data_4HU1
# 
_entry.id   4HU1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4HU1         pdb_00004hu1 10.2210/pdb4hu1/pdb 
RCSB  RCSB075919   ?            ?                   
WWPDB D_1000075919 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4HT2 . unspecified 
PDB 4HT0 . unspecified 
# 
_pdbx_database_status.entry_id                        4HU1 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2012-11-02 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'4-Substituted-2,3,5,6-tetrafluorobenzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, XII, and XIII.' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            21 
_citation.page_first                2093 
_citation.page_last                 2106 
_citation.year                      2013 
_citation.journal_id_ASTM           BMECEP 
_citation.country                   UK 
_citation.journal_id_ISSN           0968-0896 
_citation.journal_id_CSD            1200 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23394791 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2013.01.008 
# 
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 'Gylyte, J.'    4 ? 
primary 'Timm, D.'      5 ? 
primary 'Manakova, E.'  6 ? 
primary 'Grazulis, S.'  7 ? 
primary 'Matulis, D.'   8 ? 
# 
_cell.entry_id           4HU1 
_cell.length_a           56.270 
_cell.length_b           57.386 
_cell.length_c           159.552 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              8 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4HU1 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.Int_Tables_number                19 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 13'                                              29613.318 2   4.2.1.1 ? 
'human carbonic anhydrase XIII' ? 
2 non-polymer syn 'ZINC ION'                                                           65.409    2   ?       ? ? ? 
3 non-polymer syn '2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 337.268   2   ?       ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                       62.068    7   ?       ? ? ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                              106.120   1   ?       ? ? ? 
6 water       nat water                                                                18.015    553 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XIII, Carbonic anhydrase XIII, CA-XIII' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   MET n 
1 3   SER n 
1 4   ARG n 
1 5   LEU n 
1 6   SER n 
1 7   TRP n 
1 8   GLY n 
1 9   TYR n 
1 10  ARG n 
1 11  GLU n 
1 12  HIS n 
1 13  ASN n 
1 14  GLY n 
1 15  PRO n 
1 16  ILE n 
1 17  HIS n 
1 18  TRP n 
1 19  LYS n 
1 20  GLU n 
1 21  PHE n 
1 22  PHE n 
1 23  PRO n 
1 24  ILE n 
1 25  ALA n 
1 26  ASP n 
1 27  GLY n 
1 28  ASP n 
1 29  GLN n 
1 30  GLN n 
1 31  SER n 
1 32  PRO n 
1 33  ILE n 
1 34  GLU n 
1 35  ILE n 
1 36  LYS n 
1 37  THR n 
1 38  LYS n 
1 39  GLU n 
1 40  VAL n 
1 41  LYS n 
1 42  TYR n 
1 43  ASP n 
1 44  SER n 
1 45  SER n 
1 46  LEU n 
1 47  ARG n 
1 48  PRO n 
1 49  LEU n 
1 50  SER n 
1 51  ILE n 
1 52  LYS n 
1 53  TYR n 
1 54  ASP n 
1 55  PRO n 
1 56  SER n 
1 57  SER n 
1 58  ALA n 
1 59  LYS n 
1 60  ILE n 
1 61  ILE n 
1 62  SER n 
1 63  ASN n 
1 64  SER n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  PHE n 
1 69  ASN n 
1 70  VAL n 
1 71  ASP n 
1 72  PHE n 
1 73  ASP n 
1 74  ASP n 
1 75  THR n 
1 76  GLU n 
1 77  ASN n 
1 78  LYS n 
1 79  SER n 
1 80  VAL n 
1 81  LEU n 
1 82  ARG n 
1 83  GLY n 
1 84  GLY n 
1 85  PRO n 
1 86  LEU n 
1 87  THR n 
1 88  GLY n 
1 89  SER n 
1 90  TYR n 
1 91  ARG n 
1 92  LEU n 
1 93  ARG n 
1 94  GLN n 
1 95  VAL n 
1 96  HIS n 
1 97  LEU n 
1 98  HIS n 
1 99  TRP n 
1 100 GLY n 
1 101 SER n 
1 102 ALA n 
1 103 ASP n 
1 104 ASP n 
1 105 HIS n 
1 106 GLY n 
1 107 SER n 
1 108 GLU n 
1 109 HIS n 
1 110 ILE n 
1 111 VAL n 
1 112 ASP n 
1 113 GLY n 
1 114 VAL n 
1 115 SER n 
1 116 TYR n 
1 117 ALA n 
1 118 ALA n 
1 119 GLU n 
1 120 LEU n 
1 121 HIS n 
1 122 VAL n 
1 123 VAL n 
1 124 HIS n 
1 125 TRP n 
1 126 ASN n 
1 127 SER n 
1 128 ASP n 
1 129 LYS n 
1 130 TYR n 
1 131 PRO n 
1 132 SER n 
1 133 PHE n 
1 134 VAL n 
1 135 GLU n 
1 136 ALA n 
1 137 ALA n 
1 138 HIS n 
1 139 GLU n 
1 140 PRO n 
1 141 ASP n 
1 142 GLY n 
1 143 LEU n 
1 144 ALA n 
1 145 VAL n 
1 146 LEU n 
1 147 GLY n 
1 148 VAL n 
1 149 PHE n 
1 150 LEU n 
1 151 GLN n 
1 152 ILE n 
1 153 GLY n 
1 154 GLU n 
1 155 PRO n 
1 156 ASN n 
1 157 SER n 
1 158 GLN n 
1 159 LEU n 
1 160 GLN n 
1 161 LYS n 
1 162 ILE n 
1 163 THR n 
1 164 ASP n 
1 165 THR n 
1 166 LEU n 
1 167 ASP n 
1 168 SER n 
1 169 ILE n 
1 170 LYS n 
1 171 GLU n 
1 172 LYS n 
1 173 GLY n 
1 174 LYS n 
1 175 GLN n 
1 176 THR n 
1 177 ARG n 
1 178 PHE n 
1 179 THR n 
1 180 ASN n 
1 181 PHE n 
1 182 ASP n 
1 183 LEU n 
1 184 LEU n 
1 185 SER n 
1 186 LEU n 
1 187 LEU n 
1 188 PRO n 
1 189 PRO n 
1 190 SER n 
1 191 TRP n 
1 192 ASP n 
1 193 TYR n 
1 194 TRP n 
1 195 THR n 
1 196 TYR n 
1 197 PRO n 
1 198 GLY n 
1 199 SER n 
1 200 LEU n 
1 201 THR n 
1 202 VAL n 
1 203 PRO n 
1 204 PRO n 
1 205 LEU n 
1 206 LEU n 
1 207 GLU n 
1 208 SER n 
1 209 VAL n 
1 210 THR n 
1 211 TRP n 
1 212 ILE n 
1 213 VAL n 
1 214 LEU n 
1 215 LYS n 
1 216 GLN n 
1 217 PRO n 
1 218 ILE n 
1 219 ASN n 
1 220 ILE n 
1 221 SER n 
1 222 SER n 
1 223 GLN n 
1 224 GLN n 
1 225 LEU n 
1 226 ALA n 
1 227 LYS n 
1 228 PHE n 
1 229 ARG n 
1 230 SER n 
1 231 LEU n 
1 232 LEU n 
1 233 CYS n 
1 234 THR n 
1 235 ALA n 
1 236 GLU n 
1 237 GLY n 
1 238 GLU n 
1 239 ALA n 
1 240 ALA n 
1 241 ALA n 
1 242 PHE n 
1 243 LEU n 
1 244 VAL n 
1 245 SER n 
1 246 ASN n 
1 247 HIS n 
1 248 ARG n 
1 249 PRO n 
1 250 PRO n 
1 251 GLN n 
1 252 PRO n 
1 253 LEU n 
1 254 LYS n 
1 255 GLY n 
1 256 ARG n 
1 257 LYS n 
1 258 VAL n 
1 259 ARG n 
1 260 ALA n 
1 261 SER n 
1 262 PHE n 
1 263 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA13 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH13_HUMAN 
_struct_ref.pdbx_db_accession          Q8N1Q1 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSVL
RGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQK
ITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAAA
FLVSNHRPPQPLKGRKVRASFH
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 4HU1 B 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
2 1 4HU1 A 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4HU1 MET B 1 ? UNP Q8N1Q1 ? ? 'expression tag' 1 1 
2 4HU1 MET A 1 ? UNP Q8N1Q1 ? ? 'expression tag' 1 2 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                              ?                 'C3 H7 N O2' 
89.093  
ARG 'L-peptide linking' y ARGININE                                                             ?                 'C6 H15 N4 O2 1' 
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                           ?                 'C4 H8 N2 O3' 
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                      ?                 'C4 H7 N O4' 
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                             ?                 'C3 H7 N O2 S' 
121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                                       'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 
GLN 'L-peptide linking' y GLUTAMINE                                                            ?                 'C5 H10 N2 O3' 
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                      ?                 'C5 H9 N O4' 
147.129 
GLY 'peptide linking'   y GLYCINE                                                              ?                 'C2 H5 N O2' 
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                            ?                 'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                                                ?                 'H2 O' 18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                           ?                 'C6 H13 N O2' 
131.173 
LEU 'L-peptide linking' y LEUCINE                                                              ?                 'C6 H13 N O2' 
131.173 
LYS 'L-peptide linking' y LYSINE                                                               ?                 'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking' y METHIONINE                                                           ?                 'C5 H11 N O2 S' 
149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                              ?                 'C4 H10 O3' 
106.120 
PHE 'L-peptide linking' y PHENYLALANINE                                                        ?                 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                              ?                 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                               ?                 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                            ?                 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                           ?                 'C11 H12 N2 O2' 
204.225 
TYR 'L-peptide linking' y TYROSINE                                                             ?                 'C9 H11 N O3' 
181.189 
V13 non-polymer         . '2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ?                 
'C8 H7 F4 N O5 S2' 337.268 
VAL 'L-peptide linking' y VALINE                                                               ?                 'C5 H11 N O2' 
117.146 
ZN  non-polymer         . 'ZINC ION'                                                           ?                 'Zn 2' 65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4HU1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   43.7 
_exptl_crystal.density_Matthews      2.2 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    
'0.1M sodium citrate pH5.5, 0.1M sodium acetate pH4.5 and 26% of PEG4000  , VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'FLAT PANEL' 
_diffrn_detector.type                   'MAR555 flatpanel detector' 
_diffrn_detector.pdbx_collection_date   2011-11-15 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Double crystal Si(111), horizontally focussing' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.815 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X11' 
_diffrn_source.pdbx_wavelength_list        0.815 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X11 
# 
_reflns.entry_id                     4HU1 
_reflns.d_resolution_high            1.950 
_reflns.d_resolution_low             40.178 
_reflns.number_all                   38614 
_reflns.number_obs                   38614 
_reflns.pdbx_netI_over_sigmaI        9.000 
_reflns.pdbx_Rsym_value              0.135 
_reflns.pdbx_redundancy              7.300 
_reflns.percent_possible_obs         100.000 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.pdbx_Rmerge_I_obs            0.135 
_reflns.B_iso_Wilson_estimate        21.6 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.95 2.06   ? 41262 ? 0.486 1.5 0.486 ? 7.40 ? 5561 100.00 1  1 
2.06 2.18   ? 38888 ? 0.356 2.0 0.356 ? 7.40 ? 5242 100.00 2  1 
2.18 2.33   ? 36589 ? 0.280 2.5 0.280 ? 7.40 ? 4933 100.00 3  1 
2.33 2.52   ? 34398 ? 0.222 3.2 0.222 ? 7.40 ? 4641 100.00 4  1 
2.52 2.76   ? 31471 ? 0.176 3.9 0.176 ? 7.40 ? 4258 100.00 5  1 
2.76 3.08   ? 28701 ? 0.130 5.0 0.130 ? 7.40 ? 3891 100.00 6  1 
3.08 3.56   ? 25200 ? 0.099 6.1 0.099 ? 7.30 ? 3439 100.00 7  1 
3.56 4.36   ? 21461 ? 0.086 6.8 0.086 ? 7.30 ? 2956 100.00 8  1 
4.36 6.17   ? 16538 ? 0.080 7.0 0.080 ? 7.10 ? 2326 100.00 9  1 
6.17 40.178 ? 8572  ? 0.088 5.6 0.088 ? 6.30 ? 1367 99.50  10 1 
# 
_refine.entry_id                                 4HU1 
_refine.ls_d_res_high                            1.950 
_refine.ls_d_res_low                             40.1780 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.950 
_refine.ls_number_reflns_obs                     38534 
_refine.ls_number_reflns_all                     34654 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          0.175 
_refine.ls_R_factor_obs                          0.175 
_refine.ls_R_factor_R_work                       0.169 
_refine.ls_wR_factor_R_work                      0.166 
_refine.ls_R_factor_R_free                       0.235 
_refine.ls_wR_factor_R_free                      0.232 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  3880 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.689 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.030 
_refine.aniso_B[2][2]                            0.780 
_refine.aniso_B[3][3]                            -0.820 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.916 
_refine.overall_SU_R_Cruickshank_DPI             0.192 
_refine.overall_SU_R_free                        0.177 
_refine.pdbx_overall_ESU_R                       0.192 
_refine.pdbx_overall_ESU_R_Free                  0.177 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.851 
_refine.B_iso_max                                52.37 
_refine.B_iso_min                                5.74 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB ENTRY 2NNO' 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4135 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         77 
_refine_hist.number_atoms_solvent             553 
_refine_hist.number_atoms_total               4765 
_refine_hist.d_res_high                       1.950 
_refine_hist.d_res_low                        40.1780 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d         4409 0.024  0.021  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      6008 2.026  1.960  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   534  7.021  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   202  33.370 24.010 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   703  14.271 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   22   16.640 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr           634  0.143  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     3442 0.010  0.020  ? ? 'X-RAY DIFFRACTION' 
r_nbd_refined            2233 0.206  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          2914 0.310  0.200  ? ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    506  0.163  0.200  ? ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      6    0.162  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   80   0.226  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 49   0.174  0.200  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_it              2650 1.187  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcangle_it             4310 1.910  2.000  ? ? 'X-RAY DIFFRACTION' 
r_scbond_it              1759 2.966  3.000  ? ? 'X-RAY DIFFRACTION' 
r_scangle_it             1698 4.129  4.500  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.950 
_refine_ls_shell.d_res_low                        2.001 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               99.930 
_refine_ls_shell.number_reflns_R_work             2527 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.213 
_refine_ls_shell.R_factor_R_free                  0.309 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             267 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                2794 
_refine_ls_shell.number_reflns_obs                27176 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4HU1 
_struct.title                     'Crystal structure of human carbonic anhydrase isozyme XIII with the inhibitor.' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4HU1 
_struct_keywords.text            
;drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, carbonate dehydratase activity, carbon-oxygen lyase activity
;
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 2 ? 
H N N 3 ? 
I N N 5 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 6 ? 
P N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  GLY A 14  ? ILE A 16  ? GLY B 14  ILE B 16  5 ? 3  
HELX_P HELX_P2  2  HIS A 17  ? PHE A 22  ? HIS B 17  PHE B 22  1 ? 6  
HELX_P HELX_P3  3  PRO A 23  ? GLY A 27  ? PRO B 23  GLY B 27  5 ? 5  
HELX_P HELX_P4  4  LYS A 36  ? VAL A 40  ? LYS B 36  VAL B 40  5 ? 5  
HELX_P HELX_P5  5  ASP A 54  ? SER A 56  ? ASP B 54  SER B 56  5 ? 3  
HELX_P HELX_P6  6  SER A 132 ? ALA A 137 ? SER B 132 ALA B 137 1 ? 6  
HELX_P HELX_P7  7  ASN A 156 ? GLN A 158 ? ASN B 156 GLN B 158 5 ? 3  
HELX_P HELX_P8  8  LEU A 159 ? ASP A 164 ? LEU B 159 ASP B 164 1 ? 6  
HELX_P HELX_P9  9  LEU A 183 ? LEU A 187 ? LEU B 183 LEU B 187 5 ? 5  
HELX_P HELX_P10 10 SER A 221 ? ARG A 229 ? SER B 221 ARG B 229 1 ? 9  
HELX_P HELX_P11 11 GLY B 14  ? PHE B 21  ? GLY A 14  PHE A 21  5 ? 8  
HELX_P HELX_P12 12 PHE B 22  ? GLY B 27  ? PHE A 22  GLY A 27  5 ? 6  
HELX_P HELX_P13 13 LYS B 36  ? VAL B 40  ? LYS A 36  VAL A 40  5 ? 5  
HELX_P HELX_P14 14 SER B 132 ? ALA B 137 ? SER A 132 ALA A 137 1 ? 6  
HELX_P HELX_P15 15 ASN B 156 ? ASP B 164 ? ASN A 156 ASP A 164 1 ? 9  
HELX_P HELX_P16 16 THR B 165 ? LYS B 170 ? THR A 165 LYS A 170 5 ? 6  
HELX_P HELX_P17 17 ASP B 182 ? LEU B 187 ? ASP A 182 LEU A 187 1 ? 6  
HELX_P HELX_P18 18 SER B 221 ? SER B 230 ? SER A 221 SER A 230 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 1.943 ? ? 
metalc2 metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 98  B ZN  301 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
metalc3 metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 121 B ZN  301 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc4 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D V13 . N10 ? ? B ZN  301 B V13 302 1_555 ? ? ? ? ? ? ? 1.908 ? ? 
metalc5 metalc ? ? B HIS 96  NE2 ? ? ? 1_555 G ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 1.853 ? ? 
metalc6 metalc ? ? B HIS 98  NE2 ? ? ? 1_555 G ZN  . ZN  ? ? A HIS 98  A ZN  301 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc7 metalc ? ? B HIS 121 ND1 ? ? ? 1_555 G ZN  . ZN  ? ? A HIS 121 A ZN  301 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
metalc8 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 H V13 . N10 ? ? A ZN  301 A V13 302 1_555 ? ? ? ? ? ? ? 1.788 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 31  A . ? SER 31  B PRO 32  A ? PRO 32  B 1 -4.30 
2 PRO 203 A . ? PRO 203 B PRO 204 A ? PRO 204 B 1 5.03  
3 SER 31  B . ? SER 31  A PRO 32  B ? PRO 32  A 1 4.47  
4 PRO 203 B . ? PRO 203 A PRO 204 B ? PRO 204 A 1 10.23 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
D ? 2  ? 
E ? 10 ? 
F ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
D 1 2  ? parallel      
E 1 2  ? parallel      
E 2 3  ? anti-parallel 
E 3 4  ? anti-parallel 
E 4 5  ? parallel      
E 5 6  ? anti-parallel 
E 6 7  ? anti-parallel 
E 7 8  ? anti-parallel 
E 8 9  ? anti-parallel 
E 9 10 ? anti-parallel 
F 1 2  ? anti-parallel 
F 2 3  ? anti-parallel 
F 3 4  ? anti-parallel 
F 4 5  ? anti-parallel 
F 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  GLU A 34  ? ILE A 35  ? GLU B 34  ILE B 35  
A 2  ILE A 110 ? VAL A 111 ? ILE B 110 VAL B 111 
B 1  LYS A 41  ? TYR A 42  ? LYS B 41  TYR B 42  
B 2  ARG A 259 ? ALA A 260 ? ARG B 259 ALA B 260 
B 3  TYR A 193 ? GLY A 198 ? TYR B 193 GLY B 198 
B 4  VAL A 209 ? LEU A 214 ? VAL B 209 LEU B 214 
B 5  LEU A 143 ? ILE A 152 ? LEU B 143 ILE B 152 
B 6  ALA A 118 ? ASN A 126 ? ALA B 118 ASN B 126 
B 7  TYR A 90  ? TRP A 99  ? TYR B 90  TRP B 99  
B 8  PHE A 68  ? PHE A 72  ? PHE B 68  PHE B 72  
B 9  ALA A 58  ? ASN A 63  ? ALA B 58  ASN B 63  
B 10 GLN A 175 ? ARG A 177 ? GLN B 175 ARG B 177 
C 1  ARG A 47  ? LYS A 52  ? ARG B 47  LYS B 52  
C 2  VAL A 80  ? GLY A 84  ? VAL B 80  GLY B 84  
C 3  TYR A 90  ? TRP A 99  ? TYR B 90  TRP B 99  
C 4  ALA A 118 ? ASN A 126 ? ALA B 118 ASN B 126 
C 5  LEU A 143 ? ILE A 152 ? LEU B 143 ILE B 152 
C 6  ILE A 218 ? ILE A 220 ? ILE B 218 ILE B 220 
D 1  GLU B 34  ? ILE B 35  ? GLU A 34  ILE A 35  
D 2  ILE B 110 ? VAL B 111 ? ILE A 110 VAL A 111 
E 1  LYS B 41  ? TYR B 42  ? LYS A 41  TYR A 42  
E 2  ARG B 259 ? ALA B 260 ? ARG A 259 ALA A 260 
E 3  TYR B 193 ? GLY B 198 ? TYR A 193 GLY A 198 
E 4  VAL B 209 ? LEU B 214 ? VAL A 209 LEU A 214 
E 5  LEU B 143 ? ILE B 152 ? LEU A 143 ILE A 152 
E 6  ALA B 118 ? ASN B 126 ? ALA A 118 ASN A 126 
E 7  TYR B 90  ? TRP B 99  ? TYR A 90  TRP A 99  
E 8  PHE B 68  ? PHE B 72  ? PHE A 68  PHE A 72  
E 9  ALA B 58  ? ASN B 63  ? ALA A 58  ASN A 63  
E 10 GLN B 175 ? ARG B 177 ? GLN A 175 ARG A 177 
F 1  LEU B 49  ? LYS B 52  ? LEU A 49  LYS A 52  
F 2  VAL B 80  ? GLY B 83  ? VAL A 80  GLY A 83  
F 3  TYR B 90  ? TRP B 99  ? TYR A 90  TRP A 99  
F 4  ALA B 118 ? ASN B 126 ? ALA A 118 ASN A 126 
F 5  LEU B 143 ? ILE B 152 ? LEU A 143 ILE A 152 
F 6  ILE B 218 ? ILE B 220 ? ILE A 218 ILE A 220 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 35  ? N ILE B 35  O ILE A 110 ? O ILE B 110 
B 1 2  N LYS A 41  ? N LYS B 41  O ALA A 260 ? O ALA B 260 
B 2 3  O ARG A 259 ? O ARG B 259 N THR A 195 ? N THR B 195 
B 3 4  N GLY A 198 ? N GLY B 198 O VAL A 209 ? O VAL B 209 
B 4 5  O LEU A 214 ? O LEU B 214 N GLY A 147 ? N GLY B 147 
B 5 6  O VAL A 148 ? O VAL B 148 N LEU A 120 ? N LEU B 120 
B 6 7  O VAL A 123 ? O VAL B 123 N ARG A 93  ? N ARG B 93  
B 7 8  O VAL A 95  ? O VAL B 95  N VAL A 70  ? N VAL B 70  
B 8 9  O ASP A 71  ? O ASP B 71  N LYS A 59  ? N LYS B 59  
B 9 10 N ILE A 61  ? N ILE B 61  O THR A 176 ? O THR B 176 
C 1 2  N SER A 50  ? N SER B 50  O ARG A 82  ? O ARG B 82  
C 2 3  N LEU A 81  ? N LEU B 81  O TYR A 90  ? O TYR B 90  
C 3 4  N ARG A 93  ? N ARG B 93  O VAL A 123 ? O VAL B 123 
C 4 5  N LEU A 120 ? N LEU B 120 O VAL A 148 ? O VAL B 148 
C 5 6  N PHE A 149 ? N PHE B 149 O ILE A 218 ? O ILE B 218 
D 1 2  N ILE B 35  ? N ILE A 35  O ILE B 110 ? O ILE A 110 
E 1 2  N LYS B 41  ? N LYS A 41  O ALA B 260 ? O ALA A 260 
E 2 3  O ARG B 259 ? O ARG A 259 N THR B 195 ? N THR A 195 
E 3 4  N GLY B 198 ? N GLY A 198 O VAL B 209 ? O VAL A 209 
E 4 5  O ILE B 212 ? O ILE A 212 N GLY B 147 ? N GLY A 147 
E 5 6  O VAL B 148 ? O VAL A 148 N LEU B 120 ? N LEU A 120 
E 6 7  O TRP B 125 ? O TRP A 125 N ARG B 91  ? N ARG A 91  
E 7 8  O VAL B 95  ? O VAL A 95  N VAL B 70  ? N VAL A 70  
E 8 9  O ASP B 71  ? O ASP A 71  N LYS B 59  ? N LYS A 59  
E 9 10 N ILE B 61  ? N ILE A 61  O THR B 176 ? O THR A 176 
F 1 2  N SER B 50  ? N SER A 50  O ARG B 82  ? O ARG A 82  
F 2 3  N LEU B 81  ? N LEU A 81  O TYR B 90  ? O TYR A 90  
F 3 4  N ARG B 91  ? N ARG A 91  O TRP B 125 ? O TRP A 125 
F 4 5  N LEU B 120 ? N LEU A 120 O VAL B 148 ? O VAL A 148 
F 5 6  N GLN B 151 ? N GLN A 151 O ILE B 218 ? O ILE A 218 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software B ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN B 301'  
AC2 Software B V13 302 ? 13 'BINDING SITE FOR RESIDUE V13 B 302' 
AC3 Software B EDO 303 ? 5  'BINDING SITE FOR RESIDUE EDO B 303' 
AC4 Software B EDO 304 ? 4  'BINDING SITE FOR RESIDUE EDO B 304' 
AC5 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC6 Software A V13 302 ? 15 'BINDING SITE FOR RESIDUE V13 A 302' 
AC7 Software A PEG 303 ? 8  'BINDING SITE FOR RESIDUE PEG A 303' 
AC8 Software A EDO 304 ? 3  'BINDING SITE FOR RESIDUE EDO A 304' 
AC9 Software A EDO 305 ? 6  'BINDING SITE FOR RESIDUE EDO A 305' 
BC1 Software A EDO 306 ? 2  'BINDING SITE FOR RESIDUE EDO A 306' 
BC2 Software A EDO 307 ? 7  'BINDING SITE FOR RESIDUE EDO A 307' 
BC3 Software A EDO 308 ? 5  'BINDING SITE FOR RESIDUE EDO A 308' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 96  ? HIS B 96  . ? 1_555 ? 
2  AC1 4  HIS A 98  ? HIS B 98  . ? 1_555 ? 
3  AC1 4  HIS A 121 ? HIS B 121 . ? 1_555 ? 
4  AC1 4  V13 D .   ? V13 B 302 . ? 1_555 ? 
5  AC2 13 GLN A 94  ? GLN B 94  . ? 1_555 ? 
6  AC2 13 HIS A 96  ? HIS B 96  . ? 1_555 ? 
7  AC2 13 HIS A 98  ? HIS B 98  . ? 1_555 ? 
8  AC2 13 HIS A 121 ? HIS B 121 . ? 1_555 ? 
9  AC2 13 VAL A 123 ? VAL B 123 . ? 1_555 ? 
10 AC2 13 PHE A 133 ? PHE B 133 . ? 1_555 ? 
11 AC2 13 VAL A 145 ? VAL B 145 . ? 1_555 ? 
12 AC2 13 LEU A 200 ? LEU B 200 . ? 1_555 ? 
13 AC2 13 THR A 201 ? THR B 201 . ? 1_555 ? 
14 AC2 13 VAL A 202 ? VAL B 202 . ? 1_555 ? 
15 AC2 13 ZN  C .   ? ZN  B 301 . ? 1_555 ? 
16 AC2 13 HOH O .   ? HOH B 475 . ? 1_555 ? 
17 AC2 13 HOH O .   ? HOH B 542 . ? 1_555 ? 
18 AC3 5  GLY A 100 ? GLY B 100 . ? 1_555 ? 
19 AC3 5  SER A 101 ? SER B 101 . ? 1_555 ? 
20 AC3 5  HIS A 105 ? HIS B 105 . ? 1_555 ? 
21 AC3 5  SER A 245 ? SER B 245 . ? 1_555 ? 
22 AC3 5  HIS A 247 ? HIS B 247 . ? 1_555 ? 
23 AC4 4  ARG A 10  ? ARG B 10  . ? 1_555 ? 
24 AC4 4  GLU A 11  ? GLU B 11  . ? 1_555 ? 
25 AC4 4  HIS A 12  ? HIS B 12  . ? 1_555 ? 
26 AC4 4  ASN A 13  ? ASN B 13  . ? 1_555 ? 
27 AC5 4  HIS B 96  ? HIS A 96  . ? 1_555 ? 
28 AC5 4  HIS B 98  ? HIS A 98  . ? 1_555 ? 
29 AC5 4  HIS B 121 ? HIS A 121 . ? 1_555 ? 
30 AC5 4  V13 H .   ? V13 A 302 . ? 1_555 ? 
31 AC6 15 GLN B 94  ? GLN A 94  . ? 1_555 ? 
32 AC6 15 HIS B 96  ? HIS A 96  . ? 1_555 ? 
33 AC6 15 HIS B 98  ? HIS A 98  . ? 1_555 ? 
34 AC6 15 HIS B 121 ? HIS A 121 . ? 1_555 ? 
35 AC6 15 VAL B 123 ? VAL A 123 . ? 1_555 ? 
36 AC6 15 PHE B 133 ? PHE A 133 . ? 1_555 ? 
37 AC6 15 VAL B 145 ? VAL A 145 . ? 1_555 ? 
38 AC6 15 LEU B 200 ? LEU A 200 . ? 1_555 ? 
39 AC6 15 THR B 201 ? THR A 201 . ? 1_555 ? 
40 AC6 15 VAL B 202 ? VAL A 202 . ? 1_555 ? 
41 AC6 15 TRP B 211 ? TRP A 211 . ? 1_555 ? 
42 AC6 15 ZN  G .   ? ZN  A 301 . ? 1_555 ? 
43 AC6 15 HOH P .   ? HOH A 464 . ? 1_555 ? 
44 AC6 15 HOH P .   ? HOH A 542 . ? 1_555 ? 
45 AC6 15 HOH P .   ? HOH A 593 . ? 1_555 ? 
46 AC7 8  LYS B 59  ? LYS A 59  . ? 1_555 ? 
47 AC7 8  ILE B 60  ? ILE A 60  . ? 1_555 ? 
48 AC7 8  ARG B 177 ? ARG A 177 . ? 1_555 ? 
49 AC7 8  ASP A 28  ? ASP B 28  . ? 1_565 ? 
50 AC7 8  GLN A 29  ? GLN B 29  . ? 1_565 ? 
51 AC7 8  LEU A 253 ? LEU B 253 . ? 1_565 ? 
52 AC7 8  LYS A 254 ? LYS B 254 . ? 1_565 ? 
53 AC7 8  ARG A 256 ? ARG B 256 . ? 1_565 ? 
54 AC8 3  PRO B 189 ? PRO A 189 . ? 1_555 ? 
55 AC8 3  SER B 190 ? SER A 190 . ? 1_555 ? 
56 AC8 3  ARG A 82  ? ARG B 82  . ? 1_555 ? 
57 AC9 6  LYS B 38  ? LYS A 38  . ? 4_445 ? 
58 AC9 6  GLN B 160 ? GLN A 160 . ? 1_555 ? 
59 AC9 6  GLN B 223 ? GLN A 223 . ? 1_555 ? 
60 AC9 6  LYS B 227 ? LYS A 227 . ? 1_555 ? 
61 AC9 6  HOH P .   ? HOH A 425 . ? 4_445 ? 
62 AC9 6  HOH P .   ? HOH A 645 . ? 1_555 ? 
63 BC1 2  ASP B 54  ? ASP A 54  . ? 1_555 ? 
64 BC1 2  SER B 56  ? SER A 56  . ? 1_555 ? 
65 BC2 7  GLY B 100 ? GLY A 100 . ? 1_555 ? 
66 BC2 7  SER B 101 ? SER A 101 . ? 1_555 ? 
67 BC2 7  HIS B 105 ? HIS A 105 . ? 1_555 ? 
68 BC2 7  SER B 245 ? SER A 245 . ? 1_555 ? 
69 BC2 7  HIS B 247 ? HIS A 247 . ? 1_555 ? 
70 BC2 7  HOH P .   ? HOH A 414 . ? 1_555 ? 
71 BC2 7  HOH P .   ? HOH A 693 . ? 1_555 ? 
72 BC3 5  ASP B 103 ? ASP A 103 . ? 1_555 ? 
73 BC3 5  ILE B 152 ? ILE A 152 . ? 1_555 ? 
74 BC3 5  THR A 75  ? THR B 75  . ? 4_545 ? 
75 BC3 5  HOH O .   ? HOH B 638 . ? 4_545 ? 
76 BC3 5  HOH O .   ? HOH B 639 . ? 4_545 ? 
# 
_atom_sites.entry_id                    4HU1 
_atom_sites.fract_transf_matrix[1][1]   0.017771 
_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]   0.017426 
_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]   0.006268 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ARG A 1 4   ? -49.300 -46.398 22.982  1.00 42.61 ? 4   ARG B N   1 
ATOM   2    C  CA  . ARG A 1 4   ? -50.137 -45.668 24.003  1.00 42.31 ? 4   ARG B CA  1 
ATOM   3    C  C   . ARG A 1 4   ? -49.818 -44.165 24.102  1.00 42.58 ? 4   ARG B C   1 
ATOM   4    O  O   . ARG A 1 4   ? -48.646 -43.722 24.198  1.00 42.99 ? 4   ARG B O   1 
ATOM   5    C  CB  . ARG A 1 4   ? -50.181 -46.344 25.385  1.00 42.78 ? 4   ARG B CB  1 
ATOM   6    C  CG  . ARG A 1 4   ? -48.993 -46.066 26.339  1.00 42.46 ? 4   ARG B CG  1 
ATOM   7    C  CD  . ARG A 1 4   ? -49.450 -45.655 27.794  1.00 47.06 ? 4   ARG B CD  1 
ATOM   8    N  NE  . ARG A 1 4   ? -49.621 -46.700 28.850  1.00 46.82 ? 4   ARG B NE  1 
ATOM   9    C  CZ  . ARG A 1 4   ? -48.667 -47.174 29.682  1.00 44.86 ? 4   ARG B CZ  1 
ATOM   10   N  NH1 . ARG A 1 4   ? -47.373 -46.763 29.624  1.00 34.60 ? 4   ARG B NH1 1 
ATOM   11   N  NH2 . ARG A 1 4   ? -49.023 -48.105 30.582  1.00 42.47 ? 4   ARG B NH2 1 
ATOM   12   N  N   . LEU A 1 5   ? -50.886 -43.383 24.076  1.00 41.03 ? 5   LEU B N   1 
ATOM   13   C  CA  . LEU A 1 5   ? -50.779 -41.935 24.117  1.00 40.83 ? 5   LEU B CA  1 
ATOM   14   C  C   . LEU A 1 5   ? -50.704 -41.389 25.574  1.00 39.32 ? 5   LEU B C   1 
ATOM   15   O  O   . LEU A 1 5   ? -50.576 -40.151 25.795  1.00 41.51 ? 5   LEU B O   1 
ATOM   16   C  CB  . LEU A 1 5   ? -51.945 -41.318 23.330  1.00 41.03 ? 5   LEU B CB  1 
ATOM   17   C  CG  . LEU A 1 5   ? -51.854 -41.384 21.788  1.00 43.57 ? 5   LEU B CG  1 
ATOM   18   C  CD1 . LEU A 1 5   ? -53.253 -41.362 21.104  1.00 45.77 ? 5   LEU B CD1 1 
ATOM   19   C  CD2 . LEU A 1 5   ? -51.004 -40.219 21.283  1.00 45.83 ? 5   LEU B CD2 1 
ATOM   20   N  N   . SER A 1 6   ? -50.736 -42.304 26.546  1.00 35.60 ? 6   SER B N   1 
ATOM   21   C  CA  . SER A 1 6   ? -50.754 -41.935 27.965  1.00 33.03 ? 6   SER B CA  1 
ATOM   22   C  C   . SER A 1 6   ? -49.535 -42.458 28.737  1.00 29.18 ? 6   SER B C   1 
ATOM   23   O  O   . SER A 1 6   ? -49.660 -42.818 29.872  1.00 29.65 ? 6   SER B O   1 
ATOM   24   C  CB  . SER A 1 6   ? -52.038 -42.461 28.631  1.00 33.96 ? 6   SER B CB  1 
ATOM   25   O  OG  . SER A 1 6   ? -51.969 -43.877 28.812  1.00 34.65 ? 6   SER B OG  1 
ATOM   26   N  N   . TRP A 1 7   ? -48.366 -42.521 28.112  1.00 24.04 ? 7   TRP B N   1 
ATOM   27   C  CA  . TRP A 1 7   ? -47.156 -42.859 28.832  1.00 21.07 ? 7   TRP B CA  1 
ATOM   28   C  C   . TRP A 1 7   ? -46.769 -41.647 29.721  1.00 18.85 ? 7   TRP B C   1 
ATOM   29   O  O   . TRP A 1 7   ? -47.155 -40.531 29.452  1.00 19.98 ? 7   TRP B O   1 
ATOM   30   C  CB  . TRP A 1 7   ? -46.061 -43.226 27.842  1.00 19.13 ? 7   TRP B CB  1 
ATOM   31   C  CG  . TRP A 1 7   ? -45.606 -42.018 27.049  1.00 16.75 ? 7   TRP B CG  1 
ATOM   32   C  CD1 . TRP A 1 7   ? -46.061 -41.590 25.799  1.00 17.73 ? 7   TRP B CD1 1 
ATOM   33   C  CD2 . TRP A 1 7   ? -44.619 -41.075 27.470  1.00 16.72 ? 7   TRP B CD2 1 
ATOM   34   N  NE1 . TRP A 1 7   ? -45.383 -40.426 25.423  1.00 18.21 ? 7   TRP B NE1 1 
ATOM   35   C  CE2 . TRP A 1 7   ? -44.484 -40.100 26.414  1.00 17.09 ? 7   TRP B CE2 1 
ATOM   36   C  CE3 . TRP A 1 7   ? -43.777 -40.990 28.614  1.00 12.93 ? 7   TRP B CE3 1 
ATOM   37   C  CZ2 . TRP A 1 7   ? -43.554 -39.047 26.474  1.00 16.76 ? 7   TRP B CZ2 1 
ATOM   38   C  CZ3 . TRP A 1 7   ? -42.819 -39.934 28.664  1.00 17.85 ? 7   TRP B CZ3 1 
ATOM   39   C  CH2 . TRP A 1 7   ? -42.758 -38.963 27.614  1.00 16.88 ? 7   TRP B CH2 1 
ATOM   40   N  N   . GLY A 1 8   ? -46.023 -41.906 30.787  1.00 19.38 ? 8   GLY B N   1 
ATOM   41   C  CA  . GLY A 1 8   ? -45.603 -40.854 31.730  1.00 17.53 ? 8   GLY B CA  1 
ATOM   42   C  C   . GLY A 1 8   ? -44.500 -41.403 32.605  1.00 17.08 ? 8   GLY B C   1 
ATOM   43   O  O   . GLY A 1 8   ? -43.688 -42.271 32.180  1.00 16.83 ? 8   GLY B O   1 
ATOM   44   N  N   . TYR A 1 9   ? -44.457 -40.882 33.825  1.00 16.18 ? 9   TYR B N   1 
ATOM   45   C  CA  . TYR A 1 9   ? -43.474 -41.311 34.791  1.00 15.18 ? 9   TYR B CA  1 
ATOM   46   C  C   . TYR A 1 9   ? -44.139 -41.668 36.127  1.00 18.00 ? 9   TYR B C   1 
ATOM   47   O  O   . TYR A 1 9   ? -43.443 -41.817 37.136  1.00 17.62 ? 9   TYR B O   1 
ATOM   48   C  CB  . TYR A 1 9   ? -42.524 -40.131 35.026  1.00 14.37 ? 9   TYR B CB  1 
ATOM   49   C  CG  . TYR A 1 9   ? -41.686 -39.785 33.818  1.00 14.47 ? 9   TYR B CG  1 
ATOM   50   C  CD1 . TYR A 1 9   ? -40.521 -40.486 33.533  1.00 11.66 ? 9   TYR B CD1 1 
ATOM   51   C  CD2 . TYR A 1 9   ? -42.085 -38.756 32.944  1.00 15.76 ? 9   TYR B CD2 1 
ATOM   52   C  CE1 . TYR A 1 9   ? -39.744 -40.151 32.369  1.00 15.03 ? 9   TYR B CE1 1 
ATOM   53   C  CE2 . TYR A 1 9   ? -41.311 -38.416 31.819  1.00 13.91 ? 9   TYR B CE2 1 
ATOM   54   C  CZ  . TYR A 1 9   ? -40.149 -39.100 31.537  1.00 13.33 ? 9   TYR B CZ  1 
ATOM   55   O  OH  . TYR A 1 9   ? -39.400 -38.696 30.420  1.00 15.49 ? 9   TYR B OH  1 
ATOM   56   N  N   . ARG A 1 10  ? -45.469 -41.794 36.126  1.00 19.87 ? 10  ARG B N   1 
ATOM   57   C  CA  . ARG A 1 10  ? -46.214 -42.234 37.327  1.00 22.79 ? 10  ARG B CA  1 
ATOM   58   C  C   . ARG A 1 10  ? -46.120 -43.779 37.500  1.00 23.63 ? 10  ARG B C   1 
ATOM   59   O  O   . ARG A 1 10  ? -45.480 -44.487 36.693  1.00 21.82 ? 10  ARG B O   1 
ATOM   60   C  CB  . ARG A 1 10  ? -47.664 -41.711 37.272  1.00 23.18 ? 10  ARG B CB  1 
ATOM   61   C  CG  . ARG A 1 10  ? -47.736 -40.182 37.336  1.00 25.56 ? 10  ARG B CG  1 
ATOM   62   C  CD  . ARG A 1 10  ? -49.099 -39.645 36.953  1.00 31.94 ? 10  ARG B CD  1 
ATOM   63   N  NE  . ARG A 1 10  ? -50.089 -39.709 38.035  1.00 34.65 ? 10  ARG B NE  1 
ATOM   64   C  CZ  . ARG A 1 10  ? -51.370 -39.296 37.955  1.00 37.39 ? 10  ARG B CZ  1 
ATOM   65   N  NH1 . ARG A 1 10  ? -51.886 -38.744 36.851  1.00 35.75 ? 10  ARG B NH1 1 
ATOM   66   N  NH2 . ARG A 1 10  ? -52.151 -39.404 39.021  1.00 38.94 ? 10  ARG B NH2 1 
ATOM   67   N  N   . GLU A 1 11  ? -46.722 -44.331 38.567  1.00 24.94 ? 11  GLU B N   1 
ATOM   68   C  CA  . GLU A 1 11  ? -46.558 -45.795 38.808  1.00 25.49 ? 11  GLU B CA  1 
ATOM   69   C  C   . GLU A 1 11  ? -47.075 -46.677 37.626  1.00 24.42 ? 11  GLU B C   1 
ATOM   70   O  O   . GLU A 1 11  ? -46.403 -47.639 37.200  1.00 24.36 ? 11  GLU B O   1 
ATOM   71   C  CB  . GLU A 1 11  ? -47.117 -46.224 40.218  1.00 26.83 ? 11  GLU B CB  1 
ATOM   72   C  CG  . GLU A 1 11  ? -47.485 -47.705 40.368  1.00 32.47 ? 11  GLU B CG  1 
ATOM   73   C  CD  . GLU A 1 11  ? -46.305 -48.673 40.313  1.00 41.36 ? 11  GLU B CD  1 
ATOM   74   O  OE1 . GLU A 1 11  ? -45.137 -48.238 40.462  1.00 44.39 ? 11  GLU B OE1 1 
ATOM   75   O  OE2 . GLU A 1 11  ? -46.564 -49.906 40.155  1.00 48.75 ? 11  GLU B OE2 1 
ATOM   76   N  N   . HIS A 1 12  ? -48.206 -46.320 37.045  1.00 24.51 ? 12  HIS B N   1 
ATOM   77   C  CA  . HIS A 1 12  ? -48.812 -47.246 36.082  1.00 27.25 ? 12  HIS B CA  1 
ATOM   78   C  C   . HIS A 1 12  ? -48.470 -46.923 34.645  1.00 26.13 ? 12  HIS B C   1 
ATOM   79   O  O   . HIS A 1 12  ? -48.681 -47.739 33.764  1.00 26.98 ? 12  HIS B O   1 
ATOM   80   C  CB  . HIS A 1 12  ? -50.342 -47.421 36.323  1.00 28.74 ? 12  HIS B CB  1 
ATOM   81   C  CG  . HIS A 1 12  ? -50.629 -47.957 37.686  1.00 32.33 ? 12  HIS B CG  1 
ATOM   82   N  ND1 . HIS A 1 12  ? -51.093 -47.162 38.713  1.00 36.99 ? 12  HIS B ND1 1 
ATOM   83   C  CD2 . HIS A 1 12  ? -50.370 -49.170 38.230  1.00 34.78 ? 12  HIS B CD2 1 
ATOM   84   C  CE1 . HIS A 1 12  ? -51.170 -47.883 39.819  1.00 37.23 ? 12  HIS B CE1 1 
ATOM   85   N  NE2 . HIS A 1 12  ? -50.720 -49.097 39.557  1.00 36.11 ? 12  HIS B NE2 1 
ATOM   86   N  N   . ASN A 1 13  ? -47.882 -45.754 34.412  1.00 25.02 ? 13  ASN B N   1 
ATOM   87   C  CA  . ASN A 1 13  ? -47.457 -45.418 33.031  1.00 22.29 ? 13  ASN B CA  1 
ATOM   88   C  C   . ASN A 1 13  ? -45.933 -45.161 32.882  1.00 22.27 ? 13  ASN B C   1 
ATOM   89   O  O   . ASN A 1 13  ? -45.521 -44.722 31.842  1.00 20.80 ? 13  ASN B O   1 
ATOM   90   C  CB  . ASN A 1 13  ? -48.305 -44.228 32.510  1.00 21.32 ? 13  ASN B CB  1 
ATOM   91   C  CG  . ASN A 1 13  ? -48.048 -42.937 33.265  1.00 17.19 ? 13  ASN B CG  1 
ATOM   92   O  OD1 . ASN A 1 13  ? -47.188 -42.893 34.097  1.00 18.93 ? 13  ASN B OD1 1 
ATOM   93   N  ND2 . ASN A 1 13  ? -48.756 -41.876 32.935  1.00 16.22 ? 13  ASN B ND2 1 
ATOM   94   N  N   . GLY A 1 14  ? -45.139 -45.414 33.928  1.00 19.65 ? 14  GLY B N   1 
ATOM   95   C  CA  . GLY A 1 14  ? -43.733 -45.012 33.990  1.00 19.59 ? 14  GLY B CA  1 
ATOM   96   C  C   . GLY A 1 14  ? -42.824 -45.892 33.166  1.00 18.36 ? 14  GLY B C   1 
ATOM   97   O  O   . GLY A 1 14  ? -43.272 -46.865 32.590  1.00 19.97 ? 14  GLY B O   1 
ATOM   98   N  N   . PRO A 1 15  ? -41.510 -45.559 33.114  1.00 19.41 ? 15  PRO B N   1 
ATOM   99   C  CA  . PRO A 1 15  ? -40.517 -46.252 32.307  1.00 17.97 ? 15  PRO B CA  1 
ATOM   100  C  C   . PRO A 1 15  ? -40.641 -47.762 32.231  1.00 20.38 ? 15  PRO B C   1 
ATOM   101  O  O   . PRO A 1 15  ? -40.446 -48.309 31.143  1.00 17.83 ? 15  PRO B O   1 
ATOM   102  C  CB  . PRO A 1 15  ? -39.183 -45.797 32.916  1.00 20.05 ? 15  PRO B CB  1 
ATOM   103  C  CG  . PRO A 1 15  ? -39.484 -44.317 33.219  1.00 16.75 ? 15  PRO B CG  1 
ATOM   104  C  CD  . PRO A 1 15  ? -40.914 -44.365 33.790  1.00 18.40 ? 15  PRO B CD  1 
ATOM   105  N  N   . ILE A 1 16  ? -40.910 -48.440 33.355  1.00 20.70 ? 16  ILE B N   1 
ATOM   106  C  CA  . ILE A 1 16  ? -40.943 -49.894 33.348  1.00 22.67 ? 16  ILE B CA  1 
ATOM   107  C  C   . ILE A 1 16  ? -42.055 -50.505 32.475  1.00 22.41 ? 16  ILE B C   1 
ATOM   108  O  O   . ILE A 1 16  ? -41.948 -51.667 32.041  1.00 25.65 ? 16  ILE B O   1 
ATOM   109  C  CB  . ILE A 1 16  ? -40.959 -50.472 34.827  1.00 23.58 ? 16  ILE B CB  1 
ATOM   110  C  CG1 . ILE A 1 16  ? -40.590 -51.956 34.817  1.00 28.59 ? 16  ILE B CG1 1 
ATOM   111  C  CG2 . ILE A 1 16  ? -42.298 -50.189 35.498  1.00 23.17 ? 16  ILE B CG2 1 
ATOM   112  C  CD1 . ILE A 1 16  ? -39.100 -52.195 34.859  1.00 32.80 ? 16  ILE B CD1 1 
ATOM   113  N  N   . HIS A 1 17  ? -43.100 -49.721 32.206  1.00 22.19 ? 17  HIS B N   1 
ATOM   114  C  CA  . HIS A 1 17  ? -44.312 -50.112 31.475  1.00 21.61 ? 17  HIS B CA  1 
ATOM   115  C  C   . HIS A 1 17  ? -44.224 -49.702 30.025  1.00 21.50 ? 17  HIS B C   1 
ATOM   116  O  O   . HIS A 1 17  ? -45.105 -50.063 29.235  1.00 22.36 ? 17  HIS B O   1 
ATOM   117  C  CB  . HIS A 1 17  ? -45.524 -49.337 32.023  1.00 22.31 ? 17  HIS B CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? -45.817 -49.652 33.447  1.00 29.09 ? 17  HIS B CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? -46.425 -50.828 33.830  1.00 30.70 ? 17  HIS B ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? -45.525 -48.983 34.588  1.00 31.38 ? 17  HIS B CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? -46.521 -50.852 35.150  1.00 32.73 ? 17  HIS B CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? -45.979 -49.749 35.631  1.00 34.24 ? 17  HIS B NE2 1 
ATOM   123  N  N   . TRP A 1 18  ? -43.207 -48.899 29.669  1.00 18.34 ? 18  TRP B N   1 
ATOM   124  C  CA  . TRP A 1 18  ? -43.182 -48.356 28.291  1.00 17.98 ? 18  TRP B CA  1 
ATOM   125  C  C   . TRP A 1 18  ? -43.027 -49.445 27.262  1.00 18.46 ? 18  TRP B C   1 
ATOM   126  O  O   . TRP A 1 18  ? -43.598 -49.318 26.193  1.00 19.74 ? 18  TRP B O   1 
ATOM   127  C  CB  . TRP A 1 18  ? -42.061 -47.294 28.082  1.00 16.32 ? 18  TRP B CB  1 
ATOM   128  C  CG  . TRP A 1 18  ? -42.218 -46.038 28.896  1.00 13.54 ? 18  TRP B CG  1 
ATOM   129  C  CD1 . TRP A 1 18  ? -43.341 -45.590 29.593  1.00 13.55 ? 18  TRP B CD1 1 
ATOM   130  C  CD2 . TRP A 1 18  ? -41.217 -45.015 29.032  1.00 15.35 ? 18  TRP B CD2 1 
ATOM   131  N  NE1 . TRP A 1 18  ? -43.070 -44.361 30.178  1.00 12.88 ? 18  TRP B NE1 1 
ATOM   132  C  CE2 . TRP A 1 18  ? -41.777 -43.980 29.824  1.00 13.73 ? 18  TRP B CE2 1 
ATOM   133  C  CE3 . TRP A 1 18  ? -39.891 -44.866 28.546  1.00 12.50 ? 18  TRP B CE3 1 
ATOM   134  C  CZ2 . TRP A 1 18  ? -41.044 -42.815 30.151  1.00 10.79 ? 18  TRP B CZ2 1 
ATOM   135  C  CZ3 . TRP A 1 18  ? -39.162 -43.703 28.914  1.00 11.63 ? 18  TRP B CZ3 1 
ATOM   136  C  CH2 . TRP A 1 18  ? -39.764 -42.694 29.680  1.00 10.60 ? 18  TRP B CH2 1 
ATOM   137  N  N   . LYS A 1 19  ? -42.261 -50.495 27.588  1.00 20.51 ? 19  LYS B N   1 
ATOM   138  C  CA  . LYS A 1 19  ? -42.076 -51.685 26.696  1.00 23.50 ? 19  LYS B CA  1 
ATOM   139  C  C   . LYS A 1 19  ? -43.391 -52.314 26.236  1.00 24.70 ? 19  LYS B C   1 
ATOM   140  O  O   . LYS A 1 19  ? -43.382 -52.984 25.222  1.00 25.63 ? 19  LYS B O   1 
ATOM   141  C  CB  . LYS A 1 19  ? -41.221 -52.788 27.358  1.00 22.56 ? 19  LYS B CB  1 
ATOM   142  C  CG  . LYS A 1 19  ? -41.891 -53.467 28.627  1.00 23.85 ? 19  LYS B CG  1 
ATOM   143  C  CD  . LYS A 1 19  ? -40.984 -54.556 29.359  1.00 26.42 ? 19  LYS B CD  1 
ATOM   144  C  CE  . LYS A 1 19  ? -39.608 -54.117 29.952  1.00 34.93 ? 19  LYS B CE  1 
ATOM   145  N  NZ  . LYS A 1 19  ? -39.656 -53.175 31.177  1.00 33.85 ? 19  LYS B NZ  1 
ATOM   146  N  N   . GLU A 1 20  ? -44.491 -52.107 26.984  1.00 25.80 ? 20  GLU B N   1 
ATOM   147  C  CA  . GLU A 1 20  ? -45.822 -52.693 26.685  1.00 26.76 ? 20  GLU B CA  1 
ATOM   148  C  C   . GLU A 1 20  ? -46.357 -52.148 25.397  1.00 26.53 ? 20  GLU B C   1 
ATOM   149  O  O   . GLU A 1 20  ? -46.830 -52.931 24.519  1.00 28.11 ? 20  GLU B O   1 
ATOM   150  C  CB  . GLU A 1 20  ? -46.837 -52.413 27.797  1.00 26.64 ? 20  GLU B CB  1 
ATOM   151  C  CG  . GLU A 1 20  ? -46.584 -53.214 29.081  1.00 29.26 ? 20  GLU B CG  1 
ATOM   152  C  CD  . GLU A 1 20  ? -47.275 -52.609 30.319  1.00 29.49 ? 20  GLU B CD  1 
ATOM   153  O  OE1 . GLU A 1 20  ? -48.307 -51.911 30.160  1.00 30.84 ? 20  GLU B OE1 1 
ATOM   154  O  OE2 . GLU A 1 20  ? -46.736 -52.858 31.432  1.00 30.88 ? 20  GLU B OE2 1 
ATOM   155  N  N   . PHE A 1 21  ? -46.271 -50.835 25.239  1.00 24.65 ? 21  PHE B N   1 
ATOM   156  C  CA  . PHE A 1 21  ? -46.583 -50.205 23.963  1.00 24.44 ? 21  PHE B CA  1 
ATOM   157  C  C   . PHE A 1 21  ? -45.451 -49.814 23.000  1.00 23.10 ? 21  PHE B C   1 
ATOM   158  O  O   . PHE A 1 21  ? -45.703 -49.520 21.833  1.00 23.97 ? 21  PHE B O   1 
ATOM   159  C  CB  . PHE A 1 21  ? -47.586 -49.071 24.197  1.00 26.82 ? 21  PHE B CB  1 
ATOM   160  C  CG  . PHE A 1 21  ? -48.936 -49.585 24.570  1.00 31.75 ? 21  PHE B CG  1 
ATOM   161  C  CD1 . PHE A 1 21  ? -49.352 -49.604 25.893  1.00 34.47 ? 21  PHE B CD1 1 
ATOM   162  C  CD2 . PHE A 1 21  ? -49.753 -50.171 23.590  1.00 36.49 ? 21  PHE B CD2 1 
ATOM   163  C  CE1 . PHE A 1 21  ? -50.586 -50.140 26.257  1.00 34.05 ? 21  PHE B CE1 1 
ATOM   164  C  CE2 . PHE A 1 21  ? -51.005 -50.711 23.945  1.00 38.92 ? 21  PHE B CE2 1 
ATOM   165  C  CZ  . PHE A 1 21  ? -51.402 -50.691 25.297  1.00 34.58 ? 21  PHE B CZ  1 
ATOM   166  N  N   . PHE A 1 22  ? -44.221 -49.787 23.492  1.00 21.50 ? 22  PHE B N   1 
ATOM   167  C  CA  . PHE A 1 22  ? -43.045 -49.464 22.686  1.00 20.40 ? 22  PHE B CA  1 
ATOM   168  C  C   . PHE A 1 22  ? -41.963 -50.543 22.876  1.00 20.41 ? 22  PHE B C   1 
ATOM   169  O  O   . PHE A 1 22  ? -41.057 -50.379 23.667  1.00 19.19 ? 22  PHE B O   1 
ATOM   170  C  CB  . PHE A 1 22  ? -42.525 -48.027 23.070  1.00 19.71 ? 22  PHE B CB  1 
ATOM   171  C  CG  . PHE A 1 22  ? -43.595 -46.974 22.997  1.00 17.77 ? 22  PHE B CG  1 
ATOM   172  C  CD1 . PHE A 1 22  ? -43.912 -46.357 21.762  1.00 20.92 ? 22  PHE B CD1 1 
ATOM   173  C  CD2 . PHE A 1 22  ? -44.328 -46.636 24.126  1.00 22.39 ? 22  PHE B CD2 1 
ATOM   174  C  CE1 . PHE A 1 22  ? -44.944 -45.387 21.682  1.00 20.62 ? 22  PHE B CE1 1 
ATOM   175  C  CE2 . PHE A 1 22  ? -45.361 -45.709 24.078  1.00 23.02 ? 22  PHE B CE2 1 
ATOM   176  C  CZ  . PHE A 1 22  ? -45.684 -45.073 22.842  1.00 21.16 ? 22  PHE B CZ  1 
ATOM   177  N  N   . PRO A 1 23  ? -42.073 -51.703 22.195  1.00 20.93 ? 23  PRO B N   1 
ATOM   178  C  CA  . PRO A 1 23  ? -41.099 -52.726 22.587  1.00 20.35 ? 23  PRO B CA  1 
ATOM   179  C  C   . PRO A 1 23  ? -39.610 -52.447 22.307  1.00 18.89 ? 23  PRO B C   1 
ATOM   180  O  O   . PRO A 1 23  ? -38.757 -53.160 22.834  1.00 19.06 ? 23  PRO B O   1 
ATOM   181  C  CB  . PRO A 1 23  ? -41.592 -54.005 21.850  1.00 21.22 ? 23  PRO B CB  1 
ATOM   182  C  CG  . PRO A 1 23  ? -42.378 -53.466 20.682  1.00 23.92 ? 23  PRO B CG  1 
ATOM   183  C  CD  . PRO A 1 23  ? -43.038 -52.199 21.190  1.00 21.55 ? 23  PRO B CD  1 
ATOM   184  N  N   . ILE A 1 24  ? -39.321 -51.444 21.464  1.00 18.63 ? 24  ILE B N   1 
ATOM   185  C  CA  . ILE A 1 24  ? -37.958 -50.962 21.241  1.00 18.37 ? 24  ILE B CA  1 
ATOM   186  C  C   . ILE A 1 24  ? -37.291 -50.521 22.583  1.00 16.99 ? 24  ILE B C   1 
ATOM   187  O  O   . ILE A 1 24  ? -36.058 -50.373 22.625  1.00 16.93 ? 24  ILE B O   1 
ATOM   188  C  CB  . ILE A 1 24  ? -37.898 -49.870 20.117  1.00 17.81 ? 24  ILE B CB  1 
ATOM   189  C  CG1 . ILE A 1 24  ? -36.496 -49.833 19.431  1.00 16.57 ? 24  ILE B CG1 1 
ATOM   190  C  CG2 . ILE A 1 24  ? -38.375 -48.510 20.637  1.00 14.01 ? 24  ILE B CG2 1 
ATOM   191  C  CD1 . ILE A 1 24  ? -36.225 -51.026 18.500  1.00 19.76 ? 24  ILE B CD1 1 
ATOM   192  N  N   . ALA A 1 25  ? -38.100 -50.344 23.649  1.00 18.49 ? 25  ALA B N   1 
ATOM   193  C  CA  . ALA A 1 25  ? -37.580 -49.953 24.994  1.00 19.21 ? 25  ALA B CA  1 
ATOM   194  C  C   . ALA A 1 25  ? -36.461 -50.930 25.397  1.00 20.29 ? 25  ALA B C   1 
ATOM   195  O  O   . ALA A 1 25  ? -35.486 -50.571 26.082  1.00 21.46 ? 25  ALA B O   1 
ATOM   196  C  CB  . ALA A 1 25  ? -38.730 -49.983 26.044  1.00 17.10 ? 25  ALA B CB  1 
ATOM   197  N  N   . ASP A 1 26  ? -36.647 -52.194 24.985  1.00 21.20 ? 26  ASP B N   1 
ATOM   198  C  CA  . ASP A 1 26  ? -35.657 -53.265 25.235  1.00 23.09 ? 26  ASP B CA  1 
ATOM   199  C  C   . ASP A 1 26  ? -34.712 -53.522 24.054  1.00 22.85 ? 26  ASP B C   1 
ATOM   200  O  O   . ASP A 1 26  ? -34.095 -54.594 23.974  1.00 22.47 ? 26  ASP B O   1 
ATOM   201  C  CB  . ASP A 1 26  ? -36.387 -54.549 25.634  1.00 24.65 ? 26  ASP B CB  1 
ATOM   202  C  CG  . ASP A 1 26  ? -37.374 -54.327 26.805  1.00 25.57 ? 26  ASP B CG  1 
ATOM   203  O  OD1 . ASP A 1 26  ? -37.073 -53.599 27.765  1.00 29.37 ? 26  ASP B OD1 1 
ATOM   204  O  OD2 . ASP A 1 26  ? -38.472 -54.855 26.766  1.00 25.32 ? 26  ASP B OD2 1 
ATOM   205  N  N   . GLY A 1 27  ? -34.590 -52.517 23.173  1.00 21.63 ? 27  GLY B N   1 
ATOM   206  C  CA  . GLY A 1 27  ? -33.692 -52.517 22.045  1.00 20.58 ? 27  GLY B CA  1 
ATOM   207  C  C   . GLY A 1 27  ? -32.209 -52.624 22.412  1.00 18.88 ? 27  GLY B C   1 
ATOM   208  O  O   . GLY A 1 27  ? -31.831 -52.704 23.567  1.00 19.64 ? 27  GLY B O   1 
ATOM   209  N  N   . ASP A 1 28  ? -31.398 -52.665 21.378  1.00 19.65 ? 28  ASP B N   1 
ATOM   210  C  CA  . ASP A 1 28  ? -29.928 -52.709 21.428  1.00 17.09 ? 28  ASP B CA  1 
ATOM   211  C  C   . ASP A 1 28  ? -29.257 -51.322 21.380  1.00 15.43 ? 28  ASP B C   1 
ATOM   212  O  O   . ASP A 1 28  ? -28.061 -51.232 21.543  1.00 14.34 ? 28  ASP B O   1 
ATOM   213  C  CB  . ASP A 1 28  ? -29.441 -53.507 20.220  1.00 17.75 ? 28  ASP B CB  1 
ATOM   214  C  CG  . ASP A 1 28  ? -29.705 -55.025 20.389  1.00 20.88 ? 28  ASP B CG  1 
ATOM   215  O  OD1 . ASP A 1 28  ? -29.959 -55.454 21.528  1.00 22.85 ? 28  ASP B OD1 1 
ATOM   216  O  OD2 . ASP A 1 28  ? -29.755 -55.746 19.383  1.00 22.93 ? 28  ASP B OD2 1 
ATOM   217  N  N   . GLN A 1 29  ? -30.012 -50.253 21.120  1.00 13.94 ? 29  GLN B N   1 
ATOM   218  C  CA  . GLN A 1 29  ? -29.421 -48.881 21.076  1.00 14.98 ? 29  GLN B CA  1 
ATOM   219  C  C   . GLN A 1 29  ? -30.258 -47.905 21.869  1.00 14.91 ? 29  GLN B C   1 
ATOM   220  O  O   . GLN A 1 29  ? -30.579 -46.841 21.392  1.00 14.48 ? 29  GLN B O   1 
ATOM   221  C  CB  . GLN A 1 29  ? -29.215 -48.347 19.667  1.00 13.86 ? 29  GLN B CB  1 
ATOM   222  C  CG  . GLN A 1 29  ? -28.256 -49.270 18.912  1.00 21.23 ? 29  GLN B CG  1 
ATOM   223  C  CD  . GLN A 1 29  ? -27.314 -48.604 17.952  1.00 22.43 ? 29  GLN B CD  1 
ATOM   224  O  OE1 . GLN A 1 29  ? -26.188 -49.107 17.752  1.00 27.43 ? 29  GLN B OE1 1 
ATOM   225  N  NE2 . GLN A 1 29  ? -27.748 -47.493 17.318  1.00 15.44 ? 29  GLN B NE2 1 
ATOM   226  N  N   . GLN A 1 30  ? -30.583 -48.313 23.092  1.00 14.27 ? 30  GLN B N   1 
ATOM   227  C  CA  . GLN A 1 30  ? -31.442 -47.545 23.949  1.00 13.46 ? 30  GLN B CA  1 
ATOM   228  C  C   . GLN A 1 30  ? -30.646 -46.599 24.815  1.00 13.53 ? 30  GLN B C   1 
ATOM   229  O  O   . GLN A 1 30  ? -29.498 -46.859 25.173  1.00 15.08 ? 30  GLN B O   1 
ATOM   230  C  CB  . GLN A 1 30  ? -32.355 -48.456 24.771  1.00 12.47 ? 30  GLN B CB  1 
ATOM   231  C  CG  . GLN A 1 30  ? -33.487 -49.053 23.926  1.00 14.64 ? 30  GLN B CG  1 
ATOM   232  C  CD  . GLN A 1 30  ? -34.478 -48.032 23.466  1.00 11.05 ? 30  GLN B CD  1 
ATOM   233  O  OE1 . GLN A 1 30  ? -35.186 -47.498 24.263  1.00 10.32 ? 30  GLN B OE1 1 
ATOM   234  N  NE2 . GLN A 1 30  ? -34.513 -47.739 22.147  1.00 11.33 ? 30  GLN B NE2 1 
ATOM   235  N  N   . SER A 1 31  ? -31.261 -45.470 25.090  1.00 12.62 ? 31  SER B N   1 
ATOM   236  C  CA  . SER A 1 31  ? -30.699 -44.433 25.909  1.00 11.97 ? 31  SER B CA  1 
ATOM   237  C  C   . SER A 1 31  ? -31.647 -44.136 27.092  1.00 12.48 ? 31  SER B C   1 
ATOM   238  O  O   . SER A 1 31  ? -32.846 -44.451 27.052  1.00 12.01 ? 31  SER B O   1 
ATOM   239  C  CB  . SER A 1 31  ? -30.528 -43.142 25.106  1.00 11.90 ? 31  SER B CB  1 
ATOM   240  O  OG  . SER A 1 31  ? -29.455 -43.245 24.213  1.00 12.11 ? 31  SER B OG  1 
ATOM   241  N  N   . PRO A 1 32  ? -31.111 -43.553 28.181  1.00 13.44 ? 32  PRO B N   1 
ATOM   242  C  CA  . PRO A 1 32  ? -29.736 -43.241 28.424  1.00 13.19 ? 32  PRO B CA  1 
ATOM   243  C  C   . PRO A 1 32  ? -28.936 -44.499 28.832  1.00 15.21 ? 32  PRO B C   1 
ATOM   244  O  O   . PRO A 1 32  ? -29.475 -45.575 28.823  1.00 13.56 ? 32  PRO B O   1 
ATOM   245  C  CB  . PRO A 1 32  ? -29.824 -42.258 29.623  1.00 13.70 ? 32  PRO B CB  1 
ATOM   246  C  CG  . PRO A 1 32  ? -30.975 -42.829 30.418  1.00 12.02 ? 32  PRO B CG  1 
ATOM   247  C  CD  . PRO A 1 32  ? -31.969 -43.231 29.355  1.00 12.73 ? 32  PRO B CD  1 
ATOM   248  N  N   . ILE A 1 33  ? -27.676 -44.304 29.212  1.00 14.71 ? 33  ILE B N   1 
ATOM   249  C  CA  . ILE A 1 33  ? -26.752 -45.408 29.484  1.00 16.52 ? 33  ILE B CA  1 
ATOM   250  C  C   . ILE A 1 33  ? -25.920 -44.976 30.694  1.00 16.92 ? 33  ILE B C   1 
ATOM   251  O  O   . ILE A 1 33  ? -25.988 -43.818 31.117  1.00 16.06 ? 33  ILE B O   1 
ATOM   252  C  CB  . ILE A 1 33  ? -25.789 -45.730 28.293  1.00 16.23 ? 33  ILE B CB  1 
ATOM   253  C  CG1 . ILE A 1 33  ? -24.849 -44.533 28.006  1.00 15.09 ? 33  ILE B CG1 1 
ATOM   254  C  CG2 . ILE A 1 33  ? -26.568 -46.294 27.067  1.00 16.56 ? 33  ILE B CG2 1 
ATOM   255  C  CD1 . ILE A 1 33  ? -23.680 -44.795 27.132  1.00 14.48 ? 33  ILE B CD1 1 
ATOM   256  N  N   . GLU A 1 34  ? -25.201 -45.937 31.271  1.00 17.63 ? 34  GLU B N   1 
ATOM   257  C  CA  . GLU A 1 34  ? -24.114 -45.664 32.181  1.00 18.04 ? 34  GLU B CA  1 
ATOM   258  C  C   . GLU A 1 34  ? -22.822 -45.546 31.386  1.00 17.79 ? 34  GLU B C   1 
ATOM   259  O  O   . GLU A 1 34  ? -22.493 -46.399 30.571  1.00 18.75 ? 34  GLU B O   1 
ATOM   260  C  CB  . GLU A 1 34  ? -23.950 -46.836 33.163  1.00 18.09 ? 34  GLU B CB  1 
ATOM   261  C  CG  . GLU A 1 34  ? -25.112 -46.927 34.186  1.00 17.35 ? 34  GLU B CG  1 
ATOM   262  C  CD  . GLU A 1 34  ? -24.830 -48.087 35.167  1.00 20.08 ? 34  GLU B CD  1 
ATOM   263  O  OE1 . GLU A 1 34  ? -24.162 -47.801 36.213  1.00 20.41 ? 34  GLU B OE1 1 
ATOM   264  O  OE2 . GLU A 1 34  ? -25.174 -49.246 34.813  1.00 18.58 ? 34  GLU B OE2 1 
ATOM   265  N  N   . ILE A 1 35  ? -22.084 -44.504 31.662  1.00 19.11 ? 35  ILE B N   1 
ATOM   266  C  CA  . ILE A 1 35  ? -20.764 -44.322 31.101  1.00 20.71 ? 35  ILE B CA  1 
ATOM   267  C  C   . ILE A 1 35  ? -19.646 -44.775 32.106  1.00 21.68 ? 35  ILE B C   1 
ATOM   268  O  O   . ILE A 1 35  ? -19.490 -44.191 33.163  1.00 22.18 ? 35  ILE B O   1 
ATOM   269  C  CB  . ILE A 1 35  ? -20.576 -42.859 30.670  1.00 19.81 ? 35  ILE B CB  1 
ATOM   270  C  CG1 . ILE A 1 35  ? -21.629 -42.508 29.577  1.00 20.29 ? 35  ILE B CG1 1 
ATOM   271  C  CG2 . ILE A 1 35  ? -19.152 -42.664 30.140  1.00 18.30 ? 35  ILE B CG2 1 
ATOM   272  C  CD1 . ILE A 1 35  ? -21.874 -41.021 29.354  1.00 20.81 ? 35  ILE B CD1 1 
ATOM   273  N  N   . LYS A 1 36  ? -18.932 -45.850 31.727  1.00 23.00 ? 36  LYS B N   1 
ATOM   274  C  CA  . LYS A 1 36  ? -17.836 -46.389 32.507  1.00 25.26 ? 36  LYS B CA  1 
ATOM   275  C  C   . LYS A 1 36  ? -16.614 -45.807 31.878  1.00 25.47 ? 36  LYS B C   1 
ATOM   276  O  O   . LYS A 1 36  ? -16.191 -46.281 30.832  1.00 26.70 ? 36  LYS B O   1 
ATOM   277  C  CB  . LYS A 1 36  ? -17.780 -47.912 32.359  1.00 25.00 ? 36  LYS B CB  1 
ATOM   278  C  CG  . LYS A 1 36  ? -16.603 -48.637 33.116  1.00 26.98 ? 36  LYS B CG  1 
ATOM   279  C  CD  . LYS A 1 36  ? -16.862 -50.169 33.267  1.00 27.10 ? 36  LYS B CD  1 
ATOM   280  C  CE  . LYS A 1 36  ? -17.735 -50.574 34.478  1.00 27.43 ? 36  LYS B CE  1 
ATOM   281  N  NZ  . LYS A 1 36  ? -18.137 -52.075 34.402  1.00 22.00 ? 36  LYS B NZ  1 
ATOM   282  N  N   . THR A 1 37  ? -16.006 -44.829 32.524  1.00 26.29 ? 37  THR B N   1 
ATOM   283  C  CA  . THR A 1 37  ? -14.857 -44.138 31.871  1.00 27.85 ? 37  THR B CA  1 
ATOM   284  C  C   . THR A 1 37  ? -13.608 -45.010 31.518  1.00 29.02 ? 37  THR B C   1 
ATOM   285  O  O   . THR A 1 37  ? -12.937 -44.705 30.527  1.00 26.79 ? 37  THR B O   1 
ATOM   286  C  CB  . THR A 1 37  ? -14.480 -42.838 32.585  1.00 26.73 ? 37  THR B CB  1 
ATOM   287  O  OG1 . THR A 1 37  ? -14.044 -43.144 33.904  1.00 25.80 ? 37  THR B OG1 1 
ATOM   288  C  CG2 . THR A 1 37  ? -15.705 -41.981 32.674  1.00 27.20 ? 37  THR B CG2 1 
ATOM   289  N  N   . LYS A 1 38  ? -13.319 -46.077 32.279  1.00 30.03 ? 38  LYS B N   1 
ATOM   290  C  CA  . LYS A 1 38  ? -12.105 -46.886 32.023  1.00 32.40 ? 38  LYS B CA  1 
ATOM   291  C  C   . LYS A 1 38  ? -12.202 -47.656 30.712  1.00 33.13 ? 38  LYS B C   1 
ATOM   292  O  O   . LYS A 1 38  ? -11.187 -48.008 30.108  1.00 34.42 ? 38  LYS B O   1 
ATOM   293  C  CB  . LYS A 1 38  ? -11.739 -47.852 33.178  1.00 34.25 ? 38  LYS B CB  1 
ATOM   294  C  CG  . LYS A 1 38  ? -12.806 -48.904 33.519  1.00 35.44 ? 38  LYS B CG  1 
ATOM   295  C  CD  . LYS A 1 38  ? -12.236 -50.339 33.560  1.00 40.04 ? 38  LYS B CD  1 
ATOM   296  C  CE  . LYS A 1 38  ? -13.388 -51.364 33.645  1.00 39.23 ? 38  LYS B CE  1 
ATOM   297  N  NZ  . LYS A 1 38  ? -13.248 -52.525 32.706  1.00 44.03 ? 38  LYS B NZ  1 
ATOM   298  N  N   . GLU A 1 39  ? -13.439 -47.879 30.277  1.00 33.69 ? 39  GLU B N   1 
ATOM   299  C  CA  . GLU A 1 39  ? -13.752 -48.523 29.014  1.00 34.55 ? 39  GLU B CA  1 
ATOM   300  C  C   . GLU A 1 39  ? -13.900 -47.576 27.832  1.00 34.71 ? 39  GLU B C   1 
ATOM   301  O  O   . GLU A 1 39  ? -13.975 -48.021 26.685  1.00 37.07 ? 39  GLU B O   1 
ATOM   302  C  CB  . GLU A 1 39  ? -15.026 -49.349 29.180  1.00 35.74 ? 39  GLU B CB  1 
ATOM   303  C  CG  . GLU A 1 39  ? -14.962 -50.306 30.386  1.00 38.56 ? 39  GLU B CG  1 
ATOM   304  C  CD  . GLU A 1 39  ? -15.617 -51.630 30.093  1.00 42.78 ? 39  GLU B CD  1 
ATOM   305  O  OE1 . GLU A 1 39  ? -14.913 -52.651 30.158  1.00 45.97 ? 39  GLU B OE1 1 
ATOM   306  O  OE2 . GLU A 1 39  ? -16.824 -51.642 29.756  1.00 46.87 ? 39  GLU B OE2 1 
ATOM   307  N  N   . VAL A 1 40  ? -13.920 -46.278 28.102  1.00 33.82 ? 40  VAL B N   1 
ATOM   308  C  CA  . VAL A 1 40  ? -14.188 -45.305 27.098  1.00 31.99 ? 40  VAL B CA  1 
ATOM   309  C  C   . VAL A 1 40  ? -12.877 -45.018 26.404  1.00 32.47 ? 40  VAL B C   1 
ATOM   310  O  O   . VAL A 1 40  ? -11.878 -44.711 27.059  1.00 34.80 ? 40  VAL B O   1 
ATOM   311  C  CB  . VAL A 1 40  ? -14.776 -44.012 27.736  1.00 32.31 ? 40  VAL B CB  1 
ATOM   312  C  CG1 . VAL A 1 40  ? -14.556 -42.821 26.836  1.00 31.14 ? 40  VAL B CG1 1 
ATOM   313  C  CG2 . VAL A 1 40  ? -16.245 -44.194 28.094  1.00 28.76 ? 40  VAL B CG2 1 
ATOM   314  N  N   . LYS A 1 41  ? -12.859 -45.107 25.085  1.00 31.33 ? 41  LYS B N   1 
ATOM   315  C  CA  . LYS A 1 41  ? -11.667 -44.706 24.329  1.00 30.92 ? 41  LYS B CA  1 
ATOM   316  C  C   . LYS A 1 41  ? -11.794 -43.315 23.694  1.00 29.83 ? 41  LYS B C   1 
ATOM   317  O  O   . LYS A 1 41  ? -12.772 -43.029 22.990  1.00 26.09 ? 41  LYS B O   1 
ATOM   318  C  CB  . LYS A 1 41  ? -11.295 -45.760 23.259  1.00 32.17 ? 41  LYS B CB  1 
ATOM   319  C  CG  . LYS A 1 41  ? -10.721 -47.075 23.814  1.00 35.00 ? 41  LYS B CG  1 
ATOM   320  C  CD  . LYS A 1 41  ? -9.843  -47.749 22.737  1.00 42.79 ? 41  LYS B CD  1 
ATOM   321  C  CE  . LYS A 1 41  ? -9.753  -49.274 22.927  1.00 45.43 ? 41  LYS B CE  1 
ATOM   322  N  NZ  . LYS A 1 41  ? -11.094 -49.983 22.849  1.00 45.44 ? 41  LYS B NZ  1 
ATOM   323  N  N   . TYR A 1 42  ? -10.769 -42.494 23.948  1.00 28.52 ? 42  TYR B N   1 
ATOM   324  C  CA  . TYR A 1 42  ? -10.478 -41.279 23.190  1.00 28.83 ? 42  TYR B CA  1 
ATOM   325  C  C   . TYR A 1 42  ? -10.401 -41.540 21.668  1.00 29.04 ? 42  TYR B C   1 
ATOM   326  O  O   . TYR A 1 42  ? -9.707  -42.446 21.222  1.00 29.47 ? 42  TYR B O   1 
ATOM   327  C  CB  . TYR A 1 42  ? -9.160  -40.658 23.685  1.00 28.98 ? 42  TYR B CB  1 
ATOM   328  C  CG  . TYR A 1 42  ? -8.664  -39.592 22.760  1.00 30.27 ? 42  TYR B CG  1 
ATOM   329  C  CD1 . TYR A 1 42  ? -9.369  -38.403 22.623  1.00 27.64 ? 42  TYR B CD1 1 
ATOM   330  C  CD2 . TYR A 1 42  ? -7.493  -39.763 22.005  1.00 29.29 ? 42  TYR B CD2 1 
ATOM   331  C  CE1 . TYR A 1 42  ? -8.945  -37.403 21.763  1.00 30.24 ? 42  TYR B CE1 1 
ATOM   332  C  CE2 . TYR A 1 42  ? -7.069  -38.764 21.138  1.00 31.20 ? 42  TYR B CE2 1 
ATOM   333  C  CZ  . TYR A 1 42  ? -7.794  -37.576 21.052  1.00 29.24 ? 42  TYR B CZ  1 
ATOM   334  O  OH  . TYR A 1 42  ? -7.448  -36.565 20.200  1.00 32.42 ? 42  TYR B OH  1 
ATOM   335  N  N   . ASP A 1 43  ? -11.099 -40.726 20.875  1.00 29.22 ? 43  ASP B N   1 
ATOM   336  C  CA  . ASP A 1 43  ? -11.071 -40.851 19.416  1.00 28.84 ? 43  ASP B CA  1 
ATOM   337  C  C   . ASP A 1 43  ? -10.581 -39.576 18.742  1.00 28.98 ? 43  ASP B C   1 
ATOM   338  O  O   . ASP A 1 43  ? -11.335 -38.584 18.633  1.00 26.27 ? 43  ASP B O   1 
ATOM   339  C  CB  . ASP A 1 43  ? -12.483 -41.229 18.885  1.00 30.04 ? 43  ASP B CB  1 
ATOM   340  C  CG  . ASP A 1 43  ? -12.477 -41.571 17.373  1.00 31.44 ? 43  ASP B CG  1 
ATOM   341  O  OD1 . ASP A 1 43  ? -11.492 -41.243 16.661  1.00 33.23 ? 43  ASP B OD1 1 
ATOM   342  O  OD2 . ASP A 1 43  ? -13.470 -42.142 16.905  1.00 30.58 ? 43  ASP B OD2 1 
ATOM   343  N  N   . SER A 1 44  ? -9.342  -39.623 18.221  1.00 28.80 ? 44  SER B N   1 
ATOM   344  C  CA  . SER A 1 44  ? -8.695  -38.453 17.583  1.00 29.24 ? 44  SER B CA  1 
ATOM   345  C  C   . SER A 1 44  ? -9.344  -38.045 16.265  1.00 29.63 ? 44  SER B C   1 
ATOM   346  O  O   . SER A 1 44  ? -9.110  -36.905 15.781  1.00 30.19 ? 44  SER B O   1 
ATOM   347  C  CB  . SER A 1 44  ? -7.195  -38.732 17.343  1.00 29.45 ? 44  SER B CB  1 
ATOM   348  O  OG  . SER A 1 44  ? -7.041  -39.983 16.717  1.00 30.75 ? 44  SER B OG  1 
ATOM   349  N  N   . SER A 1 45  ? -10.138 -38.967 15.684  1.00 28.83 ? 45  SER B N   1 
ATOM   350  C  CA  . SER A 1 45  ? -10.922 -38.686 14.466  1.00 29.50 ? 45  SER B CA  1 
ATOM   351  C  C   . SER A 1 45  ? -12.158 -37.745 14.635  1.00 29.61 ? 45  SER B C   1 
ATOM   352  O  O   . SER A 1 45  ? -12.637 -37.093 13.655  1.00 30.85 ? 45  SER B O   1 
ATOM   353  C  CB  . SER A 1 45  ? -11.326 -39.973 13.768  1.00 29.40 ? 45  SER B CB  1 
ATOM   354  O  OG  . SER A 1 45  ? -12.534 -40.464 14.280  1.00 30.09 ? 45  SER B OG  1 
ATOM   355  N  N   . LEU A 1 46  ? -12.636 -37.630 15.860  1.00 29.84 ? 46  LEU B N   1 
ATOM   356  C  CA  . LEU A 1 46  ? -13.618 -36.564 16.202  1.00 29.57 ? 46  LEU B CA  1 
ATOM   357  C  C   . LEU A 1 46  ? -13.148 -35.127 15.861  1.00 30.06 ? 46  LEU B C   1 
ATOM   358  O  O   . LEU A 1 46  ? -12.045 -34.731 16.239  1.00 29.53 ? 46  LEU B O   1 
ATOM   359  C  CB  . LEU A 1 46  ? -14.027 -36.675 17.672  1.00 28.48 ? 46  LEU B CB  1 
ATOM   360  C  CG  . LEU A 1 46  ? -14.643 -38.032 18.039  1.00 27.31 ? 46  LEU B CG  1 
ATOM   361  C  CD1 . LEU A 1 46  ? -14.582 -38.206 19.560  1.00 23.19 ? 46  LEU B CD1 1 
ATOM   362  C  CD2 . LEU A 1 46  ? -16.104 -38.224 17.543  1.00 24.36 ? 46  LEU B CD2 1 
ATOM   363  N  N   . ARG A 1 47  ? -13.969 -34.372 15.119  1.00 29.85 ? 47  ARG B N   1 
ATOM   364  C  CA  . ARG A 1 47  ? -13.586 -33.043 14.652  1.00 31.53 ? 47  ARG B CA  1 
ATOM   365  C  C   . ARG A 1 47  ? -13.930 -32.102 15.770  1.00 29.57 ? 47  ARG B C   1 
ATOM   366  O  O   . ARG A 1 47  ? -14.642 -32.513 16.673  1.00 31.07 ? 47  ARG B O   1 
ATOM   367  C  CB  . ARG A 1 47  ? -14.354 -32.672 13.357  1.00 31.99 ? 47  ARG B CB  1 
ATOM   368  C  CG  . ARG A 1 47  ? -13.917 -33.456 12.086  1.00 32.56 ? 47  ARG B CG  1 
ATOM   369  C  CD  . ARG A 1 47  ? -14.076 -32.581 10.763  1.00 37.30 ? 47  ARG B CD  1 
ATOM   370  N  NE  . ARG A 1 47  ? -13.199 -32.993 9.618   1.00 44.73 ? 47  ARG B NE  1 
ATOM   371  C  CZ  . ARG A 1 47  ? -13.535 -33.867 8.646   1.00 50.38 ? 47  ARG B CZ  1 
ATOM   372  N  NH1 . ARG A 1 47  ? -14.741 -34.436 8.645   1.00 51.96 ? 47  ARG B NH1 1 
ATOM   373  N  NH2 . ARG A 1 47  ? -12.674 -34.173 7.657   1.00 49.58 ? 47  ARG B NH2 1 
ATOM   374  N  N   . PRO A 1 48  ? -13.396 -30.855 15.784  1.00 28.13 ? 48  PRO B N   1 
ATOM   375  C  CA  . PRO A 1 48  ? -13.947 -29.941 16.814  1.00 27.49 ? 48  PRO B CA  1 
ATOM   376  C  C   . PRO A 1 48  ? -15.488 -29.813 16.820  1.00 26.31 ? 48  PRO B C   1 
ATOM   377  O  O   . PRO A 1 48  ? -16.081 -29.747 15.763  1.00 25.65 ? 48  PRO B O   1 
ATOM   378  C  CB  . PRO A 1 48  ? -13.252 -28.602 16.511  1.00 27.79 ? 48  PRO B CB  1 
ATOM   379  C  CG  . PRO A 1 48  ? -11.876 -29.065 15.948  1.00 27.62 ? 48  PRO B CG  1 
ATOM   380  C  CD  . PRO A 1 48  ? -12.286 -30.219 15.029  1.00 28.46 ? 48  PRO B CD  1 
ATOM   381  N  N   . LEU A 1 49  ? -16.095 -29.836 18.010  1.00 24.53 ? 49  LEU B N   1 
ATOM   382  C  CA  . LEU A 1 49  ? -17.543 -29.526 18.208  1.00 24.75 ? 49  LEU B CA  1 
ATOM   383  C  C   . LEU A 1 49  ? -17.740 -28.073 17.891  1.00 23.63 ? 49  LEU B C   1 
ATOM   384  O  O   . LEU A 1 49  ? -16.955 -27.255 18.371  1.00 25.18 ? 49  LEU B O   1 
ATOM   385  C  CB  . LEU A 1 49  ? -17.946 -29.702 19.660  1.00 24.51 ? 49  LEU B CB  1 
ATOM   386  C  CG  . LEU A 1 49  ? -19.377 -30.107 19.966  1.00 26.08 ? 49  LEU B CG  1 
ATOM   387  C  CD1 . LEU A 1 49  ? -19.800 -31.344 19.173  1.00 26.63 ? 49  LEU B CD1 1 
ATOM   388  C  CD2 . LEU A 1 49  ? -19.445 -30.478 21.405  1.00 29.00 ? 49  LEU B CD2 1 
ATOM   389  N  N   . SER A 1 50  ? -18.736 -27.757 17.065  1.00 21.85 ? 50  SER B N   1 
ATOM   390  C  CA  . SER A 1 50  ? -19.001 -26.371 16.613  1.00 20.05 ? 50  SER B CA  1 
ATOM   391  C  C   . SER A 1 50  ? -20.438 -25.967 16.949  1.00 18.92 ? 50  SER B C   1 
ATOM   392  O  O   . SER A 1 50  ? -21.392 -26.626 16.524  1.00 18.15 ? 50  SER B O   1 
ATOM   393  C  CB  . SER A 1 50  ? -18.767 -26.264 15.102  1.00 19.87 ? 50  SER B CB  1 
ATOM   394  O  OG  . SER A 1 50  ? -19.571 -25.216 14.549  1.00 22.18 ? 50  SER B OG  1 
ATOM   395  N  N   . ILE A 1 51  ? -20.609 -24.880 17.721  1.00 18.62 ? 51  ILE B N   1 
ATOM   396  C  CA  . ILE A 1 51  ? -21.926 -24.573 18.245  1.00 17.61 ? 51  ILE B CA  1 
ATOM   397  C  C   . ILE A 1 51  ? -22.216 -23.144 17.896  1.00 16.54 ? 51  ILE B C   1 
ATOM   398  O  O   . ILE A 1 51  ? -21.612 -22.228 18.464  1.00 16.90 ? 51  ILE B O   1 
ATOM   399  C  CB  . ILE A 1 51  ? -22.042 -24.865 19.790  1.00 17.01 ? 51  ILE B CB  1 
ATOM   400  C  CG1 . ILE A 1 51  ? -21.792 -26.365 20.065  1.00 17.24 ? 51  ILE B CG1 1 
ATOM   401  C  CG2 . ILE A 1 51  ? -23.379 -24.413 20.326  1.00 20.19 ? 51  ILE B CG2 1 
ATOM   402  C  CD1 . ILE A 1 51  ? -21.815 -26.756 21.587  1.00 19.08 ? 51  ILE B CD1 1 
ATOM   403  N  N   . LYS A 1 52  ? -23.112 -22.974 16.928  1.00 15.59 ? 52  LYS B N   1 
ATOM   404  C  CA  . LYS A 1 52  ? -23.574 -21.635 16.492  1.00 16.38 ? 52  LYS B CA  1 
ATOM   405  C  C   . LYS A 1 52  ? -25.030 -21.541 16.913  1.00 15.63 ? 52  LYS B C   1 
ATOM   406  O  O   . LYS A 1 52  ? -25.874 -22.160 16.309  1.00 12.67 ? 52  LYS B O   1 
ATOM   407  C  CB  . LYS A 1 52  ? -23.455 -21.415 14.984  1.00 13.59 ? 52  LYS B CB  1 
ATOM   408  C  CG  . LYS A 1 52  ? -23.770 -19.953 14.544  1.00 16.89 ? 52  LYS B CG  1 
ATOM   409  C  CD  . LYS A 1 52  ? -23.437 -19.679 13.104  1.00 18.18 ? 52  LYS B CD  1 
ATOM   410  C  CE  . LYS A 1 52  ? -24.218 -20.563 12.122  1.00 20.33 ? 52  LYS B CE  1 
ATOM   411  N  NZ  . LYS A 1 52  ? -23.786 -20.099 10.812  1.00 23.42 ? 52  LYS B NZ  1 
ATOM   412  N  N   . TYR A 1 53  ? -25.300 -20.696 17.913  1.00 16.84 ? 53  TYR B N   1 
