data_4QJP
# 
_entry.id   4QJP 
# 
_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   4QJP         pdb_00004qjp 10.2210/pdb4qjp/pdb 
RCSB  RCSB086140   ?            ?                   
WWPDB D_1000086140 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4QIY . unspecified 
PDB 4QIZ . unspecified 
PDB 4QJ0 . unspecified 
PDB 4QJM . unspecified 
PDB 4QJO . unspecified 
PDB 4QJW . unspecified 
PDB 4QJX . unspecified 
PDB 4QTL . unspecified 
# 
_pdbx_database_status.entry_id                        4QJP 
_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   2014-06-04 
_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 
'Manakova, E.' 1 
'Smirnov, A.'  2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Functionalization of Fluorinated Benzenesulfonamides and Their Inhibitory Properties toward Carbonic Anhydrases' 
_citation.journal_abbrev            Chemmedchem 
_citation.journal_volume            10 
_citation.page_first                662 
_citation.page_last                 687 
_citation.year                      2015 
_citation.journal_id_ASTM           ? 
_citation.country                   DE 
_citation.journal_id_ISSN           1860-7179 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25758852 
_citation.pdbx_database_id_DOI      10.1002/cmdc.201402490 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dudutiene, V.'     1  ? 
primary 'Zubriene, A.'      2  ? 
primary 'Smirnov, A.'       3  ? 
primary 'Timm, D.D.'        4  ? 
primary 'Smirnoviene, J.'   5  ? 
primary 'Kazokaite, J.'     6  ? 
primary 'Michailoviene, V.' 7  ? 
primary 'Zaksauskas, A.'    8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Matulis, D.'       11 ? 
# 
_cell.entry_id           4QJP 
_cell.length_a           56.043 
_cell.length_b           57.544 
_cell.length_c           159.521 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              8 
_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                         4QJP 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.Int_Tables_number                19 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 13'                                                         29613.318 2   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                      65.409    2   ?       ? ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                         106.120   1   ?       ? ? ? 
4 non-polymer syn '3-(benzylamino)-2,5,6-trifluoro-4-[(2-phenylethyl)sulfonyl]benzenesulfonamide' 484.512   2   ?       ? ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                                  62.068    4   ?       ? ? ? 
6 non-polymer syn 'CITRIC ACID'                                                                   192.124   1   ?       ? ? ? 
7 water       nat water                                                                           18.015    483 ?       ? ? ? 
# 
_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 4QJP B 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
2 1 4QJP A 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
# 
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 4QJP MET B 1 ? UNP Q8N1Q1 ? ? 'expression tag' 1 1 
2 4QJP 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 
EDO non-polymer         . 1,2-ETHANEDIOL                                                                  'ETHYLENE GLYCOL' 
'C2 H6 O2'            62.068  
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 
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 
V1F non-polymer         . '3-(benzylamino)-2,5,6-trifluoro-4-[(2-phenylethyl)sulfonyl]benzenesulfonamide' ?                 
'C21 H19 F3 N2 O4 S2' 484.512 
VAL 'L-peptide linking' y VALINE                                                                          ?                 
'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                                                      ?                 'Zn 2' 
65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4QJP 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   42.2 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.pdbx_mosaicity        0.06 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    
'0.1M sodium citrate (pH 5.5), 0.1M sodium acetate (pH 4.5), 26% PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2012-12-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    
'High Heat Load (HHL) Monochromator: Si 111; Large Offset Monochromator (LOM): Si 311, Si 511' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
# 
_reflns.entry_id                     4QJP 
_reflns.d_resolution_high            1.620 
_reflns.d_resolution_low             159.521 
_reflns.number_all                   ? 
_reflns.number_obs                   65652 
_reflns.pdbx_netI_over_sigmaI        26.300 
_reflns.pdbx_Rsym_value              0.038 
_reflns.pdbx_redundancy              6.500 
_reflns.percent_possible_obs         98.500 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        19.076 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_CC_half                 ? 
_reflns.pdbx_Rpim_I_all              ? 
_reflns.pdbx_Rrim_I_all              ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
1.62 1.71   ? 43832 ? ? 0.141 5.3  0.141 ? 5.10 ? 8.10  ? 8635 ? ? 0.174 ? 90.00  0.17 0.07 1  1 ? 
1.71 1.81   ? 62508 ? ? 0.107 6.8  0.107 ? 6.90 ? 13.20 ? 9085 ? ? 0.128 ? 100.00 0.13 0.05 2  1 ? 
1.81 1.94   ? 56869 ? ? 0.076 8.9  0.076 ? 6.60 ? 17.90 ? 8555 ? ? 0.092 ? 100.00 0.09 0.04 3  1 ? 
1.94 2.09   ? 53551 ? ? 0.057 11.3 0.057 ? 6.70 ? 24.00 ? 7960 ? ? 0.068 ? 100.00 0.07 0.03 4  1 ? 
2.09 2.29   ? 50163 ? ? 0.048 13.1 0.048 ? 6.80 ? 29.40 ? 7398 ? ? 0.057 ? 100.00 0.06 0.02 5  1 ? 
2.29 2.56   ? 43876 ? ? 0.041 14.5 0.041 ? 6.60 ? 33.80 ? 6673 ? ? 0.050 ? 100.00 0.05 0.02 6  1 ? 
2.56 2.96   ? 40482 ? ? 0.037 15.8 0.037 ? 6.80 ? 39.00 ? 5958 ? ? 0.044 ? 100.00 0.04 0.02 7  1 ? 
2.96 3.62   ? 33441 ? ? 0.032 17.2 0.032 ? 6.60 ? 43.90 ? 5067 ? ? 0.038 ? 100.00 0.04 0.01 8  1 ? 
3.62 5.12   ? 25810 ? ? 0.031 17.9 0.031 ? 6.50 ? 46.80 ? 3988 ? ? 0.036 ? 100.00 0.04 0.01 9  1 ? 
5.12 159.52 ? 14386 ? ? 0.033 11.0 0.033 ? 6.20 ? 45.20 ? 2333 ? ? 0.040 ? 100.00 0.04 0.02 10 1 ? 
# 
_refine.entry_id                                 4QJP 
_refine.ls_d_res_high                            1.620 
_refine.ls_d_res_low                             54.130 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    98.560 
_refine.ls_number_reflns_obs                     65569 
_refine.ls_number_reflns_all                     65569 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES' 
_refine.ls_R_factor_all                          0.172 
_refine.ls_R_factor_obs                          0.172 
_refine.ls_R_factor_R_work                       0.168 
_refine.ls_wR_factor_R_work                      0.177 
_refine.ls_R_factor_R_free                       0.205 
_refine.ls_wR_factor_R_free                      0.220 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  6556 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               21.005 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.250 
_refine.aniso_B[2][2]                            0.650 
_refine.aniso_B[3][3]                            -0.900 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.953 
_refine.overall_SU_R_Cruickshank_DPI             0.099 
_refine.overall_SU_R_free                        0.099 
_refine.pdbx_overall_ESU_R                       0.099 
_refine.pdbx_overall_ESU_R_Free                  0.099 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.876 
_refine.B_iso_max                                76.56 
_refine.B_iso_min                                8.11 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      2NNO 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4108 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         102 
_refine_hist.number_atoms_solvent             483 
_refine_hist.number_atoms_total               4693 
_refine_hist.d_res_high                       1.620 
_refine_hist.d_res_low                        54.130 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       4473 0.025  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    6113 2.441  1.967  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 545  6.892  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 205  32.981 24.293 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 703  13.465 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 20   18.286 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr         637  0.183  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   3506 0.014  0.021  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.620 
_refine_ls_shell.d_res_low                        1.662 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               80.910 
_refine_ls_shell.number_reflns_R_work             3551 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.216 
_refine_ls_shell.R_factor_R_free                  0.260 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             374 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                3925 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  4QJP 
_struct.title                     'Crystal structure of human carbonic anhydrase isozyme XIII with inhibitor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4QJP 
_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 2 ? 
H N N 6 ? 
I N N 4 ? 
J N N 5 ? 
K N N 5 ? 
L N N 5 ? 
M N N 7 ? 
N N N 7 ? 
# 
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  ? PHE A 21  ? GLY B 14  PHE B 21  5 ? 8 
HELX_P HELX_P2  2  PHE A 22  ? GLY A 27  ? PHE B 22  GLY B 27  5 ? 6 
HELX_P HELX_P3  3  LYS A 36  ? VAL A 40  ? LYS B 36  VAL B 40  5 ? 5 
HELX_P HELX_P4  4  SER A 132 ? ALA A 137 ? SER B 132 ALA B 137 1 ? 6 
HELX_P HELX_P5  5  ASN A 156 ? GLN A 158 ? ASN B 156 GLN B 158 5 ? 3 
HELX_P HELX_P6  6  LEU A 159 ? ASP A 164 ? LEU B 159 ASP B 164 1 ? 6 
HELX_P HELX_P7  7  THR A 165 ? LYS A 170 ? THR B 165 LYS B 170 5 ? 6 
HELX_P HELX_P8  8  LEU A 183 ? LEU A 187 ? LEU B 183 LEU B 187 5 ? 5 
HELX_P HELX_P9  9  SER A 221 ? ARG A 229 ? SER B 221 ARG B 229 1 ? 9 
HELX_P HELX_P10 10 GLY B 14  ? ILE B 16  ? GLY A 14  ILE A 16  5 ? 3 
HELX_P HELX_P11 11 HIS B 17  ? PHE B 22  ? HIS A 17  PHE A 22  1 ? 6 
HELX_P HELX_P12 12 PRO B 23  ? GLY B 27  ? PRO A 23  GLY A 27  5 ? 5 
HELX_P HELX_P13 13 ASP B 54  ? SER B 56  ? ASP A 54  SER A 56  5 ? 3 
HELX_P HELX_P14 14 SER B 132 ? ALA B 137 ? SER A 132 ALA A 137 1 ? 6 
HELX_P HELX_P15 15 ASN B 156 ? ASP B 164 ? ASN A 156 ASP A 164 1 ? 9 
HELX_P HELX_P16 16 THR B 165 ? LYS B 170 ? THR A 165 LYS A 170 5 ? 6 
HELX_P HELX_P17 17 ASP B 182 ? LEU B 187 ? ASP A 182 LEU A 187 1 ? 6 
HELX_P HELX_P18 18 SER B 221 ? ARG B 229 ? SER A 221 ARG A 229 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 96  B ZN  301 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc2  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 98  B ZN  301 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc3  metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 121 B ZN  301 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc4  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 E V1F . N10 ? ? B ZN  301 B V1F 303 1_555 ? ? ? ? ? ? ? 1.972 ? ? 
metalc5  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 E V1F . O9  ? ? B ZN  301 B V1F 303 1_555 ? ? ? ? ? ? ? 2.639 ? ? 
metalc6  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 E V1F . S7  ? ? B ZN  301 B V1F 303 1_555 ? ? ? ? ? ? ? 2.884 ? ? 
metalc7  metalc ? ? B HIS 96  NE2 ? ? ? 1_555 G ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 1.941 ? ? 
metalc8  metalc ? ? B HIS 98  NE2 ? ? ? 1_555 G ZN  . ZN  ? ? A HIS 98  A ZN  301 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
metalc9  metalc ? ? B HIS 121 ND1 ? ? ? 1_555 G ZN  . ZN  ? ? A HIS 121 A ZN  301 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc10 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 I V1F . N10 ? ? A ZN  301 A V1F 303 1_555 ? ? ? ? ? ? ? 1.991 ? ? 
metalc11 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 I V1F . S7  ? ? A ZN  301 A V1F 303 1_555 ? ? ? ? ? ? ? 2.844 ? ? 
# 
_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 31  B PRO 32  A ? PRO 32  B 1 -1.31 
2 PRO 203 A . ? PRO 203 B PRO 204 A ? PRO 204 B 1 11.22 
3 SER 31  B . ? SER 31  A PRO 32  B ? PRO 32  A 1 -2.38 
4 PRO 203 B . ? PRO 203 A PRO 204 B ? PRO 204 A 1 12.53 
# 
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 34  ILE B 35  
A 2  ILE A 110 ? VAL A 111 ? ILE B 110 VAL B 111 
B 1  LYS A 41  ? TYR A 42  ? LYS B 41  TYR B 42  
B 2  ARG A 259 ? ALA A 260 ? ARG B 259 ALA B 260 
B 3  TYR A 193 ? GLY A 198 ? TYR B 193 GLY B 198 
B 4  VAL A 209 ? LEU A 214 ? VAL B 209 LEU B 214 
B 5  LEU A 143 ? ILE A 152 ? LEU B 143 ILE B 152 
B 6  ALA A 118 ? ASN A 126 ? ALA B 118 ASN B 126 
B 7  TYR A 90  ? TRP A 99  ? TYR B 90  TRP B 99  
B 8  PHE A 68  ? PHE A 72  ? PHE B 68  PHE B 72  
B 9  ALA A 58  ? ASN A 63  ? ALA B 58  ASN B 63  
B 10 GLN A 175 ? ARG A 177 ? GLN B 175 ARG B 177 
C 1  ARG A 47  ? LYS A 52  ? ARG B 47  LYS B 52  
C 2  VAL A 80  ? GLY A 84  ? VAL B 80  GLY B 84  
C 3  TYR A 90  ? TRP A 99  ? TYR B 90  TRP B 99  
C 4  ALA A 118 ? ASN A 126 ? ALA B 118 ASN B 126 
C 5  LEU A 143 ? ILE A 152 ? LEU B 143 ILE B 152 
C 6  ILE A 218 ? ILE A 220 ? ILE B 218 ILE B 220 
D 1  GLU B 34  ? ILE B 35  ? GLU A 34  ILE A 35  
D 2  ILE B 110 ? VAL B 111 ? ILE A 110 VAL A 111 
E 1  LYS B 41  ? TYR B 42  ? LYS A 41  TYR A 42  
E 2  ARG B 259 ? ALA B 260 ? ARG A 259 ALA A 260 
E 3  TYR B 193 ? GLY B 198 ? TYR A 193 GLY A 198 
E 4  VAL B 209 ? LEU B 214 ? VAL A 209 LEU A 214 
E 5  LEU B 143 ? ILE B 152 ? LEU A 143 ILE A 152 
E 6  ALA B 118 ? ASN B 126 ? ALA A 118 ASN A 126 
E 7  TYR B 90  ? TRP B 99  ? TYR A 90  TRP A 99  
E 8  PHE B 68  ? PHE B 72  ? PHE A 68  PHE A 72  
E 9  ALA B 58  ? ASN B 63  ? ALA A 58  ASN A 63  
E 10 GLN B 175 ? ARG B 177 ? GLN A 175 ARG A 177 
F 1  LEU B 49  ? LYS B 52  ? LEU A 49  LYS A 52  
F 2  VAL B 80  ? GLY B 83  ? VAL A 80  GLY A 83  
F 3  TYR B 90  ? TRP B 99  ? TYR A 90  TRP A 99  
F 4  ALA B 118 ? ASN B 126 ? ALA A 118 ASN A 126 
F 5  LEU B 143 ? ILE B 152 ? LEU A 143 ILE A 152 
F 6  ILE B 218 ? ILE B 220 ? ILE A 218 ILE A 220 
# 
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 35  O ILE A 110 ? O ILE B 110 
B 1 2  N LYS A 41  ? N LYS B 41  O ALA A 260 ? O ALA B 260 
B 2 3  O ARG A 259 ? O ARG B 259 N THR A 195 ? N THR B 195 
B 3 4  N GLY A 198 ? N GLY B 198 O VAL A 209 ? O VAL B 209 
B 4 5  O LEU A 214 ? O LEU B 214 N GLY A 147 ? N GLY B 147 
B 5 6  O VAL A 148 ? O VAL B 148 N LEU A 120 ? N LEU B 120 
B 6 7  O VAL A 123 ? O VAL B 123 N ARG A 93  ? N ARG B 93  
B 7 8  O VAL A 95  ? O VAL B 95  N VAL A 70  ? N VAL B 70  
B 8 9  O ASP A 71  ? O ASP B 71  N LYS A 59  ? N LYS B 59  
B 9 10 N ILE A 61  ? N ILE B 61  O THR A 176 ? O THR B 176 
C 1 2  N SER A 50  ? N SER B 50  O ARG A 82  ? O ARG B 82  
C 2 3  N LEU A 81  ? N LEU B 81  O TYR A 90  ? O TYR B 90  
C 3 4  N ARG A 93  ? N ARG B 93  O VAL A 123 ? O VAL B 123 
C 4 5  N LEU A 120 ? N LEU B 120 O VAL A 148 ? O VAL B 148 
C 5 6  N PHE A 149 ? N PHE B 149 O ILE A 218 ? O ILE B 218 
D 1 2  N ILE B 35  ? N ILE A 35  O ILE B 110 ? O ILE A 110 
E 1 2  N LYS B 41  ? N LYS A 41  O ALA B 260 ? O ALA A 260 
E 2 3  O ARG B 259 ? O ARG A 259 N THR B 195 ? N THR A 195 
E 3 4  N GLY B 198 ? N GLY A 198 O VAL B 209 ? O VAL A 209 
E 4 5  O ILE B 212 ? O ILE A 212 N GLY B 147 ? N GLY A 147 
E 5 6  O VAL B 148 ? O VAL A 148 N LEU B 120 ? N LEU A 120 
E 6 7  O VAL B 123 ? O VAL A 123 N GLN B 94  ? N GLN A 94  
E 7 8  O VAL B 95  ? O VAL A 95  N VAL B 70  ? N VAL A 70  
E 8 9  O ASP B 71  ? O ASP A 71  N ILE B 60  ? N ILE A 60  
E 9 10 N ILE B 61  ? N ILE A 61  O THR B 176 ? O THR A 176 
F 1 2  N SER B 50  ? N SER A 50  O ARG B 82  ? O ARG A 82  
F 2 3  N LEU B 81  ? N LEU A 81  O TYR B 90  ? O TYR A 90  
F 3 4  N GLN B 94  ? N GLN A 94  O VAL B 123 ? O VAL A 123 
F 4 5  N LEU B 120 ? N LEU A 120 O VAL B 148 ? O VAL A 148 
F 5 6  N GLN B 151 ? N GLN A 151 O ILE B 218 ? O ILE A 218 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software B ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN B 301'  
AC2 Software B PEG 302 ? 8  'BINDING SITE FOR RESIDUE PEG B 302' 
AC3 Software B V1F 303 ? 18 'BINDING SITE FOR RESIDUE V1F B 303' 
AC4 Software B EDO 304 ? 6  'BINDING SITE FOR RESIDUE EDO B 304' 
AC5 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC6 Software A CIT 302 ? 8  'BINDING SITE FOR RESIDUE CIT A 302' 
AC7 Software A V1F 303 ? 18 'BINDING SITE FOR RESIDUE V1F A 303' 
AC8 Software A EDO 304 ? 6  'BINDING SITE FOR RESIDUE EDO A 304' 
AC9 Software A EDO 305 ? 4  'BINDING SITE FOR RESIDUE EDO A 305' 
BC1 Software A EDO 306 ? 5  'BINDING SITE FOR RESIDUE EDO A 306' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 96  ? HIS B 96  . ? 1_555 ? 
2  AC1 4  HIS A 98  ? HIS B 98  . ? 1_555 ? 
3  AC1 4  HIS A 121 ? HIS B 121 . ? 1_555 ? 
4  AC1 4  V1F E .   ? V1F B 303 . ? 1_555 ? 
5  AC2 8  LYS B 59  ? LYS A 59  . ? 1_545 ? 
6  AC2 8  ILE B 60  ? ILE A 60  . ? 1_545 ? 
7  AC2 8  ARG B 177 ? ARG A 177 . ? 1_545 ? 
8  AC2 8  ASP A 28  ? ASP B 28  . ? 1_555 ? 
9  AC2 8  GLN A 29  ? GLN B 29  . ? 1_555 ? 
10 AC2 8  LEU A 253 ? LEU B 253 . ? 1_555 ? 
11 AC2 8  LYS A 254 ? LYS B 254 . ? 1_555 ? 
12 AC2 8  ARG A 256 ? ARG B 256 . ? 1_555 ? 
13 AC3 18 SER A 64  ? SER B 64  . ? 1_555 ? 
14 AC3 18 HIS A 66  ? HIS B 66  . ? 1_555 ? 
15 AC3 18 ASN A 69  ? ASN B 69  . ? 1_555 ? 
16 AC3 18 GLN A 94  ? GLN B 94  . ? 1_555 ? 
17 AC3 18 HIS A 96  ? HIS B 96  . ? 1_555 ? 
18 AC3 18 HIS A 98  ? HIS B 98  . ? 1_555 ? 
19 AC3 18 HIS A 121 ? HIS B 121 . ? 1_555 ? 
20 AC3 18 VAL A 123 ? VAL B 123 . ? 1_555 ? 
21 AC3 18 PHE A 133 ? PHE B 133 . ? 1_555 ? 
22 AC3 18 ALA A 137 ? ALA B 137 . ? 1_555 ? 
23 AC3 18 LEU A 200 ? LEU B 200 . ? 1_555 ? 
24 AC3 18 THR A 201 ? THR B 201 . ? 1_555 ? 
25 AC3 18 VAL A 202 ? VAL B 202 . ? 1_555 ? 
26 AC3 18 PRO A 204 ? PRO B 204 . ? 1_555 ? 
27 AC3 18 ZN  C .   ? ZN  B 301 . ? 1_555 ? 
28 AC3 18 HOH M .   ? HOH B 608 . ? 1_555 ? 
29 AC3 18 HOH M .   ? HOH B 637 . ? 1_555 ? 
30 AC3 18 HOH M .   ? HOH B 639 . ? 1_555 ? 
31 AC4 6  GLY A 100 ? GLY B 100 . ? 1_555 ? 
32 AC4 6  SER A 101 ? SER B 101 . ? 1_555 ? 
33 AC4 6  HIS A 105 ? HIS B 105 . ? 1_555 ? 
34 AC4 6  SER A 245 ? SER B 245 . ? 1_555 ? 
35 AC4 6  HIS A 247 ? HIS B 247 . ? 1_555 ? 
36 AC4 6  HOH M .   ? HOH B 420 . ? 1_555 ? 
37 AC5 4  HIS B 96  ? HIS A 96  . ? 1_555 ? 
38 AC5 4  HIS B 98  ? HIS A 98  . ? 1_555 ? 
39 AC5 4  HIS B 121 ? HIS A 121 . ? 1_555 ? 
40 AC5 4  V1F I .   ? V1F A 303 . ? 1_555 ? 
41 AC6 8  GLY B 100 ? GLY A 100 . ? 1_555 ? 
42 AC6 8  SER B 101 ? SER A 101 . ? 1_555 ? 
43 AC6 8  HIS B 105 ? HIS A 105 . ? 1_555 ? 
44 AC6 8  SER B 245 ? SER A 245 . ? 1_555 ? 
45 AC6 8  HIS B 247 ? HIS A 247 . ? 1_555 ? 
46 AC6 8  HOH N .   ? HOH A 485 . ? 1_555 ? 
47 AC6 8  HOH N .   ? HOH A 618 . ? 1_555 ? 
48 AC6 8  HOH M .   ? HOH B 499 . ? 4_545 ? 
49 AC7 18 HIS B 66  ? HIS A 66  . ? 1_555 ? 
50 AC7 18 ASN B 69  ? ASN A 69  . ? 1_555 ? 
51 AC7 18 GLN B 94  ? GLN A 94  . ? 1_555 ? 
52 AC7 18 HIS B 96  ? HIS A 96  . ? 1_555 ? 
53 AC7 18 HIS B 98  ? HIS A 98  . ? 1_555 ? 
54 AC7 18 HIS B 121 ? HIS A 121 . ? 1_555 ? 
55 AC7 18 VAL B 123 ? VAL A 123 . ? 1_555 ? 
56 AC7 18 PHE B 133 ? PHE A 133 . ? 1_555 ? 
57 AC7 18 VAL B 145 ? VAL A 145 . ? 1_555 ? 
58 AC7 18 LEU B 200 ? LEU A 200 . ? 1_555 ? 
59 AC7 18 THR B 201 ? THR A 201 . ? 1_555 ? 
60 AC7 18 VAL B 202 ? VAL A 202 . ? 1_555 ? 
61 AC7 18 TRP B 211 ? TRP A 211 . ? 1_555 ? 
62 AC7 18 ZN  G .   ? ZN  A 301 . ? 1_555 ? 
63 AC7 18 HOH N .   ? HOH A 487 . ? 1_555 ? 
64 AC7 18 HOH N .   ? HOH A 590 . ? 1_555 ? 
65 AC7 18 HOH N .   ? HOH A 641 . ? 1_555 ? 
66 AC7 18 HOH N .   ? HOH A 643 . ? 1_555 ? 
67 AC8 6  GLN B 160 ? GLN A 160 . ? 1_555 ? 
68 AC8 6  GLN B 223 ? GLN A 223 . ? 1_555 ? 
69 AC8 6  LYS B 227 ? LYS A 227 . ? 1_555 ? 
70 AC8 6  HOH N .   ? HOH A 458 . ? 4_445 ? 
71 AC8 6  HOH N .   ? HOH A 611 . ? 4_445 ? 
72 AC8 6  HOH N .   ? HOH A 614 . ? 1_555 ? 
73 AC9 4  LEU B 166 ? LEU A 166 . ? 1_555 ? 
74 AC9 4  ASP B 167 ? ASP A 167 . ? 1_555 ? 
75 AC9 4  LYS B 170 ? LYS A 170 . ? 1_555 ? 
76 AC9 4  SER B 230 ? SER A 230 . ? 1_555 ? 
77 BC1 5  ASP B 104 ? ASP A 104 . ? 1_555 ? 
78 BC1 5  VAL B 114 ? VAL A 114 . ? 1_555 ? 
79 BC1 5  SER B 115 ? SER A 115 . ? 1_555 ? 
80 BC1 5  SER B 157 ? SER A 157 . ? 4_545 ? 
81 BC1 5  HOH N .   ? HOH A 639 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4QJP 
_atom_sites.fract_transf_matrix[1][1]   0.017843 
_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]   0.017378 
_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]   0.006269 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 6   ? -50.575 -42.220 26.428  1.00 35.56 ? 6   SER B N   1 
ATOM   2    C  CA  . SER A 1 6   ? -50.629 -41.807 27.888  1.00 39.96 ? 6   SER B CA  1 
ATOM   3    C  C   . SER A 1 6   ? -49.431 -42.397 28.706  1.00 35.11 ? 6   SER B C   1 
ATOM   4    O  O   . SER A 1 6   ? -49.543 -42.774 29.896  1.00 33.08 ? 6   SER B O   1 
ATOM   5    C  CB  . SER A 1 6   ? -51.944 -42.288 28.513  1.00 41.73 ? 6   SER B CB  1 
ATOM   6    O  OG  . SER A 1 6   ? -51.784 -43.670 28.852  1.00 42.40 ? 6   SER B OG  1 
ATOM   7    N  N   . TRP A 1 7   ? -48.261 -42.469 28.094  1.00 25.46 ? 7   TRP B N   1 
ATOM   8    C  CA  . TRP A 1 7   ? -47.059 -42.904 28.847  1.00 23.22 ? 7   TRP B CA  1 
ATOM   9    C  C   . TRP A 1 7   ? -46.648 -41.740 29.750  1.00 20.46 ? 7   TRP B C   1 
ATOM   10   O  O   . TRP A 1 7   ? -47.031 -40.604 29.530  1.00 19.55 ? 7   TRP B O   1 
ATOM   11   C  CB  . TRP A 1 7   ? -45.913 -43.313 27.893  1.00 19.30 ? 7   TRP B CB  1 
ATOM   12   C  CG  . TRP A 1 7   ? -45.440 -42.131 27.071  1.00 17.99 ? 7   TRP B CG  1 
ATOM   13   C  CD1 . TRP A 1 7   ? -45.916 -41.679 25.837  1.00 20.14 ? 7   TRP B CD1 1 
ATOM   14   C  CD2 . TRP A 1 7   ? -44.402 -41.177 27.452  1.00 16.63 ? 7   TRP B CD2 1 
ATOM   15   N  NE1 . TRP A 1 7   ? -45.238 -40.549 25.442  1.00 22.91 ? 7   TRP B NE1 1 
ATOM   16   C  CE2 . TRP A 1 7   ? -44.313 -40.196 26.368  1.00 20.11 ? 7   TRP B CE2 1 
ATOM   17   C  CE3 . TRP A 1 7   ? -43.557 -41.045 28.543  1.00 15.95 ? 7   TRP B CE3 1 
ATOM   18   C  CZ2 . TRP A 1 7   ? -43.410 -39.145 26.403  1.00 17.41 ? 7   TRP B CZ2 1 
ATOM   19   C  CZ3 . TRP A 1 7   ? -42.652 -39.985 28.568  1.00 16.82 ? 7   TRP B CZ3 1 
ATOM   20   C  CH2 . TRP A 1 7   ? -42.581 -39.059 27.524  1.00 17.93 ? 7   TRP B CH2 1 
ATOM   21   N  N   . GLY A 1 8   ? -45.867 -42.050 30.781  1.00 20.01 ? 8   GLY B N   1 
ATOM   22   C  CA  . GLY A 1 8   ? -45.378 -40.999 31.691  1.00 18.83 ? 8   GLY B CA  1 
ATOM   23   C  C   . GLY A 1 8   ? -44.327 -41.551 32.603  1.00 16.63 ? 8   GLY B C   1 
ATOM   24   O  O   . GLY A 1 8   ? -43.522 -42.378 32.228  1.00 17.23 ? 8   GLY B O   1 
ATOM   25   N  N   . TYR A 1 9   ? -44.353 -41.111 33.886  1.00 16.80 ? 9   TYR B N   1 
ATOM   26   C  CA  . TYR A 1 9   ? -43.312 -41.544 34.808  1.00 16.64 ? 9   TYR B CA  1 
ATOM   27   C  C   . TYR A 1 9   ? -43.943 -41.833 36.158  1.00 20.16 ? 9   TYR B C   1 
ATOM   28   O  O   . TYR A 1 9   ? -43.245 -41.939 37.147  1.00 21.97 ? 9   TYR B O   1 
ATOM   29   C  CB  . TYR A 1 9   ? -42.333 -40.346 35.024  1.00 15.72 ? 9   TYR B CB  1 
ATOM   30   C  CG  . TYR A 1 9   ? -41.504 -39.989 33.785  1.00 11.60 ? 9   TYR B CG  1 
ATOM   31   C  CD1 . TYR A 1 9   ? -40.305 -40.680 33.557  1.00 12.43 ? 9   TYR B CD1 1 
ATOM   32   C  CD2 . TYR A 1 9   ? -41.962 -38.961 32.889  1.00 12.04 ? 9   TYR B CD2 1 
ATOM   33   C  CE1 . TYR A 1 9   ? -39.533 -40.377 32.395  1.00 13.61 ? 9   TYR B CE1 1 
ATOM   34   C  CE2 . TYR A 1 9   ? -41.183 -38.656 31.743  1.00 11.98 ? 9   TYR B CE2 1 
ATOM   35   C  CZ  . TYR A 1 9   ? -39.996 -39.336 31.578  1.00 13.53 ? 9   TYR B CZ  1 
ATOM   36   O  OH  . TYR A 1 9   ? -39.331 -38.973 30.396  1.00 13.65 ? 9   TYR B OH  1 
ATOM   37   N  N   . ARG A 1 10  ? -45.273 -41.969 36.135  1.00 23.07 ? 10  ARG B N   1 
ATOM   38   C  CA  . ARG A 1 10  ? -46.020 -42.560 37.302  1.00 26.50 ? 10  ARG B CA  1 
ATOM   39   C  C   . ARG A 1 10  ? -45.942 -44.108 37.410  1.00 29.39 ? 10  ARG B C   1 
ATOM   40   O  O   . ARG A 1 10  ? -45.378 -44.839 36.572  1.00 25.34 ? 10  ARG B O   1 
ATOM   41   C  CB  . ARG A 1 10  ? -47.413 -41.961 37.305  1.00 29.54 ? 10  ARG B CB  1 
ATOM   42   C  CG  . ARG A 1 10  ? -47.333 -40.463 37.268  1.00 33.43 ? 10  ARG B CG  1 
ATOM   43   C  CD  . ARG A 1 10  ? -48.651 -39.782 37.056  1.00 42.79 ? 10  ARG B CD  1 
ATOM   44   N  NE  . ARG A 1 10  ? -49.375 -39.775 38.328  1.00 50.91 ? 10  ARG B NE  1 
ATOM   45   C  CZ  . ARG A 1 10  ? -50.663 -39.451 38.484  1.00 60.32 ? 10  ARG B CZ  1 
ATOM   46   N  NH1 . ARG A 1 10  ? -51.425 -39.105 37.428  1.00 55.75 ? 10  ARG B NH1 1 
ATOM   47   N  NH2 . ARG A 1 10  ? -51.198 -39.492 39.714  1.00 58.99 ? 10  ARG B NH2 1 
ATOM   48   N  N   . GLU A 1 11  ? -46.461 -44.662 38.520  1.00 33.40 ? 11  GLU B N   1 
ATOM   49   C  CA  . GLU A 1 11  ? -46.307 -46.105 38.766  1.00 31.28 ? 11  GLU B CA  1 
ATOM   50   C  C   . GLU A 1 11  ? -46.827 -46.947 37.596  1.00 31.92 ? 11  GLU B C   1 
ATOM   51   O  O   . GLU A 1 11  ? -46.223 -47.958 37.180  1.00 36.18 ? 11  GLU B O   1 
ATOM   52   C  CB  . GLU A 1 11  ? -47.044 -46.454 40.100  1.00 38.87 ? 11  GLU B CB  1 
ATOM   53   C  CG  . GLU A 1 11  ? -47.730 -47.815 40.222  1.00 53.02 ? 11  GLU B CG  1 
ATOM   54   C  CD  . GLU A 1 11  ? -46.810 -49.009 39.969  1.00 62.24 ? 11  GLU B CD  1 
ATOM   55   O  OE1 . GLU A 1 11  ? -45.564 -48.853 40.099  1.00 65.83 ? 11  GLU B OE1 1 
ATOM   56   O  OE2 . GLU A 1 11  ? -47.336 -50.107 39.609  1.00 69.23 ? 11  GLU B OE2 1 
ATOM   57   N  N   . HIS A 1 12  ? -47.924 -46.477 37.057  1.00 32.93 ? 12  HIS B N   1 
ATOM   58   C  CA  . HIS A 1 12  ? -48.707 -47.268 36.117  1.00 39.26 ? 12  HIS B CA  1 
ATOM   59   C  C   . HIS A 1 12  ? -48.327 -47.105 34.678  1.00 34.50 ? 12  HIS B C   1 
ATOM   60   O  O   . HIS A 1 12  ? -48.602 -47.983 33.838  1.00 32.39 ? 12  HIS B O   1 
ATOM   61   C  CB  . HIS A 1 12  ? -50.212 -47.158 36.410  1.00 44.05 ? 12  HIS B CB  1 
ATOM   62   C  CG  . HIS A 1 12  ? -50.619 -48.073 37.540  1.00 58.32 ? 12  HIS B CG  1 
ATOM   63   N  ND1 . HIS A 1 12  ? -50.912 -47.619 38.784  1.00 58.09 ? 12  HIS B ND1 1 
ATOM   64   C  CD2 . HIS A 1 12  ? -50.631 -49.477 37.617  1.00 60.51 ? 12  HIS B CD2 1 
ATOM   65   C  CE1 . HIS A 1 12  ? -51.150 -48.673 39.594  1.00 62.27 ? 12  HIS B CE1 1 
ATOM   66   N  NE2 . HIS A 1 12  ? -50.981 -49.806 38.877  1.00 63.41 ? 12  HIS B NE2 1 
ATOM   67   N  N   . ASN A 1 13  ? -47.569 -46.050 34.413  1.00 27.57 ? 13  ASN B N   1 
ATOM   68   C  CA  . ASN A 1 13  ? -47.361 -45.632 32.987  1.00 25.06 ? 13  ASN B CA  1 
ATOM   69   C  C   . ASN A 1 13  ? -45.868 -45.307 32.740  1.00 23.17 ? 13  ASN B C   1 
ATOM   70   O  O   . ASN A 1 13  ? -45.523 -44.818 31.661  1.00 20.57 ? 13  ASN B O   1 
ATOM   71   C  CB  . ASN A 1 13  ? -48.293 -44.485 32.608  1.00 21.80 ? 13  ASN B CB  1 
ATOM   72   C  CG  . ASN A 1 13  ? -47.943 -43.144 33.239  1.00 20.90 ? 13  ASN B CG  1 
ATOM   73   O  OD1 . ASN A 1 13  ? -47.028 -43.046 34.024  1.00 23.40 ? 13  ASN B OD1 1 
ATOM   74   N  ND2 . ASN A 1 13  ? -48.647 -42.109 32.841  1.00 21.03 ? 13  ASN B ND2 1 
ATOM   75   N  N   . GLY A 1 14  ? -45.053 -45.528 33.754  1.00 23.32 ? 14  GLY B N   1 
ATOM   76   C  CA  . GLY A 1 14  ? -43.628 -45.131 33.768  1.00 22.30 ? 14  GLY B CA  1 
ATOM   77   C  C   . GLY A 1 14  ? -42.745 -46.071 33.026  1.00 22.57 ? 14  GLY B C   1 
ATOM   78   O  O   . GLY A 1 14  ? -43.180 -47.042 32.381  1.00 23.56 ? 14  GLY B O   1 
ATOM   79   N  N   . PRO A 1 15  ? -41.431 -45.836 33.073  1.00 21.37 ? 15  PRO B N   1 
ATOM   80   C  CA  . PRO A 1 15  ? -40.442 -46.481 32.219  1.00 19.40 ? 15  PRO B CA  1 
ATOM   81   C  C   . PRO A 1 15  ? -40.485 -48.005 32.142  1.00 23.78 ? 15  PRO B C   1 
ATOM   82   O  O   . PRO A 1 15  ? -40.216 -48.558 31.061  1.00 23.81 ? 15  PRO B O   1 
ATOM   83   C  CB  . PRO A 1 15  ? -39.082 -46.012 32.816  1.00 17.86 ? 15  PRO B CB  1 
ATOM   84   C  CG  . PRO A 1 15  ? -39.457 -44.643 33.250  1.00 18.60 ? 15  PRO B CG  1 
ATOM   85   C  CD  . PRO A 1 15  ? -40.864 -44.636 33.767  1.00 21.03 ? 15  PRO B CD  1 
ATOM   86   N  N   . ILE A 1 16  ? -40.836 -48.666 33.269  1.00 24.30 ? 16  ILE B N   1 
ATOM   87   C  CA  . ILE A 1 16  ? -40.852 -50.152 33.308  1.00 26.74 ? 16  ILE B CA  1 
ATOM   88   C  C   . ILE A 1 16  ? -41.943 -50.708 32.391  1.00 25.75 ? 16  ILE B C   1 
ATOM   89   O  O   . ILE A 1 16  ? -41.811 -51.831 31.907  1.00 30.64 ? 16  ILE B O   1 
ATOM   90   C  CB  . ILE A 1 16  ? -40.992 -50.662 34.791  1.00 28.48 ? 16  ILE B CB  1 
ATOM   91   C  CG1 . ILE A 1 16  ? -40.476 -52.093 34.971  1.00 35.45 ? 16  ILE B CG1 1 
ATOM   92   C  CG2 . ILE A 1 16  ? -42.352 -50.301 35.345  1.00 27.77 ? 16  ILE B CG2 1 
ATOM   93   C  CD1 . ILE A 1 16  ? -38.945 -52.176 35.081  1.00 38.69 ? 16  ILE B CD1 1 
ATOM   94   N  N   . HIS A 1 17  ? -42.970 -49.923 32.113  1.00 26.89 ? 17  HIS B N   1 
ATOM   95   C  CA  . HIS A 1 17  ? -44.114 -50.337 31.317  1.00 26.72 ? 17  HIS B CA  1 
ATOM   96   C  C   . HIS A 1 17  ? -44.030 -49.840 29.893  1.00 24.64 ? 17  HIS B C   1 
ATOM   97   O  O   . HIS A 1 17  ? -45.004 -50.002 29.144  1.00 24.34 ? 17  HIS B O   1 
ATOM   98   C  CB  . HIS A 1 17  ? -45.382 -49.696 31.895  1.00 29.14 ? 17  HIS B CB  1 
ATOM   99   C  CG  . HIS A 1 17  ? -45.720 -50.157 33.281  1.00 40.36 ? 17  HIS B CG  1 
ATOM   100  N  ND1 . HIS A 1 17  ? -45.946 -51.465 33.588  1.00 40.07 ? 17  HIS B ND1 1 
ATOM   101  C  CD2 . HIS A 1 17  ? -45.846 -49.442 34.473  1.00 39.22 ? 17  HIS B CD2 1 
ATOM   102  C  CE1 . HIS A 1 17  ? -46.166 -51.568 34.919  1.00 40.35 ? 17  HIS B CE1 1 
ATOM   103  N  NE2 . HIS A 1 17  ? -46.138 -50.333 35.448  1.00 41.98 ? 17  HIS B NE2 1 
ATOM   104  N  N   . TRP A 1 18  ? -42.953 -49.090 29.503  1.00 18.92 ? 18  TRP B N   1 
ATOM   105  C  CA  . TRP A 1 18  ? -43.059 -48.496 28.180  1.00 18.81 ? 18  TRP B CA  1 
ATOM   106  C  C   . TRP A 1 18  ? -42.971 -49.575 27.082  1.00 19.52 ? 18  TRP B C   1 
ATOM   107  O  O   . TRP A 1 18  ? -43.579 -49.349 26.032  1.00 21.36 ? 18  TRP B O   1 
ATOM   108  C  CB  . TRP A 1 18  ? -41.886 -47.491 27.978  1.00 18.68 ? 18  TRP B CB  1 
ATOM   109  C  CG  . TRP A 1 18  ? -42.076 -46.262 28.748  1.00 16.32 ? 18  TRP B CG  1 
ATOM   110  C  CD1 . TRP A 1 18  ? -43.169 -45.842 29.512  1.00 18.07 ? 18  TRP B CD1 1 
ATOM   111  C  CD2 . TRP A 1 18  ? -41.020 -45.240 28.963  1.00 15.37 ? 18  TRP B CD2 1 
ATOM   112  N  NE1 . TRP A 1 18  ? -42.912 -44.597 30.103  1.00 16.77 ? 18  TRP B NE1 1 
ATOM   113  C  CE2 . TRP A 1 18  ? -41.645 -44.186 29.770  1.00 14.44 ? 18  TRP B CE2 1 
ATOM   114  C  CE3 . TRP A 1 18  ? -39.710 -45.048 28.446  1.00 14.06 ? 18  TRP B CE3 1 
ATOM   115  C  CZ2 . TRP A 1 18  ? -40.962 -43.027 30.147  1.00 13.21 ? 18  TRP B CZ2 1 
ATOM   116  C  CZ3 . TRP A 1 18  ? -39.024 -43.877 28.869  1.00 12.78 ? 18  TRP B CZ3 1 
ATOM   117  C  CH2 . TRP A 1 18  ? -39.653 -42.895 29.618  1.00 11.26 ? 18  TRP B CH2 1 
ATOM   118  N  N   . LYS A 1 19  ? -42.284 -50.671 27.383  1.00 22.18 ? 19  LYS B N   1 
ATOM   119  C  CA  . LYS A 1 19  ? -42.102 -51.815 26.411  1.00 25.00 ? 19  LYS B CA  1 
ATOM   120  C  C   . LYS A 1 19  ? -43.494 -52.335 25.998  1.00 25.63 ? 19  LYS B C   1 
ATOM   121  O  O   . LYS A 1 19  ? -43.660 -52.905 24.910  1.00 25.38 ? 19  LYS B O   1 
ATOM   122  C  CB  . LYS A 1 19  ? -41.258 -52.958 27.004  1.00 26.65 ? 19  LYS B CB  1 
ATOM   123  C  CG  . LYS A 1 19  ? -41.891 -53.558 28.293  1.00 26.60 ? 19  LYS B CG  1 
ATOM   124  C  CD  . LYS A 1 19  ? -41.169 -54.728 29.006  1.00 34.35 ? 19  LYS B CD  1 
ATOM   125  C  CE  . LYS A 1 19  ? -39.923 -54.404 29.860  1.00 36.69 ? 19  LYS B CE  1 
ATOM   126  N  NZ  . LYS A 1 19  ? -40.045 -53.403 31.000  1.00 38.02 ? 19  LYS B NZ  1 
ATOM   127  N  N   . GLU A 1 20  ? -44.494 -52.107 26.831  1.00 25.76 ? 20  GLU B N   1 
ATOM   128  C  CA  . GLU A 1 20  ? -45.863 -52.533 26.501  1.00 26.46 ? 20  GLU B CA  1 
ATOM   129  C  C   . GLU A 1 20  ? -46.482 -51.889 25.303  1.00 28.21 ? 20  GLU B C   1 
ATOM   130  O  O   . GLU A 1 20  ? -47.393 -52.473 24.622  1.00 29.12 ? 20  GLU B O   1 
ATOM   131  C  CB  . GLU A 1 20  ? -46.812 -52.299 27.691  1.00 27.52 ? 20  GLU B CB  1 
ATOM   132  C  CG  . GLU A 1 20  ? -46.486 -53.214 28.813  1.00 27.62 ? 20  GLU B CG  1 
ATOM   133  C  CD  . GLU A 1 20  ? -47.177 -52.798 30.111  1.00 29.69 ? 20  GLU B CD  1 
ATOM   134  O  OE1 . GLU A 1 20  ? -48.295 -52.195 30.029  1.00 31.74 ? 20  GLU B OE1 1 
ATOM   135  O  OE2 . GLU A 1 20  ? -46.539 -53.063 31.171  1.00 29.59 ? 20  GLU B OE2 1 
ATOM   136  N  N   . PHE A 1 21  ? -46.092 -50.659 25.038  1.00 28.09 ? 21  PHE B N   1 
ATOM   137  C  CA  . PHE A 1 21  ? -46.565 -49.965 23.876  1.00 28.86 ? 21  PHE B CA  1 
ATOM   138  C  C   . PHE A 1 21  ? -45.466 -49.648 22.856  1.00 26.79 ? 21  PHE B C   1 
ATOM   139  O  O   . PHE A 1 21  ? -45.764 -49.322 21.698  1.00 25.88 ? 21  PHE B O   1 
ATOM   140  C  CB  . PHE A 1 21  ? -47.315 -48.724 24.329  1.00 36.48 ? 21  PHE B CB  1 
ATOM   141  C  CG  . PHE A 1 21  ? -48.283 -49.007 25.452  1.00 45.89 ? 21  PHE B CG  1 
ATOM   142  C  CD1 . PHE A 1 21  ? -47.915 -48.783 26.806  1.00 48.66 ? 21  PHE B CD1 1 
ATOM   143  C  CD2 . PHE A 1 21  ? -49.562 -49.532 25.177  1.00 47.43 ? 21  PHE B CD2 1 
ATOM   144  C  CE1 . PHE A 1 21  ? -48.817 -49.065 27.840  1.00 52.69 ? 21  PHE B CE1 1 
ATOM   145  C  CE2 . PHE A 1 21  ? -50.461 -49.820 26.213  1.00 42.81 ? 21  PHE B CE2 1 
ATOM   146  C  CZ  . PHE A 1 21  ? -50.093 -49.578 27.537  1.00 48.70 ? 21  PHE B CZ  1 
ATOM   147  N  N   . PHE A 1 22  ? -44.217 -49.747 23.295  1.00 23.30 ? 22  PHE B N   1 
ATOM   148  C  CA  . PHE A 1 22  ? -43.060 -49.347 22.483  1.00 25.45 ? 22  PHE B CA  1 
ATOM   149  C  C   . PHE A 1 22  ? -42.066 -50.443 22.633  1.00 27.63 ? 22  PHE B C   1 
ATOM   150  O  O   . PHE A 1 22  ? -41.092 -50.424 23.458  1.00 24.61 ? 22  PHE B O   1 
ATOM   151  C  CB  . PHE A 1 22  ? -42.494 -47.982 22.957  1.00 23.47 ? 22  PHE B CB  1 
ATOM   152  C  CG  . PHE A 1 22  ? -43.511 -46.911 22.927  1.00 22.04 ? 22  PHE B CG  1 
ATOM   153  C  CD1 . PHE A 1 22  ? -43.822 -46.305 21.716  1.00 26.55 ? 22  PHE B CD1 1 
ATOM   154  C  CD2 . PHE A 1 22  ? -44.242 -46.573 24.060  1.00 24.08 ? 22  PHE B CD2 1 
ATOM   155  C  CE1 . PHE A 1 22  ? -44.801 -45.328 21.645  1.00 25.21 ? 22  PHE B CE1 1 
ATOM   156  C  CE2 . PHE A 1 22  ? -45.257 -45.598 23.994  1.00 22.51 ? 22  PHE B CE2 1 
ATOM   157  C  CZ  . PHE A 1 22  ? -45.563 -44.998 22.783  1.00 24.67 ? 22  PHE B CZ  1 
ATOM   158  N  N   . PRO A 1 23  ? -42.275 -51.485 21.841  1.00 30.67 ? 23  PRO B N   1 
ATOM   159  C  CA  . PRO A 1 23  ? -41.397 -52.636 21.971  1.00 31.14 ? 23  PRO B CA  1 
ATOM   160  C  C   . PRO A 1 23  ? -39.887 -52.343 21.817  1.00 28.84 ? 23  PRO B C   1 
ATOM   161  O  O   . PRO A 1 23  ? -39.081 -53.025 22.434  1.00 27.89 ? 23  PRO B O   1 
ATOM   162  C  CB  . PRO A 1 23  ? -41.918 -53.588 20.849  1.00 29.92 ? 23  PRO B CB  1 
ATOM   163  C  CG  . PRO A 1 23  ? -42.631 -52.692 19.857  1.00 32.63 ? 23  PRO B CG  1 
ATOM   164  C  CD  . PRO A 1 23  ? -43.188 -51.551 20.676  1.00 33.95 ? 23  PRO B CD  1 
ATOM   165  N  N   . ILE A 1 24  ? -39.507 -51.325 21.005  1.00 22.87 ? 24  ILE B N   1 
ATOM   166  C  CA  . ILE A 1 24  ? -38.063 -51.021 20.882  1.00 23.31 ? 24  ILE B CA  1 
ATOM   167  C  C   . ILE A 1 24  ? -37.456 -50.641 22.304  1.00 20.28 ? 24  ILE B C   1 
ATOM   168  O  O   . ILE A 1 24  ? -36.241 -50.542 22.448  1.00 20.75 ? 24  ILE B O   1 
ATOM   169  C  CB  . ILE A 1 24  ? -37.842 -49.926 19.822  1.00 19.33 ? 24  ILE B CB  1 
ATOM   170  C  CG1 . ILE A 1 24  ? -36.382 -49.905 19.313  1.00 20.36 ? 24  ILE B CG1 1 
ATOM   171  C  CG2 . ILE A 1 24  ? -38.229 -48.579 20.431  1.00 17.90 ? 24  ILE B CG2 1 
ATOM   172  C  CD1 . ILE A 1 24  ? -35.937 -51.236 18.646  1.00 22.06 ? 24  ILE B CD1 1 
ATOM   173  N  N   . ALA A 1 25  ? -38.303 -50.475 23.340  1.00 21.02 ? 25  ALA B N   1 
ATOM   174  C  CA  . ALA A 1 25  ? -37.765 -50.219 24.687  1.00 23.26 ? 25  ALA B CA  1 
ATOM   175  C  C   . ALA A 1 25  ? -36.712 -51.177 25.116  1.00 21.36 ? 25  ALA B C   1 
ATOM   176  O  O   . ALA A 1 25  ? -35.830 -50.835 25.844  1.00 20.43 ? 25  ALA B O   1 
ATOM   177  C  CB  . ALA A 1 25  ? -38.894 -50.186 25.741  1.00 22.59 ? 25  ALA B CB  1 
ATOM   178  N  N   . ASP A 1 26  ? -36.789 -52.460 24.696  1.00 20.75 ? 26  ASP B N   1 
ATOM   179  C  CA  . ASP A 1 26  ? -35.761 -53.428 24.997  1.00 21.41 ? 26  ASP B CA  1 
ATOM   180  C  C   . ASP A 1 26  ? -34.763 -53.715 23.887  1.00 23.47 ? 26  ASP B C   1 
ATOM   181  O  O   . ASP A 1 26  ? -34.140 -54.771 23.876  1.00 25.33 ? 26  ASP B O   1 
ATOM   182  C  CB  . ASP A 1 26  ? -36.473 -54.773 25.359  1.00 28.07 ? 26  ASP B CB  1 
ATOM   183  C  CG  . ASP A 1 26  ? -37.412 -54.632 26.551  1.00 31.53 ? 26  ASP B CG  1 
ATOM   184  O  OD1 . ASP A 1 26  ? -36.979 -54.164 27.623  1.00 37.72 ? 26  ASP B OD1 1 
ATOM   185  O  OD2 . ASP A 1 26  ? -38.586 -54.996 26.410  1.00 39.40 ? 26  ASP B OD2 1 
ATOM   186  N  N   . GLY A 1 27  ? -34.650 -52.784 22.917  1.00 21.84 ? 27  GLY B N   1 
ATOM   187  C  CA  . GLY A 1 27  ? -33.676 -52.797 21.834  1.00 19.24 ? 27  GLY B CA  1 
ATOM   188  C  C   . GLY A 1 27  ? -32.228 -52.837 22.196  1.00 20.01 ? 27  GLY B C   1 
ATOM   189  O  O   . GLY A 1 27  ? -31.843 -52.879 23.380  1.00 22.73 ? 27  GLY B O   1 
ATOM   190  N  N   . ASP A 1 28  ? -31.414 -52.810 21.161  1.00 21.53 ? 28  ASP B N   1 
ATOM   191  C  CA  . ASP A 1 28  ? -30.003 -52.939 21.306  1.00 20.80 ? 28  ASP B CA  1 
ATOM   192  C  C   . ASP A 1 28  ? -29.325 -51.615 21.304  1.00 17.65 ? 28  ASP B C   1 
ATOM   193  O  O   . ASP A 1 28  ? -28.181 -51.587 21.526  1.00 18.79 ? 28  ASP B O   1 
ATOM   194  C  CB  . ASP A 1 28  ? -29.471 -53.787 20.107  1.00 21.79 ? 28  ASP B CB  1 
ATOM   195  C  CG  . ASP A 1 28  ? -29.749 -55.309 20.315  1.00 25.80 ? 28  ASP B CG  1 
ATOM   196  O  OD1 . ASP A 1 28  ? -29.902 -55.738 21.476  1.00 30.20 ? 28  ASP B OD1 1 
ATOM   197  O  OD2 . ASP A 1 28  ? -29.718 -56.048 19.312  1.00 28.28 ? 28  ASP B OD2 1 
ATOM   198  N  N   . GLN A 1 29  ? -30.009 -50.494 20.979  1.00 15.41 ? 29  GLN B N   1 
ATOM   199  C  CA  . GLN A 1 29  ? -29.305 -49.238 20.978  1.00 14.98 ? 29  GLN B CA  1 
ATOM   200  C  C   . GLN A 1 29  ? -30.141 -48.236 21.750  1.00 14.28 ? 29  GLN B C   1 
ATOM   201  O  O   . GLN A 1 29  ? -30.415 -47.138 21.261  1.00 14.60 ? 29  GLN B O   1 
ATOM   202  C  CB  . GLN A 1 29  ? -29.013 -48.698 19.543  1.00 17.36 ? 29  GLN B CB  1 
ATOM   203  C  CG  . GLN A 1 29  ? -28.089 -49.674 18.820  1.00 23.10 ? 29  GLN B CG  1 
ATOM   204  C  CD  . GLN A 1 29  ? -27.161 -49.036 17.786  1.00 27.34 ? 29  GLN B CD  1 
ATOM   205  O  OE1 . GLN A 1 29  ? -26.066 -49.612 17.495  1.00 33.61 ? 29  GLN B OE1 1 
ATOM   206  N  NE2 . GLN A 1 29  ? -27.586 -47.901 17.183  1.00 18.96 ? 29  GLN B NE2 1 
ATOM   207  N  N   . GLN A 1 30  ? -30.472 -48.590 22.977  1.00 14.47 ? 30  GLN B N   1 
ATOM   208  C  CA  . GLN A 1 30  ? -31.363 -47.746 23.792  1.00 12.98 ? 30  GLN B CA  1 
ATOM   209  C  C   . GLN A 1 30  ? -30.542 -46.840 24.671  1.00 14.31 ? 30  GLN B C   1 
ATOM   210  O  O   . GLN A 1 30  ? -29.411 -47.126 25.010  1.00 14.79 ? 30  GLN B O   1 
ATOM   211  C  CB  . GLN A 1 30  ? -32.278 -48.639 24.662  1.00 14.04 ? 30  GLN B CB  1 
ATOM   212  C  CG  . GLN A 1 30  ? -33.374 -49.260 23.820  1.00 17.15 ? 30  GLN B CG  1 
ATOM   213  C  CD  . GLN A 1 30  ? -34.360 -48.180 23.348  1.00 15.48 ? 30  GLN B CD  1 
ATOM   214  O  OE1 . GLN A 1 30  ? -35.139 -47.625 24.104  1.00 13.26 ? 30  GLN B OE1 1 
ATOM   215  N  NE2 . GLN A 1 30  ? -34.366 -47.925 22.032  1.00 15.00 ? 30  GLN B NE2 1 
ATOM   216  N  N   . SER A 1 31  ? -31.145 -45.688 25.036  1.00 13.55 ? 31  SER B N   1 
ATOM   217  C  CA  . SER A 1 31  ? -30.528 -44.706 25.889  1.00 13.23 ? 31  SER B CA  1 
ATOM   218  C  C   . SER A 1 31  ? -31.480 -44.376 27.027  1.00 11.29 ? 31  SER B C   1 
ATOM   219  O  O   . SER A 1 31  ? -32.702 -44.613 26.946  1.00 11.85 ? 31  SER B O   1 
ATOM   220  C  CB  . SER A 1 31  ? -30.329 -43.385 25.031  1.00 11.41 ? 31  SER B CB  1 
ATOM   221  O  OG  . SER A 1 31  ? -29.292 -43.582 24.022  1.00 10.67 ? 31  SER B OG  1 
ATOM   222  N  N   . PRO A 1 32  ? -30.950 -43.801 28.116  1.00 12.40 ? 32  PRO B N   1 
ATOM   223  C  CA  . PRO A 1 32  ? -29.566 -43.492 28.319  1.00 12.17 ? 32  PRO B CA  1 
ATOM   224  C  C   . PRO A 1 32  ? -28.774 -44.734 28.775  1.00 14.13 ? 32  PRO B C   1 
ATOM   225  O  O   . PRO A 1 32  ? -29.317 -45.821 28.732  1.00 13.89 ? 32  PRO B O   1 
ATOM   226  C  CB  . PRO A 1 32  ? -29.624 -42.520 29.530  1.00 12.24 ? 32  PRO B CB  1 
ATOM   227  C  CG  . PRO A 1 32  ? -30.798 -43.021 30.315  1.00 11.46 ? 32  PRO B CG  1 
ATOM   228  C  CD  . PRO A 1 32  ? -31.843 -43.493 29.259  1.00 12.16 ? 32  PRO B CD  1 
ATOM   229  N  N   . ILE A 1 33  ? -27.493 -44.493 29.102  1.00 12.85 ? 33  ILE B N   1 
ATOM   230  C  CA  . ILE A 1 33  ? -26.592 -45.627 29.406  1.00 15.46 ? 33  ILE B CA  1 
ATOM   231  C  C   . ILE A 1 33  ? -25.766 -45.231 30.640  1.00 16.02 ? 33  ILE B C   1 
ATOM   232  O  O   . ILE A 1 33  ? -25.676 -44.062 31.070  1.00 14.75 ? 33  ILE B O   1 
ATOM   233  C  CB  . ILE A 1 33  ? -25.604 -45.985 28.236  1.00 15.65 ? 33  ILE B CB  1 
ATOM   234  C  CG1 . ILE A 1 33  ? -24.746 -44.801 27.864  1.00 14.71 ? 33  ILE B CG1 1 
ATOM   235  C  CG2 . ILE A 1 33  ? -26.383 -46.523 27.027  1.00 14.74 ? 33  ILE B CG2 1 
ATOM   236  C  CD1 . ILE A 1 33  ? -23.470 -45.091 27.111  1.00 15.37 ? 33  ILE B CD1 1 
ATOM   237  N  N   . GLU A 1 34  ? -25.040 -46.241 31.169  1.00 17.21 ? 34  GLU B N   1 
ATOM   238  C  CA  . GLU A 1 34  ? -23.889 -46.000 32.070  1.00 16.29 ? 34  GLU B CA  1 
ATOM   239  C  C   . GLU A 1 34  ? -22.602 -45.937 31.308  1.00 13.81 ? 34  GLU B C   1 
ATOM   240  O  O   . GLU A 1 34  ? -22.398 -46.730 30.426  1.00 17.14 ? 34  GLU B O   1 
ATOM   241  C  CB  . GLU A 1 34  ? -23.782 -47.228 33.022  1.00 16.74 ? 34  GLU B CB  1 
ATOM   242  C  CG  . GLU A 1 34  ? -24.911 -47.272 34.018  1.00 19.30 ? 34  GLU B CG  1 
ATOM   243  C  CD  . GLU A 1 34  ? -24.642 -48.340 35.108  1.00 24.52 ? 34  GLU B CD  1 
ATOM   244  O  OE1 . GLU A 1 34  ? -23.984 -47.981 36.109  1.00 24.00 ? 34  GLU B OE1 1 
ATOM   245  O  OE2 . GLU A 1 34  ? -25.055 -49.479 34.916  1.00 20.25 ? 34  GLU B OE2 1 
ATOM   246  N  N   . ILE A 1 35  ? -21.798 -44.913 31.561  1.00 15.86 ? 35  ILE B N   1 
ATOM   247  C  CA  . ILE A 1 35  ? -20.485 -44.768 30.943  1.00 17.47 ? 35  ILE B CA  1 
ATOM   248  C  C   . ILE A 1 35  ? -19.440 -45.217 32.014  1.00 17.49 ? 35  ILE B C   1 
ATOM   249  O  O   . ILE A 1 35  ? -19.317 -44.534 33.020  1.00 17.47 ? 35  ILE B O   1 
ATOM   250  C  CB  . ILE A 1 35  ? -20.259 -43.291 30.544  1.00 17.99 ? 35  ILE B CB  1 
ATOM   251  C  CG1 . ILE A 1 35  ? -21.464 -42.881 29.644  1.00 17.62 ? 35  ILE B CG1 1 
ATOM   252  C  CG2 . ILE A 1 35  ? -18.880 -43.042 29.931  1.00 20.21 ? 35  ILE B CG2 1 
ATOM   253  C  CD1 . ILE A 1 35  ? -21.389 -41.436 29.165  1.00 21.80 ? 35  ILE B CD1 1 
ATOM   254  N  N   . LYS A 1 36  ? -18.707 -46.269 31.618  1.00 19.51 ? 36  LYS B N   1 
ATOM   255  C  CA  . LYS A 1 36  ? -17.575 -46.858 32.415  1.00 20.37 ? 36  LYS B CA  1 
ATOM   256  C  C   . LYS A 1 36  ? -16.287 -46.240 31.806  1.00 19.22 ? 36  LYS B C   1 
ATOM   257  O  O   . LYS A 1 36  ? -15.821 -46.701 30.757  1.00 25.68 ? 36  LYS B O   1 
ATOM   258  C  CB  . LYS A 1 36  ? -17.601 -48.418 32.307  1.00 21.00 ? 36  LYS B CB  1 
ATOM   259  C  CG  . LYS A 1 36  ? -16.467 -49.089 33.109  1.00 24.61 ? 36  LYS B CG  1 
ATOM   260  C  CD  . LYS A 1 36  ? -16.758 -50.574 33.270  1.00 27.17 ? 36  LYS B CD  1 
ATOM   261  C  CE  . LYS A 1 36  ? -17.748 -50.894 34.403  1.00 27.86 ? 36  LYS B CE  1 
ATOM   262  N  NZ  . LYS A 1 36  ? -17.879 -52.419 34.613  1.00 22.53 ? 36  LYS B NZ  1 
ATOM   263  N  N   . THR A 1 37  ? -15.756 -45.197 32.431  1.00 20.58 ? 37  THR B N   1 
ATOM   264  C  CA  . THR A 1 37  ? -14.663 -44.442 31.793  1.00 23.43 ? 37  THR B CA  1 
ATOM   265  C  C   . THR A 1 37  ? -13.406 -45.317 31.524  1.00 25.75 ? 37  THR B C   1 
ATOM   266  O  O   . THR A 1 37  ? -12.731 -45.132 30.467  1.00 26.63 ? 37  THR B O   1 
ATOM   267  C  CB  . THR A 1 37  ? -14.347 -43.110 32.494  1.00 26.96 ? 37  THR B CB  1 
ATOM   268  O  OG1 . THR A 1 37  ? -13.895 -43.357 33.822  1.00 26.06 ? 37  THR B OG1 1 
ATOM   269  C  CG2 . THR A 1 37  ? -15.630 -42.237 32.612  1.00 24.87 ? 37  THR B CG2 1 
ATOM   270  N  N   . LYS A 1 38  ? -13.124 -46.279 32.403  1.00 28.86 ? 38  LYS B N   1 
ATOM   271  C  CA  . LYS A 1 38  ? -11.937 -47.141 32.208  1.00 31.88 ? 38  LYS B CA  1 
ATOM   272  C  C   . LYS A 1 38  ? -11.971 -47.949 30.898  1.00 34.71 ? 38  LYS B C   1 
ATOM   273  O  O   . LYS A 1 38  ? -10.944 -48.297 30.357  1.00 40.51 ? 38  LYS B O   1 
ATOM   274  C  CB  . LYS A 1 38  ? -11.635 -48.004 33.470  1.00 38.01 ? 38  LYS B CB  1 
ATOM   275  C  CG  . LYS A 1 38  ? -12.606 -49.128 33.742  1.00 42.40 ? 38  LYS B CG  1 
ATOM   276  C  CD  . LYS A 1 38  ? -11.993 -50.487 33.409  1.00 51.74 ? 38  LYS B CD  1 
ATOM   277  C  CE  . LYS A 1 38  ? -13.006 -51.618 33.588  1.00 58.13 ? 38  LYS B CE  1 
ATOM   278  N  NZ  . LYS A 1 38  ? -12.705 -52.751 32.660  1.00 56.86 ? 38  LYS B NZ  1 
ATOM   279  N  N   . GLU A 1 39  ? -13.168 -48.172 30.371  1.00 32.91 ? 39  GLU B N   1 
ATOM   280  C  CA  . GLU A 1 39  ? -13.357 -48.816 29.091  1.00 36.38 ? 39  GLU B CA  1 
ATOM   281  C  C   . GLU A 1 39  ? -13.607 -47.915 27.883  1.00 34.65 ? 39  GLU B C   1 
ATOM   282  O  O   . GLU A 1 39  ? -13.832 -48.419 26.796  1.00 42.22 ? 39  GLU B O   1 
ATOM   283  C  CB  . GLU A 1 39  ? -14.505 -49.815 29.215  1.00 39.55 ? 39  GLU B CB  1 
ATOM   284  C  CG  . GLU A 1 39  ? -14.047 -50.974 30.065  1.00 47.91 ? 39  GLU B CG  1 
ATOM   285  C  CD  . GLU A 1 39  ? -15.063 -52.073 30.144  1.00 57.07 ? 39  GLU B CD  1 
ATOM   286  O  OE1 . GLU A 1 39  ? -14.639 -53.225 30.409  1.00 64.60 ? 39  GLU B OE1 1 
ATOM   287  O  OE2 . GLU A 1 39  ? -16.261 -51.774 29.940  1.00 56.72 ? 39  GLU B OE2 1 
ATOM   288  N  N   . VAL A 1 40  ? -13.557 -46.601 28.058  1.00 29.23 ? 40  VAL B N   1 
ATOM   289  C  CA  . VAL A 1 40  ? -13.800 -45.681 26.941  1.00 28.90 ? 40  VAL B CA  1 
ATOM   290  C  C   . VAL A 1 40  ? -12.489 -45.423 26.196  1.00 28.77 ? 40  VAL B C   1 
ATOM   291  O  O   . VAL A 1 40  ? -11.456 -45.335 26.810  1.00 32.98 ? 40  VAL B O   1 
ATOM   292  C  CB  . VAL A 1 40  ? -14.390 -44.352 27.457  1.00 24.84 ? 40  VAL B CB  1 
ATOM   293  C  CG1 . VAL A 1 40  ? -14.384 -43.316 26.352  1.00 24.87 ? 40  VAL B CG1 1 
ATOM   294  C  CG2 . VAL A 1 40  ? -15.786 -44.607 28.005  1.00 24.01 ? 40  VAL B CG2 1 
ATOM   295  N  N   . LYS A 1 41  ? -12.519 -45.249 24.890  1.00 32.43 ? 41  LYS B N   1 
ATOM   296  C  CA  . LYS A 1 41  ? -11.248 -44.984 24.206  1.00 35.93 ? 41  LYS B CA  1 
ATOM   297  C  C   . LYS A 1 41  ? -11.292 -43.601 23.602  1.00 32.68 ? 41  LYS B C   1 
ATOM   298  O  O   . LYS A 1 41  ? -12.284 -43.278 22.964  1.00 30.29 ? 41  LYS B O   1 
ATOM   299  C  CB  . LYS A 1 41  ? -11.025 -46.049 23.118  1.00 40.18 ? 41  LYS B CB  1 
ATOM   300  C  CG  . LYS A 1 41  ? -10.258 -47.289 23.596  1.00 47.89 ? 41  LYS B CG  1 
ATOM   301  C  CD  . LYS A 1 41  ? -10.766 -48.611 23.011  1.00 58.19 ? 41  LYS B CD  1 
ATOM   302  C  CE  . LYS A 1 41  ? -11.192 -48.541 21.540  1.00 63.96 ? 41  LYS B CE  1 
ATOM   303  N  NZ  . LYS A 1 41  ? -10.073 -48.643 20.544  1.00 60.62 ? 41  LYS B NZ  1 
ATOM   304  N  N   . TYR A 1 42  ? -10.270 -42.785 23.858  1.00 27.83 ? 42  TYR B N   1 
ATOM   305  C  CA  . TYR A 1 42  ? -10.052 -41.559 23.094  1.00 29.27 ? 42  TYR B CA  1 
ATOM   306  C  C   . TYR A 1 42  ? -10.051 -41.864 21.575  1.00 33.51 ? 42  TYR B C   1 
ATOM   307  O  O   . TYR A 1 42  ? -9.477  -42.850 21.117  1.00 31.79 ? 42  TYR B O   1 
ATOM   308  C  CB  . TYR A 1 42  ? -8.744  -40.839 23.504  1.00 28.67 ? 42  TYR B CB  1 
ATOM   309  C  CG  . TYR A 1 42  ? -8.325  -39.678 22.586  1.00 34.44 ? 42  TYR B CG  1 
ATOM   310  C  CD1 . TYR A 1 42  ? -9.038  -38.476 22.574  1.00 31.81 ? 42  TYR B CD1 1 
ATOM   311  C  CD2 . TYR A 1 42  ? -7.203  -39.795 21.728  1.00 32.29 ? 42  TYR B CD2 1 
ATOM   312  C  CE1 . TYR A 1 42  ? -8.683  -37.403 21.721  1.00 33.41 ? 42  TYR B CE1 1 
ATOM   313  C  CE2 . TYR A 1 42  ? -6.830  -38.744 20.899  1.00 36.13 ? 42  TYR B CE2 1 
ATOM   314  C  CZ  . TYR A 1 42  ? -7.545  -37.555 20.885  1.00 34.19 ? 42  TYR B CZ  1 
ATOM   315  O  OH  . TYR A 1 42  ? -7.143  -36.540 20.032  1.00 40.80 ? 42  TYR B OH  1 
ATOM   316  N  N   . ASP A 1 43  ? -10.676 -40.982 20.797  1.00 31.13 ? 43  ASP B N   1 
ATOM   317  C  CA  . ASP A 1 43  ? -10.656 -41.082 19.346  1.00 26.97 ? 43  ASP B CA  1 
ATOM   318  C  C   . ASP A 1 43  ? -10.165 -39.774 18.712  1.00 31.14 ? 43  ASP B C   1 
ATOM   319  O  O   . ASP A 1 43  ? -10.890 -38.755 18.668  1.00 24.71 ? 43  ASP B O   1 
ATOM   320  C  CB  . ASP A 1 43  ? -12.066 -41.427 18.853  1.00 34.71 ? 43  ASP B CB  1 
ATOM   321  C  CG  . ASP A 1 43  ? -12.096 -41.674 17.366  1.00 36.62 ? 43  ASP B CG  1 
ATOM   322  O  OD1 . ASP A 1 43  ? -11.063 -41.358 16.734  1.00 34.33 ? 43  ASP B OD1 1 
ATOM   323  O  OD2 . ASP A 1 43  ? -13.149 -42.094 16.829  1.00 32.58 ? 43  ASP B OD2 1 
ATOM   324  N  N   . SER A 1 44  ? -8.908  -39.788 18.224  1.00 26.90 ? 44  SER B N   1 
ATOM   325  C  CA  . SER A 1 44  ? -8.322  -38.602 17.600  1.00 30.19 ? 44  SER B CA  1 
ATOM   326  C  C   . SER A 1 44  ? -8.989  -38.234 16.294  1.00 28.74 ? 44  SER B C   1 
ATOM   327  O  O   . SER A 1 44  ? -8.748  -37.120 15.802  1.00 31.74 ? 44  SER B O   1 
ATOM   328  C  CB  . SER A 1 44  ? -6.800  -38.783 17.408  1.00 34.50 ? 44  SER B CB  1 
ATOM   329  O  OG  . SER A 1 44  ? -6.607  -40.035 16.806  1.00 39.32 ? 44  SER B OG  1 
ATOM   330  N  N   . SER A 1 45  ? -9.822  -39.141 15.732  1.00 30.84 ? 45  SER B N   1 
ATOM   331  C  CA  . SER A 1 45  ? -10.562 -38.807 14.510  1.00 29.96 ? 45  SER B CA  1 
ATOM   332  C  C   . SER A 1 45  ? -11.836 -37.908 14.704  1.00 28.93 ? 45  SER B C   1 
ATOM   333  O  O   . SER A 1 45  ? -12.370 -37.311 13.715  1.00 33.39 ? 45  SER B O   1 
ATOM   334  C  CB  . SER A 1 45  ? -10.890 -40.064 13.689  1.00 34.06 ? 45  SER B CB  1 
ATOM   335  O  OG  . SER A 1 45  ? -11.949 -40.766 14.244  1.00 32.52 ? 45  SER B OG  1 
ATOM   336  N  N   . LEU A 1 46  ? -12.317 -37.756 15.926  1.00 29.72 ? 46  LEU B N   1 
ATOM   337  C  CA  . LEU A 1 46  ? -13.362 -36.740 16.165  1.00 27.37 ? 46  LEU B CA  1 
ATOM   338  C  C   . LEU A 1 46  ? -12.887 -35.311 15.877  1.00 28.26 ? 46  LEU B C   1 
ATOM   339  O  O   . LEU A 1 46  ? -11.813 -34.909 16.351  1.00 27.59 ? 46  LEU B O   1 
ATOM   340  C  CB  . LEU A 1 46  ? -13.798 -36.825 17.616  1.00 25.37 ? 46  LEU B CB  1 
ATOM   341  C  CG  . LEU A 1 46  ? -14.329 -38.202 17.961  1.00 25.60 ? 46  LEU B CG  1 
ATOM   342  C  CD1 . LEU A 1 46  ? -14.349 -38.362 19.466  1.00 22.32 ? 46  LEU B CD1 1 
ATOM   343  C  CD2 . LEU A 1 46  ? -15.762 -38.420 17.442  1.00 29.74 ? 46  LEU B CD2 1 
ATOM   344  N  N   . ARG A 1 47  ? -13.630 -34.555 15.060  1.00 27.46 ? 47  ARG B N   1 
ATOM   345  C  CA  . ARG A 1 47  ? -13.289 -33.185 14.767  1.00 25.74 ? 47  ARG B CA  1 
ATOM   346  C  C   . ARG A 1 47  ? -13.705 -32.208 15.858  1.00 27.55 ? 47  ARG B C   1 
ATOM   347  O  O   . ARG A 1 47  ? -14.454 -32.558 16.807  1.00 26.35 ? 47  ARG B O   1 
ATOM   348  C  CB  . ARG A 1 47  ? -13.849 -32.767 13.368  1.00 36.96 ? 47  ARG B CB  1 
ATOM   349  C  CG  . ARG A 1 47  ? -13.619 -33.833 12.280  1.00 45.50 ? 47  ARG B CG  1 
ATOM   350  C  CD  . ARG A 1 47  ? -13.526 -33.245 10.875  1.00 62.31 ? 47  ARG B CD  1 
ATOM   351  N  NE  . ARG A 1 47  ? -12.738 -34.067 9.915   1.00 73.96 ? 47  ARG B NE  1 
ATOM   352  C  CZ  . ARG A 1 47  ? -13.209 -34.601 8.774   1.00 72.14 ? 47  ARG B CZ  1 
ATOM   353  N  NH1 . ARG A 1 47  ? -14.479 -34.430 8.410   1.00 68.14 ? 47  ARG B NH1 1 
ATOM   354  N  NH2 . ARG A 1 47  ? -12.411 -35.304 7.977   1.00 66.78 ? 47  ARG B NH2 1 
ATOM   355  N  N   . PRO A 1 48  ? -13.146 -30.989 15.838  1.00 21.38 ? 48  PRO B N   1 
ATOM   356  C  CA  . PRO A 1 48  ? -13.619 -30.066 16.844  1.00 24.61 ? 48  PRO B CA  1 
ATOM   357  C  C   . PRO A 1 48  ? -15.153 -29.952 16.788  1.00 23.07 ? 48  PRO B C   1 
ATOM   358  O  O   . PRO A 1 48  ? -15.707 -29.845 15.688  1.00 24.53 ? 48  PRO B O   1 
ATOM   359  C  CB  . PRO A 1 48  ? -12.943 -28.713 16.436  1.00 24.77 ? 48  PRO B CB  1 
ATOM   360  C  CG  . PRO A 1 48  ? -11.708 -29.196 15.717  1.00 23.22 ? 48  PRO B CG  1 
ATOM   361  C  CD  . PRO A 1 48  ? -12.102 -30.407 14.950  1.00 24.10 ? 48  PRO B CD  1 
ATOM   362  N  N   . LEU A 1 49  ? -15.765 -29.882 17.966  1.00 23.25 ? 49  LEU B N   1 
ATOM   363  C  CA  . LEU A 1 49  ? -17.232 -29.578 18.045  1.00 23.37 ? 49  LEU B CA  1 
ATOM   364  C  C   . LEU A 1 49  ? -17.486 -28.150 17.756  1.00 24.45 ? 49  LEU B C   1 
ATOM   365  O  O   . LEU A 1 49  ? -16.725 -27.300 18.219  1.00 26.22 ? 49  LEU B O   1 
ATOM   366  C  CB  . LEU A 1 49  ? -17.654 -29.880 19.458  1.00 24.85 ? 49  LEU B CB  1 
ATOM   367  C  CG  . LEU A 1 49  ? -19.033 -30.251 19.839  1.00 28.44 ? 49  LEU B CG  1 
ATOM   368  C  CD1 . LEU A 1 49  ? -19.315 -31.582 19.197  1.00 27.76 ? 49  LEU B CD1 1 
ATOM   369  C  CD2 . LEU A 1 49  ? -19.056 -30.469 21.344  1.00 32.06 ? 49  LEU B CD2 1 
ATOM   370  N  N   . SER A 1 50  ? -18.491 -27.832 16.900  1.00 20.47 ? 50  SER B N   1 
ATOM   371  C  CA  . SER A 1 50  ? -18.687 -26.496 16.508  1.00 18.36 ? 50  SER B CA  1 
ATOM   372  C  C   . SER A 1 50  ? -20.131 -26.153 16.933  1.00 16.13 ? 50  SER B C   1 
ATOM   373  O  O   . SER A 1 50  ? -21.026 -26.826 16.478  1.00 18.09 ? 50  SER B O   1 
ATOM   374  C  CB  . SER A 1 50  ? -18.575 -26.418 14.971  1.00 21.34 ? 50  SER B CB  1 
ATOM   375  O  OG  . SER A 1 50  ? -19.255 -25.285 14.416  1.00 23.55 ? 50  SER B OG  1 
ATOM   376  N  N   . ILE A 1 51  ? -20.331 -25.134 17.792  1.00 15.93 ? 51  ILE B N   1 
ATOM   377  C  CA  . ILE A 1 51  ? -21.662 -24.782 18.158  1.00 14.56 ? 51  ILE B CA  1 
ATOM   378  C  C   . ILE A 1 51  ? -21.944 -23.341 17.780  1.00 17.00 ? 51  ILE B C   1 
ATOM   379  O  O   . ILE A 1 51  ? -21.364 -22.402 18.339  1.00 18.35 ? 51  ILE B O   1 
ATOM   380  C  CB  . ILE A 1 51  ? -21.822 -24.973 19.641  1.00 15.31 ? 51  ILE B CB  1 
ATOM   381  C  CG1 . ILE A 1 51  ? -21.477 -26.385 19.990  1.00 15.65 ? 51  ILE B CG1 1 
ATOM   382  C  CG2 . ILE A 1 51  ? -23.257 -24.615 19.999  1.00 16.24 ? 51  ILE B CG2 1 
ATOM   383  C  CD1 . ILE A 1 51  ? -21.645 -26.727 21.526  1.00 16.16 ? 51  ILE B CD1 1 
ATOM   384  N  N   . LYS A 1 52  ? -22.830 -23.167 16.797  1.00 13.75 ? 52  LYS B N   1 
ATOM   385  C  CA  . LYS A 1 52  ? -23.249 -21.851 16.416  1.00 13.55 ? 52  LYS B CA  1 
ATOM   386  C  C   . LYS A 1 52  ? -24.688 -21.672 16.801  1.00 15.01 ? 52  LYS B C   1 
ATOM   387  O  O   . LYS A 1 52  ? -25.534 -22.357 16.266  1.00 16.12 ? 52  LYS B O   1 
ATOM   388  C  CB  . LYS A 1 52  ? -23.078 -21.607 14.868  1.00 14.07 ? 52  LYS B CB  1 
ATOM   389  C  CG  . LYS A 1 52  ? -23.560 -20.238 14.412  1.00 15.81 ? 52  LYS B CG  1 
ATOM   390  C  CD  . LYS A 1 52  ? -23.282 -19.939 12.925  1.00 17.53 ? 52  LYS B CD  1 
ATOM   391  C  CE  . LYS A 1 52  ? -24.021 -20.770 11.927  1.00 20.84 ? 52  LYS B CE  1 
ATOM   392  N  NZ  . LYS A 1 52  ? -23.663 -20.135 10.619  1.00 26.26 ? 52  LYS B NZ  1 
ATOM   393  N  N   A TYR A 1 53  ? -24.980 -20.847 17.822  0.50 15.86 ? 53  TYR B N   1 
ATOM   394  N  N   B TYR A 1 53  ? -24.910 -20.637 17.635  0.50 15.47 ? 53  TYR B N   1 
ATOM   395  C  CA  A TYR A 1 53  ? -26.383 -20.651 18.260  0.50 14.72 ? 53  TYR B CA  1 
ATOM   396  C  CA  B TYR A 1 53  ? -26.197 -20.453 18.281  0.50 14.48 ? 53  TYR B CA  1 
ATOM   397  C  C   A TYR A 1 53  ? -26.789 -19.195 18.332  0.50 14.45 ? 53  TYR B C   1 
ATOM   398  C  C   B TYR A 1 53  ? -26.692 -19.039 18.203  0.50 15.15 ? 53  TYR B C   1 
ATOM   399  O  O   A TYR A 1 53  ? -26.064 -18.355 18.833  0.50 14.61 ? 53  TYR B O   1 
ATOM   400  O  O   B TYR A 1 53  ? -25.923 -18.077 18.418  0.50 14.23 ? 53  TYR B O   1 
ATOM   401  C  CB  A TYR A 1 53  ? -26.668 -21.272 19.672  0.50 12.94 ? 53  TYR B CB  1 
ATOM   402  C  CB  B TYR A 1 53  ? -26.172 -20.951 19.778  0.50 13.08 ? 53  TYR B CB  1 
ATOM   403  C  CG  A TYR A 1 53  ? -26.567 -22.776 19.851  0.50 13.11 ? 53  TYR B CG  1 
ATOM   404  C  CG  B TYR A 1 53  ? -27.495 -20.634 20.419  0.50 12.66 ? 53  TYR B CG  1 
ATOM   405  C  CD1 A TYR A 1 53  ? -26.869 -23.710 18.769  0.50 12.48 ? 53  TYR B CD1 1 
ATOM   406  C  CD1 B TYR A 1 53  ? -28.642 -21.300 20.006  0.50 12.38 ? 53  TYR B CD1 1 
ATOM   407  C  CD2 A TYR A 1 53  ? -26.322 -23.312 21.151  0.50 12.11 ? 53  TYR B CD2 1 
ATOM   408  C  CD2 B TYR A 1 53  ? -27.630 -19.634 21.371  0.50 12.04 ? 53  TYR B CD2 1 
ATOM   409  C  CE1 A TYR A 1 53  ? -26.759 -25.060 18.975  0.50 13.49 ? 53  TYR B CE1 1 
ATOM   410  C  CE1 B TYR A 1 53  ? -29.899 -21.004 20.515  0.50 13.20 ? 53  TYR B CE1 1 
ATOM   411  C  CE2 A TYR A 1 53  ? -26.266 -24.708 21.332  0.50 12.02 ? 53  TYR B CE2 1 
ATOM   412  C  CE2 B TYR A 1 53  ? -28.848 -19.338 21.906  0.50 11.11 ? 53  TYR B CE2 1 
ATOM   413  C  CZ  A TYR A 1 53  ? -26.530 -25.551 20.283  0.50 12.31 ? 53  TYR B CZ  1 
ATOM   414  C  CZ  B TYR A 1 53  ? -29.995 -20.021 21.452  0.50 10.48 ? 53  TYR B CZ  1 
ATOM   415  O  OH  A TYR A 1 53  ? -26.414 -26.858 20.526  0.50 11.65 ? 53  TYR B OH  1 
ATOM   416  O  OH  B TYR A 1 53  ? -31.188 -19.665 22.024  0.50 15.17 ? 53  TYR B OH  1 
ATOM   417  N  N   . ASP A 1 54  ? -27.939 -18.902 17.728  1.00 14.50 ? 54  ASP B N   1 
ATOM   418  C  CA  . ASP A 1 54  ? -28.541 -17.585 17.681  1.00 13.96 ? 54  ASP B CA  1 
ATOM   419  C  C   . ASP A 1 54  ? -29.670 -17.532 18.668  1.00 14.38 ? 54  ASP B C   1 
ATOM   420  O  O   . ASP A 1 54  ? -30.703 -18.263 18.519  1.00 14.33 ? 54  ASP B O   1 
ATOM   421  C  CB  . ASP A 1 54  ? -29.051 -17.447 16.219  1.00 17.97 ? 54  ASP B CB  1 
ATOM   422  C  CG  . ASP A 1 54  ? -29.473 -16.032 15.895  1.00 19.49 ? 54  ASP B CG  1 
ATOM   423  O  OD1 . ASP A 1 54  ? -30.070 -15.360 16.758  1.00 18.26 ? 54  ASP B OD1 1 
ATOM   424  O  OD2 . ASP A 1 54  ? -29.343 -15.660 14.715  1.00 24.73 ? 54  ASP B OD2 1 
ATOM   425  N  N   . PRO A 1 55  ? -29.610 -16.625 19.647  1.00 15.37 ? 55  PRO B N   1 
ATOM   426  C  CA  . PRO A 1 55  ? -30.658 -16.468 20.592  1.00 15.61 ? 55  PRO B CA  1 
ATOM   427  C  C   . PRO A 1 55  ? -32.030 -16.186 19.952  1.00 15.80 ? 55  PRO B C   1 
ATOM   428  O  O   . PRO A 1 55  ? -33.051 -16.479 20.546  1.00 17.96 ? 55  PRO B O   1 
ATOM   429  C  CB  . PRO A 1 55  ? -30.176 -15.261 21.445  1.00 15.66 ? 55  PRO B CB  1 
ATOM   430  C  CG  . PRO A 1 55  ? -28.679 -15.342 21.375  1.00 14.73 ? 55  PRO B CG  1 
ATOM   431  C  CD  . PRO A 1 55  ? -28.464 -15.697 19.942  1.00 15.60 ? 55  PRO B CD  1 
ATOM   432  N  N   . SER A 1 56  ? -32.075 -15.567 18.779  1.00 16.12 ? 56  SER B N   1 
ATOM   433  C  CA  . SER A 1 56  ? -33.344 -15.236 18.171  1.00 17.47 ? 56  SER B CA  1 
ATOM   434  C  C   . SER A 1 56  ? -34.021 -16.473 17.549  1.00 19.09 ? 56  SER B C   1 
ATOM   435  O  O   . SER A 1 56  ? -35.215 -16.403 17.164  1.00 21.35 ? 56  SER B O   1 
ATOM   436  C  CB  . SER A 1 56  ? -33.126 -14.104 17.105  1.00 17.79 ? 56  SER B CB  1 
ATOM   437  O  OG  . SER A 1 56  ? -32.566 -14.633 15.900  1.00 19.95 ? 56  SER B OG  1 
ATOM   438  N  N   . SER A 1 57  ? -33.342 -17.640 17.524  1.00 14.53 ? 57  SER B N   1 
ATOM   439  C  CA  . SER A 1 57  ? -33.910 -18.841 16.971  1.00 14.06 ? 57  SER B CA  1 
ATOM   440  C  C   . SER A 1 57  ? -34.948 -19.419 17.919  1.00 15.54 ? 57  SER B C   1 
ATOM   441  O  O   . SER A 1 57  ? -35.820 -20.213 17.494  1.00 13.99 ? 57  SER B O   1 
ATOM   442  C  CB  . SER A 1 57  ? -32.812 -19.887 16.758  1.00 16.16 ? 57  SER B CB  1 
ATOM   443  O  OG  . SER A 1 57  ? -31.888 -19.498 15.729  1.00 24.47 ? 57  SER B OG  1 
ATOM   444  N  N   . ALA A 1 58  ? -34.821 -19.139 19.207  1.00 14.82 ? 58  ALA B N   1 
ATOM   445  C  CA  . ALA A 1 58  ? -35.818 -19.643 20.200  1.00 15.79 ? 58  ALA B CA  1 
ATOM   446  C  C   . ALA A 1 58  ? -37.160 -18.980 19.924  1.00 16.86 ? 58  ALA B C   1 
ATOM   447  O  O   . ALA A 1 58  ? -37.216 -17.774 19.699  1.00 18.79 ? 58  ALA B O   1 
ATOM   448  C  CB  . ALA A 1 58  ? -35.361 -19.338 21.646  1.00 15.65 ? 58  ALA B CB  1 
ATOM   449  N  N   . LYS A 1 59  ? -38.203 -19.768 19.929  1.00 14.35 ? 59  LYS B N   1 
ATOM   450  C  CA  . LYS A 1 59  ? -39.575 -19.228 19.717  1.00 17.26 ? 59  LYS B CA  1 
ATOM   451  C  C   . LYS A 1 59  ? -40.525 -19.330 20.889  1.00 15.65 ? 59  LYS B C   1 
ATOM   452  O  O   . LYS A 1 59  ? -41.230 -18.371 21.178  1.00 16.10 ? 59  LYS B O   1 
ATOM   453  C  CB  . LYS A 1 59  ? -40.160 -19.988 18.513  1.00 19.06 ? 59  LYS B CB  1 
ATOM   454  C  CG  . LYS A 1 59  ? -39.464 -19.658 17.190  1.00 24.57 ? 59  LYS B CG  1 
ATOM   455  C  CD  . LYS A 1 59  ? -39.087 -18.170 17.197  1.00 28.02 ? 59  LYS B CD  1 
ATOM   456  C  CE  . LYS A 1 59  ? -38.145 -17.802 16.046  1.00 38.77 ? 59  LYS B CE  1 
ATOM   457  N  NZ  . LYS A 1 59  ? -37.768 -16.371 16.021  1.00 37.63 ? 59  LYS B NZ  1 
ATOM   458  N  N   . ILE A 1 60  ? -40.720 -20.536 21.432  1.00 14.13 ? 60  ILE B N   1 
ATOM   459  C  CA  . ILE A 1 60  ? -41.779 -20.787 22.444  1.00 13.35 ? 60  ILE B CA  1 
ATOM   460  C  C   . ILE A 1 60  ? -41.199 -21.696 23.534  1.00 14.07 ? 60  ILE B C   1 
ATOM   461  O  O   . ILE A 1 60  ? -40.294 -22.470 23.259  1.00 14.65 ? 60  ILE B O   1 
ATOM   462  C  CB  . ILE A 1 60  ? -43.139 -21.406 21.947  1.00 15.89 ? 60  ILE B CB  1 
ATOM   463  C  CG1 . ILE A 1 60  ? -42.878 -22.595 21.133  1.00 19.21 ? 60  ILE B CG1 1 
ATOM   464  C  CG2 . ILE A 1 60  ? -43.784 -20.370 21.027  1.00 22.44 ? 60  ILE B CG2 1 
ATOM   465  C  CD1 . ILE A 1 60  ? -44.133 -23.441 20.931  1.00 21.31 ? 60  ILE B CD1 1 
ATOM   466  N  N   . ILE A 1 61  ? -41.757 -21.573 24.733  1.00 13.13 ? 61  ILE B N   1 
ATOM   467  C  CA  . ILE A 1 61  ? -41.545 -22.645 25.750  1.00 12.80 ? 61  ILE B CA  1 
ATOM   468  C  C   . ILE A 1 61  ? -42.911 -23.216 26.079  1.00 14.11 ? 61  ILE B C   1 
ATOM   469  O  O   . ILE A 1 61  ? -43.871 -22.445 26.161  1.00 14.44 ? 61  ILE B O   1 
ATOM   470  C  CB  . ILE A 1 61  ? -40.800 -22.092 26.993  1.00 15.20 ? 61  ILE B CB  1 
ATOM   471  C  CG1 . ILE A 1 61  ? -40.366 -23.247 27.930  1.00 14.37 ? 61  ILE B CG1 1 
ATOM   472  C  CG2 . ILE A 1 61  ? -41.575 -21.037 27.768  1.00 13.62 ? 61  ILE B CG2 1 
ATOM   473  C  CD1 . ILE A 1 61  ? -39.431 -22.779 29.041  1.00 15.53 ? 61  ILE B CD1 1 
ATOM   474  N  N   . SER A 1 62  ? -42.997 -24.531 26.290  1.00 13.57 ? 62  SER B N   1 
ATOM   475  C  CA  . SER A 1 62  ? -44.268 -25.153 26.570  1.00 13.55 ? 62  SER B CA  1 
ATOM   476  C  C   . SER A 1 62  ? -44.079 -26.290 27.549  1.00 15.28 ? 62  SER B C   1 
ATOM   477  O  O   . SER A 1 62  ? -42.939 -26.781 27.758  1.00 14.22 ? 62  SER B O   1 
ATOM   478  C  CB  . SER A 1 62  ? -44.928 -25.620 25.292  1.00 15.62 ? 62  SER B CB  1 
ATOM   479  O  OG  . SER A 1 62  ? -44.135 -26.673 24.756  1.00 19.99 ? 62  SER B OG  1 
ATOM   480  N  N   . ASN A 1 63  ? -45.193 -26.661 28.200  1.00 11.97 ? 63  ASN B N   1 
ATOM   481  C  CA  . ASN A 1 63  ? -45.201 -27.827 29.040  1.00 15.17 ? 63  ASN B CA  1 
ATOM   482  C  C   . ASN A 1 63  ? -45.821 -28.976 28.274  1.00 15.02 ? 63  ASN B C   1 
ATOM   483  O  O   . ASN A 1 63  ? -47.010 -28.991 27.969  1.00 15.48 ? 63  ASN B O   1 
ATOM   484  C  CB  . ASN A 1 63  ? -46.058 -27.510 30.313  1.00 15.17 ? 63  ASN B CB  1 
ATOM   485  C  CG  . ASN A 1 63  ? -46.175 -28.709 31.223  1.00 15.51 ? 63  ASN B CG  1 
