data_4QIZ
# 
_entry.id   4QIZ 
# 
_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   4QIZ         pdb_00004qiz 10.2210/pdb4qiz/pdb 
RCSB  RCSB086114   ?            ?                   
WWPDB D_1000086114 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4QIY . unspecified 
PDB 4QJ0 . unspecified 
PDB 4QJM . unspecified 
PDB 4QJO . unspecified 
PDB 4QJP . unspecified 
PDB 4QJW . unspecified 
PDB 4QJX . unspecified 
PDB 4QTL . unspecified 
# 
_pdbx_database_status.entry_id                        4QIZ 
_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   2014-06-03 
_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           4QIZ 
_cell.length_a           56.576 
_cell.length_b           159.618 
_cell.length_c           57.100 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4QIZ 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 13'                                                                                         
29613.318 2   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                                                      
65.409    2   ?       ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                                                                  
62.068    3   ?       ? ? ? 
4 non-polymer syn '2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 
530.537   2   ?       ? ? ? 
5 water       nat water                                                                                                           
18.015    484 ?       ? ? ? 
# 
_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                 A,B 
_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 4QIZ A 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
2 1 4QIZ B 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 4QIZ MET A 1 ? UNP Q8N1Q1 ? ? 'expression tag' 1 1 
2 4QIZ MET B 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 
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 
PHE 'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE ?                 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE ?                 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE ?                 'C5 H11 N O2'         117.146 
WWX non-polymer         . 
'2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ?                 
'C22 H21 F3 N2 O6 S2' 530.537 
ZN  non-polymer         . 'ZINC ION' ?                 'Zn 2'                65.409  
# 
_exptl.entry_id          4QIZ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.18 
_exptl_crystal.density_percent_sol   43.49 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '0.1M ammonium citrate (pH 5.0), 20% PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2012-12-02 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    
'High Heat Load (HHL) Monochromator: Si 111; Large Offset Monochromator (LOM): Si 311, Si 511' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_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_synchrotron_site       'PETRA III, EMBL c/o DESY' 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4QIZ 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             57.100 
_reflns.d_resolution_high            1.550 
_reflns.number_obs                   75960 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.900 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.037 
_reflns.pdbx_netI_over_sigmaI        27.200 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              6.600 
_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_CC_half                 ? 
_reflns.pdbx_Rpim_I_all              ? 
_reflns.pdbx_Rrim_I_all              ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_Rrim_I_all 
1 1  1.55 1.63  100.00 0.405 0.405 1.9  6.40 ? ? ? ? ? ? ? ? ? 
1 2  1.63 1.73  100.00 0.294 0.294 2.7  6.80 ? ? ? ? ? ? ? ? ? 
1 3  1.73 1.85  99.90  0.184 0.184 4.2  6.70 ? ? ? ? ? ? ? ? ? 
1 4  1.85 2.00  99.90  0.101 0.101 7.7  6.40 ? ? ? ? ? ? ? ? ? 
1 5  2.00 2.19  100.00 0.067 0.067 11.5 6.80 ? ? ? ? ? ? ? ? ? 
1 6  2.19 2.45  100.00 0.046 0.046 16.4 6.60 ? ? ? ? ? ? ? ? ? 
1 7  2.45 2.83  100.00 0.031 0.031 23.8 6.70 ? ? ? ? ? ? ? ? ? 
1 8  2.83 3.47  100.00 0.021 0.021 33.0 6.70 ? ? ? ? ? ? ? ? ? 
1 9  3.47 4.90  99.90  0.013 0.013 50.4 6.50 ? ? ? ? ? ? ? ? ? 
1 10 4.90 57.10 99.70  0.012 0.012 13.2 6.10 ? ? ? ? ? ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4QIZ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     68338 
_refine.ls_number_reflns_all                     75875 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             46.16 
_refine.ls_d_res_high                            1.55 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_R_factor_obs                          0.17851 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.17512 
_refine.ls_R_factor_R_free                       0.20936 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.9 
_refine.ls_number_reflns_R_free                  7537 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            0.50 
_refine.occupancy_max                            1.00 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_refine.B_iso_mean                               19.490 
_refine.aniso_B[1][1]                            1.40 
_refine.aniso_B[2][2]                            -1.14 
_refine.aniso_B[3][3]                            -0.26 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.pdbx_starting_model                      2NNO 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.089 
_refine.pdbx_overall_ESU_R_Free                  0.090 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.089 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4108 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.number_atoms_solvent             484 
_refine_hist.number_atoms_total               4676 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        46.16 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.025  0.020  ? 4530 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.332  1.959  ? 6203 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.947  5.000  ? 559  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       32.377 24.258 ? 209  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.315 15.000 ? 717  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       17.109 15.000 ? 20   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.180  0.200  ? 646  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.016  0.021  ? 3570 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.550 
_refine_ls_shell.d_res_low                        1.590 
_refine_ls_shell.number_reflns_R_work             4985 
_refine_ls_shell.R_factor_R_work                  0.230 
_refine_ls_shell.percent_reflns_obs               99.98 
_refine_ls_shell.R_factor_R_free                  0.280 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             541 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  4QIZ 
_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        4QIZ 
_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 3 ? 
F N N 4 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 5 ? 
# 
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 A 14  PHE A 21  5 ? 8  
HELX_P HELX_P2  2  PHE A 22  ? GLY A 27  ? PHE A 22  GLY A 27  5 ? 6  
HELX_P HELX_P3  3  SER A 132 ? ALA A 137 ? SER A 132 ALA A 137 1 ? 6  
HELX_P HELX_P4  4  ASN A 156 ? ASP A 164 ? ASN A 156 ASP A 164 1 ? 9  
HELX_P HELX_P5  5  THR A 165 ? LYS A 170 ? THR A 165 LYS A 170 5 ? 6  
HELX_P HELX_P6  6  ASP A 182 ? LEU A 187 ? ASP A 182 LEU A 187 5 ? 6  
HELX_P HELX_P7  7  SER A 221 ? ARG A 229 ? SER A 221 ARG A 229 1 ? 9  
HELX_P HELX_P8  8  GLY B 14  ? PHE B 21  ? GLY B 14  PHE B 21  5 ? 8  
HELX_P HELX_P9  9  PHE B 22  ? GLY B 27  ? PHE B 22  GLY B 27  5 ? 6  
HELX_P HELX_P10 10 LYS B 36  ? VAL B 40  ? LYS B 36  VAL B 40  5 ? 5  
HELX_P HELX_P11 11 SER B 132 ? ALA B 137 ? SER B 132 ALA B 137 1 ? 6  
HELX_P HELX_P12 12 ASN B 156 ? LEU B 166 ? ASN B 156 LEU B 166 1 ? 11 
HELX_P HELX_P13 13 ASP B 182 ? LEU B 187 ? ASP B 182 LEU B 187 5 ? 6  
HELX_P HELX_P14 14 SER B 221 ? ARG B 229 ? SER B 221 ARG B 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 ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 1.971 ? ? 
metalc2 metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 98  A ZN  301 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc3 metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN  . ZN ? ? A HIS 121 A ZN  301 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc4 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 F WWX . N4 ? ? A ZN  301 A WWX 304 1_555 ? ? ? ? ? ? ? 1.892 ? ? 
metalc5 metalc ? ? B HIS 96  NE2 ? ? ? 1_555 G ZN  . ZN ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
metalc6 metalc ? ? B HIS 98  NE2 ? ? ? 1_555 G ZN  . ZN ? ? B HIS 98  B ZN  301 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc7 metalc ? ? B HIS 121 ND1 ? ? ? 1_555 G ZN  . ZN ? ? B HIS 121 B ZN  301 1_555 ? ? ? ? ? ? ? 2.076 ? ? 
metalc8 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 I WWX . N4 ? ? B ZN  301 B WWX 303 1_555 ? ? ? ? ? ? ? 1.926 ? ? 
# 
_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  A PRO 32  A ? PRO 32  A 1 1.22  
2 PRO 203 A . ? PRO 203 A PRO 204 A ? PRO 204 A 1 13.73 
3 SER 31  B . ? SER 31  B PRO 32  B ? PRO 32  B 1 3.55  
4 PRO 203 B . ? PRO 203 B PRO 204 B ? PRO 204 B 1 12.83 
# 
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 A 34  ILE A 35  
A 2  ILE A 110 ? VAL A 111 ? ILE A 110 VAL A 111 
B 1  LYS A 41  ? TYR A 42  ? LYS A 41  TYR A 42  
B 2  ARG A 259 ? ALA A 260 ? ARG A 259 ALA A 260 
B 3  TYR A 193 ? GLY A 198 ? TYR A 193 GLY A 198 
B 4  VAL A 209 ? LEU A 214 ? VAL A 209 LEU A 214 
B 5  LEU A 143 ? ILE A 152 ? LEU A 143 ILE A 152 
B 6  ALA A 118 ? ASN A 126 ? ALA A 118 ASN A 126 
B 7  TYR A 90  ? TRP A 99  ? TYR A 90  TRP A 99  
B 8  PHE A 68  ? PHE A 72  ? PHE A 68  PHE A 72  
B 9  ALA A 58  ? ASN A 63  ? ALA A 58  ASN A 63  
B 10 GLN A 175 ? ARG A 177 ? GLN A 175 ARG A 177 
C 1  LEU A 49  ? LYS A 52  ? LEU A 49  LYS A 52  
C 2  VAL A 80  ? GLY A 83  ? VAL A 80  GLY A 83  
C 3  TYR A 90  ? TRP A 99  ? TYR A 90  TRP A 99  
C 4  ALA A 118 ? ASN A 126 ? ALA A 118 ASN A 126 
C 5  LEU A 143 ? ILE A 152 ? LEU A 143 ILE A 152 
C 6  ILE A 218 ? ILE A 220 ? ILE A 218 ILE A 220 
D 1  GLU B 34  ? ILE B 35  ? GLU B 34  ILE B 35  
D 2  ILE B 110 ? VAL B 111 ? ILE B 110 VAL B 111 
E 1  LYS B 41  ? TYR B 42  ? LYS B 41  TYR B 42  
E 2  ARG B 259 ? ALA B 260 ? ARG B 259 ALA B 260 
E 3  TYR B 193 ? GLY B 198 ? TYR B 193 GLY B 198 
E 4  VAL B 209 ? LEU B 214 ? VAL B 209 LEU B 214 
E 5  LEU B 143 ? ILE B 152 ? LEU B 143 ILE B 152 
E 6  ALA B 118 ? ASN B 126 ? ALA B 118 ASN B 126 
E 7  TYR B 90  ? TRP B 99  ? TYR B 90  TRP B 99  
E 8  PHE B 68  ? PHE B 72  ? PHE B 68  PHE B 72  
E 9  ALA B 58  ? ASN B 63  ? ALA B 58  ASN B 63  
E 10 GLN B 175 ? ARG B 177 ? GLN B 175 ARG B 177 
F 1  LEU B 49  ? LYS B 52  ? LEU B 49  LYS B 52  
F 2  VAL B 80  ? GLY B 83  ? VAL B 80  GLY B 83  
F 3  TYR B 90  ? TRP B 99  ? TYR B 90  TRP B 99  
F 4  ALA B 118 ? ASN B 126 ? ALA B 118 ASN B 126 
F 5  LEU B 143 ? ILE B 152 ? LEU B 143 ILE B 152 
F 6  ILE B 218 ? ILE B 220 ? ILE B 218 ILE B 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 A 35  O ILE A 110 ? O ILE A 110 
B 1 2  N LYS A 41  ? N LYS A 41  O ALA A 260 ? O ALA A 260 
B 2 3  O ARG A 259 ? O ARG A 259 N THR A 195 ? N THR A 195 
B 3 4  N GLY A 198 ? N GLY A 198 O VAL A 209 ? O VAL A 209 
B 4 5  O LEU A 214 ? O LEU A 214 N GLY A 147 ? N GLY A 147 
B 5 6  O VAL A 148 ? O VAL A 148 N LEU A 120 ? N LEU A 120 
B 6 7  O VAL A 123 ? O VAL A 123 N GLN A 94  ? N GLN A 94  
B 7 8  O VAL A 95  ? O VAL A 95  N VAL A 70  ? N VAL A 70  
B 8 9  O ASP A 71  ? O ASP A 71  N LYS A 59  ? N LYS A 59  
B 9 10 N ILE A 61  ? N ILE A 61  O THR A 176 ? O THR A 176 
C 1 2  N SER A 50  ? N SER A 50  O ARG A 82  ? O ARG A 82  
C 2 3  N LEU A 81  ? N LEU A 81  O TYR A 90  ? O TYR A 90  
C 3 4  N GLN A 94  ? N GLN A 94  O VAL A 123 ? O VAL A 123 
C 4 5  N LEU A 120 ? N LEU A 120 O VAL A 148 ? O VAL A 148 
C 5 6  N GLN A 151 ? N GLN A 151 O ILE A 218 ? O ILE A 218 
D 1 2  N ILE B 35  ? N ILE B 35  O ILE B 110 ? O ILE B 110 
E 1 2  N LYS B 41  ? N LYS B 41  O ALA B 260 ? O ALA B 260 
E 2 3  O ARG B 259 ? O ARG B 259 N THR B 195 ? N THR B 195 
E 3 4  N GLY B 198 ? N GLY B 198 O VAL B 209 ? O VAL B 209 
E 4 5  O ILE B 212 ? O ILE B 212 N VAL B 145 ? N VAL B 145 
E 5 6  O ALA B 144 ? O ALA B 144 N HIS B 124 ? N HIS B 124 
E 6 7  O TRP B 125 ? O TRP B 125 N ARG B 91  ? N ARG B 91  
E 7 8  O VAL B 95  ? O VAL B 95  N VAL B 70  ? N VAL B 70  
E 8 9  O ASP B 71  ? O ASP B 71  N LYS B 59  ? N LYS B 59  
E 9 10 N ILE B 61  ? N ILE B 61  O THR B 176 ? O THR B 176 
F 1 2  N SER B 50  ? N SER B 50  O ARG B 82  ? O ARG B 82  
F 2 3  N LEU B 81  ? N LEU B 81  O TYR B 90  ? O TYR B 90  
F 3 4  N ARG B 91  ? N ARG B 91  O TRP B 125 ? O TRP B 125 
F 4 5  N HIS B 124 ? N HIS B 124 O ALA B 144 ? O ALA B 144 
F 5 6  N GLN B 151 ? N GLN B 151 O ILE B 218 ? O ILE B 218 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A EDO 302 ? 5  'BINDING SITE FOR RESIDUE EDO A 302' 
AC3 Software A EDO 303 ? 8  'BINDING SITE FOR RESIDUE EDO A 303' 
AC4 Software A WWX 304 ? 14 'BINDING SITE FOR RESIDUE WWX A 304' 
AC5 Software B ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN B 301'  
AC6 Software B EDO 302 ? 3  'BINDING SITE FOR RESIDUE EDO B 302' 
AC7 Software B WWX 303 ? 15 'BINDING SITE FOR RESIDUE WWX B 303' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
2  AC1 4  HIS A 98  ? HIS A 98  . ? 1_555 ? 
3  AC1 4  HIS A 121 ? HIS A 121 . ? 1_555 ? 
4  AC1 4  WWX F .   ? WWX A 304 . ? 1_555 ? 
5  AC2 5  LYS A 161 ? LYS A 161 . ? 1_555 ? 
6  AC2 5  ARG A 177 ? ARG A 177 . ? 1_555 ? 
7  AC2 5  PHE A 178 ? PHE A 178 . ? 1_555 ? 
8  AC2 5  THR A 179 ? THR A 179 . ? 1_555 ? 
9  AC2 5  HOH J .   ? HOH A 436 . ? 1_555 ? 
10 AC3 8  ASP A 112 ? ASP A 112 . ? 4_445 ? 
11 AC3 8  GLY A 113 ? GLY A 113 . ? 4_445 ? 
12 AC3 8  GLN A 160 ? GLN A 160 . ? 1_555 ? 
13 AC3 8  GLN A 223 ? GLN A 223 . ? 1_555 ? 
14 AC3 8  GLN A 224 ? GLN A 224 . ? 1_555 ? 
15 AC3 8  HOH J .   ? HOH A 478 . ? 1_555 ? 
16 AC3 8  HOH J .   ? HOH A 491 . ? 1_555 ? 
17 AC3 8  HOH J .   ? HOH A 592 . ? 1_555 ? 
18 AC4 14 SER A 64  ? SER A 64  . ? 1_555 ? 
19 AC4 14 ASN A 69  ? ASN A 69  . ? 1_555 ? 
20 AC4 14 GLN A 94  ? GLN A 94  . ? 1_555 ? 
21 AC4 14 HIS A 96  ? HIS A 96  . ? 1_555 ? 
22 AC4 14 HIS A 98  ? HIS A 98  . ? 1_555 ? 
23 AC4 14 HIS A 121 ? HIS A 121 . ? 1_555 ? 
24 AC4 14 PHE A 133 ? PHE A 133 . ? 1_555 ? 
25 AC4 14 LEU A 200 ? LEU A 200 . ? 1_555 ? 
26 AC4 14 THR A 201 ? THR A 201 . ? 1_555 ? 
27 AC4 14 VAL A 202 ? VAL A 202 . ? 1_555 ? 
28 AC4 14 PRO A 204 ? PRO A 204 . ? 1_555 ? 
29 AC4 14 ZN  C .   ? ZN  A 301 . ? 1_555 ? 
30 AC4 14 HOH J .   ? HOH A 553 . ? 1_555 ? 
31 AC4 14 HOH J .   ? HOH A 589 . ? 1_555 ? 
32 AC5 4  HIS B 96  ? HIS B 96  . ? 1_555 ? 
33 AC5 4  HIS B 98  ? HIS B 98  . ? 1_555 ? 
34 AC5 4  HIS B 121 ? HIS B 121 . ? 1_555 ? 
35 AC5 4  WWX I .   ? WWX B 303 . ? 1_555 ? 
36 AC6 3  SER B 222 ? SER B 222 . ? 1_555 ? 
37 AC6 3  ALA B 226 ? ALA B 226 . ? 1_555 ? 
38 AC6 3  HOH K .   ? HOH B 566 . ? 1_555 ? 
39 AC7 15 SER B 64  ? SER B 64  . ? 1_555 ? 
40 AC7 15 ASN B 69  ? ASN B 69  . ? 1_555 ? 
41 AC7 15 GLN B 94  ? GLN B 94  . ? 1_555 ? 
42 AC7 15 HIS B 96  ? HIS B 96  . ? 1_555 ? 
43 AC7 15 HIS B 98  ? HIS B 98  . ? 1_555 ? 
44 AC7 15 HIS B 121 ? HIS B 121 . ? 1_555 ? 
45 AC7 15 VAL B 123 ? VAL B 123 . ? 1_555 ? 
46 AC7 15 ALA B 137 ? ALA B 137 . ? 1_555 ? 
47 AC7 15 LEU B 200 ? LEU B 200 . ? 1_555 ? 
48 AC7 15 THR B 201 ? THR B 201 . ? 1_555 ? 
49 AC7 15 VAL B 202 ? VAL B 202 . ? 1_555 ? 
50 AC7 15 ZN  G .   ? ZN  B 301 . ? 1_555 ? 
51 AC7 15 HOH K .   ? HOH B 447 . ? 1_555 ? 
52 AC7 15 HOH K .   ? HOH B 584 . ? 1_555 ? 
53 AC7 15 HOH K .   ? HOH B 616 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4QIZ 
_atom_sites.fract_transf_matrix[1][1]   0.017675 
_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]   0.006265 
_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]   0.017513 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
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   ? 14.821  -28.184 -25.273 1.00 36.68 ? 6   SER A N   1 
ATOM   2    C  CA  . SER A 1 6   ? 13.961  -27.597 -24.198 1.00 31.04 ? 6   SER A CA  1 
ATOM   3    C  C   . SER A 1 6   ? 14.057  -28.425 -22.893 1.00 29.27 ? 6   SER A C   1 
ATOM   4    O  O   . SER A 1 6   ? 14.208  -29.663 -22.930 1.00 26.83 ? 6   SER A O   1 
ATOM   5    C  CB  . SER A 1 6   ? 12.549  -27.487 -24.695 1.00 39.95 ? 6   SER A CB  1 
ATOM   6    O  OG  . SER A 1 6   ? 12.025  -26.264 -24.204 1.00 48.86 ? 6   SER A OG  1 
ATOM   7    N  N   . TRP A 1 7   ? 13.998  -27.735 -21.744 1.00 23.63 ? 7   TRP A N   1 
ATOM   8    C  CA  . TRP A 1 7   ? 14.315  -28.368 -20.462 1.00 18.09 ? 7   TRP A CA  1 
ATOM   9    C  C   . TRP A 1 7   ? 13.209  -29.329 -20.061 1.00 16.19 ? 7   TRP A C   1 
ATOM   10   O  O   . TRP A 1 7   ? 12.029  -29.216 -20.432 1.00 17.89 ? 7   TRP A O   1 
ATOM   11   C  CB  . TRP A 1 7   ? 14.594  -27.250 -19.421 1.00 16.74 ? 7   TRP A CB  1 
ATOM   12   C  CG  . TRP A 1 7   ? 13.333  -26.533 -18.963 1.00 16.83 ? 7   TRP A CG  1 
ATOM   13   C  CD1 . TRP A 1 7   ? 12.776  -25.344 -19.453 1.00 16.20 ? 7   TRP A CD1 1 
ATOM   14   C  CD2 . TRP A 1 7   ? 12.428  -26.952 -17.871 1.00 14.77 ? 7   TRP A CD2 1 
ATOM   15   N  NE1 . TRP A 1 7   ? 11.630  -25.003 -18.789 1.00 17.20 ? 7   TRP A NE1 1 
ATOM   16   C  CE2 . TRP A 1 7   ? 11.372  -25.948 -17.821 1.00 15.81 ? 7   TRP A CE2 1 
ATOM   17   C  CE3 . TRP A 1 7   ? 12.419  -28.034 -16.960 1.00 15.09 ? 7   TRP A CE3 1 
ATOM   18   C  CZ2 . TRP A 1 7   ? 10.324  -26.045 -16.909 1.00 14.03 ? 7   TRP A CZ2 1 
ATOM   19   C  CZ3 . TRP A 1 7   ? 11.365  -28.080 -16.043 1.00 15.98 ? 7   TRP A CZ3 1 
ATOM   20   C  CH2 . TRP A 1 7   ? 10.337  -27.121 -16.055 1.00 15.43 ? 7   TRP A CH2 1 
ATOM   21   N  N   . GLY A 1 8   ? 13.597  -30.291 -19.237 1.00 15.14 ? 8   GLY A N   1 
ATOM   22   C  CA  . GLY A 1 8   ? 12.586  -31.218 -18.711 1.00 14.51 ? 8   GLY A CA  1 
ATOM   23   C  C   . GLY A 1 8   ? 13.173  -32.002 -17.584 1.00 14.57 ? 8   GLY A C   1 
ATOM   24   O  O   . GLY A 1 8   ? 14.052  -31.564 -16.784 1.00 14.29 ? 8   GLY A O   1 
ATOM   25   N  N   . TYR A 1 9   ? 12.737  -33.266 -17.459 1.00 14.47 ? 9   TYR A N   1 
ATOM   26   C  CA  . TYR A 1 9   ? 13.214  -34.157 -16.431 1.00 15.41 ? 9   TYR A CA  1 
ATOM   27   C  C   . TYR A 1 9   ? 13.738  -35.499 -16.991 1.00 17.27 ? 9   TYR A C   1 
ATOM   28   O  O   . TYR A 1 9   ? 13.900  -36.437 -16.246 1.00 20.02 ? 9   TYR A O   1 
ATOM   29   C  CB  . TYR A 1 9   ? 12.030  -34.463 -15.491 1.00 13.73 ? 9   TYR A CB  1 
ATOM   30   C  CG  . TYR A 1 9   ? 11.543  -33.172 -14.722 1.00 12.42 ? 9   TYR A CG  1 
ATOM   31   C  CD1 . TYR A 1 9   ? 12.232  -32.816 -13.553 1.00 13.63 ? 9   TYR A CD1 1 
ATOM   32   C  CD2 . TYR A 1 9   ? 10.481  -32.415 -15.188 1.00 13.02 ? 9   TYR A CD2 1 
ATOM   33   C  CE1 . TYR A 1 9   ? 11.837  -31.654 -12.824 1.00 12.41 ? 9   TYR A CE1 1 
ATOM   34   C  CE2 . TYR A 1 9   ? 10.031  -31.288 -14.493 1.00 13.23 ? 9   TYR A CE2 1 
ATOM   35   C  CZ  . TYR A 1 9   ? 10.760  -30.955 -13.367 1.00 11.04 ? 9   TYR A CZ  1 
ATOM   36   O  OH  . TYR A 1 9   ? 10.334  -29.824 -12.693 1.00 12.92 ? 9   TYR A OH  1 
ATOM   37   N  N   . ARG A 1 10  ? 14.040  -35.507 -18.280 1.00 20.78 ? 10  ARG A N   1 
ATOM   38   C  CA  . ARG A 1 10  ? 14.592  -36.750 -18.959 1.00 23.16 ? 10  ARG A CA  1 
ATOM   39   C  C   . ARG A 1 10  ? 16.103  -36.738 -18.814 1.00 22.21 ? 10  ARG A C   1 
ATOM   40   O  O   . ARG A 1 10  ? 16.759  -35.777 -18.302 1.00 22.95 ? 10  ARG A O   1 
ATOM   41   C  CB  . ARG A 1 10  ? 14.100  -36.779 -20.422 1.00 25.01 ? 10  ARG A CB  1 
ATOM   42   C  CG  . ARG A 1 10  ? 12.623  -36.433 -20.507 1.00 33.23 ? 10  ARG A CG  1 
ATOM   43   C  CD  . ARG A 1 10  ? 11.968  -36.721 -21.821 1.00 35.04 ? 10  ARG A CD  1 
ATOM   44   N  NE  . ARG A 1 10  ? 11.394  -38.040 -21.638 1.00 46.04 ? 10  ARG A NE  1 
ATOM   45   C  CZ  . ARG A 1 10  ? 11.914  -39.186 -22.063 1.00 49.65 ? 10  ARG A CZ  1 
ATOM   46   N  NH1 . ARG A 1 10  ? 13.043  -39.197 -22.784 1.00 58.16 ? 10  ARG A NH1 1 
ATOM   47   N  NH2 . ARG A 1 10  ? 11.253  -40.324 -21.797 1.00 38.50 ? 10  ARG A NH2 1 
ATOM   48   N  N   . GLU A 1 11  ? 16.729  -37.845 -19.253 1.00 24.13 ? 11  GLU A N   1 
ATOM   49   C  CA  . GLU A 1 11  ? 18.156  -37.960 -19.096 1.00 26.73 ? 11  GLU A CA  1 
ATOM   50   C  C   . GLU A 1 11  ? 18.904  -36.786 -19.747 1.00 22.58 ? 11  GLU A C   1 
ATOM   51   O  O   . GLU A 1 11  ? 19.852  -36.274 -19.133 1.00 27.62 ? 11  GLU A O   1 
ATOM   52   C  CB  . GLU A 1 11  ? 18.652  -39.306 -19.677 1.00 30.37 ? 11  GLU A CB  1 
ATOM   53   C  CG  . GLU A 1 11  ? 20.162  -39.324 -19.917 1.00 37.43 ? 11  GLU A CG  1 
ATOM   54   C  CD  . GLU A 1 11  ? 21.015  -39.535 -18.671 1.00 53.63 ? 11  GLU A CD  1 
ATOM   55   O  OE1 . GLU A 1 11  ? 20.465  -39.795 -17.558 1.00 58.32 ? 11  GLU A OE1 1 
ATOM   56   O  OE2 . GLU A 1 11  ? 22.269  -39.454 -18.825 1.00 57.74 ? 11  GLU A OE2 1 
ATOM   57   N  N   A HIS A 1 12  ? 18.582  -36.358 -20.963 0.50 26.47 ? 12  HIS A N   1 
ATOM   58   N  N   B HIS A 1 12  ? 18.459  -36.403 -20.947 0.50 24.54 ? 12  HIS A N   1 
ATOM   59   C  CA  A HIS A 1 12  ? 19.456  -35.313 -21.561 0.50 24.58 ? 12  HIS A CA  1 
ATOM   60   C  CA  B HIS A 1 12  ? 19.183  -35.403 -21.742 0.50 22.45 ? 12  HIS A CA  1 
ATOM   61   C  C   A HIS A 1 12  ? 18.912  -33.904 -21.504 0.50 22.19 ? 12  HIS A C   1 
ATOM   62   C  C   B HIS A 1 12  ? 19.064  -33.972 -21.277 0.50 20.61 ? 12  HIS A C   1 
ATOM   63   O  O   A HIS A 1 12  ? 19.380  -33.006 -22.189 0.50 18.01 ? 12  HIS A O   1 
ATOM   64   O  O   B HIS A 1 12  ? 20.004  -33.157 -21.430 0.50 17.29 ? 12  HIS A O   1 
ATOM   65   C  CB  A HIS A 1 12  ? 19.879  -35.683 -22.995 0.50 29.25 ? 12  HIS A CB  1 
ATOM   66   C  CB  B HIS A 1 12  ? 18.896  -35.556 -23.264 0.50 22.75 ? 12  HIS A CB  1 
ATOM   67   C  CG  A HIS A 1 12  ? 20.354  -37.125 -23.138 0.50 33.15 ? 12  HIS A CG  1 
ATOM   68   C  CG  B HIS A 1 12  ? 17.477  -35.184 -23.714 0.50 25.47 ? 12  HIS A CG  1 
ATOM   69   N  ND1 A HIS A 1 12  ? 19.653  -38.053 -23.831 0.50 34.57 ? 12  HIS A ND1 1 
ATOM   70   N  ND1 B HIS A 1 12  ? 16.405  -35.987 -23.515 0.50 26.03 ? 12  HIS A ND1 1 
ATOM   71   C  CD2 A HIS A 1 12  ? 21.476  -37.787 -22.608 0.50 34.44 ? 12  HIS A CD2 1 
ATOM   72   C  CD2 B HIS A 1 12  ? 16.997  -34.058 -24.394 0.50 24.74 ? 12  HIS A CD2 1 
ATOM   73   C  CE1 A HIS A 1 12  ? 20.298  -39.246 -23.760 0.50 37.99 ? 12  HIS A CE1 1 
ATOM   74   C  CE1 B HIS A 1 12  ? 15.297  -35.407 -24.037 0.50 24.96 ? 12  HIS A CE1 1 
ATOM   75   N  NE2 A HIS A 1 12  ? 21.415  -39.076 -23.008 0.50 37.28 ? 12  HIS A NE2 1 
ATOM   76   N  NE2 B HIS A 1 12  ? 15.665  -34.226 -24.572 0.50 28.24 ? 12  HIS A NE2 1 
ATOM   77   N  N   . ASN A 1 13  ? 17.904  -33.671 -20.676 1.00 20.42 ? 13  ASN A N   1 
ATOM   78   C  CA  . ASN A 1 13  ? 17.432  -32.284 -20.502 1.00 16.58 ? 13  ASN A CA  1 
ATOM   79   C  C   . ASN A 1 13  ? 17.047  -32.035 -19.034 1.00 17.35 ? 13  ASN A C   1 
ATOM   80   O  O   . ASN A 1 13  ? 16.484  -30.989 -18.767 1.00 16.53 ? 13  ASN A O   1 
ATOM   81   C  CB  . ASN A 1 13  ? 16.225  -31.950 -21.464 1.00 17.04 ? 13  ASN A CB  1 
ATOM   82   C  CG  . ASN A 1 13  ? 14.950  -32.724 -21.129 1.00 17.08 ? 13  ASN A CG  1 
ATOM   83   O  OD1 . ASN A 1 13  ? 14.913  -33.476 -20.116 1.00 17.93 ? 13  ASN A OD1 1 
ATOM   84   N  ND2 . ASN A 1 13  ? 13.906  -32.515 -21.930 1.00 20.21 ? 13  ASN A ND2 1 
ATOM   85   N  N   . GLY A 1 14  ? 17.424  -32.948 -18.136 1.00 16.11 ? 14  GLY A N   1 
ATOM   86   C  CA  . GLY A 1 14  ? 16.897  -32.906 -16.733 1.00 15.89 ? 14  GLY A CA  1 
ATOM   87   C  C   . GLY A 1 14  ? 17.756  -31.988 -15.869 1.00 16.80 ? 14  GLY A C   1 
ATOM   88   O  O   . GLY A 1 14  ? 18.720  -31.259 -16.312 1.00 14.24 ? 14  GLY A O   1 
ATOM   89   N  N   . PRO A 1 15  ? 17.464  -31.979 -14.583 1.00 14.93 ? 15  PRO A N   1 
ATOM   90   C  CA  . PRO A 1 15  ? 18.101  -31.084 -13.578 1.00 16.33 ? 15  PRO A CA  1 
ATOM   91   C  C   . PRO A 1 15  ? 19.591  -30.912 -13.651 1.00 16.91 ? 15  PRO A C   1 
ATOM   92   O  O   . PRO A 1 15  ? 19.993  -29.780 -13.484 1.00 16.20 ? 15  PRO A O   1 
ATOM   93   C  CB  . PRO A 1 15  ? 17.601  -31.649 -12.233 1.00 15.88 ? 15  PRO A CB  1 
ATOM   94   C  CG  . PRO A 1 15  ? 16.221  -32.097 -12.595 1.00 16.14 ? 15  PRO A CG  1 
ATOM   95   C  CD  . PRO A 1 15  ? 16.319  -32.710 -14.022 1.00 16.18 ? 15  PRO A CD  1 
ATOM   96   N  N   . ILE A 1 16  ? 20.414  -31.973 -13.895 1.00 17.37 ? 16  ILE A N   1 
ATOM   97   C  CA  . ILE A 1 16  ? 21.841  -31.801 -13.933 1.00 18.80 ? 16  ILE A CA  1 
ATOM   98   C  C   . ILE A 1 16  ? 22.283  -30.933 -15.104 1.00 18.06 ? 16  ILE A C   1 
ATOM   99   O  O   . ILE A 1 16  ? 23.399  -30.393 -15.018 1.00 18.14 ? 16  ILE A O   1 
ATOM   100  C  CB  . ILE A 1 16  ? 22.595  -33.169 -13.920 1.00 22.41 ? 16  ILE A CB  1 
ATOM   101  C  CG1 . ILE A 1 16  ? 22.337  -33.932 -15.240 1.00 26.26 ? 16  ILE A CG1 1 
ATOM   102  C  CG2 . ILE A 1 16  ? 22.229  -33.900 -12.624 1.00 27.35 ? 16  ILE A CG2 1 
ATOM   103  C  CD1 . ILE A 1 16  ? 22.188  -35.462 -15.174 1.00 38.66 ? 16  ILE A CD1 1 
ATOM   104  N  N   . HIS A 1 17  ? 21.441  -30.849 -16.140 1.00 16.88 ? 17  HIS A N   1 
ATOM   105  C  CA  . HIS A 1 17  ? 21.796  -30.086 -17.330 1.00 16.47 ? 17  HIS A CA  1 
ATOM   106  C  C   . HIS A 1 17  ? 21.289  -28.677 -17.331 1.00 15.99 ? 17  HIS A C   1 
ATOM   107  O  O   . HIS A 1 17  ? 21.622  -27.818 -18.185 1.00 15.36 ? 17  HIS A O   1 
ATOM   108  C  CB  . HIS A 1 17  ? 21.224  -30.769 -18.571 1.00 19.09 ? 17  HIS A CB  1 
ATOM   109  C  CG  . HIS A 1 17  ? 21.817  -32.133 -18.835 1.00 20.87 ? 17  HIS A CG  1 
ATOM   110  N  ND1 . HIS A 1 17  ? 23.071  -32.302 -19.288 1.00 23.68 ? 17  HIS A ND1 1 
ATOM   111  C  CD2 . HIS A 1 17  ? 21.283  -33.409 -18.671 1.00 23.76 ? 17  HIS A CD2 1 
ATOM   112  C  CE1 . HIS A 1 17  ? 23.328  -33.617 -19.418 1.00 24.55 ? 17  HIS A CE1 1 
ATOM   113  N  NE2 . HIS A 1 17  ? 22.232  -34.294 -19.041 1.00 24.94 ? 17  HIS A NE2 1 
ATOM   114  N  N   . TRP A 1 18  ? 20.439  -28.374 -16.373 1.00 13.31 ? 18  TRP A N   1 
ATOM   115  C  CA  . TRP A 1 18  ? 19.837  -27.042 -16.436 1.00 13.03 ? 18  TRP A CA  1 
ATOM   116  C  C   . TRP A 1 18  ? 20.773  -25.899 -16.443 1.00 13.09 ? 18  TRP A C   1 
ATOM   117  O  O   . TRP A 1 18  ? 20.460  -24.872 -17.027 1.00 13.24 ? 18  TRP A O   1 
ATOM   118  C  CB  . TRP A 1 18  ? 18.767  -26.835 -15.305 1.00 11.71 ? 18  TRP A CB  1 
ATOM   119  C  CG  . TRP A 1 18  ? 17.545  -27.784 -15.429 1.00 12.42 ? 18  TRP A CG  1 
ATOM   120  C  CD1 . TRP A 1 18  ? 17.205  -28.585 -16.494 1.00 12.70 ? 18  TRP A CD1 1 
ATOM   121  C  CD2 . TRP A 1 18  ? 16.524  -27.978 -14.413 1.00 12.04 ? 18  TRP A CD2 1 
ATOM   122  N  NE1 . TRP A 1 18  ? 16.029  -29.266 -16.247 1.00 13.90 ? 18  TRP A NE1 1 
ATOM   123  C  CE2 . TRP A 1 18  ? 15.541  -28.888 -14.984 1.00 11.80 ? 18  TRP A CE2 1 
ATOM   124  C  CE3 . TRP A 1 18  ? 16.287  -27.418 -13.132 1.00 13.94 ? 18  TRP A CE3 1 
ATOM   125  C  CZ2 . TRP A 1 18  ? 14.428  -29.344 -14.271 1.00 14.00 ? 18  TRP A CZ2 1 
ATOM   126  C  CZ3 . TRP A 1 18  ? 15.164  -27.844 -12.432 1.00 13.14 ? 18  TRP A CZ3 1 
ATOM   127  C  CH2 . TRP A 1 18  ? 14.242  -28.775 -13.012 1.00 12.39 ? 18  TRP A CH2 1 
ATOM   128  N  N   . LYS A 1 19  ? 21.862  -26.062 -15.714 1.00 13.92 ? 19  LYS A N   1 
ATOM   129  C  CA  . LYS A 1 19  ? 22.916  -24.984 -15.619 1.00 12.90 ? 19  LYS A CA  1 
ATOM   130  C  C   . LYS A 1 19  ? 23.509  -24.631 -17.011 1.00 14.79 ? 19  LYS A C   1 
ATOM   131  O  O   . LYS A 1 19  ? 24.064  -23.552 -17.140 1.00 17.14 ? 19  LYS A O   1 
ATOM   132  C  CB  . LYS A 1 19  ? 24.000  -25.391 -14.644 1.00 13.95 ? 19  LYS A CB  1 
ATOM   133  C  CG  . LYS A 1 19  ? 24.759  -26.646 -15.208 1.00 18.32 ? 19  LYS A CG  1 
ATOM   134  C  CD  . LYS A 1 19  ? 25.862  -27.127 -14.294 1.00 18.51 ? 19  LYS A CD  1 
ATOM   135  C  CE  . LYS A 1 19  ? 27.024  -26.155 -14.384 1.00 25.51 ? 19  LYS A CE  1 
ATOM   136  N  NZ  . LYS A 1 19  ? 28.061  -26.547 -13.399 1.00 29.48 ? 19  LYS A NZ  1 
ATOM   137  N  N   . GLU A 1 20  ? 23.362  -25.517 -17.982 1.00 14.18 ? 20  GLU A N   1 
ATOM   138  C  CA  . GLU A 1 20  ? 23.949  -25.236 -19.316 1.00 14.20 ? 20  GLU A CA  1 
ATOM   139  C  C   . GLU A 1 20  ? 23.214  -24.082 -19.972 1.00 15.42 ? 20  GLU A C   1 
ATOM   140  O  O   . GLU A 1 20  ? 23.795  -23.375 -20.791 1.00 18.17 ? 20  GLU A O   1 
ATOM   141  C  CB  . GLU A 1 20  ? 23.855  -26.486 -20.234 1.00 14.69 ? 20  GLU A CB  1 
ATOM   142  C  CG  . GLU A 1 20  ? 24.782  -27.586 -19.691 1.00 16.71 ? 20  GLU A CG  1 
ATOM   143  C  CD  . GLU A 1 20  ? 24.330  -28.964 -20.221 1.00 20.52 ? 20  GLU A CD  1 
ATOM   144  O  OE1 . GLU A 1 20  ? 23.649  -29.005 -21.273 1.00 24.23 ? 20  GLU A OE1 1 
ATOM   145  O  OE2 . GLU A 1 20  ? 24.577  -29.999 -19.559 1.00 20.33 ? 20  GLU A OE2 1 
ATOM   146  N  N   . PHE A 1 21  ? 21.937  -23.889 -19.627 1.00 15.62 ? 21  PHE A N   1 
ATOM   147  C  CA  . PHE A 1 21  ? 21.131  -22.823 -20.184 1.00 16.92 ? 21  PHE A CA  1 
ATOM   148  C  C   . PHE A 1 21  ? 20.687  -21.752 -19.184 1.00 16.58 ? 21  PHE A C   1 
ATOM   149  O  O   . PHE A 1 21  ? 20.292  -20.673 -19.564 1.00 16.12 ? 21  PHE A O   1 
ATOM   150  C  CB  . PHE A 1 21  ? 19.888  -23.472 -20.812 1.00 20.84 ? 21  PHE A CB  1 
ATOM   151  C  CG  . PHE A 1 21  ? 20.264  -24.541 -21.825 1.00 30.58 ? 21  PHE A CG  1 
ATOM   152  C  CD1 . PHE A 1 21  ? 20.246  -25.902 -21.479 1.00 35.99 ? 21  PHE A CD1 1 
ATOM   153  C  CD2 . PHE A 1 21  ? 20.744  -24.172 -23.061 1.00 32.05 ? 21  PHE A CD2 1 
ATOM   154  C  CE1 . PHE A 1 21  ? 20.654  -26.884 -22.410 1.00 40.00 ? 21  PHE A CE1 1 
ATOM   155  C  CE2 . PHE A 1 21  ? 21.139  -25.126 -24.001 1.00 37.72 ? 21  PHE A CE2 1 
ATOM   156  C  CZ  . PHE A 1 21  ? 21.110  -26.481 -23.669 1.00 42.57 ? 21  PHE A CZ  1 
ATOM   157  N  N   . PHE A 1 22  ? 20.720  -22.105 -17.882 1.00 13.67 ? 22  PHE A N   1 
ATOM   158  C  CA  . PHE A 1 22  ? 20.180  -21.268 -16.800 1.00 13.92 ? 22  PHE A CA  1 
ATOM   159  C  C   . PHE A 1 22  ? 21.280  -21.276 -15.729 1.00 15.12 ? 22  PHE A C   1 
ATOM   160  O  O   . PHE A 1 22  ? 21.290  -22.096 -14.767 1.00 14.14 ? 22  PHE A O   1 
ATOM   161  C  CB  . PHE A 1 22  ? 18.830  -21.814 -16.250 1.00 12.48 ? 22  PHE A CB  1 
ATOM   162  C  CG  . PHE A 1 22  ? 17.731  -21.898 -17.277 1.00 12.93 ? 22  PHE A CG  1 
ATOM   163  C  CD1 . PHE A 1 22  ? 17.078  -20.777 -17.641 1.00 16.07 ? 22  PHE A CD1 1 
ATOM   164  C  CD2 . PHE A 1 22  ? 17.500  -23.074 -17.967 1.00 14.89 ? 22  PHE A CD2 1 
ATOM   165  C  CE1 . PHE A 1 22  ? 16.116  -20.828 -18.647 1.00 15.87 ? 22  PHE A CE1 1 
ATOM   166  C  CE2 . PHE A 1 22  ? 16.539  -23.146 -18.967 1.00 16.13 ? 22  PHE A CE2 1 
ATOM   167  C  CZ  . PHE A 1 22  ? 15.862  -22.005 -19.286 1.00 15.64 ? 22  PHE A CZ  1 
ATOM   168  N  N   . PRO A 1 23  ? 22.285  -20.388 -15.831 1.00 14.29 ? 23  PRO A N   1 
ATOM   169  C  CA  . PRO A 1 23  ? 23.439  -20.504 -14.924 1.00 14.38 ? 23  PRO A CA  1 
ATOM   170  C  C   . PRO A 1 23  ? 23.101  -20.295 -13.421 1.00 14.57 ? 23  PRO A C   1 
ATOM   171  O  O   . PRO A 1 23  ? 23.876  -20.760 -12.549 1.00 15.34 ? 23  PRO A O   1 
ATOM   172  C  CB  . PRO A 1 23  ? 24.455  -19.426 -15.508 1.00 15.59 ? 23  PRO A CB  1 
ATOM   173  C  CG  . PRO A 1 23  ? 23.587  -18.546 -16.367 1.00 20.54 ? 23  PRO A CG  1 
ATOM   174  C  CD  . PRO A 1 23  ? 22.573  -19.449 -16.972 1.00 15.10 ? 23  PRO A CD  1 
ATOM   175  N  N   . ILE A 1 24  ? 21.989  -19.619 -13.167 1.00 13.45 ? 24  ILE A N   1 
ATOM   176  C  CA  . ILE A 1 24  ? 21.528  -19.393 -11.804 1.00 14.56 ? 24  ILE A CA  1 
ATOM   177  C  C   . ILE A 1 24  ? 21.199  -20.773 -11.152 1.00 14.58 ? 24  ILE A C   1 
ATOM   178  O  O   . ILE A 1 24  ? 21.122  -20.848 -9.929  1.00 13.88 ? 24  ILE A O   1 
ATOM   179  C  CB  . ILE A 1 24  ? 20.333  -18.422 -11.644 1.00 13.70 ? 24  ILE A CB  1 
ATOM   180  C  CG1 . ILE A 1 24  ? 20.218  -17.876 -10.227 1.00 15.51 ? 24  ILE A CG1 1 
ATOM   181  C  CG2 . ILE A 1 24  ? 19.064  -19.083 -12.034 1.00 13.91 ? 24  ILE A CG2 1 
ATOM   182  C  CD1 . ILE A 1 24  ? 21.382  -16.985 -9.837  1.00 18.16 ? 24  ILE A CD1 1 
ATOM   183  N  N   . ALA A 1 25  ? 21.140  -21.870 -11.961 1.00 13.55 ? 25  ALA A N   1 
ATOM   184  C  CA  . ALA A 1 25  ? 20.927  -23.205 -11.343 1.00 12.29 ? 25  ALA A CA  1 
ATOM   185  C  C   . ALA A 1 25  ? 21.962  -23.507 -10.279 1.00 13.86 ? 25  ALA A C   1 
ATOM   186  O  O   . ALA A 1 25  ? 21.715  -24.292 -9.361  1.00 15.29 ? 25  ALA A O   1 
ATOM   187  C  CB  . ALA A 1 25  ? 21.014  -24.325 -12.400 1.00 11.84 ? 25  ALA A CB  1 
ATOM   188  N  N   . ASP A 1 26  ? 23.171  -22.942 -10.399 1.00 15.97 ? 26  ASP A N   1 
ATOM   189  C  CA  . ASP A 1 26  ? 24.254  -23.070 -9.336  1.00 15.41 ? 26  ASP A CA  1 
ATOM   190  C  C   . ASP A 1 26  ? 24.364  -21.829 -8.413  1.00 16.91 ? 26  ASP A C   1 
ATOM   191  O  O   . ASP A 1 26  ? 25.411  -21.629 -7.734  1.00 18.88 ? 26  ASP A O   1 
ATOM   192  C  CB  . ASP A 1 26  ? 25.633  -23.277 -10.034 1.00 16.83 ? 26  ASP A CB  1 
ATOM   193  C  CG  . ASP A 1 26  ? 25.681  -24.514 -10.826 1.00 20.28 ? 26  ASP A CG  1 
ATOM   194  O  OD1 . ASP A 1 26  ? 25.247  -25.587 -10.314 1.00 22.41 ? 26  ASP A OD1 1 
ATOM   195  O  OD2 . ASP A 1 26  ? 26.181  -24.399 -11.967 1.00 22.75 ? 26  ASP A OD2 1 
ATOM   196  N  N   . GLY A 1 27  ? 23.249  -21.124 -8.222  1.00 15.64 ? 27  GLY A N   1 
ATOM   197  C  CA  . GLY A 1 27  ? 23.206  -19.866 -7.420  1.00 15.99 ? 27  GLY A CA  1 
ATOM   198  C  C   . GLY A 1 27  ? 23.260  -20.152 -5.908  1.00 15.71 ? 27  GLY A C   1 
ATOM   199  O  O   . GLY A 1 27  ? 23.387  -21.346 -5.522  1.00 16.68 ? 27  GLY A O   1 
ATOM   200  N  N   . ASP A 1 28  ? 23.213  -19.098 -5.114  1.00 15.87 ? 28  ASP A N   1 
ATOM   201  C  CA  . ASP A 1 28  ? 23.399  -19.472 -3.682  1.00 18.46 ? 28  ASP A CA  1 
ATOM   202  C  C   . ASP A 1 28  ? 22.121  -19.578 -2.947  1.00 17.22 ? 28  ASP A C   1 
ATOM   203  O  O   . ASP A 1 28  ? 22.182  -19.788 -1.761  1.00 17.10 ? 28  ASP A O   1 
ATOM   204  C  CB  . ASP A 1 28  ? 24.377  -18.523 -2.937  1.00 22.29 ? 28  ASP A CB  1 
ATOM   205  C  CG  . ASP A 1 28  ? 25.702  -18.317 -3.658  1.00 23.31 ? 28  ASP A CG  1 
ATOM   206  O  OD1 . ASP A 1 28  ? 26.364  -19.301 -4.034  1.00 26.69 ? 28  ASP A OD1 1 
ATOM   207  O  OD2 . ASP A 1 28  ? 26.094  -17.146 -3.814  1.00 29.21 ? 28  ASP A OD2 1 
ATOM   208  N  N   . GLN A 1 29  ? 20.981  -19.390 -3.603  1.00 13.09 ? 29  GLN A N   1 
ATOM   209  C  CA  . GLN A 1 29  ? 19.707  -19.542 -2.879  1.00 13.48 ? 29  GLN A CA  1 
ATOM   210  C  C   . GLN A 1 29  ? 18.760  -20.419 -3.740  1.00 11.98 ? 29  GLN A C   1 
ATOM   211  O  O   . GLN A 1 29  ? 17.616  -20.014 -4.046  1.00 11.82 ? 29  GLN A O   1 
ATOM   212  C  CB  . GLN A 1 29  ? 19.055  -18.204 -2.604  1.00 14.89 ? 29  GLN A CB  1 
ATOM   213  C  CG  . GLN A 1 29  ? 19.966  -17.344 -1.649  1.00 18.92 ? 29  GLN A CG  1 
ATOM   214  C  CD  . GLN A 1 29  ? 19.150  -16.285 -0.851  1.00 21.94 ? 29  GLN A CD  1 
ATOM   215  O  OE1 . GLN A 1 29  ? 18.108  -15.747 -1.303  1.00 21.07 ? 29  GLN A OE1 1 
ATOM   216  N  NE2 . GLN A 1 29  ? 19.573  -16.074 0.390   1.00 29.07 ? 29  GLN A NE2 1 
ATOM   217  N  N   . GLN A 1 30  ? 19.227  -21.638 -4.123  1.00 10.37 ? 30  GLN A N   1 
ATOM   218  C  CA  . GLN A 1 30  ? 18.413  -22.509 -4.960  1.00 9.37  ? 30  GLN A CA  1 
ATOM   219  C  C   . GLN A 1 30  ? 17.508  -23.448 -4.104  1.00 9.70  ? 30  GLN A C   1 
ATOM   220  O  O   . GLN A 1 30  ? 17.819  -23.795 -2.957  1.00 10.74 ? 30  GLN A O   1 
ATOM   221  C  CB  . GLN A 1 30  ? 19.321  -23.372 -5.858  1.00 9.70  ? 30  GLN A CB  1 
ATOM   222  C  CG  . GLN A 1 30  ? 20.005  -22.437 -6.908  1.00 10.21 ? 30  GLN A CG  1 
ATOM   223  C  CD  . GLN A 1 30  ? 18.934  -22.006 -7.923  1.00 9.51  ? 30  GLN A CD  1 
ATOM   224  O  OE1 . GLN A 1 30  ? 18.374  -22.839 -8.651  1.00 9.32  ? 30  GLN A OE1 1 
ATOM   225  N  NE2 . GLN A 1 30  ? 18.575  -20.732 -7.977  1.00 10.24 ? 30  GLN A NE2 1 
ATOM   226  N  N   . SER A 1 31  ? 16.401  -23.874 -4.685  1.00 9.56  ? 31  SER A N   1 
ATOM   227  C  CA  . SER A 1 31  ? 15.460  -24.796 -4.021  1.00 9.96  ? 31  SER A CA  1 
ATOM   228  C  C   . SER A 1 31  ? 15.233  -26.011 -4.935  1.00 11.40 ? 31  SER A C   1 
ATOM   229  O  O   . SER A 1 31  ? 15.334  -25.936 -6.173  1.00 11.07 ? 31  SER A O   1 
ATOM   230  C  CB  . SER A 1 31  ? 14.131  -24.038 -3.834  1.00 12.67 ? 31  SER A CB  1 
ATOM   231  O  OG  . SER A 1 31  ? 14.357  -22.996 -2.916  1.00 11.34 ? 31  SER A OG  1 
ATOM   232  N  N   . PRO A 1 32  ? 14.749  -27.130 -4.405  1.00 10.56 ? 32  PRO A N   1 
ATOM   233  C  CA  . PRO A 1 32  ? 14.372  -27.337 -3.007  1.00 10.45 ? 32  PRO A CA  1 
ATOM   234  C  C   . PRO A 1 32  ? 15.617  -27.648 -2.188  1.00 10.15 ? 32  PRO A C   1 
ATOM   235  O  O   . PRO A 1 32  ? 16.762  -27.617 -2.662  1.00 11.13 ? 32  PRO A O   1 
ATOM   236  C  CB  . PRO A 1 32  ? 13.482  -28.580 -3.125  1.00 12.00 ? 32  PRO A CB  1 
ATOM   237  C  CG  . PRO A 1 32  ? 14.121  -29.419 -4.263  1.00 10.02 ? 32  PRO A CG  1 
ATOM   238  C  CD  . PRO A 1 32  ? 14.506  -28.360 -5.247  1.00 10.94 ? 32  PRO A CD  1 
ATOM   239  N  N   . ILE A 1 33  ? 15.386  -27.970 -0.913  1.00 9.97  ? 33  ILE A N   1 
ATOM   240  C  CA  . ILE A 1 33  ? 16.458  -28.278 0.040   1.00 9.79  ? 33  ILE A CA  1 
ATOM   241  C  C   . ILE A 1 33  ? 16.035  -29.457 0.925   1.00 11.18 ? 33  ILE A C   1 
ATOM   242  O  O   . ILE A 1 33  ? 14.873  -29.830 0.930   1.00 11.86 ? 33  ILE A O   1 
ATOM   243  C  CB  . ILE A 1 33  ? 16.858  -27.038 0.947   1.00 11.18 ? 33  ILE A CB  1 
ATOM   244  C  CG1 . ILE A 1 33  ? 15.623  -26.621 1.839   1.00 11.11 ? 33  ILE A CG1 1 
ATOM   245  C  CG2 . ILE A 1 33  ? 17.382  -25.891 0.048   1.00 11.49 ? 33  ILE A CG2 1 
ATOM   246  C  CD1 . ILE A 1 33  ? 16.028  -25.781 3.044   1.00 13.54 ? 33  ILE A CD1 1 
ATOM   247  N  N   . GLU A 1 34  ? 17.062  -29.988 1.596   1.00 11.78 ? 34  GLU A N   1 
ATOM   248  C  CA  . GLU A 1 34  ? 16.768  -30.885 2.749   1.00 13.28 ? 34  GLU A CA  1 
ATOM   249  C  C   . GLU A 1 34  ? 16.598  -30.010 3.991   1.00 12.38 ? 34  GLU A C   1 
ATOM   250  O  O   . GLU A 1 34  ? 17.516  -29.196 4.374   1.00 14.35 ? 34  GLU A O   1 
ATOM   251  C  CB  . GLU A 1 34  ? 17.933  -31.829 2.941   1.00 14.01 ? 34  GLU A CB  1 
ATOM   252  C  CG  . GLU A 1 34  ? 17.475  -32.743 4.084   1.00 16.96 ? 34  GLU A CG  1 
ATOM   253  C  CD  . GLU A 1 34  ? 18.542  -33.827 4.356   1.00 19.73 ? 34  GLU A CD  1 
ATOM   254  O  OE1 . GLU A 1 34  ? 19.634  -33.816 3.721   1.00 22.74 ? 34  GLU A OE1 1 
ATOM   255  O  OE2 . GLU A 1 34  ? 18.204  -34.688 5.181   1.00 21.24 ? 34  GLU A OE2 1 
ATOM   256  N  N   . ILE A 1 35  ? 15.449  -30.206 4.643   1.00 12.46 ? 35  ILE A N   1 
ATOM   257  C  CA  . ILE A 1 35  ? 15.202  -29.536 5.943   1.00 14.04 ? 35  ILE A CA  1 
ATOM   258  C  C   . ILE A 1 35  ? 15.789  -30.448 7.020   1.00 13.36 ? 35  ILE A C   1 
ATOM   259  O  O   . ILE A 1 35  ? 15.367  -31.623 7.093   1.00 16.06 ? 35  ILE A O   1 
ATOM   260  C  CB  . ILE A 1 35  ? 13.718  -29.381 6.094   1.00 13.21 ? 35  ILE A CB  1 
ATOM   261  C  CG1 . ILE A 1 35  ? 13.242  -28.356 5.016   1.00 15.65 ? 35  ILE A CG1 1 
ATOM   262  C  CG2 . ILE A 1 35  ? 13.362  -28.822 7.466   1.00 14.40 ? 35  ILE A CG2 1 
ATOM   263  C  CD1 . ILE A 1 35  ? 11.714  -28.289 4.834   1.00 19.44 ? 35  ILE A CD1 1 
ATOM   264  N  N   . LYS A 1 36  ? 16.771  -29.924 7.765   1.00 16.26 ? 36  LYS A N   1 
ATOM   265  C  CA  . LYS A 1 36  ? 17.506  -30.693 8.805   1.00 17.99 ? 36  LYS A CA  1 
ATOM   266  C  C   . LYS A 1 36  ? 17.032  -30.113 10.114  1.00 20.82 ? 36  LYS A C   1 
ATOM   267  O  O   . LYS A 1 36  ? 17.444  -29.008 10.516  1.00 21.14 ? 36  LYS A O   1 
ATOM   268  C  CB  . LYS A 1 36  ? 18.961  -30.457 8.644   1.00 20.15 ? 36  LYS A CB  1 
ATOM   269  C  CG  . LYS A 1 36  ? 19.469  -30.941 7.310   1.00 25.47 ? 36  LYS A CG  1 
ATOM   270  C  CD  . LYS A 1 36  ? 20.949  -30.761 7.233   1.00 27.79 ? 36  LYS A CD  1 
ATOM   271  C  CE  . LYS A 1 36  ? 21.451  -31.121 5.859   1.00 27.83 ? 36  LYS A CE  1 
ATOM   272  N  NZ  . LYS A 1 36  ? 22.911  -31.369 5.862   1.00 34.32 ? 36  LYS A NZ  1 
ATOM   273  N  N   . THR A 1 37  ? 16.149  -30.861 10.769  1.00 21.20 ? 37  THR A N   1 
ATOM   274  C  CA  . THR A 1 37  ? 15.444  -30.318 11.907  1.00 25.00 ? 37  THR A CA  1 
ATOM   275  C  C   . THR A 1 37  ? 16.370  -30.021 13.086  1.00 29.03 ? 37  THR A C   1 
ATOM   276  O  O   . THR A 1 37  ? 15.979  -29.253 13.967  1.00 32.45 ? 37  THR A O   1 
ATOM   277  C  CB  . THR A 1 37  ? 14.277  -31.204 12.367  1.00 22.07 ? 37  THR A CB  1 
ATOM   278  O  OG1 . THR A 1 37  ? 14.790  -32.450 12.904  1.00 24.80 ? 37  THR A OG1 1 
ATOM   279  C  CG2 . THR A 1 37  ? 13.262  -31.446 11.270  1.00 29.03 ? 37  THR A CG2 1 
ATOM   280  N  N   . LYS A 1 38  ? 17.581  -30.576 13.093  1.00 27.46 ? 38  LYS A N   1 
ATOM   281  C  CA  . LYS A 1 38  ? 18.481  -30.277 14.197  1.00 32.59 ? 38  LYS A CA  1 
ATOM   282  C  C   . LYS A 1 38  ? 19.102  -28.895 14.026  1.00 31.31 ? 38  LYS A C   1 
ATOM   283  O  O   . LYS A 1 38  ? 19.640  -28.351 15.007  1.00 29.49 ? 38  LYS A O   1 
ATOM   284  C  CB  . LYS A 1 38  ? 19.589  -31.340 14.335  1.00 38.36 ? 38  LYS A CB  1 
ATOM   285  C  CG  . LYS A 1 38  ? 20.568  -31.435 13.151  1.00 44.16 ? 38  LYS A CG  1 
ATOM   286  C  CD  . LYS A 1 38  ? 22.018  -31.627 13.598  1.00 50.08 ? 38  LYS A CD  1 
ATOM   287  C  CE  . LYS A 1 38  ? 22.081  -32.536 14.829  1.00 50.25 ? 38  LYS A CE  1 
ATOM   288  N  NZ  . LYS A 1 38  ? 23.409  -32.588 15.501  1.00 54.16 ? 38  LYS A NZ  1 
ATOM   289  N  N   . GLU A 1 39  ? 19.058  -28.362 12.795  1.00 24.94 ? 39  GLU A N   1 
ATOM   290  C  CA  . GLU A 1 39  ? 19.686  -27.081 12.444  1.00 29.48 ? 39  GLU A CA  1 
ATOM   291  C  C   . GLU A 1 39  ? 18.610  -25.994 12.304  1.00 26.50 ? 39  GLU A C   1 
ATOM   292  O  O   . GLU A 1 39  ? 18.915  -24.803 12.153  1.00 33.59 ? 39  GLU A O   1 
ATOM   293  C  CB  . GLU A 1 39  ? 20.420  -27.204 11.131  1.00 31.27 ? 39  GLU A CB  1 
ATOM   294  C  CG  . GLU A 1 39  ? 21.647  -28.122 11.183  1.00 36.55 ? 39  GLU A CG  1 
ATOM   295  C  CD  . GLU A 1 39  ? 22.339  -28.323 9.825   1.00 43.90 ? 39  GLU A CD  1 
ATOM   296  O  OE1 . GLU A 1 39  ? 22.090  -27.555 8.826   1.00 47.72 ? 39  GLU A OE1 1 
ATOM   297  O  OE2 . GLU A 1 39  ? 23.131  -29.293 9.745   1.00 47.00 ? 39  GLU A OE2 1 
ATOM   298  N  N   . VAL A 1 40  ? 17.341  -26.406 12.342  1.00 25.24 ? 40  VAL A N   1 
ATOM   299  C  CA  . VAL A 1 40  ? 16.178  -25.489 12.147  1.00 25.17 ? 40  VAL A CA  1 
ATOM   300  C  C   . VAL A 1 40  ? 16.166  -24.648 13.398  1.00 27.23 ? 40  VAL A C   1 
ATOM   301  O  O   . VAL A 1 40  ? 16.344  -25.210 14.493  1.00 25.85 ? 40  VAL A O   1 
ATOM   302  C  CB  . VAL A 1 40  ? 14.917  -26.346 12.029  1.00 21.72 ? 40  VAL A CB  1 
ATOM   303  C  CG1 . VAL A 1 40  ? 13.623  -25.623 12.348  1.00 25.83 ? 40  VAL A CG1 1 
ATOM   304  C  CG2 . VAL A 1 40  ? 14.886  -26.960 10.643  1.00 24.97 ? 40  VAL A CG2 1 
ATOM   305  N  N   . LYS A 1 41  ? 16.012  -23.336 13.236  1.00 24.95 ? 41  LYS A N   1 
ATOM   306  C  CA  . LYS A 1 41  ? 15.858  -22.434 14.375  1.00 28.12 ? 41  LYS A CA  1 
ATOM   307  C  C   . LYS A 1 41  ? 14.381  -21.980 14.545  1.00 23.65 ? 41  LYS A C   1 
ATOM   308  O  O   . LYS A 1 41  ? 13.786  -21.396 13.658  1.00 21.89 ? 41  LYS A O   1 
ATOM   309  C  CB  . LYS A 1 41  ? 16.833  -21.258 14.233  1.00 30.68 ? 41  LYS A CB  1 
ATOM   310  C  CG  . LYS A 1 41  ? 18.304  -21.702 14.288  1.00 40.31 ? 41  LYS A CG  1 
ATOM   311  C  CD  . LYS A 1 41  ? 18.839  -22.125 15.666  1.00 44.46 ? 41  LYS A CD  1 
ATOM   312  C  CE  . LYS A 1 41  ? 18.521  -23.563 16.140  1.00 51.59 ? 41  LYS A CE  1 
ATOM   313  N  NZ  . LYS A 1 41  ? 19.204  -24.769 15.529  1.00 48.86 ? 41  LYS A NZ  1 
ATOM   314  N  N   . TYR A 1 42  ? 13.803  -22.250 15.724  1.00 22.56 ? 42  TYR A N   1 
ATOM   315  C  CA  . TYR A 1 42  ? 12.511  -21.690 16.101  1.00 23.79 ? 42  TYR A CA  1 
ATOM   316  C  C   . TYR A 1 42  ? 12.639  -20.161 16.183  1.00 23.99 ? 42  TYR A C   1 
ATOM   317  O  O   . TYR A 1 42  ? 13.645  -19.662 16.691  1.00 25.22 ? 42  TYR A O   1 
ATOM   318  C  CB  . TYR A 1 42  ? 12.016  -22.252 17.448  1.00 24.96 ? 42  TYR A CB  1 
ATOM   319  C  CG  . TYR A 1 42  ? 10.848  -21.425 17.999  1.00 24.17 ? 42  TYR A CG  1 
ATOM   320  C  CD1 . TYR A 1 42  ? 9.587   -21.425 17.389  1.00 25.44 ? 42  TYR A CD1 1 
ATOM   321  C  CD2 . TYR A 1 42  ? 11.007  -20.595 19.158  1.00 28.32 ? 42  TYR A CD2 1 
ATOM   322  C  CE1 . TYR A 1 42  ? 8.537   -20.653 17.863  1.00 29.29 ? 42  TYR A CE1 1 
ATOM   323  C  CE2 . TYR A 1 42  ? 9.946   -19.811 19.642  1.00 28.07 ? 42  TYR A CE2 1 
ATOM   324  C  CZ  . TYR A 1 42  ? 8.713   -19.823 18.994  1.00 29.66 ? 42  TYR A CZ  1 
ATOM   325  O  OH  . TYR A 1 42  ? 7.619   -19.066 19.469  1.00 31.16 ? 42  TYR A OH  1 
ATOM   326  N  N   . ASP A 1 43  ? 11.648  -19.422 15.677  1.00 20.88 ? 43  ASP A N   1 
ATOM   327  C  CA  . ASP A 1 43  ? 11.741  -17.985 15.678  1.00 19.79 ? 43  ASP A CA  1 
ATOM   328  C  C   . ASP A 1 43  ? 10.337  -17.436 16.136  1.00 22.62 ? 43  ASP A C   1 
ATOM   329  O  O   . ASP A 1 43  ? 9.301   -17.611 15.440  1.00 20.37 ? 43  ASP A O   1 
ATOM   330  C  CB  . ASP A 1 43  ? 12.213  -17.464 14.257  1.00 21.11 ? 43  ASP A CB  1 
ATOM   331  C  CG  . ASP A 1 43  ? 12.298  -15.937 14.161  1.00 23.59 ? 43  ASP A CG  1 
ATOM   332  O  OD1 . ASP A 1 43  ? 11.867  -15.207 15.116  1.00 25.76 ? 43  ASP A OD1 1 
ATOM   333  O  OD2 . ASP A 1 43  ? 12.794  -15.405 13.130  1.00 23.22 ? 43  ASP A OD2 1 
ATOM   334  N  N   . SER A 1 44  ? 10.290  -16.812 17.319  1.00 26.60 ? 44  SER A N   1 
ATOM   335  C  CA  . SER A 1 44  ? 9.015   -16.293 17.861  1.00 28.50 ? 44  SER A CA  1 
ATOM   336  C  C   . SER A 1 44  ? 8.456   -15.065 17.180  1.00 28.65 ? 44  SER A C   1 
ATOM   337  O  O   . SER A 1 44  ? 7.288   -14.699 17.365  1.00 30.82 ? 44  SER A O   1 
ATOM   338  C  CB  . SER A 1 44  ? 9.216   -15.995 19.332  1.00 33.68 ? 44  SER A CB  1 
ATOM   339  O  OG  . SER A 1 44  ? 10.073  -14.884 19.463  1.00 38.00 ? 44  SER A OG  1 
ATOM   340  N  N   . SER A 1 45  ? 9.288   -14.407 16.376  1.00 28.43 ? 45  SER A N   1 
ATOM   341  C  CA  . SER A 1 45  ? 8.824   -13.367 15.473  1.00 25.07 ? 45  SER A CA  1 
ATOM   342  C  C   . SER A 1 45  ? 8.042   -13.837 14.244  1.00 25.13 ? 45  SER A C   1 
ATOM   343  O  O   . SER A 1 45  ? 7.426   -13.043 13.523  1.00 25.44 ? 45  SER A O   1 
ATOM   344  C  CB  . SER A 1 45  ? 10.027  -12.503 15.067  1.00 26.74 ? 45  SER A CB  1 
ATOM   345  O  OG  . SER A 1 45  ? 10.822  -13.041 13.989  1.00 29.18 ? 45  SER A OG  1 
ATOM   346  N  N   . LEU A 1 46  ? 8.103   -15.140 13.932  1.00 20.72 ? 46  LEU A N   1 
ATOM   347  C  CA  . LEU A 1 46  ? 7.280   -15.635 12.897  1.00 20.43 ? 46  LEU A CA  1 
ATOM   348  C  C   . LEU A 1 46  ? 5.825   -15.633 13.289  1.00 22.82 ? 46  LEU A C   1 
ATOM   349  O  O   . LEU A 1 46  ? 5.494   -16.147 14.360  1.00 28.96 ? 46  LEU A O   1 
ATOM   350  C  CB  . LEU A 1 46  ? 7.713   -17.107 12.516  1.00 17.62 ? 46  LEU A CB  1 
ATOM   351  C  CG  . LEU A 1 46  ? 9.021   -17.211 11.695  1.00 16.87 ? 46  LEU A CG  1 
ATOM   352  C  CD1 . LEU A 1 46  ? 9.272   -18.701 11.503  1.00 16.89 ? 46  LEU A CD1 1 
ATOM   353  C  CD2 . LEU A 1 46  ? 8.737   -16.576 10.324  1.00 16.01 ? 46  LEU A CD2 1 
ATOM   354  N  N   . ARG A 1 47  ? 4.981   -15.191 12.369  1.00 20.61 ? 47  ARG A N   1 
ATOM   355  C  CA  . ARG A 1 47  ? 3.553   -15.113 12.591  1.00 22.64 ? 47  ARG A CA  1 
ATOM   356  C  C   . ARG A 1 47  ? 2.854   -16.356 12.073  1.00 19.79 ? 47  ARG A C   1 
ATOM   357  O  O   . ARG A 1 47  ? 3.364   -17.058 11.180  1.00 17.88 ? 47  ARG A O   1 
ATOM   358  C  CB  . ARG A 1 47  ? 2.962   -13.845 11.952  1.00 23.34 ? 47  ARG A CB  1 
ATOM   359  C  CG  . ARG A 1 47  ? 3.494   -12.512 12.510  1.00 28.25 ? 47  ARG A CG  1 
ATOM   360  C  CD  . ARG A 1 47  ? 4.055   -12.604 13.937  1.00 41.34 ? 47  ARG A CD  1 
ATOM   361  N  NE  . ARG A 1 47  ? 3.074   -12.763 15.025  1.00 40.17 ? 47  ARG A NE  1 
ATOM   362  C  CZ  . ARG A 1 47  ? 3.295   -13.411 16.183  1.00 41.20 ? 47  ARG A CZ  1 
ATOM   363  N  NH1 . ARG A 1 47  ? 4.426   -14.042 16.436  1.00 49.20 ? 47  ARG A NH1 1 
ATOM   364  N  NH2 . ARG A 1 47  ? 2.360   -13.445 17.108  1.00 55.92 ? 47  ARG A NH2 1 
ATOM   365  N  N   . PRO A 1 48  ? 1.677   -16.690 12.579  1.00 16.90 ? 48  PRO A N   1 
ATOM   366  C  CA  . PRO A 1 48  ? 0.867   -17.736 12.001  1.00 16.84 ? 48  PRO A CA  1 
ATOM   367  C  C   . PRO A 1 48  ? 0.485   -17.351 10.596  1.00 16.96 ? 48  PRO A C   1 
ATOM   368  O  O   . PRO A 1 48  ? 0.437   -16.158 10.239  1.00 17.68 ? 48  PRO A O   1 
ATOM   369  C  CB  . PRO A 1 48  ? -0.375  -17.818 12.923  1.00 18.85 ? 48  PRO A CB  1 
ATOM   370  C  CG  . PRO A 1 48  ? -0.413  -16.428 13.553  1.00 18.43 ? 48  PRO A CG  1 
ATOM   371  C  CD  . PRO A 1 48  ? 0.953   -15.969 13.676  1.00 16.27 ? 48  PRO A CD  1 
ATOM   372  N  N   . LEU A 1 49  ? 0.308   -18.367 9.766   1.00 16.62 ? 49  LEU A N   1 
ATOM   373  C  CA  . LEU A 1 49  ? -0.225  -18.148 8.420   1.00 16.60 ? 49  LEU A CA  1 
ATOM   374  C  C   . LEU A 1 49  ? -1.682  -17.633 8.465   1.00 17.43 ? 49  LEU A C   1 
ATOM   375  O  O   . LEU A 1 49  ? -2.496  -18.198 9.208   1.00 17.49 ? 49  LEU A O   1 
ATOM   376  C  CB  . LEU A 1 49  ? -0.069  -19.442 7.552   1.00 16.59 ? 49  LEU A CB  1 
ATOM   377  C  CG  . LEU A 1 49  ? 1.375   -19.944 7.398   1.00 18.67 ? 49  LEU A CG  1 
ATOM   378  C  CD1 . LEU A 1 49  ? 1.351   -21.311 6.650   1.00 16.08 ? 49  LEU A CD1 1 
ATOM   379  C  CD2 . LEU A 1 49  ? 2.260   -18.904 6.707   1.00 19.37 ? 49  LEU A CD2 1 
ATOM   380  N  N   . SER A 1 50  ? -2.056  -16.650 7.629   1.00 16.41 ? 50  SER A N   1 
ATOM   381  C  CA  . SER A 1 50  ? -3.430  -16.314 7.447   1.00 18.31 ? 50  SER A CA  1 
ATOM   382  C  C   . SER A 1 50  ? -3.785  -16.481 5.964   1.00 21.44 ? 50  SER A C   1 
ATOM   383  O  O   . SER A 1 50  ? -3.094  -15.930 5.099   1.00 18.63 ? 50  SER A O   1 
ATOM   384  C  CB  . SER A 1 50  ? -3.768  -14.892 7.971   1.00 22.32 ? 50  SER A CB  1 
ATOM   385  O  OG  . SER A 1 50  ? -3.164  -13.877 7.257   1.00 32.15 ? 50  SER A OG  1 
ATOM   386  N  N   . ILE A 1 51  ? -4.783  -17.277 5.678   1.00 22.25 ? 51  ILE A N   1 
ATOM   387  C  CA  . ILE A 1 51  ? -5.042  -17.770 4.287   1.00 25.08 ? 51  ILE A CA  1 
ATOM   388  C  C   . ILE A 1 51  ? -6.478  -17.626 4.023   1.00 29.56 ? 51  ILE A C   1 
ATOM   389  O  O   . ILE A 1 51  ? -7.359  -18.182 4.761   1.00 28.37 ? 51  ILE A O   1 
ATOM   390  C  CB  . ILE A 1 51  ? -4.558  -19.234 4.077   1.00 26.81 ? 51  ILE A CB  1 
ATOM   391  C  CG1 . ILE A 1 51  ? -3.156  -19.467 4.585   1.00 28.78 ? 51  ILE A CG1 1 
ATOM   392  C  CG2 . ILE A 1 51  ? -4.635  -19.798 2.654   1.00 31.13 ? 51  ILE A CG2 1 
ATOM   393  C  CD1 . ILE A 1 51  ? -2.769  -20.918 4.521   1.00 34.01 ? 51  ILE A CD1 1 
ATOM   394  N  N   A LYS A 1 52  ? -6.744  -17.218 2.793   0.50 23.82 ? 52  LYS A N   1 
ATOM   395  N  N   B LYS A 1 52  ? -6.737  -16.529 3.295   0.50 29.80 ? 52  LYS A N   1 
ATOM   396  C  CA  A LYS A 1 52  ? -8.086  -17.209 2.312   0.50 21.74 ? 52  LYS A CA  1 
ATOM   397  C  CA  B LYS A 1 52  ? -8.006  -16.401 2.646   0.50 26.73 ? 52  LYS A CA  1 
ATOM   398  C  C   A LYS A 1 52  ? -8.029  -17.507 0.868   0.50 20.67 ? 52  LYS A C   1 
ATOM   399  C  C   B LYS A 1 52  ? -7.985  -16.790 1.185   0.50 24.12 ? 52  LYS A C   1 
ATOM   400  O  O   A LYS A 1 52  ? -7.501  -16.709 0.114   0.50 17.38 ? 52  LYS A O   1 
ATOM   401  O  O   B LYS A 1 52  ? -6.936  -16.759 0.477   0.50 19.07 ? 52  LYS A O   1 
ATOM   402  C  CB  A LYS A 1 52  ? -8.698  -15.816 2.437   0.50 19.53 ? 52  LYS A CB  1 
ATOM   403  C  CB  B LYS A 1 52  ? -8.846  -15.169 2.993   0.50 31.73 ? 52  LYS A CB  1 
ATOM   404  C  CG  A LYS A 1 52  ? -7.691  -14.732 2.639   0.50 21.13 ? 52  LYS A CG  1 
ATOM   405  C  CG  B LYS A 1 52  ? -8.604  -13.859 2.298   0.50 32.56 ? 52  LYS A CG  1 
ATOM   406  C  CD  A LYS A 1 52  ? -8.406  -13.605 3.407   0.50 18.02 ? 52  LYS A CD  1 
ATOM   407  C  CD  B LYS A 1 52  ? -9.237  -12.806 3.196   0.50 32.74 ? 52  LYS A CD  1 
ATOM   408  C  CE  A LYS A 1 52  ? -8.240  -12.268 2.693   0.50 19.64 ? 52  LYS A CE  1 
ATOM   409  C  CE  B LYS A 1 52  ? -8.794  -11.395 2.839   0.50 29.96 ? 52  LYS A CE  1 
ATOM   410  N  NZ  A LYS A 1 52  ? -9.118  -12.128 1.480   0.50 20.32 ? 52  LYS A NZ  1 
ATOM   411  N  NZ  B LYS A 1 52  ? -8.881  -10.505 4.022   0.50 24.21 ? 52  LYS A NZ  1 
ATOM   412  N  N   A TYR A 1 53  ? -8.561  -18.647 0.472   0.50 18.62 ? 53  TYR A N   1 
ATOM   413  N  N   B TYR A 1 53  ? -9.161  -17.231 0.804   0.50 20.44 ? 53  TYR A N   1 
ATOM   414  C  CA  A TYR A 1 53  ? -8.716  -18.933 -0.959  0.50 20.29 ? 53  TYR A CA  1 
ATOM   415  C  CA  B TYR A 1 53  ? -9.302  -17.955 -0.408  0.50 21.85 ? 53  TYR A CA  1 
ATOM   416  C  C   A TYR A 1 53  ? -10.227 -19.041 -1.340  0.50 19.30 ? 53  TYR A C   1 
ATOM   417  C  C   B TYR A 1 53  ? -10.703 -18.051 -0.900  0.50 23.14 ? 53  TYR A C   1 
ATOM   418  O  O   A TYR A 1 53  ? -10.887 -19.958 -0.775  0.50 26.14 ? 53  TYR A O   1 
ATOM   419  O  O   B TYR A 1 53  ? -11.683 -18.164 -0.177  0.50 19.68 ? 53  TYR A O   1 
ATOM   420  C  CB  A TYR A 1 53  ? -7.895  -20.204 -1.377  0.50 18.70 ? 53  TYR A CB  1 
ATOM   421  C  CB  B TYR A 1 53  ? -8.749  -19.366 -0.283  0.50 18.78 ? 53  TYR A CB  1 
ATOM   422  C  CG  A TYR A 1 53  ? -6.404  -20.238 -0.993  0.50 16.00 ? 53  TYR A CG  1 
ATOM   423  C  CG  B TYR A 1 53  ? -8.957  -20.167 -1.546  0.50 18.41 ? 53  TYR A CG  1 
ATOM   424  C  CD1 A TYR A 1 53  ? -5.544  -19.138 -1.241  0.50 18.69 ? 53  TYR A CD1 1 
ATOM   425  C  CD1 B TYR A 1 53  ? -8.277  -19.839 -2.730  0.50 15.41 ? 53  TYR A CD1 1 
ATOM   426  C  CD2 A TYR A 1 53  ? -5.832  -21.394 -0.469  0.50 16.55 ? 53  TYR A CD2 1 
ATOM   427  C  CD2 B TYR A 1 53  ? -9.870  -21.189 -1.580  0.50 15.59 ? 53  TYR A CD2 1 
ATOM   428  C  CE1 A TYR A 1 53  ? -4.206  -19.197 -0.920  0.50 15.79 ? 53  TYR A CE1 1 
ATOM   429  C  CE1 B TYR A 1 53  ? -8.499  -20.554 -3.887  0.50 15.43 ? 53  TYR A CE1 1 
ATOM   430  C  CE2 A TYR A 1 53  ? -4.497  -21.430 -0.156  0.50 15.24 ? 53  TYR A CE2 1 
ATOM   431  C  CE2 B TYR A 1 53  ? -10.083 -21.928 -2.735  0.50 15.64 ? 53  TYR A CE2 1 
ATOM   432  C  CZ  A TYR A 1 53  ? -3.671  -20.315 -0.395  0.50 15.46 ? 53  TYR A CZ  1 
ATOM   433  C  CZ  B TYR A 1 53  ? -9.404  -21.579 -3.893  0.50 15.22 ? 53  TYR A CZ  1 
ATOM   434  O  OH  A TYR A 1 53  ? -2.362  -20.384 -0.055  0.50 13.61 ? 53  TYR A OH  1 
ATOM   435  O  OH  B TYR A 1 53  ? -9.608  -22.286 -5.055  0.50 15.98 ? 53  TYR A OH  1 
ATOM   436  N  N   . ASP A 1 54  ? -10.775 -18.108 -2.195  1.00 23.38 ? 54  ASP A N   1 
ATOM   437  C  CA  . ASP A 1 54  ? -12.108 -18.110 -2.794  1.00 23.94 ? 54  ASP A CA  1 
ATOM   438  C  C   . ASP A 1 54  ? -12.182 -19.213 -3.885  1.00 22.51 ? 54  ASP A C   1 
ATOM   439  O  O   . ASP A 1 54  ? -11.405 -19.172 -4.853  1.00 21.36 ? 54  ASP A O   1 
ATOM   440  C  CB  . ASP A 1 54  ? -12.447 -16.776 -3.387  1.00 28.14 ? 54  ASP A CB  1 
ATOM   441  C  CG  . ASP A 1 54  ? -13.910 -16.654 -3.916  1.00 31.51 ? 54  ASP A CG  1 
ATOM   442  O  OD1 . ASP A 1 54  ? -14.616 -17.653 -4.109  1.00 25.84 ? 54  ASP A OD1 1 
ATOM   443  O  OD2 . ASP A 1 54  ? -14.285 -15.501 -4.133  1.00 43.66 ? 54  ASP A OD2 1 
ATOM   444  N  N   . PRO A 1 55  ? -12.988 -20.230 -3.643  1.00 21.39 ? 55  PRO A N   1 
ATOM   445  C  CA  . PRO A 1 55  ? -13.105 -21.331 -4.630  1.00 20.11 ? 55  PRO A CA  1 
ATOM   446  C  C   . PRO A 1 55  ? -13.497 -20.898 -6.006  1.00 21.93 ? 55  PRO A C   1 
ATOM   447  O  O   . PRO A 1 55  ? -13.199 -21.628 -6.936  1.00 20.43 ? 55  PRO A O   1 
ATOM   448  C  CB  . PRO A 1 55  ? -14.153 -22.287 -4.046  1.00 19.03 ? 55  PRO A CB  1 
ATOM   449  C  CG  . PRO A 1 55  ? -14.225 -21.914 -2.577  1.00 21.80 ? 55  PRO A CG  1 
ATOM   450  C  CD  . PRO A 1 55  ? -13.885 -20.432 -2.484  1.00 20.27 ? 55  PRO A CD  1 
ATOM   451  N  N   . SER A 1 56  ? -14.177 -19.758 -6.161  1.00 20.04 ? 56  SER A N   1 
ATOM   452  C  CA  . SER A 1 56  ? -14.584 -19.346 -7.490  1.00 22.45 ? 56  SER A CA  1 
ATOM   453  C  C   . SER A 1 56  ? -13.375 -18.632 -8.170  1.00 21.89 ? 56  SER A C   1 
ATOM   454  O  O   . SER A 1 56  ? -13.504 -18.263 -9.317  1.00 22.18 ? 56  SER A O   1 
ATOM   455  C  CB  . SER A 1 56  ? -15.808 -18.395 -7.434  1.00 26.36 ? 56  SER A CB  1 
ATOM   456  O  OG  . SER A 1 56  ? -15.393 -17.117 -6.940  1.00 31.26 ? 56  SER A OG  1 
ATOM   457  N  N   . SER A 1 57  ? -12.240 -18.415 -7.453  1.00 17.43 ? 57  SER A N   1 
ATOM   458  C  CA  . SER A 1 57  ? -11.003 -17.740 -7.970  1.00 18.64 ? 57  SER A CA  1 
ATOM   459  C  C   . SER A 1 57  ? -10.343 -18.642 -9.057  1.00 18.63 ? 57  SER A C   1 
ATOM   460  O  O   . SER A 1 57  ? -9.619  -18.153 -9.975  1.00 18.68 ? 57  SER A O   1 
ATOM   461  C  CB  . SER A 1 57  ? -9.912  -17.568 -6.862  1.00 21.71 ? 57  SER A CB  1 
ATOM   462  O  OG  . SER A 1 57  ? -10.130 -16.376 -6.138  1.00 36.34 ? 57  SER A OG  1 
ATOM   463  N  N   . ALA A 1 58  ? -10.517 -19.949 -8.926  1.00 19.02 ? 58  ALA A N   1 
ATOM   464  C  CA  . ALA A 1 58  ? -9.926  -20.844 -9.928  1.00 19.36 ? 58  ALA A CA  1 
ATOM   465  C  C   . ALA A 1 58  ? -10.575 -20.687 -11.307 1.00 17.39 ? 58  ALA A C   1 
ATOM   466  O  O   . ALA A 1 58  ? -11.751 -20.564 -11.439 1.00 18.56 ? 58  ALA A O   1 
ATOM   467  C  CB  . ALA A 1 58  ? -10.030 -22.275 -9.471  1.00 19.83 ? 58  ALA A CB  1 
ATOM   468  N  N   . LYS A 1 59  ? -9.742  -20.730 -12.355 1.00 16.06 ? 59  LYS A N   1 
ATOM   469  C  CA  . LYS A 1 59  ? -10.291 -20.524 -13.688 1.00 17.83 ? 59  LYS A CA  1 
ATOM   470  C  C   . LYS A 1 59  ? -10.079 -21.761 -14.597 1.00 16.92 ? 59  LYS A C   1 
ATOM   471  O  O   . LYS A 1 59  ? -10.975 -22.106 -15.315 1.00 15.57 ? 59  LYS A O   1 
ATOM   472  C  CB  . LYS A 1 59  ? -9.531  -19.416 -14.452 1.00 23.05 ? 59  LYS A CB  1 
ATOM   473  C  CG  . LYS A 1 59  ? -9.315  -18.043 -13.853 1.00 29.95 ? 59  LYS A CG  1 
ATOM   474  C  CD  . LYS A 1 59  ? -8.654  -17.143 -14.931 1.00 30.43 ? 59  LYS A CD  1 
ATOM   475  C  CE  . LYS A 1 59  ? -7.158  -17.276 -14.992 1.00 33.75 ? 59  LYS A CE  1 
ATOM   476  N  NZ  . LYS A 1 59  ? -6.551  -16.222 -15.894 1.00 37.53 ? 59  LYS A NZ  1 
ATOM   477  N  N   . ILE A 1 60  ? -8.827  -22.285 -14.659 1.00 15.17 ? 60  ILE A N   1 
ATOM   478  C  CA  . ILE A 1 60  ? -8.535  -23.353 -15.664 1.00 15.02 ? 60  ILE A CA  1 
ATOM   479  C  C   . ILE A 1 60  ? -7.453  -24.263 -15.112 1.00 13.08 ? 60  ILE A C   1 
ATOM   480  O  O   . ILE A 1 60  ? -6.710  -23.873 -14.175 1.00 13.70 ? 60  ILE A O   1 
ATOM   481  C  CB  . ILE A 1 60  ? -7.960  -22.792 -17.037 1.00 18.19 ? 60  ILE A CB  1 
ATOM   482  C  CG1 . ILE A 1 60  ? -6.746  -21.925 -16.783 1.00 18.49 ? 60  ILE A CG1 1 
ATOM   483  C  CG2 . ILE A 1 60  ? -9.001  -21.948 -17.783 1.00 22.25 ? 60  ILE A CG2 1 
ATOM   484  C  CD1 . ILE A 1 60  ? -5.785  -21.909 -17.966 1.00 29.41 ? 60  ILE A CD1 1 
ATOM   485  N  N   . ILE A 1 61  ? -7.338  -25.482 -15.715 1.00 13.28 ? 61  ILE A N   1 
ATOM   486  C  CA  . ILE A 1 61  ? -6.190  -26.376 -15.421 1.00 12.06 ? 61  ILE A CA  1 
ATOM   487  C  C   . ILE A 1 61  ? -5.559  -26.707 -16.784 1.00 12.07 ? 61  ILE A C   1 
ATOM   488  O  O   . ILE A 1 61  ? -6.248  -26.888 -17.771 1.00 12.36 ? 61  ILE A O   1 
ATOM   489  C  CB  . ILE A 1 61  ? -6.693  -27.632 -14.622 1.00 11.77 ? 61  ILE A CB  1 
ATOM   490  C  CG1 . ILE A 1 61  ? -5.491  -28.429 -14.159 1.00 13.45 ? 61  ILE A CG1 1 
ATOM   491  C  CG2 . ILE A 1 61  ? -7.615  -28.519 -15.440 1.00 13.37 ? 61  ILE A CG2 1 
ATOM   492  C  CD1 . ILE A 1 61  ? -5.852  -29.619 -13.272 1.00 13.22 ? 61  ILE A CD1 1 
ATOM   493  N  N   A SER A 1 62  ? -4.270  -26.743 -16.836 0.50 11.90 ? 62  SER A N   1 
ATOM   494  N  N   B SER A 1 62  ? -4.247  -26.732 -16.743 0.50 12.05 ? 62  SER A N   1 
ATOM   495  C  CA  A SER A 1 62  ? -3.590  -26.964 -18.089 0.50 13.10 ? 62  SER A CA  1 
ATOM   496  C  CA  B SER A 1 62  ? -3.371  -26.844 -17.897 0.50 12.96 ? 62  SER A CA  1 
ATOM   497  C  C   A SER A 1 62  ? -2.471  -27.956 -17.791 0.50 12.03 ? 62  SER A C   1 
ATOM   498  C  C   B SER A 1 62  ? -2.223  -27.840 -17.739 0.50 11.88 ? 62  SER A C   1 