ATOM   413  C  CA  . TYR A 1 53  ? -26.640 -20.543 18.427  1.00 16.97 ? 53  TYR B CA  1 
ATOM   414  C  C   . TYR A 1 53  ? -26.993 -19.048 18.353  1.00 17.49 ? 53  TYR B C   1 
ATOM   415  O  O   . TYR A 1 53  ? -26.267 -18.143 18.819  1.00 15.61 ? 53  TYR B O   1 
ATOM   416  C  CB  . TYR A 1 53  ? -26.786 -21.106 19.878  1.00 19.16 ? 53  TYR B CB  1 
ATOM   417  C  CG  . TYR A 1 53  ? -26.825 -22.642 20.037  1.00 20.07 ? 53  TYR B CG  1 
ATOM   418  C  CD1 . TYR A 1 53  ? -27.094 -23.531 18.940  1.00 17.70 ? 53  TYR B CD1 1 
ATOM   419  C  CD2 . TYR A 1 53  ? -26.589 -23.197 21.282  1.00 19.70 ? 53  TYR B CD2 1 
ATOM   420  C  CE1 . TYR A 1 53  ? -27.106 -24.919 19.111  1.00 22.10 ? 53  TYR B CE1 1 
ATOM   421  C  CE2 . TYR A 1 53  ? -26.619 -24.589 21.469  1.00 24.15 ? 53  TYR B CE2 1 
ATOM   422  C  CZ  . TYR A 1 53  ? -26.872 -25.439 20.391  1.00 22.16 ? 53  TYR B CZ  1 
ATOM   423  O  OH  . TYR A 1 53  ? -26.824 -26.778 20.644  1.00 21.87 ? 53  TYR B OH  1 
ATOM   424  N  N   . ASP A 1 54  ? -28.170 -18.810 17.783  1.00 16.69 ? 54  ASP B N   1 
ATOM   425  C  CA  . ASP A 1 54  ? -28.753 -17.491 17.704  1.00 15.66 ? 54  ASP B CA  1 
ATOM   426  C  C   . ASP A 1 54  ? -29.921 -17.343 18.721  1.00 16.76 ? 54  ASP B C   1 
ATOM   427  O  O   . ASP A 1 54  ? -30.920 -18.051 18.620  1.00 15.68 ? 54  ASP B O   1 
ATOM   428  C  CB  . ASP A 1 54  ? -29.315 -17.357 16.310  1.00 14.81 ? 54  ASP B CB  1 
ATOM   429  C  CG  . ASP A 1 54  ? -29.724 -15.934 15.980  1.00 16.88 ? 54  ASP B CG  1 
ATOM   430  O  OD1 . ASP A 1 54  ? -30.365 -15.272 16.811  1.00 17.29 ? 54  ASP B OD1 1 
ATOM   431  O  OD2 . ASP A 1 54  ? -29.375 -15.494 14.874  1.00 22.67 ? 54  ASP B OD2 1 
ATOM   432  N  N   . PRO A 1 55  ? -29.803 -16.417 19.685  1.00 16.83 ? 55  PRO B N   1 
ATOM   433  C  CA  . PRO A 1 55  ? -30.909 -16.248 20.640  1.00 16.94 ? 55  PRO B CA  1 
ATOM   434  C  C   . PRO A 1 55  ? -32.289 -15.927 20.044  1.00 16.92 ? 55  PRO B C   1 
ATOM   435  O  O   . PRO A 1 55  ? -33.287 -16.308 20.627  1.00 17.84 ? 55  PRO B O   1 
ATOM   436  C  CB  . PRO A 1 55  ? -30.382 -15.114 21.564  1.00 16.45 ? 55  PRO B CB  1 
ATOM   437  C  CG  . PRO A 1 55  ? -28.828 -15.269 21.462  1.00 14.48 ? 55  PRO B CG  1 
ATOM   438  C  CD  . PRO A 1 55  ? -28.662 -15.503 19.991  1.00 15.42 ? 55  PRO B CD  1 
ATOM   439  N  N   . SER A 1 56  ? -32.366 -15.306 18.876  1.00 16.18 ? 56  SER B N   1 
ATOM   440  C  CA  . SER A 1 56  ? -33.673 -15.000 18.283  1.00 17.27 ? 56  SER B CA  1 
ATOM   441  C  C   . SER A 1 56  ? -34.320 -16.236 17.627  1.00 17.77 ? 56  SER B C   1 
ATOM   442  O  O   . SER A 1 56  ? -35.465 -16.169 17.214  1.00 18.31 ? 56  SER B O   1 
ATOM   443  C  CB  . SER A 1 56  ? -33.537 -13.901 17.220  1.00 18.92 ? 56  SER B CB  1 
ATOM   444  O  OG  . SER A 1 56  ? -33.020 -14.448 16.011  1.00 21.11 ? 56  SER B OG  1 
ATOM   445  N  N   . SER A 1 57  ? -33.583 -17.363 17.547  1.00 15.46 ? 57  SER B N   1 
ATOM   446  C  CA  . SER A 1 57  ? -34.146 -18.642 17.130  1.00 15.52 ? 57  SER B CA  1 
ATOM   447  C  C   . SER A 1 57  ? -35.244 -19.161 18.068  1.00 14.62 ? 57  SER B C   1 
ATOM   448  O  O   . SER A 1 57  ? -36.153 -19.875 17.609  1.00 16.41 ? 57  SER B O   1 
ATOM   449  C  CB  . SER A 1 57  ? -33.061 -19.722 17.006  1.00 13.80 ? 57  SER B CB  1 
ATOM   450  O  OG  . SER A 1 57  ? -32.172 -19.418 15.930  1.00 18.58 ? 57  SER B OG  1 
ATOM   451  N  N   . ALA A 1 58  ? -35.135 -18.872 19.361  1.00 14.77 ? 58  ALA B N   1 
ATOM   452  C  CA  . ALA A 1 58  ? -36.097 -19.432 20.361  1.00 16.01 ? 58  ALA B CA  1 
ATOM   453  C  C   . ALA A 1 58  ? -37.476 -18.816 20.109  1.00 17.57 ? 58  ALA B C   1 
ATOM   454  O  O   . ALA A 1 58  ? -37.559 -17.629 19.767  1.00 19.79 ? 58  ALA B O   1 
ATOM   455  C  CB  . ALA A 1 58  ? -35.615 -19.137 21.834  1.00 14.35 ? 58  ALA B CB  1 
ATOM   456  N  N   . LYS A 1 59  ? -38.548 -19.583 20.239  1.00 17.18 ? 59  LYS B N   1 
ATOM   457  C  CA  . LYS A 1 59  ? -39.894 -19.038 19.904  1.00 18.72 ? 59  LYS B CA  1 
ATOM   458  C  C   . LYS A 1 59  ? -40.872 -19.172 21.050  1.00 17.50 ? 59  LYS B C   1 
ATOM   459  O  O   . LYS A 1 59  ? -41.592 -18.220 21.380  1.00 17.48 ? 59  LYS B O   1 
ATOM   460  C  CB  . LYS A 1 59  ? -40.472 -19.684 18.628  1.00 19.34 ? 59  LYS B CB  1 
ATOM   461  C  CG  . LYS A 1 59  ? -39.692 -19.319 17.352  1.00 25.00 ? 59  LYS B CG  1 
ATOM   462  C  CD  . LYS A 1 59  ? -39.380 -17.794 17.258  1.00 27.91 ? 59  LYS B CD  1 
ATOM   463  C  CE  . LYS A 1 59  ? -38.343 -17.440 16.171  1.00 29.94 ? 59  LYS B CE  1 
ATOM   464  N  NZ  . LYS A 1 59  ? -38.256 -15.933 15.986  1.00 30.87 ? 59  LYS B NZ  1 
ATOM   465  N  N   . ILE A 1 60  ? -40.918 -20.352 21.680  1.00 16.59 ? 60  ILE B N   1 
ATOM   466  C  CA  . ILE A 1 60  ? -41.934 -20.620 22.679  1.00 16.99 ? 60  ILE B CA  1 
ATOM   467  C  C   . ILE A 1 60  ? -41.390 -21.524 23.724  1.00 15.84 ? 60  ILE B C   1 
ATOM   468  O  O   . ILE A 1 60  ? -40.459 -22.299 23.462  1.00 14.82 ? 60  ILE B O   1 
ATOM   469  C  CB  . ILE A 1 60  ? -43.354 -21.177 22.098  1.00 17.30 ? 60  ILE B CB  1 
ATOM   470  C  CG1 . ILE A 1 60  ? -43.221 -22.485 21.358  1.00 20.24 ? 60  ILE B CG1 1 
ATOM   471  C  CG2 . ILE A 1 60  ? -44.057 -20.147 21.145  1.00 20.35 ? 60  ILE B CG2 1 
ATOM   472  C  CD1 . ILE A 1 60  ? -44.482 -23.371 21.440  1.00 22.17 ? 60  ILE B CD1 1 
ATOM   473  N  N   . ILE A 1 61  ? -41.983 -21.447 24.904  1.00 14.54 ? 61  ILE B N   1 
ATOM   474  C  CA  . ILE A 1 61  ? -41.764 -22.477 25.902  1.00 14.01 ? 61  ILE B CA  1 
ATOM   475  C  C   . ILE A 1 61  ? -43.152 -22.995 26.208  1.00 15.90 ? 61  ILE B C   1 
ATOM   476  O  O   . ILE A 1 61  ? -44.086 -22.223 26.267  1.00 15.36 ? 61  ILE B O   1 
ATOM   477  C  CB  . ILE A 1 61  ? -41.011 -21.932 27.152  1.00 14.33 ? 61  ILE B CB  1 
ATOM   478  C  CG1 . ILE A 1 61  ? -40.448 -23.077 28.063  1.00 10.98 ? 61  ILE B CG1 1 
ATOM   479  C  CG2 . ILE A 1 61  ? -41.892 -20.961 27.928  1.00 10.51 ? 61  ILE B CG2 1 
ATOM   480  C  CD1 . ILE A 1 61  ? -39.546 -22.526 29.272  1.00 12.77 ? 61  ILE B CD1 1 
ATOM   481  N  N   . SER A 1 62  ? -43.266 -24.316 26.413  1.00 16.16 ? 62  SER B N   1 
ATOM   482  C  CA  . SER A 1 62  ? -44.528 -24.936 26.706  1.00 16.80 ? 62  SER B CA  1 
ATOM   483  C  C   . SER A 1 62  ? -44.312 -26.084 27.708  1.00 16.40 ? 62  SER B C   1 
ATOM   484  O  O   . SER A 1 62  ? -43.172 -26.576 27.924  1.00 15.08 ? 62  SER B O   1 
ATOM   485  C  CB  . SER A 1 62  ? -45.151 -25.506 25.399  1.00 17.03 ? 62  SER B CB  1 
ATOM   486  O  OG  . SER A 1 62  ? -44.309 -26.546 24.876  1.00 20.46 ? 62  SER B OG  1 
ATOM   487  N  N   . ASN A 1 63  ? -45.413 -26.493 28.306  1.00 14.50 ? 63  ASN B N   1 
ATOM   488  C  CA  . ASN A 1 63  ? -45.448 -27.678 29.128  1.00 16.48 ? 63  ASN B CA  1 
ATOM   489  C  C   . ASN A 1 63  ? -46.020 -28.872 28.286  1.00 15.81 ? 63  ASN B C   1 
ATOM   490  O  O   . ASN A 1 63  ? -47.191 -28.928 28.014  1.00 15.73 ? 63  ASN B O   1 
ATOM   491  C  CB  . ASN A 1 63  ? -46.258 -27.424 30.439  1.00 15.78 ? 63  ASN B CB  1 
ATOM   492  C  CG  . ASN A 1 63  ? -46.313 -28.666 31.364  1.00 16.10 ? 63  ASN B CG  1 
ATOM   493  O  OD1 . ASN A 1 63  ? -45.942 -29.759 30.970  1.00 17.14 ? 63  ASN B OD1 1 
ATOM   494  N  ND2 . ASN A 1 63  ? -46.730 -28.469 32.601  1.00 16.93 ? 63  ASN B ND2 1 
ATOM   495  N  N   . SER A 1 64  ? -45.157 -29.842 27.950  1.00 16.24 ? 64  SER B N   1 
ATOM   496  C  CA  . SER A 1 64  ? -45.543 -31.044 27.188  1.00 15.48 ? 64  SER B CA  1 
ATOM   497  C  C   . SER A 1 64  ? -46.258 -32.051 28.104  1.00 15.70 ? 64  SER B C   1 
ATOM   498  O  O   . SER A 1 64  ? -46.812 -33.054 27.643  1.00 16.05 ? 64  SER B O   1 
ATOM   499  C  CB  . SER A 1 64  ? -44.277 -31.703 26.601  1.00 14.87 ? 64  SER B CB  1 
ATOM   500  O  OG  . SER A 1 64  ? -43.493 -32.294 27.615  1.00 11.59 ? 64  SER B OG  1 
ATOM   501  N  N   . GLY A 1 65  ? -46.229 -31.818 29.412  1.00 14.95 ? 65  GLY B N   1 
ATOM   502  C  CA  . GLY A 1 65  ? -46.679 -32.854 30.395  1.00 16.40 ? 65  GLY B CA  1 
ATOM   503  C  C   . GLY A 1 65  ? -45.569 -33.774 30.854  1.00 15.34 ? 65  GLY B C   1 
ATOM   504  O  O   . GLY A 1 65  ? -45.725 -34.516 31.821  1.00 16.20 ? 65  GLY B O   1 
ATOM   505  N  N   . HIS A 1 66  ? -44.426 -33.737 30.141  1.00 13.84 ? 66  HIS B N   1 
ATOM   506  C  CA  . HIS A 1 66  ? -43.265 -34.627 30.411  1.00 12.41 ? 66  HIS B CA  1 
ATOM   507  C  C   . HIS A 1 66  ? -41.995 -33.805 30.796  1.00 11.78 ? 66  HIS B C   1 
ATOM   508  O  O   . HIS A 1 66  ? -41.096 -34.347 31.419  1.00 11.78 ? 66  HIS B O   1 
ATOM   509  C  CB  . HIS A 1 66  ? -42.936 -35.446 29.183  1.00 12.44 ? 66  HIS B CB  1 
ATOM   510  C  CG  . HIS A 1 66  ? -44.139 -36.018 28.521  1.00 17.49 ? 66  HIS B CG  1 
ATOM   511  N  ND1 . HIS A 1 66  ? -44.985 -36.894 29.180  1.00 18.39 ? 66  HIS B ND1 1 
ATOM   512  C  CD2 . HIS A 1 66  ? -44.621 -35.884 27.259  1.00 18.52 ? 66  HIS B CD2 1 
ATOM   513  C  CE1 . HIS A 1 66  ? -45.940 -37.268 28.341  1.00 20.77 ? 66  HIS B CE1 1 
ATOM   514  N  NE2 . HIS A 1 66  ? -45.743 -36.668 27.180  1.00 20.16 ? 66  HIS B NE2 1 
ATOM   515  N  N   . SER A 1 67  ? -42.012 -32.521 30.443  1.00 11.78 ? 67  SER B N   1 
ATOM   516  C  CA  . SER A 1 67  ? -40.977 -31.532 30.733  1.00 13.20 ? 67  SER B CA  1 
ATOM   517  C  C   . SER A 1 67  ? -41.458 -30.192 30.264  1.00 13.75 ? 67  SER B C   1 
ATOM   518  O  O   . SER A 1 67  ? -42.575 -30.044 29.796  1.00 12.77 ? 67  SER B O   1 
ATOM   519  C  CB  . SER A 1 67  ? -39.634 -31.856 30.042  1.00 12.33 ? 67  SER B CB  1 
ATOM   520  O  OG  . SER A 1 67  ? -38.557 -30.997 30.494  1.00 14.16 ? 67  SER B OG  1 
ATOM   521  N  N   . PHE A 1 68  ? -40.650 -29.159 30.467  1.00 12.42 ? 68  PHE B N   1 
ATOM   522  C  CA  . PHE A 1 68  ? -40.884 -27.977 29.656  1.00 12.70 ? 68  PHE B CA  1 
ATOM   523  C  C   . PHE A 1 68  ? -40.153 -28.193 28.312  1.00 12.09 ? 68  PHE B C   1 
ATOM   524  O  O   . PHE A 1 68  ? -39.097 -28.836 28.274  1.00 12.12 ? 68  PHE B O   1 
ATOM   525  C  CB  . PHE A 1 68  ? -40.351 -26.683 30.335  1.00 11.07 ? 68  PHE B CB  1 
ATOM   526  C  CG  . PHE A 1 68  ? -38.884 -26.628 30.431  1.00 15.07 ? 68  PHE B CG  1 
ATOM   527  C  CD1 . PHE A 1 68  ? -38.250 -27.079 31.593  1.00 16.23 ? 68  PHE B CD1 1 
ATOM   528  C  CD2 . PHE A 1 68  ? -38.081 -26.113 29.343  1.00 14.28 ? 68  PHE B CD2 1 
ATOM   529  C  CE1 . PHE A 1 68  ? -36.824 -27.038 31.697  1.00 13.96 ? 68  PHE B CE1 1 
ATOM   530  C  CE2 . PHE A 1 68  ? -36.670 -26.099 29.421  1.00 15.89 ? 68  PHE B CE2 1 
ATOM   531  C  CZ  . PHE A 1 68  ? -36.038 -26.569 30.577  1.00 14.74 ? 68  PHE B CZ  1 
ATOM   532  N  N   . ASN A 1 69  ? -40.665 -27.596 27.242  1.00 12.68 ? 69  ASN B N   1 
ATOM   533  C  CA  . ASN A 1 69  ? -39.966 -27.653 25.926  1.00 12.66 ? 69  ASN B CA  1 
ATOM   534  C  C   . ASN A 1 69  ? -39.786 -26.219 25.437  1.00 12.95 ? 69  ASN B C   1 
ATOM   535  O  O   . ASN A 1 69  ? -40.747 -25.484 25.299  1.00 13.62 ? 69  ASN B O   1 
ATOM   536  C  CB  . ASN A 1 69  ? -40.739 -28.350 24.783  1.00 10.24 ? 69  ASN B CB  1 
ATOM   537  C  CG  . ASN A 1 69  ? -40.908 -29.839 24.956  1.00 13.37 ? 69  ASN B CG  1 
ATOM   538  O  OD1 . ASN A 1 69  ? -40.098 -30.558 25.590  1.00 14.45 ? 69  ASN B OD1 1 
ATOM   539  N  ND2 . ASN A 1 69  ? -41.925 -30.348 24.271  1.00 16.18 ? 69  ASN B ND2 1 
ATOM   540  N  N   . VAL A 1 70  ? -38.543 -25.837 25.140  1.00 12.72 ? 70  VAL B N   1 
ATOM   541  C  CA  . VAL A 1 70  ? -38.297 -24.566 24.421  1.00 13.31 ? 70  VAL B CA  1 
ATOM   542  C  C   . VAL A 1 70  ? -38.176 -24.979 22.973  1.00 14.37 ? 70  VAL B C   1 
ATOM   543  O  O   . VAL A 1 70  ? -37.343 -25.823 22.657  1.00 13.06 ? 70  VAL B O   1 
ATOM   544  C  CB  . VAL A 1 70  ? -37.025 -23.920 24.863  1.00 14.84 ? 70  VAL B CB  1 
ATOM   545  C  CG1 . VAL A 1 70  ? -36.769 -22.634 24.024  1.00 10.99 ? 70  VAL B CG1 1 
ATOM   546  C  CG2 . VAL A 1 70  ? -37.123 -23.601 26.373  1.00 11.33 ? 70  VAL B CG2 1 
ATOM   547  N  N   . ASP A 1 71  ? -39.037 -24.416 22.129  1.00 13.41 ? 71  ASP B N   1 
ATOM   548  C  CA  . ASP A 1 71  ? -39.013 -24.713 20.694  1.00 15.93 ? 71  ASP B CA  1 
ATOM   549  C  C   . ASP A 1 71  ? -38.396 -23.535 19.923  1.00 16.05 ? 71  ASP B C   1 
ATOM   550  O  O   . ASP A 1 71  ? -38.551 -22.356 20.286  1.00 15.09 ? 71  ASP B O   1 
ATOM   551  C  CB  . ASP A 1 71  ? -40.386 -25.045 20.133  1.00 16.93 ? 71  ASP B CB  1 
ATOM   552  C  CG  . ASP A 1 71  ? -40.954 -26.317 20.710  1.00 18.25 ? 71  ASP B CG  1 
ATOM   553  O  OD1 . ASP A 1 71  ? -40.224 -27.293 20.799  1.00 21.03 ? 71  ASP B OD1 1 
ATOM   554  O  OD2 . ASP A 1 71  ? -42.141 -26.345 21.080  1.00 23.83 ? 71  ASP B OD2 1 
ATOM   555  N  N   . PHE A 1 72  ? -37.687 -23.921 18.865  1.00 15.23 ? 72  PHE B N   1 
ATOM   556  C  CA  . PHE A 1 72  ? -36.847 -23.008 18.115  1.00 15.25 ? 72  PHE B CA  1 
ATOM   557  C  C   . PHE A 1 72  ? -37.320 -23.036 16.667  1.00 16.25 ? 72  PHE B C   1 
ATOM   558  O  O   . PHE A 1 72  ? -37.921 -23.986 16.185  1.00 15.36 ? 72  PHE B O   1 
ATOM   559  C  CB  . PHE A 1 72  ? -35.382 -23.381 18.180  1.00 13.08 ? 72  PHE B CB  1 
ATOM   560  C  CG  . PHE A 1 72  ? -34.778 -23.236 19.573  1.00 14.85 ? 72  PHE B CG  1 
ATOM   561  C  CD1 . PHE A 1 72  ? -34.888 -24.276 20.512  1.00 11.15 ? 72  PHE B CD1 1 
ATOM   562  C  CD2 . PHE A 1 72  ? -34.086 -22.072 19.921  1.00 14.70 ? 72  PHE B CD2 1 
ATOM   563  C  CE1 . PHE A 1 72  ? -34.296 -24.142 21.765  1.00 11.29 ? 72  PHE B CE1 1 
ATOM   564  C  CE2 . PHE A 1 72  ? -33.511 -21.939 21.186  1.00 13.59 ? 72  PHE B CE2 1 
ATOM   565  C  CZ  . PHE A 1 72  ? -33.644 -22.969 22.100  1.00 11.84 ? 72  PHE B CZ  1 
ATOM   566  N  N   . ASP A 1 73  ? -37.098 -21.932 16.030  1.00 18.55 ? 73  ASP B N   1 
ATOM   567  C  CA  . ASP A 1 73  ? -37.496 -21.821 14.661  1.00 22.64 ? 73  ASP B CA  1 
ATOM   568  C  C   . ASP A 1 73  ? -36.444 -22.633 13.983  1.00 23.01 ? 73  ASP B C   1 
ATOM   569  O  O   . ASP A 1 73  ? -35.259 -22.299 14.087  1.00 25.58 ? 73  ASP B O   1 
ATOM   570  C  CB  . ASP A 1 73  ? -37.445 -20.351 14.193  1.00 23.30 ? 73  ASP B CB  1 
ATOM   571  C  CG  . ASP A 1 73  ? -37.581 -20.257 12.673  1.00 26.90 ? 73  ASP B CG  1 
ATOM   572  O  OD1 . ASP A 1 73  ? -37.020 -21.151 12.024  1.00 29.24 ? 73  ASP B OD1 1 
ATOM   573  O  OD2 . ASP A 1 73  ? -38.233 -19.332 12.123  1.00 33.28 ? 73  ASP B OD2 1 
ATOM   574  N  N   . ASP A 1 74  ? -36.819 -23.729 13.332  1.00 23.45 ? 74  ASP B N   1 
ATOM   575  C  CA  . ASP A 1 74  ? -35.812 -24.570 12.715  1.00 23.91 ? 74  ASP B CA  1 
ATOM   576  C  C   . ASP A 1 74  ? -36.117 -24.704 11.138  1.00 24.90 ? 74  ASP B C   1 
ATOM   577  O  O   . ASP A 1 74  ? -36.212 -25.815 10.580  1.00 23.79 ? 74  ASP B O   1 
ATOM   578  C  CB  . ASP A 1 74  ? -35.815 -25.949 13.388  1.00 25.48 ? 74  ASP B CB  1 
ATOM   579  C  CG  . ASP A 1 74  ? -37.136 -26.703 13.160  1.00 24.64 ? 74  ASP B CG  1 
ATOM   580  O  OD1 . ASP A 1 74  ? -38.147 -26.096 12.641  1.00 26.46 ? 74  ASP B OD1 1 
ATOM   581  O  OD2 . ASP A 1 74  ? -37.144 -27.912 13.453  1.00 29.54 ? 74  ASP B OD2 1 
ATOM   582  N  N   . THR A 1 75  ? -36.357 -23.583 10.444  1.00 24.87 ? 75  THR B N   1 
ATOM   583  C  CA  . THR A 1 75  ? -36.338 -23.677 8.947   1.00 24.34 ? 75  THR B CA  1 
ATOM   584  C  C   . THR A 1 75  ? -35.136 -22.970 8.387   1.00 22.89 ? 75  THR B C   1 
ATOM   585  O  O   . THR A 1 75  ? -34.983 -22.848 7.166   1.00 21.01 ? 75  THR B O   1 
ATOM   586  C  CB  . THR A 1 75  ? -37.668 -23.283 8.190   1.00 26.09 ? 75  THR B CB  1 
ATOM   587  O  OG1 . THR A 1 75  ? -38.357 -22.219 8.886   1.00 31.76 ? 75  THR B OG1 1 
ATOM   588  C  CG2 . THR A 1 75  ? -38.609 -24.588 7.925   1.00 28.79 ? 75  THR B CG2 1 
ATOM   589  N  N   . GLU A 1 76  ? -34.290 -22.481 9.283   1.00 20.33 ? 76  GLU B N   1 
ATOM   590  C  CA  . GLU A 1 76  ? -33.053 -21.859 8.890   1.00 22.25 ? 76  GLU B CA  1 
ATOM   591  C  C   . GLU A 1 76  ? -31.874 -22.489 9.623   1.00 18.89 ? 76  GLU B C   1 
ATOM   592  O  O   . GLU A 1 76  ? -32.049 -23.191 10.634  1.00 16.03 ? 76  GLU B O   1 
ATOM   593  C  CB  . GLU A 1 76  ? -33.103 -20.364 9.248   1.00 22.95 ? 76  GLU B CB  1 
ATOM   594  C  CG  . GLU A 1 76  ? -33.458 -19.391 8.095   1.00 29.19 ? 76  GLU B CG  1 
ATOM   595  C  CD  . GLU A 1 76  ? -33.281 -17.928 8.547   1.00 28.42 ? 76  GLU B CD  1 
ATOM   596  O  OE1 . GLU A 1 76  ? -33.917 -17.551 9.560   1.00 40.48 ? 76  GLU B OE1 1 
ATOM   597  O  OE2 . GLU A 1 76  ? -32.483 -17.188 7.943   1.00 37.31 ? 76  GLU B OE2 1 
ATOM   598  N  N   . ASN A 1 77  ? -30.673 -22.219 9.130   1.00 17.65 ? 77  ASN B N   1 
ATOM   599  C  CA  . ASN A 1 77  ? -29.462 -22.677 9.780   1.00 17.25 ? 77  ASN B CA  1 
ATOM   600  C  C   . ASN A 1 77  ? -28.828 -21.601 10.677  1.00 17.48 ? 77  ASN B C   1 
ATOM   601  O  O   . ASN A 1 77  ? -27.620 -21.493 10.742  1.00 15.77 ? 77  ASN B O   1 
ATOM   602  C  CB  . ASN A 1 77  ? -28.489 -23.284 8.731   1.00 17.93 ? 77  ASN B CB  1 
ATOM   603  C  CG  . ASN A 1 77  ? -28.948 -24.630 8.266   1.00 16.58 ? 77  ASN B CG  1 
ATOM   604  O  OD1 . ASN A 1 77  ? -29.755 -25.274 8.973   1.00 16.43 ? 77  ASN B OD1 1 
ATOM   605  N  ND2 . ASN A 1 77  ? -28.412 -25.116 7.122   1.00 13.25 ? 77  ASN B ND2 1 
ATOM   606  N  N   . LYS A 1 78  ? -29.667 -20.819 11.383  1.00 16.14 ? 78  LYS B N   1 
ATOM   607  C  CA  . LYS A 1 78  ? -29.105 -19.785 12.282  1.00 17.57 ? 78  LYS B CA  1 
ATOM   608  C  C   . LYS A 1 78  ? -28.498 -20.455 13.539  1.00 16.14 ? 78  LYS B C   1 
ATOM   609  O  O   . LYS A 1 78  ? -27.512 -19.949 14.095  1.00 14.62 ? 78  LYS B O   1 
ATOM   610  C  CB  . LYS A 1 78  ? -30.152 -18.733 12.672  1.00 16.87 ? 78  LYS B CB  1 
ATOM   611  C  CG  . LYS A 1 78  ? -30.508 -17.774 11.470  1.00 19.97 ? 78  LYS B CG  1 
ATOM   612  C  CD  . LYS A 1 78  ? -31.570 -16.700 11.878  1.00 22.07 ? 78  LYS B CD  1 
ATOM   613  C  CE  . LYS A 1 78  ? -31.669 -15.575 10.791  1.00 25.55 ? 78  LYS B CE  1 
ATOM   614  N  NZ  . LYS A 1 78  ? -32.250 -14.303 11.323  1.00 33.81 ? 78  LYS B NZ  1 
ATOM   615  N  N   . SER A 1 79  ? -29.074 -21.603 13.939  1.00 14.74 ? 79  SER B N   1 
ATOM   616  C  CA  . SER A 1 79  ? -28.651 -22.292 15.186  1.00 13.11 ? 79  SER B CA  1 
ATOM   617  C  C   . SER A 1 79  ? -28.441 -23.742 14.843  1.00 13.86 ? 79  SER B C   1 
ATOM   618  O  O   . SER A 1 79  ? -29.442 -24.450 14.590  1.00 14.15 ? 79  SER B O   1 
ATOM   619  C  CB  . SER A 1 79  ? -29.781 -22.217 16.231  1.00 13.26 ? 79  SER B CB  1 
ATOM   620  O  OG  . SER A 1 79  ? -30.054 -20.900 16.649  1.00 12.91 ? 79  SER B OG  1 
ATOM   621  N  N   . VAL A 1 80  ? -27.172 -24.156 14.775  1.00 12.71 ? 80  VAL B N   1 
ATOM   622  C  CA  . VAL A 1 80  ? -26.788 -25.456 14.260  1.00 13.07 ? 80  VAL B CA  1 
ATOM   623  C  C   . VAL A 1 80  ? -25.602 -25.995 15.064  1.00 13.63 ? 80  VAL B C   1 
ATOM   624  O  O   . VAL A 1 80  ? -24.794 -25.231 15.599  1.00 14.52 ? 80  VAL B O   1 
ATOM   625  C  CB  . VAL A 1 80  ? -26.394 -25.401 12.756  1.00 12.97 ? 80  VAL B CB  1 
ATOM   626  C  CG1 . VAL A 1 80  ? -27.596 -25.009 11.923  1.00 12.00 ? 80  VAL B CG1 1 
ATOM   627  C  CG2 . VAL A 1 80  ? -25.196 -24.321 12.540  1.00 14.20 ? 80  VAL B CG2 1 
ATOM   628  N  N   . LEU A 1 81  ? -25.549 -27.316 15.133  1.00 13.20 ? 81  LEU B N   1 
ATOM   629  C  CA  . LEU A 1 81  ? -24.530 -28.070 15.813  1.00 14.58 ? 81  LEU B CA  1 
ATOM   630  C  C   . LEU A 1 81  ? -23.836 -28.813 14.679  1.00 15.92 ? 81  LEU B C   1 
ATOM   631  O  O   . LEU A 1 81  ? -24.492 -29.457 13.850  1.00 14.94 ? 81  LEU B O   1 
ATOM   632  C  CB  . LEU A 1 81  ? -25.168 -29.084 16.797  1.00 15.05 ? 81  LEU B CB  1 
ATOM   633  C  CG  . LEU A 1 81  ? -24.150 -30.029 17.454  1.00 14.53 ? 81  LEU B CG  1 
ATOM   634  C  CD1 . LEU A 1 81  ? -23.193 -29.167 18.294  1.00 13.68 ? 81  LEU B CD1 1 
ATOM   635  C  CD2 . LEU A 1 81  ? -24.925 -31.094 18.253  1.00 15.87 ? 81  LEU B CD2 1 
ATOM   636  N  N   . ARG A 1 82  ? -22.514 -28.660 14.617  1.00 15.45 ? 82  ARG B N   1 
ATOM   637  C  CA  . ARG A 1 82  ? -21.698 -29.375 13.606  1.00 15.56 ? 82  ARG B CA  1 
ATOM   638  C  C   . ARG A 1 82  ? -20.492 -29.908 14.325  1.00 14.54 ? 82  ARG B C   1 
ATOM   639  O  O   . ARG A 1 82  ? -20.281 -29.588 15.486  1.00 16.28 ? 82  ARG B O   1 
ATOM   640  C  CB  . ARG A 1 82  ? -21.286 -28.387 12.505  1.00 14.54 ? 82  ARG B CB  1 
ATOM   641  C  CG  . ARG A 1 82  ? -22.477 -27.923 11.626  1.00 17.05 ? 82  ARG B CG  1 
ATOM   642  C  CD  . ARG A 1 82  ? -22.131 -26.651 10.759  1.00 14.52 ? 82  ARG B CD  1 
ATOM   643  N  NE  . ARG A 1 82  ? -22.082 -25.432 11.579  1.00 21.27 ? 82  ARG B NE  1 
ATOM   644  C  CZ  . ARG A 1 82  ? -21.807 -24.204 11.131  1.00 22.63 ? 82  ARG B CZ  1 
ATOM   645  N  NH1 . ARG A 1 82  ? -21.586 -24.018 9.836   1.00 17.65 ? 82  ARG B NH1 1 
ATOM   646  N  NH2 . ARG A 1 82  ? -21.762 -23.158 11.970  1.00 16.48 ? 82  ARG B NH2 1 
ATOM   647  N  N   . GLY A 1 83  ? -19.716 -30.731 13.663  1.00 17.90 ? 83  GLY B N   1 
ATOM   648  C  CA  . GLY A 1 83  ? -18.445 -31.202 14.198  1.00 16.88 ? 83  GLY B CA  1 
ATOM   649  C  C   . GLY A 1 83  ? -18.660 -32.388 15.121  1.00 17.85 ? 83  GLY B C   1 
ATOM   650  O  O   . GLY A 1 83  ? -19.677 -33.089 15.051  1.00 15.23 ? 83  GLY B O   1 
ATOM   651  N  N   . GLY A 1 84  ? -17.732 -32.550 16.064  1.00 17.96 ? 84  GLY B N   1 
ATOM   652  C  CA  . GLY A 1 84  ? -17.678 -33.714 16.908  1.00 19.30 ? 84  GLY B CA  1 
ATOM   653  C  C   . GLY A 1 84  ? -17.804 -34.993 16.075  1.00 18.53 ? 84  GLY B C   1 
ATOM   654  O  O   . GLY A 1 84  ? -17.074 -35.189 15.126  1.00 22.61 ? 84  GLY B O   1 
ATOM   655  N  N   . PRO A 1 85  ? -18.766 -35.866 16.409  1.00 17.55 ? 85  PRO B N   1 
ATOM   656  C  CA  . PRO A 1 85  ? -18.981 -37.085 15.665  1.00 16.79 ? 85  PRO B CA  1 
ATOM   657  C  C   . PRO A 1 85  ? -19.886 -36.914 14.457  1.00 16.45 ? 85  PRO B C   1 
ATOM   658  O  O   . PRO A 1 85  ? -20.089 -37.908 13.746  1.00 17.84 ? 85  PRO B O   1 
ATOM   659  C  CB  . PRO A 1 85  ? -19.722 -37.994 16.657  1.00 17.05 ? 85  PRO B CB  1 
ATOM   660  C  CG  . PRO A 1 85  ? -20.649 -36.933 17.414  1.00 18.66 ? 85  PRO B CG  1 
ATOM   661  C  CD  . PRO A 1 85  ? -19.716 -35.697 17.529  1.00 16.89 ? 85  PRO B CD  1 
ATOM   662  N  N   . LEU A 1 86  ? -20.324 -35.679 14.156  1.00 14.64 ? 86  LEU B N   1 
ATOM   663  C  CA  . LEU A 1 86  ? -21.437 -35.525 13.222  1.00 15.85 ? 86  LEU B CA  1 
ATOM   664  C  C   . LEU A 1 86  ? -20.984 -35.316 11.789  1.00 16.91 ? 86  LEU B C   1 
ATOM   665  O  O   . LEU A 1 86  ? -20.072 -34.558 11.545  1.00 18.18 ? 86  LEU B O   1 
ATOM   666  C  CB  . LEU A 1 86  ? -22.268 -34.293 13.610  1.00 13.41 ? 86  LEU B CB  1 
ATOM   667  C  CG  . LEU A 1 86  ? -22.931 -34.378 15.017  1.00 15.04 ? 86  LEU B CG  1 
ATOM   668  C  CD1 . LEU A 1 86  ? -23.631 -33.091 15.319  1.00 12.25 ? 86  LEU B CD1 1 
ATOM   669  C  CD2 . LEU A 1 86  ? -23.882 -35.684 15.164  1.00 10.79 ? 86  LEU B CD2 1 
ATOM   670  N  N   . THR A 1 87  ? -21.691 -35.930 10.855  1.00 18.00 ? 87  THR B N   1 
ATOM   671  C  CA  . THR A 1 87  ? -21.544 -35.595 9.452   1.00 18.01 ? 87  THR B CA  1 
ATOM   672  C  C   . THR A 1 87  ? -22.659 -34.612 9.091   1.00 17.48 ? 87  THR B C   1 
ATOM   673  O  O   . THR A 1 87  ? -23.849 -34.945 9.233   1.00 19.88 ? 87  THR B O   1 
ATOM   674  C  CB  . THR A 1 87  ? -21.675 -36.888 8.596   1.00 18.45 ? 87  THR B CB  1 
ATOM   675  O  OG1 . THR A 1 87  ? -20.622 -37.782 8.983   1.00 19.58 ? 87  THR B OG1 1 
ATOM   676  C  CG2 . THR A 1 87  ? -21.616 -36.597 7.010   1.00 18.06 ? 87  THR B CG2 1 
ATOM   677  N  N   . GLY A 1 88  ? -22.268 -33.432 8.627   1.00 16.90 ? 88  GLY B N   1 
ATOM   678  C  CA  . GLY A 1 88  ? -23.189 -32.379 8.188   1.00 17.87 ? 88  GLY B CA  1 
ATOM   679  C  C   . GLY A 1 88  ? -23.771 -31.525 9.343   1.00 17.95 ? 88  GLY B C   1 
ATOM   680  O  O   . GLY A 1 88  ? -23.305 -31.583 10.484  1.00 18.54 ? 88  GLY B O   1 
ATOM   681  N  N   . SER A 1 89  ? -24.808 -30.764 9.013   1.00 16.29 ? 89  SER B N   1 
ATOM   682  C  CA  . SER A 1 89  ? -25.375 -29.770 9.895   1.00 16.18 ? 89  SER B CA  1 
ATOM   683  C  C   . SER A 1 89  ? -26.711 -30.294 10.544  1.00 14.90 ? 89  SER B C   1 
ATOM   684  O  O   . SER A 1 89  ? -27.659 -30.670 9.895   1.00 15.04 ? 89  SER B O   1 
ATOM   685  C  CB  . SER A 1 89  ? -25.570 -28.450 9.155   1.00 14.47 ? 89  SER B CB  1 
ATOM   686  O  OG  . SER A 1 89  ? -26.051 -27.413 9.995   1.00 14.59 ? 89  SER B OG  1 
ATOM   687  N  N   . TYR A 1 90  ? -26.725 -30.223 11.858  1.00 14.81 ? 90  TYR B N   1 
ATOM   688  C  CA  . TYR A 1 90  ? -27.855 -30.582 12.642  1.00 13.05 ? 90  TYR B CA  1 
ATOM   689  C  C   . TYR A 1 90  ? -28.453 -29.311 13.238  1.00 12.57 ? 90  TYR B C   1 
ATOM   690  O  O   . TYR A 1 90  ? -27.846 -28.561 14.032  1.00 12.66 ? 90  TYR B O   1 
ATOM   691  C  CB  . TYR A 1 90  ? -27.392 -31.554 13.726  1.00 12.38 ? 90  TYR B CB  1 
ATOM   692  C  CG  . TYR A 1 90  ? -27.130 -32.929 13.194  1.00 13.06 ? 90  TYR B CG  1 
ATOM   693  C  CD1 . TYR A 1 90  ? -25.977 -33.193 12.378  1.00 12.23 ? 90  TYR B CD1 1 
ATOM   694  C  CD2 . TYR A 1 90  ? -28.015 -33.975 13.466  1.00 11.22 ? 90  TYR B CD2 1 
ATOM   695  C  CE1 . TYR A 1 90  ? -25.740 -34.477 11.870  1.00 11.04 ? 90  TYR B CE1 1 
ATOM   696  C  CE2 . TYR A 1 90  ? -27.755 -35.280 12.963  1.00 12.06 ? 90  TYR B CE2 1 
ATOM   697  C  CZ  . TYR A 1 90  ? -26.636 -35.500 12.168  1.00 10.57 ? 90  TYR B CZ  1 
ATOM   698  O  OH  . TYR A 1 90  ? -26.414 -36.779 11.665  1.00 14.45 ? 90  TYR B OH  1 
ATOM   699  N  N   . ARG A 1 91  ? -29.688 -29.101 12.878  1.00 11.93 ? 91  ARG B N   1 
ATOM   700  C  CA  . ARG A 1 91  ? -30.379 -27.880 13.191  1.00 12.70 ? 91  ARG B CA  1 
ATOM   701  C  C   . ARG A 1 91  ? -31.029 -27.916 14.588  1.00 11.79 ? 91  ARG B C   1 
ATOM   702  O  O   . ARG A 1 91  ? -31.765 -28.826 14.904  1.00 12.29 ? 91  ARG B O   1 
ATOM   703  C  CB  . ARG A 1 91  ? -31.503 -27.663 12.181  1.00 12.79 ? 91  ARG B CB  1 
ATOM   704  C  CG  . ARG A 1 91  ? -32.105 -26.221 12.218  1.00 13.99 ? 91  ARG B CG  1 
ATOM   705  C  CD  . ARG A 1 91  ? -33.129 -26.079 11.127  1.00 11.85 ? 91  ARG B CD  1 
ATOM   706  N  NE  . ARG A 1 91  ? -32.442 -26.038 9.864   1.00 15.46 ? 91  ARG B NE  1 
ATOM   707  C  CZ  . ARG A 1 91  ? -32.985 -26.279 8.655   1.00 16.84 ? 91  ARG B CZ  1 
ATOM   708  N  NH1 . ARG A 1 91  ? -34.270 -26.583 8.541   1.00 16.03 ? 91  ARG B NH1 1 
ATOM   709  N  NH2 . ARG A 1 91  ? -32.209 -26.237 7.561   1.00 8.51  ? 91  ARG B NH2 1 
ATOM   710  N  N   . LEU A 1 92  ? -30.857 -26.865 15.371  1.00 12.41 ? 92  LEU B N   1 
ATOM   711  C  CA  . LEU A 1 92  ? -31.490 -26.864 16.708  1.00 10.66 ? 92  LEU B CA  1 
ATOM   712  C  C   . LEU A 1 92  ? -33.004 -26.908 16.592  1.00 12.98 ? 92  LEU B C   1 
ATOM   713  O  O   . LEU A 1 92  ? -33.585 -26.183 15.819  1.00 13.21 ? 92  LEU B O   1 
ATOM   714  C  CB  . LEU A 1 92  ? -31.042 -25.623 17.483  1.00 11.41 ? 92  LEU B CB  1 
ATOM   715  C  CG  . LEU A 1 92  ? -31.644 -25.340 18.831  1.00 10.35 ? 92  LEU B CG  1 
ATOM   716  C  CD1 . LEU A 1 92  ? -31.208 -26.481 19.762  1.00 8.06  ? 92  LEU B CD1 1 
ATOM   717  C  CD2 . LEU A 1 92  ? -31.165 -23.930 19.321  1.00 10.46 ? 92  LEU B CD2 1 
ATOM   718  N  N   . ARG A 1 93  ? -33.636 -27.801 17.356  1.00 12.70 ? 93  ARG B N   1 
ATOM   719  C  CA  . ARG A 1 93  ? -35.065 -27.988 17.372  1.00 12.72 ? 93  ARG B CA  1 
ATOM   720  C  C   . ARG A 1 93  ? -35.625 -27.564 18.725  1.00 12.49 ? 93  ARG B C   1 
ATOM   721  O  O   . ARG A 1 93  ? -36.595 -26.823 18.800  1.00 13.17 ? 93  ARG B O   1 
ATOM   722  C  CB  . ARG A 1 93  ? -35.363 -29.478 17.080  1.00 14.02 ? 93  ARG B CB  1 
ATOM   723  C  CG  . ARG A 1 93  ? -36.820 -29.899 17.302  1.00 16.75 ? 93  ARG B CG  1 
ATOM   724  C  CD  . ARG A 1 93  ? -37.761 -29.147 16.348  1.00 18.28 ? 93  ARG B CD  1 
ATOM   725  N  NE  . ARG A 1 93  ? -39.063 -29.809 16.377  1.00 22.13 ? 93  ARG B NE  1 
ATOM   726  C  CZ  . ARG A 1 93  ? -40.019 -29.671 15.449  1.00 30.98 ? 93  ARG B CZ  1 
ATOM   727  N  NH1 . ARG A 1 93  ? -39.835 -28.856 14.400  1.00 30.57 ? 93  ARG B NH1 1 
ATOM   728  N  NH2 . ARG A 1 93  ? -41.164 -30.368 15.552  1.00 30.44 ? 93  ARG B NH2 1 
ATOM   729  N  N   . GLN A 1 94  ? -35.071 -28.103 19.808  1.00 12.38 ? 94  GLN B N   1 
ATOM   730  C  CA  . GLN A 1 94  ? -35.674 -27.854 21.080  1.00 11.30 ? 94  GLN B CA  1 
ATOM   731  C  C   . GLN A 1 94  ? -34.779 -28.155 22.265  1.00 11.54 ? 94  GLN B C   1 
ATOM   732  O  O   . GLN A 1 94  ? -33.777 -28.879 22.142  1.00 10.35 ? 94  GLN B O   1 
ATOM   733  C  CB  . GLN A 1 94  ? -37.019 -28.605 21.175  1.00 14.15 ? 94  GLN B CB  1 
ATOM   734  C  CG  . GLN A 1 94  ? -36.915 -30.050 21.237  1.00 13.56 ? 94  GLN B CG  1 
ATOM   735  C  CD  . GLN A 1 94  ? -37.072 -30.536 22.673  1.00 19.76 ? 94  GLN B CD  1 
ATOM   736  O  OE1 . GLN A 1 94  ? -36.102 -30.618 23.420  1.00 17.83 ? 94  GLN B OE1 1 
ATOM   737  N  NE2 . GLN A 1 94  ? -38.276 -30.923 23.026  1.00 15.49 ? 94  GLN B NE2 1 
ATOM   738  N  N   . VAL A 1 95  ? -35.182 -27.616 23.409  1.00 10.49 ? 95  VAL B N   1 
ATOM   739  C  CA  . VAL A 1 95  ? -34.455 -27.818 24.654  1.00 9.97  ? 95  VAL B CA  1 
ATOM   740  C  C   . VAL A 1 95  ? -35.459 -28.285 25.701  1.00 9.91  ? 95  VAL B C   1 
ATOM   741  O  O   . VAL A 1 95  ? -36.577 -27.713 25.801  1.00 10.16 ? 95  VAL B O   1 
ATOM   742  C  CB  . VAL A 1 95  ? -33.634 -26.526 25.064  1.00 10.25 ? 95  VAL B CB  1 
ATOM   743  C  CG1 . VAL A 1 95  ? -33.071 -26.643 26.507  1.00 9.73  ? 95  VAL B CG1 1 
ATOM   744  C  CG2 . VAL A 1 95  ? -32.486 -26.262 24.065  1.00 8.32  ? 95  VAL B CG2 1 
ATOM   745  N  N   . HIS A 1 96  ? -35.072 -29.289 26.481  1.00 9.36  ? 96  HIS B N   1 
ATOM   746  C  CA  . HIS A 1 96  ? -35.875 -29.666 27.683  1.00 8.99  ? 96  HIS B CA  1 
ATOM   747  C  C   . HIS A 1 96  ? -34.970 -30.131 28.798  1.00 10.15 ? 96  HIS B C   1 
ATOM   748  O  O   . HIS A 1 96  ? -33.711 -30.136 28.658  1.00 10.10 ? 96  HIS B O   1 
ATOM   749  C  CB  . HIS A 1 96  ? -36.930 -30.755 27.325  1.00 6.27  ? 96  HIS B CB  1 
ATOM   750  C  CG  . HIS A 1 96  ? -36.313 -32.008 26.825  1.00 7.83  ? 96  HIS B CG  1 
ATOM   751  N  ND1 . HIS A 1 96  ? -35.938 -32.204 25.507  1.00 9.31  ? 96  HIS B ND1 1 
ATOM   752  C  CD2 . HIS A 1 96  ? -35.880 -33.095 27.517  1.00 7.19  ? 96  HIS B CD2 1 
ATOM   753  C  CE1 . HIS A 1 96  ? -35.310 -33.364 25.412  1.00 12.18 ? 96  HIS B CE1 1 
ATOM   754  N  NE2 . HIS A 1 96  ? -35.237 -33.914 26.626  1.00 8.01  ? 96  HIS B NE2 1 
ATOM   755  N  N   . LEU A 1 97  ? -35.604 -30.529 29.915  1.00 10.69 ? 97  LEU B N   1 
ATOM   756  C  CA  . LEU A 1 97  ? -34.850 -30.916 31.106  1.00 10.92 ? 97  LEU B CA  1 
ATOM   757  C  C   . LEU A 1 97  ? -35.435 -32.141 31.787  1.00 11.37 ? 97  LEU B C   1 
ATOM   758  O  O   . LEU A 1 97  ? -36.667 -32.275 31.839  1.00 13.70 ? 97  LEU B O   1 
ATOM   759  C  CB  . LEU A 1 97  ? -34.948 -29.768 32.134  1.00 8.89  ? 97  LEU B CB  1 
ATOM   760  C  CG  . LEU A 1 97  ? -34.022 -29.877 33.354  1.00 7.44  ? 97  LEU B CG  1 
ATOM   761  C  CD1 . LEU A 1 97  ? -32.531 -29.804 32.974  1.00 11.73 ? 97  LEU B CD1 1 
ATOM   762  C  CD2 . LEU A 1 97  ? -34.435 -28.722 34.378  1.00 10.50 ? 97  LEU B CD2 1 
ATOM   763  N  N   . HIS A 1 98  ? -34.572 -32.976 32.371  1.00 9.89  ? 98  HIS B N   1 
ATOM   764  C  CA  . HIS A 1 98  ? -34.999 -34.106 33.204  1.00 9.58  ? 98  HIS B CA  1 
ATOM   765  C  C   . HIS A 1 98  ? -34.515 -33.953 34.646  1.00 9.96  ? 98  HIS B C   1 
ATOM   766  O  O   . HIS A 1 98  ? -33.440 -33.423 34.890  1.00 11.69 ? 98  HIS B O   1 
ATOM   767  C  CB  . HIS A 1 98  ? -34.442 -35.424 32.652  1.00 7.65  ? 98  HIS B CB  1 
ATOM   768  C  CG  . HIS A 1 98  ? -34.866 -35.680 31.248  1.00 11.37 ? 98  HIS B CG  1 
ATOM   769  N  ND1 . HIS A 1 98  ? -36.027 -36.366 30.932  1.00 11.49 ? 98  HIS B ND1 1 
ATOM   770  C  CD2 . HIS A 1 98  ? -34.294 -35.346 30.074  1.00 12.68 ? 98  HIS B CD2 1 
ATOM   771  C  CE1 . HIS A 1 98  ? -36.124 -36.482 29.617  1.00 13.49 ? 98  HIS B CE1 1 
ATOM   772  N  NE2 . HIS A 1 98  ? -35.076 -35.889 29.077  1.00 12.39 ? 98  HIS B NE2 1 
ATOM   773  N  N   . TRP A 1 99  ? -35.336 -34.386 35.584  1.00 10.63 ? 99  TRP B N   1 
ATOM   774  C  CA  . TRP A 1 99  ? -34.924 -34.258 36.995  1.00 12.18 ? 99  TRP B CA  1 
ATOM   775  C  C   . TRP A 1 99  ? -35.573 -35.454 37.757  1.00 12.10 ? 99  TRP B C   1 
ATOM   776  O  O   . TRP A 1 99  ? -36.341 -36.215 37.171  1.00 13.44 ? 99  TRP B O   1 
ATOM   777  C  CB  . TRP A 1 99  ? -35.345 -32.885 37.546  1.00 11.91 ? 99  TRP B CB  1 
ATOM   778  C  CG  . TRP A 1 99  ? -36.878 -32.670 37.403  1.00 12.80 ? 99  TRP B CG  1 
ATOM   779  C  CD1 . TRP A 1 99  ? -37.853 -33.180 38.206  1.00 12.70 ? 99  TRP B CD1 1 
ATOM   780  C  CD2 . TRP A 1 99  ? -37.547 -31.948 36.347  1.00 14.24 ? 99  TRP B CD2 1 
ATOM   781  N  NE1 . TRP A 1 99  ? -39.128 -32.813 37.746  1.00 14.16 ? 99  TRP B NE1 1 
ATOM   782  C  CE2 . TRP A 1 99  ? -38.964 -32.037 36.611  1.00 16.17 ? 99  TRP B CE2 1 
ATOM   783  C  CE3 . TRP A 1 99  ? -37.092 -31.222 35.225  1.00 9.42  ? 99  TRP B CE3 1 
ATOM   784  C  CZ2 . TRP A 1 99  ? -39.932 -31.440 35.778  1.00 13.97 ? 99  TRP B CZ2 1 
ATOM   785  C  CZ3 . TRP A 1 99  ? -38.056 -30.596 34.379  1.00 12.75 ? 99  TRP B CZ3 1 
ATOM   786  C  CH2 . TRP A 1 99  ? -39.483 -30.746 34.639  1.00 9.70  ? 99  TRP B CH2 1 
ATOM   787  N  N   . GLY A 1 100 ? -35.289 -35.593 39.049  1.00 12.54 ? 100 GLY B N   1 
ATOM   788  C  CA  . GLY A 1 100 ? -35.996 -36.566 39.896  1.00 13.30 ? 100 GLY B CA  1 
ATOM   789  C  C   . GLY A 1 100 ? -36.769 -35.925 41.052  1.00 13.72 ? 100 GLY B C   1 
ATOM   790  O  O   . GLY A 1 100 ? -36.793 -34.695 41.210  1.00 14.12 ? 100 GLY B O   1 
ATOM   791  N  N   . SER A 1 101 ? -37.365 -36.740 41.900  1.00 13.80 ? 101 SER B N   1 
ATOM   792  C  CA  . SER A 1 101 ? -38.170 -36.179 42.993  1.00 15.95 ? 101 SER B CA  1 
ATOM   793  C  C   . SER A 1 101 ? -37.289 -35.596 44.107  1.00 15.57 ? 101 SER B C   1 
ATOM   794  O  O   . SER A 1 101 ? -37.798 -34.911 44.993  1.00 18.98 ? 101 SER B O   1 
ATOM   795  C  CB  . SER A 1 101 ? -39.148 -37.226 43.569  1.00 14.94 ? 101 SER B CB  1 
ATOM   796  O  OG  . SER A 1 101 ? -38.424 -38.411 43.816  1.00 19.27 ? 101 SER B OG  1 
ATOM   797  N  N   . ALA A 1 102 ? -36.005 -35.935 44.114  1.00 17.51 ? 102 ALA B N   1 
ATOM   798  C  CA  . ALA A 1 102 ? -35.083 -35.414 45.111  1.00 17.55 ? 102 ALA B CA  1 
ATOM   799  C  C   . ALA A 1 102 ? -33.767 -35.065 44.451  1.00 16.61 ? 102 ALA B C   1 
ATOM   800  O  O   . ALA A 1 102 ? -33.433 -35.606 43.386  1.00 16.50 ? 102 ALA B O   1 
ATOM   801  C  CB  . ALA A 1 102 ? -34.859 -36.410 46.248  1.00 16.39 ? 102 ALA B CB  1 
ATOM   802  N  N   . ASP A 1 103 ? -33.019 -34.147 45.066  1.00 16.60 ? 103 ASP B N   1 
ATOM   803  C  CA  . ASP A 1 103 ? -31.776 -33.616 44.451  1.00 17.41 ? 103 ASP B CA  1 
ATOM   804  C  C   . ASP A 1 103 ? -30.633 -34.562 44.246  1.00 18.48 ? 103 ASP B C   1 
ATOM   805  O  O   . ASP A 1 103 ? -29.733 -34.309 43.439  1.00 19.14 ? 103 ASP B O   1 
ATOM   806  C  CB  . ASP A 1 103 ? -31.204 -32.486 45.279  1.00 17.08 ? 103 ASP B CB  1 
ATOM   807  C  CG  . ASP A 1 103 ? -32.077 -31.251 45.370  1.00 18.78 ? 103 ASP B CG  1 
ATOM   808  O  OD1 . ASP A 1 103 ? -33.052 -31.072 44.611  1.00 18.61 ? 103 ASP B OD1 1 
ATOM   809  O  OD2 . ASP A 1 103 ? -31.735 -30.426 46.246  1.00 22.53 ? 103 ASP B OD2 1 
ATOM   810  N  N   . ASP A 1 104 ? -30.644 -35.668 44.973  1.00 19.27 ? 104 ASP B N   1 
ATOM   811  C  CA  . ASP A 1 104 ? -29.537 -36.646 44.944  1.00 21.27 ? 104 ASP B CA  1 
ATOM   812  C  C   . ASP A 1 104 ? -29.483 -37.442 43.621  1.00 22.00 ? 104 ASP B C   1 
ATOM   813  O  O   . ASP A 1 104 ? -28.443 -37.975 43.255  1.00 21.96 ? 104 ASP B O   1 
ATOM   814  C  CB  . ASP A 1 104 ? -29.664 -37.603 46.160  1.00 22.36 ? 104 ASP B CB  1 
ATOM   815  C  CG  . ASP A 1 104 ? -30.977 -38.390 46.161  1.00 23.76 ? 104 ASP B CG  1 
ATOM   816  O  OD1 . ASP A 1 104 ? -32.000 -37.886 46.660  1.00 29.36 ? 104 ASP B OD1 1 
ATOM   817  O  OD2 . ASP A 1 104 ? -31.001 -39.497 45.618  1.00 28.18 ? 104 ASP B OD2 1 
ATOM   818  N  N   . HIS A 1 105 ? -30.578 -37.510 42.865  1.00 21.03 ? 105 HIS B N   1 
ATOM   819  C  CA  . HIS A 1 105 ? -30.439 -38.080 41.513  1.00 22.63 ? 105 HIS B CA  1 
ATOM   820  C  C   . HIS A 1 105 ? -31.509 -37.545 40.577  1.00 21.71 ? 105 HIS B C   1 
ATOM   821  O  O   . HIS A 1 105 ? -32.380 -36.808 41.000  1.00 22.93 ? 105 HIS B O   1 
ATOM   822  C  CB  . HIS A 1 105 ? -30.428 -39.627 41.493  1.00 22.65 ? 105 HIS B CB  1 
ATOM   823  C  CG  . HIS A 1 105 ? -31.604 -40.255 42.175  1.00 28.20 ? 105 HIS B CG  1 
ATOM   824  N  ND1 . HIS A 1 105 ? -32.716 -40.704 41.487  1.00 36.37 ? 105 HIS B ND1 1 
ATOM   825  C  CD2 . HIS A 1 105 ? -31.858 -40.484 43.485  1.00 32.35 ? 105 HIS B CD2 1 
ATOM   826  C  CE1 . HIS A 1 105 ? -33.597 -41.195 42.348  1.00 35.75 ? 105 HIS B CE1 1 
ATOM   827  N  NE2 . HIS A 1 105 ? -33.099 -41.075 43.566  1.00 37.32 ? 105 HIS B NE2 1 
ATOM   828  N  N   . GLY A 1 106 ? -31.458 -37.918 39.298  1.00 19.55 ? 106 GLY B N   1 
ATOM   829  C  CA  . GLY A 1 106 ? -32.363 -37.252 38.385  1.00 17.44 ? 106 GLY B CA  1 
ATOM   830  C  C   . GLY A 1 106 ? -31.798 -37.053 37.021  1.00 16.31 ? 106 GLY B C   1 
ATOM   831  O  O   . GLY A 1 106 ? -32.570 -36.934 36.065  1.00 16.58 ? 106 GLY B O   1 
ATOM   832  N  N   . SER A 1 107 ? -30.469 -37.070 36.896  1.00 15.12 ? 107 SER B N   1 
ATOM   833  C  CA  . SER A 1 107 ? -29.880 -37.230 35.539  1.00 14.52 ? 107 SER B CA  1 
ATOM   834  C  C   . SER A 1 107 ? -30.312 -38.541 34.820  1.00 14.52 ? 107 SER B C   1 
ATOM   835  O  O   . SER A 1 107 ? -30.657 -39.593 35.468  1.00 14.28 ? 107 SER B O   1 
ATOM   836  C  CB  . SER A 1 107 ? -28.376 -37.044 35.509  1.00 11.84 ? 107 SER B CB  1 
ATOM   837  O  OG  . SER A 1 107 ? -27.662 -38.113 36.114  1.00 13.00 ? 107 SER B OG  1 
ATOM   838  N  N   . GLU A 1 108 ? -30.299 -38.478 33.487  1.00 13.01 ? 108 GLU B N   1 
ATOM   839  C  CA  . GLU A 1 108 ? -30.591 -39.712 32.710  1.00 12.87 ? 108 GLU B CA  1 
ATOM   840  C  C   . GLU A 1 108 ? -29.351 -40.582 32.540  1.00 12.70 ? 108 GLU B C   1 
ATOM   841  O  O   . GLU A 1 108 ? -29.355 -41.772 32.876  1.00 13.38 ? 108 GLU B O   1 
ATOM   842  C  CB  . GLU A 1 108 ? -31.258 -39.308 31.388  1.00 10.75 ? 108 GLU B CB  1 
ATOM   843  C  CG  . GLU A 1 108 ? -32.585 -38.612 31.680  1.00 15.82 ? 108 GLU B CG  1 
ATOM   844  C  CD  . GLU A 1 108 ? -33.628 -38.915 30.593  1.00 16.45 ? 108 GLU B CD  1 
ATOM   845  O  OE1 . GLU A 1 108 ? -33.263 -38.761 29.423  1.00 13.71 ? 108 GLU B OE1 1 
ATOM   846  O  OE2 . GLU A 1 108 ? -34.760 -39.331 30.893  1.00 12.01 ? 108 GLU B OE2 1 
ATOM   847  N  N   . HIS A 1 109 ? -28.272 -39.995 32.050  1.00 12.88 ? 109 HIS B N   1 
ATOM   848  C  CA  . HIS A 1 109 ? -26.981 -40.644 31.989  1.00 13.35 ? 109 HIS B CA  1 
ATOM   849  C  C   . HIS A 1 109 ? -26.378 -40.628 33.422  1.00 14.59 ? 109 HIS B C   1 
ATOM   850  O  O   . HIS A 1 109 ? -26.599 -39.698 34.217  1.00 14.22 ? 109 HIS B O   1 
ATOM   851  C  CB  . HIS A 1 109 ? -26.080 -39.947 30.965  1.00 13.46 ? 109 HIS B CB  1 
ATOM   852  C  CG  . HIS A 1 109 ? -26.601 -40.054 29.542  1.00 10.48 ? 109 HIS B CG  1 
ATOM   853  N  ND1 . HIS A 1 109 ? -27.558 -39.203 29.017  1.00 10.38 ? 109 HIS B ND1 1 
ATOM   854  C  CD2 . HIS A 1 109 ? -26.358 -40.980 28.578  1.00 11.56 ? 109 HIS B CD2 1 
ATOM   855  C  CE1 . HIS A 1 109 ? -27.831 -39.552 27.773  1.00 8.29  ? 109 HIS B CE1 1 
ATOM   856  N  NE2 . HIS A 1 109 ? -27.145 -40.656 27.490  1.00 12.30 ? 109 HIS B NE2 1 
ATOM   857  N  N   . ILE A 1 110 ? -25.609 -41.662 33.703  1.00 16.68 ? 110 ILE B N   1 
ATOM   858  C  CA  . ILE A 1 110 ? -24.932 -41.831 35.019  1.00 18.13 ? 110 ILE B CA  1 
ATOM   859  C  C   . ILE A 1 110 ? -23.480 -42.186 34.707  1.00 17.42 ? 110 ILE B C   1 
ATOM   860  O  O   . ILE A 1 110 ? -23.219 -43.113 33.917  1.00 17.14 ? 110 ILE B O   1 
ATOM   861  C  CB  . ILE A 1 110 ? -25.645 -42.952 35.815  1.00 18.38 ? 110 ILE B CB  1 
ATOM   862  C  CG1 . ILE A 1 110 ? -27.127 -42.573 36.118  1.00 17.89 ? 110 ILE B CG1 1 
ATOM   863  C  CG2 . ILE A 1 110 ? -24.788 -43.365 37.042  1.00 20.45 ? 110 ILE B CG2 1 
ATOM   864  C  CD1 . ILE A 1 110 ? -27.914 -43.721 36.934  1.00 21.98 ? 110 ILE B CD1 1 
ATOM   865  N  N   . VAL A 1 111 ? -22.537 -41.404 35.262  1.00 17.41 ? 111 VAL B N   1 
ATOM   866  C  CA  . VAL A 1 111 ? -21.109 -41.476 34.899  1.00 18.71 ? 111 VAL B CA  1 
ATOM   867  C  C   . VAL A 1 111 ? -20.329 -42.120 36.031  1.00 20.02 ? 111 VAL B C   1 
ATOM   868  O  O   . VAL A 1 111 ? -20.298 -41.589 37.127  1.00 19.84 ? 111 VAL B O   1 
ATOM   869  C  CB  . VAL A 1 111 ? -20.485 -40.082 34.586  1.00 19.35 ? 111 VAL B CB  1 
ATOM   870  C  CG1 . VAL A 1 111 ? -18.990 -40.222 34.264  1.00 20.38 ? 111 VAL B CG1 1 
ATOM   871  C  CG2 . VAL A 1 111 ? -21.205 -39.435 33.327  1.00 18.15 ? 111 VAL B CG2 1 
ATOM   872  N  N   . ASP A 1 112 ? -19.728 -43.262 35.746  1.00 21.04 ? 112 ASP B N   1 
ATOM   873  C  CA  . ASP A 1 112 ? -19.067 -44.075 36.795  1.00 23.51 ? 112 ASP B CA  1 
ATOM   874  C  C   . ASP A 1 112 ? -19.890 -44.111 38.113  1.00 24.29 ? 112 ASP B C   1 
ATOM   875  O  O   . ASP A 1 112 ? -19.379 -43.774 39.206  1.00 25.12 ? 112 ASP B O   1 
ATOM   876  C  CB  . ASP A 1 112 ? -17.648 -43.584 37.065  1.00 21.89 ? 112 ASP B CB  1 
ATOM   877  C  CG  . ASP A 1 112 ? -16.706 -43.799 35.885  1.00 24.28 ? 112 ASP B CG  1 
ATOM   878  O  OD1 . ASP A 1 112 ? -16.754 -44.901 35.269  1.00 25.28 ? 112 ASP B OD1 1 
ATOM   879  O  OD2 . ASP A 1 112 ? -15.876 -42.878 35.623  1.00 24.21 ? 112 ASP B OD2 1 
ATOM   880  N  N   . GLY A 1 113 ? -21.166 -44.490 38.009  1.00 24.64 ? 113 GLY B N   1 
ATOM   881  C  CA  . GLY A 1 113 ? -22.038 -44.515 39.190  1.00 25.04 ? 113 GLY B CA  1 
ATOM   882  C  C   . GLY A 1 113 ? -22.555 -43.167 39.667  1.00 25.07 ? 113 GLY B C   1 
ATOM   883  O  O   . GLY A 1 113 ? -23.521 -43.104 40.435  1.00 26.63 ? 113 GLY B O   1 
ATOM   884  N  N   . VAL A 1 114 ? -21.914 -42.081 39.253  1.00 24.55 ? 114 VAL B N   1 
ATOM   885  C  CA  . VAL A 1 114 ? -22.380 -40.761 39.635  1.00 25.06 ? 114 VAL B CA  1 
ATOM   886  C  C   . VAL A 1 114 ? -23.624 -40.304 38.844  1.00 25.76 ? 114 VAL B C   1 
ATOM   887  O  O   . VAL A 1 114 ? -23.589 -40.226 37.613  1.00 25.41 ? 114 VAL B O   1 
ATOM   888  C  CB  . VAL A 1 114 ? -21.270 -39.673 39.542  1.00 24.64 ? 114 VAL B CB  1 
ATOM   889  C  CG1 . VAL A 1 114 ? -21.766 -38.350 40.137  1.00 25.34 ? 114 VAL B CG1 1 
ATOM   890  C  CG2 . VAL A 1 114 ? -19.993 -40.125 40.259  1.00 26.46 ? 114 VAL B CG2 1 
ATOM   891  N  N   . SER A 1 115 ? -24.706 -39.995 39.573  1.00 25.50 ? 115 SER B N   1 
ATOM   892  C  CA  . SER A 1 115 ? -25.792 -39.216 38.994  1.00 25.57 ? 115 SER B CA  1 
ATOM   893  C  C   . SER A 1 115 ? -25.782 -37.762 39.525  1.00 25.31 ? 115 SER B C   1 
ATOM   894  O  O   . SER A 1 115 ? -25.294 -37.422 40.632  1.00 25.72 ? 115 SER B O   1 
ATOM   895  C  CB  . SER A 1 115 ? -27.174 -39.863 39.189  1.00 26.16 ? 115 SER B CB  1 
ATOM   896  O  OG  . SER A 1 115 ? -27.268 -40.647 40.375  1.00 30.49 ? 115 SER B OG  1 
ATOM   897  N  N   . TYR A 1 116 ? -26.397 -36.941 38.702  1.00 22.55 ? 116 TYR B N   1 
ATOM   898  C  CA  . TYR A 1 116 ? -26.538 -35.536 38.899  1.00 18.70 ? 116 TYR B CA  1 
ATOM   899  C  C   . TYR A 1 116 ? -27.961 -35.287 39.189  1.00 16.33 ? 116 TYR B C   1 
ATOM   900  O  O   . TYR A 1 116 ? -28.791 -36.232 39.112  1.00 16.75 ? 116 TYR B O   1 
ATOM   901  C  CB  . TYR A 1 116 ? -26.080 -34.922 37.601  1.00 16.84 ? 116 TYR B CB  1 
ATOM   902  C  CG  . TYR A 1 116 ? -24.625 -35.081 37.456  1.00 17.83 ? 116 TYR B CG  1 
ATOM   903  C  CD1 . TYR A 1 116 ? -23.758 -34.252 38.165  1.00 20.41 ? 116 TYR B CD1 1 
ATOM   904  C  CD2 . TYR A 1 116 ? -24.090 -36.043 36.601  1.00 21.17 ? 116 TYR B CD2 1 
ATOM   905  C  CE1 . TYR A 1 116 ? -22.390 -34.367 38.016  1.00 17.25 ? 116 TYR B CE1 1 
ATOM   906  C  CE2 . TYR A 1 116 ? -22.740 -36.190 36.469  1.00 18.95 ? 116 TYR B CE2 1 
ATOM   907  C  CZ  . TYR A 1 116 ? -21.904 -35.304 37.169  1.00 18.79 ? 116 TYR B CZ  1 
ATOM   908  O  OH  . TYR A 1 116 ? -20.556 -35.422 37.026  1.00 22.34 ? 116 TYR B OH  1 
ATOM   909  N  N   . ALA A 1 117 ? -28.220 -34.088 39.685  1.00 14.01 ? 117 ALA B N   1 
ATOM   910  C  CA  . ALA A 1 117 ? -29.568 -33.626 40.046  1.00 12.83 ? 117 ALA B CA  1 
ATOM   911  C  C   . ALA A 1 117 ? -30.507 -33.558 38.840  1.00 10.47 ? 117 ALA B C   1 
ATOM   912  O  O   . ALA A 1 117 ? -31.684 -33.760 38.980  1.00 11.35 ? 117 ALA B O   1 
ATOM   913  C  CB  . ALA A 1 117 ? -29.508 -32.193 40.703  1.00 10.88 ? 117 ALA B CB  1 
ATOM   914  N  N   . ALA A 1 118 ? -29.962 -33.227 37.671  1.00 11.04 ? 118 ALA B N   1 
ATOM   915  C  CA  . ALA A 1 118 ? -30.814 -32.978 36.510  1.00 10.39 ? 118 ALA B CA  1 
ATOM   916  C  C   . ALA A 1 118 ? -29.924 -33.058 35.269  1.00 8.77  ? 118 ALA B C   1 
ATOM   917  O  O   . ALA A 1 118 ? -28.697 -33.141 35.372  1.00 8.55  ? 118 ALA B O   1 
ATOM   918  C  CB  . ALA A 1 118 ? -31.488 -31.562 36.669  1.00 9.65  ? 118 ALA B CB  1 
ATOM   919  N  N   . GLU A 1 119 ? -30.565 -33.121 34.104  1.00 9.09  ? 119 GLU B N   1 
ATOM   920  C  CA  . GLU A 1 119 ? -29.870 -33.229 32.823  1.00 10.58 ? 119 GLU B CA  1 
ATOM   921  C  C   . GLU A 1 119 ? -30.691 -32.479 31.755  1.00 12.42 ? 119 GLU B C   1 
ATOM   922  O  O   . GLU A 1 119 ? -31.918 -32.720 31.545  1.00 11.16 ? 119 GLU B O   1 
ATOM   923  C  CB  . GLU A 1 119 ? -29.688 -34.658 32.439  1.00 10.80 ? 119 GLU B CB  1 
ATOM   924  C  CG  . GLU A 1 119 ? -28.761 -34.842 31.268  1.00 12.24 ? 119 GLU B CG  1 
ATOM   925  C  CD  . GLU A 1 119 ? -28.550 -36.297 30.940  1.00 13.49 ? 119 GLU B CD  1 
ATOM   926  O  OE1 . GLU A 1 119 ? -28.441 -37.124 31.843  1.00 11.52 ? 119 GLU B OE1 1 
ATOM   927  O  OE2 . GLU A 1 119 ? -28.498 -36.639 29.761  1.00 14.00 ? 119 GLU B OE2 1 
ATOM   928  N  N   . LEU A 1 120 ? -29.977 -31.590 31.104  1.00 11.23 ? 120 LEU B N   1 
ATOM   929  C  CA  . LEU A 1 120 ? -30.507 -30.714 30.063  1.00 13.45 ? 120 LEU B CA  1 
ATOM   930  C  C   . LEU A 1 120 ? -30.187 -31.381 28.747  1.00 12.15 ? 120 LEU B C   1 
ATOM   931  O  O   . LEU A 1 120 ? -29.021 -31.775 28.561  1.00 12.57 ? 120 LEU B O   1 
ATOM   932  C  CB  . LEU A 1 120 ? -29.753 -29.368 30.089  1.00 12.32 ? 120 LEU B CB  1 
ATOM   933  C  CG  . LEU A 1 120 ? -30.331 -28.264 29.102  1.00 16.71 ? 120 LEU B CG  1 
ATOM   934  C  CD1 . LEU A 1 120 ? -31.625 -27.610 29.649  1.00 10.04 ? 120 LEU B CD1 1 
ATOM   935  C  CD2 . LEU A 1 120 ? -29.271 -27.151 28.723  1.00 15.51 ? 120 LEU B CD2 1 
ATOM   936  N  N   . HIS A 1 121 ? -31.179 -31.389 27.823  1.00 11.88 ? 121 HIS B N   1 
ATOM   937  C  CA  . HIS A 1 121 ? -31.014 -31.964 26.532  1.00 10.93 ? 121 HIS B CA  1 
ATOM   938  C  C   . HIS A 1 121 ? -31.338 -30.928 25.460  1.00 10.84 ? 121 HIS B C   1 
ATOM   939  O  O   . HIS A 1 121 ? -32.360 -30.205 25.498  1.00 12.77 ? 121 HIS B O   1 
ATOM   940  C  CB  . HIS A 1 121 ? -31.904 -33.204 26.334  1.00 9.21  ? 121 HIS B CB  1 
ATOM   941  C  CG  . HIS A 1 121 ? -31.490 -34.403 27.122  1.00 11.43 ? 121 HIS B CG  1 
ATOM   942  N  ND1 . HIS A 1 121 ? -32.372 -35.412 27.432  1.00 9.69  ? 121 HIS B ND1 1 
ATOM   943  C  CD2 . HIS A 1 121 ? -30.307 -34.747 27.693  1.00 10.38 ? 121 HIS B CD2 1 
ATOM   944  C  CE1 . HIS A 1 121 ? -31.746 -36.326 28.162  1.00 13.29 ? 121 HIS B CE1 1 
ATOM   945  N  NE2 . HIS A 1 121 ? -30.499 -35.942 28.337  1.00 13.39 ? 121 HIS B NE2 1 
ATOM   946  N  N   . VAL A 1 122 ? -30.440 -30.866 24.485  1.00 10.54 ? 122 VAL B N   1 
ATOM   947  C  CA  . VAL A 1 122 ? -30.564 -29.956 23.362  1.00 10.22 ? 122 VAL B CA  1 
ATOM   948  C  C   . VAL A 1 122 ? -30.637 -30.824 22.129  1.00 10.18 ? 122 VAL B C   1 
ATOM   949  O  O   . VAL A 1 122 ? -29.640 -31.455 21.711  1.00 10.02 ? 122 VAL B O   1 
ATOM   950  C  CB  . VAL A 1 122 ? -29.373 -28.933 23.267  1.00 9.70  ? 122 VAL B CB  1 
ATOM   951  C  CG1 . VAL A 1 122 ? -29.637 -27.824 22.189  1.00 8.48  ? 122 VAL B CG1 1 
ATOM   952  C  CG2 . VAL A 1 122 ? -28.990 -28.348 24.646  1.00 10.05 ? 122 VAL B CG2 1 
ATOM   953  N  N   . VAL A 1 123 ? -31.817 -30.803 21.528  1.00 9.75  ? 123 VAL B N   1 
ATOM   954  C  CA  . VAL A 1 123 ? -32.171 -31.698 20.443  1.00 9.57  ? 123 VAL B CA  1 
ATOM   955  C  C   . VAL A 1 123 ? -31.947 -30.957 19.098  1.00 9.93  ? 123 VAL B C   1 
ATOM   956  O  O   . VAL A 1 123 ? -32.430 -29.829 18.906  1.00 9.02  ? 123 VAL B O   1 
ATOM   957  C  CB  . VAL A 1 123 ? -33.678 -32.121 20.534  1.00 8.45  ? 123 VAL B CB  1 
ATOM   958  C  CG1 . VAL A 1 123 ? -34.075 -33.105 19.408  1.00 8.60  ? 123 VAL B CG1 1 
ATOM   959  C  CG2 . VAL A 1 123 ? -34.020 -32.757 21.929  1.00 8.33  ? 123 VAL B CG2 1 
ATOM   960  N  N   . HIS A 1 124 ? -31.309 -31.683 18.168  1.00 11.62 ? 124 HIS B N   1 
ATOM   961  C  CA  . HIS A 1 124 ? -30.954 -31.188 16.821  1.00 11.56 ? 124 HIS B CA  1 
ATOM   962  C  C   . HIS A 1 124 ? -31.309 -32.295 15.822  1.00 11.08 ? 124 HIS B C   1 
ATOM   963  O  O   . HIS A 1 124 ? -31.292 -33.489 16.155  1.00 11.27 ? 124 HIS B O   1 
ATOM   964  C  CB  . HIS A 1 124 ? -29.439 -30.889 16.686  1.00 9.49  ? 124 HIS B CB  1 
ATOM   965  C  CG  . HIS A 1 124 ? -28.882 -30.043 17.777  1.00 13.09 ? 124 HIS B CG  1 
ATOM   966  N  ND1 . HIS A 1 124 ? -28.612 -30.543 19.039  1.00 10.67 ? 124 HIS B ND1 1 
ATOM   967  C  CD2 . HIS A 1 124 ? -28.483 -28.745 17.788  1.00 14.72 ? 124 HIS B CD2 1 
ATOM   968  C  CE1 . HIS A 1 124 ? -28.075 -29.598 19.777  1.00 10.94 ? 124 HIS B CE1 1 
ATOM   969  N  NE2 . HIS A 1 124 ? -28.009 -28.492 19.059  1.00 14.25 ? 124 HIS B NE2 1 
ATOM   970  N  N   . TRP A 1 125 ? -31.585 -31.879 14.588  1.00 11.49 ? 125 TRP B N   1 
ATOM   971  C  CA  . TRP A 1 125 ? -31.910 -32.809 13.512  1.00 11.57 ? 125 TRP B CA  1 
ATOM   972  C  C   . TRP A 1 125 ? -31.165 -32.476 12.220  1.00 12.42 ? 125 TRP B C   1 
ATOM   973  O  O   . TRP A 1 125 ? -31.011 -31.299 11.852  1.00 12.63 ? 125 TRP B O   1 
ATOM   974  C  CB  . TRP A 1 125 ? -33.431 -32.893 13.245  1.00 11.33 ? 125 TRP B CB  1 
ATOM   975  C  CG  . TRP A 1 125 ? -34.066 -31.631 12.830  1.00 13.62 ? 125 TRP B CG  1 
ATOM   976  C  CD1 . TRP A 1 125 ? -34.430 -30.564 13.665  1.00 12.74 ? 125 TRP B CD1 1 
ATOM   977  C  CD2 . TRP A 1 125 ? -34.503 -31.252 11.495  1.00 13.81 ? 125 TRP B CD2 1 
ATOM   978  N  NE1 . TRP A 1 125 ? -35.030 -29.563 12.914  1.00 12.68 ? 125 TRP B NE1 1 
ATOM   979  C  CE2 . TRP A 1 125 ? -35.088 -29.954 11.593  1.00 12.63 ? 125 TRP B CE2 1 
ATOM   980  C  CE3 . TRP A 1 125 ? -34.401 -31.846 10.231  1.00 15.75 ? 125 TRP B CE3 1 
ATOM   981  C  CZ2 . TRP A 1 125 ? -35.628 -29.276 10.469  1.00 14.24 ? 125 TRP B CZ2 1 
ATOM   982  C  CZ3 . TRP A 1 125 ? -34.949 -31.150 9.107   1.00 13.97 ? 125 TRP B CZ3 1 
ATOM   983  C  CH2 . TRP A 1 125 ? -35.495 -29.876 9.234   1.00 12.98 ? 125 TRP B CH2 1 
ATOM   984  N  N   . ASN A 1 126 ? -30.817 -33.548 11.514  1.00 13.47 ? 126 ASN B N   1 
ATOM   985  C  CA  . ASN A 1 126 ? -30.068 -33.488 10.278  1.00 14.31 ? 126 ASN B CA  1 
ATOM   986  C  C   . ASN A 1 126 ? -30.935 -32.947 9.126   1.00 12.78 ? 126 ASN B C   1 
ATOM   987  O  O   . ASN A 1 126 ? -31.676 -33.683 8.485   1.00 13.86 ? 126 ASN B O   1 
ATOM   988  C  CB  . ASN A 1 126 ? -29.538 -34.895 9.989   1.00 13.74 ? 126 ASN B CB  1 
ATOM   989  C  CG  . ASN A 1 126 ? -28.614 -34.964 8.770   1.00 14.75 ? 126 ASN B CG  1 
ATOM   990  O  OD1 . ASN A 1 126 ? -28.594 -34.057 7.900   1.00 14.46 ? 126 ASN B OD1 1 
ATOM   991  N  ND2 . ASN A 1 126 ? -27.865 -36.112 8.673   1.00 20.37 ? 126 ASN B ND2 1 
ATOM   992  N  N   . SER A 1 127 ? -30.902 -31.622 8.957   1.00 13.90 ? 127 SER B N   1 
ATOM   993  C  CA  . SER A 1 127 ? -31.579 -30.917 7.850   1.00 13.96 ? 127 SER B CA  1 
ATOM   994  C  C   . SER A 1 127 ? -30.812 -30.976 6.506   1.00 15.60 ? 127 SER B C   1 
ATOM   995  O  O   . SER A 1 127 ? -31.348 -30.565 5.466   1.00 16.75 ? 127 SER B O   1 
ATOM   996  C  CB  . SER A 1 127 ? -31.762 -29.468 8.254   1.00 13.13 ? 127 SER B CB  1 
ATOM   997  O  OG  . SER A 1 127 ? -30.499 -28.806 8.480   1.00 15.67 ? 127 SER B OG  1 
ATOM   998  N  N   . ASP A 1 128 ? -29.566 -31.459 6.540   1.00 14.25 ? 128 ASP B N   1 
ATOM   999  C  CA  . ASP A 1 128 ? -28.792 -31.766 5.334   1.00 16.97 ? 128 ASP B CA  1 
ATOM   1000 C  C   . ASP A 1 128 ? -29.349 -32.977 4.575   1.00 16.50 ? 128 ASP B C   1 
ATOM   1001 O  O   . ASP A 1 128 ? -29.276 -33.054 3.318   1.00 18.44 ? 128 ASP B O   1 
ATOM   1002 C  CB  . ASP A 1 128 ? -27.297 -31.955 5.652   1.00 16.33 ? 128 ASP B CB  1 
ATOM   1003 C  CG  . ASP A 1 128 ? -26.568 -30.679 5.913   1.00 17.25 ? 128 ASP B CG  1 
ATOM   1004 O  OD1 . ASP A 1 128 ? -25.342 -30.791 6.269   1.00 19.01 ? 128 ASP B OD1 1 
ATOM   1005 O  OD2 . ASP A 1 128 ? -27.161 -29.574 5.806   1.00 18.27 ? 128 ASP B OD2 1 
ATOM   1006 N  N   . LYS A 1 129 ? -29.983 -33.912 5.279   1.00 15.98 ? 129 LYS B N   1 
ATOM   1007 C  CA  . LYS A 1 129 ? -30.559 -35.087 4.626   1.00 14.60 ? 129 LYS B CA  1 
ATOM   1008 C  C   . LYS A 1 129 ? -32.065 -35.231 4.687   1.00 15.59 ? 129 LYS B C   1 
ATOM   1009 O  O   . LYS A 1 129 ? -32.658 -35.876 3.793   1.00 16.71 ? 129 LYS B O   1 
ATOM   1010 C  CB  . LYS A 1 129 ? -29.972 -36.430 5.186   1.00 15.10 ? 129 LYS B CB  1 
ATOM   1011 C  CG  . LYS A 1 129 ? -28.529 -36.609 4.887   1.00 15.42 ? 129 LYS B CG  1 
ATOM   1012 C  CD  . LYS A 1 129 ? -27.963 -37.883 5.429   1.00 16.81 ? 129 LYS B CD  1 
ATOM   1013 C  CE  . LYS A 1 129 ? -28.678 -39.135 4.950   1.00 19.75 ? 129 LYS B CE  1 
ATOM   1014 N  NZ  . LYS A 1 129 ? -27.912 -40.372 5.355   1.00 18.41 ? 129 LYS B NZ  1 
ATOM   1015 N  N   . TYR A 1 130 ? -32.704 -34.723 5.744   1.00 14.98 ? 130 TYR B N   1 
ATOM   1016 C  CA  . TYR A 1 130 ? -34.104 -35.026 5.976   1.00 15.28 ? 130 TYR B CA  1 
ATOM   1017 C  C   . TYR A 1 130 ? -34.902 -33.751 5.935   1.00 13.74 ? 130 TYR B C   1 
ATOM   1018 O  O   . TYR A 1 130 ? -34.357 -32.722 6.220   1.00 14.37 ? 130 TYR B O   1 
ATOM   1019 C  CB  . TYR A 1 130 ? -34.299 -35.772 7.325   1.00 14.22 ? 130 TYR B CB  1 
ATOM   1020 C  CG  . TYR A 1 130 ? -33.420 -36.992 7.321   1.00 13.68 ? 130 TYR B CG  1 
ATOM   1021 C  CD1 . TYR A 1 130 ? -33.624 -38.016 6.360   1.00 16.79 ? 130 TYR B CD1 1 
ATOM   1022 C  CD2 . TYR A 1 130 ? -32.337 -37.108 8.205   1.00 16.28 ? 130 TYR B CD2 1 
ATOM   1023 C  CE1 . TYR A 1 130 ? -32.771 -39.085 6.270   1.00 18.65 ? 130 TYR B CE1 1 
ATOM   1024 C  CE2 . TYR A 1 130 ? -31.518 -38.232 8.173   1.00 15.26 ? 130 TYR B CE2 1 
ATOM   1025 C  CZ  . TYR A 1 130 ? -31.742 -39.211 7.176   1.00 16.04 ? 130 TYR B CZ  1 
ATOM   1026 O  OH  . TYR A 1 130 ? -30.957 -40.338 7.130   1.00 13.91 ? 130 TYR B OH  1 
ATOM   1027 N  N   . PRO A 1 131 ? -36.177 -33.835 5.541   1.00 14.91 ? 131 PRO B N   1 
ATOM   1028 C  CA  . PRO A 1 131 ? -37.036 -32.670 5.288   1.00 16.28 ? 131 PRO B CA  1 
ATOM   1029 C  C   . PRO A 1 131 ? -37.608 -32.028 6.521   1.00 15.88 ? 131 PRO B C   1 
ATOM   1030 O  O   . PRO A 1 131 ? -38.113 -30.932 6.449   1.00 15.41 ? 131 PRO B O   1 
ATOM   1031 C  CB  . PRO A 1 131 ? -38.182 -33.268 4.436   1.00 15.41 ? 131 PRO B CB  1 
ATOM   1032 C  CG  . PRO A 1 131 ? -38.311 -34.634 4.898   1.00 17.17 ? 131 PRO B CG  1 
ATOM   1033 C  CD  . PRO A 1 131 ? -36.869 -35.091 5.163   1.00 16.04 ? 131 PRO B CD  1 
ATOM   1034 N  N   . SER A 1 132 ? -37.574 -32.761 7.633   1.00 16.19 ? 132 SER B N   1 
ATOM   1035 C  CA  . SER A 1 132 ? -38.274 -32.365 8.850   1.00 17.01 ? 132 SER B CA  1 
ATOM   1036 C  C   . SER A 1 132 ? -37.696 -33.129 10.052  1.00 17.82 ? 132 SER B C   1 
ATOM   1037 O  O   . SER A 1 132 ? -37.120 -34.220 9.892   1.00 18.32 ? 132 SER B O   1 
ATOM   1038 C  CB  . SER A 1 132 ? -39.782 -32.615 8.720   1.00 16.72 ? 132 SER B CB  1 
ATOM   1039 O  OG  . SER A 1 132 ? -40.056 -34.005 8.818   1.00 17.08 ? 132 SER B OG  1 
ATOM   1040 N  N   . PHE A 1 133 ? -37.815 -32.513 11.235  1.00 18.90 ? 133 PHE B N   1 
ATOM   1041 C  CA  . PHE A 1 133 ? -37.468 -33.157 12.493  1.00 18.07 ? 133 PHE B CA  1 
ATOM   1042 C  C   . PHE A 1 133 ? -38.223 -34.489 12.589  1.00 17.28 ? 133 PHE B C   1 
ATOM   1043 O  O   . PHE A 1 133 ? -37.655 -35.509 12.906  1.00 13.09 ? 133 PHE B O   1 
ATOM   1044 C  CB  . PHE A 1 133 ? -37.867 -32.275 13.685  1.00 18.82 ? 133 PHE B CB  1 
ATOM   1045 C  CG  . PHE A 1 133 ? -37.793 -33.003 14.990  1.00 19.36 ? 133 PHE B CG  1 
ATOM   1046 C  CD1 . PHE A 1 133 ? -36.541 -33.248 15.604  1.00 17.45 ? 133 PHE B CD1 1 
ATOM   1047 C  CD2 . PHE A 1 133 ? -38.962 -33.447 15.612  1.00 21.93 ? 133 PHE B CD2 1 
ATOM   1048 C  CE1 . PHE A 1 133 ? -36.479 -33.934 16.820  1.00 20.32 ? 133 PHE B CE1 1 
ATOM   1049 C  CE2 . PHE A 1 133 ? -38.906 -34.190 16.819  1.00 23.02 ? 133 PHE B CE2 1 
ATOM   1050 C  CZ  . PHE A 1 133 ? -37.636 -34.391 17.440  1.00 21.67 ? 133 PHE B CZ  1 
ATOM   1051 N  N   . VAL A 1 134 ? -39.531 -34.452 12.314  1.00 17.98 ? 134 VAL B N   1 
ATOM   1052 C  CA  . VAL A 1 134 ? -40.331 -35.646 12.400  1.00 19.39 ? 134 VAL B CA  1 
ATOM   1053 C  C   . VAL A 1 134 ? -39.753 -36.778 11.538  1.00 20.16 ? 134 VAL B C   1 
ATOM   1054 O  O   . VAL A 1 134 ? -39.621 -37.944 12.000  1.00 19.92 ? 134 VAL B O   1 
ATOM   1055 C  CB  . VAL A 1 134 ? -41.855 -35.347 12.049  1.00 21.21 ? 134 VAL B CB  1 
ATOM   1056 C  CG1 . VAL A 1 134 ? -42.525 -36.611 11.573  1.00 22.33 ? 134 VAL B CG1 1 
ATOM   1057 C  CG2 . VAL A 1 134 ? -42.526 -34.758 13.271  1.00 21.63 ? 134 VAL B CG2 1 
ATOM   1058 N  N   . GLU A 1 135 ? -39.379 -36.481 10.283  1.00 19.75 ? 135 GLU B N   1 
ATOM   1059 C  CA  . GLU A 1 135 ? -38.772 -37.526 9.467   1.00 19.77 ? 135 GLU B CA  1 
ATOM   1060 C  C   . GLU A 1 135 ? -37.401 -38.003 9.984   1.00 18.64 ? 135 GLU B C   1 
ATOM   1061 O  O   . GLU A 1 135 ? -37.094 -39.225 9.961   1.00 18.97 ? 135 GLU B O   1 
ATOM   1062 C  CB  . GLU A 1 135 ? -38.668 -37.096 7.978   1.00 20.21 ? 135 GLU B CB  1 
ATOM   1063 C  CG  . GLU A 1 135 ? -37.648 -37.936 7.242   1.00 26.44 ? 135 GLU B CG  1 
ATOM   1064 C  CD  . GLU A 1 135 ? -38.160 -39.353 7.051   1.00 33.31 ? 135 GLU B CD  1 
ATOM   1065 O  OE1 . GLU A 1 135 ? -37.357 -40.329 7.149   1.00 28.54 ? 135 GLU B OE1 1 
ATOM   1066 O  OE2 . GLU A 1 135 ? -39.390 -39.465 6.854   1.00 36.79 ? 135 GLU B OE2 1 
ATOM   1067 N  N   . ALA A 1 136 ? -36.576 -37.035 10.417  1.00 17.53 ? 136 ALA B N   1 
ATOM   1068 C  CA  . ALA A 1 136 ? -35.172 -37.249 10.867  1.00 17.15 ? 136 ALA B CA  1 
ATOM   1069 C  C   . ALA A 1 136 ? -35.172 -38.193 12.081  1.00 16.74 ? 136 ALA B C   1 
ATOM   1070 O  O   . ALA A 1 136 ? -34.302 -39.056 12.211  1.00 16.02 ? 136 ALA B O   1 
ATOM   1071 C  CB  . ALA A 1 136 ? -34.517 -35.893 11.237  1.00 15.19 ? 136 ALA B CB  1 
ATOM   1072 N  N   . ALA A 1 137 ? -36.171 -38.016 12.947  1.00 15.78 ? 137 ALA B N   1 
ATOM   1073 C  CA  . ALA A 1 137 ? -36.411 -38.871 14.133  1.00 15.32 ? 137 ALA B CA  1 
ATOM   1074 C  C   . ALA A 1 137 ? -36.548 -40.345 13.821  1.00 16.42 ? 137 ALA B C   1 
ATOM   1075 O  O   . ALA A 1 137 ? -36.415 -41.177 14.713  1.00 16.78 ? 137 ALA B O   1 
ATOM   1076 C  CB  . ALA A 1 137 ? -37.635 -38.385 14.907  1.00 14.52 ? 137 ALA B CB  1 
ATOM   1077 N  N   . HIS A 1 138 ? -36.767 -40.692 12.553  1.00 15.97 ? 138 HIS B N   1 
ATOM   1078 C  CA  . HIS A 1 138 ? -36.877 -42.061 12.200  1.00 17.41 ? 138 HIS B CA  1 
ATOM   1079 C  C   . HIS A 1 138 ? -35.663 -42.628 11.487  1.00 18.66 ? 138 HIS B C   1 
ATOM   1080 O  O   . HIS A 1 138 ? -35.725 -43.748 10.943  1.00 20.22 ? 138 HIS B O   1 
ATOM   1081 C  CB  . HIS A 1 138 ? -38.160 -42.306 11.392  1.00 18.44 ? 138 HIS B CB  1 
ATOM   1082 C  CG  . HIS A 1 138 ? -39.400 -42.108 12.212  1.00 19.31 ? 138 HIS B CG  1 
ATOM   1083 N  ND1 . HIS A 1 138 ? -39.991 -43.132 12.919  1.00 24.43 ? 138 HIS B ND1 1 
ATOM   1084 C  CD2 . HIS A 1 138 ? -40.123 -40.997 12.488  1.00 22.04 ? 138 HIS B CD2 1 
ATOM   1085 C  CE1 . HIS A 1 138 ? -41.050 -42.675 13.556  1.00 21.06 ? 138 HIS B CE1 1 
ATOM   1086 N  NE2 . HIS A 1 138 ? -41.152 -41.383 13.317  1.00 22.69 ? 138 HIS B NE2 1 
ATOM   1087 N  N   . GLU A 1 139 ? -34.554 -41.889 11.493  1.00 17.86 ? 139 GLU B N   1 
ATOM   1088 C  CA  . GLU A 1 139 ? -33.361 -42.306 10.753  1.00 17.19 ? 139 GLU B CA  1 
ATOM   1089 C  C   . GLU A 1 139 ? -32.198 -42.476 11.682  1.00 15.36 ? 139 GLU B C   1 
ATOM   1090 O  O   . GLU A 1 139 ? -31.979 -41.621 12.517  1.00 14.46 ? 139 GLU B O   1 
ATOM   1091 C  CB  . GLU A 1 139 ? -33.041 -41.153 9.797   1.00 19.40 ? 139 GLU B CB  1 
ATOM   1092 C  CG  . GLU A 1 139 ? -34.162 -40.775 8.912   1.00 20.44 ? 139 GLU B CG  1 
ATOM   1093 C  CD  . GLU A 1 139 ? -34.315 -41.702 7.788   1.00 25.71 ? 139 GLU B CD  1 
ATOM   1094 O  OE1 . GLU A 1 139 ? -33.545 -42.707 7.721   1.00 26.56 ? 139 GLU B OE1 1 
ATOM   1095 O  OE2 . GLU A 1 139 ? -35.234 -41.411 6.949   1.00 32.68 ? 139 GLU B OE2 1 
ATOM   1096 N  N   . PRO A 1 140 ? -31.375 -43.509 11.516  1.00 17.28 ? 140 PRO B N   1 
ATOM   1097 C  CA  . PRO A 1 140 ? -30.255 -43.647 12.452  1.00 15.95 ? 140 PRO B CA  1 
ATOM   1098 C  C   . PRO A 1 140 ? -29.325 -42.465 12.657  1.00 15.18 ? 140 PRO B C   1 
ATOM   1099 O  O   . PRO A 1 140 ? -28.833 -42.288 13.779  1.00 13.73 ? 140 PRO B O   1 
ATOM   1100 C  CB  . PRO A 1 140 ? -29.476 -44.842 11.868  1.00 19.18 ? 140 PRO B CB  1 
ATOM   1101 C  CG  . PRO A 1 140 ? -30.602 -45.716 11.403  1.00 20.29 ? 140 PRO B CG  1 
ATOM   1102 C  CD  . PRO A 1 140 ? -31.386 -44.643 10.582  1.00 18.69 ? 140 PRO B CD  1 
ATOM   1103 N  N   . ASP A 1 141 ? -29.077 -41.692 11.581  1.00 13.67 ? 141 ASP B N   1 
ATOM   1104 C  CA  . ASP A 1 141 ? -28.288 -40.490 11.579  1.00 13.92 ? 141 ASP B CA  1 
ATOM   1105 C  C   . ASP A 1 141 ? -29.149 -39.194 11.627  1.00 13.97 ? 141 ASP B C   1 
ATOM   1106 O  O   . ASP A 1 141 ? -28.586 -38.069 11.417  1.00 14.36 ? 141 ASP B O   1 
ATOM   1107 C  CB  . ASP A 1 141 ? -27.365 -40.416 10.335  1.00 14.43 ? 141 ASP B CB  1 
ATOM   1108 C  CG  . ASP A 1 141 ? -28.141 -40.365 9.004   1.00 12.83 ? 141 ASP B CG  1 
ATOM   1109 O  OD1 . ASP A 1 141 ? -29.349 -40.644 8.996   1.00 13.20 ? 141 ASP B OD1 1 
ATOM   1110 O  OD2 . ASP A 1 141 ? -27.512 -40.075 7.936   1.00 20.48 ? 141 ASP B OD2 1 
ATOM   1111 N  N   . GLY A 1 142 ? -30.444 -39.328 11.960  1.00 14.88 ? 142 GLY B N   1 
ATOM   1112 C  CA  . GLY A 1 142 ? -31.352 -38.189 11.905  1.00 14.02 ? 142 GLY B CA  1 
ATOM   1113 C  C   . GLY A 1 142 ? -31.153 -37.160 13.031  1.00 14.83 ? 142 GLY B C   1 
ATOM   1114 O  O   . GLY A 1 142 ? -31.227 -35.961 12.824  1.00 14.36 ? 142 GLY B O   1 
ATOM   1115 N  N   . LEU A 1 143 ? -30.930 -37.632 14.254  1.00 14.44 ? 143 LEU B N   1 
ATOM   1116 C  CA  . LEU A 1 143 ? -30.901 -36.703 15.429  1.00 13.91 ? 143 LEU B CA  1 
ATOM   1117 C  C   . LEU A 1 143 ? -29.577 -36.675 16.157  1.00 12.38 ? 143 LEU B C   1 
ATOM   1118 O  O   . LEU A 1 143 ? -28.862 -37.649 16.137  1.00 13.64 ? 143 LEU B O   1 
ATOM   1119 C  CB  . LEU A 1 143 ? -32.025 -37.054 16.427  1.00 12.98 ? 143 LEU B CB  1 
ATOM   1120 C  CG  . LEU A 1 143 ? -33.489 -37.168 15.851  1.00 12.04 ? 143 LEU B CG  1 
ATOM   1121 C  CD1 . LEU A 1 143 ? -34.459 -37.606 16.985  1.00 13.90 ? 143 LEU B CD1 1 
ATOM   1122 C  CD2 . LEU A 1 143 ? -33.952 -35.800 15.201  1.00 7.94  ? 143 LEU B CD2 1 
ATOM   1123 N  N   . ALA A 1 144 ? -29.262 -35.527 16.749  1.00 11.62 ? 144 ALA B N   1 
ATOM   1124 C  CA  . ALA A 1 144 ? -28.118 -35.281 17.656  1.00 11.72 ? 144 ALA B CA  1 
ATOM   1125 C  C   . ALA A 1 144 ? -28.615 -34.514 18.888  1.00 11.46 ? 144 ALA B C   1 
ATOM   1126 O  O   . ALA A 1 144 ? -29.227 -33.427 18.796  1.00 13.02 ? 144 ALA B O   1 
ATOM   1127 C  CB  . ALA A 1 144 ? -26.966 -34.443 16.981  1.00 11.67 ? 144 ALA B CB  1 
ATOM   1128 N  N   . VAL A 1 145 ? -28.343 -35.073 20.062  1.00 11.80 ? 145 VAL B N   1 
ATOM   1129 C  CA  . VAL A 1 145 ? -28.787 -34.442 21.284  1.00 10.01 ? 145 VAL B CA  1 
