data_4KNN
# 
_entry.id   4KNN 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.381 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   4KNN         pdb_00004knn 10.2210/pdb4knn/pdb 
RCSB  RCSB079564   ?            ?                   
WWPDB D_1000079564 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4KNI . unspecified 
PDB 4KNJ . unspecified 
PDB 4KNM . unspecified 
PDB 4KP5 . unspecified 
PDB 4KP8 . unspecified 
# 
_pdbx_database_status.entry_id                        4KNN 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2013-05-10 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smirnov, A.'  1 
'Manakova, E.' 2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Benzenesulfonamides with pyrimidine moiety as inhibitors of human carbonic anhydrases I, II, VI, VII, XII, and XIII' 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_volume            21 
_citation.page_first                6937 
_citation.page_last                 6947 
_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   24103428 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2013.09.029 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1  ? 
primary 'Zubriene, A.'      2  ? 
primary 'Smirnov, A.'       3  ? 
primary 'Torresan, J.'      4  ? 
primary 'Kisonaite, M.'     5  ? 
primary 'Kazokaite, J.'     6  ? 
primary 'Gylyte, J.'        7  ? 
primary 'Michailoviene, V.' 8  ? 
primary 'Jogaite, V.'       9  ? 
primary 'Manakova, E.'      10 ? 
primary 'Grazulis, S.'      11 ? 
primary 'Tumkevicius, S.'   12 ? 
primary 'Matulis, D.'       13 ? 
# 
_cell.entry_id           4KNN 
_cell.length_a           56.182 
_cell.length_b           57.470 
_cell.length_c           159.467 
_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                         4KNN 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.Int_Tables_number                19 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 13'                                         29613.318 2   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                      65.409    2   ?       ? ? ? 
3 non-polymer syn '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' 343.809   2   ?       ? ? ? 
4 non-polymer syn 'CITRIC ACID'                                                   192.124   2   ?       ? ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                  62.068    3   ?       ? ? ? 
6 non-polymer syn 'ACETIC ACID'                                                   60.052    3   ?       ? ? ? 
7 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                         106.120   1   ?       ? ? ? 
8 water       nat water                                                           18.015    568 ?       ? ? ? 
# 
_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 4KNN B 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
2 1 4KNN 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 4KNN MET B 1 ? UNP Q8N1Q1 ? ? 'expression tag' 1 1 
2 4KNN 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 
ACY non-polymer         . 'ACETIC ACID'                                                   ?                 'C2 H4 O2'            
60.052  
ALA 'L-peptide linking' y ALANINE                                                         ?                 'C3 H7 N O2'          
89.093  
ARG 'L-peptide linking' y ARGININE                                                        ?                 'C6 H15 N4 O2 1'      
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                      ?                 'C4 H8 N2 O3'         
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                 ?                 'C4 H7 N O4'          
133.103 
CIT non-polymer         . 'CITRIC ACID'                                                   ?                 'C6 H8 O7'            
192.124 
CYS 'L-peptide linking' y CYSTEINE                                                        ?                 'C3 H7 N O2 S'        
121.158 
E1F non-polymer         . '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' ?                 'C12 H10 Cl N3 O3 S2' 
343.809 
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 
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          4KNN 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   44.2 
_exptl_crystal.density_Matthews      2.2 
_exptl_crystal.pdbx_mosaicity        0.2 
_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              6 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    
'0.1M ammonium citrate (pH 7.0), 0.1M sodium acetate (pH 4.5) and 26% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2012-11-30 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    
'High Heat Load (HHL) Monochromator: Si 111; Large Offset Monochromator (LOM): Si 311, Si 511' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
# 
_reflns.entry_id                     4KNN 
_reflns.d_resolution_high            1.404 
_reflns.d_resolution_low             79.733 
_reflns.number_all                   ? 
_reflns.number_obs                   99914 
_reflns.pdbx_Rmerge_I_obs            0.038 
_reflns.pdbx_netI_over_sigmaI        26.400 
_reflns.pdbx_Rsym_value              0.038 
_reflns.pdbx_redundancy              6.600 
_reflns.percent_possible_obs         98.300 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        14.992 
_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.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.40 1.48  ? 82680 ? ? 0.262 3.0  0.262 ? 6.10 ? 5.50  ? 13550 ? ? 0.313 ? 92.60 0.31 0.12 1  1 
1.48 1.57  ? 92541 ? ? 0.175 4.4  0.175 ? 6.70 ? 8.70  ? 13768 ? ? 0.207 ? 99.20 0.21 0.08 2  1 
1.57 1.68  ? 86236 ? ? 0.120 6.3  0.120 ? 6.60 ? 12.50 ? 13017 ? ? 0.143 ? 99.40 0.14 0.05 3  1 
1.68 1.81  ? 83125 ? ? 0.081 9.1  0.081 ? 6.90 ? 18.50 ? 12117 ? ? 0.097 ? 99.40 0.10 0.04 4  1 
1.81 1.99  ? 72937 ? ? 0.054 12.8 0.054 ? 6.50 ? 26.60 ? 11164 ? ? 0.065 ? 99.30 0.06 0.03 5  1 
1.99 2.22  ? 70552 ? ? 0.041 16.5 0.041 ? 6.90 ? 37.40 ? 10185 ? ? 0.050 ? 99.60 0.05 0.02 6  1 
2.22 2.56  ? 58755 ? ? 0.035 18.9 0.035 ? 6.60 ? 44.00 ? 8948  ? ? 0.042 ? 98.90 0.04 0.02 7  1 
2.56 3.14  ? 53397 ? ? 0.031 19.7 0.031 ? 6.90 ? 53.50 ? 7694  ? ? 0.037 ? 99.60 0.04 0.01 8  1 
3.14 4.44  ? 38991 ? ? 0.028 20.9 0.028 ? 6.50 ? 60.00 ? 5998  ? ? 0.032 ? 99.20 0.03 0.01 9  1 
4.44 79.73 ? 21714 ? ? 0.026 19.8 0.026 ? 6.30 ? 60.40 ? 3473  ? ? 0.031 ? 99.20 0.03 0.01 10 1 
# 
_refine.entry_id                                 4KNN 
_refine.ls_d_res_high                            1.404 
_refine.ls_d_res_low                             54.070 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    98.250 
_refine.ls_number_reflns_obs                     99819 
_refine.ls_number_reflns_all                     99819 
_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                          0.169 
_refine.ls_R_factor_obs                          0.169 
_refine.ls_R_factor_R_work                       0.166 
_refine.ls_wR_factor_R_work                      0.169 
_refine.ls_R_factor_R_free                       0.191 
_refine.ls_wR_factor_R_free                      0.195 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  9987 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.534 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.310 
_refine.aniso_B[2][2]                            0.320 
_refine.aniso_B[3][3]                            -0.630 
_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               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.959 
_refine.overall_SU_R_Cruickshank_DPI             0.065 
_refine.overall_SU_R_free                        0.066 
_refine.pdbx_overall_ESU_R                       0.065 
_refine.pdbx_overall_ESU_R_Free                  0.066 
_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                   0.897 
_refine.B_iso_max                                83.21 
_refine.B_iso_min                                6.55 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      2NNO 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4108 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         101 
_refine_hist.number_atoms_solvent             568 
_refine_hist.number_atoms_total               4777 
_refine_hist.d_res_high                       1.404 
_refine_hist.d_res_low                        54.070 
# 
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         4625 0.028  0.021  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      6324 2.577  1.966  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   571  6.778  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   210  32.529 24.048 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   738  13.218 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   23   16.860 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr           650  0.178  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     3670 0.015  0.020  ? ? 'X-RAY DIFFRACTION' 
r_nbd_refined            2224 0.216  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          3131 0.320  0.200  ? ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    446  0.167  0.200  ? ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      6    0.162  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   102  0.226  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 48   0.147  0.200  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_it              2768 1.833  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcangle_it             4517 2.814  2.000  ? ? 'X-RAY DIFFRACTION' 
r_scbond_it              1857 3.202  3.000  ? ? 'X-RAY DIFFRACTION' 
r_scangle_it             1807 4.783  4.500  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.404 
_refine_ls_shell.d_res_low                        1.440 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               86.300 
_refine_ls_shell.number_reflns_R_work             5776 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.233 
_refine_ls_shell.R_factor_R_free                  0.260 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             637 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                6413 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  4KNN 
_struct.title                     
'Crystal structure of human carbonic anhydrase isozyme XIII with 2-Chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4KNN 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, LYASE-LYASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
J N N 6 ? 
K N N 2 ? 
L N N 3 ? 
M N N 4 ? 
N N N 7 ? 
O N N 5 ? 
P N N 8 ? 
Q N N 8 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  GLY A 14  ? PHE A 22  ? GLY B 14  PHE B 22  1 ? 9 
HELX_P HELX_P2  2  PRO A 23  ? GLY A 27  ? PRO B 23  GLY B 27  5 ? 5 
HELX_P HELX_P3  3  SER A 132 ? ALA A 137 ? SER B 132 ALA B 137 1 ? 6 
HELX_P HELX_P4  4  ASN A 156 ? ASP A 164 ? ASN B 156 ASP B 164 1 ? 9 
HELX_P HELX_P5  5  THR A 165 ? LYS A 170 ? THR B 165 LYS B 170 5 ? 6 
HELX_P HELX_P6  6  ASP A 182 ? LEU A 187 ? ASP B 182 LEU B 187 1 ? 6 
HELX_P HELX_P7  7  SER A 221 ? ARG A 229 ? SER B 221 ARG B 229 1 ? 9 
HELX_P HELX_P8  8  GLY B 14  ? PHE B 21  ? GLY A 14  PHE A 21  5 ? 8 
HELX_P HELX_P9  9  PHE B 22  ? GLY B 27  ? PHE A 22  GLY A 27  5 ? 6 
HELX_P HELX_P10 10 LYS B 36  ? VAL B 40  ? LYS A 36  VAL A 40  5 ? 5 
HELX_P HELX_P11 11 ASP B 54  ? SER B 56  ? ASP A 54  SER A 56  5 ? 3 
HELX_P HELX_P12 12 SER B 132 ? ALA B 137 ? SER A 132 ALA A 137 1 ? 6 
HELX_P HELX_P13 13 ASN B 156 ? GLN B 158 ? ASN A 156 GLN A 158 5 ? 3 
HELX_P HELX_P14 14 LEU B 159 ? ASP B 164 ? LEU A 159 ASP A 164 1 ? 6 
HELX_P HELX_P15 15 THR B 165 ? LYS B 170 ? THR A 165 LYS A 170 5 ? 6 
HELX_P HELX_P16 16 LEU B 183 ? LEU B 187 ? LEU A 183 LEU A 187 5 ? 5 
HELX_P HELX_P17 17 SER B 221 ? ARG B 229 ? SER A 221 ARG A 229 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 96  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc2  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 98  B ZN  301 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc3  metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 121 B ZN  301 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc4  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D E1F . N19 B ? B ZN  301 B E1F 302 1_555 ? ? ? ? ? ? ? 1.728 ? ? 
metalc5  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D E1F . N19 A ? B ZN  301 B E1F 302 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc6  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D E1F . S16 B ? B ZN  301 B E1F 302 1_555 ? ? ? ? ? ? ? 2.935 ? ? 
metalc7  metalc ? ? B HIS 96  NE2 ? ? ? 1_555 K ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc8  metalc ? ? B HIS 98  NE2 ? ? ? 1_555 K ZN  . ZN  ? ? A HIS 98  A ZN  301 1_555 ? ? ? ? ? ? ? 2.004 ? ? 
metalc9  metalc ? ? B HIS 121 ND1 ? ? ? 1_555 K ZN  . ZN  ? ? A HIS 121 A ZN  301 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc10 metalc ? ? K ZN  .   ZN  ? ? ? 1_555 L E1F . N19 ? ? A ZN  301 A E1F 302 1_555 ? ? ? ? ? ? ? 1.861 ? ? 
metalc11 metalc ? ? K ZN  .   ZN  ? ? ? 1_555 L E1F . S16 ? ? A ZN  301 A E1F 302 1_555 ? ? ? ? ? ? ? 2.996 ? ? 
# 
_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 -3.74 
2 PRO 203 A . ? PRO 203 B PRO 204 A ? PRO 204 B 1 13.51 
3 SER 31  B . ? SER 31  A PRO 32  B ? PRO 32  A 1 -0.88 
4 PRO 203 B . ? PRO 203 A PRO 204 B ? PRO 204 A 1 12.73 
# 
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  LEU A 49  ? LYS A 52  ? LEU B 49  LYS B 52  
C 2  VAL A 80  ? GLY A 83  ? VAL B 80  GLY B 83  
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  ARG B 47  ? LYS B 52  ? ARG A 47  LYS A 52  
F 2  VAL B 80  ? GLY B 84  ? VAL A 80  GLY A 84  
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 ILE A 212 ? O ILE B 212 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 GLN A 94  ? N GLN B 94  
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 ILE A 60  ? N ILE B 60  
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 GLN A 94  ? N GLN B 94  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 LEU B 214 ? O LEU A 214 N GLY B 147 ? N GLY A 147 
E 5 6  O VAL B 148 ? O VAL A 148 N LEU B 120 ? N LEU A 120 
E 6 7  O VAL B 123 ? O VAL A 123 N ARG B 93  ? N ARG A 93  
E 7 8  O VAL B 95  ? O VAL A 95  N VAL B 70  ? N VAL A 70  
E 8 9  O ASN B 69  ? O ASN A 69  N SER B 62  ? N SER A 62  
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 93  ? N ARG A 93  O VAL B 123 ? O VAL A 123 
F 4 5  N LEU B 120 ? N LEU A 120 O VAL B 148 ? O VAL A 148 
F 5 6  N GLN B 151 ? N GLN A 151 O ILE B 218 ? O ILE A 218 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software B ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN B 301'  
AC2 Software B E1F 302 ? 18 'BINDING SITE FOR RESIDUE E1F B 302' 
AC3 Software B CIT 303 ? 8  'BINDING SITE FOR RESIDUE CIT B 303' 
AC4 Software B EDO 304 ? 7  'BINDING SITE FOR RESIDUE EDO B 304' 
AC5 Software B EDO 305 ? 5  'BINDING SITE FOR RESIDUE EDO B 305' 
AC6 Software B ACY 306 ? 5  'BINDING SITE FOR RESIDUE ACY B 306' 
AC7 Software B ACY 307 ? 7  'BINDING SITE FOR RESIDUE ACY B 307' 
AC8 Software B ACY 308 ? 3  'BINDING SITE FOR RESIDUE ACY B 308' 
AC9 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
BC1 Software A E1F 302 ? 11 'BINDING SITE FOR RESIDUE E1F A 302' 
BC2 Software A CIT 303 ? 8  'BINDING SITE FOR RESIDUE CIT A 303' 
BC3 Software A PEG 304 ? 7  'BINDING SITE FOR RESIDUE PEG A 304' 
BC4 Software A EDO 305 ? 5  'BINDING SITE FOR RESIDUE EDO A 305' 
# 
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  E1F D .   ? E1F B 302 . ? 1_555 ? 