ATOM   499  O  O   A SER A 1 62  ? -2.078  -28.165 -16.668 0.50 12.27 ? 62  SER A O   1 
ATOM   500  O  O   B SER A 1 62  ? -1.517  -27.910 -16.684 0.50 10.59 ? 62  SER A O   1 
ATOM   501  C  CB  A SER A 1 62  ? -3.037  -25.616 -18.625 0.50 12.47 ? 62  SER A CB  1 
ATOM   502  C  CB  B SER A 1 62  ? -2.804  -25.492 -18.289 0.50 12.41 ? 62  SER A CB  1 
ATOM   503  O  OG  A SER A 1 62  ? -1.948  -25.133 -17.863 0.50 14.06 ? 62  SER A OG  1 
ATOM   504  O  OG  B SER A 1 62  ? -1.997  -25.668 -19.420 0.50 15.10 ? 62  SER A OG  1 
ATOM   505  N  N   . ASN A 1 63  ? -1.945  -28.539 -18.853 1.00 13.11 ? 63  ASN A N   1 
ATOM   506  C  CA  . ASN A 1 63  ? -0.746  -29.354 -18.837 1.00 12.48 ? 63  ASN A CA  1 
ATOM   507  C  C   . ASN A 1 63  ? 0.382   -28.533 -19.398 1.00 12.85 ? 63  ASN A C   1 
ATOM   508  O  O   . ASN A 1 63  ? 0.403   -28.236 -20.609 1.00 14.02 ? 63  ASN A O   1 
ATOM   509  C  CB  . ASN A 1 63  ? -0.935  -30.570 -19.702 1.00 12.37 ? 63  ASN A CB  1 
ATOM   510  C  CG  . ASN A 1 63  ? 0.317   -31.493 -19.723 1.00 13.36 ? 63  ASN A CG  1 
ATOM   511  O  OD1 . ASN A 1 63  ? 1.398   -31.153 -19.188 1.00 14.29 ? 63  ASN A OD1 1 
ATOM   512  N  ND2 . ASN A 1 63  ? 0.174   -32.681 -20.337 1.00 12.68 ? 63  ASN A ND2 1 
ATOM   513  N  N   . SER A 1 64  ? 1.324   -28.164 -18.571 1.00 12.25 ? 64  SER A N   1 
ATOM   514  C  CA  . SER A 1 64  ? 2.458   -27.310 -19.059 1.00 12.68 ? 64  SER A CA  1 
ATOM   515  C  C   . SER A 1 64  ? 3.522   -28.120 -19.772 1.00 14.00 ? 64  SER A C   1 
ATOM   516  O  O   . SER A 1 64  ? 4.457   -27.534 -20.302 1.00 16.51 ? 64  SER A O   1 
ATOM   517  C  CB  . SER A 1 64  ? 3.077   -26.578 -17.834 1.00 14.33 ? 64  SER A CB  1 
ATOM   518  O  OG  . SER A 1 64  ? 3.790   -27.502 -16.962 1.00 12.89 ? 64  SER A OG  1 
ATOM   519  N  N   . GLY A 1 65  ? 3.408   -29.476 -19.663 1.00 12.83 ? 65  GLY A N   1 
ATOM   520  C  CA  . GLY A 1 65  ? 4.422   -30.447 -20.050 1.00 12.72 ? 65  GLY A CA  1 
ATOM   521  C  C   . GLY A 1 65  ? 5.445   -30.699 -18.921 1.00 13.32 ? 65  GLY A C   1 
ATOM   522  O  O   . GLY A 1 65  ? 6.256   -31.618 -19.011 1.00 14.24 ? 65  GLY A O   1 
ATOM   523  N  N   . HIS A 1 66  ? 5.270   -29.959 -17.828 1.00 12.65 ? 66  HIS A N   1 
ATOM   524  C  CA  . HIS A 1 66  ? 6.133   -30.110 -16.655 1.00 12.00 ? 66  HIS A CA  1 
ATOM   525  C  C   . HIS A 1 66  ? 5.432   -30.480 -15.370 1.00 11.93 ? 66  HIS A C   1 
ATOM   526  O  O   . HIS A 1 66  ? 6.061   -30.954 -14.411 1.00 11.47 ? 66  HIS A O   1 
ATOM   527  C  CB  . HIS A 1 66  ? 6.906   -28.797 -16.401 1.00 13.94 ? 66  HIS A CB  1 
ATOM   528  C  CG  . HIS A 1 66  ? 7.611   -28.278 -17.647 1.00 16.53 ? 66  HIS A CG  1 
ATOM   529  N  ND1 . HIS A 1 66  ? 8.645   -28.937 -18.268 1.00 18.29 ? 66  HIS A ND1 1 
ATOM   530  C  CD2 . HIS A 1 66  ? 7.367   -27.124 -18.382 1.00 17.21 ? 66  HIS A CD2 1 
ATOM   531  C  CE1 . HIS A 1 66  ? 9.017   -28.198 -19.354 1.00 19.24 ? 66  HIS A CE1 1 
ATOM   532  N  NE2 . HIS A 1 66  ? 8.247   -27.105 -19.402 1.00 19.29 ? 66  HIS A NE2 1 
ATOM   533  N  N   . SER A 1 67  ? 4.164   -30.199 -15.362 1.00 11.24 ? 67  SER A N   1 
ATOM   534  C  CA  . SER A 1 67  ? 3.171   -30.546 -14.284 1.00 11.61 ? 67  SER A CA  1 
ATOM   535  C  C   . SER A 1 67  ? 1.802   -30.232 -14.864 1.00 12.81 ? 67  SER A C   1 
ATOM   536  O  O   . SER A 1 67  ? 1.675   -29.843 -16.023 1.00 12.27 ? 67  SER A O   1 
ATOM   537  C  CB  . SER A 1 67  ? 3.471   -29.682 -13.019 1.00 11.74 ? 67  SER A CB  1 
ATOM   538  O  OG  . SER A 1 67  ? 2.634   -30.234 -11.979 1.00 12.33 ? 67  SER A OG  1 
ATOM   539  N  N   . PHE A 1 68  ? 0.740   -30.308 -14.041 1.00 10.80 ? 68  PHE A N   1 
ATOM   540  C  CA  . PHE A 1 68  ? -0.538  -29.589 -14.299 1.00 13.56 ? 68  PHE A CA  1 
ATOM   541  C  C   . PHE A 1 68  ? -0.417  -28.234 -13.544 1.00 12.45 ? 68  PHE A C   1 
ATOM   542  O  O   . PHE A 1 68  ? 0.264   -28.170 -12.487 1.00 12.75 ? 68  PHE A O   1 
ATOM   543  C  CB  . PHE A 1 68  ? -1.788  -30.372 -13.793 1.00 14.34 ? 68  PHE A CB  1 
ATOM   544  C  CG  . PHE A 1 68  ? -1.950  -30.390 -12.278 1.00 12.89 ? 68  PHE A CG  1 
ATOM   545  C  CD1 . PHE A 1 68  ? -1.460  -31.461 -11.574 1.00 14.97 ? 68  PHE A CD1 1 
ATOM   546  C  CD2 . PHE A 1 68  ? -2.556  -29.344 -11.576 1.00 13.81 ? 68  PHE A CD2 1 
ATOM   547  C  CE1 . PHE A 1 68  ? -1.635  -31.542 -10.196 1.00 15.31 ? 68  PHE A CE1 1 
ATOM   548  C  CE2 . PHE A 1 68  ? -2.615  -29.367 -10.165 1.00 13.85 ? 68  PHE A CE2 1 
ATOM   549  C  CZ  . PHE A 1 68  ? -2.191  -30.501 -9.505  1.00 13.03 ? 68  PHE A CZ  1 
ATOM   550  N  N   A ASN A 1 69  ? -1.118  -27.224 -14.091 0.50 12.84 ? 69  ASN A N   1 
ATOM   551  N  N   B ASN A 1 69  ? -0.983  -27.156 -14.113 0.50 13.36 ? 69  ASN A N   1 
ATOM   552  C  CA  A ASN A 1 69  ? -1.222  -25.932 -13.418 0.50 13.61 ? 69  ASN A CA  1 
ATOM   553  C  CA  B ASN A 1 69  ? -1.117  -25.921 -13.310 0.50 14.25 ? 69  ASN A CA  1 
ATOM   554  C  C   A ASN A 1 69  ? -2.687  -25.654 -13.298 0.50 12.31 ? 69  ASN A C   1 
ATOM   555  C  C   B ASN A 1 69  ? -2.556  -25.487 -13.277 0.50 13.18 ? 69  ASN A C   1 
ATOM   556  O  O   A ASN A 1 69  ? -3.444  -25.694 -14.297 0.50 11.06 ? 69  ASN A O   1 
ATOM   557  O  O   B ASN A 1 69  ? -3.156  -25.244 -14.312 0.50 12.41 ? 69  ASN A O   1 
ATOM   558  C  CB  A ASN A 1 69  ? -0.593  -24.834 -14.319 0.50 14.73 ? 69  ASN A CB  1 
ATOM   559  C  CB  B ASN A 1 69  ? -0.201  -24.746 -13.806 0.50 16.21 ? 69  ASN A CB  1 
ATOM   560  C  CG  A ASN A 1 69  ? 0.936   -24.755 -14.228 0.50 17.75 ? 69  ASN A CG  1 
ATOM   561  C  CG  B ASN A 1 69  ? 0.446   -24.958 -15.201 0.50 19.54 ? 69  ASN A CG  1 
ATOM   562  O  OD1 A ASN A 1 69  ? 1.592   -24.436 -15.237 0.50 25.42 ? 69  ASN A OD1 1 
ATOM   563  O  OD1 B ASN A 1 69  ? -0.195  -25.393 -16.125 0.50 19.86 ? 69  ASN A OD1 1 
ATOM   564  N  ND2 A ASN A 1 69  ? 1.511   -25.012 -13.062 0.50 19.10 ? 69  ASN A ND2 1 
ATOM   565  N  ND2 B ASN A 1 69  ? 1.740   -24.548 -15.349 0.50 21.35 ? 69  ASN A ND2 1 
ATOM   566  N  N   . VAL A 1 70  ? -3.118  -25.304 -12.075 1.00 13.50 ? 70  VAL A N   1 
ATOM   567  C  CA  . VAL A 1 70  ? -4.471  -24.670 -11.955 1.00 12.58 ? 70  VAL A CA  1 
ATOM   568  C  C   . VAL A 1 70  ? -4.150  -23.157 -11.839 1.00 11.00 ? 70  VAL A C   1 
ATOM   569  O  O   . VAL A 1 70  ? -3.357  -22.773 -10.978 1.00 11.45 ? 70  VAL A O   1 
ATOM   570  C  CB  . VAL A 1 70  ? -5.194  -25.159 -10.702 1.00 12.41 ? 70  VAL A CB  1 
ATOM   571  C  CG1 . VAL A 1 70  ? -6.531  -24.404 -10.514 1.00 13.32 ? 70  VAL A CG1 1 
ATOM   572  C  CG2 . VAL A 1 70  ? -5.505  -26.658 -10.817 1.00 16.36 ? 70  VAL A CG2 1 
ATOM   573  N  N   . ASP A 1 71  ? -4.690  -22.341 -12.706 1.00 12.15 ? 71  ASP A N   1 
ATOM   574  C  CA  . ASP A 1 71  ? -4.453  -20.852 -12.668 1.00 13.58 ? 71  ASP A CA  1 
ATOM   575  C  C   . ASP A 1 71  ? -5.698  -20.149 -12.047 1.00 13.67 ? 71  ASP A C   1 
ATOM   576  O  O   . ASP A 1 71  ? -6.800  -20.614 -12.195 1.00 15.25 ? 71  ASP A O   1 
ATOM   577  C  CB  . ASP A 1 71  ? -4.205  -20.297 -14.082 1.00 17.09 ? 71  ASP A CB  1 
ATOM   578  C  CG  . ASP A 1 71  ? -2.905  -20.767 -14.682 1.00 21.30 ? 71  ASP A CG  1 
ATOM   579  O  OD1 . ASP A 1 71  ? -1.945  -21.079 -13.994 1.00 22.83 ? 71  ASP A OD1 1 
ATOM   580  O  OD2 . ASP A 1 71  ? -2.864  -20.819 -15.915 1.00 28.00 ? 71  ASP A OD2 1 
ATOM   581  N  N   . PHE A 1 72  ? -5.430  -19.067 -11.329 1.00 15.07 ? 72  PHE A N   1 
ATOM   582  C  CA  . PHE A 1 72  ? -6.511  -18.346 -10.628 1.00 13.88 ? 72  PHE A CA  1 
ATOM   583  C  C   . PHE A 1 72  ? -6.535  -16.886 -11.129 1.00 14.48 ? 72  PHE A C   1 
ATOM   584  O  O   . PHE A 1 72  ? -5.506  -16.286 -11.521 1.00 17.00 ? 72  PHE A O   1 
ATOM   585  C  CB  . PHE A 1 72  ? -6.242  -18.314 -9.100  1.00 14.36 ? 72  PHE A CB  1 
ATOM   586  C  CG  . PHE A 1 72  ? -6.164  -19.675 -8.493  1.00 14.55 ? 72  PHE A CG  1 
ATOM   587  C  CD1 . PHE A 1 72  ? -4.987  -20.471 -8.625  1.00 15.08 ? 72  PHE A CD1 1 
ATOM   588  C  CD2 . PHE A 1 72  ? -7.255  -20.186 -7.813  1.00 15.28 ? 72  PHE A CD2 1 
ATOM   589  C  CE1 . PHE A 1 72  ? -4.989  -21.781 -8.076  1.00 13.62 ? 72  PHE A CE1 1 
ATOM   590  C  CE2 . PHE A 1 72  ? -7.236  -21.467 -7.256  1.00 15.55 ? 72  PHE A CE2 1 
ATOM   591  C  CZ  . PHE A 1 72  ? -6.089  -22.225 -7.380  1.00 15.69 ? 72  PHE A CZ  1 
ATOM   592  N  N   A ASP A 1 73  ? -7.737  -16.307 -11.058 0.50 18.58 ? 73  ASP A N   1 
ATOM   593  N  N   B ASP A 1 73  ? -7.743  -16.323 -11.093 0.50 17.61 ? 73  ASP A N   1 
ATOM   594  C  CA  A ASP A 1 73  ? -7.936  -14.864 -11.297 0.50 18.65 ? 73  ASP A CA  1 
ATOM   595  C  CA  B ASP A 1 73  ? -7.944  -14.882 -11.309 0.50 17.09 ? 73  ASP A CA  1 
ATOM   596  C  C   A ASP A 1 73  ? -7.150  -14.156 -10.238 0.50 18.31 ? 73  ASP A C   1 
ATOM   597  C  C   B ASP A 1 73  ? -7.128  -14.191 -10.251 0.50 17.19 ? 73  ASP A C   1 
ATOM   598  O  O   A ASP A 1 73  ? -7.306  -14.470 -9.060  0.50 19.80 ? 73  ASP A O   1 
ATOM   599  O  O   B ASP A 1 73  ? -7.237  -14.562 -9.081  0.50 17.95 ? 73  ASP A O   1 
ATOM   600  C  CB  A ASP A 1 73  ? -9.414  -14.498 -11.095 0.50 21.86 ? 73  ASP A CB  1 
ATOM   601  C  CB  B ASP A 1 73  ? -9.424  -14.545 -11.067 0.50 18.51 ? 73  ASP A CB  1 
ATOM   602  C  CG  A ASP A 1 73  ? -9.694  -13.004 -11.319 0.50 26.23 ? 73  ASP A CG  1 
ATOM   603  C  CG  B ASP A 1 73  ? -10.298 -14.836 -12.276 0.50 21.52 ? 73  ASP A CG  1 
ATOM   604  O  OD1 A ASP A 1 73  ? -8.857  -12.157 -10.980 0.50 29.29 ? 73  ASP A OD1 1 
ATOM   605  O  OD1 B ASP A 1 73  ? -9.783  -14.833 -13.412 0.50 23.56 ? 73  ASP A OD1 1 
ATOM   606  O  OD2 A ASP A 1 73  ? -10.787 -12.680 -11.855 0.50 34.86 ? 73  ASP A OD2 1 
ATOM   607  O  OD2 B ASP A 1 73  ? -11.510 -15.057 -12.092 0.50 24.45 ? 73  ASP A OD2 1 
ATOM   608  N  N   . ASP A 1 74  ? -6.284  -13.229 -10.628 1.00 17.23 ? 74  ASP A N   1 
ATOM   609  C  CA  . ASP A 1 74  ? -5.398  -12.565 -9.666  1.00 17.09 ? 74  ASP A CA  1 
ATOM   610  C  C   . ASP A 1 74  ? -5.449  -11.055 -9.798  1.00 16.30 ? 74  ASP A C   1 
ATOM   611  O  O   . ASP A 1 74  ? -4.390  -10.392 -9.759  1.00 15.66 ? 74  ASP A O   1 
ATOM   612  C  CB  . ASP A 1 74  ? -3.921  -13.083 -9.673  1.00 17.41 ? 74  ASP A CB  1 
ATOM   613  C  CG  . ASP A 1 74  ? -3.198  -12.864 -10.981 1.00 19.11 ? 74  ASP A CG  1 
ATOM   614  O  OD1 . ASP A 1 74  ? -3.900  -12.565 -11.984 1.00 20.81 ? 74  ASP A OD1 1 
ATOM   615  O  OD2 . ASP A 1 74  ? -1.960  -12.995 -10.962 1.00 18.74 ? 74  ASP A OD2 1 
ATOM   616  N  N   . THR A 1 75  ? -6.674  -10.563 -10.000 1.00 19.93 ? 75  THR A N   1 
ATOM   617  C  CA  . THR A 1 75  ? -6.885  -9.076  -10.200 1.00 20.79 ? 75  THR A CA  1 
ATOM   618  C  C   . THR A 1 75  ? -7.336  -8.421  -8.906  1.00 22.56 ? 75  THR A C   1 
ATOM   619  O  O   . THR A 1 75  ? -7.291  -7.188  -8.776  1.00 18.30 ? 75  THR A O   1 
ATOM   620  C  CB  . THR A 1 75  ? -7.932  -8.802  -11.320 1.00 20.81 ? 75  THR A CB  1 
ATOM   621  O  OG1 . THR A 1 75  ? -9.173  -9.351  -10.925 1.00 23.73 ? 75  THR A OG1 1 
ATOM   622  C  CG2 . THR A 1 75  ? -7.564  -9.497  -12.618 1.00 24.87 ? 75  THR A CG2 1 
ATOM   623  N  N   . GLU A 1 76  ? -7.759  -9.222  -7.928  1.00 19.67 ? 76  GLU A N   1 
ATOM   624  C  CA  . GLU A 1 76  ? -8.319  -8.740  -6.649  1.00 21.07 ? 76  GLU A CA  1 
ATOM   625  C  C   . GLU A 1 76  ? -7.598  -9.448  -5.487  1.00 20.37 ? 76  GLU A C   1 
ATOM   626  O  O   . GLU A 1 76  ? -6.818  -10.381 -5.742  1.00 18.20 ? 76  GLU A O   1 
ATOM   627  C  CB  . GLU A 1 76  ? -9.846  -8.986  -6.598  1.00 20.34 ? 76  GLU A CB  1 
ATOM   628  C  CG  . GLU A 1 76  ? -10.649 -8.375  -7.743  1.00 29.56 ? 76  GLU A CG  1 
ATOM   629  C  CD  . GLU A 1 76  ? -12.174 -8.557  -7.627  1.00 35.21 ? 76  GLU A CD  1 
ATOM   630  O  OE1 . GLU A 1 76  ? -12.657 -9.632  -7.246  1.00 43.16 ? 76  GLU A OE1 1 
ATOM   631  O  OE2 . GLU A 1 76  ? -12.903 -7.625  -7.981  1.00 40.23 ? 76  GLU A OE2 1 
ATOM   632  N  N   . ASN A 1 77  ? -7.816  -9.003  -4.235  1.00 17.69 ? 77  ASN A N   1 
ATOM   633  C  CA  . ASN A 1 77  ? -7.233  -9.662  -3.077  1.00 17.57 ? 77  ASN A CA  1 
ATOM   634  C  C   . ASN A 1 77  ? -8.259  -10.628 -2.428  1.00 17.33 ? 77  ASN A C   1 
ATOM   635  O  O   . ASN A 1 77  ? -8.326  -10.680 -1.229  1.00 21.60 ? 77  ASN A O   1 
ATOM   636  C  CB  . ASN A 1 77  ? -6.619  -8.642  -2.081  1.00 18.71 ? 77  ASN A CB  1 
ATOM   637  C  CG  . ASN A 1 77  ? -5.365  -8.043  -2.609  1.00 20.49 ? 77  ASN A CG  1 
ATOM   638  O  OD1 . ASN A 1 77  ? -4.600  -8.724  -3.279  1.00 17.02 ? 77  ASN A OD1 1 
ATOM   639  N  ND2 . ASN A 1 77  ? -5.065  -6.824  -2.208  1.00 19.91 ? 77  ASN A ND2 1 
ATOM   640  N  N   . LYS A 1 78  ? -8.972  -11.390 -3.233  1.00 17.24 ? 78  LYS A N   1 
ATOM   641  C  CA  . LYS A 1 78  ? -9.908  -12.414 -2.717  1.00 16.52 ? 78  LYS A CA  1 
ATOM   642  C  C   . LYS A 1 78  ? -9.124  -13.647 -2.188  1.00 17.03 ? 78  LYS A C   1 
ATOM   643  O  O   . LYS A 1 78  ? -9.555  -14.288 -1.288  1.00 19.29 ? 78  LYS A O   1 
ATOM   644  C  CB  . LYS A 1 78  ? -10.909 -12.863 -3.768  1.00 21.09 ? 78  LYS A CB  1 
ATOM   645  C  CG  . LYS A 1 78  ? -11.818 -11.737 -4.359  1.00 28.33 ? 78  LYS A CG  1 
ATOM   646  C  CD  . LYS A 1 78  ? -12.904 -12.304 -5.313  1.00 31.99 ? 78  LYS A CD  1 
ATOM   647  C  CE  . LYS A 1 78  ? -12.250 -13.209 -6.395  1.00 36.04 ? 78  LYS A CE  1 
ATOM   648  N  NZ  . LYS A 1 78  ? -13.123 -14.080 -7.263  1.00 38.82 ? 78  LYS A NZ  1 
ATOM   649  N  N   . SER A 1 79  ? -8.041  -14.011 -2.884  1.00 15.25 ? 79  SER A N   1 
ATOM   650  C  CA  . SER A 1 79  ? -7.301  -15.233 -2.547  1.00 15.49 ? 79  SER A CA  1 
ATOM   651  C  C   . SER A 1 79  ? -5.908  -14.831 -2.273  1.00 13.67 ? 79  SER A C   1 
ATOM   652  O  O   . SER A 1 79  ? -5.119  -14.517 -3.185  1.00 14.50 ? 79  SER A O   1 
ATOM   653  C  CB  . SER A 1 79  ? -7.427  -16.282 -3.688  1.00 14.59 ? 79  SER A CB  1 
ATOM   654  O  OG  . SER A 1 79  ? -8.761  -16.743 -3.820  1.00 18.24 ? 79  SER A OG  1 
ATOM   655  N  N   . VAL A 1 80  ? -5.536  -14.797 -1.001  1.00 12.94 ? 80  VAL A N   1 
ATOM   656  C  CA  . VAL A 1 80  ? -4.307  -14.207 -0.564  1.00 13.14 ? 80  VAL A CA  1 
ATOM   657  C  C   . VAL A 1 80  ? -3.719  -14.926 0.630   1.00 15.14 ? 80  VAL A C   1 
ATOM   658  O  O   . VAL A 1 80  ? -4.428  -15.543 1.450   1.00 15.67 ? 80  VAL A O   1 
ATOM   659  C  CB  . VAL A 1 80  ? -4.401  -12.707 -0.156  1.00 15.06 ? 80  VAL A CB  1 
ATOM   660  C  CG1 . VAL A 1 80  ? -4.923  -11.833 -1.272  1.00 16.88 ? 80  VAL A CG1 1 
ATOM   661  C  CG2 . VAL A 1 80  ? -5.441  -12.552 0.960   1.00 19.28 ? 80  VAL A CG2 1 
ATOM   662  N  N   . LEU A 1 81  ? -2.436  -14.844 0.735   1.00 12.66 ? 81  LEU A N   1 
ATOM   663  C  CA  . LEU A 1 81  ? -1.639  -15.350 1.823   1.00 12.63 ? 81  LEU A CA  1 
ATOM   664  C  C   . LEU A 1 81  ? -0.922  -14.226 2.547   1.00 15.69 ? 81  LEU A C   1 
ATOM   665  O  O   . LEU A 1 81  ? -0.207  -13.399 1.929   1.00 13.24 ? 81  LEU A O   1 
ATOM   666  C  CB  . LEU A 1 81  ? -0.620  -16.393 1.322   1.00 11.82 ? 81  LEU A CB  1 
ATOM   667  C  CG  . LEU A 1 81  ? 0.485   -16.879 2.262   1.00 12.87 ? 81  LEU A CG  1 
ATOM   668  C  CD1 . LEU A 1 81  ? -0.159  -17.803 3.317   1.00 13.06 ? 81  LEU A CD1 1 
ATOM   669  C  CD2 . LEU A 1 81  ? 1.561   -17.741 1.549   1.00 13.00 ? 81  LEU A CD2 1 
ATOM   670  N  N   . ARG A 1 82  ? -1.102  -14.144 3.864   1.00 16.72 ? 82  ARG A N   1 
ATOM   671  C  CA  . ARG A 1 82  ? -0.422  -13.162 4.710   1.00 14.71 ? 82  ARG A CA  1 
ATOM   672  C  C   . ARG A 1 82  ? 0.124   -13.834 5.948   1.00 14.97 ? 82  ARG A C   1 
ATOM   673  O  O   . ARG A 1 82  ? -0.052  -15.069 6.206   1.00 14.28 ? 82  ARG A O   1 
ATOM   674  C  CB  . ARG A 1 82  ? -1.425  -12.002 5.091   1.00 18.71 ? 82  ARG A CB  1 
ATOM   675  C  CG  . ARG A 1 82  ? -1.987  -11.243 3.870   1.00 22.16 ? 82  ARG A CG  1 
ATOM   676  C  CD  . ARG A 1 82  ? -3.255  -10.406 4.206   1.00 27.20 ? 82  ARG A CD  1 
ATOM   677  N  NE  . ARG A 1 82  ? -4.247  -11.386 4.613   1.00 35.16 ? 82  ARG A NE  1 
ATOM   678  C  CZ  . ARG A 1 82  ? -5.468  -11.161 5.104   1.00 36.01 ? 82  ARG A CZ  1 
ATOM   679  N  NH1 . ARG A 1 82  ? -5.935  -9.926  5.275   1.00 32.78 ? 82  ARG A NH1 1 
ATOM   680  N  NH2 . ARG A 1 82  ? -6.190  -12.226 5.466   1.00 40.05 ? 82  ARG A NH2 1 
ATOM   681  N  N   . GLY A 1 83  ? 0.845   -13.060 6.732   1.00 13.63 ? 83  GLY A N   1 
ATOM   682  C  CA  . GLY A 1 83  ? 1.401   -13.593 7.932   1.00 15.74 ? 83  GLY A CA  1 
ATOM   683  C  C   . GLY A 1 83  ? 2.560   -14.499 7.619   1.00 15.32 ? 83  GLY A C   1 
ATOM   684  O  O   . GLY A 1 83  ? 3.340   -14.258 6.639   1.00 16.76 ? 83  GLY A O   1 
ATOM   685  N  N   . GLY A 1 84  ? 2.781   -15.531 8.412   1.00 17.28 ? 84  GLY A N   1 
ATOM   686  C  CA  . GLY A 1 84  ? 4.080   -16.242 8.302   1.00 20.31 ? 84  GLY A CA  1 
ATOM   687  C  C   . GLY A 1 84  ? 5.310   -15.347 8.441   1.00 18.14 ? 84  GLY A C   1 
ATOM   688  O  O   . GLY A 1 84  ? 5.354   -14.383 9.224   1.00 17.58 ? 84  GLY A O   1 
ATOM   689  N  N   . PRO A 1 85  ? 6.305   -15.517 7.552   1.00 15.82 ? 85  PRO A N   1 
ATOM   690  C  CA  . PRO A 1 85  ? 7.471   -14.693 7.455   1.00 14.86 ? 85  PRO A CA  1 
ATOM   691  C  C   . PRO A 1 85  ? 7.197   -13.446 6.554   1.00 13.91 ? 85  PRO A C   1 
ATOM   692  O  O   . PRO A 1 85  ? 8.095   -12.693 6.279   1.00 17.00 ? 85  PRO A O   1 
ATOM   693  C  CB  . PRO A 1 85  ? 8.495   -15.588 6.679   1.00 13.75 ? 85  PRO A CB  1 
ATOM   694  C  CG  . PRO A 1 85  ? 7.602   -16.376 5.809   1.00 12.94 ? 85  PRO A CG  1 
ATOM   695  C  CD  . PRO A 1 85  ? 6.260   -16.601 6.567   1.00 14.92 ? 85  PRO A CD  1 
ATOM   696  N  N   . LEU A 1 86  ? 5.989   -13.345 6.006   1.00 13.24 ? 86  LEU A N   1 
ATOM   697  C  CA  . LEU A 1 86  ? 5.773   -12.370 4.907   1.00 14.03 ? 86  LEU A CA  1 
ATOM   698  C  C   . LEU A 1 86  ? 5.499   -10.939 5.404   1.00 15.14 ? 86  LEU A C   1 
ATOM   699  O  O   . LEU A 1 86  ? 4.773   -10.768 6.402   1.00 16.38 ? 86  LEU A O   1 
ATOM   700  C  CB  . LEU A 1 86  ? 4.626   -12.831 4.020   1.00 12.73 ? 86  LEU A CB  1 
ATOM   701  C  CG  . LEU A 1 86  ? 4.842   -14.278 3.457   1.00 11.38 ? 86  LEU A CG  1 
ATOM   702  C  CD1 . LEU A 1 86  ? 3.555   -14.718 2.818   1.00 12.21 ? 86  LEU A CD1 1 
ATOM   703  C  CD2 . LEU A 1 86  ? 6.014   -14.254 2.477   1.00 14.75 ? 86  LEU A CD2 1 
ATOM   704  N  N   . THR A 1 87  ? 6.022   -9.973  4.634   1.00 15.92 ? 87  THR A N   1 
ATOM   705  C  CA  . THR A 1 87  ? 5.599   -8.574  4.818   1.00 17.29 ? 87  THR A CA  1 
ATOM   706  C  C   . THR A 1 87  ? 4.574   -8.271  3.727   1.00 16.24 ? 87  THR A C   1 
ATOM   707  O  O   . THR A 1 87  ? 4.943   -8.362  2.526   1.00 17.58 ? 87  THR A O   1 
ATOM   708  C  CB  . THR A 1 87  ? 6.828   -7.682  4.759   1.00 19.23 ? 87  THR A CB  1 
ATOM   709  O  OG1 . THR A 1 87  ? 7.653   -7.941  5.910   1.00 21.97 ? 87  THR A OG1 1 
ATOM   710  C  CG2 . THR A 1 87  ? 6.364   -6.127  4.757   1.00 20.57 ? 87  THR A CG2 1 
ATOM   711  N  N   . GLY A 1 88  ? 3.366   -7.864  4.121   1.00 15.56 ? 88  GLY A N   1 
ATOM   712  C  CA  . GLY A 1 88  ? 2.272   -7.536  3.195   1.00 16.88 ? 88  GLY A CA  1 
ATOM   713  C  C   . GLY A 1 88  ? 1.519   -8.732  2.645   1.00 17.92 ? 88  GLY A C   1 
ATOM   714  O  O   . GLY A 1 88  ? 1.629   -9.833  3.185   1.00 17.50 ? 88  GLY A O   1 
ATOM   715  N  N   . SER A 1 89  ? 0.810   -8.494  1.551   1.00 15.56 ? 89  SER A N   1 
ATOM   716  C  CA  . SER A 1 89  ? -0.171  -9.420  1.009   1.00 16.50 ? 89  SER A CA  1 
ATOM   717  C  C   . SER A 1 89  ? 0.302   -10.097 -0.293  1.00 15.14 ? 89  SER A C   1 
ATOM   718  O  O   . SER A 1 89  ? 0.677   -9.400  -1.271  1.00 14.22 ? 89  SER A O   1 
ATOM   719  C  CB  . SER A 1 89  ? -1.503  -8.700  0.740   1.00 19.27 ? 89  SER A CB  1 
ATOM   720  O  OG  . SER A 1 89  ? -2.547  -9.571  0.374   1.00 18.52 ? 89  SER A OG  1 
ATOM   721  N  N   . TYR A 1 90  ? 0.252   -11.442 -0.315  1.00 12.73 ? 90  TYR A N   1 
ATOM   722  C  CA  . TYR A 1 90  ? 0.728   -12.206 -1.496  1.00 13.44 ? 90  TYR A CA  1 
ATOM   723  C  C   . TYR A 1 90  ? -0.414  -12.880 -2.183  1.00 13.84 ? 90  TYR A C   1 
ATOM   724  O  O   . TYR A 1 90  ? -1.179  -13.662 -1.550  1.00 14.07 ? 90  TYR A O   1 
ATOM   725  C  CB  . TYR A 1 90  ? 1.858   -13.217 -1.055  1.00 12.10 ? 90  TYR A CB  1 
ATOM   726  C  CG  . TYR A 1 90  ? 3.206   -12.613 -0.757  1.00 13.70 ? 90  TYR A CG  1 
ATOM   727  C  CD1 . TYR A 1 90  ? 3.412   -11.738 0.362   1.00 12.44 ? 90  TYR A CD1 1 
ATOM   728  C  CD2 . TYR A 1 90  ? 4.265   -12.828 -1.620  1.00 11.18 ? 90  TYR A CD2 1 
ATOM   729  C  CE1 . TYR A 1 90  ? 4.637   -11.131 0.604   1.00 12.52 ? 90  TYR A CE1 1 
ATOM   730  C  CE2 . TYR A 1 90  ? 5.499   -12.259 -1.404  1.00 12.94 ? 90  TYR A CE2 1 
ATOM   731  C  CZ  . TYR A 1 90  ? 5.670   -11.382 -0.293  1.00 12.78 ? 90  TYR A CZ  1 
ATOM   732  O  OH  . TYR A 1 90  ? 6.853   -10.824 -0.114  1.00 14.71 ? 90  TYR A OH  1 
ATOM   733  N  N   . ARG A 1 91  ? -0.715  -12.523 -3.447  1.00 12.05 ? 91  ARG A N   1 
ATOM   734  C  CA  . ARG A 1 91  ? -1.850  -12.916 -4.124  1.00 12.32 ? 91  ARG A CA  1 
ATOM   735  C  C   . ARG A 1 91  ? -1.717  -14.303 -4.842  1.00 11.41 ? 91  ARG A C   1 
ATOM   736  O  O   . ARG A 1 91  ? -0.648  -14.567 -5.444  1.00 13.03 ? 91  ARG A O   1 
ATOM   737  C  CB  . ARG A 1 91  ? -2.147  -11.771 -5.126  1.00 13.18 ? 91  ARG A CB  1 
ATOM   738  C  CG  . ARG A 1 91  ? -3.502  -11.982 -5.735  1.00 12.54 ? 91  ARG A CG  1 
ATOM   739  C  CD  . ARG A 1 91  ? -3.869  -10.844 -6.752  1.00 15.60 ? 91  ARG A CD  1 
ATOM   740  N  NE  . ARG A 1 91  ? -3.961  -9.572  -6.027  1.00 14.84 ? 91  ARG A NE  1 
ATOM   741  C  CZ  . ARG A 1 91  ? -3.849  -8.372  -6.647  1.00 14.82 ? 91  ARG A CZ  1 
ATOM   742  N  NH1 . ARG A 1 91  ? -3.606  -8.293  -7.969  1.00 16.07 ? 91  ARG A NH1 1 
ATOM   743  N  NH2 . ARG A 1 91  ? -3.906  -7.275  -5.900  1.00 15.23 ? 91  ARG A NH2 1 
ATOM   744  N  N   . LEU A 1 92  ? -2.704  -15.182 -4.640  1.00 11.98 ? 92  LEU A N   1 
ATOM   745  C  CA  . LEU A 1 92  ? -2.670  -16.523 -5.222  1.00 12.03 ? 92  LEU A CA  1 
ATOM   746  C  C   . LEU A 1 92  ? -2.609  -16.387 -6.764  1.00 13.57 ? 92  LEU A C   1 
ATOM   747  O  O   . LEU A 1 92  ? -3.453  -15.720 -7.415  1.00 12.42 ? 92  LEU A O   1 
ATOM   748  C  CB  . LEU A 1 92  ? -3.958  -17.293 -4.806  1.00 12.54 ? 92  LEU A CB  1 
ATOM   749  C  CG  . LEU A 1 92  ? -4.064  -18.696 -5.439  1.00 12.39 ? 92  LEU A CG  1 
ATOM   750  C  CD1 . LEU A 1 92  ? -2.904  -19.629 -5.029  1.00 13.44 ? 92  LEU A CD1 1 
ATOM   751  C  CD2 . LEU A 1 92  ? -5.376  -19.256 -4.931  1.00 13.85 ? 92  LEU A CD2 1 
ATOM   752  N  N   . ARG A 1 93  ? -1.643  -17.164 -7.360  1.00 13.40 ? 93  ARG A N   1 
ATOM   753  C  CA  . ARG A 1 93  ? -1.540  -17.249 -8.850  1.00 13.81 ? 93  ARG A CA  1 
ATOM   754  C  C   . ARG A 1 93  ? -1.817  -18.593 -9.465  1.00 12.24 ? 93  ARG A C   1 
ATOM   755  O  O   . ARG A 1 93  ? -2.636  -18.729 -10.389 1.00 13.28 ? 93  ARG A O   1 
ATOM   756  C  CB  . ARG A 1 93  ? -0.138  -16.826 -9.162  1.00 15.43 ? 93  ARG A CB  1 
ATOM   757  C  CG  . ARG A 1 93  ? 0.329   -16.922 -10.647 1.00 21.96 ? 93  ARG A CG  1 
ATOM   758  C  CD  . ARG A 1 93  ? -0.539  -16.163 -11.595 1.00 27.09 ? 93  ARG A CD  1 
ATOM   759  N  NE  . ARG A 1 93  ? 0.225   -15.964 -12.853 1.00 24.80 ? 93  ARG A NE  1 
ATOM   760  C  CZ  . ARG A 1 93  ? -0.026  -14.982 -13.734 1.00 30.15 ? 93  ARG A CZ  1 
ATOM   761  N  NH1 . ARG A 1 93  ? -1.014  -14.110 -13.525 1.00 27.65 ? 93  ARG A NH1 1 
ATOM   762  N  NH2 . ARG A 1 93  ? 0.763   -14.869 -14.848 1.00 34.25 ? 93  ARG A NH2 1 
ATOM   763  N  N   . GLN A 1 94  ? -1.261  -19.622 -8.831  1.00 11.56 ? 94  GLN A N   1 
ATOM   764  C  CA  . GLN A 1 94  ? -1.486  -20.963 -9.389  1.00 12.83 ? 94  GLN A CA  1 
ATOM   765  C  C   . GLN A 1 94  ? -1.071  -22.040 -8.369  1.00 11.68 ? 94  GLN A C   1 
ATOM   766  O  O   . GLN A 1 94  ? -0.335  -21.773 -7.412  1.00 11.86 ? 94  GLN A O   1 
ATOM   767  C  CB  . GLN A 1 94  ? -0.671  -21.156 -10.676 1.00 15.33 ? 94  GLN A CB  1 
ATOM   768  C  CG  . GLN A 1 94  ? 0.806   -21.017 -10.544 1.00 15.09 ? 94  GLN A CG  1 
ATOM   769  C  CD  . GLN A 1 94  ? 1.465   -22.418 -10.660 1.00 19.47 ? 94  GLN A CD  1 
ATOM   770  O  OE1 . GLN A 1 94  ? 1.635   -23.090 -9.665  1.00 19.38 ? 94  GLN A OE1 1 
ATOM   771  N  NE2 . GLN A 1 94  ? 1.966   -22.770 -11.828 1.00 19.25 ? 94  GLN A NE2 1 
ATOM   772  N  N   . VAL A 1 95  ? -1.516  -23.260 -8.714  1.00 11.40 ? 95  VAL A N   1 
ATOM   773  C  CA  . VAL A 1 95  ? -1.108  -24.483 -7.936  1.00 11.63 ? 95  VAL A CA  1 
ATOM   774  C  C   . VAL A 1 95  ? -0.604  -25.532 -8.918  1.00 10.89 ? 95  VAL A C   1 
ATOM   775  O  O   . VAL A 1 95  ? -1.152  -25.686 -10.012 1.00 12.14 ? 95  VAL A O   1 
ATOM   776  C  CB  . VAL A 1 95  ? -2.355  -25.029 -7.209  1.00 12.99 ? 95  VAL A CB  1 
ATOM   777  C  CG1 . VAL A 1 95  ? -2.109  -26.440 -6.621  1.00 13.55 ? 95  VAL A CG1 1 
ATOM   778  C  CG2 . VAL A 1 95  ? -2.790  -24.000 -6.168  1.00 15.73 ? 95  VAL A CG2 1 
ATOM   779  N  N   . HIS A 1 96  ? 0.388   -26.307 -8.508  1.00 9.99  ? 96  HIS A N   1 
ATOM   780  C  CA  . HIS A 1 96  ? 0.836   -27.421 -9.353  1.00 10.57 ? 96  HIS A CA  1 
ATOM   781  C  C   . HIS A 1 96  ? 1.422   -28.514 -8.400  1.00 11.28 ? 96  HIS A C   1 
ATOM   782  O  O   . HIS A 1 96  ? 1.433   -28.324 -7.176  1.00 11.54 ? 96  HIS A O   1 
ATOM   783  C  CB  . HIS A 1 96  ? 1.868   -26.974 -10.412 1.00 11.78 ? 96  HIS A CB  1 
ATOM   784  C  CG  . HIS A 1 96  ? 3.141   -26.428 -9.748  1.00 10.48 ? 96  HIS A CG  1 
ATOM   785  N  ND1 . HIS A 1 96  ? 3.267   -25.138 -9.392  1.00 10.63 ? 96  HIS A ND1 1 
ATOM   786  C  CD2 . HIS A 1 96  ? 4.291   -27.080 -9.273  1.00 9.17  ? 96  HIS A CD2 1 
ATOM   787  C  CE1 . HIS A 1 96  ? 4.471   -24.946 -8.790  1.00 10.11 ? 96  HIS A CE1 1 
ATOM   788  N  NE2 . HIS A 1 96  ? 5.082   -26.133 -8.700  1.00 11.05 ? 96  HIS A NE2 1 
ATOM   789  N  N   . LEU A 1 97  ? 1.872   -29.640 -8.972  1.00 10.77 ? 97  LEU A N   1 
ATOM   790  C  CA  . LEU A 1 97  ? 2.289   -30.784 -8.140  1.00 10.92 ? 97  LEU A CA  1 
ATOM   791  C  C   . LEU A 1 97  ? 3.580   -31.393 -8.621  1.00 10.39 ? 97  LEU A C   1 
ATOM   792  O  O   . LEU A 1 97  ? 3.839   -31.391 -9.841  1.00 11.23 ? 97  LEU A O   1 
ATOM   793  C  CB  . LEU A 1 97  ? 1.103   -31.815 -8.157  1.00 12.04 ? 97  LEU A CB  1 
ATOM   794  C  CG  . LEU A 1 97  ? 1.352   -33.070 -7.262  1.00 12.79 ? 97  LEU A CG  1 
ATOM   795  C  CD1 . LEU A 1 97  ? 1.158   -32.703 -5.796  1.00 12.71 ? 97  LEU A CD1 1 
ATOM   796  C  CD2 . LEU A 1 97  ? 0.282   -34.152 -7.640  1.00 13.09 ? 97  LEU A CD2 1 
ATOM   797  N  N   . HIS A 1 98  ? 4.406   -31.913 -7.694  1.00 9.91  ? 98  HIS A N   1 
ATOM   798  C  CA  . HIS A 1 98  ? 5.590   -32.697 -8.151  1.00 9.56  ? 98  HIS A CA  1 
ATOM   799  C  C   . HIS A 1 98  ? 5.473   -34.103 -7.568  1.00 9.85  ? 98  HIS A C   1 
ATOM   800  O  O   . HIS A 1 98  ? 4.933   -34.329 -6.442  1.00 9.64  ? 98  HIS A O   1 
ATOM   801  C  CB  . HIS A 1 98  ? 6.861   -32.078 -7.570  1.00 10.11 ? 98  HIS A CB  1 
ATOM   802  C  CG  . HIS A 1 98  ? 7.049   -30.632 -8.005  1.00 9.91  ? 98  HIS A CG  1 
ATOM   803  N  ND1 . HIS A 1 98  ? 7.787   -30.281 -9.141  1.00 10.59 ? 98  HIS A ND1 1 
ATOM   804  C  CD2 . HIS A 1 98  ? 6.579   -29.462 -7.460  1.00 10.58 ? 98  HIS A CD2 1 
ATOM   805  C  CE1 . HIS A 1 98  ? 7.775   -28.912 -9.251  1.00 10.36 ? 98  HIS A CE1 1 
ATOM   806  N  NE2 . HIS A 1 98  ? 7.060   -28.430 -8.238  1.00 8.80  ? 98  HIS A NE2 1 
ATOM   807  N  N   . TRP A 1 99  ? 6.005   -35.035 -8.363  1.00 8.98  ? 99  TRP A N   1 
ATOM   808  C  CA  . TRP A 1 99  ? 6.012   -36.472 -7.984  1.00 9.34  ? 99  TRP A CA  1 
ATOM   809  C  C   . TRP A 1 99  ? 7.205   -37.143 -8.544  1.00 11.12 ? 99  TRP A C   1 
ATOM   810  O  O   . TRP A 1 99  ? 7.924   -36.498 -9.276  1.00 9.75  ? 99  TRP A O   1 
ATOM   811  C  CB  . TRP A 1 99  ? 4.704   -37.121 -8.487  1.00 9.85  ? 99  TRP A CB  1 
ATOM   812  C  CG  . TRP A 1 99  ? 4.520   -36.994 -9.983  1.00 9.59  ? 99  TRP A CG  1 
ATOM   813  C  CD1 . TRP A 1 99  ? 5.043   -37.813 -10.985 1.00 11.10 ? 99  TRP A CD1 1 
ATOM   814  C  CD2 . TRP A 1 99  ? 3.757   -35.965 -10.694 1.00 10.35 ? 99  TRP A CD2 1 
ATOM   815  N  NE1 . TRP A 1 99  ? 4.658   -37.369 -12.226 1.00 10.47 ? 99  TRP A NE1 1 
ATOM   816  C  CE2 . TRP A 1 99  ? 3.887   -36.268 -12.124 1.00 11.33 ? 99  TRP A CE2 1 
ATOM   817  C  CE3 . TRP A 1 99  ? 3.009   -34.870 -10.306 1.00 11.64 ? 99  TRP A CE3 1 
ATOM   818  C  CZ2 . TRP A 1 99  ? 3.284   -35.491 -13.094 1.00 10.59 ? 99  TRP A CZ2 1 
ATOM   819  C  CZ3 . TRP A 1 99  ? 2.405   -34.094 -11.294 1.00 12.51 ? 99  TRP A CZ3 1 
ATOM   820  C  CH2 . TRP A 1 99  ? 2.540   -34.398 -12.652 1.00 12.03 ? 99  TRP A CH2 1 
ATOM   821  N  N   . GLY A 1 100 ? 7.366   -38.461 -8.223  1.00 11.22 ? 100 GLY A N   1 
ATOM   822  C  CA  . GLY A 1 100 ? 8.436   -39.237 -8.844  1.00 10.16 ? 100 GLY A CA  1 
ATOM   823  C  C   . GLY A 1 100 ? 7.891   -40.526 -9.453  1.00 11.01 ? 100 GLY A C   1 
ATOM   824  O  O   . GLY A 1 100 ? 6.689   -40.648 -9.442  1.00 10.58 ? 100 GLY A O   1 
ATOM   825  N  N   . SER A 1 101 ? 8.788   -41.357 -9.976  1.00 11.93 ? 101 SER A N   1 
ATOM   826  C  CA  . SER A 1 101 ? 8.331   -42.591 -10.642 1.00 13.78 ? 101 SER A CA  1 
ATOM   827  C  C   . SER A 1 101 ? 7.943   -43.631 -9.608  1.00 15.25 ? 101 SER A C   1 
ATOM   828  O  O   . SER A 1 101 ? 7.282   -44.612 -9.960  1.00 15.16 ? 101 SER A O   1 
ATOM   829  C  CB  . SER A 1 101 ? 9.403   -43.126 -11.596 1.00 13.58 ? 101 SER A CB  1 
ATOM   830  O  OG  . SER A 1 101 ? 10.516  -43.608 -10.871 1.00 17.15 ? 101 SER A OG  1 
ATOM   831  N  N   . ALA A 1 102 ? 8.331   -43.450 -8.342  1.00 15.10 ? 102 ALA A N   1 
ATOM   832  C  CA  . ALA A 1 102 ? 7.903   -44.409 -7.330  1.00 14.38 ? 102 ALA A CA  1 
ATOM   833  C  C   . ALA A 1 102 ? 7.124   -43.695 -6.252  1.00 15.41 ? 102 ALA A C   1 
ATOM   834  O  O   . ALA A 1 102 ? 7.504   -42.518 -5.904  1.00 14.80 ? 102 ALA A O   1 
ATOM   835  C  CB  . ALA A 1 102 ? 9.111   -45.114 -6.732  1.00 16.22 ? 102 ALA A CB  1 
ATOM   836  N  N   . ASP A 1 103 ? 6.217   -44.414 -5.652  1.00 14.06 ? 103 ASP A N   1 
ATOM   837  C  CA  . ASP A 1 103 ? 5.295   -43.815 -4.693  1.00 15.97 ? 103 ASP A CA  1 
ATOM   838  C  C   . ASP A 1 103 ? 5.938   -43.333 -3.391  1.00 18.81 ? 103 ASP A C   1 
ATOM   839  O  O   . ASP A 1 103 ? 5.236   -42.592 -2.624  1.00 20.38 ? 103 ASP A O   1 
ATOM   840  C  CB  . ASP A 1 103 ? 4.123   -44.694 -4.288  1.00 16.17 ? 103 ASP A CB  1 
ATOM   841  C  CG  . ASP A 1 103 ? 3.079   -44.789 -5.348  1.00 18.60 ? 103 ASP A CG  1 
ATOM   842  O  OD1 . ASP A 1 103 ? 3.203   -44.147 -6.403  1.00 18.41 ? 103 ASP A OD1 1 
ATOM   843  O  OD2 . ASP A 1 103 ? 2.070   -45.448 -5.150  1.00 18.29 ? 103 ASP A OD2 1 
ATOM   844  N  N   . ASP A 1 104 ? 7.156   -43.771 -3.125  1.00 16.90 ? 104 ASP A N   1 
ATOM   845  C  CA  . ASP A 1 104 ? 7.827   -43.378 -1.866  1.00 19.27 ? 104 ASP A CA  1 
ATOM   846  C  C   . ASP A 1 104 ? 8.949   -42.407 -2.046  1.00 18.59 ? 104 ASP A C   1 
ATOM   847  O  O   . ASP A 1 104 ? 9.747   -42.188 -1.112  1.00 21.01 ? 104 ASP A O   1 
ATOM   848  C  CB  . ASP A 1 104 ? 8.347   -44.610 -1.115  1.00 19.63 ? 104 ASP A CB  1 
ATOM   849  C  CG  . ASP A 1 104 ? 9.393   -45.372 -1.892  1.00 23.43 ? 104 ASP A CG  1 
ATOM   850  O  OD1 . ASP A 1 104 ? 9.543   -45.250 -3.146  1.00 21.81 ? 104 ASP A OD1 1 
ATOM   851  O  OD2 . ASP A 1 104 ? 10.048  -46.243 -1.278  1.00 29.82 ? 104 ASP A OD2 1 
ATOM   852  N  N   . HIS A 1 105 ? 9.101   -41.797 -3.234  1.00 18.45 ? 105 HIS A N   1 
ATOM   853  C  CA  . HIS A 1 105 ? 10.201  -40.896 -3.441  1.00 16.89 ? 105 HIS A CA  1 
ATOM   854  C  C   . HIS A 1 105 ? 9.794   -39.837 -4.494  1.00 16.82 ? 105 HIS A C   1 
ATOM   855  O  O   . HIS A 1 105 ? 10.301  -39.871 -5.657  1.00 17.80 ? 105 HIS A O   1 
ATOM   856  C  CB  . HIS A 1 105 ? 11.490  -41.667 -3.915  1.00 20.15 ? 105 HIS A CB  1 
ATOM   857  C  CG  . HIS A 1 105 ? 12.788  -40.866 -3.787  1.00 20.11 ? 105 HIS A CG  1 
ATOM   858  N  ND1 . HIS A 1 105 ? 13.370  -40.198 -4.815  1.00 23.20 ? 105 HIS A ND1 1 
ATOM   859  C  CD2 . HIS A 1 105 ? 13.638  -40.688 -2.689  1.00 22.62 ? 105 HIS A CD2 1 
ATOM   860  C  CE1 . HIS A 1 105 ? 14.534  -39.606 -4.390  1.00 23.18 ? 105 HIS A CE1 1 
ATOM   861  N  NE2 . HIS A 1 105 ? 14.676  -39.891 -3.083  1.00 21.92 ? 105 HIS A NE2 1 
ATOM   862  N  N   . GLY A 1 106 ? 8.957   -38.885 -4.135  1.00 13.92 ? 106 GLY A N   1 
ATOM   863  C  CA  . GLY A 1 106 ? 8.425   -37.924 -5.155  1.00 12.95 ? 106 GLY A CA  1 
ATOM   864  C  C   . GLY A 1 106 ? 8.417   -36.469 -4.733  1.00 13.60 ? 106 GLY A C   1 
ATOM   865  O  O   . GLY A 1 106 ? 8.247   -35.582 -5.607  1.00 15.19 ? 106 GLY A O   1 
ATOM   866  N  N   . SER A 1 107 ? 8.715   -36.198 -3.481  1.00 11.84 ? 107 SER A N   1 
ATOM   867  C  CA  . SER A 1 107 ? 8.707   -34.782 -3.071  1.00 11.12 ? 107 SER A CA  1 
ATOM   868  C  C   . SER A 1 107 ? 9.962   -34.062 -3.514  1.00 11.29 ? 107 SER A C   1 
ATOM   869  O  O   . SER A 1 107 ? 11.016  -34.663 -3.851  1.00 11.37 ? 107 SER A O   1 
ATOM   870  C  CB  . SER A 1 107 ? 8.402   -34.661 -1.568  1.00 11.17 ? 107 SER A CB  1 
ATOM   871  O  OG  . SER A 1 107 ? 9.520   -35.217 -0.837  1.00 10.57 ? 107 SER A OG  1 
ATOM   872  N  N   . GLU A 1 108 ? 9.886   -32.708 -3.509  1.00 10.06 ? 108 GLU A N   1 
ATOM   873  C  CA  . GLU A 1 108 ? 11.039  -31.855 -3.828  1.00 10.07 ? 108 GLU A CA  1 
ATOM   874  C  C   . GLU A 1 108 ? 11.853  -31.632 -2.578  1.00 10.20 ? 108 GLU A C   1 
ATOM   875  O  O   . GLU A 1 108 ? 13.044  -32.005 -2.491  1.00 11.20 ? 108 GLU A O   1 
ATOM   876  C  CB  . GLU A 1 108 ? 10.620  -30.543 -4.504  1.00 11.06 ? 108 GLU A CB  1 
ATOM   877  C  CG  . GLU A 1 108 ? 9.990   -30.863 -5.872  1.00 12.09 ? 108 GLU A CG  1 
ATOM   878  C  CD  . GLU A 1 108 ? 10.233  -29.784 -6.891  1.00 11.78 ? 108 GLU A CD  1 
ATOM   879  O  OE1 . GLU A 1 108 ? 9.884   -28.605 -6.636  1.00 11.20 ? 108 GLU A OE1 1 
ATOM   880  O  OE2 . GLU A 1 108 ? 10.847  -30.039 -7.926  1.00 10.86 ? 108 GLU A OE2 1 
ATOM   881  N  N   . HIS A 1 109 ? 11.200  -31.030 -1.541  1.00 10.27 ? 109 HIS A N   1 
ATOM   882  C  CA  . HIS A 1 109 ? 11.868  -30.924 -0.272  1.00 10.67 ? 109 HIS A CA  1 
ATOM   883  C  C   . HIS A 1 109 ? 11.908  -32.332 0.375   1.00 10.71 ? 109 HIS A C   1 
ATOM   884  O  O   . HIS A 1 109 ? 11.021  -33.155 0.166   1.00 12.45 ? 109 HIS A O   1 
ATOM   885  C  CB  . HIS A 1 109 ? 11.126  -29.914 0.645   1.00 9.21  ? 109 HIS A CB  1 
ATOM   886  C  CG  . HIS A 1 109 ? 11.183  -28.518 0.123   1.00 9.03  ? 109 HIS A CG  1 
ATOM   887  N  ND1 . HIS A 1 109 ? 10.296  -27.998 -0.786  1.00 9.85  ? 109 HIS A ND1 1 
ATOM   888  C  CD2 . HIS A 1 109 ? 12.165  -27.547 0.371   1.00 9.86  ? 109 HIS A CD2 1 
ATOM   889  C  CE1 . HIS A 1 109 ? 10.755  -26.715 -1.106  1.00 8.35  ? 109 HIS A CE1 1 
ATOM   890  N  NE2 . HIS A 1 109 ? 11.862  -26.467 -0.405  1.00 9.07  ? 109 HIS A NE2 1 
ATOM   891  N  N   . ILE A 1 110 ? 12.894  -32.513 1.203   1.00 11.41 ? 110 ILE A N   1 
ATOM   892  C  CA  . ILE A 1 110 ? 13.063  -33.750 2.025   1.00 13.75 ? 110 ILE A CA  1 
ATOM   893  C  C   . ILE A 1 110 ? 13.242  -33.303 3.491   1.00 13.79 ? 110 ILE A C   1 
ATOM   894  O  O   . ILE A 1 110 ? 13.676  -32.190 3.759   1.00 14.13 ? 110 ILE A O   1 
ATOM   895  C  CB  . ILE A 1 110 ? 14.362  -34.435 1.544   1.00 15.74 ? 110 ILE A CB  1 
ATOM   896  C  CG1 . ILE A 1 110 ? 14.144  -34.987 0.153   1.00 18.21 ? 110 ILE A CG1 1 
ATOM   897  C  CG2 . ILE A 1 110 ? 14.899  -35.505 2.510   1.00 22.13 ? 110 ILE A CG2 1 
ATOM   898  C  CD1 . ILE A 1 110 ? 15.557  -35.111 -0.472  1.00 26.02 ? 110 ILE A CD1 1 
ATOM   899  N  N   . VAL A 1 111 ? 12.816  -34.132 4.465   1.00 13.66 ? 111 VAL A N   1 
ATOM   900  C  CA  . VAL A 1 111 ? 12.936  -33.768 5.914   1.00 14.18 ? 111 VAL A CA  1 
ATOM   901  C  C   . VAL A 1 111 ? 13.758  -34.848 6.606   1.00 14.24 ? 111 VAL A C   1 
ATOM   902  O  O   . VAL A 1 111 ? 13.324  -35.973 6.630   1.00 16.48 ? 111 VAL A O   1 
ATOM   903  C  CB  . VAL A 1 111 ? 11.534  -33.611 6.559   1.00 15.82 ? 111 VAL A CB  1 
ATOM   904  C  CG1 . VAL A 1 111 ? 11.698  -33.162 8.000   1.00 15.85 ? 111 VAL A CG1 1 
ATOM   905  C  CG2 . VAL A 1 111 ? 10.689  -32.646 5.745   1.00 16.15 ? 111 VAL A CG2 1 
ATOM   906  N  N   . ASP A 1 112 ? 14.896  -34.473 7.144   1.00 12.62 ? 112 ASP A N   1 
ATOM   907  C  CA  . ASP A 1 112 ? 15.804  -35.460 7.824   1.00 14.72 ? 112 ASP A CA  1 
ATOM   908  C  C   . ASP A 1 112 ? 15.805  -36.783 7.035   1.00 16.62 ? 112 ASP A C   1 
ATOM   909  O  O   . ASP A 1 112 ? 15.472  -37.878 7.589   1.00 16.51 ? 112 ASP A O   1 
ATOM   910  C  CB  . ASP A 1 112 ? 15.315  -35.660 9.242   1.00 17.09 ? 112 ASP A CB  1 
ATOM   911  C  CG  . ASP A 1 112 ? 15.509  -34.411 10.093  1.00 18.89 ? 112 ASP A CG  1 
ATOM   912  O  OD1 . ASP A 1 112 ? 16.457  -33.638 9.855   1.00 19.55 ? 112 ASP A OD1 1 
ATOM   913  O  OD2 . ASP A 1 112 ? 14.756  -34.283 11.075  1.00 25.01 ? 112 ASP A OD2 1 
ATOM   914  N  N   . GLY A 1 113 ? 16.252  -36.689 5.785   1.00 14.06 ? 113 GLY A N   1 
ATOM   915  C  CA  . GLY A 1 113 ? 16.435  -37.898 4.966   1.00 15.35 ? 113 GLY A CA  1 
ATOM   916  C  C   . GLY A 1 113 ? 15.198  -38.511 4.308   1.00 15.38 ? 113 GLY A C   1 
ATOM   917  O  O   . GLY A 1 113 ? 15.352  -39.362 3.369   1.00 20.98 ? 113 GLY A O   1 
ATOM   918  N  N   . VAL A 1 114 ? 14.003  -38.057 4.704   1.00 15.16 ? 114 VAL A N   1 
ATOM   919  C  CA  . VAL A 1 114 ? 12.756  -38.662 4.284   1.00 16.05 ? 114 VAL A CA  1 
ATOM   920  C  C   . VAL A 1 114 ? 12.146  -37.881 3.131   1.00 15.88 ? 114 VAL A C   1 
ATOM   921  O  O   . VAL A 1 114 ? 11.891  -36.658 3.284   1.00 16.45 ? 114 VAL A O   1 
ATOM   922  C  CB  . VAL A 1 114 ? 11.735  -38.670 5.464   1.00 16.61 ? 114 VAL A CB  1 
ATOM   923  C  CG1 . VAL A 1 114 ? 10.286  -39.028 5.036   1.00 19.85 ? 114 VAL A CG1 1 
ATOM   924  C  CG2 . VAL A 1 114 ? 12.245  -39.585 6.598   1.00 20.84 ? 114 VAL A CG2 1 
ATOM   925  N  N   . SER A 1 115 ? 11.828  -38.576 2.033   1.00 14.73 ? 115 SER A N   1 
ATOM   926  C  CA  . SER A 1 115 ? 11.038  -38.077 0.919   1.00 14.39 ? 115 SER A CA  1 
ATOM   927  C  C   . SER A 1 115 ? 9.598   -38.468 1.132   1.00 15.75 ? 115 SER A C   1 
ATOM   928  O  O   . SER A 1 115 ? 9.276   -39.562 1.719   1.00 16.71 ? 115 SER A O   1 
ATOM   929  C  CB  . SER A 1 115 ? 11.509  -38.687 -0.377  1.00 16.22 ? 115 SER A CB  1 
ATOM   930  O  OG  . SER A 1 115 ? 12.756  -38.093 -0.772  1.00 18.81 ? 115 SER A OG  1 
ATOM   931  N  N   . TYR A 1 116 ? 8.665   -37.599 0.706   1.00 11.69 ? 116 TYR A N   1 
ATOM   932  C  CA  . TYR A 1 116 ? 7.291   -37.940 0.672   1.00 12.37 ? 116 TYR A CA  1 
ATOM   933  C  C   . TYR A 1 116 ? 6.859   -38.383 -0.745  1.00 11.47 ? 116 TYR A C   1 
ATOM   934  O  O   . TYR A 1 116 ? 7.687   -38.348 -1.703  1.00 12.84 ? 116 TYR A O   1 
ATOM   935  C  CB  . TYR A 1 116 ? 6.381   -36.735 1.184   1.00 12.20 ? 116 TYR A CB  1 
ATOM   936  C  CG  . TYR A 1 116 ? 6.641   -36.463 2.629   1.00 13.36 ? 116 TYR A CG  1 
ATOM   937  C  CD1 . TYR A 1 116 ? 5.762   -37.016 3.562   1.00 15.04 ? 116 TYR A CD1 1 
ATOM   938  C  CD2 . TYR A 1 116 ? 7.740   -35.699 3.064   1.00 15.12 ? 116 TYR A CD2 1 
ATOM   939  C  CE1 . TYR A 1 116 ? 5.984   -36.829 4.912   1.00 17.20 ? 116 TYR A CE1 1 
ATOM   940  C  CE2 . TYR A 1 116 ? 7.939   -35.511 4.447   1.00 16.23 ? 116 TYR A CE2 1 
ATOM   941  C  CZ  . TYR A 1 116 ? 7.010   -36.080 5.318   1.00 17.81 ? 116 TYR A CZ  1 
ATOM   942  O  OH  . TYR A 1 116 ? 7.230   -35.845 6.683   1.00 23.82 ? 116 TYR A OH  1 
ATOM   943  N  N   . ALA A 1 117 ? 5.638   -38.837 -0.880  1.00 11.89 ? 117 ALA A N   1 
ATOM   944  C  CA  . ALA A 1 117 ? 5.155   -39.336 -2.178  1.00 11.22 ? 117 ALA A CA  1 
ATOM   945  C  C   . ALA A 1 117 ? 5.042   -38.256 -3.278  1.00 12.71 ? 117 ALA A C   1 
ATOM   946  O  O   . ALA A 1 117 ? 5.330   -38.508 -4.429  1.00 12.65 ? 117 ALA A O   1 
ATOM   947  C  CB  . ALA A 1 117 ? 3.815   -40.071 -1.994  1.00 12.25 ? 117 ALA A CB  1 
ATOM   948  N  N   . ALA A 1 118 ? 4.706   -37.037 -2.835  1.00 11.17 ? 118 ALA A N   1 
ATOM   949  C  CA  . ALA A 1 118 ? 4.533   -35.978 -3.818  1.00 11.60 ? 118 ALA A CA  1 
ATOM   950  C  C   . ALA A 1 118 ? 4.522   -34.665 -3.009  1.00 11.62 ? 118 ALA A C   1 
ATOM   951  O  O   . ALA A 1 118 ? 4.673   -34.680 -1.752  1.00 11.01 ? 118 ALA A O   1 
ATOM   952  C  CB  . ALA A 1 118 ? 3.248   -36.184 -4.558  1.00 11.83 ? 118 ALA A CB  1 
ATOM   953  N  N   . GLU A 1 119 ? 4.528   -33.548 -3.725  1.00 9.99  ? 119 GLU A N   1 
ATOM   954  C  CA  . GLU A 1 119 ? 4.627   -32.248 -3.039  1.00 10.50 ? 119 GLU A CA  1 
ATOM   955  C  C   . GLU A 1 119 ? 3.796   -31.232 -3.880  1.00 10.72 ? 119 GLU A C   1 
ATOM   956  O  O   . GLU A 1 119 ? 4.044   -31.013 -5.048  1.00 11.07 ? 119 GLU A O   1 
ATOM   957  C  CB  . GLU A 1 119 ? 6.062   -31.811 -2.859  1.00 10.98 ? 119 GLU A CB  1 
ATOM   958  C  CG  . GLU A 1 119 ? 6.200   -30.504 -2.054  1.00 12.28 ? 119 GLU A CG  1 
ATOM   959  C  CD  . GLU A 1 119 ? 7.596   -30.177 -1.773  1.00 13.60 ? 119 GLU A CD  1 
ATOM   960  O  OE1 . GLU A 1 119 ? 8.448   -31.077 -1.672  1.00 10.95 ? 119 GLU A OE1 1 
ATOM   961  O  OE2 . GLU A 1 119 ? 7.904   -28.951 -1.597  1.00 12.86 ? 119 GLU A OE2 1 
ATOM   962  N  N   . LEU A 1 120 ? 2.820   -30.633 -3.217  1.00 10.36 ? 120 LEU A N   1 
ATOM   963  C  CA  . LEU A 1 120 ? 1.876   -29.635 -3.830  1.00 9.68  ? 120 LEU A CA  1 
ATOM   964  C  C   . LEU A 1 120 ? 2.449   -28.254 -3.583  1.00 10.25 ? 120 LEU A C   1 
ATOM   965  O  O   . LEU A 1 120 ? 2.895   -27.962 -2.468  1.00 11.12 ? 120 LEU A O   1 
ATOM   966  C  CB  . LEU A 1 120 ? 0.486   -29.658 -3.118  1.00 11.64 ? 120 LEU A CB  1 
ATOM   967  C  CG  . LEU A 1 120 ? -0.621  -28.822 -3.857  1.00 12.08 ? 120 LEU A CG  1 
ATOM   968  C  CD1 . LEU A 1 120 ? -1.218  -29.495 -5.111  1.00 14.12 ? 120 LEU A CD1 1 
ATOM   969  C  CD2 . LEU A 1 120 ? -1.752  -28.571 -2.839  1.00 15.53 ? 120 LEU A CD2 1 
ATOM   970  N  N   . HIS A 1 121 ? 2.523   -27.400 -4.640  1.00 9.54  ? 121 HIS A N   1 
ATOM   971  C  CA  . HIS A 1 121 ? 2.993   -26.008 -4.419  1.00 8.53  ? 121 HIS A CA  1 
ATOM   972  C  C   . HIS A 1 121 ? 1.959   -24.988 -4.827  1.00 10.12 ? 121 HIS A C   1 
ATOM   973  O  O   . HIS A 1 121 ? 1.258   -25.111 -5.837  1.00 10.89 ? 121 HIS A O   1 
ATOM   974  C  CB  . HIS A 1 121 ? 4.224   -25.791 -5.344  1.00 9.85  ? 121 HIS A CB  1 
ATOM   975  C  CG  . HIS A 1 121 ? 5.408   -26.507 -4.854  1.00 9.65  ? 121 HIS A CG  1 
ATOM   976  N  ND1 . HIS A 1 121 ? 6.440   -26.784 -5.708  1.00 10.58 ? 121 HIS A ND1 1 
ATOM   977  C  CD2 . HIS A 1 121 ? 5.769   -26.982 -3.628  1.00 10.49 ? 121 HIS A CD2 1 
ATOM   978  C  CE1 . HIS A 1 121 ? 7.404   -27.444 -5.076  1.00 9.58  ? 121 HIS A CE1 1 
ATOM   979  N  NE2 . HIS A 1 121 ? 6.997   -27.587 -3.771  1.00 9.91  ? 121 HIS A NE2 1 
ATOM   980  N  N   . VAL A 1 122 ? 1.734   -24.053 -3.898  1.00 9.96  ? 122 VAL A N   1 
ATOM   981  C  CA  . VAL A 1 122 ? 0.712   -23.002 -4.104  1.00 10.27 ? 122 VAL A CA  1 
ATOM   982  C  C   . VAL A 1 122 ? 1.537   -21.700 -4.249  1.00 10.09 ? 122 VAL A C   1 
ATOM   983  O  O   . VAL A 1 122 ? 2.209   -21.267 -3.296  1.00 9.45  ? 122 VAL A O   1 
ATOM   984  C  CB  . VAL A 1 122 ? -0.185  -22.884 -2.878  1.00 9.39  ? 122 VAL A CB  1 
ATOM   985  C  CG1 . VAL A 1 122 ? -1.346  -21.953 -3.239  1.00 11.41 ? 122 VAL A CG1 1 
ATOM   986  C  CG2 . VAL A 1 122 ? -0.805  -24.242 -2.554  1.00 12.22 ? 122 VAL A CG2 1 
ATOM   987  N  N   . VAL A 1 123 ? 1.504   -21.059 -5.447  1.00 11.04 ? 123 VAL A N   1 
ATOM   988  C  CA  . VAL A 1 123 ? 2.409   -19.979 -5.787  1.00 10.43 ? 123 VAL A CA  1 
ATOM   989  C  C   . VAL A 1 123 ? 1.619   -18.619 -5.666  1.00 10.38 ? 123 VAL A C   1 
ATOM   990  O  O   . VAL A 1 123 ? 0.563   -18.495 -6.196  1.00 11.12 ? 123 VAL A O   1 
ATOM   991  C  CB  . VAL A 1 123 ? 2.905   -20.168 -7.243  1.00 11.25 ? 123 VAL A CB  1 
ATOM   992  C  CG1 . VAL A 1 123 ? 3.844   -19.007 -7.636  1.00 10.19 ? 123 VAL A CG1 1 
ATOM   993  C  CG2 . VAL A 1 123 ? 3.600   -21.570 -7.401  1.00 11.99 ? 123 VAL A CG2 1 
ATOM   994  N  N   . HIS A 1 124 ? 2.257   -17.687 -4.977  1.00 10.42 ? 124 HIS A N   1 
ATOM   995  C  CA  . HIS A 1 124 ? 1.671   -16.343 -4.706  1.00 11.87 ? 124 HIS A CA  1 
ATOM   996  C  C   . HIS A 1 124 ? 2.712   -15.317 -5.056  1.00 12.27 ? 124 HIS A C   1 
ATOM   997  O  O   . HIS A 1 124 ? 3.931   -15.491 -4.998  1.00 11.36 ? 124 HIS A O   1 
ATOM   998  C  CB  . HIS A 1 124 ? 1.326   -16.164 -3.192  1.00 11.44 ? 124 HIS A CB  1 
ATOM   999  C  CG  . HIS A 1 124 ? 0.580   -17.314 -2.588  1.00 12.78 ? 124 HIS A CG  1 
ATOM   1000 N  ND1 . HIS A 1 124 ? 1.205   -18.531 -2.251  1.00 12.94 ? 124 HIS A ND1 1 
ATOM   1001 C  CD2 . HIS A 1 124 ? -0.706  -17.405 -2.130  1.00 13.82 ? 124 HIS A CD2 1 
ATOM   1002 C  CE1 . HIS A 1 124 ? 0.276   -19.302 -1.627  1.00 13.59 ? 124 HIS A CE1 1 
ATOM   1003 N  NE2 . HIS A 1 124 ? -0.848  -18.644 -1.520  1.00 14.84 ? 124 HIS A NE2 1 
ATOM   1004 N  N   . TRP A 1 125 ? 2.177   -14.113 -5.357  1.00 12.02 ? 125 TRP A N   1 
ATOM   1005 C  CA  . TRP A 1 125 ? 3.070   -12.967 -5.662  1.00 12.24 ? 125 TRP A CA  1 
ATOM   1006 C  C   . TRP A 1 125 ? 2.718   -11.640 -4.950  1.00 11.74 ? 125 TRP A C   1 
ATOM   1007 O  O   . TRP A 1 125 ? 1.548   -11.386 -4.613  1.00 13.70 ? 125 TRP A O   1 
ATOM   1008 C  CB  . TRP A 1 125 ? 3.057   -12.747 -7.169  1.00 11.49 ? 125 TRP A CB  1 
ATOM   1009 C  CG  . TRP A 1 125 ? 1.780   -12.383 -7.799  1.00 11.77 ? 125 TRP A CG  1 
ATOM   1010 C  CD1 . TRP A 1 125 ? 0.774   -13.230 -8.226  1.00 12.89 ? 125 TRP A CD1 1 
ATOM   1011 C  CD2 . TRP A 1 125 ? 1.363   -11.048 -8.173  1.00 12.01 ? 125 TRP A CD2 1 
ATOM   1012 N  NE1 . TRP A 1 125 ? -0.239  -12.510 -8.804  1.00 13.99 ? 125 TRP A NE1 1 
ATOM   1013 C  CE2 . TRP A 1 125 ? 0.058   -11.194 -8.798  1.00 13.04 ? 125 TRP A CE2 1 
ATOM   1014 C  CE3 . TRP A 1 125 ? 1.918   -9.790  -8.039  1.00 14.17 ? 125 TRP A CE3 1 
ATOM   1015 C  CZ2 . TRP A 1 125 ? -0.649  -10.105 -9.269  1.00 15.32 ? 125 TRP A CZ2 1 
ATOM   1016 C  CZ3 . TRP A 1 125 ? 1.192   -8.695  -8.514  1.00 13.61 ? 125 TRP A CZ3 1 
ATOM   1017 C  CH2 . TRP A 1 125 ? -0.065  -8.855  -9.108  1.00 11.72 ? 125 TRP A CH2 1 
ATOM   1018 N  N   . ASN A 1 126 ? 3.767   -10.840 -4.694  1.00 13.05 ? 126 ASN A N   1 
ATOM   1019 C  CA  . ASN A 1 126 ? 3.576   -9.638  -3.825  1.00 13.75 ? 126 ASN A CA  1 
ATOM   1020 C  C   . ASN A 1 126 ? 2.902   -8.512  -4.615  1.00 13.24 ? 126 ASN A C   1 
ATOM   1021 O  O   . ASN A 1 126 ? 3.557   -7.739  -5.295  1.00 13.19 ? 126 ASN A O   1 
ATOM   1022 C  CB  . ASN A 1 126 ? 4.937   -9.266  -3.293  1.00 14.06 ? 126 ASN A CB  1 
ATOM   1023 C  CG  . ASN A 1 126 ? 4.891   -8.073  -2.322  1.00 14.24 ? 126 ASN A CG  1 
ATOM   1024 O  OD1 . ASN A 1 126 ? 3.897   -7.348  -2.310  1.00 16.16 ? 126 ASN A OD1 1 
ATOM   1025 N  ND2 . ASN A 1 126 ? 5.864   -7.966  -1.464  1.00 16.10 ? 126 ASN A ND2 1 
ATOM   1026 N  N   . SER A 1 127 ? 1.638   -8.366  -4.400  1.00 13.80 ? 127 SER A N   1 
ATOM   1027 C  CA  . SER A 1 127 ? 0.802   -7.437  -5.195  1.00 14.59 ? 127 SER A CA  1 
ATOM   1028 C  C   . SER A 1 127 ? 0.774   -6.110  -4.424  1.00 13.80 ? 127 SER A C   1 
ATOM   1029 O  O   . SER A 1 127 ? 0.328   -5.109  -5.036  1.00 13.77 ? 127 SER A O   1 
ATOM   1030 C  CB  . SER A 1 127 ? -0.578  -7.917  -5.462  1.00 14.32 ? 127 SER A CB  1 
ATOM   1031 O  OG  . SER A 1 127 ? -1.320  -8.217  -4.230  1.00 16.08 ? 127 SER A OG  1 
ATOM   1032 N  N   . ASP A 1 128 ? 1.393   -6.059  -3.261  1.00 13.45 ? 128 ASP A N   1 
ATOM   1033 C  CA  . ASP A 1 128 ? 1.480   -4.749  -2.486  1.00 14.81 ? 128 ASP A CA  1 
ATOM   1034 C  C   . ASP A 1 128 ? 2.655   -3.992  -3.095  1.00 15.40 ? 128 ASP A C   1 
ATOM   1035 O  O   . ASP A 1 128 ? 2.763   -2.742  -2.950  1.00 20.02 ? 128 ASP A O   1 
ATOM   1036 C  CB  . ASP A 1 128 ? 1.777   -4.988  -0.984  1.00 15.34 ? 128 ASP A CB  1 
ATOM   1037 C  CG  . ASP A 1 128 ? 0.504   -5.395  -0.208  1.00 16.44 ? 128 ASP A CG  1 
ATOM   1038 O  OD1 . ASP A 1 128 ? 0.666   -5.691  0.970   1.00 19.34 ? 128 ASP A OD1 1 
ATOM   1039 O  OD2 . ASP A 1 128 ? -0.611  -5.330  -0.779  1.00 17.29 ? 128 ASP A OD2 1 
ATOM   1040 N  N   . LYS A 1 129 ? 3.592   -4.631  -3.800  1.00 14.71 ? 129 LYS A N   1 
ATOM   1041 C  CA  . LYS A 1 129 ? 4.773   -3.959  -4.315  1.00 15.33 ? 129 LYS A CA  1 
ATOM   1042 C  C   . LYS A 1 129 ? 4.946   -3.988  -5.837  1.00 15.84 ? 129 LYS A C   1 
ATOM   1043 O  O   . LYS A 1 129 ? 5.693   -3.153  -6.355  1.00 18.16 ? 129 LYS A O   1 
ATOM   1044 C  CB  . LYS A 1 129 ? 6.085   -4.461  -3.700  1.00 16.41 ? 129 LYS A CB  1 
ATOM   1045 C  CG  . LYS A 1 129 ? 6.216   -4.160  -2.248  1.00 18.95 ? 129 LYS A CG  1 
ATOM   1046 C  CD  . LYS A 1 129 ? 7.587   -4.521  -1.670  1.00 21.26 ? 129 LYS A CD  1 
ATOM   1047 C  CE  . LYS A 1 129 ? 8.768   -3.930  -2.438  1.00 22.48 ? 129 LYS A CE  1 
ATOM   1048 N  NZ  . LYS A 1 129 ? 10.084  -4.243  -1.768  1.00 25.52 ? 129 LYS A NZ  1 
ATOM   1049 N  N   . TYR A 1 130 ? 4.405   -5.007  -6.525  1.00 15.99 ? 130 TYR A N   1 
ATOM   1050 C  CA  . TYR A 1 130 ? 4.773   -5.241  -7.901  1.00 14.04 ? 130 TYR A CA  1 
ATOM   1051 C  C   . TYR A 1 130 ? 3.532   -5.322  -8.687  1.00 13.40 ? 130 TYR A C   1 
ATOM   1052 O  O   . TYR A 1 130 ? 2.459   -5.707  -8.158  1.00 14.83 ? 130 TYR A O   1 
ATOM   1053 C  CB  . TYR A 1 130 ? 5.641   -6.574  -8.058  1.00 13.51 ? 130 TYR A CB  1 
ATOM   1054 C  CG  . TYR A 1 130 ? 6.809   -6.524  -7.187  1.00 14.93 ? 130 TYR A CG  1 
ATOM   1055 C  CD1 . TYR A 1 130 ? 7.755   -5.512  -7.346  1.00 16.56 ? 130 TYR A CD1 1 
ATOM   1056 C  CD2 . TYR A 1 130 ? 6.983   -7.391  -6.126  1.00 14.28 ? 130 TYR A CD2 1 
ATOM   1057 C  CE1 . TYR A 1 130 ? 8.823   -5.388  -6.477  1.00 18.34 ? 130 TYR A CE1 1 
ATOM   1058 C  CE2 . TYR A 1 130 ? 8.056   -7.259  -5.267  1.00 13.55 ? 130 TYR A CE2 1 
ATOM   1059 C  CZ  . TYR A 1 130 ? 9.008   -6.265  -5.479  1.00 15.34 ? 130 TYR A CZ  1 
ATOM   1060 O  OH  . TYR A 1 130 ? 10.037  -6.069  -4.640  1.00 18.56 ? 130 TYR A OH  1 
ATOM   1061 N  N   . PRO A 1 131 ? 3.567   -4.959  -9.972  1.00 14.66 ? 131 PRO A N   1 
ATOM   1062 C  CA  . PRO A 1 131 ? 2.348   -4.848  -10.737 1.00 15.77 ? 131 PRO A CA  1 
ATOM   1063 C  C   . PRO A 1 131 ? 1.811   -6.150  -11.283 1.00 16.48 ? 131 PRO A C   1 
ATOM   1064 O  O   . PRO A 1 131 ? 0.650   -6.223  -11.691 1.00 17.30 ? 131 PRO A O   1 
ATOM   1065 C  CB  . PRO A 1 131 ? 2.762   -3.979  -11.976 1.00 16.50 ? 131 PRO A CB  1 
ATOM   1066 C  CG  . PRO A 1 131 ? 4.208   -4.089  -12.012 1.00 16.18 ? 131 PRO A CG  1 
ATOM   1067 C  CD  . PRO A 1 131 ? 4.759   -4.437  -10.704 1.00 15.80 ? 131 PRO A CD  1 
ATOM   1068 N  N   . SER A 1 132 ? 2.663   -7.204  -11.316 1.00 15.52 ? 132 SER A N   1 
ATOM   1069 C  CA  . SER A 1 132 ? 2.112   -8.474  -11.849 1.00 15.73 ? 132 SER A CA  1 
ATOM   1070 C  C   . SER A 1 132 ? 3.055   -9.567  -11.344 1.00 13.51 ? 132 SER A C   1 
ATOM   1071 O  O   . SER A 1 132 ? 4.145   -9.333  -10.808 1.00 12.70 ? 132 SER A O   1 
ATOM   1072 C  CB  . SER A 1 132 ? 2.193   -8.521  -13.362 1.00 19.73 ? 132 SER A CB  1 
ATOM   1073 O  OG  . SER A 1 132 ? 3.552   -8.644  -13.671 1.00 22.14 ? 132 SER A OG  1 
ATOM   1074 N  N   . PHE A 1 133 ? 2.594   -10.802 -11.537 1.00 14.00 ? 133 PHE A N   1 
ATOM   1075 C  CA  . PHE A 1 133 ? 3.475   -11.913 -11.148 1.00 14.70 ? 133 PHE A CA  1 
ATOM   1076 C  C   . PHE A 1 133 ? 4.834   -11.914 -11.901 1.00 14.06 ? 133 PHE A C   1 
ATOM   1077 O  O   . PHE A 1 133 ? 5.860   -12.301 -11.307 1.00 14.59 ? 133 PHE A O   1 
ATOM   1078 C  CB  . PHE A 1 133 ? 2.702   -13.154 -11.593 1.00 18.57 ? 133 PHE A CB  1 
ATOM   1079 C  CG  . PHE A 1 133 ? 3.440   -14.430 -11.434 1.00 25.36 ? 133 PHE A CG  1 
ATOM   1080 C  CD1 . PHE A 1 133 ? 3.680   -14.982 -10.150 1.00 24.81 ? 133 PHE A CD1 1 
ATOM   1081 C  CD2 . PHE A 1 133 ? 3.792   -15.172 -12.563 1.00 26.21 ? 133 PHE A CD2 1 
ATOM   1082 C  CE1 . PHE A 1 133 ? 4.293   -16.241 -9.995  1.00 27.62 ? 133 PHE A CE1 1 
ATOM   1083 C  CE2 . PHE A 1 133 ? 4.466   -16.429 -12.356 1.00 30.88 ? 133 PHE A CE2 1 
ATOM   1084 C  CZ  . PHE A 1 133 ? 4.715   -16.951 -11.047 1.00 25.59 ? 133 PHE A CZ  1 
ATOM   1085 N  N   . VAL A 1 134 ? 4.864   -11.474 -13.154 1.00 15.70 ? 134 VAL A N   1 
ATOM   1086 C  CA  . VAL A 1 134 ? 6.109   -11.549 -13.908 1.00 16.23 ? 134 VAL A CA  1 
ATOM   1087 C  C   . VAL A 1 134 ? 7.089   -10.625 -13.316 1.00 17.60 ? 134 VAL A C   1 
ATOM   1088 O  O   . VAL A 1 134 ? 8.256   -10.987 -13.198 1.00 17.20 ? 134 VAL A O   1 
ATOM   1089 C  CB  . VAL A 1 134 ? 5.931   -11.226 -15.395 1.00 19.22 ? 134 VAL A CB  1 
ATOM   1090 C  CG1 . VAL A 1 134 ? 7.326   -11.194 -16.124 1.00 23.20 ? 134 VAL A CG1 1 
ATOM   1091 C  CG2 . VAL A 1 134 ? 4.991   -12.267 -15.977 1.00 23.65 ? 134 VAL A CG2 1 
ATOM   1092 N  N   A GLU A 1 135 ? 6.640   -9.432  -12.946 0.50 16.05 ? 135 GLU A N   1 
ATOM   1093 N  N   B GLU A 1 135 ? 6.703   -9.402  -12.918 0.50 16.68 ? 135 GLU A N   1 
ATOM   1094 C  CA  A GLU A 1 135 ? 7.563   -8.548  -12.310 0.50 16.44 ? 135 GLU A CA  1 
ATOM   1095 C  CA  B GLU A 1 135 ? 7.696   -8.551  -12.234 0.50 17.39 ? 135 GLU A CA  1 
ATOM   1096 C  C   A GLU A 1 135 ? 8.037   -9.071  -10.956 0.50 15.75 ? 135 GLU A C   1 
ATOM   1097 C  C   B GLU A 1 135 ? 8.088   -9.053  -10.867 0.50 16.37 ? 135 GLU A C   1 
ATOM   1098 O  O   A GLU A 1 135 ? 9.219   -9.036  -10.675 0.50 16.74 ? 135 GLU A O   1 
ATOM   1099 O  O   B GLU A 1 135 ? 9.233   -8.909  -10.443 0.50 17.00 ? 135 GLU A O   1 
ATOM   1100 C  CB  A GLU A 1 135 ? 6.983   -7.109  -12.202 0.50 17.54 ? 135 GLU A CB  1 
ATOM   1101 C  CB  B GLU A 1 135 ? 7.238   -7.065  -12.047 0.50 19.83 ? 135 GLU A CB  1 
ATOM   1102 C  CG  A GLU A 1 135 ? 6.817   -6.442  -13.553 0.50 21.99 ? 135 GLU A CG  1 
ATOM   1103 C  CG  B GLU A 1 135 ? 7.091   -6.298  -13.327 0.50 23.87 ? 135 GLU A CG  1 
ATOM   1104 C  CD  A GLU A 1 135 ? 8.109   -5.897  -14.142 0.50 21.49 ? 135 GLU A CD  1 
ATOM   1105 C  CD  B GLU A 1 135 ? 5.804   -6.689  -14.002 0.50 25.95 ? 135 GLU A CD  1 
ATOM   1106 O  OE1 A GLU A 1 135 ? 7.985   -5.327  -15.249 0.50 26.96 ? 135 GLU A OE1 1 
ATOM   1107 O  OE1 B GLU A 1 135 ? 4.722   -6.677  -13.331 0.50 20.94 ? 135 GLU A OE1 1 
ATOM   1108 O  OE2 A GLU A 1 135 ? 9.205   -5.992  -13.531 0.50 23.35 ? 135 GLU A OE2 1 
ATOM   1109 O  OE2 B GLU A 1 135 ? 5.880   -7.077  -15.195 0.50 31.79 ? 135 GLU A OE2 1 
ATOM   1110 N  N   . ALA A 1 136 ? 7.097   -9.540  -10.113 1.00 13.66 ? 136 ALA A N   1 
ATOM   1111 C  CA  . ALA A 1 136 ? 7.401   -10.083 -8.797  1.00 14.70 ? 136 ALA A CA  1 
ATOM   1112 C  C   . ALA A 1 136 ? 8.412   -11.257 -8.832  1.00 11.88 ? 136 ALA A C   1 
ATOM   1113 O  O   . ALA A 1 136 ? 9.289   -11.367 -7.956  1.00 12.07 ? 136 ALA A O   1 
ATOM   1114 C  CB  . ALA A 1 136 ? 6.090   -10.493 -8.106  1.00 14.53 ? 136 ALA A CB  1 
ATOM   1115 N  N   . ALA A 1 137 ? 8.322   -12.041 -9.902  1.00 14.67 ? 137 ALA A N   1 
ATOM   1116 C  CA  . ALA A 1 137 ? 9.239   -13.194 -10.007 1.00 13.18 ? 137 ALA A CA  1 
ATOM   1117 C  C   . ALA A 1 137 ? 10.697  -12.842 -10.109 1.00 13.91 ? 137 ALA A C   1 
ATOM   1118 O  O   . ALA A 1 137 ? 11.515  -13.730 -9.903  1.00 15.36 ? 137 ALA A O   1 
ATOM   1119 C  CB  . ALA A 1 137 ? 8.768   -14.084 -11.201 1.00 13.61 ? 137 ALA A CB  1 
ATOM   1120 N  N   . HIS A 1 138 ? 11.045  -11.552 -10.376 1.00 13.55 ? 138 HIS A N   1 
ATOM   1121 C  CA  . HIS A 1 138 ? 12.436  -11.099 -10.469 1.00 15.01 ? 138 HIS A CA  1 
ATOM   1122 C  C   . HIS A 1 138 ? 12.898  -10.309 -9.327  1.00 17.76 ? 138 HIS A C   1 
ATOM   1123 O  O   . HIS A 1 138 ? 13.919  -9.675  -9.388  1.00 19.31 ? 138 HIS A O   1 
ATOM   1124 C  CB  . HIS A 1 138 ? 12.658  -10.286 -11.801 1.00 17.44 ? 138 HIS A CB  1 
ATOM   1125 C  CG  . HIS A 1 138 ? 12.397  -11.090 -13.036 1.00 17.87 ? 138 HIS A CG  1 
ATOM   1126 N  ND1 . HIS A 1 138 ? 13.399  -11.751 -13.692 1.00 23.27 ? 138 HIS A ND1 1 
ATOM   1127 C  CD2 . HIS A 1 138 ? 11.205  -11.442 -13.695 1.00 19.34 ? 138 HIS A CD2 1 
ATOM   1128 C  CE1 . HIS A 1 138 ? 12.872  -12.413 -14.728 1.00 18.55 ? 138 HIS A CE1 1 
ATOM   1129 N  NE2 . HIS A 1 138 ? 11.546  -12.259 -14.737 1.00 21.49 ? 138 HIS A NE2 1 
ATOM   1130 N  N   . GLU A 1 139 ? 12.176  -10.348 -8.171  1.00 15.40 ? 139 GLU A N   1 
ATOM   1131 C  CA  . GLU A 1 139 ? 12.624  -9.625  -6.970  1.00 19.52 ? 139 GLU A CA  1 
ATOM   1132 C  C   . GLU A 1 139 ? 12.711  -10.547 -5.761  1.00 15.43 ? 139 GLU A C   1 
ATOM   1133 O  O   . GLU A 1 139 ? 11.922  -11.516 -5.666  1.00 13.88 ? 139 GLU A O   1 
ATOM   1134 C  CB  . GLU A 1 139 ? 11.583  -8.631  -6.605  1.00 20.76 ? 139 GLU A CB  1 
ATOM   1135 C  CG  . GLU A 1 139 ? 11.132  -7.728  -7.701  1.00 27.83 ? 139 GLU A CG  1 
ATOM   1136 C  CD  . GLU A 1 139 ? 12.079  -6.606  -7.879  1.00 30.26 ? 139 GLU A CD  1 
ATOM   1137 O  OE1 . GLU A 1 139 ? 13.254  -6.672  -7.409  1.00 34.19 ? 139 GLU A OE1 1 
ATOM   1138 O  OE2 . GLU A 1 139 ? 11.591  -5.636  -8.557  1.00 35.52 ? 139 GLU A OE2 1 
ATOM   1139 N  N   . PRO A 1 140 ? 13.643  -10.303 -4.861  1.00 18.39 ? 140 PRO A N   1 
ATOM   1140 C  CA  . PRO A 1 140 ? 13.865  -11.254 -3.736  1.00 15.53 ? 140 PRO A CA  1 
ATOM   1141 C  C   . PRO A 1 140 ? 12.647  -11.429 -2.871  1.00 17.41 ? 140 PRO A C   1 
ATOM   1142 O  O   . PRO A 1 140 ? 12.453  -12.586 -2.385  1.00 16.43 ? 140 PRO A O   1 
ATOM   1143 C  CB  . PRO A 1 140 ? 15.061  -10.683 -2.959  1.00 17.51 ? 140 PRO A CB  1 
ATOM   1144 C  CG  . PRO A 1 140 ? 15.793  -9.856  -4.061  1.00 18.20 ? 140 PRO A CG  1 
ATOM   1145 C  CD  . PRO A 1 140 ? 14.815  -9.442  -5.115  1.00 18.49 ? 140 PRO A CD  1 
ATOM   1146 N  N   . ASP A 1 141 ? 11.791  -10.393 -2.709  1.00 14.28 ? 141 ASP A N   1 
ATOM   1147 C  CA  . ASP A 1 141 ? 10.610  -10.542 -1.897  1.00 15.03 ? 141 ASP A CA  1 
ATOM   1148 C  C   . ASP A 1 141 ? 9.387   -10.690 -2.776  1.00 13.00 ? 141 ASP A C   1 
ATOM   1149 O  O   . ASP A 1 141 ? 8.284   -10.409 -2.360  1.00 14.23 ? 141 ASP A O   1 
ATOM   1150 C  CB  . ASP A 1 141 ? 10.449  -9.293  -0.995  1.00 17.36 ? 141 ASP A CB  1 
ATOM   1151 C  CG  . ASP A 1 141 ? 10.389  -7.986  -1.819  1.00 22.48 ? 141 ASP A CG  1 
ATOM   1152 O  OD1 . ASP A 1 141 ? 10.584  -8.008  -3.039  1.00 17.76 ? 141 ASP A OD1 1 
ATOM   1153 O  OD2 . ASP A 1 141 ? 10.052  -6.937  -1.203  1.00 23.12 ? 141 ASP A OD2 1 
ATOM   1154 N  N   . GLY A 1 142 ? 9.535   -11.142 -4.011  1.00 12.41 ? 142 GLY A N   1 
ATOM   1155 C  CA  . GLY A 1 142 ? 8.422   -11.116 -4.951  1.00 10.27 ? 142 GLY A CA  1 
ATOM   1156 C  C   . GLY A 1 142 ? 7.387   -12.247 -4.759  1.00 11.12 ? 142 GLY A C   1 
ATOM   1157 O  O   . GLY A 1 142 ? 6.199   -12.082 -5.020  1.00 12.39 ? 142 GLY A O   1 
ATOM   1158 N  N   . LEU A 1 143 ? 7.923   -13.488 -4.547  1.00 10.85 ? 143 LEU A N   1 
ATOM   1159 C  CA  . LEU A 1 143 ? 6.990   -14.627 -4.593  1.00 10.79 ? 143 LEU A CA  1 
ATOM   1160 C  C   . LEU A 1 143 ? 6.981   -15.338 -3.229  1.00 9.22  ? 143 LEU A C   1 
ATOM   1161 O  O   . LEU A 1 143 ? 7.979   -15.253 -2.453  1.00 9.94  ? 143 LEU A O   1 
ATOM   1162 C  CB  . LEU A 1 143 ? 7.408   -15.688 -5.653  1.00 11.47 ? 143 LEU A CB  1 
ATOM   1163 C  CG  . LEU A 1 143 ? 7.558   -15.135 -7.049  1.00 11.94 ? 143 LEU A CG  1 
ATOM   1164 C  CD1 . LEU A 1 143 ? 8.136   -16.253 -7.963  1.00 11.54 ? 143 LEU A CD1 1 
ATOM   1165 C  CD2 . LEU A 1 143 ? 6.242   -14.595 -7.624  1.00 11.62 ? 143 LEU A CD2 1 
ATOM   1166 N  N   . ALA A 1 144 ? 5.904   -16.032 -2.967  1.00 10.74 ? 144 ALA A N   1 
ATOM   1167 C  CA  . ALA A 1 144 ? 5.840   -16.912 -1.747  1.00 10.04 ? 144 ALA A CA  1 
ATOM   1168 C  C   . ALA A 1 144 ? 5.186   -18.171 -2.200  1.00 9.82  ? 144 ALA A C   1 
ATOM   1169 O  O   . ALA A 1 144 ? 4.192   -18.144 -2.915  1.00 11.49 ? 144 ALA A O   1 
ATOM   1170 C  CB  . ALA A 1 144 ? 4.935   -16.292 -0.634  1.00 10.54 ? 144 ALA A CB  1 
ATOM   1171 N  N   . VAL A 1 145 ? 5.853   -19.318 -1.886  1.00 10.66 ? 145 VAL A N   1 
ATOM   1172 C  CA  . VAL A 1 145 ? 5.265   -20.623 -2.287  1.00 10.48 ? 145 VAL A CA  1 
ATOM   1173 C  C   . VAL A 1 145 ? 5.036   -21.478 -1.031  1.00 9.65  ? 145 VAL A C   1 
ATOM   1174 O  O   . VAL A 1 145 ? 5.983   -21.614 -0.200  1.00 11.09 ? 145 VAL A O   1 
ATOM   1175 C  CB  . VAL A 1 145 ? 6.230   -21.390 -3.251  1.00 11.46 ? 145 VAL A CB  1 
ATOM   1176 C  CG1 . VAL A 1 145 ? 5.447   -22.655 -3.692  1.00 13.09 ? 145 VAL A CG1 1 
ATOM   1177 C  CG2 . VAL A 1 145 ? 6.492   -20.514 -4.510  1.00 12.80 ? 145 VAL A CG2 1 
ATOM   1178 N  N   . LEU A 1 146 ? 3.837   -21.997 -0.938  1.00 10.51 ? 146 LEU A N   1 