ATOM   1130 C  C   . VAL A 1 145 ? -27.545 -34.265 22.120  1.00 11.41 ? 145 VAL B C   1 
ATOM   1131 O  O   . VAL A 1 145 ? -26.738 -35.221 22.349  1.00 9.72  ? 145 VAL B O   1 
ATOM   1132 C  CB  . VAL A 1 145 ? -29.835 -35.312 22.108  1.00 9.98  ? 145 VAL B CB  1 
ATOM   1133 C  CG1 . VAL A 1 145 ? -30.263 -34.541 23.346  1.00 8.03  ? 145 VAL B CG1 1 
ATOM   1134 C  CG2 . VAL A 1 145 ? -31.097 -35.691 21.262  1.00 10.37 ? 145 VAL B CG2 1 
ATOM   1135 N  N   . LEU A 1 146 ? -27.430 -33.041 22.576  1.00 12.07 ? 146 LEU B N   1 
ATOM   1136 C  CA  . LEU A 1 146 ? -26.411 -32.640 23.510  1.00 14.64 ? 146 LEU B CA  1 
ATOM   1137 C  C   . LEU A 1 146 ? -26.996 -32.703 24.904  1.00 15.06 ? 146 LEU B C   1 
ATOM   1138 O  O   . LEU A 1 146 ? -28.052 -32.105 25.164  1.00 14.27 ? 146 LEU B O   1 
ATOM   1139 C  CB  . LEU A 1 146 ? -26.018 -31.211 23.178  1.00 15.52 ? 146 LEU B CB  1 
ATOM   1140 C  CG  . LEU A 1 146 ? -24.651 -30.680 23.475  1.00 21.46 ? 146 LEU B CG  1 
ATOM   1141 C  CD1 . LEU A 1 146 ? -23.729 -31.378 22.541  1.00 24.23 ? 146 LEU B CD1 1 
ATOM   1142 C  CD2 . LEU A 1 146 ? -24.647 -29.212 23.084  1.00 28.31 ? 146 LEU B CD2 1 
ATOM   1143 N  N   . GLY A 1 147 ? -26.327 -33.468 25.782  1.00 15.38 ? 147 GLY B N   1 
ATOM   1144 C  CA  . GLY A 1 147 ? -26.719 -33.570 27.200  1.00 14.41 ? 147 GLY B CA  1 
ATOM   1145 C  C   . GLY A 1 147 ? -25.743 -32.808 28.072  1.00 13.66 ? 147 GLY B C   1 
ATOM   1146 O  O   . GLY A 1 147 ? -24.533 -32.914 27.859  1.00 13.20 ? 147 GLY B O   1 
ATOM   1147 N  N   . VAL A 1 148 ? -26.307 -32.096 29.060  1.00 13.77 ? 148 VAL B N   1 
ATOM   1148 C  CA  . VAL A 1 148 ? -25.560 -31.296 29.992  1.00 13.13 ? 148 VAL B CA  1 
ATOM   1149 C  C   . VAL A 1 148 ? -26.071 -31.713 31.348  1.00 12.55 ? 148 VAL B C   1 
ATOM   1150 O  O   . VAL A 1 148 ? -27.310 -31.675 31.630  1.00 12.97 ? 148 VAL B O   1 
ATOM   1151 C  CB  . VAL A 1 148 ? -25.732 -29.754 29.731  1.00 14.54 ? 148 VAL B CB  1 
ATOM   1152 C  CG1 . VAL A 1 148 ? -24.991 -28.911 30.895  1.00 13.99 ? 148 VAL B CG1 1 
ATOM   1153 C  CG2 . VAL A 1 148 ? -25.201 -29.367 28.330  1.00 14.43 ? 148 VAL B CG2 1 
ATOM   1154 N  N   . PHE A 1 149 ? -25.149 -32.152 32.200  1.00 12.53 ? 149 PHE B N   1 
ATOM   1155 C  CA  . PHE A 1 149 ? -25.509 -32.457 33.625  1.00 11.78 ? 149 PHE B CA  1 
ATOM   1156 C  C   . PHE A 1 149 ? -25.668 -31.216 34.468  1.00 12.52 ? 149 PHE B C   1 
ATOM   1157 O  O   . PHE A 1 149 ? -24.990 -30.168 34.276  1.00 13.14 ? 149 PHE B O   1 
ATOM   1158 C  CB  . PHE A 1 149 ? -24.426 -33.337 34.232  1.00 11.11 ? 149 PHE B CB  1 
ATOM   1159 C  CG  . PHE A 1 149 ? -24.271 -34.690 33.560  1.00 12.77 ? 149 PHE B CG  1 
ATOM   1160 C  CD1 . PHE A 1 149 ? -25.322 -35.610 33.577  1.00 14.00 ? 149 PHE B CD1 1 
ATOM   1161 C  CD2 . PHE A 1 149 ? -23.065 -35.022 32.943  1.00 13.11 ? 149 PHE B CD2 1 
ATOM   1162 C  CE1 . PHE A 1 149 ? -25.194 -36.866 33.009  1.00 12.01 ? 149 PHE B CE1 1 
ATOM   1163 C  CE2 . PHE A 1 149 ? -22.877 -36.311 32.378  1.00 13.70 ? 149 PHE B CE2 1 
ATOM   1164 C  CZ  . PHE A 1 149 ? -23.967 -37.227 32.399  1.00 10.39 ? 149 PHE B CZ  1 
ATOM   1165 N  N   . LEU A 1 150 ? -26.601 -31.288 35.395  1.00 14.68 ? 150 LEU B N   1 
ATOM   1166 C  CA  . LEU A 1 150 ? -26.754 -30.177 36.327  1.00 14.91 ? 150 LEU B CA  1 
ATOM   1167 C  C   . LEU A 1 150 ? -26.484 -30.729 37.708  1.00 14.67 ? 150 LEU B C   1 
ATOM   1168 O  O   . LEU A 1 150 ? -27.112 -31.668 38.099  1.00 14.55 ? 150 LEU B O   1 
ATOM   1169 C  CB  . LEU A 1 150 ? -28.163 -29.567 36.289  1.00 14.12 ? 150 LEU B CB  1 
ATOM   1170 C  CG  . LEU A 1 150 ? -28.429 -28.629 35.118  1.00 15.06 ? 150 LEU B CG  1 
ATOM   1171 C  CD1 . LEU A 1 150 ? -28.731 -29.511 33.878  1.00 16.75 ? 150 LEU B CD1 1 
ATOM   1172 C  CD2 . LEU A 1 150 ? -29.710 -27.763 35.376  1.00 13.50 ? 150 LEU B CD2 1 
ATOM   1173 N  N   . GLN A 1 151 ? -25.538 -30.125 38.423  1.00 14.85 ? 151 GLN B N   1 
ATOM   1174 C  CA  . GLN A 1 151 ? -25.240 -30.543 39.770  1.00 15.46 ? 151 GLN B CA  1 
ATOM   1175 C  C   . GLN A 1 151 ? -25.706 -29.472 40.733  1.00 16.93 ? 151 GLN B C   1 
ATOM   1176 O  O   . GLN A 1 151 ? -25.759 -28.266 40.385  1.00 16.14 ? 151 GLN B O   1 
ATOM   1177 C  CB  . GLN A 1 151 ? -23.733 -30.782 39.980  1.00 15.02 ? 151 GLN B CB  1 
ATOM   1178 C  CG  . GLN A 1 151 ? -22.990 -29.437 39.972  1.00 17.68 ? 151 GLN B CG  1 
ATOM   1179 C  CD  . GLN A 1 151 ? -21.499 -29.551 39.970  1.00 23.34 ? 151 GLN B CD  1 
ATOM   1180 O  OE1 . GLN A 1 151 ? -20.948 -30.619 40.264  1.00 25.09 ? 151 GLN B OE1 1 
ATOM   1181 N  NE2 . GLN A 1 151 ? -20.807 -28.413 39.672  1.00 22.56 ? 151 GLN B NE2 1 
ATOM   1182 N  N   . ILE A 1 152 ? -26.055 -29.928 41.940  1.00 17.22 ? 152 ILE B N   1 
ATOM   1183 C  CA  . ILE A 1 152 ? -26.501 -29.008 42.966  1.00 19.64 ? 152 ILE B CA  1 
ATOM   1184 C  C   . ILE A 1 152 ? -25.320 -28.099 43.303  1.00 19.76 ? 152 ILE B C   1 
ATOM   1185 O  O   . ILE A 1 152 ? -24.207 -28.549 43.508  1.00 18.10 ? 152 ILE B O   1 
ATOM   1186 C  CB  . ILE A 1 152 ? -27.070 -29.702 44.216  1.00 19.07 ? 152 ILE B CB  1 
ATOM   1187 C  CG1 . ILE A 1 152 ? -28.343 -30.452 43.889  1.00 20.47 ? 152 ILE B CG1 1 
ATOM   1188 C  CG2 . ILE A 1 152 ? -27.309 -28.636 45.358  1.00 18.80 ? 152 ILE B CG2 1 
ATOM   1189 C  CD1 . ILE A 1 152 ? -29.513 -29.597 43.294  1.00 16.08 ? 152 ILE B CD1 1 
ATOM   1190 N  N   . GLY A 1 153 ? -25.552 -26.805 43.217  1.00 20.18 ? 153 GLY B N   1 
ATOM   1191 C  CA  . GLY A 1 153 ? -24.477 -25.842 43.417  1.00 20.55 ? 153 GLY B CA  1 
ATOM   1192 C  C   . GLY A 1 153 ? -25.108 -24.478 43.618  1.00 20.19 ? 153 GLY B C   1 
ATOM   1193 O  O   . GLY A 1 153 ? -26.326 -24.340 43.923  1.00 20.06 ? 153 GLY B O   1 
ATOM   1194 N  N   A GLU A 1 154 ? -24.303 -23.443 43.560  0.50 20.34 ? 154 GLU B N   1 
ATOM   1195 N  N   B GLU A 1 154 ? -24.273 -23.471 43.363  0.50 20.48 ? 154 GLU B N   1 
ATOM   1196 C  CA  A GLU A 1 154 ? -24.887 -22.138 43.803  0.50 19.27 ? 154 GLU B CA  1 
ATOM   1197 C  CA  B GLU A 1 154 ? -24.691 -22.065 43.403  0.50 20.08 ? 154 GLU B CA  1 
ATOM   1198 C  C   A GLU A 1 154 ? -25.750 -21.807 42.558  0.50 19.97 ? 154 GLU B C   1 
ATOM   1199 C  C   B GLU A 1 154 ? -25.823 -21.849 42.395  0.50 20.19 ? 154 GLU B C   1 
ATOM   1200 O  O   A GLU A 1 154 ? -25.506 -22.344 41.454  0.50 19.17 ? 154 GLU B O   1 
ATOM   1201 O  O   B GLU A 1 154 ? -25.838 -22.491 41.324  0.50 19.33 ? 154 GLU B O   1 
ATOM   1202 C  CB  A GLU A 1 154 ? -23.794 -21.095 44.141  0.50 19.58 ? 154 GLU B CB  1 
ATOM   1203 C  CB  B GLU A 1 154 ? -23.492 -21.086 43.171  0.50 19.96 ? 154 GLU B CB  1 
ATOM   1204 C  CG  A GLU A 1 154 ? -23.158 -21.291 45.534  0.50 13.86 ? 154 GLU B CG  1 
ATOM   1205 C  CG  B GLU A 1 154 ? -23.191 -20.636 41.731  0.50 20.15 ? 154 GLU B CG  1 
ATOM   1206 C  CD  A GLU A 1 154 ? -21.672 -20.985 45.563  0.50 14.18 ? 154 GLU B CD  1 
ATOM   1207 C  CD  B GLU A 1 154 ? -22.117 -19.577 41.640  0.50 17.96 ? 154 GLU B CD  1 
ATOM   1208 O  OE1 A GLU A 1 154 ? -21.091 -20.839 46.668  0.50 12.78 ? 154 GLU B OE1 1 
ATOM   1209 O  OE1 B GLU A 1 154 ? -22.397 -18.477 41.161  0.50 19.19 ? 154 GLU B OE1 1 
ATOM   1210 O  OE2 A GLU A 1 154 ? -21.050 -20.883 44.481  0.50 13.36 ? 154 GLU B OE2 1 
ATOM   1211 O  OE2 B GLU A 1 154 ? -20.979 -19.827 42.022  0.50 22.72 ? 154 GLU B OE2 1 
ATOM   1212 N  N   . PRO A 1 155 ? -26.786 -20.961 42.737  1.00 20.29 ? 155 PRO B N   1 
ATOM   1213 C  CA  . PRO A 1 155 ? -27.764 -20.708 41.692  1.00 20.55 ? 155 PRO B CA  1 
ATOM   1214 C  C   . PRO A 1 155 ? -27.186 -20.262 40.325  1.00 20.46 ? 155 PRO B C   1 
ATOM   1215 O  O   . PRO A 1 155 ? -26.194 -19.508 40.216  1.00 20.66 ? 155 PRO B O   1 
ATOM   1216 C  CB  . PRO A 1 155 ? -28.716 -19.662 42.302  1.00 21.60 ? 155 PRO B CB  1 
ATOM   1217 C  CG  . PRO A 1 155 ? -27.925 -19.088 43.455  1.00 20.52 ? 155 PRO B CG  1 
ATOM   1218 C  CD  . PRO A 1 155 ? -27.062 -20.217 43.964  1.00 18.44 ? 155 PRO B CD  1 
ATOM   1219 N  N   . ASN A 1 156 ? -27.850 -20.756 39.292  1.00 20.29 ? 156 ASN B N   1 
ATOM   1220 C  CA  . ASN A 1 156 ? -27.482 -20.483 37.917  1.00 19.21 ? 156 ASN B CA  1 
ATOM   1221 C  C   . ASN A 1 156 ? -28.352 -19.393 37.329  1.00 17.99 ? 156 ASN B C   1 
ATOM   1222 O  O   . ASN A 1 156 ? -29.509 -19.624 37.023  1.00 19.17 ? 156 ASN B O   1 
ATOM   1223 C  CB  . ASN A 1 156 ? -27.592 -21.799 37.085  1.00 19.63 ? 156 ASN B CB  1 
ATOM   1224 C  CG  . ASN A 1 156 ? -26.783 -21.725 35.841  1.00 20.28 ? 156 ASN B CG  1 
ATOM   1225 O  OD1 . ASN A 1 156 ? -26.618 -20.619 35.311  1.00 19.68 ? 156 ASN B OD1 1 
ATOM   1226 N  ND2 . ASN A 1 156 ? -26.297 -22.869 35.335  1.00 17.15 ? 156 ASN B ND2 1 
ATOM   1227 N  N   . SER A 1 157 ? -27.814 -18.184 37.228  1.00 19.75 ? 157 SER B N   1 
ATOM   1228 C  CA  . SER A 1 157 ? -28.535 -16.994 36.749  1.00 20.57 ? 157 SER B CA  1 
ATOM   1229 C  C   . SER A 1 157 ? -29.045 -17.262 35.332  1.00 22.17 ? 157 SER B C   1 
ATOM   1230 O  O   . SER A 1 157 ? -30.061 -16.674 34.839  1.00 21.12 ? 157 SER B O   1 
ATOM   1231 C  CB  . SER A 1 157 ? -27.561 -15.781 36.743  1.00 22.08 ? 157 SER B CB  1 
ATOM   1232 O  OG  . SER A 1 157 ? -26.442 -15.991 35.822  1.00 22.78 ? 157 SER B OG  1 
ATOM   1233 N  N   . GLN A 1 158 ? -28.379 -18.217 34.671  1.00 21.78 ? 158 GLN B N   1 
ATOM   1234 C  CA  . GLN A 1 158 ? -28.739 -18.497 33.265  1.00 22.21 ? 158 GLN B CA  1 
ATOM   1235 C  C   . GLN A 1 158 ? -29.994 -19.317 33.144  1.00 22.51 ? 158 GLN B C   1 
ATOM   1236 O  O   . GLN A 1 158 ? -30.509 -19.477 32.031  1.00 21.85 ? 158 GLN B O   1 
ATOM   1237 C  CB  . GLN A 1 158 ? -27.596 -19.176 32.513  1.00 22.72 ? 158 GLN B CB  1 
ATOM   1238 C  CG  . GLN A 1 158 ? -26.329 -18.366 32.484  1.00 26.29 ? 158 GLN B CG  1 
ATOM   1239 C  CD  . GLN A 1 158 ? -26.461 -17.002 31.790  1.00 32.10 ? 158 GLN B CD  1 
ATOM   1240 O  OE1 . GLN A 1 158 ? -27.249 -16.803 30.823  1.00 31.49 ? 158 GLN B OE1 1 
ATOM   1241 N  NE2 . GLN A 1 158 ? -25.649 -16.042 32.276  1.00 35.71 ? 158 GLN B NE2 1 
ATOM   1242 N  N   . LEU A 1 159 ? -30.474 -19.857 34.267  1.00 20.88 ? 159 LEU B N   1 
ATOM   1243 C  CA  . LEU A 1 159 ? -31.786 -20.512 34.265  1.00 21.63 ? 159 LEU B CA  1 
ATOM   1244 C  C   . LEU A 1 159 ? -32.989 -19.552 34.488  1.00 20.48 ? 159 LEU B C   1 
ATOM   1245 O  O   . LEU A 1 159 ? -34.107 -19.996 34.356  1.00 21.58 ? 159 LEU B O   1 
ATOM   1246 C  CB  . LEU A 1 159 ? -31.850 -21.714 35.212  1.00 20.34 ? 159 LEU B CB  1 
ATOM   1247 C  CG  . LEU A 1 159 ? -30.935 -22.912 34.955  1.00 24.07 ? 159 LEU B CG  1 
ATOM   1248 C  CD1 . LEU A 1 159 ? -30.857 -23.673 36.253  1.00 23.39 ? 159 LEU B CD1 1 
ATOM   1249 C  CD2 . LEU A 1 159 ? -31.404 -23.812 33.783  1.00 21.17 ? 159 LEU B CD2 1 
ATOM   1250 N  N   . GLN A 1 160 ? -32.765 -18.253 34.761  1.00 20.92 ? 160 GLN B N   1 
ATOM   1251 C  CA  . GLN A 1 160 ? -33.853 -17.327 35.120  1.00 20.97 ? 160 GLN B CA  1 
ATOM   1252 C  C   . GLN A 1 160 ? -34.905 -17.148 34.027  1.00 20.35 ? 160 GLN B C   1 
ATOM   1253 O  O   . GLN A 1 160 ? -36.080 -17.138 34.315  1.00 22.12 ? 160 GLN B O   1 
ATOM   1254 C  CB  . GLN A 1 160 ? -33.319 -15.905 35.513  1.00 22.42 ? 160 GLN B CB  1 
ATOM   1255 C  CG  . GLN A 1 160 ? -34.463 -14.943 36.003  1.00 19.49 ? 160 GLN B CG  1 
ATOM   1256 C  CD  . GLN A 1 160 ? -34.145 -13.461 35.909  1.00 22.77 ? 160 GLN B CD  1 
ATOM   1257 O  OE1 . GLN A 1 160 ? -32.979 -13.065 35.876  1.00 28.23 ? 160 GLN B OE1 1 
ATOM   1258 N  NE2 . GLN A 1 160 ? -35.185 -12.629 35.892  1.00 23.78 ? 160 GLN B NE2 1 
ATOM   1259 N  N   . LYS A 1 161 ? -34.489 -16.952 32.790  1.00 19.85 ? 161 LYS B N   1 
ATOM   1260 C  CA  . LYS A 1 161 ? -35.449 -16.794 31.714  1.00 19.33 ? 161 LYS B CA  1 
ATOM   1261 C  C   . LYS A 1 161 ? -36.482 -17.942 31.768  1.00 18.59 ? 161 LYS B C   1 
ATOM   1262 O  O   . LYS A 1 161 ? -37.688 -17.692 31.665  1.00 18.24 ? 161 LYS B O   1 
ATOM   1263 C  CB  . LYS A 1 161 ? -34.781 -16.785 30.330  1.00 18.76 ? 161 LYS B CB  1 
ATOM   1264 C  CG  . LYS A 1 161 ? -35.686 -16.005 29.243  1.00 20.07 ? 161 LYS B CG  1 
ATOM   1265 C  CD  . LYS A 1 161 ? -35.166 -16.227 27.852  1.00 18.52 ? 161 LYS B CD  1 
ATOM   1266 C  CE  . LYS A 1 161 ? -36.253 -16.079 26.818  1.00 18.52 ? 161 LYS B CE  1 
ATOM   1267 N  NZ  . LYS A 1 161 ? -36.690 -14.604 26.927  1.00 21.87 ? 161 LYS B NZ  1 
ATOM   1268 N  N   . ILE A 1 162 ? -35.989 -19.170 31.944  1.00 17.92 ? 162 ILE B N   1 
ATOM   1269 C  CA  . ILE A 1 162 ? -36.831 -20.392 32.035  1.00 16.42 ? 162 ILE B CA  1 
ATOM   1270 C  C   . ILE A 1 162 ? -37.670 -20.463 33.333  1.00 16.19 ? 162 ILE B C   1 
ATOM   1271 O  O   . ILE A 1 162 ? -38.887 -20.613 33.291  1.00 16.00 ? 162 ILE B O   1 
ATOM   1272 C  CB  . ILE A 1 162 ? -35.948 -21.714 31.945  1.00 15.62 ? 162 ILE B CB  1 
ATOM   1273 C  CG1 . ILE A 1 162 ? -35.271 -21.871 30.578  1.00 16.37 ? 162 ILE B CG1 1 
ATOM   1274 C  CG2 . ILE A 1 162 ? -36.811 -23.047 32.218  1.00 15.08 ? 162 ILE B CG2 1 
ATOM   1275 C  CD1 . ILE A 1 162 ? -34.173 -23.033 30.581  1.00 14.47 ? 162 ILE B CD1 1 
ATOM   1276 N  N   . THR A 1 163 ? -37.020 -20.370 34.490  1.00 17.43 ? 163 THR B N   1 
ATOM   1277 C  CA  . THR A 1 163 ? -37.757 -20.469 35.746  1.00 19.25 ? 163 THR B CA  1 
ATOM   1278 C  C   . THR A 1 163 ? -38.853 -19.374 35.937  1.00 18.62 ? 163 THR B C   1 
ATOM   1279 O  O   . THR A 1 163 ? -39.901 -19.693 36.526  1.00 20.07 ? 163 THR B O   1 
ATOM   1280 C  CB  . THR A 1 163 ? -36.853 -20.537 36.996  1.00 18.42 ? 163 THR B CB  1 
ATOM   1281 O  OG1 . THR A 1 163 ? -36.063 -19.353 37.070  1.00 21.45 ? 163 THR B OG1 1 
ATOM   1282 C  CG2 . THR A 1 163 ? -35.927 -21.808 36.923  1.00 20.34 ? 163 THR B CG2 1 
ATOM   1283 N  N   . ASP A 1 164 ? -38.577 -18.130 35.499  1.00 19.04 ? 164 ASP B N   1 
ATOM   1284 C  CA  . ASP A 1 164 ? -39.598 -17.045 35.412  1.00 19.92 ? 164 ASP B CA  1 
ATOM   1285 C  C   . ASP A 1 164 ? -40.868 -17.408 34.646  1.00 20.40 ? 164 ASP B C   1 
ATOM   1286 O  O   . ASP A 1 164 ? -41.898 -16.765 34.811  1.00 19.45 ? 164 ASP B O   1 
ATOM   1287 C  CB  . ASP A 1 164 ? -39.048 -15.799 34.718  1.00 21.43 ? 164 ASP B CB  1 
ATOM   1288 C  CG  . ASP A 1 164 ? -38.131 -14.974 35.612  1.00 24.89 ? 164 ASP B CG  1 
ATOM   1289 O  OD1 . ASP A 1 164 ? -38.073 -15.285 36.842  1.00 30.28 ? 164 ASP B OD1 1 
ATOM   1290 O  OD2 . ASP A 1 164 ? -37.442 -14.061 35.058  1.00 24.73 ? 164 ASP B OD2 1 
ATOM   1291 N  N   . THR A 1 165 ? -40.801 -18.409 33.763  1.00 19.85 ? 165 THR B N   1 
ATOM   1292 C  CA  . THR A 1 165 ? -42.000 -18.792 32.988  1.00 18.60 ? 165 THR B CA  1 
ATOM   1293 C  C   . THR A 1 165 ? -42.803 -19.921 33.544  1.00 17.72 ? 165 THR B C   1 
ATOM   1294 O  O   . THR A 1 165 ? -43.892 -20.152 33.054  1.00 16.57 ? 165 THR B O   1 
ATOM   1295 C  CB  . THR A 1 165 ? -41.667 -19.248 31.558  1.00 18.91 ? 165 THR B CB  1 
ATOM   1296 O  OG1 . THR A 1 165 ? -40.965 -20.501 31.632  1.00 19.99 ? 165 THR B OG1 1 
ATOM   1297 C  CG2 . THR A 1 165 ? -40.866 -18.259 30.870  1.00 19.01 ? 165 THR B CG2 1 
ATOM   1298 N  N   . LEU A 1 166 ? -42.288 -20.633 34.538  1.00 16.81 ? 166 LEU B N   1 
ATOM   1299 C  CA  . LEU A 1 166 ? -42.881 -21.880 34.937  1.00 18.21 ? 166 LEU B CA  1 
ATOM   1300 C  C   . LEU A 1 166 ? -44.298 -21.739 35.481  1.00 19.31 ? 166 LEU B C   1 
ATOM   1301 O  O   . LEU A 1 166 ? -45.171 -22.607 35.221  1.00 19.28 ? 166 LEU B O   1 
ATOM   1302 C  CB  . LEU A 1 166 ? -41.990 -22.741 35.855  1.00 17.72 ? 166 LEU B CB  1 
ATOM   1303 C  CG  . LEU A 1 166 ? -40.566 -23.055 35.354  1.00 17.66 ? 166 LEU B CG  1 
ATOM   1304 C  CD1 . LEU A 1 166 ? -39.693 -23.697 36.444  1.00 15.47 ? 166 LEU B CD1 1 
ATOM   1305 C  CD2 . LEU A 1 166 ? -40.666 -23.985 34.185  1.00 17.20 ? 166 LEU B CD2 1 
ATOM   1306 N  N   . ASP A 1 167 ? -44.584 -20.613 36.112  1.00 20.75 ? 167 ASP B N   1 
ATOM   1307 C  CA  . ASP A 1 167 ? -45.950 -20.435 36.622  1.00 22.02 ? 167 ASP B CA  1 
ATOM   1308 C  C   . ASP A 1 167 ? -46.996 -20.383 35.500  1.00 22.06 ? 167 ASP B C   1 
ATOM   1309 O  O   . ASP A 1 167 ? -48.024 -21.046 35.544  1.00 22.70 ? 167 ASP B O   1 
ATOM   1310 C  CB  . ASP A 1 167 ? -46.011 -19.213 37.500  1.00 23.23 ? 167 ASP B CB  1 
ATOM   1311 C  CG  . ASP A 1 167 ? -45.409 -19.478 38.862  1.00 27.52 ? 167 ASP B CG  1 
ATOM   1312 O  OD1 . ASP A 1 167 ? -45.296 -20.688 39.242  1.00 29.46 ? 167 ASP B OD1 1 
ATOM   1313 O  OD2 . ASP A 1 167 ? -45.020 -18.488 39.510  1.00 32.21 ? 167 ASP B OD2 1 
ATOM   1314 N  N   . SER A 1 168 ? -46.719 -19.569 34.498  1.00 21.94 ? 168 SER B N   1 
ATOM   1315 C  CA  . SER A 1 168 ? -47.538 -19.482 33.269  1.00 20.60 ? 168 SER B CA  1 
ATOM   1316 C  C   . SER A 1 168 ? -47.711 -20.794 32.463  1.00 19.25 ? 168 SER B C   1 
ATOM   1317 O  O   . SER A 1 168 ? -48.698 -20.940 31.742  1.00 16.61 ? 168 SER B O   1 
ATOM   1318 C  CB  . SER A 1 168 ? -46.926 -18.413 32.373  1.00 20.98 ? 168 SER B CB  1 
ATOM   1319 O  OG  . SER A 1 168 ? -45.767 -18.988 31.743  1.00 23.37 ? 168 SER B OG  1 
ATOM   1320 N  N   . ILE A 1 169 ? -46.808 -21.773 32.628  1.00 17.14 ? 169 ILE B N   1 
ATOM   1321 C  CA  . ILE A 1 169 ? -46.954 -23.074 31.929  1.00 17.26 ? 169 ILE B CA  1 
ATOM   1322 C  C   . ILE A 1 169 ? -47.186 -24.237 32.905  1.00 17.23 ? 169 ILE B C   1 
ATOM   1323 O  O   . ILE A 1 169 ? -46.808 -25.377 32.638  1.00 17.89 ? 169 ILE B O   1 
ATOM   1324 C  CB  . ILE A 1 169 ? -45.764 -23.348 30.944  1.00 16.75 ? 169 ILE B CB  1 
ATOM   1325 C  CG1 . ILE A 1 169 ? -44.402 -23.403 31.683  1.00 13.02 ? 169 ILE B CG1 1 
ATOM   1326 C  CG2 . ILE A 1 169 ? -45.773 -22.250 29.817  1.00 17.34 ? 169 ILE B CG2 1 
ATOM   1327 C  CD1 . ILE A 1 169 ? -43.211 -23.894 30.786  1.00 17.39 ? 169 ILE B CD1 1 
ATOM   1328 N  N   . LYS A 1 170 ? -47.804 -23.951 34.062  1.00 18.35 ? 170 LYS B N   1 
ATOM   1329 C  CA  . LYS A 1 170 ? -47.981 -24.968 35.091  1.00 17.98 ? 170 LYS B CA  1 
ATOM   1330 C  C   . LYS A 1 170 ? -48.697 -26.232 34.542  1.00 17.99 ? 170 LYS B C   1 
ATOM   1331 O  O   . LYS A 1 170 ? -48.305 -27.374 34.823  1.00 18.21 ? 170 LYS B O   1 
ATOM   1332 C  CB  . LYS A 1 170 ? -48.750 -24.413 36.317  1.00 19.73 ? 170 LYS B CB  1 
ATOM   1333 C  CG  . LYS A 1 170 ? -48.777 -25.469 37.472  1.00 18.34 ? 170 LYS B CG  1 
ATOM   1334 C  CD  . LYS A 1 170 ? -49.742 -25.073 38.669  1.00 22.78 ? 170 LYS B CD  1 
ATOM   1335 C  CE  . LYS A 1 170 ? -49.316 -25.801 40.051  1.00 28.75 ? 170 LYS B CE  1 
ATOM   1336 N  NZ  . LYS A 1 170 ? -47.830 -25.901 40.412  1.00 30.96 ? 170 LYS B NZ  1 
ATOM   1337 N  N   . GLU A 1 171 ? -49.708 -26.007 33.711  1.00 17.10 ? 171 GLU B N   1 
ATOM   1338 C  CA  . GLU A 1 171 ? -50.604 -27.062 33.249  1.00 18.98 ? 171 GLU B CA  1 
ATOM   1339 C  C   . GLU A 1 171 ? -50.058 -27.594 31.914  1.00 17.54 ? 171 GLU B C   1 
ATOM   1340 O  O   . GLU A 1 171 ? -49.648 -26.810 31.061  1.00 17.17 ? 171 GLU B O   1 
ATOM   1341 C  CB  . GLU A 1 171 ? -52.036 -26.507 33.053  1.00 19.90 ? 171 GLU B CB  1 
ATOM   1342 C  CG  . GLU A 1 171 ? -52.822 -26.082 34.368  1.00 23.54 ? 171 GLU B CG  1 
ATOM   1343 C  CD  . GLU A 1 171 ? -52.390 -24.713 34.966  1.00 30.19 ? 171 GLU B CD  1 
ATOM   1344 O  OE1 . GLU A 1 171 ? -52.610 -24.504 36.200  1.00 39.30 ? 171 GLU B OE1 1 
ATOM   1345 O  OE2 . GLU A 1 171 ? -51.826 -23.838 34.253  1.00 30.77 ? 171 GLU B OE2 1 
ATOM   1346 N  N   . LYS A 1 172 ? -50.068 -28.906 31.741  1.00 17.37 ? 172 LYS B N   1 
ATOM   1347 C  CA  . LYS A 1 172 ? -49.785 -29.513 30.443  1.00 16.35 ? 172 LYS B CA  1 
ATOM   1348 C  C   . LYS A 1 172 ? -50.626 -28.791 29.348  1.00 18.43 ? 172 LYS B C   1 
ATOM   1349 O  O   . LYS A 1 172 ? -51.874 -28.586 29.495  1.00 18.09 ? 172 LYS B O   1 
ATOM   1350 C  CB  . LYS A 1 172 ? -50.136 -31.016 30.529  1.00 16.33 ? 172 LYS B CB  1 
ATOM   1351 C  CG  . LYS A 1 172 ? -50.002 -31.813 29.229  1.00 16.02 ? 172 LYS B CG  1 
ATOM   1352 C  CD  . LYS A 1 172 ? -50.422 -33.318 29.395  1.00 14.34 ? 172 LYS B CD  1 
ATOM   1353 C  CE  . LYS A 1 172 ? -50.299 -34.089 28.044  1.00 17.27 ? 172 LYS B CE  1 
ATOM   1354 N  NZ  . LYS A 1 172 ? -50.310 -35.634 28.306  1.00 15.23 ? 172 LYS B NZ  1 
ATOM   1355 N  N   . GLY A 1 173 ? -49.953 -28.409 28.255  1.00 18.93 ? 173 GLY B N   1 
ATOM   1356 C  CA  . GLY A 1 173 ? -50.607 -27.790 27.076  1.00 18.82 ? 173 GLY B CA  1 
ATOM   1357 C  C   . GLY A 1 173 ? -50.415 -26.278 27.034  1.00 19.54 ? 173 GLY B C   1 
ATOM   1358 O  O   . GLY A 1 173 ? -50.602 -25.667 25.983  1.00 21.31 ? 173 GLY B O   1 
ATOM   1359 N  N   . LYS A 1 174 ? -50.044 -25.667 28.175  1.00 18.12 ? 174 LYS B N   1 
ATOM   1360 C  CA  . LYS A 1 174 ? -49.802 -24.234 28.254  1.00 17.51 ? 174 LYS B CA  1 
ATOM   1361 C  C   . LYS A 1 174 ? -48.506 -23.896 27.502  1.00 18.74 ? 174 LYS B C   1 
ATOM   1362 O  O   . LYS A 1 174 ? -47.518 -24.691 27.527  1.00 17.58 ? 174 LYS B O   1 
ATOM   1363 C  CB  . LYS A 1 174 ? -49.682 -23.794 29.706  1.00 20.57 ? 174 LYS B CB  1 
ATOM   1364 C  CG  . LYS A 1 174 ? -51.007 -23.984 30.534  1.00 20.07 ? 174 LYS B CG  1 
ATOM   1365 C  CD  . LYS A 1 174 ? -51.983 -22.901 30.157  1.00 28.09 ? 174 LYS B CD  1 
ATOM   1366 C  CE  . LYS A 1 174 ? -53.308 -23.007 30.916  1.00 32.13 ? 174 LYS B CE  1 
ATOM   1367 N  NZ  . LYS A 1 174 ? -53.150 -22.415 32.322  1.00 38.62 ? 174 LYS B NZ  1 
ATOM   1368 N  N   . GLN A 1 175 ? -48.479 -22.718 26.913  1.00 16.52 ? 175 GLN B N   1 
ATOM   1369 C  CA  . GLN A 1 175 ? -47.258 -22.255 26.270  1.00 20.01 ? 175 GLN B CA  1 
ATOM   1370 C  C   . GLN A 1 175 ? -47.206 -20.748 26.394  1.00 18.62 ? 175 GLN B C   1 
ATOM   1371 O  O   . GLN A 1 175 ? -48.249 -20.103 26.593  1.00 20.61 ? 175 GLN B O   1 
ATOM   1372 C  CB  . GLN A 1 175 ? -47.189 -22.694 24.812  1.00 18.60 ? 175 GLN B CB  1 
ATOM   1373 C  CG  . GLN A 1 175 ? -48.169 -21.960 23.923  1.00 22.63 ? 175 GLN B CG  1 
ATOM   1374 C  CD  . GLN A 1 175 ? -48.117 -22.367 22.465  1.00 21.31 ? 175 GLN B CD  1 
ATOM   1375 O  OE1 . GLN A 1 175 ? -48.333 -23.530 22.138  1.00 19.64 ? 175 GLN B OE1 1 
ATOM   1376 N  NE2 . GLN A 1 175 ? -47.817 -21.421 21.599  1.00 21.40 ? 175 GLN B NE2 1 
ATOM   1377 N  N   A THR A 1 176 ? -46.016 -20.181 26.318  0.50 18.29 ? 176 THR B N   1 
ATOM   1378 N  N   B THR A 1 176 ? -46.015 -20.188 26.253  0.50 18.17 ? 176 THR B N   1 
ATOM   1379 C  CA  A THR A 1 176 ? -45.869 -18.723 26.334  0.50 17.96 ? 176 THR B CA  1 
ATOM   1380 C  CA  B THR A 1 176 ? -45.802 -18.737 26.347  0.50 17.76 ? 176 THR B CA  1 
ATOM   1381 C  C   A THR A 1 176 ? -44.725 -18.331 25.438  0.50 17.39 ? 176 THR B C   1 
ATOM   1382 C  C   B THR A 1 176 ? -44.774 -18.366 25.313  0.50 17.37 ? 176 THR B C   1 
ATOM   1383 O  O   A THR A 1 176 ? -43.806 -19.143 25.214  0.50 16.33 ? 176 THR B O   1 
ATOM   1384 O  O   B THR A 1 176 ? -43.922 -19.216 24.987  0.50 16.20 ? 176 THR B O   1 
ATOM   1385 C  CB  A THR A 1 176 ? -45.738 -18.129 27.801  0.50 19.31 ? 176 THR B CB  1 
ATOM   1386 C  CB  B THR A 1 176 ? -45.315 -18.324 27.776  0.50 18.64 ? 176 THR B CB  1 
ATOM   1387 O  OG1 A THR A 1 176 ? -46.016 -16.727 27.787  0.50 19.62 ? 176 THR B OG1 1 
ATOM   1388 O  OG1 B THR A 1 176 ? -43.966 -18.749 27.990  0.50 21.53 ? 176 THR B OG1 1 
ATOM   1389 C  CG2 A THR A 1 176 ? -44.378 -18.360 28.408  0.50 19.35 ? 176 THR B CG2 1 
ATOM   1390 C  CG2 B THR A 1 176 ? -46.205 -18.959 28.844  0.50 16.94 ? 176 THR B CG2 1 
ATOM   1391 N  N   A ARG A 1 177 ? -44.824 -17.131 24.872  0.50 15.89 ? 177 ARG B N   1 
ATOM   1392 N  N   B ARG A 1 177 ? -44.842 -17.153 24.756  0.50 16.25 ? 177 ARG B N   1 
ATOM   1393 C  CA  A ARG A 1 177 ? -43.754 -16.502 24.104  0.50 16.90 ? 177 ARG B CA  1 
ATOM   1394 C  CA  B ARG A 1 177 ? -43.734 -16.694 23.921  0.50 17.21 ? 177 ARG B CA  1 
ATOM   1395 C  C   A ARG A 1 177 ? -42.347 -16.597 24.754  0.50 17.09 ? 177 ARG B C   1 
ATOM   1396 C  C   B ARG A 1 177 ? -42.428 -16.812 24.732  0.50 17.58 ? 177 ARG B C   1 
ATOM   1397 O  O   A ARG A 1 177 ? -42.179 -16.204 25.907  0.50 16.98 ? 177 ARG B O   1 
ATOM   1398 O  O   B ARG A 1 177 ? -42.421 -16.683 25.968  0.50 17.58 ? 177 ARG B O   1 
ATOM   1399 C  CB  A ARG A 1 177 ? -44.081 -15.029 23.936  0.50 15.86 ? 177 ARG B CB  1 
ATOM   1400 C  CB  B ARG A 1 177 ? -43.901 -15.252 23.414  0.50 16.90 ? 177 ARG B CB  1 
ATOM   1401 C  CG  A ARG A 1 177 ? -43.142 -14.342 22.979  0.50 18.71 ? 177 ARG B CG  1 
ATOM   1402 C  CG  B ARG A 1 177 ? -42.747 -14.749 22.455  0.50 17.12 ? 177 ARG B CG  1 
ATOM   1403 C  CD  A ARG A 1 177 ? -43.405 -12.872 22.817  0.50 17.35 ? 177 ARG B CD  1 
ATOM   1404 C  CD  B ARG A 1 177 ? -43.173 -13.571 21.588  0.50 17.71 ? 177 ARG B CD  1 
ATOM   1405 N  NE  A ARG A 1 177 ? -42.746 -12.494 21.578  0.50 17.96 ? 177 ARG B NE  1 
ATOM   1406 N  NE  B ARG A 1 177 ? -42.142 -12.886 20.787  0.50 16.47 ? 177 ARG B NE  1 
ATOM   1407 C  CZ  A ARG A 1 177 ? -41.933 -11.463 21.401  0.50 18.88 ? 177 ARG B CZ  1 
ATOM   1408 C  CZ  B ARG A 1 177 ? -41.624 -13.285 19.625  0.50 15.04 ? 177 ARG B CZ  1 
ATOM   1409 N  NH1 A ARG A 1 177 ? -41.671 -10.630 22.389  0.50 23.82 ? 177 ARG B NH1 1 
ATOM   1410 N  NH1 B ARG A 1 177 ? -41.947 -14.447 19.080  0.50 15.77 ? 177 ARG B NH1 1 
ATOM   1411 N  NH2 A ARG A 1 177 ? -41.394 -11.260 20.201  0.50 18.80 ? 177 ARG B NH2 1 
ATOM   1412 N  NH2 B ARG A 1 177 ? -40.733 -12.500 18.988  0.50 18.80 ? 177 ARG B NH2 1 
ATOM   1413 N  N   . PHE A 1 178 ? -41.338 -17.087 24.026  1.00 17.56 ? 178 PHE B N   1 
ATOM   1414 C  CA  . PHE A 1 178 ? -40.011 -17.274 24.653  1.00 17.67 ? 178 PHE B CA  1 
ATOM   1415 C  C   . PHE A 1 178 ? -38.988 -17.089 23.597  1.00 19.06 ? 178 PHE B C   1 
ATOM   1416 O  O   . PHE A 1 178 ? -38.698 -18.040 22.839  1.00 20.67 ? 178 PHE B O   1 
ATOM   1417 C  CB  . PHE A 1 178 ? -39.903 -18.716 25.168  1.00 16.59 ? 178 PHE B CB  1 
ATOM   1418 C  CG  . PHE A 1 178 ? -38.802 -18.937 26.140  1.00 14.02 ? 178 PHE B CG  1 
ATOM   1419 C  CD1 . PHE A 1 178 ? -38.946 -18.553 27.471  1.00 13.23 ? 178 PHE B CD1 1 
ATOM   1420 C  CD2 . PHE A 1 178 ? -37.632 -19.550 25.727  1.00 12.70 ? 178 PHE B CD2 1 
ATOM   1421 C  CE1 . PHE A 1 178 ? -37.879 -18.786 28.376  1.00 17.29 ? 178 PHE B CE1 1 
ATOM   1422 C  CE2 . PHE A 1 178 ? -36.585 -19.745 26.581  1.00 13.25 ? 178 PHE B CE2 1 
ATOM   1423 C  CZ  . PHE A 1 178 ? -36.697 -19.414 27.899  1.00 14.61 ? 178 PHE B CZ  1 
ATOM   1424 N  N   . THR A 1 179 ? -38.442 -15.888 23.516  1.00 20.56 ? 179 THR B N   1 
ATOM   1425 C  CA  . THR A 1 179 ? -37.380 -15.583 22.541  1.00 19.88 ? 179 THR B CA  1 
ATOM   1426 C  C   . THR A 1 179 ? -36.275 -14.839 23.179  1.00 20.89 ? 179 THR B C   1 
ATOM   1427 O  O   . THR A 1 179 ? -36.326 -14.523 24.363  1.00 21.40 ? 179 THR B O   1 
ATOM   1428 C  CB  . THR A 1 179 ? -37.897 -14.917 21.264  1.00 22.85 ? 179 THR B CB  1 
ATOM   1429 O  OG1 . THR A 1 179 ? -36.911 -15.072 20.186  1.00 23.39 ? 179 THR B OG1 1 
ATOM   1430 C  CG2 . THR A 1 179 ? -38.377 -13.453 21.525  1.00 17.93 ? 179 THR B CG2 1 
ATOM   1431 N  N   . ASN A 1 180 ? -35.218 -14.618 22.417  1.00 20.67 ? 180 ASN B N   1 
ATOM   1432 C  CA  . ASN A 1 180 ? -34.030 -13.968 22.912  1.00 21.14 ? 180 ASN B CA  1 
ATOM   1433 C  C   . ASN A 1 180 ? -33.433 -14.743 24.059  1.00 20.03 ? 180 ASN B C   1 
ATOM   1434 O  O   . ASN A 1 180 ? -33.180 -14.199 25.145  1.00 20.43 ? 180 ASN B O   1 
ATOM   1435 C  CB  . ASN A 1 180 ? -34.249 -12.437 23.139  1.00 22.51 ? 180 ASN B CB  1 
ATOM   1436 C  CG  . ASN A 1 180 ? -34.739 -11.730 21.817  1.00 25.22 ? 180 ASN B CG  1 
ATOM   1437 O  OD1 . ASN A 1 180 ? -34.188 -11.963 20.728  1.00 30.11 ? 180 ASN B OD1 1 
ATOM   1438 N  ND2 . ASN A 1 180 ? -35.798 -10.921 21.920  1.00 29.15 ? 180 ASN B ND2 1 
ATOM   1439 N  N   . PHE A 1 181 ? -33.238 -16.036 23.794  1.00 18.45 ? 181 PHE B N   1 
ATOM   1440 C  CA  . PHE A 1 181 ? -32.856 -17.023 24.812  1.00 17.48 ? 181 PHE B CA  1 
ATOM   1441 C  C   . PHE A 1 181 ? -31.425 -17.369 24.559  1.00 17.07 ? 181 PHE B C   1 
ATOM   1442 O  O   . PHE A 1 181 ? -31.082 -17.848 23.504  1.00 17.06 ? 181 PHE B O   1 
ATOM   1443 C  CB  . PHE A 1 181 ? -33.736 -18.310 24.738  1.00 18.11 ? 181 PHE B CB  1 
ATOM   1444 C  CG  . PHE A 1 181 ? -33.220 -19.460 25.602  1.00 17.72 ? 181 PHE B CG  1 
ATOM   1445 C  CD1 . PHE A 1 181 ? -32.858 -19.227 26.929  1.00 16.33 ? 181 PHE B CD1 1 
ATOM   1446 C  CD2 . PHE A 1 181 ? -33.166 -20.749 25.090  1.00 16.20 ? 181 PHE B CD2 1 
ATOM   1447 C  CE1 . PHE A 1 181 ? -32.392 -20.247 27.742  1.00 16.38 ? 181 PHE B CE1 1 
ATOM   1448 C  CE2 . PHE A 1 181 ? -32.720 -21.841 25.892  1.00 18.49 ? 181 PHE B CE2 1 
ATOM   1449 C  CZ  . PHE A 1 181 ? -32.338 -21.587 27.232  1.00 18.12 ? 181 PHE B CZ  1 
ATOM   1450 N  N   . ASP A 1 182 ? -30.581 -17.047 25.510  1.00 15.85 ? 182 ASP B N   1 
ATOM   1451 C  CA  . ASP A 1 182 ? -29.168 -17.345 25.429  1.00 16.74 ? 182 ASP B CA  1 
ATOM   1452 C  C   . ASP A 1 182 ? -28.868 -18.800 25.840  1.00 16.09 ? 182 ASP B C   1 
ATOM   1453 O  O   . ASP A 1 182 ? -28.493 -19.075 26.928  1.00 16.47 ? 182 ASP B O   1 
ATOM   1454 C  CB  . ASP A 1 182 ? -28.366 -16.347 26.274  1.00 16.99 ? 182 ASP B CB  1 
ATOM   1455 C  CG  . ASP A 1 182 ? -26.876 -16.578 26.193  1.00 16.48 ? 182 ASP B CG  1 
ATOM   1456 O  OD1 . ASP A 1 182 ? -26.408 -17.466 25.439  1.00 20.32 ? 182 ASP B OD1 1 
ATOM   1457 O  OD2 . ASP A 1 182 ? -26.180 -15.869 26.946  1.00 16.43 ? 182 ASP B OD2 1 
ATOM   1458 N  N   . LEU A 1 183 ? -29.026 -19.705 24.887  1.00 15.36 ? 183 LEU B N   1 
ATOM   1459 C  CA  . LEU A 1 183 ? -28.794 -21.120 25.144  1.00 14.77 ? 183 LEU B CA  1 
ATOM   1460 C  C   . LEU A 1 183 ? -27.290 -21.405 25.365  1.00 15.09 ? 183 LEU B C   1 
ATOM   1461 O  O   . LEU A 1 183 ? -26.860 -22.226 26.250  1.00 15.01 ? 183 LEU B O   1 
ATOM   1462 C  CB  . LEU A 1 183 ? -29.406 -21.923 23.980  1.00 13.12 ? 183 LEU B CB  1 
ATOM   1463 C  CG  . LEU A 1 183 ? -29.158 -23.433 24.096  1.00 15.05 ? 183 LEU B CG  1 
ATOM   1464 C  CD1 . LEU A 1 183 ? -29.651 -24.016 25.484  1.00 11.58 ? 183 LEU B CD1 1 
ATOM   1465 C  CD2 . LEU A 1 183 ? -29.827 -24.054 22.891  1.00 15.76 ? 183 LEU B CD2 1 
ATOM   1466 N  N   . LEU A 1 184 ? -26.493 -20.728 24.575  1.00 16.38 ? 184 LEU B N   1 
ATOM   1467 C  CA  . LEU A 1 184 ? -25.057 -20.874 24.601  1.00 19.22 ? 184 LEU B CA  1 
ATOM   1468 C  C   . LEU A 1 184 ? -24.492 -20.767 26.023  1.00 19.67 ? 184 LEU B C   1 
ATOM   1469 O  O   . LEU A 1 184 ? -23.702 -21.589 26.423  1.00 17.57 ? 184 LEU B O   1 
ATOM   1470 C  CB  . LEU A 1 184 ? -24.403 -19.847 23.657  1.00 19.87 ? 184 LEU B CB  1 
ATOM   1471 C  CG  . LEU A 1 184 ? -22.950 -20.219 23.376  1.00 22.76 ? 184 LEU B CG  1 
ATOM   1472 C  CD1 . LEU A 1 184 ? -22.868 -21.625 22.671  1.00 22.59 ? 184 LEU B CD1 1 
ATOM   1473 C  CD2 . LEU A 1 184 ? -22.270 -19.134 22.570  1.00 20.81 ? 184 LEU B CD2 1 
ATOM   1474 N  N   . SER A 1 185 ? -24.981 -19.786 26.794  1.00 20.10 ? 185 SER B N   1 
ATOM   1475 C  CA  . SER A 1 185 ? -24.532 -19.547 28.144  1.00 20.08 ? 185 SER B CA  1 
ATOM   1476 C  C   . SER A 1 185 ? -24.970 -20.590 29.131  1.00 20.82 ? 185 SER B C   1 
ATOM   1477 O  O   . SER A 1 185 ? -24.500 -20.605 30.275  1.00 18.78 ? 185 SER B O   1 
ATOM   1478 C  CB  . SER A 1 185 ? -24.914 -18.140 28.609  1.00 21.05 ? 185 SER B CB  1 
ATOM   1479 O  OG  . SER A 1 185 ? -24.263 -17.186 27.760  1.00 23.42 ? 185 SER B OG  1 
ATOM   1480 N  N   . LEU A 1 186 ? -25.852 -21.503 28.694  1.00 18.97 ? 186 LEU B N   1 
ATOM   1481 C  CA  . LEU A 1 186 ? -26.261 -22.566 29.594  1.00 19.38 ? 186 LEU B CA  1 
ATOM   1482 C  C   . LEU A 1 186 ? -25.230 -23.705 29.561  1.00 19.88 ? 186 LEU B C   1 
ATOM   1483 O  O   . LEU A 1 186 ? -25.193 -24.567 30.450  1.00 24.13 ? 186 LEU B O   1 
ATOM   1484 C  CB  . LEU A 1 186 ? -27.666 -23.109 29.234  1.00 19.06 ? 186 LEU B CB  1 
ATOM   1485 C  CG  . LEU A 1 186 ? -28.842 -22.608 30.075  1.00 22.23 ? 186 LEU B CG  1 
ATOM   1486 C  CD1 . LEU A 1 186 ? -30.123 -23.380 29.734  1.00 23.95 ? 186 LEU B CD1 1 
ATOM   1487 C  CD2 . LEU A 1 186 ? -28.550 -22.744 31.590  1.00 19.41 ? 186 LEU B CD2 1 
ATOM   1488 N  N   . LEU A 1 187 ? -24.393 -23.731 28.555  1.00 17.97 ? 187 LEU B N   1 
ATOM   1489 C  CA  . LEU A 1 187 ? -23.401 -24.795 28.442  1.00 17.81 ? 187 LEU B CA  1 
ATOM   1490 C  C   . LEU A 1 187 ? -22.269 -24.550 29.421  1.00 16.98 ? 187 LEU B C   1 
ATOM   1491 O  O   . LEU A 1 187 ? -21.980 -23.384 29.710  1.00 16.85 ? 187 LEU B O   1 
ATOM   1492 C  CB  . LEU A 1 187 ? -22.905 -24.864 27.016  1.00 15.36 ? 187 LEU B CB  1 
ATOM   1493 C  CG  . LEU A 1 187 ? -23.995 -25.118 25.953  1.00 20.07 ? 187 LEU B CG  1 
ATOM   1494 C  CD1 . LEU A 1 187 ? -23.323 -25.436 24.574  1.00 18.88 ? 187 LEU B CD1 1 
ATOM   1495 C  CD2 . LEU A 1 187 ? -25.091 -26.157 26.261  1.00 19.04 ? 187 LEU B CD2 1 
ATOM   1496 N  N   . PRO A 1 188 ? -21.591 -25.631 29.904  1.00 16.45 ? 188 PRO B N   1 
ATOM   1497 C  CA  . PRO A 1 188 ? -20.413 -25.424 30.744  1.00 15.70 ? 188 PRO B CA  1 
ATOM   1498 C  C   . PRO A 1 188 ? -19.237 -24.900 29.868  1.00 17.47 ? 188 PRO B C   1 
ATOM   1499 O  O   . PRO A 1 188 ? -19.300 -24.989 28.638  1.00 14.58 ? 188 PRO B O   1 
ATOM   1500 C  CB  . PRO A 1 188 ? -20.051 -26.869 31.237  1.00 15.51 ? 188 PRO B CB  1 
ATOM   1501 C  CG  . PRO A 1 188 ? -20.441 -27.739 30.029  1.00 14.32 ? 188 PRO B CG  1 
ATOM   1502 C  CD  . PRO A 1 188 ? -21.801 -27.079 29.629  1.00 16.20 ? 188 PRO B CD  1 
ATOM   1503 N  N   . PRO A 1 189 ? -18.184 -24.328 30.508  1.00 17.17 ? 189 PRO B N   1 
ATOM   1504 C  CA  . PRO A 1 189 ? -17.014 -23.782 29.809  1.00 17.77 ? 189 PRO B CA  1 
ATOM   1505 C  C   . PRO A 1 189 ? -16.327 -24.806 28.950  1.00 16.18 ? 189 PRO B C   1 
ATOM   1506 O  O   . PRO A 1 189 ? -15.948 -24.518 27.804  1.00 14.36 ? 189 PRO B O   1 
ATOM   1507 C  CB  . PRO A 1 189 ? -16.110 -23.319 30.965  1.00 18.81 ? 189 PRO B CB  1 
ATOM   1508 C  CG  . PRO A 1 189 ? -17.000 -22.992 32.006  1.00 20.06 ? 189 PRO B CG  1 
ATOM   1509 C  CD  . PRO A 1 189 ? -18.084 -24.072 31.948  1.00 17.85 ? 189 PRO B CD  1 
ATOM   1510 N  N   . SER A 1 190 ? -16.128 -25.998 29.513  1.00 15.55 ? 190 SER B N   1 
ATOM   1511 C  CA  . SER A 1 190 ? -15.494 -27.093 28.770  1.00 15.33 ? 190 SER B CA  1 
ATOM   1512 C  C   . SER A 1 190 ? -16.601 -27.917 28.056  1.00 14.44 ? 190 SER B C   1 
ATOM   1513 O  O   . SER A 1 190 ? -17.581 -28.351 28.698  1.00 12.98 ? 190 SER B O   1 
ATOM   1514 C  CB  . SER A 1 190 ? -14.707 -28.036 29.703  1.00 14.51 ? 190 SER B CB  1 
ATOM   1515 O  OG  . SER A 1 190 ? -14.216 -29.109 28.952  1.00 15.69 ? 190 SER B OG  1 
ATOM   1516 N  N   . TRP A 1 191 ? -16.364 -28.181 26.773  1.00 13.83 ? 191 TRP B N   1 
ATOM   1517 C  CA  . TRP A 1 191 ? -17.248 -28.998 25.925  1.00 15.25 ? 191 TRP B CA  1 
ATOM   1518 C  C   . TRP A 1 191 ? -16.735 -30.415 25.636  1.00 15.01 ? 191 TRP B C   1 
ATOM   1519 O  O   . TRP A 1 191 ? -17.286 -31.087 24.748  1.00 14.32 ? 191 TRP B O   1 
ATOM   1520 C  CB  . TRP A 1 191 ? -17.632 -28.268 24.604  1.00 14.96 ? 191 TRP B CB  1 
ATOM   1521 C  CG  . TRP A 1 191 ? -18.262 -26.916 24.805  1.00 14.77 ? 191 TRP B CG  1 
ATOM   1522 C  CD1 . TRP A 1 191 ? -18.799 -26.421 25.981  1.00 17.64 ? 191 TRP B CD1 1 
ATOM   1523 C  CD2 . TRP A 1 191 ? -18.538 -25.923 23.797  1.00 15.13 ? 191 TRP B CD2 1 
ATOM   1524 N  NE1 . TRP A 1 191 ? -19.322 -25.160 25.762  1.00 17.57 ? 191 TRP B NE1 1 
ATOM   1525 C  CE2 . TRP A 1 191 ? -19.203 -24.861 24.423  1.00 17.15 ? 191 TRP B CE2 1 
ATOM   1526 C  CE3 . TRP A 1 191 ? -18.289 -25.844 22.423  1.00 15.02 ? 191 TRP B CE3 1 
ATOM   1527 C  CZ2 . TRP A 1 191 ? -19.597 -23.678 23.722  1.00 19.29 ? 191 TRP B CZ2 1 
ATOM   1528 C  CZ3 . TRP A 1 191 ? -18.703 -24.707 21.712  1.00 14.27 ? 191 TRP B CZ3 1 
ATOM   1529 C  CH2 . TRP A 1 191 ? -19.359 -23.627 22.373  1.00 13.96 ? 191 TRP B CH2 1 
ATOM   1530 N  N   . ASP A 1 192 ? -15.772 -30.902 26.438  1.00 13.09 ? 192 ASP B N   1 
ATOM   1531 C  CA  . ASP A 1 192 ? -15.375 -32.280 26.339  1.00 13.09 ? 192 ASP B CA  1 
ATOM   1532 C  C   . ASP A 1 192 ? -16.622 -33.142 26.529  1.00 12.30 ? 192 ASP B C   1 
ATOM   1533 O  O   . ASP A 1 192 ? -17.492 -32.813 27.369  1.00 12.57 ? 192 ASP B O   1 
ATOM   1534 C  CB  . ASP A 1 192 ? -14.366 -32.611 27.413  1.00 13.15 ? 192 ASP B CB  1 
ATOM   1535 C  CG  . ASP A 1 192 ? -13.005 -31.910 27.197  1.00 16.30 ? 192 ASP B CG  1 
ATOM   1536 O  OD1 . ASP A 1 192 ? -12.735 -31.413 26.083  1.00 17.92 ? 192 ASP B OD1 1 
ATOM   1537 O  OD2 . ASP A 1 192 ? -12.251 -31.912 28.174  1.00 18.41 ? 192 ASP B OD2 1 
ATOM   1538 N  N   . TYR A 1 193 ? -16.706 -34.203 25.736  1.00 11.88 ? 193 TYR B N   1 
ATOM   1539 C  CA  . TYR A 1 193 ? -17.905 -35.029 25.776  1.00 12.82 ? 193 TYR B CA  1 
ATOM   1540 C  C   . TYR A 1 193 ? -17.613 -36.511 25.513  1.00 13.51 ? 193 TYR B C   1 
ATOM   1541 O  O   . TYR A 1 193 ? -16.550 -36.869 24.995  1.00 14.34 ? 193 TYR B O   1 
ATOM   1542 C  CB  . TYR A 1 193 ? -18.879 -34.463 24.751  1.00 13.51 ? 193 TYR B CB  1 
ATOM   1543 C  CG  . TYR A 1 193 ? -18.336 -34.548 23.349  1.00 14.68 ? 193 TYR B CG  1 
ATOM   1544 C  CD1 . TYR A 1 193 ? -18.458 -35.748 22.634  1.00 13.23 ? 193 TYR B CD1 1 
ATOM   1545 C  CD2 . TYR A 1 193 ? -17.643 -33.431 22.745  1.00 14.75 ? 193 TYR B CD2 1 
ATOM   1546 C  CE1 . TYR A 1 193 ? -17.971 -35.858 21.347  1.00 18.74 ? 193 TYR B CE1 1 
ATOM   1547 C  CE2 . TYR A 1 193 ? -17.118 -33.557 21.430  1.00 11.32 ? 193 TYR B CE2 1 
ATOM   1548 C  CZ  . TYR A 1 193 ? -17.300 -34.789 20.765  1.00 15.55 ? 193 TYR B CZ  1 
ATOM   1549 O  OH  . TYR A 1 193 ? -16.799 -35.009 19.467  1.00 18.79 ? 193 TYR B OH  1 
ATOM   1550 N  N   . TRP A 1 194 ? -18.586 -37.355 25.839  1.00 13.69 ? 194 TRP B N   1 
ATOM   1551 C  CA  . TRP A 1 194 ? -18.658 -38.701 25.323  1.00 14.33 ? 194 TRP B CA  1 
ATOM   1552 C  C   . TRP A 1 194 ? -19.783 -38.782 24.276  1.00 13.19 ? 194 TRP B C   1 
ATOM   1553 O  O   . TRP A 1 194 ? -20.753 -38.042 24.320  1.00 15.25 ? 194 TRP B O   1 
ATOM   1554 C  CB  . TRP A 1 194 ? -18.994 -39.685 26.440  1.00 15.04 ? 194 TRP B CB  1 
ATOM   1555 C  CG  . TRP A 1 194 ? -18.034 -39.612 27.632  1.00 14.85 ? 194 TRP B CG  1 
ATOM   1556 C  CD1 . TRP A 1 194 ? -16.774 -40.169 27.717  1.00 16.16 ? 194 TRP B CD1 1 
ATOM   1557 C  CD2 . TRP A 1 194 ? -18.264 -38.942 28.875  1.00 11.66 ? 194 TRP B CD2 1 
ATOM   1558 N  NE1 . TRP A 1 194 ? -16.215 -39.863 28.921  1.00 13.17 ? 194 TRP B NE1 1 
ATOM   1559 C  CE2 . TRP A 1 194 ? -17.107 -39.143 29.669  1.00 12.82 ? 194 TRP B CE2 1 
ATOM   1560 C  CE3 . TRP A 1 194 ? -19.341 -38.208 29.398  1.00 10.18 ? 194 TRP B CE3 1 
ATOM   1561 C  CZ2 . TRP A 1 194 ? -16.971 -38.634 30.997  1.00 14.66 ? 194 TRP B CZ2 1 
ATOM   1562 C  CZ3 . TRP A 1 194 ? -19.217 -37.676 30.750  1.00 16.28 ? 194 TRP B CZ3 1 
ATOM   1563 C  CH2 . TRP A 1 194 ? -18.014 -37.906 31.511  1.00 14.42 ? 194 TRP B CH2 1 
ATOM   1564 N  N   . THR A 1 195 ? -19.675 -39.746 23.399  1.00 13.74 ? 195 THR B N   1 
ATOM   1565 C  CA  . THR A 1 195 ? -20.631 -39.908 22.326  1.00 13.38 ? 195 THR B CA  1 
ATOM   1566 C  C   . THR A 1 195 ? -20.860 -41.377 22.075  1.00 13.85 ? 195 THR B C   1 
ATOM   1567 O  O   . THR A 1 195 ? -19.945 -42.208 22.297  1.00 14.06 ? 195 THR B O   1 
ATOM   1568 C  CB  . THR A 1 195 ? -20.227 -39.119 21.043  1.00 13.12 ? 195 THR B CB  1 
ATOM   1569 O  OG1 . THR A 1 195 ? -21.243 -39.346 20.056  1.00 10.62 ? 195 THR B OG1 1 
ATOM   1570 C  CG2 . THR A 1 195 ? -18.820 -39.540 20.481  1.00 14.10 ? 195 THR B CG2 1 
ATOM   1571 N  N   . TYR A 1 196 ? -22.113 -41.706 21.744  1.00 13.33 ? 196 TYR B N   1 
ATOM   1572 C  CA  . TYR A 1 196 ? -22.501 -43.087 21.443  1.00 13.16 ? 196 TYR B CA  1 
ATOM   1573 C  C   . TYR A 1 196 ? -23.793 -43.052 20.651  1.00 13.66 ? 196 TYR B C   1 
ATOM   1574 O  O   . TYR A 1 196 ? -24.515 -42.038 20.655  1.00 14.28 ? 196 TYR B O   1 
ATOM   1575 C  CB  . TYR A 1 196 ? -22.618 -43.911 22.774  1.00 12.09 ? 196 TYR B CB  1 
ATOM   1576 C  CG  . TYR A 1 196 ? -23.835 -43.553 23.595  1.00 10.22 ? 196 TYR B CG  1 
ATOM   1577 C  CD1 . TYR A 1 196 ? -23.841 -42.437 24.490  1.00 12.37 ? 196 TYR B CD1 1 
ATOM   1578 C  CD2 . TYR A 1 196 ? -25.030 -44.279 23.437  1.00 11.55 ? 196 TYR B CD2 1 
ATOM   1579 C  CE1 . TYR A 1 196 ? -24.989 -42.090 25.161  1.00 11.36 ? 196 TYR B CE1 1 
ATOM   1580 C  CE2 . TYR A 1 196 ? -26.168 -43.940 24.076  1.00 9.59  ? 196 TYR B CE2 1 
ATOM   1581 C  CZ  . TYR A 1 196 ? -26.153 -42.873 24.962  1.00 10.26 ? 196 TYR B CZ  1 
ATOM   1582 O  OH  . TYR A 1 196 ? -27.353 -42.609 25.580  1.00 13.27 ? 196 TYR B OH  1 
ATOM   1583 N  N   . PRO A 1 197 ? -24.096 -44.144 19.923  1.00 15.55 ? 197 PRO B N   1 
ATOM   1584 C  CA  . PRO A 1 197 ? -25.369 -44.196 19.205  1.00 14.07 ? 197 PRO B CA  1 
ATOM   1585 C  C   . PRO A 1 197 ? -26.490 -44.684 20.155  1.00 13.79 ? 197 PRO B C   1 
ATOM   1586 O  O   . PRO A 1 197 ? -26.314 -45.678 20.880  1.00 13.18 ? 197 PRO B O   1 
ATOM   1587 C  CB  . PRO A 1 197 ? -25.058 -45.204 18.061  1.00 11.79 ? 197 PRO B CB  1 
ATOM   1588 C  CG  . PRO A 1 197 ? -24.107 -46.238 18.776  1.00 14.68 ? 197 PRO B CG  1 
ATOM   1589 C  CD  . PRO A 1 197 ? -23.232 -45.336 19.638  1.00 15.12 ? 197 PRO B CD  1 
ATOM   1590 N  N   . GLY A 1 198 ? -27.592 -43.933 20.220  1.00 12.34 ? 198 GLY B N   1 
ATOM   1591 C  CA  . GLY A 1 198 ? -28.646 -44.311 21.084  1.00 12.79 ? 198 GLY B CA  1 
ATOM   1592 C  C   . GLY A 1 198 ? -29.996 -43.867 20.568  1.00 12.76 ? 198 GLY B C   1 
ATOM   1593 O  O   . GLY A 1 198 ? -30.275 -43.992 19.394  1.00 13.13 ? 198 GLY B O   1 
ATOM   1594 N  N   . SER A 1 199 ? -30.844 -43.471 21.484  1.00 12.32 ? 199 SER B N   1 
ATOM   1595 C  CA  . SER A 1 199 ? -32.276 -43.314 21.224  1.00 13.09 ? 199 SER B CA  1 
ATOM   1596 C  C   . SER A 1 199 ? -32.845 -42.089 21.874  1.00 11.93 ? 199 SER B C   1 
ATOM   1597 O  O   . SER A 1 199 ? -32.134 -41.463 22.696  1.00 11.27 ? 199 SER B O   1 
ATOM   1598 C  CB  . SER A 1 199 ? -33.073 -44.550 21.710  1.00 12.52 ? 199 SER B CB  1 
ATOM   1599 O  OG  . SER A 1 199 ? -33.149 -44.595 23.079  1.00 11.76 ? 199 SER B OG  1 
ATOM   1600 N  N   . LEU A 1 200 ? -34.137 -41.799 21.545  1.00 10.72 ? 200 LEU B N   1 
ATOM   1601 C  CA  . LEU A 1 200 ? -34.993 -40.947 22.427  1.00 11.74 ? 200 LEU B CA  1 
ATOM   1602 C  C   . LEU A 1 200 ? -35.096 -41.644 23.758  1.00 10.55 ? 200 LEU B C   1 
ATOM   1603 O  O   . LEU A 1 200 ? -35.269 -42.885 23.834  1.00 12.47 ? 200 LEU B O   1 
ATOM   1604 C  CB  . LEU A 1 200 ? -36.410 -40.647 21.915  1.00 10.03 ? 200 LEU B CB  1 
ATOM   1605 C  CG  . LEU A 1 200 ? -36.468 -40.238 20.405  1.00 14.23 ? 200 LEU B CG  1 
ATOM   1606 C  CD1 . LEU A 1 200 ? -37.860 -40.291 19.898  1.00 14.52 ? 200 LEU B CD1 1 
ATOM   1607 C  CD2 . LEU A 1 200 ? -35.912 -38.818 20.280  1.00 15.57 ? 200 LEU B CD2 1 
ATOM   1608 N  N   . THR A 1 201 ? -35.027 -40.837 24.810  1.00 11.28 ? 201 THR B N   1 
ATOM   1609 C  CA  . THR A 1 201 ? -35.215 -41.369 26.172  1.00 11.00 ? 201 THR B CA  1 
ATOM   1610 C  C   . THR A 1 201 ? -36.639 -41.346 26.567  1.00 11.48 ? 201 THR B C   1 
ATOM   1611 O  O   . THR A 1 201 ? -36.986 -41.635 27.726  1.00 11.58 ? 201 THR B O   1 
ATOM   1612 C  CB  . THR A 1 201 ? -34.323 -40.620 27.219  1.00 11.19 ? 201 THR B CB  1 
ATOM   1613 O  OG1 . THR A 1 201 ? -34.829 -39.294 27.474  1.00 11.46 ? 201 THR B OG1 1 
ATOM   1614 C  CG2 . THR A 1 201 ? -32.840 -40.669 26.742  1.00 8.34  ? 201 THR B CG2 1 
ATOM   1615 N  N   . VAL A 1 202 ? -37.487 -40.951 25.621  1.00 11.56 ? 202 VAL B N   1 
ATOM   1616 C  CA  . VAL A 1 202 ? -38.926 -40.889 25.883  1.00 12.59 ? 202 VAL B CA  1 
ATOM   1617 C  C   . VAL A 1 202 ? -39.597 -41.677 24.718  1.00 12.89 ? 202 VAL B C   1 
ATOM   1618 O  O   . VAL A 1 202 ? -39.041 -41.740 23.591  1.00 12.82 ? 202 VAL B O   1 
ATOM   1619 C  CB  . VAL A 1 202 ? -39.550 -39.414 25.994  1.00 13.32 ? 202 VAL B CB  1 
ATOM   1620 C  CG1 . VAL A 1 202 ? -39.037 -38.565 27.241  1.00 14.90 ? 202 VAL B CG1 1 
ATOM   1621 C  CG2 . VAL A 1 202 ? -39.381 -38.607 24.691  1.00 9.19  ? 202 VAL B CG2 1 
ATOM   1622 N  N   . PRO A 1 203 ? -40.752 -42.329 24.986  1.00 12.66 ? 203 PRO B N   1 
ATOM   1623 C  CA  . PRO A 1 203 ? -41.539 -42.941 23.866  1.00 12.22 ? 203 PRO B CA  1 
ATOM   1624 C  C   . PRO A 1 203 ? -41.675 -41.907 22.716  1.00 13.50 ? 203 PRO B C   1 
ATOM   1625 O  O   . PRO A 1 203 ? -41.945 -40.770 23.018  1.00 12.95 ? 203 PRO B O   1 
ATOM   1626 C  CB  . PRO A 1 203 ? -42.902 -43.213 24.519  1.00 10.93 ? 203 PRO B CB  1 
ATOM   1627 C  CG  . PRO A 1 203 ? -42.492 -43.574 26.037  1.00 12.18 ? 203 PRO B CG  1 
ATOM   1628 C  CD  . PRO A 1 203 ? -41.379 -42.510 26.314  1.00 9.94  ? 203 PRO B CD  1 
ATOM   1629 N  N   . PRO A 1 204 ? -41.547 -42.317 21.425  1.00 14.38 ? 204 PRO B N   1 
ATOM   1630 C  CA  . PRO A 1 204 ? -41.386 -43.692 20.958  1.00 14.64 ? 204 PRO B CA  1 
ATOM   1631 C  C   . PRO A 1 204 ? -39.997 -44.330 21.027  1.00 14.54 ? 204 PRO B C   1 
ATOM   1632 O  O   . PRO A 1 204 ? -39.841 -45.453 20.491  1.00 13.91 ? 204 PRO B O   1 
ATOM   1633 C  CB  . PRO A 1 204 ? -41.863 -43.618 19.479  1.00 15.58 ? 204 PRO B CB  1 
ATOM   1634 C  CG  . PRO A 1 204 ? -41.495 -42.199 19.048  1.00 15.29 ? 204 PRO B CG  1 
ATOM   1635 C  CD  . PRO A 1 204 ? -41.613 -41.338 20.291  1.00 16.03 ? 204 PRO B CD  1 
ATOM   1636 N  N   . LEU A 1 205 ? -39.012 -43.723 21.707  1.00 13.10 ? 205 LEU B N   1 
ATOM   1637 C  CA  . LEU A 1 205 ? -37.729 -44.430 22.030  1.00 13.09 ? 205 LEU B CA  1 
ATOM   1638 C  C   . LEU A 1 205 ? -37.004 -44.795 20.747  1.00 12.36 ? 205 LEU B C   1 
ATOM   1639 O  O   . LEU A 1 205 ? -36.286 -45.815 20.653  1.00 10.90 ? 205 LEU B O   1 
ATOM   1640 C  CB  . LEU A 1 205 ? -37.999 -45.688 22.878  1.00 14.05 ? 205 LEU B CB  1 
ATOM   1641 C  CG  . LEU A 1 205 ? -38.624 -45.397 24.285  1.00 15.73 ? 205 LEU B CG  1 
ATOM   1642 C  CD1 . LEU A 1 205 ? -39.137 -46.688 25.023  1.00 12.79 ? 205 LEU B CD1 1 
ATOM   1643 C  CD2 . LEU A 1 205 ? -37.790 -44.559 25.210  1.00 16.98 ? 205 LEU B CD2 1 
ATOM   1644 N  N   . LEU A 1 206 ? -37.207 -43.974 19.712  1.00 12.12 ? 206 LEU B N   1 
ATOM   1645 C  CA  . LEU A 1 206 ? -36.571 -44.298 18.404  1.00 12.34 ? 206 LEU B CA  1 
ATOM   1646 C  C   . LEU A 1 206 ? -35.061 -44.263 18.458  1.00 11.48 ? 206 LEU B C   1 
ATOM   1647 O  O   . LEU A 1 206 ? -34.474 -43.321 19.016  1.00 11.21 ? 206 LEU B O   1 
ATOM   1648 C  CB  . LEU A 1 206 ? -37.042 -43.326 17.297  1.00 12.39 ? 206 LEU B CB  1 
ATOM   1649 C  CG  . LEU A 1 206 ? -38.567 -43.298 17.129  1.00 12.48 ? 206 LEU B CG  1 
ATOM   1650 C  CD1 . LEU A 1 206 ? -38.946 -42.101 16.278  1.00 15.00 ? 206 LEU B CD1 1 
ATOM   1651 C  CD2 . LEU A 1 206 ? -38.998 -44.607 16.471  1.00 16.41 ? 206 LEU B CD2 1 
ATOM   1652 N  N   . GLU A 1 207 ? -34.429 -45.224 17.786  1.00 11.19 ? 207 GLU B N   1 
ATOM   1653 C  CA  . GLU A 1 207 ? -32.990 -45.343 17.791  1.00 10.53 ? 207 GLU B CA  1 
ATOM   1654 C  C   . GLU A 1 207 ? -32.376 -44.543 16.655  1.00 12.55 ? 207 GLU B C   1 
ATOM   1655 O  O   . GLU A 1 207 ? -31.841 -45.081 15.663  1.00 13.59 ? 207 GLU B O   1 
ATOM   1656 C  CB  . GLU A 1 207 ? -32.630 -46.828 17.782  1.00 12.00 ? 207 GLU B CB  1 
ATOM   1657 C  CG  . GLU A 1 207 ? -33.110 -47.482 19.117  1.00 10.46 ? 207 GLU B CG  1 
ATOM   1658 C  CD  . GLU A 1 207 ? -32.766 -48.950 19.212  1.00 10.80 ? 207 GLU B CD  1 
ATOM   1659 O  OE1 . GLU A 1 207 ? -32.602 -49.588 18.169  1.00 15.91 ? 207 GLU B OE1 1 
ATOM   1660 O  OE2 . GLU A 1 207 ? -32.722 -49.480 20.346  1.00 13.75 ? 207 GLU B OE2 1 
ATOM   1661 N  N   . SER A 1 208 ? -32.420 -43.238 16.841  1.00 13.85 ? 208 SER B N   1 
ATOM   1662 C  CA  . SER A 1 208 ? -32.151 -42.273 15.785  1.00 14.41 ? 208 SER B CA  1 
ATOM   1663 C  C   . SER A 1 208 ? -31.173 -41.178 16.288  1.00 14.36 ? 208 SER B C   1 
ATOM   1664 O  O   . SER A 1 208 ? -30.934 -40.168 15.585  1.00 15.50 ? 208 SER B O   1 
ATOM   1665 C  CB  . SER A 1 208 ? -33.487 -41.608 15.422  1.00 15.31 ? 208 SER B CB  1 
ATOM   1666 O  OG  . SER A 1 208 ? -34.025 -40.875 16.496  1.00 17.97 ? 208 SER B OG  1 
ATOM   1667 N  N   . VAL A 1 209 ? -30.652 -41.358 17.505  1.00 12.80 ? 209 VAL B N   1 
ATOM   1668 C  CA  . VAL A 1 209 ? -29.912 -40.245 18.221  1.00 11.46 ? 209 VAL B CA  1 
ATOM   1669 C  C   . VAL A 1 209 ? -28.405 -40.528 18.317  1.00 11.27 ? 209 VAL B C   1 
ATOM   1670 O  O   . VAL A 1 209 ? -27.985 -41.568 18.834  1.00 10.98 ? 209 VAL B O   1 
ATOM   1671 C  CB  . VAL A 1 209 ? -30.504 -39.947 19.685  1.00 10.62 ? 209 VAL B CB  1 
ATOM   1672 C  CG1 . VAL A 1 209 ? -29.649 -38.773 20.423  1.00 7.90  ? 209 VAL B CG1 1 
ATOM   1673 C  CG2 . VAL A 1 209 ? -32.043 -39.679 19.659  1.00 12.22 ? 209 VAL B CG2 1 
ATOM   1674 N  N   . THR A 1 210 ? -27.608 -39.616 17.780  1.00 11.89 ? 210 THR B N   1 
ATOM   1675 C  CA  . THR A 1 210 ? -26.189 -39.466 18.147  1.00 12.25 ? 210 THR B CA  1 
ATOM   1676 C  C   . THR A 1 210 ? -26.125 -38.633 19.439  1.00 12.32 ? 210 THR B C   1 
ATOM   1677 O  O   . THR A 1 210 ? -26.384 -37.438 19.445  1.00 11.74 ? 210 THR B O   1 
ATOM   1678 C  CB  . THR A 1 210 ? -25.290 -38.826 16.995  1.00 11.41 ? 210 THR B CB  1 
ATOM   1679 O  OG1 . THR A 1 210 ? -25.425 -39.645 15.797  1.00 12.22 ? 210 THR B OG1 1 
ATOM   1680 C  CG2 . THR A 1 210 ? -23.881 -38.716 17.425  1.00 10.38 ? 210 THR B CG2 1 
ATOM   1681 N  N   . TRP A 1 211 ? -25.801 -39.324 20.534  1.00 12.15 ? 211 TRP B N   1 
ATOM   1682 C  CA  . TRP A 1 211 ? -25.686 -38.676 21.868  1.00 12.56 ? 211 TRP B CA  1 
ATOM   1683 C  C   . TRP A 1 211 ? -24.331 -38.029 22.036  1.00 11.13 ? 211 TRP B C   1 
ATOM   1684 O  O   . TRP A 1 211 ? -23.317 -38.618 21.660  1.00 11.81 ? 211 TRP B O   1 
ATOM   1685 C  CB  . TRP A 1 211 ? -25.960 -39.695 22.963  1.00 11.21 ? 211 TRP B CB  1 
ATOM   1686 C  CG  . TRP A 1 211 ? -27.366 -39.813 23.172  1.00 12.05 ? 211 TRP B CG  1 
ATOM   1687 C  CD1 . TRP A 1 211 ? -28.172 -40.785 22.688  1.00 10.47 ? 211 TRP B CD1 1 
ATOM   1688 C  CD2 . TRP A 1 211 ? -28.198 -38.921 23.930  1.00 14.44 ? 211 TRP B CD2 1 
ATOM   1689 N  NE1 . TRP A 1 211 ? -29.491 -40.544 23.040  1.00 10.27 ? 211 TRP B NE1 1 
ATOM   1690 C  CE2 . TRP A 1 211 ? -29.529 -39.405 23.818  1.00 10.31 ? 211 TRP B CE2 1 
ATOM   1691 C  CE3 . TRP A 1 211 ? -27.956 -37.738 24.678  1.00 11.04 ? 211 TRP B CE3 1 
ATOM   1692 C  CZ2 . TRP A 1 211 ? -30.613 -38.758 24.421  1.00 12.02 ? 211 TRP B CZ2 1 
ATOM   1693 C  CZ3 . TRP A 1 211 ? -29.060 -37.093 25.296  1.00 10.46 ? 211 TRP B CZ3 1 
ATOM   1694 C  CH2 . TRP A 1 211 ? -30.364 -37.608 25.151  1.00 11.82 ? 211 TRP B CH2 1 
ATOM   1695 N  N   . ILE A 1 212 ? -24.326 -36.814 22.545  1.00 10.07 ? 212 ILE B N   1 
ATOM   1696 C  CA  . ILE A 1 212 ? -23.139 -36.065 22.828  1.00 11.95 ? 212 ILE B CA  1 
ATOM   1697 C  C   . ILE A 1 212 ? -23.347 -35.532 24.255  1.00 11.36 ? 212 ILE B C   1 
ATOM   1698 O  O   . ILE A 1 212 ? -24.064 -34.559 24.479  1.00 11.03 ? 212 ILE B O   1 
ATOM   1699 C  CB  . ILE A 1 212 ? -22.956 -34.873 21.802  1.00 12.69 ? 212 ILE B CB  1 
ATOM   1700 C  CG1 . ILE A 1 212 ? -22.672 -35.386 20.374  1.00 13.04 ? 212 ILE B CG1 1 
ATOM   1701 C  CG2 . ILE A 1 212 ? -21.802 -33.928 22.207  1.00 12.97 ? 212 ILE B CG2 1 
ATOM   1702 C  CD1 . ILE A 1 212 ? -22.930 -34.366 19.290  1.00 11.66 ? 212 ILE B CD1 1 
ATOM   1703 N  N   . VAL A 1 213 ? -22.730 -36.224 25.217  1.00 12.05 ? 213 VAL B N   1 
ATOM   1704 C  CA  . VAL A 1 213 ? -22.935 -35.987 26.650  1.00 10.15 ? 213 VAL B CA  1 
ATOM   1705 C  C   . VAL A 1 213 ? -21.706 -35.279 27.188  1.00 12.88 ? 213 VAL B C   1 
ATOM   1706 O  O   . VAL A 1 213 ? -20.613 -35.881 27.179  1.00 11.38 ? 213 VAL B O   1 
ATOM   1707 C  CB  . VAL A 1 213 ? -23.150 -37.325 27.399  1.00 11.99 ? 213 VAL B CB  1 
ATOM   1708 C  CG1 . VAL A 1 213 ? -23.440 -37.080 28.911  1.00 12.18 ? 213 VAL B CG1 1 
ATOM   1709 C  CG2 . VAL A 1 213 ? -24.347 -38.083 26.734  1.00 11.05 ? 213 VAL B CG2 1 
ATOM   1710 N  N   . LEU A 1 214 ? -21.885 -34.012 27.650  1.00 12.62 ? 214 LEU B N   1 
ATOM   1711 C  CA  . LEU A 1 214 ? -20.739 -33.187 28.064  1.00 13.85 ? 214 LEU B CA  1 
ATOM   1712 C  C   . LEU A 1 214 ? -20.270 -33.694 29.441  1.00 13.25 ? 214 LEU B C   1 
ATOM   1713 O  O   . LEU A 1 214 ? -21.085 -33.951 30.256  1.00 11.34 ? 214 LEU B O   1 
ATOM   1714 C  CB  . LEU A 1 214 ? -21.134 -31.725 28.222  1.00 12.74 ? 214 LEU B CB  1 
ATOM   1715 C  CG  . LEU A 1 214 ? -21.558 -30.967 26.950  1.00 17.57 ? 214 LEU B CG  1 
ATOM   1716 C  CD1 . LEU A 1 214 ? -21.186 -29.480 26.955  1.00 8.08  ? 214 LEU B CD1 1 
ATOM   1717 C  CD2 . LEU A 1 214 ? -21.132 -31.622 25.720  1.00 16.23 ? 214 LEU B CD2 1 
ATOM   1718 N  N   . LYS A 1 215 ? -18.969 -33.771 29.666  1.00 12.90 ? 215 LYS B N   1 
ATOM   1719 C  CA  . LYS A 1 215 ? -18.418 -34.245 30.904  1.00 14.58 ? 215 LYS B CA  1 
ATOM   1720 C  C   . LYS A 1 215 ? -18.659 -33.222 32.011  1.00 15.34 ? 215 LYS B C   1 
ATOM   1721 O  O   . LYS A 1 215 ? -18.972 -33.597 33.141  1.00 15.71 ? 215 LYS B O   1 
ATOM   1722 C  CB  . LYS A 1 215 ? -16.913 -34.483 30.677  1.00 15.94 ? 215 LYS B CB  1 
ATOM   1723 C  CG  . LYS A 1 215 ? -16.129 -34.716 31.999  1.00 18.92 ? 215 LYS B CG  1 
ATOM   1724 C  CD  . LYS A 1 215 ? -14.740 -35.275 31.683  1.00 22.52 ? 215 LYS B CD  1 
ATOM   1725 C  CE  . LYS A 1 215 ? -13.862 -35.263 32.962  1.00 26.49 ? 215 LYS B CE  1 
ATOM   1726 N  NZ  . LYS A 1 215 ? -12.652 -36.145 32.665  1.00 32.93 ? 215 LYS B NZ  1 
ATOM   1727 N  N   . GLN A 1 216 ? -18.556 -31.922 31.696  1.00 13.82 ? 216 GLN B N   1 
ATOM   1728 C  CA  . GLN A 1 216 ? -18.561 -30.899 32.803  1.00 14.41 ? 216 GLN B CA  1 
ATOM   1729 C  C   . GLN A 1 216 ? -19.987 -30.469 33.163  1.00 13.77 ? 216 GLN B C   1 
ATOM   1730 O  O   . GLN A 1 216 ? -20.708 -29.984 32.312  1.00 12.76 ? 216 GLN B O   1 
ATOM   1731 C  CB  . GLN A 1 216 ? -17.729 -29.636 32.447  1.00 14.57 ? 216 GLN B CB  1 
ATOM   1732 C  CG  . GLN A 1 216 ? -17.719 -28.608 33.604  1.00 14.02 ? 216 GLN B CG  1 
ATOM   1733 C  CD  . GLN A 1 216 ? -16.827 -27.396 33.391  1.00 16.66 ? 216 GLN B CD  1 
ATOM   1734 O  OE1 . GLN A 1 216 ? -16.348 -27.152 32.304  1.00 16.77 ? 216 GLN B OE1 1 
ATOM   1735 N  NE2 . GLN A 1 216 ? -16.629 -26.629 34.457  1.00 15.49 ? 216 GLN B NE2 1 
ATOM   1736 N  N   . PRO A 1 217 ? -20.402 -30.644 34.417  1.00 15.88 ? 217 PRO B N   1 
ATOM   1737 C  CA  . PRO A 1 217 ? -21.749 -30.195 34.802  1.00 14.53 ? 217 PRO B CA  1 
ATOM   1738 C  C   . PRO A 1 217 ? -21.884 -28.665 34.974  1.00 15.64 ? 217 PRO B C   1 
ATOM   1739 O  O   . PRO A 1 217 ? -20.855 -27.941 35.131  1.00 13.94 ? 217 PRO B O   1 
ATOM   1740 C  CB  . PRO A 1 217 ? -22.047 -30.992 36.105  1.00 15.48 ? 217 PRO B CB  1 
ATOM   1741 C  CG  . PRO A 1 217 ? -20.770 -31.422 36.595  1.00 17.38 ? 217 PRO B CG  1 
ATOM   1742 C  CD  . PRO A 1 217 ? -19.674 -31.243 35.552  1.00 16.90 ? 217 PRO B CD  1 
ATOM   1743 N  N   . ILE A 1 218 ? -23.112 -28.140 34.888  1.00 12.83 ? 218 ILE B N   1 
ATOM   1744 C  CA  . ILE A 1 218 ? -23.313 -26.757 35.255  1.00 14.64 ? 218 ILE B CA  1 
ATOM   1745 C  C   . ILE A 1 218 ? -24.023 -26.830 36.613  1.00 14.75 ? 218 ILE B C   1 
ATOM   1746 O  O   . ILE A 1 218 ? -24.351 -27.909 37.044  1.00 15.63 ? 218 ILE B O   1 
ATOM   1747 C  CB  . ILE A 1 218 ? -24.200 -25.992 34.205  1.00 13.42 ? 218 ILE B CB  1 
ATOM   1748 C  CG1 . ILE A 1 218 ? -25.585 -26.670 34.088  1.00 15.39 ? 218 ILE B CG1 1 
ATOM   1749 C  CG2 . ILE A 1 218 ? -23.455 -25.969 32.884  1.00 11.91 ? 218 ILE B CG2 1 
ATOM   1750 C  CD1 . ILE A 1 218 ? -26.634 -25.833 33.200  1.00 15.31 ? 218 ILE B CD1 1 
ATOM   1751 N  N   . ASN A 1 219 ? -24.274 -25.693 37.254  1.00 14.58 ? 219 ASN B N   1 
ATOM   1752 C  CA  . ASN A 1 219 ? -24.859 -25.696 38.586  1.00 16.28 ? 219 ASN B CA  1 
ATOM   1753 C  C   . ASN A 1 219 ? -26.335 -25.362 38.522  1.00 15.29 ? 219 ASN B C   1 
ATOM   1754 O  O   . ASN A 1 219 ? -26.791 -24.706 37.613  1.00 16.75 ? 219 ASN B O   1 
ATOM   1755 C  CB  . ASN A 1 219 ? -24.201 -24.693 39.542  1.00 17.66 ? 219 ASN B CB  1 
ATOM   1756 C  CG  . ASN A 1 219 ? -22.794 -25.125 40.039  1.00 22.96 ? 219 ASN B CG  1 
ATOM   1757 O  OD1 . ASN A 1 219 ? -22.434 -26.303 40.062  1.00 23.08 ? 219 ASN B OD1 1 
ATOM   1758 N  ND2 . ASN A 1 219 ? -22.008 -24.125 40.509  1.00 29.25 ? 219 ASN B ND2 1 
ATOM   1759 N  N   . ILE A 1 220 ? -27.073 -25.829 39.513  1.00 14.11 ? 220 ILE B N   1 
ATOM   1760 C  CA  . ILE A 1 220 ? -28.454 -25.410 39.726  1.00 13.58 ? 220 ILE B CA  1 
ATOM   1761 C  C   . ILE A 1 220 ? -28.580 -25.448 41.266  1.00 15.28 ? 220 ILE B C   1 
ATOM   1762 O  O   . ILE A 1 220 ? -28.045 -26.351 41.940  1.00 14.04 ? 220 ILE B O   1 
ATOM   1763 C  CB  . ILE A 1 220 ? -29.494 -26.337 39.032  1.00 12.39 ? 220 ILE B CB  1 
ATOM   1764 C  CG1 . ILE A 1 220 ? -30.923 -25.725 39.148  1.00 14.02 ? 220 ILE B CG1 1 
ATOM   1765 C  CG2 . ILE A 1 220 ? -29.429 -27.818 39.572  1.00 13.42 ? 220 ILE B CG2 1 
ATOM   1766 C  CD1 . ILE A 1 220 ? -32.097 -26.462 38.213  1.00 9.27  ? 220 ILE B CD1 1 
ATOM   1767 N  N   . SER A 1 221 ? -29.291 -24.485 41.829  1.00 15.39 ? 221 SER B N   1 
ATOM   1768 C  CA  . SER A 1 221 ? -29.574 -24.584 43.262  1.00 15.16 ? 221 SER B CA  1 
ATOM   1769 C  C   . SER A 1 221 ? -30.730 -25.481 43.543  1.00 16.58 ? 221 SER B C   1 
ATOM   1770 O  O   . SER A 1 221 ? -31.573 -25.787 42.661  1.00 16.41 ? 221 SER B O   1 
ATOM   1771 C  CB  . SER A 1 221 ? -29.820 -23.157 43.834  1.00 14.96 ? 221 SER B CB  1 
ATOM   1772 O  OG  . SER A 1 221 ? -31.145 -22.717 43.548  1.00 16.17 ? 221 SER B OG  1 
ATOM   1773 N  N   . SER A 1 222 ? -30.768 -25.979 44.777  1.00 15.78 ? 222 SER B N   1 
ATOM   1774 C  CA  . SER A 1 222 ? -31.891 -26.755 45.184  1.00 15.65 ? 222 SER B CA  1 
ATOM   1775 C  C   . SER A 1 222 ? -33.229 -25.995 45.052  1.00 15.08 ? 222 SER B C   1 
ATOM   1776 O  O   . SER A 1 222 ? -34.237 -26.563 44.620  1.00 13.81 ? 222 SER B O   1 
ATOM   1777 C  CB  . SER A 1 222 ? -31.629 -27.409 46.569  1.00 15.87 ? 222 SER B CB  1 
ATOM   1778 O  OG  . SER A 1 222 ? -32.894 -27.839 46.994  1.00 21.17 ? 222 SER B OG  1 
ATOM   1779 N  N   . GLN A 1 223 ? -33.219 -24.695 45.346  1.00 14.02 ? 223 GLN B N   1 
ATOM   1780 C  CA  . GLN A 1 223 ? -34.402 -23.822 45.184  1.00 15.81 ? 223 GLN B CA  1 
ATOM   1781 C  C   . GLN A 1 223 ? -34.868 -23.686 43.755  1.00 15.85 ? 223 GLN B C   1 
ATOM   1782 O  O   . GLN A 1 223 ? -36.073 -23.699 43.476  1.00 16.46 ? 223 GLN B O   1 
ATOM   1783 C  CB  . GLN A 1 223 ? -34.163 -22.432 45.772  1.00 13.97 ? 223 GLN B CB  1 
ATOM   1784 C  CG  . GLN A 1 223 ? -34.445 -22.376 47.316  1.00 18.17 ? 223 GLN B CG  1 
ATOM   1785 C  CD  . GLN A 1 223 ? -34.475 -20.958 47.867  1.00 19.24 ? 223 GLN B CD  1 
ATOM   1786 O  OE1 . GLN A 1 223 ? -35.280 -20.119 47.438  1.00 25.70 ? 223 GLN B OE1 1 
ATOM   1787 N  NE2 . GLN A 1 223 ? -33.553 -20.660 48.774  1.00 23.02 ? 223 GLN B NE2 1 
ATOM   1788 N  N   . GLN A 1 224 ? -33.912 -23.581 42.845  1.00 14.16 ? 224 GLN B N   1 
ATOM   1789 C  CA  . GLN A 1 224 ? -34.249 -23.441 41.430  1.00 15.27 ? 224 GLN B CA  1 
ATOM   1790 C  C   . GLN A 1 224 ? -34.915 -24.755 40.967  1.00 14.75 ? 224 GLN B C   1 
ATOM   1791 O  O   . GLN A 1 224 ? -35.954 -24.753 40.291  1.00 14.85 ? 224 GLN B O   1 
ATOM   1792 C  CB  . GLN A 1 224 ? -32.946 -23.155 40.644  1.00 14.20 ? 224 GLN B CB  1 
ATOM   1793 C  CG  . GLN A 1 224 ? -32.516 -21.700 40.725  1.00 13.98 ? 224 GLN B CG  1 
ATOM   1794 C  CD  . GLN A 1 224 ? -31.297 -21.475 39.875  1.00 13.03 ? 224 GLN B CD  1 
ATOM   1795 O  OE1 . GLN A 1 224 ? -30.285 -22.168 40.041  1.00 13.93 ? 224 GLN B OE1 1 
ATOM   1796 N  NE2 . GLN A 1 224 ? -31.386 -20.535 38.933  1.00 13.51 ? 224 GLN B NE2 1 
ATOM   1797 N  N   . LEU A 1 225 ? -34.277 -25.871 41.307  1.00 14.25 ? 225 LEU B N   1 
ATOM   1798 C  CA  . LEU A 1 225 ? -34.681 -27.183 40.786  1.00 14.56 ? 225 LEU B CA  1 
ATOM   1799 C  C   . LEU A 1 225 ? -36.085 -27.570 41.264  1.00 14.25 ? 225 LEU B C   1 
ATOM   1800 O  O   . LEU A 1 225 ? -36.852 -28.174 40.552  1.00 14.36 ? 225 LEU B O   1 
ATOM   1801 C  CB  . LEU A 1 225 ? -33.583 -28.238 41.145  1.00 14.62 ? 225 LEU B CB  1 
ATOM   1802 C  CG  . LEU A 1 225 ? -33.797 -29.706 40.673  1.00 15.42 ? 225 LEU B CG  1 
ATOM   1803 C  CD1 . LEU A 1 225 ? -34.131 -29.755 39.187  1.00 14.28 ? 225 LEU B CD1 1 
ATOM   1804 C  CD2 . LEU A 1 225 ? -32.658 -30.669 40.892  1.00 11.59 ? 225 LEU B CD2 1 
ATOM   1805 N  N   . ALA A 1 226 ? -36.398 -27.289 42.532  1.00 14.54 ? 226 ALA B N   1 
ATOM   1806 C  CA  . ALA A 1 226 ? -37.704 -27.534 43.111  1.00 15.41 ? 226 ALA B CA  1 
ATOM   1807 C  C   . ALA A 1 226 ? -38.854 -26.920 42.309  1.00 14.92 ? 226 ALA B C   1 
ATOM   1808 O  O   . ALA A 1 226 ? -39.977 -27.469 42.295  1.00 16.56 ? 226 ALA B O   1 
ATOM   1809 C  CB  . ALA A 1 226 ? -37.772 -27.034 44.599  1.00 15.68 ? 226 ALA B CB  1 
ATOM   1810 N  N   . LYS A 1 227 ? -38.614 -25.788 41.693  1.00 15.46 ? 227 LYS B N   1 
ATOM   1811 C  CA  . LYS A 1 227 ? -39.603 -25.139 40.822  1.00 17.13 ? 227 LYS B CA  1 
ATOM   1812 C  C   . LYS A 1 227 ? -40.052 -25.981 39.640  1.00 15.37 ? 227 LYS B C   1 
ATOM   1813 O  O   . LYS A 1 227 ? -41.216 -25.930 39.263  1.00 14.36 ? 227 LYS B O   1 
ATOM   1814 C  CB  . LYS A 1 227 ? -39.078 -23.788 40.321  1.00 16.00 ? 227 LYS B CB  1 
ATOM   1815 C  CG  . LYS A 1 227 ? -38.587 -22.826 41.408  1.00 22.02 ? 227 LYS B CG  1 
ATOM   1816 C  CD  . LYS A 1 227 ? -38.240 -21.448 40.739  1.00 22.87 ? 227 LYS B CD  1 
ATOM   1817 C  CE  . LYS A 1 227 ? -38.893 -20.200 41.486  1.00 31.83 ? 227 LYS B CE  1 
ATOM   1818 N  NZ  . LYS A 1 227 ? -38.362 -18.781 41.018  1.00 28.18 ? 227 LYS B NZ  1 
ATOM   1819 N  N   . PHE A 1 228 ? -39.152 -26.762 39.046  1.00 14.28 ? 228 PHE B N   1 
ATOM   1820 C  CA  . PHE A 1 228 ? -39.583 -27.656 37.927  1.00 16.27 ? 228 PHE B CA  1 
ATOM   1821 C  C   . PHE A 1 228 ? -40.518 -28.768 38.377  1.00 16.97 ? 228 PHE B C   1 
ATOM   1822 O  O   . PHE A 1 228 ? -41.415 -29.164 37.636  1.00 14.30 ? 228 PHE B O   1 
ATOM   1823 C  CB  . PHE A 1 228 ? -38.387 -28.274 37.210  1.00 14.91 ? 228 PHE B CB  1 
ATOM   1824 C  CG  . PHE A 1 228 ? -37.515 -27.231 36.588  1.00 16.51 ? 228 PHE B CG  1 
ATOM   1825 C  CD1 . PHE A 1 228 ? -36.422 -26.687 37.295  1.00 13.63 ? 228 PHE B CD1 1 
ATOM   1826 C  CD2 . PHE A 1 228 ? -37.834 -26.712 35.317  1.00 14.70 ? 228 PHE B CD2 1 
ATOM   1827 C  CE1 . PHE A 1 228 ? -35.624 -25.680 36.681  1.00 12.77 ? 228 PHE B CE1 1 
ATOM   1828 C  CE2 . PHE A 1 228 ? -37.073 -25.690 34.719  1.00 15.27 ? 228 PHE B CE2 1 
ATOM   1829 C  CZ  . PHE A 1 228 ? -35.961 -25.169 35.369  1.00 12.19 ? 228 PHE B CZ  1 
ATOM   1830 N  N   . ARG A 1 229 ? -40.354 -29.191 39.639  1.00 16.78 ? 229 ARG B N   1 
ATOM   1831 C  CA  . ARG A 1 229 ? -41.250 -30.194 40.219  1.00 16.79 ? 229 ARG B CA  1 
ATOM   1832 C  C   . ARG A 1 229 ? -42.680 -29.716 40.466  1.00 17.32 ? 229 ARG B C   1 
ATOM   1833 O  O   . ARG A 1 229 ? -43.545 -30.554 40.676  1.00 15.88 ? 229 ARG B O   1 
ATOM   1834 C  CB  . ARG A 1 229 ? -40.679 -30.776 41.519  1.00 16.60 ? 229 ARG B CB  1 
ATOM   1835 C  CG  . ARG A 1 229 ? -39.226 -31.223 41.399  1.00 16.85 ? 229 ARG B CG  1 
ATOM   1836 C  CD  . ARG A 1 229 ? -38.846 -32.195 42.570  1.00 14.05 ? 229 ARG B CD  1 
ATOM   1837 N  NE  . ARG A 1 229 ? -37.420 -32.485 42.479  1.00 15.87 ? 229 ARG B NE  1 
ATOM   1838 C  CZ  . ARG A 1 229 ? -36.452 -31.849 43.125  1.00 16.39 ? 229 ARG B CZ  1 
ATOM   1839 N  NH1 . ARG A 1 229 ? -36.738 -30.878 44.009  1.00 13.38 ? 229 ARG B NH1 1 
ATOM   1840 N  NH2 . ARG A 1 229 ? -35.194 -32.207 42.896  1.00 15.07 ? 229 ARG B NH2 1 
ATOM   1841 N  N   . SER A 1 230 ? -42.950 -28.413 40.410  1.00 16.15 ? 230 SER B N   1 
ATOM   1842 C  CA  . SER A 1 230 ? -44.348 -28.011 40.544  1.00 18.91 ? 230 SER B CA  1 
ATOM   1843 C  C   . SER A 1 230 ? -45.057 -27.788 39.186  1.00 18.08 ? 230 SER B C   1 
ATOM   1844 O  O   . SER A 1 230 ? -46.281 -27.429 39.135  1.00 16.21 ? 230 SER B O   1 
ATOM   1845 C  CB  . SER A 1 230 ? -44.530 -26.849 41.543  1.00 20.04 ? 230 SER B CB  1 
ATOM   1846 O  OG  . SER A 1 230 ? -43.834 -25.736 41.032  1.00 28.20 ? 230 SER B OG  1 
