 ? -5.938  -16.372 7.894   1.00  7.71  ? 147 PHE B CE2 1 
ATOM   1177 C  CZ  . PHE A 1 149 ? -5.024  -15.306 7.986   1.00  8.11  ? 147 PHE B CZ  1 
ATOM   1178 N  N   . LEU A 1 150 ? -10.614 -12.460 4.442   1.00  7.71  ? 148 LEU B N   1 
ATOM   1179 C  CA  . LEU A 1 150 ? -11.561 -12.257 3.301   1.00  7.73  ? 148 LEU B CA  1 
ATOM   1180 C  C   . LEU A 1 150 ? -10.854 -12.677 1.996   1.00  8.24  ? 148 LEU B C   1 
ATOM   1181 O  O   . LEU A 1 150 ? -9.665  -12.244 1.755   1.00  8.34  ? 148 LEU B O   1 
ATOM   1182 C  CB  . LEU A 1 150 ? -11.997 -10.757 3.172   1.00  7.76  ? 148 LEU B CB  1 
ATOM   1183 C  CG  . LEU A 1 150 ? -13.113 -10.441 4.164   1.00  8.07  ? 148 LEU B CG  1 
ATOM   1184 C  CD1 . LEU A 1 150 ? -12.568 -10.361 5.637   1.00  9.55  ? 148 LEU B CD1 1 
ATOM   1185 C  CD2 . LEU A 1 150 ? -13.509 -9.013  3.781   1.00  7.21  ? 148 LEU B CD2 1 
ATOM   1186 N  N   . GLN A 1 151 ? -11.535 -13.462 1.157   1.00  8.80  ? 149 GLN B N   1 
ATOM   1187 C  CA  . GLN A 1 151 ? -11.008 -13.811 -0.186  1.00  10.96 ? 149 GLN B CA  1 
ATOM   1188 C  C   . GLN A 1 151 ? -12.007 -13.322 -1.216  1.00  10.95 ? 149 GLN B C   1 
ATOM   1189 O  O   . GLN A 1 151 ? -13.205 -13.159 -0.885  1.00  10.07 ? 149 GLN B O   1 
ATOM   1190 C  CB  . GLN A 1 151 ? -10.758 -15.292 -0.338  1.00  14.08 ? 149 GLN B CB  1 
ATOM   1191 C  CG  . GLN A 1 151 ? -11.962 -16.128 -0.128  1.00  16.63 ? 149 GLN B CG  1 
ATOM   1192 C  CD  . GLN A 1 151 ? -11.599 -17.632 -0.292  1.00  19.74 ? 149 GLN B CD  1 
ATOM   1193 O  OE1 . GLN A 1 151 ? -10.426 -18.013 -0.435  1.00  24.92 ? 149 GLN B OE1 1 
ATOM   1194 N  NE2 . GLN A 1 151 ? -12.610 -18.434 -0.388  1.00  26.08 ? 149 GLN B NE2 1 
ATOM   1195 N  N   . ILE A 1 152 ? -11.527 -13.043 -2.445  1.00  10.98 ? 150 ILE B N   1 
ATOM   1196 C  CA  . ILE A 1 152 ? -12.490 -12.530 -3.469  1.00  11.53 ? 150 ILE B CA  1 
ATOM   1197 C  C   . ILE A 1 152 ? -13.388 -13.691 -3.912  1.00  12.74 ? 150 ILE B C   1 
ATOM   1198 O  O   . ILE A 1 152 ? -12.899 -14.797 -4.199  1.00  15.28 ? 150 ILE B O   1 
ATOM   1199 C  CB  . ILE A 1 152 ? -11.719 -11.957 -4.679  1.00  10.99 ? 150 ILE B CB  1 
ATOM   1200 C  CG1 . ILE A 1 152 ? -10.848 -10.766 -4.217  1.00  10.92 ? 150 ILE B CG1 1 
ATOM   1201 C  CG2 . ILE A 1 152 ? -12.672 -11.542 -5.829  1.00  11.42 ? 150 ILE B CG2 1 
ATOM   1202 C  CD1 . ILE A 1 152 ? -11.521 -9.636  -3.508  1.00  11.90 ? 150 ILE B CD1 1 
ATOM   1203 N  N   . GLY A 1 153 ? -14.679 -13.428 -3.925  1.00  12.62 ? 151 GLY B N   1 
ATOM   1204 C  CA  . GLY A 1 153 ? -15.644 -14.434 -4.448  1.00  14.12 ? 151 GLY B CA  1 
ATOM   1205 C  C   . GLY A 1 153 ? -16.962 -13.781 -4.654  1.00  15.37 ? 151 GLY B C   1 
ATOM   1206 O  O   . GLY A 1 153 ? -17.004 -12.638 -5.158  1.00  16.15 ? 151 GLY B O   1 
ATOM   1207 N  N   . GLU A 1 154 ? -18.032 -14.458 -4.263  1.00  15.71 ? 152 GLU B N   1 
ATOM   1208 C  CA  . GLU A 1 154 ? -19.364 -13.882 -4.479  1.00  16.57 ? 152 GLU B CA  1 
ATOM   1209 C  C   . GLU A 1 154 ? -19.548 -12.685 -3.534  1.00  14.56 ? 152 GLU B C   1 
ATOM   1210 O  O   . GLU A 1 154 ? -18.924 -12.650 -2.412  1.00  14.02 ? 152 GLU B O   1 
ATOM   1211 C  CB  . GLU A 1 154 ? -20.456 -14.863 -4.091  1.00  21.58 ? 152 GLU B CB  1 
ATOM   1212 C  CG  . GLU A 1 154 ? -20.443 -16.108 -5.007  1.00  29.41 ? 152 GLU B CG  1 
ATOM   1213 C  CD  . GLU A 1 154 ? -21.690 -16.969 -4.764  1.00  42.64 ? 152 GLU B CD  1 
ATOM   1214 O  OE1 . GLU A 1 154 ? -22.802 -16.370 -4.576  1.00  44.74 ? 152 GLU B OE1 1 
ATOM   1215 O  OE2 . GLU A 1 154 ? -21.573 -18.232 -4.745  1.00  45.75 ? 152 GLU B OE2 1 
ATOM   1216 N  N   . PRO A 1 155 ? -20.403 -11.743 -3.917  1.00  13.27 ? 153 PRO B N   1 
ATOM   1217 C  CA  . PRO A 1 155 ? -20.657 -10.592 -3.018  1.00  11.07 ? 153 PRO B CA  1 
ATOM   1218 C  C   . PRO A 1 155 ? -21.222 -11.138 -1.708  1.00  12.14 ? 153 PRO B C   1 
ATOM   1219 O  O   . PRO A 1 155 ? -21.951 -12.109 -1.718  1.00  13.59 ? 153 PRO B O   1 
ATOM   1220 C  CB  . PRO A 1 155 ? -21.777 -9.843  -3.694  1.00  11.88 ? 153 PRO B CB  1 
ATOM   1221 C  CG  . PRO A 1 155 ? -21.627 -10.199 -5.138  1.00  13.14 ? 153 PRO B CG  1 
ATOM   1222 C  CD  . PRO A 1 155 ? -21.027 -11.586 -5.251  1.00  12.82 ? 153 PRO B CD  1 
ATOM   1223 N  N   . ASN A 1 156 ? -20.936 -10.459 -0.587  1.00  12.39 ? 154 ASN B N   1 
ATOM   1224 C  CA  . ASN A 1 156 ? -21.392 -10.861 0.732   1.00  13.46 ? 154 ASN B CA  1 
ATOM   1225 C  C   . ASN A 1 156 ? -22.494 -9.925  1.199   1.00  12.45 ? 154 ASN B C   1 
ATOM   1226 O  O   . ASN A 1 156 ? -22.321 -8.687  1.323   1.00  12.12 ? 154 ASN B O   1 
ATOM   1227 C  CB  . ASN A 1 156 ? -20.158 -10.805 1.652   1.00  12.87 ? 154 ASN B CB  1 
ATOM   1228 C  CG  . ASN A 1 156 ? -20.420 -11.354 2.996   1.00  15.73 ? 154 ASN B CG  1 
ATOM   1229 O  OD1 . ASN A 1 156 ? -21.415 -10.950 3.644   1.00  16.03 ? 154 ASN B OD1 1 
ATOM   1230 N  ND2 . ASN A 1 156 ? -19.538 -12.288 3.460   1.00  14.89 ? 154 ASN B ND2 1 
ATOM   1231 N  N   . SER A 1 157 ? -23.691 -10.486 1.400   1.00  13.85 ? 155 SER B N   1 
ATOM   1232 C  CA  . SER A 1 157 ? -24.861 -9.602  1.654   1.00  14.40 ? 155 SER B CA  1 
ATOM   1233 C  C   . SER A 1 157 ? -24.730 -8.878  2.991   1.00  15.04 ? 155 SER B C   1 
ATOM   1234 O  O   . SER A 1 157 ? -25.251 -7.773  3.102   1.00  17.34 ? 155 SER B O   1 
ATOM   1235 C  CB  . SER A 1 157 ? -26.234 -10.344 1.623   1.00  16.35 ? 155 SER B CB  1 
ATOM   1236 O  OG  . SER A 1 157 ? -26.169 -11.378 2.557   1.00  19.15 ? 155 SER B OG  1 
ATOM   1237 N  N   A GLN A 1 158 ? -24.095 -9.473  4.022   0.50  14.40 ? 156 GLN B N   1 
ATOM   1238 N  N   B GLN A 1 158 ? -24.049 -9.477  3.963   0.50  13.61 ? 156 GLN B N   1 
ATOM   1239 C  CA  A GLN A 1 158 ? -23.861 -8.705  5.276   0.50  15.22 ? 156 GLN B CA  1 
ATOM   1240 C  CA  B GLN A 1 158 ? -23.802 -8.796  5.217   0.50  13.81 ? 156 GLN B CA  1 
ATOM   1241 C  C   A GLN A 1 158 ? -22.817 -7.576  5.096   0.50  14.81 ? 156 GLN B C   1 
ATOM   1242 C  C   B GLN A 1 158 ? -22.795 -7.641  5.126   0.50  14.03 ? 156 GLN B C   1 
ATOM   1243 O  O   A GLN A 1 158 ? -23.001 -6.480  5.639   0.50  16.32 ? 156 GLN B O   1 
ATOM   1244 O  O   B GLN A 1 158 ? -23.004 -6.590  5.730   0.50  15.93 ? 156 GLN B O   1 
ATOM   1245 C  CB  A GLN A 1 158 ? -23.427 -9.582  6.465   0.50  16.81 ? 156 GLN B CB  1 
ATOM   1246 C  CB  B GLN A 1 158 ? -23.344 -9.833  6.201   0.50  13.74 ? 156 GLN B CB  1 
ATOM   1247 C  CG  A GLN A 1 158 ? -24.508 -10.431 7.190   0.50  18.86 ? 156 GLN B CG  1 
ATOM   1248 C  CG  B GLN A 1 158 ? -24.479 -10.805 6.425   0.50  13.40 ? 156 GLN B CG  1 
ATOM   1249 C  CD  A GLN A 1 158 ? -25.725 -9.695  7.735   0.50  18.94 ? 156 GLN B CD  1 
ATOM   1250 C  CD  B GLN A 1 158 ? -24.178 -11.645 7.616   0.50  13.96 ? 156 GLN B CD  1 
ATOM   1251 O  OE1 A GLN A 1 158 ? -26.781 -9.902  7.175   0.50  20.95 ? 156 GLN B OE1 1 
ATOM   1252 O  OE1 B GLN A 1 158 ? -23.689 -12.744 7.467   0.50  14.06 ? 156 GLN B OE1 1 
ATOM   1253 N  NE2 A GLN A 1 158 ? -25.610 -8.852  8.836   0.50  17.63 ? 156 GLN B NE2 1 
ATOM   1254 N  NE2 B GLN A 1 158 ? -24.412 -11.100 8.808   0.50  14.37 ? 156 GLN B NE2 1 
ATOM   1255 N  N   . LEU A 1 159 ? -21.760 -7.818  4.307   1.00  13.55 ? 157 LEU B N   1 
ATOM   1256 C  CA  . LEU A 1 159 ? -20.746 -6.772  4.092   1.00  12.66 ? 157 LEU B CA  1 
ATOM   1257 C  C   . LEU A 1 159 ? -21.347 -5.658  3.220   1.00  13.37 ? 157 LEU B C   1 
ATOM   1258 O  O   . LEU A 1 159 ? -20.900 -4.527  3.325   1.00  13.31 ? 157 LEU B O   1 
ATOM   1259 C  CB  . LEU A 1 159 ? -19.497 -7.356  3.437   1.00  13.54 ? 157 LEU B CB  1 
ATOM   1260 C  CG  . LEU A 1 159 ? -18.709 -8.311  4.334   1.00  17.11 ? 157 LEU B CG  1 
ATOM   1261 C  CD1 . LEU A 1 159 ? -17.538 -8.922  3.582   1.00  16.22 ? 157 LEU B CD1 1 
ATOM   1262 C  CD2 . LEU A 1 159 ? -18.232 -7.583  5.583   1.00  15.33 ? 157 LEU B CD2 1 
ATOM   1263 N  N   . GLN A 1 160 ? -22.360 -5.978  2.368   1.00  13.72 ? 158 GLN B N   1 
ATOM   1264 C  CA  . GLN A 1 160 ? -23.030 -4.953  1.549   1.00  15.78 ? 158 GLN B CA  1 
ATOM   1265 C  C   . GLN A 1 160 ? -23.621 -3.901  2.483   1.00  14.58 ? 158 GLN B C   1 
ATOM   1266 O  O   . GLN A 1 160 ? -23.696 -2.732  2.198   1.00  16.71 ? 158 GLN B O   1 
ATOM   1267 C  CB  . GLN A 1 160 ? -24.201 -5.564  0.687   1.00  16.85 ? 158 GLN B CB  1 
ATOM   1268 C  CG  . GLN A 1 160 ? -24.763 -4.573  -0.356  1.00  16.39 ? 158 GLN B CG  1 
ATOM   1269 C  CD  . GLN A 1 160 ? -24.034 -4.489  -1.678  1.00  18.33 ? 158 GLN B CD  1 
ATOM   1270 O  OE1 . GLN A 1 160 ? -22.966 -5.050  -1.891  1.00  18.31 ? 158 GLN B OE1 1 
ATOM   1271 N  NE2 . GLN A 1 160 ? -24.622 -3.731  -2.622  1.00  19.75 ? 158 GLN B NE2 1 
ATOM   1272 N  N   . LYS A 1 161 ? -24.101 -4.346  3.632   1.00  16.25 ? 159 LYS B N   1 
ATOM   1273 C  CA  . LYS A 1 161 ? -24.609 -3.384  4.568   1.00  16.03 ? 159 LYS B CA  1 
ATOM   1274 C  C   . LYS A 1 161 ? -23.577 -2.326  5.012   1.00  16.72 ? 159 LYS B C   1 
ATOM   1275 O  O   . LYS A 1 161 ? -23.910 -1.133  5.206   1.00  17.53 ? 159 LYS B O   1 
ATOM   1276 C  CB  . LYS A 1 161 ? -25.182 -4.087  5.802   1.00  16.70 ? 159 LYS B CB  1 
ATOM   1277 C  CG  . LYS A 1 161 ? -25.739 -3.147  6.874   1.00  25.60 ? 159 LYS B CG  1 
ATOM   1278 C  CD  . LYS A 1 161 ? -26.261 -4.036  8.032   1.00  31.86 ? 159 LYS B CD  1 
ATOM   1279 C  CE  . LYS A 1 161 ? -26.780 -3.294  9.271   1.00  32.13 ? 159 LYS B CE  1 
ATOM   1280 N  NZ  . LYS A 1 161 ? -27.945 -2.443  8.888   1.00  31.07 ? 159 LYS B NZ  1 
ATOM   1281 N  N   . ILE A 1 162 ? -22.342 -2.791  5.265   1.00  14.18 ? 160 ILE B N   1 
ATOM   1282 C  CA  . ILE A 1 162 ? -21.241 -1.850  5.519   1.00  12.65 ? 160 ILE B CA  1 
ATOM   1283 C  C   . ILE A 1 162 ? -20.894 -0.999  4.279   1.00  12.56 ? 160 ILE B C   1 
ATOM   1284 O  O   . ILE A 1 162 ? -20.698 0.208   4.387   1.00  13.39 ? 160 ILE B O   1 
ATOM   1285 C  CB  . ILE A 1 162 ? -19.985 -2.717  5.953   1.00  12.18 ? 160 ILE B CB  1 
ATOM   1286 C  CG1 . ILE A 1 162 ? -20.305 -3.353  7.311   1.00  13.35 ? 160 ILE B CG1 1 
ATOM   1287 C  CG2 . ILE A 1 162 ? -18.782 -1.795  6.129   1.00  13.69 ? 160 ILE B CG2 1 
ATOM   1288 C  CD1 . ILE A 1 162 ? -19.164 -4.294  7.842   1.00  16.15 ? 160 ILE B CD1 1 
ATOM   1289 N  N   . THR A 1 163 ? -20.689 -1.626  3.104   1.00  14.06 ? 161 THR B N   1 
ATOM   1290 C  CA  . THR A 1 163 ? -20.300 -0.827  1.910   1.00  12.82 ? 161 THR B CA  1 
ATOM   1291 C  C   . THR A 1 163 ? -21.328 0.264   1.584   1.00  14.94 ? 161 THR B C   1 
ATOM   1292 O  O   . THR A 1 163 ? -20.973 1.344   1.132   1.00  15.00 ? 161 THR B O   1 
ATOM   1293 C  CB  . THR A 1 163 ? -19.874 -1.698  0.679   1.00  13.26 ? 161 THR B CB  1 
ATOM   1294 O  OG1 . THR A 1 163 ? -20.972 -2.490  0.228   1.00  16.54 ? 161 THR B OG1 1 
ATOM   1295 C  CG2 . THR A 1 163 ? -18.733 -2.617  0.956   1.00  13.83 ? 161 THR B CG2 1 
ATOM   1296 N  N   . ASP A 1 164 ? -22.613 -0.008  1.792   1.00  15.35 ? 162 ASP B N   1 
ATOM   1297 C  CA  . ASP A 1 164 ? -23.663 0.972   1.485   1.00  18.26 ? 162 ASP B CA  1 
ATOM   1298 C  C   . ASP A 1 164 ? -23.547 2.254   2.330   1.00  15.39 ? 162 ASP B C   1 
ATOM   1299 O  O   . ASP A 1 164 ? -24.088 3.309   1.934   1.00  21.47 ? 162 ASP B O   1 
ATOM   1300 C  CB  . ASP A 1 164 ? -25.043 0.367   1.711   1.00  16.64 ? 162 ASP B CB  1 
ATOM   1301 C  CG  . ASP A 1 164 ? -25.496 -0.542  0.605   1.00  21.76 ? 162 ASP B CG  1 
ATOM   1302 O  OD1 . ASP A 1 164 ? -24.907 -0.542  -0.477  1.00  22.22 ? 162 ASP B OD1 1 
ATOM   1303 O  OD2 . ASP A 1 164 ? -26.501 -1.279  0.822   1.00  23.72 ? 162 ASP B OD2 1 
ATOM   1304 N  N   . THR A 1 165 ? -22.810 2.191   3.435   1.00  16.78 ? 163 THR B N   1 
ATOM   1305 C  CA  . THR A 1 165 ? -22.628 3.349   4.352   1.00  15.00 ? 163 THR B CA  1 
ATOM   1306 C  C   . THR A 1 165 ? -21.421 4.182   4.022   1.00  15.24 ? 163 THR B C   1 
ATOM   1307 O  O   . THR A 1 165 ? -21.281 5.343   4.574   1.00  16.48 ? 163 THR B O   1 
ATOM   1308 C  CB  . THR A 1 165 ? -22.462 2.933   5.822   1.00  17.53 ? 163 THR B CB  1 
ATOM   1309 O  OG1 . THR A 1 165 ? -21.134 2.373   6.045   1.00  17.48 ? 163 THR B OG1 1 
ATOM   1310 C  CG2 . THR A 1 165 ? -23.528 1.951   6.237   1.00  16.85 ? 163 THR B CG2 1 
ATOM   1311 N  N   . LEU A 1 166 ? -20.519 3.677   3.173   1.00  14.83 ? 164 LEU B N   1 
ATOM   1312 C  CA  . LEU A 1 166 ? -19.203 4.277   3.087   1.00  14.23 ? 164 LEU B CA  1 
ATOM   1313 C  C   . LEU A 1 166 ? -19.286 5.660   2.441   1.00  16.44 ? 164 LEU B C   1 
ATOM   1314 O  O   . LEU A 1 166 ? -18.509 6.526   2.841   1.00  16.60 ? 164 LEU B O   1 
ATOM   1315 C  CB  . LEU A 1 166 ? -18.174 3.395   2.321   1.00  14.41 ? 164 LEU B CB  1 
ATOM   1316 C  CG  . LEU A 1 166 ? -17.863 2.059   3.015   1.00  12.57 ? 164 LEU B CG  1 
ATOM   1317 C  CD1 . LEU A 1 166 ? -17.037 1.128   2.127   1.00  13.83 ? 164 LEU B CD1 1 
ATOM   1318 C  CD2 . LEU A 1 166 ? -17.165 2.230   4.383   1.00  14.63 ? 164 LEU B CD2 1 
ATOM   1319 N  N   . ASP A 1 167 ? -20.192 5.883   1.480   1.00  17.52 ? 165 ASP B N   1 
ATOM   1320 C  CA  . ASP A 1 167 ? -20.263 7.271   0.922   1.00  19.88 ? 165 ASP B CA  1 
ATOM   1321 C  C   . ASP A 1 167 ? -20.547 8.340   2.020   1.00  20.90 ? 165 ASP B C   1 
ATOM   1322 O  O   . ASP A 1 167 ? -19.943 9.432   1.993   1.00  23.74 ? 165 ASP B O   1 
ATOM   1323 C  CB  . ASP A 1 167 ? -21.290 7.383   -0.225  1.00  23.11 ? 165 ASP B CB  1 
ATOM   1324 C  CG  . ASP A 1 167 ? -20.851 6.654   -1.506  1.00  25.82 ? 165 ASP B CG  1 
ATOM   1325 O  OD1 . ASP A 1 167 ? -19.664 6.322   -1.672  1.00  25.56 ? 165 ASP B OD1 1 
ATOM   1326 O  OD2 . ASP A 1 167 ? -21.721 6.450   -2.389  1.00  31.41 ? 165 ASP B OD2 1 
ATOM   1327 N  N   . SER A 1 168 ? -21.323 7.978   3.047   1.00  19.22 ? 166 SER B N   1 
ATOM   1328 C  CA  . SER A 1 168 ? -21.670 8.892   4.104   1.00  19.62 ? 166 SER B CA  1 
ATOM   1329 C  C   . SER A 1 168 ? -20.536 9.134   5.100   1.00  20.06 ? 166 SER B C   1 
ATOM   1330 O  O   . SER A 1 168 ? -20.594 10.057  5.920   1.00  20.54 ? 166 SER B O   1 
ATOM   1331 C  CB  . SER A 1 168 ? -22.947 8.467   4.830   1.00  21.21 ? 166 SER B CB  1 
ATOM   1332 O  OG  . SER A 1 168 ? -22.675 7.324   5.644   1.00  23.40 ? 166 SER B OG  1 
ATOM   1333 N  N   . ILE A 1 169 ? -19.493 8.291   5.075   1.00  14.99 ? 167 ILE B N   1 
ATOM   1334 C  CA  . ILE A 1 169 ? -18.347 8.476   5.990   1.00  15.26 ? 167 ILE B CA  1 
ATOM   1335 C  C   . ILE A 1 169 ? -16.967 8.659   5.282   1.00  15.27 ? 167 ILE B C   1 
ATOM   1336 O  O   . ILE A 1 169 ? -15.932 8.282   5.805   1.00  12.77 ? 167 ILE B O   1 
ATOM   1337 C  CB  . ILE A 1 169 ? -18.263 7.376   7.090   1.00  15.76 ? 167 ILE B CB  1 
ATOM   1338 C  CG1 . ILE A 1 169 ? -18.183 5.947   6.496   1.00  14.77 ? 167 ILE B CG1 1 
ATOM   1339 C  CG2 . ILE A 1 169 ? -19.511 7.438   7.934   1.00  16.27 ? 167 ILE B CG2 1 
ATOM   1340 C  CD1 . ILE A 1 169 ? -17.714 4.993   7.617   1.00  17.94 ? 167 ILE B CD1 1 
ATOM   1341 N  N   . LYS A 1 170 ? -16.978 9.241   4.089   1.00  16.18 ? 168 LYS B N   1 
ATOM   1342 C  CA  . LYS A 1 170 ? -15.773 9.311   3.292   1.00  17.45 ? 168 LYS B CA  1 
ATOM   1343 C  C   . LYS A 1 170 ? -14.670 10.072  4.036   1.00  17.25 ? 168 LYS B C   1 
ATOM   1344 O  O   . LYS A 1 170 ? -13.508 9.686   4.050   1.00  15.55 ? 168 LYS B O   1 
ATOM   1345 C  CB  . LYS A 1 170 ? -16.122 9.987   1.939   1.00  19.51 ? 168 LYS B CB  1 
ATOM   1346 C  CG  . LYS A 1 170 ? -14.876 10.506  1.246   1.00  24.05 ? 168 LYS B CG  1 
ATOM   1347 C  CD  . LYS A 1 170 ? -15.278 11.054  -0.132  1.00  31.24 ? 168 LYS B CD  1 
ATOM   1348 C  CE  . LYS A 1 170 ? -14.126 11.696  -0.901  1.00  37.87 ? 168 LYS B CE  1 
ATOM   1349 N  NZ  . LYS A 1 170 ? -14.748 12.445  -2.044  1.00  47.76 ? 168 LYS B NZ  1 
ATOM   1350 N  N   . GLU A 1 171 ? -15.030 11.179  4.686   1.00  19.79 ? 169 GLU B N   1 
ATOM   1351 C  CA  . GLU A 1 171 ? -14.041 11.965  5.397   1.00  21.09 ? 169 GLU B CA  1 
ATOM   1352 C  C   . GLU A 1 171 ? -13.683 11.454  6.757   1.00  18.94 ? 169 GLU B C   1 
ATOM   1353 O  O   . GLU A 1 171 ? -14.567 10.955  7.487   1.00  19.91 ? 169 GLU B O   1 
ATOM   1354 C  CB  . GLU A 1 171 ? -14.469 13.443  5.527   1.00  24.64 ? 169 GLU B CB  1 
ATOM   1355 C  CG  . GLU A 1 171 ? -14.567 14.102  4.142   1.00  31.23 ? 169 GLU B CG  1 
ATOM   1356 C  CD  . GLU A 1 171 ? -15.896 13.840  3.433   1.00  39.41 ? 169 GLU B CD  1 
ATOM   1357 O  OE1 . GLU A 1 171 ? -15.915 14.011  2.179   1.00  51.28 ? 169 GLU B OE1 1 
ATOM   1358 O  OE2 . GLU A 1 171 ? -16.919 13.401  4.069   1.00  39.79 ? 169 GLU B OE2 1 
ATOM   1359 N  N   . LYS A 1 172 ? -12.413 11.586  7.097   1.00  17.62 ? 170 LYS B N   1 
ATOM   1360 C  CA  . LYS A 1 172 ? -11.902 11.157  8.369   1.00  17.80 ? 170 LYS B CA  1 
ATOM   1361 C  C   . LYS A 1 172 ? -12.746 11.822  9.475   1.00  21.37 ? 170 LYS B C   1 
ATOM   1362 O  O   . LYS A 1 172 ? -13.025 13.059  9.385   1.00  19.41 ? 170 LYS B O   1 
ATOM   1363 C  CB  . LYS A 1 172 ? -10.437 11.553  8.553   1.00  18.42 ? 170 LYS B CB  1 
ATOM   1364 C  CG  . LYS A 1 172 ? -9.856  11.330  9.954   1.00  18.47 ? 170 LYS B CG  1 
ATOM   1365 C  CD  . LYS A 1 172 ? -8.400  11.694  9.952   1.00  18.83 ? 170 LYS B CD  1 
ATOM   1366 C  CE  . LYS A 1 172 ? -7.827  11.283  11.312  1.00  19.20 ? 170 LYS B CE  1 
ATOM   1367 N  NZ  . LYS A 1 172 ? -6.372  11.552  11.380  1.00  24.46 ? 170 LYS B NZ  1 
ATOM   1368 N  N   . GLY A 1 173 ? -13.173 11.050  10.476  1.00  15.50 ? 171 GLY B N   1 
ATOM   1369 C  CA  . GLY A 1 173 ? -13.962 11.633  11.539  1.00  16.06 ? 171 GLY B CA  1 
ATOM   1370 C  C   . GLY A 1 173 ? -15.459 11.501  11.388  1.00  15.50 ? 171 GLY B C   1 
ATOM   1371 O  O   . GLY A 1 173 ? -16.169 11.642  12.395  1.00  17.46 ? 171 GLY B O   1 
ATOM   1372 N  N   . LYS A 1 174 ? -15.953 11.237  10.179  1.00  14.99 ? 172 LYS B N   1 
ATOM   1373 C  CA  . LYS A 1 174 ? -17.400 11.140  9.981   1.00  16.72 ? 172 LYS B CA  1 
ATOM   1374 C  C   . LYS A 1 174 ? -17.955 9.830   10.538  1.00  17.76 ? 172 LYS B C   1 
ATOM   1375 O  O   . LYS A 1 174 ? -17.269 8.800   10.489  1.00  17.88 ? 172 LYS B O   1 
ATOM   1376 C  CB  . LYS A 1 174 ? -17.814 11.224  8.501   1.00  18.55 ? 172 LYS B CB  1 
ATOM   1377 C  CG  . LYS A 1 174 ? -17.525 12.582  7.795   1.00  23.63 ? 172 LYS B CG  1 
ATOM   1378 C  CD  . LYS A 1 174 ? -18.590 13.615  8.016   1.00  29.30 ? 172 LYS B CD  1 
ATOM   1379 C  CE  . LYS A 1 174 ? -18.171 14.938  7.339   1.00  35.28 ? 172 LYS B CE  1 
ATOM   1380 N  NZ  . LYS A 1 174 ? -18.256 14.815  5.843   1.00  36.14 ? 172 LYS B NZ  1 
ATOM   1381 N  N   . GLN A 1 175 ? -19.175 9.921   11.026  1.00  16.52 ? 173 GLN B N   1 
ATOM   1382 C  CA  . GLN A 1 175 ? -19.892 8.746   11.571  1.00  18.75 ? 173 GLN B CA  1 
ATOM   1383 C  C   . GLN A 1 175 ? -21.341 8.735   11.177  1.00  21.45 ? 173 GLN B C   1 
ATOM   1384 O  O   . GLN A 1 175 ? -21.941 9.790   10.830  1.00  15.74 ? 173 GLN B O   1 
ATOM   1385 C  CB  . GLN A 1 175 ? -19.704 8.635   13.089  1.00  23.55 ? 173 GLN B CB  1 
ATOM   1386 C  CG  . GLN A 1 175 ? -20.573 9.514   13.918  1.00  28.54 ? 173 GLN B CG  1 
ATOM   1387 C  CD  . GLN A 1 175 ? -20.348 9.260   15.421  1.00  37.39 ? 173 GLN B CD  1 
ATOM   1388 O  OE1 . GLN A 1 175 ? -21.299 8.963   16.177  1.00  38.89 ? 173 GLN B OE1 1 
ATOM   1389 N  NE2 . GLN A 1 175 ? -19.084 9.344   15.845  1.00  34.99 ? 173 GLN B NE2 1 
ATOM   1390 N  N   . THR A 1 176 ? -21.914 7.531   11.191  1.00  18.96 ? 174 THR B N   1 
ATOM   1391 C  CA  . THR A 1 176 ? -23.286 7.367   10.901  1.00  20.24 ? 174 THR B CA  1 
ATOM   1392 C  C   . THR A 1 176 ? -23.864 6.159   11.717  1.00  21.20 ? 174 THR B C   1 
ATOM   1393 O  O   . THR A 1 176 ? -23.089 5.310   12.218  1.00  17.84 ? 174 THR B O   1 
ATOM   1394 C  CB  . THR A 1 176 ? -23.557 7.306   9.404   1.00  23.16 ? 174 THR B CB  1 
ATOM   1395 O  OG1 . THR A 1 176 ? -24.941 7.625   9.217   1.00  26.87 ? 174 THR B OG1 1 
ATOM   1396 C  CG2 . THR A 1 176 ? -23.283 6.000   8.808   1.00  20.92 ? 174 THR B CG2 1 
ATOM   1397 N  N   . ARG A 1 177 ? -25.189 6.138   11.923  1.00  18.09 ? 175 ARG B N   1 
ATOM   1398 C  CA  . ARG A 1 177 ? -25.745 5.119   12.768  1.00  17.19 ? 175 ARG B CA  1 
ATOM   1399 C  C   . ARG A 1 177 ? -25.741 3.854   11.991  1.00  16.49 ? 175 ARG B C   1 
ATOM   1400 O  O   . ARG A 1 177 ? -25.908 3.846   10.780  1.00  17.86 ? 175 ARG B O   1 
ATOM   1401 C  CB  . ARG A 1 177 ? -27.179 5.534   13.233  1.00  20.08 ? 175 ARG B CB  1 
ATOM   1402 C  CG  . ARG A 1 177 ? -26.998 6.758   14.107  1.00  20.64 ? 175 ARG B CG  1 
ATOM   1403 C  CD  . ARG A 1 177 ? -28.223 7.269   14.848  1.00  26.11 ? 175 ARG B CD  1 
ATOM   1404 N  NE  . ARG A 1 177 ? -28.890 6.229   15.617  1.00  25.22 ? 175 ARG B NE  1 
ATOM   1405 C  CZ  . ARG A 1 177 ? -30.044 6.402   16.252  1.00  27.60 ? 175 ARG B CZ  1 
ATOM   1406 N  NH1 . ARG A 1 177 ? -30.665 7.575   16.202  1.00  18.35 ? 175 ARG B NH1 1 
ATOM   1407 N  NH2 . ARG A 1 177 ? -30.581 5.403   16.935  1.00  25.07 ? 175 ARG B NH2 1 
ATOM   1408 N  N   . PHE A 1 178 ? -25.574 2.754   12.688  1.00  15.99 ? 176 PHE B N   1 
ATOM   1409 C  CA  . PHE A 1 178 ? -25.392 1.460   12.066  1.00  15.70 ? 176 PHE B CA  1 
ATOM   1410 C  C   . PHE A 1 178 ? -25.779 0.396   13.084  1.00  15.04 ? 176 PHE B C   1 
ATOM   1411 O  O   . PHE A 1 178 ? -25.062 0.196   14.101  1.00  14.95 ? 176 PHE B O   1 
ATOM   1412 C  CB  . PHE A 1 178 ? -23.902 1.249   11.646  1.00  17.31 ? 176 PHE B CB  1 
ATOM   1413 C  CG  . PHE A 1 178 ? -23.662 -0.052  10.905  1.00  16.98 ? 176 PHE B CG  1 
ATOM   1414 C  CD1 . PHE A 1 178 ? -23.951 -0.147  9.584   1.00  18.94 ? 176 PHE B CD1 1 
ATOM   1415 C  CD2 . PHE A 1 178 ? -23.144 -1.162  11.553  1.00  16.66 ? 176 PHE B CD2 1 
ATOM   1416 C  CE1 . PHE A 1 178 ? -23.732 -1.341  8.877   1.00  19.90 ? 176 PHE B CE1 1 
ATOM   1417 C  CE2 . PHE A 1 178 ? -22.920 -2.358  10.865  1.00  17.83 ? 176 PHE B CE2 1 
ATOM   1418 C  CZ  . PHE A 1 178 ? -23.244 -2.464  9.530   1.00  19.55 ? 176 PHE B CZ  1 
ATOM   1419 N  N   . THR A 1 179 ? -26.870 -0.315  12.825  1.00  16.16 ? 177 THR B N   1 
ATOM   1420 C  CA  . THR A 1 179 ? -27.266 -1.341  13.848  1.00  18.95 ? 177 THR B CA  1 
ATOM   1421 C  C   . THR A 1 179 ? -27.906 -2.553  13.186  1.00  19.17 ? 177 THR B C   1 
ATOM   1422 O  O   . THR A 1 179 ? -27.938 -2.600  11.967  1.00  20.06 ? 177 THR B O   1 
ATOM   1423 C  CB  . THR A 1 179 ? -28.138 -0.734  14.977  1.00  20.61 ? 177 THR B CB  1 
ATOM   1424 O  OG1 . THR A 1 179 ? -28.237 -1.710  16.049  1.00  19.49 ? 177 THR B OG1 1 
ATOM   1425 C  CG2 . THR A 1 179 ? -29.535 -0.367  14.420  1.00  21.60 ? 177 THR B CG2 1 
ATOM   1426 N  N   . ASN A 1 180 ? -28.395 -3.535  13.962  1.00  19.95 ? 178 ASN B N   1 
ATOM   1427 C  CA  . ASN A 1 180 ? -28.872 -4.790  13.396  1.00  21.50 ? 178 ASN B CA  1 
ATOM   1428 C  C   . ASN A 1 180 ? -27.816 -5.461  12.513  1.00  20.63 ? 178 ASN B C   1 
ATOM   1429 O  O   . ASN A 1 180 ? -28.068 -5.752  11.347  1.00  22.15 ? 178 ASN B O   1 
ATOM   1430 C  CB  . ASN A 1 180 ? -30.139 -4.560  12.556  1.00  23.66 ? 178 ASN B CB  1 
ATOM   1431 C  CG  . ASN A 1 180 ? -30.792 -5.892  12.132  1.00  32.32 ? 178 ASN B CG  1 
ATOM   1432 O  OD1 . ASN A 1 180 ? -31.390 -6.012  11.030  1.00  35.66 ? 178 ASN B OD1 1 
ATOM   1433 N  ND2 . ASN A 1 180 ? -30.632 -6.916  12.991  1.00  25.03 ? 178 ASN B ND2 1 
ATOM   1434 N  N   . PHE A 1 181 ? -26.638 -5.728  13.086  1.00  17.39 ? 179 PHE B N   1 
ATOM   1435 C  CA  . PHE A 1 181 ? -25.539 -6.284  12.296  1.00  17.51 ? 179 PHE B CA  1 
ATOM   1436 C  C   . PHE A 1 181 ? -25.284 -7.702  12.846  1.00  15.67 ? 179 PHE B C   1 
ATOM   1437 O  O   . PHE A 1 181 ? -24.908 -7.850  13.988  1.00  16.64 ? 179 PHE B O   1 
ATOM   1438 C  CB  . PHE A 1 181 ? -24.292 -5.397  12.478  1.00  16.73 ? 179 PHE B CB  1 
ATOM   1439 C  CG  . PHE A 1 181 ? -23.033 -5.915  11.804  1.00  18.33 ? 179 PHE B CG  1 
ATOM   1440 C  CD1 . PHE A 1 181 ? -23.044 -6.297  10.480  1.00  23.48 ? 179 PHE B CD1 1 
ATOM   1441 C  CD2 . PHE A 1 181 ? -21.805 -5.942  12.527  1.00  20.99 ? 179 PHE B CD2 1 
ATOM   1442 C  CE1 . PHE A 1 181 ? -21.866 -6.755  9.840   1.00  22.15 ? 179 PHE B CE1 1 
ATOM   1443 C  CE2 . PHE A 1 181 ? -20.616 -6.388  11.914  1.00  25.12 ? 179 PHE B CE2 1 
ATOM   1444 C  CZ  . PHE A 1 181 ? -20.657 -6.805  10.552  1.00  22.69 ? 179 PHE B CZ  1 
ATOM   1445 N  N   . ASP A 1 182 ? -25.523 -8.737  12.038  1.00  16.13 ? 180 ASP B N   1 
ATOM   1446 C  CA  . ASP A 1 182 ? -25.546 -10.103 12.619  1.00  15.24 ? 180 ASP B CA  1 
ATOM   1447 C  C   . ASP A 1 182 ? -24.113 -10.645 12.417  1.00  15.15 ? 180 ASP B C   1 
ATOM   1448 O  O   . ASP A 1 182 ? -23.786 -11.357 11.424  1.00  15.07 ? 180 ASP B O   1 
ATOM   1449 C  CB  . ASP A 1 182 ? -26.577 -10.940 11.836  1.00  16.46 ? 180 ASP B CB  1 
ATOM   1450 C  CG  . ASP A 1 182 ? -26.771 -12.371 12.413  1.00  18.69 ? 180 ASP B CG  1 
ATOM   1451 O  OD1 . ASP A 1 182 ? -26.001 -12.833 13.251  1.00  15.53 ? 180 ASP B OD1 1 
ATOM   1452 O  OD2 . ASP A 1 182 ? -27.673 -13.089 11.902  1.00  17.69 ? 180 ASP B OD2 1 
ATOM   1453 N  N   . LEU A 1 183 ? -23.264 -10.273 13.356  1.00  13.84 ? 181 LEU B N   1 
ATOM   1454 C  CA  . LEU A 1 183 ? -21.855 -10.596 13.216  1.00  11.79 ? 181 LEU B CA  1 
ATOM   1455 C  C   . LEU A 1 183 ? -21.665 -12.113 13.331  1.00  12.44 ? 181 LEU B C   1 
ATOM   1456 O  O   . LEU A 1 183 ? -20.787 -12.668 12.714  1.00  11.22 ? 181 LEU B O   1 
ATOM   1457 C  CB  . LEU A 1 183 ? -21.120 -9.800  14.319  1.00  12.19 ? 181 LEU B CB  1 
ATOM   1458 C  CG  . LEU A 1 183 ? -19.612 -9.962  14.400  1.00  12.45 ? 181 LEU B CG  1 
ATOM   1459 C  CD1 . LEU A 1 183 ? -18.884 -9.647  13.089  1.00  12.05 ? 181 LEU B CD1 1 
ATOM   1460 C  CD2 . LEU A 1 183 ? -19.059 -9.189  15.644  1.00  12.57 ? 181 LEU B CD2 1 
ATOM   1461 N  N   . LEU A 1 184 ? -22.503 -12.789 14.134  1.00  13.57 ? 182 LEU B N   1 
ATOM   1462 C  CA  . LEU A 1 184 ? -22.353 -14.228 14.284  1.00  13.03 ? 182 LEU B CA  1 
ATOM   1463 C  C   . LEU A 1 184 ? -22.516 -14.943 12.913  1.00  12.55 ? 182 LEU B C   1 
ATOM   1464 O  O   . LEU A 1 184 ? -21.712 -15.890 12.615  1.00  13.08 ? 182 LEU B O   1 
ATOM   1465 C  CB  . LEU A 1 184 ? -23.412 -14.766 15.261  1.00  12.44 ? 182 LEU B CB  1 
ATOM   1466 C  CG  . LEU A 1 184 ? -23.167 -16.236 15.627  1.00  15.61 ? 182 LEU B CG  1 
ATOM   1467 C  CD1 . LEU A 1 184 ? -21.777 -16.408 16.198  1.00  15.45 ? 182 LEU B CD1 1 
ATOM   1468 C  CD2 . LEU A 1 184 ? -24.224 -16.741 16.600  1.00  13.34 ? 182 LEU B CD2 1 
ATOM   1469 N  N   A SER A 1 185 ? -23.511 -14.528 12.104  0.50  12.97 ? 183 SER B N   1 
ATOM   1470 N  N   B SER A 1 185 ? -23.514 -14.510 12.107  0.50  12.93 ? 183 SER B N   1 
ATOM   1471 C  CA  A SER A 1 185 ? -23.728 -15.165 10.798  0.50  12.42 ? 183 SER B CA  1 
ATOM   1472 C  CA  B SER A 1 185 ? -23.781 -15.107 10.780  0.50  12.45 ? 183 SER B CA  1 
ATOM   1473 C  C   A SER A 1 185 ? -22.641 -14.830 9.779   0.50  12.74 ? 183 SER B C   1 
ATOM   1474 C  C   B SER A 1 185 ? -22.742 -14.735 9.710   0.50  12.90 ? 183 SER B C   1 
ATOM   1475 O  O   A SER A 1 185 ? -22.447 -15.568 8.812   0.50  12.84 ? 183 SER B O   1 
ATOM   1476 O  O   B SER A 1 185 ? -22.675 -15.351 8.639   0.50  13.87 ? 183 SER B O   1 
ATOM   1477 C  CB  A SER A 1 185 ? -25.079 -14.773 10.164  0.50  13.96 ? 183 SER B CB  1 
ATOM   1478 C  CB  B SER A 1 185 ? -25.162 -14.696 10.211  0.50  13.65 ? 183 SER B CB  1 
ATOM   1479 O  OG  A SER A 1 185 ? -26.112 -15.180 11.014  0.50  14.11 ? 183 SER B OG  1 
ATOM   1480 O  OG  B SER A 1 185 ? -25.181 -13.313 9.880   0.50  12.97 ? 183 SER B OG  1 
ATOM   1481 N  N   . LEU A 1 186 ? -21.957 -13.726 9.999   1.00  11.60 ? 184 LEU B N   1 
ATOM   1482 C  CA  . LEU A 1 186 ? -20.861 -13.318 9.086   1.00  11.82 ? 184 LEU B CA  1 
ATOM   1483 C  C   . LEU A 1 186 ? -19.641 -14.290 9.161   1.00  11.24 ? 184 LEU B C   1 
ATOM   1484 O  O   . LEU A 1 186 ? -18.894 -14.508 8.148   1.00  11.57 ? 184 LEU B O   1 
ATOM   1485 C  CB  . LEU A 1 186 ? -20.460 -11.854 9.463   1.00  10.79 ? 184 LEU B CB  1 
ATOM   1486 C  CG  . LEU A 1 186 ? -19.348 -11.302 8.580   1.00  12.81 ? 184 LEU B CG  1 
ATOM   1487 C  CD1 . LEU A 1 186 ? -19.907 -11.006 7.151   1.00  12.83 ? 184 LEU B CD1 1 
ATOM   1488 C  CD2 . LEU A 1 186 ? -18.730 -10.023 9.229   1.00  12.52 ? 184 LEU B CD2 1 
ATOM   1489 N  N   . LEU A 1 187 ? -19.438 -14.926 10.307  1.00  10.76 ? 185 LEU B N   1 
ATOM   1490 C  CA  . LEU A 1 187 ? -18.300 -15.825 10.459  1.00  9.56  ? 185 LEU B CA  1 
ATOM   1491 C  C   . LEU A 1 187 ? -18.355 -17.031 9.504   1.00  9.59  ? 185 LEU B C   1 
ATOM   1492 O  O   . LEU A 1 187 ? -19.451 -17.455 9.100   1.00  10.19 ? 185 LEU B O   1 
ATOM   1493 C  CB  . LEU A 1 187 ? -18.207 -16.338 11.964  1.00  8.68  ? 185 LEU B CB  1 
ATOM   1494 C  CG  . LEU A 1 187 ? -18.081 -15.131 12.900  1.00  10.55 ? 185 LEU B CG  1 
ATOM   1495 C  CD1 . LEU A 1 187 ? -17.970 -15.709 14.329  1.00  10.23 ? 185 LEU B CD1 1 
ATOM   1496 C  CD2 . LEU A 1 187 ? -16.855 -14.199 12.596  1.00  11.40 ? 185 LEU B CD2 1 
ATOM   1497 N  N   . PRO A 1 188 ? -17.189 -17.606 9.114   1.00  9.03  ? 186 PRO B N   1 
ATOM   1498 C  CA  . PRO A 1 188 ? -17.185 -18.766 8.206   1.00  8.42  ? 186 PRO B CA  1 
ATOM   1499 C  C   . PRO A 1 188 ? -17.818 -20.023 8.812   1.00  9.88  ? 186 PRO B C   1 
ATOM   1500 O  O   . PRO A 1 188 ? -17.967 -20.081 10.016  1.00  10.42 ? 186 PRO B O   1 
ATOM   1501 C  CB  . PRO A 1 188 ? -15.657 -18.976 7.890   1.00  8.78  ? 186 PRO B CB  1 
ATOM   1502 C  CG  . PRO A 1 188 ? -14.945 -18.370 9.140   1.00  9.29  ? 186 PRO B CG  1 
ATOM   1503 C  CD  . PRO A 1 188 ? -15.848 -17.229 9.555   1.00  8.76  ? 186 PRO B CD  1 
ATOM   1504 N  N   . PRO A 1 189 ? -18.112 -21.021 8.021   1.00  10.54 ? 187 PRO B N   1 
ATOM   1505 C  CA  . PRO A 1 189 ? -18.657 -22.291 8.580   1.00  10.97 ? 187 PRO B CA  1 
ATOM   1506 C  C   . PRO A 1 189 ? -17.767 -22.919 9.694   1.00  11.80 ? 187 PRO B C   1 
ATOM   1507 O  O   . PRO A 1 189 ? -18.288 -23.329 10.756  1.00  13.43 ? 187 PRO B O   1 
ATOM   1508 C  CB  . PRO A 1 189 ? -18.798 -23.196 7.322   1.00  11.13 ? 187 PRO B CB  1 
ATOM   1509 C  CG  . PRO A 1 189 ? -18.925 -22.230 6.201   1.00  11.09 ? 187 PRO B CG  1 
ATOM   1510 C  CD  . PRO A 1 189 ? -18.090 -21.012 6.540   1.00  10.57 ? 187 PRO B CD  1 
ATOM   1511 N  N   . SER A 1 190 ? -16.466 -23.021 9.460   1.00  10.74 ? 188 SER B N   1 
ATOM   1512 C  CA  . SER A 1 190 ? -15.537 -23.651 10.398  1.00  11.03 ? 188 SER B CA  1 
ATOM   1513 C  C   . SER A 1 190 ? -14.882 -22.599 11.265  1.00  11.64 ? 188 SER B C   1 
ATOM   1514 O  O   . SER A 1 190 ? -14.468 -21.514 10.765  1.00  10.27 ? 188 SER B O   1 
ATOM   1515 C  CB  . SER A 1 190 ? -14.406 -24.405 9.611   1.00  12.65 ? 188 SER B CB  1 
ATOM   1516 O  OG  . SER A 1 190 ? -13.489 -24.917 10.631  1.00  12.40 ? 188 SER B OG  1 
ATOM   1517 N  N   . TRP A 1 191 ? -14.912 -22.838 12.573  1.00  10.75 ? 189 TRP B N   1 
ATOM   1518 C  CA  . TRP A 1 191 ? -14.201 -21.939 13.525  1.00  10.77 ? 189 TRP B CA  1 
ATOM   1519 C  C   . TRP A 1 191 ? -12.895 -22.520 14.066  1.00  11.73 ? 189 TRP B C   1 
ATOM   1520 O  O   . TRP A 1 191 ? -12.401 -22.041 15.126  1.00  12.88 ? 189 TRP B O   1 
ATOM   1521 C  CB  . TRP A 1 191 ? -15.115 -21.564 14.654  1.00  11.11 ? 189 TRP B CB  1 
ATOM   1522 C  CG  . TRP A 1 191 ? -16.361 -20.800 14.174  1.00  11.10 ? 189 TRP B CG  1 
ATOM   1523 C  CD1 . TRP A 1 191 ? -16.601 -20.138 12.975  1.00  9.82  ? 189 TRP B CD1 1 
ATOM   1524 C  CD2 . TRP A 1 191 ? -17.551 -20.574 14.991  1.00  11.46 ? 189 TRP B CD2 1 
ATOM   1525 N  NE1 . TRP A 1 191 ? -17.879 -19.618 12.994  1.00  11.26 ? 189 TRP B NE1 1 
ATOM   1526 C  CE2 . TRP A 1 191 ? -18.471 -19.822 14.204  1.00  11.99 ? 189 TRP B CE2 1 
ATOM   1527 C  CE3 . TRP A 1 191 ? -17.901 -20.961 16.271  1.00  12.00 ? 189 TRP B CE3 1 
ATOM   1528 C  CZ2 . TRP A 1 191 ? -19.742 -19.457 14.687  1.00  13.87 ? 189 TRP B CZ2 1 
ATOM   1529 C  CZ3 . TRP A 1 191 ? -19.124 -20.625 16.771  1.00  12.49 ? 189 TRP B CZ3 1 
ATOM   1530 C  CH2 . TRP A 1 191 ? -20.070 -19.892 16.006  1.00  13.36 ? 189 TRP B CH2 1 
ATOM   1531 N  N   . ASP A 1 192 ? -12.306 -23.447 13.311  1.00  11.83 ? 190 ASP B N   1 
ATOM   1532 C  CA  . ASP A 1 192 ? -10.952 -23.912 13.603  1.00  12.07 ? 190 ASP B CA  1 
ATOM   1533 C  C   . ASP A 1 192 ? -9.994  -22.724 13.530  1.00  10.64 ? 190 ASP B C   1 
ATOM   1534 O  O   . ASP A 1 192 ? -10.111 -21.873 12.628  1.00  9.28  ? 190 ASP B O   1 
ATOM   1535 C  CB  . ASP A 1 192 ? -10.557 -25.038 12.678  1.00  17.27 ? 190 ASP B CB  1 
ATOM   1536 C  CG  . ASP A 1 192 ? -11.384 -26.362 13.020  1.00  16.52 ? 190 ASP B CG  1 
ATOM   1537 O  OD1 . ASP A 1 192 ? -12.153 -26.379 14.011  1.00  19.12 ? 190 ASP B OD1 1 
ATOM   1538 O  OD2 . ASP A 1 192 ? -11.396 -27.233 12.203  1.00  20.42 ? 190 ASP B OD2 1 
ATOM   1539 N  N   . TYR A 1 193 ? -9.009  -22.657 14.442  1.00  9.70  ? 191 TYR B N   1 
ATOM   1540 C  CA  . TYR A 1 193 ? -8.230  -21.433 14.550  1.00  8.70  ? 191 TYR B CA  1 
ATOM   1541 C  C   . TYR A 1 193 ? -6.791  -21.696 14.970  1.00  9.18  ? 191 TYR B C   1 
ATOM   1542 O  O   . TYR A 1 193 ? -6.480  -22.834 15.491  1.00  8.03  ? 191 TYR B O   1 
ATOM   1543 C  CB  . TYR A 1 193 ? -8.886  -20.370 15.566  1.00  8.43  ? 191 TYR B CB  1 
ATOM   1544 C  CG  . TYR A 1 193 ? -8.968  -20.940 17.011  1.00  9.26  ? 191 TYR B CG  1 
ATOM   1545 C  CD1 . TYR A 1 193 ? -7.887  -20.852 17.875  1.00  10.97 ? 191 TYR B CD1 1 
ATOM   1546 C  CD2 . TYR A 1 193 ? -10.062 -21.661 17.418  1.00  10.55 ? 191 TYR B CD2 1 
ATOM   1547 C  CE1 . TYR A 1 193 ? -7.921  -21.424 19.157  1.00  9.58  ? 191 TYR B CE1 1 
ATOM   1548 C  CE2 . TYR A 1 193 ? -10.119 -22.250 18.675  1.00  9.23  ? 191 TYR B CE2 1 
ATOM   1549 C  CZ  . TYR A 1 193 ? -9.047  -22.078 19.547  1.00  10.03 ? 191 TYR B CZ  1 
ATOM   1550 O  OH  . TYR A 1 193 ? -9.027  -22.666 20.804  1.00  10.60 ? 191 TYR B OH  1 
ATOM   1551 N  N   . TRP A 1 194 ? -5.947  -20.689 14.769  1.00  8.90  ? 192 TRP B N   1 
ATOM   1552 C  CA  . TRP A 1 194 ? -4.614  -20.646 15.356  1.00  9.40  ? 192 TRP B CA  1 
ATOM   1553 C  C   . TRP A 1 194 ? -4.596  -19.568 16.404  1.00  10.73 ? 192 TRP B C   1 
ATOM   1554 O  O   . TRP A 1 194 ? -5.332  -18.558 16.311  1.00  8.46  ? 192 TRP B O   1 
ATOM   1555 C  CB  . TRP A 1 194 ? -3.557  -20.255 14.320  1.00  9.17  ? 192 TRP B CB  1 
ATOM   1556 C  CG  . TRP A 1 194 ? -3.407  -21.229 13.141  1.00  9.21  ? 192 TRP B CG  1 
ATOM   1557 C  CD1 . TRP A 1 194 ? -2.845  -22.511 13.153  1.00  10.82 ? 192 TRP B CD1 1 
ATOM   1558 C  CD2 . TRP A 1 194 ? -3.873  -21.043 11.794  1.00  9.17  ? 192 TRP B CD2 1 
ATOM   1559 N  NE1 . TRP A 1 194 ? -2.910  -23.063 11.912  1.00  9.86  ? 192 TRP B NE1 1 
ATOM   1560 C  CE2 . TRP A 1 194 ? -3.512  -22.233 11.058  1.00  9.51  ? 192 TRP B CE2 1 
ATOM   1561 C  CE3 . TRP A 1 194 ? -4.583  -20.047 11.141  1.00  9.74  ? 192 TRP B CE3 1 
ATOM   1562 C  CZ2 . TRP A 1 194 ? -3.800  -22.386 9.682   1.00  9.42  ? 192 TRP B CZ2 1 
ATOM   1563 C  CZ3 . TRP A 1 194 ? -4.847  -20.203 9.755   1.00  8.94  ? 192 TRP B CZ3 1 
ATOM   1564 C  CH2 . TRP A 1 194 ? -4.453  -21.331 9.049   1.00  9.21  ? 192 TRP B CH2 1 
ATOM   1565 N  N   . THR A 1 195 ? -3.705  -19.697 17.403  1.00  8.82  ? 193 THR B N   1 
ATOM   1566 C  CA  . THR A 1 195 ? -3.674  -18.674 18.430  1.00  9.05  ? 193 THR B CA  1 
ATOM   1567 C  C   . THR A 1 195 ? -2.243  -18.418 18.898  1.00  8.95  ? 193 THR B C   1 
ATOM   1568 O  O   . THR A 1 195 ? -1.414  -19.411 18.953  1.00  9.13  ? 193 THR B O   1 
ATOM   1569 C  CB  . THR A 1 195 ? -4.592  -19.080 19.630  1.00  8.99  ? 193 THR B CB  1 
ATOM   1570 O  OG1 . THR A 1 195 ? -4.516  -18.045 20.664  1.00  9.67  ? 193 THR B OG1 1 
ATOM   1571 C  CG2 . THR A 1 195 ? -4.167  -20.449 20.290  1.00  10.47 ? 193 THR B CG2 1 
ATOM   1572 N  N   . TYR A 1 196 ? -1.939  -17.186 19.255  1.00  8.63  ? 194 TYR B N   1 
ATOM   1573 C  CA  . TYR A 1 196 ? -0.625  -16.849 19.807  1.00  9.08  ? 194 TYR B CA  1 
ATOM   1574 C  C   . TYR A 1 196 ? -0.744  -15.513 20.536  1.00  9.21  ? 194 TYR B C   1 
ATOM   1575 O  O   . TYR A 1 196 ? -1.710  -14.736 20.302  1.00  10.26 ? 194 TYR B O   1 
ATOM   1576 C  CB  . TYR A 1 196 ? 0.443   -16.761 18.677  1.00  8.95  ? 194 TYR B CB  1 
ATOM   1577 C  CG  . TYR A 1 196 ? 0.251   -15.492 17.803  1.00  8.87  ? 194 TYR B CG  1 
ATOM   1578 C  CD1 . TYR A 1 196 ? -0.736  -15.478 16.794  1.00  8.85  ? 194 TYR B CD1 1 
ATOM   1579 C  CD2 . TYR A 1 196 ? 1.039   -14.318 18.004  1.00  8.75  ? 194 TYR B CD2 1 
ATOM   1580 C  CE1 . TYR A 1 196 ? -0.903  -14.303 16.022  1.00  7.95  ? 194 TYR B CE1 1 
ATOM   1581 C  CE2 . TYR A 1 196 ? 0.873   -13.172 17.242  1.00  8.64  ? 194 TYR B CE2 1 
ATOM   1582 C  CZ  . TYR A 1 196 ? -0.117  -13.162 16.271  1.00  8.15  ? 194 TYR B CZ  1 
ATOM   1583 O  OH  . TYR A 1 196 ? -0.278  -12.029 15.476  1.00  9.46  ? 194 TYR B OH  1 
ATOM   1584 N  N   . PRO A 1 197 ? 0.222   -15.204 21.426  1.00  10.12 ? 195 PRO B N   1 
ATOM   1585 C  CA  . PRO A 1 197 ? 0.181   -13.945 22.206  1.00  10.08 ? 195 PRO B CA  1 
ATOM   1586 C  C   . PRO A 1 197 ? 0.841   -12.857 21.361  1.00  10.31 ? 195 PRO B C   1 
ATOM   1587 O  O   . PRO A 1 197 ? 1.967   -13.094 20.803  1.00  10.71 ? 195 PRO B O   1 
ATOM   1588 C  CB  . PRO A 1 197 ? 1.099   -14.259 23.427  1.00  10.11 ? 195 PRO B CB  1 
ATOM   1589 C  CG  . PRO A 1 197 ? 2.160   -15.337 22.882  1.00  10.70 ? 195 PRO B CG  1 
ATOM   1590 C  CD  . PRO A 1 197 ? 1.237   -16.187 21.934  1.00  9.94  ? 195 PRO B CD  1 
ATOM   1591 N  N   . GLY A 1 198 ? 0.159   -11.741 21.216  1.00  10.16 ? 196 GLY B N   1 
ATOM   1592 C  CA  . GLY A 1 198 ? 0.710   -10.630 20.425  1.00  10.25 ? 196 GLY B CA  1 
ATOM   1593 C  C   . GLY A 1 198 ? 0.266   -9.249  20.799  1.00  10.49 ? 196 GLY B C   1 
ATOM   1594 O  O   . GLY A 1 198 ? 0.063   -8.949  22.000  1.00  11.49 ? 196 GLY B O   1 
ATOM   1595 N  N   . SER A 1 199 ? 0.022   -8.405  19.780  1.00  9.10  ? 197 SER B N   1 
ATOM   1596 C  CA  . SER A 1 199 ? -0.164  -6.966  20.031  1.00  9.28  ? 197 SER B CA  1 
ATOM   1597 C  C   . SER A 1 199 ? -1.229  -6.346  19.147  1.00  9.86  ? 197 SER B C   1 
ATOM   1598 O  O   . SER A 1 199 ? -1.742  -6.965  18.209  1.00  9.07  ? 197 SER B O   1 
ATOM   1599 C  CB  . SER A 1 199 ? 1.176   -6.248  19.782  1.00  8.92  ? 197 SER B CB  1 
ATOM   1600 O  OG  . SER A 1 199 ? 1.313   -6.156  18.315  1.00  9.87  ? 197 SER B OG  1 
ATOM   1601 N  N   . LEU A 1 200 ? -1.592  -5.109  19.428  1.00  9.44  ? 198 LEU B N   1 
ATOM   1602 C  CA  . LEU A 1 200 ? -2.342  -4.331  18.496  1.00  11.15 ? 198 LEU B CA  1 
ATOM   1603 C  C   . LEU A 1 200 ? -1.456  -4.222  17.242  1.00  10.35 ? 198 LEU B C   1 
ATOM   1604 O  O   . LEU A 1 200 ? -0.244  -4.146  17.348  1.00  10.99 ? 198 LEU B O   1 
ATOM   1605 C  CB  . LEU A 1 200 ? -2.562  -2.874  18.973  1.00  10.83 ? 198 LEU B CB  1 
ATOM   1606 C  CG  . LEU A 1 200 ? -3.200  -2.615  20.311  1.00  15.05 ? 198 LEU B CG  1 
ATOM   1607 C  CD1 . LEU A 1 200 ? -3.502  -1.115  20.520  1.00  14.97 ? 198 LEU B CD1 1 
ATOM   1608 C  CD2 . LEU A 1 200 ? -4.266  -3.498  20.740  1.00  16.27 ? 198 LEU B CD2 1 
ATOM   1609 N  N   . THR A 1 201 ? -2.120  -4.179  16.074  1.00  9.19  ? 199 THR B N   1 
ATOM   1610 C  CA  . THR A 1 201 ? -1.339  -4.006  14.829  1.00  8.76  ? 199 THR B CA  1 
ATOM   1611 C  C   . THR A 1 201 ? -1.274  -2.595  14.358  1.00  9.67  ? 199 THR B C   1 
ATOM   1612 O  O   . THR A 1 201 ? -0.776  -2.321  13.264  1.00  9.63  ? 199 THR B O   1 
ATOM   1613 C  CB  . THR A 1 201 ? -1.900  -4.901  13.660  1.00  8.61  ? 199 THR B CB  1 
ATOM   1614 O  OG1 . THR A 1 201 ? -3.211  -4.432  13.218  1.00  8.46  ? 199 THR B OG1 1 
ATOM   1615 C  CG2 . THR A 1 201 ? -1.953  -6.335  14.152  1.00  9.24  ? 199 THR B CG2 1 
ATOM   1616 N  N   . VAL A 1 202 ? -1.753  -1.677  15.205  1.00  9.80  ? 200 VAL B N   1 
ATOM   1617 C  CA  . VAL A 1 202 ? -1.638  -0.236  14.943  1.00  10.26 ? 200 VAL B CA  1 
ATOM   1618 C  C   . VAL A 1 202 ? -1.054  0.425   16.181  1.00  11.17 ? 200 VAL B C   1 
ATOM   1619 O  O   . VAL A 1 202 ? -1.259  -0.070  17.286  1.00  10.92 ? 200 VAL B O   1 
ATOM   1620 C  CB  . VAL A 1 202 ? -2.995  0.378   14.643  1.00  11.27 ? 200 VAL B CB  1 
ATOM   1621 C  CG1 . VAL A 1 202 ? -3.564  -0.040  13.246  1.00  11.97 ? 200 VAL B CG1 1 
ATOM   1622 C  CG2 . VAL A 1 202 ? -4.013  0.193   15.789  1.00  12.11 ? 200 VAL B CG2 1 
ATOM   1623 N  N   . PRO A 1 203 ? -0.430  1.615   16.019  1.00  10.74 ? 201 PRO B N   1 
ATOM   1624 C  CA  . PRO A 1 203 ? -0.123  2.402   17.231  1.00  12.09 ? 201 PRO B CA  1 
ATOM   1625 C  C   . PRO A 1 203 ? -1.304  2.592   18.136  1.00  10.16 ? 201 PRO B C   1 
ATOM   1626 O  O   . PRO A 1 203 ? -2.445  2.918   17.700  1.00  11.37 ? 201 PRO B O   1 
ATOM   1627 C  CB  . PRO A 1 203 ? 0.400   3.741   16.646  1.00  11.99 ? 201 PRO B CB  1 
ATOM   1628 C  CG  . PRO A 1 203 ? 1.033   3.312   15.312  1.00  12.08 ? 201 PRO B CG  1 
ATOM   1629 C  CD  . PRO A 1 203 ? -0.035  2.358   14.767  1.00  11.73 ? 201 PRO B CD  1 
ATOM   1630 N  N   . PRO A 1 204 ? -1.062  2.398   19.466  1.00  12.17 ? 202 PRO B N   1 
ATOM   1631 C  CA  . PRO A 1 204 ? 0.214   2.273   20.226  1.00  12.42 ? 202 PRO B CA  1 
ATOM   1632 C  C   . PRO A 1 204 ? 0.893   0.915   20.350  1.00  12.48 ? 202 PRO B C   1 
ATOM   1633 O  O   . PRO A 1 204 ? 1.909   0.779   21.049  1.00  13.05 ? 202 PRO B O   1 
ATOM   1634 C  CB  . PRO A 1 204 ? -0.201  2.778   21.633  1.00  13.78 ? 202 PRO B CB  1 
ATOM   1635 C  CG  . PRO A 1 204 ? -1.591  2.259   21.777  1.00  13.26 ? 202 PRO B CG  1 
ATOM   1636 C  CD  . PRO A 1 204 ? -2.222  2.459   20.368  1.00  12.77 ? 202 PRO B CD  1 
ATOM   1637 N  N   . LEU A 1 205 ? 0.361   -0.116  19.623  1.00  11.64 ? 203 LEU B N   1 
ATOM   1638 C  CA  . LEU A 1 205 ? 1.048   -1.396  19.418  1.00  10.13 ? 203 LEU B CA  1 
ATOM   1639 C  C   . LEU A 1 205 ? 1.239   -2.176  20.717  1.00  9.94  ? 203 LEU B C   1 
ATOM   1640 O  O   . LEU A 1 205 ? 2.182   -2.956  20.863  1.00  10.89 ? 203 LEU B O   1 
ATOM   1641 C  CB  . LEU A 1 205 ? 2.432   -1.215  18.673  1.00  11.22 ? 203 LEU B CB  1 
ATOM   1642 C  CG  . LEU A 1 205 ? 2.294   -0.595  17.251  1.00  10.52 ? 203 LEU B CG  1 
ATOM   1643 C  CD1 . LEU A 1 205 ? 3.754   -0.114  16.872  1.00  10.92 ? 203 LEU B CD1 1 
ATOM   1644 C  CD2 . LEU A 1 205 ? 1.735   -1.613  16.244  1.00  10.77 ? 203 LEU B CD2 1 
ATOM   1645 N  N   . LEU A 1 206 ? 0.314   -1.970  21.635  1.00  10.64 ? 204 LEU B N   1 
ATOM   1646 C  CA  . LEU A 1 206 ? 0.440   -2.562  22.995  1.00  11.35 ? 204 LEU B CA  1 
ATOM   1647 C  C   . LEU A 1 206 ? 0.364   -4.114  22.881  1.00  11.33 ? 204 LEU B C   1 
ATOM   1648 O  O   . LEU A 1 206 ? -0.447  -4.672  22.129  1.00  10.92 ? 204 LEU B O   1 
ATOM   1649 C  CB  . LEU A 1 206 ? -0.667  -2.041  23.942  1.00  12.90 ? 204 LEU B CB  1 
ATOM   1650 C  CG  . LEU A 1 206 ? -0.760  -0.499  24.123  1.00  16.68 ? 204 LEU B CG  1 
ATOM   1651 C  CD1 . LEU A 1 206 ? -2.029  -0.005  24.857  1.00  16.91 ? 204 LEU B CD1 1 
ATOM   1652 C  CD2 . LEU A 1 206 ? 0.512   0.016   24.815  1.00  18.41 ? 204 LEU B CD2 1 
ATOM   1653 N  N   . GLU A 1 207 ? 1.150   -4.770  23.719  1.00  9.86  ? 205 GLU B N   1 
ATOM   1654 C  CA  . GLU A 1 207 ? 1.309   -6.212  23.723  1.00  10.58 ? 205 GLU B CA  1 
ATOM   1655 C  C   . GLU A 1 207 ? 0.311   -6.851  24.718  1.00  10.90 ? 205 GLU B C   1 
ATOM   1656 O  O   . GLU A 1 207 ? 0.699   -7.396  25.781  1.00  11.99 ? 205 GLU B O   1 
ATOM   1657 C  CB  . GLU A 1 207 ? 2.776   -6.520  24.042  1.00  10.84 ? 205 GLU B CB  1 
ATOM   1658 C  CG  . GLU A 1 207 ? 3.653   -6.016  22.888  1.00  11.84 ? 205 GLU B CG  1 
ATOM   1659 C  CD  . GLU A 1 207 ? 5.135   -6.425  22.967  1.00  13.52 ? 205 GLU B CD  1 
ATOM   1660 O  OE1 . GLU A 1 207 ? 5.659   -6.738  24.131  1.00  14.72 ? 205 GLU B OE1 1 
ATOM   1661 O  OE2 . GLU A 1 207 ? 5.776   -6.473  21.890  1.00  12.31 ? 205 GLU B OE2 1 
ATOM   1662 N  N   . SER A 1 208 ? -0.953  -6.696  24.395  1.00  11.41 ? 206 SER B N   1 
ATOM   1663 C  CA  . SER A 1 208 ? -2.069  -7.049  25.275  1.00  11.47 ? 206 SER B CA  1 
ATOM   1664 C  C   . SER A 1 208 ? -3.049  -7.996  24.617  1.00  9.87  ? 206 SER B C   1 
ATOM   1665 O  O   . SER A 1 208 ? -4.194  -8.181  25.136  1.00  10.58 ? 206 SER B O   1 
ATOM   1666 C  CB  . SER A 1 208 ? -2.794  -5.770  25.684  1.00  13.10 ? 206 SER B CB  1 
ATOM   1667 O  OG  . SER A 1 208 ? -3.238  -4.960  24.565  1.00  14.79 ? 206 SER B OG  1 
ATOM   1668 N  N   . VAL A 1 209 ? -2.675  -8.551  23.475  1.00  8.60  ? 207 VAL B N   1 
ATOM   1669 C  CA  . VAL A 1 209 ? -3.683  -9.273  22.651  1.00  8.55  ? 207 VAL B CA  1 
ATOM   1670 C  C   . VAL A 1 209 ? -3.464  -10.775 22.596  1.00  8.59  ? 207 VAL B C   1 
ATOM   1671 O  O   . VAL A 1 209 ? -2.385  -11.263 22.170  1.00  10.69 ? 207 VAL B O   1 
ATOM   1672 C  CB  . VAL A 1 209 ? -3.742  -8.706  21.193  1.00  7.69  ? 207 VAL B CB  1 
ATOM   1673 C  CG1 . VAL A 1 209 ? -4.782  -9.514  20.417  1.00  6.54  ? 207 VAL B CG1 1 
ATOM   1674 C  CG2 . VAL A 1 209 ? -4.164  -7.195  21.136  1.00  7.84  ? 207 VAL B CG2 1 
ATOM   1675 N  N   . THR A 1 210 ? -4.527  -11.549 22.904  1.00  8.40  ? 208 THR B N   1 
ATOM   1676 C  CA  . THR A 1 210 ? -4.580  -12.974 22.539  1.00  8.83  ? 208 THR B CA  1 
ATOM   1677 C  C   . THR A 1 210 ? -5.225  -13.067 21.144  1.00  8.60  ? 208 THR B C   1 
ATOM   1678 O  O   . THR A 1 210 ? -6.437  -12.795 21.001  1.00  8.56  ? 208 THR B O   1 
ATOM   1679 C  CB  . THR A 1 210 ? -5.466  -13.752 23.531  1.00  9.72  ? 208 THR B CB  1 
ATOM   1680 O  OG1 . THR A 1 210 ? -4.871  -13.633 24.837  1.00  10.69 ? 208 THR B OG1 1 
ATOM   1681 C  CG2 . THR A 1 210 ? -5.386  -15.284 23.233  1.00  8.75  ? 208 THR B CG2 1 
ATOM   1682 N  N   . TRP A 1 211 ? -4.407  -13.457 20.151  1.00  7.77  ? 209 TRP B N   1 
ATOM   1683 C  CA  . TRP A 1 211 ? -4.914  -13.520 18.807  1.00  7.69  ? 209 TRP B CA  1 
ATOM   1684 C  C   . TRP A 1 211 ? -5.533  -14.869 18.592  1.00  7.71  ? 209 TRP B C   1 
ATOM   1685 O  O   . TRP A 1 211 ? -4.967  -15.894 18.928  1.00  8.73  ? 209 TRP B O   1 
ATOM   1686 C  CB  . TRP A 1 211 ? -3.721  -13.323 17.823  1.00  7.43  ? 209 TRP B CB  1 
ATOM   1687 C  CG  . TRP A 1 211 ? -3.485  -11.854 17.593  1.00  8.34  ? 209 TRP B CG  1 
ATOM   1688 C  CD1 . TRP A 1 211 ? -2.590  -11.003 18.254  1.00  8.84  ? 209 TRP B CD1 1 
ATOM   1689 C  CD2 . TRP A 1 211 ? -4.255  -11.017 16.724  1.00  8.37  ? 209 TRP B CD2 1 
ATOM   1690 N  NE1 . TRP A 1 211 ? -2.750  -9.693  17.841  1.00  8.94  ? 209 TRP B NE1 1 
ATOM   1691 C  CE2 . TRP A 1 211 ? -3.746  -9.648  16.883  1.00  8.64  ? 209 TRP B CE2 1 
ATOM   1692 C  CE3 . TRP A 1 211 ? -5.345  -11.255 15.844  1.00  8.09  ? 209 TRP B CE3 1 
ATOM   1693 C  CZ2 . TRP A 1 211 ? -4.302  -8.568  16.186  1.00  9.21  ? 209 TRP B CZ2 1 
ATOM   1694 C  CZ3 . TRP A 1 211 ? -5.817  -10.173 15.076  1.00  8.09  ? 209 TRP B CZ3 1 
ATOM   1695 C  CH2 . TRP A 1 211 ? -5.367  -8.857  15.303  1.00  7.87  ? 209 TRP B CH2 1 
ATOM   1696 N  N   . ILE A 1 212 ? -6.682  -14.842 17.895  1.00  7.93  ? 210 ILE B N   1 
ATOM   1697 C  CA  . ILE A 1 212 ? -7.400  -16.056 17.464  1.00  8.27  ? 210 ILE B CA  1 
ATOM   1698 C  C   . ILE A 1 212 ? -7.691  -15.863 15.973  1.00  7.32  ? 210 ILE B C   1 
ATOM   1699 O  O   . ILE A 1 212 ? -8.544  -15.035 15.606  1.00  7.05  ? 210 ILE B O   1 
ATOM   1700 C  CB  . ILE A 1 212 ? -8.723  -16.196 18.313  1.00  7.84  ? 210 ILE B CB  1 
ATOM   1701 C  CG1 . ILE A 1 212 ? -8.434  -16.292 19.826  1.00  8.18  ? 210 ILE B CG1 1 
ATOM   1702 C  CG2 . ILE A 1 212 ? -9.544  -17.465 17.833  1.00  8.86  ? 210 ILE B CG2 1 
ATOM   1703 C  CD1 . ILE A 1 212 ? -9.732  -16.128 20.675  1.00  8.52  ? 210 ILE B CD1 1 
ATOM   1704 N  N   . VAL A 1 213 ? -6.921  -16.547 15.109  1.00  7.35  ? 211 VAL B N   1 
ATOM   1705 C  CA  . VAL A 1 213 ? -7.051  -16.291 13.685  1.00  7.44  ? 211 VAL B CA  1 
ATOM   1706 C  C   . VAL A 1 213 ? -7.712  -17.528 13.081  1.00  7.55  ? 211 VAL B C   1 
ATOM   1707 O  O   . VAL A 1 213 ? -7.168  -18.687 13.213  1.00  8.69  ? 211 VAL B O   1 
ATOM   1708 C  CB  . VAL A 1 213 ? -5.638  -16.090 13.057  1.00  7.82  ? 211 VAL B CB  1 
ATOM   1709 C  CG1 . VAL A 1 213 ? -5.732  -16.009 11.504  1.00  8.81  ? 211 VAL B CG1 1 
ATOM   1710 C  CG2 . VAL A 1 213 ? -4.870  -14.881 13.665  1.00  7.90  ? 211 VAL B CG2 1 
ATOM   1711 N  N   . LEU A 1 214 ? -8.914  -17.339 12.489  1.00  8.68  ? 212 LEU B N   1 
ATOM   1712 C  CA  . LEU A 1 214 ? -9.622  -18.467 11.868  1.00  8.79  ? 212 LEU B CA  1 
ATOM   1713 C  C   . LEU A 1 214 ? -8.990  -18.876 10.559  1.00  8.62  ? 212 LEU B C   1 
ATOM   1714 O  O   . LEU A 1 214 ? -8.579  -18.042 9.751   1.00  8.69  ? 212 LEU B O   1 
ATOM   1715 C  CB  . LEU A 1 214 ? -11.092 -18.079 11.516  1.00  8.19  ? 212 LEU B CB  1 
ATOM   1716 C  CG  . LEU A 1 214 ? -11.945 -17.579 12.696  1.00  9.55  ? 212 LEU B CG  1 
ATOM   1717 C  CD1 . LEU A 1 214 ? -13.469 -17.544 12.378  1.00  9.24  ? 212 LEU B CD1 1 
ATOM   1718 C  CD2 . LEU A 1 214 ? -11.846 -18.568 13.813  1.00  10.67 ? 212 LEU B CD2 1 
ATOM   1719 N  N   . LYS A 1 215 ? -8.875  -20.186 10.390  1.00  8.65  ? 213 LYS B N   1 
ATOM   1720 C  CA  . LYS A 1 215 ? -8.326  -20.742 9.156   1.00  9.48  ? 213 LYS B CA  1 
ATOM   1721 C  C   . LYS A 1 215 ? -9.188  -20.453 7.907   1.00  9.27  ? 213 LYS B C   1 
ATOM   1722 O  O   . LYS A 1 215 ? -8.621  -20.142 6.810   1.00  10.89 ? 213 LYS B O   1 
ATOM   1723 C  CB  . LYS A 1 215 ? -8.111  -22.269 9.301   1.00  9.18  ? 213 LYS B CB  1 
ATOM   1724 C  CG  . LYS A 1 215 ? -7.606  -22.903 7.977   1.00  11.24 ? 213 LYS B CG  1 
ATOM   1725 C  CD  . LYS A 1 215 ? -7.208  -24.368 8.238   1.00  12.83 ? 213 LYS B CD  1 
ATOM   1726 C  CE  . LYS A 1 215 ? -7.037  -25.116 6.915   1.00  15.89 ? 213 LYS B CE  1 
ATOM   1727 N  NZ  . LYS A 1 215 ? -6.433  -26.424 7.250   1.00  20.45 ? 213 LYS B NZ  1 
ATOM   1728 N  N   . GLN A 1 216 ? -10.503 -20.590 8.029   1.00  9.15  ? 214 GLN B N   1 
ATOM   1729 C  CA  . GLN A 1 216 ? -11.343 -20.515 6.805   1.00  9.59  ? 214 GLN B CA  1 
ATOM   1730 C  C   . GLN A 1 216 ? -11.703 -19.074 6.459   1.00  9.39  ? 214 GLN B C   1 
ATOM   1731 O  O   . GLN A 1 216 ? -12.273 -18.371 7.301   1.00  9.08  ? 214 GLN B O   1 
ATOM   1732 C  CB  . GLN A 1 216 ? -12.641 -21.300 7.027   1.00  10.38 ? 214 GLN B CB  1 
ATOM   1733 C  CG  . GLN A 1 216 ? -13.441 -21.290 5.729   1.00  11.19 ? 214 GLN B CG  1 
ATOM   1734 C  CD  . GLN A 1 216 ? -14.693 -22.233 5.719   1.00  14.42 ? 214 GLN B CD  1 
ATOM   1735 O  OE1 . GLN A 1 216 ? -15.236 -22.528 4.599   1.00  18.40 ? 214 GLN B OE1 1 
ATOM   1736 N  NE2 . GLN A 1 216 ? -15.118 -22.729 6.838   1.00  10.90 ? 214 GLN B NE2 1 
ATOM   1737 N  N   . PRO A 1 217 ? -11.396 -18.622 5.232   1.00  9.25  ? 215 PRO B N   1 
ATOM   1738 C  CA  . PRO A 1 217 ? -11.826 -17.240 4.885   1.00  9.44  ? 215 PRO B CA  1 
ATOM   1739 C  C   . PRO A 1 217 ? -13.350 -17.109 4.546   1.00  9.27  ? 215 PRO B C   1 
ATOM   1740 O  O   . PRO A 1 217 ? -14.027 -18.137 4.354   1.00  10.61 ? 215 PRO B O   1 
ATOM   1741 C  CB  . PRO A 1 217 ? -11.118 -16.980 3.521   1.00  10.34 ? 215 PRO B CB  1 
ATOM   1742 C  CG  . PRO A 1 217 ? -10.119 -18.092 3.387   1.00  14.24 ? 215 PRO B CG  1 
ATOM   1743 C  CD  . PRO A 1 217 ? -10.660 -19.298 4.120   1.00  10.67 ? 215 PRO B CD  1 
ATOM   1744 N  N   . ILE A 1 218 ? -13.842 -15.864 4.592   1.00  8.67  ? 216 ILE B N   1 
ATOM   1745 C  CA  . ILE A 1 218 ? -15.173 -15.531 4.048   1.00  8.83  ? 216 ILE B CA  1 
ATOM   1746 C  C   . ILE A 1 218 ? -15.001 -14.838 2.712   1.00  10.06 ? 216 ILE B C   1 