ATOM   1179 C  CA  . LEU A 1 146 ? 3.411   -22.824 0.164   1.00 11.70 ? 146 LEU A CA  1 
ATOM   1180 C  C   . LEU A 1 146 ? 3.639   -24.230 -0.340  1.00 11.52 ? 146 LEU A C   1 
ATOM   1181 O  O   . LEU A 1 146 ? 3.099   -24.543 -1.416  1.00 11.73 ? 146 LEU A O   1 
ATOM   1182 C  CB  . LEU A 1 146 ? 1.934   -22.505 0.525   1.00 15.77 ? 146 LEU A CB  1 
ATOM   1183 C  CG  . LEU A 1 146 ? 1.239   -23.163 1.718   1.00 21.35 ? 146 LEU A CG  1 
ATOM   1184 C  CD1 . LEU A 1 146 ? 1.987   -22.876 3.011   1.00 22.36 ? 146 LEU A CD1 1 
ATOM   1185 C  CD2 . LEU A 1 146 ? -0.194  -22.659 1.807   1.00 26.97 ? 146 LEU A CD2 1 
ATOM   1186 N  N   . GLY A 1 147 ? 4.392   -25.041 0.397   1.00 11.16 ? 147 GLY A N   1 
ATOM   1187 C  CA  . GLY A 1 147 ? 4.568   -26.442 -0.038  1.00 12.58 ? 147 GLY A CA  1 
ATOM   1188 C  C   . GLY A 1 147 ? 3.812   -27.352 0.898   1.00 12.31 ? 147 GLY A C   1 
ATOM   1189 O  O   . GLY A 1 147 ? 3.921   -27.156 2.177   1.00 13.78 ? 147 GLY A O   1 
ATOM   1190 N  N   . VAL A 1 148 ? 3.131   -28.338 0.353   1.00 12.14 ? 148 VAL A N   1 
ATOM   1191 C  CA  . VAL A 1 148 ? 2.389   -29.293 1.230   1.00 10.91 ? 148 VAL A CA  1 
ATOM   1192 C  C   . VAL A 1 148 ? 2.810   -30.691 0.752   1.00 11.14 ? 148 VAL A C   1 
ATOM   1193 O  O   . VAL A 1 148 ? 2.718   -31.031 -0.424  1.00 12.02 ? 148 VAL A O   1 
ATOM   1194 C  CB  . VAL A 1 148 ? 0.879   -29.161 1.001   1.00 13.64 ? 148 VAL A CB  1 
ATOM   1195 C  CG1 . VAL A 1 148 ? 0.186   -30.148 1.961   1.00 12.61 ? 148 VAL A CG1 1 
ATOM   1196 C  CG2 . VAL A 1 148 ? 0.365   -27.728 1.370   1.00 13.92 ? 148 VAL A CG2 1 
ATOM   1197 N  N   . PHE A 1 149 ? 3.319   -31.495 1.690   1.00 10.40 ? 149 PHE A N   1 
ATOM   1198 C  CA  . PHE A 1 149 ? 3.658   -32.851 1.311   1.00 10.97 ? 149 PHE A CA  1 
ATOM   1199 C  C   . PHE A 1 149 ? 2.508   -33.769 1.193   1.00 12.50 ? 149 PHE A C   1 
ATOM   1200 O  O   . PHE A 1 149 ? 1.501   -33.565 1.921   1.00 13.05 ? 149 PHE A O   1 
ATOM   1201 C  CB  . PHE A 1 149 ? 4.579   -33.429 2.420   1.00 11.20 ? 149 PHE A CB  1 
ATOM   1202 C  CG  . PHE A 1 149 ? 5.882   -32.764 2.579   1.00 9.50  ? 149 PHE A CG  1 
ATOM   1203 C  CD1 . PHE A 1 149 ? 6.803   -32.746 1.471   1.00 9.48  ? 149 PHE A CD1 1 
ATOM   1204 C  CD2 . PHE A 1 149 ? 6.294   -32.188 3.741   1.00 9.74  ? 149 PHE A CD2 1 
ATOM   1205 C  CE1 . PHE A 1 149 ? 8.065   -32.224 1.586   1.00 9.80  ? 149 PHE A CE1 1 
ATOM   1206 C  CE2 . PHE A 1 149 ? 7.576   -31.610 3.879   1.00 9.65  ? 149 PHE A CE2 1 
ATOM   1207 C  CZ  . PHE A 1 149 ? 8.478   -31.629 2.782   1.00 9.25  ? 149 PHE A CZ  1 
ATOM   1208 N  N   . LEU A 1 150 ? 2.630   -34.799 0.315   1.00 11.42 ? 150 LEU A N   1 
ATOM   1209 C  CA  . LEU A 1 150 ? 1.530   -35.801 0.140   1.00 11.08 ? 150 LEU A CA  1 
ATOM   1210 C  C   . LEU A 1 150 ? 2.151   -37.146 0.476   1.00 11.99 ? 150 LEU A C   1 
ATOM   1211 O  O   . LEU A 1 150 ? 3.260   -37.474 0.075   1.00 12.29 ? 150 LEU A O   1 
ATOM   1212 C  CB  . LEU A 1 150 ? 0.954   -35.850 -1.256  1.00 12.86 ? 150 LEU A CB  1 
ATOM   1213 C  CG  . LEU A 1 150 ? -0.038  -34.755 -1.643  1.00 13.59 ? 150 LEU A CG  1 
ATOM   1214 C  CD1 . LEU A 1 150 ? 0.588   -33.380 -1.780  1.00 15.39 ? 150 LEU A CD1 1 
ATOM   1215 C  CD2 . LEU A 1 150 ? -0.710  -35.041 -2.967  1.00 17.04 ? 150 LEU A CD2 1 
ATOM   1216 N  N   . GLN A 1 151 ? 1.368   -37.909 1.248   1.00 13.22 ? 151 GLN A N   1 
ATOM   1217 C  CA  . GLN A 1 151 ? 1.745   -39.321 1.549   1.00 16.48 ? 151 GLN A CA  1 
ATOM   1218 C  C   . GLN A 1 151 ? 0.582   -40.212 1.139   1.00 13.38 ? 151 GLN A C   1 
ATOM   1219 O  O   . GLN A 1 151 ? -0.604  -39.755 0.992   1.00 14.81 ? 151 GLN A O   1 
ATOM   1220 C  CB  . GLN A 1 151 ? 1.991   -39.503 3.061   1.00 15.27 ? 151 GLN A CB  1 
ATOM   1221 C  CG  . GLN A 1 151 ? 0.775   -39.248 3.911   1.00 19.25 ? 151 GLN A CG  1 
ATOM   1222 C  CD  . GLN A 1 151 ? 1.030   -39.318 5.391   1.00 21.86 ? 151 GLN A CD  1 
ATOM   1223 O  OE1 . GLN A 1 151 ? 2.163   -39.358 5.848   1.00 22.73 ? 151 GLN A OE1 1 
ATOM   1224 N  NE2 . GLN A 1 151 ? -0.057  -39.321 6.143   1.00 24.58 ? 151 GLN A NE2 1 
ATOM   1225 N  N   . ILE A 1 152 ? 0.971   -41.465 0.825   1.00 14.61 ? 152 ILE A N   1 
ATOM   1226 C  CA  . ILE A 1 152 ? -0.071  -42.444 0.363   1.00 15.92 ? 152 ILE A CA  1 
ATOM   1227 C  C   . ILE A 1 152 ? -1.072  -42.691 1.526   1.00 18.20 ? 152 ILE A C   1 
ATOM   1228 O  O   . ILE A 1 152 ? -0.609  -42.939 2.674   1.00 19.88 ? 152 ILE A O   1 
ATOM   1229 C  CB  . ILE A 1 152 ? 0.609   -43.717 -0.125  1.00 17.19 ? 152 ILE A CB  1 
ATOM   1230 C  CG1 . ILE A 1 152 ? 1.528   -43.475 -1.349  1.00 15.82 ? 152 ILE A CG1 1 
ATOM   1231 C  CG2 . ILE A 1 152 ? -0.503  -44.740 -0.363  1.00 21.20 ? 152 ILE A CG2 1 
ATOM   1232 C  CD1 . ILE A 1 152 ? 0.769   -42.927 -2.576  1.00 18.90 ? 152 ILE A CD1 1 
ATOM   1233 N  N   . GLY A 1 153 ? -2.387  -42.551 1.324   1.00 18.60 ? 153 GLY A N   1 
ATOM   1234 C  CA  . GLY A 1 153 ? -3.423  -42.584 2.393   1.00 23.73 ? 153 GLY A CA  1 
ATOM   1235 C  C   . GLY A 1 153 ? -4.823  -42.535 1.790   1.00 27.47 ? 153 GLY A C   1 
ATOM   1236 O  O   . GLY A 1 153 ? -4.983  -42.744 0.594   1.00 34.50 ? 153 GLY A O   1 
ATOM   1237 N  N   . GLU A 1 154 ? -5.827  -42.135 2.535   1.00 27.50 ? 154 GLU A N   1 
ATOM   1238 C  CA  . GLU A 1 154 ? -7.176  -42.037 1.923   1.00 26.94 ? 154 GLU A CA  1 
ATOM   1239 C  C   . GLU A 1 154 ? -7.248  -40.892 0.843   1.00 26.76 ? 154 GLU A C   1 
ATOM   1240 O  O   . GLU A 1 154 ? -6.658  -39.768 1.120   1.00 25.29 ? 154 GLU A O   1 
ATOM   1241 C  CB  . GLU A 1 154 ? -8.164  -41.685 3.011   1.00 31.31 ? 154 GLU A CB  1 
ATOM   1242 C  CG  . GLU A 1 154 ? -8.269  -42.777 4.064   1.00 37.33 ? 154 GLU A CG  1 
ATOM   1243 C  CD  . GLU A 1 154 ? -9.281  -42.395 5.108   1.00 37.14 ? 154 GLU A CD  1 
ATOM   1244 O  OE1 . GLU A 1 154 ? -9.897  -41.309 4.982   1.00 51.22 ? 154 GLU A OE1 1 
ATOM   1245 O  OE2 . GLU A 1 154 ? -9.414  -43.128 6.082   1.00 43.10 ? 154 GLU A OE2 1 
ATOM   1246 N  N   . PRO A 1 155 ? -8.095  -41.076 -0.256  1.00 25.78 ? 155 PRO A N   1 
ATOM   1247 C  CA  . PRO A 1 155 ? -8.134  -40.139 -1.402  1.00 23.34 ? 155 PRO A CA  1 
ATOM   1248 C  C   . PRO A 1 155 ? -8.711  -38.814 -0.989  1.00 26.16 ? 155 PRO A C   1 
ATOM   1249 O  O   . PRO A 1 155 ? -9.563  -38.812 -0.075  1.00 23.93 ? 155 PRO A O   1 
ATOM   1250 C  CB  . PRO A 1 155 ? -9.007  -40.876 -2.437  1.00 26.72 ? 155 PRO A CB  1 
ATOM   1251 C  CG  . PRO A 1 155 ? -9.491  -42.165 -1.799  1.00 25.30 ? 155 PRO A CG  1 
ATOM   1252 C  CD  . PRO A 1 155 ? -8.488  -42.444 -0.694  1.00 26.19 ? 155 PRO A CD  1 
ATOM   1253 N  N   . ASN A 1 156 ? -8.198  -37.710 -1.518  1.00 25.46 ? 156 ASN A N   1 
ATOM   1254 C  CA  . ASN A 1 156 ? -8.739  -36.378 -1.187  1.00 29.86 ? 156 ASN A CA  1 
ATOM   1255 C  C   . ASN A 1 156 ? -9.677  -35.983 -2.344  1.00 28.20 ? 156 ASN A C   1 
ATOM   1256 O  O   . ASN A 1 156 ? -9.319  -36.243 -3.504  1.00 24.13 ? 156 ASN A O   1 
ATOM   1257 C  CB  . ASN A 1 156 ? -7.567  -35.425 -1.062  1.00 27.67 ? 156 ASN A CB  1 
ATOM   1258 C  CG  . ASN A 1 156 ? -7.977  -34.007 -0.700  1.00 31.94 ? 156 ASN A CG  1 
ATOM   1259 O  OD1 . ASN A 1 156 ? -8.628  -33.313 -1.514  1.00 36.14 ? 156 ASN A OD1 1 
ATOM   1260 N  ND2 . ASN A 1 156 ? -7.578  -33.536 0.514   1.00 31.60 ? 156 ASN A ND2 1 
ATOM   1261 N  N   . SER A 1 157 ? -10.849 -35.377 -2.074  1.00 20.67 ? 157 SER A N   1 
ATOM   1262 C  CA  . SER A 1 157 ? -11.825 -35.222 -3.085  1.00 22.73 ? 157 SER A CA  1 
ATOM   1263 C  C   . SER A 1 157 ? -11.410 -34.050 -3.986  1.00 23.72 ? 157 SER A C   1 
ATOM   1264 O  O   . SER A 1 157 ? -11.977 -33.939 -5.106  1.00 23.97 ? 157 SER A O   1 
ATOM   1265 C  CB  . SER A 1 157 ? -13.201 -34.905 -2.461  1.00 29.05 ? 157 SER A CB  1 
ATOM   1266 O  OG  . SER A 1 157 ? -13.241 -33.608 -1.827  1.00 29.71 ? 157 SER A OG  1 
ATOM   1267 N  N   . GLN A 1 158 ? -10.510 -33.176 -3.510  1.00 23.95 ? 158 GLN A N   1 
ATOM   1268 C  CA  . GLN A 1 158 ? -10.131 -32.064 -4.365  1.00 21.56 ? 158 GLN A CA  1 
ATOM   1269 C  C   . GLN A 1 158 ? -9.034  -32.541 -5.208  1.00 22.61 ? 158 GLN A C   1 
ATOM   1270 O  O   . GLN A 1 158 ? -8.854  -32.016 -6.334  1.00 23.95 ? 158 GLN A O   1 
ATOM   1271 C  CB  . GLN A 1 158 ? -9.806  -30.726 -3.583  1.00 21.03 ? 158 GLN A CB  1 
ATOM   1272 C  CG  . GLN A 1 158 ? -11.036 -30.113 -2.907  1.00 23.27 ? 158 GLN A CG  1 
ATOM   1273 C  CD  . GLN A 1 158 ? -12.137 -29.751 -3.898  1.00 28.95 ? 158 GLN A CD  1 
ATOM   1274 O  OE1 . GLN A 1 158 ? -11.997 -28.832 -4.745  1.00 26.98 ? 158 GLN A OE1 1 
ATOM   1275 N  NE2 . GLN A 1 158 ? -13.260 -30.474 -3.789  1.00 30.94 ? 158 GLN A NE2 1 
ATOM   1276 N  N   . LEU A 1 159 ? -8.299  -33.564 -4.726  1.00 19.95 ? 159 LEU A N   1 
ATOM   1277 C  CA  . LEU A 1 159 ? -7.377  -34.260 -5.658  1.00 18.77 ? 159 LEU A CA  1 
ATOM   1278 C  C   . LEU A 1 159 ? -8.117  -35.054 -6.708  1.00 18.28 ? 159 LEU A C   1 
ATOM   1279 O  O   . LEU A 1 159 ? -7.642  -35.141 -7.823  1.00 18.14 ? 159 LEU A O   1 
ATOM   1280 C  CB  . LEU A 1 159 ? -6.308  -35.138 -4.943  1.00 17.03 ? 159 LEU A CB  1 
ATOM   1281 C  CG  . LEU A 1 159 ? -5.379  -34.395 -4.031  1.00 18.04 ? 159 LEU A CG  1 
ATOM   1282 C  CD1 . LEU A 1 159 ? -4.440  -35.373 -3.286  1.00 18.09 ? 159 LEU A CD1 1 
ATOM   1283 C  CD2 . LEU A 1 159 ? -4.582  -33.366 -4.777  1.00 19.60 ? 159 LEU A CD2 1 
ATOM   1284 N  N   . GLN A 1 160 ? -9.237  -35.680 -6.379  1.00 17.77 ? 160 GLN A N   1 
ATOM   1285 C  CA  . GLN A 1 160 ? -10.039 -36.359 -7.403  1.00 16.86 ? 160 GLN A CA  1 
ATOM   1286 C  C   . GLN A 1 160 ? -10.598 -35.387 -8.404  1.00 15.58 ? 160 GLN A C   1 
ATOM   1287 O  O   . GLN A 1 160 ? -10.709 -35.754 -9.591  1.00 18.11 ? 160 GLN A O   1 
ATOM   1288 C  CB  . GLN A 1 160 ? -11.238 -37.090 -6.722  1.00 18.16 ? 160 GLN A CB  1 
ATOM   1289 C  CG  . GLN A 1 160 ? -11.989 -38.064 -7.632  1.00 17.56 ? 160 GLN A CG  1 
ATOM   1290 C  CD  . GLN A 1 160 ? -11.125 -39.253 -8.030  1.00 19.08 ? 160 GLN A CD  1 
ATOM   1291 O  OE1 . GLN A 1 160 ? -10.216 -39.697 -7.255  1.00 18.33 ? 160 GLN A OE1 1 
ATOM   1292 N  NE2 . GLN A 1 160 ? -11.273 -39.718 -9.249  1.00 19.21 ? 160 GLN A NE2 1 
ATOM   1293 N  N   . LYS A 1 161 ? -10.927 -34.187 -7.949  1.00 17.66 ? 161 LYS A N   1 
ATOM   1294 C  CA  . LYS A 1 161 ? -11.469 -33.141 -8.874  1.00 16.94 ? 161 LYS A CA  1 
ATOM   1295 C  C   . LYS A 1 161 ? -10.349 -32.908 -9.923  1.00 16.87 ? 161 LYS A C   1 
ATOM   1296 O  O   . LYS A 1 161 ? -10.609 -32.792 -11.134 1.00 17.83 ? 161 LYS A O   1 
ATOM   1297 C  CB  . LYS A 1 161 ? -11.757 -31.834 -8.132  1.00 18.24 ? 161 LYS A CB  1 
ATOM   1298 C  CG  . LYS A 1 161 ? -12.278 -30.697 -9.045  1.00 20.30 ? 161 LYS A CG  1 
ATOM   1299 C  CD  . LYS A 1 161 ? -12.508 -29.418 -8.244  1.00 23.21 ? 161 LYS A CD  1 
ATOM   1300 C  CE  . LYS A 1 161 ? -12.924 -28.219 -9.109  1.00 21.85 ? 161 LYS A CE  1 
ATOM   1301 N  NZ  . LYS A 1 161 ? -14.239 -28.460 -9.823  1.00 23.53 ? 161 LYS A NZ  1 
ATOM   1302 N  N   . ILE A 1 162 ? -9.109  -32.906 -9.467  1.00 16.23 ? 162 ILE A N   1 
ATOM   1303 C  CA  . ILE A 1 162 ? -7.951  -32.722 -10.411 1.00 14.06 ? 162 ILE A CA  1 
ATOM   1304 C  C   . ILE A 1 162 ? -7.822  -33.958 -11.291 1.00 16.96 ? 162 ILE A C   1 
ATOM   1305 O  O   . ILE A 1 162 ? -7.683  -33.878 -12.516 1.00 16.16 ? 162 ILE A O   1 
ATOM   1306 C  CB  . ILE A 1 162 ? -6.638  -32.346 -9.664  1.00 14.30 ? 162 ILE A CB  1 
ATOM   1307 C  CG1 . ILE A 1 162 ? -6.771  -30.973 -8.996  1.00 15.90 ? 162 ILE A CG1 1 
ATOM   1308 C  CG2 . ILE A 1 162 ? -5.413  -32.497 -10.619 1.00 13.25 ? 162 ILE A CG2 1 
ATOM   1309 C  CD1 . ILE A 1 162 ? -5.769  -30.811 -7.894  1.00 16.43 ? 162 ILE A CD1 1 
ATOM   1310 N  N   . THR A 1 163 ? -7.797  -35.175 -10.711 1.00 14.83 ? 163 THR A N   1 
ATOM   1311 C  CA  . THR A 1 163 ? -7.375  -36.293 -11.502 1.00 15.81 ? 163 THR A CA  1 
ATOM   1312 C  C   . THR A 1 163 ? -8.474  -36.609 -12.541 1.00 16.37 ? 163 THR A C   1 
ATOM   1313 O  O   . THR A 1 163 ? -8.150  -37.072 -13.606 1.00 17.70 ? 163 THR A O   1 
ATOM   1314 C  CB  . THR A 1 163 ? -7.054  -37.569 -10.694 1.00 16.73 ? 163 THR A CB  1 
ATOM   1315 O  OG1 . THR A 1 163 ? -8.208  -37.952 -9.945  1.00 18.67 ? 163 THR A OG1 1 
ATOM   1316 C  CG2 . THR A 1 163 ? -5.812  -37.356 -9.747  1.00 20.67 ? 163 THR A CG2 1 
ATOM   1317 N  N   . ASP A 1 164 ? -9.747  -36.275 -12.224 1.00 16.25 ? 164 ASP A N   1 
ATOM   1318 C  CA  . ASP A 1 164 ? -10.845 -36.451 -13.239 1.00 16.69 ? 164 ASP A CA  1 
ATOM   1319 C  C   . ASP A 1 164 ? -10.610 -35.619 -14.551 1.00 16.01 ? 164 ASP A C   1 
ATOM   1320 O  O   . ASP A 1 164 ? -11.259 -35.884 -15.552 1.00 18.37 ? 164 ASP A O   1 
ATOM   1321 C  CB  . ASP A 1 164 ? -12.190 -36.030 -12.665 1.00 16.75 ? 164 ASP A CB  1 
ATOM   1322 C  CG  . ASP A 1 164 ? -12.780 -37.080 -11.676 1.00 19.55 ? 164 ASP A CG  1 
ATOM   1323 O  OD1 . ASP A 1 164 ? -12.232 -38.214 -11.682 1.00 17.84 ? 164 ASP A OD1 1 
ATOM   1324 O  OD2 . ASP A 1 164 ? -13.728 -36.736 -10.930 1.00 20.18 ? 164 ASP A OD2 1 
ATOM   1325 N  N   . THR A 1 165 ? -9.784  -34.562 -14.492 1.00 14.04 ? 165 THR A N   1 
ATOM   1326 C  CA  . THR A 1 165 ? -9.547  -33.655 -15.658 1.00 13.82 ? 165 THR A CA  1 
ATOM   1327 C  C   . THR A 1 165 ? -8.423  -34.154 -16.527 1.00 15.81 ? 165 THR A C   1 
ATOM   1328 O  O   . THR A 1 165 ? -8.215  -33.666 -17.612 1.00 17.04 ? 165 THR A O   1 
ATOM   1329 C  CB  . THR A 1 165 ? -9.252  -32.194 -15.255 1.00 14.45 ? 165 THR A CB  1 
ATOM   1330 O  OG1 . THR A 1 165 ? -7.913  -32.087 -14.705 1.00 15.51 ? 165 THR A OG1 1 
ATOM   1331 C  CG2 . THR A 1 165 ? -10.364 -31.673 -14.347 1.00 18.02 ? 165 THR A CG2 1 
ATOM   1332 N  N   . LEU A 1 166 ? -7.592  -35.059 -16.008 1.00 15.25 ? 166 LEU A N   1 
ATOM   1333 C  CA  . LEU A 1 166 ? -6.296  -35.333 -16.651 1.00 14.82 ? 166 LEU A CA  1 
ATOM   1334 C  C   . LEU A 1 166 ? -6.408  -35.961 -18.040 1.00 16.86 ? 166 LEU A C   1 
ATOM   1335 O  O   . LEU A 1 166 ? -5.546  -35.730 -18.910 1.00 17.04 ? 166 LEU A O   1 
ATOM   1336 C  CB  . LEU A 1 166 ? -5.296  -36.107 -15.742 1.00 14.83 ? 166 LEU A CB  1 
ATOM   1337 C  CG  . LEU A 1 166 ? -5.031  -35.417 -14.365 1.00 16.49 ? 166 LEU A CG  1 
ATOM   1338 C  CD1 . LEU A 1 166 ? -4.134  -36.339 -13.522 1.00 17.68 ? 166 LEU A CD1 1 
ATOM   1339 C  CD2 . LEU A 1 166 ? -4.368  -34.053 -14.633 1.00 19.96 ? 166 LEU A CD2 1 
ATOM   1340 N  N   . ASP A 1 167 ? -7.408  -36.781 -18.266 1.00 18.48 ? 167 ASP A N   1 
ATOM   1341 C  CA  . ASP A 1 167 ? -7.584  -37.318 -19.610 1.00 19.78 ? 167 ASP A CA  1 
ATOM   1342 C  C   . ASP A 1 167 ? -7.867  -36.213 -20.600 1.00 20.05 ? 167 ASP A C   1 
ATOM   1343 O  O   . ASP A 1 167 ? -7.436  -36.328 -21.766 1.00 24.36 ? 167 ASP A O   1 
ATOM   1344 C  CB  . ASP A 1 167 ? -8.740  -38.293 -19.625 1.00 22.41 ? 167 ASP A CB  1 
ATOM   1345 C  CG  . ASP A 1 167 ? -8.366  -39.676 -19.003 1.00 25.30 ? 167 ASP A CG  1 
ATOM   1346 O  OD1 . ASP A 1 167 ? -7.188  -39.958 -18.786 1.00 29.35 ? 167 ASP A OD1 1 
ATOM   1347 O  OD2 . ASP A 1 167 ? -9.278  -40.463 -18.685 1.00 31.75 ? 167 ASP A OD2 1 
ATOM   1348 N  N   . SER A 1 168 ? -8.500  -35.131 -20.178 1.00 16.66 ? 168 SER A N   1 
ATOM   1349 C  CA  . SER A 1 168 ? -8.780  -34.080 -21.139 1.00 17.79 ? 168 SER A CA  1 
ATOM   1350 C  C   . SER A 1 168 ? -7.551  -33.154 -21.431 1.00 16.88 ? 168 SER A C   1 
ATOM   1351 O  O   . SER A 1 168 ? -7.601  -32.283 -22.309 1.00 18.04 ? 168 SER A O   1 
ATOM   1352 C  CB  . SER A 1 168 ? -9.990  -33.274 -20.685 1.00 21.33 ? 168 SER A CB  1 
ATOM   1353 O  OG  . SER A 1 168 ? -9.561  -32.423 -19.634 1.00 27.19 ? 168 SER A OG  1 
ATOM   1354 N  N   . ILE A 1 169 ? -6.511  -33.258 -20.595 1.00 16.87 ? 169 ILE A N   1 
ATOM   1355 C  CA  . ILE A 1 169 ? -5.270  -32.436 -20.719 1.00 16.21 ? 169 ILE A CA  1 
ATOM   1356 C  C   . ILE A 1 169 ? -3.988  -33.318 -20.842 1.00 15.48 ? 169 ILE A C   1 
ATOM   1357 O  O   . ILE A 1 169 ? -2.898  -32.944 -20.400 1.00 14.95 ? 169 ILE A O   1 
ATOM   1358 C  CB  . ILE A 1 169 ? -5.113  -31.357 -19.625 1.00 16.66 ? 169 ILE A CB  1 
ATOM   1359 C  CG1 . ILE A 1 169 ? -5.011  -31.974 -18.236 1.00 15.59 ? 169 ILE A CG1 1 
ATOM   1360 C  CG2 . ILE A 1 169 ? -6.351  -30.426 -19.638 1.00 17.09 ? 169 ILE A CG2 1 
ATOM   1361 C  CD1 . ILE A 1 169 ? -4.455  -30.933 -17.277 1.00 15.78 ? 169 ILE A CD1 1 
ATOM   1362 N  N   A LYS A 1 170 ? -4.112  -34.470 -21.518 0.50 14.73 ? 170 LYS A N   1 
ATOM   1363 N  N   B LYS A 1 170 ? -4.104  -34.467 -21.519 0.50 14.95 ? 170 LYS A N   1 
ATOM   1364 C  CA  A LYS A 1 170 ? -3.005  -35.419 -21.568 0.50 15.81 ? 170 LYS A CA  1 
ATOM   1365 C  CA  B LYS A 1 170 ? -2.985  -35.398 -21.567 0.50 16.16 ? 170 LYS A CA  1 
ATOM   1366 C  C   A LYS A 1 170 ? -1.758  -34.886 -22.297 0.50 15.49 ? 170 LYS A C   1 
ATOM   1367 C  C   B LYS A 1 170 ? -1.744  -34.847 -22.278 0.50 15.78 ? 170 LYS A C   1 
ATOM   1368 O  O   A LYS A 1 170 ? -0.634  -35.043 -21.811 0.50 14.98 ? 170 LYS A O   1 
ATOM   1369 O  O   B LYS A 1 170 ? -0.617  -34.970 -21.782 0.50 14.89 ? 170 LYS A O   1 
ATOM   1370 C  CB  A LYS A 1 170 ? -3.460  -36.763 -22.142 0.50 16.84 ? 170 LYS A CB  1 
ATOM   1371 C  CB  B LYS A 1 170 ? -3.398  -36.707 -22.212 0.50 17.57 ? 170 LYS A CB  1 
ATOM   1372 C  CG  A LYS A 1 170 ? -2.381  -37.839 -22.206 0.50 20.40 ? 170 LYS A CG  1 
ATOM   1373 C  CG  B LYS A 1 170 ? -2.350  -37.797 -22.112 0.50 22.04 ? 170 LYS A CG  1 
ATOM   1374 C  CD  A LYS A 1 170 ? -2.887  -39.183 -22.733 0.50 19.55 ? 170 LYS A CD  1 
ATOM   1375 C  CD  B LYS A 1 170 ? -2.211  -38.270 -20.672 0.50 20.87 ? 170 LYS A CD  1 
ATOM   1376 C  CE  A LYS A 1 170 ? -1.854  -40.312 -22.592 0.50 18.79 ? 170 LYS A CE  1 
ATOM   1377 C  CE  B LYS A 1 170 ? -3.594  -38.541 -20.116 0.50 22.39 ? 170 LYS A CE  1 
ATOM   1378 N  NZ  A LYS A 1 170 ? -1.715  -40.883 -21.177 0.50 12.84 ? 170 LYS A NZ  1 
ATOM   1379 N  NZ  B LYS A 1 170 ? -3.759  -38.072 -18.719 0.50 20.97 ? 170 LYS A NZ  1 
ATOM   1380 N  N   . GLU A 1 171 ? -1.966  -34.138 -23.393 1.00 15.16 ? 171 GLU A N   1 
ATOM   1381 C  CA  . GLU A 1 171 ? -0.881  -33.614 -24.210 1.00 16.98 ? 171 GLU A CA  1 
ATOM   1382 C  C   . GLU A 1 171 ? -0.475  -32.214 -23.730 1.00 18.41 ? 171 GLU A C   1 
ATOM   1383 O  O   . GLU A 1 171 ? -1.270  -31.404 -23.251 1.00 16.38 ? 171 GLU A O   1 
ATOM   1384 C  CB  . GLU A 1 171 ? -1.231  -33.521 -25.727 1.00 17.86 ? 171 GLU A CB  1 
ATOM   1385 C  CG  . GLU A 1 171 ? -1.740  -34.867 -26.370 1.00 20.66 ? 171 GLU A CG  1 
ATOM   1386 C  CD  . GLU A 1 171 ? -3.154  -35.289 -25.947 1.00 23.66 ? 171 GLU A CD  1 
ATOM   1387 O  OE1 . GLU A 1 171 ? -3.391  -36.521 -26.044 1.00 32.35 ? 171 GLU A OE1 1 
ATOM   1388 O  OE2 . GLU A 1 171 ? -4.034  -34.508 -25.486 1.00 29.58 ? 171 GLU A OE2 1 
ATOM   1389 N  N   . LYS A 1 172 ? 0.790   -31.928 -23.822 1.00 17.53 ? 172 LYS A N   1 
ATOM   1390 C  CA  . LYS A 1 172 ? 1.314   -30.606 -23.417 1.00 16.34 ? 172 LYS A CA  1 
ATOM   1391 C  C   . LYS A 1 172 ? 0.568   -29.477 -24.130 1.00 17.04 ? 172 LYS A C   1 
ATOM   1392 O  O   . LYS A 1 172 ? 0.415   -29.490 -25.360 1.00 19.07 ? 172 LYS A O   1 
ATOM   1393 C  CB  . LYS A 1 172 ? 2.820   -30.530 -23.821 1.00 16.77 ? 172 LYS A CB  1 
ATOM   1394 C  CG  . LYS A 1 172 ? 3.499   -29.198 -23.508 1.00 15.86 ? 172 LYS A CG  1 
ATOM   1395 C  CD  . LYS A 1 172 ? 5.006   -29.184 -23.824 1.00 21.19 ? 172 LYS A CD  1 
ATOM   1396 C  CE  . LYS A 1 172 ? 5.680   -27.875 -23.426 1.00 23.10 ? 172 LYS A CE  1 
ATOM   1397 N  NZ  . LYS A 1 172 ? 7.156   -27.946 -23.620 1.00 33.75 ? 172 LYS A NZ  1 
ATOM   1398 N  N   . GLY A 1 173 ? 0.222   -28.441 -23.377 1.00 14.75 ? 173 GLY A N   1 
ATOM   1399 C  CA  . GLY A 1 173 ? -0.557  -27.309 -23.965 1.00 16.04 ? 173 GLY A CA  1 
ATOM   1400 C  C   . GLY A 1 173 ? -2.062  -27.379 -23.851 1.00 17.41 ? 173 GLY A C   1 
ATOM   1401 O  O   . GLY A 1 173 ? -2.721  -26.323 -24.056 1.00 19.56 ? 173 GLY A O   1 
ATOM   1402 N  N   A LYS A 1 174 ? -2.649  -28.570 -23.627 0.50 15.00 ? 174 LYS A N   1 
ATOM   1403 N  N   B LYS A 1 174 ? -2.650  -28.563 -23.595 0.50 15.13 ? 174 LYS A N   1 
ATOM   1404 C  CA  A LYS A 1 174 ? -4.070  -28.678 -23.432 0.50 15.39 ? 174 LYS A CA  1 
ATOM   1405 C  CA  B LYS A 1 174 ? -4.081  -28.689 -23.430 0.50 15.64 ? 174 LYS A CA  1 
ATOM   1406 C  C   A LYS A 1 174 ? -4.481  -27.991 -22.109 0.50 14.44 ? 174 LYS A C   1 
ATOM   1407 C  C   B LYS A 1 174 ? -4.581  -28.152 -22.074 0.50 14.55 ? 174 LYS A C   1 
ATOM   1408 O  O   A LYS A 1 174 ? -3.668  -27.897 -21.130 0.50 12.71 ? 174 LYS A O   1 
ATOM   1409 O  O   B LYS A 1 174 ? -3.942  -28.294 -21.038 0.50 14.02 ? 174 LYS A O   1 
ATOM   1410 C  CB  A LYS A 1 174 ? -4.528  -30.152 -23.409 0.50 15.69 ? 174 LYS A CB  1 
ATOM   1411 C  CB  B LYS A 1 174 ? -4.529  -30.144 -23.584 0.50 15.91 ? 174 LYS A CB  1 
ATOM   1412 C  CG  A LYS A 1 174 ? -4.288  -30.923 -24.710 0.50 17.47 ? 174 LYS A CG  1 
ATOM   1413 C  CG  B LYS A 1 174 ? -4.366  -30.649 -25.010 0.50 17.99 ? 174 LYS A CG  1 
ATOM   1414 C  CD  A LYS A 1 174 ? -5.198  -30.433 -25.837 0.50 19.67 ? 174 LYS A CD  1 
ATOM   1415 C  CD  B LYS A 1 174 ? -5.262  -31.846 -25.315 0.50 17.36 ? 174 LYS A CD  1 
ATOM   1416 C  CE  A LYS A 1 174 ? -4.778  -31.152 -27.112 0.50 18.93 ? 174 LYS A CE  1 
ATOM   1417 C  CE  B LYS A 1 174 ? -6.776  -31.592 -25.325 0.50 22.12 ? 174 LYS A CE  1 
ATOM   1418 N  NZ  A LYS A 1 174 ? -5.323  -32.518 -26.965 0.50 22.56 ? 174 LYS A NZ  1 
ATOM   1419 N  NZ  B LYS A 1 174 ? -7.632  -32.769 -24.957 0.50 26.41 ? 174 LYS A NZ  1 
ATOM   1420 N  N   . GLN A 1 175 ? -5.720  -27.490 -22.118 1.00 13.84 ? 175 GLN A N   1 
ATOM   1421 C  CA  . GLN A 1 175 ? -6.333  -26.963 -20.893 1.00 13.56 ? 175 GLN A CA  1 
ATOM   1422 C  C   . GLN A 1 175 ? -7.786  -27.159 -20.859 1.00 15.61 ? 175 GLN A C   1 
ATOM   1423 O  O   . GLN A 1 175 ? -8.370  -27.592 -21.841 1.00 16.73 ? 175 GLN A O   1 
ATOM   1424 C  CB  . GLN A 1 175 ? -5.941  -25.515 -20.708 1.00 13.16 ? 175 GLN A CB  1 
ATOM   1425 C  CG  . GLN A 1 175 ? -6.471  -24.633 -21.859 1.00 13.31 ? 175 GLN A CG  1 
ATOM   1426 C  CD  . GLN A 1 175 ? -6.231  -23.181 -21.595 1.00 15.24 ? 175 GLN A CD  1 
ATOM   1427 O  OE1 . GLN A 1 175 ? -7.232  -22.420 -21.372 1.00 19.82 ? 175 GLN A OE1 1 
ATOM   1428 N  NE2 . GLN A 1 175 ? -5.005  -22.725 -21.634 1.00 15.46 ? 175 GLN A NE2 1 
ATOM   1429 N  N   . THR A 1 176 ? -8.413  -26.975 -19.712 1.00 14.57 ? 176 THR A N   1 
ATOM   1430 C  CA  . THR A 1 176 ? -9.828  -27.143 -19.600 1.00 15.08 ? 176 THR A CA  1 
ATOM   1431 C  C   . THR A 1 176 ? -10.323 -26.264 -18.439 1.00 14.22 ? 176 THR A C   1 
ATOM   1432 O  O   . THR A 1 176 ? -9.587  -26.025 -17.495 1.00 14.48 ? 176 THR A O   1 
ATOM   1433 C  CB  . THR A 1 176 ? -10.301 -28.651 -19.510 1.00 16.53 ? 176 THR A CB  1 
ATOM   1434 O  OG1 . THR A 1 176 ? -11.731 -28.773 -19.670 1.00 18.25 ? 176 THR A OG1 1 
ATOM   1435 C  CG2 . THR A 1 176 ? -9.908  -29.288 -18.189 1.00 17.82 ? 176 THR A CG2 1 
ATOM   1436 N  N   . ARG A 1 177 ? -11.602 -25.887 -18.457 1.00 15.89 ? 177 ARG A N   1 
ATOM   1437 C  CA  . ARG A 1 177 ? -12.225 -25.092 -17.363 1.00 15.46 ? 177 ARG A CA  1 
ATOM   1438 C  C   . ARG A 1 177 ? -12.034 -25.816 -16.007 1.00 16.64 ? 177 ARG A C   1 
ATOM   1439 O  O   . ARG A 1 177 ? -12.193 -27.070 -15.885 1.00 17.39 ? 177 ARG A O   1 
ATOM   1440 C  CB  . ARG A 1 177 ? -13.696 -24.950 -17.686 1.00 16.97 ? 177 ARG A CB  1 
ATOM   1441 C  CG  . ARG A 1 177 ? -14.539 -24.165 -16.622 1.00 17.28 ? 177 ARG A CG  1 
ATOM   1442 C  CD  . ARG A 1 177 ? -14.039 -22.712 -16.598 1.00 20.67 ? 177 ARG A CD  1 
ATOM   1443 N  NE  . ARG A 1 177 ? -14.932 -21.837 -15.797 1.00 19.19 ? 177 ARG A NE  1 
ATOM   1444 C  CZ  . ARG A 1 177 ? -14.571 -20.669 -15.215 1.00 20.41 ? 177 ARG A CZ  1 
ATOM   1445 N  NH1 . ARG A 1 177 ? -13.326 -20.190 -15.259 1.00 18.83 ? 177 ARG A NH1 1 
ATOM   1446 N  NH2 . ARG A 1 177 ? -15.536 -19.942 -14.570 1.00 23.44 ? 177 ARG A NH2 1 
ATOM   1447 N  N   . PHE A 1 178 ? -11.723 -25.000 -14.999 1.00 15.48 ? 178 PHE A N   1 
ATOM   1448 C  CA  . PHE A 1 178 ? -11.573 -25.549 -13.673 1.00 16.19 ? 178 PHE A CA  1 
ATOM   1449 C  C   . PHE A 1 178 ? -11.875 -24.475 -12.654 1.00 14.30 ? 178 PHE A C   1 
ATOM   1450 O  O   . PHE A 1 178 ? -11.106 -23.557 -12.431 1.00 17.84 ? 178 PHE A O   1 
ATOM   1451 C  CB  . PHE A 1 178 ? -10.118 -26.033 -13.535 1.00 16.66 ? 178 PHE A CB  1 
ATOM   1452 C  CG  . PHE A 1 178 ? -9.886  -26.940 -12.370 1.00 15.71 ? 178 PHE A CG  1 
ATOM   1453 C  CD1 . PHE A 1 178 ? -10.181 -28.313 -12.470 1.00 17.07 ? 178 PHE A CD1 1 
ATOM   1454 C  CD2 . PHE A 1 178 ? -9.333  -26.436 -11.189 1.00 15.40 ? 178 PHE A CD2 1 
ATOM   1455 C  CE1 . PHE A 1 178 ? -9.907  -29.183 -11.394 1.00 16.98 ? 178 PHE A CE1 1 
ATOM   1456 C  CE2 . PHE A 1 178 ? -9.150  -27.332 -10.085 1.00 16.02 ? 178 PHE A CE2 1 
ATOM   1457 C  CZ  . PHE A 1 178 ? -9.389  -28.686 -10.252 1.00 16.14 ? 178 PHE A CZ  1 
ATOM   1458 N  N   . THR A 1 179 ? -13.005 -24.663 -11.974 1.00 16.90 ? 179 THR A N   1 
ATOM   1459 C  CA  . THR A 1 179 ? -13.416 -23.638 -10.992 1.00 17.16 ? 179 THR A CA  1 
ATOM   1460 C  C   . THR A 1 179 ? -14.137 -24.349 -9.841  1.00 17.79 ? 179 THR A C   1 
ATOM   1461 O  O   . THR A 1 179 ? -14.295 -25.569 -9.860  1.00 18.32 ? 179 THR A O   1 
ATOM   1462 C  CB  . THR A 1 179 ? -14.244 -22.399 -11.562 1.00 19.93 ? 179 THR A CB  1 
ATOM   1463 O  OG1 . THR A 1 179 ? -14.209 -21.292 -10.598 1.00 19.50 ? 179 THR A OG1 1 
ATOM   1464 C  CG2 . THR A 1 179 ? -15.655 -22.797 -11.939 1.00 21.93 ? 179 THR A CG2 1 
ATOM   1465 N  N   A ASN A 1 180 ? -14.482 -23.556 -8.818  0.50 17.94 ? 180 ASN A N   1 
ATOM   1466 N  N   B ASN A 1 180 ? -14.596 -23.577 -8.853  0.50 18.03 ? 180 ASN A N   1 
ATOM   1467 C  CA  A ASN A 1 180 ? -15.214 -24.057 -7.627  0.50 20.26 ? 180 ASN A CA  1 
ATOM   1468 C  CA  B ASN A 1 180 ? -15.246 -24.171 -7.655  0.50 19.33 ? 180 ASN A CA  1 
ATOM   1469 C  C   A ASN A 1 180 ? -14.297 -25.051 -6.931  0.50 19.64 ? 180 ASN A C   1 
ATOM   1470 C  C   B ASN A 1 180 ? -14.239 -25.178 -7.125  0.50 18.29 ? 180 ASN A C   1 
ATOM   1471 O  O   A ASN A 1 180 ? -14.721 -26.104 -6.465  0.50 21.22 ? 180 ASN A O   1 
ATOM   1472 O  O   B ASN A 1 180 ? -14.544 -26.387 -6.991  0.50 18.23 ? 180 ASN A O   1 
ATOM   1473 C  CB  A ASN A 1 180 ? -16.574 -24.639 -8.017  0.50 20.74 ? 180 ASN A CB  1 
ATOM   1474 C  CB  B ASN A 1 180 ? -16.592 -24.834 -7.973  0.50 20.15 ? 180 ASN A CB  1 
ATOM   1475 C  CG  A ASN A 1 180 ? -17.505 -23.587 -8.598  0.50 21.28 ? 180 ASN A CG  1 
ATOM   1476 C  CG  B ASN A 1 180 ? -17.394 -25.150 -6.712  0.50 20.64 ? 180 ASN A CG  1 
ATOM   1477 O  OD1 A ASN A 1 180 ? -17.579 -22.469 -8.106  0.50 23.56 ? 180 ASN A OD1 1 
ATOM   1478 O  OD1 B ASN A 1 180 ? -17.148 -24.575 -5.633  0.50 21.70 ? 180 ASN A OD1 1 
ATOM   1479 N  ND2 A ASN A 1 180 ? -18.170 -23.931 -9.687  0.50 23.97 ? 180 ASN A ND2 1 
ATOM   1480 N  ND2 B ASN A 1 180 ? -18.344 -26.074 -6.836  0.50 23.85 ? 180 ASN A ND2 1 
ATOM   1481 N  N   . PHE A 1 181 ? -13.020 -24.677 -6.886  1.00 18.50 ? 181 PHE A N   1 
ATOM   1482 C  CA  . PHE A 1 181 ? -11.889 -25.543 -6.406  1.00 18.76 ? 181 PHE A CA  1 
ATOM   1483 C  C   . PHE A 1 181 ? -11.637 -25.194 -4.994  1.00 18.25 ? 181 PHE A C   1 
ATOM   1484 O  O   . PHE A 1 181 ? -11.227 -24.092 -4.630  1.00 20.83 ? 181 PHE A O   1 
ATOM   1485 C  CB  . PHE A 1 181 ? -10.642 -25.305 -7.295  1.00 18.76 ? 181 PHE A CB  1 
ATOM   1486 C  CG  . PHE A 1 181 ? -9.392  -26.011 -6.868  1.00 17.53 ? 181 PHE A CG  1 
ATOM   1487 C  CD1 . PHE A 1 181 ? -9.416  -27.370 -6.651  1.00 17.93 ? 181 PHE A CD1 1 
ATOM   1488 C  CD2 . PHE A 1 181 ? -8.146  -25.307 -6.848  1.00 17.87 ? 181 PHE A CD2 1 
ATOM   1489 C  CE1 . PHE A 1 181 ? -8.260  -28.026 -6.230  1.00 19.35 ? 181 PHE A CE1 1 
ATOM   1490 C  CE2 . PHE A 1 181 ? -6.953  -25.992 -6.489  1.00 16.95 ? 181 PHE A CE2 1 
ATOM   1491 C  CZ  . PHE A 1 181 ? -7.057  -27.362 -6.201  1.00 17.50 ? 181 PHE A CZ  1 
ATOM   1492 N  N   . ASP A 1 182 ? -11.887 -26.171 -4.149  1.00 20.89 ? 182 ASP A N   1 
ATOM   1493 C  CA  . ASP A 1 182 ? -11.650 -25.898 -2.726  1.00 24.20 ? 182 ASP A CA  1 
ATOM   1494 C  C   . ASP A 1 182 ? -10.179 -26.178 -2.276  1.00 21.54 ? 182 ASP A C   1 
ATOM   1495 O  O   . ASP A 1 182 ? -9.812  -27.203 -1.685  1.00 23.75 ? 182 ASP A O   1 
ATOM   1496 C  CB  . ASP A 1 182 ? -12.681 -26.590 -1.833  1.00 28.37 ? 182 ASP A CB  1 
ATOM   1497 C  CG  . ASP A 1 182 ? -12.387 -26.347 -0.384  1.00 38.75 ? 182 ASP A CG  1 
ATOM   1498 O  OD1 . ASP A 1 182 ? -11.665 -25.322 -0.148  1.00 42.05 ? 182 ASP A OD1 1 
ATOM   1499 O  OD2 . ASP A 1 182 ? -12.843 -27.160 0.477   1.00 41.14 ? 182 ASP A OD2 1 
ATOM   1500 N  N   . LEU A 1 183 ? -9.352  -25.236 -2.612  1.00 20.36 ? 183 LEU A N   1 
ATOM   1501 C  CA  . LEU A 1 183 ? -7.971  -25.405 -2.362  1.00 20.37 ? 183 LEU A CA  1 
ATOM   1502 C  C   . LEU A 1 183 ? -7.678  -25.575 -0.879  1.00 20.79 ? 183 LEU A C   1 
ATOM   1503 O  O   . LEU A 1 183 ? -6.737  -26.301 -0.523  1.00 20.48 ? 183 LEU A O   1 
ATOM   1504 C  CB  . LEU A 1 183 ? -7.218  -24.172 -2.911  1.00 19.47 ? 183 LEU A CB  1 
ATOM   1505 C  CG  . LEU A 1 183 ? -5.723  -24.121 -2.696  1.00 18.77 ? 183 LEU A CG  1 
ATOM   1506 C  CD1 . LEU A 1 183 ? -5.004  -25.307 -3.347  1.00 17.16 ? 183 LEU A CD1 1 
ATOM   1507 C  CD2 . LEU A 1 183 ? -5.212  -22.837 -3.355  1.00 21.03 ? 183 LEU A CD2 1 
ATOM   1508 N  N   . LEU A 1 184 ? -8.428  -24.864 0.000   1.00 20.33 ? 184 LEU A N   1 
ATOM   1509 C  CA  . LEU A 1 184 ? -8.097  -24.948 1.432   1.00 22.92 ? 184 LEU A CA  1 
ATOM   1510 C  C   . LEU A 1 184 ? -8.232  -26.388 1.944   1.00 20.02 ? 184 LEU A C   1 
ATOM   1511 O  O   . LEU A 1 184 ? -7.581  -26.721 2.958   1.00 19.37 ? 184 LEU A O   1 
ATOM   1512 C  CB  . LEU A 1 184 ? -8.952  -23.966 2.259   1.00 24.18 ? 184 LEU A CB  1 
ATOM   1513 C  CG  . LEU A 1 184 ? -8.690  -22.424 2.238   1.00 25.65 ? 184 LEU A CG  1 
ATOM   1514 C  CD1 . LEU A 1 184 ? -9.879  -21.654 2.884   1.00 29.90 ? 184 LEU A CD1 1 
ATOM   1515 C  CD2 . LEU A 1 184 ? -7.400  -22.078 2.940   1.00 28.95 ? 184 LEU A CD2 1 
ATOM   1516 N  N   . SER A 1 185 ? -9.041  -27.220 1.285   1.00 19.97 ? 185 SER A N   1 
ATOM   1517 C  CA  . SER A 1 185 ? -9.124  -28.655 1.529   1.00 20.93 ? 185 SER A CA  1 
ATOM   1518 C  C   . SER A 1 185 ? -7.895  -29.443 1.287   1.00 22.34 ? 185 SER A C   1 
ATOM   1519 O  O   . SER A 1 185 ? -7.785  -30.574 1.700   1.00 22.58 ? 185 SER A O   1 
ATOM   1520 C  CB  . SER A 1 185 ? -10.274 -29.293 0.720   1.00 28.95 ? 185 SER A CB  1 
ATOM   1521 O  OG  . SER A 1 185 ? -11.462 -28.914 1.377   1.00 34.53 ? 185 SER A OG  1 
ATOM   1522 N  N   . LEU A 1 186 ? -6.947  -28.874 0.552   1.00 21.58 ? 186 LEU A N   1 
ATOM   1523 C  CA  . LEU A 1 186 ? -5.653  -29.551 0.355   1.00 19.60 ? 186 LEU A CA  1 
ATOM   1524 C  C   . LEU A 1 186 ? -4.531  -29.151 1.324   1.00 20.92 ? 186 LEU A C   1 
ATOM   1525 O  O   . LEU A 1 186 ? -3.285  -29.371 1.061   1.00 19.70 ? 186 LEU A O   1 
ATOM   1526 C  CB  . LEU A 1 186 ? -5.168  -29.310 -1.082  1.00 21.01 ? 186 LEU A CB  1 
ATOM   1527 C  CG  . LEU A 1 186 ? -6.100  -29.845 -2.188  1.00 21.52 ? 186 LEU A CG  1 
ATOM   1528 C  CD1 . LEU A 1 186 ? -5.541  -29.484 -3.571  1.00 22.57 ? 186 LEU A CD1 1 
ATOM   1529 C  CD2 . LEU A 1 186 ? -6.261  -31.369 -2.080  1.00 19.57 ? 186 LEU A CD2 1 
ATOM   1530 N  N   . LEU A 1 187 ? -4.926  -28.409 2.352   1.00 17.16 ? 187 LEU A N   1 
ATOM   1531 C  CA  . LEU A 1 187 ? -4.001  -28.038 3.382   1.00 18.03 ? 187 LEU A CA  1 
ATOM   1532 C  C   . LEU A 1 187 ? -4.337  -28.991 4.565   1.00 16.93 ? 187 LEU A C   1 
ATOM   1533 O  O   . LEU A 1 187 ? -5.475  -29.394 4.693   1.00 18.43 ? 187 LEU A O   1 
ATOM   1534 C  CB  . LEU A 1 187 ? -4.228  -26.610 3.826   1.00 18.29 ? 187 LEU A CB  1 
ATOM   1535 C  CG  . LEU A 1 187 ? -4.051  -25.574 2.688   1.00 21.02 ? 187 LEU A CG  1 
ATOM   1536 C  CD1 . LEU A 1 187 ? -3.980  -24.171 3.267   1.00 22.62 ? 187 LEU A CD1 1 
ATOM   1537 C  CD2 . LEU A 1 187 ? -2.763  -25.782 1.994   1.00 19.24 ? 187 LEU A CD2 1 
ATOM   1538 N  N   . PRO A 1 188 ? -3.295  -29.328 5.348   1.00 17.23 ? 188 PRO A N   1 
ATOM   1539 C  CA  . PRO A 1 188 ? -3.465  -30.200 6.519   1.00 17.53 ? 188 PRO A CA  1 
ATOM   1540 C  C   . PRO A 1 188 ? -4.099  -29.360 7.636   1.00 18.42 ? 188 PRO A C   1 
ATOM   1541 O  O   . PRO A 1 188 ? -4.135  -28.131 7.576   1.00 16.56 ? 188 PRO A O   1 
ATOM   1542 C  CB  . PRO A 1 188 ? -2.020  -30.604 6.854   1.00 16.34 ? 188 PRO A CB  1 
ATOM   1543 C  CG  . PRO A 1 188 ? -1.249  -29.376 6.470   1.00 15.31 ? 188 PRO A CG  1 
ATOM   1544 C  CD  . PRO A 1 188 ? -1.883  -28.995 5.132   1.00 15.30 ? 188 PRO A CD  1 
ATOM   1545 N  N   . PRO A 1 189 ? -4.639  -30.033 8.654   1.00 18.37 ? 189 PRO A N   1 
ATOM   1546 C  CA  . PRO A 1 189 ? -5.245  -29.246 9.715   1.00 19.63 ? 189 PRO A CA  1 
ATOM   1547 C  C   . PRO A 1 189 ? -4.255  -28.476 10.566  1.00 19.38 ? 189 PRO A C   1 
ATOM   1548 O  O   . PRO A 1 189 ? -4.745  -27.490 11.162  1.00 21.79 ? 189 PRO A O   1 
ATOM   1549 C  CB  . PRO A 1 189 ? -6.036  -30.257 10.586  1.00 21.45 ? 189 PRO A CB  1 
ATOM   1550 C  CG  . PRO A 1 189 ? -5.471  -31.588 10.175  1.00 21.17 ? 189 PRO A CG  1 
ATOM   1551 C  CD  . PRO A 1 189 ? -4.773  -31.485 8.814   1.00 20.43 ? 189 PRO A CD  1 
ATOM   1552 N  N   . SER A 1 190 ? -2.965  -28.888 10.680  1.00 15.62 ? 190 SER A N   1 
ATOM   1553 C  CA  . SER A 1 190 ? -1.951  -28.148 11.343  1.00 16.30 ? 190 SER A CA  1 
ATOM   1554 C  C   . SER A 1 190 ? -1.269  -27.260 10.288  1.00 17.66 ? 190 SER A C   1 
ATOM   1555 O  O   . SER A 1 190 ? -0.773  -27.750 9.260   1.00 14.88 ? 190 SER A O   1 
ATOM   1556 C  CB  . SER A 1 190 ? -0.872  -29.046 11.997  1.00 19.44 ? 190 SER A CB  1 
ATOM   1557 O  OG  . SER A 1 190 ? 0.168   -28.286 12.524  1.00 20.81 ? 190 SER A OG  1 
ATOM   1558 N  N   . TRP A 1 191 ? -1.237  -25.956 10.577  1.00 16.73 ? 191 TRP A N   1 
ATOM   1559 C  CA  . TRP A 1 191 ? -0.436  -25.033 9.737   1.00 16.74 ? 191 TRP A CA  1 
ATOM   1560 C  C   . TRP A 1 191 ? 0.925   -24.705 10.286  1.00 16.40 ? 191 TRP A C   1 
ATOM   1561 O  O   . TRP A 1 191 ? 1.508   -23.667 9.944   1.00 20.25 ? 191 TRP A O   1 
ATOM   1562 C  CB  . TRP A 1 191 ? -1.311  -23.798 9.416   1.00 15.49 ? 191 TRP A CB  1 
ATOM   1563 C  CG  . TRP A 1 191 ? -2.510  -24.057 8.549   1.00 16.65 ? 191 TRP A CG  1 
ATOM   1564 C  CD1 . TRP A 1 191 ? -2.970  -25.245 8.008   1.00 15.47 ? 191 TRP A CD1 1 
ATOM   1565 C  CD2 . TRP A 1 191 ? -3.473  -23.072 8.104   1.00 17.22 ? 191 TRP A CD2 1 
ATOM   1566 N  NE1 . TRP A 1 191 ? -4.119  -25.107 7.276   1.00 17.97 ? 191 TRP A NE1 1 
ATOM   1567 C  CE2 . TRP A 1 191 ? -4.469  -23.783 7.308   1.00 16.66 ? 191 TRP A CE2 1 
ATOM   1568 C  CE3 . TRP A 1 191 ? -3.589  -21.671 8.283   1.00 21.18 ? 191 TRP A CE3 1 
ATOM   1569 C  CZ2 . TRP A 1 191 ? -5.550  -23.145 6.725   1.00 19.25 ? 191 TRP A CZ2 1 
ATOM   1570 C  CZ3 . TRP A 1 191 ? -4.696  -21.059 7.682   1.00 17.37 ? 191 TRP A CZ3 1 
ATOM   1571 C  CH2 . TRP A 1 191 ? -5.629  -21.755 6.922   1.00 18.44 ? 191 TRP A CH2 1 
ATOM   1572 N  N   . ASP A 1 192 ? 1.547   -25.593 11.076  1.00 17.46 ? 192 ASP A N   1 
ATOM   1573 C  CA  . ASP A 1 192 ? 2.918   -25.376 11.471  1.00 14.76 ? 192 ASP A CA  1 
ATOM   1574 C  C   . ASP A 1 192 ? 3.845   -25.491 10.188  1.00 15.70 ? 192 ASP A C   1 
ATOM   1575 O  O   . ASP A 1 192 ? 3.583   -26.354 9.335   1.00 15.76 ? 192 ASP A O   1 
ATOM   1576 C  CB  . ASP A 1 192 ? 3.440   -26.458 12.452  1.00 19.57 ? 192 ASP A CB  1 
ATOM   1577 C  CG  . ASP A 1 192 ? 2.743   -26.474 13.826  1.00 28.73 ? 192 ASP A CG  1 
ATOM   1578 O  OD1 . ASP A 1 192 ? 2.432   -25.430 14.375  1.00 21.87 ? 192 ASP A OD1 1 
ATOM   1579 O  OD2 . ASP A 1 192 ? 2.662   -27.597 14.398  1.00 34.21 ? 192 ASP A OD2 1 
ATOM   1580 N  N   . TYR A 1 193 ? 4.895   -24.667 10.185  1.00 13.67 ? 193 TYR A N   1 
ATOM   1581 C  CA  . TYR A 1 193 ? 5.735   -24.595 8.965   1.00 14.06 ? 193 TYR A CA  1 
ATOM   1582 C  C   . TYR A 1 193 ? 7.147   -24.311 9.233   1.00 13.93 ? 193 TYR A C   1 
ATOM   1583 O  O   . TYR A 1 193 ? 7.603   -23.791 10.269  1.00 15.84 ? 193 TYR A O   1 
ATOM   1584 C  CB  . TYR A 1 193 ? 5.187   -23.484 7.985   1.00 14.45 ? 193 TYR A CB  1 
ATOM   1585 C  CG  . TYR A 1 193 ? 5.208   -22.089 8.550   1.00 13.56 ? 193 TYR A CG  1 
ATOM   1586 C  CD1 . TYR A 1 193 ? 6.364   -21.315 8.373   1.00 14.07 ? 193 TYR A CD1 1 
ATOM   1587 C  CD2 . TYR A 1 193 ? 4.087   -21.585 9.243   1.00 15.33 ? 193 TYR A CD2 1 
ATOM   1588 C  CE1 . TYR A 1 193 ? 6.487   -20.027 8.922   1.00 14.70 ? 193 TYR A CE1 1 
ATOM   1589 C  CE2 . TYR A 1 193 ? 4.174   -20.325 9.770   1.00 14.50 ? 193 TYR A CE2 1 
ATOM   1590 C  CZ  . TYR A 1 193 ? 5.349   -19.553 9.634   1.00 14.53 ? 193 TYR A CZ  1 
ATOM   1591 O  OH  . TYR A 1 193 ? 5.518   -18.274 10.154  1.00 16.03 ? 193 TYR A OH  1 
ATOM   1592 N  N   . TRP A 1 194 ? 7.946   -24.642 8.193   1.00 11.49 ? 194 TRP A N   1 
ATOM   1593 C  CA  . TRP A 1 194 ? 9.276   -24.208 8.078   1.00 11.78 ? 194 TRP A CA  1 
ATOM   1594 C  C   . TRP A 1 194 ? 9.432   -23.162 6.972   1.00 11.72 ? 194 TRP A C   1 
ATOM   1595 O  O   . TRP A 1 194 ? 8.610   -23.125 6.074   1.00 11.86 ? 194 TRP A O   1 
ATOM   1596 C  CB  . TRP A 1 194 ? 10.203  -25.340 7.697   1.00 14.90 ? 194 TRP A CB  1 
ATOM   1597 C  CG  . TRP A 1 194 ? 10.338  -26.426 8.734   1.00 13.77 ? 194 TRP A CG  1 
ATOM   1598 C  CD1 . TRP A 1 194 ? 11.053  -26.418 9.936   1.00 17.24 ? 194 TRP A CD1 1 
ATOM   1599 C  CD2 . TRP A 1 194 ? 9.791   -27.770 8.578   1.00 15.03 ? 194 TRP A CD2 1 
ATOM   1600 N  NE1 . TRP A 1 194 ? 10.977  -27.664 10.528  1.00 16.75 ? 194 TRP A NE1 1 
ATOM   1601 C  CE2 . TRP A 1 194 ? 10.218  -28.515 9.743   1.00 16.49 ? 194 TRP A CE2 1 
ATOM   1602 C  CE3 . TRP A 1 194 ? 9.056   -28.407 7.602   1.00 13.62 ? 194 TRP A CE3 1 
ATOM   1603 C  CZ2 . TRP A 1 194 ? 9.873   -29.870 9.906   1.00 17.06 ? 194 TRP A CZ2 1 
ATOM   1604 C  CZ3 . TRP A 1 194 ? 8.711   -29.756 7.741   1.00 14.39 ? 194 TRP A CZ3 1 
ATOM   1605 C  CH2 . TRP A 1 194 ? 9.117   -30.476 8.889   1.00 14.29 ? 194 TRP A CH2 1 
ATOM   1606 N  N   . THR A 1 195 ? 10.366  -22.266 7.126   1.00 11.38 ? 195 THR A N   1 
ATOM   1607 C  CA  . THR A 1 195 ? 10.562  -21.227 6.090   1.00 12.24 ? 195 THR A CA  1 
ATOM   1608 C  C   . THR A 1 195 ? 12.020  -20.890 5.835   1.00 11.37 ? 195 THR A C   1 
ATOM   1609 O  O   . THR A 1 195 ? 12.919  -20.851 6.745   1.00 11.75 ? 195 THR A O   1 
ATOM   1610 C  CB  . THR A 1 195 ? 9.718   -19.918 6.377   1.00 12.27 ? 195 THR A CB  1 
ATOM   1611 O  OG1 . THR A 1 195 ? 9.887   -18.962 5.276   1.00 12.86 ? 195 THR A OG1 1 
ATOM   1612 C  CG2 . THR A 1 195 ? 10.178  -19.221 7.645   1.00 14.77 ? 195 THR A CG2 1 
ATOM   1613 N  N   . TYR A 1 196 ? 12.330  -20.617 4.534   1.00 11.28 ? 196 TYR A N   1 
ATOM   1614 C  CA  . TYR A 1 196 ? 13.681  -20.217 4.146   1.00 11.46 ? 196 TYR A CA  1 
ATOM   1615 C  C   . TYR A 1 196 ? 13.633  -19.441 2.816   1.00 10.76 ? 196 TYR A C   1 
ATOM   1616 O  O   . TYR A 1 196 ? 12.660  -19.579 2.086   1.00 10.86 ? 196 TYR A O   1 
ATOM   1617 C  CB  . TYR A 1 196 ? 14.687  -21.438 4.090   1.00 11.56 ? 196 TYR A CB  1 
ATOM   1618 C  CG  . TYR A 1 196 ? 14.385  -22.299 2.833   1.00 11.78 ? 196 TYR A CG  1 
ATOM   1619 C  CD1 . TYR A 1 196 ? 13.364  -23.230 2.806   1.00 11.00 ? 196 TYR A CD1 1 
ATOM   1620 C  CD2 . TYR A 1 196 ? 15.175  -22.138 1.677   1.00 10.19 ? 196 TYR A CD2 1 
ATOM   1621 C  CE1 . TYR A 1 196 ? 13.062  -23.976 1.645   1.00 11.18 ? 196 TYR A CE1 1 
ATOM   1622 C  CE2 . TYR A 1 196 ? 14.906  -22.890 0.558   1.00 10.35 ? 196 TYR A CE2 1 
ATOM   1623 C  CZ  . TYR A 1 196 ? 13.878  -23.821 0.545   1.00 10.76 ? 196 TYR A CZ  1 
ATOM   1624 O  OH  . TYR A 1 196 ? 13.590  -24.530 -0.610  1.00 11.39 ? 196 TYR A OH  1 
ATOM   1625 N  N   . PRO A 1 197 ? 14.688  -18.689 2.528   1.00 11.65 ? 197 PRO A N   1 
ATOM   1626 C  CA  . PRO A 1 197 ? 14.649  -17.964 1.230   1.00 12.47 ? 197 PRO A CA  1 
ATOM   1627 C  C   . PRO A 1 197 ? 15.236  -18.857 0.102   1.00 12.67 ? 197 PRO A C   1 
ATOM   1628 O  O   . PRO A 1 197 ? 16.220  -19.472 0.335   1.00 12.36 ? 197 PRO A O   1 
ATOM   1629 C  CB  . PRO A 1 197 ? 15.621  -16.800 1.477   1.00 11.08 ? 197 PRO A CB  1 
ATOM   1630 C  CG  . PRO A 1 197 ? 16.616  -17.298 2.511   1.00 12.87 ? 197 PRO A CG  1 
ATOM   1631 C  CD  . PRO A 1 197 ? 15.813  -18.231 3.408   1.00 11.81 ? 197 PRO A CD  1 
ATOM   1632 N  N   . GLY A 1 198 ? 14.525  -18.924 -1.013  1.00 10.17 ? 198 GLY A N   1 
ATOM   1633 C  CA  . GLY A 1 198 ? 14.994  -19.820 -2.097  1.00 10.66 ? 198 GLY A CA  1 
ATOM   1634 C  C   . GLY A 1 198 ? 14.546  -19.366 -3.450  1.00 9.76  ? 198 GLY A C   1 
ATOM   1635 O  O   . GLY A 1 198 ? 14.496  -18.110 -3.738  1.00 11.35 ? 198 GLY A O   1 
ATOM   1636 N  N   . SER A 1 199 ? 14.332  -20.359 -4.307  1.00 9.68  ? 199 SER A N   1 
ATOM   1637 C  CA  . SER A 1 199 ? 14.134  -20.075 -5.750  1.00 10.26 ? 199 SER A CA  1 
ATOM   1638 C  C   . SER A 1 199 ? 12.947  -20.866 -6.302  1.00 10.00 ? 199 SER A C   1 
ATOM   1639 O  O   . SER A 1 199 ? 12.418  -21.778 -5.658  1.00 10.88 ? 199 SER A O   1 
ATOM   1640 C  CB  . SER A 1 199 ? 15.406  -20.501 -6.501  1.00 10.53 ? 199 SER A CB  1 
ATOM   1641 O  OG  . SER A 1 199 ? 15.497  -21.965 -6.653  1.00 10.74 ? 199 SER A OG  1 
ATOM   1642 N  N   . LEU A 1 200 ? 12.548  -20.512 -7.499  1.00 9.71  ? 200 LEU A N   1 
ATOM   1643 C  CA  . LEU A 1 200 ? 11.738  -21.434 -8.300  1.00 10.03 ? 200 LEU A CA  1 
ATOM   1644 C  C   . LEU A 1 200 ? 12.560  -22.750 -8.414  1.00 9.70  ? 200 LEU A C   1 
ATOM   1645 O  O   . LEU A 1 200 ? 13.792  -22.771 -8.583  1.00 10.37 ? 200 LEU A O   1 
ATOM   1646 C  CB  . LEU A 1 200 ? 11.520  -20.843 -9.756  1.00 12.69 ? 200 LEU A CB  1 
ATOM   1647 C  CG  . LEU A 1 200 ? 10.776  -19.514 -9.784  1.00 15.72 ? 200 LEU A CG  1 
ATOM   1648 C  CD1 . LEU A 1 200 ? 10.607  -19.239 -11.279 1.00 17.65 ? 200 LEU A CD1 1 
ATOM   1649 C  CD2 . LEU A 1 200 ? 9.402   -19.569 -9.180  1.00 15.05 ? 200 LEU A CD2 1 
ATOM   1650 N  N   . THR A 1 201 ? 11.797  -23.859 -8.468  1.00 10.36 ? 201 THR A N   1 
ATOM   1651 C  CA  . THR A 1 201 ? 12.488  -25.137 -8.625  1.00 10.16 ? 201 THR A CA  1 
ATOM   1652 C  C   . THR A 1 201 ? 12.492  -25.578 -10.083 1.00 11.22 ? 201 THR A C   1 
ATOM   1653 O  O   . THR A 1 201 ? 12.879  -26.733 -10.393 1.00 10.87 ? 201 THR A O   1 
ATOM   1654 C  CB  . THR A 1 201 ? 11.826  -26.286 -7.764  1.00 9.57  ? 201 THR A CB  1 
ATOM   1655 O  OG1 . THR A 1 201 ? 10.525  -26.637 -8.247  1.00 10.62 ? 201 THR A OG1 1 
ATOM   1656 C  CG2 . THR A 1 201 ? 11.723  -25.890 -6.243  1.00 11.83 ? 201 THR A CG2 1 
ATOM   1657 N  N   . VAL A 1 202 ? 12.002  -24.765 -10.997 1.00 10.66 ? 202 VAL A N   1 
ATOM   1658 C  CA  . VAL A 1 202 ? 12.014  -25.020 -12.444 1.00 11.27 ? 202 VAL A CA  1 
ATOM   1659 C  C   . VAL A 1 202 ? 12.717  -23.861 -13.103 1.00 10.44 ? 202 VAL A C   1 
ATOM   1660 O  O   . VAL A 1 202 ? 12.710  -22.726 -12.541 1.00 10.90 ? 202 VAL A O   1 
ATOM   1661 C  CB  . VAL A 1 202 ? 10.585  -25.178 -13.023 1.00 11.29 ? 202 VAL A CB  1 
ATOM   1662 C  CG1 . VAL A 1 202 ? 9.977   -26.477 -12.445 1.00 13.79 ? 202 VAL A CG1 1 
ATOM   1663 C  CG2 . VAL A 1 202 ? 9.571   -23.936 -12.803 1.00 11.90 ? 202 VAL A CG2 1 
ATOM   1664 N  N   . PRO A 1 203 ? 13.328  -24.049 -14.260 1.00 11.85 ? 203 PRO A N   1 
ATOM   1665 C  CA  . PRO A 1 203 ? 13.764  -22.922 -15.042 1.00 11.90 ? 203 PRO A CA  1 
ATOM   1666 C  C   . PRO A 1 203 ? 12.627  -21.900 -15.200 1.00 10.81 ? 203 PRO A C   1 
ATOM   1667 O  O   . PRO A 1 203 ? 11.485  -22.241 -15.464 1.00 12.84 ? 203 PRO A O   1 
ATOM   1668 C  CB  . PRO A 1 203 ? 14.104  -23.624 -16.417 1.00 10.84 ? 203 PRO A CB  1 
ATOM   1669 C  CG  . PRO A 1 203 ? 14.653  -24.940 -15.966 1.00 11.95 ? 203 PRO A CG  1 
ATOM   1670 C  CD  . PRO A 1 203 ? 13.631  -25.329 -14.925 1.00 10.20 ? 203 PRO A CD  1 
ATOM   1671 N  N   . PRO A 1 204 ? 12.928  -20.590 -15.017 1.00 11.79 ? 204 PRO A N   1 
ATOM   1672 C  CA  . PRO A 1 204 ? 14.222  -19.956 -14.950 1.00 12.75 ? 204 PRO A CA  1 
ATOM   1673 C  C   . PRO A 1 204 ? 14.933  -19.870 -13.605 1.00 12.91 ? 204 PRO A C   1 
ATOM   1674 O  O   . PRO A 1 204 ? 15.972  -19.227 -13.489 1.00 13.34 ? 204 PRO A O   1 
ATOM   1675 C  CB  . PRO A 1 204 ? 13.896  -18.520 -15.499 1.00 12.78 ? 204 PRO A CB  1 
ATOM   1676 C  CG  . PRO A 1 204 ? 12.564  -18.262 -14.955 1.00 12.98 ? 204 PRO A CG  1 
ATOM   1677 C  CD  . PRO A 1 204 ? 11.832  -19.591 -15.156 1.00 13.38 ? 204 PRO A CD  1 
ATOM   1678 N  N   . LEU A 1 205 ? 14.390  -20.594 -12.576 1.00 10.88 ? 205 LEU A N   1 
ATOM   1679 C  CA  . LEU A 1 205 ? 15.167  -20.803 -11.336 1.00 11.16 ? 205 LEU A CA  1 
ATOM   1680 C  C   . LEU A 1 205 ? 15.454  -19.544 -10.554 1.00 10.86 ? 205 LEU A C   1 
ATOM   1681 O  O   . LEU A 1 205 ? 16.403  -19.491 -9.817  1.00 11.20 ? 205 LEU A O   1 
ATOM   1682 C  CB  . LEU A 1 205 ? 16.441  -21.606 -11.572 1.00 11.81 ? 205 LEU A CB  1 
ATOM   1683 C  CG  . LEU A 1 205 ? 16.215  -23.058 -12.199 1.00 11.41 ? 205 LEU A CG  1 
ATOM   1684 C  CD1 . LEU A 1 205 ? 17.587  -23.639 -12.674 1.00 12.23 ? 205 LEU A CD1 1 
ATOM   1685 C  CD2 . LEU A 1 205 ? 15.506  -23.997 -11.208 1.00 12.52 ? 205 LEU A CD2 1 
ATOM   1686 N  N   . LEU A 1 206 ? 14.563  -18.559 -10.760 1.00 10.93 ? 206 LEU A N   1 
ATOM   1687 C  CA  . LEU A 1 206 ? 14.763  -17.221 -10.152 1.00 11.80 ? 206 LEU A CA  1 
ATOM   1688 C  C   . LEU A 1 206 ? 14.758  -17.264 -8.635  1.00 11.90 ? 206 LEU A C   1 
ATOM   1689 O  O   . LEU A 1 206 ? 13.922  -17.957 -8.021  1.00 12.34 ? 206 LEU A O   1 
ATOM   1690 C  CB  . LEU A 1 206 ? 13.674  -16.289 -10.618 1.00 12.87 ? 206 LEU A CB  1 
ATOM   1691 C  CG  . LEU A 1 206 ? 13.642  -16.013 -12.184 1.00 13.88 ? 206 LEU A CG  1 
ATOM   1692 C  CD1 . LEU A 1 206 ? 12.386  -15.345 -12.695 1.00 13.71 ? 206 LEU A CD1 1 
ATOM   1693 C  CD2 . LEU A 1 206 ? 14.906  -15.253 -12.629 1.00 16.25 ? 206 LEU A CD2 1 
ATOM   1694 N  N   . GLU A 1 207 ? 15.653  -16.502 -8.075  1.00 11.50 ? 207 GLU A N   1 
ATOM   1695 C  CA  . GLU A 1 207 ? 15.822  -16.510 -6.585  1.00 11.62 ? 207 GLU A CA  1 
ATOM   1696 C  C   . GLU A 1 207 ? 14.880  -15.421 -6.005  1.00 11.09 ? 207 GLU A C   1 
ATOM   1697 O  O   . GLU A 1 207 ? 15.378  -14.372 -5.387  1.00 14.47 ? 207 GLU A O   1 
ATOM   1698 C  CB  . GLU A 1 207 ? 17.294  -16.412 -6.126  1.00 12.65 ? 207 GLU A CB  1 
ATOM   1699 C  CG  . GLU A 1 207 ? 18.129  -17.587 -6.698  1.00 12.00 ? 207 GLU A CG  1 
ATOM   1700 C  CD  . GLU A 1 207 ? 19.579  -17.590 -6.432  1.00 13.02 ? 207 GLU A CD  1 
ATOM   1701 O  OE1 . GLU A 1 207 ? 20.213  -16.468 -6.327  1.00 17.00 ? 207 GLU A OE1 1 
ATOM   1702 O  OE2 . GLU A 1 207 ? 20.115  -18.707 -6.356  1.00 12.69 ? 207 GLU A OE2 1 
ATOM   1703 N  N   . SER A 1 208 ? 13.617  -15.681 -6.074  1.00 12.99 ? 208 SER A N   1 
ATOM   1704 C  CA  . SER A 1 208 ? 12.624  -14.709 -5.601  1.00 11.35 ? 208 SER A CA  1 
ATOM   1705 C  C   . SER A 1 208 ? 11.613  -15.232 -4.663  1.00 12.24 ? 208 SER A C   1 
ATOM   1706 O  O   . SER A 1 208 ? 10.541  -14.630 -4.499  1.00 13.42 ? 208 SER A O   1 
ATOM   1707 C  CB  . SER A 1 208 ? 11.877  -14.220 -6.834  1.00 13.15 ? 208 SER A CB  1 
ATOM   1708 O  OG  . SER A 1 208 ? 11.518  -15.325 -7.675  1.00 14.35 ? 208 SER A OG  1 
ATOM   1709 N  N   . VAL A 1 209 ? 11.829  -16.463 -4.199  1.00 11.41 ? 209 VAL A N   1 
ATOM   1710 C  CA  . VAL A 1 209 ? 10.806  -17.179 -3.442  1.00 12.36 ? 209 VAL A CA  1 
ATOM   1711 C  C   . VAL A 1 209 ? 11.033  -17.272 -1.928  1.00 10.63 ? 209 VAL A C   1 
ATOM   1712 O  O   . VAL A 1 209 ? 12.060  -17.706 -1.440  1.00 12.54 ? 209 VAL A O   1 
ATOM   1713 C  CB  . VAL A 1 209 ? 10.672  -18.617 -3.950  1.00 10.09 ? 209 VAL A CB  1 
ATOM   1714 C  CG1 . VAL A 1 209 ? 9.572   -19.337 -3.160  1.00 10.72 ? 209 VAL A CG1 1 
ATOM   1715 C  CG2 . VAL A 1 209 ? 10.277  -18.649 -5.413  1.00 11.08 ? 209 VAL A CG2 1 
ATOM   1716 N  N   . THR A 1 210 ? 10.038  -16.802 -1.168  1.00 11.69 ? 210 THR A N   1 
ATOM   1717 C  CA  . THR A 1 210 ? 10.000  -17.141 0.242   1.00 12.55 ? 210 THR A CA  1 
ATOM   1718 C  C   . THR A 1 210 ? 9.226   -18.472 0.349   1.00 10.54 ? 210 THR A C   1 
ATOM   1719 O  O   . THR A 1 210 ? 8.060   -18.539 0.041   1.00 12.11 ? 210 THR A O   1 
ATOM   1720 C  CB  . THR A 1 210 ? 9.239   -16.065 1.045   1.00 12.32 ? 210 THR A CB  1 
ATOM   1721 O  OG1 . THR A 1 210 ? 9.923   -14.809 0.935   1.00 13.08 ? 210 THR A OG1 1 
ATOM   1722 C  CG2 . THR A 1 210 ? 9.247   -16.500 2.588   1.00 14.04 ? 210 THR A CG2 1 
ATOM   1723 N  N   . TRP A 1 211 ? 9.976   -19.537 0.720   1.00 10.29 ? 211 TRP A N   1 
ATOM   1724 C  CA  . TRP A 1 211 ? 9.348   -20.839 0.867   1.00 10.73 ? 211 TRP A CA  1 
ATOM   1725 C  C   . TRP A 1 211 ? 8.717   -20.982 2.232   1.00 9.29  ? 211 TRP A C   1 
ATOM   1726 O  O   . TRP A 1 211 ? 9.363   -20.670 3.252   1.00 10.86 ? 211 TRP A O   1 
ATOM   1727 C  CB  . TRP A 1 211 ? 10.456  -21.913 0.687   1.00 10.73 ? 211 TRP A CB  1 
ATOM   1728 C  CG  . TRP A 1 211 ? 10.640  -22.191 -0.786  1.00 9.67  ? 211 TRP A CG  1 
ATOM   1729 C  CD1 . TRP A 1 211 ? 11.625  -21.686 -1.652  1.00 10.87 ? 211 TRP A CD1 1 
ATOM   1730 C  CD2 . TRP A 1 211 ? 9.752   -22.998 -1.596  1.00 9.42  ? 211 TRP A CD2 1 
ATOM   1731 N  NE1 . TRP A 1 211 ? 11.399  -22.122 -2.949  1.00 10.53 ? 211 TRP A NE1 1 
ATOM   1732 C  CE2 . TRP A 1 211 ? 10.280  -22.937 -2.973  1.00 9.73  ? 211 TRP A CE2 1 
ATOM   1733 C  CE3 . TRP A 1 211 ? 8.667   -23.825 -1.320  1.00 10.90 ? 211 TRP A CE3 1 
ATOM   1734 C  CZ2 . TRP A 1 211 ? 9.610   -23.609 -4.029  1.00 9.33  ? 211 TRP A CZ2 1 
ATOM   1735 C  CZ3 . TRP A 1 211 ? 8.022   -24.462 -2.404  1.00 10.31 ? 211 TRP A CZ3 1 
ATOM   1736 C  CH2 . TRP A 1 211 ? 8.513   -24.336 -3.743  1.00 11.59 ? 211 TRP A CH2 1 
ATOM   1737 N  N   . ILE A 1 212 ? 7.539   -21.593 2.236   1.00 10.14 ? 212 ILE A N   1 
ATOM   1738 C  CA  . ILE A 1 212 ? 6.828   -21.901 3.524   1.00 10.34 ? 212 ILE A CA  1 
ATOM   1739 C  C   . ILE A 1 212 ? 6.373   -23.362 3.301   1.00 10.13 ? 212 ILE A C   1 
ATOM   1740 O  O   . ILE A 1 212 ? 5.429   -23.612 2.524   1.00 10.56 ? 212 ILE A O   1 
ATOM   1741 C  CB  . ILE A 1 212 ? 5.638   -20.966 3.656   1.00 10.92 ? 212 ILE A CB  1 
ATOM   1742 C  CG1 . ILE A 1 212 ? 6.094   -19.497 3.725   1.00 12.67 ? 212 ILE A CG1 1 
ATOM   1743 C  CG2 . ILE A 1 212 ? 4.751   -21.338 4.857   1.00 11.65 ? 212 ILE A CG2 1 
ATOM   1744 C  CD1 . ILE A 1 212 ? 4.877   -18.535 3.521   1.00 14.71 ? 212 ILE A CD1 1 
ATOM   1745 N  N   . VAL A 1 213 ? 7.046   -24.285 4.015   1.00 11.13 ? 213 VAL A N   1 
ATOM   1746 C  CA  . VAL A 1 213 ? 6.832   -25.707 3.817   1.00 11.67 ? 213 VAL A CA  1 
ATOM   1747 C  C   . VAL A 1 213 ? 6.092   -26.196 5.061   1.00 11.32 ? 213 VAL A C   1 
ATOM   1748 O  O   . VAL A 1 213 ? 6.624   -26.125 6.187   1.00 13.69 ? 213 VAL A O   1 
ATOM   1749 C  CB  . VAL A 1 213 ? 8.154   -26.424 3.596   1.00 12.38 ? 213 VAL A CB  1 
ATOM   1750 C  CG1 . VAL A 1 213 ? 7.948   -27.951 3.522   1.00 12.11 ? 213 VAL A CG1 1 
ATOM   1751 C  CG2 . VAL A 1 213 ? 8.816   -25.968 2.292   1.00 11.60 ? 213 VAL A CG2 1 
ATOM   1752 N  N   . LEU A 1 214 ? 4.888   -26.711 4.825   1.00 10.91 ? 214 LEU A N   1 
ATOM   1753 C  CA  . LEU A 1 214 ? 4.042   -27.205 6.005   1.00 12.55 ? 214 LEU A CA  1 
ATOM   1754 C  C   . LEU A 1 214 ? 4.605   -28.590 6.489   1.00 11.69 ? 214 LEU A C   1 
ATOM   1755 O  O   . LEU A 1 214 ? 4.995   -29.488 5.694   1.00 12.78 ? 214 LEU A O   1 
ATOM   1756 C  CB  . LEU A 1 214 ? 2.595   -27.366 5.689   1.00 14.02 ? 214 LEU A CB  1 
ATOM   1757 C  CG  . LEU A 1 214 ? 1.830   -26.053 5.347   1.00 19.63 ? 214 LEU A CG  1 
ATOM   1758 C  CD1 . LEU A 1 214 ? 0.331   -26.282 5.221   1.00 22.29 ? 214 LEU A CD1 1 
ATOM   1759 C  CD2 . LEU A 1 214 ? 2.190   -24.910 6.279   1.00 23.69 ? 214 LEU A CD2 1 
ATOM   1760 N  N   . LYS A 1 215 ? 4.679   -28.716 7.817   1.00 12.58 ? 215 LYS A N   1 
ATOM   1761 C  CA  . LYS A 1 215 ? 5.203   -29.952 8.417   1.00 14.01 ? 215 LYS A CA  1 
ATOM   1762 C  C   . LYS A 1 215 ? 4.273   -31.140 8.184   1.00 12.05 ? 215 LYS A C   1 
ATOM   1763 O  O   . LYS A 1 215 ? 4.744   -32.302 7.939   1.00 14.02 ? 215 LYS A O   1 
ATOM   1764 C  CB  . LYS A 1 215 ? 5.509   -29.719 9.888   1.00 15.80 ? 215 LYS A CB  1 
ATOM   1765 C  CG  . LYS A 1 215 ? 5.874   -31.050 10.586  1.00 17.89 ? 215 LYS A CG  1 
ATOM   1766 C  CD  . LYS A 1 215 ? 6.227   -30.822 12.040  1.00 21.54 ? 215 LYS A CD  1 
ATOM   1767 C  CE  . LYS A 1 215 ? 6.293   -32.208 12.735  1.00 24.87 ? 215 LYS A CE  1 
ATOM   1768 N  NZ  . LYS A 1 215 ? 7.010   -31.994 14.046  1.00 32.04 ? 215 LYS A NZ  1 
ATOM   1769 N  N   . GLN A 1 216 ? 2.974   -30.966 8.289   1.00 11.24 ? 216 GLN A N   1 
ATOM   1770 C  CA  . GLN A 1 216 ? 2.111   -32.109 8.233   1.00 13.68 ? 216 GLN A CA  1 
ATOM   1771 C  C   . GLN A 1 216 ? 1.685   -32.439 6.800   1.00 13.88 ? 216 GLN A C   1 
ATOM   1772 O  O   . GLN A 1 216 ? 1.170   -31.578 6.051   1.00 14.45 ? 216 GLN A O   1 
ATOM   1773 C  CB  . GLN A 1 216 ? 0.901   -31.776 9.072   1.00 13.71 ? 216 GLN A CB  1 
ATOM   1774 C  CG  . GLN A 1 216 ? -0.085  -33.012 9.093   1.00 14.45 ? 216 GLN A CG  1 
ATOM   1775 C  CD  . GLN A 1 216 ? -1.334  -32.865 10.020  1.00 17.06 ? 216 GLN A CD  1 
ATOM   1776 O  OE1 . GLN A 1 216 ? -2.057  -33.865 10.221  1.00 21.39 ? 216 GLN A OE1 1 
ATOM   1777 N  NE2 . GLN A 1 216 ? -1.665  -31.635 10.447  1.00 15.75 ? 216 GLN A NE2 1 
ATOM   1778 N  N   . PRO A 1 217 ? 1.809   -33.718 6.407   1.00 13.93 ? 217 PRO A N   1 
ATOM   1779 C  CA  . PRO A 1 217 ? 1.316   -34.101 5.052   1.00 13.91 ? 217 PRO A CA  1 
ATOM   1780 C  C   . PRO A 1 217 ? -0.140  -34.281 4.962   1.00 15.39 ? 217 PRO A C   1 
ATOM   1781 O  O   . PRO A 1 217 ? -0.877  -34.439 6.013   1.00 17.22 ? 217 PRO A O   1 
ATOM   1782 C  CB  . PRO A 1 217 ? 2.016   -35.460 4.780   1.00 14.34 ? 217 PRO A CB  1 
ATOM   1783 C  CG  . PRO A 1 217 ? 2.192   -36.012 6.164   1.00 19.34 ? 217 PRO A CG  1 
ATOM   1784 C  CD  . PRO A 1 217 ? 2.503   -34.837 7.085   1.00 15.85 ? 217 PRO A CD  1 
ATOM   1785 N  N   . ILE A 1 218 ? -0.627  -34.237 3.742   1.00 15.02 ? 218 ILE A N   1 
ATOM   1786 C  CA  . ILE A 1 218 ? -1.960  -34.663 3.429   1.00 14.05 ? 218 ILE A CA  1 
ATOM   1787 C  C   . ILE A 1 218 ? -1.902  -36.019 2.734   1.00 12.21 ? 218 ILE A C   1 
ATOM   1788 O  O   . ILE A 1 218 ? -0.855  -36.525 2.399   1.00 14.69 ? 218 ILE A O   1 
ATOM   1789 C  CB  . ILE A 1 218 ? -2.768  -33.635 2.577   1.00 13.95 ? 218 ILE A CB  1 
ATOM   1790 C  CG1 . ILE A 1 218 ? -2.101  -33.581 1.167   1.00 14.23 ? 218 ILE A CG1 1 
ATOM   1791 C  CG2 . ILE A 1 218 ? -2.898  -32.279 3.267   1.00 15.47 ? 218 ILE A CG2 1 
ATOM   1792 C  CD1 . ILE A 1 218 ? -3.013  -32.832 0.196   1.00 15.51 ? 218 ILE A CD1 1 
ATOM   1793 N  N   A ASN A 1 219 ? -3.045  -36.626 2.462   0.50 14.47 ? 219 ASN A N   1 
ATOM   1794 N  N   B ASN A 1 219 ? -3.059  -36.645 2.540   0.50 15.33 ? 219 ASN A N   1 
ATOM   1795 C  CA  A ASN A 1 219 ? -3.082  -37.925 1.854   0.50 14.37 ? 219 ASN A CA  1 
ATOM   1796 C  CA  B ASN A 1 219 ? -3.192  -37.943 1.912   0.50 16.10 ? 219 ASN A CA  1 
ATOM   1797 C  C   A ASN A 1 219 ? -3.605  -37.970 0.396   0.50 14.49 ? 219 ASN A C   1 
ATOM   1798 C  C   B ASN A 1 219 ? -3.465  -37.881 0.395   0.50 15.45 ? 219 ASN A C   1 
ATOM   1799 O  O   A ASN A 1 219 ? -4.539  -37.217 -0.040  0.50 15.22 ? 219 ASN A O   1 
ATOM   1800 O  O   B ASN A 1 219 ? -4.050  -36.924 -0.080  0.50 15.10 ? 219 ASN A O   1 
ATOM   1801 C  CB  A ASN A 1 219 ? -4.019  -38.792 2.700   0.50 17.26 ? 219 ASN A CB  1 
ATOM   1802 C  CB  B ASN A 1 219 ? -4.397  -38.693 2.579   0.50 19.37 ? 219 ASN A CB  1 
ATOM   1803 C  CG  A ASN A 1 219 ? -3.580  -38.858 4.137   0.50 16.37 ? 219 ASN A CG  1 
ATOM   1804 C  CG  B ASN A 1 219 ? -5.577  -37.781 2.936   0.50 20.50 ? 219 ASN A CG  1 
ATOM   1805 O  OD1 A ASN A 1 219 ? -4.278  -38.346 5.057   0.50 23.49 ? 219 ASN A OD1 1 
ATOM   1806 O  OD1 B ASN A 1 219 ? -5.650  -37.197 4.039   0.50 27.55 ? 219 ASN A OD1 1 
ATOM   1807 N  ND2 A ASN A 1 219 ? -2.459  -39.492 4.364   0.50 15.51 ? 219 ASN A ND2 1 
ATOM   1808 N  ND2 B ASN A 1 219 ? -6.487  -37.641 2.039   0.50 24.59 ? 219 ASN A ND2 1 
ATOM   1809 N  N   . ILE A 1 220 ? -2.975  -38.883 -0.344  1.00 13.96 ? 220 ILE A N   1 
ATOM   1810 C  CA  . ILE A 1 220 ? -3.376  -39.169 -1.700  1.00 14.87 ? 220 ILE A CA  1 
ATOM   1811 C  C   . ILE A 1 220 ? -3.406  -40.669 -1.844  1.00 14.31 ? 220 ILE A C   1 
ATOM   1812 O  O   . ILE A 1 220 ? -2.560  -41.395 -1.284  1.00 15.65 ? 220 ILE A O   1 
ATOM   1813 C  CB  . ILE A 1 220 ? -2.386  -38.508 -2.754  1.00 15.02 ? 220 ILE A CB  1 
ATOM   1814 C  CG1 . ILE A 1 220 ? -2.919  -38.731 -4.208  1.00 15.38 ? 220 ILE A CG1 1 
ATOM   1815 C  CG2 . ILE A 1 220 ? -1.004  -39.143 -2.639  1.00 14.68 ? 220 ILE A CG2 1 
ATOM   1816 C  CD1 . ILE A 1 220 ? -2.183  -37.874 -5.265  1.00 15.65 ? 220 ILE A CD1 1 
ATOM   1817 N  N   . SER A 1 221 ? -4.347  -41.157 -2.677  1.00 16.14 ? 221 SER A N   1 
ATOM   1818 C  CA  . SER A 1 221 ? -4.256  -42.566 -2.959  1.00 16.62 ? 221 SER A CA  1 
ATOM   1819 C  C   . SER A 1 221 ? -3.190  -42.953 -4.023  1.00 16.35 ? 221 SER A C   1 
ATOM   1820 O  O   . SER A 1 221 ? -2.735  -42.125 -4.838  1.00 16.18 ? 221 SER A O   1 
ATOM   1821 C  CB  . SER A 1 221 ? -5.652  -43.171 -3.326  1.00 20.32 ? 221 SER A CB  1 
ATOM   1822 O  OG  . SER A 1 221 ? -5.976  -42.604 -4.610  1.00 21.19 ? 221 SER A OG  1 
ATOM   1823 N  N   A SER A 1 222 ? -2.742  -44.198 -4.006  0.50 16.89 ? 222 SER A N   1 
ATOM   1824 N  N   B SER A 1 222 ? -2.735  -44.190 -4.014  0.50 16.11 ? 222 SER A N   1 
ATOM   1825 C  CA  A SER A 1 222 ? -1.816  -44.646 -5.018  0.50 16.87 ? 222 SER A CA  1 
ATOM   1826 C  CA  B SER A 1 222 ? -1.820  -44.610 -5.037  0.50 15.62 ? 222 SER A CA  1 
ATOM   1827 C  C   A SER A 1 222 ? -2.463  -44.513 -6.413  0.50 17.30 ? 222 SER A C   1 
ATOM   1828 C  C   B SER A 1 222 ? -2.481  -44.462 -6.416  0.50 16.36 ? 222 SER A C   1 
ATOM   1829 O  O   A SER A 1 222 ? -1.774  -44.123 -7.362  0.50 16.40 ? 222 SER A O   1 
ATOM   1830 O  O   B SER A 1 222 ? -1.824  -44.048 -7.363  0.50 15.27 ? 222 SER A O   1 
ATOM   1831 C  CB  A SER A 1 222 ? -1.253  -46.074 -4.749  0.50 18.67 ? 222 SER A CB  1 
ATOM   1832 C  CB  B SER A 1 222 ? -1.341  -46.053 -4.827  0.50 16.53 ? 222 SER A CB  1 
ATOM   1833 O  OG  A SER A 1 222 ? -0.281  -46.467 -5.706  0.50 20.03 ? 222 SER A OG  1 
ATOM   1834 O  OG  B SER A 1 222 ? -2.468  -46.819 -4.453  0.50 15.47 ? 222 SER A OG  1 
ATOM   1835 N  N   . GLN A 1 223 ? -3.768  -44.769 -6.526  1.00 19.63 ? 223 GLN A N   1 
ATOM   1836 C  CA  . GLN A 1 223 ? -4.439  -44.642 -7.797  1.00 21.54 ? 223 GLN A CA  1 
ATOM   1837 C  C   . GLN A 1 223 ? -4.418  -43.173 -8.315  1.00 21.82 ? 223 GLN A C   1 
ATOM   1838 O  O   . GLN A 1 223 ? -4.269  -42.919 -9.528  1.00 18.42 ? 223 GLN A O   1 
ATOM   1839 C  CB  . GLN A 1 223 ? -5.936  -45.068 -7.619  1.00 25.73 ? 223 GLN A CB  1 
ATOM   1840 C  CG  . GLN A 1 223 ? -6.743  -44.884 -8.890  1.00 28.41 ? 223 GLN A CG  1 
ATOM   1841 C  CD  . GLN A 1 223 ? -8.008  -45.728 -8.962  1.00 32.67 ? 223 GLN A CD  1 
ATOM   1842 O  OE1 . GLN A 1 223 ? -8.123  -46.528 -9.895  1.00 39.91 ? 223 GLN A OE1 1 
ATOM   1843 N  NE2 . GLN A 1 223 ? -8.949  -45.565 -7.992  1.00 29.03 ? 223 GLN A NE2 1 
ATOM   1844 N  N   . GLN A 1 224 ? -4.670  -42.242 -7.403  1.00 18.27 ? 224 GLN A N   1 
ATOM   1845 C  CA  . GLN A 1 224 ? -4.742  -40.818 -7.757  1.00 17.64 ? 224 GLN A CA  1 
ATOM   1846 C  C   . GLN A 1 224 ? -3.313  -40.481 -8.200  1.00 17.94 ? 224 GLN A C   1 
ATOM   1847 O  O   . GLN A 1 224 ? -3.122  -39.829 -9.235  1.00 15.39 ? 224 GLN A O   1 
ATOM   1848 C  CB  . GLN A 1 224 ? -5.249  -39.923 -6.623  1.00 20.22 ? 224 GLN A CB  1 
ATOM   1849 C  CG  . GLN A 1 224 ? -6.732  -40.121 -6.281  1.00 18.04 ? 224 GLN A CG  1 
ATOM   1850 C  CD  . GLN A 1 224 ? -7.206  -39.290 -5.076  1.00 20.85 ? 224 GLN A CD  1 
ATOM   1851 O  OE1 . GLN A 1 224 ? -6.444  -39.139 -4.068  1.00 22.77 ? 224 GLN A OE1 1 
ATOM   1852 N  NE2 . GLN A 1 224 ? -8.416  -38.798 -5.131  1.00 21.36 ? 224 GLN A NE2 1 
ATOM   1853 N  N   . LEU A 1 225 ? -2.312  -40.886 -7.392  1.00 16.07 ? 225 LEU A N   1 
ATOM   1854 C  CA  . LEU A 1 225 ? -0.939  -40.446 -7.719  1.00 14.27 ? 225 LEU A CA  1 
ATOM   1855 C  C   . LEU A 1 225 ? -0.520  -40.972 -9.066  1.00 13.02 ? 225 LEU A C   1 
ATOM   1856 O  O   . LEU A 1 225 ? 0.067   -40.234 -9.884  1.00 15.30 ? 225 LEU A O   1 
ATOM   1857 C  CB  . LEU A 1 225 ? 0.061   -40.852 -6.591  1.00 15.97 ? 225 LEU A CB  1 
ATOM   1858 C  CG  . LEU A 1 225 ? 1.498   -40.392 -6.722  1.00 15.75 ? 225 LEU A CG  1 