ATOM   1847 N  N   . LEU A 1 231 ? -44.323 -28.083 38.100  1.00 15.11 ? 231 LEU B N   1 
ATOM   1848 C  CA  . LEU A 1 231 ? -45.044 -28.404 36.858  1.00 16.13 ? 231 LEU B CA  1 
ATOM   1849 C  C   . LEU A 1 231 ? -46.035 -29.570 36.985  1.00 15.88 ? 231 LEU B C   1 
ATOM   1850 O  O   . LEU A 1 231 ? -45.752 -30.605 37.633  1.00 14.99 ? 231 LEU B O   1 
ATOM   1851 C  CB  . LEU A 1 231 ? -44.042 -28.653 35.691  1.00 16.14 ? 231 LEU B CB  1 
ATOM   1852 C  CG  . LEU A 1 231 ? -43.243 -27.424 35.288  1.00 15.10 ? 231 LEU B CG  1 
ATOM   1853 C  CD1 . LEU A 1 231 ? -42.207 -27.941 34.259  1.00 15.26 ? 231 LEU B CD1 1 
ATOM   1854 C  CD2 . LEU A 1 231 ? -44.075 -26.276 34.718  1.00 16.21 ? 231 LEU B CD2 1 
ATOM   1855 N  N   . LEU A 1 232 ? -47.198 -29.433 36.329  1.00 17.15 ? 232 LEU B N   1 
ATOM   1856 C  CA  . LEU A 1 232 ? -48.104 -30.545 36.246  1.00 18.77 ? 232 LEU B CA  1 
ATOM   1857 C  C   . LEU A 1 232 ? -47.859 -31.413 35.000  1.00 19.50 ? 232 LEU B C   1 
ATOM   1858 O  O   . LEU A 1 232 ? -47.465 -30.909 33.958  1.00 19.70 ? 232 LEU B O   1 
ATOM   1859 C  CB  . LEU A 1 232 ? -49.589 -30.092 36.290  1.00 17.81 ? 232 LEU B CB  1 
ATOM   1860 C  CG  . LEU A 1 232 ? -49.993 -29.211 37.458  1.00 20.83 ? 232 LEU B CG  1 
ATOM   1861 C  CD1 . LEU A 1 232 ? -51.492 -28.860 37.324  1.00 21.52 ? 232 LEU B CD1 1 
ATOM   1862 C  CD2 . LEU A 1 232 ? -49.685 -29.942 38.835  1.00 17.26 ? 232 LEU B CD2 1 
ATOM   1863 N  N   . CYS A 1 233 ? -48.074 -32.709 35.143  1.00 18.70 ? 233 CYS B N   1 
ATOM   1864 C  CA  . CYS A 1 233 ? -48.146 -33.591 33.979  1.00 19.68 ? 233 CYS B CA  1 
ATOM   1865 C  C   . CYS A 1 233 ? -49.602 -33.735 33.450  1.00 19.76 ? 233 CYS B C   1 
ATOM   1866 O  O   . CYS A 1 233 ? -49.883 -34.585 32.614  1.00 18.92 ? 233 CYS B O   1 
ATOM   1867 C  CB  . CYS A 1 233 ? -47.586 -34.974 34.317  1.00 20.33 ? 233 CYS B CB  1 
ATOM   1868 S  SG  . CYS A 1 233 ? -48.474 -35.915 35.639  1.00 22.10 ? 233 CYS B SG  1 
ATOM   1869 N  N   . THR A 1 234 ? -50.482 -32.880 33.941  1.00 20.26 ? 234 THR B N   1 
ATOM   1870 C  CA  . THR A 1 234 ? -51.915 -32.956 33.685  1.00 22.12 ? 234 THR B CA  1 
ATOM   1871 C  C   . THR A 1 234 ? -52.442 -31.629 33.154  1.00 23.58 ? 234 THR B C   1 
ATOM   1872 O  O   . THR A 1 234 ? -51.939 -30.548 33.460  1.00 22.53 ? 234 THR B O   1 
ATOM   1873 C  CB  . THR A 1 234 ? -52.696 -33.355 34.969  1.00 22.86 ? 234 THR B CB  1 
ATOM   1874 O  OG1 . THR A 1 234 ? -52.232 -32.534 36.040  1.00 17.52 ? 234 THR B OG1 1 
ATOM   1875 C  CG2 . THR A 1 234 ? -52.451 -34.830 35.369  1.00 22.05 ? 234 THR B CG2 1 
ATOM   1876 N  N   . ALA A 1 235 ? -53.469 -31.718 32.328  1.00 25.29 ? 235 ALA B N   1 
ATOM   1877 C  CA  . ALA A 1 235 ? -53.940 -30.543 31.622  1.00 27.55 ? 235 ALA B CA  1 
ATOM   1878 C  C   . ALA A 1 235 ? -55.007 -29.850 32.490  1.00 29.23 ? 235 ALA B C   1 
ATOM   1879 O  O   . ALA A 1 235 ? -55.493 -30.416 33.470  1.00 29.26 ? 235 ALA B O   1 
ATOM   1880 C  CB  . ALA A 1 235 ? -54.475 -30.938 30.196  1.00 26.59 ? 235 ALA B CB  1 
ATOM   1881 N  N   . GLU A 1 236 ? -55.307 -28.609 32.157  1.00 31.80 ? 236 GLU B N   1 
ATOM   1882 C  CA  . GLU A 1 236 ? -56.329 -27.841 32.848  1.00 36.06 ? 236 GLU B CA  1 
ATOM   1883 C  C   . GLU A 1 236 ? -57.637 -28.641 32.747  1.00 36.04 ? 236 GLU B C   1 
ATOM   1884 O  O   . GLU A 1 236 ? -57.986 -29.106 31.660  1.00 36.82 ? 236 GLU B O   1 
ATOM   1885 C  CB  . GLU A 1 236 ? -56.472 -26.488 32.144  1.00 35.95 ? 236 GLU B CB  1 
ATOM   1886 C  CG  . GLU A 1 236 ? -57.431 -25.521 32.778  1.00 36.97 ? 236 GLU B CG  1 
ATOM   1887 C  CD  . GLU A 1 236 ? -57.756 -24.324 31.852  1.00 38.95 ? 236 GLU B CD  1 
ATOM   1888 O  OE1 . GLU A 1 236 ? -57.087 -24.152 30.788  1.00 42.10 ? 236 GLU B OE1 1 
ATOM   1889 O  OE2 . GLU A 1 236 ? -58.680 -23.555 32.193  0.01 39.10 ? 236 GLU B OE2 1 
ATOM   1890 N  N   . GLY A 1 237 ? -58.309 -28.844 33.881  1.00 37.64 ? 237 GLY B N   1 
ATOM   1891 C  CA  . GLY A 1 237 ? -59.534 -29.678 33.934  1.00 37.50 ? 237 GLY B CA  1 
ATOM   1892 C  C   . GLY A 1 237 ? -59.330 -31.186 34.135  1.00 38.21 ? 237 GLY B C   1 
ATOM   1893 O  O   . GLY A 1 237 ? -60.308 -31.976 34.096  1.00 38.41 ? 237 GLY B O   1 
ATOM   1894 N  N   . GLU A 1 238 ? -58.081 -31.619 34.358  1.00 37.77 ? 238 GLU B N   1 
ATOM   1895 C  CA  . GLU A 1 238 ? -57.798 -33.049 34.616  1.00 37.40 ? 238 GLU B CA  1 
ATOM   1896 C  C   . GLU A 1 238 ? -57.294 -33.068 36.066  1.00 36.54 ? 238 GLU B C   1 
ATOM   1897 O  O   . GLU A 1 238 ? -56.792 -32.051 36.531  1.00 37.10 ? 238 GLU B O   1 
ATOM   1898 C  CB  . GLU A 1 238 ? -56.810 -33.611 33.557  1.00 37.65 ? 238 GLU B CB  1 
ATOM   1899 C  CG  . GLU A 1 238 ? -56.101 -34.969 33.818  1.00 36.74 ? 238 GLU B CG  1 
ATOM   1900 C  CD  . GLU A 1 238 ? -55.004 -35.318 32.744  1.00 39.19 ? 238 GLU B CD  1 
ATOM   1901 O  OE1 . GLU A 1 238 ? -54.616 -34.428 31.920  1.00 39.87 ? 238 GLU B OE1 1 
ATOM   1902 O  OE2 . GLU A 1 238 ? -54.501 -36.488 32.731  1.00 39.90 ? 238 GLU B OE2 1 
ATOM   1903 N  N   . ALA A 1 239 ? -57.491 -34.171 36.796  1.00 35.69 ? 239 ALA B N   1 
ATOM   1904 C  CA  . ALA A 1 239 ? -57.050 -34.260 38.219  1.00 34.20 ? 239 ALA B CA  1 
ATOM   1905 C  C   . ALA A 1 239 ? -55.550 -33.961 38.244  1.00 31.94 ? 239 ALA B C   1 
ATOM   1906 O  O   . ALA A 1 239 ? -54.796 -34.645 37.564  1.00 32.31 ? 239 ALA B O   1 
ATOM   1907 C  CB  . ALA A 1 239 ? -57.328 -35.645 38.785  1.00 33.76 ? 239 ALA B CB  1 
ATOM   1908 N  N   . ALA A 1 240 ? -55.158 -32.905 38.947  1.00 29.52 ? 240 ALA B N   1 
ATOM   1909 C  CA  . ALA A 1 240 ? -53.774 -32.491 39.017  1.00 26.35 ? 240 ALA B CA  1 
ATOM   1910 C  C   . ALA A 1 240 ? -52.809 -33.588 39.556  1.00 25.28 ? 240 ALA B C   1 
ATOM   1911 O  O   . ALA A 1 240 ? -53.065 -34.318 40.542  1.00 21.69 ? 240 ALA B O   1 
ATOM   1912 C  CB  . ALA A 1 240 ? -53.643 -31.204 39.783  1.00 26.05 ? 240 ALA B CB  1 
ATOM   1913 N  N   . ALA A 1 241 ? -51.697 -33.750 38.840  1.00 22.43 ? 241 ALA B N   1 
ATOM   1914 C  CA  . ALA A 1 241 ? -50.596 -34.590 39.331  1.00 20.85 ? 241 ALA B CA  1 
ATOM   1915 C  C   . ALA A 1 241 ? -49.351 -33.802 38.946  1.00 19.98 ? 241 ALA B C   1 
ATOM   1916 O  O   . ALA A 1 241 ? -49.305 -33.199 37.852  1.00 19.74 ? 241 ALA B O   1 
ATOM   1917 C  CB  . ALA A 1 241 ? -50.607 -35.959 38.659  1.00 19.90 ? 241 ALA B CB  1 
ATOM   1918 N  N   . PHE A 1 242 ? -48.395 -33.786 39.856  1.00 18.38 ? 242 PHE B N   1 
ATOM   1919 C  CA  . PHE A 1 242 ? -47.156 -33.041 39.676  1.00 18.12 ? 242 PHE B CA  1 
ATOM   1920 C  C   . PHE A 1 242 ? -46.120 -33.848 38.926  1.00 17.72 ? 242 PHE B C   1 
ATOM   1921 O  O   . PHE A 1 242 ? -45.974 -35.077 39.121  1.00 13.96 ? 242 PHE B O   1 
ATOM   1922 C  CB  . PHE A 1 242 ? -46.571 -32.576 41.033  1.00 17.96 ? 242 PHE B CB  1 
ATOM   1923 C  CG  . PHE A 1 242 ? -47.399 -31.552 41.728  1.00 18.98 ? 242 PHE B CG  1 
ATOM   1924 C  CD1 . PHE A 1 242 ? -48.392 -31.946 42.611  1.00 21.03 ? 242 PHE B CD1 1 
ATOM   1925 C  CD2 . PHE A 1 242 ? -47.181 -30.168 41.498  1.00 19.29 ? 242 PHE B CD2 1 
ATOM   1926 C  CE1 . PHE A 1 242 ? -49.174 -30.981 43.305  1.00 22.92 ? 242 PHE B CE1 1 
ATOM   1927 C  CE2 . PHE A 1 242 ? -47.948 -29.187 42.174  1.00 22.42 ? 242 PHE B CE2 1 
ATOM   1928 C  CZ  . PHE A 1 242 ? -48.973 -29.612 43.082  1.00 21.91 ? 242 PHE B CZ  1 
ATOM   1929 N  N   . LEU A 1 243 ? -45.348 -33.123 38.109  1.00 17.15 ? 243 LEU B N   1 
ATOM   1930 C  CA  . LEU A 1 243 ? -44.241 -33.746 37.398  1.00 16.76 ? 243 LEU B CA  1 
ATOM   1931 C  C   . LEU A 1 243 ? -42.957 -33.721 38.275  1.00 15.90 ? 243 LEU B C   1 
ATOM   1932 O  O   . LEU A 1 243 ? -42.031 -32.950 37.978  1.00 13.51 ? 243 LEU B O   1 
ATOM   1933 C  CB  . LEU A 1 243 ? -44.050 -32.996 36.042  1.00 16.04 ? 243 LEU B CB  1 
ATOM   1934 C  CG  . LEU A 1 243 ? -43.014 -33.543 35.071  1.00 16.47 ? 243 LEU B CG  1 
ATOM   1935 C  CD1 . LEU A 1 243 ? -43.309 -34.968 34.650  1.00 9.10  ? 243 LEU B CD1 1 
ATOM   1936 C  CD2 . LEU A 1 243 ? -42.859 -32.645 33.844  1.00 15.13 ? 243 LEU B CD2 1 
ATOM   1937 N  N   . VAL A 1 244 ? -42.883 -34.557 39.346  1.00 14.29 ? 244 VAL B N   1 
ATOM   1938 C  CA  . VAL A 1 244 ? -41.783 -34.407 40.331  1.00 14.44 ? 244 VAL B CA  1 
ATOM   1939 C  C   . VAL A 1 244 ? -40.536 -35.133 39.909  1.00 12.49 ? 244 VAL B C   1 
ATOM   1940 O  O   . VAL A 1 244 ? -39.471 -34.894 40.452  1.00 13.98 ? 244 VAL B O   1 
ATOM   1941 C  CB  . VAL A 1 244 ? -42.187 -34.939 41.812  1.00 15.53 ? 244 VAL B CB  1 
ATOM   1942 C  CG1 . VAL A 1 244 ? -43.285 -34.070 42.364  1.00 15.56 ? 244 VAL B CG1 1 
ATOM   1943 C  CG2 . VAL A 1 244 ? -42.685 -36.385 41.695  1.00 17.06 ? 244 VAL B CG2 1 
ATOM   1944 N  N   . SER A 1 245 ? -40.685 -36.037 38.934  1.00 13.96 ? 245 SER B N   1 
ATOM   1945 C  CA  . SER A 1 245 ? -39.598 -36.861 38.394  1.00 13.39 ? 245 SER B CA  1 
ATOM   1946 C  C   . SER A 1 245 ? -39.932 -37.190 36.909  1.00 13.81 ? 245 SER B C   1 
ATOM   1947 O  O   . SER A 1 245 ? -41.076 -37.532 36.551  1.00 14.71 ? 245 SER B O   1 
ATOM   1948 C  CB  . SER A 1 245 ? -39.491 -38.175 39.148  1.00 12.62 ? 245 SER B CB  1 
ATOM   1949 O  OG  . SER A 1 245 ? -38.244 -38.804 38.872  1.00 15.35 ? 245 SER B OG  1 
ATOM   1950 N  N   . ASN A 1 246 ? -38.942 -37.075 36.038  1.00 14.25 ? 246 ASN B N   1 
ATOM   1951 C  CA  . ASN A 1 246 ? -39.198 -37.286 34.581  1.00 12.97 ? 246 ASN B CA  1 
ATOM   1952 C  C   . ASN A 1 246 ? -37.927 -37.804 33.869  1.00 12.17 ? 246 ASN B C   1 
ATOM   1953 O  O   . ASN A 1 246 ? -37.544 -37.377 32.746  1.00 11.03 ? 246 ASN B O   1 
ATOM   1954 C  CB  . ASN A 1 246 ? -39.772 -36.023 33.934  1.00 12.45 ? 246 ASN B CB  1 
ATOM   1955 C  CG  . ASN A 1 246 ? -38.765 -34.901 33.913  1.00 14.16 ? 246 ASN B CG  1 
ATOM   1956 O  OD1 . ASN A 1 246 ? -37.718 -35.014 34.562  1.00 13.13 ? 246 ASN B OD1 1 
ATOM   1957 N  ND2 . ASN A 1 246 ? -39.019 -33.872 33.125  1.00 11.79 ? 246 ASN B ND2 1 
ATOM   1958 N  N   . HIS A 1 247 ? -37.267 -38.729 34.541  1.00 11.78 ? 247 HIS B N   1 
ATOM   1959 C  CA  . HIS A 1 247 ? -36.015 -39.300 34.059  1.00 14.24 ? 247 HIS B CA  1 
ATOM   1960 C  C   . HIS A 1 247 ? -36.146 -40.810 33.830  1.00 14.27 ? 247 HIS B C   1 
ATOM   1961 O  O   . HIS A 1 247 ? -36.791 -41.548 34.595  1.00 13.70 ? 247 HIS B O   1 
ATOM   1962 C  CB  . HIS A 1 247 ? -34.735 -38.930 34.924  1.00 12.97 ? 247 HIS B CB  1 
ATOM   1963 C  CG  . HIS A 1 247 ? -34.778 -39.490 36.325  1.00 14.73 ? 247 HIS B CG  1 
ATOM   1964 N  ND1 . HIS A 1 247 ? -34.032 -40.583 36.738  1.00 14.75 ? 247 HIS B ND1 1 
ATOM   1965 C  CD2 . HIS A 1 247 ? -35.541 -39.137 37.384  1.00 15.70 ? 247 HIS B CD2 1 
ATOM   1966 C  CE1 . HIS A 1 247 ? -34.308 -40.843 38.001  1.00 17.84 ? 247 HIS B CE1 1 
ATOM   1967 N  NE2 . HIS A 1 247 ? -35.245 -40.010 38.410  1.00 15.97 ? 247 HIS B NE2 1 
ATOM   1968 N  N   . ARG A 1 248 ? -35.562 -41.271 32.734  1.00 14.51 ? 248 ARG B N   1 
ATOM   1969 C  CA  . ARG A 1 248 ? -35.536 -42.688 32.446  1.00 14.94 ? 248 ARG B CA  1 
ATOM   1970 C  C   . ARG A 1 248 ? -34.238 -43.285 32.946  1.00 15.02 ? 248 ARG B C   1 
ATOM   1971 O  O   . ARG A 1 248 ? -33.205 -42.645 32.764  1.00 13.73 ? 248 ARG B O   1 
ATOM   1972 C  CB  . ARG A 1 248 ? -35.651 -42.915 30.907  1.00 14.52 ? 248 ARG B CB  1 
ATOM   1973 C  CG  . ARG A 1 248 ? -35.649 -44.414 30.569  1.00 15.85 ? 248 ARG B CG  1 
ATOM   1974 C  CD  . ARG A 1 248 ? -35.554 -44.730 29.097  1.00 14.99 ? 248 ARG B CD  1 
ATOM   1975 N  NE  . ARG A 1 248 ? -36.007 -46.117 28.799  1.00 15.34 ? 248 ARG B NE  1 
ATOM   1976 C  CZ  . ARG A 1 248 ? -35.675 -46.808 27.707  1.00 13.71 ? 248 ARG B CZ  1 
ATOM   1977 N  NH1 . ARG A 1 248 ? -34.832 -46.325 26.774  1.00 13.24 ? 248 ARG B NH1 1 
ATOM   1978 N  NH2 . ARG A 1 248 ? -36.199 -47.990 27.544  1.00 14.95 ? 248 ARG B NH2 1 
ATOM   1979 N  N   . PRO A 1 249 ? -34.274 -44.513 33.590  1.00 15.61 ? 249 PRO B N   1 
ATOM   1980 C  CA  . PRO A 1 249 ? -33.039 -45.224 33.965  1.00 15.95 ? 249 PRO B CA  1 
ATOM   1981 C  C   . PRO A 1 249 ? -32.147 -45.604 32.782  1.00 15.71 ? 249 PRO B C   1 
ATOM   1982 O  O   . PRO A 1 249 ? -32.683 -45.819 31.678  1.00 15.15 ? 249 PRO B O   1 
ATOM   1983 C  CB  . PRO A 1 249 ? -33.539 -46.464 34.721  1.00 15.96 ? 249 PRO B CB  1 
ATOM   1984 C  CG  . PRO A 1 249 ? -34.966 -46.093 35.170  1.00 18.07 ? 249 PRO B CG  1 
ATOM   1985 C  CD  . PRO A 1 249 ? -35.485 -45.263 33.988  1.00 15.42 ? 249 PRO B CD  1 
ATOM   1986 N  N   . PRO A 1 250 ? -30.799 -45.632 32.998  1.00 15.09 ? 250 PRO B N   1 
ATOM   1987 C  CA  . PRO A 1 250 ? -29.862 -46.136 32.027  1.00 13.91 ? 250 PRO B CA  1 
ATOM   1988 C  C   . PRO A 1 250 ? -30.241 -47.510 31.576  1.00 14.48 ? 250 PRO B C   1 
ATOM   1989 O  O   . PRO A 1 250 ? -30.759 -48.328 32.366  1.00 13.85 ? 250 PRO B O   1 
ATOM   1990 C  CB  . PRO A 1 250 ? -28.536 -46.206 32.774  1.00 13.63 ? 250 PRO B CB  1 
ATOM   1991 C  CG  . PRO A 1 250 ? -28.627 -45.060 33.756  1.00 13.21 ? 250 PRO B CG  1 
ATOM   1992 C  CD  . PRO A 1 250 ? -30.092 -45.092 34.181  1.00 15.55 ? 250 PRO B CD  1 
ATOM   1993 N  N   . GLN A 1 251 ? -29.989 -47.737 30.307  1.00 12.12 ? 251 GLN B N   1 
ATOM   1994 C  CA  . GLN A 1 251 ? -30.336 -48.986 29.674  1.00 12.82 ? 251 GLN B CA  1 
ATOM   1995 C  C   . GLN A 1 251 ? -28.983 -49.660 29.319  1.00 13.99 ? 251 GLN B C   1 
ATOM   1996 O  O   . GLN A 1 251 ? -27.931 -48.991 29.246  1.00 14.72 ? 251 GLN B O   1 
ATOM   1997 C  CB  . GLN A 1 251 ? -31.192 -48.690 28.431  1.00 11.93 ? 251 GLN B CB  1 
ATOM   1998 C  CG  . GLN A 1 251 ? -32.628 -48.167 28.725  1.00 11.81 ? 251 GLN B CG  1 
ATOM   1999 C  CD  . GLN A 1 251 ? -33.398 -48.952 29.824  1.00 13.88 ? 251 GLN B CD  1 
ATOM   2000 O  OE1 . GLN A 1 251 ? -33.585 -50.134 29.714  1.00 16.90 ? 251 GLN B OE1 1 
ATOM   2001 N  NE2 . GLN A 1 251 ? -33.789 -48.282 30.855  1.00 15.08 ? 251 GLN B NE2 1 
ATOM   2002 N  N   . PRO A 1 252 ? -28.975 -50.979 29.157  1.00 15.71 ? 252 PRO B N   1 
ATOM   2003 C  CA  . PRO A 1 252 ? -27.676 -51.673 28.895  1.00 17.16 ? 252 PRO B CA  1 
ATOM   2004 C  C   . PRO A 1 252 ? -27.052 -51.257 27.579  1.00 17.48 ? 252 PRO B C   1 
ATOM   2005 O  O   . PRO A 1 252 ? -27.802 -50.996 26.627  1.00 16.74 ? 252 PRO B O   1 
ATOM   2006 C  CB  . PRO A 1 252 ? -28.098 -53.145 28.820  1.00 17.16 ? 252 PRO B CB  1 
ATOM   2007 C  CG  . PRO A 1 252 ? -29.397 -53.193 29.544  1.00 17.40 ? 252 PRO B CG  1 
ATOM   2008 C  CD  . PRO A 1 252 ? -30.084 -51.946 29.188  1.00 16.67 ? 252 PRO B CD  1 
ATOM   2009 N  N   . LEU A 1 253 ? -25.712 -51.260 27.509  1.00 17.87 ? 253 LEU B N   1 
ATOM   2010 C  CA  . LEU A 1 253 ? -24.961 -50.909 26.289  1.00 19.12 ? 253 LEU B CA  1 
ATOM   2011 C  C   . LEU A 1 253 ? -25.163 -51.867 25.145  1.00 19.53 ? 253 LEU B C   1 
ATOM   2012 O  O   . LEU A 1 253 ? -25.148 -51.459 23.996  1.00 19.87 ? 253 LEU B O   1 
ATOM   2013 C  CB  . LEU A 1 253 ? -23.453 -50.733 26.551  1.00 19.34 ? 253 LEU B CB  1 
ATOM   2014 C  CG  . LEU A 1 253 ? -22.915 -49.321 26.690  1.00 23.73 ? 253 LEU B CG  1 
ATOM   2015 C  CD1 . LEU A 1 253 ? -23.496 -48.301 25.640  1.00 23.90 ? 253 LEU B CD1 1 
ATOM   2016 C  CD2 . LEU A 1 253 ? -23.196 -48.818 28.034  1.00 27.76 ? 253 LEU B CD2 1 
ATOM   2017 N  N   . LYS A 1 254 ? -25.307 -53.154 25.487  1.00 19.45 ? 254 LYS B N   1 
ATOM   2018 C  CA  . LYS A 1 254 ? -25.530 -54.201 24.541  1.00 20.87 ? 254 LYS B CA  1 
ATOM   2019 C  C   . LYS A 1 254 ? -24.502 -54.294 23.433  1.00 20.30 ? 254 LYS B C   1 
ATOM   2020 O  O   . LYS A 1 254 ? -24.870 -54.556 22.309  1.00 21.86 ? 254 LYS B O   1 
ATOM   2021 C  CB  . LYS A 1 254 ? -26.960 -54.111 23.991  1.00 22.02 ? 254 LYS B CB  1 
ATOM   2022 C  CG  . LYS A 1 254 ? -27.927 -54.632 24.999  1.00 24.02 ? 254 LYS B CG  1 
ATOM   2023 C  CD  . LYS A 1 254 ? -29.282 -54.466 24.555  1.00 31.28 ? 254 LYS B CD  1 
ATOM   2024 C  CE  . LYS A 1 254 ? -30.160 -55.524 25.213  1.00 37.93 ? 254 LYS B CE  1 
ATOM   2025 N  NZ  . LYS A 1 254 ? -29.630 -55.958 26.569  1.00 41.15 ? 254 LYS B NZ  1 
ATOM   2026 N  N   . GLY A 1 255 ? -23.227 -54.053 23.755  1.00 19.60 ? 255 GLY B N   1 
ATOM   2027 C  CA  . GLY A 1 255 ? -22.122 -54.152 22.780  1.00 19.57 ? 255 GLY B CA  1 
ATOM   2028 C  C   . GLY A 1 255 ? -21.636 -52.818 22.233  1.00 20.31 ? 255 GLY B C   1 
ATOM   2029 O  O   . GLY A 1 255 ? -20.580 -52.755 21.567  1.00 20.82 ? 255 GLY B O   1 
ATOM   2030 N  N   . ARG A 1 256 ? -22.412 -51.736 22.446  1.00 18.96 ? 256 ARG B N   1 
ATOM   2031 C  CA  . ARG A 1 256 ? -21.985 -50.415 21.962  1.00 18.60 ? 256 ARG B CA  1 
ATOM   2032 C  C   . ARG A 1 256 ? -20.794 -49.918 22.733  1.00 19.56 ? 256 ARG B C   1 
ATOM   2033 O  O   . ARG A 1 256 ? -20.626 -50.263 23.908  1.00 19.44 ? 256 ARG B O   1 
ATOM   2034 C  CB  . ARG A 1 256 ? -23.105 -49.351 22.116  1.00 18.89 ? 256 ARG B CB  1 
ATOM   2035 C  CG  . ARG A 1 256 ? -24.378 -49.711 21.318  1.00 17.75 ? 256 ARG B CG  1 
ATOM   2036 C  CD  . ARG A 1 256 ? -25.440 -48.737 21.717  1.00 14.88 ? 256 ARG B CD  1 
ATOM   2037 N  NE  . ARG A 1 256 ? -26.053 -49.104 22.992  1.00 14.42 ? 256 ARG B NE  1 
ATOM   2038 C  CZ  . ARG A 1 256 ? -26.969 -48.378 23.611  1.00 12.79 ? 256 ARG B CZ  1 
ATOM   2039 N  NH1 . ARG A 1 256 ? -27.325 -47.206 23.097  1.00 14.57 ? 256 ARG B NH1 1 
ATOM   2040 N  NH2 . ARG A 1 256 ? -27.475 -48.787 24.757  1.00 13.91 ? 256 ARG B NH2 1 
ATOM   2041 N  N   . LYS A 1 257 ? -19.992 -49.091 22.094  1.00 20.08 ? 257 LYS B N   1 
ATOM   2042 C  CA  . LYS A 1 257 ? -18.825 -48.542 22.771  1.00 23.14 ? 257 LYS B CA  1 
ATOM   2043 C  C   . LYS A 1 257 ? -18.960 -46.983 22.816  1.00 23.03 ? 257 LYS B C   1 
ATOM   2044 O  O   . LYS A 1 257 ? -19.410 -46.367 21.862  1.00 25.88 ? 257 LYS B O   1 
ATOM   2045 C  CB  . LYS A 1 257 ? -17.517 -49.056 22.128  1.00 24.32 ? 257 LYS B CB  1 
ATOM   2046 C  CG  . LYS A 1 257 ? -17.399 -50.610 22.098  1.00 25.10 ? 257 LYS B CG  1 
ATOM   2047 C  CD  . LYS A 1 257 ? -15.998 -51.021 21.762  1.00 31.43 ? 257 LYS B CD  1 
ATOM   2048 C  CE  . LYS A 1 257 ? -15.829 -52.494 21.978  1.00 33.71 ? 257 LYS B CE  1 
ATOM   2049 N  NZ  . LYS A 1 257 ? -16.187 -53.187 20.761  1.00 35.40 ? 257 LYS B NZ  1 
ATOM   2050 N  N   . VAL A 1 258 ? -18.709 -46.401 23.974  1.00 22.60 ? 258 VAL B N   1 
ATOM   2051 C  CA  . VAL A 1 258 ? -18.759 -44.946 24.175  1.00 21.16 ? 258 VAL B CA  1 
ATOM   2052 C  C   . VAL A 1 258 ? -17.386 -44.401 23.856  1.00 21.43 ? 258 VAL B C   1 
ATOM   2053 O  O   . VAL A 1 258 ? -16.386 -44.963 24.329  1.00 21.67 ? 258 VAL B O   1 
ATOM   2054 C  CB  . VAL A 1 258 ? -19.165 -44.626 25.627  1.00 22.22 ? 258 VAL B CB  1 
ATOM   2055 C  CG1 . VAL A 1 258 ? -19.361 -43.058 25.874  1.00 18.20 ? 258 VAL B CG1 1 
ATOM   2056 C  CG2 . VAL A 1 258 ? -20.398 -45.421 25.969  1.00 20.55 ? 258 VAL B CG2 1 
ATOM   2057 N  N   . ARG A 1 259 ? -17.338 -43.366 23.020  1.00 20.27 ? 259 ARG B N   1 
ATOM   2058 C  CA  . ARG A 1 259 ? -16.088 -42.661 22.688  1.00 22.59 ? 259 ARG B CA  1 
ATOM   2059 C  C   . ARG A 1 259 ? -15.990 -41.324 23.398  1.00 22.37 ? 259 ARG B C   1 
ATOM   2060 O  O   . ARG A 1 259 ? -17.000 -40.712 23.704  1.00 22.79 ? 259 ARG B O   1 
ATOM   2061 C  CB  . ARG A 1 259 ? -15.954 -42.464 21.175  1.00 22.97 ? 259 ARG B CB  1 
ATOM   2062 C  CG  . ARG A 1 259 ? -16.120 -43.762 20.376  1.00 23.36 ? 259 ARG B CG  1 
ATOM   2063 C  CD  . ARG A 1 259 ? -16.099 -43.513 18.898  1.00 25.47 ? 259 ARG B CD  1 
ATOM   2064 N  NE  . ARG A 1 259 ? -17.277 -42.751 18.439  1.00 28.50 ? 259 ARG B NE  1 
ATOM   2065 C  CZ  . ARG A 1 259 ? -17.356 -42.006 17.344  1.00 25.56 ? 259 ARG B CZ  1 
ATOM   2066 N  NH1 . ARG A 1 259 ? -16.325 -41.861 16.503  1.00 25.45 ? 259 ARG B NH1 1 
ATOM   2067 N  NH2 . ARG A 1 259 ? -18.508 -41.428 17.070  1.00 26.34 ? 259 ARG B NH2 1 
ATOM   2068 N  N   . ALA A 1 260 ? -14.757 -40.890 23.659  1.00 22.30 ? 260 ALA B N   1 
ATOM   2069 C  CA  . ALA A 1 260 ? -14.476 -39.627 24.301  1.00 20.74 ? 260 ALA B CA  1 
ATOM   2070 C  C   . ALA A 1 260 ? -13.711 -38.704 23.355  1.00 21.01 ? 260 ALA B C   1 
ATOM   2071 O  O   . ALA A 1 260 ? -12.807 -39.135 22.590  1.00 20.39 ? 260 ALA B O   1 
ATOM   2072 C  CB  . ALA A 1 260 ? -13.715 -39.861 25.578  1.00 20.89 ? 260 ALA B CB  1 
ATOM   2073 N  N   . SER A 1 261 ? -14.085 -37.425 23.427  1.00 19.98 ? 261 SER B N   1 
ATOM   2074 C  CA  . SER A 1 261 ? -13.501 -36.405 22.656  1.00 19.92 ? 261 SER B CA  1 
ATOM   2075 C  C   . SER A 1 261 ? -12.115 -35.939 23.182  1.00 20.61 ? 261 SER B C   1 
ATOM   2076 O  O   . SER A 1 261 ? -11.470 -35.056 22.572  1.00 20.42 ? 261 SER B O   1 
ATOM   2077 C  CB  . SER A 1 261 ? -14.449 -35.220 22.603  1.00 19.17 ? 261 SER B CB  1 
ATOM   2078 O  OG  . SER A 1 261 ? -14.478 -34.530 23.808  1.00 16.27 ? 261 SER B OG  1 
ATOM   2079 N  N   . PHE A 1 262 ? -11.699 -36.534 24.301  1.00 21.35 ? 262 PHE B N   1 
ATOM   2080 C  CA  . PHE A 1 262 ? -10.657 -35.967 25.136  1.00 23.38 ? 262 PHE B CA  1 
ATOM   2081 C  C   . PHE A 1 262 ? -9.875  -37.090 25.815  1.00 25.71 ? 262 PHE B C   1 
ATOM   2082 O  O   . PHE A 1 262 ? -10.397 -38.180 26.023  1.00 23.29 ? 262 PHE B O   1 
ATOM   2083 C  CB  . PHE A 1 262 ? -11.290 -35.065 26.222  1.00 22.68 ? 262 PHE B CB  1 
ATOM   2084 C  CG  . PHE A 1 262 ? -12.154 -35.815 27.195  1.00 23.42 ? 262 PHE B CG  1 
ATOM   2085 C  CD1 . PHE A 1 262 ? -11.624 -36.302 28.422  1.00 21.59 ? 262 PHE B CD1 1 
ATOM   2086 C  CD2 . PHE A 1 262 ? -13.479 -36.098 26.886  1.00 19.06 ? 262 PHE B CD2 1 
ATOM   2087 C  CE1 . PHE A 1 262 ? -12.438 -36.995 29.297  1.00 22.30 ? 262 PHE B CE1 1 
ATOM   2088 C  CE2 . PHE A 1 262 ? -14.286 -36.785 27.750  1.00 19.85 ? 262 PHE B CE2 1 
ATOM   2089 C  CZ  . PHE A 1 262 ? -13.780 -37.262 28.953  1.00 21.61 ? 262 PHE B CZ  1 
ATOM   2090 N  N   . HIS A 1 263 ? -8.618  -36.806 26.183  1.00 29.83 ? 263 HIS B N   1 
ATOM   2091 C  CA  . HIS A 1 263 ? -7.844  -37.783 26.936  1.00 34.29 ? 263 HIS B CA  1 
ATOM   2092 C  C   . HIS A 1 263 ? -7.060  -37.160 28.056  1.00 36.44 ? 263 HIS B C   1 
ATOM   2093 O  O   . HIS A 1 263 ? -6.672  -37.915 28.963  1.00 37.79 ? 263 HIS B O   1 
ATOM   2094 C  CB  . HIS A 1 263 ? -6.924  -38.618 26.028  1.00 34.94 ? 263 HIS B CB  1 
ATOM   2095 C  CG  . HIS A 1 263 ? -6.082  -37.820 25.073  1.00 39.93 ? 263 HIS B CG  1 
ATOM   2096 N  ND1 . HIS A 1 263 ? -6.134  -36.445 24.973  1.00 43.49 ? 263 HIS B ND1 1 
ATOM   2097 C  CD2 . HIS A 1 263 ? -5.190  -38.226 24.134  1.00 43.10 ? 263 HIS B CD2 1 
ATOM   2098 C  CE1 . HIS A 1 263 ? -5.312  -36.035 24.021  1.00 45.11 ? 263 HIS B CE1 1 
ATOM   2099 N  NE2 . HIS A 1 263 ? -4.717  -37.098 23.503  1.00 45.97 ? 263 HIS B NE2 1 
ATOM   2100 O  OXT . HIS A 1 263 ? -6.790  -35.931 28.043  1.00 37.75 ? 263 HIS B OXT 1 
ATOM   2101 N  N   . LEU B 1 5   ? 0.859   10.238  16.746  1.00 43.81 ? 5   LEU A N   1 
ATOM   2102 C  CA  . LEU B 1 5   ? -0.071  11.408  16.448  1.00 44.00 ? 5   LEU A CA  1 
ATOM   2103 C  C   . LEU B 1 5   ? -0.512  11.530  14.976  1.00 42.31 ? 5   LEU A C   1 
ATOM   2104 O  O   . LEU B 1 5   ? -1.665  11.836  14.698  1.00 43.52 ? 5   LEU A O   1 
ATOM   2105 C  CB  . LEU B 1 5   ? 0.473   12.769  16.977  1.00 44.06 ? 5   LEU A CB  1 
ATOM   2106 C  CG  . LEU B 1 5   ? -0.067  13.192  18.374  1.00 47.00 ? 5   LEU A CG  1 
ATOM   2107 C  CD1 . LEU B 1 5   ? 0.469   14.594  18.883  1.00 48.81 ? 5   LEU A CD1 1 
ATOM   2108 C  CD2 . LEU B 1 5   ? -1.623  13.116  18.494  1.00 45.37 ? 5   LEU A CD2 1 
ATOM   2109 N  N   . SER B 1 6   ? 0.403   11.321  14.032  1.00 39.60 ? 6   SER A N   1 
ATOM   2110 C  CA  . SER B 1 6   ? 0.052   11.478  12.627  1.00 35.26 ? 6   SER A CA  1 
ATOM   2111 C  C   . SER B 1 6   ? 0.515   10.248  11.882  1.00 31.98 ? 6   SER A C   1 
ATOM   2112 O  O   . SER B 1 6   ? 0.804   10.323  10.694  1.00 31.82 ? 6   SER A O   1 
ATOM   2113 C  CB  . SER B 1 6   ? 0.693   12.744  12.053  1.00 36.01 ? 6   SER A CB  1 
ATOM   2114 O  OG  . SER B 1 6   ? 2.084   12.841  12.398  1.00 40.40 ? 6   SER A OG  1 
ATOM   2115 N  N   . TRP B 1 7   ? 0.598   9.122   12.592  1.00 26.23 ? 7   TRP A N   1 
ATOM   2116 C  CA  . TRP B 1 7   ? 0.894   7.823   11.984  1.00 22.44 ? 7   TRP A CA  1 
ATOM   2117 C  C   . TRP B 1 7   ? -0.165  7.455   10.942  1.00 20.28 ? 7   TRP A C   1 
ATOM   2118 O  O   . TRP B 1 7   ? -1.252  7.907   11.012  1.00 22.28 ? 7   TRP A O   1 
ATOM   2119 C  CB  . TRP B 1 7   ? 0.997   6.743   13.065  1.00 20.40 ? 7   TRP A CB  1 
ATOM   2120 C  CG  . TRP B 1 7   ? -0.348  6.384   13.720  1.00 19.89 ? 7   TRP A CG  1 
ATOM   2121 C  CD1 . TRP B 1 7   ? -0.890  6.912   14.863  1.00 18.15 ? 7   TRP A CD1 1 
ATOM   2122 C  CD2 . TRP B 1 7   ? -1.272  5.350   13.266  1.00 20.70 ? 7   TRP A CD2 1 
ATOM   2123 N  NE1 . TRP B 1 7   ? -2.117  6.296   15.137  1.00 19.41 ? 7   TRP A NE1 1 
ATOM   2124 C  CE2 . TRP B 1 7   ? -2.364  5.331   14.177  1.00 19.57 ? 7   TRP A CE2 1 
ATOM   2125 C  CE3 . TRP B 1 7   ? -1.262  4.442   12.182  1.00 20.14 ? 7   TRP A CE3 1 
ATOM   2126 C  CZ2 . TRP B 1 7   ? -3.454  4.453   14.031  1.00 17.67 ? 7   TRP A CZ2 1 
ATOM   2127 C  CZ3 . TRP B 1 7   ? -2.351  3.522   12.045  1.00 18.67 ? 7   TRP A CZ3 1 
ATOM   2128 C  CH2 . TRP B 1 7   ? -3.414  3.539   12.978  1.00 19.13 ? 7   TRP A CH2 1 
ATOM   2129 N  N   . GLY B 1 8   ? 0.189   6.663   9.951   1.00 19.06 ? 8   GLY A N   1 
ATOM   2130 C  CA  . GLY B 1 8   ? -0.753  6.316   8.946   1.00 19.54 ? 8   GLY A CA  1 
ATOM   2131 C  C   . GLY B 1 8   ? -0.200  5.144   8.174   1.00 18.23 ? 8   GLY A C   1 
ATOM   2132 O  O   . GLY B 1 8   ? 0.540   4.310   8.735   1.00 19.12 ? 8   GLY A O   1 
ATOM   2133 N  N   . TYR B 1 9   ? -0.557  5.072   6.885   1.00 16.59 ? 9   TYR A N   1 
ATOM   2134 C  CA  . TYR B 1 9   ? -0.026  4.028   6.069   1.00 18.29 ? 9   TYR A CA  1 
ATOM   2135 C  C   . TYR B 1 9   ? 0.626   4.623   4.840   1.00 20.13 ? 9   TYR A C   1 
ATOM   2136 O  O   . TYR B 1 9   ? 0.833   3.970   3.861   1.00 20.79 ? 9   TYR A O   1 
ATOM   2137 C  CB  . TYR B 1 9   ? -1.117  2.998   5.724   1.00 17.18 ? 9   TYR A CB  1 
ATOM   2138 C  CG  . TYR B 1 9   ? -1.674  2.257   6.932   1.00 14.94 ? 9   TYR A CG  1 
ATOM   2139 C  CD1 . TYR B 1 9   ? -1.073  1.080   7.376   1.00 17.47 ? 9   TYR A CD1 1 
ATOM   2140 C  CD2 . TYR B 1 9   ? -2.811  2.726   7.605   1.00 18.19 ? 9   TYR A CD2 1 
ATOM   2141 C  CE1 . TYR B 1 9   ? -1.582  0.398   8.435   1.00 11.28 ? 9   TYR A CE1 1 
ATOM   2142 C  CE2 . TYR B 1 9   ? -3.349  2.047   8.676   1.00 13.90 ? 9   TYR A CE2 1 
ATOM   2143 C  CZ  . TYR B 1 9   ? -2.742  0.886   9.072   1.00 13.21 ? 9   TYR A CZ  1 
ATOM   2144 O  OH  . TYR B 1 9   ? -3.257  0.224   10.149  1.00 13.79 ? 9   TYR A OH  1 
ATOM   2145 N  N   . ARG B 1 10  ? 0.962   5.896   4.926   1.00 22.18 ? 10  ARG A N   1 
ATOM   2146 C  CA  . ARG B 1 10  ? 1.628   6.560   3.812   1.00 23.68 ? 10  ARG A CA  1 
ATOM   2147 C  C   . ARG B 1 10  ? 3.145   6.396   3.930   1.00 23.92 ? 10  ARG A C   1 
ATOM   2148 O  O   . ARG B 1 10  ? 3.692   5.796   4.870   1.00 22.06 ? 10  ARG A O   1 
ATOM   2149 C  CB  . ARG B 1 10  ? 1.162   8.014   3.739   1.00 24.63 ? 10  ARG A CB  1 
ATOM   2150 C  CG  . ARG B 1 10  ? -0.326  8.131   3.364   1.00 25.18 ? 10  ARG A CG  1 
ATOM   2151 C  CD  . ARG B 1 10  ? -0.900  9.532   3.675   1.00 26.58 ? 10  ARG A CD  1 
ATOM   2152 N  NE  . ARG B 1 10  ? -0.677  10.429  2.539   1.00 31.54 ? 10  ARG A NE  1 
ATOM   2153 C  CZ  . ARG B 1 10  ? -1.086  11.694  2.434   1.00 30.87 ? 10  ARG A CZ  1 
ATOM   2154 N  NH1 . ARG B 1 10  ? -1.774  12.282  3.413   1.00 31.84 ? 10  ARG A NH1 1 
ATOM   2155 N  NH2 . ARG B 1 10  ? -0.808  12.369  1.328   1.00 26.98 ? 10  ARG A NH2 1 
ATOM   2156 N  N   . GLU B 1 11  ? 3.839   6.846   2.905   1.00 24.84 ? 11  GLU A N   1 
ATOM   2157 C  CA  . GLU B 1 11  ? 5.283   6.733   2.869   1.00 25.72 ? 11  GLU A CA  1 
ATOM   2158 C  C   . GLU B 1 11  ? 6.030   7.261   4.107   1.00 24.36 ? 11  GLU A C   1 
ATOM   2159 O  O   . GLU B 1 11  ? 6.904   6.580   4.651   1.00 23.82 ? 11  GLU A O   1 
ATOM   2160 C  CB  . GLU B 1 11  ? 5.781   7.440   1.621   1.00 27.60 ? 11  GLU A CB  1 
ATOM   2161 C  CG  . GLU B 1 11  ? 7.302   7.487   1.553   1.00 33.69 ? 11  GLU A CG  1 
ATOM   2162 C  CD  . GLU B 1 11  ? 7.758   8.145   0.276   1.00 40.83 ? 11  GLU A CD  1 
ATOM   2163 O  OE1 . GLU B 1 11  ? 7.345   9.318   0.033   1.00 41.60 ? 11  GLU A OE1 1 
ATOM   2164 O  OE2 . GLU B 1 11  ? 8.502   7.468   -0.473  1.00 43.77 ? 11  GLU A OE2 1 
ATOM   2165 N  N   A HIS B 1 12  ? 5.660   8.465   4.527   0.50 24.45 ? 12  HIS A N   1 
ATOM   2166 N  N   B HIS B 1 12  ? 5.698   8.467   4.557   0.50 24.36 ? 12  HIS A N   1 
ATOM   2167 C  CA  A HIS B 1 12  ? 6.306   9.185   5.622   0.50 24.66 ? 12  HIS A CA  1 
ATOM   2168 C  CA  B HIS B 1 12  ? 6.462   9.089   5.648   0.50 24.26 ? 12  HIS A CA  1 
ATOM   2169 C  C   A HIS B 1 12  ? 5.942   8.606   6.980   0.50 24.16 ? 12  HIS A C   1 
ATOM   2170 C  C   B HIS B 1 12  ? 5.793   8.945   7.021   0.50 24.09 ? 12  HIS A C   1 
ATOM   2171 O  O   A HIS B 1 12  ? 6.749   8.572   7.913   0.50 24.21 ? 12  HIS A O   1 
ATOM   2172 O  O   B HIS B 1 12  ? 6.264   9.537   8.018   0.50 23.29 ? 12  HIS A O   1 
ATOM   2173 C  CB  A HIS B 1 12  ? 5.863   10.655  5.584   0.50 25.20 ? 12  HIS A CB  1 
ATOM   2174 C  CB  B HIS B 1 12  ? 6.772   10.563  5.337   0.50 25.34 ? 12  HIS A CB  1 
ATOM   2175 C  CG  A HIS B 1 12  ? 4.454   10.862  5.101   0.50 26.94 ? 12  HIS A CG  1 
ATOM   2176 C  CG  B HIS B 1 12  ? 7.561   10.766  4.078   0.50 24.52 ? 12  HIS A CG  1 
ATOM   2177 N  ND1 A HIS B 1 12  ? 3.443   11.316  5.927   0.50 26.38 ? 12  HIS A ND1 1 
ATOM   2178 N  ND1 B HIS B 1 12  ? 8.793   10.183  3.873   0.50 28.11 ? 12  HIS A ND1 1 
ATOM   2179 C  CD2 A HIS B 1 12  ? 3.890   10.680  3.878   0.50 24.40 ? 12  HIS A CD2 1 
ATOM   2180 C  CD2 B HIS B 1 12  ? 7.308   11.505  2.971   0.50 26.55 ? 12  HIS A CD2 1 
ATOM   2181 C  CE1 A HIS B 1 12  ? 2.326   11.417  5.231   0.50 25.70 ? 12  HIS A CE1 1 
ATOM   2182 C  CE1 B HIS B 1 12  ? 9.251   10.529  2.681   0.50 27.36 ? 12  HIS A CE1 1 
ATOM   2183 N  NE2 A HIS B 1 12  ? 2.574   11.052  3.985   0.50 25.81 ? 12  HIS A NE2 1 
ATOM   2184 N  NE2 B HIS B 1 12  ? 8.375   11.338  2.118   0.50 24.58 ? 12  HIS A NE2 1 
ATOM   2185 N  N   . ASN B 1 13  ? 4.695   8.178   7.082   1.00 22.79 ? 13  ASN A N   1 
ATOM   2186 C  CA  . ASN B 1 13  ? 4.074   7.904   8.391   1.00 21.44 ? 13  ASN A CA  1 
ATOM   2187 C  C   . ASN B 1 13  ? 3.706   6.462   8.585   1.00 19.99 ? 13  ASN A C   1 
ATOM   2188 O  O   . ASN B 1 13  ? 3.058   6.124   9.600   1.00 19.84 ? 13  ASN A O   1 
ATOM   2189 C  CB  . ASN B 1 13  ? 2.855   8.837   8.606   1.00 20.93 ? 13  ASN A CB  1 
ATOM   2190 C  CG  . ASN B 1 13  ? 1.736   8.580   7.645   1.00 20.82 ? 13  ASN A CG  1 
ATOM   2191 O  OD1 . ASN B 1 13  ? 1.756   7.619   6.874   1.00 22.93 ? 13  ASN A OD1 1 
ATOM   2192 N  ND2 . ASN B 1 13  ? 0.708   9.402   7.721   1.00 21.86 ? 13  ASN A ND2 1 
ATOM   2193 N  N   . GLY B 1 14  ? 4.120   5.631   7.622   1.00 19.27 ? 14  GLY A N   1 
ATOM   2194 C  CA  . GLY B 1 14  ? 3.691   4.210   7.472   1.00 18.98 ? 14  GLY A CA  1 
ATOM   2195 C  C   . GLY B 1 14  ? 4.364   3.255   8.452   1.00 19.84 ? 14  GLY A C   1 
ATOM   2196 O  O   . GLY B 1 14  ? 5.256   3.672   9.169   1.00 19.87 ? 14  GLY A O   1 
ATOM   2197 N  N   . PRO B 1 15  ? 3.910   1.972   8.501   1.00 19.19 ? 15  PRO A N   1 
ATOM   2198 C  CA  . PRO B 1 15  ? 4.415   0.953   9.397   1.00 19.55 ? 15  PRO A CA  1 
ATOM   2199 C  C   . PRO B 1 15  ? 5.954   0.977   9.705   1.00 20.30 ? 15  PRO A C   1 
ATOM   2200 O  O   . PRO B 1 15  ? 6.355   0.806   10.851  1.00 21.62 ? 15  PRO A O   1 
ATOM   2201 C  CB  . PRO B 1 15  ? 3.965   -0.340  8.687   1.00 17.65 ? 15  PRO A CB  1 
ATOM   2202 C  CG  . PRO B 1 15  ? 2.574   0.006   8.224   1.00 17.31 ? 15  PRO A CG  1 
ATOM   2203 C  CD  . PRO B 1 15  ? 2.798   1.443   7.676   1.00 19.25 ? 15  PRO A CD  1 
ATOM   2204 N  N   A ILE B 1 16  ? 6.772   1.163   8.674   0.50 21.19 ? 16  ILE A N   1 
ATOM   2205 N  N   B ILE B 1 16  ? 6.805   1.134   8.696   0.50 21.07 ? 16  ILE A N   1 
ATOM   2206 C  CA  A ILE B 1 16  ? 8.227   1.251   8.824   0.50 21.51 ? 16  ILE A CA  1 
ATOM   2207 C  CA  B ILE B 1 16  ? 8.253   1.169   8.964   0.50 21.27 ? 16  ILE A CA  1 
ATOM   2208 C  C   A ILE B 1 16  ? 8.678   2.376   9.768   0.50 21.08 ? 16  ILE A C   1 
ATOM   2209 C  C   B ILE B 1 16  ? 8.684   2.374   9.825   0.50 21.01 ? 16  ILE A C   1 
ATOM   2210 O  O   A ILE B 1 16  ? 9.733   2.299   10.390  0.50 22.30 ? 16  ILE A O   1 
ATOM   2211 O  O   B ILE B 1 16  ? 9.732   2.351   10.462  0.50 22.29 ? 16  ILE A O   1 
ATOM   2212 C  CB  A ILE B 1 16  ? 8.928   1.442   7.438   0.50 21.12 ? 16  ILE A CB  1 
ATOM   2213 C  CB  B ILE B 1 16  ? 9.153   1.049   7.664   0.50 20.84 ? 16  ILE A CB  1 
ATOM   2214 C  CG1 A ILE B 1 16  ? 10.353  0.891   7.476   0.50 21.75 ? 16  ILE A CG1 1 
ATOM   2215 C  CG1 B ILE B 1 16  ? 9.255   2.393   6.934   0.50 21.58 ? 16  ILE A CG1 1 
ATOM   2216 C  CG2 A ILE B 1 16  ? 8.895   2.927   6.995   0.50 21.73 ? 16  ILE A CG2 1 
ATOM   2217 C  CG2 B ILE B 1 16  ? 8.687   -0.102  6.774   0.50 19.20 ? 16  ILE A CG2 1 
ATOM   2218 C  CD1 A ILE B 1 16  ? 10.435  -0.581  7.149   0.50 22.75 ? 16  ILE A CD1 1 
ATOM   2219 C  CD1 B ILE B 1 16  ? 10.544  2.596   6.104   0.50 22.23 ? 16  ILE A CD1 1 
ATOM   2220 N  N   . HIS B 1 17  ? 7.877   3.419   9.865   1.00 21.86 ? 17  HIS A N   1 
ATOM   2221 C  CA  . HIS B 1 17  ? 8.218   4.587   10.665  1.00 23.17 ? 17  HIS A CA  1 
ATOM   2222 C  C   . HIS B 1 17  ? 7.549   4.617   12.012  1.00 23.28 ? 17  HIS A C   1 
ATOM   2223 O  O   . HIS B 1 17  ? 7.757   5.562   12.768  1.00 24.45 ? 17  HIS A O   1 
ATOM   2224 C  CB  . HIS B 1 17  ? 7.809   5.862   9.954   1.00 23.78 ? 17  HIS A CB  1 
ATOM   2225 C  CG  . HIS B 1 17  ? 8.471   6.061   8.629   1.00 27.28 ? 17  HIS A CG  1 
ATOM   2226 N  ND1 . HIS B 1 17  ? 9.817   6.295   8.506   1.00 30.64 ? 17  HIS A ND1 1 
ATOM   2227 C  CD2 . HIS B 1 17  ? 7.969   6.075   7.373   1.00 27.37 ? 17  HIS A CD2 1 
ATOM   2228 C  CE1 . HIS B 1 17  ? 10.127  6.415   7.227   1.00 32.60 ? 17  HIS A CE1 1 
ATOM   2229 N  NE2 . HIS B 1 17  ? 9.022   6.300   6.518   1.00 30.01 ? 17  HIS A NE2 1 
ATOM   2230 N  N   . TRP B 1 18  ? 6.711   3.631   12.317  1.00 22.82 ? 18  TRP A N   1 
ATOM   2231 C  CA  . TRP B 1 18  ? 5.911   3.690   13.562  1.00 22.09 ? 18  TRP A CA  1 
ATOM   2232 C  C   . TRP B 1 18  ? 6.717   3.626   14.844  1.00 22.99 ? 18  TRP A C   1 
ATOM   2233 O  O   . TRP B 1 18  ? 6.297   4.203   15.840  1.00 23.13 ? 18  TRP A O   1 
ATOM   2234 C  CB  . TRP B 1 18  ? 4.849   2.598   13.598  1.00 19.95 ? 18  TRP A CB  1 
ATOM   2235 C  CG  . TRP B 1 18  ? 3.693   2.777   12.586  1.00 17.44 ? 18  TRP A CG  1 
ATOM   2236 C  CD1 . TRP B 1 18  ? 3.372   3.880   11.834  1.00 15.04 ? 18  TRP A CD1 1 
ATOM   2237 C  CD2 . TRP B 1 18  ? 2.677   1.816   12.352  1.00 16.66 ? 18  TRP A CD2 1 
ATOM   2238 N  NE1 . TRP B 1 18  ? 2.235   3.634   11.087  1.00 17.25 ? 18  TRP A NE1 1 
ATOM   2239 C  CE2 . TRP B 1 18  ? 1.775   2.371   11.407  1.00 16.90 ? 18  TRP A CE2 1 
ATOM   2240 C  CE3 . TRP B 1 18  ? 2.461   0.521   12.841  1.00 12.92 ? 18  TRP A CE3 1 
ATOM   2241 C  CZ2 . TRP B 1 18  ? 0.649   1.664   10.924  1.00 18.64 ? 18  TRP A CZ2 1 
ATOM   2242 C  CZ3 . TRP B 1 18  ? 1.328   -0.226  12.342  1.00 14.29 ? 18  TRP A CZ3 1 
ATOM   2243 C  CH2 . TRP B 1 18  ? 0.432   0.374   11.405  1.00 16.57 ? 18  TRP A CH2 1 
ATOM   2244 N  N   . LYS B 1 19  ? 7.848   2.923   14.801  1.00 23.89 ? 19  LYS A N   1 
ATOM   2245 C  CA  . LYS B 1 19  ? 8.792   2.813   15.911  1.00 26.82 ? 19  LYS A CA  1 
ATOM   2246 C  C   . LYS B 1 19  ? 9.342   4.210   16.312  1.00 28.09 ? 19  LYS A C   1 
ATOM   2247 O  O   . LYS B 1 19  ? 9.690   4.442   17.473  1.00 28.78 ? 19  LYS A O   1 
ATOM   2248 C  CB  . LYS B 1 19  ? 9.972   1.911   15.507  1.00 25.49 ? 19  LYS A CB  1 
ATOM   2249 C  CG  . LYS B 1 19  ? 10.807  2.521   14.384  1.00 28.66 ? 19  LYS A CG  1 
ATOM   2250 C  CD  . LYS B 1 19  ? 11.900  1.575   13.945  1.00 31.96 ? 19  LYS A CD  1 
ATOM   2251 C  CE  . LYS B 1 19  ? 11.332  0.588   12.962  1.00 38.81 ? 19  LYS A CE  1 
ATOM   2252 N  NZ  . LYS B 1 19  ? 11.476  1.023   11.530  1.00 40.86 ? 19  LYS A NZ  1 
ATOM   2253 N  N   . GLU B 1 20  ? 9.351   5.145   15.362  1.00 29.69 ? 20  GLU A N   1 
ATOM   2254 C  CA  . GLU B 1 20  ? 9.854   6.499   15.614  1.00 31.34 ? 20  GLU A CA  1 
ATOM   2255 C  C   . GLU B 1 20  ? 9.072   7.135   16.726  1.00 32.59 ? 20  GLU A C   1 
ATOM   2256 O  O   . GLU B 1 20  ? 9.615   7.870   17.540  1.00 34.64 ? 20  GLU A O   1 
ATOM   2257 C  CB  . GLU B 1 20  ? 9.825   7.330   14.326  1.00 29.82 ? 20  GLU A CB  1 
ATOM   2258 C  CG  . GLU B 1 20  ? 10.783  6.756   13.296  1.00 32.57 ? 20  GLU A CG  1 
ATOM   2259 C  CD  . GLU B 1 20  ? 10.618  7.368   11.928  1.00 34.78 ? 20  GLU A CD  1 
ATOM   2260 O  OE1 . GLU B 1 20  ? 10.070  8.490   11.841  1.00 38.50 ? 20  GLU A OE1 1 
ATOM   2261 O  OE2 . GLU B 1 20  ? 11.024  6.714   10.944  1.00 33.90 ? 20  GLU A OE2 1 
ATOM   2262 N  N   . PHE B 1 21  ? 7.787   6.822   16.798  1.00 33.55 ? 21  PHE A N   1 
ATOM   2263 C  CA  . PHE B 1 21  ? 6.984   7.356   17.851  1.00 33.36 ? 21  PHE A CA  1 
ATOM   2264 C  C   . PHE B 1 21  ? 6.336   6.349   18.847  1.00 30.60 ? 21  PHE A C   1 
ATOM   2265 O  O   . PHE B 1 21  ? 5.833   6.733   19.889  1.00 29.86 ? 21  PHE A O   1 
ATOM   2266 C  CB  . PHE B 1 21  ? 6.055   8.404   17.259  1.00 35.71 ? 21  PHE A CB  1 
ATOM   2267 C  CG  . PHE B 1 21  ? 6.820   9.567   16.646  1.00 40.43 ? 21  PHE A CG  1 
ATOM   2268 C  CD1 . PHE B 1 21  ? 6.973   10.770  17.332  1.00 44.31 ? 21  PHE A CD1 1 
ATOM   2269 C  CD2 . PHE B 1 21  ? 7.464   9.424   15.398  1.00 44.81 ? 21  PHE A CD2 1 
ATOM   2270 C  CE1 . PHE B 1 21  ? 7.716   11.839  16.762  1.00 46.59 ? 21  PHE A CE1 1 
ATOM   2271 C  CE2 . PHE B 1 21  ? 8.230   10.474  14.831  1.00 45.23 ? 21  PHE A CE2 1 
ATOM   2272 C  CZ  . PHE B 1 21  ? 8.348   11.687  15.517  1.00 44.58 ? 21  PHE A CZ  1 
ATOM   2273 N  N   . PHE B 1 22  ? 6.412   5.063   18.518  1.00 29.27 ? 22  PHE A N   1 
ATOM   2274 C  CA  . PHE B 1 22  ? 5.986   3.966   19.397  1.00 27.13 ? 22  PHE A CA  1 
ATOM   2275 C  C   . PHE B 1 22  ? 7.030   2.878   19.372  1.00 24.89 ? 22  PHE A C   1 
ATOM   2276 O  O   . PHE B 1 22  ? 6.899   1.894   18.640  1.00 25.04 ? 22  PHE A O   1 
ATOM   2277 C  CB  . PHE B 1 22  ? 4.635   3.408   18.954  1.00 27.92 ? 22  PHE A CB  1 
ATOM   2278 C  CG  . PHE B 1 22  ? 3.629   4.466   18.679  1.00 29.09 ? 22  PHE A CG  1 
ATOM   2279 C  CD1 . PHE B 1 22  ? 2.759   4.872   19.672  1.00 26.89 ? 22  PHE A CD1 1 
ATOM   2280 C  CD2 . PHE B 1 22  ? 3.613   5.120   17.429  1.00 31.28 ? 22  PHE A CD2 1 
ATOM   2281 C  CE1 . PHE B 1 22  ? 1.825   5.898   19.437  1.00 29.04 ? 22  PHE A CE1 1 
ATOM   2282 C  CE2 . PHE B 1 22  ? 2.701   6.136   17.181  1.00 32.26 ? 22  PHE A CE2 1 
ATOM   2283 C  CZ  . PHE B 1 22  ? 1.793   6.521   18.199  1.00 30.50 ? 22  PHE A CZ  1 
ATOM   2284 N  N   . PRO B 1 23  ? 8.091   3.036   20.180  1.00 23.14 ? 23  PRO A N   1 
ATOM   2285 C  CA  . PRO B 1 23  ? 9.227   2.090   20.189  1.00 20.72 ? 23  PRO A CA  1 
ATOM   2286 C  C   . PRO B 1 23  ? 8.827   0.621   20.347  1.00 18.79 ? 23  PRO A C   1 
ATOM   2287 O  O   . PRO B 1 23  ? 9.578   -0.253  19.888  1.00 17.79 ? 23  PRO A O   1 
ATOM   2288 C  CB  . PRO B 1 23  ? 10.086  2.605   21.379  1.00 19.70 ? 23  PRO A CB  1 
ATOM   2289 C  CG  . PRO B 1 23  ? 9.923   4.113   21.250  1.00 22.29 ? 23  PRO A CG  1 
ATOM   2290 C  CD  . PRO B 1 23  ? 8.356   4.197   21.065  1.00 23.13 ? 23  PRO A CD  1 
ATOM   2291 N  N   . ILE B 1 24  ? 7.677   0.344   21.006  1.00 17.88 ? 24  ILE A N   1 
ATOM   2292 C  CA  . ILE B 1 24  ? 7.210   -1.063  21.190  1.00 16.90 ? 24  ILE A CA  1 
ATOM   2293 C  C   . ILE B 1 24  ? 6.945   -1.787  19.837  1.00 17.71 ? 24  ILE A C   1 
ATOM   2294 O  O   . ILE B 1 24  ? 6.812   -3.010  19.787  1.00 18.63 ? 24  ILE A O   1 
ATOM   2295 C  CB  . ILE B 1 24  ? 5.952   -1.168  22.129  1.00 16.17 ? 24  ILE A CB  1 
ATOM   2296 C  CG1 . ILE B 1 24  ? 5.773   -2.593  22.658  1.00 17.09 ? 24  ILE A CG1 1 
ATOM   2297 C  CG2 . ILE B 1 24  ? 4.675   -0.722  21.456  1.00 13.97 ? 24  ILE A CG2 1 
ATOM   2298 C  CD1 . ILE B 1 24  ? 6.935   -3.087  23.366  1.00 16.41 ? 24  ILE A CD1 1 
ATOM   2299 N  N   . ALA B 1 25  ? 6.920   -1.012  18.768  1.00 18.14 ? 25  ALA A N   1 
ATOM   2300 C  CA  . ALA B 1 25  ? 6.888   -1.509  17.395  1.00 17.57 ? 25  ALA A CA  1 
ATOM   2301 C  C   . ALA B 1 25  ? 7.940   -2.559  17.161  1.00 18.11 ? 25  ALA A C   1 
ATOM   2302 O  O   . ALA B 1 25  ? 7.727   -3.514  16.357  1.00 16.44 ? 25  ALA A O   1 
ATOM   2303 C  CB  . ALA B 1 25  ? 7.011   -0.349  16.430  1.00 16.91 ? 25  ALA A CB  1 
ATOM   2304 N  N   . ASP B 1 26  ? 9.069   -2.438  17.904  1.00 18.71 ? 26  ASP A N   1 
ATOM   2305 C  CA  . ASP B 1 26  ? 10.182  -3.399  17.870  1.00 20.89 ? 26  ASP A CA  1 
ATOM   2306 C  C   . ASP B 1 26  ? 10.190  -4.433  19.029  1.00 21.38 ? 26  ASP A C   1 
ATOM   2307 O  O   . ASP B 1 26  ? 11.175  -5.163  19.229  1.00 20.56 ? 26  ASP A O   1 
ATOM   2308 C  CB  . ASP B 1 26  ? 11.524  -2.638  17.763  1.00 21.58 ? 26  ASP A CB  1 
ATOM   2309 C  CG  . ASP B 1 26  ? 11.626  -1.856  16.437  1.00 23.71 ? 26  ASP A CG  1 
ATOM   2310 O  OD1 . ASP B 1 26  ? 11.380  -2.426  15.369  1.00 29.21 ? 26  ASP A OD1 1 
ATOM   2311 O  OD2 . ASP B 1 26  ? 11.932  -0.667  16.471  1.00 30.27 ? 26  ASP A OD2 1 
ATOM   2312 N  N   . GLY B 1 27  ? 9.032   -4.569  19.679  1.00 21.53 ? 27  GLY A N   1 
ATOM   2313 C  CA  . GLY B 1 27  ? 8.821   -5.499  20.796  1.00 21.49 ? 27  GLY A CA  1 
ATOM   2314 C  C   . GLY B 1 27  ? 8.924   -6.978  20.452  1.00 21.77 ? 27  GLY A C   1 
ATOM   2315 O  O   . GLY B 1 27  ? 9.016   -7.367  19.256  1.00 21.56 ? 27  GLY A O   1 
ATOM   2316 N  N   . ASP B 1 28  ? 8.898   -7.799  21.497  1.00 20.76 ? 28  ASP A N   1 
ATOM   2317 C  CA  . ASP B 1 28  ? 8.944   -9.251  21.326  1.00 20.93 ? 28  ASP A CA  1 
ATOM   2318 C  C   . ASP B 1 28  ? 7.589   -9.893  21.072  1.00 18.72 ? 28  ASP A C   1 
ATOM   2319 O  O   . ASP B 1 28  ? 7.563   -11.056 20.778  1.00 18.81 ? 28  ASP A O   1 
ATOM   2320 C  CB  . ASP B 1 28  ? 9.497   -9.944  22.581  1.00 22.91 ? 28  ASP A CB  1 
ATOM   2321 C  CG  . ASP B 1 28  ? 10.938  -9.561  22.901  1.00 26.77 ? 28  ASP A CG  1 
ATOM   2322 O  OD1 . ASP B 1 28  ? 11.670  -9.146  21.996  1.00 31.61 ? 28  ASP A OD1 1 
ATOM   2323 O  OD2 . ASP B 1 28  ? 11.285  -9.674  24.074  1.00 30.68 ? 28  ASP A OD2 1 
ATOM   2324 N  N   . GLN B 1 29  ? 6.480   -9.174  21.248  1.00 17.57 ? 29  GLN A N   1 
ATOM   2325 C  CA  . GLN B 1 29  ? 5.122   -9.777  21.046  1.00 18.47 ? 29  GLN A CA  1 
ATOM   2326 C  C   . GLN B 1 29  ? 4.296   -8.964  20.054  1.00 17.44 ? 29  GLN A C   1 
ATOM   2327 O  O   . GLN B 1 29  ? 3.155   -8.582  20.301  1.00 15.97 ? 29  GLN A O   1 
ATOM   2328 C  CB  . GLN B 1 29  ? 4.403   -9.932  22.397  1.00 18.80 ? 29  GLN A CB  1 
ATOM   2329 C  CG  . GLN B 1 29  ? 5.242   -10.821 23.300  1.00 23.37 ? 29  GLN A CG  1 
ATOM   2330 C  CD  . GLN B 1 29  ? 4.415   -11.702 24.168  1.00 28.23 ? 29  GLN A CD  1 
ATOM   2331 O  OE1 . GLN B 1 29  ? 3.303   -11.333 24.561  1.00 19.64 ? 29  GLN A OE1 1 
ATOM   2332 N  NE2 . GLN B 1 29  ? 4.952   -12.895 24.475  1.00 29.06 ? 29  GLN A NE2 1 
ATOM   2333 N  N   . GLN B 1 30  ? 4.914   -8.686  18.907  1.00 17.21 ? 30  GLN A N   1 
ATOM   2334 C  CA  . GLN B 1 30  ? 4.302   -7.871  17.917  1.00 16.38 ? 30  GLN A CA  1 
ATOM   2335 C  C   . GLN B 1 30  ? 3.451   -8.636  16.895  1.00 14.47 ? 30  GLN A C   1 
ATOM   2336 O  O   . GLN B 1 30  ? 3.711   -9.782  16.587  1.00 14.95 ? 30  GLN A O   1 
ATOM   2337 C  CB  . GLN B 1 30  ? 5.360   -6.971  17.210  1.00 17.27 ? 30  GLN A CB  1 
ATOM   2338 C  CG  . GLN B 1 30  ? 5.775   -5.701  18.054  1.00 16.32 ? 30  GLN A CG  1 
ATOM   2339 C  CD  . GLN B 1 30  ? 4.645   -4.780  18.422  1.00 17.77 ? 30  GLN A CD  1 
ATOM   2340 O  OE1 . GLN B 1 30  ? 4.131   -3.998  17.576  1.00 15.85 ? 30  GLN A OE1 1 
ATOM   2341 N  NE2 . GLN B 1 30  ? 4.256   -4.806  19.716  1.00 15.03 ? 30  GLN A NE2 1 
ATOM   2342 N  N   . SER B 1 31  ? 2.445   -7.934  16.372  1.00 14.61 ? 31  SER A N   1 
ATOM   2343 C  CA  . SER B 1 31  ? 1.481   -8.494  15.392  1.00 13.42 ? 31  SER A CA  1 
ATOM   2344 C  C   . SER B 1 31  ? 1.328   -7.591  14.172  1.00 12.83 ? 31  SER A C   1 
ATOM   2345 O  O   . SER B 1 31  ? 1.495   -6.416  14.286  1.00 12.00 ? 31  SER A O   1 
ATOM   2346 C  CB  . SER B 1 31  ? 0.123   -8.605  16.045  1.00 10.91 ? 31  SER A CB  1 
ATOM   2347 O  OG  . SER B 1 31  ? 0.177   -9.656  17.013  1.00 14.34 ? 31  SER A OG  1 
ATOM   2348 N  N   . PRO B 1 32  ? 0.924   -8.141  12.988  1.00 12.88 ? 32  PRO A N   1 
ATOM   2349 C  CA  . PRO B 1 32  ? 0.519   -9.541  12.766  1.00 13.15 ? 32  PRO A CA  1 
ATOM   2350 C  C   . PRO B 1 32  ? 1.783   -10.380 12.495  1.00 12.79 ? 32  PRO A C   1 
ATOM   2351 O  O   . PRO B 1 32  ? 2.915   -9.881  12.606  1.00 12.34 ? 32  PRO A O   1 
ATOM   2352 C  CB  . PRO B 1 32  ? -0.389  -9.427  11.507  1.00 12.62 ? 32  PRO A CB  1 
ATOM   2353 C  CG  . PRO B 1 32  ? 0.427   -8.372  10.624  1.00 14.44 ? 32  PRO A CG  1 
ATOM   2354 C  CD  . PRO B 1 32  ? 0.830   -7.313  11.748  1.00 13.09 ? 32  PRO A CD  1 
ATOM   2355 N  N   . ILE B 1 33  ? 1.595   -11.618 12.085  1.00 13.70 ? 33  ILE A N   1 
ATOM   2356 C  CA  . ILE B 1 33  ? 2.711   -12.558 11.896  1.00 14.30 ? 33  ILE A CA  1 
ATOM   2357 C  C   . ILE B 1 33  ? 2.446   -13.441 10.685  1.00 15.42 ? 33  ILE A C   1 
ATOM   2358 O  O   . ILE B 1 33  ? 1.304   -13.546 10.215  1.00 14.96 ? 33  ILE A O   1 
ATOM   2359 C  CB  . ILE B 1 33  ? 2.900   -13.508 13.161  1.00 14.95 ? 33  ILE A CB  1 
ATOM   2360 C  CG1 . ILE B 1 33  ? 1.620   -14.370 13.424  1.00 10.60 ? 33  ILE A CG1 1 
ATOM   2361 C  CG2 . ILE B 1 33  ? 3.329   -12.670 14.457  1.00 14.97 ? 33  ILE A CG2 1 
ATOM   2362 C  CD1 . ILE B 1 33  ? 1.883   -15.488 14.446  1.00 15.81 ? 33  ILE A CD1 1 
ATOM   2363 N  N   . GLU B 1 34  ? 3.492   -14.114 10.211  1.00 14.81 ? 34  GLU A N   1 
ATOM   2364 C  CA  . GLU B 1 34  ? 3.366   -15.215 9.322   1.00 14.94 ? 34  GLU A CA  1 
ATOM   2365 C  C   . GLU B 1 34  ? 2.946   -16.409 10.212  1.00 14.74 ? 34  GLU A C   1 
ATOM   2366 O  O   . GLU B 1 34  ? 3.569   -16.691 11.254  1.00 15.05 ? 34  GLU A O   1 
ATOM   2367 C  CB  . GLU B 1 34  ? 4.666   -15.662 8.677   1.00 15.18 ? 34  GLU A CB  1 
ATOM   2368 C  CG  . GLU B 1 34  ? 4.872   -14.941 7.398   1.00 20.94 ? 34  GLU A CG  1 
ATOM   2369 C  CD  . GLU B 1 34  ? 4.185   -15.513 6.165   1.00 18.25 ? 34  GLU A CD  1 
ATOM   2370 O  OE1 . GLU B 1 34  ? 3.583   -16.610 6.159   1.00 18.41 ? 34  GLU A OE1 1 
ATOM   2371 O  OE2 . GLU B 1 34  ? 4.282   -14.795 5.171   1.00 26.46 ? 34  GLU A OE2 1 
ATOM   2372 N  N   . ILE B 1 35  ? 1.899   -17.080 9.756   1.00 14.52 ? 35  ILE A N   1 
ATOM   2373 C  CA  . ILE B 1 35  ? 1.503   -18.369 10.309  1.00 15.65 ? 35  ILE A CA  1 
ATOM   2374 C  C   . ILE B 1 35  ? 2.047   -19.460 9.405   1.00 16.12 ? 35  ILE A C   1 
ATOM   2375 O  O   . ILE B 1 35  ? 1.616   -19.618 8.225   1.00 15.35 ? 35  ILE A O   1 
ATOM   2376 C  CB  . ILE B 1 35  ? -0.032  -18.439 10.457  1.00 14.48 ? 35  ILE A CB  1 
ATOM   2377 C  CG1 . ILE B 1 35  ? -0.536  -17.253 11.369  1.00 15.26 ? 35  ILE A CG1 1 
ATOM   2378 C  CG2 . ILE B 1 35  ? -0.441  -19.903 10.938  1.00 17.08 ? 35  ILE A CG2 1 
ATOM   2379 C  CD1 . ILE B 1 35  ? -2.109  -17.192 11.479  1.00 16.06 ? 35  ILE A CD1 1 
ATOM   2380 N  N   . LYS B 1 36  ? 3.034   -20.204 9.921   1.00 17.74 ? 36  LYS A N   1 
ATOM   2381 C  CA  . LYS B 1 36  ? 3.639   -21.302 9.129   1.00 18.82 ? 36  LYS A CA  1 
ATOM   2382 C  C   . LYS B 1 36  ? 3.052   -22.594 9.689   1.00 19.54 ? 36  LYS A C   1 
ATOM   2383 O  O   . LYS B 1 36  ? 3.391   -22.988 10.825  1.00 20.20 ? 36  LYS A O   1 
ATOM   2384 C  CB  . LYS B 1 36  ? 5.186   -21.339 9.253   1.00 17.66 ? 36  LYS A CB  1 
ATOM   2385 C  CG  . LYS B 1 36  ? 6.000   -20.097 8.883   1.00 16.52 ? 36  LYS A CG  1 
ATOM   2386 C  CD  . LYS B 1 36  ? 7.497   -20.414 8.952   1.00 19.02 ? 36  LYS A CD  1 
ATOM   2387 C  CE  . LYS B 1 36  ? 8.264   -19.188 8.621   1.00 24.75 ? 36  LYS A CE  1 
ATOM   2388 N  NZ  . LYS B 1 36  ? 9.776   -19.197 8.912   1.00 22.57 ? 36  LYS A NZ  1 
ATOM   2389 N  N   . THR B 1 37  ? 2.176   -23.230 8.922   1.00 20.26 ? 37  THR A N   1 
ATOM   2390 C  CA  . THR B 1 37  ? 1.348   -24.309 9.439   1.00 21.60 ? 37  THR A CA  1 
ATOM   2391 C  C   . THR B 1 37  ? 2.132   -25.571 9.890   1.00 23.41 ? 37  THR A C   1 
ATOM   2392 O  O   . THR B 1 37  ? 1.692   -26.296 10.777  1.00 24.01 ? 37  THR A O   1 
ATOM   2393 C  CB  . THR B 1 37  ? 0.219   -24.673 8.468   1.00 21.52 ? 37  THR A CB  1 
ATOM   2394 O  OG1 . THR B 1 37  ? 0.741   -25.016 7.196   1.00 23.28 ? 37  THR A OG1 1 
ATOM   2395 C  CG2 . THR B 1 37  ? -0.682  -23.527 8.305   1.00 21.84 ? 37  THR A CG2 1 
ATOM   2396 N  N   . LYS B 1 38  ? 3.330   -25.778 9.341   1.00 23.57 ? 38  LYS A N   1 
ATOM   2397 C  CA  . LYS B 1 38  ? 4.142   -26.883 9.747   1.00 24.83 ? 38  LYS A CA  1 
ATOM   2398 C  C   . LYS B 1 38  ? 4.773   -26.621 11.077  1.00 24.33 ? 38  LYS A C   1 
ATOM   2399 O  O   . LYS B 1 38  ? 5.203   -27.584 11.716  1.00 25.37 ? 38  LYS A O   1 
ATOM   2400 C  CB  . LYS B 1 38  ? 5.187   -27.231 8.673   1.00 27.02 ? 38  LYS A CB  1 
ATOM   2401 C  CG  . LYS B 1 38  ? 4.964   -28.568 7.941   1.00 31.15 ? 38  LYS A CG  1 
ATOM   2402 C  CD  . LYS B 1 38  ? 5.510   -29.755 8.801   1.00 36.35 ? 38  LYS A CD  1 
ATOM   2403 C  CE  . LYS B 1 38  ? 4.902   -31.174 8.448   1.00 38.74 ? 38  LYS A CE  1 
ATOM   2404 N  NZ  . LYS B 1 38  ? 5.088   -31.587 7.018   1.00 44.73 ? 38  LYS A NZ  1 
ATOM   2405 N  N   . GLU B 1 39  ? 4.843   -25.345 11.509  1.00 21.50 ? 39  GLU A N   1 
ATOM   2406 C  CA  . GLU B 1 39  ? 5.436   -24.991 12.777  1.00 21.86 ? 39  GLU A CA  1 
ATOM   2407 C  C   . GLU B 1 39  ? 4.440   -24.808 13.923  1.00 20.99 ? 39  GLU A C   1 
ATOM   2408 O  O   . GLU B 1 39  ? 4.838   -24.514 15.034  1.00 20.91 ? 39  GLU A O   1 
ATOM   2409 C  CB  . GLU B 1 39  ? 6.151   -23.625 12.675  1.00 21.56 ? 39  GLU A CB  1 
ATOM   2410 C  CG  . GLU B 1 39  ? 7.186   -23.494 11.505  1.00 27.97 ? 39  GLU A CG  1 
ATOM   2411 C  CD  . GLU B 1 39  ? 8.064   -24.695 11.396  1.00 33.00 ? 39  GLU A CD  1 
ATOM   2412 O  OE1 . GLU B 1 39  ? 8.630   -25.101 12.448  1.00 35.09 ? 39  GLU A OE1 1 
ATOM   2413 O  OE2 . GLU B 1 39  ? 8.122   -25.267 10.288  1.00 33.77 ? 39  GLU A OE2 1 
ATOM   2414 N  N   . VAL B 1 40  ? 3.151   -24.854 13.599  1.00 21.35 ? 40  VAL A N   1 
ATOM   2415 C  CA  . VAL B 1 40  ? 2.097   -24.542 14.511  1.00 21.65 ? 40  VAL A CA  1 
ATOM   2416 C  C   . VAL B 1 40  ? 1.949   -25.769 15.361  1.00 22.44 ? 40  VAL A C   1 
ATOM   2417 O  O   . VAL B 1 40  ? 2.100   -26.877 14.868  1.00 24.07 ? 40  VAL A O   1 
ATOM   2418 C  CB  . VAL B 1 40  ? 0.852   -24.233 13.701  1.00 21.82 ? 40  VAL A CB  1 
ATOM   2419 C  CG1 . VAL B 1 40  ? -0.378  -24.440 14.502  1.00 25.25 ? 40  VAL A CG1 1 
ATOM   2420 C  CG2 . VAL B 1 40  ? 0.929   -22.769 13.148  1.00 20.58 ? 40  VAL A CG2 1 
ATOM   2421 N  N   . LYS B 1 41  ? 1.722   -25.603 16.653  1.00 22.68 ? 41  LYS A N   1 
ATOM   2422 C  CA  . LYS B 1 41  ? 1.464   -26.765 17.515  1.00 22.31 ? 41  LYS A CA  1 
ATOM   2423 C  C   . LYS B 1 41  ? -0.036  -26.990 17.825  1.00 22.06 ? 41  LYS A C   1 
ATOM   2424 O  O   . LYS B 1 41  ? -0.674  -26.147 18.456  1.00 20.49 ? 41  LYS A O   1 
ATOM   2425 C  CB  . LYS B 1 41  ? 2.260   -26.589 18.824  1.00 22.40 ? 41  LYS A CB  1 
ATOM   2426 C  CG  . LYS B 1 41  ? 3.803   -26.904 18.683  1.00 26.41 ? 41  LYS A CG  1 
ATOM   2427 C  CD  . LYS B 1 41  ? 4.703   -25.682 18.370  1.00 30.90 ? 41  LYS A CD  1 
ATOM   2428 C  CE  . LYS B 1 41  ? 6.142   -26.106 18.130  0.01 27.06 ? 41  LYS A CE  1 
ATOM   2429 N  NZ  . LYS B 1 41  ? 6.996   -24.957 17.723  0.01 28.20 ? 41  LYS A NZ  1 
ATOM   2430 N  N   . TYR B 1 42  ? -0.589  -28.132 17.389  1.00 21.04 ? 42  TYR A N   1 
ATOM   2431 C  CA  . TYR B 1 42  ? -1.908  -28.534 17.838  1.00 21.71 ? 42  TYR A CA  1 
ATOM   2432 C  C   . TYR B 1 42  ? -1.925  -28.581 19.373  1.00 20.57 ? 42  TYR A C   1 
ATOM   2433 O  O   . TYR B 1 42  ? -1.055  -29.173 19.956  1.00 20.77 ? 42  TYR A O   1 
ATOM   2434 C  CB  . TYR B 1 42  ? -2.299  -29.893 17.253  1.00 23.28 ? 42  TYR A CB  1 
ATOM   2435 C  CG  . TYR B 1 42  ? -3.574  -30.408 17.865  1.00 24.60 ? 42  TYR A CG  1 
ATOM   2436 C  CD1 . TYR B 1 42  ? -4.775  -29.688 17.715  1.00 23.41 ? 42  TYR A CD1 1 
ATOM   2437 C  CD2 . TYR B 1 42  ? -3.575  -31.596 18.624  1.00 26.61 ? 42  TYR A CD2 1 
ATOM   2438 C  CE1 . TYR B 1 42  ? -5.992  -30.163 18.272  1.00 24.23 ? 42  TYR A CE1 1 
ATOM   2439 C  CE2 . TYR B 1 42  ? -4.762  -32.091 19.197  1.00 23.80 ? 42  TYR A CE2 1 
ATOM   2440 C  CZ  . TYR B 1 42  ? -5.950  -31.369 19.013  1.00 25.60 ? 42  TYR A CZ  1 
ATOM   2441 O  OH  . TYR B 1 42  ? -7.099  -31.838 19.597  1.00 26.56 ? 42  TYR A OH  1 
ATOM   2442 N  N   . ASP B 1 43  ? -2.859  -27.888 20.022  1.00 19.34 ? 43  ASP A N   1 
ATOM   2443 C  CA  . ASP B 1 43  ? -2.917  -27.918 21.466  1.00 19.44 ? 43  ASP A CA  1 
ATOM   2444 C  C   . ASP B 1 43  ? -4.310  -28.409 21.814  1.00 20.39 ? 43  ASP A C   1 
ATOM   2445 O  O   . ASP B 1 43  ? -5.326  -27.676 21.543  1.00 20.53 ? 43  ASP A O   1 
ATOM   2446 C  CB  . ASP B 1 43  ? -2.565  -26.542 22.052  1.00 19.25 ? 43  ASP A CB  1 
ATOM   2447 C  CG  . ASP B 1 43  ? -2.585  -26.517 23.605  1.00 21.03 ? 43  ASP A CG  1 
ATOM   2448 O  OD1 . ASP B 1 43  ? -3.171  -27.427 24.241  1.00 20.29 ? 43  ASP A OD1 1 
ATOM   2449 O  OD2 . ASP B 1 43  ? -2.035  -25.553 24.177  1.00 24.96 ? 43  ASP A OD2 1 
ATOM   2450 N  N   . SER B 1 44  ? -4.396  -29.662 22.306  1.00 19.82 ? 44  SER A N   1 
ATOM   2451 C  CA  . SER B 1 44  ? -5.718  -30.259 22.690  1.00 22.82 ? 44  SER A CA  1 
ATOM   2452 C  C   . SER B 1 44  ? -6.455  -29.595 23.863  1.00 21.76 ? 44  SER A C   1 
ATOM   2453 O  O   . SER B 1 44  ? -7.666  -29.809 24.021  1.00 22.44 ? 44  SER A O   1 
ATOM   2454 C  CB  . SER B 1 44  ? -5.685  -31.828 22.845  1.00 23.43 ? 44  SER A CB  1 
ATOM   2455 O  OG  . SER B 1 44  ? -4.743  -32.207 23.823  1.00 25.19 ? 44  SER A OG  1 
ATOM   2456 N  N   . SER B 1 45  ? -5.752  -28.764 24.637  1.00 21.84 ? 45  SER A N   1 
ATOM   2457 C  CA  . SER B 1 45  ? -6.380  -27.989 25.693  1.00 23.54 ? 45  SER A CA  1 
ATOM   2458 C  C   . SER B 1 45  ? -7.169  -26.752 25.149  1.00 22.79 ? 45  SER A C   1 
ATOM   2459 O  O   . SER B 1 45  ? -7.966  -26.117 25.883  1.00 21.55 ? 45  SER A O   1 
ATOM   2460 C  CB  . SER B 1 45  ? -5.359  -27.569 26.755  1.00 23.65 ? 45  SER A CB  1 
ATOM   2461 O  OG  . SER B 1 45  ? -4.411  -26.594 26.249  1.00 28.78 ? 45  SER A OG  1 
ATOM   2462 N  N   . LEU B 1 46  ? -6.948  -26.410 23.875  1.00 21.63 ? 46  LEU A N   1 
ATOM   2463 C  CA  . LEU B 1 46  ? -7.666  -25.253 23.319  1.00 19.99 ? 46  LEU A CA  1 
ATOM   2464 C  C   . LEU B 1 46  ? -9.147  -25.617 23.198  1.00 19.50 ? 46  LEU A C   1 
ATOM   2465 O  O   . LEU B 1 46  ? -9.507  -26.748 22.847  1.00 21.06 ? 46  LEU A O   1 
ATOM   2466 C  CB  . LEU B 1 46  ? -7.105  -24.860 21.939  1.00 18.60 ? 46  LEU A CB  1 
ATOM   2467 C  CG  . LEU B 1 46  ? -5.815  -24.074 21.999  1.00 15.96 ? 46  LEU A CG  1 
ATOM   2468 C  CD1 . LEU B 1 46  ? -5.279  -23.748 20.547  1.00 16.01 ? 46  LEU A CD1 1 
ATOM   2469 C  CD2 . LEU B 1 46  ? -5.976  -22.801 22.814  1.00 12.66 ? 46  LEU A CD2 1 
ATOM   2470 N  N   . ARG B 1 47  ? -9.998  -24.659 23.500  1.00 18.24 ? 47  ARG A N   1 
ATOM   2471 C  CA  . ARG B 1 47  ? -11.432 -24.859 23.449  1.00 18.40 ? 47  ARG A CA  1 
ATOM   2472 C  C   . ARG B 1 47  ? -12.017 -24.405 22.143  1.00 17.82 ? 47  ARG A C   1 
ATOM   2473 O  O   . ARG B 1 47  ? -11.450 -23.526 21.580  1.00 17.87 ? 47  ARG A O   1 
ATOM   2474 C  CB  . ARG B 1 47  ? -12.078 -24.273 24.707  1.00 17.02 ? 47  ARG A CB  1 
ATOM   2475 C  CG  . ARG B 1 47  ? -11.979 -25.359 25.800  1.00 19.03 ? 47  ARG A CG  1 
ATOM   2476 C  CD  . ARG B 1 47  ? -11.620 -25.145 27.250  1.00 24.62 ? 47  ARG A CD  1 
ATOM   2477 N  NE  . ARG B 1 47  ? -12.438 -24.190 27.991  1.00 29.68 ? 47  ARG A NE  1 
ATOM   2478 C  CZ  . ARG B 1 47  ? -12.605 -24.239 29.311  1.00 28.10 ? 47  ARG A CZ  1 
ATOM   2479 N  NH1 . ARG B 1 47  ? -12.024 -25.203 30.016  1.00 26.02 ? 47  ARG A NH1 1 
ATOM   2480 N  NH2 . ARG B 1 47  ? -13.353 -23.335 29.928  1.00 30.67 ? 47  ARG A NH2 1 
ATOM   2481 N  N   . PRO B 1 48  ? -13.168 -24.997 21.685  1.00 17.02 ? 48  PRO A N   1 
ATOM   2482 C  CA  . PRO B 1 48  ? -13.906 -24.307 20.586  1.00 17.26 ? 48  PRO A CA  1 
ATOM   2483 C  C   . PRO B 1 48  ? -14.344 -22.891 20.984  1.00 15.33 ? 48  PRO A C   1 
ATOM   2484 O  O   . PRO B 1 48  ? -14.493 -22.614 22.139  1.00 14.60 ? 48  PRO A O   1 
ATOM   2485 C  CB  . PRO B 1 48  ? -15.154 -25.188 20.397  1.00 16.54 ? 48  PRO A CB  1 
ATOM   2486 C  CG  . PRO B 1 48  ? -14.708 -26.571 20.771  1.00 17.13 ? 48  PRO A CG  1 
ATOM   2487 C  CD  . PRO B 1 48  ? -13.897 -26.219 22.075  1.00 17.55 ? 48  PRO A CD  1 
ATOM   2488 N  N   . LEU B 1 49  ? -14.528 -22.001 20.007  1.00 15.07 ? 49  LEU A N   1 
ATOM   2489 C  CA  . LEU B 1 49  ? -14.915 -20.621 20.361  1.00 15.16 ? 49  LEU A CA  1 
ATOM   2490 C  C   . LEU B 1 49  ? -16.404 -20.677 20.795  1.00 15.39 ? 49  LEU A C   1 
ATOM   2491 O  O   . LEU B 1 49  ? -17.202 -21.341 20.126  1.00 15.72 ? 49  LEU A O   1 
ATOM   2492 C  CB  . LEU B 1 49  ? -14.784 -19.677 19.141  1.00 12.79 ? 49  LEU A CB  1 
ATOM   2493 C  CG  . LEU B 1 49  ? -13.323 -19.634 18.641  1.00 12.10 ? 49  LEU A CG  1 
ATOM   2494 C  CD1 . LEU B 1 49  ? -13.180 -18.776 17.382  1.00 14.96 ? 49  LEU A CD1 1 
ATOM   2495 C  CD2 . LEU B 1 49  ? -12.471 -19.096 19.780  1.00 10.81 ? 49  LEU A CD2 1 
ATOM   2496 N  N   . SER B 1 50  ? -16.700 -19.959 21.868  1.00 13.14 ? 50  SER A N   1 
ATOM   2497 C  CA  . SER B 1 50  ? -18.052 -19.719 22.364  1.00 13.61 ? 50  SER A CA  1 
ATOM   2498 C  C   . SER B 1 50  ? -18.438 -18.262 22.035  1.00 13.74 ? 50  SER A C   1 
ATOM   2499 O  O   . SER B 1 50  ? -17.847 -17.328 22.561  1.00 11.96 ? 50  SER A O   1 
ATOM   2500 C  CB  . SER B 1 50  ? -18.145 -19.985 23.873  1.00 12.78 ? 50  SER A CB  1 
ATOM   2501 O  OG  . SER B 1 50  ? -19.388 -19.540 24.383  1.00 15.40 ? 50  SER A OG  1 
ATOM   2502 N  N   . ILE B 1 51  ? -19.390 -18.104 21.104  1.00 12.75 ? 51  ILE A N   1 
ATOM   2503 C  CA  . ILE B 1 51  ? -19.553 -16.799 20.479  1.00 14.08 ? 51  ILE A CA  1 
ATOM   2504 C  C   . ILE B 1 51  ? -20.967 -16.346 20.634  1.00 13.67 ? 51  ILE A C   1 
ATOM   2505 O  O   . ILE B 1 51  ? -21.889 -17.027 20.196  1.00 13.73 ? 51  ILE A O   1 
ATOM   2506 C  CB  . ILE B 1 51  ? -19.128 -16.803 18.945  1.00 12.26 ? 51  ILE A CB  1 
ATOM   2507 C  CG1 . ILE B 1 51  ? -17.720 -17.426 18.745  1.00 14.40 ? 51  ILE A CG1 1 
ATOM   2508 C  CG2 . ILE B 1 51  ? -19.137 -15.372 18.414  1.00 12.55 ? 51  ILE A CG2 1 
ATOM   2509 C  CD1 . ILE B 1 51  ? -17.093 -17.148 17.378  1.00 16.22 ? 51  ILE A CD1 1 
ATOM   2510 N  N   . LYS B 1 52  ? -21.142 -15.174 21.210  1.00 13.80 ? 52  LYS A N   1 
ATOM   2511 C  CA  . LYS B 1 52  ? -22.461 -14.607 21.378  1.00 14.05 ? 52  LYS A CA  1 
ATOM   2512 C  C   . LYS B 1 52  ? -22.428 -13.161 20.939  1.00 13.02 ? 52  LYS A C   1 
ATOM   2513 O  O   . LYS B 1 52  ? -21.838 -12.354 21.590  1.00 14.14 ? 52  LYS A O   1 
ATOM   2514 C  CB  . LYS B 1 52  ? -22.933 -14.728 22.831  1.00 14.01 ? 52  LYS A CB  1 
ATOM   2515 C  CG  . LYS B 1 52  ? -24.458 -14.374 22.980  1.00 14.58 ? 52  LYS A CG  1 
ATOM   2516 C  CD  . LYS B 1 52  ? -24.809 -14.119 24.455  1.00 15.89 ? 52  LYS A CD  1 
ATOM   2517 C  CE  . LYS B 1 52  ? -26.246 -13.650 24.492  1.00 22.35 ? 52  LYS A CE  1 
ATOM   2518 N  NZ  . LYS B 1 52  ? -26.529 -12.452 23.750  1.00 18.08 ? 52  LYS A NZ  1 
ATOM   2519 N  N   . TYR B 1 53  ? -23.079 -12.832 19.834  1.00 14.17 ? 53  TYR A N   1 
ATOM   2520 C  CA  . TYR B 1 53  ? -23.042 -11.459 19.277  1.00 14.31 ? 53  TYR A CA  1 
ATOM   2521 C  C   . TYR B 1 53  ? -24.489 -11.052 18.946  1.00 14.54 ? 53  TYR A C   1 
ATOM   2522 O  O   . TYR B 1 53  ? -25.156 -11.702 18.096  1.00 14.99 ? 53  TYR A O   1 
ATOM   2523 C  CB  . TYR B 1 53  ? -22.187 -11.348 17.962  1.00 12.58 ? 53  TYR A CB  1 
ATOM   2524 C  CG  . TYR B 1 53  ? -20.704 -11.583 18.067  1.00 12.03 ? 53  TYR A CG  1 
ATOM   2525 C  CD1 . TYR B 1 53  ? -19.981 -11.259 19.237  1.00 14.82 ? 53  TYR A CD1 1 
ATOM   2526 C  CD2 . TYR B 1 53  ? -20.003 -12.172 16.991  1.00 13.04 ? 53  TYR A CD2 1 
ATOM   2527 C  CE1 . TYR B 1 53  ? -18.608 -11.483 19.298  1.00 9.65  ? 53  TYR A CE1 1 
ATOM   2528 C  CE2 . TYR B 1 53  ? -18.618 -12.350 17.045  1.00 11.11 ? 53  TYR A CE2 1 
ATOM   2529 C  CZ  . TYR B 1 53  ? -17.946 -12.020 18.209  1.00 9.67  ? 53  TYR A CZ  1 
ATOM   2530 O  OH  . TYR B 1 53  ? -16.588 -12.248 18.308  1.00 11.96 ? 53  TYR A OH  1 
ATOM   2531 N  N   . ASP B 1 54  ? -24.952 -10.024 19.662  1.00 14.47 ? 54  ASP A N   1 
ATOM   2532 C  CA  . ASP B 1 54  ? -26.323 -9.516  19.610  1.00 16.71 ? 54  ASP A CA  1 
ATOM   2533 C  C   . ASP B 1 54  ? -26.291 -8.474  18.471  1.00 16.94 ? 54  ASP A C   1 
ATOM   2534 O  O   . ASP B 1 54  ? -25.636 -7.463  18.593  1.00 16.24 ? 54  ASP A O   1 
ATOM   2535 C  CB  . ASP B 1 54  ? -26.602 -8.820  20.952  1.00 16.98 ? 54  ASP A CB  1 
ATOM   2536 C  CG  . ASP B 1 54  ? -28.043 -8.399  21.120  1.00 21.28 ? 54  ASP A CG  1 
ATOM   2537 O  OD1 . ASP B 1 54  ? -28.669 -7.971  20.127  1.00 21.76 ? 54  ASP A OD1 1 
ATOM   2538 O  OD2 . ASP B 1 54  ? -28.501 -8.474  22.264  1.00 24.07 ? 54  ASP A OD2 1 
ATOM   2539 N  N   . PRO B 1 55  ? -26.970 -8.740  17.353  1.00 17.74 ? 55  PRO A N   1 
ATOM   2540 C  CA  . PRO B 1 55  ? -27.034 -7.760  16.263  1.00 18.42 ? 55  PRO A CA  1 
ATOM   2541 C  C   . PRO B 1 55  ? -27.422 -6.315  16.697  1.00 18.75 ? 55  PRO A C   1 
ATOM   2542 O  O   . PRO B 1 55  ? -27.121 -5.360  15.950  1.00 19.77 ? 55  PRO A O   1 
ATOM   2543 C  CB  . PRO B 1 55  ? -28.142 -8.322  15.366  1.00 18.08 ? 55  PRO A CB  1 
ATOM   2544 C  CG  . PRO B 1 55  ? -27.992 -9.782  15.564  1.00 21.23 ? 55  PRO A CG  1 
ATOM   2545 C  CD  . PRO B 1 55  ? -27.783 -9.927  17.063  1.00 17.63 ? 55  PRO A CD  1 
ATOM   2546 N  N   . SER B 1 56  ? -28.082 -6.158  17.847  1.00 19.79 ? 56  SER A N   1 
ATOM   2547 C  CA  . SER B 1 56  ? -28.592 -4.854  18.290  1.00 21.40 ? 56  SER A CA  1 
ATOM   2548 C  C   . SER B 1 56  ? -27.463 -4.067  18.997  1.00 20.31 ? 56  SER A C   1 
ATOM   2549 O  O   . SER B 1 56  ? -27.558 -2.840  19.235  1.00 20.14 ? 56  SER A O   1 
ATOM   2550 C  CB  . SER B 1 56  ? -29.824 -5.050  19.184  1.00 22.34 ? 56  SER A CB  1 
ATOM   2551 O  OG  . SER B 1 56  ? -29.449 -5.260  20.557  1.00 29.98 ? 56  SER A OG  1 
ATOM   2552 N  N   . SER B 1 57  ? -26.366 -4.778  19.290  1.00 18.92 ? 57  SER A N   1 
ATOM   2553 C  CA  . SER B 1 57  ? -25.171 -4.201  19.941  1.00 18.23 ? 57  SER A CA  1 
ATOM   2554 C  C   . SER B 1 57  ? -24.470 -3.143  19.055  1.00 17.51 ? 57  SER A C   1 
ATOM   2555 O  O   . SER B 1 57  ? -23.923 -2.183  19.574  1.00 17.09 ? 57  SER A O   1 
ATOM   2556 C  CB  . SER B 1 57  ? -24.105 -5.311  20.246  1.00 17.47 ? 57  SER A CB  1 
ATOM   2557 O  OG  . SER B 1 57  ? -24.460 -6.124  21.339  1.00 21.45 ? 57  SER A OG  1 
ATOM   2558 N  N   . ALA B 1 58  ? -24.396 -3.386  17.746  1.00 16.49 ? 58  ALA A N   1 
ATOM   2559 C  CA  . ALA B 1 58  ? -23.764 -2.428  16.839  1.00 15.96 ? 58  ALA A CA  1 
ATOM   2560 C  C   . ALA B 1 58  ? -24.516 -1.098  16.867  1.00 17.37 ? 58  ALA A C   1 
ATOM   2561 O  O   . ALA B 1 58  ? -25.742 -1.091  16.791  1.00 16.34 ? 58  ALA A O   1 
ATOM   2562 C  CB  . ALA B 1 58  ? -23.711 -2.986  15.445  1.00 16.71 ? 58  ALA A CB  1 
ATOM   2563 N  N   . LYS B 1 59  ? -23.792 0.025   17.022  1.00 15.78 ? 59  LYS A N   1 
ATOM   2564 C  CA  . LYS B 1 59  ? -24.480 1.314   17.106  1.00 16.63 ? 59  LYS A CA  1 