ATOM   486  O  OD1 . ASN A 1 63  ? -45.813 -29.820 30.879  1.00 15.98 ? 63  ASN B OD1 1 
ATOM   487  N  ND2 . ASN A 1 63  ? -46.638 -28.468 32.460  1.00 15.21 ? 63  ASN B ND2 1 
ATOM   488  N  N   . SER A 1 64  ? -45.018 -29.943 27.899  1.00 14.70 ? 64  SER B N   1 
ATOM   489  C  CA  . SER A 1 64  ? -45.474 -31.094 27.110  1.00 14.91 ? 64  SER B CA  1 
ATOM   490  C  C   . SER A 1 64  ? -46.141 -32.152 27.961  1.00 15.66 ? 64  SER B C   1 
ATOM   491  O  O   . SER A 1 64  ? -46.663 -33.143 27.399  1.00 17.79 ? 64  SER B O   1 
ATOM   492  C  CB  . SER A 1 64  ? -44.227 -31.797 26.524  1.00 14.48 ? 64  SER B CB  1 
ATOM   493  O  OG  . SER A 1 64  ? -43.401 -32.416 27.603  1.00 14.23 ? 64  SER B OG  1 
ATOM   494  N  N   . GLY A 1 65  ? -46.107 -31.949 29.293  1.00 13.55 ? 65  GLY B N   1 
ATOM   495  C  CA  . GLY A 1 65  ? -46.562 -32.980 30.274  1.00 16.67 ? 65  GLY B CA  1 
ATOM   496  C  C   . GLY A 1 65  ? -45.443 -33.892 30.746  1.00 16.48 ? 65  GLY B C   1 
ATOM   497  O  O   . GLY A 1 65  ? -45.616 -34.600 31.720  1.00 16.89 ? 65  GLY B O   1 
ATOM   498  N  N   . HIS A 1 66  ? -44.296 -33.881 30.042  1.00 14.87 ? 66  HIS B N   1 
ATOM   499  C  CA  . HIS A 1 66  ? -43.170 -34.728 30.371  1.00 13.61 ? 66  HIS B CA  1 
ATOM   500  C  C   . HIS A 1 66  ? -41.927 -33.935 30.714  1.00 14.24 ? 66  HIS B C   1 
ATOM   501  O  O   . HIS A 1 66  ? -40.997 -34.560 31.171  1.00 13.84 ? 66  HIS B O   1 
ATOM   502  C  CB  . HIS A 1 66  ? -42.843 -35.647 29.140  1.00 15.93 ? 66  HIS B CB  1 
ATOM   503  C  CG  . HIS A 1 66  ? -44.038 -36.205 28.514  1.00 17.15 ? 66  HIS B CG  1 
ATOM   504  N  ND1 . HIS A 1 66  ? -44.846 -37.074 29.181  1.00 21.88 ? 66  HIS B ND1 1 
ATOM   505  C  CD2 . HIS A 1 66  ? -44.588 -36.019 27.242  1.00 20.81 ? 66  HIS B CD2 1 
ATOM   506  C  CE1 . HIS A 1 66  ? -45.890 -37.443 28.363  1.00 23.66 ? 66  HIS B CE1 1 
ATOM   507  N  NE2 . HIS A 1 66  ? -45.723 -36.806 27.178  1.00 20.56 ? 66  HIS B NE2 1 
ATOM   508  N  N   . SER A 1 67  ? -41.916 -32.628 30.392  1.00 11.42 ? 67  SER B N   1 
ATOM   509  C  CA  . SER A 1 67  ? -40.808 -31.676 30.718  1.00 12.19 ? 67  SER B CA  1 
ATOM   510  C  C   . SER A 1 67  ? -41.263 -30.304 30.223  1.00 12.32 ? 67  SER B C   1 
ATOM   511  O  O   . SER A 1 67  ? -42.429 -30.156 29.715  1.00 12.97 ? 67  SER B O   1 
ATOM   512  C  CB  . SER A 1 67  ? -39.420 -32.058 30.016  1.00 13.11 ? 67  SER B CB  1 
ATOM   513  O  OG  . SER A 1 67  ? -38.340 -31.227 30.469  1.00 13.23 ? 67  SER B OG  1 
ATOM   514  N  N   . PHE A 1 68  ? -40.408 -29.302 30.306  1.00 11.54 ? 68  PHE B N   1 
ATOM   515  C  CA  . PHE A 1 68  ? -40.656 -28.085 29.532  1.00 11.76 ? 68  PHE B CA  1 
ATOM   516  C  C   . PHE A 1 68  ? -39.907 -28.332 28.240  1.00 12.17 ? 68  PHE B C   1 
ATOM   517  O  O   . PHE A 1 68  ? -38.889 -29.042 28.196  1.00 14.03 ? 68  PHE B O   1 
ATOM   518  C  CB  . PHE A 1 68  ? -40.160 -26.795 30.219  1.00 12.40 ? 68  PHE B CB  1 
ATOM   519  C  CG  . PHE A 1 68  ? -38.675 -26.730 30.279  1.00 12.24 ? 68  PHE B CG  1 
ATOM   520  C  CD1 . PHE A 1 68  ? -38.010 -27.171 31.432  1.00 13.85 ? 68  PHE B CD1 1 
ATOM   521  C  CD2 . PHE A 1 68  ? -37.877 -26.318 29.210  1.00 12.65 ? 68  PHE B CD2 1 
ATOM   522  C  CE1 . PHE A 1 68  ? -36.586 -27.092 31.482  1.00 12.59 ? 68  PHE B CE1 1 
ATOM   523  C  CE2 . PHE A 1 68  ? -36.477 -26.254 29.263  1.00 13.64 ? 68  PHE B CE2 1 
ATOM   524  C  CZ  . PHE A 1 68  ? -35.787 -26.683 30.430  1.00 14.37 ? 68  PHE B CZ  1 
ATOM   525  N  N   . ASN A 1 69  ? -40.420 -27.726 27.132  1.00 12.99 ? 69  ASN B N   1 
ATOM   526  C  CA  . ASN A 1 69  ? -39.662 -27.816 25.861  1.00 12.47 ? 69  ASN B CA  1 
ATOM   527  C  C   . ASN A 1 69  ? -39.521 -26.424 25.339  1.00 12.16 ? 69  ASN B C   1 
ATOM   528  O  O   . ASN A 1 69  ? -40.529 -25.675 25.158  1.00 13.57 ? 69  ASN B O   1 
ATOM   529  C  CB  . ASN A 1 69  ? -40.541 -28.501 24.794  1.00 12.67 ? 69  ASN B CB  1 
ATOM   530  C  CG  . ASN A 1 69  ? -40.715 -29.973 24.972  1.00 17.30 ? 69  ASN B CG  1 
ATOM   531  O  OD1 . ASN A 1 69  ? -39.862 -30.621 25.675  1.00 21.36 ? 69  ASN B OD1 1 
ATOM   532  N  ND2 . ASN A 1 69  ? -41.802 -30.523 24.502  1.00 16.67 ? 69  ASN B ND2 1 
ATOM   533  N  N   . VAL A 1 70  ? -38.275 -26.011 25.052  1.00 12.55 ? 70  VAL B N   1 
ATOM   534  C  CA  . VAL A 1 70  ? -38.053 -24.703 24.321  1.00 12.19 ? 70  VAL B CA  1 
ATOM   535  C  C   . VAL A 1 70  ? -37.920 -25.098 22.871  1.00 10.24 ? 70  VAL B C   1 
ATOM   536  O  O   . VAL A 1 70  ? -37.083 -25.969 22.526  1.00 11.45 ? 70  VAL B O   1 
ATOM   537  C  CB  . VAL A 1 70  ? -36.727 -24.024 24.687  1.00 12.62 ? 70  VAL B CB  1 
ATOM   538  C  CG1 . VAL A 1 70  ? -36.624 -22.758 23.832  1.00 14.42 ? 70  VAL B CG1 1 
ATOM   539  C  CG2 . VAL A 1 70  ? -36.777 -23.658 26.171  1.00 15.54 ? 70  VAL B CG2 1 
ATOM   540  N  N   . ASP A 1 71  ? -38.829 -24.551 22.020  1.00 12.18 ? 71  ASP B N   1 
ATOM   541  C  CA  . ASP A 1 71  ? -38.742 -24.961 20.567  1.00 13.35 ? 71  ASP B CA  1 
ATOM   542  C  C   . ASP A 1 71  ? -38.124 -23.840 19.774  1.00 13.15 ? 71  ASP B C   1 
ATOM   543  O  O   . ASP A 1 71  ? -38.292 -22.647 20.127  1.00 14.86 ? 71  ASP B O   1 
ATOM   544  C  CB  . ASP A 1 71  ? -40.136 -25.207 19.994  1.00 15.17 ? 71  ASP B CB  1 
ATOM   545  C  CG  . ASP A 1 71  ? -40.726 -26.505 20.509  1.00 22.78 ? 71  ASP B CG  1 
ATOM   546  O  OD1 . ASP A 1 71  ? -39.979 -27.468 20.729  1.00 27.10 ? 71  ASP B OD1 1 
ATOM   547  O  OD2 . ASP A 1 71  ? -41.926 -26.551 20.814  1.00 23.53 ? 71  ASP B OD2 1 
ATOM   548  N  N   . PHE A 1 72  ? -37.336 -24.259 18.794  1.00 12.23 ? 72  PHE B N   1 
ATOM   549  C  CA  . PHE A 1 72  ? -36.602 -23.296 17.896  1.00 12.78 ? 72  PHE B CA  1 
ATOM   550  C  C   . PHE A 1 72  ? -37.084 -23.364 16.470  1.00 15.89 ? 72  PHE B C   1 
ATOM   551  O  O   . PHE A 1 72  ? -37.643 -24.324 16.029  1.00 16.79 ? 72  PHE B O   1 
ATOM   552  C  CB  . PHE A 1 72  ? -35.112 -23.682 17.931  1.00 13.67 ? 72  PHE B CB  1 
ATOM   553  C  CG  . PHE A 1 72  ? -34.520 -23.584 19.351  1.00 12.81 ? 72  PHE B CG  1 
ATOM   554  C  CD1 . PHE A 1 72  ? -34.705 -24.615 20.322  1.00 12.83 ? 72  PHE B CD1 1 
ATOM   555  C  CD2 . PHE A 1 72  ? -33.808 -22.416 19.752  1.00 14.92 ? 72  PHE B CD2 1 
ATOM   556  C  CE1 . PHE A 1 72  ? -34.119 -24.411 21.636  1.00 11.97 ? 72  PHE B CE1 1 
ATOM   557  C  CE2 . PHE A 1 72  ? -33.252 -22.263 21.028  1.00 14.38 ? 72  PHE B CE2 1 
ATOM   558  C  CZ  . PHE A 1 72  ? -33.435 -23.260 21.965  1.00 12.20 ? 72  PHE B CZ  1 
ATOM   559  N  N   A ASP A 1 73  ? -37.061 -22.146 15.898  0.50 16.01 ? 73  ASP B N   1 
ATOM   560  N  N   B ASP A 1 73  ? -36.838 -22.302 15.716  0.50 16.09 ? 73  ASP B N   1 
ATOM   561  C  CA  A ASP A 1 73  ? -37.271 -22.041 14.484  0.50 19.19 ? 73  ASP B CA  1 
ATOM   562  C  CA  B ASP A 1 73  ? -37.216 -22.273 14.302  0.50 15.72 ? 73  ASP B CA  1 
ATOM   563  C  C   A ASP A 1 73  ? -36.182 -22.877 13.839  0.50 19.64 ? 73  ASP B C   1 
ATOM   564  C  C   B ASP A 1 73  ? -37.023 -23.607 13.611  0.50 14.86 ? 73  ASP B C   1 
ATOM   565  O  O   A ASP A 1 73  ? -34.973 -22.590 14.051  0.50 20.89 ? 73  ASP B O   1 
ATOM   566  O  O   B ASP A 1 73  ? -37.914 -24.464 13.593  0.50 15.44 ? 73  ASP B O   1 
ATOM   567  C  CB  A ASP A 1 73  ? -37.186 -20.579 14.005  0.50 18.45 ? 73  ASP B CB  1 
ATOM   568  C  CB  B ASP A 1 73  ? -36.374 -21.203 13.609  0.50 19.64 ? 73  ASP B CB  1 
ATOM   569  C  CG  A ASP A 1 73  ? -37.450 -20.491 12.521  0.50 20.12 ? 73  ASP B CG  1 
ATOM   570  C  CG  B ASP A 1 73  ? -36.809 -20.945 12.186  0.50 24.68 ? 73  ASP B CG  1 
ATOM   571  O  OD1 A ASP A 1 73  ? -36.627 -21.108 11.788  0.50 22.96 ? 73  ASP B OD1 1 
ATOM   572  O  OD1 B ASP A 1 73  ? -36.795 -21.901 11.388  0.50 25.19 ? 73  ASP B OD1 1 
ATOM   573  O  OD2 A ASP A 1 73  ? -38.429 -19.843 12.096  0.50 25.12 ? 73  ASP B OD2 1 
ATOM   574  O  OD2 B ASP A 1 73  ? -37.163 -19.788 11.869  0.50 26.94 ? 73  ASP B OD2 1 
ATOM   575  N  N   A ASP A 1 74  ? -36.656 -23.826 13.020  0.50 22.32 ? 74  ASP B N   1 
ATOM   576  N  N   B ASP A 1 74  ? -35.841 -23.763 13.029  0.50 13.48 ? 74  ASP B N   1 
ATOM   577  C  CA  A ASP A 1 74  ? -36.074 -25.065 12.459  0.50 24.56 ? 74  ASP B CA  1 
ATOM   578  C  CA  B ASP A 1 74  ? -35.457 -25.002 12.373  0.50 18.33 ? 74  ASP B CA  1 
ATOM   579  C  C   A ASP A 1 74  ? -36.313 -25.224 10.888  0.50 23.94 ? 74  ASP B C   1 
ATOM   580  C  C   B ASP A 1 74  ? -35.833 -25.143 10.896  0.50 19.43 ? 74  ASP B C   1 
ATOM   581  O  O   A ASP A 1 74  ? -36.469 -26.338 10.291  0.50 18.90 ? 74  ASP B O   1 
ATOM   582  O  O   B ASP A 1 74  ? -35.665 -26.232 10.346  0.50 16.68 ? 74  ASP B O   1 
ATOM   583  C  CB  A ASP A 1 74  ? -36.671 -26.271 13.194  0.50 24.85 ? 74  ASP B CB  1 
ATOM   584  C  CB  B ASP A 1 74  ? -35.853 -26.244 13.194  0.50 19.20 ? 74  ASP B CB  1 
ATOM   585  C  CG  A ASP A 1 74  ? -38.154 -26.552 12.820  0.50 23.68 ? 74  ASP B CG  1 
ATOM   586  C  CG  B ASP A 1 74  ? -37.117 -26.885 12.703  0.50 18.29 ? 74  ASP B CG  1 
ATOM   587  O  OD1 A ASP A 1 74  ? -38.679 -26.143 11.765  0.50 24.06 ? 74  ASP B OD1 1 
ATOM   588  O  OD1 B ASP A 1 74  ? -37.705 -26.369 11.735  0.50 18.79 ? 74  ASP B OD1 1 
ATOM   589  O  OD2 A ASP A 1 74  ? -38.817 -27.264 13.572  0.50 24.86 ? 74  ASP B OD2 1 
ATOM   590  O  OD2 B ASP A 1 74  ? -37.517 -27.907 13.297  0.50 15.92 ? 74  ASP B OD2 1 
ATOM   591  N  N   . THR A 1 75  ? -36.281 -24.072 10.227  1.00 23.56 ? 75  THR B N   1 
ATOM   592  C  CA  . THR A 1 75  ? -36.122 -24.085 8.716   1.00 20.65 ? 75  THR B CA  1 
ATOM   593  C  C   . THR A 1 75  ? -34.928 -23.231 8.321   1.00 20.05 ? 75  THR B C   1 
ATOM   594  O  O   . THR A 1 75  ? -34.622 -23.081 7.111   1.00 19.51 ? 75  THR B O   1 
ATOM   595  C  CB  . THR A 1 75  ? -37.384 -23.867 7.800   1.00 22.30 ? 75  THR B CB  1 
ATOM   596  O  OG1 . THR A 1 75  ? -37.889 -22.598 8.122   1.00 24.91 ? 75  THR B OG1 1 
ATOM   597  C  CG2 . THR A 1 75  ? -38.407 -25.117 7.877   1.00 25.83 ? 75  THR B CG2 1 
ATOM   598  N  N   . GLU A 1 76  ? -34.174 -22.729 9.286   1.00 18.38 ? 76  GLU B N   1 
ATOM   599  C  CA  . GLU A 1 76  ? -33.026 -21.988 9.031   1.00 18.40 ? 76  GLU B CA  1 
ATOM   600  C  C   . GLU A 1 76  ? -31.768 -22.630 9.647   1.00 19.31 ? 76  GLU B C   1 
ATOM   601  O  O   . GLU A 1 76  ? -31.895 -23.391 10.625  1.00 16.81 ? 76  GLU B O   1 
ATOM   602  C  CB  . GLU A 1 76  ? -33.212 -20.619 9.742   1.00 24.09 ? 76  GLU B CB  1 
ATOM   603  C  CG  . GLU A 1 76  ? -34.005 -19.620 8.914   1.00 34.53 ? 76  GLU B CG  1 
ATOM   604  C  CD  . GLU A 1 76  ? -35.378 -19.320 9.447   1.00 42.23 ? 76  GLU B CD  1 
ATOM   605  O  OE1 . GLU A 1 76  ? -36.254 -20.247 9.277   1.00 48.10 ? 76  GLU B OE1 1 
ATOM   606  O  OE2 . GLU A 1 76  ? -35.607 -18.134 9.933   1.00 38.88 ? 76  GLU B OE2 1 
ATOM   607  N  N   . ASN A 1 77  ? -30.592 -22.344 9.093   1.00 16.68 ? 77  ASN B N   1 
ATOM   608  C  CA  . ASN A 1 77  ? -29.319 -22.803 9.659   1.00 17.46 ? 77  ASN B CA  1 
ATOM   609  C  C   . ASN A 1 77  ? -28.613 -21.738 10.523  1.00 15.41 ? 77  ASN B C   1 
ATOM   610  O  O   . ASN A 1 77  ? -27.393 -21.716 10.624  1.00 17.84 ? 77  ASN B O   1 
ATOM   611  C  CB  . ASN A 1 77  ? -28.361 -23.452 8.607   1.00 18.46 ? 77  ASN B CB  1 
ATOM   612  C  CG  . ASN A 1 77  ? -28.775 -24.871 8.216   1.00 17.77 ? 77  ASN B CG  1 
ATOM   613  O  OD1 . ASN A 1 77  ? -29.575 -25.490 8.916   1.00 16.40 ? 77  ASN B OD1 1 
ATOM   614  N  ND2 . ASN A 1 77  ? -28.243 -25.402 7.064   1.00 16.12 ? 77  ASN B ND2 1 
ATOM   615  N  N   . LYS A 1 78  ? -29.380 -20.934 11.251  1.00 15.68 ? 78  LYS B N   1 
ATOM   616  C  CA  . LYS A 1 78  ? -28.761 -19.915 12.142  1.00 14.41 ? 78  LYS B CA  1 
ATOM   617  C  C   . LYS A 1 78  ? -28.175 -20.600 13.434  1.00 16.77 ? 78  LYS B C   1 
ATOM   618  O  O   . LYS A 1 78  ? -27.208 -20.112 14.090  1.00 16.30 ? 78  LYS B O   1 
ATOM   619  C  CB  . LYS A 1 78  ? -29.803 -18.889 12.545  1.00 16.39 ? 78  LYS B CB  1 
ATOM   620  C  CG  . LYS A 1 78  ? -30.177 -17.954 11.359  1.00 19.11 ? 78  LYS B CG  1 
ATOM   621  C  CD  . LYS A 1 78  ? -31.102 -16.855 11.881  1.00 29.50 ? 78  LYS B CD  1 
ATOM   622  C  CE  . LYS A 1 78  ? -31.542 -15.943 10.704  1.00 35.28 ? 78  LYS B CE  1 
ATOM   623  N  NZ  . LYS A 1 78  ? -32.008 -14.589 11.144  1.00 42.47 ? 78  LYS B NZ  1 
ATOM   624  N  N   . SER A 1 79  ? -28.846 -21.683 13.824  1.00 14.24 ? 79  SER B N   1 
ATOM   625  C  CA  . SER A 1 79  ? -28.395 -22.420 15.068  1.00 13.19 ? 79  SER B CA  1 
ATOM   626  C  C   . SER A 1 79  ? -28.188 -23.855 14.664  1.00 12.74 ? 79  SER B C   1 
ATOM   627  O  O   . SER A 1 79  ? -29.170 -24.664 14.445  1.00 14.28 ? 79  SER B O   1 
ATOM   628  C  CB  . SER A 1 79  ? -29.467 -22.335 16.173  1.00 12.05 ? 79  SER B CB  1 
ATOM   629  O  OG  . SER A 1 79  ? -29.656 -20.986 16.601  1.00 13.30 ? 79  SER B OG  1 
ATOM   630  N  N   . VAL A 1 80  ? -26.938 -24.267 14.629  1.00 12.32 ? 80  VAL B N   1 
ATOM   631  C  CA  . VAL A 1 80  ? -26.530 -25.610 14.156  1.00 11.65 ? 80  VAL B CA  1 
ATOM   632  C  C   . VAL A 1 80  ? -25.363 -26.167 14.964  1.00 13.75 ? 80  VAL B C   1 
ATOM   633  O  O   . VAL A 1 80  ? -24.560 -25.416 15.540  1.00 14.28 ? 80  VAL B O   1 
ATOM   634  C  CB  . VAL A 1 80  ? -26.110 -25.581 12.682  1.00 13.39 ? 80  VAL B CB  1 
ATOM   635  C  CG1 . VAL A 1 80  ? -27.284 -25.185 11.777  1.00 14.80 ? 80  VAL B CG1 1 
ATOM   636  C  CG2 . VAL A 1 80  ? -24.972 -24.549 12.561  1.00 16.29 ? 80  VAL B CG2 1 
ATOM   637  N  N   . LEU A 1 81  ? -25.314 -27.490 15.004  1.00 13.16 ? 81  LEU B N   1 
ATOM   638  C  CA  . LEU A 1 81  ? -24.253 -28.265 15.662  1.00 12.32 ? 81  LEU B CA  1 
ATOM   639  C  C   . LEU A 1 81  ? -23.559 -29.040 14.577  1.00 14.19 ? 81  LEU B C   1 
ATOM   640  O  O   . LEU A 1 81  ? -24.130 -29.728 13.766  1.00 14.70 ? 81  LEU B O   1 
ATOM   641  C  CB  . LEU A 1 81  ? -24.864 -29.252 16.665  1.00 13.43 ? 81  LEU B CB  1 
ATOM   642  C  CG  . LEU A 1 81  ? -23.843 -30.154 17.368  1.00 13.91 ? 81  LEU B CG  1 
ATOM   643  C  CD1 . LEU A 1 81  ? -23.009 -29.313 18.342  1.00 14.91 ? 81  LEU B CD1 1 
ATOM   644  C  CD2 . LEU A 1 81  ? -24.728 -31.212 18.141  1.00 13.59 ? 81  LEU B CD2 1 
ATOM   645  N  N   . ARG A 1 82  ? -22.219 -28.806 14.546  1.00 16.63 ? 82  ARG B N   1 
ATOM   646  C  CA  . ARG A 1 82  ? -21.393 -29.509 13.553  1.00 15.27 ? 82  ARG B CA  1 
ATOM   647  C  C   . ARG A 1 82  ? -20.146 -30.055 14.211  1.00 17.86 ? 82  ARG B C   1 
ATOM   648  O  O   . ARG A 1 82  ? -19.877 -29.774 15.356  1.00 18.71 ? 82  ARG B O   1 
ATOM   649  C  CB  . ARG A 1 82  ? -20.980 -28.467 12.459  1.00 16.69 ? 82  ARG B CB  1 
ATOM   650  C  CG  . ARG A 1 82  ? -22.153 -28.060 11.566  1.00 17.53 ? 82  ARG B CG  1 
ATOM   651  C  CD  . ARG A 1 82  ? -21.801 -26.828 10.644  1.00 17.38 ? 82  ARG B CD  1 
ATOM   652  N  NE  . ARG A 1 82  ? -21.615 -25.612 11.436  1.00 18.71 ? 82  ARG B NE  1 
ATOM   653  C  CZ  . ARG A 1 82  ? -21.420 -24.376 10.956  1.00 20.12 ? 82  ARG B CZ  1 
ATOM   654  N  NH1 . ARG A 1 82  ? -21.298 -24.209 9.620   1.00 20.90 ? 82  ARG B NH1 1 
ATOM   655  N  NH2 . ARG A 1 82  ? -21.310 -23.370 11.830  1.00 20.37 ? 82  ARG B NH2 1 
ATOM   656  N  N   . GLY A 1 83  ? -19.414 -30.910 13.488  1.00 15.45 ? 83  GLY B N   1 
ATOM   657  C  CA  . GLY A 1 83  ? -18.139 -31.319 14.106  1.00 16.52 ? 83  GLY B CA  1 
ATOM   658  C  C   . GLY A 1 83  ? -18.296 -32.495 15.057  1.00 19.38 ? 83  GLY B C   1 
ATOM   659  O  O   . GLY A 1 83  ? -19.300 -33.234 15.044  1.00 19.94 ? 83  GLY B O   1 
ATOM   660  N  N   . GLY A 1 84  ? -17.340 -32.624 15.976  1.00 20.14 ? 84  GLY B N   1 
ATOM   661  C  CA  . GLY A 1 84  ? -17.402 -33.831 16.753  1.00 21.19 ? 84  GLY B CA  1 
ATOM   662  C  C   . GLY A 1 84  ? -17.485 -35.144 15.937  1.00 15.86 ? 84  GLY B C   1 
ATOM   663  O  O   . GLY A 1 84  ? -16.726 -35.384 14.974  1.00 22.11 ? 84  GLY B O   1 
ATOM   664  N  N   . PRO A 1 85  ? -18.464 -36.029 16.255  1.00 15.62 ? 85  PRO B N   1 
ATOM   665  C  CA  . PRO A 1 85  ? -18.704 -37.249 15.595  1.00 15.93 ? 85  PRO B CA  1 
ATOM   666  C  C   . PRO A 1 85  ? -19.662 -37.125 14.354  1.00 18.41 ? 85  PRO B C   1 
ATOM   667  O  O   . PRO A 1 85  ? -19.884 -38.139 13.633  1.00 18.29 ? 85  PRO B O   1 
ATOM   668  C  CB  . PRO A 1 85  ? -19.388 -38.090 16.688  1.00 19.07 ? 85  PRO B CB  1 
ATOM   669  C  CG  . PRO A 1 85  ? -20.227 -37.085 17.359  1.00 18.04 ? 85  PRO B CG  1 
ATOM   670  C  CD  . PRO A 1 85  ? -19.358 -35.871 17.451  1.00 16.10 ? 85  PRO B CD  1 
ATOM   671  N  N   . LEU A 1 86  ? -20.135 -35.911 14.096  1.00 17.05 ? 86  LEU B N   1 
ATOM   672  C  CA  . LEU A 1 86  ? -21.198 -35.725 13.105  1.00 16.03 ? 86  LEU B CA  1 
ATOM   673  C  C   . LEU A 1 86  ? -20.644 -35.477 11.697  1.00 19.86 ? 86  LEU B C   1 
ATOM   674  O  O   . LEU A 1 86  ? -19.666 -34.699 11.503  1.00 19.33 ? 86  LEU B O   1 
ATOM   675  C  CB  . LEU A 1 86  ? -22.017 -34.464 13.466  1.00 15.21 ? 86  LEU B CB  1 
ATOM   676  C  CG  . LEU A 1 86  ? -22.588 -34.626 14.899  1.00 14.52 ? 86  LEU B CG  1 
ATOM   677  C  CD1 . LEU A 1 86  ? -23.225 -33.277 15.395  1.00 16.09 ? 86  LEU B CD1 1 
ATOM   678  C  CD2 . LEU A 1 86  ? -23.582 -35.798 15.029  1.00 15.98 ? 86  LEU B CD2 1 
ATOM   679  N  N   . THR A 1 87  ? -21.362 -36.071 10.756  1.00 20.09 ? 87  THR B N   1 
ATOM   680  C  CA  . THR A 1 87  ? -21.221 -35.710 9.311   1.00 21.96 ? 87  THR B CA  1 
ATOM   681  C  C   . THR A 1 87  ? -22.296 -34.720 8.916   1.00 20.50 ? 87  THR B C   1 
ATOM   682  O  O   . THR A 1 87  ? -23.498 -35.039 9.028   1.00 21.20 ? 87  THR B O   1 
ATOM   683  C  CB  . THR A 1 87  ? -21.409 -36.979 8.466   1.00 20.42 ? 87  THR B CB  1 
ATOM   684  O  OG1 . THR A 1 87  ? -20.362 -37.898 8.872   1.00 27.28 ? 87  THR B OG1 1 
ATOM   685  C  CG2 . THR A 1 87  ? -21.227 -36.647 6.921   1.00 24.76 ? 87  THR B CG2 1 
ATOM   686  N  N   . GLY A 1 88  ? -21.911 -33.525 8.467   1.00 18.90 ? 88  GLY B N   1 
ATOM   687  C  CA  . GLY A 1 88  ? -22.919 -32.548 8.080   1.00 19.66 ? 88  GLY B CA  1 
ATOM   688  C  C   . GLY A 1 88  ? -23.473 -31.702 9.217   1.00 19.33 ? 88  GLY B C   1 
ATOM   689  O  O   . GLY A 1 88  ? -22.937 -31.697 10.342  1.00 20.68 ? 88  GLY B O   1 
ATOM   690  N  N   . SER A 1 89  ? -24.540 -30.982 8.914   1.00 15.37 ? 89  SER B N   1 
ATOM   691  C  CA  . SER A 1 89  ? -25.035 -29.906 9.779   1.00 16.60 ? 89  SER B CA  1 
ATOM   692  C  C   . SER A 1 89  ? -26.343 -30.414 10.423  1.00 16.77 ? 89  SER B C   1 
ATOM   693  O  O   . SER A 1 89  ? -27.278 -30.865 9.751   1.00 16.46 ? 89  SER B O   1 
ATOM   694  C  CB  . SER A 1 89  ? -25.371 -28.657 8.959   1.00 15.09 ? 89  SER B CB  1 
ATOM   695  O  OG  . SER A 1 89  ? -25.590 -27.566 9.842   1.00 16.38 ? 89  SER B OG  1 
ATOM   696  N  N   . TYR A 1 90  ? -26.363 -30.335 11.761  1.00 13.94 ? 90  TYR B N   1 
ATOM   697  C  CA  . TYR A 1 90  ? -27.579 -30.724 12.522  1.00 11.02 ? 90  TYR B CA  1 
ATOM   698  C  C   . TYR A 1 90  ? -28.192 -29.511 13.124  1.00 11.81 ? 90  TYR B C   1 
ATOM   699  O  O   . TYR A 1 90  ? -27.570 -28.757 13.878  1.00 13.81 ? 90  TYR B O   1 
ATOM   700  C  CB  . TYR A 1 90  ? -27.098 -31.740 13.618  1.00 11.86 ? 90  TYR B CB  1 
ATOM   701  C  CG  . TYR A 1 90  ? -26.862 -33.095 13.094  1.00 11.04 ? 90  TYR B CG  1 
ATOM   702  C  CD1 . TYR A 1 90  ? -25.722 -33.345 12.250  1.00 11.85 ? 90  TYR B CD1 1 
ATOM   703  C  CD2 . TYR A 1 90  ? -27.748 -34.181 13.338  1.00 11.53 ? 90  TYR B CD2 1 
ATOM   704  C  CE1 . TYR A 1 90  ? -25.546 -34.614 11.756  1.00 12.61 ? 90  TYR B CE1 1 
ATOM   705  C  CE2 . TYR A 1 90  ? -27.555 -35.469 12.864  1.00 12.27 ? 90  TYR B CE2 1 
ATOM   706  C  CZ  . TYR A 1 90  ? -26.394 -35.670 12.040  1.00 13.37 ? 90  TYR B CZ  1 
ATOM   707  O  OH  . TYR A 1 90  ? -26.212 -36.961 11.577  1.00 14.12 ? 90  TYR B OH  1 
ATOM   708  N  N   . ARG A 1 91  ? -29.442 -29.257 12.735  1.00 11.40 ? 91  ARG B N   1 
ATOM   709  C  CA  . ARG A 1 91  ? -30.191 -28.039 13.045  1.00 12.84 ? 91  ARG B CA  1 
ATOM   710  C  C   . ARG A 1 91  ? -30.771 -28.115 14.448  1.00 10.40 ? 91  ARG B C   1 
ATOM   711  O  O   . ARG A 1 91  ? -31.442 -29.120 14.786  1.00 11.60 ? 91  ARG B O   1 
ATOM   712  C  CB  . ARG A 1 91  ? -31.291 -27.848 11.967  1.00 14.17 ? 91  ARG B CB  1 
ATOM   713  C  CG  . ARG A 1 91  ? -31.936 -26.496 12.074  1.00 14.57 ? 91  ARG B CG  1 
ATOM   714  C  CD  . ARG A 1 91  ? -32.976 -26.194 10.990  1.00 16.60 ? 91  ARG B CD  1 
ATOM   715  N  NE  . ARG A 1 91  ? -32.266 -26.148 9.717   1.00 18.25 ? 91  ARG B NE  1 
ATOM   716  C  CZ  . ARG A 1 91  ? -32.758 -26.553 8.554   1.00 16.35 ? 91  ARG B CZ  1 
ATOM   717  N  NH1 . ARG A 1 91  ? -34.000 -27.007 8.466   1.00 14.88 ? 91  ARG B NH1 1 
ATOM   718  N  NH2 . ARG A 1 91  ? -32.007 -26.472 7.468   1.00 15.08 ? 91  ARG B NH2 1 
ATOM   719  N  N   . LEU A 1 92  ? -30.560 -27.106 15.238  1.00 10.18 ? 92  LEU B N   1 
ATOM   720  C  CA  . LEU A 1 92  ? -31.195 -27.085 16.620  1.00 10.56 ? 92  LEU B CA  1 
ATOM   721  C  C   . LEU A 1 92  ? -32.718 -27.129 16.550  1.00 12.98 ? 92  LEU B C   1 
ATOM   722  O  O   . LEU A 1 92  ? -33.329 -26.343 15.770  1.00 12.65 ? 92  LEU B O   1 
ATOM   723  C  CB  . LEU A 1 92  ? -30.726 -25.848 17.342  1.00 10.63 ? 92  LEU B CB  1 
ATOM   724  C  CG  . LEU A 1 92  ? -31.333 -25.487 18.678  1.00 11.79 ? 92  LEU B CG  1 
ATOM   725  C  CD1 . LEU A 1 92  ? -30.965 -26.702 19.619  1.00 11.98 ? 92  LEU B CD1 1 
ATOM   726  C  CD2 . LEU A 1 92  ? -30.843 -24.141 19.197  1.00 12.81 ? 92  LEU B CD2 1 
ATOM   727  N  N   . ARG A 1 93  ? -33.347 -28.057 17.287  1.00 11.32 ? 93  ARG B N   1 
ATOM   728  C  CA  . ARG A 1 93  ? -34.801 -28.198 17.327  1.00 11.20 ? 93  ARG B CA  1 
ATOM   729  C  C   . ARG A 1 93  ? -35.413 -27.825 18.653  1.00 12.45 ? 93  ARG B C   1 
ATOM   730  O  O   . ARG A 1 93  ? -36.400 -27.087 18.679  1.00 12.39 ? 93  ARG B O   1 
ATOM   731  C  CB  . ARG A 1 93  ? -35.115 -29.673 16.983  1.00 12.97 ? 93  ARG B CB  1 
ATOM   732  C  CG  . ARG A 1 93  ? -36.568 -30.057 17.245  1.00 16.85 ? 93  ARG B CG  1 
ATOM   733  C  CD  . ARG A 1 93  ? -37.502 -29.426 16.259  1.00 20.81 ? 93  ARG B CD  1 
ATOM   734  N  NE  . ARG A 1 93  ? -38.824 -30.090 16.394  1.00 23.03 ? 93  ARG B NE  1 
ATOM   735  C  CZ  . ARG A 1 93  ? -39.775 -30.029 15.465  1.00 32.47 ? 93  ARG B CZ  1 
ATOM   736  N  NH1 . ARG A 1 93  ? -39.518 -29.352 14.332  1.00 26.05 ? 93  ARG B NH1 1 
ATOM   737  N  NH2 . ARG A 1 93  ? -40.935 -30.654 15.659  1.00 33.12 ? 93  ARG B NH2 1 
ATOM   738  N  N   . GLN A 1 94  ? -34.857 -28.346 19.782  1.00 10.30 ? 94  GLN B N   1 
ATOM   739  C  CA  . GLN A 1 94  ? -35.513 -28.162 21.053  1.00 12.39 ? 94  GLN B CA  1 
ATOM   740  C  C   . GLN A 1 94  ? -34.576 -28.392 22.227  1.00 11.62 ? 94  GLN B C   1 
ATOM   741  O  O   . GLN A 1 94  ? -33.548 -29.101 22.021  1.00 11.46 ? 94  GLN B O   1 
ATOM   742  C  CB  . GLN A 1 94  ? -36.836 -28.909 21.083  1.00 18.60 ? 94  GLN B CB  1 
ATOM   743  C  CG  . GLN A 1 94  ? -36.710 -30.321 21.131  1.00 17.27 ? 94  GLN B CG  1 
ATOM   744  C  CD  . GLN A 1 94  ? -36.970 -30.757 22.539  1.00 22.91 ? 94  GLN B CD  1 
ATOM   745  O  OE1 . GLN A 1 94  ? -36.031 -30.734 23.333  1.00 21.61 ? 94  GLN B OE1 1 
ATOM   746  N  NE2 . GLN A 1 94  ? -38.139 -31.176 22.846  1.00 23.40 ? 94  GLN B NE2 1 
ATOM   747  N  N   . VAL A 1 95  ? -34.910 -27.795 23.347  1.00 10.57 ? 95  VAL B N   1 
ATOM   748  C  CA  . VAL A 1 95  ? -34.135 -28.061 24.591  1.00 10.33 ? 95  VAL B CA  1 
ATOM   749  C  C   . VAL A 1 95  ? -35.180 -28.462 25.627  1.00 10.01 ? 95  VAL B C   1 
ATOM   750  O  O   . VAL A 1 95  ? -36.288 -27.919 25.690  1.00 10.81 ? 95  VAL B O   1 
ATOM   751  C  CB  . VAL A 1 95  ? -33.483 -26.744 24.975  1.00 10.31 ? 95  VAL B CB  1 
ATOM   752  C  CG1 . VAL A 1 95  ? -32.892 -26.821 26.442  1.00 13.04 ? 95  VAL B CG1 1 
ATOM   753  C  CG2 . VAL A 1 95  ? -32.297 -26.520 24.029  1.00 12.77 ? 95  VAL B CG2 1 
ATOM   754  N  N   . HIS A 1 96  ? -34.785 -29.429 26.503  1.00 10.10 ? 96  HIS B N   1 
ATOM   755  C  CA  . HIS A 1 96  ? -35.680 -29.833 27.667  1.00 9.53  ? 96  HIS B CA  1 
ATOM   756  C  C   . HIS A 1 96  ? -34.759 -30.365 28.731  1.00 10.41 ? 96  HIS B C   1 
ATOM   757  O  O   . HIS A 1 96  ? -33.516 -30.434 28.587  1.00 11.13 ? 96  HIS B O   1 
ATOM   758  C  CB  . HIS A 1 96  ? -36.710 -30.868 27.180  1.00 8.90  ? 96  HIS B CB  1 
ATOM   759  C  CG  . HIS A 1 96  ? -36.093 -32.103 26.709  1.00 10.11 ? 96  HIS B CG  1 
ATOM   760  N  ND1 . HIS A 1 96  ? -35.813 -32.345 25.358  1.00 10.93 ? 96  HIS B ND1 1 
ATOM   761  C  CD2 . HIS A 1 96  ? -35.621 -33.192 27.420  1.00 8.67  ? 96  HIS B CD2 1 
ATOM   762  C  CE1 . HIS A 1 96  ? -35.134 -33.505 25.263  1.00 9.76  ? 96  HIS B CE1 1 
ATOM   763  N  NE2 . HIS A 1 96  ? -35.054 -34.059 26.518  1.00 9.22  ? 96  HIS B NE2 1 
ATOM   764  N  N   . LEU A 1 97  ? -35.403 -30.735 29.855  1.00 9.63  ? 97  LEU B N   1 
ATOM   765  C  CA  . LEU A 1 97  ? -34.577 -31.060 31.078  1.00 9.10  ? 97  LEU B CA  1 
ATOM   766  C  C   . LEU A 1 97  ? -35.215 -32.313 31.757  1.00 9.77  ? 97  LEU B C   1 
ATOM   767  O  O   . LEU A 1 97  ? -36.445 -32.509 31.723  1.00 11.24 ? 97  LEU B O   1 
ATOM   768  C  CB  . LEU A 1 97  ? -34.679 -29.876 32.076  1.00 10.00 ? 97  LEU B CB  1 
ATOM   769  C  CG  . LEU A 1 97  ? -33.750 -30.061 33.315  1.00 9.43  ? 97  LEU B CG  1 
ATOM   770  C  CD1 . LEU A 1 97  ? -32.259 -29.956 32.936  1.00 10.49 ? 97  LEU B CD1 1 
ATOM   771  C  CD2 . LEU A 1 97  ? -34.190 -28.923 34.235  1.00 11.55 ? 97  LEU B CD2 1 
ATOM   772  N  N   . HIS A 1 98  ? -34.326 -33.164 32.349  1.00 8.96  ? 98  HIS B N   1 
ATOM   773  C  CA  . HIS A 1 98  ? -34.770 -34.346 33.134  1.00 8.93  ? 98  HIS B CA  1 
ATOM   774  C  C   . HIS A 1 98  ? -34.278 -34.114 34.577  1.00 9.23  ? 98  HIS B C   1 
ATOM   775  O  O   . HIS A 1 98  ? -33.208 -33.631 34.781  1.00 10.70 ? 98  HIS B O   1 
ATOM   776  C  CB  . HIS A 1 98  ? -34.233 -35.625 32.616  1.00 9.36  ? 98  HIS B CB  1 
ATOM   777  C  CG  . HIS A 1 98  ? -34.615 -35.907 31.173  1.00 9.94  ? 98  HIS B CG  1 
ATOM   778  N  ND1 . HIS A 1 98  ? -35.806 -36.506 30.848  1.00 10.26 ? 98  HIS B ND1 1 
ATOM   779  C  CD2 . HIS A 1 98  ? -33.957 -35.586 29.975  1.00 10.33 ? 98  HIS B CD2 1 
ATOM   780  C  CE1 . HIS A 1 98  ? -35.860 -36.688 29.476  1.00 9.13  ? 98  HIS B CE1 1 
ATOM   781  N  NE2 . HIS A 1 98  ? -34.792 -36.034 28.945  1.00 8.11  ? 98  HIS B NE2 1 
ATOM   782  N  N   . TRP A 1 99  ? -35.099 -34.563 35.521  1.00 9.23  ? 99  TRP B N   1 
ATOM   783  C  CA  . TRP A 1 99  ? -34.688 -34.476 36.977  1.00 10.69 ? 99  TRP B CA  1 
ATOM   784  C  C   . TRP A 1 99  ? -35.354 -35.629 37.659  1.00 10.82 ? 99  TRP B C   1 
ATOM   785  O  O   . TRP A 1 99  ? -36.167 -36.381 37.092  1.00 11.53 ? 99  TRP B O   1 
ATOM   786  C  CB  . TRP A 1 99  ? -35.151 -33.099 37.505  1.00 10.73 ? 99  TRP B CB  1 
ATOM   787  C  CG  . TRP A 1 99  ? -36.640 -32.870 37.373  1.00 11.02 ? 99  TRP B CG  1 
ATOM   788  C  CD1 . TRP A 1 99  ? -37.641 -33.329 38.202  1.00 10.73 ? 99  TRP B CD1 1 
ATOM   789  C  CD2 . TRP A 1 99  ? -37.309 -32.157 36.272  1.00 11.09 ? 99  TRP B CD2 1 
ATOM   790  N  NE1 . TRP A 1 99  ? -38.937 -32.941 37.758  1.00 10.65 ? 99  TRP B NE1 1 
ATOM   791  C  CE2 . TRP A 1 99  ? -38.755 -32.168 36.554  1.00 11.57 ? 99  TRP B CE2 1 
ATOM   792  C  CE3 . TRP A 1 99  ? -36.829 -31.406 35.195  1.00 11.90 ? 99  TRP B CE3 1 
ATOM   793  C  CZ2 . TRP A 1 99  ? -39.677 -31.538 35.707  1.00 11.80 ? 99  TRP B CZ2 1 
ATOM   794  C  CZ3 . TRP A 1 99  ? -37.759 -30.790 34.315  1.00 10.92 ? 99  TRP B CZ3 1 
ATOM   795  C  CH2 . TRP A 1 99  ? -39.150 -30.811 34.583  1.00 12.16 ? 99  TRP B CH2 1 
ATOM   796  N  N   . GLY A 1 100 ? -35.041 -35.767 38.960  1.00 12.04 ? 100 GLY B N   1 
ATOM   797  C  CA  . GLY A 1 100 ? -35.647 -36.815 39.802  1.00 12.19 ? 100 GLY B CA  1 
ATOM   798  C  C   . GLY A 1 100 ? -36.394 -36.139 40.950  1.00 12.26 ? 100 GLY B C   1 
ATOM   799  O  O   . GLY A 1 100 ? -36.452 -34.928 41.062  1.00 13.45 ? 100 GLY B O   1 
ATOM   800  N  N   . SER A 1 101 ? -37.022 -36.980 41.806  1.00 14.06 ? 101 SER B N   1 
ATOM   801  C  CA  . SER A 1 101 ? -37.841 -36.419 42.902  1.00 14.88 ? 101 SER B CA  1 
ATOM   802  C  C   . SER A 1 101 ? -37.001 -35.932 44.037  1.00 16.30 ? 101 SER B C   1 
ATOM   803  O  O   . SER A 1 101 ? -37.508 -35.214 44.869  1.00 17.12 ? 101 SER B O   1 
ATOM   804  C  CB  . SER A 1 101 ? -38.826 -37.439 43.491  1.00 14.88 ? 101 SER B CB  1 
ATOM   805  O  OG  . SER A 1 101 ? -38.136 -38.563 43.999  1.00 20.19 ? 101 SER B OG  1 
ATOM   806  N  N   . ALA A 1 102 ? -35.747 -36.310 44.057  1.00 14.77 ? 102 ALA B N   1 
ATOM   807  C  CA  . ALA A 1 102 ? -34.831 -35.676 44.971  1.00 14.55 ? 102 ALA B CA  1 
ATOM   808  C  C   . ALA A 1 102 ? -33.500 -35.282 44.315  1.00 14.19 ? 102 ALA B C   1 
ATOM   809  O  O   . ALA A 1 102 ? -33.083 -35.845 43.263  1.00 14.44 ? 102 ALA B O   1 
ATOM   810  C  CB  . ALA A 1 102 ? -34.594 -36.671 46.122  1.00 14.87 ? 102 ALA B CB  1 
ATOM   811  N  N   . ASP A 1 103 ? -32.740 -34.401 44.986  1.00 15.69 ? 103 ASP B N   1 
ATOM   812  C  CA  . ASP A 1 103 ? -31.526 -33.882 44.346  1.00 15.97 ? 103 ASP B CA  1 
ATOM   813  C  C   . ASP A 1 103 ? -30.417 -34.854 44.142  1.00 16.77 ? 103 ASP B C   1 
ATOM   814  O  O   . ASP A 1 103 ? -29.484 -34.608 43.356  1.00 20.31 ? 103 ASP B O   1 
ATOM   815  C  CB  . ASP A 1 103 ? -30.939 -32.684 45.139  1.00 18.30 ? 103 ASP B CB  1 
ATOM   816  C  CG  . ASP A 1 103 ? -31.886 -31.546 45.256  1.00 20.35 ? 103 ASP B CG  1 
ATOM   817  O  OD1 . ASP A 1 103 ? -32.835 -31.336 44.442  1.00 17.98 ? 103 ASP B OD1 1 
ATOM   818  O  OD2 . ASP A 1 103 ? -31.615 -30.715 46.158  1.00 21.53 ? 103 ASP B OD2 1 
ATOM   819  N  N   . ASP A 1 104 ? -30.427 -35.993 44.808  1.00 15.99 ? 104 ASP B N   1 
ATOM   820  C  CA  . ASP A 1 104 ? -29.254 -36.884 44.731  1.00 18.56 ? 104 ASP B CA  1 
ATOM   821  C  C   . ASP A 1 104 ? -29.188 -37.720 43.464  1.00 17.98 ? 104 ASP B C   1 
ATOM   822  O  O   . ASP A 1 104 ? -28.144 -38.309 43.192  1.00 20.86 ? 104 ASP B O   1 
ATOM   823  C  CB  . ASP A 1 104 ? -29.250 -37.904 45.899  1.00 19.60 ? 104 ASP B CB  1 
ATOM   824  C  CG  . ASP A 1 104 ? -30.472 -38.742 45.933  1.00 22.77 ? 104 ASP B CG  1 
ATOM   825  O  OD1 . ASP A 1 104 ? -31.548 -38.231 46.384  1.00 27.26 ? 104 ASP B OD1 1 
ATOM   826  O  OD2 . ASP A 1 104 ? -30.388 -39.905 45.469  1.00 27.93 ? 104 ASP B OD2 1 
ATOM   827  N  N   . HIS A 1 105 ? -30.294 -37.785 42.693  1.00 18.77 ? 105 HIS B N   1 
ATOM   828  C  CA  . HIS A 1 105 ? -30.196 -38.498 41.417  1.00 20.38 ? 105 HIS B CA  1 
ATOM   829  C  C   . HIS A 1 105 ? -31.304 -37.942 40.524  1.00 19.86 ? 105 HIS B C   1 
ATOM   830  O  O   . HIS A 1 105 ? -32.201 -37.295 40.980  1.00 21.54 ? 105 HIS B O   1 
ATOM   831  C  CB  . HIS A 1 105 ? -30.163 -40.060 41.560  1.00 26.25 ? 105 HIS B CB  1 
ATOM   832  C  CG  . HIS A 1 105 ? -31.397 -40.678 42.136  1.00 32.38 ? 105 HIS B CG  1 
ATOM   833  N  ND1 . HIS A 1 105 ? -32.427 -41.128 41.372  1.00 38.56 ? 105 HIS B ND1 1 
ATOM   834  C  CD2 . HIS A 1 105 ? -31.720 -41.016 43.464  1.00 34.47 ? 105 HIS B CD2 1 
ATOM   835  C  CE1 . HIS A 1 105 ? -33.394 -41.649 42.178  1.00 35.09 ? 105 HIS B CE1 1 
ATOM   836  N  NE2 . HIS A 1 105 ? -32.948 -41.600 43.453  1.00 38.91 ? 105 HIS B NE2 1 
ATOM   837  N  N   . GLY A 1 106 ? -31.162 -38.053 39.213  1.00 20.84 ? 106 GLY B N   1 
ATOM   838  C  CA  . GLY A 1 106 ? -32.152 -37.351 38.366  1.00 15.93 ? 106 GLY B CA  1 
ATOM   839  C  C   . GLY A 1 106 ? -31.584 -37.321 36.993  1.00 14.91 ? 106 GLY B C   1 
ATOM   840  O  O   . GLY A 1 106 ? -32.353 -37.139 36.023  1.00 15.68 ? 106 GLY B O   1 
ATOM   841  N  N   . SER A 1 107 ? -30.266 -37.401 36.898  1.00 12.14 ? 107 SER B N   1 
ATOM   842  C  CA  . SER A 1 107 ? -29.731 -37.502 35.504  1.00 12.75 ? 107 SER B CA  1 
ATOM   843  C  C   . SER A 1 107 ? -30.131 -38.823 34.815  1.00 13.84 ? 107 SER B C   1 
ATOM   844  O  O   . SER A 1 107 ? -30.490 -39.836 35.449  1.00 14.49 ? 107 SER B O   1 
ATOM   845  C  CB  . SER A 1 107 ? -28.247 -37.275 35.454  1.00 12.95 ? 107 SER B CB  1 
ATOM   846  O  OG  . SER A 1 107 ? -27.512 -38.334 36.115  1.00 13.38 ? 107 SER B OG  1 
ATOM   847  N  N   . GLU A 1 108 ? -30.090 -38.775 33.473  1.00 12.58 ? 108 GLU B N   1 
ATOM   848  C  CA  . GLU A 1 108 ? -30.360 -39.995 32.700  1.00 11.30 ? 108 GLU B CA  1 
ATOM   849  C  C   . GLU A 1 108 ? -29.100 -40.781 32.507  1.00 12.35 ? 108 GLU B C   1 
ATOM   850  O  O   . GLU A 1 108 ? -29.078 -41.999 32.823  1.00 14.01 ? 108 GLU B O   1 
ATOM   851  C  CB  . GLU A 1 108 ? -31.039 -39.549 31.357  1.00 11.33 ? 108 GLU B CB  1 
ATOM   852  C  CG  . GLU A 1 108 ? -32.359 -38.867 31.602  1.00 12.74 ? 108 GLU B CG  1 
ATOM   853  C  CD  . GLU A 1 108 ? -33.393 -39.145 30.526  1.00 13.68 ? 108 GLU B CD  1 
ATOM   854  O  OE1 . GLU A 1 108 ? -33.052 -38.956 29.360  1.00 11.76 ? 108 GLU B OE1 1 
ATOM   855  O  OE2 . GLU A 1 108 ? -34.493 -39.531 30.851  1.00 10.68 ? 108 GLU B OE2 1 
ATOM   856  N  N   . HIS A 1 109 ? -28.059 -40.196 31.921  1.00 11.63 ? 109 HIS B N   1 
ATOM   857  C  CA  . HIS A 1 109 ? -26.773 -40.849 31.930  1.00 12.18 ? 109 HIS B CA  1 
ATOM   858  C  C   . HIS A 1 109 ? -26.135 -40.867 33.310  1.00 12.80 ? 109 HIS B C   1 
ATOM   859  O  O   . HIS A 1 109 ? -26.318 -39.965 34.109  1.00 12.85 ? 109 HIS B O   1 
ATOM   860  C  CB  . HIS A 1 109 ? -25.823 -40.166 30.906  1.00 11.26 ? 109 HIS B CB  1 
ATOM   861  C  CG  . HIS A 1 109 ? -26.307 -40.355 29.454  1.00 11.88 ? 109 HIS B CG  1 
ATOM   862  N  ND1 . HIS A 1 109 ? -27.187 -39.486 28.887  1.00 11.55 ? 109 HIS B ND1 1 
ATOM   863  C  CD2 . HIS A 1 109 ? -26.120 -41.365 28.558  1.00 12.03 ? 109 HIS B CD2 1 
ATOM   864  C  CE1 . HIS A 1 109 ? -27.493 -39.907 27.619  1.00 10.36 ? 109 HIS B CE1 1 
ATOM   865  N  NE2 . HIS A 1 109 ? -26.821 -41.046 27.400  1.00 13.30 ? 109 HIS B NE2 1 
ATOM   866  N  N   . ILE A 1 110 ? -25.363 -41.930 33.524  1.00 12.46 ? 110 ILE B N   1 
ATOM   867  C  CA  . ILE A 1 110 ? -24.646 -42.089 34.840  1.00 14.13 ? 110 ILE B CA  1 
ATOM   868  C  C   . ILE A 1 110 ? -23.219 -42.428 34.521  1.00 15.21 ? 110 ILE B C   1 
ATOM   869  O  O   . ILE A 1 110 ? -22.974 -43.371 33.741  1.00 18.76 ? 110 ILE B O   1 
ATOM   870  C  CB  . ILE A 1 110 ? -25.346 -43.225 35.626  1.00 16.63 ? 110 ILE B CB  1 
ATOM   871  C  CG1 . ILE A 1 110 ? -26.804 -42.796 35.937  1.00 15.65 ? 110 ILE B CG1 1 
ATOM   872  C  CG2 . ILE A 1 110 ? -24.628 -43.492 36.949  1.00 19.45 ? 110 ILE B CG2 1 
ATOM   873  C  CD1 . ILE A 1 110 ? -27.666 -43.782 36.772  1.00 18.97 ? 110 ILE B CD1 1 
ATOM   874  N  N   . VAL A 1 111 ? -22.294 -41.738 35.180  1.00 15.59 ? 111 VAL B N   1 
ATOM   875  C  CA  . VAL A 1 111 ? -20.880 -41.853 34.850  1.00 17.10 ? 111 VAL B CA  1 
ATOM   876  C  C   . VAL A 1 111 ? -20.111 -42.512 35.992  1.00 18.76 ? 111 VAL B C   1 
ATOM   877  O  O   . VAL A 1 111 ? -20.067 -41.960 37.050  1.00 19.49 ? 111 VAL B O   1 
ATOM   878  C  CB  . VAL A 1 111 ? -20.311 -40.483 34.634  1.00 18.05 ? 111 VAL B CB  1 
ATOM   879  C  CG1 . VAL A 1 111 ? -18.805 -40.639 34.239  1.00 21.57 ? 111 VAL B CG1 1 
ATOM   880  C  CG2 . VAL A 1 111 ? -21.143 -39.816 33.487  1.00 19.59 ? 111 VAL B CG2 1 
ATOM   881  N  N   . ASP A 1 112 ? -19.581 -43.690 35.729  1.00 17.16 ? 112 ASP B N   1 
ATOM   882  C  CA  . ASP A 1 112 ? -18.859 -44.492 36.829  1.00 21.79 ? 112 ASP B CA  1 
ATOM   883  C  C   . ASP A 1 112 ? -19.668 -44.457 38.121  1.00 22.87 ? 112 ASP B C   1 
ATOM   884  O  O   . ASP A 1 112 ? -19.120 -44.206 39.209  1.00 24.58 ? 112 ASP B O   1 
ATOM   885  C  CB  . ASP A 1 112 ? -17.502 -43.904 37.051  1.00 20.34 ? 112 ASP B CB  1 
ATOM   886  C  CG  . ASP A 1 112 ? -16.579 -44.160 35.896  1.00 20.82 ? 112 ASP B CG  1 
ATOM   887  O  OD1 . ASP A 1 112 ? -16.640 -45.272 35.281  1.00 25.27 ? 112 ASP B OD1 1 
ATOM   888  O  OD2 . ASP A 1 112 ? -15.725 -43.274 35.687  1.00 23.67 ? 112 ASP B OD2 1 
ATOM   889  N  N   . GLY A 1 113 ? -20.962 -44.725 37.966  1.00 19.45 ? 113 GLY B N   1 
ATOM   890  C  CA  . GLY A 1 113 ? -21.919 -44.867 39.074  1.00 19.27 ? 113 GLY B CA  1 
ATOM   891  C  C   . GLY A 1 113 ? -22.414 -43.556 39.698  1.00 19.98 ? 113 GLY B C   1 
ATOM   892  O  O   . GLY A 1 113 ? -23.313 -43.564 40.568  1.00 22.05 ? 113 GLY B O   1 
ATOM   893  N  N   . VAL A 1 114 ? -21.867 -42.420 39.257  1.00 20.32 ? 114 VAL B N   1 
ATOM   894  C  CA  . VAL A 1 114 ? -22.287 -41.093 39.661  1.00 18.94 ? 114 VAL B CA  1 
ATOM   895  C  C   . VAL A 1 114 ? -23.507 -40.512 38.885  1.00 20.51 ? 114 VAL B C   1 
ATOM   896  O  O   . VAL A 1 114 ? -23.461 -40.371 37.671  1.00 19.55 ? 114 VAL B O   1 
ATOM   897  C  CB  . VAL A 1 114 ? -21.133 -40.076 39.544  1.00 21.37 ? 114 VAL B CB  1 
ATOM   898  C  CG1 . VAL A 1 114 ? -21.577 -38.646 39.930  1.00 22.35 ? 114 VAL B CG1 1 
ATOM   899  C  CG2 . VAL A 1 114 ? -19.901 -40.504 40.395  1.00 25.42 ? 114 VAL B CG2 1 
ATOM   900  N  N   A SER A 1 115 ? -24.550 -40.153 39.629  0.50 19.72 ? 115 SER B N   1 
ATOM   901  N  N   B SER A 1 115 ? -24.585 -40.263 39.605  0.50 17.80 ? 115 SER B N   1 
ATOM   902  C  CA  A SER A 1 115 ? -25.811 -39.579 39.114  0.50 19.01 ? 115 SER B CA  1 
ATOM   903  C  CA  B SER A 1 115 ? -25.705 -39.516 39.061  0.50 16.29 ? 115 SER B CA  1 
ATOM   904  C  C   A SER A 1 115 ? -25.994 -38.108 39.546  0.50 17.69 ? 115 SER B C   1 
ATOM   905  C  C   B SER A 1 115 ? -25.497 -38.038 39.418  0.50 16.46 ? 115 SER B C   1 
ATOM   906  O  O   A SER A 1 115 ? -26.049 -37.782 40.728  0.50 16.76 ? 115 SER B O   1 
ATOM   907  O  O   B SER A 1 115 ? -24.800 -37.647 40.389  0.50 15.42 ? 115 SER B O   1 
ATOM   908  C  CB  A SER A 1 115 ? -26.993 -40.399 39.633  0.50 21.47 ? 115 SER B CB  1 
ATOM   909  C  CB  B SER A 1 115 ? -27.066 -40.012 39.603  0.50 16.07 ? 115 SER B CB  1 
ATOM   910  O  OG  A SER A 1 115 ? -26.995 -40.437 41.059  0.50 23.67 ? 115 SER B OG  1 
ATOM   911  O  OG  B SER A 1 115 ? -27.373 -41.366 39.221  0.50 13.87 ? 115 SER B OG  1 
ATOM   912  N  N   . TYR A 1 116 ? -26.079 -37.220 38.575  1.00 15.75 ? 116 TYR B N   1 
ATOM   913  C  CA  . TYR A 1 116 ? -26.199 -35.797 38.850  1.00 16.23 ? 116 TYR B CA  1 
ATOM   914  C  C   . TYR A 1 116 ? -27.681 -35.461 39.181  1.00 16.47 ? 116 TYR B C   1 
ATOM   915  O  O   . TYR A 1 116 ? -28.536 -36.329 39.055  1.00 15.36 ? 116 TYR B O   1 
ATOM   916  C  CB  . TYR A 1 116 ? -25.710 -35.070 37.598  1.00 14.43 ? 116 TYR B CB  1 
ATOM   917  C  CG  . TYR A 1 116 ? -24.231 -35.198 37.418  1.00 15.09 ? 116 TYR B CG  1 
ATOM   918  C  CD1 . TYR A 1 116 ? -23.353 -34.398 38.195  1.00 16.59 ? 116 TYR B CD1 1 
ATOM   919  C  CD2 . TYR A 1 116 ? -23.712 -36.176 36.578  1.00 15.30 ? 116 TYR B CD2 1 
ATOM   920  C  CE1 . TYR A 1 116 ? -21.962 -34.533 38.002  1.00 19.66 ? 116 TYR B CE1 1 
ATOM   921  C  CE2 . TYR A 1 116 ? -22.345 -36.337 36.420  1.00 18.86 ? 116 TYR B CE2 1 
ATOM   922  C  CZ  . TYR A 1 116 ? -21.509 -35.506 37.162  1.00 22.47 ? 116 TYR B CZ  1 
ATOM   923  O  OH  . TYR A 1 116 ? -20.151 -35.662 36.991  1.00 30.37 ? 116 TYR B OH  1 
ATOM   924  N  N   . ALA A 1 117 ? -28.005 -34.256 39.604  1.00 13.31 ? 117 ALA B N   1 
ATOM   925  C  CA  . ALA A 1 117 ? -29.319 -33.862 39.968  1.00 13.63 ? 117 ALA B CA  1 
ATOM   926  C  C   . ALA A 1 117 ? -30.276 -33.794 38.768  1.00 12.98 ? 117 ALA B C   1 
ATOM   927  O  O   . ALA A 1 117 ? -31.473 -33.965 38.890  1.00 14.75 ? 117 ALA B O   1 
ATOM   928  C  CB  . ALA A 1 117 ? -29.294 -32.461 40.701  1.00 14.54 ? 117 ALA B CB  1 
ATOM   929  N  N   . ALA A 1 118 ? -29.696 -33.430 37.640  1.00 12.06 ? 118 ALA B N   1 
ATOM   930  C  CA  . ALA A 1 118 ? -30.619 -33.198 36.452  1.00 10.62 ? 118 ALA B CA  1 
ATOM   931  C  C   . ALA A 1 118 ? -29.716 -33.217 35.213  1.00 10.78 ? 118 ALA B C   1 
ATOM   932  O  O   . ALA A 1 118 ? -28.494 -33.406 35.265  1.00 10.44 ? 118 ALA B O   1 
ATOM   933  C  CB  . ALA A 1 118 ? -31.268 -31.867 36.503  1.00 12.28 ? 118 ALA B CB  1 
ATOM   934  N  N   . GLU A 1 119 ? -30.359 -33.305 34.030  1.00 10.26 ? 119 GLU B N   1 
ATOM   935  C  CA  . GLU A 1 119 ? -29.599 -33.460 32.768  1.00 9.47  ? 119 GLU B CA  1 
ATOM   936  C  C   . GLU A 1 119 ? -30.393 -32.645 31.709  1.00 9.59  ? 119 GLU B C   1 
ATOM   937  O  O   . GLU A 1 119 ? -31.580 -32.947 31.469  1.00 9.77  ? 119 GLU B O   1 
ATOM   938  C  CB  . GLU A 1 119 ? -29.532 -34.903 32.383  1.00 10.88 ? 119 GLU B CB  1 
ATOM   939  C  CG  . GLU A 1 119 ? -28.617 -35.123 31.145  1.00 9.53  ? 119 GLU B CG  1 
ATOM   940  C  CD  . GLU A 1 119 ? -28.347 -36.555 30.889  1.00 12.22 ? 119 GLU B CD  1 
ATOM   941  O  OE1 . GLU A 1 119 ? -28.166 -37.341 31.854  1.00 11.79 ? 119 GLU B OE1 1 
ATOM   942  O  OE2 . GLU A 1 119 ? -28.210 -36.995 29.750  1.00 11.01 ? 119 GLU B OE2 1 
ATOM   943  N  N   . LEU A 1 120 ? -29.696 -31.728 31.039  1.00 9.47  ? 120 LEU B N   1 
ATOM   944  C  CA  . LEU A 1 120 ? -30.330 -30.886 30.013  1.00 9.49  ? 120 LEU B CA  1 
ATOM   945  C  C   . LEU A 1 120 ? -30.035 -31.583 28.668  1.00 8.84  ? 120 LEU B C   1 
ATOM   946  O  O   . LEU A 1 120 ? -28.917 -32.083 28.423  1.00 9.86  ? 120 LEU B O   1 
ATOM   947  C  CB  . LEU A 1 120 ? -29.639 -29.506 30.011  1.00 11.24 ? 120 LEU B CB  1 
ATOM   948  C  CG  . LEU A 1 120 ? -30.240 -28.487 29.020  1.00 12.25 ? 120 LEU B CG  1 
ATOM   949  C  CD1 . LEU A 1 120 ? -31.436 -27.826 29.654  1.00 11.92 ? 120 LEU B CD1 1 
ATOM   950  C  CD2 . LEU A 1 120 ? -29.122 -27.447 28.719  1.00 17.51 ? 120 LEU B CD2 1 
ATOM   951  N  N   . HIS A 1 121 ? -31.041 -31.599 27.739  1.00 8.75  ? 121 HIS B N   1 
ATOM   952  C  CA  . HIS A 1 121 ? -30.791 -32.198 26.444  1.00 8.89  ? 121 HIS B CA  1 
ATOM   953  C  C   . HIS A 1 121 ? -31.070 -31.149 25.383  1.00 9.61  ? 121 HIS B C   1 
ATOM   954  O  O   . HIS A 1 121 ? -32.095 -30.443 25.434  1.00 11.06 ? 121 HIS B O   1 
ATOM   955  C  CB  . HIS A 1 121 ? -31.746 -33.388 26.204  1.00 9.35  ? 121 HIS B CB  1 
ATOM   956  C  CG  . HIS A 1 121 ? -31.358 -34.610 27.008  1.00 9.90  ? 121 HIS B CG  1 
ATOM   957  N  ND1 . HIS A 1 121 ? -32.213 -35.615 27.289  1.00 10.19 ? 121 HIS B ND1 1 
ATOM   958  C  CD2 . HIS A 1 121 ? -30.151 -34.948 27.614  1.00 10.04 ? 121 HIS B CD2 1 
ATOM   959  C  CE1 . HIS A 1 121 ? -31.579 -36.547 28.026  1.00 10.80 ? 121 HIS B CE1 1 
ATOM   960  N  NE2 . HIS A 1 121 ? -30.319 -36.137 28.224  1.00 10.71 ? 121 HIS B NE2 1 
ATOM   961  N  N   . VAL A 1 122 ? -30.146 -31.102 24.382  1.00 10.39 ? 122 VAL B N   1 
ATOM   962  C  CA  . VAL A 1 122 ? -30.273 -30.128 23.253  1.00 10.19 ? 122 VAL B CA  1 
ATOM   963  C  C   . VAL A 1 122 ? -30.393 -31.039 22.028  1.00 9.24  ? 122 VAL B C   1 
ATOM   964  O  O   . VAL A 1 122 ? -29.427 -31.686 21.583  1.00 10.14 ? 122 VAL B O   1 
ATOM   965  C  CB  . VAL A 1 122 ? -29.015 -29.218 23.225  1.00 10.71 ? 122 VAL B CB  1 
ATOM   966  C  CG1 . VAL A 1 122 ? -29.325 -28.109 22.249  1.00 10.05 ? 122 VAL B CG1 1 
ATOM   967  C  CG2 . VAL A 1 122 ? -28.779 -28.573 24.615  1.00 13.32 ? 122 VAL B CG2 1 
ATOM   968  N  N   . VAL A 1 123 ? -31.593 -30.953 21.388  1.00 9.32  ? 123 VAL B N   1 
ATOM   969  C  CA  . VAL A 1 123 ? -31.933 -31.907 20.331  1.00 9.71  ? 123 VAL B CA  1 
ATOM   970  C  C   . VAL A 1 123 ? -31.765 -31.200 18.936  1.00 9.92  ? 123 VAL B C   1 
ATOM   971  O  O   . VAL A 1 123 ? -32.229 -30.082 18.762  1.00 9.62  ? 123 VAL B O   1 
ATOM   972  C  CB  . VAL A 1 123 ? -33.399 -32.352 20.497  1.00 9.98  ? 123 VAL B CB  1 
ATOM   973  C  CG1 . VAL A 1 123 ? -33.787 -33.332 19.414  1.00 9.41  ? 123 VAL B CG1 1 
ATOM   974  C  CG2 . VAL A 1 123 ? -33.604 -33.040 21.881  1.00 10.20 ? 123 VAL B CG2 1 
ATOM   975  N  N   . HIS A 1 124 ? -31.036 -31.883 18.058  1.00 10.44 ? 124 HIS B N   1 
ATOM   976  C  CA  . HIS A 1 124 ? -30.734 -31.334 16.704  1.00 10.67 ? 124 HIS B CA  1 
ATOM   977  C  C   . HIS A 1 124 ? -31.073 -32.449 15.723  1.00 11.16 ? 124 HIS B C   1 
ATOM   978  O  O   . HIS A 1 124 ? -31.070 -33.685 15.994  1.00 10.88 ? 124 HIS B O   1 
ATOM   979  C  CB  . HIS A 1 124 ? -29.198 -31.082 16.560  1.00 10.24 ? 124 HIS B CB  1 
ATOM   980  C  CG  . HIS A 1 124 ? -28.621 -30.213 17.621  1.00 12.31 ? 124 HIS B CG  1 
ATOM   981  N  ND1 . HIS A 1 124 ? -28.373 -30.702 18.903  1.00 12.95 ? 124 HIS B ND1 1 
ATOM   982  C  CD2 . HIS A 1 124 ? -28.213 -28.910 17.598  1.00 12.25 ? 124 HIS B CD2 1 
ATOM   983  C  CE1 . HIS A 1 124 ? -27.806 -29.722 19.628  1.00 12.63 ? 124 HIS B CE1 1 
ATOM   984  N  NE2 . HIS A 1 124 ? -27.730 -28.612 18.877  1.00 13.42 ? 124 HIS B NE2 1 
ATOM   985  N  N   . TRP A 1 125 ? -31.294 -32.029 14.437  1.00 11.39 ? 125 TRP B N   1 
ATOM   986  C  CA  . TRP A 1 125 ? -31.571 -33.041 13.436  1.00 10.25 ? 125 TRP B CA  1 
ATOM   987  C  C   . TRP A 1 125 ? -30.877 -32.756 12.055  1.00 10.80 ? 125 TRP B C   1 
ATOM   988  O  O   . TRP A 1 125 ? -30.595 -31.597 11.772  1.00 13.20 ? 125 TRP B O   1 
ATOM   989  C  CB  . TRP A 1 125 ? -33.128 -33.181 13.157  1.00 12.67 ? 125 TRP B CB  1 
ATOM   990  C  CG  . TRP A 1 125 ? -33.790 -31.890 12.733  1.00 12.08 ? 125 TRP B CG  1 
ATOM   991  C  CD1 . TRP A 1 125 ? -34.172 -30.802 13.535  1.00 14.01 ? 125 TRP B CD1 1 
ATOM   992  C  CD2 . TRP A 1 125 ? -34.220 -31.538 11.368  1.00 14.60 ? 125 TRP B CD2 1 
ATOM   993  N  NE1 . TRP A 1 125 ? -34.801 -29.807 12.777  1.00 13.02 ? 125 TRP B NE1 1 
ATOM   994  C  CE2 . TRP A 1 125 ? -34.814 -30.207 11.445  1.00 13.18 ? 125 TRP B CE2 1 
ATOM   995  C  CE3 . TRP A 1 125 ? -34.070 -32.176 10.101  1.00 15.34 ? 125 TRP B CE3 1 
ATOM   996  C  CZ2 . TRP A 1 125 ? -35.367 -29.575 10.326  1.00 14.64 ? 125 TRP B CZ2 1 
ATOM   997  C  CZ3 . TRP A 1 125 ? -34.630 -31.502 8.967   1.00 16.65 ? 125 TRP B CZ3 1 
ATOM   998  C  CH2 . TRP A 1 125 ? -35.209 -30.242 9.107   1.00 14.47 ? 125 TRP B CH2 1 
ATOM   999  N  N   . ASN A 1 126 ? -30.676 -33.854 11.300  1.00 11.62 ? 126 ASN B N   1 
ATOM   1000 C  CA  . ASN A 1 126 ? -29.824 -33.760 10.096  1.00 10.89 ? 126 ASN B CA  1 
ATOM   1001 C  C   . ASN A 1 126 ? -30.628 -33.169 8.903   1.00 11.95 ? 126 ASN B C   1 
ATOM   1002 O  O   . ASN A 1 126 ? -31.282 -33.919 8.240   1.00 13.71 ? 126 ASN B O   1 
ATOM   1003 C  CB  . ASN A 1 126 ? -29.400 -35.165 9.766   1.00 13.21 ? 126 ASN B CB  1 
ATOM   1004 C  CG  . ASN A 1 126 ? -28.358 -35.195 8.645   1.00 16.19 ? 126 ASN B CG  1 
ATOM   1005 O  OD1 . ASN A 1 126 ? -28.221 -34.214 7.877   1.00 17.36 ? 126 ASN B OD1 1 
ATOM   1006 N  ND2 . ASN A 1 126 ? -27.592 -36.290 8.602   1.00 19.63 ? 126 ASN B ND2 1 
ATOM   1007 N  N   . SER A 1 127 ? -30.563 -31.848 8.769   1.00 12.70 ? 127 SER B N   1 
ATOM   1008 C  CA  . SER A 1 127 ? -31.351 -31.143 7.692   1.00 13.16 ? 127 SER B CA  1 
ATOM   1009 C  C   . SER A 1 127 ? -30.487 -31.196 6.419   1.00 14.35 ? 127 SER B C   1 
ATOM   1010 O  O   . SER A 1 127 ? -31.003 -30.749 5.371   1.00 15.06 ? 127 SER B O   1 
ATOM   1011 C  CB  . SER A 1 127 ? -31.584 -29.723 8.109   1.00 13.91 ? 127 SER B CB  1 
ATOM   1012 O  OG  . SER A 1 127 ? -30.376 -29.044 8.426   1.00 16.34 ? 127 SER B OG  1 
ATOM   1013 N  N   . ASP A 1 128 ? -29.291 -31.742 6.489   1.00 13.19 ? 128 ASP B N   1 
ATOM   1014 C  CA  . ASP A 1 128 ? -28.528 -31.937 5.212   1.00 15.51 ? 128 ASP B CA  1 
ATOM   1015 C  C   . ASP A 1 128 ? -29.068 -33.134 4.453   1.00 16.83 ? 128 ASP B C   1 
ATOM   1016 O  O   . ASP A 1 128 ? -28.912 -33.197 3.211   1.00 21.36 ? 128 ASP B O   1 
ATOM   1017 C  CB  . ASP A 1 128 ? -27.028 -32.154 5.444   1.00 16.17 ? 128 ASP B CB  1 
ATOM   1018 C  CG  . ASP A 1 128 ? -26.279 -30.847 5.735   1.00 16.91 ? 128 ASP B CG  1 
ATOM   1019 O  OD1 . ASP A 1 128 ? -25.077 -30.956 6.085   1.00 18.81 ? 128 ASP B OD1 1 
ATOM   1020 O  OD2 . ASP A 1 128 ? -26.857 -29.758 5.575   1.00 21.06 ? 128 ASP B OD2 1 
ATOM   1021 N  N   . LYS A 1 129 ? -29.686 -34.096 5.134   1.00 17.68 ? 129 LYS B N   1 
ATOM   1022 C  CA  . LYS A 1 129 ? -30.238 -35.296 4.514   1.00 14.80 ? 129 LYS B CA  1 
ATOM   1023 C  C   . LYS A 1 129 ? -31.715 -35.448 4.518   1.00 16.72 ? 129 LYS B C   1 
ATOM   1024 O  O   . LYS A 1 129 ? -32.306 -36.144 3.659   1.00 17.28 ? 129 LYS B O   1 
ATOM   1025 C  CB  . LYS A 1 129 ? -29.634 -36.608 5.096   1.00 18.24 ? 129 LYS B CB  1 
ATOM   1026 C  CG  . LYS A 1 129 ? -28.167 -36.699 4.890   1.00 20.54 ? 129 LYS B CG  1 
ATOM   1027 C  CD  . LYS A 1 129 ? -27.599 -38.022 5.325   1.00 20.40 ? 129 LYS B CD  1 
ATOM   1028 C  CE  . LYS A 1 129 ? -28.338 -39.253 4.818   1.00 23.60 ? 129 LYS B CE  1 
ATOM   1029 N  NZ  . LYS A 1 129 ? -27.558 -40.465 5.160   1.00 22.66 ? 129 LYS B NZ  1 
ATOM   1030 N  N   . TYR A 1 130 ? -32.359 -34.928 5.566   1.00 16.57 ? 130 TYR B N   1 
ATOM   1031 C  CA  . TYR A 1 130 ? -33.777 -35.232 5.802   1.00 16.12 ? 130 TYR B CA  1 
ATOM   1032 C  C   . TYR A 1 130 ? -34.672 -33.999 5.759   1.00 13.81 ? 130 TYR B C   1 
ATOM   1033 O  O   . TYR A 1 130 ? -34.203 -32.903 5.980   1.00 16.10 ? 130 TYR B O   1 
ATOM   1034 C  CB  . TYR A 1 130 ? -33.889 -36.039 7.185   1.00 15.63 ? 130 TYR B CB  1 
ATOM   1035 C  CG  . TYR A 1 130 ? -33.016 -37.254 7.139   1.00 17.23 ? 130 TYR B CG  1 
ATOM   1036 C  CD1 . TYR A 1 130 ? -33.212 -38.225 6.175   1.00 16.30 ? 130 TYR B CD1 1 
ATOM   1037 C  CD2 . TYR A 1 130 ? -31.949 -37.445 8.043   1.00 16.28 ? 130 TYR B CD2 1 
ATOM   1038 C  CE1 . TYR A 1 130 ? -32.381 -39.324 6.078   1.00 19.26 ? 130 TYR B CE1 1 
ATOM   1039 C  CE2 . TYR A 1 130 ? -31.169 -38.561 8.009   1.00 16.85 ? 130 TYR B CE2 1 
ATOM   1040 C  CZ  . TYR A 1 130 ? -31.396 -39.521 7.035   1.00 16.47 ? 130 TYR B CZ  1 
ATOM   1041 O  OH  . TYR A 1 130 ? -30.534 -40.589 6.944   1.00 20.77 ? 130 TYR B OH  1 
ATOM   1042 N  N   . PRO A 1 131 ? -35.961 -34.166 5.429   1.00 16.60 ? 131 PRO B N   1 
ATOM   1043 C  CA  . PRO A 1 131 ? -36.832 -32.999 5.107   1.00 17.15 ? 131 PRO B CA  1 
ATOM   1044 C  C   . PRO A 1 131 ? -37.408 -32.346 6.338   1.00 15.74 ? 131 PRO B C   1 
ATOM   1045 O  O   . PRO A 1 131 ? -37.878 -31.251 6.250   1.00 16.24 ? 131 PRO B O   1 
ATOM   1046 C  CB  . PRO A 1 131 ? -37.993 -33.628 4.327   1.00 18.57 ? 131 PRO B CB  1 
ATOM   1047 C  CG  . PRO A 1 131 ? -38.038 -35.023 4.763   1.00 19.42 ? 131 PRO B CG  1 
ATOM   1048 C  CD  . PRO A 1 131 ? -36.560 -35.417 4.971   1.00 15.61 ? 131 PRO B CD  1 
ATOM   1049 N  N   . SER A 1 132 ? -37.396 -33.054 7.499   1.00 14.42 ? 132 SER B N   1 
ATOM   1050 C  CA  . SER A 1 132 ? -38.080 -32.505 8.670   1.00 14.70 ? 132 SER B CA  1 
ATOM   1051 C  C   . SER A 1 132 ? -37.471 -33.277 9.882   1.00 13.27 ? 132 SER B C   1 
ATOM   1052 O  O   . SER A 1 132 ? -36.951 -34.367 9.693   1.00 14.29 ? 132 SER B O   1 
ATOM   1053 C  CB  . SER A 1 132 ? -39.580 -32.854 8.676   1.00 15.27 ? 132 SER B CB  1 
ATOM   1054 O  OG  . SER A 1 132 ? -39.845 -34.225 8.622   1.00 17.84 ? 132 SER B OG  1 
ATOM   1055 N  N   . PHE A 1 133 ? -37.655 -32.663 11.045  1.00 16.49 ? 133 PHE B N   1 
ATOM   1056 C  CA  . PHE A 1 133 ? -37.261 -33.304 12.304  1.00 17.16 ? 133 PHE B CA  1 
ATOM   1057 C  C   . PHE A 1 133 ? -37.971 -34.658 12.442  1.00 17.69 ? 133 PHE B C   1 
ATOM   1058 O  O   . PHE A 1 133 ? -37.383 -35.685 12.811  1.00 15.48 ? 133 PHE B O   1 
ATOM   1059 C  CB  . PHE A 1 133 ? -37.711 -32.406 13.439  1.00 16.16 ? 133 PHE B CB  1 
ATOM   1060 C  CG  . PHE A 1 133 ? -37.601 -33.053 14.781  1.00 18.08 ? 133 PHE B CG  1 
ATOM   1061 C  CD1 . PHE A 1 133 ? -36.326 -33.308 15.321  1.00 19.04 ? 133 PHE B CD1 1 
ATOM   1062 C  CD2 . PHE A 1 133 ? -38.746 -33.471 15.444  1.00 24.21 ? 133 PHE B CD2 1 
ATOM   1063 C  CE1 . PHE A 1 133 ? -36.204 -33.879 16.590  1.00 19.10 ? 133 PHE B CE1 1 
ATOM   1064 C  CE2 . PHE A 1 133 ? -38.644 -34.060 16.733  1.00 23.46 ? 133 PHE B CE2 1 
ATOM   1065 C  CZ  . PHE A 1 133 ? -37.331 -34.263 17.275  1.00 24.84 ? 133 PHE B CZ  1 
ATOM   1066 N  N   . VAL A 1 134 ? -39.255 -34.713 12.113  1.00 17.14 ? 134 VAL B N   1 
ATOM   1067 C  CA  . VAL A 1 134 ? -40.025 -35.886 12.352  1.00 19.46 ? 134 VAL B CA  1 
ATOM   1068 C  C   . VAL A 1 134 ? -39.548 -37.025 11.474  1.00 18.46 ? 134 VAL B C   1 
ATOM   1069 O  O   . VAL A 1 134 ? -39.418 -38.144 11.916  1.00 20.38 ? 134 VAL B O   1 
ATOM   1070 C  CB  . VAL A 1 134 ? -41.561 -35.614 12.194  1.00 24.88 ? 134 VAL B CB  1 
ATOM   1071 C  CG1 . VAL A 1 134 ? -42.289 -36.933 12.358  1.00 27.59 ? 134 VAL B CG1 1 
ATOM   1072 C  CG2 . VAL A 1 134 ? -42.021 -34.682 13.303  1.00 28.04 ? 134 VAL B CG2 1 
ATOM   1073 N  N   A GLU A 1 135 ? -39.211 -36.743 10.205  0.50 17.85 ? 135 GLU B N   1 
ATOM   1074 N  N   B GLU A 1 135 ? -39.214 -36.715 10.217  0.50 16.57 ? 135 GLU B N   1 
ATOM   1075 C  CA  A GLU A 1 135 ? -38.583 -37.766 9.370   0.50 17.86 ? 135 GLU B CA  1 
ATOM   1076 C  CA  B GLU A 1 135 ? -38.629 -37.727 9.375   0.50 15.72 ? 135 GLU B CA  1 
ATOM   1077 C  C   A GLU A 1 135 ? -37.207 -38.215 9.897   0.50 15.97 ? 135 GLU B C   1 
ATOM   1078 C  C   B GLU A 1 135 ? -37.232 -38.194 9.880   0.50 14.94 ? 135 GLU B C   1 
ATOM   1079 O  O   A GLU A 1 135 ? -36.907 -39.380 9.920   0.50 18.75 ? 135 GLU B O   1 
ATOM   1080 O  O   B GLU A 1 135 ? -36.972 -39.361 9.921   0.50 17.38 ? 135 GLU B O   1 
ATOM   1081 C  CB  A GLU A 1 135 ? -38.418 -37.277 7.903   0.50 19.93 ? 135 GLU B CB  1 
ATOM   1082 C  CB  B GLU A 1 135 ? -38.612 -37.263 7.877   0.50 15.73 ? 135 GLU B CB  1 
ATOM   1083 C  CG  A GLU A 1 135 ? -37.547 -38.238 7.124   0.50 22.28 ? 135 GLU B CG  1 
ATOM   1084 C  CG  B GLU A 1 135 ? -38.513 -38.463 6.989   0.50 14.92 ? 135 GLU B CG  1 
ATOM   1085 C  CD  A GLU A 1 135 ? -38.211 -39.580 6.900   0.50 21.95 ? 135 GLU B CD  1 
ATOM   1086 C  CD  B GLU A 1 135 ? -37.124 -39.109 7.044   0.50 13.50 ? 135 GLU B CD  1 
ATOM   1087 O  OE1 A GLU A 1 135 ? -37.506 -40.612 6.918   0.50 24.24 ? 135 GLU B OE1 1 
ATOM   1088 O  OE1 B GLU A 1 135 ? -36.151 -38.324 7.119   0.50 12.31 ? 135 GLU B OE1 1 
ATOM   1089 O  OE2 A GLU A 1 135 ? -39.446 -39.588 6.760   0.50 23.46 ? 135 GLU B OE2 1 
ATOM   1090 O  OE2 B GLU A 1 135 ? -36.977 -40.370 7.016   0.50 14.70 ? 135 GLU B OE2 1 
ATOM   1091 N  N   . ALA A 1 136 ? -36.377 -37.243 10.244  1.00 15.20 ? 136 ALA B N   1 
ATOM   1092 C  CA  . ALA A 1 136 ? -35.010 -37.500 10.704  1.00 13.18 ? 136 ALA B CA  1 
ATOM   1093 C  C   . ALA A 1 136 ? -34.995 -38.389 11.986  1.00 13.98 ? 136 ALA B C   1 
ATOM   1094 O  O   . ALA A 1 136 ? -34.123 -39.234 12.148  1.00 14.47 ? 136 ALA B O   1 
ATOM   1095 C  CB  . ALA A 1 136 ? -34.309 -36.198 11.014  1.00 13.00 ? 136 ALA B CB  1 
ATOM   1096 N  N   . ALA A 1 137 ? -36.007 -38.197 12.801  1.00 14.53 ? 137 ALA B N   1 
ATOM   1097 C  CA  . ALA A 1 137 ? -36.162 -39.091 13.989  1.00 15.05 ? 137 ALA B CA  1 
ATOM   1098 C  C   . ALA A 1 137 ? -36.307 -40.569 13.697  1.00 15.71 ? 137 ALA B C   1 
ATOM   1099 O  O   . ALA A 1 137 ? -36.122 -41.397 14.633  1.00 14.43 ? 137 ALA B O   1 
ATOM   1100 C  CB  . ALA A 1 137 ? -37.317 -38.641 14.859  1.00 15.84 ? 137 ALA B CB  1 
ATOM   1101 N  N   . HIS A 1 138 ? -36.606 -40.989 12.446  1.00 15.96 ? 138 HIS B N   1 
ATOM   1102 C  CA  . HIS A 1 138 ? -36.690 -42.362 12.100  1.00 17.42 ? 138 HIS B CA  1 
ATOM   1103 C  C   . HIS A 1 138 ? -35.494 -42.859 11.296  1.00 18.04 ? 138 HIS B C   1 
ATOM   1104 O  O   . HIS A 1 138 ? -35.619 -43.862 10.585  1.00 23.21 ? 138 HIS B O   1 
ATOM   1105 C  CB  . HIS A 1 138 ? -37.988 -42.589 11.272  1.00 17.53 ? 138 HIS B CB  1 
ATOM   1106 C  CG  . HIS A 1 138 ? -39.242 -42.313 12.058  1.00 19.46 ? 138 HIS B CG  1 
ATOM   1107 N  ND1 . HIS A 1 138 ? -39.941 -43.294 12.685  1.00 25.02 ? 138 HIS B ND1 1 
ATOM   1108 C  CD2 . HIS A 1 138 ? -39.914 -41.137 12.315  1.00 19.71 ? 138 HIS B CD2 1 
ATOM   1109 C  CE1 . HIS A 1 138 ? -41.004 -42.766 13.301  1.00 23.73 ? 138 HIS B CE1 1 
ATOM   1110 N  NE2 . HIS A 1 138 ? -40.994 -41.472 13.111  1.00 21.51 ? 138 HIS B NE2 1 
ATOM   1111 N  N   . GLU A 1 139 ? -34.360 -42.157 11.361  1.00 18.16 ? 139 GLU B N   1 
ATOM   1112 C  CA  . GLU A 1 139 ? -33.221 -42.543 10.588  1.00 20.04 ? 139 GLU B CA  1 
ATOM   1113 C  C   . GLU A 1 139 ? -32.027 -42.712 11.527  1.00 18.43 ? 139 GLU B C   1 
ATOM   1114 O  O   . GLU A 1 139 ? -31.829 -41.869 12.370  1.00 17.34 ? 139 GLU B O   1 
ATOM   1115 C  CB  . GLU A 1 139 ? -32.914 -41.402 9.613   1.00 21.93 ? 139 GLU B CB  1 
ATOM   1116 C  CG  . GLU A 1 139 ? -34.049 -40.981 8.658   1.00 23.39 ? 139 GLU B CG  1 
ATOM   1117 C  CD  . GLU A 1 139 ? -34.246 -41.930 7.531   1.00 27.07 ? 139 GLU B CD  1 
ATOM   1118 O  OE1 . GLU A 1 139 ? -33.528 -42.912 7.511   1.00 26.75 ? 139 GLU B OE1 1 
ATOM   1119 O  OE2 . GLU A 1 139 ? -35.152 -41.676 6.629   1.00 28.00 ? 139 GLU B OE2 1 
ATOM   1120 N  N   . PRO A 1 140 ? -31.158 -43.726 11.344  1.00 20.14 ? 140 PRO B N   1 
ATOM   1121 C  CA  . PRO A 1 140 ? -29.994 -43.775 12.263  1.00 18.37 ? 140 PRO B CA  1 
ATOM   1122 C  C   . PRO A 1 140 ? -29.108 -42.600 12.477  1.00 19.14 ? 140 PRO B C   1 
ATOM   1123 O  O   . PRO A 1 140 ? -28.578 -42.468 13.617  1.00 18.91 ? 140 PRO B O   1 
ATOM   1124 C  CB  . PRO A 1 140 ? -29.193 -45.080 11.821  1.00 21.61 ? 140 PRO B CB  1 
ATOM   1125 C  CG  . PRO A 1 140 ? -30.300 -45.861 11.164  1.00 28.01 ? 140 PRO B CG  1 
ATOM   1126 C  CD  . PRO A 1 140 ? -31.041 -44.801 10.350  1.00 24.74 ? 140 PRO B CD  1 
ATOM   1127 N  N   . ASP A 1 141 ? -28.836 -41.794 11.433  1.00 14.03 ? 141 ASP B N   1 
ATOM   1128 C  CA  . ASP A 1 141 ? -27.974 -40.652 11.539  1.00 16.39 ? 141 ASP B CA  1 
ATOM   1129 C  C   . ASP A 1 141 ? -28.907 -39.452 11.536  1.00 13.44 ? 141 ASP B C   1 
ATOM   1130 O  O   . ASP A 1 141 ? -28.429 -38.329 11.253  1.00 14.91 ? 141 ASP B O   1 
ATOM   1131 C  CB  . ASP A 1 141 ? -27.086 -40.565 10.285  1.00 18.38 ? 141 ASP B CB  1 
ATOM   1132 C  CG  . ASP A 1 141 ? -27.877 -40.571 8.963   1.00 17.89 ? 141 ASP B CG  1 
ATOM   1133 O  OD1 . ASP A 1 141 ? -29.017 -40.979 8.890   1.00 17.87 ? 141 ASP B OD1 1 
ATOM   1134 O  OD2 . ASP A 1 141 ? -27.281 -40.147 7.937   1.00 20.88 ? 141 ASP B OD2 1 
ATOM   1135 N  N   . GLY A 1 142 ? -30.181 -39.627 11.973  1.00 15.17 ? 142 GLY B N   1 
ATOM   1136 C  CA  . GLY A 1 142 ? -31.136 -38.533 11.854  1.00 11.79 ? 142 GLY B CA  1 
ATOM   1137 C  C   . GLY A 1 142 ? -30.989 -37.398 12.936  1.00 12.37 ? 142 GLY B C   1 
ATOM   1138 O  O   . GLY A 1 142 ? -31.093 -36.184 12.708  1.00 11.77 ? 142 GLY B O   1 
ATOM   1139 N  N   . LEU A 1 143 ? -30.662 -37.833 14.195  1.00 12.30 ? 143 LEU B N   1 
ATOM   1140 C  CA  . LEU A 1 143 ? -30.693 -36.926 15.333  1.00 12.40 ? 143 LEU B CA  1 
ATOM   1141 C  C   . LEU A 1 143 ? -29.330 -36.842 16.051  1.00 10.70 ? 143 LEU B C   1 
ATOM   1142 O  O   . LEU A 1 143 ? -28.554 -37.849 16.067  1.00 13.02 ? 143 LEU B O   1 
ATOM   1143 C  CB  . LEU A 1 143 ? -31.747 -37.330 16.424  1.00 12.60 ? 143 LEU B CB  1 
ATOM   1144 C  CG  . LEU A 1 143 ? -33.155 -37.453 15.858  1.00 11.23 ? 143 LEU B CG  1 
ATOM   1145 C  CD1 . LEU A 1 143 ? -34.143 -37.800 17.005  1.00 9.72  ? 143 LEU B CD1 1 
ATOM   1146 C  CD2 . LEU A 1 143 ? -33.666 -36.145 15.198  1.00 11.10 ? 143 LEU B CD2 1 
ATOM   1147 N  N   . ALA A 1 144 ? -29.073 -35.726 16.630  1.00 11.55 ? 144 ALA B N   1 
ATOM   1148 C  CA  . ALA A 1 144 ? -27.879 -35.562 17.550  1.00 12.85 ? 144 ALA B CA  1 
ATOM   1149 C  C   . ALA A 1 144 ? -28.290 -34.827 18.752  1.00 12.49 ? 144 ALA B C   1 
ATOM   1150 O  O   . ALA A 1 144 ? -28.902 -33.750 18.648  1.00 12.32 ? 144 ALA B O   1 
ATOM   1151 C  CB  . ALA A 1 144 ? -26.760 -34.800 16.863  1.00 13.78 ? 144 ALA B CB  1 
ATOM   1152 N  N   . VAL A 1 145 ? -27.987 -35.377 19.951  1.00 13.24 ? 145 VAL B N   1 
ATOM   1153 C  CA  . VAL A 1 145 ? -28.487 -34.744 21.185  1.00 12.82 ? 145 VAL B CA  1 
ATOM   1154 C  C   . VAL A 1 145 ? -27.268 -34.469 22.029  1.00 11.94 ? 145 VAL B C   1 
ATOM   1155 O  O   . VAL A 1 145 ? -26.477 -35.415 22.256  1.00 12.77 ? 145 VAL B O   1 
ATOM   1156 C  CB  . VAL A 1 145 ? -29.522 -35.633 21.930  1.00 13.09 ? 145 VAL B CB  1 
ATOM   1157 C  CG1 . VAL A 1 145 ? -29.995 -34.823 23.154  1.00 10.02 ? 145 VAL B CG1 1 
ATOM   1158 C  CG2 . VAL A 1 145 ? -30.751 -35.896 21.013  1.00 14.35 ? 145 VAL B CG2 1 
ATOM   1159 N  N   . LEU A 1 146 ? -27.148 -33.231 22.495  1.00 12.15 ? 146 LEU B N   1 
ATOM   1160 C  CA  . LEU A 1 146 ? -26.100 -32.873 23.455  1.00 13.29 ? 146 LEU B CA  1 
ATOM   1161 C  C   . LEU A 1 146 ? -26.737 -33.084 24.819  1.00 15.65 ? 146 LEU B C   1 
ATOM   1162 O  O   . LEU A 1 146 ? -27.808 -32.539 25.085  1.00 15.40 ? 146 LEU B O   1 
ATOM   1163 C  CB  . LEU A 1 146 ? -25.761 -31.385 23.331  1.00 17.91 ? 146 LEU B CB  1 
ATOM   1164 C  CG  . LEU A 1 146 ? -24.425 -30.736 23.185  1.00 29.75 ? 146 LEU B CG  1 
ATOM   1165 C  CD1 . LEU A 1 146 ? -23.582 -31.551 22.175  1.00 26.40 ? 146 LEU B CD1 1 
ATOM   1166 C  CD2 . LEU A 1 146 ? -24.664 -29.361 22.591  1.00 26.74 ? 146 LEU B CD2 1 
ATOM   1167 N  N   . GLY A 1 147 ? -26.023 -33.780 25.720  1.00 14.38 ? 147 GLY B N   1 
ATOM   1168 C  CA  . GLY A 1 147 ? -26.425 -33.900 27.126  1.00 13.69 ? 147 GLY B CA  1 
ATOM   1169 C  C   . GLY A 1 147 ? -25.487 -33.045 28.016  1.00 12.49 ? 147 GLY B C   1 
ATOM   1170 O  O   . GLY A 1 147 ? -24.279 -33.217 27.819  1.00 13.08 ? 147 GLY B O   1 
ATOM   1171 N  N   . VAL A 1 148 ? -26.046 -32.322 28.969  1.00 11.54 ? 148 VAL B N   1 
ATOM   1172 C  CA  . VAL A 1 148 ? -25.245 -31.515 29.929  1.00 11.73 ? 148 VAL B CA  1 
ATOM   1173 C  C   . VAL A 1 148 ? -25.793 -31.984 31.275  1.00 12.22 ? 148 VAL B C   1 
ATOM   1174 O  O   . VAL A 1 148 ? -27.011 -31.866 31.561  1.00 12.00 ? 148 VAL B O   1 
ATOM   1175 C  CB  . VAL A 1 148 ? -25.403 -30.042 29.738  1.00 13.44 ? 148 VAL B CB  1 
ATOM   1176 C  CG1 . VAL A 1 148 ? -24.627 -29.233 30.825  1.00 15.53 ? 148 VAL B CG1 1 
ATOM   1177 C  CG2 . VAL A 1 148 ? -24.951 -29.691 28.292  1.00 14.84 ? 148 VAL B CG2 1 
ATOM   1178 N  N   . PHE A 1 149 ? -24.843 -32.401 32.167  1.00 10.71 ? 149 PHE B N   1 
ATOM   1179 C  CA  . PHE A 1 149 ? -25.276 -32.596 33.528  1.00 11.34 ? 149 PHE B CA  1 
ATOM   1180 C  C   . PHE A 1 149 ? -25.405 -31.378 34.389  1.00 11.28 ? 149 PHE B C   1 
ATOM   1181 O  O   . PHE A 1 149 ? -24.650 -30.406 34.221  1.00 13.75 ? 149 PHE B O   1 
ATOM   1182 C  CB  . PHE A 1 149 ? -24.180 -33.506 34.151  1.00 11.14 ? 149 PHE B CB  1 
ATOM   1183 C  CG  . PHE A 1 149 ? -24.022 -34.835 33.499  1.00 11.04 ? 149 PHE B CG  1 
ATOM   1184 C  CD1 . PHE A 1 149 ? -25.145 -35.784 33.470  1.00 11.22 ? 149 PHE B CD1 1 
ATOM   1185 C  CD2 . PHE A 1 149 ? -22.753 -35.257 32.942  1.00 10.98 ? 149 PHE B CD2 1 
ATOM   1186 C  CE1 . PHE A 1 149 ? -24.926 -37.033 32.924  1.00 11.80 ? 149 PHE B CE1 1 
ATOM   1187 C  CE2 . PHE A 1 149 ? -22.587 -36.489 32.391  1.00 11.67 ? 149 PHE B CE2 1 
ATOM   1188 C  CZ  . PHE A 1 149 ? -23.689 -37.378 32.327  1.00 10.76 ? 149 PHE B CZ  1 
ATOM   1189 N  N   . LEU A 1 150 ? -26.334 -31.408 35.327  1.00 12.31 ? 150 LEU B N   1 
ATOM   1190 C  CA  . LEU A 1 150 ? -26.500 -30.333 36.312  1.00 13.75 ? 150 LEU B CA  1 
ATOM   1191 C  C   . LEU A 1 150 ? -26.231 -30.952 37.687  1.00 15.14 ? 150 LEU B C   1 
ATOM   1192 O  O   . LEU A 1 150 ? -26.876 -31.857 38.084  1.00 14.31 ? 150 LEU B O   1 
ATOM   1193 C  CB  . LEU A 1 150 ? -27.895 -29.696 36.306  1.00 14.27 ? 150 LEU B CB  1 
ATOM   1194 C  CG  . LEU A 1 150 ? -28.255 -28.807 35.080  1.00 15.58 ? 150 LEU B CG  1 
ATOM   1195 C  CD1 . LEU A 1 150 ? -28.543 -29.744 33.861  1.00 17.73 ? 150 LEU B CD1 1 
ATOM   1196 C  CD2 . LEU A 1 150 ? -29.552 -27.998 35.345  1.00 15.85 ? 150 LEU B CD2 1 
ATOM   1197 N  N   . GLN A 1 151 ? -25.311 -30.318 38.425  1.00 14.28 ? 151 GLN B N   1 
ATOM   1198 C  CA  . GLN A 1 151 ? -24.964 -30.743 39.780  1.00 14.32 ? 151 GLN B CA  1 
ATOM   1199 C  C   . GLN A 1 151 ? -25.433 -29.705 40.759  1.00 15.41 ? 151 GLN B C   1 
ATOM   1200 O  O   . GLN A 1 151 ? -25.527 -28.539 40.404  1.00 17.36 ? 151 GLN B O   1 
ATOM   1201 C  CB  . GLN A 1 151 ? -23.456 -30.927 39.842  1.00 15.26 ? 151 GLN B CB  1 
ATOM   1202 C  CG  . GLN A 1 151 ? -22.721 -29.612 39.815  1.00 19.15 ? 151 GLN B CG  1 
ATOM   1203 C  CD  . GLN A 1 151 ? -21.218 -29.746 39.865  1.00 22.97 ? 151 GLN B CD  1 
ATOM   1204 O  OE1 . GLN A 1 151 ? -20.651 -30.853 40.098  1.00 22.51 ? 151 GLN B OE1 1 