ATOM   1859 C  CD1 . LEU A 1 225 ? 1.571   -38.849 -6.955  1.00 17.27 ? 225 LEU A CD1 1 
ATOM   1860 C  CD2 . LEU A 1 225 ? 2.349   -40.855 -5.540  1.00 17.33 ? 225 LEU A CD2 1 
ATOM   1861 N  N   . ALA A 1 226 ? -0.859  -42.222 -9.380  1.00 12.56 ? 226 ALA A N   1 
ATOM   1862 C  CA  . ALA A 1 226 ? -0.455  -42.782 -10.650 1.00 14.21 ? 226 ALA A CA  1 
ATOM   1863 C  C   . ALA A 1 226 ? -1.014  -42.066 -11.865 1.00 14.74 ? 226 ALA A C   1 
ATOM   1864 O  O   . ALA A 1 226 ? -0.350  -42.100 -12.899 1.00 16.25 ? 226 ALA A O   1 
ATOM   1865 C  CB  . ALA A 1 226 ? -0.791  -44.321 -10.729 1.00 17.75 ? 226 ALA A CB  1 
ATOM   1866 N  N   . LYS A 1 227 ? -2.187  -41.450 -11.739 1.00 14.43 ? 227 LYS A N   1 
ATOM   1867 C  CA  . LYS A 1 227 ? -2.870  -40.783 -12.877 1.00 16.01 ? 227 LYS A CA  1 
ATOM   1868 C  C   . LYS A 1 227 ? -1.955  -39.619 -13.336 1.00 14.47 ? 227 LYS A C   1 
ATOM   1869 O  O   . LYS A 1 227 ? -1.953  -39.327 -14.545 1.00 14.33 ? 227 LYS A O   1 
ATOM   1870 C  CB  . LYS A 1 227 ? -4.208  -40.169 -12.418 1.00 16.41 ? 227 LYS A CB  1 
ATOM   1871 C  CG  . LYS A 1 227 ? -5.336  -41.162 -12.196 1.00 24.91 ? 227 LYS A CG  1 
ATOM   1872 C  CD  . LYS A 1 227 ? -6.241  -41.326 -13.415 1.00 28.20 ? 227 LYS A CD  1 
ATOM   1873 C  CE  . LYS A 1 227 ? -6.410  -40.074 -14.276 1.00 32.05 ? 227 LYS A CE  1 
ATOM   1874 N  NZ  . LYS A 1 227 ? -7.182  -40.486 -15.518 1.00 34.14 ? 227 LYS A NZ  1 
ATOM   1875 N  N   . PHE A 1 228 ? -1.228  -38.946 -12.453 1.00 12.49 ? 228 PHE A N   1 
ATOM   1876 C  CA  . PHE A 1 228 ? -0.345  -37.827 -12.909 1.00 11.88 ? 228 PHE A CA  1 
ATOM   1877 C  C   . PHE A 1 228 ? 0.746   -38.283 -13.869 1.00 12.82 ? 228 PHE A C   1 
ATOM   1878 O  O   . PHE A 1 228 ? 1.210   -37.553 -14.745 1.00 11.52 ? 228 PHE A O   1 
ATOM   1879 C  CB  . PHE A 1 228 ? 0.262   -37.134 -11.633 1.00 11.89 ? 228 PHE A CB  1 
ATOM   1880 C  CG  . PHE A 1 228 ? -0.840  -36.471 -10.842 1.00 13.10 ? 228 PHE A CG  1 
ATOM   1881 C  CD1 . PHE A 1 228 ? -1.297  -37.009 -9.679  1.00 13.53 ? 228 PHE A CD1 1 
ATOM   1882 C  CD2 . PHE A 1 228 ? -1.401  -35.273 -11.344 1.00 13.44 ? 228 PHE A CD2 1 
ATOM   1883 C  CE1 . PHE A 1 228 ? -2.315  -36.385 -8.946  1.00 13.28 ? 228 PHE A CE1 1 
ATOM   1884 C  CE2 . PHE A 1 228 ? -2.456  -34.658 -10.679 1.00 13.90 ? 228 PHE A CE2 1 
ATOM   1885 C  CZ  . PHE A 1 228 ? -2.950  -35.262 -9.462  1.00 15.03 ? 228 PHE A CZ  1 
ATOM   1886 N  N   . ARG A 1 229 ? 1.246   -39.510 -13.669 1.00 11.48 ? 229 ARG A N   1 
ATOM   1887 C  CA  . ARG A 1 229 ? 2.365   -40.036 -14.504 1.00 11.09 ? 229 ARG A CA  1 
ATOM   1888 C  C   . ARG A 1 229 ? 1.940   -40.332 -15.936 1.00 11.01 ? 229 ARG A C   1 
ATOM   1889 O  O   . ARG A 1 229 ? 2.852   -40.488 -16.816 1.00 13.35 ? 229 ARG A O   1 
ATOM   1890 C  CB  . ARG A 1 229 ? 2.885   -41.312 -13.849 1.00 10.89 ? 229 ARG A CB  1 
ATOM   1891 C  CG  . ARG A 1 229 ? 3.357   -41.052 -12.410 1.00 12.72 ? 229 ARG A CG  1 
ATOM   1892 C  CD  . ARG A 1 229 ? 4.188   -42.327 -11.998 1.00 12.24 ? 229 ARG A CD  1 
ATOM   1893 N  NE  . ARG A 1 229 ? 4.649   -42.189 -10.591 1.00 12.54 ? 229 ARG A NE  1 
ATOM   1894 C  CZ  . ARG A 1 229 ? 3.971   -42.641 -9.528  1.00 12.11 ? 229 ARG A CZ  1 
ATOM   1895 N  NH1 . ARG A 1 229 ? 2.956   -43.571 -9.653  1.00 13.94 ? 229 ARG A NH1 1 
ATOM   1896 N  NH2 . ARG A 1 229 ? 4.381   -42.279 -8.283  1.00 13.22 ? 229 ARG A NH2 1 
ATOM   1897 N  N   A SER A 1 230 ? 0.618   -40.330 -16.150 0.50 12.06 ? 230 SER A N   1 
ATOM   1898 N  N   B SER A 1 230 ? 0.648   -40.341 -16.212 0.50 12.04 ? 230 SER A N   1 
ATOM   1899 C  CA  A SER A 1 230 ? -0.037  -40.513 -17.480 0.50 13.40 ? 230 SER A CA  1 
ATOM   1900 C  CA  B SER A 1 230 ? 0.191   -40.540 -17.605 0.50 13.35 ? 230 SER A CA  1 
ATOM   1901 C  C   A SER A 1 230 ? -0.101  -39.227 -18.306 0.50 13.11 ? 230 SER A C   1 
ATOM   1902 C  C   B SER A 1 230 ? 0.155   -39.234 -18.394 0.50 12.86 ? 230 SER A C   1 
ATOM   1903 O  O   A SER A 1 230 ? -0.502  -39.263 -19.461 0.50 14.34 ? 230 SER A O   1 
ATOM   1904 O  O   B SER A 1 230 ? 0.009   -39.258 -19.619 0.50 14.48 ? 230 SER A O   1 
ATOM   1905 C  CB  A SER A 1 230 ? -1.411  -41.236 -17.413 0.50 15.22 ? 230 SER A CB  1 
ATOM   1906 C  CB  B SER A 1 230 ? -1.129  -41.285 -17.696 0.50 14.95 ? 230 SER A CB  1 
ATOM   1907 O  OG  A SER A 1 230 ? -2.480  -40.499 -16.867 0.50 20.14 ? 230 SER A OG  1 
ATOM   1908 O  OG  B SER A 1 230 ? -0.894  -42.656 -17.355 0.50 16.47 ? 230 SER A OG  1 
ATOM   1909 N  N   . LEU A 1 231 ? 0.260   -38.084 -17.708 1.00 12.54 ? 231 LEU A N   1 
ATOM   1910 C  CA  . LEU A 1 231 ? 0.409   -36.835 -18.477 1.00 12.67 ? 231 LEU A CA  1 
ATOM   1911 C  C   . LEU A 1 231 ? 1.623   -36.939 -19.361 1.00 13.42 ? 231 LEU A C   1 
ATOM   1912 O  O   . LEU A 1 231 ? 2.626   -37.583 -19.021 1.00 12.74 ? 231 LEU A O   1 
ATOM   1913 C  CB  . LEU A 1 231 ? 0.599   -35.649 -17.549 1.00 12.81 ? 231 LEU A CB  1 
ATOM   1914 C  CG  . LEU A 1 231 ? -0.653  -35.325 -16.741 1.00 13.65 ? 231 LEU A CG  1 
ATOM   1915 C  CD1 . LEU A 1 231 ? -0.291  -34.319 -15.624 1.00 14.32 ? 231 LEU A CD1 1 
ATOM   1916 C  CD2 . LEU A 1 231 ? -1.820  -34.732 -17.611 1.00 13.64 ? 231 LEU A CD2 1 
ATOM   1917 N  N   . LEU A 1 232 ? 1.561   -36.326 -20.554 1.00 13.44 ? 232 LEU A N   1 
ATOM   1918 C  CA  . LEU A 1 232 ? 2.699   -36.300 -21.448 1.00 13.77 ? 232 LEU A CA  1 
ATOM   1919 C  C   . LEU A 1 232 ? 3.475   -35.009 -21.297 1.00 14.77 ? 232 LEU A C   1 
ATOM   1920 O  O   . LEU A 1 232 ? 2.848   -33.953 -20.956 1.00 15.10 ? 232 LEU A O   1 
ATOM   1921 C  CB  . LEU A 1 232 ? 2.206   -36.370 -22.905 1.00 13.97 ? 232 LEU A CB  1 
ATOM   1922 C  CG  . LEU A 1 232 ? 1.376   -37.618 -23.214 1.00 16.77 ? 232 LEU A CG  1 
ATOM   1923 C  CD1 . LEU A 1 232 ? 1.066   -37.564 -24.714 1.00 19.60 ? 232 LEU A CD1 1 
ATOM   1924 C  CD2 . LEU A 1 232 ? 2.145   -38.879 -22.859 1.00 18.01 ? 232 LEU A CD2 1 
ATOM   1925 N  N   . CYS A 1 233 ? 4.770   -35.072 -21.549 1.00 14.53 ? 233 CYS A N   1 
ATOM   1926 C  CA  . CYS A 1 233 ? 5.628   -33.856 -21.604 1.00 14.99 ? 233 CYS A CA  1 
ATOM   1927 C  C   . CYS A 1 233 ? 5.775   -33.373 -23.026 1.00 16.61 ? 233 CYS A C   1 
ATOM   1928 O  O   . CYS A 1 233 ? 6.517   -32.421 -23.248 1.00 19.46 ? 233 CYS A O   1 
ATOM   1929 C  CB  . CYS A 1 233 ? 6.999   -34.053 -20.913 1.00 15.34 ? 233 CYS A CB  1 
ATOM   1930 S  SG  . CYS A 1 233 ? 7.990   -35.400 -21.695 1.00 19.46 ? 233 CYS A SG  1 
ATOM   1931 N  N   . THR A 1 234 ? 5.068   -34.052 -23.932 1.00 16.28 ? 234 THR A N   1 
ATOM   1932 C  CA  . THR A 1 234 ? 5.070   -33.799 -25.391 1.00 16.36 ? 234 THR A CA  1 
ATOM   1933 C  C   . THR A 1 234 ? 3.672   -33.309 -25.852 1.00 18.92 ? 234 THR A C   1 
ATOM   1934 O  O   . THR A 1 234 ? 2.610   -33.580 -25.258 1.00 17.58 ? 234 THR A O   1 
ATOM   1935 C  CB  . THR A 1 234 ? 5.437   -35.151 -26.095 1.00 16.67 ? 234 THR A CB  1 
ATOM   1936 O  OG1 . THR A 1 234 ? 4.567   -36.219 -25.693 1.00 15.76 ? 234 THR A OG1 1 
ATOM   1937 C  CG2 . THR A 1 234 ? 6.875   -35.489 -25.815 1.00 16.35 ? 234 THR A CG2 1 
ATOM   1938 N  N   . ALA A 1 235 ? 3.681   -32.627 -27.009 1.00 19.42 ? 235 ALA A N   1 
ATOM   1939 C  CA  . ALA A 1 235 ? 2.497   -31.993 -27.605 1.00 21.86 ? 235 ALA A CA  1 
ATOM   1940 C  C   . ALA A 1 235 ? 1.771   -32.971 -28.530 1.00 22.42 ? 235 ALA A C   1 
ATOM   1941 O  O   . ALA A 1 235 ? 2.306   -34.037 -28.873 1.00 24.76 ? 235 ALA A O   1 
ATOM   1942 C  CB  . ALA A 1 235 ? 2.996   -30.790 -28.411 1.00 22.49 ? 235 ALA A CB  1 
ATOM   1943 N  N   . GLU A 1 236 ? 0.535   -32.631 -28.881 1.00 24.59 ? 236 GLU A N   1 
ATOM   1944 C  CA  . GLU A 1 236 ? -0.312  -33.432 -29.791 1.00 31.63 ? 236 GLU A CA  1 
ATOM   1945 C  C   . GLU A 1 236 ? 0.462   -33.729 -31.096 1.00 32.16 ? 236 GLU A C   1 
ATOM   1946 O  O   . GLU A 1 236 ? 1.173   -32.870 -31.612 1.00 29.33 ? 236 GLU A O   1 
ATOM   1947 C  CB  . GLU A 1 236 ? -1.615  -32.650 -30.070 1.00 37.68 ? 236 GLU A CB  1 
ATOM   1948 C  CG  . GLU A 1 236 ? -2.832  -33.444 -30.541 1.00 48.71 ? 236 GLU A CG  1 
ATOM   1949 C  CD  . GLU A 1 236 ? -4.103  -32.599 -30.436 1.00 55.01 ? 236 GLU A CD  1 
ATOM   1950 O  OE1 . GLU A 1 236 ? -4.115  -31.455 -30.965 1.00 60.56 ? 236 GLU A OE1 1 
ATOM   1951 O  OE2 . GLU A 1 236 ? -5.084  -33.055 -29.804 1.00 54.18 ? 236 GLU A OE2 1 
ATOM   1952 N  N   . GLY A 1 237 ? 0.399   -34.998 -31.527 1.00 35.03 ? 237 GLY A N   1 
ATOM   1953 C  CA  . GLY A 1 237 ? 1.123   -35.467 -32.736 1.00 38.82 ? 237 GLY A CA  1 
ATOM   1954 C  C   . GLY A 1 237 ? 2.655   -35.490 -32.710 1.00 41.53 ? 237 GLY A C   1 
ATOM   1955 O  O   . GLY A 1 237 ? 3.269   -35.665 -33.746 1.00 50.08 ? 237 GLY A O   1 
ATOM   1956 N  N   . GLU A 1 238 ? 3.282   -35.312 -31.545 1.00 37.65 ? 238 GLU A N   1 
ATOM   1957 C  CA  . GLU A 1 238 ? 4.707   -35.637 -31.348 1.00 33.42 ? 238 GLU A CA  1 
ATOM   1958 C  C   . GLU A 1 238 ? 4.786   -37.039 -30.759 1.00 31.87 ? 238 GLU A C   1 
ATOM   1959 O  O   . GLU A 1 238 ? 3.785   -37.562 -30.207 1.00 26.91 ? 238 GLU A O   1 
ATOM   1960 C  CB  . GLU A 1 238 ? 5.403   -34.653 -30.408 1.00 35.48 ? 238 GLU A CB  1 
ATOM   1961 C  CG  . GLU A 1 238 ? 5.595   -33.240 -30.895 1.00 40.11 ? 238 GLU A CG  1 
ATOM   1962 C  CD  . GLU A 1 238 ? 6.022   -32.233 -29.795 1.00 51.44 ? 238 GLU A CD  1 
ATOM   1963 O  OE1 . GLU A 1 238 ? 6.103   -32.534 -28.539 1.00 42.78 ? 238 GLU A OE1 1 
ATOM   1964 O  OE2 . GLU A 1 238 ? 6.284   -31.069 -30.202 1.00 55.85 ? 238 GLU A OE2 1 
ATOM   1965 N  N   . ALA A 1 239 ? 5.953   -37.676 -30.924 1.00 29.49 ? 239 ALA A N   1 
ATOM   1966 C  CA  . ALA A 1 239 ? 6.236   -38.957 -30.292 1.00 29.75 ? 239 ALA A CA  1 
ATOM   1967 C  C   . ALA A 1 239 ? 6.005   -38.766 -28.746 1.00 22.07 ? 239 ALA A C   1 
ATOM   1968 O  O   . ALA A 1 239 ? 6.676   -37.893 -28.173 1.00 24.40 ? 239 ALA A O   1 
ATOM   1969 C  CB  . ALA A 1 239 ? 7.682   -39.324 -30.560 1.00 28.26 ? 239 ALA A CB  1 
ATOM   1970 N  N   . ALA A 1 240 ? 5.136   -39.601 -28.182 1.00 25.05 ? 240 ALA A N   1 
ATOM   1971 C  CA  . ALA A 1 240 ? 4.705   -39.530 -26.782 1.00 22.22 ? 240 ALA A CA  1 
ATOM   1972 C  C   . ALA A 1 240 ? 5.917   -39.761 -25.872 1.00 22.95 ? 240 ALA A C   1 
ATOM   1973 O  O   . ALA A 1 240 ? 6.659   -40.741 -26.016 1.00 23.06 ? 240 ALA A O   1 
ATOM   1974 C  CB  . ALA A 1 240 ? 3.589   -40.539 -26.464 1.00 25.44 ? 240 ALA A CB  1 
ATOM   1975 N  N   . ALA A 1 241 ? 6.065   -38.889 -24.890 1.00 18.91 ? 241 ALA A N   1 
ATOM   1976 C  CA  . ALA A 1 241 ? 6.966   -39.159 -23.737 1.00 15.13 ? 241 ALA A CA  1 
ATOM   1977 C  C   . ALA A 1 241 ? 6.160   -38.775 -22.481 1.00 15.59 ? 241 ALA A C   1 
ATOM   1978 O  O   . ALA A 1 241 ? 5.445   -37.736 -22.516 1.00 15.26 ? 241 ALA A O   1 
ATOM   1979 C  CB  . ALA A 1 241 ? 8.246   -38.359 -23.810 1.00 15.85 ? 241 ALA A CB  1 
ATOM   1980 N  N   . PHE A 1 242 ? 6.296   -39.622 -21.424 1.00 13.61 ? 242 PHE A N   1 
ATOM   1981 C  CA  . PHE A 1 242 ? 5.433   -39.451 -20.248 1.00 13.33 ? 242 PHE A CA  1 
ATOM   1982 C  C   . PHE A 1 242 ? 6.180   -38.705 -19.109 1.00 13.06 ? 242 PHE A C   1 
ATOM   1983 O  O   . PHE A 1 242 ? 7.340   -38.828 -18.898 1.00 14.35 ? 242 PHE A O   1 
ATOM   1984 C  CB  . PHE A 1 242 ? 5.007   -40.848 -19.730 1.00 13.26 ? 242 PHE A CB  1 
ATOM   1985 C  CG  . PHE A 1 242 ? 4.100   -41.549 -20.693 1.00 14.24 ? 242 PHE A CG  1 
ATOM   1986 C  CD1 . PHE A 1 242 ? 4.651   -42.415 -21.624 1.00 16.63 ? 242 PHE A CD1 1 
ATOM   1987 C  CD2 . PHE A 1 242 ? 2.733   -41.396 -20.596 1.00 15.75 ? 242 PHE A CD2 1 
ATOM   1988 C  CE1 . PHE A 1 242 ? 3.845   -43.059 -22.529 1.00 15.65 ? 242 PHE A CE1 1 
ATOM   1989 C  CE2 . PHE A 1 242 ? 1.907   -42.086 -21.500 1.00 16.58 ? 242 PHE A CE2 1 
ATOM   1990 C  CZ  . PHE A 1 242 ? 2.474   -42.913 -22.407 1.00 15.48 ? 242 PHE A CZ  1 
ATOM   1991 N  N   . LEU A 1 243 ? 5.336   -37.932 -18.407 1.00 12.09 ? 243 LEU A N   1 
ATOM   1992 C  CA  . LEU A 1 243 ? 5.870   -37.159 -17.258 1.00 12.32 ? 243 LEU A CA  1 
ATOM   1993 C  C   . LEU A 1 243 ? 5.831   -38.040 -16.020 1.00 11.61 ? 243 LEU A C   1 
ATOM   1994 O  O   . LEU A 1 243 ? 5.021   -37.827 -15.081 1.00 11.44 ? 243 LEU A O   1 
ATOM   1995 C  CB  . LEU A 1 243 ? 4.963   -35.882 -17.166 1.00 12.44 ? 243 LEU A CB  1 
ATOM   1996 C  CG  . LEU A 1 243 ? 5.501   -34.859 -16.147 1.00 12.71 ? 243 LEU A CG  1 
ATOM   1997 C  CD1 . LEU A 1 243 ? 6.887   -34.303 -16.521 1.00 14.10 ? 243 LEU A CD1 1 
ATOM   1998 C  CD2 . LEU A 1 243 ? 4.466   -33.698 -16.042 1.00 12.33 ? 243 LEU A CD2 1 
ATOM   1999 N  N   . VAL A 1 244 ? 6.696   -39.027 -15.970 1.00 11.96 ? 244 VAL A N   1 
ATOM   2000 C  CA  . VAL A 1 244 ? 6.633   -39.994 -14.833 1.00 12.51 ? 244 VAL A CA  1 
ATOM   2001 C  C   . VAL A 1 244 ? 7.331   -39.472 -13.544 1.00 11.85 ? 244 VAL A C   1 
ATOM   2002 O  O   . VAL A 1 244 ? 7.039   -39.970 -12.439 1.00 12.22 ? 244 VAL A O   1 
ATOM   2003 C  CB  . VAL A 1 244 ? 7.340   -41.361 -15.240 1.00 13.96 ? 244 VAL A CB  1 
ATOM   2004 C  CG1 . VAL A 1 244 ? 6.566   -41.947 -16.424 1.00 13.81 ? 244 VAL A CG1 1 
ATOM   2005 C  CG2 . VAL A 1 244 ? 8.807   -41.248 -15.496 1.00 15.64 ? 244 VAL A CG2 1 
ATOM   2006 N  N   . SER A 1 245 ? 8.130   -38.394 -13.674 1.00 11.07 ? 245 SER A N   1 
ATOM   2007 C  CA  . SER A 1 245 ? 8.773   -37.793 -12.520 1.00 12.48 ? 245 SER A CA  1 
ATOM   2008 C  C   . SER A 1 245 ? 9.028   -36.347 -12.870 1.00 12.77 ? 245 SER A C   1 
ATOM   2009 O  O   . SER A 1 245 ? 9.527   -36.088 -14.013 1.00 12.86 ? 245 SER A O   1 
ATOM   2010 C  CB  . SER A 1 245 ? 10.097  -38.494 -12.309 1.00 13.98 ? 245 SER A CB  1 
ATOM   2011 O  OG  . SER A 1 245 ? 10.714  -38.055 -11.109 1.00 14.77 ? 245 SER A OG  1 
ATOM   2012 N  N   . ASN A 1 246 ? 8.863   -35.450 -11.865 1.00 10.08 ? 246 ASN A N   1 
ATOM   2013 C  CA  . ASN A 1 246 ? 9.099   -33.999 -12.174 1.00 10.34 ? 246 ASN A CA  1 
ATOM   2014 C  C   . ASN A 1 246 ? 9.565   -33.299 -10.908 1.00 10.77 ? 246 ASN A C   1 
ATOM   2015 O  O   . ASN A 1 246 ? 9.158   -32.169 -10.650 1.00 11.99 ? 246 ASN A O   1 
ATOM   2016 C  CB  . ASN A 1 246 ? 7.842   -33.376 -12.785 1.00 9.40  ? 246 ASN A CB  1 
ATOM   2017 C  CG  . ASN A 1 246 ? 6.706   -33.368 -11.836 1.00 10.55 ? 246 ASN A CG  1 
ATOM   2018 O  OD1 . ASN A 1 246 ? 6.832   -34.040 -10.823 1.00 11.84 ? 246 ASN A OD1 1 
ATOM   2019 N  ND2 . ASN A 1 246 ? 5.639   -32.642 -12.115 1.00 11.11 ? 246 ASN A ND2 1 
ATOM   2020 N  N   . HIS A 1 247 ? 10.407  -33.941 -10.145 1.00 10.08 ? 247 HIS A N   1 
ATOM   2021 C  CA  . HIS A 1 247 ? 11.035  -33.297 -8.947  1.00 10.19 ? 247 HIS A CA  1 
ATOM   2022 C  C   . HIS A 1 247 ? 12.490  -33.018 -9.070  1.00 12.37 ? 247 HIS A C   1 
ATOM   2023 O  O   . HIS A 1 247 ? 13.294  -33.847 -9.519  1.00 14.08 ? 247 HIS A O   1 
ATOM   2024 C  CB  . HIS A 1 247 ? 10.712  -34.075 -7.657  1.00 10.54 ? 247 HIS A CB  1 
ATOM   2025 C  CG  . HIS A 1 247 ? 11.241  -35.464 -7.636  1.00 12.31 ? 247 HIS A CG  1 
ATOM   2026 N  ND1 . HIS A 1 247 ? 12.346  -35.835 -6.907  1.00 15.78 ? 247 HIS A ND1 1 
ATOM   2027 C  CD2 . HIS A 1 247 ? 10.781  -36.567 -8.263  1.00 11.16 ? 247 HIS A CD2 1 
ATOM   2028 C  CE1 . HIS A 1 247 ? 12.567  -37.180 -7.097  1.00 12.93 ? 247 HIS A CE1 1 
ATOM   2029 N  NE2 . HIS A 1 247 ? 11.675  -37.625 -7.928  1.00 17.14 ? 247 HIS A NE2 1 
ATOM   2030 N  N   . ARG A 1 248 ? 12.867  -31.818 -8.660  1.00 10.59 ? 248 ARG A N   1 
ATOM   2031 C  CA  . ARG A 1 248 ? 14.251  -31.461 -8.687  1.00 10.36 ? 248 ARG A CA  1 
ATOM   2032 C  C   . ARG A 1 248 ? 14.958  -31.975 -7.411  1.00 11.33 ? 248 ARG A C   1 
ATOM   2033 O  O   . ARG A 1 248 ? 14.400  -31.885 -6.352  1.00 11.97 ? 248 ARG A O   1 
ATOM   2034 C  CB  . ARG A 1 248 ? 14.399  -29.901 -8.758  1.00 10.89 ? 248 ARG A CB  1 
ATOM   2035 C  CG  . ARG A 1 248 ? 15.852  -29.410 -9.006  1.00 11.09 ? 248 ARG A CG  1 
ATOM   2036 C  CD  . ARG A 1 248 ? 15.954  -27.885 -8.798  1.00 11.84 ? 248 ARG A CD  1 
ATOM   2037 N  NE  . ARG A 1 248 ? 17.232  -27.435 -9.348  1.00 11.84 ? 248 ARG A NE  1 
ATOM   2038 C  CZ  . ARG A 1 248 ? 17.793  -26.253 -9.117  1.00 10.75 ? 248 ARG A CZ  1 
ATOM   2039 N  NH1 . ARG A 1 248 ? 17.186  -25.364 -8.345  1.00 10.62 ? 248 ARG A NH1 1 
ATOM   2040 N  NH2 . ARG A 1 248 ? 18.962  -25.961 -9.669  1.00 10.44 ? 248 ARG A NH2 1 
ATOM   2041 N  N   . PRO A 1 249 ? 16.165  -32.480 -7.512  1.00 11.49 ? 249 PRO A N   1 
ATOM   2042 C  CA  . PRO A 1 249 ? 16.895  -32.853 -6.271  1.00 13.51 ? 249 PRO A CA  1 
ATOM   2043 C  C   . PRO A 1 249 ? 17.145  -31.686 -5.299  1.00 13.33 ? 249 PRO A C   1 
ATOM   2044 O  O   . PRO A 1 249 ? 17.149  -30.525 -5.775  1.00 12.39 ? 249 PRO A O   1 
ATOM   2045 C  CB  . PRO A 1 249 ? 18.186  -33.416 -6.748  1.00 17.78 ? 249 PRO A CB  1 
ATOM   2046 C  CG  . PRO A 1 249 ? 18.008  -33.697 -8.235  1.00 15.83 ? 249 PRO A CG  1 
ATOM   2047 C  CD  . PRO A 1 249 ? 16.981  -32.679 -8.742  1.00 14.01 ? 249 PRO A CD  1 
ATOM   2048 N  N   . PRO A 1 250 ? 17.390  -31.965 -3.999  1.00 14.55 ? 250 PRO A N   1 
ATOM   2049 C  CA  . PRO A 1 250 ? 17.730  -30.924 -3.069  1.00 13.69 ? 250 PRO A CA  1 
ATOM   2050 C  C   . PRO A 1 250 ? 19.043  -30.269 -3.464  1.00 12.97 ? 250 PRO A C   1 
ATOM   2051 O  O   . PRO A 1 250 ? 19.983  -30.909 -4.040  1.00 12.14 ? 250 PRO A O   1 
ATOM   2052 C  CB  . PRO A 1 250 ? 17.918  -31.685 -1.739  1.00 14.41 ? 250 PRO A CB  1 
ATOM   2053 C  CG  . PRO A 1 250 ? 16.770  -32.606 -1.809  1.00 19.78 ? 250 PRO A CG  1 
ATOM   2054 C  CD  . PRO A 1 250 ? 16.893  -33.177 -3.266  1.00 17.09 ? 250 PRO A CD  1 
ATOM   2055 N  N   . GLN A 1 251 ? 19.128  -28.960 -3.221  1.00 11.21 ? 251 GLN A N   1 
ATOM   2056 C  CA  . GLN A 1 251 ? 20.277  -28.137 -3.661  1.00 11.34 ? 251 GLN A CA  1 
ATOM   2057 C  C   . GLN A 1 251 ? 21.070  -27.646 -2.426  1.00 12.83 ? 251 GLN A C   1 
ATOM   2058 O  O   . GLN A 1 251 ? 20.535  -27.670 -1.319  1.00 12.49 ? 251 GLN A O   1 
ATOM   2059 C  CB  . GLN A 1 251 ? 19.702  -26.961 -4.457  1.00 13.10 ? 251 GLN A CB  1 
ATOM   2060 C  CG  . GLN A 1 251 ? 18.925  -27.372 -5.708  1.00 12.97 ? 251 GLN A CG  1 
ATOM   2061 C  CD  . GLN A 1 251 ? 19.790  -28.113 -6.691  1.00 13.35 ? 251 GLN A CD  1 
ATOM   2062 O  OE1 . GLN A 1 251 ? 20.878  -27.687 -7.080  1.00 16.21 ? 251 GLN A OE1 1 
ATOM   2063 N  NE2 . GLN A 1 251 ? 19.313  -29.316 -7.107  1.00 13.99 ? 251 GLN A NE2 1 
ATOM   2064 N  N   . PRO A 1 252 ? 22.294  -27.194 -2.640  1.00 12.20 ? 252 PRO A N   1 
ATOM   2065 C  CA  . PRO A 1 252 ? 23.145  -26.851 -1.484  1.00 13.92 ? 252 PRO A CA  1 
ATOM   2066 C  C   . PRO A 1 252 ? 22.494  -25.754 -0.646  1.00 12.92 ? 252 PRO A C   1 
ATOM   2067 O  O   . PRO A 1 252 ? 22.051  -24.752 -1.200  1.00 12.56 ? 252 PRO A O   1 
ATOM   2068 C  CB  . PRO A 1 252 ? 24.396  -26.340 -2.188  1.00 14.13 ? 252 PRO A CB  1 
ATOM   2069 C  CG  . PRO A 1 252 ? 24.510  -27.198 -3.414  1.00 16.48 ? 252 PRO A CG  1 
ATOM   2070 C  CD  . PRO A 1 252 ? 23.078  -27.158 -3.920  1.00 13.39 ? 252 PRO A CD  1 
ATOM   2071 N  N   . LEU A 1 253 ? 22.551  -25.859 0.680   1.00 13.18 ? 253 LEU A N   1 
ATOM   2072 C  CA  . LEU A 1 253 ? 21.932  -24.892 1.558   1.00 13.46 ? 253 LEU A CA  1 
ATOM   2073 C  C   . LEU A 1 253 ? 22.666  -23.561 1.548   1.00 14.48 ? 253 LEU A C   1 
ATOM   2074 O  O   . LEU A 1 253 ? 22.064  -22.470 1.739   1.00 13.93 ? 253 LEU A O   1 
ATOM   2075 C  CB  . LEU A 1 253 ? 21.913  -25.435 3.014   1.00 15.08 ? 253 LEU A CB  1 
ATOM   2076 C  CG  . LEU A 1 253 ? 21.023  -24.658 3.974   1.00 21.48 ? 253 LEU A CG  1 
ATOM   2077 C  CD1 . LEU A 1 253 ? 19.571  -24.533 3.445   1.00 21.73 ? 253 LEU A CD1 1 
ATOM   2078 C  CD2 . LEU A 1 253 ? 21.068  -25.273 5.374   1.00 22.33 ? 253 LEU A CD2 1 
ATOM   2079 N  N   . LYS A 1 254 ? 23.989  -23.645 1.370   1.00 16.12 ? 254 LYS A N   1 
ATOM   2080 C  CA  . LYS A 1 254 ? 24.902  -22.429 1.297   1.00 15.91 ? 254 LYS A CA  1 
ATOM   2081 C  C   . LYS A 1 254 ? 24.705  -21.504 2.517   1.00 17.28 ? 254 LYS A C   1 
ATOM   2082 O  O   . LYS A 1 254 ? 24.616  -20.253 2.393   1.00 18.33 ? 254 LYS A O   1 
ATOM   2083 C  CB  . LYS A 1 254 ? 24.757  -21.734 -0.035  1.00 18.72 ? 254 LYS A CB  1 
ATOM   2084 C  CG  . LYS A 1 254 ? 25.499  -22.604 -1.103  1.00 20.25 ? 254 LYS A CG  1 
ATOM   2085 C  CD  . LYS A 1 254 ? 25.338  -21.974 -2.427  1.00 28.19 ? 254 LYS A CD  1 
ATOM   2086 C  CE  . LYS A 1 254 ? 26.024  -22.809 -3.512  1.00 27.61 ? 254 LYS A CE  1 
ATOM   2087 N  NZ  . LYS A 1 254 ? 27.310  -23.455 -3.162  1.00 33.29 ? 254 LYS A NZ  1 
ATOM   2088 N  N   . GLY A 1 255 ? 24.524  -22.131 3.667   1.00 18.17 ? 255 GLY A N   1 
ATOM   2089 C  CA  . GLY A 1 255 ? 24.506  -21.333 4.913   1.00 20.58 ? 255 GLY A CA  1 
ATOM   2090 C  C   . GLY A 1 255 ? 23.145  -20.738 5.251   1.00 18.43 ? 255 GLY A C   1 
ATOM   2091 O  O   . GLY A 1 255 ? 23.018  -20.054 6.327   1.00 18.68 ? 255 GLY A O   1 
ATOM   2092 N  N   . ARG A 1 256 ? 22.152  -20.864 4.379   1.00 15.75 ? 256 ARG A N   1 
ATOM   2093 C  CA  . ARG A 1 256 ? 20.834  -20.297 4.637   1.00 15.93 ? 256 ARG A CA  1 
ATOM   2094 C  C   . ARG A 1 256 ? 20.195  -20.823 5.946   1.00 18.56 ? 256 ARG A C   1 
ATOM   2095 O  O   . ARG A 1 256 ? 20.380  -21.970 6.324   1.00 17.01 ? 256 ARG A O   1 
ATOM   2096 C  CB  . ARG A 1 256 ? 19.868  -20.586 3.492   1.00 14.95 ? 256 ARG A CB  1 
ATOM   2097 C  CG  . ARG A 1 256 ? 20.199  -19.706 2.302   1.00 13.96 ? 256 ARG A CG  1 
ATOM   2098 C  CD  . ARG A 1 256 ? 19.285  -20.085 1.142   1.00 13.44 ? 256 ARG A CD  1 
ATOM   2099 N  NE  . ARG A 1 256 ? 19.743  -21.369 0.616   1.00 13.15 ? 256 ARG A NE  1 
ATOM   2100 C  CZ  . ARG A 1 256 ? 19.115  -22.032 -0.356  1.00 10.93 ? 256 ARG A CZ  1 
ATOM   2101 N  NH1 . ARG A 1 256 ? 17.958  -21.600 -0.797  1.00 11.15 ? 256 ARG A NH1 1 
ATOM   2102 N  NH2 . ARG A 1 256 ? 19.663  -23.183 -0.853  1.00 9.66  ? 256 ARG A NH2 1 
ATOM   2103 N  N   . LYS A 1 257 ? 19.459  -19.929 6.642   1.00 20.50 ? 257 LYS A N   1 
ATOM   2104 C  CA  . LYS A 1 257 ? 18.711  -20.305 7.852   1.00 20.89 ? 257 LYS A CA  1 
ATOM   2105 C  C   . LYS A 1 257 ? 17.297  -20.797 7.594   1.00 21.66 ? 257 LYS A C   1 
ATOM   2106 O  O   . LYS A 1 257 ? 16.497  -20.049 7.004   1.00 20.91 ? 257 LYS A O   1 
ATOM   2107 C  CB  . LYS A 1 257 ? 18.711  -19.131 8.891   1.00 22.59 ? 257 LYS A CB  1 
ATOM   2108 C  CG  . LYS A 1 257 ? 18.079  -19.522 10.278  1.00 25.17 ? 257 LYS A CG  1 
ATOM   2109 C  CD  . LYS A 1 257 ? 18.338  -18.475 11.404  1.00 28.38 ? 257 LYS A CD  1 
ATOM   2110 C  CE  . LYS A 1 257 ? 18.226  -17.078 10.842  1.00 32.21 ? 257 LYS A CE  1 
ATOM   2111 N  NZ  . LYS A 1 257 ? 17.909  -16.073 11.908  1.00 41.48 ? 257 LYS A NZ  1 
ATOM   2112 N  N   . VAL A 1 258 ? 17.000  -22.034 7.965   1.00 17.59 ? 258 VAL A N   1 
ATOM   2113 C  CA  . VAL A 1 258 ? 15.656  -22.562 7.920   1.00 17.81 ? 258 VAL A CA  1 
ATOM   2114 C  C   . VAL A 1 258 ? 15.023  -22.332 9.310   1.00 17.41 ? 258 VAL A C   1 
ATOM   2115 O  O   . VAL A 1 258 ? 15.634  -22.743 10.361  1.00 18.31 ? 258 VAL A O   1 
ATOM   2116 C  CB  . VAL A 1 258 ? 15.556  -24.063 7.537   1.00 17.36 ? 258 VAL A CB  1 
ATOM   2117 C  CG1 . VAL A 1 258 ? 14.136  -24.537 7.496   1.00 20.36 ? 258 VAL A CG1 1 
ATOM   2118 C  CG2 . VAL A 1 258 ? 16.352  -24.372 6.284   1.00 19.50 ? 258 VAL A CG2 1 
ATOM   2119 N  N   . ARG A 1 259 ? 13.913  -21.609 9.298   1.00 15.28 ? 259 ARG A N   1 
ATOM   2120 C  CA  . ARG A 1 259 ? 13.223  -21.245 10.566  1.00 16.03 ? 259 ARG A CA  1 
ATOM   2121 C  C   . ARG A 1 259 ? 11.988  -22.060 10.782  1.00 16.41 ? 259 ARG A C   1 
ATOM   2122 O  O   . ARG A 1 259 ? 11.287  -22.424 9.822   1.00 15.86 ? 259 ARG A O   1 
ATOM   2123 C  CB  . ARG A 1 259 ? 12.964  -19.702 10.582  1.00 16.30 ? 259 ARG A CB  1 
ATOM   2124 C  CG  . ARG A 1 259 ? 14.243  -18.882 10.744  1.00 16.70 ? 259 ARG A CG  1 
ATOM   2125 C  CD  . ARG A 1 259 ? 13.904  -17.391 10.675  1.00 14.08 ? 259 ARG A CD  1 
ATOM   2126 N  NE  . ARG A 1 259 ? 13.274  -16.971 9.426   1.00 15.11 ? 259 ARG A NE  1 
ATOM   2127 C  CZ  . ARG A 1 259 ? 12.469  -15.933 9.249   1.00 14.32 ? 259 ARG A CZ  1 
ATOM   2128 N  NH1 . ARG A 1 259 ? 12.022  -15.209 10.350  1.00 16.74 ? 259 ARG A NH1 1 
ATOM   2129 N  NH2 . ARG A 1 259 ? 11.942  -15.610 8.044   1.00 15.98 ? 259 ARG A NH2 1 
ATOM   2130 N  N   . ALA A 1 260 ? 11.669  -22.421 12.041  1.00 17.60 ? 260 ALA A N   1 
ATOM   2131 C  CA  . ALA A 1 260 ? 10.427  -23.074 12.342  1.00 19.06 ? 260 ALA A CA  1 
ATOM   2132 C  C   . ALA A 1 260 ? 9.450   -22.158 13.043  1.00 16.73 ? 260 ALA A C   1 
ATOM   2133 O  O   . ALA A 1 260 ? 9.901   -21.359 13.907  1.00 18.79 ? 260 ALA A O   1 
ATOM   2134 C  CB  . ALA A 1 260 ? 10.733  -24.328 13.210  1.00 16.53 ? 260 ALA A CB  1 
ATOM   2135 N  N   . SER A 1 261 ? 8.170   -22.310 12.750  1.00 15.88 ? 261 SER A N   1 
ATOM   2136 C  CA  . SER A 1 261 ? 7.066   -21.548 13.382  1.00 18.00 ? 261 SER A CA  1 
ATOM   2137 C  C   . SER A 1 261 ? 6.711   -22.161 14.758  1.00 18.52 ? 261 SER A C   1 
ATOM   2138 O  O   . SER A 1 261 ? 5.880   -21.618 15.501  1.00 21.68 ? 261 SER A O   1 
ATOM   2139 C  CB  . SER A 1 261 ? 5.812   -21.575 12.507  1.00 19.90 ? 261 SER A CB  1 
ATOM   2140 O  OG  . SER A 1 261 ? 5.164   -22.856 12.474  1.00 19.48 ? 261 SER A OG  1 
ATOM   2141 N  N   . PHE A 1 262 ? 7.299   -23.328 15.025  1.00 19.23 ? 262 PHE A N   1 
ATOM   2142 C  CA  . PHE A 1 262 ? 6.802   -24.219 16.098  1.00 23.14 ? 262 PHE A CA  1 
ATOM   2143 C  C   . PHE A 1 262 ? 8.049   -24.747 16.858  1.00 23.43 ? 262 PHE A C   1 
ATOM   2144 O  O   . PHE A 1 262 ? 9.146   -24.919 16.301  1.00 24.16 ? 262 PHE A O   1 
ATOM   2145 C  CB  . PHE A 1 262 ? 5.939   -25.346 15.533  1.00 20.37 ? 262 PHE A CB  1 
ATOM   2146 C  CG  . PHE A 1 262 ? 6.701   -26.268 14.627  1.00 21.25 ? 262 PHE A CG  1 
ATOM   2147 C  CD1 . PHE A 1 262 ? 7.328   -27.407 15.105  1.00 22.28 ? 262 PHE A CD1 1 
ATOM   2148 C  CD2 . PHE A 1 262 ? 6.935   -25.898 13.279  1.00 19.12 ? 262 PHE A CD2 1 
ATOM   2149 C  CE1 . PHE A 1 262 ? 8.076   -28.243 14.253  1.00 22.20 ? 262 PHE A CE1 1 
ATOM   2150 C  CE2 . PHE A 1 262 ? 7.652   -26.731 12.429  1.00 20.64 ? 262 PHE A CE2 1 
ATOM   2151 C  CZ  . PHE A 1 262 ? 8.252   -27.886 12.916  1.00 21.80 ? 262 PHE A CZ  1 
ATOM   2152 N  N   . HIS A 1 263 ? 7.836   -25.048 18.145  1.00 28.83 ? 263 HIS A N   1 
ATOM   2153 C  CA  . HIS A 1 263 ? 8.798   -25.801 18.959  1.00 34.92 ? 263 HIS A CA  1 
ATOM   2154 C  C   . HIS A 1 263 ? 8.072   -26.440 20.093  1.00 38.54 ? 263 HIS A C   1 
ATOM   2155 O  O   . HIS A 1 263 ? 8.777   -27.002 20.922  1.00 47.52 ? 263 HIS A O   1 
ATOM   2156 C  CB  . HIS A 1 263 ? 9.929   -24.928 19.544  1.00 36.30 ? 263 HIS A CB  1 
ATOM   2157 C  CG  . HIS A 1 263 ? 9.476   -23.881 20.571  1.00 38.78 ? 263 HIS A CG  1 
ATOM   2158 N  ND1 . HIS A 1 263 ? 8.219   -23.392 20.635  1.00 39.39 ? 263 HIS A ND1 1 
ATOM   2159 C  CD2 . HIS A 1 263 ? 10.198  -23.200 21.529  1.00 42.04 ? 263 HIS A CD2 1 
ATOM   2160 C  CE1 . HIS A 1 263 ? 8.152   -22.450 21.574  1.00 43.22 ? 263 HIS A CE1 1 
ATOM   2161 N  NE2 . HIS A 1 263 ? 9.361   -22.340 22.130  1.00 44.77 ? 263 HIS A NE2 1 
ATOM   2162 O  OXT . HIS A 1 263 ? 6.815   -26.415 20.199  1.00 39.04 ? 263 HIS A OXT 1 
ATOM   2163 N  N   . SER B 1 6   ? -39.433 -12.390 29.414  1.00 40.96 ? 6   SER B N   1 
ATOM   2164 C  CA  . SER B 1 6   ? -38.426 -12.811 28.349  1.00 36.92 ? 6   SER B CA  1 
ATOM   2165 C  C   . SER B 1 6   ? -37.090 -11.975 28.294  1.00 31.25 ? 6   SER B C   1 
ATOM   2166 O  O   . SER B 1 6   ? -37.120 -10.757 28.333  1.00 27.50 ? 6   SER B O   1 
ATOM   2167 C  CB  . SER B 1 6   ? -39.114 -12.810 27.010  1.00 41.63 ? 6   SER B CB  1 
ATOM   2168 O  OG  . SER B 1 6   ? -38.421 -13.732 26.178  1.00 48.42 ? 6   SER B OG  1 
ATOM   2169 N  N   . TRP B 1 7   ? -35.928 -12.606 28.146  1.00 23.39 ? 7   TRP B N   1 
ATOM   2170 C  CA  . TRP B 1 7   ? -34.622 -11.910 28.395  1.00 19.78 ? 7   TRP B CA  1 
ATOM   2171 C  C   . TRP B 1 7   ? -34.228 -10.947 27.282  1.00 17.76 ? 7   TRP B C   1 
ATOM   2172 O  O   . TRP B 1 7   ? -34.620 -11.096 26.082  1.00 21.56 ? 7   TRP B O   1 
ATOM   2173 C  CB  . TRP B 1 7   ? -33.512 -12.941 28.654  1.00 20.35 ? 7   TRP B CB  1 
ATOM   2174 C  CG  . TRP B 1 7   ? -33.080 -13.688 27.398  1.00 18.91 ? 7   TRP B CG  1 
ATOM   2175 C  CD1 . TRP B 1 7   ? -33.590 -14.864 26.852  1.00 20.18 ? 7   TRP B CD1 1 
ATOM   2176 C  CD2 . TRP B 1 7   ? -32.037 -13.249 26.445  1.00 16.77 ? 7   TRP B CD2 1 
ATOM   2177 N  NE1 . TRP B 1 7   ? -32.916 -15.200 25.692  1.00 19.27 ? 7   TRP B NE1 1 
ATOM   2178 C  CE2 . TRP B 1 7   ? -31.978 -14.274 25.392  1.00 17.94 ? 7   TRP B CE2 1 
ATOM   2179 C  CE3 . TRP B 1 7   ? -31.134 -12.163 26.395  1.00 15.85 ? 7   TRP B CE3 1 
ATOM   2180 C  CZ2 . TRP B 1 7   ? -31.082 -14.181 24.313  1.00 16.25 ? 7   TRP B CZ2 1 
ATOM   2181 C  CZ3 . TRP B 1 7   ? -30.249 -12.089 25.318  1.00 15.43 ? 7   TRP B CZ3 1 
ATOM   2182 C  CH2 . TRP B 1 7   ? -30.220 -13.095 24.306  1.00 17.01 ? 7   TRP B CH2 1 
ATOM   2183 N  N   . GLY B 1 8   ? -33.464 -9.931  27.641  1.00 15.87 ? 8   GLY B N   1 
ATOM   2184 C  CA  . GLY B 1 8   ? -32.874 -8.978  26.615  1.00 14.84 ? 8   GLY B CA  1 
ATOM   2185 C  C   . GLY B 1 8   ? -31.809 -8.117  27.272  1.00 15.72 ? 8   GLY B C   1 
ATOM   2186 O  O   . GLY B 1 8   ? -31.021 -8.564  28.112  1.00 15.60 ? 8   GLY B O   1 
ATOM   2187 N  N   . TYR B 1 9   ? -31.727 -6.863  26.838  1.00 18.00 ? 9   TYR B N   1 
ATOM   2188 C  CA  . TYR B 1 9   ? -30.699 -5.981  27.276  1.00 16.68 ? 9   TYR B CA  1 
ATOM   2189 C  C   . TYR B 1 9   ? -31.279 -4.629  27.810  1.00 19.79 ? 9   TYR B C   1 
ATOM   2190 O  O   . TYR B 1 9   ? -30.540 -3.697  27.992  1.00 19.40 ? 9   TYR B O   1 
ATOM   2191 C  CB  . TYR B 1 9   ? -29.752 -5.657  26.114  1.00 16.27 ? 9   TYR B CB  1 
ATOM   2192 C  CG  . TYR B 1 9   ? -28.964 -6.897  25.650  1.00 14.25 ? 9   TYR B CG  1 
ATOM   2193 C  CD1 . TYR B 1 9   ? -27.742 -7.221  26.291  1.00 14.78 ? 9   TYR B CD1 1 
ATOM   2194 C  CD2 . TYR B 1 9   ? -29.449 -7.636  24.575  1.00 15.40 ? 9   TYR B CD2 1 
ATOM   2195 C  CE1 . TYR B 1 9   ? -27.022 -8.353  25.854  1.00 13.90 ? 9   TYR B CE1 1 
ATOM   2196 C  CE2 . TYR B 1 9   ? -28.771 -8.762  24.124  1.00 13.01 ? 9   TYR B CE2 1 
ATOM   2197 C  CZ  . TYR B 1 9   ? -27.575 -9.108  24.784  1.00 13.16 ? 9   TYR B CZ  1 
ATOM   2198 O  OH  . TYR B 1 9   ? -26.899 -10.224 24.253  1.00 14.20 ? 9   TYR B OH  1 
ATOM   2199 N  N   . ARG B 1 10  ? -32.563 -4.665  28.150  1.00 21.46 ? 10  ARG B N   1 
ATOM   2200 C  CA  . ARG B 1 10  ? -33.299 -3.443  28.612  1.00 23.32 ? 10  ARG B CA  1 
ATOM   2201 C  C   . ARG B 1 10  ? -33.154 -3.433  30.119  1.00 26.69 ? 10  ARG B C   1 
ATOM   2202 O  O   . ARG B 1 10  ? -32.575 -4.368  30.725  1.00 22.49 ? 10  ARG B O   1 
ATOM   2203 C  CB  . ARG B 1 10  ? -34.765 -3.518  28.128  1.00 25.56 ? 10  ARG B CB  1 
ATOM   2204 C  CG  . ARG B 1 10  ? -34.965 -3.397  26.608  1.00 30.12 ? 10  ARG B CG  1 
ATOM   2205 C  CD  . ARG B 1 10  ? -36.321 -3.864  26.147  1.00 36.97 ? 10  ARG B CD  1 
ATOM   2206 N  NE  . ARG B 1 10  ? -37.392 -2.872  26.388  1.00 50.89 ? 10  ARG B NE  1 
ATOM   2207 C  CZ  . ARG B 1 10  ? -38.658 -2.965  25.945  1.00 51.52 ? 10  ARG B CZ  1 
ATOM   2208 N  NH1 . ARG B 1 10  ? -39.094 -3.985  25.202  1.00 48.25 ? 10  ARG B NH1 1 
ATOM   2209 N  NH2 . ARG B 1 10  ? -39.508 -2.004  26.233  1.00 49.11 ? 10  ARG B NH2 1 
ATOM   2210 N  N   . GLU B 1 11  ? -33.676 -2.383  30.773  1.00 26.02 ? 11  GLU B N   1 
ATOM   2211 C  CA  . GLU B 1 11  ? -33.450 -2.218  32.182  1.00 26.76 ? 11  GLU B CA  1 
ATOM   2212 C  C   . GLU B 1 11  ? -34.045 -3.393  32.928  1.00 25.30 ? 11  GLU B C   1 
ATOM   2213 O  O   . GLU B 1 11  ? -33.429 -3.907  33.867  1.00 26.88 ? 11  GLU B O   1 
ATOM   2214 C  CB  . GLU B 1 11  ? -34.169 -0.936  32.623  1.00 37.17 ? 11  GLU B CB  1 
ATOM   2215 C  CG  . GLU B 1 11  ? -34.182 -0.655  34.122  1.00 43.01 ? 11  GLU B CG  1 
ATOM   2216 C  CD  . GLU B 1 11  ? -32.819 -0.292  34.661  1.00 55.37 ? 11  GLU B CD  1 
ATOM   2217 O  OE1 . GLU B 1 11  ? -32.004 0.269   33.891  1.00 63.99 ? 11  GLU B OE1 1 
ATOM   2218 O  OE2 . GLU B 1 11  ? -32.559 -0.553  35.862  1.00 59.66 ? 11  GLU B OE2 1 
ATOM   2219 N  N   A HIS B 1 12  ? -35.256 -3.824  32.613  0.50 24.66 ? 12  HIS B N   1 
ATOM   2220 N  N   B HIS B 1 12  ? -35.227 -3.795  32.492  0.50 22.89 ? 12  HIS B N   1 
ATOM   2221 C  CA  A HIS B 1 12  ? -35.845 -4.880  33.483  0.50 24.96 ? 12  HIS B CA  1 
ATOM   2222 C  CA  B HIS B 1 12  ? -36.021 -4.789  33.227  0.50 23.99 ? 12  HIS B CA  1 
ATOM   2223 C  C   A HIS B 1 12  ? -35.777 -6.267  32.920  0.50 23.12 ? 12  HIS B C   1 
ATOM   2224 C  C   B HIS B 1 12  ? -35.540 -6.202  33.054  0.50 24.45 ? 12  HIS B C   1 
ATOM   2225 O  O   A HIS B 1 12  ? -36.418 -7.188  33.422  0.50 20.27 ? 12  HIS B O   1 
ATOM   2226 O  O   B HIS B 1 12  ? -35.644 -7.055  33.953  0.50 24.46 ? 12  HIS B O   1 
ATOM   2227 C  CB  A HIS B 1 12  ? -37.293 -4.590  33.931  0.50 30.79 ? 12  HIS B CB  1 
ATOM   2228 C  CB  B HIS B 1 12  ? -37.519 -4.689  32.858  0.50 25.32 ? 12  HIS B CB  1 
ATOM   2229 C  CG  A HIS B 1 12  ? -37.520 -3.175  34.397  0.50 33.25 ? 12  HIS B CG  1 
ATOM   2230 C  CG  B HIS B 1 12  ? -37.817 -4.786  31.382  0.50 28.90 ? 12  HIS B CG  1 
ATOM   2231 N  ND1 A HIS B 1 12  ? -38.452 -2.377  33.836  0.50 34.83 ? 12  HIS B ND1 1 
ATOM   2232 N  ND1 B HIS B 1 12  ? -37.508 -3.806  30.519  0.50 28.30 ? 12  HIS B ND1 1 
ATOM   2233 C  CD2 A HIS B 1 12  ? -36.884 -2.418  35.389  0.50 33.30 ? 12  HIS B CD2 1 
ATOM   2234 C  CD2 B HIS B 1 12  ? -38.459 -5.777  30.639  0.50 26.98 ? 12  HIS B CD2 1 
ATOM   2235 C  CE1 A HIS B 1 12  ? -38.428 -1.177  34.441  0.50 36.03 ? 12  HIS B CE1 1 
ATOM   2236 C  CE1 B HIS B 1 12  ? -37.928 -4.156  29.286  0.50 27.01 ? 12  HIS B CE1 1 
ATOM   2237 N  NE2 A HIS B 1 12  ? -37.452 -1.203  35.386  0.50 39.78 ? 12  HIS B NE2 1 
ATOM   2238 N  NE2 B HIS B 1 12  ? -38.510 -5.352  29.364  0.50 28.79 ? 12  HIS B NE2 1 
ATOM   2239 N  N   . ASN B 1 13  ? -34.966 -6.466  31.882  1.00 21.14 ? 13  ASN B N   1 
ATOM   2240 C  CA  . ASN B 1 13  ? -34.705 -7.867  31.462  1.00 20.25 ? 13  ASN B CA  1 
ATOM   2241 C  C   . ASN B 1 13  ? -33.244 -8.064  31.044  1.00 15.52 ? 13  ASN B C   1 
ATOM   2242 O  O   . ASN B 1 13  ? -32.954 -9.129  30.486  1.00 18.98 ? 13  ASN B O   1 
ATOM   2243 C  CB  . ASN B 1 13  ? -35.643 -8.298  30.317  1.00 18.08 ? 13  ASN B CB  1 
ATOM   2244 C  CG  . ASN B 1 13  ? -35.391 -7.517  29.031  1.00 17.26 ? 13  ASN B CG  1 
ATOM   2245 O  OD1 . ASN B 1 13  ? -34.476 -6.712  28.947  1.00 19.11 ? 13  ASN B OD1 1 
ATOM   2246 N  ND2 . ASN B 1 13  ? -36.195 -7.838  27.982  1.00 18.79 ? 13  ASN B ND2 1 
ATOM   2247 N  N   . GLY B 1 14  ? -32.365 -7.127  31.417  1.00 17.22 ? 14  GLY B N   1 
ATOM   2248 C  CA  . GLY B 1 14  ? -30.959 -7.130  30.926  1.00 16.09 ? 14  GLY B CA  1 
ATOM   2249 C  C   . GLY B 1 14  ? -30.079 -8.039  31.780  1.00 16.95 ? 14  GLY B C   1 
ATOM   2250 O  O   . GLY B 1 14  ? -30.554 -8.738  32.719  1.00 16.14 ? 14  GLY B O   1 
ATOM   2251 N  N   . PRO B 1 15  ? -28.757 -8.022  31.540  1.00 14.85 ? 15  PRO B N   1 
ATOM   2252 C  CA  . PRO B 1 15  ? -27.755 -8.967  32.086  1.00 15.73 ? 15  PRO B CA  1 
ATOM   2253 C  C   . PRO B 1 15  ? -27.827 -9.095  33.640  1.00 16.43 ? 15  PRO B C   1 
ATOM   2254 O  O   . PRO B 1 15  ? -27.690 -10.196 34.108  1.00 15.59 ? 15  PRO B O   1 
ATOM   2255 C  CB  . PRO B 1 15  ? -26.415 -8.358  31.597  1.00 16.37 ? 15  PRO B CB  1 
ATOM   2256 C  CG  . PRO B 1 15  ? -26.822 -7.826  30.226  1.00 16.08 ? 15  PRO B CG  1 
ATOM   2257 C  CD  . PRO B 1 15  ? -28.256 -7.297  30.346  1.00 15.14 ? 15  PRO B CD  1 
ATOM   2258 N  N   . ILE B 1 16  ? -28.088 -8.025  34.394  1.00 16.51 ? 16  ILE B N   1 
ATOM   2259 C  CA  . ILE B 1 16  ? -28.089 -8.146  35.853  1.00 19.58 ? 16  ILE B CA  1 
ATOM   2260 C  C   . ILE B 1 16  ? -29.212 -9.027  36.338  1.00 19.61 ? 16  ILE B C   1 
ATOM   2261 O  O   . ILE B 1 16  ? -29.098 -9.588  37.399  1.00 18.77 ? 16  ILE B O   1 
ATOM   2262 C  CB  . ILE B 1 16  ? -28.151 -6.735  36.504  1.00 22.58 ? 16  ILE B CB  1 
ATOM   2263 C  CG1 . ILE B 1 16  ? -27.396 -6.815  37.857  1.00 27.92 ? 16  ILE B CG1 1 
ATOM   2264 C  CG2 . ILE B 1 16  ? -29.564 -6.179  36.437  1.00 23.45 ? 16  ILE B CG2 1 
ATOM   2265 C  CD1 . ILE B 1 16  ? -27.192 -5.485  38.597  1.00 36.35 ? 16  ILE B CD1 1 
ATOM   2266 N  N   . HIS B 1 17  ? -30.277 -9.141  35.541  1.00 17.01 ? 17  HIS B N   1 
ATOM   2267 C  CA  . HIS B 1 17  ? -31.466 -9.984  35.862  1.00 14.85 ? 17  HIS B CA  1 
ATOM   2268 C  C   . HIS B 1 17  ? -31.410 -11.384 35.338  1.00 14.55 ? 17  HIS B C   1 
ATOM   2269 O  O   . HIS B 1 17  ? -32.259 -12.218 35.674  1.00 14.08 ? 17  HIS B O   1 
ATOM   2270 C  CB  . HIS B 1 17  ? -32.769 -9.364  35.335  1.00 16.25 ? 17  HIS B CB  1 
ATOM   2271 C  CG  . HIS B 1 17  ? -32.991 -7.998  35.886  1.00 19.98 ? 17  HIS B CG  1 
ATOM   2272 N  ND1 . HIS B 1 17  ? -33.292 -7.793  37.221  1.00 21.94 ? 17  HIS B ND1 1 
ATOM   2273 C  CD2 . HIS B 1 17  ? -32.933 -6.737  35.278  1.00 20.39 ? 17  HIS B CD2 1 
ATOM   2274 C  CE1 . HIS B 1 17  ? -33.410 -6.449  37.436  1.00 25.29 ? 17  HIS B CE1 1 
ATOM   2275 N  NE2 . HIS B 1 17  ? -33.256 -5.810  36.240  1.00 25.86 ? 17  HIS B NE2 1 
ATOM   2276 N  N   . TRP B 1 18  ? -30.453 -11.688 34.460  1.00 14.14 ? 18  TRP B N   1 
ATOM   2277 C  CA  . TRP B 1 18  ? -30.466 -13.072 33.897  1.00 13.39 ? 18  TRP B CA  1 
ATOM   2278 C  C   . TRP B 1 18  ? -30.426 -14.183 34.880  1.00 12.65 ? 18  TRP B C   1 
ATOM   2279 O  O   . TRP B 1 18  ? -31.101 -15.186 34.694  1.00 14.37 ? 18  TRP B O   1 
ATOM   2280 C  CB  . TRP B 1 18  ? -29.317 -13.190 32.870  1.00 13.31 ? 18  TRP B CB  1 
ATOM   2281 C  CG  . TRP B 1 18  ? -29.525 -12.265 31.659  1.00 12.56 ? 18  TRP B CG  1 
ATOM   2282 C  CD1 . TRP B 1 18  ? -30.638 -11.537 31.297  1.00 13.64 ? 18  TRP B CD1 1 
ATOM   2283 C  CD2 . TRP B 1 18  ? -28.536 -12.071 30.585  1.00 13.20 ? 18  TRP B CD2 1 
ATOM   2284 N  NE1 . TRP B 1 18  ? -30.440 -10.853 30.083  1.00 13.88 ? 18  TRP B NE1 1 
ATOM   2285 C  CE2 . TRP B 1 18  ? -29.169 -11.179 29.592  1.00 12.40 ? 18  TRP B CE2 1 
ATOM   2286 C  CE3 . TRP B 1 18  ? -27.257 -12.567 30.358  1.00 12.89 ? 18  TRP B CE3 1 
ATOM   2287 C  CZ2 . TRP B 1 18  ? -28.508 -10.753 28.448  1.00 14.19 ? 18  TRP B CZ2 1 
ATOM   2288 C  CZ3 . TRP B 1 18  ? -26.565 -12.142 29.190  1.00 13.90 ? 18  TRP B CZ3 1 
ATOM   2289 C  CH2 . TRP B 1 18  ? -27.239 -11.254 28.257  1.00 12.59 ? 18  TRP B CH2 1 
ATOM   2290 N  N   . LYS B 1 19  ? -29.684 -13.993 35.972  1.00 12.41 ? 19  LYS B N   1 
ATOM   2291 C  CA  . LYS B 1 19  ? -29.585 -15.053 37.024  1.00 12.59 ? 19  LYS B CA  1 
ATOM   2292 C  C   . LYS B 1 19  ? -30.900 -15.402 37.684  1.00 15.61 ? 19  LYS B C   1 
ATOM   2293 O  O   . LYS B 1 19  ? -30.973 -16.506 38.248  1.00 16.22 ? 19  LYS B O   1 
ATOM   2294 C  CB  . LYS B 1 19  ? -28.573 -14.645 38.133  1.00 14.29 ? 19  LYS B CB  1 
ATOM   2295 C  CG  . LYS B 1 19  ? -29.107 -13.396 38.927  1.00 16.36 ? 19  LYS B CG  1 
ATOM   2296 C  CD  . LYS B 1 19  ? -28.115 -12.949 39.980  1.00 18.02 ? 19  LYS B CD  1 
ATOM   2297 C  CE  . LYS B 1 19  ? -28.427 -13.689 41.279  1.00 25.73 ? 19  LYS B CE  1 
ATOM   2298 N  NZ  . LYS B 1 19  ? -27.394 -13.564 42.357  1.00 29.01 ? 19  LYS B NZ  1 
ATOM   2299 N  N   . GLU B 1 20  ? -31.899 -14.532 37.567  1.00 16.71 ? 20  GLU B N   1 
ATOM   2300 C  CA  . GLU B 1 20  ? -33.251 -14.830 38.118  1.00 16.46 ? 20  GLU B CA  1 
ATOM   2301 C  C   . GLU B 1 20  ? -33.861 -16.044 37.443  1.00 17.63 ? 20  GLU B C   1 
ATOM   2302 O  O   . GLU B 1 20  ? -34.664 -16.765 38.043  1.00 17.88 ? 20  GLU B O   1 
ATOM   2303 C  CB  . GLU B 1 20  ? -34.208 -13.594 37.914  1.00 17.03 ? 20  GLU B CB  1 
ATOM   2304 C  CG  . GLU B 1 20  ? -33.667 -12.457 38.768  1.00 16.84 ? 20  GLU B CG  1 
ATOM   2305 C  CD  . GLU B 1 20  ? -34.291 -11.126 38.405  1.00 18.01 ? 20  GLU B CD  1 
ATOM   2306 O  OE1 . GLU B 1 20  ? -35.394 -11.128 37.758  1.00 21.58 ? 20  GLU B OE1 1 
ATOM   2307 O  OE2 . GLU B 1 20  ? -33.616 -10.132 38.695  1.00 21.15 ? 20  GLU B OE2 1 
ATOM   2308 N  N   . PHE B 1 21  ? -33.481 -16.307 36.197  1.00 16.04 ? 21  PHE B N   1 
ATOM   2309 C  CA  . PHE B 1 21  ? -34.091 -17.284 35.328  1.00 17.75 ? 21  PHE B CA  1 
ATOM   2310 C  C   . PHE B 1 21  ? -33.106 -18.306 34.855  1.00 16.16 ? 21  PHE B C   1 
ATOM   2311 O  O   . PHE B 1 21  ? -33.503 -19.385 34.508  1.00 16.45 ? 21  PHE B O   1 
ATOM   2312 C  CB  . PHE B 1 21  ? -34.852 -16.608 34.119  1.00 20.13 ? 21  PHE B CB  1 
ATOM   2313 C  CG  . PHE B 1 21  ? -36.040 -15.785 34.615  1.00 29.14 ? 21  PHE B CG  1 
ATOM   2314 C  CD1 . PHE B 1 21  ? -35.881 -14.431 34.883  1.00 32.92 ? 21  PHE B CD1 1 
ATOM   2315 C  CD2 . PHE B 1 21  ? -37.192 -16.421 35.000  1.00 30.63 ? 21  PHE B CD2 1 
ATOM   2316 C  CE1 . PHE B 1 21  ? -36.932 -13.700 35.442  1.00 34.72 ? 21  PHE B CE1 1 
ATOM   2317 C  CE2 . PHE B 1 21  ? -38.258 -15.703 35.568  1.00 34.08 ? 21  PHE B CE2 1 
ATOM   2318 C  CZ  . PHE B 1 21  ? -38.118 -14.346 35.774  1.00 37.47 ? 21  PHE B CZ  1 
ATOM   2319 N  N   . PHE B 1 22  ? -31.815 -17.975 34.904  1.00 13.59 ? 22  PHE B N   1 
ATOM   2320 C  CA  . PHE B 1 22  ? -30.695 -18.825 34.434  1.00 13.55 ? 22  PHE B CA  1 
ATOM   2321 C  C   . PHE B 1 22  ? -29.612 -18.771 35.482  1.00 14.01 ? 22  PHE B C   1 
ATOM   2322 O  O   . PHE B 1 22  ? -28.710 -17.922 35.463  1.00 13.58 ? 22  PHE B O   1 
ATOM   2323 C  CB  . PHE B 1 22  ? -30.134 -18.387 33.076  1.00 15.01 ? 22  PHE B CB  1 
ATOM   2324 C  CG  . PHE B 1 22  ? -31.209 -18.300 32.003  1.00 15.25 ? 22  PHE B CG  1 
ATOM   2325 C  CD1 . PHE B 1 22  ? -31.516 -19.433 31.284  1.00 16.94 ? 22  PHE B CD1 1 
ATOM   2326 C  CD2 . PHE B 1 22  ? -31.948 -17.103 31.775  1.00 14.70 ? 22  PHE B CD2 1 
ATOM   2327 C  CE1 . PHE B 1 22  ? -32.514 -19.374 30.278  1.00 18.17 ? 22  PHE B CE1 1 
ATOM   2328 C  CE2 . PHE B 1 22  ? -32.976 -17.082 30.817  1.00 15.54 ? 22  PHE B CE2 1 
ATOM   2329 C  CZ  . PHE B 1 22  ? -33.250 -18.201 30.081  1.00 15.97 ? 22  PHE B CZ  1 
ATOM   2330 N  N   . PRO B 1 23  ? -29.734 -19.623 36.536  1.00 14.54 ? 23  PRO B N   1 
ATOM   2331 C  CA  . PRO B 1 23  ? -28.713 -19.562 37.643  1.00 14.63 ? 23  PRO B CA  1 
ATOM   2332 C  C   . PRO B 1 23  ? -27.275 -19.772 37.262  1.00 13.53 ? 23  PRO B C   1 
ATOM   2333 O  O   . PRO B 1 23  ? -26.402 -19.282 37.980  1.00 15.51 ? 23  PRO B O   1 
ATOM   2334 C  CB  . PRO B 1 23  ? -29.168 -20.675 38.636  1.00 14.98 ? 23  PRO B CB  1 
ATOM   2335 C  CG  . PRO B 1 23  ? -30.346 -21.324 37.995  1.00 20.99 ? 23  PRO B CG  1 
ATOM   2336 C  CD  . PRO B 1 23  ? -30.824 -20.589 36.789  1.00 16.25 ? 23  PRO B CD  1 
ATOM   2337 N  N   . ILE B 1 24  ? -27.037 -20.387 36.080  1.00 13.59 ? 24  ILE B N   1 
ATOM   2338 C  CA  . ILE B 1 24  ? -25.678 -20.563 35.671  1.00 13.55 ? 24  ILE B CA  1 
ATOM   2339 C  C   . ILE B 1 24  ? -25.050 -19.229 35.371  1.00 13.39 ? 24  ILE B C   1 
ATOM   2340 O  O   . ILE B 1 24  ? -23.881 -19.181 35.173  1.00 13.51 ? 24  ILE B O   1 
ATOM   2341 C  CB  . ILE B 1 24  ? -25.591 -21.563 34.486  1.00 13.42 ? 24  ILE B CB  1 
ATOM   2342 C  CG1 . ILE B 1 24  ? -24.180 -22.088 34.320  1.00 14.86 ? 24  ILE B CG1 1 
ATOM   2343 C  CG2 . ILE B 1 24  ? -25.983 -20.868 33.197  1.00 14.21 ? 24  ILE B CG2 1 
ATOM   2344 C  CD1 . ILE B 1 24  ? -23.614 -22.865 35.520  1.00 20.57 ? 24  ILE B CD1 1 
ATOM   2345 N  N   . ALA B 1 25  ? -25.838 -18.133 35.271  1.00 13.57 ? 25  ALA B N   1 
ATOM   2346 C  CA  . ALA B 1 25  ? -25.268 -16.785 35.047  1.00 13.50 ? 25  ALA B CA  1 
ATOM   2347 C  C   . ALA B 1 25  ? -24.163 -16.449 36.054  1.00 13.68 ? 25  ALA B C   1 
ATOM   2348 O  O   . ALA B 1 25  ? -23.261 -15.658 35.786  1.00 14.19 ? 25  ALA B O   1 
ATOM   2349 C  CB  . ALA B 1 25  ? -26.405 -15.711 35.164  1.00 12.32 ? 25  ALA B CB  1 
ATOM   2350 N  N   . ASP B 1 26  ? -24.249 -17.068 37.268  1.00 14.64 ? 26  ASP B N   1 
ATOM   2351 C  CA  . ASP B 1 26  ? -23.209 -16.897 38.320  1.00 16.21 ? 26  ASP B CA  1 
ATOM   2352 C  C   . ASP B 1 26  ? -22.274 -18.113 38.406  1.00 17.36 ? 26  ASP B C   1 
ATOM   2353 O  O   . ASP B 1 26  ? -21.530 -18.336 39.441  1.00 17.02 ? 26  ASP B O   1 
ATOM   2354 C  CB  . ASP B 1 26  ? -23.965 -16.732 39.690  1.00 15.99 ? 26  ASP B CB  1 
ATOM   2355 C  CG  . ASP B 1 26  ? -24.709 -15.472 39.744  1.00 19.64 ? 26  ASP B CG  1 
ATOM   2356 O  OD1 . ASP B 1 26  ? -24.090 -14.437 39.429  1.00 21.82 ? 26  ASP B OD1 1 
ATOM   2357 O  OD2 . ASP B 1 26  ? -25.878 -15.539 40.243  1.00 21.92 ? 26  ASP B OD2 1 
ATOM   2358 N  N   . GLY B 1 27  ? -22.147 -18.859 37.306  1.00 15.02 ? 27  GLY B N   1 
ATOM   2359 C  CA  . GLY B 1 27  ? -21.317 -20.089 37.257  1.00 16.19 ? 27  GLY B CA  1 
ATOM   2360 C  C   . GLY B 1 27  ? -19.811 -19.850 37.292  1.00 14.92 ? 27  GLY B C   1 
ATOM   2361 O  O   . GLY B 1 27  ? -19.344 -18.733 37.361  1.00 16.92 ? 27  GLY B O   1 
ATOM   2362 N  N   A ASP B 1 28  ? -18.978 -20.857 37.284  0.50 16.43 ? 28  ASP B N   1 
ATOM   2363 N  N   B ASP B 1 28  ? -19.112 -20.982 37.198  0.50 17.44 ? 28  ASP B N   1 
ATOM   2364 C  CA  A ASP B 1 28  ? -17.612 -20.397 37.400  0.50 15.13 ? 28  ASP B CA  1 
ATOM   2365 C  CA  B ASP B 1 28  ? -17.673 -20.971 37.360  0.50 17.10 ? 28  ASP B CA  1 
ATOM   2366 C  C   A ASP B 1 28  ? -16.897 -20.303 36.064  0.50 13.51 ? 28  ASP B C   1 
ATOM   2367 C  C   B ASP B 1 28  ? -16.895 -20.696 36.072  0.50 13.92 ? 28  ASP B C   1 
ATOM   2368 O  O   A ASP B 1 28  ? -15.745 -19.906 36.084  0.50 14.28 ? 28  ASP B O   1 
ATOM   2369 O  O   B ASP B 1 28  ? -15.707 -20.518 36.176  0.50 14.60 ? 28  ASP B O   1 
ATOM   2370 C  CB  A ASP B 1 28  ? -16.771 -21.152 38.436  0.50 16.94 ? 28  ASP B CB  1 
ATOM   2371 C  CB  B ASP B 1 28  ? -17.091 -22.124 38.221  0.50 23.29 ? 28  ASP B CB  1 
ATOM   2372 C  CG  A ASP B 1 28  ? -17.579 -21.562 39.692  0.50 15.27 ? 28  ASP B CG  1 
ATOM   2373 C  CG  B ASP B 1 28  ? -17.336 -23.470 37.661  0.50 25.61 ? 28  ASP B CG  1 
ATOM   2374 O  OD1 A ASP B 1 28  ? -18.038 -20.656 40.474  0.50 18.63 ? 28  ASP B OD1 1 
ATOM   2375 O  OD1 B ASP B 1 28  ? -17.332 -23.487 36.427  0.50 33.48 ? 28  ASP B OD1 1 
ATOM   2376 O  OD2 A ASP B 1 28  ? -17.743 -22.803 39.831  0.50 13.87 ? 28  ASP B OD2 1 
ATOM   2377 O  OD2 B ASP B 1 28  ? -17.494 -24.519 38.424  0.50 20.94 ? 28  ASP B OD2 1 
ATOM   2378 N  N   . GLN B 1 29  ? -17.589 -20.533 34.924  1.00 12.70 ? 29  GLN B N   1 
ATOM   2379 C  CA  . GLN B 1 29  ? -16.833 -20.340 33.620  1.00 12.42 ? 29  GLN B CA  1 
ATOM   2380 C  C   . GLN B 1 29  ? -17.688 -19.458 32.722  1.00 10.79 ? 29  GLN B C   1 
ATOM   2381 O  O   . GLN B 1 29  ? -18.024 -19.837 31.617  1.00 12.74 ? 29  GLN B O   1 
ATOM   2382 C  CB  . GLN B 1 29  ? -16.484 -21.686 32.901  1.00 14.46 ? 29  GLN B CB  1 
ATOM   2383 C  CG  . GLN B 1 29  ? -15.497 -22.516 33.764  1.00 15.33 ? 29  GLN B CG  1 
ATOM   2384 C  CD  . GLN B 1 29  ? -14.693 -23.527 32.947  1.00 18.52 ? 29  GLN B CD  1 
ATOM   2385 O  OE1 . GLN B 1 29  ? -15.234 -24.134 31.984  1.00 19.67 ? 29  GLN B OE1 1 
ATOM   2386 N  NE2 . GLN B 1 29  ? -13.428 -23.754 33.397  1.00 21.86 ? 29  GLN B NE2 1 
ATOM   2387 N  N   . GLN B 1 30  ? -18.014 -18.258 33.242  1.00 10.53 ? 30  GLN B N   1 
ATOM   2388 C  CA  . GLN B 1 30  ? -18.927 -17.355 32.495  1.00 10.54 ? 30  GLN B CA  1 
ATOM   2389 C  C   . GLN B 1 30  ? -18.107 -16.378 31.598  1.00 10.06 ? 30  GLN B C   1 
ATOM   2390 O  O   . GLN B 1 30  ? -16.985 -16.018 31.874  1.00 10.39 ? 30  GLN B O   1 
ATOM   2391 C  CB  . GLN B 1 30  ? -19.868 -16.628 33.433  1.00 10.98 ? 30  GLN B CB  1 
ATOM   2392 C  CG  . GLN B 1 30  ? -20.918 -17.556 34.030  1.00 9.55  ? 30  GLN B CG  1 
ATOM   2393 C  CD  . GLN B 1 30  ? -21.896 -17.936 32.983  1.00 10.28 ? 30  GLN B CD  1 
ATOM   2394 O  OE1 . GLN B 1 30  ? -22.674 -17.094 32.470  1.00 10.58 ? 30  GLN B OE1 1 
ATOM   2395 N  NE2 . GLN B 1 30  ? -21.881 -19.237 32.606  1.00 11.59 ? 30  GLN B NE2 1 
ATOM   2396 N  N   . SER B 1 31  ? -18.750 -15.973 30.514  1.00 10.52 ? 31  SER B N   1 
ATOM   2397 C  CA  . SER B 1 31  ? -18.099 -15.079 29.510  1.00 9.99  ? 31  SER B CA  1 
ATOM   2398 C  C   . SER B 1 31  ? -19.067 -13.899 29.240  1.00 9.30  ? 31  SER B C   1 
ATOM   2399 O  O   . SER B 1 31  ? -20.300 -13.976 29.488  1.00 10.89 ? 31  SER B O   1 
ATOM   2400 C  CB  . SER B 1 31  ? -17.919 -15.868 28.160  1.00 10.85 ? 31  SER B CB  1 
ATOM   2401 O  OG  . SER B 1 31  ? -16.908 -16.836 28.337  1.00 10.83 ? 31  SER B OG  1 
ATOM   2402 N  N   . PRO B 1 32  ? -18.520 -12.761 28.791  1.00 10.58 ? 32  PRO B N   1 
ATOM   2403 C  CA  . PRO B 1 32  ? -17.128 -12.531 28.461  1.00 10.12 ? 32  PRO B CA  1 
ATOM   2404 C  C   . PRO B 1 32  ? -16.272 -12.175 29.694  1.00 11.42 ? 32  PRO B C   1 
ATOM   2405 O  O   . PRO B 1 32  ? -16.818 -12.222 30.849  1.00 12.99 ? 32  PRO B O   1 
ATOM   2406 C  CB  . PRO B 1 32  ? -17.247 -11.298 27.494  1.00 10.59 ? 32  PRO B CB  1 
ATOM   2407 C  CG  . PRO B 1 32  ? -18.363 -10.506 28.180  1.00 9.71  ? 32  PRO B CG  1 
ATOM   2408 C  CD  . PRO B 1 32  ? -19.366 -11.569 28.540  1.00 11.01 ? 32  PRO B CD  1 
ATOM   2409 N  N   . ILE B 1 33  ? -15.029 -11.824 29.438  1.00 10.24 ? 33  ILE B N   1 
ATOM   2410 C  CA  . ILE B 1 33  ? -14.088 -11.496 30.532  1.00 11.22 ? 33  ILE B CA  1 
ATOM   2411 C  C   . ILE B 1 33  ? -13.229 -10.363 30.080  1.00 12.08 ? 33  ILE B C   1 
ATOM   2412 O  O   . ILE B 1 33  ? -13.167 -9.976  28.885  1.00 13.62 ? 33  ILE B O   1 
ATOM   2413 C  CB  . ILE B 1 33  ? -13.183 -12.706 30.884  1.00 12.25 ? 33  ILE B CB  1 
ATOM   2414 C  CG1 . ILE B 1 33  ? -12.235 -13.110 29.685  1.00 11.75 ? 33  ILE B CG1 1 
ATOM   2415 C  CG2 . ILE B 1 33  ? -14.057 -13.896 31.411  1.00 11.65 ? 33  ILE B CG2 1 
ATOM   2416 C  CD1 . ILE B 1 33  ? -11.097 -14.071 30.087  1.00 13.12 ? 33  ILE B CD1 1 
ATOM   2417 N  N   . GLU B 1 34  ? -12.511 -9.791  31.080  1.00 12.54 ? 34  GLU B N   1 
ATOM   2418 C  CA  . GLU B 1 34  ? -11.419 -8.945  30.748  1.00 12.07 ? 34  GLU B CA  1 
ATOM   2419 C  C   . GLU B 1 34  ? -10.149 -9.728  30.559  1.00 13.50 ? 34  GLU B C   1 
ATOM   2420 O  O   . GLU B 1 34  ? -9.762  -10.535 31.447  1.00 16.21 ? 34  GLU B O   1 
ATOM   2421 C  CB  . GLU B 1 34  ? -11.218 -7.891  31.922  1.00 13.88 ? 34  GLU B CB  1 
ATOM   2422 C  CG  . GLU B 1 34  ? -10.105 -6.945  31.430  1.00 16.00 ? 34  GLU B CG  1 
ATOM   2423 C  CD  . GLU B 1 34  ? -9.575  -5.939  32.481  1.00 19.03 ? 34  GLU B CD  1 
ATOM   2424 O  OE1 . GLU B 1 34  ? -9.864  -6.122  33.681  1.00 21.42 ? 34  GLU B OE1 1 
ATOM   2425 O  OE2 . GLU B 1 34  ? -8.886  -4.940  32.090  1.00 19.81 ? 34  GLU B OE2 1 
ATOM   2426 N  N   . ILE B 1 35  ? -9.525  -9.592  29.408  1.00 12.91 ? 35  ILE B N   1 
ATOM   2427 C  CA  . ILE B 1 35  ? -8.214  -10.189 29.168  1.00 13.81 ? 35  ILE B CA  1 
ATOM   2428 C  C   . ILE B 1 35  ? -7.101  -9.207  29.727  1.00 15.46 ? 35  ILE B C   1 
ATOM   2429 O  O   . ILE B 1 35  ? -7.005  -8.055  29.225  1.00 18.01 ? 35  ILE B O   1 
ATOM   2430 C  CB  . ILE B 1 35  ? -8.083  -10.329 27.665  1.00 14.33 ? 35  ILE B CB  1 
ATOM   2431 C  CG1 . ILE B 1 35  ? -9.115  -11.357 27.150  1.00 14.99 ? 35  ILE B CG1 1 
ATOM   2432 C  CG2 . ILE B 1 35  ? -6.627  -10.737 27.280  1.00 17.30 ? 35  ILE B CG2 1 
ATOM   2433 C  CD1 . ILE B 1 35  ? -9.384  -11.388 25.655  1.00 19.27 ? 35  ILE B CD1 1 
ATOM   2434 N  N   . LYS B 1 36  ? -6.312  -9.690  30.703  1.00 18.50 ? 36  LYS B N   1 
ATOM   2435 C  CA  . LYS B 1 36  ? -5.337  -8.887  31.483  1.00 22.03 ? 36  LYS B CA  1 
ATOM   2436 C  C   . LYS B 1 36  ? -3.996  -9.382  30.902  1.00 24.37 ? 36  LYS B C   1 
ATOM   2437 O  O   . LYS B 1 36  ? -3.553  -10.495 31.215  1.00 23.90 ? 36  LYS B O   1 
ATOM   2438 C  CB  . LYS B 1 36  ? -5.500  -9.196  32.950  1.00 23.09 ? 36  LYS B CB  1 
ATOM   2439 C  CG  . LYS B 1 36  ? -6.838  -8.641  33.498  1.00 29.27 ? 36  LYS B CG  1 
ATOM   2440 C  CD  . LYS B 1 36  ? -7.201  -9.044  34.954  1.00 31.34 ? 36  LYS B CD  1 
ATOM   2441 C  CE  . LYS B 1 36  ? -7.938  -10.398 34.909  1.00 39.18 ? 36  LYS B CE  1 
ATOM   2442 N  NZ  . LYS B 1 36  ? -8.516  -11.015 36.162  1.00 44.28 ? 36  LYS B NZ  1 
ATOM   2443 N  N   . THR B 1 37  ? -3.421  -8.633  29.980  1.00 23.10 ? 37  THR B N   1 
ATOM   2444 C  CA  . THR B 1 37  ? -2.225  -9.159  29.305  1.00 25.86 ? 37  THR B CA  1 
ATOM   2445 C  C   . THR B 1 37  ? -1.070  -9.561  30.275  1.00 31.05 ? 37  THR B C   1 
ATOM   2446 O  O   . THR B 1 37  ? -0.343  -10.525 29.972  1.00 33.14 ? 37  THR B O   1 
ATOM   2447 C  CB  . THR B 1 37  ? -1.778  -8.303  28.136  1.00 24.16 ? 37  THR B CB  1 
ATOM   2448 O  OG1 . THR B 1 37  ? -1.381  -7.020  28.606  1.00 30.08 ? 37  THR B OG1 1 
ATOM   2449 C  CG2 . THR B 1 37  ? -2.899  -8.124  27.098  1.00 26.64 ? 37  THR B CG2 1 
ATOM   2450 N  N   . LYS B 1 38  ? -0.934  -8.916  31.447  1.00 33.67 ? 38  LYS B N   1 
ATOM   2451 C  CA  . LYS B 1 38  ? 0.144   -9.371  32.394  1.00 38.59 ? 38  LYS B CA  1 
ATOM   2452 C  C   . LYS B 1 38  ? -0.063  -10.717 33.106  1.00 35.81 ? 38  LYS B C   1 
ATOM   2453 O  O   . LYS B 1 38  ? 0.887   -11.313 33.615  1.00 34.85 ? 38  LYS B O   1 
ATOM   2454 C  CB  . LYS B 1 38  ? 0.570   -8.280  33.393  1.00 48.45 ? 38  LYS B CB  1 
ATOM   2455 C  CG  . LYS B 1 38  ? -0.551  -7.556  34.108  1.00 54.40 ? 38  LYS B CG  1 
ATOM   2456 C  CD  . LYS B 1 38  ? -0.103  -6.144  34.528  1.00 66.15 ? 38  LYS B CD  1 
ATOM   2457 C  CE  . LYS B 1 38  ? 0.071   -5.177  33.339  1.00 64.64 ? 38  LYS B CE  1 
ATOM   2458 N  NZ  . LYS B 1 38  ? 0.269   -3.744  33.714  1.00 55.74 ? 38  LYS B NZ  1 
ATOM   2459 N  N   . GLU B 1 39  ? -1.296  -11.206 33.067  1.00 29.32 ? 39  GLU B N   1 
ATOM   2460 C  CA  . GLU B 1 39  ? -1.680  -12.441 33.650  1.00 30.49 ? 39  GLU B CA  1 
ATOM   2461 C  C   . GLU B 1 39  ? -1.787  -13.489 32.545  1.00 25.57 ? 39  GLU B C   1 
ATOM   2462 O  O   . GLU B 1 39  ? -2.003  -14.673 32.859  1.00 27.33 ? 39  GLU B O   1 
ATOM   2463 C  CB  . GLU B 1 39  ? -3.041  -12.291 34.340  1.00 32.86 ? 39  GLU B CB  1 
ATOM   2464 C  CG  . GLU B 1 39  ? -3.084  -11.203 35.424  1.00 38.13 ? 39  GLU B CG  1 
ATOM   2465 C  CD  . GLU B 1 39  ? -4.351  -11.259 36.291  1.00 45.50 ? 39  GLU B CD  1 
ATOM   2466 O  OE1 . GLU B 1 39  ? -4.607  -10.246 37.007  1.00 48.86 ? 39  GLU B OE1 1 
ATOM   2467 O  OE2 . GLU B 1 39  ? -5.117  -12.293 36.257  1.00 43.36 ? 39  GLU B OE2 1 
ATOM   2468 N  N   . VAL B 1 40  ? -1.711  -13.069 31.276  1.00 24.92 ? 40  VAL B N   1 
ATOM   2469 C  CA  . VAL B 1 40  ? -1.850  -14.038 30.158  1.00 23.47 ? 40  VAL B CA  1 
ATOM   2470 C  C   . VAL B 1 40  ? -0.602  -14.911 30.111  1.00 25.78 ? 40  VAL B C   1 
ATOM   2471 O  O   . VAL B 1 40  ? 0.501   -14.377 30.277  1.00 25.28 ? 40  VAL B O   1 
ATOM   2472 C  CB  . VAL B 1 40  ? -2.122  -13.302 28.835  1.00 21.86 ? 40  VAL B CB  1 
ATOM   2473 C  CG1 . VAL B 1 40  ? -1.811  -14.164 27.600  1.00 24.41 ? 40  VAL B CG1 1 
ATOM   2474 C  CG2 . VAL B 1 40  ? -3.576  -12.824 28.854  1.00 22.20 ? 40  VAL B CG2 1 
ATOM   2475 N  N   . LYS B 1 41  ? -0.798  -16.225 29.901  1.00 20.50 ? 41  LYS B N   1 
ATOM   2476 C  CA  . LYS B 1 41  ? 0.290   -17.207 29.810  1.00 22.71 ? 41  LYS B CA  1 
ATOM   2477 C  C   . LYS B 1 41  ? 0.504   -17.614 28.347  1.00 18.82 ? 41  LYS B C   1 
ATOM   2478 O  O   . LYS B 1 41  ? -0.365  -18.263 27.789  1.00 18.45 ? 41  LYS B O   1 
ATOM   2479 C  CB  . LYS B 1 41  ? -0.124  -18.499 30.590  1.00 25.34 ? 41  LYS B CB  1 
ATOM   2480 C  CG  . LYS B 1 41  ? -0.276  -18.334 32.110  1.00 31.79 ? 41  LYS B CG  1 
ATOM   2481 C  CD  . LYS B 1 41  ? 0.962   -17.724 32.751  1.00 39.59 ? 41  LYS B CD  1 
ATOM   2482 C  CE  . LYS B 1 41  ? 0.719   -16.288 33.202  1.00 45.28 ? 41  LYS B CE  1 
ATOM   2483 N  NZ  . LYS B 1 41  ? 0.296   -16.239 34.618  1.00 46.63 ? 41  LYS B NZ  1 
ATOM   2484 N  N   . TYR B 1 42  ? 1.695   -17.291 27.774  1.00 20.53 ? 42  TYR B N   1 
ATOM   2485 C  CA  . TYR B 1 42  ? 2.071   -17.852 26.447  1.00 21.62 ? 42  TYR B CA  1 
ATOM   2486 C  C   . TYR B 1 42  ? 2.165   -19.390 26.568  1.00 20.67 ? 42  TYR B C   1 
ATOM   2487 O  O   . TYR B 1 42  ? 2.714   -19.884 27.563  1.00 23.00 ? 42  TYR B O   1 
ATOM   2488 C  CB  . TYR B 1 42  ? 3.429   -17.274 25.925  1.00 23.29 ? 42  TYR B CB  1 
ATOM   2489 C  CG  . TYR B 1 42  ? 3.980   -18.057 24.716  1.00 26.39 ? 42  TYR B CG  1 
ATOM   2490 C  CD1 . TYR B 1 42  ? 3.373   -17.991 23.447  1.00 28.98 ? 42  TYR B CD1 1 
ATOM   2491 C  CD2 . TYR B 1 42  ? 5.058   -18.957 24.871  1.00 27.03 ? 42  TYR B CD2 1 
ATOM   2492 C  CE1 . TYR B 1 42  ? 3.812   -18.780 22.363  1.00 28.15 ? 42  TYR B CE1 1 
ATOM   2493 C  CE2 . TYR B 1 42  ? 5.525   -19.732 23.790  1.00 31.21 ? 42  TYR B CE2 1 
ATOM   2494 C  CZ  . TYR B 1 42  ? 4.899   -19.629 22.531  1.00 30.44 ? 42  TYR B CZ  1 
ATOM   2495 O  OH  . TYR B 1 42  ? 5.350   -20.402 21.469  1.00 30.61 ? 42  TYR B OH  1 
ATOM   2496 N  N   . ASP B 1 43  ? 1.612   -20.136 25.603  1.00 17.50 ? 43  ASP B N   1 
ATOM   2497 C  CA  . ASP B 1 43  ? 1.615   -21.588 25.631  1.00 17.54 ? 43  ASP B CA  1 
ATOM   2498 C  C   . ASP B 1 43  ? 2.112   -22.097 24.270  1.00 19.11 ? 43  ASP B C   1 
ATOM   2499 O  O   . ASP B 1 43  ? 1.396   -22.024 23.282  1.00 18.49 ? 43  ASP B O   1 
ATOM   2500 C  CB  . ASP B 1 43  ? 0.204   -22.127 25.928  1.00 19.26 ? 43  ASP B CB  1 
ATOM   2501 C  CG  . ASP B 1 43  ? 0.173   -23.598 26.133  1.00 20.59 ? 43  ASP B CG  1 
ATOM   2502 O  OD1 . ASP B 1 43  ? 1.120   -24.346 25.670  1.00 20.73 ? 43  ASP B OD1 1 
ATOM   2503 O  OD2 . ASP B 1 43  ? -0.813  -24.049 26.758  1.00 20.49 ? 43  ASP B OD2 1 
ATOM   2504 N  N   . SER B 1 44  ? 3.271   -22.722 24.279  1.00 20.60 ? 44  SER B N   1 
ATOM   2505 C  CA  . SER B 1 44  ? 3.901   -23.241 23.031  1.00 21.83 ? 44  SER B CA  1 
ATOM   2506 C  C   . SER B 1 44  ? 3.233   -24.467 22.489  1.00 22.21 ? 44  SER B C   1 
ATOM   2507 O  O   . SER B 1 44  ? 3.428   -24.828 21.293  1.00 26.84 ? 44  SER B O   1 
ATOM   2508 C  CB  . SER B 1 44  ? 5.397   -23.524 23.272  1.00 28.34 ? 44  SER B CB  1 
ATOM   2509 O  OG  . SER B 1 44  ? 5.399   -24.659 24.048  1.00 26.08 ? 44  SER B OG  1 
ATOM   2510 N  N   . SER B 1 45  ? 2.338   -25.086 23.258  1.00 20.10 ? 45  SER B N   1 
ATOM   2511 C  CA  . SER B 1 45  ? 1.531   -26.171 22.777  1.00 21.41 ? 45  SER B CA  1 
ATOM   2512 C  C   . SER B 1 45  ? 0.304   -25.745 21.978  1.00 20.49 ? 45  SER B C   1 
ATOM   2513 O  O   . SER B 1 45  ? -0.332  -26.555 21.337  1.00 22.16 ? 45  SER B O   1 
ATOM   2514 C  CB  . SER B 1 45  ? 1.095   -27.087 23.946  1.00 24.68 ? 45  SER B CB  1 
ATOM   2515 O  OG  . SER B 1 45  ? 0.024   -26.517 24.718  1.00 26.39 ? 45  SER B OG  1 
ATOM   2516 N  N   . LEU B 1 46  ? -0.110  -24.474 22.066  1.00 17.65 ? 46  LEU B N   1 
ATOM   2517 C  CA  . LEU B 1 46  ? -1.160  -24.020 21.195  1.00 17.55 ? 46  LEU B CA  1 
ATOM   2518 C  C   . LEU B 1 46  ? -0.770  -24.030 19.699  1.00 17.00 ? 46  LEU B C   1 
ATOM   2519 O  O   . LEU B 1 46  ? 0.295   -23.540 19.316  1.00 24.12 ? 46  LEU B O   1 
ATOM   2520 C  CB  . LEU B 1 46  ? -1.540  -22.562 21.599  1.00 15.35 ? 46  LEU B CB  1 
ATOM   2521 C  CG  . LEU B 1 46  ? -2.338  -22.508 22.912  1.00 15.02 ? 46  LEU B CG  1 
ATOM   2522 C  CD1 . LEU B 1 46  ? -2.459  -21.021 23.305  1.00 15.60 ? 46  LEU B CD1 1 
ATOM   2523 C  CD2 . LEU B 1 46  ? -3.732  -23.101 22.741  1.00 15.81 ? 46  LEU B CD2 1 
ATOM   2524 N  N   . ARG B 1 47  ? -1.704  -24.459 18.904  1.00 17.26 ? 47  ARG B N   1 
ATOM   2525 C  CA  . ARG B 1 47  ? -1.487  -24.562 17.432  1.00 18.35 ? 47  ARG B CA  1 
ATOM   2526 C  C   . ARG B 1 47  ? -2.008  -23.294 16.771  1.00 15.44 ? 47  ARG B C   1 
ATOM   2527 O  O   . ARG B 1 47  ? -2.910  -22.582 17.272  1.00 14.47 ? 47  ARG B O   1 
ATOM   2528 C  CB  . ARG B 1 47  ? -2.154  -25.856 16.860  1.00 19.55 ? 47  ARG B CB  1 
ATOM   2529 C  CG  . ARG B 1 47  ? -1.448  -27.107 17.428  1.00 23.82 ? 47  ARG B CG  1 
ATOM   2530 C  CD  . ARG B 1 47  ? 0.037   -27.378 16.934  1.00 29.23 ? 47  ARG B CD  1 
ATOM   2531 N  NE  . ARG B 1 47  ? 1.025   -26.242 16.897  1.00 31.66 ? 47  ARG B NE  1 
ATOM   2532 C  CZ  . ARG B 1 47  ? 2.062   -26.021 17.718  1.00 32.97 ? 47  ARG B CZ  1 
ATOM   2533 N  NH1 . ARG B 1 47  ? 2.373   -26.843 18.723  1.00 42.37 ? 47  ARG B NH1 1 
ATOM   2534 N  NH2 . ARG B 1 47  ? 2.797   -24.936 17.549  1.00 40.08 ? 47  ARG B NH2 1 
ATOM   2535 N  N   . PRO B 1 48  ? -1.518  -22.989 15.587  1.00 15.56 ? 48  PRO B N   1 
ATOM   2536 C  CA  . PRO B 1 48  ? -2.118  -21.920 14.791  1.00 15.09 ? 48  PRO B CA  1 
ATOM   2537 C  C   . PRO B 1 48  ? -3.516  -22.248 14.370  1.00 13.87 ? 48  PRO B C   1 
ATOM   2538 O  O   . PRO B 1 48  ? -3.882  -23.476 14.260  1.00 14.60 ? 48  PRO B O   1 
ATOM   2539 C  CB  . PRO B 1 48  ? -1.142  -21.833 13.553  1.00 15.13 ? 48  PRO B CB  1 