5  AC2 18 ARG A 93  ? ARG B 93  . ? 1_555 ? 
6  AC2 18 GLN A 94  ? GLN B 94  . ? 1_555 ? 
7  AC2 18 HIS A 96  ? HIS B 96  . ? 1_555 ? 
8  AC2 18 HIS A 98  ? HIS B 98  . ? 1_555 ? 
9  AC2 18 HIS A 121 ? HIS B 121 . ? 1_555 ? 
10 AC2 18 VAL A 123 ? VAL B 123 . ? 1_555 ? 
11 AC2 18 PHE A 133 ? PHE B 133 . ? 1_555 ? 
12 AC2 18 VAL A 145 ? VAL B 145 . ? 1_555 ? 
13 AC2 18 SER A 199 ? SER B 199 . ? 1_555 ? 
14 AC2 18 LEU A 200 ? LEU B 200 . ? 1_555 ? 
15 AC2 18 THR A 201 ? THR B 201 . ? 1_555 ? 
16 AC2 18 VAL A 202 ? VAL B 202 . ? 1_555 ? 
17 AC2 18 TRP A 211 ? TRP B 211 . ? 1_555 ? 
18 AC2 18 ZN  C .   ? ZN  B 301 . ? 1_555 ? 
19 AC2 18 HOH P .   ? HOH B 467 . ? 1_555 ? 
20 AC2 18 HOH P .   ? HOH B 601 . ? 1_555 ? 
21 AC2 18 HOH P .   ? HOH B 623 . ? 1_555 ? 
22 AC2 18 HOH P .   ? HOH B 644 . ? 1_555 ? 
23 AC3 8  HOH Q .   ? HOH A 466 . ? 4_545 ? 
24 AC3 8  GLY A 100 ? GLY B 100 . ? 1_555 ? 
25 AC3 8  SER A 101 ? SER B 101 . ? 1_555 ? 
26 AC3 8  HIS A 105 ? HIS B 105 . ? 1_555 ? 
27 AC3 8  SER A 245 ? SER B 245 . ? 1_555 ? 
28 AC3 8  HIS A 247 ? HIS B 247 . ? 1_555 ? 
29 AC3 8  HOH P .   ? HOH B 456 . ? 1_555 ? 
30 AC3 8  HOH P .   ? HOH B 529 . ? 1_555 ? 
31 AC4 7  ARG B 82  ? ARG A 82  . ? 1_555 ? 
32 AC4 7  GLY B 83  ? GLY A 83  . ? 1_555 ? 
33 AC4 7  PRO A 189 ? PRO B 189 . ? 1_555 ? 
34 AC4 7  SER A 190 ? SER B 190 . ? 1_555 ? 
35 AC4 7  HOH P .   ? HOH B 541 . ? 1_555 ? 
36 AC4 7  HOH P .   ? HOH B 610 . ? 1_555 ? 
37 AC4 7  HOH P .   ? HOH B 680 . ? 1_555 ? 
38 AC5 5  TYR B 42  ? TYR A 42  . ? 1_555 ? 
39 AC5 5  SER B 44  ? SER A 44  . ? 1_555 ? 
40 AC5 5  HIS B 263 ? HIS A 263 . ? 1_555 ? 
41 AC5 5  TYR A 42  ? TYR B 42  . ? 1_555 ? 
42 AC5 5  HIS A 263 ? HIS B 263 . ? 1_555 ? 
43 AC6 5  TYR A 42  ? TYR B 42  . ? 1_555 ? 
44 AC6 5  ASP A 43  ? ASP B 43  . ? 1_555 ? 
45 AC6 5  LYS A 257 ? LYS B 257 . ? 1_555 ? 
46 AC6 5  ARG A 259 ? ARG B 259 . ? 1_555 ? 
47 AC6 5  ACY I .   ? ACY B 307 . ? 1_555 ? 
48 AC7 7  HOH Q .   ? HOH A 444 . ? 1_655 ? 
49 AC7 7  HOH Q .   ? HOH A 622 . ? 1_655 ? 
50 AC7 7  LYS A 257 ? LYS B 257 . ? 1_555 ? 
51 AC7 7  ARG A 259 ? ARG B 259 . ? 1_555 ? 
52 AC7 7  ACY H .   ? ACY B 306 . ? 1_555 ? 
53 AC7 7  HOH P .   ? HOH B 498 . ? 1_555 ? 
54 AC7 7  HOH P .   ? HOH B 607 . ? 1_555 ? 
55 AC8 3  ASP B 104 ? ASP A 104 . ? 3_455 ? 
56 AC8 3  GLU A 76  ? GLU B 76  . ? 1_555 ? 
57 AC8 3  HOH P .   ? HOH B 548 . ? 1_555 ? 
58 AC9 4  HIS B 96  ? HIS A 96  . ? 1_555 ? 
59 AC9 4  HIS B 98  ? HIS A 98  . ? 1_555 ? 
60 AC9 4  HIS B 121 ? HIS A 121 . ? 1_555 ? 
61 AC9 4  E1F L .   ? E1F A 302 . ? 1_555 ? 
62 BC1 11 HIS B 96  ? HIS A 96  . ? 1_555 ? 
63 BC1 11 HIS B 98  ? HIS A 98  . ? 1_555 ? 
64 BC1 11 HIS B 121 ? HIS A 121 . ? 1_555 ? 
65 BC1 11 PHE B 133 ? PHE A 133 . ? 1_555 ? 
66 BC1 11 VAL B 145 ? VAL A 145 . ? 1_555 ? 
67 BC1 11 LEU B 200 ? LEU A 200 . ? 1_555 ? 
68 BC1 11 THR B 201 ? THR A 201 . ? 1_555 ? 
69 BC1 11 VAL B 202 ? VAL A 202 . ? 1_555 ? 
70 BC1 11 TRP B 211 ? TRP A 211 . ? 1_555 ? 
71 BC1 11 ZN  K .   ? ZN  A 301 . ? 1_555 ? 
72 BC1 11 HOH Q .   ? HOH A 589 . ? 1_555 ? 
73 BC2 8  GLY B 100 ? GLY A 100 . ? 1_555 ? 
74 BC2 8  SER B 101 ? SER A 101 . ? 1_555 ? 
75 BC2 8  HIS B 105 ? HIS A 105 . ? 1_555 ? 
76 BC2 8  GLU B 154 ? GLU A 154 . ? 3_445 ? 
77 BC2 8  SER B 245 ? SER A 245 . ? 1_555 ? 
78 BC2 8  HIS B 247 ? HIS A 247 . ? 1_555 ? 
79 BC2 8  HOH Q .   ? HOH A 575 . ? 1_555 ? 
80 BC2 8  HOH Q .   ? HOH A 620 . ? 1_555 ? 
81 BC3 7  ASP B 28  ? ASP A 28  . ? 1_555 ? 
82 BC3 7  GLN B 29  ? GLN A 29  . ? 1_555 ? 
83 BC3 7  LYS B 254 ? LYS A 254 . ? 1_555 ? 
84 BC3 7  ARG B 256 ? ARG A 256 . ? 1_555 ? 
85 BC3 7  LYS A 59  ? LYS B 59  . ? 1_545 ? 
86 BC3 7  ILE A 60  ? ILE B 60  . ? 1_545 ? 
87 BC3 7  ARG A 177 ? ARG B 177 . ? 1_545 ? 
88 BC4 5  LYS B 161 ? LYS A 161 . ? 1_555 ? 
89 BC4 5  ARG B 177 ? ARG A 177 . ? 1_555 ? 
90 BC4 5  PHE B 178 ? PHE A 178 . ? 1_555 ? 
91 BC4 5  THR B 179 ? THR A 179 . ? 1_555 ? 
92 BC4 5  HOH Q .   ? HOH A 476 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4KNN 
_atom_sites.fract_transf_matrix[1][1]   0.017799 
_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]   0.017400 
_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]   0.006271 
_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  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 6   ? 1.039   12.741  12.544  1.00 43.35 ? 6   SER B N   1 
ATOM   2    C  CA  . SER A 1 6   ? 0.782   11.434  13.230  1.00 43.31 ? 6   SER B CA  1 
ATOM   3    C  C   . SER A 1 6   ? 0.876   10.227  12.284  1.00 42.03 ? 6   SER B C   1 
ATOM   4    O  O   . SER A 1 6   ? 0.997   10.326  11.037  1.00 39.16 ? 6   SER B O   1 
ATOM   5    C  CB  . SER A 1 6   ? -0.577  11.435  13.969  1.00 45.66 ? 6   SER B CB  1 
ATOM   6    O  OG  . SER A 1 6   ? -0.472  11.711  15.368  1.00 43.45 ? 6   SER B OG  1 
ATOM   7    N  N   . TRP A 1 7   ? 0.801   9.063   12.884  1.00 32.78 ? 7   TRP B N   1 
ATOM   8    C  CA  . TRP A 1 7   ? 1.035   7.832   12.160  1.00 24.48 ? 7   TRP B CA  1 
ATOM   9    C  C   . TRP A 1 7   ? -0.002  7.514   11.085  1.00 21.47 ? 7   TRP B C   1 
ATOM   10   O  O   . TRP A 1 7   ? -1.165  7.957   11.122  1.00 21.15 ? 7   TRP B O   1 
ATOM   11   C  CB  . TRP A 1 7   ? 1.169   6.667   13.181  1.00 24.39 ? 7   TRP B CB  1 
ATOM   12   C  CG  . TRP A 1 7   ? -0.173  6.289   13.805  1.00 24.61 ? 7   TRP B CG  1 
ATOM   13   C  CD1 . TRP A 1 7   ? -0.818  6.782   14.994  1.00 21.37 ? 7   TRP B CD1 1 
ATOM   14   C  CD2 . TRP A 1 7   ? -1.091  5.265   13.289  1.00 19.56 ? 7   TRP B CD2 1 
ATOM   15   N  NE1 . TRP A 1 7   ? -2.029  6.181   15.185  1.00 23.97 ? 7   TRP B NE1 1 
ATOM   16   C  CE2 . TRP A 1 7   ? -2.245  5.215   14.209  1.00 19.90 ? 7   TRP B CE2 1 
ATOM   17   C  CE3 . TRP A 1 7   ? -1.044  4.388   12.207  1.00 17.96 ? 7   TRP B CE3 1 
ATOM   18   C  CZ2 . TRP A 1 7   ? -3.318  4.337   14.003  1.00 20.71 ? 7   TRP B CZ2 1 
ATOM   19   C  CZ3 . TRP A 1 7   ? -2.122  3.523   12.011  1.00 18.29 ? 7   TRP B CZ3 1 
ATOM   20   C  CH2 . TRP A 1 7   ? -3.219  3.495   12.895  1.00 20.50 ? 7   TRP B CH2 1 
ATOM   21   N  N   . GLY A 1 8   ? 0.399   6.696   10.121  1.00 20.04 ? 8   GLY B N   1 
ATOM   22   C  CA  . GLY A 1 8   ? -0.562  6.306   9.052   1.00 19.14 ? 8   GLY B CA  1 
ATOM   23   C  C   . GLY A 1 8   ? 0.080   5.165   8.274   1.00 15.81 ? 8   GLY B C   1 
ATOM   24   O  O   . GLY A 1 8   ? 0.851   4.362   8.808   1.00 17.82 ? 8   GLY B O   1 
ATOM   25   N  N   . TYR A 1 9   ? -0.219  5.068   6.962   1.00 15.63 ? 9   TYR B N   1 
ATOM   26   C  CA  . TYR A 1 9   ? 0.265   4.027   6.125   1.00 18.04 ? 9   TYR B CA  1 
ATOM   27   C  C   . TYR A 1 9   ? 0.937   4.584   4.845   1.00 19.00 ? 9   TYR B C   1 
ATOM   28   O  O   . TYR A 1 9   ? 1.232   3.775   3.922   1.00 21.22 ? 9   TYR B O   1 
ATOM   29   C  CB  . TYR A 1 9   ? -0.937  3.103   5.734   1.00 17.10 ? 9   TYR B CB  1 
ATOM   30   C  CG  . TYR A 1 9   ? -1.484  2.356   6.931   1.00 12.60 ? 9   TYR B CG  1 
ATOM   31   C  CD1 . TYR A 1 9   ? -0.883  1.154   7.281   1.00 13.01 ? 9   TYR B CD1 1 
ATOM   32   C  CD2 . TYR A 1 9   ? -2.570  2.834   7.626   1.00 13.54 ? 9   TYR B CD2 1 
ATOM   33   C  CE1 . TYR A 1 9   ? -1.373  0.413   8.412   1.00 11.39 ? 9   TYR B CE1 1 
ATOM   34   C  CE2 . TYR A 1 9   ? -3.146  2.094   8.719   1.00 13.04 ? 9   TYR B CE2 1 
ATOM   35   C  CZ  . TYR A 1 9   ? -2.488  0.935   9.038   1.00 11.71 ? 9   TYR B CZ  1 
ATOM   36   O  OH  . TYR A 1 9   ? -3.079  0.173   10.058  1.00 13.46 ? 9   TYR B OH  1 
ATOM   37   N  N   . ARG A 1 10  ? 1.256   5.882   4.889   1.00 20.30 ? 10  ARG B N   1 
ATOM   38   C  CA  . ARG A 1 10  ? 1.879   6.564   3.706   1.00 24.07 ? 10  ARG B CA  1 
ATOM   39   C  C   . ARG A 1 10  ? 3.360   6.470   3.939   1.00 22.72 ? 10  ARG B C   1 
ATOM   40   O  O   . ARG A 1 10  ? 3.830   5.899   4.909   1.00 21.93 ? 10  ARG B O   1 
ATOM   41   C  CB  . ARG A 1 10  ? 1.430   7.992   3.693   1.00 24.40 ? 10  ARG B CB  1 
ATOM   42   C  CG  . ARG A 1 10  ? -0.086  8.196   3.541   1.00 30.10 ? 10  ARG B CG  1 
ATOM   43   C  CD  . ARG A 1 10  ? -0.513  9.631   3.889   1.00 35.56 ? 10  ARG B CD  1 
ATOM   44   N  NE  . ARG A 1 10  ? -0.344  10.550  2.761   1.00 40.29 ? 10  ARG B NE  1 
ATOM   45   C  CZ  . ARG A 1 10  ? -0.788  11.814  2.722   1.00 39.64 ? 10  ARG B CZ  1 
ATOM   46   N  NH1 . ARG A 1 10  ? -1.458  12.344  3.739   1.00 41.19 ? 10  ARG B NH1 1 
ATOM   47   N  NH2 . ARG A 1 10  ? -0.569  12.539  1.630   1.00 41.23 ? 10  ARG B NH2 1 
ATOM   48   N  N   . GLU A 1 11  ? 4.148   7.064   3.041   1.00 30.28 ? 11  GLU B N   1 
ATOM   49   C  CA  . GLU A 1 11  ? 5.560   6.730   2.952   1.00 28.70 ? 11  GLU B CA  1 
ATOM   50   C  C   . GLU A 1 11  ? 6.323   7.168   4.209   1.00 25.37 ? 11  GLU B C   1 
ATOM   51   O  O   . GLU A 1 11  ? 7.168   6.452   4.723   1.00 28.32 ? 11  GLU B O   1 
ATOM   52   C  CB  . GLU A 1 11  ? 6.180   7.444   1.732   1.00 32.84 ? 11  GLU B CB  1 
ATOM   53   C  CG  . GLU A 1 11  ? 7.711   7.227   1.681   1.00 40.46 ? 11  GLU B CG  1 
ATOM   54   C  CD  . GLU A 1 11  ? 8.439   8.032   0.596   1.00 53.76 ? 11  GLU B CD  1 
ATOM   55   O  OE1 . GLU A 1 11  ? 9.525   7.557   0.154   1.00 59.76 ? 11  GLU B OE1 1 
ATOM   56   O  OE2 . GLU A 1 11  ? 7.933   9.118   0.188   1.00 51.51 ? 11  GLU B OE2 1 
ATOM   57   N  N   . HIS A 1 12  ? 5.954   8.337   4.681   1.00 28.51 ? 12  HIS B N   1 
ATOM   58   C  CA  . HIS A 1 12  ? 6.654   9.036   5.708   1.00 32.62 ? 12  HIS B CA  1 
ATOM   59   C  C   . HIS A 1 12  ? 6.119   8.709   7.053   1.00 31.42 ? 12  HIS B C   1 
ATOM   60   O  O   . HIS A 1 12  ? 6.746   8.983   8.043   1.00 30.04 ? 12  HIS B O   1 
ATOM   61   C  CB  . HIS A 1 12  ? 6.456   10.535  5.445   1.00 42.41 ? 12  HIS B CB  1 
ATOM   62   C  CG  . HIS A 1 12  ? 5.006   10.894  5.082   1.00 53.55 ? 12  HIS B CG  1 
ATOM   63   N  ND1 . HIS A 1 12  ? 4.064   11.275  6.020   1.00 55.03 ? 12  HIS B ND1 1 
ATOM   64   C  CD2 . HIS A 1 12  ? 4.337   10.900  3.899   1.00 56.38 ? 12  HIS B CD2 1 
ATOM   65   C  CE1 . HIS A 1 12  ? 2.901   11.516  5.445   1.00 54.74 ? 12  HIS B CE1 1 
ATOM   66   N  NE2 . HIS A 1 12  ? 3.039   11.296  4.145   1.00 59.78 ? 12  HIS B NE2 1 
ATOM   67   N  N   . ASN A 1 13  ? 4.905   8.144   7.119   1.00 23.33 ? 13  ASN B N   1 
ATOM   68   C  CA  . ASN A 1 13  ? 4.364   7.920   8.424   1.00 23.73 ? 13  ASN B CA  1 
ATOM   69   C  C   . ASN A 1 13  ? 3.945   6.460   8.648   1.00 20.70 ? 13  ASN B C   1 
ATOM   70   O  O   . ASN A 1 13  ? 3.261   6.187   9.679   1.00 21.88 ? 13  ASN B O   1 
ATOM   71   C  CB  . ASN A 1 13  ? 3.230   8.886   8.704   1.00 22.60 ? 13  ASN B CB  1 
ATOM   72   C  CG  . ASN A 1 13  ? 1.961   8.600   7.878   1.00 20.39 ? 13  ASN B CG  1 
ATOM   73   O  OD1 . ASN A 1 13  ? 1.990   7.754   6.981   1.00 22.03 ? 13  ASN B OD1 1 
ATOM   74   N  ND2 . ASN A 1 13  ? 0.942   9.379   8.044   1.00 22.57 ? 13  ASN B ND2 1 
ATOM   75   N  N   . GLY A 1 14  ? 4.416   5.602   7.739   1.00 19.88 ? 14  GLY B N   1 
ATOM   76   C  CA  . GLY A 1 14  ? 3.845   4.225   7.643   1.00 20.21 ? 14  GLY B CA  1 
ATOM   77   C  C   . GLY A 1 14  ? 4.605   3.245   8.504   1.00 22.64 ? 14  GLY B C   1 
ATOM   78   O  O   . GLY A 1 14  ? 5.523   3.595   9.264   1.00 20.00 ? 14  GLY B O   1 
ATOM   79   N  N   . PRO A 1 15  ? 4.255   1.960   8.427   1.00 18.94 ? 15  PRO B N   1 
ATOM   80   C  CA  . PRO A 1 15  ? 4.735   0.956   9.384   1.00 16.92 ? 15  PRO B CA  1 
ATOM   81   C  C   . PRO A 1 15  ? 6.225   0.968   9.671   1.00 19.27 ? 15  PRO B C   1 
ATOM   82   O  O   . PRO A 1 15  ? 6.657   0.755   10.851  1.00 19.98 ? 15  PRO B O   1 
ATOM   83   C  CB  . PRO A 1 15  ? 4.198   -0.385  8.816   1.00 16.86 ? 15  PRO B CB  1 
ATOM   84   C  CG  . PRO A 1 15  ? 2.935   0.076   8.189   1.00 16.80 ? 15  PRO B CG  1 
ATOM   85   C  CD  . PRO A 1 15  ? 3.098   1.498   7.632   1.00 18.60 ? 15  PRO B CD  1 
ATOM   86   N  N   . ILE A 1 16  ? 7.056   1.159   8.608   1.00 20.42 ? 16  ILE B N   1 
ATOM   87   C  CA  . ILE A 1 16  ? 8.490   1.087   8.873   1.00 24.44 ? 16  ILE B CA  1 
ATOM   88   C  C   . ILE A 1 16  ? 8.959   2.262   9.776   1.00 22.14 ? 16  ILE B C   1 
ATOM   89   O  O   . ILE A 1 16  ? 10.025  2.169   10.384  1.00 28.16 ? 16  ILE B O   1 
ATOM   90   C  CB  . ILE A 1 16  ? 9.261   0.931   7.539   1.00 26.80 ? 16  ILE B CB  1 
ATOM   91   C  CG1 . ILE A 1 16  ? 10.637  0.267   7.732   1.00 36.03 ? 16  ILE B CG1 1 
ATOM   92   C  CG2 . ILE A 1 16  ? 9.353   2.279   6.897   1.00 24.98 ? 16  ILE B CG2 1 
ATOM   93   C  CD1 . ILE A 1 16  ? 10.605  -1.264  7.798   1.00 42.51 ? 16  ILE B CD1 1 
ATOM   94   N  N   . HIS A 1 17  ? 8.148   3.298   9.907   1.00 21.49 ? 17  HIS B N   1 
ATOM   95   C  CA  . HIS A 1 17  ? 8.510   4.416   10.767  1.00 24.27 ? 17  HIS B CA  1 
ATOM   96   C  C   . HIS A 1 17  ? 7.915   4.358   12.105  1.00 27.56 ? 17  HIS B C   1 
ATOM   97   O  O   . HIS A 1 17  ? 8.334   5.094   12.981  1.00 24.13 ? 17  HIS B O   1 
ATOM   98   C  CB  . HIS A 1 17  ? 8.158   5.765   10.149  1.00 24.94 ? 17  HIS B CB  1 
ATOM   99   C  CG  . HIS A 1 17  ? 8.840   6.026   8.818   1.00 28.98 ? 17  HIS B CG  1 
ATOM   100  N  ND1 . HIS A 1 17  ? 10.203  6.142   8.699   1.00 33.31 ? 17  HIS B ND1 1 
ATOM   101  C  CD2 . HIS A 1 17  ? 8.335   6.093   7.550   1.00 31.66 ? 17  HIS B CD2 1 
ATOM   102  C  CE1 . HIS A 1 17  ? 10.528  6.310   7.380   1.00 33.70 ? 17  HIS B CE1 1 
ATOM   103  N  NE2 . HIS A 1 17  ? 9.396   6.332   6.681   1.00 33.60 ? 17  HIS B NE2 1 
ATOM   104  N  N   . TRP A 1 18  ? 6.955   3.461   12.369  1.00 21.87 ? 18  TRP B N   1 
ATOM   105  C  CA  . TRP A 1 18  ? 6.335   3.474   13.669  1.00 20.08 ? 18  TRP B CA  1 
ATOM   106  C  C   . TRP A 1 18  ? 7.298   3.283   14.817  1.00 21.00 ? 18  TRP B C   1 
ATOM   107  O  O   . TRP A 1 18  ? 7.001   3.932   15.860  1.00 25.26 ? 18  TRP B O   1 
ATOM   108  C  CB  . TRP A 1 18  ? 5.161   2.411   13.706  1.00 17.35 ? 18  TRP B CB  1 
ATOM   109  C  CG  . TRP A 1 18  ? 4.044   2.678   12.701  1.00 18.79 ? 18  TRP B CG  1 
ATOM   110  C  CD1 . TRP A 1 18  ? 3.768   3.780   11.928  1.00 18.88 ? 18  TRP B CD1 1 
ATOM   111  C  CD2 . TRP A 1 18  ? 2.954   1.728   12.433  1.00 15.10 ? 18  TRP B CD2 1 
ATOM   112  N  NE1 . TRP A 1 18  ? 2.595   3.631   11.190  1.00 19.25 ? 18  TRP B NE1 1 
ATOM   113  C  CE2 . TRP A 1 18  ? 2.076   2.342   11.455  1.00 14.52 ? 18  TRP B CE2 1 
ATOM   114  C  CE3 . TRP A 1 18  ? 2.675   0.443   12.906  1.00 14.13 ? 18  TRP B CE3 1 
ATOM   115  C  CZ2 . TRP A 1 18  ? 0.958   1.707   10.952  1.00 16.26 ? 18  TRP B CZ2 1 
ATOM   116  C  CZ3 . TRP A 1 18  ? 1.563   -0.206  12.362  1.00 14.55 ? 18  TRP B CZ3 1 
ATOM   117  C  CH2 . TRP A 1 18  ? 0.709   0.416   11.467  1.00 14.78 ? 18  TRP B CH2 1 
ATOM   118  N  N   . LYS A 1 19  ? 8.334   2.463   14.648  1.00 22.56 ? 19  LYS B N   1 
ATOM   119  C  CA  . LYS A 1 19  ? 9.416   2.143   15.670  1.00 23.68 ? 19  LYS B CA  1 
ATOM   120  C  C   . LYS A 1 19  ? 10.099  3.393   16.171  1.00 34.82 ? 19  LYS B C   1 
ATOM   121  O  O   . LYS A 1 19  ? 10.625  3.393   17.296  1.00 30.10 ? 19  LYS B O   1 
ATOM   122  C  CB  . LYS A 1 19  ? 10.506  1.145   15.223  1.00 26.80 ? 19  LYS B CB  1 
ATOM   123  C  CG  . LYS A 1 19  ? 11.445  1.680   14.129  1.00 29.59 ? 19  LYS B CG  1 
ATOM   124  C  CD  . LYS A 1 19  ? 12.828  1.068   14.239  1.00 39.12 ? 19  LYS B CD  1 
ATOM   125  C  CE  . LYS A 1 19  ? 12.964  -0.250  13.505  1.00 43.35 ? 19  LYS B CE  1 
ATOM   126  N  NZ  . LYS A 1 19  ? 14.302  -0.852  13.830  1.00 50.89 ? 19  LYS B NZ  1 
ATOM   127  N  N   . GLU A 1 20  ? 10.145  4.414   15.321  1.00 29.21 ? 20  GLU B N   1 
ATOM   128  C  CA  . GLU A 1 20  ? 10.787  5.696   15.683  1.00 34.09 ? 20  GLU B CA  1 
ATOM   129  C  C   . GLU A 1 20  ? 10.017  6.408   16.826  1.00 37.12 ? 20  GLU B C   1 
ATOM   130  O  O   . GLU A 1 20  ? 10.668  7.048   17.710  1.00 31.69 ? 20  GLU B O   1 
ATOM   131  C  CB  . GLU A 1 20  ? 10.841  6.605   14.448  1.00 32.07 ? 20  GLU B CB  1 
ATOM   132  C  CG  . GLU A 1 20  ? 11.799  6.178   13.334  1.00 31.04 ? 20  GLU B CG  1 
ATOM   133  C  CD  . GLU A 1 20  ? 11.366  6.765   11.961  1.00 32.83 ? 20  GLU B CD  1 
ATOM   134  O  OE1 . GLU A 1 20  ? 10.621  7.760   11.968  1.00 33.82 ? 20  GLU B OE1 1 
ATOM   135  O  OE2 . GLU A 1 20  ? 11.762  6.183   10.922  1.00 38.24 ? 20  GLU B OE2 1 
ATOM   136  N  N   A PHE A 1 21  ? 8.685   6.251   16.815  0.50 37.65 ? 21  PHE B N   1 
ATOM   137  N  N   B PHE A 1 21  ? 8.677   6.322   16.790  0.50 36.66 ? 21  PHE B N   1 
ATOM   138  C  CA  A PHE A 1 21  ? 7.737   6.939   17.725  0.50 37.17 ? 21  PHE B CA  1 
ATOM   139  C  CA  B PHE A 1 21  ? 7.697   6.954   17.729  0.50 35.18 ? 21  PHE B CA  1 
ATOM   140  C  C   A PHE A 1 21  ? 6.827   6.056   18.644  0.50 36.44 ? 21  PHE B C   1 
ATOM   141  C  C   B PHE A 1 21  ? 7.254   5.953   18.854  0.50 33.32 ? 21  PHE B C   1 
ATOM   142  O  O   A PHE A 1 21  ? 6.019   6.603   19.443  0.50 28.69 ? 21  PHE B O   1 
ATOM   143  O  O   B PHE A 1 21  ? 7.161   6.282   20.026  0.50 24.05 ? 21  PHE B O   1 
ATOM   144  C  CB  A PHE A 1 21  ? 6.859   7.877   16.918  0.50 40.94 ? 21  PHE B CB  1 
ATOM   145  C  CB  B PHE A 1 21  ? 6.463   7.332   16.894  0.50 37.75 ? 21  PHE B CB  1 
ATOM   146  C  CG  A PHE A 1 21  ? 7.600   9.041   16.320  0.50 44.23 ? 21  PHE B CG  1 
ATOM   147  C  CG  B PHE A 1 21  ? 5.638   8.523   17.399  0.50 45.02 ? 21  PHE B CG  1 
ATOM   148  C  CD1 A PHE A 1 21  ? 7.692   10.243  17.002  0.50 47.14 ? 21  PHE B CD1 1 
ATOM   149  C  CD1 B PHE A 1 21  ? 5.273   9.538   16.506  0.50 41.15 ? 21  PHE B CD1 1 
ATOM   150  C  CD2 A PHE A 1 21  ? 8.181   8.941   15.064  0.50 46.79 ? 21  PHE B CD2 1 
ATOM   151  C  CD2 B PHE A 1 21  ? 5.154   8.599   18.709  0.50 46.40 ? 21  PHE B CD2 1 
ATOM   152  C  CE1 A PHE A 1 21  ? 8.370   11.322  16.453  0.50 49.00 ? 21  PHE B CE1 1 
ATOM   153  C  CE1 B PHE A 1 21  ? 4.492   10.615  16.915  0.50 45.43 ? 21  PHE B CE1 1 