ATOM   1205 N  NE2 . GLN A 1 151 ? -20.548 -28.604 39.706  1.00 25.87 ? 151 GLN B NE2 1 
ATOM   1206 N  N   . ILE A 1 152 ? -25.818 -30.127 41.976  1.00 15.73 ? 152 ILE B N   1 
ATOM   1207 C  CA  . ILE A 1 152 ? -26.251 -29.128 42.953  1.00 17.09 ? 152 ILE B CA  1 
ATOM   1208 C  C   . ILE A 1 152 ? -25.068 -28.222 43.301  1.00 19.61 ? 152 ILE B C   1 
ATOM   1209 O  O   . ILE A 1 152 ? -23.948 -28.724 43.557  1.00 21.12 ? 152 ILE B O   1 
ATOM   1210 C  CB  . ILE A 1 152 ? -26.763 -29.823 44.238  1.00 17.25 ? 152 ILE B CB  1 
ATOM   1211 C  CG1 . ILE A 1 152 ? -28.058 -30.598 43.890  1.00 16.88 ? 152 ILE B CG1 1 
ATOM   1212 C  CG2 . ILE A 1 152 ? -27.215 -28.806 45.308  1.00 17.63 ? 152 ILE B CG2 1 
ATOM   1213 C  CD1 . ILE A 1 152 ? -29.237 -29.762 43.334  1.00 18.99 ? 152 ILE B CD1 1 
ATOM   1214 N  N   . GLY A 1 153 ? -25.266 -26.918 43.159  1.00 18.04 ? 153 GLY B N   1 
ATOM   1215 C  CA  . GLY A 1 153 ? -24.204 -26.003 43.584  1.00 21.22 ? 153 GLY B CA  1 
ATOM   1216 C  C   . GLY A 1 153 ? -24.824 -24.626 43.656  1.00 18.69 ? 153 GLY B C   1 
ATOM   1217 O  O   . GLY A 1 153 ? -25.998 -24.468 44.005  1.00 23.79 ? 153 GLY B O   1 
ATOM   1218 N  N   . GLU A 1 154 ? -24.011 -23.655 43.360  1.00 23.80 ? 154 GLU B N   1 
ATOM   1219 C  CA  . GLU A 1 154 ? -24.533 -22.314 43.663  1.00 25.09 ? 154 GLU B CA  1 
ATOM   1220 C  C   . GLU A 1 154 ? -25.528 -21.994 42.564  1.00 22.11 ? 154 GLU B C   1 
ATOM   1221 O  O   . GLU A 1 154 ? -25.450 -22.642 41.519  1.00 22.36 ? 154 GLU B O   1 
ATOM   1222 C  CB  . GLU A 1 154 ? -23.387 -21.328 43.950  1.00 30.17 ? 154 GLU B CB  1 
ATOM   1223 C  CG  . GLU A 1 154 ? -22.868 -21.477 45.432  1.00 29.28 ? 154 GLU B CG  1 
ATOM   1224 C  CD  . GLU A 1 154 ? -21.366 -21.121 45.598  1.00 33.53 ? 154 GLU B CD  1 
ATOM   1225 O  OE1 . GLU A 1 154 ? -20.927 -20.754 46.734  1.00 34.83 ? 154 GLU B OE1 1 
ATOM   1226 O  OE2 . GLU A 1 154 ? -20.587 -21.176 44.607  1.00 39.51 ? 154 GLU B OE2 1 
ATOM   1227 N  N   . PRO A 1 155 ? -26.519 -21.109 42.814  1.00 20.78 ? 155 PRO B N   1 
ATOM   1228 C  CA  . PRO A 1 155 ? -27.555 -20.988 41.745  1.00 19.43 ? 155 PRO B CA  1 
ATOM   1229 C  C   . PRO A 1 155 ? -26.976 -20.490 40.425  1.00 19.91 ? 155 PRO B C   1 
ATOM   1230 O  O   . PRO A 1 155 ? -26.016 -19.738 40.359  1.00 19.76 ? 155 PRO B O   1 
ATOM   1231 C  CB  . PRO A 1 155 ? -28.568 -19.954 42.279  1.00 20.24 ? 155 PRO B CB  1 
ATOM   1232 C  CG  . PRO A 1 155 ? -27.914 -19.375 43.509  1.00 18.67 ? 155 PRO B CG  1 
ATOM   1233 C  CD  . PRO A 1 155 ? -26.841 -20.289 44.005  1.00 18.81 ? 155 PRO B CD  1 
ATOM   1234 N  N   . ASN A 1 156 ? -27.641 -20.909 39.359  1.00 17.61 ? 156 ASN B N   1 
ATOM   1235 C  CA  . ASN A 1 156 ? -27.193 -20.614 38.035  1.00 19.64 ? 156 ASN B CA  1 
ATOM   1236 C  C   . ASN A 1 156 ? -28.067 -19.535 37.383  1.00 18.44 ? 156 ASN B C   1 
ATOM   1237 O  O   . ASN A 1 156 ? -29.257 -19.757 37.038  1.00 18.40 ? 156 ASN B O   1 
ATOM   1238 C  CB  . ASN A 1 156 ? -27.289 -21.867 37.210  1.00 18.97 ? 156 ASN B CB  1 
ATOM   1239 C  CG  . ASN A 1 156 ? -26.535 -21.760 35.877  1.00 21.68 ? 156 ASN B CG  1 
ATOM   1240 O  OD1 . ASN A 1 156 ? -26.364 -20.668 35.259  1.00 21.84 ? 156 ASN B OD1 1 
ATOM   1241 N  ND2 . ASN A 1 156 ? -26.067 -22.893 35.416  1.00 17.68 ? 156 ASN B ND2 1 
ATOM   1242 N  N   . SER A 1 157 ? -27.457 -18.353 37.206  1.00 22.90 ? 157 SER B N   1 
ATOM   1243 C  CA  . SER A 1 157 ? -28.261 -17.170 36.693  1.00 21.78 ? 157 SER B CA  1 
ATOM   1244 C  C   . SER A 1 157 ? -28.793 -17.405 35.282  1.00 22.62 ? 157 SER B C   1 
ATOM   1245 O  O   . SER A 1 157 ? -29.784 -16.745 34.826  1.00 22.90 ? 157 SER B O   1 
ATOM   1246 C  CB  . SER A 1 157 ? -27.413 -15.878 36.666  1.00 25.62 ? 157 SER B CB  1 
ATOM   1247 O  OG  . SER A 1 157 ? -26.150 -16.218 36.093  1.00 29.31 ? 157 SER B OG  1 
ATOM   1248 N  N   . GLN A 1 158 ? -28.152 -18.346 34.572  1.00 19.91 ? 158 GLN B N   1 
ATOM   1249 C  CA  . GLN A 1 158 ? -28.545 -18.593 33.179  1.00 20.21 ? 158 GLN B CA  1 
ATOM   1250 C  C   . GLN A 1 158 ? -29.750 -19.439 33.093  1.00 20.97 ? 158 GLN B C   1 
ATOM   1251 O  O   . GLN A 1 158 ? -30.272 -19.662 32.000  1.00 23.42 ? 158 GLN B O   1 
ATOM   1252 C  CB  . GLN A 1 158 ? -27.419 -19.272 32.432  1.00 22.73 ? 158 GLN B CB  1 
ATOM   1253 C  CG  . GLN A 1 158 ? -26.103 -18.494 32.418  1.00 26.41 ? 158 GLN B CG  1 
ATOM   1254 C  CD  . GLN A 1 158 ? -26.228 -17.103 31.791  1.00 32.46 ? 158 GLN B CD  1 
ATOM   1255 O  OE1 . GLN A 1 158 ? -27.034 -16.890 30.868  1.00 36.95 ? 158 GLN B OE1 1 
ATOM   1256 N  NE2 . GLN A 1 158 ? -25.412 -16.168 32.255  1.00 39.59 ? 158 GLN B NE2 1 
ATOM   1257 N  N   . LEU A 1 159 ? -30.224 -19.983 34.208  1.00 21.68 ? 159 LEU B N   1 
ATOM   1258 C  CA  . LEU A 1 159 ? -31.529 -20.649 34.196  1.00 20.72 ? 159 LEU B CA  1 
ATOM   1259 C  C   . LEU A 1 159 ? -32.723 -19.685 34.401  1.00 18.99 ? 159 LEU B C   1 
ATOM   1260 O  O   . LEU A 1 159 ? -33.869 -20.143 34.334  1.00 19.25 ? 159 LEU B O   1 
ATOM   1261 C  CB  . LEU A 1 159 ? -31.567 -21.741 35.271  1.00 20.62 ? 159 LEU B CB  1 
ATOM   1262 C  CG  . LEU A 1 159 ? -30.644 -22.913 34.934  1.00 19.93 ? 159 LEU B CG  1 
ATOM   1263 C  CD1 . LEU A 1 159 ? -30.627 -23.778 36.161  1.00 21.18 ? 159 LEU B CD1 1 
ATOM   1264 C  CD2 . LEU A 1 159 ? -31.127 -23.743 33.731  1.00 21.37 ? 159 LEU B CD2 1 
ATOM   1265 N  N   . GLN A 1 160 ? -32.486 -18.389 34.744  1.00 20.06 ? 160 GLN B N   1 
ATOM   1266 C  CA  . GLN A 1 160 ? -33.560 -17.470 35.073  1.00 20.47 ? 160 GLN B CA  1 
ATOM   1267 C  C   . GLN A 1 160 ? -34.601 -17.325 33.971  1.00 19.82 ? 160 GLN B C   1 
ATOM   1268 O  O   . GLN A 1 160 ? -35.788 -17.245 34.270  1.00 20.55 ? 160 GLN B O   1 
ATOM   1269 C  CB  . GLN A 1 160 ? -33.022 -16.057 35.457  1.00 23.01 ? 160 GLN B CB  1 
ATOM   1270 C  CG  . GLN A 1 160 ? -34.134 -15.180 35.987  1.00 22.35 ? 160 GLN B CG  1 
ATOM   1271 C  CD  . GLN A 1 160 ? -33.842 -13.706 35.980  1.00 28.09 ? 160 GLN B CD  1 
ATOM   1272 O  OE1 . GLN A 1 160 ? -32.684 -13.276 36.000  1.00 31.73 ? 160 GLN B OE1 1 
ATOM   1273 N  NE2 . GLN A 1 160 ? -34.909 -12.901 35.991  1.00 27.22 ? 160 GLN B NE2 1 
ATOM   1274 N  N   . LYS A 1 161 ? -34.153 -17.223 32.735  1.00 21.43 ? 161 LYS B N   1 
ATOM   1275 C  CA  . LYS A 1 161 ? -35.170 -16.984 31.706  1.00 19.84 ? 161 LYS B CA  1 
ATOM   1276 C  C   . LYS A 1 161 ? -36.161 -18.153 31.695  1.00 20.08 ? 161 LYS B C   1 
ATOM   1277 O  O   . LYS A 1 161 ? -37.377 -17.956 31.673  1.00 20.05 ? 161 LYS B O   1 
ATOM   1278 C  CB  . LYS A 1 161 ? -34.540 -16.798 30.356  1.00 23.22 ? 161 LYS B CB  1 
ATOM   1279 C  CG  . LYS A 1 161 ? -35.554 -16.239 29.312  1.00 21.92 ? 161 LYS B CG  1 
ATOM   1280 C  CD  . LYS A 1 161 ? -34.897 -16.231 27.914  1.00 20.68 ? 161 LYS B CD  1 
ATOM   1281 C  CE  . LYS A 1 161 ? -35.945 -16.003 26.828  1.00 20.86 ? 161 LYS B CE  1 
ATOM   1282 N  NZ  . LYS A 1 161 ? -36.496 -14.556 27.000  1.00 23.55 ? 161 LYS B NZ  1 
ATOM   1283 N  N   . ILE A 1 162 ? -35.627 -19.358 31.889  1.00 18.98 ? 162 ILE B N   1 
ATOM   1284 C  CA  . ILE A 1 162 ? -36.541 -20.535 31.984  1.00 15.60 ? 162 ILE B CA  1 
ATOM   1285 C  C   . ILE A 1 162 ? -37.456 -20.513 33.250  1.00 16.85 ? 162 ILE B C   1 
ATOM   1286 O  O   . ILE A 1 162 ? -38.675 -20.727 33.210  1.00 18.08 ? 162 ILE B O   1 
ATOM   1287 C  CB  . ILE A 1 162 ? -35.721 -21.861 31.955  1.00 13.85 ? 162 ILE B CB  1 
ATOM   1288 C  CG1 . ILE A 1 162 ? -35.019 -21.954 30.587  1.00 14.10 ? 162 ILE B CG1 1 
ATOM   1289 C  CG2 . ILE A 1 162 ? -36.719 -23.001 32.139  1.00 13.99 ? 162 ILE B CG2 1 
ATOM   1290 C  CD1 . ILE A 1 162 ? -34.020 -23.108 30.460  1.00 14.30 ? 162 ILE B CD1 1 
ATOM   1291 N  N   . THR A 1 163 ? -36.821 -20.354 34.412  1.00 17.04 ? 163 THR B N   1 
ATOM   1292 C  CA  . THR A 1 163 ? -37.586 -20.525 35.651  1.00 19.15 ? 163 THR B CA  1 
ATOM   1293 C  C   . THR A 1 163 ? -38.673 -19.460 35.802  1.00 17.16 ? 163 THR B C   1 
ATOM   1294 O  O   . THR A 1 163 ? -39.698 -19.769 36.387  1.00 19.20 ? 163 THR B O   1 
ATOM   1295 C  CB  . THR A 1 163 ? -36.657 -20.508 36.892  1.00 18.82 ? 163 THR B CB  1 
ATOM   1296 O  OG1 . THR A 1 163 ? -35.864 -19.315 36.906  1.00 20.96 ? 163 THR B OG1 1 
ATOM   1297 C  CG2 . THR A 1 163 ? -35.741 -21.813 36.850  1.00 19.77 ? 163 THR B CG2 1 
ATOM   1298 N  N   . ASP A 1 164 ? -38.408 -18.251 35.315  1.00 19.33 ? 164 ASP B N   1 
ATOM   1299 C  CA  . ASP A 1 164 ? -39.386 -17.143 35.281  1.00 18.26 ? 164 ASP B CA  1 
ATOM   1300 C  C   . ASP A 1 164 ? -40.648 -17.501 34.522  1.00 20.44 ? 164 ASP B C   1 
ATOM   1301 O  O   . ASP A 1 164 ? -41.694 -16.887 34.746  1.00 23.22 ? 164 ASP B O   1 
ATOM   1302 C  CB  . ASP A 1 164 ? -38.752 -15.931 34.632  1.00 20.85 ? 164 ASP B CB  1 
ATOM   1303 C  CG  . ASP A 1 164 ? -37.940 -15.062 35.593  1.00 26.17 ? 164 ASP B CG  1 
ATOM   1304 O  OD1 . ASP A 1 164 ? -37.867 -15.404 36.798  1.00 29.64 ? 164 ASP B OD1 1 
ATOM   1305 O  OD2 . ASP A 1 164 ? -37.339 -14.058 35.096  1.00 26.21 ? 164 ASP B OD2 1 
ATOM   1306 N  N   . THR A 1 165 ? -40.598 -18.510 33.623  1.00 19.98 ? 165 THR B N   1 
ATOM   1307 C  CA  . THR A 1 165 ? -41.772 -18.832 32.811  1.00 18.28 ? 165 THR B CA  1 
ATOM   1308 C  C   . THR A 1 165 ? -42.568 -19.981 33.378  1.00 19.23 ? 165 THR B C   1 
ATOM   1309 O  O   . THR A 1 165 ? -43.670 -20.293 32.906  1.00 20.42 ? 165 THR B O   1 
ATOM   1310 C  CB  . THR A 1 165 ? -41.404 -19.251 31.373  1.00 19.29 ? 165 THR B CB  1 
ATOM   1311 O  OG1 . THR A 1 165 ? -40.804 -20.578 31.377  1.00 20.57 ? 165 THR B OG1 1 
ATOM   1312 C  CG2 . THR A 1 165 ? -40.548 -18.229 30.741  1.00 19.79 ? 165 THR B CG2 1 
ATOM   1313 N  N   . LEU A 1 166 ? -42.079 -20.649 34.429  1.00 17.52 ? 166 LEU B N   1 
ATOM   1314 C  CA  . LEU A 1 166 ? -42.717 -21.872 34.837  1.00 16.92 ? 166 LEU B CA  1 
ATOM   1315 C  C   . LEU A 1 166 ? -44.138 -21.764 35.381  1.00 19.51 ? 166 LEU B C   1 
ATOM   1316 O  O   . LEU A 1 166 ? -44.985 -22.614 35.063  1.00 20.60 ? 166 LEU B O   1 
ATOM   1317 C  CB  . LEU A 1 166 ? -41.839 -22.782 35.772  1.00 17.89 ? 166 LEU B CB  1 
ATOM   1318 C  CG  . LEU A 1 166 ? -40.433 -23.147 35.278  1.00 19.20 ? 166 LEU B CG  1 
ATOM   1319 C  CD1 . LEU A 1 166 ? -39.569 -23.793 36.422  1.00 19.22 ? 166 LEU B CD1 1 
ATOM   1320 C  CD2 . LEU A 1 166 ? -40.484 -24.038 34.048  1.00 21.46 ? 166 LEU B CD2 1 
ATOM   1321 N  N   . ASP A 1 167 ? -44.434 -20.660 36.065  1.00 20.74 ? 167 ASP B N   1 
ATOM   1322 C  CA  . ASP A 1 167 ? -45.835 -20.521 36.569  1.00 21.31 ? 167 ASP B CA  1 
ATOM   1323 C  C   . ASP A 1 167 ? -46.760 -20.414 35.376  1.00 23.21 ? 167 ASP B C   1 
ATOM   1324 O  O   . ASP A 1 167 ? -47.835 -21.050 35.361  1.00 24.93 ? 167 ASP B O   1 
ATOM   1325 C  CB  . ASP A 1 167 ? -45.927 -19.263 37.425  1.00 25.57 ? 167 ASP B CB  1 
ATOM   1326 C  CG  . ASP A 1 167 ? -45.353 -19.487 38.825  1.00 30.26 ? 167 ASP B CG  1 
ATOM   1327 O  OD1 . ASP A 1 167 ? -45.198 -20.674 39.284  1.00 34.37 ? 167 ASP B OD1 1 
ATOM   1328 O  OD2 . ASP A 1 167 ? -45.044 -18.459 39.468  1.00 38.03 ? 167 ASP B OD2 1 
ATOM   1329 N  N   . SER A 1 168 ? -46.299 -19.685 34.364  1.00 20.85 ? 168 SER B N   1 
ATOM   1330 C  CA  . SER A 1 168 ? -47.144 -19.523 33.156  1.00 21.24 ? 168 SER B CA  1 
ATOM   1331 C  C   . SER A 1 168 ? -47.382 -20.810 32.372  1.00 21.06 ? 168 SER B C   1 
ATOM   1332 O  O   . SER A 1 168 ? -48.361 -20.892 31.558  1.00 21.78 ? 168 SER B O   1 
ATOM   1333 C  CB  . SER A 1 168 ? -46.582 -18.410 32.254  1.00 24.17 ? 168 SER B CB  1 
ATOM   1334 O  OG  . SER A 1 168 ? -45.440 -18.851 31.524  1.00 26.21 ? 168 SER B OG  1 
ATOM   1335 N  N   . ILE A 1 169 ? -46.505 -21.805 32.521  1.00 17.99 ? 169 ILE B N   1 
ATOM   1336 C  CA  . ILE A 1 169 ? -46.725 -23.081 31.806  1.00 17.13 ? 169 ILE B CA  1 
ATOM   1337 C  C   . ILE A 1 169 ? -46.957 -24.216 32.792  1.00 16.14 ? 169 ILE B C   1 
ATOM   1338 O  O   . ILE A 1 169 ? -46.624 -25.362 32.560  1.00 17.19 ? 169 ILE B O   1 
ATOM   1339 C  CB  . ILE A 1 169 ? -45.625 -23.429 30.774  1.00 18.01 ? 169 ILE B CB  1 
ATOM   1340 C  CG1 . ILE A 1 169 ? -44.241 -23.554 31.418  1.00 17.19 ? 169 ILE B CG1 1 
ATOM   1341 C  CG2 . ILE A 1 169 ? -45.608 -22.348 29.717  1.00 18.18 ? 169 ILE B CG2 1 
ATOM   1342 C  CD1 . ILE A 1 169 ? -43.219 -24.261 30.500  1.00 16.97 ? 169 ILE B CD1 1 
ATOM   1343 N  N   . LYS A 1 170 ? -47.621 -23.914 33.945  1.00 16.59 ? 170 LYS B N   1 
ATOM   1344 C  CA  . LYS A 1 170 ? -47.828 -24.949 34.930  1.00 17.20 ? 170 LYS B CA  1 
ATOM   1345 C  C   . LYS A 1 170 ? -48.556 -26.181 34.470  1.00 14.97 ? 170 LYS B C   1 
ATOM   1346 O  O   . LYS A 1 170 ? -48.146 -27.304 34.774  1.00 17.90 ? 170 LYS B O   1 
ATOM   1347 C  CB  . LYS A 1 170 ? -48.578 -24.347 36.147  1.00 21.18 ? 170 LYS B CB  1 
ATOM   1348 C  CG  . LYS A 1 170 ? -48.733 -25.308 37.316  1.00 25.05 ? 170 LYS B CG  1 
ATOM   1349 C  CD  . LYS A 1 170 ? -49.388 -24.606 38.523  1.00 31.77 ? 170 LYS B CD  1 
ATOM   1350 C  CE  . LYS A 1 170 ? -49.404 -25.483 39.816  1.00 35.24 ? 170 LYS B CE  1 
ATOM   1351 N  NZ  . LYS A 1 170 ? -48.096 -25.993 40.427  1.00 29.62 ? 170 LYS B NZ  1 
ATOM   1352 N  N   . GLU A 1 171 ? -49.633 -26.027 33.653  1.00 17.17 ? 171 GLU B N   1 
ATOM   1353 C  CA  . GLU A 1 171 ? -50.426 -27.162 33.236  1.00 16.19 ? 171 GLU B CA  1 
ATOM   1354 C  C   . GLU A 1 171 ? -49.933 -27.657 31.908  1.00 15.72 ? 171 GLU B C   1 
ATOM   1355 O  O   . GLU A 1 171 ? -49.481 -26.805 31.081  1.00 17.49 ? 171 GLU B O   1 
ATOM   1356 C  CB  . GLU A 1 171 ? -51.934 -26.770 33.087  1.00 19.72 ? 171 GLU B CB  1 
ATOM   1357 C  CG  . GLU A 1 171 ? -52.593 -26.192 34.372  1.00 23.07 ? 171 GLU B CG  1 
ATOM   1358 C  CD  . GLU A 1 171 ? -52.195 -24.734 34.739  1.00 27.70 ? 171 GLU B CD  1 
ATOM   1359 O  OE1 . GLU A 1 171 ? -52.511 -24.303 35.883  1.00 42.76 ? 171 GLU B OE1 1 
ATOM   1360 O  OE2 . GLU A 1 171 ? -51.582 -23.945 33.992  1.00 27.21 ? 171 GLU B OE2 1 
ATOM   1361 N  N   . LYS A 1 172 ? -50.045 -28.949 31.688  1.00 16.79 ? 172 LYS B N   1 
ATOM   1362 C  CA  . LYS A 1 172 ? -49.782 -29.589 30.363  1.00 14.97 ? 172 LYS B CA  1 
ATOM   1363 C  C   . LYS A 1 172 ? -50.527 -28.825 29.249  1.00 16.87 ? 172 LYS B C   1 
ATOM   1364 O  O   . LYS A 1 172 ? -51.749 -28.589 29.374  1.00 17.79 ? 172 LYS B O   1 
ATOM   1365 C  CB  . LYS A 1 172 ? -50.204 -31.052 30.377  1.00 17.55 ? 172 LYS B CB  1 
ATOM   1366 C  CG  . LYS A 1 172 ? -49.892 -31.772 29.098  1.00 17.87 ? 172 LYS B CG  1 
ATOM   1367 C  CD  . LYS A 1 172 ? -50.354 -33.227 29.167  1.00 20.86 ? 172 LYS B CD  1 
ATOM   1368 C  CE  . LYS A 1 172 ? -50.036 -33.882 27.850  1.00 21.70 ? 172 LYS B CE  1 
ATOM   1369 N  NZ  . LYS A 1 172 ? -50.137 -35.381 28.051  1.00 31.15 ? 172 LYS B NZ  1 
ATOM   1370 N  N   . GLY A 1 173 ? -49.764 -28.502 28.195  1.00 15.35 ? 173 GLY B N   1 
ATOM   1371 C  CA  . GLY A 1 173 ? -50.277 -27.914 26.949  1.00 16.27 ? 173 GLY B CA  1 
ATOM   1372 C  C   . GLY A 1 173 ? -50.162 -26.429 26.948  1.00 18.07 ? 173 GLY B C   1 
ATOM   1373 O  O   . GLY A 1 173 ? -50.258 -25.785 25.881  1.00 19.57 ? 173 GLY B O   1 
ATOM   1374 N  N   . LYS A 1 174 ? -49.882 -25.794 28.095  1.00 17.24 ? 174 LYS B N   1 
ATOM   1375 C  CA  . LYS A 1 174 ? -49.627 -24.396 28.097  1.00 15.09 ? 174 LYS B CA  1 
ATOM   1376 C  C   . LYS A 1 174 ? -48.337 -24.025 27.370  1.00 15.79 ? 174 LYS B C   1 
ATOM   1377 O  O   . LYS A 1 174 ? -47.374 -24.767 27.420  1.00 15.99 ? 174 LYS B O   1 
ATOM   1378 C  CB  . LYS A 1 174 ? -49.527 -23.805 29.515  1.00 19.92 ? 174 LYS B CB  1 
ATOM   1379 C  CG  . LYS A 1 174 ? -50.861 -23.979 30.284  1.00 25.73 ? 174 LYS B CG  1 
ATOM   1380 C  CD  . LYS A 1 174 ? -51.753 -22.789 29.939  1.00 28.28 ? 174 LYS B CD  1 
ATOM   1381 C  CE  . LYS A 1 174 ? -53.102 -22.862 30.670  1.00 33.78 ? 174 LYS B CE  1 
ATOM   1382 N  NZ  . LYS A 1 174 ? -52.849 -22.671 32.128  1.00 40.60 ? 174 LYS B NZ  1 
ATOM   1383 N  N   . GLN A 1 175 ? -48.349 -22.863 26.766  1.00 15.35 ? 175 GLN B N   1 
ATOM   1384 C  CA  . GLN A 1 175 ? -47.170 -22.332 26.075  1.00 16.42 ? 175 GLN B CA  1 
ATOM   1385 C  C   . GLN A 1 175 ? -46.996 -20.817 26.284  1.00 18.48 ? 175 GLN B C   1 
ATOM   1386 O  O   . GLN A 1 175 ? -47.974 -20.038 26.589  1.00 20.21 ? 175 GLN B O   1 
ATOM   1387 C  CB  . GLN A 1 175 ? -47.070 -22.697 24.603  1.00 18.10 ? 175 GLN B CB  1 
ATOM   1388 C  CG  . GLN A 1 175 ? -47.954 -21.833 23.710  1.00 20.41 ? 175 GLN B CG  1 
ATOM   1389 C  CD  . GLN A 1 175 ? -47.960 -22.366 22.293  1.00 19.43 ? 175 GLN B CD  1 
ATOM   1390 O  OE1 . GLN A 1 175 ? -48.149 -23.557 22.087  1.00 22.17 ? 175 GLN B OE1 1 
ATOM   1391 N  NE2 . GLN A 1 175 ? -47.720 -21.471 21.294  1.00 22.27 ? 175 GLN B NE2 1 
ATOM   1392 N  N   A THR A 1 176 ? -45.781 -20.367 26.082  0.50 16.02 ? 176 THR B N   1 
ATOM   1393 N  N   B THR A 1 176 ? -45.771 -20.352 26.217  0.50 16.02 ? 176 THR B N   1 
ATOM   1394 C  CA  A THR A 1 176 ? -45.556 -18.928 26.114  0.50 16.87 ? 176 THR B CA  1 
ATOM   1395 C  CA  B THR A 1 176 ? -45.557 -18.894 26.211  0.50 16.95 ? 176 THR B CA  1 
ATOM   1396 C  C   A THR A 1 176 ? -44.349 -18.480 25.334  0.50 17.50 ? 176 THR B C   1 
ATOM   1397 C  C   B THR A 1 176 ? -44.462 -18.535 25.245  0.50 17.94 ? 176 THR B C   1 
ATOM   1398 O  O   A THR A 1 176 ? -43.386 -19.210 25.150  0.50 15.37 ? 176 THR B O   1 
ATOM   1399 O  O   B THR A 1 176 ? -43.697 -19.422 24.836  0.50 16.71 ? 176 THR B O   1 
ATOM   1400 C  CB  A THR A 1 176 ? -45.538 -18.388 27.557  0.50 21.08 ? 176 THR B CB  1 
ATOM   1401 C  CB  B THR A 1 176 ? -45.370 -18.236 27.629  0.50 20.96 ? 176 THR B CB  1 
ATOM   1402 O  OG1 A THR A 1 176 ? -45.652 -16.936 27.517  0.50 18.74 ? 176 THR B OG1 1 
ATOM   1403 O  OG1 B THR A 1 176 ? -44.000 -17.928 27.913  0.50 20.45 ? 176 THR B OG1 1 
ATOM   1404 C  CG2 A THR A 1 176 ? -44.308 -18.878 28.282  0.50 17.43 ? 176 THR B CG2 1 
ATOM   1405 C  CG2 B THR A 1 176 ? -46.097 -18.973 28.760  0.50 15.57 ? 176 THR B CG2 1 
ATOM   1406 N  N   . ARG A 1 177 ? -44.411 -17.271 24.841  1.00 15.75 ? 177 ARG B N   1 
ATOM   1407 C  CA  . ARG A 1 177 ? -43.399 -16.780 23.971  1.00 16.04 ? 177 ARG B CA  1 
ATOM   1408 C  C   . ARG A 1 177 ? -42.001 -16.897 24.629  1.00 18.44 ? 177 ARG B C   1 
ATOM   1409 O  O   . ARG A 1 177 ? -41.869 -16.619 25.840  1.00 20.79 ? 177 ARG B O   1 
ATOM   1410 C  CB  . ARG A 1 177 ? -43.651 -15.286 23.758  1.00 18.20 ? 177 ARG B CB  1 
ATOM   1411 C  CG  . ARG A 1 177 ? -42.599 -14.733 22.823  1.00 20.00 ? 177 ARG B CG  1 
ATOM   1412 C  CD  . ARG A 1 177 ? -42.935 -13.262 22.447  1.00 26.60 ? 177 ARG B CD  1 
ATOM   1413 N  NE  . ARG A 1 177 ? -42.022 -12.900 21.361  1.00 30.08 ? 177 ARG B NE  1 
ATOM   1414 C  CZ  . ARG A 1 177 ? -41.443 -11.706 21.242  1.00 38.63 ? 177 ARG B CZ  1 
ATOM   1415 N  NH1 . ARG A 1 177 ? -41.686 -10.755 22.133  1.00 46.55 ? 177 ARG B NH1 1 
ATOM   1416 N  NH2 . ARG A 1 177 ? -40.633 -11.452 20.214  1.00 42.20 ? 177 ARG B NH2 1 
ATOM   1417 N  N   . PHE A 1 178 ? -41.015 -17.306 23.851  1.00 15.45 ? 178 PHE B N   1 
ATOM   1418 C  CA  . PHE A 1 178 ? -39.704 -17.481 24.488  1.00 16.10 ? 178 PHE B CA  1 
ATOM   1419 C  C   . PHE A 1 178 ? -38.673 -17.281 23.434  1.00 13.74 ? 178 PHE B C   1 
ATOM   1420 O  O   . PHE A 1 178 ? -38.323 -18.195 22.633  1.00 17.13 ? 178 PHE B O   1 
ATOM   1421 C  CB  . PHE A 1 178 ? -39.613 -18.887 25.068  1.00 14.93 ? 178 PHE B CB  1 
ATOM   1422 C  CG  . PHE A 1 178 ? -38.513 -19.070 26.065  1.00 14.24 ? 178 PHE B CG  1 
ATOM   1423 C  CD1 . PHE A 1 178 ? -38.691 -18.740 27.403  1.00 14.97 ? 178 PHE B CD1 1 
ATOM   1424 C  CD2 . PHE A 1 178 ? -37.343 -19.652 25.636  1.00 12.85 ? 178 PHE B CD2 1 
ATOM   1425 C  CE1 . PHE A 1 178 ? -37.654 -19.010 28.253  1.00 15.55 ? 178 PHE B CE1 1 
ATOM   1426 C  CE2 . PHE A 1 178 ? -36.246 -19.918 26.488  1.00 13.95 ? 178 PHE B CE2 1 
ATOM   1427 C  CZ  . PHE A 1 178 ? -36.453 -19.599 27.821  1.00 15.78 ? 178 PHE B CZ  1 
ATOM   1428 N  N   . THR A 1 179 ? -38.186 -16.033 23.382  1.00 16.22 ? 179 THR B N   1 
ATOM   1429 C  CA  . THR A 1 179 ? -37.102 -15.764 22.430  1.00 17.26 ? 179 THR B CA  1 
ATOM   1430 C  C   . THR A 1 179 ? -35.969 -14.973 23.063  1.00 18.14 ? 179 THR B C   1 
ATOM   1431 O  O   . THR A 1 179 ? -35.983 -14.637 24.233  1.00 21.19 ? 179 THR B O   1 
ATOM   1432 C  CB  . THR A 1 179 ? -37.637 -15.116 21.155  1.00 21.38 ? 179 THR B CB  1 
ATOM   1433 O  OG1 . THR A 1 179 ? -36.651 -15.219 20.067  1.00 21.13 ? 179 THR B OG1 1 
ATOM   1434 C  CG2 . THR A 1 179 ? -38.101 -13.647 21.468  1.00 20.90 ? 179 THR B CG2 1 
ATOM   1435 N  N   . ASN A 1 180 ? -34.919 -14.801 22.270  1.00 17.55 ? 180 ASN B N   1 
ATOM   1436 C  CA  . ASN A 1 180 ? -33.688 -14.138 22.755  1.00 20.39 ? 180 ASN B CA  1 
ATOM   1437 C  C   . ASN A 1 180 ? -33.135 -14.938 23.934  1.00 20.80 ? 180 ASN B C   1 
ATOM   1438 O  O   . ASN A 1 180 ? -32.797 -14.436 25.028  1.00 19.99 ? 180 ASN B O   1 
ATOM   1439 C  CB  . ASN A 1 180 ? -33.913 -12.635 23.002  1.00 24.96 ? 180 ASN B CB  1 
ATOM   1440 C  CG  . ASN A 1 180 ? -34.279 -11.913 21.669  1.00 31.56 ? 180 ASN B CG  1 
ATOM   1441 O  OD1 . ASN A 1 180 ? -33.641 -12.156 20.606  1.00 32.14 ? 180 ASN B OD1 1 
ATOM   1442 N  ND2 . ASN A 1 180 ? -35.339 -11.073 21.709  1.00 34.68 ? 180 ASN B ND2 1 
ATOM   1443 N  N   . PHE A 1 181 ? -33.052 -16.254 23.687  1.00 17.06 ? 181 PHE B N   1 
ATOM   1444 C  CA  . PHE A 1 181 ? -32.572 -17.160 24.746  1.00 16.57 ? 181 PHE B CA  1 
ATOM   1445 C  C   . PHE A 1 181 ? -31.077 -17.460 24.501  1.00 16.08 ? 181 PHE B C   1 
ATOM   1446 O  O   . PHE A 1 181 ? -30.718 -18.018 23.525  1.00 16.74 ? 181 PHE B O   1 
ATOM   1447 C  CB  . PHE A 1 181 ? -33.389 -18.441 24.620  1.00 18.46 ? 181 PHE B CB  1 
ATOM   1448 C  CG  . PHE A 1 181 ? -32.934 -19.627 25.505  1.00 16.99 ? 181 PHE B CG  1 
ATOM   1449 C  CD1 . PHE A 1 181 ? -32.565 -19.491 26.863  1.00 17.28 ? 181 PHE B CD1 1 
ATOM   1450 C  CD2 . PHE A 1 181 ? -32.895 -20.898 24.915  1.00 15.96 ? 181 PHE B CD2 1 
ATOM   1451 C  CE1 . PHE A 1 181 ? -32.173 -20.629 27.624  1.00 16.82 ? 181 PHE B CE1 1 
ATOM   1452 C  CE2 . PHE A 1 181 ? -32.562 -22.048 25.671  1.00 17.94 ? 181 PHE B CE2 1 
ATOM   1453 C  CZ  . PHE A 1 181 ? -32.195 -21.910 27.020  1.00 16.29 ? 181 PHE B CZ  1 
ATOM   1454 N  N   . ASP A 1 182 ? -30.298 -17.241 25.551  1.00 16.15 ? 182 ASP B N   1 
ATOM   1455 C  CA  . ASP A 1 182 ? -28.837 -17.527 25.503  1.00 18.55 ? 182 ASP B CA  1 
ATOM   1456 C  C   . ASP A 1 182 ? -28.551 -18.973 25.950  1.00 17.74 ? 182 ASP B C   1 
ATOM   1457 O  O   . ASP A 1 182 ? -28.201 -19.233 27.106  1.00 20.59 ? 182 ASP B O   1 
ATOM   1458 C  CB  . ASP A 1 182 ? -28.117 -16.561 26.433  1.00 16.78 ? 182 ASP B CB  1 
ATOM   1459 C  CG  . ASP A 1 182 ? -26.606 -16.694 26.389  1.00 21.17 ? 182 ASP B CG  1 
ATOM   1460 O  OD1 . ASP A 1 182 ? -26.050 -17.502 25.600  1.00 21.61 ? 182 ASP B OD1 1 
ATOM   1461 O  OD2 . ASP A 1 182 ? -26.011 -15.936 27.207  1.00 22.30 ? 182 ASP B OD2 1 
ATOM   1462 N  N   . LEU A 1 183 ? -28.697 -19.876 25.004  1.00 17.84 ? 183 LEU B N   1 
ATOM   1463 C  CA  . LEU A 1 183 ? -28.429 -21.314 25.226  1.00 17.42 ? 183 LEU B CA  1 
ATOM   1464 C  C   . LEU A 1 183 ? -26.927 -21.593 25.411  1.00 20.31 ? 183 LEU B C   1 
ATOM   1465 O  O   . LEU A 1 183 ? -26.489 -22.456 26.246  1.00 16.36 ? 183 LEU B O   1 
ATOM   1466 C  CB  . LEU A 1 183 ? -29.003 -22.131 24.052  1.00 17.21 ? 183 LEU B CB  1 
ATOM   1467 C  CG  . LEU A 1 183 ? -28.780 -23.677 24.031  1.00 17.03 ? 183 LEU B CG  1 
ATOM   1468 C  CD1 . LEU A 1 183 ? -29.323 -24.271 25.340  1.00 16.29 ? 183 LEU B CD1 1 
ATOM   1469 C  CD2 . LEU A 1 183 ? -29.440 -24.353 22.839  1.00 16.91 ? 183 LEU B CD2 1 
ATOM   1470 N  N   . LEU A 1 184 ? -26.080 -20.903 24.639  1.00 19.71 ? 184 LEU B N   1 
ATOM   1471 C  CA  . LEU A 1 184 ? -24.668 -21.131 24.739  1.00 21.28 ? 184 LEU B CA  1 
ATOM   1472 C  C   . LEU A 1 184 ? -24.159 -21.012 26.121  1.00 19.17 ? 184 LEU B C   1 
ATOM   1473 O  O   . LEU A 1 184 ? -23.295 -21.799 26.531  1.00 22.64 ? 184 LEU B O   1 
ATOM   1474 C  CB  . LEU A 1 184 ? -23.982 -20.134 23.803  1.00 23.01 ? 184 LEU B CB  1 
ATOM   1475 C  CG  . LEU A 1 184 ? -23.122 -20.462 22.584  1.00 32.48 ? 184 LEU B CG  1 
ATOM   1476 C  CD1 . LEU A 1 184 ? -22.064 -19.377 22.460  1.00 28.07 ? 184 LEU B CD1 1 
ATOM   1477 C  CD2 . LEU A 1 184 ? -22.483 -21.838 22.674  1.00 28.40 ? 184 LEU B CD2 1 
ATOM   1478 N  N   . SER A 1 185 ? -24.667 -20.023 26.900  1.00 20.93 ? 185 SER B N   1 
ATOM   1479 C  CA  . SER A 1 185 ? -24.212 -19.797 28.216  1.00 20.00 ? 185 SER B CA  1 
ATOM   1480 C  C   . SER A 1 185 ? -24.674 -20.840 29.234  1.00 19.58 ? 185 SER B C   1 
ATOM   1481 O  O   . SER A 1 185 ? -24.244 -20.774 30.366  1.00 21.13 ? 185 SER B O   1 
ATOM   1482 C  CB  . SER A 1 185 ? -24.564 -18.419 28.773  1.00 21.49 ? 185 SER B CB  1 
ATOM   1483 O  OG  . SER A 1 185 ? -24.003 -17.383 27.917  1.00 28.38 ? 185 SER B OG  1 
ATOM   1484 N  N   . LEU A 1 186 ? -25.537 -21.757 28.828  1.00 18.32 ? 186 LEU B N   1 
ATOM   1485 C  CA  . LEU A 1 186 ? -25.910 -22.859 29.689  1.00 20.75 ? 186 LEU B CA  1 
ATOM   1486 C  C   . LEU A 1 186 ? -24.897 -23.973 29.635  1.00 23.03 ? 186 LEU B C   1 
ATOM   1487 O  O   . LEU A 1 186 ? -24.706 -24.583 30.688  1.00 32.67 ? 186 LEU B O   1 
ATOM   1488 C  CB  . LEU A 1 186 ? -27.340 -23.410 29.418  1.00 21.59 ? 186 LEU B CB  1 
ATOM   1489 C  CG  . LEU A 1 186 ? -28.409 -22.599 30.126  1.00 23.22 ? 186 LEU B CG  1 
ATOM   1490 C  CD1 . LEU A 1 186 ? -29.765 -23.130 29.625  1.00 21.20 ? 186 LEU B CD1 1 
ATOM   1491 C  CD2 . LEU A 1 186 ? -28.284 -22.852 31.641  1.00 22.04 ? 186 LEU B CD2 1 
ATOM   1492 N  N   . LEU A 1 187 ? -24.124 -24.139 28.550  1.00 17.31 ? 187 LEU B N   1 
ATOM   1493 C  CA  . LEU A 1 187 ? -23.067 -25.069 28.445  1.00 18.71 ? 187 LEU B CA  1 
ATOM   1494 C  C   . LEU A 1 187 ? -21.880 -24.751 29.373  1.00 18.92 ? 187 LEU B C   1 
ATOM   1495 O  O   . LEU A 1 187 ? -21.576 -23.552 29.735  1.00 18.88 ? 187 LEU B O   1 
ATOM   1496 C  CB  . LEU A 1 187 ? -22.508 -25.168 27.026  1.00 18.06 ? 187 LEU B CB  1 
ATOM   1497 C  CG  . LEU A 1 187 ? -23.572 -25.382 25.916  1.00 24.72 ? 187 LEU B CG  1 
ATOM   1498 C  CD1 . LEU A 1 187 ? -22.924 -25.809 24.587  1.00 24.73 ? 187 LEU B CD1 1 
ATOM   1499 C  CD2 . LEU A 1 187 ? -24.723 -26.306 26.234  1.00 24.33 ? 187 LEU B CD2 1 
ATOM   1500 N  N   . PRO A 1 188 ? -21.208 -25.831 29.839  1.00 18.03 ? 188 PRO B N   1 
ATOM   1501 C  CA  . PRO A 1 188 ? -20.090 -25.584 30.742  1.00 17.44 ? 188 PRO B CA  1 
ATOM   1502 C  C   . PRO A 1 188 ? -18.876 -25.093 29.929  1.00 17.64 ? 188 PRO B C   1 
ATOM   1503 O  O   . PRO A 1 188 ? -18.847 -25.175 28.675  1.00 17.21 ? 188 PRO B O   1 
ATOM   1504 C  CB  . PRO A 1 188 ? -19.752 -27.010 31.268  1.00 16.81 ? 188 PRO B CB  1 
ATOM   1505 C  CG  . PRO A 1 188 ? -20.079 -27.901 30.147  1.00 17.10 ? 188 PRO B CG  1 
ATOM   1506 C  CD  . PRO A 1 188 ? -21.375 -27.294 29.598  1.00 16.68 ? 188 PRO B CD  1 
ATOM   1507 N  N   . PRO A 1 189 ? -17.836 -24.615 30.660  1.00 18.42 ? 189 PRO B N   1 
ATOM   1508 C  CA  . PRO A 1 189 ? -16.717 -24.008 29.915  1.00 18.53 ? 189 PRO B CA  1 
ATOM   1509 C  C   . PRO A 1 189 ? -16.014 -25.038 29.048  1.00 17.35 ? 189 PRO B C   1 
ATOM   1510 O  O   . PRO A 1 189 ? -15.638 -24.765 27.901  1.00 19.32 ? 189 PRO B O   1 
ATOM   1511 C  CB  . PRO A 1 189 ? -15.758 -23.619 31.042  1.00 19.21 ? 189 PRO B CB  1 
ATOM   1512 C  CG  . PRO A 1 189 ? -16.722 -23.167 32.119  1.00 22.02 ? 189 PRO B CG  1 
ATOM   1513 C  CD  . PRO A 1 189 ? -17.845 -24.189 32.070  1.00 19.00 ? 189 PRO B CD  1 
ATOM   1514 N  N   . SER A 1 190 ? -15.774 -26.251 29.592  1.00 16.39 ? 190 SER B N   1 
ATOM   1515 C  CA  . SER A 1 190 ? -15.206 -27.282 28.756  1.00 13.42 ? 190 SER B CA  1 
ATOM   1516 C  C   . SER A 1 190 ? -16.261 -28.084 27.993  1.00 18.55 ? 190 SER B C   1 
ATOM   1517 O  O   . SER A 1 190 ? -17.258 -28.461 28.615  1.00 14.96 ? 190 SER B O   1 
ATOM   1518 C  CB  . SER A 1 190 ? -14.456 -28.350 29.633  1.00 14.93 ? 190 SER B CB  1 
ATOM   1519 O  OG  . SER A 1 190 ? -13.927 -29.380 28.850  1.00 17.19 ? 190 SER B OG  1 
ATOM   1520 N  N   . TRP A 1 191 ? -16.003 -28.372 26.725  1.00 14.29 ? 191 TRP B N   1 
ATOM   1521 C  CA  . TRP A 1 191 ? -16.941 -29.167 25.946  1.00 17.72 ? 191 TRP B CA  1 
ATOM   1522 C  C   . TRP A 1 191 ? -16.401 -30.542 25.639  1.00 17.62 ? 191 TRP B C   1 
ATOM   1523 O  O   . TRP A 1 191 ? -16.844 -31.209 24.714  1.00 20.76 ? 191 TRP B O   1 
ATOM   1524 C  CB  . TRP A 1 191 ? -17.370 -28.439 24.627  1.00 16.93 ? 191 TRP B CB  1 
ATOM   1525 C  CG  . TRP A 1 191 ? -18.038 -27.162 24.828  1.00 14.42 ? 191 TRP B CG  1 
ATOM   1526 C  CD1 . TRP A 1 191 ? -18.512 -26.615 25.996  1.00 16.09 ? 191 TRP B CD1 1 
ATOM   1527 C  CD2 . TRP A 1 191 ? -18.306 -26.170 23.801  1.00 14.38 ? 191 TRP B CD2 1 
ATOM   1528 N  NE1 . TRP A 1 191 ? -19.052 -25.384 25.774  1.00 15.95 ? 191 TRP B NE1 1 
ATOM   1529 C  CE2 . TRP A 1 191 ? -18.963 -25.076 24.443  1.00 16.80 ? 191 TRP B CE2 1 
ATOM   1530 C  CE3 . TRP A 1 191 ? -18.117 -26.147 22.420  1.00 16.08 ? 191 TRP B CE3 1 
ATOM   1531 C  CZ2 . TRP A 1 191 ? -19.366 -23.906 23.739  1.00 15.74 ? 191 TRP B CZ2 1 
ATOM   1532 C  CZ3 . TRP A 1 191 ? -18.490 -24.970 21.681  1.00 15.15 ? 191 TRP B CZ3 1 
ATOM   1533 C  CH2 . TRP A 1 191 ? -19.075 -23.870 22.338  1.00 17.36 ? 191 TRP B CH2 1 
ATOM   1534 N  N   . ASP A 1 192 ? -15.480 -31.046 26.489  1.00 15.32 ? 192 ASP B N   1 
ATOM   1535 C  CA  . ASP A 1 192 ? -15.070 -32.397 26.283  1.00 15.22 ? 192 ASP B CA  1 
ATOM   1536 C  C   . ASP A 1 192 ? -16.288 -33.357 26.497  1.00 13.04 ? 192 ASP B C   1 
ATOM   1537 O  O   . ASP A 1 192 ? -17.129 -33.066 27.300  1.00 13.69 ? 192 ASP B O   1 
ATOM   1538 C  CB  . ASP A 1 192 ? -14.080 -32.763 27.409  1.00 17.68 ? 192 ASP B CB  1 
ATOM   1539 C  CG  . ASP A 1 192 ? -12.679 -32.164 27.238  1.00 22.71 ? 192 ASP B CG  1 
ATOM   1540 O  OD1 . ASP A 1 192 ? -12.382 -31.674 26.144  1.00 23.77 ? 192 ASP B OD1 1 
ATOM   1541 O  OD2 . ASP A 1 192 ? -11.943 -32.271 28.282  1.00 25.34 ? 192 ASP B OD2 1 
ATOM   1542 N  N   . TYR A 1 193 ? -16.362 -34.385 25.707  1.00 12.22 ? 193 TYR B N   1 
ATOM   1543 C  CA  . TYR A 1 193 ? -17.558 -35.258 25.689  1.00 15.29 ? 193 TYR B CA  1 
ATOM   1544 C  C   . TYR A 1 193 ? -17.286 -36.743 25.448  1.00 15.59 ? 193 TYR B C   1 
ATOM   1545 O  O   . TYR A 1 193 ? -16.206 -37.166 24.918  1.00 15.72 ? 193 TYR B O   1 
ATOM   1546 C  CB  . TYR A 1 193 ? -18.593 -34.751 24.592  1.00 15.16 ? 193 TYR B CB  1 
ATOM   1547 C  CG  . TYR A 1 193 ? -18.033 -34.860 23.224  1.00 15.74 ? 193 TYR B CG  1 
ATOM   1548 C  CD1 . TYR A 1 193 ? -18.179 -35.996 22.486  1.00 13.91 ? 193 TYR B CD1 1 
ATOM   1549 C  CD2 . TYR A 1 193 ? -17.344 -33.777 22.711  1.00 17.44 ? 193 TYR B CD2 1 
ATOM   1550 C  CE1 . TYR A 1 193 ? -17.643 -36.121 21.202  1.00 18.34 ? 193 TYR B CE1 1 
ATOM   1551 C  CE2 . TYR A 1 193 ? -16.777 -33.840 21.457  1.00 15.42 ? 193 TYR B CE2 1 
ATOM   1552 C  CZ  . TYR A 1 193 ? -16.927 -35.000 20.729  1.00 15.92 ? 193 TYR B CZ  1 
ATOM   1553 O  OH  . TYR A 1 193 ? -16.353 -35.127 19.462  1.00 18.71 ? 193 TYR B OH  1 
ATOM   1554 N  N   . TRP A 1 194 ? -18.299 -37.582 25.754  1.00 12.86 ? 194 TRP B N   1 
ATOM   1555 C  CA  . TRP A 1 194 ? -18.380 -38.898 25.314  1.00 12.70 ? 194 TRP B CA  1 
ATOM   1556 C  C   . TRP A 1 194 ? -19.454 -39.011 24.206  1.00 13.85 ? 194 TRP B C   1 
ATOM   1557 O  O   . TRP A 1 194 ? -20.425 -38.232 24.243  1.00 16.12 ? 194 TRP B O   1 
ATOM   1558 C  CB  . TRP A 1 194 ? -18.861 -39.838 26.417  1.00 15.13 ? 194 TRP B CB  1 
ATOM   1559 C  CG  . TRP A 1 194 ? -17.898 -39.868 27.569  1.00 13.16 ? 194 TRP B CG  1 
ATOM   1560 C  CD1 . TRP A 1 194 ? -16.655 -40.499 27.630  1.00 17.82 ? 194 TRP B CD1 1 
ATOM   1561 C  CD2 . TRP A 1 194 ? -18.046 -39.188 28.859  1.00 13.75 ? 194 TRP B CD2 1 
ATOM   1562 N  NE1 . TRP A 1 194 ? -16.049 -40.274 28.839  1.00 18.35 ? 194 TRP B NE1 1 
ATOM   1563 C  CE2 . TRP A 1 194 ? -16.828 -39.501 29.630  1.00 15.57 ? 194 TRP B CE2 1 
ATOM   1564 C  CE3 . TRP A 1 194 ? -19.040 -38.412 29.447  1.00 13.78 ? 194 TRP B CE3 1 
ATOM   1565 C  CZ2 . TRP A 1 194 ? -16.632 -39.031 30.915  1.00 16.70 ? 194 TRP B CZ2 1 
ATOM   1566 C  CZ3 . TRP A 1 194 ? -18.818 -37.934 30.747  1.00 17.15 ? 194 TRP B CZ3 1 
ATOM   1567 C  CH2 . TRP A 1 194 ? -17.651 -38.247 31.463  1.00 17.16 ? 194 TRP B CH2 1 
ATOM   1568 N  N   . THR A 1 195 ? -19.280 -39.974 23.332  1.00 13.70 ? 195 THR B N   1 
ATOM   1569 C  CA  . THR A 1 195 ? -20.259 -40.173 22.267  1.00 15.58 ? 195 THR B CA  1 
ATOM   1570 C  C   . THR A 1 195 ? -20.536 -41.596 21.970  1.00 15.15 ? 195 THR B C   1 
ATOM   1571 O  O   . THR A 1 195 ? -19.649 -42.479 22.074  1.00 17.05 ? 195 THR B O   1 
ATOM   1572 C  CB  . THR A 1 195 ? -19.910 -39.300 21.047  1.00 15.51 ? 195 THR B CB  1 
ATOM   1573 O  OG1 . THR A 1 195 ? -20.908 -39.527 20.032  1.00 15.28 ? 195 THR B OG1 1 
ATOM   1574 C  CG2 . THR A 1 195 ? -18.556 -39.730 20.416  1.00 16.52 ? 195 THR B CG2 1 
ATOM   1575 N  N   . TYR A 1 196 ? -21.794 -41.921 21.667  1.00 14.71 ? 196 TYR B N   1 
ATOM   1576 C  CA  . TYR A 1 196 ? -22.183 -43.284 21.377  1.00 13.02 ? 196 TYR B CA  1 
ATOM   1577 C  C   . TYR A 1 196 ? -23.516 -43.281 20.609  1.00 14.10 ? 196 TYR B C   1 
ATOM   1578 O  O   . TYR A 1 196 ? -24.207 -42.272 20.636  1.00 13.86 ? 196 TYR B O   1 
ATOM   1579 C  CB  . TYR A 1 196 ? -22.280 -44.150 22.688  1.00 13.47 ? 196 TYR B CB  1 
ATOM   1580 C  CG  . TYR A 1 196 ? -23.541 -43.814 23.494  1.00 12.26 ? 196 TYR B CG  1 
ATOM   1581 C  CD1 . TYR A 1 196 ? -23.565 -42.705 24.346  1.00 12.79 ? 196 TYR B CD1 1 
ATOM   1582 C  CD2 . TYR A 1 196 ? -24.725 -44.593 23.338  1.00 12.92 ? 196 TYR B CD2 1 
ATOM   1583 C  CE1 . TYR A 1 196 ? -24.761 -42.394 25.046  1.00 11.53 ? 196 TYR B CE1 1 
ATOM   1584 C  CE2 . TYR A 1 196 ? -25.958 -44.278 24.020  1.00 12.28 ? 196 TYR B CE2 1 
ATOM   1585 C  CZ  . TYR A 1 196 ? -25.918 -43.177 24.887  1.00 11.00 ? 196 TYR B CZ  1 
ATOM   1586 O  OH  . TYR A 1 196 ? -27.096 -42.823 25.535  1.00 12.05 ? 196 TYR B OH  1 
ATOM   1587 N  N   . PRO A 1 197 ? -23.866 -44.393 19.926  1.00 16.64 ? 197 PRO B N   1 
ATOM   1588 C  CA  . PRO A 1 197 ? -25.134 -44.490 19.152  1.00 15.08 ? 197 PRO B CA  1 
ATOM   1589 C  C   . PRO A 1 197 ? -26.252 -44.942 20.082  1.00 15.39 ? 197 PRO B C   1 
ATOM   1590 O  O   . PRO A 1 197 ? -26.092 -45.959 20.759  1.00 16.51 ? 197 PRO B O   1 
ATOM   1591 C  CB  . PRO A 1 197 ? -24.797 -45.523 18.070  1.00 17.06 ? 197 PRO B CB  1 
ATOM   1592 C  CG  . PRO A 1 197 ? -23.708 -46.398 18.717  1.00 14.89 ? 197 PRO B CG  1 
ATOM   1593 C  CD  . PRO A 1 197 ? -22.914 -45.507 19.630  1.00 17.99 ? 197 PRO B CD  1 
ATOM   1594 N  N   . GLY A 1 198 ? -27.331 -44.148 20.170  1.00 13.91 ? 198 GLY B N   1 
ATOM   1595 C  CA  . GLY A 1 198 ? -28.456 -44.617 20.962  1.00 13.23 ? 198 GLY B CA  1 
ATOM   1596 C  C   . GLY A 1 198 ? -29.781 -44.090 20.485  1.00 12.76 ? 198 GLY B C   1 
ATOM   1597 O  O   . GLY A 1 198 ? -30.057 -44.094 19.277  1.00 13.80 ? 198 GLY B O   1 
ATOM   1598 N  N   . SER A 1 199 ? -30.614 -43.706 21.432  1.00 12.54 ? 199 SER B N   1 
ATOM   1599 C  CA  . SER A 1 199 ? -32.083 -43.560 21.116  1.00 13.22 ? 199 SER B CA  1 
ATOM   1600 C  C   . SER A 1 199 ? -32.667 -42.338 21.813  1.00 11.07 ? 199 SER B C   1 
ATOM   1601 O  O   . SER A 1 199 ? -32.065 -41.716 22.712  1.00 10.92 ? 199 SER B O   1 
ATOM   1602 C  CB  . SER A 1 199 ? -32.889 -44.835 21.564  1.00 14.73 ? 199 SER B CB  1 
ATOM   1603 O  OG  . SER A 1 199 ? -33.016 -44.821 23.003  1.00 13.41 ? 199 SER B OG  1 
ATOM   1604 N  N   . LEU A 1 200 ? -33.896 -42.002 21.429  1.00 10.51 ? 200 LEU B N   1 
ATOM   1605 C  CA  . LEU A 1 200 ? -34.676 -41.027 22.258  1.00 10.58 ? 200 LEU B CA  1 
ATOM   1606 C  C   . LEU A 1 200 ? -34.850 -41.770 23.602  1.00 12.10 ? 200 LEU B C   1 
ATOM   1607 O  O   . LEU A 1 200 ? -35.053 -42.961 23.689  1.00 12.03 ? 200 LEU B O   1 
ATOM   1608 C  CB  . LEU A 1 200 ? -36.070 -40.861 21.742  1.00 11.71 ? 200 LEU B CB  1 
ATOM   1609 C  CG  . LEU A 1 200 ? -36.092 -40.333 20.251  1.00 12.34 ? 200 LEU B CG  1 
ATOM   1610 C  CD1 . LEU A 1 200 ? -37.581 -40.286 19.863  1.00 14.03 ? 200 LEU B CD1 1 
ATOM   1611 C  CD2 . LEU A 1 200 ? -35.536 -38.939 20.243  1.00 12.72 ? 200 LEU B CD2 1 
ATOM   1612 N  N   . THR A 1 201 ? -34.872 -40.993 24.658  1.00 11.07 ? 201 THR B N   1 
ATOM   1613 C  CA  . THR A 1 201 ? -35.074 -41.598 26.032  1.00 10.82 ? 201 THR B CA  1 
ATOM   1614 C  C   . THR A 1 201 ? -36.525 -41.518 26.448  1.00 11.82 ? 201 THR B C   1 
ATOM   1615 O  O   . THR A 1 201 ? -36.836 -41.783 27.650  1.00 11.14 ? 201 THR B O   1 
ATOM   1616 C  CB  . THR A 1 201 ? -34.133 -40.927 27.096  1.00 10.71 ? 201 THR B CB  1 
ATOM   1617 O  OG1 . THR A 1 201 ? -34.589 -39.603 27.391  1.00 10.51 ? 201 THR B OG1 1 
ATOM   1618 C  CG2 . THR A 1 201 ? -32.712 -40.851 26.604  1.00 11.70 ? 201 THR B CG2 1 
ATOM   1619 N  N   . VAL A 1 202 ? -37.374 -41.037 25.567  1.00 11.30 ? 202 VAL B N   1 
ATOM   1620 C  CA  . VAL A 1 202 ? -38.847 -41.027 25.769  1.00 12.21 ? 202 VAL B CA  1 
ATOM   1621 C  C   . VAL A 1 202 ? -39.491 -41.775 24.632  1.00 12.86 ? 202 VAL B C   1 
ATOM   1622 O  O   . VAL A 1 202 ? -38.876 -41.816 23.560  1.00 12.34 ? 202 VAL B O   1 
ATOM   1623 C  CB  . VAL A 1 202 ? -39.374 -39.614 25.830  1.00 11.60 ? 202 VAL B CB  1 
ATOM   1624 C  CG1 . VAL A 1 202 ? -38.833 -38.866 27.057  1.00 13.18 ? 202 VAL B CG1 1 
ATOM   1625 C  CG2 . VAL A 1 202 ? -39.131 -38.758 24.575  1.00 10.89 ? 202 VAL B CG2 1 
ATOM   1626 N  N   . PRO A 1 203 ? -40.638 -42.446 24.871  1.00 12.71 ? 203 PRO B N   1 
ATOM   1627 C  CA  . PRO A 1 203 ? -41.447 -42.912 23.722  1.00 13.68 ? 203 PRO B CA  1 
ATOM   1628 C  C   . PRO A 1 203 ? -41.513 -41.795 22.662  1.00 13.32 ? 203 PRO B C   1 
ATOM   1629 O  O   . PRO A 1 203 ? -41.769 -40.649 22.884  1.00 12.79 ? 203 PRO B O   1 
ATOM   1630 C  CB  . PRO A 1 203 ? -42.811 -43.199 24.375  1.00 13.26 ? 203 PRO B CB  1 
ATOM   1631 C  CG  . PRO A 1 203 ? -42.410 -43.603 25.826  1.00 13.14 ? 203 PRO B CG  1 
ATOM   1632 C  CD  . PRO A 1 203 ? -41.363 -42.529 26.176  1.00 11.94 ? 203 PRO B CD  1 
ATOM   1633 N  N   . PRO A 1 204 ? -41.308 -42.199 21.373  1.00 12.75 ? 204 PRO B N   1 
ATOM   1634 C  CA  . PRO A 1 204 ? -41.268 -43.578 20.906  1.00 14.86 ? 204 PRO B CA  1 
ATOM   1635 C  C   . PRO A 1 204 ? -39.917 -44.333 20.924  1.00 15.33 ? 204 PRO B C   1 
ATOM   1636 O  O   . PRO A 1 204 ? -39.817 -45.452 20.304  1.00 17.33 ? 204 PRO B O   1 
ATOM   1637 C  CB  . PRO A 1 204 ? -41.763 -43.413 19.419  1.00 14.60 ? 204 PRO B CB  1 
ATOM   1638 C  CG  . PRO A 1 204 ? -41.285 -42.043 19.017  1.00 16.46 ? 204 PRO B CG  1 
ATOM   1639 C  CD  . PRO A 1 204 ? -41.392 -41.193 20.308  1.00 15.37 ? 204 PRO B CD  1 
ATOM   1640 N  N   . LEU A 1 205 ? -38.902 -43.757 21.581  1.00 13.99 ? 205 LEU B N   1 
ATOM   1641 C  CA  . LEU A 1 205 ? -37.691 -44.507 21.872  1.00 13.14 ? 205 LEU B CA  1 
ATOM   1642 C  C   . LEU A 1 205 ? -36.941 -44.906 20.619  1.00 14.42 ? 205 LEU B C   1 
ATOM   1643 O  O   . LEU A 1 205 ? -36.105 -45.866 20.621  1.00 12.36 ? 205 LEU B O   1 
ATOM   1644 C  CB  . LEU A 1 205 ? -37.936 -45.746 22.773  1.00 13.94 ? 205 LEU B CB  1 
ATOM   1645 C  CG  . LEU A 1 205 ? -38.629 -45.365 24.145  1.00 13.97 ? 205 LEU B CG  1 
ATOM   1646 C  CD1 . LEU A 1 205 ? -39.110 -46.660 24.850  1.00 17.30 ? 205 LEU B CD1 1 
ATOM   1647 C  CD2 . LEU A 1 205 ? -37.619 -44.675 25.079  1.00 13.21 ? 205 LEU B CD2 1 
ATOM   1648 N  N   . LEU A 1 206 ? -37.071 -44.057 19.564  1.00 13.74 ? 206 LEU B N   1 
ATOM   1649 C  CA  . LEU A 1 206 ? -36.436 -44.451 18.255  1.00 14.15 ? 206 LEU B CA  1 
ATOM   1650 C  C   . LEU A 1 206 ? -34.902 -44.429 18.361  1.00 12.74 ? 206 LEU B C   1 
ATOM   1651 O  O   . LEU A 1 206 ? -34.302 -43.539 18.965  1.00 14.31 ? 206 LEU B O   1 
ATOM   1652 C  CB  . LEU A 1 206 ? -36.893 -43.462 17.131  1.00 14.11 ? 206 LEU B CB  1 
ATOM   1653 C  CG  . LEU A 1 206 ? -38.424 -43.549 17.008  1.00 15.21 ? 206 LEU B CG  1 
ATOM   1654 C  CD1 . LEU A 1 206 ? -38.893 -42.233 16.296  1.00 16.42 ? 206 LEU B CD1 1 
ATOM   1655 C  CD2 . LEU A 1 206 ? -38.774 -44.802 16.252  1.00 18.81 ? 206 LEU B CD2 1 
ATOM   1656 N  N   . GLU A 1 207 ? -34.275 -45.390 17.647  1.00 13.44 ? 207 GLU B N   1 
ATOM   1657 C  CA  . GLU A 1 207 ? -32.847 -45.502 17.670  1.00 13.13 ? 207 GLU B CA  1 
ATOM   1658 C  C   . GLU A 1 207 ? -32.201 -44.690 16.569  1.00 14.24 ? 207 GLU B C   1 
ATOM   1659 O  O   . GLU A 1 207 ? -31.694 -45.229 15.557  1.00 16.18 ? 207 GLU B O   1 
ATOM   1660 C  CB  . GLU A 1 207 ? -32.446 -46.989 17.710  1.00 13.90 ? 207 GLU B CB  1 
ATOM   1661 C  CG  . GLU A 1 207 ? -33.023 -47.765 18.942  1.00 14.27 ? 207 GLU B CG  1 
ATOM   1662 C  CD  . GLU A 1 207 ? -32.699 -49.192 19.079  1.00 17.30 ? 207 GLU B CD  1 
ATOM   1663 O  OE1 . GLU A 1 207 ? -32.632 -49.861 17.985  1.00 17.70 ? 207 GLU B OE1 1 
ATOM   1664 O  OE2 . GLU A 1 207 ? -32.722 -49.717 20.222  1.00 15.70 ? 207 GLU B OE2 1 
ATOM   1665 N  N   . SER A 1 208 ? -32.289 -43.384 16.705  1.00 12.99 ? 208 SER B N   1 
ATOM   1666 C  CA  . SER A 1 208 ? -31.828 -42.455 15.682  1.00 13.33 ? 208 SER B CA  1 
ATOM   1667 C  C   . SER A 1 208 ? -30.928 -41.415 16.219  1.00 13.47 ? 208 SER B C   1 
ATOM   1668 O  O   . SER A 1 208 ? -30.578 -40.365 15.539  1.00 13.81 ? 208 SER B O   1 
ATOM   1669 C  CB  . SER A 1 208 ? -33.072 -41.796 15.141  1.00 15.66 ? 208 SER B CB  1 
ATOM   1670 O  OG  . SER A 1 208 ? -33.799 -41.207 16.265  1.00 15.97 ? 208 SER B OG  1 
ATOM   1671 N  N   . VAL A 1 209 ? -30.402 -41.613 17.483  1.00 12.58 ? 209 VAL B N   1 
ATOM   1672 C  CA  . VAL A 1 209 ? -29.655 -40.527 18.070  1.00 12.62 ? 209 VAL B CA  1 
ATOM   1673 C  C   . VAL A 1 209 ? -28.136 -40.775 18.228  1.00 11.71 ? 209 VAL B C   1 
ATOM   1674 O  O   . VAL A 1 209 ? -27.716 -41.828 18.796  1.00 14.19 ? 209 VAL B O   1 
ATOM   1675 C  CB  . VAL A 1 209 ? -30.195 -40.254 19.529  1.00 12.10 ? 209 VAL B CB  1 
ATOM   1676 C  CG1 . VAL A 1 209 ? -29.405 -39.122 20.179  1.00 12.55 ? 209 VAL B CG1 1 
ATOM   1677 C  CG2 . VAL A 1 209 ? -31.703 -39.882 19.490  1.00 12.22 ? 209 VAL B CG2 1 
ATOM   1678 N  N   . THR A 1 210 ? -27.359 -39.799 17.746  1.00 12.67 ? 210 THR B N   1 
ATOM   1679 C  CA  . THR A 1 210 ? -25.932 -39.759 18.106  1.00 12.20 ? 210 THR B CA  1 
ATOM   1680 C  C   . THR A 1 210 ? -25.844 -38.897 19.323  1.00 12.97 ? 210 THR B C   1 
ATOM   1681 O  O   . THR A 1 210 ? -26.029 -37.665 19.335  1.00 12.98 ? 210 THR B O   1 
ATOM   1682 C  CB  . THR A 1 210 ? -25.109 -39.140 16.963  1.00 13.60 ? 210 THR B CB  1 
ATOM   1683 O  OG1 . THR A 1 210 ? -25.246 -40.029 15.847  1.00 14.62 ? 210 THR B OG1 1 
ATOM   1684 C  CG2 . THR A 1 210 ? -23.600 -39.060 17.395  1.00 14.30 ? 210 THR B CG2 1 
ATOM   1685 N  N   . TRP A 1 211 ? -25.533 -39.612 20.424  1.00 13.03 ? 211 TRP B N   1 
ATOM   1686 C  CA  . TRP A 1 211 ? -25.408 -38.882 21.753  1.00 11.95 ? 211 TRP B CA  1 
ATOM   1687 C  C   . TRP A 1 211 ? -24.041 -38.220 21.920  1.00 11.52 ? 211 TRP B C   1 
ATOM   1688 O  O   . TRP A 1 211 ? -23.035 -38.843 21.628  1.00 14.18 ? 211 TRP B O   1 
ATOM   1689 C  CB  . TRP A 1 211 ? -25.660 -39.918 22.891  1.00 10.86 ? 211 TRP B CB  1 
ATOM   1690 C  CG  . TRP A 1 211 ? -27.111 -40.071 23.095  1.00 10.46 ? 211 TRP B CG  1 
ATOM   1691 C  CD1 . TRP A 1 211 ? -27.965 -41.047 22.641  1.00 9.24  ? 211 TRP B CD1 1 
ATOM   1692 C  CD2 . TRP A 1 211 ? -27.933 -39.150 23.896  1.00 9.93  ? 211 TRP B CD2 1 
ATOM   1693 N  NE1 . TRP A 1 211 ? -29.275 -40.732 23.040  1.00 10.63 ? 211 TRP B NE1 1 
ATOM   1694 C  CE2 . TRP A 1 211 ? -29.323 -39.627 23.788  1.00 10.22 ? 211 TRP B CE2 1 
ATOM   1695 C  CE3 . TRP A 1 211 ? -27.655 -37.952 24.622  1.00 11.18 ? 211 TRP B CE3 1 
ATOM   1696 C  CZ2 . TRP A 1 211 ? -30.384 -38.957 24.399  1.00 11.25 ? 211 TRP B CZ2 1 
ATOM   1697 C  CZ3 . TRP A 1 211 ? -28.738 -37.267 25.199  1.00 11.02 ? 211 TRP B CZ3 1 
ATOM   1698 C  CH2 . TRP A 1 211 ? -30.069 -37.783 25.146  1.00 10.88 ? 211 TRP B CH2 1 
ATOM   1699 N  N   . ILE A 1 212 ? -24.048 -37.029 22.428  1.00 11.25 ? 212 ILE B N   1 
ATOM   1700 C  CA  . ILE A 1 212 ? -22.843 -36.281 22.766  1.00 12.73 ? 212 ILE B CA  1 
ATOM   1701 C  C   . ILE A 1 212 ? -23.038 -35.790 24.176  1.00 13.29 ? 212 ILE B C   1 
ATOM   1702 O  O   . ILE A 1 212 ? -23.795 -34.863 24.429  1.00 13.39 ? 212 ILE B O   1 
ATOM   1703 C  CB  . ILE A 1 212 ? -22.597 -35.118 21.755  1.00 13.96 ? 212 ILE B CB  1 
ATOM   1704 C  CG1 . ILE A 1 212 ? -22.473 -35.680 20.350  1.00 13.37 ? 212 ILE B CG1 1 
ATOM   1705 C  CG2 . ILE A 1 212 ? -21.390 -34.251 22.125  1.00 15.48 ? 212 ILE B CG2 1 
ATOM   1706 C  CD1 . ILE A 1 212 ? -22.557 -34.624 19.226  1.00 16.45 ? 212 ILE B CD1 1 
ATOM   1707 N  N   . VAL A 1 213 ? -22.371 -36.502 25.149  1.00 12.50 ? 213 VAL B N   1 
ATOM   1708 C  CA  . VAL A 1 213 ? -22.643 -36.220 26.543  1.00 11.92 ? 213 VAL B CA  1 
ATOM   1709 C  C   . VAL A 1 213 ? -21.413 -35.474 27.102  1.00 13.30 ? 213 VAL B C   1 
ATOM   1710 O  O   . VAL A 1 213 ? -20.334 -36.087 27.122  1.00 13.04 ? 213 VAL B O   1 
ATOM   1711 C  CB  . VAL A 1 213 ? -22.912 -37.558 27.303  1.00 11.60 ? 213 VAL B CB  1 
ATOM   1712 C  CG1 . VAL A 1 213 ? -23.070 -37.286 28.787  1.00 12.55 ? 213 VAL B CG1 1 
ATOM   1713 C  CG2 . VAL A 1 213 ? -24.227 -38.243 26.776  1.00 12.96 ? 213 VAL B CG2 1 
ATOM   1714 N  N   . LEU A 1 214 ? -21.616 -34.243 27.576  1.00 13.77 ? 214 LEU B N   1 
ATOM   1715 C  CA  . LEU A 1 214 ? -20.458 -33.402 27.990  1.00 13.52 ? 214 LEU B CA  1 
ATOM   1716 C  C   . LEU A 1 214 ? -20.019 -33.912 29.370  1.00 13.23 ? 214 LEU B C   1 
ATOM   1717 O  O   . LEU A 1 214 ? -20.845 -34.220 30.236  1.00 13.78 ? 214 LEU B O   1 
ATOM   1718 C  CB  . LEU A 1 214 ? -20.785 -31.950 28.022  1.00 13.93 ? 214 LEU B CB  1 
ATOM   1719 C  CG  . LEU A 1 214 ? -20.559 -31.281 26.654  1.00 17.41 ? 214 LEU B CG  1 
ATOM   1720 C  CD1 . LEU A 1 214 ? -21.241 -31.969 25.515  1.00 20.03 ? 214 LEU B CD1 1 
ATOM   1721 C  CD2 . LEU A 1 214 ? -20.925 -29.768 26.853  1.00 16.77 ? 214 LEU B CD2 1 
ATOM   1722 N  N   . LYS A 1 215 ? -18.696 -34.037 29.565  1.00 13.51 ? 215 LYS B N   1 
ATOM   1723 C  CA  . LYS A 1 215 ? -18.173 -34.474 30.867  1.00 13.58 ? 215 LYS B CA  1 
ATOM   1724 C  C   . LYS A 1 215 ? -18.358 -33.448 32.041  1.00 15.46 ? 215 LYS B C   1 
ATOM   1725 O  O   . LYS A 1 215 ? -18.668 -33.812 33.215  1.00 15.50 ? 215 LYS B O   1 
ATOM   1726 C  CB  . LYS A 1 215 ? -16.657 -34.807 30.644  1.00 14.95 ? 215 LYS B CB  1 
ATOM   1727 C  CG  . LYS A 1 215 ? -15.946 -34.989 32.020  1.00 18.05 ? 215 LYS B CG  1 
ATOM   1728 C  CD  . LYS A 1 215 ? -14.517 -35.431 31.820  1.00 21.98 ? 215 LYS B CD  1 
ATOM   1729 C  CE  . LYS A 1 215 ? -13.825 -35.620 33.162  1.00 28.78 ? 215 LYS B CE  1 
ATOM   1730 N  NZ  . LYS A 1 215 ? -12.479 -36.084 32.661  1.00 31.27 ? 215 LYS B NZ  1 
ATOM   1731 N  N   . GLN A 1 216 ? -18.189 -32.132 31.787  1.00 12.35 ? 216 GLN B N   1 
ATOM   1732 C  CA  . GLN A 1 216 ? -18.261 -31.131 32.837  1.00 13.01 ? 216 GLN B CA  1 
ATOM   1733 C  C   . GLN A 1 216 ? -19.688 -30.754 33.179  1.00 14.07 ? 216 GLN B C   1 
ATOM   1734 O  O   . GLN A 1 216 ? -20.395 -30.265 32.265  1.00 14.30 ? 216 GLN B O   1 
ATOM   1735 C  CB  . GLN A 1 216 ? -17.428 -29.842 32.444  1.00 13.92 ? 216 GLN B CB  1 
ATOM   1736 C  CG  . GLN A 1 216 ? -17.557 -28.788 33.579  1.00 16.96 ? 216 GLN B CG  1 
ATOM   1737 C  CD  . GLN A 1 216 ? -16.583 -27.638 33.485  1.00 20.00 ? 216 GLN B CD  1 
ATOM   1738 O  OE1 . GLN A 1 216 ? -16.032 -27.440 32.441  1.00 21.31 ? 216 GLN B OE1 1 
ATOM   1739 N  NE2 . GLN A 1 216 ? -16.430 -26.862 34.584  1.00 23.20 ? 216 GLN B NE2 1 
ATOM   1740 N  N   . PRO A 1 217 ? -20.159 -30.867 34.410  1.00 14.30 ? 217 PRO B N   1 
ATOM   1741 C  CA  . PRO A 1 217 ? -21.485 -30.433 34.781  1.00 13.48 ? 217 PRO B CA  1 
ATOM   1742 C  C   . PRO A 1 217 ? -21.574 -28.949 34.915  1.00 14.51 ? 217 PRO B C   1 
ATOM   1743 O  O   . PRO A 1 217 ? -20.513 -28.270 35.106  1.00 17.90 ? 217 PRO B O   1 
ATOM   1744 C  CB  . PRO A 1 217 ? -21.740 -31.056 36.165  1.00 15.75 ? 217 PRO B CB  1 
ATOM   1745 C  CG  . PRO A 1 217 ? -20.368 -31.422 36.626  1.00 19.51 ? 217 PRO B CG  1 
ATOM   1746 C  CD  . PRO A 1 217 ? -19.435 -31.572 35.494  1.00 14.63 ? 217 PRO B CD  1 
ATOM   1747 N  N   . ILE A 1 218 ? -22.791 -28.415 34.816  1.00 13.81 ? 218 ILE B N   1 
ATOM   1748 C  CA  . ILE A 1 218 ? -23.076 -27.034 35.253  1.00 14.12 ? 218 ILE B CA  1 
ATOM   1749 C  C   . ILE A 1 218 ? -23.806 -27.042 36.559  1.00 15.67 ? 218 ILE B C   1 
ATOM   1750 O  O   . ILE A 1 218 ? -24.201 -28.127 37.023  1.00 16.40 ? 218 ILE B O   1 
ATOM   1751 C  CB  . ILE A 1 218 ? -23.904 -26.243 34.166  1.00 14.83 ? 218 ILE B CB  1 
ATOM   1752 C  CG1 . ILE A 1 218 ? -25.301 -26.861 34.012  1.00 14.73 ? 218 ILE B CG1 1 
ATOM   1753 C  CG2 . ILE A 1 218 ? -23.169 -26.221 32.829  1.00 14.24 ? 218 ILE B CG2 1 
ATOM   1754 C  CD1 . ILE A 1 218 ? -26.282 -25.985 33.150  1.00 14.05 ? 218 ILE B CD1 1 
ATOM   1755 N  N   . ASN A 1 219 ? -23.910 -25.880 37.243  1.00 14.85 ? 219 ASN B N   1 
ATOM   1756 C  CA  . ASN A 1 219 ? -24.591 -25.835 38.526  1.00 15.47 ? 219 ASN B CA  1 
ATOM   1757 C  C   . ASN A 1 219 ? -26.064 -25.571 38.446  1.00 14.62 ? 219 ASN B C   1 
ATOM   1758 O  O   . ASN A 1 219 ? -26.568 -24.897 37.506  1.00 16.74 ? 219 ASN B O   1 
ATOM   1759 C  CB  . ASN A 1 219 ? -24.003 -24.776 39.451  1.00 18.37 ? 219 ASN B CB  1 
ATOM   1760 C  CG  . ASN A 1 219 ? -22.622 -25.092 39.916  1.00 25.61 ? 219 ASN B CG  1 
ATOM   1761 O  OD1 . ASN A 1 219 ? -22.153 -26.257 40.003  1.00 27.02 ? 219 ASN B OD1 1 
ATOM   1762 N  ND2 . ASN A 1 219 ? -21.951 -24.004 40.328  1.00 35.04 ? 219 ASN B ND2 1 
ATOM   1763 N  N   . ILE A 1 220 ? -26.797 -26.036 39.454  1.00 13.87 ? 220 ILE B N   1 
ATOM   1764 C  CA  . ILE A 1 220 ? -28.147 -25.578 39.705  1.00 15.63 ? 220 ILE B CA  1 
ATOM   1765 C  C   . ILE A 1 220 ? -28.299 -25.588 41.231  1.00 15.10 ? 220 ILE B C   1 
ATOM   1766 O  O   . ILE A 1 220 ? -27.873 -26.547 41.880  1.00 13.47 ? 220 ILE B O   1 
ATOM   1767 C  CB  . ILE A 1 220 ? -29.203 -26.518 39.008  1.00 14.98 ? 220 ILE B CB  1 
ATOM   1768 C  CG1 . ILE A 1 220 ? -30.607 -25.933 39.140  1.00 13.47 ? 220 ILE B CG1 1 
ATOM   1769 C  CG2 . ILE A 1 220 ? -29.147 -27.965 39.548  1.00 15.60 ? 220 ILE B CG2 1 
ATOM   1770 C  CD1 . ILE A 1 220 ? -31.724 -26.647 38.252  1.00 14.27 ? 220 ILE B CD1 1 
ATOM   1771 N  N   . SER A 1 221 ? -29.025 -24.641 41.812  1.00 16.11 ? 221 SER B N   1 
ATOM   1772 C  CA  . SER A 1 221 ? -29.330 -24.829 43.239  1.00 15.36 ? 221 SER B CA  1 
ATOM   1773 C  C   . SER A 1 221 ? -30.522 -25.743 43.515  1.00 16.24 ? 221 SER B C   1 
ATOM   1774 O  O   . SER A 1 221 ? -31.357 -26.021 42.644  1.00 15.50 ? 221 SER B O   1 
ATOM   1775 C  CB  . SER A 1 221 ? -29.648 -23.442 43.859  1.00 16.01 ? 221 SER B CB  1 
ATOM   1776 O  OG  . SER A 1 221 ? -30.949 -22.979 43.533  1.00 15.22 ? 221 SER B OG  1 
ATOM   1777 N  N   A SER A 1 222 ? -30.634 -26.170 44.757  0.50 16.22 ? 222 SER B N   1 
ATOM   1778 N  N   B SER A 1 222 ? -30.685 -26.181 44.758  0.50 16.09 ? 222 SER B N   1 
ATOM   1779 C  CA  A SER A 1 222 ? -31.787 -26.929 45.149  0.50 15.25 ? 222 SER B CA  1 
ATOM   1780 C  CA  B SER A 1 222 ? -31.870 -26.966 45.122  0.50 15.05 ? 222 SER B CA  1 
ATOM   1781 C  C   A SER A 1 222 ? -33.094 -26.209 44.970  0.50 14.97 ? 222 SER B C   1 
ATOM   1782 C  C   B SER A 1 222 ? -33.168 -26.205 44.990  0.50 14.89 ? 222 SER B C   1 
ATOM   1783 O  O   A SER A 1 222 ? -34.069 -26.816 44.513  0.50 15.23 ? 222 SER B O   1 
ATOM   1784 O  O   B SER A 1 222 ? -34.210 -26.755 44.573  0.50 14.19 ? 222 SER B O   1 
ATOM   1785 C  CB  A SER A 1 222 ? -31.698 -27.390 46.624  0.50 15.29 ? 222 SER B CB  1 
ATOM   1786 C  CB  B SER A 1 222 ? -31.764 -27.554 46.575  0.50 14.97 ? 222 SER B CB  1 
ATOM   1787 O  OG  A SER A 1 222 ? -32.834 -28.155 46.886  0.50 16.30 ? 222 SER B OG  1 
ATOM   1788 O  OG  B SER A 1 222 ? -30.666 -28.451 46.655  0.50 16.80 ? 222 SER B OG  1 
ATOM   1789 N  N   . GLN A 1 223 ? -33.159 -24.913 45.335  1.00 15.50 ? 223 GLN B N   1 
ATOM   1790 C  CA  . GLN A 1 223 ? -34.325 -24.140 45.208  1.00 15.56 ? 223 GLN B CA  1 
ATOM   1791 C  C   . GLN A 1 223 ? -34.738 -23.989 43.712  1.00 16.73 ? 223 GLN B C   1 
ATOM   1792 O  O   . GLN A 1 223 ? -35.908 -24.017 43.417  1.00 17.49 ? 223 GLN B O   1 
ATOM   1793 C  CB  . GLN A 1 223 ? -34.122 -22.720 45.789  1.00 16.90 ? 223 GLN B CB  1 
ATOM   1794 C  CG  . GLN A 1 223 ? -34.172 -22.711 47.301  1.00 22.07 ? 223 GLN B CG  1 
ATOM   1795 C  CD  . GLN A 1 223 ? -34.277 -21.284 47.839  1.00 22.42 ? 223 GLN B CD  1 
ATOM   1796 O  OE1 . GLN A 1 223 ? -35.030 -20.490 47.339  1.00 21.79 ? 223 GLN B OE1 1 
ATOM   1797 N  NE2 . GLN A 1 223 ? -33.456 -20.962 48.873  1.00 23.85 ? 223 GLN B NE2 1 
ATOM   1798 N  N   . GLN A 1 224 ? -33.749 -23.861 42.850  1.00 16.62 ? 224 GLN B N   1 
ATOM   1799 C  CA  . GLN A 1 224 ? -34.081 -23.734 41.391  1.00 16.30 ? 224 GLN B CA  1 
ATOM   1800 C  C   . GLN A 1 224 ? -34.603 -25.033 40.883  1.00 15.80 ? 224 GLN B C   1 
ATOM   1801 O  O   . GLN A 1 224 ? -35.657 -25.050 40.204  1.00 16.51 ? 224 GLN B O   1 
ATOM   1802 C  CB  . GLN A 1 224 ? -32.854 -23.410 40.538  1.00 13.84 ? 224 GLN B CB  1 
ATOM   1803 C  CG  . GLN A 1 224 ? -32.330 -22.012 40.744  1.00 14.75 ? 224 GLN B CG  1 
ATOM   1804 C  CD  . GLN A 1 224 ? -31.086 -21.751 39.873  1.00 14.10 ? 224 GLN B CD  1 
ATOM   1805 O  OE1 . GLN A 1 224 ? -30.086 -22.453 39.964  1.00 15.98 ? 224 GLN B OE1 1 
ATOM   1806 N  NE2 . GLN A 1 224 ? -31.158 -20.724 38.984  1.00 16.18 ? 224 GLN B NE2 1 
ATOM   1807 N  N   . LEU A 1 225 ? -33.900 -26.130 41.256  1.00 13.54 ? 225 LEU B N   1 
ATOM   1808 C  CA  . LEU A 1 225 ? -34.390 -27.422 40.742  1.00 14.72 ? 225 LEU B CA  1 
ATOM   1809 C  C   . LEU A 1 225 ? -35.810 -27.739 41.201  1.00 16.42 ? 225 LEU B C   1 
ATOM   1810 O  O   . LEU A 1 225 ? -36.649 -28.258 40.428  1.00 17.74 ? 225 LEU B O   1 
ATOM   1811 C  CB  . LEU A 1 225 ? -33.357 -28.557 41.063  1.00 15.26 ? 225 LEU B CB  1 
ATOM   1812 C  CG  . LEU A 1 225 ? -33.670 -29.921 40.470  1.00 17.38 ? 225 LEU B CG  1 
ATOM   1813 C  CD1 . LEU A 1 225 ? -33.787 -29.757 38.976  1.00 18.34 ? 225 LEU B CD1 1 
ATOM   1814 C  CD2 . LEU A 1 225 ? -32.409 -30.684 40.797  1.00 16.59 ? 225 LEU B CD2 1 
ATOM   1815 N  N   . ALA A 1 226 ? -36.165 -27.470 42.476  1.00 15.39 ? 226 ALA B N   1 
ATOM   1816 C  CA  . ALA A 1 226 ? -37.465 -27.735 42.952  1.00 15.33 ? 226 ALA B CA  1 
ATOM   1817 C  C   . ALA A 1 226 ? -38.587 -27.045 42.182  1.00 14.62 ? 226 ALA B C   1 
ATOM   1818 O  O   . ALA A 1 226 ? -39.685 -27.557 42.170  1.00 16.18 ? 226 ALA B O   1 
ATOM   1819 C  CB  . ALA A 1 226 ? -37.543 -27.323 44.446  1.00 18.59 ? 226 ALA B CB  1 
ATOM   1820 N  N   . LYS A 1 227 ? -38.314 -25.893 41.592  1.00 16.94 ? 227 LYS B N   1 
ATOM   1821 C  CA  . LYS A 1 227 ? -39.337 -25.265 40.763  1.00 16.80 ? 227 LYS B CA  1 
ATOM   1822 C  C   . LYS A 1 227 ? -39.806 -26.116 39.593  1.00 15.67 ? 227 LYS B C   1 
ATOM   1823 O  O   . LYS A 1 227 ? -41.025 -26.066 39.244  1.00 15.99 ? 227 LYS B O   1 
ATOM   1824 C  CB  . LYS A 1 227 ? -38.883 -23.869 40.290  1.00 19.03 ? 227 LYS B CB  1 
ATOM   1825 C  CG  . LYS A 1 227 ? -38.424 -23.031 41.492  1.00 23.98 ? 227 LYS B CG  1 
ATOM   1826 C  CD  . LYS A 1 227 ? -37.861 -21.691 41.019  1.00 29.47 ? 227 LYS B CD  1 
ATOM   1827 C  CE  . LYS A 1 227 ? -39.007 -20.776 40.585  1.00 37.64 ? 227 LYS B CE  1 
ATOM   1828 N  NZ  . LYS A 1 227 ? -38.645 -19.316 40.688  1.00 42.76 ? 227 LYS B NZ  1 
ATOM   1829 N  N   . PHE A 1 228 ? -38.893 -26.871 39.000  1.00 15.41 ? 228 PHE B N   1 
ATOM   1830 C  CA  . PHE A 1 228 ? -39.319 -27.725 37.883  1.00 14.03 ? 228 PHE B CA  1 
ATOM   1831 C  C   . PHE A 1 228 ? -40.295 -28.794 38.323  1.00 13.10 ? 228 PHE B C   1 
ATOM   1832 O  O   . PHE A 1 228 ? -41.199 -29.232 37.548  1.00 13.97 ? 228 PHE B O   1 
ATOM   1833 C  CB  . PHE A 1 228 ? -38.074 -28.343 37.213  1.00 13.60 ? 228 PHE B CB  1 
ATOM   1834 C  CG  . PHE A 1 228 ? -37.262 -27.297 36.537  1.00 13.93 ? 228 PHE B CG  1 
ATOM   1835 C  CD1 . PHE A 1 228 ? -36.124 -26.747 37.150  1.00 15.57 ? 228 PHE B CD1 1 
ATOM   1836 C  CD2 . PHE A 1 228 ? -37.642 -26.850 35.253  1.00 14.69 ? 228 PHE B CD2 1 
ATOM   1837 C  CE1 . PHE A 1 228 ? -35.360 -25.797 36.483  1.00 15.51 ? 228 PHE B CE1 1 
ATOM   1838 C  CE2 . PHE A 1 228 ? -36.908 -25.852 34.657  1.00 13.72 ? 228 PHE B CE2 1 
ATOM   1839 C  CZ  . PHE A 1 228 ? -35.738 -25.334 35.250  1.00 16.25 ? 228 PHE B CZ  1 
ATOM   1840 N  N   . ARG A 1 229 ? -40.116 -29.283 39.566  1.00 13.55 ? 229 ARG B N   1 
ATOM   1841 C  CA  . ARG A 1 229 ? -41.032 -30.315 40.033  1.00 15.10 ? 229 ARG B CA  1 
ATOM   1842 C  C   . ARG A 1 229 ? -42.456 -29.805 40.356  1.00 14.53 ? 229 ARG B C   1 
ATOM   1843 O  O   . ARG A 1 229 ? -43.290 -30.640 40.630  1.00 14.58 ? 229 ARG B O   1 
ATOM   1844 C  CB  . ARG A 1 229 ? -40.455 -30.915 41.352  1.00 14.30 ? 229 ARG B CB  1 
ATOM   1845 C  CG  . ARG A 1 229 ? -39.095 -31.480 41.232  1.00 15.62 ? 229 ARG B CG  1 
ATOM   1846 C  CD  . ARG A 1 229 ? -38.744 -32.327 42.492  1.00 14.73 ? 229 ARG B CD  1 
ATOM   1847 N  NE  . ARG A 1 229 ? -37.354 -32.742 42.446  1.00 14.40 ? 229 ARG B NE  1 
ATOM   1848 C  CZ  . ARG A 1 229 ? -36.310 -32.088 43.009  1.00 14.44 ? 229 ARG B CZ  1 
ATOM   1849 N  NH1 . ARG A 1 229 ? -36.589 -31.057 43.847  1.00 14.84 ? 229 ARG B NH1 1 
ATOM   1850 N  NH2 . ARG A 1 229 ? -35.085 -32.510 42.825  1.00 13.62 ? 229 ARG B NH2 1 
ATOM   1851 N  N   . SER A 1 230 ? -42.753 -28.494 40.303  1.00 15.66 ? 230 SER B N   1 
ATOM   1852 C  CA  . SER A 1 230 ? -44.100 -27.923 40.474  1.00 19.65 ? 230 SER B CA  1 
ATOM   1853 C  C   . SER A 1 230 ? -44.860 -27.886 39.129  1.00 18.62 ? 230 SER B C   1 
ATOM   1854 O  O   . SER A 1 230 ? -46.077 -27.574 39.098  1.00 19.72 ? 230 SER B O   1 
ATOM   1855 C  CB  . SER A 1 230 ? -44.055 -26.495 41.059  1.00 23.27 ? 230 SER B CB  1 
ATOM   1856 O  OG  . SER A 1 230 ? -43.611 -25.596 40.061  1.00 36.71 ? 230 SER B OG  1 
ATOM   1857 N  N   . LEU A 1 231 ? -44.168 -28.257 38.038  1.00 16.67 ? 231 LEU B N   1 
ATOM   1858 C  CA  . LEU A 1 231 ? -44.915 -28.370 36.778  1.00 16.18 ? 231 LEU B CA  1 
ATOM   1859 C  C   . LEU A 1 231 ? -45.862 -29.518 36.931  1.00 15.81 ? 231 LEU B C   1 
ATOM   1860 O  O   . LEU A 1 231 ? -45.521 -30.505 37.605  1.00 15.87 ? 231 LEU B O   1 
ATOM   1861 C  CB  . LEU A 1 231 ? -43.985 -28.656 35.538  1.00 14.05 ? 231 LEU B CB  1 
ATOM   1862 C  CG  . LEU A 1 231 ? -43.078 -27.527 35.206  1.00 15.23 ? 231 LEU B CG  1 
ATOM   1863 C  CD1 . LEU A 1 231 ? -42.082 -28.064 34.202  1.00 15.40 ? 231 LEU B CD1 1 
ATOM   1864 C  CD2 . LEU A 1 231 ? -43.848 -26.460 34.450  1.00 16.25 ? 231 LEU B CD2 1 
ATOM   1865 N  N   . LEU A 1 232 ? -46.996 -29.485 36.203  1.00 15.25 ? 232 LEU B N   1 
ATOM   1866 C  CA  . LEU A 1 232 ? -47.943 -30.593 36.184  1.00 16.56 ? 232 LEU B CA  1 
ATOM   1867 C  C   . LEU A 1 232 ? -47.820 -31.462 34.977  1.00 17.42 ? 232 LEU B C   1 
ATOM   1868 O  O   . LEU A 1 232 ? -47.407 -30.933 33.908  1.00 17.36 ? 232 LEU B O   1 
ATOM   1869 C  CB  . LEU A 1 232 ? -49.381 -30.030 36.200  1.00 19.72 ? 232 LEU B CB  1 
ATOM   1870 C  CG  . LEU A 1 232 ? -49.681 -29.110 37.363  1.00 20.91 ? 232 LEU B CG  1 
ATOM   1871 C  CD1 . LEU A 1 232 ? -51.150 -28.755 37.309  1.00 23.28 ? 232 LEU B CD1 1 
ATOM   1872 C  CD2 . LEU A 1 232 ? -49.410 -29.899 38.643  1.00 20.93 ? 232 LEU B CD2 1 
ATOM   1873 N  N   . CYS A 1 233 ? -48.126 -32.730 35.141  1.00 18.09 ? 233 CYS B N   1 
ATOM   1874 C  CA  . CYS A 1 233 ? -48.168 -33.659 33.962  1.00 18.29 ? 233 CYS B CA  1 
ATOM   1875 C  C   . CYS A 1 233 ? -49.612 -33.765 33.480  1.00 20.26 ? 233 CYS B C   1 
ATOM   1876 O  O   . CYS A 1 233 ? -49.913 -34.543 32.557  1.00 20.13 ? 233 CYS B O   1 
ATOM   1877 C  CB  . CYS A 1 233 ? -47.555 -35.031 34.179  1.00 17.48 ? 233 CYS B CB  1 
ATOM   1878 S  SG  . CYS A 1 233 ? -48.384 -35.967 35.551  1.00 23.25 ? 233 CYS B SG  1 
ATOM   1879 N  N   . THR A 1 234 ? -50.472 -33.013 34.146  1.00 20.34 ? 234 THR B N   1 
ATOM   1880 C  CA  . THR A 1 234 ? -51.892 -32.952 33.826  1.00 22.00 ? 234 THR B CA  1 
ATOM   1881 C  C   . THR A 1 234 ? -52.303 -31.587 33.229  1.00 21.97 ? 234 THR B C   1 
ATOM   1882 O  O   . THR A 1 234 ? -51.722 -30.551 33.449  1.00 21.35 ? 234 THR B O   1 
ATOM   1883 C  CB  . THR A 1 234 ? -52.723 -33.247 35.097  1.00 20.29 ? 234 THR B CB  1 
ATOM   1884 O  OG1 . THR A 1 234 ? -52.250 -32.375 36.143  1.00 22.46 ? 234 THR B OG1 1 
ATOM   1885 C  CG2 . THR A 1 234 ? -52.598 -34.732 35.466  1.00 22.86 ? 234 THR B CG2 1 
ATOM   1886 N  N   . ALA A 1 235 ? -53.382 -31.618 32.437  1.00 23.15 ? 235 ALA B N   1 
ATOM   1887 C  CA  . ALA A 1 235 ? -53.907 -30.454 31.801  1.00 27.77 ? 235 ALA B CA  1 
ATOM   1888 C  C   . ALA A 1 235 ? -54.891 -29.699 32.746  1.00 30.04 ? 235 ALA B C   1 
ATOM   1889 O  O   . ALA A 1 235 ? -55.388 -30.289 33.695  1.00 34.92 ? 235 ALA B O   1 
ATOM   1890 C  CB  . ALA A 1 235 ? -54.550 -30.881 30.445  1.00 27.06 ? 235 ALA B CB  1 
ATOM   1891 N  N   . GLU A 1 236 ? -55.064 -28.403 32.555  1.00 33.94 ? 236 GLU B N   1 
ATOM   1892 C  CA  . GLU A 1 236 ? -56.126 -27.622 33.190  1.00 38.95 ? 236 GLU B CA  1 
ATOM   1893 C  C   . GLU A 1 236 ? -57.481 -28.379 33.240  1.00 40.77 ? 236 GLU B C   1 
ATOM   1894 O  O   . GLU A 1 236 ? -57.912 -28.957 32.223  1.00 36.55 ? 236 GLU B O   1 
ATOM   1895 C  CB  . GLU A 1 236 ? -56.337 -26.362 32.367  1.00 41.48 ? 236 GLU B CB  1 
ATOM   1896 C  CG  . GLU A 1 236 ? -56.736 -25.144 33.161  1.00 47.64 ? 236 GLU B CG  1 
ATOM   1897 C  CD  . GLU A 1 236 ? -56.419 -23.893 32.366  1.00 57.99 ? 236 GLU B CD  1 
ATOM   1898 O  OE1 . GLU A 1 236 ? -56.712 -23.889 31.134  1.00 50.25 ? 236 GLU B OE1 1 
ATOM   1899 O  OE2 . GLU A 1 236 ? -55.860 -22.937 32.964  1.00 57.38 ? 236 GLU B OE2 1 
ATOM   1900 N  N   . GLY A 1 237 ? -58.125 -28.377 34.412  1.00 43.12 ? 237 GLY B N   1 
ATOM   1901 C  CA  . GLY A 1 237 ? -59.466 -28.961 34.570  1.00 44.54 ? 237 GLY B CA  1 
ATOM   1902 C  C   . GLY A 1 237 ? -59.438 -30.446 34.887  1.00 52.09 ? 237 GLY B C   1 
ATOM   1903 O  O   . GLY A 1 237 ? -60.491 -31.107 34.928  1.00 50.39 ? 237 GLY B O   1 
ATOM   1904 N  N   . GLU A 1 238 ? -58.227 -30.969 35.091  1.00 45.04 ? 238 GLU B N   1 
ATOM   1905 C  CA  . GLU A 1 238 ? -57.982 -32.393 35.257  1.00 45.59 ? 238 GLU B CA  1 
ATOM   1906 C  C   . GLU A 1 238 ? -57.385 -32.414 36.693  1.00 46.72 ? 238 GLU B C   1 
ATOM   1907 O  O   . GLU A 1 238 ? -56.818 -31.403 37.132  1.00 40.39 ? 238 GLU B O   1 
ATOM   1908 C  CB  . GLU A 1 238 ? -57.062 -32.897 34.109  1.00 46.58 ? 238 GLU B CB  1 
ATOM   1909 C  CG  . GLU A 1 238 ? -56.641 -34.364 34.132  1.00 45.99 ? 238 GLU B CG  1 
ATOM   1910 C  CD  . GLU A 1 238 ? -55.554 -34.766 33.114  1.00 54.58 ? 238 GLU B CD  1 
ATOM   1911 O  OE1 . GLU A 1 238 ? -55.212 -34.008 32.168  1.00 49.02 ? 238 GLU B OE1 1 
ATOM   1912 O  OE2 . GLU A 1 238 ? -55.023 -35.903 33.238  1.00 57.26 ? 238 GLU B OE2 1 
ATOM   1913 N  N   . ALA A 1 239 ? -57.634 -33.472 37.476  1.00 43.59 ? 239 ALA B N   1 
ATOM   1914 C  CA  . ALA A 1 239 ? -57.060 -33.556 38.841  1.00 35.46 ? 239 ALA B CA  1 
ATOM   1915 C  C   . ALA A 1 239 ? -55.526 -33.443 38.691  1.00 29.13 ? 239 ALA B C   1 
ATOM   1916 O  O   . ALA A 1 239 ? -54.930 -34.188 37.876  1.00 31.11 ? 239 ALA B O   1 
ATOM   1917 C  CB  . ALA A 1 239 ? -57.443 -34.874 39.510  1.00 32.77 ? 239 ALA B CB  1 
ATOM   1918 N  N   . ALA A 1 240 ? -54.944 -32.512 39.444  1.00 32.39 ? 240 ALA B N   1 
ATOM   1919 C  CA  . ALA A 1 240 ? -53.521 -32.244 39.342  1.00 27.81 ? 240 ALA B CA  1 
ATOM   1920 C  C   . ALA A 1 240 ? -52.643 -33.452 39.706  1.00 28.90 ? 240 ALA B C   1 
ATOM   1921 O  O   . ALA A 1 240 ? -52.898 -34.189 40.678  1.00 23.89 ? 240 ALA B O   1 
ATOM   1922 C  CB  . ALA A 1 240 ? -53.141 -30.991 40.119  1.00 31.35 ? 240 ALA B CB  1 