ATOM   2540 C  CG  . PRO B 1 48  ? -0.457  -23.116 13.570  1.00 18.19 ? 48  PRO B CG  1 
ATOM   2541 C  CD  . PRO B 1 48  ? -0.317  -23.576 14.974  1.00 16.40 ? 48  PRO B CD  1 
ATOM   2542 N  N   . LEU B 1 49  ? -4.379  -21.256 14.154  1.00 14.40 ? 49  LEU B N   1 
ATOM   2543 C  CA  . LEU B 1 49  ? -5.722  -21.478 13.699  1.00 16.29 ? 49  LEU B CA  1 
ATOM   2544 C  C   . LEU B 1 49  ? -5.658  -21.957 12.252  1.00 15.99 ? 49  LEU B C   1 
ATOM   2545 O  O   . LEU B 1 49  ? -4.874  -21.380 11.459  1.00 19.09 ? 49  LEU B O   1 
ATOM   2546 C  CB  . LEU B 1 49  ? -6.667  -20.247 13.805  1.00 14.50 ? 49  LEU B CB  1 
ATOM   2547 C  CG  . LEU B 1 49  ? -6.683  -19.676 15.218  1.00 14.45 ? 49  LEU B CG  1 
ATOM   2548 C  CD1 . LEU B 1 49  ? -7.580  -18.399 15.183  1.00 13.12 ? 49  LEU B CD1 1 
ATOM   2549 C  CD2 . LEU B 1 49  ? -7.280  -20.743 16.140  1.00 14.96 ? 49  LEU B CD2 1 
ATOM   2550 N  N   . SER B 1 50  ? -6.397  -23.006 11.933  1.00 14.81 ? 50  SER B N   1 
ATOM   2551 C  CA  . SER B 1 50  ? -6.612  -23.372 10.519  1.00 18.40 ? 50  SER B CA  1 
ATOM   2552 C  C   . SER B 1 50  ? -8.072  -23.172 10.209  1.00 19.97 ? 50  SER B C   1 
ATOM   2553 O  O   . SER B 1 50  ? -8.970  -23.709 10.916  1.00 18.32 ? 50  SER B O   1 
ATOM   2554 C  CB  . SER B 1 50  ? -6.039  -24.786 10.216  1.00 21.00 ? 50  SER B CB  1 
ATOM   2555 O  OG  . SER B 1 50  ? -6.779  -25.797 10.758  1.00 28.33 ? 50  SER B OG  1 
ATOM   2556 N  N   . ILE B 1 51  ? -8.380  -22.261 9.277   1.00 20.49 ? 51  ILE B N   1 
ATOM   2557 C  CA  . ILE B 1 51  ? -9.753  -21.738 9.053   1.00 23.95 ? 51  ILE B CA  1 
ATOM   2558 C  C   . ILE B 1 51  ? -10.052 -21.800 7.643   1.00 31.21 ? 51  ILE B C   1 
ATOM   2559 O  O   . ILE B 1 51  ? -9.253  -21.354 6.763   1.00 29.23 ? 51  ILE B O   1 
ATOM   2560 C  CB  . ILE B 1 51  ? -9.947  -20.284 9.462   1.00 25.93 ? 51  ILE B CB  1 
ATOM   2561 C  CG1 . ILE B 1 51  ? -9.500  -20.072 10.880  1.00 30.17 ? 51  ILE B CG1 1 
ATOM   2562 C  CG2 . ILE B 1 51  ? -11.391 -19.860 9.383   1.00 30.00 ? 51  ILE B CG2 1 
ATOM   2563 C  CD1 . ILE B 1 51  ? -9.419  -18.605 11.315  1.00 31.35 ? 51  ILE B CD1 1 
ATOM   2564 N  N   . LYS B 1 52  ? -11.191 -22.401 7.406   1.00 28.20 ? 52  LYS B N   1 
ATOM   2565 C  CA  . LYS B 1 52  ? -11.589 -22.760 6.105   1.00 30.30 ? 52  LYS B CA  1 
ATOM   2566 C  C   . LYS B 1 52  ? -13.032 -22.439 6.042   1.00 27.34 ? 52  LYS B C   1 
ATOM   2567 O  O   . LYS B 1 52  ? -13.824 -22.989 6.781   1.00 20.25 ? 52  LYS B O   1 
ATOM   2568 C  CB  . LYS B 1 52  ? -11.314 -24.252 6.011   1.00 31.96 ? 52  LYS B CB  1 
ATOM   2569 C  CG  . LYS B 1 52  ? -11.985 -24.944 4.895   1.00 33.86 ? 52  LYS B CG  1 
ATOM   2570 C  CD  . LYS B 1 52  ? -11.472 -26.360 4.839   1.00 36.12 ? 52  LYS B CD  1 
ATOM   2571 C  CE  . LYS B 1 52  ? -12.617 -27.252 4.421   1.00 38.43 ? 52  LYS B CE  1 
ATOM   2572 N  NZ  . LYS B 1 52  ? -12.143 -28.650 4.587   1.00 44.57 ? 52  LYS B NZ  1 
ATOM   2573 N  N   A TYR B 1 53  ? -13.460 -21.301 5.407   0.50 24.28 ? 53  TYR B N   1 
ATOM   2574 N  N   B TYR B 1 53  ? -13.293 -21.926 4.880   0.50 28.98 ? 53  TYR B N   1 
ATOM   2575 C  CA  A TYR B 1 53  ? -14.908 -20.900 5.241   0.50 23.62 ? 53  TYR B CA  1 
ATOM   2576 C  CA  B TYR B 1 53  ? -14.486 -21.325 4.733   0.50 25.49 ? 53  TYR B CA  1 
ATOM   2577 C  C   A TYR B 1 53  ? -15.350 -20.662 3.771   0.50 24.19 ? 53  TYR B C   1 
ATOM   2578 C  C   B TYR B 1 53  ? -14.868 -21.516 3.332   0.50 28.52 ? 53  TYR B C   1 
ATOM   2579 O  O   A TYR B 1 53  ? -14.914 -19.640 3.196   0.50 28.16 ? 53  TYR B O   1 
ATOM   2580 O  O   B TYR B 1 53  ? -14.067 -21.636 2.403   0.50 24.67 ? 53  TYR B O   1 
ATOM   2581 C  CB  A TYR B 1 53  ? -15.314 -19.626 6.048   0.50 21.01 ? 53  TYR B CB  1 
ATOM   2582 C  CB  B TYR B 1 53  ? -14.343 -19.895 5.069   0.50 25.02 ? 53  TYR B CB  1 
ATOM   2583 C  CG  A TYR B 1 53  ? -15.031 -19.600 7.545   0.50 18.07 ? 53  TYR B CG  1 
ATOM   2584 C  CG  B TYR B 1 53  ? -15.628 -19.227 4.889   0.50 22.75 ? 53  TYR B CG  1 
ATOM   2585 C  CD1 A TYR B 1 53  ? -15.279 -20.729 8.362   0.50 18.93 ? 53  TYR B CD1 1 
ATOM   2586 C  CD1 B TYR B 1 53  ? -16.717 -19.527 5.725   0.50 19.15 ? 53  TYR B CD1 1 
ATOM   2587 C  CD2 A TYR B 1 53  ? -14.498 -18.439 8.147   0.50 18.53 ? 53  TYR B CD2 1 
ATOM   2588 C  CD2 B TYR B 1 53  ? -15.802 -18.330 3.858   0.50 20.85 ? 53  TYR B CD2 1 
ATOM   2589 C  CE1 A TYR B 1 53  ? -14.977 -20.675 9.715   0.50 18.06 ? 53  TYR B CE1 1 
ATOM   2590 C  CE1 B TYR B 1 53  ? -17.918 -18.925 5.547   0.50 19.32 ? 53  TYR B CE1 1 
ATOM   2591 C  CE2 A TYR B 1 53  ? -14.252 -18.384 9.501   0.50 18.93 ? 53  TYR B CE2 1 
ATOM   2592 C  CE2 B TYR B 1 53  ? -16.977 -17.707 3.687   0.50 20.37 ? 53  TYR B CE2 1 
ATOM   2593 C  CZ  A TYR B 1 53  ? -14.493 -19.529 10.274  0.50 18.37 ? 53  TYR B CZ  1 
ATOM   2594 C  CZ  B TYR B 1 53  ? -18.047 -17.983 4.531   0.50 18.59 ? 53  TYR B CZ  1 
ATOM   2595 O  OH  A TYR B 1 53  ? -14.204 -19.498 11.588  0.50 17.73 ? 53  TYR B OH  1 
ATOM   2596 O  OH  B TYR B 1 53  ? -19.215 -17.367 4.293   0.50 19.75 ? 53  TYR B OH  1 
ATOM   2597 N  N   . ASP B 1 54  ? -16.147 -21.601 3.189   1.00 24.22 ? 54  ASP B N   1 
ATOM   2598 C  CA  . ASP B 1 54  ? -16.671 -21.649 1.841   1.00 27.70 ? 54  ASP B CA  1 
ATOM   2599 C  C   . ASP B 1 54  ? -17.761 -20.589 1.765   1.00 26.40 ? 54  ASP B C   1 
ATOM   2600 O  O   . ASP B 1 54  ? -18.795 -20.702 2.431   1.00 26.49 ? 54  ASP B O   1 
ATOM   2601 C  CB  . ASP B 1 54  ? -17.171 -23.071 1.523   1.00 30.66 ? 54  ASP B CB  1 
ATOM   2602 C  CG  . ASP B 1 54  ? -17.841 -23.180 0.164   1.00 37.70 ? 54  ASP B CG  1 
ATOM   2603 O  OD1 . ASP B 1 54  ? -17.887 -22.177 -0.571  1.00 33.41 ? 54  ASP B OD1 1 
ATOM   2604 O  OD2 . ASP B 1 54  ? -18.343 -24.272 -0.163  1.00 42.95 ? 54  ASP B OD2 1 
ATOM   2605 N  N   . PRO B 1 55  ? -17.515 -19.513 0.966   1.00 24.39 ? 55  PRO B N   1 
ATOM   2606 C  CA  . PRO B 1 55  ? -18.437 -18.406 0.877   1.00 24.61 ? 55  PRO B CA  1 
ATOM   2607 C  C   . PRO B 1 55  ? -19.831 -18.855 0.450   1.00 23.03 ? 55  PRO B C   1 
ATOM   2608 O  O   . PRO B 1 55  ? -20.819 -18.181 0.797   1.00 24.86 ? 55  PRO B O   1 
ATOM   2609 C  CB  . PRO B 1 55  ? -17.747 -17.437 -0.088  1.00 21.62 ? 55  PRO B CB  1 
ATOM   2610 C  CG  . PRO B 1 55  ? -16.296 -17.793 -0.109  1.00 25.02 ? 55  PRO B CG  1 
ATOM   2611 C  CD  . PRO B 1 55  ? -16.318 -19.313 0.103   1.00 21.16 ? 55  PRO B CD  1 
ATOM   2612 N  N   . SER B 1 56  ? -19.972 -20.039 -0.164  1.00 26.11 ? 56  SER B N   1 
ATOM   2613 C  CA  . SER B 1 56  ? -21.305 -20.493 -0.569  1.00 24.58 ? 56  SER B CA  1 
ATOM   2614 C  C   . SER B 1 56  ? -22.042 -21.208 0.591   1.00 25.48 ? 56  SER B C   1 
ATOM   2615 O  O   . SER B 1 56  ? -23.231 -21.515 0.451   1.00 26.26 ? 56  SER B O   1 
ATOM   2616 C  CB  . SER B 1 56  ? -21.156 -21.464 -1.750  1.00 31.08 ? 56  SER B CB  1 
ATOM   2617 O  OG  . SER B 1 56  ? -20.605 -22.679 -1.257  1.00 35.97 ? 56  SER B OG  1 
ATOM   2618 N  N   . SER B 1 57  ? -21.327 -21.463 1.742   1.00 20.55 ? 57  SER B N   1 
ATOM   2619 C  CA  . SER B 1 57  ? -21.880 -22.044 2.964   1.00 21.57 ? 57  SER B CA  1 
ATOM   2620 C  C   . SER B 1 57  ? -22.940 -21.152 3.554   1.00 21.96 ? 57  SER B C   1 
ATOM   2621 O  O   . SER B 1 57  ? -23.874 -21.643 4.217   1.00 19.44 ? 57  SER B O   1 
ATOM   2622 C  CB  . SER B 1 57  ? -20.738 -22.124 4.054   1.00 24.64 ? 57  SER B CB  1 
ATOM   2623 O  OG  . SER B 1 57  ? -19.902 -23.205 3.751   1.00 31.43 ? 57  SER B OG  1 
ATOM   2624 N  N   . ALA B 1 58  ? -22.789 -19.841 3.401   1.00 22.29 ? 58  ALA B N   1 
ATOM   2625 C  CA  . ALA B 1 58  ? -23.734 -18.902 4.044   1.00 23.60 ? 58  ALA B CA  1 
ATOM   2626 C  C   . ALA B 1 58  ? -25.097 -19.068 3.369   1.00 23.40 ? 58  ALA B C   1 
ATOM   2627 O  O   . ALA B 1 58  ? -25.156 -19.234 2.147   1.00 24.99 ? 58  ALA B O   1 
ATOM   2628 C  CB  . ALA B 1 58  ? -23.207 -17.439 3.943   1.00 19.66 ? 58  ALA B CB  1 
ATOM   2629 N  N   . LYS B 1 59  ? -26.161 -19.023 4.167   1.00 20.22 ? 59  LYS B N   1 
ATOM   2630 C  CA  . LYS B 1 59  ? -27.531 -19.202 3.625   1.00 19.97 ? 59  LYS B CA  1 
ATOM   2631 C  C   . LYS B 1 59  ? -28.464 -17.998 3.859   1.00 19.67 ? 59  LYS B C   1 
ATOM   2632 O  O   . LYS B 1 59  ? -29.187 -17.561 2.960   1.00 21.33 ? 59  LYS B O   1 
ATOM   2633 C  CB  . LYS B 1 59  ? -28.220 -20.472 4.152   1.00 23.74 ? 59  LYS B CB  1 
ATOM   2634 C  CG  . LYS B 1 59  ? -27.589 -21.775 3.669   1.00 33.82 ? 59  LYS B CG  1 
ATOM   2635 C  CD  . LYS B 1 59  ? -28.053 -22.295 2.267   1.00 34.49 ? 59  LYS B CD  1 
ATOM   2636 C  CE  . LYS B 1 59  ? -27.340 -21.707 1.024   1.00 36.84 ? 59  LYS B CE  1 
ATOM   2637 N  NZ  . LYS B 1 59  ? -26.193 -22.445 0.386   1.00 36.93 ? 59  LYS B NZ  1 
ATOM   2638 N  N   A ILE B 1 60  ? -28.504 -17.477 5.079   0.50 18.84 ? 60  ILE B N   1 
ATOM   2639 N  N   B ILE B 1 60  ? -28.445 -17.459 5.079   0.50 19.06 ? 60  ILE B N   1 
ATOM   2640 C  CA  A ILE B 1 60  ? -29.469 -16.409 5.349   0.50 18.42 ? 60  ILE B CA  1 
ATOM   2641 C  CA  B ILE B 1 60  ? -29.539 -16.576 5.515   0.50 18.90 ? 60  ILE B CA  1 
ATOM   2642 C  C   A ILE B 1 60  ? -28.916 -15.521 6.406   0.50 15.17 ? 60  ILE B C   1 
ATOM   2643 C  C   B ILE B 1 60  ? -28.998 -15.595 6.515   0.50 15.64 ? 60  ILE B C   1 
ATOM   2644 O  O   A ILE B 1 60  ? -27.921 -15.852 7.134   0.50 17.72 ? 60  ILE B O   1 
ATOM   2645 O  O   B ILE B 1 60  ? -28.046 -15.933 7.308   0.50 17.52 ? 60  ILE B O   1 
ATOM   2646 C  CB  A ILE B 1 60  ? -30.907 -16.807 5.824   0.50 17.39 ? 60  ILE B CB  1 
ATOM   2647 C  CB  B ILE B 1 60  ? -30.720 -17.315 6.194   0.50 18.54 ? 60  ILE B CB  1 
ATOM   2648 C  CG1 A ILE B 1 60  ? -30.899 -17.725 7.058   0.50 16.03 ? 60  ILE B CG1 1 
ATOM   2649 C  CG1 B ILE B 1 60  ? -30.225 -18.149 7.395   0.50 22.50 ? 60  ILE B CG1 1 
ATOM   2650 C  CG2 A ILE B 1 60  ? -31.830 -17.131 4.630   0.50 16.28 ? 60  ILE B CG2 1 
ATOM   2651 C  CG2 B ILE B 1 60  ? -31.526 -18.100 5.159   0.50 20.76 ? 60  ILE B CG2 1 
ATOM   2652 C  CD1 A ILE B 1 60  ? -30.222 -17.110 8.311   0.50 14.14 ? 60  ILE B CD1 1 
ATOM   2653 C  CD1 B ILE B 1 60  ? -30.999 -19.405 7.680   0.50 19.53 ? 60  ILE B CD1 1 
ATOM   2654 N  N   . ILE B 1 61  ? -29.606 -14.411 6.521   1.00 18.63 ? 61  ILE B N   1 
ATOM   2655 C  CA  . ILE B 1 61  ? -29.408 -13.452 7.645   1.00 16.72 ? 61  ILE B CA  1 
ATOM   2656 C  C   . ILE B 1 61  ? -30.767 -13.110 8.300   1.00 16.07 ? 61  ILE B C   1 
ATOM   2657 O  O   . ILE B 1 61  ? -31.780 -12.871 7.634   1.00 13.98 ? 61  ILE B O   1 
ATOM   2658 C  CB  . ILE B 1 61  ? -28.655 -12.158 7.216   1.00 15.92 ? 61  ILE B CB  1 
ATOM   2659 C  CG1 . ILE B 1 61  ? -28.141 -11.401 8.492   1.00 14.83 ? 61  ILE B CG1 1 
ATOM   2660 C  CG2 . ILE B 1 61  ? -29.508 -11.313 6.351   1.00 15.70 ? 61  ILE B CG2 1 
ATOM   2661 C  CD1 . ILE B 1 61  ? -27.252 -10.155 8.174   1.00 13.82 ? 61  ILE B CD1 1 
ATOM   2662 N  N   . SER B 1 62  ? -30.777 -13.092 9.617   1.00 15.18 ? 62  SER B N   1 
ATOM   2663 C  CA  . SER B 1 62  ? -32.021 -12.782 10.308  1.00 16.10 ? 62  SER B CA  1 
ATOM   2664 C  C   . SER B 1 62  ? -31.828 -11.921 11.532  1.00 15.57 ? 62  SER B C   1 
ATOM   2665 O  O   . SER B 1 62  ? -30.739 -11.819 12.047  1.00 16.48 ? 62  SER B O   1 
ATOM   2666 C  CB  . SER B 1 62  ? -32.758 -14.073 10.681  1.00 23.74 ? 62  SER B CB  1 
ATOM   2667 O  OG  . SER B 1 62  ? -32.414 -14.499 11.988  1.00 21.41 ? 62  SER B OG  1 
ATOM   2668 N  N   . ASN B 1 63  ? -32.933 -11.320 11.972  1.00 17.06 ? 63  ASN B N   1 
ATOM   2669 C  CA  . ASN B 1 63  ? -32.907 -10.567 13.260  1.00 15.89 ? 63  ASN B CA  1 
ATOM   2670 C  C   . ASN B 1 63  ? -33.555 -11.451 14.344  1.00 15.91 ? 63  ASN B C   1 
ATOM   2671 O  O   . ASN B 1 63  ? -34.746 -11.783 14.315  1.00 16.21 ? 63  ASN B O   1 
ATOM   2672 C  CB  . ASN B 1 63  ? -33.738 -9.330  13.055  1.00 14.76 ? 63  ASN B CB  1 
ATOM   2673 C  CG  . ASN B 1 63  ? -33.872 -8.505  14.341  1.00 14.72 ? 63  ASN B CG  1 
ATOM   2674 O  OD1 . ASN B 1 63  ? -33.236 -8.840  15.370  1.00 14.92 ? 63  ASN B OD1 1 
ATOM   2675 N  ND2 . ASN B 1 63  ? -34.514 -7.338  14.218  1.00 13.39 ? 63  ASN B ND2 1 
ATOM   2676 N  N   . SER B 1 64  ? -32.757 -11.879 15.283  1.00 13.79 ? 64  SER B N   1 
ATOM   2677 C  CA  . SER B 1 64  ? -33.235 -12.732 16.392  1.00 14.02 ? 64  SER B CA  1 
ATOM   2678 C  C   . SER B 1 64  ? -33.893 -11.902 17.469  1.00 14.32 ? 64  SER B C   1 
ATOM   2679 O  O   . SER B 1 64  ? -34.434 -12.438 18.388  1.00 18.84 ? 64  SER B O   1 
ATOM   2680 C  CB  . SER B 1 64  ? -32.063 -13.451 17.097  1.00 14.79 ? 64  SER B CB  1 
ATOM   2681 O  OG  . SER B 1 64  ? -31.145 -12.512 17.679  1.00 15.37 ? 64  SER B OG  1 
ATOM   2682 N  N   . GLY B 1 65  ? -33.743 -10.593 17.370  1.00 14.63 ? 65  GLY B N   1 
ATOM   2683 C  CA  . GLY B 1 65  ? -34.198 -9.679  18.449  1.00 14.57 ? 65  GLY B CA  1 
ATOM   2684 C  C   . GLY B 1 65  ? -33.051 -9.391  19.440  1.00 13.22 ? 65  GLY B C   1 
ATOM   2685 O  O   . GLY B 1 65  ? -33.136 -8.461  20.255  1.00 15.88 ? 65  GLY B O   1 
ATOM   2686 N  N   . HIS B 1 66  ? -31.943 -10.149 19.315  1.00 13.31 ? 66  HIS B N   1 
ATOM   2687 C  CA  . HIS B 1 66  ? -30.739 -9.933  20.154  1.00 13.40 ? 66  HIS B CA  1 
ATOM   2688 C  C   . HIS B 1 66  ? -29.482 -9.511  19.467  1.00 13.57 ? 66  HIS B C   1 
ATOM   2689 O  O   . HIS B 1 66  ? -28.491 -9.083  20.095  1.00 14.55 ? 66  HIS B O   1 
ATOM   2690 C  CB  . HIS B 1 66  ? -30.464 -11.250 20.933  1.00 13.63 ? 66  HIS B CB  1 
ATOM   2691 C  CG  . HIS B 1 66  ? -31.726 -11.819 21.606  1.00 15.87 ? 66  HIS B CG  1 
ATOM   2692 N  ND1 . HIS B 1 66  ? -32.413 -11.184 22.619  1.00 16.91 ? 66  HIS B ND1 1 
ATOM   2693 C  CD2 . HIS B 1 66  ? -32.417 -12.985 21.343  1.00 14.78 ? 66  HIS B CD2 1 
ATOM   2694 C  CE1 . HIS B 1 66  ? -33.476 -11.943 23.013  1.00 16.79 ? 66  HIS B CE1 1 
ATOM   2695 N  NE2 . HIS B 1 66  ? -33.517 -13.029 22.248  1.00 16.85 ? 66  HIS B NE2 1 
ATOM   2696 N  N   . SER B 1 67  ? -29.530 -9.719  18.162  1.00 12.28 ? 67  SER B N   1 
ATOM   2697 C  CA  . SER B 1 67  ? -28.480 -9.410  17.184  1.00 11.31 ? 67  SER B CA  1 
ATOM   2698 C  C   . SER B 1 67  ? -29.004 -9.734  15.808  1.00 12.47 ? 67  SER B C   1 
ATOM   2699 O  O   . SER B 1 67  ? -30.171 -10.120 15.711  1.00 14.35 ? 67  SER B O   1 
ATOM   2700 C  CB  . SER B 1 67  ? -27.179 -10.228 17.558  1.00 11.42 ? 67  SER B CB  1 
ATOM   2701 O  OG  . SER B 1 67  ? -26.052 -9.790  16.751  1.00 12.92 ? 67  SER B OG  1 
ATOM   2702 N  N   . PHE B 1 68  ? -28.150 -9.576  14.762  1.00 12.87 ? 68  PHE B N   1 
ATOM   2703 C  CA  . PHE B 1 68  ? -28.446 -10.324 13.512  1.00 13.69 ? 68  PHE B CA  1 
ATOM   2704 C  C   . PHE B 1 68  ? -27.712 -11.642 13.633  1.00 15.37 ? 68  PHE B C   1 
ATOM   2705 O  O   . PHE B 1 68  ? -26.645 -11.713 14.336  1.00 15.01 ? 68  PHE B O   1 
ATOM   2706 C  CB  . PHE B 1 68  ? -27.963 -9.506  12.295  1.00 14.65 ? 68  PHE B CB  1 
ATOM   2707 C  CG  . PHE B 1 68  ? -26.505 -9.485  12.127  1.00 13.68 ? 68  PHE B CG  1 
ATOM   2708 C  CD1 . PHE B 1 68  ? -25.752 -8.401  12.607  1.00 14.97 ? 68  PHE B CD1 1 
ATOM   2709 C  CD2 . PHE B 1 68  ? -25.780 -10.586 11.549  1.00 14.18 ? 68  PHE B CD2 1 
ATOM   2710 C  CE1 . PHE B 1 68  ? -24.364 -8.373  12.455  1.00 14.83 ? 68  PHE B CE1 1 
ATOM   2711 C  CE2 . PHE B 1 68  ? -24.385 -10.547 11.397  1.00 15.90 ? 68  PHE B CE2 1 
ATOM   2712 C  CZ  . PHE B 1 68  ? -23.652 -9.439  11.879  1.00 13.90 ? 68  PHE B CZ  1 
ATOM   2713 N  N   A ASN B 1 69  ? -28.126 -12.649 12.869  0.50 14.90 ? 69  ASN B N   1 
ATOM   2714 N  N   B ASN B 1 69  ? -28.189 -12.673 12.895  0.50 13.93 ? 69  ASN B N   1 
ATOM   2715 C  CA  A ASN B 1 69  ? -27.340 -13.881 12.757  0.50 14.44 ? 69  ASN B CA  1 
ATOM   2716 C  CA  B ASN B 1 69  ? -27.300 -13.843 12.695  0.50 13.49 ? 69  ASN B CA  1 
ATOM   2717 C  C   A ASN B 1 69  ? -27.275 -14.457 11.334  0.50 12.89 ? 69  ASN B C   1 
ATOM   2718 C  C   B ASN B 1 69  ? -27.292 -14.262 11.225  0.50 11.94 ? 69  ASN B C   1 
ATOM   2719 O  O   A ASN B 1 69  ? -28.311 -14.766 10.746  0.50 14.45 ? 69  ASN B O   1 
ATOM   2720 O  O   B ASN B 1 69  ? -28.360 -14.169 10.521  0.50 12.82 ? 69  ASN B O   1 
ATOM   2721 C  CB  A ASN B 1 69  ? -27.868 -14.942 13.727  0.50 18.14 ? 69  ASN B CB  1 
ATOM   2722 C  CB  B ASN B 1 69  ? -27.657 -15.075 13.552  0.50 14.63 ? 69  ASN B CB  1 
ATOM   2723 C  CG  A ASN B 1 69  ? -28.852 -14.374 14.731  0.50 17.73 ? 69  ASN B CG  1 
ATOM   2724 C  CG  B ASN B 1 69  ? -29.075 -15.417 13.467  0.50 12.79 ? 69  ASN B CG  1 
ATOM   2725 O  OD1 A ASN B 1 69  ? -29.968 -14.874 14.875  0.50 21.82 ? 69  ASN B OD1 1 
ATOM   2726 O  OD1 B ASN B 1 69  ? -29.450 -16.548 13.022  0.50 17.22 ? 69  ASN B OD1 1 
ATOM   2727 N  ND2 A ASN B 1 69  ? -28.442 -13.324 15.432  0.50 15.12 ? 69  ASN B ND2 1 
ATOM   2728 N  ND2 B ASN B 1 69  ? -29.895 -14.557 13.954  0.50 12.48 ? 69  ASN B ND2 1 
ATOM   2729 N  N   . VAL B 1 70  ? -26.068 -14.610 10.783  1.00 13.74 ? 70  VAL B N   1 
ATOM   2730 C  CA  . VAL B 1 70  ? -25.926 -15.246 9.455   1.00 13.34 ? 70  VAL B CA  1 
ATOM   2731 C  C   . VAL B 1 70  ? -25.815 -16.749 9.861   1.00 12.04 ? 70  VAL B C   1 
ATOM   2732 O  O   . VAL B 1 70  ? -24.915 -17.084 10.585  1.00 13.15 ? 70  VAL B O   1 
ATOM   2733 C  CB  . VAL B 1 70  ? -24.688 -14.769 8.738   1.00 15.92 ? 70  VAL B CB  1 
ATOM   2734 C  CG1 . VAL B 1 70  ? -24.451 -15.514 7.409   1.00 15.95 ? 70  VAL B CG1 1 
ATOM   2735 C  CG2 . VAL B 1 70  ? -24.740 -13.250 8.441   1.00 16.65 ? 70  VAL B CG2 1 
ATOM   2736 N  N   . ASP B 1 71  ? -26.726 -17.574 9.310   1.00 13.85 ? 71  ASP B N   1 
ATOM   2737 C  CA  . ASP B 1 71  ? -26.692 -19.037 9.544   1.00 15.73 ? 71  ASP B CA  1 
ATOM   2738 C  C   . ASP B 1 71  ? -26.010 -19.714 8.314   1.00 17.66 ? 71  ASP B C   1 
ATOM   2739 O  O   . ASP B 1 71  ? -26.094 -19.227 7.139   1.00 18.23 ? 71  ASP B O   1 
ATOM   2740 C  CB  . ASP B 1 71  ? -28.078 -19.622 9.771   1.00 19.08 ? 71  ASP B CB  1 
ATOM   2741 C  CG  . ASP B 1 71  ? -28.670 -19.221 11.106  1.00 23.13 ? 71  ASP B CG  1 
ATOM   2742 O  OD1 . ASP B 1 71  ? -27.906 -18.815 12.007  1.00 23.07 ? 71  ASP B OD1 1 
ATOM   2743 O  OD2 . ASP B 1 71  ? -29.909 -19.303 11.243  1.00 31.15 ? 71  ASP B OD2 1 
ATOM   2744 N  N   . PHE B 1 72  ? -25.316 -20.802 8.605   1.00 15.84 ? 72  PHE B N   1 
ATOM   2745 C  CA  . PHE B 1 72  ? -24.529 -21.529 7.557   1.00 14.93 ? 72  PHE B CA  1 
ATOM   2746 C  C   . PHE B 1 72  ? -25.050 -22.955 7.494   1.00 15.17 ? 72  PHE B C   1 
ATOM   2747 O  O   . PHE B 1 72  ? -25.448 -23.552 8.505   1.00 14.44 ? 72  PHE B O   1 
ATOM   2748 C  CB  . PHE B 1 72  ? -23.091 -21.544 7.900   1.00 16.09 ? 72  PHE B CB  1 
ATOM   2749 C  CG  . PHE B 1 72  ? -22.459 -20.150 7.864   1.00 17.21 ? 72  PHE B CG  1 
ATOM   2750 C  CD1 . PHE B 1 72  ? -22.693 -19.250 8.909   1.00 19.01 ? 72  PHE B CD1 1 
ATOM   2751 C  CD2 . PHE B 1 72  ? -21.748 -19.720 6.769   1.00 18.38 ? 72  PHE B CD2 1 
ATOM   2752 C  CE1 . PHE B 1 72  ? -22.114 -17.969 8.903   1.00 18.71 ? 72  PHE B CE1 1 
ATOM   2753 C  CE2 . PHE B 1 72  ? -21.196 -18.437 6.721   1.00 19.52 ? 72  PHE B CE2 1 
ATOM   2754 C  CZ  . PHE B 1 72  ? -21.397 -17.561 7.789   1.00 18.65 ? 72  PHE B CZ  1 
ATOM   2755 N  N   . ASP B 1 73  ? -24.988 -23.480 6.262   1.00 18.74 ? 73  ASP B N   1 
ATOM   2756 C  CA  . ASP B 1 73  ? -25.202 -24.906 6.096   1.00 19.35 ? 73  ASP B CA  1 
ATOM   2757 C  C   . ASP B 1 73  ? -24.155 -25.607 6.851   1.00 15.48 ? 73  ASP B C   1 
ATOM   2758 O  O   . ASP B 1 73  ? -22.981 -25.331 6.673   1.00 18.58 ? 73  ASP B O   1 
ATOM   2759 C  CB  . ASP B 1 73  ? -24.939 -25.320 4.614   1.00 24.31 ? 73  ASP B CB  1 
ATOM   2760 C  CG  . ASP B 1 73  ? -26.115 -25.050 3.723   1.00 34.98 ? 73  ASP B CG  1 
ATOM   2761 O  OD1 . ASP B 1 73  ? -27.278 -25.050 4.260   1.00 40.45 ? 73  ASP B OD1 1 
ATOM   2762 O  OD2 . ASP B 1 73  ? -25.855 -24.818 2.490   1.00 38.71 ? 73  ASP B OD2 1 
ATOM   2763 N  N   . ASP B 1 74  ? -24.543 -26.659 7.582   1.00 18.34 ? 74  ASP B N   1 
ATOM   2764 C  CA  . ASP B 1 74  ? -23.531 -27.271 8.508   1.00 15.75 ? 74  ASP B CA  1 
ATOM   2765 C  C   . ASP B 1 74  ? -23.762 -28.812 8.522   1.00 16.20 ? 74  ASP B C   1 
ATOM   2766 O  O   . ASP B 1 74  ? -23.802 -29.462 9.599   1.00 17.56 ? 74  ASP B O   1 
ATOM   2767 C  CB  . ASP B 1 74  ? -23.603 -26.731 9.922   1.00 17.27 ? 74  ASP B CB  1 
ATOM   2768 C  CG  . ASP B 1 74  ? -24.946 -27.022 10.639  1.00 17.20 ? 74  ASP B CG  1 
ATOM   2769 O  OD1 . ASP B 1 74  ? -26.000 -27.345 10.016  1.00 18.74 ? 74  ASP B OD1 1 
ATOM   2770 O  OD2 . ASP B 1 74  ? -24.963 -26.912 11.885  1.00 17.44 ? 74  ASP B OD2 1 
ATOM   2771 N  N   . THR B 1 75  ? -23.989 -29.360 7.327   1.00 16.71 ? 75  THR B N   1 
ATOM   2772 C  CA  . THR B 1 75  ? -24.132 -30.856 7.170   1.00 15.50 ? 75  THR B CA  1 
ATOM   2773 C  C   . THR B 1 75  ? -22.845 -31.488 6.686   1.00 18.40 ? 75  THR B C   1 
ATOM   2774 O  O   . THR B 1 75  ? -22.726 -32.735 6.653   1.00 17.07 ? 75  THR B O   1 
ATOM   2775 C  CB  . THR B 1 75  ? -25.254 -31.225 6.155   1.00 18.63 ? 75  THR B CB  1 
ATOM   2776 O  OG1 . THR B 1 75  ? -24.938 -30.682 4.867   1.00 21.10 ? 75  THR B OG1 1 
ATOM   2777 C  CG2 . THR B 1 75  ? -26.576 -30.708 6.597   1.00 21.61 ? 75  THR B CG2 1 
ATOM   2778 N  N   . GLU B 1 76  ? -21.867 -30.702 6.231   1.00 16.71 ? 76  GLU B N   1 
ATOM   2779 C  CA  . GLU B 1 76  ? -20.629 -31.154 5.667   1.00 17.95 ? 76  GLU B CA  1 
ATOM   2780 C  C   . GLU B 1 76  ? -19.482 -30.369 6.345   1.00 18.70 ? 76  GLU B C   1 
ATOM   2781 O  O   . GLU B 1 76  ? -19.724 -29.374 7.008   1.00 19.77 ? 76  GLU B O   1 
ATOM   2782 C  CB  . GLU B 1 76  ? -20.592 -30.930 4.142   1.00 19.69 ? 76  GLU B CB  1 
ATOM   2783 C  CG  . GLU B 1 76  ? -21.776 -31.551 3.410   1.00 23.82 ? 76  GLU B CG  1 
ATOM   2784 C  CD  . GLU B 1 76  ? -21.680 -31.407 1.909   1.00 32.26 ? 76  GLU B CD  1 
ATOM   2785 O  OE1 . GLU B 1 76  ? -21.187 -30.366 1.446   1.00 39.19 ? 76  GLU B OE1 1 
ATOM   2786 O  OE2 . GLU B 1 76  ? -22.152 -32.311 1.208   1.00 37.30 ? 76  GLU B OE2 1 
ATOM   2787 N  N   . ASN B 1 77  ? -18.242 -30.757 6.117   1.00 16.45 ? 77  ASN B N   1 
ATOM   2788 C  CA  . ASN B 1 77  ? -17.052 -30.078 6.719   1.00 15.52 ? 77  ASN B CA  1 
ATOM   2789 C  C   . ASN B 1 77  ? -16.431 -29.168 5.677   1.00 15.01 ? 77  ASN B C   1 
ATOM   2790 O  O   . ASN B 1 77  ? -15.229 -29.103 5.597   1.00 19.07 ? 77  ASN B O   1 
ATOM   2791 C  CB  . ASN B 1 77  ? -16.050 -31.082 7.322   1.00 17.03 ? 77  ASN B CB  1 
ATOM   2792 C  CG  . ASN B 1 77  ? -16.558 -31.668 8.644   1.00 16.56 ? 77  ASN B CG  1 
ATOM   2793 O  OD1 . ASN B 1 77  ? -17.333 -31.033 9.360   1.00 16.12 ? 77  ASN B OD1 1 
ATOM   2794 N  ND2 . ASN B 1 77  ? -16.182 -32.880 8.950   1.00 17.33 ? 77  ASN B ND2 1 
ATOM   2795 N  N   . LYS B 1 78  ? -17.250 -28.398 5.014   1.00 16.34 ? 78  LYS B N   1 
ATOM   2796 C  CA  . LYS B 1 78  ? -16.754 -27.425 4.057   1.00 17.13 ? 78  LYS B CA  1 
ATOM   2797 C  C   . LYS B 1 78  ? -16.211 -26.171 4.799   1.00 16.87 ? 78  LYS B C   1 
ATOM   2798 O  O   . LYS B 1 78  ? -15.312 -25.516 4.322   1.00 19.34 ? 78  LYS B O   1 
ATOM   2799 C  CB  . LYS B 1 78  ? -17.861 -27.022 3.118   1.00 21.76 ? 78  LYS B CB  1 
ATOM   2800 C  CG  . LYS B 1 78  ? -18.249 -28.183 2.202   1.00 30.79 ? 78  LYS B CG  1 
ATOM   2801 C  CD  . LYS B 1 78  ? -18.693 -27.742 0.830   1.00 37.47 ? 78  LYS B CD  1 
ATOM   2802 C  CE  . LYS B 1 78  ? -20.202 -27.888 0.668   1.00 40.61 ? 78  LYS B CE  1 
ATOM   2803 N  NZ  . LYS B 1 78  ? -20.483 -28.690 -0.559  1.00 43.77 ? 78  LYS B NZ  1 
ATOM   2804 N  N   . SER B 1 79  ? -16.901 -25.765 5.872   1.00 14.05 ? 79  SER B N   1 
ATOM   2805 C  CA  . SER B 1 79  ? -16.489 -24.531 6.597   1.00 15.00 ? 79  SER B CA  1 
ATOM   2806 C  C   . SER B 1 79  ? -16.201 -24.935 8.024   1.00 12.06 ? 79  SER B C   1 
ATOM   2807 O  O   . SER B 1 79  ? -17.230 -25.271 8.735   1.00 13.98 ? 79  SER B O   1 
ATOM   2808 C  CB  . SER B 1 79  ? -17.609 -23.499 6.570   1.00 15.65 ? 79  SER B CB  1 
ATOM   2809 O  OG  . SER B 1 79  ? -17.794 -23.083 5.213   1.00 16.56 ? 79  SER B OG  1 
ATOM   2810 N  N   . VAL B 1 80  ? -14.948 -24.973 8.436   1.00 13.66 ? 80  VAL B N   1 
ATOM   2811 C  CA  . VAL B 1 80  ? -14.556 -25.528 9.725   1.00 14.16 ? 80  VAL B CA  1 
ATOM   2812 C  C   . VAL B 1 80  ? -13.405 -24.792 10.303  1.00 17.33 ? 80  VAL B C   1 
ATOM   2813 O  O   . VAL B 1 80  ? -12.576 -24.163 9.601   1.00 17.38 ? 80  VAL B O   1 
ATOM   2814 C  CB  . VAL B 1 80  ? -14.142 -27.049 9.665   1.00 14.89 ? 80  VAL B CB  1 
ATOM   2815 C  CG1 . VAL B 1 80  ? -15.306 -27.886 9.049   1.00 15.04 ? 80  VAL B CG1 1 
ATOM   2816 C  CG2 . VAL B 1 80  ? -12.830 -27.168 8.775   1.00 15.94 ? 80  VAL B CG2 1 
ATOM   2817 N  N   . LEU B 1 81  ? -13.293 -24.866 11.601  1.00 13.96 ? 81  LEU B N   1 
ATOM   2818 C  CA  . LEU B 1 81  ? -12.261 -24.340 12.358  1.00 12.50 ? 81  LEU B CA  1 
ATOM   2819 C  C   . LEU B 1 81  ? -11.513 -25.482 13.058  1.00 14.20 ? 81  LEU B C   1 
ATOM   2820 O  O   . LEU B 1 81  ? -12.157 -26.319 13.710  1.00 14.08 ? 81  LEU B O   1 
ATOM   2821 C  CB  . LEU B 1 81  ? -12.833 -23.347 13.423  1.00 12.06 ? 81  LEU B CB  1 
ATOM   2822 C  CG  . LEU B 1 81  ? -11.738 -22.787 14.354  1.00 12.30 ? 81  LEU B CG  1 
ATOM   2823 C  CD1 . LEU B 1 81  ? -10.722 -21.884 13.712  1.00 14.26 ? 81  LEU B CD1 1 
ATOM   2824 C  CD2 . LEU B 1 81  ? -12.572 -21.995 15.406  1.00 13.59 ? 81  LEU B CD2 1 
ATOM   2825 N  N   . ARG B 1 82  ? -10.210 -25.555 12.850  1.00 14.49 ? 82  ARG B N   1 
ATOM   2826 C  CA  . ARG B 1 82  ? -9.307  -26.495 13.535  1.00 14.12 ? 82  ARG B CA  1 
ATOM   2827 C  C   . ARG B 1 82  ? -8.049  -25.849 14.077  1.00 13.32 ? 82  ARG B C   1 
ATOM   2828 O  O   . ARG B 1 82  ? -7.788  -24.640 13.852  1.00 14.58 ? 82  ARG B O   1 
ATOM   2829 C  CB  . ARG B 1 82  ? -8.934  -27.660 12.540  1.00 18.40 ? 82  ARG B CB  1 
ATOM   2830 C  CG  . ARG B 1 82  ? -10.091 -28.369 11.936  1.00 18.81 ? 82  ARG B CG  1 
ATOM   2831 C  CD  . ARG B 1 82  ? -9.688  -29.362 10.805  1.00 25.77 ? 82  ARG B CD  1 
ATOM   2832 N  NE  . ARG B 1 82  ? -9.454  -28.482 9.677   1.00 30.77 ? 82  ARG B NE  1 
ATOM   2833 C  CZ  . ARG B 1 82  ? -8.882  -28.772 8.503   1.00 36.47 ? 82  ARG B CZ  1 
ATOM   2834 N  NH1 . ARG B 1 82  ? -8.519  -30.002 8.210   1.00 33.89 ? 82  ARG B NH1 1 
ATOM   2835 N  NH2 . ARG B 1 82  ? -8.713  -27.791 7.605   1.00 40.41 ? 82  ARG B NH2 1 
ATOM   2836 N  N   . GLY B 1 83  ? -7.212  -26.617 14.773  1.00 13.07 ? 83  GLY B N   1 
ATOM   2837 C  CA  . GLY B 1 83  ? -6.013  -26.110 15.387  1.00 13.98 ? 83  GLY B CA  1 
ATOM   2838 C  C   . GLY B 1 83  ? -6.355  -25.175 16.518  1.00 14.20 ? 83  GLY B C   1 
ATOM   2839 O  O   . GLY B 1 83  ? -7.388  -25.433 17.256  1.00 14.35 ? 83  GLY B O   1 
ATOM   2840 N  N   . GLY B 1 84  ? -5.522  -24.166 16.756  1.00 14.90 ? 84  GLY B N   1 
ATOM   2841 C  CA  . GLY B 1 84  ? -5.700  -23.389 17.964  1.00 16.33 ? 84  GLY B CA  1 
ATOM   2842 C  C   . GLY B 1 84  ? -5.623  -24.324 19.196  1.00 14.01 ? 84  GLY B C   1 
ATOM   2843 O  O   . GLY B 1 84  ? -4.754  -25.183 19.304  1.00 17.99 ? 84  GLY B O   1 
ATOM   2844 N  N   . PRO B 1 85  ? -6.525  -24.132 20.163  1.00 14.18 ? 85  PRO B N   1 
ATOM   2845 C  CA  . PRO B 1 85  ? -6.513  -24.968 21.349  1.00 13.38 ? 85  PRO B CA  1 
ATOM   2846 C  C   . PRO B 1 85  ? -7.408  -26.221 21.152  1.00 12.65 ? 85  PRO B C   1 
ATOM   2847 O  O   . PRO B 1 85  ? -7.566  -26.957 22.082  1.00 15.43 ? 85  PRO B O   1 
ATOM   2848 C  CB  . PRO B 1 85  ? -7.241  -24.065 22.410  1.00 14.40 ? 85  PRO B CB  1 
ATOM   2849 C  CG  . PRO B 1 85  ? -8.270  -23.323 21.537  1.00 12.88 ? 85  PRO B CG  1 
ATOM   2850 C  CD  . PRO B 1 85  ? -7.469  -22.997 20.255  1.00 12.88 ? 85  PRO B CD  1 
ATOM   2851 N  N   . LEU B 1 86  ? -7.993  -26.401 19.969  1.00 11.95 ? 86  LEU B N   1 
ATOM   2852 C  CA  . LEU B 1 86  ? -9.072  -27.370 19.780  1.00 11.89 ? 86  LEU B CA  1 
ATOM   2853 C  C   . LEU B 1 86  ? -8.537  -28.771 19.456  1.00 13.30 ? 86  LEU B C   1 
ATOM   2854 O  O   . LEU B 1 86  ? -7.567  -28.928 18.687  1.00 14.93 ? 86  LEU B O   1 
ATOM   2855 C  CB  . LEU B 1 86  ? -9.955  -26.914 18.616  1.00 12.82 ? 86  LEU B CB  1 
ATOM   2856 C  CG  . LEU B 1 86  ? -10.547 -25.486 18.729  1.00 12.18 ? 86  LEU B CG  1 
ATOM   2857 C  CD1 . LEU B 1 86  ? -11.156 -25.096 17.412  1.00 13.53 ? 86  LEU B CD1 1 
ATOM   2858 C  CD2 . LEU B 1 86  ? -11.591 -25.500 19.833  1.00 13.43 ? 86  LEU B CD2 1 
ATOM   2859 N  N   . THR B 1 87  ? -9.251  -29.735 19.974  1.00 13.46 ? 87  THR B N   1 
ATOM   2860 C  CA  . THR B 1 87  ? -9.076  -31.140 19.513  1.00 14.37 ? 87  THR B CA  1 
ATOM   2861 C  C   . THR B 1 87  ? -10.178 -31.401 18.513  1.00 13.77 ? 87  THR B C   1 
ATOM   2862 O  O   . THR B 1 87  ? -11.359 -31.372 18.875  1.00 16.40 ? 87  THR B O   1 
ATOM   2863 C  CB  . THR B 1 87  ? -9.223  -32.062 20.753  1.00 14.70 ? 87  THR B CB  1 
ATOM   2864 O  OG1 . THR B 1 87  ? -8.126  -31.815 21.614  1.00 20.15 ? 87  THR B OG1 1 
ATOM   2865 C  CG2 . THR B 1 87  ? -9.115  -33.617 20.287  1.00 16.85 ? 87  THR B CG2 1 
ATOM   2866 N  N   . GLY B 1 88  ? -9.810  -31.777 17.307  1.00 15.84 ? 88  GLY B N   1 
ATOM   2867 C  CA  . GLY B 1 88  ? -10.765 -32.153 16.290  1.00 12.59 ? 88  GLY B CA  1 
ATOM   2868 C  C   . GLY B 1 88  ? -11.348 -30.988 15.531  1.00 15.32 ? 88  GLY B C   1 
ATOM   2869 O  O   . GLY B 1 88  ? -10.813 -29.868 15.596  1.00 17.57 ? 88  GLY B O   1 
ATOM   2870 N  N   . SER B 1 89  ? -12.428 -31.242 14.812  1.00 12.88 ? 89  SER B N   1 
ATOM   2871 C  CA  . SER B 1 89  ? -13.001 -30.289 13.825  1.00 15.58 ? 89  SER B CA  1 
ATOM   2872 C  C   . SER B 1 89  ? -14.305 -29.651 14.293  1.00 14.09 ? 89  SER B C   1 
ATOM   2873 O  O   . SER B 1 89  ? -15.282 -30.370 14.645  1.00 13.06 ? 89  SER B O   1 
ATOM   2874 C  CB  . SER B 1 89  ? -13.149 -30.975 12.396  1.00 16.52 ? 89  SER B CB  1 
ATOM   2875 O  OG  . SER B 1 89  ? -13.543 -30.089 11.329  1.00 16.93 ? 89  SER B OG  1 
ATOM   2876 N  N   . TYR B 1 90  ? -14.365 -28.281 14.259  1.00 11.86 ? 90  TYR B N   1 
ATOM   2877 C  CA  . TYR B 1 90  ? -15.524 -27.547 14.754  1.00 11.08 ? 90  TYR B CA  1 
ATOM   2878 C  C   . TYR B 1 90  ? -16.188 -26.880 13.528  1.00 11.65 ? 90  TYR B C   1 
ATOM   2879 O  O   . TYR B 1 90  ? -15.509 -26.101 12.787  1.00 13.76 ? 90  TYR B O   1 
ATOM   2880 C  CB  . TYR B 1 90  ? -14.926 -26.518 15.791  1.00 11.31 ? 90  TYR B CB  1 
ATOM   2881 C  CG  . TYR B 1 90  ? -14.667 -27.132 17.117  1.00 11.60 ? 90  TYR B CG  1 
ATOM   2882 C  CD1 . TYR B 1 90  ? -13.606 -28.002 17.335  1.00 11.21 ? 90  TYR B CD1 1 
ATOM   2883 C  CD2 . TYR B 1 90  ? -15.634 -26.951 18.188  1.00 12.33 ? 90  TYR B CD2 1 
ATOM   2884 C  CE1 . TYR B 1 90  ? -13.359 -28.581 18.542  1.00 12.06 ? 90  TYR B CE1 1 
ATOM   2885 C  CE2 . TYR B 1 90  ? -15.423 -27.552 19.426  1.00 11.54 ? 90  TYR B CE2 1 
ATOM   2886 C  CZ  . TYR B 1 90  ? -14.274 -28.370 19.609  1.00 10.92 ? 90  TYR B CZ  1 
ATOM   2887 O  OH  . TYR B 1 90  ? -14.046 -28.984 20.783  1.00 13.11 ? 90  TYR B OH  1 
ATOM   2888 N  N   . ARG B 1 91  ? -17.401 -27.254 13.269  1.00 11.50 ? 91  ARG B N   1 
ATOM   2889 C  CA  . ARG B 1 91  ? -18.142 -26.867 12.068  1.00 12.09 ? 91  ARG B CA  1 
ATOM   2890 C  C   . ARG B 1 91  ? -18.779 -25.516 12.272  1.00 11.85 ? 91  ARG B C   1 
ATOM   2891 O  O   . ARG B 1 91  ? -19.433 -25.232 13.306  1.00 12.26 ? 91  ARG B O   1 
ATOM   2892 C  CB  . ARG B 1 91  ? -19.165 -27.977 11.764  1.00 14.22 ? 91  ARG B CB  1 
ATOM   2893 C  CG  . ARG B 1 91  ? -19.702 -27.856 10.334  1.00 12.68 ? 91  ARG B CG  1 
ATOM   2894 C  CD  . ARG B 1 91  ? -20.692 -28.996 9.967   1.00 14.20 ? 91  ARG B CD  1 
ATOM   2895 N  NE  . ARG B 1 91  ? -20.002 -30.272 9.928   1.00 13.56 ? 91  ARG B NE  1 
ATOM   2896 C  CZ  . ARG B 1 91  ? -20.588 -31.452 10.077  1.00 11.73 ? 91  ARG B CZ  1 
ATOM   2897 N  NH1 . ARG B 1 91  ? -21.897 -31.543 10.275  1.00 14.64 ? 91  ARG B NH1 1 
ATOM   2898 N  NH2 . ARG B 1 91  ? -19.850 -32.548 10.024  1.00 12.01 ? 91  ARG B NH2 1 
ATOM   2899 N  N   . LEU B 1 92  ? -18.623 -24.640 11.275  1.00 13.15 ? 92  LEU B N   1 
ATOM   2900 C  CA  . LEU B 1 92  ? -19.313 -23.356 11.337  1.00 10.80 ? 92  LEU B CA  1 
ATOM   2901 C  C   . LEU B 1 92  ? -20.799 -23.429 11.367  1.00 11.94 ? 92  LEU B C   1 
ATOM   2902 O  O   . LEU B 1 92  ? -21.433 -24.155 10.552  1.00 11.84 ? 92  LEU B O   1 
ATOM   2903 C  CB  . LEU B 1 92  ? -18.854 -22.522 10.129  1.00 11.96 ? 92  LEU B CB  1 
ATOM   2904 C  CG  . LEU B 1 92  ? -19.622 -21.167 9.928   1.00 11.75 ? 92  LEU B CG  1 
ATOM   2905 C  CD1 . LEU B 1 92  ? -19.129 -20.177 11.027  1.00 12.56 ? 92  LEU B CD1 1 
ATOM   2906 C  CD2 . LEU B 1 92  ? -19.003 -20.611 8.583   1.00 14.02 ? 92  LEU B CD2 1 
ATOM   2907 N  N   . ARG B 1 93  ? -21.474 -22.682 12.310  1.00 10.12 ? 93  ARG B N   1 
ATOM   2908 C  CA  . ARG B 1 93  ? -22.871 -22.563 12.267  1.00 11.40 ? 93  ARG B CA  1 
ATOM   2909 C  C   . ARG B 1 93  ? -23.437 -21.177 12.101  1.00 11.47 ? 93  ARG B C   1 
ATOM   2910 O  O   . ARG B 1 93  ? -24.383 -20.996 11.362  1.00 12.89 ? 93  ARG B O   1 
ATOM   2911 C  CB  . ARG B 1 93  ? -23.464 -23.178 13.554  1.00 13.27 ? 93  ARG B CB  1 
ATOM   2912 C  CG  . ARG B 1 93  ? -25.024 -23.150 13.559  1.00 16.21 ? 93  ARG B CG  1 
ATOM   2913 C  CD  . ARG B 1 93  ? -25.851 -23.581 12.269  1.00 22.25 ? 93  ARG B CD  1 
ATOM   2914 N  NE  . ARG B 1 93  ? -27.277 -23.378 12.539  1.00 27.30 ? 93  ARG B NE  1 
ATOM   2915 C  CZ  . ARG B 1 93  ? -28.310 -23.527 11.693  1.00 37.95 ? 93  ARG B CZ  1 
ATOM   2916 N  NH1 . ARG B 1 93  ? -28.159 -23.891 10.411  1.00 44.02 ? 93  ARG B NH1 1 
ATOM   2917 N  NH2 . ARG B 1 93  ? -29.536 -23.328 12.166  1.00 41.94 ? 93  ARG B NH2 1 
ATOM   2918 N  N   A GLN B 1 94  ? -22.792 -20.191 12.734  0.50 11.06 ? 94  GLN B N   1 
ATOM   2919 N  N   B GLN B 1 94  ? -22.925 -20.169 12.806  0.50 11.97 ? 94  GLN B N   1 
ATOM   2920 C  CA  A GLN B 1 94  ? -23.429 -18.886 12.755  0.50 11.59 ? 94  GLN B CA  1 
ATOM   2921 C  CA  B GLN B 1 94  ? -23.513 -18.823 12.601  0.50 12.78 ? 94  GLN B CA  1 
ATOM   2922 C  C   A GLN B 1 94  ? -22.457 -17.729 12.958  0.50 10.96 ? 94  GLN B C   1 
ATOM   2923 C  C   B GLN B 1 94  ? -22.558 -17.738 12.967  0.50 11.65 ? 94  GLN B C   1 
ATOM   2924 O  O   A GLN B 1 94  ? -21.377 -17.911 13.495  0.50 11.47 ? 94  GLN B O   1 
ATOM   2925 O  O   B GLN B 1 94  ? -21.643 -17.958 13.689  0.50 11.59 ? 94  GLN B O   1 
ATOM   2926 C  CB  A GLN B 1 94  ? -24.570 -18.904 13.760  0.50 11.66 ? 94  GLN B CB  1 
ATOM   2927 C  CB  B GLN B 1 94  ? -24.868 -18.569 13.296  0.50 14.75 ? 94  GLN B CB  1 
ATOM   2928 C  CG  A GLN B 1 94  ? -24.239 -18.878 15.179  0.50 12.69 ? 94  GLN B CG  1 
ATOM   2929 C  CG  B GLN B 1 94  ? -24.890 -18.527 14.799  0.50 16.35 ? 94  GLN B CG  1 
ATOM   2930 C  CD  A GLN B 1 94  ? -24.618 -17.484 15.615  0.50 14.70 ? 94  GLN B CD  1 
ATOM   2931 C  CD  B GLN B 1 94  ? -26.059 -17.692 15.455  0.50 15.27 ? 94  GLN B CD  1 
ATOM   2932 O  OE1 A GLN B 1 94  ? -23.807 -16.652 15.469  0.50 16.92 ? 94  GLN B OE1 1 
ATOM   2933 O  OE1 B GLN B 1 94  ? -27.240 -17.952 15.239  0.50 19.33 ? 94  GLN B OE1 1 
ATOM   2934 N  NE2 A GLN B 1 94  ? -25.892 -17.231 15.980  0.50 14.37 ? 94  GLN B NE2 1 
ATOM   2935 N  NE2 B GLN B 1 94  ? -25.698 -16.699 16.272  0.50 14.38 ? 94  GLN B NE2 1 
ATOM   2936 N  N   . VAL B 1 95  ? -22.815 -16.547 12.454  1.00 11.66 ? 95  VAL B N   1 
ATOM   2937 C  CA  . VAL B 1 95  ? -21.977 -15.340 12.796  1.00 11.99 ? 95  VAL B CA  1 
ATOM   2938 C  C   . VAL B 1 95  ? -22.972 -14.304 13.326  1.00 10.79 ? 95  VAL B C   1 
ATOM   2939 O  O   . VAL B 1 95  ? -24.105 -14.179 12.793  1.00 10.54 ? 95  VAL B O   1 
ATOM   2940 C  CB  . VAL B 1 95  ? -21.396 -14.763 11.498  1.00 13.99 ? 95  VAL B CB  1 
ATOM   2941 C  CG1 . VAL B 1 95  ? -20.890 -13.342 11.769  1.00 16.44 ? 95  VAL B CG1 1 
ATOM   2942 C  CG2 . VAL B 1 95  ? -20.278 -15.670 11.018  1.00 15.84 ? 95  VAL B CG2 1 
ATOM   2943 N  N   . HIS B 1 96  ? -22.572 -13.571 14.361  1.00 11.33 ? 96  HIS B N   1 
ATOM   2944 C  CA  . HIS B 1 96  ? -23.451 -12.459 14.899  1.00 11.03 ? 96  HIS B CA  1 
ATOM   2945 C  C   . HIS B 1 96  ? -22.538 -11.370 15.425  1.00 11.12 ? 96  HIS B C   1 
ATOM   2946 O  O   . HIS B 1 96  ? -21.326 -11.509 15.390  1.00 11.78 ? 96  HIS B O   1 
ATOM   2947 C  CB  . HIS B 1 96  ? -24.515 -12.948 15.931  1.00 10.00 ? 96  HIS B CB  1 
ATOM   2948 C  CG  . HIS B 1 96  ? -23.868 -13.510 17.136  1.00 9.97  ? 96  HIS B CG  1 
ATOM   2949 N  ND1 . HIS B 1 96  ? -23.609 -14.893 17.278  1.00 10.96 ? 96  HIS B ND1 1 
ATOM   2950 C  CD2 . HIS B 1 96  ? -23.304 -12.871 18.199  1.00 10.59 ? 96  HIS B CD2 1 
ATOM   2951 C  CE1 . HIS B 1 96  ? -22.840 -15.046 18.401  1.00 11.11 ? 96  HIS B CE1 1 
ATOM   2952 N  NE2 . HIS B 1 96  ? -22.695 -13.815 19.007  1.00 11.39 ? 96  HIS B NE2 1 
ATOM   2953 N  N   . LEU B 1 97  ? -23.127 -10.236 15.932  1.00 9.64  ? 97  LEU B N   1 
ATOM   2954 C  CA  . LEU B 1 97  ? -22.263 -9.124  16.387  1.00 9.96  ? 97  LEU B CA  1 
ATOM   2955 C  C   . LEU B 1 97  ? -22.801 -8.540  17.677  1.00 9.65  ? 97  LEU B C   1 
ATOM   2956 O  O   . LEU B 1 97  ? -24.031 -8.504  17.867  1.00 11.00 ? 97  LEU B O   1 
ATOM   2957 C  CB  . LEU B 1 97  ? -22.382 -8.047  15.252  1.00 10.68 ? 97  LEU B CB  1 
ATOM   2958 C  CG  . LEU B 1 97  ? -21.486 -6.786  15.460  1.00 12.08 ? 97  LEU B CG  1 
ATOM   2959 C  CD1 . LEU B 1 97  ? -20.059 -7.070  15.162  1.00 12.94 ? 97  LEU B CD1 1 
ATOM   2960 C  CD2 . LEU B 1 97  ? -21.939 -5.709  14.395  1.00 14.44 ? 97  LEU B CD2 1 
ATOM   2961 N  N   . HIS B 1 98  ? -21.908 -7.976  18.496  1.00 10.40 ? 98  HIS B N   1 
ATOM   2962 C  CA  . HIS B 1 98  ? -22.290 -7.178  19.697  1.00 9.54  ? 98  HIS B CA  1 
ATOM   2963 C  C   . HIS B 1 98  ? -21.758 -5.768  19.536  1.00 9.78  ? 98  HIS B C   1 
ATOM   2964 O  O   . HIS B 1 98  ? -20.688 -5.536  18.932  1.00 9.77  ? 98  HIS B O   1 
ATOM   2965 C  CB  . HIS B 1 98  ? -21.668 -7.873  20.942  1.00 10.17 ? 98  HIS B CB  1 
ATOM   2966 C  CG  . HIS B 1 98  ? -22.153 -9.329  21.156  1.00 11.26 ? 98  HIS B CG  1 
ATOM   2967 N  ND1 . HIS B 1 98  ? -23.315 -9.677  21.866  1.00 10.47 ? 98  HIS B ND1 1 
ATOM   2968 C  CD2 . HIS B 1 98  ? -21.592 -10.482 20.667  1.00 11.36 ? 98  HIS B CD2 1 
ATOM   2969 C  CE1 . HIS B 1 98  ? -23.432 -11.034 21.824  1.00 9.73  ? 98  HIS B CE1 1 
ATOM   2970 N  NE2 . HIS B 1 98  ? -22.344 -11.497 21.078  1.00 8.47  ? 98  HIS B NE2 1 
ATOM   2971 N  N   . TRP B 1 99  ? -22.601 -4.864  20.077  1.00 10.08 ? 99  TRP B N   1 
ATOM   2972 C  CA  . TRP B 1 99  ? -22.243 -3.415  20.091  1.00 11.25 ? 99  TRP B CA  1 
ATOM   2973 C  C   . TRP B 1 99  ? -22.799 -2.807  21.346  1.00 11.31 ? 99  TRP B C   1 
ATOM   2974 O  O   . TRP B 1 99  ? -23.564 -3.424  22.146  1.00 11.17 ? 99  TRP B O   1 
ATOM   2975 C  CB  . TRP B 1 99  ? -22.773 -2.751  18.796  1.00 13.26 ? 99  TRP B CB  1 
ATOM   2976 C  CG  . TRP B 1 99  ? -24.215 -2.861  18.644  1.00 12.63 ? 99  TRP B CG  1 
ATOM   2977 C  CD1 . TRP B 1 99  ? -25.189 -2.068  19.184  1.00 12.91 ? 99  TRP B CD1 1 
ATOM   2978 C  CD2 . TRP B 1 99  ? -24.954 -3.925  17.861  1.00 12.17 ? 99  TRP B CD2 1 
ATOM   2979 N  NE1 . TRP B 1 99  ? -26.445 -2.507  18.777  1.00 12.82 ? 99  TRP B NE1 1 
ATOM   2980 C  CE2 . TRP B 1 99  ? -26.352 -3.650  18.000  1.00 12.91 ? 99  TRP B CE2 1 
ATOM   2981 C  CE3 . TRP B 1 99  ? -24.535 -5.083  17.124  1.00 11.70 ? 99  TRP B CE3 1 
ATOM   2982 C  CZ2 . TRP B 1 99  ? -27.374 -4.442  17.382  1.00 12.52 ? 99  TRP B CZ2 1 
ATOM   2983 C  CZ3 . TRP B 1 99  ? -25.532 -5.877  16.483  1.00 13.17 ? 99  TRP B CZ3 1 
ATOM   2984 C  CH2 . TRP B 1 99  ? -26.909 -5.539  16.598  1.00 12.31 ? 99  TRP B CH2 1 
ATOM   2985 N  N   . GLY B 1 100 ? -22.505 -1.485  21.444  1.00 11.69 ? 100 GLY B N   1 
ATOM   2986 C  CA  . GLY B 1 100 ? -23.067 -0.733  22.544  1.00 13.14 ? 100 GLY B CA  1 
ATOM   2987 C  C   . GLY B 1 100 ? -23.735 0.544   22.015  1.00 15.47 ? 100 GLY B C   1 
ATOM   2988 O  O   . GLY B 1 100 ? -23.746 0.736   20.822  1.00 14.84 ? 100 GLY B O   1 
ATOM   2989 N  N   . SER B 1 101 ? -24.295 1.337   22.941  1.00 13.63 ? 101 SER B N   1 
ATOM   2990 C  CA  . SER B 1 101 ? -25.037 2.554   22.467  1.00 15.63 ? 101 SER B CA  1 
ATOM   2991 C  C   . SER B 1 101 ? -24.028 3.662   22.117  1.00 14.88 ? 101 SER B C   1 
ATOM   2992 O  O   . SER B 1 101 ? -24.449 4.665   21.541  1.00 17.33 ? 101 SER B O   1 
ATOM   2993 C  CB  . SER B 1 101 ? -26.048 3.027   23.500  1.00 16.34 ? 101 SER B CB  1 
ATOM   2994 O  OG  . SER B 1 101 ? -25.342 3.608   24.616  1.00 19.50 ? 101 SER B OG  1 
ATOM   2995 N  N   . ALA B 1 102 ? -22.773 3.567   22.538  1.00 14.26 ? 102 ALA B N   1 
ATOM   2996 C  CA  . ALA B 1 102 ? -21.753 4.500   22.185  1.00 16.23 ? 102 ALA B CA  1 
ATOM   2997 C  C   . ALA B 1 102 ? -20.596 3.837   21.419  1.00 16.54 ? 102 ALA B C   1 
ATOM   2998 O  O   . ALA B 1 102 ? -20.231 2.642   21.707  1.00 17.00 ? 102 ALA B O   1 
ATOM   2999 C  CB  . ALA B 1 102 ? -21.171 5.076   23.466  1.00 18.17 ? 102 ALA B CB  1 
ATOM   3000 N  N   . ASP B 1 103 ? -19.982 4.539   20.498  1.00 15.89 ? 103 ASP B N   1 
ATOM   3001 C  CA  . ASP B 1 103 ? -18.976 3.926   19.631  1.00 18.85 ? 103 ASP B CA  1 
ATOM   3002 C  C   . ASP B 1 103 ? -17.704 3.483   20.358  1.00 19.22 ? 103 ASP B C   1 
ATOM   3003 O  O   . ASP B 1 103 ? -16.940 2.693   19.776  1.00 19.60 ? 103 ASP B O   1 
ATOM   3004 C  CB  . ASP B 1 103 ? -18.610 4.871   18.518  1.00 19.37 ? 103 ASP B CB  1 
ATOM   3005 C  CG  . ASP B 1 103 ? -19.605 4.919   17.407  1.00 19.10 ? 103 ASP B CG  1 
ATOM   3006 O  OD1 . ASP B 1 103 ? -20.628 4.198   17.389  1.00 20.95 ? 103 ASP B OD1 1 
ATOM   3007 O  OD2 . ASP B 1 103 ? -19.343 5.633   16.412  1.00 21.85 ? 103 ASP B OD2 1 
ATOM   3008 N  N   . ASP B 1 104 ? -17.450 3.937   21.574  1.00 19.77 ? 104 ASP B N   1 
ATOM   3009 C  CA  . ASP B 1 104 ? -16.213 3.529   22.220  1.00 22.82 ? 104 ASP B CA  1 
ATOM   3010 C  C   . ASP B 1 104 ? -16.400 2.527   23.339  1.00 24.71 ? 104 ASP B C   1 
ATOM   3011 O  O   . ASP B 1 104 ? -15.497 2.327   24.148  1.00 28.41 ? 104 ASP B O   1 
ATOM   3012 C  CB  . ASP B 1 104 ? -15.491 4.780   22.744  1.00 27.26 ? 104 ASP B CB  1 
ATOM   3013 C  CG  . ASP B 1 104 ? -16.313 5.541   23.758  1.00 29.72 ? 104 ASP B CG  1 
ATOM   3014 O  OD1 . ASP B 1 104 ? -17.556 5.392   23.848  1.00 29.33 ? 104 ASP B OD1 1 
ATOM   3015 O  OD2 . ASP B 1 104 ? -15.680 6.328   24.509  1.00 32.94 ? 104 ASP B OD2 1 
ATOM   3016 N  N   . HIS B 1 105 ? -17.550 1.853   23.383  1.00 19.46 ? 105 HIS B N   1 
ATOM   3017 C  CA  . HIS B 1 105 ? -17.839 0.933   24.502  1.00 21.64 ? 105 HIS B CA  1 
ATOM   3018 C  C   . HIS B 1 105 ? -18.883 -0.073  24.021  1.00 17.80 ? 105 HIS B C   1 
ATOM   3019 O  O   . HIS B 1 105 ? -20.032 -0.108  24.473  1.00 20.71 ? 105 HIS B O   1 
ATOM   3020 C  CB  . HIS B 1 105 ? -18.291 1.676   25.787  1.00 24.15 ? 105 HIS B CB  1 
ATOM   3021 C  CG  . HIS B 1 105 ? -18.095 0.889   27.066  1.00 29.11 ? 105 HIS B CG  1 
ATOM   3022 N  ND1 . HIS B 1 105 ? -19.101 0.227   27.695  1.00 31.59 ? 105 HIS B ND1 1 
ATOM   3023 C  CD2 . HIS B 1 105 ? -16.956 0.711   27.854  1.00 26.44 ? 105 HIS B CD2 1 
ATOM   3024 C  CE1 . HIS B 1 105 ? -18.609 -0.349  28.829  1.00 27.49 ? 105 HIS B CE1 1 
ATOM   3025 N  NE2 . HIS B 1 105 ? -17.298 -0.063  28.903  1.00 30.60 ? 105 HIS B NE2 1 
ATOM   3026 N  N   . GLY B 1 106 ? -18.491 -0.969  23.132  1.00 16.23 ? 106 GLY B N   1 
ATOM   3027 C  CA  . GLY B 1 106 ? -19.445 -1.900  22.593  1.00 12.95 ? 106 GLY B CA  1 
ATOM   3028 C  C   . GLY B 1 106 ? -19.024 -3.362  22.572  1.00 13.95 ? 106 GLY B C   1 
ATOM   3029 O  O   . GLY B 1 106 ? -19.874 -4.225  22.328  1.00 13.92 ? 106 GLY B O   1 
ATOM   3030 N  N   . SER B 1 107 ? -17.773 -3.624  22.851  1.00 12.66 ? 107 SER B N   1 
ATOM   3031 C  CA  . SER B 1 107 ? -17.299 -5.067  22.798  1.00 11.27 ? 107 SER B CA  1 
ATOM   3032 C  C   . SER B 1 107 ? -17.797 -5.807  24.029  1.00 12.40 ? 107 SER B C   1 
ATOM   3033 O  O   . SER B 1 107 ? -18.120 -5.212  25.056  1.00 13.22 ? 107 SER B O   1 
ATOM   3034 C  CB  . SER B 1 107 ? -15.827 -5.152  22.527  1.00 12.05 ? 107 SER B CB  1 
ATOM   3035 O  OG  . SER B 1 107 ? -15.058 -4.562  23.589  1.00 11.60 ? 107 SER B OG  1 
ATOM   3036 N  N   . GLU B 1 108 ? -17.770 -7.162  23.931  1.00 10.53 ? 108 GLU B N   1 
ATOM   3037 C  CA  . GLU B 1 108 ? -18.047 -7.991  25.090  1.00 9.58  ? 108 GLU B CA  1 
ATOM   3038 C  C   . GLU B 1 108 ? -16.776 -8.229  25.886  1.00 11.27 ? 108 GLU B C   1 
ATOM   3039 O  O   . GLU B 1 108 ? -16.648 -7.875  27.058  1.00 11.94 ? 108 GLU B O   1 
ATOM   3040 C  CB  . GLU B 1 108 ? -18.686 -9.301  24.612  1.00 9.65  ? 108 GLU B CB  1 
ATOM   3041 C  CG  . GLU B 1 108 ? -20.068 -9.132  23.948  1.00 13.11 ? 108 GLU B CG  1 
ATOM   3042 C  CD  . GLU B 1 108 ? -21.036 -10.222 24.323  1.00 13.61 ? 108 GLU B CD  1 
ATOM   3043 O  OE1 . GLU B 1 108 ? -20.756 -11.366 23.899  1.00 12.90 ? 108 GLU B OE1 1 
ATOM   3044 O  OE2 . GLU B 1 108 ? -22.033 -9.931  24.953  1.00 11.65 ? 108 GLU B OE2 1 
ATOM   3045 N  N   . HIS B 1 109 ? -15.744 -8.783  25.261  1.00 9.88  ? 109 HIS B N   1 
ATOM   3046 C  CA  . HIS B 1 109 ? -14.448 -8.883  25.844  1.00 10.65 ? 109 HIS B CA  1 
ATOM   3047 C  C   . HIS B 1 109 ? -13.809 -7.495  25.911  1.00 11.73 ? 109 HIS B C   1 
ATOM   3048 O  O   . HIS B 1 109 ? -14.028 -6.629  25.085  1.00 11.35 ? 109 HIS B O   1 
ATOM   3049 C  CB  . HIS B 1 109 ? -13.552 -9.860  25.031  1.00 12.40 ? 109 HIS B CB  1 
ATOM   3050 C  CG  . HIS B 1 109 ? -14.023 -11.296 25.191  1.00 10.28 ? 109 HIS B CG  1 
ATOM   3051 N  ND1 . HIS B 1 109 ? -14.939 -11.854 24.376  1.00 10.93 ? 109 HIS B ND1 1 
ATOM   3052 C  CD2 . HIS B 1 109 ? -13.753 -12.247 26.183  1.00 11.23 ? 109 HIS B CD2 1 
ATOM   3053 C  CE1 . HIS B 1 109 ? -15.220 -13.106 24.797  1.00 9.94  ? 109 HIS B CE1 1 
ATOM   3054 N  NE2 . HIS B 1 109 ? -14.485 -13.347 25.897  1.00 10.16 ? 109 HIS B NE2 1 
ATOM   3055 N  N   . ILE B 1 110 ? -13.055 -7.304  26.962  1.00 11.91 ? 110 ILE B N   1 
ATOM   3056 C  CA  . ILE B 1 110 ? -12.224 -6.051  27.188  1.00 14.03 ? 110 ILE B CA  1 
ATOM   3057 C  C   . ILE B 1 110 ? -10.752 -6.442  27.268  1.00 15.69 ? 110 ILE B C   1 
ATOM   3058 O  O   . ILE B 1 110 ? -10.448 -7.523  27.811  1.00 14.63 ? 110 ILE B O   1 
ATOM   3059 C  CB  . ILE B 1 110 ? -12.761 -5.392  28.527  1.00 17.84 ? 110 ILE B CB  1 
ATOM   3060 C  CG1 . ILE B 1 110 ? -14.266 -4.993  28.354  1.00 19.99 ? 110 ILE B CG1 1 
ATOM   3061 C  CG2 . ILE B 1 110 ? -11.858 -4.240  29.068  1.00 21.26 ? 110 ILE B CG2 1 
ATOM   3062 C  CD1 . ILE B 1 110 ? -14.858 -4.654  29.717  1.00 22.56 ? 110 ILE B CD1 1 
ATOM   3063 N  N   . VAL B 1 111 ? -9.809  -5.571  26.840  1.00 12.94 ? 111 VAL B N   1 
ATOM   3064 C  CA  . VAL B 1 111 ? -8.415  -5.886  26.891  1.00 15.31 ? 111 VAL B CA  1 
ATOM   3065 C  C   . VAL B 1 111 ? -7.687  -4.759  27.666  1.00 15.51 ? 111 VAL B C   1 
ATOM   3066 O  O   . VAL B 1 111 ? -7.720  -3.619  27.198  1.00 15.87 ? 111 VAL B O   1 
ATOM   3067 C  CB  . VAL B 1 111 ? -7.806  -5.994  25.481  1.00 17.55 ? 111 VAL B CB  1 
ATOM   3068 C  CG1 . VAL B 1 111 ? -6.339  -6.333  25.620  1.00 16.22 ? 111 VAL B CG1 1 
ATOM   3069 C  CG2 . VAL B 1 111 ? -8.535  -7.087  24.681  1.00 15.92 ? 111 VAL B CG2 1 
ATOM   3070 N  N   . ASP B 1 112 ? -7.096  -5.118  28.804  1.00 16.37 ? 112 ASP B N   1 
ATOM   3071 C  CA  . ASP B 1 112 ? -6.325  -4.155  29.689  1.00 16.39 ? 112 ASP B CA  1 
ATOM   3072 C  C   . ASP B 1 112 ? -7.159  -2.849  29.783  1.00 14.81 ? 112 ASP B C   1 
ATOM   3073 O  O   . ASP B 1 112 ? -6.679  -1.734  29.476  1.00 16.31 ? 112 ASP B O   1 
ATOM   3074 C  CB  . ASP B 1 112 ? -4.936  -3.897  29.094  1.00 19.74 ? 112 ASP B CB  1 
ATOM   3075 C  CG  . ASP B 1 112 ? -4.052  -5.124  29.214  1.00 19.14 ? 112 ASP B CG  1 
ATOM   3076 O  OD1 . ASP B 1 112 ? -4.353  -5.947  30.109  1.00 25.21 ? 112 ASP B OD1 1 
ATOM   3077 O  OD2 . ASP B 1 112 ? -3.121  -5.174  28.369  1.00 26.40 ? 112 ASP B OD2 1 
ATOM   3078 N  N   . GLY B 1 113 ? -8.375  -3.029  30.247  1.00 13.13 ? 113 GLY B N   1 
ATOM   3079 C  CA  . GLY B 1 113 ? -9.288  -1.916  30.536  1.00 14.95 ? 113 GLY B CA  1 
ATOM   3080 C  C   . GLY B 1 113 ? -9.954  -1.265  29.333  1.00 16.69 ? 113 GLY B C   1 
ATOM   3081 O  O   . GLY B 1 113 ? -10.831 -0.390  29.536  1.00 23.21 ? 113 GLY B O   1 
ATOM   3082 N  N   . VAL B 1 114 ? -9.577  -1.673  28.110  1.00 17.49 ? 114 VAL B N   1 
ATOM   3083 C  CA  . VAL B 1 114 ? -10.058 -1.030  26.860  1.00 19.19 ? 114 VAL B CA  1 
ATOM   3084 C  C   . VAL B 1 114 ? -11.181 -1.821  26.230  1.00 16.18 ? 114 VAL B C   1 
ATOM   3085 O  O   . VAL B 1 114 ? -10.990 -3.025  25.969  1.00 16.76 ? 114 VAL B O   1 
ATOM   3086 C  CB  . VAL B 1 114 ? -8.937  -0.979  25.792  1.00 21.67 ? 114 VAL B CB  1 
ATOM   3087 C  CG1 . VAL B 1 114 ? -9.542  -0.486  24.458  1.00 23.31 ? 114 VAL B CG1 1 
ATOM   3088 C  CG2 . VAL B 1 114 ? -7.811  -0.072  26.318  1.00 18.89 ? 114 VAL B CG2 1 
ATOM   3089 N  N   . SER B 1 115 ? -12.317 -1.164  25.981  1.00 16.71 ? 115 SER B N   1 
ATOM   3090 C  CA  . SER B 1 115 ? -13.402 -1.745  25.162  1.00 14.12 ? 115 SER B CA  1 
ATOM   3091 C  C   . SER B 1 115 ? -13.177 -1.311  23.730  1.00 17.29 ? 115 SER B C   1 
ATOM   3092 O  O   . SER B 1 115 ? -12.588 -0.275  23.441  1.00 21.09 ? 115 SER B O   1 
ATOM   3093 C  CB  . SER B 1 115 ? -14.738 -1.230  25.566  1.00 16.66 ? 115 SER B CB  1 
ATOM   3094 O  OG  . SER B 1 115 ? -15.089 -1.748  26.838  1.00 21.26 ? 115 SER B OG  1 
ATOM   3095 N  N   . TYR B 1 116 ? -13.532 -2.198  22.815  1.00 12.34 ? 116 TYR B N   1 
ATOM   3096 C  CA  . TYR B 1 116 ? -13.677 -1.842  21.419  1.00 12.89 ? 116 TYR B CA  1 
ATOM   3097 C  C   . TYR B 1 116 ? -15.065 -1.389  21.018  1.00 11.62 ? 116 TYR B C   1 
ATOM   3098 O  O   . TYR B 1 116 ? -15.993 -1.427  21.835  1.00 11.78 ? 116 TYR B O   1 
ATOM   3099 C  CB  . TYR B 1 116 ? -13.163 -3.041  20.574  1.00 12.49 ? 116 TYR B CB  1 
ATOM   3100 C  CG  . TYR B 1 116 ? -11.722 -3.238  20.721  1.00 14.20 ? 116 TYR B CG  1 
ATOM   3101 C  CD1 . TYR B 1 116 ? -10.823 -2.638  19.786  1.00 16.07 ? 116 TYR B CD1 1 
ATOM   3102 C  CD2 . TYR B 1 116 ? -11.197 -4.054  21.752  1.00 16.10 ? 116 TYR B CD2 1 
ATOM   3103 C  CE1 . TYR B 1 116 ? -9.463  -2.796  19.890  1.00 18.04 ? 116 TYR B CE1 1 
ATOM   3104 C  CE2 . TYR B 1 116 ? -9.829  -4.210  21.854  1.00 17.39 ? 116 TYR B CE2 1 
ATOM   3105 C  CZ  . TYR B 1 116 ? -8.996  -3.607  20.935  1.00 17.64 ? 116 TYR B CZ  1 
ATOM   3106 O  OH  . TYR B 1 116 ? -7.628  -3.851  21.121  1.00 25.37 ? 116 TYR B OH  1 
ATOM   3107 N  N   . ALA B 1 117 ? -15.249 -0.931  19.770  1.00 13.22 ? 117 ALA B N   1 
ATOM   3108 C  CA  . ALA B 1 117 ? -16.523 -0.438  19.326  1.00 13.12 ? 117 ALA B CA  1 
ATOM   3109 C  C   . ALA B 1 117 ? -17.561 -1.543  19.179  1.00 13.09 ? 117 ALA B C   1 
ATOM   3110 O  O   . ALA B 1 117 ? -18.720 -1.310  19.387  1.00 11.62 ? 117 ALA B O   1 
ATOM   3111 C  CB  . ALA B 1 117 ? -16.380 0.231   17.958  1.00 16.20 ? 117 ALA B CB  1 
ATOM   3112 N  N   . ALA B 1 118 ? -17.095 -2.732  18.816  1.00 10.47 ? 118 ALA B N   1 
ATOM   3113 C  CA  . ALA B 1 118 ? -18.051 -3.827  18.602  1.00 10.15 ? 118 ALA B CA  1 
ATOM   3114 C  C   . ALA B 1 118 ? -17.225 -5.142  18.570  1.00 10.49 ? 118 ALA B C   1 
ATOM   3115 O  O   . ALA B 1 118 ? -16.041 -5.111  18.702  1.00 10.36 ? 118 ALA B O   1 
ATOM   3116 C  CB  . ALA B 1 118 ? -18.868 -3.656  17.327  1.00 10.14 ? 118 ALA B CB  1 
ATOM   3117 N  N   . GLU B 1 119 ? -17.945 -6.275  18.548  1.00 10.20 ? 119 GLU B N   1 
ATOM   3118 C  CA  . GLU B 1 119 ? -17.222 -7.561  18.574  1.00 10.34 ? 119 GLU B CA  1 
ATOM   3119 C  C   . GLU B 1 119 ? -18.082 -8.578  17.758  1.00 10.11 ? 119 GLU B C   1 
ATOM   3120 O  O   . GLU B 1 119 ? -19.238 -8.829  18.061  1.00 10.67 ? 119 GLU B O   1 
ATOM   3121 C  CB  . GLU B 1 119 ? -17.110 -8.056  19.998  1.00 10.51 ? 119 GLU B CB  1 
ATOM   3122 C  CG  . GLU B 1 119 ? -16.142 -9.249  20.140  1.00 11.25 ? 119 GLU B CG  1 
ATOM   3123 C  CD  . GLU B 1 119 ? -15.903 -9.619  21.611  1.00 12.67 ? 119 GLU B CD  1 
ATOM   3124 O  OE1 . GLU B 1 119 ? -15.853 -8.709  22.467  1.00 11.88 ? 119 GLU B OE1 1 
ATOM   3125 O  OE2 . GLU B 1 119 ? -15.803 -10.852 21.894  1.00 13.12 ? 119 GLU B OE2 1 
ATOM   3126 N  N   . LEU B 1 120 ? -17.461 -9.151  16.742  1.00 10.20 ? 120 LEU B N   1 
ATOM   3127 C  CA  . LEU B 1 120 ? -18.040 -10.187 15.833  1.00 9.58  ? 120 LEU B CA  1 
ATOM   3128 C  C   . LEU B 1 120 ? -17.757 -11.574 16.423  1.00 10.42 ? 120 LEU B C   1 
ATOM   3129 O  O   . LEU B 1 120 ? -16.588 -11.824 16.819  1.00 10.57 ? 120 LEU B O   1 
ATOM   3130 C  CB  . LEU B 1 120 ? -17.277 -10.110 14.469  1.00 10.49 ? 120 LEU B CB  1 
ATOM   3131 C  CG  . LEU B 1 120 ? -17.929 -10.930 13.356  1.00 12.71 ? 120 LEU B CG  1 
ATOM   3132 C  CD1 . LEU B 1 120 ? -19.178 -10.224 12.850  1.00 13.53 ? 120 LEU B CD1 1 
ATOM   3133 C  CD2 . LEU B 1 120 ? -16.949 -11.172 12.219  1.00 14.60 ? 120 LEU B CD2 1 
ATOM   3134 N  N   . HIS B 1 121 ? -18.798 -12.418 16.465  1.00 10.74 ? 121 HIS B N   1 
ATOM   3135 C  CA  . HIS B 1 121 ? -18.550 -13.820 16.970  1.00 9.53  ? 121 HIS B CA  1 
ATOM   3136 C  C   . HIS B 1 121 ? -18.913 -14.793 15.927  1.00 9.80  ? 121 HIS B C   1 
ATOM   3137 O  O   . HIS B 1 121 ? -19.879 -14.644 15.225  1.00 11.45 ? 121 HIS B O   1 
ATOM   3138 C  CB  . HIS B 1 121 ? -19.422 -14.078 18.197  1.00 10.41 ? 121 HIS B CB  1 
ATOM   3139 C  CG  . HIS B 1 121 ? -18.926 -13.376 19.381  1.00 10.24 ? 121 HIS B CG  1 
ATOM   3140 N  ND1 . HIS B 1 121 ? -19.794 -13.098 20.442  1.00 13.82 ? 121 HIS B ND1 1 
ATOM   3141 C  CD2 . HIS B 1 121 ? -17.704 -12.822 19.686  1.00 10.72 ? 121 HIS B CD2 1 
ATOM   3142 C  CE1 . HIS B 1 121 ? -19.006 -12.445 21.393  1.00 10.02 ? 121 HIS B CE1 1 
ATOM   3143 N  NE2 . HIS B 1 121 ? -17.813 -12.251 20.928  1.00 10.71 ? 121 HIS B NE2 1 
ATOM   3144 N  N   . VAL B 1 122 ? -17.999 -15.759 15.720  1.00 11.06 ? 122 VAL B N   1 
ATOM   3145 C  CA  . VAL B 1 122 ? -18.218 -16.816 14.708  1.00 10.41 ? 122 VAL B CA  1 
ATOM   3146 C  C   . VAL B 1 122 ? -18.317 -18.184 15.522  1.00 8.79  ? 122 VAL B C   1 
ATOM   3147 O  O   . VAL B 1 122 ? -17.315 -18.553 16.219  1.00 10.48 ? 122 VAL B O   1 
ATOM   3148 C  CB  . VAL B 1 122 ? -16.989 -16.902 13.801  1.00 11.41 ? 122 VAL B CB  1 
ATOM   3149 C  CG1 . VAL B 1 122 ? -17.277 -17.847 12.624  1.00 13.70 ? 122 VAL B CG1 1 
ATOM   3150 C  CG2 . VAL B 1 122 ? -16.617 -15.508 13.268  1.00 15.00 ? 122 VAL B CG2 1 
ATOM   3151 N  N   . VAL B 1 123 ? -19.527 -18.765 15.451  1.00 10.81 ? 123 VAL B N   1 
ATOM   3152 C  CA  . VAL B 1 123 ? -19.883 -19.857 16.370  1.00 10.59 ? 123 VAL B CA  1 
ATOM   3153 C  C   . VAL B 1 123 ? -19.691 -21.209 15.602  1.00 9.17  ? 123 VAL B C   1 
ATOM   3154 O  O   . VAL B 1 123 ? -20.321 -21.333 14.548  1.00 11.78 ? 123 VAL B O   1 
ATOM   3155 C  CB  . VAL B 1 123 ? -21.293 -19.699 16.894  1.00 9.96  ? 123 VAL B CB  1 
ATOM   3156 C  CG1 . VAL B 1 123 ? -21.628 -20.754 17.971  1.00 11.29 ? 123 VAL B CG1 1 
ATOM   3157 C  CG2 . VAL B 1 123 ? -21.486 -18.280 17.506  1.00 11.09 ? 123 VAL B CG2 1 
ATOM   3158 N  N   . HIS B 1 124 ? -18.905 -22.082 16.215  1.00 10.20 ? 124 HIS B N   1 
ATOM   3159 C  CA  . HIS B 1 124 ? -18.696 -23.475 15.646  1.00 10.55 ? 124 HIS B CA  1 
ATOM   3160 C  C   . HIS B 1 124 ? -19.087 -24.535 16.649  1.00 12.70 ? 124 HIS B C   1 
ATOM   3161 O  O   . HIS B 1 124 ? -19.115 -24.288 17.856  1.00 10.80 ? 124 HIS B O   1 
ATOM   3162 C  CB  . HIS B 1 124 ? -17.250 -23.648 15.284  1.00 11.74 ? 124 HIS B CB  1 
ATOM   3163 C  CG  . HIS B 1 124 ? -16.625 -22.472 14.573  1.00 14.25 ? 124 HIS B CG  1 
ATOM   3164 N  ND1 . HIS B 1 124 ? -16.275 -21.338 15.209  1.00 13.13 ? 124 HIS B ND1 1 
ATOM   3165 C  CD2 . HIS B 1 124 ? -16.232 -22.314 13.245  1.00 13.67 ? 124 HIS B CD2 1 
ATOM   3166 C  CE1 . HIS B 1 124 ? -15.714 -20.487 14.329  1.00 13.85 ? 124 HIS B CE1 1 
ATOM   3167 N  NE2 . HIS B 1 124 ? -15.688 -21.086 13.128  1.00 13.27 ? 124 HIS B NE2 1 
ATOM   3168 N  N   . TRP B 1 125 ? -19.381 -25.750 16.147  1.00 10.49 ? 125 TRP B N   1 
ATOM   3169 C  CA  . TRP B 1 125 ? -19.740 -26.854 17.049  1.00 11.15 ? 125 TRP B CA  1 
ATOM   3170 C  C   . TRP B 1 125 ? -19.008 -28.144 16.670  1.00 11.42 ? 125 TRP B C   1 
ATOM   3171 O  O   . TRP B 1 125 ? -18.642 -28.375 15.502  1.00 12.76 ? 125 TRP B O   1 
ATOM   3172 C  CB  . TRP B 1 125 ? -21.185 -27.153 17.047  1.00 11.93 ? 125 TRP B CB  1 
ATOM   3173 C  CG  . TRP B 1 125 ? -21.795 -27.464 15.722  1.00 11.93 ? 125 TRP B CG  1 
ATOM   3174 C  CD1 . TRP B 1 125 ? -22.213 -26.588 14.720  1.00 12.14 ? 125 TRP B CD1 1 
ATOM   3175 C  CD2 . TRP B 1 125 ? -22.136 -28.797 15.216  1.00 10.75 ? 125 TRP B CD2 1 
ATOM   3176 N  NE1 . TRP B 1 125 ? -22.723 -27.245 13.638  1.00 11.96 ? 125 TRP B NE1 1 
ATOM   3177 C  CE2 . TRP B 1 125 ? -22.762 -28.613 13.928  1.00 12.38 ? 125 TRP B CE2 1 
ATOM   3178 C  CE3 . TRP B 1 125 ? -22.038 -30.098 15.783  1.00 11.98 ? 125 TRP B CE3 1 
ATOM   3179 C  CZ2 . TRP B 1 125 ? -23.259 -29.692 13.168  1.00 11.95 ? 125 TRP B CZ2 1 
ATOM   3180 C  CZ3 . TRP B 1 125 ? -22.508 -31.190 15.031  1.00 11.93 ? 125 TRP B CZ3 1 
ATOM   3181 C  CH2 . TRP B 1 125 ? -23.101 -31.000 13.775  1.00 12.35 ? 125 TRP B CH2 1 
ATOM   3182 N  N   . ASN B 1 126 ? -18.690 -28.947 17.688  1.00 11.33 ? 126 ASN B N   1 
ATOM   3183 C  CA  . ASN B 1 126 ? -17.787 -30.175 17.478  1.00 11.41 ? 126 ASN B CA  1 
ATOM   3184 C  C   . ASN B 1 126 ? -18.582 -31.342 16.821  1.00 12.18 ? 126 ASN B C   1 
ATOM   3185 O  O   . ASN B 1 126 ? -19.315 -32.056 17.543  1.00 11.81 ? 126 ASN B O   1 
ATOM   3186 C  CB  . ASN B 1 126 ? -17.339 -30.596 18.889  1.00 11.99 ? 126 ASN B CB  1 
ATOM   3187 C  CG  . ASN B 1 126 ? -16.310 -31.697 18.872  1.00 12.84 ? 126 ASN B CG  1 
ATOM   3188 O  OD1 . ASN B 1 126 ? -16.257 -32.399 17.867  1.00 12.68 ? 126 ASN B OD1 1 
ATOM   3189 N  ND2 . ASN B 1 126 ? -15.450 -31.786 19.891  1.00 15.25 ? 126 ASN B ND2 1 
ATOM   3190 N  N   . SER B 1 127 ? -18.492 -31.413 15.499  1.00 13.37 ? 127 SER B N   1 
ATOM   3191 C  CA  . SER B 1 127 ? -19.218 -32.369 14.716  1.00 12.43 ? 127 SER B CA  1 
ATOM   3192 C  C   . SER B 1 127 ? -18.473 -33.716 14.782  1.00 14.83 ? 127 SER B C   1 
ATOM   3193 O  O   . SER B 1 127 ? -19.035 -34.712 14.311  1.00 13.67 ? 127 SER B O   1 
ATOM   3194 C  CB  . SER B 1 127 ? -19.404 -31.855 13.259  1.00 12.76 ? 127 SER B CB  1 
ATOM   3195 O  OG  . SER B 1 127 ? -18.124 -31.552 12.731  1.00 14.02 ? 127 SER B OG  1 
ATOM   3196 N  N   . ASP B 1 128 ? -17.266 -33.725 15.295  1.00 13.40 ? 128 ASP B N   1 
ATOM   3197 C  CA  . ASP B 1 128 ? -16.452 -35.037 15.485  1.00 14.48 ? 128 ASP B CA  1 
ATOM   3198 C  C   . ASP B 1 128 ? -17.086 -35.842 16.633  1.00 15.85 ? 128 ASP B C   1 
ATOM   3199 O  O   . ASP B 1 128 ? -16.846 -37.050 16.754  1.00 18.34 ? 128 ASP B O   1 
ATOM   3200 C  CB  . ASP B 1 128 ? -14.996 -34.796 15.779  1.00 14.39 ? 128 ASP B CB  1 
ATOM   3201 C  CG  . ASP B 1 128 ? -14.203 -34.391 14.492  1.00 13.12 ? 128 ASP B CG  1 
ATOM   3202 O  OD1 . ASP B 1 128 ? -13.041 -34.020 14.644  1.00 17.28 ? 128 ASP B OD1 1 
ATOM   3203 O  OD2 . ASP B 1 128 ? -14.782 -34.512 13.355  1.00 16.33 ? 128 ASP B OD2 1 
ATOM   3204 N  N   . LYS B 1 129 ? -17.780 -35.196 17.539  1.00 15.19 ? 129 LYS B N   1 
ATOM   3205 C  CA  . LYS B 1 129 ? -18.307 -35.858 18.730  1.00 15.13 ? 129 LYS B CA  1 
ATOM   3206 C  C   . LYS B 1 129 ? -19.818 -35.780 18.862  1.00 14.52 ? 129 LYS B C   1 
ATOM   3207 O  O   . LYS B 1 129 ? -20.414 -36.638 19.570  1.00 13.20 ? 129 LYS B O   1 
ATOM   3208 C  CB  . LYS B 1 129 ? -17.633 -35.328 20.038  1.00 15.49 ? 129 LYS B CB  1 
ATOM   3209 C  CG  . LYS B 1 129 ? -16.215 -35.683 20.207  1.00 18.81 ? 129 LYS B CG  1 
ATOM   3210 C  CD  . LYS B 1 129 ? -15.686 -35.287 21.595  1.00 19.05 ? 129 LYS B CD  1 
ATOM   3211 C  CE  . LYS B 1 129 ? -16.481 -35.935 22.761  1.00 18.52 ? 129 LYS B CE  1 
ATOM   3212 N  NZ  . LYS B 1 129 ? -15.769 -35.625 24.081  1.00 18.47 ? 129 LYS B NZ  1 
ATOM   3213 N  N   . TYR B 1 130 ? -20.498 -34.734 18.338  1.00 13.80 ? 130 TYR B N   1 
ATOM   3214 C  CA  . TYR B 1 130 ? -21.897 -34.488 18.685  1.00 11.40 ? 130 TYR B CA  1 
ATOM   3215 C  C   . TYR B 1 130 ? -22.738 -34.453 17.415  1.00 10.70 ? 130 TYR B C   1 
ATOM   3216 O  O   . TYR B 1 130 ? -22.190 -34.068 16.377  1.00 11.88 ? 130 TYR B O   1 
ATOM   3217 C  CB  . TYR B 1 130 ? -22.066 -33.103 19.484  1.00 11.69 ? 130 TYR B CB  1 
ATOM   3218 C  CG  . TYR B 1 130 ? -21.191 -33.168 20.715  1.00 12.65 ? 130 TYR B CG  1 
ATOM   3219 C  CD1 . TYR B 1 130 ? -21.455 -34.181 21.721  1.00 13.90 ? 130 TYR B CD1 1 