ATOM   154  C  CE2 A PHE A 1 21  ? 8.855   10.013  14.510  0.50 46.90 ? 21  PHE B CE2 1 
ATOM   155  C  CE2 B PHE A 1 21  ? 4.370   9.680   19.122  0.50 47.49 ? 21  PHE B CE2 1 
ATOM   156  C  CZ  A PHE A 1 21  ? 8.953   11.205  15.206  0.50 46.96 ? 21  PHE B CZ  1 
ATOM   157  C  CZ  B PHE A 1 21  ? 4.046   10.691  18.222  0.50 48.13 ? 21  PHE B CZ  1 
ATOM   158  N  N   . PHE A 1 22  ? 6.941   4.725   18.476  1.00 30.94 ? 22  PHE B N   1 
ATOM   159  C  CA  . PHE A 1 22  ? 6.490   3.705   19.456  1.00 30.12 ? 22  PHE B CA  1 
ATOM   160  C  C   . PHE A 1 22  ? 7.470   2.581   19.428  1.00 28.87 ? 22  PHE B C   1 
ATOM   161  O  O   . PHE A 1 22  ? 7.325   1.647   18.638  1.00 27.84 ? 22  PHE B O   1 
ATOM   162  C  CB  . PHE A 1 22  ? 5.117   3.146   19.056  1.00 31.87 ? 22  PHE B CB  1 
ATOM   163  C  CG  . PHE A 1 22  ? 4.140   4.182   18.801  1.00 27.19 ? 22  PHE B CG  1 
ATOM   164  C  CD1 . PHE A 1 22  ? 3.178   4.535   19.753  1.00 26.47 ? 22  PHE B CD1 1 
ATOM   165  C  CD2 . PHE A 1 22  ? 4.130   4.859   17.557  1.00 30.85 ? 22  PHE B CD2 1 
ATOM   166  C  CE1 . PHE A 1 22  ? 2.256   5.547   19.487  1.00 29.53 ? 22  PHE B CE1 1 
ATOM   167  C  CE2 . PHE A 1 22  ? 3.219   5.883   17.304  1.00 31.85 ? 22  PHE B CE2 1 
ATOM   168  C  CZ  . PHE A 1 22  ? 2.266   6.232   18.280  1.00 34.06 ? 22  PHE B CZ  1 
ATOM   169  N  N   . PRO A 1 23  ? 8.491   2.597   20.311  1.00 25.09 ? 23  PRO B N   1 
ATOM   170  C  CA  . PRO A 1 23  ? 9.554   1.658   20.303  1.00 25.52 ? 23  PRO B CA  1 
ATOM   171  C  C   . PRO A 1 23  ? 9.153   0.239   20.548  1.00 23.29 ? 23  PRO B C   1 
ATOM   172  O  O   . PRO A 1 23  ? 9.901   -0.715  20.204  1.00 23.55 ? 23  PRO B O   1 
ATOM   173  C  CB  . PRO A 1 23  ? 10.500  2.205   21.397  1.00 25.72 ? 23  PRO B CB  1 
ATOM   174  C  CG  . PRO A 1 23  ? 10.204  3.609   21.315  1.00 29.15 ? 23  PRO B CG  1 
ATOM   175  C  CD  . PRO A 1 23  ? 8.757   3.691   21.271  1.00 30.40 ? 23  PRO B CD  1 
ATOM   176  N  N   . ILE A 1 24  ? 7.942   0.074   21.185  1.00 22.47 ? 24  ILE B N   1 
ATOM   177  C  CA  . ILE A 1 24  ? 7.454   -1.287  21.348  1.00 21.98 ? 24  ILE B CA  1 
ATOM   178  C  C   . ILE A 1 24  ? 7.105   -1.877  19.942  1.00 19.35 ? 24  ILE B C   1 
ATOM   179  O  O   . ILE A 1 24  ? 7.047   -3.047  19.850  1.00 19.95 ? 24  ILE B O   1 
ATOM   180  C  CB  . ILE A 1 24  ? 6.166   -1.329  22.249  1.00 20.50 ? 24  ILE B CB  1 
ATOM   181  C  CG1 . ILE A 1 24  ? 6.005   -2.735  22.759  1.00 20.44 ? 24  ILE B CG1 1 
ATOM   182  C  CG2 . ILE A 1 24  ? 4.909   -0.901  21.453  1.00 19.93 ? 24  ILE B CG2 1 
ATOM   183  C  CD1 . ILE A 1 24  ? 7.204   -3.238  23.548  1.00 22.39 ? 24  ILE B CD1 1 
ATOM   184  N  N   . ALA A 1 25  ? 7.144   -1.047  18.874  1.00 21.15 ? 25  ALA B N   1 
ATOM   185  C  CA  . ALA A 1 25  ? 7.054   -1.627  17.532  1.00 21.17 ? 25  ALA B CA  1 
ATOM   186  C  C   . ALA A 1 25  ? 8.078   -2.676  17.339  1.00 17.62 ? 25  ALA B C   1 
ATOM   187  O  O   . ALA A 1 25  ? 7.952   -3.552  16.511  1.00 18.72 ? 25  ALA B O   1 
ATOM   188  C  CB  . ALA A 1 25  ? 7.218   -0.561  16.478  1.00 18.52 ? 25  ALA B CB  1 
ATOM   189  N  N   . ASP A 1 26  ? 9.234   -2.536  17.998  1.00 20.91 ? 26  ASP B N   1 
ATOM   190  C  CA  . ASP A 1 26  ? 10.279  -3.500  17.977  1.00 22.12 ? 26  ASP B CA  1 
ATOM   191  C  C   . ASP A 1 26  ? 10.356  -4.498  19.128  1.00 22.91 ? 26  ASP B C   1 
ATOM   192  O  O   . ASP A 1 26  ? 11.367  -5.144  19.352  1.00 23.33 ? 26  ASP B O   1 
ATOM   193  C  CB  . ASP A 1 26  ? 11.688  -2.814  17.860  1.00 27.39 ? 26  ASP B CB  1 
ATOM   194  C  CG  . ASP A 1 26  ? 11.920  -2.179  16.500  1.00 34.44 ? 26  ASP B CG  1 
ATOM   195  O  OD1 . ASP A 1 26  ? 11.636  -2.816  15.435  1.00 35.13 ? 26  ASP B OD1 1 
ATOM   196  O  OD2 . ASP A 1 26  ? 12.352  -1.018  16.533  1.00 35.94 ? 26  ASP B OD2 1 
ATOM   197  N  N   . GLY A 1 27  ? 9.208   -4.664  19.773  1.00 22.76 ? 27  GLY B N   1 
ATOM   198  C  CA  . GLY A 1 27  ? 9.042   -5.584  20.878  1.00 19.74 ? 27  GLY B CA  1 
ATOM   199  C  C   . GLY A 1 27  ? 9.141   -7.075  20.544  1.00 19.34 ? 27  GLY B C   1 
ATOM   200  O  O   . GLY A 1 27  ? 9.205   -7.478  19.365  1.00 21.39 ? 27  GLY B O   1 
ATOM   201  N  N   . ASP A 1 28  ? 9.027   -7.905  21.582  1.00 21.48 ? 28  ASP B N   1 
ATOM   202  C  CA  . ASP A 1 28  ? 9.180   -9.278  21.498  1.00 21.32 ? 28  ASP B CA  1 
ATOM   203  C  C   . ASP A 1 28  ? 7.841   -10.031 21.157  1.00 16.59 ? 28  ASP B C   1 
ATOM   204  O  O   . ASP A 1 28  ? 7.876   -11.211 20.818  1.00 20.21 ? 28  ASP B O   1 
ATOM   205  C  CB  . ASP A 1 28  ? 9.548   -9.809  22.915  1.00 27.38 ? 28  ASP B CB  1 
ATOM   206  C  CG  . ASP A 1 28  ? 11.064  -9.706  23.223  1.00 36.40 ? 28  ASP B CG  1 
ATOM   207  O  OD1 . ASP A 1 28  ? 11.837  -9.374  22.315  1.00 37.27 ? 28  ASP B OD1 1 
ATOM   208  O  OD2 . ASP A 1 28  ? 11.423  -10.031 24.372  1.00 42.26 ? 28  ASP B OD2 1 
ATOM   209  N  N   . GLN A 1 29  ? 6.726   -9.278  21.272  1.00 16.16 ? 29  GLN B N   1 
ATOM   210  C  CA  . GLN A 1 29  ? 5.418   -9.961  21.033  1.00 14.73 ? 29  GLN B CA  1 
ATOM   211  C  C   . GLN A 1 29  ? 4.510   -9.160  20.091  1.00 14.10 ? 29  GLN B C   1 
ATOM   212  O  O   . GLN A 1 29  ? 3.376   -8.757  20.415  1.00 13.63 ? 29  GLN B O   1 
ATOM   213  C  CB  . GLN A 1 29  ? 4.685   -10.314 22.311  1.00 15.45 ? 29  GLN B CB  1 
ATOM   214  C  CG  . GLN A 1 29  ? 5.553   -11.281 23.162  1.00 19.78 ? 29  GLN B CG  1 
ATOM   215  C  CD  . GLN A 1 29  ? 4.774   -12.100 24.163  1.00 24.75 ? 29  GLN B CD  1 
ATOM   216  O  OE1 . GLN A 1 29  ? 3.657   -11.786 24.497  1.00 20.38 ? 29  GLN B OE1 1 
ATOM   217  N  NE2 . GLN A 1 29  ? 5.406   -13.157 24.669  1.00 22.97 ? 29  GLN B NE2 1 
ATOM   218  N  N   . GLN A 1 30  ? 5.123   -8.752  18.955  1.00 14.43 ? 30  GLN B N   1 
ATOM   219  C  CA  . GLN A 1 30  ? 4.424   -7.946  17.934  1.00 13.68 ? 30  GLN B CA  1 
ATOM   220  C  C   . GLN A 1 30  ? 3.652   -8.788  16.884  1.00 10.46 ? 30  GLN B C   1 
ATOM   221  O  O   . GLN A 1 30  ? 3.966   -9.900  16.631  1.00 12.89 ? 30  GLN B O   1 
ATOM   222  C  CB  . GLN A 1 30  ? 5.438   -7.016  17.251  1.00 14.27 ? 30  GLN B CB  1 
ATOM   223  C  CG  . GLN A 1 30  ? 5.967   -5.923  18.253  1.00 14.58 ? 30  GLN B CG  1 
ATOM   224  C  CD  . GLN A 1 30  ? 4.921   -4.953  18.517  1.00 13.31 ? 30  GLN B CD  1 
ATOM   225  O  OE1 . GLN A 1 30  ? 4.495   -4.188  17.697  1.00 14.06 ? 30  GLN B OE1 1 
ATOM   226  N  NE2 . GLN A 1 30  ? 4.458   -4.852  19.856  1.00 12.70 ? 30  GLN B NE2 1 
ATOM   227  N  N   . SER A 1 31  ? 2.576   -8.109  16.435  1.00 11.12 ? 31  SER B N   1 
ATOM   228  C  CA  . SER A 1 31  ? 1.701   -8.712  15.429  1.00 10.15 ? 31  SER B CA  1 
ATOM   229  C  C   . SER A 1 31  ? 1.609   -7.785  14.213  1.00 10.75 ? 31  SER B C   1 
ATOM   230  O  O   . SER A 1 31  ? 1.801   -6.576  14.312  1.00 10.78 ? 31  SER B O   1 
ATOM   231  C  CB  . SER A 1 31  ? 0.283   -8.831  16.059  1.00 11.32 ? 31  SER B CB  1 
ATOM   232  O  OG  . SER A 1 31  ? 0.382   -9.799  17.135  1.00 10.58 ? 31  SER B OG  1 
ATOM   233  N  N   . PRO A 1 32  ? 1.186   -8.339  13.057  1.00 10.29 ? 32  PRO B N   1 
ATOM   234  C  CA  . PRO A 1 32  ? 0.864   -9.717  12.755  1.00 10.55 ? 32  PRO B CA  1 
ATOM   235  C  C   . PRO A 1 32  ? 2.095   -10.563 12.534  1.00 9.77  ? 32  PRO B C   1 
ATOM   236  O  O   . PRO A 1 32  ? 3.247   -10.026 12.679  1.00 10.96 ? 32  PRO B O   1 
ATOM   237  C  CB  . PRO A 1 32  ? -0.003  -9.560  11.447  1.00 9.58  ? 32  PRO B CB  1 
ATOM   238  C  CG  . PRO A 1 32  ? 0.768   -8.433  10.713  1.00 10.32 ? 32  PRO B CG  1 
ATOM   239  C  CD  . PRO A 1 32  ? 1.116   -7.416  11.843  1.00 10.54 ? 32  PRO B CD  1 
ATOM   240  N  N   . ILE A 1 33  ? 1.859   -11.772 12.155  1.00 10.30 ? 33  ILE B N   1 
ATOM   241  C  CA  . ILE A 1 33  ? 2.996   -12.717 11.948  1.00 11.47 ? 33  ILE B CA  1 
ATOM   242  C  C   . ILE A 1 33  ? 2.709   -13.518 10.704  1.00 11.81 ? 33  ILE B C   1 
ATOM   243  O  O   . ILE A 1 33  ? 1.569   -13.649 10.190  1.00 11.57 ? 33  ILE B O   1 
ATOM   244  C  CB  . ILE A 1 33  ? 3.205   -13.684 13.171  1.00 11.77 ? 33  ILE B CB  1 
ATOM   245  C  CG1 . ILE A 1 33  ? 1.939   -14.536 13.418  1.00 13.37 ? 33  ILE B CG1 1 
ATOM   246  C  CG2 . ILE A 1 33  ? 3.668   -12.909 14.424  1.00 12.27 ? 33  ILE B CG2 1 
ATOM   247  C  CD1 . ILE A 1 33  ? 2.236   -15.703 14.388  1.00 12.70 ? 33  ILE B CD1 1 
ATOM   248  N  N   . GLU A 1 34  ? 3.766   -14.192 10.233  1.00 12.15 ? 34  GLU B N   1 
ATOM   249  C  CA  . GLU A 1 34  ? 3.664   -15.331 9.315   1.00 13.02 ? 34  GLU B CA  1 
ATOM   250  C  C   . GLU A 1 34  ? 3.203   -16.557 10.061  1.00 12.78 ? 34  GLU B C   1 
ATOM   251  O  O   . GLU A 1 34  ? 3.858   -16.946 11.059  1.00 14.22 ? 34  GLU B O   1 
ATOM   252  C  CB  . GLU A 1 34  ? 5.042   -15.684 8.713   1.00 17.02 ? 34  GLU B CB  1 
ATOM   253  C  CG  . GLU A 1 34  ? 5.847   -14.556 8.080   1.00 23.26 ? 34  GLU B CG  1 
ATOM   254  C  CD  . GLU A 1 34  ? 5.300   -14.131 6.747   1.00 20.43 ? 34  GLU B CD  1 
ATOM   255  O  OE1 . GLU A 1 34  ? 4.562   -14.908 6.017   1.00 18.15 ? 34  GLU B OE1 1 
ATOM   256  O  OE2 . GLU A 1 34  ? 5.745   -12.967 6.334   1.00 25.72 ? 34  GLU B OE2 1 
ATOM   257  N  N   . ILE A 1 35  ? 2.139   -17.203 9.611   1.00 13.20 ? 35  ILE B N   1 
ATOM   258  C  CA  . ILE A 1 35  ? 1.729   -18.457 10.149  1.00 13.72 ? 35  ILE B CA  1 
ATOM   259  C  C   . ILE A 1 35  ? 2.187   -19.589 9.212   1.00 14.66 ? 35  ILE B C   1 
ATOM   260  O  O   . ILE A 1 35  ? 1.832   -19.637 8.084   1.00 14.49 ? 35  ILE B O   1 
ATOM   261  C  CB  . ILE A 1 35  ? 0.173   -18.479 10.222  1.00 13.95 ? 35  ILE B CB  1 
ATOM   262  C  CG1 . ILE A 1 35  ? -0.249  -17.397 11.261  1.00 15.35 ? 35  ILE B CG1 1 
ATOM   263  C  CG2 . ILE A 1 35  ? -0.348  -19.823 10.744  1.00 16.65 ? 35  ILE B CG2 1 
ATOM   264  C  CD1 . ILE A 1 35  ? -1.792  -17.167 11.256  1.00 16.75 ? 35  ILE B CD1 1 
ATOM   265  N  N   . LYS A 1 36  ? 3.106   -20.389 9.721   1.00 14.79 ? 36  LYS B N   1 
ATOM   266  C  CA  . LYS A 1 36  ? 3.699   -21.522 8.994   1.00 14.58 ? 36  LYS B CA  1 
ATOM   267  C  C   . LYS A 1 36  ? 3.068   -22.781 9.491   1.00 14.13 ? 36  LYS B C   1 
ATOM   268  O  O   . LYS A 1 36  ? 3.412   -23.208 10.628  1.00 17.52 ? 36  LYS B O   1 
ATOM   269  C  CB  . LYS A 1 36  ? 5.276   -21.541 9.238   1.00 14.15 ? 36  LYS B CB  1 
ATOM   270  C  CG  . LYS A 1 36  ? 6.036   -20.320 8.666   1.00 16.24 ? 36  LYS B CG  1 
ATOM   271  C  CD  . LYS A 1 36  ? 7.509   -20.470 8.953   1.00 17.62 ? 36  LYS B CD  1 
ATOM   272  C  CE  . LYS A 1 36  ? 8.302   -19.364 8.441   1.00 19.04 ? 36  LYS B CE  1 
ATOM   273  N  NZ  . LYS A 1 36  ? 9.719   -19.495 8.866   1.00 21.36 ? 36  LYS B NZ  1 
ATOM   274  N  N   . THR A 1 37  ? 2.166   -23.296 8.707   1.00 17.96 ? 37  THR B N   1 
ATOM   275  C  CA  . THR A 1 37  ? 1.345   -24.424 9.257   1.00 20.63 ? 37  THR B CA  1 
ATOM   276  C  C   . THR A 1 37  ? 2.127   -25.677 9.745   1.00 24.36 ? 37  THR B C   1 
ATOM   277  O  O   . THR A 1 37  ? 1.671   -26.368 10.654  1.00 27.73 ? 37  THR B O   1 
ATOM   278  C  CB  . THR A 1 37  ? 0.258   -24.797 8.320   1.00 23.14 ? 37  THR B CB  1 
ATOM   279  O  OG1 . THR A 1 37  ? 0.835   -25.229 7.069   1.00 25.12 ? 37  THR B OG1 1 
ATOM   280  C  CG2 . THR A 1 37  ? -0.690  -23.635 8.126   1.00 21.69 ? 37  THR B CG2 1 
ATOM   281  N  N   . LYS A 1 38  ? 3.289   -26.006 9.170   1.00 22.64 ? 38  LYS B N   1 
ATOM   282  C  CA  . LYS A 1 38  ? 4.144   -27.087 9.651   1.00 23.33 ? 38  LYS B CA  1 
ATOM   283  C  C   . LYS A 1 38  ? 4.835   -26.807 10.953  1.00 23.52 ? 38  LYS B C   1 
ATOM   284  O  O   . LYS A 1 38  ? 5.321   -27.780 11.597  1.00 24.99 ? 38  LYS B O   1 
ATOM   285  C  CB  . LYS A 1 38  ? 5.183   -27.493 8.560   1.00 24.14 ? 38  LYS B CB  1 
ATOM   286  C  CG  . LYS A 1 38  ? 4.466   -28.195 7.413   1.00 34.01 ? 38  LYS B CG  1 
ATOM   287  C  CD  . LYS A 1 38  ? 4.122   -29.658 7.720   1.00 38.72 ? 38  LYS B CD  1 
ATOM   288  C  CE  . LYS A 1 38  ? 3.577   -30.363 6.477   1.00 49.78 ? 38  LYS B CE  1 
ATOM   289  N  NZ  . LYS A 1 38  ? 2.540   -31.422 6.761   1.00 50.68 ? 38  LYS B NZ  1 
ATOM   290  N  N   . GLU A 1 39  ? 4.923   -25.541 11.399  1.00 18.14 ? 39  GLU B N   1 
ATOM   291  C  CA  . GLU A 1 39  ? 5.577   -25.169 12.629  1.00 20.26 ? 39  GLU B CA  1 
ATOM   292  C  C   . GLU A 1 39  ? 4.605   -25.003 13.784  1.00 19.16 ? 39  GLU B C   1 
ATOM   293  O  O   . GLU A 1 39  ? 5.001   -24.820 14.947  1.00 21.47 ? 39  GLU B O   1 
ATOM   294  C  CB  . GLU A 1 39  ? 6.423   -23.865 12.488  1.00 21.97 ? 39  GLU B CB  1 
ATOM   295  C  CG  . GLU A 1 39  ? 7.469   -23.898 11.343  1.00 26.28 ? 39  GLU B CG  1 
ATOM   296  C  CD  . GLU A 1 39  ? 8.282   -25.104 11.395  1.00 33.50 ? 39  GLU B CD  1 
ATOM   297  O  OE1 . GLU A 1 39  ? 8.839   -25.366 12.482  1.00 37.10 ? 39  GLU B OE1 1 
ATOM   298  O  OE2 . GLU A 1 39  ? 8.280   -25.807 10.381  1.00 30.72 ? 39  GLU B OE2 1 
ATOM   299  N  N   . VAL A 1 40  ? 3.305   -24.933 13.434  1.00 18.29 ? 40  VAL B N   1 
ATOM   300  C  CA  . VAL A 1 40  ? 2.366   -24.724 14.499  1.00 18.33 ? 40  VAL B CA  1 
ATOM   301  C  C   . VAL A 1 40  ? 2.188   -25.968 15.327  1.00 21.33 ? 40  VAL B C   1 
ATOM   302  O  O   . VAL A 1 40  ? 2.364   -27.111 14.807  1.00 22.66 ? 40  VAL B O   1 
ATOM   303  C  CB  . VAL A 1 40  ? 1.009   -24.161 13.982  1.00 20.09 ? 40  VAL B CB  1 
ATOM   304  C  CG1 . VAL A 1 40  ? 1.159   -22.856 13.187  1.00 19.39 ? 40  VAL B CG1 1 
ATOM   305  C  CG2 . VAL A 1 40  ? 0.180   -25.201 13.310  1.00 24.60 ? 40  VAL B CG2 1 
ATOM   306  N  N   . LYS A 1 41  ? 1.955   -25.782 16.603  1.00 20.14 ? 41  LYS B N   1 
ATOM   307  C  CA  . LYS A 1 41  ? 1.757   -26.928 17.441  1.00 19.65 ? 41  LYS B CA  1 
ATOM   308  C  C   . LYS A 1 41  ? 0.256   -27.219 17.687  1.00 20.24 ? 41  LYS B C   1 
ATOM   309  O  O   . LYS A 1 41  ? -0.402  -26.349 18.274  1.00 16.56 ? 41  LYS B O   1 
ATOM   310  C  CB  . LYS A 1 41  ? 2.454   -26.595 18.768  1.00 22.64 ? 41  LYS B CB  1 
ATOM   311  C  CG  . LYS A 1 41  ? 3.976   -26.734 18.583  1.00 32.82 ? 41  LYS B CG  1 
ATOM   312  C  CD  . LYS A 1 41  ? 4.789   -25.963 19.616  1.00 38.98 ? 41  LYS B CD  1 
ATOM   313  C  CE  . LYS A 1 41  ? 6.268   -26.337 19.539  1.00 45.18 ? 41  LYS B CE  1 
ATOM   314  N  NZ  . LYS A 1 41  ? 7.078   -25.257 20.151  1.00 44.45 ? 41  LYS B NZ  1 
ATOM   315  N  N   . TYR A 1 42  ? -0.245  -28.407 17.374  1.00 18.54 ? 42  TYR B N   1 
ATOM   316  C  CA  . TYR A 1 42  ? -1.591  -28.752 17.755  1.00 19.12 ? 42  TYR B CA  1 
ATOM   317  C  C   . TYR A 1 42  ? -1.653  -28.828 19.268  1.00 19.50 ? 42  TYR B C   1 
ATOM   318  O  O   . TYR A 1 42  ? -0.757  -29.407 19.891  1.00 19.53 ? 42  TYR B O   1 
ATOM   319  C  CB  . TYR A 1 42  ? -2.013  -30.103 17.204  1.00 20.85 ? 42  TYR B CB  1 
ATOM   320  C  CG  . TYR A 1 42  ? -3.282  -30.568 17.786  1.00 20.63 ? 42  TYR B CG  1 
ATOM   321  C  CD1 . TYR A 1 42  ? -4.482  -29.923 17.487  1.00 20.41 ? 42  TYR B CD1 1 
ATOM   322  C  CD2 . TYR A 1 42  ? -3.347  -31.758 18.563  1.00 22.84 ? 42  TYR B CD2 1 
ATOM   323  C  CE1 . TYR A 1 42  ? -5.688  -30.358 18.071  1.00 22.08 ? 42  TYR B CE1 1 
ATOM   324  C  CE2 . TYR A 1 42  ? -4.535  -32.245 19.092  1.00 22.26 ? 42  TYR B CE2 1 
ATOM   325  C  CZ  . TYR A 1 42  ? -5.741  -31.564 18.828  1.00 24.87 ? 42  TYR B CZ  1 
ATOM   326  O  OH  . TYR A 1 42  ? -6.952  -31.957 19.299  1.00 27.66 ? 42  TYR B OH  1 
ATOM   327  N  N   . ASP A 1 43  ? -2.676  -28.299 19.912  1.00 15.29 ? 43  ASP B N   1 
ATOM   328  C  CA  . ASP A 1 43  ? -2.772  -28.307 21.317  1.00 16.18 ? 43  ASP B CA  1 
ATOM   329  C  C   . ASP A 1 43  ? -4.142  -28.801 21.738  1.00 17.76 ? 43  ASP B C   1 
ATOM   330  O  O   . ASP A 1 43  ? -5.163  -28.084 21.513  1.00 17.06 ? 43  ASP B O   1 
ATOM   331  C  CB  . ASP A 1 43  ? -2.496  -26.937 21.917  1.00 16.65 ? 43  ASP B CB  1 
ATOM   332  C  CG  . ASP A 1 43  ? -2.495  -26.922 23.424  1.00 18.14 ? 43  ASP B CG  1 
ATOM   333  O  OD1 . ASP A 1 43  ? -3.065  -27.886 24.059  1.00 19.09 ? 43  ASP B OD1 1 
ATOM   334  O  OD2 . ASP A 1 43  ? -1.938  -26.005 24.043  1.00 19.87 ? 43  ASP B OD2 1 
ATOM   335  N  N   . SER A 1 44  ? -4.226  -30.003 22.359  1.00 19.52 ? 44  SER B N   1 
ATOM   336  C  CA  . SER A 1 44  ? -5.526  -30.579 22.697  1.00 20.60 ? 44  SER B CA  1 
ATOM   337  C  C   . SER A 1 44  ? -6.162  -29.871 23.893  1.00 20.35 ? 44  SER B C   1 
ATOM   338  O  O   . SER A 1 44  ? -7.379  -30.061 24.106  1.00 22.95 ? 44  SER B O   1 
ATOM   339  C  CB  . SER A 1 44  ? -5.438  -32.137 22.861  1.00 21.36 ? 44  SER B CB  1 
ATOM   340  O  OG  . SER A 1 44  ? -4.584  -32.347 23.915  1.00 26.56 ? 44  SER B OG  1 
ATOM   341  N  N   . SER A 1 45  ? -5.515  -28.982 24.604  1.00 18.32 ? 45  SER B N   1 
ATOM   342  C  CA  . SER A 1 45  ? -6.138  -28.256 25.676  1.00 19.07 ? 45  SER B CA  1 
ATOM   343  C  C   . SER A 1 45  ? -6.964  -27.020 25.131  1.00 17.16 ? 45  SER B C   1 
ATOM   344  O  O   . SER A 1 45  ? -7.726  -26.430 25.913  1.00 19.95 ? 45  SER B O   1 
ATOM   345  C  CB  . SER A 1 45  ? -5.138  -27.863 26.726  1.00 20.12 ? 45  SER B CB  1 
ATOM   346  O  OG  . SER A 1 45  ? -4.204  -26.831 26.208  1.00 22.52 ? 45  SER B OG  1 
ATOM   347  N  N   . LEU A 1 46  ? -6.721  -26.622 23.880  1.00 16.37 ? 46  LEU B N   1 
ATOM   348  C  CA  . LEU A 1 46  ? -7.480  -25.483 23.335  1.00 15.79 ? 46  LEU B CA  1 
ATOM   349  C  C   . LEU A 1 46  ? -8.937  -25.929 23.138  1.00 16.68 ? 46  LEU B C   1 
ATOM   350  O  O   . LEU A 1 46  ? -9.228  -27.108 22.769  1.00 20.21 ? 46  LEU B O   1 
ATOM   351  C  CB  . LEU A 1 46  ? -6.916  -25.142 21.948  1.00 15.37 ? 46  LEU B CB  1 
ATOM   352  C  CG  . LEU A 1 46  ? -5.621  -24.363 21.980  1.00 13.17 ? 46  LEU B CG  1 
ATOM   353  C  CD1 . LEU A 1 46  ? -5.061  -24.277 20.510  1.00 14.32 ? 46  LEU B CD1 1 