ATOM   1923 N  N   . ALA A 1 241 ? -51.564 -33.641 38.928  1.00 21.51 ? 241 ALA B N   1 
ATOM   1924 C  CA  . ALA A 1 241 ? -50.534 -34.541 39.331  1.00 19.00 ? 241 ALA B CA  1 
ATOM   1925 C  C   . ALA A 1 241 ? -49.247 -33.833 38.952  1.00 18.83 ? 241 ALA B C   1 
ATOM   1926 O  O   . ALA A 1 241 ? -49.241 -33.189 37.878  1.00 20.64 ? 241 ALA B O   1 
ATOM   1927 C  CB  . ALA A 1 241 ? -50.607 -35.869 38.621  1.00 19.05 ? 241 ALA B CB  1 
ATOM   1928 N  N   . PHE A 1 242 ? -48.199 -33.963 39.780  1.00 16.40 ? 242 PHE B N   1 
ATOM   1929 C  CA  . PHE A 1 242 ? -46.968 -33.195 39.587  1.00 15.04 ? 242 PHE B CA  1 
ATOM   1930 C  C   . PHE A 1 242 ? -45.886 -33.989 38.880  1.00 14.14 ? 242 PHE B C   1 
ATOM   1931 O  O   . PHE A 1 242 ? -45.694 -35.211 39.093  1.00 16.20 ? 242 PHE B O   1 
ATOM   1932 C  CB  . PHE A 1 242 ? -46.391 -32.799 40.997  1.00 14.33 ? 242 PHE B CB  1 
ATOM   1933 C  CG  . PHE A 1 242 ? -47.250 -31.784 41.661  1.00 17.13 ? 242 PHE B CG  1 
ATOM   1934 C  CD1 . PHE A 1 242 ? -48.324 -32.272 42.429  1.00 19.90 ? 242 PHE B CD1 1 
ATOM   1935 C  CD2 . PHE A 1 242 ? -47.098 -30.383 41.449  1.00 19.62 ? 242 PHE B CD2 1 
ATOM   1936 C  CE1 . PHE A 1 242 ? -49.171 -31.364 43.074  1.00 22.80 ? 242 PHE B CE1 1 
ATOM   1937 C  CE2 . PHE A 1 242 ? -47.966 -29.474 42.095  1.00 25.30 ? 242 PHE B CE2 1 
ATOM   1938 C  CZ  . PHE A 1 242 ? -49.002 -30.014 42.903  1.00 20.23 ? 242 PHE B CZ  1 
ATOM   1939 N  N   . LEU A 1 243 ? -45.095 -33.280 38.049  1.00 13.21 ? 243 LEU B N   1 
ATOM   1940 C  CA  . LEU A 1 243 ? -44.000 -33.915 37.330  1.00 12.92 ? 243 LEU B CA  1 
ATOM   1941 C  C   . LEU A 1 243 ? -42.774 -33.831 38.288  1.00 13.39 ? 243 LEU B C   1 
ATOM   1942 O  O   . LEU A 1 243 ? -41.808 -33.116 38.030  1.00 13.93 ? 243 LEU B O   1 
ATOM   1943 C  CB  . LEU A 1 243 ? -43.813 -33.089 35.993  1.00 13.92 ? 243 LEU B CB  1 
ATOM   1944 C  CG  . LEU A 1 243 ? -42.754 -33.675 35.077  1.00 14.03 ? 243 LEU B CG  1 
ATOM   1945 C  CD1 . LEU A 1 243 ? -43.160 -35.054 34.564  1.00 13.67 ? 243 LEU B CD1 1 
ATOM   1946 C  CD2 . LEU A 1 243 ? -42.726 -32.644 33.879  1.00 15.74 ? 243 LEU B CD2 1 
ATOM   1947 N  N   . VAL A 1 244 ? -42.768 -34.674 39.319  1.00 14.13 ? 244 VAL B N   1 
ATOM   1948 C  CA  . VAL A 1 244 ? -41.642 -34.644 40.233  1.00 14.07 ? 244 VAL B CA  1 
ATOM   1949 C  C   . VAL A 1 244 ? -40.431 -35.392 39.758  1.00 12.47 ? 244 VAL B C   1 
ATOM   1950 O  O   . VAL A 1 244 ? -39.341 -35.167 40.306  1.00 12.79 ? 244 VAL B O   1 
ATOM   1951 C  CB  . VAL A 1 244 ? -42.062 -35.148 41.657  1.00 17.11 ? 244 VAL B CB  1 
ATOM   1952 C  CG1 . VAL A 1 244 ? -43.106 -34.184 42.278  1.00 17.20 ? 244 VAL B CG1 1 
ATOM   1953 C  CG2 . VAL A 1 244 ? -42.560 -36.560 41.649  1.00 17.65 ? 244 VAL B CG2 1 
ATOM   1954 N  N   . SER A 1 245 ? -40.582 -36.276 38.737  1.00 11.61 ? 245 SER B N   1 
ATOM   1955 C  CA  . SER A 1 245 ? -39.456 -37.003 38.262  1.00 12.50 ? 245 SER B CA  1 
ATOM   1956 C  C   . SER A 1 245 ? -39.805 -37.325 36.801  1.00 11.59 ? 245 SER B C   1 
ATOM   1957 O  O   . SER A 1 245 ? -40.929 -37.704 36.475  1.00 11.55 ? 245 SER B O   1 
ATOM   1958 C  CB  . SER A 1 245 ? -39.316 -38.294 39.093  1.00 13.45 ? 245 SER B CB  1 
ATOM   1959 O  OG  . SER A 1 245 ? -38.151 -39.017 38.736  1.00 15.07 ? 245 SER B OG  1 
ATOM   1960 N  N   . ASN A 1 246 ? -38.765 -37.266 35.964  1.00 11.34 ? 246 ASN B N   1 
ATOM   1961 C  CA  . ASN A 1 246 ? -39.022 -37.496 34.524  1.00 10.48 ? 246 ASN B CA  1 
ATOM   1962 C  C   . ASN A 1 246 ? -37.770 -38.032 33.863  1.00 11.39 ? 246 ASN B C   1 
ATOM   1963 O  O   . ASN A 1 246 ? -37.451 -37.597 32.757  1.00 11.61 ? 246 ASN B O   1 
ATOM   1964 C  CB  . ASN A 1 246 ? -39.553 -36.230 33.868  1.00 10.65 ? 246 ASN B CB  1 
ATOM   1965 C  CG  . ASN A 1 246 ? -38.528 -35.148 33.828  1.00 10.18 ? 246 ASN B CG  1 
ATOM   1966 O  OD1 . ASN A 1 246 ? -37.522 -35.250 34.499  1.00 11.31 ? 246 ASN B OD1 1 
ATOM   1967 N  ND2 . ASN A 1 246 ? -38.774 -34.103 33.056  1.00 11.39 ? 246 ASN B ND2 1 
ATOM   1968 N  N   . HIS A 1 247 ? -37.040 -38.949 34.496  1.00 10.91 ? 247 HIS B N   1 
ATOM   1969 C  CA  . HIS A 1 247 ? -35.820 -39.543 33.970  1.00 11.92 ? 247 HIS B CA  1 
ATOM   1970 C  C   . HIS A 1 247 ? -35.955 -41.026 33.745  1.00 12.01 ? 247 HIS B C   1 
ATOM   1971 O  O   . HIS A 1 247 ? -36.499 -41.786 34.637  1.00 14.40 ? 247 HIS B O   1 
ATOM   1972 C  CB  . HIS A 1 247 ? -34.582 -39.148 34.827  1.00 10.77 ? 247 HIS B CB  1 
ATOM   1973 C  CG  . HIS A 1 247 ? -34.612 -39.742 36.224  1.00 11.83 ? 247 HIS B CG  1 
ATOM   1974 N  ND1 . HIS A 1 247 ? -33.937 -40.865 36.535  1.00 14.51 ? 247 HIS B ND1 1 
ATOM   1975 C  CD2 . HIS A 1 247 ? -35.331 -39.361 37.320  1.00 12.18 ? 247 HIS B CD2 1 
ATOM   1976 C  CE1 . HIS A 1 247 ? -34.189 -41.158 37.855  1.00 16.47 ? 247 HIS B CE1 1 
ATOM   1977 N  NE2 . HIS A 1 247 ? -35.038 -40.275 38.316  1.00 16.34 ? 247 HIS B NE2 1 
ATOM   1978 N  N   . ARG A 1 248 ? -35.453 -41.512 32.614  1.00 12.28 ? 248 ARG B N   1 
ATOM   1979 C  CA  . ARG A 1 248 ? -35.437 -42.969 32.352  1.00 12.64 ? 248 ARG B CA  1 
ATOM   1980 C  C   . ARG A 1 248 ? -34.130 -43.532 32.918  1.00 12.83 ? 248 ARG B C   1 
ATOM   1981 O  O   . ARG A 1 248 ? -33.047 -42.953 32.781  1.00 12.74 ? 248 ARG B O   1 
ATOM   1982 C  CB  . ARG A 1 248 ? -35.465 -43.137 30.798  1.00 12.80 ? 248 ARG B CB  1 
ATOM   1983 C  CG  . ARG A 1 248 ? -35.547 -44.656 30.432  1.00 13.11 ? 248 ARG B CG  1 
ATOM   1984 C  CD  . ARG A 1 248 ? -35.350 -44.905 28.943  1.00 12.00 ? 248 ARG B CD  1 
ATOM   1985 N  NE  . ARG A 1 248 ? -35.852 -46.295 28.691  1.00 13.70 ? 248 ARG B NE  1 
ATOM   1986 C  CZ  . ARG A 1 248 ? -35.624 -46.964 27.556  1.00 16.55 ? 248 ARG B CZ  1 
ATOM   1987 N  NH1 . ARG A 1 248 ? -34.864 -46.472 26.579  1.00 14.23 ? 248 ARG B NH1 1 
ATOM   1988 N  NH2 . ARG A 1 248 ? -36.247 -48.117 27.386  1.00 16.83 ? 248 ARG B NH2 1 
ATOM   1989 N  N   . PRO A 1 249 ? -34.166 -44.753 33.517  1.00 13.38 ? 249 PRO B N   1 
ATOM   1990 C  CA  . PRO A 1 249 ? -32.895 -45.371 33.958  1.00 13.68 ? 249 PRO B CA  1 
ATOM   1991 C  C   . PRO A 1 249 ? -32.025 -45.807 32.785  1.00 14.57 ? 249 PRO B C   1 
ATOM   1992 O  O   . PRO A 1 249 ? -32.574 -46.034 31.685  1.00 14.04 ? 249 PRO B O   1 
ATOM   1993 C  CB  . PRO A 1 249 ? -33.373 -46.672 34.690  1.00 16.06 ? 249 PRO B CB  1 
ATOM   1994 C  CG  . PRO A 1 249 ? -34.818 -46.403 35.027  1.00 16.65 ? 249 PRO B CG  1 
ATOM   1995 C  CD  . PRO A 1 249 ? -35.410 -45.426 33.933  1.00 14.55 ? 249 PRO B CD  1 
ATOM   1996 N  N   . PRO A 1 250 ? -30.717 -45.905 32.968  1.00 13.72 ? 250 PRO B N   1 
ATOM   1997 C  CA  . PRO A 1 250 ? -29.811 -46.369 31.925  1.00 14.76 ? 250 PRO B CA  1 
ATOM   1998 C  C   . PRO A 1 250 ? -30.235 -47.761 31.490  1.00 15.64 ? 250 PRO B C   1 
ATOM   1999 O  O   . PRO A 1 250 ? -30.659 -48.611 32.356  1.00 16.34 ? 250 PRO B O   1 
ATOM   2000 C  CB  . PRO A 1 250 ? -28.430 -46.461 32.654  1.00 14.82 ? 250 PRO B CB  1 
ATOM   2001 C  CG  . PRO A 1 250 ? -28.526 -45.371 33.724  1.00 15.79 ? 250 PRO B CG  1 
ATOM   2002 C  CD  . PRO A 1 250 ? -29.932 -45.428 34.186  1.00 16.27 ? 250 PRO B CD  1 
ATOM   2003 N  N   . GLN A 1 251 ? -30.015 -48.020 30.209  1.00 13.79 ? 251 GLN B N   1 
ATOM   2004 C  CA  . GLN A 1 251 ? -30.270 -49.326 29.587  1.00 14.72 ? 251 GLN B CA  1 
ATOM   2005 C  C   . GLN A 1 251 ? -28.899 -49.917 29.265  1.00 13.50 ? 251 GLN B C   1 
ATOM   2006 O  O   . GLN A 1 251 ? -27.878 -49.227 29.147  1.00 14.05 ? 251 GLN B O   1 
ATOM   2007 C  CB  . GLN A 1 251 ? -31.111 -49.072 28.327  1.00 15.83 ? 251 GLN B CB  1 
ATOM   2008 C  CG  . GLN A 1 251 ? -32.437 -48.349 28.668  1.00 14.43 ? 251 GLN B CG  1 
ATOM   2009 C  CD  . GLN A 1 251 ? -33.295 -49.112 29.666  1.00 17.60 ? 251 GLN B CD  1 
ATOM   2010 O  OE1 . GLN A 1 251 ? -33.582 -50.341 29.479  1.00 20.05 ? 251 GLN B OE1 1 
ATOM   2011 N  NE2 . GLN A 1 251 ? -33.655 -48.464 30.780  1.00 17.86 ? 251 GLN B NE2 1 
ATOM   2012 N  N   . PRO A 1 252 ? -28.877 -51.258 29.029  1.00 17.24 ? 252 PRO B N   1 
ATOM   2013 C  CA  . PRO A 1 252 ? -27.609 -51.957 28.800  1.00 18.15 ? 252 PRO B CA  1 
ATOM   2014 C  C   . PRO A 1 252 ? -27.014 -51.567 27.456  1.00 16.99 ? 252 PRO B C   1 
ATOM   2015 O  O   . PRO A 1 252 ? -27.787 -51.354 26.455  1.00 17.76 ? 252 PRO B O   1 
ATOM   2016 C  CB  . PRO A 1 252 ? -28.020 -53.445 28.839  1.00 18.58 ? 252 PRO B CB  1 
ATOM   2017 C  CG  . PRO A 1 252 ? -29.251 -53.453 29.624  1.00 18.95 ? 252 PRO B CG  1 
ATOM   2018 C  CD  . PRO A 1 252 ? -29.993 -52.175 29.217  1.00 19.19 ? 252 PRO B CD  1 
ATOM   2019 N  N   A LEU A 1 253 ? -25.680 -51.493 27.427  0.50 18.04 ? 253 LEU B N   1 
ATOM   2020 N  N   B LEU A 1 253 ? -25.685 -51.520 27.415  0.50 17.32 ? 253 LEU B N   1 
ATOM   2021 C  CA  A LEU A 1 253 ? -24.907 -51.173 26.210  0.50 17.92 ? 253 LEU B CA  1 
ATOM   2022 C  CA  B LEU A 1 253 ? -24.903 -51.245 26.196  0.50 16.67 ? 253 LEU B CA  1 
ATOM   2023 C  C   A LEU A 1 253 ? -25.035 -52.204 25.114  0.50 19.12 ? 253 LEU B C   1 
ATOM   2024 C  C   B LEU A 1 253 ? -25.138 -52.216 25.100  0.50 18.74 ? 253 LEU B C   1 
ATOM   2025 O  O   A LEU A 1 253 ? -24.925 -51.834 23.936  0.50 19.00 ? 253 LEU B O   1 
ATOM   2026 O  O   B LEU A 1 253 ? -25.168 -51.845 23.925  0.50 19.84 ? 253 LEU B O   1 
ATOM   2027 C  CB  A LEU A 1 253 ? -23.398 -50.876 26.495  0.50 22.59 ? 253 LEU B CB  1 
ATOM   2028 C  CB  B LEU A 1 253 ? -23.400 -51.277 26.500  0.50 19.99 ? 253 LEU B CB  1 
ATOM   2029 C  CG  A LEU A 1 253 ? -22.856 -49.435 26.593  0.50 23.84 ? 253 LEU B CG  1 
ATOM   2030 C  CG  B LEU A 1 253 ? -23.029 -50.021 27.245  0.50 18.52 ? 253 LEU B CG  1 
ATOM   2031 C  CD1 A LEU A 1 253 ? -23.174 -48.551 25.388  0.50 22.08 ? 253 LEU B CD1 1 
ATOM   2032 C  CD1 B LEU A 1 253 ? -21.539 -50.016 27.559  0.50 19.53 ? 253 LEU B CD1 1 
ATOM   2033 C  CD2 A LEU A 1 253 ? -23.409 -48.791 27.857  0.50 24.74 ? 253 LEU B CD2 1 
ATOM   2034 C  CD2 B LEU A 1 253 ? -23.388 -48.769 26.432  0.50 19.44 ? 253 LEU B CD2 1 
ATOM   2035 N  N   . LYS A 1 254 ? -25.252 -53.475 25.488  1.00 19.04 ? 254 LYS B N   1 
ATOM   2036 C  CA  . LYS A 1 254 ? -25.476 -54.543 24.532  1.00 22.37 ? 254 LYS B CA  1 
ATOM   2037 C  C   . LYS A 1 254 ? -24.472 -54.540 23.406  1.00 22.09 ? 254 LYS B C   1 
ATOM   2038 O  O   . LYS A 1 254 ? -24.895 -54.816 22.283  1.00 27.12 ? 254 LYS B O   1 
ATOM   2039 C  CB  . LYS A 1 254 ? -26.904 -54.483 23.955  1.00 26.53 ? 254 LYS B CB  1 
ATOM   2040 C  CG  . LYS A 1 254 ? -27.843 -55.215 24.862  1.00 29.68 ? 254 LYS B CG  1 
ATOM   2041 C  CD  . LYS A 1 254 ? -29.275 -54.876 24.687  1.00 37.11 ? 254 LYS B CD  1 
ATOM   2042 C  CE  . LYS A 1 254 ? -30.050 -55.807 25.608  1.00 39.69 ? 254 LYS B CE  1 
ATOM   2043 N  NZ  . LYS A 1 254 ? -31.431 -55.550 25.107  1.00 39.80 ? 254 LYS B NZ  1 
ATOM   2044 N  N   . GLY A 1 255 ? -23.183 -54.307 23.718  1.00 21.44 ? 255 GLY B N   1 
ATOM   2045 C  CA  . GLY A 1 255 ? -22.133 -54.456 22.693  1.00 22.85 ? 255 GLY B CA  1 
ATOM   2046 C  C   . GLY A 1 255 ? -21.607 -53.148 22.161  1.00 21.99 ? 255 GLY B C   1 
ATOM   2047 O  O   . GLY A 1 255 ? -20.493 -53.052 21.589  1.00 22.10 ? 255 GLY B O   1 
ATOM   2048 N  N   . ARG A 1 256 ? -22.379 -52.051 22.363  1.00 20.67 ? 256 ARG B N   1 
ATOM   2049 C  CA  . ARG A 1 256 ? -21.858 -50.774 21.900  1.00 19.97 ? 256 ARG B CA  1 
ATOM   2050 C  C   . ARG A 1 256 ? -20.657 -50.212 22.656  1.00 20.02 ? 256 ARG B C   1 
ATOM   2051 O  O   . ARG A 1 256 ? -20.545 -50.435 23.881  1.00 25.71 ? 256 ARG B O   1 
ATOM   2052 C  CB  . ARG A 1 256 ? -22.975 -49.679 22.066  1.00 20.44 ? 256 ARG B CB  1 
ATOM   2053 C  CG  . ARG A 1 256 ? -24.147 -49.919 21.120  1.00 18.38 ? 256 ARG B CG  1 
ATOM   2054 C  CD  . ARG A 1 256 ? -25.335 -48.982 21.563  1.00 17.59 ? 256 ARG B CD  1 
ATOM   2055 N  NE  . ARG A 1 256 ? -25.917 -49.371 22.853  1.00 17.57 ? 256 ARG B NE  1 
ATOM   2056 C  CZ  . ARG A 1 256 ? -26.864 -48.660 23.463  1.00 17.09 ? 256 ARG B CZ  1 
ATOM   2057 N  NH1 . ARG A 1 256 ? -27.225 -47.480 22.917  1.00 15.02 ? 256 ARG B NH1 1 
ATOM   2058 N  NH2 . ARG A 1 256 ? -27.449 -49.058 24.550  1.00 14.41 ? 256 ARG B NH2 1 
ATOM   2059 N  N   . LYS A 1 257 ? -19.807 -49.474 21.987  1.00 22.18 ? 257 LYS B N   1 
ATOM   2060 C  CA  . LYS A 1 257 ? -18.722 -48.894 22.714  1.00 24.24 ? 257 LYS B CA  1 
ATOM   2061 C  C   . LYS A 1 257 ? -18.882 -47.326 22.750  1.00 24.51 ? 257 LYS B C   1 
ATOM   2062 O  O   . LYS A 1 257 ? -19.472 -46.677 21.861  1.00 26.93 ? 257 LYS B O   1 
ATOM   2063 C  CB  . LYS A 1 257 ? -17.367 -49.292 22.156  1.00 29.73 ? 257 LYS B CB  1 
ATOM   2064 C  CG  . LYS A 1 257 ? -16.987 -50.782 22.271  1.00 29.09 ? 257 LYS B CG  1 
ATOM   2065 C  CD  . LYS A 1 257 ? -15.813 -51.043 21.319  1.00 34.64 ? 257 LYS B CD  1 
ATOM   2066 C  CE  . LYS A 1 257 ? -15.410 -52.504 21.186  1.00 31.23 ? 257 LYS B CE  1 
ATOM   2067 N  NZ  . LYS A 1 257 ? -16.493 -53.293 20.576  1.00 39.22 ? 257 LYS B NZ  1 
ATOM   2068 N  N   . VAL A 1 258 ? -18.433 -46.754 23.842  1.00 23.96 ? 258 VAL B N   1 
ATOM   2069 C  CA  . VAL A 1 258 ? -18.493 -45.342 24.042  1.00 21.40 ? 258 VAL B CA  1 
ATOM   2070 C  C   . VAL A 1 258 ? -17.121 -44.738 23.696  1.00 21.63 ? 258 VAL B C   1 
ATOM   2071 O  O   . VAL A 1 258 ? -16.107 -45.293 24.186  1.00 26.64 ? 258 VAL B O   1 
ATOM   2072 C  CB  . VAL A 1 258 ? -18.871 -45.059 25.492  1.00 19.54 ? 258 VAL B CB  1 
ATOM   2073 C  CG1 . VAL A 1 258 ? -18.885 -43.545 25.763  1.00 21.73 ? 258 VAL B CG1 1 
ATOM   2074 C  CG2 . VAL A 1 258 ? -20.197 -45.735 25.868  1.00 19.34 ? 258 VAL B CG2 1 
ATOM   2075 N  N   . ARG A 1 259 ? -17.064 -43.706 22.870  1.00 21.18 ? 259 ARG B N   1 
ATOM   2076 C  CA  . ARG A 1 259 ? -15.813 -42.945 22.553  1.00 20.91 ? 259 ARG B CA  1 
ATOM   2077 C  C   . ARG A 1 259 ? -15.631 -41.676 23.332  1.00 22.42 ? 259 ARG B C   1 
ATOM   2078 O  O   . ARG A 1 259 ? -16.616 -41.004 23.613  1.00 20.03 ? 259 ARG B O   1 
ATOM   2079 C  CB  . ARG A 1 259 ? -15.734 -42.601 21.053  1.00 25.50 ? 259 ARG B CB  1 
ATOM   2080 C  CG  . ARG A 1 259 ? -15.719 -43.883 20.231  1.00 25.88 ? 259 ARG B CG  1 
ATOM   2081 C  CD  . ARG A 1 259 ? -15.663 -43.524 18.747  1.00 30.41 ? 259 ARG B CD  1 
ATOM   2082 N  NE  . ARG A 1 259 ? -16.942 -42.925 18.303  1.00 32.44 ? 259 ARG B NE  1 
ATOM   2083 C  CZ  . ARG A 1 259 ? -17.046 -42.114 17.250  1.00 32.19 ? 259 ARG B CZ  1 
ATOM   2084 N  NH1 . ARG A 1 259 ? -15.972 -41.757 16.562  1.00 31.52 ? 259 ARG B NH1 1 
ATOM   2085 N  NH2 . ARG A 1 259 ? -18.228 -41.611 16.909  1.00 28.46 ? 259 ARG B NH2 1 
ATOM   2086 N  N   . ALA A 1 260 ? -14.399 -41.209 23.536  1.00 18.00 ? 260 ALA B N   1 
ATOM   2087 C  CA  . ALA A 1 260 ? -14.187 -39.949 24.250  1.00 20.36 ? 260 ALA B CA  1 
ATOM   2088 C  C   . ALA A 1 260 ? -13.487 -38.978 23.318  1.00 21.11 ? 260 ALA B C   1 
ATOM   2089 O  O   . ALA A 1 260 ? -12.614 -39.422 22.519  1.00 22.10 ? 260 ALA B O   1 
ATOM   2090 C  CB  . ALA A 1 260 ? -13.306 -40.132 25.492  1.00 21.45 ? 260 ALA B CB  1 
ATOM   2091 N  N   . SER A 1 261 ? -13.783 -37.673 23.479  1.00 19.55 ? 261 SER B N   1 
ATOM   2092 C  CA  . SER A 1 261 ? -13.225 -36.606 22.682  1.00 20.47 ? 261 SER B CA  1 
ATOM   2093 C  C   . SER A 1 261 ? -11.856 -36.159 23.239  1.00 24.18 ? 261 SER B C   1 
ATOM   2094 O  O   . SER A 1 261 ? -11.194 -35.254 22.651  1.00 25.25 ? 261 SER B O   1 
ATOM   2095 C  CB  . SER A 1 261 ? -14.128 -35.387 22.707  1.00 18.51 ? 261 SER B CB  1 
ATOM   2096 O  OG  . SER A 1 261 ? -14.075 -34.638 23.891  1.00 17.12 ? 261 SER B OG  1 
ATOM   2097 N  N   . PHE A 1 262 ? -11.462 -36.728 24.381  1.00 20.64 ? 262 PHE B N   1 
ATOM   2098 C  CA  . PHE A 1 262 ? -10.405 -36.116 25.207  1.00 24.08 ? 262 PHE B CA  1 
ATOM   2099 C  C   . PHE A 1 262 ? -9.558  -37.273 25.791  1.00 26.00 ? 262 PHE B C   1 
ATOM   2100 O  O   . PHE A 1 262 ? -10.011 -38.387 25.886  1.00 25.22 ? 262 PHE B O   1 
ATOM   2101 C  CB  . PHE A 1 262 ? -11.019 -35.226 26.325  1.00 24.35 ? 262 PHE B CB  1 
ATOM   2102 C  CG  . PHE A 1 262 ? -11.884 -36.000 27.258  1.00 25.45 ? 262 PHE B CG  1 
ATOM   2103 C  CD1 . PHE A 1 262 ? -11.348 -36.592 28.411  1.00 25.14 ? 262 PHE B CD1 1 
ATOM   2104 C  CD2 . PHE A 1 262 ? -13.246 -36.209 26.967  1.00 19.67 ? 262 PHE B CD2 1 
ATOM   2105 C  CE1 . PHE A 1 262 ? -12.153 -37.354 29.234  1.00 26.70 ? 262 PHE B CE1 1 
ATOM   2106 C  CE2 . PHE A 1 262 ? -14.030 -36.978 27.778  1.00 23.09 ? 262 PHE B CE2 1 
ATOM   2107 C  CZ  . PHE A 1 262 ? -13.513 -37.547 28.922  1.00 27.65 ? 262 PHE B CZ  1 
ATOM   2108 N  N   . HIS A 1 263 ? -8.265  -37.024 26.036  1.00 31.22 ? 263 HIS B N   1 
ATOM   2109 C  CA  . HIS A 1 263 ? -7.449  -38.081 26.692  1.00 43.75 ? 263 HIS B CA  1 
ATOM   2110 C  C   . HIS A 1 263 ? -6.574  -37.538 27.746  1.00 53.41 ? 263 HIS B C   1 
ATOM   2111 O  O   . HIS A 1 263 ? -6.266  -38.261 28.706  1.00 58.12 ? 263 HIS B O   1 
ATOM   2112 C  CB  . HIS A 1 263 ? -6.622  -38.924 25.711  1.00 52.03 ? 263 HIS B CB  1 
ATOM   2113 C  CG  . HIS A 1 263 ? -5.712  -38.125 24.784  1.00 55.74 ? 263 HIS B CG  1 
ATOM   2114 N  ND1 . HIS A 1 263 ? -5.734  -36.775 24.704  1.00 63.64 ? 263 HIS B ND1 1 
ATOM   2115 C  CD2 . HIS A 1 263 ? -4.783  -38.555 23.831  1.00 63.10 ? 263 HIS B CD2 1 
ATOM   2116 C  CE1 . HIS A 1 263 ? -4.847  -36.359 23.764  1.00 66.72 ? 263 HIS B CE1 1 
ATOM   2117 N  NE2 . HIS A 1 263 ? -4.262  -37.450 23.236  1.00 67.16 ? 263 HIS B NE2 1 
ATOM   2118 O  OXT . HIS A 1 263 ? -6.160  -36.378 27.627  1.00 55.21 ? 263 HIS B OXT 1 
ATOM   2119 N  N   . SER B 1 6   ? -0.333  11.095  14.814  1.00 46.87 ? 6   SER A N   1 
ATOM   2120 C  CA  . SER B 1 6   ? 0.103   11.528  13.432  1.00 49.63 ? 6   SER A CA  1 
ATOM   2121 C  C   . SER B 1 6   ? 0.670   10.406  12.515  1.00 47.83 ? 6   SER A C   1 
ATOM   2122 O  O   . SER B 1 6   ? 1.004   10.633  11.341  1.00 50.92 ? 6   SER A O   1 
ATOM   2123 C  CB  . SER B 1 6   ? 1.091   12.692  13.524  1.00 57.02 ? 6   SER A CB  1 
ATOM   2124 O  OG  . SER B 1 6   ? 1.618   12.982  12.237  1.00 52.39 ? 6   SER A OG  1 
ATOM   2125 N  N   . TRP B 1 7   ? 0.755   9.191   13.036  1.00 35.98 ? 7   TRP A N   1 
ATOM   2126 C  CA  . TRP B 1 7   ? 1.075   7.972   12.239  1.00 29.67 ? 7   TRP A CA  1 
ATOM   2127 C  C   . TRP B 1 7   ? 0.060   7.575   11.148  1.00 24.27 ? 7   TRP A C   1 
ATOM   2128 O  O   . TRP B 1 7   ? -1.110  8.006   11.186  1.00 27.24 ? 7   TRP A O   1 
ATOM   2129 C  CB  . TRP B 1 7   ? 1.242   6.787   13.223  1.00 25.92 ? 7   TRP A CB  1 
ATOM   2130 C  CG  . TRP B 1 7   ? -0.095  6.404   13.866  1.00 24.74 ? 7   TRP A CG  1 
ATOM   2131 C  CD1 . TRP B 1 7   ? -0.717  6.889   15.053  1.00 23.77 ? 7   TRP A CD1 1 
ATOM   2132 C  CD2 . TRP B 1 7   ? -1.038  5.377   13.353  1.00 23.31 ? 7   TRP A CD2 1 
ATOM   2133 N  NE1 . TRP B 1 7   ? -1.924  6.282   15.263  1.00 25.68 ? 7   TRP A NE1 1 
ATOM   2134 C  CE2 . TRP B 1 7   ? -2.162  5.336   14.308  1.00 22.84 ? 7   TRP A CE2 1 
ATOM   2135 C  CE3 . TRP B 1 7   ? -1.010  4.480   12.281  1.00 21.45 ? 7   TRP A CE3 1 
ATOM   2136 C  CZ2 . TRP B 1 7   ? -3.248  4.476   14.124  1.00 23.44 ? 7   TRP A CZ2 1 
ATOM   2137 C  CZ3 . TRP B 1 7   ? -2.088  3.642   12.096  1.00 22.10 ? 7   TRP A CZ3 1 
ATOM   2138 C  CH2 . TRP B 1 7   ? -3.170  3.611   13.029  1.00 23.42 ? 7   TRP A CH2 1 
ATOM   2139 N  N   . GLY B 1 8   ? 0.481   6.753   10.196  1.00 23.92 ? 8   GLY A N   1 
ATOM   2140 C  CA  . GLY B 1 8   ? -0.398  6.281   9.127   1.00 23.32 ? 8   GLY A CA  1 
ATOM   2141 C  C   . GLY B 1 8   ? 0.214   5.162   8.369   1.00 22.55 ? 8   GLY A C   1 
ATOM   2142 O  O   . GLY B 1 8   ? 0.966   4.368   8.910   1.00 22.03 ? 8   GLY A O   1 
ATOM   2143 N  N   . TYR B 1 9   ? -0.050  5.117   7.064   1.00 19.73 ? 9   TYR A N   1 
ATOM   2144 C  CA  . TYR B 1 9   ? 0.423   4.030   6.241   1.00 20.41 ? 9   TYR A CA  1 
ATOM   2145 C  C   . TYR B 1 9   ? 1.064   4.630   4.988   1.00 24.62 ? 9   TYR A C   1 
ATOM   2146 O  O   . TYR B 1 9   ? 1.344   3.878   4.042   1.00 26.98 ? 9   TYR A O   1 
ATOM   2147 C  CB  . TYR B 1 9   ? -0.754  3.120   5.808   1.00 20.94 ? 9   TYR A CB  1 
ATOM   2148 C  CG  . TYR B 1 9   ? -1.360  2.350   6.981   1.00 16.55 ? 9   TYR A CG  1 
ATOM   2149 C  CD1 . TYR B 1 9   ? -0.732  1.180   7.401   1.00 17.91 ? 9   TYR A CD1 1 
ATOM   2150 C  CD2 . TYR B 1 9   ? -2.458  2.860   7.644   1.00 17.21 ? 9   TYR A CD2 1 
ATOM   2151 C  CE1 . TYR B 1 9   ? -1.280  0.449   8.470   1.00 15.56 ? 9   TYR A CE1 1 
ATOM   2152 C  CE2 . TYR B 1 9   ? -3.021  2.152   8.728   1.00 17.31 ? 9   TYR A CE2 1 
ATOM   2153 C  CZ  . TYR B 1 9   ? -2.378  1.008   9.081   1.00 15.47 ? 9   TYR A CZ  1 
ATOM   2154 O  OH  . TYR B 1 9   ? -2.980  0.290   10.126  1.00 15.91 ? 9   TYR A OH  1 
ATOM   2155 N  N   . ARG B 1 10  ? 1.283   5.928   5.044   1.00 25.92 ? 10  ARG A N   1 
ATOM   2156 C  CA  . ARG B 1 10  ? 1.946   6.622   3.896   1.00 30.25 ? 10  ARG A CA  1 
ATOM   2157 C  C   . ARG B 1 10  ? 3.423   6.420   4.020   1.00 31.33 ? 10  ARG A C   1 
ATOM   2158 O  O   . ARG B 1 10  ? 3.920   5.856   4.986   1.00 27.33 ? 10  ARG A O   1 
ATOM   2159 C  CB  . ARG B 1 10  ? 1.547   8.090   3.834   1.00 32.37 ? 10  ARG A CB  1 
ATOM   2160 C  CG  . ARG B 1 10  ? 0.063   8.325   3.523   1.00 37.18 ? 10  ARG A CG  1 
ATOM   2161 C  CD  . ARG B 1 10  ? -0.376  9.712   3.967   1.00 43.22 ? 10  ARG A CD  1 
ATOM   2162 N  NE  . ARG B 1 10  ? -0.117  10.725  2.928   1.00 47.59 ? 10  ARG A NE  1 
ATOM   2163 C  CZ  . ARG B 1 10  ? -0.628  11.961  2.903   1.00 47.24 ? 10  ARG A CZ  1 
ATOM   2164 N  NH1 . ARG B 1 10  ? -1.469  12.387  3.844   1.00 46.98 ? 10  ARG A NH1 1 
ATOM   2165 N  NH2 . ARG B 1 10  ? -0.322  12.767  1.896   1.00 49.21 ? 10  ARG A NH2 1 
ATOM   2166 N  N   . GLU B 1 11  ? 4.160   6.874   3.012   1.00 35.18 ? 11  GLU A N   1 
ATOM   2167 C  CA  . GLU B 1 11  ? 5.604   6.678   2.940   1.00 36.93 ? 11  GLU A CA  1 
ATOM   2168 C  C   . GLU B 1 11  ? 6.379   7.187   4.194   1.00 30.80 ? 11  GLU A C   1 
ATOM   2169 O  O   . GLU B 1 11  ? 7.251   6.501   4.746   1.00 29.90 ? 11  GLU A O   1 
ATOM   2170 C  CB  . GLU B 1 11  ? 6.092   7.398   1.674   1.00 42.51 ? 11  GLU A CB  1 
ATOM   2171 C  CG  . GLU B 1 11  ? 7.537   7.104   1.282   1.00 50.47 ? 11  GLU A CG  1 
ATOM   2172 C  CD  . GLU B 1 11  ? 8.272   8.344   0.729   1.00 63.04 ? 11  GLU A CD  1 
ATOM   2173 O  OE1 . GLU B 1 11  ? 7.646   9.251   0.099   1.00 54.52 ? 11  GLU A OE1 1 
ATOM   2174 O  OE2 . GLU B 1 11  ? 9.505   8.412   0.920   1.00 65.10 ? 11  GLU A OE2 1 
ATOM   2175 N  N   . HIS B 1 12  ? 6.009   8.363   4.649   1.00 33.75 ? 12  HIS A N   1 
ATOM   2176 C  CA  . HIS B 1 12  ? 6.656   9.081   5.733   1.00 35.74 ? 12  HIS A CA  1 
ATOM   2177 C  C   . HIS B 1 12  ? 6.186   8.760   7.112   1.00 34.73 ? 12  HIS A C   1 
ATOM   2178 O  O   . HIS B 1 12  ? 6.873   9.046   8.066   1.00 34.41 ? 12  HIS A O   1 
ATOM   2179 C  CB  . HIS B 1 12  ? 6.419   10.573  5.496   1.00 46.32 ? 12  HIS A CB  1 
ATOM   2180 C  CG  . HIS B 1 12  ? 4.990   10.910  5.038   1.00 56.81 ? 12  HIS A CG  1 
ATOM   2181 N  ND1 . HIS B 1 12  ? 4.030   11.338  5.886   1.00 58.19 ? 12  HIS A ND1 1 
ATOM   2182 C  CD2 . HIS B 1 12  ? 4.395   10.865  3.771   1.00 59.49 ? 12  HIS A CD2 1 
ATOM   2183 C  CE1 . HIS B 1 12  ? 2.884   11.556  5.202   1.00 58.50 ? 12  HIS A CE1 1 
ATOM   2184 N  NE2 . HIS B 1 12  ? 3.108   11.268  3.911   1.00 62.97 ? 12  HIS A NE2 1 
ATOM   2185 N  N   . ASN B 1 13  ? 4.990   8.187   7.255   1.00 27.57 ? 13  ASN A N   1 
ATOM   2186 C  CA  . ASN B 1 13  ? 4.452   8.007   8.579   1.00 26.63 ? 13  ASN A CA  1 
ATOM   2187 C  C   . ASN B 1 13  ? 4.035   6.528   8.772   1.00 23.16 ? 13  ASN A C   1 
ATOM   2188 O  O   . ASN B 1 13  ? 3.333   6.207   9.762   1.00 24.26 ? 13  ASN A O   1 
ATOM   2189 C  CB  . ASN B 1 13  ? 3.298   8.984   8.818   1.00 28.72 ? 13  ASN A CB  1 
ATOM   2190 C  CG  . ASN B 1 13  ? 2.065   8.703   7.946   1.00 27.55 ? 13  ASN A CG  1 
ATOM   2191 O  OD1 . ASN B 1 13  ? 2.086   7.821   7.082   1.00 31.58 ? 13  ASN A OD1 1 
ATOM   2192 N  ND2 . ASN B 1 13  ? 1.035   9.503   8.107   1.00 29.54 ? 13  ASN A ND2 1 
ATOM   2193 N  N   . GLY B 1 14  ? 4.461   5.690   7.833   1.00 23.83 ? 14  GLY A N   1 
ATOM   2194 C  CA  . GLY B 1 14  ? 3.969   4.313   7.716   1.00 25.87 ? 14  GLY A CA  1 
ATOM   2195 C  C   . GLY B 1 14  ? 4.666   3.323   8.623   1.00 25.76 ? 14  GLY A C   1 
ATOM   2196 O  O   . GLY B 1 14  ? 5.573   3.672   9.352   1.00 24.45 ? 14  GLY A O   1 
ATOM   2197 N  N   . PRO B 1 15  ? 4.227   2.048   8.597   1.00 21.11 ? 15  PRO A N   1 
ATOM   2198 C  CA  . PRO B 1 15  ? 4.793   1.016   9.524   1.00 20.85 ? 15  PRO A CA  1 
ATOM   2199 C  C   . PRO B 1 15  ? 6.300   0.981   9.821   1.00 24.95 ? 15  PRO A C   1 
ATOM   2200 O  O   . PRO B 1 15  ? 6.742   0.688   10.968  1.00 23.09 ? 15  PRO A O   1 
ATOM   2201 C  CB  . PRO B 1 15  ? 4.325   -0.295  8.921   1.00 22.67 ? 15  PRO A CB  1 
ATOM   2202 C  CG  . PRO B 1 15  ? 3.003   0.064   8.384   1.00 19.18 ? 15  PRO A CG  1 
ATOM   2203 C  CD  . PRO B 1 15  ? 3.096   1.488   7.805   1.00 20.83 ? 15  PRO A CD  1 
ATOM   2204 N  N   . ILE B 1 16  ? 7.111   1.222   8.785   1.00 24.63 ? 16  ILE A N   1 
ATOM   2205 C  CA  . ILE B 1 16  ? 8.522   1.202   8.914   1.00 29.64 ? 16  ILE A CA  1 
ATOM   2206 C  C   . ILE B 1 16  ? 9.013   2.300   9.889   1.00 25.60 ? 16  ILE A C   1 
ATOM   2207 O  O   . ILE B 1 16  ? 10.079  2.136   10.508  1.00 30.77 ? 16  ILE A O   1 
ATOM   2208 C  CB  . ILE B 1 16  ? 9.181   1.248   7.472   1.00 31.34 ? 16  ILE A CB  1 
ATOM   2209 C  CG1 . ILE B 1 16  ? 10.154  0.078   7.292   1.00 39.47 ? 16  ILE A CG1 1 
ATOM   2210 C  CG2 . ILE B 1 16  ? 9.705   2.612   7.131   1.00 36.26 ? 16  ILE A CG2 1 
ATOM   2211 C  CD1 . ILE B 1 16  ? 9.442   -1.263  7.228   1.00 44.16 ? 16  ILE A CD1 1 
ATOM   2212 N  N   . HIS B 1 17  ? 8.250   3.382   10.045  1.00 26.48 ? 17  HIS A N   1 
ATOM   2213 C  CA  . HIS B 1 17  ? 8.628   4.480   10.912  1.00 30.91 ? 17  HIS A CA  1 
ATOM   2214 C  C   . HIS B 1 17  ? 7.924   4.469   12.240  1.00 33.23 ? 17  HIS A C   1 
ATOM   2215 O  O   . HIS B 1 17  ? 8.140   5.357   13.084  1.00 29.35 ? 17  HIS A O   1 
ATOM   2216 C  CB  . HIS B 1 17  ? 8.352   5.822   10.239  1.00 30.05 ? 17  HIS A CB  1 
ATOM   2217 C  CG  . HIS B 1 17  ? 8.955   5.946   8.874   1.00 34.48 ? 17  HIS A CG  1 
ATOM   2218 N  ND1 . HIS B 1 17  ? 10.312  5.987   8.669   1.00 40.56 ? 17  HIS A ND1 1 
ATOM   2219 C  CD2 . HIS B 1 17  ? 8.367   6.032   7.627   1.00 33.99 ? 17  HIS A CD2 1 
ATOM   2220 C  CE1 . HIS B 1 17  ? 10.559  6.102   7.336   1.00 38.61 ? 17  HIS A CE1 1 
ATOM   2221 N  NE2 . HIS B 1 17  ? 9.378   6.135   6.698   1.00 40.71 ? 17  HIS A NE2 1 
ATOM   2222 N  N   . TRP B 1 18  ? 7.093   3.458   12.515  1.00 24.22 ? 18  TRP A N   1 
ATOM   2223 C  CA  . TRP B 1 18  ? 6.430   3.557   13.807  1.00 23.54 ? 18  TRP A CA  1 
ATOM   2224 C  C   . TRP B 1 18  ? 7.409   3.330   14.946  1.00 23.66 ? 18  TRP A C   1 
ATOM   2225 O  O   . TRP B 1 18  ? 7.179   3.876   16.015  1.00 29.55 ? 18  TRP A O   1 
ATOM   2226 C  CB  . TRP B 1 18  ? 5.221   2.543   13.888  1.00 22.58 ? 18  TRP A CB  1 
ATOM   2227 C  CG  . TRP B 1 18  ? 4.129   2.737   12.860  1.00 22.64 ? 18  TRP A CG  1 
ATOM   2228 C  CD1 . TRP B 1 18  ? 3.844   3.860   12.063  1.00 20.70 ? 18  TRP A CD1 1 
ATOM   2229 C  CD2 . TRP B 1 18  ? 3.028   1.788   12.592  1.00 19.84 ? 18  TRP A CD2 1 
ATOM   2230 N  NE1 . TRP B 1 18  ? 2.709   3.675   11.332  1.00 23.39 ? 18  TRP A NE1 1 
ATOM   2231 C  CE2 . TRP B 1 18  ? 2.203   2.402   11.573  1.00 21.18 ? 18  TRP A CE2 1 
ATOM   2232 C  CE3 . TRP B 1 18  ? 2.733   0.479   13.026  1.00 19.54 ? 18  TRP A CE3 1 
ATOM   2233 C  CZ2 . TRP B 1 18  ? 1.051   1.793   11.096  1.00 21.72 ? 18  TRP A CZ2 1 
ATOM   2234 C  CZ3 . TRP B 1 18  ? 1.606   -0.165  12.478  1.00 16.43 ? 18  TRP A CZ3 1 
ATOM   2235 C  CH2 . TRP B 1 18  ? 0.785   0.470   11.569  1.00 18.98 ? 18  TRP A CH2 1 
ATOM   2236 N  N   . LYS B 1 19  ? 8.451   2.531   14.729  1.00 27.08 ? 19  LYS A N   1 
ATOM   2237 C  CA  . LYS B 1 19  ? 9.500   2.231   15.775  1.00 28.69 ? 19  LYS A CA  1 
ATOM   2238 C  C   . LYS B 1 19  ? 10.201  3.507   16.274  1.00 38.93 ? 19  LYS A C   1 
ATOM   2239 O  O   . LYS B 1 19  ? 10.703  3.556   17.412  1.00 36.37 ? 19  LYS A O   1 
ATOM   2240 C  CB  . LYS B 1 19  ? 10.546  1.198   15.311  1.00 32.99 ? 19  LYS A CB  1 
ATOM   2241 C  CG  . LYS B 1 19  ? 11.590  1.694   14.295  1.00 31.63 ? 19  LYS A CG  1 
ATOM   2242 C  CD  . LYS B 1 19  ? 12.485  0.519   13.877  1.00 35.27 ? 19  LYS A CD  1 
ATOM   2243 C  CE  . LYS B 1 19  ? 13.906  0.672   14.418  1.00 45.49 ? 19  LYS A CE  1 
ATOM   2244 N  NZ  . LYS B 1 19  ? 14.736  -0.565  14.305  1.00 52.39 ? 19  LYS A NZ  1 
ATOM   2245 N  N   . GLU B 1 20  ? 10.239  4.519   15.418  1.00 38.62 ? 20  GLU A N   1 
ATOM   2246 C  CA  . GLU B 1 20  ? 10.802  5.825   15.804  1.00 41.49 ? 20  GLU A CA  1 
ATOM   2247 C  C   . GLU B 1 20  ? 10.000  6.484   16.919  1.00 42.86 ? 20  GLU A C   1 
ATOM   2248 O  O   . GLU B 1 20  ? 10.596  7.161   17.773  1.00 37.59 ? 20  GLU A O   1 
ATOM   2249 C  CB  . GLU B 1 20  ? 10.816  6.787   14.610  1.00 43.57 ? 20  GLU A CB  1 
ATOM   2250 C  CG  . GLU B 1 20  ? 11.701  6.339   13.460  1.00 42.84 ? 20  GLU A CG  1 
ATOM   2251 C  CD  . GLU B 1 20  ? 11.235  6.939   12.138  1.00 44.84 ? 20  GLU A CD  1 
ATOM   2252 O  OE1 . GLU B 1 20  ? 10.583  8.017   12.161  1.00 45.04 ? 20  GLU A OE1 1 
ATOM   2253 O  OE2 . GLU B 1 20  ? 11.512  6.331   11.079  1.00 42.83 ? 20  GLU A OE2 1 
ATOM   2254 N  N   . PHE B 1 21  ? 8.679   6.271   16.906  1.00 42.62 ? 21  PHE A N   1 
ATOM   2255 C  CA  . PHE B 1 21  ? 7.708   6.967   17.799  1.00 44.14 ? 21  PHE A CA  1 
ATOM   2256 C  C   . PHE B 1 21  ? 6.883   6.147   18.835  1.00 44.95 ? 21  PHE A C   1 
ATOM   2257 O  O   . PHE B 1 21  ? 6.321   6.684   19.802  1.00 44.39 ? 21  PHE A O   1 
ATOM   2258 C  CB  . PHE B 1 21  ? 6.841   7.903   16.977  1.00 49.20 ? 21  PHE A CB  1 
ATOM   2259 C  CG  . PHE B 1 21  ? 7.596   9.123   16.536  1.00 59.98 ? 21  PHE A CG  1 
ATOM   2260 C  CD1 . PHE B 1 21  ? 7.728   10.228  17.390  1.00 64.72 ? 21  PHE A CD1 1 
ATOM   2261 C  CD2 . PHE B 1 21  ? 8.253   9.154   15.297  1.00 66.93 ? 21  PHE A CD2 1 
ATOM   2262 C  CE1 . PHE B 1 21  ? 8.470   11.359  17.006  1.00 70.72 ? 21  PHE A CE1 1 
ATOM   2263 C  CE2 . PHE B 1 21  ? 8.991   10.285  14.904  1.00 68.82 ? 21  PHE A CE2 1 
ATOM   2264 C  CZ  . PHE B 1 21  ? 9.102   11.385  15.760  1.00 68.37 ? 21  PHE A CZ  1 
ATOM   2265 N  N   . PHE B 1 22  ? 6.813   4.845   18.604  1.00 38.87 ? 22  PHE A N   1 
ATOM   2266 C  CA  . PHE B 1 22  ? 6.356   3.867   19.586  1.00 34.55 ? 22  PHE A CA  1 
ATOM   2267 C  C   . PHE B 1 22  ? 7.398   2.795   19.607  1.00 34.11 ? 22  PHE A C   1 
ATOM   2268 O  O   . PHE B 1 22  ? 7.396   1.837   18.824  1.00 30.13 ? 22  PHE A O   1 
ATOM   2269 C  CB  . PHE B 1 22  ? 5.033   3.280   19.166  1.00 37.31 ? 22  PHE A CB  1 
ATOM   2270 C  CG  . PHE B 1 22  ? 4.008   4.291   18.989  1.00 36.31 ? 22  PHE A CG  1 
ATOM   2271 C  CD1 . PHE B 1 22  ? 3.163   4.605   20.031  1.00 33.13 ? 22  PHE A CD1 1 
ATOM   2272 C  CD2 . PHE B 1 22  ? 3.917   5.002   17.778  1.00 36.01 ? 22  PHE A CD2 1 
ATOM   2273 C  CE1 . PHE B 1 22  ? 2.207   5.575   19.868  1.00 38.12 ? 22  PHE A CE1 1 
ATOM   2274 C  CE2 . PHE B 1 22  ? 2.969   5.979   17.626  1.00 37.43 ? 22  PHE A CE2 1 
ATOM   2275 C  CZ  . PHE B 1 22  ? 2.101   6.266   18.683  1.00 37.81 ? 22  PHE A CZ  1 
ATOM   2276 N  N   . PRO B 1 23  ? 8.338   2.932   20.514  1.00 32.84 ? 23  PRO A N   1 
ATOM   2277 C  CA  . PRO B 1 23  ? 9.439   1.997   20.582  1.00 31.31 ? 23  PRO A CA  1 
ATOM   2278 C  C   . PRO B 1 23  ? 9.084   0.501   20.714  1.00 28.42 ? 23  PRO A C   1 
ATOM   2279 O  O   . PRO B 1 23  ? 9.854   -0.399  20.313  1.00 29.04 ? 23  PRO A O   1 
ATOM   2280 C  CB  . PRO B 1 23  ? 10.198  2.503   21.804  1.00 33.83 ? 23  PRO A CB  1 
ATOM   2281 C  CG  . PRO B 1 23  ? 9.997   3.967   21.718  1.00 37.58 ? 23  PRO A CG  1 
ATOM   2282 C  CD  . PRO B 1 23  ? 8.611   4.196   21.238  1.00 34.49 ? 23  PRO A CD  1 
ATOM   2283 N  N   . ILE B 1 24  ? 7.910   0.226   21.318  1.00 25.11 ? 24  ILE A N   1 
ATOM   2284 C  CA  . ILE B 1 24  ? 7.471   -1.166  21.489  1.00 24.49 ? 24  ILE A CA  1 
ATOM   2285 C  C   . ILE B 1 24  ? 7.169   -1.807  20.088  1.00 22.60 ? 24  ILE A C   1 
ATOM   2286 O  O   . ILE B 1 24  ? 7.078   -3.020  19.983  1.00 21.71 ? 24  ILE A O   1 
ATOM   2287 C  CB  . ILE B 1 24  ? 6.141   -1.222  22.348  1.00 21.10 ? 24  ILE A CB  1 
ATOM   2288 C  CG1 . ILE B 1 24  ? 5.985   -2.630  22.945  1.00 24.87 ? 24  ILE A CG1 1 
ATOM   2289 C  CG2 . ILE B 1 24  ? 4.952   -0.751  21.540  1.00 21.74 ? 24  ILE A CG2 1 
ATOM   2290 C  CD1 . ILE B 1 24  ? 7.164   -3.056  23.835  1.00 26.91 ? 24  ILE A CD1 1 
ATOM   2291 N  N   . ALA B 1 25  ? 7.156   -0.969  19.057  1.00 23.68 ? 25  ALA A N   1 
ATOM   2292 C  CA  . ALA B 1 25  ? 7.084   -1.461  17.672  1.00 21.94 ? 25  ALA A CA  1 
ATOM   2293 C  C   . ALA B 1 25  ? 8.095   -2.523  17.424  1.00 21.12 ? 25  ALA A C   1 
ATOM   2294 O  O   . ALA B 1 25  ? 7.872   -3.388  16.554  1.00 22.01 ? 25  ALA A O   1 
ATOM   2295 C  CB  . ALA B 1 25  ? 7.315   -0.372  16.672  1.00 23.39 ? 25  ALA A CB  1 
ATOM   2296 N  N   . ASP B 1 26  ? 9.239   -2.427  18.127  1.00 24.99 ? 26  ASP A N   1 
ATOM   2297 C  CA  . ASP B 1 26  ? 10.303  -3.374  18.074  1.00 26.46 ? 26  ASP A CA  1 
ATOM   2298 C  C   . ASP B 1 26  ? 10.332  -4.330  19.232  1.00 30.50 ? 26  ASP A C   1 
ATOM   2299 O  O   . ASP B 1 26  ? 11.352  -5.030  19.432  1.00 24.91 ? 26  ASP A O   1 
ATOM   2300 C  CB  . ASP B 1 26  ? 11.671  -2.630  18.066  1.00 33.86 ? 26  ASP A CB  1 
ATOM   2301 C  CG  . ASP B 1 26  ? 11.939  -1.946  16.752  1.00 41.31 ? 26  ASP A CG  1 
ATOM   2302 O  OD1 . ASP B 1 26  ? 11.725  -2.593  15.694  1.00 40.86 ? 26  ASP A OD1 1 
ATOM   2303 O  OD2 . ASP B 1 26  ? 12.328  -0.755  16.794  1.00 46.67 ? 26  ASP A OD2 1 
ATOM   2304 N  N   . GLY B 1 27  ? 9.219   -4.380  19.981  1.00 26.67 ? 27  GLY A N   1 
ATOM   2305 C  CA  . GLY B 1 27  ? 9.053   -5.390  21.034  1.00 24.71 ? 27  GLY A CA  1 
ATOM   2306 C  C   . GLY B 1 27  ? 9.113   -6.862  20.681  1.00 23.13 ? 27  GLY A C   1 
ATOM   2307 O  O   . GLY B 1 27  ? 9.211   -7.277  19.479  1.00 28.60 ? 27  GLY A O   1 
ATOM   2308 N  N   . ASP B 1 28  ? 9.001   -7.713  21.712  1.00 23.79 ? 28  ASP A N   1 
ATOM   2309 C  CA  . ASP B 1 28  ? 9.125   -9.109  21.527  1.00 20.11 ? 28  ASP A CA  1 
ATOM   2310 C  C   . ASP B 1 28  ? 7.784   -9.866  21.257  1.00 17.91 ? 28  ASP A C   1 
ATOM   2311 O  O   . ASP B 1 28  ? 7.821   -11.055 21.033  1.00 21.52 ? 28  ASP A O   1 
ATOM   2312 C  CB  . ASP B 1 28  ? 9.689   -9.810  22.781  1.00 28.90 ? 28  ASP A CB  1 
ATOM   2313 C  CG  . ASP B 1 28  ? 11.180  -9.522  22.994  1.00 36.50 ? 28  ASP A CG  1 
ATOM   2314 O  OD1 . ASP B 1 28  ? 11.821  -9.084  22.042  1.00 38.89 ? 28  ASP A OD1 1 
ATOM   2315 O  OD2 . ASP B 1 28  ? 11.666  -9.736  24.119  1.00 47.51 ? 28  ASP A OD2 1 
ATOM   2316 N  N   . GLN B 1 29  ? 6.645   -9.173  21.365  1.00 17.80 ? 29  GLN A N   1 
ATOM   2317 C  CA  . GLN B 1 29  ? 5.392   -9.902  21.112  1.00 17.89 ? 29  GLN A CA  1 
ATOM   2318 C  C   . GLN B 1 29  ? 4.523   -9.053  20.168  1.00 17.83 ? 29  GLN A C   1 
ATOM   2319 O  O   . GLN B 1 29  ? 3.373   -8.722  20.451  1.00 15.29 ? 29  GLN A O   1 
ATOM   2320 C  CB  . GLN B 1 29  ? 4.621   -10.179 22.395  1.00 18.64 ? 29  GLN A CB  1 
ATOM   2321 C  CG  . GLN B 1 29  ? 5.500   -10.922 23.448  1.00 23.36 ? 29  GLN A CG  1 
ATOM   2322 C  CD  . GLN B 1 29  ? 4.660   -11.882 24.346  1.00 25.46 ? 29  GLN A CD  1 
ATOM   2323 O  OE1 . GLN B 1 29  ? 3.543   -11.598 24.697  1.00 25.73 ? 29  GLN A OE1 1 
ATOM   2324 N  NE2 . GLN B 1 29  ? 5.243   -13.046 24.674  1.00 27.28 ? 29  GLN A NE2 1 
ATOM   2325 N  N   . GLN B 1 30  ? 5.143   -8.620  19.052  1.00 16.30 ? 30  GLN A N   1 
ATOM   2326 C  CA  . GLN B 1 30  ? 4.397   -7.784  18.029  1.00 14.62 ? 30  GLN A CA  1 
ATOM   2327 C  C   . GLN B 1 30  ? 3.644   -8.662  17.026  1.00 12.12 ? 30  GLN A C   1 
ATOM   2328 O  O   . GLN B 1 30  ? 3.990   -9.761  16.752  1.00 12.66 ? 30  GLN A O   1 
ATOM   2329 C  CB  . GLN B 1 30  ? 5.434   -6.915  17.270  1.00 14.26 ? 30  GLN A CB  1 
ATOM   2330 C  CG  . GLN B 1 30  ? 5.936   -5.826  18.289  1.00 12.95 ? 30  GLN A CG  1 
ATOM   2331 C  CD  . GLN B 1 30  ? 4.886   -4.826  18.591  1.00 16.41 ? 30  GLN A CD  1 
ATOM   2332 O  OE1 . GLN B 1 30  ? 4.479   -4.040  17.778  1.00 16.88 ? 30  GLN A OE1 1 
ATOM   2333 N  NE2 . GLN B 1 30  ? 4.463   -4.753  19.921  1.00 15.95 ? 30  GLN A NE2 1 
ATOM   2334 N  N   . SER B 1 31  ? 2.574   -8.039  16.547  1.00 12.74 ? 31  SER A N   1 
ATOM   2335 C  CA  . SER B 1 31  ? 1.694   -8.618  15.499  1.00 11.63 ? 31  SER A CA  1 
ATOM   2336 C  C   . SER B 1 31  ? 1.584   -7.712  14.306  1.00 11.32 ? 31  SER A C   1 
ATOM   2337 O  O   . SER B 1 31  ? 1.765   -6.530  14.402  1.00 12.10 ? 31  SER A O   1 
ATOM   2338 C  CB  . SER B 1 31  ? 0.302   -8.660  16.136  1.00 11.90 ? 31  SER A CB  1 
ATOM   2339 O  OG  . SER B 1 31  ? 0.366   -9.691  17.173  1.00 11.32 ? 31  SER A OG  1 
ATOM   2340 N  N   . PRO B 1 32  ? 1.190   -8.276  13.156  1.00 10.72 ? 32  PRO A N   1 
ATOM   2341 C  CA  . PRO B 1 32  ? 0.882   -9.642  12.823  1.00 11.05 ? 32  PRO A CA  1 
ATOM   2342 C  C   . PRO B 1 32  ? 2.153   -10.414 12.552  1.00 11.33 ? 32  PRO A C   1 
ATOM   2343 O  O   . PRO B 1 32  ? 3.287   -9.911  12.739  1.00 13.29 ? 32  PRO A O   1 
ATOM   2344 C  CB  . PRO B 1 32  ? 0.050   -9.465  11.514  1.00 11.60 ? 32  PRO A CB  1 
ATOM   2345 C  CG  . PRO B 1 32  ? 0.744   -8.281  10.832  1.00 11.70 ? 32  PRO A CG  1 
ATOM   2346 C  CD  . PRO B 1 32  ? 1.078   -7.341  11.976  1.00 11.77 ? 32  PRO A CD  1 
ATOM   2347 N  N   . ILE B 1 33  ? 1.904   -11.655 12.230  1.00 11.71 ? 33  ILE A N   1 
ATOM   2348 C  CA  . ILE B 1 33  ? 3.016   -12.615 12.008  1.00 12.95 ? 33  ILE A CA  1 
ATOM   2349 C  C   . ILE B 1 33  ? 2.723   -13.464 10.806  1.00 14.99 ? 33  ILE A C   1 
ATOM   2350 O  O   . ILE B 1 33  ? 1.580   -13.563 10.324  1.00 14.44 ? 33  ILE A O   1 
ATOM   2351 C  CB  . ILE B 1 33  ? 3.231   -13.555 13.269  1.00 13.47 ? 33  ILE A CB  1 
ATOM   2352 C  CG1 . ILE B 1 33  ? 2.005   -14.492 13.500  1.00 14.05 ? 33  ILE A CG1 1 
ATOM   2353 C  CG2 . ILE B 1 33  ? 3.613   -12.725 14.530  1.00 14.27 ? 33  ILE A CG2 1 
ATOM   2354 C  CD1 . ILE B 1 33  ? 2.326   -15.643 14.501  1.00 14.68 ? 33  ILE A CD1 1 
ATOM   2355 N  N   A GLU B 1 34  ? 3.777   -14.113 10.298  0.50 15.71 ? 34  GLU A N   1 
ATOM   2356 N  N   B GLU B 1 34  ? 3.791   -14.147 10.381  0.50 14.98 ? 34  GLU A N   1 
ATOM   2357 C  CA  A GLU B 1 34  ? 3.601   -15.238 9.378   0.50 16.27 ? 34  GLU A CA  1 
ATOM   2358 C  CA  B GLU B 1 34  ? 3.721   -15.268 9.461   0.50 15.21 ? 34  GLU A CA  1 
ATOM   2359 C  C   A GLU B 1 34  ? 3.189   -16.417 10.184  0.50 15.75 ? 34  GLU A C   1 
ATOM   2360 C  C   B GLU B 1 34  ? 3.274   -16.549 10.149  0.50 15.07 ? 34  GLU A C   1 
ATOM   2361 O  O   A GLU B 1 34  ? 3.817   -16.714 11.232  0.50 16.84 ? 34  GLU A O   1 
ATOM   2362 O  O   B GLU B 1 34  ? 3.965   -17.082 11.073  0.50 15.09 ? 34  GLU A O   1 
ATOM   2363 C  CB  A GLU B 1 34  ? 4.903   -15.630 8.644   0.50 17.51 ? 34  GLU A CB  1 
ATOM   2364 C  CB  B GLU B 1 34  ? 5.104   -15.539 8.823   0.50 15.40 ? 34  GLU A CB  1 
ATOM   2365 C  CG  A GLU B 1 34  ? 5.043   -15.084 7.239   0.50 19.35 ? 34  GLU A CG  1 
ATOM   2366 C  CG  B GLU B 1 34  ? 5.849   -14.383 8.186   0.50 15.96 ? 34  GLU A CG  1 
ATOM   2367 C  CD  A GLU B 1 34  ? 4.347   -15.851 6.084   0.50 14.12 ? 34  GLU A CD  1 
ATOM   2368 C  CD  B GLU B 1 34  ? 5.401   -14.022 6.794   0.50 15.98 ? 34  GLU A CD  1 
ATOM   2369 O  OE1 A GLU B 1 34  ? 3.624   -16.938 6.118   0.50 10.84 ? 34  GLU A OE1 1 
ATOM   2370 O  OE1 B GLU B 1 34  ? 5.783   -12.898 6.354   0.50 17.27 ? 34  GLU A OE1 1 
ATOM   2371 O  OE2 A GLU B 1 34  ? 4.550   -15.218 5.028   0.50 22.13 ? 34  GLU A OE2 1 
ATOM   2372 O  OE2 B GLU B 1 34  ? 4.671   -14.818 6.134   0.50 13.94 ? 34  GLU A OE2 1 
ATOM   2373 N  N   . ILE B 1 35  ? 2.160   -17.103 9.700   1.00 14.93 ? 35  ILE A N   1 
ATOM   2374 C  CA  . ILE B 1 35  ? 1.740   -18.392 10.281  1.00 14.98 ? 35  ILE A CA  1 
ATOM   2375 C  C   . ILE B 1 35  ? 2.259   -19.466 9.373   1.00 15.52 ? 35  ILE A C   1 
ATOM   2376 O  O   . ILE B 1 35  ? 1.847   -19.522 8.230   1.00 16.94 ? 35  ILE A O   1 
ATOM   2377 C  CB  . ILE B 1 35  ? 0.176   -18.442 10.453  1.00 16.90 ? 35  ILE A CB  1 
ATOM   2378 C  CG1 . ILE B 1 35  ? -0.221  -17.318 11.452  1.00 19.21 ? 35  ILE A CG1 1 
ATOM   2379 C  CG2 . ILE B 1 35  ? -0.272  -19.830 10.909  1.00 18.30 ? 35  ILE A CG2 1 
ATOM   2380 C  CD1 . ILE B 1 35  ? -1.700  -17.062 11.436  1.00 20.57 ? 35  ILE A CD1 1 
ATOM   2381 N  N   . LYS B 1 36  ? 3.209   -20.282 9.876   1.00 19.07 ? 36  LYS A N   1 
ATOM   2382 C  CA  . LYS B 1 36  ? 3.781   -21.415 9.110   1.00 17.50 ? 36  LYS A CA  1 
ATOM   2383 C  C   . LYS B 1 36  ? 3.169   -22.718 9.649   1.00 17.55 ? 36  LYS A C   1 
ATOM   2384 O  O   . LYS B 1 36  ? 3.458   -23.114 10.802  1.00 20.20 ? 36  LYS A O   1 
ATOM   2385 C  CB  . LYS B 1 36  ? 5.313   -21.401 9.329   1.00 18.42 ? 36  LYS A CB  1 
ATOM   2386 C  CG  . LYS B 1 36  ? 6.097   -20.265 8.672   1.00 20.54 ? 36  LYS A CG  1 
ATOM   2387 C  CD  . LYS B 1 36  ? 7.570   -20.413 9.013   1.00 22.43 ? 36  LYS A CD  1 
ATOM   2388 C  CE  . LYS B 1 36  ? 8.456   -19.426 8.354   1.00 23.17 ? 36  LYS A CE  1 
ATOM   2389 N  NZ  . LYS B 1 36  ? 9.865   -19.617 8.851   1.00 23.43 ? 36  LYS A NZ  1 
ATOM   2390 N  N   . THR B 1 37  ? 2.276   -23.258 8.862   1.00 22.70 ? 37  THR A N   1 
ATOM   2391 C  CA  . THR B 1 37  ? 1.390   -24.307 9.347   1.00 24.05 ? 37  THR A CA  1 
ATOM   2392 C  C   . THR B 1 37  ? 2.082   -25.595 9.785   1.00 27.45 ? 37  THR A C   1 
ATOM   2393 O  O   . THR B 1 37  ? 1.504   -26.294 10.564  1.00 29.10 ? 37  THR A O   1 
ATOM   2394 C  CB  . THR B 1 37  ? 0.243   -24.598 8.385   1.00 25.00 ? 37  THR A CB  1 
ATOM   2395 O  OG1 . THR B 1 37  ? 0.782   -24.984 7.126   1.00 27.03 ? 37  THR A OG1 1 
ATOM   2396 C  CG2 . THR B 1 37  ? -0.605  -23.410 8.184   1.00 24.08 ? 37  THR A CG2 1 
ATOM   2397 N  N   . LYS B 1 38  ? 3.280   -25.896 9.256   1.00 26.03 ? 38  LYS A N   1 
ATOM   2398 C  CA  . LYS B 1 38  ? 4.069   -27.052 9.664   1.00 26.44 ? 38  LYS A CA  1 
ATOM   2399 C  C   . LYS B 1 38  ? 4.815   -26.781 10.926  1.00 24.66 ? 38  LYS A C   1 
ATOM   2400 O  O   . LYS B 1 38  ? 5.369   -27.730 11.557  1.00 28.71 ? 38  LYS A O   1 
ATOM   2401 C  CB  . LYS B 1 38  ? 5.072   -27.490 8.577   1.00 29.12 ? 38  LYS A CB  1 
ATOM   2402 C  CG  . LYS B 1 38  ? 4.354   -28.085 7.374   1.00 34.30 ? 38  LYS A CG  1 
ATOM   2403 C  CD  . LYS B 1 38  ? 4.191   -29.609 7.429   1.00 41.40 ? 38  LYS A CD  1 
ATOM   2404 C  CE  . LYS B 1 38  ? 3.680   -30.101 6.094   1.00 48.84 ? 38  LYS A CE  1 
ATOM   2405 N  NZ  . LYS B 1 38  ? 3.834   -31.579 6.021   1.00 59.48 ? 38  LYS A NZ  1 
ATOM   2406 N  N   . GLU B 1 39  ? 4.868   -25.515 11.344  1.00 22.36 ? 39  GLU A N   1 
ATOM   2407 C  CA  . GLU B 1 39  ? 5.513   -25.169 12.570  1.00 23.60 ? 39  GLU A CA  1 
ATOM   2408 C  C   . GLU B 1 39  ? 4.602   -24.984 13.766  1.00 22.29 ? 39  GLU A C   1 
ATOM   2409 O  O   . GLU B 1 39  ? 5.079   -24.785 14.875  1.00 24.75 ? 39  GLU A O   1 
ATOM   2410 C  CB  . GLU B 1 39  ? 6.358   -23.882 12.432  1.00 26.70 ? 39  GLU A CB  1 
ATOM   2411 C  CG  . GLU B 1 39  ? 7.344   -23.847 11.278  1.00 29.23 ? 39  GLU A CG  1 
ATOM   2412 C  CD  . GLU B 1 39  ? 8.192   -25.076 11.216  1.00 35.57 ? 39  GLU A CD  1 
ATOM   2413 O  OE1 . GLU B 1 39  ? 8.790   -25.417 12.259  1.00 42.53 ? 39  GLU A OE1 1 
ATOM   2414 O  OE2 . GLU B 1 39  ? 8.217   -25.711 10.138  1.00 35.96 ? 39  GLU A OE2 1 
ATOM   2415 N  N   . VAL B 1 40  ? 3.280   -24.945 13.519  1.00 21.46 ? 40  VAL A N   1 
ATOM   2416 C  CA  . VAL B 1 40  ? 2.408   -24.611 14.613  1.00 22.82 ? 40  VAL A CA  1 
ATOM   2417 C  C   . VAL B 1 40  ? 2.279   -25.863 15.467  1.00 23.40 ? 40  VAL A C   1 
ATOM   2418 O  O   . VAL B 1 40  ? 2.493   -26.995 14.954  1.00 25.86 ? 40  VAL A O   1 
ATOM   2419 C  CB  . VAL B 1 40  ? 1.039   -24.117 14.122  1.00 23.80 ? 40  VAL A CB  1 
ATOM   2420 C  CG1 . VAL B 1 40  ? 1.196   -22.937 13.181  1.00 25.61 ? 40  VAL A CG1 1 
ATOM   2421 C  CG2 . VAL B 1 40  ? 0.272   -25.217 13.469  1.00 26.75 ? 40  VAL A CG2 1 
ATOM   2422 N  N   . LYS B 1 41  ? 2.008   -25.669 16.757  1.00 19.71 ? 41  LYS A N   1 
ATOM   2423 C  CA  . LYS B 1 41  ? 1.770   -26.796 17.642  1.00 25.35 ? 41  LYS A CA  1 
ATOM   2424 C  C   . LYS B 1 41  ? 0.276   -27.021 17.892  1.00 24.48 ? 41  LYS A C   1 
ATOM   2425 O  O   . LYS B 1 41  ? -0.400  -26.149 18.513  1.00 22.18 ? 41  LYS A O   1 
ATOM   2426 C  CB  . LYS B 1 41  ? 2.475   -26.556 18.984  1.00 26.84 ? 41  LYS A CB  1 
ATOM   2427 C  CG  . LYS B 1 41  ? 3.986   -26.236 18.922  1.00 36.78 ? 41  LYS A CG  1 
ATOM   2428 C  CD  . LYS B 1 41  ? 4.849   -27.025 17.904  1.00 42.38 ? 41  LYS A CD  1 
ATOM   2429 C  CE  . LYS B 1 41  ? 6.182   -26.271 17.694  1.00 46.71 ? 41  LYS A CE  1 
ATOM   2430 N  NZ  . LYS B 1 41  ? 6.906   -26.421 16.376  1.00 44.21 ? 41  LYS A NZ  1 
ATOM   2431 N  N   . TYR B 1 42  ? -0.200  -28.223 17.501  1.00 21.95 ? 42  TYR A N   1 
ATOM   2432 C  CA  . TYR B 1 42  ? -1.542  -28.625 17.843  1.00 23.21 ? 42  TYR A CA  1 
ATOM   2433 C  C   . TYR B 1 42  ? -1.579  -28.756 19.361  1.00 22.33 ? 42  TYR A C   1 
ATOM   2434 O  O   . TYR B 1 42  ? -0.669  -29.383 19.972  1.00 23.73 ? 42  TYR A O   1 
ATOM   2435 C  CB  . TYR B 1 42  ? -1.944  -29.979 17.219  1.00 22.71 ? 42  TYR A CB  1 
ATOM   2436 C  CG  . TYR B 1 42  ? -3.206  -30.521 17.803  1.00 23.83 ? 42  TYR A CG  1 
ATOM   2437 C  CD1 . TYR B 1 42  ? -4.446  -29.869 17.607  1.00 22.77 ? 42  TYR A CD1 1 
ATOM   2438 C  CD2 . TYR B 1 42  ? -3.203  -31.692 18.604  1.00 25.15 ? 42  TYR A CD2 1 
ATOM   2439 C  CE1 . TYR B 1 42  ? -5.608  -30.333 18.220  1.00 28.02 ? 42  TYR A CE1 1 
ATOM   2440 C  CE2 . TYR B 1 42  ? -4.370  -32.177 19.199  1.00 25.61 ? 42  TYR A CE2 1 
ATOM   2441 C  CZ  . TYR B 1 42  ? -5.576  -31.525 18.974  1.00 29.51 ? 42  TYR A CZ  1 
ATOM   2442 O  OH  . TYR B 1 42  ? -6.750  -31.952 19.542  1.00 30.48 ? 42  TYR A OH  1 
ATOM   2443 N  N   . ASP B 1 43  ? -2.586  -28.184 19.991  1.00 20.01 ? 43  ASP A N   1 
ATOM   2444 C  CA  . ASP B 1 43  ? -2.726  -28.139 21.419  1.00 18.18 ? 43  ASP A CA  1 
ATOM   2445 C  C   . ASP B 1 43  ? -4.101  -28.648 21.823  1.00 21.86 ? 43  ASP A C   1 
ATOM   2446 O  O   . ASP B 1 43  ? -5.120  -27.926 21.652  1.00 21.13 ? 43  ASP A O   1 
ATOM   2447 C  CB  . ASP B 1 43  ? -2.491  -26.749 21.987  1.00 18.69 ? 43  ASP A CB  1 
ATOM   2448 C  CG  . ASP B 1 43  ? -2.407  -26.746 23.502  1.00 20.15 ? 43  ASP A CG  1 
ATOM   2449 O  OD1 . ASP B 1 43  ? -2.947  -27.714 24.151  1.00 21.89 ? 43  ASP A OD1 1 
ATOM   2450 O  OD2 . ASP B 1 43  ? -1.781  -25.873 24.047  1.00 24.93 ? 43  ASP A OD2 1 
ATOM   2451 N  N   . SER B 1 44  ? -4.182  -29.881 22.330  1.00 20.79 ? 44  SER A N   1 
ATOM   2452 C  CA  . SER B 1 44  ? -5.505  -30.481 22.639  1.00 22.90 ? 44  SER A CA  1 
ATOM   2453 C  C   . SER B 1 44  ? -6.158  -29.810 23.867  1.00 23.68 ? 44  SER A C   1 
ATOM   2454 O  O   . SER B 1 44  ? -7.360  -30.031 24.103  1.00 25.03 ? 44  SER A O   1 
ATOM   2455 C  CB  . SER B 1 44  ? -5.439  -32.028 22.835  1.00 26.81 ? 44  SER A CB  1 
ATOM   2456 O  OG  . SER B 1 44  ? -4.565  -32.253 23.900  1.00 28.51 ? 44  SER A OG  1 
ATOM   2457 N  N   . SER B 1 45  ? -5.431  -28.968 24.599  1.00 21.21 ? 45  SER A N   1 
ATOM   2458 C  CA  . SER B 1 45  ? -6.006  -28.215 25.699  1.00 22.91 ? 45  SER A CA  1 
ATOM   2459 C  C   . SER B 1 45  ? -6.834  -26.977 25.246  1.00 21.84 ? 45  SER A C   1 
ATOM   2460 O  O   . SER B 1 45  ? -7.545  -26.387 26.091  1.00 23.34 ? 45  SER A O   1 
ATOM   2461 C  CB  . SER B 1 45  ? -4.963  -27.804 26.734  1.00 26.36 ? 45  SER A CB  1 
ATOM   2462 O  OG  . SER B 1 45  ? -4.095  -26.712 26.304  1.00 23.14 ? 45  SER A OG  1 
ATOM   2463 N  N   . LEU B 1 46  ? -6.681  -26.577 23.974  1.00 19.57 ? 46  LEU A N   1 
ATOM   2464 C  CA  . LEU B 1 46  ? -7.412  -25.384 23.415  1.00 17.96 ? 46  LEU A CA  1 
ATOM   2465 C  C   . LEU B 1 46  ? -8.844  -25.810 23.284  1.00 19.49 ? 46  LEU A C   1 
ATOM   2466 O  O   . LEU B 1 46  ? -9.157  -26.950 23.000  1.00 22.88 ? 46  LEU A O   1 
ATOM   2467 C  CB  . LEU B 1 46  ? -6.915  -25.097 21.994  1.00 17.61 ? 46  LEU A CB  1 
ATOM   2468 C  CG  . LEU B 1 46  ? -5.595  -24.309 22.026  1.00 15.41 ? 46  LEU A CG  1 
ATOM   2469 C  CD1 . LEU B 1 46  ? -5.014  -24.191 20.587  1.00 16.28 ? 46  LEU A CD1 1 
ATOM   2470 C  CD2 . LEU B 1 46  ? -5.738  -22.953 22.760  1.00 15.87 ? 46  LEU A CD2 1 
ATOM   2471 N  N   . ARG B 1 47  ? -9.726  -24.864 23.396  1.00 17.42 ? 47  ARG A N   1 
ATOM   2472 C  CA  . ARG B 1 47  ? -11.148 -25.182 23.330  1.00 16.92 ? 47  ARG A CA  1 
ATOM   2473 C  C   . ARG B 1 47  ? -11.763 -24.622 22.056  1.00 17.96 ? 47  ARG A C   1 
ATOM   2474 O  O   . ARG B 1 47  ? -11.212 -23.718 21.501  1.00 18.51 ? 47  ARG A O   1 
ATOM   2475 C  CB  . ARG B 1 47  ? -11.849 -24.510 24.487  1.00 15.20 ? 47  ARG A CB  1 
ATOM   2476 C  CG  . ARG B 1 47  ? -11.472 -25.240 25.777  1.00 18.85 ? 47  ARG A CG  1 
ATOM   2477 C  CD  . ARG B 1 47  ? -12.085 -24.601 26.942  1.00 21.88 ? 47  ARG A CD  1 
ATOM   2478 N  NE  . ARG B 1 47  ? -11.774 -25.374 28.148  1.00 26.99 ? 47  ARG A NE  1 
ATOM   2479 C  CZ  . ARG B 1 47  ? -12.076 -24.889 29.372  1.00 25.95 ? 47  ARG A CZ  1 
ATOM   2480 N  NH1 . ARG B 1 47  ? -12.658 -23.696 29.462  1.00 32.53 ? 47  ARG A NH1 1 
ATOM   2481 N  NH2 . ARG B 1 47  ? -11.790 -25.597 30.461  1.00 31.27 ? 47  ARG A NH2 1 
ATOM   2482 N  N   . PRO B 1 48  ? -12.908 -25.173 21.618  1.00 16.10 ? 48  PRO A N   1 
ATOM   2483 C  CA  . PRO B 1 48  ? -13.622 -24.458 20.509  1.00 15.06 ? 48  PRO A CA  1 
ATOM   2484 C  C   . PRO B 1 48  ? -14.012 -23.044 20.963  1.00 15.47 ? 48  PRO A C   1 
ATOM   2485 O  O   . PRO B 1 48  ? -14.221 -22.784 22.147  1.00 14.04 ? 48  PRO A O   1 
ATOM   2486 C  CB  . PRO B 1 48  ? -14.896 -25.324 20.298  1.00 16.71 ? 48  PRO A CB  1 
ATOM   2487 C  CG  . PRO B 1 48  ? -14.536 -26.746 20.760  1.00 17.55 ? 48  PRO A CG  1 
ATOM   2488 C  CD  . PRO B 1 48  ? -13.642 -26.402 21.982  1.00 15.70 ? 48  PRO A CD  1 
ATOM   2489 N  N   . LEU B 1 49  ? -14.206 -22.149 19.994  1.00 14.69 ? 49  LEU A N   1 
ATOM   2490 C  CA  . LEU B 1 49  ? -14.660 -20.781 20.378  1.00 15.85 ? 49  LEU A CA  1 
ATOM   2491 C  C   . LEU B 1 49  ? -16.139 -20.852 20.827  1.00 14.79 ? 49  LEU A C   1 
ATOM   2492 O  O   . LEU B 1 49  ? -16.946 -21.578 20.180  1.00 12.95 ? 49  LEU A O   1 
ATOM   2493 C  CB  . LEU B 1 49  ? -14.578 -19.952 19.147  1.00 14.08 ? 49  LEU A CB  1 
ATOM   2494 C  CG  . LEU B 1 49  ? -13.092 -19.848 18.690  1.00 14.33 ? 49  LEU A CG  1 
ATOM   2495 C  CD1 . LEU B 1 49  ? -13.092 -19.020 17.408  1.00 14.82 ? 49  LEU A CD1 1 
ATOM   2496 C  CD2 . LEU B 1 49  ? -12.278 -19.189 19.808  1.00 15.70 ? 49  LEU A CD2 1 
ATOM   2497 N  N   . SER B 1 50  ? -16.452 -20.089 21.858  1.00 13.17 ? 50  SER A N   1 
ATOM   2498 C  CA  . SER B 1 50  ? -17.860 -19.928 22.340  1.00 13.59 ? 50  SER A CA  1 
ATOM   2499 C  C   . SER B 1 50  ? -18.241 -18.483 22.014  1.00 14.05 ? 50  SER A C   1 
ATOM   2500 O  O   . SER B 1 50  ? -17.697 -17.563 22.617  1.00 13.67 ? 50  SER A O   1 
ATOM   2501 C  CB  . SER B 1 50  ? -17.891 -20.169 23.830  1.00 15.22 ? 50  SER A CB  1 
ATOM   2502 O  OG  . SER B 1 50  ? -19.173 -19.849 24.283  1.00 18.12 ? 50  SER A OG  1 
ATOM   2503 N  N   . ILE B 1 51  ? -19.086 -18.326 20.975  1.00 11.72 ? 51  ILE A N   1 
ATOM   2504 C  CA  . ILE B 1 51  ? -19.322 -16.957 20.458  1.00 12.99 ? 51  ILE A CA  1 
ATOM   2505 C  C   . ILE B 1 51  ? -20.761 -16.507 20.593  1.00 12.17 ? 51  ILE A C   1 
ATOM   2506 O  O   . ILE B 1 51  ? -21.630 -17.196 20.115  1.00 14.93 ? 51  ILE A O   1 
ATOM   2507 C  CB  . ILE B 1 51  ? -18.931 -16.947 18.958  1.00 13.51 ? 51  ILE A CB  1 
ATOM   2508 C  CG1 . ILE B 1 51  ? -17.585 -17.641 18.771  1.00 14.14 ? 51  ILE A CG1 1 
ATOM   2509 C  CG2 . ILE B 1 51  ? -18.920 -15.487 18.430  1.00 15.03 ? 51  ILE A CG2 1 
ATOM   2510 C  CD1 . ILE B 1 51  ? -17.039 -17.392 17.336  1.00 14.86 ? 51  ILE A CD1 1 
ATOM   2511 N  N   . LYS B 1 52  ? -20.984 -15.335 21.203  1.00 11.67 ? 52  LYS A N   1 
ATOM   2512 C  CA  . LYS B 1 52  ? -22.295 -14.781 21.285  1.00 13.39 ? 52  LYS A CA  1 
ATOM   2513 C  C   . LYS B 1 52  ? -22.268 -13.353 20.887  1.00 13.94 ? 52  LYS A C   1 
ATOM   2514 O  O   . LYS B 1 52  ? -21.666 -12.547 21.595  1.00 13.25 ? 52  LYS A O   1 
ATOM   2515 C  CB  . LYS B 1 52  ? -22.789 -14.900 22.711  1.00 13.74 ? 52  LYS A CB  1 
ATOM   2516 C  CG  . LYS B 1 52  ? -24.229 -14.379 22.821  1.00 15.42 ? 52  LYS A CG  1 
ATOM   2517 C  CD  . LYS B 1 52  ? -24.546 -14.233 24.278  1.00 15.42 ? 52  LYS A CD  1 
ATOM   2518 C  CE  . LYS B 1 52  ? -26.035 -13.832 24.408  1.00 16.44 ? 52  LYS A CE  1 
ATOM   2519 N  NZ  . LYS B 1 52  ? -26.482 -12.534 23.724  1.00 16.22 ? 52  LYS A NZ  1 
ATOM   2520 N  N   . TYR B 1 53  ? -22.893 -12.999 19.750  1.00 14.41 ? 53  TYR A N   1 
ATOM   2521 C  CA  . TYR B 1 53  ? -22.822 -11.597 19.276  1.00 14.54 ? 53  TYR A CA  1 
ATOM   2522 C  C   . TYR B 1 53  ? -24.273 -11.183 18.997  1.00 14.35 ? 53  TYR A C   1 
ATOM   2523 O  O   . TYR B 1 53  ? -24.904 -11.800 18.135  1.00 16.24 ? 53  TYR A O   1 
ATOM   2524 C  CB  . TYR B 1 53  ? -22.005 -11.546 17.956  1.00 13.93 ? 53  TYR A CB  1 
ATOM   2525 C  CG  . TYR B 1 53  ? -20.545 -11.751 18.065  1.00 11.95 ? 53  TYR A CG  1 
ATOM   2526 C  CD1 . TYR B 1 53  ? -19.813 -11.432 19.244  1.00 13.07 ? 53  TYR A CD1 1 
ATOM   2527 C  CD2 . TYR B 1 53  ? -19.824 -12.308 16.993  1.00 11.76 ? 53  TYR A CD2 1 
ATOM   2528 C  CE1 . TYR B 1 53  ? -18.403 -11.618 19.253  1.00 11.82 ? 53  TYR A CE1 1 
ATOM   2529 C  CE2 . TYR B 1 53  ? -18.424 -12.512 17.065  1.00 12.94 ? 53  TYR A CE2 1 
ATOM   2530 C  CZ  . TYR B 1 53  ? -17.740 -12.160 18.206  1.00 11.58 ? 53  TYR A CZ  1 
ATOM   2531 O  OH  . TYR B 1 53  ? -16.408 -12.328 18.269  1.00 12.64 ? 53  TYR A OH  1 
ATOM   2532 N  N   . ASP B 1 54  ? -24.749 -10.134 19.699  1.00 15.07 ? 54  ASP A N   1 
ATOM   2533 C  CA  . ASP B 1 54  ? -26.154 -9.661  19.603  1.00 15.20 ? 54  ASP A CA  1 
ATOM   2534 C  C   . ASP B 1 54  ? -26.164 -8.602  18.468  1.00 16.62 ? 54  ASP A C   1 
ATOM   2535 O  O   . ASP B 1 54  ? -25.375 -7.665  18.504  1.00 17.43 ? 54  ASP A O   1 
ATOM   2536 C  CB  . ASP B 1 54  ? -26.505 -9.009  20.924  1.00 16.05 ? 54  ASP A CB  1 
ATOM   2537 C  CG  . ASP B 1 54  ? -27.944 -8.534  21.002  1.00 22.20 ? 54  ASP A CG  1 
ATOM   2538 O  OD1 . ASP B 1 54  ? -28.567 -8.211  19.946  1.00 20.51 ? 54  ASP A OD1 1 
ATOM   2539 O  OD2 . ASP B 1 54  ? -28.454 -8.595  22.152  1.00 24.80 ? 54  ASP A OD2 1 
ATOM   2540 N  N   . PRO B 1 55  ? -26.909 -8.866  17.360  1.00 18.16 ? 55  PRO A N   1 
ATOM   2541 C  CA  . PRO B 1 55  ? -26.927 -7.887  16.211  1.00 17.33 ? 55  PRO A CA  1 
ATOM   2542 C  C   . PRO B 1 55  ? -27.292 -6.448  16.636  1.00 18.95 ? 55  PRO A C   1 
ATOM   2543 O  O   . PRO B 1 55  ? -26.877 -5.485  15.962  1.00 20.78 ? 55  PRO A O   1 
ATOM   2544 C  CB  . PRO B 1 55  ? -27.984 -8.452  15.292  1.00 20.37 ? 55  PRO A CB  1 
ATOM   2545 C  CG  . PRO B 1 55  ? -27.898 -9.955  15.636  1.00 19.26 ? 55  PRO A CG  1 
ATOM   2546 C  CD  . PRO B 1 55  ? -27.809 -10.028 17.132  1.00 18.62 ? 55  PRO A CD  1 
ATOM   2547 N  N   . SER B 1 56  ? -27.983 -6.315  17.745  1.00 19.15 ? 56  SER A N   1 
ATOM   2548 C  CA  . SER B 1 56  ? -28.377 -4.976  18.247  1.00 22.54 ? 56  SER A CA  1 
ATOM   2549 C  C   . SER B 1 56  ? -27.277 -4.235  19.021  1.00 20.90 ? 56  SER A C   1 
ATOM   2550 O  O   . SER B 1 56  ? -27.380 -3.046  19.398  1.00 22.94 ? 56  SER A O   1 
ATOM   2551 C  CB  . SER B 1 56  ? -29.676 -5.077  19.074  1.00 24.49 ? 56  SER A CB  1 
ATOM   2552 O  OG  . SER B 1 56  ? -29.389 -5.501  20.412  1.00 33.69 ? 56  SER A OG  1 
ATOM   2553 N  N   . SER B 1 57  ? -26.164 -4.919  19.308  1.00 16.06 ? 57  SER A N   1 
ATOM   2554 C  CA  . SER B 1 57  ? -25.025 -4.315  20.011  1.00 17.29 ? 57  SER A CA  1 
ATOM   2555 C  C   . SER B 1 57  ? -24.323 -3.296  19.108  1.00 17.58 ? 57  SER A C   1 
ATOM   2556 O  O   . SER B 1 57  ? -23.697 -2.435  19.660  1.00 18.69 ? 57  SER A O   1 
ATOM   2557 C  CB  . SER B 1 57  ? -23.939 -5.439  20.311  1.00 17.79 ? 57  SER A CB  1 
ATOM   2558 O  OG  . SER B 1 57  ? -24.386 -6.242  21.376  1.00 19.50 ? 57  SER A OG  1 
ATOM   2559 N  N   . ALA B 1 58  ? -24.347 -3.489  17.763  1.00 17.53 ? 58  ALA A N   1 
ATOM   2560 C  CA  . ALA B 1 58  ? -23.628 -2.558  16.868  1.00 16.93 ? 58  ALA A CA  1 
ATOM   2561 C  C   . ALA B 1 58  ? -24.416 -1.265  16.921  1.00 15.88 ? 58  ALA A C   1 
ATOM   2562 O  O   . ALA B 1 58  ? -25.607 -1.307  16.836  1.00 16.37 ? 58  ALA A O   1 
ATOM   2563 C  CB  . ALA B 1 58  ? -23.588 -3.058  15.424  1.00 15.89 ? 58  ALA A CB  1 
ATOM   2564 N  N   . LYS B 1 59  ? -23.682 -0.156  17.031  1.00 14.55 ? 59  LYS A N   1 
ATOM   2565 C  CA  . LYS B 1 59  ? -24.389 1.128   17.164  1.00 15.97 ? 59  LYS A CA  1 
ATOM   2566 C  C   . LYS B 1 59  ? -23.930 2.211   16.167  1.00 18.15 ? 59  LYS A C   1 
ATOM   2567 O  O   . LYS B 1 59  ? -24.777 2.978   15.725  1.00 17.34 ? 59  LYS A O   1 
ATOM   2568 C  CB  . LYS B 1 59  ? -24.088 1.681   18.554  1.00 17.50 ? 59  LYS A CB  1 
ATOM   2569 C  CG  . LYS B 1 59  ? -24.699 0.846   19.677  1.00 17.47 ? 59  LYS A CG  1 
ATOM   2570 C  CD  . LYS B 1 59  ? -26.192 0.642   19.597  1.00 18.17 ? 59  LYS A CD  1 
ATOM   2571 C  CE  . LYS B 1 59  ? -26.726 -0.184  20.784  1.00 20.32 ? 59  LYS A CE  1 
ATOM   2572 N  NZ  . LYS B 1 59  ? -28.127 -0.619  20.608  1.00 20.10 ? 59  LYS A NZ  1 
ATOM   2573 N  N   . ILE B 1 60  ? -22.653 2.279   15.860  1.00 17.86 ? 60  ILE A N   1 
ATOM   2574 C  CA  . ILE B 1 60  ? -22.139 3.398   15.060  1.00 21.07 ? 60  ILE A CA  1 
ATOM   2575 C  C   . ILE B 1 60  ? -21.029 2.877   14.188  1.00 19.11 ? 60  ILE A C   1 
ATOM   2576 O  O   . ILE B 1 60  ? -20.264 1.983   14.617  1.00 18.82 ? 60  ILE A O   1 
ATOM   2577 C  CB  . ILE B 1 60  ? -21.566 4.429   16.052  1.00 19.03 ? 60  ILE A CB  1 
ATOM   2578 C  CG1 . ILE B 1 60  ? -22.733 5.030   16.837  1.00 25.41 ? 60  ILE A CG1 1 
ATOM   2579 C  CG2 . ILE B 1 60  ? -20.730 5.560   15.378  1.00 20.51 ? 60  ILE A CG2 1 
ATOM   2580 C  CD1 . ILE B 1 60  ? -22.295 5.970   17.936  1.00 30.60 ? 60  ILE A CD1 1 
ATOM   2581 N  N   . ILE B 1 61  ? -20.884 3.453   12.998  1.00 16.01 ? 61  ILE A N   1 
ATOM   2582 C  CA  . ILE B 1 61  ? -19.728 3.187   12.130  1.00 15.51 ? 61  ILE A CA  1 
ATOM   2583 C  C   . ILE B 1 61  ? -18.990 4.509   11.887  1.00 18.31 ? 61  ILE A C   1 
ATOM   2584 O  O   . ILE B 1 61  ? -19.678 5.531   11.732  1.00 17.83 ? 61  ILE A O   1 
ATOM   2585 C  CB  . ILE B 1 61  ? -20.108 2.442   10.837  1.00 16.91 ? 61  ILE A CB  1 
ATOM   2586 C  CG1 . ILE B 1 61  ? -18.818 1.966   10.144  1.00 14.56 ? 61  ILE A CG1 1 
ATOM   2587 C  CG2 . ILE B 1 61  ? -21.040 3.271   9.963   1.00 17.03 ? 61  ILE A CG2 1 
ATOM   2588 C  CD1 . ILE B 1 61  ? -19.078 1.080   8.942   1.00 18.16 ? 61  ILE A CD1 1 
ATOM   2589 N  N   . SER B 1 62  ? -17.669 4.475   11.972  1.00 19.50 ? 62  SER A N   1 
ATOM   2590 C  CA  . SER B 1 62  ? -16.948 5.759   11.808  1.00 18.41 ? 62  SER A CA  1 
ATOM   2591 C  C   . SER B 1 62  ? -15.700 5.580   11.004  1.00 21.42 ? 62  SER A C   1 
ATOM   2592 O  O   . SER B 1 62  ? -15.202 4.474   10.847  1.00 18.12 ? 62  SER A O   1 
ATOM   2593 C  CB  . SER B 1 62  ? -16.660 6.393   13.140  1.00 21.61 ? 62  SER A CB  1 
ATOM   2594 O  OG  . SER B 1 62  ? -15.807 5.570   13.919  1.00 25.38 ? 62  SER A OG  1 
ATOM   2595 N  N   . ASN B 1 63  ? -15.239 6.673   10.365  1.00 18.29 ? 63  ASN A N   1 
ATOM   2596 C  CA  . ASN B 1 63  ? -13.932 6.630   9.739   1.00 18.99 ? 63  ASN A CA  1 
ATOM   2597 C  C   . ASN B 1 63  ? -12.897 7.159   10.693  1.00 18.62 ? 63  ASN A C   1 
ATOM   2598 O  O   . ASN B 1 63  ? -12.874 8.350   11.020  1.00 22.55 ? 63  ASN A O   1 
ATOM   2599 C  CB  . ASN B 1 63  ? -13.977 7.425   8.427   1.00 19.71 ? 63  ASN A CB  1 
ATOM   2600 C  CG  . ASN B 1 63  ? -12.651 7.466   7.693   1.00 20.80 ? 63  ASN A CG  1 
ATOM   2601 O  OD1 . ASN B 1 63  ? -11.583 6.957   8.146   1.00 18.69 ? 63  ASN A OD1 1 
ATOM   2602 N  ND2 . ASN B 1 63  ? -12.710 8.100   6.460   1.00 17.75 ? 63  ASN A ND2 1 
ATOM   2603 N  N   . SER B 1 64  ? -12.006 6.308   11.155  1.00 17.80 ? 64  SER A N   1 
ATOM   2604 C  CA  . SER B 1 64  ? -10.882 6.747   12.007  1.00 18.76 ? 64  SER A CA  1 
ATOM   2605 C  C   . SER B 1 64  ? -9.712  7.455   11.331  1.00 18.73 ? 64  SER A C   1 
ATOM   2606 O  O   . SER B 1 64  ? -8.841  8.002   11.991  1.00 22.55 ? 64  SER A O   1 
ATOM   2607 C  CB  . SER B 1 64  ? -10.321 5.591   12.816  1.00 20.70 ? 64  SER A CB  1 
ATOM   2608 O  OG  . SER B 1 64  ? -9.653  4.666   11.929  1.00 19.40 ? 64  SER A OG  1 
ATOM   2609 N  N   . GLY B 1 65  ? -9.698  7.452   10.005  1.00 16.93 ? 65  GLY A N   1 
ATOM   2610 C  CA  . GLY B 1 65  ? -8.487  7.850   9.256   1.00 19.95 ? 65  GLY A CA  1 
ATOM   2611 C  C   . GLY B 1 65  ? -7.643  6.637   8.937   1.00 19.72 ? 65  GLY A C   1 
ATOM   2612 O  O   . GLY B 1 65  ? -6.868  6.680   8.015   1.00 20.66 ? 65  GLY A O   1 
ATOM   2613 N  N   . HIS B 1 66  ? -7.791  5.548   9.718   1.00 18.03 ? 66  HIS A N   1 
ATOM   2614 C  CA  . HIS B 1 66  ? -6.971  4.299   9.601   1.00 16.79 ? 66  HIS A CA  1 
ATOM   2615 C  C   . HIS B 1 66  ? -7.693  3.051   9.134   1.00 15.15 ? 66  HIS A C   1 
ATOM   2616 O  O   . HIS B 1 66  ? -7.044  2.097   8.736   1.00 15.53 ? 66  HIS A O   1 
ATOM   2617 C  CB  . HIS B 1 66  ? -6.331  4.013   10.952  1.00 19.64 ? 66  HIS A CB  1 
ATOM   2618 C  CG  . HIS B 1 66  ? -5.813  5.240   11.615  1.00 24.48 ? 66  HIS A CG  1 
ATOM   2619 N  ND1 . HIS B 1 66  ? -4.837  6.017   11.036  1.00 26.48 ? 66  HIS A ND1 1 
ATOM   2620 C  CD2 . HIS B 1 66  ? -6.170  5.854   12.803  1.00 27.65 ? 66  HIS A CD2 1 
ATOM   2621 C  CE1 . HIS B 1 66  ? -4.556  7.070   11.861  1.00 26.97 ? 66  HIS A CE1 1 
ATOM   2622 N  NE2 . HIS B 1 66  ? -5.363  6.974   12.946  1.00 25.04 ? 66  HIS A NE2 1 
ATOM   2623 N  N   . SER B 1 67  ? -9.036  3.080   9.254   1.00 17.02 ? 67  SER A N   1 
ATOM   2624 C  CA  . SER B 1 67  ? -9.976  2.022   8.803   1.00 15.15 ? 67  SER A CA  1 
ATOM   2625 C  C   . SER B 1 67  ? -11.343 2.555   9.058   1.00 15.76 ? 67  SER A C   1 
ATOM   2626 O  O   . SER B 1 67  ? -11.498 3.722   9.464   1.00 17.76 ? 67  SER A O   1 
ATOM   2627 C  CB  . SER B 1 67  ? -9.779  0.698   9.620   1.00 14.77 ? 67  SER A CB  1 
ATOM   2628 O  OG  . SER B 1 67  ? -10.567 -0.324  8.998   1.00 13.77 ? 67  SER A OG  1 
ATOM   2629 N  N   . PHE B 1 68  ? -12.401 1.772   8.821   1.00 15.02 ? 68  PHE A N   1 
ATOM   2630 C  CA  . PHE B 1 68  ? -13.712 2.138   9.468   1.00 14.52 ? 68  PHE A CA  1 
ATOM   2631 C  C   . PHE B 1 68  ? -13.712 1.349   10.808  1.00 15.85 ? 68  PHE A C   1 
ATOM   2632 O  O   . PHE B 1 68  ? -13.082 0.341   10.919  1.00 15.94 ? 68  PHE A O   1 
ATOM   2633 C  CB  . PHE B 1 68  ? -14.946 1.655   8.621   1.00 15.62 ? 68  PHE A CB  1 
ATOM   2634 C  CG  . PHE B 1 68  ? -15.077 0.125   8.566   1.00 16.03 ? 68  PHE A CG  1 
ATOM   2635 C  CD1 . PHE B 1 68  ? -14.502 -0.585  7.504   1.00 17.37 ? 68  PHE A CD1 1 
ATOM   2636 C  CD2 . PHE B 1 68  ? -15.745 -0.601  9.566   1.00 17.21 ? 68  PHE A CD2 1 
ATOM   2637 C  CE1 . PHE B 1 68  ? -14.574 -1.975  7.472   1.00 16.60 ? 68  PHE A CE1 1 
ATOM   2638 C  CE2 . PHE B 1 68  ? -15.845 -2.009  9.512   1.00 19.95 ? 68  PHE A CE2 1 
ATOM   2639 C  CZ  . PHE B 1 68  ? -15.248 -2.703  8.476   1.00 18.23 ? 68  PHE A CZ  1 
ATOM   2640 N  N   . ASN B 1 69  ? -14.460 1.838   11.786  1.00 15.58 ? 69  ASN A N   1 
ATOM   2641 C  CA  . ASN B 1 69  ? -14.706 1.099   13.009  1.00 17.60 ? 69  ASN A CA  1 