ATOM   3220 C  CD2 . TYR B 1 130 ? -20.079 -32.391 20.902  1.00 12.65 ? 130 TYR B CD2 1 
ATOM   3221 C  CE1 . TYR B 1 130 ? -20.580 -34.379 22.812  1.00 13.33 ? 130 TYR B CE1 1 
ATOM   3222 C  CE2 . TYR B 1 130 ? -19.265 -32.548 21.980  1.00 12.08 ? 130 TYR B CE2 1 
ATOM   3223 C  CZ  . TYR B 1 130 ? -19.507 -33.554 22.977  1.00 13.68 ? 130 TYR B CZ  1 
ATOM   3224 O  OH  . TYR B 1 130 ? -18.720 -33.721 24.056  1.00 15.14 ? 130 TYR B OH  1 
ATOM   3225 N  N   . PRO B 1 131 ? -23.997 -34.856 17.458  1.00 12.16 ? 131 PRO B N   1 
ATOM   3226 C  CA  . PRO B 1 131 ? -24.834 -34.897 16.224  1.00 13.20 ? 131 PRO B CA  1 
ATOM   3227 C  C   . PRO B 1 131 ? -25.246 -33.581 15.628  1.00 15.73 ? 131 PRO B C   1 
ATOM   3228 O  O   . PRO B 1 131 ? -25.570 -33.519 14.441  1.00 16.74 ? 131 PRO B O   1 
ATOM   3229 C  CB  . PRO B 1 131 ? -26.051 -35.747 16.615  1.00 16.69 ? 131 PRO B CB  1 
ATOM   3230 C  CG  . PRO B 1 131 ? -26.024 -35.836 18.112  1.00 16.93 ? 131 PRO B CG  1 
ATOM   3231 C  CD  . PRO B 1 131 ? -24.733 -35.395 18.656  1.00 11.61 ? 131 PRO B CD  1 
ATOM   3232 N  N   . SER B 1 132 ? -25.273 -32.554 16.492  1.00 14.79 ? 132 SER B N   1 
ATOM   3233 C  CA  . SER B 1 132 ? -25.824 -31.230 16.138  1.00 13.45 ? 132 SER B CA  1 
ATOM   3234 C  C   . SER B 1 132 ? -25.296 -30.237 17.097  1.00 12.23 ? 132 SER B C   1 
ATOM   3235 O  O   . SER B 1 132 ? -24.698 -30.595 18.101  1.00 11.20 ? 132 SER B O   1 
ATOM   3236 C  CB  . SER B 1 132 ? -27.353 -31.086 16.095  1.00 17.51 ? 132 SER B CB  1 
ATOM   3237 O  OG  . SER B 1 132 ? -27.840 -31.118 17.393  1.00 19.26 ? 132 SER B OG  1 
ATOM   3238 N  N   . PHE B 1 133 ? -25.425 -28.964 16.709  1.00 14.68 ? 133 PHE B N   1 
ATOM   3239 C  CA  . PHE B 1 133 ? -25.001 -27.896 17.616  1.00 13.43 ? 133 PHE B CA  1 
ATOM   3240 C  C   . PHE B 1 133 ? -25.809 -27.905 18.922  1.00 14.10 ? 133 PHE B C   1 
ATOM   3241 O  O   . PHE B 1 133 ? -25.292 -27.418 19.922  1.00 14.08 ? 133 PHE B O   1 
ATOM   3242 C  CB  . PHE B 1 133 ? -25.112 -26.476 16.950  1.00 17.95 ? 133 PHE B CB  1 
ATOM   3243 C  CG  . PHE B 1 133 ? -26.522 -26.046 16.643  1.00 20.79 ? 133 PHE B CG  1 
ATOM   3244 C  CD1 . PHE B 1 133 ? -27.264 -25.342 17.574  1.00 19.07 ? 133 PHE B CD1 1 
ATOM   3245 C  CD2 . PHE B 1 133 ? -27.114 -26.307 15.393  1.00 26.83 ? 133 PHE B CD2 1 
ATOM   3246 C  CE1 . PHE B 1 133 ? -28.553 -24.923 17.278  1.00 26.39 ? 133 PHE B CE1 1 
ATOM   3247 C  CE2 . PHE B 1 133 ? -28.415 -25.898 15.093  1.00 28.99 ? 133 PHE B CE2 1 
ATOM   3248 C  CZ  . PHE B 1 133 ? -29.139 -25.241 16.058  1.00 29.56 ? 133 PHE B CZ  1 
ATOM   3249 N  N   . VAL B 1 134 ? -27.028 -28.456 18.923  1.00 14.83 ? 134 VAL B N   1 
ATOM   3250 C  CA  . VAL B 1 134 ? -27.873 -28.455 20.144  1.00 16.37 ? 134 VAL B CA  1 
ATOM   3251 C  C   . VAL B 1 134 ? -27.250 -29.288 21.183  1.00 14.65 ? 134 VAL B C   1 
ATOM   3252 O  O   . VAL B 1 134 ? -26.996 -28.858 22.367  1.00 15.87 ? 134 VAL B O   1 
ATOM   3253 C  CB  . VAL B 1 134 ? -29.318 -28.928 19.885  1.00 17.37 ? 134 VAL B CB  1 
ATOM   3254 C  CG1 . VAL B 1 134 ? -30.072 -29.099 21.228  1.00 22.52 ? 134 VAL B CG1 1 
ATOM   3255 C  CG2 . VAL B 1 134 ? -30.023 -27.907 19.033  1.00 20.88 ? 134 VAL B CG2 1 
ATOM   3256 N  N   . GLU B 1 135 ? -26.876 -30.529 20.775  1.00 13.93 ? 135 GLU B N   1 
ATOM   3257 C  CA  . GLU B 1 135 ? -26.099 -31.353 21.782  1.00 15.18 ? 135 GLU B CA  1 
ATOM   3258 C  C   . GLU B 1 135 ? -24.776 -30.758 22.183  1.00 15.62 ? 135 GLU B C   1 
ATOM   3259 O  O   . GLU B 1 135 ? -24.350 -30.849 23.347  1.00 16.57 ? 135 GLU B O   1 
ATOM   3260 C  CB  . GLU B 1 135 ? -25.910 -32.887 21.394  1.00 17.39 ? 135 GLU B CB  1 
ATOM   3261 C  CG  . GLU B 1 135 ? -27.200 -33.679 21.239  1.00 19.25 ? 135 GLU B CG  1 
ATOM   3262 C  CD  . GLU B 1 135 ? -27.896 -33.306 19.971  1.00 22.86 ? 135 GLU B CD  1 
ATOM   3263 O  OE1 . GLU B 1 135 ? -27.241 -32.655 19.071  1.00 22.44 ? 135 GLU B OE1 1 
ATOM   3264 O  OE2 . GLU B 1 135 ? -29.073 -33.672 19.865  1.00 29.06 ? 135 GLU B OE2 1 
ATOM   3265 N  N   . ALA B 1 136 ? -23.972 -30.308 21.186  1.00 12.38 ? 136 ALA B N   1 
ATOM   3266 C  CA  . ALA B 1 136 ? -22.694 -29.764 21.486  1.00 12.97 ? 136 ALA B CA  1 
ATOM   3267 C  C   . ALA B 1 136 ? -22.822 -28.602 22.480  1.00 12.76 ? 136 ALA B C   1 
ATOM   3268 O  O   . ALA B 1 136 ? -21.901 -28.463 23.268  1.00 13.23 ? 136 ALA B O   1 
ATOM   3269 C  CB  . ALA B 1 136 ? -22.023 -29.289 20.182  1.00 12.69 ? 136 ALA B CB  1 
ATOM   3270 N  N   . ALA B 1 137 ? -23.882 -27.781 22.401  1.00 13.90 ? 137 ALA B N   1 
ATOM   3271 C  CA  . ALA B 1 137 ? -23.942 -26.642 23.330  1.00 14.12 ? 137 ALA B CA  1 
ATOM   3272 C  C   . ALA B 1 137 ? -24.045 -27.044 24.774  1.00 15.68 ? 137 ALA B C   1 
ATOM   3273 O  O   . ALA B 1 137 ? -23.876 -26.197 25.642  1.00 13.74 ? 137 ALA B O   1 
ATOM   3274 C  CB  . ALA B 1 137 ? -25.157 -25.792 22.909  1.00 13.57 ? 137 ALA B CB  1 
ATOM   3275 N  N   . HIS B 1 138 ? -24.298 -28.324 25.050  1.00 15.92 ? 138 HIS B N   1 
ATOM   3276 C  CA  . HIS B 1 138 ? -24.359 -28.819 26.427  1.00 13.82 ? 138 HIS B CA  1 
ATOM   3277 C  C   . HIS B 1 138 ? -23.176 -29.572 26.924  1.00 17.42 ? 138 HIS B C   1 
ATOM   3278 O  O   . HIS B 1 138 ? -23.256 -30.253 27.968  1.00 19.37 ? 138 HIS B O   1 
ATOM   3279 C  CB  . HIS B 1 138 ? -25.695 -29.648 26.596  1.00 15.37 ? 138 HIS B CB  1 
ATOM   3280 C  CG  . HIS B 1 138 ? -26.908 -28.812 26.442  1.00 16.36 ? 138 HIS B CG  1 
ATOM   3281 N  ND1 . HIS B 1 138 ? -27.515 -28.245 27.508  1.00 19.58 ? 138 HIS B ND1 1 
ATOM   3282 C  CD2 . HIS B 1 138 ? -27.636 -28.430 25.320  1.00 17.70 ? 138 HIS B CD2 1 
ATOM   3283 C  CE1 . HIS B 1 138 ? -28.564 -27.528 27.091  1.00 18.63 ? 138 HIS B CE1 1 
ATOM   3284 N  NE2 . HIS B 1 138 ? -28.640 -27.633 25.761  1.00 21.88 ? 138 HIS B NE2 1 
ATOM   3285 N  N   . GLU B 1 139 ? -22.080 -29.485 26.202  1.00 15.45 ? 139 GLU B N   1 
ATOM   3286 C  CA  . GLU B 1 139 ? -20.840 -30.206 26.606  1.00 16.83 ? 139 GLU B CA  1 
ATOM   3287 C  C   . GLU B 1 139 ? -19.645 -29.276 26.680  1.00 14.39 ? 139 GLU B C   1 
ATOM   3288 O  O   . GLU B 1 139 ? -19.584 -28.312 25.864  1.00 11.72 ? 139 GLU B O   1 
ATOM   3289 C  CB  . GLU B 1 139 ? -20.495 -31.266 25.547  1.00 19.92 ? 139 GLU B CB  1 
ATOM   3290 C  CG  . GLU B 1 139 ? -21.682 -32.178 25.248  1.00 25.12 ? 139 GLU B CG  1 
ATOM   3291 C  CD  . GLU B 1 139 ? -21.647 -33.369 26.157  1.00 30.78 ? 139 GLU B CD  1 
ATOM   3292 O  OE1 . GLU B 1 139 ? -22.459 -34.326 25.928  1.00 35.56 ? 139 GLU B OE1 1 
ATOM   3293 O  OE2 . GLU B 1 139 ? -20.782 -33.384 27.056  1.00 27.63 ? 139 GLU B OE2 1 
ATOM   3294 N  N   . PRO B 1 140 ? -18.696 -29.472 27.620  1.00 13.87 ? 140 PRO B N   1 
ATOM   3295 C  CA  . PRO B 1 140 ? -17.567 -28.522 27.839  1.00 13.29 ? 140 PRO B CA  1 
ATOM   3296 C  C   . PRO B 1 140 ? -16.699 -28.324 26.567  1.00 13.59 ? 140 PRO B C   1 
ATOM   3297 O  O   . PRO B 1 140 ? -16.206 -27.211 26.383  1.00 14.73 ? 140 PRO B O   1 
ATOM   3298 C  CB  . PRO B 1 140 ? -16.776 -29.087 29.012  1.00 15.20 ? 140 PRO B CB  1 
ATOM   3299 C  CG  . PRO B 1 140 ? -17.859 -29.847 29.777  1.00 16.55 ? 140 PRO B CG  1 
ATOM   3300 C  CD  . PRO B 1 140 ? -18.789 -30.466 28.726  1.00 17.63 ? 140 PRO B CD  1 
ATOM   3301 N  N   . ASP B 1 141 ? -16.555 -29.380 25.741  1.00 12.79 ? 141 ASP B N   1 
ATOM   3302 C  CA  . ASP B 1 141 ? -15.816 -29.290 24.486  1.00 13.02 ? 141 ASP B CA  1 
ATOM   3303 C  C   . ASP B 1 141 ? -16.741 -29.145 23.299  1.00 11.09 ? 141 ASP B C   1 
ATOM   3304 O  O   . ASP B 1 141 ? -16.241 -29.359 22.150  1.00 12.97 ? 141 ASP B O   1 
ATOM   3305 C  CB  . ASP B 1 141 ? -14.976 -30.580 24.294  1.00 14.04 ? 141 ASP B CB  1 
ATOM   3306 C  CG  . ASP B 1 141 ? -15.851 -31.800 24.185  1.00 15.31 ? 141 ASP B CG  1 
ATOM   3307 O  OD1 . ASP B 1 141 ? -17.083 -31.774 24.448  1.00 15.10 ? 141 ASP B OD1 1 
ATOM   3308 O  OD2 . ASP B 1 141 ? -15.246 -32.901 23.940  1.00 18.23 ? 141 ASP B OD2 1 
ATOM   3309 N  N   . GLY B 1 142 ? -17.974 -28.655 23.451  1.00 10.11 ? 142 GLY B N   1 
ATOM   3310 C  CA  . GLY B 1 142 ? -18.945 -28.687 22.357  1.00 10.32 ? 142 GLY B CA  1 
ATOM   3311 C  C   . GLY B 1 142 ? -18.775 -27.560 21.339  1.00 11.05 ? 142 GLY B C   1 
ATOM   3312 O  O   . GLY B 1 142 ? -19.064 -27.717 20.186  1.00 11.36 ? 142 GLY B O   1 
ATOM   3313 N  N   . LEU B 1 143 ? -18.515 -26.348 21.863  1.00 11.43 ? 143 LEU B N   1 
ATOM   3314 C  CA  . LEU B 1 143 ? -18.543 -25.159 20.951  1.00 10.29 ? 143 LEU B CA  1 
ATOM   3315 C  C   . LEU B 1 143 ? -17.228 -24.424 20.933  1.00 10.23 ? 143 LEU B C   1 
ATOM   3316 O  O   . LEU B 1 143 ? -16.464 -24.478 21.885  1.00 10.84 ? 143 LEU B O   1 
ATOM   3317 C  CB  . LEU B 1 143 ? -19.655 -24.172 21.469  1.00 11.08 ? 143 LEU B CB  1 
ATOM   3318 C  CG  . LEU B 1 143 ? -21.084 -24.705 21.583  1.00 10.44 ? 143 LEU B CG  1 
ATOM   3319 C  CD1 . LEU B 1 143 ? -21.979 -23.502 22.017  1.00 9.95  ? 143 LEU B CD1 1 
ATOM   3320 C  CD2 . LEU B 1 143 ? -21.573 -25.285 20.276  1.00 11.11 ? 143 LEU B CD2 1 
ATOM   3321 N  N   . ALA B 1 144 ? -16.907 -23.790 19.833  1.00 10.05 ? 144 ALA B N   1 
ATOM   3322 C  CA  . ALA B 1 144 ? -15.760 -22.877 19.770  1.00 10.60 ? 144 ALA B CA  1 
ATOM   3323 C  C   . ALA B 1 144 ? -16.268 -21.598 19.127  1.00 9.00  ? 144 ALA B C   1 
ATOM   3324 O  O   . ALA B 1 144 ? -16.953 -21.627 18.114  1.00 11.12 ? 144 ALA B O   1 
ATOM   3325 C  CB  . ALA B 1 144 ? -14.648 -23.463 18.861  1.00 9.50  ? 144 ALA B CB  1 
ATOM   3326 N  N   . VAL B 1 145 ? -15.955 -20.444 19.780  1.00 9.93  ? 145 VAL B N   1 
ATOM   3327 C  CA  . VAL B 1 145 ? -16.447 -19.192 19.160  1.00 10.60 ? 145 VAL B CA  1 
ATOM   3328 C  C   . VAL B 1 145 ? -15.182 -18.324 18.973  1.00 10.34 ? 145 VAL B C   1 
ATOM   3329 O  O   . VAL B 1 145 ? -14.303 -18.156 19.898  1.00 10.69 ? 145 VAL B O   1 
ATOM   3330 C  CB  . VAL B 1 145 ? -17.371 -18.432 20.176  1.00 11.59 ? 145 VAL B CB  1 
ATOM   3331 C  CG1 . VAL B 1 145 ? -17.782 -17.144 19.488  1.00 11.11 ? 145 VAL B CG1 1 
ATOM   3332 C  CG2 . VAL B 1 145 ? -18.614 -19.261 20.445  1.00 12.53 ? 145 VAL B CG2 1 
ATOM   3333 N  N   . LEU B 1 146 ? -15.029 -17.873 17.704  1.00 11.41 ? 146 LEU B N   1 
ATOM   3334 C  CA  . LEU B 1 146 ? -13.955 -16.927 17.411  1.00 11.67 ? 146 LEU B CA  1 
ATOM   3335 C  C   . LEU B 1 146 ? -14.472 -15.496 17.604  1.00 10.60 ? 146 LEU B C   1 
ATOM   3336 O  O   . LEU B 1 146 ? -15.534 -15.215 17.037  1.00 10.82 ? 146 LEU B O   1 
ATOM   3337 C  CB  . LEU B 1 146 ? -13.477 -17.225 15.934  1.00 15.53 ? 146 LEU B CB  1 
ATOM   3338 C  CG  . LEU B 1 146 ? -12.283 -16.467 15.403  1.00 16.74 ? 146 LEU B CG  1 
ATOM   3339 C  CD1 . LEU B 1 146 ? -11.044 -16.778 16.224  1.00 20.02 ? 146 LEU B CD1 1 
ATOM   3340 C  CD2 . LEU B 1 146 ? -12.078 -17.002 13.965  1.00 20.76 ? 146 LEU B CD2 1 
ATOM   3341 N  N   . GLY B 1 147 ? -13.703 -14.652 18.292  1.00 11.06 ? 147 GLY B N   1 
ATOM   3342 C  CA  . GLY B 1 147 ? -14.165 -13.237 18.537  1.00 11.78 ? 147 GLY B CA  1 
ATOM   3343 C  C   . GLY B 1 147 ? -13.190 -12.344 17.763  1.00 11.29 ? 147 GLY B C   1 
ATOM   3344 O  O   . GLY B 1 147 ? -11.990 -12.547 17.794  1.00 13.31 ? 147 GLY B O   1 
ATOM   3345 N  N   . VAL B 1 148 ? -13.773 -11.360 17.113  1.00 10.75 ? 148 VAL B N   1 
ATOM   3346 C  CA  . VAL B 1 148 ? -12.903 -10.361 16.388  1.00 10.87 ? 148 VAL B CA  1 
ATOM   3347 C  C   . VAL B 1 148 ? -13.418 -8.983  16.837  1.00 11.19 ? 148 VAL B C   1 
ATOM   3348 O  O   . VAL B 1 148 ? -14.602 -8.725  16.715  1.00 12.05 ? 148 VAL B O   1 
ATOM   3349 C  CB  . VAL B 1 148 ? -13.164 -10.489 14.858  1.00 12.64 ? 148 VAL B CB  1 
ATOM   3350 C  CG1 . VAL B 1 148 ? -12.312 -9.473  14.115  1.00 13.96 ? 148 VAL B CG1 1 
ATOM   3351 C  CG2 . VAL B 1 148 ? -12.756 -11.919 14.336  1.00 14.70 ? 148 VAL B CG2 1 
ATOM   3352 N  N   . PHE B 1 149 ? -12.507 -8.153  17.301  1.00 9.91  ? 149 PHE B N   1 
ATOM   3353 C  CA  . PHE B 1 149 ? -12.870 -6.799  17.715  1.00 11.06 ? 149 PHE B CA  1 
ATOM   3354 C  C   . PHE B 1 149 ? -13.000 -5.889  16.511  1.00 11.87 ? 149 PHE B C   1 
ATOM   3355 O  O   . PHE B 1 149 ? -12.222 -6.052  15.538  1.00 13.57 ? 149 PHE B O   1 
ATOM   3356 C  CB  . PHE B 1 149 ? -11.720 -6.300  18.564  1.00 10.89 ? 149 PHE B CB  1 
ATOM   3357 C  CG  . PHE B 1 149 ? -11.620 -6.974  19.897  1.00 9.24  ? 149 PHE B CG  1 
ATOM   3358 C  CD1 . PHE B 1 149 ? -12.724 -6.978  20.774  1.00 9.75  ? 149 PHE B CD1 1 
ATOM   3359 C  CD2 . PHE B 1 149 ? -10.437 -7.554  20.278  1.00 10.63 ? 149 PHE B CD2 1 
ATOM   3360 C  CE1 . PHE B 1 149 ? -12.650 -7.579  22.054  1.00 10.48 ? 149 PHE B CE1 1 
ATOM   3361 C  CE2 . PHE B 1 149 ? -10.309 -8.198  21.558  1.00 10.84 ? 149 PHE B CE2 1 
ATOM   3362 C  CZ  . PHE B 1 149 ? -11.435 -8.179  22.457  1.00 11.46 ? 149 PHE B CZ  1 
ATOM   3363 N  N   . LEU B 1 150 ? -13.971 -4.984  16.610  1.00 12.18 ? 150 LEU B N   1 
ATOM   3364 C  CA  . LEU B 1 150 ? -14.131 -3.901  15.622  1.00 11.86 ? 150 LEU B CA  1 
ATOM   3365 C  C   . LEU B 1 150 ? -13.729 -2.562  16.260  1.00 13.99 ? 150 LEU B C   1 
ATOM   3366 O  O   . LEU B 1 150 ? -14.144 -2.256  17.343  1.00 12.52 ? 150 LEU B O   1 
ATOM   3367 C  CB  . LEU B 1 150 ? -15.530 -3.801  15.090  1.00 13.12 ? 150 LEU B CB  1 
ATOM   3368 C  CG  . LEU B 1 150 ? -15.997 -4.868  14.085  1.00 12.62 ? 150 LEU B CG  1 
ATOM   3369 C  CD1 . LEU B 1 150 ? -15.951 -6.272  14.701  1.00 17.11 ? 150 LEU B CD1 1 
ATOM   3370 C  CD2 . LEU B 1 150 ? -17.411 -4.602  13.487  1.00 13.47 ? 150 LEU B CD2 1 
ATOM   3371 N  N   . GLN B 1 151 ? -12.923 -1.781  15.520  1.00 13.12 ? 151 GLN B N   1 
ATOM   3372 C  CA  . GLN B 1 151 ? -12.602 -0.394  15.938  1.00 14.92 ? 151 GLN B CA  1 
ATOM   3373 C  C   . GLN B 1 151 ? -13.125 0.590   14.861  1.00 15.60 ? 151 GLN B C   1 
ATOM   3374 O  O   . GLN B 1 151 ? -13.173 0.207   13.689  1.00 16.55 ? 151 GLN B O   1 
ATOM   3375 C  CB  . GLN B 1 151 ? -11.124 -0.257  16.129  1.00 17.23 ? 151 GLN B CB  1 
ATOM   3376 C  CG  . GLN B 1 151 ? -10.333 -0.442  14.877  1.00 20.23 ? 151 GLN B CG  1 
ATOM   3377 C  CD  . GLN B 1 151 ? -8.861  -0.312  15.125  1.00 24.91 ? 151 GLN B CD  1 
ATOM   3378 O  OE1 . GLN B 1 151 ? -8.407  -0.137  16.282  1.00 25.74 ? 151 GLN B OE1 1 
ATOM   3379 N  NE2 . GLN B 1 151 ? -8.111  -0.368  14.049  1.00 24.72 ? 151 GLN B NE2 1 
ATOM   3380 N  N   . ILE B 1 152 ? -13.521 1.797   15.288  1.00 16.27 ? 152 ILE B N   1 
ATOM   3381 C  CA  . ILE B 1 152 ? -14.054 2.799   14.349  1.00 16.76 ? 152 ILE B CA  1 
ATOM   3382 C  C   . ILE B 1 152 ? -12.875 3.199   13.470  1.00 18.01 ? 152 ILE B C   1 
ATOM   3383 O  O   . ILE B 1 152 ? -11.821 3.524   14.003  1.00 20.78 ? 152 ILE B O   1 
ATOM   3384 C  CB  . ILE B 1 152 ? -14.647 4.047   15.121  1.00 17.39 ? 152 ILE B CB  1 
ATOM   3385 C  CG1 . ILE B 1 152 ? -15.832 3.683   15.976  1.00 17.33 ? 152 ILE B CG1 1 
ATOM   3386 C  CG2 . ILE B 1 152 ? -14.879 5.254   14.188  1.00 21.70 ? 152 ILE B CG2 1 
ATOM   3387 C  CD1 . ILE B 1 152 ? -16.972 3.027   15.243  1.00 17.60 ? 152 ILE B CD1 1 
ATOM   3388 N  N   . GLY B 1 153 ? -13.114 3.197   12.162  1.00 19.46 ? 153 GLY B N   1 
ATOM   3389 C  CA  . GLY B 1 153 ? -12.101 3.421   11.169  1.00 20.94 ? 153 GLY B CA  1 
ATOM   3390 C  C   . GLY B 1 153 ? -12.753 3.764   9.841   1.00 22.16 ? 153 GLY B C   1 
ATOM   3391 O  O   . GLY B 1 153 ? -13.887 4.334   9.780   1.00 21.45 ? 153 GLY B O   1 
ATOM   3392 N  N   . GLU B 1 154 ? -12.048 3.376   8.792   1.00 21.77 ? 154 GLU B N   1 
ATOM   3393 C  CA  . GLU B 1 154 ? -12.565 3.511   7.426   1.00 22.74 ? 154 GLU B CA  1 
ATOM   3394 C  C   . GLU B 1 154 ? -13.807 2.600   7.286   1.00 22.26 ? 154 GLU B C   1 
ATOM   3395 O  O   . GLU B 1 154 ? -13.919 1.569   7.938   1.00 20.98 ? 154 GLU B O   1 
ATOM   3396 C  CB  . GLU B 1 154 ? -11.475 3.122   6.405   1.00 23.32 ? 154 GLU B CB  1 
ATOM   3397 C  CG  . GLU B 1 154 ? -10.230 4.009   6.559   1.00 27.94 ? 154 GLU B CG  1 
ATOM   3398 C  CD  . GLU B 1 154 ? -9.100  3.614   5.617   1.00 34.07 ? 154 GLU B CD  1 
ATOM   3399 O  OE1 . GLU B 1 154 ? -9.365  2.843   4.667   1.00 38.21 ? 154 GLU B OE1 1 
ATOM   3400 O  OE2 . GLU B 1 154 ? -7.929  4.083   5.850   1.00 39.08 ? 154 GLU B OE2 1 
ATOM   3401 N  N   . PRO B 1 155 ? -14.768 2.962   6.419   1.00 20.39 ? 155 PRO B N   1 
ATOM   3402 C  CA  . PRO B 1 155 ? -15.835 2.015   6.088   1.00 23.63 ? 155 PRO B CA  1 
ATOM   3403 C  C   . PRO B 1 155 ? -15.221 0.671   5.677   1.00 21.09 ? 155 PRO B C   1 
ATOM   3404 O  O   . PRO B 1 155 ? -14.183 0.619   4.959   1.00 25.01 ? 155 PRO B O   1 
ATOM   3405 C  CB  . PRO B 1 155 ? -16.490 2.594   4.833   1.00 22.24 ? 155 PRO B CB  1 
ATOM   3406 C  CG  . PRO B 1 155 ? -15.998 4.026   4.721   1.00 25.77 ? 155 PRO B CG  1 
ATOM   3407 C  CD  . PRO B 1 155 ? -14.790 4.209   5.609   1.00 21.22 ? 155 PRO B CD  1 
ATOM   3408 N  N   . ASN B 1 156 ? -15.910 -0.383  6.049   1.00 23.65 ? 156 ASN B N   1 
ATOM   3409 C  CA  . ASN B 1 156 ? -15.520 -1.748  5.718   1.00 24.14 ? 156 ASN B CA  1 
ATOM   3410 C  C   . ASN B 1 156 ? -16.406 -2.260  4.607   1.00 26.27 ? 156 ASN B C   1 
ATOM   3411 O  O   . ASN B 1 156 ? -17.625 -2.460  4.805   1.00 24.20 ? 156 ASN B O   1 
ATOM   3412 C  CB  . ASN B 1 156 ? -15.636 -2.592  6.983   1.00 26.51 ? 156 ASN B CB  1 
ATOM   3413 C  CG  . ASN B 1 156 ? -15.065 -3.980  6.824   1.00 27.95 ? 156 ASN B CG  1 
ATOM   3414 O  OD1 . ASN B 1 156 ? -15.451 -4.711  5.920   1.00 32.28 ? 156 ASN B OD1 1 
ATOM   3415 N  ND2 . ASN B 1 156 ? -14.141 -4.354  7.713   1.00 23.54 ? 156 ASN B ND2 1 
ATOM   3416 N  N   . SER B 1 157 ? -15.808 -2.466  3.423   1.00 29.53 ? 157 SER B N   1 
ATOM   3417 C  CA  . SER B 1 157 ? -16.617 -2.869  2.264   1.00 34.57 ? 157 SER B CA  1 
ATOM   3418 C  C   . SER B 1 157 ? -17.369 -4.212  2.463   1.00 29.90 ? 157 SER B C   1 
ATOM   3419 O  O   . SER B 1 157 ? -18.483 -4.386  1.951   1.00 31.66 ? 157 SER B O   1 
ATOM   3420 C  CB  . SER B 1 157 ? -15.782 -2.872  0.985   1.00 34.25 ? 157 SER B CB  1 
ATOM   3421 O  OG  . SER B 1 157 ? -14.489 -3.383  1.235   1.00 42.35 ? 157 SER B OG  1 
ATOM   3422 N  N   . GLN B 1 158 ? -16.846 -5.118  3.286   1.00 37.21 ? 158 GLN B N   1 
ATOM   3423 C  CA  . GLN B 1 158 ? -17.612 -6.415  3.515   1.00 33.79 ? 158 GLN B CA  1 
ATOM   3424 C  C   . GLN B 1 158 ? -18.693 -6.487  4.648   1.00 38.62 ? 158 GLN B C   1 
ATOM   3425 O  O   . GLN B 1 158 ? -19.756 -7.168  4.543   1.00 37.87 ? 158 GLN B O   1 
ATOM   3426 C  CB  . GLN B 1 158 ? -16.714 -7.661  3.524   1.00 45.12 ? 158 GLN B CB  1 
ATOM   3427 C  CG  . GLN B 1 158 ? -15.296 -7.462  4.050   1.00 49.91 ? 158 GLN B CG  1 
ATOM   3428 C  CD  . GLN B 1 158 ? -14.306 -6.940  3.008   1.00 56.37 ? 158 GLN B CD  1 
ATOM   3429 O  OE1 . GLN B 1 158 ? -13.455 -6.098  3.326   1.00 63.39 ? 158 GLN B OE1 1 
ATOM   3430 N  NE2 . GLN B 1 158 ? -14.412 -7.427  1.763   1.00 52.61 ? 158 GLN B NE2 1 
ATOM   3431 N  N   . LEU B 1 159 ? -18.484 -5.682  5.678   1.00 29.36 ? 159 LEU B N   1 
ATOM   3432 C  CA  . LEU B 1 159 ? -19.567 -5.347  6.569   1.00 22.33 ? 159 LEU B CA  1 
ATOM   3433 C  C   . LEU B 1 159 ? -20.687 -4.656  5.842   1.00 21.87 ? 159 LEU B C   1 
ATOM   3434 O  O   . LEU B 1 159 ? -21.804 -4.620  6.288   1.00 19.19 ? 159 LEU B O   1 
ATOM   3435 C  CB  . LEU B 1 159 ? -19.073 -4.494  7.769   1.00 19.98 ? 159 LEU B CB  1 
ATOM   3436 C  CG  . LEU B 1 159 ? -18.195 -5.181  8.757   1.00 23.32 ? 159 LEU B CG  1 
ATOM   3437 C  CD1 . LEU B 1 159 ? -17.502 -4.204  9.748   1.00 20.41 ? 159 LEU B CD1 1 
ATOM   3438 C  CD2 . LEU B 1 159 ? -18.973 -6.237  9.470   1.00 23.53 ? 159 LEU B CD2 1 
ATOM   3439 N  N   . GLN B 1 160 ? -20.351 -3.973  4.743   1.00 19.49 ? 160 GLN B N   1 
ATOM   3440 C  CA  . GLN B 1 160 ? -21.393 -3.302  3.994   1.00 21.03 ? 160 GLN B CA  1 
ATOM   3441 C  C   . GLN B 1 160 ? -22.440 -4.264  3.434   1.00 17.71 ? 160 GLN B C   1 
ATOM   3442 O  O   . GLN B 1 160 ? -23.624 -3.857  3.468   1.00 21.38 ? 160 GLN B O   1 
ATOM   3443 C  CB  . GLN B 1 160 ? -20.774 -2.417  2.862   1.00 20.26 ? 160 GLN B CB  1 
ATOM   3444 C  CG  . GLN B 1 160 ? -21.836 -1.504  2.232   1.00 24.47 ? 160 GLN B CG  1 
ATOM   3445 C  CD  . GLN B 1 160 ? -22.259 -0.368  3.096   1.00 21.27 ? 160 GLN B CD  1 
ATOM   3446 O  OE1 . GLN B 1 160 ? -21.446 0.192   3.849   1.00 20.82 ? 160 GLN B OE1 1 
ATOM   3447 N  NE2 . GLN B 1 160 ? -23.487 0.085   2.941   1.00 22.00 ? 160 GLN B NE2 1 
ATOM   3448 N  N   . LYS B 1 161 ? -22.045 -5.474  3.022   1.00 17.95 ? 161 LYS B N   1 
ATOM   3449 C  CA  . LYS B 1 161 ? -23.007 -6.523  2.552   1.00 20.05 ? 161 LYS B CA  1 
ATOM   3450 C  C   . LYS B 1 161 ? -24.066 -6.748  3.702   1.00 20.57 ? 161 LYS B C   1 
ATOM   3451 O  O   . LYS B 1 161 ? -25.261 -6.798  3.451   1.00 18.58 ? 161 LYS B O   1 
ATOM   3452 C  CB  . LYS B 1 161 ? -22.254 -7.811  2.142   1.00 24.59 ? 161 LYS B CB  1 
ATOM   3453 C  CG  . LYS B 1 161 ? -23.084 -8.954  1.513   1.00 26.32 ? 161 LYS B CG  1 
ATOM   3454 C  CD  . LYS B 1 161 ? -22.233 -10.181 1.171   1.00 27.71 ? 161 LYS B CD  1 
ATOM   3455 C  CE  . LYS B 1 161 ? -23.082 -11.476 0.933   1.00 27.64 ? 161 LYS B CE  1 
ATOM   3456 N  NZ  . LYS B 1 161 ? -23.935 -11.538 -0.354  1.00 26.51 ? 161 LYS B NZ  1 
ATOM   3457 N  N   . ILE B 1 162 ? -23.614 -6.773  4.967   1.00 18.41 ? 162 ILE B N   1 
ATOM   3458 C  CA  . ILE B 1 162 ? -24.555 -6.924  6.053   1.00 16.68 ? 162 ILE B CA  1 
ATOM   3459 C  C   . ILE B 1 162 ? -25.437 -5.718  6.277   1.00 18.12 ? 162 ILE B C   1 
ATOM   3460 O  O   . ILE B 1 162 ? -26.642 -5.830  6.462   1.00 18.10 ? 162 ILE B O   1 
ATOM   3461 C  CB  . ILE B 1 162 ? -23.769 -7.267  7.375   1.00 15.77 ? 162 ILE B CB  1 
ATOM   3462 C  CG1 . ILE B 1 162 ? -23.028 -8.589  7.202   1.00 15.60 ? 162 ILE B CG1 1 
ATOM   3463 C  CG2 . ILE B 1 162 ? -24.745 -7.259  8.610   1.00 14.06 ? 162 ILE B CG2 1 
ATOM   3464 C  CD1 . ILE B 1 162 ? -22.041 -8.855  8.355   1.00 16.92 ? 162 ILE B CD1 1 
ATOM   3465 N  N   . THR B 1 163 ? -24.860 -4.485  6.368   1.00 16.58 ? 163 THR B N   1 
ATOM   3466 C  CA  . THR B 1 163 ? -25.699 -3.358  6.704   1.00 19.23 ? 163 THR B CA  1 
ATOM   3467 C  C   . THR B 1 163 ? -26.819 -3.048  5.608   1.00 15.57 ? 163 THR B C   1 
ATOM   3468 O  O   . THR B 1 163 ? -27.910 -2.619  5.972   1.00 19.61 ? 163 THR B O   1 
ATOM   3469 C  CB  . THR B 1 163 ? -24.910 -2.094  7.100   1.00 20.65 ? 163 THR B CB  1 
ATOM   3470 O  OG1 . THR B 1 163 ? -24.063 -1.787  5.997   1.00 24.44 ? 163 THR B OG1 1 
ATOM   3471 C  CG2 . THR B 1 163 ? -24.052 -2.251  8.422   1.00 23.50 ? 163 THR B CG2 1 
ATOM   3472 N  N   . ASP B 1 164 ? -26.490 -3.396  4.356   1.00 20.20 ? 164 ASP B N   1 
ATOM   3473 C  CA  . ASP B 1 164 ? -27.428 -3.240  3.224   1.00 20.32 ? 164 ASP B CA  1 
ATOM   3474 C  C   . ASP B 1 164 ? -28.710 -4.058  3.476   1.00 23.45 ? 164 ASP B C   1 
ATOM   3475 O  O   . ASP B 1 164 ? -29.787 -3.734  2.953   1.00 25.76 ? 164 ASP B O   1 
ATOM   3476 C  CB  . ASP B 1 164 ? -26.797 -3.669  1.906   1.00 21.99 ? 164 ASP B CB  1 
ATOM   3477 C  CG  . ASP B 1 164 ? -25.830 -2.630  1.333   1.00 22.98 ? 164 ASP B CG  1 
ATOM   3478 O  OD1 . ASP B 1 164 ? -25.813 -1.460  1.804   1.00 22.14 ? 164 ASP B OD1 1 
ATOM   3479 O  OD2 . ASP B 1 164 ? -25.080 -3.033  0.413   1.00 23.58 ? 164 ASP B OD2 1 
ATOM   3480 N  N   . THR B 1 165 ? -28.600 -5.154  4.232   1.00 19.38 ? 165 THR B N   1 
ATOM   3481 C  CA  . THR B 1 165 ? -29.809 -5.957  4.535   1.00 19.32 ? 165 THR B CA  1 
ATOM   3482 C  C   . THR B 1 165 ? -30.668 -5.535  5.705   1.00 18.95 ? 165 THR B C   1 
ATOM   3483 O  O   . THR B 1 165 ? -31.807 -5.968  5.892   1.00 19.86 ? 165 THR B O   1 
ATOM   3484 C  CB  . THR B 1 165 ? -29.441 -7.425  4.770   1.00 17.69 ? 165 THR B CB  1 
ATOM   3485 O  OG1 . THR B 1 165 ? -28.781 -7.600  6.061   1.00 18.86 ? 165 THR B OG1 1 
ATOM   3486 C  CG2 . THR B 1 165 ? -28.609 -8.002  3.685   1.00 20.18 ? 165 THR B CG2 1 
ATOM   3487 N  N   . LEU B 1 166 ? -30.132 -4.656  6.567   1.00 18.18 ? 166 LEU B N   1 
ATOM   3488 C  CA  . LEU B 1 166 ? -30.807 -4.520  7.842   1.00 20.78 ? 166 LEU B CA  1 
ATOM   3489 C  C   . LEU B 1 166 ? -32.159 -3.838  7.774   1.00 18.94 ? 166 LEU B C   1 
ATOM   3490 O  O   . LEU B 1 166 ? -33.034 -4.028  8.624   1.00 22.34 ? 166 LEU B O   1 
ATOM   3491 C  CB  . LEU B 1 166 ? -29.905 -3.717  8.815   1.00 21.24 ? 166 LEU B CB  1 
ATOM   3492 C  CG  . LEU B 1 166 ? -28.524 -4.322  9.045   1.00 22.79 ? 166 LEU B CG  1 
ATOM   3493 C  CD1 . LEU B 1 166 ? -27.739 -3.346  9.928   1.00 23.16 ? 166 LEU B CD1 1 
ATOM   3494 C  CD2 . LEU B 1 166 ? -28.655 -5.680  9.738   1.00 23.11 ? 166 LEU B CD2 1 
ATOM   3495 N  N   . ASP B 1 167 ? -32.388 -3.049  6.724   1.00 23.24 ? 167 ASP B N   1 
ATOM   3496 C  CA  . ASP B 1 167 ? -33.699 -2.469  6.552   1.00 25.80 ? 167 ASP B CA  1 
ATOM   3497 C  C   . ASP B 1 167 ? -34.749 -3.569  6.269   1.00 23.30 ? 167 ASP B C   1 
ATOM   3498 O  O   . ASP B 1 167 ? -35.888 -3.435  6.722   1.00 25.61 ? 167 ASP B O   1 
ATOM   3499 C  CB  . ASP B 1 167 ? -33.704 -1.451  5.384   1.00 31.71 ? 167 ASP B CB  1 
ATOM   3500 C  CG  . ASP B 1 167 ? -33.158 -0.048  5.784   1.00 33.47 ? 167 ASP B CG  1 
ATOM   3501 O  OD1 . ASP B 1 167 ? -33.184 0.362   6.983   1.00 33.90 ? 167 ASP B OD1 1 
ATOM   3502 O  OD2 . ASP B 1 167 ? -32.714 0.647   4.861   1.00 37.78 ? 167 ASP B OD2 1 
ATOM   3503 N  N   A SER B 1 168 ? -34.345 -4.639  5.565   0.50 21.48 ? 168 SER B N   1 
ATOM   3504 N  N   B SER B 1 168 ? -34.365 -4.648  5.582   0.50 22.04 ? 168 SER B N   1 
ATOM   3505 C  CA  A SER B 1 168 ? -35.260 -5.774  5.283   0.50 20.91 ? 168 SER B CA  1 
ATOM   3506 C  CA  B SER B 1 168 ? -35.338 -5.728  5.312   0.50 21.86 ? 168 SER B CA  1 
ATOM   3507 C  C   A SER B 1 168 ? -35.600 -6.606  6.550   0.50 20.40 ? 168 SER B C   1 
ATOM   3508 C  C   B SER B 1 168 ? -35.413 -6.799  6.431   0.50 20.52 ? 168 SER B C   1 
ATOM   3509 O  O   A SER B 1 168 ? -36.676 -7.230  6.651   0.50 17.00 ? 168 SER B O   1 
ATOM   3510 O  O   B SER B 1 168 ? -36.135 -7.804  6.313   0.50 19.62 ? 168 SER B O   1 
ATOM   3511 C  CB  A SER B 1 168 ? -34.727 -6.667  4.139   0.50 20.21 ? 168 SER B CB  1 
ATOM   3512 C  CB  B SER B 1 168 ? -35.063 -6.386  3.967   0.50 21.87 ? 168 SER B CB  1 
ATOM   3513 O  OG  A SER B 1 168 ? -33.566 -7.420  4.484   0.50 18.70 ? 168 SER B OG  1 
ATOM   3514 O  OG  B SER B 1 168 ? -34.526 -5.458  3.041   0.50 21.04 ? 168 SER B OG  1 
ATOM   3515 N  N   . ILE B 1 169 ? -34.697 -6.562  7.540   1.00 19.67 ? 169 ILE B N   1 
ATOM   3516 C  CA  . ILE B 1 169 ? -34.848 -7.413  8.745   1.00 19.30 ? 169 ILE B CA  1 
ATOM   3517 C  C   . ILE B 1 169 ? -35.009 -6.559  10.054  1.00 20.20 ? 169 ILE B C   1 
ATOM   3518 O  O   . ILE B 1 169 ? -34.540 -6.957  11.144  1.00 17.39 ? 169 ILE B O   1 
ATOM   3519 C  CB  . ILE B 1 169 ? -33.753 -8.476  8.894   1.00 21.15 ? 169 ILE B CB  1 
ATOM   3520 C  CG1 . ILE B 1 169 ? -32.390 -7.848  9.116   1.00 19.32 ? 169 ILE B CG1 1 
ATOM   3521 C  CG2 . ILE B 1 169 ? -33.572 -9.394  7.661   1.00 17.50 ? 169 ILE B CG2 1 
ATOM   3522 C  CD1 . ILE B 1 169 ? -31.342 -8.882  9.662   1.00 20.34 ? 169 ILE B CD1 1 
ATOM   3523 N  N   . LYS B 1 170 ? -35.688 -5.422  9.959   1.00 20.79 ? 170 LYS B N   1 
ATOM   3524 C  CA  . LYS B 1 170 ? -35.790 -4.503  11.106  1.00 20.80 ? 170 LYS B CA  1 
ATOM   3525 C  C   . LYS B 1 170 ? -36.479 -5.087  12.322  1.00 20.89 ? 170 LYS B C   1 
ATOM   3526 O  O   . LYS B 1 170 ? -35.982 -4.952  13.389  1.00 20.28 ? 170 LYS B O   1 
ATOM   3527 C  CB  . LYS B 1 170 ? -36.412 -3.140  10.705  1.00 27.88 ? 170 LYS B CB  1 
ATOM   3528 C  CG  . LYS B 1 170 ? -36.457 -2.107  11.815  1.00 29.37 ? 170 LYS B CG  1 
ATOM   3529 C  CD  . LYS B 1 170 ? -37.205 -0.815  11.416  1.00 39.00 ? 170 LYS B CD  1 
ATOM   3530 C  CE  . LYS B 1 170 ? -36.880 0.414   12.294  1.00 40.06 ? 170 LYS B CE  1 
ATOM   3531 N  NZ  . LYS B 1 170 ? -35.459 0.854   12.327  1.00 48.28 ? 170 LYS B NZ  1 
ATOM   3532 N  N   . GLU B 1 171 ? -37.590 -5.783  12.114  1.00 21.24 ? 171 GLU B N   1 
ATOM   3533 C  CA  . GLU B 1 171 ? -38.379 -6.329  13.192  1.00 20.85 ? 171 GLU B CA  1 
ATOM   3534 C  C   . GLU B 1 171 ? -37.851 -7.729  13.560  1.00 20.33 ? 171 GLU B C   1 
ATOM   3535 O  O   . GLU B 1 171 ? -37.365 -8.502  12.668  1.00 18.95 ? 171 GLU B O   1 
ATOM   3536 C  CB  . GLU B 1 171 ? -39.892 -6.453  12.821  1.00 26.20 ? 171 GLU B CB  1 
ATOM   3537 C  CG  . GLU B 1 171 ? -40.574 -5.180  12.231  1.00 30.69 ? 171 GLU B CG  1 
ATOM   3538 C  CD  . GLU B 1 171 ? -40.055 -4.746  10.841  1.00 35.52 ? 171 GLU B CD  1 
ATOM   3539 O  OE1 . GLU B 1 171 ? -40.136 -3.517  10.591  1.00 51.77 ? 171 GLU B OE1 1 
ATOM   3540 O  OE2 . GLU B 1 171 ? -39.498 -5.549  9.996   1.00 33.18 ? 171 GLU B OE2 1 
ATOM   3541 N  N   . LYS B 1 172 ? -37.928 -8.066  14.853  1.00 18.03 ? 172 LYS B N   1 
ATOM   3542 C  CA  . LYS B 1 172 ? -37.522 -9.369  15.346  1.00 17.80 ? 172 LYS B CA  1 
ATOM   3543 C  C   . LYS B 1 172 ? -38.243 -10.478 14.581  1.00 17.66 ? 172 LYS B C   1 
ATOM   3544 O  O   . LYS B 1 172 ? -39.478 -10.367 14.336  1.00 18.26 ? 172 LYS B O   1 
ATOM   3545 C  CB  . LYS B 1 172 ? -37.904 -9.471  16.870  1.00 19.06 ? 172 LYS B CB  1 
ATOM   3546 C  CG  . LYS B 1 172 ? -37.607 -10.804 17.487  1.00 19.76 ? 172 LYS B CG  1 
ATOM   3547 C  CD  . LYS B 1 172 ? -38.130 -10.905 18.920  1.00 23.30 ? 172 LYS B CD  1 
ATOM   3548 C  CE  . LYS B 1 172 ? -37.752 -12.220 19.538  1.00 22.78 ? 172 LYS B CE  1 
ATOM   3549 N  NZ  . LYS B 1 172 ? -38.218 -12.292 20.955  1.00 34.26 ? 172 LYS B NZ  1 
ATOM   3550 N  N   . GLY B 1 173 ? -37.499 -11.488 14.167  1.00 19.62 ? 173 GLY B N   1 
ATOM   3551 C  CA  . GLY B 1 173 ? -38.121 -12.666 13.437  1.00 16.39 ? 173 GLY B CA  1 
ATOM   3552 C  C   . GLY B 1 173 ? -37.959 -12.552 11.921  1.00 19.33 ? 173 GLY B C   1 
ATOM   3553 O  O   . GLY B 1 173 ? -38.117 -13.607 11.209  1.00 21.92 ? 173 GLY B O   1 
ATOM   3554 N  N   . LYS B 1 174 ? -37.687 -11.365 11.369  1.00 18.10 ? 174 LYS B N   1 
ATOM   3555 C  CA  . LYS B 1 174 ? -37.523 -11.270 9.886   1.00 22.16 ? 174 LYS B CA  1 
ATOM   3556 C  C   . LYS B 1 174 ? -36.171 -11.801 9.427   1.00 21.22 ? 174 LYS B C   1 
ATOM   3557 O  O   . LYS B 1 174 ? -35.168 -11.799 10.156  1.00 16.71 ? 174 LYS B O   1 
ATOM   3558 C  CB  . LYS B 1 174 ? -37.669 -9.817  9.427   1.00 22.27 ? 174 LYS B CB  1 
ATOM   3559 C  CG  . LYS B 1 174 ? -38.983 -9.200  9.811   1.00 25.55 ? 174 LYS B CG  1 
ATOM   3560 C  CD  . LYS B 1 174 ? -40.121 -9.612  8.902   1.00 32.76 ? 174 LYS B CD  1 
ATOM   3561 C  CE  . LYS B 1 174 ? -41.389 -8.837  9.270   1.00 32.96 ? 174 LYS B CE  1 
ATOM   3562 N  NZ  . LYS B 1 174 ? -41.205 -7.467  8.706   1.00 41.57 ? 174 LYS B NZ  1 
ATOM   3563 N  N   . GLN B 1 175 ? -36.126 -12.274 8.175   1.00 21.61 ? 175 GLN B N   1 
ATOM   3564 C  CA  . GLN B 1 175 ? -34.845 -12.722 7.643   1.00 19.32 ? 175 GLN B CA  1 
ATOM   3565 C  C   . GLN B 1 175 ? -34.785 -12.492 6.157   1.00 21.79 ? 175 GLN B C   1 
ATOM   3566 O  O   . GLN B 1 175 ? -35.781 -12.175 5.559   1.00 22.36 ? 175 GLN B O   1 
ATOM   3567 C  CB  . GLN B 1 175 ? -34.566 -14.214 8.035   1.00 20.02 ? 175 GLN B CB  1 
ATOM   3568 C  CG  . GLN B 1 175 ? -35.683 -15.146 7.493   1.00 18.35 ? 175 GLN B CG  1 
ATOM   3569 C  CD  . GLN B 1 175 ? -35.327 -16.617 7.698   1.00 21.64 ? 175 GLN B CD  1 
ATOM   3570 O  OE1 . GLN B 1 175 ? -35.093 -17.342 6.703   1.00 28.41 ? 175 GLN B OE1 1 
ATOM   3571 N  NE2 . GLN B 1 175 ? -35.172 -17.066 8.952   1.00 20.07 ? 175 GLN B NE2 1 
ATOM   3572 N  N   . THR B 1 176 ? -33.621 -12.703 5.582   1.00 21.25 ? 176 THR B N   1 
ATOM   3573 C  CA  . THR B 1 176 ? -33.447 -12.643 4.106   1.00 22.80 ? 176 THR B CA  1 
ATOM   3574 C  C   . THR B 1 176 ? -32.260 -13.446 3.636   1.00 22.84 ? 176 THR B C   1 
ATOM   3575 O  O   . THR B 1 176 ? -31.362 -13.789 4.427   1.00 21.77 ? 176 THR B O   1 
ATOM   3576 C  CB  . THR B 1 176 ? -33.498 -11.227 3.565   1.00 23.93 ? 176 THR B CB  1 
ATOM   3577 O  OG1 . THR B 1 176 ? -33.489 -11.299 2.133   1.00 24.37 ? 176 THR B OG1 1 
ATOM   3578 C  CG2 . THR B 1 176 ? -32.179 -10.505 4.004   1.00 25.25 ? 176 THR B CG2 1 
ATOM   3579 N  N   . ARG B 1 177 ? -32.298 -13.912 2.369   1.00 20.38 ? 177 ARG B N   1 
ATOM   3580 C  CA  . ARG B 1 177 ? -31.196 -14.700 1.738   1.00 22.32 ? 177 ARG B CA  1 
ATOM   3581 C  C   . ARG B 1 177 ? -29.856 -13.978 1.872   1.00 21.35 ? 177 ARG B C   1 
ATOM   3582 O  O   . ARG B 1 177 ? -29.768 -12.717 1.733   1.00 18.67 ? 177 ARG B O   1 
ATOM   3583 C  CB  . ARG B 1 177 ? -31.573 -14.940 0.240   1.00 26.13 ? 177 ARG B CB  1 
ATOM   3584 C  CG  . ARG B 1 177 ? -30.506 -15.649 -0.610  1.00 25.45 ? 177 ARG B CG  1 
ATOM   3585 C  CD  . ARG B 1 177 ? -30.198 -17.042 -0.076  1.00 27.69 ? 177 ARG B CD  1 
ATOM   3586 N  NE  . ARG B 1 177 ? -29.422 -17.894 -1.010  1.00 30.44 ? 177 ARG B NE  1 
ATOM   3587 C  CZ  . ARG B 1 177 ? -28.833 -19.039 -0.645  1.00 26.73 ? 177 ARG B CZ  1 
ATOM   3588 N  NH1 . ARG B 1 177 ? -28.889 -19.445 0.623   1.00 25.75 ? 177 ARG B NH1 1 
ATOM   3589 N  NH2 . ARG B 1 177 ? -28.205 -19.800 -1.551  1.00 29.96 ? 177 ARG B NH2 1 
ATOM   3590 N  N   . PHE B 1 178 ? -28.819 -14.769 2.165   1.00 21.40 ? 178 PHE B N   1 
ATOM   3591 C  CA  . PHE B 1 178 ? -27.515 -14.174 2.303   1.00 19.00 ? 178 PHE B CA  1 
ATOM   3592 C  C   . PHE B 1 178 ? -26.490 -15.216 2.030   1.00 22.80 ? 178 PHE B C   1 
ATOM   3593 O  O   . PHE B 1 178 ? -26.225 -16.056 2.896   1.00 22.46 ? 178 PHE B O   1 
ATOM   3594 C  CB  . PHE B 1 178 ? -27.429 -13.719 3.817   1.00 20.65 ? 178 PHE B CB  1 
ATOM   3595 C  CG  . PHE B 1 178 ? -26.320 -12.723 4.132   1.00 18.81 ? 178 PHE B CG  1 
ATOM   3596 C  CD1 . PHE B 1 178 ? -26.516 -11.390 3.869   1.00 17.84 ? 178 PHE B CD1 1 
ATOM   3597 C  CD2 . PHE B 1 178 ? -25.166 -13.133 4.711   1.00 20.38 ? 178 PHE B CD2 1 
ATOM   3598 C  CE1 . PHE B 1 178 ? -25.452 -10.447 4.081   1.00 17.62 ? 178 PHE B CE1 1 
ATOM   3599 C  CE2 . PHE B 1 178 ? -24.104 -12.204 4.973   1.00 18.69 ? 178 PHE B CE2 1 
ATOM   3600 C  CZ  . PHE B 1 178 ? -24.279 -10.880 4.688   1.00 16.67 ? 178 PHE B CZ  1 
ATOM   3601 N  N   . THR B 1 179 ? -25.947 -15.187 0.831   1.00 22.59 ? 179 THR B N   1 
ATOM   3602 C  CA  . THR B 1 179 ? -24.940 -16.168 0.463   1.00 24.07 ? 179 THR B CA  1 
ATOM   3603 C  C   . THR B 1 179 ? -23.773 -15.514 -0.260  1.00 22.05 ? 179 THR B C   1 
ATOM   3604 O  O   . THR B 1 179 ? -23.733 -14.268 -0.503  1.00 22.63 ? 179 THR B O   1 
ATOM   3605 C  CB  . THR B 1 179 ? -25.512 -17.366 -0.349  1.00 25.46 ? 179 THR B CB  1 
ATOM   3606 O  OG1 . THR B 1 179 ? -24.551 -18.440 -0.333  1.00 25.24 ? 179 THR B OG1 1 
ATOM   3607 C  CG2 . THR B 1 179 ? -25.863 -16.953 -1.802  1.00 27.63 ? 179 THR B CG2 1 
ATOM   3608 N  N   . ASN B 1 180 ? -22.778 -16.326 -0.596  1.00 24.60 ? 180 ASN B N   1 
ATOM   3609 C  CA  . ASN B 1 180 ? -21.558 -15.759 -1.232  1.00 25.93 ? 180 ASN B CA  1 
ATOM   3610 C  C   . ASN B 1 180 ? -20.881 -14.735 -0.290  1.00 25.15 ? 180 ASN B C   1 
ATOM   3611 O  O   . ASN B 1 180 ? -20.541 -13.613 -0.675  1.00 24.10 ? 180 ASN B O   1 
ATOM   3612 C  CB  . ASN B 1 180 ? -21.938 -15.139 -2.619  1.00 30.38 ? 180 ASN B CB  1 
ATOM   3613 C  CG  . ASN B 1 180 ? -22.492 -16.195 -3.579  1.00 39.82 ? 180 ASN B CG  1 
ATOM   3614 O  OD1 . ASN B 1 180 ? -22.069 -17.382 -3.547  1.00 38.37 ? 180 ASN B OD1 1 
ATOM   3615 N  ND2 . ASN B 1 180 ? -23.461 -15.789 -4.417  1.00 44.43 ? 180 ASN B ND2 1 
ATOM   3616 N  N   . PHE B 1 181 ? -20.733 -15.099 0.994   1.00 25.55 ? 181 PHE B N   1 
ATOM   3617 C  CA  . PHE B 1 181 ? -20.351 -14.160 2.096   1.00 23.54 ? 181 PHE B CA  1 
ATOM   3618 C  C   . PHE B 1 181 ? -18.939 -14.485 2.349   1.00 25.23 ? 181 PHE B C   1 
ATOM   3619 O  O   . PHE B 1 181 ? -18.621 -15.627 2.722   1.00 26.78 ? 181 PHE B O   1 
ATOM   3620 C  CB  . PHE B 1 181 ? -21.263 -14.426 3.318   1.00 24.57 ? 181 PHE B CB  1 
ATOM   3621 C  CG  . PHE B 1 181 ? -20.874 -13.718 4.600   1.00 23.08 ? 181 PHE B CG  1 
ATOM   3622 C  CD1 . PHE B 1 181 ? -20.566 -12.357 4.628   1.00 23.23 ? 181 PHE B CD1 1 
ATOM   3623 C  CD2 . PHE B 1 181 ? -20.877 -14.439 5.800   1.00 22.88 ? 181 PHE B CD2 1 
ATOM   3624 C  CE1 . PHE B 1 181 ? -20.185 -11.753 5.805   1.00 25.09 ? 181 PHE B CE1 1 
ATOM   3625 C  CE2 . PHE B 1 181 ? -20.581 -13.797 7.026   1.00 24.18 ? 181 PHE B CE2 1 
ATOM   3626 C  CZ  . PHE B 1 181 ? -20.254 -12.454 7.011   1.00 22.07 ? 181 PHE B CZ  1 
ATOM   3627 N  N   . ASP B 1 182 ? -18.066 -13.488 2.131   1.00 24.03 ? 182 ASP B N   1 
ATOM   3628 C  CA  . ASP B 1 182 ? -16.648 -13.735 2.341   1.00 29.81 ? 182 ASP B CA  1 
ATOM   3629 C  C   . ASP B 1 182 ? -16.329 -13.467 3.784   1.00 25.43 ? 182 ASP B C   1 
ATOM   3630 O  O   . ASP B 1 182 ? -15.944 -12.388 4.200   1.00 25.88 ? 182 ASP B O   1 
ATOM   3631 C  CB  . ASP B 1 182 ? -15.693 -12.925 1.445   1.00 35.58 ? 182 ASP B CB  1 
ATOM   3632 C  CG  . ASP B 1 182 ? -14.230 -13.389 1.631   1.00 48.41 ? 182 ASP B CG  1 
ATOM   3633 O  OD1 . ASP B 1 182 ? -14.034 -14.495 2.244   1.00 48.94 ? 182 ASP B OD1 1 
ATOM   3634 O  OD2 . ASP B 1 182 ? -13.302 -12.679 1.167   1.00 52.47 ? 182 ASP B OD2 1 
ATOM   3635 N  N   . LEU B 1 183 ? -16.611 -14.474 4.573   1.00 23.31 ? 183 LEU B N   1 
ATOM   3636 C  CA  . LEU B 1 183 ? -16.372 -14.297 6.000   1.00 22.90 ? 183 LEU B CA  1 
ATOM   3637 C  C   . LEU B 1 183 ? -14.925 -14.083 6.302   1.00 21.62 ? 183 LEU B C   1 
ATOM   3638 O  O   . LEU B 1 183 ? -14.620 -13.309 7.240   1.00 21.36 ? 183 LEU B O   1 
ATOM   3639 C  CB  . LEU B 1 183 ? -16.926 -15.514 6.713   1.00 19.49 ? 183 LEU B CB  1 
ATOM   3640 C  CG  . LEU B 1 183 ? -16.796 -15.550 8.243   1.00 20.06 ? 183 LEU B CG  1 
ATOM   3641 C  CD1 . LEU B 1 183 ? -17.495 -14.345 8.911   1.00 20.39 ? 183 LEU B CD1 1 
ATOM   3642 C  CD2 . LEU B 1 183 ? -17.433 -16.909 8.599   1.00 20.33 ? 183 LEU B CD2 1 
ATOM   3643 N  N   . LEU B 1 184 ? -14.001 -14.825 5.612   1.00 21.77 ? 184 LEU B N   1 
ATOM   3644 C  CA  . LEU B 1 184 ? -12.556 -14.738 5.896   1.00 23.30 ? 184 LEU B CA  1 
ATOM   3645 C  C   . LEU B 1 184 ? -12.077 -13.291 5.751   1.00 22.31 ? 184 LEU B C   1 
ATOM   3646 O  O   . LEU B 1 184 ? -11.073 -12.895 6.386   1.00 25.01 ? 184 LEU B O   1 
ATOM   3647 C  CB  . LEU B 1 184 ? -11.687 -15.754 5.062   1.00 25.07 ? 184 LEU B CB  1 
ATOM   3648 C  CG  . LEU B 1 184 ? -11.736 -17.278 5.319   1.00 28.40 ? 184 LEU B CG  1 
ATOM   3649 C  CD1 . LEU B 1 184 ? -11.064 -18.128 4.217   1.00 27.35 ? 184 LEU B CD1 1 
ATOM   3650 C  CD2 . LEU B 1 184 ? -11.094 -17.654 6.635   1.00 30.13 ? 184 LEU B CD2 1 
ATOM   3651 N  N   . SER B 1 185 ? -12.786 -12.489 4.942   1.00 25.55 ? 185 SER B N   1 
ATOM   3652 C  CA  . SER B 1 185 ? -12.529 -11.041 4.852   1.00 29.64 ? 185 SER B CA  1 
ATOM   3653 C  C   . SER B 1 185 ? -12.732 -10.194 6.047   1.00 31.69 ? 185 SER B C   1 
ATOM   3654 O  O   . SER B 1 185 ? -12.200 -9.091  6.116   1.00 33.31 ? 185 SER B O   1 
ATOM   3655 C  CB  . SER B 1 185 ? -13.321 -10.434 3.682   1.00 35.56 ? 185 SER B CB  1 
ATOM   3656 O  OG  . SER B 1 185 ? -12.528 -10.683 2.537   1.00 40.28 ? 185 SER B OG  1 
ATOM   3657 N  N   . LEU B 1 186 ? -13.535 -10.682 6.992   1.00 25.59 ? 186 LEU B N   1 
ATOM   3658 C  CA  . LEU B 1 186 ? -13.743 -10.022 8.264   1.00 23.79 ? 186 LEU B CA  1 
ATOM   3659 C  C   . LEU B 1 186 ? -12.850 -10.493 9.362   1.00 24.66 ? 186 LEU B C   1 
ATOM   3660 O  O   . LEU B 1 186 ? -13.138 -10.135 10.593  1.00 24.05 ? 186 LEU B O   1 
ATOM   3661 C  CB  . LEU B 1 186 ? -15.155 -10.270 8.760   1.00 21.92 ? 186 LEU B CB  1 
ATOM   3662 C  CG  . LEU B 1 186 ? -16.269 -9.742  7.863   1.00 21.70 ? 186 LEU B CG  1 
ATOM   3663 C  CD1 . LEU B 1 186 ? -17.665 -10.061 8.406   1.00 22.12 ? 186 LEU B CD1 1 
ATOM   3664 C  CD2 . LEU B 1 186 ? -16.094 -8.224  7.632   1.00 21.82 ? 186 LEU B CD2 1 
ATOM   3665 N  N   . LEU B 1 187 ? -11.795 -11.263 8.989   1.00 19.37 ? 187 LEU B N   1 
ATOM   3666 C  CA  . LEU B 1 187 ? -10.804 -11.521 9.962   1.00 18.81 ? 187 LEU B CA  1 
ATOM   3667 C  C   . LEU B 1 187 ? -9.628  -10.570 9.668   1.00 16.85 ? 187 LEU B C   1 
ATOM   3668 O  O   . LEU B 1 187 ? -9.309  -10.265 8.492   1.00 20.05 ? 187 LEU B O   1 
ATOM   3669 C  CB  . LEU B 1 187 ? -10.261 -12.976 9.889   1.00 20.10 ? 187 LEU B CB  1 
ATOM   3670 C  CG  . LEU B 1 187 ? -11.347 -14.022 9.900   1.00 22.99 ? 187 LEU B CG  1 
ATOM   3671 C  CD1 . LEU B 1 187 ? -10.806 -15.465 9.825   1.00 23.08 ? 187 LEU B CD1 1 
ATOM   3672 C  CD2 . LEU B 1 187 ? -12.309 -13.849 11.083  1.00 20.70 ? 187 LEU B CD2 1 
ATOM   3673 N  N   . PRO B 1 188 ? -8.845  -10.261 10.704  1.00 17.55 ? 188 PRO B N   1 
ATOM   3674 C  CA  . PRO B 1 188 ? -7.697  -9.411  10.462  1.00 16.90 ? 188 PRO B CA  1 
ATOM   3675 C  C   . PRO B 1 188 ? -6.554  -10.201 9.805   1.00 17.26 ? 188 PRO B C   1 
ATOM   3676 O  O   . PRO B 1 188 ? -6.603  -11.449 9.766   1.00 15.79 ? 188 PRO B O   1 
ATOM   3677 C  CB  . PRO B 1 188 ? -7.228  -9.048  11.880  1.00 17.41 ? 188 PRO B CB  1 
ATOM   3678 C  CG  . PRO B 1 188 ? -7.732  -10.224 12.781  1.00 15.15 ? 188 PRO B CG  1 
ATOM   3679 C  CD  . PRO B 1 188 ? -9.038  -10.558 12.154  1.00 14.85 ? 188 PRO B CD  1 
ATOM   3680 N  N   . PRO B 1 189 ? -5.511  -9.506  9.312   1.00 15.33 ? 189 PRO B N   1 
ATOM   3681 C  CA  . PRO B 1 189 ? -4.441  -10.293 8.731   1.00 15.50 ? 189 PRO B CA  1 
ATOM   3682 C  C   . PRO B 1 189 ? -3.600  -11.081 9.714   1.00 17.84 ? 189 PRO B C   1 
ATOM   3683 O  O   . PRO B 1 189 ? -3.029  -12.069 9.318   1.00 21.49 ? 189 PRO B O   1 
ATOM   3684 C  CB  . PRO B 1 189 ? -3.552  -9.250  8.044   1.00 17.81 ? 189 PRO B CB  1 
ATOM   3685 C  CG  . PRO B 1 189 ? -3.868  -7.975  8.683   1.00 18.57 ? 189 PRO B CG  1 
ATOM   3686 C  CD  . PRO B 1 189 ? -5.314  -8.041  9.130   1.00 15.05 ? 189 PRO B CD  1 
ATOM   3687 N  N   . SER B 1 190 ? -3.543  -10.672 11.001  1.00 16.14 ? 190 SER B N   1 
ATOM   3688 C  CA  . SER B 1 190 ? -2.831  -11.429 12.006  1.00 15.02 ? 190 SER B CA  1 
ATOM   3689 C  C   . SER B 1 190 ? -3.845  -12.333 12.691  1.00 14.73 ? 190 SER B C   1 
ATOM   3690 O  O   . SER B 1 190 ? -4.874  -11.819 13.202  1.00 14.24 ? 190 SER B O   1 
ATOM   3691 C  CB  . SER B 1 190 ? -2.186  -10.513 13.072  1.00 15.92 ? 190 SER B CB  1 
ATOM   3692 O  OG  . SER B 1 190 ? -1.673  -11.360 14.133  1.00 18.23 ? 190 SER B OG  1 
ATOM   3693 N  N   . TRP B 1 191 ? -3.545  -13.647 12.736  1.00 14.21 ? 191 TRP B N   1 
ATOM   3694 C  CA  . TRP B 1 191 ? -4.428  -14.598 13.481  1.00 13.65 ? 191 TRP B CA  1 
ATOM   3695 C  C   . TRP B 1 191 ? -3.834  -14.925 14.797  1.00 14.76 ? 191 TRP B C   1 
ATOM   3696 O  O   . TRP B 1 191 ? -4.079  -15.982 15.368  1.00 16.80 ? 191 TRP B O   1 
ATOM   3697 C  CB  . TRP B 1 191 ? -4.714  -15.873 12.580  1.00 13.91 ? 191 TRP B CB  1 
ATOM   3698 C  CG  . TRP B 1 191 ? -5.555  -15.565 11.435  1.00 15.43 ? 191 TRP B CG  1 
ATOM   3699 C  CD1 . TRP B 1 191 ? -6.081  -14.341 11.042  1.00 15.96 ? 191 TRP B CD1 1 
ATOM   3700 C  CD2 . TRP B 1 191 ? -6.002  -16.519 10.404  1.00 17.20 ? 191 TRP B CD2 1 
ATOM   3701 N  NE1 . TRP B 1 191 ? -6.787  -14.438 9.891   1.00 17.12 ? 191 TRP B NE1 1 
ATOM   3702 C  CE2 . TRP B 1 191 ? -6.786  -15.760 9.459   1.00 18.09 ? 191 TRP B CE2 1 
ATOM   3703 C  CE3 . TRP B 1 191 ? -5.803  -17.895 10.192  1.00 17.21 ? 191 TRP B CE3 1 
ATOM   3704 C  CZ2 . TRP B 1 191 ? -7.406  -16.361 8.350   1.00 17.61 ? 191 TRP B CZ2 1 
ATOM   3705 C  CZ3 . TRP B 1 191 ? -6.439  -18.452 9.102   1.00 16.97 ? 191 TRP B CZ3 1 
ATOM   3706 C  CH2 . TRP B 1 191 ? -7.229  -17.710 8.213   1.00 18.82 ? 191 TRP B CH2 1 
ATOM   3707 N  N   . ASP B 1 192 ? -3.114  -14.020 15.415  1.00 14.57 ? 192 ASP B N   1 
ATOM   3708 C  CA  . ASP B 1 192 ? -2.644  -14.211 16.804  1.00 15.34 ? 192 ASP B CA  1 
ATOM   3709 C  C   . ASP B 1 192 ? -3.902  -14.145 17.753  1.00 14.20 ? 192 ASP B C   1 
ATOM   3710 O  O   . ASP B 1 192 ? -4.836  -13.398 17.532  1.00 14.68 ? 192 ASP B O   1 
ATOM   3711 C  CB  . ASP B 1 192 ? -1.723  -13.055 17.270  1.00 18.26 ? 192 ASP B CB  1 
ATOM   3712 C  CG  . ASP B 1 192 ? -0.329  -13.015 16.672  1.00 25.44 ? 192 ASP B CG  1 
ATOM   3713 O  OD1 . ASP B 1 192 ? 0.170   -14.039 16.236  1.00 21.42 ? 192 ASP B OD1 1 
ATOM   3714 O  OD2 . ASP B 1 192 ? 0.329   -11.918 16.843  1.00 27.38 ? 192 ASP B OD2 1 
ATOM   3715 N  N   . TYR B 1 193 ? -3.915  -15.001 18.785  1.00 12.66 ? 193 TYR B N   1 
ATOM   3716 C  CA  . TYR B 1 193 ? -5.148  -15.056 19.638  1.00 12.46 ? 193 TYR B CA  1 
ATOM   3717 C  C   . TYR B 1 193 ? -4.839  -15.369 21.081  1.00 11.20 ? 193 TYR B C   1 
ATOM   3718 O  O   . TYR B 1 193 ? -3.809  -15.848 21.483  1.00 13.00 ? 193 TYR B O   1 
ATOM   3719 C  CB  . TYR B 1 193 ? -6.151  -16.123 19.071  1.00 11.41 ? 193 TYR B CB  1 
ATOM   3720 C  CG  . TYR B 1 193 ? -5.517  -17.558 19.142  1.00 13.41 ? 193 TYR B CG  1 
ATOM   3721 C  CD1 . TYR B 1 193 ? -5.713  -18.371 20.261  1.00 14.16 ? 193 TYR B CD1 1 
ATOM   3722 C  CD2 . TYR B 1 193 ? -4.750  -18.056 18.096  1.00 15.38 ? 193 TYR B CD2 1 
ATOM   3723 C  CE1 . TYR B 1 193 ? -5.144  -19.653 20.350  1.00 15.49 ? 193 TYR B CE1 1 
ATOM   3724 C  CE2 . TYR B 1 193 ? -4.224  -19.324 18.162  1.00 13.67 ? 193 TYR B CE2 1 
ATOM   3725 C  CZ  . TYR B 1 193 ? -4.328  -20.094 19.318  1.00 14.71 ? 193 TYR B CZ  1 
ATOM   3726 O  OH  . TYR B 1 193 ? -3.881  -21.365 19.485  1.00 14.74 ? 193 TYR B OH  1 
ATOM   3727 N  N   . TRP B 1 194 ? -5.863  -15.074 21.906  1.00 11.84 ? 194 TRP B N   1 
ATOM   3728 C  CA  . TRP B 1 194 ? -5.938  -15.520 23.296  1.00 11.25 ? 194 TRP B CA  1 
ATOM   3729 C  C   . TRP B 1 194 ? -7.037  -16.541 23.373  1.00 11.13 ? 194 TRP B C   1 
ATOM   3730 O  O   . TRP B 1 194 ? -7.965  -16.555 22.532  1.00 11.31 ? 194 TRP B O   1 
ATOM   3731 C  CB  . TRP B 1 194 ? -6.391  -14.364 24.172  1.00 11.35 ? 194 TRP B CB  1 
ATOM   3732 C  CG  . TRP B 1 194 ? -5.409  -13.253 24.259  1.00 13.61 ? 194 TRP B CG  1 
ATOM   3733 C  CD1 . TRP B 1 194 ? -4.213  -13.239 24.886  1.00 13.17 ? 194 TRP B CD1 1 
ATOM   3734 C  CD2 . TRP B 1 194 ? -5.617  -11.887 23.747  1.00 13.36 ? 194 TRP B CD2 1 
ATOM   3735 N  NE1 . TRP B 1 194 ? -3.651  -11.991 24.798  1.00 13.90 ? 194 TRP B NE1 1 
ATOM   3736 C  CE2 . TRP B 1 194 ? -4.450  -11.174 24.089  1.00 12.95 ? 194 TRP B CE2 1 
ATOM   3737 C  CE3 . TRP B 1 194 ? -6.639  -11.254 23.027  1.00 13.36 ? 194 TRP B CE3 1 
ATOM   3738 C  CZ2 . TRP B 1 194 ? -4.307  -9.791  23.795  1.00 14.67 ? 194 TRP B CZ2 1 
ATOM   3739 C  CZ3 . TRP B 1 194 ? -6.472  -9.909  22.671  1.00 13.77 ? 194 TRP B CZ3 1 
ATOM   3740 C  CH2 . TRP B 1 194 ? -5.345  -9.180  23.098  1.00 12.73 ? 194 TRP B CH2 1 
ATOM   3741 N  N   . THR B 1 195 ? -6.977  -17.451 24.384  1.00 10.51 ? 195 THR B N   1 
ATOM   3742 C  CA  . THR B 1 195 ? -8.011  -18.469 24.497  1.00 10.57 ? 195 THR B CA  1 
ATOM   3743 C  C   . THR B 1 195 ? -8.218  -18.823 25.957  1.00 9.84  ? 195 THR B C   1 
ATOM   3744 O  O   . THR B 1 195 ? -7.277  -18.794 26.805  1.00 10.98 ? 195 THR B O   1 
ATOM   3745 C  CB  . THR B 1 195 ? -7.628  -19.768 23.662  1.00 11.08 ? 195 THR B CB  1 
ATOM   3746 O  OG1 . THR B 1 195 ? -8.645  -20.743 23.855  1.00 10.74 ? 195 THR B OG1 1 
ATOM   3747 C  CG2 . THR B 1 195 ? -6.206  -20.352 24.072  1.00 12.28 ? 195 THR B CG2 1 
ATOM   3748 N  N   . TYR B 1 196 ? -9.510  -19.117 26.257  1.00 10.00 ? 196 TYR B N   1 
ATOM   3749 C  CA  . TYR B 1 196 ? -9.860  -19.473 27.647  1.00 10.19 ? 196 TYR B CA  1 
ATOM   3750 C  C   . TYR B 1 196 ? -11.149 -20.245 27.564  1.00 8.95  ? 196 TYR B C   1 
ATOM   3751 O  O   . TYR B 1 196 ? -11.938 -20.160 26.613  1.00 9.61  ? 196 TYR B O   1 
ATOM   3752 C  CB  . TYR B 1 196 ? -9.950  -18.232 28.578  1.00 11.48 ? 196 TYR B CB  1 
ATOM   3753 C  CG  . TYR B 1 196 ? -11.217 -17.423 28.324  1.00 10.15 ? 196 TYR B CG  1 
ATOM   3754 C  CD1 . TYR B 1 196 ? -11.291 -16.499 27.282  1.00 11.22 ? 196 TYR B CD1 1 
ATOM   3755 C  CD2 . TYR B 1 196 ? -12.348 -17.610 29.107  1.00 10.53 ? 196 TYR B CD2 1 
ATOM   3756 C  CE1 . TYR B 1 196 ? -12.451 -15.775 27.046  1.00 10.11 ? 196 TYR B CE1 1 
ATOM   3757 C  CE2 . TYR B 1 196 ? -13.508 -16.891 28.878  1.00 11.55 ? 196 TYR B CE2 1 
ATOM   3758 C  CZ  . TYR B 1 196 ? -13.558 -15.976 27.849  1.00 9.32  ? 196 TYR B CZ  1 
ATOM   3759 O  OH  . TYR B 1 196 ? -14.721 -15.268 27.634  1.00 10.68 ? 196 TYR B OH  1 
ATOM   3760 N  N   . PRO B 1 197 ? -11.476 -21.065 28.597  1.00 9.30  ? 197 PRO B N   1 
ATOM   3761 C  CA  . PRO B 1 197 ? -12.739 -21.763 28.637  1.00 9.41  ? 197 PRO B CA  1 
ATOM   3762 C  C   . PRO B 1 197 ? -13.882 -20.905 29.222  1.00 9.41  ? 197 PRO B C   1 
ATOM   3763 O  O   . PRO B 1 197 ? -13.633 -20.302 30.288  1.00 10.65 ? 197 PRO B O   1 
ATOM   3764 C  CB  . PRO B 1 197 ? -12.420 -22.966 29.593  1.00 10.51 ? 197 PRO B CB  1 
ATOM   3765 C  CG  . PRO B 1 197 ? -11.405 -22.420 30.529  1.00 12.48 ? 197 PRO B CG  1 
ATOM   3766 C  CD  . PRO B 1 197 ? -10.545 -21.433 29.698  1.00 10.16 ? 197 PRO B CD  1 
ATOM   3767 N  N   . GLY B 1 198 ? -15.003 -20.851 28.506  1.00 9.07  ? 198 GLY B N   1 
ATOM   3768 C  CA  . GLY B 1 198 ? -16.115 -20.051 28.997  1.00 8.91  ? 198 GLY B CA  1 
ATOM   3769 C  C   . GLY B 1 198 ? -17.480 -20.467 28.539  1.00 9.57  ? 198 GLY B C   1 
ATOM   3770 O  O   . GLY B 1 198 ? -17.764 -21.728 28.491  1.00 10.88 ? 198 GLY B O   1 
ATOM   3771 N  N   . SER B 1 199 ? -18.319 -19.491 28.242  1.00 9.98  ? 199 SER B N   1 
ATOM   3772 C  CA  . SER B 1 199 ? -19.729 -19.815 28.120  1.00 9.62  ? 199 SER B CA  1 
ATOM   3773 C  C   . SER B 1 199 ? -20.323 -19.064 26.943  1.00 10.72 ? 199 SER B C   1 
ATOM   3774 O  O   . SER B 1 199 ? -19.708 -18.085 26.421  1.00 9.59  ? 199 SER B O   1 
ATOM   3775 C  CB  . SER B 1 199 ? -20.527 -19.403 29.411  1.00 10.16 ? 199 SER B CB  1 
ATOM   3776 O  OG  . SER B 1 199 ? -20.602 -17.970 29.505  1.00 9.39  ? 199 SER B OG  1 
ATOM   3777 N  N   . LEU B 1 200 ? -21.557 -19.434 26.597  1.00 10.66 ? 200 LEU B N   1 
ATOM   3778 C  CA  . LEU B 1 200 ? -22.407 -18.520 25.748  1.00 10.83 ? 200 LEU B CA  1 
ATOM   3779 C  C   . LEU B 1 200 ? -22.536 -17.179 26.559  1.00 12.17 ? 200 LEU B C   1 
ATOM   3780 O  O   . LEU B 1 200 ? -22.609 -17.169 27.819  1.00 10.21 ? 200 LEU B O   1 
ATOM   3781 C  CB  . LEU B 1 200 ? -23.787 -19.097 25.581  1.00 12.30 ? 200 LEU B CB  1 
ATOM   3782 C  CG  . LEU B 1 200 ? -23.841 -20.417 24.791  1.00 13.11 ? 200 LEU B CG  1 
ATOM   3783 C  CD1 . LEU B 1 200 ? -25.264 -20.768 24.737  1.00 13.23 ? 200 LEU B CD1 1 
ATOM   3784 C  CD2 . LEU B 1 200 ? -23.201 -20.320 23.410  1.00 13.76 ? 200 LEU B CD2 1 
ATOM   3785 N  N   . THR B 1 201 ? -22.510 -16.051 25.830  1.00 10.56 ? 201 THR B N   1 
ATOM   3786 C  CA  . THR B 1 201 ? -22.735 -14.748 26.544  1.00 10.20 ? 201 THR B CA  1 
ATOM   3787 C  C   . THR B 1 201 ? -24.222 -14.312 26.517  1.00 11.39 ? 201 THR B C   1 
ATOM   3788 O  O   . THR B 1 201 ? -24.532 -13.174 26.979  1.00 10.41 ? 201 THR B O   1 
ATOM   3789 C  CB  . THR B 1 201 ? -21.862 -13.620 25.921  1.00 10.81 ? 201 THR B CB  1 
ATOM   3790 O  OG1 . THR B 1 201 ? -22.414 -13.317 24.649  1.00 10.54 ? 201 THR B OG1 1 
ATOM   3791 C  CG2 . THR B 1 201 ? -20.368 -14.025 25.857  1.00 11.64 ? 201 THR B CG2 1 
ATOM   3792 N  N   . VAL B 1 202 ? -25.138 -15.162 26.063  1.00 10.26 ? 202 VAL B N   1 
ATOM   3793 C  CA  . VAL B 1 202 ? -26.595 -14.948 26.072  1.00 12.19 ? 202 VAL B CA  1 
ATOM   3794 C  C   . VAL B 1 202 ? -27.189 -16.153 26.789  1.00 11.58 ? 202 VAL B C   1 
ATOM   3795 O  O   . VAL B 1 202 ? -26.638 -17.248 26.740  1.00 12.67 ? 202 VAL B O   1 
ATOM   3796 C  CB  . VAL B 1 202 ? -27.170 -14.824 24.624  1.00 11.07 ? 202 VAL B CB  1 
ATOM   3797 C  CG1 . VAL B 1 202 ? -26.675 -13.504 23.978  1.00 12.20 ? 202 VAL B CG1 1 
ATOM   3798 C  CG2 . VAL B 1 202 ? -26.897 -16.130 23.799  1.00 12.89 ? 202 VAL B CG2 1 
ATOM   3799 N  N   . PRO B 1 203 ? -28.302 -15.984 27.487  1.00 10.42 ? 203 PRO B N   1 
ATOM   3800 C  CA  . PRO B 1 203 ? -29.064 -17.104 27.938  1.00 12.06 ? 203 PRO B CA  1 
ATOM   3801 C  C   . PRO B 1 203 ? -29.232 -18.129 26.798  1.00 12.03 ? 203 PRO B C   1 
ATOM   3802 O  O   . PRO B 1 203 ? -29.521 -17.758 25.658  1.00 12.73 ? 203 PRO B O   1 
ATOM   3803 C  CB  . PRO B 1 203 ? -30.454 -16.451 28.352  1.00 12.39 ? 203 PRO B CB  1 
ATOM   3804 C  CG  . PRO B 1 203 ? -30.034 -15.035 28.738  1.00 12.70 ? 203 PRO B CG  1 
ATOM   3805 C  CD  . PRO B 1 203 ? -28.949 -14.668 27.719  1.00 11.15 ? 203 PRO B CD  1 
ATOM   3806 N  N   . PRO B 1 204 ? -29.086 -19.407 27.103  1.00 13.05 ? 204 PRO B N   1 
ATOM   3807 C  CA  . PRO B 1 204 ? -29.029 -20.063 28.434  1.00 13.43 ? 204 PRO B CA  1 
ATOM   3808 C  C   . PRO B 1 204 ? -27.612 -20.107 29.074  1.00 11.98 ? 204 PRO B C   1 
ATOM   3809 O  O   . PRO B 1 204 ? -27.459 -20.768 30.094  1.00 14.40 ? 204 PRO B O   1 
ATOM   3810 C  CB  . PRO B 1 204 ? -29.525 -21.502 28.093  1.00 12.87 ? 204 PRO B CB  1 
ATOM   3811 C  CG  . PRO B 1 204 ? -28.988 -21.725 26.681  1.00 14.48 ? 204 PRO B CG  1 
ATOM   3812 C  CD  . PRO B 1 204 ? -29.181 -20.402 26.011  1.00 13.17 ? 204 PRO B CD  1 
ATOM   3813 N  N   . LEU B 1 205 ? -26.606 -19.393 28.534  1.00 12.01 ? 205 LEU B N   1 
ATOM   3814 C  CA  . LEU B 1 205 ? -25.336 -19.150 29.262  1.00 11.87 ? 205 LEU B CA  1 
ATOM   3815 C  C   . LEU B 1 205 ? -24.521 -20.398 29.558  1.00 9.72  ? 205 LEU B C   1 
ATOM   3816 O  O   . LEU B 1 205 ? -23.766 -20.463 30.509  1.00 10.78 ? 205 LEU B O   1 
ATOM   3817 C  CB  . LEU B 1 205 ? -25.590 -18.355 30.601  1.00 10.89 ? 205 LEU B CB  1 
ATOM   3818 C  CG  . LEU B 1 205 ? -26.215 -16.957 30.342  1.00 11.83 ? 205 LEU B CG  1 
ATOM   3819 C  CD1 . LEU B 1 205 ? -26.628 -16.360 31.709  1.00 13.79 ? 205 LEU B CD1 1 
ATOM   3820 C  CD2 . LEU B 1 205 ? -25.265 -15.975 29.661  1.00 10.49 ? 205 LEU B CD2 1 
ATOM   3821 N  N   . LEU B 1 206 ? -24.693 -21.387 28.674  1.00 9.84  ? 206 LEU B N   1 
ATOM   3822 C  CA  . LEU B 1 206 ? -24.085 -22.705 28.883  1.00 11.86 ? 206 LEU B CA  1 
ATOM   3823 C  C   . LEU B 1 206 ? -22.601 -22.658 28.829  1.00 11.66 ? 206 LEU B C   1 
ATOM   3824 O  O   . LEU B 1 206 ? -22.017 -21.954 27.968  1.00 11.02 ? 206 LEU B O   1 
ATOM   3825 C  CB  . LEU B 1 206 ? -24.584 -23.716 27.794  1.00 11.90 ? 206 LEU B CB  1 
ATOM   3826 C  CG  . LEU B 1 206 ? -26.079 -23.898 27.809  1.00 11.66 ? 206 LEU B CG  1 
ATOM   3827 C  CD1 . LEU B 1 206 ? -26.558 -24.546 26.505  1.00 14.61 ? 206 LEU B CD1 1 
ATOM   3828 C  CD2 . LEU B 1 206 ? -26.597 -24.704 29.034  1.00 11.27 ? 206 LEU B CD2 1 
ATOM   3829 N  N   . GLU B 1 207 ? -21.904 -23.422 29.692  1.00 11.62 ? 207 GLU B N   1 
ATOM   3830 C  CA  . GLU B 1 207 ? -20.465 -23.391 29.865  1.00 12.14 ? 207 GLU B CA  1 
ATOM   3831 C  C   . GLU B 1 207 ? -19.857 -24.434 28.923  1.00 12.65 ? 207 GLU B C   1 
ATOM   3832 O  O   . GLU B 1 207 ? -19.339 -25.472 29.374  1.00 14.48 ? 207 GLU B O   1 
ATOM   3833 C  CB  . GLU B 1 207 ? -20.064 -23.589 31.319  1.00 12.17 ? 207 GLU B CB  1 
ATOM   3834 C  CG  . GLU B 1 207 ? -20.595 -22.319 32.075  1.00 12.25 ? 207 GLU B CG  1 
ATOM   3835 C  CD  . GLU B 1 207 ? -20.292 -22.344 33.555  1.00 14.45 ? 207 GLU B CD  1 
ATOM   3836 O  OE1 . GLU B 1 207 ? -20.217 -23.509 34.136  1.00 15.22 ? 207 GLU B OE1 1 
ATOM   3837 O  OE2 . GLU B 1 207 ? -20.292 -21.248 34.151  1.00 13.07 ? 207 GLU B OE2 1 
ATOM   3838 N  N   . SER B 1 208 ? -20.015 -24.189 27.601  1.00 12.01 ? 208 SER B N   1 
ATOM   3839 C  CA  . SER B 1 208 ? -19.605 -25.176 26.607  1.00 10.77 ? 208 SER B CA  1 
ATOM   3840 C  C   . SER B 1 208 ? -18.694 -24.543 25.580  1.00 12.70 ? 208 SER B C   1 
ATOM   3841 O  O   . SER B 1 208 ? -18.409 -25.160 24.537  1.00 11.68 ? 208 SER B O   1 
ATOM   3842 C  CB  . SER B 1 208 ? -20.860 -25.645 25.933  1.00 11.44 ? 208 SER B CB  1 
ATOM   3843 O  OG  . SER B 1 208 ? -21.599 -24.521 25.493  1.00 14.04 ? 208 SER B OG  1 
ATOM   3844 N  N   . VAL B 1 209 ? -18.141 -23.362 25.881  1.00 10.07 ? 209 VAL B N   1 
ATOM   3845 C  CA  . VAL B 1 209 ? -17.376 -22.621 24.809  1.00 10.94 ? 209 VAL B CA  1 
ATOM   3846 C  C   . VAL B 1 209 ? -15.928 -22.478 25.045  1.00 10.51 ? 209 VAL B C   1 
ATOM   3847 O  O   . VAL B 1 209 ? -15.408 -22.034 26.076  1.00 12.21 ? 209 VAL B O   1 
ATOM   3848 C  CB  . VAL B 1 209 ? -17.913 -21.170 24.670  1.00 9.78  ? 209 VAL B CB  1 
ATOM   3849 C  CG1 . VAL B 1 209 ? -17.089 -20.474 23.562  1.00 11.05 ? 209 VAL B CG1 1 
ATOM   3850 C  CG2 . VAL B 1 209 ? -19.401 -21.191 24.267  1.00 11.85 ? 209 VAL B CG2 1 
ATOM   3851 N  N   . THR B 1 210 ? -15.141 -22.986 24.046  1.00 9.93  ? 210 THR B N   1 
ATOM   3852 C  CA  . THR B 1 210 ? -13.714 -22.603 23.979  1.00 11.12 ? 210 THR B CA  1 
ATOM   3853 C  C   . THR B 1 210 ? -13.612 -21.281 23.229  1.00 9.23  ? 210 THR B C   1 
ATOM   3854 O  O   . THR B 1 210 ? -13.990 -21.219 22.033  1.00 10.83 ? 210 THR B O   1 
ATOM   3855 C  CB  . THR B 1 210 ? -12.941 -23.677 23.215  1.00 11.35 ? 210 THR B CB  1 
ATOM   3856 O  OG1 . THR B 1 210 ? -13.041 -24.935 23.919  1.00 11.93 ? 210 THR B OG1 1 
ATOM   3857 C  CG2 . THR B 1 210 ? -11.492 -23.274 23.181  1.00 11.78 ? 210 THR B CG2 1 
ATOM   3858 N  N   . TRP B 1 211 ? -13.281 -20.224 23.945  1.00 10.17 ? 211 TRP B N   1 
ATOM   3859 C  CA  . TRP B 1 211 ? -13.159 -18.873 23.332  1.00 11.16 ? 211 TRP B CA  1 
ATOM   3860 C  C   . TRP B 1 211 ? -11.792 -18.750 22.714  1.00 9.22  ? 211 TRP B C   1 
ATOM   3861 O  O   . TRP B 1 211 ? -10.743 -19.080 23.350  1.00 10.05 ? 211 TRP B O   1 
ATOM   3862 C  CB  . TRP B 1 211 ? -13.372 -17.836 24.420  1.00 11.08 ? 211 TRP B CB  1 
ATOM   3863 C  CG  . TRP B 1 211 ? -14.834 -17.633 24.669  1.00 10.42 ? 211 TRP B CG  1 
ATOM   3864 C  CD1 . TRP B 1 211 ? -15.667 -18.136 25.676  1.00 10.25 ? 211 TRP B CD1 1 
ATOM   3865 C  CD2 . TRP B 1 211 ? -15.696 -16.825 23.821  1.00 9.69  ? 211 TRP B CD2 1 
ATOM   3866 N  NE1 . TRP B 1 211 ? -16.939 -17.745 25.421  1.00 10.36 ? 211 TRP B NE1 1 
ATOM   3867 C  CE2 . TRP B 1 211 ? -17.060 -16.928 24.341  1.00 10.49 ? 211 TRP B CE2 1 
ATOM   3868 C  CE3 . TRP B 1 211 ? -15.444 -16.016 22.702  1.00 10.00 ? 211 TRP B CE3 1 
ATOM   3869 C  CZ2 . TRP B 1 211 ? -18.142 -16.302 23.741  1.00 10.78 ? 211 TRP B CZ2 1 
ATOM   3870 C  CZ3 . TRP B 1 211 ? -16.531 -15.364 22.125  1.00 10.02 ? 211 TRP B CZ3 1 
ATOM   3871 C  CH2 . TRP B 1 211 ? -17.859 -15.470 22.661  1.00 10.40 ? 211 TRP B CH2 1 
ATOM   3872 N  N   . ILE B 1 212 ? -11.829 -18.165 21.518  1.00 10.50 ? 212 ILE B N   1 
ATOM   3873 C  CA  . ILE B 1 212 ? -10.629 -17.846 20.778  1.00 10.61 ? 212 ILE B CA  1 
ATOM   3874 C  C   . ILE B 1 212 ? -10.800 -16.373 20.331  1.00 9.83  ? 212 ILE B C   1 
ATOM   3875 O  O   . ILE B 1 212 ? -11.586 -16.090 19.493  1.00 10.36 ? 212 ILE B O   1 
ATOM   3876 C  CB  . ILE B 1 212 ? -10.508 -18.765 19.552  1.00 10.74 ? 212 ILE B CB  1 
ATOM   3877 C  CG1 . ILE B 1 212 ? -10.280 -20.196 20.020  1.00 10.97 ? 212 ILE B CG1 1 
ATOM   3878 C  CG2 . ILE B 1 212 ? -9.271  -18.388 18.702  1.00 13.64 ? 212 ILE B CG2 1 
ATOM   3879 C  CD1 . ILE B 1 212 ? -10.530 -21.232 18.869  1.00 12.18 ? 212 ILE B CD1 1 
ATOM   3880 N  N   . VAL B 1 213 ? -10.075 -15.453 20.994  1.00 10.24 ? 213 VAL B N   1 
ATOM   3881 C  CA  . VAL B 1 213 ? -10.223 -14.047 20.740  1.00 11.14 ? 213 VAL B CA  1 
ATOM   3882 C  C   . VAL B 1 213 ? -8.930  -13.516 20.022  1.00 9.78  ? 213 VAL B C   1 
ATOM   3883 O  O   . VAL B 1 213 ? -7.830  -13.555 20.527  1.00 11.62 ? 213 VAL B O   1 
ATOM   3884 C  CB  . VAL B 1 213 ? -10.482 -13.258 22.046  1.00 11.25 ? 213 VAL B CB  1 
ATOM   3885 C  CG1 . VAL B 1 213 ? -10.601 -11.750 21.757  1.00 10.58 ? 213 VAL B CG1 1 
ATOM   3886 C  CG2 . VAL B 1 213 ? -11.738 -13.725 22.786  1.00 12.25 ? 213 VAL B CG2 1 
ATOM   3887 N  N   . LEU B 1 214 ? -9.207  -12.998 18.859  1.00 11.35 ? 214 LEU B N   1 
ATOM   3888 C  CA  . LEU B 1 214 ? -8.107  -12.476 18.004  1.00 12.93 ? 214 LEU B CA  1 
ATOM   3889 C  C   . LEU B 1 214 ? -7.607  -11.130 18.586  1.00 12.02 ? 214 LEU B C   1 
ATOM   3890 O  O   . LEU B 1 214 ? -8.401  -10.279 19.008  1.00 14.06 ? 214 LEU B O   1 
ATOM   3891 C  CB  . LEU B 1 214 ? -8.563  -12.220 16.556  1.00 15.56 ? 214 LEU B CB  1 
ATOM   3892 C  CG  . LEU B 1 214 ? -8.821  -13.546 15.762  1.00 19.90 ? 214 LEU B CG  1 
ATOM   3893 C  CD1 . LEU B 1 214 ? -8.762  -13.333 14.257  1.00 21.60 ? 214 LEU B CD1 1 
ATOM   3894 C  CD2 . LEU B 1 214 ? -7.915  -14.651 16.165  1.00 18.87 ? 214 LEU B CD2 1 
ATOM   3895 N  N   . LYS B 1 215 ? -6.318  -10.955 18.599  1.00 12.37 ? 215 LYS B N   1 
ATOM   3896 C  CA  . LYS B 1 215 ? -5.733  -9.707  19.178  1.00 12.59 ? 215 LYS B CA  1 
ATOM   3897 C  C   . LYS B 1 215 ? -5.999  -8.507  18.267  1.00 13.69 ? 215 LYS B C   1 
ATOM   3898 O  O   . LYS B 1 215 ? -6.268  -7.393  18.765  1.00 13.14 ? 215 LYS B O   1 
ATOM   3899 C  CB  . LYS B 1 215 ? -4.280  -9.897  19.393  1.00 13.31 ? 215 LYS B CB  1 