ATOM   2565 C  C   . LYS B 1 59  ? -24.126 2.345   15.972  1.00 18.18 ? 59  LYS A C   1 
ATOM   2566 O  O   . LYS B 1 59  ? -25.001 3.036   15.432  1.00 17.08 ? 59  LYS A O   1 
ATOM   2567 C  CB  . LYS B 1 59  ? -24.224 1.948   18.485  1.00 14.22 ? 59  LYS A CB  1 
ATOM   2568 C  CG  . LYS B 1 59  ? -24.817 1.080   19.637  1.00 11.97 ? 59  LYS A CG  1 
ATOM   2569 C  CD  . LYS B 1 59  ? -26.352 0.915   19.567  1.00 13.69 ? 59  LYS A CD  1 
ATOM   2570 C  CE  . LYS B 1 59  ? -26.829 0.075   20.745  1.00 14.91 ? 59  LYS A CE  1 
ATOM   2571 N  NZ  . LYS B 1 59  ? -28.140 -0.594  20.538  1.00 17.20 ? 59  LYS A NZ  1 
ATOM   2572 N  N   . ILE B 1 60  ? -22.822 2.432   15.687  1.00 19.45 ? 60  ILE A N   1 
ATOM   2573 C  CA  . ILE B 1 60  ? -22.242 3.501   14.889  1.00 21.73 ? 60  ILE A CA  1 
ATOM   2574 C  C   . ILE B 1 60  ? -21.200 2.892   13.977  1.00 19.13 ? 60  ILE A C   1 
ATOM   2575 O  O   . ILE B 1 60  ? -20.498 1.976   14.378  1.00 19.34 ? 60  ILE A O   1 
ATOM   2576 C  CB  . ILE B 1 60  ? -21.593 4.541   15.875  1.00 21.39 ? 60  ILE A CB  1 
ATOM   2577 C  CG1 . ILE B 1 60  ? -22.731 5.334   16.576  1.00 26.64 ? 60  ILE A CG1 1 
ATOM   2578 C  CG2 . ILE B 1 60  ? -20.701 5.539   15.162  1.00 23.70 ? 60  ILE A CG2 1 
ATOM   2579 C  CD1 . ILE B 1 60  ? -22.371 6.006   17.947  1.00 24.83 ? 60  ILE A CD1 1 
ATOM   2580 N  N   . ILE B 1 61  ? -21.093 3.432   12.776  1.00 18.25 ? 61  ILE A N   1 
ATOM   2581 C  CA  . ILE B 1 61  ? -19.904 3.204   11.922  1.00 17.08 ? 61  ILE A CA  1 
ATOM   2582 C  C   . ILE B 1 61  ? -19.175 4.536   11.620  1.00 17.33 ? 61  ILE A C   1 
ATOM   2583 O  O   . ILE B 1 61  ? -19.817 5.542   11.309  1.00 18.96 ? 61  ILE A O   1 
ATOM   2584 C  CB  . ILE B 1 61  ? -20.254 2.447   10.618  1.00 17.64 ? 61  ILE A CB  1 
ATOM   2585 C  CG1 . ILE B 1 61  ? -18.962 1.954   9.899   1.00 12.63 ? 61  ILE A CG1 1 
ATOM   2586 C  CG2 . ILE B 1 61  ? -21.197 3.272   9.695   1.00 17.95 ? 61  ILE A CG2 1 
ATOM   2587 C  CD1 . ILE B 1 61  ? -19.258 0.905   8.826   1.00 15.39 ? 61  ILE A CD1 1 
ATOM   2588 N  N   . SER B 1 62  ? -17.861 4.556   11.791  1.00 18.41 ? 62  SER A N   1 
ATOM   2589 C  CA  . SER B 1 62  ? -17.105 5.775   11.611  1.00 18.46 ? 62  SER A CA  1 
ATOM   2590 C  C   . SER B 1 62  ? -15.856 5.536   10.764  1.00 17.94 ? 62  SER A C   1 
ATOM   2591 O  O   . SER B 1 62  ? -15.308 4.413   10.689  1.00 16.89 ? 62  SER A O   1 
ATOM   2592 C  CB  . SER B 1 62  ? -16.718 6.445   12.950  1.00 18.98 ? 62  SER A CB  1 
ATOM   2593 O  OG  . SER B 1 62  ? -16.042 5.543   13.749  1.00 22.85 ? 62  SER A OG  1 
ATOM   2594 N  N   . ASN B 1 63  ? -15.413 6.612   10.124  1.00 16.76 ? 63  ASN A N   1 
ATOM   2595 C  CA  . ASN B 1 63  ? -14.104 6.602   9.517   1.00 17.29 ? 63  ASN A CA  1 
ATOM   2596 C  C   . ASN B 1 63  ? -13.077 7.107   10.516  1.00 17.04 ? 63  ASN A C   1 
ATOM   2597 O  O   . ASN B 1 63  ? -13.070 8.292   10.813  1.00 18.11 ? 63  ASN A O   1 
ATOM   2598 C  CB  . ASN B 1 63  ? -14.110 7.450   8.233   1.00 16.86 ? 63  ASN A CB  1 
ATOM   2599 C  CG  . ASN B 1 63  ? -12.808 7.410   7.511   1.00 18.82 ? 63  ASN A CG  1 
ATOM   2600 O  OD1 . ASN B 1 63  ? -11.800 6.851   8.021   1.00 17.94 ? 63  ASN A OD1 1 
ATOM   2601 N  ND2 . ASN B 1 63  ? -12.785 8.028   6.290   1.00 16.58 ? 63  ASN A ND2 1 
ATOM   2602 N  N   . SER B 1 64  ? -12.194 6.225   11.006  1.00 16.62 ? 64  SER A N   1 
ATOM   2603 C  CA  . SER B 1 64  ? -11.108 6.622   11.933  1.00 18.11 ? 64  SER A CA  1 
ATOM   2604 C  C   . SER B 1 64  ? -9.925  7.365   11.209  1.00 17.28 ? 64  SER A C   1 
ATOM   2605 O  O   . SER B 1 64  ? -9.061  7.953   11.833  1.00 17.37 ? 64  SER A O   1 
ATOM   2606 C  CB  . SER B 1 64  ? -10.573 5.407   12.696  1.00 18.61 ? 64  SER A CB  1 
ATOM   2607 O  OG  . SER B 1 64  ? -9.836  4.575   11.833  1.00 16.17 ? 64  SER A OG  1 
ATOM   2608 N  N   . GLY B 1 65  ? -9.904  7.338   9.879   1.00 15.36 ? 65  GLY A N   1 
ATOM   2609 C  CA  . GLY B 1 65  ? -8.704  7.721   9.191   1.00 15.48 ? 65  GLY A CA  1 
ATOM   2610 C  C   . GLY B 1 65  ? -7.867  6.516   8.844   1.00 13.43 ? 65  GLY A C   1 
ATOM   2611 O  O   . GLY B 1 65  ? -7.085  6.572   7.911   1.00 14.90 ? 65  GLY A O   1 
ATOM   2612 N  N   . HIS B 1 66  ? -8.028  5.406   9.581   1.00 13.65 ? 66  HIS A N   1 
ATOM   2613 C  CA  . HIS B 1 66  ? -7.170  4.195   9.513   1.00 12.51 ? 66  HIS A CA  1 
ATOM   2614 C  C   . HIS B 1 66  ? -7.879  2.896   9.014   1.00 13.39 ? 66  HIS A C   1 
ATOM   2615 O  O   . HIS B 1 66  ? -7.198  1.901   8.662   1.00 12.69 ? 66  HIS A O   1 
ATOM   2616 C  CB  . HIS B 1 66  ? -6.587  3.933   10.899  1.00 12.58 ? 66  HIS A CB  1 
ATOM   2617 C  CG  . HIS B 1 66  ? -5.994  5.156   11.520  1.00 18.53 ? 66  HIS A CG  1 
ATOM   2618 N  ND1 . HIS B 1 66  ? -4.962  5.850   10.921  1.00 18.58 ? 66  HIS A ND1 1 
ATOM   2619 C  CD2 . HIS B 1 66  ? -6.353  5.876   12.608  1.00 16.81 ? 66  HIS A CD2 1 
ATOM   2620 C  CE1 . HIS B 1 66  ? -4.695  6.929   11.632  1.00 18.91 ? 66  HIS A CE1 1 
ATOM   2621 N  NE2 . HIS B 1 66  ? -5.488  6.942   12.684  1.00 18.30 ? 66  HIS A NE2 1 
ATOM   2622 N  N   . SER B 1 67  ? -9.222  2.956   9.070   1.00 14.67 ? 67  SER A N   1 
ATOM   2623 C  CA  . SER B 1 67  ? -10.206 1.944   8.676   1.00 14.82 ? 67  SER A CA  1 
ATOM   2624 C  C   . SER B 1 67  ? -11.585 2.533   8.885   1.00 16.40 ? 67  SER A C   1 
ATOM   2625 O  O   . SER B 1 67  ? -11.706 3.718   9.305   1.00 15.68 ? 67  SER A O   1 
ATOM   2626 C  CB  . SER B 1 67  ? -10.078 0.647   9.521   1.00 15.06 ? 67  SER A CB  1 
ATOM   2627 O  OG  . SER B 1 67  ? -10.764 -0.396  8.846   1.00 12.91 ? 67  SER A OG  1 
ATOM   2628 N  N   . PHE B 1 68  ? -12.646 1.743   8.608   1.00 15.15 ? 68  PHE A N   1 
ATOM   2629 C  CA  . PHE B 1 68  ? -13.935 2.027   9.284   1.00 15.17 ? 68  PHE A CA  1 
ATOM   2630 C  C   . PHE B 1 68  ? -13.915 1.343   10.672  1.00 15.17 ? 68  PHE A C   1 
ATOM   2631 O  O   . PHE B 1 68  ? -13.298 0.302   10.799  1.00 14.22 ? 68  PHE A O   1 
ATOM   2632 C  CB  . PHE B 1 68  ? -15.146 1.512   8.469   1.00 15.30 ? 68  PHE A CB  1 
ATOM   2633 C  CG  . PHE B 1 68  ? -15.263 -0.018  8.405   1.00 17.42 ? 68  PHE A CG  1 
ATOM   2634 C  CD1 . PHE B 1 68  ? -14.705 -0.725  7.349   1.00 16.56 ? 68  PHE A CD1 1 
ATOM   2635 C  CD2 . PHE B 1 68  ? -15.895 -0.733  9.451   1.00 15.38 ? 68  PHE A CD2 1 
ATOM   2636 C  CE1 . PHE B 1 68  ? -14.788 -2.111  7.294   1.00 15.32 ? 68  PHE A CE1 1 
ATOM   2637 C  CE2 . PHE B 1 68  ? -15.951 -2.118  9.423   1.00 17.71 ? 68  PHE A CE2 1 
ATOM   2638 C  CZ  . PHE B 1 68  ? -15.408 -2.829  8.347   1.00 12.26 ? 68  PHE A CZ  1 
ATOM   2639 N  N   . ASN B 1 69  ? -14.593 1.915   11.690  1.00 14.70 ? 69  ASN A N   1 
ATOM   2640 C  CA  . ASN B 1 69  ? -14.829 1.218   12.970  1.00 15.40 ? 69  ASN A CA  1 
ATOM   2641 C  C   . ASN B 1 69  ? -16.347 1.085   13.109  1.00 15.30 ? 69  ASN A C   1 
ATOM   2642 O  O   . ASN B 1 69  ? -17.078 2.113   13.056  1.00 16.64 ? 69  ASN A O   1 
ATOM   2643 C  CB  . ASN B 1 69  ? -14.285 1.991   14.192  1.00 15.11 ? 69  ASN A CB  1 
ATOM   2644 C  CG  . ASN B 1 69  ? -12.770 2.079   14.241  1.00 16.35 ? 69  ASN A CG  1 
ATOM   2645 O  OD1 . ASN B 1 69  ? -12.209 3.017   14.823  1.00 22.39 ? 69  ASN A OD1 1 
ATOM   2646 N  ND2 . ASN B 1 69  ? -12.096 1.100   13.675  1.00 13.21 ? 69  ASN A ND2 1 
ATOM   2647 N  N   . VAL B 1 70  ? -16.834 -0.153  13.254  1.00 14.33 ? 70  VAL A N   1 
ATOM   2648 C  CA  . VAL B 1 70  ? -18.185 -0.378  13.776  1.00 14.88 ? 70  VAL A CA  1 
ATOM   2649 C  C   . VAL B 1 70  ? -18.084 -0.411  15.315  1.00 15.81 ? 70  VAL A C   1 
ATOM   2650 O  O   . VAL B 1 70  ? -17.444 -1.311  15.881  1.00 15.95 ? 70  VAL A O   1 
ATOM   2651 C  CB  . VAL B 1 70  ? -18.860 -1.638  13.190  1.00 16.40 ? 70  VAL A CB  1 
ATOM   2652 C  CG1 . VAL B 1 70  ? -20.280 -1.949  13.902  1.00 15.63 ? 70  VAL A CG1 1 
ATOM   2653 C  CG2 . VAL B 1 70  ? -19.020 -1.438  11.615  1.00 13.73 ? 70  VAL A CG2 1 
ATOM   2654 N  N   . ASP B 1 71  ? -18.693 0.567   16.000  1.00 15.39 ? 71  ASP A N   1 
ATOM   2655 C  CA  . ASP B 1 71  ? -18.645 0.552   17.450  1.00 16.43 ? 71  ASP A CA  1 
ATOM   2656 C  C   . ASP B 1 71  ? -19.878 -0.081  18.054  1.00 15.98 ? 71  ASP A C   1 
ATOM   2657 O  O   . ASP B 1 71  ? -20.992 0.188   17.647  1.00 14.59 ? 71  ASP A O   1 
ATOM   2658 C  CB  . ASP B 1 71  ? -18.428 1.948   18.016  1.00 16.37 ? 71  ASP A CB  1 
ATOM   2659 C  CG  . ASP B 1 71  ? -17.018 2.479   17.726  1.00 20.69 ? 71  ASP A CG  1 
ATOM   2660 O  OD1 . ASP B 1 71  ? -16.031 1.731   17.763  1.00 23.13 ? 71  ASP A OD1 1 
ATOM   2661 O  OD2 . ASP B 1 71  ? -16.882 3.672   17.472  1.00 25.14 ? 71  ASP A OD2 1 
ATOM   2662 N  N   . PHE B 1 72  ? -19.640 -0.960  19.017  1.00 16.36 ? 72  PHE A N   1 
ATOM   2663 C  CA  . PHE B 1 72  ? -20.737 -1.722  19.690  1.00 15.25 ? 72  PHE A CA  1 
ATOM   2664 C  C   . PHE B 1 72  ? -20.926 -1.115  21.062  1.00 15.34 ? 72  PHE A C   1 
ATOM   2665 O  O   . PHE B 1 72  ? -19.995 -0.630  21.693  1.00 17.21 ? 72  PHE A O   1 
ATOM   2666 C  CB  . PHE B 1 72  ? -20.447 -3.241  19.776  1.00 14.04 ? 72  PHE A CB  1 
ATOM   2667 C  CG  . PHE B 1 72  ? -20.327 -3.911  18.403  1.00 13.96 ? 72  PHE A CG  1 
ATOM   2668 C  CD1 . PHE B 1 72  ? -19.210 -3.717  17.628  1.00 17.18 ? 72  PHE A CD1 1 
ATOM   2669 C  CD2 . PHE B 1 72  ? -21.343 -4.657  17.898  1.00 15.76 ? 72  PHE A CD2 1 
ATOM   2670 C  CE1 . PHE B 1 72  ? -19.089 -4.268  16.395  1.00 21.15 ? 72  PHE A CE1 1 
ATOM   2671 C  CE2 . PHE B 1 72  ? -21.227 -5.260  16.658  1.00 18.67 ? 72  PHE A CE2 1 
ATOM   2672 C  CZ  . PHE B 1 72  ? -20.083 -5.055  15.913  1.00 16.51 ? 72  PHE A CZ  1 
ATOM   2673 N  N   . ASP B 1 73  ? -22.156 -1.158  21.533  1.00 16.19 ? 73  ASP A N   1 
ATOM   2674 C  CA  . ASP B 1 73  ? -22.428 -0.778  22.955  1.00 15.67 ? 73  ASP A CA  1 
ATOM   2675 C  C   . ASP B 1 73  ? -21.846 -1.857  23.871  1.00 15.32 ? 73  ASP A C   1 
ATOM   2676 O  O   . ASP B 1 73  ? -22.310 -2.983  23.834  1.00 16.06 ? 73  ASP A O   1 
ATOM   2677 C  CB  . ASP B 1 73  ? -23.936 -0.691  23.082  1.00 15.46 ? 73  ASP A CB  1 
ATOM   2678 C  CG  . ASP B 1 73  ? -24.371 -0.390  24.485  1.00 16.64 ? 73  ASP A CG  1 
ATOM   2679 O  OD1 . ASP B 1 73  ? -23.500 -0.036  25.319  1.00 18.94 ? 73  ASP A OD1 1 
ATOM   2680 O  OD2 . ASP B 1 73  ? -25.590 -0.459  24.715  1.00 21.75 ? 73  ASP A OD2 1 
ATOM   2681 N  N   . ASP B 1 74  ? -20.763 -1.566  24.594  1.00 15.52 ? 74  ASP A N   1 
ATOM   2682 C  CA  . ASP B 1 74  ? -20.179 -2.589  25.431  1.00 17.06 ? 74  ASP A CA  1 
ATOM   2683 C  C   . ASP B 1 74  ? -20.500 -2.170  26.866  1.00 17.64 ? 74  ASP A C   1 
ATOM   2684 O  O   . ASP B 1 74  ? -19.652 -2.329  27.724  1.00 17.75 ? 74  ASP A O   1 
ATOM   2685 C  CB  . ASP B 1 74  ? -18.628 -2.720  25.258  1.00 14.64 ? 74  ASP A CB  1 
ATOM   2686 C  CG  . ASP B 1 74  ? -17.903 -1.426  25.527  1.00 18.43 ? 74  ASP A CG  1 
ATOM   2687 O  OD1 . ASP B 1 74  ? -18.551 -0.340  25.645  1.00 20.91 ? 74  ASP A OD1 1 
ATOM   2688 O  OD2 . ASP B 1 74  ? -16.700 -1.432  25.648  1.00 17.68 ? 74  ASP A OD2 1 
ATOM   2689 N  N   . THR B 1 75  ? -21.699 -1.590  27.075  1.00 19.10 ? 75  THR A N   1 
ATOM   2690 C  CA  . THR B 1 75  ? -22.218 -1.274  28.451  1.00 19.89 ? 75  THR A CA  1 
ATOM   2691 C  C   . THR B 1 75  ? -22.330 -2.509  29.327  1.00 20.66 ? 75  THR A C   1 
ATOM   2692 O  O   . THR B 1 75  ? -21.977 -2.466  30.494  1.00 21.67 ? 75  THR A O   1 
ATOM   2693 C  CB  . THR B 1 75  ? -23.604 -0.519  28.379  1.00 20.05 ? 75  THR A CB  1 
ATOM   2694 O  OG1 . THR B 1 75  ? -23.369 0.749   27.799  1.00 19.51 ? 75  THR A OG1 1 
ATOM   2695 C  CG2 . THR B 1 75  ? -24.190 -0.249  29.741  1.00 21.52 ? 75  THR A CG2 1 
ATOM   2696 N  N   . GLU B 1 76  ? -22.868 -3.597  28.787  1.00 22.25 ? 76  GLU A N   1 
ATOM   2697 C  CA  . GLU B 1 76  ? -22.885 -4.858  29.515  1.00 23.62 ? 76  GLU A CA  1 
ATOM   2698 C  C   . GLU B 1 76  ? -22.459 -6.015  28.642  1.00 22.33 ? 76  GLU A C   1 
ATOM   2699 O  O   . GLU B 1 76  ? -21.874 -5.808  27.590  1.00 20.96 ? 76  GLU A O   1 
ATOM   2700 C  CB  . GLU B 1 76  ? -24.243 -5.146  30.182  1.00 23.89 ? 76  GLU A CB  1 
ATOM   2701 C  CG  . GLU B 1 76  ? -25.485 -4.933  29.330  1.00 28.59 ? 76  GLU A CG  1 
ATOM   2702 C  CD  . GLU B 1 76  ? -26.744 -5.356  30.086  1.00 29.02 ? 76  GLU A CD  1 
ATOM   2703 O  OE1 . GLU B 1 76  ? -27.872 -5.320  29.509  1.00 37.31 ? 76  GLU A OE1 1 
ATOM   2704 O  OE2 . GLU B 1 76  ? -26.580 -5.735  31.270  1.00 35.53 ? 76  GLU A OE2 1 
ATOM   2705 N  N   . ASN B 1 77  ? -22.699 -7.222  29.132  1.00 21.42 ? 77  ASN A N   1 
ATOM   2706 C  CA  . ASN B 1 77  ? -22.233 -8.445  28.490  1.00 22.36 ? 77  ASN A CA  1 
ATOM   2707 C  C   . ASN B 1 77  ? -23.269 -9.068  27.536  1.00 21.67 ? 77  ASN A C   1 
ATOM   2708 O  O   . ASN B 1 77  ? -23.409 -10.270 27.533  1.00 23.33 ? 77  ASN A O   1 
ATOM   2709 C  CB  . ASN B 1 77  ? -21.934 -9.508  29.559  1.00 22.04 ? 77  ASN A CB  1 
ATOM   2710 C  CG  . ASN B 1 77  ? -20.510 -9.465  30.111  1.00 20.32 ? 77  ASN A CG  1 
ATOM   2711 O  OD1 . ASN B 1 77  ? -19.574 -8.910  29.513  1.00 20.49 ? 77  ASN A OD1 1 
ATOM   2712 N  ND2 . ASN B 1 77  ? -20.333 -10.138 31.259  1.00 20.57 ? 77  ASN A ND2 1 
ATOM   2713 N  N   . LYS B 1 78  ? -23.960 -8.290  26.725  1.00 21.45 ? 78  LYS A N   1 
ATOM   2714 C  CA  . LYS B 1 78  ? -24.838 -8.860  25.640  1.00 22.80 ? 78  LYS A CA  1 
ATOM   2715 C  C   . LYS B 1 78  ? -24.013 -9.654  24.573  1.00 20.00 ? 78  LYS A C   1 
ATOM   2716 O  O   . LYS B 1 78  ? -24.446 -10.709 24.095  1.00 18.76 ? 78  LYS A O   1 
ATOM   2717 C  CB  . LYS B 1 78  ? -25.623 -7.716  24.947  1.00 22.88 ? 78  LYS A CB  1 
ATOM   2718 C  CG  . LYS B 1 78  ? -26.594 -6.971  25.890  1.00 26.02 ? 78  LYS A CG  1 
ATOM   2719 C  CD  . LYS B 1 78  ? -27.618 -6.163  25.100  1.00 28.32 ? 78  LYS A CD  1 
ATOM   2720 C  CE  . LYS B 1 78  ? -28.680 -5.431  26.010  1.00 32.95 ? 78  LYS A CE  1 
ATOM   2721 N  NZ  . LYS B 1 78  ? -28.424 -3.949  26.146  1.00 35.23 ? 78  LYS A NZ  1 
ATOM   2722 N  N   . SER B 1 79  ? -22.821 -9.155  24.235  1.00 18.57 ? 79  SER A N   1 
ATOM   2723 C  CA  . SER B 1 79  ? -22.016 -9.705  23.144  1.00 16.23 ? 79  SER A CA  1 
ATOM   2724 C  C   . SER B 1 79  ? -20.656 -10.034 23.725  1.00 15.32 ? 79  SER A C   1 
ATOM   2725 O  O   . SER B 1 79  ? -19.931 -9.132  24.179  1.00 13.28 ? 79  SER A O   1 
ATOM   2726 C  CB  . SER B 1 79  ? -21.909 -8.691  21.988  1.00 17.25 ? 79  SER A CB  1 
ATOM   2727 O  OG  . SER B 1 79  ? -23.218 -8.398  21.473  1.00 15.67 ? 79  SER A OG  1 
ATOM   2728 N  N   . VAL B 1 80  ? -20.343 -11.345 23.778  1.00 14.31 ? 80  VAL A N   1 
ATOM   2729 C  CA  . VAL B 1 80  ? -19.103 -11.799 24.411  1.00 13.84 ? 80  VAL A CA  1 
ATOM   2730 C  C   . VAL B 1 80  ? -18.451 -12.948 23.648  1.00 14.30 ? 80  VAL A C   1 
ATOM   2731 O  O   . VAL B 1 80  ? -19.134 -13.760 22.950  1.00 15.73 ? 80  VAL A O   1 
ATOM   2732 C  CB  . VAL B 1 80  ? -19.264 -12.134 25.909  1.00 13.77 ? 80  VAL A CB  1 
ATOM   2733 C  CG1 . VAL B 1 80  ? -19.788 -10.888 26.695  1.00 15.37 ? 80  VAL A CG1 1 
ATOM   2734 C  CG2 . VAL B 1 80  ? -20.218 -13.351 26.120  1.00 14.58 ? 80  VAL A CG2 1 
ATOM   2735 N  N   . LEU B 1 81  ? -17.127 -12.980 23.744  1.00 12.58 ? 81  LEU A N   1 
ATOM   2736 C  CA  . LEU B 1 81  ? -16.425 -14.103 23.252  1.00 13.54 ? 81  LEU A CA  1 
ATOM   2737 C  C   . LEU B 1 81  ? -15.819 -14.867 24.452  1.00 13.61 ? 81  LEU A C   1 
ATOM   2738 O  O   . LEU B 1 81  ? -15.163 -14.256 25.316  1.00 10.42 ? 81  LEU A O   1 
ATOM   2739 C  CB  . LEU B 1 81  ? -15.342 -13.640 22.256  1.00 14.66 ? 81  LEU A CB  1 
ATOM   2740 C  CG  . LEU B 1 81  ? -14.308 -14.658 21.745  1.00 11.31 ? 81  LEU A CG  1 
ATOM   2741 C  CD1 . LEU B 1 81  ? -14.956 -15.735 20.753  1.00 11.42 ? 81  LEU A CD1 1 
ATOM   2742 C  CD2 . LEU B 1 81  ? -13.161 -13.894 21.047  1.00 13.41 ? 81  LEU A CD2 1 
ATOM   2743 N  N   . ARG B 1 82  ? -15.987 -16.205 24.430  1.00 14.64 ? 82  ARG A N   1 
ATOM   2744 C  CA  . ARG B 1 82  ? -15.433 -17.108 25.445  1.00 15.54 ? 82  ARG A CA  1 
ATOM   2745 C  C   . ARG B 1 82  ? -14.845 -18.338 24.761  1.00 15.67 ? 82  ARG A C   1 
ATOM   2746 O  O   . ARG B 1 82  ? -14.866 -18.422 23.508  1.00 15.39 ? 82  ARG A O   1 
ATOM   2747 C  CB  . ARG B 1 82  ? -16.521 -17.491 26.466  1.00 14.68 ? 82  ARG A CB  1 
ATOM   2748 C  CG  . ARG B 1 82  ? -17.015 -16.320 27.334  1.00 14.09 ? 82  ARG A CG  1 
ATOM   2749 C  CD  . ARG B 1 82  ? -18.338 -16.688 28.029  1.00 19.71 ? 82  ARG A CD  1 
ATOM   2750 N  NE  . ARG B 1 82  ? -19.431 -16.776 27.097  1.00 26.09 ? 82  ARG A NE  1 
ATOM   2751 C  CZ  . ARG B 1 82  ? -20.698 -17.032 27.447  1.00 30.59 ? 82  ARG A CZ  1 
ATOM   2752 N  NH1 . ARG B 1 82  ? -21.041 -17.198 28.741  1.00 28.56 ? 82  ARG A NH1 1 
ATOM   2753 N  NH2 . ARG B 1 82  ? -21.619 -17.107 26.504  1.00 25.42 ? 82  ARG A NH2 1 
ATOM   2754 N  N   . GLY B 1 83  ? -14.291 -19.259 25.550  1.00 15.26 ? 83  GLY A N   1 
ATOM   2755 C  CA  . GLY B 1 83  ? -13.709 -20.476 25.019  1.00 14.97 ? 83  GLY A CA  1 
ATOM   2756 C  C   . GLY B 1 83  ? -12.455 -20.084 24.251  1.00 14.77 ? 83  GLY A C   1 
ATOM   2757 O  O   . GLY B 1 83  ? -11.802 -19.113 24.608  1.00 13.75 ? 83  GLY A O   1 
ATOM   2758 N  N   . GLY B 1 84  ? -12.161 -20.820 23.179  1.00 14.87 ? 84  GLY A N   1 
ATOM   2759 C  CA  . GLY B 1 84  ? -10.869 -20.654 22.486  1.00 15.78 ? 84  GLY A CA  1 
ATOM   2760 C  C   . GLY B 1 84  ? -9.697  -20.833 23.461  1.00 15.51 ? 84  GLY A C   1 
ATOM   2761 O  O   . GLY B 1 84  ? -9.700  -21.777 24.274  1.00 16.43 ? 84  GLY A O   1 
ATOM   2762 N  N   . PRO B 1 85  ? -8.670  -19.931 23.379  1.00 15.38 ? 85  PRO A N   1 
ATOM   2763 C  CA  . PRO B 1 85  ? -7.517  -19.905 24.350  1.00 17.19 ? 85  PRO A CA  1 
ATOM   2764 C  C   . PRO B 1 85  ? -7.802  -19.066 25.570  1.00 14.98 ? 85  PRO A C   1 
ATOM   2765 O  O   . PRO B 1 85  ? -6.945  -18.921 26.387  1.00 16.79 ? 85  PRO A O   1 
ATOM   2766 C  CB  . PRO B 1 85  ? -6.408  -19.174 23.571  1.00 15.82 ? 85  PRO A CB  1 
ATOM   2767 C  CG  . PRO B 1 85  ? -7.238  -18.076 22.749  1.00 14.15 ? 85  PRO A CG  1 
ATOM   2768 C  CD  . PRO B 1 85  ? -8.522  -18.894 22.311  1.00 16.26 ? 85  PRO A CD  1 
ATOM   2769 N  N   . LEU B 1 86  ? -9.011  -18.520 25.692  1.00 14.47 ? 86  LEU A N   1 
ATOM   2770 C  CA  . LEU B 1 86  ? -9.264  -17.458 26.659  1.00 12.81 ? 86  LEU A CA  1 
ATOM   2771 C  C   . LEU B 1 86  ? -9.742  -17.967 28.007  1.00 14.16 ? 86  LEU A C   1 
ATOM   2772 O  O   . LEU B 1 86  ? -10.529 -18.899 28.087  1.00 15.17 ? 86  LEU A O   1 
ATOM   2773 C  CB  . LEU B 1 86  ? -10.303 -16.455 26.130  1.00 14.74 ? 86  LEU A CB  1 
ATOM   2774 C  CG  . LEU B 1 86  ? -10.143 -15.886 24.716  1.00 11.02 ? 86  LEU A CG  1 
ATOM   2775 C  CD1 . LEU B 1 86  ? -11.453 -15.180 24.316  1.00 14.73 ? 86  LEU A CD1 1 
ATOM   2776 C  CD2 . LEU B 1 86  ? -9.021  -14.899 24.756  1.00 8.17  ? 86  LEU A CD2 1 
ATOM   2777 N  N   . THR B 1 87  ? -9.323  -17.260 29.040  1.00 14.95 ? 87  THR A N   1 
ATOM   2778 C  CA  . THR B 1 87  ? -9.869  -17.445 30.374  1.00 16.93 ? 87  THR A CA  1 
ATOM   2779 C  C   . THR B 1 87  ? -10.827 -16.315 30.605  1.00 16.13 ? 87  THR A C   1 
ATOM   2780 O  O   . THR B 1 87  ? -10.436 -15.145 30.654  1.00 16.25 ? 87  THR A O   1 
ATOM   2781 C  CB  . THR B 1 87  ? -8.770  -17.348 31.464  1.00 16.07 ? 87  THR A CB  1 
ATOM   2782 O  OG1 . THR B 1 87  ? -7.759  -18.332 31.197  1.00 22.17 ? 87  THR A OG1 1 
ATOM   2783 C  CG2 . THR B 1 87  ? -9.376  -17.577 32.919  1.00 20.64 ? 87  THR A CG2 1 
ATOM   2784 N  N   . GLY B 1 88  ? -12.075 -16.668 30.830  1.00 16.34 ? 88  GLY A N   1 
ATOM   2785 C  CA  . GLY B 1 88  ? -13.059 -15.650 31.185  1.00 16.96 ? 88  GLY A CA  1 
ATOM   2786 C  C   . GLY B 1 88  ? -13.737 -15.072 29.929  1.00 16.69 ? 88  GLY A C   1 
ATOM   2787 O  O   . GLY B 1 88  ? -13.632 -15.646 28.832  1.00 18.26 ? 88  GLY A O   1 
ATOM   2788 N  N   . SER B 1 89  ? -14.374 -13.923 30.089  1.00 14.64 ? 89  SER A N   1 
ATOM   2789 C  CA  . SER B 1 89  ? -15.353 -13.461 29.092  1.00 15.40 ? 89  SER A CA  1 
ATOM   2790 C  C   . SER B 1 89  ? -14.818 -12.158 28.583  1.00 14.64 ? 89  SER A C   1 
ATOM   2791 O  O   . SER B 1 89  ? -14.500 -11.260 29.358  1.00 13.83 ? 89  SER A O   1 
ATOM   2792 C  CB  . SER B 1 89  ? -16.708 -13.263 29.799  1.00 15.25 ? 89  SER A CB  1 
ATOM   2793 O  OG  . SER B 1 89  ? -17.684 -12.736 28.959  1.00 18.95 ? 89  SER A OG  1 
ATOM   2794 N  N   . TYR B 1 90  ? -14.707 -12.082 27.258  1.00 15.30 ? 90  TYR A N   1 
ATOM   2795 C  CA  . TYR B 1 90  ? -14.211 -10.877 26.544  1.00 15.16 ? 90  TYR A CA  1 
ATOM   2796 C  C   . TYR B 1 90  ? -15.352 -10.261 25.827  1.00 14.60 ? 90  TYR A C   1 
ATOM   2797 O  O   . TYR B 1 90  ? -16.018 -10.898 24.996  1.00 15.32 ? 90  TYR A O   1 
ATOM   2798 C  CB  . TYR B 1 90  ? -13.123 -11.311 25.578  1.00 15.24 ? 90  TYR A CB  1 
ATOM   2799 C  CG  . TYR B 1 90  ? -11.829 -11.649 26.317  1.00 12.86 ? 90  TYR A CG  1 
ATOM   2800 C  CD1 . TYR B 1 90  ? -11.752 -12.781 27.117  1.00 13.70 ? 90  TYR A CD1 1 
ATOM   2801 C  CD2 . TYR B 1 90  ? -10.699 -10.825 26.214  1.00 11.98 ? 90  TYR A CD2 1 
ATOM   2802 C  CE1 . TYR B 1 90  ? -10.581 -13.086 27.851  1.00 11.96 ? 90  TYR A CE1 1 
ATOM   2803 C  CE2 . TYR B 1 90  ? -9.502  -11.153 26.897  1.00 14.58 ? 90  TYR A CE2 1 
ATOM   2804 C  CZ  . TYR B 1 90  ? -9.482  -12.311 27.698  1.00 12.03 ? 90  TYR A CZ  1 
ATOM   2805 O  OH  . TYR B 1 90  ? -8.347  -12.655 28.383  1.00 15.54 ? 90  TYR A OH  1 
ATOM   2806 N  N   . ARG B 1 91  ? -15.573 -9.003  26.142  1.00 13.64 ? 91  ARG A N   1 
ATOM   2807 C  CA  . ARG B 1 91  ? -16.747 -8.301  25.713  1.00 14.05 ? 91  ARG A CA  1 
ATOM   2808 C  C   . ARG B 1 91  ? -16.458 -7.614  24.338  1.00 14.14 ? 91  ARG A C   1 
ATOM   2809 O  O   . ARG B 1 91  ? -15.489 -6.923  24.183  1.00 12.69 ? 91  ARG A O   1 
ATOM   2810 C  CB  . ARG B 1 91  ? -17.115 -7.243  26.742  1.00 12.55 ? 91  ARG A CB  1 
ATOM   2811 C  CG  . ARG B 1 91  ? -18.380 -6.503  26.476  1.00 13.52 ? 91  ARG A CG  1 
ATOM   2812 C  CD  . ARG B 1 91  ? -18.597 -5.424  27.538  1.00 12.64 ? 91  ARG A CD  1 
ATOM   2813 N  NE  . ARG B 1 91  ? -18.761 -6.106  28.854  1.00 18.15 ? 91  ARG A NE  1 
ATOM   2814 C  CZ  . ARG B 1 91  ? -18.892 -5.489  30.027  1.00 15.71 ? 91  ARG A CZ  1 
ATOM   2815 N  NH1 . ARG B 1 91  ? -18.977 -4.164  30.032  1.00 10.60 ? 91  ARG A NH1 1 
ATOM   2816 N  NH2 . ARG B 1 91  ? -18.992 -6.206  31.178  1.00 13.57 ? 91  ARG A NH2 1 
ATOM   2817 N  N   . LEU B 1 92  ? -17.373 -7.804  23.390  1.00 13.68 ? 92  LEU A N   1 
ATOM   2818 C  CA  . LEU B 1 92  ? -17.311 -7.102  22.084  1.00 13.34 ? 92  LEU A CA  1 
ATOM   2819 C  C   . LEU B 1 92  ? -17.279 -5.584  22.157  1.00 13.07 ? 92  LEU A C   1 
ATOM   2820 O  O   . LEU B 1 92  ? -18.135 -4.956  22.757  1.00 14.10 ? 92  LEU A O   1 
ATOM   2821 C  CB  . LEU B 1 92  ? -18.491 -7.503  21.228  1.00 11.94 ? 92  LEU A CB  1 
ATOM   2822 C  CG  . LEU B 1 92  ? -18.508 -6.900  19.820  1.00 12.09 ? 92  LEU A CG  1 
ATOM   2823 C  CD1 . LEU B 1 92  ? -17.253 -7.344  18.976  1.00 11.51 ? 92  LEU A CD1 1 
ATOM   2824 C  CD2 . LEU B 1 92  ? -19.808 -7.391  19.178  1.00 14.32 ? 92  LEU A CD2 1 
ATOM   2825 N  N   . ARG B 1 93  ? -16.273 -4.984  21.521  1.00 11.64 ? 93  ARG A N   1 
ATOM   2826 C  CA  . ARG B 1 93  ? -16.161 -3.556  21.524  1.00 13.00 ? 93  ARG A CA  1 
ATOM   2827 C  C   . ARG B 1 93  ? -16.314 -2.967  20.115  1.00 13.10 ? 93  ARG A C   1 
ATOM   2828 O  O   . ARG B 1 93  ? -16.995 -1.942  19.934  1.00 14.61 ? 93  ARG A O   1 
ATOM   2829 C  CB  . ARG B 1 93  ? -14.785 -3.217  22.071  1.00 13.70 ? 93  ARG A CB  1 
ATOM   2830 C  CG  . ARG B 1 93  ? -14.399 -1.802  21.941  1.00 18.04 ? 93  ARG A CG  1 
ATOM   2831 C  CD  . ARG B 1 93  ? -14.571 -1.071  23.188  1.00 21.26 ? 93  ARG A CD  1 
ATOM   2832 N  NE  . ARG B 1 93  ? -14.087 0.300   23.025  1.00 23.20 ? 93  ARG A NE  1 
ATOM   2833 C  CZ  . ARG B 1 93  ? -14.395 1.279   23.877  1.00 26.35 ? 93  ARG A CZ  1 
ATOM   2834 N  NH1 . ARG B 1 93  ? -15.156 1.003   24.972  1.00 20.77 ? 93  ARG A NH1 1 
ATOM   2835 N  NH2 . ARG B 1 93  ? -13.914 2.517   23.635  1.00 24.88 ? 93  ARG A NH2 1 
ATOM   2836 N  N   . GLN B 1 94  ? -15.581 -3.514  19.153  1.00 12.09 ? 94  GLN A N   1 
ATOM   2837 C  CA  . GLN B 1 94  ? -15.485 -2.795  17.878  1.00 13.97 ? 94  GLN A CA  1 
ATOM   2838 C  C   . GLN B 1 94  ? -15.134 -3.740  16.764  1.00 12.50 ? 94  GLN A C   1 
ATOM   2839 O  O   . GLN B 1 94  ? -14.498 -4.753  17.033  1.00 12.80 ? 94  GLN A O   1 
ATOM   2840 C  CB  . GLN B 1 94  ? -14.388 -1.727  18.119  1.00 15.15 ? 94  GLN A CB  1 
ATOM   2841 C  CG  . GLN B 1 94  ? -14.064 -0.945  17.032  1.00 22.62 ? 94  GLN A CG  1 
ATOM   2842 C  CD  . GLN B 1 94  ? -12.713 -1.296  16.475  1.00 20.60 ? 94  GLN A CD  1 
ATOM   2843 O  OE1 . GLN B 1 94  ? -12.444 -2.419  16.011  1.00 15.94 ? 94  GLN A OE1 1 
ATOM   2844 N  NE2 . GLN B 1 94  ? -11.893 -0.307  16.433  1.00 19.59 ? 94  GLN A NE2 1 
ATOM   2845 N  N   . VAL B 1 95  ? -15.494 -3.420  15.503  1.00 11.44 ? 95  VAL A N   1 
ATOM   2846 C  CA  . VAL B 1 95  ? -15.039 -4.218  14.352  1.00 11.80 ? 95  VAL A CA  1 
ATOM   2847 C  C   . VAL B 1 95  ? -14.431 -3.262  13.298  1.00 12.04 ? 95  VAL A C   1 
ATOM   2848 O  O   . VAL B 1 95  ? -14.989 -2.184  13.046  1.00 11.77 ? 95  VAL A O   1 
ATOM   2849 C  CB  . VAL B 1 95  ? -16.188 -4.949  13.664  1.00 10.99 ? 95  VAL A CB  1 
ATOM   2850 C  CG1 . VAL B 1 95  ? -15.789 -5.430  12.203  1.00 11.40 ? 95  VAL A CG1 1 
ATOM   2851 C  CG2 . VAL B 1 95  ? -16.742 -6.157  14.556  1.00 12.97 ? 95  VAL A CG2 1 
ATOM   2852 N  N   . HIS B 1 96  ? -13.337 -3.719  12.665  1.00 12.22 ? 96  HIS A N   1 
ATOM   2853 C  CA  . HIS B 1 96  ? -12.737 -2.945  11.599  1.00 10.80 ? 96  HIS A CA  1 
ATOM   2854 C  C   . HIS B 1 96  ? -12.126 -3.895  10.579  1.00 10.75 ? 96  HIS A C   1 
ATOM   2855 O  O   . HIS B 1 96  ? -12.185 -5.078  10.730  1.00 9.89  ? 96  HIS A O   1 
ATOM   2856 C  CB  . HIS B 1 96  ? -11.691 -1.957  12.148  1.00 10.41 ? 96  HIS A CB  1 
ATOM   2857 C  CG  . HIS B 1 96  ? -10.507 -2.630  12.762  1.00 9.62  ? 96  HIS A CG  1 
ATOM   2858 N  ND1 . HIS B 1 96  ? -10.474 -2.939  14.100  1.00 10.96 ? 96  HIS A ND1 1 
ATOM   2859 C  CD2 . HIS B 1 96  ? -9.327  -3.067  12.237  1.00 7.52  ? 96  HIS A CD2 1 
ATOM   2860 C  CE1 . HIS B 1 96  ? -9.350  -3.578  14.374  1.00 10.64 ? 96  HIS A CE1 1 
ATOM   2861 N  NE2 . HIS B 1 96  ? -8.616  -3.653  13.273  1.00 6.09  ? 96  HIS A NE2 1 
ATOM   2862 N  N   . LEU B 1 97  ? -11.573 -3.320  9.530   1.00 9.81  ? 97  LEU A N   1 
ATOM   2863 C  CA  . LEU B 1 97  ? -11.082 -4.075  8.412   1.00 10.23 ? 97  LEU A CA  1 
ATOM   2864 C  C   . LEU B 1 97  ? -9.755  -3.550  7.888   1.00 9.21  ? 97  LEU A C   1 
ATOM   2865 O  O   . LEU B 1 97  ? -9.454  -2.345  7.964   1.00 11.94 ? 97  LEU A O   1 
ATOM   2866 C  CB  . LEU B 1 97  ? -12.118 -4.061  7.298   1.00 10.06 ? 97  LEU A CB  1 
ATOM   2867 C  CG  . LEU B 1 97  ? -11.838 -4.899  6.083   1.00 8.33  ? 97  LEU A CG  1 
ATOM   2868 C  CD1 . LEU B 1 97  ? -12.094 -6.317  6.406   1.00 5.74  ? 97  LEU A CD1 1 
ATOM   2869 C  CD2 . LEU B 1 97  ? -12.826 -4.421  4.943   1.00 8.46  ? 97  LEU A CD2 1 
ATOM   2870 N  N   . HIS B 1 98  ? -8.909  -4.482  7.469   1.00 9.86  ? 98  HIS A N   1 
ATOM   2871 C  CA  . HIS B 1 98  ? -7.679  -4.122  6.826   1.00 9.73  ? 98  HIS A CA  1 
ATOM   2872 C  C   . HIS B 1 98  ? -7.709  -4.717  5.386   1.00 9.76  ? 98  HIS A C   1 
ATOM   2873 O  O   . HIS B 1 98  ? -8.222  -5.808  5.157   1.00 10.72 ? 98  HIS A O   1 
ATOM   2874 C  CB  . HIS B 1 98  ? -6.444  -4.661  7.553   1.00 10.19 ? 98  HIS A CB  1 
ATOM   2875 C  CG  . HIS B 1 98  ? -6.346  -4.237  8.977   1.00 12.35 ? 98  HIS A CG  1 
ATOM   2876 N  ND1 . HIS B 1 98  ? -5.775  -3.043  9.367   1.00 11.76 ? 98  HIS A ND1 1 
ATOM   2877 C  CD2 . HIS B 1 98  ? -6.808  -4.828  10.112  1.00 13.05 ? 98  HIS A CD2 1 
ATOM   2878 C  CE1 . HIS B 1 98  ? -5.831  -2.945  10.686  1.00 11.41 ? 98  HIS A CE1 1 
ATOM   2879 N  NE2 . HIS B 1 98  ? -6.459  -4.011  11.159  1.00 13.62 ? 98  HIS A NE2 1 
ATOM   2880 N  N   . TRP B 1 99  ? -7.079  -4.009  4.474   1.00 10.12 ? 99  TRP A N   1 
ATOM   2881 C  CA  . TRP B 1 99  ? -7.006  -4.370  3.087   1.00 10.94 ? 99  TRP A CA  1 
ATOM   2882 C  C   . TRP B 1 99  ? -5.707  -3.780  2.490   1.00 10.33 ? 99  TRP A C   1 
ATOM   2883 O  O   . TRP B 1 99  ? -4.878  -3.152  3.163   1.00 10.67 ? 99  TRP A O   1 
ATOM   2884 C  CB  . TRP B 1 99  ? -8.255  -3.865  2.308   1.00 10.08 ? 99  TRP A CB  1 
ATOM   2885 C  CG  . TRP B 1 99  ? -8.443  -2.286  2.378   1.00 10.19 ? 99  TRP A CG  1 
ATOM   2886 C  CD1 . TRP B 1 99  ? -7.825  -1.333  1.579   1.00 11.92 ? 99  TRP A CD1 1 
ATOM   2887 C  CD2 . TRP B 1 99  ? -9.218  -1.563  3.337   1.00 10.85 ? 99  TRP A CD2 1 
ATOM   2888 N  NE1 . TRP B 1 99  ? -8.201  -0.084  1.975   1.00 11.93 ? 99  TRP A NE1 1 
ATOM   2889 C  CE2 . TRP B 1 99  ? -9.078  -0.207  3.045   1.00 10.19 ? 99  TRP A CE2 1 
ATOM   2890 C  CE3 . TRP B 1 99  ? -10.062 -1.961  4.433   1.00 9.91  ? 99  TRP A CE3 1 
ATOM   2891 C  CZ2 . TRP B 1 99  ? -9.690  0.793   3.823   1.00 11.22 ? 99  TRP A CZ2 1 
ATOM   2892 C  CZ3 . TRP B 1 99  ? -10.701 -0.999  5.156   1.00 9.74  ? 99  TRP A CZ3 1 
ATOM   2893 C  CH2 . TRP B 1 99  ? -10.536 0.371   4.851   1.00 11.85 ? 99  TRP A CH2 1 
ATOM   2894 N  N   . GLY B 1 100 ? -5.505  -4.051  1.217   1.00 12.63 ? 100 GLY A N   1 
ATOM   2895 C  CA  . GLY B 1 100 ? -4.338  -3.537  0.469   1.00 12.04 ? 100 GLY A CA  1 
ATOM   2896 C  C   . GLY B 1 100 ? -4.790  -2.834  -0.786  1.00 13.84 ? 100 GLY A C   1 
ATOM   2897 O  O   . GLY B 1 100 ? -5.990  -2.816  -1.101  1.00 14.19 ? 100 GLY A O   1 
ATOM   2898 N  N   . SER B 1 101 ? -3.849  -2.294  -1.564  1.00 15.24 ? 101 SER A N   1 
ATOM   2899 C  CA  . SER B 1 101 ? -4.241  -1.694  -2.867  1.00 14.69 ? 101 SER A CA  1 
ATOM   2900 C  C   . SER B 1 101 ? -4.603  -2.686  -3.993  1.00 15.07 ? 101 SER A C   1 
ATOM   2901 O  O   . SER B 1 101 ? -5.246  -2.284  -4.975  1.00 15.05 ? 101 SER A O   1 
ATOM   2902 C  CB  . SER B 1 101 ? -3.178  -0.657  -3.340  1.00 14.19 ? 101 SER A CB  1 
ATOM   2903 O  OG  . SER B 1 101 ? -2.073  -1.315  -3.820  1.00 15.76 ? 101 SER A OG  1 
ATOM   2904 N  N   . ALA B 1 102 ? -4.272  -3.965  -3.819  1.00 14.40 ? 102 ALA A N   1 
ATOM   2905 C  CA  . ALA B 1 102 ? -4.564  -4.989  -4.779  1.00 17.18 ? 102 ALA A CA  1 
ATOM   2906 C  C   . ALA B 1 102 ? -5.235  -6.127  -3.997  1.00 16.95 ? 102 ALA A C   1 
ATOM   2907 O  O   . ALA B 1 102 ? -4.880  -6.354  -2.847  1.00 17.81 ? 102 ALA A O   1 
ATOM   2908 C  CB  . ALA B 1 102 ? -3.278  -5.530  -5.464  1.00 15.29 ? 102 ALA A CB  1 
ATOM   2909 N  N   . ASP B 1 103 ? -6.167  -6.831  -4.653  1.00 18.51 ? 103 ASP A N   1 
ATOM   2910 C  CA  . ASP B 1 103 ? -6.941  -7.926  -4.075  1.00 21.35 ? 103 ASP A CA  1 
ATOM   2911 C  C   . ASP B 1 103 ? -6.134  -9.138  -3.655  1.00 22.84 ? 103 ASP A C   1 
ATOM   2912 O  O   . ASP B 1 103 ? -6.672  -9.987  -2.963  1.00 24.56 ? 103 ASP A O   1 
ATOM   2913 C  CB  . ASP B 1 103 ? -8.047  -8.429  -5.019  1.00 20.70 ? 103 ASP A CB  1 
ATOM   2914 C  CG  . ASP B 1 103 ? -9.129  -7.460  -5.208  1.00 18.52 ? 103 ASP A CG  1 
ATOM   2915 O  OD1 . ASP B 1 103 ? -9.174  -6.395  -4.592  1.00 20.37 ? 103 ASP A OD1 1 
ATOM   2916 O  OD2 . ASP B 1 103 ? -9.966  -7.731  -6.082  1.00 26.67 ? 103 ASP A OD2 1 
ATOM   2917 N  N   . ASP B 1 104 ? -4.879  -9.235  -4.098  1.00 24.41 ? 104 ASP A N   1 
ATOM   2918 C  CA  . ASP B 1 104 ? -4.052  -10.413 -3.877  1.00 25.26 ? 104 ASP A CA  1 
ATOM   2919 C  C   . ASP B 1 104 ? -3.173  -10.258 -2.615  1.00 24.92 ? 104 ASP A C   1 
ATOM   2920 O  O   . ASP B 1 104 ? -2.493  -11.217 -2.236  1.00 25.22 ? 104 ASP A O   1 
ATOM   2921 C  CB  . ASP B 1 104 ? -3.133  -10.609 -5.092  1.00 27.14 ? 104 ASP A CB  1 
ATOM   2922 C  CG  . ASP B 1 104 ? -2.608  -9.276  -5.634  1.00 30.55 ? 104 ASP A CG  1 
ATOM   2923 O  OD1 . ASP B 1 104 ? -3.110  -8.784  -6.700  1.00 37.43 ? 104 ASP A OD1 1 
ATOM   2924 O  OD2 . ASP B 1 104 ? -1.707  -8.673  -5.010  1.00 34.53 ? 104 ASP A OD2 1 
ATOM   2925 N  N   . HIS B 1 105 ? -3.208  -9.075  -1.981  1.00 22.25 ? 105 HIS A N   1 
ATOM   2926 C  CA  . HIS B 1 105 ? -2.348  -8.763  -0.884  1.00 21.03 ? 105 HIS A CA  1 
ATOM   2927 C  C   . HIS B 1 105 ? -2.933  -7.705  0.116   1.00 18.79 ? 105 HIS A C   1 
ATOM   2928 O  O   . HIS B 1 105 ? -2.464  -6.555  0.173   1.00 17.05 ? 105 HIS A O   1 
ATOM   2929 C  CB  . HIS B 1 105 ? -1.037  -8.265  -1.515  1.00 24.38 ? 105 HIS A CB  1 
ATOM   2930 C  CG  . HIS B 1 105 ? 0.142   -8.477  -0.663  1.00 27.82 ? 105 HIS A CG  1 
ATOM   2931 N  ND1 . HIS B 1 105 ? 0.566   -7.539  0.260   1.00 33.97 ? 105 HIS A ND1 1 
ATOM   2932 C  CD2 . HIS B 1 105 ? 1.001   -9.524  -0.573  1.00 34.07 ? 105 HIS A CD2 1 
ATOM   2933 C  CE1 . HIS B 1 105 ? 1.645   -7.996  0.876   1.00 35.85 ? 105 HIS A CE1 1 
ATOM   2934 N  NE2 . HIS B 1 105 ? 1.927   -9.197  0.394   1.00 37.86 ? 105 HIS A NE2 1 
ATOM   2935 N  N   . GLY B 1 106 ? -3.949  -8.074  0.865   1.00 15.22 ? 106 GLY A N   1 
ATOM   2936 C  CA  . GLY B 1 106 ? -4.568  -7.114  1.783   1.00 15.50 ? 106 GLY A CA  1 
ATOM   2937 C  C   . GLY B 1 106 ? -4.645  -7.494  3.242   1.00 14.71 ? 106 GLY A C   1 
ATOM   2938 O  O   . GLY B 1 106 ? -4.887  -6.628  4.088   1.00 14.42 ? 106 GLY A O   1 
ATOM   2939 N  N   . SER B 1 107 ? -4.401  -8.773  3.563   1.00 14.68 ? 107 SER A N   1 
ATOM   2940 C  CA  . SER B 1 107 ? -4.511  -9.249  4.951   1.00 12.77 ? 107 SER A CA  1 
ATOM   2941 C  C   . SER B 1 107 ? -3.250  -8.867  5.802   1.00 13.34 ? 107 SER A C   1 
ATOM   2942 O  O   . SER B 1 107 ? -2.180  -8.511  5.270   1.00 13.82 ? 107 SER A O   1 
ATOM   2943 C  CB  . SER B 1 107 ? -4.803  -10.767 4.960   1.00 10.40 ? 107 SER A CB  1 
ATOM   2944 O  OG  . SER B 1 107 ? -3.684  -11.570 4.527   1.00 10.31 ? 107 SER A OG  1 
ATOM   2945 N  N   . GLU B 1 108 ? -3.386  -8.930  7.135   1.00 11.34 ? 108 GLU A N   1 
ATOM   2946 C  CA  . GLU B 1 108 ? -2.293  -8.669  8.075   1.00 11.41 ? 108 GLU A CA  1 
ATOM   2947 C  C   . GLU B 1 108 ? -1.529  -9.997  8.385   1.00 12.15 ? 108 GLU A C   1 
ATOM   2948 O  O   . GLU B 1 108 ? -0.316  -10.101 8.235   1.00 13.65 ? 108 GLU A O   1 
ATOM   2949 C  CB  . GLU B 1 108 ? -2.921  -8.057  9.360   1.00 10.38 ? 108 GLU A CB  1 
ATOM   2950 C  CG  . GLU B 1 108 ? -3.375  -6.652  9.041   1.00 12.89 ? 108 GLU A CG  1 
ATOM   2951 C  CD  . GLU B 1 108 ? -3.225  -5.614  10.186  1.00 9.59  ? 108 GLU A CD  1 
ATOM   2952 O  OE1 . GLU B 1 108 ? -3.802  -5.824  11.248  1.00 11.96 ? 108 GLU A OE1 1 
ATOM   2953 O  OE2 . GLU B 1 108 ? -2.604  -4.562  9.972   1.00 14.79 ? 108 GLU A OE2 1 
ATOM   2954 N  N   . HIS B 1 109 ? -2.249  -10.979 8.896   1.00 12.03 ? 109 HIS A N   1 
ATOM   2955 C  CA  . HIS B 1 109 ? -1.748  -12.354 8.974   1.00 13.00 ? 109 HIS A CA  1 
ATOM   2956 C  C   . HIS B 1 109 ? -1.638  -12.937 7.578   1.00 12.97 ? 109 HIS A C   1 
ATOM   2957 O  O   . HIS B 1 109 ? -2.387  -12.537 6.669   1.00 10.37 ? 109 HIS A O   1 
ATOM   2958 C  CB  . HIS B 1 109 ? -2.631  -13.163 9.938   1.00 12.51 ? 109 HIS A CB  1 
ATOM   2959 C  CG  . HIS B 1 109 ? -2.583  -12.585 11.327  1.00 10.65 ? 109 HIS A CG  1 
ATOM   2960 N  ND1 . HIS B 1 109 ? -3.489  -11.649 11.794  1.00 8.47  ? 109 HIS A ND1 1 
ATOM   2961 C  CD2 . HIS B 1 109 ? -1.676  -12.765 12.317  1.00 10.30 ? 109 HIS A CD2 1 
ATOM   2962 C  CE1 . HIS B 1 109 ? -3.168  -11.330 13.042  1.00 9.66  ? 109 HIS A CE1 1 
ATOM   2963 N  NE2 . HIS B 1 109 ? -2.027  -11.929 13.349  1.00 9.01  ? 109 HIS A NE2 1 
ATOM   2964 N  N   . ILE B 1 110 ? -0.614  -13.773 7.415   1.00 13.70 ? 110 ILE A N   1 
ATOM   2965 C  CA  . ILE B 1 110 ? -0.270  -14.410 6.137   1.00 15.13 ? 110 ILE A CA  1 
ATOM   2966 C  C   . ILE B 1 110 ? -0.118  -15.855 6.553   1.00 14.91 ? 110 ILE A C   1 
ATOM   2967 O  O   . ILE B 1 110 ? 0.413   -16.120 7.631   1.00 15.00 ? 110 ILE A O   1 
ATOM   2968 C  CB  . ILE B 1 110 ? 1.090   -13.924 5.666   1.00 16.26 ? 110 ILE A CB  1 
ATOM   2969 C  CG1 . ILE B 1 110 ? 1.250   -12.421 5.955   1.00 19.26 ? 110 ILE A CG1 1 
ATOM   2970 C  CG2 . ILE B 1 110 ? 1.412   -14.441 4.132   1.00 14.08 ? 110 ILE A CG2 1 
ATOM   2971 C  CD1 . ILE B 1 110 ? 0.947   -11.467 4.885   1.00 21.68 ? 110 ILE A CD1 1 
ATOM   2972 N  N   . VAL B 1 111 ? -0.592  -16.765 5.716   1.00 14.95 ? 111 VAL A N   1 
ATOM   2973 C  CA  . VAL B 1 111 ? -0.594  -18.154 6.058   1.00 14.39 ? 111 VAL A CA  1 
ATOM   2974 C  C   . VAL B 1 111 ? 0.232   -18.879 5.018   1.00 15.53 ? 111 VAL A C   1 
ATOM   2975 O  O   . VAL B 1 111 ? -0.183  -18.984 3.861   1.00 13.40 ? 111 VAL A O   1 
ATOM   2976 C  CB  . VAL B 1 111 ? -2.031  -18.811 6.094   1.00 15.40 ? 111 VAL A CB  1 
ATOM   2977 C  CG1 . VAL B 1 111 ? -1.827  -20.201 6.527   1.00 15.55 ? 111 VAL A CG1 1 
ATOM   2978 C  CG2 . VAL B 1 111 ? -2.954  -18.114 7.121   1.00 11.86 ? 111 VAL A CG2 1 
ATOM   2979 N  N   . ASP B 1 112 ? 1.386   -19.390 5.444   1.00 15.43 ? 112 ASP A N   1 
ATOM   2980 C  CA  . ASP B 1 112 ? 2.323   -19.991 4.530   1.00 16.38 ? 112 ASP A CA  1 
ATOM   2981 C  C   . ASP B 1 112 ? 2.503   -19.170 3.243   1.00 16.78 ? 112 ASP A C   1 
ATOM   2982 O  O   . ASP B 1 112 ? 2.415   -19.711 2.141   1.00 16.73 ? 112 ASP A O   1 
ATOM   2983 C  CB  . ASP B 1 112 ? 1.897   -21.432 4.222   1.00 16.67 ? 112 ASP A CB  1 
ATOM   2984 C  CG  . ASP B 1 112 ? 2.082   -22.314 5.406   1.00 17.78 ? 112 ASP A CG  1 
ATOM   2985 O  OD1 . ASP B 1 112 ? 3.185   -22.298 6.002   1.00 21.61 ? 112 ASP A OD1 1 
ATOM   2986 O  OD2 . ASP B 1 112 ? 1.149   -23.020 5.725   1.00 21.07 ? 112 ASP A OD2 1 
ATOM   2987 N  N   . GLY B 1 113 ? 2.785   -17.892 3.426   1.00 14.91 ? 113 GLY A N   1 
ATOM   2988 C  CA  . GLY B 1 113 ? 2.930   -16.954 2.308   1.00 15.91 ? 113 GLY A CA  1 
ATOM   2989 C  C   . GLY B 1 113 ? 1.671   -16.449 1.642   1.00 16.72 ? 113 GLY A C   1 
ATOM   2990 O  O   . GLY B 1 113 ? 1.752   -15.523 0.812   1.00 18.86 ? 113 GLY A O   1 
ATOM   2991 N  N   . VAL B 1 114 ? 0.520   -17.068 1.952   1.00 16.07 ? 114 VAL A N   1 
ATOM   2992 C  CA  . VAL B 1 114 ? -0.776  -16.636 1.351   1.00 17.07 ? 114 VAL A CA  1 
ATOM   2993 C  C   . VAL B 1 114 ? -1.298  -15.411 2.106   1.00 15.49 ? 114 VAL A C   1 
ATOM   2994 O  O   . VAL B 1 114 ? -1.547  -15.444 3.305   1.00 16.43 ? 114 VAL A O   1 
ATOM   2995 C  CB  . VAL B 1 114 ? -1.811  -17.849 1.228   1.00 17.02 ? 114 VAL A CB  1 
ATOM   2996 C  CG1 . VAL B 1 114 ? -3.149  -17.421 0.549   1.00 17.68 ? 114 VAL A CG1 1 
ATOM   2997 C  CG2 . VAL B 1 114 ? -1.174  -18.979 0.459   1.00 18.01 ? 114 VAL A CG2 1 
ATOM   2998 N  N   A SER B 1 115 ? -1.335  -14.286 1.397   0.50 16.31 ? 115 SER A N   1 
ATOM   2999 N  N   B SER B 1 115 ? -1.423  -14.292 1.397   0.50 16.52 ? 115 SER A N   1 
ATOM   3000 C  CA  A SER B 1 115 ? -2.061  -13.112 1.843   0.50 14.95 ? 115 SER A CA  1 
ATOM   3001 C  CA  B SER B 1 115 ? -2.039  -13.095 1.964   0.50 15.29 ? 115 SER A CA  1 
ATOM   3002 C  C   A SER B 1 115 ? -3.474  -13.313 1.381   0.50 14.65 ? 115 SER A C   1 
ATOM   3003 C  C   B SER B 1 115 ? -3.377  -12.864 1.311   0.50 15.47 ? 115 SER A C   1 
ATOM   3004 O  O   A SER B 1 115 ? -3.721  -13.943 0.330   0.50 12.55 ? 115 SER A O   1 
ATOM   3005 O  O   B SER B 1 115 ? -3.464  -12.741 0.079   0.50 15.08 ? 115 SER A O   1 
ATOM   3006 C  CB  A SER B 1 115 ? -1.498  -11.845 1.202   0.50 15.85 ? 115 SER A CB  1 
ATOM   3007 C  CB  B SER B 1 115 ? -1.150  -11.873 1.782   0.50 15.94 ? 115 SER A CB  1 
ATOM   3008 O  OG  A SER B 1 115 ? -0.301  -11.447 1.829   0.50 16.45 ? 115 SER A OG  1 
ATOM   3009 O  OG  B SER B 1 115 ? -1.907  -10.687 1.982   0.50 14.56 ? 115 SER A OG  1 
ATOM   3010 N  N   . TYR B 1 116 ? -4.422  -12.759 2.139   1.00 14.49 ? 116 TYR A N   1 
ATOM   3011 C  CA  . TYR B 1 116 ? -5.779  -12.700 1.684   1.00 14.71 ? 116 TYR A CA  1 
ATOM   3012 C  C   . TYR B 1 116 ? -6.121  -11.342 1.114   1.00 13.16 ? 116 TYR A C   1 
ATOM   3013 O  O   . TYR B 1 116 ? -5.319  -10.411 1.179   1.00 12.87 ? 116 TYR A O   1 
ATOM   3014 C  CB  . TYR B 1 116 ? -6.751  -13.245 2.791   1.00 14.37 ? 116 TYR A CB  1 
ATOM   3015 C  CG  . TYR B 1 116 ? -6.493  -14.710 3.015   1.00 17.00 ? 116 TYR A CG  1 
ATOM   3016 C  CD1 . TYR B 1 116 ? -7.200  -15.676 2.309   1.00 15.80 ? 116 TYR A CD1 1 
ATOM   3017 C  CD2 . TYR B 1 116 ? -5.537  -15.142 3.942   1.00 14.98 ? 116 TYR A CD2 1 
ATOM   3018 C  CE1 . TYR B 1 116 ? -6.925  -17.018 2.501   1.00 19.21 ? 116 TYR A CE1 1 
ATOM   3019 C  CE2 . TYR B 1 116 ? -5.284  -16.479 4.156   1.00 15.65 ? 116 TYR A CE2 1 
ATOM   3020 C  CZ  . TYR B 1 116 ? -6.015  -17.397 3.426   1.00 20.06 ? 116 TYR A CZ  1 
ATOM   3021 O  OH  . TYR B 1 116 ? -5.794  -18.719 3.628   1.00 24.51 ? 116 TYR A OH  1 
ATOM   3022 N  N   . ALA B 1 117 ? -7.293  -11.202 0.504   1.00 11.90 ? 117 ALA A N   1 
ATOM   3023 C  CA  . ALA B 1 117 ? -7.710  -9.900  -0.003  1.00 11.09 ? 117 ALA A CA  1 
ATOM   3024 C  C   . ALA B 1 117 ? -7.913  -8.829  1.112   1.00 12.20 ? 117 ALA A C   1 
ATOM   3025 O  O   . ALA B 1 117 ? -7.725  -7.600  0.885   1.00 12.91 ? 117 ALA A O   1 
ATOM   3026 C  CB  . ALA B 1 117 ? -8.979  -10.057 -0.782  1.00 9.25  ? 117 ALA A CB  1 
ATOM   3027 N  N   . ALA B 1 118 ? -8.405  -9.281  2.275   1.00 11.61 ? 118 ALA A N   1 
ATOM   3028 C  CA  . ALA B 1 118 ? -8.651  -8.405  3.413   1.00 11.17 ? 118 ALA A CA  1 
ATOM   3029 C  C   . ALA B 1 118 ? -8.716  -9.214  4.673   1.00 11.12 ? 118 ALA A C   1 
ATOM   3030 O  O   . ALA B 1 118 ? -8.609  -10.456 4.632   1.00 9.76  ? 118 ALA A O   1 
ATOM   3031 C  CB  . ALA B 1 118 ? -9.944  -7.548  3.273   1.00 8.00  ? 118 ALA A CB  1 
ATOM   3032 N  N   . GLU B 1 119 ? -8.757  -8.485  5.796   1.00 10.95 ? 119 GLU A N   1 
ATOM   3033 C  CA  . GLU B 1 119 ? -8.846  -9.143  7.077   1.00 10.88 ? 119 GLU A CA  1 
ATOM   3034 C  C   . GLU B 1 119 ? -9.680  -8.328  8.058   1.00 9.57  ? 119 GLU A C   1 
ATOM   3035 O  O   . GLU B 1 119 ? -9.337  -7.173  8.419   1.00 10.19 ? 119 GLU A O   1 
ATOM   3036 C  CB  . GLU B 1 119 ? -7.444  -9.431  7.655   1.00 11.41 ? 119 GLU A CB  1 
ATOM   3037 C  CG  . GLU B 1 119 ? -7.473  -10.271 8.953   1.00 8.69  ? 119 GLU A CG  1 
ATOM   3038 C  CD  . GLU B 1 119 ? -6.040  -10.597 9.417   1.00 11.58 ? 119 GLU A CD  1 
ATOM   3039 O  OE1 . GLU B 1 119 ? -5.138  -10.681 8.547   1.00 8.77  ? 119 GLU A OE1 1 
ATOM   3040 O  OE2 . GLU B 1 119 ? -5.816  -10.793 10.645  1.00 10.88 ? 119 GLU A OE2 1 
ATOM   3041 N  N   . LEU B 1 120 ? -10.713 -9.012  8.566   1.00 9.34  ? 120 LEU A N   1 
ATOM   3042 C  CA  . LEU B 1 120 ? -11.648 -8.434  9.491   1.00 10.84 ? 120 LEU A CA  1 
ATOM   3043 C  C   . LEU B 1 120 ? -11.168 -8.715  10.899  1.00 11.50 ? 120 LEU A C   1 
ATOM   3044 O  O   . LEU B 1 120 ? -10.835 -9.863  11.229  1.00 11.91 ? 120 LEU A O   1 
ATOM   3045 C  CB  . LEU B 1 120 ? -13.052 -8.995  9.270   1.00 10.37 ? 120 LEU A CB  1 
ATOM   3046 C  CG  . LEU B 1 120 ? -14.135 -8.252  10.063  1.00 10.76 ? 120 LEU A CG  1 
ATOM   3047 C  CD1 . LEU B 1 120 ? -14.682 -7.059  9.301   1.00 13.56 ? 120 LEU A CD1 1 
ATOM   3048 C  CD2 . LEU B 1 120 ? -15.265 -9.140  10.390  1.00 15.23 ? 120 LEU A CD2 1 
ATOM   3049 N  N   . HIS B 1 121 ? -11.201 -7.677  11.734  1.00 11.51 ? 121 HIS A N   1 
ATOM   3050 C  CA  . HIS B 1 121 ? -10.805 -7.827  13.144  1.00 10.75 ? 121 HIS A CA  1 
ATOM   3051 C  C   . HIS B 1 121 ? -11.959 -7.486  14.052  1.00 11.55 ? 121 HIS A C   1 
ATOM   3052 O  O   . HIS B 1 121 ? -12.542 -6.420  13.929  1.00 11.32 ? 121 HIS A O   1 
ATOM   3053 C  CB  . HIS B 1 121 ? -9.599  -6.960  13.475  1.00 10.62 ? 121 HIS A CB  1 
ATOM   3054 C  CG  . HIS B 1 121 ? -8.338  -7.453  12.819  1.00 11.64 ? 121 HIS A CG  1 
ATOM   3055 N  ND1 . HIS B 1 121 ? -7.215  -6.679  12.681  1.00 12.29 ? 121 HIS A ND1 1 
ATOM   3056 C  CD2 . HIS B 1 121 ? -8.008  -8.688  12.366  1.00 8.88  ? 121 HIS A CD2 1 
ATOM   3057 C  CE1 . HIS B 1 121 ? -6.255  -7.411  12.115  1.00 10.96 ? 121 HIS A CE1 1 
ATOM   3058 N  NE2 . HIS B 1 121 ? -6.731  -8.616  11.875  1.00 10.93 ? 121 HIS A NE2 1 
ATOM   3059 N  N   . VAL B 1 122 ? -12.249 -8.393  14.984  1.00 9.73  ? 122 VAL A N   1 
ATOM   3060 C  CA  . VAL B 1 122 ? -13.311 -8.207  15.926  1.00 11.45 ? 122 VAL A CA  1 
ATOM   3061 C  C   . VAL B 1 122 ? -12.614 -8.059  17.290  1.00 11.11 ? 122 VAL A C   1 
ATOM   3062 O  O   . VAL B 1 122 ? -11.986 -9.013  17.766  1.00 10.75 ? 122 VAL A O   1 
ATOM   3063 C  CB  . VAL B 1 122 ? -14.317 -9.457  15.964  1.00 10.24 ? 122 VAL A CB  1 
ATOM   3064 C  CG1 . VAL B 1 122 ? -15.480 -9.179  16.934  1.00 11.95 ? 122 VAL A CG1 1 
ATOM   3065 C  CG2 . VAL B 1 122 ? -14.862 -9.828  14.511  1.00 11.72 ? 122 VAL A CG2 1 
ATOM   3066 N  N   . VAL B 1 123 ? -12.764 -6.899  17.921  1.00 9.55  ? 123 VAL A N   1 
ATOM   3067 C  CA  . VAL B 1 123 ? -11.941 -6.506  19.086  1.00 9.66  ? 123 VAL A CA  1 
ATOM   3068 C  C   . VAL B 1 123 ? -12.813 -6.691  20.357  1.00 9.61  ? 123 VAL A C   1 
ATOM   3069 O  O   . VAL B 1 123 ? -13.975 -6.282  20.384  1.00 10.53 ? 123 VAL A O   1 
ATOM   3070 C  CB  . VAL B 1 123 ? -11.481 -5.018  19.033  1.00 10.81 ? 123 VAL A CB  1 
ATOM   3071 C  CG1 . VAL B 1 123 ? -10.598 -4.697  20.293  1.00 9.84  ? 123 VAL A CG1 1 
ATOM   3072 C  CG2 . VAL B 1 123 ? -10.582 -4.717  17.770  1.00 9.04  ? 123 VAL A CG2 1 
ATOM   3073 N  N   . HIS B 1 124 ? -12.269 -7.372  21.351  1.00 11.54 ? 124 HIS A N   1 
ATOM   3074 C  CA  . HIS B 1 124 ? -12.994 -7.666  22.612  1.00 11.57 ? 124 HIS A CA  1 
ATOM   3075 C  C   . HIS B 1 124 ? -12.094 -7.337  23.788  1.00 10.78 ? 124 HIS A C   1 
ATOM   3076 O  O   . HIS B 1 124 ? -10.891 -7.340  23.690  1.00 13.09 ? 124 HIS A O   1 
ATOM   3077 C  CB  . HIS B 1 124 ? -13.276 -9.161  22.749  1.00 11.40 ? 124 HIS A CB  1 
ATOM   3078 C  CG  . HIS B 1 124 ? -13.935 -9.774  21.555  1.00 13.70 ? 124 HIS A CG  1 
ATOM   3079 N  ND1 . HIS B 1 124 ? -13.241 -10.119 20.419  1.00 13.27 ? 124 HIS A ND1 1 
ATOM   3080 C  CD2 . HIS B 1 124 ? -15.206 -10.189 21.361  1.00 15.28 ? 124 HIS A CD2 1 
ATOM   3081 C  CE1 . HIS B 1 124 ? -14.048 -10.737 19.588  1.00 13.97 ? 124 HIS A CE1 1 
ATOM   3082 N  NE2 . HIS B 1 124 ? -15.254 -10.770 20.125  1.00 13.22 ? 124 HIS A NE2 1 
ATOM   3083 N  N   . TRP B 1 125 ? -12.676 -7.110  24.962  1.00 12.68 ? 125 TRP A N   1 
ATOM   3084 C  CA  . TRP B 1 125 ? -11.844 -6.890  26.128  1.00 12.58 ? 125 TRP A CA  1 
ATOM   3085 C  C   . TRP B 1 125 ? -12.374 -7.647  27.364  1.00 11.81 ? 125 TRP A C   1 
ATOM   3086 O  O   . TRP B 1 125 ? -13.544 -7.790  27.531  1.00 12.78 ? 125 TRP A O   1 
ATOM   3087 C  CB  . TRP B 1 125 ? -11.673 -5.390  26.449  1.00 10.49 ? 125 TRP A CB  1 
ATOM   3088 C  CG  . TRP B 1 125 ? -12.990 -4.697  26.703  1.00 13.78 ? 125 TRP A CG  1 
ATOM   3089 C  CD1 . TRP B 1 125 ? -13.851 -4.211  25.744  1.00 11.91 ? 125 TRP A CD1 1 
ATOM   3090 C  CD2 . TRP B 1 125 ? -13.577 -4.376  27.983  1.00 10.48 ? 125 TRP A CD2 1 
ATOM   3091 N  NE1 . TRP B 1 125 ? -14.948 -3.629  26.349  1.00 17.76 ? 125 TRP A NE1 1 
ATOM   3092 C  CE2 . TRP B 1 125 ? -14.796 -3.706  27.723  1.00 15.70 ? 125 TRP A CE2 1 
ATOM   3093 C  CE3 . TRP B 1 125 ? -13.145 -4.522  29.322  1.00 11.12 ? 125 TRP A CE3 1 
ATOM   3094 C  CZ2 . TRP B 1 125 ? -15.641 -3.236  28.753  1.00 15.69 ? 125 TRP A CZ2 1 
ATOM   3095 C  CZ3 . TRP B 1 125 ? -13.989 -4.026  30.368  1.00 13.50 ? 125 TRP A CZ3 1 
ATOM   3096 C  CH2 . TRP B 1 125 ? -15.226 -3.416  30.073  1.00 15.64 ? 125 TRP A CH2 1 
ATOM   3097 N  N   . ASN B 1 126 ? -11.450 -7.987  28.248  1.00 14.37 ? 126 ASN A N   1 
ATOM   3098 C  CA  . ASN B 1 126 ? -11.635 -8.838  29.422  1.00 13.84 ? 126 ASN A CA  1 
ATOM   3099 C  C   . ASN B 1 126 ? -12.327 -8.053  30.541  1.00 13.41 ? 126 ASN A C   1 
ATOM   3100 O  O   . ASN B 1 126 ? -11.672 -7.385  31.371  1.00 12.88 ? 126 ASN A O   1 
ATOM   3101 C  CB  . ASN B 1 126 ? -10.265 -9.359  29.895  1.00 14.31 ? 126 ASN A CB  1 
ATOM   3102 C  CG  . ASN B 1 126 ? -10.401 -10.454 30.975  1.00 15.89 ? 126 ASN A CG  1 
ATOM   3103 O  OD1 . ASN B 1 126 ? -11.482 -10.629 31.553  1.00 16.49 ? 126 ASN A OD1 1 
ATOM   3104 N  ND2 . ASN B 1 126 ? -9.342  -11.203 31.196  1.00 12.51 ? 126 ASN A ND2 1 
ATOM   3105 N  N   . SER B 1 127 ? -13.666 -8.104  30.576  1.00 15.67 ? 127 SER A N   1 
ATOM   3106 C  CA  . SER B 1 127 ? -14.392 -7.379  31.644  1.00 15.07 ? 127 SER A CA  1 
ATOM   3107 C  C   . SER B 1 127 ? -14.516 -8.230  32.928  1.00 16.51 ? 127 SER A C   1 
ATOM   3108 O  O   . SER B 1 127 ? -14.962 -7.742  33.948  1.00 14.85 ? 127 SER A O   1 
ATOM   3109 C  CB  . SER B 1 127 ? -15.767 -6.950  31.168  1.00 14.14 ? 127 SER A CB  1 
ATOM   3110 O  OG  . SER B 1 127 ? -16.476 -8.086  30.804  1.00 18.13 ? 127 SER A OG  1 
ATOM   3111 N  N   . ASP B 1 128 ? -14.069 -9.491  32.866  1.00 17.12 ? 128 ASP A N   1 
ATOM   3112 C  CA  . ASP B 1 128 ? -13.973 -10.303 34.083  1.00 18.13 ? 128 ASP A CA  1 
ATOM   3113 C  C   . ASP B 1 128 ? -12.835 -9.822  34.958  1.00 19.00 ? 128 ASP A C   1 
ATOM   3114 O  O   . ASP B 1 128 ? -12.835 -10.081 36.167  1.00 18.93 ? 128 ASP A O   1 
ATOM   3115 C  CB  . ASP B 1 128 ? -13.743 -11.781 33.751  1.00 18.33 ? 128 ASP A CB  1 
ATOM   3116 C  CG  . ASP B 1 128 ? -14.985 -12.471 33.280  1.00 18.46 ? 128 ASP A CG  1 
ATOM   3117 O  OD1 . ASP B 1 128 ? -14.881 -13.664 32.902  1.00 17.74 ? 128 ASP A OD1 1 
ATOM   3118 O  OD2 . ASP B 1 128 ? -16.042 -11.802 33.237  1.00 21.10 ? 128 ASP A OD2 1 
ATOM   3119 N  N   . LYS B 1 129 ? -11.817 -9.177  34.361  1.00 17.90 ? 129 LYS A N   1 
ATOM   3120 C  CA  . LYS B 1 129 ? -10.671 -8.787  35.124  1.00 17.58 ? 129 LYS A CA  1 
ATOM   3121 C  C   . LYS B 1 129 ? -10.524 -7.314  35.162  1.00 17.36 ? 129 LYS A C   1 
ATOM   3122 O  O   . LYS B 1 129 ? -9.860  -6.800  36.108  1.00 16.68 ? 129 LYS A O   1 
ATOM   3123 C  CB  . LYS B 1 129 ? -9.358  -9.435  34.641  1.00 18.38 ? 129 LYS A CB  1 
ATOM   3124 C  CG  . LYS B 1 129 ? -9.165  -10.832 35.115  1.00 21.82 ? 129 LYS A CG  1 
ATOM   3125 C  CD  . LYS B 1 129 ? -7.729  -11.287 34.868  1.00 28.27 ? 129 LYS A CD  1 
ATOM   3126 C  CE  . LYS B 1 129 ? -6.638  -10.499 35.613  1.00 25.34 ? 129 LYS A CE  1 
ATOM   3127 N  NZ  . LYS B 1 129 ? -5.278  -11.012 35.176  1.00 25.52 ? 129 LYS A NZ  1 
ATOM   3128 N  N   . TYR B 1 130 ? -11.057 -6.621  34.120  1.00 16.03 ? 130 TYR A N   1 
ATOM   3129 C  CA  . TYR B 1 130 ? -10.833 -5.171  33.968  1.00 17.07 ? 130 TYR A CA  1 
ATOM   3130 C  C   . TYR B 1 130 ? -12.134 -4.355  33.938  1.00 16.47 ? 130 TYR A C   1 
ATOM   3131 O  O   . TYR B 1 130 ? -13.179 -4.815  33.484  1.00 17.36 ? 130 TYR A O   1 
ATOM   3132 C  CB  . TYR B 1 130 ? -9.863  -4.787  32.792  1.00 16.37 ? 130 TYR A CB  1 
ATOM   3133 C  CG  . TYR B 1 130 ? -8.602  -5.577  32.917  1.00 16.98 ? 130 TYR A CG  1 
ATOM   3134 C  CD1 . TYR B 1 130 ? -7.652  -5.241  33.904  1.00 18.13 ? 130 TYR A CD1 1 
ATOM   3135 C  CD2 . TYR B 1 130 ? -8.395  -6.760  32.147  1.00 16.33 ? 130 TYR A CD2 1 
ATOM   3136 C  CE1 . TYR B 1 130 ? -6.522  -6.050  34.108  1.00 21.00 ? 130 TYR A CE1 1 
ATOM   3137 C  CE2 . TYR B 1 130 ? -7.268  -7.555  32.320  1.00 15.70 ? 130 TYR A CE2 1 
ATOM   3138 C  CZ  . TYR B 1 130 ? -6.318  -7.172  33.286  1.00 16.74 ? 130 TYR A CZ  1 
ATOM   3139 O  OH  . TYR B 1 130 ? -5.218  -7.925  33.466  1.00 17.81 ? 130 TYR A OH  1 
ATOM   3140 N  N   . PRO B 1 131 ? -12.085 -3.161  34.494  1.00 17.20 ? 131 PRO A N   1 
ATOM   3141 C  CA  . PRO B 1 131 ? -13.289 -2.342  34.611  1.00 16.92 ? 131 PRO A CA  1 
ATOM   3142 C  C   . PRO B 1 131 ? -13.654 -1.671  33.264  1.00 17.70 ? 131 PRO A C   1 
ATOM   3143 O  O   . PRO B 1 131 ? -14.767 -1.204  33.102  1.00 18.28 ? 131 PRO A O   1 
ATOM   3144 C  CB  . PRO B 1 131 ? -12.850 -1.288  35.622  1.00 17.36 ? 131 PRO A CB  1 
ATOM   3145 C  CG  . PRO B 1 131 ? -11.460 -1.136  35.408  1.00 15.12 ? 131 PRO A CG  1 
ATOM   3146 C  CD  . PRO B 1 131 ? -10.923 -2.502  35.115  1.00 17.65 ? 131 PRO A CD  1 
ATOM   3147 N  N   . SER B 1 132 ? -12.693 -1.568  32.341  1.00 17.43 ? 132 SER A N   1 
ATOM   3148 C  CA  . SER B 1 132 ? -12.929 -0.842  31.076  1.00 16.44 ? 132 SER A CA  1 
ATOM   3149 C  C   . SER B 1 132 ? -11.932 -1.317  30.005  1.00 16.20 ? 132 SER A C   1 
ATOM   3150 O  O   . SER B 1 132 ? -10.866 -1.898  30.318  1.00 12.33 ? 132 SER A O   1 
ATOM   3151 C  CB  . SER B 1 132 ? -12.706 0.640   31.260  1.00 15.68 ? 132 SER A CB  1 
ATOM   3152 O  OG  . SER B 1 132 ? -11.313 0.880   31.442  1.00 19.67 ? 132 SER A OG  1 
ATOM   3153 N  N   . PHE B 1 133 ? -12.320 -1.063  28.760  1.00 16.42 ? 133 PHE A N   1 
ATOM   3154 C  CA  . PHE B 1 133 ? -11.458 -1.298  27.610  1.00 17.11 ? 133 PHE A CA  1 
ATOM   3155 C  C   . PHE B 1 133 ? -10.104 -0.700  27.754  1.00 17.84 ? 133 PHE A C   1 
ATOM   3156 O  O   . PHE B 1 133 ? -9.108  -1.417  27.553  1.00 18.11 ? 133 PHE A O   1 
ATOM   3157 C  CB  . PHE B 1 133 ? -12.143 -0.810  26.322  1.00 17.06 ? 133 PHE A CB  1 
ATOM   3158 C  CG  . PHE B 1 133 ? -11.273 -0.906  25.122  1.00 17.34 ? 133 PHE A CG  1 
ATOM   3159 C  CD1 . PHE B 1 133 ? -10.990 -2.129  24.593  1.00 13.51 ? 133 PHE A CD1 1 
ATOM   3160 C  CD2 . PHE B 1 133 ? -10.724 0.249   24.551  1.00 20.16 ? 133 PHE A CD2 1 
ATOM   3161 C  CE1 . PHE B 1 133 ? -10.188 -2.224  23.455  1.00 21.30 ? 133 PHE A CE1 1 
ATOM   3162 C  CE2 . PHE B 1 133 ? -9.868  0.184   23.430  1.00 20.54 ? 133 PHE A CE2 1 
ATOM   3163 C  CZ  . PHE B 1 133 ? -9.614  -1.074  22.870  1.00 18.57 ? 133 PHE A CZ  1 
ATOM   3164 N  N   . VAL B 1 134 ? -10.038 0.600   28.105  1.00 19.60 ? 134 VAL A N   1 
ATOM   3165 C  CA  . VAL B 1 134 ? -8.770  1.326   28.308  1.00 20.92 ? 134 VAL A CA  1 
ATOM   3166 C  C   . VAL B 1 134 ? -7.842  0.627   29.305  1.00 20.09 ? 134 VAL A C   1 
ATOM   3167 O  O   . VAL B 1 134 ? -6.669  0.390   29.051  1.00 20.34 ? 134 VAL A O   1 
ATOM   3168 C  CB  . VAL B 1 134 ? -9.028  2.828   28.784  1.00 21.57 ? 134 VAL A CB  1 
ATOM   3169 C  CG1 . VAL B 1 134 ? -7.684  3.535   28.974  1.00 26.36 ? 134 VAL A CG1 1 
ATOM   3170 C  CG2 . VAL B 1 134 ? -9.828  3.590   27.734  1.00 26.16 ? 134 VAL A CG2 1 
ATOM   3171 N  N   . GLU B 1 135 ? -8.391  0.191   30.429  1.00 19.76 ? 135 GLU A N   1 
ATOM   3172 C  CA  . GLU B 1 135 ? -7.562  -0.556  31.369  1.00 20.04 ? 135 GLU A CA  1 
ATOM   3173 C  C   . GLU B 1 135 ? -7.110  -1.907  30.829  1.00 18.89 ? 135 GLU A C   1 
ATOM   3174 O  O   . GLU B 1 135 ? -5.938  -2.293  31.003  1.00 18.05 ? 135 GLU A O   1 
ATOM   3175 C  CB  . GLU B 1 135 ? -8.295  -0.764  32.707  1.00 19.89 ? 135 GLU A CB  1 
ATOM   3176 C  CG  . GLU B 1 135 ? -8.579  0.551   33.464  1.00 23.29 ? 135 GLU A CG  1 
ATOM   3177 C  CD  . GLU B 1 135 ? -7.305  1.182   34.030  1.00 22.65 ? 135 GLU A CD  1 
ATOM   3178 O  OE1 . GLU B 1 135 ? -6.226  0.539   33.960  1.00 24.36 ? 135 GLU A OE1 1 
ATOM   3179 O  OE2 . GLU B 1 135 ? -7.399  2.295   34.575  1.00 27.29 ? 135 GLU A OE2 1 
ATOM   3180 N  N   . ALA B 1 136 ? -8.030  -2.582  30.142  1.00 16.03 ? 136 ALA A N   1 
ATOM   3181 C  CA  . ALA B 1 136 ? -7.801  -3.922  29.598  1.00 14.80 ? 136 ALA A CA  1 
ATOM   3182 C  C   . ALA B 1 136 ? -6.690  -3.872  28.505  1.00 15.93 ? 136 ALA A C   1 
ATOM   3183 O  O   . ALA B 1 136 ? -5.789  -4.763  28.415  1.00 14.67 ? 136 ALA A O   1 
ATOM   3184 C  CB  . ALA B 1 136 ? -9.134  -4.505  29.033  1.00 13.00 ? 136 ALA A CB  1 
ATOM   3185 N  N   . ALA B 1 137 ? -6.737  -2.797  27.729  1.00 16.96 ? 137 ALA A N   1 
ATOM   3186 C  CA  . ALA B 1 137 ? -5.795  -2.555  26.605  1.00 18.03 ? 137 ALA A CA  1 
ATOM   3187 C  C   . ALA B 1 137 ? -4.340  -2.550  26.976  1.00 19.45 ? 137 ALA A C   1 
ATOM   3188 O  O   . ALA B 1 137 ? -3.502  -2.654  26.081  1.00 20.91 ? 137 ALA A O   1 
ATOM   3189 C  CB  . ALA B 1 137 ? -6.143  -1.239  25.886  1.00 16.03 ? 137 ALA A CB  1 
ATOM   3190 N  N   . HIS B 1 138 ? -4.022  -2.413  28.269  1.00 21.64 ? 138 HIS A N   1 
ATOM   3191 C  CA  . HIS B 1 138 ? -2.625  -2.279  28.763  1.00 21.48 ? 138 HIS A CA  1 
ATOM   3192 C  C   . HIS B 1 138 ? -2.188  -3.459  29.609  1.00 20.71 ? 138 HIS A C   1 
ATOM   3193 O  O   . HIS B 1 138 ? -1.226  -3.353  30.378  1.00 21.13 ? 138 HIS A O   1 
ATOM   3194 C  CB  . HIS B 1 138 ? -2.458  -0.988  29.600  1.00 23.43 ? 138 HIS A CB  1 
ATOM   3195 C  CG  . HIS B 1 138 ? -2.664  0.271   28.812  1.00 24.26 ? 138 HIS A CG  1 
ATOM   3196 N  ND1 . HIS B 1 138 ? -1.622  0.994   28.280  1.00 29.28 ? 138 HIS A ND1 1 
ATOM   3197 C  CD2 . HIS B 1 138 ? -3.799  0.933   28.467  1.00 28.56 ? 138 HIS A CD2 1 
ATOM   3198 C  CE1 . HIS B 1 138 ? -2.105  2.039   27.629  1.00 28.28 ? 138 HIS A CE1 1 
ATOM   3199 N  NE2 . HIS B 1 138 ? -3.422  2.032   27.739  1.00 25.98 ? 138 HIS A NE2 1 
ATOM   3200 N  N   A GLU B 1 139 ? -2.905  -4.578  29.511  0.50 19.50 ? 139 GLU A N   1 
ATOM   3201 N  N   B GLU B 1 139 ? -2.874  -4.588  29.446  0.50 19.59 ? 139 GLU A N   1 
ATOM   3202 C  CA  A GLU B 1 139 ? -2.487  -5.794  30.176  0.50 18.36 ? 139 GLU A CA  1 
ATOM   3203 C  CA  B GLU B 1 139 ? -2.584  -5.787  30.190  0.50 18.51 ? 139 GLU A CA  1 
ATOM   3204 C  C   A GLU B 1 139 ? -2.438  -6.960  29.193  0.50 18.27 ? 139 GLU A C   1 
ATOM   3205 C  C   B GLU B 1 139 ? -2.475  -6.977  29.204  0.50 18.36 ? 139 GLU A C   1 
ATOM   3206 O  O   A GLU B 1 139 ? -3.264  -7.042  28.281  0.50 16.90 ? 139 GLU A O   1 
ATOM   3207 O  O   B GLU B 1 139 ? -3.294  -7.083  28.286  0.50 17.04 ? 139 GLU A O   1 
ATOM   3208 C  CB  A GLU B 1 139 ? -3.420  -6.162  31.346  0.50 19.07 ? 139 GLU A CB  1 
ATOM   3209 C  CB  B GLU B 1 139 ? -3.713  -6.040  31.211  0.50 19.15 ? 139 GLU A CB  1 
ATOM   3210 C  CG  A GLU B 1 139 ? -3.358  -5.253  32.558  0.50 18.60 ? 139 GLU A CG  1 
ATOM   3211 C  CG  B GLU B 1 139 ? -4.074  -4.853  32.156  0.50 19.51 ? 139 GLU A CG  1 
ATOM   3212 C  CD  A GLU B 1 139 ? -1.946  -4.844  32.964  0.50 20.74 ? 139 GLU A CD  1 
ATOM   3213 C  CD  B GLU B 1 139 ? -3.421  -4.949  33.562  0.50 25.74 ? 139 GLU A CD  1 
ATOM   3214 O  OE1 A GLU B 1 139 ? -1.110  -5.729  33.222  0.50 20.80 ? 139 GLU A OE1 1 
ATOM   3215 O  OE1 B GLU B 1 139 ? -3.814  -4.180  34.502  0.50 26.18 ? 139 GLU A OE1 1 
ATOM   3216 O  OE2 A GLU B 1 139 ? -1.680  -3.623  33.023  0.50 23.26 ? 139 GLU A OE2 1 
ATOM   3217 O  OE2 B GLU B 1 139 ? -2.519  -5.785  33.727  0.50 26.34 ? 139 GLU A OE2 1 
ATOM   3218 N  N   . PRO B 1 140 ? -1.495  -7.889  29.412  1.00 18.02 ? 140 PRO A N   1 
ATOM   3219 C  CA  . PRO B 1 140 ? -1.267  -9.010  28.422  1.00 18.27 ? 140 PRO A CA  1 
ATOM   3220 C  C   . PRO B 1 140 ? -2.458  -9.886  28.156  1.00 17.74 ? 140 PRO A C   1 
ATOM   3221 O  O   . PRO B 1 140 ? -2.592  -10.424 27.075  1.00 18.09 ? 140 PRO A O   1 
ATOM   3222 C  CB  . PRO B 1 140 ? -0.129  -9.834  29.047  1.00 17.56 ? 140 PRO A CB  1 
ATOM   3223 C  CG  . PRO B 1 140 ? 0.572   -8.837  29.970  1.00 18.06 ? 140 PRO A CG  1 
ATOM   3224 C  CD  . PRO B 1 140 ? -0.550  -7.970  30.546  1.00 18.50 ? 140 PRO A CD  1 
ATOM   3225 N  N   . ASP B 1 141 ? -3.294  -10.063 29.169  1.00 17.00 ? 141 ASP A N   1 
ATOM   3226 C  CA  . ASP B 1 141 ? -4.510  -10.834 29.048  1.00 16.54 ? 141 ASP A CA  1 
ATOM   3227 C  C   . ASP B 1 141 ? -5.803  -9.956  28.862  1.00 14.75 ? 141 ASP A C   1 
ATOM   3228 O  O   . ASP B 1 141 ? -6.947  -10.459 29.025  1.00 16.38 ? 141 ASP A O   1 
ATOM   3229 C  CB  . ASP B 1 141 ? -4.674  -11.679 30.304  1.00 16.58 ? 141 ASP A CB  1 
ATOM   3230 C  CG  . ASP B 1 141 ? -4.959  -10.823 31.575  1.00 17.77 ? 141 ASP A CG  1 
ATOM   3231 O  OD1 . ASP B 1 141 ? -4.701  -9.579  31.661  1.00 19.39 ? 141 ASP A OD1 1 
ATOM   3232 O  OD2 . ASP B 1 141 ? -5.419  -11.438 32.525  1.00 22.57 ? 141 ASP A OD2 1 
ATOM   3233 N  N   . GLY B 1 142 ? -5.608  -8.684  28.558  1.00 15.29 ? 142 GLY A N   1 
ATOM   3234 C  CA  . GLY B 1 142 ? -6.710  -7.715  28.477  1.00 14.94 ? 142 GLY A CA  1 
ATOM   3235 C  C   . GLY B 1 142 ? -7.611  -7.764  27.233  1.00 13.61 ? 142 GLY A C   1 
ATOM   3236 O  O   . GLY B 1 142 ? -8.807  -7.557  27.337  1.00 13.96 ? 142 GLY A O   1 
ATOM   3237 N  N   . LEU B 1 143 ? -7.014  -7.931  26.051  1.00 13.90 ? 143 LEU A N   1 
ATOM   3238 C  CA  . LEU B 1 143 ? -7.734  -7.943  24.764  1.00 12.77 ? 143 LEU A CA  1 
ATOM   3239 C  C   . LEU B 1 143 ? -7.756  -9.321  24.081  1.00 12.77 ? 143 LEU A C   1 
ATOM   3240 O  O   . LEU B 1 143 ? -6.806  -10.133 24.201  1.00 13.79 ? 143 LEU A O   1 
ATOM   3241 C  CB  . LEU B 1 143 ? -7.159  -6.867  23.770  1.00 13.45 ? 143 LEU A CB  1 
ATOM   3242 C  CG  . LEU B 1 143 ? -7.096  -5.434  24.329  1.00 14.58 ? 143 LEU A CG  1 
ATOM   3243 C  CD1 . LEU B 1 143 ? -6.499  -4.407  23.327  1.00 17.93 ? 143 LEU A CD1 1 
ATOM   3244 C  CD2 . LEU B 1 143 ? -8.513  -4.948  24.822  1.00 11.09 ? 143 LEU A CD2 1 
ATOM   3245 N  N   . ALA B 1 144 ? -8.812  -9.573  23.285  1.00 14.07 ? 144 ALA A N   1 
ATOM   3246 C  CA  . ALA B 1 144 ? -8.745  -10.676 22.330  1.00 12.42 ? 144 ALA A CA  1 
ATOM   3247 C  C   . ALA B 1 144 ? -9.308  -10.165 21.030  1.00 12.66 ? 144 ALA A C   1 
ATOM   3248 O  O   . ALA B 1 144 ? -10.364 -9.502  21.012  1.00 11.92 ? 144 ALA A O   1 
ATOM   3249 C  CB  . ALA B 1 144 ? -9.610  -11.887 22.800  1.00 12.83 ? 144 ALA A CB  1 
ATOM   3250 N  N   . VAL B 1 145 ? -8.587  -10.470 19.961  1.00 12.20 ? 145 VAL A N   1 
ATOM   3251 C  CA  . VAL B 1 145 ? -8.991  -10.044 18.623  1.00 11.48 ? 145 VAL A CA  1 
ATOM   3252 C  C   . VAL B 1 145 ? -9.228  -11.280 17.795  1.00 11.55 ? 145 VAL A C   1 
ATOM   3253 O  O   . VAL B 1 145 ? -8.369  -12.138 17.733  1.00 12.32 ? 145 VAL A O   1 
ATOM   3254 C  CB  . VAL B 1 145 ? -8.004  -9.064  17.938  1.00 11.59 ? 145 VAL A CB  1 
ATOM   3255 C  CG1 . VAL B 1 145 ? -8.601  -8.661  16.578  1.00 9.27  ? 145 VAL A CG1 1 
ATOM   3256 C  CG2 . VAL B 1 145 ? -7.856  -7.747  18.793  1.00 12.55 ? 145 VAL A CG2 1 
ATOM   3257 N  N   . LEU B 1 146 ? -10.433 -11.365 17.216  1.00 11.41 ? 146 LEU A N   1 
ATOM   3258 C  CA  . LEU B 1 146 ? -10.794 -12.420 16.316  1.00 11.65 ? 146 LEU A CA  1 
ATOM   3259 C  C   . LEU B 1 146 ? -10.523 -11.910 14.894  1.00 12.75 ? 146 LEU A C   1 
ATOM   3260 O  O   . LEU B 1 146 ? -11.002 -10.831 14.482  1.00 12.53 ? 146 LEU A O   1 
ATOM   3261 C  CB  . LEU B 1 146 ? -12.281 -12.766 16.472  1.00 11.96 ? 146 LEU A CB  1 
ATOM   3262 C  CG  . LEU B 1 146 ? -12.887 -13.917 15.601  1.00 15.41 ? 146 LEU A CG  1 
ATOM   3263 C  CD1 . LEU B 1 146 ? -12.095 -15.314 15.874  1.00 14.74 ? 146 LEU A CD1 1 
ATOM   3264 C  CD2 . LEU B 1 146 ? -14.415 -14.027 15.859  1.00 12.86 ? 146 LEU A CD2 1 
ATOM   3265 N  N   . GLY B 1 147 ? -9.728  -12.685 14.166  1.00 12.90 ? 147 GLY A N   1 
ATOM   3266 C  CA  . GLY B 1 147 ? -9.282  -12.296 12.831  1.00 13.44 ? 147 GLY A CA  1 
ATOM   3267 C  C   . GLY B 1 147 ? -10.018 -13.200 11.873  1.00 11.56 ? 147 GLY A C   1 
ATOM   3268 O  O   . GLY B 1 147 ? -10.038 -14.389 12.047  1.00 12.33 ? 147 GLY A O   1 
ATOM   3269 N  N   . VAL B 1 148 ? -10.596 -12.619 10.839  1.00 12.26 ? 148 VAL A N   1 
ATOM   3270 C  CA  . VAL B 1 148 ? -11.276 -13.371 9.820   1.00 12.64 ? 148 VAL A CA  1 
ATOM   3271 C  C   . VAL B 1 148 ? -10.756 -12.918 8.466   1.00 12.76 ? 148 VAL A C   1 
ATOM   3272 O  O   . VAL B 1 148 ? -10.870 -11.737 8.099   1.00 12.28 ? 148 VAL A O   1 
ATOM   3273 C  CB  . VAL B 1 148 ? -12.794 -13.150 9.860   1.00 10.99 ? 148 VAL A CB  1 
ATOM   3274 C  CG1 . VAL B 1 148 ? -13.497 -13.976 8.720   1.00 11.36 ? 148 VAL A CG1 1 
ATOM   3275 C  CG2 . VAL B 1 148 ? -13.360 -13.484 11.278  1.00 14.19 ? 148 VAL A CG2 1 
ATOM   3276 N  N   . PHE B 1 149 ? -10.213 -13.855 7.712   1.00 13.06 ? 149 PHE A N   1 
ATOM   3277 C  CA  . PHE B 1 149 ? -9.774  -13.514 6.346   1.00 14.08 ? 149 PHE A CA  1 
ATOM   3278 C  C   . PHE B 1 149 ? -10.936 -13.302 5.363   1.00 13.57 ? 149 PHE A C   1 
ATOM   3279 O  O   . PHE B 1 149 ? -11.971 -13.978 5.455   1.00 14.55 ? 149 PHE A O   1 
ATOM   3280 C  CB  . PHE B 1 149 ? -8.849  -14.611 5.785   1.00 14.14 ? 149 PHE A CB  1 
ATOM   3281 C  CG  . PHE B 1 149 ? -7.598  -14.815 6.590   1.00 13.06 ? 149 PHE A CG  1 