ATOM   2642 C  C   . ASN B 1 69  ? -16.175 1.032   13.243  1.00 17.52 ? 69  ASN A C   1 
ATOM   2643 O  O   . ASN B 1 69  ? -16.882 2.123   13.230  1.00 16.28 ? 69  ASN A O   1 
ATOM   2644 C  CB  . ASN B 1 69  ? -14.181 1.917   14.186  1.00 17.58 ? 69  ASN A CB  1 
ATOM   2645 C  CG  . ASN B 1 69  ? -12.661 2.067   14.216  1.00 22.30 ? 69  ASN A CG  1 
ATOM   2646 O  OD1 . ASN B 1 69  ? -11.956 1.215   13.667  1.00 26.98 ? 69  ASN A OD1 1 
ATOM   2647 N  ND2 . ASN B 1 69  ? -12.174 3.153   14.685  1.00 20.79 ? 69  ASN A ND2 1 
ATOM   2648 N  N   . VAL B 1 70  ? -16.694 -0.206  13.444  1.00 15.72 ? 70  VAL A N   1 
ATOM   2649 C  CA  . VAL B 1 70  ? -18.016 -0.401  13.902  1.00 15.37 ? 70  VAL A CA  1 
ATOM   2650 C  C   . VAL B 1 70  ? -17.890 -0.507  15.407  1.00 17.37 ? 70  VAL A C   1 
ATOM   2651 O  O   . VAL B 1 70  ? -17.160 -1.365  15.940  1.00 16.94 ? 70  VAL A O   1 
ATOM   2652 C  CB  . VAL B 1 70  ? -18.672 -1.673  13.303  1.00 16.25 ? 70  VAL A CB  1 
ATOM   2653 C  CG1 . VAL B 1 70  ? -19.995 -1.949  13.973  1.00 16.99 ? 70  VAL A CG1 1 
ATOM   2654 C  CG2 . VAL B 1 70  ? -18.925 -1.515  11.792  1.00 16.19 ? 70  VAL A CG2 1 
ATOM   2655 N  N   . ASP B 1 71  ? -18.519 0.416   16.112  1.00 14.43 ? 71  ASP A N   1 
ATOM   2656 C  CA  . ASP B 1 71  ? -18.465 0.446   17.597  1.00 16.39 ? 71  ASP A CA  1 
ATOM   2657 C  C   . ASP B 1 71  ? -19.717 -0.221  18.137  1.00 14.76 ? 71  ASP A C   1 
ATOM   2658 O  O   . ASP B 1 71  ? -20.852 -0.021  17.674  1.00 13.85 ? 71  ASP A O   1 
ATOM   2659 C  CB  . ASP B 1 71  ? -18.395 1.864   18.150  1.00 17.07 ? 71  ASP A CB  1 
ATOM   2660 C  CG  . ASP B 1 71  ? -17.051 2.525   17.883  1.00 25.94 ? 71  ASP A CG  1 
ATOM   2661 O  OD1 . ASP B 1 71  ? -15.988 1.843   17.794  1.00 30.23 ? 71  ASP A OD1 1 
ATOM   2662 O  OD2 . ASP B 1 71  ? -17.075 3.776   17.773  1.00 29.13 ? 71  ASP A OD2 1 
ATOM   2663 N  N   . PHE B 1 72  ? -19.503 -1.044  19.161  1.00 14.47 ? 72  PHE A N   1 
ATOM   2664 C  CA  . PHE B 1 72  ? -20.583 -1.814  19.861  1.00 15.83 ? 72  PHE A CA  1 
ATOM   2665 C  C   . PHE B 1 72  ? -20.762 -1.221  21.228  1.00 15.55 ? 72  PHE A C   1 
ATOM   2666 O  O   . PHE B 1 72  ? -19.802 -0.811  21.885  1.00 20.28 ? 72  PHE A O   1 
ATOM   2667 C  CB  . PHE B 1 72  ? -20.211 -3.330  19.945  1.00 14.91 ? 72  PHE A CB  1 
ATOM   2668 C  CG  . PHE B 1 72  ? -20.028 -3.977  18.579  1.00 14.04 ? 72  PHE A CG  1 
ATOM   2669 C  CD1 . PHE B 1 72  ? -18.858 -3.714  17.791  1.00 17.63 ? 72  PHE A CD1 1 
ATOM   2670 C  CD2 . PHE B 1 72  ? -21.051 -4.725  18.031  1.00 14.54 ? 72  PHE A CD2 1 
ATOM   2671 C  CE1 . PHE B 1 72  ? -18.749 -4.242  16.482  1.00 17.70 ? 72  PHE A CE1 1 
ATOM   2672 C  CE2 . PHE B 1 72  ? -20.908 -5.328  16.733  1.00 16.67 ? 72  PHE A CE2 1 
ATOM   2673 C  CZ  . PHE B 1 72  ? -19.722 -5.054  15.986  1.00 15.65 ? 72  PHE A CZ  1 
ATOM   2674 N  N   . ASP B 1 73  ? -21.965 -1.340  21.707  1.00 15.90 ? 73  ASP A N   1 
ATOM   2675 C  CA  . ASP B 1 73  ? -22.267 -0.926  23.094  1.00 15.83 ? 73  ASP A CA  1 
ATOM   2676 C  C   . ASP B 1 73  ? -21.698 -2.015  23.957  1.00 17.41 ? 73  ASP A C   1 
ATOM   2677 O  O   . ASP B 1 73  ? -22.174 -3.116  23.902  1.00 21.36 ? 73  ASP A O   1 
ATOM   2678 C  CB  . ASP B 1 73  ? -23.765 -0.865  23.224  1.00 17.41 ? 73  ASP A CB  1 
ATOM   2679 C  CG  . ASP B 1 73  ? -24.174 -0.477  24.616  1.00 16.64 ? 73  ASP A CG  1 
ATOM   2680 O  OD1 . ASP B 1 73  ? -23.301 -0.224  25.448  1.00 20.75 ? 73  ASP A OD1 1 
ATOM   2681 O  OD2 . ASP B 1 73  ? -25.401 -0.445  24.815  1.00 23.38 ? 73  ASP A OD2 1 
ATOM   2682 N  N   . ASP B 1 74  ? -20.646 -1.685  24.650  1.00 15.86 ? 74  ASP A N   1 
ATOM   2683 C  CA  . ASP B 1 74  ? -19.988 -2.652  25.564  1.00 17.70 ? 74  ASP A CA  1 
ATOM   2684 C  C   . ASP B 1 74  ? -20.278 -2.292  27.051  1.00 17.07 ? 74  ASP A C   1 
ATOM   2685 O  O   . ASP B 1 74  ? -19.415 -2.477  27.872  1.00 18.45 ? 74  ASP A O   1 
ATOM   2686 C  CB  . ASP B 1 74  ? -18.455 -2.732  25.283  1.00 17.62 ? 74  ASP A CB  1 
ATOM   2687 C  CG  . ASP B 1 74  ? -17.672 -1.475  25.683  1.00 21.34 ? 74  ASP A CG  1 
ATOM   2688 O  OD1 . ASP B 1 74  ? -18.324 -0.376  25.875  1.00 23.61 ? 74  ASP A OD1 1 
ATOM   2689 O  OD2 . ASP B 1 74  ? -16.437 -1.500  25.771  1.00 19.76 ? 74  ASP A OD2 1 
ATOM   2690 N  N   . THR B 1 75  ? -21.436 -1.680  27.259  1.00 21.25 ? 75  THR A N   1 
ATOM   2691 C  CA  . THR B 1 75  ? -21.997 -1.375  28.642  1.00 19.86 ? 75  THR A CA  1 
ATOM   2692 C  C   . THR B 1 75  ? -22.176 -2.655  29.421  1.00 22.22 ? 75  THR A C   1 
ATOM   2693 O  O   . THR B 1 75  ? -21.995 -2.652  30.628  1.00 19.60 ? 75  THR A O   1 
ATOM   2694 C  CB  . THR B 1 75  ? -23.413 -0.704  28.542  1.00 21.55 ? 75  THR A CB  1 
ATOM   2695 O  OG1 . THR B 1 75  ? -23.313 0.514   27.815  1.00 23.11 ? 75  THR A OG1 1 
ATOM   2696 C  CG2 . THR B 1 75  ? -24.030 -0.371  29.913  1.00 25.41 ? 75  THR A CG2 1 
ATOM   2697 N  N   . GLU B 1 76  ? -22.700 -3.707  28.820  1.00 22.71 ? 76  GLU A N   1 
ATOM   2698 C  CA  . GLU B 1 76  ? -22.731 -4.995  29.573  1.00 27.48 ? 76  GLU A CA  1 
ATOM   2699 C  C   . GLU B 1 76  ? -22.369 -6.192  28.707  1.00 24.32 ? 76  GLU A C   1 
ATOM   2700 O  O   . GLU B 1 76  ? -21.742 -5.974  27.640  1.00 21.40 ? 76  GLU A O   1 
ATOM   2701 C  CB  . GLU B 1 76  ? -24.056 -5.193  30.305  1.00 33.55 ? 76  GLU A CB  1 
ATOM   2702 C  CG  . GLU B 1 76  ? -25.287 -5.259  29.418  1.00 31.66 ? 76  GLU A CG  1 
ATOM   2703 C  CD  . GLU B 1 76  ? -26.543 -5.514  30.253  1.00 40.67 ? 76  GLU A CD  1 
ATOM   2704 O  OE1 . GLU B 1 76  ? -27.645 -5.742  29.678  1.00 51.36 ? 76  GLU A OE1 1 
ATOM   2705 O  OE2 . GLU B 1 76  ? -26.422 -5.530  31.496  1.00 44.06 ? 76  GLU A OE2 1 
ATOM   2706 N  N   . ASN B 1 77  ? -22.659 -7.409  29.169  1.00 21.21 ? 77  ASN A N   1 
ATOM   2707 C  CA  . ASN B 1 77  ? -22.194 -8.629  28.528  1.00 20.06 ? 77  ASN A CA  1 
ATOM   2708 C  C   . ASN B 1 77  ? -23.200 -9.249  27.621  1.00 18.77 ? 77  ASN A C   1 
ATOM   2709 O  O   . ASN B 1 77  ? -23.340 -10.489 27.657  1.00 24.03 ? 77  ASN A O   1 
ATOM   2710 C  CB  . ASN B 1 77  ? -21.822 -9.740  29.562  1.00 23.13 ? 77  ASN A CB  1 
ATOM   2711 C  CG  . ASN B 1 77  ? -20.471 -9.591  30.100  1.00 18.43 ? 77  ASN A CG  1 
ATOM   2712 O  OD1 . ASN B 1 77  ? -19.560 -9.038  29.480  1.00 16.39 ? 77  ASN A OD1 1 
ATOM   2713 N  ND2 . ASN B 1 77  ? -20.251 -10.228 31.261  1.00 21.07 ? 77  ASN A ND2 1 
ATOM   2714 N  N   . LYS B 1 78  ? -23.803 -8.467  26.725  1.00 16.12 ? 78  LYS A N   1 
ATOM   2715 C  CA  . LYS B 1 78  ? -24.677 -9.029  25.648  1.00 16.09 ? 78  LYS A CA  1 
ATOM   2716 C  C   . LYS B 1 78  ? -23.867 -9.801  24.556  1.00 16.18 ? 78  LYS A C   1 
ATOM   2717 O  O   . LYS B 1 78  ? -24.275 -10.883 24.079  1.00 16.05 ? 78  LYS A O   1 
ATOM   2718 C  CB  . LYS B 1 78  ? -25.501 -7.940  24.955  1.00 21.32 ? 78  LYS A CB  1 
ATOM   2719 C  CG  . LYS B 1 78  ? -26.641 -7.411  25.826  1.00 26.66 ? 78  LYS A CG  1 
ATOM   2720 C  CD  . LYS B 1 78  ? -27.629 -6.660  24.925  1.00 33.39 ? 78  LYS A CD  1 
ATOM   2721 C  CE  . LYS B 1 78  ? -28.928 -6.358  25.695  1.00 44.01 ? 78  LYS A CE  1 
ATOM   2722 N  NZ  . LYS B 1 78  ? -28.552 -5.653  26.957  1.00 45.85 ? 78  LYS A NZ  1 
ATOM   2723 N  N   . SER B 1 79  ? -22.676 -9.297  24.240  1.00 13.40 ? 79  SER A N   1 
ATOM   2724 C  CA  . SER B 1 79  ? -21.896 -9.883  23.123  1.00 13.02 ? 79  SER A CA  1 
ATOM   2725 C  C   . SER B 1 79  ? -20.513 -10.185 23.728  1.00 12.69 ? 79  SER A C   1 
ATOM   2726 O  O   . SER B 1 79  ? -19.780 -9.268  24.147  1.00 12.32 ? 79  SER A O   1 
ATOM   2727 C  CB  . SER B 1 79  ? -21.817 -8.850  22.021  1.00 12.73 ? 79  SER A CB  1 
ATOM   2728 O  OG  . SER B 1 79  ? -23.106 -8.634  21.398  1.00 13.65 ? 79  SER A OG  1 
ATOM   2729 N  N   . VAL B 1 80  ? -20.186 -11.500 23.797  1.00 12.61 ? 80  VAL A N   1 
ATOM   2730 C  CA  . VAL B 1 80  ? -18.948 -11.966 24.433  1.00 11.65 ? 80  VAL A CA  1 
ATOM   2731 C  C   . VAL B 1 80  ? -18.337 -13.103 23.653  1.00 12.08 ? 80  VAL A C   1 
ATOM   2732 O  O   . VAL B 1 80  ? -19.063 -13.955 22.978  1.00 13.27 ? 80  VAL A O   1 
ATOM   2733 C  CB  . VAL B 1 80  ? -19.179 -12.422 25.904  1.00 13.10 ? 80  VAL A CB  1 
ATOM   2734 C  CG1 . VAL B 1 80  ? -19.645 -11.256 26.794  1.00 15.06 ? 80  VAL A CG1 1 
ATOM   2735 C  CG2 . VAL B 1 80  ? -20.214 -13.514 25.966  1.00 16.00 ? 80  VAL A CG2 1 
ATOM   2736 N  N   . LEU B 1 81  ? -17.004 -13.211 23.826  1.00 11.42 ? 81  LEU A N   1 
ATOM   2737 C  CA  . LEU B 1 81  ? -16.257 -14.347 23.307  1.00 10.51 ? 81  LEU A CA  1 
ATOM   2738 C  C   . LEU B 1 81  ? -15.655 -15.058 24.469  1.00 11.99 ? 81  LEU A C   1 
ATOM   2739 O  O   . LEU B 1 81  ? -15.042 -14.407 25.313  1.00 12.53 ? 81  LEU A O   1 
ATOM   2740 C  CB  . LEU B 1 81  ? -15.055 -13.812 22.440  1.00 12.94 ? 81  LEU A CB  1 
ATOM   2741 C  CG  . LEU B 1 81  ? -14.078 -14.878 21.816  1.00 12.86 ? 81  LEU A CG  1 
ATOM   2742 C  CD1 . LEU B 1 81  ? -14.817 -15.765 20.833  1.00 13.21 ? 81  LEU A CD1 1 
ATOM   2743 C  CD2 . LEU B 1 81  ? -12.966 -14.075 21.074  1.00 14.18 ? 81  LEU A CD2 1 
ATOM   2744 N  N   . ARG B 1 82  ? -15.857 -16.381 24.467  1.00 12.27 ? 82  ARG A N   1 
ATOM   2745 C  CA  . ARG B 1 82  ? -15.252 -17.298 25.523  1.00 13.25 ? 82  ARG A CA  1 
ATOM   2746 C  C   . ARG B 1 82  ? -14.680 -18.506 24.846  1.00 12.68 ? 82  ARG A C   1 
ATOM   2747 O  O   . ARG B 1 82  ? -14.728 -18.643 23.622  1.00 13.77 ? 82  ARG A O   1 
ATOM   2748 C  CB  . ARG B 1 82  ? -16.375 -17.760 26.483  1.00 14.36 ? 82  ARG A CB  1 
ATOM   2749 C  CG  . ARG B 1 82  ? -16.813 -16.577 27.349  1.00 15.61 ? 82  ARG A CG  1 
ATOM   2750 C  CD  . ARG B 1 82  ? -18.088 -16.948 28.099  1.00 17.44 ? 82  ARG A CD  1 
ATOM   2751 N  NE  . ARG B 1 82  ? -19.194 -17.015 27.162  1.00 18.42 ? 82  ARG A NE  1 
ATOM   2752 C  CZ  . ARG B 1 82  ? -20.480 -17.188 27.501  1.00 26.86 ? 82  ARG A CZ  1 
ATOM   2753 N  NH1 . ARG B 1 82  ? -20.795 -17.238 28.803  1.00 27.29 ? 82  ARG A NH1 1 
ATOM   2754 N  NH2 . ARG B 1 82  ? -21.435 -17.276 26.568  1.00 24.18 ? 82  ARG A NH2 1 
ATOM   2755 N  N   . GLY B 1 83  ? -14.019 -19.368 25.635  1.00 12.78 ? 83  GLY A N   1 
ATOM   2756 C  CA  . GLY B 1 83  ? -13.412 -20.543 25.015  1.00 13.94 ? 83  GLY A CA  1 
ATOM   2757 C  C   . GLY B 1 83  ? -12.154 -20.226 24.251  1.00 12.93 ? 83  GLY A C   1 
ATOM   2758 O  O   . GLY B 1 83  ? -11.466 -19.270 24.612  1.00 14.68 ? 83  GLY A O   1 
ATOM   2759 N  N   . GLY B 1 84  ? -11.898 -21.038 23.205  1.00 16.52 ? 84  GLY A N   1 
ATOM   2760 C  CA  . GLY B 1 84  ? -10.594 -20.854 22.431  1.00 15.03 ? 84  GLY A CA  1 
ATOM   2761 C  C   . GLY B 1 84  ? -9.480  -20.991 23.496  1.00 15.29 ? 84  GLY A C   1 
ATOM   2762 O  O   . GLY B 1 84  ? -9.531  -21.869 24.384  1.00 16.14 ? 84  GLY A O   1 
ATOM   2763 N  N   . PRO B 1 85  ? -8.415  -20.153 23.413  1.00 14.52 ? 85  PRO A N   1 
ATOM   2764 C  CA  . PRO B 1 85  ? -7.350  -20.118 24.437  1.00 14.76 ? 85  PRO A CA  1 
ATOM   2765 C  C   . PRO B 1 85  ? -7.652  -19.279 25.676  1.00 12.43 ? 85  PRO A C   1 
ATOM   2766 O  O   . PRO B 1 85  ? -6.773  -19.063 26.572  1.00 16.10 ? 85  PRO A O   1 
ATOM   2767 C  CB  . PRO B 1 85  ? -6.194  -19.363 23.688  1.00 14.35 ? 85  PRO A CB  1 
ATOM   2768 C  CG  . PRO B 1 85  ? -7.010  -18.366 22.791  1.00 12.94 ? 85  PRO A CG  1 
ATOM   2769 C  CD  . PRO B 1 85  ? -8.249  -19.115 22.314  1.00 13.42 ? 85  PRO A CD  1 
ATOM   2770 N  N   . LEU B 1 86  ? -8.857  -18.695 25.750  1.00 13.09 ? 86  LEU A N   1 
ATOM   2771 C  CA  . LEU B 1 86  ? -9.147  -17.652 26.730  1.00 11.96 ? 86  LEU A CA  1 
ATOM   2772 C  C   . LEU B 1 86  ? -9.621  -18.193 28.107  1.00 13.09 ? 86  LEU A C   1 
ATOM   2773 O  O   . LEU B 1 86  ? -10.399 -19.124 28.147  1.00 15.70 ? 86  LEU A O   1 
ATOM   2774 C  CB  . LEU B 1 86  ? -10.274 -16.734 26.221  1.00 13.44 ? 86  LEU A CB  1 
ATOM   2775 C  CG  . LEU B 1 86  ? -9.966  -16.094 24.834  1.00 13.27 ? 86  LEU A CG  1 
ATOM   2776 C  CD1 . LEU B 1 86  ? -11.219 -15.391 24.326  1.00 12.69 ? 86  LEU A CD1 1 
ATOM   2777 C  CD2 . LEU B 1 86  ? -8.832  -15.100 24.983  1.00 13.84 ? 86  LEU A CD2 1 
ATOM   2778 N  N   . THR B 1 87  ? -9.124  -17.509 29.126  1.00 13.04 ? 87  THR A N   1 
ATOM   2779 C  CA  . THR B 1 87  ? -9.698  -17.682 30.512  1.00 15.78 ? 87  THR A CA  1 
ATOM   2780 C  C   . THR B 1 87  ? -10.699 -16.574 30.706  1.00 16.44 ? 87  THR A C   1 
ATOM   2781 O  O   . THR B 1 87  ? -10.328 -15.387 30.668  1.00 18.13 ? 87  THR A O   1 
ATOM   2782 C  CB  . THR B 1 87  ? -8.599  -17.565 31.538  1.00 17.38 ? 87  THR A CB  1 
ATOM   2783 O  OG1 . THR B 1 87  ? -7.706  -18.671 31.322  1.00 20.88 ? 87  THR A OG1 1 
ATOM   2784 C  CG2 . THR B 1 87  ? -9.206  -17.697 32.974  1.00 23.34 ? 87  THR A CG2 1 
ATOM   2785 N  N   . GLY B 1 88  ? -11.946 -16.950 31.030  1.00 15.80 ? 88  GLY A N   1 
ATOM   2786 C  CA  . GLY B 1 88  ? -12.958 -15.907 31.343  1.00 17.35 ? 88  GLY A CA  1 
ATOM   2787 C  C   . GLY B 1 88  ? -13.614 -15.311 30.064  1.00 15.09 ? 88  GLY A C   1 
ATOM   2788 O  O   . GLY B 1 88  ? -13.451 -15.870 28.990  1.00 16.19 ? 88  GLY A O   1 
ATOM   2789 N  N   . SER B 1 89  ? -14.334 -14.213 30.235  1.00 14.03 ? 89  SER A N   1 
ATOM   2790 C  CA  . SER B 1 89  ? -15.246 -13.685 29.212  1.00 13.62 ? 89  SER A CA  1 
ATOM   2791 C  C   . SER B 1 89  ? -14.720 -12.358 28.665  1.00 12.54 ? 89  SER A C   1 
ATOM   2792 O  O   . SER B 1 89  ? -14.376 -11.459 29.427  1.00 14.21 ? 89  SER A O   1 
ATOM   2793 C  CB  . SER B 1 89  ? -16.548 -13.333 29.948  1.00 14.81 ? 89  SER A CB  1 
ATOM   2794 O  OG  . SER B 1 89  ? -17.503 -13.048 28.967  1.00 15.06 ? 89  SER A OG  1 
ATOM   2795 N  N   . TYR B 1 90  ? -14.661 -12.280 27.318  1.00 11.59 ? 90  TYR A N   1 
ATOM   2796 C  CA  . TYR B 1 90  ? -14.099 -11.109 26.666  1.00 10.41 ? 90  TYR A CA  1 
ATOM   2797 C  C   . TYR B 1 90  ? -15.227 -10.409 25.912  1.00 10.54 ? 90  TYR A C   1 
ATOM   2798 O  O   . TYR B 1 90  ? -15.867 -11.029 25.055  1.00 13.23 ? 90  TYR A O   1 
ATOM   2799 C  CB  . TYR B 1 90  ? -12.957 -11.519 25.729  1.00 11.16 ? 90  TYR A CB  1 
ATOM   2800 C  CG  . TYR B 1 90  ? -11.638 -11.844 26.447  1.00 10.97 ? 90  TYR A CG  1 
ATOM   2801 C  CD1 . TYR B 1 90  ? -11.571 -12.981 27.309  1.00 12.66 ? 90  TYR A CD1 1 
ATOM   2802 C  CD2 . TYR B 1 90  ? -10.530 -11.006 26.310  1.00 10.79 ? 90  TYR A CD2 1 
ATOM   2803 C  CE1 . TYR B 1 90  ? -10.368 -13.286 27.981  1.00 11.72 ? 90  TYR A CE1 1 
ATOM   2804 C  CE2 . TYR B 1 90  ? -9.326  -11.317 26.967  1.00 12.01 ? 90  TYR A CE2 1 
ATOM   2805 C  CZ  . TYR B 1 90  ? -9.306  -12.450 27.826  1.00 11.51 ? 90  TYR A CZ  1 
ATOM   2806 O  OH  . TYR B 1 90  ? -8.122  -12.738 28.463  1.00 13.17 ? 90  TYR A OH  1 
ATOM   2807 N  N   . ARG B 1 91  ? -15.499 -9.162  26.284  1.00 10.63 ? 91  ARG A N   1 
ATOM   2808 C  CA  . ARG B 1 91  ? -16.601 -8.375  25.771  1.00 11.58 ? 91  ARG A CA  1 
ATOM   2809 C  C   . ARG B 1 91  ? -16.297 -7.743  24.407  1.00 10.34 ? 91  ARG A C   1 
ATOM   2810 O  O   . ARG B 1 91  ? -15.261 -7.116  24.233  1.00 10.80 ? 91  ARG A O   1 
ATOM   2811 C  CB  . ARG B 1 91  ? -16.998 -7.324  26.839  1.00 11.07 ? 91  ARG A CB  1 
ATOM   2812 C  CG  . ARG B 1 91  ? -18.304 -6.607  26.519  1.00 12.96 ? 91  ARG A CG  1 
ATOM   2813 C  CD  . ARG B 1 91  ? -18.588 -5.637  27.666  1.00 14.08 ? 91  ARG A CD  1 
ATOM   2814 N  NE  . ARG B 1 91  ? -18.736 -6.323  28.943  1.00 13.57 ? 91  ARG A NE  1 
ATOM   2815 C  CZ  . ARG B 1 91  ? -18.867 -5.699  30.108  1.00 15.67 ? 91  ARG A CZ  1 
ATOM   2816 N  NH1 . ARG B 1 91  ? -18.864 -4.373  30.157  1.00 15.32 ? 91  ARG A NH1 1 
ATOM   2817 N  NH2 . ARG B 1 91  ? -19.008 -6.400  31.223  1.00 14.11 ? 91  ARG A NH2 1 
ATOM   2818 N  N   . LEU B 1 92  ? -17.255 -7.890  23.487  1.00 9.78  ? 92  LEU A N   1 
ATOM   2819 C  CA  . LEU B 1 92  ? -17.116 -7.196  22.187  1.00 10.47 ? 92  LEU A CA  1 
ATOM   2820 C  C   . LEU B 1 92  ? -17.103 -5.700  22.244  1.00 11.82 ? 92  LEU A C   1 
ATOM   2821 O  O   . LEU B 1 92  ? -18.016 -5.101  22.856  1.00 13.47 ? 92  LEU A O   1 
ATOM   2822 C  CB  . LEU B 1 92  ? -18.283 -7.623  21.325  1.00 11.73 ? 92  LEU A CB  1 
ATOM   2823 C  CG  . LEU B 1 92  ? -18.305 -7.071  19.881  1.00 10.58 ? 92  LEU A CG  1 
ATOM   2824 C  CD1 . LEU B 1 92  ? -17.069 -7.475  19.081  1.00 13.14 ? 92  LEU A CD1 1 
ATOM   2825 C  CD2 . LEU B 1 92  ? -19.578 -7.566  19.232  1.00 11.42 ? 92  LEU A CD2 1 
ATOM   2826 N  N   . ARG B 1 93  ? -16.115 -5.093  21.582  1.00 11.64 ? 93  ARG A N   1 
ATOM   2827 C  CA  . ARG B 1 93  ? -15.957 -3.646  21.545  1.00 12.73 ? 93  ARG A CA  1 
ATOM   2828 C  C   . ARG B 1 93  ? -16.061 -3.046  20.158  1.00 13.72 ? 93  ARG A C   1 
ATOM   2829 O  O   . ARG B 1 93  ? -16.790 -2.099  20.010  1.00 14.47 ? 93  ARG A O   1 
ATOM   2830 C  CB  . ARG B 1 93  ? -14.633 -3.270  22.190  1.00 14.28 ? 93  ARG A CB  1 
ATOM   2831 C  CG  . ARG B 1 93  ? -14.243 -1.801  21.937  1.00 18.80 ? 93  ARG A CG  1 
ATOM   2832 C  CD  . ARG B 1 93  ? -14.438 -1.100  23.194  1.00 20.09 ? 93  ARG A CD  1 
ATOM   2833 N  NE  . ARG B 1 93  ? -13.859 0.251   23.107  1.00 24.19 ? 93  ARG A NE  1 
ATOM   2834 C  CZ  . ARG B 1 93  ? -14.186 1.213   23.971  1.00 24.16 ? 93  ARG A CZ  1 
ATOM   2835 N  NH1 . ARG B 1 93  ? -15.030 0.972   25.001  1.00 21.75 ? 93  ARG A NH1 1 
ATOM   2836 N  NH2 . ARG B 1 93  ? -13.690 2.418   23.757  1.00 22.98 ? 93  ARG A NH2 1 
ATOM   2837 N  N   . GLN B 1 94  ? -15.370 -3.620  19.169  1.00 12.07 ? 94  GLN A N   1 
ATOM   2838 C  CA  . GLN B 1 94  ? -15.232 -2.853  17.925  1.00 12.61 ? 94  GLN A CA  1 
ATOM   2839 C  C   . GLN B 1 94  ? -14.877 -3.866  16.855  1.00 12.24 ? 94  GLN A C   1 
ATOM   2840 O  O   . GLN B 1 94  ? -14.239 -4.905  17.099  1.00 11.74 ? 94  GLN A O   1 
ATOM   2841 C  CB  . GLN B 1 94  ? -14.007 -1.901  18.167  1.00 16.01 ? 94  GLN A CB  1 
ATOM   2842 C  CG  . GLN B 1 94  ? -13.738 -0.883  17.127  1.00 24.33 ? 94  GLN A CG  1 
ATOM   2843 C  CD  . GLN B 1 94  ? -12.480 -1.294  16.479  1.00 23.61 ? 94  GLN A CD  1 
ATOM   2844 O  OE1 . GLN B 1 94  ? -12.309 -2.474  16.139  1.00 20.75 ? 94  GLN A OE1 1 
ATOM   2845 N  NE2 . GLN B 1 94  ? -11.674 -0.383  16.214  1.00 28.89 ? 94  GLN A NE2 1 
ATOM   2846 N  N   . VAL B 1 95  ? -15.220 -3.540  15.605  1.00 11.83 ? 95  VAL A N   1 
ATOM   2847 C  CA  . VAL B 1 95  ? -14.796 -4.385  14.446  1.00 12.54 ? 95  VAL A CA  1 
ATOM   2848 C  C   . VAL B 1 95  ? -14.174 -3.369  13.444  1.00 12.89 ? 95  VAL A C   1 
ATOM   2849 O  O   . VAL B 1 95  ? -14.708 -2.276  13.262  1.00 12.38 ? 95  VAL A O   1 
ATOM   2850 C  CB  . VAL B 1 95  ? -15.971 -5.018  13.792  1.00 10.86 ? 95  VAL A CB  1 
ATOM   2851 C  CG1 . VAL B 1 95  ? -15.696 -5.593  12.368  1.00 13.52 ? 95  VAL A CG1 1 
ATOM   2852 C  CG2 . VAL B 1 95  ? -16.491 -6.192  14.734  1.00 10.56 ? 95  VAL A CG2 1 
ATOM   2853 N  N   . HIS B 1 96  ? -13.139 -3.816  12.757  1.00 10.84 ? 96  HIS A N   1 
ATOM   2854 C  CA  . HIS B 1 96  ? -12.571 -3.002  11.664  1.00 10.38 ? 96  HIS A CA  1 
ATOM   2855 C  C   . HIS B 1 96  ? -11.917 -3.934  10.658  1.00 10.60 ? 96  HIS A C   1 
ATOM   2856 O  O   . HIS B 1 96  ? -11.920 -5.131  10.818  1.00 11.08 ? 96  HIS A O   1 
ATOM   2857 C  CB  . HIS B 1 96  ? -11.587 -1.980  12.251  1.00 10.66 ? 96  HIS A CB  1 
ATOM   2858 C  CG  . HIS B 1 96  ? -10.410 -2.612  12.895  1.00 10.78 ? 96  HIS A CG  1 
ATOM   2859 N  ND1 . HIS B 1 96  ? -10.406 -2.919  14.245  1.00 10.38 ? 96  HIS A ND1 1 
ATOM   2860 C  CD2 . HIS B 1 96  ? -9.236  -3.042  12.374  1.00 10.10 ? 96  HIS A CD2 1 
ATOM   2861 C  CE1 . HIS B 1 96  ? -9.251  -3.595  14.531  1.00 11.56 ? 96  HIS A CE1 1 
ATOM   2862 N  NE2 . HIS B 1 96  ? -8.463  -3.645  13.411  1.00 11.80 ? 96  HIS A NE2 1 
ATOM   2863 N  N   . LEU B 1 97  ? -11.337 -3.382  9.580   1.00 9.99  ? 97  LEU A N   1 
ATOM   2864 C  CA  . LEU B 1 97  ? -10.862 -4.151  8.450   1.00 10.40 ? 97  LEU A CA  1 
ATOM   2865 C  C   . LEU B 1 97  ? -9.482  -3.630  8.039   1.00 10.25 ? 97  LEU A C   1 
ATOM   2866 O  O   . LEU B 1 97  ? -9.278  -2.418  8.046   1.00 11.68 ? 97  LEU A O   1 
ATOM   2867 C  CB  . LEU B 1 97  ? -11.912 -3.991  7.283   1.00 12.26 ? 97  LEU A CB  1 
ATOM   2868 C  CG  . LEU B 1 97  ? -11.596 -4.893  6.082   1.00 11.65 ? 97  LEU A CG  1 
ATOM   2869 C  CD1 . LEU B 1 97  ? -11.875 -6.391  6.420   1.00 12.13 ? 97  LEU A CD1 1 
ATOM   2870 C  CD2 . LEU B 1 97  ? -12.626 -4.427  5.043   1.00 14.00 ? 97  LEU A CD2 1 
ATOM   2871 N  N   . HIS B 1 98  ? -8.605  -4.513  7.583   1.00 9.14  ? 98  HIS A N   1 
ATOM   2872 C  CA  . HIS B 1 98  ? -7.381  -4.097  6.928   1.00 10.53 ? 98  HIS A CA  1 
ATOM   2873 C  C   . HIS B 1 98  ? -7.377  -4.617  5.471   1.00 11.38 ? 98  HIS A C   1 
ATOM   2874 O  O   . HIS B 1 98  ? -7.873  -5.704  5.203   1.00 10.87 ? 98  HIS A O   1 
ATOM   2875 C  CB  . HIS B 1 98  ? -6.157  -4.721  7.629   1.00 10.69 ? 98  HIS A CB  1 
ATOM   2876 C  CG  . HIS B 1 98  ? -6.048  -4.272  9.088   1.00 10.66 ? 98  HIS A CG  1 
ATOM   2877 N  ND1 . HIS B 1 98  ? -5.434  -3.134  9.438   1.00 11.96 ? 98  HIS A ND1 1 
ATOM   2878 C  CD2 . HIS B 1 98  ? -6.575  -4.806  10.277  1.00 12.26 ? 98  HIS A CD2 1 
ATOM   2879 C  CE1 . HIS B 1 98  ? -5.513  -2.956  10.774  1.00 11.68 ? 98  HIS A CE1 1 
ATOM   2880 N  NE2 . HIS B 1 98  ? -6.213  -3.984  11.288  1.00 9.02  ? 98  HIS A NE2 1 
ATOM   2881 N  N   . TRP B 1 99  ? -6.778  -3.852  4.544   1.00 11.08 ? 99  TRP A N   1 
ATOM   2882 C  CA  . TRP B 1 99  ? -6.735  -4.278  3.130   1.00 11.32 ? 99  TRP A CA  1 
ATOM   2883 C  C   . TRP B 1 99  ? -5.435  -3.678  2.586   1.00 11.15 ? 99  TRP A C   1 
ATOM   2884 O  O   . TRP B 1 99  ? -4.599  -3.040  3.282   1.00 12.25 ? 99  TRP A O   1 
ATOM   2885 C  CB  . TRP B 1 99  ? -7.983  -3.735  2.407   1.00 11.93 ? 99  TRP A CB  1 
ATOM   2886 C  CG  . TRP B 1 99  ? -8.158  -2.243  2.480   1.00 11.22 ? 99  TRP A CG  1 
ATOM   2887 C  CD1 . TRP B 1 99  ? -7.546  -1.246  1.681   1.00 11.86 ? 99  TRP A CD1 1 
ATOM   2888 C  CD2 . TRP B 1 99  ? -8.961  -1.498  3.446   1.00 12.64 ? 99  TRP A CD2 1 
ATOM   2889 N  NE1 . TRP B 1 99  ? -7.898  0.010   2.098   1.00 11.30 ? 99  TRP A NE1 1 
ATOM   2890 C  CE2 . TRP B 1 99  ? -8.775  -0.089  3.188   1.00 12.70 ? 99  TRP A CE2 1 
ATOM   2891 C  CE3 . TRP B 1 99  ? -9.779  -1.889  4.516   1.00 12.68 ? 99  TRP A CE3 1 
ATOM   2892 C  CZ2 . TRP B 1 99  ? -9.415  0.915   3.932   1.00 12.69 ? 99  TRP A CZ2 1 
ATOM   2893 C  CZ3 . TRP B 1 99  ? -10.413 -0.891  5.284   1.00 12.60 ? 99  TRP A CZ3 1 
ATOM   2894 C  CH2 . TRP B 1 99  ? -10.292 0.470   5.001   1.00 12.19 ? 99  TRP A CH2 1 
ATOM   2895 N  N   . GLY B 1 100 ? -5.273  -3.901  1.288   1.00 12.21 ? 100 GLY A N   1 
ATOM   2896 C  CA  . GLY B 1 100 ? -4.082  -3.457  0.557   1.00 12.93 ? 100 GLY A CA  1 
ATOM   2897 C  C   . GLY B 1 100 ? -4.561  -2.770  -0.732  1.00 11.50 ? 100 GLY A C   1 
ATOM   2898 O  O   . GLY B 1 100 ? -5.731  -2.706  -0.987  1.00 12.79 ? 100 GLY A O   1 
ATOM   2899 N  N   . SER B 1 101 ? -3.600  -2.202  -1.476  1.00 13.14 ? 101 SER A N   1 
ATOM   2900 C  CA  . SER B 1 101 ? -4.028  -1.560  -2.771  1.00 13.97 ? 101 SER A CA  1 
ATOM   2901 C  C   . SER B 1 101 ? -4.388  -2.566  -3.826  1.00 15.37 ? 101 SER A C   1 
ATOM   2902 O  O   . SER B 1 101 ? -5.051  -2.187  -4.825  1.00 15.60 ? 101 SER A O   1 
ATOM   2903 C  CB  . SER B 1 101 ? -2.957  -0.571  -3.204  1.00 14.31 ? 101 SER A CB  1 
ATOM   2904 O  OG  . SER B 1 101 ? -1.829  -1.251  -3.753  1.00 17.71 ? 101 SER A OG  1 
ATOM   2905 N  N   . ALA B 1 102 ? -4.000  -3.804  -3.648  1.00 14.93 ? 102 ALA A N   1 
ATOM   2906 C  CA  . ALA B 1 102 ? -4.306  -4.846  -4.557  1.00 16.37 ? 102 ALA A CA  1 
ATOM   2907 C  C   . ALA B 1 102 ? -4.967  -6.007  -3.878  1.00 16.40 ? 102 ALA A C   1 
ATOM   2908 O  O   . ALA B 1 102 ? -4.571  -6.334  -2.736  1.00 15.98 ? 102 ALA A O   1 
ATOM   2909 C  CB  . ALA B 1 102 ? -2.984  -5.356  -5.137  1.00 19.94 ? 102 ALA A CB  1 
ATOM   2910 N  N   . ASP B 1 103 ? -5.837  -6.691  -4.586  1.00 14.38 ? 103 ASP A N   1 
ATOM   2911 C  CA  . ASP B 1 103 ? -6.510  -7.919  -4.012  1.00 17.04 ? 103 ASP A CA  1 
ATOM   2912 C  C   . ASP B 1 103 ? -5.480  -8.973  -3.663  1.00 22.06 ? 103 ASP A C   1 
ATOM   2913 O  O   . ASP B 1 103 ? -5.773  -9.816  -2.822  1.00 26.21 ? 103 ASP A O   1 
ATOM   2914 C  CB  . ASP B 1 103 ? -7.612  -8.489  -4.928  1.00 17.85 ? 103 ASP A CB  1 
ATOM   2915 C  CG  . ASP B 1 103 ? -8.751  -7.520  -5.140  1.00 18.23 ? 103 ASP A CG  1 
ATOM   2916 O  OD1 . ASP B 1 103 ? -8.854  -6.440  -4.509  1.00 20.22 ? 103 ASP A OD1 1 
ATOM   2917 O  OD2 . ASP B 1 103 ? -9.571  -7.857  -6.052  1.00 24.81 ? 103 ASP A OD2 1 
ATOM   2918 N  N   . ASP B 1 104 ? -4.302  -8.909  -4.319  1.00 20.25 ? 104 ASP A N   1 
ATOM   2919 C  CA  . ASP B 1 104 ? -3.205  -9.820  -4.139  1.00 26.94 ? 104 ASP A CA  1 
ATOM   2920 C  C   . ASP B 1 104 ? -2.649  -9.907  -2.717  1.00 23.18 ? 104 ASP A C   1 
ATOM   2921 O  O   . ASP B 1 104 ? -2.041  -10.925 -2.309  1.00 22.71 ? 104 ASP A O   1 
ATOM   2922 C  CB  . ASP B 1 104 ? -2.006  -9.558  -5.104  1.00 26.81 ? 104 ASP A CB  1 
ATOM   2923 C  CG  . ASP B 1 104 ? -2.395  -8.727  -6.310  1.00 37.77 ? 104 ASP A CG  1 
ATOM   2924 O  OD1 . ASP B 1 104 ? -3.598  -8.694  -6.650  1.00 35.79 ? 104 ASP A OD1 1 
ATOM   2925 O  OD2 . ASP B 1 104 ? -1.499  -8.108  -6.922  1.00 36.29 ? 104 ASP A OD2 1 
ATOM   2926 N  N   . HIS B 1 105 ? -2.809  -8.820  -1.941  1.00 20.72 ? 105 HIS A N   1 
ATOM   2927 C  CA  . HIS B 1 105 ? -1.931  -8.652  -0.813  1.00 19.87 ? 105 HIS A CA  1 
ATOM   2928 C  C   . HIS B 1 105 ? -2.527  -7.634  0.133   1.00 16.97 ? 105 HIS A C   1 
ATOM   2929 O  O   . HIS B 1 105 ? -2.162  -6.446  0.116   1.00 20.07 ? 105 HIS A O   1 
ATOM   2930 C  CB  . HIS B 1 105 ? -0.585  -8.103  -1.384  1.00 25.07 ? 105 HIS A CB  1 
ATOM   2931 C  CG  . HIS B 1 105 ? 0.587   -8.269  -0.495  1.00 32.63 ? 105 HIS A CG  1 
ATOM   2932 N  ND1 . HIS B 1 105 ? 1.061   -7.252  0.274   1.00 37.64 ? 105 HIS A ND1 1 
ATOM   2933 C  CD2 . HIS B 1 105 ? 1.435   -9.367  -0.271  1.00 35.90 ? 105 HIS A CD2 1 
ATOM   2934 C  CE1 . HIS B 1 105 ? 2.145   -7.675  0.968   1.00 36.91 ? 105 HIS A CE1 1 
ATOM   2935 N  NE2 . HIS B 1 105 ? 2.370   -8.970  0.643   1.00 36.34 ? 105 HIS A NE2 1 
ATOM   2936 N  N   . GLY B 1 106 ? -3.496  -8.051  0.946   1.00 15.21 ? 106 GLY A N   1 
ATOM   2937 C  CA  . GLY B 1 106 ? -4.202  -7.118  1.800   1.00 14.06 ? 106 GLY A CA  1 
ATOM   2938 C  C   . GLY B 1 106 ? -4.271  -7.473  3.305   1.00 13.07 ? 106 GLY A C   1 
ATOM   2939 O  O   . GLY B 1 106 ? -4.592  -6.605  4.147   1.00 16.71 ? 106 GLY A O   1 
ATOM   2940 N  N   . SER B 1 107 ? -4.056  -8.722  3.637   1.00 12.89 ? 107 SER A N   1 
ATOM   2941 C  CA  . SER B 1 107 ? -4.220  -9.182  5.033   1.00 12.08 ? 107 SER A CA  1 
ATOM   2942 C  C   . SER B 1 107 ? -2.979  -8.815  5.818   1.00 11.99 ? 107 SER A C   1 
ATOM   2943 O  O   . SER B 1 107 ? -1.907  -8.391  5.284   1.00 13.69 ? 107 SER A O   1 
ATOM   2944 C  CB  . SER B 1 107 ? -4.530  -10.651 5.072   1.00 11.74 ? 107 SER A CB  1 
ATOM   2945 O  OG  . SER B 1 107 ? -3.402  -11.453 4.633   1.00 12.50 ? 107 SER A OG  1 
ATOM   2946 N  N   . GLU B 1 108 ? -3.150  -8.866  7.160   1.00 10.92 ? 108 GLU A N   1 
ATOM   2947 C  CA  . GLU B 1 108 ? -1.999  -8.657  8.087   1.00 12.11 ? 108 GLU A CA  1 
ATOM   2948 C  C   . GLU B 1 108 ? -1.296  -9.968  8.409   1.00 12.53 ? 108 GLU A C   1 
ATOM   2949 O  O   . GLU B 1 108 ? -0.081  -10.068 8.208   1.00 12.74 ? 108 GLU A O   1 
ATOM   2950 C  CB  . GLU B 1 108 ? -2.592  -8.015  9.383   1.00 11.80 ? 108 GLU A CB  1 
ATOM   2951 C  CG  . GLU B 1 108 ? -3.062  -6.596  9.069   1.00 13.77 ? 108 GLU A CG  1 
ATOM   2952 C  CD  . GLU B 1 108 ? -2.950  -5.597  10.159  1.00 14.25 ? 108 GLU A CD  1 
ATOM   2953 O  OE1 . GLU B 1 108 ? -3.447  -5.850  11.269  1.00 12.60 ? 108 GLU A OE1 1 
ATOM   2954 O  OE2 . GLU B 1 108 ? -2.436  -4.531  9.936   1.00 13.14 ? 108 GLU A OE2 1 
ATOM   2955 N  N   . HIS B 1 109 ? -1.984  -10.960 8.946   1.00 11.67 ? 109 HIS A N   1 
ATOM   2956 C  CA  . HIS B 1 109 ? -1.429  -12.295 9.043   1.00 13.08 ? 109 HIS A CA  1 
ATOM   2957 C  C   . HIS B 1 109 ? -1.310  -12.934 7.667   1.00 13.01 ? 109 HIS A C   1 
ATOM   2958 O  O   . HIS B 1 109 ? -2.105  -12.643 6.791   1.00 12.88 ? 109 HIS A O   1 
ATOM   2959 C  CB  . HIS B 1 109 ? -2.327  -13.151 9.973   1.00 11.38 ? 109 HIS A CB  1 
ATOM   2960 C  CG  . HIS B 1 109 ? -2.342  -12.626 11.408  1.00 10.76 ? 109 HIS A CG  1 
ATOM   2961 N  ND1 . HIS B 1 109 ? -3.257  -11.748 11.886  1.00 10.34 ? 109 HIS A ND1 1 
ATOM   2962 C  CD2 . HIS B 1 109 ? -1.430  -12.843 12.421  1.00 10.58 ? 109 HIS A CD2 1 
ATOM   2963 C  CE1 . HIS B 1 109 ? -2.891  -11.411 13.151  1.00 11.22 ? 109 HIS A CE1 1 
ATOM   2964 N  NE2 . HIS B 1 109 ? -1.790  -12.104 13.463  1.00 11.25 ? 109 HIS A NE2 1 
ATOM   2965 N  N   . ILE B 1 110 ? -0.277  -13.766 7.480   1.00 13.30 ? 110 ILE A N   1 
ATOM   2966 C  CA  . ILE B 1 110 ? 0.069   -14.401 6.201   1.00 15.08 ? 110 ILE A CA  1 
ATOM   2967 C  C   . ILE B 1 110 ? 0.197   -15.886 6.538   1.00 16.26 ? 110 ILE A C   1 
ATOM   2968 O  O   . ILE B 1 110 ? 0.812   -16.181 7.614   1.00 17.59 ? 110 ILE A O   1 
ATOM   2969 C  CB  . ILE B 1 110 ? 1.439   -13.879 5.717   1.00 17.25 ? 110 ILE A CB  1 
ATOM   2970 C  CG1 . ILE B 1 110 ? 1.521   -12.353 5.827   1.00 23.00 ? 110 ILE A CG1 1 
ATOM   2971 C  CG2 . ILE B 1 110 ? 1.725   -14.404 4.241   1.00 15.52 ? 110 ILE A CG2 1 
ATOM   2972 C  CD1 . ILE B 1 110 ? 0.665   -11.557 4.916   1.00 23.74 ? 110 ILE A CD1 1 
ATOM   2973 N  N   . VAL B 1 111 ? -0.363  -16.773 5.713   1.00 15.55 ? 111 VAL A N   1 
ATOM   2974 C  CA  . VAL B 1 111 ? -0.425  -18.165 6.060   1.00 14.57 ? 111 VAL A CA  1 
ATOM   2975 C  C   . VAL B 1 111 ? 0.396   -18.937 4.986   1.00 17.69 ? 111 VAL A C   1 
ATOM   2976 O  O   . VAL B 1 111 ? -0.038  -19.069 3.831   1.00 17.96 ? 111 VAL A O   1 
ATOM   2977 C  CB  . VAL B 1 111 ? -1.880  -18.741 6.068   1.00 16.42 ? 111 VAL A CB  1 
ATOM   2978 C  CG1 . VAL B 1 111 ? -1.765  -20.207 6.423   1.00 16.57 ? 111 VAL A CG1 1 
ATOM   2979 C  CG2 . VAL B 1 111 ? -2.732  -18.042 7.141   1.00 17.37 ? 111 VAL A CG2 1 
ATOM   2980 N  N   . ASP B 1 112 ? 1.576   -19.414 5.389   1.00 17.21 ? 112 ASP A N   1 
ATOM   2981 C  CA  . ASP B 1 112 ? 2.507   -20.041 4.438   1.00 15.87 ? 112 ASP A CA  1 
ATOM   2982 C  C   . ASP B 1 112 ? 2.669   -19.195 3.200   1.00 17.42 ? 112 ASP A C   1 
ATOM   2983 O  O   . ASP B 1 112 ? 2.680   -19.707 2.029   1.00 19.03 ? 112 ASP A O   1 
ATOM   2984 C  CB  . ASP B 1 112 ? 1.970   -21.453 4.102   1.00 19.60 ? 112 ASP A CB  1 
ATOM   2985 C  CG  . ASP B 1 112 ? 2.104   -22.392 5.280   1.00 21.56 ? 112 ASP A CG  1 
ATOM   2986 O  OD1 . ASP B 1 112 ? 3.187   -22.385 5.898   1.00 23.99 ? 112 ASP A OD1 1 
ATOM   2987 O  OD2 . ASP B 1 112 ? 1.166   -23.188 5.476   1.00 27.43 ? 112 ASP A OD2 1 
ATOM   2988 N  N   . GLY B 1 113 ? 2.909   -17.909 3.424   1.00 13.56 ? 113 GLY A N   1 
ATOM   2989 C  CA  . GLY B 1 113 ? 3.182   -17.024 2.302   1.00 15.53 ? 113 GLY A CA  1 
ATOM   2990 C  C   . GLY B 1 113 ? 1.958   -16.478 1.598   1.00 15.13 ? 113 GLY A C   1 
ATOM   2991 O  O   . GLY B 1 113 ? 2.101   -15.570 0.756   1.00 16.40 ? 113 GLY A O   1 
ATOM   2992 N  N   . VAL B 1 114 ? 0.763   -16.990 1.927   1.00 15.52 ? 114 VAL A N   1 
ATOM   2993 C  CA  . VAL B 1 114 ? -0.454  -16.474 1.300   1.00 19.24 ? 114 VAL A CA  1 
ATOM   2994 C  C   . VAL B 1 114 ? -0.963  -15.254 2.077   1.00 18.60 ? 114 VAL A C   1 
ATOM   2995 O  O   . VAL B 1 114 ? -1.278  -15.370 3.266   1.00 17.29 ? 114 VAL A O   1 
ATOM   2996 C  CB  . VAL B 1 114 ? -1.528  -17.568 1.216   1.00 19.53 ? 114 VAL A CB  1 
ATOM   2997 C  CG1 . VAL B 1 114 ? -2.863  -16.941 0.729   1.00 20.71 ? 114 VAL A CG1 1 
ATOM   2998 C  CG2 . VAL B 1 114 ? -1.046  -18.667 0.263   1.00 20.05 ? 114 VAL A CG2 1 
ATOM   2999 N  N   A SER B 1 115 ? -0.951  -14.101 1.422   0.50 18.75 ? 115 SER A N   1 
ATOM   3000 N  N   B SER B 1 115 ? -0.988  -14.083 1.425   0.50 18.12 ? 115 SER A N   1 
ATOM   3001 C  CA  A SER B 1 115 ? -1.750  -12.986 1.865   0.50 16.91 ? 115 SER A CA  1 
ATOM   3002 C  CA  B SER B 1 115 ? -1.663  -12.863 1.930   0.50 15.78 ? 115 SER A CA  1 
ATOM   3003 C  C   A SER B 1 115 ? -3.155  -13.183 1.322   0.50 15.83 ? 115 SER A C   1 
ATOM   3004 C  C   B SER B 1 115 ? -3.041  -12.724 1.276   0.50 14.99 ? 115 SER A C   1 
ATOM   3005 O  O   A SER B 1 115 ? -3.389  -13.710 0.196   0.50 14.07 ? 115 SER A O   1 
ATOM   3006 O  O   B SER B 1 115 ? -3.126  -12.675 0.025   0.50 13.10 ? 115 SER A O   1 
ATOM   3007 C  CB  A SER B 1 115 ? -1.169  -11.691 1.351   0.50 18.11 ? 115 SER A CB  1 
ATOM   3008 C  CB  B SER B 1 115 ? -0.823  -11.639 1.625   0.50 16.37 ? 115 SER A CB  1 
ATOM   3009 O  OG  A SER B 1 115 ? 0.035   -11.372 2.013   0.50 17.29 ? 115 SER A OG  1 
ATOM   3010 O  OG  B SER B 1 115 ? -1.554  -10.429 1.840   0.50 14.73 ? 115 SER A OG  1 
ATOM   3011 N  N   . TYR B 1 116 ? -4.133  -12.713 2.100   1.00 13.09 ? 116 TYR A N   1 
ATOM   3012 C  CA  . TYR B 1 116 ? -5.482  -12.681 1.613   1.00 14.08 ? 116 TYR A CA  1 
ATOM   3013 C  C   . TYR B 1 116 ? -5.860  -11.299 1.174   1.00 10.88 ? 116 TYR A C   1 
ATOM   3014 O  O   . TYR B 1 116 ? -5.095  -10.341 1.350   1.00 14.73 ? 116 TYR A O   1 
ATOM   3015 C  CB  . TYR B 1 116 ? -6.420  -13.228 2.742   1.00 12.62 ? 116 TYR A CB  1 
ATOM   3016 C  CG  . TYR B 1 116 ? -6.223  -14.677 2.943   1.00 14.60 ? 116 TYR A CG  1 
ATOM   3017 C  CD1 . TYR B 1 116 ? -6.939  -15.648 2.210   1.00 16.77 ? 116 TYR A CD1 1 
ATOM   3018 C  CD2 . TYR B 1 116 ? -5.287  -15.107 3.888   1.00 15.23 ? 116 TYR A CD2 1 
ATOM   3019 C  CE1 . TYR B 1 116 ? -6.666  -16.997 2.413   1.00 18.04 ? 116 TYR A CE1 1 
ATOM   3020 C  CE2 . TYR B 1 116 ? -5.034  -16.415 4.097   1.00 16.42 ? 116 TYR A CE2 1 
ATOM   3021 C  CZ  . TYR B 1 116 ? -5.757  -17.350 3.370   1.00 21.23 ? 116 TYR A CZ  1 
ATOM   3022 O  OH  . TYR B 1 116 ? -5.606  -18.716 3.507   1.00 24.65 ? 116 TYR A OH  1 
ATOM   3023 N  N   . ALA B 1 117 ? -7.068  -11.135 0.597   1.00 12.17 ? 117 ALA A N   1 
ATOM   3024 C  CA  . ALA B 1 117 ? -7.446  -9.824  0.085   1.00 12.90 ? 117 ALA A CA  1 
ATOM   3025 C  C   . ALA B 1 117 ? -7.668  -8.773  1.205   1.00 13.79 ? 117 ALA A C   1 
ATOM   3026 O  O   . ALA B 1 117 ? -7.427  -7.627  1.027   1.00 12.61 ? 117 ALA A O   1 
ATOM   3027 C  CB  . ALA B 1 117 ? -8.709  -9.942  -0.799  1.00 14.76 ? 117 ALA A CB  1 
ATOM   3028 N  N   . ALA B 1 118 ? -8.092  -9.261  2.384   1.00 11.19 ? 118 ALA A N   1 
ATOM   3029 C  CA  . ALA B 1 118 ? -8.313  -8.293  3.457   1.00 11.11 ? 118 ALA A CA  1 
ATOM   3030 C  C   . ALA B 1 118 ? -8.406  -9.127  4.740   1.00 10.51 ? 118 ALA A C   1 
ATOM   3031 O  O   . ALA B 1 118 ? -8.396  -10.376 4.687   1.00 9.85  ? 118 ALA A O   1 
ATOM   3032 C  CB  . ALA B 1 118 ? -9.608  -7.504  3.243   1.00 12.14 ? 118 ALA A CB  1 
ATOM   3033 N  N   . GLU B 1 119 ? -8.476  -8.423  5.888   1.00 9.75  ? 119 GLU A N   1 
ATOM   3034 C  CA  . GLU B 1 119 ? -8.551  -9.210  7.147   1.00 9.20  ? 119 GLU A CA  1 
ATOM   3035 C  C   . GLU B 1 119 ? -9.434  -8.355  8.095   1.00 10.22 ? 119 GLU A C   1 
ATOM   3036 O  O   . GLU B 1 119 ? -9.104  -7.207  8.405   1.00 10.27 ? 119 GLU A O   1 
ATOM   3037 C  CB  . GLU B 1 119 ? -7.132  -9.380  7.744   1.00 10.10 ? 119 GLU A CB  1 
ATOM   3038 C  CG  . GLU B 1 119 ? -7.133  -10.247 9.015   1.00 9.29  ? 119 GLU A CG  1 
ATOM   3039 C  CD  . GLU B 1 119 ? -5.693  -10.545 9.462   1.00 12.03 ? 119 GLU A CD  1 
ATOM   3040 O  OE1 . GLU B 1 119 ? -4.798  -10.687 8.621   1.00 10.71 ? 119 GLU A OE1 1 
ATOM   3041 O  OE2 . GLU B 1 119 ? -5.506  -10.711 10.709  1.00 12.44 ? 119 GLU A OE2 1 
ATOM   3042 N  N   . LEU B 1 120 ? -10.424 -9.028  8.645   1.00 9.46  ? 120 LEU A N   1 
ATOM   3043 C  CA  . LEU B 1 120 ? -11.356 -8.374  9.560   1.00 9.89  ? 120 LEU A CA  1 
ATOM   3044 C  C   . LEU B 1 120 ? -10.870 -8.701  11.015  1.00 9.99  ? 120 LEU A C   1 
ATOM   3045 O  O   . LEU B 1 120 ? -10.489 -9.858  11.295  1.00 10.08 ? 120 LEU A O   1 
ATOM   3046 C  CB  . LEU B 1 120 ? -12.720 -9.009  9.384   1.00 11.21 ? 120 LEU A CB  1 
ATOM   3047 C  CG  . LEU B 1 120 ? -13.866 -8.338  10.173  1.00 11.80 ? 120 LEU A CG  1 
ATOM   3048 C  CD1 . LEU B 1 120 ? -14.305 -7.125  9.403   1.00 13.12 ? 120 LEU A CD1 1 
ATOM   3049 C  CD2 . LEU B 1 120 ? -15.031 -9.284  10.349  1.00 17.17 ? 120 LEU A CD2 1 
ATOM   3050 N  N   . HIS B 1 121 ? -10.907 -7.687  11.849  1.00 9.76  ? 121 HIS A N   1 
ATOM   3051 C  CA  . HIS B 1 121 ? -10.584 -7.844  13.305  1.00 10.16 ? 121 HIS A CA  1 
ATOM   3052 C  C   . HIS B 1 121 ? -11.733 -7.495  14.140  1.00 10.63 ? 121 HIS A C   1 
ATOM   3053 O  O   . HIS B 1 121 ? -12.317 -6.448  14.032  1.00 11.83 ? 121 HIS A O   1 
ATOM   3054 C  CB  . HIS B 1 121 ? -9.385  -6.904  13.645  1.00 9.79  ? 121 HIS A CB  1 
ATOM   3055 C  CG  . HIS B 1 121 ? -8.091  -7.389  12.988  1.00 9.51  ? 121 HIS A CG  1 
ATOM   3056 N  ND1 . HIS B 1 121 ? -6.978  -6.590  12.821  1.00 10.70 ? 121 HIS A ND1 1 
ATOM   3057 C  CD2 . HIS B 1 121 ? -7.774  -8.641  12.448  1.00 11.01 ? 121 HIS A CD2 1 
ATOM   3058 C  CE1 . HIS B 1 121 ? -6.008  -7.374  12.222  1.00 9.60  ? 121 HIS A CE1 1 
ATOM   3059 N  NE2 . HIS B 1 121 ? -6.485  -8.578  12.019  1.00 10.84 ? 121 HIS A NE2 1 
ATOM   3060 N  N   . VAL B 1 122 ? -12.014 -8.429  15.077  1.00 9.66  ? 122 VAL A N   1 
ATOM   3061 C  CA  . VAL B 1 122 ? -13.094 -8.244  16.038  1.00 9.43  ? 122 VAL A CA  1 
ATOM   3062 C  C   . VAL B 1 122 ? -12.401 -8.133  17.427  1.00 11.60 ? 122 VAL A C   1 
ATOM   3063 O  O   . VAL B 1 122 ? -11.759 -9.091  17.906  1.00 10.74 ? 122 VAL A O   1 
ATOM   3064 C  CB  . VAL B 1 122 ? -13.985 -9.468  16.075  1.00 10.36 ? 122 VAL A CB  1 
ATOM   3065 C  CG1 . VAL B 1 122 ? -15.202 -9.147  16.982  1.00 11.84 ? 122 VAL A CG1 1 
ATOM   3066 C  CG2 . VAL B 1 122 ? -14.475 -9.834  14.626  1.00 13.39 ? 122 VAL A CG2 1 
ATOM   3067 N  N   . VAL B 1 123 ? -12.579 -6.959  18.043  1.00 8.43  ? 123 VAL A N   1 
ATOM   3068 C  CA  . VAL B 1 123 ? -11.764 -6.636  19.254  1.00 9.23  ? 123 VAL A CA  1 
ATOM   3069 C  C   . VAL B 1 123 ? -12.596 -6.786  20.529  1.00 8.82  ? 123 VAL A C   1 
ATOM   3070 O  O   . VAL B 1 123 ? -13.720 -6.303  20.562  1.00 11.40 ? 123 VAL A O   1 
ATOM   3071 C  CB  . VAL B 1 123 ? -11.278 -5.169  19.161  1.00 9.50  ? 123 VAL A CB  1 
ATOM   3072 C  CG1 . VAL B 1 123 ? -10.441 -4.761  20.372  1.00 12.14 ? 123 VAL A CG1 1 
ATOM   3073 C  CG2 . VAL B 1 123 ? -10.446 -5.000  17.886  1.00 9.89  ? 123 VAL A CG2 1 
ATOM   3074 N  N   . HIS B 1 124 ? -12.042 -7.519  21.539  1.00 9.72  ? 124 HIS A N   1 
ATOM   3075 C  CA  . HIS B 1 124 ? -12.817 -7.798  22.769  1.00 10.09 ? 124 HIS A CA  1 
ATOM   3076 C  C   . HIS B 1 124 ? -11.882 -7.508  23.916  1.00 10.31 ? 124 HIS A C   1 
ATOM   3077 O  O   . HIS B 1 124 ? -10.652 -7.622  23.810  1.00 10.91 ? 124 HIS A O   1 
ATOM   3078 C  CB  . HIS B 1 124 ? -13.135 -9.314  22.850  1.00 10.21 ? 124 HIS A CB  1 
ATOM   3079 C  CG  . HIS B 1 124 ? -13.741 -9.930  21.594  1.00 9.92  ? 124 HIS A CG  1 
ATOM   3080 N  ND1 . HIS B 1 124 ? -13.013 -10.202 20.475  1.00 10.15 ? 124 HIS A ND1 1 
ATOM   3081 C  CD2 . HIS B 1 124 ? -15.037 -10.404 21.338  1.00 10.79 ? 124 HIS A CD2 1 
ATOM   3082 C  CE1 . HIS B 1 124 ? -13.857 -10.814 19.591  1.00 9.97  ? 124 HIS A CE1 1 
ATOM   3083 N  NE2 . HIS B 1 124 ? -15.054 -10.975 20.145  1.00 10.11 ? 124 HIS A NE2 1 
ATOM   3084 N  N   . TRP B 1 125 ? -12.483 -7.278  25.108  1.00 11.58 ? 125 TRP A N   1 
ATOM   3085 C  CA  . TRP B 1 125 ? -11.669 -7.016  26.299  1.00 11.75 ? 125 TRP A CA  1 
ATOM   3086 C  C   . TRP B 1 125 ? -12.200 -7.807  27.518  1.00 12.49 ? 125 TRP A C   1 
ATOM   3087 O  O   . TRP B 1 125 ? -13.417 -7.981  27.682  1.00 12.63 ? 125 TRP A O   1 
ATOM   3088 C  CB  . TRP B 1 125 ? -11.606 -5.489  26.614  1.00 12.60 ? 125 TRP A CB  1 
ATOM   3089 C  CG  . TRP B 1 125 ? -12.916 -4.848  26.830  1.00 11.39 ? 125 TRP A CG  1 
ATOM   3090 C  CD1 . TRP B 1 125 ? -13.792 -4.361  25.881  1.00 11.58 ? 125 TRP A CD1 1 
ATOM   3091 C  CD2 . TRP B 1 125 ? -13.536 -4.540  28.124  1.00 13.39 ? 125 TRP A CD2 1 
ATOM   3092 N  NE1 . TRP B 1 125 ? -14.891 -3.755  26.433  1.00 13.17 ? 125 TRP A NE1 1 
ATOM   3093 C  CE2 . TRP B 1 125 ? -14.782 -3.874  27.841  1.00 14.32 ? 125 TRP A CE2 1 
ATOM   3094 C  CE3 . TRP B 1 125 ? -13.159 -4.804  29.458  1.00 14.20 ? 125 TRP A CE3 1 
ATOM   3095 C  CZ2 . TRP B 1 125 ? -15.657 -3.435  28.837  1.00 14.25 ? 125 TRP A CZ2 1 
ATOM   3096 C  CZ3 . TRP B 1 125 ? -14.013 -4.298  30.474  1.00 13.93 ? 125 TRP A CZ3 1 
ATOM   3097 C  CH2 . TRP B 1 125 ? -15.223 -3.644  30.177  1.00 14.58 ? 125 TRP A CH2 1 
ATOM   3098 N  N   . ASN B 1 126 ? -11.240 -8.160  28.359  1.00 12.94 ? 126 ASN A N   1 
ATOM   3099 C  CA  . ASN B 1 126 ? -11.505 -9.034  29.542  1.00 12.90 ? 126 ASN A CA  1 
ATOM   3100 C  C   . ASN B 1 126 ? -12.195 -8.239  30.660  1.00 13.25 ? 126 ASN A C   1 
ATOM   3101 O  O   . ASN B 1 126 ? -11.526 -7.599  31.510  1.00 13.13 ? 126 ASN A O   1 
ATOM   3102 C  CB  . ASN B 1 126 ? -10.168 -9.545  29.957  1.00 13.67 ? 126 ASN A CB  1 
ATOM   3103 C  CG  . ASN B 1 126 ? -10.279 -10.587 31.080  1.00 14.54 ? 126 ASN A CG  1 
ATOM   3104 O  OD1 . ASN B 1 126 ? -11.320 -10.724 31.701  1.00 14.34 ? 126 ASN A OD1 1 
ATOM   3105 N  ND2 . ASN B 1 126 ? -9.241  -11.317 31.263  1.00 16.48 ? 126 ASN A ND2 1 
ATOM   3106 N  N   . SER B 1 127 ? -13.514 -8.336  30.681  1.00 13.41 ? 127 SER A N   1 
ATOM   3107 C  CA  . SER B 1 127 ? -14.316 -7.586  31.685  1.00 13.69 ? 127 SER A CA  1 
ATOM   3108 C  C   . SER B 1 127 ? -14.370 -8.404  32.981  1.00 14.57 ? 127 SER A C   1 
ATOM   3109 O  O   . SER B 1 127 ? -14.880 -7.843  33.946  1.00 17.02 ? 127 SER A O   1 
ATOM   3110 C  CB  . SER B 1 127 ? -15.702 -7.217  31.169  1.00 13.95 ? 127 SER A CB  1 
ATOM   3111 O  OG  . SER B 1 127 ? -16.440 -8.382  30.851  1.00 16.29 ? 127 SER A OG  1 
ATOM   3112 N  N   . ASP B 1 128 ? -13.944 -9.686  32.968  1.00 15.41 ? 128 ASP A N   1 
ATOM   3113 C  CA  . ASP B 1 128 ? -13.943 -10.507 34.160  1.00 16.30 ? 128 ASP A CA  1 
ATOM   3114 C  C   . ASP B 1 128 ? -12.800 -10.060 35.082  1.00 16.79 ? 128 ASP A C   1 
ATOM   3115 O  O   . ASP B 1 128 ? -12.863 -10.331 36.302  1.00 19.40 ? 128 ASP A O   1 
ATOM   3116 C  CB  . ASP B 1 128 ? -13.733 -11.992 33.828  1.00 15.02 ? 128 ASP A CB  1 
ATOM   3117 C  CG  . ASP B 1 128 ? -15.003 -12.710 33.382  1.00 16.49 ? 128 ASP A CG  1 
ATOM   3118 O  OD1 . ASP B 1 128 ? -14.857 -13.899 32.979  1.00 18.61 ? 128 ASP A OD1 1 
ATOM   3119 O  OD2 . ASP B 1 128 ? -16.119 -12.140 33.460  1.00 21.78 ? 128 ASP A OD2 1 
ATOM   3120 N  N   . LYS B 1 129 ? -11.762 -9.420  34.561  1.00 16.54 ? 129 LYS A N   1 
ATOM   3121 C  CA  . LYS B 1 129 ? -10.628 -8.964  35.357  1.00 15.23 ? 129 LYS A CA  1 
ATOM   3122 C  C   . LYS B 1 129 ? -10.450 -7.454  35.380  1.00 16.41 ? 129 LYS A C   1 
ATOM   3123 O  O   . LYS B 1 129 ? -9.760  -6.924  36.279  1.00 16.20 ? 129 LYS A O   1 
ATOM   3124 C  CB  . LYS B 1 129 ? -9.332  -9.628  34.850  1.00 16.29 ? 129 LYS A CB  1 
ATOM   3125 C  CG  . LYS B 1 129 ? -9.079  -11.064 35.303  1.00 21.84 ? 129 LYS A CG  1 
ATOM   3126 C  CD  . LYS B 1 129 ? -7.616  -11.496 34.989  1.00 21.95 ? 129 LYS A CD  1 
ATOM   3127 C  CE  . LYS B 1 129 ? -6.509  -10.677 35.722  1.00 23.94 ? 129 LYS A CE  1 
ATOM   3128 N  NZ  . LYS B 1 129 ? -5.131  -11.264 35.425  1.00 25.41 ? 129 LYS A NZ  1 
ATOM   3129 N  N   . TYR B 1 130 ? -10.934 -6.731  34.340  1.00 14.70 ? 130 TYR A N   1 
ATOM   3130 C  CA  . TYR B 1 130 ? -10.639 -5.326  34.168  1.00 15.03 ? 130 TYR A CA  1 
ATOM   3131 C  C   . TYR B 1 130 ? -11.919 -4.536  34.049  1.00 15.62 ? 130 TYR A C   1 
ATOM   3132 O  O   . TYR B 1 130 ? -12.971 -5.081  33.598  1.00 14.90 ? 130 TYR A O   1 
ATOM   3133 C  CB  . TYR B 1 130 ? -9.701  -5.065  32.890  1.00 16.38 ? 130 TYR A CB  1 
ATOM   3134 C  CG  . TYR B 1 130 ? -8.440  -5.833  33.043  1.00 15.61 ? 130 TYR A CG  1 
ATOM   3135 C  CD1 . TYR B 1 130 ? -7.522  -5.525  34.060  1.00 17.85 ? 130 TYR A CD1 1 
ATOM   3136 C  CD2 . TYR B 1 130 ? -8.189  -6.969  32.260  1.00 13.83 ? 130 TYR A CD2 1 
ATOM   3137 C  CE1 . TYR B 1 130 ? -6.402  -6.331  34.267  1.00 19.16 ? 130 TYR A CE1 1 
ATOM   3138 C  CE2 . TYR B 1 130 ? -7.078  -7.770  32.426  1.00 14.89 ? 130 TYR A CE2 1 
ATOM   3139 C  CZ  . TYR B 1 130 ? -6.136  -7.424  33.431  1.00 18.29 ? 130 TYR A CZ  1 
ATOM   3140 O  OH  . TYR B 1 130 ? -5.092  -8.268  33.625  1.00 18.74 ? 130 TYR A OH  1 
ATOM   3141 N  N   . PRO B 1 131 ? -11.906 -3.258  34.515  1.00 15.29 ? 131 PRO A N   1 
ATOM   3142 C  CA  . PRO B 1 131 ? -13.158 -2.495  34.586  1.00 16.57 ? 131 PRO A CA  1 
ATOM   3143 C  C   . PRO B 1 131 ? -13.548 -1.827  33.288  1.00 16.31 ? 131 PRO A C   1 
ATOM   3144 O  O   . PRO B 1 131 ? -14.691 -1.318  33.190  1.00 16.72 ? 131 PRO A O   1 
ATOM   3145 C  CB  . PRO B 1 131 ? -12.831 -1.378  35.613  1.00 16.45 ? 131 PRO A CB  1 
ATOM   3146 C  CG  . PRO B 1 131 ? -11.362 -1.256  35.621  1.00 16.34 ? 131 PRO A CG  1 
ATOM   3147 C  CD  . PRO B 1 131 ? -10.796 -2.613  35.262  1.00 15.36 ? 131 PRO A CD  1 
ATOM   3148 N  N   . SER B 1 132 ? -12.578 -1.752  32.351  1.00 15.78 ? 132 SER A N   1 
ATOM   3149 C  CA  . SER B 1 132 ? -12.874 -1.001  31.117  1.00 16.35 ? 132 SER A CA  1 
ATOM   3150 C  C   . SER B 1 132 ? -11.882 -1.490  30.058  1.00 14.24 ? 132 SER A C   1 
ATOM   3151 O  O   . SER B 1 132 ? -10.825 -2.085  30.338  1.00 13.50 ? 132 SER A O   1 
ATOM   3152 C  CB  . SER B 1 132 ? -12.593 0.483   31.327  1.00 17.06 ? 132 SER A CB  1 
ATOM   3153 O  OG  . SER B 1 132 ? -11.218 0.724   31.568  1.00 18.19 ? 132 SER A OG  1 
ATOM   3154 N  N   . PHE B 1 133 ? -12.281 -1.259  28.808  1.00 13.95 ? 133 PHE A N   1 
ATOM   3155 C  CA  . PHE B 1 133 ? -11.351 -1.522  27.678  1.00 17.08 ? 133 PHE A CA  1 
ATOM   3156 C  C   . PHE B 1 133 ? -10.012 -0.856  27.859  1.00 15.32 ? 133 PHE A C   1 
ATOM   3157 O  O   . PHE B 1 133 ? -8.980  -1.453  27.618  1.00 16.04 ? 133 PHE A O   1 
ATOM   3158 C  CB  . PHE B 1 133 ? -12.059 -1.058  26.401  1.00 16.14 ? 133 PHE A CB  1 
ATOM   3159 C  CG  . PHE B 1 133 ? -11.163 -1.071  25.163  1.00 18.56 ? 133 PHE A CG  1 
ATOM   3160 C  CD1 . PHE B 1 133 ? -10.873 -2.279  24.533  1.00 18.33 ? 133 PHE A CD1 1 
ATOM   3161 C  CD2 . PHE B 1 133 ? -10.595 0.095   24.700  1.00 20.79 ? 133 PHE A CD2 1 
ATOM   3162 C  CE1 . PHE B 1 133 ? -10.017 -2.336  23.461  1.00 18.01 ? 133 PHE A CE1 1 
ATOM   3163 C  CE2 . PHE B 1 133 ? -9.724  0.071   23.598  1.00 21.75 ? 133 PHE A CE2 1 
ATOM   3164 C  CZ  . PHE B 1 133 ? -9.455  -1.142  22.999  1.00 19.31 ? 133 PHE A CZ  1 
ATOM   3165 N  N   . VAL B 1 134 ? -9.993  0.432   28.265  1.00 17.62 ? 134 VAL A N   1 
ATOM   3166 C  CA  . VAL B 1 134 ? -8.747  1.186   28.418  1.00 20.66 ? 134 VAL A CA  1 
ATOM   3167 C  C   . VAL B 1 134 ? -7.798  0.498   29.379  1.00 19.64 ? 134 VAL A C   1 
ATOM   3168 O  O   . VAL B 1 134 ? -6.597  0.303   29.093  1.00 18.79 ? 134 VAL A O   1 
ATOM   3169 C  CB  . VAL B 1 134 ? -9.019  2.650   28.867  1.00 23.73 ? 134 VAL A CB  1 
ATOM   3170 C  CG1 . VAL B 1 134 ? -7.672  3.338   29.090  1.00 26.47 ? 134 VAL A CG1 1 
ATOM   3171 C  CG2 . VAL B 1 134 ? -9.742  3.434   27.772  1.00 29.26 ? 134 VAL A CG2 1 
ATOM   3172 N  N   . GLU B 1 135 ? -8.302  0.008   30.533  1.00 17.27 ? 135 GLU A N   1 
ATOM   3173 C  CA  . GLU B 1 135 ? -7.444  -0.714  31.451  1.00 19.46 ? 135 GLU A CA  1 
ATOM   3174 C  C   . GLU B 1 135 ? -6.983  -2.071  30.902  1.00 18.40 ? 135 GLU A C   1 
ATOM   3175 O  O   . GLU B 1 135 ? -5.826  -2.465  31.034  1.00 18.17 ? 135 GLU A O   1 
ATOM   3176 C  CB  . GLU B 1 135 ? -8.153  -0.945  32.836  1.00 19.73 ? 135 GLU A CB  1 
ATOM   3177 C  CG  . GLU B 1 135 ? -8.429  0.435   33.547  1.00 21.56 ? 135 GLU A CG  1 
ATOM   3178 C  CD  . GLU B 1 135 ? -7.189  1.105   34.080  1.00 23.93 ? 135 GLU A CD  1 
ATOM   3179 O  OE1 . GLU B 1 135 ? -6.073  0.540   33.985  1.00 24.22 ? 135 GLU A OE1 1 
ATOM   3180 O  OE2 . GLU B 1 135 ? -7.379  2.201   34.665  1.00 27.02 ? 135 GLU A OE2 1 
ATOM   3181 N  N   . ALA B 1 136 ? -7.919  -2.761  30.246  1.00 14.96 ? 136 ALA A N   1 
ATOM   3182 C  CA  . ALA B 1 136 ? -7.595  -4.111  29.720  1.00 12.87 ? 136 ALA A CA  1 
ATOM   3183 C  C   . ALA B 1 136 ? -6.476  -4.019  28.647  1.00 13.29 ? 136 ALA A C   1 
ATOM   3184 O  O   . ALA B 1 136 ? -5.642  -4.891  28.557  1.00 15.27 ? 136 ALA A O   1 
ATOM   3185 C  CB  . ALA B 1 136 ? -8.848  -4.747  29.130  1.00 12.43 ? 136 ALA A CB  1 
ATOM   3186 N  N   . ALA B 1 137 ? -6.488  -2.915  27.918  1.00 16.10 ? 137 ALA A N   1 
ATOM   3187 C  CA  . ALA B 1 137 ? -5.582  -2.796  26.775  1.00 16.48 ? 137 ALA A CA  1 
ATOM   3188 C  C   . ALA B 1 137 ? -4.118  -2.690  27.193  1.00 16.72 ? 137 ALA A C   1 
ATOM   3189 O  O   . ALA B 1 137 ? -3.213  -2.800  26.343  1.00 16.66 ? 137 ALA A O   1 
ATOM   3190 C  CB  . ALA B 1 137 ? -6.005  -1.597  25.899  1.00 14.94 ? 137 ALA A CB  1 
ATOM   3191 N  N   . HIS B 1 138 ? -3.886  -2.460  28.510  1.00 17.98 ? 138 HIS A N   1 
ATOM   3192 C  CA  . HIS B 1 138 ? -2.509  -2.391  29.044  1.00 19.00 ? 138 HIS A CA  1 
ATOM   3193 C  C   . HIS B 1 138 ? -2.045  -3.598  29.822  1.00 20.58 ? 138 HIS A C   1 
ATOM   3194 O  O   . HIS B 1 138 ? -1.065  -3.537  30.551  1.00 24.03 ? 138 HIS A O   1 
ATOM   3195 C  CB  . HIS B 1 138 ? -2.395  -1.087  29.878  1.00 22.30 ? 138 HIS A CB  1 
ATOM   3196 C  CG  . HIS B 1 138 ? -2.475  0.175   29.057  1.00 23.58 ? 138 HIS A CG  1 
ATOM   3197 N  ND1 . HIS B 1 138 ? -1.367  0.753   28.482  1.00 27.32 ? 138 HIS A ND1 1 
ATOM   3198 C  CD2 . HIS B 1 138 ? -3.554  0.948   28.681  1.00 24.74 ? 138 HIS A CD2 1 
ATOM   3199 C  CE1 . HIS B 1 138 ? -1.764  1.846   27.809  1.00 26.68 ? 138 HIS A CE1 1 
ATOM   3200 N  NE2 . HIS B 1 138 ? -3.073  1.984   27.946  1.00 25.59 ? 138 HIS A NE2 1 
ATOM   3201 N  N   . GLU B 1 139 ? -2.729  -4.733  29.697  1.00 18.91 ? 139 GLU A N   1 
ATOM   3202 C  CA  . GLU B 1 139 ? -2.373  -5.953  30.365  1.00 18.98 ? 139 GLU A CA  1 
ATOM   3203 C  C   . GLU B 1 139 ? -2.204  -7.102  29.421  1.00 16.88 ? 139 GLU A C   1 
ATOM   3204 O  O   . GLU B 1 139 ? -3.004  -7.186  28.420  1.00 15.53 ? 139 GLU A O   1 
ATOM   3205 C  CB  . GLU B 1 139 ? -3.559  -6.360  31.296  1.00 21.54 ? 139 GLU A CB  1 
ATOM   3206 C  CG  . GLU B 1 139 ? -3.909  -5.305  32.324  1.00 28.81 ? 139 GLU A CG  1 
ATOM   3207 C  CD  . GLU B 1 139 ? -3.033  -5.415  33.552  1.00 31.26 ? 139 GLU A CD  1 
ATOM   3208 O  OE1 . GLU B 1 139 ? -1.962  -6.082  33.516  1.00 35.52 ? 139 GLU A OE1 1 
ATOM   3209 O  OE2 . GLU B 1 139 ? -3.403  -4.747  34.567  1.00 35.35 ? 139 GLU A OE2 1 
ATOM   3210 N  N   . PRO B 1 140 ? -1.289  -8.027  29.673  1.00 18.13 ? 140 PRO A N   1 
ATOM   3211 C  CA  . PRO B 1 140 ? -1.079  -9.125  28.721  1.00 17.68 ? 140 PRO A CA  1 
ATOM   3212 C  C   . PRO B 1 140 ? -2.299  -9.948  28.454  1.00 15.86 ? 140 PRO A C   1 
ATOM   3213 O  O   . PRO B 1 140 ? -2.471  -10.365 27.291  1.00 16.77 ? 140 PRO A O   1 
ATOM   3214 C  CB  . PRO B 1 140 ? 0.025   -9.992  29.367  1.00 17.38 ? 140 PRO A CB  1 
ATOM   3215 C  CG  . PRO B 1 140 ? 0.804   -8.940  30.097  1.00 23.39 ? 140 PRO A CG  1 
ATOM   3216 C  CD  . PRO B 1 140 ? -0.197  -8.038  30.702  1.00 19.67 ? 140 PRO A CD  1 
ATOM   3217 N  N   . ASP B 1 141 ? -3.197  -10.117 29.423  1.00 13.70 ? 141 ASP A N   1 
ATOM   3218 C  CA  . ASP B 1 141 ? -4.364  -10.943 29.200  1.00 14.53 ? 141 ASP A CA  1 
ATOM   3219 C  C   . ASP B 1 141 ? -5.617  -10.054 29.008  1.00 15.17 ? 141 ASP A C   1 
ATOM   3220 O  O   . ASP B 1 141 ? -6.770  -10.525 29.154  1.00 15.69 ? 141 ASP A O   1 
ATOM   3221 C  CB  . ASP B 1 141 ? -4.614  -11.892 30.369  1.00 14.53 ? 141 ASP A CB  1 
ATOM   3222 C  CG  . ASP B 1 141 ? -4.786  -11.107 31.666  1.00 17.05 ? 141 ASP A CG  1 
ATOM   3223 O  OD1 . ASP B 1 141 ? -4.518  -9.850  31.697  1.00 16.31 ? 141 ASP A OD1 1 
ATOM   3224 O  OD2 . ASP B 1 141 ? -5.300  -11.781 32.658  1.00 20.91 ? 141 ASP A OD2 1 
ATOM   3225 N  N   . GLY B 1 142 ? -5.419  -8.799  28.618  1.00 12.70 ? 142 GLY A N   1 
ATOM   3226 C  CA  . GLY B 1 142 ? -6.536  -7.837  28.573  1.00 11.92 ? 142 GLY A CA  1 
ATOM   3227 C  C   . GLY B 1 142 ? -7.436  -7.939  27.334  1.00 12.07 ? 142 GLY A C   1 
ATOM   3228 O  O   . GLY B 1 142 ? -8.666  -7.729  27.414  1.00 12.63 ? 142 GLY A O   1 
ATOM   3229 N  N   . LEU B 1 143 ? -6.803  -8.214  26.204  1.00 13.47 ? 143 LEU A N   1 
ATOM   3230 C  CA  . LEU B 1 143 ? -7.585  -8.089  24.956  1.00 11.93 ? 143 LEU A CA  1 
ATOM   3231 C  C   . LEU B 1 143 ? -7.556  -9.417  24.186  1.00 10.55 ? 143 LEU A C   1 
ATOM   3232 O  O   . LEU B 1 143 ? -6.653  -10.251 24.295  1.00 11.52 ? 143 LEU A O   1 
ATOM   3233 C  CB  . LEU B 1 143 ? -6.931  -7.016  23.974  1.00 11.48 ? 143 LEU A CB  1 
ATOM   3234 C  CG  . LEU B 1 143 ? -6.879  -5.597  24.578  1.00 11.39 ? 143 LEU A CG  1 
ATOM   3235 C  CD1 . LEU B 1 143 ? -6.354  -4.648  23.378  1.00 12.21 ? 143 LEU A CD1 1 
ATOM   3236 C  CD2 . LEU B 1 143 ? -8.281  -5.156  25.045  1.00 12.22 ? 143 LEU A CD2 1 
ATOM   3237 N  N   . ALA B 1 144 ? -8.643  -9.647  23.412  1.00 10.63 ? 144 ALA A N   1 
ATOM   3238 C  CA  . ALA B 1 144 ? -8.680  -10.844 22.535  1.00 11.05 ? 144 ALA A CA  1 
ATOM   3239 C  C   . ALA B 1 144 ? -9.153  -10.340 21.203  1.00 9.61  ? 144 ALA A C   1 
ATOM   3240 O  O   . ALA B 1 144 ? -10.186 -9.643  21.132  1.00 9.98  ? 144 ALA A O   1 
ATOM   3241 C  CB  . ALA B 1 144 ? -9.632  -11.970 23.000  1.00 11.92 ? 144 ALA A CB  1 
ATOM   3242 N  N   . VAL B 1 145 ? -8.386  -10.645 20.127  1.00 9.49  ? 145 VAL A N   1 
ATOM   3243 C  CA  . VAL B 1 145 ? -8.843  -10.209 18.762  1.00 9.33  ? 145 VAL A CA  1 
ATOM   3244 C  C   . VAL B 1 145 ? -9.015  -11.421 17.905  1.00 9.23  ? 145 VAL A C   1 
ATOM   3245 O  O   . VAL B 1 145 ? -8.101  -12.245 17.805  1.00 10.48 ? 145 VAL A O   1 
ATOM   3246 C  CB  . VAL B 1 145 ? -7.843  -9.222  18.149  1.00 10.69 ? 145 VAL A CB  1 
ATOM   3247 C  CG1 . VAL B 1 145 ? -8.419  -8.679  16.791  1.00 10.60 ? 145 VAL A CG1 1 
ATOM   3248 C  CG2 . VAL B 1 145 ? -7.693  -8.020  19.114  1.00 11.96 ? 145 VAL A CG2 1 
ATOM   3249 N  N   . LEU B 1 146 ? -10.197 -11.505 17.276  1.00 9.58  ? 146 LEU A N   1 
ATOM   3250 C  CA  . LEU B 1 146 ? -10.504 -12.607 16.352  1.00 10.49 ? 146 LEU A CA  1 
ATOM   3251 C  C   . LEU B 1 146 ? -10.179 -12.066 14.973  1.00 11.99 ? 146 LEU A C   1 
ATOM   3252 O  O   . LEU B 1 146 ? -10.696 -10.963 14.609  1.00 13.30 ? 146 LEU A O   1 
ATOM   3253 C  CB  . LEU B 1 146 ? -12.006 -12.982 16.494  1.00 11.68 ? 146 LEU A CB  1 
ATOM   3254 C  CG  . LEU B 1 146 ? -12.537 -14.096 15.601  1.00 17.50 ? 146 LEU A CG  1 
ATOM   3255 C  CD1 . LEU B 1 146 ? -11.850 -15.439 15.909  1.00 17.57 ? 146 LEU A CD1 1 
ATOM   3256 C  CD2 . LEU B 1 146 ? -14.069 -14.153 15.869  1.00 17.65 ? 146 LEU A CD2 1 
ATOM   3257 N  N   . GLY B 1 147 ? -9.357  -12.785 14.220  1.00 10.33 ? 147 GLY A N   1 
ATOM   3258 C  CA  . GLY B 1 147 ? -9.004  -12.290 12.881  1.00 10.77 ? 147 GLY A CA  1 
ATOM   3259 C  C   . GLY B 1 147 ? -9.684  -13.230 11.867  1.00 11.00 ? 147 GLY A C   1 
ATOM   3260 O  O   . GLY B 1 147 ? -9.666  -14.462 12.025  1.00 11.92 ? 147 GLY A O   1 
ATOM   3261 N  N   . VAL B 1 148 ? -10.317 -12.637 10.808  1.00 10.38 ? 148 VAL A N   1 
ATOM   3262 C  CA  . VAL B 1 148 ? -11.018 -13.455 9.766   1.00 9.52  ? 148 VAL A CA  1 
ATOM   3263 C  C   . VAL B 1 148 ? -10.461 -12.952 8.455   1.00 10.08 ? 148 VAL A C   1 
ATOM   3264 O  O   . VAL B 1 148 ? -10.554 -11.747 8.193   1.00 11.36 ? 148 VAL A O   1 
ATOM   3265 C  CB  . VAL B 1 148 ? -12.551 -13.186 9.818   1.00 11.42 ? 148 VAL A CB  1 
ATOM   3266 C  CG1 . VAL B 1 148 ? -13.257 -14.103 8.761   1.00 11.21 ? 148 VAL A CG1 1 
ATOM   3267 C  CG2 . VAL B 1 148 ? -13.076 -13.474 11.284  1.00 12.78 ? 148 VAL A CG2 1 
ATOM   3268 N  N   . PHE B 1 149 ? -9.934  -13.854 7.621   1.00 10.49 ? 149 PHE A N   1 
ATOM   3269 C  CA  . PHE B 1 149 ? -9.459  -13.482 6.308   1.00 11.60 ? 149 PHE A CA  1 
ATOM   3270 C  C   . PHE B 1 149 ? -10.623 -13.334 5.354   1.00 12.51 ? 149 PHE A C   1 
ATOM   3271 O  O   . PHE B 1 149 ? -11.679 -13.973 5.521   1.00 11.96 ? 149 PHE A O   1 
ATOM   3272 C  CB  . PHE B 1 149 ? -8.607  -14.648 5.806   1.00 11.78 ? 149 PHE A CB  1 
ATOM   3273 C  CG  . PHE B 1 149 ? -7.338  -14.806 6.619   1.00 11.27 ? 149 PHE A CG  1 
ATOM   3274 C  CD1 . PHE B 1 149 ? -6.462  -13.730 6.757   1.00 10.96 ? 149 PHE A CD1 1 
ATOM   3275 C  CD2 . PHE B 1 149 ? -7.079  -16.076 7.167   1.00 11.62 ? 149 PHE A CD2 1 
ATOM   3276 C  CE1 . PHE B 1 149 ? -5.264  -13.875 7.476   1.00 10.53 ? 149 PHE A CE1 1 
ATOM   3277 C  CE2 . PHE B 1 149 ? -5.872  -16.227 7.892   1.00 12.43 ? 149 PHE A CE2 1 
ATOM   3278 C  CZ  . PHE B 1 149 ? -5.000  -15.149 7.993   1.00 10.77 ? 149 PHE A CZ  1 
ATOM   3279 N  N   . LEU B 1 150 ? -10.464 -12.416 4.427   1.00 10.82 ? 150 LEU A N   1 
ATOM   3280 C  CA  . LEU B 1 150 ? -11.401 -12.208 3.290   1.00 12.08 ? 150 LEU A CA  1 
ATOM   3281 C  C   . LEU B 1 150 ? -10.668 -12.584 2.001   1.00 12.09 ? 150 LEU A C   1 
ATOM   3282 O  O   . LEU B 1 150 ? -9.555  -12.099 1.749   1.00 12.41 ? 150 LEU A O   1 
ATOM   3283 C  CB  . LEU B 1 150 ? -11.879 -10.751 3.213   1.00 11.93 ? 150 LEU A CB  1 
ATOM   3284 C  CG  . LEU B 1 150 ? -12.930 -10.333 4.277   1.00 12.45 ? 150 LEU A CG  1 
ATOM   3285 C  CD1 . LEU B 1 150 ? -12.344 -10.290 5.720   1.00 12.46 ? 150 LEU A CD1 1 
ATOM   3286 C  CD2 . LEU B 1 150 ? -13.466 -8.934  3.815   1.00 12.52 ? 150 LEU A CD2 1 
ATOM   3287 N  N   . GLN B 1 151 ? -11.342 -13.385 1.154   1.00 12.81 ? 151 GLN A N   1 
ATOM   3288 C  CA  . GLN B 1 151 ? -10.817 -13.710 -0.192  1.00 16.54 ? 151 GLN A CA  1 
ATOM   3289 C  C   . GLN B 1 151 ? -11.831 -13.160 -1.177  1.00 15.73 ? 151 GLN A C   1 
ATOM   3290 O  O   . GLN B 1 151 ? -13.049 -12.989 -0.818  1.00 14.59 ? 151 GLN A O   1 
ATOM   3291 C  CB  . GLN B 1 151 ? -10.573 -15.166 -0.352  1.00 21.40 ? 151 GLN A CB  1 
ATOM   3292 C  CG  . GLN B 1 151 ? -11.790 -16.007 -0.254  1.00 22.79 ? 151 GLN A CG  1 
ATOM   3293 C  CD  . GLN B 1 151 ? -11.426 -17.492 -0.409  1.00 26.19 ? 151 GLN A CD  1 
ATOM   3294 O  OE1 . GLN B 1 151 ? -10.245 -17.871 -0.518  1.00 28.68 ? 151 GLN A OE1 1 
ATOM   3295 N  NE2 . GLN B 1 151 ? -12.432 -18.309 -0.451  1.00 30.93 ? 151 GLN A NE2 1 
ATOM   3296 N  N   . ILE B 1 152 ? -11.361 -12.864 -2.407  1.00 16.19 ? 152 ILE A N   1 
ATOM   3297 C  CA  . ILE B 1 152 ? -12.307 -12.383 -3.432  1.00 15.56 ? 152 ILE A CA  1 
ATOM   3298 C  C   . ILE B 1 152 ? -13.192 -13.556 -3.903  1.00 15.62 ? 152 ILE A C   1 
ATOM   3299 O  O   . ILE B 1 152 ? -12.726 -14.683 -4.179  1.00 21.84 ? 152 ILE A O   1 
ATOM   3300 C  CB  . ILE B 1 152 ? -11.562 -11.705 -4.645  1.00 15.29 ? 152 ILE A CB  1 
ATOM   3301 C  CG1 . ILE B 1 152 ? -10.688 -10.573 -4.094  1.00 13.98 ? 152 ILE A CG1 1 
ATOM   3302 C  CG2 . ILE B 1 152 ? -12.567 -11.264 -5.725  1.00 16.77 ? 152 ILE A CG2 1 
ATOM   3303 C  CD1 . ILE B 1 152 ? -11.462 -9.439  -3.499  1.00 14.91 ? 152 ILE A CD1 1 
ATOM   3304 N  N   . GLY B 1 153 ? -14.492 -13.313 -3.910  1.00 15.69 ? 153 GLY A N   1 
ATOM   3305 C  CA  . GLY B 1 153 ? -15.446 -14.269 -4.467  1.00 17.91 ? 153 GLY A CA  1 
ATOM   3306 C  C   . GLY B 1 153 ? -16.777 -13.586 -4.617  1.00 15.42 ? 153 GLY A C   1 
ATOM   3307 O  O   . GLY B 1 153 ? -16.841 -12.387 -5.108  1.00 18.29 ? 153 GLY A O   1 
ATOM   3308 N  N   A GLU B 1 154 ? -17.847 -14.276 -4.266  0.50 18.00 ? 154 GLU A N   1 
ATOM   3309 N  N   B GLU B 1 154 ? -17.834 -14.323 -4.216  0.50 16.80 ? 154 GLU A N   1 
ATOM   3310 C  CA  A GLU B 1 154 ? -19.147 -13.662 -4.504  0.50 19.24 ? 154 GLU A CA  1 
ATOM   3311 C  CA  B GLU B 1 154 ? -19.248 -13.832 -4.186  0.50 17.78 ? 154 GLU A CA  1 
ATOM   3312 C  C   A GLU B 1 154 ? -19.370 -12.614 -3.444  0.50 17.35 ? 154 GLU A C   1 
ATOM   3313 C  C   B GLU B 1 154 ? -19.306 -12.520 -3.391  0.50 16.69 ? 154 GLU A C   1 
ATOM   3314 O  O   A GLU B 1 154 ? -18.843 -12.792 -2.287  0.50 16.76 ? 154 GLU A O   1 
ATOM   3315 O  O   B GLU B 1 154 ? -18.597 -12.388 -2.374  0.50 16.04 ? 154 GLU A O   1 
ATOM   3316 C  CB  A GLU B 1 154 ? -20.233 -14.689 -4.401  0.50 22.17 ? 154 GLU A CB  1 
ATOM   3317 C  CB  B GLU B 1 154 ? -20.159 -14.890 -3.504  0.50 18.28 ? 154 GLU A CB  1 
ATOM   3318 C  CG  A GLU B 1 154 ? -19.785 -15.966 -5.071  0.50 24.95 ? 154 GLU A CG  1 
ATOM   3319 C  CG  B GLU B 1 154 ? -21.637 -14.596 -3.213  0.50 19.09 ? 154 GLU A CG  1 
ATOM   3320 C  CD  A GLU B 1 154 ? -20.878 -16.982 -5.142  0.50 33.36 ? 154 GLU A CD  1 
ATOM   3321 C  CD  B GLU B 1 154 ? -22.533 -15.854 -3.091  0.50 19.36 ? 154 GLU A CD  1 
ATOM   3322 O  OE1 A GLU B 1 154 ? -22.042 -16.603 -4.857  0.50 33.82 ? 154 GLU A OE1 1 
ATOM   3323 O  OE1 B GLU B 1 154 ? -22.899 -16.386 -4.169  0.50 20.61 ? 154 GLU A OE1 1 
ATOM   3324 O  OE2 A GLU B 1 154 ? -20.564 -18.148 -5.512  0.50 37.88 ? 154 GLU A OE2 1 
ATOM   3325 O  OE2 B GLU B 1 154 ? -22.950 -16.316 -1.982  0.50 18.09 ? 154 GLU A OE2 1 
ATOM   3326 N  N   . PRO B 1 155 ? -20.162 -11.574 -3.776  1.00 17.38 ? 155 PRO A N   1 
ATOM   3327 C  CA  . PRO B 1 155 ? -20.432 -10.448 -2.897  1.00 14.96 ? 155 PRO A CA  1 
ATOM   3328 C  C   . PRO B 1 155 ? -20.996 -10.987 -1.570  1.00 14.37 ? 155 PRO A C   1 
ATOM   3329 O  O   . PRO B 1 155 ? -21.664 -12.034 -1.518  1.00 16.28 ? 155 PRO A O   1 
ATOM   3330 C  CB  . PRO B 1 155 ? -21.525 -9.627  -3.585  1.00 16.42 ? 155 PRO A CB  1 
ATOM   3331 C  CG  . PRO B 1 155 ? -21.426 -10.010 -5.018  1.00 16.14 ? 155 PRO A CG  1 
ATOM   3332 C  CD  . PRO B 1 155 ? -20.889 -11.421 -5.102  1.00 16.00 ? 155 PRO A CD  1 
ATOM   3333 N  N   . ASN B 1 156 ? -20.678 -10.288 -0.494  1.00 15.29 ? 156 ASN A N   1 
ATOM   3334 C  CA  . ASN B 1 156 ? -21.095 -10.729 0.822   1.00 15.73 ? 156 ASN A CA  1 
ATOM   3335 C  C   . ASN B 1 156 ? -22.232 -9.847  1.258   1.00 15.81 ? 156 ASN A C   1 
ATOM   3336 O  O   . ASN B 1 156 ? -22.093 -8.634  1.392   1.00 13.74 ? 156 ASN A O   1 
ATOM   3337 C  CB  . ASN B 1 156 ? -19.884 -10.554 1.765   1.00 16.63 ? 156 ASN A CB  1 
ATOM   3338 C  CG  . ASN B 1 156 ? -20.119 -11.150 3.090   1.00 20.16 ? 156 ASN A CG  1 
ATOM   3339 O  OD1 . ASN B 1 156 ? -21.090 -10.768 3.776   1.00 20.60 ? 156 ASN A OD1 1 
ATOM   3340 N  ND2 . ASN B 1 156 ? -19.279 -12.123 3.462   1.00 17.55 ? 156 ASN A ND2 1 
ATOM   3341 N  N   . SER B 1 157 ? -23.425 -10.460 1.451   1.00 15.27 ? 157 SER A N   1 
ATOM   3342 C  CA  . SER B 1 157 ? -24.602 -9.616  1.761   1.00 17.19 ? 157 SER A CA  1 
ATOM   3343 C  C   . SER B 1 157 ? -24.497 -8.833  3.053   1.00 18.45 ? 157 SER A C   1 
ATOM   3344 O  O   . SER B 1 157 ? -25.059 -7.693  3.150   1.00 23.25 ? 157 SER A O   1 
ATOM   3345 C  CB  . SER B 1 157 ? -25.942 -10.457 1.712   1.00 18.85 ? 157 SER A CB  1 
ATOM   3346 O  OG  . SER B 1 157 ? -25.917 -11.469 2.713   1.00 22.54 ? 157 SER A OG  1 
ATOM   3347 N  N   A GLN B 1 158 ? -23.787 -9.394  4.018   0.50 17.04 ? 158 GLN A N   1 
ATOM   3348 N  N   B GLN B 1 158 ? -23.802 -9.366  4.058   0.50 19.02 ? 158 GLN A N   1 
ATOM   3349 C  CA  A GLN B 1 158 ? -23.608 -8.714  5.296   0.50 16.67 ? 158 GLN A CA  1 
ATOM   3350 C  CA  B GLN B 1 158 ? -23.664 -8.601  5.325   0.50 19.66 ? 158 GLN A CA  1 
ATOM   3351 C  C   A GLN B 1 158 ? -22.690 -7.526  5.158   0.50 17.45 ? 158 GLN A C   1 
ATOM   3352 C  C   B GLN B 1 158 ? -22.570 -7.533  5.287   0.50 19.53 ? 158 GLN A C   1 
ATOM   3353 O  O   A GLN B 1 158 ? -23.039 -6.409  5.629   0.50 17.79 ? 158 GLN A O   1 
ATOM   3354 O  O   B GLN B 1 158 ? -22.645 -6.493  5.978   0.50 20.57 ? 158 GLN A O   1 
ATOM   3355 C  CB  A GLN B 1 158 ? -23.121 -9.713  6.289   0.50 17.03 ? 158 GLN A CB  1 
ATOM   3356 C  CB  B GLN B 1 158 ? -23.572 -9.509  6.540   0.50 23.25 ? 158 GLN A CB  1 
ATOM   3357 C  CG  A GLN B 1 158 ? -24.255 -10.701 6.516   0.50 17.09 ? 158 GLN A CG  1 
ATOM   3358 C  CG  B GLN B 1 158 ? -24.977 -9.783  7.115   0.50 25.83 ? 158 GLN A CG  1 
ATOM   3359 C  CD  A GLN B 1 158 ? -23.893 -11.646 7.581   0.50 19.36 ? 158 GLN A CD  1 
ATOM   3360 C  CD  B GLN B 1 158 ? -24.992 -9.593  8.588   0.50 25.85 ? 158 GLN A CD  1 