ATOM   3900 C  CG  . LYS B 1 215 ? -3.508  -8.629  19.858  1.00 15.46 ? 215 LYS B CG  1 
ATOM   3901 C  CD  . LYS B 1 215 ? -2.068  -8.912  20.211  1.00 17.97 ? 215 LYS B CD  1 
ATOM   3902 C  CE  . LYS B 1 215 ? -1.382  -7.533  20.400  1.00 22.06 ? 215 LYS B CE  1 
ATOM   3903 N  NZ  . LYS B 1 215 ? -0.001  -7.690  20.983  1.00 27.13 ? 215 LYS B NZ  1 
ATOM   3904 N  N   . GLN B 1 216 ? -5.898  -8.668  16.952  1.00 12.37 ? 216 GLN B N   1 
ATOM   3905 C  CA  . GLN B 1 216 ? -5.934  -7.483  16.074  1.00 12.93 ? 216 GLN B CA  1 
ATOM   3906 C  C   . GLN B 1 216 ? -7.331  -7.180  15.653  1.00 13.91 ? 216 GLN B C   1 
ATOM   3907 O  O   . GLN B 1 216 ? -8.055  -8.095  15.212  1.00 13.05 ? 216 GLN B O   1 
ATOM   3908 C  CB  . GLN B 1 216 ? -4.966  -7.800  14.879  1.00 14.17 ? 216 GLN B CB  1 
ATOM   3909 C  CG  . GLN B 1 216 ? -5.134  -6.658  13.830  1.00 15.33 ? 216 GLN B CG  1 
ATOM   3910 C  CD  . GLN B 1 216 ? -4.197  -6.798  12.614  1.00 20.11 ? 216 GLN B CD  1 
ATOM   3911 O  OE1 . GLN B 1 216 ? -3.791  -7.890  12.243  1.00 16.82 ? 216 GLN B OE1 1 
ATOM   3912 N  NE2 . GLN B 1 216 ? -3.962  -5.653  11.906  1.00 19.66 ? 216 GLN B NE2 1 
ATOM   3913 N  N   . PRO B 1 217 ? -7.819  -5.942  15.823  1.00 12.74 ? 217 PRO B N   1 
ATOM   3914 C  CA  . PRO B 1 217 ? -9.169  -5.573  15.368  1.00 13.49 ? 217 PRO B CA  1 
ATOM   3915 C  C   . PRO B 1 217 ? -9.248  -5.330  13.881  1.00 14.06 ? 217 PRO B C   1 
ATOM   3916 O  O   . PRO B 1 217 ? -8.179  -5.147  13.193  1.00 15.52 ? 217 PRO B O   1 
ATOM   3917 C  CB  . PRO B 1 217 ? -9.464  -4.225  16.117  1.00 14.66 ? 217 PRO B CB  1 
ATOM   3918 C  CG  . PRO B 1 217 ? -8.086  -3.666  16.241  1.00 17.58 ? 217 PRO B CG  1 
ATOM   3919 C  CD  . PRO B 1 217 ? -7.094  -4.827  16.470  1.00 15.22 ? 217 PRO B CD  1 
ATOM   3920 N  N   . ILE B 1 218 ? -10.470 -5.364  13.411  1.00 13.41 ? 218 ILE B N   1 
ATOM   3921 C  CA  . ILE B 1 218 ? -10.875 -4.876  12.052  1.00 14.26 ? 218 ILE B CA  1 
ATOM   3922 C  C   . ILE B 1 218 ? -11.554 -3.545  12.170  1.00 14.41 ? 218 ILE B C   1 
ATOM   3923 O  O   . ILE B 1 218 ? -11.928 -3.109  13.261  1.00 14.31 ? 218 ILE B O   1 
ATOM   3924 C  CB  . ILE B 1 218 ? -11.725 -5.897  11.290  1.00 14.76 ? 218 ILE B CB  1 
ATOM   3925 C  CG1 . ILE B 1 218 ? -13.108 -6.091  11.959  1.00 14.08 ? 218 ILE B CG1 1 
ATOM   3926 C  CG2 . ILE B 1 218 ? -10.986 -7.253  11.123  1.00 17.82 ? 218 ILE B CG2 1 
ATOM   3927 C  CD1 . ILE B 1 218 ? -14.061 -6.846  11.035  1.00 15.28 ? 218 ILE B CD1 1 
ATOM   3928 N  N   A ASN B 1 219 ? -11.782 -2.896  11.029  0.50 15.17 ? 219 ASN B N   1 
ATOM   3929 N  N   B ASN B 1 219 ? -11.718 -2.873  11.018  0.50 13.82 ? 219 ASN B N   1 
ATOM   3930 C  CA  A ASN B 1 219 ? -12.366 -1.580  11.067  0.50 16.86 ? 219 ASN B CA  1 
ATOM   3931 C  CA  B ASN B 1 219 ? -12.352 -1.562  10.977  0.50 14.86 ? 219 ASN B CA  1 
ATOM   3932 C  C   A ASN B 1 219 ? -13.831 -1.564  10.656  0.50 16.49 ? 219 ASN B C   1 
ATOM   3933 C  C   B ASN B 1 219 ? -13.848 -1.584  10.667  0.50 15.00 ? 219 ASN B C   1 
ATOM   3934 O  O   A ASN B 1 219 ? -14.276 -2.405  9.869   0.50 18.17 ? 219 ASN B O   1 
ATOM   3935 O  O   B ASN B 1 219 ? -14.328 -2.451  9.933   0.50 16.38 ? 219 ASN B O   1 
ATOM   3936 C  CB  A ASN B 1 219 ? -11.519 -0.665  10.152  0.50 19.16 ? 219 ASN B CB  1 
ATOM   3937 C  CB  B ASN B 1 219 ? -11.642 -0.691  9.887   0.50 14.41 ? 219 ASN B CB  1 
ATOM   3938 C  CG  A ASN B 1 219 ? -10.078 -0.608  10.594  0.50 22.23 ? 219 ASN B CG  1 
ATOM   3939 C  CG  B ASN B 1 219 ? -11.754 -1.297  8.484   0.50 15.29 ? 219 ASN B CG  1 
ATOM   3940 O  OD1 A ASN B 1 219 ? -9.767  0.040   11.587  0.50 25.37 ? 219 ASN B OD1 1 
ATOM   3941 O  OD1 B ASN B 1 219 ? -12.365 -0.704  7.538   0.50 17.56 ? 219 ASN B OD1 1 
ATOM   3942 N  ND2 A ASN B 1 219 ? -9.183  -1.290  9.853   0.50 28.22 ? 219 ASN B ND2 1 
ATOM   3943 N  ND2 B ASN B 1 219 ? -11.247 -2.498  8.347   0.50 13.36 ? 219 ASN B ND2 1 
ATOM   3944 N  N   . ILE B 1 220 ? -14.590 -0.615  11.206  1.00 15.68 ? 220 ILE B N   1 
ATOM   3945 C  CA  . ILE B 1 220 ? -15.955 -0.382  10.785  1.00 15.47 ? 220 ILE B CA  1 
ATOM   3946 C  C   . ILE B 1 220 ? -16.158 1.163   10.806  1.00 15.70 ? 220 ILE B C   1 
ATOM   3947 O  O   . ILE B 1 220 ? -15.585 1.826   11.624  1.00 15.86 ? 220 ILE B O   1 
ATOM   3948 C  CB  . ILE B 1 220 ? -16.986 -1.079  11.782  1.00 15.48 ? 220 ILE B CB  1 
ATOM   3949 C  CG1 . ILE B 1 220 ? -18.407 -0.987  11.218  1.00 16.44 ? 220 ILE B CG1 1 
ATOM   3950 C  CG2 . ILE B 1 220 ? -16.844 -0.541  13.204  1.00 16.56 ? 220 ILE B CG2 1 
ATOM   3951 C  CD1 . ILE B 1 220 ? -19.496 -1.879  11.853  1.00 15.64 ? 220 ILE B CD1 1 
ATOM   3952 N  N   . SER B 1 221 ? -16.989 1.750   9.951   1.00 17.84 ? 221 SER B N   1 
ATOM   3953 C  CA  . SER B 1 221 ? -17.278 3.174   10.144  1.00 18.67 ? 221 SER B CA  1 
ATOM   3954 C  C   . SER B 1 221 ? -18.360 3.405   11.159  1.00 19.04 ? 221 SER B C   1 
ATOM   3955 O  O   . SER B 1 221 ? -19.156 2.475   11.480  1.00 15.59 ? 221 SER B O   1 
ATOM   3956 C  CB  . SER B 1 221 ? -17.651 3.833   8.797   1.00 20.28 ? 221 SER B CB  1 
ATOM   3957 O  OG  . SER B 1 221 ? -18.961 3.338   8.371   1.00 21.43 ? 221 SER B OG  1 
ATOM   3958 N  N   A SER B 1 222 ? -18.397 4.623   11.709  0.50 17.68 ? 222 SER B N   1 
ATOM   3959 N  N   B SER B 1 222 ? -18.417 4.607   11.745  0.50 18.04 ? 222 SER B N   1 
ATOM   3960 C  CA  A SER B 1 222 ? -19.417 5.002   12.665  0.50 17.23 ? 222 SER B CA  1 
ATOM   3961 C  CA  B SER B 1 222 ? -19.486 4.919   12.687  0.50 17.86 ? 222 SER B CA  1 
ATOM   3962 C  C   A SER B 1 222 ? -20.830 4.876   12.091  0.50 19.93 ? 222 SER B C   1 
ATOM   3963 C  C   B SER B 1 222 ? -20.848 4.731   12.015  0.50 19.55 ? 222 SER B C   1 
ATOM   3964 O  O   A SER B 1 222 ? -21.749 4.492   12.832  0.50 19.70 ? 222 SER B O   1 
ATOM   3965 O  O   B SER B 1 222 ? -21.756 4.169   12.580  0.50 19.93 ? 222 SER B O   1 
ATOM   3966 C  CB  A SER B 1 222 ? -19.127 6.417   13.188  0.50 17.92 ? 222 SER B CB  1 
ATOM   3967 C  CB  B SER B 1 222 ? -19.312 6.339   13.218  0.50 19.94 ? 222 SER B CB  1 
ATOM   3968 O  OG  A SER B 1 222 ? -20.047 6.768   14.202  0.50 17.58 ? 222 SER B OG  1 
ATOM   3969 O  OG  B SER B 1 222 ? -19.032 7.210   12.153  0.50 21.51 ? 222 SER B OG  1 
ATOM   3970 N  N   . GLN B 1 223 ? -20.992 5.234   10.811  1.00 21.09 ? 223 GLN B N   1 
ATOM   3971 C  CA  . GLN B 1 223 ? -22.280 5.138   10.143  1.00 22.26 ? 223 GLN B CA  1 
ATOM   3972 C  C   . GLN B 1 223 ? -22.702 3.672   9.890   1.00 20.38 ? 223 GLN B C   1 
ATOM   3973 O  O   . GLN B 1 223 ? -23.858 3.323   10.051  1.00 20.73 ? 223 GLN B O   1 
ATOM   3974 C  CB  . GLN B 1 223 ? -22.285 5.944   8.803   1.00 30.90 ? 223 GLN B CB  1 
ATOM   3975 C  CG  . GLN B 1 223 ? -23.658 6.037   8.110   1.00 42.07 ? 223 GLN B CG  1 
ATOM   3976 C  CD  . GLN B 1 223 ? -23.650 6.028   6.563   1.00 47.57 ? 223 GLN B CD  1 
ATOM   3977 O  OE1 . GLN B 1 223 ? -22.767 5.448   5.902   1.00 61.58 ? 223 GLN B OE1 1 
ATOM   3978 N  NE2 . GLN B 1 223 ? -24.661 6.651   5.985   1.00 49.72 ? 223 GLN B NE2 1 
ATOM   3979 N  N   . GLN B 1 224 ? -21.757 2.800   9.592   1.00 16.45 ? 224 GLN B N   1 
ATOM   3980 C  CA  . GLN B 1 224 ? -22.059 1.382   9.462   1.00 16.70 ? 224 GLN B CA  1 
ATOM   3981 C  C   . GLN B 1 224 ? -22.452 0.851   10.824  1.00 17.01 ? 224 GLN B C   1 
ATOM   3982 O  O   . GLN B 1 224 ? -23.501 0.186   10.928  1.00 16.69 ? 224 GLN B O   1 
ATOM   3983 C  CB  . GLN B 1 224 ? -20.924 0.561   8.982   1.00 17.03 ? 224 GLN B CB  1 
ATOM   3984 C  CG  . GLN B 1 224 ? -20.649 0.700   7.467   1.00 21.00 ? 224 GLN B CG  1 
ATOM   3985 C  CD  . GLN B 1 224 ? -19.380 0.015   7.042   1.00 23.28 ? 224 GLN B CD  1 
ATOM   3986 O  OE1 . GLN B 1 224 ? -18.354 -0.014  7.770   1.00 20.14 ? 224 GLN B OE1 1 
ATOM   3987 N  NE2 . GLN B 1 224 ? -19.402 -0.554  5.829   1.00 23.90 ? 224 GLN B NE2 1 
ATOM   3988 N  N   . LEU B 1 225 ? -21.671 1.168   11.870  1.00 16.65 ? 225 LEU B N   1 
ATOM   3989 C  CA  . LEU B 1 225 ? -22.030 0.659   13.207  1.00 14.94 ? 225 LEU B CA  1 
ATOM   3990 C  C   . LEU B 1 225 ? -23.348 1.144   13.687  1.00 14.79 ? 225 LEU B C   1 
ATOM   3991 O  O   . LEU B 1 225 ? -24.133 0.395   14.260  1.00 13.87 ? 225 LEU B O   1 
ATOM   3992 C  CB  . LEU B 1 225 ? -20.907 1.082   14.198  1.00 14.95 ? 225 LEU B CB  1 
ATOM   3993 C  CG  . LEU B 1 225 ? -21.161 0.547   15.625  1.00 15.82 ? 225 LEU B CG  1 
ATOM   3994 C  CD1 . LEU B 1 225 ? -21.270 -1.003  15.658  1.00 16.13 ? 225 LEU B CD1 1 
ATOM   3995 C  CD2 . LEU B 1 225 ? -19.979 0.961   16.462  1.00 17.26 ? 225 LEU B CD2 1 
ATOM   3996 N  N   . ALA B 1 226 ? -23.695 2.416   13.375  1.00 14.53 ? 226 ALA B N   1 
ATOM   3997 C  CA  . ALA B 1 226 ? -24.954 2.980   13.809  1.00 15.28 ? 226 ALA B CA  1 
ATOM   3998 C  C   . ALA B 1 226 ? -26.164 2.260   13.218  1.00 15.24 ? 226 ALA B C   1 
ATOM   3999 O  O   . ALA B 1 226 ? -27.197 2.245   13.866  1.00 17.71 ? 226 ALA B O   1 
ATOM   4000 C  CB  . ALA B 1 226 ? -25.029 4.483   13.440  1.00 18.01 ? 226 ALA B CB  1 
ATOM   4001 N  N   . LYS B 1 227 ? -25.992 1.638   12.043  1.00 14.80 ? 227 LYS B N   1 
ATOM   4002 C  CA  . LYS B 1 227 ? -27.165 0.999   11.410  1.00 16.78 ? 227 LYS B CA  1 
ATOM   4003 C  C   . LYS B 1 227 ? -27.647 -0.248  12.249  1.00 14.22 ? 227 LYS B C   1 
ATOM   4004 O  O   . LYS B 1 227 ? -28.804 -0.548  12.241  1.00 17.70 ? 227 LYS B O   1 
ATOM   4005 C  CB  . LYS B 1 227 ? -26.822 0.515   10.002  1.00 19.92 ? 227 LYS B CB  1 
ATOM   4006 C  CG  . LYS B 1 227 ? -26.758 1.656   8.977   1.00 30.25 ? 227 LYS B CG  1 
ATOM   4007 C  CD  . LYS B 1 227 ? -27.511 1.339   7.672   1.00 33.66 ? 227 LYS B CD  1 
ATOM   4008 C  CE  . LYS B 1 227 ? -28.504 0.190   7.790   1.00 39.19 ? 227 LYS B CE  1 
ATOM   4009 N  NZ  . LYS B 1 227 ? -29.633 0.405   6.847   1.00 39.37 ? 227 LYS B NZ  1 
ATOM   4010 N  N   . PHE B 1 228 ? -26.737 -0.883  13.005  1.00 13.68 ? 228 PHE B N   1 
ATOM   4011 C  CA  . PHE B 1 228 ? -27.187 -2.053  13.810  1.00 11.79 ? 228 PHE B CA  1 
ATOM   4012 C  C   . PHE B 1 228 ? -28.146 -1.633  14.879  1.00 12.93 ? 228 PHE B C   1 
ATOM   4013 O  O   . PHE B 1 228 ? -29.012 -2.394  15.296  1.00 12.86 ? 228 PHE B O   1 
ATOM   4014 C  CB  . PHE B 1 228 ? -25.888 -2.717  14.358  1.00 12.23 ? 228 PHE B CB  1 
ATOM   4015 C  CG  . PHE B 1 228 ? -25.114 -3.367  13.266  1.00 12.65 ? 228 PHE B CG  1 
ATOM   4016 C  CD1 . PHE B 1 228 ? -23.960 -2.856  12.843  1.00 14.19 ? 228 PHE B CD1 1 
ATOM   4017 C  CD2 . PHE B 1 228 ? -25.660 -4.510  12.605  1.00 12.21 ? 228 PHE B CD2 1 
ATOM   4018 C  CE1 . PHE B 1 228 ? -23.242 -3.464  11.811  1.00 14.10 ? 228 PHE B CE1 1 
ATOM   4019 C  CE2 . PHE B 1 228 ? -24.900 -5.156  11.616  1.00 13.98 ? 228 PHE B CE2 1 
ATOM   4020 C  CZ  . PHE B 1 228 ? -23.729 -4.592  11.179  1.00 14.62 ? 228 PHE B CZ  1 
ATOM   4021 N  N   . ARG B 1 229 ? -27.922 -0.388  15.439  1.00 12.46 ? 229 ARG B N   1 
ATOM   4022 C  CA  . ARG B 1 229 ? -28.790 0.086   16.523  1.00 13.46 ? 229 ARG B CA  1 
ATOM   4023 C  C   . ARG B 1 229 ? -30.250 0.368   16.119  1.00 14.83 ? 229 ARG B C   1 
ATOM   4024 O  O   . ARG B 1 229 ? -31.149 0.524   17.010  1.00 15.28 ? 229 ARG B O   1 
ATOM   4025 C  CB  . ARG B 1 229 ? -28.177 1.364   17.101  1.00 12.60 ? 229 ARG B CB  1 
ATOM   4026 C  CG  . ARG B 1 229 ? -26.731 1.185   17.569  1.00 12.88 ? 229 ARG B CG  1 
ATOM   4027 C  CD  . ARG B 1 229 ? -26.328 2.393   18.496  1.00 14.86 ? 229 ARG B CD  1 
ATOM   4028 N  NE  . ARG B 1 229 ? -24.944 2.221   18.850  1.00 13.88 ? 229 ARG B NE  1 
ATOM   4029 C  CZ  . ARG B 1 229 ? -23.895 2.744   18.187  1.00 13.71 ? 229 ARG B CZ  1 
ATOM   4030 N  NH1 . ARG B 1 229 ? -24.081 3.684   17.200  1.00 19.05 ? 229 ARG B NH1 1 
ATOM   4031 N  NH2 . ARG B 1 229 ? -22.645 2.438   18.536  1.00 15.05 ? 229 ARG B NH2 1 
ATOM   4032 N  N   A SER B 1 230 ? -30.551 0.408   14.820  0.50 14.93 ? 230 SER B N   1 
ATOM   4033 N  N   B SER B 1 230 ? -30.454 0.399   14.809  0.50 14.94 ? 230 SER B N   1 
ATOM   4034 C  CA  A SER B 1 230 ? -31.940 0.566   14.399  0.50 16.69 ? 230 SER B CA  1 
ATOM   4035 C  CA  B SER B 1 230 ? -31.756 0.557   14.255  0.50 16.64 ? 230 SER B CA  1 
ATOM   4036 C  C   A SER B 1 230 ? -32.722 -0.758  14.312  0.50 15.71 ? 230 SER B C   1 
ATOM   4037 C  C   B SER B 1 230 ? -32.577 -0.725  14.048  0.50 15.65 ? 230 SER B C   1 
ATOM   4038 O  O   A SER B 1 230 ? -33.955 -0.746  14.159  0.50 16.91 ? 230 SER B O   1 
ATOM   4039 O  O   B SER B 1 230 ? -33.689 -0.637  13.601  0.50 14.95 ? 230 SER B O   1 
ATOM   4040 C  CB  A SER B 1 230 ? -32.059 1.278   13.022  0.50 17.42 ? 230 SER B CB  1 
ATOM   4041 C  CB  B SER B 1 230 ? -31.674 1.370   12.944  0.50 17.58 ? 230 SER B CB  1 
ATOM   4042 O  OG  A SER B 1 230 ? -31.405 0.541   11.992  0.50 18.49 ? 230 SER B OG  1 
ATOM   4043 O  OG  B SER B 1 230 ? -31.759 2.742   13.288  0.50 19.92 ? 230 SER B OG  1 
ATOM   4044 N  N   . LEU B 1 231 ? -32.000 -1.892  14.374  1.00 15.65 ? 231 LEU B N   1 
ATOM   4045 C  CA  . LEU B 1 231 ? -32.729 -3.128  14.454  1.00 16.06 ? 231 LEU B CA  1 
ATOM   4046 C  C   . LEU B 1 231 ? -33.607 -3.093  15.718  1.00 15.42 ? 231 LEU B C   1 
ATOM   4047 O  O   . LEU B 1 231 ? -33.220 -2.461  16.754  1.00 15.79 ? 231 LEU B O   1 
ATOM   4048 C  CB  . LEU B 1 231 ? -31.727 -4.282  14.652  1.00 13.23 ? 231 LEU B CB  1 
ATOM   4049 C  CG  . LEU B 1 231 ? -30.895 -4.581  13.432  1.00 14.79 ? 231 LEU B CG  1 
ATOM   4050 C  CD1 . LEU B 1 231 ? -29.876 -5.645  13.824  1.00 15.30 ? 231 LEU B CD1 1 
ATOM   4051 C  CD2 . LEU B 1 231 ? -31.727 -4.976  12.198  1.00 17.21 ? 231 LEU B CD2 1 
ATOM   4052 N  N   . LEU B 1 232 ? -34.817 -3.668  15.644  1.00 14.67 ? 232 LEU B N   1 
ATOM   4053 C  CA  . LEU B 1 232 ? -35.692 -3.760  16.808  1.00 15.91 ? 232 LEU B CA  1 
ATOM   4054 C  C   . LEU B 1 232 ? -35.480 -5.042  17.593  1.00 16.89 ? 232 LEU B C   1 
ATOM   4055 O  O   . LEU B 1 232 ? -35.152 -6.092  16.978  1.00 15.95 ? 232 LEU B O   1 
ATOM   4056 C  CB  . LEU B 1 232 ? -37.178 -3.714  16.449  1.00 16.57 ? 232 LEU B CB  1 
ATOM   4057 C  CG  . LEU B 1 232 ? -37.539 -2.489  15.555  1.00 20.47 ? 232 LEU B CG  1 
ATOM   4058 C  CD1 . LEU B 1 232 ? -39.032 -2.612  15.202  1.00 21.72 ? 232 LEU B CD1 1 
ATOM   4059 C  CD2 . LEU B 1 232 ? -37.263 -1.219  16.358  1.00 22.61 ? 232 LEU B CD2 1 
ATOM   4060 N  N   . CYS B 1 233 ? -35.687 -4.962  18.924  1.00 15.17 ? 233 CYS B N   1 
ATOM   4061 C  CA  . CYS B 1 233 ? -35.714 -6.199  19.760  1.00 17.10 ? 233 CYS B CA  1 
ATOM   4062 C  C   . CYS B 1 233 ? -37.140 -6.720  19.889  1.00 17.65 ? 233 CYS B C   1 
ATOM   4063 O  O   . CYS B 1 233 ? -37.406 -7.720  20.612  1.00 20.70 ? 233 CYS B O   1 
ATOM   4064 C  CB  . CYS B 1 233 ? -34.995 -5.985  21.116  1.00 15.09 ? 233 CYS B CB  1 
ATOM   4065 S  SG  . CYS B 1 233 ? -35.889 -4.738  22.097  1.00 20.98 ? 233 CYS B SG  1 
ATOM   4066 N  N   . THR B 1 234 ? -38.057 -6.096  19.107  1.00 18.78 ? 234 THR B N   1 
ATOM   4067 C  CA  . THR B 1 234 ? -39.475 -6.394  19.142  1.00 18.20 ? 234 THR B CA  1 
ATOM   4068 C  C   . THR B 1 234 ? -39.986 -6.852  17.756  1.00 22.11 ? 234 THR B C   1 
ATOM   4069 O  O   . THR B 1 234 ? -39.428 -6.487  16.682  1.00 21.46 ? 234 THR B O   1 
ATOM   4070 C  CB  . THR B 1 234 ? -40.295 -5.125  19.612  1.00 18.88 ? 234 THR B CB  1 
ATOM   4071 O  OG1 . THR B 1 234 ? -39.949 -4.023  18.809  1.00 20.17 ? 234 THR B OG1 1 
ATOM   4072 C  CG2 . THR B 1 234 ? -40.006 -4.760  21.055  1.00 19.77 ? 234 THR B CG2 1 
ATOM   4073 N  N   . ALA B 1 235 ? -41.058 -7.619  17.809  1.00 26.93 ? 235 ALA B N   1 
ATOM   4074 C  CA  . ALA B 1 235 ? -41.692 -8.156  16.592  1.00 34.09 ? 235 ALA B CA  1 
ATOM   4075 C  C   . ALA B 1 235 ? -42.615 -7.147  15.904  1.00 43.12 ? 235 ALA B C   1 
ATOM   4076 O  O   . ALA B 1 235 ? -42.922 -6.085  16.436  1.00 41.59 ? 235 ALA B O   1 
ATOM   4077 C  CB  . ALA B 1 235 ? -42.435 -9.435  16.915  1.00 34.41 ? 235 ALA B CB  1 
ATOM   4078 N  N   . GLU B 1 236 ? -43.019 -7.462  14.682  1.00 49.48 ? 236 GLU B N   1 
ATOM   4079 C  CA  . GLU B 1 236 ? -44.016 -6.636  14.028  1.00 54.41 ? 236 GLU B CA  1 
ATOM   4080 C  C   . GLU B 1 236 ? -45.307 -6.834  14.819  1.00 46.18 ? 236 GLU B C   1 
ATOM   4081 O  O   . GLU B 1 236 ? -45.609 -7.964  15.269  1.00 42.70 ? 236 GLU B O   1 
ATOM   4082 C  CB  . GLU B 1 236 ? -44.179 -7.070  12.579  1.00 65.37 ? 236 GLU B CB  1 
ATOM   4083 C  CG  . GLU B 1 236 ? -44.586 -5.961  11.629  1.00 71.24 ? 236 GLU B CG  1 
ATOM   4084 C  CD  . GLU B 1 236 ? -44.597 -6.445  10.192  1.00 77.70 ? 236 GLU B CD  1 
ATOM   4085 O  OE1 . GLU B 1 236 ? -44.506 -7.679  9.965   1.00 72.78 ? 236 GLU B OE1 1 
ATOM   4086 O  OE2 . GLU B 1 236 ? -44.690 -5.587  9.291   1.00 81.85 ? 236 GLU B OE2 1 
ATOM   4087 N  N   . GLY B 1 237 ? -46.014 -5.726  15.027  1.00 52.46 ? 237 GLY B N   1 
ATOM   4088 C  CA  . GLY B 1 237 ? -47.259 -5.706  15.828  1.00 57.56 ? 237 GLY B CA  1 
ATOM   4089 C  C   . GLY B 1 237 ? -47.112 -5.624  17.349  1.00 58.53 ? 237 GLY B C   1 
ATOM   4090 O  O   . GLY B 1 237 ? -48.105 -5.519  18.075  1.00 58.27 ? 237 GLY B O   1 
ATOM   4091 N  N   . GLU B 1 238 ? -45.876 -5.702  17.836  1.00 52.80 ? 238 GLU B N   1 
ATOM   4092 C  CA  . GLU B 1 238 ? -45.555 -5.518  19.252  1.00 46.58 ? 238 GLU B CA  1 
ATOM   4093 C  C   . GLU B 1 238 ? -45.068 -4.038  19.313  1.00 42.42 ? 238 GLU B C   1 
ATOM   4094 O  O   . GLU B 1 238 ? -44.661 -3.502  18.283  1.00 45.84 ? 238 GLU B O   1 
ATOM   4095 C  CB  . GLU B 1 238 ? -44.497 -6.569  19.640  1.00 46.06 ? 238 GLU B CB  1 
ATOM   4096 C  CG  . GLU B 1 238 ? -43.858 -6.414  21.021  1.00 52.88 ? 238 GLU B CG  1 
ATOM   4097 C  CD  . GLU B 1 238 ? -42.724 -7.418  21.334  1.00 54.85 ? 238 GLU B CD  1 
ATOM   4098 O  OE1 . GLU B 1 238 ? -42.414 -7.551  22.562  1.00 45.90 ? 238 GLU B OE1 1 
ATOM   4099 O  OE2 . GLU B 1 238 ? -42.146 -8.048  20.388  1.00 41.64 ? 238 GLU B OE2 1 
ATOM   4100 N  N   . ALA B 1 239 ? -45.153 -3.345  20.458  1.00 37.15 ? 239 ALA B N   1 
ATOM   4101 C  CA  . ALA B 1 239 ? -44.620 -1.948  20.534  1.00 38.13 ? 239 ALA B CA  1 
ATOM   4102 C  C   . ALA B 1 239 ? -43.067 -1.876  20.405  1.00 33.16 ? 239 ALA B C   1 
ATOM   4103 O  O   . ALA B 1 239 ? -42.384 -2.558  21.148  1.00 33.48 ? 239 ALA B O   1 
ATOM   4104 C  CB  . ALA B 1 239 ? -45.028 -1.280  21.845  1.00 40.54 ? 239 ALA B CB  1 
ATOM   4105 N  N   . ALA B 1 240 ? -42.585 -0.984  19.545  1.00 29.39 ? 240 ALA B N   1 
ATOM   4106 C  CA  . ALA B 1 240 ? -41.186 -0.885  19.106  1.00 32.90 ? 240 ALA B CA  1 
ATOM   4107 C  C   . ALA B 1 240 ? -40.151 -0.469  20.157  1.00 27.10 ? 240 ALA B C   1 
ATOM   4108 O  O   . ALA B 1 240 ? -40.259 0.579   20.810  1.00 27.60 ? 240 ALA B O   1 
ATOM   4109 C  CB  . ALA B 1 240 ? -41.058 -0.014  17.864  1.00 32.20 ? 240 ALA B CB  1 
ATOM   4110 N  N   . ALA B 1 241 ? -39.110 -1.300  20.271  1.00 20.90 ? 241 ALA B N   1 
ATOM   4111 C  CA  . ALA B 1 241 ? -37.963 -1.002  21.160  1.00 17.73 ? 241 ALA B CA  1 
ATOM   4112 C  C   . ALA B 1 241 ? -36.707 -1.357  20.359  1.00 16.68 ? 241 ALA B C   1 
ATOM   4113 O  O   . ALA B 1 241 ? -36.752 -2.321  19.605  1.00 18.97 ? 241 ALA B O   1 
ATOM   4114 C  CB  . ALA B 1 241 ? -38.057 -1.775  22.439  1.00 16.66 ? 241 ALA B CB  1 
ATOM   4115 N  N   . PHE B 1 242 ? -35.703 -0.488  20.376  1.00 16.43 ? 242 PHE B N   1 
ATOM   4116 C  CA  . PHE B 1 242 ? -34.511 -0.597  19.558  1.00 14.95 ? 242 PHE B CA  1 
ATOM   4117 C  C   . PHE B 1 242 ? -33.428 -1.379  20.238  1.00 15.48 ? 242 PHE B C   1 
ATOM   4118 O  O   . PHE B 1 242 ? -33.204 -1.245  21.442  1.00 16.83 ? 242 PHE B O   1 
ATOM   4119 C  CB  . PHE B 1 242 ? -33.998 0.814   19.197  1.00 15.31 ? 242 PHE B CB  1 
ATOM   4120 C  CG  . PHE B 1 242 ? -34.919 1.518   18.287  1.00 17.67 ? 242 PHE B CG  1 
ATOM   4121 C  CD1 . PHE B 1 242 ? -35.909 2.358   18.784  1.00 18.21 ? 242 PHE B CD1 1 
ATOM   4122 C  CD2 . PHE B 1 242 ? -34.758 1.351   16.916  1.00 16.14 ? 242 PHE B CD2 1 
ATOM   4123 C  CE1 . PHE B 1 242 ? -36.796 3.029   17.933  1.00 20.68 ? 242 PHE B CE1 1 
ATOM   4124 C  CE2 . PHE B 1 242 ? -35.641 2.026   16.042  1.00 18.52 ? 242 PHE B CE2 1 
ATOM   4125 C  CZ  . PHE B 1 242 ? -36.602 2.894   16.564  1.00 18.16 ? 242 PHE B CZ  1 
ATOM   4126 N  N   . LEU B 1 243 ? -32.673 -2.117  19.419  1.00 14.07 ? 243 LEU B N   1 
ATOM   4127 C  CA  . LEU B 1 243 ? -31.523 -2.911  19.949  1.00 14.63 ? 243 LEU B CA  1 
ATOM   4128 C  C   . LEU B 1 243 ? -30.325 -1.971  19.934  1.00 13.63 ? 243 LEU B C   1 
ATOM   4129 O  O   . LEU B 1 243 ? -29.354 -2.130  19.195  1.00 13.23 ? 243 LEU B O   1 
ATOM   4130 C  CB  . LEU B 1 243 ? -31.316 -4.163  19.064  1.00 14.10 ? 243 LEU B CB  1 
ATOM   4131 C  CG  . LEU B 1 243 ? -30.315 -5.173  19.658  1.00 13.29 ? 243 LEU B CG  1 
ATOM   4132 C  CD1 . LEU B 1 243 ? -30.834 -5.771  20.953  1.00 16.26 ? 243 LEU B CD1 1 
ATOM   4133 C  CD2 . LEU B 1 243 ? -30.306 -6.261  18.565  1.00 14.05 ? 243 LEU B CD2 1 
ATOM   4134 N  N   . VAL B 1 244 ? -30.308 -1.007  20.852  1.00 14.02 ? 244 VAL B N   1 
ATOM   4135 C  CA  . VAL B 1 244 ? -29.159 -0.050  20.873  1.00 12.75 ? 244 VAL B CA  1 
ATOM   4136 C  C   . VAL B 1 244 ? -27.836 -0.506  21.472  1.00 11.77 ? 244 VAL B C   1 
ATOM   4137 O  O   . VAL B 1 244 ? -26.720 -0.009  21.136  1.00 13.71 ? 244 VAL B O   1 
ATOM   4138 C  CB  . VAL B 1 244 ? -29.577 1.300   21.550  1.00 13.95 ? 244 VAL B CB  1 
ATOM   4139 C  CG1 . VAL B 1 244 ? -30.799 1.931   20.810  1.00 16.24 ? 244 VAL B CG1 1 
ATOM   4140 C  CG2 . VAL B 1 244 ? -29.817 1.084   22.990  1.00 15.39 ? 244 VAL B CG2 1 
ATOM   4141 N  N   . SER B 1 245 ? -27.996 -1.611  22.218  1.00 12.27 ? 245 SER B N   1 
ATOM   4142 C  CA  . SER B 1 245 ? -26.870 -2.237  22.918  1.00 12.52 ? 245 SER B CA  1 
ATOM   4143 C  C   . SER B 1 245 ? -27.234 -3.694  23.178  1.00 11.26 ? 245 SER B C   1 
ATOM   4144 O  O   . SER B 1 245 ? -28.352 -4.039  23.591  1.00 13.46 ? 245 SER B O   1 
ATOM   4145 C  CB  . SER B 1 245 ? -26.700 -1.550  24.279  1.00 15.51 ? 245 SER B CB  1 
ATOM   4146 O  OG  . SER B 1 245 ? -25.452 -1.989  24.871  1.00 14.20 ? 245 SER B OG  1 
ATOM   4147 N  N   . ASN B 1 246 ? -26.224 -4.574  22.972  1.00 11.79 ? 246 ASN B N   1 
ATOM   4148 C  CA  . ASN B 1 246 ? -26.425 -6.013  23.211  1.00 11.64 ? 246 ASN B CA  1 
ATOM   4149 C  C   . ASN B 1 246 ? -25.115 -6.669  23.623  1.00 13.30 ? 246 ASN B C   1 
ATOM   4150 O  O   . ASN B 1 246 ? -24.796 -7.804  23.155  1.00 13.20 ? 246 ASN B O   1 
ATOM   4151 C  CB  . ASN B 1 246 ? -27.012 -6.695  21.938  1.00 12.56 ? 246 ASN B CB  1 
ATOM   4152 C  CG  . ASN B 1 246 ? -26.056 -6.627  20.753  1.00 12.49 ? 246 ASN B CG  1 
ATOM   4153 O  OD1 . ASN B 1 246 ? -25.079 -5.941  20.794  1.00 12.30 ? 246 ASN B OD1 1 
ATOM   4154 N  ND2 . ASN B 1 246 ? -26.415 -7.345  19.656  1.00 10.81 ? 246 ASN B ND2 1 
ATOM   4155 N  N   . HIS B 1 247 ? -24.339 -6.035  24.497  1.00 13.39 ? 247 HIS B N   1 
ATOM   4156 C  CA  . HIS B 1 247 ? -23.165 -6.703  25.064  1.00 13.03 ? 247 HIS B CA  1 
ATOM   4157 C  C   . HIS B 1 247 ? -23.319 -7.023  26.527  1.00 14.31 ? 247 HIS B C   1 
ATOM   4158 O  O   . HIS B 1 247 ? -23.887 -6.197  27.274  1.00 14.40 ? 247 HIS B O   1 
ATOM   4159 C  CB  . HIS B 1 247 ? -21.901 -5.903  24.771  1.00 13.37 ? 247 HIS B CB  1 
ATOM   4160 C  CG  . HIS B 1 247 ? -21.926 -4.516  25.376  1.00 13.62 ? 247 HIS B CG  1 
ATOM   4161 N  ND1 . HIS B 1 247 ? -21.248 -4.176  26.498  1.00 18.31 ? 247 HIS B ND1 1 
ATOM   4162 C  CD2 . HIS B 1 247 ? -22.548 -3.381  24.939  1.00 13.20 ? 247 HIS B CD2 1 
ATOM   4163 C  CE1 . HIS B 1 247 ? -21.456 -2.831  26.776  1.00 16.28 ? 247 HIS B CE1 1 
ATOM   4164 N  NE2 . HIS B 1 247 ? -22.248 -2.365  25.863  1.00 16.72 ? 247 HIS B NE2 1 
ATOM   4165 N  N   . ARG B 1 248 ? -22.856 -8.191  26.971  1.00 11.02 ? 248 ARG B N   1 
ATOM   4166 C  CA  . ARG B 1 248 ? -22.865 -8.549  28.389  1.00 10.76 ? 248 ARG B CA  1 
ATOM   4167 C  C   . ARG B 1 248 ? -21.616 -7.984  29.073  1.00 10.77 ? 248 ARG B C   1 
ATOM   4168 O  O   . ARG B 1 248 ? -20.565 -8.003  28.511  1.00 12.80 ? 248 ARG B O   1 
ATOM   4169 C  CB  . ARG B 1 248 ? -22.809 -10.079 28.494  1.00 11.13 ? 248 ARG B CB  1 
ATOM   4170 C  CG  . ARG B 1 248 ? -23.143 -10.575 29.945  1.00 10.54 ? 248 ARG B CG  1 
ATOM   4171 C  CD  . ARG B 1 248 ? -22.930 -12.095 30.034  1.00 11.24 ? 248 ARG B CD  1 
ATOM   4172 N  NE  . ARG B 1 248 ? -23.455 -12.545 31.327  1.00 12.39 ? 248 ARG B NE  1 
ATOM   4173 C  CZ  . ARG B 1 248 ? -23.177 -13.692 31.928  1.00 13.23 ? 248 ARG B CZ  1 
ATOM   4174 N  NH1 . ARG B 1 248 ? -22.368 -14.583 31.376  1.00 11.87 ? 248 ARG B NH1 1 
ATOM   4175 N  NH2 . ARG B 1 248 ? -23.720 -13.956 33.110  1.00 13.80 ? 248 ARG B NH2 1 
ATOM   4176 N  N   . PRO B 1 249 ? -21.733 -7.496  30.324  1.00 11.76 ? 249 PRO B N   1 
ATOM   4177 C  CA  . PRO B 1 249 ? -20.539 -7.079  31.063  1.00 13.54 ? 249 PRO B CA  1 
ATOM   4178 C  C   . PRO B 1 249 ? -19.552 -8.207  31.267  1.00 13.14 ? 249 PRO B C   1 
ATOM   4179 O  O   . PRO B 1 249 ? -19.979 -9.379  31.237  1.00 12.69 ? 249 PRO B O   1 
ATOM   4180 C  CB  . PRO B 1 249 ? -21.125 -6.587  32.427  1.00 13.39 ? 249 PRO B CB  1 
ATOM   4181 C  CG  . PRO B 1 249 ? -22.504 -6.194  32.115  1.00 14.82 ? 249 PRO B CG  1 
ATOM   4182 C  CD  . PRO B 1 249 ? -22.978 -7.229  31.085  1.00 14.90 ? 249 PRO B CD  1 
ATOM   4183 N  N   . PRO B 1 250 ? -18.272 -7.885  31.481  1.00 15.72 ? 250 PRO B N   1 
ATOM   4184 C  CA  . PRO B 1 250 ? -17.256 -8.879  31.820  1.00 14.06 ? 250 PRO B CA  1 
ATOM   4185 C  C   . PRO B 1 250 ? -17.630 -9.565  33.159  1.00 12.73 ? 250 PRO B C   1 
ATOM   4186 O  O   . PRO B 1 250 ? -18.232 -8.959  34.097  1.00 14.33 ? 250 PRO B O   1 
ATOM   4187 C  CB  . PRO B 1 250 ? -15.967 -8.084  32.034  1.00 16.16 ? 250 PRO B CB  1 
ATOM   4188 C  CG  . PRO B 1 250 ? -16.504 -6.731  32.473  1.00 18.94 ? 250 PRO B CG  1 
ATOM   4189 C  CD  . PRO B 1 250 ? -17.831 -6.491  31.781  1.00 19.50 ? 250 PRO B CD  1 
ATOM   4190 N  N   . GLN B 1 251 ? -17.295 -10.858 33.211  1.00 12.37 ? 251 GLN B N   1 
ATOM   4191 C  CA  . GLN B 1 251 ? -17.698 -11.729 34.347  1.00 12.13 ? 251 GLN B CA  1 
ATOM   4192 C  C   . GLN B 1 251 ? -16.439 -12.203 35.088  1.00 13.50 ? 251 GLN B C   1 
ATOM   4193 O  O   . GLN B 1 251 ? -15.302 -12.129 34.580  1.00 13.97 ? 251 GLN B O   1 
ATOM   4194 C  CB  . GLN B 1 251 ? -18.468 -12.970 33.802  1.00 11.31 ? 251 GLN B CB  1 
ATOM   4195 C  CG  . GLN B 1 251 ? -19.722 -12.567 33.043  1.00 12.25 ? 251 GLN B CG  1 
ATOM   4196 C  CD  . GLN B 1 251 ? -20.705 -11.808 33.905  1.00 14.15 ? 251 GLN B CD  1 
ATOM   4197 O  OE1 . GLN B 1 251 ? -21.060 -12.302 34.979  1.00 16.94 ? 251 GLN B OE1 1 
ATOM   4198 N  NE2 . GLN B 1 251 ? -21.210 -10.643 33.418  1.00 15.11 ? 251 GLN B NE2 1 
ATOM   4199 N  N   . PRO B 1 252 ? -16.614 -12.658 36.349  1.00 12.36 ? 252 PRO B N   1 
ATOM   4200 C  CA  . PRO B 1 252 ? -15.461 -13.044 37.201  1.00 14.12 ? 252 PRO B CA  1 
ATOM   4201 C  C   . PRO B 1 252 ? -14.601 -14.138 36.549  1.00 13.83 ? 252 PRO B C   1 
ATOM   4202 O  O   . PRO B 1 252 ? -15.142 -15.150 36.070  1.00 13.21 ? 252 PRO B O   1 
ATOM   4203 C  CB  . PRO B 1 252 ? -16.182 -13.560 38.477  1.00 13.59 ? 252 PRO B CB  1 
ATOM   4204 C  CG  . PRO B 1 252 ? -17.480 -12.892 38.457  1.00 16.37 ? 252 PRO B CG  1 
ATOM   4205 C  CD  . PRO B 1 252 ? -17.927 -12.749 37.038  1.00 15.74 ? 252 PRO B CD  1 
ATOM   4206 N  N   . LEU B 1 253 ? -13.287 -13.957 36.548  1.00 13.82 ? 253 LEU B N   1 
ATOM   4207 C  CA  . LEU B 1 253 ? -12.380 -14.957 35.985  1.00 15.47 ? 253 LEU B CA  1 
ATOM   4208 C  C   . LEU B 1 253 ? -12.401 -16.276 36.735  1.00 14.57 ? 253 LEU B C   1 
ATOM   4209 O  O   . LEU B 1 253 ? -12.244 -17.353 36.132  1.00 13.23 ? 253 LEU B O   1 
ATOM   4210 C  CB  . LEU B 1 253 ? -10.975 -14.415 35.797  1.00 15.58 ? 253 LEU B CB  1 
ATOM   4211 C  CG  . LEU B 1 253 ? -9.950  -15.113 34.883  1.00 20.27 ? 253 LEU B CG  1 
ATOM   4212 C  CD1 . LEU B 1 253 ? -10.474 -15.199 33.418  1.00 19.41 ? 253 LEU B CD1 1 
ATOM   4213 C  CD2 . LEU B 1 253 ? -8.563  -14.429 34.972  1.00 24.08 ? 253 LEU B CD2 1 
ATOM   4214 N  N   . LYS B 1 254 ? -12.604 -16.212 38.060  1.00 15.07 ? 254 LYS B N   1 
ATOM   4215 C  CA  . LYS B 1 254 ? -12.641 -17.451 38.925  1.00 15.59 ? 254 LYS B CA  1 
ATOM   4216 C  C   . LYS B 1 254 ? -11.387 -18.342 38.711  1.00 15.30 ? 254 LYS B C   1 
ATOM   4217 O  O   . LYS B 1 254 ? -11.511 -19.549 38.740  1.00 17.56 ? 254 LYS B O   1 
ATOM   4218 C  CB  . LYS B 1 254 ? -13.947 -18.131 38.826  1.00 16.53 ? 254 LYS B CB  1 
ATOM   4219 C  CG  . LYS B 1 254 ? -15.008 -17.190 39.488  1.00 20.29 ? 254 LYS B CG  1 
ATOM   4220 C  CD  . LYS B 1 254 ? -16.377 -17.856 39.564  1.00 21.74 ? 254 LYS B CD  1 
ATOM   4221 C  CE  . LYS B 1 254 ? -17.330 -17.032 40.382  1.00 22.46 ? 254 LYS B CE  1 
ATOM   4222 N  NZ  . LYS B 1 254 ? -18.705 -17.607 40.159  1.00 24.52 ? 254 LYS B NZ  1 
ATOM   4223 N  N   . GLY B 1 255 ? -10.229 -17.742 38.538  1.00 14.76 ? 255 GLY B N   1 
ATOM   4224 C  CA  . GLY B 1 255 ? -8.990  -18.500 38.425  1.00 17.60 ? 255 GLY B CA  1 
ATOM   4225 C  C   . GLY B 1 255 ? -8.677  -19.100 37.078  1.00 15.46 ? 255 GLY B C   1 
ATOM   4226 O  O   . GLY B 1 255 ? -7.665  -19.732 36.910  1.00 15.08 ? 255 GLY B O   1 
ATOM   4227 N  N   . ARG B 1 256 ? -9.552  -18.900 36.099  1.00 13.19 ? 256 ARG B N   1 
ATOM   4228 C  CA  . ARG B 1 256 ? -9.263  -19.439 34.776  1.00 13.28 ? 256 ARG B CA  1 
ATOM   4229 C  C   . ARG B 1 256 ? -8.044  -18.848 34.186  1.00 13.24 ? 256 ARG B C   1 
ATOM   4230 O  O   . ARG B 1 256 ? -7.687  -17.709 34.416  1.00 15.44 ? 256 ARG B O   1 
ATOM   4231 C  CB  . ARG B 1 256 ? -10.444 -19.140 33.822  1.00 11.18 ? 256 ARG B CB  1 
ATOM   4232 C  CG  . ARG B 1 256 ? -11.647 -20.031 34.182  1.00 11.06 ? 256 ARG B CG  1 
ATOM   4233 C  CD  . ARG B 1 256 ? -12.841 -19.704 33.291  1.00 11.44 ? 256 ARG B CD  1 
ATOM   4234 N  NE  . ARG B 1 256 ? -13.450 -18.455 33.740  1.00 10.18 ? 256 ARG B NE  1 
ATOM   4235 C  CZ  . ARG B 1 256 ? -14.395 -17.769 33.086  1.00 9.91  ? 256 ARG B CZ  1 
ATOM   4236 N  NH1 . ARG B 1 256 ? -14.869 -18.211 31.932  1.00 11.00 ? 256 ARG B NH1 1 
ATOM   4237 N  NH2 . ARG B 1 256 ? -14.858 -16.638 33.599  1.00 9.99  ? 256 ARG B NH2 1 
ATOM   4238 N  N   . LYS B 1 257 ? -7.334  -19.713 33.407  1.00 15.28 ? 257 LYS B N   1 
ATOM   4239 C  CA  . LYS B 1 257 ? -6.093  -19.348 32.731  1.00 16.46 ? 257 LYS B CA  1 
ATOM   4240 C  C   . LYS B 1 257 ? -6.379  -18.892 31.280  1.00 15.55 ? 257 LYS B C   1 
ATOM   4241 O  O   . LYS B 1 257 ? -6.976  -19.615 30.516  1.00 18.45 ? 257 LYS B O   1 
ATOM   4242 C  CB  . LYS B 1 257 ? -5.157  -20.574 32.742  1.00 21.00 ? 257 LYS B CB  1 
ATOM   4243 C  CG  . LYS B 1 257 ? -3.822  -20.232 32.044  1.00 21.34 ? 257 LYS B CG  1 
ATOM   4244 C  CD  . LYS B 1 257 ? -2.980  -21.438 31.619  1.00 30.44 ? 257 LYS B CD  1 
ATOM   4245 C  CE  . LYS B 1 257 ? -2.348  -22.114 32.793  1.00 34.18 ? 257 LYS B CE  1 
ATOM   4246 N  NZ  . LYS B 1 257 ? -2.265  -23.549 32.387  1.00 38.07 ? 257 LYS B NZ  1 
ATOM   4247 N  N   . VAL B 1 258 ? -6.032  -17.638 30.984  1.00 14.46 ? 258 VAL B N   1 
ATOM   4248 C  CA  . VAL B 1 258 ? -6.127  -17.105 29.620  1.00 15.53 ? 258 VAL B CA  1 
ATOM   4249 C  C   . VAL B 1 258 ? -4.754  -17.300 28.971  1.00 14.18 ? 258 VAL B C   1 
ATOM   4250 O  O   . VAL B 1 258 ? -3.763  -16.840 29.539  1.00 15.98 ? 258 VAL B O   1 
ATOM   4251 C  CB  . VAL B 1 258 ? -6.510  -15.594 29.618  1.00 13.70 ? 258 VAL B CB  1 
ATOM   4252 C  CG1 . VAL B 1 258 ? -6.595  -15.134 28.157  1.00 14.03 ? 258 VAL B CG1 1 
ATOM   4253 C  CG2 . VAL B 1 258 ? -7.853  -15.346 30.378  1.00 16.84 ? 258 VAL B CG2 1 
ATOM   4254 N  N   . ARG B 1 259 ? -4.709  -18.020 27.833  1.00 13.05 ? 259 ARG B N   1 
ATOM   4255 C  CA  . ARG B 1 259 ? -3.453  -18.347 27.196  1.00 13.31 ? 259 ARG B CA  1 
ATOM   4256 C  C   . ARG B 1 259 ? -3.309  -17.548 25.948  1.00 14.32 ? 259 ARG B C   1 
ATOM   4257 O  O   . ARG B 1 259 ? -4.319  -17.209 25.349  1.00 16.26 ? 259 ARG B O   1 
ATOM   4258 C  CB  . ARG B 1 259 ? -3.408  -19.853 26.896  1.00 13.96 ? 259 ARG B CB  1 
ATOM   4259 C  CG  . ARG B 1 259 ? -3.363  -20.685 28.158  1.00 13.94 ? 259 ARG B CG  1 
ATOM   4260 C  CD  . ARG B 1 259 ? -3.280  -22.198 27.870  1.00 13.56 ? 259 ARG B CD  1 
ATOM   4261 N  NE  . ARG B 1 259 ? -4.521  -22.677 27.254  1.00 14.48 ? 259 ARG B NE  1 
ATOM   4262 C  CZ  . ARG B 1 259 ? -4.643  -23.725 26.443  1.00 14.81 ? 259 ARG B CZ  1 
ATOM   4263 N  NH1 . ARG B 1 259 ? -3.586  -24.467 26.116  1.00 17.42 ? 259 ARG B NH1 1 
ATOM   4264 N  NH2 . ARG B 1 259 ? -5.835  -24.041 25.960  1.00 14.25 ? 259 ARG B NH2 1 
ATOM   4265 N  N   . ALA B 1 260 ? -2.062  -17.313 25.526  1.00 14.49 ? 260 ALA B N   1 
ATOM   4266 C  CA  . ALA B 1 260 ? -1.796  -16.604 24.298  1.00 17.06 ? 260 ALA B CA  1 
ATOM   4267 C  C   . ALA B 1 260 ? -1.057  -17.489 23.320  1.00 17.17 ? 260 ALA B C   1 
ATOM   4268 O  O   . ALA B 1 260 ? -0.184  -18.291 23.714  1.00 16.09 ? 260 ALA B O   1 
ATOM   4269 C  CB  . ALA B 1 260 ? -1.025  -15.307 24.527  1.00 16.09 ? 260 ALA B CB  1 
ATOM   4270 N  N   . SER B 1 261 ? -1.346  -17.281 22.039  1.00 15.90 ? 261 SER B N   1 
ATOM   4271 C  CA  . SER B 1 261 ? -0.634  -18.005 20.972  1.00 18.37 ? 261 SER B CA  1 
ATOM   4272 C  C   . SER B 1 261 ? 0.708   -17.324 20.642  1.00 19.26 ? 261 SER B C   1 
ATOM   4273 O  O   . SER B 1 261 ? 1.481   -17.854 19.798  1.00 20.60 ? 261 SER B O   1 
ATOM   4274 C  CB  . SER B 1 261 ? -1.517  -18.069 19.687  1.00 17.59 ? 261 SER B CB  1 
ATOM   4275 O  OG  . SER B 1 261 ? -1.598  -16.764 19.110  1.00 18.66 ? 261 SER B OG  1 
ATOM   4276 N  N   . PHE B 1 262 ? 1.001   -16.188 21.265  1.00 19.66 ? 262 PHE B N   1 
ATOM   4277 C  CA  . PHE B 1 262 ? 2.051   -15.270 20.814  1.00 20.91 ? 262 PHE B CA  1 
ATOM   4278 C  C   . PHE B 1 262 ? 2.753   -14.694 22.048  1.00 22.58 ? 262 PHE B C   1 
ATOM   4279 O  O   . PHE B 1 262 ? 2.170   -14.618 23.149  1.00 21.61 ? 262 PHE B O   1 
ATOM   4280 C  CB  . PHE B 1 262 ? 1.435   -14.189 19.956  1.00 21.38 ? 262 PHE B CB  1 
ATOM   4281 C  CG  . PHE B 1 262 ? 0.457   -13.324 20.668  1.00 17.98 ? 262 PHE B CG  1 
ATOM   4282 C  CD1 . PHE B 1 262 ? 0.882   -12.080 21.213  1.00 18.33 ? 262 PHE B CD1 1 
ATOM   4283 C  CD2 . PHE B 1 262 ? -0.873  -13.728 20.855  1.00 18.28 ? 262 PHE B CD2 1 
ATOM   4284 C  CE1 . PHE B 1 262 ? 0.002   -11.281 21.930  1.00 20.92 ? 262 PHE B CE1 1 
ATOM   4285 C  CE2 . PHE B 1 262 ? -1.739  -12.928 21.615  1.00 19.31 ? 262 PHE B CE2 1 
ATOM   4286 C  CZ  . PHE B 1 262 ? -1.316  -11.703 22.129  1.00 17.65 ? 262 PHE B CZ  1 
ATOM   4287 N  N   . HIS B 1 263 ? 4.004   -14.289 21.855  1.00 29.25 ? 263 HIS B N   1 
ATOM   4288 C  CA  . HIS B 1 263 ? 4.870   -13.715 22.891  1.00 34.76 ? 263 HIS B CA  1 
ATOM   4289 C  C   . HIS B 1 263 ? 6.063   -13.142 22.202  1.00 40.86 ? 263 HIS B C   1 
ATOM   4290 O  O   . HIS B 1 263 ? 6.884   -12.460 22.810  1.00 53.50 ? 263 HIS B O   1 
ATOM   4291 C  CB  . HIS B 1 263 ? 5.358   -14.741 23.935  1.00 37.98 ? 263 HIS B CB  1 
ATOM   4292 C  CG  . HIS B 1 263 ? 6.402   -15.723 23.428  1.00 36.61 ? 263 HIS B CG  1 
ATOM   4293 N  ND1 . HIS B 1 263 ? 6.513   -16.096 22.126  1.00 39.39 ? 263 HIS B ND1 1 
ATOM   4294 C  CD2 . HIS B 1 263 ? 7.329   -16.472 24.121  1.00 36.28 ? 263 HIS B CD2 1 
ATOM   4295 C  CE1 . HIS B 1 263 ? 7.474   -17.021 22.009  1.00 44.88 ? 263 HIS B CE1 1 
ATOM   4296 N  NE2 . HIS B 1 263 ? 7.973   -17.252 23.228  1.00 42.13 ? 263 HIS B NE2 1 
ATOM   4297 O  OXT . HIS B 1 263 ? 6.228   -13.331 20.997  1.00 50.96 ? 263 HIS B OXT 1 
HETATM 4298 ZN ZN  . ZN  C 2 .   ? 6.752   -26.504 -7.722  1.00 10.80 ? 301 ZN  A ZN  1 
HETATM 4299 C  C1  . EDO D 3 .   ? -14.743 -28.068 -13.718 1.00 29.01 ? 302 EDO A C1  1 
HETATM 4300 O  O1  . EDO D 3 .   ? -14.675 -26.996 -12.770 1.00 24.59 ? 302 EDO A O1  1 
HETATM 4301 C  C2  . EDO D 3 .   ? -13.823 -29.205 -13.408 1.00 27.36 ? 302 EDO A C2  1 
HETATM 4302 O  O2  . EDO D 3 .   ? -14.068 -29.952 -12.234 1.00 26.41 ? 302 EDO A O2  1 
HETATM 4303 C  C1  . EDO E 3 .   ? -8.340  -41.812 -8.981  1.00 26.66 ? 303 EDO A C1  1 
HETATM 4304 O  O1  . EDO E 3 .   ? -9.204  -42.094 -7.875  1.00 23.84 ? 303 EDO A O1  1 
HETATM 4305 C  C2  . EDO E 3 .   ? -8.785  -42.500 -10.254 1.00 26.68 ? 303 EDO A C2  1 
HETATM 4306 O  O2  . EDO E 3 .   ? -9.955  -41.931 -10.755 1.00 26.06 ? 303 EDO A O2  1 
HETATM 4307 O  O16 . WWX F 4 .   ? 3.671   -25.290 -13.527 1.00 36.03 ? 304 WWX A O16 1 
HETATM 4308 S  S14 . WWX F 4 .   ? 4.641   -24.194 -14.133 1.00 35.25 ? 304 WWX A S14 1 
HETATM 4309 O  O15 . WWX F 4 .   ? 3.781   -22.934 -14.450 1.00 33.83 ? 304 WWX A O15 1 
HETATM 4310 C  C18 . WWX F 4 .   ? 6.887   -24.436 -15.782 1.00 30.23 ? 304 WWX A C18 1 
HETATM 4311 O  O20 . WWX F 4 .   ? 6.774   -23.044 -15.791 1.00 47.87 ? 304 WWX A O20 1 
HETATM 4312 C  C17 . WWX F 4 .   ? 5.415   -24.877 -15.626 1.00 35.69 ? 304 WWX A C17 1 
HETATM 4313 C  C8  . WWX F 4 .   ? 5.570   -23.858 -12.601 1.00 19.11 ? 304 WWX A C8  1 
HETATM 4314 C  C7  . WWX F 4 .   ? 6.089   -25.068 -12.071 1.00 21.80 ? 304 WWX A C7  1 
HETATM 4315 F  F12 . WWX F 4 .   ? 5.953   -26.375 -12.782 1.00 22.72 ? 304 WWX A F12 1 
HETATM 4316 C  C6  . WWX F 4 .   ? 6.862   -24.959 -10.833 1.00 15.59 ? 304 WWX A C6  1 
HETATM 4317 F  F11 . WWX F 4 .   ? 7.305   -26.155 -10.424 1.00 26.47 ? 304 WWX A F11 1 
HETATM 4318 C  C9  . WWX F 4 .   ? 5.717   -22.527 -11.991 1.00 23.67 ? 304 WWX A C9  1 
HETATM 4319 C  C10 . WWX F 4 .   ? 6.428   -22.600 -10.786 1.00 25.11 ? 304 WWX A C10 1 
HETATM 4320 F  F13 . WWX F 4 .   ? 6.614   -21.482 -10.003 1.00 20.20 ? 304 WWX A F13 1 
HETATM 4321 C  C5  . WWX F 4 .   ? 7.010   -23.737 -10.134 1.00 19.13 ? 304 WWX A C5  1 
HETATM 4322 S  S1  . WWX F 4 .   ? 7.874   -23.733 -8.415  1.00 19.28 ? 304 WWX A S1  1 
HETATM 4323 O  O3  . WWX F 4 .   ? 9.155   -22.980 -8.119  1.00 22.58 ? 304 WWX A O3  1 
HETATM 4324 N  N4  . WWX F 4 .   ? 8.201   -25.373 -8.169  1.00 15.38 ? 304 WWX A N4  1 
HETATM 4325 O  O2  . WWX F 4 .   ? 6.974   -23.361 -7.289  1.00 18.75 ? 304 WWX A O2  1 
HETATM 4326 N  N19 . WWX F 4 .   ? 5.076   -21.236 -12.614 1.00 19.46 ? 304 WWX A N19 1 
HETATM 4327 C  C21 . WWX F 4 .   ? 5.413   -20.042 -13.412 1.00 37.11 ? 304 WWX A C21 1 
HETATM 4328 C  C30 . WWX F 4 .   ? 5.127   -20.044 -14.916 1.00 40.22 ? 304 WWX A C30 1 
HETATM 4329 C  C35 . WWX F 4 .   ? 3.823   -20.296 -15.439 1.00 60.75 ? 304 WWX A C35 1 
HETATM 4330 C  C34 . WWX F 4 .   ? 3.577   -20.328 -16.847 1.00 63.78 ? 304 WWX A C34 1 
HETATM 4331 C  C33 . WWX F 4 .   ? 4.628   -20.122 -17.778 1.00 60.40 ? 304 WWX A C33 1 
HETATM 4332 C  C32 . WWX F 4 .   ? 5.937   -19.876 -17.319 1.00 51.06 ? 304 WWX A C32 1 
HETATM 4333 C  C31 . WWX F 4 .   ? 6.156   -19.855 -15.918 1.00 53.80 ? 304 WWX A C31 1 
HETATM 4334 C  C22 . WWX F 4 .   ? 6.869   -19.802 -13.404 1.00 33.22 ? 304 WWX A C22 1 
HETATM 4335 O  O29 . WWX F 4 .   ? 7.511   -20.851 -14.073 1.00 43.68 ? 304 WWX A O29 1 
HETATM 4336 C  C23 . WWX F 4 .   ? 7.256   -18.398 -13.852 1.00 31.21 ? 304 WWX A C23 1 
HETATM 4337 C  C28 . WWX F 4 .   ? 8.632   -18.143 -14.065 1.00 27.76 ? 304 WWX A C28 1 
HETATM 4338 C  C27 . WWX F 4 .   ? 9.101   -16.858 -14.357 1.00 29.61 ? 304 WWX A C27 1 
HETATM 4339 C  C26 . WWX F 4 .   ? 8.239   -15.814 -14.521 1.00 28.11 ? 304 WWX A C26 1 
HETATM 4340 C  C25 . WWX F 4 .   ? 6.867   -16.062 -14.371 1.00 29.84 ? 304 WWX A C25 1 
HETATM 4341 C  C24 . WWX F 4 .   ? 6.332   -17.315 -14.025 1.00 29.97 ? 304 WWX A C24 1 
HETATM 4342 ZN ZN  . ZN  G 2 .   ? -21.821 -13.422 20.754  1.00 11.08 ? 301 ZN  B ZN  1 
HETATM 4343 C  C1  . EDO H 3 .   ? -23.996 8.128   12.794  1.00 43.13 ? 302 EDO B C1  1 
HETATM 4344 O  O1  . EDO H 3 .   ? -22.651 7.757   13.044  1.00 41.24 ? 302 EDO B O1  1 
HETATM 4345 C  C2  . EDO H 3 .   ? -24.433 7.962   11.368  1.00 41.03 ? 302 EDO B C2  1 
HETATM 4346 O  O2  . EDO H 3 .   ? -25.614 7.231   11.231  1.00 40.83 ? 302 EDO B O2  1 
HETATM 4347 O  O16 . WWX I 4 .   ? -27.603 -14.965 17.533  1.00 26.43 ? 303 WWX B O16 1 
HETATM 4348 S  S14 . WWX I 4 .   ? -28.195 -15.838 18.706  1.00 27.05 ? 303 WWX B S14 1 
HETATM 4349 O  O15 . WWX I 4 .   ? -28.594 -17.214 18.077  1.00 24.43 ? 303 WWX B O15 1 
HETATM 4350 C  C18 . WWX I 4 .   ? -30.209 -16.144 20.296  1.00 31.83 ? 303 WWX B C18 1 
HETATM 4351 O  O20 . WWX I 4 .   ? -29.337 -16.411 21.290  1.00 37.62 ? 303 WWX B O20 1 
HETATM 4352 C  C17 . WWX I 4 .   ? -29.578 -15.090 19.416  1.00 25.37 ? 303 WWX B C17 1 
HETATM 4353 C  C8  . WWX I 4 .   ? -26.775 -16.059 19.679  1.00 16.70 ? 303 WWX B C8  1 
HETATM 4354 C  C7  . WWX I 4 .   ? -26.162 -14.906 20.208  1.00 15.16 ? 303 WWX B C7  1 
HETATM 4355 F  F12 . WWX I 4 .   ? -26.801 -13.660 20.060  1.00 17.74 ? 303 WWX B F12 1 
HETATM 4356 C  C6  . WWX I 4 .   ? -25.026 -14.926 20.899  1.00 13.84 ? 303 WWX B C6  1 
HETATM 4357 F  F11 . WWX I 4 .   ? -24.696 -13.721 21.402  1.00 15.73 ? 303 WWX B F11 1 
HETATM 4358 C  C9  . WWX I 4 .   ? -26.117 -17.296 19.859  1.00 16.51 ? 303 WWX B C9  1 
HETATM 4359 C  C10 . WWX I 4 .   ? -24.969 -17.258 20.576  1.00 15.76 ? 303 WWX B C10 1 
HETATM 4360 F  F13 . WWX I 4 .   ? -24.155 -18.397 20.751  1.00 15.66 ? 303 WWX B F13 1 
HETATM 4361 C  C5  . WWX I 4 .   ? -24.322 -16.103 21.125  1.00 13.40 ? 303 WWX B C5  1 
HETATM 4362 S  S1  . WWX I 4 .   ? -22.710 -16.194 21.890  1.00 15.46 ? 303 WWX B S1  1 
HETATM 4363 O  O3  . WWX I 4 .   ? -22.825 -16.909 23.222  1.00 15.64 ? 303 WWX B O3  1 
HETATM 4364 N  N4  . WWX I 4 .   ? -22.167 -14.628 22.215  1.00 13.08 ? 303 WWX B N4  1 
HETATM 4365 O  O2  . WWX I 4 .   ? -21.761 -16.805 20.860  1.00 14.07 ? 303 WWX B O2  1 
HETATM 4366 N  N19 . WWX I 4 .   ? -26.681 -18.520 19.288  1.00 19.82 ? 303 WWX B N19 1 
HETATM 4367 C  C21 . WWX I 4 .   ? -26.590 -19.752 20.080  1.00 18.44 ? 303 WWX B C21 1 
HETATM 4368 C  C30 . WWX I 4 .   ? -25.837 -20.794 19.305  1.00 18.32 ? 303 WWX B C30 1 
HETATM 4369 C  C35 . WWX I 4 .   ? -25.090 -21.886 19.933  1.00 17.41 ? 303 WWX B C35 1 
HETATM 4370 C  C34 . WWX I 4 .   ? -24.479 -22.906 19.168  1.00 16.56 ? 303 WWX B C34 1 
HETATM 4371 C  C33 . WWX I 4 .   ? -24.456 -22.813 17.837  1.00 19.11 ? 303 WWX B C33 1 
HETATM 4372 C  C32 . WWX I 4 .   ? -25.072 -21.717 17.210  1.00 19.91 ? 303 WWX B C32 1 
HETATM 4373 C  C31 . WWX I 4 .   ? -25.764 -20.710 17.924  1.00 20.64 ? 303 WWX B C31 1 
HETATM 4374 C  C22 . WWX I 4 .   ? -28.048 -20.203 20.319  1.00 17.11 ? 303 WWX B C22 1 
HETATM 4375 O  O29 . WWX I 4 .   ? -28.689 -20.236 19.081  1.00 18.18 ? 303 WWX B O29 1 
HETATM 4376 C  C23 . WWX I 4 .   ? -28.156 -21.500 21.049  1.00 17.55 ? 303 WWX B C23 1 
HETATM 4377 C  C28 . WWX I 4 .   ? -28.153 -22.674 20.279  1.00 18.17 ? 303 WWX B C28 1 
HETATM 4378 C  C27 . WWX I 4 .   ? -28.240 -23.907 20.983  1.00 19.62 ? 303 WWX B C27 1 
HETATM 4379 C  C26 . WWX I 4 .   ? -28.259 -23.952 22.380  1.00 18.50 ? 303 WWX B C26 1 
HETATM 4380 C  C25 . WWX I 4 .   ? -28.218 -22.782 23.098  1.00 19.16 ? 303 WWX B C25 1 
HETATM 4381 C  C24 . WWX I 4 .   ? -28.175 -21.536 22.465  1.00 16.47 ? 303 WWX B C24 1 
HETATM 4382 O  O   . HOH J 5 .   ? 3.000   -30.687 4.276   1.00 14.18 ? 401 HOH A O   1 
HETATM 4383 O  O   . HOH J 5 .   ? 22.459  -25.616 -7.076  1.00 18.29 ? 402 HOH A O   1 
HETATM 4384 O  O   . HOH J 5 .   ? 5.285   -40.348 1.996   1.00 18.12 ? 403 HOH A O   1 
HETATM 4385 O  O   . HOH J 5 .   ? 19.766  -29.212 0.826   1.00 16.87 ? 404 HOH A O   1 
HETATM 4386 O  O   . HOH J 5 .   ? 1.941   -28.481 9.407   1.00 15.43 ? 405 HOH A O   1 
HETATM 4387 O  O   . HOH J 5 .   ? 14.322  -14.270 -0.990  1.00 17.18 ? 406 HOH A O   1 
HETATM 4388 O  O   . HOH J 5 .   ? 15.881  -16.029 -2.378  1.00 19.68 ? 407 HOH A O   1 
HETATM 4389 O  O   . HOH J 5 .   ? -8.729  -22.058 -24.451 1.00 18.27 ? 408 HOH A O   1 
HETATM 4390 O  O   . HOH J 5 .   ? 12.290  -17.362 5.625   1.00 13.31 ? 409 HOH A O   1 
HETATM 4391 O  O   . HOH J 5 .   ? 7.571   -29.080 -12.763 1.00 17.47 ? 410 HOH A O   1 
HETATM 4392 O  O   . HOH J 5 .   ? 27.495  -21.768 -22.834 1.00 14.81 ? 411 HOH A O   1 
HETATM 4393 O  O   . HOH J 5 .   ? 26.070  -22.186 -13.310 1.00 22.42 ? 412 HOH A O   1 
HETATM 4394 O  O   . HOH J 5 .   ? 5.867   -40.216 -6.465  1.00 9.88  ? 413 HOH A O   1 
HETATM 4395 O  O   . HOH J 5 .   ? 9.938   -13.605 -1.445  1.00 14.02 ? 414 HOH A O   1 
HETATM 4396 O  O   . HOH J 5 .   ? 7.768   -10.668 2.538   1.00 15.77 ? 415 HOH A O   1 
HETATM 4397 O  O   . HOH J 5 .   ? 16.751  -39.012 -1.229  1.00 23.06 ? 416 HOH A O   1 
HETATM 4398 O  O   . HOH J 5 .   ? -11.252 -43.136 2.506   1.00 32.29 ? 417 HOH A O   1 
HETATM 4399 O  O   . HOH J 5 .   ? -7.326  -13.082 -5.541  1.00 18.46 ? 418 HOH A O   1 
HETATM 4400 O  O   . HOH J 5 .   ? 3.491   -42.456 1.626   1.00 21.08 ? 419 HOH A O   1 
HETATM 4401 O  O   . HOH J 5 .   ? 11.342  -29.122 -10.458 1.00 12.99 ? 420 HOH A O   1 
HETATM 4402 O  O   . HOH J 5 .   ? 7.841   -1.569  -6.097  1.00 18.59 ? 421 HOH A O   1 
HETATM 4403 O  O   . HOH J 5 .   ? -0.213  -4.815  -7.806  1.00 15.55 ? 422 HOH A O   1 
HETATM 4404 O  O   . HOH J 5 .   ? 5.341   -45.716 -11.501 1.00 17.51 ? 423 HOH A O   1 
HETATM 4405 O  O   . HOH J 5 .   ? 1.901   -10.528 5.807   1.00 17.45 ? 424 HOH A O   1 
HETATM 4406 O  O   . HOH J 5 .   ? -7.376  -23.472 -26.664 1.00 19.30 ? 425 HOH A O   1 
HETATM 4407 O  O   . HOH J 5 .   ? 0.748   -21.049 10.763  1.00 20.80 ? 426 HOH A O   1 
HETATM 4408 O  O   . HOH J 5 .   ? 24.651  -33.899 1.857   1.00 23.06 ? 427 HOH A O   1 
HETATM 4409 O  O   . HOH J 5 .   ? 8.411   -41.641 -21.680 1.00 16.48 ? 428 HOH A O   1 
HETATM 4410 O  O   . HOH J 5 .   ? 21.964  -27.820 -13.460 1.00 15.57 ? 429 HOH A O   1 
HETATM 4411 O  O   . HOH J 5 .   ? 12.341  -37.067 -3.254  1.00 15.90 ? 430 HOH A O   1 
HETATM 4412 O  O   . HOH J 5 .   ? 0.704   -45.354 -7.768  1.00 29.70 ? 431 HOH A O   1 
HETATM 4413 O  O   . HOH J 5 .   ? -9.983  -24.418 -30.237 1.00 15.29 ? 432 HOH A O   1 
HETATM 4414 O  O   . HOH J 5 .   ? 2.709   -36.552 -27.707 1.00 22.22 ? 433 HOH A O   1 
HETATM 4415 O  O   . HOH J 5 .   ? 12.875  -15.309 3.967   1.00 19.74 ? 434 HOH A O   1 
HETATM 4416 O  O   . HOH J 5 .   ? -4.788  -18.546 -17.045 1.00 47.44 ? 435 HOH A O   1 
HETATM 4417 O  O   . HOH J 5 .   ? -13.143 -32.500 -12.294 1.00 18.85 ? 436 HOH A O   1 
HETATM 4418 O  O   . HOH J 5 .   ? 20.101  -18.243 -15.111 1.00 16.96 ? 437 HOH A O   1 
HETATM 4419 O  O   . HOH J 5 .   ? 11.485  -46.043 -11.670 1.00 15.53 ? 438 HOH A O   1 
HETATM 4420 O  O   . HOH J 5 .   ? 14.582  -18.129 7.150   1.00 17.14 ? 439 HOH A O   1 
HETATM 4421 O  O   . HOH J 5 .   ? 9.335   -12.919 3.004   1.00 21.20 ? 440 HOH A O   1 
HETATM 4422 O  O   . HOH J 5 .   ? 19.090  -23.749 9.237   1.00 29.39 ? 441 HOH A O   1 
HETATM 4423 O  O   . HOH J 5 .   ? 19.329  -28.639 -11.018 1.00 15.27 ? 442 HOH A O   1 
HETATM 4424 O  O   . HOH J 5 .   ? 21.699  -22.972 -3.441  1.00 16.45 ? 443 HOH A O   1 
HETATM 4425 O  O   . HOH J 5 .   ? 10.348  -13.223 11.114  1.00 28.46 ? 444 HOH A O   1 
HETATM 4426 O  O   . HOH J 5 .   ? -6.955  -27.125 -24.757 1.00 21.82 ? 445 HOH A O   1 
HETATM 4427 O  O   . HOH J 5 .   ? 10.656  -41.941 -7.377  1.00 18.05 ? 446 HOH A O   1 
HETATM 4428 O  O   . HOH J 5 .   ? 9.751   -37.590 -16.292 1.00 17.36 ? 447 HOH A O   1 
HETATM 4429 O  O   . HOH J 5 .   ? -2.254  -9.850  -2.186  1.00 15.77 ? 448 HOH A O   1 
HETATM 4430 O  O   . HOH J 5 .   ? 8.904   -31.814 -18.425 1.00 16.43 ? 449 HOH A O   1 
HETATM 4431 O  O   . HOH J 5 .   ? -10.746 -35.786 -18.375 1.00 22.00 ? 450 HOH A O   1 
HETATM 4432 O  O   . HOH J 5 .   ? 16.412  -16.265 6.461   1.00 22.58 ? 451 HOH A O   1 
HETATM 4433 O  O   . HOH J 5 .   ? -0.121  -10.977 -12.402 1.00 19.78 ? 452 HOH A O   1 
HETATM 4434 O  O   . HOH J 5 .   ? 11.579  -40.452 -9.703  1.00 22.06 ? 453 HOH A O   1 
HETATM 4435 O  O   . HOH J 5 .   ? 20.114  -14.844 -4.063  1.00 22.03 ? 454 HOH A O   1 
HETATM 4436 O  O   . HOH J 5 .   ? 7.325   -33.265 7.685   1.00 18.33 ? 455 HOH A O   1 
HETATM 4437 O  O   . HOH J 5 .   ? -13.266 -28.925 -17.492 1.00 23.72 ? 456 HOH A O   1 
HETATM 4438 O  O   . HOH J 5 .   ? 4.250   -11.898 8.857   1.00 21.34 ? 457 HOH A O   1 
HETATM 4439 O  O   . HOH J 5 .   ? 2.807   -7.212  6.860   1.00 28.78 ? 458 HOH A O   1 
HETATM 4440 O  O   . HOH J 5 .   ? 14.947  -39.093 0.593   1.00 24.07 ? 459 HOH A O   1 
HETATM 4441 O  O   . HOH J 5 .   ? 7.761   -30.225 -21.982 1.00 22.68 ? 460 HOH A O   1 
HETATM 4442 O  O   . HOH J 5 .   ? -1.298  -8.380  -12.659 1.00 29.56 ? 461 HOH A O   1 
HETATM 4443 O  O   . HOH J 5 .   ? 23.807  -28.200 1.897   1.00 24.72 ? 462 HOH A O   1 
HETATM 4444 O  O   . HOH J 5 .   ? -13.687 -40.741 -12.139 1.00 25.04 ? 463 HOH A O   1 
HETATM 4445 O  O   . HOH J 5 .   ? 9.130   -10.167 5.716   1.00 22.21 ? 464 HOH A O   1 
HETATM 4446 O  O   . HOH J 5 .   ? 17.664  -13.391 -3.973  1.00 21.56 ? 465 HOH A O   1 
HETATM 4447 O  O   . HOH J 5 .   ? 11.283  -13.228 4.915   1.00 19.68 ? 466 HOH A O   1 
HETATM 4448 O  O   . HOH J 5 .   ? 22.898  -16.554 -6.230  1.00 20.78 ? 467 HOH A O   1 
HETATM 4449 O  O   . HOH J 5 .   ? -9.083  -38.118 -16.225 1.00 22.05 ? 468 HOH A O   1 
HETATM 4450 O  O   . HOH J 5 .   ? 24.552  -29.620 -12.682 1.00 26.88 ? 469 HOH A O   1 
HETATM 4451 O  O   . HOH J 5 .   ? 12.791  -15.083 1.276   1.00 16.65 ? 470 HOH A O   1 
HETATM 4452 O  O   . HOH J 5 .   ? 7.935   -34.237 10.161  1.00 22.47 ? 471 HOH A O   1 
HETATM 4453 O  O   . HOH J 5 .   ? 9.779   -8.735  2.750   1.00 24.07 ? 472 HOH A O   1 
HETATM 4454 O  O   . HOH J 5 .   ? 12.308  -35.892 -11.498 1.00 17.30 ? 473 HOH A O   1 
HETATM 4455 O  O   . HOH J 5 .   ? -5.957  -14.998 -6.745  1.00 19.17 ? 474 HOH A O   1 
HETATM 4456 O  O   . HOH J 5 .   ? 12.264  -41.464 2.384   1.00 25.32 ? 475 HOH A O   1 
HETATM 4457 O  O   . HOH J 5 .   ? 17.695  -14.940 -9.638  1.00 19.54 ? 476 HOH A O   1 
HETATM 4458 O  O   . HOH J 5 .   ? 13.880  -38.890 9.498   1.00 22.82 ? 477 HOH A O   1 
HETATM 4459 O  O   . HOH J 5 .   ? -9.621  -39.436 -11.927 1.00 21.83 ? 478 HOH A O   1 
HETATM 4460 O  O   . HOH J 5 .   ? -3.539  -34.011 6.710   1.00 24.16 ? 479 HOH A O   1 
HETATM 4461 O  O   . HOH J 5 .   ? 17.577  -17.347 -14.689 1.00 21.65 ? 480 HOH A O   1 
HETATM 4462 O  O   . HOH J 5 .   ? 11.002  -46.962 -4.537  1.00 22.58 ? 481 HOH A O   1 
HETATM 4463 O  O   . HOH J 5 .   ? -9.939  -46.710 -11.717 1.00 28.21 ? 482 HOH A O   1 
HETATM 4464 O  O   . HOH J 5 .   ? -13.303 -25.935 -20.913 1.00 22.36 ? 483 HOH A O   1 
HETATM 4465 O  O   . HOH J 5 .   ? 2.677   -45.603 -11.637 1.00 22.21 ? 484 HOH A O   1 
HETATM 4466 O  O   . HOH J 5 .   ? 23.978  -23.959 -5.492  1.00 27.79 ? 485 HOH A O   1 
HETATM 4467 O  O   . HOH J 5 .   ? 5.265   -15.487 19.095  1.00 36.70 ? 486 HOH A O   1 
HETATM 4468 O  O   . HOH J 5 .   ? 13.867  -33.787 -4.694  1.00 24.27 ? 487 HOH A O   1 
HETATM 4469 O  O   . HOH J 5 .   ? 2.170   -47.236 -3.064  1.00 20.48 ? 488 HOH A O   1 
HETATM 4470 O  O   . HOH J 5 .   ? 13.953  -42.204 4.381   1.00 23.54 ? 489 HOH A O   1 
HETATM 4471 O  O   . HOH J 5 .   ? 23.267  -18.663 0.494   1.00 22.94 ? 490 HOH A O   1 
HETATM 4472 O  O   . HOH J 5 .   ? -8.530  -43.042 -5.352  1.00 23.36 ? 491 HOH A O   1 
HETATM 4473 O  O   . HOH J 5 .   ? -2.405  -5.803  -8.991  1.00 19.07 ? 492 HOH A O   1 
HETATM 4474 O  O   . HOH J 5 .   ? 16.151  -11.446 -12.191 1.00 26.11 ? 493 HOH A O   1 
HETATM 4475 O  O   . HOH J 5 .   ? 4.802   -44.034 -0.143  1.00 25.61 ? 494 HOH A O   1 
HETATM 4476 O  O   . HOH J 5 .   ? 16.665  -38.289 -22.506 1.00 37.78 ? 495 HOH A O   1 
HETATM 4477 O  O   . HOH J 5 .   ? -2.717  -24.299 -21.839 1.00 26.32 ? 496 HOH A O   1 
HETATM 4478 O  O   . HOH J 5 .   ? 11.103  -26.916 15.761  1.00 31.87 ? 497 HOH A O   1 
HETATM 4479 O  O   . HOH J 5 .   ? 18.521  -15.417 -12.520 1.00 24.96 ? 498 HOH A O   1 
HETATM 4480 O  O   . HOH J 5 .   ? -15.000 -38.256 -9.229  1.00 20.21 ? 499 HOH A O   1 
HETATM 4481 O  O   . HOH J 5 .   ? -1.193  -36.207 8.163   1.00 26.49 ? 500 HOH A O   1 
HETATM 4482 O  O   . HOH J 5 .   ? 5.095   -40.259 4.761   1.00 32.87 ? 501 HOH A O   1 
HETATM 4483 O  O   . HOH J 5 .   ? -4.752  -8.408  1.236   1.00 27.74 ? 502 HOH A O   1 
HETATM 4484 O  O   . HOH J 5 .   ? 6.071   -6.492  0.984   1.00 23.65 ? 503 HOH A O   1 
HETATM 4485 O  O   . HOH J 5 .   ? -0.649  -30.435 -27.668 1.00 21.64 ? 504 HOH A O   1 
HETATM 4486 O  O   . HOH J 5 .   ? -1.266  -14.178 10.887  1.00 20.71 ? 505 HOH A O   1 
HETATM 4487 O  O   . HOH J 5 .   ? 9.122   -6.747  1.277   1.00 26.74 ? 506 HOH A O   1 
HETATM 4488 O  O   . HOH J 5 .   ? -1.197  -5.522  2.746   1.00 33.34 ? 507 HOH A O   1 
HETATM 4489 O  O   . HOH J 5 .   ? 15.433  -12.085 -7.239  1.00 23.60 ? 508 HOH A O   1 
HETATM 4490 O  O   . HOH J 5 .   ? -8.915  -30.177 -23.102 1.00 30.08 ? 509 HOH A O   1 
HETATM 4491 O  O   . HOH J 5 .   ? 25.708  -29.634 -16.841 1.00 37.53 ? 510 HOH A O   1 
HETATM 4492 O  O   . HOH J 5 .   ? 22.444  -28.321 5.596   1.00 32.81 ? 511 HOH A O   1 
HETATM 4493 O  O   . HOH J 5 .   ? 17.807  -27.421 6.880   1.00 19.73 ? 512 HOH A O   1 
HETATM 4494 O  O   . HOH J 5 .   ? 10.436  -34.032 -19.070 1.00 18.72 ? 513 HOH A O   1 
HETATM 4495 O  O   . HOH J 5 .   ? -14.780 -34.287 -10.868 1.00 23.41 ? 514 HOH A O   1 
HETATM 4496 O  O   . HOH J 5 .   ? 12.911  -17.303 19.172  1.00 37.16 ? 515 HOH A O   1 
HETATM 4497 O  O   . HOH J 5 .   ? -13.899 -33.212 -14.810 1.00 28.06 ? 516 HOH A O   1 
HETATM 4498 O  O   . HOH J 5 .   ? 26.358  -23.992 -21.790 1.00 20.24 ? 517 HOH A O   1 
HETATM 4499 O  O   . HOH J 5 .   ? 19.731  -14.233 -7.828  1.00 26.33 ? 518 HOH A O   1 
HETATM 4500 O  O   . HOH J 5 .   ? -11.499 -15.546 -15.344 1.00 41.11 ? 519 HOH A O   1 
HETATM 4501 O  O   . HOH J 5 .   ? -1.586  -7.562  4.982   1.00 35.00 ? 520 HOH A O   1 
HETATM 4502 O  O   . HOH J 5 .   ? -13.147 -31.594 -16.983 1.00 33.17 ? 521 HOH A O   1 
HETATM 4503 O  O   . HOH J 5 .   ? 13.706  -40.237 -7.587  1.00 30.01 ? 522 HOH A O   1 
HETATM 4504 O  O   . HOH J 5 .   ? 4.955   -34.726 10.233  1.00 33.73 ? 523 HOH A O   1 
HETATM 4505 O  O   . HOH J 5 .   ? -4.224  -34.245 12.335  1.00 33.68 ? 524 HOH A O   1 
HETATM 4506 O  O   . HOH J 5 .   ? -7.780  -27.985 5.138   1.00 40.06 ? 525 HOH A O   1 
HETATM 4507 O  O   . HOH J 5 .   ? 11.703  -28.497 13.225  1.00 25.39 ? 526 HOH A O   1 
HETATM 4508 O  O   . HOH J 5 .   ? 2.455   -29.955 11.947  1.00 25.71 ? 527 HOH A O   1 
HETATM 4509 O  O   . HOH J 5 .   ? 11.037  -33.315 -21.716 1.00 25.26 ? 528 HOH A O   1 
HETATM 4510 O  O   . HOH J 5 .   ? 15.512  -14.500 4.735   1.00 22.34 ? 529 HOH A O   1 
HETATM 4511 O  O   . HOH J 5 .   ? 23.718  -21.999 -23.322 1.00 31.11 ? 530 HOH A O   1 
HETATM 4512 O  O   . HOH J 5 .   ? 19.161  -34.564 -14.291 1.00 23.58 ? 531 HOH A O   1 
HETATM 4513 O  O   . HOH J 5 .   ? 26.918  -24.535 -6.212  1.00 29.70 ? 532 HOH A O   1 
HETATM 4514 O  O   . HOH J 5 .   ? 10.721  -13.081 7.620   1.00 22.01 ? 533 HOH A O   1 
HETATM 4515 O  O   . HOH J 5 .   ? 11.407  -36.943 8.885   1.00 38.58 ? 534 HOH A O   1 
HETATM 4516 O  O   . HOH J 5 .   ? 17.042  -17.141 -17.850 1.00 31.48 ? 535 HOH A O   1 
HETATM 4517 O  O   . HOH J 5 .   ? 6.908   -10.385 9.637   1.00 48.80 ? 536 HOH A O   1 
HETATM 4518 O  O   . HOH J 5 .   ? -5.561  -46.111 -4.455  1.00 27.50 ? 537 HOH A O   1 
HETATM 4519 O  O   . HOH J 5 .   ? -3.656  -23.426 -16.191 1.00 24.79 ? 538 HOH A O   1 
HETATM 4520 O  O   . HOH J 5 .   ? 20.027  -28.563 3.537   1.00 24.91 ? 539 HOH A O   1 
HETATM 4521 O  O   . HOH J 5 .   ? 10.144  -33.354 11.897  1.00 26.76 ? 540 HOH A O   1 
HETATM 4522 O  O   . HOH J 5 .   ? 23.419  -27.328 -11.174 1.00 24.49 ? 541 HOH A O   1 
HETATM 4523 O  O   . HOH J 5 .   ? -16.385 -19.611 -10.781 1.00 26.92 ? 542 HOH A O   1 
HETATM 4524 O  O   . HOH J 5 .   ? -5.145  -45.935 2.309   1.00 31.68 ? 543 HOH A O   1 
HETATM 4525 O  O   . HOH J 5 .   ? 7.534   -41.620 1.148   1.00 27.91 ? 544 HOH A O   1 
HETATM 4526 O  O   . HOH J 5 .   ? -7.666  -13.055 7.347   1.00 37.37 ? 545 HOH A O   1 
HETATM 4527 O  O   . HOH J 5 .   ? 13.603  -44.419 -1.443  1.00 59.43 ? 546 HOH A O   1 
HETATM 4528 O  O   . HOH J 5 .   ? 22.056  -28.692 -9.337  1.00 29.84 ? 547 HOH A O   1 
HETATM 4529 O  O   . HOH J 5 .   ? -5.823  -33.667 4.936   1.00 39.49 ? 548 HOH A O   1 
HETATM 4530 O  O   . HOH J 5 .   ? -4.700  -14.033 4.137   1.00 35.85 ? 549 HOH A O   1 
HETATM 4531 O  O   . HOH J 5 .   ? -14.237 -34.254 -6.227  1.00 39.01 ? 550 HOH A O   1 
HETATM 4532 O  O   . HOH J 5 .   ? 16.693  -13.449 0.146   1.00 33.93 ? 551 HOH A O   1 
HETATM 4533 O  O   . HOH J 5 .   ? 27.982  -25.348 -1.075  1.00 41.89 ? 552 HOH A O   1 
HETATM 4534 O  O   . HOH J 5 .   ? 9.001   -22.046 -16.219 1.00 36.42 ? 553 HOH A O   1 
HETATM 4535 O  O   . HOH J 5 .   ? 11.998  -10.718 1.603   1.00 40.37 ? 554 HOH A O   1 
HETATM 4536 O  O   . HOH J 5 .   ? -7.274  -31.328 5.820   1.00 28.80 ? 555 HOH A O   1 
HETATM 4537 O  O   . HOH J 5 .   ? -12.777 -19.966 0.967   1.00 38.70 ? 556 HOH A O   1 
HETATM 4538 O  O   . HOH J 5 .   ? 15.630  -12.860 -9.660  1.00 25.53 ? 557 HOH A O   1 
HETATM 4539 O  O   . HOH J 5 .   ? 3.293   -23.179 14.235  1.00 25.38 ? 558 HOH A O   1 
HETATM 4540 O  O   . HOH J 5 .   ? 18.324  -28.507 -19.975 1.00 35.29 ? 559 HOH A O   1 
HETATM 4541 O  O   . HOH J 5 .   ? 10.446  -30.728 -21.944 1.00 32.31 ? 560 HOH A O   1 
HETATM 4542 O  O   . HOH J 5 .   ? 22.856  -36.993 -19.414 1.00 41.84 ? 561 HOH A O   1 
HETATM 4543 O  O   . HOH J 5 .   ? 24.679  -27.779 -23.612 1.00 27.72 ? 562 HOH A O   1 
HETATM 4544 O  O   . HOH J 5 .   ? 8.581   -42.381 -24.394 1.00 25.01 ? 563 HOH A O   1 
HETATM 4545 O  O   . HOH J 5 .   ? 2.869   -38.572 8.422   1.00 34.03 ? 564 HOH A O   1 
HETATM 4546 O  O   . HOH J 5 .   ? -2.982  -4.140  0.278   1.00 39.21 ? 565 HOH A O   1 
HETATM 4547 O  O   . HOH J 5 .   ? 24.750  -35.882 14.122  1.00 31.81 ? 566 HOH A O   1 
HETATM 4548 O  O   . HOH J 5 .   ? -12.580 -14.583 -9.551  1.00 38.73 ? 567 HOH A O   1 
HETATM 4549 O  O   . HOH J 5 .   ? -1.302  -42.405 5.433   1.00 34.48 ? 568 HOH A O   1 
HETATM 4550 O  O   . HOH J 5 .   ? 21.472  -15.169 -12.775 1.00 28.37 ? 569 HOH A O   1 
HETATM 4551 O  O   . HOH J 5 .   ? -13.216 -18.097 -12.782 1.00 43.05 ? 570 HOH A O   1 
HETATM 4552 O  O   . HOH J 5 .   ? -3.862  -10.796 -14.056 1.00 41.41 ? 571 HOH A O   1 
HETATM 4553 O  O   . HOH J 5 .   ? 21.272  -31.425 0.291   1.00 28.72 ? 572 HOH A O   1 
HETATM 4554 O  O   . HOH J 5 .   ? -7.789  -46.117 3.774   1.00 25.27 ? 573 HOH A O   1 
HETATM 4555 O  O   . HOH J 5 .   ? 21.743  -13.625 -9.890  1.00 39.93 ? 574 HOH A O   1 
HETATM 4556 O  O   . HOH J 5 .   ? 2.249   -20.727 13.290  1.00 29.30 ? 575 HOH A O   1 
HETATM 4557 O  O   . HOH J 5 .   ? 2.839   -34.271 10.876  1.00 30.67 ? 576 HOH A O   1 
HETATM 4558 O  O   . HOH J 5 .   ? 26.355  -22.680 -15.950 1.00 17.26 ? 577 HOH A O   1 
HETATM 4559 O  O   . HOH J 5 .   ? 12.950  -43.024 6.990   1.00 22.67 ? 578 HOH A O   1 
HETATM 4560 O  O   . HOH J 5 .   ? 14.782  -36.163 -4.222  1.00 20.49 ? 579 HOH A O   1 
HETATM 4561 O  O   . HOH J 5 .   ? 26.754  -17.289 -16.539 1.00 18.41 ? 580 HOH A O   1 
HETATM 4562 O  O   . HOH J 5 .   ? -9.167  -25.320 -27.686 1.00 21.48 ? 581 HOH A O   1 
HETATM 4563 O  O   . HOH J 5 .   ? -4.458  -44.532 -11.774 1.00 23.90 ? 582 HOH A O   1 
HETATM 4564 O  O   . HOH J 5 .   ? 25.878  -16.141 -14.348 1.00 25.93 ? 583 HOH A O   1 
HETATM 4565 O  O   . HOH J 5 .   ? 10.220  -31.161 13.458  1.00 28.57 ? 584 HOH A O   1 
HETATM 4566 O  O   . HOH J 5 .   ? 10.716  -27.237 -21.889 1.00 27.88 ? 585 HOH A O   1 
HETATM 4567 O  O   . HOH J 5 .   ? -15.049 -28.505 -5.472  1.00 36.99 ? 586 HOH A O   1 
HETATM 4568 O  O   . HOH J 5 .   ? 28.477  -23.895 -16.799 1.00 29.56 ? 587 HOH A O   1 
HETATM 4569 O  O   . HOH J 5 .   ? -12.410 -27.545 -22.836 1.00 35.26 ? 588 HOH A O   1 
HETATM 4570 O  O   . HOH J 5 .   ? 2.236   -26.943 -14.978 1.00 29.82 ? 589 HOH A O   1 
HETATM 4571 O  O   . HOH J 5 .   ? 23.958  -16.758 -12.572 1.00 25.53 ? 590 HOH A O   1 
HETATM 4572 O  O   . HOH J 5 .   ? 1.508   -18.661 -13.894 1.00 43.16 ? 591 HOH A O   1 
HETATM 4573 O  O   . HOH J 5 .   ? -11.353 -43.188 -12.780 1.00 35.93 ? 592 HOH A O   1 
HETATM 4574 O  O   . HOH J 5 .   ? -9.690  -26.023 -23.980 1.00 30.54 ? 593 HOH A O   1 
HETATM 4575 O  O   . HOH J 5 .   ? -8.876  -11.984 -8.360  1.00 32.05 ? 594 HOH A O   1 
HETATM 4576 O  O   . HOH J 5 .   ? 2.728   -4.080  2.138   1.00 34.25 ? 595 HOH A O   1 
HETATM 4577 O  O   . HOH J 5 .   ? 20.681  -30.881 -9.340  1.00 30.50 ? 596 HOH A O   1 
HETATM 4578 O  O   . HOH J 5 .   ? 25.498  -19.242 -10.485 1.00 34.74 ? 597 HOH A O   1 
HETATM 4579 O  O   . HOH J 5 .   ? 12.090  -35.120 11.328  1.00 34.79 ? 598 HOH A O   1 