ATOM   354  C  CD2 . LEU A 1 46  ? -5.817  -23.000 22.660  1.00 14.80 ? 46  LEU B CD2 1 
ATOM   355  N  N   . ARG A 1 47  ? -9.823  -24.992 23.324  1.00 13.74 ? 47  ARG B N   1 
ATOM   356  C  CA  . ARG A 1 47  ? -11.207 -25.301 23.266  1.00 12.36 ? 47  ARG B CA  1 
ATOM   357  C  C   . ARG A 1 47  ? -11.843 -24.731 21.968  1.00 11.34 ? 47  ARG B C   1 
ATOM   358  O  O   . ARG A 1 47  ? -11.302 -23.762 21.393  1.00 13.32 ? 47  ARG B O   1 
ATOM   359  C  CB  . ARG A 1 47  ? -11.889 -24.643 24.443  1.00 12.01 ? 47  ARG B CB  1 
ATOM   360  C  CG  . ARG A 1 47  ? -11.469 -25.364 25.750  1.00 15.39 ? 47  ARG B CG  1 
ATOM   361  C  CD  . ARG A 1 47  ? -12.164 -24.720 26.861  1.00 19.64 ? 47  ARG B CD  1 
ATOM   362  N  NE  . ARG A 1 47  ? -11.895 -25.474 28.114  1.00 22.66 ? 47  ARG B NE  1 
ATOM   363  C  CZ  . ARG A 1 47  ? -12.179 -24.992 29.334  1.00 23.01 ? 47  ARG B CZ  1 
ATOM   364  N  NH1 . ARG A 1 47  ? -12.749 -23.783 29.489  1.00 27.66 ? 47  ARG B NH1 1 
ATOM   365  N  NH2 . ARG A 1 47  ? -11.877 -25.746 30.367  1.00 27.23 ? 47  ARG B NH2 1 
ATOM   366  N  N   . PRO A 1 48  ? -12.918 -25.279 21.517  1.00 11.17 ? 48  PRO B N   1 
ATOM   367  C  CA  . PRO A 1 48  ? -13.685 -24.566 20.428  1.00 11.09 ? 48  PRO B CA  1 
ATOM   368  C  C   . PRO A 1 48  ? -14.049 -23.160 20.870  1.00 11.53 ? 48  PRO B C   1 
ATOM   369  O  O   . PRO A 1 48  ? -14.236 -22.883 22.065  1.00 10.60 ? 48  PRO B O   1 
ATOM   370  C  CB  . PRO A 1 48  ? -14.960 -25.420 20.257  1.00 11.75 ? 48  PRO B CB  1 
ATOM   371  C  CG  . PRO A 1 48  ? -14.531 -26.810 20.802  1.00 11.80 ? 48  PRO B CG  1 
ATOM   372  C  CD  . PRO A 1 48  ? -13.631 -26.472 21.977  1.00 11.66 ? 48  PRO B CD  1 
ATOM   373  N  N   . LEU A 1 49  ? -14.234 -22.258 19.883  1.00 10.81 ? 49  LEU B N   1 
ATOM   374  C  CA  . LEU A 1 49  ? -14.691 -20.897 20.285  1.00 11.19 ? 49  LEU B CA  1 
ATOM   375  C  C   . LEU A 1 49  ? -16.194 -20.944 20.774  1.00 10.79 ? 49  LEU B C   1 
ATOM   376  O  O   . LEU A 1 49  ? -17.015 -21.617 20.127  1.00 11.00 ? 49  LEU B O   1 
ATOM   377  C  CB  . LEU A 1 49  ? -14.547 -20.000 19.054  1.00 12.28 ? 49  LEU B CB  1 
ATOM   378  C  CG  . LEU A 1 49  ? -13.091 -19.850 18.546  1.00 10.86 ? 49  LEU B CG  1 
ATOM   379  C  CD1 . LEU A 1 49  ? -13.119 -18.973 17.304  1.00 13.74 ? 49  LEU B CD1 1 
ATOM   380  C  CD2 . LEU A 1 49  ? -12.278 -19.281 19.729  1.00 13.99 ? 49  LEU B CD2 1 
ATOM   381  N  N   . SER A 1 50  ? -16.465 -20.183 21.819  1.00 10.00 ? 50  SER B N   1 
ATOM   382  C  CA  . SER A 1 50  ? -17.844 -20.003 22.304  1.00 11.30 ? 50  SER B CA  1 
ATOM   383  C  C   . SER A 1 50  ? -18.256 -18.521 21.944  1.00 10.42 ? 50  SER B C   1 
ATOM   384  O  O   . SER A 1 50  ? -17.675 -17.600 22.544  1.00 10.93 ? 50  SER B O   1 
ATOM   385  C  CB  . SER A 1 50  ? -17.856 -20.277 23.807  1.00 11.04 ? 50  SER B CB  1 
ATOM   386  O  OG  . SER A 1 50  ? -19.137 -19.826 24.252  1.00 14.91 ? 50  SER B OG  1 
ATOM   387  N  N   . ILE A 1 51  ? -19.141 -18.377 20.950  1.00 9.36  ? 51  ILE B N   1 
ATOM   388  C  CA  . ILE A 1 51  ? -19.318 -17.032 20.343  1.00 11.22 ? 51  ILE B CA  1 
ATOM   389  C  C   . ILE A 1 51  ? -20.755 -16.592 20.539  1.00 9.92  ? 51  ILE B C   1 
ATOM   390  O  O   . ILE A 1 51  ? -21.656 -17.255 20.108  1.00 10.73 ? 51  ILE B O   1 
ATOM   391  C  CB  . ILE A 1 51  ? -18.919 -17.071 18.884  1.00 10.73 ? 51  ILE B CB  1 
ATOM   392  C  CG1 . ILE A 1 51  ? -17.579 -17.711 18.700  1.00 11.06 ? 51  ILE B CG1 1 
ATOM   393  C  CG2 . ILE A 1 51  ? -18.908 -15.605 18.425  1.00 13.65 ? 51  ILE B CG2 1 
ATOM   394  C  CD1 . ILE A 1 51  ? -17.047 -17.590 17.217  1.00 12.35 ? 51  ILE B CD1 1 
ATOM   395  N  N   . LYS A 1 52  ? -20.976 -15.439 21.141  1.00 10.84 ? 52  LYS B N   1 
ATOM   396  C  CA  . LYS A 1 52  ? -22.291 -14.849 21.249  1.00 10.29 ? 52  LYS B CA  1 
ATOM   397  C  C   . LYS A 1 52  ? -22.248 -13.406 20.839  1.00 10.31 ? 52  LYS B C   1 
ATOM   398  O  O   . LYS A 1 52  ? -21.594 -12.588 21.497  1.00 10.86 ? 52  LYS B O   1 
ATOM   399  C  CB  . LYS A 1 52  ? -22.832 -14.958 22.698  1.00 10.76 ? 52  LYS B CB  1 
ATOM   400  C  CG  . LYS A 1 52  ? -24.201 -14.390 22.801  1.00 13.21 ? 52  LYS B CG  1 
ATOM   401  C  CD  . LYS A 1 52  ? -24.643 -14.382 24.261  1.00 12.76 ? 52  LYS B CD  1 
ATOM   402  C  CE  . LYS A 1 52  ? -26.111 -13.944 24.347  1.00 14.27 ? 52  LYS B CE  1 
ATOM   403  N  NZ  . LYS A 1 52  ? -26.466 -12.601 23.676  1.00 13.60 ? 52  LYS B NZ  1 
ATOM   404  N  N   . TYR A 1 53  ? -22.850 -13.075 19.700  1.00 10.50 ? 53  TYR B N   1 
ATOM   405  C  CA  . TYR A 1 53  ? -22.891 -11.681 19.183  1.00 10.88 ? 53  TYR B CA  1 
ATOM   406  C  C   . TYR A 1 53  ? -24.299 -11.258 18.925  1.00 11.71 ? 53  TYR B C   1 
ATOM   407  O  O   . TYR A 1 53  ? -24.962 -11.858 18.098  1.00 11.51 ? 53  TYR B O   1 
ATOM   408  C  CB  . TYR A 1 53  ? -22.004 -11.552 17.918  1.00 10.84 ? 53  TYR B CB  1 
ATOM   409  C  CG  . TYR A 1 53  ? -20.550 -11.820 18.019  1.00 9.38  ? 53  TYR B CG  1 
ATOM   410  C  CD1 . TYR A 1 53  ? -19.839 -11.482 19.193  1.00 9.94  ? 53  TYR B CD1 1 
ATOM   411  C  CD2 . TYR A 1 53  ? -19.835 -12.417 16.944  1.00 9.24  ? 53  TYR B CD2 1 
ATOM   412  C  CE1 . TYR A 1 53  ? -18.444 -11.687 19.238  1.00 9.28  ? 53  TYR B CE1 1 
ATOM   413  C  CE2 . TYR A 1 53  ? -18.481 -12.576 17.021  1.00 9.36  ? 53  TYR B CE2 1 
ATOM   414  C  CZ  . TYR A 1 53  ? -17.770 -12.235 18.141  1.00 9.17  ? 53  TYR B CZ  1 
ATOM   415  O  OH  . TYR A 1 53  ? -16.437 -12.446 18.191  1.00 10.02 ? 53  TYR B OH  1 
ATOM   416  N  N   . ASP A 1 54  ? -24.747 -10.238 19.654  1.00 11.50 ? 54  ASP B N   1 
ATOM   417  C  CA  . ASP A 1 54  ? -26.143 -9.740  19.547  1.00 13.25 ? 54  ASP B CA  1 
ATOM   418  C  C   . ASP A 1 54  ? -26.152 -8.687  18.391  1.00 13.81 ? 54  ASP B C   1 
ATOM   419  O  O   . ASP A 1 54  ? -25.416 -7.686  18.451  1.00 14.87 ? 54  ASP B O   1 
ATOM   420  C  CB  . ASP A 1 54  ? -26.552 -9.160  20.882  1.00 14.22 ? 54  ASP B CB  1 
ATOM   421  C  CG  . ASP A 1 54  ? -28.002 -8.677  20.939  1.00 18.35 ? 54  ASP B CG  1 
ATOM   422  O  OD1 . ASP A 1 54  ? -28.527 -8.265  19.859  1.00 16.17 ? 54  ASP B OD1 1 
ATOM   423  O  OD2 . ASP A 1 54  ? -28.498 -8.739  22.075  1.00 22.64 ? 54  ASP B OD2 1 
ATOM   424  N  N   . PRO A 1 55  ? -26.855 -8.952  17.278  1.00 14.13 ? 55  PRO B N   1 
ATOM   425  C  CA  . PRO A 1 55  ? -26.935 -7.916  16.176  1.00 14.45 ? 55  PRO B CA  1 
ATOM   426  C  C   . PRO A 1 55  ? -27.339 -6.517  16.647  1.00 15.52 ? 55  PRO B C   1 
ATOM   427  O  O   . PRO A 1 55  ? -26.940 -5.587  15.886  1.00 17.42 ? 55  PRO B O   1 
ATOM   428  C  CB  . PRO A 1 55  ? -27.924 -8.531  15.165  1.00 15.08 ? 55  PRO B CB  1 
ATOM   429  C  CG  . PRO A 1 55  ? -27.946 -10.042 15.597  1.00 16.90 ? 55  PRO B CG  1 
ATOM   430  C  CD  . PRO A 1 55  ? -27.798 -10.054 17.071  1.00 15.37 ? 55  PRO B CD  1 
ATOM   431  N  N   . SER A 1 56  ? -28.021 -6.382  17.742  1.00 14.58 ? 56  SER B N   1 
ATOM   432  C  CA  . SER A 1 56  ? -28.453 -5.046  18.185  1.00 16.97 ? 56  SER B CA  1 
ATOM   433  C  C   . SER A 1 56  ? -27.342 -4.355  18.961  1.00 18.13 ? 56  SER B C   1 
ATOM   434  O  O   . SER A 1 56  ? -27.437 -3.169  19.326  1.00 20.83 ? 56  SER B O   1 
ATOM   435  C  CB  . SER A 1 56  ? -29.725 -5.250  19.061  1.00 20.30 ? 56  SER B CB  1 
ATOM   436  O  OG  . SER A 1 56  ? -29.421 -5.703  20.363  1.00 26.19 ? 56  SER B OG  1 
ATOM   437  N  N   . SER A 1 57  ? -26.188 -5.037  19.257  1.00 14.44 ? 57  SER B N   1 
ATOM   438  C  CA  . SER A 1 57  ? -25.052 -4.495  19.967  1.00 14.38 ? 57  SER B CA  1 
ATOM   439  C  C   . SER A 1 57  ? -24.353 -3.429  19.063  1.00 14.04 ? 57  SER B C   1 
ATOM   440  O  O   . SER A 1 57  ? -23.708 -2.555  19.588  1.00 13.69 ? 57  SER B O   1 
ATOM   441  C  CB  . SER A 1 57  ? -23.982 -5.626  20.264  1.00 15.73 ? 57  SER B CB  1 
ATOM   442  O  OG  . SER A 1 57  ? -24.411 -6.327  21.357  1.00 16.45 ? 57  SER B OG  1 
ATOM   443  N  N   . ALA A 1 58  ? -24.358 -3.644  17.742  1.00 12.87 ? 58  ALA B N   1 
ATOM   444  C  CA  . ALA A 1 58  ? -23.760 -2.686  16.831  1.00 12.31 ? 58  ALA B CA  1 
ATOM   445  C  C   . ALA A 1 58  ? -24.519 -1.342  16.891  1.00 12.29 ? 58  ALA B C   1 
ATOM   446  O  O   . ALA A 1 58  ? -25.712 -1.352  16.813  1.00 15.30 ? 58  ALA B O   1 
ATOM   447  C  CB  . ALA A 1 58  ? -23.720 -3.188  15.356  1.00 13.55 ? 58  ALA B CB  1 
ATOM   448  N  N   . LYS A 1 59  ? -23.726 -0.247  17.020  1.00 11.64 ? 59  LYS B N   1 
ATOM   449  C  CA  . LYS A 1 59  ? -24.458 1.051   17.097  1.00 12.84 ? 59  LYS B CA  1 
ATOM   450  C  C   . LYS A 1 59  ? -24.005 2.119   16.100  1.00 12.31 ? 59  LYS B C   1 
ATOM   451  O  O   . LYS A 1 59  ? -24.899 2.903   15.642  1.00 14.55 ? 59  LYS B O   1 
ATOM   452  C  CB  . LYS A 1 59  ? -24.248 1.615   18.539  1.00 14.44 ? 59  LYS B CB  1 
ATOM   453  C  CG  . LYS A 1 59  ? -24.791 0.751   19.683  1.00 13.89 ? 59  LYS B CG  1 
ATOM   454  C  CD  . LYS A 1 59  ? -26.257 0.511   19.570  1.00 14.55 ? 59  LYS B CD  1 
ATOM   455  C  CE  . LYS A 1 59  ? -26.693 -0.315  20.782  1.00 16.08 ? 59  LYS B CE  1 
ATOM   456  N  NZ  . LYS A 1 59  ? -28.078 -0.703  20.692  1.00 17.49 ? 59  LYS B NZ  1 
ATOM   457  N  N   . ILE A 1 60  ? -22.693 2.222   15.836  1.00 12.00 ? 60  ILE B N   1 
ATOM   458  C  CA  . ILE A 1 60  ? -22.204 3.360   15.049  1.00 15.35 ? 60  ILE B CA  1 
ATOM   459  C  C   . ILE A 1 60  ? -21.132 2.856   14.153  1.00 13.80 ? 60  ILE B C   1 
ATOM   460  O  O   . ILE A 1 60  ? -20.350 1.910   14.539  1.00 14.30 ? 60  ILE B O   1 
ATOM   461  C  CB  . ILE A 1 60  ? -21.551 4.338   16.059  1.00 15.48 ? 60  ILE B CB  1 
ATOM   462  C  CG1 . ILE A 1 60  ? -22.738 4.917   16.857  1.00 20.56 ? 60  ILE B CG1 1 
ATOM   463  C  CG2 . ILE A 1 60  ? -20.728 5.468   15.378  1.00 17.17 ? 60  ILE B CG2 1 
ATOM   464  C  CD1 . ILE A 1 60  ? -22.323 5.649   18.069  1.00 24.12 ? 60  ILE B CD1 1 
ATOM   465  N  N   . ILE A 1 61  ? -20.995 3.412   12.964  1.00 12.64 ? 61  ILE B N   1 
ATOM   466  C  CA  . ILE A 1 61  ? -19.827 3.077   12.097  1.00 12.13 ? 61  ILE B CA  1 
ATOM   467  C  C   . ILE A 1 61  ? -19.095 4.451   11.849  1.00 12.49 ? 61  ILE B C   1 
ATOM   468  O  O   . ILE A 1 61  ? -19.811 5.503   11.628  1.00 14.49 ? 61  ILE B O   1 
ATOM   469  C  CB  . ILE A 1 61  ? -20.241 2.333   10.824  1.00 11.90 ? 61  ILE B CB  1 
ATOM   470  C  CG1 . ILE A 1 61  ? -18.994 1.925   10.054  1.00 13.09 ? 61  ILE B CG1 1 
ATOM   471  C  CG2 . ILE A 1 61  ? -21.105 3.240   9.940   1.00 14.17 ? 61  ILE B CG2 1 
ATOM   472  C  CD1 . ILE A 1 61  ? -19.210 0.947   8.937   1.00 14.72 ? 61  ILE B CD1 1 
ATOM   473  N  N   . SER A 1 62  ? -17.797 4.470   11.887  1.00 13.19 ? 62  SER B N   1 
ATOM   474  C  CA  . SER A 1 62  ? -17.025 5.706   11.744  1.00 13.87 ? 62  SER B CA  1 
ATOM   475  C  C   . SER A 1 62  ? -15.751 5.488   10.955  1.00 15.42 ? 62  SER B C   1 
ATOM   476  O  O   . SER A 1 62  ? -15.298 4.355   10.769  1.00 12.81 ? 62  SER B O   1 
ATOM   477  C  CB  . SER A 1 62  ? -16.669 6.342   13.063  1.00 16.48 ? 62  SER B CB  1 
ATOM   478  O  OG  . SER A 1 62  ? -15.887 5.463   13.883  1.00 18.66 ? 62  SER B OG  1 
ATOM   479  N  N   . ASN A 1 63  ? -15.195 6.577   10.388  1.00 13.90 ? 63  ASN B N   1 
ATOM   480  C  CA  . ASN A 1 63  ? -13.957 6.505   9.700   1.00 13.32 ? 63  ASN B CA  1 
ATOM   481  C  C   . ASN A 1 63  ? -12.921 7.041   10.609  1.00 13.18 ? 63  ASN B C   1 
ATOM   482  O  O   . ASN A 1 63  ? -12.938 8.293   10.957  1.00 16.25 ? 63  ASN B O   1 
ATOM   483  C  CB  . ASN A 1 63  ? -14.045 7.328   8.405   1.00 14.02 ? 63  ASN B CB  1 
ATOM   484  C  CG  . ASN A 1 63  ? -12.707 7.322   7.668   1.00 13.63 ? 63  ASN B CG  1 
ATOM   485  O  OD1 . ASN A 1 63  ? -11.671 6.814   8.108   1.00 13.98 ? 63  ASN B OD1 1 
ATOM   486  N  ND2 . ASN A 1 63  ? -12.704 8.084   6.502   1.00 14.67 ? 63  ASN B ND2 1 
ATOM   487  N  N   . SER A 1 64  ? -11.968 6.287   11.120  1.00 12.22 ? 64  SER B N   1 
ATOM   488  C  CA  . SER A 1 64  ? -10.916 6.823   11.975  1.00 13.73 ? 64  SER B CA  1 
ATOM   489  C  C   . SER A 1 64  ? -9.779  7.513   11.296  1.00 15.79 ? 64  SER B C   1 
ATOM   490  O  O   . SER A 1 64  ? -8.871  8.052   11.953  1.00 17.53 ? 64  SER B O   1 
ATOM   491  C  CB  . SER A 1 64  ? -10.298 5.710   12.759  1.00 15.18 ? 64  SER B CB  1 
ATOM   492  O  OG  . SER A 1 64  ? -9.612  4.759   11.879  1.00 14.53 ? 64  SER B OG  1 
ATOM   493  N  N   . GLY A 1 65  ? -9.775  7.412   9.960   1.00 13.84 ? 65  GLY B N   1 
ATOM   494  C  CA  . GLY A 1 65  ? -8.579  7.800   9.156   1.00 16.02 ? 65  GLY B CA  1 
ATOM   495  C  C   . GLY A 1 65  ? -7.685  6.588   8.886   1.00 13.14 ? 65  GLY B C   1 
ATOM   496  O  O   . GLY A 1 65  ? -6.880  6.641   7.947   1.00 14.77 ? 65  GLY B O   1 
ATOM   497  N  N   . HIS A 1 66  ? -7.830  5.464   9.635   1.00 11.34 ? 66  HIS B N   1 
ATOM   498  C  CA  . HIS A 1 66  ? -6.979  4.301   9.597   1.00 11.89 ? 66  HIS B CA  1 
ATOM   499  C  C   . HIS A 1 66  ? -7.746  3.042   9.143   1.00 10.17 ? 66  HIS B C   1 
ATOM   500  O  O   . HIS A 1 66  ? -7.057  2.056   8.752   1.00 10.82 ? 66  HIS B O   1 
ATOM   501  C  CB  . HIS A 1 66  ? -6.314  4.044   10.959  1.00 13.84 ? 66  HIS B CB  1 
ATOM   502  C  CG  . HIS A 1 66  ? -5.775  5.250   11.608  1.00 17.11 ? 66  HIS B CG  1 
ATOM   503  N  ND1 . HIS A 1 66  ? -4.785  6.021   11.084  1.00 19.49 ? 66  HIS B ND1 1 
ATOM   504  C  CD2 . HIS A 1 66  ? -6.139  5.784   12.810  1.00 18.99 ? 66  HIS B CD2 1 
ATOM   505  C  CE1 . HIS A 1 66  ? -4.554  7.064   11.961  1.00 18.88 ? 66  HIS B CE1 1 
ATOM   506  N  NE2 . HIS A 1 66  ? -5.315  6.865   13.037  1.00 23.28 ? 66  HIS B NE2 1 
ATOM   507  N  N   . SER A 1 67  ? -9.066  3.081   9.267   1.00 10.01 ? 67  SER B N   1 
ATOM   508  C  CA  . SER A 1 67  ? -9.960  2.000   8.840   1.00 9.90  ? 67  SER B CA  1 
ATOM   509  C  C   . SER A 1 67  ? -11.370 2.517   9.040   1.00 10.76 ? 67  SER B C   1 
ATOM   510  O  O   . SER A 1 67  ? -11.547 3.711   9.504   1.00 12.48 ? 67  SER B O   1 
ATOM   511  C  CB  . SER A 1 67  ? -9.756  0.697   9.662   1.00 9.40  ? 67  SER B CB  1 
ATOM   512  O  OG  . SER A 1 67  ? -10.552 -0.347  9.033   1.00 10.43 ? 67  SER B OG  1 
ATOM   513  N  N   . PHE A 1 68  ? -12.420 1.742   8.788   1.00 10.12 ? 68  PHE B N   1 
ATOM   514  C  CA  . PHE A 1 68  ? -13.681 2.038   9.436   1.00 9.82  ? 68  PHE B CA  1 
ATOM   515  C  C   . PHE A 1 68  ? -13.714 1.267   10.780  1.00 10.87 ? 68  PHE B C   1 
ATOM   516  O  O   . PHE A 1 68  ? -13.044 0.294   10.951  1.00 13.30 ? 68  PHE B O   1 
ATOM   517  C  CB  . PHE A 1 68  ? -14.903 1.605   8.629   1.00 11.53 ? 68  PHE B CB  1 
ATOM   518  C  CG  . PHE A 1 68  ? -15.052 0.095   8.553   1.00 11.48 ? 68  PHE B CG  1 
ATOM   519  C  CD1 . PHE A 1 68  ? -14.480 -0.655  7.496   1.00 11.73 ? 68  PHE B CD1 1 
ATOM   520  C  CD2 . PHE A 1 68  ? -15.761 -0.624  9.515   1.00 12.83 ? 68  PHE B CD2 1 
ATOM   521  C  CE1 . PHE A 1 68  ? -14.569 -2.016  7.440   1.00 12.59 ? 68  PHE B CE1 1 
ATOM   522  C  CE2 . PHE A 1 68  ? -15.872 -2.025  9.474   1.00 14.22 ? 68  PHE B CE2 1 
ATOM   523  C  CZ  . PHE A 1 68  ? -15.240 -2.700  8.421   1.00 13.43 ? 68  PHE B CZ  1 
ATOM   524  N  N   . ASN A 1 69  ? -14.542 1.780   11.683  1.00 11.57 ? 69  ASN B N   1 
ATOM   525  C  CA  . ASN A 1 69  ? -14.851 1.000   12.935  1.00 12.94 ? 69  ASN B CA  1 
ATOM   526  C  C   . ASN A 1 69  ? -16.308 0.889   13.137  1.00 11.29 ? 69  ASN B C   1 
ATOM   527  O  O   . ASN A 1 69  ? -17.034 1.928   13.069  1.00 13.27 ? 69  ASN B O   1 
ATOM   528  C  CB  . ASN A 1 69  ? -14.262 1.693   14.139  1.00 14.06 ? 69  ASN B CB  1 
ATOM   529  C  CG  . ASN A 1 69  ? -12.824 1.588   14.138  1.00 16.27 ? 69  ASN B CG  1 
ATOM   530  O  OD1 . ASN A 1 69  ? -12.193 2.512   13.823  1.00 19.97 ? 69  ASN B OD1 1 
ATOM   531  N  ND2 . ASN A 1 69  ? -12.265 0.448   14.567  1.00 17.70 ? 69  ASN B ND2 1 
ATOM   532  N  N   . VAL A 1 70  ? -16.850 -0.334  13.334  1.00 12.13 ? 70  VAL B N   1 
ATOM   533  C  CA  . VAL A 1 70  ? -18.138 -0.574  13.830  1.00 11.51 ? 70  VAL B CA  1 
ATOM   534  C  C   . VAL A 1 70  ? -17.992 -0.660  15.333  1.00 12.64 ? 70  VAL B C   1 
ATOM   535  O  O   . VAL A 1 70  ? -17.243 -1.518  15.836  1.00 13.91 ? 70  VAL B O   1 
ATOM   536  C  CB  . VAL A 1 70  ? -18.843 -1.816  13.257  1.00 12.26 ? 70  VAL B CB  1 
ATOM   537  C  CG1 . VAL A 1 70  ? -20.215 -2.053  13.956  1.00 14.66 ? 70  VAL B CG1 1 
ATOM   538  C  CG2 . VAL A 1 70  ? -19.059 -1.620  11.748  1.00 13.11 ? 70  VAL B CG2 1 
ATOM   539  N  N   . ASP A 1 71  ? -18.584 0.329   16.054  1.00 12.54 ? 71  ASP B N   1 
ATOM   540  C  CA  . ASP A 1 71  ? -18.579 0.334   17.565  1.00 11.65 ? 71  ASP B CA  1 
ATOM   541  C  C   . ASP A 1 71  ? -19.850 -0.340  18.041  1.00 10.94 ? 71  ASP B C   1 
ATOM   542  O  O   . ASP A 1 71  ? -20.962 -0.091  17.603  1.00 11.04 ? 71  ASP B O   1 
ATOM   543  C  CB  . ASP A 1 71  ? -18.513 1.793   18.114  1.00 13.80 ? 71  ASP B CB  1 
ATOM   544  C  CG  . ASP A 1 71  ? -17.265 2.461   17.748  1.00 18.84 ? 71  ASP B CG  1 
ATOM   545  O  OD1 . ASP A 1 71  ? -16.189 1.844   17.540  1.00 20.58 ? 71  ASP B OD1 1 
ATOM   546  O  OD2 . ASP A 1 71  ? -17.336 3.719   17.702  1.00 24.28 ? 71  ASP B OD2 1 
ATOM   547  N  N   . PHE A 1 72  ? -19.576 -1.216  19.011  1.00 12.83 ? 72  PHE B N   1 
ATOM   548  C  CA  . PHE A 1 72  ? -20.650 -1.994  19.721  1.00 12.67 ? 72  PHE B CA  1 
ATOM   549  C  C   . PHE A 1 72  ? -20.783 -1.392  21.109  1.00 12.52 ? 72  PHE B C   1 
ATOM   550  O  O   . PHE A 1 72  ? -19.829 -0.945  21.719  1.00 14.73 ? 72  PHE B O   1 
ATOM   551  C  CB  . PHE A 1 72  ? -20.289 -3.492  19.837  1.00 12.37 ? 72  PHE B CB  1 
ATOM   552  C  CG  . PHE A 1 72  ? -20.144 -4.144  18.484  1.00 11.47 ? 72  PHE B CG  1 
ATOM   553  C  CD1 . PHE A 1 72  ? -19.004 -3.906  17.733  1.00 14.27 ? 72  PHE B CD1 1 
ATOM   554  C  CD2 . PHE A 1 72  ? -21.154 -4.903  17.916  1.00 13.63 ? 72  PHE B CD2 1 