ATOM   3361 O  OE1 A GLN B 1 158 ? -23.318 -12.661 7.301   0.50 18.61 ? 158 GLN A OE1 1 
ATOM   3362 O  OE1 B GLN B 1 158 ? -24.395 -10.407 9.298   0.50 32.54 ? 158 GLN A OE1 1 
ATOM   3363 N  NE2 A GLN B 1 158 ? -24.153 -11.284 8.836   0.50 19.46 ? 158 GLN A NE2 1 
ATOM   3364 N  NE2 B GLN B 1 158 ? -25.592 -8.507  9.077   0.50 19.45 ? 158 GLN A NE2 1 
ATOM   3365 N  N   . LEU B 1 159 ? -21.593 -7.712  4.407   1.00 17.14 ? 159 LEU A N   1 
ATOM   3366 C  CA  . LEU B 1 159 ? -20.658 -6.617  4.176   1.00 17.63 ? 159 LEU A CA  1 
ATOM   3367 C  C   . LEU B 1 159 ? -21.208 -5.495  3.326   1.00 18.54 ? 159 LEU A C   1 
ATOM   3368 O  O   . LEU B 1 159 ? -20.736 -4.349  3.409   1.00 17.95 ? 159 LEU A O   1 
ATOM   3369 C  CB  . LEU B 1 159 ? -19.328 -7.085  3.589   1.00 16.41 ? 159 LEU A CB  1 
ATOM   3370 C  CG  . LEU B 1 159 ? -18.625 -8.143  4.454   1.00 18.05 ? 159 LEU A CG  1 
ATOM   3371 C  CD1 . LEU B 1 159 ? -17.411 -8.721  3.702   1.00 17.70 ? 159 LEU A CD1 1 
ATOM   3372 C  CD2 . LEU B 1 159 ? -18.296 -7.587  5.858   1.00 19.90 ? 159 LEU A CD2 1 
ATOM   3373 N  N   . GLN B 1 160 ? -22.182 -5.824  2.490   1.00 19.68 ? 160 GLN A N   1 
ATOM   3374 C  CA  . GLN B 1 160 ? -22.883 -4.761  1.692   1.00 21.91 ? 160 GLN A CA  1 
ATOM   3375 C  C   . GLN B 1 160 ? -23.517 -3.730  2.640   1.00 21.26 ? 160 GLN A C   1 
ATOM   3376 O  O   . GLN B 1 160 ? -23.539 -2.518  2.403   1.00 22.58 ? 160 GLN A O   1 
ATOM   3377 C  CB  . GLN B 1 160 ? -23.953 -5.380  0.767   1.00 26.41 ? 160 GLN A CB  1 
ATOM   3378 C  CG  . GLN B 1 160 ? -24.544 -4.390  -0.226  1.00 23.56 ? 160 GLN A CG  1 
ATOM   3379 C  CD  . GLN B 1 160 ? -23.782 -4.316  -1.542  1.00 29.62 ? 160 GLN A CD  1 
ATOM   3380 O  OE1 . GLN B 1 160 ? -22.764 -4.946  -1.765  1.00 26.35 ? 160 GLN A OE1 1 
ATOM   3381 N  NE2 . GLN B 1 160 ? -24.312 -3.531  -2.452  1.00 29.84 ? 160 GLN A NE2 1 
ATOM   3382 N  N   . LYS B 1 161 ? -23.996 -4.171  3.787   1.00 22.78 ? 161 LYS A N   1 
ATOM   3383 C  CA  . LYS B 1 161 ? -24.486 -3.208  4.743   1.00 24.10 ? 161 LYS A CA  1 
ATOM   3384 C  C   . LYS B 1 161 ? -23.425 -2.153  5.196   1.00 25.16 ? 161 LYS A C   1 
ATOM   3385 O  O   . LYS B 1 161 ? -23.743 -0.984  5.397   1.00 22.83 ? 161 LYS A O   1 
ATOM   3386 C  CB  . LYS B 1 161 ? -25.104 -4.003  5.889   1.00 26.68 ? 161 LYS A CB  1 
ATOM   3387 C  CG  . LYS B 1 161 ? -25.000 -3.460  7.285   1.00 39.57 ? 161 LYS A CG  1 
ATOM   3388 C  CD  . LYS B 1 161 ? -26.100 -2.504  7.646   1.00 36.68 ? 161 LYS A CD  1 
ATOM   3389 C  CE  . LYS B 1 161 ? -26.507 -2.757  9.099   1.00 35.79 ? 161 LYS A CE  1 
ATOM   3390 N  NZ  . LYS B 1 161 ? -27.903 -2.275  9.125   1.00 35.85 ? 161 LYS A NZ  1 
ATOM   3391 N  N   . ILE B 1 162 ? -22.169 -2.601  5.382   1.00 21.10 ? 162 ILE A N   1 
ATOM   3392 C  CA  . ILE B 1 162 ? -21.070 -1.669  5.645   1.00 18.14 ? 162 ILE A CA  1 
ATOM   3393 C  C   . ILE B 1 162 ? -20.737 -0.839  4.406   1.00 16.54 ? 162 ILE A C   1 
ATOM   3394 O  O   . ILE B 1 162 ? -20.566 0.375   4.514   1.00 19.27 ? 162 ILE A O   1 
ATOM   3395 C  CB  . ILE B 1 162 ? -19.800 -2.440  6.156   1.00 16.98 ? 162 ILE A CB  1 
ATOM   3396 C  CG1 . ILE B 1 162 ? -20.186 -3.115  7.499   1.00 17.33 ? 162 ILE A CG1 1 
ATOM   3397 C  CG2 . ILE B 1 162 ? -18.614 -1.493  6.331   1.00 17.26 ? 162 ILE A CG2 1 
ATOM   3398 C  CD1 . ILE B 1 162 ? -19.056 -4.021  8.037   1.00 19.02 ? 162 ILE A CD1 1 
ATOM   3399 N  N   . THR B 1 163 ? -20.594 -1.469  3.238   1.00 17.72 ? 163 THR A N   1 
ATOM   3400 C  CA  . THR B 1 163 ? -20.218 -0.694  2.025   1.00 17.37 ? 163 THR A CA  1 
ATOM   3401 C  C   . THR B 1 163 ? -21.240 0.409   1.735   1.00 20.61 ? 163 THR A C   1 
ATOM   3402 O  O   . THR B 1 163 ? -20.851 1.473   1.377   1.00 20.85 ? 163 THR A O   1 
ATOM   3403 C  CB  . THR B 1 163 ? -19.800 -1.562  0.799   1.00 21.14 ? 163 THR A CB  1 
ATOM   3404 O  OG1 . THR B 1 163 ? -20.851 -2.406  0.429   1.00 23.80 ? 163 THR A OG1 1 
ATOM   3405 C  CG2 . THR B 1 163 ? -18.701 -2.482  1.163   1.00 20.06 ? 163 THR A CG2 1 
ATOM   3406 N  N   . ASP B 1 164 ? -22.534 0.131   1.965   1.00 20.88 ? 164 ASP A N   1 
ATOM   3407 C  CA  . ASP B 1 164 ? -23.583 1.168   1.789   1.00 23.34 ? 164 ASP A CA  1 
ATOM   3408 C  C   . ASP B 1 164 ? -23.399 2.418   2.637   1.00 23.82 ? 164 ASP A C   1 
ATOM   3409 O  O   . ASP B 1 164 ? -23.932 3.492   2.273   1.00 28.40 ? 164 ASP A O   1 
ATOM   3410 C  CB  . ASP B 1 164 ? -24.947 0.568   2.001   1.00 24.22 ? 164 ASP A CB  1 
ATOM   3411 C  CG  . ASP B 1 164 ? -25.378 -0.333  0.849   1.00 26.93 ? 164 ASP A CG  1 
ATOM   3412 O  OD1 . ASP B 1 164 ? -24.794 -0.308  -0.263  1.00 27.96 ? 164 ASP A OD1 1 
ATOM   3413 O  OD2 . ASP B 1 164 ? -26.306 -1.135  1.059   1.00 32.44 ? 164 ASP A OD2 1 
ATOM   3414 N  N   . THR B 1 165 ? -22.671 2.347   3.757   1.00 21.11 ? 165 THR A N   1 
ATOM   3415 C  CA  . THR B 1 165 ? -22.536 3.462   4.636   1.00 18.46 ? 165 THR A CA  1 
ATOM   3416 C  C   . THR B 1 165 ? -21.324 4.318   4.237   1.00 18.61 ? 165 THR A C   1 
ATOM   3417 O  O   . THR B 1 165 ? -21.141 5.400   4.771   1.00 20.93 ? 165 THR A O   1 
ATOM   3418 C  CB  . THR B 1 165 ? -22.302 3.127   6.151   1.00 22.13 ? 165 THR A CB  1 
ATOM   3419 O  OG1 . THR B 1 165 ? -21.019 2.451   6.306   1.00 20.10 ? 165 THR A OG1 1 
ATOM   3420 C  CG2 . THR B 1 165 ? -23.472 2.308   6.721   1.00 23.14 ? 165 THR A CG2 1 
ATOM   3421 N  N   . LEU B 1 166 ? -20.453 3.804   3.382   1.00 18.48 ? 166 LEU A N   1 
ATOM   3422 C  CA  . LEU B 1 166 ? -19.116 4.415   3.305   1.00 17.77 ? 166 LEU A CA  1 
ATOM   3423 C  C   . LEU B 1 166 ? -19.162 5.812   2.701   1.00 20.66 ? 166 LEU A C   1 
ATOM   3424 O  O   . LEU B 1 166 ? -18.353 6.641   3.118   1.00 20.28 ? 166 LEU A O   1 
ATOM   3425 C  CB  . LEU B 1 166 ? -18.075 3.566   2.526   1.00 18.65 ? 166 LEU A CB  1 
ATOM   3426 C  CG  . LEU B 1 166 ? -17.808 2.161   3.100   1.00 18.67 ? 166 LEU A CG  1 
ATOM   3427 C  CD1 . LEU B 1 166 ? -16.888 1.348   2.226   1.00 20.94 ? 166 LEU A CD1 1 
ATOM   3428 C  CD2 . LEU B 1 166 ? -17.166 2.220   4.500   1.00 19.42 ? 166 LEU A CD2 1 
ATOM   3429 N  N   . ASP B 1 167 ? -20.086 6.013   1.759   1.00 20.43 ? 167 ASP A N   1 
ATOM   3430 C  CA  . ASP B 1 167 ? -20.190 7.365   1.177   1.00 27.35 ? 167 ASP A CA  1 
ATOM   3431 C  C   . ASP B 1 167 ? -20.449 8.389   2.257   1.00 27.37 ? 167 ASP A C   1 
ATOM   3432 O  O   . ASP B 1 167 ? -19.907 9.530   2.193   1.00 30.56 ? 167 ASP A O   1 
ATOM   3433 C  CB  . ASP B 1 167 ? -21.226 7.433   0.028   1.00 28.57 ? 167 ASP A CB  1 
ATOM   3434 C  CG  . ASP B 1 167 ? -20.706 6.776   -1.262  1.00 30.64 ? 167 ASP A CG  1 
ATOM   3435 O  OD1 . ASP B 1 167 ? -19.470 6.574   -1.402  1.00 33.86 ? 167 ASP A OD1 1 
ATOM   3436 O  OD2 . ASP B 1 167 ? -21.520 6.491   -2.169  1.00 38.25 ? 167 ASP A OD2 1 
ATOM   3437 N  N   . SER B 1 168 ? -21.176 8.008   3.322   1.00 23.40 ? 168 SER A N   1 
ATOM   3438 C  CA  . SER B 1 168 ? -21.484 8.939   4.386   1.00 24.77 ? 168 SER A CA  1 
ATOM   3439 C  C   . SER B 1 168 ? -20.374 9.187   5.441   1.00 23.73 ? 168 SER A C   1 
ATOM   3440 O  O   . SER B 1 168 ? -20.448 10.083  6.265   1.00 28.26 ? 168 SER A O   1 
ATOM   3441 C  CB  . SER B 1 168 ? -22.793 8.522   5.038   1.00 26.25 ? 168 SER A CB  1 
ATOM   3442 O  OG  . SER B 1 168 ? -22.528 7.375   5.789   1.00 32.14 ? 168 SER A OG  1 
ATOM   3443 N  N   . ILE B 1 169 ? -19.316 8.370   5.387   1.00 20.51 ? 169 ILE A N   1 
ATOM   3444 C  CA  . ILE B 1 169 ? -18.163 8.523   6.248   1.00 19.47 ? 169 ILE A CA  1 
ATOM   3445 C  C   . ILE B 1 169 ? -16.827 8.617   5.480   1.00 18.71 ? 169 ILE A C   1 
ATOM   3446 O  O   . ILE B 1 169 ? -15.791 8.272   5.991   1.00 16.72 ? 169 ILE A O   1 
ATOM   3447 C  CB  . ILE B 1 169 ? -18.120 7.396   7.350   1.00 19.33 ? 169 ILE A CB  1 
ATOM   3448 C  CG1 . ILE B 1 169 ? -17.994 6.006   6.738   1.00 18.65 ? 169 ILE A CG1 1 
ATOM   3449 C  CG2 . ILE B 1 169 ? -19.367 7.485   8.179   1.00 20.51 ? 169 ILE A CG2 1 
ATOM   3450 C  CD1 . ILE B 1 169 ? -17.564 4.961   7.781   1.00 20.75 ? 169 ILE A CD1 1 
ATOM   3451 N  N   . LYS B 1 170 ? -16.863 9.254   4.289   1.00 19.65 ? 170 LYS A N   1 
ATOM   3452 C  CA  . LYS B 1 170 ? -15.608 9.373   3.522   1.00 20.51 ? 170 LYS A CA  1 
ATOM   3453 C  C   . LYS B 1 170 ? -14.494 10.079  4.264   1.00 18.23 ? 170 LYS A C   1 
ATOM   3454 O  O   . LYS B 1 170 ? -13.351 9.690   4.176   1.00 20.29 ? 170 LYS A O   1 
ATOM   3455 C  CB  . LYS B 1 170 ? -15.925 10.147  2.182   1.00 23.63 ? 170 LYS A CB  1 
ATOM   3456 C  CG  . LYS B 1 170 ? -14.675 10.441  1.337   1.00 33.13 ? 170 LYS A CG  1 
ATOM   3457 C  CD  . LYS B 1 170 ? -14.977 11.009  -0.090  1.00 35.18 ? 170 LYS A CD  1 
ATOM   3458 C  CE  . LYS B 1 170 ? -13.864 10.633  -1.111  1.00 38.34 ? 170 LYS A CE  1 
ATOM   3459 N  NZ  . LYS B 1 170 ? -13.807 9.201   -1.724  1.00 28.17 ? 170 LYS A NZ  1 
ATOM   3460 N  N   . GLU B 1 171 ? -14.759 11.203  4.920   1.00 21.42 ? 171 GLU A N   1 
ATOM   3461 C  CA  . GLU B 1 171 ? -13.739 11.973  5.586   1.00 23.46 ? 171 GLU A CA  1 
ATOM   3462 C  C   . GLU B 1 171 ? -13.409 11.471  6.928   1.00 22.59 ? 171 GLU A C   1 
ATOM   3463 O  O   . GLU B 1 171 ? -14.339 10.999  7.636   1.00 23.25 ? 171 GLU A O   1 
ATOM   3464 C  CB  . GLU B 1 171 ? -14.210 13.447  5.782   1.00 28.19 ? 171 GLU A CB  1 
ATOM   3465 C  CG  . GLU B 1 171 ? -14.343 14.163  4.438   1.00 34.41 ? 171 GLU A CG  1 
ATOM   3466 C  CD  . GLU B 1 171 ? -15.602 13.807  3.672   1.00 38.65 ? 171 GLU A CD  1 
ATOM   3467 O  OE1 . GLU B 1 171 ? -15.519 13.890  2.420   1.00 55.55 ? 171 GLU A OE1 1 
ATOM   3468 O  OE2 . GLU B 1 171 ? -16.671 13.458  4.273   1.00 43.92 ? 171 GLU A OE2 1 
ATOM   3469 N  N   . LYS B 1 172 ? -12.140 11.616  7.291   1.00 24.13 ? 172 LYS A N   1 
ATOM   3470 C  CA  . LYS B 1 172 ? -11.683 11.273  8.630   1.00 25.28 ? 172 LYS A CA  1 
ATOM   3471 C  C   . LYS B 1 172 ? -12.512 11.928  9.697   1.00 26.65 ? 172 LYS A C   1 
ATOM   3472 O  O   . LYS B 1 172 ? -12.878 13.140  9.590   1.00 26.25 ? 172 LYS A O   1 
ATOM   3473 C  CB  . LYS B 1 172 ? -10.197 11.536  8.835   1.00 26.39 ? 172 LYS A CB  1 
ATOM   3474 C  CG  . LYS B 1 172 ? -9.686  11.270  10.245  1.00 22.88 ? 172 LYS A CG  1 
ATOM   3475 C  CD  . LYS B 1 172 ? -8.190  11.566  10.226  1.00 27.75 ? 172 LYS A CD  1 
ATOM   3476 C  CE  . LYS B 1 172 ? -7.636  11.342  11.623  1.00 28.27 ? 172 LYS A CE  1 
ATOM   3477 N  NZ  . LYS B 1 172 ? -6.143  11.342  11.655  1.00 31.62 ? 172 LYS A NZ  1 
ATOM   3478 N  N   . GLY B 1 173 ? -12.921 11.104  10.665  1.00 22.91 ? 173 GLY A N   1 
ATOM   3479 C  CA  . GLY B 1 173 ? -13.745 11.606  11.742  1.00 20.02 ? 173 GLY A CA  1 
ATOM   3480 C  C   . GLY B 1 173 ? -15.236 11.553  11.551  1.00 20.15 ? 173 GLY A C   1 
ATOM   3481 O  O   . GLY B 1 173 ? -15.973 11.778  12.513  1.00 22.52 ? 173 GLY A O   1 
ATOM   3482 N  N   . LYS B 1 174 ? -15.751 11.304  10.380  1.00 18.52 ? 174 LYS A N   1 
ATOM   3483 C  CA  . LYS B 1 174 ? -17.195 11.210  10.281  1.00 21.53 ? 174 LYS A CA  1 
ATOM   3484 C  C   . LYS B 1 174 ? -17.735 9.898   10.837  1.00 22.96 ? 174 LYS A C   1 
ATOM   3485 O  O   . LYS B 1 174 ? -16.995 8.895   10.828  1.00 22.54 ? 174 LYS A O   1 
ATOM   3486 C  CB  . LYS B 1 174 ? -17.645 11.312  8.848   1.00 24.69 ? 174 LYS A CB  1 
ATOM   3487 C  CG  . LYS B 1 174 ? -17.449 12.759  8.307   1.00 28.66 ? 174 LYS A CG  1 
ATOM   3488 C  CD  . LYS B 1 174 ? -18.382 13.041  7.178   1.00 36.30 ? 174 LYS A CD  1 
ATOM   3489 C  CE  . LYS B 1 174 ? -18.353 14.547  6.972   1.00 41.58 ? 174 LYS A CE  1 
ATOM   3490 N  NZ  . LYS B 1 174 ? -18.527 14.763  5.521   1.00 46.84 ? 174 LYS A NZ  1 
ATOM   3491 N  N   . GLN B 1 175 ? -19.001 9.963   11.248  1.00 21.36 ? 175 GLN A N   1 
ATOM   3492 C  CA  . GLN B 1 175 ? -19.728 8.833   11.800  1.00 22.71 ? 175 GLN A CA  1 
ATOM   3493 C  C   . GLN B 1 175 ? -21.155 8.807   11.379  1.00 27.53 ? 175 GLN A C   1 
ATOM   3494 O  O   . GLN B 1 175 ? -21.752 9.843   10.961  1.00 22.78 ? 175 GLN A O   1 
ATOM   3495 C  CB  . GLN B 1 175 ? -19.593 8.797   13.333  1.00 26.41 ? 175 GLN A CB  1 
ATOM   3496 C  CG  . GLN B 1 175 ? -20.392 9.760   14.188  1.00 38.30 ? 175 GLN A CG  1 
ATOM   3497 C  CD  . GLN B 1 175 ? -20.103 9.438   15.674  1.00 43.39 ? 175 GLN A CD  1 
ATOM   3498 O  OE1 . GLN B 1 175 ? -21.022 9.326   16.502  1.00 41.45 ? 175 GLN A OE1 1 
ATOM   3499 N  NE2 . GLN B 1 175 ? -18.822 9.169   15.978  1.00 44.63 ? 175 GLN A NE2 1 
ATOM   3500 N  N   . THR B 1 176 ? -21.732 7.617   11.458  1.00 19.95 ? 176 THR A N   1 
ATOM   3501 C  CA  . THR B 1 176 ? -23.112 7.441   11.197  1.00 22.67 ? 176 THR A CA  1 
ATOM   3502 C  C   . THR B 1 176 ? -23.692 6.227   11.933  1.00 22.89 ? 176 THR A C   1 
ATOM   3503 O  O   . THR B 1 176 ? -22.925 5.345   12.391  1.00 21.52 ? 176 THR A O   1 
ATOM   3504 C  CB  . THR B 1 176 ? -23.416 7.425   9.701   1.00 24.45 ? 176 THR A CB  1 
ATOM   3505 O  OG1 . THR B 1 176 ? -24.792 7.756   9.495   1.00 24.37 ? 176 THR A OG1 1 
ATOM   3506 C  CG2 . THR B 1 176 ? -23.123 6.113   9.058   1.00 25.40 ? 176 THR A CG2 1 
ATOM   3507 N  N   . ARG B 1 177 ? -25.019 6.195   12.103  1.00 21.10 ? 177 ARG A N   1 
ATOM   3508 C  CA  . ARG B 1 177 ? -25.610 5.124   12.886  1.00 19.98 ? 177 ARG A CA  1 
ATOM   3509 C  C   . ARG B 1 177 ? -25.576 3.893   12.118  1.00 21.13 ? 177 ARG A C   1 
ATOM   3510 O  O   . ARG B 1 177 ? -25.711 3.925   10.919  1.00 19.65 ? 177 ARG A O   1 
ATOM   3511 C  CB  . ARG B 1 177 ? -27.035 5.461   13.324  1.00 23.24 ? 177 ARG A CB  1 
ATOM   3512 C  CG  . ARG B 1 177 ? -26.854 6.672   14.218  1.00 26.18 ? 177 ARG A CG  1 
ATOM   3513 C  CD  . ARG B 1 177 ? -28.154 7.197   14.772  1.00 34.08 ? 177 ARG A CD  1 
ATOM   3514 N  NE  . ARG B 1 177 ? -28.883 6.121   15.420  1.00 34.52 ? 177 ARG A NE  1 
ATOM   3515 C  CZ  . ARG B 1 177 ? -30.007 6.295   16.098  1.00 34.33 ? 177 ARG A CZ  1 
ATOM   3516 N  NH1 . ARG B 1 177 ? -30.520 7.511   16.215  1.00 22.91 ? 177 ARG A NH1 1 
ATOM   3517 N  NH2 . ARG B 1 177 ? -30.617 5.258   16.657  1.00 33.65 ? 177 ARG A NH2 1 
ATOM   3518 N  N   . PHE B 1 178 ? -25.383 2.782   12.806  1.00 21.80 ? 178 PHE A N   1 
ATOM   3519 C  CA  . PHE B 1 178 ? -25.240 1.510   12.130  1.00 19.09 ? 178 PHE A CA  1 
ATOM   3520 C  C   . PHE B 1 178 ? -25.594 0.422   13.151  1.00 19.11 ? 178 PHE A C   1 
ATOM   3521 O  O   . PHE B 1 178 ? -24.933 0.280   14.187  1.00 18.83 ? 178 PHE A O   1 
ATOM   3522 C  CB  . PHE B 1 178 ? -23.760 1.351   11.684  1.00 23.05 ? 178 PHE A CB  1 
ATOM   3523 C  CG  . PHE B 1 178 ? -23.472 0.075   10.990  1.00 22.15 ? 178 PHE A CG  1 
ATOM   3524 C  CD1 . PHE B 1 178 ? -23.642 -0.034  9.627   1.00 20.19 ? 178 PHE A CD1 1 
ATOM   3525 C  CD2 . PHE B 1 178 ? -22.998 -1.016  11.715  1.00 20.01 ? 178 PHE A CD2 1 
ATOM   3526 C  CE1 . PHE B 1 178 ? -23.397 -1.238  8.963   1.00 22.83 ? 178 PHE A CE1 1 
ATOM   3527 C  CE2 . PHE B 1 178 ? -22.740 -2.213  11.029  1.00 20.12 ? 178 PHE A CE2 1 
ATOM   3528 C  CZ  . PHE B 1 178 ? -22.926 -2.324  9.701   1.00 21.86 ? 178 PHE A CZ  1 
ATOM   3529 N  N   . THR B 1 179 ? -26.669 -0.307  12.882  1.00 19.85 ? 179 THR A N   1 
ATOM   3530 C  CA  . THR B 1 179 ? -27.079 -1.357  13.856  1.00 24.50 ? 179 THR A CA  1 
ATOM   3531 C  C   . THR B 1 179 ? -27.680 -2.538  13.137  1.00 23.97 ? 179 THR A C   1 
ATOM   3532 O  O   . THR B 1 179 ? -27.714 -2.582  11.916  1.00 24.50 ? 179 THR A O   1 
ATOM   3533 C  CB  . THR B 1 179 ? -28.017 -0.815  14.929  1.00 27.19 ? 179 THR A CB  1 
ATOM   3534 O  OG1 . THR B 1 179 ? -28.052 -1.736  16.069  1.00 25.61 ? 179 THR A OG1 1 
ATOM   3535 C  CG2 . THR B 1 179 ? -29.427 -0.558  14.329  1.00 27.63 ? 179 THR A CG2 1 
ATOM   3536 N  N   A ASN B 1 180 ? -28.198 -3.535  13.849  0.50 23.92 ? 180 ASN A N   1 
ATOM   3537 N  N   B ASN B 1 180 ? -28.096 -3.479  13.989  0.50 24.97 ? 180 ASN A N   1 
ATOM   3538 C  CA  A ASN B 1 180 ? -28.595 -4.800  13.164  0.50 21.53 ? 180 ASN A CA  1 
ATOM   3539 C  CA  B ASN B 1 180 ? -28.613 -4.766  13.587  0.50 24.18 ? 180 ASN A CA  1 
ATOM   3540 C  C   A ASN B 1 180 ? -27.495 -5.433  12.330  0.50 21.86 ? 180 ASN A C   1 
ATOM   3541 C  C   B ASN B 1 180 ? -27.639 -5.443  12.561  0.50 23.64 ? 180 ASN A C   1 
ATOM   3542 O  O   A ASN B 1 180 ? -27.655 -5.733  11.123  0.50 22.92 ? 180 ASN A O   1 
ATOM   3543 O  O   B ASN B 1 180 ? -28.045 -5.747  11.448  0.50 27.00 ? 180 ASN A O   1 
ATOM   3544 C  CB  A ASN B 1 180 ? -29.816 -4.626  12.269  0.50 23.03 ? 180 ASN A CB  1 
ATOM   3545 C  CB  B ASN B 1 180 ? -30.077 -4.576  13.112  0.50 26.09 ? 180 ASN A CB  1 
ATOM   3546 C  CG  A ASN B 1 180 ? -30.528 -5.944  12.055  0.50 23.66 ? 180 ASN A CG  1 
ATOM   3547 C  CG  B ASN B 1 180 ? -31.005 -3.918  14.172  0.50 24.84 ? 180 ASN A CG  1 
ATOM   3548 O  OD1 A ASN B 1 180 ? -30.465 -6.822  12.924  0.50 22.69 ? 180 ASN A OD1 1 
ATOM   3549 O  OD1 B ASN B 1 180 ? -30.925 -4.136  15.395  0.50 24.08 ? 180 ASN A OD1 1 
ATOM   3550 N  ND2 A ASN B 1 180 ? -31.180 -6.107  10.908  0.50 24.79 ? 180 ASN A ND2 1 
ATOM   3551 N  ND2 B ASN B 1 180 ? -31.894 -3.068  13.676  0.50 27.68 ? 180 ASN A ND2 1 
ATOM   3552 N  N   . PHE B 1 181 ? -26.357 -5.661  12.962  1.00 18.97 ? 181 PHE A N   1 
ATOM   3553 C  CA  . PHE B 1 181 ? -25.262 -6.277  12.194  1.00 20.28 ? 181 PHE A CA  1 
ATOM   3554 C  C   . PHE B 1 181 ? -25.004 -7.676  12.740  1.00 18.33 ? 181 PHE A C   1 
ATOM   3555 O  O   . PHE B 1 181 ? -24.650 -7.816  13.932  1.00 20.13 ? 181 PHE A O   1 
ATOM   3556 C  CB  . PHE B 1 181 ? -24.006 -5.396  12.397  1.00 19.96 ? 181 PHE A CB  1 
ATOM   3557 C  CG  . PHE B 1 181 ? -22.749 -5.909  11.775  1.00 22.89 ? 181 PHE A CG  1 
ATOM   3558 C  CD1 . PHE B 1 181 ? -22.719 -6.308  10.425  1.00 26.63 ? 181 PHE A CD1 1 
ATOM   3559 C  CD2 . PHE B 1 181 ? -21.529 -5.796  12.492  1.00 22.59 ? 181 PHE A CD2 1 
ATOM   3560 C  CE1 . PHE B 1 181 ? -21.525 -6.728  9.833   1.00 28.36 ? 181 PHE A CE1 1 
ATOM   3561 C  CE2 . PHE B 1 181 ? -20.340 -6.179  11.899  1.00 26.35 ? 181 PHE A CE2 1 
ATOM   3562 C  CZ  . PHE B 1 181 ? -20.328 -6.669  10.569  1.00 26.46 ? 181 PHE A CZ  1 
ATOM   3563 N  N   . ASP B 1 182 ? -25.269 -8.680  11.904  1.00 16.63 ? 182 ASP A N   1 
ATOM   3564 C  CA  . ASP B 1 182 ? -25.300 -10.047 12.461  1.00 17.39 ? 182 ASP A CA  1 
ATOM   3565 C  C   . ASP B 1 182 ? -23.876 -10.594 12.301  1.00 15.99 ? 182 ASP A C   1 
ATOM   3566 O  O   . ASP B 1 182 ? -23.556 -11.348 11.386  1.00 16.99 ? 182 ASP A O   1 
ATOM   3567 C  CB  . ASP B 1 182 ? -26.345 -10.883 11.668  1.00 18.34 ? 182 ASP A CB  1 
ATOM   3568 C  CG  . ASP B 1 182 ? -26.531 -12.265 12.275  1.00 20.64 ? 182 ASP A CG  1 
ATOM   3569 O  OD1 . ASP B 1 182 ? -25.704 -12.674 13.149  1.00 19.63 ? 182 ASP A OD1 1 
ATOM   3570 O  OD2 . ASP B 1 182 ? -27.519 -12.940 11.892  1.00 20.04 ? 182 ASP A OD2 1 
ATOM   3571 N  N   . LEU B 1 183 ? -22.998 -10.201 13.228  1.00 16.42 ? 183 LEU A N   1 
ATOM   3572 C  CA  . LEU B 1 183 ? -21.615 -10.507 13.129  1.00 16.24 ? 183 LEU A CA  1 
ATOM   3573 C  C   . LEU B 1 183 ? -21.422 -12.040 13.206  1.00 15.88 ? 183 LEU A C   1 
ATOM   3574 O  O   . LEU B 1 183 ? -20.511 -12.621 12.586  1.00 15.00 ? 183 LEU A O   1 
ATOM   3575 C  CB  . LEU B 1 183 ? -20.876 -9.755  14.303  1.00 14.79 ? 183 LEU A CB  1 
ATOM   3576 C  CG  . LEU B 1 183 ? -19.382 -9.997  14.356  1.00 14.30 ? 183 LEU A CG  1 
ATOM   3577 C  CD1 . LEU B 1 183 ? -18.643 -9.646  13.032  1.00 14.85 ? 183 LEU A CD1 1 
ATOM   3578 C  CD2 . LEU B 1 183 ? -18.838 -9.220  15.583  1.00 13.93 ? 183 LEU A CD2 1 
ATOM   3579 N  N   . LEU B 1 184 ? -22.301 -12.731 13.987  1.00 14.94 ? 184 LEU A N   1 
ATOM   3580 C  CA  . LEU B 1 184 ? -22.117 -14.161 14.113  1.00 16.40 ? 184 LEU A CA  1 
ATOM   3581 C  C   . LEU B 1 184 ? -22.277 -14.837 12.768  1.00 14.71 ? 184 LEU A C   1 
ATOM   3582 O  O   . LEU B 1 184 ? -21.532 -15.744 12.434  1.00 16.03 ? 184 LEU A O   1 
ATOM   3583 C  CB  . LEU B 1 184 ? -23.134 -14.759 15.199  1.00 16.30 ? 184 LEU A CB  1 
ATOM   3584 C  CG  . LEU B 1 184 ? -22.946 -16.247 15.588  1.00 15.80 ? 184 LEU A CG  1 
ATOM   3585 C  CD1 . LEU B 1 184 ? -21.618 -16.460 16.292  1.00 19.15 ? 184 LEU A CD1 1 
ATOM   3586 C  CD2 . LEU B 1 184 ? -24.086 -16.802 16.449  1.00 17.71 ? 184 LEU A CD2 1 
ATOM   3587 N  N   A SER B 1 185 ? -23.284 -14.423 12.005  0.50 15.76 ? 185 SER A N   1 
ATOM   3588 N  N   B SER B 1 185 ? -23.295 -14.435 12.009  0.50 15.76 ? 185 SER A N   1 
ATOM   3589 C  CA  A SER B 1 185 ? -23.502 -15.049 10.688  0.50 15.83 ? 185 SER A CA  1 
ATOM   3590 C  CA  B SER B 1 185 ? -23.499 -15.073 10.694  0.50 15.79 ? 185 SER A CA  1 
ATOM   3591 C  C   A SER B 1 185 ? -22.503 -14.646 9.640   0.50 16.44 ? 185 SER A C   1 
ATOM   3592 C  C   B SER B 1 185 ? -22.418 -14.747 9.698   0.50 16.34 ? 185 SER A C   1 
ATOM   3593 O  O   A SER B 1 185 ? -22.482 -15.199 8.586   0.50 17.72 ? 185 SER A O   1 
ATOM   3594 O  O   B SER B 1 185 ? -22.238 -15.489 8.752   0.50 16.94 ? 185 SER A O   1 
ATOM   3595 C  CB  A SER B 1 185 ? -24.890 -14.645 10.142  0.50 17.71 ? 185 SER A CB  1 
ATOM   3596 C  CB  B SER B 1 185 ? -24.859 -14.650 10.063  0.50 18.01 ? 185 SER A CB  1 
ATOM   3597 O  OG  A SER B 1 185 ? -25.879 -14.949 11.100  0.50 19.45 ? 185 SER A OG  1 
ATOM   3598 O  OG  B SER B 1 185 ? -24.900 -13.262 9.793   0.50 20.47 ? 185 SER A OG  1 
ATOM   3599 N  N   . LEU B 1 186 ? -21.690 -13.658 9.927   1.00 16.06 ? 186 LEU A N   1 
ATOM   3600 C  CA  . LEU B 1 186 ? -20.631 -13.268 8.988   1.00 14.23 ? 186 LEU A CA  1 
ATOM   3601 C  C   . LEU B 1 186 ? -19.437 -14.235 9.121   1.00 14.09 ? 186 LEU A C   1 
ATOM   3602 O  O   . LEU B 1 186 ? -18.666 -14.407 8.168   1.00 13.80 ? 186 LEU A O   1 
ATOM   3603 C  CB  . LEU B 1 186 ? -20.225 -11.814 9.306   1.00 13.45 ? 186 LEU A CB  1 
ATOM   3604 C  CG  . LEU B 1 186 ? -19.083 -11.163 8.546   1.00 17.39 ? 186 LEU A CG  1 
ATOM   3605 C  CD1 . LEU B 1 186 ? -19.660 -10.833 7.145   1.00 15.31 ? 186 LEU A CD1 1 
ATOM   3606 C  CD2 . LEU B 1 186 ? -18.561 -9.886  9.184   1.00 16.84 ? 186 LEU A CD2 1 
ATOM   3607 N  N   . LEU B 1 187 ? -19.258 -14.865 10.282  1.00 12.54 ? 187 LEU A N   1 
ATOM   3608 C  CA  . LEU B 1 187 ? -18.122 -15.803 10.366  1.00 12.46 ? 187 LEU A CA  1 
ATOM   3609 C  C   . LEU B 1 187 ? -18.148 -17.041 9.464   1.00 13.87 ? 187 LEU A C   1 
ATOM   3610 O  O   . LEU B 1 187 ? -19.257 -17.439 8.985   1.00 14.04 ? 187 LEU A O   1 
ATOM   3611 C  CB  . LEU B 1 187 ? -17.949 -16.252 11.861  1.00 11.55 ? 187 LEU A CB  1 
ATOM   3612 C  CG  . LEU B 1 187 ? -17.917 -15.094 12.835  1.00 12.89 ? 187 LEU A CG  1 
ATOM   3613 C  CD1 . LEU B 1 187 ? -17.804 -15.746 14.228  1.00 13.65 ? 187 LEU A CD1 1 
ATOM   3614 C  CD2 . LEU B 1 187 ? -16.684 -14.152 12.598  1.00 13.65 ? 187 LEU A CD2 1 
ATOM   3615 N  N   . PRO B 1 188 ? -16.975 -17.585 9.087   1.00 12.48 ? 188 PRO A N   1 
ATOM   3616 C  CA  . PRO B 1 188 ? -16.944 -18.694 8.145   1.00 13.67 ? 188 PRO A CA  1 
ATOM   3617 C  C   . PRO B 1 188 ? -17.554 -19.963 8.767   1.00 15.75 ? 188 PRO A C   1 
ATOM   3618 O  O   . PRO B 1 188 ? -17.759 -20.021 9.971   1.00 15.31 ? 188 PRO A O   1 
ATOM   3619 C  CB  . PRO B 1 188 ? -15.432 -18.894 7.871   1.00 14.16 ? 188 PRO A CB  1 
ATOM   3620 C  CG  . PRO B 1 188 ? -14.773 -18.293 9.132   1.00 15.18 ? 188 PRO A CG  1 
ATOM   3621 C  CD  . PRO B 1 188 ? -15.621 -17.176 9.504   1.00 13.07 ? 188 PRO A CD  1 
ATOM   3622 N  N   . PRO B 1 189 ? -17.872 -20.947 7.918   1.00 14.36 ? 189 PRO A N   1 
ATOM   3623 C  CA  . PRO B 1 189 ? -18.419 -22.211 8.462   1.00 17.11 ? 189 PRO A CA  1 
ATOM   3624 C  C   . PRO B 1 189 ? -17.536 -22.864 9.569   1.00 16.86 ? 189 PRO A C   1 
ATOM   3625 O  O   . PRO B 1 189 ? -18.059 -23.309 10.629  1.00 17.92 ? 189 PRO A O   1 
ATOM   3626 C  CB  . PRO B 1 189 ? -18.535 -23.098 7.177   1.00 19.43 ? 189 PRO A CB  1 
ATOM   3627 C  CG  . PRO B 1 189 ? -18.741 -22.107 6.074   1.00 18.20 ? 189 PRO A CG  1 
ATOM   3628 C  CD  . PRO B 1 189 ? -17.802 -20.942 6.429   1.00 17.92 ? 189 PRO A CD  1 
ATOM   3629 N  N   . SER B 1 190 ? -16.205 -22.877 9.350   1.00 15.54 ? 190 SER A N   1 
ATOM   3630 C  CA  . SER B 1 190 ? -15.335 -23.539 10.280  1.00 14.37 ? 190 SER A CA  1 
ATOM   3631 C  C   . SER B 1 190 ? -14.700 -22.497 11.195  1.00 18.41 ? 190 SER A C   1 
ATOM   3632 O  O   . SER B 1 190 ? -14.251 -21.454 10.690  1.00 15.40 ? 190 SER A O   1 
ATOM   3633 C  CB  . SER B 1 190 ? -14.202 -24.268 9.469   1.00 16.37 ? 190 SER A CB  1 
ATOM   3634 O  OG  . SER B 1 190 ? -13.203 -24.758 10.375  1.00 18.42 ? 190 SER A OG  1 
ATOM   3635 N  N   . TRP B 1 191 ? -14.663 -22.755 12.515  1.00 15.70 ? 191 TRP A N   1 
ATOM   3636 C  CA  . TRP B 1 191 ? -13.946 -21.897 13.435  1.00 14.89 ? 191 TRP A CA  1 
ATOM   3637 C  C   . TRP B 1 191 ? -12.683 -22.514 13.963  1.00 14.88 ? 191 TRP A C   1 
ATOM   3638 O  O   . TRP B 1 191 ? -12.234 -22.128 15.044  1.00 17.90 ? 191 TRP A O   1 
ATOM   3639 C  CB  . TRP B 1 191 ? -14.880 -21.520 14.560  1.00 14.69 ? 191 TRP A CB  1 
ATOM   3640 C  CG  . TRP B 1 191 ? -16.136 -20.767 14.087  1.00 14.21 ? 191 TRP A CG  1 
ATOM   3641 C  CD1 . TRP B 1 191 ? -16.373 -20.144 12.857  1.00 14.87 ? 191 TRP A CD1 1 
ATOM   3642 C  CD2 . TRP B 1 191 ? -17.322 -20.518 14.906  1.00 15.18 ? 191 TRP A CD2 1 
ATOM   3643 N  NE1 . TRP B 1 191 ? -17.633 -19.549 12.848  1.00 14.59 ? 191 TRP A NE1 1 
ATOM   3644 C  CE2 . TRP B 1 191 ? -18.231 -19.719 14.107  1.00 13.66 ? 191 TRP A CE2 1 
ATOM   3645 C  CE3 . TRP B 1 191 ? -17.715 -20.922 16.197  1.00 16.40 ? 191 TRP A CE3 1 
ATOM   3646 C  CZ2 . TRP B 1 191 ? -19.490 -19.347 14.561  1.00 19.29 ? 191 TRP A CZ2 1 
ATOM   3647 C  CZ3 . TRP B 1 191 ? -18.940 -20.496 16.668  1.00 17.57 ? 191 TRP A CZ3 1 
ATOM   3648 C  CH2 . TRP B 1 191 ? -19.841 -19.754 15.874  1.00 19.12 ? 191 TRP A CH2 1 
ATOM   3649 N  N   . ASP B 1 192 ? -12.067 -23.418 13.202  1.00 16.45 ? 192 ASP A N   1 
ATOM   3650 C  CA  . ASP B 1 192 ? -10.716 -23.874 13.542  1.00 15.03 ? 192 ASP A CA  1 
ATOM   3651 C  C   . ASP B 1 192 ? -9.728  -22.652 13.433  1.00 14.42 ? 192 ASP A C   1 
ATOM   3652 O  O   . ASP B 1 192 ? -9.887  -21.775 12.565  1.00 13.90 ? 192 ASP A O   1 
ATOM   3653 C  CB  . ASP B 1 192 ? -10.308 -25.001 12.649  1.00 19.02 ? 192 ASP A CB  1 
ATOM   3654 C  CG  . ASP B 1 192 ? -11.161 -26.259 12.945  1.00 18.21 ? 192 ASP A CG  1 
ATOM   3655 O  OD1 . ASP B 1 192 ? -11.920 -26.330 13.989  1.00 22.45 ? 192 ASP A OD1 1 
ATOM   3656 O  OD2 . ASP B 1 192 ? -11.154 -27.067 12.071  1.00 23.21 ? 192 ASP A OD2 1 
ATOM   3657 N  N   . TYR B 1 193 ? -8.789  -22.548 14.402  1.00 11.87 ? 193 TYR A N   1 
ATOM   3658 C  CA  . TYR B 1 193 ? -8.026  -21.316 14.539  1.00 11.88 ? 193 TYR A CA  1 
ATOM   3659 C  C   . TYR B 1 193 ? -6.604  -21.597 14.982  1.00 13.98 ? 193 TYR A C   1 
ATOM   3660 O  O   . TYR B 1 193 ? -6.331  -22.712 15.465  1.00 13.51 ? 193 TYR A O   1 
ATOM   3661 C  CB  . TYR B 1 193 ? -8.691  -20.341 15.578  1.00 13.35 ? 193 TYR A CB  1 
ATOM   3662 C  CG  . TYR B 1 193 ? -8.769  -20.905 16.995  1.00 12.25 ? 193 TYR A CG  1 
ATOM   3663 C  CD1 . TYR B 1 193 ? -7.669  -20.787 17.847  1.00 13.57 ? 193 TYR A CD1 1 
ATOM   3664 C  CD2 . TYR B 1 193 ? -9.864  -21.637 17.417  1.00 14.53 ? 193 TYR A CD2 1 
ATOM   3665 C  CE1 . TYR B 1 193 ? -7.712  -21.372 19.114  1.00 14.16 ? 193 TYR A CE1 1 
ATOM   3666 C  CE2 . TYR B 1 193 ? -9.927  -22.180 18.680  1.00 12.50 ? 193 TYR A CE2 1 
ATOM   3667 C  CZ  . TYR B 1 193 ? -8.829  -22.045 19.527  1.00 14.14 ? 193 TYR A CZ  1 
ATOM   3668 O  OH  . TYR B 1 193 ? -8.837  -22.627 20.797  1.00 14.33 ? 193 TYR A OH  1 
ATOM   3669 N  N   . TRP B 1 194 ? -5.763  -20.612 14.730  1.00 12.89 ? 194 TRP A N   1 
ATOM   3670 C  CA  . TRP B 1 194 ? -4.439  -20.547 15.324  1.00 12.12 ? 194 TRP A CA  1 
ATOM   3671 C  C   . TRP B 1 194 ? -4.445  -19.472 16.394  1.00 13.05 ? 194 TRP A C   1 
ATOM   3672 O  O   . TRP B 1 194 ? -5.218  -18.472 16.338  1.00 13.53 ? 194 TRP A O   1 
ATOM   3673 C  CB  . TRP B 1 194 ? -3.392  -20.157 14.271  1.00 13.99 ? 194 TRP A CB  1 
ATOM   3674 C  CG  . TRP B 1 194 ? -3.305  -21.130 13.132  1.00 13.12 ? 194 TRP A CG  1 
ATOM   3675 C  CD1 . TRP B 1 194 ? -2.721  -22.399 13.153  1.00 13.70 ? 194 TRP A CD1 1 
ATOM   3676 C  CD2 . TRP B 1 194 ? -3.778  -20.953 11.785  1.00 13.72 ? 194 TRP A CD2 1 
ATOM   3677 N  NE1 . TRP B 1 194 ? -2.793  -22.971 11.922  1.00 14.35 ? 194 TRP A NE1 1 
ATOM   3678 C  CE2 . TRP B 1 194 ? -3.422  -22.149 11.064  1.00 14.75 ? 194 TRP A CE2 1 
ATOM   3679 C  CE3 . TRP B 1 194 ? -4.427  -19.902 11.105  1.00 14.28 ? 194 TRP A CE3 1 
ATOM   3680 C  CZ2 . TRP B 1 194 ? -3.743  -22.323 9.698   1.00 14.66 ? 194 TRP A CZ2 1 
ATOM   3681 C  CZ3 . TRP B 1 194 ? -4.694  -20.067 9.734   1.00 13.64 ? 194 TRP A CZ3 1 
ATOM   3682 C  CH2 . TRP B 1 194 ? -4.369  -21.237 9.062   1.00 14.46 ? 194 TRP A CH2 1 
ATOM   3683 N  N   . THR B 1 195 ? -3.571  -19.599 17.404  1.00 11.00 ? 195 THR A N   1 
ATOM   3684 C  CA  . THR B 1 195 ? -3.491  -18.577 18.415  1.00 10.77 ? 195 THR A CA  1 
ATOM   3685 C  C   . THR B 1 195 ? -2.080  -18.335 18.898  1.00 11.84 ? 195 THR A C   1 
ATOM   3686 O  O   . THR B 1 195 ? -1.293  -19.266 18.959  1.00 13.10 ? 195 THR A O   1 
ATOM   3687 C  CB  . THR B 1 195 ? -4.442  -18.923 19.651  1.00 11.94 ? 195 THR A CB  1 
ATOM   3688 O  OG1 . THR B 1 195 ? -4.425  -17.924 20.637  1.00 12.35 ? 195 THR A OG1 1 
ATOM   3689 C  CG2 . THR B 1 195 ? -3.985  -20.317 20.347  1.00 13.56 ? 195 THR A CG2 1 
ATOM   3690 N  N   . TYR B 1 196 ? -1.804  -17.108 19.266  1.00 12.23 ? 196 TYR A N   1 
ATOM   3691 C  CA  . TYR B 1 196 ? -0.489  -16.748 19.835  1.00 11.89 ? 196 TYR A CA  1 
ATOM   3692 C  C   . TYR B 1 196 ? -0.630  -15.451 20.568  1.00 11.86 ? 196 TYR A C   1 
ATOM   3693 O  O   . TYR B 1 196 ? -1.556  -14.630 20.344  1.00 11.69 ? 196 TYR A O   1 
ATOM   3694 C  CB  . TYR B 1 196 ? 0.575   -16.652 18.702  1.00 11.30 ? 196 TYR A CB  1 
ATOM   3695 C  CG  . TYR B 1 196 ? 0.370   -15.402 17.842  1.00 11.51 ? 196 TYR A CG  1 
ATOM   3696 C  CD1 . TYR B 1 196 ? -0.622  -15.402 16.818  1.00 11.05 ? 196 TYR A CD1 1 
ATOM   3697 C  CD2 . TYR B 1 196 ? 1.178   -14.277 18.028  1.00 13.06 ? 196 TYR A CD2 1 
ATOM   3698 C  CE1 . TYR B 1 196 ? -0.809  -14.206 16.056  1.00 10.60 ? 196 TYR A CE1 1 
ATOM   3699 C  CE2 . TYR B 1 196 ? 0.996   -13.115 17.267  1.00 12.47 ? 196 TYR A CE2 1 
ATOM   3700 C  CZ  . TYR B 1 196 ? -0.024  -13.128 16.267  1.00 12.08 ? 196 TYR A CZ  1 
ATOM   3701 O  OH  . TYR B 1 196 ? -0.175  -11.932 15.555  1.00 12.19 ? 196 TYR A OH  1 
ATOM   3702 N  N   . PRO B 1 197 ? 0.308   -15.184 21.507  1.00 13.65 ? 197 PRO A N   1 
ATOM   3703 C  CA  . PRO B 1 197 ? 0.290   -13.921 22.172  1.00 12.34 ? 197 PRO A CA  1 
ATOM   3704 C  C   . PRO B 1 197 ? 0.946   -12.778 21.357  1.00 12.63 ? 197 PRO A C   1 
ATOM   3705 O  O   . PRO B 1 197 ? 2.046   -12.975 20.846  1.00 12.70 ? 197 PRO A O   1 
ATOM   3706 C  CB  . PRO B 1 197 ? 1.142   -14.235 23.461  1.00 13.37 ? 197 PRO A CB  1 
ATOM   3707 C  CG  . PRO B 1 197 ? 2.167   -15.250 22.909  1.00 13.04 ? 197 PRO A CG  1 
ATOM   3708 C  CD  . PRO B 1 197 ? 1.390   -16.114 21.919  1.00 13.33 ? 197 PRO A CD  1 
ATOM   3709 N  N   . GLY B 1 198 ? 0.284   -11.653 21.259  1.00 11.70 ? 198 GLY A N   1 
ATOM   3710 C  CA  . GLY B 1 198 ? 0.783   -10.510 20.449  1.00 11.95 ? 198 GLY A CA  1 
ATOM   3711 C  C   . GLY B 1 198 ? 0.292   -9.188  20.840  1.00 13.30 ? 198 GLY A C   1 
ATOM   3712 O  O   . GLY B 1 198 ? 0.141   -8.845  22.038  1.00 12.78 ? 198 GLY A O   1 
ATOM   3713 N  N   . SER B 1 199 ? 0.153   -8.348  19.816  1.00 11.45 ? 199 SER A N   1 
ATOM   3714 C  CA  . SER B 1 199 ? -0.024  -6.944  20.086  1.00 11.45 ? 199 SER A CA  1 
ATOM   3715 C  C   . SER B 1 199 ? -1.152  -6.324  19.240  1.00 11.70 ? 199 SER A C   1 
ATOM   3716 O  O   . SER B 1 199 ? -1.633  -6.946  18.259  1.00 10.67 ? 199 SER A O   1 
ATOM   3717 C  CB  . SER B 1 199 ? 1.265   -6.136  19.784  1.00 12.53 ? 199 SER A CB  1 
ATOM   3718 O  OG  . SER B 1 199 ? 1.458   -6.058  18.344  1.00 12.16 ? 199 SER A OG  1 
ATOM   3719 N  N   . LEU B 1 200 ? -1.510  -5.120  19.569  1.00 12.83 ? 200 LEU A N   1 
ATOM   3720 C  CA  . LEU B 1 200 ? -2.273  -4.290  18.598  1.00 12.47 ? 200 LEU A CA  1 
ATOM   3721 C  C   . LEU B 1 200 ? -1.365  -4.181  17.343  1.00 13.69 ? 200 LEU A C   1 
ATOM   3722 O  O   . LEU B 1 200 ? -0.155  -4.029  17.455  1.00 13.04 ? 200 LEU A O   1 
ATOM   3723 C  CB  . LEU B 1 200 ? -2.530  -2.861  19.093  1.00 12.36 ? 200 LEU A CB  1 
ATOM   3724 C  CG  . LEU B 1 200 ? -3.261  -2.805  20.464  1.00 14.26 ? 200 LEU A CG  1 
ATOM   3725 C  CD1 . LEU B 1 200 ? -3.270  -1.325  20.838  1.00 14.54 ? 200 LEU A CD1 1 
ATOM   3726 C  CD2 . LEU B 1 200 ? -4.671  -3.321  20.360  1.00 13.49 ? 200 LEU A CD2 1 
ATOM   3727 N  N   . THR B 1 201 ? -1.987  -4.159  16.158  1.00 11.87 ? 201 THR A N   1 
ATOM   3728 C  CA  . THR B 1 201 ? -1.199  -3.958  14.928  1.00 11.65 ? 201 THR A CA  1 
ATOM   3729 C  C   . THR B 1 201 ? -1.199  -2.512  14.508  1.00 13.43 ? 201 THR A C   1 
ATOM   3730 O  O   . THR B 1 201 ? -0.732  -2.219  13.397  1.00 13.83 ? 201 THR A O   1 
ATOM   3731 C  CB  . THR B 1 201 ? -1.763  -4.824  13.776  1.00 11.52 ? 201 THR A CB  1 
ATOM   3732 O  OG1 . THR B 1 201 ? -3.037  -4.316  13.356  1.00 12.32 ? 201 THR A OG1 1 
ATOM   3733 C  CG2 . THR B 1 201 ? -1.851  -6.358  14.266  1.00 12.18 ? 201 THR A CG2 1 
ATOM   3734 N  N   . VAL B 1 202 ? -1.734  -1.596  15.331  1.00 13.69 ? 202 VAL A N   1 
ATOM   3735 C  CA  . VAL B 1 202 ? -1.700  -0.184  15.082  1.00 14.04 ? 202 VAL A CA  1 
ATOM   3736 C  C   . VAL B 1 202 ? -1.081  0.465   16.333  1.00 15.35 ? 202 VAL A C   1 
ATOM   3737 O  O   . VAL B 1 202 ? -1.214  -0.050  17.419  1.00 14.79 ? 202 VAL A O   1 
ATOM   3738 C  CB  . VAL B 1 202 ? -3.080  0.418   14.821  1.00 16.41 ? 202 VAL A CB  1 
ATOM   3739 C  CG1 . VAL B 1 202 ? -3.585  -0.069  13.454  1.00 16.62 ? 202 VAL A CG1 1 
ATOM   3740 C  CG2 . VAL B 1 202 ? -4.094  0.233   16.004  1.00 16.46 ? 202 VAL A CG2 1 
ATOM   3741 N  N   . PRO B 1 203 ? -0.416  1.601   16.198  1.00 16.20 ? 203 PRO A N   1 
ATOM   3742 C  CA  . PRO B 1 203 ? -0.084  2.359   17.371  1.00 17.44 ? 203 PRO A CA  1 
ATOM   3743 C  C   . PRO B 1 203 ? -1.332  2.525   18.288  1.00 15.48 ? 203 PRO A C   1 
ATOM   3744 O  O   . PRO B 1 203 ? -2.478  2.827   17.863  1.00 15.73 ? 203 PRO A O   1 
ATOM   3745 C  CB  . PRO B 1 203 ? 0.436   3.675   16.757  1.00 17.21 ? 203 PRO A CB  1 
ATOM   3746 C  CG  . PRO B 1 203 ? 1.006   3.258   15.431  1.00 16.62 ? 203 PRO A CG  1 
ATOM   3747 C  CD  . PRO B 1 203 ? -0.074  2.317   14.938  1.00 17.34 ? 203 PRO A CD  1 
ATOM   3748 N  N   . PRO B 1 204 ? -1.112  2.377   19.638  1.00 18.38 ? 204 PRO A N   1 
ATOM   3749 C  CA  . PRO B 1 204 ? 0.146   2.327   20.385  1.00 17.84 ? 204 PRO A CA  1 
ATOM   3750 C  C   . PRO B 1 204 ? 0.846   0.977   20.477  1.00 14.65 ? 204 PRO A C   1 
ATOM   3751 O  O   . PRO B 1 204 ? 1.854   0.813   21.207  1.00 15.44 ? 204 PRO A O   1 
ATOM   3752 C  CB  . PRO B 1 204 ? -0.316  2.816   21.814  1.00 17.86 ? 204 PRO A CB  1 
ATOM   3753 C  CG  . PRO B 1 204 ? -1.675  2.230   21.921  1.00 18.28 ? 204 PRO A CG  1 
ATOM   3754 C  CD  . PRO B 1 204 ? -2.269  2.516   20.545  1.00 19.00 ? 204 PRO A CD  1 
ATOM   3755 N  N   . LEU B 1 205 ? 0.376   -0.054  19.681  1.00 14.74 ? 205 LEU A N   1 
ATOM   3756 C  CA  . LEU B 1 205 ? 1.128   -1.325  19.528  1.00 12.54 ? 205 LEU A CA  1 
ATOM   3757 C  C   . LEU B 1 205 ? 1.333   -2.122  20.825  1.00 12.79 ? 205 LEU A C   1 
ATOM   3758 O  O   . LEU B 1 205 ? 2.216   -2.965  20.936  1.00 12.87 ? 205 LEU A O   1 
ATOM   3759 C  CB  . LEU B 1 205 ? 2.512   -1.164  18.803  1.00 15.82 ? 205 LEU A CB  1 
ATOM   3760 C  CG  . LEU B 1 205 ? 2.361   -0.496  17.408  1.00 16.65 ? 205 LEU A CG  1 
ATOM   3761 C  CD1 . LEU B 1 205 ? 3.804   -0.079  16.955  1.00 16.39 ? 205 LEU A CD1 1 
ATOM   3762 C  CD2 . LEU B 1 205 ? 1.694   -1.439  16.374  1.00 15.43 ? 205 LEU A CD2 1 
ATOM   3763 N  N   . LEU B 1 206 ? 0.366   -1.927  21.734  1.00 15.34 ? 206 LEU A N   1 
ATOM   3764 C  CA  . LEU B 1 206 ? 0.480   -2.513  23.107  1.00 14.49 ? 206 LEU A CA  1 
ATOM   3765 C  C   . LEU B 1 206 ? 0.403   -4.042  23.050  1.00 15.58 ? 206 LEU A C   1 
ATOM   3766 O  O   . LEU B 1 206 ? -0.405  -4.601  22.262  1.00 14.97 ? 206 LEU A O   1 
ATOM   3767 C  CB  . LEU B 1 206 ? -0.722  -2.038  23.945  1.00 14.82 ? 206 LEU A CB  1 
ATOM   3768 C  CG  . LEU B 1 206 ? -0.700  -0.568  24.245  1.00 17.32 ? 206 LEU A CG  1 
ATOM   3769 C  CD1 . LEU B 1 206 ? -2.020  -0.110  24.807  1.00 17.88 ? 206 LEU A CD1 1 
ATOM   3770 C  CD2 . LEU B 1 206 ? 0.511   -0.194  25.149  1.00 20.54 ? 206 LEU A CD2 1 
ATOM   3771 N  N   . GLU B 1 207 ? 1.204   -4.755  23.842  1.00 14.06 ? 207 GLU A N   1 
ATOM   3772 C  CA  . GLU B 1 207 ? 1.364   -6.186  23.798  1.00 14.10 ? 207 GLU A CA  1 
ATOM   3773 C  C   . GLU B 1 207 ? 0.368   -6.840  24.779  1.00 15.82 ? 207 GLU A C   1 
ATOM   3774 O  O   . GLU B 1 207 ? 0.756   -7.391  25.804  1.00 15.17 ? 207 GLU A O   1 
ATOM   3775 C  CB  . GLU B 1 207 ? 2.818   -6.550  24.103  1.00 17.47 ? 207 GLU A CB  1 
ATOM   3776 C  CG  . GLU B 1 207 ? 3.681   -5.979  22.977  1.00 18.04 ? 207 GLU A CG  1 
ATOM   3777 C  CD  . GLU B 1 207 ? 5.150   -6.391  23.061  1.00 24.15 ? 207 GLU A CD  1 
ATOM   3778 O  OE1 . GLU B 1 207 ? 5.713   -6.701  24.209  1.00 20.23 ? 207 GLU A OE1 1 
ATOM   3779 O  OE2 . GLU B 1 207 ? 5.773   -6.406  21.963  1.00 19.80 ? 207 GLU A OE2 1 
ATOM   3780 N  N   . SER B 1 208 ? -0.905  -6.702  24.463  1.00 13.67 ? 208 SER A N   1 
ATOM   3781 C  CA  . SER B 1 208 ? -2.013  -7.052  25.366  1.00 12.77 ? 208 SER A CA  1 
ATOM   3782 C  C   . SER B 1 208 ? -2.993  -7.934  24.624  1.00 11.83 ? 208 SER A C   1 
ATOM   3783 O  O   . SER B 1 208 ? -4.112  -8.182  25.107  1.00 13.50 ? 208 SER A O   1 
ATOM   3784 C  CB  . SER B 1 208 ? -2.679  -5.766  25.782  1.00 14.61 ? 208 SER A CB  1 
ATOM   3785 O  OG  . SER B 1 208 ? -3.098  -4.961  24.626  1.00 17.45 ? 208 SER A OG  1 
ATOM   3786 N  N   . VAL B 1 209 ? -2.606  -8.502  23.472  1.00 10.58 ? 209 VAL A N   1 
ATOM   3787 C  CA  . VAL B 1 209 ? -3.676  -9.151  22.694  1.00 11.00 ? 209 VAL A CA  1 
ATOM   3788 C  C   . VAL B 1 209 ? -3.417  -10.651 22.578  1.00 9.72  ? 209 VAL A C   1 
ATOM   3789 O  O   . VAL B 1 209 ? -2.317  -11.156 22.216  1.00 11.81 ? 209 VAL A O   1 
ATOM   3790 C  CB  . VAL B 1 209 ? -3.692  -8.606  21.231  1.00 9.70  ? 209 VAL A CB  1 
ATOM   3791 C  CG1 . VAL B 1 209 ? -4.718  -9.448  20.453  1.00 10.23 ? 209 VAL A CG1 1 
ATOM   3792 C  CG2 . VAL B 1 209 ? -4.045  -7.089  21.237  1.00 10.87 ? 209 VAL A CG2 1 
ATOM   3793 N  N   . THR B 1 210 ? -4.435  -11.494 22.911  1.00 10.77 ? 210 THR A N   1 
ATOM   3794 C  CA  . THR B 1 210 ? -4.433  -12.863 22.567  1.00 10.32 ? 210 THR A CA  1 
ATOM   3795 C  C   . THR B 1 210 ? -5.069  -12.921 21.174  1.00 10.70 ? 210 THR A C   1 
ATOM   3796 O  O   . THR B 1 210 ? -6.263  -12.687 21.029  1.00 11.63 ? 210 THR A O   1 
ATOM   3797 C  CB  . THR B 1 210 ? -5.332  -13.702 23.525  1.00 12.19 ? 210 THR A CB  1 
ATOM   3798 O  OG1 . THR B 1 210 ? -4.723  -13.566 24.841  1.00 13.88 ? 210 THR A OG1 1 
ATOM   3799 C  CG2 . THR B 1 210 ? -5.298  -15.224 23.171  1.00 11.73 ? 210 THR A CG2 1 
ATOM   3800 N  N   . TRP B 1 211 ? -4.234  -13.287 20.206  1.00 10.22 ? 211 TRP A N   1 
ATOM   3801 C  CA  . TRP B 1 211 ? -4.773  -13.397 18.846  1.00 9.78  ? 211 TRP A CA  1 
ATOM   3802 C  C   . TRP B 1 211 ? -5.395  -14.779 18.587  1.00 10.66 ? 211 TRP A C   1 
ATOM   3803 O  O   . TRP B 1 211 ? -4.840  -15.806 18.960  1.00 11.83 ? 211 TRP A O   1 
ATOM   3804 C  CB  . TRP B 1 211 ? -3.599  -13.251 17.889  1.00 9.37  ? 211 TRP A CB  1 
ATOM   3805 C  CG  . TRP B 1 211 ? -3.391  -11.787 17.649  1.00 9.97  ? 211 TRP A CG  1 
ATOM   3806 C  CD1 . TRP B 1 211 ? -2.489  -10.933 18.274  1.00 10.40 ? 211 TRP A CD1 1 
ATOM   3807 C  CD2 . TRP B 1 211 ? -4.176  -10.934 16.762  1.00 9.87  ? 211 TRP A CD2 1 
ATOM   3808 N  NE1 . TRP B 1 211 ? -2.635  -9.649  17.812  1.00 10.60 ? 211 TRP A NE1 1 
ATOM   3809 C  CE2 . TRP B 1 211 ? -3.632  -9.583  16.902  1.00 10.77 ? 211 TRP A CE2 1 
ATOM   3810 C  CE3 . TRP B 1 211 ? -5.221  -11.152 15.880  1.00 9.60  ? 211 TRP A CE3 1 
ATOM   3811 C  CZ2 . TRP B 1 211 ? -4.131  -8.516  16.179  1.00 9.60  ? 211 TRP A CZ2 1 
ATOM   3812 C  CZ3 . TRP B 1 211 ? -5.716  -10.070 15.158  1.00 9.11  ? 211 TRP A CZ3 1 
ATOM   3813 C  CH2 . TRP B 1 211 ? -5.184  -8.784  15.305  1.00 9.26  ? 211 TRP A CH2 1 
ATOM   3814 N  N   . ILE B 1 212 ? -6.536  -14.754 17.904  1.00 10.45 ? 212 ILE A N   1 
ATOM   3815 C  CA  . ILE B 1 212 ? -7.255  -15.984 17.516  1.00 10.75 ? 212 ILE A CA  1 
ATOM   3816 C  C   . ILE B 1 212 ? -7.504  -15.761 15.988  1.00 10.32 ? 212 ILE A C   1 
ATOM   3817 O  O   . ILE B 1 212 ? -8.372  -14.942 15.657  1.00 11.45 ? 212 ILE A O   1 
ATOM   3818 C  CB  . ILE B 1 212 ? -8.566  -16.108 18.303  1.00 11.86 ? 212 ILE A CB  1 
ATOM   3819 C  CG1 . ILE B 1 212 ? -8.274  -16.213 19.779  1.00 11.46 ? 212 ILE A CG1 1 
ATOM   3820 C  CG2 . ILE B 1 212 ? -9.327  -17.314 17.778  1.00 11.38 ? 212 ILE A CG2 1 
ATOM   3821 C  CD1 . ILE B 1 212 ? -9.531  -16.043 20.679  1.00 9.88  ? 212 ILE A CD1 1 
ATOM   3822 N  N   . VAL B 1 213 ? -6.806  -16.470 15.118  1.00 11.70 ? 213 VAL A N   1 
ATOM   3823 C  CA  . VAL B 1 213 ? -6.914  -16.208 13.670  1.00 10.50 ? 213 VAL A CA  1 
ATOM   3824 C  C   . VAL B 1 213 ? -7.583  -17.427 13.066  1.00 11.32 ? 213 VAL A C   1 
ATOM   3825 O  O   . VAL B 1 213 ? -7.085  -18.570 13.181  1.00 12.16 ? 213 VAL A O   1 
ATOM   3826 C  CB  . VAL B 1 213 ? -5.500  -16.051 13.091  1.00 11.85 ? 213 VAL A CB  1 
ATOM   3827 C  CG1 . VAL B 1 213 ? -5.579  -15.918 11.542  1.00 12.23 ? 213 VAL A CG1 1 
ATOM   3828 C  CG2 . VAL B 1 213 ? -4.800  -14.844 13.690  1.00 11.66 ? 213 VAL A CG2 1 
ATOM   3829 N  N   . LEU B 1 214 ? -8.743  -17.215 12.475  1.00 11.36 ? 214 LEU A N   1 
ATOM   3830 C  CA  . LEU B 1 214 ? -9.450  -18.348 11.847  1.00 11.74 ? 214 LEU A CA  1 
ATOM   3831 C  C   . LEU B 1 214 ? -8.806  -18.780 10.555  1.00 11.50 ? 214 LEU A C   1 
ATOM   3832 O  O   . LEU B 1 214 ? -8.362  -17.963 9.730   1.00 11.20 ? 214 LEU A O   1 
ATOM   3833 C  CB  . LEU B 1 214 ? -10.961 -17.971 11.506  1.00 11.21 ? 214 LEU A CB  1 
ATOM   3834 C  CG  . LEU B 1 214 ? -11.784 -17.557 12.704  1.00 11.12 ? 214 LEU A CG  1 
ATOM   3835 C  CD1 . LEU B 1 214 ? -13.265 -17.479 12.335  1.00 11.15 ? 214 LEU A CD1 1 
ATOM   3836 C  CD2 . LEU B 1 214 ? -11.680 -18.620 13.802  1.00 13.74 ? 214 LEU A CD2 1 
ATOM   3837 N  N   . LYS B 1 215 ? -8.724  -20.111 10.344  1.00 12.54 ? 215 LYS A N   1 
ATOM   3838 C  CA  . LYS B 1 215 ? -8.144  -20.635 9.096   1.00 13.95 ? 215 LYS A CA  1 
ATOM   3839 C  C   . LYS B 1 215 ? -8.960  -20.369 7.810   1.00 12.79 ? 215 LYS A C   1 
ATOM   3840 O  O   . LYS B 1 215 ? -8.368  -20.004 6.784   1.00 15.32 ? 215 LYS A O   1 
ATOM   3841 C  CB  . LYS B 1 215 ? -7.918  -22.154 9.271   1.00 14.70 ? 215 LYS A CB  1 
ATOM   3842 C  CG  . LYS B 1 215 ? -7.380  -22.782 7.978   1.00 16.15 ? 215 LYS A CG  1 
ATOM   3843 C  CD  . LYS B 1 215 ? -7.043  -24.245 8.237   1.00 18.63 ? 215 LYS A CD  1 
ATOM   3844 C  CE  . LYS B 1 215 ? -6.753  -24.856 6.898   1.00 23.33 ? 215 LYS A CE  1 
ATOM   3845 N  NZ  . LYS B 1 215 ? -6.327  -26.253 7.103   1.00 28.83 ? 215 LYS A NZ  1 
ATOM   3846 N  N   . GLN B 1 216 ? -10.253 -20.441 7.918   1.00 13.82 ? 216 GLN A N   1 
ATOM   3847 C  CA  . GLN B 1 216 ? -11.127 -20.384 6.723   1.00 13.39 ? 216 GLN A CA  1 
ATOM   3848 C  C   . GLN B 1 216 ? -11.500 -18.943 6.420   1.00 12.14 ? 216 GLN A C   1 
ATOM   3849 O  O   . GLN B 1 216 ? -12.084 -18.289 7.286   1.00 13.02 ? 216 GLN A O   1 
ATOM   3850 C  CB  . GLN B 1 216 ? -12.349 -21.219 6.919   1.00 14.66 ? 216 GLN A CB  1 
ATOM   3851 C  CG  . GLN B 1 216 ? -13.203 -21.189 5.675   1.00 14.75 ? 216 GLN A CG  1 
ATOM   3852 C  CD  . GLN B 1 216 ? -14.441 -22.140 5.701   1.00 18.60 ? 216 GLN A CD  1 
ATOM   3853 O  OE1 . GLN B 1 216 ? -14.898 -22.657 6.751   1.00 19.91 ? 216 GLN A OE1 1 
ATOM   3854 N  NE2 . GLN B 1 216 ? -14.958 -22.416 4.504   1.00 17.96 ? 216 GLN A NE2 1 
ATOM   3855 N  N   . PRO B 1 217 ? -11.204 -18.484 5.198   1.00 13.82 ? 217 PRO A N   1 
ATOM   3856 C  CA  . PRO B 1 217 ? -11.616 -17.139 4.842   1.00 14.07 ? 217 PRO A CA  1 
ATOM   3857 C  C   . PRO B 1 217 ? -13.145 -17.043 4.500   1.00 14.73 ? 217 PRO A C   1 
ATOM   3858 O  O   . PRO B 1 217 ? -13.800 -18.096 4.241   1.00 14.57 ? 217 PRO A O   1 
ATOM   3859 C  CB  . PRO B 1 217 ? -10.825 -16.866 3.532   1.00 16.17 ? 217 PRO A CB  1 
ATOM   3860 C  CG  . PRO B 1 217 ? -9.715  -17.922 3.556   1.00 21.76 ? 217 PRO A CG  1 
ATOM   3861 C  CD  . PRO B 1 217 ? -10.427 -19.127 4.102   1.00 15.57 ? 217 PRO A CD  1 
ATOM   3862 N  N   . ILE B 1 218 ? -13.676 -15.809 4.581   1.00 12.46 ? 218 ILE A N   1 
ATOM   3863 C  CA  . ILE B 1 218 ? -15.011 -15.459 4.014   1.00 13.05 ? 218 ILE A CA  1 
ATOM   3864 C  C   . ILE B 1 218 ? -14.813 -14.741 2.727   1.00 12.31 ? 218 ILE A C   1 
ATOM   3865 O  O   . ILE B 1 218 ? -13.700 -14.353 2.388   1.00 14.62 ? 218 ILE A O   1 
ATOM   3866 C  CB  . ILE B 1 218 ? -15.853 -14.649 5.014   1.00 12.56 ? 218 ILE A CB  1 
ATOM   3867 C  CG1 . ILE B 1 218 ? -15.239 -13.292 5.282   1.00 12.94 ? 218 ILE A CG1 1 
ATOM   3868 C  CG2 . ILE B 1 218 ? -15.931 -15.466 6.326   1.00 13.64 ? 218 ILE A CG2 1 
ATOM   3869 C  CD1 . ILE B 1 218 ? -16.061 -12.382 6.162   1.00 13.99 ? 218 ILE A CD1 1 
ATOM   3870 N  N   A ASN B 1 219 ? -15.887 -14.595 1.943   0.50 12.76 ? 219 ASN A N   1 
ATOM   3871 N  N   B ASN B 1 219 ? -15.939 -14.564 2.005   0.50 12.27 ? 219 ASN A N   1 
ATOM   3872 C  CA  A ASN B 1 219 ? -15.734 -13.971 0.635   0.50 13.15 ? 219 ASN A CA  1 
ATOM   3873 C  CA  B ASN B 1 219 ? -15.941 -13.893 0.705   0.50 12.69 ? 219 ASN A CA  1 
ATOM   3874 C  C   A ASN B 1 219 ? -16.205 -12.546 0.646   0.50 13.45 ? 219 ASN A C   1 
ATOM   3875 C  C   B ASN B 1 219 ? -16.227 -12.415 0.728   0.50 13.13 ? 219 ASN A C   1 
ATOM   3876 O  O   A ASN B 1 219 ? -17.044 -12.197 1.442   0.50 13.91 ? 219 ASN A O   1 
ATOM   3877 O  O   B ASN B 1 219 ? -16.951 -11.887 1.588   0.50 13.28 ? 219 ASN A O   1 
ATOM   3878 C  CB  A ASN B 1 219 ? -16.558 -14.783 -0.404  0.50 16.43 ? 219 ASN A CB  1 
ATOM   3879 C  CB  B ASN B 1 219 ? -16.998 -14.578 -0.261  0.50 14.16 ? 219 ASN A CB  1 
ATOM   3880 C  CG  A ASN B 1 219 ? -16.029 -16.178 -0.581  0.50 18.33 ? 219 ASN A CG  1 
ATOM   3881 C  CG  B ASN B 1 219 ? -18.390 -14.659 0.344   0.50 16.62 ? 219 ASN A CG  1 
ATOM   3882 O  OD1 A ASN B 1 219 ? -15.065 -16.410 -1.335  0.50 23.70 ? 219 ASN A OD1 1 
ATOM   3883 O  OD1 B ASN B 1 219 ? -19.370 -13.983 -0.123  0.50 18.87 ? 219 ASN A OD1 1 
ATOM   3884 N  ND2 A ASN B 1 219 ? -16.607 -17.117 0.150   0.50 22.15 ? 219 ASN A ND2 1 
ATOM   3885 N  ND2 B ASN B 1 219 ? -18.522 -15.485 1.393   0.50 16.59 ? 219 ASN A ND2 1 
ATOM   3886 N  N   . ILE B 1 220 ? -15.652 -11.713 -0.243  1.00 12.27 ? 220 ILE A N   1 
ATOM   3887 C  CA  . ILE B 1 220 ? -16.048 -10.396 -0.505  1.00 13.19 ? 220 ILE A CA  1 
ATOM   3888 C  C   . ILE B 1 220 ? -15.906 -10.179 -2.049  1.00 12.78 ? 220 ILE A C   1 
ATOM   3889 O  O   . ILE B 1 220 ? -15.003 -10.790 -2.635  1.00 13.26 ? 220 ILE A O   1 
ATOM   3890 C  CB  . ILE B 1 220 ? -15.176 -9.339  0.270   1.00 12.26 ? 220 ILE A CB  1 
ATOM   3891 C  CG1 . ILE B 1 220 ? -15.797 -7.934  0.166   1.00 13.22 ? 220 ILE A CG1 1 
ATOM   3892 C  CG2 . ILE B 1 220 ? -13.698 -9.422  -0.063  1.00 13.17 ? 220 ILE A CG2 1 
ATOM   3893 C  CD1 . ILE B 1 220 ? -15.113 -6.913  1.115   1.00 12.89 ? 220 ILE A CD1 1 
ATOM   3894 N  N   . SER B 1 221 ? -16.725 -9.344  -2.644  1.00 12.79 ? 221 SER A N   1 
ATOM   3895 C  CA  . SER B 1 221 ? -16.443 -9.148  -4.090  1.00 13.07 ? 221 SER A CA  1 
ATOM   3896 C  C   . SER B 1 221 ? -15.335 -8.121  -4.239  1.00 12.60 ? 221 SER A C   1 
ATOM   3897 O  O   . SER B 1 221 ? -15.093 -7.268  -3.343  1.00 12.69 ? 221 SER A O   1 
ATOM   3898 C  CB  . SER B 1 221 ? -17.686 -8.639  -4.860  1.00 11.77 ? 221 SER A CB  1 
ATOM   3899 O  OG  . SER B 1 221 ? -18.015 -7.330  -4.509  1.00 14.20 ? 221 SER A OG  1 
ATOM   3900 N  N   A SER B 1 222 ? -14.698 -8.161  -5.419  0.50 13.61 ? 222 SER A N   1 
ATOM   3901 N  N   B SER B 1 222 ? -14.674 -8.116  -5.416  0.50 12.37 ? 222 SER A N   1 
ATOM   3902 C  CA  A SER B 1 222 ? -13.726 -7.111  -5.702  0.50 15.51 ? 222 SER A CA  1 
ATOM   3903 C  CA  B SER B 1 222 ? -13.701 -7.012  -5.649  0.50 13.06 ? 222 SER A CA  1 
ATOM   3904 C  C   A SER B 1 222 ? -14.302 -5.702  -5.650  0.50 14.61 ? 222 SER A C   1 
ATOM   3905 C  C   B SER B 1 222 ? -14.327 -5.643  -5.598  0.50 13.24 ? 222 SER A C   1 
ATOM   3906 O  O   A SER B 1 222 ? -13.590 -4.799  -5.208  0.50 14.29 ? 222 SER A O   1 
ATOM   3907 O  O   B SER B 1 222 ? -13.687 -4.701  -5.137  0.50 12.92 ? 222 SER A O   1 
ATOM   3908 C  CB  A SER B 1 222 ? -13.011 -7.379  -7.035  0.50 16.85 ? 222 SER A CB  1 
ATOM   3909 C  CB  B SER B 1 222 ? -12.950 -7.177  -6.981  0.50 12.40 ? 222 SER A CB  1 
ATOM   3910 O  OG  A SER B 1 222 ? -12.055 -6.384  -7.251  0.50 21.71 ? 222 SER A OG  1 
ATOM   3911 O  OG  B SER B 1 222 ? -13.870 -7.205  -8.066  0.50 12.95 ? 222 SER A OG  1 
ATOM   3912 N  N   . GLN B 1 223 ? -15.566 -5.486  -6.098  1.00 14.18 ? 223 GLN A N   1 
ATOM   3913 C  CA  . GLN B 1 223 ? -16.155 -4.146  -6.032  1.00 15.87 ? 223 GLN A CA  1 
ATOM   3914 C  C   . GLN B 1 223 ? -16.483 -3.674  -4.622  1.00 13.92 ? 223 GLN A C   1 
ATOM   3915 O  O   . GLN B 1 223 ? -16.263 -2.489  -4.295  1.00 16.72 ? 223 GLN A O   1 
ATOM   3916 C  CB  . GLN B 1 223 ? -17.409 -4.057  -6.892  1.00 18.46 ? 223 GLN A CB  1 
ATOM   3917 C  CG  . GLN B 1 223 ? -17.109 -4.320  -8.375  1.00 22.44 ? 223 GLN A CG  1 
ATOM   3918 C  CD  . GLN B 1 223 ? -17.099 -5.780  -8.782  1.00 22.95 ? 223 GLN A CD  1 
ATOM   3919 O  OE1 . GLN B 1 223 ? -17.247 -6.745  -7.985  1.00 21.64 ? 223 GLN A OE1 1 
ATOM   3920 N  NE2 . GLN B 1 223 ? -16.850 -5.983  -10.106 1.00 22.38 ? 223 GLN A NE2 1 
ATOM   3921 N  N   . GLN B 1 224 ? -16.991 -4.574  -3.785  1.00 15.50 ? 224 GLN A N   1 
ATOM   3922 C  CA  . GLN B 1 224 ? -17.143 -4.216  -2.361  1.00 14.07 ? 224 GLN A CA  1 
ATOM   3923 C  C   . GLN B 1 224 ? -15.810 -3.846  -1.704  1.00 12.77 ? 224 GLN A C   1 
ATOM   3924 O  O   . GLN B 1 224 ? -15.760 -2.841  -1.014  1.00 13.76 ? 224 GLN A O   1 
ATOM   3925 C  CB  . GLN B 1 224 ? -17.727 -5.404  -1.566  1.00 14.85 ? 224 GLN A CB  1 
ATOM   3926 C  CG  . GLN B 1 224 ? -19.179 -5.727  -1.928  1.00 15.29 ? 224 GLN A CG  1 
ATOM   3927 C  CD  . GLN B 1 224 ? -19.682 -6.961  -1.171  1.00 13.58 ? 224 GLN A CD  1 
ATOM   3928 O  OE1 . GLN B 1 224 ? -19.016 -7.983  -1.085  1.00 13.98 ? 224 GLN A OE1 1 
ATOM   3929 N  NE2 . GLN B 1 224 ? -20.964 -6.835  -0.669  1.00 14.57 ? 224 GLN A NE2 1 
ATOM   3930 N  N   . LEU B 1 225 ? -14.767 -4.673  -1.939  1.00 13.01 ? 225 LEU A N   1 
ATOM   3931 C  CA  . LEU B 1 225 ? -13.482 -4.343  -1.277  1.00 11.72 ? 225 LEU A CA  1 
ATOM   3932 C  C   . LEU B 1 225 ? -12.947 -3.012  -1.717  1.00 12.75 ? 225 LEU A C   1 
ATOM   3933 O  O   . LEU B 1 225 ? -12.473 -2.187  -0.958  1.00 12.60 ? 225 LEU A O   1 
ATOM   3934 C  CB  . LEU B 1 225 ? -12.529 -5.465  -1.476  1.00 11.50 ? 225 LEU A CB  1 
ATOM   3935 C  CG  . LEU B 1 225 ? -11.135 -5.240  -0.835  1.00 11.11 ? 225 LEU A CG  1 
ATOM   3936 C  CD1 . LEU B 1 225 ? -11.361 -5.100  0.725   1.00 13.95 ? 225 LEU A CD1 1 
ATOM   3937 C  CD2 . LEU B 1 225 ? -10.245 -6.471  -1.155  1.00 12.59 ? 225 LEU A CD2 1 
ATOM   3938 N  N   . ALA B 1 226 ? -13.057 -2.770  -3.045  1.00 12.90 ? 226 ALA A N   1 
ATOM   3939 C  CA  . ALA B 1 226 ? -12.548 -1.488  -3.537  1.00 13.22 ? 226 ALA A CA  1 
ATOM   3940 C  C   . ALA B 1 226 ? -13.192 -0.263  -2.936  1.00 13.74 ? 226 ALA A C   1 
ATOM   3941 O  O   . ALA B 1 226 ? -12.588 0.773   -2.869  1.00 15.26 ? 226 ALA A O   1 
ATOM   3942 C  CB  . ALA B 1 226 ? -12.719 -1.447  -5.052  1.00 14.90 ? 226 ALA A CB  1 
ATOM   3943 N  N   . LYS B 1 227 ? -14.451 -0.363  -2.454  1.00 14.07 ? 227 LYS A N   1 
ATOM   3944 C  CA  . LYS B 1 227 ? -15.088 0.758   -1.838  1.00 15.29 ? 227 LYS A CA  1 
ATOM   3945 C  C   . LYS B 1 227 ? -14.359 1.275   -0.618  1.00 16.10 ? 227 LYS A C   1 
ATOM   3946 O  O   . LYS B 1 227 ? -14.376 2.450   -0.313  1.00 16.69 ? 227 LYS A O   1 
ATOM   3947 C  CB  . LYS B 1 227 ? -16.503 0.414   -1.415  1.00 19.56 ? 227 LYS A CB  1 
ATOM   3948 C  CG  . LYS B 1 227 ? -17.446 0.299   -2.578  1.00 29.31 ? 227 LYS A CG  1 
ATOM   3949 C  CD  . LYS B 1 227 ? -18.125 1.659   -2.790  1.00 34.78 ? 227 LYS A CD  1 
ATOM   3950 C  CE  . LYS B 1 227 ? -19.218 1.952   -1.782  1.00 33.07 ? 227 LYS A CE  1 
ATOM   3951 N  NZ  . LYS B 1 227 ? -19.469 3.426   -1.911  1.00 36.78 ? 227 LYS A NZ  1 
ATOM   3952 N  N   . PHE B 1 228 ? -13.735 0.331   0.137   1.00 15.25 ? 228 PHE A N   1 
ATOM   3953 C  CA  . PHE B 1 228 ? -12.996 0.767   1.314   1.00 13.84 ? 228 PHE A CA  1 
ATOM   3954 C  C   . PHE B 1 228 ? -11.852 1.663   1.012   1.00 14.45 ? 228 PHE A C   1 
ATOM   3955 O  O   . PHE B 1 228 ? -11.448 2.526   1.818   1.00 14.16 ? 228 PHE A O   1 
ATOM   3956 C  CB  . PHE B 1 228 ? -12.489 -0.471  2.177   1.00 13.55 ? 228 PHE A CB  1 
ATOM   3957 C  CG  . PHE B 1 228 ? -13.636 -1.222  2.712   1.00 14.79 ? 228 PHE A CG  1 
ATOM   3958 C  CD1 . PHE B 1 228 ? -14.004 -2.375  2.127   1.00 13.92 ? 228 PHE A CD1 1 
ATOM   3959 C  CD2 . PHE B 1 228 ? -14.335 -0.757  3.815   1.00 14.93 ? 228 PHE A CD2 1 
ATOM   3960 C  CE1 . PHE B 1 228 ? -15.125 -3.057  2.534   1.00 15.45 ? 228 PHE A CE1 1 
ATOM   3961 C  CE2 . PHE B 1 228 ? -15.435 -1.462  4.288   1.00 14.26 ? 228 PHE A CE2 1 
ATOM   3962 C  CZ  . PHE B 1 228 ? -15.848 -2.631  3.679   1.00 14.13 ? 228 PHE A CZ  1 
ATOM   3963 N  N   . ARG B 1 229 ? -11.244 1.499   -0.178  1.00 13.92 ? 229 ARG A N   1 
ATOM   3964 C  CA  . ARG B 1 229 ? -10.075 2.296   -0.511  1.00 13.82 ? 229 ARG A CA  1 
ATOM   3965 C  C   . ARG B 1 229 ? -10.420 3.711   -0.857  1.00 15.30 ? 229 ARG A C   1 
ATOM   3966 O  O   . ARG B 1 229 ? -9.513  4.547   -0.919  1.00 15.93 ? 229 ARG A O   1 
ATOM   3967 C  CB  . ARG B 1 229 ? -9.416  1.661   -1.784  1.00 13.03 ? 229 ARG A CB  1 
ATOM   3968 C  CG  . ARG B 1 229 ? -8.909  0.258   -1.556  1.00 15.10 ? 229 ARG A CG  1 
ATOM   3969 C  CD  . ARG B 1 229 ? -8.079  -0.194  -2.760  1.00 16.65 ? 229 ARG A CD  1 
ATOM   3970 N  NE  . ARG B 1 229 ? -7.751  -1.608  -2.592  1.00 12.79 ? 229 ARG A NE  1 
ATOM   3971 C  CZ  . ARG B 1 229 ? -8.363  -2.670  -3.155  1.00 13.17 ? 229 ARG A CZ  1 
ATOM   3972 N  NH1 . ARG B 1 229 ? -9.291  -2.546  -4.118  1.00 14.48 ? 229 ARG A NH1 1 
ATOM   3973 N  NH2 . ARG B 1 229 ? -8.005  -3.947  -2.828  1.00 14.14 ? 229 ARG A NH2 1 
ATOM   3974 N  N   . SER B 1 230 ? -11.714 4.001   -1.028  1.00 16.70 ? 230 SER A N   1 
ATOM   3975 C  CA  . SER B 1 230 ? -12.162 5.408   -1.209  1.00 19.44 ? 230 SER A CA  1 
ATOM   3976 C  C   . SER B 1 230 ? -12.318 6.191   0.088   1.00 18.17 ? 230 SER A C   1 
ATOM   3977 O  O   . SER B 1 230 ? -12.571 7.426   0.059   1.00 19.14 ? 230 SER A O   1 
ATOM   3978 C  CB  . SER B 1 230 ? -13.440 5.458   -2.053  1.00 23.53 ? 230 SER A CB  1 
ATOM   3979 O  OG  . SER B 1 230 ? -14.534 4.911   -1.348  1.00 27.12 ? 230 SER A OG  1 
ATOM   3980 N  N   . LEU B 1 231 ? -12.156 5.540   1.274   1.00 18.39 ? 231 LEU A N   1 
ATOM   3981 C  CA  . LEU B 1 231 ? -12.128 6.327   2.455   1.00 16.41 ? 231 LEU A CA  1 
ATOM   3982 C  C   . LEU B 1 231 ? -10.920 7.256   2.445   1.00 18.61 ? 231 LEU A C   1 
ATOM   3983 O  O   . LEU B 1 231 ? -9.875  6.902   1.945   1.00 18.17 ? 231 LEU A O   1 
ATOM   3984 C  CB  . LEU B 1 231 ? -11.968 5.393   3.699   1.00 16.61 ? 231 LEU A CB  1 
ATOM   3985 C  CG  . LEU B 1 231 ? -13.256 4.607   3.876   1.00 16.39 ? 231 LEU A CG  1 
ATOM   3986 C  CD1 . LEU B 1 231 ? -12.967 3.521   4.931   1.00 18.52 ? 231 LEU A CD1 1 
ATOM   3987 C  CD2 . LEU B 1 231 ? -14.406 5.499   4.359   1.00 17.57 ? 231 LEU A CD2 1 
ATOM   3988 N  N   . LEU B 1 232 ? -11.031 8.419   3.081   1.00 18.68 ? 232 LEU A N   1 
ATOM   3989 C  CA  . LEU B 1 232 ? -9.862  9.324   3.220   1.00 18.77 ? 232 LEU A CA  1 
ATOM   3990 C  C   . LEU B 1 232 ? -9.152  9.105   4.537   1.00 21.08 ? 232 LEU A C   1 
ATOM   3991 O  O   . LEU B 1 232 ? -9.806  8.743   5.558   1.00 21.10 ? 232 LEU A O   1 
ATOM   3992 C  CB  . LEU B 1 232 ? -10.373 10.785  3.156   1.00 21.79 ? 232 LEU A CB  1 
ATOM   3993 C  CG  . LEU B 1 232 ? -11.169 11.182  1.923   1.00 23.86 ? 232 LEU A CG  1 
ATOM   3994 C  CD1 . LEU B 1 232 ? -11.499 12.681  2.119   1.00 28.35 ? 232 LEU A CD1 1 
ATOM   3995 C  CD2 . LEU B 1 232 ? -10.226 10.910  0.773   1.00 28.10 ? 232 LEU A CD2 1 
ATOM   3996 N  N   . CYS B 1 233 ? -7.835  9.297   4.531   1.00 23.06 ? 233 CYS A N   1 
ATOM   3997 C  CA  . CYS B 1 233 ? -7.090  9.266   5.766   1.00 22.24 ? 233 CYS A CA  1 
ATOM   3998 C  C   . CYS B 1 233 ? -6.898  10.678  6.267   1.00 23.99 ? 233 CYS A C   1 
ATOM   3999 O  O   . CYS B 1 233 ? -6.245  10.887  7.289   1.00 26.54 ? 233 CYS A O   1 
ATOM   4000 C  CB  . CYS B 1 233 ? -5.720  8.529   5.674   1.00 21.70 ? 233 CYS A CB  1 
ATOM   4001 S  SG  . CYS B 1 233 ? -4.585  9.304   4.462   1.00 29.73 ? 233 CYS A SG  1 
ATOM   4002 N  N   . THR B 1 234 ? -7.530  11.613  5.545   1.00 24.07 ? 234 THR A N   1 
ATOM   4003 C  CA  . THR B 1 234 ? -7.536  13.039  5.879   1.00 27.68 ? 234 THR A CA  1 
ATOM   4004 C  C   . THR B 1 234 ? -8.913  13.604  6.268   1.00 27.54 ? 234 THR A C   1 
ATOM   4005 O  O   . THR B 1 234 ? -9.990  13.147  5.790   1.00 27.43 ? 234 THR A O   1 
ATOM   4006 C  CB  . THR B 1 234 ? -6.977  13.803  4.639   1.00 27.04 ? 234 THR A CB  1 
ATOM   4007 O  OG1 . THR B 1 234 ? -7.717  13.382  3.477   1.00 29.28 ? 234 THR A OG1 1 
ATOM   4008 C  CG2 . THR B 1 234 ? -5.499  13.522  4.396   1.00 30.01 ? 234 THR A CG2 1 
ATOM   4009 N  N   . ALA B 1 235 ? -8.903  14.584  7.197   1.00 33.20 ? 235 ALA A N   1 
ATOM   4010 C  CA  . ALA B 1 235 ? -10.130 15.268  7.730   1.00 32.31 ? 235 ALA A CA  1 
ATOM   4011 C  C   . ALA B 1 235 ? -10.735 16.241  6.738   1.00 39.02 ? 235 ALA A C   1 
ATOM   4012 O  O   . ALA B 1 235 ? -10.047 16.725  5.833   1.00 38.44 ? 235 ALA A O   1 
ATOM   4013 C  CB  . ALA B 1 235 ? -9.828  16.010  9.050   1.00 32.71 ? 235 ALA A CB  1 
ATOM   4014 N  N   . GLU B 1 236 ? -12.022 16.516  6.906   1.00 46.29 ? 236 GLU A N   1 
ATOM   4015 C  CA  . GLU B 1 236 ? -12.724 17.547  6.118   1.00 53.80 ? 236 GLU A CA  1 
ATOM   4016 C  C   . GLU B 1 236 ? -11.826 18.790  5.980   1.00 50.60 ? 236 GLU A C   1 
ATOM   4017 O  O   . GLU B 1 236 ? -11.290 19.281  6.973   1.00 44.84 ? 236 GLU A O   1 
ATOM   4018 C  CB  . GLU B 1 236 ? -14.063 17.907  6.780   1.00 54.75 ? 236 GLU A CB  1 
ATOM   4019 C  CG  . GLU B 1 236 ? -15.012 16.725  6.963   1.00 62.76 ? 236 GLU A CG  1 
ATOM   4020 C  CD  . GLU B 1 236 ? -14.911 15.980  8.326   1.00 68.38 ? 236 GLU A CD  1 
ATOM   4021 O  OE1 . GLU B 1 236 ? -13.803 15.524  8.765   1.00 47.26 ? 236 GLU A OE1 1 
ATOM   4022 O  OE2 . GLU B 1 236 ? -15.986 15.820  8.965   1.00 76.56 ? 236 GLU A OE2 1 
ATOM   4023 N  N   . GLY B 1 237 ? -11.596 19.229  4.743   1.00 54.43 ? 237 GLY A N   1 
ATOM   4024 C  CA  . GLY B 1 237 ? -10.788 20.426  4.494   1.00 55.56 ? 237 GLY A CA  1 
ATOM   4025 C  C   . GLY B 1 237 ? -9.264  20.390  4.580   1.00 55.41 ? 237 GLY A C   1 
ATOM   4026 O  O   . GLY B 1 237 ? -8.646  21.456  4.570   1.00 43.76 ? 237 GLY A O   1 
ATOM   4027 N  N   . GLU B 1 238 ? -8.626  19.216  4.670   1.00 48.10 ? 238 GLU A N   1 
ATOM   4028 C  CA  . GLU B 1 238 ? -7.174  19.172  4.395   1.00 48.47 ? 238 GLU A CA  1 
ATOM   4029 C  C   . GLU B 1 238 ? -7.047  18.601  2.999   1.00 46.83 ? 238 GLU A C   1 
ATOM   4030 O  O   . GLU B 1 238 ? -8.034  18.185  2.413   1.00 42.74 ? 238 GLU A O   1 
ATOM   4031 C  CB  . GLU B 1 238 ? -6.333  18.289  5.321   1.00 53.77 ? 238 GLU A CB  1 
ATOM   4032 C  CG  . GLU B 1 238 ? -6.904  17.816  6.634   1.00 60.16 ? 238 GLU A CG  1 
ATOM   4033 C  CD  . GLU B 1 238 ? -6.138  16.594  7.114   1.00 67.47 ? 238 GLU A CD  1 
ATOM   4034 O  OE1 . GLU B 1 238 ? -6.712  15.762  7.860   1.00 56.34 ? 238 GLU A OE1 1 
ATOM   4035 O  OE2 . GLU B 1 238 ? -4.952  16.457  6.706   1.00 74.16 ? 238 GLU A OE2 1 
ATOM   4036 N  N   . ALA B 1 239 ? -5.828  18.535  2.481   1.00 46.59 ? 239 ALA A N   1 
ATOM   4037 C  CA  . ALA B 1 239 ? -5.602  17.996  1.145   1.00 43.69 ? 239 ALA A CA  1 
ATOM   4038 C  C   . ALA B 1 239 ? -5.910  16.464  1.170   1.00 38.70 ? 239 ALA A C   1 
ATOM   4039 O  O   . ALA B 1 239 ? -5.291  15.753  1.976   1.00 40.09 ? 239 ALA A O   1 
ATOM   4040 C  CB  . ALA B 1 239 ? -4.147  18.264  0.723   1.00 44.19 ? 239 ALA A CB  1 
ATOM   4041 N  N   . ALA B 1 240 ? -6.837  16.018  0.296   1.00 35.69 ? 240 ALA A N   1 
ATOM   4042 C  CA  . ALA B 1 240 ? -7.334  14.601  0.233   1.00 34.79 ? 240 ALA A CA  1 
ATOM   4043 C  C   . ALA B 1 240 ? -6.225  13.599  -0.009  1.00 35.24 ? 240 ALA A C   1 
ATOM   4044 O  O   . ALA B 1 240 ? -5.348  13.791  -0.859  1.00 34.33 ? 240 ALA A O   1 
ATOM   4045 C  CB  . ALA B 1 240 ? -8.450  14.431  -0.817  1.00 36.93 ? 240 ALA A CB  1 
ATOM   4046 N  N   . ALA B 1 241 ? -6.220  12.536  0.792   1.00 25.52 ? 241 ALA A N   1 
ATOM   4047 C  CA  . ALA B 1 241 ? -5.305  11.423  0.526   1.00 23.11 ? 241 ALA A CA  1 
ATOM   4048 C  C   . ALA B 1 241 ? -6.119  10.193  0.849   1.00 19.74 ? 241 ALA A C   1 
ATOM   4049 O  O   . ALA B 1 241 ? -6.967  10.254  1.765   1.00 21.31 ? 241 ALA A O   1 
ATOM   4050 C  CB  . ALA B 1 241 ? -4.058  11.532  1.349   1.00 22.30 ? 241 ALA A CB  1 
ATOM   4051 N  N   . PHE B 1 242 ? -6.000  9.166   0.006   1.00 18.36 ? 242 PHE A N   1 
ATOM   4052 C  CA  . PHE B 1 242 ? -6.875  8.001   0.162   1.00 17.60 ? 242 PHE A CA  1 
ATOM   4053 C  C   . PHE B 1 242 ? -6.250  6.859   0.938   1.00 15.40 ? 242 PHE A C   1 
ATOM   4054 O  O   . PHE B 1 242 ? -5.089  6.629   0.803   1.00 17.53 ? 242 PHE A O   1 
ATOM   4055 C  CB  . PHE B 1 242 ? -7.218  7.525   -1.268  1.00 18.77 ? 242 PHE A CB  1 
ATOM   4056 C  CG  . PHE B 1 242 ? -8.064  8.492   -1.978  1.00 20.81 ? 242 PHE A CG  1 
ATOM   4057 C  CD1 . PHE B 1 242 ? -7.480  9.447   -2.847  1.00 22.25 ? 242 PHE A CD1 1 
ATOM   4058 C  CD2 . PHE B 1 242 ? -9.435  8.480   -1.822  1.00 20.34 ? 242 PHE A CD2 1 
ATOM   4059 C  CE1 . PHE B 1 242 ? -8.331  10.363  -3.484  1.00 21.39 ? 242 PHE A CE1 1 
ATOM   4060 C  CE2 . PHE B 1 242 ? -10.257 9.384   -2.458  1.00 25.11 ? 242 PHE A CE2 1 
ATOM   4061 C  CZ  . PHE B 1 242 ? -9.700  10.315  -3.290  1.00 24.70 ? 242 PHE A CZ  1 
ATOM   4062 N  N   . LEU B 1 243 ? -7.123  6.173   1.717   1.00 16.44 ? 243 LEU A N   1 
ATOM   4063 C  CA  . LEU B 1 243 ? -6.711  5.019   2.537   1.00 16.31 ? 243 LEU A CA  1 
ATOM   4064 C  C   . LEU B 1 243 ? -6.657  3.774   1.619   1.00 15.33 ? 243 LEU A C   1 
ATOM   4065 O  O   . LEU B 1 243 ? -7.487  2.837   1.771   1.00 15.70 ? 243 LEU A O   1 
ATOM   4066 C  CB  . LEU B 1 243 ? -7.638  4.961   3.799   1.00 15.91 ? 243 LEU A CB  1 
ATOM   4067 C  CG  . LEU B 1 243 ? -7.210  3.814   4.725   1.00 17.04 ? 243 LEU A CG  1 
ATOM   4068 C  CD1 . LEU B 1 243 ? -5.858  4.173   5.314   1.00 16.23 ? 243 LEU A CD1 1 
ATOM   4069 C  CD2 . LEU B 1 243 ? -8.308  3.761   5.798   1.00 16.48 ? 243 LEU A CD2 1 
ATOM   4070 N  N   . VAL B 1 244 ? -5.710  3.761   0.639   1.00 15.58 ? 244 VAL A N   1 
ATOM   4071 C  CA  . VAL B 1 244 ? -5.709  2.653   -0.340  1.00 15.74 ? 244 VAL A CA  1 
ATOM   4072 C  C   . VAL B 1 244 ? -5.164  1.383   0.273   1.00 14.78 ? 244 VAL A C   1 
ATOM   4073 O  O   . VAL B 1 244 ? -5.348  0.300   -0.245  1.00 14.45 ? 244 VAL A O   1 
ATOM   4074 C  CB  . VAL B 1 244 ? -4.913  3.007   -1.657  1.00 16.02 ? 244 VAL A CB  1 
ATOM   4075 C  CG1 . VAL B 1 244 ? -5.657  4.163   -2.346  1.00 14.27 ? 244 VAL A CG1 1 
ATOM   4076 C  CG2 . VAL B 1 244 ? -3.448  3.331   -1.370  1.00 16.54 ? 244 VAL A CG2 1 
ATOM   4077 N  N   . SER B 1 245 ? -4.431  1.512   1.398   1.00 14.79 ? 245 SER A N   1 
ATOM   4078 C  CA  . SER B 1 245 ? -3.769  0.350   2.015   1.00 14.15 ? 245 SER A CA  1 