ATOM   1747 O  O   . ILE A 1 218 ? -13.878 -14.451 2.340   1.00  10.38 ? 216 ILE B O   1 
ATOM   1748 C  CB  . ILE A 1 218 ? -16.025 -14.763 5.050   1.00  8.93  ? 216 ILE B CB  1 
ATOM   1749 C  CG1 . ILE A 1 218 ? -15.455 -13.364 5.336   1.00  9.62  ? 216 ILE B CG1 1 
ATOM   1750 C  CG2 . ILE A 1 218 ? -16.108 -15.557 6.400   1.00  8.77  ? 216 ILE B CG2 1 
ATOM   1751 C  CD1 . ILE A 1 218 ? -16.343 -12.446 6.141   1.00  12.32 ? 216 ILE B CD1 1 
ATOM   1752 N  N   A ASN A 1 219 ? -16.092 -14.727 1.952   0.50  10.38 ? 217 ASN B N   1 
ATOM   1753 N  N   B ASN A 1 219 ? -16.129 -14.721 1.988   0.50  9.66  ? 217 ASN B N   1 
ATOM   1754 C  CA  A ASN A 1 219 ? -15.968 -14.115 0.616   0.50  11.01 ? 217 ASN B CA  1 
ATOM   1755 C  CA  B ASN A 1 219 ? -16.144 -14.080 0.648   0.50  10.01 ? 217 ASN B CA  1 
ATOM   1756 C  C   A ASN A 1 219 ? -16.454 -12.655 0.587   0.50  10.81 ? 217 ASN B C   1 
ATOM   1757 C  C   B ASN A 1 219 ? -16.381 -12.575 0.701   0.50  9.99  ? 217 ASN B C   1 
ATOM   1758 O  O   A ASN A 1 219 ? -17.363 -12.263 1.312   0.50  10.40 ? 217 ASN B O   1 
ATOM   1759 O  O   B ASN A 1 219 ? -17.046 -12.077 1.593   0.50  9.66  ? 217 ASN B O   1 
ATOM   1760 C  CB  A ASN A 1 219 ? -16.700 -14.971 -0.461  0.50  14.11 ? 217 ASN B CB  1 
ATOM   1761 C  CB  B ASN A 1 219 ? -17.224 -14.744 -0.285  0.50  11.24 ? 217 ASN B CB  1 
ATOM   1762 C  CG  A ASN A 1 219 ? -16.196 -16.395 -0.530  0.50  16.04 ? 217 ASN B CG  1 
ATOM   1763 C  CG  B ASN A 1 219 ? -18.611 -14.763 0.336   0.50  12.11 ? 217 ASN B CG  1 
ATOM   1764 O  OD1 A ASN A 1 219 ? -16.867 -17.332 -0.064  0.50  24.83 ? 217 ASN B OD1 1 
ATOM   1765 O  OD1 B ASN A 1 219 ? -19.630 -14.235 -0.232  0.50  12.17 ? 217 ASN B OD1 1 
ATOM   1766 N  ND2 A ASN A 1 219 ? -15.023 -16.590 -1.094  0.50  16.62 ? 217 ASN B ND2 1 
ATOM   1767 N  ND2 B ASN A 1 219 ? -18.685 -15.338 1.546   0.50  12.11 ? 217 ASN B ND2 1 
ATOM   1768 N  N   . ILE A 1 220 ? -15.843 -11.848 -0.288  1.00  9.46  ? 218 ILE B N   1 
ATOM   1769 C  CA  . ILE A 1 220 ? -16.259 -10.503 -0.582  1.00  8.73  ? 218 ILE B CA  1 
ATOM   1770 C  C   . ILE A 1 220 ? -16.063 -10.315 -2.108  1.00  8.91  ? 218 ILE B C   1 
ATOM   1771 O  O   . ILE A 1 220 ? -15.185 -10.985 -2.725  1.00  9.14  ? 218 ILE B O   1 
ATOM   1772 C  CB  . ILE A 1 220 ? -15.433 -9.446  0.255   1.00  8.36  ? 218 ILE B CB  1 
ATOM   1773 C  CG1 . ILE A 1 220 ? -15.966 -8.018  0.031   1.00  9.00  ? 218 ILE B CG1 1 
ATOM   1774 C  CG2 . ILE A 1 220 ? -13.926 -9.514  -0.107  1.00  8.56  ? 218 ILE B CG2 1 
ATOM   1775 C  CD1 . ILE A 1 220 ? -15.350 -6.945  0.955   1.00  9.62  ? 218 ILE B CD1 1 
ATOM   1776 N  N   . SER A 1 221 ? -16.899 -9.492  -2.762  1.00  9.36  ? 219 SER B N   1 
ATOM   1777 C  CA  . SER A 1 221 ? -16.593 -9.295  -4.201  1.00  9.20  ? 219 SER B CA  1 
ATOM   1778 C  C   . SER A 1 221 ? -15.479 -8.295  -4.386  1.00  9.77  ? 219 SER B C   1 
ATOM   1779 O  O   . SER A 1 221 ? -15.271 -7.480  -3.476  1.00  8.61  ? 219 SER B O   1 
ATOM   1780 C  CB  . SER A 1 221 ? -17.820 -8.780  -4.986  1.00  8.38  ? 219 SER B CB  1 
ATOM   1781 O  OG  . SER A 1 221 ? -18.240 -7.473  -4.592  1.00  9.27  ? 219 SER B OG  1 
ATOM   1782 N  N   . SER A 1 222 ? -14.811 -8.299  -5.558  1.00  10.28 ? 220 SER B N   1 
ATOM   1783 C  CA  . SER A 1 222 ? -13.812 -7.220  -5.811  1.00  11.37 ? 220 SER B CA  1 
ATOM   1784 C  C   . SER A 1 222 ? -14.445 -5.834  -5.736  1.00  10.30 ? 220 SER B C   1 
ATOM   1785 O  O   . SER A 1 222 ? -13.807 -4.924  -5.226  1.00  10.24 ? 220 SER B O   1 
ATOM   1786 C  CB  . SER A 1 222 ? -13.061 -7.388  -7.140  1.00  11.69 ? 220 SER B CB  1 
ATOM   1787 O  OG  . SER A 1 222 ? -14.070 -7.411  -8.156  1.00  19.06 ? 220 SER B OG  1 
ATOM   1788 N  N   . GLN A 1 223 ? -15.712 -5.672  -6.216  1.00  10.41 ? 221 GLN B N   1 
ATOM   1789 C  CA  . GLN A 1 223 ? -16.361 -4.327  -6.163  1.00  11.00 ? 221 GLN B CA  1 
ATOM   1790 C  C   . GLN A 1 223 ? -16.656 -3.811  -4.756  1.00  11.05 ? 221 GLN B C   1 
ATOM   1791 O  O   . GLN A 1 223 ? -16.396 -2.620  -4.454  1.00  11.82 ? 221 GLN B O   1 
ATOM   1792 C  CB  . GLN A 1 223 ? -17.635 -4.293  -7.063  1.00  11.79 ? 221 GLN B CB  1 
ATOM   1793 C  CG  . GLN A 1 223 ? -17.291 -4.503  -8.560  1.00  13.88 ? 221 GLN B CG  1 
ATOM   1794 C  CD  . GLN A 1 223 ? -17.219 -5.943  -9.029  1.00  16.27 ? 221 GLN B CD  1 
ATOM   1795 O  OE1 . GLN A 1 223 ? -17.074 -6.198  -10.258 1.00  19.34 ? 221 GLN B OE1 1 
ATOM   1796 N  NE2 . GLN A 1 223 ? -17.359 -6.916  -8.121  1.00  12.99 ? 221 GLN B NE2 1 
ATOM   1797 N  N   . GLN A 1 224 ? -17.125 -4.708  -3.875  1.00  10.12 ? 222 GLN B N   1 
ATOM   1798 C  CA  . GLN A 1 224 ? -17.358 -4.360  -2.463  1.00  9.48  ? 222 GLN B CA  1 
ATOM   1799 C  C   . GLN A 1 224 ? -16.013 -3.978  -1.785  1.00  9.13  ? 222 GLN B C   1 
ATOM   1800 O  O   . GLN A 1 224 ? -15.912 -2.944  -1.107  1.00  10.60 ? 222 GLN B O   1 
ATOM   1801 C  CB  . GLN A 1 224 ? -17.889 -5.541  -1.704  1.00  10.46 ? 222 GLN B CB  1 
ATOM   1802 C  CG  . GLN A 1 224 ? -19.386 -5.807  -2.032  1.00  9.70  ? 222 GLN B CG  1 
ATOM   1803 C  CD  . GLN A 1 224 ? -19.914 -7.040  -1.281  1.00  9.81  ? 222 GLN B CD  1 
ATOM   1804 O  OE1 . GLN A 1 224 ? -19.231 -8.100  -1.193  1.00  11.01 ? 222 GLN B OE1 1 
ATOM   1805 N  NE2 . GLN A 1 224 ? -21.175 -6.906  -0.727  1.00  10.43 ? 222 GLN B NE2 1 
ATOM   1806 N  N   . LEU A 1 225 ? -14.982 -4.779  -2.065  1.00  8.27  ? 223 LEU B N   1 
ATOM   1807 C  CA  . LEU A 1 225 ? -13.647 -4.509  -1.382  1.00  8.34  ? 223 LEU B CA  1 
ATOM   1808 C  C   . LEU A 1 225 ? -13.147 -3.163  -1.871  1.00  9.52  ? 223 LEU B C   1 
ATOM   1809 O  O   . LEU A 1 225 ? -12.602 -2.372  -1.090  1.00  9.54  ? 223 LEU B O   1 
ATOM   1810 C  CB  . LEU A 1 225 ? -12.626 -5.578  -1.695  1.00  8.73  ? 223 LEU B CB  1 
ATOM   1811 C  CG  . LEU A 1 225 ? -11.285 -5.470  -0.917  1.00  8.50  ? 223 LEU B CG  1 
ATOM   1812 C  CD1 . LEU A 1 225 ? -11.408 -5.268  0.609   1.00  9.68  ? 223 LEU B CD1 1 
ATOM   1813 C  CD2 . LEU A 1 225 ? -10.408 -6.697  -1.210  1.00  8.53  ? 223 LEU B CD2 1 
ATOM   1814 N  N   . ALA A 1 226 ? -13.286 -2.903  -3.186  1.00  9.41  ? 224 ALA B N   1 
ATOM   1815 C  CA  . ALA A 1 226 ? -12.718 -1.659  -3.700  1.00  10.28 ? 224 ALA B CA  1 
ATOM   1816 C  C   . ALA A 1 226 ? -13.337 -0.420  -3.053  1.00  10.94 ? 224 ALA B C   1 
ATOM   1817 O  O   . ALA A 1 226 ? -12.694 0.638   -2.963  1.00  11.83 ? 224 ALA B O   1 
ATOM   1818 C  CB  . ALA A 1 226 ? -12.923 -1.612  -5.226  1.00  10.94 ? 224 ALA B CB  1 
ATOM   1819 N  N   . LYS A 1 227 ? -14.627 -0.466  -2.624  1.00  11.36 ? 225 LYS B N   1 
ATOM   1820 C  CA  . LYS A 1 227 ? -15.215 0.633   -1.981  1.00  12.02 ? 225 LYS B CA  1 
ATOM   1821 C  C   . LYS A 1 227 ? -14.461 1.113   -0.747  1.00  11.56 ? 225 LYS B C   1 
ATOM   1822 O  O   . LYS A 1 227 ? -14.471 2.318   -0.476  1.00  11.23 ? 225 LYS B O   1 
ATOM   1823 C  CB  . LYS A 1 227 ? -16.669 0.348   -1.623  1.00  14.77 ? 225 LYS B CB  1 
ATOM   1824 C  CG  . LYS A 1 227 ? -17.502 0.252   -2.877  1.00  20.76 ? 225 LYS B CG  1 
ATOM   1825 C  CD  . LYS A 1 227 ? -18.992 0.606   -2.639  1.00  24.38 ? 225 LYS B CD  1 
ATOM   1826 C  CE  . LYS A 1 227 ? -19.255 1.798   -1.754  1.00  24.27 ? 225 LYS B CE  1 
ATOM   1827 N  NZ  . LYS A 1 227 ? -19.695 3.061   -2.436  1.00  28.40 ? 225 LYS B NZ  1 
ATOM   1828 N  N   . PHE A 1 228 ? -13.849 0.205   0.025   1.00  10.12 ? 226 PHE B N   1 
ATOM   1829 C  CA  . PHE A 1 228 ? -13.110 0.680   1.206   1.00  9.65  ? 226 PHE B CA  1 
ATOM   1830 C  C   . PHE A 1 228 ? -11.899 1.591   0.899   1.00  10.57 ? 226 PHE B C   1 
ATOM   1831 O  O   . PHE A 1 228 ? -11.549 2.460   1.710   1.00  12.24 ? 226 PHE B O   1 
ATOM   1832 C  CB  . PHE A 1 228 ? -12.600 -0.511  2.049   1.00  9.76  ? 226 PHE B CB  1 
ATOM   1833 C  CG  . PHE A 1 228 ? -13.718 -1.316  2.647   1.00  10.04 ? 226 PHE B CG  1 
ATOM   1834 C  CD1 . PHE A 1 228 ? -14.122 -2.500  2.023   1.00  10.09 ? 226 PHE B CD1 1 
ATOM   1835 C  CD2 . PHE A 1 228 ? -14.460 -0.815  3.719   1.00  10.24 ? 226 PHE B CD2 1 
ATOM   1836 C  CE1 . PHE A 1 228 ? -15.295 -3.191  2.511   1.00  11.16 ? 226 PHE B CE1 1 
ATOM   1837 C  CE2 . PHE A 1 228 ? -15.546 -1.554  4.251   1.00  10.97 ? 226 PHE B CE2 1 
ATOM   1838 C  CZ  . PHE A 1 228 ? -15.973 -2.712  3.649   1.00  10.26 ? 226 PHE B CZ  1 
ATOM   1839 N  N   . ARG A 1 229 ? -11.311 1.414   -0.278  1.00  10.74 ? 227 ARG B N   1 
ATOM   1840 C  CA  . ARG A 1 229 ? -10.153 2.195   -0.682  1.00  10.11 ? 227 ARG B CA  1 
ATOM   1841 C  C   . ARG A 1 229 ? -10.520 3.632   -0.983  1.00  10.47 ? 227 ARG B C   1 
ATOM   1842 O  O   . ARG A 1 229 ? -9.582  4.447   -1.078  1.00  11.92 ? 227 ARG B O   1 
ATOM   1843 C  CB  . ARG A 1 229 ? -9.506  1.581   -1.945  1.00  9.52  ? 227 ARG B CB  1 
ATOM   1844 C  CG  . ARG A 1 229 ? -9.012  0.141   -1.671  1.00  9.96  ? 227 ARG B CG  1 
ATOM   1845 C  CD  . ARG A 1 229 ? -8.252  -0.380  -2.920  1.00  10.48 ? 227 ARG B CD  1 
ATOM   1846 N  NE  . ARG A 1 229 ? -7.856  -1.777  -2.702  1.00  9.63  ? 227 ARG B NE  1 
ATOM   1847 C  CZ  . ARG A 1 229 ? -8.465  -2.855  -3.235  1.00  10.34 ? 227 ARG B CZ  1 
ATOM   1848 N  NH1 . ARG A 1 229 ? -9.372  -2.723  -4.194  1.00  11.15 ? 227 ARG B NH1 1 
ATOM   1849 N  NH2 . ARG A 1 229 ? -8.060  -4.109  -2.918  1.00  10.87 ? 227 ARG B NH2 1 
ATOM   1850 N  N   A SER A 1 230 ? -11.815 3.933   -1.179  0.50  12.64 ? 228 SER B N   1 
ATOM   1851 N  N   B SER A 1 230 ? -11.829 3.886   -1.144  0.50  12.02 ? 228 SER B N   1 
ATOM   1852 C  CA  A SER A 1 230 ? -12.301 5.345   -1.342  0.50  13.31 ? 228 SER B CA  1 
ATOM   1853 C  CA  B SER A 1 230 ? -12.440 5.241   -1.302  0.50  12.29 ? 228 SER B CA  1 
ATOM   1854 C  C   A SER A 1 230 ? -12.321 6.164   -0.055  0.50  12.43 ? 228 SER B C   1 
ATOM   1855 C  C   B SER A 1 230 ? -12.645 6.076   -0.034  0.50  11.96 ? 228 SER B C   1 
ATOM   1856 O  O   A SER A 1 230 ? -12.313 7.405   -0.101  0.50  10.98 ? 228 SER B O   1 
ATOM   1857 O  O   B SER A 1 230 ? -13.049 7.245   -0.068  0.50  11.32 ? 228 SER B O   1 
ATOM   1858 C  CB  A SER A 1 230 ? -13.655 5.453   -2.070  0.50  16.16 ? 228 SER B CB  1 
ATOM   1859 C  CB  B SER A 1 230 ? -13.695 5.181   -2.173  0.50  13.96 ? 228 SER B CB  1 
ATOM   1860 O  OG  A SER A 1 230 ? -14.712 4.844   -1.338  0.50  16.36 ? 228 SER B OG  1 
ATOM   1861 O  OG  B SER A 1 230 ? -13.269 5.225   -3.511  0.50  12.91 ? 228 SER B OG  1 
ATOM   1862 N  N   . LEU A 1 231 ? -12.299 5.493   1.112   1.00  12.17 ? 229 LEU B N   1 
ATOM   1863 C  CA  . LEU A 1 231 ? -12.237 6.272   2.360   1.00  11.44 ? 229 LEU B CA  1 
ATOM   1864 C  C   . LEU A 1 231 ? -11.041 7.217   2.349   1.00  13.35 ? 229 LEU B C   1 
ATOM   1865 O  O   . LEU A 1 231 ? -9.939  6.832   1.871   1.00  12.24 ? 229 LEU B O   1 
ATOM   1866 C  CB  . LEU A 1 231 ? -12.104 5.272   3.531   1.00  11.39 ? 229 LEU B CB  1 
ATOM   1867 C  CG  . LEU A 1 231 ? -13.393 4.483   3.799   1.00  11.65 ? 229 LEU B CG  1 
ATOM   1868 C  CD1 . LEU A 1 231 ? -13.097 3.474   4.966   1.00  13.01 ? 229 LEU B CD1 1 
ATOM   1869 C  CD2 . LEU A 1 231 ? -14.539 5.433   4.194   1.00  12.28 ? 229 LEU B CD2 1 
ATOM   1870 N  N   . LEU A 1 232 ? -11.160 8.407   2.932   1.00  14.04 ? 230 LEU B N   1 
ATOM   1871 C  CA  . LEU A 1 232 ? -9.984  9.338   3.056   1.00  15.55 ? 230 LEU B CA  1 
ATOM   1872 C  C   . LEU A 1 232 ? -9.249  9.095   4.374   1.00  15.09 ? 230 LEU B C   1 
ATOM   1873 O  O   . LEU A 1 232 ? -9.879  8.725   5.388   1.00  16.09 ? 230 LEU B O   1 
ATOM   1874 C  CB  . LEU A 1 232 ? -10.458 10.796  2.964   1.00  16.06 ? 230 LEU B CB  1 
ATOM   1875 C  CG  . LEU A 1 232 ? -11.123 11.176  1.639   1.00  16.83 ? 230 LEU B CG  1 
ATOM   1876 C  CD1 . LEU A 1 232 ? -11.569 12.607  1.713   1.00  20.11 ? 230 LEU B CD1 1 
ATOM   1877 C  CD2 . LEU A 1 232 ? -10.206 10.899  0.432   1.00  21.33 ? 230 LEU B CD2 1 
ATOM   1878 N  N   . CYS A 1 233 ? -7.933  9.259   4.340   1.00  14.65 ? 231 CYS B N   1 
ATOM   1879 C  CA  . CYS A 1 233 ? -7.155  9.233   5.583   1.00  16.27 ? 231 CYS B CA  1 
ATOM   1880 C  C   . CYS A 1 233 ? -7.011  10.627  6.140   1.00  20.16 ? 231 CYS B C   1 
ATOM   1881 O  O   . CYS A 1 233 ? -6.345  10.825  7.150   1.00  17.61 ? 231 CYS B O   1 
ATOM   1882 C  CB  . CYS A 1 233 ? -5.773  8.530   5.502   1.00  17.64 ? 231 CYS B CB  1 
ATOM   1883 S  SG  . CYS A 1 233 ? -4.733  9.281   4.205   1.00  19.23 ? 231 CYS B SG  1 
ATOM   1884 N  N   . THR A 1 234 ? -7.610  11.553  5.432   1.00  19.05 ? 232 THR B N   1 
ATOM   1885 C  CA  . THR A 1 234 ? -7.466  13.000  5.727   1.00  23.83 ? 232 THR B CA  1 
ATOM   1886 C  C   . THR A 1 234 ? -8.897  13.545  6.104   1.00  21.09 ? 232 THR B C   1 
ATOM   1887 O  O   . THR A 1 234 ? -9.975  13.028  5.640   1.00  23.86 ? 232 THR B O   1 
ATOM   1888 C  CB  . THR A 1 234 ? -6.950  13.694  4.445   1.00  19.34 ? 232 THR B CB  1 
ATOM   1889 O  OG1 . THR A 1 234 ? -7.866  13.373  3.388   1.00  21.95 ? 232 THR B OG1 1 
ATOM   1890 C  CG2 . THR A 1 234 ? -5.547  13.349  4.031   1.00  21.12 ? 232 THR B CG2 1 
ATOM   1891 N  N   . ALA A 1 235 ? -8.934  14.581  6.960   1.00  29.51 ? 233 ALA B N   1 
ATOM   1892 C  CA  . ALA A 1 235 ? -10.207 15.203  7.435   1.00  28.26 ? 233 ALA B CA  1 
ATOM   1893 C  C   . ALA A 1 235 ? -10.813 16.226  6.445   1.00  36.54 ? 233 ALA B C   1 
ATOM   1894 O  O   . ALA A 1 235 ? -10.128 16.703  5.543   1.00  32.59 ? 233 ALA B O   1 
ATOM   1895 C  CB  . ALA A 1 235 ? -9.987  15.862  8.801   1.00  31.46 ? 233 ALA B CB  1 
ATOM   1896 N  N   . GLU A 1 236 ? -12.111 16.522  6.567   1.00  38.45 ? 234 GLU B N   1 
ATOM   1897 C  CA  . GLU A 1 236 ? -12.706 17.649  5.782   1.00  42.51 ? 234 GLU B CA  1 
ATOM   1898 C  C   . GLU A 1 236 ? -11.791 18.908  5.980   1.00  40.14 ? 234 GLU B C   1 
ATOM   1899 O  O   . GLU A 1 236 ? -11.376 19.198  7.103   1.00  38.52 ? 234 GLU B O   1 
ATOM   1900 C  CB  . GLU A 1 236 ? -14.183 17.888  6.184   1.00  43.31 ? 234 GLU B CB  1 
ATOM   1901 C  CG  . GLU A 1 236 ? -14.940 18.849  5.276   0.010 42.31 ? 234 GLU B CG  1 
ATOM   1902 C  CD  . GLU A 1 236 ? -15.328 18.232  3.944   0.010 42.18 ? 234 GLU B CD  1 
ATOM   1903 O  OE1 . GLU A 1 236 ? -14.972 18.809  2.895   0.010 41.95 ? 234 GLU B OE1 1 
ATOM   1904 O  OE2 . GLU A 1 236 ? -15.988 17.171  3.941   0.010 41.97 ? 234 GLU B OE2 1 
ATOM   1905 N  N   . GLY A 1 237 ? -11.404 19.584  4.889   1.00  43.76 ? 235 GLY B N   1 
ATOM   1906 C  CA  . GLY A 1 237 ? -10.526 20.759  4.986   1.00  43.91 ? 235 GLY B CA  1 
ATOM   1907 C  C   . GLY A 1 237 ? -9.021  20.542  4.876   1.00  48.17 ? 235 GLY B C   1 
ATOM   1908 O  O   . GLY A 1 237 ? -8.255  21.501  4.896   1.00  52.49 ? 235 GLY B O   1 
ATOM   1909 N  N   . GLU A 1 238 ? -8.596  19.284  4.757   1.00  47.49 ? 236 GLU B N   1 
ATOM   1910 C  CA  . GLU A 1 238 ? -7.177  18.880  4.557   1.00  43.27 ? 236 GLU B CA  1 
ATOM   1911 C  C   . GLU A 1 238 ? -7.008  18.469  3.055   1.00  40.47 ? 236 GLU B C   1 
ATOM   1912 O  O   . GLU A 1 238 ? -7.985  18.146  2.369   1.00  34.60 ? 236 GLU B O   1 
ATOM   1913 C  CB  . GLU A 1 238 ? -6.902  17.680  5.503   1.00  49.84 ? 236 GLU B CB  1 
ATOM   1914 C  CG  . GLU A 1 238 ? -5.464  17.313  5.909   1.00  46.95 ? 236 GLU B CG  1 
ATOM   1915 C  CD  . GLU A 1 238 ? -5.395  16.074  6.844   1.00  55.74 ? 236 GLU B CD  1 
ATOM   1916 O  OE1 . GLU A 1 238 ? -6.449  15.642  7.439   1.00  46.82 ? 236 GLU B OE1 1 
ATOM   1917 O  OE2 . GLU A 1 238 ? -4.271  15.502  6.987   1.00  48.19 ? 236 GLU B OE2 1 
ATOM   1918 N  N   . ALA A 1 239 ? -5.789  18.458  2.533   1.00  38.13 ? 237 ALA B N   1 
ATOM   1919 C  CA  . ALA A 1 239 ? -5.589  17.959  1.143   1.00  36.83 ? 237 ALA B CA  1 
ATOM   1920 C  C   . ALA A 1 239 ? -5.966  16.438  1.085   1.00  31.93 ? 237 ALA B C   1 
ATOM   1921 O  O   . ALA A 1 239 ? -5.377  15.663  1.863   1.00  33.16 ? 237 ALA B O   1 
ATOM   1922 C  CB  . ALA A 1 239 ? -4.127  18.134  0.746   1.00  34.38 ? 237 ALA B CB  1 
ATOM   1923 N  N   . ALA A 1 240 ? -6.881  16.046  0.194   1.00  28.41 ? 238 ALA B N   1 
ATOM   1924 C  CA  . ALA A 1 240 ? -7.380  14.653  0.169   1.00  26.31 ? 238 ALA B CA  1 
ATOM   1925 C  C   . ALA A 1 240 ? -6.298  13.619  -0.139  1.00  25.92 ? 238 ALA B C   1 
ATOM   1926 O  O   . ALA A 1 240 ? -5.498  13.797  -1.043  1.00  23.86 ? 238 ALA B O   1 
ATOM   1927 C  CB  . ALA A 1 240 ? -8.579  14.488  -0.763  1.00  29.37 ? 238 ALA B CB  1 
ATOM   1928 N  N   . ALA A 1 241 ? -6.264  12.549  0.657   1.00  19.94 ? 239 ALA B N   1 
ATOM   1929 C  CA  . ALA A 1 241 ? -5.445  11.393  0.338   1.00  15.93 ? 239 ALA B CA  1 
ATOM   1930 C  C   . ALA A 1 241 ? -6.284  10.163  0.680   1.00  15.77 ? 239 ALA B C   1 
ATOM   1931 O  O   . ALA A 1 241 ? -7.087  10.183  1.673   1.00  15.01 ? 239 ALA B O   1 
ATOM   1932 C  CB  . ALA A 1 241 ? -4.112  11.375  1.105   1.00  15.07 ? 239 ALA B CB  1 
ATOM   1933 N  N   . PHE A 1 242 ? -6.167  9.113   -0.156  1.00  14.13 ? 240 PHE B N   1 
ATOM   1934 C  CA  . PHE A 1 242 ? -7.025  7.934   0.039   1.00  12.73 ? 240 PHE B CA  1 
ATOM   1935 C  C   . PHE A 1 242 ? -6.389  6.782   0.840   1.00  12.18 ? 240 PHE B C   1 
ATOM   1936 O  O   . PHE A 1 242 ? -5.176  6.555   0.749   1.00  12.27 ? 240 PHE B O   1 
ATOM   1937 C  CB  . PHE A 1 242 ? -7.374  7.387   -1.343  1.00  13.87 ? 240 PHE B CB  1 
ATOM   1938 C  CG  . PHE A 1 242 ? -8.211  8.321   -2.133  1.00  15.18 ? 240 PHE B CG  1 
ATOM   1939 C  CD1 . PHE A 1 242 ? -7.623  9.252   -3.004  1.00  16.57 ? 240 PHE B CD1 1 
ATOM   1940 C  CD2 . PHE A 1 242 ? -9.577  8.347   -1.937  1.00  16.98 ? 240 PHE B CD2 1 
ATOM   1941 C  CE1 . PHE A 1 242 ? -8.460  10.126  -3.702  1.00  17.06 ? 240 PHE B CE1 1 
ATOM   1942 C  CE2 . PHE A 1 242 ? -10.436 9.214   -2.643  1.00  18.98 ? 240 PHE B CE2 1 
ATOM   1943 C  CZ  . PHE A 1 242 ? -9.859  10.135  -3.486  1.00  20.25 ? 240 PHE B CZ  1 
ATOM   1944 N  N   . LEU A 1 243 ? -7.251  6.042   1.577   1.00  10.88 ? 241 LEU B N   1 
ATOM   1945 C  CA  . LEU A 1 243 ? -6.739  4.932   2.417   1.00  10.04 ? 241 LEU B CA  1 
ATOM   1946 C  C   . LEU A 1 243 ? -6.733  3.681   1.514   1.00  9.32  ? 241 LEU B C   1 
ATOM   1947 O  O   . LEU A 1 243 ? -7.611  2.735   1.678   1.00  9.15  ? 241 LEU B O   1 
ATOM   1948 C  CB  . LEU A 1 243 ? -7.651  4.785   3.651   1.00  10.76 ? 241 LEU B CB  1 
ATOM   1949 C  CG  . LEU A 1 243 ? -7.252  3.773   4.712   1.00  10.39 ? 241 LEU B CG  1 
ATOM   1950 C  CD1 . LEU A 1 243 ? -5.919  4.225   5.273   1.00  10.55 ? 241 LEU B CD1 1 
ATOM   1951 C  CD2 . LEU A 1 243 ? -8.387  3.746   5.803   1.00  10.89 ? 241 LEU B CD2 1 
ATOM   1952 N  N   . VAL A 1 244 ? -5.776  3.691   0.530   1.00  9.44  ? 242 VAL B N   1 
ATOM   1953 C  CA  . VAL A 1 244 ? -5.763  2.537   -0.461  1.00  9.33  ? 242 VAL B CA  1 
ATOM   1954 C  C   . VAL A 1 244 ? -5.249  1.239   0.165   1.00  10.07 ? 242 VAL B C   1 
ATOM   1955 O  O   . VAL A 1 244 ? -5.503  0.132   -0.355  1.00  9.22  ? 242 VAL B O   1 
ATOM   1956 C  CB  . VAL A 1 244 ? -4.995  2.913   -1.797  1.00  10.82 ? 242 VAL B CB  1 
ATOM   1957 C  CG1 . VAL A 1 244 ? -5.717  4.132   -2.461  1.00  9.67  ? 242 VAL B CG1 1 
ATOM   1958 C  CG2 . VAL A 1 244 ? -3.529  3.142   -1.472  1.00  11.27 ? 242 VAL B CG2 1 
ATOM   1959 N  N   . SER A 1 245 ? -4.539  1.352   1.311   1.00  10.04 ? 243 SER B N   1 
ATOM   1960 C  CA  . SER A 1 245 ? -3.888  0.198   1.942   1.00  10.51 ? 243 SER B CA  1 
ATOM   1961 C  C   . SER A 1 245 ? -3.671  0.515   3.407   1.00  9.93  ? 243 SER B C   1 
ATOM   1962 O  O   . SER A 1 245 ? -3.305  1.640   3.782   1.00  10.65 ? 243 SER B O   1 
ATOM   1963 C  CB  . SER A 1 245 ? -2.504  -0.046  1.294   1.00  11.61 ? 243 SER B CB  1 
ATOM   1964 O  OG  . SER A 1 245 ? -1.887  -1.240  1.760   1.00  11.70 ? 243 SER B OG  1 
ATOM   1965 N  N   . ASN A 1 246 ? -3.914  -0.475  4.275   1.00  9.45  ? 244 ASN B N   1 
ATOM   1966 C  CA  . ASN A 1 246 ? -3.841  -0.160  5.725   1.00  8.62  ? 244 ASN B CA  1 
ATOM   1967 C  C   . ASN A 1 246 ? -3.492  -1.449  6.488   1.00  8.60  ? 244 ASN B C   1 
ATOM   1968 O  O   . ASN A 1 246 ? -4.081  -1.759  7.484   1.00  9.71  ? 244 ASN B O   1 
ATOM   1969 C  CB  . ASN A 1 246 ? -5.172  0.455   6.199   1.00  8.48  ? 244 ASN B CB  1 
ATOM   1970 C  CG  . ASN A 1 246 ? -6.334  -0.500  6.155   1.00  8.70  ? 244 ASN B CG  1 
ATOM   1971 O  OD1 . ASN A 1 246 ? -6.318  -1.493  5.396   1.00  9.35  ? 244 ASN B OD1 1 
ATOM   1972 N  ND2 . ASN A 1 246 ? -7.406  -0.140  6.835   1.00  8.88  ? 244 ASN B ND2 1 
ATOM   1973 N  N   . HIS A 1 247 ? -2.558  -2.202  5.949   1.00  8.90  ? 245 HIS B N   1 
ATOM   1974 C  CA  . HIS A 1 247 ? -2.106  -3.440  6.609   1.00  9.31  ? 245 HIS B CA  1 
ATOM   1975 C  C   . HIS A 1 247 ? -0.679  -3.342  7.024   1.00  10.04 ? 245 HIS B C   1 
ATOM   1976 O  O   . HIS A 1 247 ? 0.182   -2.786  6.269   1.00  12.72 ? 245 HIS B O   1 
ATOM   1977 C  CB  . HIS A 1 247 ? -2.309  -4.712  5.744   1.00  9.24  ? 245 HIS B CB  1 
ATOM   1978 C  CG  . HIS A 1 247 ? -1.633  -4.642  4.409   1.00  10.36 ? 245 HIS B CG  1 
ATOM   1979 N  ND1 . HIS A 1 247 ? -0.449  -5.270  4.137   1.00  14.25 ? 245 HIS B ND1 1 
ATOM   1980 C  CD2 . HIS A 1 247 ? -2.017  -4.014  3.278   1.00  10.34 ? 245 HIS B CD2 1 
ATOM   1981 C  CE1 . HIS A 1 247 ? -0.117  -4.968  2.821   1.00  11.75 ? 245 HIS B CE1 1 
ATOM   1982 N  NE2 . HIS A 1 247 ? -1.077  -4.220  2.341   1.00  14.04 ? 245 HIS B NE2 1 
ATOM   1983 N  N   . ARG A 1 248 ? -0.359  -3.878  8.194   1.00  10.71 ? 246 ARG B N   1 
ATOM   1984 C  CA  . ARG A 1 248 ? 1.017   -3.855  8.713   1.00  10.38 ? 246 ARG B CA  1 
ATOM   1985 C  C   . ARG A 1 248 ? 1.759   -5.124  8.275   1.00  10.50 ? 246 ARG B C   1 
ATOM   1986 O  O   . ARG A 1 248 ? 1.140   -6.180  8.220   1.00  11.90 ? 246 ARG B O   1 
ATOM   1987 C  CB  . ARG A 1 248 ? 0.940   -3.854  10.266  1.00  10.76 ? 246 ARG B CB  1 
ATOM   1988 C  CG  . ARG A 1 248 ? 2.357   -3.676  10.910  1.00  10.26 ? 246 ARG B CG  1 
ATOM   1989 C  CD  . ARG A 1 248 ? 2.323   -3.822  12.440  1.00  10.01 ? 246 ARG B CD  1 
ATOM   1990 N  NE  . ARG A 1 248 ? 3.651   -3.388  12.955  1.00  10.39 ? 246 ARG B NE  1 
ATOM   1991 C  CZ  . ARG A 1 248 ? 4.180   -3.693  14.145  1.00  11.64 ? 246 ARG B CZ  1 
ATOM   1992 N  NH1 . ARG A 1 248 ? 3.561   -4.523  15.001  1.00  9.57  ? 246 ARG B NH1 1 
ATOM   1993 N  NH2 . ARG A 1 248 ? 5.404   -3.175  14.453  1.00  12.76 ? 246 ARG B NH2 1 
ATOM   1994 N  N   . PRO A 1 249 ? 3.095   -5.071  7.946   1.00  10.29 ? 247 PRO B N   1 
ATOM   1995 C  CA  . PRO A 1 249 ? 3.778   -6.289  7.535   1.00  11.55 ? 247 PRO B CA  1 
ATOM   1996 C  C   . PRO A 1 249 ? 3.948   -7.223  8.711   1.00  11.58 ? 247 PRO B C   1 
ATOM   1997 O  O   . PRO A 1 249 ? 3.840   -6.743  9.866   1.00  11.93 ? 247 PRO B O   1 
ATOM   1998 C  CB  . PRO A 1 249 ? 5.202   -5.750  7.090   1.00  12.76 ? 247 PRO B CB  1 
ATOM   1999 C  CG  . PRO A 1 249 ? 5.045   -4.263  6.862   1.00  13.23 ? 247 PRO B CG  1 
ATOM   2000 C  CD  . PRO A 1 249 ? 3.893   -3.830  7.775   1.00  12.74 ? 247 PRO B CD  1 
ATOM   2001 N  N   . PRO A 1 250 ? 4.192   -8.488  8.463   1.00  14.10 ? 248 PRO B N   1 
ATOM   2002 C  CA  . PRO A 1 250 ? 4.463   -9.482  9.515   1.00  13.23 ? 248 PRO B CA  1 
ATOM   2003 C  C   . PRO A 1 250 ? 5.751   -9.170  10.336  1.00  12.81 ? 248 PRO B C   1 
ATOM   2004 O  O   . PRO A 1 250 ? 6.713   -8.497  9.838   1.00  13.14 ? 248 PRO B O   1 
ATOM   2005 C  CB  . PRO A 1 250 ? 4.583   -10.814 8.777   1.00  15.50 ? 248 PRO B CB  1 
ATOM   2006 C  CG  . PRO A 1 250 ? 5.027   -10.374 7.445   1.00  20.81 ? 248 PRO B CG  1 
ATOM   2007 C  CD  . PRO A 1 250 ? 4.487   -9.016  7.114   1.00  15.29 ? 248 PRO B CD  1 
ATOM   2008 N  N   . GLN A 1 251 ? 5.704   -9.544  11.615  1.00  11.58 ? 249 GLN B N   1 
ATOM   2009 C  CA  . GLN A 1 251 ? 6.722   -9.140  12.592  1.00  11.62 ? 249 GLN B CA  1 
ATOM   2010 C  C   . GLN A 1 251 ? 7.358   -10.422 13.104  1.00  11.71 ? 249 GLN B C   1 
ATOM   2011 O  O   . GLN A 1 251 ? 6.763   -11.491 12.996  1.00  12.75 ? 249 GLN B O   1 
ATOM   2012 C  CB  . GLN A 1 251 ? 6.042   -8.384  13.765  1.00  10.95 ? 249 GLN B CB  1 
ATOM   2013 C  CG  . GLN A 1 251 ? 5.350   -7.101  13.289  1.00  11.71 ? 249 GLN B CG  1 
ATOM   2014 C  CD  . GLN A 1 251 ? 6.249   -6.127  12.515  1.00  15.50 ? 249 GLN B CD  1 
ATOM   2015 O  OE1 . GLN A 1 251 ? 5.890   -5.638  11.443  1.00  17.19 ? 249 GLN B OE1 1 
ATOM   2016 N  NE2 . GLN A 1 251 ? 7.441   -5.824  13.077  1.00  15.24 ? 249 GLN B NE2 1 
ATOM   2017 N  N   . PRO A 1 252 ? 8.621   -10.330 13.579  1.00  13.29 ? 250 PRO B N   1 
ATOM   2018 C  CA  . PRO A 1 252 ? 9.361   -11.510 14.047  1.00  13.29 ? 250 PRO B CA  1 
ATOM   2019 C  C   . PRO A 1 252 ? 8.644   -12.251 15.179  1.00  12.98 ? 250 PRO B C   1 
ATOM   2020 O  O   . PRO A 1 252 ? 8.167   -11.644 16.119  1.00  13.92 ? 250 PRO B O   1 
ATOM   2021 C  CB  . PRO A 1 252 ? 10.698  -10.920 14.541  1.00  14.70 ? 250 PRO B CB  1 
ATOM   2022 C  CG  . PRO A 1 252 ? 10.812  -9.576  13.851  1.00  15.84 ? 250 PRO B CG  1 
ATOM   2023 C  CD  . PRO A 1 252 ? 9.388   -9.080  13.765  1.00  14.28 ? 250 PRO B CD  1 
ATOM   2024 N  N   . LEU A 1 253 ? 8.607   -13.572 15.054  1.00  13.02 ? 251 LEU B N   1 
ATOM   2025 C  CA  . LEU A 1 253 ? 7.913   -14.389 16.033  1.00  14.00 ? 251 LEU B CA  1 
ATOM   2026 C  C   . LEU A 1 253 ? 8.670   -14.466 17.359  1.00  15.48 ? 251 LEU B C   1 
ATOM   2027 O  O   . LEU A 1 253 ? 8.073   -14.543 18.425  1.00  14.36 ? 251 LEU B O   1 
ATOM   2028 C  CB  . LEU A 1 253 ? 7.730   -15.791 15.458  1.00  14.08 ? 251 LEU B CB  1 
ATOM   2029 C  CG  . LEU A 1 253 ? 6.817   -16.732 16.240  1.00  14.17 ? 251 LEU B CG  1 
ATOM   2030 C  CD1 . LEU A 1 253 ? 5.382   -16.189 16.419  1.00  13.34 ? 251 LEU B CD1 1 
ATOM   2031 C  CD2 . LEU A 1 253 ? 6.803   -18.058 15.432  1.00  15.07 ? 251 LEU B CD2 1 
ATOM   2032 N  N   . LYS A 1 254 ? 10.015  -14.319 17.300  1.00  17.17 ? 252 LYS B N   1 
ATOM   2033 C  CA  . LYS A 1 254 ? 10.791  -14.177 18.565  1.00  16.78 ? 252 LYS B CA  1 
ATOM   2034 C  C   . LYS A 1 254 ? 10.497  -15.274 19.626  1.00  14.22 ? 252 LYS B C   1 
ATOM   2035 O  O   . LYS A 1 254 ? 10.421  -15.014 20.830  1.00  16.21 ? 252 LYS B O   1 
ATOM   2036 C  CB  . LYS A 1 254 ? 10.770  -12.760 19.144  1.00  17.50 ? 252 LYS B CB  1 
ATOM   2037 C  CG  . LYS A 1 254 ? 11.620  -11.852 18.224  1.00  23.09 ? 252 LYS B CG  1 
ATOM   2038 C  CD  . LYS A 1 254 ? 11.591  -10.443 18.756  1.00  23.60 ? 252 LYS B CD  1 
ATOM   2039 C  CE  . LYS A 1 254 ? 12.273  -9.347  17.903  1.00  26.87 ? 252 LYS B CE  1 
ATOM   2040 N  NZ  . LYS A 1 254 ? 13.721  -9.543  17.996  1.00  31.27 ? 252 LYS B NZ  1 
ATOM   2041 N  N   . GLY A 1 255 ? 10.387  -16.484 19.144  1.00  15.35 ? 253 GLY B N   1 
ATOM   2042 C  CA  . GLY A 1 255 ? 10.269  -17.642 20.058  1.00  14.69 ? 253 GLY B CA  1 
ATOM   2043 C  C   . GLY A 1 255 ? 8.889   -17.933 20.623  1.00  14.58 ? 253 GLY B C   1 
ATOM   2044 O  O   . GLY A 1 255 ? 8.713   -18.862 21.428  1.00  17.11 ? 253 GLY B O   1 
ATOM   2045 N  N   . ARG A 1 256 ? 7.868   -17.188 20.157  1.00  14.02 ? 254 ARG B N   1 
ATOM   2046 C  CA  . ARG A 1 256 ? 6.523   -17.512 20.592  1.00  13.05 ? 254 ARG B CA  1 
ATOM   2047 C  C   . ARG A 1 256 ? 5.997   -18.804 19.939  1.00  14.10 ? 254 ARG B C   1 
ATOM   2048 O  O   . ARG A 1 256 ? 6.417   -19.181 18.827  1.00  16.53 ? 254 ARG B O   1 
ATOM   2049 C  CB  . ARG A 1 256 ? 5.580   -16.372 20.225  1.00  12.76 ? 254 ARG B CB  1 
ATOM   2050 C  CG  . ARG A 1 256 ? 5.762   -15.103 21.055  1.00  11.64 ? 254 ARG B CG  1 
ATOM   2051 C  CD  . ARG A 1 256 ? 4.937   -13.957 20.482  1.00  10.78 ? 254 ARG B CD  1 
ATOM   2052 N  NE  . ARG A 1 256 ? 5.540   -13.374 19.237  1.00  11.02 ? 254 ARG B NE  1 
ATOM   2053 C  CZ  . ARG A 1 256 ? 4.970   -12.446 18.497  1.00  9.41  ? 254 ARG B CZ  1 
ATOM   2054 N  NH1 . ARG A 1 256 ? 3.728   -11.989 18.807  1.00  8.04  ? 254 ARG B NH1 1 
ATOM   2055 N  NH2 . ARG A 1 256 ? 5.635   -11.907 17.451  1.00  9.10  ? 254 ARG B NH2 1 
ATOM   2056 N  N   . LYS A 1 257 ? 5.101   -19.468 20.647  1.00  14.98 ? 255 LYS B N   1 
ATOM   2057 C  CA  . LYS A 1 257 ? 4.473   -20.725 20.201  1.00  17.05 ? 255 LYS B CA  1 
ATOM   2058 C  C   . LYS A 1 257 ? 3.137   -20.384 19.517  1.00  15.55 ? 255 LYS B C   1 
ATOM   2059 O  O   . LYS A 1 257 ? 2.249   -19.766 20.159  1.00  15.15 ? 255 LYS B O   1 
ATOM   2060 C  CB  . LYS A 1 257 ? 4.186   -21.632 21.460  1.00  21.77 ? 255 LYS B CB  1 
ATOM   2061 C  CG  . LYS A 1 257 ? 3.806   -23.053 21.147  1.00  25.06 ? 255 LYS B CG  1 
ATOM   2062 C  CD  . LYS A 1 257 ? 3.244   -23.804 22.402  1.00  25.60 ? 255 LYS B CD  1 
ATOM   2063 C  CE  . LYS A 1 257 ? 4.247   -24.139 23.520  1.00  28.66 ? 255 LYS B CE  1 
ATOM   2064 N  NZ  . LYS A 1 257 ? 3.639   -25.277 24.337  1.00  26.46 ? 255 LYS B NZ  1 
ATOM   2065 N  N   . VAL A 1 258 ? 2.989   -20.735 18.240  1.00  14.27 ? 256 VAL B N   1 
ATOM   2066 C  CA  . VAL A 1 258 ? 1.661   -20.597 17.593  1.00  12.89 ? 256 VAL B CA  1 
ATOM   2067 C  C   . VAL A 1 258 ? 1.019   -21.976 17.735  1.00  12.97 ? 256 VAL B C   1 
ATOM   2068 O  O   . VAL A 1 258 ? 1.624   -23.041 17.395  1.00  14.99 ? 256 VAL B O   1 
ATOM   2069 C  CB  . VAL A 1 258 ? 1.735   -20.267 16.097  1.00  13.45 ? 256 VAL B CB  1 
ATOM   2070 C  CG1 . VAL A 1 258 ? 0.292   -20.081 15.531  1.00  11.72 ? 256 VAL B CG1 1 
ATOM   2071 C  CG2 . VAL A 1 258 ? 2.557   -18.969 15.941  1.00  17.10 ? 256 VAL B CG2 1 
ATOM   2072 N  N   . ARG A 1 259 ? -0.210  -22.005 18.243  1.00  12.47 ? 257 ARG B N   1 
ATOM   2073 C  CA  . ARG A 1 259 ? -0.903  -23.264 18.509  1.00  11.03 ? 257 ARG B CA  1 
ATOM   2074 C  C   . ARG A 1 259 ? -2.136  -23.407 17.619  1.00  12.33 ? 257 ARG B C   1 
ATOM   2075 O  O   . ARG A 1 259 ? -2.692  -22.384 17.204  1.00  11.46 ? 257 ARG B O   1 
ATOM   2076 C  CB  . ARG A 1 259 ? -1.366  -23.290 19.985  1.00  11.92 ? 257 ARG B CB  1 
ATOM   2077 C  CG  . ARG A 1 259 ? -0.203  -23.319 20.990  1.00  12.25 ? 257 ARG B CG  1 
ATOM   2078 C  CD  . ARG A 1 259 ? -0.781  -23.367 22.439  1.00  12.30 ? 257 ARG B CD  1 
ATOM   2079 N  NE  . ARG A 1 259 ? -1.377  -22.105 22.804  1.00  11.93 ? 257 ARG B NE  1 
ATOM   2080 C  CZ  . ARG A 1 259 ? -2.290  -21.996 23.777  1.00  11.60 ? 257 ARG B CZ  1 
ATOM   2081 N  NH1 . ARG A 1 259 ? -2.722  -23.136 24.464  1.00  13.05 ? 257 ARG B NH1 1 
ATOM   2082 N  NH2 . ARG A 1 259 ? -2.753  -20.812 24.095  1.00  10.91 ? 257 ARG B NH2 1 
ATOM   2083 N  N   . ALA A 1 260 ? -2.536  -24.640 17.309  1.00  11.29 ? 258 ALA B N   1 
ATOM   2084 C  CA  . ALA A 1 260 ? -3.749  -24.911 16.493  1.00  11.71 ? 258 ALA B CA  1 
ATOM   2085 C  C   . ALA A 1 260 ? -4.785  -25.589 17.327  1.00  12.79 ? 258 ALA B C   1 
ATOM   2086 O  O   . ALA A 1 260 ? -4.446  -26.463 18.125  1.00  13.05 ? 258 ALA B O   1 
ATOM   2087 C  CB  . ALA A 1 260 ? -3.404  -25.804 15.269  1.00  11.41 ? 258 ALA B CB  1 
ATOM   2088 N  N   . SER A 1 261 ? -6.067  -25.299 17.072  1.00  11.35 ? 259 SER B N   1 
ATOM   2089 C  CA  . SER A 1 261 ? -7.153  -26.006 17.748  1.00  11.52 ? 259 SER B CA  1 
ATOM   2090 C  C   . SER A 1 261 ? -7.578  -27.252 17.047  1.00  12.73 ? 259 SER B C   1 
ATOM   2091 O  O   . SER A 1 261 ? -8.598  -27.826 17.471  1.00  12.03 ? 259 SER B O   1 
ATOM   2092 C  CB  . SER A 1 261 ? -8.396  -25.107 17.796  1.00  11.85 ? 259 SER B CB  1 
ATOM   2093 O  OG  . SER A 1 261 ? -8.992  -24.879 16.477  1.00  11.19 ? 259 SER B OG  1 
ATOM   2094 N  N   . PHE A 1 262 ? -6.889  -27.606 15.937  1.00  13.49 ? 260 PHE B N   1 
ATOM   2095 C  CA  . PHE A 1 262 ? -7.328  -28.702 15.090  1.00  14.25 ? 260 PHE B CA  1 
ATOM   2096 C  C   . PHE A 1 262 ? -6.077  -29.388 14.561  1.00  16.90 ? 260 PHE B C   1 
ATOM   2097 O  O   . PHE A 1 262 ? -4.974  -28.793 14.550  1.00  15.88 ? 260 PHE B O   1 
ATOM   2098 C  CB  . PHE A 1 262 ? -8.139  -28.111 13.957  1.00  14.52 ? 260 PHE B CB  1 
ATOM   2099 C  CG  . PHE A 1 262 ? -7.323  -27.197 13.091  1.00  14.48 ? 260 PHE B CG  1 
ATOM   2100 C  CD1 . PHE A 1 262 ? -6.737  -27.664 11.928  1.00  16.24 ? 260 PHE B CD1 1 
ATOM   2101 C  CD2 . PHE A 1 262 ? -7.115  -25.826 13.478  1.00  12.20 ? 260 PHE B CD2 1 
ATOM   2102 C  CE1 . PHE A 1 262 ? -5.958  -26.796 11.168  1.00  18.06 ? 260 PHE B CE1 1 
ATOM   2103 C  CE2 . PHE A 1 262 ? -6.370  -24.973 12.699  1.00  12.26 ? 260 PHE B CE2 1 
ATOM   2104 C  CZ  . PHE A 1 262 ? -5.784  -25.454 11.557  1.00  15.63 ? 260 PHE B CZ  1 
ATOM   2105 N  N   . HIS A 1 263 ? -6.229  -30.633 14.083  1.00  20.25 ? 261 HIS B N   1 
ATOM   2106 C  CA  . HIS A 1 263 ? -5.098  -31.321 13.376  1.00  23.27 ? 261 HIS B CA  1 
ATOM   2107 C  C   . HIS A 1 263 ? -5.687  -32.287 12.348  1.00  31.84 ? 261 HIS B C   1 
ATOM   2108 O  O   . HIS A 1 263 ? -4.968  -33.034 11.689  1.00  35.32 ? 261 HIS B O   1 
ATOM   2109 C  CB  . HIS A 1 263 ? -4.133  -32.009 14.342  1.00  26.62 ? 261 HIS B CB  1 
ATOM   2110 C  CG  . HIS A 1 263 ? -4.799  -33.045 15.225  1.00  33.94 ? 261 HIS B CG  1 
ATOM   2111 N  ND1 . HIS A 1 263 ? -4.109  -33.846 16.062  1.00  39.00 ? 261 HIS B ND1 1 
ATOM   2112 C  CD2 . HIS A 1 263 ? -6.144  -33.394 15.369  1.00  38.91 ? 261 HIS B CD2 1 
ATOM   2113 C  CE1 . HIS A 1 263 ? -4.965  -34.657 16.714  1.00  40.82 ? 261 HIS B CE1 1 
ATOM   2114 N  NE2 . HIS A 1 263 ? -6.208  -34.386 16.283  1.00  36.07 ? 261 HIS B NE2 1 
ATOM   2115 O  OXT . HIS A 1 263 ? -6.902  -32.344 12.159  1.00  30.24 ? 261 HIS B OXT 1 
ATOM   2116 N  N   . ARG B 1 4   ? -50.653 -46.698 24.991  1.00  43.17 ? 2   ARG A N   1 
ATOM   2117 C  CA  . ARG B 1 4   ? -49.830 -46.130 23.887  1.00  49.47 ? 2   ARG A CA  1 
ATOM   2118 C  C   . ARG B 1 4   ? -49.876 -44.593 23.947  1.00  55.53 ? 2   ARG A C   1 
ATOM   2119 O  O   . ARG B 1 4   ? -48.817 -43.940 23.929  1.00  62.21 ? 2   ARG A O   1 
ATOM   2120 C  CB  . ARG B 1 4   ? -50.289 -46.672 22.513  1.00  48.16 ? 2   ARG A CB  1 
ATOM   2121 C  CG  . ARG B 1 4   ? -49.192 -46.861 21.460  1.00  46.00 ? 2   ARG A CG  1 
ATOM   2122 C  CD  . ARG B 1 4   ? -48.957 -45.606 20.630  0.010 46.65 ? 2   ARG A CD  1 
ATOM   2123 N  NE  . ARG B 1 4   ? -49.961 -45.439 19.582  0.010 46.43 ? 2   ARG A NE  1 
ATOM   2124 C  CZ  . ARG B 1 4   ? -50.994 -44.605 19.656  0.010 46.33 ? 2   ARG A CZ  1 
ATOM   2125 N  NH1 . ARG B 1 4   ? -51.165 -43.850 20.732  0.010 46.33 ? 2   ARG A NH1 1 
ATOM   2126 N  NH2 . ARG B 1 4   ? -51.855 -44.524 18.651  0.010 46.27 ? 2   ARG A NH2 1 
ATOM   2127 N  N   . LEU B 1 5   ? -51.087 -44.022 24.028  1.00  56.28 ? 3   LEU A N   1 
ATOM   2128 C  CA  . LEU B 1 5   ? -51.295 -42.559 24.206  1.00  50.55 ? 3   LEU A CA  1 
ATOM   2129 C  C   . LEU B 1 5   ? -51.589 -42.181 25.698  1.00  52.74 ? 3   LEU A C   1 
ATOM   2130 O  O   . LEU B 1 5   ? -52.513 -41.399 26.013  1.00  58.00 ? 3   LEU A O   1 
ATOM   2131 C  CB  . LEU B 1 5   ? -52.408 -42.051 23.279  0.010 51.96 ? 3   LEU A CB  1 
ATOM   2132 C  CG  . LEU B 1 5   ? -52.203 -42.147 21.762  0.010 51.56 ? 3   LEU A CG  1 
ATOM   2133 C  CD1 . LEU B 1 5   ? -53.530 -41.996 21.033  0.010 51.49 ? 3   LEU A CD1 1 
ATOM   2134 C  CD2 . LEU B 1 5   ? -51.192 -41.125 21.260  0.010 51.50 ? 3   LEU A CD2 1 
ATOM   2135 N  N   . SER B 1 6   ? -50.812 -42.758 26.612  1.00  37.23 ? 4   SER A N   1 
ATOM   2136 C  CA  . SER B 1 6   ? -50.936 -42.459 28.031  1.00  34.12 ? 4   SER A CA  1 
ATOM   2137 C  C   . SER B 1 6   ? -49.734 -42.954 28.813  1.00  24.70 ? 4   SER A C   1 
ATOM   2138 O  O   . SER B 1 6   ? -49.804 -43.097 30.033  1.00  26.41 ? 4   SER A O   1 
ATOM   2139 C  CB  . SER B 1 6   ? -52.234 -43.039 28.621  1.00  40.48 ? 4   SER A CB  1 
ATOM   2140 O  OG  . SER B 1 6   ? -52.124 -44.437 28.775  1.00  40.56 ? 4   SER A OG  1 
ATOM   2141 N  N   . TRP B 1 7   ? -48.584 -43.106 28.157  1.00  20.25 ? 5   TRP A N   1 
ATOM   2142 C  CA  . TRP B 1 7   ? -47.350 -43.335 28.902  1.00  17.16 ? 5   TRP A CA  1 
ATOM   2143 C  C   . TRP B 1 7   ? -47.007 -42.116 29.815  1.00  14.33 ? 5   TRP A C   1 
ATOM   2144 O  O   . TRP B 1 7   ? -47.419 -40.977 29.569  1.00  15.07 ? 5   TRP A O   1 
ATOM   2145 C  CB  . TRP B 1 7   ? -46.201 -43.631 27.949  1.00  14.40 ? 5   TRP A CB  1 
ATOM   2146 C  CG  . TRP B 1 7   ? -45.762 -42.439 27.111  1.00  15.05 ? 5   TRP A CG  1 
ATOM   2147 C  CD1 . TRP B 1 7   ? -46.232 -42.049 25.852  1.00  18.12 ? 5   TRP A CD1 1 
ATOM   2148 C  CD2 . TRP B 1 7   ? -44.744 -41.428 27.462  1.00  14.85 ? 5   TRP A CD2 1 
ATOM   2149 N  NE1 . TRP B 1 7   ? -45.596 -40.905 25.421  1.00  17.49 ? 5   TRP A NE1 1 
ATOM   2150 C  CE2 . TRP B 1 7   ? -44.697 -40.480 26.342  1.00  16.25 ? 5   TRP A CE2 1 
ATOM   2151 C  CE3 . TRP B 1 7   ? -43.905 -41.221 28.557  1.00  13.29 ? 5   TRP A CE3 1 
ATOM   2152 C  CZ2 . TRP B 1 7   ? -43.837 -39.389 26.340  1.00  14.98 ? 5   TRP A CZ2 1 
ATOM   2153 C  CZ3 . TRP B 1 7   ? -43.047 -40.121 28.543  1.00  13.77 ? 5   TRP A CZ3 1 
ATOM   2154 C  CH2 . TRP B 1 7   ? -43.013 -39.228 27.461  1.00  13.59 ? 5   TRP A CH2 1 
ATOM   2155 N  N   . GLY B 1 8   ? -46.219 -42.370 30.860  1.00  13.58 ? 6   GLY A N   1 
ATOM   2156 C  CA  . GLY B 1 8   ? -45.769 -41.269 31.762  1.00  12.92 ? 6   GLY A CA  1 
ATOM   2157 C  C   . GLY B 1 8   ? -44.740 -41.801 32.681  1.00  12.81 ? 6   GLY A C   1 
ATOM   2158 O  O   . GLY B 1 8   ? -43.940 -42.636 32.268  1.00  12.92 ? 6   GLY A O   1 
ATOM   2159 N  N   . TYR B 1 9   ? -44.731 -41.333 33.954  1.00  12.37 ? 7   TYR A N   1 
ATOM   2160 C  CA  . TYR B 1 9   ? -43.696 -41.751 34.914  1.00  12.58 ? 7   TYR A CA  1 
ATOM   2161 C  C   . TYR B 1 9   ? -44.351 -42.139 36.232  1.00  15.80 ? 7   TYR A C   1 
ATOM   2162 O  O   . TYR B 1 9   ? -43.673 -42.298 37.246  1.00  17.29 ? 7   TYR A O   1 
ATOM   2163 C  CB  . TYR B 1 9   ? -42.778 -40.543 35.160  1.00  11.43 ? 7   TYR A CB  1 
ATOM   2164 C  CG  . TYR B 1 9   ? -41.930 -40.179 33.907  1.00  9.27  ? 7   TYR A CG  1 
ATOM   2165 C  CD1 . TYR B 1 9   ? -40.686 -40.844 33.667  1.00  11.06 ? 7   TYR A CD1 1 
ATOM   2166 C  CD2 . TYR B 1 9   ? -42.396 -39.157 33.010  1.00  10.38 ? 7   TYR A CD2 1 
ATOM   2167 C  CE1 . TYR B 1 9   ? -39.947 -40.530 32.531  1.00  10.25 ? 7   TYR A CE1 1 
ATOM   2168 C  CE2 . TYR B 1 9   ? -41.629 -38.835 31.886  1.00  10.57 ? 7   TYR A CE2 1 
ATOM   2169 C  CZ  . TYR B 1 9   ? -40.397 -39.492 31.720  1.00  10.15 ? 7   TYR A CZ  1 
ATOM   2170 O  OH  . TYR B 1 9   ? -39.647 -39.150 30.599  1.00  10.55 ? 7   TYR A OH  1 
ATOM   2171 N  N   . ARG B 1 10  ? -45.657 -42.341 36.172  1.00  16.35 ? 8   ARG A N   1 
ATOM   2172 C  CA  . ARG B 1 10  ? -46.382 -42.820 37.396  1.00  20.38 ? 8   ARG A CA  1 
ATOM   2173 C  C   . ARG B 1 10  ? -46.295 -44.373 37.512  1.00  21.87 ? 8   ARG A C   1 
ATOM   2174 O  O   . ARG B 1 10  ? -45.745 -45.091 36.656  1.00  17.00 ? 8   ARG A O   1 
ATOM   2175 C  CB  . ARG B 1 10  ? -47.784 -42.300 37.329  1.00  22.46 ? 8   ARG A CB  1 
ATOM   2176 C  CG  . ARG B 1 10  ? -47.850 -40.769 37.498  1.00  27.88 ? 8   ARG A CG  1 
ATOM   2177 C  CD  . ARG B 1 10  ? -49.200 -40.185 37.105  1.00  28.21 ? 8   ARG A CD  1 
ATOM   2178 N  NE  . ARG B 1 10  ? -50.146 -40.162 38.231  1.00  33.62 ? 8   ARG A NE  1 
ATOM   2179 C  CZ  . ARG B 1 10  ? -51.411 -39.737 38.173  1.00  36.65 ? 8   ARG A CZ  1 
ATOM   2180 N  NH1 . ARG B 1 10  ? -51.919 -39.272 37.035  1.00  35.52 ? 8   ARG A NH1 1 
ATOM   2181 N  NH2 . ARG B 1 10  ? -52.171 -39.766 39.265  1.00  38.36 ? 8   ARG A NH2 1 
ATOM   2182 N  N   . GLU B 1 11  ? -46.850 -44.913 38.610  1.00  24.01 ? 9   GLU A N   1 
ATOM   2183 C  CA  . GLU B 1 11  ? -46.763 -46.353 38.834  1.00  22.78 ? 9   GLU A CA  1 
ATOM   2184 C  C   . GLU B 1 11  ? -47.196 -47.266 37.635  1.00  23.65 ? 9   GLU A C   1 
ATOM   2185 O  O   . GLU B 1 11  ? -46.485 -48.199 37.269  1.00  22.89 ? 9   GLU A O   1 
ATOM   2186 C  CB  . GLU B 1 11  ? -47.542 -46.697 40.153  1.00  28.12 ? 9   GLU A CB  1 
ATOM   2187 C  CG  . GLU B 1 11  ? -47.702 -48.174 40.392  1.00  34.96 ? 9   GLU A CG  1 
ATOM   2188 C  CD  . GLU B 1 11  ? -46.399 -48.905 40.624  1.00  44.46 ? 9   GLU A CD  1 
ATOM   2189 O  OE1 . GLU B 1 11  ? -45.341 -48.258 40.882  1.00  51.34 ? 9   GLU A OE1 1 
ATOM   2190 O  OE2 . GLU B 1 11  ? -46.447 -50.157 40.556  1.00  56.29 ? 9   GLU A OE2 1 
ATOM   2191 N  N   . HIS B 1 12  ? -48.347 -47.003 37.056  1.00  22.79 ? 10  HIS A N   1 
ATOM   2192 C  CA  . HIS B 1 12  ? -48.976 -47.855 36.025  1.00  27.72 ? 10  HIS A CA  1 
ATOM   2193 C  C   . HIS B 1 12  ? -48.666 -47.523 34.613  1.00  27.43 ? 10  HIS A C   1 
ATOM   2194 O  O   . HIS B 1 12  ? -48.855 -48.330 33.734  1.00  25.91 ? 10  HIS A O   1 
ATOM   2195 C  CB  . HIS B 1 12  ? -50.484 -47.943 36.267  1.00  32.75 ? 10  HIS A CB  1 
ATOM   2196 C  CG  . HIS B 1 12  ? -50.828 -48.537 37.604  1.00  35.14 ? 10  HIS A CG  1 
ATOM   2197 N  ND1 . HIS B 1 12  ? -51.699 -47.970 38.459  1.00  41.87 ? 10  HIS A ND1 1 
ATOM   2198 C  CD2 . HIS B 1 12  ? -50.330 -49.667 38.241  1.00  41.78 ? 10  HIS A CD2 1 
ATOM   2199 C  CE1 . HIS B 1 12  ? -51.770 -48.713 39.578  1.00  39.37 ? 10  HIS A CE1 1 
ATOM   2200 N  NE2 . HIS B 1 12  ? -50.932 -49.751 39.440  1.00  35.83 ? 10  HIS A NE2 1 
ATOM   2201 N  N   . ASN B 1 13  ? -48.092 -46.337 34.404  1.00  23.35 ? 11  ASN A N   1 
ATOM   2202 C  CA  . ASN B 1 13  ? -47.691 -45.947 33.040  1.00  17.82 ? 11  ASN A CA  1 
ATOM   2203 C  C   . ASN B 1 13  ? -46.192 -45.590 32.914  1.00  16.49 ? 11  ASN A C   1 
ATOM   2204 O  O   . ASN B 1 13  ? -45.761 -45.137 31.846  1.00  15.78 ? 11  ASN A O   1 
ATOM   2205 C  CB  . ASN B 1 13  ? -48.527 -44.814 32.546  1.00  16.36 ? 11  ASN A CB  1 
ATOM   2206 C  CG  . ASN B 1 13  ? -48.243 -43.509 33.264  1.00  15.93 ? 11  ASN A CG  1 
ATOM   2207 O  OD1 . ASN B 1 13  ? -47.362 -43.471 34.130  1.00  15.52 ? 11  ASN A OD1 1 
ATOM   2208 N  ND2 . ASN B 1 13  ? -49.005 -42.487 32.950  1.00  14.78 ? 11  ASN A ND2 1 
ATOM   2209 N  N   . GLY B 1 14  ? -45.427 -45.805 33.961  1.00  16.08 ? 12  GLY A N   1 
ATOM   2210 C  CA  . GLY B 1 14  ? -43.990 -45.493 33.948  1.00  14.92 ? 12  GLY A CA  1 
ATOM   2211 C  C   . GLY B 1 14  ? -43.067 -46.369 33.143  1.00  14.47 ? 12  GLY A C   1 
ATOM   2212 O  O   . GLY B 1 14  ? -43.492 -47.334 32.510  1.00  16.70 ? 12  GLY A O   1 
ATOM   2213 N  N   . PRO B 1 15  ? -41.735 -46.099 33.213  1.00  15.24 ? 13  PRO A N   1 
ATOM   2214 C  CA  . PRO B 1 15  ? -40.794 -46.717 32.341  1.00  14.31 ? 13  PRO A CA  1 
ATOM   2215 C  C   . PRO B 1 15  ? -40.806 -48.260 32.267  1.00  17.37 ? 13  PRO A C   1 
ATOM   2216 O  O   . PRO B 1 15  ? -40.626 -48.798 31.200  1.00  16.13 ? 13  PRO A O   1 
ATOM   2217 C  CB  . PRO B 1 15  ? -39.419 -46.222 32.896  1.00  15.29 ? 13  PRO A CB  1 
ATOM   2218 C  CG  . PRO B 1 15  ? -39.770 -44.784 33.396  1.00  14.57 ? 13  PRO A CG  1 
ATOM   2219 C  CD  . PRO B 1 15  ? -41.180 -44.879 33.916  1.00  15.99 ? 13  PRO A CD  1 
ATOM   2220 N  N   . ILE B 1 16  ? -41.039 -48.931 33.408  1.00  20.21 ? 14  ILE A N   1 
ATOM   2221 C  CA  . ILE B 1 16  ? -41.046 -50.375 33.390  1.00  20.83 ? 14  ILE A CA  1 
ATOM   2222 C  C   . ILE B 1 16  ? -42.208 -50.921 32.523  1.00  20.54 ? 14  ILE A C   1 
ATOM   2223 O  O   . ILE B 1 16  ? -42.169 -52.067 32.062  1.00  24.09 ? 14  ILE A O   1 
ATOM   2224 C  CB  . ILE B 1 16  ? -41.036 -50.905 34.845  1.00  26.43 ? 14  ILE A CB  1 
ATOM   2225 C  CG1 . ILE B 1 16  ? -40.609 -52.380 34.881  1.00  32.77 ? 14  ILE A CG1 1 
ATOM   2226 C  CG2 . ILE B 1 16  ? -42.385 -50.679 35.518  1.00  25.61 ? 14  ILE A CG2 1 
ATOM   2227 C  CD1 . ILE B 1 16  ? -39.175 -52.602 35.305  1.00  37.26 ? 14  ILE A CD1 1 
ATOM   2228 N  N   . HIS B 1 17  ? -43.245 -50.131 32.283  1.00  20.50 ? 15  HIS A N   1 
ATOM   2229 C  CA  . HIS B 1 17  ? -44.362 -50.571 31.464  1.00  19.79 ? 15  HIS A CA  1 
ATOM   2230 C  C   . HIS B 1 17  ? -44.246 -50.152 30.026  1.00  18.58 ? 15  HIS A C   1 
ATOM   2231 O  O   . HIS B 1 17  ? -45.079 -50.561 29.180  1.00  18.65 ? 15  HIS A O   1 
ATOM   2232 C  CB  . HIS B 1 17  ? -45.690 -50.041 32.060  1.00  24.03 ? 15  HIS A CB  1 
ATOM   2233 C  CG  . HIS B 1 17  ? -45.954 -50.541 33.460  1.00  30.21 ? 15  HIS A CG  1 
ATOM   2234 N  ND1 . HIS B 1 17  ? -46.173 -51.839 33.731  1.00  30.99 ? 15  HIS A ND1 1 
ATOM   2235 C  CD2 . HIS B 1 17  ? -45.994 -49.872 34.679  1.00  31.02 ? 15  HIS A CD2 1 
ATOM   2236 C  CE1 . HIS B 1 17  ? -46.357 -51.996 35.054  1.00  33.30 ? 15  HIS A CE1 1 
ATOM   2237 N  NE2 . HIS B 1 17  ? -46.248 -50.791 35.635  1.00  27.90 ? 15  HIS A NE2 1 
ATOM   2238 N  N   . TRP B 1 18  ? -43.245 -49.307 29.693  1.00  12.30 ? 16  TRP A N   1 
ATOM   2239 C  CA  . TRP B 1 18  ? -43.285 -48.795 28.320  1.00  13.92 ? 16  TRP A CA  1 
ATOM   2240 C  C   . TRP B 1 18  ? -43.183 -49.898 27.263  1.00  13.79 ? 16  TRP A C   1 
ATOM   2241 O  O   . TRP B 1 18  ? -43.770 -49.694 26.221  1.00  16.74 ? 16  TRP A O   1 
ATOM   2242 C  CB  . TRP B 1 18  ? -42.162 -47.725 28.072  1.00  13.25 ? 16  TRP A CB  1 
ATOM   2243 C  CG  . TRP B 1 18  ? -42.366 -46.510 28.859  1.00  12.49 ? 16  TRP A CG  1 
ATOM   2244 C  CD1 . TRP B 1 18  ? -43.458 -46.113 29.610  1.00  13.90 ? 16  TRP A CD1 1 
ATOM   2245 C  CD2 . TRP B 1 18  ? -41.345 -45.445 29.046  1.00  12.00 ? 16  TRP A CD2 1 
ATOM   2246 N  NE1 . TRP B 1 18  ? -43.236 -44.857 30.228  1.00  13.98 ? 16  TRP A NE1 1 
ATOM   2247 C  CE2 . TRP B 1 18  ? -41.960 -44.439 29.926  1.00  12.01 ? 16  TRP A CE2 1 
ATOM   2248 C  CE3 . TRP B 1 18  ? -40.022 -45.259 28.564  1.00  11.48 ? 16  TRP A CE3 1 
ATOM   2249 C  CZ2 . TRP B 1 18  ? -41.295 -43.273 30.273  1.00  11.45 ? 16  TRP A CZ2 1 
ATOM   2250 C  CZ3 . TRP B 1 18  ? -39.348 -44.128 29.003  1.00  9.92  ? 16  TRP A CZ3 1 
ATOM   2251 C  CH2 . TRP B 1 18  ? -39.996 -43.135 29.802  1.00  9.89  ? 16  TRP A CH2 1 
ATOM   2252 N  N   . LYS B 1 19  ? -42.395 -50.949 27.511  1.00  16.80 ? 17  LYS A N   1 
ATOM   2253 C  CA  . LYS B 1 19  ? -42.253 -52.147 26.613  1.00  18.93 ? 17  LYS A CA  1 
ATOM   2254 C  C   . LYS B 1 19  ? -43.616 -52.755 26.182  1.00  22.63 ? 17  LYS A C   1 
ATOM   2255 O  O   . LYS B 1 19  ? -43.698 -53.376 25.104  1.00  21.69 ? 17  LYS A O   1 
ATOM   2256 C  CB  . LYS B 1 19  ? -41.407 -53.225 27.281  1.00  19.18 ? 17  LYS A CB  1 
ATOM   2257 C  CG  . LYS B 1 19  ? -42.072 -53.935 28.472  1.00  20.10 ? 17  LYS A CG  1 
ATOM   2258 C  CD  . LYS B 1 19  ? -41.137 -55.007 29.137  1.00  26.52 ? 17  LYS A CD  1 
ATOM   2259 C  CE  . LYS B 1 19  ? -39.767 -54.607 29.783  1.00  28.29 ? 17  LYS A CE  1 
ATOM   2260 N  NZ  . LYS B 1 19  ? -39.684 -53.806 31.097  1.00  28.88 ? 17  LYS A NZ  1 
ATOM   2261 N  N   . GLU B 1 20  ? -44.690 -52.516 26.955  1.00  22.81 ? 18  GLU A N   1 
ATOM   2262 C  CA  . GLU B 1 20  ? -46.028 -53.040 26.580  1.00  21.54 ? 18  GLU A CA  1 
ATOM   2263 C  C   . GLU B 1 20  ? -46.593 -52.453 25.340  1.00  22.75 ? 18  GLU A C   1 
ATOM   2264 O  O   . GLU B 1 20  ? -47.321 -53.139 24.541  1.00  24.76 ? 18  GLU A O   1 
ATOM   2265 C  CB  . GLU B 1 20  ? -47.061 -52.817 27.691  1.00  23.54 ? 18  GLU A CB  1 
ATOM   2266 C  CG  . GLU B 1 20  ? -46.654 -53.556 28.936  1.00  27.39 ? 18  GLU A CG  1 
ATOM   2267 C  CD  . GLU B 1 20  ? -47.428 -53.088 30.151  1.00  30.16 ? 18  GLU A CD  1 
ATOM   2268 O  OE1 . GLU B 1 20  ? -48.534 -52.477 29.973  1.00  32.31 ? 18  GLU A OE1 1 
ATOM   2269 O  OE2 . GLU B 1 20  ? -46.891 -53.321 31.256  1.00  29.12 ? 18  GLU A OE2 1 
ATOM   2270 N  N   . PHE B 1 21  ? -46.313 -51.196 25.112  1.00  19.94 ? 19  PHE A N   1 
ATOM   2271 C  CA  . PHE B 1 21  ? -46.684 -50.620 23.873  1.00  20.44 ? 19  PHE A CA  1 
ATOM   2272 C  C   . PHE B 1 21  ? -45.544 -50.230 22.940  1.00  20.45 ? 19  PHE A C   1 
ATOM   2273 O  O   . PHE B 1 21  ? -45.825 -49.919 21.793  1.00  22.36 ? 19  PHE A O   1 
ATOM   2274 C  CB  . PHE B 1 21  ? -47.674 -49.505 24.096  1.00  23.83 ? 19  PHE A CB  1 
ATOM   2275 C  CG  . PHE B 1 21  ? -49.019 -50.036 24.530  1.00  30.80 ? 19  PHE A CG  1 
ATOM   2276 C  CD1 . PHE B 1 21  ? -49.389 -50.022 25.835  1.00  32.87 ? 19  PHE A CD1 1 
ATOM   2277 C  CD2 . PHE B 1 21  ? -49.858 -50.640 23.595  1.00  34.40 ? 19  PHE A CD2 1 
ATOM   2278 C  CE1 . PHE B 1 21  ? -50.634 -50.526 26.241  1.00  35.98 ? 19  PHE A CE1 1 
ATOM   2279 C  CE2 . PHE B 1 21  ? -51.089 -51.164 23.972  1.00  39.01 ? 19  PHE A CE2 1 
ATOM   2280 C  CZ  . PHE B 1 21  ? -51.480 -51.105 25.306  1.00  40.91 ? 19  PHE A CZ  1 
ATOM   2281 N  N   . PHE B 1 22  ? -44.305 -50.291 23.424  1.00  19.43 ? 20  PHE A N   1 
ATOM   2282 C  CA  . PHE B 1 22  ? -43.119 -49.816 22.646  1.00  17.74 ? 20  PHE A CA  1 
ATOM   2283 C  C   . PHE B 1 22  ? -42.033 -50.866 22.839  1.00  19.04 ? 20  PHE A C   1 
ATOM   2284 O  O   . PHE B 1 22  ? -41.139 -50.734 23.646  1.00  16.98 ? 20  PHE A O   1 
ATOM   2285 C  CB  . PHE B 1 22  ? -42.688 -48.407 23.160  1.00  17.69 ? 20  PHE A CB  1 
ATOM   2286 C  CG  . PHE B 1 22  ? -43.761 -47.358 23.007  1.00  16.69 ? 20  PHE A CG  1 
ATOM   2287 C  CD1 . PHE B 1 22  ? -43.988 -46.719 21.805  1.00  19.32 ? 20  PHE A CD1 1 
ATOM   2288 C  CD2 . PHE B 1 22  ? -44.538 -47.017 24.088  1.00  18.30 ? 20  PHE A CD2 1 
ATOM   2289 C  CE1 . PHE B 1 22  ? -45.002 -45.789 21.654  1.00  17.76 ? 20  PHE A CE1 1 
ATOM   2290 C  CE2 . PHE B 1 22  ? -45.552 -46.082 23.981  1.00  16.31 ? 20  PHE A CE2 1 
ATOM   2291 C  CZ  . PHE B 1 22  ? -45.834 -45.493 22.727  1.00  16.99 ? 20  PHE A CZ  1 
ATOM   2292 N  N   . PRO B 1 23  ? -42.165 -52.039 22.159  1.00  19.51 ? 21  PRO A N   1 
ATOM   2293 C  CA  . PRO B 1 23  ? -41.274 -53.128 22.472  1.00  21.03 ? 21  PRO A CA  1 
ATOM   2294 C  C   . PRO B 1 23  ? -39.765 -52.867 22.191  1.00  16.82 ? 21  PRO A C   1 
ATOM   2295 O  O   . PRO B 1 23  ? -38.936 -53.598 22.785  1.00  19.29 ? 21  PRO A O   1 
ATOM   2296 C  CB  . PRO B 1 23  ? -41.841 -54.337 21.657  1.00  24.21 ? 21  PRO A CB  1 
ATOM   2297 C  CG  . PRO B 1 23  ? -42.683 -53.710 20.581  1.00  21.42 ? 21  PRO A CG  1 
ATOM   2298 C  CD  . PRO B 1 23  ? -43.234 -52.414 21.202  1.00  22.59 ? 21  PRO A CD  1 
ATOM   2299 N  N   . ILE B 1 24  ? -39.469 -51.817 21.408  1.00  18.03 ? 22  ILE A N   1 
ATOM   2300 C  CA  . ILE B 1 24  ? -38.096 -51.350 21.138  1.00  15.89 ? 22  ILE A CA  1 
ATOM   2301 C  C   . ILE B 1 24  ? -37.430 -50.883 22.492  1.00  14.28 ? 22  ILE A C   1 
ATOM   2302 O  O   . ILE B 1 24  ? -36.172 -50.727 22.547  1.00  15.53 ? 22  ILE A O   1 
ATOM   2303 C  CB  . ILE B 1 24  ? -38.093 -50.259 20.036  1.00  14.20 ? 22  ILE A CB  1 
ATOM   2304 C  CG1 . ILE B 1 24  ? -36.675 -50.157 19.387  1.00  16.46 ? 22  ILE A CG1 1 
ATOM   2305 C  CG2 . ILE B 1 24  ? -38.536 -48.932 20.671  1.00  12.89 ? 22  ILE A CG2 1 
ATOM   2306 C  CD1 . ILE B 1 24  ? -36.139 -51.481 18.765  1.00  19.28 ? 22  ILE A CD1 1 
ATOM   2307 N  N   . ALA B 1 25  ? -38.240 -50.729 23.572  1.00  15.25 ? 23  ALA A N   1 
ATOM   2308 C  CA  . ALA B 1 25  ? -37.726 -50.405 24.925  1.00  15.69 ? 23  ALA A CA  1 
ATOM   2309 C  C   . ALA B 1 25  ? -36.667 -51.383 25.318  1.00  16.84 ? 23  ALA A C   1 
ATOM   2310 O  O   . ALA B 1 25  ? -35.733 -51.070 26.027  1.00  17.67 ? 23  ALA A O   1 
ATOM   2311 C  CB  . ALA B 1 25  ? -38.864 -50.501 25.988  1.00  14.01 ? 23  ALA A CB  1 
ATOM   2312 N  N   . ASP B 1 26  ? -36.826 -52.644 24.841  1.00  17.22 ? 24  ASP A N   1 
ATOM   2313 C  CA  . ASP B 1 26  ? -35.777 -53.633 25.119  1.00  17.77 ? 24  ASP A CA  1 
ATOM   2314 C  C   . ASP B 1 26  ? -34.802 -53.952 23.993  1.00  19.11 ? 24  ASP A C   1 
ATOM   2315 O  O   . ASP B 1 26  ? -34.218 -55.061 23.975  1.00  18.59 ? 24  ASP A O   1 
ATOM   2316 C  CB  . ASP B 1 26  ? -36.456 -54.964 25.546  1.00  21.91 ? 24  ASP A CB  1 
ATOM   2317 C  CG  . ASP B 1 26  ? -37.359 -54.774 26.755  1.00  24.48 ? 24  ASP A CG  1 