ATOM   555  C  CE1 . PHE A 1 72  ? -18.838 -4.449  16.477  1.00 14.01 ? 72  PHE B CE1 1 
ATOM   556  C  CE2 . PHE A 1 72  ? -21.001 -5.454  16.652  1.00 15.37 ? 72  PHE B CE2 1 
ATOM   557  C  CZ  . PHE A 1 72  ? -19.837 -5.227  15.929  1.00 13.71 ? 72  PHE B CZ  1 
ATOM   558  N  N   . ASP A 1 73  ? -22.017 -1.472  21.596  1.00 12.81 ? 73  ASP B N   1 
ATOM   559  C  CA  . ASP A 1 73  ? -22.255 -1.006  23.015  1.00 13.95 ? 73  ASP B CA  1 
ATOM   560  C  C   . ASP A 1 73  ? -21.657 -2.096  23.935  1.00 12.98 ? 73  ASP B C   1 
ATOM   561  O  O   . ASP A 1 73  ? -22.245 -3.198  23.894  1.00 16.27 ? 73  ASP B O   1 
ATOM   562  C  CB  . ASP A 1 73  ? -23.763 -0.948  23.214  1.00 14.52 ? 73  ASP B CB  1 
ATOM   563  C  CG  . ASP A 1 73  ? -24.146 -0.521  24.601  1.00 14.04 ? 73  ASP B CG  1 
ATOM   564  O  OD1 . ASP A 1 73  ? -23.231 -0.255  25.402  1.00 17.38 ? 73  ASP B OD1 1 
ATOM   565  O  OD2 . ASP A 1 73  ? -25.358 -0.454  24.890  1.00 19.66 ? 73  ASP B OD2 1 
ATOM   566  N  N   . ASP A 1 74  ? -20.609 -1.763  24.597  1.00 12.42 ? 74  ASP B N   1 
ATOM   567  C  CA  . ASP A 1 74  ? -19.891 -2.645  25.505  1.00 14.76 ? 74  ASP B CA  1 
ATOM   568  C  C   . ASP A 1 74  ? -20.176 -2.294  27.046  1.00 13.67 ? 74  ASP B C   1 
ATOM   569  O  O   . ASP A 1 74  ? -19.320 -2.552  27.840  1.00 15.83 ? 74  ASP B O   1 
ATOM   570  C  CB  . ASP A 1 74  ? -18.344 -2.790  25.223  1.00 15.05 ? 74  ASP B CB  1 
ATOM   571  C  CG  . ASP A 1 74  ? -17.587 -1.525  25.606  1.00 14.97 ? 74  ASP B CG  1 
ATOM   572  O  OD1 . ASP A 1 74  ? -18.266 -0.492  25.817  1.00 19.34 ? 74  ASP B OD1 1 
ATOM   573  O  OD2 . ASP A 1 74  ? -16.333 -1.533  25.689  1.00 18.47 ? 74  ASP B OD2 1 
ATOM   574  N  N   . THR A 1 75  ? -21.353 -1.723  27.212  1.00 16.20 ? 75  THR B N   1 
ATOM   575  C  CA  . THR A 1 75  ? -21.953 -1.480  28.607  1.00 17.16 ? 75  THR B CA  1 
ATOM   576  C  C   . THR A 1 75  ? -22.172 -2.762  29.320  1.00 17.78 ? 75  THR B C   1 
ATOM   577  O  O   . THR A 1 75  ? -22.043 -2.740  30.519  1.00 16.72 ? 75  THR B O   1 
ATOM   578  C  CB  . THR A 1 75  ? -23.369 -0.718  28.544  1.00 17.43 ? 75  THR B CB  1 
ATOM   579  O  OG1 . THR A 1 75  ? -23.229 0.454   27.793  1.00 19.96 ? 75  THR B OG1 1 
ATOM   580  C  CG2 . THR A 1 75  ? -23.921 -0.323  29.918  1.00 18.67 ? 75  THR B CG2 1 
ATOM   581  N  N   . GLU A 1 76  ? -22.738 -3.800  28.718  1.00 19.99 ? 76  GLU B N   1 
ATOM   582  C  CA  . GLU A 1 76  ? -22.788 -5.079  29.477  1.00 24.05 ? 76  GLU B CA  1 
ATOM   583  C  C   . GLU A 1 76  ? -22.475 -6.254  28.595  1.00 18.77 ? 76  GLU B C   1 
ATOM   584  O  O   . GLU A 1 76  ? -21.718 -6.010  27.620  1.00 19.55 ? 76  GLU B O   1 
ATOM   585  C  CB  . GLU A 1 76  ? -24.068 -5.256  30.274  1.00 30.10 ? 76  GLU B CB  1 
ATOM   586  C  CG  . GLU A 1 76  ? -25.316 -5.305  29.437  1.00 30.97 ? 76  GLU B CG  1 
ATOM   587  C  CD  . GLU A 1 76  ? -26.539 -5.602  30.291  1.00 43.32 ? 76  GLU B CD  1 
ATOM   588  O  OE1 . GLU A 1 76  ? -26.366 -5.610  31.534  1.00 45.68 ? 76  GLU B OE1 1 
ATOM   589  O  OE2 . GLU A 1 76  ? -27.649 -5.832  29.728  1.00 45.08 ? 76  GLU B OE2 1 
ATOM   590  N  N   . ASN A 1 77  ? -22.698 -7.465  29.040  1.00 17.90 ? 77  ASN B N   1 
ATOM   591  C  CA  . ASN A 1 77  ? -22.198 -8.638  28.465  1.00 16.29 ? 77  ASN B CA  1 
ATOM   592  C  C   . ASN A 1 77  ? -23.197 -9.248  27.511  1.00 15.90 ? 77  ASN B C   1 
ATOM   593  O  O   . ASN A 1 77  ? -23.391 -10.496 27.563  1.00 22.17 ? 77  ASN B O   1 
ATOM   594  C  CB  . ASN A 1 77  ? -21.900 -9.715  29.549  1.00 20.32 ? 77  ASN B CB  1 
ATOM   595  C  CG  . ASN A 1 77  ? -20.559 -9.617  30.039  1.00 16.59 ? 77  ASN B CG  1 
ATOM   596  O  OD1 . ASN A 1 77  ? -19.642 -9.073  29.419  1.00 13.44 ? 77  ASN B OD1 1 
ATOM   597  N  ND2 . ASN A 1 77  ? -20.315 -10.376 31.164  1.00 19.18 ? 77  ASN B ND2 1 
ATOM   598  N  N   . LYS A 1 78  ? -23.814 -8.509  26.625  1.00 12.48 ? 78  LYS B N   1 
ATOM   599  C  CA  . LYS A 1 78  ? -24.662 -9.118  25.635  1.00 14.90 ? 78  LYS B CA  1 
ATOM   600  C  C   . LYS A 1 78  ? -23.830 -9.871  24.531  1.00 13.37 ? 78  LYS B C   1 
ATOM   601  O  O   . LYS A 1 78  ? -24.301 -10.940 23.990  1.00 13.47 ? 78  LYS B O   1 
ATOM   602  C  CB  . LYS A 1 78  ? -25.619 -8.138  24.924  1.00 16.20 ? 78  LYS B CB  1 
ATOM   603  C  CG  . LYS A 1 78  ? -26.628 -7.539  25.902  1.00 21.49 ? 78  LYS B CG  1 
ATOM   604  C  CD  . LYS A 1 78  ? -27.381 -6.417  25.156  1.00 29.09 ? 78  LYS B CD  1 
ATOM   605  C  CE  . LYS A 1 78  ? -28.405 -5.646  26.039  1.00 33.92 ? 78  LYS B CE  1 
ATOM   606  N  NZ  . LYS A 1 78  ? -29.773 -6.014  25.558  1.00 42.75 ? 78  LYS B NZ  1 
ATOM   607  N  N   . SER A 1 79  ? -22.621 -9.368  24.204  1.00 10.93 ? 79  SER B N   1 
ATOM   608  C  CA  . SER A 1 79  ? -21.850 -9.953  23.101  1.00 9.98  ? 79  SER B CA  1 
ATOM   609  C  C   . SER A 1 79  ? -20.516 -10.233 23.622  1.00 9.37  ? 79  SER B C   1 
ATOM   610  O  O   . SER A 1 79  ? -19.745 -9.336  24.045  1.00 10.15 ? 79  SER B O   1 
ATOM   611  C  CB  . SER A 1 79  ? -21.803 -8.911  21.998  1.00 9.68  ? 79  SER B CB  1 
ATOM   612  O  OG  . SER A 1 79  ? -23.094 -8.731  21.387  1.00 11.17 ? 79  SER B OG  1 
ATOM   613  N  N   . VAL A 1 80  ? -20.185 -11.550 23.697  1.00 10.00 ? 80  VAL B N   1 
ATOM   614  C  CA  . VAL A 1 80  ? -18.954 -11.999 24.341  1.00 9.46  ? 80  VAL B CA  1 
ATOM   615  C  C   . VAL A 1 80  ? -18.319 -13.166 23.593  1.00 11.31 ? 80  VAL B C   1 
ATOM   616  O  O   . VAL A 1 80  ? -19.039 -14.004 22.957  1.00 10.36 ? 80  VAL B O   1 
ATOM   617  C  CB  . VAL A 1 80  ? -19.183 -12.463 25.839  1.00 11.28 ? 80  VAL B CB  1 
ATOM   618  C  CG1 . VAL A 1 80  ? -19.711 -11.280 26.704  1.00 13.22 ? 80  VAL B CG1 1 
ATOM   619  C  CG2 . VAL A 1 80  ? -20.203 -13.606 25.985  1.00 13.97 ? 80  VAL B CG2 1 
ATOM   620  N  N   . LEU A 1 81  ? -17.011 -13.264 23.755  1.00 10.32 ? 81  LEU B N   1 
ATOM   621  C  CA  . LEU A 1 81  ? -16.282 -14.433 23.211  1.00 9.63  ? 81  LEU B CA  1 
ATOM   622  C  C   . LEU A 1 81  ? -15.693 -15.134 24.418  1.00 9.61  ? 81  LEU B C   1 
ATOM   623  O  O   . LEU A 1 81  ? -15.043 -14.526 25.248  1.00 9.40  ? 81  LEU B O   1 
ATOM   624  C  CB  . LEU A 1 81  ? -15.103 -13.864 22.333  1.00 10.40 ? 81  LEU B CB  1 
ATOM   625  C  CG  . LEU A 1 81  ? -14.169 -14.934 21.690  1.00 10.90 ? 81  LEU B CG  1 
ATOM   626  C  CD1 . LEU A 1 81  ? -14.919 -15.892 20.772  1.00 12.07 ? 81  LEU B CD1 1 
ATOM   627  C  CD2 . LEU A 1 81  ? -13.003 -14.188 20.972  1.00 11.31 ? 81  LEU B CD2 1 
ATOM   628  N  N   . ARG A 1 82  ? -15.830 -16.479 24.416  1.00 9.46  ? 82  ARG B N   1 
ATOM   629  C  CA  . ARG A 1 82  ? -15.277 -17.368 25.468  1.00 10.57 ? 82  ARG B CA  1 
ATOM   630  C  C   . ARG A 1 82  ? -14.722 -18.587 24.746  1.00 10.26 ? 82  ARG B C   1 
ATOM   631  O  O   . ARG A 1 82  ? -14.788 -18.728 23.530  1.00 10.65 ? 82  ARG B O   1 
ATOM   632  C  CB  . ARG A 1 82  ? -16.417 -17.756 26.420  1.00 12.00 ? 82  ARG B CB  1 
ATOM   633  C  CG  . ARG A 1 82  ? -16.835 -16.607 27.288  1.00 12.00 ? 82  ARG B CG  1 
ATOM   634  C  CD  . ARG A 1 82  ? -18.117 -16.937 28.047  1.00 14.92 ? 82  ARG B CD  1 
ATOM   635  N  NE  . ARG A 1 82  ? -19.209 -17.026 27.156  1.00 15.80 ? 82  ARG B NE  1 
ATOM   636  C  CZ  . ARG A 1 82  ? -20.467 -17.238 27.514  1.00 19.42 ? 82  ARG B CZ  1 
ATOM   637  N  NH1 . ARG A 1 82  ? -20.739 -17.477 28.822  1.00 22.99 ? 82  ARG B NH1 1 
ATOM   638  N  NH2 . ARG A 1 82  ? -21.401 -17.354 26.571  1.00 19.84 ? 82  ARG B NH2 1 
ATOM   639  N  N   . GLY A 1 83  ? -14.081 -19.471 25.548  1.00 10.03 ? 83  GLY B N   1 
ATOM   640  C  CA  . GLY A 1 83  ? -13.524 -20.635 24.981  1.00 11.32 ? 83  GLY B CA  1 
ATOM   641  C  C   . GLY A 1 83  ? -12.232 -20.318 24.218  1.00 9.93  ? 83  GLY B C   1 
ATOM   642  O  O   . GLY A 1 83  ? -11.511 -19.387 24.533  1.00 11.19 ? 83  GLY B O   1 
ATOM   643  N  N   . GLY A 1 84  ? -11.958 -21.154 23.194  1.00 12.01 ? 84  GLY B N   1 
ATOM   644  C  CA  . GLY A 1 84  ? -10.656 -20.907 22.426  1.00 12.12 ? 84  GLY B CA  1 
ATOM   645  C  C   . GLY A 1 84  ? -9.524  -21.082 23.419  1.00 12.18 ? 84  GLY B C   1 
ATOM   646  O  O   . GLY A 1 84  ? -9.535  -21.985 24.298  1.00 13.34 ? 84  GLY B O   1 
ATOM   647  N  N   . PRO A 1 85  ? -8.502  -20.202 23.418  1.00 11.28 ? 85  PRO B N   1 
ATOM   648  C  CA  . PRO A 1 85  ? -7.382  -20.192 24.377  1.00 11.58 ? 85  PRO B CA  1 
ATOM   649  C  C   . PRO A 1 85  ? -7.699  -19.360 25.604  1.00 12.06 ? 85  PRO B C   1 
ATOM   650  O  O   . PRO A 1 85  ? -6.858  -19.163 26.471  1.00 13.43 ? 85  PRO B O   1 
ATOM   651  C  CB  . PRO A 1 85  ? -6.218  -19.455 23.620  1.00 10.50 ? 85  PRO B CB  1 
ATOM   652  C  CG  . PRO A 1 85  ? -7.033  -18.427 22.746  1.00 10.95 ? 85  PRO B CG  1 
ATOM   653  C  CD  . PRO A 1 85  ? -8.295  -19.210 22.285  1.00 11.00 ? 85  PRO B CD  1 
ATOM   654  N  N   . LEU A 1 86  ? -8.881  -18.760 25.712  1.00 11.04 ? 86  LEU B N   1 
ATOM   655  C  CA  . LEU A 1 86  ? -9.171  -17.724 26.668  1.00 11.15 ? 86  LEU B CA  1 
ATOM   656  C  C   . LEU A 1 86  ? -9.626  -18.234 28.068  1.00 12.40 ? 86  LEU B C   1 
ATOM   657  O  O   . LEU A 1 86  ? -10.393 -19.171 28.132  1.00 13.12 ? 86  LEU B O   1 
ATOM   658  C  CB  . LEU A 1 86  ? -10.270 -16.793 26.135  1.00 10.67 ? 86  LEU B CB  1 
ATOM   659  C  CG  . LEU A 1 86  ? -9.984  -16.166 24.737  1.00 9.76  ? 86  LEU B CG  1 
ATOM   660  C  CD1 . LEU A 1 86  ? -11.282 -15.519 24.319  1.00 11.42 ? 86  LEU B CD1 1 
ATOM   661  C  CD2 . LEU A 1 86  ? -8.897  -15.139 24.826  1.00 10.77 ? 86  LEU B CD2 1 
ATOM   662  N  N   . THR A 1 87  ? -9.152  -17.502 29.057  1.00 12.78 ? 87  THR B N   1 
ATOM   663  C  CA  . THR A 1 87  ? -9.693  -17.699 30.472  1.00 14.98 ? 87  THR B CA  1 
ATOM   664  C  C   . THR A 1 87  ? -10.693 -16.617 30.676  1.00 15.11 ? 87  THR B C   1 
ATOM   665  O  O   . THR A 1 87  ? -10.282 -15.440 30.605  1.00 13.96 ? 87  THR B O   1 
ATOM   666  C  CB  . THR A 1 87  ? -8.546  -17.599 31.394  1.00 15.21 ? 87  THR B CB  1 
ATOM   667  O  OG1 . THR A 1 87  ? -7.686  -18.763 31.228  1.00 19.66 ? 87  THR B OG1 1 
ATOM   668  C  CG2 . THR A 1 87  ? -9.017  -17.546 32.929  1.00 20.93 ? 87  THR B CG2 1 
ATOM   669  N  N   . GLY A 1 88  ? -11.958 -17.003 30.912  1.00 13.81 ? 88  GLY B N   1 
ATOM   670  C  CA  . GLY A 1 88  ? -12.924 -15.948 31.239  1.00 14.75 ? 88  GLY B CA  1 
ATOM   671  C  C   . GLY A 1 88  ? -13.560 -15.335 29.956  1.00 13.10 ? 88  GLY B C   1 
ATOM   672  O  O   . GLY A 1 88  ? -13.418 -15.894 28.850  1.00 15.29 ? 88  GLY B O   1 
ATOM   673  N  N   . SER A 1 89  ? -14.300 -14.242 30.162  1.00 12.35 ? 89  SER B N   1 
ATOM   674  C  CA  . SER A 1 89  ? -15.209 -13.706 29.161  1.00 12.52 ? 89  SER B CA  1 
ATOM   675  C  C   . SER A 1 89  ? -14.678 -12.401 28.638  1.00 12.15 ? 89  SER B C   1 
ATOM   676  O  O   . SER A 1 89  ? -14.338 -11.470 29.372  1.00 12.45 ? 89  SER B O   1 
ATOM   677  C  CB  . SER A 1 89  ? -16.596 -13.493 29.826  1.00 14.01 ? 89  SER B CB  1 
ATOM   678  O  OG  . SER A 1 89  ? -17.522 -13.091 28.885  1.00 13.51 ? 89  SER B OG  1 
ATOM   679  N  N   . TYR A 1 90  ? -14.591 -12.354 27.304  1.00 9.77  ? 90  TYR B N   1 
ATOM   680  C  CA  . TYR A 1 90  ? -14.091 -11.175 26.544  1.00 9.62  ? 90  TYR B CA  1 
ATOM   681  C  C   . TYR A 1 90  ? -15.213 -10.481 25.818  1.00 10.03 ? 90  TYR B C   1 
ATOM   682  O  O   . TYR A 1 90  ? -15.899 -11.083 24.967  1.00 10.75 ? 90  TYR B O   1 
ATOM   683  C  CB  . TYR A 1 90  ? -12.971 -11.619 25.628  1.00 9.22  ? 90  TYR B CB  1 
ATOM   684  C  CG  . TYR A 1 90  ? -11.679 -11.897 26.392  1.00 8.06  ? 90  TYR B CG  1 
ATOM   685  C  CD1 . TYR A 1 90  ? -11.602 -13.049 27.227  1.00 10.02 ? 90  TYR B CD1 1 
ATOM   686  C  CD2 . TYR A 1 90  ? -10.551 -11.078 26.248  1.00 8.77  ? 90  TYR B CD2 1 
ATOM   687  C  CE1 . TYR A 1 90  ? -10.388 -13.340 27.880  1.00 9.64  ? 90  TYR B CE1 1 
ATOM   688  C  CE2 . TYR A 1 90  ? -9.337  -11.382 26.858  1.00 9.21  ? 90  TYR B CE2 1 
ATOM   689  C  CZ  . TYR A 1 90  ? -9.307  -12.491 27.747  1.00 9.48  ? 90  TYR B CZ  1 
ATOM   690  O  OH  . TYR A 1 90  ? -8.102  -12.816 28.418  1.00 11.29 ? 90  TYR B OH  1 
ATOM   691  N  N   . ARG A 1 91  ? -15.514 -9.229  26.162  1.00 8.86  ? 91  ARG B N   1 
ATOM   692  C  CA  . ARG A 1 91  ? -16.613 -8.464  25.664  1.00 9.61  ? 91  ARG B CA  1 
ATOM   693  C  C   . ARG A 1 91  ? -16.325 -7.787  24.320  1.00 8.89  ? 91  ARG B C   1 
ATOM   694  O  O   . ARG A 1 91  ? -15.274 -7.162  24.202  1.00 9.72  ? 91  ARG B O   1 
ATOM   695  C  CB  . ARG A 1 91  ? -16.979 -7.364  26.712  1.00 10.06 ? 91  ARG B CB  1 
ATOM   696  C  CG  . ARG A 1 91  ? -18.293 -6.755  26.478  1.00 11.02 ? 91  ARG B CG  1 
ATOM   697  C  CD  . ARG A 1 91  ? -18.581 -5.703  27.517  1.00 11.53 ? 91  ARG B CD  1 
ATOM   698  N  NE  . ARG A 1 91  ? -18.706 -6.345  28.824  1.00 10.96 ? 91  ARG B NE  1 
ATOM   699  C  CZ  . ARG A 1 91  ? -18.898 -5.706  29.973  1.00 12.53 ? 91  ARG B CZ  1 
ATOM   700  N  NH1 . ARG A 1 91  ? -18.985 -4.383  29.998  1.00 12.29 ? 91  ARG B NH1 1 
ATOM   701  N  NH2 . ARG A 1 91  ? -19.002 -6.398  31.101  1.00 11.39 ? 91  ARG B NH2 1 
ATOM   702  N  N   . LEU A 1 92  ? -17.269 -7.960  23.402  1.00 9.50  ? 92  LEU B N   1 
ATOM   703  C  CA  . LEU A 1 92  ? -17.119 -7.305  22.072  1.00 10.27 ? 92  LEU B CA  1 
ATOM   704  C  C   . LEU A 1 92  ? -17.091 -5.800  22.223  1.00 10.34 ? 92  LEU B C   1 
ATOM   705  O  O   . LEU A 1 92  ? -18.028 -5.152  22.759  1.00 11.26 ? 92  LEU B O   1 
ATOM   706  C  CB  . LEU A 1 92  ? -18.295 -7.753  21.238  1.00 10.13 ? 92  LEU B CB  1 
ATOM   707  C  CG  . LEU A 1 92  ? -18.343 -7.155  19.802  1.00 9.24  ? 92  LEU B CG  1 
ATOM   708  C  CD1 . LEU A 1 92  ? -17.096 -7.583  18.979  1.00 12.18 ? 92  LEU B CD1 1 
ATOM   709  C  CD2 . LEU A 1 92  ? -19.603 -7.626  19.171  1.00 9.86  ? 92  LEU B CD2 1 
ATOM   710  N  N   . ARG A 1 93  ? -16.086 -5.185  21.619  1.00 9.78  ? 93  ARG B N   1 
ATOM   711  C  CA  . ARG A 1 93  ? -15.956 -3.730  21.551  1.00 10.14 ? 93  ARG B CA  1 
ATOM   712  C  C   . ARG A 1 93  ? -16.128 -3.142  20.100  1.00 9.82  ? 93  ARG B C   1 
ATOM   713  O  O   . ARG A 1 93  ? -16.858 -2.202  19.936  1.00 10.37 ? 93  ARG B O   1 
ATOM   714  C  CB  . ARG A 1 93  ? -14.651 -3.339  22.105  1.00 13.49 ? 93  ARG B CB  1 
ATOM   715  C  CG  . ARG A 1 93  ? -14.383 -1.865  21.921  1.00 17.16 ? 93  ARG B CG  1 
ATOM   716  C  CD  . ARG A 1 93  ? -14.442 -1.104  23.135  1.00 20.49 ? 93  ARG B CD  1 
ATOM   717  N  NE  . ARG A 1 93  ? -13.843 0.209   23.004  1.00 19.10 ? 93  ARG B NE  1 
ATOM   718  C  CZ  . ARG A 1 93  ? -14.103 1.189   23.851  1.00 20.46 ? 93  ARG B CZ  1 
ATOM   719  N  NH1 . ARG A 1 93  ? -14.947 0.976   24.848  1.00 20.30 ? 93  ARG B NH1 1 
ATOM   720  N  NH2 . ARG A 1 93  ? -13.529 2.371   23.713  1.00 19.86 ? 93  ARG B NH2 1 
ATOM   721  N  N   . GLN A 1 94  ? -15.385 -3.665  19.109  1.00 10.45 ? 94  GLN B N   1 
ATOM   722  C  CA  . GLN A 1 94  ? -15.383 -2.986  17.788  1.00 10.82 ? 94  GLN B CA  1 
ATOM   723  C  C   . GLN A 1 94  ? -14.869 -3.953  16.783  1.00 9.27  ? 94  GLN B C   1 
ATOM   724  O  O   . GLN A 1 94  ? -14.186 -4.956  17.058  1.00 9.61  ? 94  GLN B O   1 
ATOM   725  C  CB  . GLN A 1 94  ? -14.555 -1.715  17.806  1.00 14.66 ? 94  GLN B CB  1 
ATOM   726  C  CG  . GLN A 1 94  ? -13.210 -1.824  18.213  1.00 13.47 ? 94  GLN B CG  1 
ATOM   727  C  CD  . GLN A 1 94  ? -12.137 -1.797  17.071  1.00 15.47 ? 94  GLN B CD  1 
ATOM   728  O  OE1 . GLN A 1 94  ? -12.439 -2.209  15.938  1.00 15.39 ? 94  GLN B OE1 1 
ATOM   729  N  NE2 . GLN A 1 94  ? -10.904 -1.435  17.386  1.00 17.79 ? 94  GLN B NE2 1 
ATOM   730  N  N   . VAL A 1 95  ? -15.273 -3.661  15.532  1.00 10.30 ? 95  VAL B N   1 
ATOM   731  C  CA  . VAL A 1 95  ? -14.845 -4.433  14.324  1.00 9.27  ? 95  VAL B CA  1 
ATOM   732  C  C   . VAL A 1 95  ? -14.243 -3.407  13.336  1.00 9.31  ? 95  VAL B C   1 
ATOM   733  O  O   . VAL A 1 95  ? -14.810 -2.349  13.106  1.00 9.45  ? 95  VAL B O   1 
ATOM   734  C  CB  . VAL A 1 95  ? -16.008 -5.115  13.682  1.00 8.88  ? 95  VAL B CB  1 
ATOM   735  C  CG1 . VAL A 1 95  ? -15.754 -5.622  12.248  1.00 11.08 ? 95  VAL B CG1 1 
ATOM   736  C  CG2 . VAL A 1 95  ? -16.543 -6.341  14.547  1.00 11.14 ? 95  VAL B CG2 1 
ATOM   737  N  N   . HIS A 1 96  ? -13.168 -3.848  12.720  1.00 8.54  ? 96  HIS B N   1 
ATOM   738  C  CA  . HIS A 1 96  ? -12.569 -3.046  11.634  1.00 8.66  ? 96  HIS B CA  1 
ATOM   739  C  C   . HIS A 1 96  ? -11.897 -3.993  10.655  1.00 9.75  ? 96  HIS B C   1 
ATOM   740  O  O   . HIS A 1 96  ? -11.976 -5.187  10.777  1.00 8.56  ? 96  HIS B O   1 
ATOM   741  C  CB  . HIS A 1 96  ? -11.591 -2.003  12.213  1.00 9.47  ? 96  HIS B CB  1 
ATOM   742  C  CG  . HIS A 1 96  ? -10.423 -2.580  12.844  1.00 7.49  ? 96  HIS B CG  1 
ATOM   743  N  ND1 . HIS A 1 96  ? -10.483 -2.939  14.204  1.00 8.76  ? 96  HIS B ND1 1 
ATOM   744  C  CD2 . HIS A 1 96  ? -9.234  -3.072  12.377  1.00 8.48  ? 96  HIS B CD2 1 
ATOM   745  C  CE1 . HIS A 1 96  ? -9.294  -3.477  14.519  1.00 8.40  ? 96  HIS B CE1 1 
ATOM   746  N  NE2 . HIS A 1 96  ? -8.562  -3.666  13.417  1.00 10.38 ? 96  HIS B NE2 1 
ATOM   747  N  N   . LEU A 1 97  ? -11.350 -3.416  9.562   1.00 9.03  ? 97  LEU B N   1 
ATOM   748  C  CA  . LEU A 1 97  ? -10.870 -4.188  8.416   1.00 8.77  ? 97  LEU B CA  1 
ATOM   749  C  C   . LEU A 1 97  ? -9.497  -3.636  7.982   1.00 8.22  ? 97  LEU B C   1 
ATOM   750  O  O   . LEU A 1 97  ? -9.220  -2.420  7.983   1.00 9.39  ? 97  LEU B O   1 
ATOM   751  C  CB  . LEU A 1 97  ? -11.875 -4.087  7.224   1.00 9.17  ? 97  LEU B CB  1 
ATOM   752  C  CG  . LEU A 1 97  ? -11.578 -4.962  6.046   1.00 8.31  ? 97  LEU B CG  1 
ATOM   753  C  CD1 . LEU A 1 97  ? -11.865 -6.420  6.387   1.00 9.09  ? 97  LEU B CD1 1 
ATOM   754  C  CD2 . LEU A 1 97  ? -12.532 -4.545  4.948   1.00 11.07 ? 97  LEU B CD2 1 