ATOM   4079 C  C   . SER B 1 245 ? -3.548  0.650   3.487   1.00 13.86 ? 245 SER A C   1 
ATOM   4080 O  O   . SER B 1 245 ? -3.198  1.756   3.840   1.00 15.05 ? 245 SER A O   1 
ATOM   4081 C  CB  . SER B 1 245 ? -2.417  0.025   1.360   1.00 16.41 ? 245 SER A CB  1 
ATOM   4082 O  OG  . SER B 1 245 ? -1.834  -1.144  1.914   1.00 16.82 ? 245 SER A OG  1 
ATOM   4083 N  N   . ASN B 1 246 ? -3.775  -0.371  4.350   1.00 14.15 ? 246 ASN A N   1 
ATOM   4084 C  CA  . ASN B 1 246 ? -3.764  -0.104  5.831   1.00 13.13 ? 246 ASN A CA  1 
ATOM   4085 C  C   . ASN B 1 246 ? -3.412  -1.369  6.563   1.00 12.80 ? 246 ASN A C   1 
ATOM   4086 O  O   . ASN B 1 246 ? -4.018  -1.613  7.607   1.00 14.94 ? 246 ASN A O   1 
ATOM   4087 C  CB  . ASN B 1 246 ? -5.087  0.499   6.363   1.00 12.06 ? 246 ASN A CB  1 
ATOM   4088 C  CG  . ASN B 1 246 ? -6.265  -0.431  6.233   1.00 11.98 ? 246 ASN A CG  1 
ATOM   4089 O  OD1 . ASN B 1 246 ? -6.164  -1.443  5.540   1.00 14.13 ? 246 ASN A OD1 1 
ATOM   4090 N  ND2 . ASN B 1 246 ? -7.349  -0.123  6.957   1.00 14.19 ? 246 ASN A ND2 1 
ATOM   4091 N  N   . HIS B 1 247 ? -2.422  -2.084  6.054   1.00 12.50 ? 247 HIS A N   1 
ATOM   4092 C  CA  . HIS B 1 247 ? -1.996  -3.342  6.709   1.00 12.21 ? 247 HIS A CA  1 
ATOM   4093 C  C   . HIS B 1 247 ? -0.563  -3.241  7.115   1.00 14.42 ? 247 HIS A C   1 
ATOM   4094 O  O   . HIS B 1 247 ? 0.307   -2.643  6.358   1.00 16.64 ? 247 HIS A O   1 
ATOM   4095 C  CB  . HIS B 1 247 ? -2.248  -4.599  5.858   1.00 14.34 ? 247 HIS A CB  1 
ATOM   4096 C  CG  . HIS B 1 247 ? -1.555  -4.545  4.509   1.00 15.35 ? 247 HIS A CG  1 
ATOM   4097 N  ND1 . HIS B 1 247 ? -0.356  -5.144  4.241   1.00 21.32 ? 247 HIS A ND1 1 
ATOM   4098 C  CD2 . HIS B 1 247 ? -1.938  -3.899  3.374   1.00 15.05 ? 247 HIS A CD2 1 
ATOM   4099 C  CE1 . HIS B 1 247 ? -0.040  -4.908  2.894   1.00 14.90 ? 247 HIS A CE1 1 
ATOM   4100 N  NE2 . HIS B 1 247 ? -0.990  -4.135  2.408   1.00 19.99 ? 247 HIS A NE2 1 
ATOM   4101 N  N   . ARG B 1 248 ? -0.233  -3.787  8.312   1.00 13.16 ? 248 ARG A N   1 
ATOM   4102 C  CA  . ARG B 1 248 ? 1.116   -3.668  8.826   1.00 12.66 ? 248 ARG A CA  1 
ATOM   4103 C  C   . ARG B 1 248 ? 1.828   -4.978  8.367   1.00 12.95 ? 248 ARG A C   1 
ATOM   4104 O  O   . ARG B 1 248 ? 1.260   -6.067  8.344   1.00 15.92 ? 248 ARG A O   1 
ATOM   4105 C  CB  . ARG B 1 248 ? 1.017   -3.695  10.372  1.00 12.56 ? 248 ARG A CB  1 
ATOM   4106 C  CG  . ARG B 1 248 ? 2.407   -3.588  11.067  1.00 13.76 ? 248 ARG A CG  1 
ATOM   4107 C  CD  . ARG B 1 248 ? 2.404   -3.781  12.598  1.00 14.12 ? 248 ARG A CD  1 
ATOM   4108 N  NE  . ARG B 1 248 ? 3.707   -3.276  13.076  1.00 15.77 ? 248 ARG A NE  1 
ATOM   4109 C  CZ  . ARG B 1 248 ? 4.188   -3.572  14.276  1.00 16.53 ? 248 ARG A CZ  1 
ATOM   4110 N  NH1 . ARG B 1 248 ? 3.538   -4.395  15.092  1.00 15.13 ? 248 ARG A NH1 1 
ATOM   4111 N  NH2 . ARG B 1 248 ? 5.347   -3.061  14.674  1.00 18.50 ? 248 ARG A NH2 1 
ATOM   4112 N  N   . PRO B 1 249 ? 3.120   -4.905  8.028   1.00 14.21 ? 249 PRO A N   1 
ATOM   4113 C  CA  . PRO B 1 249 ? 3.863   -6.057  7.634   1.00 15.34 ? 249 PRO A CA  1 
ATOM   4114 C  C   . PRO B 1 249 ? 4.033   -7.060  8.767   1.00 17.66 ? 249 PRO A C   1 
ATOM   4115 O  O   . PRO B 1 249 ? 3.935   -6.629  9.901   1.00 16.46 ? 249 PRO A O   1 
ATOM   4116 C  CB  . PRO B 1 249 ? 5.270   -5.454  7.330   1.00 17.63 ? 249 PRO A CB  1 
ATOM   4117 C  CG  . PRO B 1 249 ? 4.954   -4.086  6.898   1.00 20.15 ? 249 PRO A CG  1 
ATOM   4118 C  CD  . PRO B 1 249 ? 3.848   -3.643  7.832   1.00 18.53 ? 249 PRO A CD  1 
ATOM   4119 N  N   . PRO B 1 250 ? 4.265   -8.321  8.476   1.00 16.86 ? 250 PRO A N   1 
ATOM   4120 C  CA  . PRO B 1 250 ? 4.522   -9.312  9.592   1.00 15.93 ? 250 PRO A CA  1 
ATOM   4121 C  C   . PRO B 1 250 ? 5.810   -8.975  10.430  1.00 17.00 ? 250 PRO A C   1 
ATOM   4122 O  O   . PRO B 1 250 ? 6.820   -8.352  9.934   1.00 17.64 ? 250 PRO A O   1 
ATOM   4123 C  CB  . PRO B 1 250 ? 4.697   -10.632 8.898   1.00 19.50 ? 250 PRO A CB  1 
ATOM   4124 C  CG  . PRO B 1 250 ? 5.249   -10.180 7.587   1.00 24.59 ? 250 PRO A CG  1 
ATOM   4125 C  CD  . PRO B 1 250 ? 4.577   -8.907  7.161   1.00 20.09 ? 250 PRO A CD  1 
ATOM   4126 N  N   . GLN B 1 251 ? 5.731   -9.345  11.715  1.00 14.94 ? 251 GLN A N   1 
ATOM   4127 C  CA  . GLN B 1 251 ? 6.797   -8.980  12.652  1.00 14.26 ? 251 GLN A CA  1 
ATOM   4128 C  C   . GLN B 1 251 ? 7.419   -10.298 13.139  1.00 14.18 ? 251 GLN A C   1 
ATOM   4129 O  O   . GLN B 1 251 ? 6.872   -11.381 13.120  1.00 16.18 ? 251 GLN A O   1 
ATOM   4130 C  CB  . GLN B 1 251 ? 6.151   -8.225  13.837  1.00 13.97 ? 251 GLN A CB  1 
ATOM   4131 C  CG  . GLN B 1 251 ? 5.426   -6.986  13.384  1.00 14.75 ? 251 GLN A CG  1 
ATOM   4132 C  CD  . GLN B 1 251 ? 6.366   -5.969  12.672  1.00 19.97 ? 251 GLN A CD  1 
ATOM   4133 O  OE1 . GLN B 1 251 ? 7.477   -5.653  13.181  1.00 21.72 ? 251 GLN A OE1 1 
ATOM   4134 N  NE2 . GLN B 1 251 ? 5.937   -5.444  11.551  1.00 18.96 ? 251 GLN A NE2 1 
ATOM   4135 N  N   . PRO B 1 252 ? 8.684   -10.224 13.617  1.00 14.37 ? 252 PRO A N   1 
ATOM   4136 C  CA  . PRO B 1 252 ? 9.436   -11.414 14.064  1.00 15.59 ? 252 PRO A CA  1 
ATOM   4137 C  C   . PRO B 1 252 ? 8.752   -12.164 15.207  1.00 15.52 ? 252 PRO A C   1 
ATOM   4138 O  O   . PRO B 1 252 ? 8.255   -11.528 16.198  1.00 17.14 ? 252 PRO A O   1 
ATOM   4139 C  CB  . PRO B 1 252 ? 10.747  -10.810 14.606  1.00 16.91 ? 252 PRO A CB  1 
ATOM   4140 C  CG  . PRO B 1 252 ? 10.811  -9.466  14.038  1.00 20.22 ? 252 PRO A CG  1 
ATOM   4141 C  CD  . PRO B 1 252 ? 9.388   -8.972  13.834  1.00 16.03 ? 252 PRO A CD  1 
ATOM   4142 N  N   . LEU B 1 253 ? 8.777   -13.446 15.042  1.00 16.30 ? 253 LEU A N   1 
ATOM   4143 C  CA  . LEU B 1 253 ? 8.090   -14.317 15.996  1.00 18.09 ? 253 LEU A CA  1 
ATOM   4144 C  C   . LEU B 1 253 ? 8.767   -14.275 17.391  1.00 20.79 ? 253 LEU A C   1 
ATOM   4145 O  O   . LEU B 1 253 ? 8.123   -14.343 18.447  1.00 17.87 ? 253 LEU A O   1 
ATOM   4146 C  CB  . LEU B 1 253 ? 7.985   -15.727 15.497  1.00 21.65 ? 253 LEU A CB  1 
ATOM   4147 C  CG  . LEU B 1 253 ? 7.017   -16.678 16.253  1.00 20.66 ? 253 LEU A CG  1 
ATOM   4148 C  CD1 . LEU B 1 253 ? 5.599   -16.117 16.429  1.00 19.41 ? 253 LEU A CD1 1 
ATOM   4149 C  CD2 . LEU B 1 253 ? 6.942   -18.006 15.492  1.00 24.52 ? 253 LEU A CD2 1 
ATOM   4150 N  N   . LYS B 1 254 ? 10.075  -14.076 17.373  1.00 20.02 ? 254 LYS A N   1 
ATOM   4151 C  CA  . LYS B 1 254 ? 10.821  -13.971 18.601  1.00 18.76 ? 254 LYS A CA  1 
ATOM   4152 C  C   . LYS B 1 254 ? 10.547  -15.112 19.653  1.00 18.29 ? 254 LYS A C   1 
ATOM   4153 O  O   . LYS B 1 254 ? 10.505  -14.840 20.841  1.00 19.83 ? 254 LYS A O   1 
ATOM   4154 C  CB  . LYS B 1 254 ? 10.773  -12.608 19.178  1.00 20.35 ? 254 LYS A CB  1 
ATOM   4155 C  CG  . LYS B 1 254 ? 11.594  -11.704 18.274  1.00 23.91 ? 254 LYS A CG  1 
ATOM   4156 C  CD  . LYS B 1 254 ? 11.580  -10.334 18.734  1.00 29.68 ? 254 LYS A CD  1 
ATOM   4157 C  CE  . LYS B 1 254 ? 12.614  -9.578  17.907  1.00 32.29 ? 254 LYS A CE  1 
ATOM   4158 N  NZ  . LYS B 1 254 ? 12.655  -8.274  18.537  1.00 36.56 ? 254 LYS A NZ  1 
ATOM   4159 N  N   . GLY B 1 255 ? 10.445  -16.314 19.161  1.00 18.10 ? 255 GLY A N   1 
ATOM   4160 C  CA  . GLY B 1 255 ? 10.325  -17.520 20.019  1.00 18.20 ? 255 GLY A CA  1 
ATOM   4161 C  C   . GLY B 1 255 ? 8.982   -17.765 20.661  1.00 19.25 ? 255 GLY A C   1 
ATOM   4162 O  O   . GLY B 1 255 ? 8.824   -18.658 21.504  1.00 18.05 ? 255 GLY A O   1 
ATOM   4163 N  N   . ARG B 1 256 ? 7.977   -17.020 20.212  1.00 16.85 ? 256 ARG A N   1 
ATOM   4164 C  CA  . ARG B 1 256 ? 6.601   -17.355 20.627  1.00 16.35 ? 256 ARG A CA  1 
ATOM   4165 C  C   . ARG B 1 256 ? 6.088   -18.622 20.001  1.00 16.41 ? 256 ARG A C   1 
ATOM   4166 O  O   . ARG B 1 256 ? 6.533   -19.096 18.928  1.00 17.43 ? 256 ARG A O   1 
ATOM   4167 C  CB  . ARG B 1 256 ? 5.688   -16.159 20.283  1.00 13.91 ? 256 ARG A CB  1 
ATOM   4168 C  CG  . ARG B 1 256 ? 5.881   -14.959 21.116  1.00 15.81 ? 256 ARG A CG  1 
ATOM   4169 C  CD  . ARG B 1 256 ? 5.050   -13.833 20.502  1.00 15.66 ? 256 ARG A CD  1 
ATOM   4170 N  NE  . ARG B 1 256 ? 5.634   -13.303 19.258  1.00 15.16 ? 256 ARG A NE  1 
ATOM   4171 C  CZ  . ARG B 1 256 ? 5.069   -12.319 18.529  1.00 16.01 ? 256 ARG A CZ  1 
ATOM   4172 N  NH1 . ARG B 1 256 ? 3.867   -11.755 18.839  1.00 14.62 ? 256 ARG A NH1 1 
ATOM   4173 N  NH2 . ARG B 1 256 ? 5.726   -11.855 17.464  1.00 14.34 ? 256 ARG A NH2 1 
ATOM   4174 N  N   . LYS B 1 257 ? 5.163   -19.300 20.713  1.00 17.05 ? 257 LYS A N   1 
ATOM   4175 C  CA  . LYS B 1 257 ? 4.559   -20.526 20.263  1.00 17.05 ? 257 LYS A CA  1 
ATOM   4176 C  C   . LYS B 1 257 ? 3.206   -20.257 19.589  1.00 16.33 ? 257 LYS A C   1 
ATOM   4177 O  O   . LYS B 1 257 ? 2.330   -19.629 20.225  1.00 18.41 ? 257 LYS A O   1 
ATOM   4178 C  CB  . LYS B 1 257 ? 4.301   -21.477 21.494  1.00 22.91 ? 257 LYS A CB  1 
ATOM   4179 C  CG  . LYS B 1 257 ? 3.809   -22.839 21.114  1.00 24.10 ? 257 LYS A CG  1 
ATOM   4180 C  CD  . LYS B 1 257 ? 3.214   -23.682 22.295  1.00 25.69 ? 257 LYS A CD  1 
ATOM   4181 C  CE  . LYS B 1 257 ? 4.226   -24.012 23.403  1.00 27.64 ? 257 LYS A CE  1 
ATOM   4182 N  NZ  . LYS B 1 257 ? 3.624   -25.119 24.230  1.00 25.10 ? 257 LYS A NZ  1 
ATOM   4183 N  N   . VAL B 1 258 ? 3.085   -20.630 18.329  1.00 16.74 ? 258 VAL A N   1 
ATOM   4184 C  CA  . VAL B 1 258 ? 1.742   -20.459 17.689  1.00 15.25 ? 258 VAL A CA  1 
ATOM   4185 C  C   . VAL B 1 258 ? 1.135   -21.817 17.806  1.00 16.81 ? 258 VAL A C   1 
ATOM   4186 O  O   . VAL B 1 258 ? 1.733   -22.830 17.351  1.00 18.80 ? 258 VAL A O   1 
ATOM   4187 C  CB  . VAL B 1 258 ? 1.912   -20.079 16.236  1.00 16.53 ? 258 VAL A CB  1 
ATOM   4188 C  CG1 . VAL B 1 258 ? 0.532   -19.941 15.549  1.00 15.75 ? 258 VAL A CG1 1 
ATOM   4189 C  CG2 . VAL B 1 258 ? 2.703   -18.772 16.188  1.00 19.53 ? 258 VAL A CG2 1 
ATOM   4190 N  N   . ARG B 1 259 ? -0.113  -21.860 18.341  1.00 14.63 ? 259 ARG A N   1 
ATOM   4191 C  CA  . ARG B 1 259 ? -0.811  -23.138 18.534  1.00 14.87 ? 259 ARG A CA  1 
ATOM   4192 C  C   . ARG B 1 259 ? -2.010  -23.269 17.572  1.00 16.74 ? 259 ARG A C   1 
ATOM   4193 O  O   . ARG B 1 259 ? -2.545  -22.273 17.147  1.00 15.79 ? 259 ARG A O   1 
ATOM   4194 C  CB  . ARG B 1 259 ? -1.325  -23.208 19.963  1.00 13.75 ? 259 ARG A CB  1 
ATOM   4195 C  CG  . ARG B 1 259 ? -0.147  -23.207 20.945  1.00 16.93 ? 259 ARG A CG  1 
ATOM   4196 C  CD  . ARG B 1 259 ? -0.656  -23.285 22.394  1.00 15.95 ? 259 ARG A CD  1 
ATOM   4197 N  NE  . ARG B 1 259 ? -1.253  -22.050 22.802  1.00 15.12 ? 259 ARG A NE  1 
ATOM   4198 C  CZ  . ARG B 1 259 ? -2.215  -21.937 23.741  1.00 14.01 ? 259 ARG A CZ  1 
ATOM   4199 N  NH1 . ARG B 1 259 ? -2.630  -23.027 24.426  1.00 16.85 ? 259 ARG A NH1 1 
ATOM   4200 N  NH2 . ARG B 1 259 ? -2.683  -20.759 24.074  1.00 14.58 ? 259 ARG A NH2 1 
ATOM   4201 N  N   . ALA B 1 260 ? -2.376  -24.506 17.283  1.00 15.49 ? 260 ALA A N   1 
ATOM   4202 C  CA  . ALA B 1 260 ? -3.514  -24.795 16.368  1.00 15.95 ? 260 ALA A CA  1 
ATOM   4203 C  C   . ALA B 1 260 ? -4.525  -25.471 17.206  1.00 18.49 ? 260 ALA A C   1 
ATOM   4204 O  O   . ALA B 1 260 ? -4.203  -26.377 18.086  1.00 17.04 ? 260 ALA A O   1 
ATOM   4205 C  CB  . ALA B 1 260 ? -3.053  -25.673 15.206  1.00 18.18 ? 260 ALA A CB  1 
ATOM   4206 N  N   . SER B 1 261 ? -5.799  -25.136 16.969  1.00 16.13 ? 261 SER A N   1 
ATOM   4207 C  CA  . SER B 1 261 ? -6.912  -25.853 17.636  1.00 17.37 ? 261 SER A CA  1 
ATOM   4208 C  C   . SER B 1 261 ? -7.321  -27.132 16.941  1.00 17.61 ? 261 SER A C   1 
ATOM   4209 O  O   . SER B 1 261 ? -8.324  -27.757 17.328  1.00 18.01 ? 261 SER A O   1 
ATOM   4210 C  CB  . SER B 1 261 ? -8.116  -24.928 17.637  1.00 15.94 ? 261 SER A CB  1 
ATOM   4211 O  OG  . SER B 1 261 ? -8.757  -24.807 16.352  1.00 15.68 ? 261 SER A OG  1 
ATOM   4212 N  N   . PHE B 1 262 ? -6.639  -27.456 15.845  1.00 17.55 ? 262 PHE A N   1 
ATOM   4213 C  CA  . PHE B 1 262 ? -7.116  -28.522 14.982  1.00 18.86 ? 262 PHE A CA  1 
ATOM   4214 C  C   . PHE B 1 262 ? -5.859  -29.237 14.431  1.00 19.32 ? 262 PHE A C   1 
ATOM   4215 O  O   . PHE B 1 262 ? -4.747  -28.645 14.412  1.00 18.58 ? 262 PHE A O   1 
ATOM   4216 C  CB  . PHE B 1 262 ? -7.963  -27.988 13.830  1.00 20.42 ? 262 PHE A CB  1 
ATOM   4217 C  CG  . PHE B 1 262 ? -7.168  -27.043 12.945  1.00 19.01 ? 262 PHE A CG  1 
ATOM   4218 C  CD1 . PHE B 1 262 ? -6.579  -27.497 11.770  1.00 20.89 ? 262 PHE A CD1 1 
ATOM   4219 C  CD2 . PHE B 1 262 ? -6.922  -25.694 13.362  1.00 16.58 ? 262 PHE A CD2 1 
ATOM   4220 C  CE1 . PHE B 1 262 ? -5.765  -26.651 10.990  1.00 22.73 ? 262 PHE A CE1 1 
ATOM   4221 C  CE2 . PHE B 1 262 ? -6.116  -24.847 12.599  1.00 17.97 ? 262 PHE A CE2 1 
ATOM   4222 C  CZ  . PHE B 1 262 ? -5.562  -25.298 11.413  1.00 19.62 ? 262 PHE A CZ  1 
ATOM   4223 N  N   . HIS B 1 263 ? -6.028  -30.466 13.936  1.00 22.94 ? 263 HIS A N   1 
ATOM   4224 C  CA  . HIS B 1 263 ? -4.895  -31.145 13.202  1.00 28.29 ? 263 HIS A CA  1 
ATOM   4225 C  C   . HIS B 1 263 ? -5.439  -32.114 12.193  1.00 38.14 ? 263 HIS A C   1 
ATOM   4226 O  O   . HIS B 1 263 ? -4.675  -32.771 11.461  1.00 39.43 ? 263 HIS A O   1 
ATOM   4227 C  CB  . HIS B 1 263 ? -3.950  -31.902 14.155  1.00 31.10 ? 263 HIS A CB  1 
ATOM   4228 C  CG  . HIS B 1 263 ? -4.628  -32.886 15.074  1.00 33.80 ? 263 HIS A CG  1 
ATOM   4229 N  ND1 . HIS B 1 263 ? -3.920  -33.728 15.878  1.00 38.30 ? 263 HIS A ND1 1 
ATOM   4230 C  CD2 . HIS B 1 263 ? -5.970  -33.134 15.341  1.00 38.92 ? 263 HIS A CD2 1 
ATOM   4231 C  CE1 . HIS B 1 263 ? -4.781  -34.469 16.622  1.00 39.87 ? 263 HIS A CE1 1 
ATOM   4232 N  NE2 . HIS B 1 263 ? -6.032  -34.123 16.275  1.00 40.97 ? 263 HIS A NE2 1 
ATOM   4233 O  OXT . HIS B 1 263 ? -6.657  -32.277 12.100  1.00 32.85 ? 263 HIS A OXT 1 
HETATM 4234 ZN ZN  . ZN  C 2 .   ? -34.192 -35.825 27.012  1.00 10.81 ? 301 ZN  B ZN  1 
HETATM 4235 C  C1  . PEG D 3 .   ? -25.751 -52.295 19.895  1.00 25.38 ? 302 PEG B C1  1 
HETATM 4236 O  O1  . PEG D 3 .   ? -26.268 -53.202 20.794  1.00 24.48 ? 302 PEG B O1  1 
HETATM 4237 C  C2  . PEG D 3 .   ? -25.706 -52.341 18.339  1.00 23.77 ? 302 PEG B C2  1 
HETATM 4238 O  O2  . PEG D 3 .   ? -26.762 -52.689 17.483  1.00 28.36 ? 302 PEG B O2  1 
HETATM 4239 C  C3  . PEG D 3 .   ? -26.941 -53.851 16.683  1.00 31.18 ? 302 PEG B C3  1 
HETATM 4240 C  C4  . PEG D 3 .   ? -28.264 -54.387 16.223  1.00 32.63 ? 302 PEG B C4  1 
HETATM 4241 O  O4  . PEG D 3 .   ? -29.263 -55.050 17.058  1.00 33.46 ? 302 PEG B O4  1 
HETATM 4242 F  F26 . V1F E 4 .   ? -37.130 -36.216 25.533  1.00 17.57 ? 303 V1F B F26 1 
HETATM 4243 C  C5  . V1F E 4 .   ? -36.938 -35.995 24.216  1.00 17.81 ? 303 V1F B C5  1 
HETATM 4244 C  C4  . V1F E 4 .   ? -35.780 -36.286 23.539  1.00 16.74 ? 303 V1F B C4  1 
HETATM 4245 S  S7  . V1F E 4 .   ? -34.323 -36.934 24.353  1.00 17.94 ? 303 V1F B S7  1 
HETATM 4246 O  O9  . V1F E 4 .   ? -33.426 -35.878 24.487  1.00 17.15 ? 303 V1F B O9  1 
HETATM 4247 N  N10 . V1F E 4 .   ? -34.648 -37.456 26.002  1.00 17.76 ? 303 V1F B N10 1 
HETATM 4248 O  O8  . V1F E 4 .   ? -34.066 -38.065 23.606  1.00 15.30 ? 303 V1F B O8  1 
HETATM 4249 C  C3  . V1F E 4 .   ? -35.721 -36.009 22.186  1.00 18.39 ? 303 V1F B C3  1 
HETATM 4250 F  F12 . V1F E 4 .   ? -34.572 -36.304 21.508  1.00 18.32 ? 303 V1F B F12 1 
HETATM 4251 C  C2  . V1F E 4 .   ? -36.809 -35.502 21.544  1.00 22.07 ? 303 V1F B C2  1 
HETATM 4252 F  F13 . V1F E 4 .   ? -36.699 -35.218 20.200  1.00 22.69 ? 303 V1F B F13 1 
HETATM 4253 C  C6  . V1F E 4 .   ? -38.040 -35.396 23.571  1.00 19.89 ? 303 V1F B C6  1 
HETATM 4254 C  C1  . V1F E 4 .   ? -37.953 -35.219 22.181  1.00 20.98 ? 303 V1F B C1  1 
HETATM 4255 S  S11 . V1F E 4 .   ? -39.432 -34.627 21.287  1.00 27.75 ? 303 V1F B S11 1 
HETATM 4256 O  O22 . V1F E 4 .   ? -38.954 -33.827 20.078  1.00 38.30 ? 303 V1F B O22 1 
HETATM 4257 O  O23 . V1F E 4 .   ? -40.227 -33.651 22.155  1.00 28.80 ? 303 V1F B O23 1 
HETATM 4258 C  C21 . V1F E 4 .   ? -40.672 -35.945 21.146  1.00 32.95 ? 303 V1F B C21 1 
HETATM 4259 C  C24 . V1F E 4 .   ? -40.012 -37.229 20.688  1.00 35.95 ? 303 V1F B C24 1 
HETATM 4260 C  C30 . V1F E 4 .   ? -40.552 -37.601 19.329  1.00 35.89 ? 303 V1F B C30 1 
HETATM 4261 C  C29 . V1F E 4 .   ? -39.706 -37.532 18.191  1.00 38.40 ? 303 V1F B C29 1 
HETATM 4262 C  C28 . V1F E 4 .   ? -40.143 -37.894 16.888  1.00 34.14 ? 303 V1F B C28 1 
HETATM 4263 C  C32 . V1F E 4 .   ? -41.881 -38.046 19.172  1.00 39.56 ? 303 V1F B C32 1 
HETATM 4264 C  C31 . V1F E 4 .   ? -42.338 -38.414 17.876  1.00 39.83 ? 303 V1F B C31 1 
HETATM 4265 C  C27 . V1F E 4 .   ? -41.479 -38.339 16.736  1.00 41.93 ? 303 V1F B C27 1 
HETATM 4266 N  N25 . V1F E 4 .   ? -39.246 -35.176 24.277  1.00 21.34 ? 303 V1F B N25 1 
HETATM 4267 C  C14 . V1F E 4 .   ? -40.121 -34.088 24.718  1.00 40.26 ? 303 V1F B C14 1 
HETATM 4268 C  C15 . V1F E 4 .   ? -41.608 -34.408 24.464  1.00 44.86 ? 303 V1F B C15 1 
HETATM 4269 C  C20 . V1F E 4 .   ? -42.180 -35.661 24.863  1.00 40.29 ? 303 V1F B C20 1 
HETATM 4270 C  C19 . V1F E 4 .   ? -43.551 -35.874 24.537  1.00 57.98 ? 303 V1F B C19 1 
HETATM 4271 C  C18 . V1F E 4 .   ? -44.362 -34.891 23.873  1.00 54.50 ? 303 V1F B C18 1 
HETATM 4272 C  C17 . V1F E 4 .   ? -43.773 -33.666 23.478  1.00 50.84 ? 303 V1F B C17 1 
HETATM 4273 C  C16 . V1F E 4 .   ? -42.413 -33.447 23.799  1.00 32.88 ? 303 V1F B C16 1 
HETATM 4274 C  C1  . EDO F 5 .   ? -37.285 -41.200 40.809  1.00 32.19 ? 304 EDO B C1  1 
HETATM 4275 O  O1  . EDO F 5 .   ? -36.347 -40.060 40.999  1.00 25.12 ? 304 EDO B O1  1 
HETATM 4276 C  C2  . EDO F 5 .   ? -36.697 -42.586 40.307  1.00 32.16 ? 304 EDO B C2  1 
HETATM 4277 O  O2  . EDO F 5 .   ? -35.265 -42.875 40.466  1.00 31.93 ? 304 EDO B O2  1 
HETATM 4278 ZN ZN  . ZN  G 2 .   ? -6.781  -4.585  13.179  1.00 12.73 ? 301 ZN  A ZN  1 
HETATM 4279 C  C1  . CIT H 6 .   ? 1.636   -0.423  0.866   1.00 63.70 ? 302 CIT A C1  1 
HETATM 4280 O  O1  . CIT H 6 .   ? 0.934   0.485   0.349   1.00 67.76 ? 302 CIT A O1  1 
HETATM 4281 O  O2  . CIT H 6 .   ? 2.699   -0.203  1.305   1.00 73.02 ? 302 CIT A O2  1 
HETATM 4282 C  C2  . CIT H 6 .   ? 1.194   -1.857  1.024   1.00 51.54 ? 302 CIT A C2  1 
HETATM 4283 C  C3  . CIT H 6 .   ? 1.144   -2.655  -0.278  1.00 46.35 ? 302 CIT A C3  1 
HETATM 4284 O  O7  . CIT H 6 .   ? 2.349   -2.541  -1.010  1.00 50.46 ? 302 CIT A O7  1 
HETATM 4285 C  C4  . CIT H 6 .   ? 1.000   -4.161  -0.132  1.00 35.47 ? 302 CIT A C4  1 
HETATM 4286 C  C5  . CIT H 6 .   ? 2.340   -4.559  0.306   1.00 47.76 ? 302 CIT A C5  1 
HETATM 4287 O  O3  . CIT H 6 .   ? 3.199   -4.803  -0.593  1.00 55.54 ? 302 CIT A O3  1 
HETATM 4288 O  O4  . CIT H 6 .   ? 2.507   -4.625  1.542   1.00 36.48 ? 302 CIT A O4  1 
HETATM 4289 C  C6  . CIT H 6 .   ? 0.007   -2.100  -1.029  1.00 40.55 ? 302 CIT A C6  1 
HETATM 4290 O  O5  . CIT H 6 .   ? 0.225   -1.549  -2.079  1.00 37.82 ? 302 CIT A O5  1 
HETATM 4291 O  O6  . CIT H 6 .   ? -1.100  -2.233  -0.583  1.00 29.22 ? 302 CIT A O6  1 
HETATM 4292 F  F26 . V1F I 4 .   ? -6.553  -1.680  14.746  1.00 21.19 ? 303 V1F A F26 1 
HETATM 4293 C  C5  . V1F I 4 .   ? -6.959  -1.815  15.918  1.00 23.13 ? 303 V1F A C5  1 
HETATM 4294 C  C4  . V1F I 4 .   ? -6.775  -3.068  16.684  1.00 20.65 ? 303 V1F A C4  1 
HETATM 4295 S  S7  . V1F I 4 .   ? -6.076  -4.530  15.934  1.00 20.64 ? 303 V1F A S7  1 
HETATM 4296 O  O9  . V1F I 4 .   ? -7.100  -5.647  15.680  1.00 21.68 ? 303 V1F A O9  1 
HETATM 4297 N  N10 . V1F I 4 .   ? -5.230  -4.323  14.400  1.00 21.45 ? 303 V1F A N10 1 
HETATM 4298 O  O8  . V1F I 4 .   ? -5.064  -5.236  16.850  1.00 18.41 ? 303 V1F A O8  1 
HETATM 4299 C  C3  . V1F I 4 .   ? -7.233  -3.127  17.987  1.00 21.57 ? 303 V1F A C3  1 
HETATM 4300 F  F12 . V1F I 4 .   ? -7.093  -4.259  18.664  1.00 20.76 ? 303 V1F A F12 1 
HETATM 4301 C  C2  . V1F I 4 .   ? -7.805  -2.048  18.627  1.00 25.17 ? 303 V1F A C2  1 
HETATM 4302 F  F13 . V1F I 4 .   ? -8.204  -2.175  19.897  1.00 26.16 ? 303 V1F A F13 1 
HETATM 4303 C  C6  . V1F I 4 .   ? -7.544  -0.775  16.629  1.00 26.29 ? 303 V1F A C6  1 
HETATM 4304 C  C1  . V1F I 4 .   ? -7.970  -0.861  17.945  1.00 28.37 ? 303 V1F A C1  1 
HETATM 4305 S  S11 . V1F I 4 .   ? -8.668  0.600   18.665  1.00 35.48 ? 303 V1F A S11 1 
HETATM 4306 O  O22 . V1F I 4 .   ? -9.500  0.246   19.914  1.00 42.39 ? 303 V1F A O22 1 
HETATM 4307 O  O23 . V1F I 4 .   ? -9.709  1.252   17.763  1.00 33.90 ? 303 V1F A O23 1 
HETATM 4308 C  C21 . V1F I 4 .   ? -7.439  1.930   18.977  1.00 42.84 ? 303 V1F A C21 1 
HETATM 4309 C  C24 . V1F I 4 .   ? -6.249  1.335   19.720  1.00 47.12 ? 303 V1F A C24 1 
HETATM 4310 C  C30 . V1F I 4 .   ? -6.062  1.809   21.144  1.00 48.73 ? 303 V1F A C30 1 
HETATM 4311 C  C29 . V1F I 4 .   ? -6.024  0.854   22.194  1.00 46.46 ? 303 V1F A C29 1 
HETATM 4312 C  C28 . V1F I 4 .   ? -5.819  1.280   23.518  1.00 47.32 ? 303 V1F A C28 1 
HETATM 4313 C  C32 . V1F I 4 .   ? -5.881  3.184   21.453  1.00 49.21 ? 303 V1F A C32 1 
HETATM 4314 C  C31 . V1F I 4 .   ? -5.687  3.609   22.775  1.00 50.26 ? 303 V1F A C31 1 
HETATM 4315 C  C27 . V1F I 4 .   ? -5.655  2.646   23.810  1.00 54.62 ? 303 V1F A C27 1 
HETATM 4316 N  N25 . V1F I 4 .   ? -7.642  0.399   15.902  1.00 27.62 ? 303 V1F A N25 1 
HETATM 4317 C  C14 . V1F I 4 .   ? -8.702  0.980   15.115  1.00 46.30 ? 303 V1F A C14 1 
HETATM 4318 C  C15 . V1F I 4 .   ? -8.412  2.460   15.452  1.00 59.54 ? 303 V1F A C15 1 
HETATM 4319 C  C20 . V1F I 4 .   ? -7.117  3.015   15.143  1.00 57.82 ? 303 V1F A C20 1 
HETATM 4320 C  C19 . V1F I 4 .   ? -6.830  4.362   15.496  1.00 67.13 ? 303 V1F A C19 1 
HETATM 4321 C  C18 . V1F I 4 .   ? -7.799  5.185   16.140  1.00 72.29 ? 303 V1F A C18 1 
HETATM 4322 C  C17 . V1F I 4 .   ? -9.076  4.653   16.462  1.00 68.25 ? 303 V1F A C17 1 
HETATM 4323 C  C16 . V1F I 4 .   ? -9.375  3.308   16.120  1.00 56.42 ? 303 V1F A C16 1 
HETATM 4324 C  C1  . EDO J 5 .   ? -20.527 -1.433  -3.657  1.00 38.52 ? 304 EDO A C1  1 
HETATM 4325 O  O1  . EDO J 5 .   ? -21.932 -1.261  -3.503  1.00 40.82 ? 304 EDO A O1  1 
HETATM 4326 C  C2  . EDO J 5 .   ? -20.370 -2.746  -4.397  1.00 34.08 ? 304 EDO A C2  1 
HETATM 4327 O  O2  . EDO J 5 .   ? -20.243 -2.381  -5.786  1.00 37.45 ? 304 EDO A O2  1 
HETATM 4328 C  C1  . EDO K 5 .   ? -16.654 6.570   0.088   1.00 29.88 ? 305 EDO A C1  1 
HETATM 4329 O  O1  . EDO K 5 .   ? -15.931 7.222   1.122   1.00 36.78 ? 305 EDO A O1  1 
HETATM 4330 C  C2  . EDO K 5 .   ? -17.180 7.609   -0.903  1.00 37.92 ? 305 EDO A C2  1 
HETATM 4331 O  O2  . EDO K 5 .   ? -16.127 8.091   -1.730  1.00 46.03 ? 305 EDO A O2  1 
HETATM 4332 C  C1  . EDO L 5 .   ? -0.698  -14.725 -1.563  1.00 30.53 ? 306 EDO A C1  1 
HETATM 4333 O  O1  . EDO L 5 .   ? -0.694  -13.312 -1.655  1.00 30.39 ? 306 EDO A O1  1 
HETATM 4334 C  C2  . EDO L 5 .   ? -0.911  -15.338 -2.941  1.00 41.30 ? 306 EDO A C2  1 
HETATM 4335 O  O2  . EDO L 5 .   ? -0.746  -16.745 -2.752  1.00 44.87 ? 306 EDO A O2  1 
HETATM 4336 O  O   . HOH M 7 .   ? -22.213 -32.095 31.392  1.00 13.86 ? 401 HOH B O   1 
HETATM 4337 O  O   . HOH M 7 .   ? -17.085 -31.134 29.299  1.00 17.77 ? 402 HOH B O   1 
HETATM 4338 O  O   . HOH M 7 .   ? -37.045 -40.030 29.817  1.00 12.23 ? 403 HOH B O   1 
HETATM 4339 O  O   . HOH M 7 .   ? -33.343 -34.274 40.821  1.00 12.20 ? 404 HOH B O   1 
HETATM 4340 O  O   . HOH M 7 .   ? -34.759 -28.231 6.051   1.00 14.78 ? 405 HOH B O   1 
HETATM 4341 O  O   . HOH M 7 .   ? -28.346 -27.739 9.966   1.00 14.49 ? 406 HOH B O   1 
HETATM 4342 O  O   . HOH M 7 .   ? -30.054 -40.502 38.147  1.00 20.40 ? 407 HOH B O   1 
HETATM 4343 O  O   . HOH M 7 .   ? -27.597 -39.935 14.587  1.00 16.48 ? 408 HOH B O   1 
HETATM 4344 O  O   . HOH M 7 .   ? -31.843 -42.297 35.028  1.00 16.94 ? 409 HOH B O   1 
HETATM 4345 O  O   . HOH M 7 .   ? -29.843 -51.052 24.555  1.00 17.94 ? 410 HOH B O   1 
HETATM 4346 O  O   . HOH M 7 .   ? -28.794 -45.688 17.272  1.00 23.95 ? 411 HOH B O   1 
HETATM 4347 O  O   . HOH M 7 .   ? -24.500 -17.272 20.553  1.00 16.96 ? 412 HOH B O   1 
HETATM 4348 O  O   . HOH M 7 .   ? -31.565 -22.464 13.057  1.00 16.36 ? 413 HOH B O   1 
HETATM 4349 O  O   . HOH M 7 .   ? -34.198 -49.733 15.794  1.00 21.26 ? 414 HOH B O   1 
HETATM 4350 O  O   . HOH M 7 .   ? -40.222 -34.112 45.065  1.00 20.90 ? 415 HOH B O   1 
HETATM 4351 O  O   . HOH M 7 .   ? -33.045 -23.674 15.010  1.00 15.68 ? 416 HOH B O   1 
HETATM 4352 O  O   . HOH M 7 .   ? -38.824 -30.026 10.983  1.00 20.21 ? 417 HOH B O   1 
HETATM 4353 O  O   . HOH M 7 .   ? -20.304 -31.975 10.992  1.00 21.20 ? 418 HOH B O   1 
HETATM 4354 O  O   . HOH M 7 .   ? -38.551 -40.783 36.690  1.00 14.92 ? 419 HOH B O   1 
HETATM 4355 O  O   . HOH M 7 .   ? -34.366 -38.704 42.717  1.00 24.35 ? 420 HOH B O   1 
HETATM 4356 O  O   . HOH M 7 .   ? -25.080 -36.475 7.166   1.00 27.21 ? 421 HOH B O   1 
HETATM 4357 O  O   . HOH M 7 .   ? -43.166 -37.741 37.810  1.00 21.30 ? 422 HOH B O   1 
HETATM 4358 O  O   . HOH M 7 .   ? -27.431 -44.073 15.397  1.00 20.58 ? 423 HOH B O   1 
HETATM 4359 O  O   . HOH M 7 .   ? -25.012 -54.950 28.145  1.00 25.01 ? 424 HOH B O   1 
HETATM 4360 O  O   . HOH M 7 .   ? -32.506 -52.582 18.525  1.00 22.00 ? 425 HOH B O   1 
HETATM 4361 O  O   . HOH M 7 .   ? -48.549 -35.827 42.000  1.00 23.09 ? 426 HOH B O   1 
HETATM 4362 O  O   . HOH M 7 .   ? -23.601 -37.951 11.497  1.00 17.73 ? 427 HOH B O   1 
HETATM 4363 O  O   . HOH M 7 .   ? -42.486 -25.298 23.139  1.00 18.12 ? 428 HOH B O   1 
HETATM 4364 O  O   . HOH M 7 .   ? -35.840 -47.419 16.193  1.00 17.19 ? 429 HOH B O   1 
HETATM 4365 O  O   . HOH M 7 .   ? -45.080 -37.302 32.131  1.00 18.61 ? 430 HOH B O   1 
HETATM 4366 O  O   . HOH M 7 .   ? -38.836 -24.053 4.717   1.00 19.65 ? 431 HOH B O   1 
HETATM 4367 O  O   . HOH M 7 .   ? -17.118 -34.249 12.413  1.00 23.82 ? 432 HOH B O   1 
HETATM 4368 O  O   . HOH M 7 .   ? -28.803 -25.703 46.917  1.00 16.27 ? 433 HOH B O   1 
HETATM 4369 O  O   . HOH M 7 .   ? -19.048 -36.404 34.263  1.00 21.96 ? 434 HOH B O   1 
HETATM 4370 O  O   . HOH M 7 .   ? -28.556 -27.922 48.546  1.00 22.32 ? 435 HOH B O   1 
HETATM 4371 O  O   . HOH M 7 .   ? -25.157 -52.738 32.454  1.00 17.21 ? 436 HOH B O   1 
HETATM 4372 O  O   . HOH M 7 .   ? -44.380 -17.561 34.877  1.00 25.86 ? 437 HOH B O   1 
HETATM 4373 O  O   . HOH M 7 .   ? -30.618 -20.216 49.434  1.00 18.83 ? 438 HOH B O   1 
HETATM 4374 O  O   . HOH M 7 .   ? -38.392 -38.471 46.852  1.00 22.61 ? 439 HOH B O   1 
HETATM 4375 O  O   . HOH M 7 .   ? -20.839 -41.913 18.560  1.00 25.70 ? 440 HOH B O   1 
HETATM 4376 O  O   . HOH M 7 .   ? -19.841 -21.062 19.974  1.00 18.01 ? 441 HOH B O   1 
HETATM 4377 O  O   . HOH M 7 .   ? -30.154 -47.481 14.733  1.00 21.89 ? 442 HOH B O   1 
HETATM 4378 O  O   . HOH M 7 .   ? -31.720 -17.275 38.252  1.00 23.88 ? 443 HOH B O   1 
HETATM 4379 O  O   . HOH M 7 .   ? -15.565 -24.792 16.483  1.00 20.03 ? 444 HOH B O   1 
HETATM 4380 O  O   . HOH M 7 .   ? -16.242 -22.523 26.358  1.00 17.46 ? 445 HOH B O   1 
HETATM 4381 O  O   . HOH M 7 .   ? -24.309 -22.745 33.004  1.00 22.19 ? 446 HOH B O   1 
HETATM 4382 O  O   . HOH M 7 .   ? -35.097 -19.496 40.744  1.00 27.89 ? 447 HOH B O   1 
HETATM 4383 O  O   . HOH M 7 .   ? -40.109 -50.704 29.271  1.00 26.57 ? 448 HOH B O   1 
HETATM 4384 O  O   . HOH M 7 .   ? -31.925 -38.194 2.024   1.00 20.76 ? 449 HOH B O   1 
HETATM 4385 O  O   . HOH M 7 .   ? -41.334 -47.300 35.809  1.00 30.17 ? 450 HOH B O   1 
HETATM 4386 O  O   . HOH M 7 .   ? -21.503 -28.745 7.782   1.00 26.27 ? 451 HOH B O   1 
HETATM 4387 O  O   . HOH M 7 .   ? -31.331 -16.237 28.070  1.00 25.89 ? 452 HOH B O   1 
HETATM 4388 O  O   . HOH M 7 .   ? -21.898 -21.624 8.454   1.00 25.27 ? 453 HOH B O   1 
HETATM 4389 O  O   . HOH M 7 .   ? -54.218 -30.434 36.264  1.00 26.64 ? 454 HOH B O   1 
HETATM 4390 O  O   . HOH M 7 .   ? -42.416 -16.712 19.383  1.00 22.07 ? 455 HOH B O   1 
HETATM 4391 O  O   . HOH M 7 .   ? -33.683 -19.258 38.524  1.00 19.50 ? 456 HOH B O   1 
HETATM 4392 O  O   . HOH M 7 .   ? -12.566 -55.502 27.998  1.00 23.17 ? 457 HOH B O   1 
HETATM 4393 O  O   . HOH M 7 .   ? -21.477 -49.088 36.858  1.00 27.18 ? 458 HOH B O   1 
HETATM 4394 O  O   . HOH M 7 .   ? -25.643 -18.162 10.500  1.00 24.61 ? 459 HOH B O   1 
HETATM 4395 O  O   . HOH M 7 .   ? -34.138 -33.101 46.971  1.00 30.03 ? 460 HOH B O   1 
HETATM 4396 O  O   . HOH M 7 .   ? -21.609 -19.654 41.545  1.00 27.52 ? 461 HOH B O   1 
HETATM 4397 O  O   . HOH M 7 .   ? -29.885 -21.377 47.014  1.00 20.77 ? 462 HOH B O   1 
HETATM 4398 O  O   . HOH M 7 .   ? -10.505 -35.912 18.473  1.00 30.59 ? 463 HOH B O   1 
HETATM 4399 O  O   . HOH M 7 .   ? -13.337 -40.838 29.858  1.00 24.61 ? 464 HOH B O   1 
HETATM 4400 O  O   . HOH M 7 .   ? -28.853 -11.996 19.759  1.00 20.45 ? 465 HOH B O   1 
HETATM 4401 O  O   . HOH M 7 .   ? -18.294 -19.173 49.590  1.00 21.54 ? 466 HOH B O   1 
HETATM 4402 O  O   . HOH M 7 .   ? -14.461 -46.785 35.075  1.00 24.71 ? 467 HOH B O   1 
HETATM 4403 O  O   . HOH M 7 .   ? -26.373 -24.525 46.421  1.00 24.20 ? 468 HOH B O   1 
HETATM 4404 O  O   . HOH M 7 .   ? -29.296 -12.917 17.133  1.00 24.67 ? 469 HOH B O   1 
HETATM 4405 O  O   . HOH M 7 .   ? -40.837 -31.895 11.929  1.00 23.35 ? 470 HOH B O   1 
HETATM 4406 O  O   . HOH M 7 .   ? -27.037 -21.985 47.255  1.00 25.13 ? 471 HOH B O   1 
HETATM 4407 O  O   . HOH M 7 .   ? -26.658 -15.189 14.330  1.00 19.31 ? 472 HOH B O   1 
HETATM 4408 O  O   . HOH M 7 .   ? -33.427 -51.540 27.086  1.00 28.07 ? 473 HOH B O   1 
HETATM 4409 O  O   . HOH M 7 .   ? -24.294 -39.962 42.589  1.00 22.46 ? 474 HOH B O   1 
HETATM 4410 O  O   . HOH M 7 .   ? -36.457 -19.023 50.355  1.00 30.70 ? 475 HOH B O   1 
HETATM 4411 O  O   . HOH M 7 .   ? -38.434 -48.381 16.572  1.00 23.63 ? 476 HOH B O   1 
HETATM 4412 O  O   . HOH M 7 .   ? -17.135 -48.380 25.805  1.00 27.11 ? 477 HOH B O   1 
HETATM 4413 O  O   . HOH M 7 .   ? -31.432 -16.438 32.360  1.00 26.26 ? 478 HOH B O   1 
HETATM 4414 O  O   . HOH M 7 .   ? -22.463 -23.581 36.572  1.00 28.27 ? 479 HOH B O   1 
HETATM 4415 O  O   . HOH M 7 .   ? -22.152 -45.738 35.502  1.00 20.57 ? 480 HOH B O   1 
HETATM 4416 O  O   . HOH M 7 .   ? -41.302 -49.626 19.538  1.00 26.16 ? 481 HOH B O   1 
HETATM 4417 O  O   . HOH M 7 .   ? -21.902 -25.249 14.103  1.00 22.85 ? 482 HOH B O   1 
HETATM 4418 O  O   . HOH M 7 .   ? -24.780 -39.225 7.670   1.00 25.82 ? 483 HOH B O   1 
HETATM 4419 O  O   . HOH M 7 .   ? -18.021 -24.138 35.734  1.00 39.00 ? 484 HOH B O   1 
HETATM 4420 O  O   . HOH M 7 .   ? -45.193 -24.295 37.522  1.00 33.00 ? 485 HOH B O   1 
HETATM 4421 O  O   . HOH M 7 .   ? -19.787 -25.525 34.471  1.00 26.48 ? 486 HOH B O   1 
HETATM 4422 O  O   . HOH M 7 .   ? -26.192 -17.721 13.129  1.00 25.08 ? 487 HOH B O   1 
HETATM 4423 O  O   . HOH M 7 .   ? -20.090 -47.777 34.784  1.00 26.31 ? 488 HOH B O   1 
HETATM 4424 O  O   . HOH M 7 .   ? -29.934 -31.096 47.923  1.00 37.73 ? 489 HOH B O   1 
HETATM 4425 O  O   . HOH M 7 .   ? -35.216 -29.532 47.621  1.00 26.50 ? 490 HOH B O   1 
HETATM 4426 O  O   . HOH M 7 .   ? -14.662 -31.583 30.840  1.00 26.28 ? 491 HOH B O   1 
HETATM 4427 O  O   . HOH M 7 .   ? -38.486 -15.416 31.102  1.00 25.92 ? 492 HOH B O   1 
HETATM 4428 O  O   . HOH M 7 .   ? -40.725 -31.342 4.749   1.00 30.09 ? 493 HOH B O   1 
HETATM 4429 O  O   . HOH M 7 .   ? -48.532 -35.921 30.406  1.00 28.95 ? 494 HOH B O   1 
HETATM 4430 O  O   . HOH M 7 .   ? -23.299 -39.608 13.705  1.00 27.47 ? 495 HOH B O   1 
HETATM 4431 O  O   . HOH M 7 .   ? -24.481 -18.055 42.146  1.00 31.97 ? 496 HOH B O   1 
HETATM 4432 O  O   . HOH M 7 .   ? -42.741 -29.036 22.018  1.00 36.38 ? 497 HOH B O   1 
HETATM 4433 O  O   . HOH M 7 .   ? -40.429 -47.178 18.401  1.00 24.94 ? 498 HOH B O   1 
HETATM 4434 O  O   . HOH M 7 .   ? -25.906 -27.493 4.278   1.00 34.15 ? 499 HOH B O   1 
HETATM 4435 O  O   . HOH M 7 .   ? -21.380 -23.499 33.920  1.00 36.15 ? 500 HOH B O   1 
HETATM 4436 O  O   . HOH M 7 .   ? -45.400 -37.461 36.751  1.00 32.60 ? 501 HOH B O   1 
HETATM 4437 O  O   . HOH M 7 .   ? -36.745 -54.687 20.945  1.00 39.16 ? 502 HOH B O   1 
HETATM 4438 O  O   . HOH M 7 .   ? -41.706 -26.851 43.624  1.00 31.29 ? 503 HOH B O   1 
HETATM 4439 O  O   . HOH M 7 .   ? -56.804 -25.471 26.578  1.00 31.90 ? 504 HOH B O   1 
HETATM 4440 O  O   . HOH M 7 .   ? -36.867 -32.751 46.631  1.00 33.65 ? 505 HOH B O   1 
HETATM 4441 O  O   . HOH M 7 .   ? -18.285 -27.935 36.626  1.00 28.58 ? 506 HOH B O   1 
HETATM 4442 O  O   . HOH M 7 .   ? -18.892 -46.110 41.555  1.00 30.71 ? 507 HOH B O   1 
HETATM 4443 O  O   . HOH M 7 .   ? -20.304 -39.217 11.211  1.00 31.10 ? 508 HOH B O   1 
HETATM 4444 O  O   . HOH M 7 .   ? -14.314 -33.160 19.130  1.00 25.17 ? 509 HOH B O   1 
HETATM 4445 O  O   . HOH M 7 .   ? -42.245 -19.131 37.346  1.00 28.63 ? 510 HOH B O   1 
HETATM 4446 O  O   . HOH M 7 .   ? -36.855 -13.642 32.483  1.00 29.79 ? 511 HOH B O   1 
HETATM 4447 O  O   . HOH M 7 .   ? -14.233 -47.022 23.383  1.00 32.18 ? 512 HOH B O   1 
HETATM 4448 O  O   . HOH M 7 .   ? -19.162 -52.206 19.226  1.00 35.75 ? 513 HOH B O   1 
HETATM 4449 O  O   . HOH M 7 .   ? -19.584 -33.086 7.500   1.00 33.14 ? 514 HOH B O   1 
HETATM 4450 O  O   . HOH M 7 .   ? -29.307 -18.251 29.491  1.00 31.98 ? 515 HOH B O   1 
HETATM 4451 O  O   . HOH M 7 .   ? -26.140 -17.809 23.021  1.00 26.74 ? 516 HOH B O   1 
HETATM 4452 O  O   . HOH M 7 .   ? -31.798 -23.850 49.929  1.00 27.78 ? 517 HOH B O   1 
HETATM 4453 O  O   . HOH M 7 .   ? -41.504 -14.054 19.031  1.00 34.12 ? 518 HOH B O   1 
HETATM 4454 O  O   . HOH M 7 .   ? -15.416 -53.114 35.429  1.00 36.51 ? 519 HOH B O   1 
HETATM 4455 O  O   . HOH M 7 .   ? -33.505 -45.281 13.104  1.00 32.53 ? 520 HOH B O   1 
HETATM 4456 O  O   . HOH M 7 .   ? -21.310 -28.111 43.720  1.00 31.72 ? 521 HOH B O   1 
HETATM 4457 O  O   . HOH M 7 .   ? -13.544 -28.317 25.032  1.00 21.90 ? 522 HOH B O   1 
HETATM 4458 O  O   . HOH M 7 .   ? -27.202 -46.983 14.684  1.00 33.15 ? 523 HOH B O   1 
HETATM 4459 O  O   . HOH M 7 .   ? -36.644 -13.124 18.175  1.00 32.17 ? 524 HOH B O   1 
HETATM 4460 O  O   . HOH M 7 .   ? -35.022 -26.566 47.977  1.00 24.55 ? 525 HOH B O   1 
HETATM 4461 O  O   . HOH M 7 .   ? -35.903 -45.774 13.880  1.00 28.75 ? 526 HOH B O   1 
HETATM 4462 O  O   . HOH M 7 .   ? -11.867 -34.238 20.093  1.00 25.33 ? 527 HOH B O   1 
HETATM 4463 O  O   . HOH M 7 .   ? -25.776 -33.072 41.999  1.00 24.57 ? 528 HOH B O   1 
HETATM 4464 O  O   . HOH M 7 .   ? -50.985 -21.571 26.378  1.00 26.89 ? 529 HOH B O   1 
HETATM 4465 O  O   . HOH M 7 .   ? -34.357 -54.437 28.290  1.00 43.58 ? 530 HOH B O   1 
HETATM 4466 O  O   . HOH M 7 .   ? -16.289 -55.005 31.703  1.00 33.13 ? 531 HOH B O   1 
HETATM 4467 O  O   . HOH M 7 .   ? -34.058 -13.706 31.927  1.00 44.51 ? 532 HOH B O   1 
HETATM 4468 O  O   . HOH M 7 .   ? -14.871 -25.747 25.561  1.00 29.90 ? 533 HOH B O   1 
HETATM 4469 O  O   . HOH M 7 .   ? -14.524 -24.564 34.924  1.00 37.10 ? 534 HOH B O   1 
HETATM 4470 O  O   . HOH M 7 .   ? -12.544 -32.234 23.796  1.00 32.21 ? 535 HOH B O   1 
HETATM 4471 O  O   . HOH M 7 .   ? -23.768 -32.936 4.654   1.00 29.26 ? 536 HOH B O   1 
HETATM 4472 O  O   . HOH M 7 .   ? -17.709 -47.614 36.256  1.00 33.37 ? 537 HOH B O   1 
HETATM 4473 O  O   . HOH M 7 .   ? -13.046 -38.967 32.491  1.00 29.02 ? 538 HOH B O   1 
HETATM 4474 O  O   . HOH M 7 .   ? -49.011 -19.232 29.055  1.00 37.37 ? 539 HOH B O   1 
HETATM 4475 O  O   . HOH M 7 .   ? -24.938 -42.511 16.267  1.00 26.26 ? 540 HOH B O   1 
HETATM 4476 O  O   . HOH M 7 .   ? -32.016 -53.413 26.057  1.00 30.83 ? 541 HOH B O   1 
HETATM 4477 O  O   . HOH M 7 .   ? -24.843 -25.178 8.489   1.00 27.63 ? 542 HOH B O   1 
HETATM 4478 O  O   . HOH M 7 .   ? -23.088 -29.162 5.864   1.00 26.58 ? 543 HOH B O   1 
HETATM 4479 O  O   . HOH M 7 .   ? -43.385 -15.217 27.681  1.00 30.86 ? 544 HOH B O   1 
HETATM 4480 O  O   . HOH M 7 .   ? -14.797 -38.817 34.503  1.00 36.35 ? 545 HOH B O   1 
HETATM 4481 O  O   . HOH M 7 .   ? -14.900 -30.199 22.839  1.00 36.77 ? 546 HOH B O   1 
HETATM 4482 O  O   . HOH M 7 .   ? -20.727 -26.207 7.397   1.00 27.38 ? 547 HOH B O   1 
HETATM 4483 O  O   . HOH M 7 .   ? -24.899 -22.405 9.089   1.00 28.39 ? 548 HOH B O   1 
HETATM 4484 O  O   . HOH M 7 .   ? -14.289 -30.302 20.294  1.00 27.27 ? 549 HOH B O   1 
HETATM 4485 O  O   . HOH M 7 .   ? -38.217 -46.004 12.518  1.00 31.78 ? 550 HOH B O   1 
HETATM 4486 O  O   . HOH M 7 .   ? -48.726 -25.858 23.788  1.00 28.58 ? 551 HOH B O   1 
HETATM 4487 O  O   . HOH M 7 .   ? -18.775 -53.836 32.175  1.00 27.40 ? 552 HOH B O   1 
HETATM 4488 O  O   . HOH M 7 .   ? -25.897 -43.082 40.928  1.00 29.11 ? 553 HOH B O   1 
HETATM 4489 O  O   . HOH M 7 .   ? -43.249 -55.302 24.144  1.00 35.12 ? 554 HOH B O   1 
HETATM 4490 O  O   . HOH M 7 .   ? -21.244 -24.058 43.346  1.00 36.44 ? 555 HOH B O   1 
HETATM 4491 O  O   . HOH M 7 .   ? -46.752 -15.566 25.472  1.00 28.33 ? 556 HOH B O   1 
HETATM 4492 O  O   . HOH M 7 .   ? -18.276 -54.691 22.531  1.00 39.09 ? 557 HOH B O   1 
HETATM 4493 O  O   . HOH M 7 .   ? -20.742 -22.344 27.178  1.00 31.22 ? 558 HOH B O   1 
HETATM 4494 O  O   . HOH M 7 .   ? -53.811 -27.308 29.994  1.00 30.01 ? 559 HOH B O   1 
HETATM 4495 O  O   . HOH M 7 .   ? -22.099 -54.463 26.370  1.00 31.51 ? 560 HOH B O   1 
HETATM 4496 O  O   . HOH M 7 .   ? -21.962 -19.372 30.790  1.00 28.86 ? 561 HOH B O   1 
HETATM 4497 O  O   . HOH M 7 .   ? -39.279 -26.646 16.865  1.00 30.33 ? 562 HOH B O   1 
HETATM 4498 O  O   . HOH M 7 .   ? -7.546  -33.781 25.405  1.00 35.78 ? 563 HOH B O   1 
HETATM 4499 O  O   . HOH M 7 .   ? -48.740 -54.661 24.916  1.00 28.31 ? 564 HOH B O   1 
HETATM 4500 O  O   . HOH M 7 .   ? -22.323 -42.735 16.370  1.00 31.97 ? 565 HOH B O   1 
HETATM 4501 O  O   . HOH M 7 .   ? -36.565 -43.422 36.726  1.00 31.51 ? 566 HOH B O   1 
HETATM 4502 O  O   . HOH M 7 .   ? -40.085 -12.325 18.172  1.00 38.12 ? 567 HOH B O   1 
HETATM 4503 O  O   . HOH M 7 .   ? -51.385 -19.392 28.089  1.00 42.13 ? 568 HOH B O   1 
HETATM 4504 O  O   . HOH M 7 .   ? -33.001 -19.930 13.308  1.00 29.83 ? 569 HOH B O   1 
HETATM 4505 O  O   . HOH M 7 .   ? -26.529 -23.087 5.544   1.00 31.62 ? 570 HOH B O   1 
HETATM 4506 O  O   . HOH M 7 .   ? -35.544 -16.937 13.498  1.00 36.42 ? 571 HOH B O   1 
HETATM 4507 O  O   . HOH M 7 .   ? -29.656 -13.779 13.288  1.00 40.35 ? 572 HOH B O   1 
HETATM 4508 O  O   . HOH M 7 .   ? -9.589  -34.428 14.126  1.00 39.16 ? 573 HOH B O   1 
HETATM 4509 O  O   . HOH M 7 .   ? -40.057 -23.097 12.685  1.00 34.67 ? 574 HOH B O   1 
HETATM 4510 O  O   . HOH M 7 .   ? -10.558 -40.945 27.317  1.00 43.98 ? 575 HOH B O   1 
HETATM 4511 O  O   . HOH M 7 .   ? -40.660 -26.130 13.019  1.00 29.46 ? 576 HOH B O   1 
HETATM 4512 O  O   . HOH M 7 .   ? -21.286 -41.411 14.255  1.00 33.57 ? 577 HOH B O   1 
HETATM 4513 O  O   . HOH M 7 .   ? -23.604 -36.985 42.427  1.00 45.04 ? 578 HOH B O   1 
HETATM 4514 O  O   . HOH M 7 .   ? -16.795 -37.329 35.396  1.00 29.36 ? 579 HOH B O   1 
HETATM 4515 O  O   . HOH M 7 .   ? -21.643 -38.495 43.839  1.00 36.02 ? 580 HOH B O   1 
HETATM 4516 O  O   . HOH M 7 .   ? -31.270 -11.824 20.829  1.00 35.39 ? 581 HOH B O   1 
HETATM 4517 O  O   . HOH M 7 .   ? -40.885 -14.656 31.870  1.00 32.89 ? 582 HOH B O   1 
HETATM 4518 O  O   . HOH M 7 .   ? -49.026 -42.434 24.076  1.00 46.60 ? 583 HOH B O   1 
HETATM 4519 O  O   . HOH M 7 .   ? -23.345 -39.901 9.751   1.00 26.81 ? 584 HOH B O   1 
HETATM 4520 O  O   . HOH M 7 .   ? -20.157 -21.718 31.031  1.00 40.12 ? 585 HOH B O   1 
HETATM 4521 O  O   . HOH M 7 .   ? -39.272 -53.201 18.277  1.00 36.27 ? 586 HOH B O   1 
HETATM 4522 O  O   . HOH M 7 .   ? -23.795 -21.313 37.965  1.00 46.13 ? 587 HOH B O   1 
HETATM 4523 O  O   . HOH M 7 .   ? -31.331 -17.959 41.211  1.00 29.25 ? 588 HOH B O   1 
HETATM 4524 O  O   . HOH M 7 .   ? -37.264 -49.237 32.485  1.00 32.75 ? 589 HOH B O   1 
HETATM 4525 O  O   . HOH M 7 .   ? -33.924 -24.973 50.300  1.00 43.27 ? 590 HOH B O   1 
HETATM 4526 O  O   . HOH M 7 .   ? -26.771 -35.356 42.508  1.00 32.41 ? 591 HOH B O   1 
HETATM 4527 O  O   . HOH M 7 .   ? -7.875  -43.677 25.375  1.00 38.88 ? 592 HOH B O   1 
HETATM 4528 O  O   . HOH M 7 .   ? -12.752 -45.238 37.000  1.00 38.71 ? 593 HOH B O   1 
HETATM 4529 O  O   . HOH M 7 .   ? -4.349  -36.095 19.686  1.00 43.26 ? 594 HOH B O   1 
HETATM 4530 O  O   . HOH M 7 .   ? -29.361 -16.949 39.985  1.00 33.99 ? 595 HOH B O   1 
HETATM 4531 O  O   . HOH M 7 .   ? -11.855 -29.227 20.394  1.00 34.01 ? 596 HOH B O   1 
HETATM 4532 O  O   . HOH M 7 .   ? -16.580 -29.665 37.309  1.00 33.40 ? 597 HOH B O   1 
HETATM 4533 O  O   . HOH M 7 .   ? -24.416 -25.254 47.432  1.00 35.53 ? 598 HOH B O   1 
HETATM 4534 O  O   . HOH M 7 .   ? -24.329 -42.475 12.214  1.00 44.02 ? 599 HOH B O   1 
HETATM 4535 O  O   . HOH M 7 .   ? -18.572 -26.209 38.737  1.00 36.87 ? 600 HOH B O   1 
HETATM 4536 O  O   . HOH M 7 .   ? -15.931 -31.677 35.509  1.00 43.13 ? 601 HOH B O   1 
HETATM 4537 O  O   . HOH M 7 .   ? -11.024 -31.651 18.874  1.00 36.61 ? 602 HOH B O   1 
HETATM 4538 O  O   . HOH M 7 .   ? -38.932 -50.941 16.341  1.00 30.25 ? 603 HOH B O   1 
HETATM 4539 O  O   . HOH M 7 .   ? -36.494 -51.880 15.147  1.00 38.70 ? 604 HOH B O   1 
HETATM 4540 O  O   . HOH M 7 .   ? -45.721 -38.549 34.352  1.00 27.43 ? 605 HOH B O   1 
HETATM 4541 O  O   . HOH M 7 .   ? -48.437 -39.104 33.552  1.00 29.79 ? 606 HOH B O   1 
HETATM 4542 O  O   . HOH M 7 .   ? -47.892 -38.578 31.212  1.00 37.09 ? 607 HOH B O   1 
HETATM 4543 O  O   . HOH M 7 .   ? -41.004 -32.720 26.852  1.00 22.83 ? 608 HOH B O   1 
HETATM 4544 O  O   . HOH M 7 .   ? -42.359 -34.150 17.815  1.00 38.93 ? 609 HOH B O   1 
HETATM 4545 O  O   . HOH M 7 .   ? -40.385 -30.247 20.987  1.00 43.12 ? 610 HOH B O   1 
HETATM 4546 O  O   . HOH M 7 .   ? -42.968 -18.233 17.035  1.00 32.44 ? 611 HOH B O   1 
HETATM 4547 O  O   . HOH M 7 .   ? -39.338 -28.587 18.521  1.00 39.72 ? 612 HOH B O   1 
HETATM 4548 O  O   . HOH M 7 .   ? -44.885 -29.177 24.002  1.00 38.29 ? 613 HOH B O   1 
HETATM 4549 O  O   . HOH M 7 .   ? -46.143 -26.030 20.248  1.00 42.49 ? 614 HOH B O   1 
HETATM 4550 O  O   . HOH M 7 .   ? -23.166 -31.145 44.340  1.00 34.02 ? 615 HOH B O   1 
HETATM 4551 O  O   . HOH M 7 .   ? -37.974 -51.607 28.728  1.00 38.05 ? 616 HOH B O   1 
HETATM 4552 O  O   . HOH M 7 .   ? -28.664 -34.808 1.069   1.00 35.87 ? 617 HOH B O   1 
HETATM 4553 O  O   . HOH M 7 .   ? -24.498 -35.655 4.695   1.00 38.31 ? 618 HOH B O   1 
HETATM 4554 O  O   . HOH M 7 .   ? -54.446 -27.392 37.264  1.00 34.88 ? 619 HOH B O   1 
HETATM 4555 O  O   . HOH M 7 .   ? -54.442 -34.180 42.889  1.00 32.70 ? 620 HOH B O   1 
HETATM 4556 O  O   . HOH M 7 .   ? -13.378 -53.455 26.390  1.00 38.29 ? 621 HOH B O   1 
HETATM 4557 O  O   . HOH M 7 .   ? -11.058 -29.181 25.798  1.00 41.35 ? 622 HOH B O   1 
HETATM 4558 O  O   . HOH M 7 .   ? -13.389 -26.874 32.627  1.00 42.80 ? 623 HOH B O   1 
HETATM 4559 O  O   . HOH M 7 .   ? -24.772 -17.910 38.129  1.00 31.08 ? 624 HOH B O   1 
HETATM 4560 O  O   . HOH M 7 .   ? -26.643 -16.780 40.373  1.00 34.75 ? 625 HOH B O   1 
HETATM 4561 O  O   . HOH M 7 .   ? -42.186 -34.963 7.760   1.00 34.37 ? 626 HOH B O   1 
HETATM 4562 O  O   . HOH M 7 .   ? -23.697 -15.748 42.384  1.00 35.94 ? 627 HOH B O   1 
HETATM 4563 O  O   . HOH M 7 .   ? -2.094  -34.455 20.482  1.00 42.79 ? 628 HOH B O   1 
HETATM 4564 O  O   . HOH M 7 .   ? -26.562 -48.556 12.024  1.00 38.50 ? 629 HOH B O   1 
HETATM 4565 O  O   . HOH M 7 .   ? -25.533 -37.510 44.121  1.00 36.62 ? 630 HOH B O   1 
HETATM 4566 O  O   . HOH M 7 .   ? -48.103 -39.124 27.287  1.00 42.72 ? 631 HOH B O   1 
HETATM 4567 O  O   . HOH M 7 .   ? -49.201 -36.343 25.630  1.00 38.79 ? 632 HOH B O   1 
HETATM 4568 O  O   . HOH M 7 .   ? -27.476 -18.950 8.399   1.00 38.19 ? 633 HOH B O   1 
HETATM 4569 O  O   . HOH M 7 .   ? -31.069 -11.603 14.659  1.00 41.39 ? 634 HOH B O   1 
HETATM 4570 O  O   . HOH M 7 .   ? -38.859 -14.557 28.527  1.00 27.86 ? 635 HOH B O   1 
HETATM 4571 O  O   . HOH M 7 .   ? -38.973 -13.944 25.383  1.00 25.87 ? 636 HOH B O   1 
HETATM 4572 O  O   . HOH M 7 .   ? -39.785 -35.168 27.041  1.00 27.67 ? 637 HOH B O   1 
HETATM 4573 O  O   . HOH M 7 .   ? -39.308 -36.219 29.570  1.00 17.01 ? 638 HOH B O   1 
HETATM 4574 O  O   . HOH M 7 .   ? -42.144 -37.775 22.911  1.00 30.00 ? 639 HOH B O   1 
HETATM 4575 O  O   . HOH N 7 .   ? -4.980  -12.342 -2.078  1.00 26.91 ? 401 HOH A O   1 
HETATM 4576 O  O   . HOH N 7 .   ? 12.081  0.821   19.069  1.00 35.88 ? 402 HOH A O   1 
HETATM 4577 O  O   . HOH N 7 .   ? -2.019  -2.025  10.994  1.00 13.72 ? 403 HOH A O   1 
HETATM 4578 O  O   . HOH N 7 .   ? -5.688  1.687   -5.021  1.00 17.43 ? 404 HOH A O   1 
HETATM 4579 O  O   . HOH N 7 .   ? -7.176  -15.385 28.735  1.00 15.25 ? 405 HOH A O   1 
HETATM 4580 O  O   . HOH N 7 .   ? -1.954  -13.992 24.719  1.00 13.48 ? 406 HOH A O   1 
HETATM 4581 O  O   . HOH N 7 .   ? -2.152  -18.312 22.416  1.00 14.94 ? 407 HOH A O   1 
HETATM 4582 O  O   . HOH N 7 .   ? -20.811 -5.355  22.994  1.00 16.33 ? 408 HOH A O   1 
HETATM 4583 O  O   . HOH N 7 .   ? 0.167   -19.737 21.915  1.00 17.17 ? 409 HOH A O   1 
HETATM 4584 O  O   . HOH N 7 .   ? -11.453 -21.668 10.310  1.00 15.01 ? 410 HOH A O   1 
HETATM 4585 O  O   . HOH N 7 .   ? -0.461  -11.805 25.728  1.00 15.07 ? 411 HOH A O   1 
HETATM 4586 O  O   . HOH N 7 .   ? -1.612  -16.615 24.625  1.00 16.29 ? 412 HOH A O   1 
HETATM 4587 O  O   . HOH N 7 .   ? -17.265 -10.359 28.869  1.00 14.90 ? 413 HOH A O   1 
HETATM 4588 O  O   . HOH N 7 .   ? -6.555  -5.684  -0.725  1.00 13.00 ? 414 HOH A O   1 
HETATM 4589 O  O   . HOH N 7 .   ? -0.914  -0.630  -6.214  1.00 15.73 ? 415 HOH A O   1 
HETATM 4590 O  O   . HOH N 7 .   ? -17.819 -23.674 18.356  1.00 14.32 ? 416 HOH A O   1 
HETATM 4591 O  O   . HOH N 7 .   ? -4.912  -11.280 26.087  1.00 15.55 ? 417 HOH A O   1 
HETATM 4592 O  O   . HOH N 7 .   ? -4.112  6.022   8.163   1.00 21.49 ? 418 HOH A O   1 
HETATM 4593 O  O   . HOH N 7 .   ? -13.367 -23.258 17.407  1.00 17.47 ? 419 HOH A O   1 
HETATM 4594 O  O   . HOH N 7 .   ? -13.130 -18.459 28.275  1.00 17.29 ? 420 HOH A O   1 
HETATM 4595 O  O   . HOH N 7 .   ? -26.453 -12.748 21.015  1.00 19.79 ? 421 HOH A O   1 
HETATM 4596 O  O   . HOH N 7 .   ? -20.295 -20.685 11.061  1.00 20.44 ? 422 HOH A O   1 
HETATM 4597 O  O   . HOH N 7 .   ? 4.500   -24.523 6.955   1.00 20.21 ? 423 HOH A O   1 
HETATM 4598 O  O   . HOH N 7 .   ? -10.293 -16.505 8.381   1.00 12.25 ? 424 HOH A O   1 
HETATM 4599 O  O   . HOH N 7 .   ? 5.844   -1.800  11.969  1.00 21.23 ? 425 HOH A O   1 
HETATM 4600 O  O   . HOH N 7 .   ? -22.459 -19.491 18.652  1.00 17.03 ? 426 HOH A O   1 
HETATM 4601 O  O   . HOH N 7 .   ? -4.240  -20.497 26.532  1.00 21.12 ? 427 HOH A O   1 
HETATM 4602 O  O   . HOH N 7 .   ? -19.550 -14.183 5.601   1.00 18.51 ? 428 HOH A O   1 
HETATM 4603 O  O   . HOH N 7 .   ? -5.725  -19.843 6.043   1.00 18.74 ? 429 HOH A O   1 
HETATM 4604 O  O   . HOH N 7 .   ? -5.439  -15.651 26.636  1.00 16.50 ? 430 HOH A O   1 
HETATM 4605 O  O   . HOH N 7 .   ? -11.509 -25.425 16.780  1.00 21.97 ? 431 HOH A O   1 
HETATM 4606 O  O   . HOH N 7 .   ? 1.253   -10.306 24.244  1.00 17.87 ? 432 HOH A O   1 
HETATM 4607 O  O   . HOH N 7 .   ? -0.363  -0.736  4.278   1.00 19.87 ? 433 HOH A O   1 
HETATM 4608 O  O   . HOH N 7 .   ? -3.434  -25.789 8.307   1.00 22.17 ? 434 HOH A O   1 
HETATM 4609 O  O   . HOH N 7 .   ? -19.771 -16.965 24.454  1.00 22.72 ? 435 HOH A O   1 
HETATM 4610 O  O   . HOH N 7 .   ? -24.552 -11.543 15.431  1.00 18.67 ? 436 HOH A O   1 
HETATM 4611 O  O   . HOH N 7 .   ? -14.868 -0.031  28.349  1.00 23.39 ? 437 HOH A O   1 
HETATM 4612 O  O   . HOH N 7 .   ? -21.548 -0.726  34.879  1.00 18.42 ? 438 HOH A O   1 
HETATM 4613 O  O   . HOH N 7 .   ? -2.079  -25.726 11.013  1.00 23.20 ? 439 HOH A O   1 
HETATM 4614 O  O   . HOH N 7 .   ? -9.209  -13.958 32.786  1.00 23.48 ? 440 HOH A O   1 
HETATM 4615 O  O   . HOH N 7 .   ? -9.496  -0.252  -6.112  1.00 17.36 ? 441 HOH A O   1 
HETATM 4616 O  O   . HOH N 7 .   ? 4.202   -19.508 12.454  1.00 26.52 ? 442 HOH A O   1 
HETATM 4617 O  O   . HOH N 7 .   ? -15.879 -23.704 24.017  1.00 20.39 ? 443 HOH A O   1 
HETATM 4618 O  O   . HOH N 7 .   ? 1.382   -8.265  6.822   1.00 20.29 ? 444 HOH A O   1 
HETATM 4619 O  O   . HOH N 7 .   ? -2.755  4.027   2.392   1.00 21.15 ? 445 HOH A O   1 
HETATM 4620 O  O   . HOH N 7 .   ? -25.131 -14.691 19.298  1.00 16.73 ? 446 HOH A O   1 
HETATM 4621 O  O   . HOH N 7 .   ? 1.866   -19.310 23.979  1.00 18.84 ? 447 HOH A O   1 
HETATM 4622 O  O   . HOH N 7 .   ? -21.440 3.984   0.148   1.00 25.58 ? 448 HOH A O   1 
HETATM 4623 O  O   . HOH N 7 .   ? 0.278   -5.600  28.377  1.00 25.41 ? 449 HOH A O   1 
HETATM 4624 O  O   . HOH N 7 .   ? -21.167 -18.096 10.862  1.00 19.07 ? 450 HOH A O   1 
HETATM 4625 O  O   . HOH N 7 .   ? -10.574 -21.664 26.924  1.00 22.28 ? 451 HOH A O   1 
HETATM 4626 O  O   . HOH N 7 .   ? -21.908 -6.667  25.064  1.00 19.75 ? 452 HOH A O   1 
HETATM 4627 O  O   . HOH N 7 .   ? 7.708   -9.330  17.866  1.00 20.99 ? 453 HOH A O   1 
HETATM 4628 O  O   . HOH N 7 .   ? -1.718  -4.799  -2.211  1.00 20.61 ? 454 HOH A O   1 
HETATM 4629 O  O   . HOH N 7 .   ? 10.017  -14.723 12.733  1.00 28.19 ? 455 HOH A O   1 
HETATM 4630 O  O   . HOH N 7 .   ? 0.584   -17.713 25.780  1.00 20.78 ? 456 HOH A O   1 
HETATM 4631 O  O   . HOH N 7 .   ? 5.028   -4.673  26.605  1.00 28.10 ? 457 HOH A O   1 
HETATM 4632 O  O   . HOH N 7 .   ? 7.296   -24.334 7.475   1.00 23.48 ? 458 HOH A O   1 
HETATM 4633 O  O   . HOH N 7 .   ? -16.425 -18.955 4.167   1.00 27.82 ? 459 HOH A O   1 
HETATM 4634 O  O   . HOH N 7 .   ? 6.443   -13.336 11.336  1.00 22.01 ? 460 HOH A O   1 
HETATM 4635 O  O   . HOH N 7 .   ? 7.703   -22.220 5.657   1.00 19.95 ? 461 HOH A O   1 
HETATM 4636 O  O   . HOH N 7 .   ? 4.198   -15.665 -0.886  1.00 21.79 ? 462 HOH A O   1 
HETATM 4637 O  O   . HOH N 7 .   ? -15.030 -25.314 13.907  1.00 23.57 ? 463 HOH A O   1 
HETATM 4638 O  O   . HOH N 7 .   ? 2.163   -7.973  4.282   1.00 21.35 ? 464 HOH A O   1 
HETATM 4639 O  O   . HOH N 7 .   ? -17.404 -17.040 -3.296  1.00 25.32 ? 465 HOH A O   1 
HETATM 4640 O  O   . HOH N 7 .   ? -3.606  -17.739 26.288  1.00 20.22 ? 466 HOH A O   1 
HETATM 4641 O  O   . HOH N 7 .   ? -24.448 -4.514  23.548  1.00 23.43 ? 467 HOH A O   1 
HETATM 4642 O  O   . HOH N 7 .   ? -0.488  -8.500  3.000   1.00 22.25 ? 468 HOH A O   1 
HETATM 4643 O  O   . HOH N 7 .   ? -10.577 -27.049 18.916  1.00 22.95 ? 469 HOH A O   1 
HETATM 4644 O  O   . HOH N 7 .   ? -5.999  -18.576 29.130  1.00 23.22 ? 470 HOH A O   1 
HETATM 4645 O  O   . HOH N 7 .   ? -26.578 -14.278 17.046  1.00 21.29 ? 471 HOH A O   1 
HETATM 4646 O  O   . HOH N 7 .   ? -17.878 -23.493 13.164  1.00 24.50 ? 472 HOH A O   1 
HETATM 4647 O  O   . HOH N 7 .   ? -7.361  -13.859 -1.006  1.00 25.44 ? 473 HOH A O   1 
HETATM 4648 O  O   . HOH N 7 .   ? -26.769 -7.116  -0.757  1.00 24.94 ? 474 HOH A O   1 
HETATM 4649 O  O   . HOH N 7 .   ? 6.092   1.795   6.118   1.00 34.21 ? 475 HOH A O   1 
HETATM 4650 O  O   . HOH N 7 .   ? 2.849   -3.128  25.746  1.00 22.59 ? 476 HOH A O   1 
HETATM 4651 O  O   . HOH N 7 .   ? 10.301  -7.280  16.968  1.00 33.10 ? 477 HOH A O   1 
HETATM 4652 O  O   . HOH N 7 .   ? 8.341   -6.807  24.344  1.00 28.15 ? 478 HOH A O   1 
HETATM 4653 O  O   . HOH N 7 .   ? -5.516  9.553   9.704   1.00 26.57 ? 479 HOH A O   1 
HETATM 4654 O  O   . HOH N 7 .   ? 2.404   -2.911  4.782   1.00 27.95 ? 480 HOH A O   1 
HETATM 4655 O  O   . HOH N 7 .   ? -5.370  -15.652 30.752  1.00 23.32 ? 481 HOH A O   1 
HETATM 4656 O  O   . HOH N 7 .   ? -4.558  -23.908 26.193  1.00 28.70 ? 482 HOH A O   1 
HETATM 4657 O  O   . HOH N 7 .   ? 2.865   -8.907  26.943  1.00 25.30 ? 483 HOH A O   1 
HETATM 4658 O  O   . HOH N 7 .   ? -16.871 -2.686  34.038  1.00 23.48 ? 484 HOH A O   1 
HETATM 4659 O  O   . HOH N 7 .   ? 3.417   -5.604  3.971   1.00 27.90 ? 485 HOH A O   1 
HETATM 4660 O  O   . HOH N 7 .   ? -23.362 -18.029 8.085   1.00 25.42 ? 486 HOH A O   1 
HETATM 4661 O  O   . HOH N 7 .   ? -9.680  2.319   12.799  1.00 30.44 ? 487 HOH A O   1 
HETATM 4662 O  O   . HOH N 7 .   ? -17.518 4.083   15.244  1.00 34.73 ? 488 HOH A O   1 
HETATM 4663 O  O   . HOH N 7 .   ? -9.310  -10.403 -7.504  1.00 30.25 ? 489 HOH A O   1 
HETATM 4664 O  O   . HOH N 7 .   ? -2.653  -27.976 12.578  1.00 22.31 ? 490 HOH A O   1 
HETATM 4665 O  O   . HOH N 7 .   ? -11.016 -0.170  -8.564  1.00 26.20 ? 491 HOH A O   1 
HETATM 4666 O  O   . HOH N 7 .   ? 5.372   -8.622  25.815  1.00 29.86 ? 492 HOH A O   1 
HETATM 4667 O  O   . HOH N 7 .   ? -1.778  -31.489 22.297  1.00 33.37 ? 493 HOH A O   1 
HETATM 4668 O  O   . HOH N 7 .   ? -19.899 -13.713 30.161  1.00 26.30 ? 494 HOH A O   1 
HETATM 4669 O  O   . HOH N 7 .   ? 8.553   0.339   12.997  1.00 28.41 ? 495 HOH A O   1 
HETATM 4670 O  O   . HOH N 7 .   ? 5.570   -22.221 4.234   1.00 22.81 ? 496 HOH A O   1 
HETATM 4671 O  O   . HOH N 7 .   ? -24.497 -8.063  31.151  1.00 36.14 ? 497 HOH A O   1 
HETATM 4672 O  O   . HOH N 7 .   ? -28.529 -10.501 24.183  1.00 34.99 ? 498 HOH A O   1 
HETATM 4673 O  O   . HOH N 7 .   ? -4.685  -1.704  33.450  1.00 27.55 ? 499 HOH A O   1 
HETATM 4674 O  O   . HOH N 7 .   ? -17.497 0.626   21.603  1.00 29.71 ? 500 HOH A O   1 
HETATM 4675 O  O   . HOH N 7 .   ? -10.693 -24.173 8.629   1.00 19.51 ? 501 HOH A O   1 
HETATM 4676 O  O   . HOH N 7 .   ? -22.557 -11.320 32.679  1.00 22.84 ? 502 HOH A O   1 
HETATM 4677 O  O   . HOH N 7 .   ? 5.316   -21.963 17.063  1.00 32.13 ? 503 HOH A O   1 
HETATM 4678 O  O   . HOH N 7 .   ? 2.227   -12.651 0.726   1.00 29.45 ? 504 HOH A O   1 
HETATM 4679 O  O   . HOH N 7 .   ? -28.602 -12.325 9.467   1.00 34.62 ? 505 HOH A O   1 
HETATM 4680 O  O   . HOH N 7 .   ? -18.647 -20.989 26.915  1.00 27.25 ? 506 HOH A O   1 
HETATM 4681 O  O   . HOH N 7 .   ? -6.405  -14.093 32.700  1.00 27.57 ? 507 HOH A O   1 
HETATM 4682 O  O   . HOH N 7 .   ? -8.739  -31.477 14.616  1.00 32.46 ? 508 HOH A O   1 
HETATM 4683 O  O   . HOH N 7 .   ? 4.267   -18.266 23.123  1.00 21.98 ? 509 HOH A O   1 
HETATM 4684 O  O   . HOH N 7 .   ? -23.896 -4.355  26.332  1.00 29.84 ? 510 HOH A O   1 
HETATM 4685 O  O   . HOH N 7 .   ? 8.742   -5.813  15.356  1.00 25.58 ? 511 HOH A O   1 
HETATM 4686 O  O   . HOH N 7 .   ? -15.102 -11.236 37.717  1.00 31.29 ? 512 HOH A O   1 
HETATM 4687 O  O   . HOH N 7 .   ? -16.771 -15.660 33.074  1.00 31.87 ? 513 HOH A O   1 
HETATM 4688 O  O   . HOH N 7 .   ? -28.338 0.643   10.814  1.00 29.91 ? 514 HOH A O   1 
HETATM 4689 O  O   . HOH N 7 .   ? 6.011   2.249   22.568  1.00 26.67 ? 515 HOH A O   1 
HETATM 4690 O  O   . HOH N 7 .   ? 8.717   -19.773 17.731  1.00 30.95 ? 516 HOH A O   1 
HETATM 4691 O  O   . HOH N 7 .   ? -14.441 -21.767 27.975  1.00 34.23 ? 517 HOH A O   1 
HETATM 4692 O  O   . HOH N 7 .   ? -9.639  2.630   36.301  1.00 35.90 ? 518 HOH A O   1 
HETATM 4693 O  O   . HOH N 7 .   ? 7.848   9.104   20.578  1.00 45.26 ? 519 HOH A O   1 
HETATM 4694 O  O   . HOH N 7 .   ? -27.651 -1.171  23.659  1.00 31.24 ? 520 HOH A O   1 
HETATM 4695 O  O   . HOH N 7 .   ? 13.434  4.580   11.688  1.00 47.33 ? 521 HOH A O   1 
HETATM 4696 O  O   . HOH N 7 .   ? -7.942  -25.951 28.568  1.00 39.12 ? 522 HOH A O   1 
HETATM 4697 O  O   . HOH N 7 .   ? -0.978  -23.491 4.425   1.00 33.30 ? 523 HOH A O   1 
HETATM 4698 O  O   . HOH N 7 .   ? -15.503 -10.088 -7.333  1.00 22.64 ? 524 HOH A O   1 
HETATM 4699 O  O   . HOH N 7 .   ? -23.387 6.267   2.565   1.00 27.20 ? 525 HOH A O   1 
HETATM 4700 O  O   . HOH N 7 .   ? 3.432   1.675   23.134  1.00 30.10 ? 526 HOH A O   1 
HETATM 4701 O  O   . HOH N 7 .   ? -12.812 -19.495 31.823  1.00 32.23 ? 527 HOH A O   1 
HETATM 4702 O  O   . HOH N 7 .   ? 1.305   -26.447 23.014  1.00 37.20 ? 528 HOH A O   1 
HETATM 4703 O  O   . HOH N 7 .   ? -6.178  14.662  10.500  1.00 44.47 ? 529 HOH A O   1 
HETATM 4704 O  O   . HOH N 7 .   ? -15.560 -25.404 6.464   1.00 33.15 ? 530 HOH A O   1 
HETATM 4705 O  O   . HOH N 7 .   ? -9.647  -8.823  39.171  1.00 34.57 ? 531 HOH A O   1 
HETATM 4706 O  O   . HOH N 7 .   ? -23.199 -12.727 4.553   1.00 38.76 ? 532 HOH A O   1 
HETATM 4707 O  O   . HOH N 7 .   ? -7.896  -28.350 20.672  1.00 28.17 ? 533 HOH A O   1 
HETATM 4708 O  O   . HOH N 7 .   ? -12.663 -23.635 32.959  1.00 38.63 ? 534 HOH A O   1 
HETATM 4709 O  O   . HOH N 7 .   ? 4.544   -0.578  5.120   1.00 37.60 ? 535 HOH A O   1 
HETATM 4710 O  O   . HOH N 7 .   ? 7.580   -3.324  10.146  1.00 25.59 ? 536 HOH A O   1 
HETATM 4711 O  O   . HOH N 7 .   ? -13.669 -4.432  -9.345  1.00 35.06 ? 537 HOH A O   1 
HETATM 4712 O  O   . HOH N 7 .   ? -14.110 -27.396 10.377  1.00 28.76 ? 538 HOH A O   1 
HETATM 4713 O  O   . HOH N 7 .   ? -8.801  -13.490 -3.213  1.00 22.91 ? 539 HOH A O   1 
HETATM 4714 O  O   . HOH N 7 .   ? 6.311   -15.969 12.348  1.00 28.85 ? 540 HOH A O   1 
HETATM 4715 O  O   . HOH N 7 .   ? -17.155 -24.614 4.201   1.00 31.29 ? 541 HOH A O   1 
HETATM 4716 O  O   . HOH N 7 .   ? -27.463 -1.439  3.266   1.00 45.37 ? 542 HOH A O   1 
HETATM 4717 O  O   . HOH N 7 .   ? -19.987 12.710  11.615  1.00 27.90 ? 543 HOH A O   1 
HETATM 4718 O  O   . HOH N 7 .   ? -16.429 -0.488  -5.974  1.00 22.64 ? 544 HOH A O   1 
HETATM 4719 O  O   . HOH N 7 .   ? -10.417 -26.578 9.759   1.00 30.80 ? 545 HOH A O   1 
HETATM 4720 O  O   . HOH N 7 .   ? -11.832 -27.973 27.867  1.00 33.14 ? 546 HOH A O   1 
HETATM 4721 O  O   . HOH N 7 .   ? 1.685   -13.063 27.043  1.00 30.96 ? 547 HOH A O   1 
HETATM 4722 O  O   . HOH N 7 .   ? -18.211 -11.537 -7.116  1.00 36.06 ? 548 HOH A O   1 
HETATM 4723 O  O   . HOH N 7 .   ? -1.415  -21.000 2.504   1.00 35.23 ? 549 HOH A O   1 
HETATM 4724 O  O   . HOH N 7 .   ? -29.346 -13.653 24.730  1.00 35.01 ? 550 HOH A O   1 
HETATM 4725 O  O   . HOH N 7 .   ? -3.106  6.248   3.396   1.00 37.16 ? 551 HOH A O   1 
HETATM 4726 O  O   . HOH N 7 .   ? -18.607 -2.050  31.732  1.00 36.09 ? 552 HOH A O   1 
HETATM 4727 O  O   . HOH N 7 .   ? -4.526  4.212   26.744  1.00 40.42 ? 553 HOH A O   1 
HETATM 4728 O  O   . HOH N 7 .   ? 4.043   -9.660  3.249   1.00 35.36 ? 554 HOH A O   1 
HETATM 4729 O  O   . HOH N 7 .   ? -30.448 -7.369  23.152  1.00 43.05 ? 555 HOH A O   1 
HETATM 4730 O  O   . HOH N 7 .   ? -24.017 -6.294  16.347  1.00 25.81 ? 556 HOH A O   1 
HETATM 4731 O  O   . HOH N 7 .   ? 1.761   -28.334 12.219  1.00 34.90 ? 557 HOH A O   1 
HETATM 4732 O  O   . HOH N 7 .   ? -9.381  15.555  3.185   1.00 31.06 ? 558 HOH A O   1 
HETATM 4733 O  O   . HOH N 7 .   ? -21.873 10.927  8.498   1.00 36.74 ? 559 HOH A O   1 
HETATM 4734 O  O   . HOH N 7 .   ? -3.486  -24.157 5.901   1.00 35.65 ? 560 HOH A O   1 
HETATM 4735 O  O   . HOH N 7 .   ? -12.987 -11.439 40.406  1.00 27.60 ? 561 HOH A O   1 
HETATM 4736 O  O   . HOH N 7 .   ? 1.746   -7.762  -6.886  1.00 38.38 ? 562 HOH A O   1 
HETATM 4737 O  O   . HOH N 7 .   ? 3.993   -0.483  25.415  1.00 28.71 ? 563 HOH A O   1 
HETATM 4738 O  O   . HOH N 7 .   ? 1.161   -0.807  29.112  1.00 34.94 ? 564 HOH A O   1 
HETATM 4739 O  O   . HOH N 7 .   ? -10.731 2.903   32.687  1.00 32.93 ? 565 HOH A O   1 
HETATM 4740 O  O   . HOH N 7 .   ? 8.553   -4.477  7.562   1.00 35.57 ? 566 HOH A O   1 
HETATM 4741 O  O   . HOH N 7 .   ? -19.213 -16.523 31.162  1.00 31.97 ? 567 HOH A O   1 
HETATM 4742 O  O   . HOH N 7 .   ? -1.882  9.416   6.666   1.00 37.23 ? 568 HOH A O   1 
HETATM 4743 O  O   . HOH N 7 .   ? 8.922   -13.282 22.212  1.00 32.00 ? 569 HOH A O   1 
HETATM 4744 O  O   . HOH N 7 .   ? -31.080 -8.628  19.984  1.00 34.44 ? 570 HOH A O   1 
HETATM 4745 O  O   . HOH N 7 .   ? -2.456  6.675   6.140   1.00 29.86 ? 571 HOH A O   1 
HETATM 4746 O  O   . HOH N 7 .   ? -12.754 -27.577 7.884   1.00 37.17 ? 572 HOH A O   1 
HETATM 4747 O  O   . HOH N 7 .   ? -17.992 -20.437 29.495  1.00 32.47 ? 573 HOH A O   1 
HETATM 4748 O  O   . HOH N 7 .   ? -23.234 -13.931 28.162  1.00 43.28 ? 574 HOH A O   1 
HETATM 4749 O  O   . HOH N 7 .   ? -3.552  11.817  -2.851  1.00 38.94 ? 575 HOH A O   1 
HETATM 4750 O  O   . HOH N 7 .   ? -13.366 -15.381 34.700  1.00 31.74 ? 576 HOH A O   1 
HETATM 4751 O  O   . HOH N 7 .   ? -26.207 -2.812  26.511  1.00 34.81 ? 577 HOH A O   1 
HETATM 4752 O  O   . HOH N 7 .   ? 2.939   0.735   27.557  1.00 34.63 ? 578 HOH A O   1 
HETATM 4753 O  O   . HOH N 7 .   ? -28.775 -4.939  33.638  1.00 45.79 ? 579 HOH A O   1 
HETATM 4754 O  O   . HOH N 7 .   ? 13.422  -11.198 25.435  1.00 38.42 ? 580 HOH A O   1 
HETATM 4755 O  O   . HOH N 7 .   ? -14.541 -20.094 29.581  1.00 37.13 ? 581 HOH A O   1 
HETATM 4756 O  O   . HOH N 7 .   ? 0.709   -3.168  27.565  1.00 26.62 ? 582 HOH A O   1 
HETATM 4757 O  O   . HOH N 7 .   ? -15.118 1.628   20.428  1.00 40.72 ? 583 HOH A O   1 
HETATM 4758 O  O   . HOH N 7 .   ? -4.959  -22.260 5.132   1.00 28.02 ? 584 HOH A O   1 
HETATM 4759 O  O   . HOH N 7 .   ? -10.497 -14.487 35.074  1.00 27.95 ? 585 HOH A O   1 
HETATM 4760 O  O   . HOH N 7 .   ? -27.421 0.737   28.644  1.00 28.59 ? 586 HOH A O   1 
HETATM 4761 O  O   . HOH N 7 .   ? 2.258   -15.622 26.893  1.00 24.99 ? 587 HOH A O   1 
HETATM 4762 O  O   . HOH N 7 .   ? 7.169   -20.291 12.777  1.00 37.58 ? 588 HOH A O   1 
HETATM 4763 O  O   . HOH N 7 .   ? -17.977 -26.558 11.186  1.00 37.27 ? 589 HOH A O   1 
HETATM 4764 O  O   . HOH N 7 .   ? -12.139 0.743   20.802  1.00 29.82 ? 590 HOH A O   1 
HETATM 4765 O  O   . HOH N 7 .   ? 5.302   -21.093 14.260  1.00 40.39 ? 591 HOH A O   1 
HETATM 4766 O  O   . HOH N 7 .   ? -0.290  3.657   1.252   1.00 32.51 ? 592 HOH A O   1 
HETATM 4767 O  O   . HOH N 7 .   ? 9.652   -10.265 10.370  1.00 35.04 ? 593 HOH A O   1 
HETATM 4768 O  O   . HOH N 7 .   ? -16.729 0.277   30.149  1.00 34.61 ? 594 HOH A O   1 
HETATM 4769 O  O   . HOH N 7 .   ? -26.335 -0.075  5.510   1.00 34.83 ? 595 HOH A O   1 
HETATM 4770 O  O   . HOH N 7 .   ? -20.813 -19.244 7.502   1.00 25.84 ? 596 HOH A O   1 
HETATM 4771 O  O   . HOH N 7 .   ? -5.128  -7.900  37.437  1.00 38.32 ? 597 HOH A O   1 
HETATM 4772 O  O   . HOH N 7 .   ? -26.469 -9.489  29.677  1.00 39.79 ? 598 HOH A O   1 
HETATM 4773 O  O   . HOH N 7 .   ? -18.475 -17.316 4.326   1.00 32.14 ? 599 HOH A O   1 
HETATM 4774 O  O   . HOH N 7 .   ? -11.115 -28.929 22.985  1.00 40.11 ? 600 HOH A O   1 
HETATM 4775 O  O   . HOH N 7 .   ? 12.129  -14.228 15.344  1.00 31.44 ? 601 HOH A O   1 
HETATM 4776 O  O   . HOH N 7 .   ? -19.886 1.447   24.815  1.00 30.66 ? 602 HOH A O   1 
HETATM 4777 O  O   . HOH N 7 .   ? -23.936 8.987   15.243  1.00 35.72 ? 603 HOH A O   1 
HETATM 4778 O  O   . HOH N 7 .   ? 2.200   -21.711 25.263  1.00 34.36 ? 604 HOH A O   1 
HETATM 4779 O  O   . HOH N 7 .   ? -5.025  -31.773 26.818  1.00 38.64 ? 605 HOH A O   1 
HETATM 4780 O  O   . HOH N 7 .   ? -12.741 -18.104 34.439  1.00 38.87 ? 606 HOH A O   1 
HETATM 4781 O  O   . HOH N 7 .   ? -24.698 -13.983 3.236   1.00 34.54 ? 607 HOH A O   1 
HETATM 4782 O  O   . HOH N 7 .   ? -10.213 -15.697 -4.208  1.00 32.63 ? 608 HOH A O   1 
HETATM 4783 O  O   . HOH N 7 .   ? -8.286  -27.637 8.468   1.00 35.10 ? 609 HOH A O   1 
HETATM 4784 O  O   . HOH N 7 .   ? -13.527 -20.207 2.346   1.00 27.99 ? 610 HOH A O   1 
HETATM 4785 O  O   . HOH N 7 .   ? 4.474   -26.040 4.679   1.00 38.08 ? 611 HOH A O   1 
HETATM 4786 O  O   . HOH N 7 .   ? -10.699 -11.205 38.665  1.00 37.98 ? 612 HOH A O   1 
HETATM 4787 O  O   . HOH N 7 .   ? -0.192  3.299   26.496  1.00 42.76 ? 613 HOH A O   1 
HETATM 4788 O  O   . HOH N 7 .   ? -22.059 -0.644  -1.253  1.00 30.85 ? 614 HOH A O   1 
HETATM 4789 O  O   . HOH N 7 .   ? -21.998 -14.815 0.161   1.00 33.19 ? 615 HOH A O   1 
HETATM 4790 O  O   . HOH N 7 .   ? -13.698 7.992   -4.380  1.00 35.29 ? 616 HOH A O   1 
HETATM 4791 O  O   . HOH N 7 .   ? -26.967 -2.421  28.972  1.00 35.70 ? 617 HOH A O   1 
HETATM 4792 O  O   . HOH N 7 .   ? -0.258  2.169   -1.351  1.00 45.88 ? 618 HOH A O   1 
HETATM 4793 O  O   . HOH N 7 .   ? 3.059   15.866  12.284  1.00 52.14 ? 619 HOH A O   1 
HETATM 4794 O  O   . HOH N 7 .   ? -7.959  -22.532 4.178   1.00 40.15 ? 620 HOH A O   1 
HETATM 4795 O  O   . HOH N 7 .   ? 1.488   -30.449 16.548  1.00 37.02 ? 621 HOH A O   1 
HETATM 4796 O  O   . HOH N 7 .   ? 8.539   11.071  3.035   1.00 52.30 ? 622 HOH A O   1 
HETATM 4797 O  O   . HOH N 7 .   ? -8.930  -23.147 28.650  1.00 35.64 ? 623 HOH A O   1 