ATOM   2318 O  OD1 . ASP B 1 26  ? -36.873 -54.237 27.748  1.00  28.86 ? 24  ASP A OD1 1 
ATOM   2319 O  OD2 . ASP B 1 26  ? -38.548 -55.127 26.720  1.00  28.24 ? 24  ASP A OD2 1 
ATOM   2320 N  N   . GLY B 1 27  ? -34.623 -53.007 23.062  1.00  16.42 ? 25  GLY A N   1 
ATOM   2321 C  CA  . GLY B 1 27  ? -33.743 -53.079 21.938  1.00  15.87 ? 25  GLY A CA  1 
ATOM   2322 C  C   . GLY B 1 27  ? -32.233 -53.064 22.306  1.00  17.52 ? 25  GLY A C   1 
ATOM   2323 O  O   . GLY B 1 27  ? -31.804 -53.069 23.499  1.00  18.90 ? 25  GLY A O   1 
ATOM   2324 N  N   . ASP B 1 28  ? -31.453 -52.969 21.250  1.00  16.02 ? 26  ASP A N   1 
ATOM   2325 C  CA  . ASP B 1 28  ? -30.038 -53.114 21.334  1.00  14.83 ? 26  ASP A CA  1 
ATOM   2326 C  C   . ASP B 1 28  ? -29.354 -51.769 21.395  1.00  14.55 ? 26  ASP A C   1 
ATOM   2327 O  O   . ASP B 1 28  ? -28.149 -51.692 21.593  1.00  13.21 ? 26  ASP A O   1 
ATOM   2328 C  CB  . ASP B 1 28  ? -29.567 -53.931 20.117  1.00  18.85 ? 26  ASP A CB  1 
ATOM   2329 C  CG  . ASP B 1 28  ? -29.805 -55.471 20.319  1.00  24.43 ? 26  ASP A CG  1 
ATOM   2330 O  OD1 . ASP B 1 28  ? -30.062 -55.884 21.479  1.00  24.99 ? 26  ASP A OD1 1 
ATOM   2331 O  OD2 . ASP B 1 28  ? -29.781 -56.210 19.294  1.00  24.03 ? 26  ASP A OD2 1 
ATOM   2332 N  N   . GLN B 1 29  ? -30.107 -50.697 21.113  1.00  11.95 ? 27  GLN A N   1 
ATOM   2333 C  CA  . GLN B 1 29  ? -29.487 -49.340 21.064  1.00  12.09 ? 27  GLN A CA  1 
ATOM   2334 C  C   . GLN B 1 29  ? -30.346 -48.340 21.869  1.00  12.55 ? 27  GLN A C   1 
ATOM   2335 O  O   . GLN B 1 29  ? -30.638 -47.260 21.375  1.00  10.40 ? 27  GLN A O   1 
ATOM   2336 C  CB  . GLN B 1 29  ? -29.186 -48.803 19.642  1.00  14.02 ? 27  GLN A CB  1 
ATOM   2337 C  CG  . GLN B 1 29  ? -28.193 -49.727 18.886  1.00  16.91 ? 27  GLN A CG  1 
ATOM   2338 C  CD  . GLN B 1 29  ? -27.322 -49.060 17.854  1.00  19.19 ? 27  GLN A CD  1 
ATOM   2339 O  OE1 . GLN B 1 29  ? -26.219 -49.638 17.517  1.00  26.69 ? 27  GLN A OE1 1 
ATOM   2340 N  NE2 . GLN B 1 29  ? -27.786 -47.946 17.243  1.00  14.49 ? 27  GLN A NE2 1 
ATOM   2341 N  N   . GLN B 1 30  ? -30.651 -48.700 23.117  1.00  12.09 ? 28  GLN A N   1 
ATOM   2342 C  CA  . GLN B 1 30  ? -31.527 -47.895 23.936  1.00  10.40 ? 28  GLN A CA  1 
ATOM   2343 C  C   . GLN B 1 30  ? -30.704 -46.981 24.819  1.00  10.16 ? 28  GLN A C   1 
ATOM   2344 O  O   . GLN B 1 30  ? -29.554 -47.239 25.138  1.00  11.44 ? 28  GLN A O   1 
ATOM   2345 C  CB  . GLN B 1 30  ? -32.413 -48.802 24.808  1.00  10.61 ? 28  GLN A CB  1 
ATOM   2346 C  CG  . GLN B 1 30  ? -33.454 -49.453 23.899  1.00  11.32 ? 28  GLN A CG  1 
ATOM   2347 C  CD  . GLN B 1 30  ? -34.475 -48.402 23.421  1.00  10.20 ? 28  GLN A CD  1 
ATOM   2348 O  OE1 . GLN B 1 30  ? -35.301 -47.863 24.201  1.00  10.36 ? 28  GLN A OE1 1 
ATOM   2349 N  NE2 . GLN B 1 30  ? -34.444 -48.116 22.092  1.00  11.73 ? 28  GLN A NE2 1 
ATOM   2350 N  N   . SER B 1 31  ? -31.339 -45.858 25.175  1.00  9.68  ? 29  SER A N   1 
ATOM   2351 C  CA  . SER B 1 31  ? -30.781 -44.815 26.033  1.00  8.47  ? 29  SER A CA  1 
ATOM   2352 C  C   . SER B 1 31  ? -31.724 -44.536 27.175  1.00  8.80  ? 29  SER A C   1 
ATOM   2353 O  O   . SER B 1 31  ? -32.941 -44.763 27.051  1.00  8.43  ? 29  SER A O   1 
ATOM   2354 C  CB  . SER B 1 31  ? -30.605 -43.462 25.204  1.00  8.07  ? 29  SER A CB  1 
ATOM   2355 O  OG  . SER B 1 31  ? -29.601 -43.707 24.198  1.00  7.96  ? 29  SER A OG  1 
ATOM   2356 N  N   . PRO B 1 32  ? -31.214 -43.970 28.290  1.00  8.73  ? 30  PRO A N   1 
ATOM   2357 C  CA  . PRO B 1 32  ? -29.804 -43.619 28.516  1.00  9.23  ? 30  PRO A CA  1 
ATOM   2358 C  C   . PRO B 1 32  ? -29.001 -44.876 28.954  1.00  10.03 ? 30  PRO A C   1 
ATOM   2359 O  O   . PRO B 1 32  ? -29.495 -46.017 28.831  1.00  10.32 ? 30  PRO A O   1 
ATOM   2360 C  CB  . PRO B 1 32  ? -29.918 -42.598 29.676  1.00  9.67  ? 30  PRO A CB  1 
ATOM   2361 C  CG  . PRO B 1 32  ? -31.071 -43.240 30.521  1.00  9.11  ? 30  PRO A CG  1 
ATOM   2362 C  CD  . PRO B 1 32  ? -32.074 -43.714 29.494  1.00  9.30  ? 30  PRO A CD  1 
ATOM   2363 N  N   . ILE B 1 33  ? -27.748 -44.658 29.278  1.00  10.18 ? 31  ILE A N   1 
ATOM   2364 C  CA  . ILE B 1 33  ? -26.788 -45.752 29.564  1.00  11.64 ? 31  ILE A CA  1 
ATOM   2365 C  C   . ILE B 1 33  ? -25.914 -45.365 30.762  1.00  11.84 ? 31  ILE A C   1 
ATOM   2366 O  O   . ILE B 1 33  ? -25.925 -44.215 31.259  1.00  11.10 ? 31  ILE A O   1 
ATOM   2367 C  CB  . ILE B 1 33  ? -25.842 -46.095 28.379  1.00  11.04 ? 31  ILE A CB  1 
ATOM   2368 C  CG1 . ILE B 1 33  ? -24.945 -44.916 28.030  1.00  10.82 ? 31  ILE A CG1 1 
ATOM   2369 C  CG2 . ILE B 1 33  ? -26.612 -46.715 27.198  1.00  12.15 ? 31  ILE A CG2 1 
ATOM   2370 C  CD1 . ILE B 1 33  ? -23.696 -45.194 27.189  1.00  11.62 ? 31  ILE A CD1 1 
ATOM   2371 N  N   . GLU B 1 34  ? -25.251 -46.381 31.348  1.00  12.37 ? 32  GLU A N   1 
ATOM   2372 C  CA  . GLU B 1 34  ? -24.105 -46.129 32.233  1.00  11.58 ? 32  GLU A CA  1 
ATOM   2373 C  C   . GLU B 1 34  ? -22.786 -46.010 31.485  1.00  11.53 ? 32  GLU A C   1 
ATOM   2374 O  O   . GLU B 1 34  ? -22.505 -46.813 30.624  1.00  13.89 ? 32  GLU A O   1 
ATOM   2375 C  CB  . GLU B 1 34  ? -23.996 -47.356 33.204  1.00  12.79 ? 32  GLU A CB  1 
ATOM   2376 C  CG  . GLU B 1 34  ? -25.093 -47.383 34.204  1.00  14.50 ? 32  GLU A CG  1 
ATOM   2377 C  CD  . GLU B 1 34  ? -24.829 -48.530 35.239  1.00  17.62 ? 32  GLU A CD  1 
ATOM   2378 O  OE1 . GLU B 1 34  ? -24.166 -48.191 36.275  1.00  22.45 ? 32  GLU A OE1 1 
ATOM   2379 O  OE2 . GLU B 1 34  ? -25.261 -49.676 34.982  1.00  16.06 ? 32  GLU A OE2 1 
ATOM   2380 N  N   . ILE B 1 35  ? -21.988 -45.010 31.804  1.00  15.12 ? 33  ILE A N   1 
ATOM   2381 C  CA  . ILE B 1 35  ? -20.700 -44.843 31.132  1.00  15.83 ? 33  ILE A CA  1 
ATOM   2382 C  C   . ILE B 1 35  ? -19.628 -45.273 32.151  1.00  17.81 ? 33  ILE A C   1 
ATOM   2383 O  O   . ILE B 1 35  ? -19.518 -44.659 33.163  1.00  16.09 ? 33  ILE A O   1 
ATOM   2384 C  CB  . ILE B 1 35  ? -20.509 -43.337 30.771  1.00  17.23 ? 33  ILE A CB  1 
ATOM   2385 C  CG1 . ILE B 1 35  ? -21.676 -42.875 29.816  1.00  15.81 ? 33  ILE A CG1 1 
ATOM   2386 C  CG2 . ILE B 1 35  ? -19.120 -43.074 30.203  1.00  16.98 ? 33  ILE A CG2 1 
ATOM   2387 C  CD1 . ILE B 1 35  ? -21.766 -41.391 29.499  1.00  18.09 ? 33  ILE A CD1 1 
ATOM   2388 N  N   . LYS B 1 36  ? -18.893 -46.324 31.771  1.00  18.36 ? 34  LYS A N   1 
ATOM   2389 C  CA  . LYS B 1 36  ? -17.787 -46.885 32.565  1.00  22.13 ? 34  LYS A CA  1 
ATOM   2390 C  C   . LYS B 1 36  ? -16.501 -46.260 31.988  1.00  21.53 ? 34  LYS A C   1 
ATOM   2391 O  O   . LYS B 1 36  ? -15.989 -46.717 30.959  1.00  24.85 ? 34  LYS A O   1 
ATOM   2392 C  CB  . LYS B 1 36  ? -17.850 -48.390 32.368  1.00  24.87 ? 34  LYS A CB  1 
ATOM   2393 C  CG  . LYS B 1 36  ? -17.454 -49.155 33.580  1.00  36.68 ? 34  LYS A CG  1 
ATOM   2394 C  CD  . LYS B 1 36  ? -15.986 -49.397 33.511  1.00  37.20 ? 34  LYS A CD  1 
ATOM   2395 C  CE  . LYS B 1 36  ? -15.785 -50.860 33.253  1.00  44.77 ? 34  LYS A CE  1 
ATOM   2396 N  NZ  . LYS B 1 36  ? -17.078 -51.326 32.694  1.00  47.33 ? 34  LYS A NZ  1 
ATOM   2397 N  N   . THR B 1 37  ? -15.995 -45.194 32.618  1.00  23.11 ? 35  THR A N   1 
ATOM   2398 C  CA  . THR B 1 37  ? -14.821 -44.481 31.990  1.00  24.71 ? 35  THR A CA  1 
ATOM   2399 C  C   . THR B 1 37  ? -13.580 -45.377 31.679  1.00  27.55 ? 35  THR A C   1 
ATOM   2400 O  O   . THR B 1 37  ? -12.895 -45.158 30.641  1.00  29.41 ? 35  THR A O   1 
ATOM   2401 C  CB  . THR B 1 37  ? -14.447 -43.159 32.664  1.00  22.26 ? 35  THR A CB  1 
ATOM   2402 O  OG1 . THR B 1 37  ? -14.008 -43.405 33.990  1.00  25.46 ? 35  THR A OG1 1 
ATOM   2403 C  CG2 . THR B 1 37  ? -15.696 -42.261 32.737  1.00  25.42 ? 35  THR A CG2 1 
ATOM   2404 N  N   . LYS B 1 38  ? -13.291 -46.391 32.510  1.00  26.79 ? 36  LYS A N   1 
ATOM   2405 C  CA  . LYS B 1 38  ? -12.101 -47.212 32.249  1.00  30.38 ? 36  LYS A CA  1 
ATOM   2406 C  C   . LYS B 1 38  ? -12.193 -47.985 30.928  1.00  32.77 ? 36  LYS A C   1 
ATOM   2407 O  O   . LYS B 1 38  ? -11.170 -48.311 30.351  1.00  33.00 ? 36  LYS A O   1 
ATOM   2408 C  CB  . LYS B 1 38  ? -11.689 -48.132 33.431  1.00  38.74 ? 36  LYS A CB  1 
ATOM   2409 C  CG  . LYS B 1 38  ? -12.522 -49.389 33.688  1.00  45.85 ? 36  LYS A CG  1 
ATOM   2410 C  CD  . LYS B 1 38  ? -11.688 -50.574 34.236  1.00  51.50 ? 36  LYS A CD  1 
ATOM   2411 C  CE  . LYS B 1 38  ? -10.945 -50.266 35.558  1.00  55.59 ? 36  LYS A CE  1 
ATOM   2412 N  NZ  . LYS B 1 38  ? -10.511 -51.465 36.369  1.00  50.85 ? 36  LYS A NZ  1 
ATOM   2413 N  N   . GLU B 1 39  ? -13.425 -48.188 30.433  1.00  31.64 ? 37  GLU A N   1 
ATOM   2414 C  CA  . GLU B 1 39  ? -13.619 -48.830 29.154  1.00  32.52 ? 37  GLU A CA  1 
ATOM   2415 C  C   . GLU B 1 39  ? -13.791 -47.923 27.934  1.00  32.57 ? 37  GLU A C   1 
ATOM   2416 O  O   . GLU B 1 39  ? -14.014 -48.447 26.854  1.00  39.92 ? 37  GLU A O   1 
ATOM   2417 C  CB  . GLU B 1 39  ? -14.735 -49.855 29.237  1.00  37.80 ? 37  GLU A CB  1 
ATOM   2418 C  CG  . GLU B 1 39  ? -14.279 -51.076 30.037  1.00  45.39 ? 37  GLU A CG  1 
ATOM   2419 C  CD  . GLU B 1 39  ? -15.292 -52.207 30.015  1.00  49.27 ? 37  GLU A CD  1 
ATOM   2420 O  OE1 . GLU B 1 39  ? -14.858 -53.384 30.108  1.00  53.21 ? 37  GLU A OE1 1 
ATOM   2421 O  OE2 . GLU B 1 39  ? -16.501 -51.902 29.886  1.00  47.76 ? 37  GLU A OE2 1 
ATOM   2422 N  N   . VAL B 1 40  ? -13.648 -46.604 28.085  1.00  25.12 ? 38  VAL A N   1 
ATOM   2423 C  CA  . VAL B 1 40  ? -13.973 -45.690 27.007  1.00  24.85 ? 38  VAL A CA  1 
ATOM   2424 C  C   . VAL B 1 40  ? -12.640 -45.405 26.358  1.00  26.28 ? 38  VAL A C   1 
ATOM   2425 O  O   . VAL B 1 40  ? -11.639 -45.227 27.045  1.00  31.22 ? 38  VAL A O   1 
ATOM   2426 C  CB  . VAL B 1 40  ? -14.630 -44.385 27.551  1.00  23.19 ? 38  VAL A CB  1 
ATOM   2427 C  CG1 . VAL B 1 40  ? -14.652 -43.241 26.530  1.00  24.81 ? 38  VAL A CG1 1 
ATOM   2428 C  CG2 . VAL B 1 40  ? -16.014 -44.635 28.085  1.00  18.57 ? 38  VAL A CG2 1 
ATOM   2429 N  N   . LYS B 1 41  ? -12.612 -45.363 25.045  1.00  25.88 ? 39  LYS A N   1 
ATOM   2430 C  CA  . LYS B 1 41  ? -11.384 -45.065 24.325  1.00  28.38 ? 39  LYS A CA  1 
ATOM   2431 C  C   . LYS B 1 41  ? -11.506 -43.649 23.802  1.00  25.02 ? 39  LYS A C   1 
ATOM   2432 O  O   . LYS B 1 41  ? -12.553 -43.296 23.216  1.00  23.71 ? 39  LYS A O   1 
ATOM   2433 C  CB  . LYS B 1 41  ? -11.263 -46.071 23.135  1.00  33.41 ? 39  LYS A CB  1 
ATOM   2434 C  CG  . LYS B 1 41  ? -10.833 -47.486 23.487  1.00  45.30 ? 39  LYS A CG  1 
ATOM   2435 C  CD  . LYS B 1 41  ? -9.500  -47.888 22.843  1.00  57.34 ? 39  LYS A CD  1 
ATOM   2436 C  CE  . LYS B 1 41  ? -8.696  -48.863 23.731  1.00  62.64 ? 39  LYS A CE  1 
ATOM   2437 N  NZ  . LYS B 1 41  ? -9.078  -50.308 23.643  1.00  68.57 ? 39  LYS A NZ  1 
ATOM   2438 N  N   . TYR B 1 42  ? -10.454 -42.841 23.999  1.00  20.07 ? 40  TYR A N   1 
ATOM   2439 C  CA  . TYR B 1 42  ? -10.300 -41.594 23.270  1.00  21.43 ? 40  TYR A CA  1 
ATOM   2440 C  C   . TYR B 1 42  ? -10.281 -41.936 21.759  1.00  22.41 ? 40  TYR A C   1 
ATOM   2441 O  O   . TYR B 1 42  ? -9.605  -42.906 21.312  1.00  23.53 ? 40  TYR A O   1 
ATOM   2442 C  CB  . TYR B 1 42  ? -8.971  -40.906 23.717  1.00  19.63 ? 40  TYR A CB  1 
ATOM   2443 C  CG  . TYR B 1 42  ? -8.520  -39.807 22.778  1.00  22.54 ? 40  TYR A CG  1 
ATOM   2444 C  CD1 . TYR B 1 42  ? -9.225  -38.595 22.720  1.00  20.83 ? 40  TYR A CD1 1 
ATOM   2445 C  CD2 . TYR B 1 42  ? -7.388  -39.967 21.965  1.00  22.17 ? 40  TYR A CD2 1 
ATOM   2446 C  CE1 . TYR B 1 42  ? -8.837  -37.594 21.837  1.00  24.28 ? 40  TYR A CE1 1 
ATOM   2447 C  CE2 . TYR B 1 42  ? -6.974  -38.964 21.100  1.00  25.51 ? 40  TYR A CE2 1 
ATOM   2448 C  CZ  . TYR B 1 42  ? -7.679  -37.785 21.044  1.00  25.12 ? 40  TYR A CZ  1 
ATOM   2449 O  OH  . TYR B 1 42  ? -7.276  -36.796 20.180  1.00  29.08 ? 40  TYR A OH  1 
ATOM   2450 N  N   . ASP B 1 43  ? -10.992 -41.133 20.952  1.00  22.14 ? 41  ASP A N   1 
ATOM   2451 C  CA  . ASP B 1 43  ? -10.922 -41.231 19.497  1.00  20.12 ? 41  ASP A CA  1 
ATOM   2452 C  C   . ASP B 1 43  ? -10.381 -39.957 18.826  1.00  21.90 ? 41  ASP A C   1 
ATOM   2453 O  O   . ASP B 1 43  ? -11.106 -38.931 18.717  1.00  21.48 ? 41  ASP A O   1 
ATOM   2454 C  CB  . ASP B 1 43  ? -12.354 -41.556 18.956  1.00  23.56 ? 41  ASP A CB  1 
ATOM   2455 C  CG  . ASP B 1 43  ? -12.402 -41.773 17.411  1.00  25.89 ? 41  ASP A CG  1 
ATOM   2456 O  OD1 . ASP B 1 43  ? -11.414 -41.528 16.693  1.00  25.05 ? 41  ASP A OD1 1 
ATOM   2457 O  OD2 . ASP B 1 43  ? -13.450 -42.232 16.905  1.00  23.20 ? 41  ASP A OD2 1 
ATOM   2458 N  N   . SER B 1 44  ? -9.127  -39.979 18.313  1.00  19.71 ? 42  SER A N   1 
ATOM   2459 C  CA  . SER B 1 44  ? -8.568  -38.800 17.677  1.00  20.65 ? 42  SER A CA  1 
ATOM   2460 C  C   . SER B 1 44  ? -9.253  -38.384 16.413  1.00  22.94 ? 42  SER A C   1 
ATOM   2461 O  O   . SER B 1 44  ? -9.015  -37.247 15.992  1.00  24.68 ? 42  SER A O   1 
ATOM   2462 C  CB  . SER B 1 44  ? -7.044  -38.991 17.395  1.00  27.06 ? 42  SER A CB  1 
ATOM   2463 O  OG  . SER B 1 44  ? -6.865  -40.191 16.714  1.00  27.78 ? 42  SER A OG  1 
ATOM   2464 N  N   . SER B 1 45  ? -10.113 -39.255 15.804  1.00  21.83 ? 43  SER A N   1 
ATOM   2465 C  CA  . SER B 1 45  ? -10.785 -38.885 14.534  1.00  21.99 ? 43  SER A CA  1 
ATOM   2466 C  C   . SER B 1 45  ? -12.027 -37.944 14.693  1.00  19.87 ? 43  SER A C   1 
ATOM   2467 O  O   . SER B 1 45  ? -12.481 -37.288 13.732  1.00  21.39 ? 43  SER A O   1 
ATOM   2468 C  CB  . SER B 1 45  ? -11.115 -40.120 13.697  1.00  25.42 ? 43  SER A CB  1 
ATOM   2469 O  OG  . SER B 1 45  ? -12.186 -40.823 14.251  1.00  23.51 ? 43  SER A OG  1 
ATOM   2470 N  N   . LEU B 1 46  ? -12.504 -37.829 15.909  1.00  20.60 ? 44  LEU A N   1 
ATOM   2471 C  CA  . LEU B 1 46  ? -13.559 -36.798 16.236  1.00  21.29 ? 44  LEU A CA  1 
ATOM   2472 C  C   . LEU B 1 46  ? -13.086 -35.372 15.982  1.00  21.98 ? 44  LEU A C   1 
ATOM   2473 O  O   . LEU B 1 46  ? -11.955 -35.047 16.347  1.00  22.24 ? 44  LEU A O   1 
ATOM   2474 C  CB  . LEU B 1 46  ? -14.018 -36.980 17.687  1.00  18.92 ? 44  LEU A CB  1 
ATOM   2475 C  CG  . LEU B 1 46  ? -14.624 -38.361 18.132  1.00  18.35 ? 44  LEU A CG  1 
ATOM   2476 C  CD1 . LEU B 1 46  ? -14.514 -38.458 19.626  1.00  16.27 ? 44  LEU A CD1 1 
ATOM   2477 C  CD2 . LEU B 1 46  ? -16.105 -38.572 17.756  1.00  21.51 ? 44  LEU A CD2 1 
ATOM   2478 N  N   . ARG B 1 47  ? -13.890 -34.559 15.259  1.00  20.96 ? 45  ARG A N   1 
ATOM   2479 C  CA  . ARG B 1 47  ? -13.504 -33.232 14.831  1.00  22.00 ? 45  ARG A CA  1 
ATOM   2480 C  C   . ARG B 1 47  ? -13.932 -32.272 15.957  1.00  20.37 ? 45  ARG A C   1 
ATOM   2481 O  O   . ARG B 1 47  ? -14.717 -32.669 16.856  1.00  19.55 ? 45  ARG A O   1 
ATOM   2482 C  CB  . ARG B 1 47  ? -14.236 -32.890 13.506  1.00  26.65 ? 45  ARG A CB  1 
ATOM   2483 C  CG  . ARG B 1 47  ? -13.876 -33.810 12.358  1.00  33.93 ? 45  ARG A CG  1 
ATOM   2484 C  CD  . ARG B 1 47  ? -13.396 -32.983 11.175  1.00  56.20 ? 45  ARG A CD  1 
ATOM   2485 N  NE  . ARG B 1 47  ? -14.200 -33.226 9.969   1.00  70.23 ? 45  ARG A NE  1 
ATOM   2486 C  CZ  . ARG B 1 47  ? -13.836 -33.984 8.930   1.00  73.07 ? 45  ARG A CZ  1 
ATOM   2487 N  NH1 . ARG B 1 47  ? -12.650 -34.599 8.903   1.00  73.50 ? 45  ARG A NH1 1 
ATOM   2488 N  NH2 . ARG B 1 47  ? -14.675 -34.117 7.906   1.00  68.20 ? 45  ARG A NH2 1 
ATOM   2489 N  N   . PRO B 1 48  ? -13.414 -31.027 15.986  1.00  18.24 ? 46  PRO A N   1 
ATOM   2490 C  CA  . PRO B 1 48  ? -13.926 -30.117 16.969  1.00  19.15 ? 46  PRO A CA  1 
ATOM   2491 C  C   . PRO B 1 48  ? -15.450 -30.019 16.921  1.00  18.38 ? 46  PRO A C   1 
ATOM   2492 O  O   . PRO B 1 48  ? -16.005 -29.901 15.838  1.00  20.14 ? 46  PRO A O   1 
ATOM   2493 C  CB  . PRO B 1 48  ? -13.242 -28.751 16.593  1.00  19.36 ? 46  PRO A CB  1 
ATOM   2494 C  CG  . PRO B 1 48  ? -11.909 -29.214 16.086  1.00  18.40 ? 46  PRO A CG  1 
ATOM   2495 C  CD  . PRO B 1 48  ? -12.263 -30.431 15.222  1.00  19.37 ? 46  PRO A CD  1 
ATOM   2496 N  N   . LEU B 1 49  ? -16.066 -29.946 18.090  1.00  19.87 ? 47  LEU A N   1 
ATOM   2497 C  CA  . LEU B 1 49  ? -17.531 -29.650 18.227  1.00  20.87 ? 47  LEU A CA  1 
ATOM   2498 C  C   . LEU B 1 49  ? -17.751 -28.209 17.948  1.00  20.34 ? 47  LEU A C   1 
ATOM   2499 O  O   . LEU B 1 49  ? -16.950 -27.397 18.373  1.00  22.10 ? 47  LEU A O   1 
ATOM   2500 C  CB  . LEU B 1 49  ? -17.941 -29.975 19.661  1.00  23.79 ? 47  LEU A CB  1 
ATOM   2501 C  CG  . LEU B 1 49  ? -19.371 -30.285 19.934  1.00  25.44 ? 47  LEU A CG  1 
ATOM   2502 C  CD1 . LEU B 1 49  ? -19.787 -31.496 19.116  1.00  24.33 ? 47  LEU A CD1 1 
ATOM   2503 C  CD2 . LEU B 1 49  ? -19.516 -30.599 21.403  1.00  29.26 ? 47  LEU A CD2 1 
ATOM   2504 N  N   . SER B 1 50  ? -18.767 -27.866 17.125  1.00  15.45 ? 48  SER A N   1 
ATOM   2505 C  CA  . SER B 1 50  ? -19.016 -26.483 16.675  1.00  14.13 ? 48  SER A CA  1 
ATOM   2506 C  C   . SER B 1 50  ? -20.462 -26.144 17.050  1.00  13.24 ? 48  SER A C   1 
ATOM   2507 O  O   . SER B 1 50  ? -21.352 -26.864 16.642  1.00  14.70 ? 48  SER A O   1 
ATOM   2508 C  CB  . SER B 1 50  ? -18.950 -26.435 15.130  1.00  13.13 ? 48  SER A CB  1 
ATOM   2509 O  OG  . SER B 1 50  ? -19.576 -25.262 14.595  1.00  14.29 ? 48  SER A OG  1 
ATOM   2510 N  N   . ILE B 1 51  ? -20.663 -25.176 17.933  1.00  12.43 ? 49  ILE A N   1 
ATOM   2511 C  CA  . ILE B 1 51  ? -22.011 -24.813 18.329  1.00  10.76 ? 49  ILE A CA  1 
ATOM   2512 C  C   . ILE B 1 51  ? -22.260 -23.350 17.937  1.00  11.82 ? 49  ILE A C   1 
ATOM   2513 O  O   . ILE B 1 51  ? -21.618 -22.406 18.520  1.00  12.37 ? 49  ILE A O   1 
ATOM   2514 C  CB  . ILE B 1 51  ? -22.132 -25.006 19.833  1.00  12.70 ? 49  ILE A CB  1 
ATOM   2515 C  CG1 . ILE B 1 51  ? -21.862 -26.484 20.168  1.00  13.02 ? 49  ILE A CG1 1 
ATOM   2516 C  CG2 . ILE B 1 51  ? -23.545 -24.575 20.266  1.00  12.20 ? 49  ILE A CG2 1 
ATOM   2517 C  CD1 . ILE B 1 51  ? -21.983 -26.797 21.667  1.00  12.66 ? 49  ILE A CD1 1 
ATOM   2518 N  N   . LYS B 1 52  ? -23.107 -23.134 16.923  1.00  10.65 ? 50  LYS A N   1 
ATOM   2519 C  CA  . LYS B 1 52  ? -23.507 -21.767 16.546  1.00  10.25 ? 50  LYS A CA  1 
ATOM   2520 C  C   . LYS B 1 52  ? -25.004 -21.646 16.949  1.00  11.50 ? 50  LYS A C   1 
ATOM   2521 O  O   . LYS B 1 52  ? -25.887 -22.313 16.375  1.00  11.75 ? 50  LYS A O   1 
ATOM   2522 C  CB  . LYS B 1 52  ? -23.388 -21.550 15.007  1.00  11.55 ? 50  LYS A CB  1 
ATOM   2523 C  CG  . LYS B 1 52  ? -24.041 -20.263 14.509  1.00  12.31 ? 50  LYS A CG  1 
ATOM   2524 C  CD  . LYS B 1 52  ? -23.579 -19.934 13.084  1.00  15.75 ? 50  LYS A CD  1 
ATOM   2525 C  CE  . LYS B 1 52  ? -24.260 -20.866 12.122  1.00  15.12 ? 50  LYS A CE  1 
ATOM   2526 N  NZ  . LYS B 1 52  ? -23.825 -20.382 10.771  1.00  21.88 ? 50  LYS A NZ  1 
ATOM   2527 N  N   A TYR B 1 53  ? -25.305 -20.869 17.991  0.50  10.00 ? 51  TYR A N   1 
ATOM   2528 N  N   B TYR B 1 53  ? -25.243 -20.699 17.856  0.50  10.74 ? 51  TYR A N   1 
ATOM   2529 C  CA  A TYR B 1 53  ? -26.714 -20.700 18.420  0.50  9.29  ? 51  TYR A CA  1 
ATOM   2530 C  CA  B TYR B 1 53  ? -26.532 -20.568 18.507  0.50  10.52 ? 51  TYR A CA  1 
ATOM   2531 C  C   A TYR B 1 53  ? -27.100 -19.230 18.425  0.50  9.93  ? 51  TYR A C   1 
ATOM   2532 C  C   B TYR B 1 53  ? -27.033 -19.128 18.360  0.50  10.82 ? 51  TYR A C   1 
ATOM   2533 O  O   A TYR B 1 53  ? -26.363 -18.370 18.924  0.50  9.32  ? 51  TYR A O   1 
ATOM   2534 O  O   B TYR B 1 53  ? -26.276 -18.169 18.659  0.50  10.12 ? 51  TYR A O   1 
ATOM   2535 C  CB  A TYR B 1 53  ? -26.998 -21.258 19.832  0.50  8.64  ? 51  TYR A CB  1 
ATOM   2536 C  CB  B TYR B 1 53  ? -26.420 -20.942 20.006  0.50  10.62 ? 51  TYR A CB  1 
ATOM   2537 C  CG  A TYR B 1 53  ? -26.937 -22.757 20.030  0.50  7.02  ? 51  TYR A CG  1 
ATOM   2538 C  CG  B TYR B 1 53  ? -27.738 -20.659 20.622  0.50  9.77  ? 51  TYR A CG  1 
ATOM   2539 C  CD1 A TYR B 1 53  ? -27.182 -23.671 18.954  0.50  6.51  ? 51  TYR A CD1 1 
ATOM   2540 C  CD1 B TYR B 1 53  ? -28.865 -21.357 20.177  0.50  9.98  ? 51  TYR A CD1 1 
ATOM   2541 C  CD2 A TYR B 1 53  ? -26.696 -23.287 21.320  0.50  6.67  ? 51  TYR A CD2 1 
ATOM   2542 C  CD2 B TYR B 1 53  ? -27.887 -19.590 21.524  0.50  10.30 ? 51  TYR A CD2 1 
ATOM   2543 C  CE1 A TYR B 1 53  ? -27.133 -25.030 19.176  0.50  6.49  ? 51  TYR A CE1 1 
ATOM   2544 C  CE1 B TYR B 1 53  ? -30.135 -21.011 20.647  0.50  9.63  ? 51  TYR A CE1 1 
ATOM   2545 C  CE2 A TYR B 1 53  ? -26.680 -24.667 21.540  0.50  6.53  ? 51  TYR A CE2 1 
ATOM   2546 C  CE2 B TYR B 1 53  ? -29.108 -19.254 22.020  0.50  9.18  ? 51  TYR A CE2 1 
ATOM   2547 C  CZ  A TYR B 1 53  ? -26.929 -25.530 20.478  0.50  6.18  ? 51  TYR A CZ  1 
ATOM   2548 C  CZ  B TYR B 1 53  ? -30.230 -19.969 21.559  0.50  9.34  ? 51  TYR A CZ  1 
ATOM   2549 O  OH  A TYR B 1 53  ? -26.801 -26.868 20.724  0.50  5.80  ? 51  TYR A OH  1 
ATOM   2550 O  OH  B TYR B 1 53  ? -31.442 -19.637 22.041  0.50  10.85 ? 51  TYR A OH  1 
ATOM   2551 N  N   . ASP B 1 54  ? -28.262 -18.953 17.848  1.00  10.84 ? 52  ASP A N   1 
ATOM   2552 C  CA  . ASP B 1 54  ? -28.852 -17.579 17.784  1.00  10.17 ? 52  ASP A CA  1 
ATOM   2553 C  C   . ASP B 1 54  ? -30.018 -17.490 18.784  1.00  11.33 ? 52  ASP A C   1 
ATOM   2554 O  O   . ASP B 1 54  ? -31.024 -18.194 18.633  1.00  9.70  ? 52  ASP A O   1 
ATOM   2555 C  CB  . ASP B 1 54  ? -29.431 -17.417 16.354  1.00  12.92 ? 52  ASP A CB  1 
ATOM   2556 C  CG  . ASP B 1 54  ? -29.886 -15.998 16.045  1.00  13.43 ? 52  ASP A CG  1 
ATOM   2557 O  OD1 . ASP B 1 54  ? -30.471 -15.323 16.919  1.00  13.08 ? 52  ASP A OD1 1 
ATOM   2558 O  OD2 . ASP B 1 54  ? -29.657 -15.568 14.880  1.00  14.75 ? 52  ASP A OD2 1 
ATOM   2559 N  N   . PRO B 1 55  ? -29.941 -16.580 19.756  1.00  10.70 ? 53  PRO A N   1 
ATOM   2560 C  CA  . PRO B 1 55  ? -31.013 -16.476 20.775  1.00  10.95 ? 53  PRO A CA  1 
ATOM   2561 C  C   . PRO B 1 55  ? -32.373 -16.137 20.173  1.00  12.20 ? 53  PRO A C   1 
ATOM   2562 O  O   . PRO B 1 55  ? -33.411 -16.448 20.772  1.00  14.05 ? 53  PRO A O   1 
ATOM   2563 C  CB  . PRO B 1 55  ? -30.530 -15.279 21.654  1.00  10.59 ? 53  PRO A CB  1 
ATOM   2564 C  CG  . PRO B 1 55  ? -29.010 -15.317 21.511  1.00  10.86 ? 53  PRO A CG  1 
ATOM   2565 C  CD  . PRO B 1 55  ? -28.802 -15.626 20.046  1.00  10.07 ? 53  PRO A CD  1 
ATOM   2566 N  N   . SER B 1 56  ? -32.404 -15.476 19.004  1.00  12.34 ? 54  SER A N   1 
ATOM   2567 C  CA  . SER B 1 56  ? -33.718 -15.237 18.322  1.00  13.61 ? 54  SER A CA  1 
ATOM   2568 C  C   . SER B 1 56  ? -34.384 -16.474 17.722  1.00  13.03 ? 54  SER A C   1 
ATOM   2569 O  O   . SER B 1 56  ? -35.540 -16.417 17.306  1.00  13.89 ? 54  SER A O   1 
ATOM   2570 C  CB  . SER B 1 56  ? -33.575 -14.089 17.276  1.00  12.92 ? 54  SER A CB  1 
ATOM   2571 O  OG  . SER B 1 56  ? -33.071 -14.575 16.032  1.00  17.70 ? 54  SER A OG  1 
ATOM   2572 N  N   . SER B 1 57  ? -33.706 -17.630 17.696  1.00  10.90 ? 55  SER A N   1 
ATOM   2573 C  CA  . SER B 1 57  ? -34.335 -18.843 17.171  1.00  10.57 ? 55  SER A CA  1 
ATOM   2574 C  C   . SER B 1 57  ? -35.352 -19.435 18.156  1.00  10.20 ? 55  SER A C   1 
ATOM   2575 O  O   . SER B 1 57  ? -36.216 -20.230 17.713  1.00  12.34 ? 55  SER A O   1 
ATOM   2576 C  CB  . SER B 1 57  ? -33.241 -19.931 16.979  1.00  10.46 ? 55  SER A CB  1 
ATOM   2577 O  OG  . SER B 1 57  ? -32.349 -19.556 15.948  1.00  15.62 ? 55  SER A OG  1 
ATOM   2578 N  N   . ALA B 1 58  ? -35.248 -19.074 19.450  1.00  10.29 ? 56  ALA A N   1 
ATOM   2579 C  CA  . ALA B 1 58  ? -36.237 -19.633 20.475  1.00  11.70 ? 56  ALA A CA  1 
ATOM   2580 C  C   . ALA B 1 58  ? -37.597 -19.013 20.190  1.00  13.42 ? 56  ALA A C   1 
ATOM   2581 O  O   . ALA B 1 58  ? -37.666 -17.791 19.912  1.00  14.57 ? 56  ALA A O   1 
ATOM   2582 C  CB  . ALA B 1 58  ? -35.752 -19.370 21.909  1.00  11.27 ? 56  ALA A CB  1 
ATOM   2583 N  N   . LYS B 1 59  ? -38.653 -19.803 20.246  1.00  11.79 ? 57  LYS A N   1 
ATOM   2584 C  CA  . LYS B 1 59  ? -39.995 -19.249 19.965  1.00  14.74 ? 57  LYS A CA  1 
ATOM   2585 C  C   . LYS B 1 59  ? -41.000 -19.386 21.115  1.00  12.29 ? 57  LYS A C   1 
ATOM   2586 O  O   . LYS B 1 59  ? -41.721 -18.418 21.404  1.00  13.03 ? 57  LYS A O   1 
ATOM   2587 C  CB  . LYS B 1 59  ? -40.547 -20.012 18.768  1.00  17.05 ? 57  LYS A CB  1 
ATOM   2588 C  CG  . LYS B 1 59  ? -39.855 -19.674 17.434  1.00  21.87 ? 57  LYS A CG  1 
ATOM   2589 C  CD  . LYS B 1 59  ? -39.450 -18.196 17.336  1.00  25.90 ? 57  LYS A CD  1 
ATOM   2590 C  CE  . LYS B 1 59  ? -38.660 -17.937 16.047  1.00  31.08 ? 57  LYS A CE  1 
ATOM   2591 N  NZ  . LYS B 1 59  ? -37.933 -16.638 16.138  1.00  27.76 ? 57  LYS A NZ  1 
ATOM   2592 N  N   . ILE B 1 60  ? -41.110 -20.584 21.696  1.00  10.59 ? 58  ILE A N   1 
ATOM   2593 C  CA  . ILE B 1 60  ? -42.175 -20.817 22.709  1.00  11.45 ? 58  ILE A CA  1 
ATOM   2594 C  C   . ILE B 1 60  ? -41.639 -21.747 23.787  1.00  11.55 ? 58  ILE A C   1 
ATOM   2595 O  O   . ILE B 1 60  ? -40.716 -22.545 23.505  1.00  10.88 ? 58  ILE A O   1 
ATOM   2596 C  CB  . ILE B 1 60  ? -43.544 -21.389 22.146  1.00  13.26 ? 58  ILE A CB  1 
ATOM   2597 C  CG1 . ILE B 1 60  ? -43.409 -22.649 21.383  1.00  15.64 ? 58  ILE A CG1 1 
ATOM   2598 C  CG2 . ILE B 1 60  ? -44.112 -20.462 21.035  1.00  16.68 ? 58  ILE A CG2 1 
ATOM   2599 C  CD1 . ILE B 1 60  ? -44.727 -23.411 21.242  1.00  19.94 ? 58  ILE A CD1 1 
ATOM   2600 N  N   . ILE B 1 61  ? -42.208 -21.663 24.982  1.00  9.70  ? 59  ILE A N   1 
ATOM   2601 C  CA  . ILE B 1 61  ? -41.941 -22.724 25.969  1.00  10.15 ? 59  ILE A CA  1 
ATOM   2602 C  C   . ILE B 1 61  ? -43.319 -23.320 26.289  1.00  11.03 ? 59  ILE A C   1 
ATOM   2603 O  O   . ILE B 1 61  ? -44.362 -22.516 26.395  1.00  12.03 ? 59  ILE A O   1 
ATOM   2604 C  CB  . ILE B 1 61  ? -41.210 -22.221 27.223  1.00  11.24 ? 59  ILE A CB  1 
ATOM   2605 C  CG1 . ILE B 1 61  ? -40.830 -23.379 28.191  1.00  11.17 ? 59  ILE A CG1 1 
ATOM   2606 C  CG2 . ILE B 1 61  ? -42.041 -21.161 28.001  1.00  10.16 ? 59  ILE A CG2 1 
ATOM   2607 C  CD1 . ILE B 1 61  ? -39.910 -22.917 29.348  1.00  13.70 ? 59  ILE A CD1 1 
ATOM   2608 N  N   . SER B 1 62  ? -43.387 -24.648 26.462  1.00  11.20 ? 60  SER A N   1 
ATOM   2609 C  CA  . SER B 1 62  ? -44.678 -25.310 26.730  1.00  11.98 ? 60  SER A CA  1 
ATOM   2610 C  C   . SER B 1 62  ? -44.511 -26.417 27.749  1.00  12.71 ? 60  SER A C   1 
ATOM   2611 O  O   . SER B 1 62  ? -43.382 -26.909 27.946  1.00  11.41 ? 60  SER A O   1 
ATOM   2612 C  CB  . SER B 1 62  ? -45.228 -25.817 25.410  1.00  15.78 ? 60  SER A CB  1 
ATOM   2613 O  OG  . SER B 1 62  ? -44.458 -26.945 24.988  1.00  16.66 ? 60  SER A OG  1 
ATOM   2614 N  N   . ASN B 1 63  ? -45.601 -26.832 28.366  1.00  10.95 ? 61  ASN A N   1 
ATOM   2615 C  CA  . ASN B 1 63  ? -45.585 -28.044 29.252  1.00  11.78 ? 61  ASN A CA  1 
ATOM   2616 C  C   . ASN B 1 63  ? -46.210 -29.183 28.436  1.00  12.00 ? 61  ASN A C   1 
ATOM   2617 O  O   . ASN B 1 63  ? -47.408 -29.185 28.085  1.00  12.88 ? 61  ASN A O   1 
ATOM   2618 C  CB  . ASN B 1 63  ? -46.384 -27.732 30.540  1.00  11.86 ? 61  ASN A CB  1 
ATOM   2619 C  CG  . ASN B 1 63  ? -46.525 -28.957 31.418  1.00  12.16 ? 61  ASN A CG  1 
ATOM   2620 O  OD1 . ASN B 1 63  ? -46.146 -30.063 31.039  1.00  13.18 ? 61  ASN A OD1 1 
ATOM   2621 N  ND2 . ASN B 1 63  ? -47.026 -28.756 32.617  1.00  11.43 ? 61  ASN A ND2 1 
ATOM   2622 N  N   . SER B 1 64  ? -45.409 -30.185 28.074  1.00  12.84 ? 62  SER A N   1 
ATOM   2623 C  CA  . SER B 1 64  ? -45.905 -31.285 27.264  1.00  12.56 ? 62  SER A CA  1 
ATOM   2624 C  C   . SER B 1 64  ? -46.616 -32.326 28.134  1.00  12.47 ? 62  SER A C   1 
ATOM   2625 O  O   . SER B 1 64  ? -47.099 -33.344 27.567  1.00  14.56 ? 62  SER A O   1 
ATOM   2626 C  CB  . SER B 1 64  ? -44.712 -32.028 26.647  1.00  12.69 ? 62  SER A CB  1 
ATOM   2627 O  OG  . SER B 1 64  ? -43.884 -32.577 27.750  1.00  11.88 ? 62  SER A OG  1 
ATOM   2628 N  N   . GLY B 1 65  ? -46.540 -32.176 29.457  1.00  10.92 ? 63  GLY A N   1 
ATOM   2629 C  CA  . GLY B 1 65  ? -47.030 -33.221 30.452  1.00  12.06 ? 63  GLY A CA  1 
ATOM   2630 C  C   . GLY B 1 65  ? -45.870 -34.119 30.873  1.00  11.06 ? 63  GLY A C   1 
ATOM   2631 O  O   . GLY B 1 65  ? -46.022 -34.858 31.868  1.00  11.97 ? 63  GLY A O   1 
ATOM   2632 N  N   . HIS B 1 66  ? -44.708 -34.093 30.115  1.00  9.68  ? 64  HIS A N   1 
ATOM   2633 C  CA  . HIS B 1 66  ? -43.563 -34.966 30.461  1.00  9.20  ? 64  HIS A CA  1 
ATOM   2634 C  C   . HIS B 1 66  ? -42.269 -34.164 30.779  1.00  9.43  ? 64  HIS A C   1 
ATOM   2635 O  O   . HIS B 1 66  ? -41.366 -34.708 31.357  1.00  8.96  ? 64  HIS A O   1 
ATOM   2636 C  CB  . HIS B 1 66  ? -43.251 -35.872 29.259  1.00  11.23 ? 64  HIS A CB  1 
ATOM   2637 C  CG  . HIS B 1 66  ? -44.470 -36.376 28.574  1.00  13.20 ? 64  HIS A CG  1 
ATOM   2638 N  ND1 . HIS B 1 66  ? -45.286 -37.270 29.167  1.00  16.14 ? 64  HIS A ND1 1 
ATOM   2639 C  CD2 . HIS B 1 66  ? -44.877 -36.253 27.284  1.00  14.31 ? 64  HIS A CD2 1 
ATOM   2640 C  CE1 . HIS B 1 66  ? -46.322 -37.566 28.301  1.00  17.41 ? 64  HIS A CE1 1 
ATOM   2641 N  NE2 . HIS B 1 66  ? -46.051 -36.977 27.154  1.00  18.69 ? 64  HIS A NE2 1 
ATOM   2642 N  N   . SER B 1 67  ? -42.270 -32.894 30.372  1.00  7.77  ? 65  SER A N   1 
ATOM   2643 C  CA  . SER B 1 67  ? -41.215 -31.902 30.771  1.00  9.04  ? 65  SER A CA  1 
ATOM   2644 C  C   . SER B 1 67  ? -41.673 -30.559 30.303  1.00  8.83  ? 65  SER A C   1 
ATOM   2645 O  O   . SER B 1 67  ? -42.806 -30.386 29.779  1.00  9.28  ? 65  SER A O   1 
ATOM   2646 C  CB  . SER B 1 67  ? -39.873 -32.275 30.002  1.00  8.43  ? 65  SER A CB  1 
ATOM   2647 O  OG  . SER B 1 67  ? -38.776 -31.476 30.540  1.00  9.89  ? 65  SER A OG  1 
ATOM   2648 N  N   . PHE B 1 68  ? -40.844 -29.542 30.464  1.00  9.21  ? 66  PHE A N   1 
ATOM   2649 C  CA  . PHE B 1 68  ? -41.116 -28.290 29.688  1.00  8.87  ? 66  PHE A CA  1 
ATOM   2650 C  C   . PHE B 1 68  ? -40.368 -28.479 28.383  1.00  10.20 ? 66  PHE A C   1 
ATOM   2651 O  O   . PHE B 1 68  ? -39.362 -29.221 28.312  1.00  12.00 ? 66  PHE A O   1 
ATOM   2652 C  CB  . PHE B 1 68  ? -40.593 -26.990 30.437  1.00  8.60  ? 66  PHE A CB  1 
ATOM   2653 C  CG  . PHE B 1 68  ? -39.085 -26.887 30.480  1.00  8.66  ? 66  PHE A CG  1 
ATOM   2654 C  CD1 . PHE B 1 68  ? -38.385 -27.330 31.597  1.00  9.11  ? 66  PHE A CD1 1 
ATOM   2655 C  CD2 . PHE B 1 68  ? -38.338 -26.450 29.358  1.00  9.31  ? 66  PHE A CD2 1 
ATOM   2656 C  CE1 . PHE B 1 68  ? -36.967 -27.265 31.621  1.00  8.73  ? 66  PHE A CE1 1 
ATOM   2657 C  CE2 . PHE B 1 68  ? -36.926 -26.394 29.385  1.00  9.98  ? 66  PHE A CE2 1 
ATOM   2658 C  CZ  . PHE B 1 68  ? -36.245 -26.782 30.518  1.00  9.96  ? 66  PHE A CZ  1 
ATOM   2659 N  N   . ASN B 1 69  ? -40.838 -27.830 27.314  1.00  9.77  ? 67  ASN A N   1 
ATOM   2660 C  CA  . ASN B 1 69  ? -40.091 -27.919 26.016  1.00  9.72  ? 67  ASN A CA  1 
ATOM   2661 C  C   . ASN B 1 69  ? -39.903 -26.497 25.562  1.00  9.73  ? 67  ASN A C   1 
ATOM   2662 O  O   . ASN B 1 69  ? -40.894 -25.800 25.322  1.00  10.56 ? 67  ASN A O   1 
ATOM   2663 C  CB  . ASN B 1 69  ? -40.922 -28.586 24.899  1.00  10.86 ? 67  ASN A CB  1 
ATOM   2664 C  CG  . ASN B 1 69  ? -41.192 -30.039 25.123  1.00  17.19 ? 67  ASN A CG  1 
ATOM   2665 O  OD1 . ASN B 1 69  ? -40.403 -30.724 25.798  1.00  20.02 ? 67  ASN A OD1 1 
ATOM   2666 N  ND2 . ASN B 1 69  ? -42.228 -30.565 24.398  1.00  17.90 ? 67  ASN A ND2 1 
ATOM   2667 N  N   . VAL B 1 70  ? -38.649 -26.048 25.353  1.00  10.02 ? 68  VAL A N   1 
ATOM   2668 C  CA  . VAL B 1 70  ? -38.455 -24.770 24.590  1.00  10.39 ? 68  VAL A CA  1 
ATOM   2669 C  C   . VAL B 1 70  ? -38.278 -25.143 23.129  1.00  10.39 ? 68  VAL A C   1 
ATOM   2670 O  O   . VAL B 1 70  ? -37.405 -25.971 22.765  1.00  11.01 ? 68  VAL A O   1 
ATOM   2671 C  CB  . VAL B 1 70  ? -37.159 -24.060 25.013  1.00  11.22 ? 68  VAL A CB  1 
ATOM   2672 C  CG1 . VAL B 1 70  ? -36.969 -22.775 24.156  1.00  10.81 ? 68  VAL A CG1 1 
ATOM   2673 C  CG2 . VAL B 1 70  ? -37.229 -23.774 26.521  1.00  12.31 ? 68  VAL A CG2 1 
ATOM   2674 N  N   . ASP B 1 71  ? -39.100 -24.585 22.253  1.00  10.10 ? 69  ASP A N   1 
ATOM   2675 C  CA  . ASP B 1 71  ? -39.046 -24.996 20.842  1.00  12.81 ? 69  ASP A CA  1 
ATOM   2676 C  C   . ASP B 1 71  ? -38.469 -23.829 20.019  1.00  12.70 ? 69  ASP A C   1 
ATOM   2677 O  O   . ASP B 1 71  ? -38.675 -22.637 20.364  1.00  13.09 ? 69  ASP A O   1 
ATOM   2678 C  CB  . ASP B 1 71  ? -40.464 -25.308 20.318  1.00  14.54 ? 69  ASP A CB  1 
ATOM   2679 C  CG  . ASP B 1 71  ? -41.041 -26.586 20.910  1.00  19.10 ? 69  ASP A CG  1 
ATOM   2680 O  OD1 . ASP B 1 71  ? -40.318 -27.533 21.227  1.00  19.59 ? 69  ASP A OD1 1 
ATOM   2681 O  OD2 . ASP B 1 71  ? -42.273 -26.667 21.065  1.00  20.67 ? 69  ASP A OD2 1 
ATOM   2682 N  N   . PHE B 1 72  ? -37.726 -24.236 18.986  1.00  12.62 ? 70  PHE A N   1 
ATOM   2683 C  CA  . PHE B 1 72  ? -36.980 -23.309 18.177  1.00  11.12 ? 70  PHE A CA  1 
ATOM   2684 C  C   . PHE B 1 72  ? -37.435 -23.403 16.730  1.00  13.17 ? 70  PHE A C   1 
ATOM   2685 O  O   . PHE B 1 72  ? -37.943 -24.424 16.212  1.00  12.92 ? 70  PHE A O   1 
ATOM   2686 C  CB  . PHE B 1 72  ? -35.453 -23.698 18.267  1.00  10.87 ? 70  PHE A CB  1 
ATOM   2687 C  CG  . PHE B 1 72  ? -34.872 -23.554 19.669  1.00  10.63 ? 70  PHE A CG  1 
ATOM   2688 C  CD1 . PHE B 1 72  ? -35.027 -24.591 20.608  1.00  11.96 ? 70  PHE A CD1 1 
ATOM   2689 C  CD2 . PHE B 1 72  ? -34.104 -22.422 20.037  1.00  11.58 ? 70  PHE A CD2 1 
ATOM   2690 C  CE1 . PHE B 1 72  ? -34.455 -24.463 21.890  1.00  9.89  ? 70  PHE A CE1 1 
ATOM   2691 C  CE2 . PHE B 1 72  ? -33.579 -22.277 21.323  1.00  10.35 ? 70  PHE A CE2 1 
ATOM   2692 C  CZ  . PHE B 1 72  ? -33.727 -23.327 22.195  1.00  10.07 ? 70  PHE A CZ  1 
ATOM   2693 N  N   . ASP B 1 73  ? -37.193 -22.272 16.064  1.00  15.48 ? 71  ASP A N   1 
ATOM   2694 C  CA  . ASP B 1 73  ? -37.458 -22.151 14.648  1.00  17.65 ? 71  ASP A CA  1 
ATOM   2695 C  C   . ASP B 1 73  ? -36.349 -22.843 14.032  1.00  23.01 ? 71  ASP A C   1 
ATOM   2696 O  O   . ASP B 1 73  ? -35.183 -22.368 14.145  1.00  26.20 ? 71  ASP A O   1 
ATOM   2697 C  CB  . ASP B 1 73  ? -37.296 -20.666 14.237  1.00  19.61 ? 71  ASP A CB  1 
ATOM   2698 C  CG  . ASP B 1 73  ? -37.561 -20.489 12.718  1.00  24.72 ? 71  ASP A CG  1 
ATOM   2699 O  OD1 . ASP B 1 73  ? -36.955 -21.202 11.922  1.00  23.38 ? 71  ASP A OD1 1 
ATOM   2700 O  OD2 . ASP B 1 73  ? -38.389 -19.660 12.368  1.00  32.47 ? 71  ASP A OD2 1 
ATOM   2701 N  N   . ASP B 1 74  ? -36.637 -24.000 13.469  1.00  18.97 ? 72  ASP A N   1 
ATOM   2702 C  CA  . ASP B 1 74  ? -35.758 -24.795 12.693  1.00  23.45 ? 72  ASP A CA  1 
ATOM   2703 C  C   . ASP B 1 74  ? -36.232 -24.906 11.104  1.00  24.32 ? 72  ASP A C   1 
ATOM   2704 O  O   . ASP B 1 74  ? -36.415 -26.029 10.492  1.00  22.74 ? 72  ASP A O   1 
ATOM   2705 C  CB  . ASP B 1 74  ? -35.884 -26.200 13.316  1.00  25.43 ? 72  ASP A CB  1 
ATOM   2706 C  CG  . ASP B 1 74  ? -37.272 -26.811 13.018  1.00  26.37 ? 72  ASP A CG  1 
ATOM   2707 O  OD1 . ASP B 1 74  ? -38.168 -26.012 12.502  1.00  24.69 ? 72  ASP A OD1 1 
ATOM   2708 O  OD2 . ASP B 1 74  ? -37.427 -28.067 13.222  1.00  24.01 ? 72  ASP A OD2 1 
ATOM   2709 N  N   . THR B 1 75  ? -36.572 -23.796 10.437  1.00  24.27 ? 73  THR A N   1 
ATOM   2710 C  CA  . THR B 1 75  ? -36.483 -23.899 8.936   1.00  21.31 ? 73  THR A CA  1 
ATOM   2711 C  C   . THR B 1 75  ? -35.265 -23.132 8.469   1.00  18.46 ? 73  THR A C   1 
ATOM   2712 O  O   . THR B 1 75  ? -34.991 -23.034 7.231   1.00  15.66 ? 73  THR A O   1 
ATOM   2713 C  CB  . THR B 1 75  ? -37.772 -23.661 8.060   1.00  25.39 ? 73  THR A CB  1 
ATOM   2714 O  OG1 . THR B 1 75  ? -38.346 -22.407 8.432   1.00  29.57 ? 73  THR A OG1 1 
ATOM   2715 C  CG2 . THR B 1 75  ? -38.813 -24.950 8.109   1.00  27.90 ? 73  THR A CG2 1 
ATOM   2716 N  N   . GLU B 1 76  ? -34.458 -22.630 9.406   1.00  15.07 ? 74  GLU A N   1 
ATOM   2717 C  CA  . GLU B 1 76  ? -33.212 -21.981 9.044   1.00  16.17 ? 74  GLU A CA  1 
ATOM   2718 C  C   . GLU B 1 76  ? -31.991 -22.593 9.753   1.00  13.54 ? 74  GLU A C   1 
ATOM   2719 O  O   . GLU B 1 76  ? -32.209 -23.346 10.701  1.00  12.33 ? 74  GLU A O   1 
ATOM   2720 C  CB  . GLU B 1 76  ? -33.308 -20.490 9.414   1.00  25.21 ? 74  GLU A CB  1 
ATOM   2721 C  CG  . GLU B 1 76  ? -33.853 -19.639 8.267   1.00  30.64 ? 74  GLU A CG  1 
ATOM   2722 C  CD  . GLU B 1 76  ? -33.327 -18.200 8.192   1.00  35.30 ? 74  GLU A CD  1 
ATOM   2723 O  OE1 . GLU B 1 76  ? -32.156 -17.923 8.493   1.00  41.59 ? 74  GLU A OE1 1 
ATOM   2724 O  OE2 . GLU B 1 76  ? -34.080 -17.325 7.735   1.00  46.41 ? 74  GLU A OE2 1 
ATOM   2725 N  N   . ASN B 1 77  ? -30.772 -22.293 9.286   1.00  13.39 ? 75  ASN A N   1 
ATOM   2726 C  CA  . ASN B 1 77  ? -29.516 -22.842 9.873   1.00  13.86 ? 75  ASN A CA  1 
ATOM   2727 C  C   . ASN B 1 77  ? -28.847 -21.767 10.724  1.00  12.85 ? 75  ASN A C   1 
ATOM   2728 O  O   . ASN B 1 77  ? -27.642 -21.724 10.815  1.00  13.38 ? 75  ASN A O   1 
ATOM   2729 C  CB  . ASN B 1 77  ? -28.550 -23.415 8.768   1.00  15.77 ? 75  ASN A CB  1 
ATOM   2730 C  CG  . ASN B 1 77  ? -29.008 -24.823 8.254   1.00  16.95 ? 75  ASN A CG  1 
ATOM   2731 O  OD1 . ASN B 1 77  ? -29.780 -25.472 8.954   1.00  16.40 ? 75  ASN A OD1 1 
ATOM   2732 N  ND2 . ASN B 1 77  ? -28.426 -25.335 7.160   1.00  15.15 ? 75  ASN A ND2 1 
ATOM   2733 N  N   . LYS B 1 78  ? -29.666 -20.960 11.412  1.00  12.28 ? 76  LYS A N   1 
ATOM   2734 C  CA  . LYS B 1 78  ? -29.082 -19.942 12.353  1.00  12.05 ? 76  LYS A CA  1 
ATOM   2735 C  C   . LYS B 1 78  ? -28.520 -20.631 13.611  1.00  12.89 ? 76  LYS A C   1 
ATOM   2736 O  O   . LYS B 1 78  ? -27.544 -20.147 14.218  1.00  10.27 ? 76  LYS A O   1 
ATOM   2737 C  CB  . LYS B 1 78  ? -30.162 -18.935 12.692  1.00  14.71 ? 76  LYS A CB  1 
ATOM   2738 C  CG  . LYS B 1 78  ? -30.504 -18.016 11.491  1.00  18.95 ? 76  LYS A CG  1 
ATOM   2739 C  CD  . LYS B 1 78  ? -31.508 -16.928 11.946  1.00  26.34 ? 76  LYS A CD  1 
ATOM   2740 C  CE  . LYS B 1 78  ? -31.745 -15.858 10.862  1.00  34.08 ? 76  LYS A CE  1 
ATOM   2741 N  NZ  . LYS B 1 78  ? -32.254 -14.591 11.469  1.00  38.10 ? 76  LYS A NZ  1 
ATOM   2742 N  N   . SER B 1 79  ? -29.167 -21.758 14.005  1.00  10.95 ? 77  SER A N   1 
ATOM   2743 C  CA  . SER B 1 79  ? -28.753 -22.480 15.250  1.00  9.63  ? 77  SER A CA  1 
ATOM   2744 C  C   . SER B 1 79  ? -28.526 -23.924 14.867  1.00  9.78  ? 77  SER A C   1 
ATOM   2745 O  O   . SER B 1 79  ? -29.498 -24.658 14.660  1.00  10.00 ? 77  SER A O   1 
ATOM   2746 C  CB  . SER B 1 79  ? -29.872 -22.378 16.351  1.00  9.38  ? 77  SER A CB  1 
ATOM   2747 O  OG  . SER B 1 79  ? -29.973 -21.011 16.728  1.00  9.95  ? 77  SER A OG  1 
ATOM   2748 N  N   . VAL B 1 80  ? -27.241 -24.294 14.859  1.00  10.05 ? 78  VAL A N   1 
ATOM   2749 C  CA  . VAL B 1 80  ? -26.818 -25.638 14.325  1.00  9.86  ? 78  VAL A CA  1 
ATOM   2750 C  C   . VAL B 1 80  ? -25.661 -26.168 15.134  1.00  10.12 ? 78  VAL A C   1 
ATOM   2751 O  O   . VAL B 1 80  ? -24.822 -25.410 15.719  1.00  10.15 ? 78  VAL A O   1 
ATOM   2752 C  CB  . VAL B 1 80  ? -26.421 -25.566 12.821  1.00  9.67  ? 78  VAL A CB  1 
ATOM   2753 C  CG1 . VAL B 1 80  ? -27.651 -25.178 11.926  1.00  10.77 ? 78  VAL A CG1 1 
ATOM   2754 C  CG2 . VAL B 1 80  ? -25.290 -24.519 12.630  1.00  12.14 ? 78  VAL A CG2 1 
ATOM   2755 N  N   . LEU B 1 81  ? -25.595 -27.499 15.164  1.00  9.94  ? 79  LEU A N   1 
ATOM   2756 C  CA  . LEU B 1 81  ? -24.570 -28.291 15.816  1.00  10.02 ? 79  LEU A CA  1 
ATOM   2757 C  C   . LEU B 1 81  ? -23.856 -29.032 14.703  1.00  10.42 ? 79  LEU A C   1 
ATOM   2758 O  O   . LEU B 1 81  ? -24.495 -29.685 13.918  1.00  10.69 ? 79  LEU A O   1 
ATOM   2759 C  CB  . LEU B 1 81  ? -25.245 -29.286 16.820  1.00  10.04 ? 79  LEU A CB  1 
ATOM   2760 C  CG  . LEU B 1 81  ? -24.176 -30.157 17.527  1.00  10.58 ? 79  LEU A CG  1 
ATOM   2761 C  CD1 . LEU B 1 81  ? -23.275 -29.370 18.523  1.00  10.66 ? 79  LEU A CD1 1 
ATOM   2762 C  CD2 . LEU B 1 81  ? -24.966 -31.286 18.266  1.00  11.01 ? 79  LEU A CD2 1 
ATOM   2763 N  N   . ARG B 1 82  ? -22.518 -28.868 14.673  1.00  11.71 ? 80  ARG A N   1 
ATOM   2764 C  CA  . ARG B 1 82  ? -21.655 -29.524 13.683  1.00  11.27 ? 80  ARG A CA  1 
ATOM   2765 C  C   . ARG B 1 82  ? -20.410 -30.060 14.365  1.00  11.74 ? 80  ARG A C   1 
ATOM   2766 O  O   . ARG B 1 82  ? -20.151 -29.800 15.572  1.00  11.67 ? 80  ARG A O   1 
ATOM   2767 C  CB  . ARG B 1 82  ? -21.312 -28.527 12.529  1.00  12.03 ? 80  ARG A CB  1 
ATOM   2768 C  CG  . ARG B 1 82  ? -22.460 -28.199 11.625  1.00  11.56 ? 80  ARG A CG  1 
ATOM   2769 C  CD  . ARG B 1 82  ? -22.075 -26.944 10.770  1.00  13.20 ? 80  ARG A CD  1 
ATOM   2770 N  NE  . ARG B 1 82  ? -21.930 -25.729 11.567  1.00  14.08 ? 80  ARG A NE  1 
ATOM   2771 C  CZ  . ARG B 1 82  ? -21.776 -24.476 11.074  1.00  15.52 ? 80  ARG A CZ  1 
ATOM   2772 N  NH1 . ARG B 1 82  ? -21.635 -24.287 9.762   1.00  14.23 ? 80  ARG A NH1 1 
ATOM   2773 N  NH2 . ARG B 1 82  ? -21.673 -23.427 11.936  1.00  14.47 ? 80  ARG A NH2 1 
ATOM   2774 N  N   . GLY B 1 83  ? -19.694 -30.921 13.651  1.00  11.69 ? 81  GLY A N   1 
ATOM   2775 C  CA  . GLY B 1 83  ? -18.446 -31.422 14.198  1.00  13.50 ? 81  GLY A CA  1 
ATOM   2776 C  C   . GLY B 1 83  ? -18.606 -32.611 15.167  1.00  13.36 ? 81  GLY A C   1 
ATOM   2777 O  O   . GLY B 1 83  ? -19.590 -33.375 15.162  1.00  13.81 ? 81  GLY A O   1 
ATOM   2778 N  N   . GLY B 1 84  ? -17.614 -32.780 16.033  1.00  13.53 ? 82  GLY A N   1 
ATOM   2779 C  CA  . GLY B 1 84  ? -17.628 -33.954 16.882  1.00  14.50 ? 82  GLY A CA  1 
ATOM   2780 C  C   . GLY B 1 84  ? -17.766 -35.252 16.070  1.00  12.48 ? 82  GLY A C   1 
ATOM   2781 O  O   . GLY B 1 84  ? -17.025 -35.486 15.096  1.00  17.26 ? 82  GLY A O   1 
ATOM   2782 N  N   . PRO B 1 85  ? -18.758 -36.108 16.425  1.00  12.17 ? 83  PRO A N   1 
ATOM   2783 C  CA  . PRO B 1 85  ? -18.978 -37.308 15.732  1.00  11.91 ? 83  PRO A CA  1 
ATOM   2784 C  C   . PRO B 1 85  ? -19.864 -37.154 14.484  1.00  11.89 ? 83  PRO A C   1 
ATOM   2785 O  O   . PRO B 1 85  ? -20.022 -38.124 13.721  1.00  12.04 ? 83  PRO A O   1 
ATOM   2786 C  CB  . PRO B 1 85  ? -19.664 -38.175 16.777  1.00  13.26 ? 83  PRO A CB  1 
ATOM   2787 C  CG  . PRO B 1 85  ? -20.594 -37.182 17.450  1.00  14.13 ? 83  PRO A CG  1 
ATOM   2788 C  CD  . PRO B 1 85  ? -19.671 -35.966 17.592  1.00  11.61 ? 83  PRO A CD  1 
ATOM   2789 N  N   . LEU B 1 86  ? -20.346 -35.954 14.220  1.00  11.20 ? 84  LEU A N   1 
ATOM   2790 C  CA  . LEU B 1 86  ? -21.381 -35.814 13.226  1.00  12.06 ? 84  LEU A CA  1 
ATOM   2791 C  C   . LEU B 1 86  ? -20.869 -35.571 11.813  1.00  13.92 ? 84  LEU A C   1 
ATOM   2792 O  O   . LEU B 1 86  ? -19.930 -34.811 11.611  1.00  13.68 ? 84  LEU A O   1 
ATOM   2793 C  CB  . LEU B 1 86  ? -22.310 -34.595 13.606  1.00  11.31 ? 84  LEU A CB  1 
ATOM   2794 C  CG  . LEU B 1 86  ? -22.886 -34.724 15.077  1.00  11.50 ? 84  LEU A CG  1 
ATOM   2795 C  CD1 . LEU B 1 86  ? -23.465 -33.326 15.420  1.00  11.79 ? 84  LEU A CD1 1 
ATOM   2796 C  CD2 . LEU B 1 86  ? -23.844 -35.953 15.282  1.00  10.77 ? 84  LEU A CD2 1 
ATOM   2797 N  N   . THR B 1 87  ? -21.592 -36.122 10.860  1.00  15.05 ? 85  THR A N   1 
ATOM   2798 C  CA  . THR B 1 87  ? -21.509 -35.758 9.432   1.00  15.22 ? 85  THR A CA  1 
ATOM   2799 C  C   . THR B 1 87  ? -22.624 -34.769 9.042   1.00  13.80 ? 85  THR A C   1 
ATOM   2800 O  O   . THR B 1 87  ? -23.822 -35.070 9.184   1.00  15.32 ? 85  THR A O   1 
ATOM   2801 C  CB  . THR B 1 87  ? -21.587 -37.063 8.574   1.00  17.30 ? 85  THR A CB  1 
ATOM   2802 O  OG1 . THR B 1 87  ? -20.466 -37.870 8.960   1.00  19.80 ? 85  THR A OG1 1 
ATOM   2803 C  CG2 . THR B 1 87  ? -21.424 -36.732 7.034   1.00  18.66 ? 85  THR A CG2 1 
ATOM   2804 N  N   . GLY B 1 88  ? -22.251 -33.588 8.539   1.00  12.44 ? 86  GLY A N   1 
ATOM   2805 C  CA  . GLY B 1 88  ? -23.316 -32.650 8.143   1.00  13.67 ? 86  GLY A CA  1 
ATOM   2806 C  C   . GLY B 1 88  ? -23.796 -31.751 9.306   1.00  15.01 ? 86  GLY A C   1 
ATOM   2807 O  O   . GLY B 1 88  ? -23.181 -31.791 10.434  1.00  13.73 ? 86  GLY A O   1 
ATOM   2808 N  N   . SER B 1 89  ? -24.839 -30.984 8.987   1.00  11.99 ? 87  SER A N   1 
ATOM   2809 C  CA  . SER B 1 89  ? -25.373 -29.946 9.878   1.00  13.16 ? 87  SER A CA  1 
ATOM   2810 C  C   . SER B 1 89  ? -26.675 -30.408 10.561  1.00  12.01 ? 87  SER A C   1 
ATOM   2811 O  O   . SER B 1 89  ? -27.611 -30.844 9.883   1.00  12.28 ? 87  SER A O   1 
ATOM   2812 C  CB  . SER B 1 89  ? -25.656 -28.686 9.062   1.00  11.93 ? 87  SER A CB  1 
ATOM   2813 O  OG  . SER B 1 89  ? -25.943 -27.624 9.975   1.00  13.29 ? 87  SER A OG  1 
ATOM   2814 N  N   . TYR B 1 90  ? -26.686 -30.309 11.905  1.00  10.45 ? 88  TYR A N   1 
ATOM   2815 C  CA  . TYR B 1 90  ? -27.870 -30.742 12.670  1.00  9.35  ? 88  TYR A CA  1 
ATOM   2816 C  C   . TYR B 1 90  ? -28.532 -29.503 13.302  1.00  9.80  ? 88  TYR A C   1 
ATOM   2817 O  O   . TYR B 1 90  ? -27.868 -28.695 14.082  1.00  10.91 ? 88  TYR A O   1 
ATOM   2818 C  CB  . TYR B 1 90  ? -27.429 -31.727 13.792  1.00  8.50  ? 88  TYR A CB  1 
ATOM   2819 C  CG  . TYR B 1 90  ? -27.164 -33.116 13.246  1.00  8.78  ? 88  TYR A CG  1 
ATOM   2820 C  CD1 . TYR B 1 90  ? -26.059 -33.364 12.441  1.00  8.57  ? 88  TYR A CD1 1 
ATOM   2821 C  CD2 . TYR B 1 90  ? -28.033 -34.168 13.506  1.00  9.59  ? 88  TYR A CD2 1 
ATOM   2822 C  CE1 . TYR B 1 90  ? -25.816 -34.624 11.926  1.00  9.30  ? 88  TYR A CE1 1 
ATOM   2823 C  CE2 . TYR B 1 90  ? -27.798 -35.432 12.995  1.00  8.80  ? 88  TYR A CE2 1 
ATOM   2824 C  CZ  . TYR B 1 90  ? -26.689 -35.654 12.207  1.00  10.20 ? 88  TYR A CZ  1 
ATOM   2825 O  OH  . TYR B 1 90  ? -26.452 -36.910 11.696  1.00  10.03 ? 88  TYR A OH  1 
ATOM   2826 N  N   . ARG B 1 91  ? -29.790 -29.321 12.942  1.00  8.46  ? 89  ARG A N   1 
ATOM   2827 C  CA  . ARG B 1 91  ? -30.522 -28.062 13.249  1.00  9.18  ? 89  ARG A CA  1 
ATOM   2828 C  C   . ARG B 1 91  ? -31.137 -28.123 14.622  1.00  7.69  ? 89  ARG A C   1 
ATOM   2829 O  O   . ARG B 1 91  ? -31.836 -29.133 14.922  1.00  8.05  ? 89  ARG A O   1 
ATOM   2830 C  CB  . ARG B 1 91  ? -31.606 -27.925 12.163  1.00  9.75  ? 89  ARG A CB  1 
ATOM   2831 C  CG  . ARG B 1 91  ? -32.224 -26.522 12.208  1.00  11.68 ? 89  ARG A CG  1 
ATOM   2832 C  CD  . ARG B 1 91  ? -33.289 -26.362 11.143  1.00  10.80 ? 89  ARG A CD  1 
ATOM   2833 N  NE  . ARG B 1 91  ? -32.581 -26.218 9.886   1.00  12.55 ? 89  ARG A NE  1 
ATOM   2834 C  CZ  . ARG B 1 91  ? -33.107 -26.469 8.701   1.00  11.62 ? 89  ARG A CZ  1 
ATOM   2835 N  NH1 . ARG B 1 91  ? -34.363 -26.846 8.589   1.00  11.06 ? 89  ARG A NH1 1 
ATOM   2836 N  NH2 . ARG B 1 91  ? -32.353 -26.306 7.622   1.00  10.50 ? 89  ARG A NH2 1 
ATOM   2837 N  N   . LEU B 1 92  ? -30.924 -27.111 15.482  1.00  7.58  ? 90  LEU A N   1 
ATOM   2838 C  CA  . LEU B 1 92  ? -31.551 -27.082 16.820  1.00  7.13  ? 90  LEU A CA  1 
ATOM   2839 C  C   . LEU B 1 92  ? -33.070 -27.133 16.742  1.00  7.65  ? 90  LEU A C   1 
ATOM   2840 O  O   . LEU B 1 92  ? -33.650 -26.347 16.001  1.00  8.32  ? 90  LEU A O   1 
ATOM   2841 C  CB  . LEU B 1 92  ? -31.026 -25.785 17.574  1.00  7.53  ? 90  LEU A CB  1 
ATOM   2842 C  CG  . LEU B 1 92  ? -31.672 -25.527 18.898  1.00  7.26  ? 90  LEU A CG  1 
ATOM   2843 C  CD1 . LEU B 1 92  ? -31.260 -26.723 19.812  1.00  8.02  ? 90  LEU A CD1 1 
ATOM   2844 C  CD2 . LEU B 1 92  ? -31.225 -24.210 19.535  1.00  8.68  ? 90  LEU A CD2 1 
ATOM   2845 N  N   . ARG B 1 93  ? -33.700 -27.996 17.526  1.00  7.78  ? 91  ARG A N   1 
ATOM   2846 C  CA  . ARG B 1 93  ? -35.158 -28.163 17.539  1.00  8.83  ? 91  ARG A CA  1 
ATOM   2847 C  C   . ARG B 1 93  ? -35.767 -27.839 18.884  1.00  9.39  ? 91  ARG A C   1 
ATOM   2848 O  O   . ARG B 1 93  ? -36.759 -27.125 18.960  1.00  9.44  ? 91  ARG A O   1 
ATOM   2849 C  CB  . ARG B 1 93  ? -35.464 -29.621 17.159  1.00  11.03 ? 91  ARG A CB  1 
ATOM   2850 C  CG  . ARG B 1 93  ? -36.939 -29.978 17.310  1.00  12.89 ? 91  ARG A CG  1 
ATOM   2851 C  CD  . ARG B 1 93  ? -37.849 -29.330 16.287  1.00  16.78 ? 91  ARG A CD  1 
ATOM   2852 N  NE  . ARG B 1 93  ? -39.190 -29.974 16.417  1.00  21.90 ? 91  ARG A NE  1 
ATOM   2853 C  CZ  . ARG B 1 93  ? -40.126 -29.978 15.470  1.00  31.16 ? 91  ARG A CZ  1 
ATOM   2854 N  NH1 . ARG B 1 93  ? -39.872 -29.340 14.291  1.00  30.38 ? 91  ARG A NH1 1 
ATOM   2855 N  NH2 . ARG B 1 93  ? -41.312 -30.623 15.686  1.00  31.60 ? 91  ARG A NH2 1 
ATOM   2856 N  N   A GLN B 1 94  ? -35.219 -28.384 19.963  0.50  8.55  ? 92  GLN A N   1 
ATOM   2857 N  N   B GLN B 1 94  ? -35.191 -28.400 19.949  0.50  8.28  ? 92  GLN A N   1 
ATOM   2858 C  CA  A GLN B 1 94  ? -35.899 -28.180 21.238  0.50  8.94  ? 92  GLN A CA  1 
ATOM   2859 C  CA  B GLN B 1 94  ? -35.846 -28.373 21.259  0.50  8.56  ? 92  GLN A CA  1 
ATOM   2860 C  C   A GLN B 1 94  ? -34.995 -28.499 22.423  0.50  8.61  ? 92  GLN A C   1 
ATOM   2861 C  C   B GLN B 1 94  ? -34.859 -28.425 22.421  0.50  8.24  ? 92  GLN A C   1 
ATOM   2862 O  O   A GLN B 1 94  ? -34.058 -29.301 22.279  0.50  8.31  ? 92  GLN A O   1 
ATOM   2863 O  O   B GLN B 1 94  ? -33.767 -29.018 22.289  0.50  7.61  ? 92  GLN A O   1 
ATOM   2864 C  CB  A GLN B 1 94  ? -37.258 -28.961 21.217  0.50  10.09 ? 92  GLN A CB  1 
ATOM   2865 C  CB  B GLN B 1 94  ? -36.794 -29.587 21.353  0.50  8.88  ? 92  GLN A CB  1 
ATOM   2866 C  CG  A GLN B 1 94  ? -37.297 -30.468 21.436  0.50  11.33 ? 92  GLN A CG  1 
ATOM   2867 C  CG  B GLN B 1 94  ? -37.725 -29.558 22.603  0.50  10.78 ? 92  GLN A CG  1 
ATOM   2868 C  CD  A GLN B 1 94  ? -37.279 -30.882 22.917  0.50  12.33 ? 92  GLN A CD  1 
ATOM   2869 C  CD  B GLN B 1 94  ? -38.574 -30.777 22.617  0.50  12.09 ? 92  GLN A CD  1 
ATOM   2870 O  OE1 A GLN B 1 94  ? -36.255 -30.768 23.538  0.50  14.40 ? 92  GLN A OE1 1 
ATOM   2871 O  OE1 B GLN B 1 94  ? -38.090 -31.915 22.966  0.50  15.87 ? 92  GLN A OE1 1 
ATOM   2872 N  NE2 A GLN B 1 94  ? -38.421 -31.326 23.493  0.50  13.37 ? 92  GLN A NE2 1 
ATOM   2873 N  NE2 B GLN B 1 94  ? -39.855 -30.609 22.239  0.50  13.03 ? 92  GLN A NE2 1 
ATOM   2874 N  N   . VAL B 1 95  ? -35.219 -27.828 23.545  1.00  8.16  ? 93  VAL A N   1 
ATOM   2875 C  CA  . VAL B 1 95  ? -34.471 -28.059 24.813  1.00  8.35  ? 93  VAL A CA  1 
ATOM   2876 C  C   . VAL B 1 95  ? -35.491 -28.512 25.863  1.00  8.99  ? 93  VAL A C   1 
ATOM   2877 O  O   . VAL B 1 95  ? -36.606 -27.912 25.941  1.00  7.91  ? 93  VAL A O   1 
ATOM   2878 C  CB  . VAL B 1 95  ? -33.756 -26.736 25.259  1.00  9.64  ? 93  VAL A CB  1 
ATOM   2879 C  CG1 . VAL B 1 95  ? -33.292 -26.924 26.732  1.00  9.69  ? 93  VAL A CG1 1 
ATOM   2880 C  CG2 . VAL B 1 95  ? -32.563 -26.452 24.303  1.00  10.39 ? 93  VAL A CG2 1 
ATOM   2881 N  N   . HIS B 1 96  ? -35.157 -29.556 26.664  1.00  8.53  ? 94  HIS A N   1 
ATOM   2882 C  CA  . HIS B 1 96  ? -36.017 -29.933 27.809  1.00  7.87  ? 94  HIS A CA  1 
ATOM   2883 C  C   . HIS B 1 96  ? -35.132 -30.485 28.902  1.00  8.22  ? 94  HIS A C   1 
ATOM   2884 O  O   . HIS B 1 96  ? -33.846 -30.486 28.785  1.00  7.90  ? 94  HIS A O   1 
ATOM   2885 C  CB  . HIS B 1 96  ? -37.065 -30.983 27.400  1.00  7.40  ? 94  HIS A CB  1 
ATOM   2886 C  CG  . HIS B 1 96  ? -36.477 -32.242 26.874  1.00  8.18  ? 94  HIS A CG  1 
ATOM   2887 N  ND1 . HIS B 1 96  ? -36.376 -32.492 25.535  1.00  9.18  ? 94  HIS A ND1 1 
ATOM   2888 C  CD2 . HIS B 1 96  ? -35.967 -33.362 27.542  1.00  8.35  ? 94  HIS A CD2 1 