ATOM   755  N  N   . HIS A 1 98  ? -8.662  -4.536  7.494   1.00 7.30  ? 98  HIS B N   1 
ATOM   756  C  CA  . HIS A 1 98  ? -7.375  -4.118  6.870   1.00 8.16  ? 98  HIS B CA  1 
ATOM   757  C  C   . HIS A 1 98  ? -7.362  -4.726  5.445   1.00 8.34  ? 98  HIS B C   1 
ATOM   758  O  O   . HIS A 1 98  ? -7.815  -5.822  5.201   1.00 8.89  ? 98  HIS B O   1 
ATOM   759  C  CB  . HIS A 1 98  ? -6.191  -4.760  7.589   1.00 8.45  ? 98  HIS B CB  1 
ATOM   760  C  CG  . HIS A 1 98  ? -6.108  -4.338  9.034   1.00 9.69  ? 98  HIS B CG  1 
ATOM   761  N  ND1 . HIS A 1 98  ? -5.426  -3.211  9.449   1.00 9.02  ? 98  HIS B ND1 1 
ATOM   762  C  CD2 . HIS A 1 98  ? -6.685  -4.852  10.147  1.00 9.84  ? 98  HIS B CD2 1 
ATOM   763  C  CE1 . HIS A 1 98  ? -5.554  -3.074  10.759  1.00 9.40  ? 98  HIS B CE1 1 
ATOM   764  N  NE2 . HIS A 1 98  ? -6.317  -4.055  11.206  1.00 7.72  ? 98  HIS B NE2 1 
ATOM   765  N  N   . TRP A 1 99  ? -6.806  -3.921  4.498   1.00 8.30  ? 99  TRP B N   1 
ATOM   766  C  CA  . TRP A 1 99  ? -6.813  -4.308  3.080   1.00 7.86  ? 99  TRP B CA  1 
ATOM   767  C  C   . TRP A 1 99  ? -5.513  -3.734  2.534   1.00 8.81  ? 99  TRP B C   1 
ATOM   768  O  O   . TRP A 1 99  ? -4.665  -3.114  3.203   1.00 8.28  ? 99  TRP B O   1 
ATOM   769  C  CB  . TRP A 1 99  ? -8.001  -3.756  2.386   1.00 8.14  ? 99  TRP B CB  1 
ATOM   770  C  CG  . TRP A 1 99  ? -8.209  -2.244  2.468   1.00 9.52  ? 99  TRP B CG  1 
ATOM   771  C  CD1 . TRP A 1 99  ? -7.593  -1.251  1.681   1.00 9.88  ? 99  TRP B CD1 1 
ATOM   772  C  CD2 . TRP A 1 99  ? -8.990  -1.525  3.408   1.00 8.49  ? 99  TRP B CD2 1 
ATOM   773  N  NE1 . TRP A 1 99  ? -7.945  -0.024  2.081   1.00 9.16  ? 99  TRP B NE1 1 
ATOM   774  C  CE2 . TRP A 1 99  ? -8.851  -0.140  3.140   1.00 8.65  ? 99  TRP B CE2 1 
ATOM   775  C  CE3 . TRP A 1 99  ? -9.805  -1.942  4.501   1.00 10.25 ? 99  TRP B CE3 1 
ATOM   776  C  CZ2 . TRP A 1 99  ? -9.421  0.819   3.894   1.00 8.84  ? 99  TRP B CZ2 1 
ATOM   777  C  CZ3 . TRP A 1 99  ? -10.471 -0.964  5.252   1.00 9.07  ? 99  TRP B CZ3 1 
ATOM   778  C  CH2 . TRP A 1 99  ? -10.301 0.410   4.943   1.00 9.13  ? 99  TRP B CH2 1 
ATOM   779  N  N   . GLY A 1 100 ? -5.345  -3.986  1.215   1.00 9.61  ? 100 GLY B N   1 
ATOM   780  C  CA  . GLY A 1 100 ? -4.138  -3.448  0.459   1.00 9.77  ? 100 GLY B CA  1 
ATOM   781  C  C   . GLY A 1 100 ? -4.690  -2.789  -0.758  1.00 8.38  ? 100 GLY B C   1 
ATOM   782  O  O   . GLY A 1 100 ? -5.877  -2.734  -1.047  1.00 10.46 ? 100 GLY B O   1 
ATOM   783  N  N   . SER A 1 101 ? -3.703  -2.238  -1.502  1.00 10.22 ? 101 SER B N   1 
ATOM   784  C  CA  . SER A 1 101 ? -4.071  -1.616  -2.812  1.00 10.70 ? 101 SER B CA  1 
ATOM   785  C  C   . SER A 1 101 ? -4.451  -2.616  -3.878  1.00 11.52 ? 101 SER B C   1 
ATOM   786  O  O   . SER A 1 101 ? -5.104  -2.121  -4.873  1.00 12.03 ? 101 SER B O   1 
ATOM   787  C  CB  . SER A 1 101 ? -2.931  -0.663  -3.317  1.00 13.00 ? 101 SER B CB  1 
ATOM   788  O  OG  . SER A 1 101 ? -1.921  -1.415  -3.869  1.00 13.49 ? 101 SER B OG  1 
ATOM   789  N  N   . ALA A 1 102 ? -4.091  -3.855  -3.745  1.00 10.24 ? 102 ALA B N   1 
ATOM   790  C  CA  . ALA A 1 102 ? -4.478  -4.836  -4.744  1.00 11.70 ? 102 ALA B CA  1 
ATOM   791  C  C   . ALA A 1 102 ? -5.027  -6.056  -4.001  1.00 11.43 ? 102 ALA B C   1 
ATOM   792  O  O   . ALA A 1 102 ? -4.673  -6.332  -2.813  1.00 11.78 ? 102 ALA B O   1 
ATOM   793  C  CB  . ALA A 1 102 ? -3.327  -5.175  -5.585  1.00 13.35 ? 102 ALA B CB  1 
ATOM   794  N  N   . ASP A 1 103 ? -5.877  -6.758  -4.657  1.00 11.54 ? 103 ASP B N   1 
ATOM   795  C  CA  . ASP A 1 103 ? -6.527  -7.965  -4.058  1.00 11.74 ? 103 ASP B CA  1 
ATOM   796  C  C   . ASP A 1 103 ? -5.485  -8.994  -3.723  1.00 14.38 ? 103 ASP B C   1 
ATOM   797  O  O   . ASP A 1 103 ? -5.755  -9.866  -2.928  1.00 18.62 ? 103 ASP B O   1 
ATOM   798  C  CB  . ASP A 1 103 ? -7.597  -8.528  -5.013  1.00 12.53 ? 103 ASP B CB  1 
ATOM   799  C  CG  . ASP A 1 103 ? -8.749  -7.573  -5.262  1.00 13.19 ? 103 ASP B CG  1 
ATOM   800  O  OD1 . ASP A 1 103 ? -8.895  -6.577  -4.524  1.00 13.45 ? 103 ASP B OD1 1 
ATOM   801  O  OD2 . ASP A 1 103 ? -9.522  -7.838  -6.208  1.00 16.00 ? 103 ASP B OD2 1 
ATOM   802  N  N   . ASP A 1 104 ? -4.302  -8.873  -4.371  1.00 16.22 ? 104 ASP B N   1 
ATOM   803  C  CA  . ASP A 1 104 ? -3.185  -9.754  -4.251  1.00 23.05 ? 104 ASP B CA  1 
ATOM   804  C  C   . ASP A 1 104 ? -2.664  -9.881  -2.848  1.00 19.95 ? 104 ASP B C   1 
ATOM   805  O  O   . ASP A 1 104 ? -2.160  -10.915 -2.416  1.00 18.97 ? 104 ASP B O   1 
ATOM   806  C  CB  . ASP A 1 104 ? -2.021  -9.309  -5.218  1.00 19.18 ? 104 ASP B CB  1 
ATOM   807  C  CG  . ASP A 1 104 ? -2.529  -8.743  -6.527  1.00 24.64 ? 104 ASP B CG  1 
ATOM   808  O  OD1 . ASP A 1 104 ? -3.754  -8.557  -6.672  1.00 19.86 ? 104 ASP B OD1 1 
ATOM   809  O  OD2 . ASP A 1 104 ? -1.697  -8.465  -7.410  1.00 25.21 ? 104 ASP B OD2 1 
ATOM   810  N  N   . HIS A 1 105 ? -2.754  -8.779  -2.085  1.00 17.60 ? 105 HIS B N   1 
ATOM   811  C  CA  . HIS A 1 105 ? -1.969  -8.666  -0.883  1.00 15.08 ? 105 HIS B CA  1 
ATOM   812  C  C   . HIS A 1 105 ? -2.602  -7.620  0.034   1.00 13.33 ? 105 HIS B C   1 
ATOM   813  O  O   . HIS A 1 105 ? -2.262  -6.425  0.023   1.00 16.96 ? 105 HIS B O   1 
ATOM   814  C  CB  . HIS A 1 105 ? -0.553  -8.260  -1.427  1.00 20.15 ? 105 HIS B CB  1 
ATOM   815  C  CG  . HIS A 1 105 ? 0.572   -8.412  -0.474  1.00 26.26 ? 105 HIS B CG  1 
ATOM   816  N  ND1 . HIS A 1 105 ? 1.058   -7.333  0.218   1.00 25.80 ? 105 HIS B ND1 1 
ATOM   817  C  CD2 . HIS A 1 105 ? 1.353   -9.467  -0.142  1.00 26.00 ? 105 HIS B CD2 1 
ATOM   818  C  CE1 . HIS A 1 105 ? 2.063   -7.718  0.978   1.00 26.18 ? 105 HIS B CE1 1 
ATOM   819  N  NE2 . HIS A 1 105 ? 2.259   -9.010  0.786   1.00 29.52 ? 105 HIS B NE2 1 
ATOM   820  N  N   . GLY A 1 106 ? -3.513  -8.074  0.886   1.00 12.80 ? 106 GLY B N   1 
ATOM   821  C  CA  . GLY A 1 106 ? -4.214  -7.181  1.766   1.00 12.03 ? 106 GLY B CA  1 
ATOM   822  C  C   . GLY A 1 106 ? -4.291  -7.530  3.244   1.00 11.89 ? 106 GLY B C   1 
ATOM   823  O  O   . GLY A 1 106 ? -4.635  -6.661  4.028   1.00 14.09 ? 106 GLY B O   1 
ATOM   824  N  N   . SER A 1 107 ? -4.051  -8.791  3.591   1.00 11.29 ? 107 SER B N   1 
ATOM   825  C  CA  . SER A 1 107 ? -4.252  -9.218  4.976   1.00 10.23 ? 107 SER B CA  1 
ATOM   826  C  C   . SER A 1 107 ? -2.982  -8.830  5.724   1.00 9.36  ? 107 SER B C   1 
ATOM   827  O  O   . SER A 1 107 ? -1.941  -8.401  5.238   1.00 12.11 ? 107 SER B O   1 
ATOM   828  C  CB  . SER A 1 107 ? -4.521  -10.692 5.015   1.00 9.96  ? 107 SER B CB  1 
ATOM   829  O  OG  . SER A 1 107 ? -3.415  -11.507 4.532   1.00 9.79  ? 107 SER B OG  1 
ATOM   830  N  N   . GLU A 1 108 ? -3.139  -8.935  7.056   1.00 9.55  ? 108 GLU B N   1 
ATOM   831  C  CA  . GLU A 1 108 ? -2.022  -8.711  8.036   1.00 9.95  ? 108 GLU B CA  1 
ATOM   832  C  C   . GLU A 1 108 ? -1.286  -9.998  8.342   1.00 8.94  ? 108 GLU B C   1 
ATOM   833  O  O   . GLU A 1 108 ? -0.092  -10.146 8.067   1.00 10.22 ? 108 GLU B O   1 
ATOM   834  C  CB  . GLU A 1 108 ? -2.601  -8.059  9.325   1.00 9.94  ? 108 GLU B CB  1 
ATOM   835  C  CG  . GLU A 1 108 ? -3.175  -6.653  8.953   1.00 12.51 ? 108 GLU B CG  1 
ATOM   836  C  CD  . GLU A 1 108 ? -2.971  -5.659  10.028  1.00 11.60 ? 108 GLU B CD  1 
ATOM   837  O  OE1 . GLU A 1 108 ? -3.442  -5.931  11.156  1.00 11.51 ? 108 GLU B OE1 1 
ATOM   838  O  OE2 . GLU A 1 108 ? -2.463  -4.579  9.804   1.00 10.41 ? 108 GLU B OE2 1 
ATOM   839  N  N   . HIS A 1 109 ? -2.023  -11.020 8.859   1.00 8.62  ? 109 HIS B N   1 
ATOM   840  C  CA  . HIS A 1 109 ? -1.438  -12.356 8.978   1.00 9.86  ? 109 HIS B CA  1 
ATOM   841  C  C   . HIS A 1 109 ? -1.351  -12.971 7.577   1.00 10.14 ? 109 HIS B C   1 
ATOM   842  O  O   . HIS A 1 109 ? -2.177  -12.684 6.695   1.00 9.95  ? 109 HIS B O   1 
ATOM   843  C  CB  . HIS A 1 109 ? -2.333  -13.234 9.860   1.00 9.57  ? 109 HIS B CB  1 
ATOM   844  C  CG  . HIS A 1 109 ? -2.316  -12.735 11.287  1.00 9.55  ? 109 HIS B CG  1 
ATOM   845  N  ND1 . HIS A 1 109 ? -3.190  -11.774 11.754  1.00 8.30  ? 109 HIS B ND1 1 
ATOM   846  C  CD2 . HIS A 1 109 ? -1.432  -12.948 12.295  1.00 9.78  ? 109 HIS B CD2 1 
ATOM   847  C  CE1 . HIS A 1 109 ? -2.901  -11.485 13.012  1.00 9.50  ? 109 HIS B CE1 1 
ATOM   848  N  NE2 . HIS A 1 109 ? -1.841  -12.187 13.366  1.00 9.93  ? 109 HIS B NE2 1 
ATOM   849  N  N   . ILE A 1 110 ? -0.291  -13.798 7.389   1.00 11.29 ? 110 ILE B N   1 
ATOM   850  C  CA  . ILE A 1 110 ? -0.008  -14.416 6.100   1.00 11.80 ? 110 ILE B CA  1 
ATOM   851  C  C   . ILE A 1 110 ? 0.175   -15.936 6.383   1.00 12.19 ? 110 ILE B C   1 
ATOM   852  O  O   . ILE A 1 110 ? 0.825   -16.247 7.391   1.00 14.92 ? 110 ILE B O   1 
ATOM   853  C  CB  . ILE A 1 110 ? 1.323   -13.829 5.573   1.00 14.42 ? 110 ILE B CB  1 
ATOM   854  C  CG1 . ILE A 1 110 ? 1.409   -12.302 5.612   1.00 20.56 ? 110 ILE B CG1 1 
ATOM   855  C  CG2 . ILE A 1 110 ? 1.623   -14.441 4.166   1.00 14.54 ? 110 ILE B CG2 1 
ATOM   856  C  CD1 . ILE A 1 110 ? 0.465   -11.610 4.794   1.00 21.34 ? 110 ILE B CD1 1 
ATOM   857  N  N   . VAL A 1 111 ? -0.420  -16.807 5.566   1.00 11.65 ? 111 VAL B N   1 
ATOM   858  C  CA  . VAL A 1 111 ? -0.416  -18.206 5.919   1.00 12.66 ? 111 VAL B CA  1 
ATOM   859  C  C   . VAL A 1 111 ? 0.372   -18.959 4.830   1.00 13.22 ? 111 VAL B C   1 
ATOM   860  O  O   . VAL A 1 111 ? 0.012   -18.992 3.673   1.00 12.91 ? 111 VAL B O   1 
ATOM   861  C  CB  . VAL A 1 111 ? -1.847  -18.813 5.926   1.00 14.65 ? 111 VAL B CB  1 
ATOM   862  C  CG1 . VAL A 1 111 ? -1.782  -20.291 6.342   1.00 15.29 ? 111 VAL B CG1 1 
ATOM   863  C  CG2 . VAL A 1 111 ? -2.699  -18.053 6.935   1.00 14.75 ? 111 VAL B CG2 1 
ATOM   864  N  N   . ASP A 1 112 ? 1.569   -19.441 5.235   1.00 12.83 ? 112 ASP B N   1 
ATOM   865  C  CA  . ASP A 1 112 ? 2.524   -20.126 4.310   1.00 13.54 ? 112 ASP B CA  1 
ATOM   866  C  C   . ASP A 1 112 ? 2.683   -19.274 3.099   1.00 14.07 ? 112 ASP B C   1 
ATOM   867  O  O   . ASP A 1 112 ? 2.678   -19.791 1.934   1.00 14.99 ? 112 ASP B O   1 
ATOM   868  C  CB  . ASP A 1 112 ? 2.031   -21.584 4.039   1.00 14.72 ? 112 ASP B CB  1 
ATOM   869  C  CG  . ASP A 1 112 ? 2.262   -22.421 5.267   1.00 16.08 ? 112 ASP B CG  1 
ATOM   870  O  OD1 . ASP A 1 112 ? 3.345   -22.406 5.888   1.00 18.05 ? 112 ASP B OD1 1 
ATOM   871  O  OD2 . ASP A 1 112 ? 1.264   -23.166 5.608   1.00 22.90 ? 112 ASP B OD2 1 
ATOM   872  N  N   . GLY A 1 113 ? 2.876   -17.963 3.333   1.00 11.73 ? 113 GLY B N   1 
ATOM   873  C  CA  . GLY A 1 113 ? 3.102   -17.033 2.216   1.00 11.91 ? 113 GLY B CA  1 
ATOM   874  C  C   . GLY A 1 113 ? 1.923   -16.518 1.486   1.00 12.98 ? 113 GLY B C   1 
ATOM   875  O  O   . GLY A 1 113 ? 2.045   -15.618 0.639   1.00 14.14 ? 113 GLY B O   1 
ATOM   876  N  N   . VAL A 1 114 ? 0.727   -17.022 1.837   1.00 13.59 ? 114 VAL B N   1 
ATOM   877  C  CA  . VAL A 1 114 ? -0.565  -16.506 1.201   1.00 15.15 ? 114 VAL B CA  1 
ATOM   878  C  C   . VAL A 1 114 ? -1.061  -15.261 1.960   1.00 14.27 ? 114 VAL B C   1 
ATOM   879  O  O   . VAL A 1 114 ? -1.353  -15.379 3.178   1.00 14.86 ? 114 VAL B O   1 
ATOM   880  C  CB  . VAL A 1 114 ? -1.594  -17.624 1.190   1.00 16.04 ? 114 VAL B CB  1 
ATOM   881  C  CG1 . VAL A 1 114 ? -2.933  -16.971 0.737   1.00 17.47 ? 114 VAL B CG1 1 
ATOM   882  C  CG2 . VAL A 1 114 ? -1.113  -18.787 0.284   1.00 20.06 ? 114 VAL B CG2 1 
ATOM   883  N  N   A SER A 1 115 ? -1.140  -14.193 1.260   0.50 13.41 ? 115 SER B N   1 
ATOM   884  N  N   B SER A 1 115 ? -1.002  -14.090 1.326   0.50 13.15 ? 115 SER B N   1 
ATOM   885  C  CA  A SER A 1 115 ? -1.857  -13.088 1.803   0.50 13.49 ? 115 SER B CA  1 
ATOM   886  C  CA  B SER A 1 115 ? -1.666  -12.811 1.805   0.50 11.50 ? 115 SER B CA  1 
ATOM   887  C  C   A SER A 1 115 ? -3.240  -13.283 1.250   0.50 12.41 ? 115 SER B C   1 
ATOM   888  C  C   B SER A 1 115 ? -3.092  -12.725 1.182   0.50 12.20 ? 115 SER B C   1 
ATOM   889  O  O   A SER A 1 115 ? -3.501  -13.759 0.081   0.50 12.18 ? 115 SER B O   1 
ATOM   890  O  O   B SER A 1 115 ? -3.212  -12.680 -0.069  0.50 10.33 ? 115 SER B O   1 
ATOM   891  C  CB  A SER A 1 115 ? -1.266  -11.807 1.317   0.50 15.50 ? 115 SER B CB  1 
ATOM   892  C  CB  B SER A 1 115 ? -0.864  -11.552 1.502   0.50 13.58 ? 115 SER B CB  1 
ATOM   893  O  OG  A SER A 1 115 ? -0.057  -11.482 1.994   0.50 15.58 ? 115 SER B OG  1 
ATOM   894  O  OG  B SER A 1 115 ? -1.668  -10.407 1.800   0.50 12.08 ? 115 SER B OG  1 
ATOM   895  N  N   . TYR A 1 116 ? -4.167  -12.784 2.041   1.00 10.59 ? 116 TYR B N   1 
ATOM   896  C  CA  . TYR A 1 116 ? -5.543  -12.693 1.569   1.00 11.06 ? 116 TYR B CA  1 
ATOM   897  C  C   . TYR A 1 116 ? -5.876  -11.311 1.106   1.00 9.37  ? 116 TYR B C   1 
ATOM   898  O  O   . TYR A 1 116 ? -5.085  -10.367 1.261   1.00 11.33 ? 116 TYR B O   1 
ATOM   899  C  CB  . TYR A 1 116 ? -6.481  -13.249 2.672   1.00 10.50 ? 116 TYR B CB  1 
ATOM   900  C  CG  . TYR A 1 116 ? -6.259  -14.682 2.870   1.00 10.49 ? 116 TYR B CG  1 
ATOM   901  C  CD1 . TYR A 1 116 ? -6.993  -15.612 2.111   1.00 13.86 ? 116 TYR B CD1 1 
ATOM   902  C  CD2 . TYR A 1 116 ? -5.308  -15.176 3.814   1.00 11.06 ? 116 TYR B CD2 1 
ATOM   903  C  CE1 . TYR A 1 116 ? -6.722  -17.018 2.269   1.00 14.46 ? 116 TYR B CE1 1 
ATOM   904  C  CE2 . TYR A 1 116 ? -5.130  -16.529 3.982   1.00 13.74 ? 116 TYR B CE2 1 
ATOM   905  C  CZ  . TYR A 1 116 ? -5.826  -17.392 3.226   1.00 14.67 ? 116 TYR B CZ  1 
ATOM   906  O  OH  . TYR A 1 116 ? -5.592  -18.814 3.360   1.00 19.01 ? 116 TYR B OH  1 
ATOM   907  N  N   . ALA A 1 117 ? -7.090  -11.150 0.514   1.00 9.81  ? 117 ALA B N   1 
ATOM   908  C  CA  . ALA A 1 117 ? -7.486  -9.801  0.036   1.00 9.95  ? 117 ALA B CA  1 
ATOM   909  C  C   . ALA A 1 117 ? -7.673  -8.774  1.165   1.00 10.17 ? 117 ALA B C   1 
ATOM   910  O  O   . ALA A 1 117 ? -7.497  -7.587  0.970   1.00 9.89  ? 117 ALA B O   1 
ATOM   911  C  CB  . ALA A 1 117 ? -8.712  -9.882  -0.896  1.00 10.42 ? 117 ALA B CB  1 
ATOM   912  N  N   . ALA A 1 118 ? -8.156  -9.256  2.314   1.00 8.15  ? 118 ALA B N   1 
ATOM   913  C  CA  . ALA A 1 118 ? -8.334  -8.331  3.468   1.00 7.68  ? 118 ALA B CA  1 
ATOM   914  C  C   . ALA A 1 118 ? -8.393  -9.233  4.697   1.00 7.56  ? 118 ALA B C   1 
ATOM   915  O  O   . ALA A 1 118 ? -8.391  -10.465 4.642   1.00 7.97  ? 118 ALA B O   1 
ATOM   916  C  CB  . ALA A 1 118 ? -9.658  -7.541  3.246   1.00 9.02  ? 118 ALA B CB  1 
ATOM   917  N  N   . GLU A 1 119 ? -8.497  -8.514  5.824   1.00 7.38  ? 119 GLU B N   1 
ATOM   918  C  CA  . GLU A 1 119 ? -8.552  -9.251  7.123   1.00 7.91  ? 119 GLU B CA  1 
ATOM   919  C  C   . GLU A 1 119 ? -9.444  -8.399  8.088   1.00 8.04  ? 119 GLU B C   1 
ATOM   920  O  O   . GLU A 1 119 ? -9.120  -7.231  8.340   1.00 8.12  ? 119 GLU B O   1 
ATOM   921  C  CB  . GLU A 1 119 ? -7.124  -9.414  7.692   1.00 8.15  ? 119 GLU B CB  1 
ATOM   922  C  CG  . GLU A 1 119 ? -7.117  -10.260 8.970   1.00 8.69  ? 119 GLU B CG  1 
ATOM   923  C  CD  . GLU A 1 119 ? -5.698  -10.536 9.388   1.00 8.90  ? 119 GLU B CD  1 
ATOM   924  O  OE1 . GLU A 1 119 ? -4.801  -10.718 8.541   1.00 9.46  ? 119 GLU B OE1 1 
ATOM   925  O  OE2 . GLU A 1 119 ? -5.473  -10.703 10.628  1.00 9.41  ? 119 GLU B OE2 1 
ATOM   926  N  N   . LEU A 1 120 ? -10.457 -9.051  8.555   1.00 7.31  ? 120 LEU B N   1 
ATOM   927  C  CA  . LEU A 1 120 ? -11.370 -8.460  9.555   1.00 7.41  ? 120 LEU B CA  1 
ATOM   928  C  C   . LEU A 1 120 ? -10.868 -8.760  10.966  1.00 8.38  ? 120 LEU B C   1 
ATOM   929  O  O   . LEU A 1 120 ? -10.495 -9.882  11.256  1.00 8.15  ? 120 LEU B O   1 
ATOM   930  C  CB  . LEU A 1 120 ? -12.727 -9.083  9.371   1.00 9.76  ? 120 LEU B CB  1 
ATOM   931  C  CG  . LEU A 1 120 ? -13.901 -8.406  10.112  1.00 9.74  ? 120 LEU B CG  1 
ATOM   932  C  CD1 . LEU A 1 120 ? -14.366 -7.162  9.336   1.00 10.91 ? 120 LEU B CD1 1 
ATOM   933  C  CD2 . LEU A 1 120 ? -15.008 -9.423  10.335  1.00 13.87 ? 120 LEU B CD2 1 
ATOM   934  N  N   . HIS A 1 121 ? -10.889 -7.729  11.794  1.00 8.10  ? 121 HIS B N   1 
ATOM   935  C  CA  . HIS A 1 121 ? -10.532 -7.910  13.230  1.00 7.89  ? 121 HIS B CA  1 
ATOM   936  C  C   . HIS A 1 121 ? -11.714 -7.545  14.089  1.00 8.45  ? 121 HIS B C   1 
ATOM   937  O  O   . HIS A 1 121 ? -12.349 -6.515  13.977  1.00 9.04  ? 121 HIS B O   1 
ATOM   938  C  CB  . HIS A 1 121 ? -9.382  -6.962  13.598  1.00 8.10  ? 121 HIS B CB  1 
ATOM   939  C  CG  . HIS A 1 121 ? -8.110  -7.439  12.981  1.00 7.48  ? 121 HIS B CG  1 
ATOM   940  N  ND1 . HIS A 1 121 ? -7.004  -6.633  12.808  1.00 8.14  ? 121 HIS B ND1 1 
ATOM   941  C  CD2 . HIS A 1 121 ? -7.789  -8.637  12.431  1.00 7.84  ? 121 HIS B CD2 1 
ATOM   942  C  CE1 . HIS A 1 121 ? -6.009  -7.350  12.252  1.00 9.06  ? 121 HIS B CE1 1 
ATOM   943  N  NE2 . HIS A 1 121 ? -6.478  -8.556  12.010  1.00 8.38  ? 121 HIS B NE2 1 
ATOM   944  N  N   . VAL A 1 122 ? -12.020 -8.494  15.008  1.00 8.43  ? 122 VAL B N   1 
ATOM   945  C  CA  . VAL A 1 122 ? -13.115 -8.378  15.996  1.00 7.73  ? 122 VAL B CA  1 
ATOM   946  C  C   . VAL A 1 122 ? -12.447 -8.221  17.354  1.00 7.85  ? 122 VAL B C   1 
ATOM   947  O  O   . VAL A 1 122 ? -11.799 -9.189  17.838  1.00 8.16  ? 122 VAL B O   1 
ATOM   948  C  CB  . VAL A 1 122 ? -14.017 -9.579  15.930  1.00 7.65  ? 122 VAL B CB  1 
ATOM   949  C  CG1 . VAL A 1 122 ? -15.242 -9.318  16.834  1.00 8.47  ? 122 VAL B CG1 1 
ATOM   950  C  CG2 . VAL A 1 122 ? -14.502 -9.907  14.498  1.00 9.97  ? 122 VAL B CG2 1 
ATOM   951  N  N   . VAL A 1 123 ? -12.530 -7.035  17.977  1.00 7.67  ? 123 VAL B N   1 
ATOM   952  C  CA  . VAL A 1 123 ? -11.714 -6.729  19.160  1.00 8.05  ? 123 VAL B CA  1 
ATOM   953  C  C   . VAL A 1 123 ? -12.608 -6.845  20.425  1.00 8.05  ? 123 VAL B C   1 
ATOM   954  O  O   . VAL A 1 123 ? -13.717 -6.349  20.482  1.00 9.59  ? 123 VAL B O   1 
ATOM   955  C  CB  . VAL A 1 123 ? -11.212 -5.262  19.090  1.00 9.24  ? 123 VAL B CB  1 