HETATM 4580 O  O   . HOH J 5 .   ? 6.357   -18.134 15.973  1.00 32.14 ? 599 HOH A O   1 
HETATM 4581 O  O   . HOH J 5 .   ? 5.220   -36.902 8.407   1.00 30.99 ? 600 HOH A O   1 
HETATM 4582 O  O   . HOH J 5 .   ? -6.550  -35.128 -24.003 1.00 35.08 ? 601 HOH A O   1 
HETATM 4583 O  O   . HOH J 5 .   ? -9.844  -8.527  4.411   1.00 35.11 ? 602 HOH A O   1 
HETATM 4584 O  O   . HOH J 5 .   ? -11.929 -29.889 -22.156 1.00 32.77 ? 603 HOH A O   1 
HETATM 4585 O  O   . HOH J 5 .   ? 5.920   -23.884 -18.682 1.00 37.22 ? 604 HOH A O   1 
HETATM 4586 O  O   . HOH J 5 .   ? -17.240 -18.055 -4.129  1.00 40.53 ? 605 HOH A O   1 
HETATM 4587 O  O   . HOH J 5 .   ? 8.994   -23.059 -19.195 1.00 38.70 ? 606 HOH A O   1 
HETATM 4588 O  O   . HOH J 5 .   ? 3.907   -41.706 -29.937 1.00 38.73 ? 607 HOH A O   1 
HETATM 4589 O  O   . HOH J 5 .   ? 0.699   -21.110 -14.093 1.00 34.39 ? 608 HOH A O   1 
HETATM 4590 O  O   . HOH J 5 .   ? 0.362   -24.534 -18.503 1.00 29.63 ? 609 HOH A O   1 
HETATM 4591 O  O   . HOH J 5 .   ? 12.257  -38.658 -16.184 1.00 28.20 ? 610 HOH A O   1 
HETATM 4592 O  O   . HOH J 5 .   ? 27.439  -27.423 -10.835 1.00 37.20 ? 611 HOH A O   1 
HETATM 4593 O  O   . HOH J 5 .   ? -2.359  -11.755 -16.258 1.00 52.92 ? 612 HOH A O   1 
HETATM 4594 O  O   . HOH J 5 .   ? -11.758 -39.122 -16.242 1.00 41.31 ? 613 HOH A O   1 
HETATM 4595 O  O   . HOH J 5 .   ? -1.138  -43.501 -21.521 1.00 35.41 ? 614 HOH A O   1 
HETATM 4596 O  O   . HOH J 5 .   ? 20.319  -33.970 0.960   1.00 31.71 ? 615 HOH A O   1 
HETATM 4597 O  O   . HOH J 5 .   ? 2.268   -11.528 -14.863 1.00 29.76 ? 616 HOH A O   1 
HETATM 4598 O  O   . HOH J 5 .   ? 5.029   -4.091  1.551   1.00 26.56 ? 617 HOH A O   1 
HETATM 4599 O  O   . HOH J 5 .   ? 0.467   -1.023  -1.992  1.00 38.47 ? 618 HOH A O   1 
HETATM 4600 O  O   . HOH J 5 .   ? -4.880  -35.238 8.587   1.00 34.02 ? 619 HOH A O   1 
HETATM 4601 O  O   . HOH J 5 .   ? 15.241  -41.855 0.983   1.00 42.86 ? 620 HOH A O   1 
HETATM 4602 O  O   . HOH J 5 .   ? 14.966  -35.788 -9.329  1.00 28.86 ? 621 HOH A O   1 
HETATM 4603 O  O   . HOH J 5 .   ? 25.002  -26.351 -7.528  1.00 33.41 ? 622 HOH A O   1 
HETATM 4604 O  O   . HOH J 5 .   ? 3.120   -4.475  6.048   1.00 42.19 ? 623 HOH A O   1 
HETATM 4605 O  O   . HOH J 5 .   ? 15.449  -40.045 -20.416 1.00 35.87 ? 624 HOH A O   1 
HETATM 4606 O  O   . HOH J 5 .   ? -6.853  -16.087 -20.366 1.00 30.40 ? 625 HOH A O   1 
HETATM 4607 O  O   . HOH J 5 .   ? -16.270 -14.955 -2.823  1.00 40.05 ? 626 HOH A O   1 
HETATM 4608 O  O   . HOH J 5 .   ? 15.232  -23.539 17.573  1.00 41.08 ? 627 HOH A O   1 
HETATM 4609 O  O   . HOH J 5 .   ? 14.660  -36.096 -13.364 1.00 33.38 ? 628 HOH A O   1 
HETATM 4610 O  O   . HOH J 5 .   ? 3.506   -5.395  -15.723 1.00 48.99 ? 629 HOH A O   1 
HETATM 4611 O  O   . HOH J 5 .   ? 15.851  -36.548 -6.568  1.00 30.52 ? 630 HOH A O   1 
HETATM 4612 O  O   . HOH J 5 .   ? 22.723  -34.879 0.073   1.00 30.05 ? 631 HOH A O   1 
HETATM 4613 O  O   . HOH J 5 .   ? 16.713  -35.564 -11.346 1.00 34.35 ? 632 HOH A O   1 
HETATM 4614 O  O   . HOH J 5 .   ? 0.046   -8.874  6.931   1.00 37.52 ? 633 HOH A O   1 
HETATM 4615 O  O   . HOH J 5 .   ? 24.835  -27.369 4.350   1.00 31.46 ? 634 HOH A O   1 
HETATM 4616 O  O   . HOH J 5 .   ? 22.838  -30.753 -1.882  1.00 34.84 ? 635 HOH A O   1 
HETATM 4617 O  O   . HOH J 5 .   ? -0.078  -32.369 14.142  1.00 42.89 ? 636 HOH A O   1 
HETATM 4618 O  O   . HOH J 5 .   ? 2.217   -32.442 12.522  1.00 36.60 ? 637 HOH A O   1 
HETATM 4619 O  O   . HOH J 5 .   ? 0.913   -36.685 9.814   1.00 39.80 ? 638 HOH A O   1 
HETATM 4620 O  O   . HOH J 5 .   ? 6.260   -3.884  -15.819 1.00 38.70 ? 639 HOH A O   1 
HETATM 4621 O  O   . HOH J 5 .   ? 10.569  -6.484  -11.202 1.00 33.04 ? 640 HOH A O   1 
HETATM 4622 O  O   . HOH J 5 .   ? -5.434  -24.821 -25.704 1.00 31.47 ? 641 HOH A O   1 
HETATM 4623 O  O   . HOH J 5 .   ? -1.325  -21.759 -17.843 1.00 42.13 ? 642 HOH A O   1 
HETATM 4624 O  O   . HOH J 5 .   ? 17.144  -13.639 2.551   1.00 29.22 ? 643 HOH A O   1 
HETATM 4625 O  O   . HOH J 5 .   ? 0.203   -48.459 -1.894  1.00 33.44 ? 644 HOH A O   1 
HETATM 4626 O  O   . HOH J 5 .   ? 9.328   -36.569 -18.637 1.00 23.19 ? 645 HOH A O   1 
HETATM 4627 O  O   . HOH K 5 .   ? -26.202 -32.740 -1.374  1.00 39.51 ? 401 HOH B O   1 
HETATM 4628 O  O   . HOH K 5 .   ? -9.859  -8.998  17.069  1.00 13.76 ? 402 HOH B O   1 
HETATM 4629 O  O   . HOH K 5 .   ? -4.831  -11.206 15.866  1.00 15.00 ? 403 HOH B O   1 
HETATM 4630 O  O   . HOH K 5 .   ? -6.928  -21.509 28.530  1.00 14.45 ? 404 HOH B O   1 
HETATM 4631 O  O   . HOH K 5 .   ? -20.785 0.402   20.127  1.00 12.32 ? 405 HOH B O   1 
HETATM 4632 O  O   . HOH K 5 .   ? -15.447 -26.212 23.790  1.00 13.40 ? 406 HOH B O   1 
HETATM 4633 O  O   . HOH K 5 .   ? -8.327  -22.350 26.222  1.00 13.14 ? 407 HOH B O   1 
HETATM 4634 O  O   . HOH K 5 .   ? -21.739 -34.950 13.699  1.00 13.42 ? 408 HOH B O   1 
HETATM 4635 O  O   . HOH K 5 .   ? -27.120 -17.942 40.274  1.00 18.84 ? 409 HOH B O   1 
HETATM 4636 O  O   . HOH K 5 .   ? -26.215 -7.308  0.866   1.00 22.81 ? 410 HOH B O   1 
HETATM 4637 O  O   . HOH K 5 .   ? -17.675 -2.871  26.367  1.00 17.04 ? 411 HOH B O   1 
HETATM 4638 O  O   . HOH K 5 .   ? -9.347  -5.698  8.309   1.00 33.44 ? 412 HOH B O   1 
HETATM 4639 O  O   . HOH K 5 .   ? -14.837 -25.598 28.144  1.00 16.16 ? 413 HOH B O   1 
HETATM 4640 O  O   . HOH K 5 .   ? -38.080 -17.704 5.277   1.00 22.39 ? 414 HOH B O   1 
HETATM 4641 O  O   . HOH K 5 .   ? -32.610 -8.316  22.933  1.00 17.72 ? 415 HOH B O   1 
HETATM 4642 O  O   . HOH K 5 .   ? -17.365 -16.940 35.749  1.00 13.86 ? 416 HOH B O   1 
HETATM 4643 O  O   . HOH K 5 .   ? -10.934 -26.809 23.366  1.00 17.91 ? 417 HOH B O   1 
HETATM 4644 O  O   . HOH K 5 .   ? -19.609 -26.713 6.603   1.00 19.58 ? 418 HOH B O   1 
HETATM 4645 O  O   . HOH K 5 .   ? -31.714 -24.666 4.920   1.00 23.49 ? 419 HOH B O   1 
HETATM 4646 O  O   . HOH K 5 .   ? -11.209 -30.890 23.832  1.00 20.29 ? 420 HOH B O   1 
HETATM 4647 O  O   . HOH K 5 .   ? -16.358 -23.913 29.724  1.00 17.82 ? 421 HOH B O   1 
HETATM 4648 O  O   . HOH K 5 .   ? -18.417 -6.327  28.426  1.00 21.72 ? 422 HOH B O   1 
HETATM 4649 O  O   . HOH K 5 .   ? -11.462 -29.113 21.783  1.00 13.89 ? 423 HOH B O   1 
HETATM 4650 O  O   . HOH K 5 .   ? -30.425 -2.526  23.908  1.00 17.84 ? 424 HOH B O   1 
HETATM 4651 O  O   . HOH K 5 .   ? -26.021 5.964   25.616  1.00 17.66 ? 425 HOH B O   1 
HETATM 4652 O  O   . HOH K 5 .   ? -30.548 -25.635 1.068   1.00 23.92 ? 426 HOH B O   1 
HETATM 4653 O  O   . HOH K 5 .   ? -16.121 -29.963 11.653  1.00 15.68 ? 427 HOH B O   1 
HETATM 4654 O  O   . HOH K 5 .   ? -12.648 -24.620 26.648  1.00 13.60 ? 428 HOH B O   1 
HETATM 4655 O  O   . HOH K 5 .   ? -5.319  -2.745  25.182  1.00 38.39 ? 429 HOH B O   1 
HETATM 4656 O  O   . HOH K 5 .   ? -26.635 -12.819 -0.568  1.00 29.10 ? 430 HOH B O   1 
HETATM 4657 O  O   . HOH K 5 .   ? -8.227  -29.146 15.811  1.00 14.47 ? 431 HOH B O   1 
HETATM 4658 O  O   . HOH K 5 .   ? -17.895 -26.531 31.701  1.00 25.71 ? 432 HOH B O   1 
HETATM 4659 O  O   . HOH K 5 .   ? -7.093  -32.527 16.955  1.00 27.81 ? 433 HOH B O   1 
HETATM 4660 O  O   . HOH K 5 .   ? -27.479 -12.249 36.056  1.00 17.66 ? 434 HOH B O   1 
HETATM 4661 O  O   . HOH K 5 .   ? -3.190  -18.591 14.615  1.00 17.27 ? 435 HOH B O   1 
HETATM 4662 O  O   . HOH K 5 .   ? -23.622 -25.029 31.559  1.00 20.04 ? 436 HOH B O   1 
HETATM 4663 O  O   . HOH K 5 .   ? -25.122 -11.177 33.417  1.00 17.46 ? 437 HOH B O   1 
HETATM 4664 O  O   . HOH K 5 .   ? -13.328 -10.447 33.788  1.00 18.72 ? 438 HOH B O   1 
HETATM 4665 O  O   . HOH K 5 .   ? -12.999 -33.272 20.117  1.00 21.46 ? 439 HOH B O   1 
HETATM 4666 O  O   . HOH K 5 .   ? -21.031 -14.442 36.540  1.00 17.94 ? 440 HOH B O   1 
HETATM 4667 O  O   . HOH K 5 .   ? -28.519 -22.693 31.671  1.00 19.53 ? 441 HOH B O   1 
HETATM 4668 O  O   . HOH K 5 .   ? -25.842 -4.064  26.470  1.00 19.41 ? 442 HOH B O   1 
HETATM 4669 O  O   . HOH K 5 .   ? -24.657 -10.869 25.392  1.00 12.92 ? 443 HOH B O   1 
HETATM 4670 O  O   . HOH K 5 .   ? -20.192 -23.493 36.811  1.00 19.61 ? 444 HOH B O   1 
HETATM 4671 O  O   . HOH K 5 .   ? -21.762 -25.672 33.768  1.00 22.63 ? 445 HOH B O   1 
HETATM 4672 O  O   . HOH K 5 .   ? -6.488  -6.364  21.308  1.00 16.77 ? 446 HOH B O   1 
HETATM 4673 O  O   . HOH K 5 .   ? -30.028 -18.256 23.083  1.00 29.52 ? 447 HOH B O   1 
HETATM 4674 O  O   . HOH K 5 .   ? -20.689 -24.915 8.037   1.00 19.54 ? 448 HOH B O   1 
HETATM 4675 O  O   . HOH K 5 .   ? -26.396 -28.898 13.696  1.00 18.58 ? 449 HOH B O   1 
HETATM 4676 O  O   . HOH K 5 .   ? -8.252  -29.523 23.083  1.00 19.88 ? 450 HOH B O   1 
HETATM 4677 O  O   . HOH K 5 .   ? -24.017 0.444   25.770  1.00 24.66 ? 451 HOH B O   1 
HETATM 4678 O  O   . HOH K 5 .   ? -5.085  -27.781 18.248  1.00 19.03 ? 452 HOH B O   1 
HETATM 4679 O  O   . HOH K 5 .   ? -2.882  -26.627 24.382  1.00 29.19 ? 453 HOH B O   1 
HETATM 4680 O  O   . HOH K 5 .   ? -12.926 -14.159 40.001  1.00 24.34 ? 454 HOH B O   1 
HETATM 4681 O  O   . HOH K 5 .   ? -19.476 -16.089 37.801  1.00 26.74 ? 455 HOH B O   1 
HETATM 4682 O  O   . HOH K 5 .   ? -22.181 -28.016 5.254   1.00 23.05 ? 456 HOH B O   1 
HETATM 4683 O  O   . HOH K 5 .   ? -4.049  -5.520  22.173  1.00 21.21 ? 457 HOH B O   1 
HETATM 4684 O  O   . HOH K 5 .   ? -6.331  -26.542 24.725  1.00 19.96 ? 458 HOH B O   1 
HETATM 4685 O  O   . HOH K 5 .   ? -28.578 -5.437  33.205  1.00 25.79 ? 459 HOH B O   1 
HETATM 4686 O  O   . HOH K 5 .   ? -33.390 -1.589  10.516  1.00 32.40 ? 460 HOH B O   1 
HETATM 4687 O  O   . HOH K 5 .   ? -21.670 2.012   24.810  1.00 22.20 ? 461 HOH B O   1 
HETATM 4688 O  O   . HOH K 5 .   ? -2.501  -6.382  32.010  1.00 28.98 ? 462 HOH B O   1 
HETATM 4689 O  O   . HOH K 5 .   ? -1.011  -11.130 25.725  1.00 27.93 ? 463 HOH B O   1 
HETATM 4690 O  O   . HOH K 5 .   ? -33.471 -6.253  24.470  1.00 21.97 ? 464 HOH B O   1 
HETATM 4691 O  O   . HOH K 5 .   ? 1.780   -21.463 20.474  1.00 26.59 ? 465 HOH B O   1 
HETATM 4692 O  O   . HOH K 5 .   ? -21.167 -27.838 29.394  1.00 27.93 ? 466 HOH B O   1 
HETATM 4693 O  O   . HOH K 5 .   ? -17.322 7.477   16.584  1.00 28.70 ? 467 HOH B O   1 
HETATM 4694 O  O   . HOH K 5 .   ? -4.814  -0.813  27.894  1.00 26.09 ? 468 HOH B O   1 
HETATM 4695 O  O   . HOH K 5 .   ? -32.934 -3.723  23.472  1.00 23.65 ? 469 HOH B O   1 
HETATM 4696 O  O   . HOH K 5 .   ? 5.016   -22.437 26.606  1.00 30.26 ? 470 HOH B O   1 
HETATM 4697 O  O   . HOH K 5 .   ? -12.584 -31.252 9.110   1.00 28.44 ? 471 HOH B O   1 
HETATM 4698 O  O   . HOH K 5 .   ? -0.641  -8.496  23.954  1.00 30.77 ? 472 HOH B O   1 
HETATM 4699 O  O   . HOH K 5 .   ? -8.147  -8.661  6.763   1.00 32.11 ? 473 HOH B O   1 
HETATM 4700 O  O   . HOH K 5 .   ? -31.109 -9.696  39.496  1.00 40.66 ? 474 HOH B O   1 
HETATM 4701 O  O   . HOH K 5 .   ? -11.026 -34.221 13.044  1.00 25.83 ? 475 HOH B O   1 
HETATM 4702 O  O   . HOH K 5 .   ? -4.749  -15.830 32.870  1.00 26.40 ? 476 HOH B O   1 
HETATM 4703 O  O   . HOH K 5 .   ? -7.551  -5.492  10.393  1.00 25.68 ? 477 HOH B O   1 
HETATM 4704 O  O   . HOH K 5 .   ? -31.134 -11.037 0.484   1.00 28.82 ? 478 HOH B O   1 
HETATM 4705 O  O   . HOH K 5 .   ? -9.197  -32.188 12.320  1.00 31.85 ? 479 HOH B O   1 
HETATM 4706 O  O   . HOH K 5 .   ? -30.257 -1.692  5.044   1.00 29.33 ? 480 HOH B O   1 
HETATM 4707 O  O   . HOH K 5 .   ? -32.457 -4.135  3.201   1.00 28.84 ? 481 HOH B O   1 
HETATM 4708 O  O   . HOH K 5 .   ? -26.184 5.683   17.003  1.00 23.40 ? 482 HOH B O   1 
HETATM 4709 O  O   . HOH K 5 .   ? -12.278 -11.534 37.576  1.00 28.29 ? 483 HOH B O   1 
HETATM 4710 O  O   . HOH K 5 .   ? -17.884 -25.103 34.128  1.00 23.28 ? 484 HOH B O   1 
HETATM 4711 O  O   . HOH K 5 .   ? -12.815 -33.125 22.891  1.00 21.84 ? 485 HOH B O   1 
HETATM 4712 O  O   . HOH K 5 .   ? -26.363 -31.484 12.603  1.00 26.02 ? 486 HOH B O   1 
HETATM 4713 O  O   . HOH K 5 .   ? -2.252  -9.710  16.396  1.00 23.06 ? 487 HOH B O   1 
HETATM 4714 O  O   . HOH K 5 .   ? -29.041 -24.396 2.263   1.00 45.52 ? 488 HOH B O   1 
HETATM 4715 O  O   . HOH K 5 .   ? -36.008 -9.889  21.736  1.00 21.47 ? 489 HOH B O   1 
HETATM 4716 O  O   . HOH K 5 .   ? -13.435 -21.341 37.361  1.00 19.30 ? 490 HOH B O   1 
HETATM 4717 O  O   . HOH K 5 .   ? -41.845 -3.814  16.928  1.00 30.57 ? 491 HOH B O   1 
HETATM 4718 O  O   . HOH K 5 .   ? -13.670 -25.133 2.164   1.00 41.14 ? 492 HOH B O   1 
HETATM 4719 O  O   . HOH K 5 .   ? -9.021  -15.130 38.771  1.00 29.34 ? 493 HOH B O   1 
HETATM 4720 O  O   . HOH K 5 .   ? -3.067  -25.330 12.678  1.00 22.45 ? 494 HOH B O   1 
HETATM 4721 O  O   . HOH K 5 .   ? -9.936  -25.616 9.115   1.00 28.98 ? 495 HOH B O   1 
HETATM 4722 O  O   . HOH K 5 .   ? -9.407  2.175   9.231   1.00 31.51 ? 496 HOH B O   1 
HETATM 4723 O  O   . HOH K 5 .   ? -38.775 -12.623 6.936   1.00 27.92 ? 497 HOH B O   1 
HETATM 4724 O  O   . HOH K 5 .   ? -22.324 4.956   15.522  1.00 29.07 ? 498 HOH B O   1 
HETATM 4725 O  O   . HOH K 5 .   ? -3.153  -19.402 11.822  1.00 22.68 ? 499 HOH B O   1 
HETATM 4726 O  O   . HOH K 5 .   ? -22.046 -36.666 27.464  1.00 33.95 ? 500 HOH B O   1 
HETATM 4727 O  O   . HOH K 5 .   ? -33.637 -3.097  36.841  1.00 41.07 ? 501 HOH B O   1 
HETATM 4728 O  O   . HOH K 5 .   ? -14.575 4.320   19.179  1.00 29.48 ? 502 HOH B O   1 
HETATM 4729 O  O   . HOH K 5 .   ? -35.505 -16.010 40.576  1.00 21.94 ? 503 HOH B O   1 
HETATM 4730 O  O   . HOH K 5 .   ? 0.086   -16.285 17.273  1.00 22.66 ? 504 HOH B O   1 
HETATM 4731 O  O   . HOH K 5 .   ? -12.880 2.628   17.828  1.00 25.02 ? 505 HOH B O   1 
HETATM 4732 O  O   . HOH K 5 .   ? -28.039 -21.254 14.537  1.00 32.15 ? 506 HOH B O   1 
HETATM 4733 O  O   . HOH K 5 .   ? -2.126  -5.157  9.745   1.00 29.79 ? 507 HOH B O   1 
HETATM 4734 O  O   . HOH K 5 .   ? -12.180 -6.576  7.780   1.00 30.62 ? 508 HOH B O   1 
HETATM 4735 O  O   . HOH K 5 .   ? 4.321   -11.280 22.378  1.00 38.40 ? 509 HOH B O   1 
HETATM 4736 O  O   . HOH K 5 .   ? -13.686 -0.770  29.082  1.00 31.27 ? 510 HOH B O   1 
HETATM 4737 O  O   . HOH K 5 .   ? -18.676 -9.804  2.432   1.00 38.24 ? 511 HOH B O   1 
HETATM 4738 O  O   . HOH K 5 .   ? -37.285 -18.087 38.191  1.00 23.85 ? 512 HOH B O   1 
HETATM 4739 O  O   . HOH K 5 .   ? -35.859 -6.904  25.108  1.00 24.16 ? 513 HOH B O   1 
HETATM 4740 O  O   . HOH K 5 .   ? -26.257 -24.492 32.689  1.00 31.28 ? 514 HOH B O   1 
HETATM 4741 O  O   . HOH K 5 .   ? -7.225  -12.233 31.812  1.00 30.75 ? 515 HOH B O   1 
HETATM 4742 O  O   . HOH K 5 .   ? -20.047 -15.192 41.123  1.00 26.20 ? 516 HOH B O   1 
HETATM 4743 O  O   . HOH K 5 .   ? -1.209  -7.851  11.315  1.00 34.37 ? 517 HOH B O   1 
HETATM 4744 O  O   . HOH K 5 .   ? -41.777 -9.571  13.038  1.00 33.82 ? 518 HOH B O   1 
HETATM 4745 O  O   . HOH K 5 .   ? -23.008 -11.193 36.366  1.00 30.48 ? 519 HOH B O   1 
HETATM 4746 O  O   . HOH K 5 .   ? -9.262  0.525   18.784  1.00 41.42 ? 520 HOH B O   1 
HETATM 4747 O  O   . HOH K 5 .   ? -0.937  -18.670 16.295  1.00 25.10 ? 521 HOH B O   1 
HETATM 4748 O  O   . HOH K 5 .   ? -32.594 -15.292 14.385  1.00 28.63 ? 522 HOH B O   1 
HETATM 4749 O  O   . HOH K 5 .   ? -30.390 -1.389  26.276  1.00 26.88 ? 523 HOH B O   1 
HETATM 4750 O  O   . HOH K 5 .   ? -35.929 -13.250 24.660  1.00 31.83 ? 524 HOH B O   1 
HETATM 4751 O  O   . HOH K 5 .   ? -16.202 6.271   10.616  1.00 28.08 ? 525 HOH B O   1 
HETATM 4752 O  O   . HOH K 5 .   ? -20.095 4.763   6.604   1.00 30.39 ? 526 HOH B O   1 
HETATM 4753 O  O   . HOH K 5 .   ? -27.510 -27.301 7.162   1.00 38.58 ? 527 HOH B O   1 
HETATM 4754 O  O   . HOH K 5 .   ? -12.515 -35.565 18.890  1.00 29.82 ? 528 HOH B O   1 
HETATM 4755 O  O   . HOH K 5 .   ? -21.343 -13.749 39.199  1.00 28.73 ? 529 HOH B O   1 
HETATM 4756 O  O   . HOH K 5 .   ? -26.139 -0.266  4.571   1.00 30.89 ? 530 HOH B O   1 
HETATM 4757 O  O   . HOH K 5 .   ? -9.508  -31.771 9.623   1.00 35.20 ? 531 HOH B O   1 
HETATM 4758 O  O   . HOH K 5 .   ? -25.119 -12.675 37.495  1.00 22.07 ? 532 HOH B O   1 
HETATM 4759 O  O   . HOH K 5 .   ? -36.327 -20.190 34.850  1.00 24.39 ? 533 HOH B O   1 
HETATM 4760 O  O   . HOH K 5 .   ? -8.956  -7.186  37.949  1.00 27.30 ? 534 HOH B O   1 
HETATM 4761 O  O   . HOH K 5 .   ? -41.420 -12.987 9.064   1.00 39.59 ? 535 HOH B O   1 
HETATM 4762 O  O   . HOH K 5 .   ? -12.417 -23.265 35.738  1.00 23.73 ? 536 HOH B O   1 
HETATM 4763 O  O   . HOH K 5 .   ? -26.394 -9.871  -0.075  1.00 30.75 ? 537 HOH B O   1 
HETATM 4764 O  O   . HOH K 5 .   ? -6.011  -3.393  13.010  1.00 27.23 ? 538 HOH B O   1 
HETATM 4765 O  O   . HOH K 5 .   ? -23.799 -26.360 35.993  1.00 44.46 ? 539 HOH B O   1 
HETATM 4766 O  O   . HOH K 5 .   ? -25.965 -28.450 29.989  1.00 28.22 ? 540 HOH B O   1 
HETATM 4767 O  O   . HOH K 5 .   ? -11.559 -9.984  -0.195  1.00 42.82 ? 541 HOH B O   1 
HETATM 4768 O  O   . HOH K 5 .   ? -30.554 -26.387 23.762  1.00 36.25 ? 542 HOH B O   1 
HETATM 4769 O  O   . HOH K 5 .   ? -33.867 -16.494 16.119  1.00 40.51 ? 543 HOH B O   1 
HETATM 4770 O  O   . HOH K 5 .   ? -23.620 -26.989 29.577  1.00 29.64 ? 544 HOH B O   1 
HETATM 4771 O  O   . HOH K 5 .   ? 1.515   -12.803 24.999  1.00 33.72 ? 545 HOH B O   1 
HETATM 4772 O  O   . HOH K 5 .   ? -23.409 -9.118  34.727  1.00 29.49 ? 546 HOH B O   1 
HETATM 4773 O  O   . HOH K 5 .   ? -12.318 -30.380 6.099   1.00 37.19 ? 547 HOH B O   1 
HETATM 4774 O  O   . HOH K 5 .   ? -6.465  -2.406  33.162  1.00 30.80 ? 548 HOH B O   1 
HETATM 4775 O  O   . HOH K 5 .   ? -29.338 3.999   13.404  1.00 39.95 ? 549 HOH B O   1 
HETATM 4776 O  O   . HOH K 5 .   ? 5.049   -23.982 19.217  1.00 31.43 ? 550 HOH B O   1 
HETATM 4777 O  O   . HOH K 5 .   ? -36.142 -9.460  24.471  1.00 31.40 ? 551 HOH B O   1 
HETATM 4778 O  O   . HOH K 5 .   ? -16.335 -39.345 18.276  1.00 28.55 ? 552 HOH B O   1 
HETATM 4779 O  O   . HOH K 5 .   ? -12.913 1.814   21.802  1.00 29.12 ? 553 HOH B O   1 
HETATM 4780 O  O   . HOH K 5 .   ? -11.301 2.994   2.602   1.00 34.86 ? 554 HOH B O   1 
HETATM 4781 O  O   . HOH K 5 .   ? -18.870 7.047   25.469  1.00 32.99 ? 555 HOH B O   1 
HETATM 4782 O  O   . HOH K 5 .   ? -35.663 -14.946 14.402  1.00 44.80 ? 556 HOH B O   1 
HETATM 4783 O  O   . HOH K 5 .   ? -26.372 -25.342 35.458  1.00 35.48 ? 557 HOH B O   1 
HETATM 4784 O  O   . HOH K 5 .   ? -9.138  -26.466 25.234  1.00 23.33 ? 558 HOH B O   1 
HETATM 4785 O  O   . HOH K 5 .   ? -9.854  -23.615 34.458  1.00 24.34 ? 559 HOH B O   1 
HETATM 4786 O  O   . HOH K 5 .   ? -12.229 0.584   19.415  1.00 24.63 ? 560 HOH B O   1 
HETATM 4787 O  O   . HOH K 5 .   ? -34.365 -11.619 32.442  1.00 27.15 ? 561 HOH B O   1 
HETATM 4788 O  O   . HOH K 5 .   ? -16.080 -1.784  -2.353  1.00 30.80 ? 562 HOH B O   1 
HETATM 4789 O  O   . HOH K 5 .   ? -18.508 -3.796  28.987  1.00 22.37 ? 563 HOH B O   1 
HETATM 4790 O  O   . HOH K 5 .   ? -13.085 1.126   2.455   1.00 29.38 ? 564 HOH B O   1 
HETATM 4791 O  O   . HOH K 5 .   ? -23.187 -1.817  -0.997  1.00 30.90 ? 565 HOH B O   1 
HETATM 4792 O  O   . HOH K 5 .   ? -25.957 4.939   9.870   1.00 30.63 ? 566 HOH B O   1 
HETATM 4793 O  O   . HOH K 5 .   ? -11.006 -7.336  35.624  1.00 30.81 ? 567 HOH B O   1 
HETATM 4794 O  O   . HOH K 5 .   ? -35.832 -15.530 11.132  1.00 30.22 ? 568 HOH B O   1 
HETATM 4795 O  O   . HOH K 5 .   ? -27.639 -25.644 12.656  1.00 37.59 ? 569 HOH B O   1 
HETATM 4796 O  O   . HOH K 5 .   ? -24.571 -33.434 0.904   1.00 30.45 ? 570 HOH B O   1 
HETATM 4797 O  O   . HOH K 5 .   ? -26.519 -10.219 38.481  1.00 27.16 ? 571 HOH B O   1 
HETATM 4798 O  O   . HOH K 5 .   ? -37.062 -9.727  5.122   1.00 34.02 ? 572 HOH B O   1 
HETATM 4799 O  O   . HOH K 5 .   ? -24.939 -5.447  -0.810  1.00 30.48 ? 573 HOH B O   1 
HETATM 4800 O  O   . HOH K 5 .   ? -39.672 -14.972 8.795   1.00 43.15 ? 574 HOH B O   1 
HETATM 4801 O  O   . HOH K 5 .   ? -24.164 -20.949 39.232  1.00 29.80 ? 575 HOH B O   1 
HETATM 4802 O  O   . HOH K 5 .   ? -31.040 -21.188 9.245   1.00 39.70 ? 576 HOH B O   1 
HETATM 4803 O  O   . HOH K 5 .   ? -38.195 -4.788  7.855   1.00 39.91 ? 577 HOH B O   1 
HETATM 4804 O  O   . HOH K 5 .   ? -11.793 -35.616 16.526  1.00 32.14 ? 578 HOH B O   1 
HETATM 4805 O  O   . HOH K 5 .   ? -5.778  -2.692  19.391  1.00 30.17 ? 579 HOH B O   1 
HETATM 4806 O  O   . HOH K 5 .   ? -8.892  3.149   13.128  1.00 38.08 ? 580 HOH B O   1 
HETATM 4807 O  O   . HOH K 5 .   ? -24.993 2.273   4.180   1.00 33.40 ? 581 HOH B O   1 
HETATM 4808 O  O   . HOH K 5 .   ? -14.761 -34.218 6.746   1.00 35.14 ? 582 HOH B O   1 
HETATM 4809 O  O   . HOH K 5 .   ? -35.137 -15.041 18.996  1.00 33.89 ? 583 HOH B O   1 
HETATM 4810 O  O   . HOH K 5 .   ? -31.459 -17.203 16.942  1.00 41.30 ? 584 HOH B O   1 
HETATM 4811 O  O   . HOH K 5 .   ? -5.884  -13.538 33.596  1.00 33.17 ? 585 HOH B O   1 
HETATM 4812 O  O   . HOH K 5 .   ? -25.929 0.744   0.320   1.00 31.43 ? 586 HOH B O   1 
HETATM 4813 O  O   . HOH K 5 .   ? -35.273 -16.367 4.305   1.00 37.86 ? 587 HOH B O   1 
HETATM 4814 O  O   . HOH K 5 .   ? -10.497 -11.278 33.871  1.00 29.59 ? 588 HOH B O   1 
HETATM 4815 O  O   . HOH K 5 .   ? -23.455 -4.294  29.289  1.00 27.06 ? 589 HOH B O   1 
HETATM 4816 O  O   . HOH K 5 .   ? -29.966 -33.793 17.465  1.00 37.69 ? 590 HOH B O   1 
HETATM 4817 O  O   . HOH K 5 .   ? -17.859 -23.804 42.300  1.00 34.56 ? 591 HOH B O   1 
HETATM 4818 O  O   . HOH K 5 .   ? -13.768 -26.681 30.235  1.00 37.18 ? 592 HOH B O   1 
HETATM 4819 O  O   . HOH K 5 .   ? -13.695 -35.077 11.077  1.00 39.76 ? 593 HOH B O   1 
HETATM 4820 O  O   . HOH K 5 .   ? 4.557   -18.840 29.457  1.00 37.60 ? 594 HOH B O   1 
HETATM 4821 O  O   . HOH K 5 .   ? -28.770 -6.589  0.275   1.00 39.35 ? 595 HOH B O   1 
HETATM 4822 O  O   . HOH K 5 .   ? -27.039 -10.868 21.575  1.00 23.76 ? 596 HOH B O   1 
HETATM 4823 O  O   . HOH K 5 .   ? -18.511 -2.522  -0.446  1.00 36.85 ? 597 HOH B O   1 
HETATM 4824 O  O   . HOH K 5 .   ? -11.128 -9.915  35.787  1.00 36.75 ? 598 HOH B O   1 
HETATM 4825 O  O   . HOH K 5 .   ? -30.687 -30.404 16.818  1.00 42.28 ? 599 HOH B O   1 
HETATM 4826 O  O   . HOH K 5 .   ? -29.065 -24.240 5.879   1.00 39.09 ? 600 HOH B O   1 
HETATM 4827 O  O   . HOH K 5 .   ? -34.678 -13.890 0.701   1.00 25.10 ? 601 HOH B O   1 
HETATM 4828 O  O   . HOH K 5 .   ? -8.854  -35.530 16.800  1.00 38.73 ? 602 HOH B O   1 
HETATM 4829 O  O   . HOH K 5 .   ? -3.872  -5.001  18.965  1.00 38.16 ? 603 HOH B O   1 
HETATM 4830 O  O   . HOH K 5 .   ? -17.935 -21.611 -3.209  1.00 43.46 ? 604 HOH B O   1 
HETATM 4831 O  O   . HOH K 5 .   ? 1.171   -9.646  18.702  1.00 40.32 ? 605 HOH B O   1 
HETATM 4832 O  O   . HOH K 5 .   ? -34.201 0.026   23.663  1.00 34.57 ? 606 HOH B O   1 
HETATM 4833 O  O   . HOH K 5 .   ? -37.534 -12.387 38.879  1.00 29.64 ? 607 HOH B O   1 
HETATM 4834 O  O   . HOH K 5 .   ? -27.378 -3.766  28.653  1.00 44.14 ? 608 HOH B O   1 
HETATM 4835 O  O   . HOH K 5 .   ? -5.780  -1.120  16.988  1.00 34.91 ? 609 HOH B O   1 
HETATM 4836 O  O   . HOH K 5 .   ? -7.213  -30.926 13.969  1.00 28.61 ? 610 HOH B O   1 
HETATM 4837 O  O   . HOH K 5 .   ? -16.366 8.751   14.303  1.00 33.50 ? 611 HOH B O   1 
HETATM 4838 O  O   . HOH K 5 .   ? -34.578 -15.238 21.937  1.00 40.03 ? 612 HOH B O   1 
HETATM 4839 O  O   . HOH K 5 .   ? -29.354 -34.481 14.891  1.00 38.73 ? 613 HOH B O   1 
HETATM 4840 O  O   . HOH K 5 .   ? 0.947   -6.901  26.352  1.00 40.98 ? 614 HOH B O   1 
HETATM 4841 O  O   . HOH K 5 .   ? -0.038  -9.715  9.182   1.00 43.67 ? 615 HOH B O   1 
HETATM 4842 O  O   . HOH K 5 .   ? -32.640 -15.955 20.010  1.00 36.80 ? 616 HOH B O   1 
HETATM 4843 O  O   . HOH K 5 .   ? -3.299  -5.161  16.611  1.00 37.48 ? 617 HOH B O   1 
HETATM 4844 O  O   . HOH K 5 .   ? -28.945 -22.190 6.913   1.00 41.74 ? 618 HOH B O   1 
HETATM 4845 O  O   . HOH K 5 .   ? -12.879 -22.958 0.902   1.00 33.68 ? 619 HOH B O   1 
HETATM 4846 O  O   . HOH K 5 .   ? -11.183 -26.003 31.133  1.00 32.82 ? 620 HOH B O   1 
HETATM 4847 O  O   . HOH K 5 .   ? -29.520 -32.094 13.062  1.00 34.94 ? 621 HOH B O   1 
HETATM 4848 O  O   . HOH K 5 .   ? -4.301  -2.866  15.157  1.00 30.28 ? 622 HOH B O   1 
HETATM 4849 O  O   . HOH K 5 .   ? -16.364 -25.913 36.350  1.00 38.74 ? 623 HOH B O   1 
HETATM 4850 O  O   . HOH K 5 .   ? -1.744  -6.988  16.300  1.00 36.22 ? 624 HOH B O   1 
HETATM 4851 O  O   . HOH K 5 .   ? -4.625  -29.772 14.260  1.00 35.76 ? 625 HOH B O   1 
HETATM 4852 O  O   . HOH K 5 .   ? -38.621 2.303   22.491  1.00 30.51 ? 626 HOH B O   1 
HETATM 4853 O  O   . HOH K 5 .   ? 3.875   -24.254 27.970  1.00 46.45 ? 627 HOH B O   1 
HETATM 4854 O  O   . HOH K 5 .   ? -25.029 -33.297 24.876  1.00 37.73 ? 628 HOH B O   1 
HETATM 4855 O  O   . HOH K 5 .   ? -28.351 4.266   10.917  1.00 35.82 ? 629 HOH B O   1 
HETATM 4856 O  O   . HOH K 5 .   ? -22.242 -23.965 38.576  1.00 33.72 ? 630 HOH B O   1 
HETATM 4857 O  O   . HOH K 5 .   ? -26.343 -23.177 38.036  1.00 37.81 ? 631 HOH B O   1 
HETATM 4858 O  O   . HOH K 5 .   ? -23.965 -1.666  -4.108  1.00 44.05 ? 632 HOH B O   1 
HETATM 4859 O  O   . HOH K 5 .   ? -21.066 -3.177  -1.402  1.00 32.88 ? 633 HOH B O   1 
HETATM 4860 O  O   . HOH K 5 .   ? -15.315 -14.277 42.171  1.00 35.76 ? 634 HOH B O   1 
HETATM 4861 O  O   . HOH K 5 .   ? -29.677 -26.768 29.925  1.00 35.96 ? 635 HOH B O   1 
HETATM 4862 O  O   . HOH K 5 .   ? -30.657 -25.414 27.504  1.00 36.63 ? 636 HOH B O   1 
HETATM 4863 O  O   . HOH K 5 .   ? -32.764 -20.816 26.723  1.00 37.16 ? 637 HOH B O   1 
HETATM 4864 O  O   . HOH K 5 .   ? -33.185 -17.270 23.460  1.00 34.31 ? 638 HOH B O   1 
HETATM 4865 O  O   . HOH K 5 .   ? -32.082 -13.968 41.568  1.00 31.15 ? 639 HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   ARG 4   4   ?   ?   ?   A . n 
A 1 5   LEU 5   5   ?   ?   ?   A . n 
A 1 6   SER 6   6   6   SER SER A . n 
A 1 7   TRP 7   7   7   TRP TRP A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  TRP 18  18  18  TRP TRP A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ARG 82  82  82  ARG ARG A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  TRP 99  99  99  TRP TRP A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 GLY 106 106 106 GLY GLY A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 HIS 109 109 109 HIS HIS A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 HIS 124 124 124 HIS HIS A . n 
A 1 125 TRP 125 125 125 TRP TRP A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 PRO 140 140 140 PRO PRO A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 GLY 142 142 142 GLY GLY A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 GLN 151 151 151 GLN GLN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 GLU 154 154 154 GLU GLU A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 GLN 158 158 158 GLN GLN A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 GLN 160 160 160 GLN GLN A . n 
A 1 161 LYS 161 161 161 LYS LYS A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 THR 165 165 165 THR THR A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 LYS 172 172 172 LYS LYS A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 PRO 189 189 189 PRO PRO A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 TRP 191 191 191 TRP TRP A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 TRP 194 194 194 TRP TRP A . n 
A 1 195 THR 195 195 195 THR THR A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 PRO 203 203 203 PRO PRO A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 TRP 211 211 211 TRP TRP A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 VAL 213 213 213 VAL VAL A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 PRO 217 217 217 PRO PRO A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 GLN 223 223 223 GLN GLN A . n 
A 1 224 GLN 224 224 224 GLN GLN A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 PHE 228 228 228 PHE PHE A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 CYS 233 233 233 CYS CYS A . n 
A 1 234 THR 234 234 234 THR THR A . n 
A 1 235 ALA 235 235 235 ALA ALA A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 SER 245 245 245 SER SER A . n 
A 1 246 ASN 246 246 246 ASN ASN A . n 
A 1 247 HIS 247 247 247 HIS HIS A . n 
A 1 248 ARG 248 248 248 ARG ARG A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 PRO 250 250 250 PRO PRO A . n 
A 1 251 GLN 251 251 251 GLN GLN A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 LYS 257 257 257 LYS LYS A . n 
A 1 258 VAL 258 258 258 VAL VAL A . n 
A 1 259 ARG 259 259 259 ARG ARG A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 HIS 263 263 263 HIS HIS A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   MET 2   2   ?   ?   ?   B . n 
B 1 3   SER 3   3   ?   ?   ?   B . n 
B 1 4   ARG 4   4   ?   ?   ?   B . n 
B 1 5   LEU 5   5   ?   ?   ?   B . n 
B 1 6   SER 6   6   6   SER SER B . n 
B 1 7   TRP 7   7   7   TRP TRP B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  GLU 11  11  11  GLU GLU B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  ILE 16  16  16  ILE ILE B . n 
B 1 17  HIS 17  17  17  HIS HIS B . n 
B 1 18  TRP 18  18  18  TRP TRP B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  GLU 20  20  20  GLU GLU B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  PHE 22  22  22  PHE PHE B . n 
B 1 23  PRO 23  23  23  PRO PRO B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  ASP 26  26  26  ASP ASP B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  GLN 29  29  29  GLN GLN B . n 
B 1 30  GLN 30  30  30  GLN GLN B . n 
B 1 31  SER 31  31  31  SER SER B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  GLU 34  34  34  GLU GLU B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  LYS 38  38  38  LYS LYS B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  VAL 40  40  40  VAL VAL B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  ASP 43  43  43  ASP ASP B . n 
B 1 44  SER 44  44  44  SER SER B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  ARG 47  47  47  ARG ARG B . n 
B 1 48  PRO 48  48  48  PRO PRO B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  ILE 51  51  51  ILE ILE B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  TYR 53  53  53  TYR TYR B . n 
B 1 54  ASP 54  54  54  ASP ASP B . n 
B 1 55  PRO 55  55  55  PRO PRO B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  SER 57  57  57  SER SER B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  LYS 59  59  59  LYS LYS B . n 
B 1 60  ILE 60  60  60  ILE ILE B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  SER 64  64  64  SER SER B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  PHE 68  68  68  PHE PHE B . n 
B 1 69  ASN 69  69  69  ASN ASN B . n 
B 1 70  VAL 70  70  70  VAL VAL B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  PHE 72  72  72  PHE PHE B . n 
B 1 73  ASP 73  73  73  ASP ASP B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  THR 75  75  75  THR THR B . n 
B 1 76  GLU 76  76  76  GLU GLU B . n 
B 1 77  ASN 77  77  77  ASN ASN B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  SER 79  79  79  SER SER B . n 
B 1 80  VAL 80  80  80  VAL VAL B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  ARG 82  82  82  ARG ARG B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  PRO 85  85  85  PRO PRO B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  GLY 88  88  88  GLY GLY B . n 
B 1 89  SER 89  89  89  SER SER B . n 
B 1 90  TYR 90  90  90  TYR TYR B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  ARG 93  93  93  ARG ARG B . n 
B 1 94  GLN 94  94  94  GLN GLN B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  HIS 98  98  98  HIS HIS B . n 
B 1 99  TRP 99  99  99  TRP TRP B . n 
B 1 100 GLY 100 100 100 GLY GLY B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 ASP 104 104 104 ASP ASP B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 GLY 106 106 106 GLY GLY B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLU 108 108 108 GLU GLU B . n 
B 1 109 HIS 109 109 109 HIS HIS B . n 
B 1 110 ILE 110 110 110 ILE ILE B . n 
B 1 111 VAL 111 111 111 VAL VAL B . n 
B 1 112 ASP 112 112 112 ASP ASP B . n 
B 1 113 GLY 113 113 113 GLY GLY B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 ALA 118 118 118 ALA ALA B . n 
B 1 119 GLU 119 119 119 GLU GLU B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 HIS 121 121 121 HIS HIS B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 VAL 123 123 123 VAL VAL B . n 
B 1 124 HIS 124 124 124 HIS HIS B . n 
B 1 125 TRP 125 125 125 TRP TRP B . n 
B 1 126 ASN 126 126 126 ASN ASN B . n 
B 1 127 SER 127 127 127 SER SER B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 LYS 129 129 129 LYS LYS B . n 
B 1 130 TYR 130 130 130 TYR TYR B . n 
B 1 131 PRO 131 131 131 PRO PRO B . n 
B 1 132 SER 132 132 132 SER SER B . n 
B 1 133 PHE 133 133 133 PHE PHE B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 ALA 136 136 136 ALA ALA B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 PRO 140 140 140 PRO PRO B . n 
B 1 141 ASP 141 141 141 ASP ASP B . n 
B 1 142 GLY 142 142 142 GLY GLY B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 ALA 144 144 144 ALA ALA B . n 
B 1 145 VAL 145 145 145 VAL VAL B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 PHE 149 149 149 PHE PHE B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 GLN 151 151 151 GLN GLN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 GLY 153 153 153 GLY GLY B . n 
B 1 154 GLU 154 154 154 GLU GLU B . n 
B 1 155 PRO 155 155 155 PRO PRO B . n 
B 1 156 ASN 156 156 156 ASN ASN B . n 
B 1 157 SER 157 157 157 SER SER B . n 
B 1 158 GLN 158 158 158 GLN GLN B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 GLN 160 160 160 GLN GLN B . n 
B 1 161 LYS 161 161 161 LYS LYS B . n 
B 1 162 ILE 162 162 162 ILE ILE B . n 
B 1 163 THR 163 163 163 THR THR B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 THR 165 165 165 THR THR B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ASP 167 167 167 ASP ASP B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 LYS 170 170 170 LYS LYS B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 LYS 172 172 172 LYS LYS B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 LYS 174 174 174 LYS LYS B . n 
B 1 175 GLN 175 175 175 GLN GLN B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 ASP 182 182 182 ASP ASP B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 SER 185 185 185 SER SER B . n 
B 1 186 LEU 186 186 186 LEU LEU B . n 
B 1 187 LEU 187 187 187 LEU LEU B . n 
B 1 188 PRO 188 188 188 PRO PRO B . n 
B 1 189 PRO 189 189 189 PRO PRO B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 TRP 191 191 191 TRP TRP B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 TRP 194 194 194 TRP TRP B . n 
B 1 195 THR 195 195 195 THR THR B . n 
B 1 196 TYR 196 196 196 TYR TYR B . n 
B 1 197 PRO 197 197 197 PRO PRO B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 SER 199 199 199 SER SER B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 PRO 203 203 203 PRO PRO B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 GLU 207 207 207 GLU GLU B . n 
B 1 208 SER 208 208 208 SER SER B . n 
B 1 209 VAL 209 209 209 VAL VAL B . n 
B 1 210 THR 210 210 210 THR THR B . n 
B 1 211 TRP 211 211 211 TRP TRP B . n 
B 1 212 ILE 212 212 212 ILE ILE B . n 
B 1 213 VAL 213 213 213 VAL VAL B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 LYS 215 215 215 LYS LYS B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 PRO 217 217 217 PRO PRO B . n 
B 1 218 ILE 218 218 218 ILE ILE B . n 
B 1 219 ASN 219 219 219 ASN ASN B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 SER 221 221 221 SER SER B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 GLN 223 223 223 GLN GLN B . n 
B 1 224 GLN 224 224 224 GLN GLN B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 ALA 226 226 226 ALA ALA B . n 
B 1 227 LYS 227 227 227 LYS LYS B . n 
B 1 228 PHE 228 228 228 PHE PHE B . n 
B 1 229 ARG 229 229 229 ARG ARG B . n 
B 1 230 SER 230 230 230 SER SER B . n 
B 1 231 LEU 231 231 231 LEU LEU B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 CYS 233 233 233 CYS CYS B . n 
B 1 234 THR 234 234 234 THR THR B . n 
B 1 235 ALA 235 235 235 ALA ALA B . n 
B 1 236 GLU 236 236 236 GLU GLU B . n 
B 1 237 GLY 237 237 237 GLY GLY B . n 
B 1 238 GLU 238 238 238 GLU GLU B . n 
B 1 239 ALA 239 239 239 ALA ALA B . n 
B 1 240 ALA 240 240 240 ALA ALA B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 PHE 242 242 242 PHE PHE B . n 
B 1 243 LEU 243 243 243 LEU LEU B . n 
B 1 244 VAL 244 244 244 VAL VAL B . n 
B 1 245 SER 245 245 245 SER SER B . n 
B 1 246 ASN 246 246 246 ASN ASN B . n 
B 1 247 HIS 247 247 247 HIS HIS B . n 
B 1 248 ARG 248 248 248 ARG ARG B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 PRO 250 250 250 PRO PRO B . n 
B 1 251 GLN 251 251 251 GLN GLN B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 LYS 254 254 254 LYS LYS B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 ARG 256 256 256 ARG ARG B . n 
B 1 257 LYS 257 257 257 LYS LYS B . n 
B 1 258 VAL 258 258 258 VAL VAL B . n 
B 1 259 ARG 259 259 259 ARG ARG B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 SER 261 261 261 SER SER B . n 
B 1 262 PHE 262 262 262 PHE PHE B . n 
B 1 263 HIS 263 263 263 HIS HIS B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN  1   301 301 ZN  ZN  A . 
D 3 EDO 1   302 302 EDO EDO A . 
E 3 EDO 1   303 303 EDO EDO A . 
F 4 WWX 1   304 304 WWX WWX A . 
G 2 ZN  1   301 301 ZN  ZN  B . 
H 3 EDO 1   302 302 EDO EDO B . 
I 4 WWX 1   303 303 WWX WWX B . 
J 5 HOH 1   401 401 HOH HOH A . 
J 5 HOH 2   402 402 HOH HOH A . 
J 5 HOH 3   403 403 HOH HOH A . 
J 5 HOH 4   404 404 HOH HOH A . 
J 5 HOH 5   405 405 HOH HOH A . 
J 5 HOH 6   406 406 HOH HOH A . 
J 5 HOH 7   407 407 HOH HOH A . 
J 5 HOH 8   408 408 HOH HOH A . 
J 5 HOH 9   409 409 HOH HOH A . 
J 5 HOH 10  410 410 HOH HOH A . 
J 5 HOH 11  411 411 HOH HOH A . 
J 5 HOH 12  412 412 HOH HOH A . 
J 5 HOH 13  413 413 HOH HOH A . 
J 5 HOH 14  414 414 HOH HOH A . 
J 5 HOH 15  415 415 HOH HOH A . 
J 5 HOH 16  416 416 HOH HOH A . 
J 5 HOH 17  417 417 HOH HOH A . 
J 5 HOH 18  418 418 HOH HOH A . 
J 5 HOH 19  419 419 HOH HOH A . 
J 5 HOH 20  420 420 HOH HOH A . 
J 5 HOH 21  421 421 HOH HOH A . 
J 5 HOH 22  422 422 HOH HOH A . 
J 5 HOH 23  423 423 HOH HOH A . 
J 5 HOH 24  424 424 HOH HOH A . 
J 5 HOH 25  425 425 HOH HOH A . 
J 5 HOH 26  426 426 HOH HOH A . 
J 5 HOH 27  427 427 HOH HOH A . 
J 5 HOH 28  428 428 HOH HOH A . 
J 5 HOH 29  429 429 HOH HOH A . 
J 5 HOH 30  430 430 HOH HOH A . 
J 5 HOH 31  431 431 HOH HOH A . 
J 5 HOH 32  432 432 HOH HOH A . 
J 5 HOH 33  433 433 HOH HOH A . 
J 5 HOH 34  434 434 HOH HOH A . 
J 5 HOH 35  435 435 HOH HOH A . 
J 5 HOH 36  436 436 HOH HOH A . 
J 5 HOH 37  437 437 HOH HOH A . 
J 5 HOH 38  438 438 HOH HOH A . 
J 5 HOH 39  439 439 HOH HOH A . 
J 5 HOH 40  440 440 HOH HOH A . 
J 5 HOH 41  441 441 HOH HOH A . 
J 5 HOH 42  442 442 HOH HOH A . 
J 5 HOH 43  443 443 HOH HOH A . 
J 5 HOH 44  444 444 HOH HOH A . 
J 5 HOH 45  445 445 HOH HOH A . 
J 5 HOH 46  446 446 HOH HOH A . 
J 5 HOH 47  447 447 HOH HOH A . 
J 5 HOH 48  448 448 HOH HOH A . 
J 5 HOH 49  449 449 HOH HOH A . 
J 5 HOH 50  450 450 HOH HOH A . 
J 5 HOH 51  451 451 HOH HOH A . 
J 5 HOH 52  452 452 HOH HOH A . 
J 5 HOH 53  453 453 HOH HOH A . 
J 5 HOH 54  454 454 HOH HOH A . 
J 5 HOH 55  455 455 HOH HOH A . 
J 5 HOH 56  456 456 HOH HOH A . 
J 5 HOH 57  457 457 HOH HOH A . 
J 5 HOH 58  458 458 HOH HOH A . 
J 5 HOH 59  459 459 HOH HOH A . 
J 5 HOH 60  460 460 HOH HOH A . 
J 5 HOH 61  461 461 HOH HOH A . 
J 5 HOH 62  462 462 HOH HOH A . 
J 5 HOH 63  463 463 HOH HOH A . 
J 5 HOH 64  464 464 HOH HOH A . 
J 5 HOH 65  465 465 HOH HOH A . 
J 5 HOH 66  466 466 HOH HOH A . 
J 5 HOH 67  467 467 HOH HOH A . 
J 5 HOH 68  468 468 HOH HOH A . 
J 5 HOH 69  469 469 HOH HOH A . 
J 5 HOH 70  470 470 HOH HOH A . 
J 5 HOH 71  471 471 HOH HOH A . 
J 5 HOH 72  472 472 HOH HOH A . 
J 5 HOH 73  473 473 HOH HOH A . 
J 5 HOH 74  474 474 HOH HOH A . 
J 5 HOH 75  475 475 HOH HOH A . 
J 5 HOH 76  476 476 HOH HOH A . 
J 5 HOH 77  477 477 HOH HOH A . 
J 5 HOH 78  478 478 HOH HOH A . 
J 5 HOH 79  479 479 HOH HOH A . 
J 5 HOH 80  480 480 HOH HOH A . 
J 5 HOH 81  481 481 HOH HOH A . 
J 5 HOH 82  482 482 HOH HOH A . 
J 5 HOH 83  483 483 HOH HOH A . 
J 5 HOH 84  484 484 HOH HOH A . 
J 5 HOH 85  485 485 HOH HOH A . 
J 5 HOH 86  486 486 HOH HOH A . 
J 5 HOH 87  487 487 HOH HOH A . 
J 5 HOH 88  488 488 HOH HOH A . 
J 5 HOH 89  489 489 HOH HOH A . 
J 5 HOH 90  490 490 HOH HOH A . 
J 5 HOH 91  491 491 HOH HOH A . 
J 5 HOH 92  492 492 HOH HOH A . 
J 5 HOH 93  493 493 HOH HOH A . 
J 5 HOH 94  494 494 HOH HOH A . 
J 5 HOH 95  495 495 HOH HOH A . 
J 5 HOH 96  496 496 HOH HOH A . 
J 5 HOH 97  497 497 HOH HOH A . 
J 5 HOH 98  498 498 HOH HOH A . 
J 5 HOH 99  499 499 HOH HOH A . 
J 5 HOH 100 500 500 HOH HOH A . 
J 5 HOH 101 501 501 HOH HOH A . 
J 5 HOH 102 502 502 HOH HOH A . 
J 5 HOH 103 503 503 HOH HOH A . 
J 5 HOH 104 504 504 HOH HOH A . 
J 5 HOH 105 505 505 HOH HOH A . 
J 5 HOH 106 506 506 HOH HOH A . 
J 5 HOH 107 507 507 HOH HOH A . 
J 5 HOH 108 508 508 HOH HOH A . 
J 5 HOH 109 509 509 HOH HOH A . 
J 5 HOH 110 510 510 HOH HOH A . 
J 5 HOH 111 511 511 HOH HOH A . 
J 5 HOH 112 512 512 HOH HOH A . 
J 5 HOH 113 513 513 HOH HOH A . 
J 5 HOH 114 514 514 HOH HOH A . 
J 5 HOH 115 515 515 HOH HOH A . 
J 5 HOH 116 516 516 HOH HOH A . 
J 5 HOH 117 517 517 HOH HOH A . 
J 5 HOH 118 518 518 HOH HOH A . 
J 5 HOH 119 519 519 HOH HOH A . 
J 5 HOH 120 520 520 HOH HOH A . 
J 5 HOH 121 521 521 HOH HOH A . 
J 5 HOH 122 522 522 HOH HOH A . 
J 5 HOH 123 523 523 HOH HOH A . 
J 5 HOH 124 524 524 HOH HOH A . 
J 5 HOH 125 525 525 HOH HOH A . 
J 5 HOH 126 526 526 HOH HOH A . 
J 5 HOH 127 527 527 HOH HOH A . 
J 5 HOH 128 528 528 HOH HOH A . 
J 5 HOH 129 529 529 HOH HOH A . 
J 5 HOH 130 530 530 HOH HOH A . 
J 5 HOH 131 531 531 HOH HOH A . 
J 5 HOH 132 532 532 HOH HOH A . 
J 5 HOH 133 533 533 HOH HOH A . 
J 5 HOH 134 534 534 HOH HOH A . 
J 5 HOH 135 535 535 HOH HOH A . 
J 5 HOH 136 536 536 HOH HOH A . 
J 5 HOH 137 537 537 HOH HOH A . 
J 5 HOH 138 538 538 HOH HOH A . 
J 5 HOH 139 539 539 HOH HOH A . 
J 5 HOH 140 540 540 HOH HOH A . 
J 5 HOH 141 541 541 HOH HOH A . 
J 5 HOH 142 542 542 HOH HOH A . 
J 5 HOH 143 543 543 HOH HOH A . 
J 5 HOH 144 544 544 HOH HOH A . 
J 5 HOH 145 545 545 HOH HOH A . 
J 5 HOH 146 546 546 HOH HOH A . 
J 5 HOH 147 547 547 HOH HOH A . 
J 5 HOH 148 548 548 HOH HOH A . 
J 5 HOH 149 549 549 HOH HOH A . 
J 5 HOH 150 550 550 HOH HOH A . 
J 5 HOH 151 551 551 HOH HOH A . 
J 5 HOH 152 552 552 HOH HOH A . 
J 5 HOH 153 553 553 HOH HOH A . 
J 5 HOH 154 554 554 HOH HOH A . 
J 5 HOH 155 555 555 HOH HOH A . 
J 5 HOH 156 556 556 HOH HOH A . 
J 5 HOH 157 557 557 HOH HOH A . 
J 5 HOH 158 558 558 HOH HOH A . 
J 5 HOH 159 559 559 HOH HOH A . 
J 5 HOH 160 560 560 HOH HOH A . 
J 5 HOH 161 561 561 HOH HOH A . 
J 5 HOH 162 562 562 HOH HOH A . 
J 5 HOH 163 563 563 HOH HOH A . 
J 5 HOH 164 564 564 HOH HOH A . 
J 5 HOH 165 565 565 HOH HOH A . 
J 5 HOH 166 566 566 HOH HOH A . 
J 5 HOH 167 567 567 HOH HOH A . 
J 5 HOH 168 568 568 HOH HOH A . 
J 5 HOH 169 569 569 HOH HOH A . 
J 5 HOH 170 570 570 HOH HOH A . 
J 5 HOH 171 571 571 HOH HOH A . 
J 5 HOH 172 572 572 HOH HOH A . 
J 5 HOH 173 573 573 HOH HOH A . 
J 5 HOH 174 574 574 HOH HOH A . 
J 5 HOH 175 575 575 HOH HOH A . 
J 5 HOH 176 576 576 HOH HOH A . 
J 5 HOH 177 577 577 HOH HOH A . 
J 5 HOH 178 578 578 HOH HOH A . 
J 5 HOH 179 579 579 HOH HOH A . 
J 5 HOH 180 580 580 HOH HOH A . 
J 5 HOH 181 581 581 HOH HOH A . 
J 5 HOH 182 582 582 HOH HOH A . 
J 5 HOH 183 583 583 HOH HOH A . 
J 5 HOH 184 584 584 HOH HOH A . 
J 5 HOH 185 585 585 HOH HOH A . 
J 5 HOH 186 586 586 HOH HOH A . 
J 5 HOH 187 587 587 HOH HOH A . 
J 5 HOH 188 588 588 HOH HOH A . 
J 5 HOH 189 589 589 HOH HOH A . 
J 5 HOH 190 590 590 HOH HOH A . 
J 5 HOH 191 591 591 HOH HOH A . 
J 5 HOH 192 592 592 HOH HOH A . 
J 5 HOH 193 593 593 HOH HOH A . 
J 5 HOH 194 594 594 HOH HOH A . 
J 5 HOH 195 595 595 HOH HOH A . 
J 5 HOH 196 596 596 HOH HOH A . 
J 5 HOH 197 597 597 HOH HOH A . 
J 5 HOH 198 598 598 HOH HOH A . 
J 5 HOH 199 599 599 HOH HOH A . 
J 5 HOH 200 600 600 HOH HOH A . 
J 5 HOH 201 601 601 HOH HOH A . 
J 5 HOH 202 602 602 HOH HOH A . 
J 5 HOH 203 603 603 HOH HOH A . 
J 5 HOH 204 604 604 HOH HOH A . 
J 5 HOH 205 605 605 HOH HOH A . 
J 5 HOH 206 606 606 HOH HOH A . 
J 5 HOH 207 607 607 HOH HOH A . 
J 5 HOH 208 608 608 HOH HOH A . 
J 5 HOH 209 609 609 HOH HOH A . 
J 5 HOH 210 610 610 HOH HOH A . 
J 5 HOH 211 611 611 HOH HOH A . 
J 5 HOH 212 612 612 HOH HOH A . 
J 5 HOH 213 613 613 HOH HOH A . 
J 5 HOH 214 614 614 HOH HOH A . 
J 5 HOH 215 615 615 HOH HOH A . 
J 5 HOH 216 616 616 HOH HOH A . 
J 5 HOH 217 617 617 HOH HOH A . 
J 5 HOH 218 618 618 HOH HOH A . 
J 5 HOH 219 619 619 HOH HOH A . 
J 5 HOH 220 620 620 HOH HOH A . 
J 5 HOH 221 621 621 HOH HOH A . 
J 5 HOH 222 622 622 HOH HOH A . 
J 5 HOH 223 623 623 HOH HOH A . 
J 5 HOH 224 624 624 HOH HOH A . 
J 5 HOH 225 625 625 HOH HOH A . 
J 5 HOH 226 626 626 HOH HOH A . 
J 5 HOH 227 627 627 HOH HOH A . 
J 5 HOH 228 628 628 HOH HOH A . 
J 5 HOH 229 629 629 HOH HOH A . 
J 5 HOH 230 630 630 HOH HOH A . 
J 5 HOH 231 631 631 HOH HOH A . 
J 5 HOH 232 632 632 HOH HOH A . 
J 5 HOH 233 633 633 HOH HOH A . 
J 5 HOH 234 634 634 HOH HOH A . 
J 5 HOH 235 635 635 HOH HOH A . 
J 5 HOH 236 636 636 HOH HOH A . 
J 5 HOH 237 637 637 HOH HOH A . 
J 5 HOH 238 638 638 HOH HOH A . 
J 5 HOH 239 639 639 HOH HOH A . 
J 5 HOH 240 640 640 HOH HOH A . 
J 5 HOH 241 641 641 HOH HOH A . 
J 5 HOH 242 642 642 HOH HOH A . 
J 5 HOH 243 643 643 HOH HOH A . 
J 5 HOH 244 644 644 HOH HOH A . 
J 5 HOH 245 645 645 HOH HOH A . 
K 5 HOH 1   401 401 HOH HOH B . 
K 5 HOH 2   402 402 HOH HOH B . 
K 5 HOH 3   403 403 HOH HOH B . 
K 5 HOH 4   404 404 HOH HOH B . 
K 5 HOH 5   405 405 HOH HOH B . 
K 5 HOH 6   406 406 HOH HOH B . 
K 5 HOH 7   407 407 HOH HOH B . 
K 5 HOH 8   408 408 HOH HOH B . 
K 5 HOH 9   409 409 HOH HOH B . 
K 5 HOH 10  410 410 HOH HOH B . 
K 5 HOH 11  411 411 HOH HOH B . 
K 5 HOH 12  412 412 HOH HOH B . 
K 5 HOH 13  413 413 HOH HOH B . 
K 5 HOH 14  414 414 HOH HOH B . 
K 5 HOH 15  415 415 HOH HOH B . 
K 5 HOH 16  416 416 HOH HOH B . 
K 5 HOH 17  417 417 HOH HOH B . 
K 5 HOH 18  418 418 HOH HOH B . 
K 5 HOH 19  419 419 HOH HOH B . 
K 5 HOH 20  420 420 HOH HOH B . 
K 5 HOH 21  421 421 HOH HOH B . 
K 5 HOH 22  422 422 HOH HOH B . 
K 5 HOH 23  423 423 HOH HOH B . 
K 5 HOH 24  424 424 HOH HOH B . 
K 5 HOH 25  425 425 HOH HOH B . 
K 5 HOH 26  426 426 HOH HOH B . 
K 5 HOH 27  427 427 HOH HOH B . 
K 5 HOH 28  428 428 HOH HOH B . 
K 5 HOH 29  429 429 HOH HOH B . 
K 5 HOH 30  430 430 HOH HOH B . 
K 5 HOH 31  431 431 HOH HOH B . 
K 5 HOH 32  432 432 HOH HOH B . 
K 5 HOH 33  433 433 HOH HOH B . 
K 5 HOH 34  434 434 HOH HOH B . 
K 5 HOH 35  435 435 HOH HOH B . 
K 5 HOH 36  436 436 HOH HOH B . 
K 5 HOH 37  437 437 HOH HOH B . 
K 5 HOH 38  438 438 HOH HOH B . 
K 5 HOH 39  439 439 HOH HOH B . 
K 5 HOH 40  440 440 HOH HOH B . 
K 5 HOH 41  441 441 HOH HOH B . 
K 5 HOH 42  442 442 HOH HOH B . 
K 5 HOH 43  443 443 HOH HOH B . 
K 5 HOH 44  444 444 HOH HOH B . 
K 5 HOH 45  445 445 HOH HOH B . 
K 5 HOH 46  446 446 HOH HOH B . 
K 5 HOH 47  447 447 HOH HOH B . 
K 5 HOH 48  448 448 HOH HOH B . 
K 5 HOH 49  449 449 HOH HOH B . 
K 5 HOH 50  450 450 HOH HOH B . 
K 5 HOH 51  451 451 HOH HOH B . 
K 5 HOH 52  452 452 HOH HOH B . 
K 5 HOH 53  453 453 HOH HOH B . 
K 5 HOH 54  454 454 HOH HOH B . 
K 5 HOH 55  455 455 HOH HOH B . 
K 5 HOH 56  456 456 HOH HOH B . 
K 5 HOH 57  457 457 HOH HOH B . 
K 5 HOH 58  458 458 HOH HOH B . 
K 5 HOH 59  459 459 HOH HOH B . 
K 5 HOH 60  460 460 HOH HOH B . 
K 5 HOH 61  461 461 HOH HOH B . 
K 5 HOH 62  462 462 HOH HOH B . 
K 5 HOH 63  463 463 HOH HOH B . 
K 5 HOH 64  464 464 HOH HOH B . 
K 5 HOH 65  465 465 HOH HOH B . 
K 5 HOH 66  466 466 HOH HOH B . 
K 5 HOH 67  467 467 HOH HOH B . 
K 5 HOH 68  468 468 HOH HOH B . 
K 5 HOH 69  469 469 HOH HOH B . 
K 5 HOH 70  470 470 HOH HOH B . 
K 5 HOH 71  471 471 HOH HOH B . 
K 5 HOH 72  472 472 HOH HOH B . 
K 5 HOH 73  473 473 HOH HOH B . 
K 5 HOH 74  474 474 HOH HOH B . 
K 5 HOH 75  475 475 HOH HOH B . 
K 5 HOH 76  476 476 HOH HOH B . 
K 5 HOH 77  477 477 HOH HOH B . 
K 5 HOH 78  478 478 HOH HOH B . 
K 5 HOH 79  479 479 HOH HOH B . 
K 5 HOH 80  480 480 HOH HOH B . 
K 5 HOH 81  481 481 HOH HOH B . 
K 5 HOH 82  482 482 HOH HOH B . 
K 5 HOH 83  483 483 HOH HOH B . 
K 5 HOH 84  484 484 HOH HOH B . 
K 5 HOH 85  485 485 HOH HOH B . 
K 5 HOH 86  486 486 HOH HOH B . 
K 5 HOH 87  487 487 HOH HOH B . 
K 5 HOH 88  488 488 HOH HOH B . 
K 5 HOH 89  489 489 HOH HOH B . 
K 5 HOH 90  490 490 HOH HOH B . 
K 5 HOH 91  491 491 HOH HOH B . 
K 5 HOH 92  492 492 HOH HOH B . 
K 5 HOH 93  493 493 HOH HOH B . 
K 5 HOH 94  494 494 HOH HOH B . 
K 5 HOH 95  495 495 HOH HOH B . 
K 5 HOH 96  496 496 HOH HOH B . 
K 5 HOH 97  497 497 HOH HOH B . 
K 5 HOH 98  498 498 HOH HOH B . 
K 5 HOH 99  499 499 HOH HOH B . 
K 5 HOH 100 500 500 HOH HOH B . 
K 5 HOH 101 501 501 HOH HOH B . 
K 5 HOH 102 502 502 HOH HOH B . 
K 5 HOH 103 503 503 HOH HOH B . 
K 5 HOH 104 504 504 HOH HOH B . 
K 5 HOH 105 505 505 HOH HOH B . 
K 5 HOH 106 506 506 HOH HOH B . 
K 5 HOH 107 507 507 HOH HOH B . 
K 5 HOH 108 508 508 HOH HOH B . 
K 5 HOH 109 509 509 HOH HOH B . 
K 5 HOH 110 510 510 HOH HOH B . 
K 5 HOH 111 511 511 HOH HOH B . 
K 5 HOH 112 512 512 HOH HOH B . 
K 5 HOH 113 513 513 HOH HOH B . 
K 5 HOH 114 514 514 HOH HOH B . 
K 5 HOH 115 515 515 HOH HOH B . 
K 5 HOH 116 516 516 HOH HOH B . 
K 5 HOH 117 517 517 HOH HOH B . 
K 5 HOH 118 518 518 HOH HOH B . 
K 5 HOH 119 519 519 HOH HOH B . 
K 5 HOH 120 520 520 HOH HOH B . 
K 5 HOH 121 521 521 HOH HOH B . 
K 5 HOH 122 522 522 HOH HOH B . 
K 5 HOH 123 523 523 HOH HOH B . 
K 5 HOH 124 524 524 HOH HOH B . 
K 5 HOH 125 525 525 HOH HOH B . 
K 5 HOH 126 526 526 HOH HOH B . 
K 5 HOH 127 527 527 HOH HOH B . 
K 5 HOH 128 528 528 HOH HOH B . 
K 5 HOH 129 529 529 HOH HOH B . 
K 5 HOH 130 530 530 HOH HOH B . 
K 5 HOH 131 531 531 HOH HOH B . 
K 5 HOH 132 532 532 HOH HOH B . 
K 5 HOH 133 533 533 HOH HOH B . 
K 5 HOH 134 534 534 HOH HOH B . 
K 5 HOH 135 535 535 HOH HOH B . 
K 5 HOH 136 536 536 HOH HOH B . 
K 5 HOH 137 537 537 HOH HOH B . 
K 5 HOH 138 538 538 HOH HOH B . 
K 5 HOH 139 539 539 HOH HOH B . 
K 5 HOH 140 540 540 HOH HOH B . 
K 5 HOH 141 541 541 HOH HOH B . 
K 5 HOH 142 542 542 HOH HOH B . 
K 5 HOH 143 543 543 HOH HOH B . 
K 5 HOH 144 544 544 HOH HOH B . 
K 5 HOH 145 545 545 HOH HOH B . 
K 5 HOH 146 546 546 HOH HOH B . 
K 5 HOH 147 547 547 HOH HOH B . 
K 5 HOH 148 548 548 HOH HOH B . 
K 5 HOH 149 549 549 HOH HOH B . 
K 5 HOH 150 550 550 HOH HOH B . 
K 5 HOH 151 551 551 HOH HOH B . 
K 5 HOH 152 552 552 HOH HOH B . 
K 5 HOH 153 553 553 HOH HOH B . 
K 5 HOH 154 554 554 HOH HOH B . 
K 5 HOH 155 555 555 HOH HOH B . 
K 5 HOH 156 556 556 HOH HOH B . 
K 5 HOH 157 557 557 HOH HOH B . 
K 5 HOH 158 558 558 HOH HOH B . 
K 5 HOH 159 559 559 HOH HOH B . 
K 5 HOH 160 560 560 HOH HOH B . 
K 5 HOH 161 561 561 HOH HOH B . 
K 5 HOH 162 562 562 HOH HOH B . 
K 5 HOH 163 563 563 HOH HOH B . 
K 5 HOH 164 564 564 HOH HOH B . 
K 5 HOH 165 565 565 HOH HOH B . 
K 5 HOH 166 566 566 HOH HOH B . 
K 5 HOH 167 567 567 HOH HOH B . 
K 5 HOH 168 568 568 HOH HOH B . 
K 5 HOH 169 569 569 HOH HOH B . 
K 5 HOH 170 570 570 HOH HOH B . 
K 5 HOH 171 571 571 HOH HOH B . 
K 5 HOH 172 572 572 HOH HOH B . 
K 5 HOH 173 573 573 HOH HOH B . 
K 5 HOH 174 574 574 HOH HOH B . 
K 5 HOH 175 575 575 HOH HOH B . 
K 5 HOH 176 576 576 HOH HOH B . 
K 5 HOH 177 577 577 HOH HOH B . 
K 5 HOH 178 578 578 HOH HOH B . 
K 5 HOH 179 579 579 HOH HOH B . 
K 5 HOH 180 580 580 HOH HOH B . 
K 5 HOH 181 581 581 HOH HOH B . 
K 5 HOH 182 582 582 HOH HOH B . 
K 5 HOH 183 583 583 HOH HOH B . 
K 5 HOH 184 584 584 HOH HOH B . 
K 5 HOH 185 585 585 HOH HOH B . 
K 5 HOH 186 586 586 HOH HOH B . 
K 5 HOH 187 587 587 HOH HOH B . 
K 5 HOH 188 588 588 HOH HOH B . 
K 5 HOH 189 589 589 HOH HOH B . 
K 5 HOH 190 590 590 HOH HOH B . 
K 5 HOH 191 591 591 HOH HOH B . 
K 5 HOH 192 592 592 HOH HOH B . 
K 5 HOH 193 593 593 HOH HOH B . 
K 5 HOH 194 594 594 HOH HOH B . 
K 5 HOH 195 595 595 HOH HOH B . 
K 5 HOH 196 596 596 HOH HOH B . 
K 5 HOH 197 597 597 HOH HOH B . 
K 5 HOH 198 598 598 HOH HOH B . 
K 5 HOH 199 599 599 HOH HOH B . 
K 5 HOH 200 600 600 HOH HOH B . 
K 5 HOH 201 601 601 HOH HOH B . 
K 5 HOH 202 602 602 HOH HOH B . 
K 5 HOH 203 603 603 HOH HOH B . 
K 5 HOH 204 604 604 HOH HOH B . 
K 5 HOH 205 605 605 HOH HOH B . 
K 5 HOH 206 606 606 HOH HOH B . 
K 5 HOH 207 607 607 HOH HOH B . 
K 5 HOH 208 608 608 HOH HOH B . 
K 5 HOH 209 609 609 HOH HOH B . 
K 5 HOH 210 610 610 HOH HOH B . 
K 5 HOH 211 611 611 HOH HOH B . 
K 5 HOH 212 612 612 HOH HOH B . 
K 5 HOH 213 613 613 HOH HOH B . 
K 5 HOH 214 614 614 HOH HOH B . 
K 5 HOH 215 615 615 HOH HOH B . 
K 5 HOH 216 616 616 HOH HOH B . 
K 5 HOH 217 617 617 HOH HOH B . 
K 5 HOH 218 618 618 HOH HOH B . 
K 5 HOH 219 619 619 HOH HOH B . 
K 5 HOH 220 620 620 HOH HOH B . 
K 5 HOH 221 621 621 HOH HOH B . 
K 5 HOH 222 622 622 HOH HOH B . 
K 5 HOH 223 623 623 HOH HOH B . 
K 5 HOH 224 624 624 HOH HOH B . 
K 5 HOH 225 625 625 HOH HOH B . 
K 5 HOH 226 626 626 HOH HOH B . 
K 5 HOH 227 627 627 HOH HOH B . 
K 5 HOH 228 628 628 HOH HOH B . 
K 5 HOH 229 629 629 HOH HOH B . 
K 5 HOH 230 630 630 HOH HOH B . 
K 5 HOH 231 631 631 HOH HOH B . 
K 5 HOH 232 632 632 HOH HOH B . 
K 5 HOH 233 633 633 HOH HOH B . 
K 5 HOH 234 634 634 HOH HOH B . 
K 5 HOH 235 635 635 HOH HOH B . 
K 5 HOH 236 636 636 HOH HOH B . 
K 5 HOH 237 637 637 HOH HOH B . 
K 5 HOH 238 638 638 HOH HOH B . 
K 5 HOH 239 639 639 HOH HOH B . 
# 
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,J 
2 1 B,G,H,I,K   
# 
_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  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 98  ? A HIS 98  ? 1_555 100.5 ? 
2  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 121 ? A HIS 121 ? 1_555 112.5 ? 
3  NE2 ? A HIS 98  ? A HIS 98  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 121 ? A HIS 121 ? 1_555 98.3  ? 
4  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N4  ? F WWX .   ? A WWX 304 ? 1_555 114.8 ? 
5  NE2 ? A HIS 98  ? A HIS 98  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N4  ? F WWX .   ? A WWX 304 ? 1_555 113.2 ? 
6  ND1 ? A HIS 121 ? A HIS 121 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N4  ? F WWX .   ? A WWX 304 ? 1_555 115.4 ? 
7  NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 98  ? B HIS 98  ? 1_555 102.4 ? 
8  NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 121 ? B HIS 121 ? 1_555 109.1 ? 
9  NE2 ? B HIS 98  ? B HIS 98  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 121 ? B HIS 121 ? 1_555 97.4  ? 
10 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 N4  ? I WWX .   ? B WWX 303 ? 1_555 117.6 ? 
11 NE2 ? B HIS 98  ? B HIS 98  ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 N4  ? I WWX .   ? B WWX 303 ? 1_555 115.4 ? 
12 ND1 ? B HIS 121 ? B HIS 121 ? 1_555 ZN ? G ZN . ? B ZN 301 ? 1_555 N4  ? I WWX .   ? B WWX 303 ? 1_555 112.8 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-04-15 
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_comp_id'  
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
17 3 'Structure model' '_pdbx_struct_conn_angle.value'               
18 3 'Structure model' '_struct_conn.pdbx_dist_value'                
19 3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
20 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
21 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
22 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
23 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
24 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
25 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
26 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
27 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
28 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
29 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
30 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
31 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
32 3 'Structure model' '_struct_ref_seq_dif.details'                 
33 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
34 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
35 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 ASN A 13  ? ? -142.12 12.68   
2  1 ASN A 77  ? ? -97.66  43.45   
3  1 HIS A 105 ? ? -151.41 74.12   
4  1 ASP A 112 ? ? 38.76   61.51   
5  1 ASN A 246 ? ? -151.21 40.34   
6  1 ASN B 13  ? ? -141.20 16.47   
7  1 GLN B 29  ? ? -148.96 57.36   
8  1 SER B 67  ? ? -176.42 -176.88 
9  1 ASP B 74  ? ? -144.00 43.01   
10 1 ASN B 77  ? ? -101.04 46.89   
11 1 HIS B 105 ? ? -157.31 70.39   
12 1 ASN B 246 ? ? -150.59 42.95   
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 ILE A 51 ? ? 11.66  
2 1 LYS B 52 ? ? -11.10 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1 ? A MET 1 
2  1 Y 1 A MET 2 ? A MET 2 
3  1 Y 1 A SER 3 ? A SER 3 
4  1 Y 1 A ARG 4 ? A ARG 4 
5  1 Y 1 A LEU 5 ? A LEU 5 
6  1 Y 1 B MET 1 ? B MET 1 
7  1 Y 1 B MET 2 ? B MET 2 
8  1 Y 1 B SER 3 ? B SER 3 
9  1 Y 1 B ARG 4 ? B ARG 4 
10 1 Y 1 B 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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
VAL N    N  N N 382 
VAL CA   C  N S 383 
VAL C    C  N N 384 
VAL O    O  N N 385 
VAL CB   C  N N 386 
VAL CG1  C  N N 387 
VAL CG2  C  N N 388 
VAL OXT  O  N N 389 
VAL H    H  N N 390 
VAL H2   H  N N 391 
VAL HA   H  N N 392 
VAL HB   H  N N 393 
VAL HG11 H  N N 394 
VAL HG12 H  N N 395 
VAL HG13 H  N N 396 
VAL HG21 H  N N 397 
VAL HG22 H  N N 398 
VAL HG23 H  N N 399 
VAL HXT  H  N N 400 
WWX O16  O  N N 401 
WWX S14  S  N N 402 
WWX O15  O  N N 403 
WWX C18  C  N N 404 
WWX O20  O  N N 405 
WWX C17  C  N N 406 
WWX C8   C  Y N 407 
WWX C7   C  Y N 408 
WWX F12  F  N N 409 
WWX C6   C  Y N 410 
WWX F11  F  N N 411 
WWX C9   C  Y N 412 
WWX C10  C  Y N 413 
WWX F13  F  N N 414 
WWX C5   C  Y N 415 
WWX S1   S  N N 416 
WWX O3   O  N N 417 
WWX N4   N  N N 418 
WWX O2   O  N N 419 
WWX N19  N  N N 420 
WWX C21  C  N R 421 
WWX C30  C  Y N 422 
WWX C35  C  Y N 423 
WWX C34  C  Y N 424 
WWX C33  C  Y N 425 
WWX C32  C  Y N 426 
WWX C31  C  Y N 427 
WWX C22  C  N S 428 
WWX O29  O  N N 429 
WWX C23  C  Y N 430 
WWX C28  C  Y N 431 
WWX C27  C  Y N 432 
WWX C26  C  Y N 433 
WWX C25  C  Y N 434 
WWX C24  C  Y N 435 
WWX H1   H  N N 436 
WWX H2   H  N N 437 
WWX H3   H  N N 438 
WWX H4   H  N N 439 
WWX H5   H  N N 440 
WWX H6   H  N N 441 
WWX H7   H  N N 442 
WWX H8   H  N N 443 
WWX H9   H  N N 444 
WWX H10  H  N N 445 
WWX H11  H  N N 446 
WWX H12  H  N N 447 
WWX H13  H  N N 448 
WWX H14  H  N N 449 
WWX H15  H  N N 450 
WWX H16  H  N N 451 
WWX H17  H  N N 452 
WWX H18  H  N N 453 
WWX H19  H  N N 454 
WWX H20  H  N N 455 
WWX H21  H  N N 456 
ZN  ZN   ZN N N 457 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
WWX O20 C18  sing N N 385 
WWX C18 C17  sing N N 386 
WWX C17 S14  sing N N 387 
WWX C25 C26  doub Y N 388 
WWX C25 C24  sing Y N 389 
WWX C26 C27  sing Y N 390 
WWX C24 C23  doub Y N 391 
WWX C27 C28  doub Y N 392 
WWX C23 C28  sing Y N 393 
WWX C23 C22  sing N N 394 
WWX O29 C22  sing N N 395 
WWX C22 C21  sing N N 396 
WWX O15 S14  doub N N 397 
WWX S14 O16  doub N N 398 
WWX S14 C8   sing N N 399 
WWX F12 C7   sing N N 400 
WWX C8  C7   doub Y N 401 
WWX C8  C9   sing Y N 402 
WWX C7  C6   sing Y N 403 
WWX C21 N19  sing N N 404 
WWX C21 C30  sing N N 405 
WWX N19 C9   sing N N 406 
WWX F11 C6   sing N N 407 
WWX C9  C10  doub Y N 408 
WWX C6  C5   doub Y N 409 
WWX C10 C5   sing Y N 410 
WWX C10 F13  sing N N 411 
WWX C5  S1   sing N N 412 
WWX C30 C31  doub Y N 413 
WWX C30 C35  sing Y N 414 
WWX C31 C32  sing Y N 415 
WWX C35 C34  doub Y N 416 
WWX O3  S1   doub N N 417 
WWX N4  S1   sing N N 418 
WWX S1  O2   doub N N 419 
WWX C32 C33  doub Y N 420 
WWX C34 C33  sing Y N 421 
WWX C18 H1   sing N N 422 
WWX C18 H2   sing N N 423 
WWX O20 H3   sing N N 424 
WWX C17 H4   sing N N 425 
WWX C17 H5   sing N N 426 
WWX N4  H6   sing N N 427 
WWX N4  H7   sing N N 428 
WWX N19 H8   sing N N 429 
WWX C21 H9   sing N N 430 
WWX C35 H10  sing N N 431 
WWX C34 H11  sing N N 432 
WWX C33 H12  sing N N 433 
WWX C32 H13  sing N N 434 
WWX C31 H14  sing N N 435 
WWX C22 H15  sing N N 436 
WWX O29 H16  sing N N 437 
WWX C28 H17  sing N N 438 
WWX C27 H18  sing N N 439 
WWX C26 H19  sing N N 440 
WWX C25 H20  sing N N 441 
WWX C24 H21  sing N N 442 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                                      ZN  
3 1,2-ETHANEDIOL                                                                                                  EDO 
4 '2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' WWX 
5 water                                                                                                           HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2NNO 
_pdbx_initial_refinement_model.details          ? 
# 