ATOM   2889 C  CE1 . HIS B 1 96  ? -35.777 -33.723 25.353  1.00  8.94  ? 94  HIS A CE1 1 
ATOM   2890 N  NE2 . HIS B 1 96  ? -35.496 -34.250 26.574  1.00  8.09  ? 94  HIS A NE2 1 
ATOM   2891 N  N   . LEU B 1 97  ? -35.811 -30.930 30.008  1.00  7.39  ? 95  LEU A N   1 
ATOM   2892 C  CA  . LEU B 1 97  ? -35.027 -31.339 31.217  1.00  7.47  ? 95  LEU A CA  1 
ATOM   2893 C  C   . LEU B 1 97  ? -35.626 -32.565 31.882  1.00  7.20  ? 95  LEU A C   1 
ATOM   2894 O  O   . LEU B 1 97  ? -36.860 -32.720 31.854  1.00  8.21  ? 95  LEU A O   1 
ATOM   2895 C  CB  . LEU B 1 97  ? -35.030 -30.165 32.259  1.00  7.64  ? 95  LEU A CB  1 
ATOM   2896 C  CG  . LEU B 1 97  ? -34.167 -30.281 33.526  1.00  7.28  ? 95  LEU A CG  1 
ATOM   2897 C  CD1 . LEU B 1 97  ? -32.706 -30.079 33.089  1.00  9.19  ? 95  LEU A CD1 1 
ATOM   2898 C  CD2 . LEU B 1 97  ? -34.657 -29.137 34.458  1.00  9.54  ? 95  LEU A CD2 1 
ATOM   2899 N  N   . HIS B 1 98  ? -34.762 -33.371 32.497  1.00  7.15  ? 96  HIS A N   1 
ATOM   2900 C  CA  . HIS B 1 98  ? -35.192 -34.577 33.275  1.00  7.15  ? 96  HIS A CA  1 
ATOM   2901 C  C   . HIS B 1 98  ? -34.689 -34.355 34.700  1.00  7.04  ? 96  HIS A C   1 
ATOM   2902 O  O   . HIS B 1 98  ? -33.596 -33.864 34.924  1.00  7.17  ? 96  HIS A O   1 
ATOM   2903 C  CB  . HIS B 1 98  ? -34.630 -35.866 32.732  1.00  7.25  ? 96  HIS A CB  1 
ATOM   2904 C  CG  . HIS B 1 98  ? -35.002 -36.099 31.310  1.00  8.09  ? 96  HIS A CG  1 
ATOM   2905 N  ND1 . HIS B 1 98  ? -36.172 -36.716 30.969  1.00  7.32  ? 96  HIS A ND1 1 
ATOM   2906 C  CD2 . HIS B 1 98  ? -34.356 -35.765 30.115  1.00  8.67  ? 96  HIS A CD2 1 
ATOM   2907 C  CE1 . HIS B 1 98  ? -36.257 -36.827 29.625  1.00  8.73  ? 96  HIS A CE1 1 
ATOM   2908 N  NE2 . HIS B 1 98  ? -35.160 -36.260 29.080  1.00  7.37  ? 96  HIS A NE2 1 
ATOM   2909 N  N   . TRP B 1 99  ? -35.535 -34.742 35.647  1.00  7.70  ? 97  TRP A N   1 
ATOM   2910 C  CA  . TRP B 1 99  ? -35.172 -34.668 37.081  1.00  8.24  ? 97  TRP A CA  1 
ATOM   2911 C  C   . TRP B 1 99  ? -35.746 -35.845 37.831  1.00  9.26  ? 97  TRP A C   1 
ATOM   2912 O  O   . TRP B 1 99  ? -36.518 -36.646 37.289  1.00  9.32  ? 97  TRP A O   1 
ATOM   2913 C  CB  . TRP B 1 99  ? -35.605 -33.336 37.722  1.00  9.09  ? 97  TRP A CB  1 
ATOM   2914 C  CG  . TRP B 1 99  ? -37.095 -33.092 37.543  1.00  8.67  ? 97  TRP A CG  1 
ATOM   2915 C  CD1 . TRP B 1 99  ? -38.119 -33.572 38.343  1.00  8.73  ? 97  TRP A CD1 1 
ATOM   2916 C  CD2 . TRP B 1 99  ? -37.747 -32.330 36.460  1.00  8.67  ? 97  TRP A CD2 1 
ATOM   2917 N  NE1 . TRP B 1 99  ? -39.368 -33.145 37.887  1.00  9.25  ? 97  TRP A NE1 1 
ATOM   2918 C  CE2 . TRP B 1 99  ? -39.199 -32.417 36.691  1.00  9.39  ? 97  TRP A CE2 1 
ATOM   2919 C  CE3 . TRP B 1 99  ? -37.281 -31.654 35.345  1.00  8.75  ? 97  TRP A CE3 1 
ATOM   2920 C  CZ2 . TRP B 1 99  ? -40.126 -31.798 35.873  1.00  9.34  ? 97  TRP A CZ2 1 
ATOM   2921 C  CZ3 . TRP B 1 99  ? -38.237 -31.056 34.507  1.00  8.12  ? 97  TRP A CZ3 1 
ATOM   2922 C  CH2 . TRP B 1 99  ? -39.617 -31.114 34.733  1.00  8.26  ? 97  TRP A CH2 1 
ATOM   2923 N  N   . GLY B 1 100 ? -35.465 -35.890 39.117  1.00  9.38  ? 98  GLY A N   1 
ATOM   2924 C  CA  . GLY B 1 100 ? -36.093 -36.967 39.987  1.00  9.95  ? 98  GLY A CA  1 
ATOM   2925 C  C   . GLY B 1 100 ? -36.878 -36.328 41.159  1.00  10.38 ? 98  GLY A C   1 
ATOM   2926 O  O   . GLY B 1 100 ? -36.935 -35.076 41.290  1.00  11.21 ? 98  GLY A O   1 
ATOM   2927 N  N   . SER B 1 101 ? -37.482 -37.203 42.018  1.00  11.75 ? 99  SER A N   1 
ATOM   2928 C  CA  . SER B 1 101 ? -38.367 -36.641 43.097  1.00  12.16 ? 99  SER A CA  1 
ATOM   2929 C  C   . SER B 1 101 ? -37.505 -36.106 44.226  1.00  14.35 ? 99  SER A C   1 
ATOM   2930 O  O   . SER B 1 101 ? -38.040 -35.460 45.095  1.00  15.43 ? 99  SER A O   1 
ATOM   2931 C  CB  . SER B 1 101 ? -39.356 -37.659 43.670  1.00  13.85 ? 99  SER A CB  1 
ATOM   2932 O  OG  . SER B 1 101 ? -38.586 -38.725 44.123  1.00  17.61 ? 99  SER A OG  1 
ATOM   2933 N  N   . ALA B 1 102 ? -36.216 -36.376 44.237  1.00  13.62 ? 100 ALA A N   1 
ATOM   2934 C  CA  . ALA B 1 102 ? -35.331 -35.747 45.247  1.00  14.58 ? 100 ALA A CA  1 
ATOM   2935 C  C   . ALA B 1 102 ? -33.983 -35.380 44.626  1.00  14.68 ? 100 ALA A C   1 
ATOM   2936 O  O   . ALA B 1 102 ? -33.568 -35.974 43.581  1.00  14.06 ? 100 ALA A O   1 
ATOM   2937 C  CB  . ALA B 1 102 ? -35.118 -36.736 46.392  1.00  15.27 ? 100 ALA A CB  1 
ATOM   2938 N  N   . ASP B 1 103 ? -33.266 -34.438 45.239  1.00  13.31 ? 101 ASP A N   1 
ATOM   2939 C  CA  . ASP B 1 103 ? -31.961 -33.969 44.661  1.00  13.42 ? 101 ASP A CA  1 
ATOM   2940 C  C   . ASP B 1 103 ? -30.843 -34.954 44.416  1.00  15.52 ? 101 ASP A C   1 
ATOM   2941 O  O   . ASP B 1 103 ? -29.875 -34.635 43.653  1.00  16.86 ? 101 ASP A O   1 
ATOM   2942 C  CB  . ASP B 1 103 ? -31.376 -32.841 45.525  1.00  14.84 ? 101 ASP A CB  1 
ATOM   2943 C  CG  . ASP B 1 103 ? -32.258 -31.617 45.596  1.00  14.89 ? 101 ASP A CG  1 
ATOM   2944 O  OD1 . ASP B 1 103 ? -33.195 -31.469 44.779  1.00  17.08 ? 101 ASP A OD1 1 
ATOM   2945 O  OD2 . ASP B 1 103 ? -31.992 -30.782 46.484  1.00  16.36 ? 101 ASP A OD2 1 
ATOM   2946 N  N   . ASP B 1 104 ? -30.870 -36.128 45.079  1.00  15.74 ? 102 ASP A N   1 
ATOM   2947 C  CA  . ASP B 1 104 ? -29.690 -37.030 45.037  1.00  18.46 ? 102 ASP A CA  1 
ATOM   2948 C  C   . ASP B 1 104 ? -29.610 -37.835 43.755  1.00  18.54 ? 102 ASP A C   1 
ATOM   2949 O  O   . ASP B 1 104 ? -28.560 -38.401 43.467  1.00  18.63 ? 102 ASP A O   1 
ATOM   2950 C  CB  . ASP B 1 104 ? -29.724 -38.049 46.211  1.00  19.81 ? 102 ASP A CB  1 
ATOM   2951 C  CG  . ASP B 1 104 ? -30.974 -38.869 46.219  1.00  21.25 ? 102 ASP A CG  1 
ATOM   2952 O  OD1 . ASP B 1 104 ? -31.997 -38.328 46.704  1.00  22.38 ? 102 ASP A OD1 1 
ATOM   2953 O  OD2 . ASP B 1 104 ? -30.941 -40.055 45.783  1.00  24.91 ? 102 ASP A OD2 1 
ATOM   2954 N  N   . HIS B 1 105 ? -30.691 -37.879 42.979  1.00  16.73 ? 103 HIS A N   1 
ATOM   2955 C  CA  . HIS B 1 105 ? -30.608 -38.565 41.681  1.00  19.78 ? 103 HIS A CA  1 
ATOM   2956 C  C   . HIS B 1 105 ? -31.665 -38.023 40.739  1.00  17.85 ? 103 HIS A C   1 
ATOM   2957 O  O   . HIS B 1 105 ? -32.535 -37.270 41.158  1.00  20.54 ? 103 HIS A O   1 
ATOM   2958 C  CB  . HIS B 1 105 ? -30.598 -40.110 41.790  1.00  21.37 ? 103 HIS A CB  1 
ATOM   2959 C  CG  . HIS B 1 105 ? -31.876 -40.701 42.339  1.00  30.24 ? 103 HIS A CG  1 
ATOM   2960 N  ND1 . HIS B 1 105 ? -32.140 -40.785 43.671  1.00  34.97 ? 103 HIS A ND1 1 
ATOM   2961 C  CD2 . HIS B 1 105 ? -32.984 -41.252 41.685  1.00  35.79 ? 103 HIS A CD2 1 
ATOM   2962 C  CE1 . HIS B 1 105 ? -33.352 -41.353 43.869  1.00  37.53 ? 103 HIS A CE1 1 
ATOM   2963 N  NE2 . HIS B 1 105 ? -33.872 -41.647 42.650  1.00  40.94 ? 103 HIS A NE2 1 
ATOM   2964 N  N   . GLY B 1 106 ? -31.542 -38.265 39.441  1.00  16.39 ? 104 GLY A N   1 
ATOM   2965 C  CA  . GLY B 1 106 ? -32.560 -37.597 38.587  1.00  13.72 ? 104 GLY A CA  1 
ATOM   2966 C  C   . GLY B 1 106 ? -31.964 -37.413 37.198  1.00  12.10 ? 104 GLY A C   1 
ATOM   2967 O  O   . GLY B 1 106 ? -32.696 -37.353 36.245  1.00  13.21 ? 104 GLY A O   1 
ATOM   2968 N  N   . SER B 1 107 ? -30.640 -37.513 37.070  1.00  11.20 ? 105 SER A N   1 
ATOM   2969 C  CA  . SER B 1 107 ? -30.070 -37.617 35.712  1.00  10.44 ? 105 SER A CA  1 
ATOM   2970 C  C   . SER B 1 107 ? -30.503 -38.918 34.983  1.00  10.68 ? 105 SER A C   1 
ATOM   2971 O  O   . SER B 1 107 ? -30.800 -39.965 35.658  1.00  11.29 ? 105 SER A O   1 
ATOM   2972 C  CB  . SER B 1 107 ? -28.577 -37.461 35.641  1.00  10.32 ? 105 SER A CB  1 
ATOM   2973 O  OG  . SER B 1 107 ? -27.861 -38.499 36.376  1.00  11.39 ? 105 SER A OG  1 
ATOM   2974 N  N   . GLU B 1 108 ? -30.434 -38.875 33.654  1.00  10.76 ? 106 GLU A N   1 
ATOM   2975 C  CA  . GLU B 1 108 ? -30.709 -40.130 32.862  1.00  9.95  ? 106 GLU A CA  1 
ATOM   2976 C  C   . GLU B 1 108 ? -29.448 -40.946 32.673  1.00  10.21 ? 106 GLU A C   1 
ATOM   2977 O  O   . GLU B 1 108 ? -29.401 -42.148 33.075  1.00  12.07 ? 106 GLU A O   1 
ATOM   2978 C  CB  . GLU B 1 108 ? -31.392 -39.691 31.541  1.00  9.54  ? 106 GLU A CB  1 
ATOM   2979 C  CG  . GLU B 1 108 ? -32.745 -39.106 31.846  1.00  9.62  ? 106 GLU A CG  1 
ATOM   2980 C  CD  . GLU B 1 108 ? -33.800 -39.326 30.736  1.00  10.89 ? 106 GLU A CD  1 
ATOM   2981 O  OE1 . GLU B 1 108 ? -33.412 -39.136 29.541  1.00  10.53 ? 106 GLU A OE1 1 
ATOM   2982 O  OE2 . GLU B 1 108 ? -34.922 -39.708 31.060  1.00  9.76  ? 106 GLU A OE2 1 
ATOM   2983 N  N   . HIS B 1 109 ? -28.386 -40.366 32.111  1.00  9.72  ? 107 HIS A N   1 
ATOM   2984 C  CA  . HIS B 1 109 ? -27.039 -41.019 32.043  1.00  10.00 ? 107 HIS A CA  1 
ATOM   2985 C  C   . HIS B 1 109 ? -26.397 -41.052 33.416  1.00  12.77 ? 107 HIS A C   1 
ATOM   2986 O  O   . HIS B 1 109 ? -26.694 -40.196 34.259  1.00  11.05 ? 107 HIS A O   1 
ATOM   2987 C  CB  . HIS B 1 109 ? -26.111 -40.286 31.034  1.00  9.49  ? 107 HIS A CB  1 
ATOM   2988 C  CG  . HIS B 1 109 ? -26.630 -40.453 29.606  1.00  9.52  ? 107 HIS A CG  1 
ATOM   2989 N  ND1 . HIS B 1 109 ? -27.521 -39.612 29.047  1.00  9.21  ? 107 HIS A ND1 1 
ATOM   2990 C  CD2 . HIS B 1 109 ? -26.360 -41.417 28.658  1.00  8.69  ? 107 HIS A CD2 1 
ATOM   2991 C  CE1 . HIS B 1 109 ? -27.860 -40.028 27.788  1.00  9.21  ? 107 HIS A CE1 1 
ATOM   2992 N  NE2 . HIS B 1 109 ? -27.178 -41.140 27.546  1.00  9.70  ? 107 HIS A NE2 1 
ATOM   2993 N  N   . ILE B 1 110 ? -25.615 -42.081 33.671  1.00  12.48 ? 108 ILE A N   1 
ATOM   2994 C  CA  . ILE B 1 110 ? -24.930 -42.228 35.031  1.00  14.22 ? 108 ILE A CA  1 
ATOM   2995 C  C   . ILE B 1 110 ? -23.462 -42.573 34.709  1.00  17.21 ? 108 ILE A C   1 
ATOM   2996 O  O   . ILE B 1 110 ? -23.242 -43.499 33.918  1.00  17.46 ? 108 ILE A O   1 
ATOM   2997 C  CB  . ILE B 1 110 ? -25.632 -43.329 35.890  1.00  17.17 ? 108 ILE A CB  1 
ATOM   2998 C  CG1 . ILE B 1 110 ? -27.075 -42.877 36.231  1.00  18.19 ? 108 ILE A CG1 1 
ATOM   2999 C  CG2 . ILE B 1 110 ? -24.774 -43.604 37.143  1.00  16.62 ? 108 ILE A CG2 1 
ATOM   3000 C  CD1 . ILE B 1 110 ? -27.961 -43.903 36.957  1.00  23.35 ? 108 ILE A CD1 1 
ATOM   3001 N  N   A VAL B 1 111 ? -22.512 -41.808 35.300  0.50  14.72 ? 109 VAL A N   1 
ATOM   3002 N  N   B VAL B 1 111 ? -22.476 -41.851 35.262  0.50  15.67 ? 109 VAL A N   1 
ATOM   3003 C  CA  A VAL B 1 111 ? -21.069 -41.916 34.991  0.50  15.94 ? 109 VAL A CA  1 
ATOM   3004 C  CA  B VAL B 1 111 ? -21.082 -42.047 34.813  0.50  17.50 ? 109 VAL A CA  1 
ATOM   3005 C  C   A VAL B 1 111 ? -20.360 -42.613 36.136  0.50  16.96 ? 109 VAL A C   1 
ATOM   3006 C  C   B VAL B 1 111 ? -20.253 -42.542 35.996  0.50  17.89 ? 109 VAL A C   1 
ATOM   3007 O  O   A VAL B 1 111 ? -20.463 -42.151 37.247  0.50  17.04 ? 109 VAL A O   1 
ATOM   3008 O  O   B VAL B 1 111 ? -20.151 -41.858 36.995  0.50  17.82 ? 109 VAL A O   1 
ATOM   3009 C  CB  A VAL B 1 111 ? -20.430 -40.539 34.802  0.50  15.42 ? 109 VAL A CB  1 
ATOM   3010 C  CB  B VAL B 1 111 ? -20.516 -40.727 34.367  0.50  18.67 ? 109 VAL A CB  1 
ATOM   3011 C  CG1 A VAL B 1 111 ? -19.000 -40.722 34.208  0.50  13.89 ? 109 VAL A CG1 1 
ATOM   3012 C  CG1 B VAL B 1 111 ? -21.199 -40.224 33.085  0.50  17.47 ? 109 VAL A CG1 1 
ATOM   3013 C  CG2 A VAL B 1 111 ? -21.363 -39.686 33.907  0.50  14.30 ? 109 VAL A CG2 1 
ATOM   3014 C  CG2 B VAL B 1 111 ? -20.722 -39.777 35.521  0.50  17.28 ? 109 VAL A CG2 1 
ATOM   3015 N  N   . ASP B 1 112 ? -19.724 -43.754 35.882  1.00  18.92 ? 110 ASP A N   1 
ATOM   3016 C  CA  . ASP B 1 112 ? -18.955 -44.437 36.995  1.00  20.60 ? 110 ASP A CA  1 
ATOM   3017 C  C   . ASP B 1 112 ? -19.830 -44.439 38.295  1.00  20.94 ? 110 ASP A C   1 
ATOM   3018 O  O   . ASP B 1 112 ? -19.328 -44.209 39.410  1.00  22.97 ? 110 ASP A O   1 
ATOM   3019 C  CB  . ASP B 1 112 ? -17.589 -43.809 37.231  1.00  19.70 ? 110 ASP A CB  1 
ATOM   3020 C  CG  . ASP B 1 112 ? -16.663 -44.052 36.067  1.00  23.62 ? 110 ASP A CG  1 
ATOM   3021 O  OD1 . ASP B 1 112 ? -16.869 -45.131 35.420  1.00  26.57 ? 110 ASP A OD1 1 
ATOM   3022 O  OD2 . ASP B 1 112 ? -15.733 -43.208 35.837  1.00  23.43 ? 110 ASP A OD2 1 
ATOM   3023 N  N   . GLY B 1 113 ? -21.130 -44.738 38.103  1.00  20.31 ? 111 GLY A N   1 
ATOM   3024 C  CA  . GLY B 1 113 ? -22.076 -44.826 39.237  1.00  21.29 ? 111 GLY A CA  1 
ATOM   3025 C  C   . GLY B 1 113 ? -22.538 -43.496 39.784  1.00  21.33 ? 111 GLY A C   1 
ATOM   3026 O  O   . GLY B 1 113 ? -23.359 -43.469 40.686  1.00  24.54 ? 111 GLY A O   1 
ATOM   3027 N  N   . VAL B 1 114 ? -22.065 -42.383 39.252  1.00  20.70 ? 112 VAL A N   1 
ATOM   3028 C  CA  . VAL B 1 114 ? -22.520 -41.065 39.742  1.00  22.47 ? 112 VAL A CA  1 
ATOM   3029 C  C   . VAL B 1 114 ? -23.792 -40.520 39.043  1.00  24.19 ? 112 VAL A C   1 
ATOM   3030 O  O   . VAL B 1 114 ? -23.827 -40.349 37.821  1.00  22.16 ? 112 VAL A O   1 
ATOM   3031 C  CB  . VAL B 1 114 ? -21.407 -40.005 39.747  1.00  24.42 ? 112 VAL A CB  1 
ATOM   3032 C  CG1 . VAL B 1 114 ? -21.865 -38.762 40.541  1.00  27.86 ? 112 VAL A CG1 1 
ATOM   3033 C  CG2 . VAL B 1 114 ? -20.112 -40.573 40.403  1.00  24.18 ? 112 VAL A CG2 1 
ATOM   3034 N  N   . SER B 1 115 ? -24.828 -40.268 39.828  1.00  22.62 ? 113 SER A N   1 
ATOM   3035 C  CA  . SER B 1 115 ? -26.028 -39.567 39.327  1.00  23.78 ? 113 SER A CA  1 
ATOM   3036 C  C   . SER B 1 115 ? -25.982 -38.105 39.812  1.00  25.63 ? 113 SER A C   1 
ATOM   3037 O  O   . SER B 1 115 ? -25.531 -37.759 40.907  1.00  27.73 ? 113 SER A O   1 
ATOM   3038 C  CB  . SER B 1 115 ? -27.335 -40.151 39.887  1.00  25.45 ? 113 SER A CB  1 
ATOM   3039 O  OG  . SER B 1 115 ? -27.553 -41.505 39.500  1.00  29.54 ? 113 SER A OG  1 
ATOM   3040 N  N   . TYR B 1 116 ? -26.500 -37.300 38.939  1.00  20.00 ? 114 TYR A N   1 
ATOM   3041 C  CA  . TYR B 1 116 ? -26.646 -35.877 39.142  1.00  15.22 ? 114 TYR A CA  1 
ATOM   3042 C  C   . TYR B 1 116 ? -28.071 -35.636 39.443  1.00  13.36 ? 114 TYR A C   1 
ATOM   3043 O  O   . TYR B 1 116 ? -28.875 -36.568 39.339  1.00  13.82 ? 114 TYR A O   1 
ATOM   3044 C  CB  . TYR B 1 116 ? -26.183 -35.296 37.822  1.00  13.32 ? 114 TYR A CB  1 
ATOM   3045 C  CG  . TYR B 1 116 ? -24.684 -35.387 37.688  1.00  13.24 ? 114 TYR A CG  1 
ATOM   3046 C  CD1 . TYR B 1 116 ? -23.851 -34.510 38.401  1.00  14.23 ? 114 TYR A CD1 1 
ATOM   3047 C  CD2 . TYR B 1 116 ? -24.094 -36.327 36.836  1.00  15.20 ? 114 TYR A CD2 1 
ATOM   3048 C  CE1 . TYR B 1 116 ? -22.475 -34.546 38.239  1.00  15.66 ? 114 TYR A CE1 1 
ATOM   3049 C  CE2 . TYR B 1 116 ? -22.743 -36.398 36.684  1.00  16.66 ? 114 TYR A CE2 1 
ATOM   3050 C  CZ  . TYR B 1 116 ? -21.952 -35.480 37.376  1.00  17.25 ? 114 TYR A CZ  1 
ATOM   3051 O  OH  . TYR B 1 116 ? -20.606 -35.545 37.233  1.00  27.39 ? 114 TYR A OH  1 
ATOM   3052 N  N   . ALA B 1 117 ? -28.428 -34.419 39.871  1.00  10.55 ? 115 ALA A N   1 
ATOM   3053 C  CA  . ALA B 1 117 ? -29.779 -34.080 40.212  1.00  11.65 ? 115 ALA A CA  1 
ATOM   3054 C  C   . ALA B 1 117 ? -30.721 -34.000 39.008  1.00  9.70  ? 115 ALA A C   1 
ATOM   3055 O  O   . ALA B 1 117 ? -31.919 -34.109 39.148  1.00  10.39 ? 115 ALA A O   1 
ATOM   3056 C  CB  . ALA B 1 117 ? -29.787 -32.695 40.919  1.00  11.48 ? 115 ALA A CB  1 
ATOM   3057 N  N   . ALA B 1 118 ? -30.163 -33.634 37.854  1.00  9.09  ? 116 ALA A N   1 
ATOM   3058 C  CA  . ALA B 1 118 ? -31.031 -33.373 36.664  1.00  8.17  ? 116 ALA A CA  1 
ATOM   3059 C  C   . ALA B 1 118 ? -30.144 -33.476 35.410  1.00  7.85  ? 116 ALA A C   1 
ATOM   3060 O  O   . ALA B 1 118 ? -28.914 -33.546 35.468  1.00  7.37  ? 116 ALA A O   1 
ATOM   3061 C  CB  . ALA B 1 118 ? -31.715 -32.026 36.722  1.00  9.29  ? 116 ALA A CB  1 
ATOM   3062 N  N   . GLU B 1 119 ? -30.800 -33.571 34.246  1.00  7.42  ? 117 GLU A N   1 
ATOM   3063 C  CA  . GLU B 1 119 ? -30.003 -33.643 32.975  1.00  6.88  ? 117 GLU A CA  1 
ATOM   3064 C  C   . GLU B 1 119 ? -30.817 -32.860 31.874  1.00  6.92  ? 117 GLU A C   1 
ATOM   3065 O  O   . GLU B 1 119 ? -32.008 -33.124 31.614  1.00  7.04  ? 117 GLU A O   1 
ATOM   3066 C  CB  . GLU B 1 119 ? -29.826 -35.117 32.602  1.00  7.83  ? 117 GLU A CB  1 
ATOM   3067 C  CG  . GLU B 1 119 ? -28.990 -35.319 31.317  1.00  7.53  ? 117 GLU A CG  1 
ATOM   3068 C  CD  . GLU B 1 119 ? -28.762 -36.778 31.021  1.00  9.52  ? 117 GLU A CD  1 
ATOM   3069 O  OE1 . GLU B 1 119 ? -28.528 -37.575 31.993  1.00  9.84  ? 117 GLU A OE1 1 
ATOM   3070 O  OE2 . GLU B 1 119 ? -28.655 -37.158 29.812  1.00  9.16  ? 117 GLU A OE2 1 
ATOM   3071 N  N   . LEU B 1 120 ? -30.144 -31.938 31.205  1.00  6.99  ? 118 LEU A N   1 
ATOM   3072 C  CA  . LEU B 1 120 ? -30.743 -31.130 30.147  1.00  7.31  ? 118 LEU A CA  1 
ATOM   3073 C  C   . LEU B 1 120 ? -30.423 -31.808 28.811  1.00  7.43  ? 118 LEU A C   1 
ATOM   3074 O  O   . LEU B 1 120 ? -29.287 -32.269 28.595  1.00  7.20  ? 118 LEU A O   1 
ATOM   3075 C  CB  . LEU B 1 120 ? -30.065 -29.703 30.207  1.00  7.81  ? 118 LEU A CB  1 
ATOM   3076 C  CG  . LEU B 1 120 ? -30.698 -28.693 29.175  1.00  9.34  ? 118 LEU A CG  1 
ATOM   3077 C  CD1 . LEU B 1 120 ? -31.908 -28.040 29.843  1.00  9.64  ? 118 LEU A CD1 1 
ATOM   3078 C  CD2 . LEU B 1 120 ? -29.681 -27.528 28.761  1.00  11.13 ? 118 LEU A CD2 1 
ATOM   3079 N  N   . HIS B 1 121 ? -31.414 -31.838 27.901  1.00  6.94  ? 119 HIS A N   1 
ATOM   3080 C  CA  . HIS B 1 121 ? -31.206 -32.418 26.552  1.00  7.60  ? 119 HIS A CA  1 
ATOM   3081 C  C   . HIS B 1 121 ? -31.444 -31.341 25.500  1.00  7.26  ? 119 HIS A C   1 
ATOM   3082 O  O   . HIS B 1 121 ? -32.442 -30.588 25.557  1.00  8.38  ? 119 HIS A O   1 
ATOM   3083 C  CB  . HIS B 1 121 ? -32.165 -33.589 26.331  1.00  8.13  ? 119 HIS A CB  1 
ATOM   3084 C  CG  . HIS B 1 121 ? -31.766 -34.819 27.124  1.00  7.67  ? 119 HIS A CG  1 
ATOM   3085 N  ND1 . HIS B 1 121 ? -32.662 -35.860 27.415  1.00  7.85  ? 119 HIS A ND1 1 
ATOM   3086 C  CD2 . HIS B 1 121 ? -30.570 -35.114 27.742  1.00  8.19  ? 119 HIS A CD2 1 
ATOM   3087 C  CE1 . HIS B 1 121 ? -31.978 -36.784 28.182  1.00  7.58  ? 119 HIS A CE1 1 
ATOM   3088 N  NE2 . HIS B 1 121 ? -30.700 -36.346 28.344  1.00  8.25  ? 119 HIS A NE2 1 
ATOM   3089 N  N   . VAL B 1 122 ? -30.479 -31.186 24.569  1.00  7.51  ? 120 VAL A N   1 
ATOM   3090 C  CA  . VAL B 1 122 ? -30.636 -30.190 23.495  1.00  7.23  ? 120 VAL A CA  1 
ATOM   3091 C  C   . VAL B 1 122 ? -30.737 -31.029 22.195  1.00  6.69  ? 120 VAL A C   1 
ATOM   3092 O  O   . VAL B 1 122 ? -29.729 -31.689 21.782  1.00  6.94  ? 120 VAL A O   1 
ATOM   3093 C  CB  . VAL B 1 122 ? -29.390 -29.270 23.509  1.00  7.02  ? 120 VAL A CB  1 
ATOM   3094 C  CG1 . VAL B 1 122 ? -29.595 -28.143 22.486  1.00  6.56  ? 120 VAL A CG1 1 
ATOM   3095 C  CG2 . VAL B 1 122 ? -29.073 -28.707 24.956  1.00  7.93  ? 120 VAL A CG2 1 
ATOM   3096 N  N   . VAL B 1 123 ? -31.922 -31.000 21.562  1.00  7.18  ? 121 VAL A N   1 
ATOM   3097 C  CA  . VAL B 1 123 ? -32.235 -31.974 20.489  1.00  6.30  ? 121 VAL A CA  1 
ATOM   3098 C  C   . VAL B 1 123 ? -32.097 -31.287 19.115  1.00  6.76  ? 121 VAL A C   1 
ATOM   3099 O  O   . VAL B 1 123 ? -32.595 -30.136 18.939  1.00  6.95  ? 121 VAL A O   1 
ATOM   3100 C  CB  . VAL B 1 123 ? -33.720 -32.383 20.655  1.00  6.37  ? 121 VAL A CB  1 
ATOM   3101 C  CG1 . VAL B 1 123 ? -34.042 -33.408 19.583  1.00  7.02  ? 121 VAL A CG1 1 
ATOM   3102 C  CG2 . VAL B 1 123 ? -33.888 -33.035 22.030  1.00  6.95  ? 121 VAL A CG2 1 
ATOM   3103 N  N   . HIS B 1 124 ? -31.354 -31.937 18.181  1.00  6.90  ? 122 HIS A N   1 
ATOM   3104 C  CA  . HIS B 1 124 ? -31.040 -31.356 16.830  1.00  7.37  ? 122 HIS A CA  1 
ATOM   3105 C  C   . HIS B 1 124 ? -31.337 -32.482 15.822  1.00  8.00  ? 122 HIS A C   1 
ATOM   3106 O  O   . HIS B 1 124 ? -31.368 -33.714 16.162  1.00  8.25  ? 122 HIS A O   1 
ATOM   3107 C  CB  . HIS B 1 124 ? -29.528 -31.023 16.657  1.00  7.53  ? 122 HIS A CB  1 
ATOM   3108 C  CG  . HIS B 1 124 ? -28.957 -30.187 17.797  1.00  8.20  ? 122 HIS A CG  1 
ATOM   3109 N  ND1 . HIS B 1 124 ? -28.741 -30.699 19.036  1.00  9.08  ? 122 HIS A ND1 1 
ATOM   3110 C  CD2 . HIS B 1 124 ? -28.495 -28.867 17.814  1.00  8.50  ? 122 HIS A CD2 1 
ATOM   3111 C  CE1 . HIS B 1 124 ? -28.145 -29.785 19.812  1.00  9.37  ? 122 HIS A CE1 1 
ATOM   3112 N  NE2 . HIS B 1 124 ? -27.996 -28.651 19.087  1.00  9.08  ? 122 HIS A NE2 1 
ATOM   3113 N  N   . TRP B 1 125 ? -31.653 -32.074 14.607  1.00  7.87  ? 123 TRP A N   1 
ATOM   3114 C  CA  . TRP B 1 125 ? -31.919 -33.092 13.581  1.00  7.57  ? 123 TRP A CA  1 
ATOM   3115 C  C   . TRP B 1 125 ? -31.210 -32.739 12.220  1.00  8.36  ? 123 TRP A C   1 
ATOM   3116 O  O   . TRP B 1 125 ? -30.915 -31.555 11.902  1.00  9.55  ? 123 TRP A O   1 
ATOM   3117 C  CB  . TRP B 1 125 ? -33.454 -33.201 13.310  1.00  8.69  ? 123 TRP A CB  1 
ATOM   3118 C  CG  . TRP B 1 125 ? -34.121 -31.894 12.894  1.00  9.04  ? 123 TRP A CG  1 
ATOM   3119 C  CD1 . TRP B 1 125 ? -34.513 -30.791 13.716  1.00  9.17  ? 123 TRP A CD1 1 
ATOM   3120 C  CD2 . TRP B 1 125 ? -34.504 -31.510 11.528  1.00  9.77  ? 123 TRP A CD2 1 
ATOM   3121 N  NE1 . TRP B 1 125 ? -35.134 -29.803 12.955  1.00  9.89  ? 123 TRP A NE1 1 
ATOM   3122 C  CE2 . TRP B 1 125 ? -35.138 -30.199 11.614  1.00  9.83  ? 123 TRP A CE2 1 
ATOM   3123 C  CE3 . TRP B 1 125 ? -34.421 -32.169 10.288  1.00  10.55 ? 123 TRP A CE3 1 
ATOM   3124 C  CZ2 . TRP B 1 125 ? -35.638 -29.525 10.479  1.00  9.82  ? 123 TRP A CZ2 1 
ATOM   3125 C  CZ3 . TRP B 1 125 ? -34.926 -31.515 9.152   1.00  10.95 ? 123 TRP A CZ3 1 
ATOM   3126 C  CH2 . TRP B 1 125 ? -35.521 -30.221 9.228   1.00  9.58  ? 123 TRP A CH2 1 
ATOM   3127 N  N   . ASN B 1 126 ? -30.936 -33.814 11.470  1.00  8.96  ? 124 ASN A N   1 
ATOM   3128 C  CA  . ASN B 1 126 ? -30.131 -33.748 10.236  1.00  8.89  ? 124 ASN A CA  1 
ATOM   3129 C  C   . ASN B 1 126 ? -30.952 -33.201 9.072   1.00  9.59  ? 124 ASN A C   1 
ATOM   3130 O  O   . ASN B 1 126 ? -31.680 -33.936 8.411   1.00  9.26  ? 124 ASN A O   1 
ATOM   3131 C  CB  . ASN B 1 126 ? -29.715 -35.196 9.894   1.00  9.61  ? 124 ASN A CB  1 
ATOM   3132 C  CG  . ASN B 1 126 ? -28.731 -35.245 8.778   1.00  12.45 ? 124 ASN A CG  1 
ATOM   3133 O  OD1 . ASN B 1 126 ? -28.649 -34.299 7.972   1.00  12.02 ? 124 ASN A OD1 1 
ATOM   3134 N  ND2 . ASN B 1 126 ? -27.891 -36.308 8.776   1.00  12.72 ? 124 ASN A ND2 1 
ATOM   3135 N  N   . SER B 1 127 ? -30.911 -31.906 8.909   1.00  9.16  ? 125 SER A N   1 
ATOM   3136 C  CA  . SER B 1 127 ? -31.666 -31.202 7.849   1.00  10.93 ? 125 SER A CA  1 
ATOM   3137 C  C   . SER B 1 127 ? -30.849 -31.210 6.535   1.00  11.09 ? 125 SER A C   1 
ATOM   3138 O  O   . SER B 1 127 ? -31.377 -30.754 5.493   1.00  11.88 ? 125 SER A O   1 
ATOM   3139 C  CB  . SER B 1 127 ? -31.892 -29.712 8.287   1.00  10.89 ? 125 SER A CB  1 
ATOM   3140 O  OG  . SER B 1 127 ? -30.663 -28.991 8.600   1.00  11.29 ? 125 SER A OG  1 
ATOM   3141 N  N   . ASP B 1 128 ? -29.602 -31.677 6.578   1.00  9.86  ? 126 ASP A N   1 
ATOM   3142 C  CA  . ASP B 1 128 ? -28.845 -31.973 5.336   1.00  11.87 ? 126 ASP A CA  1 
ATOM   3143 C  C   . ASP B 1 128 ? -29.396 -33.145 4.556   1.00  11.68 ? 126 ASP A C   1 
ATOM   3144 O  O   . ASP B 1 128 ? -29.284 -33.198 3.280   1.00  12.77 ? 126 ASP A O   1 
ATOM   3145 C  CB  . ASP B 1 128 ? -27.365 -32.179 5.691   1.00  12.43 ? 126 ASP A CB  1 
ATOM   3146 C  CG  . ASP B 1 128 ? -26.605 -30.879 5.844   1.00  13.27 ? 126 ASP A CG  1 
ATOM   3147 O  OD1 . ASP B 1 128 ? -25.396 -30.999 6.183   1.00  15.31 ? 126 ASP A OD1 1 
ATOM   3148 O  OD2 . ASP B 1 128 ? -27.179 -29.740 5.702   1.00  14.43 ? 126 ASP A OD2 1 
ATOM   3149 N  N   . LYS B 1 129 ? -30.010 -34.100 5.264   1.00  11.68 ? 127 LYS A N   1 
ATOM   3150 C  CA  . LYS B 1 129 ? -30.570 -35.294 4.601   1.00  11.44 ? 127 LYS A CA  1 
ATOM   3151 C  C   . LYS B 1 129 ? -32.071 -35.460 4.657   1.00  11.66 ? 127 LYS A C   1 
ATOM   3152 O  O   . LYS B 1 129 ? -32.667 -36.108 3.767   1.00  12.78 ? 127 LYS A O   1 
ATOM   3153 C  CB  . LYS B 1 129 ? -29.948 -36.586 5.181   1.00  13.89 ? 127 LYS A CB  1 
ATOM   3154 C  CG  . LYS B 1 129 ? -28.507 -36.694 4.904   1.00  15.00 ? 127 LYS A CG  1 
ATOM   3155 C  CD  . LYS B 1 129 ? -27.890 -38.018 5.364   1.00  16.10 ? 127 LYS A CD  1 
ATOM   3156 C  CE  . LYS B 1 129 ? -28.646 -39.215 4.833   1.00  17.54 ? 127 LYS A CE  1 
ATOM   3157 N  NZ  . LYS B 1 129 ? -27.970 -40.540 5.123   1.00  15.83 ? 127 LYS A NZ  1 
ATOM   3158 N  N   . TYR B 1 130 ? -32.712 -34.992 5.721   1.00  11.89 ? 128 TYR A N   1 
ATOM   3159 C  CA  . TYR B 1 130 ? -34.130 -35.226 5.945   1.00  11.68 ? 128 TYR A CA  1 
ATOM   3160 C  C   . TYR B 1 130 ? -35.017 -33.954 5.904   1.00  11.54 ? 128 TYR A C   1 
ATOM   3161 O  O   . TYR B 1 130 ? -34.556 -32.881 6.229   1.00  11.60 ? 128 TYR A O   1 
ATOM   3162 C  CB  . TYR B 1 130 ? -34.264 -35.991 7.316   1.00  12.14 ? 128 TYR A CB  1 
ATOM   3163 C  CG  . TYR B 1 130 ? -33.385 -37.243 7.286   1.00  14.28 ? 128 TYR A CG  1 
ATOM   3164 C  CD1 . TYR B 1 130 ? -33.626 -38.257 6.281   1.00  14.68 ? 128 TYR A CD1 1 
ATOM   3165 C  CD2 . TYR B 1 130 ? -32.283 -37.440 8.167   1.00  14.36 ? 128 TYR A CD2 1 
ATOM   3166 C  CE1 . TYR B 1 130 ? -32.808 -39.375 6.203   1.00  16.92 ? 128 TYR A CE1 1 
ATOM   3167 C  CE2 . TYR B 1 130 ? -31.492 -38.578 8.116   1.00  14.21 ? 128 TYR A CE2 1 
ATOM   3168 C  CZ  . TYR B 1 130 ? -31.783 -39.558 7.146   1.00  17.50 ? 128 TYR A CZ  1 
ATOM   3169 O  OH  . TYR B 1 130 ? -31.017 -40.661 7.030   1.00  17.96 ? 128 TYR A OH  1 
ATOM   3170 N  N   . PRO B 1 131 ? -36.299 -34.109 5.583   1.00  12.96 ? 129 PRO A N   1 
ATOM   3171 C  CA  . PRO B 1 131 ? -37.154 -32.911 5.304   1.00  14.49 ? 129 PRO A CA  1 
ATOM   3172 C  C   . PRO B 1 131 ? -37.757 -32.316 6.536   1.00  14.77 ? 129 PRO A C   1 
ATOM   3173 O  O   . PRO B 1 131 ? -38.298 -31.199 6.498   1.00  14.93 ? 129 PRO A O   1 
ATOM   3174 C  CB  . PRO B 1 131 ? -38.261 -33.485 4.393   1.00  16.03 ? 129 PRO A CB  1 
ATOM   3175 C  CG  . PRO B 1 131 ? -38.407 -34.877 4.918   1.00  16.43 ? 129 PRO A CG  1 
ATOM   3176 C  CD  . PRO B 1 131 ? -36.950 -35.331 5.130   1.00  13.08 ? 129 PRO A CD  1 
ATOM   3177 N  N   . SER B 1 132 ? -37.700 -33.041 7.656   1.00  13.62 ? 130 SER A N   1 
ATOM   3178 C  CA  . SER B 1 132 ? -38.387 -32.604 8.861   1.00  14.50 ? 130 SER A CA  1 
ATOM   3179 C  C   . SER B 1 132 ? -37.811 -33.384 10.050  1.00  13.93 ? 130 SER A C   1 
ATOM   3180 O  O   . SER B 1 132 ? -37.204 -34.477 9.938   1.00  12.38 ? 130 SER A O   1 
ATOM   3181 C  CB  . SER B 1 132 ? -39.908 -32.868 8.784   1.00  16.68 ? 130 SER A CB  1 
ATOM   3182 O  OG  . SER B 1 132 ? -40.185 -34.258 8.807   1.00  16.21 ? 130 SER A OG  1 
ATOM   3183 N  N   . PHE B 1 133 ? -38.000 -32.763 11.219  1.00  16.03 ? 131 PHE A N   1 
ATOM   3184 C  CA  . PHE B 1 133 ? -37.626 -33.465 12.466  1.00  15.60 ? 131 PHE A CA  1 
ATOM   3185 C  C   . PHE B 1 133 ? -38.338 -34.825 12.583  1.00  15.43 ? 131 PHE A C   1 
ATOM   3186 O  O   . PHE B 1 133 ? -37.717 -35.802 12.921  1.00  12.77 ? 131 PHE A O   1 
ATOM   3187 C  CB  . PHE B 1 133 ? -37.964 -32.566 13.669  1.00  14.98 ? 131 PHE A CB  1 
ATOM   3188 C  CG  . PHE B 1 133 ? -37.874 -33.304 14.983  1.00  17.03 ? 131 PHE A CG  1 
ATOM   3189 C  CD1 . PHE B 1 133 ? -36.611 -33.464 15.638  1.00  15.80 ? 131 PHE A CD1 1 
ATOM   3190 C  CD2 . PHE B 1 133 ? -38.995 -33.950 15.509  1.00  20.42 ? 131 PHE A CD2 1 
ATOM   3191 C  CE1 . PHE B 1 133 ? -36.533 -34.196 16.821  1.00  16.74 ? 131 PHE A CE1 1 
ATOM   3192 C  CE2 . PHE B 1 133 ? -38.910 -34.692 16.685  1.00  22.23 ? 131 PHE A CE2 1 
ATOM   3193 C  CZ  . PHE B 1 133 ? -37.649 -34.799 17.342  1.00  21.34 ? 131 PHE A CZ  1 
ATOM   3194 N  N   . VAL B 1 134 ? -39.644 -34.907 12.308  1.00  15.47 ? 132 VAL A N   1 
ATOM   3195 C  CA  . VAL B 1 134 ? -40.348 -36.126 12.358  1.00  16.00 ? 132 VAL A CA  1 
ATOM   3196 C  C   . VAL B 1 134 ? -39.788 -37.234 11.500  1.00  16.33 ? 132 VAL A C   1 
ATOM   3197 O  O   . VAL B 1 134 ? -39.615 -38.362 11.965  1.00  17.57 ? 132 VAL A O   1 
ATOM   3198 C  CB  . VAL B 1 134 ? -41.884 -35.896 12.138  1.00  21.66 ? 132 VAL A CB  1 
ATOM   3199 C  CG1 . VAL B 1 134 ? -42.595 -37.238 11.953  1.00  23.49 ? 132 VAL A CG1 1 
ATOM   3200 C  CG2 . VAL B 1 134 ? -42.445 -35.140 13.342  1.00  23.06 ? 132 VAL A CG2 1 
ATOM   3201 N  N   A GLU B 1 135 ? -39.433 -36.951 10.234  0.50  14.20 ? 133 GLU A N   1 
ATOM   3202 N  N   B GLU B 1 135 ? -39.460 -36.930 10.238  0.50  14.05 ? 133 GLU A N   1 
ATOM   3203 C  CA  A GLU B 1 135 ? -38.751 -37.962 9.414   0.50  13.50 ? 133 GLU A CA  1 
ATOM   3204 C  CA  B GLU B 1 135 ? -38.767 -37.908 9.429   0.50  13.29 ? 133 GLU A CA  1 
ATOM   3205 C  C   A GLU B 1 135 ? -37.327 -38.318 9.889   0.50  12.44 ? 133 GLU A C   1 
ATOM   3206 C  C   B GLU B 1 135 ? -37.427 -38.310 10.048  0.50  12.41 ? 133 GLU A C   1 
ATOM   3207 O  O   A GLU B 1 135 ? -36.886 -39.447 9.679   0.50  12.17 ? 133 GLU A O   1 
ATOM   3208 O  O   B GLU B 1 135 ? -37.173 -39.483 10.142  0.50  13.06 ? 133 GLU A O   1 
ATOM   3209 C  CB  A GLU B 1 135 ? -38.680 -37.549 7.929   0.50  14.80 ? 133 GLU A CB  1 
ATOM   3210 C  CB  B GLU B 1 135 ? -38.554 -37.410 7.995   0.50  14.15 ? 133 GLU A CB  1 
ATOM   3211 C  CG  A GLU B 1 135 ? -37.670 -38.375 7.146   0.50  15.42 ? 133 GLU A CG  1 
ATOM   3212 C  CG  B GLU B 1 135 ? -39.836 -37.311 7.195   0.50  13.93 ? 133 GLU A CG  1 
ATOM   3213 C  CD  A GLU B 1 135 ? -38.089 -39.830 6.962   0.50  16.18 ? 133 GLU A CD  1 
ATOM   3214 C  CD  B GLU B 1 135 ? -40.446 -38.641 6.840   0.50  16.87 ? 133 GLU A CD  1 
ATOM   3215 O  OE1 A GLU B 1 135 ? -39.247 -40.147 6.577   0.50  18.64 ? 133 GLU A OE1 1 
ATOM   3216 O  OE1 B GLU B 1 135 ? -39.794 -39.649 7.113   0.50  18.70 ? 133 GLU A OE1 1 
ATOM   3217 O  OE2 A GLU B 1 135 ? -37.252 -40.674 7.152   0.50  12.48 ? 133 GLU A OE2 1 
ATOM   3218 O  OE2 B GLU B 1 135 ? -41.590 -38.675 6.299   0.50  18.25 ? 133 GLU A OE2 1 
ATOM   3219 N  N   . ALA B 1 136 ? -36.587 -37.328 10.408  1.00  11.04 ? 134 ALA A N   1 
ATOM   3220 C  CA  . ALA B 1 136 ? -35.203 -37.542 10.883  1.00  11.33 ? 134 ALA A CA  1 
ATOM   3221 C  C   . ALA B 1 136 ? -35.212 -38.484 12.128  1.00  11.50 ? 134 ALA A C   1 
ATOM   3222 O  O   . ALA B 1 136 ? -34.320 -39.385 12.265  1.00  10.11 ? 134 ALA A O   1 
ATOM   3223 C  CB  . ALA B 1 136 ? -34.561 -36.221 11.238  1.00  12.53 ? 134 ALA A CB  1 
ATOM   3224 N  N   . ALA B 1 137 ? -36.216 -38.270 12.981  1.00  11.84 ? 135 ALA A N   1 
ATOM   3225 C  CA  . ALA B 1 137 ? -36.407 -39.194 14.128  1.00  11.02 ? 135 ALA A CA  1 
ATOM   3226 C  C   . ALA B 1 137 ? -36.554 -40.706 13.828  1.00  13.17 ? 135 ALA A C   1 
ATOM   3227 O  O   . ALA B 1 137 ? -36.362 -41.493 14.770  1.00  12.03 ? 135 ALA A O   1 
ATOM   3228 C  CB  . ALA B 1 137 ? -37.578 -38.735 14.977  1.00  11.71 ? 135 ALA A CB  1 
ATOM   3229 N  N   . HIS B 1 138 ? -36.820 -41.119 12.571  1.00  15.16 ? 136 HIS A N   1 
ATOM   3230 C  CA  . HIS B 1 138 ? -36.911 -42.516 12.140  1.00  16.57 ? 136 HIS A CA  1 
ATOM   3231 C  C   . HIS B 1 138 ? -35.678 -43.039 11.374  1.00  16.69 ? 136 HIS A C   1 
ATOM   3232 O  O   . HIS B 1 138 ? -35.705 -44.101 10.746  1.00  16.97 ? 136 HIS A O   1 
ATOM   3233 C  CB  . HIS B 1 138 ? -38.248 -42.776 11.366  1.00  16.81 ? 136 HIS A CB  1 
ATOM   3234 C  CG  . HIS B 1 138 ? -39.450 -42.507 12.198  1.00  16.70 ? 136 HIS A CG  1 
ATOM   3235 N  ND1 . HIS B 1 138 ? -40.144 -43.477 12.868  1.00  20.27 ? 136 HIS A ND1 1 
ATOM   3236 C  CD2 . HIS B 1 138 ? -40.102 -41.323 12.464  1.00  18.23 ? 136 HIS A CD2 1 
ATOM   3237 C  CE1 . HIS B 1 138 ? -41.177 -42.917 13.512  1.00  17.88 ? 136 HIS A CE1 1 
ATOM   3238 N  NE2 . HIS B 1 138 ? -41.148 -41.607 13.284  1.00  21.38 ? 136 HIS A NE2 1 
ATOM   3239 N  N   A GLU B 1 139 ? -34.559 -42.334 11.506  0.50  16.13 ? 137 GLU A N   1 
ATOM   3240 N  N   B GLU B 1 139 ? -34.578 -42.274 11.429  0.50  15.41 ? 137 GLU A N   1 
ATOM   3241 C  CA  A GLU B 1 139 ? -33.369 -42.707 10.802  0.50  15.79 ? 137 GLU A CA  1 
ATOM   3242 C  CA  B GLU B 1 139 ? -33.354 -42.520 10.682  0.50  15.05 ? 137 GLU A CA  1 
ATOM   3243 C  C   A GLU B 1 139 ? -32.129 -42.747 11.669  0.50  14.32 ? 137 GLU A C   1 
ATOM   3244 C  C   B GLU B 1 139 ? -32.131 -42.708 11.637  0.50  13.84 ? 137 GLU A C   1 
ATOM   3245 O  O   A GLU B 1 139 ? -31.980 -41.931 12.567  0.50  13.35 ? 137 GLU A O   1 
ATOM   3246 O  O   B GLU B 1 139 ? -32.000 -41.945 12.581  0.50  13.04 ? 137 GLU A O   1 
ATOM   3247 C  CB  A GLU B 1 139 ? -33.206 -41.714 9.680   0.50  18.16 ? 137 GLU A CB  1 
ATOM   3248 C  CB  B GLU B 1 139 ? -33.117 -41.280 9.774   0.50  15.35 ? 137 GLU A CB  1 
ATOM   3249 C  CG  A GLU B 1 139 ? -34.282 -41.979 8.660   0.50  18.94 ? 137 GLU A CG  1 
ATOM   3250 C  CG  B GLU B 1 139 ? -34.253 -40.935 8.774   0.50  16.24 ? 137 GLU A CG  1 
ATOM   3251 C  CD  A GLU B 1 139 ? -33.815 -42.996 7.645   0.50  22.10 ? 137 GLU A CD  1 
ATOM   3252 C  CD  B GLU B 1 139 ? -34.453 -41.965 7.668   0.50  18.46 ? 137 GLU A CD  1 
ATOM   3253 O  OE1 A GLU B 1 139 ? -34.095 -44.217 7.755   0.50  24.41 ? 137 GLU A OE1 1 
ATOM   3254 O  OE1 B GLU B 1 139 ? -33.738 -42.993 7.727   0.50  19.26 ? 137 GLU A OE1 1 
ATOM   3255 O  OE2 A GLU B 1 139 ? -33.116 -42.545 6.732   0.50  23.79 ? 137 GLU A OE2 1 
ATOM   3256 O  OE2 B GLU B 1 139 ? -35.353 -41.753 6.774   0.50  17.88 ? 137 GLU A OE2 1 
ATOM   3257 N  N   . PRO B 1 140 ? -31.234 -43.698 11.422  1.00  15.40 ? 138 PRO A N   1 
ATOM   3258 C  CA  . PRO B 1 140 ? -30.156 -43.872 12.394  1.00  14.29 ? 138 PRO A CA  1 
ATOM   3259 C  C   . PRO B 1 140 ? -29.281 -42.666 12.587  1.00  13.11 ? 138 PRO A C   1 
ATOM   3260 O  O   . PRO B 1 140 ? -28.790 -42.451 13.718  1.00  12.83 ? 138 PRO A O   1 
ATOM   3261 C  CB  . PRO B 1 140 ? -29.345 -45.078 11.818  1.00  18.12 ? 138 PRO A CB  1 
ATOM   3262 C  CG  . PRO B 1 140 ? -30.478 -45.915 11.269  1.00  20.72 ? 138 PRO A CG  1 
ATOM   3263 C  CD  . PRO B 1 140 ? -31.242 -44.861 10.478  1.00  18.20 ? 138 PRO A CD  1 
ATOM   3264 N  N   . ASP B 1 141 ? -29.058 -41.911 11.506  1.00  11.04 ? 139 ASP A N   1 
ATOM   3265 C  CA  . ASP B 1 141 ? -28.243 -40.707 11.566  1.00  11.35 ? 139 ASP A CA  1 
ATOM   3266 C  C   . ASP B 1 141 ? -29.159 -39.445 11.642  1.00  10.73 ? 139 ASP A C   1 
ATOM   3267 O  O   . ASP B 1 141 ? -28.683 -38.323 11.320  1.00  11.08 ? 139 ASP A O   1 
ATOM   3268 C  CB  . ASP B 1 141 ? -27.342 -40.566 10.317  1.00  12.38 ? 139 ASP A CB  1 
ATOM   3269 C  CG  . ASP B 1 141 ? -28.146 -40.653 8.994   1.00  13.89 ? 139 ASP A CG  1 
ATOM   3270 O  OD1 . ASP B 1 141 ? -29.319 -40.961 9.038   1.00  13.76 ? 139 ASP A OD1 1 
ATOM   3271 O  OD2 . ASP B 1 141 ? -27.570 -40.341 7.912   1.00  16.88 ? 139 ASP A OD2 1 
ATOM   3272 N  N   . GLY B 1 142 ? -30.414 -39.623 12.101  1.00  11.05 ? 140 GLY A N   1 
ATOM   3273 C  CA  . GLY B 1 142 ? -31.375 -38.548 11.995  1.00  8.93  ? 140 GLY A CA  1 
ATOM   3274 C  C   . GLY B 1 142 ? -31.126 -37.442 13.067  1.00  9.23  ? 140 GLY A C   1 
ATOM   3275 O  O   . GLY B 1 142 ? -31.322 -36.269 12.854  1.00  8.78  ? 140 GLY A O   1 
ATOM   3276 N  N   . LEU B 1 143 ? -30.883 -37.871 14.308  1.00  9.37  ? 141 LEU A N   1 
ATOM   3277 C  CA  . LEU B 1 143 ? -30.949 -36.898 15.471  1.00  9.25  ? 141 LEU A CA  1 
ATOM   3278 C  C   . LEU B 1 143 ? -29.569 -36.864 16.170  1.00  9.32  ? 141 LEU A C   1 
ATOM   3279 O  O   . LEU B 1 143 ? -28.864 -37.829 16.166  1.00  10.54 ? 141 LEU A O   1 
ATOM   3280 C  CB  . LEU B 1 143 ? -31.958 -37.320 16.516  1.00  8.74  ? 141 LEU A CB  1 
ATOM   3281 C  CG  . LEU B 1 143 ? -33.428 -37.569 15.996  1.00  7.99  ? 141 LEU A CG  1 
ATOM   3282 C  CD1 . LEU B 1 143 ? -34.405 -37.944 17.143  1.00  8.25  ? 141 LEU A CD1 1 
ATOM   3283 C  CD2 . LEU B 1 143 ? -33.875 -36.223 15.295  1.00  9.80  ? 141 LEU A CD2 1 
ATOM   3284 N  N   . ALA B 1 144 ? -29.282 -35.735 16.800  1.00  8.70  ? 142 ALA A N   1 
ATOM   3285 C  CA  . ALA B 1 144 ? -28.023 -35.550 17.640  1.00  8.69  ? 142 ALA A CA  1 
ATOM   3286 C  C   . ALA B 1 144 ? -28.493 -34.814 18.893  1.00  8.05  ? 142 ALA A C   1 
ATOM   3287 O  O   . ALA B 1 144 ? -29.155 -33.784 18.802  1.00  9.47  ? 142 ALA A O   1 
ATOM   3288 C  CB  . ALA B 1 144 ? -27.003 -34.685 16.892  1.00  10.27 ? 142 ALA A CB  1 
ATOM   3289 N  N   . VAL B 1 145 ? -28.175 -35.334 20.072  1.00  8.14  ? 143 VAL A N   1 
ATOM   3290 C  CA  . VAL B 1 145 ? -28.687 -34.711 21.311  1.00  7.06  ? 143 VAL A CA  1 
ATOM   3291 C  C   . VAL B 1 145 ? -27.487 -34.454 22.207  1.00  7.98  ? 143 VAL A C   1 
ATOM   3292 O  O   . VAL B 1 145 ? -26.683 -35.427 22.439  1.00  7.58  ? 143 VAL A O   1 
ATOM   3293 C  CB  . VAL B 1 145 ? -29.734 -35.602 22.058  1.00  7.68  ? 143 VAL A CB  1 
ATOM   3294 C  CG1 . VAL B 1 145 ? -30.252 -34.901 23.281  1.00  7.22  ? 143 VAL A CG1 1 
ATOM   3295 C  CG2 . VAL B 1 145 ? -30.919 -35.931 21.085  1.00  9.16  ? 143 VAL A CG2 1 
ATOM   3296 N  N   . LEU B 1 146 ? -27.364 -33.202 22.712  1.00  8.03  ? 144 LEU A N   1 
ATOM   3297 C  CA  . LEU B 1 146 ? -26.373 -32.857 23.737  1.00  8.29  ? 144 LEU A CA  1 
ATOM   3298 C  C   . LEU B 1 146 ? -27.017 -33.135 25.074  1.00  8.97  ? 144 LEU A C   1 
ATOM   3299 O  O   . LEU B 1 146 ? -28.147 -32.651 25.290  1.00  10.73 ? 144 LEU A O   1 
ATOM   3300 C  CB  . LEU B 1 146 ? -25.942 -31.371 23.761  1.00  10.49 ? 144 LEU A CB  1 
ATOM   3301 C  CG  . LEU B 1 146 ? -25.397 -30.949 22.471  1.00  13.30 ? 144 LEU A CG  1 
ATOM   3302 C  CD1 . LEU B 1 146 ? -25.152 -29.451 22.516  1.00  14.89 ? 144 LEU A CD1 1 
ATOM   3303 C  CD2 . LEU B 1 146 ? -24.019 -31.590 22.275  1.00  14.07 ? 144 LEU A CD2 1 
ATOM   3304 N  N   . GLY B 1 147 ? -26.329 -33.892 25.950  1.00  8.95  ? 145 GLY A N   1 
ATOM   3305 C  CA  . GLY B 1 147 ? -26.753 -34.054 27.352  1.00  8.84  ? 145 GLY A CA  1 
ATOM   3306 C  C   . GLY B 1 147 ? -25.824 -33.255 28.266  1.00  9.03  ? 145 GLY A C   1 
ATOM   3307 O  O   . GLY B 1 147 ? -24.598 -33.309 28.096  1.00  8.97  ? 145 GLY A O   1 
ATOM   3308 N  N   . VAL B 1 148 ? -26.411 -32.481 29.156  1.00  8.18  ? 146 VAL A N   1 
ATOM   3309 C  CA  . VAL B 1 148 ? -25.694 -31.667 30.156  1.00  8.88  ? 146 VAL A CA  1 
ATOM   3310 C  C   . VAL B 1 148 ? -26.184 -32.053 31.532  1.00  8.54  ? 146 VAL A C   1 
ATOM   3311 O  O   . VAL B 1 148 ? -27.407 -31.978 31.825  1.00  8.62  ? 146 VAL A O   1 
ATOM   3312 C  CB  . VAL B 1 148 ? -25.862 -30.150 29.890  1.00  9.45  ? 146 VAL A CB  1 
ATOM   3313 C  CG1 . VAL B 1 148 ? -25.071 -29.347 30.944  1.00  10.26 ? 146 VAL A CG1 1 
ATOM   3314 C  CG2 . VAL B 1 148 ? -25.300 -29.808 28.471  1.00  10.61 ? 146 VAL A CG2 1 
ATOM   3315 N  N   . PHE B 1 149 ? -25.229 -32.429 32.416  1.00  7.88  ? 147 PHE A N   1 
ATOM   3316 C  CA  . PHE B 1 149 ? -25.662 -32.792 33.792  1.00  8.50  ? 147 PHE A CA  1 
ATOM   3317 C  C   . PHE B 1 149 ? -25.836 -31.571 34.639  1.00  8.53  ? 147 PHE A C   1 
ATOM   3318 O  O   . PHE B 1 149 ? -25.117 -30.585 34.432  1.00  9.01  ? 147 PHE A O   1 
ATOM   3319 C  CB  . PHE B 1 149 ? -24.540 -33.679 34.414  1.00  8.20  ? 147 PHE A CB  1 
ATOM   3320 C  CG  . PHE B 1 149 ? -24.384 -35.044 33.743  1.00  8.72  ? 147 PHE A CG  1 
ATOM   3321 C  CD1 . PHE B 1 149 ? -25.470 -35.954 33.696  1.00  9.87  ? 147 PHE A CD1 1 
ATOM   3322 C  CD2 . PHE B 1 149 ? -23.149 -35.375 33.114  1.00  9.24  ? 147 PHE A CD2 1 
ATOM   3323 C  CE1 . PHE B 1 149 ? -25.290 -37.214 33.077  1.00  8.81  ? 147 PHE A CE1 1 
ATOM   3324 C  CE2 . PHE B 1 149 ? -22.918 -36.632 32.554  1.00  9.73  ? 147 PHE A CE2 1 
ATOM   3325 C  CZ  . PHE B 1 149 ? -24.036 -37.530 32.462  1.00  9.07  ? 147 PHE A CZ  1 
ATOM   3326 N  N   . LEU B 1 150 ? -26.796 -31.594 35.573  1.00  9.18  ? 148 LEU A N   1 
ATOM   3327 C  CA  . LEU B 1 150 ? -26.951 -30.496 36.552  1.00  9.91  ? 148 LEU A CA  1 
ATOM   3328 C  C   . LEU B 1 150 ? -26.653 -31.071 37.919  1.00  10.41 ? 148 LEU A C   1 
ATOM   3329 O  O   . LEU B 1 150 ? -27.280 -32.034 38.303  1.00  11.01 ? 148 LEU A O   1 
ATOM   3330 C  CB  . LEU B 1 150 ? -28.396 -29.888 36.543  1.00  10.78 ? 148 LEU A CB  1 
ATOM   3331 C  CG  . LEU B 1 150 ? -28.720 -29.020 35.313  1.00  10.29 ? 148 LEU A CG  1 
ATOM   3332 C  CD1 . LEU B 1 150 ? -28.940 -29.931 34.101  1.00  12.38 ? 148 LEU A CD1 1 
ATOM   3333 C  CD2 . LEU B 1 150 ? -30.029 -28.199 35.533  1.00  11.86 ? 148 LEU A CD2 1 
ATOM   3334 N  N   . GLN B 1 151 ? -25.738 -30.405 38.640  1.00  9.65  ? 149 GLN A N   1 
ATOM   3335 C  CA  . GLN B 1 151 ? -25.374 -30.829 39.984  1.00  11.42 ? 149 GLN A CA  1 
ATOM   3336 C  C   . GLN B 1 151 ? -25.886 -29.789 40.961  1.00  12.40 ? 149 GLN A C   1 
ATOM   3337 O  O   . GLN B 1 151 ? -25.938 -28.615 40.592  1.00  12.10 ? 149 GLN A O   1 
ATOM   3338 C  CB  . GLN B 1 151 ? -23.851 -31.005 40.142  1.00  12.78 ? 149 GLN A CB  1 
ATOM   3339 C  CG  . GLN B 1 151 ? -23.088 -29.724 39.967  1.00  16.25 ? 149 GLN A CG  1 
ATOM   3340 C  CD  . GLN B 1 151 ? -21.581 -29.850 40.114  1.00  18.77 ? 149 GLN A CD  1 
ATOM   3341 O  OE1 . GLN B 1 151 ? -21.002 -30.958 40.305  1.00  19.65 ? 149 GLN A OE1 1 
ATOM   3342 N  NE2 . GLN B 1 151 ? -20.925 -28.675 40.042  1.00  20.49 ? 149 GLN A NE2 1 
ATOM   3343 N  N   . ILE B 1 152 ? -26.320 -30.229 42.169  1.00  12.88 ? 150 ILE A N   1 
ATOM   3344 C  CA  . ILE B 1 152 ? -26.740 -29.208 43.155  1.00  13.29 ? 150 ILE A CA  1 
ATOM   3345 C  C   . ILE B 1 152 ? -25.534 -28.330 43.492  1.00  15.80 ? 150 ILE A C   1 
ATOM   3346 O  O   . ILE B 1 152 ? -24.419 -28.824 43.729  1.00  15.15 ? 150 ILE A O   1 
ATOM   3347 C  CB  . ILE B 1 152 ? -27.280 -29.857 44.435  1.00  14.38 ? 150 ILE A CB  1 
ATOM   3348 C  CG1 . ILE B 1 152 ? -28.536 -30.658 44.128  1.00  15.09 ? 150 ILE A CG1 1 
ATOM   3349 C  CG2 . ILE B 1 152 ? -27.585 -28.807 45.533  1.00  14.90 ? 150 ILE A CG2 1 
ATOM   3350 C  CD1 . ILE B 1 152 ? -29.723 -29.905 43.526  1.00  14.94 ? 150 ILE A CD1 1 
ATOM   3351 N  N   . GLY B 1 153 ? -25.764 -27.032 43.483  1.00  15.69 ? 151 GLY A N   1 
ATOM   3352 C  CA  . GLY B 1 153 ? -24.680 -26.083 43.675  1.00  17.60 ? 151 GLY A CA  1 
ATOM   3353 C  C   . GLY B 1 153 ? -25.329 -24.698 43.828  1.00  17.86 ? 151 GLY A C   1 
ATOM   3354 O  O   . GLY B 1 153 ? -26.545 -24.553 44.095  1.00  19.93 ? 151 GLY A O   1 
ATOM   3355 N  N   A GLU B 1 154 ? -24.503 -23.718 43.444  0.50  21.38 ? 152 GLU A N   1 
ATOM   3356 N  N   B GLU B 1 154 ? -24.539 -23.673 43.879  0.50  19.58 ? 152 GLU A N   1 
ATOM   3357 C  CA  A GLU B 1 154 ? -24.865 -22.269 43.413  0.50  20.73 ? 152 GLU A CA  1 
ATOM   3358 C  CA  B GLU B 1 154 ? -25.194 -22.390 44.102  0.50  17.82 ? 152 GLU A CA  1 
ATOM   3359 C  C   A GLU B 1 154 ? -26.052 -22.025 42.483  0.50  20.68 ? 152 GLU A C   1 
ATOM   3360 C  C   B GLU B 1 154 ? -26.048 -22.097 42.826  0.50  19.48 ? 152 GLU A C   1 
ATOM   3361 O  O   A GLU B 1 154 ? -26.098 -22.614 41.379  0.50  18.78 ? 152 GLU A O   1 
ATOM   3362 O  O   B GLU B 1 154 ? -25.883 -22.772 41.791  0.50  18.67 ? 152 GLU A O   1 
ATOM   3363 C  CB  A GLU B 1 154 ? -23.636 -21.384 43.048  0.50  23.04 ? 152 GLU A CB  1 
ATOM   3364 C  CB  B GLU B 1 154 ? -24.138 -21.352 44.509  0.50  18.91 ? 152 GLU A CB  1 
ATOM   3365 C  CG  A GLU B 1 154 ? -23.575 -20.756 41.654  0.50  24.49 ? 152 GLU A CG  1 
ATOM   3366 C  CG  B GLU B 1 154 ? -23.411 -21.688 45.817  0.50  16.14 ? 152 GLU A CG  1 
ATOM   3367 C  CD  A GLU B 1 154 ? -22.556 -19.626 41.588  0.50  21.73 ? 152 GLU A CD  1 
ATOM   3368 C  CD  B GLU B 1 154 ? -21.971 -21.225 45.791  0.50  16.83 ? 152 GLU A CD  1 
ATOM   3369 O  OE1 A GLU B 1 154 ? -22.859 -18.470 41.244  0.50  23.78 ? 152 GLU A OE1 1 
ATOM   3370 O  OE1 B GLU B 1 154 ? -21.386 -21.132 44.686  0.50  16.75 ? 152 GLU A OE1 1 
ATOM   3371 O  OE2 A GLU B 1 154 ? -21.443 -19.888 41.919  0.50  21.70 ? 152 GLU A OE2 1 
ATOM   3372 O  OE2 B GLU B 1 154 ? -21.416 -20.892 46.864  0.50  17.56 ? 152 GLU A OE2 1 
ATOM   3373 N  N   . PRO B 1 155 ? -27.034 -21.183 42.913  1.00  18.01 ? 153 PRO A N   1 
ATOM   3374 C  CA  . PRO B 1 155 ? -28.066 -21.002 41.873  1.00  18.27 ? 153 PRO A CA  1 
ATOM   3375 C  C   . PRO B 1 155 ? -27.480 -20.547 40.518  1.00  18.20 ? 153 PRO A C   1 
ATOM   3376 O  O   . PRO B 1 155 ? -26.480 -19.807 40.447  1.00  18.82 ? 153 PRO A O   1 
ATOM   3377 C  CB  . PRO B 1 155 ? -28.994 -19.884 42.438  1.00  16.93 ? 153 PRO A CB  1 
ATOM   3378 C  CG  . PRO B 1 155 ? -28.260 -19.370 43.616  1.00  16.03 ? 153 PRO A CG  1 
ATOM   3379 C  CD  . PRO B 1 155 ? -27.378 -20.469 44.151  1.00  17.68 ? 153 PRO A CD  1 
ATOM   3380 N  N   . ASN B 1 156 ? -28.158 -20.973 39.455  1.00  15.42 ? 154 ASN A N   1 
ATOM   3381 C  CA  . ASN B 1 156 ? -27.721 -20.743 38.120  1.00  15.66 ? 154 ASN A CA  1 
ATOM   3382 C  C   . ASN B 1 156 ? -28.597 -19.680 37.449  1.00  15.57 ? 154 ASN A C   1 
ATOM   3383 O  O   . ASN B 1 156 ? -29.815 -19.892 37.156  1.00  14.80 ? 154 ASN A O   1 
ATOM   3384 C  CB  . ASN B 1 156 ? -27.817 -22.062 37.332  1.00  17.16 ? 154 ASN A CB  1 
ATOM   3385 C  CG  . ASN B 1 156 ? -27.038 -22.000 36.034  1.00  18.65 ? 154 ASN A CG  1 
ATOM   3386 O  OD1 . ASN B 1 156 ? -26.904 -20.906 35.424  1.00  20.91 ? 154 ASN A OD1 1 
ATOM   3387 N  ND2 . ASN B 1 156 ? -26.545 -23.160 35.570  1.00  15.62 ? 154 ASN A ND2 1 
ATOM   3388 N  N   . SER B 1 157 ? -28.028 -18.465 37.325  1.00  18.61 ? 155 SER A N   1 
ATOM   3389 C  CA  . SER B 1 157 ? -28.781 -17.329 36.777  1.00  19.97 ? 155 SER A CA  1 
ATOM   3390 C  C   . SER B 1 157 ? -29.258 -17.587 35.359  1.00  19.10 ? 155 SER A C   1 
ATOM   3391 O  O   . SER B 1 157 ? -30.258 -17.025 34.910  1.00  20.12 ? 155 SER A O   1 
ATOM   3392 C  CB  . SER B 1 157 ? -27.931 -16.044 36.814  1.00  23.98 ? 155 SER A CB  1 
ATOM   3393 O  OG  . SER B 1 157 ? -26.779 -16.276 35.986  1.00  25.86 ? 155 SER A OG  1 
ATOM   3394 N  N   . GLN B 1 158 ? -28.592 -18.541 34.701  1.00  18.69 ? 156 GLN A N   1 
ATOM   3395 C  CA  . GLN B 1 158 ? -28.966 -18.834 33.331  1.00  18.85 ? 156 GLN A CA  1 
ATOM   3396 C  C   . GLN B 1 158 ? -30.233 -19.611 33.245  1.00  19.83 ? 156 GLN A C   1 
ATOM   3397 O  O   . GLN B 1 158 ? -30.732 -19.775 32.146  1.00  22.92 ? 156 GLN A O   1 
ATOM   3398 C  CB  . GLN B 1 158 ? -27.860 -19.576 32.574  1.00  23.90 ? 156 GLN A CB  1 
ATOM   3399 C  CG  . GLN B 1 158 ? -26.525 -18.852 32.611  1.00  28.25 ? 156 GLN A CG  1 
ATOM   3400 C  CD  . GLN B 1 158 ? -26.525 -17.462 31.945  1.00  31.32 ? 156 GLN A CD  1 
ATOM   3401 O  OE1 . GLN B 1 158 ? -25.658 -16.629 32.266  1.00  37.93 ? 156 GLN A OE1 1 
ATOM   3402 N  NE2 . GLN B 1 158 ? -27.427 -17.229 30.966  1.00  27.89 ? 156 GLN A NE2 1 
ATOM   3403 N  N   . LEU B 1 159 ? -30.708 -20.198 34.360  1.00  19.97 ? 157 LEU A N   1 
ATOM   3404 C  CA  . LEU B 1 159 ? -32.009 -20.852 34.333  1.00  18.15 ? 157 LEU A CA  1 
ATOM   3405 C  C   . LEU B 1 159 ? -33.190 -19.896 34.608  1.00  22.30 ? 157 LEU A C   1 
ATOM   3406 O  O   . LEU B 1 159 ? -34.334 -20.406 34.553  1.00  20.08 ? 157 LEU A O   1 
ATOM   3407 C  CB  . LEU B 1 159 ? -32.106 -21.993 35.374  1.00  20.66 ? 157 LEU A CB  1 
ATOM   3408 C  CG  . LEU B 1 159 ? -31.144 -23.160 35.155  1.00  17.28 ? 157 LEU A CG  1 
ATOM   3409 C  CD1 . LEU B 1 159 ? -31.066 -24.010 36.405  1.00  18.91 ? 157 LEU A CD1 1 
ATOM   3410 C  CD2 . LEU B 1 159 ? -31.542 -24.057 33.987  1.00  16.89 ? 157 LEU A CD2 1 
ATOM   3411 N  N   . GLN B 1 160 ? -32.951 -18.582 34.878  1.00  22.70 ? 158 GLN A N   1 
ATOM   3412 C  CA  . GLN B 1 160 ? -34.024 -17.638 35.290  1.00  20.06 ? 158 GLN A CA  1 
ATOM   3413 C  C   . GLN B 1 160 ? -35.081 -17.462 34.200  1.00  18.61 ? 158 GLN A C   1 
ATOM   3414 O  O   . GLN B 1 160 ? -36.286 -17.392 34.505  1.00  20.79 ? 158 GLN A O   1 
ATOM   3415 C  CB  . GLN B 1 160 ? -33.483 -16.199 35.632  1.00  22.67 ? 158 GLN A CB  1 
ATOM   3416 C  CG  . GLN B 1 160 ? -34.596 -15.243 36.116  1.00  24.08 ? 158 GLN A CG  1 
ATOM   3417 C  CD  . GLN B 1 160 ? -34.302 -13.735 36.059  1.00  33.17 ? 158 GLN A CD  1 
ATOM   3418 O  OE1 . GLN B 1 160 ? -35.216 -12.906 36.277  1.00  33.78 ? 158 GLN A OE1 1 
ATOM   3419 N  NE2 . GLN B 1 160 ? -33.041 -13.356 35.825  1.00  30.71 ? 158 GLN A NE2 1 
ATOM   3420 N  N   . LYS B 1 161 ? -34.662 -17.328 32.948  1.00  18.53 ? 159 LYS A N   1 
ATOM   3421 C  CA  . LYS B 1 161 ? -35.659 -17.067 31.943  1.00  17.77 ? 159 LYS A CA  1 
ATOM   3422 C  C   . LYS B 1 161 ? -36.633 -18.247 31.997  1.00  17.92 ? 159 LYS A C   1 
ATOM   3423 O  O   . LYS B 1 161 ? -37.864 -18.041 32.013  1.00  17.78 ? 159 LYS A O   1 
ATOM   3424 C  CB  . LYS B 1 161 ? -35.052 -16.939 30.539  1.00  18.74 ? 159 LYS A CB  1 
ATOM   3425 C  CG  . LYS B 1 161 ? -36.016 -16.263 29.544  1.00  20.42 ? 159 LYS A CG  1 
ATOM   3426 C  CD  . LYS B 1 161 ? -35.331 -16.071 28.189  1.00  19.23 ? 159 LYS A CD  1 
ATOM   3427 C  CE  . LYS B 1 161 ? -36.375 -16.085 27.062  1.00  19.52 ? 159 LYS A CE  1 
ATOM   3428 N  NZ  . LYS B 1 161 ? -36.994 -14.672 27.071  1.00  18.96 ? 159 LYS A NZ  1 
ATOM   3429 N  N   . ILE B 1 162 ? -36.108 -19.484 32.117  1.00  18.04 ? 160 ILE A N   1 
ATOM   3430 C  CA  . ILE B 1 162 ? -36.998 -20.676 32.226  1.00  13.12 ? 160 ILE A CA  1 
ATOM   3431 C  C   . ILE B 1 162 ? -37.917 -20.673 33.508  1.00  12.71 ? 160 ILE A C   1 
ATOM   3432 O  O   . ILE B 1 162 ? -39.155 -20.851 33.415  1.00  12.53 ? 160 ILE A O   1 
ATOM   3433 C  CB  . ILE B 1 162 ? -36.205 -22.019 32.169  1.00  11.34 ? 160 ILE A CB  1 
ATOM   3434 C  CG1 . ILE B 1 162 ? -35.579 -22.159 30.767  1.00  11.26 ? 160 ILE A CG1 1 
ATOM   3435 C  CG2 . ILE B 1 162 ? -37.159 -23.182 32.372  1.00  10.35 ? 160 ILE A CG2 1 
ATOM   3436 C  CD1 . ILE B 1 162 ? -34.478 -23.244 30.654  1.00  10.84 ? 160 ILE A CD1 1 
ATOM   3437 N  N   . THR B 1 163 ? -37.298 -20.576 34.652  1.00  13.96 ? 161 THR A N   1 
ATOM   3438 C  CA  . THR B 1 163 ? -38.042 -20.805 35.869  1.00  16.37 ? 161 THR A CA  1 
ATOM   3439 C  C   . THR B 1 163 ? -39.115 -19.711 36.049  1.00  15.86 ? 161 THR A C   1 
ATOM   3440 O  O   . THR B 1 163 ? -40.150 -20.025 36.628  1.00  15.52 ? 161 THR A O   1 
ATOM   3441 C  CB  . THR B 1 163 ? -37.160 -20.847 37.124  1.00  19.47 ? 161 THR A CB  1 
ATOM   3442 O  OG1 . THR B 1 163 ? -36.445 -19.591 37.225  1.00  17.69 ? 161 THR A OG1 1 
ATOM   3443 C  CG2 . THR B 1 163 ? -36.244 -22.144 37.104  1.00  18.15 ? 161 THR A CG2 1 
ATOM   3444 N  N   . ASP B 1 164 ? -38.856 -18.473 35.602  1.00  17.41 ? 162 ASP A N   1 
ATOM   3445 C  CA  . ASP B 1 164 ? -39.860 -17.402 35.581  1.00  16.96 ? 162 ASP A CA  1 
ATOM   3446 C  C   . ASP B 1 164 ? -41.107 -17.711 34.786  1.00  18.74 ? 162 ASP A C   1 
ATOM   3447 O  O   . ASP B 1 164 ? -42.175 -17.072 35.000  1.00  19.06 ? 162 ASP A O   1 
ATOM   3448 C  CB  . ASP B 1 164 ? -39.304 -16.143 34.924  1.00  20.59 ? 162 ASP A CB  1 
ATOM   3449 C  CG  . ASP B 1 164 ? -38.415 -15.340 35.833  1.00  24.61 ? 162 ASP A CG  1 
ATOM   3450 O  OD1 . ASP B 1 164 ? -38.265 -15.739 37.038  1.00  27.55 ? 162 ASP A OD1 1 
ATOM   3451 O  OD2 . ASP B 1 164 ? -37.918 -14.273 35.312  1.00  26.93 ? 162 ASP A OD2 1 
ATOM   3452 N  N   . THR B 1 165 ? -41.031 -18.699 33.870  1.00  14.98 ? 163 THR A N   1 
ATOM   3453 C  CA  . THR B 1 165 ? -42.235 -18.997 33.099  1.00  14.73 ? 163 THR A CA  1 
ATOM   3454 C  C   . THR B 1 165 ? -43.068 -20.151 33.630  1.00  14.98 ? 163 THR A C   1 
ATOM   3455 O  O   . THR B 1 165 ? -44.193 -20.378 33.129  1.00  15.85 ? 163 THR A O   1 
ATOM   3456 C  CB  . THR B 1 165 ? -41.920 -19.371 31.655  1.00  16.65 ? 163 THR A CB  1 
ATOM   3457 O  OG1 . THR B 1 165 ? -41.251 -20.635 31.648  1.00  16.12 ? 163 THR A OG1 1 
ATOM   3458 C  CG2 . THR B 1 165 ? -41.097 -18.315 30.974  1.00  16.12 ? 163 THR A CG2 1 
ATOM   3459 N  N   . LEU B 1 166 ? -42.568 -20.863 34.638  1.00  14.29 ? 164 LEU A N   1 