ATOM   956  C  CG1 . VAL A 1 123 ? -10.411 -4.847  20.317  1.00 11.31 ? 123 VAL B CG1 1 
ATOM   957  C  CG2 . VAL A 1 123 ? -10.375 -5.018  17.801  1.00 10.73 ? 123 VAL B CG2 1 
ATOM   958  N  N   . HIS A 1 124 ? -12.040 -7.576  21.412  1.00 8.24  ? 124 HIS B N   1 
ATOM   959  C  CA  . HIS A 1 124 ? -12.788 -7.855  22.679  1.00 8.72  ? 124 HIS B CA  1 
ATOM   960  C  C   . HIS A 1 124 ? -11.838 -7.579  23.816  1.00 8.34  ? 124 HIS B C   1 
ATOM   961  O  O   . HIS A 1 124 ? -10.635 -7.650  23.725  1.00 8.89  ? 124 HIS B O   1 
ATOM   962  C  CB  . HIS A 1 124 ? -13.143 -9.352  22.769  1.00 8.76  ? 124 HIS B CB  1 
ATOM   963  C  CG  . HIS A 1 124 ? -13.771 -9.973  21.558  1.00 8.40  ? 124 HIS B CG  1 
ATOM   964  N  ND1 . HIS A 1 124 ? -13.023 -10.268 20.415  1.00 8.84  ? 124 HIS B ND1 1 
ATOM   965  C  CD2 . HIS A 1 124 ? -15.061 -10.457 21.292  1.00 9.05  ? 124 HIS B CD2 1 
ATOM   966  C  CE1 . HIS A 1 124 ? -13.855 -10.887 19.524  1.00 9.71  ? 124 HIS B CE1 1 
ATOM   967  N  NE2 . HIS A 1 124 ? -15.072 -11.013 20.040  1.00 9.06  ? 124 HIS B NE2 1 
ATOM   968  N  N   . TRP A 1 125 ? -12.482 -7.285  25.012  1.00 9.57  ? 125 TRP B N   1 
ATOM   969  C  CA  . TRP A 1 125 ? -11.678 -7.059  26.248  1.00 10.19 ? 125 TRP B CA  1 
ATOM   970  C  C   . TRP A 1 125 ? -12.185 -7.856  27.453  1.00 9.82  ? 125 TRP B C   1 
ATOM   971  O  O   . TRP A 1 125 ? -13.399 -8.120  27.588  1.00 9.22  ? 125 TRP B O   1 
ATOM   972  C  CB  . TRP A 1 125 ? -11.586 -5.567  26.565  1.00 11.16 ? 125 TRP B CB  1 
ATOM   973  C  CG  . TRP A 1 125 ? -12.911 -4.894  26.775  1.00 10.50 ? 125 TRP B CG  1 
ATOM   974  C  CD1 . TRP A 1 125 ? -13.732 -4.362  25.869  1.00 10.94 ? 125 TRP B CD1 1 
ATOM   975  C  CD2 . TRP A 1 125 ? -13.519 -4.558  28.090  1.00 11.77 ? 125 TRP B CD2 1 
ATOM   976  N  NE1 . TRP A 1 125 ? -14.840 -3.767  26.395  1.00 12.46 ? 125 TRP B NE1 1 
ATOM   977  C  CE2 . TRP A 1 125 ? -14.751 -3.922  27.819  1.00 12.07 ? 125 TRP B CE2 1 
ATOM   978  C  CE3 . TRP A 1 125 ? -13.137 -4.824  29.394  1.00 12.03 ? 125 TRP B CE3 1 
ATOM   979  C  CZ2 . TRP A 1 125 ? -15.583 -3.427  28.839  1.00 13.42 ? 125 TRP B CZ2 1 
ATOM   980  C  CZ3 . TRP A 1 125 ? -13.981 -4.372  30.407  1.00 13.98 ? 125 TRP B CZ3 1 
ATOM   981  C  CH2 . TRP A 1 125 ? -15.138 -3.740  30.146  1.00 14.45 ? 125 TRP B CH2 1 
ATOM   982  N  N   . ASN A 1 126 ? -11.210 -8.178  28.305  1.00 10.68 ? 126 ASN B N   1 
ATOM   983  C  CA  . ASN A 1 126 ? -11.465 -9.085  29.457  1.00 11.03 ? 126 ASN B CA  1 
ATOM   984  C  C   . ASN A 1 126 ? -12.201 -8.270  30.587  1.00 9.79  ? 126 ASN B C   1 
ATOM   985  O  O   . ASN A 1 126 ? -11.534 -7.664  31.434  1.00 11.99 ? 126 ASN B O   1 
ATOM   986  C  CB  . ASN A 1 126 ? -10.171 -9.578  29.888  1.00 11.31 ? 126 ASN B CB  1 
ATOM   987  C  CG  . ASN A 1 126 ? -10.268 -10.598 31.020  1.00 12.24 ? 126 ASN B CG  1 
ATOM   988  O  OD1 . ASN A 1 126 ? -11.328 -10.733 31.644  1.00 12.72 ? 126 ASN B OD1 1 
ATOM   989  N  ND2 . ASN A 1 126 ? -9.191  -11.349 31.203  1.00 14.89 ? 126 ASN B ND2 1 
ATOM   990  N  N   . SER A 1 127 ? -13.540 -8.364  30.588  1.00 10.83 ? 127 SER B N   1 
ATOM   991  C  CA  . SER A 1 127 ? -14.323 -7.681  31.646  1.00 11.72 ? 127 SER B CA  1 
ATOM   992  C  C   . SER A 1 127 ? -14.384 -8.529  32.897  1.00 13.09 ? 127 SER B C   1 
ATOM   993  O  O   . SER A 1 127 ? -14.917 -7.970  33.874  1.00 14.09 ? 127 SER B O   1 
ATOM   994  C  CB  . SER A 1 127 ? -15.699 -7.320  31.136  1.00 12.19 ? 127 SER B CB  1 
ATOM   995  O  OG  . SER A 1 127 ? -16.455 -8.474  30.786  1.00 15.32 ? 127 SER B OG  1 
ATOM   996  N  N   . ASP A 1 128 ? -13.931 -9.774  32.905  1.00 12.39 ? 128 ASP B N   1 
ATOM   997  C  CA  . ASP A 1 128 ? -13.915 -10.572 34.170  1.00 13.27 ? 128 ASP B CA  1 
ATOM   998  C  C   . ASP A 1 128 ? -12.731 -10.101 34.996  1.00 14.33 ? 128 ASP B C   1 
ATOM   999  O  O   . ASP A 1 128 ? -12.705 -10.371 36.210  1.00 17.69 ? 128 ASP B O   1 
ATOM   1000 C  CB  . ASP A 1 128 ? -13.721 -12.046 33.876  1.00 13.94 ? 128 ASP B CB  1 
ATOM   1001 C  CG  . ASP A 1 128 ? -14.962 -12.752 33.376  1.00 14.37 ? 128 ASP B CG  1 
ATOM   1002 O  OD1 . ASP A 1 128 ? -14.814 -13.962 32.900  1.00 17.75 ? 128 ASP B OD1 1 
ATOM   1003 O  OD2 . ASP A 1 128 ? -16.107 -12.213 33.431  1.00 21.40 ? 128 ASP B OD2 1 
ATOM   1004 N  N   . LYS A 1 129 ? -11.731 -9.444  34.473  1.00 13.47 ? 129 LYS B N   1 
ATOM   1005 C  CA  . LYS A 1 129 ? -10.582 -9.021  35.258  1.00 14.84 ? 129 LYS B CA  1 
ATOM   1006 C  C   . LYS A 1 129 ? -10.404 -7.539  35.312  1.00 13.61 ? 129 LYS B C   1 
ATOM   1007 O  O   . LYS A 1 129 ? -9.692  -7.003  36.172  1.00 15.26 ? 129 LYS B O   1 
ATOM   1008 C  CB  . LYS A 1 129 ? -9.251  -9.633  34.764  1.00 16.34 ? 129 LYS B CB  1 
ATOM   1009 C  CG  . LYS A 1 129 ? -9.086  -11.117 35.172  1.00 22.36 ? 129 LYS B CG  1 
ATOM   1010 C  CD  . LYS A 1 129 ? -7.656  -11.624 34.900  1.00 20.69 ? 129 LYS B CD  1 
ATOM   1011 C  CE  . LYS A 1 129 ? -6.578  -10.879 35.663  1.00 23.65 ? 129 LYS B CE  1 
ATOM   1012 N  NZ  . LYS A 1 129 ? -5.116  -11.240 35.371  1.00 24.79 ? 129 LYS B NZ  1 
ATOM   1013 N  N   . TYR A 1 130 ? -10.925 -6.800  34.313  1.00 12.45 ? 130 TYR B N   1 
ATOM   1014 C  CA  . TYR A 1 130 ? -10.705 -5.378  34.169  1.00 11.69 ? 130 TYR B CA  1 
ATOM   1015 C  C   . TYR A 1 130 ? -11.949 -4.647  34.056  1.00 12.08 ? 130 TYR B C   1 
ATOM   1016 O  O   . TYR A 1 130 ? -12.990 -5.166  33.610  1.00 12.94 ? 130 TYR B O   1 
ATOM   1017 C  CB  . TYR A 1 130 ? -9.761  -5.062  32.889  1.00 13.54 ? 130 TYR B CB  1 
ATOM   1018 C  CG  . TYR A 1 130 ? -8.475  -5.872  32.999  1.00 13.05 ? 130 TYR B CG  1 
ATOM   1019 C  CD1 . TYR A 1 130 ? -7.520  -5.545  33.953  1.00 14.55 ? 130 TYR B CD1 1 
ATOM   1020 C  CD2 . TYR A 1 130 ? -8.259  -7.006  32.226  1.00 12.47 ? 130 TYR B CD2 1 
ATOM   1021 C  CE1 . TYR A 1 130 ? -6.363  -6.304  34.112  1.00 15.53 ? 130 TYR B CE1 1 
ATOM   1022 C  CE2 . TYR A 1 130 ? -7.104  -7.780  32.379  1.00 13.27 ? 130 TYR B CE2 1 
ATOM   1023 C  CZ  . TYR A 1 130 ? -6.162  -7.428  33.323  1.00 16.49 ? 130 TYR B CZ  1 
ATOM   1024 O  OH  . TYR A 1 130 ? -5.019  -8.191  33.454  1.00 17.69 ? 130 TYR B OH  1 
ATOM   1025 N  N   . PRO A 1 131 ? -11.933 -3.361  34.482  1.00 13.03 ? 131 PRO B N   1 
ATOM   1026 C  CA  . PRO A 1 131 ? -13.176 -2.653  34.586  1.00 12.75 ? 131 PRO B CA  1 
ATOM   1027 C  C   . PRO A 1 131 ? -13.600 -1.953  33.239  1.00 13.66 ? 131 PRO B C   1 
ATOM   1028 O  O   . PRO A 1 131 ? -14.735 -1.423  33.136  1.00 14.78 ? 131 PRO B O   1 
ATOM   1029 C  CB  . PRO A 1 131 ? -12.903 -1.540  35.673  1.00 15.66 ? 131 PRO B CB  1 
ATOM   1030 C  CG  . PRO A 1 131 ? -11.406 -1.391  35.591  1.00 14.35 ? 131 PRO B CG  1 
ATOM   1031 C  CD  . PRO A 1 131 ? -10.855 -2.762  35.323  1.00 12.42 ? 131 PRO B CD  1 
ATOM   1032 N  N   . SER A 1 132 ? -12.607 -1.859  32.323  1.00 13.47 ? 132 SER B N   1 
ATOM   1033 C  CA  . SER A 1 132 ? -12.903 -1.103  31.106  1.00 15.91 ? 132 SER B CA  1 
ATOM   1034 C  C   . SER A 1 132 ? -11.894 -1.600  30.086  1.00 13.16 ? 132 SER B C   1 
ATOM   1035 O  O   . SER A 1 132 ? -10.827 -2.131  30.350  1.00 11.86 ? 132 SER B O   1 
ATOM   1036 C  CB  . SER A 1 132 ? -12.600 0.390   31.355  1.00 14.94 ? 132 SER B CB  1 
ATOM   1037 O  OG  . SER A 1 132 ? -11.218 0.576   31.575  1.00 18.91 ? 132 SER B OG  1 
ATOM   1038 N  N   . PHE A 1 133 ? -12.266 -1.317  28.814  1.00 13.19 ? 133 PHE B N   1 
ATOM   1039 C  CA  . PHE A 1 133 ? -11.339 -1.572  27.704  1.00 13.20 ? 133 PHE B CA  1 
ATOM   1040 C  C   . PHE A 1 133 ? -9.983  -0.889  27.869  1.00 13.05 ? 133 PHE B C   1 
ATOM   1041 O  O   . PHE A 1 133 ? -8.965  -1.485  27.662  1.00 14.33 ? 133 PHE B O   1 
ATOM   1042 C  CB  . PHE A 1 133 ? -11.960 -1.041  26.411  1.00 15.05 ? 133 PHE B CB  1 
ATOM   1043 C  CG  . PHE A 1 133 ? -11.028 -1.095  25.203  1.00 16.46 ? 133 PHE B CG  1 
ATOM   1044 C  CD1 . PHE A 1 133 ? -10.702 -2.283  24.567  1.00 17.91 ? 133 PHE B CD1 1 
ATOM   1045 C  CD2 . PHE A 1 133 ? -10.387 0.081   24.806  1.00 17.74 ? 133 PHE B CD2 1 
ATOM   1046 C  CE1 . PHE A 1 133 ? -9.813  -2.275  23.482  1.00 19.75 ? 133 PHE B CE1 1 
ATOM   1047 C  CE2 . PHE A 1 133 ? -9.481  0.091   23.723  1.00 19.61 ? 133 PHE B CE2 1 
ATOM   1048 C  CZ  . PHE A 1 133 ? -9.183  -1.103  23.151  1.00 20.00 ? 133 PHE B CZ  1 
ATOM   1049 N  N   . VAL A 1 134 ? -9.997  0.389   28.321  1.00 14.42 ? 134 VAL B N   1 
ATOM   1050 C  CA  . VAL A 1 134 ? -8.756  1.106   28.411  1.00 17.98 ? 134 VAL B CA  1 
ATOM   1051 C  C   . VAL A 1 134 ? -7.785  0.448   29.391  1.00 16.25 ? 134 VAL B C   1 
ATOM   1052 O  O   . VAL A 1 134 ? -6.560  0.329   29.168  1.00 18.78 ? 134 VAL B O   1 
ATOM   1053 C  CB  . VAL A 1 134 ? -9.057  2.590   28.755  1.00 23.02 ? 134 VAL B CB  1 
ATOM   1054 C  CG1 . VAL A 1 134 ? -7.759  3.345   29.124  1.00 26.77 ? 134 VAL B CG1 1 
ATOM   1055 C  CG2 . VAL A 1 134 ? -9.727  3.341   27.585  1.00 27.07 ? 134 VAL B CG2 1 
ATOM   1056 N  N   . GLU A 1 135 ? -8.318  -0.090  30.537  1.00 13.92 ? 135 GLU B N   1 
ATOM   1057 C  CA  . GLU A 1 135 ? -7.431  -0.817  31.435  1.00 16.30 ? 135 GLU B CA  1 
ATOM   1058 C  C   . GLU A 1 135 ? -6.908  -2.169  30.922  1.00 15.62 ? 135 GLU B C   1 
ATOM   1059 O  O   . GLU A 1 135 ? -5.747  -2.583  31.013  1.00 16.10 ? 135 GLU B O   1 
ATOM   1060 C  CB  . GLU A 1 135 ? -8.159  -1.076  32.815  1.00 15.97 ? 135 GLU B CB  1 
ATOM   1061 C  CG  . GLU A 1 135 ? -8.398  0.292   33.589  1.00 18.57 ? 135 GLU B CG  1 
ATOM   1062 C  CD  . GLU A 1 135 ? -7.125  0.996   34.091  1.00 23.25 ? 135 GLU B CD  1 
ATOM   1063 O  OE1 . GLU A 1 135 ? -7.301  2.110   34.639  1.00 26.97 ? 135 GLU B OE1 1 
ATOM   1064 O  OE2 . GLU A 1 135 ? -6.048  0.419   34.020  1.00 21.12 ? 135 GLU B OE2 1 
ATOM   1065 N  N   . ALA A 1 136 ? -7.872  -2.868  30.313  1.00 13.23 ? 136 ALA B N   1 
ATOM   1066 C  CA  . ALA A 1 136 ? -7.535  -4.159  29.708  1.00 13.02 ? 136 ALA B CA  1 
ATOM   1067 C  C   . ALA A 1 136 ? -6.426  -4.040  28.578  1.00 13.22 ? 136 ALA B C   1 
ATOM   1068 O  O   . ALA A 1 136 ? -5.644  -4.949  28.451  1.00 13.87 ? 136 ALA B O   1 
ATOM   1069 C  CB  . ALA A 1 136 ? -8.792  -4.774  29.097  1.00 13.09 ? 136 ALA B CB  1 
ATOM   1070 N  N   . ALA A 1 137 ? -6.480  -2.947  27.877  1.00 14.32 ? 137 ALA B N   1 
ATOM   1071 C  CA  . ALA A 1 137 ? -5.566  -2.777  26.746  1.00 14.92 ? 137 ALA B CA  1 
ATOM   1072 C  C   . ALA A 1 137 ? -4.088  -2.739  27.118  1.00 15.21 ? 137 ALA B C   1 
ATOM   1073 O  O   . ALA A 1 137 ? -3.217  -2.927  26.244  1.00 15.05 ? 137 ALA B O   1 
ATOM   1074 C  CB  . ALA A 1 137 ? -5.958  -1.560  25.938  1.00 13.39 ? 137 ALA B CB  1 
ATOM   1075 N  N   . HIS A 1 138 ? -3.824  -2.597  28.429  1.00 16.10 ? 138 HIS B N   1 
ATOM   1076 C  CA  . HIS A 1 138 ? -2.465  -2.536  28.930  1.00 18.79 ? 138 HIS B CA  1 
ATOM   1077 C  C   . HIS A 1 138 ? -2.023  -3.723  29.663  1.00 19.34 ? 138 HIS B C   1 
ATOM   1078 O  O   . HIS A 1 138 ? -0.978  -3.629  30.350  1.00 22.76 ? 138 HIS B O   1 
ATOM   1079 C  CB  . HIS A 1 138 ? -2.331  -1.270  29.841  1.00 19.67 ? 138 HIS B CB  1 
ATOM   1080 C  CG  . HIS A 1 138 ? -2.413  0.045   29.072  1.00 20.92 ? 138 HIS B CG  1 
ATOM   1081 N  ND1 . HIS A 1 138 ? -1.275  0.640   28.571  1.00 24.67 ? 138 HIS B ND1 1 
ATOM   1082 C  CD2 . HIS A 1 138 ? -3.491  0.803   28.628  1.00 23.52 ? 138 HIS B CD2 1 
ATOM   1083 C  CE1 . HIS A 1 138 ? -1.646  1.756   27.892  1.00 24.63 ? 138 HIS B CE1 1 
ATOM   1084 N  NE2 . HIS A 1 138 ? -2.968  1.883   27.949  1.00 23.32 ? 138 HIS B NE2 1 
ATOM   1085 N  N   . GLU A 1 139 ? -2.700  -4.895  29.540  1.00 16.38 ? 139 GLU B N   1 
ATOM   1086 C  CA  . GLU A 1 139 ? -2.310  -6.019  30.211  1.00 17.36 ? 139 GLU B CA  1 
ATOM   1087 C  C   . GLU A 1 139 ? -2.182  -7.220  29.306  1.00 15.90 ? 139 GLU B C   1 
ATOM   1088 O  O   . GLU A 1 139 ? -2.956  -7.341  28.344  1.00 13.75 ? 139 GLU B O   1 
ATOM   1089 C  CB  . GLU A 1 139 ? -3.384  -6.365  31.308  1.00 22.59 ? 139 GLU B CB  1 
ATOM   1090 C  CG  . GLU A 1 139 ? -3.408  -5.503  32.617  1.00 28.13 ? 139 GLU B CG  1 
ATOM   1091 C  CD  . GLU A 1 139 ? -2.006  -5.192  33.165  1.00 31.82 ? 139 GLU B CD  1 
ATOM   1092 O  OE1 . GLU A 1 139 ? -1.110  -6.047  33.175  1.00 34.58 ? 139 GLU B OE1 1 
ATOM   1093 O  OE2 . GLU A 1 139 ? -1.760  -4.030  33.537  1.00 48.61 ? 139 GLU B OE2 1 
ATOM   1094 N  N   . PRO A 1 140 ? -1.328  -8.169  29.590  1.00 15.16 ? 140 PRO B N   1 
ATOM   1095 C  CA  . PRO A 1 140 ? -1.070  -9.259  28.614  1.00 14.93 ? 140 PRO B CA  1 
ATOM   1096 C  C   . PRO A 1 140 ? -2.293  -10.089 28.302  1.00 14.25 ? 140 PRO B C   1 
ATOM   1097 O  O   . PRO A 1 140 ? -2.423  -10.677 27.201  1.00 13.57 ? 140 PRO B O   1 
ATOM   1098 C  CB  . PRO A 1 140 ? 0.047   -10.087 29.277  1.00 15.66 ? 140 PRO B CB  1 
ATOM   1099 C  CG  . PRO A 1 140 ? 0.845   -8.990  29.982  1.00 21.74 ? 140 PRO B CG  1 
ATOM   1100 C  CD  . PRO A 1 140 ? -0.237  -8.151  30.638  1.00 16.81 ? 140 PRO B CD  1 
ATOM   1101 N  N   . ASP A 1 141 ? -3.205  -10.206 29.253  1.00 11.92 ? 141 ASP B N   1 
ATOM   1102 C  CA  . ASP A 1 141 ? -4.407  -11.013 29.138  1.00 12.67 ? 141 ASP B CA  1 
ATOM   1103 C  C   . ASP A 1 141 ? -5.614  -10.105 28.883  1.00 12.74 ? 141 ASP B C   1 
ATOM   1104 O  O   . ASP A 1 141 ? -6.753  -10.570 29.050  1.00 13.00 ? 141 ASP B O   1 
ATOM   1105 C  CB  . ASP A 1 141 ? -4.654  -11.911 30.408  1.00 15.58 ? 141 ASP B CB  1 
ATOM   1106 C  CG  . ASP A 1 141 ? -4.830  -11.097 31.673  1.00 14.83 ? 141 ASP B CG  1 
ATOM   1107 O  OD1 . ASP A 1 141 ? -4.542  -9.879  31.645  1.00 15.73 ? 141 ASP B OD1 1 
ATOM   1108 O  OD2 . ASP A 1 141 ? -5.250  -11.670 32.697  1.00 18.65 ? 141 ASP B OD2 1 
ATOM   1109 N  N   . GLY A 1 142 ? -5.380  -8.854  28.514  1.00 10.99 ? 142 GLY B N   1 
ATOM   1110 C  CA  . GLY A 1 142 ? -6.475  -7.922  28.488  1.00 11.06 ? 142 GLY B CA  1 
ATOM   1111 C  C   . GLY A 1 142 ? -7.415  -8.031  27.249  1.00 10.23 ? 142 GLY B C   1 
ATOM   1112 O  O   . GLY A 1 142 ? -8.636  -7.808  27.360  1.00 11.18 ? 142 GLY B O   1 
ATOM   1113 N  N   . LEU A 1 143 ? -6.806  -8.236  26.049  1.00 10.56 ? 143 LEU B N   1 
ATOM   1114 C  CA  . LEU A 1 143 ? -7.635  -8.150  24.831  1.00 10.79 ? 143 LEU B CA  1 
ATOM   1115 C  C   . LEU A 1 143 ? -7.542  -9.499  24.127  1.00 10.11 ? 143 LEU B C   1 
ATOM   1116 O  O   . LEU A 1 143 ? -6.616  -10.290 24.192  1.00 10.06 ? 143 LEU B O   1 
ATOM   1117 C  CB  . LEU A 1 143 ? -7.034  -7.090  23.844  1.00 10.85 ? 143 LEU B CB  1 
ATOM   1118 C  CG  . LEU A 1 143 ? -6.960  -5.711  24.478  1.00 12.14 ? 143 LEU B CG  1 
ATOM   1119 C  CD1 . LEU A 1 143 ? -6.450  -4.656  23.383  1.00 12.94 ? 143 LEU B CD1 1 
ATOM   1120 C  CD2 . LEU A 1 143 ? -8.308  -5.186  25.001  1.00 11.78 ? 143 LEU B CD2 1 
ATOM   1121 N  N   . ALA A 1 144 ? -8.637  -9.743  23.313  1.00 10.01 ? 144 ALA B N   1 
ATOM   1122 C  CA  . ALA A 1 144 ? -8.673  -10.929 22.403  1.00 9.36  ? 144 ALA B CA  1 
ATOM   1123 C  C   . ALA A 1 144 ? -9.162  -10.399 21.079  1.00 8.08  ? 144 ALA B C   1 
ATOM   1124 O  O   . ALA A 1 144 ? -10.189 -9.709  21.052  1.00 9.51  ? 144 ALA B O   1 
ATOM   1125 C  CB  . ALA A 1 144 ? -9.617  -12.038 22.922  1.00 9.91  ? 144 ALA B CB  1 
ATOM   1126 N  N   . VAL A 1 145 ? -8.453  -10.772 19.994  1.00 8.43  ? 145 VAL B N   1 
ATOM   1127 C  CA  . VAL A 1 145 ? -8.885  -10.349 18.650  1.00 8.90  ? 145 VAL B CA  1 
ATOM   1128 C  C   . VAL A 1 145 ? -9.084  -11.624 17.829  1.00 8.27  ? 145 VAL B C   1 
ATOM   1129 O  O   . VAL A 1 145 ? -8.207  -12.454 17.717  1.00 9.51  ? 145 VAL B O   1 
ATOM   1130 C  CB  . VAL A 1 145 ? -7.841  -9.409  17.985  1.00 9.74  ? 145 VAL B CB  1 
ATOM   1131 C  CG1 . VAL A 1 145 ? -8.424  -8.968  16.590  1.00 11.75 ? 145 VAL B CG1 1 
ATOM   1132 C  CG2 . VAL A 1 145 ? -7.690  -8.137  18.862  1.00 11.26 ? 145 VAL B CG2 1 
ATOM   1133 N  N   . LEU A 1 146 ? -10.296 -11.670 17.267  1.00 8.19  ? 146 LEU B N   1 
ATOM   1134 C  CA  . LEU A 1 146 ? -10.616 -12.678 16.267  1.00 8.65  ? 146 LEU B CA  1 
ATOM   1135 C  C   . LEU A 1 146 ? -10.298 -12.184 14.878  1.00 10.00 ? 146 LEU B C   1 
ATOM   1136 O  O   . LEU A 1 146 ? -10.859 -11.076 14.528  1.00 10.37 ? 146 LEU B O   1 
ATOM   1137 C  CB  . LEU A 1 146 ? -12.119 -13.090 16.380  1.00 10.76 ? 146 LEU B CB  1 
ATOM   1138 C  CG  . LEU A 1 146 ? -12.620 -14.175 15.510  1.00 11.83 ? 146 LEU B CG  1 
ATOM   1139 C  CD1 . LEU A 1 146 ? -12.013 -15.552 15.826  1.00 14.47 ? 146 LEU B CD1 1 
ATOM   1140 C  CD2 . LEU A 1 146 ? -14.161 -14.216 15.652  1.00 13.61 ? 146 LEU B CD2 1 
ATOM   1141 N  N   . GLY A 1 147 ? -9.398  -12.825 14.150  1.00 8.90  ? 147 GLY B N   1 
ATOM   1142 C  CA  . GLY A 1 147 ? -9.073  -12.359 12.808  1.00 8.48  ? 147 GLY B CA  1 
ATOM   1143 C  C   . GLY A 1 147 ? -9.733  -13.288 11.824  1.00 9.39  ? 147 GLY B C   1 
ATOM   1144 O  O   . GLY A 1 147 ? -9.667  -14.559 11.953  1.00 9.12  ? 147 GLY B O   1 
ATOM   1145 N  N   . VAL A 1 148 ? -10.349 -12.705 10.784  1.00 8.36  ? 148 VAL B N   1 
ATOM   1146 C  CA  . VAL A 1 148 ? -11.019 -13.463 9.752   1.00 8.55  ? 148 VAL B CA  1 
ATOM   1147 C  C   . VAL A 1 148 ? -10.485 -12.970 8.414   1.00 8.01  ? 148 VAL B C   1 
ATOM   1148 O  O   . VAL A 1 148 ? -10.611 -11.752 8.091   1.00 8.10  ? 148 VAL B O   1 
ATOM   1149 C  CB  . VAL A 1 148 ? -12.533 -13.216 9.793   1.00 8.11  ? 148 VAL B CB  1 
ATOM   1150 C  CG1 . VAL A 1 148 ? -13.273 -14.122 8.784   1.00 9.81  ? 148 VAL B CG1 1 
ATOM   1151 C  CG2 . VAL A 1 148 ? -13.092 -13.499 11.266  1.00 11.17 ? 148 VAL B CG2 1 
ATOM   1152 N  N   . PHE A 1 149 ? -9.973  -13.881 7.568   1.00 7.80  ? 149 PHE B N   1 
ATOM   1153 C  CA  . PHE A 1 149 ? -9.514  -13.511 6.233   1.00 8.01  ? 149 PHE B CA  1 
ATOM   1154 C  C   . PHE A 1 149 ? -10.682 -13.330 5.327   1.00 8.71  ? 149 PHE B C   1 
ATOM   1155 O  O   . PHE A 1 149 ? -11.715 -14.043 5.430   1.00 9.51  ? 149 PHE B O   1 