ATOM   3282 C  CD1 . PHE B 1 149 ? -6.695  -13.734 6.808   1.00 11.23 ? 149 PHE A CD1 1 
ATOM   3283 C  CD2 . PHE B 1 149 ? -7.302  -16.088 7.087   1.00 11.51 ? 149 PHE A CD2 1 
ATOM   3284 C  CE1 . PHE B 1 149 ? -5.486  -13.980 7.496   1.00 7.39  ? 149 PHE A CE1 1 
ATOM   3285 C  CE2 . PHE B 1 149 ? -6.135  -16.351 7.802   1.00 8.16  ? 149 PHE A CE2 1 
ATOM   3286 C  CZ  . PHE B 1 149 ? -5.233  -15.292 8.016   1.00 9.82  ? 149 PHE A CZ  1 
ATOM   3287 N  N   . LEU B 1 150 ? -10.749 -12.382 4.420   1.00 11.28 ? 150 LEU A N   1 
ATOM   3288 C  CA  . LEU B 1 150 ? -11.672 -12.274 3.255   1.00 12.96 ? 150 LEU A CA  1 
ATOM   3289 C  C   . LEU B 1 150 ? -10.991 -12.617 1.971   1.00 13.06 ? 150 LEU A C   1 
ATOM   3290 O  O   . LEU B 1 150 ? -9.874  -12.150 1.712   1.00 13.25 ? 150 LEU A O   1 
ATOM   3291 C  CB  . LEU B 1 150 ? -12.313 -10.871 3.114   1.00 12.25 ? 150 LEU A CB  1 
ATOM   3292 C  CG  . LEU B 1 150 ? -13.420 -10.388 4.079   1.00 14.86 ? 150 LEU A CG  1 
ATOM   3293 C  CD1 . LEU B 1 150 ? -12.840 -10.383 5.462   1.00 14.47 ? 150 LEU A CD1 1 
ATOM   3294 C  CD2 . LEU B 1 150 ? -13.845 -8.885  3.707   1.00 12.12 ? 150 LEU A CD2 1 
ATOM   3295 N  N   . GLN B 1 151 ? -11.637 -13.454 1.155   1.00 12.52 ? 151 GLN A N   1 
ATOM   3296 C  CA  . GLN B 1 151 ? -11.125 -13.671 -0.203  1.00 14.76 ? 151 GLN A CA  1 
ATOM   3297 C  C   . GLN B 1 151 ? -12.156 -13.171 -1.231  1.00 14.58 ? 151 GLN A C   1 
ATOM   3298 O  O   . GLN B 1 151 ? -13.358 -13.064 -0.935  1.00 13.13 ? 151 GLN A O   1 
ATOM   3299 C  CB  . GLN B 1 151 ? -10.814 -15.160 -0.373  1.00 15.55 ? 151 GLN A CB  1 
ATOM   3300 C  CG  . GLN B 1 151 ? -12.033 -15.950 -0.363  1.00 18.15 ? 151 GLN A CG  1 
ATOM   3301 C  CD  . GLN B 1 151 ? -11.783 -17.455 -0.263  1.00 24.95 ? 151 GLN A CD  1 
ATOM   3302 O  OE1 . GLN B 1 151 ? -10.649 -17.935 -0.252  1.00 23.90 ? 151 GLN A OE1 1 
ATOM   3303 N  NE2 . GLN B 1 151 ? -12.873 -18.196 -0.214  1.00 31.63 ? 151 GLN A NE2 1 
ATOM   3304 N  N   . ILE B 1 152 ? -11.686 -12.889 -2.443  1.00 15.74 ? 152 ILE A N   1 
ATOM   3305 C  CA  . ILE B 1 152 ? -12.602 -12.442 -3.487  1.00 16.18 ? 152 ILE A CA  1 
ATOM   3306 C  C   . ILE B 1 152 ? -13.507 -13.652 -3.897  1.00 16.71 ? 152 ILE A C   1 
ATOM   3307 O  O   . ILE B 1 152 ? -13.024 -14.748 -4.131  1.00 17.17 ? 152 ILE A O   1 
ATOM   3308 C  CB  . ILE B 1 152 ? -11.840 -11.757 -4.697  1.00 15.98 ? 152 ILE A CB  1 
ATOM   3309 C  CG1 . ILE B 1 152 ? -10.938 -10.570 -4.220  1.00 13.61 ? 152 ILE A CG1 1 
ATOM   3310 C  CG2 . ILE B 1 152 ? -12.824 -11.397 -5.904  1.00 16.52 ? 152 ILE A CG2 1 
ATOM   3311 C  CD1 . ILE B 1 152 ? -11.642 -9.508  -3.367  1.00 8.59  ? 152 ILE A CD1 1 
ATOM   3312 N  N   . GLY B 1 153 ? -14.809 -13.418 -3.961  1.00 16.88 ? 153 GLY A N   1 
ATOM   3313 C  CA  . GLY B 1 153 ? -15.733 -14.414 -4.470  1.00 16.83 ? 153 GLY A CA  1 
ATOM   3314 C  C   . GLY B 1 153 ? -17.045 -13.730 -4.641  1.00 17.99 ? 153 GLY A C   1 
ATOM   3315 O  O   . GLY B 1 153 ? -17.073 -12.560 -5.044  1.00 17.06 ? 153 GLY A O   1 
ATOM   3316 N  N   . GLU B 1 154 ? -18.143 -14.425 -4.308  1.00 18.70 ? 154 GLU A N   1 
ATOM   3317 C  CA  . GLU B 1 154 ? -19.461 -13.793 -4.357  1.00 20.47 ? 154 GLU A CA  1 
ATOM   3318 C  C   . GLU B 1 154 ? -19.602 -12.570 -3.442  1.00 18.81 ? 154 GLU A C   1 
ATOM   3319 O  O   . GLU B 1 154 ? -18.992 -12.532 -2.343  1.00 20.18 ? 154 GLU A O   1 
ATOM   3320 C  CB  . GLU B 1 154 ? -20.532 -14.797 -3.973  1.00 20.76 ? 154 GLU A CB  1 
ATOM   3321 C  CG  . GLU B 1 154 ? -20.631 -15.955 -4.999  1.00 25.88 ? 154 GLU A CG  1 
ATOM   3322 C  CD  . GLU B 1 154 ? -21.774 -16.920 -4.674  1.00 28.25 ? 154 GLU A CD  1 
ATOM   3323 O  OE1 . GLU B 1 154 ? -22.946 -16.420 -4.473  1.00 37.18 ? 154 GLU A OE1 1 
ATOM   3324 O  OE2 . GLU B 1 154 ? -21.515 -18.170 -4.615  1.00 36.29 ? 154 GLU A OE2 1 
ATOM   3325 N  N   . PRO B 1 155 ? -20.423 -11.579 -3.861  1.00 16.70 ? 155 PRO A N   1 
ATOM   3326 C  CA  . PRO B 1 155 ? -20.726 -10.451 -2.958  1.00 15.43 ? 155 PRO A CA  1 
ATOM   3327 C  C   . PRO B 1 155 ? -21.289 -11.059 -1.649  1.00 14.83 ? 155 PRO A C   1 
ATOM   3328 O  O   . PRO B 1 155 ? -21.911 -12.100 -1.634  1.00 13.98 ? 155 PRO A O   1 
ATOM   3329 C  CB  . PRO B 1 155 ? -21.822 -9.622  -3.672  1.00 15.18 ? 155 PRO A CB  1 
ATOM   3330 C  CG  . PRO B 1 155 ? -21.916 -10.192 -5.089  1.00 18.02 ? 155 PRO A CG  1 
ATOM   3331 C  CD  . PRO B 1 155 ? -21.178 -11.544 -5.135  1.00 16.28 ? 155 PRO A CD  1 
ATOM   3332 N  N   . ASN B 1 156 ? -21.048 -10.357 -0.569  1.00 15.63 ? 156 ASN A N   1 
ATOM   3333 C  CA  . ASN B 1 156 ? -21.418 -10.781 0.768   1.00 15.73 ? 156 ASN A CA  1 
ATOM   3334 C  C   . ASN B 1 156 ? -22.510 -9.829  1.168   1.00 14.49 ? 156 ASN A C   1 
ATOM   3335 O  O   . ASN B 1 156 ? -22.265 -8.650  1.255   1.00 13.06 ? 156 ASN A O   1 
ATOM   3336 C  CB  . ASN B 1 156 ? -20.225 -10.617 1.686   1.00 14.29 ? 156 ASN A CB  1 
ATOM   3337 C  CG  . ASN B 1 156 ? -20.447 -11.282 2.978   1.00 19.60 ? 156 ASN A CG  1 
ATOM   3338 O  OD1 . ASN B 1 156 ? -21.468 -11.024 3.631   1.00 17.84 ? 156 ASN A OD1 1 
ATOM   3339 N  ND2 . ASN B 1 156 ? -19.490 -12.165 3.387   1.00 17.32 ? 156 ASN A ND2 1 
ATOM   3340 N  N   . SER B 1 157 ? -23.732 -10.322 1.315   1.00 14.47 ? 157 SER A N   1 
ATOM   3341 C  CA  . SER B 1 157 ? -24.870 -9.461  1.560   1.00 15.90 ? 157 SER A CA  1 
ATOM   3342 C  C   . SER B 1 157 ? -24.748 -8.755  2.907   1.00 16.90 ? 157 SER A C   1 
ATOM   3343 O  O   . SER B 1 157 ? -25.292 -7.674  3.110   1.00 17.28 ? 157 SER A O   1 
ATOM   3344 C  CB  . SER B 1 157 ? -26.194 -10.305 1.556   1.00 18.29 ? 157 SER A CB  1 
ATOM   3345 O  OG  . SER B 1 157 ? -26.132 -11.324 2.562   1.00 19.37 ? 157 SER A OG  1 
ATOM   3346 N  N   . GLN B 1 158 ? -24.066 -9.369  3.859   1.00 16.19 ? 158 GLN A N   1 
ATOM   3347 C  CA  . GLN B 1 158 ? -23.838 -8.656  5.132   1.00 18.16 ? 158 GLN A CA  1 
ATOM   3348 C  C   . GLN B 1 158 ? -22.793 -7.525  5.048   1.00 19.08 ? 158 GLN A C   1 
ATOM   3349 O  O   . GLN B 1 158 ? -22.928 -6.451  5.673   1.00 20.17 ? 158 GLN A O   1 
ATOM   3350 C  CB  . GLN B 1 158 ? -23.434 -9.695  6.156   1.00 17.16 ? 158 GLN A CB  1 
ATOM   3351 C  CG  . GLN B 1 158 ? -24.616 -10.481 6.530   1.00 21.59 ? 158 GLN A CG  1 
ATOM   3352 C  CD  . GLN B 1 158 ? -24.265 -11.468 7.568   1.00 25.59 ? 158 GLN A CD  1 
ATOM   3353 O  OE1 . GLN B 1 158 ? -23.950 -12.615 7.235   1.00 30.20 ? 158 GLN A OE1 1 
ATOM   3354 N  NE2 . GLN B 1 158 ? -24.285 -11.047 8.843   1.00 26.64 ? 158 GLN A NE2 1 
ATOM   3355 N  N   . LEU B 1 159 ? -21.814 -7.708  4.171   1.00 18.17 ? 159 LEU A N   1 
ATOM   3356 C  CA  . LEU B 1 159 ? -20.838 -6.652  3.985   1.00 17.29 ? 159 LEU A CA  1 
ATOM   3357 C  C   . LEU B 1 159 ? -21.405 -5.532  3.148   1.00 17.20 ? 159 LEU A C   1 
ATOM   3358 O  O   . LEU B 1 159 ? -20.893 -4.419  3.210   1.00 17.69 ? 159 LEU A O   1 
ATOM   3359 C  CB  . LEU B 1 159 ? -19.569 -7.199  3.397   1.00 15.60 ? 159 LEU A CB  1 
ATOM   3360 C  CG  . LEU B 1 159 ? -18.845 -8.230  4.290   1.00 17.28 ? 159 LEU A CG  1 
ATOM   3361 C  CD1 . LEU B 1 159 ? -17.634 -8.738  3.549   1.00 16.77 ? 159 LEU A CD1 1 
ATOM   3362 C  CD2 . LEU B 1 159 ? -18.521 -7.625  5.663   1.00 17.67 ? 159 LEU A CD2 1 
ATOM   3363 N  N   . GLN B 1 160 ? -22.474 -5.829  2.396   1.00 17.14 ? 160 GLN A N   1 
ATOM   3364 C  CA  . GLN B 1 160 ? -23.165 -4.789  1.588   1.00 18.22 ? 160 GLN A CA  1 
ATOM   3365 C  C   . GLN B 1 160 ? -23.739 -3.741  2.502   1.00 18.47 ? 160 GLN A C   1 
ATOM   3366 O  O   . GLN B 1 160 ? -23.753 -2.539  2.170   1.00 19.20 ? 160 GLN A O   1 
ATOM   3367 C  CB  . GLN B 1 160 ? -24.220 -5.408  0.645   1.00 18.49 ? 160 GLN A CB  1 
ATOM   3368 C  CG  . GLN B 1 160 ? -24.762 -4.416  -0.390  1.00 21.48 ? 160 GLN A CG  1 
ATOM   3369 C  CD  . GLN B 1 160 ? -23.987 -4.317  -1.675  1.00 26.29 ? 160 GLN A CD  1 
ATOM   3370 O  OE1 . GLN B 1 160 ? -22.905 -4.893  -1.845  1.00 22.89 ? 160 GLN A OE1 1 
ATOM   3371 N  NE2 . GLN B 1 160 ? -24.565 -3.577  -2.630  1.00 28.34 ? 160 GLN A NE2 1 
ATOM   3372 N  N   . LYS B 1 161 ? -24.126 -4.161  3.713   1.00 19.15 ? 161 LYS A N   1 
ATOM   3373 C  CA  . LYS B 1 161 ? -24.627 -3.212  4.689   1.00 20.04 ? 161 LYS A CA  1 
ATOM   3374 C  C   . LYS B 1 161 ? -23.591 -2.138  5.079   1.00 19.85 ? 161 LYS A C   1 
ATOM   3375 O  O   . LYS B 1 161 ? -23.911 -0.942  5.241   1.00 19.37 ? 161 LYS A O   1 
ATOM   3376 C  CB  . LYS B 1 161 ? -25.127 -3.898  5.942   1.00 19.61 ? 161 LYS A CB  1 
ATOM   3377 C  CG  . LYS B 1 161 ? -25.812 -2.852  6.898   1.00 22.15 ? 161 LYS A CG  1 
ATOM   3378 C  CD  . LYS B 1 161 ? -26.397 -3.450  8.250   1.00 24.07 ? 161 LYS A CD  1 
ATOM   3379 C  CE  . LYS B 1 161 ? -27.333 -2.461  8.962   1.00 21.10 ? 161 LYS A CE  1 
ATOM   3380 N  NZ  . LYS B 1 161 ? -28.687 -3.151  9.089   1.00 30.27 ? 161 LYS A NZ  1 
ATOM   3381 N  N   . ILE B 1 162 ? -22.355 -2.583  5.312   1.00 20.10 ? 162 ILE A N   1 
ATOM   3382 C  CA  . ILE B 1 162 ? -21.241 -1.666  5.544   1.00 17.89 ? 162 ILE A CA  1 
ATOM   3383 C  C   . ILE B 1 162 ? -20.858 -0.855  4.308   1.00 17.64 ? 162 ILE A C   1 
ATOM   3384 O  O   . ILE B 1 162 ? -20.723 0.361   4.422   1.00 17.32 ? 162 ILE A O   1 
ATOM   3385 C  CB  . ILE B 1 162 ? -19.973 -2.475  6.051   1.00 18.10 ? 162 ILE A CB  1 
ATOM   3386 C  CG1 . ILE B 1 162 ? -20.305 -3.187  7.377   1.00 14.14 ? 162 ILE A CG1 1 
ATOM   3387 C  CG2 . ILE B 1 162 ? -18.730 -1.553  6.219   1.00 16.49 ? 162 ILE A CG2 1 
ATOM   3388 C  CD1 . ILE B 1 162 ? -19.259 -4.211  7.884   1.00 18.90 ? 162 ILE A CD1 1 
ATOM   3389 N  N   . THR B 1 163 ? -20.666 -1.501  3.152   1.00 17.48 ? 163 THR A N   1 
ATOM   3390 C  CA  . THR B 1 163 ? -20.311 -0.737  1.925   1.00 18.51 ? 163 THR A CA  1 
ATOM   3391 C  C   . THR B 1 163 ? -21.344 0.358   1.581   1.00 18.29 ? 163 THR A C   1 
ATOM   3392 O  O   . THR B 1 163 ? -20.996 1.402   1.090   1.00 17.79 ? 163 THR A O   1 
ATOM   3393 C  CB  . THR B 1 163 ? -19.923 -1.622  0.677   1.00 17.69 ? 163 THR A CB  1 
ATOM   3394 O  OG1 . THR B 1 163 ? -21.030 -2.419  0.226   1.00 21.99 ? 163 THR A OG1 1 
ATOM   3395 C  CG2 . THR B 1 163 ? -18.791 -2.548  0.976   1.00 19.95 ? 163 THR A CG2 1 
ATOM   3396 N  N   . ASP B 1 164 ? -22.601 0.127   1.933   1.00 20.38 ? 164 ASP A N   1 
ATOM   3397 C  CA  . ASP B 1 164 ? -23.688 1.066   1.649   1.00 22.26 ? 164 ASP A CA  1 
ATOM   3398 C  C   . ASP B 1 164 ? -23.553 2.378   2.394   1.00 21.72 ? 164 ASP A C   1 
ATOM   3399 O  O   . ASP B 1 164 ? -24.045 3.435   1.926   1.00 23.21 ? 164 ASP A O   1 
ATOM   3400 C  CB  . ASP B 1 164 ? -25.035 0.378   1.902   1.00 21.10 ? 164 ASP A CB  1 
ATOM   3401 C  CG  . ASP B 1 164 ? -25.470 -0.448  0.728   1.00 26.37 ? 164 ASP A CG  1 
ATOM   3402 O  OD1 . ASP B 1 164 ? -24.829 -0.325  -0.327  1.00 29.24 ? 164 ASP A OD1 1 
ATOM   3403 O  OD2 . ASP B 1 164 ? -26.454 -1.203  0.821   1.00 25.93 ? 164 ASP A OD2 1 
ATOM   3404 N  N   . THR B 1 165 ? -22.826 2.325   3.505   1.00 19.16 ? 165 THR A N   1 
ATOM   3405 C  CA  . THR B 1 165 ? -22.639 3.457   4.393   1.00 18.09 ? 165 THR A CA  1 
ATOM   3406 C  C   . THR B 1 165 ? -21.426 4.282   4.107   1.00 17.64 ? 165 THR A C   1 
ATOM   3407 O  O   . THR B 1 165 ? -21.274 5.344   4.697   1.00 18.55 ? 165 THR A O   1 
ATOM   3408 C  CB  . THR B 1 165 ? -22.509 3.010   5.905   1.00 18.95 ? 165 THR A CB  1 
ATOM   3409 O  OG1 . THR B 1 165 ? -21.200 2.437   6.123   1.00 17.69 ? 165 THR A OG1 1 
ATOM   3410 C  CG2 . THR B 1 165 ? -23.610 2.045   6.288   1.00 19.33 ? 165 THR A CG2 1 
ATOM   3411 N  N   . LEU B 1 166 ? -20.528 3.815   3.238   1.00 17.92 ? 166 LEU A N   1 
ATOM   3412 C  CA  . LEU B 1 166 ? -19.163 4.400   3.110   1.00 17.33 ? 166 LEU A CA  1 
ATOM   3413 C  C   . LEU B 1 166 ? -19.127 5.759   2.486   1.00 18.60 ? 166 LEU A C   1 
ATOM   3414 O  O   . LEU B 1 166 ? -18.332 6.584   2.896   1.00 16.31 ? 166 LEU A O   1 
ATOM   3415 C  CB  . LEU B 1 166 ? -18.193 3.482   2.323   1.00 16.70 ? 166 LEU A CB  1 
ATOM   3416 C  CG  . LEU B 1 166 ? -17.914 2.138   3.015   1.00 17.88 ? 166 LEU A CG  1 
ATOM   3417 C  CD1 . LEU B 1 166 ? -17.099 1.160   2.143   1.00 20.37 ? 166 LEU A CD1 1 
ATOM   3418 C  CD2 . LEU B 1 166 ? -17.306 2.167   4.476   1.00 16.48 ? 166 LEU A CD2 1 
ATOM   3419 N  N   . ASP B 1 167 ? -20.015 5.983   1.518   1.00 20.10 ? 167 ASP A N   1 
ATOM   3420 C  CA  . ASP B 1 167 ? -20.197 7.298   0.907   1.00 22.27 ? 167 ASP A CA  1 
ATOM   3421 C  C   . ASP B 1 167 ? -20.500 8.372   1.992   1.00 22.67 ? 167 ASP A C   1 
ATOM   3422 O  O   . ASP B 1 167 ? -19.895 9.479   1.999   1.00 24.36 ? 167 ASP A O   1 
ATOM   3423 C  CB  . ASP B 1 167 ? -21.298 7.209   -0.174  1.00 22.79 ? 167 ASP A CB  1 
ATOM   3424 C  CG  . ASP B 1 167 ? -20.798 6.586   -1.494  1.00 25.52 ? 167 ASP A CG  1 
ATOM   3425 O  OD1 . ASP B 1 167 ? -19.579 6.326   -1.641  1.00 29.75 ? 167 ASP A OD1 1 
ATOM   3426 O  OD2 . ASP B 1 167 ? -21.639 6.403   -2.412  1.00 29.73 ? 167 ASP A OD2 1 
ATOM   3427 N  N   . SER B 1 168 ? -21.303 8.001   2.989   1.00 21.64 ? 168 SER A N   1 
ATOM   3428 C  CA  . SER B 1 168 ? -21.650 8.877   4.083   1.00 21.15 ? 168 SER A CA  1 
ATOM   3429 C  C   . SER B 1 168 ? -20.528 9.169   5.080   1.00 21.26 ? 168 SER A C   1 
ATOM   3430 O  O   . SER B 1 168 ? -20.621 10.110  5.905   1.00 19.46 ? 168 SER A O   1 
ATOM   3431 C  CB  . SER B 1 168 ? -22.876 8.361   4.836   1.00 23.15 ? 168 SER A CB  1 
ATOM   3432 O  OG  . SER B 1 168 ? -22.513 7.233   5.618   1.00 24.06 ? 168 SER A OG  1 
ATOM   3433 N  N   . ILE B 1 169 ? -19.495 8.319   5.058   1.00 19.01 ? 169 ILE A N   1 
ATOM   3434 C  CA  . ILE B 1 169 ? -18.358 8.517   5.923   1.00 17.39 ? 169 ILE A CA  1 
ATOM   3435 C  C   . ILE B 1 169 ? -17.006 8.646   5.226   1.00 18.14 ? 169 ILE A C   1 
ATOM   3436 O  O   . ILE B 1 169 ? -15.984 8.234   5.774   1.00 15.15 ? 169 ILE A O   1 
ATOM   3437 C  CB  . ILE B 1 169 ? -18.283 7.401   7.076   1.00 17.29 ? 169 ILE A CB  1 
ATOM   3438 C  CG1 . ILE B 1 169 ? -18.079 5.965   6.504   1.00 14.33 ? 169 ILE A CG1 1 
ATOM   3439 C  CG2 . ILE B 1 169 ? -19.498 7.461   7.939   1.00 16.38 ? 169 ILE A CG2 1 
ATOM   3440 C  CD1 . ILE B 1 169 ? -17.564 4.927   7.687   1.00 16.06 ? 169 ILE A CD1 1 
ATOM   3441 N  N   . LYS B 1 170 ? -16.991 9.228   4.042   1.00 18.76 ? 170 LYS A N   1 
ATOM   3442 C  CA  . LYS B 1 170 ? -15.760 9.344   3.258   1.00 22.16 ? 170 LYS A CA  1 
ATOM   3443 C  C   . LYS B 1 170 ? -14.616 10.037  4.024   1.00 21.26 ? 170 LYS A C   1 
ATOM   3444 O  O   . LYS B 1 170 ? -13.452 9.575   4.008   1.00 19.29 ? 170 LYS A O   1 
ATOM   3445 C  CB  . LYS B 1 170 ? -16.012 9.995   1.851   1.00 20.49 ? 170 LYS A CB  1 
ATOM   3446 C  CG  . LYS B 1 170 ? -14.647 10.382  1.180   1.00 26.21 ? 170 LYS A CG  1 
ATOM   3447 C  CD  . LYS B 1 170 ? -14.644 11.065  -0.247  1.00 28.60 ? 170 LYS A CD  1 
ATOM   3448 C  CE  . LYS B 1 170 ? -14.832 10.065  -1.412  1.00 33.76 ? 170 LYS A CE  1 
ATOM   3449 N  NZ  . LYS B 1 170 ? -13.716 9.131   -1.806  1.00 30.76 ? 170 LYS A NZ  1 
ATOM   3450 N  N   . GLU B 1 171 ? -14.945 11.127  4.701   1.00 22.23 ? 171 GLU A N   1 
ATOM   3451 C  CA  . GLU B 1 171 ? -13.934 11.910  5.406   1.00 23.70 ? 171 GLU A CA  1 
ATOM   3452 C  C   . GLU B 1 171 ? -13.632 11.323  6.776   1.00 22.93 ? 171 GLU A C   1 
ATOM   3453 O  O   . GLU B 1 171 ? -14.560 10.900  7.508   1.00 21.57 ? 171 GLU A O   1 
ATOM   3454 C  CB  . GLU B 1 171 ? -14.412 13.359  5.593   1.00 24.66 ? 171 GLU A CB  1 
ATOM   3455 C  CG  . GLU B 1 171 ? -14.621 14.133  4.256   1.00 29.66 ? 171 GLU A CG  1 
ATOM   3456 C  CD  . GLU B 1 171 ? -15.878 13.696  3.476   1.00 35.18 ? 171 GLU A CD  1 
ATOM   3457 O  OE1 . GLU B 1 171 ? -15.837 13.797  2.211   1.00 42.10 ? 171 GLU A OE1 1 
ATOM   3458 O  OE2 . GLU B 1 171 ? -16.884 13.198  4.093   1.00 35.66 ? 171 GLU A OE2 1 
ATOM   3459 N  N   . LYS B 1 172 ? -12.342 11.333  7.119   1.00 21.77 ? 172 LYS A N   1 
ATOM   3460 C  CA  . LYS B 1 172 ? -11.878 10.990  8.440   1.00 22.43 ? 172 LYS A CA  1 
ATOM   3461 C  C   . LYS B 1 172 ? -12.712 11.739  9.493   1.00 22.91 ? 172 LYS A C   1 
ATOM   3462 O  O   . LYS B 1 172 ? -12.971 12.962  9.373   1.00 24.18 ? 172 LYS A O   1 
ATOM   3463 C  CB  . LYS B 1 172 ? -10.386 11.341  8.580   1.00 21.32 ? 172 LYS A CB  1 
ATOM   3464 C  CG  . LYS B 1 172 ? -9.897  11.158  9.975   1.00 21.45 ? 172 LYS A CG  1 
ATOM   3465 C  CD  . LYS B 1 172 ? -8.463  11.544  10.091  1.00 15.71 ? 172 LYS A CD  1 
ATOM   3466 C  CE  . LYS B 1 172 ? -7.946  11.157  11.443  1.00 19.30 ? 172 LYS A CE  1 
ATOM   3467 N  NZ  . LYS B 1 172 ? -6.456  11.150  11.417  1.00 21.89 ? 172 LYS A NZ  1 
ATOM   3468 N  N   . GLY B 1 173 ? -13.180 11.009  10.486  1.00 21.77 ? 173 GLY A N   1 
ATOM   3469 C  CA  . GLY B 1 173 ? -13.995 11.601  11.509  1.00 21.38 ? 173 GLY A CA  1 
ATOM   3470 C  C   . GLY B 1 173 ? -15.476 11.494  11.318  1.00 20.53 ? 173 GLY A C   1 
ATOM   3471 O  O   . GLY B 1 173 ? -16.180 11.650  12.298  1.00 19.90 ? 173 GLY A O   1 
ATOM   3472 N  N   . LYS B 1 174 ? -15.955 11.270  10.084  1.00 18.68 ? 174 LYS A N   1 
ATOM   3473 C  CA  . LYS B 1 174 ? -17.398 11.149  9.805   1.00 20.65 ? 174 LYS A CA  1 
ATOM   3474 C  C   . LYS B 1 174 ? -17.969 9.853   10.441  1.00 20.95 ? 174 LYS A C   1 
ATOM   3475 O  O   . LYS B 1 174 ? -17.272 8.846   10.504  1.00 18.60 ? 174 LYS A O   1 
ATOM   3476 C  CB  . LYS B 1 174 ? -17.712 11.163  8.306   1.00 21.67 ? 174 LYS A CB  1 
ATOM   3477 C  CG  . LYS B 1 174 ? -17.497 12.583  7.514   1.00 23.49 ? 174 LYS A CG  1 
ATOM   3478 C  CD  . LYS B 1 174 ? -18.579 13.580  7.837   1.00 29.87 ? 174 LYS A CD  1 
ATOM   3479 C  CE  . LYS B 1 174 ? -18.464 14.884  6.964   1.00 30.26 ? 174 LYS A CE  1 
ATOM   3480 N  NZ  . LYS B 1 174 ? -18.969 14.708  5.520   1.00 36.94 ? 174 LYS A NZ  1 
ATOM   3481 N  N   . GLN B 1 175 ? -19.202 9.928   10.930  1.00 20.41 ? 175 GLN A N   1 
ATOM   3482 C  CA  . GLN B 1 175 ? -19.868 8.767   11.463  1.00 23.19 ? 175 GLN A CA  1 
ATOM   3483 C  C   . GLN B 1 175 ? -21.318 8.759   11.052  1.00 22.06 ? 175 GLN A C   1 
ATOM   3484 O  O   . GLN B 1 175 ? -21.905 9.791   10.690  1.00 19.13 ? 175 GLN A O   1 
ATOM   3485 C  CB  . GLN B 1 175 ? -19.691 8.622   12.982  1.00 23.37 ? 175 GLN A CB  1 
ATOM   3486 C  CG  . GLN B 1 175 ? -20.533 9.475   13.838  1.00 26.88 ? 175 GLN A CG  1 
ATOM   3487 C  CD  . GLN B 1 175 ? -20.296 9.136   15.336  1.00 29.64 ? 175 GLN A CD  1 
ATOM   3488 O  OE1 . GLN B 1 175 ? -21.258 9.024   16.125  1.00 36.42 ? 175 GLN A OE1 1 
ATOM   3489 N  NE2 . GLN B 1 175 ? -19.012 8.982   15.722  1.00 33.35 ? 175 GLN A NE2 1 
ATOM   3490 N  N   . THR B 1 176 ? -21.900 7.579   11.132  1.00 21.24 ? 176 THR A N   1 
ATOM   3491 C  CA  . THR B 1 176 ? -23.255 7.382   10.782  1.00 21.74 ? 176 THR A CA  1 
ATOM   3492 C  C   . THR B 1 176 ? -23.807 6.231   11.654  1.00 22.74 ? 176 THR A C   1 
ATOM   3493 O  O   . THR B 1 176 ? -23.037 5.407   12.209  1.00 20.11 ? 176 THR A O   1 
ATOM   3494 C  CB  . THR B 1 176 ? -23.466 7.229   9.238   1.00 22.92 ? 176 THR A CB  1 
ATOM   3495 O  OG1 . THR B 1 176 ? -24.841 7.498   8.971   1.00 27.45 ? 176 THR A OG1 1 
ATOM   3496 C  CG2 . THR B 1 176 ? -23.143 5.813   8.712   1.00 22.85 ? 176 THR A CG2 1 
ATOM   3497 N  N   . ARG B 1 177 ? -25.128 6.202   11.819  1.00 21.22 ? 177 ARG A N   1 
ATOM   3498 C  CA  . ARG B 1 177 ? -25.697 5.204   12.698  1.00 22.37 ? 177 ARG A CA  1 
ATOM   3499 C  C   . ARG B 1 177 ? -25.683 3.939   11.949  1.00 21.30 ? 177 ARG A C   1 
ATOM   3500 O  O   . ARG B 1 177 ? -25.846 3.956   10.733  1.00 22.05 ? 177 ARG A O   1 
ATOM   3501 C  CB  . ARG B 1 177 ? -27.120 5.575   13.103  1.00 22.83 ? 177 ARG A CB  1 
ATOM   3502 C  CG  . ARG B 1 177 ? -27.179 6.647   14.061  1.00 28.00 ? 177 ARG A CG  1 
ATOM   3503 C  CD  . ARG B 1 177 ? -28.133 6.062   15.057  1.00 34.58 ? 177 ARG A CD  1 
ATOM   3504 N  NE  . ARG B 1 177 ? -29.097 7.081   15.457  1.00 35.49 ? 177 ARG A NE  1 
ATOM   3505 C  CZ  . ARG B 1 177 ? -30.114 6.881   16.286  1.00 29.50 ? 177 ARG A CZ  1 
ATOM   3506 N  NH1 . ARG B 1 177 ? -30.328 5.681   16.812  1.00 30.05 ? 177 ARG A NH1 1 
ATOM   3507 N  NH2 . ARG B 1 177 ? -30.931 7.886   16.566  1.00 23.04 ? 177 ARG A NH2 1 
ATOM   3508 N  N   . PHE B 1 178 ? -25.461 2.844   12.677  1.00 20.48 ? 178 PHE A N   1 
ATOM   3509 C  CA  . PHE B 1 178 ? -25.318 1.532   12.074  1.00 20.16 ? 178 PHE A CA  1 
ATOM   3510 C  C   . PHE B 1 178 ? -25.678 0.457   13.101  1.00 20.67 ? 178 PHE A C   1 
ATOM   3511 O  O   . PHE B 1 178 ? -24.972 0.288   14.106  1.00 20.12 ? 178 PHE A O   1 
ATOM   3512 C  CB  . PHE B 1 178 ? -23.857 1.362   11.609  1.00 19.69 ? 178 PHE A CB  1 
ATOM   3513 C  CG  . PHE B 1 178 ? -23.609 0.088   10.921  1.00 16.52 ? 178 PHE A CG  1 
ATOM   3514 C  CD1 . PHE B 1 178 ? -23.831 -0.009  9.580   1.00 18.66 ? 178 PHE A CD1 1 
ATOM   3515 C  CD2 . PHE B 1 178 ? -23.104 -1.019  11.600  1.00 18.94 ? 178 PHE A CD2 1 
ATOM   3516 C  CE1 . PHE B 1 178 ? -23.673 -1.206  8.919   1.00 19.27 ? 178 PHE A CE1 1 
ATOM   3517 C  CE2 . PHE B 1 178 ? -22.894 -2.246  10.920  1.00 17.29 ? 178 PHE A CE2 1 
ATOM   3518 C  CZ  . PHE B 1 178 ? -23.202 -2.335  9.600   1.00 20.05 ? 178 PHE A CZ  1 
ATOM   3519 N  N   . THR B 1 179 ? -26.750 -0.282  12.853  1.00 20.63 ? 179 THR A N   1 
ATOM   3520 C  CA  . THR B 1 179 ? -27.162 -1.276  13.849  1.00 23.55 ? 179 THR A CA  1 
ATOM   3521 C  C   . THR B 1 179 ? -27.807 -2.442  13.118  1.00 22.89 ? 179 THR A C   1 
ATOM   3522 O  O   . THR B 1 179 ? -27.851 -2.452  11.903  1.00 21.87 ? 179 THR A O   1 
ATOM   3523 C  CB  . THR B 1 179 ? -28.091 -0.711  14.983  1.00 23.37 ? 179 THR A CB  1 
ATOM   3524 O  OG1 . THR B 1 179 ? -28.237 -1.727  15.989  1.00 26.62 ? 179 THR A OG1 1 
ATOM   3525 C  CG2 . THR B 1 179 ? -29.483 -0.297  14.428  1.00 23.85 ? 179 THR A CG2 1 
ATOM   3526 N  N   . ASN B 1 180 ? -28.282 -3.435  13.855  1.00 23.40 ? 180 ASN A N   1 
ATOM   3527 C  CA  . ASN B 1 180 ? -28.674 -4.681  13.219  1.00 23.80 ? 180 ASN A CA  1 
ATOM   3528 C  C   . ASN B 1 180 ? -27.586 -5.411  12.396  1.00 22.55 ? 180 ASN A C   1 
ATOM   3529 O  O   . ASN B 1 180 ? -27.801 -5.848  11.297  1.00 23.23 ? 180 ASN A O   1 
ATOM   3530 C  CB  . ASN B 1 180 ? -29.920 -4.545  12.341  1.00 24.80 ? 180 ASN A CB  1 
ATOM   3531 C  CG  . ASN B 1 180 ? -30.578 -5.926  12.113  1.00 30.59 ? 180 ASN A CG  1 
ATOM   3532 O  OD1 . ASN B 1 180 ? -30.560 -6.797  13.039  1.00 32.12 ? 180 ASN A OD1 1 
ATOM   3533 N  ND2 . ASN B 1 180 ? -31.079 -6.169  10.882  1.00 30.46 ? 180 ASN A ND2 1 
ATOM   3534 N  N   . PHE B 1 181 ? -26.429 -5.592  12.968  1.00 21.19 ? 181 PHE A N   1 
ATOM   3535 C  CA  . PHE B 1 181 ? -25.386 -6.198  12.280  1.00 19.83 ? 181 PHE A CA  1 
ATOM   3536 C  C   . PHE B 1 181 ? -25.235 -7.603  12.868  1.00 19.31 ? 181 PHE A C   1 
ATOM   3537 O  O   . PHE B 1 181 ? -24.855 -7.748  14.028  1.00 19.08 ? 181 PHE A O   1 
ATOM   3538 C  CB  . PHE B 1 181 ? -24.142 -5.305  12.496  1.00 20.52 ? 181 PHE A CB  1 
ATOM   3539 C  CG  . PHE B 1 181 ? -22.909 -5.806  11.817  1.00 21.38 ? 181 PHE A CG  1 
ATOM   3540 C  CD1 . PHE B 1 181 ? -22.947 -6.187  10.470  1.00 27.03 ? 181 PHE A CD1 1 
ATOM   3541 C  CD2 . PHE B 1 181 ? -21.691 -5.817  12.500  1.00 24.85 ? 181 PHE A CD2 1 
ATOM   3542 C  CE1 . PHE B 1 181 ? -21.781 -6.681  9.827   1.00 26.19 ? 181 PHE A CE1 1 
ATOM   3543 C  CE2 . PHE B 1 181 ? -20.540 -6.260  11.893  1.00 26.57 ? 181 PHE A CE2 1 
ATOM   3544 C  CZ  . PHE B 1 181 ? -20.582 -6.701  10.529  1.00 25.31 ? 181 PHE A CZ  1 
ATOM   3545 N  N   . ASP B 1 182 ? -25.511 -8.626  12.067  1.00 18.28 ? 182 ASP A N   1 
ATOM   3546 C  CA  . ASP B 1 182 ? -25.503 -10.017 12.546  1.00 18.43 ? 182 ASP A CA  1 
ATOM   3547 C  C   . ASP B 1 182 ? -24.071 -10.514 12.353  1.00 18.66 ? 182 ASP A C   1 
ATOM   3548 O  O   . ASP B 1 182 ? -23.724 -11.255 11.392  1.00 19.13 ? 182 ASP A O   1 
ATOM   3549 C  CB  . ASP B 1 182 ? -26.526 -10.832 11.742  1.00 18.38 ? 182 ASP A CB  1 
ATOM   3550 C  CG  . ASP B 1 182 ? -26.787 -12.204 12.327  1.00 21.39 ? 182 ASP A CG  1 
ATOM   3551 O  OD1 . ASP B 1 182 ? -26.044 -12.662 13.215  1.00 16.87 ? 182 ASP A OD1 1 
ATOM   3552 O  OD2 . ASP B 1 182 ? -27.741 -12.858 11.850  1.00 25.93 ? 182 ASP A OD2 1 
ATOM   3553 N  N   . LEU B 1 183 ? -23.211 -10.070 13.265  1.00 17.30 ? 183 LEU A N   1 
ATOM   3554 C  CA  . LEU B 1 183 ? -21.831 -10.385 13.150  1.00 17.00 ? 183 LEU A CA  1 
ATOM   3555 C  C   . LEU B 1 183 ? -21.643 -11.921 13.225  1.00 17.49 ? 183 LEU A C   1 
ATOM   3556 O  O   . LEU B 1 183 ? -20.723 -12.475 12.610  1.00 16.85 ? 183 LEU A O   1 
ATOM   3557 C  CB  . LEU B 1 183 ? -21.077 -9.612  14.260  1.00 17.59 ? 183 LEU A CB  1 
ATOM   3558 C  CG  . LEU B 1 183 ? -19.579 -9.786  14.440  1.00 17.79 ? 183 LEU A CG  1 
ATOM   3559 C  CD1 . LEU B 1 183 ? -18.858 -9.554  13.084  1.00 13.74 ? 183 LEU A CD1 1 
ATOM   3560 C  CD2 . LEU B 1 183 ? -19.045 -8.869  15.592  1.00 13.43 ? 183 LEU A CD2 1 
ATOM   3561 N  N   . LEU B 1 184 ? -22.508 -12.595 14.001  1.00 16.40 ? 184 LEU A N   1 
ATOM   3562 C  CA  . LEU B 1 184 ? -22.337 -14.004 14.202  1.00 17.91 ? 184 LEU A CA  1 
ATOM   3563 C  C   . LEU B 1 184 ? -22.530 -14.786 12.883  1.00 16.80 ? 184 LEU A C   1 
ATOM   3564 O  O   . LEU B 1 184 ? -21.814 -15.778 12.615  1.00 16.86 ? 184 LEU A O   1 
ATOM   3565 C  CB  . LEU B 1 184 ? -23.247 -14.518 15.342  1.00 17.01 ? 184 LEU A CB  1 
ATOM   3566 C  CG  . LEU B 1 184 ? -23.182 -16.038 15.582  1.00 19.66 ? 184 LEU A CG  1 
ATOM   3567 C  CD1 . LEU B 1 184 ? -21.867 -16.384 16.225  1.00 16.15 ? 184 LEU A CD1 1 
ATOM   3568 C  CD2 . LEU B 1 184 ? -24.369 -16.541 16.446  1.00 19.29 ? 184 LEU A CD2 1 
ATOM   3569 N  N   . SER B 1 185 ? -23.493 -14.320 12.095  1.00 15.96 ? 185 SER A N   1 
ATOM   3570 C  CA  . SER B 1 185 ? -23.775 -14.828 10.774  1.00 17.91 ? 185 SER A CA  1 
ATOM   3571 C  C   . SER B 1 185 ? -22.692 -14.553 9.766   1.00 16.86 ? 185 SER A C   1 
ATOM   3572 O  O   . SER B 1 185 ? -22.570 -15.278 8.778   1.00 15.98 ? 185 SER A O   1 
ATOM   3573 C  CB  . SER B 1 185 ? -25.018 -14.165 10.216  1.00 19.12 ? 185 SER A CB  1 
ATOM   3574 O  OG  . SER B 1 185 ? -26.083 -14.888 10.773  1.00 25.51 ? 185 SER A OG  1 
ATOM   3575 N  N   . LEU B 1 186 ? -21.921 -13.521 10.028  1.00 14.96 ? 186 LEU A N   1 
ATOM   3576 C  CA  . LEU B 1 186 ? -20.863 -13.134 9.140   1.00 14.51 ? 186 LEU A CA  1 
ATOM   3577 C  C   . LEU B 1 186 ? -19.701 -14.154 9.151   1.00 14.70 ? 186 LEU A C   1 
ATOM   3578 O  O   . LEU B 1 186 ? -18.976 -14.321 8.137   1.00 14.46 ? 186 LEU A O   1 
ATOM   3579 C  CB  . LEU B 1 186 ? -20.418 -11.703 9.506   1.00 14.54 ? 186 LEU A CB  1 
ATOM   3580 C  CG  . LEU B 1 186 ? -19.326 -11.107 8.623   1.00 16.90 ? 186 LEU A CG  1 
ATOM   3581 C  CD1 . LEU B 1 186 ? -19.816 -11.016 7.128   1.00 15.89 ? 186 LEU A CD1 1 
ATOM   3582 C  CD2 . LEU B 1 186 ? -18.731 -9.745  9.125   1.00 17.79 ? 186 LEU A CD2 1 
ATOM   3583 N  N   . LEU B 1 187 ? -19.528 -14.849 10.276  1.00 13.48 ? 187 LEU A N   1 
ATOM   3584 C  CA  . LEU B 1 187 ? -18.364 -15.683 10.461  1.00 13.17 ? 187 LEU A CA  1 
ATOM   3585 C  C   . LEU B 1 187 ? -18.425 -16.883 9.523   1.00 13.97 ? 187 LEU A C   1 
ATOM   3586 O  O   . LEU B 1 187 ? -19.560 -17.321 9.134   1.00 14.30 ? 187 LEU A O   1 
ATOM   3587 C  CB  . LEU B 1 187 ? -18.236 -16.076 11.942  1.00 12.75 ? 187 LEU A CB  1 
ATOM   3588 C  CG  . LEU B 1 187 ? -18.139 -14.976 12.988  1.00 14.77 ? 187 LEU A CG  1 
ATOM   3589 C  CD1 . LEU B 1 187 ? -18.012 -15.582 14.413  1.00 14.09 ? 187 LEU A CD1 1 
ATOM   3590 C  CD2 . LEU B 1 187 ? -16.950 -13.964 12.649  1.00 15.07 ? 187 LEU A CD2 1 
ATOM   3591 N  N   . PRO B 1 188 ? -17.243 -17.448 9.158   1.00 13.76 ? 188 PRO A N   1 
ATOM   3592 C  CA  . PRO B 1 188 ? -17.258 -18.578 8.242   1.00 13.34 ? 188 PRO A CA  1 
ATOM   3593 C  C   . PRO B 1 188 ? -17.863 -19.817 8.931   1.00 13.37 ? 188 PRO A C   1 
ATOM   3594 O  O   . PRO B 1 188 ? -17.949 -19.833 10.154  1.00 13.43 ? 188 PRO A O   1 
ATOM   3595 C  CB  . PRO B 1 188 ? -15.779 -18.809 7.934   1.00 12.80 ? 188 PRO A CB  1 
ATOM   3596 C  CG  . PRO B 1 188 ? -15.001 -18.108 9.058   1.00 15.69 ? 188 PRO A CG  1 
ATOM   3597 C  CD  . PRO B 1 188 ? -15.881 -17.022 9.520   1.00 12.95 ? 188 PRO A CD  1 
ATOM   3598 N  N   . PRO B 1 189 ? -18.208 -20.832 8.160   1.00 13.24 ? 189 PRO A N   1 
ATOM   3599 C  CA  . PRO B 1 189 ? -18.828 -22.083 8.634   1.00 14.99 ? 189 PRO A CA  1 
ATOM   3600 C  C   . PRO B 1 189 ? -17.927 -22.799 9.691   1.00 15.71 ? 189 PRO A C   1 
ATOM   3601 O  O   . PRO B 1 189 ? -18.422 -23.224 10.742  1.00 16.07 ? 189 PRO A O   1 
ATOM   3602 C  CB  . PRO B 1 189 ? -18.917 -22.918 7.345   1.00 14.19 ? 189 PRO A CB  1 
ATOM   3603 C  CG  . PRO B 1 189 ? -19.044 -21.944 6.281   1.00 15.93 ? 189 PRO A CG  1 
ATOM   3604 C  CD  . PRO B 1 189 ? -18.092 -20.802 6.678   1.00 14.52 ? 189 PRO A CD  1 
ATOM   3605 N  N   . SER B 1 190 ? -16.613 -22.834 9.405   1.00 15.20 ? 190 SER A N   1 
ATOM   3606 C  CA  . SER B 1 190 ? -15.607 -23.400 10.330  1.00 16.20 ? 190 SER A CA  1 
ATOM   3607 C  C   . SER B 1 190 ? -14.985 -22.336 11.260  1.00 16.64 ? 190 SER A C   1 
ATOM   3608 O  O   . SER B 1 190 ? -14.493 -21.261 10.818  1.00 15.36 ? 190 SER A O   1 
ATOM   3609 C  CB  . SER B 1 190 ? -14.514 -24.138 9.576   1.00 15.37 ? 190 SER A CB  1 
ATOM   3610 O  OG  . SER B 1 190 ? -13.605 -24.720 10.518  1.00 16.38 ? 190 SER A OG  1 
ATOM   3611 N  N   . TRP B 1 191 ? -15.032 -22.617 12.558  1.00 15.75 ? 191 TRP A N   1 
ATOM   3612 C  CA  . TRP B 1 191 ? -14.332 -21.756 13.504  1.00 17.78 ? 191 TRP A CA  1 
ATOM   3613 C  C   . TRP B 1 191 ? -13.001 -22.280 14.075  1.00 16.89 ? 191 TRP A C   1 
ATOM   3614 O  O   . TRP B 1 191 ? -12.565 -21.881 15.140  1.00 16.73 ? 191 TRP A O   1 
ATOM   3615 C  CB  . TRP B 1 191 ? -15.248 -21.301 14.619  1.00 16.37 ? 191 TRP A CB  1 
ATOM   3616 C  CG  . TRP B 1 191 ? -16.488 -20.557 14.168  1.00 19.14 ? 191 TRP A CG  1 
ATOM   3617 C  CD1 . TRP B 1 191 ? -16.737 -19.963 12.928  1.00 15.32 ? 191 TRP A CD1 1 
ATOM   3618 C  CD2 . TRP B 1 191 ? -17.674 -20.326 14.973  1.00 17.73 ? 191 TRP A CD2 1 
ATOM   3619 N  NE1 . TRP B 1 191 ? -18.027 -19.401 12.945  1.00 14.54 ? 191 TRP A NE1 1 
ATOM   3620 C  CE2 . TRP B 1 191 ? -18.604 -19.606 14.173  1.00 17.06 ? 191 TRP A CE2 1 
ATOM   3621 C  CE3 . TRP B 1 191 ? -18.059 -20.716 16.272  1.00 16.06 ? 191 TRP A CE3 1 
ATOM   3622 C  CZ2 . TRP B 1 191 ? -19.888 -19.227 14.659  1.00 17.02 ? 191 TRP A CZ2 1 
ATOM   3623 C  CZ3 . TRP B 1 191 ? -19.329 -20.315 16.762  1.00 16.47 ? 191 TRP A CZ3 1 
ATOM   3624 C  CH2 . TRP B 1 191 ? -20.219 -19.599 15.966  1.00 15.14 ? 191 TRP A CH2 1 
ATOM   3625 N  N   . ASP B 1 192 ? -12.376 -23.157 13.324  1.00 17.35 ? 192 ASP A N   1 
ATOM   3626 C  CA  . ASP B 1 192 ? -11.040 -23.589 13.598  1.00 17.96 ? 192 ASP A CA  1 
ATOM   3627 C  C   . ASP B 1 192 ? -10.066 -22.400 13.446  1.00 16.34 ? 192 ASP A C   1 
ATOM   3628 O  O   . ASP B 1 192 ? -10.226 -21.594 12.532  1.00 15.01 ? 192 ASP A O   1 
ATOM   3629 C  CB  . ASP B 1 192 ? -10.684 -24.765 12.720  1.00 19.02 ? 192 ASP A CB  1 
ATOM   3630 C  CG  . ASP B 1 192 ? -11.493 -26.028 13.082  1.00 19.31 ? 192 ASP A CG  1 
ATOM   3631 O  OD1 . ASP B 1 192 ? -12.162 -26.130 14.156  1.00 25.70 ? 192 ASP A OD1 1 
ATOM   3632 O  OD2 . ASP B 1 192 ? -11.486 -26.897 12.238  1.00 22.80 ? 192 ASP A OD2 1 
ATOM   3633 N  N   . TYR B 1 193 ? -9.114  -22.321 14.380  1.00 14.33 ? 193 TYR A N   1 
ATOM   3634 C  CA  . TYR B 1 193 ? -8.293  -21.145 14.535  1.00 13.63 ? 193 TYR A CA  1 
ATOM   3635 C  C   . TYR B 1 193 ? -6.837  -21.492 14.954  1.00 13.12 ? 193 TYR A C   1 
ATOM   3636 O  O   . TYR B 1 193 ? -6.537  -22.590 15.474  1.00 11.80 ? 193 TYR A O   1 
ATOM   3637 C  CB  . TYR B 1 193 ? -8.917  -20.155 15.560  1.00 12.64 ? 193 TYR A CB  1 
ATOM   3638 C  CG  . TYR B 1 193 ? -9.015  -20.747 16.968  1.00 12.39 ? 193 TYR A CG  1 
ATOM   3639 C  CD1 . TYR B 1 193 ? -7.927  -20.657 17.871  1.00 12.15 ? 193 TYR A CD1 1 
ATOM   3640 C  CD2 . TYR B 1 193 ? -10.133 -21.487 17.355  1.00 11.38 ? 193 TYR A CD2 1 
ATOM   3641 C  CE1 . TYR B 1 193 ? -7.951  -21.226 19.109  1.00 12.81 ? 193 TYR A CE1 1 
ATOM   3642 C  CE2 . TYR B 1 193 ? -10.204 -22.030 18.651  1.00 11.53 ? 193 TYR A CE2 1 
ATOM   3643 C  CZ  . TYR B 1 193 ? -9.093  -21.902 19.516  1.00 15.27 ? 193 TYR A CZ  1 
ATOM   3644 O  OH  . TYR B 1 193 ? -9.059  -22.435 20.800  1.00 14.61 ? 193 TYR A OH  1 
ATOM   3645 N  N   . TRP B 1 194 ? -5.965  -20.516 14.705  1.00 12.16 ? 194 TRP A N   1 
ATOM   3646 C  CA  . TRP B 1 194 ? -4.650  -20.417 15.276  1.00 13.21 ? 194 TRP A CA  1 
ATOM   3647 C  C   . TRP B 1 194 ? -4.688  -19.293 16.298  1.00 14.08 ? 194 TRP A C   1 
ATOM   3648 O  O   . TRP B 1 194 ? -5.480  -18.344 16.161  1.00 12.99 ? 194 TRP A O   1 
ATOM   3649 C  CB  . TRP B 1 194 ? -3.693  -20.011 14.196  1.00 12.18 ? 194 TRP A CB  1 
ATOM   3650 C  CG  . TRP B 1 194 ? -3.596  -20.977 13.030  1.00 14.44 ? 194 TRP A CG  1 
ATOM   3651 C  CD1 . TRP B 1 194 ? -3.056  -22.234 13.056  1.00 13.79 ? 194 TRP A CD1 1 
ATOM   3652 C  CD2 . TRP B 1 194 ? -4.050  -20.769 11.701  1.00 15.85 ? 194 TRP A CD2 1 
ATOM   3653 N  NE1 . TRP B 1 194 ? -3.094  -22.783 11.812  1.00 15.86 ? 194 TRP A NE1 1 
ATOM   3654 C  CE2 . TRP B 1 194 ? -3.730  -21.933 10.966  1.00 14.51 ? 194 TRP A CE2 1 
ATOM   3655 C  CE3 . TRP B 1 194 ? -4.752  -19.730 11.063  1.00 14.66 ? 194 TRP A CE3 1 
ATOM   3656 C  CZ2 . TRP B 1 194 ? -4.032  -22.081 9.582   1.00 11.05 ? 194 TRP A CZ2 1 
ATOM   3657 C  CZ3 . TRP B 1 194 ? -5.027  -19.856 9.689   1.00 14.69 ? 194 TRP A CZ3 1 
ATOM   3658 C  CH2 . TRP B 1 194 ? -4.644  -21.032 8.972   1.00 12.40 ? 194 TRP A CH2 1 
ATOM   3659 N  N   . THR B 1 195 ? -3.795  -19.364 17.300  1.00 13.47 ? 195 THR A N   1 
ATOM   3660 C  CA  . THR B 1 195 ? -3.786  -18.430 18.371  1.00 12.66 ? 195 THR A CA  1 
ATOM   3661 C  C   . THR B 1 195 ? -2.339  -18.267 18.820  1.00 12.03 ? 195 THR A C   1 
ATOM   3662 O  O   . THR B 1 195 ? -1.544  -19.253 18.805  1.00 13.33 ? 195 THR A O   1 
ATOM   3663 C  CB  . THR B 1 195 ? -4.700  -18.888 19.640  1.00 13.65 ? 195 THR A CB  1 
ATOM   3664 O  OG1 . THR B 1 195 ? -4.689  -17.841 20.608  1.00 13.91 ? 195 THR A OG1 1 
ATOM   3665 C  CG2 . THR B 1 195 ? -4.197  -20.182 20.340  1.00 13.18 ? 195 THR A CG2 1 
ATOM   3666 N  N   . TYR B 1 196 ? -2.016  -17.021 19.154  1.00 12.28 ? 196 TYR A N   1 
ATOM   3667 C  CA  . TYR B 1 196 ? -0.730  -16.640 19.700  1.00 13.64 ? 196 TYR A CA  1 
ATOM   3668 C  C   . TYR B 1 196 ? -0.839  -15.332 20.479  1.00 14.32 ? 196 TYR A C   1 
ATOM   3669 O  O   . TYR B 1 196 ? -1.734  -14.488 20.216  1.00 14.60 ? 196 TYR A O   1 
ATOM   3670 C  CB  . TYR B 1 196 ? 0.295   -16.498 18.586  1.00 12.80 ? 196 TYR A CB  1 
ATOM   3671 C  CG  . TYR B 1 196 ? 0.065   -15.288 17.733  1.00 10.35 ? 196 TYR A CG  1 
ATOM   3672 C  CD1 . TYR B 1 196 ? -0.949  -15.281 16.726  1.00 9.50  ? 196 TYR A CD1 1 
ATOM   3673 C  CD2 . TYR B 1 196 ? 0.838   -14.121 17.922  1.00 11.31 ? 196 TYR A CD2 1 
ATOM   3674 C  CE1 . TYR B 1 196 ? -1.141  -14.088 15.938  1.00 11.96 ? 196 TYR A CE1 1 
ATOM   3675 C  CE2 . TYR B 1 196 ? 0.671   -12.953 17.132  1.00 9.93  ? 196 TYR A CE2 1 
ATOM   3676 C  CZ  . TYR B 1 196 ? -0.305  -12.949 16.177  1.00 10.41 ? 196 TYR A CZ  1 
ATOM   3677 O  OH  . TYR B 1 196 ? -0.416  -11.779 15.425  1.00 12.86 ? 196 TYR A OH  1 
ATOM   3678 N  N   . PRO B 1 197 ? 0.073   -15.126 21.469  1.00 15.00 ? 197 PRO A N   1 
ATOM   3679 C  CA  . PRO B 1 197 ? 0.030   -13.827 22.143  1.00 13.90 ? 197 PRO A CA  1 
ATOM   3680 C  C   . PRO B 1 197 ? 0.723   -12.741 21.298  1.00 14.42 ? 197 PRO A C   1 
ATOM   3681 O  O   . PRO B 1 197 ? 1.817   -12.952 20.764  1.00 14.67 ? 197 PRO A O   1 
ATOM   3682 C  CB  . PRO B 1 197 ? 0.843   -14.068 23.437  1.00 12.62 ? 197 PRO A CB  1 
ATOM   3683 C  CG  . PRO B 1 197 ? 1.832   -15.155 23.027  1.00 16.18 ? 197 PRO A CG  1 
ATOM   3684 C  CD  . PRO B 1 197 ? 1.151   -15.999 21.987  1.00 14.14 ? 197 PRO A CD  1 
ATOM   3685 N  N   . GLY B 1 198 ? 0.075   -11.581 21.156  1.00 13.46 ? 198 GLY A N   1 
ATOM   3686 C  CA  . GLY B 1 198 ? 0.661   -10.536 20.365  1.00 12.65 ? 198 GLY A CA  1 
ATOM   3687 C  C   . GLY B 1 198 ? 0.193   -9.144  20.760  1.00 11.68 ? 198 GLY A C   1 
ATOM   3688 O  O   . GLY B 1 198 ? 0.022   -8.819  21.940  1.00 12.11 ? 198 GLY A O   1 
ATOM   3689 N  N   . SER B 1 199 ? -0.012  -8.298  19.761  1.00 13.33 ? 199 SER A N   1 
ATOM   3690 C  CA  . SER B 1 199 ? -0.242  -6.862  20.006  1.00 12.44 ? 199 SER A CA  1 
ATOM   3691 C  C   . SER B 1 199 ? -1.366  -6.287  19.168  1.00 13.15 ? 199 SER A C   1 
ATOM   3692 O  O   . SER B 1 199 ? -1.805  -6.904  18.189  1.00 12.21 ? 199 SER A O   1 
ATOM   3693 C  CB  . SER B 1 199 ? 1.071   -6.079  19.681  1.00 13.54 ? 199 SER A CB  1 
ATOM   3694 O  OG  . SER B 1 199 ? 1.240   -6.027  18.234  1.00 11.07 ? 199 SER A OG  1 
ATOM   3695 N  N   . LEU B 1 200 ? -1.765  -5.038  19.477  1.00 14.77 ? 200 LEU A N   1 
ATOM   3696 C  CA  . LEU B 1 200 ? -2.395  -4.181  18.455  1.00 15.24 ? 200 LEU A CA  1 
ATOM   3697 C  C   . LEU B 1 200 ? -1.498  -4.115  17.192  1.00 13.93 ? 200 LEU A C   1 
ATOM   3698 O  O   . LEU B 1 200 ? -0.282  -3.985  17.302  1.00 13.78 ? 200 LEU A O   1 
ATOM   3699 C  CB  . LEU B 1 200 ? -2.676  -2.720  18.937  1.00 15.65 ? 200 LEU A CB  1 
ATOM   3700 C  CG  . LEU B 1 200 ? -3.367  -2.569  20.318  1.00 19.58 ? 200 LEU A CG  1 
ATOM   3701 C  CD1 . LEU B 1 200 ? -3.516  -1.127  20.718  1.00 20.17 ? 200 LEU A CD1 1 
ATOM   3702 C  CD2 . LEU B 1 200 ? -4.740  -3.264  20.405  1.00 20.05 ? 200 LEU A CD2 1 
ATOM   3703 N  N   . THR B 1 201 ? -2.131  -4.168  16.020  1.00 12.28 ? 201 THR A N   1 
ATOM   3704 C  CA  . THR B 1 201 ? -1.414  -4.038  14.744  1.00 11.98 ? 201 THR A CA  1 
ATOM   3705 C  C   . THR B 1 201 ? -1.372  -2.578  14.315  1.00 11.95 ? 201 THR A C   1 
ATOM   3706 O  O   . THR B 1 201 ? -0.904  -2.261  13.220  1.00 12.47 ? 201 THR A O   1 
ATOM   3707 C  CB  . THR B 1 201 ? -2.037  -4.926  13.642  1.00 11.83 ? 201 THR A CB  1 
ATOM   3708 O  OG1 . THR B 1 201 ? -3.356  -4.418  13.292  1.00 10.40 ? 201 THR A OG1 1 
ATOM   3709 C  CG2 . THR B 1 201 ? -2.062  -6.450  14.110  1.00 11.38 ? 201 THR A CG2 1 
ATOM   3710 N  N   . VAL B 1 202 ? -1.856  -1.684  15.193  1.00 11.68 ? 202 VAL A N   1 
ATOM   3711 C  CA  . VAL B 1 202 ? -1.858  -0.238  14.932  1.00 11.77 ? 202 VAL A CA  1 
ATOM   3712 C  C   . VAL B 1 202 ? -1.262  0.420   16.173  1.00 13.55 ? 202 VAL A C   1 
ATOM   3713 O  O   . VAL B 1 202 ? -1.385  -0.100  17.297  1.00 13.84 ? 202 VAL A O   1 
ATOM   3714 C  CB  . VAL B 1 202 ? -3.262  0.384   14.651  1.00 10.61 ? 202 VAL A CB  1 
ATOM   3715 C  CG1 . VAL B 1 202 ? -3.852  -0.024  13.347  1.00 13.75 ? 202 VAL A CG1 1 
ATOM   3716 C  CG2 . VAL B 1 202 ? -4.267  0.142   15.855  1.00 14.03 ? 202 VAL A CG2 1 
ATOM   3717 N  N   . PRO B 1 203 ? -0.630  1.592   15.996  1.00 14.68 ? 203 PRO A N   1 
ATOM   3718 C  CA  . PRO B 1 203 ? -0.277  2.359   17.180  1.00 14.65 ? 203 PRO A CA  1 
ATOM   3719 C  C   . PRO B 1 203 ? -1.489  2.566   18.102  1.00 15.43 ? 203 PRO A C   1 
ATOM   3720 O  O   . PRO B 1 203 ? -2.613  2.824   17.621  1.00 15.38 ? 203 PRO A O   1 
ATOM   3721 C  CB  . PRO B 1 203 ? 0.213   3.691   16.587  1.00 13.98 ? 203 PRO A CB  1 
ATOM   3722 C  CG  . PRO B 1 203 ? 0.864   3.247   15.234  1.00 15.40 ? 203 PRO A CG  1 
ATOM   3723 C  CD  . PRO B 1 203 ? -0.183  2.251   14.730  1.00 12.91 ? 203 PRO A CD  1 
ATOM   3724 N  N   . PRO B 1 204 ? -1.286  2.405   19.433  1.00 15.23 ? 204 PRO A N   1 
ATOM   3725 C  CA  . PRO B 1 204 ? 0.028   2.255   20.130  1.00 16.29 ? 204 PRO A CA  1 
ATOM   3726 C  C   . PRO B 1 204 ? 0.675   0.883   20.280  1.00 16.12 ? 204 PRO A C   1 
ATOM   3727 O  O   . PRO B 1 204 ? 1.645   0.747   21.046  1.00 15.30 ? 204 PRO A O   1 
ATOM   3728 C  CB  . PRO B 1 204 ? -0.250  2.881   21.506  1.00 16.21 ? 204 PRO A CB  1 
ATOM   3729 C  CG  . PRO B 1 204 ? -1.718  2.557   21.768  1.00 17.05 ? 204 PRO A CG  1 
ATOM   3730 C  CD  . PRO B 1 204 ? -2.420  2.484   20.382  1.00 15.51 ? 204 PRO A CD  1 
ATOM   3731 N  N   . LEU B 1 205 ? 0.219   -0.102  19.510  1.00 15.39 ? 205 LEU A N   1 
ATOM   3732 C  CA  . LEU B 1 205 ? 0.971   -1.326  19.344  1.00 13.72 ? 205 LEU A CA  1 
ATOM   3733 C  C   . LEU B 1 205 ? 1.151   -2.093  20.669  1.00 14.08 ? 205 LEU A C   1 
ATOM   3734 O  O   . LEU B 1 205 ? 2.048   -2.856  20.800  1.00 12.21 ? 205 LEU A O   1 
ATOM   3735 C  CB  . LEU B 1 205 ? 2.293   -1.034  18.624  1.00 15.20 ? 205 LEU A CB  1 
ATOM   3736 C  CG  . LEU B 1 205 ? 2.195   -0.530  17.138  1.00 13.93 ? 205 LEU A CG  1 
ATOM   3737 C  CD1 . LEU B 1 205 ? 3.548   -0.009  16.741  1.00 12.65 ? 205 LEU A CD1 1 
ATOM   3738 C  CD2 . LEU B 1 205 ? 1.690   -1.618  16.208  1.00 10.03 ? 205 LEU A CD2 1 
ATOM   3739 N  N   . LEU B 1 206 ? 0.253   -1.844  21.636  1.00 14.19 ? 206 LEU A N   1 
ATOM   3740 C  CA  . LEU B 1 206 ? 0.288   -2.470  22.972  1.00 15.38 ? 206 LEU A CA  1 
ATOM   3741 C  C   . LEU B 1 206 ? 0.210   -3.977  22.883  1.00 15.31 ? 206 LEU A C   1 
ATOM   3742 O  O   . LEU B 1 206 ? -0.595  -4.567  22.118  1.00 12.90 ? 206 LEU A O   1 
ATOM   3743 C  CB  . LEU B 1 206 ? -0.850  -1.931  23.860  1.00 15.39 ? 206 LEU A CB  1 
ATOM   3744 C  CG  . LEU B 1 206 ? -0.855  -0.392  23.997  1.00 15.78 ? 206 LEU A CG  1 
ATOM   3745 C  CD1 . LEU B 1 206 ? -2.217  0.122   24.571  1.00 19.06 ? 206 LEU A CD1 1 
ATOM   3746 C  CD2 . LEU B 1 206 ? 0.396   0.074   24.863  1.00 19.51 ? 206 LEU A CD2 1 
ATOM   3747 N  N   . GLU B 1 207 ? 1.033   -4.608  23.700  1.00 13.70 ? 207 GLU A N   1 
ATOM   3748 C  CA  . GLU B 1 207 ? 1.168   -6.040  23.610  1.00 13.95 ? 207 GLU A CA  1 
ATOM   3749 C  C   . GLU B 1 207 ? 0.209   -6.661  24.604  1.00 14.59 ? 207 GLU A C   1 
ATOM   3750 O  O   . GLU B 1 207 ? 0.595   -7.209  25.650  1.00 16.37 ? 207 GLU A O   1 
ATOM   3751 C  CB  . GLU B 1 207 ? 2.617   -6.434  23.817  1.00 13.27 ? 207 GLU A CB  1 
ATOM   3752 C  CG  . GLU B 1 207 ? 3.564   -5.754  22.760  1.00 13.97 ? 207 GLU A CG  1 
ATOM   3753 C  CD  . GLU B 1 207 ? 4.975   -6.327  22.822  1.00 18.29 ? 207 GLU A CD  1 
ATOM   3754 O  OE1 . GLU B 1 207 ? 5.458   -6.648  23.966  1.00 17.72 ? 207 GLU A OE1 1 
ATOM   3755 O  OE2 . GLU B 1 207 ? 5.611   -6.451  21.739  1.00 16.62 ? 207 GLU A OE2 1 
ATOM   3756 N  N   . SER B 1 208 ? -1.067  -6.520  24.286  1.00 14.52 ? 208 SER A N   1 
ATOM   3757 C  CA  . SER B 1 208 ? -2.141  -6.887  25.187  1.00 14.49 ? 208 SER A CA  1 
ATOM   3758 C  C   . SER B 1 208 ? -3.135  -7.840  24.501  1.00 14.39 ? 208 SER A C   1 
ATOM   3759 O  O   . SER B 1 208 ? -4.248  -8.020  24.992  1.00 14.04 ? 208 SER A O   1 
ATOM   3760 C  CB  . SER B 1 208 ? -2.887  -5.616  25.569  1.00 14.22 ? 208 SER A CB  1 
ATOM   3761 O  OG  . SER B 1 208 ? -3.271  -4.811  24.448  1.00 15.33 ? 208 SER A OG  1 
ATOM   3762 N  N   . VAL B 1 209 ? -2.767  -8.379  23.348  1.00 12.77 ? 209 VAL A N   1 
ATOM   3763 C  CA  . VAL B 1 209 ? -3.773  -9.075  22.523  1.00 12.65 ? 209 VAL A CA  1 
ATOM   3764 C  C   . VAL B 1 209 ? -3.604  -10.599 22.455  1.00 11.70 ? 209 VAL A C   1 
ATOM   3765 O  O   . VAL B 1 209 ? -2.543  -11.073 22.084  1.00 12.55 ? 209 VAL A O   1 
ATOM   3766 C  CB  . VAL B 1 209 ? -3.881  -8.495  21.041  1.00 12.60 ? 209 VAL A CB  1 
ATOM   3767 C  CG1 . VAL B 1 209 ? -4.993  -9.268  20.279  1.00 10.80 ? 209 VAL A CG1 1 
ATOM   3768 C  CG2 . VAL B 1 209 ? -4.210  -7.016  21.024  1.00 11.60 ? 209 VAL A CG2 1 
ATOM   3769 N  N   . THR B 1 210 ? -4.665  -11.359 22.770  1.00 11.58 ? 210 THR A N   1 
ATOM   3770 C  CA  . THR B 1 210 ? -4.683  -12.764 22.427  1.00 12.21 ? 210 THR A CA  1 
ATOM   3771 C  C   . THR B 1 210 ? -5.305  -12.831 21.010  1.00 12.73 ? 210 THR A C   1 
ATOM   3772 O  O   . THR B 1 210 ? -6.515  -12.566 20.823  1.00 12.33 ? 210 THR A O   1 
ATOM   3773 C  CB  . THR B 1 210 ? -5.513  -13.653 23.437  1.00 12.42 ? 210 THR A CB  1 
ATOM   3774 O  OG1 . THR B 1 210 ? -5.008  -13.402 24.744  1.00 14.07 ? 210 THR A OG1 1 
ATOM   3775 C  CG2 . THR B 1 210 ? -5.372  -15.228 23.089  1.00 10.67 ? 210 THR A CG2 1 
ATOM   3776 N  N   . TRP B 1 211 ? -4.486  -13.241 20.051  1.00 12.20 ? 211 TRP A N   1 
ATOM   3777 C  CA  . TRP B 1 211 ? -4.920  -13.282 18.665  1.00 11.82 ? 211 TRP A CA  1 
ATOM   3778 C  C   . TRP B 1 211 ? -5.580  -14.622 18.484  1.00 12.69 ? 211 TRP A C   1 
ATOM   3779 O  O   . TRP B 1 211 ? -5.092  -15.632 18.963  1.00 14.01 ? 211 TRP A O   1 
ATOM   3780 C  CB  . TRP B 1 211 ? -3.750  -13.091 17.699  1.00 9.51  ? 211 TRP A CB  1 
ATOM   3781 C  CG  . TRP B 1 211 ? -3.522  -11.638 17.530  1.00 10.31 ? 211 TRP A CG  1 
ATOM   3782 C  CD1 . TRP B 1 211 ? -2.601  -10.827 18.200  1.00 7.15  ? 211 TRP A CD1 1 
ATOM   3783 C  CD2 . TRP B 1 211 ? -4.295  -10.813 16.709  1.00 10.67 ? 211 TRP A CD2 1 
ATOM   3784 N  NE1 . TRP B 1 211 ? -2.800  -9.524  17.815  1.00 11.64 ? 211 TRP A NE1 1 
ATOM   3785 C  CE2 . TRP B 1 211 ? -3.819  -9.491  16.874  1.00 13.35 ? 211 TRP A CE2 1 
ATOM   3786 C  CE3 . TRP B 1 211 ? -5.363  -11.072 15.802  1.00 11.16 ? 211 TRP A CE3 1 
ATOM   3787 C  CZ2 . TRP B 1 211 ? -4.426  -8.387  16.216  1.00 9.96  ? 211 TRP A CZ2 1 
ATOM   3788 C  CZ3 . TRP B 1 211 ? -5.934  -9.985  15.097  1.00 10.70 ? 211 TRP A CZ3 1 
ATOM   3789 C  CH2 . TRP B 1 211 ? -5.455  -8.656  15.307  1.00 9.38  ? 211 TRP A CH2 1 
ATOM   3790 N  N   . ILE B 1 212 ? -6.737  -14.601 17.838  1.00 14.55 ? 212 ILE A N   1 
ATOM   3791 C  CA  . ILE B 1 212 ? -7.446  -15.827 17.470  1.00 13.22 ? 212 ILE A CA  1 
ATOM   3792 C  C   . ILE B 1 212 ? -7.764  -15.592 15.986  1.00 12.12 ? 212 ILE A C   1 
ATOM   3793 O  O   . ILE B 1 212 ? -8.619  -14.777 15.654  1.00 13.30 ? 212 ILE A O   1 
ATOM   3794 C  CB  . ILE B 1 212 ? -8.781  -15.980 18.243  1.00 12.81 ? 212 ILE A CB  1 
ATOM   3795 C  CG1 . ILE B 1 212 ? -8.543  -16.109 19.784  1.00 14.62 ? 212 ILE A CG1 1 
ATOM   3796 C  CG2 . ILE B 1 212 ? -9.552  -17.249 17.693  1.00 15.33 ? 212 ILE A CG2 1 
ATOM   3797 C  CD1 . ILE B 1 212 ? -9.799  -15.751 20.614  1.00 10.88 ? 212 ILE A CD1 1 
ATOM   3798 N  N   . VAL B 1 213 ? -7.070  -16.287 15.102  1.00 12.63 ? 213 VAL A N   1 
ATOM   3799 C  CA  . VAL B 1 213 ? -7.227  -16.089 13.636  1.00 11.81 ? 213 VAL A CA  1 
ATOM   3800 C  C   . VAL B 1 213 ? -7.906  -17.357 13.060  1.00 12.70 ? 213 VAL A C   1 
ATOM   3801 O  O   . VAL B 1 213 ? -7.377  -18.485 13.178  1.00 12.35 ? 213 VAL A O   1 
ATOM   3802 C  CB  . VAL B 1 213 ? -5.814  -15.947 12.942  1.00 11.65 ? 213 VAL A CB  1 
ATOM   3803 C  CG1 . VAL B 1 213 ? -5.930  -15.811 11.401  1.00 13.01 ? 213 VAL A CG1 1 
ATOM   3804 C  CG2 . VAL B 1 213 ? -5.018  -14.824 13.542  1.00 10.94 ? 213 VAL A CG2 1 
ATOM   3805 N  N   . LEU B 1 214 ? -9.054  -17.177 12.426  1.00 12.13 ? 214 LEU A N   1 
ATOM   3806 C  CA  . LEU B 1 214 ? -9.809  -18.307 11.859  1.00 11.66 ? 214 LEU A CA  1 
ATOM   3807 C  C   . LEU B 1 214 ? -9.095  -18.781 10.583  1.00 12.37 ? 214 LEU A C   1 
ATOM   3808 O  O   . LEU B 1 214 ? -8.626  -17.964 9.815   1.00 10.89 ? 214 LEU A O   1 
ATOM   3809 C  CB  . LEU B 1 214 ? -11.237 -17.887 11.528  1.00 10.12 ? 214 LEU A CB  1 
ATOM   3810 C  CG  . LEU B 1 214 ? -12.102 -17.376 12.674  1.00 13.91 ? 214 LEU A CG  1 
ATOM   3811 C  CD1 . LEU B 1 214 ? -13.580 -17.290 12.255  1.00 12.34 ? 214 LEU A CD1 1 
ATOM   3812 C  CD2 . LEU B 1 214 ? -12.030 -18.370 13.800  1.00 18.21 ? 214 LEU A CD2 1 
ATOM   3813 N  N   . LYS B 1 215 ? -9.018  -20.089 10.374  1.00 10.93 ? 215 LYS A N   1 
ATOM   3814 C  CA  . LYS B 1 215 ? -8.449  -20.648 9.142   1.00 12.77 ? 215 LYS A CA  1 
ATOM   3815 C  C   . LYS B 1 215 ? -9.251  -20.276 7.907   1.00 12.44 ? 215 LYS A C   1 
ATOM   3816 O  O   . LYS B 1 215 ? -8.660  -19.850 6.891   1.00 14.92 ? 215 LYS A O   1 
ATOM   3817 C  CB  . LYS B 1 215 ? -8.316  -22.159 9.196   1.00 11.62 ? 215 LYS A CB  1 
ATOM   3818 C  CG  . LYS B 1 215 ? -7.720  -22.789 7.923   1.00 16.82 ? 215 LYS A CG  1 
ATOM   3819 C  CD  . LYS B 1 215 ? -7.213  -24.211 8.156   1.00 15.48 ? 215 LYS A CD  1 
ATOM   3820 C  CE  . LYS B 1 215 ? -6.940  -24.921 6.822   1.00 18.95 ? 215 LYS A CE  1 
ATOM   3821 N  NZ  . LYS B 1 215 ? -6.679  -26.337 7.130   1.00 24.05 ? 215 LYS A NZ  1 
ATOM   3822 N  N   . GLN B 1 216 ? -10.571 -20.418 8.014   1.00 11.85 ? 216 GLN A N   1 
ATOM   3823 C  CA  . GLN B 1 216 ? -11.449 -20.343 6.836   1.00 13.06 ? 216 GLN A CA  1 
ATOM   3824 C  C   . GLN B 1 216 ? -11.836 -18.882 6.488   1.00 12.78 ? 216 GLN A C   1 
ATOM   3825 O  O   . GLN B 1 216 ? -12.395 -18.171 7.320   1.00 13.03 ? 216 GLN A O   1 
ATOM   3826 C  CB  . GLN B 1 216 ? -12.663 -21.241 6.981   1.00 14.00 ? 216 GLN A CB  1 
ATOM   3827 C  CG  . GLN B 1 216 ? -13.545 -21.223 5.707   1.00 11.15 ? 216 GLN A CG  1 
ATOM   3828 C  CD  . GLN B 1 216 ? -14.729 -22.145 5.813   1.00 16.22 ? 216 GLN A CD  1 
ATOM   3829 O  OE1 . GLN B 1 216 ? -15.117 -22.533 6.882   1.00 13.20 ? 216 GLN A OE1 1 
ATOM   3830 N  NE2 . GLN B 1 216 ? -15.303 -22.496 4.679   1.00 16.18 ? 216 GLN A NE2 1 
ATOM   3831 N  N   . PRO B 1 217 ? -11.518 -18.444 5.259   1.00 12.73 ? 217 PRO A N   1 
ATOM   3832 C  CA  . PRO B 1 217 ? -11.986 -17.103 4.845   1.00 12.55 ? 217 PRO A CA  1 
ATOM   3833 C  C   . PRO B 1 217 ? -13.499 -16.983 4.606   1.00 12.44 ? 217 PRO A C   1 
ATOM   3834 O  O   . PRO B 1 217 ? -14.209 -17.983 4.441   1.00 11.43 ? 217 PRO A O   1 
ATOM   3835 C  CB  . PRO B 1 217 ? -11.199 -16.819 3.530   1.00 13.00 ? 217 PRO A CB  1 
ATOM   3836 C  CG  . PRO B 1 217 ? -10.177 -17.945 3.459   1.00 15.71 ? 217 PRO A CG  1 
ATOM   3837 C  CD  . PRO B 1 217 ? -10.728 -19.116 4.190   1.00 13.24 ? 217 PRO A CD  1 
ATOM   3838 N  N   . ILE B 1 218 ? -13.975 -15.751 4.525   1.00 12.40 ? 218 ILE A N   1 
ATOM   3839 C  CA  . ILE B 1 218 ? -15.326 -15.446 4.052   1.00 12.86 ? 218 ILE A CA  1 
ATOM   3840 C  C   . ILE B 1 218 ? -15.123 -14.734 2.716   1.00 14.08 ? 218 ILE A C   1 
ATOM   3841 O  O   . ILE B 1 218 ? -13.984 -14.351 2.371   1.00 13.82 ? 218 ILE A O   1 
ATOM   3842 C  CB  . ILE B 1 218 ? -16.087 -14.574 5.070   1.00 13.15 ? 218 ILE A CB  1 
ATOM   3843 C  CG1 . ILE B 1 218 ? -15.424 -13.196 5.317   1.00 8.72  ? 218 ILE A CG1 1 
ATOM   3844 C  CG2 . ILE B 1 218 ? -16.159 -15.333 6.469   1.00 11.38 ? 218 ILE A CG2 1 
ATOM   3845 C  CD1 . ILE B 1 218 ? -16.355 -12.206 6.133   1.00 14.99 ? 218 ILE A CD1 1 
ATOM   3846 N  N   A ASN B 1 219 ? -16.181 -14.576 1.943   0.50 13.43 ? 219 ASN A N   1 
ATOM   3847 N  N   B ASN B 1 219 ? -16.234 -14.500 2.027   0.50 13.50 ? 219 ASN A N   1 
ATOM   3848 C  CA  A ASN B 1 219 ? -15.994 -14.008 0.619   0.50 14.70 ? 219 ASN A CA  1 
ATOM   3849 C  CA  B ASN B 1 219 ? -16.229 -13.964 0.676   0.50 15.27 ? 219 ASN A CA  1 
ATOM   3850 C  C   A ASN B 1 219 ? -16.510 -12.579 0.621   0.50 14.47 ? 219 ASN A C   1 
ATOM   3851 C  C   B ASN B 1 219 ? -16.566 -12.497 0.650   0.50 14.85 ? 219 ASN A C   1 
ATOM   3852 O  O   A ASN B 1 219 ? -17.342 -12.174 1.483   0.50 15.07 ? 219 ASN A O   1 
ATOM   3853 O  O   B ASN B 1 219 ? -17.353 -11.985 1.492   0.50 15.08 ? 219 ASN A O   1 
ATOM   3854 C  CB  A ASN B 1 219 ? -16.672 -14.876 -0.490  0.50 15.51 ? 219 ASN A CB  1 
ATOM   3855 C  CB  B ASN B 1 219 ? -17.248 -14.745 -0.203  0.50 16.05 ? 219 ASN A CB  1 
ATOM   3856 C  CG  A ASN B 1 219 ? -16.026 -16.261 -0.682  0.50 17.55 ? 219 ASN A CG  1 
ATOM   3857 C  CG  B ASN B 1 219 ? -18.617 -14.829 0.432   0.50 19.50 ? 219 ASN A CG  1 
ATOM   3858 O  OD1 A ASN B 1 219 ? -15.414 -16.537 -1.727  0.50 20.77 ? 219 ASN A OD1 1 
ATOM   3859 O  OD1 B ASN B 1 219 ? -18.782 -15.472 1.495   0.50 23.03 ? 219 ASN A OD1 1 
ATOM   3860 N  ND2 A ASN B 1 219 ? -16.230 -17.169 0.296   0.50 23.30 ? 219 ASN A ND2 1 
ATOM   3861 N  ND2 B ASN B 1 219 ? -19.623 -14.150 -0.184  0.50 18.13 ? 219 ASN A ND2 1 
ATOM   3862 N  N   . ILE B 1 220 ? -15.991 -11.808 -0.329  1.00 14.71 ? 220 ILE A N   1 
ATOM   3863 C  CA  . ILE B 1 220 ? -16.375 -10.439 -0.598  1.00 12.00 ? 220 ILE A CA  1 
ATOM   3864 C  C   . ILE B 1 220 ? -16.160 -10.272 -2.098  1.00 12.76 ? 220 ILE A C   1 
ATOM   3865 O  O   . ILE B 1 220 ? -15.297 -10.916 -2.701  1.00 13.10 ? 220 ILE A O   1 
ATOM   3866 C  CB  . ILE B 1 220 ? -15.470 -9.400  0.195   1.00 12.44 ? 220 ILE A CB  1 
ATOM   3867 C  CG1 . ILE B 1 220 ? -16.120 -7.985  0.123   1.00 10.98 ? 220 ILE A CG1 1 
ATOM   3868 C  CG2 . ILE B 1 220 ? -14.003 -9.521  -0.225  1.00 10.74 ? 220 ILE A CG2 1 
ATOM   3869 C  CD1 . ILE B 1 220 ? -15.454 -6.838  1.006   1.00 12.84 ? 220 ILE A CD1 1 
ATOM   3870 N  N   . SER B 1 221 ? -16.935 -9.398  -2.722  1.00 13.28 ? 221 SER A N   1 
ATOM   3871 C  CA  . SER B 1 221 ? -16.682 -9.206  -4.141  1.00 13.07 ? 221 SER A CA  1 
ATOM   3872 C  C   . SER B 1 221 ? -15.565 -8.186  -4.308  1.00 12.23 ? 221 SER A C   1 
ATOM   3873 O  O   . SER B 1 221 ? -15.301 -7.391  -3.413  1.00 9.97  ? 221 SER A O   1 
ATOM   3874 C  CB  . SER B 1 221 ? -17.960 -8.836  -4.893  1.00 10.85 ? 221 SER A CB  1 
ATOM   3875 O  OG  . SER B 1 221 ? -18.344 -7.512  -4.580  1.00 12.89 ? 221 SER A OG  1 
ATOM   3876 N  N   A SER B 1 222 ? -14.911 -8.219  -5.457  0.50 12.28 ? 222 SER A N   1 
ATOM   3877 N  N   B SER B 1 222 ? -14.897 -8.216  -5.470  0.50 12.04 ? 222 SER A N   1 
ATOM   3878 C  CA  A SER B 1 222 ? -13.904 -7.233  -5.699  0.50 14.36 ? 222 SER A CA  1 
ATOM   3879 C  CA  B SER B 1 222 ? -13.892 -7.199  -5.787  0.50 13.89 ? 222 SER A CA  1 
ATOM   3880 C  C   A SER B 1 222 ? -14.483 -5.806  -5.710  0.50 13.89 ? 222 SER A C   1 
ATOM   3881 C  C   B SER B 1 222 ? -14.502 -5.806  -5.671  0.50 13.58 ? 222 SER A C   1 
ATOM   3882 O  O   A SER B 1 222 ? -13.783 -4.861  -5.328  0.50 14.28 ? 222 SER A O   1 
ATOM   3883 O  O   B SER B 1 222 ? -13.852 -4.888  -5.158  0.50 13.97 ? 222 SER A O   1 
ATOM   3884 C  CB  A SER B 1 222 ? -13.146 -7.577  -6.971  0.50 13.99 ? 222 SER A CB  1 
ATOM   3885 C  CB  B SER B 1 222 ? -13.260 -7.426  -7.180  0.50 13.57 ? 222 SER A CB  1 
ATOM   3886 O  OG  A SER B 1 222 ? -12.454 -6.439  -7.352  0.50 15.84 ? 222 SER A OG  1 
ATOM   3887 O  OG  B SER B 1 222 ? -14.193 -7.176  -8.226  0.50 13.24 ? 222 SER A OG  1 
ATOM   3888 N  N   . GLN B 1 223 ? -15.733 -5.644  -6.166  1.00 13.71 ? 223 GLN A N   1 
ATOM   3889 C  CA  . GLN B 1 223 ? -16.392 -4.309  -6.129  1.00 14.34 ? 223 GLN A CA  1 
ATOM   3890 C  C   . GLN B 1 223 ? -16.718 -3.833  -4.720  1.00 14.05 ? 223 GLN A C   1 
ATOM   3891 O  O   . GLN B 1 223 ? -16.566 -2.636  -4.419  1.00 15.83 ? 223 GLN A O   1 
ATOM   3892 C  CB  . GLN B 1 223 ? -17.674 -4.225  -6.995  1.00 15.16 ? 223 GLN A CB  1 
ATOM   3893 C  CG  . GLN B 1 223 ? -17.385 -4.462  -8.505  1.00 16.04 ? 223 GLN A CG  1 
ATOM   3894 C  CD  . GLN B 1 223 ? -17.298 -5.919  -8.936  1.00 16.29 ? 223 GLN A CD  1 
ATOM   3895 O  OE1 . GLN B 1 223 ? -17.023 -6.211  -10.138 1.00 21.24 ? 223 GLN A OE1 1 
ATOM   3896 N  NE2 . GLN B 1 223 ? -17.453 -6.853  -8.004  1.00 12.90 ? 223 GLN A NE2 1 
ATOM   3897 N  N   . GLN B 1 224 ? -17.179 -4.731  -3.862  1.00 12.53 ? 224 GLN A N   1 
ATOM   3898 C  CA  . GLN B 1 224 ? -17.405 -4.342  -2.483  1.00 12.88 ? 224 GLN A CA  1 
ATOM   3899 C  C   . GLN B 1 224 ? -16.078 -3.925  -1.835  1.00 12.40 ? 224 GLN A C   1 
ATOM   3900 O  O   . GLN B 1 224 ? -15.996 -2.890  -1.160  1.00 12.38 ? 224 GLN A O   1 
ATOM   3901 C  CB  . GLN B 1 224 ? -18.004 -5.491  -1.708  1.00 13.35 ? 224 GLN A CB  1 
ATOM   3902 C  CG  . GLN B 1 224 ? -19.509 -5.744  -2.019  1.00 16.10 ? 224 GLN A CG  1 
ATOM   3903 C  CD  . GLN B 1 224 ? -19.992 -6.943  -1.292  1.00 13.63 ? 224 GLN A CD  1 
ATOM   3904 O  OE1 . GLN B 1 224 ? -19.274 -7.938  -1.197  1.00 11.68 ? 224 GLN A OE1 1 
ATOM   3905 N  NE2 . GLN B 1 224 ? -21.203 -6.866  -0.742  1.00 9.92  ? 224 GLN A NE2 1 
ATOM   3906 N  N   . LEU B 1 225 ? -15.046 -4.767  -2.012  1.00 12.86 ? 225 LEU A N   1 
ATOM   3907 C  CA  . LEU B 1 225 ? -13.766 -4.479  -1.382  1.00 13.22 ? 225 LEU A CA  1 
ATOM   3908 C  C   . LEU B 1 225 ? -13.196 -3.117  -1.837  1.00 12.88 ? 225 LEU A C   1 
ATOM   3909 O  O   . LEU B 1 225 ? -12.602 -2.363  -1.049  1.00 11.53 ? 225 LEU A O   1 
ATOM   3910 C  CB  . LEU B 1 225 ? -12.770 -5.651  -1.610  1.00 11.33 ? 225 LEU A CB  1 
ATOM   3911 C  CG  . LEU B 1 225 ? -11.349 -5.392  -1.078  1.00 11.74 ? 225 LEU A CG  1 
ATOM   3912 C  CD1 . LEU B 1 225 ? -11.331 -5.173  0.506   1.00 13.46 ? 225 LEU A CD1 1 
ATOM   3913 C  CD2 . LEU B 1 225 ? -10.425 -6.553  -1.402  1.00 10.66 ? 225 LEU A CD2 1 
ATOM   3914 N  N   . ALA B 1 226 ? -13.293 -2.868  -3.149  1.00 14.32 ? 226 ALA A N   1 
ATOM   3915 C  CA  . ALA B 1 226 ? -12.836 -1.619  -3.719  1.00 15.42 ? 226 ALA A CA  1 
ATOM   3916 C  C   . ALA B 1 226 ? -13.434 -0.380  -3.060  1.00 16.15 ? 226 ALA A C   1 
ATOM   3917 O  O   . ALA B 1 226 ? -12.768 0.667   -2.974  1.00 15.34 ? 226 ALA A O   1 
ATOM   3918 C  CB  . ALA B 1 226 ? -13.097 -1.623  -5.254  1.00 15.17 ? 226 ALA A CB  1 
ATOM   3919 N  N   . LYS B 1 227 ? -14.682 -0.479  -2.580  1.00 15.60 ? 227 LYS A N   1 
ATOM   3920 C  CA  . LYS B 1 227 ? -15.350 0.656   -1.894  1.00 15.90 ? 227 LYS A CA  1 
ATOM   3921 C  C   . LYS B 1 227 ? -14.587 1.165   -0.688  1.00 15.53 ? 227 LYS A C   1 
ATOM   3922 O  O   . LYS B 1 227 ? -14.514 2.358   -0.484  1.00 15.03 ? 227 LYS A O   1 
ATOM   3923 C  CB  . LYS B 1 227 ? -16.828 0.336   -1.579  1.00 17.25 ? 227 LYS A CB  1 
ATOM   3924 C  CG  . LYS B 1 227 ? -17.659 0.466   -2.908  1.00 22.61 ? 227 LYS A CG  1 
ATOM   3925 C  CD  . LYS B 1 227 ? -19.130 0.284   -2.789  1.00 25.49 ? 227 LYS A CD  1 
ATOM   3926 C  CE  . LYS B 1 227 ? -19.833 1.318   -1.897  1.00 27.73 ? 227 LYS A CE  1 
ATOM   3927 N  NZ  . LYS B 1 227 ? -19.342 2.675   -2.123  1.00 27.33 ? 227 LYS A NZ  1 
ATOM   3928 N  N   . PHE B 1 228 ? -13.874 0.276   0.022   1.00 14.58 ? 228 PHE A N   1 
ATOM   3929 C  CA  . PHE B 1 228 ? -13.128 0.726   1.224   1.00 13.14 ? 228 PHE A CA  1 
ATOM   3930 C  C   . PHE B 1 228 ? -11.972 1.602   0.899   1.00 14.36 ? 228 PHE A C   1 
ATOM   3931 O  O   . PHE B 1 228 ? -11.624 2.469   1.695   1.00 14.90 ? 228 PHE A O   1 
ATOM   3932 C  CB  . PHE B 1 228 ? -12.631 -0.494  2.012   1.00 12.75 ? 228 PHE A CB  1 
ATOM   3933 C  CG  . PHE B 1 228 ? -13.744 -1.278  2.543   1.00 13.21 ? 228 PHE A CG  1 
ATOM   3934 C  CD1 . PHE B 1 228 ? -14.149 -2.474  1.917   1.00 10.01 ? 228 PHE A CD1 1 
ATOM   3935 C  CD2 . PHE B 1 228 ? -14.460 -0.789  3.643   1.00 15.77 ? 228 PHE A CD2 1 
ATOM   3936 C  CE1 . PHE B 1 228 ? -15.321 -3.157  2.383   1.00 14.39 ? 228 PHE A CE1 1 
ATOM   3937 C  CE2 . PHE B 1 228 ? -15.578 -1.483  4.137   1.00 9.27  ? 228 PHE A CE2 1 
ATOM   3938 C  CZ  . PHE B 1 228 ? -16.013 -2.670  3.527   1.00 11.47 ? 228 PHE A CZ  1 
ATOM   3939 N  N   . ARG B 1 229 ? -11.394 1.404   -0.292  1.00 14.08 ? 229 ARG A N   1 
ATOM   3940 C  CA  . ARG B 1 229 ? -10.204 2.181   -0.725  1.00 14.18 ? 229 ARG A CA  1 
ATOM   3941 C  C   . ARG B 1 229 ? -10.534 3.636   -1.004  1.00 13.57 ? 229 ARG A C   1 
ATOM   3942 O  O   . ARG B 1 229 ? -9.652  4.479   -1.025  1.00 13.66 ? 229 ARG A O   1 
ATOM   3943 C  CB  . ARG B 1 229 ? -9.584  1.530   -1.987  1.00 14.24 ? 229 ARG A CB  1 
ATOM   3944 C  CG  . ARG B 1 229 ? -9.059  0.078   -1.745  1.00 13.80 ? 229 ARG A CG  1 
ATOM   3945 C  CD  . ARG B 1 229 ? -8.235  -0.436  -2.930  1.00 14.96 ? 229 ARG A CD  1 
ATOM   3946 N  NE  . ARG B 1 229 ? -7.872  -1.843  -2.710  1.00 15.50 ? 229 ARG A NE  1 
ATOM   3947 C  CZ  . ARG B 1 229 ? -8.520  -2.888  -3.234  1.00 16.44 ? 229 ARG A CZ  1 
ATOM   3948 N  NH1 . ARG B 1 229 ? -9.504  -2.688  -4.096  1.00 14.74 ? 229 ARG A NH1 1 
ATOM   3949 N  NH2 . ARG B 1 229 ? -8.143  -4.136  -2.956  1.00 11.91 ? 229 ARG A NH2 1 
ATOM   3950 N  N   . SER B 1 230 ? -11.801 3.926   -1.266  1.00 14.12 ? 230 SER A N   1 
ATOM   3951 C  CA  . SER B 1 230 ? -12.226 5.326   -1.416  1.00 16.24 ? 230 SER A CA  1 
ATOM   3952 C  C   . SER B 1 230 ? -12.573 6.061   -0.123  1.00 14.82 ? 230 SER A C   1 
ATOM   3953 O  O   . SER B 1 230 ? -12.876 7.251   -0.130  1.00 14.59 ? 230 SER A O   1 
ATOM   3954 C  CB  . SER B 1 230 ? -13.392 5.409   -2.417  1.00 18.33 ? 230 SER A CB  1 
ATOM   3955 O  OG  . SER B 1 230 ? -14.489 5.054   -1.615  1.00 26.98 ? 230 SER A OG  1 
ATOM   3956 N  N   . LEU B 1 231 ? -12.451 5.422   1.035   1.00 13.82 ? 231 LEU A N   1 
ATOM   3957 C  CA  . LEU B 1 231 ? -12.356 6.230   2.291   1.00 13.38 ? 231 LEU A CA  1 
ATOM   3958 C  C   . LEU B 1 231 ? -11.126 7.151   2.329   1.00 14.28 ? 231 LEU A C   1 
ATOM   3959 O  O   . LEU B 1 231 ? -10.078 6.751   1.878   1.00 14.35 ? 231 LEU A O   1 
ATOM   3960 C  CB  . LEU B 1 231 ? -12.210 5.258   3.491   1.00 13.11 ? 231 LEU A CB  1 
ATOM   3961 C  CG  . LEU B 1 231 ? -13.541 4.522   3.689   1.00 10.07 ? 231 LEU A CG  1 
ATOM   3962 C  CD1 . LEU B 1 231 ? -13.330 3.298   4.630   1.00 16.53 ? 231 LEU A CD1 1 
ATOM   3963 C  CD2 . LEU B 1 231 ? -14.642 5.496   4.166   1.00 11.22 ? 231 LEU A CD2 1 
ATOM   3964 N  N   . LEU B 1 232 ? -11.218 8.334   2.935   1.00 15.74 ? 232 LEU A N   1 
ATOM   3965 C  CA  . LEU B 1 232 ? -10.002 9.190   3.091   1.00 16.04 ? 232 LEU A CA  1 
ATOM   3966 C  C   . LEU B 1 232 ? -9.355  8.952   4.432   1.00 16.52 ? 232 LEU A C   1 
ATOM   3967 O  O   . LEU B 1 232 ? -10.032 8.611   5.389   1.00 17.53 ? 232 LEU A O   1 
ATOM   3968 C  CB  . LEU B 1 232 ? -10.349 10.679  2.928   1.00 15.89 ? 232 LEU A CB  1 
ATOM   3969 C  CG  . LEU B 1 232 ? -11.191 11.087  1.733   1.00 16.30 ? 232 LEU A CG  1 
ATOM   3970 C  CD1 . LEU B 1 232 ? -11.656 12.512  1.896   1.00 21.98 ? 232 LEU A CD1 1 
ATOM   3971 C  CD2 . LEU B 1 232 ? -10.365 10.838  0.460   1.00 19.65 ? 232 LEU A CD2 1 
ATOM   3972 N  N   . CYS B 1 233 ? -8.029  9.075   4.479   1.00 17.41 ? 233 CYS A N   1 
ATOM   3973 C  CA  . CYS B 1 233 ? -7.307  9.097   5.743   1.00 19.58 ? 233 CYS A CA  1 
ATOM   3974 C  C   . CYS B 1 233 ? -7.150  10.549  6.189   1.00 19.57 ? 233 CYS A C   1 
ATOM   3975 O  O   . CYS B 1 233 ? -6.404  10.844  7.101   1.00 18.86 ? 233 CYS A O   1 
ATOM   3976 C  CB  . CYS B 1 233 ? -5.925  8.449   5.589   1.00 19.93 ? 233 CYS A CB  1 
ATOM   3977 S  SG  . CYS B 1 233 ? -4.852  9.219   4.277   1.00 21.00 ? 233 CYS A SG  1 
ATOM   3978 N  N   . THR B 1 234 ? -7.824  11.438  5.498   1.00 21.54 ? 234 THR A N   1 
ATOM   3979 C  CA  . THR B 1 234 ? -7.691  12.884  5.766   1.00 24.07 ? 234 THR A CA  1 
ATOM   3980 C  C   . THR B 1 234 ? -9.048  13.482  6.137   1.00 24.92 ? 234 THR A C   1 
ATOM   3981 O  O   . THR B 1 234 ? -10.116 13.021  5.646   1.00 24.94 ? 234 THR A O   1 
ATOM   3982 C  CB  . THR B 1 234 ? -7.138  13.591  4.499   1.00 22.88 ? 234 THR A CB  1 
ATOM   3983 O  OG1 . THR B 1 234 ? -7.914  13.125  3.389   1.00 23.64 ? 234 THR A OG1 1 
ATOM   3984 C  CG2 . THR B 1 234 ? -5.657  13.261  4.280   1.00 22.46 ? 234 THR A CG2 1 
ATOM   3985 N  N   . ALA B 1 235 ? -9.036  14.462  7.059   1.00 28.44 ? 235 ALA A N   1 
ATOM   3986 C  CA  . ALA B 1 235 ? -10.284 15.105  7.524   1.00 29.92 ? 235 ALA A CA  1 
ATOM   3987 C  C   . ALA B 1 235 ? -10.863 16.104  6.499   1.00 31.71 ? 235 ALA A C   1 
ATOM   3988 O  O   . ALA B 1 235 ? -10.204 16.462  5.515   1.00 31.04 ? 235 ALA A O   1 
ATOM   3989 C  CB  . ALA B 1 235 ? -10.049 15.806  8.869   1.00 30.90 ? 235 ALA A CB  1 
ATOM   3990 N  N   . GLU B 1 236 ? -12.122 16.493  6.697   1.00 33.89 ? 236 GLU A N   1 
ATOM   3991 C  CA  . GLU B 1 236 ? -12.709 17.683  6.013   1.00 36.44 ? 236 GLU A CA  1 
ATOM   3992 C  C   . GLU B 1 236 ? -11.726 18.876  6.052   1.00 37.03 ? 236 GLU A C   1 
ATOM   3993 O  O   . GLU B 1 236 ? -11.182 19.215  7.123   1.00 37.29 ? 236 GLU A O   1 
ATOM   3994 C  CB  . GLU B 1 236 ? -14.047 18.090  6.676   1.00 35.93 ? 236 GLU A CB  1 
ATOM   3995 C  CG  . GLU B 1 236 ? -14.889 19.075  5.862   0.01 36.22 ? 236 GLU A CG  1 
ATOM   3996 C  CD  . GLU B 1 236 ? -15.445 18.472  4.580   0.01 36.12 ? 236 GLU A CD  1 
ATOM   3997 O  OE1 . GLU B 1 236 ? -15.338 19.127  3.523   0.01 36.13 ? 236 GLU A OE1 1 
ATOM   3998 O  OE2 . GLU B 1 236 ? -15.986 17.345  4.627   0.01 36.16 ? 236 GLU A OE2 1 