ATOM   3460 C  CA  . LEU B 1 166 ? -43.204 -22.140 35.038  1.00  13.11 ? 164 LEU A CA  1 
ATOM   3461 C  C   . LEU B 1 166 ? -44.617 -22.002 35.557  1.00  15.14 ? 164 LEU A C   1 
ATOM   3462 O  O   . LEU B 1 166 ? -45.497 -22.827 35.220  1.00  15.27 ? 164 LEU A O   1 
ATOM   3463 C  CB  . LEU B 1 166 ? -42.357 -23.028 35.965  1.00  14.71 ? 164 LEU A CB  1 
ATOM   3464 C  CG  . LEU B 1 166 ? -40.947 -23.301 35.419  1.00  13.72 ? 164 LEU A CG  1 
ATOM   3465 C  CD1 . LEU B 1 166 ? -40.079 -23.984 36.513  1.00  15.56 ? 164 LEU A CD1 1 
ATOM   3466 C  CD2 . LEU B 1 166 ? -41.065 -24.121 34.152  1.00  15.85 ? 164 LEU A CD2 1 
ATOM   3467 N  N   . ASP B 1 167 ? -44.899 -20.874 36.191  1.00  15.91 ? 165 ASP A N   1 
ATOM   3468 C  CA  . ASP B 1 167 ? -46.287 -20.739 36.726  1.00  19.43 ? 165 ASP A CA  1 
ATOM   3469 C  C   . ASP B 1 167 ? -47.254 -20.622 35.568  1.00  19.07 ? 165 ASP A C   1 
ATOM   3470 O  O   . ASP B 1 167 ? -48.357 -21.197 35.602  1.00  21.67 ? 165 ASP A O   1 
ATOM   3471 C  CB  . ASP B 1 167 ? -46.381 -19.508 37.606  1.00  21.26 ? 165 ASP A CB  1 
ATOM   3472 C  CG  . ASP B 1 167 ? -45.845 -19.774 39.036  1.00  24.38 ? 165 ASP A CG  1 
ATOM   3473 O  OD1 . ASP B 1 167 ? -45.830 -20.945 39.498  1.00  30.30 ? 165 ASP A OD1 1 
ATOM   3474 O  OD2 . ASP B 1 167 ? -45.468 -18.780 39.708  1.00  29.66 ? 165 ASP A OD2 1 
ATOM   3475 N  N   . SER B 1 168 ? -46.835 -19.899 34.539  1.00  18.11 ? 166 SER A N   1 
ATOM   3476 C  CA  . SER B 1 168 ? -47.686 -19.737 33.323  1.00  17.96 ? 166 SER A CA  1 
ATOM   3477 C  C   . SER B 1 168 ? -47.923 -21.006 32.512  1.00  14.92 ? 166 SER A C   1 
ATOM   3478 O  O   . SER B 1 168 ? -48.881 -21.054 31.726  1.00  16.16 ? 166 SER A O   1 
ATOM   3479 C  CB  . SER B 1 168 ? -47.162 -18.601 32.432  1.00  17.97 ? 166 SER A CB  1 
ATOM   3480 O  OG  . SER B 1 168 ? -46.049 -19.052 31.667  1.00  19.07 ? 166 SER A OG  1 
ATOM   3481 N  N   . ILE B 1 169 ? -47.078 -22.026 32.711  1.00  12.88 ? 167 ILE A N   1 
ATOM   3482 C  CA  . ILE B 1 169 ? -47.295 -23.344 32.013  1.00  11.74 ? 167 ILE A CA  1 
ATOM   3483 C  C   . ILE B 1 169 ? -47.521 -24.473 32.989  1.00  12.90 ? 167 ILE A C   1 
ATOM   3484 O  O   . ILE B 1 169 ? -47.091 -25.608 32.760  1.00  14.20 ? 167 ILE A O   1 
ATOM   3485 C  CB  . ILE B 1 169 ? -46.213 -23.672 30.996  1.00  12.40 ? 167 ILE A CB  1 
ATOM   3486 C  CG1 . ILE B 1 169 ? -44.819 -23.745 31.667  1.00  13.45 ? 167 ILE A CG1 1 
ATOM   3487 C  CG2 . ILE B 1 169 ? -46.213 -22.630 29.848  1.00  11.34 ? 167 ILE A CG2 1 
ATOM   3488 C  CD1 . ILE B 1 169 ? -43.723 -24.329 30.696  1.00  15.00 ? 167 ILE A CD1 1 
ATOM   3489 N  N   . LYS B 1 170 ? -48.201 -24.196 34.126  1.00  14.76 ? 168 LYS A N   1 
ATOM   3490 C  CA  . LYS B 1 170 ? -48.366 -25.268 35.139  1.00  14.20 ? 168 LYS A CA  1 
ATOM   3491 C  C   . LYS B 1 170 ? -49.119 -26.493 34.602  1.00  14.39 ? 168 LYS A C   1 
ATOM   3492 O  O   . LYS B 1 170 ? -48.704 -27.671 34.799  1.00  15.71 ? 168 LYS A O   1 
ATOM   3493 C  CB  . LYS B 1 170 ? -49.114 -24.694 36.403  1.00  19.79 ? 168 LYS A CB  1 
ATOM   3494 C  CG  . LYS B 1 170 ? -49.174 -25.747 37.523  1.00  21.55 ? 168 LYS A CG  1 
ATOM   3495 C  CD  . LYS B 1 170 ? -49.877 -25.273 38.822  1.00  27.78 ? 168 LYS A CD  1 
ATOM   3496 C  CE  . LYS B 1 170 ? -49.594 -26.222 40.027  1.00  33.25 ? 168 LYS A CE  1 
ATOM   3497 N  NZ  . LYS B 1 170 ? -48.185 -26.252 40.596  1.00  27.49 ? 168 LYS A NZ  1 
ATOM   3498 N  N   . GLU B 1 171 ? -50.168 -26.243 33.797  1.00  16.29 ? 169 GLU A N   1 
ATOM   3499 C  CA  . GLU B 1 171 ? -50.987 -27.367 33.278  1.00  17.52 ? 169 GLU A CA  1 
ATOM   3500 C  C   . GLU B 1 171 ? -50.444 -27.890 31.989  1.00  16.08 ? 169 GLU A C   1 
ATOM   3501 O  O   . GLU B 1 171 ? -49.946 -27.080 31.190  1.00  15.37 ? 169 GLU A O   1 
ATOM   3502 C  CB  . GLU B 1 171 ? -52.438 -26.944 33.016  1.00  19.77 ? 169 GLU A CB  1 
ATOM   3503 C  CG  . GLU B 1 171 ? -53.169 -26.613 34.301  1.00  25.40 ? 169 GLU A CG  1 
ATOM   3504 C  CD  . GLU B 1 171 ? -52.801 -25.213 34.849  1.00  34.40 ? 169 GLU A CD  1 
ATOM   3505 O  OE1 . GLU B 1 171 ? -52.995 -24.989 36.073  1.00  47.89 ? 169 GLU A OE1 1 
ATOM   3506 O  OE2 . GLU B 1 171 ? -52.277 -24.331 34.089  1.00  38.64 ? 169 GLU A OE2 1 
ATOM   3507 N  N   . LYS B 1 172 ? -50.556 -29.201 31.798  1.00  15.02 ? 170 LYS A N   1 
ATOM   3508 C  CA  . LYS B 1 172 ? -50.211 -29.851 30.503  1.00  15.51 ? 170 LYS A CA  1 
ATOM   3509 C  C   . LYS B 1 172 ? -50.959 -29.123 29.371  1.00  16.47 ? 170 LYS A C   1 
ATOM   3510 O  O   . LYS B 1 172 ? -52.177 -28.847 29.456  1.00  15.34 ? 170 LYS A O   1 
ATOM   3511 C  CB  . LYS B 1 172 ? -50.595 -31.328 30.533  1.00  15.89 ? 170 LYS A CB  1 
ATOM   3512 C  CG  . LYS B 1 172 ? -50.392 -32.068 29.235  1.00  16.96 ? 170 LYS A CG  1 
ATOM   3513 C  CD  . LYS B 1 172 ? -50.694 -33.572 29.363  1.00  18.69 ? 170 LYS A CD  1 
ATOM   3514 C  CE  . LYS B 1 172 ? -50.490 -34.249 28.002  1.00  20.00 ? 170 LYS A CE  1 
ATOM   3515 N  NZ  . LYS B 1 172 ? -50.529 -35.753 28.109  1.00  24.08 ? 170 LYS A NZ  1 
ATOM   3516 N  N   . GLY B 1 173 ? -50.247 -28.839 28.290  1.00  15.45 ? 171 GLY A N   1 
ATOM   3517 C  CA  . GLY B 1 173 ? -50.761 -28.151 27.089  1.00  15.52 ? 171 GLY A CA  1 
ATOM   3518 C  C   . GLY B 1 173 ? -50.673 -26.653 27.049  1.00  15.37 ? 171 GLY A C   1 
ATOM   3519 O  O   . GLY B 1 173 ? -50.808 -26.065 25.942  1.00  20.11 ? 171 GLY A O   1 
ATOM   3520 N  N   . LYS B 1 174 ? -50.313 -26.015 28.186  1.00  13.51 ? 172 LYS A N   1 
ATOM   3521 C  CA  . LYS B 1 174 ? -50.069 -24.556 28.255  1.00  14.38 ? 172 LYS A CA  1 
ATOM   3522 C  C   . LYS B 1 174 ? -48.763 -24.196 27.521  1.00  14.77 ? 172 LYS A C   1 
ATOM   3523 O  O   . LYS B 1 174 ? -47.802 -24.988 27.560  1.00  14.80 ? 172 LYS A O   1 
ATOM   3524 C  CB  . LYS B 1 174 ? -50.016 -24.062 29.698  1.00  16.69 ? 172 LYS A CB  1 
ATOM   3525 C  CG  . LYS B 1 174 ? -51.370 -24.216 30.453  1.00  23.63 ? 172 LYS A CG  1 
ATOM   3526 C  CD  . LYS B 1 174 ? -52.397 -23.234 29.945  1.00  30.01 ? 172 LYS A CD  1 
ATOM   3527 C  CE  . LYS B 1 174 ? -53.695 -23.254 30.765  1.00  35.85 ? 172 LYS A CE  1 
ATOM   3528 N  NZ  . LYS B 1 174 ? -53.330 -22.743 32.125  1.00  40.96 ? 172 LYS A NZ  1 
ATOM   3529 N  N   . GLN B 1 175 ? -48.767 -23.027 26.880  1.00  13.28 ? 173 GLN A N   1 
ATOM   3530 C  CA  . GLN B 1 175 ? -47.546 -22.501 26.245  1.00  15.47 ? 173 GLN A CA  1 
ATOM   3531 C  C   . GLN B 1 175 ? -47.462 -20.986 26.435  1.00  15.68 ? 173 GLN A C   1 
ATOM   3532 O  O   . GLN B 1 175 ? -48.476 -20.274 26.771  1.00  16.16 ? 173 GLN A O   1 
ATOM   3533 C  CB  . GLN B 1 175 ? -47.464 -22.929 24.765  1.00  14.79 ? 173 GLN A CB  1 
ATOM   3534 C  CG  . GLN B 1 175 ? -48.365 -22.080 23.865  1.00  17.45 ? 173 GLN A CG  1 
ATOM   3535 C  CD  . GLN B 1 175 ? -48.415 -22.573 22.421  1.00  18.79 ? 173 GLN A CD  1 
ATOM   3536 O  OE1 . GLN B 1 175 ? -48.241 -21.791 21.476  1.00  21.19 ? 173 GLN A OE1 1 
ATOM   3537 N  NE2 . GLN B 1 175 ? -48.594 -23.870 22.244  1.00  19.22 ? 173 GLN A NE2 1 
ATOM   3538 N  N   A THR B 1 176 ? -46.251 -20.446 26.345  0.50  13.47 ? 174 THR A N   1 
ATOM   3539 N  N   B THR B 1 176 ? -46.245 -20.484 26.252  0.50  14.02 ? 174 THR A N   1 
ATOM   3540 C  CA  A THR B 1 176 ? -46.132 -18.984 26.330  0.50  14.19 ? 174 THR A CA  1 
ATOM   3541 C  CA  B THR B 1 176 ? -45.949 -19.088 26.489  0.50  15.26 ? 174 THR A CA  1 
ATOM   3542 C  C   A THR B 1 176 ? -44.961 -18.581 25.485  0.50  14.33 ? 174 THR A C   1 
ATOM   3543 C  C   B THR B 1 176 ? -44.921 -18.619 25.478  0.50  14.89 ? 174 THR A C   1 
ATOM   3544 O  O   A THR B 1 176 ? -44.026 -19.373 25.229  0.50  14.43 ? 174 THR A O   1 
ATOM   3545 O  O   B THR B 1 176 ? -43.993 -19.382 25.150  0.50  14.77 ? 174 THR A O   1 
ATOM   3546 C  CB  A THR B 1 176 ? -45.974 -18.413 27.759  0.50  15.34 ? 174 THR A CB  1 
ATOM   3547 C  CB  B THR B 1 176 ? -45.383 -18.985 27.915  0.50  16.40 ? 174 THR A CB  1 
ATOM   3548 O  OG1 A THR B 1 176 ? -46.202 -16.993 27.772  0.50  15.03 ? 174 THR A OG1 1 
ATOM   3549 O  OG1 B THR B 1 176 ? -46.471 -19.146 28.848  0.50  17.07 ? 174 THR A OG1 1 
ATOM   3550 C  CG2 A THR B 1 176 ? -44.576 -18.774 28.343  0.50  13.75 ? 174 THR A CG2 1 
ATOM   3551 C  CG2 B THR B 1 176 ? -44.738 -17.636 28.115  0.50  16.33 ? 174 THR A CG2 1 
ATOM   3552 N  N   A ARG B 1 177 ? -45.016 -17.352 25.012  0.50  13.06 ? 175 ARG A N   1 
ATOM   3553 N  N   B ARG B 1 177 ? -45.040 -17.411 24.933  0.50  13.05 ? 175 ARG A N   1 
ATOM   3554 C  CA  A ARG B 1 177 ? -43.960 -16.762 24.223  0.50  13.14 ? 175 ARG A CA  1 
ATOM   3555 C  CA  B ARG B 1 177 ? -43.939 -16.938 24.086  0.50  12.72 ? 175 ARG A CA  1 
ATOM   3556 C  C   A ARG B 1 177 ? -42.551 -16.824 24.876  0.50  12.89 ? 175 ARG A C   1 
ATOM   3557 C  C   B ARG B 1 177 ? -42.634 -17.062 24.876  0.50  12.42 ? 175 ARG A C   1 
ATOM   3558 O  O   A ARG B 1 177 ? -42.379 -16.359 26.000  0.50  14.25 ? 175 ARG A O   1 
ATOM   3559 O  O   B ARG B 1 177 ? -42.642 -16.935 26.115  0.50  13.53 ? 175 ARG A O   1 
ATOM   3560 C  CB  A ARG B 1 177 ? -44.362 -15.317 23.995  0.50  12.93 ? 175 ARG A CB  1 
ATOM   3561 C  CB  B ARG B 1 177 ? -44.130 -15.497 23.591  0.50  12.54 ? 175 ARG A CB  1 
ATOM   3562 C  CG  A ARG B 1 177 ? -43.273 -14.555 23.261  0.50  15.35 ? 175 ARG A CG  1 
ATOM   3563 C  CG  B ARG B 1 177 ? -42.983 -15.011 22.643  0.50  12.95 ? 175 ARG A CG  1 
ATOM   3564 C  CD  A ARG B 1 177 ? -43.800 -13.235 22.756  0.50  15.21 ? 175 ARG A CD  1 
ATOM   3565 C  CD  B ARG B 1 177 ? -43.418 -13.883 21.718  0.50  14.91 ? 175 ARG A CD  1 
ATOM   3566 N  NE  A ARG B 1 177 ? -43.036 -12.839 21.591  0.50  18.02 ? 175 ARG A NE  1 
ATOM   3567 N  NE  B ARG B 1 177 ? -42.386 -13.133 20.966  0.50  15.39 ? 175 ARG A NE  1 
ATOM   3568 C  CZ  A ARG B 1 177 ? -42.069 -11.934 21.556  0.50  20.03 ? 175 ARG A CZ  1 
ATOM   3569 C  CZ  B ARG B 1 177 ? -41.871 -13.414 19.767  0.50  16.03 ? 175 ARG A CZ  1 
ATOM   3570 N  NH1 A ARG B 1 177 ? -41.672 -11.329 22.661  0.50  22.63 ? 175 ARG A NH1 1 
ATOM   3571 N  NH1 B ARG B 1 177 ? -42.168 -14.505 19.105  0.50  15.01 ? 175 ARG A NH1 1 
ATOM   3572 N  NH2 A ARG B 1 177 ? -41.463 -11.663 20.377  0.50  21.59 ? 175 ARG A NH2 1 
ATOM   3573 N  NH2 B ARG B 1 177 ? -40.992 -12.556 19.202  0.50  16.95 ? 175 ARG A NH2 1 
ATOM   3574 N  N   . PHE B 1 178 ? -41.536 -17.323 24.152  1.00  13.15 ? 176 PHE A N   1 
ATOM   3575 C  CA  . PHE B 1 178 ? -40.242 -17.493 24.761  1.00  12.92 ? 176 PHE A CA  1 
ATOM   3576 C  C   . PHE B 1 178 ? -39.126 -17.257 23.781  1.00  13.14 ? 176 PHE A C   1 
ATOM   3577 O  O   . PHE B 1 178 ? -38.826 -18.142 23.008  1.00  13.06 ? 176 PHE A O   1 
ATOM   3578 C  CB  . PHE B 1 178 ? -40.124 -18.930 25.296  1.00  12.63 ? 176 PHE A CB  1 
ATOM   3579 C  CG  . PHE B 1 178 ? -38.986 -19.130 26.294  1.00  12.76 ? 176 PHE A CG  1 
ATOM   3580 C  CD1 . PHE B 1 178 ? -39.126 -18.751 27.612  1.00  14.18 ? 176 PHE A CD1 1 
ATOM   3581 C  CD2 . PHE B 1 178 ? -37.756 -19.738 25.910  1.00  12.05 ? 176 PHE A CD2 1 
ATOM   3582 C  CE1 . PHE B 1 178 ? -38.122 -18.991 28.549  1.00  17.04 ? 176 PHE A CE1 1 
ATOM   3583 C  CE2 . PHE B 1 178 ? -36.750 -19.957 26.839  1.00  12.55 ? 176 PHE A CE2 1 
ATOM   3584 C  CZ  . PHE B 1 178 ? -36.919 -19.579 28.161  1.00  14.57 ? 176 PHE A CZ  1 
ATOM   3585 N  N   . THR B 1 179 ? -38.655 -16.008 23.659  1.00  14.45 ? 177 THR A N   1 
ATOM   3586 C  CA  . THR B 1 179 ? -37.558 -15.745 22.643  1.00  15.31 ? 177 THR A CA  1 
ATOM   3587 C  C   . THR B 1 179 ? -36.421 -14.997 23.250  1.00  15.69 ? 177 THR A C   1 
ATOM   3588 O  O   . THR B 1 179 ? -36.441 -14.649 24.416  1.00  18.97 ? 177 THR A O   1 
ATOM   3589 C  CB  . THR B 1 179 ? -38.013 -15.129 21.275  1.00  17.47 ? 177 THR A CB  1 
ATOM   3590 O  OG1 . THR B 1 179 ? -36.977 -15.259 20.194  1.00  17.22 ? 177 THR A OG1 1 
ATOM   3591 C  CG2 . THR B 1 179 ? -38.501 -13.724 21.503  1.00  18.53 ? 177 THR A CG2 1 
ATOM   3592 N  N   . ASN B 1 180 ? -35.382 -14.836 22.442  1.00  16.47 ? 178 ASN A N   1 
ATOM   3593 C  CA  . ASN B 1 180 ? -34.136 -14.233 22.962  1.00  18.28 ? 178 ASN A CA  1 
ATOM   3594 C  C   . ASN B 1 180 ? -33.556 -14.999 24.124  1.00  17.69 ? 178 ASN A C   1 
ATOM   3595 O  O   . ASN B 1 180 ? -33.204 -14.434 25.180  1.00  16.74 ? 178 ASN A O   1 
ATOM   3596 C  CB  . ASN B 1 180 ? -34.321 -12.712 23.207  1.00  22.33 ? 178 ASN A CB  1 
ATOM   3597 C  CG  . ASN B 1 180 ? -34.711 -11.972 21.897  1.00  27.47 ? 178 ASN A CG  1 
ATOM   3598 O  OD1 . ASN B 1 180 ? -34.047 -12.110 20.850  1.00  31.95 ? 178 ASN A OD1 1 
ATOM   3599 N  ND2 . ASN B 1 180 ? -35.830 -11.195 21.953  1.00  30.57 ? 178 ASN A ND2 1 
ATOM   3600 N  N   . PHE B 1 181 ? -33.443 -16.311 23.915  1.00  15.21 ? 179 PHE A N   1 
ATOM   3601 C  CA  . PHE B 1 181 ? -32.971 -17.215 24.955  1.00  13.65 ? 179 PHE A CA  1 
ATOM   3602 C  C   . PHE B 1 181 ? -31.480 -17.533 24.693  1.00  13.81 ? 179 PHE A C   1 
ATOM   3603 O  O   . PHE B 1 181 ? -31.136 -18.015 23.640  1.00  13.70 ? 179 PHE A O   1 
ATOM   3604 C  CB  . PHE B 1 181 ? -33.858 -18.507 24.962  1.00  16.56 ? 179 PHE A CB  1 
ATOM   3605 C  CG  . PHE B 1 181 ? -33.344 -19.656 25.786  1.00  15.68 ? 179 PHE A CG  1 
ATOM   3606 C  CD1 . PHE B 1 181 ? -32.985 -19.494 27.132  1.00  17.68 ? 179 PHE A CD1 1 
ATOM   3607 C  CD2 . PHE B 1 181 ? -33.282 -20.935 25.215  1.00  17.34 ? 179 PHE A CD2 1 
ATOM   3608 C  CE1 . PHE B 1 181 ? -32.553 -20.613 27.932  1.00  16.19 ? 179 PHE A CE1 1 
ATOM   3609 C  CE2 . PHE B 1 181 ? -32.809 -22.025 25.947  1.00  19.41 ? 179 PHE A CE2 1 
ATOM   3610 C  CZ  . PHE B 1 181 ? -32.488 -21.887 27.310  1.00  17.31 ? 179 PHE A CZ  1 
ATOM   3611 N  N   . ASP B 1 182 ? -30.653 -17.278 25.685  1.00  14.87 ? 180 ASP A N   1 
ATOM   3612 C  CA  . ASP B 1 182 ? -29.207 -17.516 25.545  1.00  15.00 ? 180 ASP A CA  1 
ATOM   3613 C  C   . ASP B 1 182 ? -28.879 -18.988 25.956  1.00  12.85 ? 180 ASP A C   1 
ATOM   3614 O  O   . ASP B 1 182 ? -28.569 -19.258 27.096  1.00  15.29 ? 180 ASP A O   1 
ATOM   3615 C  CB  . ASP B 1 182 ? -28.436 -16.563 26.436  1.00  13.71 ? 180 ASP A CB  1 
ATOM   3616 C  CG  . ASP B 1 182 ? -26.908 -16.756 26.375  1.00  16.79 ? 180 ASP A CG  1 
ATOM   3617 O  OD1 . ASP B 1 182 ? -26.382 -17.573 25.585  1.00  17.53 ? 180 ASP A OD1 1 
ATOM   3618 O  OD2 . ASP B 1 182 ? -26.266 -16.068 27.151  1.00  18.02 ? 180 ASP A OD2 1 
ATOM   3619 N  N   . LEU B 1 183 ? -29.043 -19.901 25.008  1.00  12.33 ? 181 LEU A N   1 
ATOM   3620 C  CA  . LEU B 1 183 ? -28.791 -21.310 25.315  1.00  12.13 ? 181 LEU A CA  1 
ATOM   3621 C  C   . LEU B 1 183 ? -27.302 -21.580 25.528  1.00  13.05 ? 181 LEU A C   1 
ATOM   3622 O  O   . LEU B 1 183 ? -26.865 -22.428 26.352  1.00  13.28 ? 181 LEU A O   1 
ATOM   3623 C  CB  . LEU B 1 183 ? -29.364 -22.146 24.151  1.00  12.56 ? 181 LEU A CB  1 
ATOM   3624 C  CG  . LEU B 1 183 ? -29.129 -23.679 24.295  1.00  12.27 ? 181 LEU A CG  1 
ATOM   3625 C  CD1 . LEU B 1 183 ? -29.630 -24.271 25.617  1.00  11.17 ? 181 LEU A CD1 1 
ATOM   3626 C  CD2 . LEU B 1 183 ? -29.852 -24.326 23.138  1.00  12.67 ? 181 LEU A CD2 1 
ATOM   3627 N  N   . LEU B 1 184 ? -26.467 -20.849 24.783  1.00  15.71 ? 182 LEU A N   1 
ATOM   3628 C  CA  . LEU B 1 184 ? -25.089 -21.182 24.768  1.00  16.61 ? 182 LEU A CA  1 
ATOM   3629 C  C   . LEU B 1 184 ? -24.538 -21.032 26.193  1.00  18.03 ? 182 LEU A C   1 
ATOM   3630 O  O   . LEU B 1 184 ? -23.689 -21.800 26.649  1.00  21.38 ? 182 LEU A O   1 
ATOM   3631 C  CB  . LEU B 1 184 ? -24.405 -20.257 23.763  1.00  17.38 ? 182 LEU A CB  1 
ATOM   3632 C  CG  . LEU B 1 184 ? -22.974 -20.542 23.480  1.00  22.19 ? 182 LEU A CG  1 
ATOM   3633 C  CD1 . LEU B 1 184 ? -22.969 -21.841 22.739  1.00  23.04 ? 182 LEU A CD1 1 
ATOM   3634 C  CD2 . LEU B 1 184 ? -22.491 -19.325 22.629  1.00  20.46 ? 182 LEU A CD2 1 
ATOM   3635 N  N   . SER B 1 185 ? -25.057 -20.029 26.930  1.00  17.88 ? 183 SER A N   1 
ATOM   3636 C  CA  . SER B 1 185 ? -24.574 -19.736 28.276  1.00  19.47 ? 183 SER A CA  1 
ATOM   3637 C  C   . SER B 1 185 ? -25.007 -20.758 29.305  1.00  18.50 ? 183 SER A C   1 
ATOM   3638 O  O   . SER B 1 185 ? -24.531 -20.776 30.450  1.00  18.70 ? 183 SER A O   1 
ATOM   3639 C  CB  . SER B 1 185 ? -24.923 -18.290 28.748  1.00  20.99 ? 183 SER A CB  1 
ATOM   3640 O  OG  . SER B 1 185 ? -24.269 -17.345 27.828  1.00  22.58 ? 183 SER A OG  1 
ATOM   3641 N  N   . LEU B 1 186 ? -25.938 -21.591 28.896  1.00  17.45 ? 184 LEU A N   1 
ATOM   3642 C  CA  . LEU B 1 186 ? -26.395 -22.629 29.783  1.00  16.27 ? 184 LEU A CA  1 
ATOM   3643 C  C   . LEU B 1 186 ? -25.415 -23.801 29.752  1.00  19.48 ? 184 LEU A C   1 
ATOM   3644 O  O   . LEU B 1 186 ? -25.364 -24.536 30.757  1.00  22.28 ? 184 LEU A O   1 
ATOM   3645 C  CB  . LEU B 1 186 ? -27.822 -23.122 29.382  1.00  19.78 ? 184 LEU A CB  1 
ATOM   3646 C  CG  . LEU B 1 186 ? -28.789 -23.724 30.383  1.00  18.90 ? 184 LEU A CG  1 
ATOM   3647 C  CD1 . LEU B 1 186 ? -28.767 -23.101 31.780  1.00  18.56 ? 184 LEU A CD1 1 
ATOM   3648 C  CD2 . LEU B 1 186 ? -30.212 -23.729 29.774  1.00  15.39 ? 184 LEU A CD2 1 
ATOM   3649 N  N   . LEU B 1 187 ? -24.629 -23.987 28.665  1.00  15.29 ? 185 LEU A N   1 
ATOM   3650 C  CA  . LEU B 1 187 ? -23.615 -25.030 28.595  1.00  13.96 ? 185 LEU A CA  1 
ATOM   3651 C  C   . LEU B 1 187 ? -22.410 -24.805 29.523  1.00  13.09 ? 185 LEU A C   1 
ATOM   3652 O  O   . LEU B 1 187 ? -22.027 -23.632 29.825  1.00  13.18 ? 185 LEU A O   1 
ATOM   3653 C  CB  . LEU B 1 187 ? -23.024 -25.233 27.162  1.00  13.68 ? 185 LEU A CB  1 
ATOM   3654 C  CG  . LEU B 1 187 ? -24.156 -25.312 26.116  1.00  16.85 ? 185 LEU A CG  1 
ATOM   3655 C  CD1 . LEU B 1 187 ? -23.492 -25.590 24.769  1.00  17.56 ? 185 LEU A CD1 1 
ATOM   3656 C  CD2 . LEU B 1 187 ? -25.192 -26.347 26.396  1.00  18.81 ? 185 LEU A CD2 1 
ATOM   3657 N  N   . PRO B 1 188 ? -21.752 -25.887 29.966  1.00  13.44 ? 186 PRO A N   1 
ATOM   3658 C  CA  . PRO B 1 188 ? -20.595 -25.644 30.816  1.00  12.18 ? 186 PRO A CA  1 
ATOM   3659 C  C   . PRO B 1 188 ? -19.376 -25.122 30.013  1.00  13.62 ? 186 PRO A C   1 
ATOM   3660 O  O   . PRO B 1 188 ? -19.351 -25.177 28.767  1.00  12.60 ? 186 PRO A O   1 
ATOM   3661 C  CB  . PRO B 1 188 ? -20.239 -27.091 31.336  1.00  13.62 ? 186 PRO A CB  1 
ATOM   3662 C  CG  . PRO B 1 188 ? -20.568 -27.967 30.154  1.00  12.12 ? 186 PRO A CG  1 
ATOM   3663 C  CD  . PRO B 1 188 ? -21.944 -27.376 29.803  1.00  12.51 ? 186 PRO A CD  1 
ATOM   3664 N  N   . PRO B 1 189 ? -18.330 -24.665 30.727  1.00  13.45 ? 187 PRO A N   1 
ATOM   3665 C  CA  . PRO B 1 189 ? -17.194 -24.100 29.971  1.00  13.20 ? 187 PRO A CA  1 
ATOM   3666 C  C   . PRO B 1 189 ? -16.369 -25.071 29.182  1.00  13.16 ? 187 PRO A C   1 
ATOM   3667 O  O   . PRO B 1 189 ? -16.001 -24.761 28.021  1.00  14.65 ? 187 PRO A O   1 
ATOM   3668 C  CB  . PRO B 1 189 ? -16.293 -23.503 31.083  1.00  15.24 ? 187 PRO A CB  1 
ATOM   3669 C  CG  . PRO B 1 189 ? -17.163 -23.302 32.230  1.00  15.96 ? 187 PRO A CG  1 
ATOM   3670 C  CD  . PRO B 1 189 ? -18.247 -24.342 32.175  1.00  13.23 ? 187 PRO A CD  1 
ATOM   3671 N  N   . SER B 1 190 ? -16.161 -26.299 29.702  1.00  12.48 ? 188 SER A N   1 
ATOM   3672 C  CA  . SER B 1 190 ? -15.515 -27.366 28.932  1.00  11.51 ? 188 SER A CA  1 
ATOM   3673 C  C   . SER B 1 190 ? -16.599 -28.169 28.139  1.00  11.83 ? 188 SER A C   1 
ATOM   3674 O  O   . SER B 1 190 ? -17.619 -28.558 28.756  1.00  11.35 ? 188 SER A O   1 
ATOM   3675 C  CB  . SER B 1 190 ? -14.820 -28.415 29.855  1.00  10.79 ? 188 SER A CB  1 
ATOM   3676 O  OG  . SER B 1 190 ? -14.264 -29.439 29.005  1.00  12.53 ? 188 SER A OG  1 
ATOM   3677 N  N   . TRP B 1 191 ? -16.326 -28.476 26.854  1.00  10.68 ? 189 TRP A N   1 
ATOM   3678 C  CA  . TRP B 1 191 ? -17.295 -29.236 26.040  1.00  11.50 ? 189 TRP A CA  1 
ATOM   3679 C  C   . TRP B 1 191 ? -16.800 -30.641 25.773  1.00  11.22 ? 189 TRP A C   1 
ATOM   3680 O  O   . TRP B 1 191 ? -17.306 -31.375 24.870  1.00  12.52 ? 189 TRP A O   1 
ATOM   3681 C  CB  . TRP B 1 191 ? -17.582 -28.476 24.697  1.00  11.69 ? 189 TRP A CB  1 
ATOM   3682 C  CG  . TRP B 1 191 ? -18.294 -27.223 24.899  1.00  10.47 ? 189 TRP A CG  1 
ATOM   3683 C  CD1 . TRP B 1 191 ? -18.848 -26.684 26.091  1.00  10.77 ? 189 TRP A CD1 1 
ATOM   3684 C  CD2 . TRP B 1 191 ? -18.530 -26.213 23.867  1.00  11.16 ? 189 TRP A CD2 1 
ATOM   3685 N  NE1 . TRP B 1 191 ? -19.404 -25.417 25.818  1.00  12.32 ? 189 TRP A NE1 1 
ATOM   3686 C  CE2 . TRP B 1 191 ? -19.244 -25.116 24.494  1.00  11.41 ? 189 TRP A CE2 1 
ATOM   3687 C  CE3 . TRP B 1 191 ? -18.279 -26.164 22.502  1.00  11.84 ? 189 TRP A CE3 1 
ATOM   3688 C  CZ2 . TRP B 1 191 ? -19.649 -23.971 23.772  1.00  11.61 ? 189 TRP A CZ2 1 
ATOM   3689 C  CZ3 . TRP B 1 191 ? -18.662 -25.001 21.789  1.00  10.60 ? 189 TRP A CZ3 1 
ATOM   3690 C  CH2 . TRP B 1 191 ? -19.326 -23.949 22.422  1.00  11.78 ? 189 TRP A CH2 1 
ATOM   3691 N  N   . ASP B 1 192 ? -15.862 -31.103 26.604  1.00  9.87  ? 190 ASP A N   1 
ATOM   3692 C  CA  . ASP B 1 192 ? -15.363 -32.492 26.483  1.00  11.47 ? 190 ASP A CA  1 
ATOM   3693 C  C   . ASP B 1 192 ? -16.558 -33.390 26.657  1.00  10.27 ? 190 ASP A C   1 
ATOM   3694 O  O   . ASP B 1 192 ? -17.424 -33.129 27.519  1.00  11.26 ? 190 ASP A O   1 
ATOM   3695 C  CB  . ASP B 1 192 ? -14.410 -32.834 27.630  1.00  11.95 ? 190 ASP A CB  1 
ATOM   3696 C  CG  . ASP B 1 192 ? -12.988 -32.213 27.464  1.00  15.97 ? 190 ASP A CG  1 
ATOM   3697 O  OD1 . ASP B 1 192 ? -12.652 -31.780 26.374  1.00  14.94 ? 190 ASP A OD1 1 
ATOM   3698 O  OD2 . ASP B 1 192 ? -12.221 -32.245 28.467  1.00  19.06 ? 190 ASP A OD2 1 
ATOM   3699 N  N   . TYR B 1 193 ? -16.588 -34.477 25.903  1.00  8.87  ? 191 TYR A N   1 
ATOM   3700 C  CA  . TYR B 1 193 ? -17.804 -35.316 25.907  1.00  9.66  ? 191 TYR A CA  1 
ATOM   3701 C  C   . TYR B 1 193 ? -17.537 -36.803 25.675  1.00  9.74  ? 191 TYR A C   1 
ATOM   3702 O  O   . TYR B 1 193 ? -16.465 -37.200 25.134  1.00  11.11 ? 191 TYR A O   1 
ATOM   3703 C  CB  . TYR B 1 193 ? -18.837 -34.839 24.795  1.00  9.89  ? 191 TYR A CB  1 
ATOM   3704 C  CG  . TYR B 1 193 ? -18.279 -34.960 23.410  1.00  10.31 ? 191 TYR A CG  1 
ATOM   3705 C  CD1 . TYR B 1 193 ? -18.446 -36.134 22.631  1.00  10.37 ? 191 TYR A CD1 1 
ATOM   3706 C  CD2 . TYR B 1 193 ? -17.587 -33.869 22.872  1.00  10.65 ? 191 TYR A CD2 1 
ATOM   3707 C  CE1 . TYR B 1 193 ? -17.885 -36.224 21.363  1.00  11.34 ? 191 TYR A CE1 1 
ATOM   3708 C  CE2 . TYR B 1 193 ? -17.043 -33.911 21.607  1.00  10.65 ? 191 TYR A CE2 1 
ATOM   3709 C  CZ  . TYR B 1 193 ? -17.216 -35.055 20.853  1.00  10.87 ? 191 TYR A CZ  1 
ATOM   3710 O  OH  . TYR B 1 193 ? -16.631 -35.180 19.604  1.00  12.18 ? 191 TYR A OH  1 
ATOM   3711 N  N   . TRP B 1 194 ? -18.608 -37.594 25.959  1.00  9.45  ? 192 TRP A N   1 
ATOM   3712 C  CA  . TRP B 1 194 ? -18.668 -39.001 25.481  1.00  9.94  ? 192 TRP A CA  1 
ATOM   3713 C  C   . TRP B 1 194 ? -19.710 -39.131 24.394  1.00  9.94  ? 192 TRP A C   1 
ATOM   3714 O  O   . TRP B 1 194 ? -20.731 -38.426 24.437  1.00  11.94 ? 192 TRP A O   1 
ATOM   3715 C  CB  . TRP B 1 194 ? -19.023 -39.948 26.577  1.00  11.88 ? 192 TRP A CB  1 
ATOM   3716 C  CG  . TRP B 1 194 ? -18.089 -39.953 27.790  1.00  10.48 ? 192 TRP A CG  1 
ATOM   3717 C  CD1 . TRP B 1 194 ? -16.809 -40.522 27.872  1.00  13.01 ? 192 TRP A CD1 1 
ATOM   3718 C  CD2 . TRP B 1 194 ? -18.264 -39.244 29.021  1.00  10.87 ? 192 TRP A CD2 1 
ATOM   3719 N  NE1 . TRP B 1 194 ? -16.238 -40.252 29.076  1.00  12.63 ? 192 TRP A NE1 1 
ATOM   3720 C  CE2 . TRP B 1 194 ? -17.062 -39.521 29.827  1.00  11.26 ? 192 TRP A CE2 1 
ATOM   3721 C  CE3 . TRP B 1 194 ? -19.320 -38.505 29.582  1.00  10.18 ? 192 TRP A CE3 1 
ATOM   3722 C  CZ2 . TRP B 1 194 ? -16.893 -39.021 31.155  1.00  12.56 ? 192 TRP A CZ2 1 
ATOM   3723 C  CZ3 . TRP B 1 194 ? -19.157 -38.034 30.933  1.00  13.44 ? 192 TRP A CZ3 1 
ATOM   3724 C  CH2 . TRP B 1 194 ? -17.962 -38.306 31.697  1.00  13.56 ? 192 TRP A CH2 1 
ATOM   3725 N  N   . THR B 1 195 ? -19.555 -40.116 23.486  1.00  10.32 ? 193 THR A N   1 
ATOM   3726 C  CA  . THR B 1 195 ? -20.543 -40.230 22.377  1.00  9.97  ? 193 THR A CA  1 
ATOM   3727 C  C   . THR B 1 195 ? -20.791 -41.707 22.111  1.00  10.92 ? 193 THR A C   1 
ATOM   3728 O  O   . THR B 1 195 ? -19.838 -42.542 22.243  1.00  10.97 ? 193 THR A O   1 
ATOM   3729 C  CB  . THR B 1 195 ? -20.101 -39.420 21.109  1.00  11.31 ? 193 THR A CB  1 
ATOM   3730 O  OG1 . THR B 1 195 ? -21.134 -39.571 20.087  1.00  9.93  ? 193 THR A OG1 1 
ATOM   3731 C  CG2 . THR B 1 195 ? -18.732 -39.896 20.494  1.00  11.31 ? 193 THR A CG2 1 
ATOM   3732 N  N   . TYR B 1 196 ? -22.045 -42.035 21.729  1.00  10.45 ? 194 TYR A N   1 
ATOM   3733 C  CA  . TYR B 1 196 ? -22.431 -43.442 21.487  1.00  9.95  ? 194 TYR A CA  1 
ATOM   3734 C  C   . TYR B 1 196 ? -23.742 -43.369 20.723  1.00  9.96  ? 194 TYR A C   1 
ATOM   3735 O  O   . TYR B 1 196 ? -24.477 -42.347 20.798  1.00  10.70 ? 194 TYR A O   1 
ATOM   3736 C  CB  . TYR B 1 196 ? -22.554 -44.214 22.813  1.00  10.14 ? 194 TYR A CB  1 
ATOM   3737 C  CG  . TYR B 1 196 ? -23.799 -43.900 23.638  1.00  8.70  ? 194 TYR A CG  1 
ATOM   3738 C  CD1 . TYR B 1 196 ? -23.837 -42.773 24.539  1.00  8.87  ? 194 TYR A CD1 1 
ATOM   3739 C  CD2 . TYR B 1 196 ? -25.009 -44.662 23.462  1.00  9.53  ? 194 TYR A CD2 1 
ATOM   3740 C  CE1 . TYR B 1 196 ? -25.015 -42.466 25.229  1.00  7.48  ? 194 TYR A CE1 1 
ATOM   3741 C  CE2 . TYR B 1 196 ? -26.191 -44.383 24.205  1.00  9.26  ? 194 TYR A CE2 1 
ATOM   3742 C  CZ  . TYR B 1 196 ? -26.182 -43.235 25.057  1.00  8.38  ? 194 TYR A CZ  1 
ATOM   3743 O  OH  . TYR B 1 196 ? -27.342 -42.936 25.739  1.00  8.21  ? 194 TYR A OH  1 
ATOM   3744 N  N   . PRO B 1 197 ? -24.108 -44.429 19.998  1.00  11.25 ? 195 PRO A N   1 
ATOM   3745 C  CA  . PRO B 1 197 ? -25.399 -44.538 19.250  1.00  9.55  ? 195 PRO A CA  1 
ATOM   3746 C  C   . PRO B 1 197 ? -26.488 -45.016 20.188  1.00  9.72  ? 195 PRO A C   1 
ATOM   3747 O  O   . PRO B 1 197 ? -26.334 -46.045 20.875  1.00  11.10 ? 195 PRO A O   1 
ATOM   3748 C  CB  . PRO B 1 197 ? -25.071 -45.568 18.130  1.00  10.68 ? 195 PRO A CB  1 
ATOM   3749 C  CG  . PRO B 1 197 ? -23.991 -46.478 18.776  1.00  12.05 ? 195 PRO A CG  1 
ATOM   3750 C  CD  . PRO B 1 197 ? -23.198 -45.592 19.748  1.00  11.01 ? 195 PRO A CD  1 
ATOM   3751 N  N   . GLY B 1 198 ? -27.586 -44.220 20.307  1.00  9.53  ? 196 GLY A N   1 
ATOM   3752 C  CA  . GLY B 1 198 ? -28.667 -44.641 21.118  1.00  7.70  ? 196 GLY A CA  1 
ATOM   3753 C  C   . GLY B 1 198 ? -30.026 -44.172 20.608  1.00  8.84  ? 196 GLY A C   1 
ATOM   3754 O  O   . GLY B 1 198 ? -30.308 -44.212 19.408  1.00  9.10  ? 196 GLY A O   1 
ATOM   3755 N  N   . SER B 1 199 ? -30.872 -43.887 21.583  1.00  8.14  ? 197 SER A N   1 
ATOM   3756 C  CA  . SER B 1 199 ? -32.346 -43.685 21.296  1.00  9.04  ? 197 SER A CA  1 
ATOM   3757 C  C   . SER B 1 199 ? -32.940 -42.463 21.960  1.00  8.88  ? 197 SER A C   1 
ATOM   3758 O  O   . SER B 1 199 ? -32.289 -41.818 22.785  1.00  8.66  ? 197 SER A O   1 
ATOM   3759 C  CB  . SER B 1 199 ? -33.172 -44.930 21.763  1.00  8.89  ? 197 SER A CB  1 
ATOM   3760 O  OG  . SER B 1 199 ? -33.208 -44.900 23.163  1.00  8.07  ? 197 SER A OG  1 
ATOM   3761 N  N   . LEU B 1 200 ? -34.205 -42.138 21.602  1.00  8.80  ? 198 LEU A N   1 
ATOM   3762 C  CA  . LEU B 1 200 ? -35.006 -41.205 22.412  1.00  9.27  ? 198 LEU A CA  1 
ATOM   3763 C  C   . LEU B 1 200 ? -35.108 -41.945 23.771  1.00  9.70  ? 198 LEU A C   1 
ATOM   3764 O  O   . LEU B 1 200 ? -35.229 -43.150 23.852  1.00  9.56  ? 198 LEU A O   1 
ATOM   3765 C  CB  . LEU B 1 200 ? -36.468 -41.075 21.955  1.00  10.31 ? 198 LEU A CB  1 
ATOM   3766 C  CG  . LEU B 1 200 ? -36.777 -40.618 20.527  1.00  13.70 ? 198 LEU A CG  1 
ATOM   3767 C  CD1 . LEU B 1 200 ? -38.212 -40.271 20.162  1.00  14.16 ? 198 LEU A CD1 1 
ATOM   3768 C  CD2 . LEU B 1 200 ? -35.741 -39.838 19.734  1.00  14.09 ? 198 LEU A CD2 1 
ATOM   3769 N  N   . THR B 1 201 ? -35.163 -41.169 24.854  1.00  7.97  ? 199 THR A N   1 
ATOM   3770 C  CA  . THR B 1 201 ? -35.352 -41.746 26.214  1.00  7.55  ? 199 THR A CA  1 
ATOM   3771 C  C   . THR B 1 201 ? -36.823 -41.685 26.660  1.00  8.16  ? 199 THR A C   1 
ATOM   3772 O  O   . THR B 1 201 ? -37.093 -41.997 27.845  1.00  8.79  ? 199 THR A O   1 
ATOM   3773 C  CB  . THR B 1 201 ? -34.463 -41.015 27.287  1.00  7.03  ? 199 THR A CB  1 
ATOM   3774 O  OG1 . THR B 1 201 ? -34.908 -39.674 27.508  1.00  8.54  ? 199 THR A OG1 1 
ATOM   3775 C  CG2 . THR B 1 201 ? -32.979 -41.020 26.795  1.00  7.61  ? 199 THR A CG2 1 
ATOM   3776 N  N   . VAL B 1 202 ? -37.716 -41.316 25.719  1.00  7.65  ? 200 VAL A N   1 
ATOM   3777 C  CA  . VAL B 1 202 ? -39.161 -41.355 25.928  1.00  9.61  ? 200 VAL A CA  1 
ATOM   3778 C  C   . VAL B 1 202 ? -39.763 -42.146 24.792  1.00  9.64  ? 200 VAL A C   1 
ATOM   3779 O  O   . VAL B 1 202 ? -39.197 -42.122 23.724  1.00  10.47 ? 200 VAL A O   1 
ATOM   3780 C  CB  . VAL B 1 202 ? -39.764 -39.949 26.032  1.00  9.51  ? 200 VAL A CB  1 
ATOM   3781 C  CG1 . VAL B 1 202 ? -39.205 -39.281 27.307  1.00  12.13 ? 200 VAL A CG1 1 
ATOM   3782 C  CG2 . VAL B 1 202 ? -39.537 -39.041 24.819  1.00  9.51  ? 200 VAL A CG2 1 
ATOM   3783 N  N   . PRO B 1 203 ? -40.960 -42.711 24.993  1.00  9.35  ? 201 PRO A N   1 
ATOM   3784 C  CA  . PRO B 1 203 ? -41.748 -43.235 23.860  1.00  10.28 ? 201 PRO A CA  1 
ATOM   3785 C  C   . PRO B 1 203 ? -41.834 -42.176 22.787  1.00  9.82  ? 201 PRO A C   1 
ATOM   3786 O  O   . PRO B 1 203 ? -42.125 -41.013 23.054  1.00  9.88  ? 201 PRO A O   1 
ATOM   3787 C  CB  . PRO B 1 203 ? -43.119 -43.524 24.525  1.00  9.40  ? 201 PRO A CB  1 
ATOM   3788 C  CG  . PRO B 1 203 ? -42.721 -43.978 25.903  1.00  10.12 ? 201 PRO A CG  1 
ATOM   3789 C  CD  . PRO B 1 203 ? -41.712 -42.834 26.267  1.00  9.89  ? 201 PRO A CD  1 
ATOM   3790 N  N   . PRO B 1 204 ? -41.596 -42.569 21.526  1.00  10.38 ? 202 PRO A N   1 
ATOM   3791 C  CA  . PRO B 1 204 ? -41.518 -43.930 21.036  1.00  11.23 ? 202 PRO A CA  1 
ATOM   3792 C  C   . PRO B 1 204 ? -40.118 -44.628 21.049  1.00  11.12 ? 202 PRO A C   1 
ATOM   3793 O  O   . PRO B 1 204 ? -39.968 -45.747 20.455  1.00  11.94 ? 202 PRO A O   1 
ATOM   3794 C  CB  . PRO B 1 204 ? -42.042 -43.758 19.593  1.00  11.28 ? 202 PRO A CB  1 
ATOM   3795 C  CG  . PRO B 1 204 ? -41.534 -42.392 19.172  1.00  13.09 ? 202 PRO A CG  1 
ATOM   3796 C  CD  . PRO B 1 204 ? -41.718 -41.550 20.458  1.00  11.37 ? 202 PRO A CD  1 
ATOM   3797 N  N   . LEU B 1 205 ? -39.128 -43.995 21.713  1.00  10.10 ? 203 LEU A N   1 
ATOM   3798 C  CA  . LEU B 1 205 ? -37.878 -44.736 22.013  1.00  9.97  ? 203 LEU A CA  1 
ATOM   3799 C  C   . LEU B 1 205 ? -37.095 -45.120 20.759  1.00  9.78  ? 203 LEU A C   1 
ATOM   3800 O  O   . LEU B 1 205 ? -36.313 -46.062 20.764  1.00  8.88  ? 203 LEU A O   1 
ATOM   3801 C  CB  . LEU B 1 205 ? -38.111 -45.959 22.926  1.00  9.29  ? 203 LEU A CB  1 
ATOM   3802 C  CG  . LEU B 1 205 ? -38.808 -45.713 24.264  1.00  9.72  ? 203 LEU A CG  1 
ATOM   3803 C  CD1 . LEU B 1 205 ? -39.167 -47.069 24.962  1.00  9.69  ? 203 LEU A CD1 1 
ATOM   3804 C  CD2 . LEU B 1 205 ? -37.856 -44.949 25.205  1.00  9.84  ? 203 LEU A CD2 1 
ATOM   3805 N  N   . LEU B 1 206 ? -37.271 -44.297 19.682  1.00  9.15  ? 204 LEU A N   1 
ATOM   3806 C  CA  . LEU B 1 206 ? -36.675 -44.607 18.359  1.00  9.30  ? 204 LEU A CA  1 
ATOM   3807 C  C   . LEU B 1 206 ? -35.123 -44.596 18.386  1.00  9.34  ? 204 LEU A C   1 
ATOM   3808 O  O   . LEU B 1 206 ? -34.532 -43.696 19.025  1.00  10.17 ? 204 LEU A O   1 
ATOM   3809 C  CB  . LEU B 1 206 ? -37.156 -43.569 17.341  1.00  9.74  ? 204 LEU A CB  1 
ATOM   3810 C  CG  . LEU B 1 206 ? -38.674 -43.591 17.061  1.00  9.88  ? 204 LEU A CG  1 
ATOM   3811 C  CD1 . LEU B 1 206 ? -39.141 -42.343 16.302  1.00  11.27 ? 204 LEU A CD1 1 
ATOM   3812 C  CD2 . LEU B 1 206 ? -38.989 -44.875 16.272  1.00  13.18 ? 204 LEU A CD2 1 
ATOM   3813 N  N   . GLU B 1 207 ? -34.470 -45.570 17.736  1.00  9.10  ? 205 GLU A N   1 
ATOM   3814 C  CA  . GLU B 1 207 ? -32.978 -45.645 17.770  1.00  8.98  ? 205 GLU A CA  1 
ATOM   3815 C  C   . GLU B 1 207 ? -32.350 -44.825 16.683  1.00  10.12 ? 205 GLU A C   1 
ATOM   3816 O  O   . GLU B 1 207 ? -31.880 -45.351 15.628  1.00  11.31 ? 205 GLU A O   1 
ATOM   3817 C  CB  . GLU B 1 207 ? -32.532 -47.149 17.808  1.00  9.79  ? 205 GLU A CB  1 
ATOM   3818 C  CG  . GLU B 1 207 ? -33.165 -47.870 18.984  1.00  10.11 ? 205 GLU A CG  1 
ATOM   3819 C  CD  . GLU B 1 207 ? -32.867 -49.326 19.126  1.00  13.36 ? 205 GLU A CD  1 
ATOM   3820 O  OE1 . GLU B 1 207 ? -32.792 -49.989 18.059  1.00  14.46 ? 205 GLU A OE1 1 
ATOM   3821 O  OE2 . GLU B 1 207 ? -32.825 -49.843 20.269  1.00  12.58 ? 205 GLU A OE2 1 
ATOM   3822 N  N   . SER B 1 208 ? -32.489 -43.516 16.837  1.00  9.72  ? 206 SER A N   1 
ATOM   3823 C  CA  . SER B 1 208 ? -32.090 -42.585 15.826  1.00  10.13 ? 206 SER A CA  1 
ATOM   3824 C  C   . SER B 1 208 ? -31.168 -41.504 16.390  1.00  10.98 ? 206 SER A C   1 
ATOM   3825 O  O   . SER B 1 208 ? -30.873 -40.507 15.700  1.00  10.28 ? 206 SER A O   1 
ATOM   3826 C  CB  . SER B 1 208 ? -33.426 -41.953 15.327  1.00  11.58 ? 206 SER A CB  1 
ATOM   3827 O  OG  . SER B 1 208 ? -34.114 -41.314 16.382  1.00  11.44 ? 206 SER A OG  1 
ATOM   3828 N  N   . VAL B 1 209 ? -30.629 -41.703 17.611  1.00  10.64 ? 207 VAL A N   1 
ATOM   3829 C  CA  . VAL B 1 209 ? -29.873 -40.538 18.225  1.00  8.89  ? 207 VAL A CA  1 
ATOM   3830 C  C   . VAL B 1 209 ? -28.368 -40.831 18.318  1.00  9.21  ? 207 VAL A C   1 
ATOM   3831 O  O   . VAL B 1 209 ? -27.954 -41.903 18.876  1.00  9.19  ? 207 VAL A O   1 
ATOM   3832 C  CB  . VAL B 1 209 ? -30.397 -40.284 19.675  1.00  10.58 ? 207 VAL A CB  1 
ATOM   3833 C  CG1 . VAL B 1 209 ? -29.667 -39.126 20.390  1.00  10.06 ? 207 VAL A CG1 1 
ATOM   3834 C  CG2 . VAL B 1 209 ? -31.888 -39.910 19.602  1.00  8.56  ? 207 VAL A CG2 1 
ATOM   3835 N  N   . THR B 1 210 ? -27.576 -39.855 17.856  1.00  8.04  ? 208 THR A N   1 
ATOM   3836 C  CA  . THR B 1 210 ? -26.127 -39.808 18.247  1.00  7.97  ? 208 THR A CA  1 
ATOM   3837 C  C   . THR B 1 210 ? -26.050 -38.947 19.495  1.00  8.16  ? 208 THR A C   1 
ATOM   3838 O  O   . THR B 1 210 ? -26.242 -37.722 19.462  1.00  8.64  ? 208 THR A O   1 
ATOM   3839 C  CB  . THR B 1 210 ? -25.322 -39.145 17.105  1.00  8.07  ? 208 THR A CB  1 
ATOM   3840 O  OG1 . THR B 1 210 ? -25.458 -40.008 15.951  1.00  9.68  ? 208 THR A OG1 1 
ATOM   3841 C  CG2 . THR B 1 210 ? -23.798 -39.081 17.469  1.00  8.10  ? 208 THR A CG2 1 
ATOM   3842 N  N   . TRP B 1 211 ? -25.781 -39.658 20.588  1.00  8.11  ? 209 TRP A N   1 
ATOM   3843 C  CA  . TRP B 1 211 ? -25.619 -38.985 21.921  1.00  7.52  ? 209 TRP A CA  1 
ATOM   3844 C  C   . TRP B 1 211 ? -24.298 -38.323 22.114  1.00  7.29  ? 209 TRP A C   1 
ATOM   3845 O  O   . TRP B 1 211 ? -23.253 -38.880 21.769  1.00  8.50  ? 209 TRP A O   1 
ATOM   3846 C  CB  . TRP B 1 211 ? -25.869 -40.043 23.022  1.00  6.75  ? 209 TRP A CB  1 
ATOM   3847 C  CG  . TRP B 1 211 ? -27.353 -40.187 23.245  1.00  7.22  ? 209 TRP A CG  1 
ATOM   3848 C  CD1 . TRP B 1 211 ? -28.206 -41.157 22.771  1.00  7.01  ? 209 TRP A CD1 1 
ATOM   3849 C  CD2 . TRP B 1 211 ? -28.178 -39.267 24.038  1.00  7.88  ? 209 TRP A CD2 1 
ATOM   3850 N  NE1 . TRP B 1 211 ? -29.527 -40.875 23.157  1.00  7.62  ? 209 TRP A NE1 1 
ATOM   3851 C  CE2 . TRP B 1 211 ? -29.545 -39.723 23.929  1.00  7.45  ? 209 TRP A CE2 1 
ATOM   3852 C  CE3 . TRP B 1 211 ? -27.896 -38.086 24.762  1.00  7.57  ? 209 TRP A CE3 1 
ATOM   3853 C  CZ2 . TRP B 1 211 ? -30.597 -39.036 24.479  1.00  7.73  ? 209 TRP A CZ2 1 
ATOM   3854 C  CZ3 . TRP B 1 211 ? -28.950 -37.414 25.368  1.00  7.72  ? 209 TRP A CZ3 1 
ATOM   3855 C  CH2 . TRP B 1 211 ? -30.286 -37.847 25.220  1.00  6.78  ? 209 TRP A CH2 1 
ATOM   3856 N  N   . ILE B 1 212 ? -24.304 -37.087 22.607  1.00  7.55  ? 210 ILE A N   1 
ATOM   3857 C  CA  . ILE B 1 212 ? -23.079 -36.361 22.922  1.00  7.89  ? 210 ILE A CA  1 
ATOM   3858 C  C   . ILE B 1 212 ? -23.252 -35.855 24.344  1.00  8.38  ? 210 ILE A C   1 
ATOM   3859 O  O   . ILE B 1 212 ? -23.998 -34.895 24.610  1.00  9.37  ? 210 ILE A O   1 
ATOM   3860 C  CB  . ILE B 1 212 ? -22.917 -35.140 21.947  1.00  9.04  ? 210 ILE A CB  1 
ATOM   3861 C  CG1 . ILE B 1 212 ? -22.750 -35.737 20.531  1.00  8.91  ? 210 ILE A CG1 1 
ATOM   3862 C  CG2 . ILE B 1 212 ? -21.711 -34.245 22.353  1.00  11.02 ? 210 ILE A CG2 1 
ATOM   3863 C  CD1 . ILE B 1 212 ? -22.785 -34.666 19.423  1.00  9.02  ? 210 ILE A CD1 1 
ATOM   3864 N  N   . VAL B 1 213 ? -22.693 -36.579 25.320  1.00  8.44  ? 211 VAL A N   1 
ATOM   3865 C  CA  . VAL B 1 213 ? -22.973 -36.325 26.714  1.00  8.53  ? 211 VAL A CA  1 
ATOM   3866 C  C   . VAL B 1 213 ? -21.768 -35.569 27.261  1.00  9.04  ? 211 VAL A C   1 
ATOM   3867 O  O   . VAL B 1 213 ? -20.661 -36.131 27.287  1.00  8.77  ? 211 VAL A O   1 
ATOM   3868 C  CB  . VAL B 1 213 ? -23.168 -37.650 27.489  1.00  8.94  ? 211 VAL A CB  1 
ATOM   3869 C  CG1 . VAL B 1 213 ? -23.447 -37.381 28.956  1.00  10.21 ? 211 VAL A CG1 1 
ATOM   3870 C  CG2 . VAL B 1 213 ? -24.415 -38.405 26.889  1.00  8.90  ? 211 VAL A CG2 1 
ATOM   3871 N  N   . LEU B 1 214 ? -21.984 -34.339 27.766  1.00  8.90  ? 212 LEU A N   1 
ATOM   3872 C  CA  . LEU B 1 214 ? -20.820 -33.542 28.232  1.00  10.04 ? 212 LEU A CA  1 
ATOM   3873 C  C   . LEU B 1 214 ? -20.385 -34.044 29.602  1.00  9.08  ? 212 LEU A C   1 
ATOM   3874 O  O   . LEU B 1 214 ? -21.182 -34.350 30.463  1.00  9.60  ? 212 LEU A O   1 
ATOM   3875 C  CB  . LEU B 1 214 ? -21.139 -32.069 28.385  1.00  10.36 ? 212 LEU A CB  1 
ATOM   3876 C  CG  . LEU B 1 214 ? -21.573 -31.321 27.100  1.00  15.56 ? 212 LEU A CG  1 
ATOM   3877 C  CD1 . LEU B 1 214 ? -21.388 -29.763 27.113  1.00  13.37 ? 212 LEU A CD1 1 
ATOM   3878 C  CD2 . LEU B 1 214 ? -21.339 -32.009 25.770  1.00  16.97 ? 212 LEU A CD2 1 
ATOM   3879 N  N   . LYS B 1 215 ? -19.071 -34.085 29.804  1.00  9.16  ? 213 LYS A N   1 
ATOM   3880 C  CA  . LYS B 1 215 ? -18.489 -34.493 31.097  1.00  9.95  ? 213 LYS A CA  1 
ATOM   3881 C  C   . LYS B 1 215 ? -18.726 -33.503 32.240  1.00  10.84 ? 213 LYS A C   1 
ATOM   3882 O  O   . LYS B 1 215 ? -19.040 -33.916 33.394  1.00  10.85 ? 213 LYS A O   1 
ATOM   3883 C  CB  . LYS B 1 215 ? -16.939 -34.692 30.883  1.00  11.02 ? 213 LYS A CB  1 
ATOM   3884 C  CG  . LYS B 1 215 ? -16.226 -35.058 32.257  1.00  14.10 ? 213 LYS A CG  1 
ATOM   3885 C  CD  . LYS B 1 215 ? -14.774 -35.423 31.986  1.00  17.97 ? 213 LYS A CD  1 
ATOM   3886 C  CE  . LYS B 1 215 ? -13.970 -35.517 33.284  1.00  24.02 ? 213 LYS A CE  1 
ATOM   3887 N  NZ  . LYS B 1 215 ? -12.704 -36.254 32.904  1.00  27.11 ? 213 LYS A NZ  1 
ATOM   3888 N  N   . GLN B 1 216 ? -18.600 -32.188 31.948  1.00  10.08 ? 214 GLN A N   1 
ATOM   3889 C  CA  . GLN B 1 216 ? -18.658 -31.194 33.039  1.00  10.35 ? 214 GLN A CA  1 
ATOM   3890 C  C   . GLN B 1 216 ? -20.096 -30.782 33.343  1.00  10.11 ? 214 GLN A C   1 
ATOM   3891 O  O   . GLN B 1 216 ? -20.770 -30.295 32.441  1.00  10.10 ? 214 GLN A O   1 
ATOM   3892 C  CB  . GLN B 1 216 ? -17.849 -29.921 32.627  1.00  10.80 ? 214 GLN A CB  1 
ATOM   3893 C  CG  . GLN B 1 216 ? -18.002 -28.795 33.728  1.00  13.39 ? 214 GLN A CG  1 
ATOM   3894 C  CD  . GLN B 1 216 ? -17.062 -27.609 33.651  1.00  16.85 ? 214 GLN A CD  1 
ATOM   3895 O  OE1 . GLN B 1 216 ? -16.838 -26.928 34.695  1.00  22.00 ? 214 GLN A OE1 1 
ATOM   3896 N  NE2 . GLN B 1 216 ? -16.450 -27.384 32.524  1.00  11.97 ? 214 GLN A NE2 1 
ATOM   3897 N  N   . PRO B 1 217 ? -20.568 -30.930 34.566  1.00  10.67 ? 215 PRO A N   1 
ATOM   3898 C  CA  . PRO B 1 217 ? -21.916 -30.509 34.955  1.00  10.44 ? 215 PRO A CA  1 
ATOM   3899 C  C   . PRO B 1 217 ? -22.065 -28.999 35.093  1.00  10.75 ? 215 PRO A C   1 
ATOM   3900 O  O   . PRO B 1 217 ? -21.005 -28.253 35.256  1.00  12.81 ? 215 PRO A O   1 
ATOM   3901 C  CB  . PRO B 1 217 ? -22.144 -31.172 36.372  1.00  11.97 ? 215 PRO A CB  1 
ATOM   3902 C  CG  . PRO B 1 217 ? -20.776 -31.611 36.789  1.00  14.44 ? 215 PRO A CG  1 
ATOM   3903 C  CD  . PRO B 1 217 ? -19.788 -31.550 35.667  1.00  12.03 ? 215 PRO A CD  1 
ATOM   3904 N  N   . ILE B 1 218 ? -23.288 -28.491 35.003  1.00  11.13 ? 216 ILE A N   1 
ATOM   3905 C  CA  . ILE B 1 218 ? -23.562 -27.107 35.428  1.00  11.93 ? 216 ILE A CA  1 
ATOM   3906 C  C   . ILE B 1 218 ? -24.284 -27.137 36.751  1.00  11.97 ? 216 ILE A C   1 
ATOM   3907 O  O   . ILE B 1 218 ? -24.668 -28.189 37.245  1.00  11.14 ? 216 ILE A O   1 
ATOM   3908 C  CB  . ILE B 1 218 ? -24.405 -26.320 34.351  1.00  11.01 ? 216 ILE A CB  1 
ATOM   3909 C  CG1 . ILE B 1 218 ? -25.788 -26.977 34.195  1.00  10.59 ? 216 ILE A CG1 1 
ATOM   3910 C  CG2 . ILE B 1 218 ? -23.648 -26.310 33.013  1.00  10.40 ? 216 ILE A CG2 1 
ATOM   3911 C  CD1 . ILE B 1 218 ? -26.738 -26.222 33.250  1.00  10.93 ? 216 ILE A CD1 1 
ATOM   3912 N  N   A ASN B 1 219 ? -24.452 -25.975 37.392  0.50  10.40 ? 217 ASN A N   1 
ATOM   3913 N  N   B ASN B 1 219 ? -24.498 -25.980 37.363  0.50  10.57 ? 217 ASN A N   1 
ATOM   3914 C  CA  A ASN B 1 219 ? -25.068 -25.955 38.720  0.50  11.45 ? 217 ASN A CA  1 
ATOM   3915 C  CA  B ASN B 1 219 ? -25.119 -26.012 38.667  0.50  11.79 ? 217 ASN A CA  1 
ATOM   3916 C  C   A ASN B 1 219 ? -26.569 -25.691 38.642  0.50  11.13 ? 217 ASN A C   1 
ATOM   3917 C  C   B ASN B 1 219 ? -26.586 -25.670 38.642  0.50  11.37 ? 217 ASN A C   1 
ATOM   3918 O  O   A ASN B 1 219 ? -27.056 -25.104 37.665  0.50  11.63 ? 217 ASN A O   1 
ATOM   3919 O  O   B ASN B 1 219 ? -27.069 -25.039 37.695  0.50  12.00 ? 217 ASN A O   1 
ATOM   3920 C  CB  A ASN B 1 219 ? -24.490 -24.841 39.605  0.50  12.38 ? 217 ASN A CB  1 
ATOM   3921 C  CB  B ASN B 1 219 ? -24.410 -25.063 39.603  0.50  13.02 ? 217 ASN A CB  1 
ATOM   3922 C  CG  A ASN B 1 219 ? -23.049 -25.094 40.027  0.50  14.11 ? 217 ASN A CG  1 
ATOM   3923 C  CG  B ASN B 1 219 ? -23.016 -25.523 39.872  0.50  15.01 ? 217 ASN A CG  1 
ATOM   3924 O  OD1 A ASN B 1 219 ? -22.302 -24.116 40.294  0.50  18.53 ? 217 ASN A OD1 1 
ATOM   3925 O  OD1 B ASN B 1 219 ? -22.795 -26.251 40.803  0.50  17.52 ? 217 ASN A OD1 1 
ATOM   3926 N  ND2 A ASN B 1 219 ? -22.609 -26.376 40.003  0.50  13.37 ? 217 ASN A ND2 1 
ATOM   3927 N  ND2 B ASN B 1 219 ? -22.086 -25.200 38.962  0.50  15.70 ? 217 ASN A ND2 1 
ATOM   3928 N  N   . ILE B 1 220 ? -27.286 -26.117 39.677  1.00  11.18 ? 218 ILE A N   1 
ATOM   3929 C  CA  . ILE B 1 220 ? -28.650 -25.690 39.893  1.00  11.25 ? 218 ILE A CA  1 
ATOM   3930 C  C   . ILE B 1 220 ? -28.801 -25.701 41.413  1.00  11.59 ? 218 ILE A C   1 
ATOM   3931 O  O   . ILE B 1 220 ? -28.296 -26.604 42.066  1.00  9.69  ? 218 ILE A O   1 
ATOM   3932 C  CB  . ILE B 1 220 ? -29.666 -26.613 39.147  1.00  10.52 ? 218 ILE A CB  1 
ATOM   3933 C  CG1 . ILE B 1 220 ? -31.079 -26.067 39.336  1.00  11.77 ? 218 ILE A CG1 1 
ATOM   3934 C  CG2 . ILE B 1 220 ? -29.652 -28.044 39.763  1.00  10.35 ? 218 ILE A CG2 1 
ATOM   3935 C  CD1 . ILE B 1 220 ? -32.175 -26.751 38.395  1.00  11.97 ? 218 ILE A CD1 1 
ATOM   3936 N  N   . SER B 1 221 ? -29.558 -24.748 41.977  1.00  12.72 ? 219 SER A N   1 
ATOM   3937 C  CA  . SER B 1 221 ? -29.851 -24.889 43.430  1.00  12.18 ? 219 SER A CA  1 
ATOM   3938 C  C   . SER B 1 221 ? -31.052 -25.798 43.747  1.00  11.43 ? 219 SER A C   1 
ATOM   3939 O  O   . SER B 1 221 ? -31.883 -26.103 42.864  1.00  11.19 ? 219 SER A O   1 
ATOM   3940 C  CB  . SER B 1 221 ? -30.110 -23.502 44.084  1.00  11.55 ? 219 SER A CB  1 
ATOM   3941 O  OG  . SER B 1 221 ? -31.410 -23.007 43.696  1.00  11.50 ? 219 SER A OG  1 
ATOM   3942 N  N   A SER B 1 222 ? -31.150 -26.266 44.990  0.50  12.23 ? 220 SER A N   1 
ATOM   3943 N  N   B SER B 1 222 ? -31.154 -26.245 44.991  0.50  11.93 ? 220 SER A N   1 
ATOM   3944 C  CA  A SER B 1 222 ? -32.311 -27.079 45.366  0.50  11.64 ? 220 SER A CA  1 
ATOM   3945 C  CA  B SER B 1 222 ? -32.306 -27.041 45.408  0.50  11.22 ? 220 SER A CA  1 
ATOM   3946 C  C   A SER B 1 222 ? -33.616 -26.280 45.180  0.50  11.42 ? 220 SER A C   1 
ATOM   3947 C  C   B SER B 1 222 ? -33.612 -26.277 45.195  0.50  11.17 ? 220 SER A C   1 
ATOM   3948 O  O   A SER B 1 222 ? -34.625 -26.833 44.709  0.50  11.50 ? 220 SER A O   1 
ATOM   3949 O  O   B SER B 1 222 ? -34.611 -26.844 44.718  0.50  11.32 ? 220 SER A O   1 
ATOM   3950 C  CB  A SER B 1 222 ? -32.196 -27.616 46.808  0.50  12.66 ? 220 SER A CB  1 
ATOM   3951 C  CB  B SER B 1 222 ? -32.134 -27.446 46.876  0.50  11.67 ? 220 SER A CB  1 
ATOM   3952 O  OG  A SER B 1 222 ? -33.453 -28.164 47.162  0.50  13.00 ? 220 SER A OG  1 
ATOM   3953 O  OG  B SER B 1 222 ? -31.155 -28.448 46.918  0.50  11.24 ? 220 SER A OG  1 
ATOM   3954 N  N   . GLN B 1 223 ? -33.599 -24.977 45.534  1.00  11.41 ? 221 GLN A N   1 
ATOM   3955 C  CA  . GLN B 1 223 ? -34.785 -24.133 45.370  1.00  11.82 ? 221 GLN A CA  1 
ATOM   3956 C  C   . GLN B 1 223 ? -35.211 -24.053 43.909  1.00  11.44 ? 221 GLN A C   1 
ATOM   3957 O  O   . GLN B 1 223 ? -36.426 -24.081 43.624  1.00  13.60 ? 221 GLN A O   1 
ATOM   3958 C  CB  . GLN B 1 223 ? -34.565 -22.720 45.933  1.00  11.67 ? 221 GLN A CB  1 
ATOM   3959 C  CG  . GLN B 1 223 ? -34.681 -22.721 47.446  1.00  13.68 ? 221 GLN A CG  1 
ATOM   3960 C  CD  . GLN B 1 223 ? -34.762 -21.316 48.057  1.00  16.32 ? 221 GLN A CD  1 
ATOM   3961 O  OE1 . GLN B 1 223 ? -35.593 -20.503 47.700  1.00  17.73 ? 221 GLN A OE1 1 
ATOM   3962 N  NE2 . GLN B 1 223 ? -33.911 -21.068 49.004  1.00  18.84 ? 221 GLN A NE2 1 
ATOM   3963 N  N   . GLN B 1 224 ? -34.236 -23.887 43.004  1.00  11.05 ? 222 GLN A N   1 
ATOM   3964 C  CA  . GLN B 1 224 ? -34.600 -23.816 41.593  1.00  11.33 ? 222 GLN A CA  1 
ATOM   3965 C  C   . GLN B 1 224 ? -35.177 -25.135 41.142  1.00  10.56 ? 222 GLN A C   1 
ATOM   3966 O  O   . GLN B 1 224 ? -36.180 -25.147 40.412  1.00  12.99 ? 222 GLN A O   1 
ATOM   3967 C  CB  . GLN B 1 224 ? -33.317 -23.577 40.743  1.00  10.42 ? 222 GLN A CB  1 
ATOM   3968 C  CG  . GLN B 1 224 ? -32.842 -22.131 40.868  1.00  12.27 ? 222 GLN A CG  1 
ATOM   3969 C  CD  . GLN B 1 224 ? -31.602 -21.860 40.020  1.00  12.63 ? 222 GLN A CD  1 
ATOM   3970 O  OE1 . GLN B 1 224 ? -30.557 -22.514 40.195  1.00  11.75 ? 222 GLN A OE1 1 
ATOM   3971 N  NE2 . GLN B 1 224 ? -31.685 -20.843 39.166  1.00  12.85 ? 222 GLN A NE2 1 
ATOM   3972 N  N   . LEU B 1 225 ? -34.421 -26.218 41.420  1.00  11.33 ? 223 LEU A N   1 
ATOM   3973 C  CA  . LEU B 1 225 ? -34.877 -27.557 40.938  1.00  11.27 ? 223 LEU A CA  1 
ATOM   3974 C  C   . LEU B 1 225 ? -36.291 -27.890 41.424  1.00  11.83 ? 223 LEU A C   1 
ATOM   3975 O  O   . LEU B 1 225 ? -37.140 -28.428 40.686  1.00  11.76 ? 223 LEU A O   1 
ATOM   3976 C  CB  . LEU B 1 225 ? -33.821 -28.623 41.340  1.00  12.26 ? 223 LEU A CB  1 
ATOM   3977 C  CG  . LEU B 1 225 ? -34.111 -29.997 40.690  1.00  12.84 ? 223 LEU A CG  1 
ATOM   3978 C  CD1 . LEU B 1 225 ? -34.281 -29.989 39.173  1.00  12.86 ? 223 LEU A CD1 1 
ATOM   3979 C  CD2 . LEU B 1 225 ? -33.016 -30.966 41.117  1.00  11.63 ? 223 LEU A CD2 1 
ATOM   3980 N  N   . ALA B 1 226 ? -36.616 -27.561 42.689  1.00  12.16 ? 224 ALA A N   1 
ATOM   3981 C  CA  . ALA B 1 226 ? -37.958 -27.816 43.152  1.00  12.56 ? 224 ALA A CA  1 
ATOM   3982 C  C   . ALA B 1 226 ? -39.115 -27.205 42.376  1.00  13.69 ? 224 ALA A C   1 
ATOM   3983 O  O   . ALA B 1 226 ? -40.241 -27.733 42.390  1.00  13.38 ? 224 ALA A O   1 
ATOM   3984 C  CB  . ALA B 1 226 ? -38.093 -27.427 44.634  1.00  13.88 ? 224 ALA A CB  1 
ATOM   3985 N  N   . LYS B 1 227 ? -38.846 -26.112 41.706  1.00  13.45 ? 225 LYS A N   1 
ATOM   3986 C  CA  . LYS B 1 227 ? -39.876 -25.412 40.933  1.00  12.20 ? 225 LYS A CA  1 
ATOM   3987 C  C   . LYS B 1 227 ? -40.330 -26.306 39.789  1.00  11.11 ? 225 LYS A C   1 
ATOM   3988 O  O   . LYS B 1 227 ? -41.502 -26.278 39.423  1.00  11.58 ? 225 LYS A O   1 
ATOM   3989 C  CB  . LYS B 1 227 ? -39.348 -24.072 40.424  1.00  15.71 ? 225 LYS A CB  1 
ATOM   3990 C  CG  . LYS B 1 227 ? -39.083 -23.038 41.536  1.00  19.58 ? 225 LYS A CG  1 
ATOM   3991 C  CD  . LYS B 1 227 ? -38.448 -23.643 42.796  1.00  27.89 ? 225 LYS A CD  1 
ATOM   3992 C  CE  . LYS B 1 227 ? -39.091 -23.271 44.169  1.00  30.14 ? 225 LYS A CE  1 
ATOM   3993 N  NZ  . LYS B 1 227 ? -38.492 -23.864 45.409  1.00  21.08 ? 225 LYS A NZ  1 
ATOM   3994 N  N   . PHE B 1 228 ? -39.426 -27.069 39.200  1.00  12.13 ? 226 PHE A N   1 
ATOM   3995 C  CA  . PHE B 1 228 ? -39.810 -27.936 38.062  1.00  12.41 ? 226 PHE A CA  1 
ATOM   3996 C  C   . PHE B 1 228 ? -40.758 -29.046 38.497  1.00  11.67 ? 226 PHE A C   1 
ATOM   3997 O  O   . PHE B 1 228 ? -41.637 -29.462 37.716  1.00  10.90 ? 226 PHE A O   1 
ATOM   3998 C  CB  . PHE B 1 228 ? -38.581 -28.545 37.353  1.00  11.84 ? 226 PHE A CB  1 
ATOM   3999 C  CG  . PHE B 1 228 ? -37.755 -27.526 36.708  1.00  12.85 ? 226 PHE A CG  1 
ATOM   4000 C  CD1 . PHE B 1 228 ? -36.609 -27.004 37.334  1.00  12.30 ? 226 PHE A CD1 1 
ATOM   4001 C  CD2 . PHE B 1 228 ? -38.135 -27.098 35.412  1.00  11.92 ? 226 PHE A CD2 1 
ATOM   4002 C  CE1 . PHE B 1 228 ? -35.872 -26.023 36.685  1.00  13.02 ? 226 PHE A CE1 1 
ATOM   4003 C  CE2 . PHE B 1 228 ? -37.426 -26.119 34.804  1.00  12.56 ? 226 PHE A CE2 1 
ATOM   4004 C  CZ  . PHE B 1 228 ? -36.309 -25.606 35.406  1.00  12.87 ? 226 PHE A CZ  1 
ATOM   4005 N  N   . ARG B 1 229 ? -40.622 -29.479 39.760  1.00  11.36 ? 227 ARG A N   1 
ATOM   4006 C  CA  . ARG B 1 229 ? -41.528 -30.512 40.256  1.00  11.47 ? 227 ARG A CA  1 
ATOM   4007 C  C   . ARG B 1 229 ? -42.931 -30.056 40.535  1.00  12.58 ? 227 ARG A C   1 
ATOM   4008 O  O   . ARG B 1 229 ? -43.771 -30.892 40.841  1.00  13.68 ? 227 ARG A O   1 
ATOM   4009 C  CB  . ARG B 1 229 ? -40.982 -31.105 41.584  1.00  10.54 ? 227 ARG A CB  1 
ATOM   4010 C  CG  . ARG B 1 229 ? -39.551 -31.629 41.463  1.00  10.40 ? 227 ARG A CG  1 
ATOM   4011 C  CD  . ARG B 1 229 ? -39.159 -32.546 42.649  1.00  10.90 ? 227 ARG A CD  1 
ATOM   4012 N  NE  . ARG B 1 229 ? -37.749 -32.915 42.584  1.00  11.74 ? 227 ARG A NE  1 
ATOM   4013 C  CZ  . ARG B 1 229 ? -36.744 -32.263 43.205  1.00  11.18 ? 227 ARG A CZ  1 
ATOM   4014 N  NH1 . ARG B 1 229 ? -37.023 -31.226 44.053  1.00  10.31 ? 227 ARG A NH1 1 
ATOM   4015 N  NH2 . ARG B 1 229 ? -35.492 -32.599 43.012  1.00  12.49 ? 227 ARG A NH2 1 
ATOM   4016 N  N   . SER B 1 230 ? -43.195 -28.742 40.510  1.00  13.89 ? 228 SER A N   1 
ATOM   4017 C  CA  . SER B 1 230 ? -44.560 -28.284 40.608  1.00  14.79 ? 228 SER A CA  1 
ATOM   4018 C  C   . SER B 1 230 ? -45.303 -28.165 39.269  1.00  14.65 ? 228 SER A C   1 
ATOM   4019 O  O   . SER B 1 230 ? -46.505 -27.767 39.234  1.00  14.05 ? 228 SER A O   1 
ATOM   4020 C  CB  . SER B 1 230 ? -44.659 -27.022 41.471  1.00  20.32 ? 228 SER A CB  1 
ATOM   4021 O  OG  . SER B 1 230 ? -44.221 -25.982 40.679  1.00  30.16 ? 228 SER A OG  1 
ATOM   4022 N  N   . LEU B 1 231 ? -44.592 -28.447 38.148  1.00  11.72 ? 229 LEU A N   1 
ATOM   4023 C  CA  . LEU B 1 231 ? -45.341 -28.666 36.925  1.00  10.68 ? 229 LEU A CA  1 
ATOM   4024 C  C   . LEU B 1 231 ? -46.327 -29.802 37.072  1.00  11.43 ? 229 LEU A C   1 
ATOM   4025 O  O   . LEU B 1 231 ? -46.030 -30.795 37.775  1.00  12.70 ? 229 LEU A O   1 
ATOM   4026 C  CB  . LEU B 1 231 ? -44.378 -28.929 35.685  1.00  11.07 ? 229 LEU A CB  1 
ATOM   4027 C  CG  . LEU B 1 231 ? -43.555 -27.743 35.299  1.00  9.92  ? 229 LEU A CG  1 
ATOM   4028 C  CD1 . LEU B 1 231 ? -42.471 -28.287 34.338  1.00  10.88 ? 229 LEU A CD1 1 
ATOM   4029 C  CD2 . LEU B 1 231 ? -44.351 -26.642 34.541  1.00  11.34 ? 229 LEU A CD2 1 