HETATM 4798 O  O   . HOH N 7 .   ? -7.359  -16.686 -1.096  1.00 36.98 ? 624 HOH A O   1 
HETATM 4799 O  O   . HOH N 7 .   ? -24.276 4.331   -0.792  1.00 45.57 ? 625 HOH A O   1 
HETATM 4800 O  O   . HOH N 7 .   ? -10.228 -22.931 4.131   1.00 32.32 ? 626 HOH A O   1 
HETATM 4801 O  O   . HOH N 7 .   ? -10.891 -24.566 6.009   1.00 33.14 ? 627 HOH A O   1 
HETATM 4802 O  O   . HOH N 7 .   ? 6.137   -6.082  3.740   1.00 37.23 ? 628 HOH A O   1 
HETATM 4803 O  O   . HOH N 7 .   ? -26.816 -3.134  22.928  1.00 32.07 ? 629 HOH A O   1 
HETATM 4804 O  O   . HOH N 7 .   ? -29.646 -0.941  18.476  1.00 37.98 ? 630 HOH A O   1 
HETATM 4805 O  O   . HOH N 7 .   ? -29.916 -9.317  12.563  1.00 42.37 ? 631 HOH A O   1 
HETATM 4806 O  O   . HOH N 7 .   ? -28.528 -9.285  9.350   1.00 43.09 ? 632 HOH A O   1 
HETATM 4807 O  O   . HOH N 7 .   ? -4.370  -10.986 -8.293  1.00 43.72 ? 633 HOH A O   1 
HETATM 4808 O  O   . HOH N 7 .   ? -2.630  -14.336 29.040  1.00 46.42 ? 634 HOH A O   1 
HETATM 4809 O  O   . HOH N 7 .   ? -24.832 -6.691  7.851   1.00 36.94 ? 635 HOH A O   1 
HETATM 4810 O  O   . HOH N 7 .   ? -21.920 -15.339 5.731   1.00 35.86 ? 636 HOH A O   1 
HETATM 4811 O  O   . HOH N 7 .   ? 8.036   -22.663 18.547  1.00 49.03 ? 637 HOH A O   1 
HETATM 4812 O  O   . HOH N 7 .   ? 8.759   -15.612 8.463   1.00 33.72 ? 638 HOH A O   1 
HETATM 4813 O  O   . HOH N 7 .   ? 0.464   -18.283 -4.463  1.00 39.33 ? 639 HOH A O   1 
HETATM 4814 O  O   . HOH N 7 .   ? -3.108  8.665   9.423   1.00 45.61 ? 640 HOH A O   1 
HETATM 4815 O  O   . HOH N 7 .   ? -11.810 2.924   18.936  1.00 49.77 ? 641 HOH A O   1 
HETATM 4816 O  O   . HOH N 7 .   ? -13.492 0.886   -7.851  1.00 36.94 ? 642 HOH A O   1 
HETATM 4817 O  O   . HOH N 7 .   ? -7.237  0.903   12.868  1.00 33.71 ? 643 HOH A O   1 
HETATM 4818 O  O   . HOH N 7 .   ? -5.824  0.419   10.651  1.00 18.33 ? 644 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   2   ?   ?   ?   B . n 
A 1 3   SER 3   3   ?   ?   ?   B . n 
A 1 4   ARG 4   4   ?   ?   ?   B . n 
A 1 5   LEU 5   5   ?   ?   ?   B . n 
A 1 6   SER 6   6   6   SER SER B . n 
A 1 7   TRP 7   7   7   TRP TRP B . n 
A 1 8   GLY 8   8   8   GLY GLY B . n 
A 1 9   TYR 9   9   9   TYR TYR B . n 
A 1 10  ARG 10  10  10  ARG ARG B . n 
A 1 11  GLU 11  11  11  GLU GLU B . n 
A 1 12  HIS 12  12  12  HIS HIS B . n 
A 1 13  ASN 13  13  13  ASN ASN B . n 
A 1 14  GLY 14  14  14  GLY GLY B . n 
A 1 15  PRO 15  15  15  PRO PRO B . n 
A 1 16  ILE 16  16  16  ILE ILE B . n 
A 1 17  HIS 17  17  17  HIS HIS B . n 
A 1 18  TRP 18  18  18  TRP TRP B . n 
A 1 19  LYS 19  19  19  LYS LYS B . n 
A 1 20  GLU 20  20  20  GLU GLU B . n 
A 1 21  PHE 21  21  21  PHE PHE B . n 
A 1 22  PHE 22  22  22  PHE PHE B . n 
A 1 23  PRO 23  23  23  PRO PRO B . n 
A 1 24  ILE 24  24  24  ILE ILE B . n 
A 1 25  ALA 25  25  25  ALA ALA B . n 
A 1 26  ASP 26  26  26  ASP ASP B . n 
A 1 27  GLY 27  27  27  GLY GLY B . n 
A 1 28  ASP 28  28  28  ASP ASP B . n 
A 1 29  GLN 29  29  29  GLN GLN B . n 
A 1 30  GLN 30  30  30  GLN GLN B . n 
A 1 31  SER 31  31  31  SER SER B . n 
A 1 32  PRO 32  32  32  PRO PRO B . n 
A 1 33  ILE 33  33  33  ILE ILE B . n 
A 1 34  GLU 34  34  34  GLU GLU B . n 
A 1 35  ILE 35  35  35  ILE ILE B . n 
A 1 36  LYS 36  36  36  LYS LYS B . n 
A 1 37  THR 37  37  37  THR THR B . n 
A 1 38  LYS 38  38  38  LYS LYS B . n 
A 1 39  GLU 39  39  39  GLU GLU B . n 
A 1 40  VAL 40  40  40  VAL VAL B . n 
A 1 41  LYS 41  41  41  LYS LYS B . n 
A 1 42  TYR 42  42  42  TYR TYR B . n 
A 1 43  ASP 43  43  43  ASP ASP B . n 
A 1 44  SER 44  44  44  SER SER B . n 
A 1 45  SER 45  45  45  SER SER B . n 
A 1 46  LEU 46  46  46  LEU LEU B . n 
A 1 47  ARG 47  47  47  ARG ARG B . n 
A 1 48  PRO 48  48  48  PRO PRO B . n 
A 1 49  LEU 49  49  49  LEU LEU B . n 
A 1 50  SER 50  50  50  SER SER B . n 
A 1 51  ILE 51  51  51  ILE ILE B . n 
A 1 52  LYS 52  52  52  LYS LYS B . n 
A 1 53  TYR 53  53  53  TYR TYR B . n 
A 1 54  ASP 54  54  54  ASP ASP B . n 
A 1 55  PRO 55  55  55  PRO PRO B . n 
A 1 56  SER 56  56  56  SER SER B . n 
A 1 57  SER 57  57  57  SER SER B . n 
A 1 58  ALA 58  58  58  ALA ALA B . n 
A 1 59  LYS 59  59  59  LYS LYS B . n 
A 1 60  ILE 60  60  60  ILE ILE B . n 
A 1 61  ILE 61  61  61  ILE ILE B . n 
A 1 62  SER 62  62  62  SER SER B . n 
A 1 63  ASN 63  63  63  ASN ASN B . n 
A 1 64  SER 64  64  64  SER SER B . n 
A 1 65  GLY 65  65  65  GLY GLY B . n 
A 1 66  HIS 66  66  66  HIS HIS B . n 
A 1 67  SER 67  67  67  SER SER B . n 
A 1 68  PHE 68  68  68  PHE PHE B . n 
A 1 69  ASN 69  69  69  ASN ASN B . n 
A 1 70  VAL 70  70  70  VAL VAL B . n 
A 1 71  ASP 71  71  71  ASP ASP B . n 
A 1 72  PHE 72  72  72  PHE PHE B . n 
A 1 73  ASP 73  73  73  ASP ASP B . n 
A 1 74  ASP 74  74  74  ASP ASP B . n 
A 1 75  THR 75  75  75  THR THR B . n 
A 1 76  GLU 76  76  76  GLU GLU B . n 
A 1 77  ASN 77  77  77  ASN ASN B . n 
A 1 78  LYS 78  78  78  LYS LYS B . n 
A 1 79  SER 79  79  79  SER SER B . n 
A 1 80  VAL 80  80  80  VAL VAL B . n 
A 1 81  LEU 81  81  81  LEU LEU B . n 
A 1 82  ARG 82  82  82  ARG ARG B . n 
A 1 83  GLY 83  83  83  GLY GLY B . n 
A 1 84  GLY 84  84  84  GLY GLY B . n 
A 1 85  PRO 85  85  85  PRO PRO B . n 
A 1 86  LEU 86  86  86  LEU LEU B . n 
A 1 87  THR 87  87  87  THR THR B . n 
A 1 88  GLY 88  88  88  GLY GLY B . n 
A 1 89  SER 89  89  89  SER SER B . n 
A 1 90  TYR 90  90  90  TYR TYR B . n 
A 1 91  ARG 91  91  91  ARG ARG B . n 
A 1 92  LEU 92  92  92  LEU LEU B . n 
A 1 93  ARG 93  93  93  ARG ARG B . n 
A 1 94  GLN 94  94  94  GLN GLN B . n 
A 1 95  VAL 95  95  95  VAL VAL B . n 
A 1 96  HIS 96  96  96  HIS HIS B . n 
A 1 97  LEU 97  97  97  LEU LEU B . n 
A 1 98  HIS 98  98  98  HIS HIS B . n 
A 1 99  TRP 99  99  99  TRP TRP B . n 
A 1 100 GLY 100 100 100 GLY GLY B . n 
A 1 101 SER 101 101 101 SER SER B . n 
A 1 102 ALA 102 102 102 ALA ALA B . n 
A 1 103 ASP 103 103 103 ASP ASP B . n 
A 1 104 ASP 104 104 104 ASP ASP B . n 
A 1 105 HIS 105 105 105 HIS HIS B . n 
A 1 106 GLY 106 106 106 GLY GLY B . n 
A 1 107 SER 107 107 107 SER SER B . n 
A 1 108 GLU 108 108 108 GLU GLU B . n 
A 1 109 HIS 109 109 109 HIS HIS B . n 
A 1 110 ILE 110 110 110 ILE ILE B . n 
A 1 111 VAL 111 111 111 VAL VAL B . n 
A 1 112 ASP 112 112 112 ASP ASP B . n 
A 1 113 GLY 113 113 113 GLY GLY B . n 
A 1 114 VAL 114 114 114 VAL VAL B . n 
A 1 115 SER 115 115 115 SER SER B . n 
A 1 116 TYR 116 116 116 TYR TYR B . n 
A 1 117 ALA 117 117 117 ALA ALA B . n 
A 1 118 ALA 118 118 118 ALA ALA B . n 
A 1 119 GLU 119 119 119 GLU GLU B . n 
A 1 120 LEU 120 120 120 LEU LEU B . n 
A 1 121 HIS 121 121 121 HIS HIS B . n 
A 1 122 VAL 122 122 122 VAL VAL B . n 
A 1 123 VAL 123 123 123 VAL VAL B . n 
A 1 124 HIS 124 124 124 HIS HIS B . n 
A 1 125 TRP 125 125 125 TRP TRP B . n 
A 1 126 ASN 126 126 126 ASN ASN B . n 
A 1 127 SER 127 127 127 SER SER B . n 
A 1 128 ASP 128 128 128 ASP ASP B . n 
A 1 129 LYS 129 129 129 LYS LYS B . n 
A 1 130 TYR 130 130 130 TYR TYR B . n 
A 1 131 PRO 131 131 131 PRO PRO B . n 
A 1 132 SER 132 132 132 SER SER B . n 
A 1 133 PHE 133 133 133 PHE PHE B . n 
A 1 134 VAL 134 134 134 VAL VAL B . n 
A 1 135 GLU 135 135 135 GLU GLU B . n 
A 1 136 ALA 136 136 136 ALA ALA B . n 
A 1 137 ALA 137 137 137 ALA ALA B . n 
A 1 138 HIS 138 138 138 HIS HIS B . n 
A 1 139 GLU 139 139 139 GLU GLU B . n 
A 1 140 PRO 140 140 140 PRO PRO B . n 
A 1 141 ASP 141 141 141 ASP ASP B . n 
A 1 142 GLY 142 142 142 GLY GLY B . n 
A 1 143 LEU 143 143 143 LEU LEU B . n 
A 1 144 ALA 144 144 144 ALA ALA B . n 
A 1 145 VAL 145 145 145 VAL VAL B . n 
A 1 146 LEU 146 146 146 LEU LEU B . n 
A 1 147 GLY 147 147 147 GLY GLY B . n 
A 1 148 VAL 148 148 148 VAL VAL B . n 
A 1 149 PHE 149 149 149 PHE PHE B . n 
A 1 150 LEU 150 150 150 LEU LEU B . n 
A 1 151 GLN 151 151 151 GLN GLN B . n 
A 1 152 ILE 152 152 152 ILE ILE B . n 
A 1 153 GLY 153 153 153 GLY GLY B . n 
A 1 154 GLU 154 154 154 GLU GLU B . n 
A 1 155 PRO 155 155 155 PRO PRO B . n 
A 1 156 ASN 156 156 156 ASN ASN B . n 
A 1 157 SER 157 157 157 SER SER B . n 
A 1 158 GLN 158 158 158 GLN GLN B . n 
A 1 159 LEU 159 159 159 LEU LEU B . n 
A 1 160 GLN 160 160 160 GLN GLN B . n 
A 1 161 LYS 161 161 161 LYS LYS B . n 
A 1 162 ILE 162 162 162 ILE ILE B . n 
A 1 163 THR 163 163 163 THR THR B . n 
A 1 164 ASP 164 164 164 ASP ASP B . n 
A 1 165 THR 165 165 165 THR THR B . n 
A 1 166 LEU 166 166 166 LEU LEU B . n 
A 1 167 ASP 167 167 167 ASP ASP B . n 
A 1 168 SER 168 168 168 SER SER B . n 
A 1 169 ILE 169 169 169 ILE ILE B . n 
A 1 170 LYS 170 170 170 LYS LYS B . n 
A 1 171 GLU 171 171 171 GLU GLU B . n 
A 1 172 LYS 172 172 172 LYS LYS B . n 
A 1 173 GLY 173 173 173 GLY GLY B . n 
A 1 174 LYS 174 174 174 LYS LYS B . n 
A 1 175 GLN 175 175 175 GLN GLN B . n 
A 1 176 THR 176 176 176 THR THR B . n 
A 1 177 ARG 177 177 177 ARG ARG B . n 
A 1 178 PHE 178 178 178 PHE PHE B . n 
A 1 179 THR 179 179 179 THR THR B . n 
A 1 180 ASN 180 180 180 ASN ASN B . n 
A 1 181 PHE 181 181 181 PHE PHE B . n 
A 1 182 ASP 182 182 182 ASP ASP B . n 
A 1 183 LEU 183 183 183 LEU LEU B . n 
A 1 184 LEU 184 184 184 LEU LEU B . n 
A 1 185 SER 185 185 185 SER SER B . n 
A 1 186 LEU 186 186 186 LEU LEU B . n 
A 1 187 LEU 187 187 187 LEU LEU B . n 
A 1 188 PRO 188 188 188 PRO PRO B . n 
A 1 189 PRO 189 189 189 PRO PRO B . n 
A 1 190 SER 190 190 190 SER SER B . n 
A 1 191 TRP 191 191 191 TRP TRP B . n 
A 1 192 ASP 192 192 192 ASP ASP B . n 
A 1 193 TYR 193 193 193 TYR TYR B . n 
A 1 194 TRP 194 194 194 TRP TRP B . n 
A 1 195 THR 195 195 195 THR THR B . n 
A 1 196 TYR 196 196 196 TYR TYR B . n 
A 1 197 PRO 197 197 197 PRO PRO B . n 
A 1 198 GLY 198 198 198 GLY GLY B . n 
A 1 199 SER 199 199 199 SER SER B . n 
A 1 200 LEU 200 200 200 LEU LEU B . n 
A 1 201 THR 201 201 201 THR THR B . n 
A 1 202 VAL 202 202 202 VAL VAL B . n 
A 1 203 PRO 203 203 203 PRO PRO B . n 
A 1 204 PRO 204 204 204 PRO PRO B . n 
A 1 205 LEU 205 205 205 LEU LEU B . n 
A 1 206 LEU 206 206 206 LEU LEU B . n 
A 1 207 GLU 207 207 207 GLU GLU B . n 
A 1 208 SER 208 208 208 SER SER B . n 
A 1 209 VAL 209 209 209 VAL VAL B . n 
A 1 210 THR 210 210 210 THR THR B . n 
A 1 211 TRP 211 211 211 TRP TRP B . n 
A 1 212 ILE 212 212 212 ILE ILE B . n 
A 1 213 VAL 213 213 213 VAL VAL B . n 
A 1 214 LEU 214 214 214 LEU LEU B . n 
A 1 215 LYS 215 215 215 LYS LYS B . n 
A 1 216 GLN 216 216 216 GLN GLN B . n 
A 1 217 PRO 217 217 217 PRO PRO B . n 
A 1 218 ILE 218 218 218 ILE ILE B . n 
A 1 219 ASN 219 219 219 ASN ASN B . n 
A 1 220 ILE 220 220 220 ILE ILE B . n 
A 1 221 SER 221 221 221 SER SER B . n 
A 1 222 SER 222 222 222 SER SER B . n 
A 1 223 GLN 223 223 223 GLN GLN B . n 
A 1 224 GLN 224 224 224 GLN GLN B . n 
A 1 225 LEU 225 225 225 LEU LEU B . n 
A 1 226 ALA 226 226 226 ALA ALA B . n 
A 1 227 LYS 227 227 227 LYS LYS B . n 
A 1 228 PHE 228 228 228 PHE PHE B . n 
A 1 229 ARG 229 229 229 ARG ARG B . n 
A 1 230 SER 230 230 230 SER SER B . n 
A 1 231 LEU 231 231 231 LEU LEU B . n 
A 1 232 LEU 232 232 232 LEU LEU B . n 
A 1 233 CYS 233 233 233 CYS CYS B . n 
A 1 234 THR 234 234 234 THR THR B . n 
A 1 235 ALA 235 235 235 ALA ALA B . n 
A 1 236 GLU 236 236 236 GLU GLU B . n 
A 1 237 GLY 237 237 237 GLY GLY B . n 
A 1 238 GLU 238 238 238 GLU GLU B . n 
A 1 239 ALA 239 239 239 ALA ALA B . n 
A 1 240 ALA 240 240 240 ALA ALA B . n 
A 1 241 ALA 241 241 241 ALA ALA B . n 
A 1 242 PHE 242 242 242 PHE PHE B . n 
A 1 243 LEU 243 243 243 LEU LEU B . n 
A 1 244 VAL 244 244 244 VAL VAL B . n 
A 1 245 SER 245 245 245 SER SER B . n 
A 1 246 ASN 246 246 246 ASN ASN B . n 
A 1 247 HIS 247 247 247 HIS HIS B . n 
A 1 248 ARG 248 248 248 ARG ARG B . n 
A 1 249 PRO 249 249 249 PRO PRO B . n 
A 1 250 PRO 250 250 250 PRO PRO B . n 
A 1 251 GLN 251 251 251 GLN GLN B . n 
A 1 252 PRO 252 252 252 PRO PRO B . n 
A 1 253 LEU 253 253 253 LEU LEU B . n 
A 1 254 LYS 254 254 254 LYS LYS B . n 
A 1 255 GLY 255 255 255 GLY GLY B . n 
A 1 256 ARG 256 256 256 ARG ARG B . n 
A 1 257 LYS 257 257 257 LYS LYS B . n 
A 1 258 VAL 258 258 258 VAL VAL B . n 
A 1 259 ARG 259 259 259 ARG ARG B . n 
A 1 260 ALA 260 260 260 ALA ALA B . n 
A 1 261 SER 261 261 261 SER SER B . n 
A 1 262 PHE 262 262 262 PHE PHE B . n 
A 1 263 HIS 263 263 263 HIS HIS B . n 
B 1 1   MET 1   1   ?   ?   ?   A . n 
B 1 2   MET 2   2   ?   ?   ?   A . n 
B 1 3   SER 3   3   ?   ?   ?   A . n 
B 1 4   ARG 4   4   ?   ?   ?   A . n 
B 1 5   LEU 5   5   ?   ?   ?   A . n 
B 1 6   SER 6   6   6   SER SER A . n 
B 1 7   TRP 7   7   7   TRP TRP A . n 
B 1 8   GLY 8   8   8   GLY GLY A . n 
B 1 9   TYR 9   9   9   TYR TYR A . n 
B 1 10  ARG 10  10  10  ARG ARG A . n 
B 1 11  GLU 11  11  11  GLU GLU A . n 
B 1 12  HIS 12  12  12  HIS HIS A . n 
B 1 13  ASN 13  13  13  ASN ASN A . n 
B 1 14  GLY 14  14  14  GLY GLY A . n 
B 1 15  PRO 15  15  15  PRO PRO A . n 
B 1 16  ILE 16  16  16  ILE ILE A . n 
B 1 17  HIS 17  17  17  HIS HIS A . n 
B 1 18  TRP 18  18  18  TRP TRP A . n 
B 1 19  LYS 19  19  19  LYS LYS A . n 
B 1 20  GLU 20  20  20  GLU GLU A . n 
B 1 21  PHE 21  21  21  PHE PHE A . n 
B 1 22  PHE 22  22  22  PHE PHE A . n 
B 1 23  PRO 23  23  23  PRO PRO A . n 
B 1 24  ILE 24  24  24  ILE ILE A . n 
B 1 25  ALA 25  25  25  ALA ALA A . n 
B 1 26  ASP 26  26  26  ASP ASP A . n 
B 1 27  GLY 27  27  27  GLY GLY A . n 
B 1 28  ASP 28  28  28  ASP ASP A . n 
B 1 29  GLN 29  29  29  GLN GLN A . n 
B 1 30  GLN 30  30  30  GLN GLN A . n 
B 1 31  SER 31  31  31  SER SER A . n 
B 1 32  PRO 32  32  32  PRO PRO A . n 
B 1 33  ILE 33  33  33  ILE ILE A . n 
B 1 34  GLU 34  34  34  GLU GLU A . n 
B 1 35  ILE 35  35  35  ILE ILE A . n 
B 1 36  LYS 36  36  36  LYS LYS A . n 
B 1 37  THR 37  37  37  THR THR A . n 
B 1 38  LYS 38  38  38  LYS LYS A . n 
B 1 39  GLU 39  39  39  GLU GLU A . n 
B 1 40  VAL 40  40  40  VAL VAL A . n 
B 1 41  LYS 41  41  41  LYS LYS A . n 
B 1 42  TYR 42  42  42  TYR TYR A . n 
B 1 43  ASP 43  43  43  ASP ASP A . n 
B 1 44  SER 44  44  44  SER SER A . n 
B 1 45  SER 45  45  45  SER SER A . n 
B 1 46  LEU 46  46  46  LEU LEU A . n 
B 1 47  ARG 47  47  47  ARG ARG A . n 
B 1 48  PRO 48  48  48  PRO PRO A . n 
B 1 49  LEU 49  49  49  LEU LEU A . n 
B 1 50  SER 50  50  50  SER SER A . n 
B 1 51  ILE 51  51  51  ILE ILE A . n 
B 1 52  LYS 52  52  52  LYS LYS A . n 
B 1 53  TYR 53  53  53  TYR TYR A . n 
B 1 54  ASP 54  54  54  ASP ASP A . n 
B 1 55  PRO 55  55  55  PRO PRO A . n 
B 1 56  SER 56  56  56  SER SER A . n 
B 1 57  SER 57  57  57  SER SER A . n 
B 1 58  ALA 58  58  58  ALA ALA A . n 
B 1 59  LYS 59  59  59  LYS LYS A . n 
B 1 60  ILE 60  60  60  ILE ILE A . n 
B 1 61  ILE 61  61  61  ILE ILE A . n 
B 1 62  SER 62  62  62  SER SER A . n 
B 1 63  ASN 63  63  63  ASN ASN A . n 
B 1 64  SER 64  64  64  SER SER A . n 
B 1 65  GLY 65  65  65  GLY GLY A . n 
B 1 66  HIS 66  66  66  HIS HIS A . n 
B 1 67  SER 67  67  67  SER SER A . n 
B 1 68  PHE 68  68  68  PHE PHE A . n 
B 1 69  ASN 69  69  69  ASN ASN A . n 
B 1 70  VAL 70  70  70  VAL VAL A . n 
B 1 71  ASP 71  71  71  ASP ASP A . n 
B 1 72  PHE 72  72  72  PHE PHE A . n 
B 1 73  ASP 73  73  73  ASP ASP A . n 
B 1 74  ASP 74  74  74  ASP ASP A . n 
B 1 75  THR 75  75  75  THR THR A . n 
B 1 76  GLU 76  76  76  GLU GLU A . n 
B 1 77  ASN 77  77  77  ASN ASN A . n 
B 1 78  LYS 78  78  78  LYS LYS A . n 
B 1 79  SER 79  79  79  SER SER A . n 
B 1 80  VAL 80  80  80  VAL VAL A . n 
B 1 81  LEU 81  81  81  LEU LEU A . n 
B 1 82  ARG 82  82  82  ARG ARG A . n 
B 1 83  GLY 83  83  83  GLY GLY A . n 
B 1 84  GLY 84  84  84  GLY GLY A . n 
B 1 85  PRO 85  85  85  PRO PRO A . n 
B 1 86  LEU 86  86  86  LEU LEU A . n 
B 1 87  THR 87  87  87  THR THR A . n 
B 1 88  GLY 88  88  88  GLY GLY A . n 
B 1 89  SER 89  89  89  SER SER A . n 
B 1 90  TYR 90  90  90  TYR TYR A . n 
B 1 91  ARG 91  91  91  ARG ARG A . n 
B 1 92  LEU 92  92  92  LEU LEU A . n 
B 1 93  ARG 93  93  93  ARG ARG A . n 
B 1 94  GLN 94  94  94  GLN GLN A . n 
B 1 95  VAL 95  95  95  VAL VAL A . n 
B 1 96  HIS 96  96  96  HIS HIS A . n 
B 1 97  LEU 97  97  97  LEU LEU A . n 
B 1 98  HIS 98  98  98  HIS HIS A . n 
B 1 99  TRP 99  99  99  TRP TRP A . n 
B 1 100 GLY 100 100 100 GLY GLY A . n 
B 1 101 SER 101 101 101 SER SER A . n 
B 1 102 ALA 102 102 102 ALA ALA A . n 
B 1 103 ASP 103 103 103 ASP ASP A . n 
B 1 104 ASP 104 104 104 ASP ASP A . n 
B 1 105 HIS 105 105 105 HIS HIS A . n 
B 1 106 GLY 106 106 106 GLY GLY A . n 
B 1 107 SER 107 107 107 SER SER A . n 
B 1 108 GLU 108 108 108 GLU GLU A . n 
B 1 109 HIS 109 109 109 HIS HIS A . n 
B 1 110 ILE 110 110 110 ILE ILE A . n 
B 1 111 VAL 111 111 111 VAL VAL A . n 
B 1 112 ASP 112 112 112 ASP ASP A . n 
B 1 113 GLY 113 113 113 GLY GLY A . n 
B 1 114 VAL 114 114 114 VAL VAL A . n 
B 1 115 SER 115 115 115 SER SER A . n 
B 1 116 TYR 116 116 116 TYR TYR A . n 
B 1 117 ALA 117 117 117 ALA ALA A . n 
B 1 118 ALA 118 118 118 ALA ALA A . n 
B 1 119 GLU 119 119 119 GLU GLU A . n 
B 1 120 LEU 120 120 120 LEU LEU A . n 
B 1 121 HIS 121 121 121 HIS HIS A . n 
B 1 122 VAL 122 122 122 VAL VAL A . n 
B 1 123 VAL 123 123 123 VAL VAL A . n 
B 1 124 HIS 124 124 124 HIS HIS A . n 
B 1 125 TRP 125 125 125 TRP TRP A . n 
B 1 126 ASN 126 126 126 ASN ASN A . n 
B 1 127 SER 127 127 127 SER SER A . n 
B 1 128 ASP 128 128 128 ASP ASP A . n 
B 1 129 LYS 129 129 129 LYS LYS A . n 
B 1 130 TYR 130 130 130 TYR TYR A . n 
B 1 131 PRO 131 131 131 PRO PRO A . n 
B 1 132 SER 132 132 132 SER SER A . n 
B 1 133 PHE 133 133 133 PHE PHE A . n 
B 1 134 VAL 134 134 134 VAL VAL A . n 
B 1 135 GLU 135 135 135 GLU GLU A . n 
B 1 136 ALA 136 136 136 ALA ALA A . n 
B 1 137 ALA 137 137 137 ALA ALA A . n 
B 1 138 HIS 138 138 138 HIS HIS A . n 
B 1 139 GLU 139 139 139 GLU GLU A . n 
B 1 140 PRO 140 140 140 PRO PRO A . n 
B 1 141 ASP 141 141 141 ASP ASP A . n 
B 1 142 GLY 142 142 142 GLY GLY A . n 
B 1 143 LEU 143 143 143 LEU LEU A . n 
B 1 144 ALA 144 144 144 ALA ALA A . n 
B 1 145 VAL 145 145 145 VAL VAL A . n 
B 1 146 LEU 146 146 146 LEU LEU A . n 
B 1 147 GLY 147 147 147 GLY GLY A . n 
B 1 148 VAL 148 148 148 VAL VAL A . n 
B 1 149 PHE 149 149 149 PHE PHE A . n 
B 1 150 LEU 150 150 150 LEU LEU A . n 
B 1 151 GLN 151 151 151 GLN GLN A . n 
B 1 152 ILE 152 152 152 ILE ILE A . n 
B 1 153 GLY 153 153 153 GLY GLY A . n 
B 1 154 GLU 154 154 154 GLU GLU A . n 
B 1 155 PRO 155 155 155 PRO PRO A . n 
B 1 156 ASN 156 156 156 ASN ASN A . n 
B 1 157 SER 157 157 157 SER SER A . n 
B 1 158 GLN 158 158 158 GLN GLN A . n 
B 1 159 LEU 159 159 159 LEU LEU A . n 
B 1 160 GLN 160 160 160 GLN GLN A . n 
B 1 161 LYS 161 161 161 LYS LYS A . n 
B 1 162 ILE 162 162 162 ILE ILE A . n 
B 1 163 THR 163 163 163 THR THR A . n 
B 1 164 ASP 164 164 164 ASP ASP A . n 
B 1 165 THR 165 165 165 THR THR A . n 
B 1 166 LEU 166 166 166 LEU LEU A . n 
B 1 167 ASP 167 167 167 ASP ASP A . n 
B 1 168 SER 168 168 168 SER SER A . n 
B 1 169 ILE 169 169 169 ILE ILE A . n 
B 1 170 LYS 170 170 170 LYS LYS A . n 
B 1 171 GLU 171 171 171 GLU GLU A . n 
B 1 172 LYS 172 172 172 LYS LYS A . n 
B 1 173 GLY 173 173 173 GLY GLY A . n 
B 1 174 LYS 174 174 174 LYS LYS A . n 
B 1 175 GLN 175 175 175 GLN GLN A . n 
B 1 176 THR 176 176 176 THR THR A . n 
B 1 177 ARG 177 177 177 ARG ARG A . n 
B 1 178 PHE 178 178 178 PHE PHE A . n 
B 1 179 THR 179 179 179 THR THR A . n 
B 1 180 ASN 180 180 180 ASN ASN A . n 
B 1 181 PHE 181 181 181 PHE PHE A . n 
B 1 182 ASP 182 182 182 ASP ASP A . n 
B 1 183 LEU 183 183 183 LEU LEU A . n 
B 1 184 LEU 184 184 184 LEU LEU A . n 
B 1 185 SER 185 185 185 SER SER A . n 
B 1 186 LEU 186 186 186 LEU LEU A . n 
B 1 187 LEU 187 187 187 LEU LEU A . n 
B 1 188 PRO 188 188 188 PRO PRO A . n 
B 1 189 PRO 189 189 189 PRO PRO A . n 
B 1 190 SER 190 190 190 SER SER A . n 
B 1 191 TRP 191 191 191 TRP TRP A . n 
B 1 192 ASP 192 192 192 ASP ASP A . n 
B 1 193 TYR 193 193 193 TYR TYR A . n 
B 1 194 TRP 194 194 194 TRP TRP A . n 
B 1 195 THR 195 195 195 THR THR A . n 
B 1 196 TYR 196 196 196 TYR TYR A . n 
B 1 197 PRO 197 197 197 PRO PRO A . n 
B 1 198 GLY 198 198 198 GLY GLY A . n 
B 1 199 SER 199 199 199 SER SER A . n 
B 1 200 LEU 200 200 200 LEU LEU A . n 
B 1 201 THR 201 201 201 THR THR A . n 
B 1 202 VAL 202 202 202 VAL VAL A . n 
B 1 203 PRO 203 203 203 PRO PRO A . n 
B 1 204 PRO 204 204 204 PRO PRO A . n 
B 1 205 LEU 205 205 205 LEU LEU A . n 
B 1 206 LEU 206 206 206 LEU LEU A . n 
B 1 207 GLU 207 207 207 GLU GLU A . n 
B 1 208 SER 208 208 208 SER SER A . n 
B 1 209 VAL 209 209 209 VAL VAL A . n 
B 1 210 THR 210 210 210 THR THR A . n 
B 1 211 TRP 211 211 211 TRP TRP A . n 
B 1 212 ILE 212 212 212 ILE ILE A . n 
B 1 213 VAL 213 213 213 VAL VAL A . n 
B 1 214 LEU 214 214 214 LEU LEU A . n 
B 1 215 LYS 215 215 215 LYS LYS A . n 
B 1 216 GLN 216 216 216 GLN GLN A . n 
B 1 217 PRO 217 217 217 PRO PRO A . n 
B 1 218 ILE 218 218 218 ILE ILE A . n 
B 1 219 ASN 219 219 219 ASN ASN A . n 
B 1 220 ILE 220 220 220 ILE ILE A . n 
B 1 221 SER 221 221 221 SER SER A . n 
B 1 222 SER 222 222 222 SER SER A . n 
B 1 223 GLN 223 223 223 GLN GLN A . n 
B 1 224 GLN 224 224 224 GLN GLN A . n 
B 1 225 LEU 225 225 225 LEU LEU A . n 
B 1 226 ALA 226 226 226 ALA ALA A . n 
B 1 227 LYS 227 227 227 LYS LYS A . n 
B 1 228 PHE 228 228 228 PHE PHE A . n 
B 1 229 ARG 229 229 229 ARG ARG A . n 
B 1 230 SER 230 230 230 SER SER A . n 
B 1 231 LEU 231 231 231 LEU LEU A . n 
B 1 232 LEU 232 232 232 LEU LEU A . n 
B 1 233 CYS 233 233 233 CYS CYS A . n 
B 1 234 THR 234 234 234 THR THR A . n 
B 1 235 ALA 235 235 235 ALA ALA A . n 
B 1 236 GLU 236 236 236 GLU GLU A . n 
B 1 237 GLY 237 237 237 GLY GLY A . n 
B 1 238 GLU 238 238 238 GLU GLU A . n 
B 1 239 ALA 239 239 239 ALA ALA A . n 
B 1 240 ALA 240 240 240 ALA ALA A . n 
B 1 241 ALA 241 241 241 ALA ALA A . n 
B 1 242 PHE 242 242 242 PHE PHE A . n 
B 1 243 LEU 243 243 243 LEU LEU A . n 
B 1 244 VAL 244 244 244 VAL VAL A . n 
B 1 245 SER 245 245 245 SER SER A . n 
B 1 246 ASN 246 246 246 ASN ASN A . n 
B 1 247 HIS 247 247 247 HIS HIS A . n 
B 1 248 ARG 248 248 248 ARG ARG A . n 
B 1 249 PRO 249 249 249 PRO PRO A . n 
B 1 250 PRO 250 250 250 PRO PRO A . n 
B 1 251 GLN 251 251 251 GLN GLN A . n 
B 1 252 PRO 252 252 252 PRO PRO A . n 
B 1 253 LEU 253 253 253 LEU LEU A . n 
B 1 254 LYS 254 254 254 LYS LYS A . n 
B 1 255 GLY 255 255 255 GLY GLY A . n 
B 1 256 ARG 256 256 256 ARG ARG A . n 
B 1 257 LYS 257 257 257 LYS LYS A . n 
B 1 258 VAL 258 258 258 VAL VAL A . n 
B 1 259 ARG 259 259 259 ARG ARG A . n 
B 1 260 ALA 260 260 260 ALA ALA A . n 
B 1 261 SER 261 261 261 SER SER A . n 
B 1 262 PHE 262 262 262 PHE PHE A . n 
B 1 263 HIS 263 263 263 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 1   ZN  ZN  B . 
D 3 PEG 1   302 1   PEG PEG B . 
E 4 V1F 1   303 1   V1F V1F B . 
F 5 EDO 1   304 1   EDO EDO B . 
G 2 ZN  1   301 2   ZN  ZN  A . 
H 6 CIT 1   302 1   CIT CIT A . 
I 4 V1F 1   303 2   V1F V1F A . 
J 5 EDO 1   304 4   EDO EDO A . 
K 5 EDO 1   305 5   EDO EDO A . 
L 5 EDO 1   306 6   EDO EDO A . 
M 7 HOH 1   401 1   HOH HOH B . 
M 7 HOH 2   402 2   HOH HOH B . 
M 7 HOH 3   403 7   HOH HOH B . 
M 7 HOH 4   404 9   HOH HOH B . 
M 7 HOH 5   405 16  HOH HOH B . 
M 7 HOH 6   406 19  HOH HOH B . 
M 7 HOH 7   407 22  HOH HOH B . 
M 7 HOH 8   408 23  HOH HOH B . 
M 7 HOH 9   409 24  HOH HOH B . 
M 7 HOH 10  410 28  HOH HOH B . 
M 7 HOH 11  411 30  HOH HOH B . 
M 7 HOH 12  412 31  HOH HOH B . 
M 7 HOH 13  413 35  HOH HOH B . 
M 7 HOH 14  414 36  HOH HOH B . 
M 7 HOH 15  415 37  HOH HOH B . 
M 7 HOH 16  416 39  HOH HOH B . 
M 7 HOH 17  417 40  HOH HOH B . 
M 7 HOH 18  418 41  HOH HOH B . 
M 7 HOH 19  419 44  HOH HOH B . 
M 7 HOH 20  420 47  HOH HOH B . 
M 7 HOH 21  421 50  HOH HOH B . 
M 7 HOH 22  422 51  HOH HOH B . 
M 7 HOH 23  423 52  HOH HOH B . 
M 7 HOH 24  424 53  HOH HOH B . 
M 7 HOH 25  425 58  HOH HOH B . 
M 7 HOH 26  426 59  HOH HOH B . 
M 7 HOH 27  427 60  HOH HOH B . 
M 7 HOH 28  428 61  HOH HOH B . 
M 7 HOH 29  429 62  HOH HOH B . 
M 7 HOH 30  430 64  HOH HOH B . 
M 7 HOH 31  431 66  HOH HOH B . 
M 7 HOH 32  432 68  HOH HOH B . 
M 7 HOH 33  433 70  HOH HOH B . 
M 7 HOH 34  434 73  HOH HOH B . 
M 7 HOH 35  435 74  HOH HOH B . 
M 7 HOH 36  436 75  HOH HOH B . 
M 7 HOH 37  437 76  HOH HOH B . 
M 7 HOH 38  438 77  HOH HOH B . 
M 7 HOH 39  439 78  HOH HOH B . 
M 7 HOH 40  440 83  HOH HOH B . 
M 7 HOH 41  441 84  HOH HOH B . 
M 7 HOH 42  442 86  HOH HOH B . 
M 7 HOH 43  443 87  HOH HOH B . 
M 7 HOH 44  444 89  HOH HOH B . 
M 7 HOH 45  445 90  HOH HOH B . 
M 7 HOH 46  446 91  HOH HOH B . 
M 7 HOH 47  447 94  HOH HOH B . 
M 7 HOH 48  448 97  HOH HOH B . 
M 7 HOH 49  449 100 HOH HOH B . 
M 7 HOH 50  450 102 HOH HOH B . 
M 7 HOH 51  451 104 HOH HOH B . 
M 7 HOH 52  452 106 HOH HOH B . 
M 7 HOH 53  453 107 HOH HOH B . 
M 7 HOH 54  454 108 HOH HOH B . 
M 7 HOH 55  455 111 HOH HOH B . 
M 7 HOH 56  456 112 HOH HOH B . 
M 7 HOH 57  457 114 HOH HOH B . 
M 7 HOH 58  458 117 HOH HOH B . 
M 7 HOH 59  459 118 HOH HOH B . 
M 7 HOH 60  460 120 HOH HOH B . 
M 7 HOH 61  461 122 HOH HOH B . 
M 7 HOH 62  462 124 HOH HOH B . 
M 7 HOH 63  463 127 HOH HOH B . 
M 7 HOH 64  464 128 HOH HOH B . 
M 7 HOH 65  465 129 HOH HOH B . 
M 7 HOH 66  466 131 HOH HOH B . 
M 7 HOH 67  467 132 HOH HOH B . 
M 7 HOH 68  468 133 HOH HOH B . 
M 7 HOH 69  469 135 HOH HOH B . 
M 7 HOH 70  470 136 HOH HOH B . 
M 7 HOH 71  471 139 HOH HOH B . 
M 7 HOH 72  472 140 HOH HOH B . 
M 7 HOH 73  473 141 HOH HOH B . 
M 7 HOH 74  474 142 HOH HOH B . 
M 7 HOH 75  475 144 HOH HOH B . 
M 7 HOH 76  476 146 HOH HOH B . 
M 7 HOH 77  477 147 HOH HOH B . 
M 7 HOH 78  478 148 HOH HOH B . 
M 7 HOH 79  479 149 HOH HOH B . 
M 7 HOH 80  480 150 HOH HOH B . 
M 7 HOH 81  481 152 HOH HOH B . 
M 7 HOH 82  482 153 HOH HOH B . 
M 7 HOH 83  483 154 HOH HOH B . 
M 7 HOH 84  484 155 HOH HOH B . 
M 7 HOH 85  485 156 HOH HOH B . 
M 7 HOH 86  486 158 HOH HOH B . 
M 7 HOH 87  487 160 HOH HOH B . 
M 7 HOH 88  488 164 HOH HOH B . 
M 7 HOH 89  489 166 HOH HOH B . 
M 7 HOH 90  490 167 HOH HOH B . 
M 7 HOH 91  491 170 HOH HOH B . 
M 7 HOH 92  492 174 HOH HOH B . 
M 7 HOH 93  493 177 HOH HOH B . 
M 7 HOH 94  494 179 HOH HOH B . 
M 7 HOH 95  495 180 HOH HOH B . 
M 7 HOH 96  496 184 HOH HOH B . 
M 7 HOH 97  497 185 HOH HOH B . 
M 7 HOH 98  498 187 HOH HOH B . 
M 7 HOH 99  499 188 HOH HOH B . 
M 7 HOH 100 500 189 HOH HOH B . 
M 7 HOH 101 501 190 HOH HOH B . 
M 7 HOH 102 502 193 HOH HOH B . 
M 7 HOH 103 503 195 HOH HOH B . 
M 7 HOH 104 504 196 HOH HOH B . 
M 7 HOH 105 505 197 HOH HOH B . 
M 7 HOH 106 506 198 HOH HOH B . 
M 7 HOH 107 507 200 HOH HOH B . 
M 7 HOH 108 508 202 HOH HOH B . 
M 7 HOH 109 509 206 HOH HOH B . 
M 7 HOH 110 510 208 HOH HOH B . 
M 7 HOH 111 511 209 HOH HOH B . 
M 7 HOH 112 512 210 HOH HOH B . 
M 7 HOH 113 513 211 HOH HOH B . 
M 7 HOH 114 514 214 HOH HOH B . 
M 7 HOH 115 515 215 HOH HOH B . 
M 7 HOH 116 516 216 HOH HOH B . 
M 7 HOH 117 517 217 HOH HOH B . 
M 7 HOH 118 518 220 HOH HOH B . 
M 7 HOH 119 519 223 HOH HOH B . 
M 7 HOH 120 520 226 HOH HOH B . 
M 7 HOH 121 521 230 HOH HOH B . 
M 7 HOH 122 522 231 HOH HOH B . 
M 7 HOH 123 523 235 HOH HOH B . 
M 7 HOH 124 524 236 HOH HOH B . 
M 7 HOH 125 525 239 HOH HOH B . 
M 7 HOH 126 526 243 HOH HOH B . 
M 7 HOH 127 527 244 HOH HOH B . 
M 7 HOH 128 528 245 HOH HOH B . 
M 7 HOH 129 529 248 HOH HOH B . 
M 7 HOH 130 530 250 HOH HOH B . 
M 7 HOH 131 531 251 HOH HOH B . 
M 7 HOH 132 532 254 HOH HOH B . 
M 7 HOH 133 533 257 HOH HOH B . 
M 7 HOH 134 534 261 HOH HOH B . 
M 7 HOH 135 535 263 HOH HOH B . 
M 7 HOH 136 536 264 HOH HOH B . 
M 7 HOH 137 537 265 HOH HOH B . 
M 7 HOH 138 538 267 HOH HOH B . 
M 7 HOH 139 539 268 HOH HOH B . 
M 7 HOH 140 540 271 HOH HOH B . 
M 7 HOH 141 541 276 HOH HOH B . 
M 7 HOH 142 542 278 HOH HOH B . 
M 7 HOH 143 543 280 HOH HOH B . 
M 7 HOH 144 544 282 HOH HOH B . 
M 7 HOH 145 545 286 HOH HOH B . 
M 7 HOH 146 546 292 HOH HOH B . 
M 7 HOH 147 547 294 HOH HOH B . 
M 7 HOH 148 548 295 HOH HOH B . 
M 7 HOH 149 549 298 HOH HOH B . 
M 7 HOH 150 550 303 HOH HOH B . 
M 7 HOH 151 551 308 HOH HOH B . 
M 7 HOH 152 552 309 HOH HOH B . 
M 7 HOH 153 553 310 HOH HOH B . 
M 7 HOH 154 554 312 HOH HOH B . 
M 7 HOH 155 555 313 HOH HOH B . 
M 7 HOH 156 556 315 HOH HOH B . 
M 7 HOH 157 557 316 HOH HOH B . 
M 7 HOH 158 558 319 HOH HOH B . 
M 7 HOH 159 559 320 HOH HOH B . 
M 7 HOH 160 560 321 HOH HOH B . 
M 7 HOH 161 561 322 HOH HOH B . 
M 7 HOH 162 562 324 HOH HOH B . 
M 7 HOH 163 563 326 HOH HOH B . 
M 7 HOH 164 564 329 HOH HOH B . 
M 7 HOH 165 565 331 HOH HOH B . 
M 7 HOH 166 566 334 HOH HOH B . 
M 7 HOH 167 567 335 HOH HOH B . 
M 7 HOH 168 568 336 HOH HOH B . 
M 7 HOH 169 569 338 HOH HOH B . 
M 7 HOH 170 570 340 HOH HOH B . 
M 7 HOH 171 571 343 HOH HOH B . 
M 7 HOH 172 572 345 HOH HOH B . 
M 7 HOH 173 573 347 HOH HOH B . 
M 7 HOH 174 574 348 HOH HOH B . 
M 7 HOH 175 575 349 HOH HOH B . 
M 7 HOH 176 576 351 HOH HOH B . 
M 7 HOH 177 577 353 HOH HOH B . 
M 7 HOH 178 578 354 HOH HOH B . 
M 7 HOH 179 579 365 HOH HOH B . 
M 7 HOH 180 580 366 HOH HOH B . 
M 7 HOH 181 581 367 HOH HOH B . 
M 7 HOH 182 582 369 HOH HOH B . 
M 7 HOH 183 583 371 HOH HOH B . 
M 7 HOH 184 584 375 HOH HOH B . 
M 7 HOH 185 585 378 HOH HOH B . 
M 7 HOH 186 586 380 HOH HOH B . 
M 7 HOH 187 587 385 HOH HOH B . 
M 7 HOH 188 588 386 HOH HOH B . 
M 7 HOH 189 589 390 HOH HOH B . 
M 7 HOH 190 590 392 HOH HOH B . 
M 7 HOH 191 591 396 HOH HOH B . 
M 7 HOH 192 592 397 HOH HOH B . 
M 7 HOH 193 593 398 HOH HOH B . 
M 7 HOH 194 594 399 HOH HOH B . 
M 7 HOH 195 595 401 HOH HOH B . 
M 7 HOH 196 596 406 HOH HOH B . 
M 7 HOH 197 597 411 HOH HOH B . 
M 7 HOH 198 598 413 HOH HOH B . 
M 7 HOH 199 599 417 HOH HOH B . 
M 7 HOH 200 600 419 HOH HOH B . 
M 7 HOH 201 601 424 HOH HOH B . 
M 7 HOH 202 602 425 HOH HOH B . 
M 7 HOH 203 603 427 HOH HOH B . 
M 7 HOH 204 604 428 HOH HOH B . 
M 7 HOH 205 605 431 HOH HOH B . 
M 7 HOH 206 606 432 HOH HOH B . 
M 7 HOH 207 607 433 HOH HOH B . 
M 7 HOH 208 608 434 HOH HOH B . 
M 7 HOH 209 609 435 HOH HOH B . 
M 7 HOH 210 610 436 HOH HOH B . 
M 7 HOH 211 611 437 HOH HOH B . 
M 7 HOH 212 612 448 HOH HOH B . 
M 7 HOH 213 613 449 HOH HOH B . 
M 7 HOH 214 614 450 HOH HOH B . 
M 7 HOH 215 615 451 HOH HOH B . 
M 7 HOH 216 616 452 HOH HOH B . 
M 7 HOH 217 617 453 HOH HOH B . 
M 7 HOH 218 618 454 HOH HOH B . 
M 7 HOH 219 619 455 HOH HOH B . 
M 7 HOH 220 620 456 HOH HOH B . 
M 7 HOH 221 621 457 HOH HOH B . 
M 7 HOH 222 622 459 HOH HOH B . 
M 7 HOH 223 623 460 HOH HOH B . 
M 7 HOH 224 624 461 HOH HOH B . 
M 7 HOH 225 625 462 HOH HOH B . 
M 7 HOH 226 626 465 HOH HOH B . 
M 7 HOH 227 627 466 HOH HOH B . 
M 7 HOH 228 628 467 HOH HOH B . 
M 7 HOH 229 629 468 HOH HOH B . 
M 7 HOH 230 630 469 HOH HOH B . 
M 7 HOH 231 631 471 HOH HOH B . 
M 7 HOH 232 632 472 HOH HOH B . 
M 7 HOH 233 633 473 HOH HOH B . 
M 7 HOH 234 634 474 HOH HOH B . 
M 7 HOH 235 635 477 HOH HOH B . 
M 7 HOH 236 636 478 HOH HOH B . 
M 7 HOH 237 637 481 HOH HOH B . 
M 7 HOH 238 638 482 HOH HOH B . 
M 7 HOH 239 639 483 HOH HOH B . 
N 7 HOH 1   401 157 HOH HOH A . 
N 7 HOH 2   402 470 HOH HOH A . 
N 7 HOH 3   403 3   HOH HOH A . 
N 7 HOH 4   404 4   HOH HOH A . 
N 7 HOH 5   405 5   HOH HOH A . 
N 7 HOH 6   406 6   HOH HOH A . 
N 7 HOH 7   407 8   HOH HOH A . 
N 7 HOH 8   408 10  HOH HOH A . 
N 7 HOH 9   409 11  HOH HOH A . 
N 7 HOH 10  410 12  HOH HOH A . 
N 7 HOH 11  411 13  HOH HOH A . 
N 7 HOH 12  412 14  HOH HOH A . 
N 7 HOH 13  413 15  HOH HOH A . 
N 7 HOH 14  414 17  HOH HOH A . 
N 7 HOH 15  415 18  HOH HOH A . 
N 7 HOH 16  416 20  HOH HOH A . 
N 7 HOH 17  417 21  HOH HOH A . 
N 7 HOH 18  418 25  HOH HOH A . 
N 7 HOH 19  419 26  HOH HOH A . 
N 7 HOH 20  420 27  HOH HOH A . 
N 7 HOH 21  421 29  HOH HOH A . 
N 7 HOH 22  422 32  HOH HOH A . 
N 7 HOH 23  423 33  HOH HOH A . 
N 7 HOH 24  424 34  HOH HOH A . 
N 7 HOH 25  425 38  HOH HOH A . 
N 7 HOH 26  426 42  HOH HOH A . 
N 7 HOH 27  427 43  HOH HOH A . 
N 7 HOH 28  428 45  HOH HOH A . 
N 7 HOH 29  429 46  HOH HOH A . 
N 7 HOH 30  430 48  HOH HOH A . 
N 7 HOH 31  431 49  HOH HOH A . 
N 7 HOH 32  432 54  HOH HOH A . 
N 7 HOH 33  433 55  HOH HOH A . 
N 7 HOH 34  434 56  HOH HOH A . 
N 7 HOH 35  435 57  HOH HOH A . 
N 7 HOH 36  436 63  HOH HOH A . 
N 7 HOH 37  437 65  HOH HOH A . 
N 7 HOH 38  438 67  HOH HOH A . 
N 7 HOH 39  439 69  HOH HOH A . 
N 7 HOH 40  440 71  HOH HOH A . 
N 7 HOH 41  441 72  HOH HOH A . 
N 7 HOH 42  442 79  HOH HOH A . 
N 7 HOH 43  443 80  HOH HOH A . 
N 7 HOH 44  444 81  HOH HOH A . 
N 7 HOH 45  445 82  HOH HOH A . 
N 7 HOH 46  446 85  HOH HOH A . 
N 7 HOH 47  447 88  HOH HOH A . 
N 7 HOH 48  448 92  HOH HOH A . 
N 7 HOH 49  449 93  HOH HOH A . 
N 7 HOH 50  450 95  HOH HOH A . 
N 7 HOH 51  451 96  HOH HOH A . 
N 7 HOH 52  452 98  HOH HOH A . 
N 7 HOH 53  453 99  HOH HOH A . 
N 7 HOH 54  454 101 HOH HOH A . 
N 7 HOH 55  455 103 HOH HOH A . 
N 7 HOH 56  456 105 HOH HOH A . 
N 7 HOH 57  457 109 HOH HOH A . 
N 7 HOH 58  458 110 HOH HOH A . 
N 7 HOH 59  459 113 HOH HOH A . 
N 7 HOH 60  460 115 HOH HOH A . 
N 7 HOH 61  461 116 HOH HOH A . 
N 7 HOH 62  462 119 HOH HOH A . 
N 7 HOH 63  463 121 HOH HOH A . 
N 7 HOH 64  464 123 HOH HOH A . 
N 7 HOH 65  465 125 HOH HOH A . 
N 7 HOH 66  466 126 HOH HOH A . 
N 7 HOH 67  467 130 HOH HOH A . 
N 7 HOH 68  468 134 HOH HOH A . 
N 7 HOH 69  469 137 HOH HOH A . 
N 7 HOH 70  470 138 HOH HOH A . 
N 7 HOH 71  471 143 HOH HOH A . 
N 7 HOH 72  472 145 HOH HOH A . 
N 7 HOH 73  473 151 HOH HOH A . 
N 7 HOH 74  474 159 HOH HOH A . 
N 7 HOH 75  475 161 HOH HOH A . 
N 7 HOH 76  476 162 HOH HOH A . 
N 7 HOH 77  477 163 HOH HOH A . 
N 7 HOH 78  478 165 HOH HOH A . 
N 7 HOH 79  479 168 HOH HOH A . 
N 7 HOH 80  480 169 HOH HOH A . 
N 7 HOH 81  481 171 HOH HOH A . 
N 7 HOH 82  482 172 HOH HOH A . 
N 7 HOH 83  483 173 HOH HOH A . 
N 7 HOH 84  484 175 HOH HOH A . 
N 7 HOH 85  485 176 HOH HOH A . 
N 7 HOH 86  486 178 HOH HOH A . 
N 7 HOH 87  487 181 HOH HOH A . 
N 7 HOH 88  488 182 HOH HOH A . 
N 7 HOH 89  489 183 HOH HOH A . 
N 7 HOH 90  490 186 HOH HOH A . 
N 7 HOH 91  491 191 HOH HOH A . 
N 7 HOH 92  492 192 HOH HOH A . 
N 7 HOH 93  493 194 HOH HOH A . 
N 7 HOH 94  494 199 HOH HOH A . 
N 7 HOH 95  495 201 HOH HOH A . 
N 7 HOH 96  496 203 HOH HOH A . 
N 7 HOH 97  497 204 HOH HOH A . 
N 7 HOH 98  498 205 HOH HOH A . 
N 7 HOH 99  499 207 HOH HOH A . 
N 7 HOH 100 500 212 HOH HOH A . 
N 7 HOH 101 501 213 HOH HOH A . 
N 7 HOH 102 502 218 HOH HOH A . 
N 7 HOH 103 503 219 HOH HOH A . 
N 7 HOH 104 504 221 HOH HOH A . 
N 7 HOH 105 505 222 HOH HOH A . 
N 7 HOH 106 506 224 HOH HOH A . 
N 7 HOH 107 507 225 HOH HOH A . 
N 7 HOH 108 508 227 HOH HOH A . 
N 7 HOH 109 509 228 HOH HOH A . 
N 7 HOH 110 510 229 HOH HOH A . 
N 7 HOH 111 511 232 HOH HOH A . 
N 7 HOH 112 512 233 HOH HOH A . 
N 7 HOH 113 513 234 HOH HOH A . 
N 7 HOH 114 514 237 HOH HOH A . 
N 7 HOH 115 515 238 HOH HOH A . 
N 7 HOH 116 516 240 HOH HOH A . 
N 7 HOH 117 517 241 HOH HOH A . 
N 7 HOH 118 518 242 HOH HOH A . 
N 7 HOH 119 519 246 HOH HOH A . 
N 7 HOH 120 520 247 HOH HOH A . 
N 7 HOH 121 521 249 HOH HOH A . 
N 7 HOH 122 522 252 HOH HOH A . 
N 7 HOH 123 523 253 HOH HOH A . 
N 7 HOH 124 524 255 HOH HOH A . 
N 7 HOH 125 525 256 HOH HOH A . 
N 7 HOH 126 526 258 HOH HOH A . 
N 7 HOH 127 527 259 HOH HOH A . 
N 7 HOH 128 528 260 HOH HOH A . 
N 7 HOH 129 529 262 HOH HOH A . 
N 7 HOH 130 530 266 HOH HOH A . 
N 7 HOH 131 531 269 HOH HOH A . 
N 7 HOH 132 532 270 HOH HOH A . 
N 7 HOH 133 533 272 HOH HOH A . 
N 7 HOH 134 534 273 HOH HOH A . 
N 7 HOH 135 535 274 HOH HOH A . 
N 7 HOH 136 536 275 HOH HOH A . 
N 7 HOH 137 537 277 HOH HOH A . 
N 7 HOH 138 538 279 HOH HOH A . 
N 7 HOH 139 539 281 HOH HOH A . 
N 7 HOH 140 540 283 HOH HOH A . 
N 7 HOH 141 541 284 HOH HOH A . 
N 7 HOH 142 542 285 HOH HOH A . 
N 7 HOH 143 543 287 HOH HOH A . 
N 7 HOH 144 544 288 HOH HOH A . 
N 7 HOH 145 545 289 HOH HOH A . 
N 7 HOH 146 546 290 HOH HOH A . 
N 7 HOH 147 547 291 HOH HOH A . 
N 7 HOH 148 548 293 HOH HOH A . 
N 7 HOH 149 549 296 HOH HOH A . 
N 7 HOH 150 550 297 HOH HOH A . 
N 7 HOH 151 551 299 HOH HOH A . 
N 7 HOH 152 552 300 HOH HOH A . 
N 7 HOH 153 553 301 HOH HOH A . 
N 7 HOH 154 554 302 HOH HOH A . 
N 7 HOH 155 555 304 HOH HOH A . 
N 7 HOH 156 556 305 HOH HOH A . 
N 7 HOH 157 557 306 HOH HOH A . 
N 7 HOH 158 558 307 HOH HOH A . 
N 7 HOH 159 559 311 HOH HOH A . 
N 7 HOH 160 560 314 HOH HOH A . 
N 7 HOH 161 561 317 HOH HOH A . 
N 7 HOH 162 562 318 HOH HOH A . 
N 7 HOH 163 563 323 HOH HOH A . 
N 7 HOH 164 564 325 HOH HOH A . 
N 7 HOH 165 565 327 HOH HOH A . 
N 7 HOH 166 566 328 HOH HOH A . 
N 7 HOH 167 567 330 HOH HOH A . 
N 7 HOH 168 568 332 HOH HOH A . 
N 7 HOH 169 569 333 HOH HOH A . 
N 7 HOH 170 570 337 HOH HOH A . 
N 7 HOH 171 571 339 HOH HOH A . 
N 7 HOH 172 572 341 HOH HOH A . 
N 7 HOH 173 573 342 HOH HOH A . 
N 7 HOH 174 574 344 HOH HOH A . 
N 7 HOH 175 575 346 HOH HOH A . 
N 7 HOH 176 576 350 HOH HOH A . 
N 7 HOH 177 577 352 HOH HOH A . 
N 7 HOH 178 578 355 HOH HOH A . 
N 7 HOH 179 579 356 HOH HOH A . 
N 7 HOH 180 580 357 HOH HOH A . 
N 7 HOH 181 581 358 HOH HOH A . 
N 7 HOH 182 582 359 HOH HOH A . 
N 7 HOH 183 583 360 HOH HOH A . 
N 7 HOH 184 584 361 HOH HOH A . 
N 7 HOH 185 585 362 HOH HOH A . 
N 7 HOH 186 586 363 HOH HOH A . 
N 7 HOH 187 587 364 HOH HOH A . 
N 7 HOH 188 588 368 HOH HOH A . 
N 7 HOH 189 589 370 HOH HOH A . 
N 7 HOH 190 590 372 HOH HOH A . 
N 7 HOH 191 591 373 HOH HOH A . 
N 7 HOH 192 592 374 HOH HOH A . 
N 7 HOH 193 593 376 HOH HOH A . 
N 7 HOH 194 594 377 HOH HOH A . 
N 7 HOH 195 595 379 HOH HOH A . 
N 7 HOH 196 596 381 HOH HOH A . 
N 7 HOH 197 597 382 HOH HOH A . 
N 7 HOH 198 598 383 HOH HOH A . 
N 7 HOH 199 599 384 HOH HOH A . 
N 7 HOH 200 600 387 HOH HOH A . 
N 7 HOH 201 601 388 HOH HOH A . 
N 7 HOH 202 602 389 HOH HOH A . 
N 7 HOH 203 603 391 HOH HOH A . 
N 7 HOH 204 604 393 HOH HOH A . 
N 7 HOH 205 605 394 HOH HOH A . 
N 7 HOH 206 606 395 HOH HOH A . 
N 7 HOH 207 607 400 HOH HOH A . 
N 7 HOH 208 608 402 HOH HOH A . 
N 7 HOH 209 609 403 HOH HOH A . 
N 7 HOH 210 610 404 HOH HOH A . 
N 7 HOH 211 611 405 HOH HOH A . 
N 7 HOH 212 612 407 HOH HOH A . 
N 7 HOH 213 613 408 HOH HOH A . 
N 7 HOH 214 614 409 HOH HOH A . 
N 7 HOH 215 615 410 HOH HOH A . 
N 7 HOH 216 616 412 HOH HOH A . 
N 7 HOH 217 617 414 HOH HOH A . 
N 7 HOH 218 618 415 HOH HOH A . 
N 7 HOH 219 619 416 HOH HOH A . 
N 7 HOH 220 620 418 HOH HOH A . 
N 7 HOH 221 621 420 HOH HOH A . 
N 7 HOH 222 622 421 HOH HOH A . 
N 7 HOH 223 623 422 HOH HOH A . 
N 7 HOH 224 624 423 HOH HOH A . 
N 7 HOH 225 625 426 HOH HOH A . 
N 7 HOH 226 626 429 HOH HOH A . 
N 7 HOH 227 627 430 HOH HOH A . 
N 7 HOH 228 628 438 HOH HOH A . 
N 7 HOH 229 629 439 HOH HOH A . 
N 7 HOH 230 630 440 HOH HOH A . 
N 7 HOH 231 631 441 HOH HOH A . 
N 7 HOH 232 632 442 HOH HOH A . 
N 7 HOH 233 633 443 HOH HOH A . 
N 7 HOH 234 634 444 HOH HOH A . 
N 7 HOH 235 635 445 HOH HOH A . 
N 7 HOH 236 636 446 HOH HOH A . 
N 7 HOH 237 637 447 HOH HOH A . 
N 7 HOH 238 638 458 HOH HOH A . 
N 7 HOH 239 639 463 HOH HOH A . 
N 7 HOH 240 640 464 HOH HOH A . 
N 7 HOH 241 641 475 HOH HOH A . 
N 7 HOH 242 642 476 HOH HOH A . 
N 7 HOH 243 643 479 HOH HOH A . 
N 7 HOH 244 644 480 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,M     
2 1 B,G,H,I,J,K,L,N 
# 
_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 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 NE2 ? A HIS 98  ? B HIS 98  ? 1_555 101.3 ? 
2  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 ND1 ? A HIS 121 ? B HIS 121 ? 1_555 111.2 ? 
3  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 ND1 ? A HIS 121 ? B HIS 121 ? 1_555 99.8  ? 
4  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? E V1F .   ? B V1F 303 ? 1_555 119.8 ? 
5  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? E V1F .   ? B V1F 303 ? 1_555 109.5 ? 
6  ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? E V1F .   ? B V1F 303 ? 1_555 112.6 ? 
7  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O9  ? E V1F .   ? B V1F 303 ? 1_555 84.7  ? 
8  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O9  ? E V1F .   ? B V1F 303 ? 1_555 172.9 ? 
9  ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O9  ? E V1F .   ? B V1F 303 ? 1_555 81.3  ? 
10 N10 ? E V1F .   ? B V1F 303 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O9  ? E V1F .   ? B V1F 303 ? 1_555 63.9  ? 
11 NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? E V1F .   ? B V1F 303 ? 1_555 95.2  ? 
12 NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? E V1F .   ? B V1F 303 ? 1_555 145.4 ? 
13 ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? E V1F .   ? B V1F 303 ? 1_555 102.2 ? 
14 N10 ? E V1F .   ? B V1F 303 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? E V1F .   ? B V1F 303 ? 1_555 36.8  ? 
15 O9  ? E V1F .   ? B V1F 303 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? E V1F .   ? B V1F 303 ? 1_555 28.8  ? 
16 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 101.9 ? 
17 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 114.3 ? 
18 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 98.7  ? 
19 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N10 ? I V1F .   ? A V1F 303 ? 1_555 122.5 ? 
20 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N10 ? I V1F .   ? A V1F 303 ? 1_555 108.0 ? 
21 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N10 ? I V1F .   ? A V1F 303 ? 1_555 108.1 ? 
22 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 S7  ? I V1F .   ? A V1F 303 ? 1_555 95.1  ? 
23 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 S7  ? I V1F .   ? A V1F 303 ? 1_555 144.5 ? 
24 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 S7  ? I V1F .   ? A V1F 303 ? 1_555 102.3 ? 
25 N10 ? I V1F .   ? A V1F 303 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 S7  ? I V1F .   ? A V1F 303 ? 1_555 37.9  ? 
# 
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 2015-04-15 
2 'Structure model' 1 1 2018-05-16 
3 'Structure model' 1 2 2023-11-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Refinement description' 
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Database references'    
5 3 'Structure model' 'Derived calculations'   
6 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  2 'Structure model' diffrn_source                 
2  2 'Structure model' software                      
3  3 'Structure model' chem_comp_atom                
4  3 'Structure model' chem_comp_bond                
5  3 'Structure model' database_2                    
6  3 'Structure model' pdbx_initial_refinement_model 
7  3 'Structure model' pdbx_struct_conn_angle        
8  3 'Structure model' struct_conn                   
9  3 'Structure model' struct_ref_seq_dif            
10 3 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
2  2 'Structure model' '_software.version'                           
3  3 'Structure model' '_database_2.pdbx_DOI'                        
4  3 'Structure model' '_database_2.pdbx_database_accession'         
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_asym_id'  
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_asym_id'  
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_asym_id'  
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
17 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
18 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
19 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
20 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
21 3 'Structure model' '_pdbx_struct_conn_angle.value'               
22 3 'Structure model' '_struct_conn.pdbx_dist_value'                
23 3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
24 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
25 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
26 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
27 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
28 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
29 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
30 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
31 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
32 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
33 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
34 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
35 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
36 3 'Structure model' '_struct_ref_seq_dif.details'                 
37 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
38 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
39 3 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      5.6.0117 ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
SCALA       3.3.20   2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk 'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 2 
PDB_EXTRACT 3.006    'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 3 
HKL-2000    .        ?               ?       ?                    ?                     'data collection' ? ?          ? 4 
XDS         .        ?               ?       ?                    ?                     'data reduction'  ? ?          ? 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 ILE B 24  ? ? -59.85  -8.37   
2  1 SER B 67  ? ? -177.26 -175.02 
3  1 ASP B 73  ? B -37.58  -91.95  
4  1 ASP B 74  ? B 88.15   10.95   
5  1 ASN B 77  ? ? -97.84  35.64   
6  1 ASN B 246 ? ? -153.39 41.53   
7  1 SER A 67  ? ? -175.82 -175.90 
8  1 ASN A 77  ? ? -97.29  49.09   
9  1 HIS A 105 ? ? -163.19 79.55   
10 1 ASN A 246 ? ? -154.46 43.29   
# 
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 2 ? A MET 2 
3  1 Y 1 B SER 3 ? A SER 3 
4  1 Y 1 B ARG 4 ? A ARG 4 
5  1 Y 1 B LEU 5 ? A LEU 5 
6  1 Y 1 A MET 1 ? B MET 1 
7  1 Y 1 A MET 2 ? B MET 2 
8  1 Y 1 A SER 3 ? B SER 3 
9  1 Y 1 A ARG 4 ? B ARG 4 
10 1 Y 1 A LEU 5 ? B LEU 5 
# 
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 
EDO C1   C  N N 109 
EDO O1   O  N N 110 
EDO C2   C  N N 111 
EDO O2   O  N N 112 
EDO H11  H  N N 113 
EDO H12  H  N N 114 
EDO HO1  H  N N 115 
EDO H21  H  N N 116 
EDO H22  H  N N 117 
EDO HO2  H  N N 118 
GLN N    N  N N 119 
GLN CA   C  N S 120 
GLN C    C  N N 121 
GLN O    O  N N 122 
GLN CB   C  N N 123 
GLN CG   C  N N 124 
GLN CD   C  N N 125 
GLN OE1  O  N N 126 
GLN NE2  N  N N 127 
GLN OXT  O  N N 128 
GLN H    H  N N 129 
GLN H2   H  N N 130 
GLN HA   H  N N 131 
GLN HB2  H  N N 132 
GLN HB3  H  N N 133 
GLN HG2  H  N N 134 
GLN HG3  H  N N 135 
GLN HE21 H  N N 136 
GLN HE22 H  N N 137 
GLN HXT  H  N N 138 
GLU N    N  N N 139 
GLU CA   C  N S 140 
GLU C    C  N N 141 
GLU O    O  N N 142 
GLU CB   C  N N 143 
GLU CG   C  N N 144 
GLU CD   C  N N 145 
GLU OE1  O  N N 146 
GLU OE2  O  N N 147 
GLU OXT  O  N N 148 
GLU H    H  N N 149 
GLU H2   H  N N 150 
GLU HA   H  N N 151 
GLU HB2  H  N N 152 
GLU HB3  H  N N 153 
GLU HG2  H  N N 154 
GLU HG3  H  N N 155 
GLU HE2  H  N N 156 
GLU HXT  H  N N 157 
GLY N    N  N N 158 
GLY CA   C  N N 159 
GLY C    C  N N 160 
GLY O    O  N N 161 
GLY OXT  O  N N 162 
GLY H    H  N N 163 
GLY H2   H  N N 164 
GLY HA2  H  N N 165 
GLY HA3  H  N N 166 
GLY HXT  H  N N 167 
HIS N    N  N N 168 
HIS CA   C  N S 169 
HIS C    C  N N 170 
HIS O    O  N N 171 
HIS CB   C  N N 172 
HIS CG   C  Y N 173 
HIS ND1  N  Y N 174 
HIS CD2  C  Y N 175 
HIS CE1  C  Y N 176 
HIS NE2  N  Y N 177 
HIS OXT  O  N N 178 
HIS H    H  N N 179 
HIS H2   H  N N 180 
HIS HA   H  N N 181 
HIS HB2  H  N N 182 
HIS HB3  H  N N 183 
HIS HD1  H  N N 184 
HIS HD2  H  N N 185 
HIS HE1  H  N N 186 
HIS HE2  H  N N 187 
HIS HXT  H  N N 188 
HOH O    O  N N 189 
HOH H1   H  N N 190 
HOH H2   H  N N 191 
ILE N    N  N N 192 
ILE CA   C  N S 193 
ILE C    C  N N 194 
ILE O    O  N N 195 
ILE CB   C  N S 196 
ILE CG1  C  N N 197 
ILE CG2  C  N N 198 
ILE CD1  C  N N 199 
ILE OXT  O  N N 200 
ILE H    H  N N 201 
ILE H2   H  N N 202 
ILE HA   H  N N 203 
ILE HB   H  N N 204 
ILE HG12 H  N N 205 
ILE HG13 H  N N 206 
ILE HG21 H  N N 207 
ILE HG22 H  N N 208 
ILE HG23 H  N N 209 
ILE HD11 H  N N 210 
ILE HD12 H  N N 211 
ILE HD13 H  N N 212 
ILE HXT  H  N N 213 
LEU N    N  N N 214 
LEU CA   C  N S 215 
LEU C    C  N N 216 
LEU O    O  N N 217 
LEU CB   C  N N 218 
LEU CG   C  N N 219 
LEU CD1  C  N N 220 
LEU CD2  C  N N 221 
LEU OXT  O  N N 222 
LEU H    H  N N 223 
LEU H2   H  N N 224 
LEU HA   H  N N 225 
LEU HB2  H  N N 226 
LEU HB3  H  N N 227 
LEU HG   H  N N 228 
LEU HD11 H  N N 229 
LEU HD12 H  N N 230 
LEU HD13 H  N N 231 
LEU HD21 H  N N 232 
LEU HD22 H  N N 233 
LEU HD23 H  N N 234 
LEU HXT  H  N N 235 
LYS N    N  N N 236 
LYS CA   C  N S 237 
LYS C    C  N N 238 
LYS O    O  N N 239 
LYS CB   C  N N 240 
LYS CG   C  N N 241 
LYS CD   C  N N 242 
LYS CE   C  N N 243 
LYS NZ   N  N N 244 
LYS OXT  O  N N 245 
LYS H    H  N N 246 
LYS H2   H  N N 247 
LYS HA   H  N N 248 
LYS HB2  H  N N 249 
LYS HB3  H  N N 250 
LYS HG2  H  N N 251 
LYS HG3  H  N N 252 
LYS HD2  H  N N 253 
LYS HD3  H  N N 254 
LYS HE2  H  N N 255 
LYS HE3  H  N N 256 
LYS HZ1  H  N N 257 
LYS HZ2  H  N N 258 
LYS HZ3  H  N N 259 
LYS HXT  H  N N 260 
MET N    N  N N 261 
MET CA   C  N S 262 
MET C    C  N N 263 
MET O    O  N N 264 
MET CB   C  N N 265 
MET CG   C  N N 266 
MET SD   S  N N 267 
MET CE   C  N N 268 
MET OXT  O  N N 269 
MET H    H  N N 270 
MET H2   H  N N 271 
MET HA   H  N N 272 
MET HB2  H  N N 273 
MET HB3  H  N N 274 
MET HG2  H  N N 275 
MET HG3  H  N N 276 
MET HE1  H  N N 277 
MET HE2  H  N N 278 
MET HE3  H  N N 279 
MET HXT  H  N N 280 
PEG C1   C  N N 281 
PEG O1   O  N N 282 
PEG C2   C  N N 283 
PEG O2   O  N N 284 
PEG C3   C  N N 285 
PEG C4   C  N N 286 
PEG O4   O  N N 287 
PEG H11  H  N N 288 
PEG H12  H  N N 289 
PEG HO1  H  N N 290 
PEG H21  H  N N 291 
PEG H22  H  N N 292 
PEG H31  H  N N 293 
PEG H32  H  N N 294 
PEG H41  H  N N 295 
PEG H42  H  N N 296 
PEG HO4  H  N N 297 
PHE N    N  N N 298 
PHE CA   C  N S 299 
PHE C    C  N N 300 
PHE O    O  N N 301 
PHE CB   C  N N 302 
PHE CG   C  Y N 303 
PHE CD1  C  Y N 304 
PHE CD2  C  Y N 305 
PHE CE1  C  Y N 306 
PHE CE2  C  Y N 307 
PHE CZ   C  Y N 308 
PHE OXT  O  N N 309 
PHE H    H  N N 310 
PHE H2   H  N N 311 
PHE HA   H  N N 312 
PHE HB2  H  N N 313 
PHE HB3  H  N N 314 
PHE HD1  H  N N 315 
PHE HD2  H  N N 316 
PHE HE1  H  N N 317 
PHE HE2  H  N N 318 
PHE HZ   H  N N 319 
PHE HXT  H  N N 320 
PRO N    N  N N 321 
PRO CA   C  N S 322 
PRO C    C  N N 323 
PRO O    O  N N 324 
PRO CB   C  N N 325 
PRO CG   C  N N 326 
PRO CD   C  N N 327 
PRO OXT  O  N N 328 
PRO H    H  N N 329 
PRO HA   H  N N 330 
PRO HB2  H  N N 331 
PRO HB3  H  N N 332 
PRO HG2  H  N N 333 
PRO HG3  H  N N 334 
PRO HD2  H  N N 335 
PRO HD3  H  N N 336 
PRO HXT  H  N N 337 
SER N    N  N N 338 
SER CA   C  N S 339 
SER C    C  N N 340 
SER O    O  N N 341 
SER CB   C  N N 342 
SER OG   O  N N 343 
SER OXT  O  N N 344 
SER H    H  N N 345 
SER H2   H  N N 346 
SER HA   H  N N 347 
SER HB2  H  N N 348 
SER HB3  H  N N 349 
SER HG   H  N N 350 
SER HXT  H  N N 351 
THR N    N  N N 352 
THR CA   C  N S 353 
THR C    C  N N 354 
THR O    O  N N 355 
THR CB   C  N R 356 
THR OG1  O  N N 357 
THR CG2  C  N N 358 
THR OXT  O  N N 359 
THR H    H  N N 360 
THR H2   H  N N 361 
THR HA   H  N N 362 
THR HB   H  N N 363 
THR HG1  H  N N 364 
THR HG21 H  N N 365 
THR HG22 H  N N 366 
THR HG23 H  N N 367 
THR HXT  H  N N 368 
TRP N    N  N N 369 
TRP CA   C  N S 370 
TRP C    C  N N 371 
TRP O    O  N N 372 
TRP CB   C  N N 373 
TRP CG   C  Y N 374 
TRP CD1  C  Y N 375 
TRP CD2  C  Y N 376 
TRP NE1  N  Y N 377 
TRP CE2  C  Y N 378 
TRP CE3  C  Y N 379 
TRP CZ2  C  Y N 380 
TRP CZ3  C  Y N 381 
TRP CH2  C  Y N 382 
TRP OXT  O  N N 383 
TRP H    H  N N 384 
TRP H2   H  N N 385 
TRP HA   H  N N 386 
TRP HB2  H  N N 387 
TRP HB3  H  N N 388 
TRP HD1  H  N N 389 
TRP HE1  H  N N 390 
TRP HE3  H  N N 391 
TRP HZ2  H  N N 392 
TRP HZ3  H  N N 393 
TRP HH2  H  N N 394 
TRP HXT  H  N N 395 
TYR N    N  N N 396 
TYR CA   C  N S 397 
TYR C    C  N N 398 
TYR O    O  N N 399 
TYR CB   C  N N 400 
TYR CG   C  Y N 401 
TYR CD1  C  Y N 402 
TYR CD2  C  Y N 403 
TYR CE1  C  Y N 404 
TYR CE2  C  Y N 405 
TYR CZ   C  Y N 406 
TYR OH   O  N N 407 
TYR OXT  O  N N 408 
TYR H    H  N N 409 
TYR H2   H  N N 410 
TYR HA   H  N N 411 
TYR HB2  H  N N 412 
TYR HB3  H  N N 413 
TYR HD1  H  N N 414 
TYR HD2  H  N N 415 
TYR HE1  H  N N 416 
TYR HE2  H  N N 417 
TYR HH   H  N N 418 
TYR HXT  H  N N 419 
V1F F26  F  N N 420 
V1F C5   C  Y N 421 
V1F C4   C  Y N 422 
V1F S7   S  N N 423 
V1F O9   O  N N 424 
V1F N10  N  N N 425 
V1F O8   O  N N 426 
V1F C3   C  Y N 427 
V1F F12  F  N N 428 
V1F C2   C  Y N 429 
V1F F13  F  N N 430 
V1F C6   C  Y N 431 
V1F C1   C  Y N 432 
V1F S11  S  N N 433 
V1F O22  O  N N 434 
V1F O23  O  N N 435 
V1F C21  C  N N 436 
V1F C24  C  N N 437 
V1F C30  C  Y N 438 
V1F C29  C  Y N 439 
V1F C28  C  Y N 440 
V1F C32  C  Y N 441 
V1F C31  C  Y N 442 
V1F C27  C  Y N 443 
V1F N25  N  N N 444 
V1F C14  C  N N 445 
V1F C15  C  Y N 446 
V1F C20  C  Y N 447 
V1F C19  C  Y N 448 
V1F C18  C  Y N 449 
V1F C17  C  Y N 450 
V1F C16  C  Y N 451 
V1F H1   H  N N 452 
V1F H2   H  N N 453 
V1F H3   H  N N 454 
V1F H4   H  N N 455 
V1F H5   H  N N 456 
V1F H6   H  N N 457 
V1F H7   H  N N 458 
V1F H8   H  N N 459 
V1F H9   H  N N 460 
V1F H10  H  N N 461 
V1F H11  H  N N 462 
V1F H12  H  N N 463 
V1F H13  H  N N 464 
V1F H14  H  N N 465 
V1F H15  H  N N 466 
V1F H16  H  N N 467 
V1F H17  H  N N 468 
V1F H18  H  N N 469 
V1F H19  H  N N 470 
VAL N    N  N N 471 
VAL CA   C  N S 472 
VAL C    C  N N 473 
VAL O    O  N N 474 
VAL CB   C  N N 475 
VAL CG1  C  N N 476 
VAL CG2  C  N N 477 
VAL OXT  O  N N 478 
VAL H    H  N N 479 
VAL H2   H  N N 480 
VAL HA   H  N N 481 
VAL HB   H  N N 482 
VAL HG11 H  N N 483 
VAL HG12 H  N N 484 
VAL HG13 H  N N 485 
VAL HG21 H  N N 486 
VAL HG22 H  N N 487 
VAL HG23 H  N N 488 
VAL HXT  H  N N 489 
ZN  ZN   ZN N N 490 
# 
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 
EDO C1  O1   sing N N 103 
EDO C1  C2   sing N N 104 
EDO C1  H11  sing N N 105 
EDO C1  H12  sing N N 106 
EDO O1  HO1  sing N N 107 
EDO C2  O2   sing N N 108 
EDO C2  H21  sing N N 109 
EDO C2  H22  sing N N 110 
EDO O2  HO2  sing N N 111 
GLN N   CA   sing N N 112 
GLN N   H    sing N N 113 
GLN N   H2   sing N N 114 
GLN CA  C    sing N N 115 
GLN CA  CB   sing N N 116 
GLN CA  HA   sing N N 117 
GLN C   O    doub N N 118 
GLN C   OXT  sing N N 119 
GLN CB  CG   sing N N 120 
GLN CB  HB2  sing N N 121 
GLN CB  HB3  sing N N 122 
GLN CG  CD   sing N N 123 
GLN CG  HG2  sing N N 124 
GLN CG  HG3  sing N N 125 
GLN CD  OE1  doub N N 126 
GLN CD  NE2  sing N N 127 
GLN NE2 HE21 sing N N 128 
GLN NE2 HE22 sing N N 129 
GLN OXT HXT  sing N N 130 
GLU N   CA   sing N N 131 
GLU N   H    sing N N 132 
GLU N   H2   sing N N 133 
GLU CA  C    sing N N 134 
GLU CA  CB   sing N N 135 
GLU CA  HA   sing N N 136 
GLU C   O    doub N N 137 
GLU C   OXT  sing N N 138 
GLU CB  CG   sing N N 139 
GLU CB  HB2  sing N N 140 
GLU CB  HB3  sing N N 141 
GLU CG  CD   sing N N 142 
GLU CG  HG2  sing N N 143 
GLU CG  HG3  sing N N 144 
GLU CD  OE1  doub N N 145 
GLU CD  OE2  sing N N 146 
GLU OE2 HE2  sing N N 147 
GLU OXT HXT  sing N N 148 
GLY N   CA   sing N N 149 
GLY N   H    sing N N 150 
GLY N   H2   sing N N 151 
GLY CA  C    sing N N 152 
GLY CA  HA2  sing N N 153 
GLY CA  HA3  sing N N 154 
GLY C   O    doub N N 155 
GLY C   OXT  sing N N 156 
GLY OXT HXT  sing N N 157 
HIS N   CA   sing N N 158 
HIS N   H    sing N N 159 
HIS N   H2   sing N N 160 
HIS CA  C    sing N N 161 
HIS CA  CB   sing N N 162 
HIS CA  HA   sing N N 163 
HIS C   O    doub N N 164 
HIS C   OXT  sing N N 165 
HIS CB  CG   sing N N 166 
HIS CB  HB2  sing N N 167 
HIS CB  HB3  sing N N 168 
HIS CG  ND1  sing Y N 169 
HIS CG  CD2  doub Y N 170 
HIS ND1 CE1  doub Y N 171 
HIS ND1 HD1  sing N N 172 
HIS CD2 NE2  sing Y N 173 
HIS CD2 HD2  sing N N 174 
HIS CE1 NE2  sing Y N 175 
HIS CE1 HE1  sing N N 176 
HIS NE2 HE2  sing N N 177 
HIS OXT HXT  sing N N 178 
HOH O   H1   sing N N 179 
HOH O   H2   sing N N 180 
ILE N   CA   sing N N 181 
ILE N   H    sing N N 182 
ILE N   H2   sing N N 183 
ILE CA  C    sing N N 184 
ILE CA  CB   sing N N 185 
ILE CA  HA   sing N N 186 
ILE C   O    doub N N 187 
ILE C   OXT  sing N N 188 
ILE CB  CG1  sing N N 189 
ILE CB  CG2  sing N N 190 
ILE CB  HB   sing N N 191 
ILE CG1 CD1  sing N N 192 
ILE CG1 HG12 sing N N 193 
ILE CG1 HG13 sing N N 194 
ILE CG2 HG21 sing N N 195 
ILE CG2 HG22 sing N N 196 
ILE CG2 HG23 sing N N 197 
ILE CD1 HD11 sing N N 198 
ILE CD1 HD12 sing N N 199 
ILE CD1 HD13 sing N N 200 
ILE OXT HXT  sing N N 201 
LEU N   CA   sing N N 202 
LEU N   H    sing N N 203 
LEU N   H2   sing N N 204 
LEU CA  C    sing N N 205 
LEU CA  CB   sing N N 206 
LEU CA  HA   sing N N 207 
LEU C   O    doub N N 208 
LEU C   OXT  sing N N 209 
LEU CB  CG   sing N N 210 
LEU CB  HB2  sing N N 211 
LEU CB  HB3  sing N N 212 
LEU CG  CD1  sing N N 213 
LEU CG  CD2  sing N N 214 
LEU CG  HG   sing N N 215 
LEU CD1 HD11 sing N N 216 
LEU CD1 HD12 sing N N 217 
LEU CD1 HD13 sing N N 218 
LEU CD2 HD21 sing N N 219 
LEU CD2 HD22 sing N N 220 
LEU CD2 HD23 sing N N 221 
LEU OXT HXT  sing N N 222 
LYS N   CA   sing N N 223 
LYS N   H    sing N N 224 
LYS N   H2   sing N N 225 
LYS CA  C    sing N N 226 
LYS CA  CB   sing N N 227 
LYS CA  HA   sing N N 228 
LYS C   O    doub N N 229 
LYS C   OXT  sing N N 230 
LYS CB  CG   sing N N 231 
LYS CB  HB2  sing N N 232 
LYS CB  HB3  sing N N 233 
LYS CG  CD   sing N N 234 
LYS CG  HG2  sing N N 235 
LYS CG  HG3  sing N N 236 
LYS CD  CE   sing N N 237 
LYS CD  HD2  sing N N 238 
LYS CD  HD3  sing N N 239 
LYS CE  NZ   sing N N 240 
LYS CE  HE2  sing N N 241 
LYS CE  HE3  sing N N 242 
LYS NZ  HZ1  sing N N 243 
LYS NZ  HZ2  sing N N 244 
LYS NZ  HZ3  sing N N 245 
LYS OXT HXT  sing N N 246 
MET N   CA   sing N N 247 
MET N   H    sing N N 248 
MET N   H2   sing N N 249 
MET CA  C    sing N N 250 
MET CA  CB   sing N N 251 
MET CA  HA   sing N N 252 
MET C   O    doub N N 253 
MET C   OXT  sing N N 254 
MET CB  CG   sing N N 255 
MET CB  HB2  sing N N 256 
MET CB  HB3  sing N N 257 
MET CG  SD   sing N N 258 
MET CG  HG2  sing N N 259 
MET CG  HG3  sing N N 260 
MET SD  CE   sing N N 261 
MET CE  HE1  sing N N 262 
MET CE  HE2  sing N N 263 
MET CE  HE3  sing N N 264 
MET OXT HXT  sing N N 265 
PEG C1  O1   sing N N 266 
PEG C1  C2   sing N N 267 
PEG C1  H11  sing N N 268 
PEG C1  H12  sing N N 269 
PEG O1  HO1  sing N N 270 
PEG C2  O2   sing N N 271 
PEG C2  H21  sing N N 272 
PEG C2  H22  sing N N 273 
PEG O2  C3   sing N N 274 
PEG C3  C4   sing N N 275 
PEG C3  H31  sing N N 276 
PEG C3  H32  sing N N 277 
PEG C4  O4   sing N N 278 
PEG C4  H41  sing N N 279 
PEG C4  H42  sing N N 280 
PEG O4  HO4  sing N N 281 
PHE N   CA   sing N N 282 
PHE N   H    sing N N 283 
PHE N   H2   sing N N 284 
PHE CA  C    sing N N 285 
PHE CA  CB   sing N N 286 
PHE CA  HA   sing N N 287 
PHE C   O    doub N N 288 
PHE C   OXT  sing N N 289 
PHE CB  CG   sing N N 290 
PHE CB  HB2  sing N N 291 
PHE CB  HB3  sing N N 292 
PHE CG  CD1  doub Y N 293 
PHE CG  CD2  sing Y N 294 
PHE CD1 CE1  sing Y N 295 
PHE CD1 HD1  sing N N 296 
PHE CD2 CE2  doub Y N 297 
PHE CD2 HD2  sing N N 298 
PHE CE1 CZ   doub Y N 299 
PHE CE1 HE1  sing N N 300 
PHE CE2 CZ   sing Y N 301 
PHE CE2 HE2  sing N N 302 
PHE CZ  HZ   sing N N 303 
PHE OXT HXT  sing N N 304 
PRO N   CA   sing N N 305 
PRO N   CD   sing N N 306 
PRO N   H    sing N N 307 
PRO CA  C    sing N N 308 
PRO CA  CB   sing N N 309 
PRO CA  HA   sing N N 310 
PRO C   O    doub N N 311 
PRO C   OXT  sing N N 312 
PRO CB  CG   sing N N 313 
PRO CB  HB2  sing N N 314 
PRO CB  HB3  sing N N 315 
PRO CG  CD   sing N N 316 
PRO CG  HG2  sing N N 317 
PRO CG  HG3  sing N N 318 
PRO CD  HD2  sing N N 319 
PRO CD  HD3  sing N N 320 
PRO OXT HXT  sing N N 321 
SER N   CA   sing N N 322 
SER N   H    sing N N 323 
SER N   H2   sing N N 324 
SER CA  C    sing N N 325 
SER CA  CB   sing N N 326 
SER CA  HA   sing N N 327 
SER C   O    doub N N 328 
SER C   OXT  sing N N 329 
SER CB  OG   sing N N 330 
SER CB  HB2  sing N N 331 
SER CB  HB3  sing N N 332 
SER OG  HG   sing N N 333 
SER OXT HXT  sing N N 334 
THR N   CA   sing N N 335 
THR N   H    sing N N 336 
THR N   H2   sing N N 337 
THR CA  C    sing N N 338 
THR CA  CB   sing N N 339 
THR CA  HA   sing N N 340 
THR C   O    doub N N 341 
THR C   OXT  sing N N 342 
THR CB  OG1  sing N N 343 
THR CB  CG2  sing N N 344 
THR CB  HB   sing N N 345 
THR OG1 HG1  sing N N 346 
THR CG2 HG21 sing N N 347 
THR CG2 HG22 sing N N 348 
THR CG2 HG23 sing N N 349 
THR OXT HXT  sing N N 350 
TRP N   CA   sing N N 351 
TRP N   H    sing N N 352 
TRP N   H2   sing N N 353 
TRP CA  C    sing N N 354 
TRP CA  CB   sing N N 355 
TRP CA  HA   sing N N 356 
TRP C   O    doub N N 357 
TRP C   OXT  sing N N 358 
TRP CB  CG   sing N N 359 
TRP CB  HB2  sing N N 360 
TRP CB  HB3  sing N N 361 
TRP CG  CD1  doub Y N 362 
TRP CG  CD2  sing Y N 363 
TRP CD1 NE1  sing Y N 364 
TRP CD1 HD1  sing N N 365 
TRP CD2 CE2  doub Y N 366 
TRP CD2 CE3  sing Y N 367 
TRP NE1 CE2  sing Y N 368 
TRP NE1 HE1  sing N N 369 
TRP CE2 CZ2  sing Y N 370 
TRP CE3 CZ3  doub Y N 371 
TRP CE3 HE3  sing N N 372 
TRP CZ2 CH2  doub Y N 373 
TRP CZ2 HZ2  sing N N 374 
TRP CZ3 CH2  sing Y N 375 
TRP CZ3 HZ3  sing N N 376 
TRP CH2 HH2  sing N N 377 
TRP OXT HXT  sing N N 378 
TYR N   CA   sing N N 379 
TYR N   H    sing N N 380 
TYR N   H2   sing N N 381 
TYR CA  C    sing N N 382 
TYR CA  CB   sing N N 383 
TYR CA  HA   sing N N 384 
TYR C   O    doub N N 385 
TYR C   OXT  sing N N 386 
TYR CB  CG   sing N N 387 
TYR CB  HB2  sing N N 388 
TYR CB  HB3  sing N N 389 
TYR CG  CD1  doub Y N 390 
TYR CG  CD2  sing Y N 391 
TYR CD1 CE1  sing Y N 392 
TYR CD1 HD1  sing N N 393 
TYR CD2 CE2  doub Y N 394 
TYR CD2 HD2  sing N N 395 
TYR CE1 CZ   doub Y N 396 
TYR CE1 HE1  sing N N 397 
TYR CE2 CZ   sing Y N 398 
TYR CE2 HE2  sing N N 399 
TYR CZ  OH   sing N N 400 
TYR OH  HH   sing N N 401 
TYR OXT HXT  sing N N 402 
V1F C17 C18  doub Y N 403 
V1F C17 C16  sing Y N 404 
V1F C18 C19  sing Y N 405 
V1F C16 C15  doub Y N 406 
V1F C31 C32  doub Y N 407 
V1F C31 C27  sing Y N 408 
V1F C32 C30  sing Y N 409 
V1F C19 C20  doub Y N 410 
V1F C27 C28  doub Y N 411 
V1F C30 C24  sing N N 412 
V1F C30 C29  doub Y N 413 
V1F C24 C21  sing N N 414 
V1F C15 C20  sing Y N 415 
V1F C15 C14  sing N N 416 
V1F C28 C29  sing Y N 417 
V1F C14 N25  sing N N 418 
V1F C21 S11  sing N N 419 
V1F O23 S11  doub N N 420 
V1F N25 C6   sing N N 421 
V1F S11 C1   sing N N 422 
V1F S11 O22  doub N N 423 
V1F C6  C1   doub Y N 424 
V1F C6  C5   sing Y N 425 
V1F C1  C2   sing Y N 426 
V1F F26 C5   sing N N 427 
V1F C5  C4   doub Y N 428 
V1F C2  F13  sing N N 429 
V1F C2  C3   doub Y N 430 
V1F C4  C3   sing Y N 431 
V1F C4  S7   sing N N 432 
V1F C3  F12  sing N N 433 
V1F N10 S7   sing N N 434 
V1F O9  S7   doub N N 435 
V1F S7  O8   doub N N 436 
V1F N10 H1   sing N N 437 
V1F N10 H2   sing N N 438 
V1F C21 H3   sing N N 439 
V1F C21 H4   sing N N 440 
V1F C24 H5   sing N N 441 
V1F C24 H6   sing N N 442 
V1F C29 H7   sing N N 443 
V1F C28 H8   sing N N 444 
V1F C32 H9   sing N N 445 
V1F C31 H10  sing N N 446 
V1F C27 H11  sing N N 447 
V1F N25 H12  sing N N 448 
V1F C14 H13  sing N N 449 
V1F C14 H14  sing N N 450 
V1F C20 H15  sing N N 451 
V1F C19 H16  sing N N 452 
V1F C18 H17  sing N N 453 
V1F C17 H18  sing N N 454 
V1F C16 H19  sing N N 455 
VAL N   CA   sing N N 456 
VAL N   H    sing N N 457 
VAL N   H2   sing N N 458 
VAL CA  C    sing N N 459 
VAL CA  CB   sing N N 460 
VAL CA  HA   sing N N 461 
VAL C   O    doub N N 462 
VAL C   OXT  sing N N 463 
VAL CB  CG1  sing N N 464 
VAL CB  CG2  sing N N 465 
VAL CB  HB   sing N N 466 
VAL CG1 HG11 sing N N 467 
VAL CG1 HG12 sing N N 468 
VAL CG1 HG13 sing N N 469 
VAL CG2 HG21 sing N N 470 
VAL CG2 HG22 sing N N 471 
VAL CG2 HG23 sing N N 472 
VAL OXT HXT  sing N N 473 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                      ZN  
3 'DI(HYDROXYETHYL)ETHER'                                                         PEG 
4 '3-(benzylamino)-2,5,6-trifluoro-4-[(2-phenylethyl)sulfonyl]benzenesulfonamide' V1F 
5 1,2-ETHANEDIOL                                                                  EDO 
6 'CITRIC ACID'                                                                   CIT 
7 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          ? 
# 