ATOM   3999 N  N   . GLY B 1 237 ? -11.468 19.471  4.883   1.00 38.76 ? 237 GLY A N   1 
ATOM   4000 C  CA  . GLY B 1 237 ? -10.598 20.672  4.788   1.00 39.02 ? 237 GLY A CA  1 
ATOM   4001 C  C   . GLY B 1 237 ? -9.091  20.441  4.715   1.00 39.05 ? 237 GLY A C   1 
ATOM   4002 O  O   . GLY B 1 237 ? -8.308  21.378  4.478   1.00 39.71 ? 237 GLY A O   1 
ATOM   4003 N  N   . GLU B 1 238 ? -8.671  19.198  4.941   1.00 38.58 ? 238 GLU A N   1 
ATOM   4004 C  CA  . GLU B 1 238 ? -7.279  18.765  4.770   1.00 37.39 ? 238 GLU A CA  1 
ATOM   4005 C  C   . GLU B 1 238 ? -7.156  18.292  3.304   1.00 35.83 ? 238 GLU A C   1 
ATOM   4006 O  O   . GLU B 1 238 ? -8.105  17.749  2.745   1.00 35.47 ? 238 GLU A O   1 
ATOM   4007 C  CB  . GLU B 1 238 ? -7.024  17.616  5.769   1.00 37.35 ? 238 GLU A CB  1 
ATOM   4008 C  CG  . GLU B 1 238 ? -5.627  17.011  5.871   1.00 37.95 ? 238 GLU A CG  1 
ATOM   4009 C  CD  . GLU B 1 238 ? -5.570  15.802  6.886   1.00 40.50 ? 238 GLU A CD  1 
ATOM   4010 O  OE1 . GLU B 1 238 ? -6.614  15.489  7.560   1.00 43.02 ? 238 GLU A OE1 1 
ATOM   4011 O  OE2 . GLU B 1 238 ? -4.473  15.170  7.016   1.00 41.66 ? 238 GLU A OE2 1 
ATOM   4012 N  N   . ALA B 1 239 ? -6.019  18.512  2.658   1.00 34.31 ? 239 ALA A N   1 
ATOM   4013 C  CA  . ALA B 1 239 ? -5.794  17.930  1.311   1.00 31.94 ? 239 ALA A CA  1 
ATOM   4014 C  C   . ALA B 1 239 ? -6.077  16.380  1.233   1.00 30.15 ? 239 ALA A C   1 
ATOM   4015 O  O   . ALA B 1 239 ? -5.461  15.588  1.964   1.00 30.31 ? 239 ALA A O   1 
ATOM   4016 C  CB  . ALA B 1 239 ? -4.351  18.263  0.823   1.00 32.25 ? 239 ALA A CB  1 
ATOM   4017 N  N   . ALA B 1 240 ? -6.999  15.983  0.353   1.00 27.21 ? 240 ALA A N   1 
ATOM   4018 C  CA  . ALA B 1 240 ? -7.461  14.585  0.264   1.00 25.24 ? 240 ALA A CA  1 
ATOM   4019 C  C   . ALA B 1 240 ? -6.382  13.523  -0.016  1.00 23.02 ? 240 ALA A C   1 
ATOM   4020 O  O   . ALA B 1 240 ? -5.477  13.683  -0.866  1.00 21.98 ? 240 ALA A O   1 
ATOM   4021 C  CB  . ALA B 1 240 ? -8.635  14.459  -0.679  1.00 24.54 ? 240 ALA A CB  1 
ATOM   4022 N  N   . ALA B 1 241 ? -6.455  12.427  0.734   1.00 19.97 ? 241 ALA A N   1 
ATOM   4023 C  CA  . ALA B 1 241 ? -5.607  11.278  0.446   1.00 18.23 ? 241 ALA A CA  1 
ATOM   4024 C  C   . ALA B 1 241 ? -6.437  10.051  0.770   1.00 17.46 ? 241 ALA A C   1 
ATOM   4025 O  O   . ALA B 1 241 ? -7.196  10.064  1.770   1.00 15.42 ? 241 ALA A O   1 
ATOM   4026 C  CB  . ALA B 1 241 ? -4.346  11.295  1.237   1.00 15.37 ? 241 ALA A CB  1 
ATOM   4027 N  N   . PHE B 1 242 ? -6.354  9.069   -0.126  1.00 16.54 ? 242 PHE A N   1 
ATOM   4028 C  CA  . PHE B 1 242 ? -7.184  7.864   -0.018  1.00 17.35 ? 242 PHE A CA  1 
ATOM   4029 C  C   . PHE B 1 242 ? -6.539  6.767   0.824   1.00 16.54 ? 242 PHE A C   1 
ATOM   4030 O  O   . PHE B 1 242 ? -5.301  6.541   0.783   1.00 14.67 ? 242 PHE A O   1 
ATOM   4031 C  CB  . PHE B 1 242 ? -7.598  7.323   -1.393  1.00 17.22 ? 242 PHE A CB  1 
ATOM   4032 C  CG  . PHE B 1 242 ? -8.402  8.296   -2.188  1.00 20.16 ? 242 PHE A CG  1 
ATOM   4033 C  CD1 . PHE B 1 242 ? -7.780  9.199   -3.077  1.00 17.93 ? 242 PHE A CD1 1 
ATOM   4034 C  CD2 . PHE B 1 242 ? -9.778  8.356   -2.019  1.00 18.95 ? 242 PHE A CD2 1 
ATOM   4035 C  CE1 . PHE B 1 242 ? -8.561  10.131  -3.760  1.00 20.32 ? 242 PHE A CE1 1 
ATOM   4036 C  CE2 . PHE B 1 242 ? -10.542 9.264   -2.719  1.00 20.66 ? 242 PHE A CE2 1 
ATOM   4037 C  CZ  . PHE B 1 242 ? -9.939  10.159  -3.570  1.00 19.47 ? 242 PHE A CZ  1 
ATOM   4038 N  N   . LEU B 1 243 ? -7.392  6.029   1.530   1.00 16.41 ? 243 LEU A N   1 
ATOM   4039 C  CA  . LEU B 1 243 ? -6.865  4.931   2.324   1.00 15.43 ? 243 LEU A CA  1 
ATOM   4040 C  C   . LEU B 1 243 ? -6.843  3.651   1.441   1.00 14.18 ? 243 LEU A C   1 
ATOM   4041 O  O   . LEU B 1 243 ? -7.709  2.767   1.555   1.00 12.09 ? 243 LEU A O   1 
ATOM   4042 C  CB  . LEU B 1 243 ? -7.770  4.745   3.586   1.00 16.21 ? 243 LEU A CB  1 
ATOM   4043 C  CG  . LEU B 1 243 ? -7.387  3.754   4.695   1.00 14.36 ? 243 LEU A CG  1 
ATOM   4044 C  CD1 . LEU B 1 243 ? -6.056  4.181   5.295   1.00 9.93  ? 243 LEU A CD1 1 
ATOM   4045 C  CD2 . LEU B 1 243 ? -8.469  3.673   5.790   1.00 12.22 ? 243 LEU A CD2 1 
ATOM   4046 N  N   . VAL B 1 244 ? -5.927  3.602   0.491   1.00 12.85 ? 244 VAL A N   1 
ATOM   4047 C  CA  . VAL B 1 244 ? -5.953  2.487   -0.464  1.00 12.80 ? 244 VAL A CA  1 
ATOM   4048 C  C   . VAL B 1 244 ? -5.408  1.184   0.167   1.00 12.02 ? 244 VAL A C   1 
ATOM   4049 O  O   . VAL B 1 244 ? -5.571  0.086   -0.381  1.00 11.43 ? 244 VAL A O   1 
ATOM   4050 C  CB  . VAL B 1 244 ? -5.230  2.898   -1.817  1.00 12.85 ? 244 VAL A CB  1 
ATOM   4051 C  CG1 . VAL B 1 244 ? -5.925  4.122   -2.457  1.00 11.97 ? 244 VAL A CG1 1 
ATOM   4052 C  CG2 . VAL B 1 244 ? -3.792  3.182   -1.591  1.00 13.68 ? 244 VAL A CG2 1 
ATOM   4053 N  N   . SER B 1 245 ? -4.681  1.316   1.284   1.00 11.12 ? 245 SER A N   1 
ATOM   4054 C  CA  . SER B 1 245 ? -4.024  0.163   1.934   1.00 11.91 ? 245 SER A CA  1 
ATOM   4055 C  C   . SER B 1 245 ? -3.803  0.521   3.413   1.00 12.50 ? 245 SER A C   1 
ATOM   4056 O  O   . SER B 1 245 ? -3.393  1.604   3.740   1.00 11.18 ? 245 SER A O   1 
ATOM   4057 C  CB  . SER B 1 245 ? -2.616  -0.035  1.294   1.00 11.57 ? 245 SER A CB  1 
ATOM   4058 O  OG  . SER B 1 245 ? -2.095  -1.269  1.730   1.00 13.44 ? 245 SER A OG  1 
ATOM   4059 N  N   . ASN B 1 246 ? -4.138  -0.394  4.315   1.00 12.85 ? 246 ASN A N   1 
ATOM   4060 C  CA  . ASN B 1 246 ? -4.005  -0.153  5.745   1.00 12.22 ? 246 ASN A CA  1 
ATOM   4061 C  C   . ASN B 1 246 ? -3.659  -1.462  6.497   1.00 12.90 ? 246 ASN A C   1 
ATOM   4062 O  O   . ASN B 1 246 ? -4.248  -1.769  7.551   1.00 12.00 ? 246 ASN A O   1 
ATOM   4063 C  CB  . ASN B 1 246 ? -5.319  0.491   6.300   1.00 11.02 ? 246 ASN A CB  1 
ATOM   4064 C  CG  . ASN B 1 246 ? -6.544  -0.436  6.141   1.00 12.12 ? 246 ASN A CG  1 
ATOM   4065 O  OD1 . ASN B 1 246 ? -6.515  -1.374  5.363   1.00 13.26 ? 246 ASN A OD1 1 
ATOM   4066 N  ND2 . ASN B 1 246 ? -7.600  -0.193  6.918   1.00 10.04 ? 246 ASN A ND2 1 
ATOM   4067 N  N   . HIS B 1 247 ? -2.648  -2.198  6.017   1.00 13.05 ? 247 HIS A N   1 
ATOM   4068 C  CA  . HIS B 1 247 ? -2.329  -3.449  6.677   1.00 13.67 ? 247 HIS A CA  1 
ATOM   4069 C  C   . HIS B 1 247 ? -0.888  -3.308  7.061   1.00 14.21 ? 247 HIS A C   1 
ATOM   4070 O  O   . HIS B 1 247 ? -0.097  -2.676  6.322   1.00 14.44 ? 247 HIS A O   1 
ATOM   4071 C  CB  . HIS B 1 247 ? -2.607  -4.696  5.769   1.00 12.16 ? 247 HIS A CB  1 
ATOM   4072 C  CG  . HIS B 1 247 ? -1.898  -4.648  4.431   1.00 15.74 ? 247 HIS A CG  1 
ATOM   4073 N  ND1 . HIS B 1 247 ? -0.677  -5.260  4.194   1.00 16.72 ? 247 HIS A ND1 1 
ATOM   4074 C  CD2 . HIS B 1 247 ? -2.236  -4.019  3.269   1.00 9.69  ? 247 HIS A CD2 1 
ATOM   4075 C  CE1 . HIS B 1 247 ? -0.286  -4.992  2.949   1.00 13.46 ? 247 HIS A CE1 1 
ATOM   4076 N  NE2 . HIS B 1 247 ? -1.220  -4.251  2.376   1.00 14.44 ? 247 HIS A NE2 1 
ATOM   4077 N  N   . ARG B 1 248 ? -0.545  -3.847  8.235   1.00 12.72 ? 248 ARG A N   1 
ATOM   4078 C  CA  . ARG B 1 248 ? 0.824   -3.768  8.727   1.00 14.26 ? 248 ARG A CA  1 
ATOM   4079 C  C   . ARG B 1 248 ? 1.560   -5.023  8.267   1.00 14.20 ? 248 ARG A C   1 
ATOM   4080 O  O   . ARG B 1 248 ? 0.951   -6.123  8.251   1.00 13.77 ? 248 ARG A O   1 
ATOM   4081 C  CB  . ARG B 1 248 ? 0.844   -3.638  10.290  1.00 15.55 ? 248 ARG A CB  1 
ATOM   4082 C  CG  . ARG B 1 248 ? 2.284   -3.756  10.888  1.00 13.90 ? 248 ARG A CG  1 
ATOM   4083 C  CD  . ARG B 1 248 ? 2.265   -3.791  12.426  1.00 12.77 ? 248 ARG A CD  1 
ATOM   4084 N  NE  . ARG B 1 248 ? 3.525   -3.268  12.952  1.00 16.65 ? 248 ARG A NE  1 
ATOM   4085 C  CZ  . ARG B 1 248 ? 4.019   -3.546  14.167  1.00 15.92 ? 248 ARG A CZ  1 
ATOM   4086 N  NH1 . ARG B 1 248 ? 3.386   -4.406  14.975  1.00 14.52 ? 248 ARG A NH1 1 
ATOM   4087 N  NH2 . ARG B 1 248 ? 5.153   -2.969  14.558  1.00 15.38 ? 248 ARG A NH2 1 
ATOM   4088 N  N   . PRO B 1 249 ? 2.872   -4.885  7.854   1.00 14.65 ? 249 PRO A N   1 
ATOM   4089 C  CA  . PRO B 1 249 ? 3.659   -6.071  7.526   1.00 16.07 ? 249 PRO A CA  1 
ATOM   4090 C  C   . PRO B 1 249 ? 3.795   -7.062  8.695   1.00 16.83 ? 249 PRO A C   1 
ATOM   4091 O  O   . PRO B 1 249 ? 3.651   -6.652  9.845   1.00 15.64 ? 249 PRO A O   1 
ATOM   4092 C  CB  . PRO B 1 249 ? 5.086   -5.475  7.137   1.00 15.69 ? 249 PRO A CB  1 
ATOM   4093 C  CG  . PRO B 1 249 ? 4.796   -4.060  6.733   1.00 16.35 ? 249 PRO A CG  1 
ATOM   4094 C  CD  . PRO B 1 249 ? 3.637   -3.628  7.656   1.00 14.99 ? 249 PRO A CD  1 
ATOM   4095 N  N   . PRO B 1 250 ? 4.089   -8.350  8.407   1.00 17.35 ? 250 PRO A N   1 
ATOM   4096 C  CA  . PRO B 1 250 ? 4.206   -9.357  9.482   1.00 17.64 ? 250 PRO A CA  1 
ATOM   4097 C  C   . PRO B 1 250 ? 5.475   -9.102  10.321  1.00 16.18 ? 250 PRO A C   1 
ATOM   4098 O  O   . PRO B 1 250 ? 6.435   -8.468  9.813   1.00 15.42 ? 250 PRO A O   1 
ATOM   4099 C  CB  . PRO B 1 250 ? 4.273   -10.683 8.707   1.00 16.13 ? 250 PRO A CB  1 
ATOM   4100 C  CG  . PRO B 1 250 ? 3.690   -10.337 7.304   1.00 21.80 ? 250 PRO A CG  1 
ATOM   4101 C  CD  . PRO B 1 250 ? 4.343   -8.981  7.095   1.00 18.69 ? 250 PRO A CD  1 
ATOM   4102 N  N   . GLN B 1 251 ? 5.444   -9.460  11.600  1.00 15.34 ? 251 GLN A N   1 
ATOM   4103 C  CA  . GLN B 1 251 ? 6.472   -9.009  12.513  1.00 15.14 ? 251 GLN A CA  1 
ATOM   4104 C  C   . GLN B 1 251 ? 7.173   -10.275 13.016  1.00 15.69 ? 251 GLN A C   1 
ATOM   4105 O  O   . GLN B 1 251 ? 6.571   -11.345 12.953  1.00 15.45 ? 251 GLN A O   1 
ATOM   4106 C  CB  . GLN B 1 251 ? 5.808   -8.263  13.662  1.00 15.94 ? 251 GLN A CB  1 
ATOM   4107 C  CG  . GLN B 1 251 ? 5.117   -6.921  13.216  1.00 12.49 ? 251 GLN A CG  1 
ATOM   4108 C  CD  . GLN B 1 251 ? 6.120   -5.938  12.541  1.00 19.42 ? 251 GLN A CD  1 
ATOM   4109 O  OE1 . GLN B 1 251 ? 7.246   -5.729  13.031  1.00 22.49 ? 251 GLN A OE1 1 
ATOM   4110 N  NE2 . GLN B 1 251 ? 5.735   -5.394  11.400  1.00 15.98 ? 251 GLN A NE2 1 
ATOM   4111 N  N   . PRO B 1 252 ? 8.452   -10.167 13.489  1.00 17.03 ? 252 PRO A N   1 
ATOM   4112 C  CA  . PRO B 1 252 ? 9.181   -11.345 13.967  1.00 16.68 ? 252 PRO A CA  1 
ATOM   4113 C  C   . PRO B 1 252 ? 8.453   -12.096 15.102  1.00 16.57 ? 252 PRO A C   1 
ATOM   4114 O  O   . PRO B 1 252 ? 8.026   -11.485 16.102  1.00 15.62 ? 252 PRO A O   1 
ATOM   4115 C  CB  . PRO B 1 252 ? 10.523  -10.744 14.479  1.00 18.30 ? 252 PRO A CB  1 
ATOM   4116 C  CG  . PRO B 1 252 ? 10.607  -9.365  13.817  1.00 19.25 ? 252 PRO A CG  1 
ATOM   4117 C  CD  . PRO B 1 252 ? 9.240   -8.917  13.602  1.00 14.88 ? 252 PRO A CD  1 
ATOM   4118 N  N   . LEU B 1 253 ? 8.336   -13.409 14.956  1.00 17.23 ? 253 LEU A N   1 
ATOM   4119 C  CA  . LEU B 1 253 ? 7.718   -14.271 15.951  1.00 18.27 ? 253 LEU A CA  1 
ATOM   4120 C  C   . LEU B 1 253 ? 8.444   -14.275 17.325  1.00 18.25 ? 253 LEU A C   1 
ATOM   4121 O  O   . LEU B 1 253 ? 7.800   -14.296 18.425  1.00 17.66 ? 253 LEU A O   1 
ATOM   4122 C  CB  . LEU B 1 253 ? 7.509   -15.683 15.357  1.00 18.86 ? 253 LEU A CB  1 
ATOM   4123 C  CG  . LEU B 1 253 ? 6.477   -16.600 16.044  1.00 18.03 ? 253 LEU A CG  1 
ATOM   4124 C  CD1 . LEU B 1 253 ? 5.175   -15.903 16.294  1.00 21.24 ? 253 LEU A CD1 1 
ATOM   4125 C  CD2 . LEU B 1 253 ? 6.285   -17.855 15.278  1.00 20.41 ? 253 LEU A CD2 1 
ATOM   4126 N  N   . LYS B 1 254 ? 9.784   -14.167 17.255  1.00 18.37 ? 254 LYS A N   1 
ATOM   4127 C  CA  . LYS B 1 254 ? 10.628  -14.118 18.412  1.00 18.14 ? 254 LYS A CA  1 
ATOM   4128 C  C   . LYS B 1 254 ? 10.317  -15.209 19.494  1.00 17.69 ? 254 LYS A C   1 
ATOM   4129 O  O   . LYS B 1 254 ? 10.200  -14.916 20.664  1.00 18.36 ? 254 LYS A O   1 
ATOM   4130 C  CB  . LYS B 1 254 ? 10.598  -12.715 18.975  1.00 18.46 ? 254 LYS A CB  1 
ATOM   4131 C  CG  . LYS B 1 254 ? 11.595  -11.830 18.271  1.00 23.30 ? 254 LYS A CG  1 
ATOM   4132 C  CD  . LYS B 1 254 ? 11.358  -10.441 18.513  1.00 20.97 ? 254 LYS A CD  1 
ATOM   4133 C  CE  . LYS B 1 254 ? 12.416  -9.718  17.695  1.00 21.88 ? 254 LYS A CE  1 
ATOM   4134 N  NZ  . LYS B 1 254 ? 12.596  -8.403  18.273  1.00 25.95 ? 254 LYS A NZ  1 
ATOM   4135 N  N   . GLY B 1 255 ? 10.179  -16.465 19.085  1.00 18.05 ? 255 GLY A N   1 
ATOM   4136 C  CA  . GLY B 1 255 ? 10.070  -17.556 20.067  1.00 18.14 ? 255 GLY A CA  1 
ATOM   4137 C  C   . GLY B 1 255 ? 8.664   -17.848 20.574  1.00 18.48 ? 255 GLY A C   1 
ATOM   4138 O  O   . GLY B 1 255 ? 8.460   -18.812 21.376  1.00 17.60 ? 255 GLY A O   1 
ATOM   4139 N  N   . ARG B 1 256 ? 7.681   -17.037 20.125  1.00 17.58 ? 256 ARG A N   1 
ATOM   4140 C  CA  . ARG B 1 256 ? 6.298   -17.315 20.473  1.00 16.48 ? 256 ARG A CA  1 
ATOM   4141 C  C   . ARG B 1 256 ? 5.786   -18.591 19.891  1.00 18.77 ? 256 ARG A C   1 
ATOM   4142 O  O   . ARG B 1 256 ? 6.136   -18.991 18.766  1.00 18.17 ? 256 ARG A O   1 
ATOM   4143 C  CB  . ARG B 1 256 ? 5.367   -16.151 20.088  1.00 18.50 ? 256 ARG A CB  1 
ATOM   4144 C  CG  . ARG B 1 256 ? 5.556   -14.933 20.978  1.00 15.44 ? 256 ARG A CG  1 
ATOM   4145 C  CD  . ARG B 1 256 ? 4.845   -13.726 20.469  1.00 18.56 ? 256 ARG A CD  1 
ATOM   4146 N  NE  . ARG B 1 256 ? 5.445   -13.192 19.234  1.00 17.46 ? 256 ARG A NE  1 
ATOM   4147 C  CZ  . ARG B 1 256 ? 4.846   -12.289 18.441  1.00 11.41 ? 256 ARG A CZ  1 
ATOM   4148 N  NH1 . ARG B 1 256 ? 3.657   -11.830 18.761  1.00 9.12  ? 256 ARG A NH1 1 
ATOM   4149 N  NH2 . ARG B 1 256 ? 5.465   -11.801 17.355  1.00 12.74 ? 256 ARG A NH2 1 
ATOM   4150 N  N   . LYS B 1 257 ? 4.902   -19.251 20.632  1.00 18.61 ? 257 LYS A N   1 
ATOM   4151 C  CA  . LYS B 1 257 ? 4.324   -20.464 20.112  1.00 19.80 ? 257 LYS A CA  1 
ATOM   4152 C  C   . LYS B 1 257 ? 2.931   -20.153 19.482  1.00 18.04 ? 257 LYS A C   1 
ATOM   4153 O  O   . LYS B 1 257 ? 2.084   -19.548 20.105  1.00 15.75 ? 257 LYS A O   1 
ATOM   4154 C  CB  . LYS B 1 257 ? 4.249   -21.442 21.299  1.00 21.94 ? 257 LYS A CB  1 
ATOM   4155 C  CG  . LYS B 1 257 ? 3.463   -22.692 21.041  1.00 24.81 ? 257 LYS A CG  1 
ATOM   4156 C  CD  . LYS B 1 257 ? 3.025   -23.351 22.392  1.00 22.59 ? 257 LYS A CD  1 
ATOM   4157 C  CE  . LYS B 1 257 ? 4.198   -23.829 23.292  1.00 28.53 ? 257 LYS A CE  1 
ATOM   4158 N  NZ  . LYS B 1 257 ? 3.652   -24.832 24.287  1.00 28.55 ? 257 LYS A NZ  1 
ATOM   4159 N  N   . VAL B 1 258 ? 2.755   -20.489 18.213  1.00 17.17 ? 258 VAL A N   1 
ATOM   4160 C  CA  . VAL B 1 258 ? 1.490   -20.382 17.561  1.00 16.72 ? 258 VAL A CA  1 
ATOM   4161 C  C   . VAL B 1 258 ? 0.842   -21.761 17.697  1.00 17.12 ? 258 VAL A C   1 
ATOM   4162 O  O   . VAL B 1 258 ? 1.432   -22.768 17.346  1.00 18.11 ? 258 VAL A O   1 
ATOM   4163 C  CB  . VAL B 1 258 ? 1.640   -20.016 16.036  1.00 16.00 ? 258 VAL A CB  1 
ATOM   4164 C  CG1 . VAL B 1 258 ? 0.260   -19.750 15.441  1.00 15.83 ? 258 VAL A CG1 1 
ATOM   4165 C  CG2 . VAL B 1 258 ? 2.476   -18.739 15.882  1.00 19.35 ? 258 VAL A CG2 1 
ATOM   4166 N  N   . ARG B 1 259 ? -0.393  -21.798 18.199  1.00 15.65 ? 259 ARG A N   1 
ATOM   4167 C  CA  . ARG B 1 259 ? -1.087  -23.066 18.459  1.00 14.81 ? 259 ARG A CA  1 
ATOM   4168 C  C   . ARG B 1 259 ? -2.291  -23.173 17.523  1.00 15.67 ? 259 ARG A C   1 
ATOM   4169 O  O   . ARG B 1 259 ? -2.822  -22.133 17.098  1.00 13.92 ? 259 ARG A O   1 
ATOM   4170 C  CB  . ARG B 1 259 ? -1.548  -23.076 19.909  1.00 12.98 ? 259 ARG A CB  1 
ATOM   4171 C  CG  . ARG B 1 259 ? -0.368  -23.233 20.829  1.00 13.12 ? 259 ARG A CG  1 
ATOM   4172 C  CD  . ARG B 1 259 ? -0.793  -23.141 22.304  1.00 15.20 ? 259 ARG A CD  1 
ATOM   4173 N  NE  . ARG B 1 259 ? -1.471  -21.923 22.715  1.00 11.88 ? 259 ARG A NE  1 
ATOM   4174 C  CZ  . ARG B 1 259 ? -2.363  -21.867 23.746  1.00 13.77 ? 259 ARG A CZ  1 
ATOM   4175 N  NH1 . ARG B 1 259 ? -2.760  -23.004 24.413  1.00 14.64 ? 259 ARG A NH1 1 
ATOM   4176 N  NH2 . ARG B 1 259 ? -2.848  -20.689 24.130  1.00 11.87 ? 259 ARG A NH2 1 
ATOM   4177 N  N   . ALA B 1 260 ? -2.686  -24.404 17.196  1.00 15.15 ? 260 ALA A N   1 
ATOM   4178 C  CA  . ALA B 1 260 ? -3.870  -24.676 16.355  1.00 14.10 ? 260 ALA A CA  1 
ATOM   4179 C  C   . ALA B 1 260 ? -4.907  -25.358 17.207  1.00 16.02 ? 260 ALA A C   1 
ATOM   4180 O  O   . ALA B 1 260 ? -4.571  -26.229 18.005  1.00 16.47 ? 260 ALA A O   1 
ATOM   4181 C  CB  . ALA B 1 260 ? -3.540  -25.556 15.172  1.00 13.69 ? 260 ALA A CB  1 
ATOM   4182 N  N   . SER B 1 261 ? -6.187  -25.031 17.001  1.00 15.15 ? 261 SER A N   1 
ATOM   4183 C  CA  . SER B 1 261 ? -7.268  -25.686 17.746  1.00 15.06 ? 261 SER A CA  1 
ATOM   4184 C  C   . SER B 1 261 ? -7.734  -26.985 17.020  1.00 16.89 ? 261 SER A C   1 
ATOM   4185 O  O   . SER B 1 261 ? -8.759  -27.617 17.404  1.00 15.90 ? 261 SER A O   1 
ATOM   4186 C  CB  . SER B 1 261 ? -8.448  -24.737 17.819  1.00 16.19 ? 261 SER A CB  1 
ATOM   4187 O  OG  . SER B 1 261 ? -9.107  -24.691 16.537  1.00 12.74 ? 261 SER A OG  1 
ATOM   4188 N  N   . PHE B 1 262 ? -7.024  -27.345 15.934  1.00 17.83 ? 262 PHE A N   1 
ATOM   4189 C  CA  . PHE B 1 262 ? -7.502  -28.399 15.042  1.00 20.60 ? 262 PHE A CA  1 
ATOM   4190 C  C   . PHE B 1 262 ? -6.268  -29.086 14.520  1.00 22.64 ? 262 PHE A C   1 
ATOM   4191 O  O   . PHE B 1 262 ? -5.178  -28.513 14.543  1.00 21.47 ? 262 PHE A O   1 
ATOM   4192 C  CB  . PHE B 1 262 ? -8.258  -27.796 13.873  1.00 19.80 ? 262 PHE A CB  1 
ATOM   4193 C  CG  . PHE B 1 262 ? -7.421  -26.904 13.047  1.00 19.51 ? 262 PHE A CG  1 
ATOM   4194 C  CD1 . PHE B 1 262 ? -6.853  -27.382 11.843  1.00 17.05 ? 262 PHE A CD1 1 
ATOM   4195 C  CD2 . PHE B 1 262 ? -7.169  -25.575 13.462  1.00 13.48 ? 262 PHE A CD2 1 
ATOM   4196 C  CE1 . PHE B 1 262 ? -6.055  -26.547 11.056  1.00 19.16 ? 262 PHE A CE1 1 
ATOM   4197 C  CE2 . PHE B 1 262 ? -6.369  -24.706 12.670  1.00 15.87 ? 262 PHE A CE2 1 
ATOM   4198 C  CZ  . PHE B 1 262 ? -5.815  -25.185 11.474  1.00 17.97 ? 262 PHE A CZ  1 
ATOM   4199 N  N   . HIS B 1 263 ? -6.455  -30.302 14.020  1.00 24.81 ? 263 HIS A N   1 
ATOM   4200 C  CA  . HIS B 1 263 ? -5.351  -31.055 13.428  1.00 28.29 ? 263 HIS A CA  1 
ATOM   4201 C  C   . HIS B 1 263 ? -5.926  -32.008 12.390  1.00 30.47 ? 263 HIS A C   1 
ATOM   4202 O  O   . HIS B 1 263 ? -5.156  -32.692 11.661  1.00 31.14 ? 263 HIS A O   1 
ATOM   4203 C  CB  . HIS B 1 263 ? -4.518  -31.776 14.513  1.00 28.72 ? 263 HIS A CB  1 
ATOM   4204 C  CG  . HIS B 1 263 ? -5.286  -32.756 15.340  1.00 33.23 ? 263 HIS A CG  1 
ATOM   4205 N  ND1 . HIS B 1 263 ? -4.662  -33.651 16.185  1.00 38.93 ? 263 HIS A ND1 1 
ATOM   4206 C  CD2 . HIS B 1 263 ? -6.616  -32.983 15.472  1.00 35.92 ? 263 HIS A CD2 1 
ATOM   4207 C  CE1 . HIS B 1 263 ? -5.578  -34.389 16.791  1.00 38.30 ? 263 HIS A CE1 1 
ATOM   4208 N  NE2 . HIS B 1 263 ? -6.768  -34.015 16.361  1.00 35.66 ? 263 HIS A NE2 1 
ATOM   4209 O  OXT . HIS B 1 263 ? -7.190  -32.047 12.253  1.00 30.62 ? 263 HIS A OXT 1 
HETATM 4210 ZN ZN  . ZN  C 2 .   ? -34.368 -35.567 27.162  1.00 11.49 ? 301 ZN  B ZN  1 
HETATM 4211 O  O20 . V13 D 3 .   ? -38.815 -33.083 20.504  1.00 24.67 ? 302 V13 B O20 1 
HETATM 4212 S  S15 . V13 D 3 .   ? -39.497 -34.038 21.460  1.00 24.96 ? 302 V13 B S15 1 
HETATM 4213 O  O19 . V13 D 3 .   ? -40.178 -33.016 22.364  1.00 24.55 ? 302 V13 B O19 1 
HETATM 4214 C  C16 . V13 D 3 .   ? -40.780 -34.963 20.591  1.00 29.20 ? 302 V13 B C16 1 
HETATM 4215 C  C17 . V13 D 3 .   ? -40.065 -36.212 20.165  1.00 30.35 ? 302 V13 B C17 1 
HETATM 4216 O  O18 . V13 D 3 .   ? -40.092 -37.056 21.269  1.00 35.94 ? 302 V13 B O18 1 
HETATM 4217 C  C1  . V13 D 3 .   ? -38.082 -34.838 22.324  1.00 19.55 ? 302 V13 B C1  1 
HETATM 4218 C  C6  . V13 D 3 .   ? -36.910 -35.226 21.641  1.00 16.90 ? 302 V13 B C6  1 
HETATM 4219 F  F11 . V13 D 3 .   ? -36.755 -34.967 20.337  1.00 19.54 ? 302 V13 B F11 1 
HETATM 4220 C  C5  . V13 D 3 .   ? -35.858 -35.852 22.290  1.00 17.04 ? 302 V13 B C5  1 
HETATM 4221 F  F12 . V13 D 3 .   ? -34.722 -36.154 21.629  1.00 15.99 ? 302 V13 B F12 1 
HETATM 4222 C  C4  . V13 D 3 .   ? -35.978 -36.140 23.667  1.00 14.90 ? 302 V13 B C4  1 
HETATM 4223 S  S7  . V13 D 3 .   ? -34.576 -36.918 24.437  1.00 12.67 ? 302 V13 B S7  1 
HETATM 4224 O  O9  . V13 D 3 .   ? -33.573 -35.908 24.242  1.00 8.90  ? 302 V13 B O9  1 
HETATM 4225 N  N10 . V13 D 3 .   ? -34.730 -37.132 26.132  1.00 13.25 ? 302 V13 B N10 1 
HETATM 4226 O  O8  . V13 D 3 .   ? -34.251 -38.230 23.783  1.00 10.91 ? 302 V13 B O8  1 
HETATM 4227 C  C3  . V13 D 3 .   ? -37.144 -35.785 24.329  1.00 13.65 ? 302 V13 B C3  1 
HETATM 4228 F  F13 . V13 D 3 .   ? -37.403 -36.064 25.586  1.00 14.85 ? 302 V13 B F13 1 
HETATM 4229 C  C2  . V13 D 3 .   ? -38.181 -35.174 23.643  1.00 15.49 ? 302 V13 B C2  1 
HETATM 4230 F  F14 . V13 D 3 .   ? -39.275 -34.873 24.327  1.00 18.37 ? 302 V13 B F14 1 
HETATM 4231 C  C1  . EDO E 4 .   ? -37.345 -40.918 40.972  1.00 31.65 ? 303 EDO B C1  1 
HETATM 4232 O  O1  . EDO E 4 .   ? -36.480 -39.792 40.945  1.00 29.51 ? 303 EDO B O1  1 
HETATM 4233 C  C2  . EDO E 4 .   ? -36.809 -42.294 40.735  1.00 36.41 ? 303 EDO B C2  1 
HETATM 4234 O  O2  . EDO E 4 .   ? -35.442 -42.586 40.512  1.00 34.03 ? 303 EDO B O2  1 
HETATM 4235 C  C1  . EDO F 4 .   ? -50.764 -43.160 37.602  1.00 48.27 ? 304 EDO B C1  1 
HETATM 4236 O  O1  . EDO F 4 .   ? -50.030 -44.331 37.822  1.00 48.04 ? 304 EDO B O1  1 
HETATM 4237 C  C2  . EDO F 4 .   ? -51.244 -42.947 36.247  1.00 49.20 ? 304 EDO B C2  1 
HETATM 4238 O  O2  . EDO F 4 .   ? -50.884 -43.950 35.383  1.00 47.79 ? 304 EDO B O2  1 
HETATM 4239 ZN ZN  . ZN  G 2 .   ? -7.050  -4.604  12.997  1.00 12.42 ? 301 ZN  A ZN  1 
HETATM 4240 O  O20 . V13 H 3 .   ? -10.380 -0.198  19.230  1.00 28.98 ? 302 V13 A O20 1 
HETATM 4241 S  S15 . V13 H 3 .   ? -9.028  0.401   18.703  1.00 24.32 ? 302 V13 A S15 1 
HETATM 4242 O  O19 . V13 H 3 .   ? -9.554  1.396   17.709  1.00 23.92 ? 302 V13 A O19 1 
HETATM 4243 C  C16 . V13 H 3 .   ? -8.128  1.181   20.067  1.00 27.63 ? 302 V13 A C16 1 
HETATM 4244 C  C17 . V13 H 3 .   ? -7.098  1.996   19.331  1.00 31.72 ? 302 V13 A C17 1 
HETATM 4245 O  O18 . V13 H 3 .   ? -6.271  1.100   18.682  1.00 34.60 ? 302 V13 A O18 1 
HETATM 4246 C  C1  . V13 H 3 .   ? -8.236  -0.970  17.881  1.00 21.34 ? 302 V13 A C1  1 
HETATM 4247 C  C6  . V13 H 3 .   ? -7.776  -0.817  16.551  1.00 19.17 ? 302 V13 A C6  1 
HETATM 4248 F  F11 . V13 H 3 .   ? -7.973  0.327   15.840  1.00 19.51 ? 302 V13 A F11 1 
HETATM 4249 C  C5  . V13 H 3 .   ? -7.147  -1.870  15.910  1.00 18.97 ? 302 V13 A C5  1 
HETATM 4250 F  F12 . V13 H 3 .   ? -6.780  -1.645  14.656  1.00 18.86 ? 302 V13 A F12 1 
HETATM 4251 C  C4  . V13 H 3 .   ? -6.892  -3.034  16.612  1.00 15.70 ? 302 V13 A C4  1 
HETATM 4252 S  S7  . V13 H 3 .   ? -6.131  -4.468  15.866  1.00 14.28 ? 302 V13 A S7  1 
HETATM 4253 O  O9  . V13 H 3 .   ? -7.201  -5.461  15.893  1.00 10.56 ? 302 V13 A O9  1 
HETATM 4254 N  N10 . V13 H 3 .   ? -5.745  -4.259  14.170  1.00 15.11 ? 302 V13 A N10 1 
HETATM 4255 O  O8  . V13 H 3 .   ? -4.940  -4.826  16.712  1.00 17.04 ? 302 V13 A O8  1 
HETATM 4256 C  C3  . V13 H 3 .   ? -7.349  -3.149  17.934  1.00 17.31 ? 302 V13 A C3  1 
HETATM 4257 F  F13 . V13 H 3 .   ? -7.210  -4.283  18.636  1.00 15.91 ? 302 V13 A F13 1 
HETATM 4258 C  C2  . V13 H 3 .   ? -7.995  -2.116  18.589  1.00 19.65 ? 302 V13 A C2  1 
HETATM 4259 F  F14 . V13 H 3 .   ? -8.325  -2.336  19.875  1.00 19.49 ? 302 V13 A F14 1 
HETATM 4260 C  C1  . PEG I 5 .   ? -25.741 4.466   19.490  1.00 26.86 ? 303 PEG A C1  1 
HETATM 4261 O  O1  . PEG I 5 .   ? -26.133 4.739   20.822  1.00 18.60 ? 303 PEG A O1  1 
HETATM 4262 C  C2  . PEG I 5 .   ? -25.880 5.507   18.382  1.00 23.29 ? 303 PEG A C2  1 
HETATM 4263 O  O2  . PEG I 5 .   ? -26.960 5.115   17.510  1.00 28.53 ? 303 PEG A O2  1 
HETATM 4264 C  C3  . PEG I 5 .   ? -27.117 3.811   16.864  1.00 26.88 ? 303 PEG A C3  1 
HETATM 4265 C  C4  . PEG I 5 .   ? -28.535 3.421   16.472  1.00 27.56 ? 303 PEG A C4  1 
HETATM 4266 O  O4  . PEG I 5 .   ? -29.259 2.325   17.110  1.00 25.45 ? 303 PEG A O4  1 
HETATM 4267 C  C1  . EDO J 4 .   ? -18.209 -26.761 11.295  1.00 35.63 ? 304 EDO A C1  1 
HETATM 4268 O  O1  . EDO J 4 .   ? -17.750 -28.073 11.542  1.00 33.79 ? 304 EDO A O1  1 
HETATM 4269 C  C2  . EDO J 4 .   ? -18.022 -26.158 9.974   1.00 36.65 ? 304 EDO A C2  1 
HETATM 4270 O  O2  . EDO J 4 .   ? -17.370 -26.835 8.955   1.00 37.64 ? 304 EDO A O2  1 
HETATM 4271 C  C1  . EDO K 4 .   ? -21.163 -2.499  -3.800  1.00 33.11 ? 305 EDO A C1  1 
HETATM 4272 O  O1  . EDO K 4 .   ? -21.888 -1.279  -3.859  1.00 36.23 ? 305 EDO A O1  1 
HETATM 4273 C  C2  . EDO K 4 .   ? -20.408 -2.968  -4.933  1.00 30.95 ? 305 EDO A C2  1 
HETATM 4274 O  O2  . EDO K 4 .   ? -20.392 -2.262  -6.129  1.00 31.16 ? 305 EDO A O2  1 
HETATM 4275 C  C1  . EDO L 4 .   ? -32.343 -7.933  20.900  1.00 42.63 ? 306 EDO A C1  1 
HETATM 4276 O  O1  . EDO L 4 .   ? -31.270 -8.279  20.047  1.00 39.76 ? 306 EDO A O1  1 
HETATM 4277 C  C2  . EDO L 4 .   ? -32.124 -7.664  22.331  1.00 44.00 ? 306 EDO A C2  1 
HETATM 4278 O  O2  . EDO L 4 .   ? -30.862 -7.689  22.935  1.00 40.00 ? 306 EDO A O2  1 
HETATM 4279 C  C1  . EDO M 4 .   ? 1.286   -3.145  -0.548  1.00 37.07 ? 307 EDO A C1  1 
HETATM 4280 O  O1  . EDO M 4 .   ? 0.943   -4.493  -0.221  1.00 38.33 ? 307 EDO A O1  1 
HETATM 4281 C  C2  . EDO M 4 .   ? 0.209   -2.150  -0.813  1.00 37.68 ? 307 EDO A C2  1 
HETATM 4282 O  O2  . EDO M 4 .   ? -1.152  -2.478  -0.741  1.00 26.10 ? 307 EDO A O2  1 
HETATM 4283 C  C1  . EDO N 4 .   ? -9.661  -11.189 -7.637  1.00 37.98 ? 308 EDO A C1  1 
HETATM 4284 O  O1  . EDO N 4 .   ? -9.664  -9.773  -7.650  1.00 27.38 ? 308 EDO A O1  1 
HETATM 4285 C  C2  . EDO N 4 .   ? -8.968  -12.160 -6.774  1.00 41.68 ? 308 EDO A C2  1 
HETATM 4286 O  O2  . EDO N 4 .   ? -8.119  -11.875 -5.707  1.00 48.24 ? 308 EDO A O2  1 
HETATM 4287 O  O   . HOH O 6 .   ? -22.465 -31.842 31.403  1.00 12.84 ? 401 HOH B O   1 
HETATM 4288 O  O   . HOH O 6 .   ? -17.353 -30.895 29.478  1.00 16.94 ? 402 HOH B O   1 
HETATM 4289 O  O   . HOH O 6 .   ? -33.195 -23.544 15.021  1.00 15.85 ? 403 HOH B O   1 
HETATM 4290 O  O   . HOH O 6 .   ? -24.702 -17.108 20.634  1.00 15.09 ? 404 HOH B O   1 
HETATM 4291 O  O   . HOH O 6 .   ? -38.592 -40.562 36.695  1.00 11.61 ? 405 HOH B O   1 
HETATM 4292 O  O   . HOH O 6 .   ? -20.079 -20.786 20.086  1.00 14.32 ? 406 HOH B O   1 
HETATM 4293 O  O   . HOH O 6 .   ? -28.949 -45.274 17.344  1.00 16.09 ? 407 HOH B O   1 
HETATM 4294 O  O   . HOH O 6 .   ? -40.990 -47.088 35.927  1.00 22.64 ? 408 HOH B O   1 
HETATM 4295 O  O   . HOH O 6 .   ? -39.359 -36.157 29.743  1.00 11.77 ? 409 HOH B O   1 
HETATM 4296 O  O   . HOH O 6 .   ? -37.152 -39.790 29.934  1.00 12.00 ? 410 HOH B O   1 
HETATM 4297 O  O   . HOH O 6 .   ? -41.178 -32.689 26.744  1.00 20.61 ? 411 HOH B O   1 
HETATM 4298 O  O   . HOH O 6 .   ? -32.089 -42.043 35.185  1.00 13.82 ? 412 HOH B O   1 
HETATM 4299 O  O   . HOH O 6 .   ? -18.050 -23.620 18.424  1.00 14.28 ? 413 HOH B O   1 
HETATM 4300 O  O   . HOH O 6 .   ? -29.988 -50.688 24.584  1.00 16.46 ? 414 HOH B O   1 
HETATM 4301 O  O   . HOH O 6 .   ? -21.132 -41.759 18.601  1.00 16.74 ? 415 HOH B O   1 
HETATM 4302 O  O   . HOH O 6 .   ? -27.469 -56.390 31.232  1.00 15.90 ? 416 HOH B O   1 
HETATM 4303 O  O   . HOH O 6 .   ? -34.702 -32.848 47.119  1.00 20.09 ? 417 HOH B O   1 
HETATM 4304 O  O   . HOH O 6 .   ? -31.702 -22.307 13.139  1.00 11.10 ? 418 HOH B O   1 
HETATM 4305 O  O   . HOH O 6 .   ? -27.853 -39.562 14.634  1.00 19.04 ? 419 HOH B O   1 
HETATM 4306 O  O   . HOH O 6 .   ? -20.731 -31.906 11.150  1.00 21.86 ? 420 HOH B O   1 
HETATM 4307 O  O   . HOH O 6 .   ? -30.278 -40.334 38.209  1.00 20.44 ? 421 HOH B O   1 
HETATM 4308 O  O   . HOH O 6 .   ? -23.623 -39.205 13.852  1.00 22.02 ? 422 HOH B O   1 
HETATM 4309 O  O   . HOH O 6 .   ? -42.568 -25.202 23.272  1.00 19.34 ? 423 HOH B O   1 
HETATM 4310 O  O   . HOH O 6 .   ? -22.183 -21.530 8.483   1.00 16.76 ? 424 HOH B O   1 
HETATM 4311 O  O   . HOH O 6 .   ? -37.870 -47.731 30.239  1.00 15.47 ? 425 HOH B O   1 
HETATM 4312 O  O   . HOH O 6 .   ? -29.188 -11.860 19.693  1.00 19.63 ? 426 HOH B O   1 
HETATM 4313 O  O   . HOH O 6 .   ? -40.979 -31.864 12.016  1.00 24.50 ? 427 HOH B O   1 
HETATM 4314 O  O   . HOH O 6 .   ? -40.453 -33.979 45.024  1.00 18.69 ? 428 HOH B O   1 
HETATM 4315 O  O   . HOH O 6 .   ? -26.951 -15.082 14.365  1.00 21.39 ? 429 HOH B O   1 
HETATM 4316 O  O   . HOH O 6 .   ? -24.994 -54.635 28.147  1.00 16.42 ? 430 HOH B O   1 
HETATM 4317 O  O   . HOH O 6 .   ? -54.272 -30.808 36.021  1.00 23.73 ? 431 HOH B O   1 
HETATM 4318 O  O   . HOH O 6 .   ? -36.098 -47.216 16.336  1.00 14.79 ? 432 HOH B O   1 
HETATM 4319 O  O   . HOH O 6 .   ? -16.536 -22.348 26.271  1.00 14.67 ? 433 HOH B O   1 
HETATM 4320 O  O   . HOH O 6 .   ? -31.215 -23.746 47.275  1.00 16.69 ? 434 HOH B O   1 
HETATM 4321 O  O   . HOH O 6 .   ? -30.091 -47.137 14.845  1.00 17.15 ? 435 HOH B O   1 
HETATM 4322 O  O   . HOH O 6 .   ? -32.529 -52.458 18.746  1.00 16.97 ? 436 HOH B O   1 
HETATM 4323 O  O   . HOH O 6 .   ? -43.274 -37.811 38.057  1.00 15.37 ? 437 HOH B O   1 
HETATM 4324 O  O   . HOH O 6 .   ? -33.363 -51.364 27.273  1.00 27.64 ? 438 HOH B O   1 
HETATM 4325 O  O   . HOH O 6 .   ? -19.293 -36.011 34.371  1.00 19.75 ? 439 HOH B O   1 
HETATM 4326 O  O   . HOH O 6 .   ? -29.934 -21.266 47.077  1.00 16.32 ? 440 HOH B O   1 
HETATM 4327 O  O   . HOH O 6 .   ? -15.119 -30.100 22.766  1.00 30.91 ? 441 HOH B O   1 
HETATM 4328 O  O   . HOH O 6 .   ? -48.473 -18.019 23.870  1.00 27.82 ? 442 HOH B O   1 
HETATM 4329 O  O   . HOH O 6 .   ? -24.588 -22.588 32.933  1.00 18.50 ? 443 HOH B O   1 
HETATM 4330 O  O   . HOH O 6 .   ? -34.546 -38.272 42.836  1.00 21.92 ? 444 HOH B O   1 
HETATM 4331 O  O   . HOH O 6 .   ? -33.594 -44.877 13.307  1.00 22.17 ? 445 HOH B O   1 
HETATM 4332 O  O   . HOH O 6 .   ? -40.242 -50.405 29.481  1.00 19.01 ? 446 HOH B O   1 
HETATM 4333 O  O   . HOH O 6 .   ? -36.989 -54.451 21.031  1.00 34.62 ? 447 HOH B O   1 
HETATM 4334 O  O   . HOH O 6 .   ? -41.345 -49.597 19.566  1.00 17.97 ? 448 HOH B O   1 
HETATM 4335 O  O   . HOH O 6 .   ? -48.998 -54.416 24.787  1.00 28.71 ? 449 HOH B O   1 
HETATM 4336 O  O   . HOH O 6 .   ? -33.653 -33.896 40.900  1.00 14.46 ? 450 HOH B O   1 
HETATM 4337 O  O   . HOH O 6 .   ? -23.920 -37.685 11.585  1.00 16.54 ? 451 HOH B O   1 
HETATM 4338 O  O   . HOH O 6 .   ? -25.139 -25.133 8.702   1.00 23.25 ? 452 HOH B O   1 
HETATM 4339 O  O   . HOH O 6 .   ? -45.972 -38.362 34.260  1.00 15.86 ? 453 HOH B O   1 
HETATM 4340 O  O   . HOH O 6 .   ? -28.999 -19.034 21.946  1.00 25.72 ? 454 HOH B O   1 
HETATM 4341 O  O   . HOH O 6 .   ? -25.685 -48.558 30.458  1.00 17.21 ? 455 HOH B O   1 
HETATM 4342 O  O   . HOH O 6 .   ? -38.892 -29.681 11.220  1.00 17.55 ? 456 HOH B O   1 
HETATM 4343 O  O   . HOH O 6 .   ? -28.729 -27.667 10.112  1.00 14.49 ? 457 HOH B O   1 
HETATM 4344 O  O   . HOH O 6 .   ? -51.211 -21.707 26.533  1.00 20.79 ? 458 HOH B O   1 
HETATM 4345 O  O   . HOH O 6 .   ? -24.283 -52.511 29.885  1.00 20.60 ? 459 HOH B O   1 
HETATM 4346 O  O   . HOH O 6 .   ? -29.391 -12.784 17.340  1.00 18.56 ? 460 HOH B O   1 
HETATM 4347 O  O   . HOH O 6 .   ? -33.775 -19.227 38.666  1.00 20.48 ? 461 HOH B O   1 
HETATM 4348 O  O   . HOH O 6 .   ? -40.529 -47.181 18.604  1.00 20.60 ? 462 HOH B O   1 
HETATM 4349 O  O   . HOH O 6 .   ? -25.259 -36.129 7.374   1.00 21.01 ? 463 HOH B O   1 
HETATM 4350 O  O   . HOH O 6 .   ? -40.589 -29.622 21.305  1.00 27.65 ? 464 HOH B O   1 
HETATM 4351 O  O   . HOH O 6 .   ? -27.732 -56.433 28.771  1.00 28.60 ? 465 HOH B O   1 
HETATM 4352 O  O   . HOH O 6 .   ? -24.663 -39.542 42.514  1.00 28.48 ? 466 HOH B O   1 
HETATM 4353 O  O   . HOH O 6 .   ? -13.895 -28.083 24.993  1.00 21.05 ? 467 HOH B O   1 
HETATM 4354 O  O   . HOH O 6 .   ? -27.266 -54.037 32.954  1.00 17.62 ? 468 HOH B O   1 
HETATM 4355 O  O   . HOH O 6 .   ? -14.910 -31.293 31.032  1.00 25.30 ? 469 HOH B O   1 
HETATM 4356 O  O   . HOH O 6 .   ? -42.904 -16.636 19.505  1.00 15.05 ? 470 HOH B O   1 
HETATM 4357 O  O   . HOH O 6 .   ? -48.581 -35.943 30.410  1.00 21.32 ? 471 HOH B O   1 
HETATM 4358 O  O   . HOH O 6 .   ? -31.369 -16.090 28.005  1.00 17.80 ? 472 HOH B O   1 
HETATM 4359 O  O   . HOH O 6 .   ? -38.990 -50.648 16.094  1.00 25.58 ? 473 HOH B O   1 
HETATM 4360 O  O   . HOH O 6 .   ? -21.812 -53.995 26.440  1.00 24.96 ? 474 HOH B O   1 
HETATM 4361 O  O   . HOH O 6 .   ? -39.533 -34.840 27.396  1.00 17.17 ? 475 HOH B O   1 
HETATM 4362 O  O   . HOH O 6 .   ? -26.113 -33.002 41.757  1.00 25.52 ? 476 HOH B O   1 
HETATM 4363 O  O   . HOH O 6 .   ? -34.497 -49.387 15.939  1.00 21.13 ? 477 HOH B O   1 
HETATM 4364 O  O   . HOH O 6 .   ? -13.632 -40.763 29.891  1.00 21.85 ? 478 HOH B O   1 
HETATM 4365 O  O   . HOH O 6 .   ? -25.836 -18.032 10.597  1.00 26.48 ? 479 HOH B O   1 
HETATM 4366 O  O   . HOH O 6 .   ? -23.619 -39.816 9.878   1.00 21.22 ? 480 HOH B O   1 
HETATM 4367 O  O   . HOH O 6 .   ? -20.585 -39.005 11.265  1.00 20.70 ? 481 HOH B O   1 
HETATM 4368 O  O   . HOH O 6 .   ? -48.563 -39.088 33.538  1.00 27.22 ? 482 HOH B O   1 
HETATM 4369 O  O   . HOH O 6 .   ? -15.038 -25.580 25.475  1.00 19.40 ? 483 HOH B O   1 
HETATM 4370 O  O   . HOH O 6 .   ? -14.518 -32.985 19.122  1.00 19.97 ? 484 HOH B O   1 
HETATM 4371 O  O   . HOH O 6 .   ? -12.928 -32.085 23.885  1.00 22.43 ? 485 HOH B O   1 
HETATM 4372 O  O   . HOH O 6 .   ? -12.295 -33.867 20.081  1.00 21.97 ? 486 HOH B O   1 
HETATM 4373 O  O   . HOH O 6 .   ? -31.285 -11.605 21.073  1.00 32.51 ? 487 HOH B O   1 
HETATM 4374 O  O   . HOH O 6 .   ? -51.786 -36.699 32.138  1.00 28.26 ? 488 HOH B O   1 
HETATM 4375 O  O   . HOH O 6 .   ? -50.880 -38.419 34.272  1.00 28.01 ? 489 HOH B O   1 
HETATM 4376 O  O   . HOH O 6 .   ? -37.587 -51.307 28.847  1.00 34.81 ? 490 HOH B O   1 
HETATM 4377 O  O   . HOH O 6 .   ? -47.352 -44.598 43.363  1.00 31.96 ? 491 HOH B O   1 
HETATM 4378 O  O   . HOH O 6 .   ? -47.538 -42.499 40.730  1.00 38.10 ? 492 HOH B O   1 
HETATM 4379 O  O   . HOH O 6 .   ? -43.686 -55.222 24.262  1.00 37.67 ? 493 HOH B O   1 
HETATM 4380 O  O   . HOH O 6 .   ? -38.536 -45.826 12.869  1.00 29.13 ? 494 HOH B O   1 
HETATM 4381 O  O   . HOH O 6 .   ? -36.088 -45.370 14.277  1.00 25.56 ? 495 HOH B O   1 
HETATM 4382 O  O   . HOH O 6 .   ? -38.772 -46.047 10.304  1.00 36.32 ? 496 HOH B O   1 
HETATM 4383 O  O   . HOH O 6 .   ? -37.250 -49.034 32.386  1.00 29.38 ? 497 HOH B O   1 
HETATM 4384 O  O   . HOH O 6 .   ? -20.273 -47.541 34.623  1.00 25.29 ? 498 HOH B O   1 
HETATM 4385 O  O   . HOH O 6 .   ? -20.678 -47.789 39.180  1.00 23.47 ? 499 HOH B O   1 
HETATM 4386 O  O   . HOH O 6 .   ? -32.154 -17.152 38.255  1.00 25.60 ? 500 HOH B O   1 
HETATM 4387 O  O   . HOH O 6 .   ? -30.677 -14.218 36.155  1.00 28.87 ? 501 HOH B O   1 
HETATM 4388 O  O   . HOH O 6 .   ? -17.309 -48.274 25.894  1.00 27.32 ? 502 HOH B O   1 
HETATM 4389 O  O   . HOH O 6 .   ? -14.992 -38.581 34.550  1.00 32.23 ? 503 HOH B O   1 
HETATM 4390 O  O   . HOH O 6 .   ? -13.298 -38.806 32.322  1.00 26.47 ? 504 HOH B O   1 
HETATM 4391 O  O   . HOH O 6 .   ? -15.686 -39.508 14.253  1.00 33.65 ? 505 HOH B O   1 
HETATM 4392 O  O   . HOH O 6 .   ? -17.472 -34.321 12.575  1.00 27.00 ? 506 HOH B O   1 
HETATM 4393 O  O   . HOH O 6 .   ? -26.391 -17.279 22.722  1.00 29.89 ? 507 HOH B O   1 
HETATM 4394 O  O   . HOH O 6 .   ? -42.680 -37.131 23.468  1.00 33.95 ? 508 HOH B O   1 
HETATM 4395 O  O   . HOH O 6 .   ? -43.178 -28.545 21.974  1.00 31.34 ? 509 HOH B O   1 
HETATM 4396 O  O   . HOH O 6 .   ? -22.203 -25.018 14.278  1.00 22.74 ? 510 HOH B O   1 
HETATM 4397 O  O   . HOH O 6 .   ? -22.228 -45.273 35.744  1.00 27.42 ? 511 HOH B O   1 
HETATM 4398 O  O   . HOH O 6 .   ? -24.636 -46.434 38.426  1.00 21.57 ? 512 HOH B O   1 
HETATM 4399 O  O   . HOH O 6 .   ? -26.747 -45.480 39.929  1.00 26.78 ? 513 HOH B O   1 
HETATM 4400 O  O   . HOH O 6 .   ? -18.248 -39.431 37.483  1.00 35.47 ? 514 HOH B O   1 
HETATM 4401 O  O   . HOH O 6 .   ? -18.525 -33.881 38.151  1.00 40.02 ? 515 HOH B O   1 
HETATM 4402 O  O   . HOH O 6 .   ? -18.726 -27.590 36.649  1.00 24.66 ? 516 HOH B O   1 
HETATM 4403 O  O   . HOH O 6 .   ? -16.796 -29.542 37.551  1.00 23.74 ? 517 HOH B O   1 
HETATM 4404 O  O   . HOH O 6 .   ? -13.051 -32.695 38.848  1.00 44.34 ? 518 HOH B O   1 
HETATM 4405 O  O   . HOH O 6 .   ? -15.299 -24.329 35.233  1.00 31.49 ? 519 HOH B O   1 
HETATM 4406 O  O   . HOH O 6 .   ? -22.752 -23.271 36.532  1.00 28.41 ? 520 HOH B O   1 
HETATM 4407 O  O   . HOH O 6 .   ? -26.657 -24.259 46.385  1.00 21.77 ? 521 HOH B O   1 
HETATM 4408 O  O   . HOH O 6 .   ? -27.147 -21.724 47.182  1.00 22.55 ? 522 HOH B O   1 
HETATM 4409 O  O   . HOH O 6 .   ? -24.673 -18.019 42.152  1.00 27.22 ? 523 HOH B O   1 
HETATM 4410 O  O   . HOH O 6 .   ? -21.454 -23.791 43.669  1.00 31.23 ? 524 HOH B O   1 
HETATM 4411 O  O   . HOH O 6 .   ? -23.797 -21.469 38.075  1.00 34.65 ? 525 HOH B O   1 
HETATM 4412 O  O   . HOH O 6 .   ? -37.532 -17.292 38.293  1.00 28.05 ? 526 HOH B O   1 
HETATM 4413 O  O   . HOH O 6 .   ? -44.558 -17.499 34.792  1.00 24.47 ? 527 HOH B O   1 
HETATM 4414 O  O   . HOH O 6 .   ? -42.510 -19.060 37.415  1.00 22.82 ? 528 HOH B O   1 
HETATM 4415 O  O   . HOH O 6 .   ? -45.532 -24.237 37.648  1.00 23.15 ? 529 HOH B O   1 
HETATM 4416 O  O   . HOH O 6 .   ? -47.258 -15.633 25.470  1.00 27.33 ? 530 HOH B O   1 
HETATM 4417 O  O   . HOH O 6 .   ? -13.491 -26.905 32.855  1.00 31.12 ? 531 HOH B O   1 
HETATM 4418 O  O   . HOH O 6 .   ? -19.574 -43.906 19.928  1.00 36.45 ? 532 HOH B O   1 
HETATM 4419 O  O   . HOH O 6 .   ? -38.608 -48.185 16.814  1.00 18.55 ? 533 HOH B O   1 
HETATM 4420 O  O   . HOH O 6 .   ? -54.102 -27.136 29.728  1.00 27.34 ? 534 HOH B O   1 
HETATM 4421 O  O   . HOH O 6 .   ? -31.904 -53.407 26.031  1.00 25.29 ? 535 HOH B O   1 
HETATM 4422 O  O   . HOH O 6 .   ? -20.797 -48.528 19.184  1.00 31.46 ? 536 HOH B O   1 
HETATM 4423 O  O   . HOH O 6 .   ? -18.575 -49.555 18.144  1.00 34.60 ? 537 HOH B O   1 
HETATM 4424 O  O   . HOH O 6 .   ? -7.938  -33.751 25.414  1.00 37.53 ? 538 HOH B O   1 
HETATM 4425 O  O   . HOH O 6 .   ? -10.918 -39.830 27.962  1.00 35.05 ? 539 HOH B O   1 
HETATM 4426 O  O   . HOH O 6 .   ? -45.877 -41.719 21.551  1.00 39.63 ? 540 HOH B O   1 
HETATM 4427 O  O   . HOH O 6 .   ? -42.520 -33.727 24.313  1.00 34.13 ? 541 HOH B O   1 
HETATM 4428 O  O   . HOH O 6 .   ? -39.916 -31.401 18.639  1.00 32.25 ? 542 HOH B O   1 
HETATM 4429 O  O   . HOH O 6 .   ? -47.960 -39.076 27.235  1.00 20.20 ? 543 HOH B O   1 
HETATM 4430 O  O   . HOH O 6 .   ? -48.378 -38.593 30.943  1.00 31.30 ? 544 HOH B O   1 
HETATM 4431 O  O   . HOH O 6 .   ? -39.363 -28.513 8.825   1.00 27.28 ? 545 HOH B O   1 
HETATM 4432 O  O   . HOH O 6 .   ? -25.130 -38.953 7.678   1.00 35.48 ? 546 HOH B O   1 
HETATM 4433 O  O   . HOH O 6 .   ? -21.306 -25.955 7.535   1.00 25.89 ? 547 HOH B O   1 
HETATM 4434 O  O   . HOH O 6 .   ? -19.839 -32.824 7.621   1.00 28.44 ? 548 HOH B O   1 
HETATM 4435 O  O   . HOH O 6 .   ? -21.463 -32.836 4.869   1.00 38.54 ? 549 HOH B O   1 
HETATM 4436 O  O   . HOH O 6 .   ? -19.139 -40.352 14.310  1.00 28.75 ? 550 HOH B O   1 
HETATM 4437 O  O   . HOH O 6 .   ? -21.847 -41.177 14.363  1.00 24.62 ? 551 HOH B O   1 
HETATM 4438 O  O   . HOH O 6 .   ? -25.245 -42.207 16.221  1.00 24.26 ? 552 HOH B O   1 
HETATM 4439 O  O   . HOH O 6 .   ? -27.780 -43.813 15.588  1.00 16.95 ? 553 HOH B O   1 
HETATM 4440 O  O   . HOH O 6 .   ? -25.211 -22.077 9.451   1.00 23.08 ? 554 HOH B O   1 
HETATM 4441 O  O   . HOH O 6 .   ? -41.731 -26.560 43.562  1.00 22.21 ? 555 HOH B O   1 
HETATM 4442 O  O   . HOH O 6 .   ? -45.661 -37.250 36.834  1.00 18.56 ? 556 HOH B O   1 
HETATM 4443 O  O   . HOH O 6 .   ? -45.201 -37.031 32.163  1.00 19.11 ? 557 HOH B O   1 
HETATM 4444 O  O   . HOH O 6 .   ? -13.689 -43.682 14.918  1.00 35.18 ? 558 HOH B O   1 
HETATM 4445 O  O   . HOH O 6 .   ? -25.797 -42.664 40.794  1.00 22.86 ? 559 HOH B O   1 
HETATM 4446 O  O   . HOH O 6 .   ? -14.485 -46.329 34.870  1.00 23.73 ? 560 HOH B O   1 
HETATM 4447 O  O   . HOH O 6 .   ? -37.594 -51.652 31.808  1.00 35.60 ? 561 HOH B O   1 
HETATM 4448 O  O   . HOH O 6 .   ? -21.564 -48.598 36.898  1.00 28.05 ? 562 HOH B O   1 
HETATM 4449 O  O   . HOH O 6 .   ? -34.838 -29.158 44.966  1.00 17.16 ? 563 HOH B O   1 
HETATM 4450 O  O   . HOH O 6 .   ? -14.613 -30.117 20.276  1.00 30.22 ? 564 HOH B O   1 
HETATM 4451 O  O   . HOH O 6 .   ? -21.125 -21.919 27.229  1.00 25.25 ? 565 HOH B O   1 
HETATM 4452 O  O   . HOH O 6 .   ? -20.138 -25.171 34.490  1.00 23.81 ? 566 HOH B O   1 
HETATM 4453 O  O   . HOH O 6 .   ? -21.737 -23.266 34.177  1.00 24.72 ? 567 HOH B O   1 
HETATM 4454 O  O   . HOH O 6 .   ? -39.360 -13.795 25.540  1.00 26.03 ? 568 HOH B O   1 
HETATM 4455 O  O   . HOH O 6 .   ? -38.730 -15.338 31.332  1.00 24.79 ? 569 HOH B O   1 
HETATM 4456 O  O   . HOH O 6 .   ? -31.730 -16.474 32.319  1.00 23.19 ? 570 HOH B O   1 
HETATM 4457 O  O   . HOH O 6 .   ? -21.766 -28.533 8.021   1.00 22.56 ? 571 HOH B O   1 
HETATM 4458 O  O   . HOH O 6 .   ? -23.612 -28.899 6.104   1.00 21.31 ? 572 HOH B O   1 
HETATM 4459 O  O   . HOH O 6 .   ? -24.936 -35.373 4.851   1.00 31.21 ? 573 HOH B O   1 
HETATM 4460 O  O   . HOH O 6 .   ? -24.262 -32.537 4.667   1.00 26.83 ? 574 HOH B O   1 
HETATM 4461 O  O   . HOH O 6 .   ? -4.970  -36.503 18.823  1.00 39.75 ? 575 HOH B O   1 
HETATM 4462 O  O   . HOH O 6 .   ? -51.813 -46.099 31.819  1.00 37.70 ? 576 HOH B O   1 
HETATM 4463 O  O   . HOH O 6 .   ? -46.681 -37.115 40.656  1.00 32.76 ? 577 HOH B O   1 
HETATM 4464 O  O   . HOH O 6 .   ? -39.801 -47.329 14.255  1.00 26.21 ? 578 HOH B O   1 
HETATM 4465 O  O   . HOH O 6 .   ? -51.668 -38.818 30.163  1.00 36.10 ? 579 HOH B O   1 
HETATM 4466 O  O   . HOH O 6 .   ? -26.376 -17.740 13.215  1.00 25.53 ? 580 HOH B O   1 
HETATM 4467 O  O   . HOH O 6 .   ? -22.575 -42.674 16.678  1.00 25.11 ? 581 HOH B O   1 
HETATM 4468 O  O   . HOH O 6 .   ? -27.525 -46.710 14.698  1.00 25.86 ? 582 HOH B O   1 
HETATM 4469 O  O   . HOH O 6 .   ? -28.187 -30.369 1.603   1.00 52.37 ? 583 HOH B O   1 
HETATM 4470 O  O   . HOH O 6 .   ? -49.276 -19.231 29.045  1.00 33.92 ? 584 HOH B O   1 
HETATM 4471 O  O   . HOH O 6 .   ? -41.120 -15.707 28.184  1.00 31.52 ? 585 HOH B O   1 
HETATM 4472 O  O   . HOH O 6 .   ? -31.494 -11.228 15.926  1.00 33.93 ? 586 HOH B O   1 
HETATM 4473 O  O   . HOH O 6 .   ? -30.218 -13.439 13.438  1.00 34.99 ? 587 HOH B O   1 
HETATM 4474 O  O   . HOH O 6 .   ? -37.046 -12.974 18.064  1.00 31.52 ? 588 HOH B O   1 
HETATM 4475 O  O   . HOH O 6 .   ? -37.899 -11.312 24.568  1.00 43.28 ? 589 HOH B O   1 
HETATM 4476 O  O   . HOH O 6 .   ? -34.329 -12.657 27.147  1.00 34.19 ? 590 HOH B O   1 
HETATM 4477 O  O   . HOH O 6 .   ? -29.411 -18.251 29.489  1.00 27.09 ? 591 HOH B O   1 
HETATM 4478 O  O   . HOH O 6 .   ? -23.413 -13.889 28.453  1.00 45.64 ? 592 HOH B O   1 
HETATM 4479 O  O   . HOH O 6 .   ? -18.309 -23.746 35.503  1.00 31.74 ? 593 HOH B O   1 
HETATM 4480 O  O   . HOH O 6 .   ? -40.930 -15.212 39.059  1.00 39.02 ? 594 HOH B O   1 
HETATM 4481 O  O   . HOH O 6 .   ? -26.246 -27.375 4.410   1.00 34.33 ? 595 HOH B O   1 
HETATM 4482 O  O   . HOH O 6 .   ? -23.532 -30.830 44.519  1.00 29.50 ? 596 HOH B O   1 
HETATM 4483 O  O   . HOH O 6 .   ? -34.716 -54.243 28.873  1.00 35.53 ? 597 HOH B O   1 
HETATM 4484 O  O   . HOH O 6 .   ? -21.639 -27.913 43.879  1.00 32.55 ? 598 HOH B O   1 
HETATM 4485 O  O   . HOH O 6 .   ? -39.762 -28.111 18.532  1.00 39.37 ? 599 HOH B O   1 
HETATM 4486 O  O   . HOH O 6 .   ? -22.337 -19.225 30.682  1.00 28.73 ? 600 HOH B O   1 
HETATM 4487 O  O   . HOH O 6 .   ? -18.685 -53.607 32.097  1.00 29.74 ? 601 HOH B O   1 
HETATM 4488 O  O   . HOH O 6 .   ? -39.018 -14.630 28.615  1.00 33.82 ? 602 HOH B O   1 
HETATM 4489 O  O   . HOH O 6 .   ? -38.447 -18.608 43.789  1.00 31.07 ? 603 HOH B O   1 
HETATM 4490 O  O   . HOH O 6 .   ? -37.243 -13.660 32.680  1.00 27.76 ? 604 HOH B O   1 
HETATM 4491 O  O   . HOH O 6 .   ? -11.792 -27.981 28.048  1.00 33.12 ? 605 HOH B O   1 
HETATM 4492 O  O   . HOH O 6 .   ? -51.060 -19.066 31.959  1.00 42.01 ? 606 HOH B O   1 
HETATM 4493 O  O   . HOH O 6 .   ? -18.331 -31.273 39.153  1.00 32.23 ? 607 HOH B O   1 
HETATM 4494 O  O   . HOH O 6 .   ? -3.090  -34.794 20.855  1.00 42.76 ? 608 HOH B O   1 
HETATM 4495 O  O   . HOH O 6 .   ? -40.371 -26.752 13.037  1.00 32.96 ? 609 HOH B O   1 
HETATM 4496 O  O   . HOH O 6 .   ? -24.277 -48.472 15.281  1.00 38.05 ? 610 HOH B O   1 
HETATM 4497 O  O   . HOH O 6 .   ? -32.508 -44.243 37.386  1.00 31.23 ? 611 HOH B O   1 
HETATM 4498 O  O   . HOH O 6 .   ? -35.306 -26.529 48.096  1.00 27.83 ? 612 HOH B O   1 
HETATM 4499 O  O   . HOH O 6 .   ? -34.761 -13.087 31.899  1.00 41.64 ? 613 HOH B O   1 
HETATM 4500 O  O   . HOH O 6 .   ? -36.658 -43.045 36.811  1.00 29.74 ? 614 HOH B O   1 
HETATM 4501 O  O   . HOH O 6 .   ? -10.845 -35.624 18.691  1.00 34.22 ? 615 HOH B O   1 
HETATM 4502 O  O   . HOH O 6 .   ? -38.529 -54.034 18.985  1.00 33.25 ? 616 HOH B O   1 
HETATM 4503 O  O   . HOH O 6 .   ? -28.111 -40.892 44.859  1.00 32.25 ? 617 HOH B O   1 
HETATM 4504 O  O   . HOH O 6 .   ? -43.512 -47.028 37.268  1.00 37.18 ? 618 HOH B O   1 
HETATM 4505 O  O   . HOH O 6 .   ? -33.467 -20.158 13.296  1.00 35.48 ? 619 HOH B O   1 
HETATM 4506 O  O   . HOH O 6 .   ? -24.535 -25.514 47.422  1.00 31.24 ? 620 HOH B O   1 
HETATM 4507 O  O   . HOH O 6 .   ? -24.816 -31.785 2.297   1.00 34.01 ? 621 HOH B O   1 
HETATM 4508 O  O   . HOH O 6 .   ? -39.376 -26.423 17.021  1.00 32.51 ? 622 HOH B O   1 
HETATM 4509 O  O   . HOH O 6 .   ? -40.069 -52.424 18.037  1.00 32.03 ? 623 HOH B O   1 
HETATM 4510 O  O   . HOH O 6 .   ? -19.675 -47.350 29.288  1.00 33.47 ? 624 HOH B O   1 
HETATM 4511 O  O   . HOH O 6 .   ? -16.377 -33.342 35.564  1.00 39.19 ? 625 HOH B O   1 
HETATM 4512 O  O   . HOH O 6 .   ? -19.112 -25.976 38.619  1.00 32.13 ? 626 HOH B O   1 
HETATM 4513 O  O   . HOH O 6 .   ? -35.572 -58.009 25.996  1.00 40.15 ? 627 HOH B O   1 
HETATM 4514 O  O   . HOH O 6 .   ? -9.623  -39.017 30.682  1.00 38.61 ? 628 HOH B O   1 
HETATM 4515 O  O   . HOH O 6 .   ? -16.916 -36.739 35.219  1.00 26.34 ? 629 HOH B O   1 
HETATM 4516 O  O   . HOH O 6 .   ? -23.316 -34.811 41.572  1.00 37.78 ? 630 HOH B O   1 
HETATM 4517 O  O   . HOH O 6 .   ? -35.919 -16.708 13.674  1.00 38.92 ? 631 HOH B O   1 
HETATM 4518 O  O   . HOH O 6 .   ? -40.440 -22.752 13.026  1.00 37.34 ? 632 HOH B O   1 
HETATM 4519 O  O   . HOH O 6 .   ? -14.860 -31.247 33.707  1.00 38.51 ? 633 HOH B O   1 
HETATM 4520 O  O   . HOH O 6 .   ? -9.586  -32.974 22.781  1.00 34.85 ? 634 HOH B O   1 
HETATM 4521 O  O   . HOH O 6 .   ? -44.116 -44.090 40.992  1.00 33.69 ? 635 HOH B O   1 
HETATM 4522 O  O   . HOH O 6 .   ? -46.217 -31.293 23.353  1.00 33.23 ? 636 HOH B O   1 
HETATM 4523 O  O   . HOH O 6 .   ? -47.751 -22.665 18.852  1.00 29.90 ? 637 HOH B O   1 
HETATM 4524 O  O   . HOH O 6 .   ? -36.389 -17.765 10.174  1.00 36.30 ? 638 HOH B O   1 
HETATM 4525 O  O   . HOH O 6 .   ? -36.664 -20.474 9.573   1.00 49.32 ? 639 HOH B O   1 
HETATM 4526 O  O   . HOH O 6 .   ? -42.477 -34.381 7.888   1.00 30.65 ? 640 HOH B O   1 
HETATM 4527 O  O   . HOH O 6 .   ? -24.796 -42.506 12.511  1.00 37.38 ? 641 HOH B O   1 
HETATM 4528 O  O   . HOH O 6 .   ? -42.547 -45.979 17.070  1.00 38.19 ? 642 HOH B O   1 
HETATM 4529 O  O   . HOH O 6 .   ? -19.579 -22.029 40.402  1.00 38.33 ? 643 HOH B O   1 
HETATM 4530 O  O   . HOH O 6 .   ? -34.233 -24.620 50.295  1.00 26.30 ? 644 HOH B O   1 
HETATM 4531 O  O   . HOH O 6 .   ? -48.448 -29.625 24.982  1.00 42.92 ? 645 HOH B O   1 
HETATM 4532 O  O   . HOH O 6 .   ? -46.622 -23.012 39.256  1.00 32.02 ? 646 HOH B O   1 
HETATM 4533 O  O   . HOH O 6 .   ? -54.716 -28.038 37.499  1.00 35.33 ? 647 HOH B O   1 
HETATM 4534 O  O   . HOH O 6 .   ? -29.126 -20.354 7.553   1.00 27.37 ? 648 HOH B O   1 
HETATM 4535 O  O   . HOH O 6 .   ? -43.597 -53.972 32.446  1.00 39.63 ? 649 HOH B O   1 
HETATM 4536 O  O   . HOH O 6 .   ? -24.931 -17.719 38.162  1.00 37.92 ? 650 HOH B O   1 
HETATM 4537 O  O   . HOH O 6 .   ? -41.086 -37.910 16.314  1.00 30.00 ? 651 HOH B O   1 
HETATM 4538 O  O   . HOH O 6 .   ? -50.595 -54.409 26.897  1.00 42.01 ? 652 HOH B O   1 
HETATM 4539 O  O   . HOH P 6 .   ? -1.072  -0.790  -6.237  1.00 16.72 ? 401 HOH A O   1 
HETATM 4540 O  O   . HOH P 6 .   ? -2.212  -13.783 24.612  1.00 14.57 ? 402 HOH A O   1 
HETATM 4541 O  O   . HOH P 6 .   ? -5.141  -11.185 25.961  1.00 14.74 ? 403 HOH A O   1 
HETATM 4542 O  O   . HOH P 6 .   ? -4.427  -20.150 26.252  1.00 20.16 ? 404 HOH A O   1 
HETATM 4543 O  O   . HOH P 6 .   ? -13.237 -18.345 28.237  1.00 15.50 ? 405 HOH A O   1 
HETATM 4544 O  O   . HOH P 6 .   ? -6.064  -19.985 6.185   1.00 15.62 ? 406 HOH A O   1 
HETATM 4545 O  O   . HOH P 6 .   ? -13.591 -22.993 17.414  1.00 14.36 ? 407 HOH A O   1 
HETATM 4546 O  O   . HOH P 6 .   ? -6.768  -5.875  -0.863  1.00 9.10  ? 408 HOH A O   1 
HETATM 4547 O  O   . HOH P 6 .   ? -0.631  -0.846  4.226   1.00 14.58 ? 409 HOH A O   1 
HETATM 4548 O  O   . HOH P 6 .   ? -11.879 -21.607 10.391  1.00 13.66 ? 410 HOH A O   1 
HETATM 4549 O  O   . HOH P 6 .   ? -2.297  -2.049  10.839  1.00 13.04 ? 411 HOH A O   1 
HETATM 4550 O  O   . HOH P 6 .   ? -11.679 -25.240 16.741  1.00 19.58 ? 412 HOH A O   1 
HETATM 4551 O  O   . HOH P 6 .   ? -2.459  -18.015 22.356  1.00 15.18 ? 413 HOH A O   1 
HETATM 4552 O  O   . HOH P 6 .   ? -1.943  -4.811  -2.108  1.00 19.87 ? 414 HOH A O   1 
HETATM 4553 O  O   . HOH P 6 .   ? 5.749   -1.741  11.827  1.00 17.96 ? 415 HOH A O   1 
HETATM 4554 O  O   . HOH P 6 .   ? -5.872  1.419   -5.236  1.00 13.05 ? 416 HOH A O   1 
HETATM 4555 O  O   . HOH P 6 .   ? -6.932  -0.679  -6.100  1.00 14.63 ? 417 HOH A O   1 
HETATM 4556 O  O   . HOH P 6 .   ? -7.385  -15.147 28.613  1.00 13.31 ? 418 HOH A O   1 
HETATM 4557 O  O   . HOH P 6 .   ? -1.840  -16.605 24.398  1.00 16.96 ? 419 HOH A O   1 
HETATM 4558 O  O   . HOH P 6 .   ? -25.400 -14.502 19.405  1.00 13.67 ? 420 HOH A O   1 
HETATM 4559 O  O   . HOH P 6 .   ? -15.784 -24.411 16.585  1.00 19.90 ? 421 HOH A O   1 
HETATM 4560 O  O   . HOH P 6 .   ? -0.682  -11.618 25.620  1.00 16.48 ? 422 HOH A O   1 
HETATM 4561 O  O   . HOH P 6 .   ? -19.740 -14.174 5.672   1.00 12.79 ? 423 HOH A O   1 
HETATM 4562 O  O   . HOH P 6 .   ? -0.089  -19.725 21.674  1.00 15.15 ? 424 HOH A O   1 
HETATM 4563 O  O   . HOH P 6 .   ? 7.256   -24.036 7.608   1.00 21.50 ? 425 HOH A O   1 
HETATM 4564 O  O   . HOH P 6 .   ? -20.859 -5.313  22.988  1.00 15.77 ? 426 HOH A O   1 
HETATM 4565 O  O   . HOH P 6 .   ? -2.940  3.800   2.210   1.00 18.19 ? 427 HOH A O   1 
HETATM 4566 O  O   . HOH P 6 .   ? -16.155 -23.471 24.066  1.00 19.68 ? 428 HOH A O   1 
HETATM 4567 O  O   . HOH P 6 .   ? -9.355  -13.688 32.750  1.00 18.61 ? 429 HOH A O   1 
HETATM 4568 O  O   . HOH P 6 .   ? -26.663 -12.589 21.133  1.00 16.76 ? 430 HOH A O   1 
HETATM 4569 O  O   . HOH P 6 .   ? 8.051   -6.956  24.022  1.00 19.88 ? 431 HOH A O   1 
HETATM 4570 O  O   . HOH P 6 .   ? -10.603 -16.474 8.292   1.00 13.53 ? 432 HOH A O   1 
HETATM 4571 O  O   . HOH P 6 .   ? -28.968 -12.161 9.487   1.00 29.92 ? 433 HOH A O   1 
HETATM 4572 O  O   . HOH P 6 .   ? 1.014   -10.205 24.062  1.00 18.76 ? 434 HOH A O   1 
HETATM 4573 O  O   . HOH P 6 .   ? -22.705 -6.501  -4.333  1.00 18.40 ? 435 HOH A O   1 
HETATM 4574 O  O   . HOH P 6 .   ? -22.697 -19.403 18.877  1.00 15.95 ? 436 HOH A O   1 
HETATM 4575 O  O   . HOH P 6 .   ? -18.208 -23.235 13.348  1.00 20.79 ? 437 HOH A O   1 
HETATM 4576 O  O   . HOH P 6 .   ? -3.158  -14.436 28.861  1.00 30.40 ? 438 HOH A O   1 
HETATM 4577 O  O   . HOH P 6 .   ? -10.697 -21.362 26.838  1.00 18.43 ? 439 HOH A O   1 
HETATM 4578 O  O   . HOH P 6 .   ? -26.984 -14.025 16.969  1.00 16.91 ? 440 HOH A O   1 
HETATM 4579 O  O   . HOH P 6 .   ? 0.982   -8.286  6.694   1.00 15.50 ? 441 HOH A O   1 
HETATM 4580 O  O   . HOH P 6 .   ? -4.392  5.871   8.044   1.00 16.54 ? 442 HOH A O   1 
HETATM 4581 O  O   . HOH P 6 .   ? 6.061   -13.360 11.266  1.00 16.36 ? 443 HOH A O   1 
HETATM 4582 O  O   . HOH P 6 .   ? -22.020 -6.583  25.063  1.00 22.03 ? 444 HOH A O   1 
HETATM 4583 O  O   . HOH P 6 .   ? 5.318   -8.613  25.594  1.00 24.45 ? 445 HOH A O   1 
HETATM 4584 O  O   . HOH P 6 .   ? -15.793 -10.143 -7.377  1.00 19.49 ? 446 HOH A O   1 
HETATM 4585 O  O   . HOH P 6 .   ? -5.635  -15.530 26.443  1.00 20.05 ? 447 HOH A O   1 
HETATM 4586 O  O   . HOH P 6 .   ? 2.282   -2.805  4.553   1.00 22.16 ? 448 HOH A O   1 
HETATM 4587 O  O   . HOH P 6 .   ? -10.008 2.053   12.651  1.00 20.15 ? 449 HOH A O   1 
HETATM 4588 O  O   . HOH P 6 .   ? -19.792 -16.630 24.420  1.00 16.46 ? 450 HOH A O   1 
HETATM 4589 O  O   . HOH P 6 .   ? 8.214   0.738   12.756  1.00 17.75 ? 451 HOH A O   1 
HETATM 4590 O  O   . HOH P 6 .   ? -20.619 -20.430 11.216  1.00 20.51 ? 452 HOH A O   1 
HETATM 4591 O  O   . HOH P 6 .   ? 0.252   -5.491  28.154  1.00 22.06 ? 453 HOH A O   1 
HETATM 4592 O  O   . HOH P 6 .   ? -10.947 -24.109 8.755   1.00 15.40 ? 454 HOH A O   1 
HETATM 4593 O  O   . HOH P 6 .   ? 7.598   -22.026 5.671   1.00 17.11 ? 455 HOH A O   1 
HETATM 4594 O  O   . HOH P 6 .   ? -3.311  5.942   3.490   1.00 23.13 ? 456 HOH A O   1 
HETATM 4595 O  O   . HOH P 6 .   ? -5.755  9.439   9.569   1.00 17.42 ? 457 HOH A O   1 
HETATM 4596 O  O   . HOH P 6 .   ? -15.419 -25.090 13.896  1.00 19.64 ? 458 HOH A O   1 
HETATM 4597 O  O   . HOH P 6 .   ? 4.214   -19.244 12.424  1.00 21.96 ? 459 HOH A O   1 
HETATM 4598 O  O   . HOH P 6 .   ? 1.515   -19.238 23.799  1.00 23.09 ? 460 HOH A O   1 
HETATM 4599 O  O   . HOH P 6 .   ? -9.107  -13.612 -3.160  1.00 18.80 ? 461 HOH A O   1 
HETATM 4600 O  O   . HOH P 6 .   ? -21.381 -18.054 11.106  1.00 18.34 ? 462 HOH A O   1 
HETATM 4601 O  O   . HOH P 6 .   ? -14.134 -20.162 2.599   1.00 28.33 ? 463 HOH A O   1 
HETATM 4602 O  O   . HOH P 6 .   ? -9.498  3.185   15.670  1.00 26.39 ? 464 HOH A O   1 
HETATM 4603 O  O   . HOH P 6 .   ? 9.589   -14.518 12.631  1.00 25.12 ? 465 HOH A O   1 
HETATM 4604 O  O   . HOH P 6 .   ? -2.154  -25.463 11.193  1.00 15.05 ? 466 HOH A O   1 
HETATM 4605 O  O   . HOH P 6 .   ? -3.686  -25.624 8.180   1.00 17.28 ? 467 HOH A O   1 
HETATM 4606 O  O   . HOH P 6 .   ? 1.907   -8.091  4.286   1.00 20.15 ? 468 HOH A O   1 
HETATM 4607 O  O   . HOH P 6 .   ? -2.216  9.270   6.789   1.00 31.75 ? 469 HOH A O   1 
HETATM 4608 O  O   . HOH P 6 .   ? -2.717  6.684   6.043   1.00 19.73 ? 470 HOH A O   1 
HETATM 4609 O  O   . HOH P 6 .   ? -2.980  7.718   0.514   1.00 33.10 ? 471 HOH A O   1 
HETATM 4610 O  O   . HOH P 6 .   ? -4.072  9.251   -2.226  1.00 19.48 ? 472 HOH A O   1 
HETATM 4611 O  O   . HOH P 6 .   ? -6.110  0.406   10.448  1.00 19.45 ? 473 HOH A O   1 
HETATM 4612 O  O   . HOH P 6 .   ? -7.555  0.769   12.753  1.00 21.38 ? 474 HOH A O   1 
HETATM 4613 O  O   . HOH P 6 .   ? -6.890  2.937   14.292  1.00 22.06 ? 475 HOH A O   1 
HETATM 4614 O  O   . HOH P 6 .   ? -15.657 1.637   20.507  1.00 25.20 ? 476 HOH A O   1 
HETATM 4615 O  O   . HOH P 6 .   ? -16.656 0.291   30.324  1.00 40.47 ? 477 HOH A O   1 
HETATM 4616 O  O   . HOH P 6 .   ? -20.810 -0.517  32.039  1.00 19.96 ? 478 HOH A O   1 
HETATM 4617 O  O   . HOH P 6 .   ? -16.968 -2.511  33.887  1.00 22.39 ? 479 HOH A O   1 
HETATM 4618 O  O   . HOH P 6 .   ? -9.763  2.664   36.206  1.00 27.94 ? 480 HOH A O   1 
HETATM 4619 O  O   . HOH P 6 .   ? 3.803   -0.534  4.757   1.00 27.95 ? 481 HOH A O   1 
HETATM 4620 O  O   . HOH P 6 .   ? 7.162   -3.263  10.017  1.00 25.12 ? 482 HOH A O   1 
HETATM 4621 O  O   . HOH P 6 .   ? -0.809  -8.812  2.913   1.00 22.43 ? 483 HOH A O   1 
HETATM 4622 O  O   . HOH P 6 .   ? 1.787   -12.809 0.972   1.00 25.23 ? 484 HOH A O   1 
HETATM 4623 O  O   . HOH P 6 .   ? 5.664   2.380   22.453  1.00 18.70 ? 485 HOH A O   1 
HETATM 4624 O  O   . HOH P 6 .   ? 4.824   -4.787  26.454  1.00 27.31 ? 486 HOH A O   1 
HETATM 4625 O  O   . HOH P 6 .   ? 0.647   -3.060  27.349  1.00 24.94 ? 487 HOH A O   1 
HETATM 4626 O  O   . HOH P 6 .   ? 2.556   -8.754  26.699  1.00 24.77 ? 488 HOH A O   1 
HETATM 4627 O  O   . HOH P 6 .   ? 5.012   -16.130 24.688  1.00 27.41 ? 489 HOH A O   1 
HETATM 4628 O  O   . HOH P 6 .   ? 2.740   -3.109  25.476  1.00 20.53 ? 490 HOH A O   1 
HETATM 4629 O  O   . HOH P 6 .   ? 8.461   -5.690  15.220  1.00 22.78 ? 491 HOH A O   1 
HETATM 4630 O  O   . HOH P 6 .   ? 10.137  -7.167  16.767  1.00 23.83 ? 492 HOH A O   1 
HETATM 4631 O  O   . HOH P 6 .   ? 7.485   -9.278  17.803  1.00 22.31 ? 493 HOH A O   1 
HETATM 4632 O  O   . HOH P 6 .   ? -5.569  -15.288 30.873  1.00 25.03 ? 494 HOH A O   1 
HETATM 4633 O  O   . HOH P 6 .   ? -6.068  -18.249 29.017  1.00 24.00 ? 495 HOH A O   1 
HETATM 4634 O  O   . HOH P 6 .   ? 0.392   -17.542 25.610  1.00 19.55 ? 496 HOH A O   1 
HETATM 4635 O  O   . HOH P 6 .   ? -4.895  -23.755 26.181  1.00 28.43 ? 497 HOH A O   1 
HETATM 4636 O  O   . HOH P 6 .   ? -2.027  -31.148 22.863  1.00 33.42 ? 498 HOH A O   1 
HETATM 4637 O  O   . HOH P 6 .   ? 6.272   -16.147 12.236  1.00 32.63 ? 499 HOH A O   1 
HETATM 4638 O  O   . HOH P 6 .   ? 6.886   -20.278 12.910  1.00 34.13 ? 500 HOH A O   1 
HETATM 4639 O  O   . HOH P 6 .   ? 7.182   -21.135 15.340  1.00 24.20 ? 501 HOH A O   1 
HETATM 4640 O  O   . HOH P 6 .   ? 12.736  -18.588 17.383  1.00 37.90 ? 502 HOH A O   1 
HETATM 4641 O  O   . HOH P 6 .   ? 8.265   -15.475 8.424   1.00 29.26 ? 503 HOH A O   1 
HETATM 4642 O  O   . HOH P 6 .   ? -3.550  -24.059 6.100   1.00 28.27 ? 504 HOH A O   1 
HETATM 4643 O  O   . HOH P 6 .   ? -1.022  -23.316 4.499   1.00 29.14 ? 505 HOH A O   1 
HETATM 4644 O  O   . HOH P 6 .   ? 0.592   -21.840 -1.751  1.00 24.27 ? 506 HOH A O   1 
HETATM 4645 O  O   . HOH P 6 .   ? 4.495   -24.413 7.095   1.00 18.90 ? 507 HOH A O   1 
HETATM 4646 O  O   . HOH P 6 .   ? 11.394  -24.717 12.018  1.00 28.42 ? 508 HOH A O   1 
HETATM 4647 O  O   . HOH P 6 .   ? -3.055  -28.089 12.658  1.00 22.89 ? 509 HOH A O   1 
HETATM 4648 O  O   . HOH P 6 .   ? -10.992 -27.047 18.999  1.00 23.76 ? 510 HOH A O   1 
HETATM 4649 O  O   . HOH P 6 .   ? -10.612 -26.573 10.035  1.00 26.59 ? 511 HOH A O   1 
HETATM 4650 O  O   . HOH P 6 .   ? -14.814 -21.491 27.872  1.00 33.17 ? 512 HOH A O   1 
HETATM 4651 O  O   . HOH P 6 .   ? -24.696 -11.435 15.589  1.00 20.65 ? 513 HOH A O   1 
HETATM 4652 O  O   . HOH P 6 .   ? -28.661 -10.109 24.153  1.00 29.80 ? 514 HOH A O   1 
HETATM 4653 O  O   . HOH P 6 .   ? -29.699 -13.343 24.891  1.00 29.97 ? 515 HOH A O   1 
HETATM 4654 O  O   . HOH P 6 .   ? -24.653 -8.169  30.744  1.00 27.02 ? 516 HOH A O   1 
HETATM 4655 O  O   . HOH P 6 .   ? -24.072 -3.959  26.244  1.00 27.10 ? 517 HOH A O   1 
HETATM 4656 O  O   . HOH P 6 .   ? -26.600 -1.314  26.820  1.00 34.80 ? 518 HOH A O   1 
HETATM 4657 O  O   . HOH P 6 .   ? -19.099 5.104   19.093  1.00 31.79 ? 519 HOH A O   1 
HETATM 4658 O  O   . HOH P 6 .   ? -28.454 0.602   10.881  1.00 24.84 ? 520 HOH A O   1 
HETATM 4659 O  O   . HOH P 6 .   ? -31.508 -4.016  15.601  1.00 27.96 ? 521 HOH A O   1 
HETATM 4660 O  O   . HOH P 6 .   ? -6.451  14.696  10.649  1.00 39.55 ? 522 HOH A O   1 
HETATM 4661 O  O   . HOH P 6 .   ? -17.122 -10.034 28.762  1.00 24.69 ? 523 HOH A O   1 
HETATM 4662 O  O   . HOH P 6 .   ? -19.913 -13.789 30.099  1.00 21.71 ? 524 HOH A O   1 
HETATM 4663 O  O   . HOH P 6 .   ? -22.565 -11.123 32.678  1.00 32.63 ? 525 HOH A O   1 
HETATM 4664 O  O   . HOH P 6 .   ? -9.709  -0.462  -6.168  1.00 22.24 ? 526 HOH A O   1 
HETATM 4665 O  O   . HOH P 6 .   ? -7.701  -14.166 -0.899  1.00 20.07 ? 527 HOH A O   1 
HETATM 4666 O  O   . HOH P 6 .   ? 1.309   -21.756 0.824   1.00 19.89 ? 528 HOH A O   1 
HETATM 4667 O  O   . HOH P 6 .   ? -3.865  -21.199 2.885   1.00 41.27 ? 529 HOH A O   1 
HETATM 4668 O  O   . HOH P 6 .   ? -6.546  -13.949 32.680  1.00 26.75 ? 530 HOH A O   1 
HETATM 4669 O  O   . HOH P 6 .   ? -7.619  -6.948  37.512  1.00 24.49 ? 531 HOH A O   1 
HETATM 4670 O  O   . HOH P 6 .   ? -17.604 -9.631  32.929  1.00 16.62 ? 532 HOH A O   1 
HETATM 4671 O  O   . HOH P 6 .   ? -13.702 -17.327 -3.791  1.00 36.16 ? 533 HOH A O   1 
HETATM 4672 O  O   . HOH P 6 .   ? -21.625 3.812   -0.038  1.00 22.65 ? 534 HOH A O   1 
HETATM 4673 O  O   . HOH P 6 .   ? -9.407  15.503  3.140   1.00 23.37 ? 535 HOH A O   1 
HETATM 4674 O  O   . HOH P 6 .   ? -29.073 -8.942  9.706   1.00 38.03 ? 536 HOH A O   1 
HETATM 4675 O  O   . HOH P 6 .   ? -16.910 -18.902 4.393   1.00 26.80 ? 537 HOH A O   1 
HETATM 4676 O  O   . HOH P 6 .   ? 4.054   -18.136 23.031  1.00 20.62 ? 538 HOH A O   1 
HETATM 4677 O  O   . HOH P 6 .   ? -15.874 -25.349 6.577   1.00 31.52 ? 539 HOH A O   1 
HETATM 4678 O  O   . HOH P 6 .   ? -13.227 -27.649 8.215   1.00 30.02 ? 540 HOH A O   1 
HETATM 4679 O  O   . HOH P 6 .   ? -21.063 -19.050 7.678   1.00 28.23 ? 541 HOH A O   1 
HETATM 4680 O  O   . HOH P 6 .   ? -12.457 1.034   20.981  1.00 28.38 ? 542 HOH A O   1 
HETATM 4681 O  O   . HOH P 6 .   ? -17.675 0.692   21.645  1.00 35.93 ? 543 HOH A O   1 
HETATM 4682 O  O   . HOH P 6 .   ? -1.248  4.110   25.115  1.00 44.26 ? 544 HOH A O   1 
HETATM 4683 O  O   . HOH P 6 .   ? 8.386   -4.381  7.471   1.00 35.62 ? 545 HOH A O   1 
HETATM 4684 O  O   . HOH P 6 .   ? 3.802   -9.562  3.042   1.00 28.23 ? 546 HOH A O   1 
HETATM 4685 O  O   . HOH P 6 .   ? -16.412 -0.650  -6.285  1.00 17.57 ? 547 HOH A O   1 
HETATM 4686 O  O   . HOH P 6 .   ? -14.375 -1.581  -8.429  1.00 34.54 ? 548 HOH A O   1 
HETATM 4687 O  O   . HOH P 6 .   ? 3.209   2.039   22.814  1.00 20.47 ? 549 HOH A O   1 
HETATM 4688 O  O   . HOH P 6 .   ? -23.669 -17.868 8.164   1.00 22.47 ? 550 HOH A O   1 
HETATM 4689 O  O   . HOH P 6 .   ? -14.880 0.294   28.187  1.00 25.79 ? 551 HOH A O   1 
HETATM 4690 O  O   . HOH P 6 .   ? -12.707 2.228   27.998  1.00 25.79 ? 552 HOH A O   1 
HETATM 4691 O  O   . HOH P 6 .   ? -24.207 -13.082 0.865   1.00 14.69 ? 553 HOH A O   1 
HETATM 4692 O  O   . HOH P 6 .   ? -17.806 -17.050 -3.201  1.00 23.80 ? 554 HOH A O   1 
HETATM 4693 O  O   . HOH P 6 .   ? 10.271  -17.803 16.491  1.00 23.80 ? 555 HOH A O   1 
HETATM 4694 O  O   . HOH P 6 .   ? -11.116 -4.733  -5.034  1.00 21.08 ? 556 HOH A O   1 
HETATM 4695 O  O   . HOH P 6 .   ? -18.774 -17.222 4.388   1.00 22.77 ? 557 HOH A O   1 
HETATM 4696 O  O   . HOH P 6 .   ? -27.777 -1.148  3.583   1.00 33.76 ? 558 HOH A O   1 
HETATM 4697 O  O   . HOH P 6 .   ? -26.414 0.090   5.285   1.00 32.32 ? 559 HOH A O   1 
HETATM 4698 O  O   . HOH P 6 .   ? -23.573 6.010   2.301   1.00 21.07 ? 560 HOH A O   1 
HETATM 4699 O  O   . HOH P 6 .   ? -13.009 -23.212 32.353  1.00 29.62 ? 561 HOH A O   1 
HETATM 4700 O  O   . HOH P 6 .   ? -12.997 2.558   -4.810  1.00 23.44 ? 562 HOH A O   1 
HETATM 4701 O  O   . HOH P 6 .   ? -13.715 -4.846  -9.785  1.00 32.55 ? 563 HOH A O   1 
HETATM 4702 O  O   . HOH P 6 .   ? 3.899   10.545  16.233  1.00 49.68 ? 564 HOH A O   1 
HETATM 4703 O  O   . HOH P 6 .   ? -2.900  9.505   9.373   1.00 33.21 ? 565 HOH A O   1 
HETATM 4704 O  O   . HOH P 6 .   ? -2.368  11.737  5.818   1.00 31.35 ? 566 HOH A O   1 
HETATM 4705 O  O   . HOH P 6 .   ? 5.907   1.735   5.975   1.00 27.77 ? 567 HOH A O   1 
HETATM 4706 O  O   . HOH P 6 .   ? 3.073   -5.657  3.997   1.00 23.35 ? 568 HOH A O   1 
HETATM 4707 O  O   . HOH P 6 .   ? -0.567  3.537   1.166   1.00 29.04 ? 569 HOH A O   1 
HETATM 4708 O  O   . HOH P 6 .   ? 1.186   -12.948 27.035  1.00 36.44 ? 570 HOH A O   1 
HETATM 4709 O  O   . HOH P 6 .   ? -3.884  -17.489 26.257  1.00 19.08 ? 571 HOH A O   1 
HETATM 4710 O  O   . HOH P 6 .   ? 4.781   -22.031 16.699  1.00 31.00 ? 572 HOH A O   1 
HETATM 4711 O  O   . HOH P 6 .   ? 8.414   -19.630 17.436  1.00 29.42 ? 573 HOH A O   1 
HETATM 4712 O  O   . HOH P 6 .   ? -5.222  -22.025 5.204   1.00 29.21 ? 574 HOH A O   1 
HETATM 4713 O  O   . HOH P 6 .   ? -8.562  -27.639 8.553   1.00 28.72 ? 575 HOH A O   1 
HETATM 4714 O  O   . HOH P 6 .   ? 0.728   -30.738 19.301  1.00 30.47 ? 576 HOH A O   1 
HETATM 4715 O  O   . HOH P 6 .   ? -0.997  -25.328 26.632  1.00 27.79 ? 577 HOH A O   1 
HETATM 4716 O  O   . HOH P 6 .   ? -18.933 -20.896 26.756  1.00 26.31 ? 578 HOH A O   1 