ATOM   4030 N  N   . LEU B 1 232 ? -47.480 -29.696 36.396  1.00  11.53 ? 230 LEU A N   1 
ATOM   4031 C  CA  . LEU B 1 232 ? -48.391 -30.837 36.369  1.00  12.54 ? 230 LEU A CA  1 
ATOM   4032 C  C   . LEU B 1 232 ? -48.203 -31.744 35.133  1.00  14.02 ? 230 LEU A C   1 
ATOM   4033 O  O   . LEU B 1 232 ? -47.799 -31.259 34.036  1.00  13.91 ? 230 LEU A O   1 
ATOM   4034 C  CB  . LEU B 1 232 ? -49.860 -30.351 36.395  1.00  13.67 ? 230 LEU A CB  1 
ATOM   4035 C  CG  . LEU B 1 232 ? -50.166 -29.413 37.550  1.00  15.69 ? 230 LEU A CG  1 
ATOM   4036 C  CD1 . LEU B 1 232 ? -51.676 -29.049 37.393  1.00  17.20 ? 230 LEU A CD1 1 
ATOM   4037 C  CD2 . LEU B 1 232 ? -49.989 -30.270 38.780  1.00  14.86 ? 230 LEU A CD2 1 
ATOM   4038 N  N   . CYS B 1 233 ? -48.472 -33.026 35.290  1.00  13.56 ? 231 CYS A N   1 
ATOM   4039 C  CA  . CYS B 1 233 ? -48.503 -33.930 34.094  1.00  13.71 ? 231 CYS A CA  1 
ATOM   4040 C  C   . CYS B 1 233 ? -49.957 -34.077 33.552  1.00  15.32 ? 231 CYS A C   1 
ATOM   4041 O  O   . CYS B 1 233 ? -50.233 -34.848 32.639  1.00  15.90 ? 231 CYS A O   1 
ATOM   4042 C  CB  . CYS B 1 233 ? -47.895 -35.315 34.394  1.00  13.88 ? 231 CYS A CB  1 
ATOM   4043 S  SG  . CYS B 1 233 ? -48.831 -36.285 35.703  1.00  17.00 ? 231 CYS A SG  1 
ATOM   4044 N  N   . THR B 1 234 ? -50.847 -33.299 34.113  1.00  15.76 ? 232 THR A N   1 
ATOM   4045 C  CA  . THR B 1 234 ? -52.246 -33.378 33.738  1.00  17.25 ? 232 THR A CA  1 
ATOM   4046 C  C   . THR B 1 234 ? -52.724 -32.025 33.180  1.00  17.61 ? 232 THR A C   1 
ATOM   4047 O  O   . THR B 1 234 ? -52.179 -30.975 33.509  1.00  17.39 ? 232 THR A O   1 
ATOM   4048 C  CB  . THR B 1 234 ? -53.060 -33.715 34.995  1.00  18.02 ? 232 THR A CB  1 
ATOM   4049 O  OG1 . THR B 1 234 ? -52.645 -32.869 36.061  1.00  16.63 ? 232 THR A OG1 1 
ATOM   4050 C  CG2 . THR B 1 234 ? -52.821 -35.191 35.424  1.00  18.62 ? 232 THR A CG2 1 
ATOM   4051 N  N   . ALA B 1 235 ? -53.767 -32.038 32.336  1.00  20.07 ? 233 ALA A N   1 
ATOM   4052 C  CA  . ALA B 1 235 ? -54.240 -30.840 31.653  1.00  23.46 ? 233 ALA A CA  1 
ATOM   4053 C  C   . ALA B 1 235 ? -55.313 -30.125 32.530  1.00  28.51 ? 233 ALA A C   1 
ATOM   4054 O  O   . ALA B 1 235 ? -55.805 -30.705 33.502  1.00  26.93 ? 233 ALA A O   1 
ATOM   4055 C  CB  . ALA B 1 235 ? -54.824 -31.221 30.271  1.00  21.17 ? 233 ALA A CB  1 
ATOM   4056 N  N   . GLU B 1 236 ? -55.668 -28.878 32.192  1.00  29.41 ? 234 GLU A N   1 
ATOM   4057 C  CA  . GLU B 1 236 ? -56.714 -28.139 32.931  1.00  36.20 ? 234 GLU A CA  1 
ATOM   4058 C  C   . GLU B 1 236 ? -58.000 -28.992 33.001  1.00  35.71 ? 234 GLU A C   1 
ATOM   4059 O  O   . GLU B 1 236 ? -58.305 -29.731 32.050  1.00  35.58 ? 234 GLU A O   1 
ATOM   4060 C  CB  . GLU B 1 236 ? -57.006 -26.847 32.207  1.00  40.21 ? 234 GLU A CB  1 
ATOM   4061 C  CG  . GLU B 1 236 ? -57.299 -25.676 33.125  1.00  48.79 ? 234 GLU A CG  1 
ATOM   4062 C  CD  . GLU B 1 236 ? -56.941 -24.365 32.451  1.00  58.02 ? 234 GLU A CD  1 
ATOM   4063 O  OE1 . GLU B 1 236 ? -57.325 -24.196 31.253  1.00  48.01 ? 234 GLU A OE1 1 
ATOM   4064 O  OE2 . GLU B 1 236 ? -56.263 -23.528 33.119  1.00  61.92 ? 234 GLU A OE2 1 
ATOM   4065 N  N   . GLY B 1 237 ? -58.686 -28.949 34.148  1.00  40.87 ? 235 GLY A N   1 
ATOM   4066 C  CA  . GLY B 1 237 ? -59.881 -29.799 34.375  1.00  48.16 ? 235 GLY A CA  1 
ATOM   4067 C  C   . GLY B 1 237 ? -59.760 -31.330 34.390  1.00  48.08 ? 235 GLY A C   1 
ATOM   4068 O  O   . GLY B 1 237 ? -60.776 -32.032 34.347  1.00  49.95 ? 235 GLY A O   1 
ATOM   4069 N  N   . GLU B 1 238 ? -58.538 -31.865 34.433  1.00  44.39 ? 236 GLU A N   1 
ATOM   4070 C  CA  . GLU B 1 238 ? -58.279 -33.313 34.677  1.00  34.80 ? 236 GLU A CA  1 
ATOM   4071 C  C   . GLU B 1 238 ? -57.756 -33.307 36.142  1.00  35.95 ? 236 GLU A C   1 
ATOM   4072 O  O   . GLU B 1 238 ? -57.262 -32.255 36.589  1.00  36.87 ? 236 GLU A O   1 
ATOM   4073 C  CB  . GLU B 1 238 ? -57.288 -33.840 33.601  1.00  38.41 ? 236 GLU A CB  1 
ATOM   4074 C  CG  . GLU B 1 238 ? -56.442 -35.092 33.890  1.00  34.02 ? 236 GLU A CG  1 
ATOM   4075 C  CD  . GLU B 1 238 ? -55.463 -35.504 32.748  1.00  41.89 ? 236 GLU A CD  1 
ATOM   4076 O  OE1 . GLU B 1 238 ? -55.005 -34.674 31.874  1.00  36.16 ? 236 GLU A OE1 1 
ATOM   4077 O  OE2 . GLU B 1 238 ? -55.064 -36.700 32.765  1.00  42.17 ? 236 GLU A OE2 1 
ATOM   4078 N  N   . ALA B 1 239 ? -57.934 -34.380 36.926  1.00  30.17 ? 237 ALA A N   1 
ATOM   4079 C  CA  . ALA B 1 239 ? -57.500 -34.371 38.372  1.00  32.61 ? 237 ALA A CA  1 
ATOM   4080 C  C   . ALA B 1 239 ? -55.979 -34.192 38.417  1.00  28.90 ? 237 ALA A C   1 
ATOM   4081 O  O   . ALA B 1 239 ? -55.281 -34.926 37.720  1.00  29.54 ? 237 ALA A O   1 
ATOM   4082 C  CB  . ALA B 1 239 ? -57.871 -35.661 39.100  1.00  32.78 ? 237 ALA A CB  1 
ATOM   4083 N  N   . ALA B 1 240 ? -55.530 -33.212 39.182  1.00  25.27 ? 238 ALA A N   1 
ATOM   4084 C  CA  . ALA B 1 240 ? -54.133 -32.778 39.208  1.00  21.79 ? 238 ALA A CA  1 
ATOM   4085 C  C   . ALA B 1 240 ? -53.186 -33.924 39.634  1.00  23.28 ? 238 ALA A C   1 
ATOM   4086 O  O   . ALA B 1 240 ? -53.436 -34.639 40.626  1.00  20.72 ? 238 ALA A O   1 
ATOM   4087 C  CB  . ALA B 1 240 ? -53.977 -31.539 40.101  1.00  21.84 ? 238 ALA A CB  1 
ATOM   4088 N  N   . ALA B 1 241 ? -52.044 -34.073 38.925  1.00  16.96 ? 239 ALA A N   1 
ATOM   4089 C  CA  . ALA B 1 241 ? -50.979 -34.914 39.468  1.00  15.59 ? 239 ALA A CA  1 
ATOM   4090 C  C   . ALA B 1 241 ? -49.694 -34.174 39.071  1.00  13.89 ? 239 ALA A C   1 
ATOM   4091 O  O   . ALA B 1 241 ? -49.618 -33.594 37.942  1.00  13.86 ? 239 ALA A O   1 
ATOM   4092 C  CB  . ALA B 1 241 ? -50.999 -36.315 38.790  1.00  14.88 ? 239 ALA A CB  1 
ATOM   4093 N  N   . PHE B 1 242 ? -48.711 -34.222 39.949  1.00  12.75 ? 240 PHE A N   1 
ATOM   4094 C  CA  . PHE B 1 242 ? -47.456 -33.458 39.735  1.00  12.17 ? 240 PHE A CA  1 
ATOM   4095 C  C   . PHE B 1 242 ? -46.412 -34.272 39.010  1.00  11.63 ? 240 PHE A C   1 
ATOM   4096 O  O   . PHE B 1 242 ? -46.256 -35.485 39.190  1.00  12.55 ? 240 PHE A O   1 
ATOM   4097 C  CB  . PHE B 1 242 ? -46.875 -33.019 41.095  1.00  11.53 ? 240 PHE A CB  1 
ATOM   4098 C  CG  . PHE B 1 242 ? -47.686 -31.906 41.756  1.00  12.92 ? 240 PHE A CG  1 
ATOM   4099 C  CD1 . PHE B 1 242 ? -48.729 -32.263 42.639  1.00  14.54 ? 240 PHE A CD1 1 
ATOM   4100 C  CD2 . PHE B 1 242 ? -47.478 -30.562 41.483  1.00  15.72 ? 240 PHE A CD2 1 
ATOM   4101 C  CE1 . PHE B 1 242 ? -49.478 -31.267 43.277  1.00  15.77 ? 240 PHE A CE1 1 
ATOM   4102 C  CE2 . PHE B 1 242 ? -48.209 -29.551 42.119  1.00  17.75 ? 240 PHE A CE2 1 
ATOM   4103 C  CZ  . PHE B 1 242 ? -49.189 -29.921 43.049  1.00  17.02 ? 240 PHE A CZ  1 
ATOM   4104 N  N   . LEU B 1 243 ? -45.627 -33.564 38.150  1.00  12.21 ? 241 LEU A N   1 
ATOM   4105 C  CA  . LEU B 1 243 ? -44.514 -34.180 37.424  1.00  10.05 ? 241 LEU A CA  1 
ATOM   4106 C  C   . LEU B 1 243 ? -43.268 -34.124 38.347  1.00  9.04  ? 241 LEU A C   1 
ATOM   4107 O  O   . LEU B 1 243 ? -42.276 -33.360 38.149  1.00  9.23  ? 241 LEU A O   1 
ATOM   4108 C  CB  . LEU B 1 243 ? -44.291 -33.380 36.105  1.00  11.21 ? 241 LEU A CB  1 
ATOM   4109 C  CG  . LEU B 1 243 ? -43.240 -33.937 35.171  1.00  11.67 ? 241 LEU A CG  1 
ATOM   4110 C  CD1 . LEU B 1 243 ? -43.614 -35.326 34.670  1.00  9.33  ? 241 LEU A CD1 1 
ATOM   4111 C  CD2 . LEU B 1 243 ? -43.076 -32.943 33.961  1.00  11.51 ? 241 LEU A CD2 1 
ATOM   4112 N  N   . VAL B 1 244 ? -43.299 -34.929 39.436  1.00  9.58  ? 242 VAL A N   1 
ATOM   4113 C  CA  . VAL B 1 244 ? -42.181 -34.886 40.404  1.00  9.79  ? 242 VAL A CA  1 
ATOM   4114 C  C   . VAL B 1 244 ? -40.921 -35.568 39.940  1.00  8.71  ? 242 VAL A C   1 
ATOM   4115 O  O   . VAL B 1 244 ? -39.868 -35.312 40.487  1.00  10.60 ? 242 VAL A O   1 
ATOM   4116 C  CB  . VAL B 1 244 ? -42.579 -35.424 41.831  1.00  12.13 ? 242 VAL A CB  1 
ATOM   4117 C  CG1 . VAL B 1 244 ? -43.623 -34.468 42.420  1.00  13.27 ? 242 VAL A CG1 1 
ATOM   4118 C  CG2 . VAL B 1 244 ? -43.058 -36.852 41.724  1.00  14.27 ? 242 VAL A CG2 1 
ATOM   4119 N  N   . SER B 1 245 ? -41.031 -36.502 38.979  1.00  9.42  ? 243 SER A N   1 
ATOM   4120 C  CA  . SER B 1 245 ? -39.904 -37.241 38.505  1.00  9.29  ? 243 SER A CA  1 
ATOM   4121 C  C   . SER B 1 245 ? -40.213 -37.623 37.008  1.00  8.66  ? 243 SER A C   1 
ATOM   4122 O  O   . SER B 1 245 ? -41.334 -37.994 36.662  1.00  9.44  ? 243 SER A O   1 
ATOM   4123 C  CB  . SER B 1 245 ? -39.725 -38.548 39.322  1.00  10.08 ? 243 SER A CB  1 
ATOM   4124 O  OG  . SER B 1 245 ? -38.548 -39.247 38.936  1.00  11.85 ? 243 SER A OG  1 
ATOM   4125 N  N   . ASN B 1 246 ? -39.203 -37.488 36.155  1.00  9.11  ? 244 ASN A N   1 
ATOM   4126 C  CA  . ASN B 1 246 ? -39.447 -37.740 34.691  1.00  8.40  ? 244 ASN A CA  1 
ATOM   4127 C  C   . ASN B 1 246 ? -38.138 -38.225 34.031  1.00  9.07  ? 244 ASN A C   1 
ATOM   4128 O  O   . ASN B 1 246 ? -37.820 -37.740 32.918  1.00  8.71  ? 244 ASN A O   1 
ATOM   4129 C  CB  . ASN B 1 246 ? -39.993 -36.469 34.007  1.00  9.03  ? 244 ASN A CB  1 
ATOM   4130 C  CG  . ASN B 1 246 ? -39.003 -35.320 34.039  1.00  9.14  ? 244 ASN A CG  1 
ATOM   4131 O  OD1 . ASN B 1 246 ? -38.008 -35.373 34.758  1.00  9.79  ? 244 ASN A OD1 1 
ATOM   4132 N  ND2 . ASN B 1 246 ? -39.249 -34.308 33.237  1.00  8.20  ? 244 ASN A ND2 1 
ATOM   4133 N  N   . HIS B 1 247 ? -37.410 -39.160 34.681  1.00  8.84  ? 245 HIS A N   1 
ATOM   4134 C  CA  . HIS B 1 247 ? -36.178 -39.739 34.097  1.00  9.60  ? 245 HIS A CA  1 
ATOM   4135 C  C   . HIS B 1 247 ? -36.303 -41.239 33.876  1.00  10.01 ? 245 HIS A C   1 
ATOM   4136 O  O   . HIS B 1 247 ? -36.912 -41.976 34.735  1.00  12.16 ? 245 HIS A O   1 
ATOM   4137 C  CB  . HIS B 1 247 ? -34.937 -39.416 34.981  1.00  10.08 ? 245 HIS A CB  1 
ATOM   4138 C  CG  . HIS B 1 247 ? -35.009 -40.005 36.357  1.00  10.58 ? 245 HIS A CG  1 
ATOM   4139 N  ND1 . HIS B 1 247 ? -34.207 -41.045 36.785  1.00  12.69 ? 245 HIS A ND1 1 
ATOM   4140 C  CD2 . HIS B 1 247 ? -35.776 -39.608 37.434  1.00  9.92  ? 245 HIS A CD2 1 
ATOM   4141 C  CE1 . HIS B 1 247 ? -34.532 -41.342 38.077  1.00  12.85 ? 245 HIS A CE1 1 
ATOM   4142 N  NE2 . HIS B 1 247 ? -35.491 -40.455 38.483  1.00  13.10 ? 245 HIS A NE2 1 
ATOM   4143 N  N   . ARG B 1 248 ? -35.761 -41.711 32.763  1.00  9.15  ? 246 ARG A N   1 
ATOM   4144 C  CA  . ARG B 1 248 ? -35.748 -43.164 32.473  1.00  10.38 ? 246 ARG A CA  1 
ATOM   4145 C  C   . ARG B 1 248 ? -34.428 -43.733 33.048  1.00  10.51 ? 246 ARG A C   1 
ATOM   4146 O  O   . ARG B 1 248 ? -33.390 -43.090 32.955  1.00  11.42 ? 246 ARG A O   1 
ATOM   4147 C  CB  . ARG B 1 248 ? -35.697 -43.334 30.930  1.00  9.53  ? 246 ARG A CB  1 
ATOM   4148 C  CG  . ARG B 1 248 ? -35.800 -44.858 30.604  1.00  11.68 ? 246 ARG A CG  1 
ATOM   4149 C  CD  . ARG B 1 248 ? -35.519 -45.082 29.133  1.00  10.81 ? 246 ARG A CD  1 
ATOM   4150 N  NE  . ARG B 1 248 ? -36.061 -46.418 28.819  1.00  10.87 ? 246 ARG A NE  1 
ATOM   4151 C  CZ  . ARG B 1 248 ? -35.820 -47.148 27.738  1.00  11.90 ? 246 ARG A CZ  1 
ATOM   4152 N  NH1 . ARG B 1 248 ? -35.018 -46.711 26.781  1.00  9.97  ? 246 ARG A NH1 1 
ATOM   4153 N  NH2 . ARG B 1 248 ? -36.394 -48.345 27.608  1.00  12.89 ? 246 ARG A NH2 1 
ATOM   4154 N  N   . PRO B 1 249 ? -34.442 -44.977 33.637  1.00  11.75 ? 247 PRO A N   1 
ATOM   4155 C  CA  . PRO B 1 249 ? -33.176 -45.584 34.035  1.00  11.37 ? 247 PRO A CA  1 
ATOM   4156 C  C   . PRO B 1 249 ? -32.268 -46.014 32.898  1.00  11.54 ? 247 PRO A C   1 
ATOM   4157 O  O   . PRO B 1 249 ? -32.758 -46.220 31.785  1.00  12.10 ? 247 PRO A O   1 
ATOM   4158 C  CB  . PRO B 1 249 ? -33.608 -46.840 34.837  1.00  12.98 ? 247 PRO A CB  1 
ATOM   4159 C  CG  . PRO B 1 249 ? -35.040 -46.697 35.101  1.00  14.02 ? 247 PRO A CG  1 
ATOM   4160 C  CD  . PRO B 1 249 ? -35.625 -45.743 34.034  1.00  13.76 ? 247 PRO A CD  1 
ATOM   4161 N  N   . PRO B 1 250 ? -30.968 -46.111 33.155  1.00  12.47 ? 248 PRO A N   1 
ATOM   4162 C  CA  . PRO B 1 250 ? -30.068 -46.532 32.119  1.00  12.25 ? 248 PRO A CA  1 
ATOM   4163 C  C   . PRO B 1 250 ? -30.432 -47.947 31.665  1.00  14.01 ? 248 PRO A C   1 
ATOM   4164 O  O   . PRO B 1 250 ? -30.857 -48.820 32.489  1.00  14.12 ? 248 PRO A O   1 
ATOM   4165 C  CB  . PRO B 1 250 ? -28.706 -46.520 32.803  1.00  13.28 ? 248 PRO A CB  1 
ATOM   4166 C  CG  . PRO B 1 250 ? -28.786 -45.383 33.814  1.00  13.94 ? 248 PRO A CG  1 
ATOM   4167 C  CD  . PRO B 1 250 ? -30.222 -45.609 34.349  1.00  15.49 ? 248 PRO A CD  1 
ATOM   4168 N  N   . GLN B 1 251 ? -30.227 -48.147 30.379  1.00  10.79 ? 249 GLN A N   1 
ATOM   4169 C  CA  . GLN B 1 251 ? -30.430 -49.421 29.708  1.00  12.18 ? 249 GLN A CA  1 
ATOM   4170 C  C   . GLN B 1 251 ? -29.090 -50.109 29.377  1.00  10.77 ? 249 GLN A C   1 
ATOM   4171 O  O   . GLN B 1 251 ? -28.012 -49.464 29.250  1.00  11.46 ? 249 GLN A O   1 
ATOM   4172 C  CB  . GLN B 1 251 ? -31.286 -49.140 28.480  1.00  12.14 ? 249 GLN A CB  1 
ATOM   4173 C  CG  . GLN B 1 251 ? -32.705 -48.638 28.768  1.00  12.47 ? 249 GLN A CG  1 
ATOM   4174 C  CD  . GLN B 1 251 ? -33.452 -49.347 29.866  1.00  15.79 ? 249 GLN A CD  1 
ATOM   4175 O  OE1 . GLN B 1 251 ? -33.861 -48.734 30.858  1.00  16.53 ? 249 GLN A OE1 1 
ATOM   4176 N  NE2 . GLN B 1 251 ? -33.621 -50.644 29.711  1.00  13.96 ? 249 GLN A NE2 1 
ATOM   4177 N  N   . PRO B 1 252 ? -29.114 -51.446 29.189  1.00  11.57 ? 250 PRO A N   1 
ATOM   4178 C  CA  . PRO B 1 252 ? -27.801 -52.102 28.932  1.00  13.83 ? 250 PRO A CA  1 
ATOM   4179 C  C   . PRO B 1 252 ? -27.170 -51.742 27.578  1.00  13.85 ? 250 PRO A C   1 
ATOM   4180 O  O   . PRO B 1 252 ? -27.873 -51.512 26.563  1.00  13.94 ? 250 PRO A O   1 
ATOM   4181 C  CB  . PRO B 1 252 ? -28.162 -53.625 28.929  1.00  14.16 ? 250 PRO A CB  1 
ATOM   4182 C  CG  . PRO B 1 252 ? -29.493 -53.724 29.501  1.00  15.18 ? 250 PRO A CG  1 
ATOM   4183 C  CD  . PRO B 1 252 ? -30.224 -52.396 29.204  1.00  13.14 ? 250 PRO A CD  1 
ATOM   4184 N  N   . LEU B 1 253 ? -25.841 -51.690 27.552  1.00  13.35 ? 251 LEU A N   1 
ATOM   4185 C  CA  . LEU B 1 253 ? -25.103 -51.319 26.326  1.00  13.70 ? 251 LEU A CA  1 
ATOM   4186 C  C   . LEU B 1 253 ? -25.230 -52.320 25.197  1.00  16.08 ? 251 LEU A C   1 
ATOM   4187 O  O   . LEU B 1 253 ? -25.230 -51.943 24.038  1.00  14.88 ? 251 LEU A O   1 
ATOM   4188 C  CB  . LEU B 1 253 ? -23.614 -51.250 26.699  1.00  16.84 ? 251 LEU A CB  1 
ATOM   4189 C  CG  . LEU B 1 253 ? -22.728 -50.004 26.669  1.00  23.59 ? 251 LEU A CG  1 
ATOM   4190 C  CD1 . LEU B 1 253 ? -23.443 -48.681 26.465  1.00  21.75 ? 251 LEU A CD1 1 
ATOM   4191 C  CD2 . LEU B 1 253 ? -21.717 -50.060 27.830  1.00  23.38 ? 251 LEU A CD2 1 
ATOM   4192 N  N   . LYS B 1 254 ? -25.373 -53.581 25.560  1.00  15.39 ? 252 LYS A N   1 
ATOM   4193 C  CA  . LYS B 1 254 ? -25.572 -54.673 24.561  1.00  16.08 ? 252 LYS A CA  1 
ATOM   4194 C  C   . LYS B 1 254 ? -24.519 -54.650 23.444  1.00  16.19 ? 252 LYS A C   1 
ATOM   4195 O  O   . LYS B 1 254 ? -24.845 -54.740 22.270  1.00  20.70 ? 252 LYS A O   1 
ATOM   4196 C  CB  . LYS B 1 254 ? -26.994 -54.644 23.955  1.00  19.24 ? 252 LYS A CB  1 
ATOM   4197 C  CG  . LYS B 1 254 ? -28.077 -55.052 24.970  1.00  22.28 ? 252 LYS A CG  1 
ATOM   4198 C  CD  . LYS B 1 254 ? -29.425 -55.109 24.310  1.00  29.18 ? 252 LYS A CD  1 
ATOM   4199 C  CE  . LYS B 1 254 ? -30.478 -55.493 25.318  1.00  32.10 ? 252 LYS A CE  1 
ATOM   4200 N  NZ  . LYS B 1 254 ? -29.667 -56.212 26.338  1.00  35.51 ? 252 LYS A NZ  1 
ATOM   4201 N  N   . GLY B 1 255 ? -23.270 -54.449 23.798  1.00  16.49 ? 253 GLY A N   1 
ATOM   4202 C  CA  . GLY B 1 255 ? -22.166 -54.586 22.787  1.00  19.27 ? 253 GLY A CA  1 
ATOM   4203 C  C   . GLY B 1 255 ? -21.660 -53.232 22.284  1.00  19.06 ? 253 GLY A C   1 
ATOM   4204 O  O   . GLY B 1 255 ? -20.567 -53.144 21.702  1.00  19.19 ? 253 GLY A O   1 
ATOM   4205 N  N   . ARG B 1 256 ? -22.459 -52.145 22.441  1.00  16.87 ? 254 ARG A N   1 
ATOM   4206 C  CA  . ARG B 1 256 ? -21.960 -50.840 21.973  1.00  16.46 ? 254 ARG A CA  1 
ATOM   4207 C  C   . ARG B 1 256 ? -20.767 -50.373 22.777  1.00  16.77 ? 254 ARG A C   1 
ATOM   4208 O  O   . ARG B 1 256 ? -20.662 -50.669 23.981  1.00  19.36 ? 254 ARG A O   1 
ATOM   4209 C  CB  . ARG B 1 256 ? -23.057 -49.763 22.179  1.00  15.61 ? 254 ARG A CB  1 
ATOM   4210 C  CG  . ARG B 1 256 ? -24.313 -50.042 21.318  1.00  13.56 ? 254 ARG A CG  1 
ATOM   4211 C  CD  . ARG B 1 256 ? -25.461 -49.103 21.741  1.00  13.27 ? 254 ARG A CD  1 
ATOM   4212 N  NE  . ARG B 1 256 ? -26.063 -49.455 23.020  1.00  12.10 ? 254 ARG A NE  1 
ATOM   4213 C  CZ  . ARG B 1 256 ? -27.001 -48.752 23.646  1.00  12.09 ? 254 ARG A CZ  1 
ATOM   4214 N  NH1 . ARG B 1 256 ? -27.330 -47.540 23.129  1.00  10.92 ? 254 ARG A NH1 1 
ATOM   4215 N  NH2 . ARG B 1 256 ? -27.505 -49.184 24.754  1.00  11.99 ? 254 ARG A NH2 1 
ATOM   4216 N  N   . LYS B 1 257 ? -19.970 -49.555 22.156  1.00  18.52 ? 255 LYS A N   1 
ATOM   4217 C  CA  . LYS B 1 257 ? -18.859 -48.936 22.852  1.00  21.79 ? 255 LYS A CA  1 
ATOM   4218 C  C   . LYS B 1 257 ? -19.044 -47.406 22.880  1.00  20.56 ? 255 LYS A C   1 
ATOM   4219 O  O   . LYS B 1 257 ? -19.579 -46.747 21.935  1.00  24.66 ? 255 LYS A O   1 
ATOM   4220 C  CB  . LYS B 1 257 ? -17.530 -49.274 22.173  1.00  24.08 ? 255 LYS A CB  1 
ATOM   4221 C  CG  . LYS B 1 257 ? -17.178 -50.772 22.243  1.00  27.09 ? 255 LYS A CG  1 
ATOM   4222 C  CD  . LYS B 1 257 ? -15.971 -50.973 21.385  1.00  30.93 ? 255 LYS A CD  1 
ATOM   4223 C  CE  . LYS B 1 257 ? -15.419 -52.374 21.559  1.00  34.46 ? 255 LYS A CE  1 
ATOM   4224 N  NZ  . LYS B 1 257 ? -16.209 -53.262 20.715  1.00  36.27 ? 255 LYS A NZ  1 
ATOM   4225 N  N   . VAL B 1 258 ? -18.661 -46.860 24.009  1.00  18.11 ? 256 VAL A N   1 
ATOM   4226 C  CA  . VAL B 1 258 ? -18.683 -45.398 24.161  1.00  17.49 ? 256 VAL A CA  1 
ATOM   4227 C  C   . VAL B 1 258 ? -17.307 -44.783 23.874  1.00  16.80 ? 256 VAL A C   1 
ATOM   4228 O  O   . VAL B 1 258 ? -16.291 -45.357 24.337  1.00  19.97 ? 256 VAL A O   1 
ATOM   4229 C  CB  . VAL B 1 258 ? -19.051 -45.142 25.617  1.00  15.40 ? 256 VAL A CB  1 
ATOM   4230 C  CG1 . VAL B 1 258 ? -19.056 -43.618 25.923  1.00  15.60 ? 256 VAL A CG1 1 
ATOM   4231 C  CG2 . VAL B 1 258 ? -20.383 -45.877 25.910  1.00  15.86 ? 256 VAL A CG2 1 
ATOM   4232 N  N   . ARG B 1 259 ? -17.261 -43.709 23.107  1.00  17.69 ? 257 ARG A N   1 
ATOM   4233 C  CA  . ARG B 1 259 ? -15.988 -43.034 22.713  1.00  17.85 ? 257 ARG A CA  1 
ATOM   4234 C  C   . ARG B 1 259 ? -15.882 -41.742 23.471  1.00  18.54 ? 257 ARG A C   1 
ATOM   4235 O  O   . ARG B 1 259 ? -16.871 -41.117 23.807  1.00  17.41 ? 257 ARG A O   1 
ATOM   4236 C  CB  . ARG B 1 259 ? -15.926 -42.711 21.231  1.00  20.09 ? 257 ARG A CB  1 
ATOM   4237 C  CG  . ARG B 1 259 ? -16.022 -43.963 20.354  1.00  21.86 ? 257 ARG A CG  1 
ATOM   4238 C  CD  . ARG B 1 259 ? -15.868 -43.562 18.898  1.00  22.90 ? 257 ARG A CD  1 
ATOM   4239 N  NE  . ARG B 1 259 ? -17.131 -42.997 18.383  1.00  21.69 ? 257 ARG A NE  1 
ATOM   4240 C  CZ  . ARG B 1 259 ? -17.254 -42.209 17.309  1.00  21.12 ? 257 ARG A CZ  1 
ATOM   4241 N  NH1 . ARG B 1 259 ? -16.199 -41.878 16.581  1.00  22.04 ? 257 ARG A NH1 1 
ATOM   4242 N  NH2 . ARG B 1 259 ? -18.447 -41.752 16.969  1.00  18.81 ? 257 ARG A NH2 1 
ATOM   4243 N  N   . ALA B 1 260 ? -14.659 -41.319 23.746  1.00  15.69 ? 258 ALA A N   1 
ATOM   4244 C  CA  . ALA B 1 260 ? -14.404 -40.020 24.456  1.00  15.57 ? 258 ALA A CA  1 
ATOM   4245 C  C   . ALA B 1 260 ? -13.719 -39.049 23.531  1.00  16.18 ? 258 ALA A C   1 
ATOM   4246 O  O   . ALA B 1 260 ? -12.868 -39.452 22.709  1.00  17.89 ? 258 ALA A O   1 
ATOM   4247 C  CB  . ALA B 1 260 ? -13.546 -40.265 25.704  1.00  16.45 ? 258 ALA A CB  1 
ATOM   4248 N  N   . SER B 1 261 ? -14.057 -37.751 23.665  1.00  12.34 ? 259 SER A N   1 
ATOM   4249 C  CA  . SER B 1 261 ? -13.512 -36.712 22.883  1.00  13.16 ? 259 SER A CA  1 
ATOM   4250 C  C   . SER B 1 261 ? -12.139 -36.233 23.393  1.00  14.82 ? 259 SER A C   1 
ATOM   4251 O  O   . SER B 1 261 ? -11.524 -35.329 22.752  1.00  16.04 ? 259 SER A O   1 
ATOM   4252 C  CB  . SER B 1 261 ? -14.437 -35.509 22.888  1.00  14.34 ? 259 SER A CB  1 
ATOM   4253 O  OG  . SER B 1 261 ? -14.417 -34.771 24.065  1.00  13.72 ? 259 SER A OG  1 
ATOM   4254 N  N   . PHE B 1 262 ? -11.712 -36.799 24.533  1.00  15.11 ? 260 PHE A N   1 
ATOM   4255 C  CA  . PHE B 1 262 ? -10.633 -36.195 25.341  1.00  17.95 ? 260 PHE A CA  1 
ATOM   4256 C  C   . PHE B 1 262 ? -9.814  -37.382 25.950  1.00  20.18 ? 260 PHE A C   1 
ATOM   4257 O  O   . PHE B 1 262 ? -10.306 -38.500 26.078  1.00  17.90 ? 260 PHE A O   1 
ATOM   4258 C  CB  . PHE B 1 262 ? -11.288 -35.292 26.456  1.00  16.43 ? 260 PHE A CB  1 
ATOM   4259 C  CG  . PHE B 1 262 ? -12.162 -36.076 27.402  1.00  17.03 ? 260 PHE A CG  1 
ATOM   4260 C  CD1 . PHE B 1 262 ? -11.630 -36.590 28.628  1.00  17.80 ? 260 PHE A CD1 1 
ATOM   4261 C  CD2 . PHE B 1 262 ? -13.510 -36.367 27.093  1.00  14.13 ? 260 PHE A CD2 1 
ATOM   4262 C  CE1 . PHE B 1 262 ? -12.428 -37.317 29.500  1.00  19.74 ? 260 PHE A CE1 1 
ATOM   4263 C  CE2 . PHE B 1 262 ? -14.282 -37.107 27.942  1.00  16.14 ? 260 PHE A CE2 1 
ATOM   4264 C  CZ  . PHE B 1 262 ? -13.758 -37.605 29.148  1.00  18.96 ? 260 PHE A CZ  1 
ATOM   4265 N  N   . HIS B 1 263 ? -8.533  -37.137 26.287  1.00  30.30 ? 261 HIS A N   1 
ATOM   4266 C  CA  . HIS B 1 263 ? -7.791  -38.132 27.086  1.00  37.70 ? 261 HIS A CA  1 
ATOM   4267 C  C   . HIS B 1 263 ? -7.131  -37.618 28.320  1.00  46.83 ? 261 HIS A C   1 
ATOM   4268 O  O   . HIS B 1 263 ? -6.546  -38.404 29.064  1.00  47.82 ? 261 HIS A O   1 
ATOM   4269 C  CB  . HIS B 1 263 ? -6.763  -38.929 26.269  1.00  42.69 ? 261 HIS A CB  1 
ATOM   4270 C  CG  . HIS B 1 263 ? -5.968  -38.110 25.266  1.00  47.50 ? 261 HIS A CG  1 
ATOM   4271 N  ND1 . HIS B 1 263 ? -5.836  -36.774 25.345  1.00  51.00 ? 261 HIS A ND1 1 
ATOM   4272 C  CD2 . HIS B 1 263 ? -5.248  -38.510 24.132  1.00  51.22 ? 261 HIS A CD2 1 
ATOM   4273 C  CE1 . HIS B 1 263 ? -5.096  -36.326 24.297  1.00  59.31 ? 261 HIS A CE1 1 
ATOM   4274 N  NE2 . HIS B 1 263 ? -4.730  -37.396 23.560  1.00  57.83 ? 261 HIS A NE2 1 
ATOM   4275 O  OXT . HIS B 1 263 ? -7.117  -36.414 28.593  1.00  53.32 ? 261 HIS A OXT 1 
HETATM 4276 ZN ZN  . ZN  C 2 .   ? -6.881  -4.558  13.211  1.00  10.95 ? 301 ZN  B ZN  1 
HETATM 4277 CL CL  A EWW D 3 .   ? -6.577  -5.113  19.261  0.50  26.44 ? 302 EWW B CL  1 
HETATM 4278 CL CL  B EWW D 3 .   ? -7.073  -4.765  19.219  0.50  28.22 ? 302 EWW B CL  1 
HETATM 4279 C  C3  A EWW D 3 .   ? -6.610  -3.485  18.543  0.50  25.04 ? 302 EWW B C3  1 
HETATM 4280 C  C3  B EWW D 3 .   ? -6.832  -3.231  18.396  0.50  28.77 ? 302 EWW B C3  1 
HETATM 4281 C  C4  A EWW D 3 .   ? -6.361  -3.273  17.175  0.50  21.99 ? 302 EWW B C4  1 
HETATM 4282 C  C4  B EWW D 3 .   ? -6.378  -3.171  17.063  0.50  26.03 ? 302 EWW B C4  1 
HETATM 4283 S  S6  A EWW D 3 .   ? -5.965  -4.607  16.041  0.50  19.05 ? 302 EWW B S6  1 
HETATM 4284 S  S6  B EWW D 3 .   ? -5.967  -4.639  16.098  0.50  22.90 ? 302 EWW B S6  1 
HETATM 4285 O  O8  A EWW D 3 .   ? -7.247  -5.325  15.726  0.50  18.18 ? 302 EWW B O8  1 
HETATM 4286 O  O8  B EWW D 3 .   ? -7.208  -5.510  15.932  0.50  22.99 ? 302 EWW B O8  1 
HETATM 4287 N  N11 A EWW D 3 .   ? -5.667  -3.809  14.412  0.50  17.80 ? 302 EWW B N11 1 
HETATM 4288 N  N11 B EWW D 3 .   ? -5.678  -4.141  14.365  0.50  23.23 ? 302 EWW B N11 1 
HETATM 4289 O  O7  A EWW D 3 .   ? -4.603  -5.335  16.631  0.50  18.88 ? 302 EWW B O7  1 
HETATM 4290 O  O7  B EWW D 3 .   ? -4.594  -5.258  16.798  0.50  24.58 ? 302 EWW B O7  1 
HETATM 4291 C  C5  A EWW D 3 .   ? -6.368  -2.021  16.586  0.50  24.31 ? 302 EWW B C5  1 
HETATM 4292 C  C5  B EWW D 3 .   ? -6.188  -1.961  16.421  0.50  28.38 ? 302 EWW B C5  1 
HETATM 4293 C  C2  A EWW D 3 .   ? -6.867  -2.345  19.322  0.50  26.64 ? 302 EWW B C2  1 
HETATM 4294 C  C2  B EWW D 3 .   ? -7.109  -2.043  19.089  0.50  30.02 ? 302 EWW B C2  1 
HETATM 4295 C  C22 A EWW D 3 .   ? -6.888  -1.070  18.730  0.50  28.14 ? 302 EWW B C22 1 
HETATM 4296 C  C22 B EWW D 3 .   ? -6.915  -0.818  18.445  0.50  31.82 ? 302 EWW B C22 1 
HETATM 4297 C  C1  A EWW D 3 .   ? -6.639  -0.912  17.382  0.50  25.15 ? 302 EWW B C1  1 
HETATM 4298 C  C1  B EWW D 3 .   ? -6.464  -0.795  17.137  0.50  30.70 ? 302 EWW B C1  1 
HETATM 4299 C  C9  A EWW D 3 .   ? -7.109  0.144   19.540  0.50  30.93 ? 302 EWW B C9  1 
HETATM 4300 C  C9  B EWW D 3 .   ? -7.129  0.470   19.137  0.50  35.36 ? 302 EWW B C9  1 
HETATM 4301 O  O12 A EWW D 3 .   ? -7.034  0.015   20.749  0.50  29.52 ? 302 EWW B O12 1 
HETATM 4302 O  O12 B EWW D 3 .   ? -6.690  1.488   18.590  0.50  32.79 ? 302 EWW B O12 1 
HETATM 4303 C  C10 A EWW D 3 .   ? -7.319  1.513   18.937  0.50  33.59 ? 302 EWW B C10 1 
HETATM 4304 C  C10 B EWW D 3 .   ? -7.770  0.526   20.505  0.50  36.62 ? 302 EWW B C10 1 
HETATM 4305 S  S13 A EWW D 3 .   ? -7.713  2.688   20.277  0.50  36.71 ? 302 EWW B S13 1 
HETATM 4306 S  S13 B EWW D 3 .   ? -6.598  -0.075  21.784  0.50  40.74 ? 302 EWW B S13 1 
HETATM 4307 C  C14 A EWW D 3 .   ? -9.395  2.058   20.468  0.50  32.52 ? 302 EWW B C14 1 
HETATM 4308 C  C14 B EWW D 3 .   ? -6.461  1.533   22.551  0.010 36.74 ? 302 EWW B C14 1 
HETATM 4309 N  N17 A EWW D 3 .   ? -10.353 2.842   20.996  0.50  30.29 ? 302 EWW B N17 1 
HETATM 4310 N  N17 B EWW D 3 .   ? -5.291  2.223   22.477  0.010 36.10 ? 302 EWW B N17 1 
HETATM 4311 C  C18 A EWW D 3 .   ? -11.626 2.368   21.137  0.50  30.54 ? 302 EWW B C18 1 
HETATM 4312 C  C18 B EWW D 3 .   ? -5.171  3.457   23.061  0.010 35.41 ? 302 EWW B C18 1 
HETATM 4313 O  O21 A EWW D 3 .   ? -12.395 3.160   21.606  0.50  32.17 ? 302 EWW B O21 1 
HETATM 4314 O  O21 B EWW D 3 .   ? -4.119  4.065   22.988  0.010 34.70 ? 302 EWW B O21 1 
HETATM 4315 C  C19 A EWW D 3 .   ? -11.987 1.059   20.765  0.50  24.61 ? 302 EWW B C19 1 
HETATM 4316 C  C19 B EWW D 3 .   ? -6.254  4.013   23.736  0.010 35.02 ? 302 EWW B C19 1 
HETATM 4317 C  C16 A EWW D 3 .   ? -10.952 0.292   20.200  0.50  27.46 ? 302 EWW B C16 1 
HETATM 4318 C  C16 B EWW D 3 .   ? -7.443  3.286   23.799  0.010 34.83 ? 302 EWW B C16 1 
HETATM 4319 N  N15 A EWW D 3 .   ? -9.694  0.790   20.087  0.50  28.61 ? 302 EWW B N15 1 
HETATM 4320 N  N15 B EWW D 3 .   ? -7.526  2.066   23.209  0.010 35.62 ? 302 EWW B N15 1 
HETATM 4321 C  C20 A EWW D 3 .   ? -11.119 -1.106  19.760  0.50  24.88 ? 302 EWW B C20 1 
HETATM 4322 C  C20 B EWW D 3 .   ? -8.619  3.849   24.512  0.50  32.67 ? 302 EWW B C20 1 
HETATM 4323 C  C1  . PEG E 4 .   ? -25.700 5.216   19.420  1.00  28.14 ? 303 PEG B C1  1 
HETATM 4324 O  O1  . PEG E 4 .   ? -26.293 4.591   20.635  1.00  22.78 ? 303 PEG B O1  1 
HETATM 4325 C  C2  . PEG E 4 .   ? -26.392 5.503   18.064  1.00  26.49 ? 303 PEG B C2  1 
HETATM 4326 O  O2  . PEG E 4 .   ? -26.598 4.444   17.118  1.00  35.22 ? 303 PEG B O2  1 
HETATM 4327 C  C3  . PEG E 4 .   ? -27.919 4.152   16.707  1.00  31.68 ? 303 PEG B C3  1 
HETATM 4328 C  C4  . PEG E 4 .   ? -28.253 2.708   16.444  1.00  29.47 ? 303 PEG B C4  1 
HETATM 4329 O  O4  . PEG E 4 .   ? -29.537 2.403   17.082  1.00  27.67 ? 303 PEG B O4  1 
HETATM 4330 S  S   . DMS F 5 .   ? -1.725  -14.546 28.737  1.00  62.43 ? 304 DMS B S   1 
HETATM 4331 O  O   . DMS F 5 .   ? -1.645  -16.047 28.852  1.00  51.98 ? 304 DMS B O   1 
HETATM 4332 C  C1  . DMS F 5 .   ? -3.393  -14.286 28.633  1.00  40.35 ? 304 DMS B C1  1 
HETATM 4333 C  C2  . DMS F 5 .   ? -1.336  -13.683 30.183  1.00  59.36 ? 304 DMS B C2  1 
HETATM 4334 C  C1  . CIT G 6 .   ? 1.845   -4.000  0.051   1.00  36.32 ? 305 CIT B C1  1 
HETATM 4335 O  O1  . CIT G 6 .   ? 0.886   -4.701  -0.355  1.00  31.64 ? 305 CIT B O1  1 
HETATM 4336 O  O2  . CIT G 6 .   ? 2.475   -4.411  1.101   1.00  32.45 ? 305 CIT B O2  1 
HETATM 4337 C  C2  . CIT G 6 .   ? 2.219   -2.713  -0.705  1.00  38.15 ? 305 CIT B C2  1 
HETATM 4338 C  C3  . CIT G 6 .   ? 1.165   -1.565  -0.772  1.00  43.34 ? 305 CIT B C3  1 
HETATM 4339 O  O7  . CIT G 6 .   ? 0.780   -1.273  0.569   1.00  41.04 ? 305 CIT B O7  1 
HETATM 4340 C  C4  . CIT G 6 .   ? 1.531   -0.228  -1.531  1.00  51.81 ? 305 CIT B C4  1 
HETATM 4341 C  C5  . CIT G 6 .   ? 1.065   1.150   -0.956  1.00  59.85 ? 305 CIT B C5  1 
HETATM 4342 O  O3  . CIT G 6 .   ? 0.734   2.120   -1.750  1.00  46.44 ? 305 CIT B O3  1 
HETATM 4343 O  O4  . CIT G 6 .   ? 1.054   1.293   0.314   1.00  53.54 ? 305 CIT B O4  1 
HETATM 4344 C  C6  . CIT G 6 .   ? -0.021  -2.130  -1.483  1.00  35.13 ? 305 CIT B C6  1 
HETATM 4345 O  O5  . CIT G 6 .   ? 0.020   -2.330  -2.739  1.00  30.34 ? 305 CIT B O5  1 
HETATM 4346 O  O6  . CIT G 6 .   ? -0.958  -2.430  -0.748  1.00  23.53 ? 305 CIT B O6  1 
HETATM 4347 C  C1  . PEG H 4 .   ? -9.743  -10.622 -7.764  1.00  28.31 ? 306 PEG B C1  1 
HETATM 4348 O  O1  . PEG H 4 .   ? -9.969  -9.219  -7.807  1.00  28.99 ? 306 PEG B O1  1 
HETATM 4349 C  C2  . PEG H 4 .   ? -8.467  -11.043 -7.095  1.00  34.23 ? 306 PEG B C2  1 
HETATM 4350 O  O2  . PEG H 4 .   ? -8.645  -12.453 -6.841  1.00  47.85 ? 306 PEG B O2  1 
HETATM 4351 C  C3  . PEG H 4 .   ? -7.644  -13.081 -6.018  1.00  45.05 ? 306 PEG B C3  1 
HETATM 4352 C  C4  . PEG H 4 .   ? -7.787  -12.561 -4.602  1.00  37.03 ? 306 PEG B C4  1 
HETATM 4353 O  O4  . PEG H 4 .   ? -6.539  -12.138 -4.080  1.00  47.80 ? 306 PEG B O4  1 
HETATM 4354 C  C1  . EDO I 7 .   ? -17.774 -26.844 11.582  1.00  28.84 ? 307 EDO B C1  1 
HETATM 4355 O  O1  . EDO I 7 .   ? -17.796 -28.285 11.764  1.00  29.45 ? 307 EDO B O1  1 
HETATM 4356 C  C2  . EDO I 7 .   ? -18.204 -26.630 10.135  1.00  29.38 ? 307 EDO B C2  1 
HETATM 4357 O  O2  . EDO I 7 .   ? -17.054 -26.861 9.286   1.00  29.83 ? 307 EDO B O2  1 
HETATM 4358 C  C1  . CIT J 6 .   ? 8.421   -27.308 7.133   1.00  49.25 ? 308 CIT B C1  1 
HETATM 4359 O  O1  . CIT J 6 .   ? 9.063   -28.458 7.129   1.00  38.75 ? 308 CIT B O1  1 
HETATM 4360 O  O2  . CIT J 6 .   ? 8.178   -26.718 8.258   1.00  45.10 ? 308 CIT B O2  1 
HETATM 4361 C  C2  . CIT J 6 .   ? 8.034   -26.488 5.851   1.00  33.91 ? 308 CIT B C2  1 
HETATM 4362 C  C3  . CIT J 6 .   ? 6.978   -26.683 4.702   1.00  44.88 ? 308 CIT B C3  1 
HETATM 4363 O  O7  . CIT J 6 .   ? 7.601   -25.811 3.836   1.00  39.51 ? 308 CIT B O7  1 
HETATM 4364 C  C4  . CIT J 6 .   ? 6.839   -27.957 3.824   1.00  38.68 ? 308 CIT B C4  1 
HETATM 4365 C  C5  . CIT J 6 .   ? 5.896   -27.976 2.581   1.00  49.89 ? 308 CIT B C5  1 
HETATM 4366 O  O3  . CIT J 6 .   ? 6.280   -28.065 1.353   1.00  29.12 ? 308 CIT B O3  1 
HETATM 4367 O  O4  . CIT J 6 .   ? 4.655   -27.949 2.811   1.00  55.92 ? 308 CIT B O4  1 
HETATM 4368 C  C6  . CIT J 6 .   ? 5.681   -25.879 4.930   1.00  46.73 ? 308 CIT B C6  1 
HETATM 4369 O  O5  . CIT J 6 .   ? 4.481   -26.324 4.834   1.00  37.94 ? 308 CIT B O5  1 
HETATM 4370 O  O6  . CIT J 6 .   ? 5.889   -24.664 5.215   1.00  63.58 ? 308 CIT B O6  1 
HETATM 4371 C  C1  . EDO K 7 .   ? -23.220 -12.910 4.304   1.00  32.88 ? 309 EDO B C1  1 
HETATM 4372 O  O1  . EDO K 7 .   ? -22.666 -13.735 5.355   1.00  39.20 ? 309 EDO B O1  1 
HETATM 4373 C  C2  . EDO K 7 .   ? -24.699 -13.158 4.133   1.00  35.21 ? 309 EDO B C2  1 
HETATM 4374 O  O2  . EDO K 7 .   ? -24.909 -14.345 3.374   1.00  31.33 ? 309 EDO B O2  1 
HETATM 4375 ZN ZN  . ZN  L 2 .   ? -34.654 -35.988 27.084  1.00  8.49  ? 301 ZN  A ZN  1 
HETATM 4376 CL CL  . EWW M 3 .   ? -34.380 -36.940 21.172  1.00  21.66 ? 302 EWW A CL  1 
HETATM 4377 C  C3  . EWW M 3 .   ? -35.937 -36.774 21.954  1.00  25.42 ? 302 EWW A C3  1 
HETATM 4378 C  C4  . EWW M 3 .   ? -36.078 -36.893 23.344  1.00  21.36 ? 302 EWW A C4  1 
HETATM 4379 S  S6  . EWW M 3 .   ? -34.678 -37.341 24.394  1.00  16.64 ? 302 EWW A S6  1 
HETATM 4380 O  O8  . EWW M 3 .   ? -33.817 -36.186 24.422  1.00  13.50 ? 302 EWW A O8  1 
HETATM 4381 N  N11 . EWW M 3 .   ? -35.308 -37.412 26.118  1.00  15.87 ? 302 EWW A N11 1 
HETATM 4382 O  O7  . EWW M 3 .   ? -34.142 -38.779 23.903  1.00  18.79 ? 302 EWW A O7  1 
HETATM 4383 C  C5  . EWW M 3 .   ? -37.309 -36.770 23.966  1.00  26.11 ? 302 EWW A C5  1 
HETATM 4384 C  C2  . EWW M 3 .   ? -37.037 -36.489 21.157  1.00  30.22 ? 302 EWW A C2  1 
HETATM 4385 C  C22 . EWW M 3 .   ? -38.291 -36.314 21.759  1.00  36.47 ? 302 EWW A C22 1 
HETATM 4386 C  C1  . EWW M 3 .   ? -38.423 -36.504 23.140  1.00  31.25 ? 302 EWW A C1  1 
HETATM 4387 C  C9  . EWW M 3 .   ? -39.449 -36.012 20.867  1.00  50.45 ? 302 EWW A C9  1 
HETATM 4388 O  O12 . EWW M 3 .   ? -40.472 -35.421 21.223  1.00  64.43 ? 302 EWW A O12 1 
HETATM 4389 C  C10 . EWW M 3 .   ? -39.339 -36.453 19.456  1.00  50.07 ? 302 EWW A C10 1 
HETATM 4390 S  S13 . EWW M 3 .   ? -40.072 -38.096 19.378  1.00  83.24 ? 302 EWW A S13 1 
HETATM 4391 C  C14 . EWW M 3 .   ? -41.098 -37.780 17.951  1.00  77.46 ? 302 EWW A C14 1 
HETATM 4392 N  N17 . EWW M 3 .   ? -40.986 -38.629 16.894  1.00  68.03 ? 302 EWW A N17 1 
HETATM 4393 C  C18 . EWW M 3 .   ? -41.769 -38.416 15.800  1.00  75.06 ? 302 EWW A C18 1 
HETATM 4394 O  O21 . EWW M 3 .   ? -41.664 -39.180 14.868  1.00  81.86 ? 302 EWW A O21 1 
HETATM 4395 C  C19 . EWW M 3 .   ? -42.686 -37.345 15.754  1.00  84.65 ? 302 EWW A C19 1 
HETATM 4396 C  C16 . EWW M 3 .   ? -42.783 -36.467 16.849  1.00  88.70 ? 302 EWW A C16 1 
HETATM 4397 N  N15 . EWW M 3 .   ? -41.978 -36.712 17.932  1.00  90.96 ? 302 EWW A N15 1 
HETATM 4398 C  C20 . EWW M 3 .   ? -43.733 -35.310 16.842  1.00  81.02 ? 302 EWW A C20 1 
HETATM 4399 NI NI  . NI  N 8 .   ? -37.062 -40.347 41.347  1.00  67.68 ? 303 NI  A NI  1 
HETATM 4400 O  O   . HOH O 9 .   ? -2.145  -2.113  10.782  1.00  11.68 ? 401 HOH B O   1 
HETATM 4401 O  O   . HOH O 9 .   ? -5.769  1.538   -5.138  1.00  10.87 ? 402 HOH B O   1 
HETATM 4402 O  O   . HOH O 9 .   ? -6.611  -5.817  -0.810  1.00  7.68  ? 403 HOH B O   1 
HETATM 4403 O  O   . HOH O 9 .   ? -22.738 -19.449 18.849  1.00  11.65 ? 404 HOH B O   1 
HETATM 4404 O  O   . HOH O 9 .   ? -2.010  -13.988 24.711  1.00  11.92 ? 405 HOH B O   1 
HETATM 4405 O  O   . HOH O 9 .   ? -5.899  -20.037 6.110   1.00  15.35 ? 406 HOH B O   1 
HETATM 4406 O  O   . HOH O 9 .   ? -26.729 -12.701 21.114  1.00  13.18 ? 407 HOH B O   1 
HETATM 4407 O  O   . HOH O 9 .   ? -13.598 -23.306 17.460  1.00  11.94 ? 408 HOH B O   1 
HETATM 4408 O  O   . HOH O 9 .   ? -20.929 -5.388  23.026  1.00  13.91 ? 409 HOH B O   1 
HETATM 4409 O  O   . HOH O 9 .   ? -18.101 -23.720 18.491  1.00  11.00 ? 410 HOH B O   1 
HETATM 4410 O  O   . HOH O 9 .   ? 0.088   -19.898 21.836  1.00  12.26 ? 411 HOH B O   1 
HETATM 4411 O  O   . HOH O 9 .   ? -0.601  -11.864 25.774  1.00  12.07 ? 412 HOH B O   1 
HETATM 4412 O  O   . HOH O 9 .   ? -11.693 -21.812 10.383  1.00  10.90 ? 413 HOH B O   1 
HETATM 4413 O  O   . HOH O 9 .   ? -0.954  -0.757  -6.339  1.00  11.80 ? 414 HOH B O   1 
HETATM 4414 O  O   . HOH O 9 .   ? -4.197  6.095   7.942   1.00  15.70 ? 415 HOH B O   1 
HETATM 4415 O  O   . HOH O 9 .   ? -10.477 -16.546 8.379   1.00  7.59  ? 416 HOH B O   1 
HETATM 4416 O  O   . HOH O 9 .   ? -1.733  -16.697 24.615  1.00  13.23 ? 417 HOH B O   1 
HETATM 4417 O  O   . HOH O 9 .   ? 6.306   -13.489 11.283  1.00  17.90 ? 418 HOH B O   1 
HETATM 4418 O  O   . HOH O 9 .   ? 5.826   -1.844  11.717  1.00  16.75 ? 419 HOH B O   1 
HETATM 4419 O  O   . HOH O 9 .   ? -7.331  -15.322 28.768  1.00  11.14 ? 420 HOH B O   1 
HETATM 4420 O  O   . HOH O 9 .   ? -20.458 -20.696 11.243  1.00  18.11 ? 421 HOH B O   1 
HETATM 4421 O  O   . HOH O 9 .   ? -5.575  -15.751 26.601  1.00  12.36 ? 422 HOH B O   1 
HETATM 4422 O  O   . HOH O 9 .   ? -25.399 -14.711 19.366  1.00  13.63 ? 423 HOH B O   1 
HETATM 4423 O  O   . HOH O 9 .   ? -5.022  -11.323 26.120  1.00  13.06 ? 424 HOH B O   1 
HETATM 4424 O  O   . HOH O 9 .   ? -19.898 -16.848 24.461  1.00  18.59 ? 425 HOH B O   1 
HETATM 4425 O  O   . HOH O 9 .   ? -15.971 -5.371  34.780  1.00  17.21 ? 426 HOH B O   1 
HETATM 4426 O  O   . HOH O 9 .   ? -2.350  -18.359 22.453  1.00  11.67 ? 427 HOH B O   1 
HETATM 4427 O  O   . HOH O 9 .   ? -9.574  -0.395  -6.253  1.00  13.78 ? 428 HOH B O   1 
HETATM 4428 O  O   . HOH O 9 .   ? 1.245   -8.345  6.774   1.00  15.46 ? 429 HOH B O   1 
HETATM 4429 O  O   . HOH O 9 .   ? -4.346  -20.456 26.436  1.00  16.78 ? 430 HOH B O   1 
HETATM 4430 O  O   . HOH O 9 .   ? -24.807 -11.693 15.497  1.00  15.11 ? 431 HOH B O   1 
HETATM 4431 O  O   . HOH O 9 .   ? -19.669 -14.361 5.561   1.00  17.15 ? 432 HOH B O   1 
HETATM 4432 O  O   . HOH O 9 .   ? 1.243   -21.768 0.729   1.00  17.94 ? 433 HOH B O   1 
HETATM 4433 O  O   . HOH O 9 .   ? 1.737   -19.400 23.995  1.00  15.85 ? 434 HOH B O   1 
HETATM 4434 O  O   . HOH O 9 .   ? -26.944 -14.295 17.121  1.00  15.65 ? 435 HOH B O   1 
HETATM 4435 O  O   . HOH O 9 .   ? -5.905  0.435   10.476  1.00  14.77 ? 436 HOH B O   1 
HETATM 4436 O  O   . HOH O 9 .   ? -1.758  -4.947  -2.136  1.00  14.98 ? 437 HOH B O   1 
HETATM 4437 O  O   . HOH O 9 .   ? -17.335 -10.335 28.815  1.00  11.33 ? 438 HOH B O   1 
HETATM 4438 O  O   . HOH O 9 .   ? -2.778  3.885   2.174   1.00  15.23 ? 439 HOH B O   1 
HETATM 4439 O  O   . HOH O 9 .   ? -22.087 -6.663  25.140  1.00  18.21 ? 440 HOH B O   1 
HETATM 4440 O  O   . HOH O 9 .   ? -3.269  6.239   3.353   1.00  19.62 ? 441 HOH B O   1 
HETATM 4441 O  O   . HOH O 9 .   ? -21.460 -18.135 10.978  1.00  14.84 ? 442 HOH B O   1 
HETATM 4442 O  O   . HOH O 9 .   ? 0.528   -17.624 25.716  1.00  16.55 ? 443 HOH B O   1 
HETATM 4443 O  O   . HOH O 9 .   ? -13.376 -18.539 28.300  1.00  14.11 ? 444 HOH B O   1 
HETATM 4444 O  O   . HOH O 9 .   ? -10.760 -21.595 27.052  1.00  17.22 ? 445 HOH B O   1 
HETATM 4445 O  O   . HOH O 9 .   ? -5.714  9.499   9.595   1.00  17.06 ? 446 HOH B O   1 
HETATM 4446 O  O   . HOH O 9 .   ? -16.189 -23.737 24.076  1.00  14.41 ? 447 HOH B O   1 
HETATM 4447 O  O   . HOH O 9 .   ? -21.627 -0.650  34.805  1.00  14.94 ? 448 HOH B O   1 
HETATM 4448 O  O   . HOH O 9 .   ? 5.616   -22.335 4.298   1.00  17.07 ? 449 HOH B O   1 
HETATM 4449 O  O   . HOH O 9 .   ? 1.181   -10.294 24.245  1.00  13.01 ? 450 HOH B O   1 
HETATM 4450 O  O   . HOH O 9 .   ? -0.494  -0.794  4.160   1.00  15.13 ? 451 HOH B O   1 
HETATM 4451 O  O   . HOH O 9 .   ? 4.147   -15.618 -0.968  1.00  16.68 ? 452 HOH B O   1 
HETATM 4452 O  O   . HOH O 9 .   ? -15.193 -25.420 14.099  1.00  18.12 ? 453 HOH B O   1 
HETATM 4453 O  O   . HOH O 9 .   ? -17.693 -17.038 -3.233  1.00  19.36 ? 454 HOH B O   1 
HETATM 4454 O  O   . HOH O 9 .   ? -2.613  6.702   5.832   1.00  16.37 ? 455 HOH B O   1 
HETATM 4455 O  O   . HOH O 9 .   ? 8.424   0.514   12.884  1.00  21.69 ? 456 HOH B O   1 
HETATM 4456 O  O   . HOH O 9 .   ? -3.634  -25.978 8.322   1.00  14.94 ? 457 HOH B O   1 
HETATM 4457 O  O   . HOH O 9 .   ? -0.521  -8.871  2.918   1.00  18.76 ? 458 HOH B O   1 
HETATM 4458 O  O   . HOH O 9 .   ? -11.016 -4.870  -5.013  1.00  16.70 ? 459 HOH B O   1 
HETATM 4459 O  O   . HOH O 9 .   ? -5.436  -15.513 30.816  1.00  18.37 ? 460 HOH B O   1 
HETATM 4460 O  O   . HOH O 9 .   ? 7.836   -22.174 5.785   1.00  12.99 ? 461 HOH B O   1 
HETATM 4461 O  O   . HOH O 9 .   ? 2.857   -3.231  25.647  1.00  17.16 ? 462 HOH B O   1 
HETATM 4462 O  O   . HOH O 9 .   ? 7.714   -9.384  17.856  1.00  15.10 ? 463 HOH B O   1 
HETATM 4463 O  O   . HOH O 9 .   ? -11.735 -25.399 16.910  1.00  18.90 ? 464 HOH B O   1 
HETATM 4464 O  O   . HOH O 9 .   ? 3.338   1.932   22.946  1.00  19.88 ? 465 HOH B O   1 
HETATM 4465 O  O   . HOH O 9 .   ? -17.776 -9.752  32.943  1.00  19.94 ? 466 HOH B O   1 
HETATM 4466 O  O   . HOH O 9 .   ? 2.316   -2.923  4.651   1.00  22.81 ? 467 HOH B O   1 
HETATM 4467 O  O   . HOH O 9 .   ? -21.625 3.884   -0.070  1.00  19.65 ? 468 HOH B O   1 
HETATM 4468 O  O   . HOH O 9 .   ? -10.892 -24.248 8.734   1.00  14.66 ? 469 HOH B O   1 
HETATM 4469 O  O   . HOH O 9 .   ? 2.091   -8.097  4.206   1.00  16.05 ? 470 HOH B O   1 
HETATM 4470 O  O   . HOH O 9 .   ? 7.467   -24.234 7.694   1.00  16.97 ? 471 HOH B O   1 
HETATM 4471 O  O   . HOH O 9 .   ? -5.051  -22.444 5.150   1.00  21.84 ? 472 HOH B O   1 
HETATM 4472 O  O   . HOH O 9 .   ? -3.788  -17.791 26.277  1.00  17.08 ? 473 HOH B O   1 
HETATM 4473 O  O   . HOH O 9 .   ? -23.571 6.049   2.366   1.00  20.91 ? 474 HOH B O   1 
HETATM 4474 O  O   . HOH O 9 .   ? 9.895   -14.892 12.633  1.00  22.25 ? 475 HOH B O   1 
HETATM 4475 O  O   . HOH O 9 .   ? 2.730   -8.945  26.823  1.00  22.22 ? 476 HOH B O   1 
HETATM 4476 O  O   . HOH O 9 .   ? -12.947 -27.828 8.054   1.00  28.81 ? 477 HOH B O   1 
HETATM 4477 O  O   . HOH O 9 .   ? 5.415   -8.736  25.827  1.00  22.83 ? 478 HOH B O   1 
HETATM 4478 O  O   . HOH O 9 .   ? -6.071  -18.663 29.216  1.00  20.38 ? 479 HOH B O   1 
HETATM 4479 O  O   . HOH O 9 .   ? 4.165   -18.358 23.108  1.00  17.70 ? 480 HOH B O   1 
HETATM 4480 O  O   . HOH O 9 .   ? -10.827 -27.108 19.029  1.00  18.44 ? 481 HOH B O   1 
HETATM 4481 O  O   . HOH O 9 .   ? 0.756   -22.067 -1.804  1.00  24.48 ? 482 HOH B O   1 
HETATM 4482 O  O   . HOH O 9 .   ? -9.458  2.643   13.140  1.00  21.99 ? 483 HOH B O   1 
HETATM 4483 O  O   . HOH O 9 .   ? -21.067 -19.334 7.569   1.00  19.06 ? 484 HOH B O   1 
HETATM 4484 O  O   . HOH O 9 .   ? -6.390  -14.062 32.903  1.00  22.44 ? 485 HOH B O   1 
HETATM 4485 O  O   . HOH O 9 .   ? -17.746 4.080   15.033  1.00  24.38 ? 486 HOH B O   1 
HETATM 4486 O  O   . HOH O 9 .   ? -28.655 -10.327 24.248  1.00  23.91 ? 487 HOH B O   1 
HETATM 4487 O  O   . HOH O 9 .   ? 5.031   -4.888  26.501  1.00  20.09 ? 488 HOH B O   1 
HETATM 4488 O  O   . HOH O 9 .   ? 3.366   -5.672  4.030   1.00  22.07 ? 489 HOH B O   1 
HETATM 4489 O  O   . HOH O 9 .   ? 4.265   -19.491 12.386  1.00  22.76 ? 490 HOH B O   1 
HETATM 4490 O  O   . HOH O 9 .   ? 7.297   -21.298 15.292  1.00  24.73 ? 491 HOH B O   1 
HETATM 4491 O  O   . HOH O 9 .   ? -24.100 -4.281  26.314  1.00  23.06 ? 492 HOH B O   1 
HETATM 4492 O  O   . HOH O 9 .   ? 8.802   -5.902  15.312  1.00  18.09 ? 493 HOH B O   1 
HETATM 4493 O  O   . HOH O 9 .   ? 6.182   1.781   5.935   1.00  22.87 ? 494 HOH B O   1 
HETATM 4494 O  O   . HOH O 9 .   ? -15.787 -25.441 6.525   1.00  30.56 ? 495 HOH B O   1 
HETATM 4495 O  O   . HOH O 9 .   ? -20.072 -13.516 30.196  1.00  21.26 ? 496 HOH B O   1 
HETATM 4496 O  O   . HOH O 9 .   ? 7.331   -3.240  9.961   1.00  22.70 ? 497 HOH B O   1 
HETATM 4497 O  O   . HOH O 9 .   ? 8.313   -6.904  24.268  1.00  21.38 ? 498 HOH B O   1 
HETATM 4498 O  O   . HOH O 9 .   ? 6.049   2.271   22.315  1.00  19.61 ? 499 HOH B O   1 
HETATM 4499 O  O   . HOH O 9 .   ? 10.381  -7.292  16.864  1.00  25.43 ? 500 HOH B O   1 
HETATM 4500 O  O   . HOH O 9 .   ? 8.912   -13.515 22.094  1.00  22.95 ? 501 HOH B O   1 
HETATM 4501 O  O   . HOH O 9 .   ? 7.071   -20.347 12.905  1.00  26.37 ? 502 HOH B O   1 
HETATM 4502 O  O   . HOH O 9 .   ? 8.677   -15.608 8.416   1.00  27.22 ? 503 HOH B O   1 
HETATM 4503 O  O   . HOH O 9 .   ? 12.660  -18.637 7.543   1.00  18.92 ? 504 HOH B O   1 
HETATM 4504 O  O   . HOH O 9 .   ? -2.166  -25.758 11.154  1.00  19.76 ? 505 HOH B O   1 
HETATM 4505 O  O   . HOH O 9 .   ? -3.365  -24.235 5.957   1.00  24.13 ? 506 HOH B O   1 
HETATM 4506 O  O   . HOH O 9 .   ? -0.902  -23.639 4.406   1.00  25.65 ? 507 HOH B O   1 
HETATM 4507 O  O   . HOH O 9 .   ? -1.411  -21.359 2.750   1.00  24.37 ? 508 HOH B O   1 
HETATM 4508 O  O   . HOH O 9 .   ? 5.022   -22.167 16.818  1.00  25.96 ? 509 HOH B O   1 
HETATM 4509 O  O   . HOH O 9 .   ? 11.611  -25.056 12.166  1.00  31.90 ? 510 HOH B O   1 
HETATM 4510 O  O   . HOH O 9 .   ? -2.895  -28.110 12.757  1.00  21.65 ? 511 HOH B O   1 
HETATM 4511 O  O   . HOH O 9 .   ? -9.002  -31.700 14.445  1.00  27.84 ? 512 HOH B O   1 
HETATM 4512 O  O   . HOH O 9 .   ? -1.877  -31.618 22.562  1.00  28.85 ? 513 HOH B O   1 
HETATM 4513 O  O   . HOH O 9 .   ? -1.001  -25.724 26.647  1.00  24.90 ? 514 HOH B O   1 
HETATM 4514 O  O   . HOH O 9 .   ? -8.065  -28.494 20.874  1.00  24.95 ? 515 HOH B O   1 
HETATM 4515 O  O   . HOH O 9 .   ? -24.635 -4.519  23.553  1.00  21.79 ? 516 HOH B O   1 
HETATM 4516 O  O   . HOH O 9 .   ? -20.883 -0.684  32.278  1.00  22.94 ? 517 HOH B O   1 
HETATM 4517 O  O   . HOH O 9 .   ? -18.428 -1.951  31.716  1.00  31.61 ? 518 HOH B O   1 
HETATM 4518 O  O   . HOH O 9 .   ? -16.311 2.645   31.844  1.00  28.74 ? 519 HOH B O   1 
HETATM 4519 O  O   . HOH O 9 .   ? -21.156 2.209   31.730  1.00  24.32 ? 520 HOH B O   1 
HETATM 4520 O  O   . HOH O 9 .   ? -18.837 3.704   32.224  1.00  22.95 ? 521 HOH B O   1 
HETATM 4521 O  O   . HOH O 9 .   ? -19.137 -4.245  33.278  1.00  22.89 ? 522 HOH B O   1 
HETATM 4522 O  O   . HOH O 9 .   ? -17.108 -2.823  34.160  1.00  16.83 ? 523 HOH B O   1 
HETATM 4523 O  O   . HOH O 9 .   ? -24.170 -6.306  16.330  1.00  22.84 ? 524 HOH B O   1 
HETATM 4524 O  O   . HOH O 9 .   ? -19.049 5.274   19.212  1.00  29.59 ? 525 HOH B O   1 
HETATM 4525 O  O   . HOH O 9 .   ? -15.267 1.456   20.179  1.00  29.73 ? 526 HOH B O   1 
HETATM 4526 O  O   . HOH O 9 .   ? -17.634 0.646   21.456  1.00  25.64 ? 527 HOH B O   1 
HETATM 4527 O  O   . HOH O 9 .   ? -2.895  9.151   12.819  1.00  22.51 ? 528 HOH B O   1 
HETATM 4528 O  O   . HOH O 9 .   ? -19.841 1.458   24.678  1.00  27.12 ? 529 HOH B O   1 
HETATM 4529 O  O   . HOH O 9 .   ? -26.944 -3.247  23.013  1.00  27.59 ? 530 HOH B O   1 
HETATM 4530 O  O   . HOH O 9 .   ? -24.808 -8.063  31.128  1.00  33.94 ? 531 HOH B O   1 
HETATM 4531 O  O   . HOH O 9 .   ? -10.574 -14.444 35.086  1.00  27.91 ? 532 HOH B O   1 
HETATM 4532 O  O   . HOH O 9 .   ? -22.685 -11.302 32.699  1.00  22.65 ? 533 HOH B O   1 
HETATM 4533 O  O   . HOH O 9 .   ? -0.256  3.647   1.049   1.00  23.10 ? 534 HOH B O   1 
HETATM 4534 O  O   . HOH O 9 .   ? -0.747  5.862   -0.947  1.00  27.36 ? 535 HOH B O   1 
HETATM 4535 O  O   . HOH O 9 .   ? -8.990  -13.635 -3.097  1.00  22.61 ? 536 HOH B O   1 
HETATM 4536 O  O   . HOH O 9 .   ? -7.476  -14.046 -1.085  1.00  20.18 ? 537 HOH B O   1 
HETATM 4537 O  O   . HOH O 9 .   ? 2.028   -12.943 0.719   1.00  23.28 ? 538 HOH B O   1 
HETATM 4538 O  O   . HOH O 9 .   ? -16.808 -19.047 4.314   1.00  24.60 ? 539 HOH B O   1 
HETATM 4539 O  O   . HOH O 9 .   ? -17.421 -24.704 4.174   1.00  24.28 ? 540 HOH B O   1 
HETATM 4540 O  O   . HOH O 9 .   ? -15.019 -11.250 37.760  1.00  27.38 ? 541 HOH B O   1 
HETATM 4541 O  O   . HOH O 9 .   ? -9.376  -8.793  39.453  1.00  32.79 ? 542 HOH B O   1 
HETATM 4542 O  O   . HOH O 9 .   ? -13.196 -11.609 40.432  1.00  22.95 ? 543 HOH B O   1 
HETATM 4543 O  O   . HOH O 9 .   ? -9.478  2.520   36.384  1.00  31.84 ? 544 HOH B O   1 
HETATM 4544 O  O   . HOH O 9 .   ? -4.254  0.361   37.672  1.00  45.23 ? 545 HOH B O   1 
HETATM 4545 O  O   . HOH O 9 .   ? -4.756  -2.009  33.629  1.00  22.83 ? 546 HOH B O   1 
HETATM 4546 O  O   . HOH O 9 .   ? 2.012   -15.750 26.930  1.00  21.31 ? 547 HOH B O   1 
HETATM 4547 O  O   . HOH O 9 .   ? 0.308   -5.728  28.315  1.00  20.40 ? 548 HOH B O   1 
HETATM 4548 O  O   . HOH O 9 .   ? -16.408 -0.595  -6.164  1.00  18.52 ? 549 HOH B O   1 
HETATM 4549 O  O   . HOH O 9 .   ? -11.023 -0.327  -8.755  1.00  25.32 ? 550 HOH B O   1 
HETATM 4550 O  O   . HOH O 9 .   ? -28.518 0.537   10.761  1.00  21.98 ? 551 HOH B O   1 
HETATM 4551 O  O   . HOH O 9 .   ? -24.867 14.935  12.654  1.00  32.61 ? 552 HOH B O   1 
HETATM 4552 O  O   . HOH O 9 .   ? -14.021 8.865   -1.929  1.00  30.88 ? 553 HOH B O   1 
HETATM 4553 O  O   . HOH O 9 .   ? -13.432 13.924  14.871  1.00  36.59 ? 554 HOH B O   1 
HETATM 4554 O  O   . HOH O 9 .   ? -22.158 10.753  8.301   1.00  30.06 ? 555 HOH B O   1 
HETATM 4555 O  O   . HOH O 9 .   ? -31.517 -3.979  15.706  1.00  32.05 ? 556 HOH B O   1 
HETATM 4556 O  O   . HOH O 9 .   ? -23.491 -18.226 8.210   1.00  19.23 ? 557 HOH B O   1 
HETATM 4557 O  O   . HOH O 9 .   ? -10.647 -26.741 9.894   1.00  28.43 ? 558 HOH B O   1 
HETATM 4558 O  O   . HOH O 9 .   ? -11.067 -24.783 6.224   1.00  21.64 ? 559 HOH B O   1 
HETATM 4559 O  O   . HOH O 9 .   ? -1.812  9.304   6.495   1.00  26.67 ? 560 HOH B O   1 
HETATM 4560 O  O   . HOH O 9 .   ? -9.454  15.564  3.059   1.00  22.03 ? 561 HOH B O   1 
HETATM 4561 O  O   . HOH O 9 .   ? 6.073   -5.835  3.800   1.00  36.20 ? 562 HOH B O   1 
HETATM 4562 O  O   . HOH O 9 .   ? 8.665   -19.782 17.547  1.00  22.97 ? 563 HOH B O   1 
HETATM 4563 O  O   . HOH O 9 .   ? 10.638  -17.702 16.703  1.00  22.43 ? 564 HOH B O   1 
HETATM 4564 O  O   . HOH O 9 .   ? 11.898  -14.379 15.388  1.00  27.16 ? 565 HOH B O   1 
HETATM 4565 O  O   . HOH O 9 .   ? 4.072   -9.781  3.221   1.00  33.28 ? 566 HOH B O   1 
HETATM 4566 O  O   . HOH O 9 .   ? 8.650   -4.939  7.529   1.00  32.59 ? 567 HOH B O   1 
HETATM 4567 O  O   . HOH O 9 .   ? -12.551 -19.446 31.915  1.00  29.01 ? 568 HOH B O   1 
HETATM 4568 O  O   . HOH O 9 .   ? -8.879  -22.978 28.771  1.00  31.03 ? 569 HOH B O   1 
HETATM 4569 O  O   . HOH O 9 .   ? -16.788 -15.806 33.070  1.00  31.47 ? 570 HOH B O   1 
HETATM 4570 O  O   . HOH O 9 .   ? -13.259 -15.262 34.729  1.00  30.79 ? 571 HOH B O   1 
HETATM 4571 O  O   . HOH O 9 .   ? -18.984 -21.030 26.893  1.00  20.44 ? 572 HOH B O   1 
HETATM 4572 O  O   . HOH O 9 .   ? -13.653 4.382   26.528  1.00  40.64 ? 573 HOH B O   1 
HETATM 4573 O  O   . HOH O 9 .   ? -13.449 -17.489 -4.173  1.00  39.27 ? 574 HOH B O   1 
HETATM 4574 O  O   . HOH O 9 .   ? -14.019 -20.553 2.545   1.00  27.36 ? 575 HOH B O   1 
HETATM 4575 O  O   . HOH O 9 .   ? -18.783 -17.441 4.458   1.00  28.06 ? 576 HOH B O   1 
HETATM 4576 O  O   . HOH O 9 .   ? -18.381 2.989   22.495  1.00  37.54 ? 577 HOH B O   1 
HETATM 4577 O  O   . HOH O 9 .   ? -21.975 3.997   29.553  1.00  26.88 ? 578 HOH B O   1 
HETATM 4578 O  O   . HOH O 9 .   ? -14.811 8.402   24.782  1.00  43.80 ? 579 HOH B O   1 
HETATM 4579 O  O   . HOH O 9 .   ? -14.496 10.626  23.328  1.00  30.59 ? 580 HOH B O   1 
HETATM 4580 O  O   . HOH O 9 .   ? -14.261 10.650  20.381  1.00  38.72 ? 581 HOH B O   1 
HETATM 4581 O  O   . HOH O 9 .   ? -3.047  8.838   9.301   1.00  29.76 ? 582 HOH B O   1 
HETATM 4582 O  O   . HOH O 9 .   ? 9.604   -1.720  13.469  1.00  34.01 ? 583 HOH B O   1 
HETATM 4583 O  O   . HOH O 9 .   ? 14.303  -11.921 15.286  1.00  40.99 ? 584 HOH B O   1 
HETATM 4584 O  O   . HOH O 9 .   ? 13.092  -18.454 17.301  1.00  23.63 ? 585 HOH B O   1 
HETATM 4585 O  O   . HOH O 9 .   ? 0.667   -3.084  27.402  1.00  25.85 ? 586 HOH B O   1 
HETATM 4586 O  O   . HOH O 9 .   ? 13.087  -6.211  16.524  1.00  43.34 ? 587 HOH B O   1 
HETATM 4587 O  O   . HOH O 9 .   ? 1.818   -28.722 12.385  1.00  36.83 ? 588 HOH B O   1 
HETATM 4588 O  O   . HOH O 9 .   ? 4.714   -24.635 7.124   1.00  16.02 ? 589 HOH B O   1 
HETATM 4589 O  O   . HOH O 9 .   ? -13.198 -23.631 32.604  1.00  32.43 ? 590 HOH B O   1 
HETATM 4590 O  O   . HOH O 9 .   ? -28.496 -12.622 9.316   1.00  31.20 ? 591 HOH B O   1 
HETATM 4591 O  O   . HOH O 9 .   ? -20.962 9.014   19.280  1.00  33.55 ? 592 HOH B O   1 
HETATM 4592 O  O   . HOH O 9 .   ? -21.606 12.516  15.773  1.00  32.15 ? 593 HOH B O   1 
HETATM 4593 O  O   . HOH O 9 .   ? -18.719 7.927   18.314  1.00  41.02 ? 594 HOH B O   1 
HETATM 4594 O  O   . HOH O 9 .   ? -23.379 -13.671 28.449  1.00  41.99 ? 595 HOH B O   1 
HETATM 4595 O  O   . HOH O 9 .   ? -4.717  -24.006 26.306  1.00  23.21 ? 596 HOH B O   1 
HETATM 4596 O  O   . HOH O 9 .   ? -12.008 -28.127 28.051  1.00  30.41 ? 597 HOH B O   1 
HETATM 4597 O  O   . HOH O 9 .   ? -11.106 -29.217 23.202  1.00  32.63 ? 598 HOH B O   1 
HETATM 4598 O  O   . HOH O 9 .   ? -7.980  -33.332 26.010  1.00  32.14 ? 599 HOH B O   1 
HETATM 4599 O  O   . HOH O 9 .   ? 0.914   -26.189 1.342   1.00  31.80 ? 600 HOH B O   1 
HETATM 4600 O  O   . HOH O 9 .   ? 4.966   -12.558 1.975   1.00  32.04 ? 601 HOH B O   1 
HETATM 4601 O  O   . HOH O 9 .   ? -8.467  -27.934 8.444   1.00  21.53 ? 602 HOH B O   1 
HETATM 4602 O  O   . HOH O 9 .   ? -14.433 -27.595 10.311  1.00  22.69 ? 603 HOH B O   1 
HETATM 4603 O  O   . HOH O 9 .   ? -11.125 3.079   32.979  1.00  25.02 ? 604 HOH B O   1 
HETATM 4604 O  O   . HOH O 9 .   ? 2.536   0.994   27.499  1.00  32.32 ? 605 HOH B O   1 
HETATM 4605 O  O   . HOH O 9 .   ? 1.609   -13.172 27.087  1.00  31.84 ? 606 HOH B O   1 
HETATM 4606 O  O   . HOH O 9 .   ? -28.976 -9.565  9.413   1.00  44.50 ? 607 HOH B O   1 
HETATM 4607 O  O   . HOH O 9 .   ? -21.313 1.895   -4.891  1.00  38.76 ? 608 HOH B O   1 
HETATM 4608 O  O   . HOH O 9 .   ? 7.450   2.922   24.735  1.00  28.06 ? 609 HOH B O   1 
HETATM 4609 O  O   . HOH O 9 .   ? 3.937   -0.468  25.333  1.00  23.81 ? 610 HOH B O   1 
HETATM 4610 O  O   . HOH O 9 .   ? -13.625 -4.771  -9.583  1.00  30.12 ? 611 HOH B O   1 
HETATM 4611 O  O   . HOH O 9 .   ? -15.015 -1.242  -8.371  1.00  29.83 ? 612 HOH B O   1 
HETATM 4612 O  O   . HOH O 9 .   ? -16.309 6.792   0.552   1.00  24.02 ? 613 HOH B O   1 
HETATM 4613 O  O   . HOH O 9 .   ? -3.931  9.333   -2.115  1.00  15.89 ? 614 HOH B O   1 
HETATM 4614 O  O   . HOH O 9 .   ? -2.587  7.723   0.234   1.00  29.28 ? 615 HOH B O   1 
HETATM 4615 O  O   . HOH O 9 .   ? -3.494  11.925  -2.724  1.00  28.55 ? 616 HOH B O   1 
HETATM 4616 O  O   . HOH O 9 .   ? 8.810   -22.757 18.871  1.00  34.19 ? 617 HOH B O   1 
HETATM 4617 O  O   . HOH O 9 .   ? 7.903   -18.336 24.094  1.00  27.05 ? 618 HOH B O   1 
HETATM 4618 O  O   . HOH O 9 .   ? -30.693 -7.248  23.262  1.00  30.20 ? 619 HOH B O   1 
HETATM 4619 O  O   . HOH O 9 .   ? -10.697 -30.071 12.109  1.00  36.81 ? 620 HOH B O   1 
HETATM 4620 O  O   . HOH O 9 .   ? -31.308 -8.573  19.783  1.00  29.97 ? 621 HOH B O   1 
HETATM 4621 O  O   . HOH O 9 .   ? -7.689  -22.983 3.755   1.00  28.24 ? 622 HOH B O   1 
HETATM 4622 O  O   . HOH O 9 .   ? -3.747  -21.191 2.676   1.00  38.88 ? 623 HOH B O   1 
HETATM 4623 O  O   . HOH O 9 .   ? -10.263 -22.952 4.313   1.00  29.32 ? 624 HOH B O   1 
HETATM 4624 O  O   . HOH O 9 .   ? -11.632 -22.253 2.273   1.00  32.43 ? 625 HOH B O   1 
HETATM 4625 O  O   . HOH O 9 .   ? -19.716 -16.505 31.262  1.00  32.19 ? 626 HOH B O   1 
HETATM 4626 O  O   . HOH O 9 .   ? -7.372  0.531   13.054  1.00  28.80 ? 627 HOH B O   1 
HETATM 4627 O  O   . HOH O 9 .   ? -8.713  8.669   14.329  1.00  30.20 ? 628 HOH B O   1 
HETATM 4628 O  O   . HOH O 9 .   ? 1.050   9.724   16.429  1.00  37.66 ? 629 HOH B O   1 
HETATM 4629 O  O   . HOH O 9 .   ? 4.996   7.698   12.314  1.00  42.10 ? 630 HOH B O   1 
HETATM 4630 O  O   . HOH O 9 .   ? -7.958  -11.088 -10.014 1.00  33.75 ? 631 HOH B O   1 
HETATM 4631 O  O   . HOH O 9 .   ? -1.005  -8.310  -7.293  1.00  25.84 ? 632 HOH B O   1 
HETATM 4632 O  O   . HOH O 9 .   ? -16.533 0.131   30.850  1.00  40.75 ? 633 HOH B O   1 
HETATM 4633 O  O   . HOH O 9 .   ? -20.966 -19.096 4.827   1.00  28.99 ? 634 HOH B O   1 
HETATM 4634 O  O   . HOH O 9 .   ? -26.467 -0.189  5.153   1.00  27.87 ? 635 HOH B O   1 
HETATM 4635 O  O   . HOH O 9 .   ? -0.942  -14.014 -1.585  1.00  24.38 ? 636 HOH B O   1 
HETATM 4636 O  O   . HOH O 9 .   ? 1.246   -0.827  28.893  1.00  27.52 ? 637 HOH B O   1 
HETATM 4637 O  O   . HOH O 9 .   ? -13.676 8.081   -4.477  1.00  34.67 ? 638 HOH B O   1 
HETATM 4638 O  O   . HOH O 9 .   ? -9.671  3.425   16.507  1.00  37.72 ? 639 HOH B O   1 
HETATM 4639 O  O   . HOH O 9 .   ? -11.033 2.571   18.064  1.00  37.57 ? 640 HOH B O   1 
HETATM 4640 O  O   . HOH O 9 .   ? -3.016  6.269   18.303  1.00  43.91 ? 641 HOH B O   1 
HETATM 4641 O  O   . HOH O 9 .   ? 0.080   3.681   25.791  1.00  47.10 ? 642 HOH B O   1 
HETATM 4642 O  O   . HOH O 9 .   ? -2.753  9.559   15.887  1.00  35.94 ? 643 HOH B O   1 
HETATM 4643 O  O   . HOH O 9 .   ? 2.848   15.434  12.092  1.00  35.59 ? 644 HOH B O   1 
HETATM 4644 O  O   . HOH O 9 .   ? -6.300  14.697  10.634  1.00  35.06 ? 645 HOH B O   1 
HETATM 4645 O  O   . HOH O 9 .   ? -2.656  12.132  10.096  1.00  38.21 ? 646 HOH B O   1 
HETATM 4646 O  O   . HOH O 9 .   ? 0.161   10.941  -0.961  1.00  36.69 ? 647 HOH B O   1 
HETATM 4647 O  O   . HOH O 9 .   ? 12.206  0.301   18.935  1.00  37.27 ? 648 HOH B O   1 
HETATM 4648 O  O   . HOH O 9 .   ? 6.225   -16.175 12.193  1.00  33.26 ? 649 HOH B O   1 
HETATM 4649 O  O   . HOH O 9 .   ? 1.504   -30.466 16.780  1.00  37.48 ? 650 HOH B O   1 
HETATM 4650 O  O   . HOH O 9 .   ? -14.428 -21.929 28.196  1.00  29.60 ? 651 HOH B O   1 
HETATM 4651 O  O   . HOH O 9 .   ? -15.115 -19.501 29.940  1.00  32.92 ? 652 HOH B O   1 
HETATM 4652 O  O   . HOH O 9 .   ? -18.463 1.140   28.091  1.00  36.35 ? 653 HOH B O   1 
HETATM 4653 O  O   . HOH O 9 .   ? -26.314 -2.568  26.429  1.00  34.57 ? 654 HOH B O   1 
HETATM 4654 O  O   . HOH O 9 .   ? -28.692 -5.554  33.212  1.00  36.94 ? 655 HOH B O   1 
HETATM 4655 O  O   . HOH O 9 .   ? -10.363 -15.698 -4.501  1.00  30.81 ? 656 HOH B O   1 
HETATM 4656 O  O   . HOH O 9 .   ? -7.484  -16.599 -1.119  1.00  36.22 ? 657 HOH B O   1 
HETATM 4657 O  O   . HOH O 9 .   ? 5.928   -14.136 -0.155  1.00  31.87 ? 658 HOH B O   1 
HETATM 4658 O  O   . HOH O 9 .   ? -27.714 -10.471 4.613   1.00  40.57 ? 659 HOH B O   1 
HETATM 4659 O  O   . HOH O 9 .   ? -18.362 -11.800 -7.358  1.00  32.03 ? 660 HOH B O   1 
HETATM 4660 O  O   . HOH O 9 .   ? -27.848 -1.497  3.382   1.00  38.26 ? 661 HOH B O   1 
HETATM 4661 O  O   . HOH O 9 .   ? -17.970 13.317  1.223   1.00  45.67 ? 662 HOH B O   1 
HETATM 4662 O  O   . HOH O 9 .   ? -13.269 8.843   14.190  1.00  41.26 ? 663 HOH B O   1 
HETATM 4663 O  O   . HOH O 9 .   ? -12.936 2.692   -4.926  1.00  28.47 ? 664 HOH B O   1 
HETATM 4664 O  O   . HOH O 9 .   ? 9.057   -3.982  12.033  1.00  39.70 ? 665 HOH B O   1 
HETATM 4665 O  O   . HOH O 9 .   ? 5.790   -19.979 24.660  1.00  33.94 ? 666 HOH B O   1 
HETATM 4666 O  O   . HOH O 9 .   ? -7.482  1.657   15.583  1.00  38.24 ? 667 HOH B O   1 
HETATM 4667 O  O   . HOH O 9 .   ? -14.318 4.401   16.825  1.00  37.86 ? 668 HOH B O   1 
HETATM 4668 O  O   . HOH O 9 .   ? 1.390   0.966   4.109   1.00  29.09 ? 669 HOH B O   1 
HETATM 4669 O  O   . HOH O 9 .   ? 11.289  -0.325  10.864  1.00  39.38 ? 670 HOH B O   1 
HETATM 4670 O  O   . HOH O 9 .   ? 5.392   -28.356 14.651  1.00  35.38 ? 671 HOH B O   1 
HETATM 4671 O  O   . HOH O 9 .   ? -0.760  -29.497 13.477  1.00  33.77 ? 672 HOH B O   1 
HETATM 4672 O  O   . HOH O 9 .   ? 1.177   -31.012 19.630  1.00  33.32 ? 673 HOH B O   1 
HETATM 4673 O  O   . HOH O 9 .   ? -8.126  -25.657 29.423  1.00  43.73 ? 674 HOH B O   1 
HETATM 4674 O  O   . HOH O 9 .   ? -30.170 -9.486  12.687  1.00  39.75 ? 675 HOH B O   1 
HETATM 4675 O  O   . HOH O 9 .   ? -16.875 10.035  18.809  1.00  34.00 ? 676 HOH B O   1 
HETATM 4676 O  O   . HOH O 9 .   ? -10.533 14.483  11.854  1.00  36.25 ? 677 HOH B O   1 
HETATM 4677 O  O   . HOH O 9 .   ? -5.051  -12.949 -1.877  1.00  29.37 ? 678 HOH B O   1 
HETATM 4678 O  O   . HOH O 9 .   ? -9.783  -20.369 0.335   1.00  34.54 ? 679 HOH B O   1 
HETATM 4679 O  O   . HOH O 9 .   ? -21.908 -15.820 5.756   1.00  32.90 ? 680 HOH B O   1 
HETATM 4680 O  O   . HOH O 9 .   ? -26.739 8.629   11.286  1.00  31.85 ? 681 HOH B O   1 
HETATM 4681 O  O   . HOH O 9 .   ? -15.357 -18.270 -2.563  1.00  39.53 ? 682 HOH B O   1 
HETATM 4682 O  O   . HOH O 9 .   ? 10.530  -18.036 13.593  1.00  33.21 ? 683 HOH B O   1 
HETATM 4683 O  O   . HOH O 9 .   ? -9.230  -13.751 32.851  1.00  19.11 ? 684 HOH B O   1 
HETATM 4684 O  O   . HOH O 9 .   ? -22.079 3.154   26.527  1.00  30.03 ? 685 HOH B O   1 
HETATM 4685 O  O   . HOH O 9 .   ? -12.783 -17.985 34.495  1.00  32.16 ? 686 HOH B O   1 
HETATM 4686 O  O   . HOH O 9 .   ? -20.151 12.768  11.412  1.00  24.01 ? 687 HOH B O   1 
HETATM 4687 O  O   . HOH O 9 .   ? -17.087 7.914   -1.351  1.00  36.89 ? 688 HOH B O   1 
HETATM 4688 O  O   . HOH O 9 .   ? 1.098   -26.490 23.354  1.00  34.32 ? 689 HOH B O   1 
HETATM 4689 O  O   . HOH O 9 .   ? -29.744 -13.467 24.998  1.00  36.36 ? 690 HOH B O   1 
HETATM 4690 O  O   . HOH P 9 .   ? -18.958 -40.684 14.306  1.00  25.18 ? 401 HOH A O   1 
HETATM 4691 O  O   . HOH P 9 .   ? -28.908 -27.998 48.734  1.00  17.00 ? 402 HOH A O   1 
HETATM 4692 O  O   . HOH P 9 .   ? -30.727 -57.078 31.344  1.00  30.17 ? 403 HOH A O   1 
HETATM 4693 O  O   . HOH P 9 .   ? -23.760 -31.476 44.755  1.00  35.87 ? 404 HOH A O   1 
HETATM 4694 O  O   . HOH P 9 .   ? -27.266 -35.439 42.807  1.00  32.78 ? 405 HOH A O   1 
HETATM 4695 O  O   . HOH P 9 .   ? -40.528 -26.578 13.243  1.00  36.24 ? 406 HOH A O   1 
HETATM 4696 O  O   . HOH P 9 .   ? -22.650 -32.167 31.629  1.00  9.72  ? 407 HOH A O   1 
HETATM 4697 O  O   . HOH P 9 .   ? -17.468 -31.120 29.514  1.00  13.16 ? 408 HOH A O   1 
HETATM 4698 O  O   . HOH P 9 .   ? -24.823 -17.272 20.697  1.00  14.66 ? 409 HOH A O   1 
HETATM 4699 O  O   . HOH P 9 .   ? -28.706 -27.778 10.144  1.00  12.33 ? 410 HOH A O   1 
HETATM 4700 O  O   . HOH P 9 .   ? -30.373 -40.568 38.335  1.00  19.58 ? 411 HOH A O   1 
HETATM 4701 O  O   . HOH P 9 .   ? -37.383 -40.213 30.050  1.00  9.64  ? 412 HOH A O   1 
HETATM 4702 O  O   . HOH P 9 .   ? -35.093 -28.225 6.142   1.00  12.33 ? 413 HOH A O   1 
HETATM 4703 O  O   . HOH P 9 .   ? -39.619 -36.536 29.804  1.00  12.34 ? 414 HOH A O   1 
HETATM 4704 O  O   . HOH P 9 .   ? -27.892 -39.876 14.694  1.00  12.76 ? 415 HOH A O   1 
HETATM 4705 O  O   . HOH P 9 .   ? -32.204 -42.502 35.319  1.00  15.92 ? 416 HOH A O   1 
HETATM 4706 O  O   . HOH P 9 .   ? -38.928 -40.999 36.800  1.00  12.77 ? 417 HOH A O   1 
HETATM 4707 O  O   . HOH P 9 .   ? -33.803 -34.404 41.082  1.00  10.12 ? 418 HOH A O   1 
HETATM 4708 O  O   . HOH P 9 .   ? -33.373 -23.653 15.134  1.00  11.93 ? 419 HOH A O   1 
HETATM 4709 O  O   . HOH P 9 .   ? -16.553 -22.565 26.422  1.00  15.33 ? 420 HOH A O   1 
HETATM 4710 O  O   . HOH P 9 .   ? -20.621 -32.088 11.104  1.00  14.51 ? 421 HOH A O   1 
HETATM 4711 O  O   . HOH P 9 .   ? -31.901 -22.543 13.211  1.00  11.89 ? 422 HOH A O   1 
HETATM 4712 O  O   . HOH P 9 .   ? -43.501 -38.089 38.124  1.00  14.44 ? 423 HOH A O   1 
HETATM 4713 O  O   . HOH P 9 .   ? -15.801 -24.871 16.625  1.00  13.25 ? 424 HOH A O   1 
HETATM 4714 O  O   . HOH P 9 .   ? -21.029 -41.904 18.660  1.00  16.61 ? 425 HOH A O   1 
HETATM 4715 O  O   . HOH P 9 .   ? -22.193 -21.741 8.470   1.00  19.78 ? 426 HOH A O   1 
HETATM 4716 O  O   . HOH P 9 .   ? -43.136 -16.838 19.676  1.00  18.70 ? 427 HOH A O   1 
HETATM 4717 O  O   . HOH P 9 .   ? -30.015 -51.172 24.643  1.00  14.88 ? 428 HOH A O   1 
HETATM 4718 O  O   . HOH P 9 .   ? -20.108 -21.060 20.197  1.00  14.69 ? 429 HOH A O   1 
HETATM 4719 O  O   . HOH P 9 .   ? -29.037 -45.597 17.416  1.00  14.84 ? 430 HOH A O   1 
HETATM 4720 O  O   . HOH P 9 .   ? -27.388 -54.632 32.942  1.00  12.27 ? 431 HOH A O   1 
HETATM 4721 O  O   . HOH P 9 .   ? -49.028 -35.876 42.231  1.00  20.29 ? 432 HOH A O   1 
HETATM 4722 O  O   . HOH P 9 .   ? -19.404 -36.345 34.597  1.00  17.84 ? 433 HOH A O   1 
HETATM 4723 O  O   . HOH P 9 .   ? -41.318 -47.530 35.977  1.00  21.68 ? 434 HOH A O   1 
HETATM 4724 O  O   . HOH P 9 .   ? -54.799 -31.018 36.096  1.00  20.12 ? 435 HOH A O   1 
HETATM 4725 O  O   . HOH P 9 .   ? -23.602 -40.088 9.832   1.00  18.38 ? 436 HOH A O   1 
HETATM 4726 O  O   . HOH P 9 .   ? -29.559 -12.896 17.218  1.00  18.50 ? 437 HOH A O   1 
HETATM 4727 O  O   . HOH P 9 .   ? -30.177 -47.530 14.859  1.00  15.31 ? 438 HOH A O   1 
HETATM 4728 O  O   . HOH P 9 .   ? -23.883 -38.004 11.621  1.00  11.79 ? 439 HOH A O   1 
HETATM 4729 O  O   . HOH P 9 .   ? -24.795 -22.885 33.134  1.00  20.13 ? 440 HOH A O   1 
HETATM 4730 O  O   . HOH P 9 .   ? -34.408 -49.816 15.817  1.00  18.28 ? 441 HOH A O   1 
HETATM 4731 O  O   . HOH P 9 .   ? -34.809 -33.144 47.293  1.00  20.13 ? 442 HOH A O   1 
HETATM 4732 O  O   . HOH P 9 .   ? -36.126 -47.546 16.260  1.00  14.95 ? 443 HOH A O   1 
HETATM 4733 O  O   . HOH P 9 .   ? -29.180 -11.958 19.926  1.00  15.87 ? 444 HOH A O   1 
HETATM 4734 O  O   . HOH P 9 .   ? -25.153 -55.163 28.229  1.00  19.46 ? 445 HOH A O   1 
HETATM 4735 O  O   . HOH P 9 .   ? -27.694 -44.061 15.611  1.00  16.50 ? 446 HOH A O   1 
HETATM 4736 O  O   . HOH P 9 .   ? -12.869 -55.611 28.161  1.00  21.49 ? 447 HOH A O   1 
HETATM 4737 O  O   . HOH P 9 .   ? -30.987 -20.201 49.563  1.00  17.04 ? 448 HOH A O   1 
HETATM 4738 O  O   . HOH P 9 .   ? -25.424 -36.396 7.275   1.00  19.41 ? 449 HOH A O   1 
HETATM 4739 O  O   . HOH P 9 .   ? -38.687 -48.505 16.648  1.00  17.28 ? 450 HOH A O   1 
HETATM 4740 O  O   . HOH P 9 .   ? -26.936 -15.219 14.506  1.00  16.17 ? 451 HOH A O   1 
HETATM 4741 O  O   . HOH P 9 .   ? -25.134 -25.172 8.850   1.00  19.49 ? 452 HOH A O   1 
HETATM 4742 O  O   . HOH P 9 .   ? -15.061 -57.782 28.360  1.00  19.60 ? 453 HOH A O   1 
HETATM 4743 O  O   . HOH P 9 .   ? -37.941 -48.189 30.226  1.00  17.09 ? 454 HOH A O   1 
HETATM 4744 O  O   . HOH P 9 .   ? -32.563 -52.772 18.628  1.00  16.50 ? 455 HOH A O   1 
HETATM 4745 O  O   . HOH P 9 .   ? -41.452 -50.007 19.671  1.00  19.74 ? 456 HOH A O   1 
HETATM 4746 O  O   . HOH P 9 .   ? -40.268 -50.957 29.519  1.00  18.19 ? 457 HOH A O   1 
HETATM 4747 O  O   . HOH P 9 .   ? -25.285 -52.812 32.568  1.00  13.21 ? 458 HOH A O   1 
HETATM 4748 O  O   . HOH P 9 .   ? -32.356 -24.031 50.206  1.00  21.57 ? 459 HOH A O   1 
HETATM 4749 O  O   . HOH P 9 .   ? -25.256 -22.353 9.435   1.00  20.41 ? 460 HOH A O   1 
HETATM 4750 O  O   . HOH P 9 .   ? -48.712 -39.569 33.831  1.00  27.26 ? 461 HOH A O   1 
HETATM 4751 O  O   . HOH P 9 .   ? -25.830 -18.231 10.644  1.00  20.82 ? 462 HOH A O   1 
HETATM 4752 O  O   . HOH P 9 .   ? -46.272 -38.805 34.487  1.00  16.22 ? 463 HOH A O   1 
HETATM 4753 O  O   . HOH P 9 .   ? -12.132 -34.272 20.295  1.00  17.67 ? 464 HOH A O   1 
HETATM 4754 O  O   . HOH P 9 .   ? -22.599 -48.167 41.159  1.00  20.87 ? 465 HOH A O   1 
HETATM 4755 O  O   . HOH P 9 .   ? -22.241 -25.193 14.251  1.00  18.51 ? 466 HOH A O   1 
HETATM 4756 O  O   . HOH P 9 .   ? -39.218 -30.017 11.170  1.00  22.60 ? 467 HOH A O   1 
HETATM 4757 O  O   . HOH P 9 .   ? -30.739 -14.530 38.813  1.00  21.91 ? 468 HOH A O   1 
HETATM 4758 O  O   . HOH P 9 .   ? -18.114 -23.580 13.389  1.00  19.65 ? 469 HOH A O   1 
HETATM 4759 O  O   . HOH P 9 .   ? -23.525 -39.560 13.867  1.00  19.48 ? 470 HOH A O   1 
HETATM 4760 O  O   . HOH P 9 .   ? -40.723 -47.432 18.503  1.00  17.70 ? 471 HOH A O   1 
HETATM 4761 O  O   . HOH P 9 .   ? -45.522 -37.550 32.268  1.00  15.16 ? 472 HOH A O   1 
HETATM 4762 O  O   . HOH P 9 .   ? -42.911 -25.386 23.274  1.00  18.40 ? 473 HOH A O   1 
HETATM 4763 O  O   . HOH P 9 .   ? -14.650 -33.403 19.284  1.00  20.98 ? 474 HOH A O   1 
HETATM 4764 O  O   . HOH P 9 .   ? -20.601 -39.268 11.217  1.00  21.65 ? 475 HOH A O   1 
HETATM 4765 O  O   . HOH P 9 .   ? -38.855 -15.551 31.409  1.00  23.05 ? 476 HOH A O   1 
HETATM 4766 O  O   . HOH P 9 .   ? -51.489 -21.875 26.538  1.00  22.38 ? 477 HOH A O   1 
HETATM 4767 O  O   . HOH P 9 .   ? -18.771 -27.860 36.871  1.00  20.43 ? 478 HOH A O   1 
HETATM 4768 O  O   . HOH P 9 .   ? -45.955 -37.686 37.052  1.00  18.77 ? 479 HOH A O   1 
HETATM 4769 O  O   . HOH P 9 .   ? -39.096 -51.138 16.197  1.00  21.57 ? 480 HOH A O   1 
HETATM 4770 O  O   . HOH P 9 .   ? -48.363 -39.503 27.384  1.00  23.85 ? 481 HOH A O   1 
HETATM 4771 O  O   . HOH P 9 .   ? -33.633 -45.316 13.211  1.00  22.09 ? 482 HOH A O   1 
HETATM 4772 O  O   . HOH P 9 .   ? -24.877 -18.131 42.356  1.00  28.42 ? 483 HOH A O   1 
HETATM 4773 O  O   . HOH P 9 .   ? -34.760 -38.688 42.966  1.00  23.81 ? 484 HOH A O   1 
HETATM 4774 O  O   . HOH P 9 .   ? -24.599 -40.244 42.713  1.00  26.06 ? 485 HOH A O   1 
HETATM 4775 O  O   . HOH P 9 .   ? -13.636 -41.016 30.172  1.00  26.50 ? 486 HOH A O   1 
HETATM 4776 O  O   . HOH P 9 .   ? -48.901 -36.263 30.452  1.00  19.22 ? 487 HOH A O   1 
HETATM 4777 O  O   . HOH P 9 .   ? -22.031 -23.486 34.304  1.00  24.86 ? 488 HOH A O   1 
HETATM 4778 O  O   . HOH P 9 .   ? -31.900 -16.611 32.554  1.00  23.82 ? 489 HOH A O   1 
HETATM 4779 O  O   . HOH P 9 .   ? -52.151 -36.941 32.220  1.00  27.55 ? 490 HOH A O   1 
HETATM 4780 O  O   . HOH P 9 .   ? -26.366 -50.326 32.802  1.00  16.40 ? 491 HOH A O   1 
HETATM 4781 O  O   . HOH P 9 .   ? -41.032 -32.030 12.151  1.00  23.36 ? 492 HOH A O   1 
HETATM 4782 O  O   . HOH P 9 .   ? -24.224 -32.971 4.694   1.00  19.01 ? 493 HOH A O   1 
HETATM 4783 O  O   . HOH P 9 .   ? -15.160 -25.813 25.461  1.00  19.70 ? 494 HOH A O   1 
HETATM 4784 O  O   . HOH P 9 .   ? -19.874 -32.975 7.602   1.00  21.99 ? 495 HOH A O   1 
HETATM 4785 O  O   . HOH P 9 .   ? -24.171 -48.645 15.433  1.00  35.57 ? 496 HOH A O   1 
HETATM 4786 O  O   . HOH P 9 .   ? -20.205 -25.568 34.631  1.00  18.50 ? 497 HOH A O   1 
HETATM 4787 O  O   . HOH P 9 .   ? -21.279 -26.309 7.557   1.00  24.98 ? 498 HOH A O   1 
HETATM 4788 O  O   . HOH P 9 .   ? -23.389 -29.151 5.876   1.00  23.58 ? 499 HOH A O   1 
HETATM 4789 O  O   . HOH P 9 .   ? -21.542 -41.392 14.319  1.00  23.74 ? 500 HOH A O   1 
HETATM 4790 O  O   . HOH P 9 .   ? -10.642 -36.068 18.523  1.00  23.03 ? 501 HOH A O   1 
HETATM 4791 O  O   . HOH P 9 .   ? -13.013 -32.545 23.799  1.00  23.29 ? 502 HOH A O   1 
HETATM 4792 O  O   . HOH P 9 .   ? -14.433 -30.365 20.433  1.00  26.06 ? 503 HOH A O   1 
HETATM 4793 O  O   . HOH P 9 .   ? -13.953 -28.357 25.120  1.00  21.77 ? 504 HOH A O   1 
HETATM 4794 O  O   . HOH P 9 .   ? -26.598 -17.525 22.893  1.00  23.90 ? 505 HOH A O   1 
HETATM 4795 O  O   . HOH P 9 .   ? -35.779 -43.163 40.652  1.00  29.04 ? 506 HOH A O   1 
HETATM 4796 O  O   . HOH P 9 .   ? -30.370 -13.755 13.446  1.00  33.09 ? 507 HOH A O   1 
HETATM 4797 O  O   . HOH P 9 .   ? -33.430 -19.873 13.528  1.00  23.89 ? 508 HOH A O   1 
HETATM 4798 O  O   . HOH P 9 .   ? -37.257 -13.388 18.115  1.00  28.53 ? 509 HOH A O   1 
HETATM 4799 O  O   . HOH P 9 .   ? -26.311 -17.858 13.237  1.00  18.50 ? 510 HOH A O   1 
HETATM 4800 O  O   . HOH P 9 .   ? -25.578 -21.454 7.036   1.00  29.17 ? 511 HOH A O   1 
HETATM 4801 O  O   . HOH P 9 .   ? -48.104 -38.805 31.117  1.00  25.02 ? 512 HOH A O   1 
HETATM 4802 O  O   . HOH P 9 .   ? -43.167 -28.961 21.993  1.00  28.95 ? 513 HOH A O   1 
HETATM 4803 O  O   . HOH P 9 .   ? -47.380 -47.130 29.392  1.00  27.22 ? 514 HOH A O   1 
HETATM 4804 O  O   . HOH P 9 .   ? -21.664 -24.149 43.682  1.00  37.61 ? 515 HOH A O   1 
HETATM 4805 O  O   . HOH P 9 .   ? -16.911 -29.857 37.635  1.00  27.13 ? 516 HOH A O   1 
HETATM 4806 O  O   . HOH P 9 .   ? -36.742 -54.917 21.046  1.00  35.41 ? 517 HOH A O   1 
HETATM 4807 O  O   . HOH P 9 .   ? -33.521 -51.852 27.297  1.00  22.34 ? 518 HOH A O   1 
HETATM 4808 O  O   . HOH P 9 .   ? -29.215 -50.971 32.648  1.00  24.45 ? 519 HOH A O   1 
HETATM 4809 O  O   . HOH P 9 .   ? -29.759 -53.488 33.544  1.00  19.16 ? 520 HOH A O   1 
HETATM 4810 O  O   . HOH P 9 .   ? -27.531 -56.899 28.690  1.00  24.68 ? 521 HOH A O   1 
HETATM 4811 O  O   . HOH P 9 .   ? -22.270 -45.835 35.769  1.00  19.50 ? 522 HOH A O   1 
HETATM 4812 O  O   . HOH P 9 .   ? -21.009 -48.310 39.132  1.00  25.09 ? 523 HOH A O   1 
HETATM 4813 O  O   . HOH P 9 .   ? -24.807 -46.750 38.648  1.00  22.02 ? 524 HOH A O   1 
HETATM 4814 O  O   . HOH P 9 .   ? -14.503 -46.705 35.202  1.00  21.95 ? 525 HOH A O   1 
HETATM 4815 O  O   . HOH P 9 .   ? -15.007 -38.772 34.597  1.00  35.08 ? 526 HOH A O   1 
HETATM 4816 O  O   . HOH P 9 .   ? -17.346 -48.531 25.894  1.00  25.42 ? 527 HOH A O   1 
HETATM 4817 O  O   . HOH P 9 .   ? -10.872 -40.289 28.183  1.00  34.09 ? 528 HOH A O   1 
HETATM 4818 O  O   . HOH P 9 .   ? -31.541 -11.578 21.057  1.00  27.79 ? 529 HOH A O   1 
HETATM 4819 O  O   . HOH P 9 .   ? -39.485 -13.978 25.579  1.00  23.26 ? 530 HOH A O   1 
HETATM 4820 O  O   . HOH P 9 .   ? -39.959 -35.401 27.058  1.00  26.82 ? 531 HOH A O   1 
HETATM 4821 O  O   . HOH P 9 .   ? -30.107 -30.887 48.211  1.00  28.09 ? 532 HOH A O   1 
HETATM 4822 O  O   . HOH P 9 .   ? -26.102 -33.283 42.191  1.00  20.47 ? 533 HOH A O   1 
HETATM 4823 O  O   . HOH P 9 .   ? -36.106 -45.804 13.970  1.00  25.53 ? 534 HOH A O   1 
HETATM 4824 O  O   . HOH P 9 .   ? -38.473 -46.247 12.593  1.00  28.56 ? 535 HOH A O   1 
HETATM 4825 O  O   . HOH P 9 .   ? -25.103 -39.182 7.593   1.00  20.20 ? 536 HOH A O   1 
HETATM 4826 O  O   . HOH P 9 .   ? -25.005 -35.735 4.713   1.00  28.80 ? 537 HOH A O   1 
HETATM 4827 O  O   . HOH P 9 .   ? -22.512 -43.008 16.536  1.00  22.93 ? 538 HOH A O   1 
HETATM 4828 O  O   . HOH P 9 .   ? -24.089 -21.426 38.262  1.00  39.01 ? 539 HOH A O   1 
HETATM 4829 O  O   . HOH P 9 .   ? -22.958 -23.535 36.606  1.00  27.64 ? 540 HOH A O   1 
HETATM 4830 O  O   . HOH P 9 .   ? -19.258 -20.541 47.447  1.00  27.53 ? 541 HOH A O   1 
HETATM 4831 O  O   . HOH P 9 .   ? -30.018 -17.042 39.904  1.00  25.62 ? 542 HOH A O   1 
HETATM 4832 O  O   . HOH P 9 .   ? -37.724 -17.566 38.370  1.00  29.62 ? 543 HOH A O   1 
HETATM 4833 O  O   . HOH P 9 .   ? -42.731 -19.389 37.601  1.00  24.47 ? 544 HOH A O   1 
HETATM 4834 O  O   . HOH P 9 .   ? -44.857 -17.705 34.911  1.00  23.43 ? 545 HOH A O   1 
HETATM 4835 O  O   . HOH P 9 .   ? -45.749 -24.486 37.666  1.00  24.95 ? 546 HOH A O   1 
HETATM 4836 O  O   . HOH P 9 .   ? -54.417 -27.581 29.662  1.00  25.35 ? 547 HOH A O   1 
HETATM 4837 O  O   . HOH P 9 .   ? -47.405 -15.803 25.426  1.00  26.12 ? 548 HOH A O   1 
HETATM 4838 O  O   . HOH P 9 .   ? -22.259 -19.314 30.904  1.00  23.78 ? 549 HOH A O   1 
HETATM 4839 O  O   . HOH P 9 .   ? -27.234 -14.329 28.913  1.00  33.04 ? 550 HOH A O   1 
HETATM 4840 O  O   . HOH P 9 .   ? -15.305 -30.265 22.914  1.00  29.58 ? 551 HOH A O   1 
HETATM 4841 O  O   . HOH P 9 .   ? -14.968 -31.509 31.199  1.00  21.10 ? 552 HOH A O   1 
HETATM 4842 O  O   . HOH P 9 .   ? -13.656 -27.137 33.043  1.00  40.33 ? 553 HOH A O   1 
HETATM 4843 O  O   . HOH P 9 .   ? -19.435 -44.082 19.680  1.00  34.80 ? 554 HOH A O   1 
HETATM 4844 O  O   . HOH P 9 .   ? -25.245 -42.600 16.343  1.00  17.69 ? 555 HOH A O   1 
HETATM 4845 O  O   . HOH P 9 .   ? -27.378 -46.880 14.793  1.00  25.12 ? 556 HOH A O   1 
HETATM 4846 O  O   . HOH P 9 .   ? -42.410 -38.085 22.781  1.00  31.74 ? 557 HOH A O   1 
HETATM 4847 O  O   . HOH P 9 .   ? -45.929 -41.980 21.504  1.00  43.26 ? 558 HOH A O   1 
HETATM 4848 O  O   . HOH P 9 .   ? -39.013 -46.605 9.995   1.00  32.44 ? 559 HOH A O   1 
HETATM 4849 O  O   . HOH P 9 .   ? -18.602 -23.925 35.805  1.00  25.20 ? 560 HOH A O   1 
HETATM 4850 O  O   . HOH P 9 .   ? -17.213 -37.354 35.701  1.00  23.71 ? 561 HOH A O   1 
HETATM 4851 O  O   . HOH P 9 .   ? -42.209 -26.887 43.715  1.00  28.15 ? 562 HOH A O   1 
HETATM 4852 O  O   . HOH P 9 .   ? -21.150 -22.402 27.414  1.00  21.50 ? 563 HOH A O   1 
HETATM 4853 O  O   . HOH P 9 .   ? -18.631 -20.462 29.582  1.00  29.60 ? 564 HOH A O   1 
HETATM 4854 O  O   . HOH P 9 .   ? -16.177 -31.595 35.630  1.00  28.31 ? 565 HOH A O   1 
HETATM 4855 O  O   . HOH P 9 .   ? -13.336 -39.085 32.758  1.00  23.42 ? 566 HOH A O   1 
HETATM 4856 O  O   . HOH P 9 .   ? -19.132 -26.052 38.924  1.00  26.02 ? 567 HOH A O   1 
HETATM 4857 O  O   . HOH P 9 .   ? -15.317 -24.446 35.231  1.00  27.86 ? 568 HOH A O   1 
HETATM 4858 O  O   . HOH P 9 .   ? -16.605 -34.143 35.753  1.00  35.46 ? 569 HOH A O   1 
HETATM 4859 O  O   . HOH P 9 .   ? -27.986 -19.127 8.594   1.00  30.59 ? 570 HOH A O   1 
HETATM 4860 O  O   . HOH P 9 .   ? -21.833 -28.846 8.037   1.00  20.97 ? 571 HOH A O   1 
HETATM 4861 O  O   . HOH P 9 .   ? -51.657 -38.979 30.234  1.00  30.34 ? 572 HOH A O   1 
HETATM 4862 O  O   . HOH P 9 .   ? -50.492 -44.804 37.704  1.00  30.28 ? 573 HOH A O   1 
HETATM 4863 O  O   . HOH P 9 .   ? -39.869 -47.800 14.255  1.00  25.25 ? 574 HOH A O   1 
HETATM 4864 O  O   . HOH P 9 .   ? -39.777 -53.044 18.069  1.00  28.50 ? 575 HOH A O   1 
HETATM 4865 O  O   . HOH P 9 .   ? -20.305 -47.896 34.840  1.00  22.68 ? 576 HOH A O   1 
HETATM 4866 O  O   . HOH P 9 .   ? -21.708 -49.263 36.942  1.00  23.87 ? 577 HOH A O   1 
HETATM 4867 O  O   . HOH P 9 .   ? -32.540 -44.632 37.485  1.00  31.68 ? 578 HOH A O   1 
HETATM 4868 O  O   . HOH P 9 .   ? -18.795 -47.810 28.842  1.00  47.61 ? 579 HOH A O   1 
HETATM 4869 O  O   . HOH P 9 .   ? -47.734 -33.957 25.054  1.00  27.23 ? 580 HOH A O   1 
HETATM 4870 O  O   . HOH P 9 .   ? -37.846 -51.791 28.942  1.00  35.07 ? 581 HOH A O   1 
HETATM 4871 O  O   . HOH P 9 .   ? -17.392 -34.323 12.583  1.00  18.08 ? 582 HOH A O   1 
HETATM 4872 O  O   . HOH P 9 .   ? -12.053 -29.278 20.727  1.00  27.03 ? 583 HOH A O   1 
HETATM 4873 O  O   . HOH P 9 .   ? -31.681 -11.167 16.123  1.00  31.95 ? 584 HOH A O   1 
HETATM 4874 O  O   . HOH P 9 .   ? -49.621 -19.509 29.249  1.00  30.62 ? 585 HOH A O   1 
HETATM 4875 O  O   . HOH P 9 .   ? -43.351 -25.717 18.507  1.00  34.58 ? 586 HOH A O   1 
HETATM 4876 O  O   . HOH P 9 .   ? -39.829 -28.504 18.672  1.00  32.75 ? 587 HOH A O   1 
HETATM 4877 O  O   . HOH P 9 .   ? -50.929 -38.456 27.949  1.00  31.84 ? 588 HOH A O   1 
HETATM 4878 O  O   . HOH P 9 .   ? -24.294 -46.208 41.657  1.00  27.69 ? 589 HOH A O   1 
HETATM 4879 O  O   . HOH P 9 .   ? -21.278 -32.800 41.713  1.00  37.34 ? 590 HOH A O   1 
HETATM 4880 O  O   . HOH P 9 .   ? -40.102 -15.116 28.384  1.00  33.93 ? 591 HOH A O   1 
HETATM 4881 O  O   . HOH P 9 .   ? -41.419 -35.980 24.544  1.00  33.85 ? 592 HOH A O   1 
HETATM 4882 O  O   . HOH P 9 .   ? -41.679 -33.035 26.654  1.00  23.11 ? 593 HOH A O   1 
HETATM 4883 O  O   . HOH P 9 .   ? -45.193 -29.301 24.302  1.00  32.76 ? 594 HOH A O   1 
HETATM 4884 O  O   . HOH P 9 .   ? -49.218 -26.243 23.886  1.00  30.55 ? 595 HOH A O   1 
HETATM 4885 O  O   . HOH P 9 .   ? -39.748 -26.645 17.030  1.00  24.77 ? 596 HOH A O   1 
HETATM 4886 O  O   . HOH P 9 .   ? -41.695 -32.880 21.787  1.00  34.49 ? 597 HOH A O   1 
HETATM 4887 O  O   . HOH P 9 .   ? -29.501 -18.408 29.581  1.00  27.79 ? 598 HOH A O   1 
HETATM 4888 O  O   . HOH P 9 .   ? -31.587 -16.064 28.042  1.00  20.99 ? 599 HOH A O   1 
HETATM 4889 O  O   . HOH P 9 .   ? -37.475 -13.632 32.781  1.00  28.02 ? 600 HOH A O   1 
HETATM 4890 O  O   . HOH P 9 .   ? -36.825 -43.748 36.695  1.00  22.52 ? 601 HOH A O   1 
HETATM 4891 O  O   . HOH P 9 .   ? -26.299 -27.356 4.767   1.00  35.00 ? 602 HOH A O   1 
HETATM 4892 O  O   . HOH P 9 .   ? -14.936 -42.764 12.733  1.00  35.25 ? 603 HOH A O   1 
HETATM 4893 O  O   . HOH P 9 .   ? -8.289  -42.083 12.134  1.00  38.03 ? 604 HOH A O   1 
HETATM 4894 O  O   . HOH P 9 .   ? -4.619  -36.626 19.354  1.00  36.24 ? 605 HOH A O   1 
HETATM 4895 O  O   . HOH P 9 .   ? -27.960 -58.757 23.496  1.00  29.39 ? 606 HOH A O   1 
HETATM 4896 O  O   . HOH P 9 .   ? -27.200 -59.954 28.849  1.00  34.16 ? 607 HOH A O   1 
HETATM 4897 O  O   . HOH P 9 .   ? -19.716 -22.165 40.627  1.00  42.90 ? 608 HOH A O   1 
HETATM 4898 O  O   . HOH P 9 .   ? -25.154 -17.924 38.405  1.00  37.03 ? 609 HOH A O   1 
HETATM 4899 O  O   . HOH P 9 .   ? -28.552 -12.472 35.683  1.00  37.63 ? 610 HOH A O   1 
HETATM 4900 O  O   . HOH P 9 .   ? -34.562 -13.289 31.984  1.00  41.77 ? 611 HOH A O   1 
HETATM 4901 O  O   . HOH P 9 .   ? -34.518 -12.733 27.281  1.00  40.76 ? 612 HOH A O   1 
HETATM 4902 O  O   . HOH P 9 .   ? -31.674 -17.622 29.778  1.00  35.20 ? 613 HOH A O   1 
HETATM 4903 O  O   . HOH P 9 .   ? -33.113 -19.689 31.224  1.00  25.18 ? 614 HOH A O   1 
HETATM 4904 O  O   . HOH P 9 .   ? -23.534 -34.757 41.987  1.00  38.79 ? 615 HOH A O   1 
HETATM 4905 O  O   . HOH P 9 .   ? -23.811 -37.138 43.164  1.00  39.33 ? 616 HOH A O   1 
HETATM 4906 O  O   . HOH P 9 .   ? -25.816 -37.595 44.253  1.00  37.59 ? 617 HOH A O   1 
HETATM 4907 O  O   . HOH P 9 .   ? -20.545 -21.704 31.126  1.00  36.44 ? 618 HOH A O   1 
HETATM 4908 O  O   . HOH P 9 .   ? -51.273 -38.770 34.520  1.00  30.73 ? 619 HOH A O   1 
HETATM 4909 O  O   . HOH P 9 .   ? -43.778 -47.786 37.416  1.00  37.52 ? 620 HOH A O   1 
HETATM 4910 O  O   . HOH P 9 .   ? -35.734 -52.259 15.296  1.00  35.89 ? 621 HOH A O   1 
HETATM 4911 O  O   . HOH P 9 .   ? -32.196 -53.674 26.090  1.00  24.74 ? 622 HOH A O   1 
HETATM 4912 O  O   . HOH P 9 .   ? -17.885 -47.654 36.205  1.00  31.29 ? 623 HOH A O   1 
HETATM 4913 O  O   . HOH P 9 .   ? -15.311 -40.021 14.559  1.00  39.67 ? 624 HOH A O   1 
HETATM 4914 O  O   . HOH P 9 .   ? -11.301 -31.764 18.945  1.00  24.33 ? 625 HOH A O   1 
HETATM 4915 O  O   . HOH P 9 .   ? -34.772 -18.588 11.570  1.00  30.61 ? 626 HOH A O   1 
HETATM 4916 O  O   . HOH P 9 .   ? -34.678 -11.118 18.680  1.00  38.88 ? 627 HOH A O   1 
HETATM 4917 O  O   . HOH P 9 .   ? -42.720 -33.630 23.978  1.00  38.86 ? 628 HOH A O   1 
HETATM 4918 O  O   . HOH P 9 .   ? -40.469 -22.851 12.554  1.00  31.77 ? 629 HOH A O   1 
HETATM 4919 O  O   . HOH P 9 .   ? -18.625 -33.859 38.461  1.00  38.03 ? 630 HOH A O   1 
HETATM 4920 O  O   . HOH P 9 .   ? -18.480 -31.603 39.527  1.00  34.58 ? 631 HOH A O   1 
HETATM 4921 O  O   . HOH P 9 .   ? -21.970 -28.125 44.213  1.00  30.23 ? 632 HOH A O   1 
HETATM 4922 O  O   . HOH P 9 .   ? -30.872 -57.553 28.150  1.00  41.58 ? 633 HOH A O   1 
HETATM 4923 O  O   . HOH P 9 .   ? -8.427  -34.173 29.581  1.00  32.64 ? 634 HOH A O   1 
HETATM 4924 O  O   . HOH P 9 .   ? -9.483  -39.433 30.578  1.00  37.38 ? 635 HOH A O   1 
HETATM 4925 O  O   . HOH P 9 .   ? -45.097 -41.190 18.375  1.00  42.55 ? 636 HOH A O   1 
HETATM 4926 O  O   . HOH P 9 .   ? -38.530 -33.364 20.422  1.00  42.14 ? 637 HOH A O   1 
HETATM 4927 O  O   . HOH P 9 .   ? -43.748 -38.697 18.946  1.00  41.99 ? 638 HOH A O   1 
HETATM 4928 O  O   . HOH P 9 .   ? -31.710 -11.913 23.746  1.00  42.78 ? 639 HOH A O   1 
HETATM 4929 O  O   . HOH P 9 .   ? -24.117 -25.857 6.603   1.00  44.55 ? 640 HOH A O   1 
HETATM 4930 O  O   . HOH P 9 .   ? -27.075 -23.050 5.644   1.00  31.81 ? 641 HOH A O   1 
HETATM 4931 O  O   . HOH P 9 .   ? -9.820  -34.608 14.100  1.00  37.89 ? 642 HOH A O   1 
HETATM 4932 O  O   . HOH P 9 .   ? -53.607 -47.198 28.933  1.00  43.69 ? 643 HOH A O   1 
HETATM 4933 O  O   . HOH P 9 .   ? -37.778 -52.167 31.766  1.00  35.72 ? 644 HOH A O   1 
HETATM 4934 O  O   . HOH P 9 .   ? -15.544 -53.259 35.876  1.00  36.14 ? 645 HOH A O   1 
HETATM 4935 O  O   . HOH P 9 .   ? -7.734  -42.284 18.719  1.00  38.87 ? 646 HOH A O   1 
HETATM 4936 O  O   . HOH P 9 .   ? -10.323 -45.095 19.314  1.00  35.88 ? 647 HOH A O   1 
HETATM 4937 O  O   . HOH P 9 .   ? -19.807 -30.271 7.901   1.00  41.50 ? 648 HOH A O   1 
HETATM 4938 O  O   . HOH P 9 .   ? -23.023 -22.528 5.869   1.00  38.02 ? 649 HOH A O   1 
HETATM 4939 O  O   . HOH P 9 .   ? -24.103 -39.806 5.254   1.00  31.94 ? 650 HOH A O   1 
HETATM 4940 O  O   . HOH P 9 .   ? -42.588 -34.695 7.925   1.00  35.93 ? 651 HOH A O   1 
HETATM 4941 O  O   . HOH P 9 .   ? -27.129 -16.967 40.447  1.00  29.67 ? 652 HOH A O   1 
HETATM 4942 O  O   . HOH P 9 .   ? -55.126 -28.155 37.406  1.00  30.80 ? 653 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  ?   ?   ?   B . n 
A 1 2   MET 2   0   ?   ?   ?   B . n 
A 1 3   SER 3   1   ?   ?   ?   B . n 
A 1 4   ARG 4   2   ?   ?   ?   B . n 
A 1 5   LEU 5   3   ?   ?   ?   B . n 
A 1 6   SER 6   4   4   SER SER B . n 
A 1 7   TRP 7   5   5   TRP TRP B . n 
A 1 8   GLY 8   6   6   GLY GLY B . n 
A 1 9   TYR 9   7   7   TYR TYR B . n 
A 1 10  ARG 10  8   8   ARG ARG B . n 
A 1 11  GLU 11  9   9   GLU GLU B . n 
A 1 12  HIS 12  10  10  HIS HIS B . n 
A 1 13  ASN 13  11  11  ASN ASN B . n 
A 1 14  GLY 14  12  12  GLY GLY B . n 
A 1 15  PRO 15  13  13  PRO PRO B . n 
A 1 16  ILE 16  14  14  ILE ILE B . n 
A 1 17  HIS 17  15  15  HIS HIS B . n 
A 1 18  TRP 18  16  16  TRP TRP B . n 
A 1 19  LYS 19  17  17  LYS LYS B . n 
A 1 20  GLU 20  18  18  GLU GLU B . n 
A 1 21  PHE 21  19  19  PHE PHE B . n 
A 1 22  PHE 22  20  20  PHE PHE B . n 
A 1 23  PRO 23  21  21  PRO PRO B . n 
A 1 24  ILE 24  22  22  ILE ILE B . n 
A 1 25  ALA 25  23  23  ALA ALA B . n 
A 1 26  ASP 26  24  24  ASP ASP B . n 
A 1 27  GLY 27  25  25  GLY GLY B . n 
A 1 28  ASP 28  26  26  ASP ASP B . n 
A 1 29  GLN 29  27  27  GLN GLN B . n 
A 1 30  GLN 30  28  28  GLN GLN B . n 
A 1 31  SER 31  29  29  SER SER B . n 
A 1 32  PRO 32  30  30  PRO PRO B . n 
A 1 33  ILE 33  31  31  ILE ILE B . n 
A 1 34  GLU 34  32  32  GLU GLU B . n 
A 1 35  ILE 35  33  33  ILE ILE B . n 
A 1 36  LYS 36  34  34  LYS LYS B . n 
A 1 37  THR 37  35  35  THR THR B . n 
A 1 38  LYS 38  36  36  LYS LYS B . n 
A 1 39  GLU 39  37  37  GLU GLU B . n 
A 1 40  VAL 40  38  38  VAL VAL B . n 
A 1 41  LYS 41  39  39  LYS LYS B . n 
A 1 42  TYR 42  40  40  TYR TYR B . n 
A 1 43  ASP 43  41  41  ASP ASP B . n 
A 1 44  SER 44  42  42  SER SER B . n 
A 1 45  SER 45  43  43  SER SER B . n 
A 1 46  LEU 46  44  44  LEU LEU B . n 
A 1 47  ARG 47  45  45  ARG ARG B . n 
A 1 48  PRO 48  46  46  PRO PRO B . n 
A 1 49  LEU 49  47  47  LEU LEU B . n 
A 1 50  SER 50  48  48  SER SER B . n 
A 1 51  ILE 51  49  49  ILE ILE B . n 
A 1 52  LYS 52  50  50  LYS LYS B . n 
A 1 53  TYR 53  51  51  TYR TYR B . n 
A 1 54  ASP 54  52  52  ASP ASP B . n 
A 1 55  PRO 55  53  53  PRO PRO B . n 
A 1 56  SER 56  54  54  SER SER B . n 
A 1 57  SER 57  55  55  SER SER B . n 
A 1 58  ALA 58  56  56  ALA ALA B . n 
A 1 59  LYS 59  57  57  LYS LYS B . n 
A 1 60  ILE 60  58  58  ILE ILE B . n 
A 1 61  ILE 61  59  59  ILE ILE B . n 
A 1 62  SER 62  60  60  SER SER B . n 
A 1 63  ASN 63  61  61  ASN ASN B . n 
A 1 64  SER 64  62  62  SER SER B . n 
A 1 65  GLY 65  63  63  GLY GLY B . n 
A 1 66  HIS 66  64  64  HIS HIS B . n 
A 1 67  SER 67  65  65  SER SER B . n 
A 1 68  PHE 68  66  66  PHE PHE B . n 
A 1 69  ASN 69  67  67  ASN ASN B . n 
A 1 70  VAL 70  68  68  VAL VAL B . n 
A 1 71  ASP 71  69  69  ASP ASP B . n 
A 1 72  PHE 72  70  70  PHE PHE B . n 
A 1 73  ASP 73  71  71  ASP ASP B . n 
A 1 74  ASP 74  72  72  ASP ASP B . n 
A 1 75  THR 75  73  73  THR THR B . n 
A 1 76  GLU 76  74  74  GLU GLU B . n 
A 1 77  ASN 77  75  75  ASN ASN B . n 
A 1 78  LYS 78  76  76  LYS LYS B . n 
A 1 79  SER 79  77  77  SER SER B . n 
A 1 80  VAL 80  78  78  VAL VAL B . n 
A 1 81  LEU 81  79  79  LEU LEU B . n 
A 1 82  ARG 82  80  80  ARG ARG B . n 
A 1 83  GLY 83  81  81  GLY GLY B . n 
A 1 84  GLY 84  82  82  GLY GLY B . n 
A 1 85  PRO 85  83  83  PRO PRO B . n 
A 1 86  LEU 86  84  84  LEU LEU B . n 
A 1 87  THR 87  85  85  THR THR B . n 
A 1 88  GLY 88  86  86  GLY GLY B . n 
A 1 89  SER 89  87  87  SER SER B . n 
A 1 90  TYR 90  88  88  TYR TYR B . n 
A 1 91  ARG 91  89  89  ARG ARG B . n 
A 1 92  LEU 92  90  90  LEU LEU B . n 
A 1 93  ARG 93  91  91  ARG ARG B . n 
A 1 94  GLN 94  92  92  GLN GLN B . n 
A 1 95  VAL 95  93  93  VAL VAL B . n 
A 1 96  HIS 96  94  94  HIS HIS B . n 
A 1 97  LEU 97  95  95  LEU LEU B . n 
A 1 98  HIS 98  96  96  HIS HIS B . n 
A 1 99  TRP 99  97  97  TRP TRP B . n 
A 1 100 GLY 100 98  98  GLY GLY B . n 
A 1 101 SER 101 99  99  SER SER B . n 
A 1 102 ALA 102 100 100 ALA ALA B . n 
A 1 103 ASP 103 101 101 ASP ASP B . n 
A 1 104 ASP 104 102 102 ASP ASP B . n 
A 1 105 HIS 105 103 103 HIS HIS B . n 
A 1 106 GLY 106 104 104 GLY GLY B . n 
A 1 107 SER 107 105 105 SER SER B . n 
A 1 108 GLU 108 106 106 GLU GLU B . n 
A 1 109 HIS 109 107 107 HIS HIS B . n 
A 1 110 ILE 110 108 108 ILE ILE B . n 
A 1 111 VAL 111 109 109 VAL VAL B . n 
A 1 112 ASP 112 110 110 ASP ASP B . n 
A 1 113 GLY 113 111 111 GLY GLY B . n 
A 1 114 VAL 114 112 112 VAL VAL B . n 
A 1 115 SER 115 113 113 SER SER B . n 
A 1 116 TYR 116 114 114 TYR TYR B . n 
A 1 117 ALA 117 115 115 ALA ALA B . n 
A 1 118 ALA 118 116 116 ALA ALA B . n 
A 1 119 GLU 119 117 117 GLU GLU B . n 
A 1 120 LEU 120 118 118 LEU LEU B . n 
A 1 121 HIS 121 119 119 HIS HIS B . n 
A 1 122 VAL 122 120 120 VAL VAL B . n 
A 1 123 VAL 123 121 121 VAL VAL B . n 
A 1 124 HIS 124 122 122 HIS HIS B . n 
A 1 125 TRP 125 123 123 TRP TRP B . n 
A 1 126 ASN 126 124 124 ASN ASN B . n 
A 1 127 SER 127 125 125 SER SER B . n 
A 1 128 ASP 128 126 126 ASP ASP B . n 
A 1 129 LYS 129 127 127 LYS LYS B . n 
A 1 130 TYR 130 128 128 TYR TYR B . n 
A 1 131 PRO 131 129 129 PRO PRO B . n 
A 1 132 SER 132 130 130 SER SER B . n 
A 1 133 PHE 133 131 131 PHE PHE B . n 
A 1 134 VAL 134 132 132 VAL VAL B . n 
A 1 135 GLU 135 133 133 GLU GLU B . n 
A 1 136 ALA 136 134 134 ALA ALA B . n 
A 1 137 ALA 137 135 135 ALA ALA B . n 
A 1 138 HIS 138 136 136 HIS HIS B . n 
A 1 139 GLU 139 137 137 GLU GLU B . n 
A 1 140 PRO 140 138 138 PRO PRO B . n 
A 1 141 ASP 141 139 139 ASP ASP B . n 
A 1 142 GLY 142 140 140 GLY GLY B . n 
A 1 143 LEU 143 141 141 LEU LEU B . n 
A 1 144 ALA 144 142 142 ALA ALA B . n 
A 1 145 VAL 145 143 143 VAL VAL B . n 
A 1 146 LEU 146 144 144 LEU LEU B . n 
A 1 147 GLY 147 145 145 GLY GLY B . n 
A 1 148 VAL 148 146 146 VAL VAL B . n 
A 1 149 PHE 149 147 147 PHE PHE B . n 
A 1 150 LEU 150 148 148 LEU LEU B . n 
A 1 151 GLN 151 149 149 GLN GLN B . n 
A 1 152 ILE 152 150 150 ILE ILE B . n 
A 1 153 GLY 153 151 151 GLY GLY B . n 
A 1 154 GLU 154 152 152 GLU GLU B . n 
A 1 155 PRO 155 153 153 PRO PRO B . n 
A 1 156 ASN 156 154 154 ASN ASN B . n 
A 1 157 SER 157 155 155 SER SER B . n 
A 1 158 GLN 158 156 156 GLN GLN B . n 
A 1 159 LEU 159 157 157 LEU LEU B . n 
A 1 160 GLN 160 158 158 GLN GLN B . n 
A 1 161 LYS 161 159 159 LYS LYS B . n 
A 1 162 ILE 162 160 160 ILE ILE B . n 
A 1 163 THR 163 161 161 THR THR B . n 
A 1 164 ASP 164 162 162 ASP ASP B . n 
A 1 165 THR 165 163 163 THR THR B . n 
A 1 166 LEU 166 164 164 LEU LEU B . n 
A 1 167 ASP 167 165 165 ASP ASP B . n 
A 1 168 SER 168 166 166 SER SER B . n 
A 1 169 ILE 169 167 167 ILE ILE B . n 
A 1 170 LYS 170 168 168 LYS LYS B . n 
A 1 171 GLU 171 169 169 GLU GLU B . n 
A 1 172 LYS 172 170 170 LYS LYS B . n 
A 1 173 GLY 173 171 171 GLY GLY B . n 
A 1 174 LYS 174 172 172 LYS LYS B . n 
A 1 175 GLN 175 173 173 GLN GLN B . n 
A 1 176 THR 176 174 174 THR THR B . n 
A 1 177 ARG 177 175 175 ARG ARG B . n 
A 1 178 PHE 178 176 176 PHE PHE B . n 
A 1 179 THR 179 177 177 THR THR B . n 
A 1 180 ASN 180 178 178 ASN ASN B . n 
A 1 181 PHE 181 179 179 PHE PHE B . n 
A 1 182 ASP 182 180 180 ASP ASP B . n 
A 1 183 LEU 183 181 181 LEU LEU B . n 
A 1 184 LEU 184 182 182 LEU LEU B . n 
A 1 185 SER 185 183 183 SER SER B . n 
A 1 186 LEU 186 184 184 LEU LEU B . n 
A 1 187 LEU 187 185 185 LEU LEU B . n 
A 1 188 PRO 188 186 186 PRO PRO B . n 
A 1 189 PRO 189 187 187 PRO PRO B . n 
A 1 190 SER 190 188 188 SER SER B . n 
A 1 191 TRP 191 189 189 TRP TRP B . n 
A 1 192 ASP 192 190 190 ASP ASP B . n 
A 1 193 TYR 193 191 191 TYR TYR B . n 
A 1 194 TRP 194 192 192 TRP TRP B . n 
A 1 195 THR 195 193 193 THR THR B . n 
A 1 196 TYR 196 194 194 TYR TYR B . n 
A 1 197 PRO 197 195 195 PRO PRO B . n 
A 1 198 GLY 198 196 196 GLY GLY B . n 
A 1 199 SER 199 197 197 SER SER B . n 
A 1 200 LEU 200 198 198 LEU LEU B . n 
A 1 201 THR 201 199 199 THR THR B . n 
A 1 202 VAL 202 200 200 VAL VAL B . n 
A 1 203 PRO 203 201 201 PRO PRO B . n 
A 1 204 PRO 204 202 202 PRO PRO B . n 
A 1 205 LEU 205 203 203 LEU LEU B . n 
A 1 206 LEU 206 204 204 LEU LEU B . n 
A 1 207 GLU 207 205 205 GLU GLU B . n 
A 1 208 SER 208 206 206 SER SER B . n 
A 1 209 VAL 209 207 207 VAL VAL B . n 
A 1 210 THR 210 208 208 THR THR B . n 
A 1 211 TRP 211 209 209 TRP TRP B . n 
A 1 212 ILE 212 210 210 ILE ILE B . n 
A 1 213 VAL 213 211 211 VAL VAL B . n 
A 1 214 LEU 214 212 212 LEU LEU B . n 
A 1 215 LYS 215 213 213 LYS LYS B . n 
A 1 216 GLN 216 214 214 GLN GLN B . n 
A 1 217 PRO 217 215 215 PRO PRO B . n 
A 1 218 ILE 218 216 216 ILE ILE B . n 
A 1 219 ASN 219 217 217 ASN ASN B . n 
A 1 220 ILE 220 218 218 ILE ILE B . n 
A 1 221 SER 221 219 219 SER SER B . n 
A 1 222 SER 222 220 220 SER SER B . n 
A 1 223 GLN 223 221 221 GLN GLN B . n 
A 1 224 GLN 224 222 222 GLN GLN B . n 
A 1 225 LEU 225 223 223 LEU LEU B . n 
A 1 226 ALA 226 224 224 ALA ALA B . n 
A 1 227 LYS 227 225 225 LYS LYS B . n 
A 1 228 PHE 228 226 226 PHE PHE B . n 
A 1 229 ARG 229 227 227 ARG ARG B . n 
A 1 230 SER 230 228 228 SER SER B . n 
A 1 231 LEU 231 229 229 LEU LEU B . n 
A 1 232 LEU 232 230 230 LEU LEU B . n 
A 1 233 CYS 233 231 231 CYS CYS B . n 
A 1 234 THR 234 232 232 THR THR B . n 
A 1 235 ALA 235 233 233 ALA ALA B . n 
A 1 236 GLU 236 234 234 GLU GLU B . n 
A 1 237 GLY 237 235 235 GLY GLY B . n 
A 1 238 GLU 238 236 236 GLU GLU B . n 
A 1 239 ALA 239 237 237 ALA ALA B . n 
A 1 240 ALA 240 238 238 ALA ALA B . n 
A 1 241 ALA 241 239 239 ALA ALA B . n 
A 1 242 PHE 242 240 240 PHE PHE B . n 
A 1 243 LEU 243 241 241 LEU LEU B . n 
A 1 244 VAL 244 242 242 VAL VAL B . n 
A 1 245 SER 245 243 243 SER SER B . n 
A 1 246 ASN 246 244 244 ASN ASN B . n 
A 1 247 HIS 247 245 245 HIS HIS B . n 
A 1 248 ARG 248 246 246 ARG ARG B . n 
A 1 249 PRO 249 247 247 PRO PRO B . n 
A 1 250 PRO 250 248 248 PRO PRO B . n 
A 1 251 GLN 251 249 249 GLN GLN B . n 
A 1 252 PRO 252 250 250 PRO PRO B . n 
A 1 253 LEU 253 251 251 LEU LEU B . n 
A 1 254 LYS 254 252 252 LYS LYS B . n 
A 1 255 GLY 255 253 253 GLY GLY B . n 
A 1 256 ARG 256 254 254 ARG ARG B . n 
A 1 257 LYS 257 255 255 LYS LYS B . n 
A 1 258 VAL 258 256 256 VAL VAL B . n 
A 1 259 ARG 259 257 257 ARG ARG B . n 
A 1 260 ALA 260 258 258 ALA ALA B . n 
A 1 261 SER 261 259 259 SER SER B . n 
A 1 262 PHE 262 260 260 PHE PHE B . n 
A 1 263 HIS 263 261 261 HIS HIS B . n 
B 1 1   MET 1   -1  ?   ?   ?   A . n 
B 1 2   MET 2   0   ?   ?   ?   A . n 
B 1 3   SER 3   1   ?   ?   ?   A . n 
B 1 4   ARG 4   2   2   ARG ARG A . n 
B 1 5   LEU 5   3   3   LEU LEU A . n 
B 1 6   SER 6   4   4   SER SER A . n 
B 1 7   TRP 7   5   5   TRP TRP A . n 
B 1 8   GLY 8   6   6   GLY GLY A . n 
B 1 9   TYR 9   7   7   TYR TYR A . n 
B 1 10  ARG 10  8   8   ARG ARG A . n 
B 1 11  GLU 11  9   9   GLU GLU A . n 
B 1 12  HIS 12  10  10  HIS HIS A . n 
B 1 13  ASN 13  11  11  ASN ASN A . n 
B 1 14  GLY 14  12  12  GLY GLY A . n 
B 1 15  PRO 15  13  13  PRO PRO A . n 
B 1 16  ILE 16  14  14  ILE ILE A . n 
B 1 17  HIS 17  15  15  HIS HIS A . n 
B 1 18  TRP 18  16  16  TRP TRP A . n 
B 1 19  LYS 19  17  17  LYS LYS A . n 
B 1 20  GLU 20  18  18  GLU GLU A . n 
B 1 21  PHE 21  19  19  PHE PHE A . n 
B 1 22  PHE 22  20  20  PHE PHE A . n 
B 1 23  PRO 23  21  21  PRO PRO A . n 
B 1 24  ILE 24  22  22  ILE ILE A . n 
B 1 25  ALA 25  23  23  ALA ALA A . n 
B 1 26  ASP 26  24  24  ASP ASP A . n 
B 1 27  GLY 27  25  25  GLY GLY A . n 
B 1 28  ASP 28  26  26  ASP ASP A . n 
B 1 29  GLN 29  27  27  GLN GLN A . n 
B 1 30  GLN 30  28  28  GLN GLN A . n 
B 1 31  SER 31  29  29  SER SER A . n 
B 1 32  PRO 32  30  30  PRO PRO A . n 
B 1 33  ILE 33  31  31  ILE ILE A . n 
B 1 34  GLU 34  32  32  GLU GLU A . n 
B 1 35  ILE 35  33  33  ILE ILE A . n 
B 1 36  LYS 36  34  34  LYS LYS A . n 
B 1 37  THR 37  35  35  THR THR A . n 
B 1 38  LYS 38  36  36  LYS LYS A . n 
B 1 39  GLU 39  37  37  GLU GLU A . n 
B 1 40  VAL 40  38  38  VAL VAL A . n 
B 1 41  LYS 41  39  39  LYS LYS A . n 
B 1 42  TYR 42  40  40  TYR TYR A . n 
B 1 43  ASP 43  41  41  ASP ASP A . n 
B 1 44  SER 44  42  42  SER SER A . n 
B 1 45  SER 45  43  43  SER SER A . n 
B 1 46  LEU 46  44  44  LEU LEU A . n 
B 1 47  ARG 47  45  45  ARG ARG A . n 
B 1 48  PRO 48  46  46  PRO PRO A . n 
B 1 49  LEU 49  47  47  LEU LEU A . n 
B 1 50  SER 50  48  48  SER SER A . n 
B 1 51  ILE 51  49  49  ILE ILE A . n 
B 1 52  LYS 52  50  50  LYS LYS A . n 
B 1 53  TYR 53  51  51  TYR TYR A . n 
B 1 54  ASP 54  52  52  ASP ASP A . n 
B 1 55  PRO 55  53  53  PRO PRO A . n 
B 1 56  SER 56  54  54  SER SER A . n 
B 1 57  SER 57  55  55  SER SER A . n 
B 1 58  ALA 58  56  56  ALA ALA A . n 
B 1 59  LYS 59  57  57  LYS LYS A . n 
B 1 60  ILE 60  58  58  ILE ILE A . n 
B 1 61  ILE 61  59  59  ILE ILE A . n 
B 1 62  SER 62  60  60  SER SER A . n 
B 1 63  ASN 63  61  61  ASN ASN A . n 
B 1 64  SER 64  62  62  SER SER A . n 
B 1 65  GLY 65  63  63  GLY GLY A . n 
B 1 66  HIS 66  64  64  HIS HIS A . n 
B 1 67  SER 67  65  65  SER SER A . n 
B 1 68  PHE 68  66  66  PHE PHE A . n 
B 1 69  ASN 69  67  67  ASN ASN A . n 
B 1 70  VAL 70  68  68  VAL VAL A . n 
B 1 71  ASP 71  69  69  ASP ASP A . n 
B 1 72  PHE 72  70  70  PHE PHE A . n 
B 1 73  ASP 73  71  71  ASP ASP A . n 
B 1 74  ASP 74  72  72  ASP ASP A . n 
B 1 75  THR 75  73  73  THR THR A . n 
B 1 76  GLU 76  74  74  GLU GLU A . n 
B 1 77  ASN 77  75  75  ASN ASN A . n 
B 1 78  LYS 78  76  76  LYS LYS A . n 
B 1 79  SER 79  77  77  SER SER A . n 
B 1 80  VAL 80  78  78  VAL VAL A . n 
B 1 81  LEU 81  79  79  LEU LEU A . n 
B 1 82  ARG 82  80  80  ARG ARG A . n 
B 1 83  GLY 83  81  81  GLY GLY A . n 
B 1 84  GLY 84  82  82  GLY GLY A . n 
B 1 85  PRO 85  83  83  PRO PRO A . n 
B 1 86  LEU 86  84  84  LEU LEU A . n 
B 1 87  THR 87  85  85  THR THR A . n 
B 1 88  GLY 88  86  86  GLY GLY A . n 
B 1 89  SER 89  87  87  SER SER A . n 
B 1 90  TYR 90  88  88  TYR TYR A . n 
B 1 91  ARG 91  89  89  ARG ARG A . n 
B 1 92  LEU 92  90  90  LEU LEU A . n 
B 1 93  ARG 93  91  91  ARG ARG A . n 
B 1 94  GLN 94  92  92  GLN GLN A . n 
B 1 95  VAL 95  93  93  VAL VAL A . n 
B 1 96  HIS 96  94  94  HIS HIS A . n 
B 1 97  LEU 97  95  95  LEU LEU A . n 
B 1 98  HIS 98  96  96  HIS HIS A . n 
B 1 99  TRP 99  97  97  TRP TRP A . n 
B 1 100 GLY 100 98  98  GLY GLY A . n 
B 1 101 SER 101 99  99  SER SER A . n 
B 1 102 ALA 102 100 100 ALA ALA A . n 
B 1 103 ASP 103 101 101 ASP ASP A . n 
B 1 104 ASP 104 102 102 ASP ASP A . n 
B 1 105 HIS 105 103 103 HIS HIS A . n 
B 1 106 GLY 106 104 104 GLY GLY A . n 
B 1 107 SER 107 105 105 SER SER A . n 
B 1 108 GLU 108 106 106 GLU GLU A . n 
B 1 109 HIS 109 107 107 HIS HIS A . n 
B 1 110 ILE 110 108 108 ILE ILE A . n 
B 1 111 VAL 111 109 109 VAL VAL A . n 
B 1 112 ASP 112 110 110 ASP ASP A . n 
B 1 113 GLY 113 111 111 GLY GLY A . n 
B 1 114 VAL 114 112 112 VAL VAL A . n 
B 1 115 SER 115 113 113 SER SER A . n 
B 1 116 TYR 116 114 114 TYR TYR A . n 
B 1 117 ALA 117 115 115 ALA ALA A . n 
B 1 118 ALA 118 116 116 ALA ALA A . n 
B 1 119 GLU 119 117 117 GLU GLU A . n 
B 1 120 LEU 120 118 118 LEU LEU A . n 
B 1 121 HIS 121 119 119 HIS HIS A . n 
B 1 122 VAL 122 120 120 VAL VAL A . n 
B 1 123 VAL 123 121 121 VAL VAL A . n 
B 1 124 HIS 124 122 122 HIS HIS A . n 
B 1 125 TRP 125 123 123 TRP TRP A . n 
B 1 126 ASN 126 124 124 ASN ASN A . n 
B 1 127 SER 127 125 125 SER SER A . n 
B 1 128 ASP 128 126 126 ASP ASP A . n 
B 1 129 LYS 129 127 127 LYS LYS A . n 
B 1 130 TYR 130 128 128 TYR TYR A . n 
B 1 131 PRO 131 129 129 PRO PRO A . n 
B 1 132 SER 132 130 130 SER SER A . n 
B 1 133 PHE 133 131 131 PHE PHE A . n 
B 1 134 VAL 134 132 132 VAL VAL A . n 
B 1 135 GLU 135 133 133 GLU GLU A . n 
B 1 136 ALA 136 134 134 ALA ALA A . n 
B 1 137 ALA 137 135 135 ALA ALA A . n 
B 1 138 HIS 138 136 136 HIS HIS A . n 
B 1 139 GLU 139 137 137 GLU GLU A . n 
B 1 140 PRO 140 138 138 PRO PRO A . n 
B 1 141 ASP 141 139 139 ASP ASP A . n 
B 1 142 GLY 142 140 140 GLY GLY A . n 
B 1 143 LEU 143 141 141 LEU LEU A . n 
B 1 144 ALA 144 142 142 ALA ALA A . n 
B 1 145 VAL 145 143 143 VAL VAL A . n 
B 1 146 LEU 146 144 144 LEU LEU A . n 
B 1 147 GLY 147 145 145 GLY GLY A . n 
B 1 148 VAL 148 146 146 VAL VAL A . n 
B 1 149 PHE 149 147 147 PHE PHE A . n 
B 1 150 LEU 150 148 148 LEU LEU A . n 
B 1 151 GLN 151 149 149 GLN GLN A . n 
B 1 152 ILE 152 150 150 ILE ILE A . n 
B 1 153 GLY 153 151 151 GLY GLY A . n 
B 1 154 GLU 154 152 152 GLU GLU A . n 
B 1 155 PRO 155 153 153 PRO PRO A . n 
B 1 156 ASN 156 154 154 ASN ASN A . n 
B 1 157 SER 157 155 155 SER SER A . n 
B 1 158 GLN 158 156 156 GLN GLN A . n 
B 1 159 LEU 159 157 157 LEU LEU A . n 
B 1 160 GLN 160 158 158 GLN GLN A . n 
B 1 161 LYS 161 159 159 LYS LYS A . n 
B 1 162 ILE 162 160 160 ILE ILE A . n 
B 1 163 THR 163 161 161 THR THR A . n 
B 1 164 ASP 164 162 162 ASP ASP A . n 
B 1 165 THR 165 163 163 THR THR A . n 
B 1 166 LEU 166 164 164 LEU LEU A . n 
B 1 167 ASP 167 165 165 ASP ASP A . n 
B 1 168 SER 168 166 166 SER SER A . n 
B 1 169 ILE 169 167 167 ILE ILE A . n 
B 1 170 LYS 170 168 168 LYS LYS A . n 
B 1 171 GLU 171 169 169 GLU GLU A . n 
B 1 172 LYS 172 170 170 LYS LYS A . n 
B 1 173 GLY 173 171 171 GLY GLY A . n 
B 1 174 LYS 174 172 172 LYS LYS A . n 
B 1 175 GLN 175 173 173 GLN GLN A . n 
B 1 176 THR 176 174 174 THR THR A . n 
B 1 177 ARG 177 175 175 ARG ARG A . n 
B 1 178 PHE 178 176 176 PHE PHE A . n 
B 1 179 THR 179 177 177 THR THR A . n 
B 1 180 ASN 180 178 178 ASN ASN A . n 
B 1 181 PHE 181 179 179 PHE PHE A . n 
B 1 182 ASP 182 180 180 ASP ASP A . n 
B 1 183 LEU 183 181 181 LEU LEU A . n 
B 1 184 LEU 184 182 182 LEU LEU A . n 
B 1 185 SER 185 183 183 SER SER A . n 
B 1 186 LEU 186 184 184 LEU LEU A . n 
B 1 187 LEU 187 185 185 LEU LEU A . n 
B 1 188 PRO 188 186 186 PRO PRO A . n 
B 1 189 PRO 189 187 187 PRO PRO A . n 
B 1 190 SER 190 188 188 SER SER A . n 
B 1 191 TRP 191 189 189 TRP TRP A . n 
B 1 192 ASP 192 190 190 ASP ASP A . n 
B 1 193 TYR 193 191 191 TYR TYR A . n 
B 1 194 TRP 194 192 192 TRP TRP A . n 
B 1 195 THR 195 193 193 THR THR A . n 
B 1 196 TYR 196 194 194 TYR TYR A . n 
B 1 197 PRO 197 195 195 PRO PRO A . n 
B 1 198 GLY 198 196 196 GLY GLY A . n 
B 1 199 SER 199 197 197 SER SER A . n 
B 1 200 LEU 200 198 198 LEU LEU A . n 
B 1 201 THR 201 199 199 THR THR A . n 
B 1 202 VAL 202 200 200 VAL VAL A . n 
B 1 203 PRO 203 201 201 PRO PRO A . n 
B 1 204 PRO 204 202 202 PRO PRO A . n 
B 1 205 LEU 205 203 203 LEU LEU A . n 
B 1 206 LEU 206 204 204 LEU LEU A . n 
B 1 207 GLU 207 205 205 GLU GLU A . n 
B 1 208 SER 208 206 206 SER SER A . n 
B 1 209 VAL 209 207 207 VAL VAL A . n 
B 1 210 THR 210 208 208 THR THR A . n 
B 1 211 TRP 211 209 209 TRP TRP A . n 
B 1 212 ILE 212 210 210 ILE ILE A . n 
B 1 213 VAL 213 211 211 VAL VAL A . n 
B 1 214 LEU 214 212 212 LEU LEU A . n 
B 1 215 LYS 215 213 213 LYS LYS A . n 
B 1 216 GLN 216 214 214 GLN GLN A . n 
B 1 217 PRO 217 215 215 PRO PRO A . n 
B 1 218 ILE 218 216 216 ILE ILE A . n 
B 1 219 ASN 219 217 217 ASN ASN A . n 
B 1 220 ILE 220 218 218 ILE ILE A . n 
B 1 221 SER 221 219 219 SER SER A . n 
B 1 222 SER 222 220 220 SER SER A . n 
B 1 223 GLN 223 221 221 GLN GLN A . n 
B 1 224 GLN 224 222 222 GLN GLN A . n 
B 1 225 LEU 225 223 223 LEU LEU A . n 
B 1 226 ALA 226 224 224 ALA ALA A . n 
B 1 227 LYS 227 225 225 LYS LYS A . n 
B 1 228 PHE 228 226 226 PHE PHE A . n 
B 1 229 ARG 229 227 227 ARG ARG A . n 
B 1 230 SER 230 228 228 SER SER A . n 
B 1 231 LEU 231 229 229 LEU LEU A . n 
B 1 232 LEU 232 230 230 LEU LEU A . n 
B 1 233 CYS 233 231 231 CYS CYS A . n 
B 1 234 THR 234 232 232 THR THR A . n 
B 1 235 ALA 235 233 233 ALA ALA A . n 
B 1 236 GLU 236 234 234 GLU GLU A . n 
B 1 237 GLY 237 235 235 GLY GLY A . n 
B 1 238 GLU 238 236 236 GLU GLU A . n 
B 1 239 ALA 239 237 237 ALA ALA A . n 
B 1 240 ALA 240 238 238 ALA ALA A . n 
B 1 241 ALA 241 239 239 ALA ALA A . n 
B 1 242 PHE 242 240 240 PHE PHE A . n 
B 1 243 LEU 243 241 241 LEU LEU A . n 
B 1 244 VAL 244 242 242 VAL VAL A . n 
B 1 245 SER 245 243 243 SER SER A . n 
B 1 246 ASN 246 244 244 ASN ASN A . n 
B 1 247 HIS 247 245 245 HIS HIS A . n 
B 1 248 ARG 248 246 246 ARG ARG A . n 
B 1 249 PRO 249 247 247 PRO PRO A . n 
B 1 250 PRO 250 248 248 PRO PRO A . n 
B 1 251 GLN 251 249 249 GLN GLN A . n 
B 1 252 PRO 252 250 250 PRO PRO A . n 
B 1 253 LEU 253 251 251 LEU LEU A . n 
B 1 254 LYS 254 252 252 LYS LYS A . n 
B 1 255 GLY 255 253 253 GLY GLY A . n 
B 1 256 ARG 256 254 254 ARG ARG A . n 
B 1 257 LYS 257 255 255 LYS LYS A . n 
B 1 258 VAL 258 256 256 VAL VAL A . n 
B 1 259 ARG 259 257 257 ARG ARG A . n 
B 1 260 ALA 260 258 258 ALA ALA A . n 
B 1 261 SER 261 259 259 SER SER A . n 
B 1 262 PHE 262 260 260 PHE PHE A . n 
B 1 263 HIS 263 261 261 HIS HIS 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 
C 2 ZN  1   301 301 ZN  ZN  B . 