HETATM 4717 O  O   . HOH P 6 .   ? -19.566 -16.500 31.045  1.00 29.35 ? 579 HOH A O   1 
HETATM 4718 O  O   . HOH P 6 .   ? -24.252 -6.218  16.348  1.00 25.56 ? 580 HOH A O   1 
HETATM 4719 O  O   . HOH P 6 .   ? -17.838 4.072   15.063  1.00 26.31 ? 581 HOH A O   1 
HETATM 4720 O  O   . HOH P 6 .   ? -12.970 -19.302 31.659  1.00 35.92 ? 582 HOH A O   1 
HETATM 4721 O  O   . HOH P 6 .   ? -1.070  -14.183 -1.489  1.00 27.66 ? 583 HOH A O   1 
HETATM 4722 O  O   . HOH P 6 .   ? -11.122 3.191   32.722  1.00 35.86 ? 584 HOH A O   1 
HETATM 4723 O  O   . HOH P 6 .   ? -5.026  -2.001  33.561  1.00 31.71 ? 585 HOH A O   1 
HETATM 4724 O  O   . HOH P 6 .   ? -22.353 -15.236 5.866   1.00 26.28 ? 586 HOH A O   1 
HETATM 4725 O  O   . HOH P 6 .   ? -23.148 -12.998 4.736   1.00 36.17 ? 587 HOH A O   1 
HETATM 4726 O  O   . HOH P 6 .   ? -25.798 -8.490  9.101   1.00 27.19 ? 588 HOH A O   1 
HETATM 4727 O  O   . HOH P 6 .   ? -17.192 7.641   -1.151  1.00 35.27 ? 589 HOH A O   1 
HETATM 4728 O  O   . HOH P 6 .   ? -11.128 -24.587 6.415   1.00 30.60 ? 590 HOH A O   1 
HETATM 4729 O  O   . HOH P 6 .   ? -9.180  -31.332 14.550  1.00 29.23 ? 591 HOH A O   1 
HETATM 4730 O  O   . HOH P 6 .   ? -17.407 -24.406 4.226   1.00 32.19 ? 592 HOH A O   1 
HETATM 4731 O  O   . HOH P 6 .   ? -5.377  3.254   16.965  1.00 34.12 ? 593 HOH A O   1 
HETATM 4732 O  O   . HOH P 6 .   ? -2.437  12.259  9.618   1.00 38.33 ? 594 HOH A O   1 
HETATM 4733 O  O   . HOH P 6 .   ? -7.920  4.849   20.894  1.00 42.06 ? 595 HOH A O   1 
HETATM 4734 O  O   . HOH P 6 .   ? -6.274  2.110   24.528  1.00 40.75 ? 596 HOH A O   1 
HETATM 4735 O  O   . HOH P 6 .   ? 3.854   -0.722  25.311  1.00 30.10 ? 597 HOH A O   1 
HETATM 4736 O  O   . HOH P 6 .   ? 2.531   0.546   27.602  1.00 34.10 ? 598 HOH A O   1 
HETATM 4737 O  O   . HOH P 6 .   ? 8.114   9.244   20.685  1.00 39.57 ? 599 HOH A O   1 
HETATM 4738 O  O   . HOH P 6 .   ? 13.962  3.985   16.161  1.00 41.42 ? 600 HOH A O   1 
HETATM 4739 O  O   . HOH P 6 .   ? 12.161  0.667   18.756  1.00 36.63 ? 601 HOH A O   1 
HETATM 4740 O  O   . HOH P 6 .   ? 13.680  0.049   20.909  1.00 34.31 ? 602 HOH A O   1 
HETATM 4741 O  O   . HOH P 6 .   ? 12.931  -5.638  23.234  1.00 38.72 ? 603 HOH A O   1 
HETATM 4742 O  O   . HOH P 6 .   ? 12.957  -6.018  16.292  1.00 34.35 ? 604 HOH A O   1 
HETATM 4743 O  O   . HOH P 6 .   ? 14.135  -8.204  14.450  1.00 43.63 ? 605 HOH A O   1 
HETATM 4744 O  O   . HOH P 6 .   ? 14.204  -11.878 14.874  1.00 40.82 ? 606 HOH A O   1 
HETATM 4745 O  O   . HOH P 6 .   ? 11.637  -14.491 15.253  1.00 26.73 ? 607 HOH A O   1 
HETATM 4746 O  O   . HOH P 6 .   ? 8.523   -13.223 22.088  1.00 30.63 ? 608 HOH A O   1 
HETATM 4747 O  O   . HOH P 6 .   ? 1.624   -15.470 26.764  1.00 25.14 ? 609 HOH A O   1 
HETATM 4748 O  O   . HOH P 6 .   ? -2.979  9.022   12.979  1.00 25.99 ? 610 HOH A O   1 
HETATM 4749 O  O   . HOH P 6 .   ? -2.600  6.204   18.918  1.00 41.28 ? 611 HOH A O   1 
HETATM 4750 O  O   . HOH P 6 .   ? -13.419 2.115   18.035  1.00 39.57 ? 612 HOH A O   1 
HETATM 4751 O  O   . HOH P 6 .   ? -13.207 4.425   26.283  1.00 43.12 ? 613 HOH A O   1 
HETATM 4752 O  O   . HOH P 6 .   ? -16.028 2.422   31.911  1.00 38.06 ? 614 HOH A O   1 
HETATM 4753 O  O   . HOH P 6 .   ? -18.478 -1.986  31.714  1.00 38.06 ? 615 HOH A O   1 
HETATM 4754 O  O   . HOH P 6 .   ? -26.334 -1.940  31.827  1.00 24.15 ? 616 HOH A O   1 
HETATM 4755 O  O   . HOH P 6 .   ? -26.925 -2.152  29.012  1.00 31.69 ? 617 HOH A O   1 
HETATM 4756 O  O   . HOH P 6 .   ? -24.753 -4.452  23.485  1.00 22.41 ? 618 HOH A O   1 
HETATM 4757 O  O   . HOH P 6 .   ? -18.163 -20.258 29.433  1.00 28.86 ? 619 HOH A O   1 
HETATM 4758 O  O   . HOH P 6 .   ? -15.185 -19.530 29.706  1.00 34.68 ? 620 HOH A O   1 
HETATM 4759 O  O   . HOH P 6 .   ? -27.773 -10.353 4.799   1.00 42.40 ? 621 HOH A O   1 
HETATM 4760 O  O   . HOH P 6 .   ? -1.662  -29.771 25.994  1.00 33.26 ? 622 HOH A O   1 
HETATM 4761 O  O   . HOH P 6 .   ? -27.622 -2.862  -0.829  1.00 40.12 ? 623 HOH A O   1 
HETATM 4762 O  O   . HOH P 6 .   ? -11.980 -21.535 -2.194  1.00 36.06 ? 624 HOH A O   1 
HETATM 4763 O  O   . HOH P 6 .   ? -25.096 9.784   7.780   1.00 35.28 ? 625 HOH A O   1 
HETATM 4764 O  O   . HOH P 6 .   ? -1.560  -21.212 2.892   1.00 24.19 ? 626 HOH A O   1 
HETATM 4765 O  O   . HOH P 6 .   ? -10.724 13.707  -3.557  1.00 44.61 ? 627 HOH A O   1 
HETATM 4766 O  O   . HOH P 6 .   ? -13.222 -15.295 34.527  1.00 33.35 ? 628 HOH A O   1 
HETATM 4767 O  O   . HOH P 6 .   ? -24.823 -13.696 3.222   1.00 27.70 ? 629 HOH A O   1 
HETATM 4768 O  O   . HOH P 6 .   ? -24.963 -6.728  7.968   1.00 28.85 ? 630 HOH A O   1 
HETATM 4769 O  O   . HOH P 6 .   ? -1.988  9.261   -1.047  1.00 34.63 ? 631 HOH A O   1 
HETATM 4770 O  O   . HOH P 6 .   ? 1.242   -21.870 25.142  1.00 33.91 ? 632 HOH A O   1 
HETATM 4771 O  O   . HOH P 6 .   ? -24.263 4.448   -1.127  1.00 34.41 ? 633 HOH A O   1 
HETATM 4772 O  O   . HOH P 6 .   ? -14.431 -27.352 10.338  1.00 31.81 ? 634 HOH A O   1 
HETATM 4773 O  O   . HOH P 6 .   ? -13.517 8.076   -4.349  1.00 31.48 ? 635 HOH A O   1 
HETATM 4774 O  O   . HOH P 6 .   ? -21.774 10.599  8.291   1.00 40.64 ? 636 HOH A O   1 
HETATM 4775 O  O   . HOH P 6 .   ? -21.483 12.530  16.083  1.00 31.30 ? 637 HOH A O   1 
HETATM 4776 O  O   . HOH P 6 .   ? -16.265 6.918   0.719   1.00 21.74 ? 638 HOH A O   1 
HETATM 4777 O  O   . HOH P 6 .   ? -0.488  -28.956 9.571   1.00 35.63 ? 639 HOH A O   1 
HETATM 4778 O  O   . HOH P 6 .   ? 1.361   -1.910  31.808  1.00 42.87 ? 640 HOH A O   1 
HETATM 4779 O  O   . HOH P 6 .   ? 10.151  6.068   4.089   1.00 42.55 ? 641 HOH A O   1 
HETATM 4780 O  O   . HOH P 6 .   ? -21.378 2.003   -4.910  1.00 37.33 ? 642 HOH A O   1 
HETATM 4781 O  O   . HOH P 6 .   ? -10.526 -14.060 35.137  1.00 32.37 ? 643 HOH A O   1 
HETATM 4782 O  O   . HOH P 6 .   ? -20.133 12.564  11.449  1.00 22.38 ? 644 HOH A O   1 
HETATM 4783 O  O   . HOH P 6 .   ? -22.137 -0.741  -1.273  1.00 25.88 ? 645 HOH A O   1 
HETATM 4784 O  O   . HOH P 6 .   ? 8.683   -3.858  12.142  1.00 31.78 ? 646 HOH A O   1 
HETATM 4785 O  O   . HOH P 6 .   ? -10.733 -15.428 -4.508  1.00 29.24 ? 647 HOH A O   1 
HETATM 4786 O  O   . HOH P 6 .   ? 10.729  8.817   4.915   1.00 41.28 ? 648 HOH A O   1 
HETATM 4787 O  O   . HOH P 6 .   ? 1.998   -5.460  29.695  1.00 43.59 ? 649 HOH A O   1 
HETATM 4788 O  O   . HOH P 6 .   ? -16.759 -15.451 32.960  1.00 31.31 ? 650 HOH A O   1 
HETATM 4789 O  O   . HOH P 6 .   ? -15.198 -11.239 37.474  1.00 31.30 ? 651 HOH A O   1 
HETATM 4790 O  O   . HOH P 6 .   ? -13.834 15.430  8.698   1.00 27.32 ? 652 HOH A O   1 
HETATM 4791 O  O   . HOH P 6 .   ? 9.893   -20.065 11.853  1.00 39.23 ? 653 HOH A O   1 
HETATM 4792 O  O   . HOH P 6 .   ? 1.094   -30.463 16.592  1.00 38.40 ? 654 HOH A O   1 
HETATM 4793 O  O   . HOH P 6 .   ? -8.752  -22.705 28.485  1.00 43.06 ? 655 HOH A O   1 
HETATM 4794 O  O   . HOH P 6 .   ? -4.568  11.752  -3.159  1.00 34.98 ? 656 HOH A O   1 
HETATM 4795 O  O   . HOH P 6 .   ? 9.147   -1.780  13.462  1.00 35.70 ? 657 HOH A O   1 
HETATM 4796 O  O   . HOH P 6 .   ? -4.318  -12.506 38.741  1.00 35.56 ? 658 HOH A O   1 
HETATM 4797 O  O   . HOH P 6 .   ? -8.581  -25.968 28.190  1.00 48.12 ? 659 HOH A O   1 
HETATM 4798 O  O   . HOH P 6 .   ? -12.101 15.860  1.577   1.00 36.88 ? 660 HOH A O   1 
HETATM 4799 O  O   . HOH P 6 .   ? 10.863  -0.848  10.406  1.00 31.93 ? 661 HOH A O   1 
HETATM 4800 O  O   . HOH P 6 .   ? 11.303  -19.943 13.633  1.00 38.64 ? 662 HOH A O   1 
HETATM 4801 O  O   . HOH P 6 .   ? -0.895  6.144   -0.976  1.00 38.12 ? 663 HOH A O   1 
HETATM 4802 O  O   . HOH P 6 .   ? -12.989 -11.293 40.242  1.00 30.68 ? 664 HOH A O   1 
HETATM 4803 O  O   . HOH P 6 .   ? 0.986   -26.457 22.629  1.00 34.69 ? 665 HOH A O   1 
HETATM 4804 O  O   . HOH P 6 .   ? -10.571 -20.768 31.737  1.00 46.79 ? 666 HOH A O   1 
HETATM 4805 O  O   . HOH P 6 .   ? -6.770  -22.200 27.159  1.00 36.58 ? 667 HOH A O   1 
HETATM 4806 O  O   . HOH P 6 .   ? -9.712  -26.888 5.093   1.00 35.31 ? 668 HOH A O   1 
HETATM 4807 O  O   . HOH P 6 .   ? 4.746   7.906   11.890  1.00 33.95 ? 669 HOH A O   1 
HETATM 4808 O  O   . HOH P 6 .   ? -8.144  -28.161 20.672  1.00 29.75 ? 670 HOH A O   1 
HETATM 4809 O  O   . HOH P 6 .   ? -17.189 4.801   -3.514  1.00 38.65 ? 671 HOH A O   1 
HETATM 4810 O  O   . HOH P 6 .   ? -26.529 2.662   8.447   1.00 36.28 ? 672 HOH A O   1 
HETATM 4811 O  O   . HOH P 6 .   ? -29.058 -6.286  7.607   1.00 42.76 ? 673 HOH A O   1 
HETATM 4812 O  O   . HOH P 6 .   ? 3.651   3.115   2.667   1.00 35.84 ? 674 HOH A O   1 
HETATM 4813 O  O   . HOH P 6 .   ? -7.290  -20.351 2.083   1.00 35.27 ? 675 HOH A O   1 
HETATM 4814 O  O   . HOH P 6 .   ? 0.283   0.542   31.347  1.00 37.30 ? 676 HOH A O   1 
HETATM 4815 O  O   . HOH P 6 .   ? 9.910   -27.752 9.889   1.00 29.42 ? 677 HOH A O   1 
HETATM 4816 O  O   . HOH P 6 .   ? -11.575 3.657   18.940  1.00 30.82 ? 678 HOH A O   1 
HETATM 4817 O  O   . HOH P 6 .   ? 10.688  -2.595  22.903  1.00 36.33 ? 679 HOH A O   1 
HETATM 4818 O  O   . HOH P 6 .   ? -27.279 3.636   1.980   1.00 33.72 ? 680 HOH A O   1 
HETATM 4819 O  O   . HOH P 6 .   ? -2.541  -20.969 28.002  1.00 32.22 ? 681 HOH A O   1 
HETATM 4820 O  O   . HOH P 6 .   ? 6.713   3.717   4.311   1.00 45.09 ? 682 HOH A O   1 
HETATM 4821 O  O   . HOH P 6 .   ? -7.961  -22.577 4.019   1.00 37.96 ? 683 HOH A O   1 
HETATM 4822 O  O   . HOH P 6 .   ? -12.023 -29.119 20.321  1.00 35.33 ? 684 HOH A O   1 
HETATM 4823 O  O   . HOH P 6 .   ? -10.339 -22.854 4.549   1.00 33.75 ? 685 HOH A O   1 
HETATM 4824 O  O   . HOH P 6 .   ? 9.615   -16.970 7.185   1.00 38.96 ? 686 HOH A O   1 
HETATM 4825 O  O   . HOH P 6 .   ? -10.703 14.227  11.845  1.00 31.66 ? 687 HOH A O   1 
HETATM 4826 O  O   . HOH P 6 .   ? 4.738   -12.415 1.943   1.00 33.16 ? 688 HOH A O   1 
HETATM 4827 O  O   . HOH P 6 .   ? 6.080   -5.725  3.673   1.00 32.61 ? 689 HOH A O   1 
HETATM 4828 O  O   . HOH P 6 .   ? -34.498 3.302   18.110  1.00 35.26 ? 690 HOH A O   1 
HETATM 4829 O  O   . HOH P 6 .   ? -13.919 -21.986 34.211  1.00 41.39 ? 691 HOH A O   1 
HETATM 4830 O  O   . HOH P 6 .   ? 5.955   -0.980  5.202   1.00 41.19 ? 692 HOH A O   1 
HETATM 4831 O  O   . HOH P 6 .   ? 2.490   -4.536  1.347   1.00 41.39 ? 693 HOH A O   1 
HETATM 4832 O  O   . HOH P 6 .   ? -3.964  -27.474 29.521  1.00 41.14 ? 694 HOH A O   1 
HETATM 4833 O  O   . HOH P 6 .   ? -8.628  15.524  12.253  1.00 44.23 ? 695 HOH A O   1 
HETATM 4834 O  O   . HOH P 6 .   ? 1.099   -0.834  28.771  1.00 30.59 ? 696 HOH A O   1 
HETATM 4835 O  O   . HOH P 6 .   ? -2.860  9.731   16.108  1.00 41.99 ? 697 HOH A O   1 
HETATM 4836 O  O   . HOH P 6 .   ? -28.495 -4.050  33.037  1.00 44.80 ? 698 HOH A O   1 
HETATM 4837 O  O   . HOH P 6 .   ? 1.685   4.043   24.588  1.00 45.87 ? 699 HOH A O   1 
HETATM 4838 O  O   . HOH P 6 .   ? 4.914   -28.129 14.678  1.00 40.54 ? 700 HOH A O   1 
HETATM 4839 O  O   . HOH P 6 .   ? -10.916 -29.467 12.227  1.00 33.32 ? 701 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   B . n 
A 1 2   MET 2   2   ?   ?   ?   B . n 
A 1 3   SER 3   3   ?   ?   ?   B . n 
A 1 4   ARG 4   4   4   ARG ARG B . n 
A 1 5   LEU 5   5   5   LEU LEU B . n 
A 1 6   SER 6   6   6   SER SER B . n 
A 1 7   TRP 7   7   7   TRP TRP B . n 
A 1 8   GLY 8   8   8   GLY GLY B . n 
A 1 9   TYR 9   9   9   TYR TYR B . n 
A 1 10  ARG 10  10  10  ARG ARG B . n 
A 1 11  GLU 11  11  11  GLU GLU B . n 
A 1 12  HIS 12  12  12  HIS HIS B . n 
A 1 13  ASN 13  13  13  ASN ASN B . n 
A 1 14  GLY 14  14  14  GLY GLY B . n 
A 1 15  PRO 15  15  15  PRO PRO B . n 
A 1 16  ILE 16  16  16  ILE ILE B . n 
A 1 17  HIS 17  17  17  HIS HIS B . n 
A 1 18  TRP 18  18  18  TRP TRP B . n 
A 1 19  LYS 19  19  19  LYS LYS B . n 
A 1 20  GLU 20  20  20  GLU GLU B . n 
A 1 21  PHE 21  21  21  PHE PHE B . n 
A 1 22  PHE 22  22  22  PHE PHE B . n 
A 1 23  PRO 23  23  23  PRO PRO B . n 
A 1 24  ILE 24  24  24  ILE ILE B . n 
A 1 25  ALA 25  25  25  ALA ALA B . n 
A 1 26  ASP 26  26  26  ASP ASP B . n 
A 1 27  GLY 27  27  27  GLY GLY B . n 
A 1 28  ASP 28  28  28  ASP ASP B . n 
A 1 29  GLN 29  29  29  GLN GLN B . n 
A 1 30  GLN 30  30  30  GLN GLN B . n 
A 1 31  SER 31  31  31  SER SER B . n 
A 1 32  PRO 32  32  32  PRO PRO B . n 
A 1 33  ILE 33  33  33  ILE ILE B . n 
A 1 34  GLU 34  34  34  GLU GLU B . n 
A 1 35  ILE 35  35  35  ILE ILE B . n 
A 1 36  LYS 36  36  36  LYS LYS B . n 
A 1 37  THR 37  37  37  THR THR B . n 
A 1 38  LYS 38  38  38  LYS LYS B . n 
A 1 39  GLU 39  39  39  GLU GLU B . n 
A 1 40  VAL 40  40  40  VAL VAL B . n 
A 1 41  LYS 41  41  41  LYS LYS B . n 
A 1 42  TYR 42  42  42  TYR TYR B . n 
A 1 43  ASP 43  43  43  ASP ASP B . n 
A 1 44  SER 44  44  44  SER SER B . n 
A 1 45  SER 45  45  45  SER SER B . n 
A 1 46  LEU 46  46  46  LEU LEU B . n 
A 1 47  ARG 47  47  47  ARG ARG B . n 
A 1 48  PRO 48  48  48  PRO PRO B . n 
A 1 49  LEU 49  49  49  LEU LEU B . n 
A 1 50  SER 50  50  50  SER SER B . n 
A 1 51  ILE 51  51  51  ILE ILE B . n 
A 1 52  LYS 52  52  52  LYS LYS B . n 
A 1 53  TYR 53  53  53  TYR TYR B . n 
A 1 54  ASP 54  54  54  ASP ASP B . n 
A 1 55  PRO 55  55  55  PRO PRO B . n 
A 1 56  SER 56  56  56  SER SER B . n 
A 1 57  SER 57  57  57  SER SER B . n 
A 1 58  ALA 58  58  58  ALA ALA B . n 
A 1 59  LYS 59  59  59  LYS LYS B . n 
A 1 60  ILE 60  60  60  ILE ILE B . n 
A 1 61  ILE 61  61  61  ILE ILE B . n 
A 1 62  SER 62  62  62  SER SER B . n 
A 1 63  ASN 63  63  63  ASN ASN B . n 
A 1 64  SER 64  64  64  SER SER B . n 
A 1 65  GLY 65  65  65  GLY GLY B . n 
A 1 66  HIS 66  66  66  HIS HIS B . n 
A 1 67  SER 67  67  67  SER SER B . n 
A 1 68  PHE 68  68  68  PHE PHE B . n 
A 1 69  ASN 69  69  69  ASN ASN B . n 
A 1 70  VAL 70  70  70  VAL VAL B . n 
A 1 71  ASP 71  71  71  ASP ASP B . n 
A 1 72  PHE 72  72  72  PHE PHE B . n 
A 1 73  ASP 73  73  73  ASP ASP B . n 
A 1 74  ASP 74  74  74  ASP ASP B . n 
A 1 75  THR 75  75  75  THR THR B . n 
A 1 76  GLU 76  76  76  GLU GLU B . n 
A 1 77  ASN 77  77  77  ASN ASN B . n 
A 1 78  LYS 78  78  78  LYS LYS B . n 
A 1 79  SER 79  79  79  SER SER B . n 
A 1 80  VAL 80  80  80  VAL VAL B . n 
A 1 81  LEU 81  81  81  LEU LEU B . n 
A 1 82  ARG 82  82  82  ARG ARG B . n 
A 1 83  GLY 83  83  83  GLY GLY B . n 
A 1 84  GLY 84  84  84  GLY GLY B . n 
A 1 85  PRO 85  85  85  PRO PRO B . n 
A 1 86  LEU 86  86  86  LEU LEU B . n 
A 1 87  THR 87  87  87  THR THR B . n 
A 1 88  GLY 88  88  88  GLY GLY B . n 
A 1 89  SER 89  89  89  SER SER B . n 
A 1 90  TYR 90  90  90  TYR TYR B . n 
A 1 91  ARG 91  91  91  ARG ARG B . n 
A 1 92  LEU 92  92  92  LEU LEU B . n 
A 1 93  ARG 93  93  93  ARG ARG B . n 
A 1 94  GLN 94  94  94  GLN GLN B . n 
A 1 95  VAL 95  95  95  VAL VAL B . n 
A 1 96  HIS 96  96  96  HIS HIS B . n 
A 1 97  LEU 97  97  97  LEU LEU B . n 
A 1 98  HIS 98  98  98  HIS HIS B . n 
A 1 99  TRP 99  99  99  TRP TRP B . n 
A 1 100 GLY 100 100 100 GLY GLY B . n 
A 1 101 SER 101 101 101 SER SER B . n 
A 1 102 ALA 102 102 102 ALA ALA B . n 
A 1 103 ASP 103 103 103 ASP ASP B . n 
A 1 104 ASP 104 104 104 ASP ASP B . n 
A 1 105 HIS 105 105 105 HIS HIS B . n 
A 1 106 GLY 106 106 106 GLY GLY B . n 
A 1 107 SER 107 107 107 SER SER B . n 
A 1 108 GLU 108 108 108 GLU GLU B . n 
A 1 109 HIS 109 109 109 HIS HIS B . n 
A 1 110 ILE 110 110 110 ILE ILE B . n 
A 1 111 VAL 111 111 111 VAL VAL B . n 
A 1 112 ASP 112 112 112 ASP ASP B . n 
A 1 113 GLY 113 113 113 GLY GLY B . n 
A 1 114 VAL 114 114 114 VAL VAL B . n 
A 1 115 SER 115 115 115 SER SER B . n 
A 1 116 TYR 116 116 116 TYR TYR B . n 
A 1 117 ALA 117 117 117 ALA ALA B . n 
A 1 118 ALA 118 118 118 ALA ALA B . n 
A 1 119 GLU 119 119 119 GLU GLU B . n 
A 1 120 LEU 120 120 120 LEU LEU B . n 
A 1 121 HIS 121 121 121 HIS HIS B . n 
A 1 122 VAL 122 122 122 VAL VAL B . n 
A 1 123 VAL 123 123 123 VAL VAL B . n 
A 1 124 HIS 124 124 124 HIS HIS B . n 
A 1 125 TRP 125 125 125 TRP TRP B . n 
A 1 126 ASN 126 126 126 ASN ASN B . n 
A 1 127 SER 127 127 127 SER SER B . n 
A 1 128 ASP 128 128 128 ASP ASP B . n 
A 1 129 LYS 129 129 129 LYS LYS B . n 
A 1 130 TYR 130 130 130 TYR TYR B . n 
A 1 131 PRO 131 131 131 PRO PRO B . n 
A 1 132 SER 132 132 132 SER SER B . n 
A 1 133 PHE 133 133 133 PHE PHE B . n 
A 1 134 VAL 134 134 134 VAL VAL B . n 
A 1 135 GLU 135 135 135 GLU GLU B . n 
A 1 136 ALA 136 136 136 ALA ALA B . n 
A 1 137 ALA 137 137 137 ALA ALA B . n 
A 1 138 HIS 138 138 138 HIS HIS B . n 
A 1 139 GLU 139 139 139 GLU GLU B . n 
A 1 140 PRO 140 140 140 PRO PRO B . n 
A 1 141 ASP 141 141 141 ASP ASP B . n 
A 1 142 GLY 142 142 142 GLY GLY B . n 
A 1 143 LEU 143 143 143 LEU LEU B . n 
A 1 144 ALA 144 144 144 ALA ALA B . n 
A 1 145 VAL 145 145 145 VAL VAL B . n 
A 1 146 LEU 146 146 146 LEU LEU B . n 
A 1 147 GLY 147 147 147 GLY GLY B . n 
A 1 148 VAL 148 148 148 VAL VAL B . n 
A 1 149 PHE 149 149 149 PHE PHE B . n 
A 1 150 LEU 150 150 150 LEU LEU B . n 
A 1 151 GLN 151 151 151 GLN GLN B . n 
A 1 152 ILE 152 152 152 ILE ILE B . n 
A 1 153 GLY 153 153 153 GLY GLY B . n 
A 1 154 GLU 154 154 154 GLU GLU B . n 
A 1 155 PRO 155 155 155 PRO PRO B . n 
A 1 156 ASN 156 156 156 ASN ASN B . n 
A 1 157 SER 157 157 157 SER SER B . n 
A 1 158 GLN 158 158 158 GLN GLN B . n 
A 1 159 LEU 159 159 159 LEU LEU B . n 
A 1 160 GLN 160 160 160 GLN GLN B . n 
A 1 161 LYS 161 161 161 LYS LYS B . n 
A 1 162 ILE 162 162 162 ILE ILE B . n 
A 1 163 THR 163 163 163 THR THR B . n 
A 1 164 ASP 164 164 164 ASP ASP B . n 
A 1 165 THR 165 165 165 THR THR B . n 
A 1 166 LEU 166 166 166 LEU LEU B . n 
A 1 167 ASP 167 167 167 ASP ASP B . n 
A 1 168 SER 168 168 168 SER SER B . n 
A 1 169 ILE 169 169 169 ILE ILE B . n 
A 1 170 LYS 170 170 170 LYS LYS B . n 
A 1 171 GLU 171 171 171 GLU GLU B . n 
A 1 172 LYS 172 172 172 LYS LYS B . n 
A 1 173 GLY 173 173 173 GLY GLY B . n 
A 1 174 LYS 174 174 174 LYS LYS B . n 
A 1 175 GLN 175 175 175 GLN GLN B . n 
A 1 176 THR 176 176 176 THR THR B . n 
A 1 177 ARG 177 177 177 ARG ARG B . n 
A 1 178 PHE 178 178 178 PHE PHE B . n 
A 1 179 THR 179 179 179 THR THR B . n 
A 1 180 ASN 180 180 180 ASN ASN B . n 
A 1 181 PHE 181 181 181 PHE PHE B . n 
A 1 182 ASP 182 182 182 ASP ASP B . n 
A 1 183 LEU 183 183 183 LEU LEU B . n 
A 1 184 LEU 184 184 184 LEU LEU B . n 
A 1 185 SER 185 185 185 SER SER B . n 
A 1 186 LEU 186 186 186 LEU LEU B . n 
A 1 187 LEU 187 187 187 LEU LEU B . n 
A 1 188 PRO 188 188 188 PRO PRO B . n 
A 1 189 PRO 189 189 189 PRO PRO B . n 
A 1 190 SER 190 190 190 SER SER B . n 
A 1 191 TRP 191 191 191 TRP TRP B . n 
A 1 192 ASP 192 192 192 ASP ASP B . n 
A 1 193 TYR 193 193 193 TYR TYR B . n 
A 1 194 TRP 194 194 194 TRP TRP B . n 
A 1 195 THR 195 195 195 THR THR B . n 
A 1 196 TYR 196 196 196 TYR TYR B . n 
A 1 197 PRO 197 197 197 PRO PRO B . n 
A 1 198 GLY 198 198 198 GLY GLY B . n 
A 1 199 SER 199 199 199 SER SER B . n 
A 1 200 LEU 200 200 200 LEU LEU B . n 
A 1 201 THR 201 201 201 THR THR B . n 
A 1 202 VAL 202 202 202 VAL VAL B . n 
A 1 203 PRO 203 203 203 PRO PRO B . n 
A 1 204 PRO 204 204 204 PRO PRO B . n 
A 1 205 LEU 205 205 205 LEU LEU B . n 
A 1 206 LEU 206 206 206 LEU LEU B . n 
A 1 207 GLU 207 207 207 GLU GLU B . n 
A 1 208 SER 208 208 208 SER SER B . n 
A 1 209 VAL 209 209 209 VAL VAL B . n 
A 1 210 THR 210 210 210 THR THR B . n 
A 1 211 TRP 211 211 211 TRP TRP B . n 
A 1 212 ILE 212 212 212 ILE ILE B . n 
A 1 213 VAL 213 213 213 VAL VAL B . n 
A 1 214 LEU 214 214 214 LEU LEU B . n 
A 1 215 LYS 215 215 215 LYS LYS B . n 
A 1 216 GLN 216 216 216 GLN GLN B . n 
A 1 217 PRO 217 217 217 PRO PRO B . n 
A 1 218 ILE 218 218 218 ILE ILE B . n 
A 1 219 ASN 219 219 219 ASN ASN B . n 
A 1 220 ILE 220 220 220 ILE ILE B . n 
A 1 221 SER 221 221 221 SER SER B . n 
A 1 222 SER 222 222 222 SER SER B . n 
A 1 223 GLN 223 223 223 GLN GLN B . n 
A 1 224 GLN 224 224 224 GLN GLN B . n 
A 1 225 LEU 225 225 225 LEU LEU B . n 
A 1 226 ALA 226 226 226 ALA ALA B . n 
A 1 227 LYS 227 227 227 LYS LYS B . n 
A 1 228 PHE 228 228 228 PHE PHE B . n 
A 1 229 ARG 229 229 229 ARG ARG B . n 
A 1 230 SER 230 230 230 SER SER B . n 
A 1 231 LEU 231 231 231 LEU LEU B . n 
A 1 232 LEU 232 232 232 LEU LEU B . n 
A 1 233 CYS 233 233 233 CYS CYS B . n 
A 1 234 THR 234 234 234 THR THR B . n 
A 1 235 ALA 235 235 235 ALA ALA B . n 
A 1 236 GLU 236 236 236 GLU GLU B . n 
A 1 237 GLY 237 237 237 GLY GLY B . n 
A 1 238 GLU 238 238 238 GLU GLU B . n 
A 1 239 ALA 239 239 239 ALA ALA B . n 
A 1 240 ALA 240 240 240 ALA ALA B . n 
A 1 241 ALA 241 241 241 ALA ALA B . n 
A 1 242 PHE 242 242 242 PHE PHE B . n 
A 1 243 LEU 243 243 243 LEU LEU B . n 
A 1 244 VAL 244 244 244 VAL VAL B . n 
A 1 245 SER 245 245 245 SER SER B . n 
A 1 246 ASN 246 246 246 ASN ASN B . n 
A 1 247 HIS 247 247 247 HIS HIS B . n 
A 1 248 ARG 248 248 248 ARG ARG B . n 
A 1 249 PRO 249 249 249 PRO PRO B . n 
A 1 250 PRO 250 250 250 PRO PRO B . n 
A 1 251 GLN 251 251 251 GLN GLN B . n 
A 1 252 PRO 252 252 252 PRO PRO B . n 
A 1 253 LEU 253 253 253 LEU LEU B . n 
A 1 254 LYS 254 254 254 LYS LYS B . n 
A 1 255 GLY 255 255 255 GLY GLY B . n 
A 1 256 ARG 256 256 256 ARG ARG B . n 
A 1 257 LYS 257 257 257 LYS LYS B . n 
A 1 258 VAL 258 258 258 VAL VAL B . n 
A 1 259 ARG 259 259 259 ARG ARG B . n 
A 1 260 ALA 260 260 260 ALA ALA B . n 
A 1 261 SER 261 261 261 SER SER B . n 
A 1 262 PHE 262 262 262 PHE PHE B . n 
A 1 263 HIS 263 263 263 HIS HIS B . n 
B 1 1   MET 1   1   ?   ?   ?   A . n 
B 1 2   MET 2   2   ?   ?   ?   A . n 
B 1 3   SER 3   3   ?   ?   ?   A . n 
B 1 4   ARG 4   4   ?   ?   ?   A . n 
B 1 5   LEU 5   5   5   LEU LEU A . n 
B 1 6   SER 6   6   6   SER SER A . n 
B 1 7   TRP 7   7   7   TRP TRP A . n 
B 1 8   GLY 8   8   8   GLY GLY A . n 
B 1 9   TYR 9   9   9   TYR TYR A . n 
B 1 10  ARG 10  10  10  ARG ARG A . n 
B 1 11  GLU 11  11  11  GLU GLU A . n 
B 1 12  HIS 12  12  12  HIS HIS A . n 
B 1 13  ASN 13  13  13  ASN ASN A . n 
B 1 14  GLY 14  14  14  GLY GLY A . n 
B 1 15  PRO 15  15  15  PRO PRO A . n 
B 1 16  ILE 16  16  16  ILE ILE A . n 
B 1 17  HIS 17  17  17  HIS HIS A . n 
B 1 18  TRP 18  18  18  TRP TRP A . n 
B 1 19  LYS 19  19  19  LYS LYS A . n 
B 1 20  GLU 20  20  20  GLU GLU A . n 
B 1 21  PHE 21  21  21  PHE PHE A . n 
B 1 22  PHE 22  22  22  PHE PHE A . n 
B 1 23  PRO 23  23  23  PRO PRO A . n 
B 1 24  ILE 24  24  24  ILE ILE A . n 
B 1 25  ALA 25  25  25  ALA ALA A . n 
B 1 26  ASP 26  26  26  ASP ASP A . n 
B 1 27  GLY 27  27  27  GLY GLY A . n 
B 1 28  ASP 28  28  28  ASP ASP A . n 
B 1 29  GLN 29  29  29  GLN GLN A . n 
B 1 30  GLN 30  30  30  GLN GLN A . n 
B 1 31  SER 31  31  31  SER SER A . n 
B 1 32  PRO 32  32  32  PRO PRO A . n 
B 1 33  ILE 33  33  33  ILE ILE A . n 
B 1 34  GLU 34  34  34  GLU GLU A . n 
B 1 35  ILE 35  35  35  ILE ILE A . n 
B 1 36  LYS 36  36  36  LYS LYS A . n 
B 1 37  THR 37  37  37  THR THR A . n 
B 1 38  LYS 38  38  38  LYS LYS A . n 
B 1 39  GLU 39  39  39  GLU GLU A . n 
B 1 40  VAL 40  40  40  VAL VAL A . n 
B 1 41  LYS 41  41  41  LYS LYS A . n 
B 1 42  TYR 42  42  42  TYR TYR A . n 
B 1 43  ASP 43  43  43  ASP ASP A . n 
B 1 44  SER 44  44  44  SER SER A . n 
B 1 45  SER 45  45  45  SER SER A . n 
B 1 46  LEU 46  46  46  LEU LEU A . n 
B 1 47  ARG 47  47  47  ARG ARG A . n 
B 1 48  PRO 48  48  48  PRO PRO A . n 
B 1 49  LEU 49  49  49  LEU LEU A . n 
B 1 50  SER 50  50  50  SER SER A . n 
B 1 51  ILE 51  51  51  ILE ILE A . n 
B 1 52  LYS 52  52  52  LYS LYS A . n 
B 1 53  TYR 53  53  53  TYR TYR A . n 
B 1 54  ASP 54  54  54  ASP ASP A . n 
B 1 55  PRO 55  55  55  PRO PRO A . n 
B 1 56  SER 56  56  56  SER SER A . n 
B 1 57  SER 57  57  57  SER SER A . n 
B 1 58  ALA 58  58  58  ALA ALA A . n 
B 1 59  LYS 59  59  59  LYS LYS A . n 
B 1 60  ILE 60  60  60  ILE ILE A . n 
B 1 61  ILE 61  61  61  ILE ILE A . n 
B 1 62  SER 62  62  62  SER SER A . n 
B 1 63  ASN 63  63  63  ASN ASN A . n 
B 1 64  SER 64  64  64  SER SER A . n 
B 1 65  GLY 65  65  65  GLY GLY A . n 
B 1 66  HIS 66  66  66  HIS HIS A . n 
B 1 67  SER 67  67  67  SER SER A . n 
B 1 68  PHE 68  68  68  PHE PHE A . n 
B 1 69  ASN 69  69  69  ASN ASN A . n 
B 1 70  VAL 70  70  70  VAL VAL A . n 
B 1 71  ASP 71  71  71  ASP ASP A . n 
B 1 72  PHE 72  72  72  PHE PHE A . n 
B 1 73  ASP 73  73  73  ASP ASP A . n 
B 1 74  ASP 74  74  74  ASP ASP A . n 
B 1 75  THR 75  75  75  THR THR A . n 
B 1 76  GLU 76  76  76  GLU GLU A . n 
B 1 77  ASN 77  77  77  ASN ASN A . n 
B 1 78  LYS 78  78  78  LYS LYS A . n 
B 1 79  SER 79  79  79  SER SER A . n 
B 1 80  VAL 80  80  80  VAL VAL A . n 
B 1 81  LEU 81  81  81  LEU LEU A . n 
B 1 82  ARG 82  82  82  ARG ARG A . n 
B 1 83  GLY 83  83  83  GLY GLY A . n 
B 1 84  GLY 84  84  84  GLY GLY A . n 
B 1 85  PRO 85  85  85  PRO PRO A . n 
B 1 86  LEU 86  86  86  LEU LEU A . n 
B 1 87  THR 87  87  87  THR THR A . n 
B 1 88  GLY 88  88  88  GLY GLY A . n 
B 1 89  SER 89  89  89  SER SER A . n 
B 1 90  TYR 90  90  90  TYR TYR A . n 
B 1 91  ARG 91  91  91  ARG ARG A . n 
B 1 92  LEU 92  92  92  LEU LEU A . n 
B 1 93  ARG 93  93  93  ARG ARG A . n 
B 1 94  GLN 94  94  94  GLN GLN A . n 
B 1 95  VAL 95  95  95  VAL VAL A . n 
B 1 96  HIS 96  96  96  HIS HIS A . n 
B 1 97  LEU 97  97  97  LEU LEU A . n 
B 1 98  HIS 98  98  98  HIS HIS A . n 
B 1 99  TRP 99  99  99  TRP TRP A . n 
B 1 100 GLY 100 100 100 GLY GLY A . n 
B 1 101 SER 101 101 101 SER SER A . n 
B 1 102 ALA 102 102 102 ALA ALA A . n 
B 1 103 ASP 103 103 103 ASP ASP A . n 
B 1 104 ASP 104 104 104 ASP ASP A . n 
B 1 105 HIS 105 105 105 HIS HIS A . n 
B 1 106 GLY 106 106 106 GLY GLY A . n 
B 1 107 SER 107 107 107 SER SER A . n 
B 1 108 GLU 108 108 108 GLU GLU A . n 
B 1 109 HIS 109 109 109 HIS HIS A . n 
B 1 110 ILE 110 110 110 ILE ILE A . n 
B 1 111 VAL 111 111 111 VAL VAL A . n 
B 1 112 ASP 112 112 112 ASP ASP A . n 
B 1 113 GLY 113 113 113 GLY GLY A . n 
B 1 114 VAL 114 114 114 VAL VAL A . n 
B 1 115 SER 115 115 115 SER SER A . n 
B 1 116 TYR 116 116 116 TYR TYR A . n 
B 1 117 ALA 117 117 117 ALA ALA A . n 
B 1 118 ALA 118 118 118 ALA ALA A . n 
B 1 119 GLU 119 119 119 GLU GLU A . n 
B 1 120 LEU 120 120 120 LEU LEU A . n 
B 1 121 HIS 121 121 121 HIS HIS A . n 
B 1 122 VAL 122 122 122 VAL VAL A . n 
B 1 123 VAL 123 123 123 VAL VAL A . n 
B 1 124 HIS 124 124 124 HIS HIS A . n 
B 1 125 TRP 125 125 125 TRP TRP A . n 
B 1 126 ASN 126 126 126 ASN ASN A . n 
B 1 127 SER 127 127 127 SER SER A . n 
B 1 128 ASP 128 128 128 ASP ASP A . n 
B 1 129 LYS 129 129 129 LYS LYS A . n 
B 1 130 TYR 130 130 130 TYR TYR A . n 
B 1 131 PRO 131 131 131 PRO PRO A . n 
B 1 132 SER 132 132 132 SER SER A . n 
B 1 133 PHE 133 133 133 PHE PHE A . n 
B 1 134 VAL 134 134 134 VAL VAL A . n 
B 1 135 GLU 135 135 135 GLU GLU A . n 
B 1 136 ALA 136 136 136 ALA ALA A . n 
B 1 137 ALA 137 137 137 ALA ALA A . n 
B 1 138 HIS 138 138 138 HIS HIS A . n 
B 1 139 GLU 139 139 139 GLU GLU A . n 
B 1 140 PRO 140 140 140 PRO PRO A . n 
B 1 141 ASP 141 141 141 ASP ASP A . n 
B 1 142 GLY 142 142 142 GLY GLY A . n 
B 1 143 LEU 143 143 143 LEU LEU A . n 
B 1 144 ALA 144 144 144 ALA ALA A . n 
B 1 145 VAL 145 145 145 VAL VAL A . n 
B 1 146 LEU 146 146 146 LEU LEU A . n 
B 1 147 GLY 147 147 147 GLY GLY A . n 
B 1 148 VAL 148 148 148 VAL VAL A . n 
B 1 149 PHE 149 149 149 PHE PHE A . n 
B 1 150 LEU 150 150 150 LEU LEU A . n 
B 1 151 GLN 151 151 151 GLN GLN A . n 
B 1 152 ILE 152 152 152 ILE ILE A . n 
B 1 153 GLY 153 153 153 GLY GLY A . n 
B 1 154 GLU 154 154 154 GLU GLU A . n 
B 1 155 PRO 155 155 155 PRO PRO A . n 
B 1 156 ASN 156 156 156 ASN ASN A . n 
B 1 157 SER 157 157 157 SER SER A . n 
B 1 158 GLN 158 158 158 GLN GLN A . n 
B 1 159 LEU 159 159 159 LEU LEU A . n 
B 1 160 GLN 160 160 160 GLN GLN A . n 
B 1 161 LYS 161 161 161 LYS LYS A . n 
B 1 162 ILE 162 162 162 ILE ILE A . n 
B 1 163 THR 163 163 163 THR THR A . n 
B 1 164 ASP 164 164 164 ASP ASP A . n 
B 1 165 THR 165 165 165 THR THR A . n 
B 1 166 LEU 166 166 166 LEU LEU A . n 
B 1 167 ASP 167 167 167 ASP ASP A . n 
B 1 168 SER 168 168 168 SER SER A . n 
B 1 169 ILE 169 169 169 ILE ILE A . n 
B 1 170 LYS 170 170 170 LYS LYS A . n 
B 1 171 GLU 171 171 171 GLU GLU A . n 
B 1 172 LYS 172 172 172 LYS LYS A . n 
B 1 173 GLY 173 173 173 GLY GLY A . n 
B 1 174 LYS 174 174 174 LYS LYS A . n 
B 1 175 GLN 175 175 175 GLN GLN A . n 
B 1 176 THR 176 176 176 THR THR A . n 
B 1 177 ARG 177 177 177 ARG ARG A . n 
B 1 178 PHE 178 178 178 PHE PHE A . n 
B 1 179 THR 179 179 179 THR THR A . n 
B 1 180 ASN 180 180 180 ASN ASN A . n 
B 1 181 PHE 181 181 181 PHE PHE A . n 
B 1 182 ASP 182 182 182 ASP ASP A . n 
B 1 183 LEU 183 183 183 LEU LEU A . n 
B 1 184 LEU 184 184 184 LEU LEU A . n 
B 1 185 SER 185 185 185 SER SER A . n 
B 1 186 LEU 186 186 186 LEU LEU A . n 
B 1 187 LEU 187 187 187 LEU LEU A . n 
B 1 188 PRO 188 188 188 PRO PRO A . n 
B 1 189 PRO 189 189 189 PRO PRO A . n 
B 1 190 SER 190 190 190 SER SER A . n 
B 1 191 TRP 191 191 191 TRP TRP A . n 
B 1 192 ASP 192 192 192 ASP ASP A . n 
B 1 193 TYR 193 193 193 TYR TYR A . n 
B 1 194 TRP 194 194 194 TRP TRP A . n 
B 1 195 THR 195 195 195 THR THR A . n 
B 1 196 TYR 196 196 196 TYR TYR A . n 
B 1 197 PRO 197 197 197 PRO PRO A . n 
B 1 198 GLY 198 198 198 GLY GLY A . n 
B 1 199 SER 199 199 199 SER SER A . n 
B 1 200 LEU 200 200 200 LEU LEU A . n 
B 1 201 THR 201 201 201 THR THR A . n 
B 1 202 VAL 202 202 202 VAL VAL A . n 
B 1 203 PRO 203 203 203 PRO PRO A . n 
B 1 204 PRO 204 204 204 PRO PRO A . n 
B 1 205 LEU 205 205 205 LEU LEU A . n 
B 1 206 LEU 206 206 206 LEU LEU A . n 
B 1 207 GLU 207 207 207 GLU GLU A . n 
B 1 208 SER 208 208 208 SER SER A . n 
B 1 209 VAL 209 209 209 VAL VAL A . n 
B 1 210 THR 210 210 210 THR THR A . n 
B 1 211 TRP 211 211 211 TRP TRP A . n 
B 1 212 ILE 212 212 212 ILE ILE A . n 
B 1 213 VAL 213 213 213 VAL VAL A . n 
B 1 214 LEU 214 214 214 LEU LEU A . n 
B 1 215 LYS 215 215 215 LYS LYS A . n 
B 1 216 GLN 216 216 216 GLN GLN A . n 
B 1 217 PRO 217 217 217 PRO PRO A . n 
B 1 218 ILE 218 218 218 ILE ILE A . n 
B 1 219 ASN 219 219 219 ASN ASN A . n 
B 1 220 ILE 220 220 220 ILE ILE A . n 
B 1 221 SER 221 221 221 SER SER A . n 
B 1 222 SER 222 222 222 SER SER A . n 
B 1 223 GLN 223 223 223 GLN GLN A . n 
B 1 224 GLN 224 224 224 GLN GLN A . n 
B 1 225 LEU 225 225 225 LEU LEU A . n 
B 1 226 ALA 226 226 226 ALA ALA A . n 
B 1 227 LYS 227 227 227 LYS LYS A . n 
B 1 228 PHE 228 228 228 PHE PHE A . n 
B 1 229 ARG 229 229 229 ARG ARG A . n 
B 1 230 SER 230 230 230 SER SER A . n 
B 1 231 LEU 231 231 231 LEU LEU A . n 
B 1 232 LEU 232 232 232 LEU LEU A . n 
B 1 233 CYS 233 233 233 CYS CYS A . n 
B 1 234 THR 234 234 234 THR THR A . n 
B 1 235 ALA 235 235 235 ALA ALA A . n 
B 1 236 GLU 236 236 236 GLU GLU A . n 
B 1 237 GLY 237 237 237 GLY GLY A . n 
B 1 238 GLU 238 238 238 GLU GLU A . n 
B 1 239 ALA 239 239 239 ALA ALA A . n 
B 1 240 ALA 240 240 240 ALA ALA A . n 
B 1 241 ALA 241 241 241 ALA ALA A . n 
B 1 242 PHE 242 242 242 PHE PHE A . n 
B 1 243 LEU 243 243 243 LEU LEU A . n 
B 1 244 VAL 244 244 244 VAL VAL A . n 
B 1 245 SER 245 245 245 SER SER A . n 
B 1 246 ASN 246 246 246 ASN ASN A . n 
B 1 247 HIS 247 247 247 HIS HIS A . n 
B 1 248 ARG 248 248 248 ARG ARG A . n 
B 1 249 PRO 249 249 249 PRO PRO A . n 
B 1 250 PRO 250 250 250 PRO PRO A . n 
B 1 251 GLN 251 251 251 GLN GLN A . n 
B 1 252 PRO 252 252 252 PRO PRO A . n 
B 1 253 LEU 253 253 253 LEU LEU A . n 
B 1 254 LYS 254 254 254 LYS LYS A . n 
B 1 255 GLY 255 255 255 GLY GLY A . n 
B 1 256 ARG 256 256 256 ARG ARG A . n 
B 1 257 LYS 257 257 257 LYS LYS A . n 
B 1 258 VAL 258 258 258 VAL VAL A . n 
B 1 259 ARG 259 259 259 ARG ARG A . n 
B 1 260 ALA 260 260 260 ALA ALA A . n 
B 1 261 SER 261 261 261 SER SER A . n 
B 1 262 PHE 262 262 262 PHE PHE A . n 
B 1 263 HIS 263 263 263 HIS HIS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN  1   301 1   ZN  ZN  B . 
D 3 V13 1   302 1   V13 V13 B . 
E 4 EDO 1   303 7   EDO EGL B . 
F 4 EDO 1   304 8   EDO EGL B . 
G 2 ZN  1   301 2   ZN  ZN  A . 
H 3 V13 1   302 2   V13 V13 A . 
I 5 PEG 1   303 1   PEG PEG A . 
J 4 EDO 1   304 2   EDO EGL A . 
K 4 EDO 1   305 3   EDO EGL A . 
L 4 EDO 1   306 4   EDO EGL A . 
M 4 EDO 1   307 5   EDO EGL A . 
N 4 EDO 1   308 6   EDO EGL A . 
O 6 HOH 1   401 1   HOH HOH B . 
O 6 HOH 2   402 2   HOH HOH B . 
O 6 HOH 3   403 5   HOH HOH B . 
O 6 HOH 4   404 6   HOH HOH B . 
O 6 HOH 5   405 8   HOH HOH B . 
O 6 HOH 6   406 9   HOH HOH B . 
O 6 HOH 7   407 10  HOH HOH B . 
O 6 HOH 8   408 11  HOH HOH B . 
O 6 HOH 9   409 13  HOH HOH B . 
O 6 HOH 10  410 17  HOH HOH B . 
O 6 HOH 11  411 19  HOH HOH B . 
O 6 HOH 12  412 20  HOH HOH B . 
O 6 HOH 13  413 24  HOH HOH B . 
O 6 HOH 14  414 25  HOH HOH B . 
O 6 HOH 15  415 26  HOH HOH B . 
O 6 HOH 16  416 27  HOH HOH B . 
O 6 HOH 17  417 34  HOH HOH B . 
O 6 HOH 18  418 35  HOH HOH B . 
O 6 HOH 19  419 37  HOH HOH B . 
O 6 HOH 20  420 39  HOH HOH B . 
O 6 HOH 21  421 41  HOH HOH B . 
O 6 HOH 22  422 42  HOH HOH B . 
O 6 HOH 23  423 43  HOH HOH B . 
O 6 HOH 24  424 48  HOH HOH B . 
O 6 HOH 25  425 50  HOH HOH B . 
O 6 HOH 26  426 51  HOH HOH B . 
O 6 HOH 27  427 53  HOH HOH B . 
O 6 HOH 28  428 54  HOH HOH B . 
O 6 HOH 29  429 56  HOH HOH B . 
O 6 HOH 30  430 57  HOH HOH B . 
O 6 HOH 31  431 58  HOH HOH B . 
O 6 HOH 32  432 59  HOH HOH B . 
O 6 HOH 33  433 62  HOH HOH B . 
O 6 HOH 34  434 65  HOH HOH B . 
O 6 HOH 35  435 68  HOH HOH B . 
O 6 HOH 36  436 69  HOH HOH B . 
O 6 HOH 37  437 70  HOH HOH B . 
O 6 HOH 38  438 71  HOH HOH B . 
O 6 HOH 39  439 74  HOH HOH B . 
O 6 HOH 40  440 75  HOH HOH B . 
O 6 HOH 41  441 80  HOH HOH B . 
O 6 HOH 42  442 82  HOH HOH B . 
O 6 HOH 43  443 83  HOH HOH B . 
O 6 HOH 44  444 85  HOH HOH B . 
O 6 HOH 45  445 86  HOH HOH B . 
O 6 HOH 46  446 89  HOH HOH B . 
O 6 HOH 47  447 90  HOH HOH B . 
O 6 HOH 48  448 92  HOH HOH B . 
O 6 HOH 49  449 96  HOH HOH B . 
O 6 HOH 50  450 97  HOH HOH B . 
O 6 HOH 51  451 98  HOH HOH B . 
O 6 HOH 52  452 100 HOH HOH B . 
O 6 HOH 53  453 101 HOH HOH B . 
O 6 HOH 54  454 103 HOH HOH B . 
O 6 HOH 55  455 106 HOH HOH B . 
O 6 HOH 56  456 108 HOH HOH B . 
O 6 HOH 57  457 109 HOH HOH B . 
O 6 HOH 58  458 111 HOH HOH B . 
O 6 HOH 59  459 112 HOH HOH B . 
O 6 HOH 60  460 113 HOH HOH B . 
O 6 HOH 61  461 114 HOH HOH B . 
O 6 HOH 62  462 115 HOH HOH B . 
O 6 HOH 63  463 116 HOH HOH B . 
O 6 HOH 64  464 119 HOH HOH B . 
O 6 HOH 65  465 120 HOH HOH B . 
O 6 HOH 66  466 121 HOH HOH B . 
O 6 HOH 67  467 122 HOH HOH B . 
O 6 HOH 68  468 123 HOH HOH B . 
O 6 HOH 69  469 126 HOH HOH B . 
O 6 HOH 70  470 129 HOH HOH B . 
O 6 HOH 71  471 130 HOH HOH B . 
O 6 HOH 72  472 131 HOH HOH B . 
O 6 HOH 73  473 135 HOH HOH B . 
O 6 HOH 74  474 137 HOH HOH B . 
O 6 HOH 75  475 139 HOH HOH B . 
O 6 HOH 76  476 142 HOH HOH B . 
O 6 HOH 77  477 145 HOH HOH B . 
O 6 HOH 78  478 146 HOH HOH B . 
O 6 HOH 79  479 147 HOH HOH B . 
O 6 HOH 80  480 148 HOH HOH B . 
O 6 HOH 81  481 149 HOH HOH B . 
O 6 HOH 82  482 150 HOH HOH B . 
O 6 HOH 83  483 194 HOH HOH B . 
O 6 HOH 84  484 196 HOH HOH B . 
O 6 HOH 85  485 197 HOH HOH B . 
O 6 HOH 86  486 198 HOH HOH B . 
O 6 HOH 87  487 200 HOH HOH B . 
O 6 HOH 88  488 226 HOH HOH B . 
O 6 HOH 89  489 227 HOH HOH B . 
O 6 HOH 90  490 228 HOH HOH B . 
O 6 HOH 91  491 229 HOH HOH B . 
O 6 HOH 92  492 230 HOH HOH B . 
O 6 HOH 93  493 231 HOH HOH B . 
O 6 HOH 94  494 232 HOH HOH B . 
O 6 HOH 95  495 233 HOH HOH B . 
O 6 HOH 96  496 234 HOH HOH B . 
O 6 HOH 97  497 235 HOH HOH B . 
O 6 HOH 98  498 236 HOH HOH B . 
O 6 HOH 99  499 237 HOH HOH B . 
O 6 HOH 100 500 238 HOH HOH B . 
O 6 HOH 101 501 239 HOH HOH B . 
O 6 HOH 102 502 240 HOH HOH B . 
O 6 HOH 103 503 241 HOH HOH B . 
O 6 HOH 104 504 242 HOH HOH B . 
O 6 HOH 105 505 243 HOH HOH B . 
O 6 HOH 106 506 244 HOH HOH B . 
O 6 HOH 107 507 247 HOH HOH B . 
O 6 HOH 108 508 248 HOH HOH B . 
O 6 HOH 109 509 249 HOH HOH B . 
O 6 HOH 110 510 251 HOH HOH B . 
O 6 HOH 111 511 252 HOH HOH B . 
O 6 HOH 112 512 253 HOH HOH B . 
O 6 HOH 113 513 254 HOH HOH B . 
O 6 HOH 114 514 255 HOH HOH B . 
O 6 HOH 115 515 256 HOH HOH B . 
O 6 HOH 116 516 257 HOH HOH B . 
O 6 HOH 117 517 258 HOH HOH B . 
O 6 HOH 118 518 259 HOH HOH B . 
O 6 HOH 119 519 260 HOH HOH B . 
O 6 HOH 120 520 261 HOH HOH B . 
O 6 HOH 121 521 262 HOH HOH B . 
O 6 HOH 122 522 263 HOH HOH B . 
O 6 HOH 123 523 264 HOH HOH B . 
O 6 HOH 124 524 265 HOH HOH B . 
O 6 HOH 125 525 266 HOH HOH B . 
O 6 HOH 126 526 267 HOH HOH B . 
O 6 HOH 127 527 268 HOH HOH B . 
O 6 HOH 128 528 269 HOH HOH B . 
O 6 HOH 129 529 270 HOH HOH B . 
O 6 HOH 130 530 271 HOH HOH B . 
O 6 HOH 131 531 272 HOH HOH B . 
O 6 HOH 132 532 273 HOH HOH B . 
O 6 HOH 133 533 274 HOH HOH B . 
O 6 HOH 134 534 275 HOH HOH B . 
O 6 HOH 135 535 276 HOH HOH B . 
O 6 HOH 136 536 277 HOH HOH B . 
O 6 HOH 137 537 278 HOH HOH B . 
O 6 HOH 138 538 279 HOH HOH B . 
O 6 HOH 139 539 280 HOH HOH B . 
O 6 HOH 140 540 281 HOH HOH B . 
O 6 HOH 141 541 283 HOH HOH B . 
O 6 HOH 142 542 284 HOH HOH B . 
O 6 HOH 143 543 285 HOH HOH B . 
O 6 HOH 144 544 286 HOH HOH B . 
O 6 HOH 145 545 291 HOH HOH B . 
O 6 HOH 146 546 294 HOH HOH B . 
O 6 HOH 147 547 296 HOH HOH B . 
O 6 HOH 148 548 298 HOH HOH B . 
O 6 HOH 149 549 299 HOH HOH B . 
O 6 HOH 150 550 300 HOH HOH B . 
O 6 HOH 151 551 301 HOH HOH B . 
O 6 HOH 152 552 302 HOH HOH B . 
O 6 HOH 153 553 303 HOH HOH B . 
O 6 HOH 154 554 304 HOH HOH B . 
O 6 HOH 155 555 307 HOH HOH B . 
O 6 HOH 156 556 312 HOH HOH B . 
O 6 HOH 157 557 313 HOH HOH B . 
O 6 HOH 158 558 314 HOH HOH B . 
O 6 HOH 159 559 315 HOH HOH B . 
O 6 HOH 160 560 316 HOH HOH B . 
O 6 HOH 161 561 317 HOH HOH B . 
O 6 HOH 162 562 318 HOH HOH B . 
O 6 HOH 163 563 323 HOH HOH B . 
O 6 HOH 164 564 327 HOH HOH B . 
O 6 HOH 165 565 342 HOH HOH B . 
O 6 HOH 166 566 345 HOH HOH B . 
O 6 HOH 167 567 346 HOH HOH B . 
O 6 HOH 168 568 348 HOH HOH B . 
O 6 HOH 169 569 349 HOH HOH B . 
O 6 HOH 170 570 350 HOH HOH B . 
O 6 HOH 171 571 361 HOH HOH B . 
O 6 HOH 172 572 362 HOH HOH B . 
O 6 HOH 173 573 363 HOH HOH B . 
O 6 HOH 174 574 364 HOH HOH B . 
O 6 HOH 175 575 367 HOH HOH B . 
O 6 HOH 176 576 368 HOH HOH B . 
O 6 HOH 177 577 369 HOH HOH B . 
O 6 HOH 178 578 370 HOH HOH B . 
O 6 HOH 179 579 371 HOH HOH B . 
O 6 HOH 180 580 372 HOH HOH B . 
O 6 HOH 181 581 373 HOH HOH B . 
O 6 HOH 182 582 374 HOH HOH B . 
O 6 HOH 183 583 375 HOH HOH B . 
O 6 HOH 184 584 376 HOH HOH B . 
O 6 HOH 185 585 377 HOH HOH B . 
O 6 HOH 186 586 405 HOH HOH B . 
O 6 HOH 187 587 406 HOH HOH B . 
O 6 HOH 188 588 407 HOH HOH B . 
O 6 HOH 189 589 408 HOH HOH B . 
O 6 HOH 190 590 409 HOH HOH B . 
O 6 HOH 191 591 410 HOH HOH B . 
O 6 HOH 192 592 411 HOH HOH B . 
O 6 HOH 193 593 414 HOH HOH B . 
O 6 HOH 194 594 416 HOH HOH B . 
O 6 HOH 195 595 419 HOH HOH B . 
O 6 HOH 196 596 420 HOH HOH B . 
O 6 HOH 197 597 427 HOH HOH B . 
O 6 HOH 198 598 430 HOH HOH B . 
O 6 HOH 199 599 431 HOH HOH B . 
O 6 HOH 200 600 435 HOH HOH B . 
O 6 HOH 201 601 437 HOH HOH B . 
O 6 HOH 202 602 439 HOH HOH B . 
O 6 HOH 203 603 448 HOH HOH B . 
O 6 HOH 204 604 452 HOH HOH B . 
O 6 HOH 205 605 453 HOH HOH B . 
O 6 HOH 206 606 454 HOH HOH B . 
O 6 HOH 207 607 459 HOH HOH B . 
O 6 HOH 208 608 461 HOH HOH B . 
O 6 HOH 209 609 462 HOH HOH B . 
O 6 HOH 210 610 463 HOH HOH B . 
O 6 HOH 211 611 467 HOH HOH B . 
O 6 HOH 212 612 470 HOH HOH B . 
O 6 HOH 213 613 471 HOH HOH B . 
O 6 HOH 214 614 472 HOH HOH B . 
O 6 HOH 215 615 473 HOH HOH B . 
O 6 HOH 216 616 474 HOH HOH B . 
O 6 HOH 217 617 475 HOH HOH B . 
O 6 HOH 218 618 477 HOH HOH B . 
O 6 HOH 219 619 480 HOH HOH B . 
O 6 HOH 220 620 484 HOH HOH B . 
O 6 HOH 221 621 486 HOH HOH B . 
O 6 HOH 222 622 488 HOH HOH B . 
O 6 HOH 223 623 492 HOH HOH B . 
O 6 HOH 224 624 495 HOH HOH B . 
O 6 HOH 225 625 496 HOH HOH B . 
O 6 HOH 226 626 497 HOH HOH B . 
O 6 HOH 227 627 500 HOH HOH B . 
O 6 HOH 228 628 502 HOH HOH B . 
O 6 HOH 229 629 508 HOH HOH B . 
O 6 HOH 230 630 509 HOH HOH B . 
O 6 HOH 231 631 510 HOH HOH B . 
O 6 HOH 232 632 514 HOH HOH B . 
O 6 HOH 233 633 515 HOH HOH B . 
O 6 HOH 234 634 516 HOH HOH B . 
O 6 HOH 235 635 518 HOH HOH B . 
O 6 HOH 236 636 521 HOH HOH B . 
O 6 HOH 237 637 522 HOH HOH B . 
O 6 HOH 238 638 529 HOH HOH B . 
O 6 HOH 239 639 530 HOH HOH B . 
O 6 HOH 240 640 531 HOH HOH B . 
O 6 HOH 241 641 532 HOH HOH B . 
O 6 HOH 242 642 533 HOH HOH B . 
O 6 HOH 243 643 535 HOH HOH B . 
O 6 HOH 244 644 536 HOH HOH B . 
O 6 HOH 245 645 537 HOH HOH B . 
O 6 HOH 246 646 542 HOH HOH B . 
O 6 HOH 247 647 543 HOH HOH B . 
O 6 HOH 248 648 544 HOH HOH B . 
O 6 HOH 249 649 548 HOH HOH B . 
O 6 HOH 250 650 549 HOH HOH B . 
O 6 HOH 251 651 553 HOH HOH B . 
O 6 HOH 252 652 384 HOH HOH B . 
P 6 HOH 1   401 3   HOH HOH A . 
P 6 HOH 2   402 4   HOH HOH A . 
P 6 HOH 3   403 7   HOH HOH A . 
P 6 HOH 4   404 12  HOH HOH A . 
P 6 HOH 5   405 14  HOH HOH A . 
P 6 HOH 6   406 15  HOH HOH A . 
P 6 HOH 7   407 16  HOH HOH A . 
P 6 HOH 8   408 18  HOH HOH A . 
P 6 HOH 9   409 21  HOH HOH A . 
P 6 HOH 10  410 22  HOH HOH A . 
P 6 HOH 11  411 23  HOH HOH A . 
P 6 HOH 12  412 28  HOH HOH A . 
P 6 HOH 13  413 29  HOH HOH A . 
P 6 HOH 14  414 30  HOH HOH A . 
P 6 HOH 15  415 31  HOH HOH A . 
P 6 HOH 16  416 32  HOH HOH A . 
P 6 HOH 17  417 33  HOH HOH A . 
P 6 HOH 18  418 36  HOH HOH A . 
P 6 HOH 19  419 38  HOH HOH A . 
P 6 HOH 20  420 40  HOH HOH A . 
P 6 HOH 21  421 44  HOH HOH A . 
P 6 HOH 22  422 45  HOH HOH A . 
P 6 HOH 23  423 46  HOH HOH A . 
P 6 HOH 24  424 47  HOH HOH A . 
P 6 HOH 25  425 49  HOH HOH A . 
P 6 HOH 26  426 52  HOH HOH A . 
P 6 HOH 27  427 55  HOH HOH A . 
P 6 HOH 28  428 60  HOH HOH A . 
P 6 HOH 29  429 61  HOH HOH A . 
P 6 HOH 30  430 63  HOH HOH A . 
P 6 HOH 31  431 64  HOH HOH A . 
P 6 HOH 32  432 66  HOH HOH A . 
P 6 HOH 33  433 67  HOH HOH A . 
P 6 HOH 34  434 72  HOH HOH A . 
P 6 HOH 35  435 73  HOH HOH A . 
P 6 HOH 36  436 76  HOH HOH A . 
P 6 HOH 37  437 77  HOH HOH A . 
P 6 HOH 38  438 78  HOH HOH A . 
P 6 HOH 39  439 79  HOH HOH A . 
P 6 HOH 40  440 81  HOH HOH A . 
P 6 HOH 41  441 84  HOH HOH A . 
P 6 HOH 42  442 87  HOH HOH A . 
P 6 HOH 43  443 88  HOH HOH A . 
P 6 HOH 44  444 91  HOH HOH A . 
P 6 HOH 45  445 93  HOH HOH A . 
P 6 HOH 46  446 94  HOH HOH A . 
P 6 HOH 47  447 95  HOH HOH A . 
P 6 HOH 48  448 99  HOH HOH A . 
P 6 HOH 49  449 102 HOH HOH A . 
P 6 HOH 50  450 104 HOH HOH A . 
P 6 HOH 51  451 105 HOH HOH A . 
P 6 HOH 52  452 107 HOH HOH A . 
P 6 HOH 53  453 110 HOH HOH A . 
P 6 HOH 54  454 117 HOH HOH A . 
P 6 HOH 55  455 118 HOH HOH A . 
P 6 HOH 56  456 124 HOH HOH A . 
P 6 HOH 57  457 125 HOH HOH A . 
P 6 HOH 58  458 127 HOH HOH A . 
P 6 HOH 59  459 128 HOH HOH A . 
P 6 HOH 60  460 132 HOH HOH A . 
P 6 HOH 61  461 133 HOH HOH A . 
P 6 HOH 62  462 134 HOH HOH A . 
P 6 HOH 63  463 136 HOH HOH A . 
P 6 HOH 64  464 138 HOH HOH A . 
P 6 HOH 65  465 140 HOH HOH A . 
P 6 HOH 66  466 141 HOH HOH A . 
P 6 HOH 67  467 143 HOH HOH A . 
P 6 HOH 68  468 144 HOH HOH A . 
P 6 HOH 69  469 151 HOH HOH A . 
P 6 HOH 70  470 152 HOH HOH A . 
P 6 HOH 71  471 153 HOH HOH A . 
P 6 HOH 72  472 154 HOH HOH A . 
P 6 HOH 73  473 155 HOH HOH A . 
P 6 HOH 74  474 156 HOH HOH A . 
P 6 HOH 75  475 157 HOH HOH A . 
P 6 HOH 76  476 158 HOH HOH A . 
P 6 HOH 77  477 159 HOH HOH A . 
P 6 HOH 78  478 160 HOH HOH A . 
P 6 HOH 79  479 161 HOH HOH A . 
P 6 HOH 80  480 162 HOH HOH A . 
P 6 HOH 81  481 163 HOH HOH A . 
P 6 HOH 82  482 164 HOH HOH A . 
P 6 HOH 83  483 165 HOH HOH A . 
P 6 HOH 84  484 166 HOH HOH A . 
P 6 HOH 85  485 167 HOH HOH A . 
P 6 HOH 86  486 168 HOH HOH A . 
P 6 HOH 87  487 169 HOH HOH A . 
P 6 HOH 88  488 170 HOH HOH A . 
P 6 HOH 89  489 171 HOH HOH A . 
P 6 HOH 90  490 172 HOH HOH A . 
P 6 HOH 91  491 173 HOH HOH A . 
P 6 HOH 92  492 174 HOH HOH A . 
P 6 HOH 93  493 175 HOH HOH A . 
P 6 HOH 94  494 176 HOH HOH A . 
P 6 HOH 95  495 177 HOH HOH A . 
P 6 HOH 96  496 178 HOH HOH A . 
P 6 HOH 97  497 179 HOH HOH A . 
P 6 HOH 98  498 180 HOH HOH A . 
P 6 HOH 99  499 181 HOH HOH A . 
P 6 HOH 100 500 182 HOH HOH A . 
P 6 HOH 101 501 183 HOH HOH A . 
P 6 HOH 102 502 184 HOH HOH A . 
P 6 HOH 103 503 185 HOH HOH A . 
P 6 HOH 104 504 186 HOH HOH A . 
P 6 HOH 105 505 187 HOH HOH A . 
P 6 HOH 106 506 188 HOH HOH A . 
P 6 HOH 107 507 189 HOH HOH A . 
P 6 HOH 108 508 190 HOH HOH A . 
P 6 HOH 109 509 191 HOH HOH A . 
P 6 HOH 110 510 192 HOH HOH A . 
P 6 HOH 111 511 193 HOH HOH A . 
P 6 HOH 112 512 195 HOH HOH A . 
P 6 HOH 113 513 199 HOH HOH A . 
P 6 HOH 114 514 201 HOH HOH A . 
P 6 HOH 115 515 202 HOH HOH A . 
P 6 HOH 116 516 203 HOH HOH A . 
P 6 HOH 117 517 204 HOH HOH A . 
P 6 HOH 118 518 205 HOH HOH A . 
P 6 HOH 119 519 206 HOH HOH A . 
P 6 HOH 120 520 207 HOH HOH A . 
P 6 HOH 121 521 208 HOH HOH A . 
P 6 HOH 122 522 209 HOH HOH A . 
P 6 HOH 123 523 210 HOH HOH A . 
P 6 HOH 124 524 211 HOH HOH A . 
P 6 HOH 125 525 212 HOH HOH A . 
P 6 HOH 126 526 213 HOH HOH A . 
P 6 HOH 127 527 214 HOH HOH A . 
P 6 HOH 128 528 215 HOH HOH A . 
P 6 HOH 129 529 216 HOH HOH A . 
P 6 HOH 130 530 217 HOH HOH A . 
P 6 HOH 131 531 218 HOH HOH A . 
P 6 HOH 132 532 219 HOH HOH A . 
P 6 HOH 133 533 220 HOH HOH A . 
P 6 HOH 134 534 221 HOH HOH A . 
P 6 HOH 135 535 222 HOH HOH A . 
P 6 HOH 136 536 223 HOH HOH A . 
P 6 HOH 137 537 224 HOH HOH A . 
P 6 HOH 138 538 225 HOH HOH A . 
P 6 HOH 139 539 245 HOH HOH A . 
P 6 HOH 140 540 246 HOH HOH A . 
P 6 HOH 141 541 250 HOH HOH A . 
P 6 HOH 142 542 282 HOH HOH A . 
P 6 HOH 143 543 287 HOH HOH A . 
P 6 HOH 144 544 288 HOH HOH A . 
P 6 HOH 145 545 289 HOH HOH A . 
P 6 HOH 146 546 290 HOH HOH A . 
P 6 HOH 147 547 292 HOH HOH A . 
P 6 HOH 148 548 293 HOH HOH A . 
P 6 HOH 149 549 295 HOH HOH A . 
P 6 HOH 150 550 297 HOH HOH A . 
P 6 HOH 151 551 305 HOH HOH A . 
P 6 HOH 152 552 306 HOH HOH A . 
P 6 HOH 153 553 308 HOH HOH A . 
P 6 HOH 154 554 309 HOH HOH A . 
P 6 HOH 155 555 310 HOH HOH A . 
P 6 HOH 156 556 311 HOH HOH A . 
P 6 HOH 157 557 319 HOH HOH A . 
P 6 HOH 158 558 320 HOH HOH A . 
P 6 HOH 159 559 321 HOH HOH A . 
P 6 HOH 160 560 322 HOH HOH A . 
P 6 HOH 161 561 324 HOH HOH A . 
P 6 HOH 162 562 325 HOH HOH A . 
P 6 HOH 163 563 326 HOH HOH A . 
P 6 HOH 164 564 328 HOH HOH A . 
P 6 HOH 165 565 329 HOH HOH A . 
P 6 HOH 166 566 330 HOH HOH A . 
P 6 HOH 167 567 331 HOH HOH A . 
P 6 HOH 168 568 332 HOH HOH A . 
P 6 HOH 169 569 333 HOH HOH A . 
P 6 HOH 170 570 334 HOH HOH A . 
P 6 HOH 171 571 335 HOH HOH A . 
P 6 HOH 172 572 336 HOH HOH A . 
P 6 HOH 173 573 337 HOH HOH A . 
P 6 HOH 174 574 338 HOH HOH A . 
P 6 HOH 175 575 339 HOH HOH A . 
P 6 HOH 176 576 340 HOH HOH A . 
P 6 HOH 177 577 341 HOH HOH A . 
P 6 HOH 178 578 343 HOH HOH A . 
P 6 HOH 179 579 344 HOH HOH A . 
P 6 HOH 180 580 347 HOH HOH A . 
P 6 HOH 181 581 351 HOH HOH A . 
P 6 HOH 182 582 352 HOH HOH A . 
P 6 HOH 183 583 353 HOH HOH A . 
P 6 HOH 184 584 354 HOH HOH A . 
P 6 HOH 185 585 355 HOH HOH A . 
P 6 HOH 186 586 356 HOH HOH A . 
P 6 HOH 187 587 357 HOH HOH A . 
P 6 HOH 188 588 358 HOH HOH A . 
P 6 HOH 189 589 359 HOH HOH A . 
P 6 HOH 190 590 360 HOH HOH A . 
P 6 HOH 191 591 365 HOH HOH A . 
P 6 HOH 192 592 366 HOH HOH A . 
P 6 HOH 193 593 378 HOH HOH A . 
P 6 HOH 194 594 379 HOH HOH A . 
P 6 HOH 195 595 380 HOH HOH A . 
P 6 HOH 196 596 381 HOH HOH A . 
P 6 HOH 197 597 382 HOH HOH A . 
P 6 HOH 198 598 383 HOH HOH A . 
P 6 HOH 199 599 385 HOH HOH A . 
P 6 HOH 200 600 386 HOH HOH A . 
P 6 HOH 201 601 387 HOH HOH A . 
P 6 HOH 202 602 388 HOH HOH A . 
P 6 HOH 203 603 389 HOH HOH A . 
P 6 HOH 204 604 390 HOH HOH A . 
P 6 HOH 205 605 391 HOH HOH A . 
P 6 HOH 206 606 392 HOH HOH A . 
P 6 HOH 207 607 393 HOH HOH A . 
P 6 HOH 208 608 394 HOH HOH A . 
P 6 HOH 209 609 395 HOH HOH A . 
P 6 HOH 210 610 396 HOH HOH A . 
P 6 HOH 211 611 397 HOH HOH A . 
P 6 HOH 212 612 398 HOH HOH A . 
P 6 HOH 213 613 399 HOH HOH A . 
P 6 HOH 214 614 400 HOH HOH A . 
P 6 HOH 215 615 401 HOH HOH A . 
P 6 HOH 216 616 402 HOH HOH A . 
P 6 HOH 217 617 403 HOH HOH A . 
P 6 HOH 218 618 404 HOH HOH A . 
P 6 HOH 219 619 412 HOH HOH A . 
P 6 HOH 220 620 413 HOH HOH A . 
P 6 HOH 221 621 415 HOH HOH A . 
P 6 HOH 222 622 417 HOH HOH A . 
P 6 HOH 223 623 418 HOH HOH A . 
P 6 HOH 224 624 421 HOH HOH A . 
P 6 HOH 225 625 422 HOH HOH A . 
P 6 HOH 226 626 423 HOH HOH A . 
P 6 HOH 227 627 424 HOH HOH A . 
P 6 HOH 228 628 425 HOH HOH A . 
P 6 HOH 229 629 426 HOH HOH A . 
P 6 HOH 230 630 428 HOH HOH A . 
P 6 HOH 231 631 429 HOH HOH A . 
P 6 HOH 232 632 432 HOH HOH A . 
P 6 HOH 233 633 433 HOH HOH A . 
P 6 HOH 234 634 434 HOH HOH A . 
P 6 HOH 235 635 436 HOH HOH A . 
P 6 HOH 236 636 438 HOH HOH A . 
P 6 HOH 237 637 440 HOH HOH A . 
P 6 HOH 238 638 441 HOH HOH A . 
P 6 HOH 239 639 442 HOH HOH A . 
P 6 HOH 240 640 443 HOH HOH A . 
P 6 HOH 241 641 444 HOH HOH A . 
P 6 HOH 242 642 445 HOH HOH A . 
P 6 HOH 243 643 446 HOH HOH A . 
P 6 HOH 244 644 447 HOH HOH A . 
P 6 HOH 245 645 449 HOH HOH A . 
P 6 HOH 246 646 450 HOH HOH A . 
P 6 HOH 247 647 451 HOH HOH A . 
P 6 HOH 248 648 455 HOH HOH A . 
P 6 HOH 249 649 456 HOH HOH A . 
P 6 HOH 250 650 457 HOH HOH A . 
P 6 HOH 251 651 458 HOH HOH A . 
P 6 HOH 252 652 460 HOH HOH A . 
P 6 HOH 253 653 464 HOH HOH A . 
P 6 HOH 254 654 465 HOH HOH A . 
P 6 HOH 255 655 466 HOH HOH A . 
P 6 HOH 256 656 468 HOH HOH A . 
P 6 HOH 257 657 469 HOH HOH A . 
P 6 HOH 258 658 476 HOH HOH A . 
P 6 HOH 259 659 478 HOH HOH A . 
P 6 HOH 260 660 479 HOH HOH A . 
P 6 HOH 261 661 481 HOH HOH A . 
P 6 HOH 262 662 482 HOH HOH A . 
P 6 HOH 263 663 483 HOH HOH A . 
P 6 HOH 264 664 485 HOH HOH A . 
P 6 HOH 265 665 487 HOH HOH A . 
P 6 HOH 266 666 489 HOH HOH A . 
P 6 HOH 267 667 490 HOH HOH A . 
P 6 HOH 268 668 491 HOH HOH A . 
P 6 HOH 269 669 493 HOH HOH A . 
P 6 HOH 270 670 494 HOH HOH A . 
P 6 HOH 271 671 498 HOH HOH A . 
P 6 HOH 272 672 499 HOH HOH A . 
P 6 HOH 273 673 501 HOH HOH A . 
P 6 HOH 274 674 503 HOH HOH A . 
P 6 HOH 275 675 504 HOH HOH A . 
P 6 HOH 276 676 505 HOH HOH A . 
P 6 HOH 277 677 506 HOH HOH A . 
P 6 HOH 278 678 507 HOH HOH A . 
P 6 HOH 279 679 511 HOH HOH A . 
P 6 HOH 280 680 512 HOH HOH A . 
P 6 HOH 281 681 513 HOH HOH A . 
P 6 HOH 282 682 517 HOH HOH A . 
P 6 HOH 283 683 519 HOH HOH A . 
P 6 HOH 284 684 520 HOH HOH A . 
P 6 HOH 285 685 523 HOH HOH A . 
P 6 HOH 286 686 524 HOH HOH A . 
P 6 HOH 287 687 525 HOH HOH A . 
P 6 HOH 288 688 526 HOH HOH A . 
P 6 HOH 289 689 527 HOH HOH A . 
P 6 HOH 290 690 528 HOH HOH A . 
P 6 HOH 291 691 534 HOH HOH A . 
P 6 HOH 292 692 538 HOH HOH A . 
P 6 HOH 293 693 539 HOH HOH A . 
P 6 HOH 294 694 540 HOH HOH A . 
P 6 HOH 295 695 541 HOH HOH A . 
P 6 HOH 296 696 545 HOH HOH A . 
P 6 HOH 297 697 546 HOH HOH A . 
P 6 HOH 298 698 547 HOH HOH A . 
P 6 HOH 299 699 550 HOH HOH A . 
P 6 HOH 300 700 551 HOH HOH A . 
P 6 HOH 301 701 552 HOH HOH A . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,O         
2 1 B,G,H,I,J,K,L,M,N,P 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 NE2 ? A HIS 98  ? B HIS 98  ? 1_555 103.6 ? 
2  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 ND1 ? A HIS 121 ? B HIS 121 ? 1_555 114.4 ? 
3  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 ND1 ? A HIS 121 ? B HIS 121 ? 1_555 103.1 ? 
4  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D V13 .   ? B V13 302 ? 1_555 117.6 ? 
5  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D V13 .   ? B V13 302 ? 1_555 107.9 ? 
6  ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D V13 .   ? B V13 302 ? 1_555 108.8 ? 
7  NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 103.4 ? 
8  NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 117.5 ? 
9  NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 100.1 ? 
10 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N10 ? H V13 .   ? A V13 302 ? 1_555 114.8 ? 
11 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N10 ? H V13 .   ? A V13 302 ? 1_555 109.1 ? 
12 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N10 ? H V13 .   ? A V13 302 ? 1_555 110.2 ? 
# 
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 2013-04-10 
2 'Structure model' 1 1 2023-09-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' diffrn_source                 
5 2 'Structure model' pdbx_initial_refinement_model 
6 2 'Structure model' pdbx_struct_conn_angle        
7 2 'Structure model' struct_conn                   
8 2 'Structure model' struct_ref_seq_dif            
9 2 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_database_2.pdbx_DOI'                        
2  2 'Structure model' '_database_2.pdbx_database_accession'         
3  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_asym_id'  
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_asym_id'  
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_asym_id'  
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
15 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
16 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
17 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
18 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
19 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
20 2 'Structure model' '_pdbx_struct_conn_angle.value'               
21 2 'Structure model' '_struct_conn.pdbx_dist_value'                
22 2 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
23 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
24 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
25 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
26 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
27 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
28 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
29 2 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
30 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
31 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
32 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
33 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
34 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
35 2 'Structure model' '_struct_ref_seq_dif.details'                 
36 2 'Structure model' '_struct_site.pdbx_auth_asym_id'              
37 2 'Structure model' '_struct_site.pdbx_auth_comp_id'              
38 2 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.3.20 2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
MAR345dtb   .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
MOLREP      .      ?               ?       ?                    ?                        phasing           ? ?          ? 6 
# 
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 B 77  ? ? -97.06  38.34   
2 1 PHE B 178 ? ? -160.50 96.47   
3 1 ASN B 246 ? ? -151.47 42.39   
4 1 SER A 67  ? ? -177.58 -178.50 
5 1 ASN A 77  ? ? -93.38  42.52   
6 1 HIS A 105 ? ? -152.82 69.77   
7 1 ASN A 246 ? ? -147.30 49.59   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 B MET 1 ? A MET 1 
2 1 Y 1 B MET 2 ? A MET 2 
3 1 Y 1 B SER 3 ? A SER 3 
4 1 Y 1 A MET 1 ? B MET 1 
5 1 Y 1 A MET 2 ? B MET 2 
6 1 Y 1 A SER 3 ? B SER 3 
7 1 Y 1 A ARG 4 ? B ARG 4 
# 
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 
PEG C1   C  N N 260 
PEG O1   O  N N 261 
PEG C2   C  N N 262 
PEG O2   O  N N 263 
PEG C3   C  N N 264 
PEG C4   C  N N 265 
PEG O4   O  N N 266 
PEG H11  H  N N 267 
PEG H12  H  N N 268 
PEG HO1  H  N N 269 
PEG H21  H  N N 270 
PEG H22  H  N N 271 
PEG H31  H  N N 272 
PEG H32  H  N N 273 
PEG H41  H  N N 274 
PEG H42  H  N N 275 
PEG HO4  H  N N 276 
PHE N    N  N N 277 
PHE CA   C  N S 278 
PHE C    C  N N 279 
PHE O    O  N N 280 
PHE CB   C  N N 281 
PHE CG   C  Y N 282 
PHE CD1  C  Y N 283 
PHE CD2  C  Y N 284 
PHE CE1  C  Y N 285 
PHE CE2  C  Y N 286 
PHE CZ   C  Y N 287 
PHE OXT  O  N N 288 
PHE H    H  N N 289 
PHE H2   H  N N 290 
PHE HA   H  N N 291 
PHE HB2  H  N N 292 
PHE HB3  H  N N 293 
PHE HD1  H  N N 294 
PHE HD2  H  N N 295 
PHE HE1  H  N N 296 
PHE HE2  H  N N 297 
PHE HZ   H  N N 298 
PHE HXT  H  N N 299 
PRO N    N  N N 300 
PRO CA   C  N S 301 
PRO C    C  N N 302 
PRO O    O  N N 303 
PRO CB   C  N N 304 
PRO CG   C  N N 305 
PRO CD   C  N N 306 
PRO OXT  O  N N 307 
PRO H    H  N N 308 
PRO HA   H  N N 309 
PRO HB2  H  N N 310 
PRO HB3  H  N N 311 
PRO HG2  H  N N 312 
PRO HG3  H  N N 313 
PRO HD2  H  N N 314 
PRO HD3  H  N N 315 
PRO HXT  H  N N 316 
SER N    N  N N 317 
SER CA   C  N S 318 
SER C    C  N N 319 
SER O    O  N N 320 
SER CB   C  N N 321 
SER OG   O  N N 322 
SER OXT  O  N N 323 
SER H    H  N N 324 
SER H2   H  N N 325 
SER HA   H  N N 326 
SER HB2  H  N N 327 
SER HB3  H  N N 328 
SER HG   H  N N 329 
SER HXT  H  N N 330 
THR N    N  N N 331 
THR CA   C  N S 332 
THR C    C  N N 333 
THR O    O  N N 334 
THR CB   C  N R 335 
THR OG1  O  N N 336 
THR CG2  C  N N 337 
THR OXT  O  N N 338 
THR H    H  N N 339 
THR H2   H  N N 340 
THR HA   H  N N 341 
THR HB   H  N N 342 
THR HG1  H  N N 343 
THR HG21 H  N N 344 
THR HG22 H  N N 345 
THR HG23 H  N N 346 
THR HXT  H  N N 347 
TRP N    N  N N 348 
TRP CA   C  N S 349 
TRP C    C  N N 350 
TRP O    O  N N 351 
TRP CB   C  N N 352 
TRP CG   C  Y N 353 
TRP CD1  C  Y N 354 
TRP CD2  C  Y N 355 
TRP NE1  N  Y N 356 
TRP CE2  C  Y N 357 
TRP CE3  C  Y N 358 
TRP CZ2  C  Y N 359 
TRP CZ3  C  Y N 360 
TRP CH2  C  Y N 361 
TRP OXT  O  N N 362 
TRP H    H  N N 363 
TRP H2   H  N N 364 
TRP HA   H  N N 365 
TRP HB2  H  N N 366 
TRP HB3  H  N N 367 
TRP HD1  H  N N 368 
TRP HE1  H  N N 369 
TRP HE3  H  N N 370 
TRP HZ2  H  N N 371 
TRP HZ3  H  N N 372 
TRP HH2  H  N N 373 
TRP HXT  H  N N 374 
TYR N    N  N N 375 
TYR CA   C  N S 376 
TYR C    C  N N 377 
TYR O    O  N N 378 
TYR CB   C  N N 379 
TYR CG   C  Y N 380 
TYR CD1  C  Y N 381 
TYR CD2  C  Y N 382 
TYR CE1  C  Y N 383 
TYR CE2  C  Y N 384 
TYR CZ   C  Y N 385 
TYR OH   O  N N 386 
TYR OXT  O  N N 387 
TYR H    H  N N 388 
TYR H2   H  N N 389 
TYR HA   H  N N 390 
TYR HB2  H  N N 391 
TYR HB3  H  N N 392 
TYR HD1  H  N N 393 
TYR HD2  H  N N 394 
TYR HE1  H  N N 395 
TYR HE2  H  N N 396 
TYR HH   H  N N 397 
TYR HXT  H  N N 398 
V13 O20  O  N N 399 
V13 S15  S  N N 400 
V13 O19  O  N N 401 
V13 C16  C  N N 402 
V13 C17  C  N N 403 
V13 O18  O  N N 404 
V13 C1   C  Y N 405 
V13 C6   C  Y N 406 
V13 F11  F  N N 407 
V13 C5   C  Y N 408 
V13 F12  F  N N 409 
V13 C4   C  Y N 410 
V13 S7   S  N N 411 
V13 O9   O  N N 412 
V13 N10  N  N N 413 
V13 O8   O  N N 414 
V13 C3   C  Y N 415 
V13 F13  F  N N 416 
V13 C2   C  Y N 417 
V13 F14  F  N N 418 
V13 H1   H  N N 419 
V13 H2   H  N N 420 
V13 H3   H  N N 421 
V13 H4   H  N N 422 
V13 H5   H  N N 423 
V13 H6   H  N N 424 
V13 H7   H  N N 425 
VAL N    N  N N 426 
VAL CA   C  N S 427 
VAL C    C  N N 428 
VAL O    O  N N 429 
VAL CB   C  N N 430 
VAL CG1  C  N N 431 
VAL CG2  C  N N 432 
VAL OXT  O  N N 433 
VAL H    H  N N 434 
VAL H2   H  N N 435 
VAL HA   H  N N 436 
VAL HB   H  N N 437 
VAL HG11 H  N N 438 
VAL HG12 H  N N 439 
VAL HG13 H  N N 440 
VAL HG21 H  N N 441 
VAL HG22 H  N N 442 
VAL HG23 H  N N 443 
VAL HXT  H  N N 444 
ZN  ZN   ZN N N 445 
# 
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 
PEG C1  O1   sing N N 246 
PEG C1  C2   sing N N 247 
PEG C1  H11  sing N N 248 
PEG C1  H12  sing N N 249 
PEG O1  HO1  sing N N 250 
PEG C2  O2   sing N N 251 
PEG C2  H21  sing N N 252 
PEG C2  H22  sing N N 253 
PEG O2  C3   sing N N 254 
PEG C3  C4   sing N N 255 
PEG C3  H31  sing N N 256 
PEG C3  H32  sing N N 257 
PEG C4  O4   sing N N 258 
PEG C4  H41  sing N N 259 
PEG C4  H42  sing N N 260 
PEG O4  HO4  sing N N 261 
PHE N   CA   sing N N 262 
PHE N   H    sing N N 263 
PHE N   H2   sing N N 264 
PHE CA  C    sing N N 265 
PHE CA  CB   sing N N 266 
PHE CA  HA   sing N N 267 
PHE C   O    doub N N 268 
PHE C   OXT  sing N N 269 
PHE CB  CG   sing N N 270 
PHE CB  HB2  sing N N 271 
PHE CB  HB3  sing N N 272 
PHE CG  CD1  doub Y N 273 
PHE CG  CD2  sing Y N 274 
PHE CD1 CE1  sing Y N 275 
PHE CD1 HD1  sing N N 276 
PHE CD2 CE2  doub Y N 277 
PHE CD2 HD2  sing N N 278 
PHE CE1 CZ   doub Y N 279 
PHE CE1 HE1  sing N N 280 
PHE CE2 CZ   sing Y N 281 
PHE CE2 HE2  sing N N 282 
PHE CZ  HZ   sing N N 283 
PHE OXT HXT  sing N N 284 
PRO N   CA   sing N N 285 
PRO N   CD   sing N N 286 
PRO N   H    sing N N 287 
PRO CA  C    sing N N 288 
PRO CA  CB   sing N N 289 
PRO CA  HA   sing N N 290 
PRO C   O    doub N N 291 
PRO C   OXT  sing N N 292 
PRO CB  CG   sing N N 293 
PRO CB  HB2  sing N N 294 
PRO CB  HB3  sing N N 295 
PRO CG  CD   sing N N 296 
PRO CG  HG2  sing N N 297 
PRO CG  HG3  sing N N 298 
PRO CD  HD2  sing N N 299 
PRO CD  HD3  sing N N 300 
PRO OXT HXT  sing N N 301 
SER N   CA   sing N N 302 
SER N   H    sing N N 303 
SER N   H2   sing N N 304 
SER CA  C    sing N N 305 
SER CA  CB   sing N N 306 
SER CA  HA   sing N N 307 
SER C   O    doub N N 308 
SER C   OXT  sing N N 309 
SER CB  OG   sing N N 310 
SER CB  HB2  sing N N 311 
SER CB  HB3  sing N N 312 
SER OG  HG   sing N N 313 
SER OXT HXT  sing N N 314 
THR N   CA   sing N N 315 
THR N   H    sing N N 316 
THR N   H2   sing N N 317 
THR CA  C    sing N N 318 
THR CA  CB   sing N N 319 
THR CA  HA   sing N N 320 
THR C   O    doub N N 321 
THR C   OXT  sing N N 322 
THR CB  OG1  sing N N 323 
THR CB  CG2  sing N N 324 
THR CB  HB   sing N N 325 
THR OG1 HG1  sing N N 326 
THR CG2 HG21 sing N N 327 
THR CG2 HG22 sing N N 328 
THR CG2 HG23 sing N N 329 
THR OXT HXT  sing N N 330 
TRP N   CA   sing N N 331 
TRP N   H    sing N N 332 
TRP N   H2   sing N N 333 
TRP CA  C    sing N N 334 
TRP CA  CB   sing N N 335 
TRP CA  HA   sing N N 336 
TRP C   O    doub N N 337 
TRP C   OXT  sing N N 338 
TRP CB  CG   sing N N 339 
TRP CB  HB2  sing N N 340 
TRP CB  HB3  sing N N 341 
TRP CG  CD1  doub Y N 342 
TRP CG  CD2  sing Y N 343 
TRP CD1 NE1  sing Y N 344 
TRP CD1 HD1  sing N N 345 
TRP CD2 CE2  doub Y N 346 
TRP CD2 CE3  sing Y N 347 
TRP NE1 CE2  sing Y N 348 
TRP NE1 HE1  sing N N 349 
TRP CE2 CZ2  sing Y N 350 
TRP CE3 CZ3  doub Y N 351 
TRP CE3 HE3  sing N N 352 
TRP CZ2 CH2  doub Y N 353 
TRP CZ2 HZ2  sing N N 354 
TRP CZ3 CH2  sing Y N 355 
TRP CZ3 HZ3  sing N N 356 
TRP CH2 HH2  sing N N 357 
TRP OXT HXT  sing N N 358 
TYR N   CA   sing N N 359 
TYR N   H    sing N N 360 
TYR N   H2   sing N N 361 
TYR CA  C    sing N N 362 
TYR CA  CB   sing N N 363 
TYR CA  HA   sing N N 364 
TYR C   O    doub N N 365 
TYR C   OXT  sing N N 366 
TYR CB  CG   sing N N 367 
TYR CB  HB2  sing N N 368 
TYR CB  HB3  sing N N 369 
TYR CG  CD1  doub Y N 370 
TYR CG  CD2  sing Y N 371 
TYR CD1 CE1  sing Y N 372 
TYR CD1 HD1  sing N N 373 
TYR CD2 CE2  doub Y N 374 
TYR CD2 HD2  sing N N 375 
TYR CE1 CZ   doub Y N 376 
TYR CE1 HE1  sing N N 377 
TYR CE2 CZ   sing Y N 378 
TYR CE2 HE2  sing N N 379 
TYR CZ  OH   sing N N 380 
TYR OH  HH   sing N N 381 
TYR OXT HXT  sing N N 382 
V13 C17 C16  sing N N 383 
V13 C17 O18  sing N N 384 
V13 F11 C6   sing N N 385 
V13 O20 S15  doub N N 386 
V13 C16 S15  sing N N 387 
V13 S15 C1   sing N N 388 
V13 S15 O19  doub N N 389 
V13 F12 C5   sing N N 390 
V13 C6  C5   doub Y N 391 
V13 C6  C1   sing Y N 392 
V13 C5  C4   sing Y N 393 
V13 C1  C2   doub Y N 394 
V13 C2  F14  sing N N 395 
V13 C2  C3   sing Y N 396 
V13 C4  C3   doub Y N 397 
V13 C4  S7   sing N N 398 
V13 O8  S7   doub N N 399 
V13 O9  S7   doub N N 400 
V13 C3  F13  sing N N 401 
V13 S7  N10  sing N N 402 
V13 C16 H1   sing N N 403 
V13 C16 H2   sing N N 404 
V13 C17 H3   sing N N 405 
V13 C17 H4   sing N N 406 
V13 O18 H5   sing N N 407 
V13 N10 H6   sing N N 408 
V13 N10 H7   sing N N 409 
VAL N   CA   sing N N 410 
VAL N   H    sing N N 411 
VAL N   H2   sing N N 412 
VAL CA  C    sing N N 413 
VAL CA  CB   sing N N 414 
VAL CA  HA   sing N N 415 
VAL C   O    doub N N 416 
VAL C   OXT  sing N N 417 
VAL CB  CG1  sing N N 418 
VAL CB  CG2  sing N N 419 
VAL CB  HB   sing N N 420 
VAL CG1 HG11 sing N N 421 
VAL CG1 HG12 sing N N 422 
VAL CG1 HG13 sing N N 423 
VAL CG2 HG21 sing N N 424 
VAL CG2 HG22 sing N N 425 
VAL CG2 HG23 sing N N 426 
VAL OXT HXT  sing N N 427 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                           ZN  
3 '2,3,5,6-tetrafluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' V13 
4 1,2-ETHANEDIOL                                                       EDO 
5 'DI(HYDROXYETHYL)ETHER'                                              PEG 
6 water                                                                HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2NNO 
_pdbx_initial_refinement_model.details          'PDB ENTRY 2NNO' 
# 