D 3 EWW 1   302 302 EWW EWW B . 
E 4 PEG 1   303 303 PEG PEG B . 
F 5 DMS 1   304 304 DMS DMS B . 
G 6 CIT 1   305 305 CIT CIT B . 
H 4 PEG 1   306 306 PEG PEG B . 
I 7 EDO 1   307 307 EDO EDO B . 
J 6 CIT 1   308 308 CIT CIT B . 
K 7 EDO 1   309 309 EDO EDO B . 
L 2 ZN  1   301 301 ZN  ZN  A . 
M 3 EWW 1   302 302 EWW EWW A . 
N 8 NI  1   303 303 NI  NI  A . 
O 9 HOH 1   401 401 HOH HOH B . 
O 9 HOH 2   402 402 HOH HOH B . 
O 9 HOH 3   403 403 HOH HOH B . 
O 9 HOH 4   404 404 HOH HOH B . 
O 9 HOH 5   405 405 HOH HOH B . 
O 9 HOH 6   406 406 HOH HOH B . 
O 9 HOH 7   407 407 HOH HOH B . 
O 9 HOH 8   408 408 HOH HOH B . 
O 9 HOH 9   409 409 HOH HOH B . 
O 9 HOH 10  410 410 HOH HOH B . 
O 9 HOH 11  411 411 HOH HOH B . 
O 9 HOH 12  412 412 HOH HOH B . 
O 9 HOH 13  413 413 HOH HOH B . 
O 9 HOH 14  414 414 HOH HOH B . 
O 9 HOH 15  415 415 HOH HOH B . 
O 9 HOH 16  416 416 HOH HOH B . 
O 9 HOH 17  417 417 HOH HOH B . 
O 9 HOH 18  418 418 HOH HOH B . 
O 9 HOH 19  419 419 HOH HOH B . 
O 9 HOH 20  420 420 HOH HOH B . 
O 9 HOH 21  421 421 HOH HOH B . 
O 9 HOH 22  422 422 HOH HOH B . 
O 9 HOH 23  423 423 HOH HOH B . 
O 9 HOH 24  424 424 HOH HOH B . 
O 9 HOH 25  425 425 HOH HOH B . 
O 9 HOH 26  426 426 HOH HOH B . 
O 9 HOH 27  427 427 HOH HOH B . 
O 9 HOH 28  428 428 HOH HOH B . 
O 9 HOH 29  429 429 HOH HOH B . 
O 9 HOH 30  430 430 HOH HOH B . 
O 9 HOH 31  431 431 HOH HOH B . 
O 9 HOH 32  432 432 HOH HOH B . 
O 9 HOH 33  433 433 HOH HOH B . 
O 9 HOH 34  434 434 HOH HOH B . 
O 9 HOH 35  435 435 HOH HOH B . 
O 9 HOH 36  436 436 HOH HOH B . 
O 9 HOH 37  437 437 HOH HOH B . 
O 9 HOH 38  438 438 HOH HOH B . 
O 9 HOH 39  439 439 HOH HOH B . 
O 9 HOH 40  440 440 HOH HOH B . 
O 9 HOH 41  441 441 HOH HOH B . 
O 9 HOH 42  442 442 HOH HOH B . 
O 9 HOH 43  443 443 HOH HOH B . 
O 9 HOH 44  444 444 HOH HOH B . 
O 9 HOH 45  445 445 HOH HOH B . 
O 9 HOH 46  446 446 HOH HOH B . 
O 9 HOH 47  447 447 HOH HOH B . 
O 9 HOH 48  448 448 HOH HOH B . 
O 9 HOH 49  449 449 HOH HOH B . 
O 9 HOH 50  450 450 HOH HOH B . 
O 9 HOH 51  451 451 HOH HOH B . 
O 9 HOH 52  452 452 HOH HOH B . 
O 9 HOH 53  453 453 HOH HOH B . 
O 9 HOH 54  454 454 HOH HOH B . 
O 9 HOH 55  455 455 HOH HOH B . 
O 9 HOH 56  456 456 HOH HOH B . 
O 9 HOH 57  457 457 HOH HOH B . 
O 9 HOH 58  458 458 HOH HOH B . 
O 9 HOH 59  459 459 HOH HOH B . 
O 9 HOH 60  460 460 HOH HOH B . 
O 9 HOH 61  461 461 HOH HOH B . 
O 9 HOH 62  462 462 HOH HOH B . 
O 9 HOH 63  463 463 HOH HOH B . 
O 9 HOH 64  464 464 HOH HOH B . 
O 9 HOH 65  465 465 HOH HOH B . 
O 9 HOH 66  466 466 HOH HOH B . 
O 9 HOH 67  467 467 HOH HOH B . 
O 9 HOH 68  468 468 HOH HOH B . 
O 9 HOH 69  469 469 HOH HOH B . 
O 9 HOH 70  470 470 HOH HOH B . 
O 9 HOH 71  471 471 HOH HOH B . 
O 9 HOH 72  472 472 HOH HOH B . 
O 9 HOH 73  473 473 HOH HOH B . 
O 9 HOH 74  474 474 HOH HOH B . 
O 9 HOH 75  475 475 HOH HOH B . 
O 9 HOH 76  476 476 HOH HOH B . 
O 9 HOH 77  477 477 HOH HOH B . 
O 9 HOH 78  478 478 HOH HOH B . 
O 9 HOH 79  479 479 HOH HOH B . 
O 9 HOH 80  480 480 HOH HOH B . 
O 9 HOH 81  481 481 HOH HOH B . 
O 9 HOH 82  482 482 HOH HOH B . 
O 9 HOH 83  483 483 HOH HOH B . 
O 9 HOH 84  484 484 HOH HOH B . 
O 9 HOH 85  485 485 HOH HOH B . 
O 9 HOH 86  486 486 HOH HOH B . 
O 9 HOH 87  487 487 HOH HOH B . 
O 9 HOH 88  488 488 HOH HOH B . 
O 9 HOH 89  489 489 HOH HOH B . 
O 9 HOH 90  490 490 HOH HOH B . 
O 9 HOH 91  491 491 HOH HOH B . 
O 9 HOH 92  492 492 HOH HOH B . 
O 9 HOH 93  493 493 HOH HOH B . 
O 9 HOH 94  494 494 HOH HOH B . 
O 9 HOH 95  495 495 HOH HOH B . 
O 9 HOH 96  496 496 HOH HOH B . 
O 9 HOH 97  497 497 HOH HOH B . 
O 9 HOH 98  498 498 HOH HOH B . 
O 9 HOH 99  499 499 HOH HOH B . 
O 9 HOH 100 500 500 HOH HOH B . 
O 9 HOH 101 501 501 HOH HOH B . 
O 9 HOH 102 502 502 HOH HOH B . 
O 9 HOH 103 503 503 HOH HOH B . 
O 9 HOH 104 504 504 HOH HOH B . 
O 9 HOH 105 505 505 HOH HOH B . 
O 9 HOH 106 506 506 HOH HOH B . 
O 9 HOH 107 507 507 HOH HOH B . 
O 9 HOH 108 508 508 HOH HOH B . 
O 9 HOH 109 509 509 HOH HOH B . 
O 9 HOH 110 510 510 HOH HOH B . 
O 9 HOH 111 511 511 HOH HOH B . 
O 9 HOH 112 512 512 HOH HOH B . 
O 9 HOH 113 513 513 HOH HOH B . 
O 9 HOH 114 514 514 HOH HOH B . 
O 9 HOH 115 515 515 HOH HOH B . 
O 9 HOH 116 516 516 HOH HOH B . 
O 9 HOH 117 517 517 HOH HOH B . 
O 9 HOH 118 518 518 HOH HOH B . 
O 9 HOH 119 519 519 HOH HOH B . 
O 9 HOH 120 520 520 HOH HOH B . 
O 9 HOH 121 521 521 HOH HOH B . 
O 9 HOH 122 522 522 HOH HOH B . 
O 9 HOH 123 523 523 HOH HOH B . 
O 9 HOH 124 524 524 HOH HOH B . 
O 9 HOH 125 525 525 HOH HOH B . 
O 9 HOH 126 526 526 HOH HOH B . 
O 9 HOH 127 527 527 HOH HOH B . 
O 9 HOH 128 528 528 HOH HOH B . 
O 9 HOH 129 529 529 HOH HOH B . 
O 9 HOH 130 530 530 HOH HOH B . 
O 9 HOH 131 531 531 HOH HOH B . 
O 9 HOH 132 532 532 HOH HOH B . 
O 9 HOH 133 533 533 HOH HOH B . 
O 9 HOH 134 534 534 HOH HOH B . 
O 9 HOH 135 535 535 HOH HOH B . 
O 9 HOH 136 536 536 HOH HOH B . 
O 9 HOH 137 537 537 HOH HOH B . 
O 9 HOH 138 538 538 HOH HOH B . 
O 9 HOH 139 539 539 HOH HOH B . 
O 9 HOH 140 540 540 HOH HOH B . 
O 9 HOH 141 541 541 HOH HOH B . 
O 9 HOH 142 542 542 HOH HOH B . 
O 9 HOH 143 543 543 HOH HOH B . 
O 9 HOH 144 544 544 HOH HOH B . 
O 9 HOH 145 545 545 HOH HOH B . 
O 9 HOH 146 546 546 HOH HOH B . 
O 9 HOH 147 547 547 HOH HOH B . 
O 9 HOH 148 548 548 HOH HOH B . 
O 9 HOH 149 549 549 HOH HOH B . 
O 9 HOH 150 550 550 HOH HOH B . 
O 9 HOH 151 551 551 HOH HOH B . 
O 9 HOH 152 552 552 HOH HOH B . 
O 9 HOH 153 553 553 HOH HOH B . 
O 9 HOH 154 554 554 HOH HOH B . 
O 9 HOH 155 555 555 HOH HOH B . 
O 9 HOH 156 556 556 HOH HOH B . 
O 9 HOH 157 557 557 HOH HOH B . 
O 9 HOH 158 558 558 HOH HOH B . 
O 9 HOH 159 559 559 HOH HOH B . 
O 9 HOH 160 560 560 HOH HOH B . 
O 9 HOH 161 561 561 HOH HOH B . 
O 9 HOH 162 562 562 HOH HOH B . 
O 9 HOH 163 563 563 HOH HOH B . 
O 9 HOH 164 564 564 HOH HOH B . 
O 9 HOH 165 565 565 HOH HOH B . 
O 9 HOH 166 566 566 HOH HOH B . 
O 9 HOH 167 567 567 HOH HOH B . 
O 9 HOH 168 568 568 HOH HOH B . 
O 9 HOH 169 569 569 HOH HOH B . 
O 9 HOH 170 570 570 HOH HOH B . 
O 9 HOH 171 571 571 HOH HOH B . 
O 9 HOH 172 572 572 HOH HOH B . 
O 9 HOH 173 573 573 HOH HOH B . 
O 9 HOH 174 574 574 HOH HOH B . 
O 9 HOH 175 575 575 HOH HOH B . 
O 9 HOH 176 576 576 HOH HOH B . 
O 9 HOH 177 577 577 HOH HOH B . 
O 9 HOH 178 578 578 HOH HOH B . 
O 9 HOH 179 579 579 HOH HOH B . 
O 9 HOH 180 580 580 HOH HOH B . 
O 9 HOH 181 581 581 HOH HOH B . 
O 9 HOH 182 582 582 HOH HOH B . 
O 9 HOH 183 583 583 HOH HOH B . 
O 9 HOH 184 584 584 HOH HOH B . 
O 9 HOH 185 585 585 HOH HOH B . 
O 9 HOH 186 586 586 HOH HOH B . 
O 9 HOH 187 587 587 HOH HOH B . 
O 9 HOH 188 588 588 HOH HOH B . 
O 9 HOH 189 589 589 HOH HOH B . 
O 9 HOH 190 590 590 HOH HOH B . 
O 9 HOH 191 591 591 HOH HOH B . 
O 9 HOH 192 592 592 HOH HOH B . 
O 9 HOH 193 593 593 HOH HOH B . 
O 9 HOH 194 594 594 HOH HOH B . 
O 9 HOH 195 595 595 HOH HOH B . 
O 9 HOH 196 596 596 HOH HOH B . 
O 9 HOH 197 597 597 HOH HOH B . 
O 9 HOH 198 598 598 HOH HOH B . 
O 9 HOH 199 599 599 HOH HOH B . 
O 9 HOH 200 600 600 HOH HOH B . 
O 9 HOH 201 601 601 HOH HOH B . 
O 9 HOH 202 602 602 HOH HOH B . 
O 9 HOH 203 603 603 HOH HOH B . 
O 9 HOH 204 604 604 HOH HOH B . 
O 9 HOH 205 605 605 HOH HOH B . 
O 9 HOH 206 606 606 HOH HOH B . 
O 9 HOH 207 607 607 HOH HOH B . 
O 9 HOH 208 608 608 HOH HOH B . 
O 9 HOH 209 609 609 HOH HOH B . 
O 9 HOH 210 610 610 HOH HOH B . 
O 9 HOH 211 611 611 HOH HOH B . 
O 9 HOH 212 612 612 HOH HOH B . 
O 9 HOH 213 613 613 HOH HOH B . 
O 9 HOH 214 614 614 HOH HOH B . 
O 9 HOH 215 615 615 HOH HOH B . 
O 9 HOH 216 616 616 HOH HOH B . 
O 9 HOH 217 617 617 HOH HOH B . 
O 9 HOH 218 618 618 HOH HOH B . 
O 9 HOH 219 619 619 HOH HOH B . 
O 9 HOH 220 620 620 HOH HOH B . 
O 9 HOH 221 621 621 HOH HOH B . 
O 9 HOH 222 622 622 HOH HOH B . 
O 9 HOH 223 623 623 HOH HOH B . 
O 9 HOH 224 624 624 HOH HOH B . 
O 9 HOH 225 625 625 HOH HOH B . 
O 9 HOH 226 626 626 HOH HOH B . 
O 9 HOH 227 627 627 HOH HOH B . 
O 9 HOH 228 628 628 HOH HOH B . 
O 9 HOH 229 629 629 HOH HOH B . 
O 9 HOH 230 630 630 HOH HOH B . 
O 9 HOH 231 631 631 HOH HOH B . 
O 9 HOH 232 632 632 HOH HOH B . 
O 9 HOH 233 633 633 HOH HOH B . 
O 9 HOH 234 634 634 HOH HOH B . 
O 9 HOH 235 635 635 HOH HOH B . 
O 9 HOH 236 636 636 HOH HOH B . 
O 9 HOH 237 637 637 HOH HOH B . 
O 9 HOH 238 638 638 HOH HOH B . 
O 9 HOH 239 639 639 HOH HOH B . 
O 9 HOH 240 640 640 HOH HOH B . 
O 9 HOH 241 641 641 HOH HOH B . 
O 9 HOH 242 642 642 HOH HOH B . 
O 9 HOH 243 643 643 HOH HOH B . 
O 9 HOH 244 644 644 HOH HOH B . 
O 9 HOH 245 645 645 HOH HOH B . 
O 9 HOH 246 646 646 HOH HOH B . 
O 9 HOH 247 647 647 HOH HOH B . 
O 9 HOH 248 648 648 HOH HOH B . 
O 9 HOH 249 649 649 HOH HOH B . 
O 9 HOH 250 650 650 HOH HOH B . 
O 9 HOH 251 651 651 HOH HOH B . 
O 9 HOH 252 652 652 HOH HOH B . 
O 9 HOH 253 653 653 HOH HOH B . 
O 9 HOH 254 654 654 HOH HOH B . 
O 9 HOH 255 655 655 HOH HOH B . 
O 9 HOH 256 656 656 HOH HOH B . 
O 9 HOH 257 657 657 HOH HOH B . 
O 9 HOH 258 658 658 HOH HOH B . 
O 9 HOH 259 659 659 HOH HOH B . 
O 9 HOH 260 660 660 HOH HOH B . 
O 9 HOH 261 661 661 HOH HOH B . 
O 9 HOH 262 662 662 HOH HOH B . 
O 9 HOH 263 663 663 HOH HOH B . 
O 9 HOH 264 664 664 HOH HOH B . 
O 9 HOH 265 665 665 HOH HOH B . 
O 9 HOH 266 666 666 HOH HOH B . 
O 9 HOH 267 667 667 HOH HOH B . 
O 9 HOH 268 668 668 HOH HOH B . 
O 9 HOH 269 669 669 HOH HOH B . 
O 9 HOH 270 670 670 HOH HOH B . 
O 9 HOH 271 671 671 HOH HOH B . 
O 9 HOH 272 672 672 HOH HOH B . 
O 9 HOH 273 673 673 HOH HOH B . 
O 9 HOH 274 674 674 HOH HOH B . 
O 9 HOH 275 675 675 HOH HOH B . 
O 9 HOH 276 676 676 HOH HOH B . 
O 9 HOH 277 677 677 HOH HOH B . 
O 9 HOH 278 678 678 HOH HOH B . 
O 9 HOH 279 679 679 HOH HOH B . 
O 9 HOH 280 680 680 HOH HOH B . 
O 9 HOH 281 681 681 HOH HOH B . 
O 9 HOH 282 682 682 HOH HOH B . 
O 9 HOH 283 683 683 HOH HOH B . 
O 9 HOH 284 684 684 HOH HOH B . 
O 9 HOH 285 685 685 HOH HOH B . 
O 9 HOH 286 686 686 HOH HOH B . 
O 9 HOH 287 687 687 HOH HOH B . 
O 9 HOH 288 688 688 HOH HOH B . 
O 9 HOH 289 689 689 HOH HOH B . 
O 9 HOH 290 690 568 HOH HOH B . 
P 9 HOH 1   401 401 HOH HOH A . 
P 9 HOH 2   402 402 HOH HOH A . 
P 9 HOH 3   403 403 HOH HOH A . 
P 9 HOH 4   404 404 HOH HOH A . 
P 9 HOH 5   405 405 HOH HOH A . 
P 9 HOH 6   406 406 HOH HOH A . 
P 9 HOH 7   407 407 HOH HOH A . 
P 9 HOH 8   408 408 HOH HOH A . 
P 9 HOH 9   409 409 HOH HOH A . 
P 9 HOH 10  410 410 HOH HOH A . 
P 9 HOH 11  411 411 HOH HOH A . 
P 9 HOH 12  412 412 HOH HOH A . 
P 9 HOH 13  413 413 HOH HOH A . 
P 9 HOH 14  414 414 HOH HOH A . 
P 9 HOH 15  415 415 HOH HOH A . 
P 9 HOH 16  416 416 HOH HOH A . 
P 9 HOH 17  417 417 HOH HOH A . 
P 9 HOH 18  418 418 HOH HOH A . 
P 9 HOH 19  419 419 HOH HOH A . 
P 9 HOH 20  420 420 HOH HOH A . 
P 9 HOH 21  421 421 HOH HOH A . 
P 9 HOH 22  422 422 HOH HOH A . 
P 9 HOH 23  423 423 HOH HOH A . 
P 9 HOH 24  424 424 HOH HOH A . 
P 9 HOH 25  425 425 HOH HOH A . 
P 9 HOH 26  426 426 HOH HOH A . 
P 9 HOH 27  427 427 HOH HOH A . 
P 9 HOH 28  428 428 HOH HOH A . 
P 9 HOH 29  429 429 HOH HOH A . 
P 9 HOH 30  430 430 HOH HOH A . 
P 9 HOH 31  431 431 HOH HOH A . 
P 9 HOH 32  432 432 HOH HOH A . 
P 9 HOH 33  433 433 HOH HOH A . 
P 9 HOH 34  434 434 HOH HOH A . 
P 9 HOH 35  435 435 HOH HOH A . 
P 9 HOH 36  436 436 HOH HOH A . 
P 9 HOH 37  437 437 HOH HOH A . 
P 9 HOH 38  438 438 HOH HOH A . 
P 9 HOH 39  439 439 HOH HOH A . 
P 9 HOH 40  440 440 HOH HOH A . 
P 9 HOH 41  441 441 HOH HOH A . 
P 9 HOH 42  442 442 HOH HOH A . 
P 9 HOH 43  443 443 HOH HOH A . 
P 9 HOH 44  444 444 HOH HOH A . 
P 9 HOH 45  445 445 HOH HOH A . 
P 9 HOH 46  446 446 HOH HOH A . 
P 9 HOH 47  447 447 HOH HOH A . 
P 9 HOH 48  448 448 HOH HOH A . 
P 9 HOH 49  449 449 HOH HOH A . 
P 9 HOH 50  450 450 HOH HOH A . 
P 9 HOH 51  451 451 HOH HOH A . 
P 9 HOH 52  452 452 HOH HOH A . 
P 9 HOH 53  453 453 HOH HOH A . 
P 9 HOH 54  454 454 HOH HOH A . 
P 9 HOH 55  455 455 HOH HOH A . 
P 9 HOH 56  456 456 HOH HOH A . 
P 9 HOH 57  457 457 HOH HOH A . 
P 9 HOH 58  458 458 HOH HOH A . 
P 9 HOH 59  459 459 HOH HOH A . 
P 9 HOH 60  460 460 HOH HOH A . 
P 9 HOH 61  461 461 HOH HOH A . 
P 9 HOH 62  462 462 HOH HOH A . 
P 9 HOH 63  463 463 HOH HOH A . 
P 9 HOH 64  464 464 HOH HOH A . 
P 9 HOH 65  465 465 HOH HOH A . 
P 9 HOH 66  466 466 HOH HOH A . 
P 9 HOH 67  467 467 HOH HOH A . 
P 9 HOH 68  468 468 HOH HOH A . 
P 9 HOH 69  469 469 HOH HOH A . 
P 9 HOH 70  470 470 HOH HOH A . 
P 9 HOH 71  471 471 HOH HOH A . 
P 9 HOH 72  472 472 HOH HOH A . 
P 9 HOH 73  473 473 HOH HOH A . 
P 9 HOH 74  474 474 HOH HOH A . 
P 9 HOH 75  475 475 HOH HOH A . 
P 9 HOH 76  476 476 HOH HOH A . 
P 9 HOH 77  477 477 HOH HOH A . 
P 9 HOH 78  478 478 HOH HOH A . 
P 9 HOH 79  479 479 HOH HOH A . 
P 9 HOH 80  480 480 HOH HOH A . 
P 9 HOH 81  481 481 HOH HOH A . 
P 9 HOH 82  482 482 HOH HOH A . 
P 9 HOH 83  483 483 HOH HOH A . 
P 9 HOH 84  484 484 HOH HOH A . 
P 9 HOH 85  485 485 HOH HOH A . 
P 9 HOH 86  486 486 HOH HOH A . 
P 9 HOH 87  487 487 HOH HOH A . 
P 9 HOH 88  488 488 HOH HOH A . 
P 9 HOH 89  489 489 HOH HOH A . 
P 9 HOH 90  490 490 HOH HOH A . 
P 9 HOH 91  491 491 HOH HOH A . 
P 9 HOH 92  492 492 HOH HOH A . 
P 9 HOH 93  493 493 HOH HOH A . 
P 9 HOH 94  494 494 HOH HOH A . 
P 9 HOH 95  495 495 HOH HOH A . 
P 9 HOH 96  496 496 HOH HOH A . 
P 9 HOH 97  497 497 HOH HOH A . 
P 9 HOH 98  498 498 HOH HOH A . 
P 9 HOH 99  499 499 HOH HOH A . 
P 9 HOH 100 500 500 HOH HOH A . 
P 9 HOH 101 501 501 HOH HOH A . 
P 9 HOH 102 502 502 HOH HOH A . 
P 9 HOH 103 503 503 HOH HOH A . 
P 9 HOH 104 504 504 HOH HOH A . 
P 9 HOH 105 505 505 HOH HOH A . 
P 9 HOH 106 506 506 HOH HOH A . 
P 9 HOH 107 507 507 HOH HOH A . 
P 9 HOH 108 508 508 HOH HOH A . 
P 9 HOH 109 509 509 HOH HOH A . 
P 9 HOH 110 510 510 HOH HOH A . 
P 9 HOH 111 511 511 HOH HOH A . 
P 9 HOH 112 512 512 HOH HOH A . 
P 9 HOH 113 513 513 HOH HOH A . 
P 9 HOH 114 514 514 HOH HOH A . 
P 9 HOH 115 515 515 HOH HOH A . 
P 9 HOH 116 516 516 HOH HOH A . 
P 9 HOH 117 517 517 HOH HOH A . 
P 9 HOH 118 518 518 HOH HOH A . 
P 9 HOH 119 519 519 HOH HOH A . 
P 9 HOH 120 520 520 HOH HOH A . 
P 9 HOH 121 521 521 HOH HOH A . 
P 9 HOH 122 522 522 HOH HOH A . 
P 9 HOH 123 523 523 HOH HOH A . 
P 9 HOH 124 524 524 HOH HOH A . 
P 9 HOH 125 525 525 HOH HOH A . 
P 9 HOH 126 526 526 HOH HOH A . 
P 9 HOH 127 527 527 HOH HOH A . 
P 9 HOH 128 528 528 HOH HOH A . 
P 9 HOH 129 529 529 HOH HOH A . 
P 9 HOH 130 530 530 HOH HOH A . 
P 9 HOH 131 531 531 HOH HOH A . 
P 9 HOH 132 532 532 HOH HOH A . 
P 9 HOH 133 533 533 HOH HOH A . 
P 9 HOH 134 534 534 HOH HOH A . 
P 9 HOH 135 535 535 HOH HOH A . 
P 9 HOH 136 536 536 HOH HOH A . 
P 9 HOH 137 537 537 HOH HOH A . 
P 9 HOH 138 538 538 HOH HOH A . 
P 9 HOH 139 539 539 HOH HOH A . 
P 9 HOH 140 540 540 HOH HOH A . 
P 9 HOH 141 541 541 HOH HOH A . 
P 9 HOH 142 542 542 HOH HOH A . 
P 9 HOH 143 543 543 HOH HOH A . 
P 9 HOH 144 544 544 HOH HOH A . 
P 9 HOH 145 545 545 HOH HOH A . 
P 9 HOH 146 546 546 HOH HOH A . 
P 9 HOH 147 547 547 HOH HOH A . 
P 9 HOH 148 548 548 HOH HOH A . 
P 9 HOH 149 549 549 HOH HOH A . 
P 9 HOH 150 550 550 HOH HOH A . 
P 9 HOH 151 551 551 HOH HOH A . 
P 9 HOH 152 552 552 HOH HOH A . 
P 9 HOH 153 553 553 HOH HOH A . 
P 9 HOH 154 554 554 HOH HOH A . 
P 9 HOH 155 555 555 HOH HOH A . 
P 9 HOH 156 556 556 HOH HOH A . 
P 9 HOH 157 557 557 HOH HOH A . 
P 9 HOH 158 558 558 HOH HOH A . 
P 9 HOH 159 559 559 HOH HOH A . 
P 9 HOH 160 560 560 HOH HOH A . 
P 9 HOH 161 561 561 HOH HOH A . 
P 9 HOH 162 562 562 HOH HOH A . 
P 9 HOH 163 563 563 HOH HOH A . 
P 9 HOH 164 564 564 HOH HOH A . 
P 9 HOH 165 565 565 HOH HOH A . 
P 9 HOH 166 566 566 HOH HOH A . 
P 9 HOH 167 567 567 HOH HOH A . 
P 9 HOH 168 568 569 HOH HOH A . 
P 9 HOH 169 569 570 HOH HOH A . 
P 9 HOH 170 570 571 HOH HOH A . 
P 9 HOH 171 571 572 HOH HOH A . 
P 9 HOH 172 572 573 HOH HOH A . 
P 9 HOH 173 573 574 HOH HOH A . 
P 9 HOH 174 574 575 HOH HOH A . 
P 9 HOH 175 575 576 HOH HOH A . 
P 9 HOH 176 576 577 HOH HOH A . 
P 9 HOH 177 577 578 HOH HOH A . 
P 9 HOH 178 578 579 HOH HOH A . 
P 9 HOH 179 579 580 HOH HOH A . 
P 9 HOH 180 580 581 HOH HOH A . 
P 9 HOH 181 581 582 HOH HOH A . 
P 9 HOH 182 582 583 HOH HOH A . 
P 9 HOH 183 583 584 HOH HOH A . 
P 9 HOH 184 584 585 HOH HOH A . 
P 9 HOH 185 585 586 HOH HOH A . 
P 9 HOH 186 586 587 HOH HOH A . 
P 9 HOH 187 587 588 HOH HOH A . 
P 9 HOH 188 588 589 HOH HOH A . 
P 9 HOH 189 589 590 HOH HOH A . 
P 9 HOH 190 590 591 HOH HOH A . 
P 9 HOH 191 591 592 HOH HOH A . 
P 9 HOH 192 592 593 HOH HOH A . 
P 9 HOH 193 593 594 HOH HOH A . 
P 9 HOH 194 594 595 HOH HOH A . 
P 9 HOH 195 595 596 HOH HOH A . 
P 9 HOH 196 596 597 HOH HOH A . 
P 9 HOH 197 597 598 HOH HOH A . 
P 9 HOH 198 598 599 HOH HOH A . 
P 9 HOH 199 599 600 HOH HOH A . 
P 9 HOH 200 600 601 HOH HOH A . 
P 9 HOH 201 601 602 HOH HOH A . 
P 9 HOH 202 602 603 HOH HOH A . 
P 9 HOH 203 603 604 HOH HOH A . 
P 9 HOH 204 604 605 HOH HOH A . 
P 9 HOH 205 605 606 HOH HOH A . 
P 9 HOH 206 606 607 HOH HOH A . 
P 9 HOH 207 607 608 HOH HOH A . 
P 9 HOH 208 608 609 HOH HOH A . 
P 9 HOH 209 609 610 HOH HOH A . 
P 9 HOH 210 610 611 HOH HOH A . 
P 9 HOH 211 611 612 HOH HOH A . 
P 9 HOH 212 612 613 HOH HOH A . 
P 9 HOH 213 613 614 HOH HOH A . 
P 9 HOH 214 614 615 HOH HOH A . 
P 9 HOH 215 615 616 HOH HOH A . 
P 9 HOH 216 616 617 HOH HOH A . 
P 9 HOH 217 617 618 HOH HOH A . 
P 9 HOH 218 618 619 HOH HOH A . 
P 9 HOH 219 619 620 HOH HOH A . 
P 9 HOH 220 620 621 HOH HOH A . 
P 9 HOH 221 621 622 HOH HOH A . 
P 9 HOH 222 622 623 HOH HOH A . 
P 9 HOH 223 623 624 HOH HOH A . 
P 9 HOH 224 624 625 HOH HOH A . 
P 9 HOH 225 625 626 HOH HOH A . 
P 9 HOH 226 626 627 HOH HOH A . 
P 9 HOH 227 627 628 HOH HOH A . 
P 9 HOH 228 628 629 HOH HOH A . 
P 9 HOH 229 629 630 HOH HOH A . 
P 9 HOH 230 630 631 HOH HOH A . 
P 9 HOH 231 631 632 HOH HOH A . 
P 9 HOH 232 632 633 HOH HOH A . 
P 9 HOH 233 633 634 HOH HOH A . 
P 9 HOH 234 634 635 HOH HOH A . 
P 9 HOH 235 635 636 HOH HOH A . 
P 9 HOH 236 636 637 HOH HOH A . 
P 9 HOH 237 637 638 HOH HOH A . 
P 9 HOH 238 638 639 HOH HOH A . 
P 9 HOH 239 639 640 HOH HOH A . 
P 9 HOH 240 640 641 HOH HOH A . 
P 9 HOH 241 641 642 HOH HOH A . 
P 9 HOH 242 642 643 HOH HOH A . 
P 9 HOH 243 643 644 HOH HOH A . 
P 9 HOH 244 644 645 HOH HOH A . 
P 9 HOH 245 645 646 HOH HOH A . 
P 9 HOH 246 646 647 HOH HOH A . 
P 9 HOH 247 647 648 HOH HOH A . 
P 9 HOH 248 648 649 HOH HOH A . 
P 9 HOH 249 649 650 HOH HOH A . 
P 9 HOH 250 650 651 HOH HOH A . 
P 9 HOH 251 651 652 HOH HOH A . 
P 9 HOH 252 652 653 HOH HOH A . 
P 9 HOH 253 653 654 HOH HOH A . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,K,O 
2 1 B,L,M,N,P             
# 
_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 96  ? B HIS 94  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 NE2 ? A HIS 98  ? B HIS 96  ? 1_555 101.0 ? 
2  NE2 ? A HIS 96  ? B HIS 94  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 ND1 ? A HIS 121 ? B HIS 119 ? 1_555 114.9 ? 
3  NE2 ? A HIS 98  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 ND1 ? A HIS 121 ? B HIS 119 ? 1_555 97.7  ? 
4  NE2 ? A HIS 96  ? B HIS 94  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N11 B D EWW .   ? B EWW 302 ? 1_555 114.7 ? 
5  NE2 ? A HIS 98  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N11 B D EWW .   ? B EWW 302 ? 1_555 111.7 ? 
6  ND1 ? A HIS 121 ? B HIS 119 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N11 B D EWW .   ? B EWW 302 ? 1_555 114.6 ? 
7  NE2 ? A HIS 96  ? B HIS 94  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N11 A D EWW .   ? B EWW 302 ? 1_555 107.5 ? 
8  NE2 ? A HIS 98  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N11 A D EWW .   ? B EWW 302 ? 1_555 108.1 ? 
9  ND1 ? A HIS 121 ? B HIS 119 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N11 A D EWW .   ? B EWW 302 ? 1_555 124.3 ? 
10 N11 B D EWW .   ? B EWW 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N11 A D EWW .   ? B EWW 302 ? 1_555 9.7   ? 
11 NE2 ? A HIS 96  ? B HIS 94  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O8  A D EWW .   ? B EWW 302 ? 1_555 85.0  ? 
12 NE2 ? A HIS 98  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O8  A D EWW .   ? B EWW 302 ? 1_555 172.9 ? 
13 ND1 ? A HIS 121 ? B HIS 119 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O8  A D EWW .   ? B EWW 302 ? 1_555 83.0  ? 
14 N11 B D EWW .   ? B EWW 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O8  A D EWW .   ? B EWW 302 ? 1_555 62.0  ? 
15 N11 A D EWW .   ? B EWW 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O8  A D EWW .   ? B EWW 302 ? 1_555 66.1  ? 
16 NE2 ? A HIS 96  ? B HIS 94  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S6  A D EWW .   ? B EWW 302 ? 1_555 99.8  ? 
17 NE2 ? A HIS 98  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S6  A D EWW .   ? B EWW 302 ? 1_555 143.4 ? 
18 ND1 ? A HIS 121 ? B HIS 119 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S6  A D EWW .   ? B EWW 302 ? 1_555 100.4 ? 
19 N11 B D EWW .   ? B EWW 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S6  A D EWW .   ? B EWW 302 ? 1_555 31.7  ? 
20 N11 A D EWW .   ? B EWW 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S6  A D EWW .   ? B EWW 302 ? 1_555 36.2  ? 
21 O8  A D EWW .   ? B EWW 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S6  A D EWW .   ? B EWW 302 ? 1_555 30.3  ? 
22 NE2 ? B HIS 96  ? A HIS 94  ? 1_555 ZN ? L ZN . ? A ZN 301 ? 1_555 NE2 ? B HIS 98  ? A HIS 96  ? 1_555 104.9 ? 
23 NE2 ? B HIS 96  ? A HIS 94  ? 1_555 ZN ? L ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS 121 ? A HIS 119 ? 1_555 113.7 ? 
24 NE2 ? B HIS 98  ? A HIS 96  ? 1_555 ZN ? L ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS 121 ? A HIS 119 ? 1_555 95.2  ? 
25 NE2 ? B HIS 96  ? A HIS 94  ? 1_555 ZN ? L ZN . ? A ZN 301 ? 1_555 N11 ? M EWW .   ? A EWW 302 ? 1_555 112.9 ? 
26 NE2 ? B HIS 98  ? A HIS 96  ? 1_555 ZN ? L ZN . ? A ZN 301 ? 1_555 N11 ? M EWW .   ? A EWW 302 ? 1_555 108.4 ? 
27 ND1 ? B HIS 121 ? A HIS 119 ? 1_555 ZN ? L ZN . ? A ZN 301 ? 1_555 N11 ? M EWW .   ? A EWW 302 ? 1_555 119.0 ? 
# 
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 2015-01-21 
2 'Structure model' 1 1 2023-11-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' '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' diffrn_source                 
5 2 'Structure model' pdbx_initial_refinement_model 
6 2 'Structure model' pdbx_struct_conn_angle        
7 2 'Structure model' struct_conn                   
8 2 'Structure model' struct_ref_seq_dif            
9 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' '_diffrn_source.pdbx_synchrotron_site'        
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_alt_id'  
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_alt_id'  
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
15 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
16 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
17 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
18 2 'Structure model' '_pdbx_struct_conn_angle.value'               
19 2 'Structure model' '_struct_conn.pdbx_dist_value'                
20 2 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
21 2 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
22 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
23 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
24 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
25 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
26 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
27 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
28 2 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
29 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
30 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
31 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
32 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
33 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
34 2 'Structure model' '_struct_ref_seq_dif.details'                 
35 2 'Structure model' '_struct_site.pdbx_auth_asym_id'              
36 2 'Structure model' '_struct_site.pdbx_auth_comp_id'              
37 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       3.2.19 22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345dtb   .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER B 65  ? ? -173.92 -177.43 
2 1 ASN B 75  ? ? -95.45  42.86   
3 1 HIS B 103 ? ? -152.15 75.57   
4 1 ASN B 244 ? ? -153.72 42.81   
5 1 LEU A 3   ? ? -99.05  44.69   
6 1 SER A 4   ? ? -165.37 24.37   
7 1 SER A 65  ? ? -171.21 -175.18 
8 1 PHE A 176 ? ? -158.38 89.54   
9 1 ASN A 244 ? ? -151.63 44.56   
# 
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 B MET -1 ? A MET 1 
2 1 Y 1 B MET 0  ? A MET 2 
3 1 Y 1 B SER 1  ? A SER 3 
4 1 Y 1 B ARG 2  ? A ARG 4 
5 1 Y 1 B LEU 3  ? A LEU 5 
6 1 Y 1 A MET -1 ? B MET 1 
7 1 Y 1 A MET 0  ? B MET 2 
8 1 Y 1 A SER 1  ? B SER 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  
CIT C1   C  N N 74  
CIT O1   O  N N 75  
CIT O2   O  N N 76  
CIT C2   C  N N 77  
CIT C3   C  N N 78  
CIT O7   O  N N 79  
CIT C4   C  N N 80  
CIT C5   C  N N 81  
CIT O3   O  N N 82  
CIT O4   O  N N 83  
CIT C6   C  N N 84  
CIT O5   O  N N 85  
CIT O6   O  N N 86  
CIT HO2  H  N N 87  
CIT H21  H  N N 88  
CIT H22  H  N N 89  
CIT HO7  H  N N 90  
CIT H41  H  N N 91  
CIT H42  H  N N 92  
CIT HO4  H  N N 93  
CIT HO6  H  N N 94  
CYS N    N  N N 95  
CYS CA   C  N R 96  
CYS C    C  N N 97  
CYS O    O  N N 98  
CYS CB   C  N N 99  
CYS SG   S  N N 100 
CYS OXT  O  N N 101 
CYS H    H  N N 102 
CYS H2   H  N N 103 
CYS HA   H  N N 104 
CYS HB2  H  N N 105 
CYS HB3  H  N N 106 
CYS HG   H  N N 107 
CYS HXT  H  N N 108 
DMS S    S  N N 109 
DMS O    O  N N 110 
DMS C1   C  N N 111 
DMS C2   C  N N 112 
DMS H11  H  N N 113 
DMS H12  H  N N 114 
DMS H13  H  N N 115 
DMS H21  H  N N 116 
DMS H22  H  N N 117 
DMS H23  H  N N 118 
EDO C1   C  N N 119 
EDO O1   O  N N 120 
EDO C2   C  N N 121 
EDO O2   O  N N 122 
EDO H11  H  N N 123 
EDO H12  H  N N 124 
EDO HO1  H  N N 125 
EDO H21  H  N N 126 
EDO H22  H  N N 127 
EDO HO2  H  N N 128 
EWW CL   CL N N 129 
EWW C3   C  Y N 130 
EWW C4   C  Y N 131 
EWW S6   S  N N 132 
EWW O8   O  N N 133 
EWW N11  N  N N 134 
EWW O7   O  N N 135 
EWW C5   C  Y N 136 
EWW C2   C  Y N 137 
EWW C22  C  Y N 138 
EWW C1   C  Y N 139 
EWW C9   C  N N 140 
EWW O12  O  N N 141 
EWW C10  C  N N 142 
EWW S13  S  N N 143 
EWW C14  C  N N 144 
EWW N17  N  N N 145 
EWW C18  C  N N 146 
EWW O21  O  N N 147 
EWW C19  C  N N 148 
EWW C16  C  N N 149 
EWW N15  N  N N 150 
EWW C20  C  N N 151 
EWW H1   H  N N 152 
EWW H2   H  N N 153 
EWW H3   H  N N 154 
EWW H4   H  N N 155 
EWW H5   H  N N 156 
EWW H6   H  N N 157 
EWW H7   H  N N 158 
EWW H8   H  N N 159 
EWW H10  H  N N 160 
EWW H11  H  N N 161 
EWW H12  H  N N 162 
EWW H13  H  N N 163 
GLN N    N  N N 164 
GLN CA   C  N S 165 
GLN C    C  N N 166 
GLN O    O  N N 167 
GLN CB   C  N N 168 
GLN CG   C  N N 169 
GLN CD   C  N N 170 
GLN OE1  O  N N 171 
GLN NE2  N  N N 172 
GLN OXT  O  N N 173 
GLN H    H  N N 174 
GLN H2   H  N N 175 
GLN HA   H  N N 176 
GLN HB2  H  N N 177 
GLN HB3  H  N N 178 
GLN HG2  H  N N 179 
GLN HG3  H  N N 180 
GLN HE21 H  N N 181 
GLN HE22 H  N N 182 
GLN HXT  H  N N 183 
GLU N    N  N N 184 
GLU CA   C  N S 185 
GLU C    C  N N 186 
GLU O    O  N N 187 
GLU CB   C  N N 188 
GLU CG   C  N N 189 
GLU CD   C  N N 190 
GLU OE1  O  N N 191 
GLU OE2  O  N N 192 
GLU OXT  O  N N 193 
GLU H    H  N N 194 
GLU H2   H  N N 195 
GLU HA   H  N N 196 
GLU HB2  H  N N 197 
GLU HB3  H  N N 198 
GLU HG2  H  N N 199 
GLU HG3  H  N N 200 
GLU HE2  H  N N 201 
GLU HXT  H  N N 202 
GLY N    N  N N 203 
GLY CA   C  N N 204 
GLY C    C  N N 205 
GLY O    O  N N 206 
GLY OXT  O  N N 207 
GLY H    H  N N 208 
GLY H2   H  N N 209 
GLY HA2  H  N N 210 
GLY HA3  H  N N 211 
GLY HXT  H  N N 212 
HIS N    N  N N 213 
HIS CA   C  N S 214 
HIS C    C  N N 215 
HIS O    O  N N 216 
HIS CB   C  N N 217 
HIS CG   C  Y N 218 
HIS ND1  N  Y N 219 
HIS CD2  C  Y N 220 
HIS CE1  C  Y N 221 
HIS NE2  N  Y N 222 
HIS OXT  O  N N 223 
HIS H    H  N N 224 
HIS H2   H  N N 225 
HIS HA   H  N N 226 
HIS HB2  H  N N 227 
HIS HB3  H  N N 228 
HIS HD1  H  N N 229 
HIS HD2  H  N N 230 
HIS HE1  H  N N 231 
HIS HE2  H  N N 232 
HIS HXT  H  N N 233 
HOH O    O  N N 234 
HOH H1   H  N N 235 
HOH H2   H  N N 236 
ILE N    N  N N 237 
ILE CA   C  N S 238 
ILE C    C  N N 239 
ILE O    O  N N 240 
ILE CB   C  N S 241 
ILE CG1  C  N N 242 
ILE CG2  C  N N 243 
ILE CD1  C  N N 244 
ILE OXT  O  N N 245 
ILE H    H  N N 246 
ILE H2   H  N N 247 
ILE HA   H  N N 248 
ILE HB   H  N N 249 
ILE HG12 H  N N 250 
ILE HG13 H  N N 251 
ILE HG21 H  N N 252 
ILE HG22 H  N N 253 
ILE HG23 H  N N 254 
ILE HD11 H  N N 255 
ILE HD12 H  N N 256 
ILE HD13 H  N N 257 
ILE HXT  H  N N 258 
LEU N    N  N N 259 
LEU CA   C  N S 260 
LEU C    C  N N 261 
LEU O    O  N N 262 
LEU CB   C  N N 263 
LEU CG   C  N N 264 
LEU CD1  C  N N 265 
LEU CD2  C  N N 266 
LEU OXT  O  N N 267 
LEU H    H  N N 268 
LEU H2   H  N N 269 
LEU HA   H  N N 270 
LEU HB2  H  N N 271 
LEU HB3  H  N N 272 
LEU HG   H  N N 273 
LEU HD11 H  N N 274 
LEU HD12 H  N N 275 
LEU HD13 H  N N 276 
LEU HD21 H  N N 277 
LEU HD22 H  N N 278 
LEU HD23 H  N N 279 
LEU HXT  H  N N 280 
LYS N    N  N N 281 
LYS CA   C  N S 282 
LYS C    C  N N 283 
LYS O    O  N N 284 
LYS CB   C  N N 285 
LYS CG   C  N N 286 
LYS CD   C  N N 287 
LYS CE   C  N N 288 
LYS NZ   N  N N 289 
LYS OXT  O  N N 290 
LYS H    H  N N 291 
LYS H2   H  N N 292 
LYS HA   H  N N 293 
LYS HB2  H  N N 294 
LYS HB3  H  N N 295 
LYS HG2  H  N N 296 
LYS HG3  H  N N 297 
LYS HD2  H  N N 298 
LYS HD3  H  N N 299 
LYS HE2  H  N N 300 
LYS HE3  H  N N 301 
LYS HZ1  H  N N 302 
LYS HZ2  H  N N 303 
LYS HZ3  H  N N 304 
LYS HXT  H  N N 305 
MET N    N  N N 306 
MET CA   C  N S 307 
MET C    C  N N 308 
MET O    O  N N 309 
MET CB   C  N N 310 
MET CG   C  N N 311 
MET SD   S  N N 312 
MET CE   C  N N 313 
MET OXT  O  N N 314 
MET H    H  N N 315 
MET H2   H  N N 316 
MET HA   H  N N 317 
MET HB2  H  N N 318 
MET HB3  H  N N 319 
MET HG2  H  N N 320 
MET HG3  H  N N 321 
MET HE1  H  N N 322 
MET HE2  H  N N 323 
MET HE3  H  N N 324 
MET HXT  H  N N 325 
NI  NI   NI N N 326 
PEG C1   C  N N 327 
PEG O1   O  N N 328 
PEG C2   C  N N 329 
PEG O2   O  N N 330 
PEG C3   C  N N 331 
PEG C4   C  N N 332 
PEG O4   O  N N 333 
PEG H11  H  N N 334 
PEG H12  H  N N 335 
PEG HO1  H  N N 336 
PEG H21  H  N N 337 
PEG H22  H  N N 338 
PEG H31  H  N N 339 
PEG H32  H  N N 340 
PEG H41  H  N N 341 
PEG H42  H  N N 342 
PEG HO4  H  N N 343 
PHE N    N  N N 344 
PHE CA   C  N S 345 
PHE C    C  N N 346 
PHE O    O  N N 347 
PHE CB   C  N N 348 
PHE CG   C  Y N 349 
PHE CD1  C  Y N 350 
PHE CD2  C  Y N 351 
PHE CE1  C  Y N 352 
PHE CE2  C  Y N 353 
PHE CZ   C  Y N 354 
PHE OXT  O  N N 355 
PHE H    H  N N 356 
PHE H2   H  N N 357 
PHE HA   H  N N 358 
PHE HB2  H  N N 359 
PHE HB3  H  N N 360 
PHE HD1  H  N N 361 
PHE HD2  H  N N 362 
PHE HE1  H  N N 363 
PHE HE2  H  N N 364 
PHE HZ   H  N N 365 
PHE HXT  H  N N 366 
PRO N    N  N N 367 
PRO CA   C  N S 368 
PRO C    C  N N 369 
PRO O    O  N N 370 
PRO CB   C  N N 371 
PRO CG   C  N N 372 
PRO CD   C  N N 373 
PRO OXT  O  N N 374 
PRO H    H  N N 375 
PRO HA   H  N N 376 
PRO HB2  H  N N 377 
PRO HB3  H  N N 378 
PRO HG2  H  N N 379 
PRO HG3  H  N N 380 
PRO HD2  H  N N 381 
PRO HD3  H  N N 382 
PRO HXT  H  N N 383 
SER N    N  N N 384 
SER CA   C  N S 385 
SER C    C  N N 386 
SER O    O  N N 387 
SER CB   C  N N 388 
SER OG   O  N N 389 
SER OXT  O  N N 390 
SER H    H  N N 391 
SER H2   H  N N 392 
SER HA   H  N N 393 
SER HB2  H  N N 394 
SER HB3  H  N N 395 
SER HG   H  N N 396 
SER HXT  H  N N 397 
THR N    N  N N 398 
THR CA   C  N S 399 
THR C    C  N N 400 
THR O    O  N N 401 
THR CB   C  N R 402 
THR OG1  O  N N 403 
THR CG2  C  N N 404 
THR OXT  O  N N 405 
THR H    H  N N 406 
THR H2   H  N N 407 
THR HA   H  N N 408 
THR HB   H  N N 409 
THR HG1  H  N N 410 
THR HG21 H  N N 411 
THR HG22 H  N N 412 
THR HG23 H  N N 413 
THR HXT  H  N N 414 
TRP N    N  N N 415 
TRP CA   C  N S 416 
TRP C    C  N N 417 
TRP O    O  N N 418 
TRP CB   C  N N 419 
TRP CG   C  Y N 420 
TRP CD1  C  Y N 421 
TRP CD2  C  Y N 422 
TRP NE1  N  Y N 423 
TRP CE2  C  Y N 424 
TRP CE3  C  Y N 425 
TRP CZ2  C  Y N 426 
TRP CZ3  C  Y N 427 
TRP CH2  C  Y N 428 
TRP OXT  O  N N 429 
TRP H    H  N N 430 
TRP H2   H  N N 431 
TRP HA   H  N N 432 
TRP HB2  H  N N 433 
TRP HB3  H  N N 434 
TRP HD1  H  N N 435 
TRP HE1  H  N N 436 
TRP HE3  H  N N 437 
TRP HZ2  H  N N 438 
TRP HZ3  H  N N 439 
TRP HH2  H  N N 440 
TRP HXT  H  N N 441 
TYR N    N  N N 442 
TYR CA   C  N S 443 
TYR C    C  N N 444 
TYR O    O  N N 445 
TYR CB   C  N N 446 
TYR CG   C  Y N 447 
TYR CD1  C  Y N 448 
TYR CD2  C  Y N 449 
TYR CE1  C  Y N 450 
TYR CE2  C  Y N 451 
TYR CZ   C  Y N 452 
TYR OH   O  N N 453 
TYR OXT  O  N N 454 
TYR H    H  N N 455 
TYR H2   H  N N 456 
TYR HA   H  N N 457 
TYR HB2  H  N N 458 
TYR HB3  H  N N 459 
TYR HD1  H  N N 460 
TYR HD2  H  N N 461 
TYR HE1  H  N N 462 
TYR HE2  H  N N 463 
TYR HH   H  N N 464 
TYR HXT  H  N N 465 
VAL N    N  N N 466 
VAL CA   C  N S 467 
VAL C    C  N N 468 
VAL O    O  N N 469 
VAL CB   C  N N 470 
VAL CG1  C  N N 471 
VAL CG2  C  N N 472 
VAL OXT  O  N N 473 
VAL H    H  N N 474 
VAL H2   H  N N 475 
VAL HA   H  N N 476 
VAL HB   H  N N 477 
VAL HG11 H  N N 478 
VAL HG12 H  N N 479 
VAL HG13 H  N N 480 
VAL HG21 H  N N 481 
VAL HG22 H  N N 482 
VAL HG23 H  N N 483 
VAL HXT  H  N N 484 
ZN  ZN   ZN N N 485 
# 
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  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
DMS S   O    doub N N 103 
DMS S   C1   sing N N 104 
DMS S   C2   sing N N 105 
DMS C1  H11  sing N N 106 
DMS C1  H12  sing N N 107 
DMS C1  H13  sing N N 108 
DMS C2  H21  sing N N 109 
DMS C2  H22  sing N N 110 
DMS C2  H23  sing N N 111 
EDO C1  O1   sing N N 112 
EDO C1  C2   sing N N 113 
EDO C1  H11  sing N N 114 
EDO C1  H12  sing N N 115 
EDO O1  HO1  sing N N 116 
EDO C2  O2   sing N N 117 
EDO C2  H21  sing N N 118 
EDO C2  H22  sing N N 119 
EDO O2  HO2  sing N N 120 
EWW S13 C14  sing N N 121 
EWW S13 C10  sing N N 122 
EWW N17 C14  sing N N 123 
EWW N17 C18  sing N N 124 
EWW O21 C18  doub N N 125 
EWW C14 N15  doub N N 126 
EWW C10 C9   sing N N 127 
EWW C18 C19  sing N N 128 
EWW O12 C9   doub N N 129 
EWW C9  C22  sing N N 130 
EWW C1  C22  doub Y N 131 
EWW C1  C5   sing Y N 132 
EWW N15 C16  sing N N 133 
EWW C22 C2   sing Y N 134 
EWW C19 C16  doub N N 135 
EWW C5  C4   doub Y N 136 
EWW C16 C20  sing N N 137 
EWW C2  C3   doub Y N 138 
EWW C4  C3   sing Y N 139 
EWW C4  S6   sing N N 140 
EWW C3  CL   sing N N 141 
EWW N11 S6   sing N N 142 
EWW O8  S6   doub N N 143 
EWW S6  O7   doub N N 144 
EWW N11 H1   sing N N 145 
EWW N11 H2   sing N N 146 
EWW C5  H3   sing N N 147 
EWW C2  H4   sing N N 148 
EWW C1  H5   sing N N 149 
EWW C10 H6   sing N N 150 
EWW C10 H7   sing N N 151 
EWW C19 H8   sing N N 152 
EWW C20 H10  sing N N 153 
EWW C20 H11  sing N N 154 
EWW C20 H12  sing N N 155 
EWW N17 H13  sing N N 156 
GLN N   CA   sing N N 157 
GLN N   H    sing N N 158 
GLN N   H2   sing N N 159 
GLN CA  C    sing N N 160 
GLN CA  CB   sing N N 161 
GLN CA  HA   sing N N 162 
GLN C   O    doub N N 163 
GLN C   OXT  sing N N 164 
GLN CB  CG   sing N N 165 
GLN CB  HB2  sing N N 166 
GLN CB  HB3  sing N N 167 
GLN CG  CD   sing N N 168 
GLN CG  HG2  sing N N 169 
GLN CG  HG3  sing N N 170 
GLN CD  OE1  doub N N 171 
GLN CD  NE2  sing N N 172 
GLN NE2 HE21 sing N N 173 
GLN NE2 HE22 sing N N 174 
GLN OXT HXT  sing N N 175 
GLU N   CA   sing N N 176 
GLU N   H    sing N N 177 
GLU N   H2   sing N N 178 
GLU CA  C    sing N N 179 
GLU CA  CB   sing N N 180 
GLU CA  HA   sing N N 181 
GLU C   O    doub N N 182 
GLU C   OXT  sing N N 183 
GLU CB  CG   sing N N 184 
GLU CB  HB2  sing N N 185 
GLU CB  HB3  sing N N 186 
GLU CG  CD   sing N N 187 
GLU CG  HG2  sing N N 188 
GLU CG  HG3  sing N N 189 
GLU CD  OE1  doub N N 190 
GLU CD  OE2  sing N N 191 
GLU OE2 HE2  sing N N 192 
GLU OXT HXT  sing N N 193 
GLY N   CA   sing N N 194 
GLY N   H    sing N N 195 
GLY N   H2   sing N N 196 
GLY CA  C    sing N N 197 
GLY CA  HA2  sing N N 198 
GLY CA  HA3  sing N N 199 
GLY C   O    doub N N 200 
GLY C   OXT  sing N N 201 
GLY OXT HXT  sing N N 202 
HIS N   CA   sing N N 203 
HIS N   H    sing N N 204 
HIS N   H2   sing N N 205 
HIS CA  C    sing N N 206 
HIS CA  CB   sing N N 207 
HIS CA  HA   sing N N 208 
HIS C   O    doub N N 209 
HIS C   OXT  sing N N 210 
HIS CB  CG   sing N N 211 
HIS CB  HB2  sing N N 212 
HIS CB  HB3  sing N N 213 
HIS CG  ND1  sing Y N 214 
HIS CG  CD2  doub Y N 215 
HIS ND1 CE1  doub Y N 216 
HIS ND1 HD1  sing N N 217 
HIS CD2 NE2  sing Y N 218 
HIS CD2 HD2  sing N N 219 
HIS CE1 NE2  sing Y N 220 
HIS CE1 HE1  sing N N 221 
HIS NE2 HE2  sing N N 222 
HIS OXT HXT  sing N N 223 
HOH O   H1   sing N N 224 
HOH O   H2   sing N N 225 
ILE N   CA   sing N N 226 
ILE N   H    sing N N 227 
ILE N   H2   sing N N 228 
ILE CA  C    sing N N 229 
ILE CA  CB   sing N N 230 
ILE CA  HA   sing N N 231 
ILE C   O    doub N N 232 
ILE C   OXT  sing N N 233 
ILE CB  CG1  sing N N 234 
ILE CB  CG2  sing N N 235 
ILE CB  HB   sing N N 236 
ILE CG1 CD1  sing N N 237 
ILE CG1 HG12 sing N N 238 
ILE CG1 HG13 sing N N 239 
ILE CG2 HG21 sing N N 240 
ILE CG2 HG22 sing N N 241 
ILE CG2 HG23 sing N N 242 
ILE CD1 HD11 sing N N 243 
ILE CD1 HD12 sing N N 244 
ILE CD1 HD13 sing N N 245 
ILE OXT HXT  sing N N 246 
LEU N   CA   sing N N 247 
LEU N   H    sing N N 248 
LEU N   H2   sing N N 249 
LEU CA  C    sing N N 250 
LEU CA  CB   sing N N 251 
LEU CA  HA   sing N N 252 
LEU C   O    doub N N 253 
LEU C   OXT  sing N N 254 
LEU CB  CG   sing N N 255 
LEU CB  HB2  sing N N 256 
LEU CB  HB3  sing N N 257 
LEU CG  CD1  sing N N 258 
LEU CG  CD2  sing N N 259 
LEU CG  HG   sing N N 260 
LEU CD1 HD11 sing N N 261 
LEU CD1 HD12 sing N N 262 
LEU CD1 HD13 sing N N 263 
LEU CD2 HD21 sing N N 264 
LEU CD2 HD22 sing N N 265 
LEU CD2 HD23 sing N N 266 
LEU OXT HXT  sing N N 267 
LYS N   CA   sing N N 268 
LYS N   H    sing N N 269 
LYS N   H2   sing N N 270 
LYS CA  C    sing N N 271 
LYS CA  CB   sing N N 272 
LYS CA  HA   sing N N 273 
LYS C   O    doub N N 274 
LYS C   OXT  sing N N 275 
LYS CB  CG   sing N N 276 
LYS CB  HB2  sing N N 277 
LYS CB  HB3  sing N N 278 
LYS CG  CD   sing N N 279 
LYS CG  HG2  sing N N 280 
LYS CG  HG3  sing N N 281 
LYS CD  CE   sing N N 282 
LYS CD  HD2  sing N N 283 
LYS CD  HD3  sing N N 284 
LYS CE  NZ   sing N N 285 
LYS CE  HE2  sing N N 286 
LYS CE  HE3  sing N N 287 
LYS NZ  HZ1  sing N N 288 
LYS NZ  HZ2  sing N N 289 
LYS NZ  HZ3  sing N N 290 
LYS OXT HXT  sing N N 291 
MET N   CA   sing N N 292 
MET N   H    sing N N 293 
MET N   H2   sing N N 294 
MET CA  C    sing N N 295 
MET CA  CB   sing N N 296 
MET CA  HA   sing N N 297 
MET C   O    doub N N 298 
MET C   OXT  sing N N 299 
MET CB  CG   sing N N 300 
MET CB  HB2  sing N N 301 
MET CB  HB3  sing N N 302 
MET CG  SD   sing N N 303 
MET CG  HG2  sing N N 304 
MET CG  HG3  sing N N 305 
MET SD  CE   sing N N 306 
MET CE  HE1  sing N N 307 
MET CE  HE2  sing N N 308 
MET CE  HE3  sing N N 309 
MET OXT HXT  sing N N 310 
PEG C1  O1   sing N N 311 
PEG C1  C2   sing N N 312 
PEG C1  H11  sing N N 313 
PEG C1  H12  sing N N 314 
PEG O1  HO1  sing N N 315 
PEG C2  O2   sing N N 316 
PEG C2  H21  sing N N 317 
PEG C2  H22  sing N N 318 
PEG O2  C3   sing N N 319 
PEG C3  C4   sing N N 320 
PEG C3  H31  sing N N 321 
PEG C3  H32  sing N N 322 
PEG C4  O4   sing N N 323 
PEG C4  H41  sing N N 324 
PEG C4  H42  sing N N 325 
PEG O4  HO4  sing N N 326 
PHE N   CA   sing N N 327 
PHE N   H    sing N N 328 
PHE N   H2   sing N N 329 
PHE CA  C    sing N N 330 
PHE CA  CB   sing N N 331 
PHE CA  HA   sing N N 332 
PHE C   O    doub N N 333 
PHE C   OXT  sing N N 334 
PHE CB  CG   sing N N 335 
PHE CB  HB2  sing N N 336 
PHE CB  HB3  sing N N 337 
PHE CG  CD1  doub Y N 338 
PHE CG  CD2  sing Y N 339 
PHE CD1 CE1  sing Y N 340 
PHE CD1 HD1  sing N N 341 
PHE CD2 CE2  doub Y N 342 
PHE CD2 HD2  sing N N 343 
PHE CE1 CZ   doub Y N 344 
PHE CE1 HE1  sing N N 345 
PHE CE2 CZ   sing Y N 346 
PHE CE2 HE2  sing N N 347 
PHE CZ  HZ   sing N N 348 
PHE OXT HXT  sing N N 349 
PRO N   CA   sing N N 350 
PRO N   CD   sing N N 351 
PRO N   H    sing N N 352 
PRO CA  C    sing N N 353 
PRO CA  CB   sing N N 354 
PRO CA  HA   sing N N 355 
PRO C   O    doub N N 356 
PRO C   OXT  sing N N 357 
PRO CB  CG   sing N N 358 
PRO CB  HB2  sing N N 359 
PRO CB  HB3  sing N N 360 
PRO CG  CD   sing N N 361 
PRO CG  HG2  sing N N 362 
PRO CG  HG3  sing N N 363 
PRO CD  HD2  sing N N 364 
PRO CD  HD3  sing N N 365 
PRO OXT HXT  sing N N 366 
SER N   CA   sing N N 367 
SER N   H    sing N N 368 
SER N   H2   sing N N 369 
SER CA  C    sing N N 370 
SER CA  CB   sing N N 371 
SER CA  HA   sing N N 372 
SER C   O    doub N N 373 
SER C   OXT  sing N N 374 
SER CB  OG   sing N N 375 
SER CB  HB2  sing N N 376 
SER CB  HB3  sing N N 377 
SER OG  HG   sing N N 378 
SER OXT HXT  sing N N 379 
THR N   CA   sing N N 380 
THR N   H    sing N N 381 
THR N   H2   sing N N 382 
THR CA  C    sing N N 383 
THR CA  CB   sing N N 384 
THR CA  HA   sing N N 385 
THR C   O    doub N N 386 
THR C   OXT  sing N N 387 
THR CB  OG1  sing N N 388 
THR CB  CG2  sing N N 389 
THR CB  HB   sing N N 390 
THR OG1 HG1  sing N N 391 
THR CG2 HG21 sing N N 392 
THR CG2 HG22 sing N N 393 
THR CG2 HG23 sing N N 394 
THR OXT HXT  sing N N 395 
TRP N   CA   sing N N 396 
TRP N   H    sing N N 397 
TRP N   H2   sing N N 398 
TRP CA  C    sing N N 399 
TRP CA  CB   sing N N 400 
TRP CA  HA   sing N N 401 
TRP C   O    doub N N 402 
TRP C   OXT  sing N N 403 
TRP CB  CG   sing N N 404 
TRP CB  HB2  sing N N 405 
TRP CB  HB3  sing N N 406 
TRP CG  CD1  doub Y N 407 
TRP CG  CD2  sing Y N 408 
TRP CD1 NE1  sing Y N 409 
TRP CD1 HD1  sing N N 410 
TRP CD2 CE2  doub Y N 411 
TRP CD2 CE3  sing Y N 412 
TRP NE1 CE2  sing Y N 413 
TRP NE1 HE1  sing N N 414 
TRP CE2 CZ2  sing Y N 415 
TRP CE3 CZ3  doub Y N 416 
TRP CE3 HE3  sing N N 417 
TRP CZ2 CH2  doub Y N 418 
TRP CZ2 HZ2  sing N N 419 
TRP CZ3 CH2  sing Y N 420 
TRP CZ3 HZ3  sing N N 421 
TRP CH2 HH2  sing N N 422 
TRP OXT HXT  sing N N 423 
TYR N   CA   sing N N 424 
TYR N   H    sing N N 425 
TYR N   H2   sing N N 426 
TYR CA  C    sing N N 427 
TYR CA  CB   sing N N 428 
TYR CA  HA   sing N N 429 
TYR C   O    doub N N 430 
TYR C   OXT  sing N N 431 
TYR CB  CG   sing N N 432 
TYR CB  HB2  sing N N 433 
TYR CB  HB3  sing N N 434 
TYR CG  CD1  doub Y N 435 
TYR CG  CD2  sing Y N 436 
TYR CD1 CE1  sing Y N 437 
TYR CD1 HD1  sing N N 438 
TYR CD2 CE2  doub Y N 439 
TYR CD2 HD2  sing N N 440 
TYR CE1 CZ   doub Y N 441 
TYR CE1 HE1  sing N N 442 
TYR CE2 CZ   sing Y N 443 
TYR CE2 HE2  sing N N 444 
TYR CZ  OH   sing N N 445 
TYR OH  HH   sing N N 446 
TYR OXT HXT  sing N N 447 
VAL N   CA   sing N N 448 
VAL N   H    sing N N 449 
VAL N   H2   sing N N 450 
VAL CA  C    sing N N 451 
VAL CA  CB   sing N N 452 
VAL CA  HA   sing N N 453 
VAL C   O    doub N N 454 
VAL C   OXT  sing N N 455 
VAL CB  CG1  sing N N 456 
VAL CB  CG2  sing N N 457 
VAL CB  HB   sing N N 458 
VAL CG1 HG11 sing N N 459 
VAL CG1 HG12 sing N N 460 
VAL CG1 HG13 sing N N 461 
VAL CG2 HG21 sing N N 462 
VAL CG2 HG22 sing N N 463 
VAL CG2 HG23 sing N N 464 
VAL OXT HXT  sing N N 465 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                  ZN  
3 '2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' EWW 
4 'DI(HYDROXYETHYL)ETHER'                                                                     PEG 
5 'DIMETHYL SULFOXIDE'                                                                        DMS 
6 'CITRIC ACID'                                                                               CIT 
7 1,2-ETHANEDIOL                                                                              EDO 
8 'NICKEL (II) ION'                                                                           NI  
9 water                                                                                       HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2NNO 
_pdbx_initial_refinement_model.details          ? 
# 