ATOM   1156 C  CB  . PHE A 1 149 ? -8.597  -14.659 5.687   1.00 8.33  ? 149 PHE B CB  1 
ATOM   1157 C  CG  . PHE A 1 149 ? -7.314  -14.824 6.528   1.00 8.05  ? 149 PHE B CG  1 
ATOM   1158 C  CD1 . PHE A 1 149 ? -6.449  -13.778 6.688   1.00 8.75  ? 149 PHE B CD1 1 
ATOM   1159 C  CD2 . PHE A 1 149 ? -7.027  -16.070 7.100   1.00 9.31  ? 149 PHE B CD2 1 
ATOM   1160 C  CE1 . PHE A 1 149 ? -5.274  -13.971 7.411   1.00 10.12 ? 149 PHE B CE1 1 
ATOM   1161 C  CE2 . PHE A 1 149 ? -5.829  -16.217 7.806   1.00 9.20  ? 149 PHE B CE2 1 
ATOM   1162 C  CZ  . PHE A 1 149 ? -4.968  -15.222 7.973   1.00 9.04  ? 149 PHE B CZ  1 
ATOM   1163 N  N   . LEU A 1 150 ? -10.468 -12.434 4.364   1.00 8.23  ? 150 LEU B N   1 
ATOM   1164 C  CA  . LEU A 1 150 ? -11.437 -12.244 3.198   1.00 9.01  ? 150 LEU B CA  1 
ATOM   1165 C  C   . LEU A 1 150 ? -10.727 -12.609 1.921   1.00 9.01  ? 150 LEU B C   1 
ATOM   1166 O  O   . LEU A 1 150 ? -9.620  -12.110 1.691   1.00 9.26  ? 150 LEU B O   1 
ATOM   1167 C  CB  . LEU A 1 150 ? -11.911 -10.792 3.133   1.00 9.06  ? 150 LEU B CB  1 
ATOM   1168 C  CG  . LEU A 1 150 ? -12.955 -10.411 4.151   1.00 11.05 ? 150 LEU B CG  1 
ATOM   1169 C  CD1 . LEU A 1 150 ? -12.470 -10.366 5.617   1.00 11.48 ? 150 LEU B CD1 1 
ATOM   1170 C  CD2 . LEU A 1 150 ? -13.506 -8.972  3.762   1.00 10.15 ? 150 LEU B CD2 1 
ATOM   1171 N  N   . GLN A 1 151 ? -11.358 -13.399 1.061   1.00 10.77 ? 151 GLN B N   1 
ATOM   1172 C  CA  . GLN A 1 151 ? -10.876 -13.686 -0.275  1.00 11.06 ? 151 GLN B CA  1 
ATOM   1173 C  C   . GLN A 1 151 ? -11.903 -13.178 -1.266  1.00 10.25 ? 151 GLN B C   1 
ATOM   1174 O  O   . GLN A 1 151 ? -13.100 -13.039 -0.938  1.00 11.42 ? 151 GLN B O   1 
ATOM   1175 C  CB  . GLN A 1 151 ? -10.624 -15.164 -0.410  1.00 16.79 ? 151 GLN B CB  1 
ATOM   1176 C  CG  . GLN A 1 151 ? -11.810 -15.989 -0.307  1.00 16.64 ? 151 GLN B CG  1 
ATOM   1177 C  CD  . GLN A 1 151 ? -11.502 -17.461 -0.444  1.00 20.18 ? 151 GLN B CD  1 
ATOM   1178 O  OE1 . GLN A 1 151 ? -10.326 -17.863 -0.462  1.00 25.12 ? 151 GLN B OE1 1 
ATOM   1179 N  NE2 . GLN A 1 151 ? -12.569 -18.238 -0.563  1.00 23.52 ? 151 GLN B NE2 1 
ATOM   1180 N  N   . ILE A 1 152 ? -11.490 -12.871 -2.514  1.00 11.64 ? 152 ILE B N   1 
ATOM   1181 C  CA  . ILE A 1 152 ? -12.436 -12.383 -3.508  1.00 11.74 ? 152 ILE B CA  1 
ATOM   1182 C  C   . ILE A 1 152 ? -13.348 -13.535 -3.967  1.00 11.87 ? 152 ILE B C   1 
ATOM   1183 O  O   . ILE A 1 152 ? -12.817 -14.674 -4.235  1.00 14.98 ? 152 ILE B O   1 
ATOM   1184 C  CB  . ILE A 1 152 ? -11.648 -11.794 -4.712  1.00 13.00 ? 152 ILE B CB  1 
ATOM   1185 C  CG1 . ILE A 1 152 ? -10.758 -10.605 -4.255  1.00 13.46 ? 152 ILE B CG1 1 
ATOM   1186 C  CG2 . ILE A 1 152 ? -12.638 -11.377 -5.822  1.00 14.34 ? 152 ILE B CG2 1 
ATOM   1187 C  CD1 . ILE A 1 152 ? -11.544 -9.490  -3.573  1.00 14.12 ? 152 ILE B CD1 1 
ATOM   1188 N  N   . GLY A 1 153 ? -14.641 -13.254 -3.964  1.00 11.08 ? 153 GLY B N   1 
ATOM   1189 C  CA  . GLY A 1 153 ? -15.580 -14.292 -4.432  1.00 14.18 ? 153 GLY B CA  1 
ATOM   1190 C  C   . GLY A 1 153 ? -16.884 -13.627 -4.577  1.00 13.29 ? 153 GLY B C   1 
ATOM   1191 O  O   . GLY A 1 153 ? -16.928 -12.464 -5.119  1.00 16.63 ? 153 GLY B O   1 
ATOM   1192 N  N   . GLU A 1 154 ? -17.925 -14.338 -4.216  1.00 13.36 ? 154 GLU B N   1 
ATOM   1193 C  CA  . GLU A 1 154 ? -19.253 -13.806 -4.387  1.00 15.52 ? 154 GLU B CA  1 
ATOM   1194 C  C   . GLU A 1 154 ? -19.433 -12.603 -3.458  1.00 14.29 ? 154 GLU B C   1 
ATOM   1195 O  O   . GLU A 1 154 ? -18.805 -12.549 -2.332  1.00 14.67 ? 154 GLU B O   1 
ATOM   1196 C  CB  . GLU A 1 154 ? -20.236 -14.886 -3.889  1.00 18.30 ? 154 GLU B CB  1 
ATOM   1197 C  CG  . GLU A 1 154 ? -21.625 -14.636 -3.174  1.00 24.49 ? 154 GLU B CG  1 
ATOM   1198 C  CD  . GLU A 1 154 ? -22.595 -15.883 -3.051  1.00 28.52 ? 154 GLU B CD  1 
ATOM   1199 O  OE1 . GLU A 1 154 ? -22.964 -16.502 -4.113  1.00 27.79 ? 154 GLU B OE1 1 
ATOM   1200 O  OE2 . GLU A 1 154 ? -23.041 -16.258 -1.919  1.00 26.45 ? 154 GLU B OE2 1 
ATOM   1201 N  N   . PRO A 1 155 ? -20.275 -11.651 -3.770  1.00 13.33 ? 155 PRO B N   1 
ATOM   1202 C  CA  . PRO A 1 155 ? -20.520 -10.522 -2.905  1.00 12.15 ? 155 PRO B CA  1 
ATOM   1203 C  C   . PRO A 1 155 ? -21.055 -11.079 -1.601  1.00 11.55 ? 155 PRO B C   1 
ATOM   1204 O  O   . PRO A 1 155 ? -21.786 -12.053 -1.545  1.00 14.08 ? 155 PRO B O   1 
ATOM   1205 C  CB  . PRO A 1 155 ? -21.643 -9.696  -3.629  1.00 13.80 ? 155 PRO B CB  1 
ATOM   1206 C  CG  . PRO A 1 155 ? -21.511 -10.118 -5.057  1.00 13.62 ? 155 PRO B CG  1 
ATOM   1207 C  CD  . PRO A 1 155 ? -20.981 -11.492 -5.106  1.00 13.01 ? 155 PRO B CD  1 
ATOM   1208 N  N   . ASN A 1 156 ? -20.763 -10.335 -0.544  1.00 11.64 ? 156 ASN B N   1 
ATOM   1209 C  CA  . ASN A 1 156 ? -21.203 -10.733 0.809   1.00 11.82 ? 156 ASN B CA  1 
ATOM   1210 C  C   . ASN A 1 156 ? -22.338 -9.810  1.254   1.00 11.59 ? 156 ASN B C   1 
ATOM   1211 O  O   . ASN A 1 156 ? -22.142 -8.611  1.383   1.00 11.04 ? 156 ASN B O   1 
ATOM   1212 C  CB  . ASN A 1 156 ? -19.965 -10.645 1.727   1.00 12.98 ? 156 ASN B CB  1 
ATOM   1213 C  CG  . ASN A 1 156 ? -20.203 -11.239 3.018   1.00 15.23 ? 156 ASN B CG  1 
ATOM   1214 O  OD1 . ASN A 1 156 ? -21.133 -10.779 3.794   1.00 16.21 ? 156 ASN B OD1 1 
ATOM   1215 N  ND2 . ASN A 1 156 ? -19.318 -12.180 3.402   1.00 13.65 ? 156 ASN B ND2 1 
ATOM   1216 N  N   . SER A 1 157 ? -23.522 -10.417 1.477   1.00 13.35 ? 157 SER B N   1 
ATOM   1217 C  CA  . SER A 1 157 ? -24.683 -9.564  1.816   1.00 14.30 ? 157 SER B CA  1 
ATOM   1218 C  C   . SER A 1 157 ? -24.528 -8.819  3.120   1.00 14.37 ? 157 SER B C   1 
ATOM   1219 O  O   . SER A 1 157 ? -25.005 -7.666  3.257   1.00 17.78 ? 157 SER B O   1 
ATOM   1220 C  CB  . SER A 1 157 ? -26.007 -10.442 1.816   1.00 16.85 ? 157 SER B CB  1 
ATOM   1221 O  OG  . SER A 1 157 ? -25.901 -11.485 2.760   1.00 22.00 ? 157 SER B OG  1 
ATOM   1222 N  N   A GLN A 1 158 ? -23.877 -9.403  4.131   0.50 14.70 ? 158 GLN B N   1 
ATOM   1223 N  N   B GLN A 1 158 ? -23.816 -9.385  4.047   0.50 13.60 ? 158 GLN B N   1 
ATOM   1224 C  CA  A GLN A 1 158 ? -23.666 -8.618  5.396   0.50 14.53 ? 158 GLN B CA  1 
ATOM   1225 C  CA  B GLN A 1 158 ? -23.606 -8.712  5.311   0.50 13.25 ? 158 GLN B CA  1 
ATOM   1226 C  C   A GLN A 1 158 ? -22.666 -7.487  5.160   0.50 14.79 ? 158 GLN B C   1 
ATOM   1227 C  C   B GLN A 1 158 ? -22.578 -7.568  5.238   0.50 13.79 ? 158 GLN B C   1 
ATOM   1228 O  O   A GLN A 1 158 ? -22.922 -6.349  5.633   0.50 14.63 ? 158 GLN B O   1 
ATOM   1229 O  O   B GLN A 1 158 ? -22.733 -6.483  5.827   0.50 14.34 ? 158 GLN B O   1 
ATOM   1230 C  CB  A GLN A 1 158 ? -23.163 -9.403  6.649   0.50 15.76 ? 158 GLN B CB  1 
ATOM   1231 C  CB  B GLN A 1 158 ? -23.165 -9.796  6.248   0.50 13.01 ? 158 GLN B CB  1 
ATOM   1232 C  CG  A GLN A 1 158 ? -24.134 -10.210 7.528   0.50 18.68 ? 158 GLN B CG  1 
ATOM   1233 C  CG  B GLN A 1 158 ? -24.355 -10.719 6.521   0.50 13.01 ? 158 GLN B CG  1 
ATOM   1234 C  CD  A GLN A 1 158 ? -25.439 -9.567  7.952   0.50 16.88 ? 158 GLN B CD  1 
ATOM   1235 C  CD  B GLN A 1 158 ? -24.033 -11.613 7.619   0.50 16.07 ? 158 GLN B CD  1 
ATOM   1236 O  OE1 A GLN A 1 158 ? -26.437 -9.941  7.370   0.50 22.55 ? 158 GLN B OE1 1 
ATOM   1237 O  OE1 B GLN A 1 158 ? -23.498 -12.702 7.384   0.50 17.74 ? 158 GLN B OE1 1 
ATOM   1238 N  NE2 A GLN A 1 158 ? -25.477 -8.630  8.971   0.50 14.42 ? 158 GLN B NE2 1 
ATOM   1239 N  NE2 B GLN A 1 158 ? -24.284 -11.140 8.856   0.50 15.06 ? 158 GLN B NE2 1 
ATOM   1240 N  N   . LEU A 1 159 ? -21.582 -7.763  4.418   1.00 11.87 ? 159 LEU B N   1 
ATOM   1241 C  CA  . LEU A 1 159 ? -20.638 -6.669  4.123   1.00 12.55 ? 159 LEU B CA  1 
ATOM   1242 C  C   . LEU A 1 159 ? -21.196 -5.570  3.255   1.00 13.70 ? 159 LEU B C   1 
ATOM   1243 O  O   . LEU A 1 159 ? -20.754 -4.420  3.365   1.00 14.79 ? 159 LEU B O   1 
ATOM   1244 C  CB  . LEU A 1 159 ? -19.368 -7.213  3.510   1.00 13.29 ? 159 LEU B CB  1 
ATOM   1245 C  CG  . LEU A 1 159 ? -18.688 -8.191  4.450   1.00 13.43 ? 159 LEU B CG  1 
ATOM   1246 C  CD1 . LEU A 1 159 ? -17.480 -8.742  3.705   1.00 16.80 ? 159 LEU B CD1 1 
ATOM   1247 C  CD2 . LEU A 1 159 ? -18.273 -7.573  5.775   1.00 15.77 ? 159 LEU B CD2 1 
ATOM   1248 N  N   . GLN A 1 160 ? -22.210 -5.874  2.435   1.00 13.77 ? 160 GLN B N   1 
ATOM   1249 C  CA  . GLN A 1 160 ? -22.859 -4.867  1.637   1.00 15.01 ? 160 GLN B CA  1 
ATOM   1250 C  C   . GLN A 1 160 ? -23.514 -3.815  2.568   1.00 15.85 ? 160 GLN B C   1 
ATOM   1251 O  O   . GLN A 1 160 ? -23.556 -2.654  2.247   1.00 15.84 ? 160 GLN B O   1 
ATOM   1252 C  CB  . GLN A 1 160 ? -23.929 -5.573  0.742   1.00 15.76 ? 160 GLN B CB  1 
ATOM   1253 C  CG  . GLN A 1 160 ? -24.590 -4.520  -0.175  1.00 16.60 ? 160 GLN B CG  1 
ATOM   1254 C  CD  . GLN A 1 160 ? -23.889 -4.438  -1.507  1.00 19.83 ? 160 GLN B CD  1 
ATOM   1255 O  OE1 . GLN A 1 160 ? -22.843 -4.979  -1.736  1.00 17.60 ? 160 GLN B OE1 1 
ATOM   1256 N  NE2 . GLN A 1 160 ? -24.483 -3.693  -2.415  1.00 20.21 ? 160 GLN B NE2 1 
ATOM   1257 N  N   A LYS A 1 161 ? -23.999 -4.209  3.748   0.50 15.30 ? 161 LYS B N   1 
ATOM   1258 N  N   B LYS A 1 161 ? -23.995 -4.206  3.741   0.50 15.53 ? 161 LYS B N   1 
ATOM   1259 C  CA  A LYS A 1 161 ? -24.535 -3.241  4.698   0.50 17.18 ? 161 LYS B CA  1 
ATOM   1260 C  CA  B LYS A 1 161 ? -24.511 -3.247  4.699   0.50 17.67 ? 161 LYS B CA  1 
ATOM   1261 C  C   A LYS A 1 161 ? -23.465 -2.186  5.089   0.50 16.24 ? 161 LYS B C   1 
ATOM   1262 C  C   B LYS A 1 161 ? -23.459 -2.185  5.081   0.50 16.45 ? 161 LYS B C   1 
ATOM   1263 O  O   A LYS A 1 161 ? -23.763 -0.990  5.265   0.50 17.21 ? 161 LYS B O   1 
ATOM   1264 O  O   B LYS A 1 161 ? -23.764 -0.991  5.257   0.50 17.32 ? 161 LYS B O   1 
ATOM   1265 C  CB  A LYS A 1 161 ? -25.070 -3.942  5.976   0.50 17.65 ? 161 LYS B CB  1 
ATOM   1266 C  CB  B LYS A 1 161 ? -24.931 -4.000  5.962   0.50 18.90 ? 161 LYS B CB  1 
ATOM   1267 C  CG  A LYS A 1 161 ? -26.076 -5.098  5.758   0.50 19.56 ? 161 LYS B CG  1 
ATOM   1268 C  CG  B LYS A 1 161 ? -25.577 -3.160  7.041   0.50 22.02 ? 161 LYS B CG  1 
ATOM   1269 C  CD  A LYS A 1 161 ? -26.636 -5.698  7.059   0.50 19.78 ? 161 LYS B CD  1 
ATOM   1270 C  CD  B LYS A 1 161 ? -25.989 -4.031  8.211   0.50 23.41 ? 161 LYS B CD  1 
ATOM   1271 C  CE  A LYS A 1 161 ? -27.937 -6.404  6.792   0.50 23.29 ? 161 LYS B CE  1 
ATOM   1272 C  CE  B LYS A 1 161 ? -26.500 -3.166  9.342   0.50 22.24 ? 161 LYS B CE  1 
ATOM   1273 N  NZ  A LYS A 1 161 ? -27.746 -7.480  5.791   0.50 25.71 ? 161 LYS B NZ  1 
ATOM   1274 N  NZ  B LYS A 1 161 ? -27.699 -2.473  8.829   0.50 21.74 ? 161 LYS B NZ  1 
ATOM   1275 N  N   . ILE A 1 162 ? -22.216 -2.658  5.272   1.00 14.42 ? 162 ILE B N   1 
ATOM   1276 C  CA  . ILE A 1 162 ? -21.109 -1.745  5.560   1.00 14.64 ? 162 ILE B CA  1 
ATOM   1277 C  C   . ILE A 1 162 ? -20.730 -0.915  4.376   1.00 13.77 ? 162 ILE B C   1 
ATOM   1278 O  O   . ILE A 1 162 ? -20.616 0.332   4.488   1.00 14.46 ? 162 ILE B O   1 
ATOM   1279 C  CB  . ILE A 1 162 ? -19.860 -2.558  6.056   1.00 14.01 ? 162 ILE B CB  1 
ATOM   1280 C  CG1 . ILE A 1 162 ? -20.243 -3.217  7.408   1.00 14.15 ? 162 ILE B CG1 1 
ATOM   1281 C  CG2 . ILE A 1 162 ? -18.659 -1.600  6.239   1.00 13.80 ? 162 ILE B CG2 1 
ATOM   1282 C  CD1 . ILE A 1 162 ? -19.099 -4.113  7.926   1.00 15.50 ? 162 ILE B CD1 1 
ATOM   1283 N  N   . THR A 1 163 ? -20.614 -1.541  3.198   1.00 13.12 ? 163 THR B N   1 
ATOM   1284 C  CA  . THR A 1 163 ? -20.238 -0.768  2.045   1.00 13.41 ? 163 THR B CA  1 
ATOM   1285 C  C   . THR A 1 163 ? -21.270 0.289   1.686   1.00 14.29 ? 163 THR B C   1 
ATOM   1286 O  O   . THR A 1 163 ? -20.867 1.402   1.281   1.00 16.68 ? 163 THR B O   1 
ATOM   1287 C  CB  . THR A 1 163 ? -19.761 -1.638  0.840   1.00 15.21 ? 163 THR B CB  1 
ATOM   1288 O  OG1 . THR A 1 163 ? -20.809 -2.472  0.438   1.00 17.80 ? 163 THR B OG1 1 
ATOM   1289 C  CG2 . THR A 1 163 ? -18.646 -2.539  1.132   1.00 15.01 ? 163 THR B CG2 1 
ATOM   1290 N  N   . ASP A 1 164 ? -22.541 0.006   1.981   1.00 16.39 ? 164 ASP B N   1 
ATOM   1291 C  CA  . ASP A 1 164 ? -23.595 0.999   1.703   1.00 17.55 ? 164 ASP B CA  1 
ATOM   1292 C  C   . ASP A 1 164 ? -23.470 2.259   2.514   1.00 17.57 ? 164 ASP B C   1 
ATOM   1293 O  O   . ASP A 1 164 ? -24.095 3.271   2.103   1.00 23.38 ? 164 ASP B O   1 
ATOM   1294 C  CB  . ASP A 1 164 ? -24.963 0.423   1.901   1.00 18.31 ? 164 ASP B CB  1 
ATOM   1295 C  CG  . ASP A 1 164 ? -25.422 -0.419  0.707   1.00 20.53 ? 164 ASP B CG  1 
ATOM   1296 O  OD1 . ASP A 1 164 ? -24.802 -0.438  -0.368  1.00 22.40 ? 164 ASP B OD1 1 
ATOM   1297 O  OD2 . ASP A 1 164 ? -26.387 -1.203  0.880   1.00 25.34 ? 164 ASP B OD2 1 
ATOM   1298 N  N   . THR A 1 165 ? -22.738 2.257   3.625   1.00 16.86 ? 165 THR B N   1 
ATOM   1299 C  CA  . THR A 1 165 ? -22.563 3.408   4.501   1.00 15.45 ? 165 THR B CA  1 
ATOM   1300 C  C   . THR A 1 165 ? -21.362 4.217   4.133   1.00 15.58 ? 165 THR B C   1 
ATOM   1301 O  O   . THR A 1 165 ? -21.172 5.302   4.685   1.00 16.67 ? 165 THR B O   1 
ATOM   1302 C  CB  . THR A 1 165 ? -22.381 3.022   6.003   1.00 17.65 ? 165 THR B CB  1 
ATOM   1303 O  OG1 . THR A 1 165 ? -21.045 2.435   6.243   1.00 18.75 ? 165 THR B OG1 1 
ATOM   1304 C  CG2 . THR A 1 165 ? -23.522 2.077   6.514   1.00 19.06 ? 165 THR B CG2 1 
ATOM   1305 N  N   . LEU A 1 166 ? -20.460 3.703   3.329   1.00 13.88 ? 166 LEU B N   1 
ATOM   1306 C  CA  . LEU A 1 166 ? -19.169 4.354   3.218   1.00 15.12 ? 166 LEU B CA  1 
ATOM   1307 C  C   . LEU A 1 166 ? -19.234 5.792   2.641   1.00 15.80 ? 166 LEU B C   1 
ATOM   1308 O  O   . LEU A 1 166 ? -18.380 6.615   3.092   1.00 15.46 ? 166 LEU B O   1 
ATOM   1309 C  CB  . LEU A 1 166 ? -18.135 3.478   2.497   1.00 14.69 ? 166 LEU B CB  1 
ATOM   1310 C  CG  . LEU A 1 166 ? -17.823 2.088   3.115   1.00 12.90 ? 166 LEU B CG  1 
ATOM   1311 C  CD1 . LEU A 1 166 ? -16.908 1.351   2.225   1.00 16.41 ? 166 LEU B CD1 1 
ATOM   1312 C  CD2 . LEU A 1 166 ? -17.178 2.213   4.491   1.00 17.09 ? 166 LEU B CD2 1 
ATOM   1313 N  N   . ASP A 1 167 ? -20.112 6.004   1.687   1.00 18.26 ? 167 ASP B N   1 
ATOM   1314 C  CA  . ASP A 1 167 ? -20.206 7.379   1.133   1.00 21.74 ? 167 ASP B CA  1 
ATOM   1315 C  C   . ASP A 1 167 ? -20.486 8.350   2.263   1.00 22.61 ? 167 ASP B C   1 
ATOM   1316 O  O   . ASP A 1 167 ? -19.955 9.474   2.264   1.00 24.42 ? 167 ASP B O   1 
ATOM   1317 C  CB  . ASP A 1 167 ? -21.237 7.437   -0.006  1.00 24.56 ? 167 ASP B CB  1 
ATOM   1318 C  CG  . ASP A 1 167 ? -20.706 6.783   -1.264  1.00 22.98 ? 167 ASP B CG  1 
ATOM   1319 O  OD1 . ASP A 1 167 ? -19.495 6.569   -1.414  1.00 27.96 ? 167 ASP B OD1 1 
ATOM   1320 O  OD2 . ASP A 1 167 ? -21.513 6.470   -2.158  1.00 32.49 ? 167 ASP B OD2 1 
ATOM   1321 N  N   . SER A 1 168 ? -21.230 7.955   3.281   1.00 18.01 ? 168 SER B N   1 
ATOM   1322 C  CA  . SER A 1 168 ? -21.577 8.885   4.357   1.00 19.36 ? 168 SER B CA  1 
ATOM   1323 C  C   . SER A 1 168 ? -20.467 9.118   5.384   1.00 17.62 ? 168 SER B C   1 
ATOM   1324 O  O   . SER A 1 168 ? -20.525 10.001  6.201   1.00 20.57 ? 168 SER B O   1 
ATOM   1325 C  CB  . SER A 1 168 ? -22.847 8.476   5.048   1.00 18.98 ? 168 SER B CB  1 
ATOM   1326 O  OG  . SER A 1 168 ? -22.665 7.321   5.880   1.00 24.73 ? 168 SER B OG  1 
ATOM   1327 N  N   . ILE A 1 169 ? -19.379 8.332   5.350   1.00 15.06 ? 169 ILE B N   1 
ATOM   1328 C  CA  . ILE A 1 169 ? -18.249 8.475   6.225   1.00 14.83 ? 169 ILE B CA  1 
ATOM   1329 C  C   . ILE A 1 169 ? -16.863 8.587   5.516   1.00 15.04 ? 169 ILE B C   1 
ATOM   1330 O  O   . ILE A 1 169 ? -15.817 8.217   6.024   1.00 14.86 ? 169 ILE B O   1 
ATOM   1331 C  CB  . ILE A 1 169 ? -18.187 7.379   7.312   1.00 13.27 ? 169 ILE B CB  1 
ATOM   1332 C  CG1 . ILE A 1 169 ? -18.084 5.951   6.667   1.00 15.75 ? 169 ILE B CG1 1 
ATOM   1333 C  CG2 . ILE A 1 169 ? -19.456 7.386   8.141   1.00 15.33 ? 169 ILE B CG2 1 
ATOM   1334 C  CD1 . ILE A 1 169 ? -17.633 4.924   7.687   1.00 16.46 ? 169 ILE B CD1 1 
ATOM   1335 N  N   . LYS A 1 170 ? -16.895 9.234   4.323   1.00 16.29 ? 170 LYS B N   1 
ATOM   1336 C  CA  . LYS A 1 170 ? -15.698 9.256   3.512   1.00 17.08 ? 170 LYS B CA  1 
ATOM   1337 C  C   . LYS A 1 170 ? -14.598 10.026  4.212   1.00 15.68 ? 170 LYS B C   1 
ATOM   1338 O  O   . LYS A 1 170 ? -13.440 9.672   4.171   1.00 16.08 ? 170 LYS B O   1 
ATOM   1339 C  CB  . LYS A 1 170 ? -16.034 9.891   2.138   1.00 20.54 ? 170 LYS B CB  1 
ATOM   1340 C  CG  . LYS A 1 170 ? -14.821 10.275  1.386   1.00 28.32 ? 170 LYS B CG  1 
ATOM   1341 C  CD  . LYS A 1 170 ? -15.305 11.262  0.324   1.00 36.70 ? 170 LYS B CD  1 
ATOM   1342 C  CE  . LYS A 1 170 ? -14.424 11.286  -0.892  1.00 36.71 ? 170 LYS B CE  1 
ATOM   1343 N  NZ  . LYS A 1 170 ? -13.453 12.408  -0.817  1.00 48.84 ? 170 LYS B NZ  1 
ATOM   1344 N  N   . GLU A 1 171 ? -14.941 11.163  4.847   1.00 18.57 ? 171 GLU B N   1 
ATOM   1345 C  CA  . GLU A 1 171 ? -13.913 11.914  5.562   1.00 18.54 ? 171 GLU B CA  1 
ATOM   1346 C  C   . GLU A 1 171 ? -13.514 11.442  6.921   1.00 17.08 ? 171 GLU B C   1 
ATOM   1347 O  O   . GLU A 1 171 ? -14.413 10.941  7.638   1.00 16.95 ? 171 GLU B O   1 
ATOM   1348 C  CB  . GLU A 1 171 ? -14.293 13.422  5.716   1.00 21.68 ? 171 GLU B CB  1 
ATOM   1349 C  CG  . GLU A 1 171 ? -14.345 14.111  4.349   1.00 27.50 ? 171 GLU B CG  1 
ATOM   1350 C  CD  . GLU A 1 171 ? -15.687 13.921  3.691   1.00 30.63 ? 171 GLU B CD  1 
ATOM   1351 O  OE1 . GLU A 1 171 ? -15.722 14.188  2.469   1.00 42.98 ? 171 GLU B OE1 1 
ATOM   1352 O  OE2 . GLU A 1 171 ? -16.703 13.441  4.316   1.00 35.97 ? 171 GLU B OE2 1 
ATOM   1353 N  N   . LYS A 1 172 ? -12.248 11.557  7.272   1.00 18.90 ? 172 LYS B N   1 
ATOM   1354 C  CA  . LYS A 1 172 ? -11.806 11.212  8.552   1.00 16.66 ? 172 LYS B CA  1 
ATOM   1355 C  C   . LYS A 1 172 ? -12.628 11.854  9.650   1.00 19.07 ? 172 LYS B C   1 
ATOM   1356 O  O   . LYS A 1 172 ? -12.904 13.089  9.611   1.00 21.87 ? 172 LYS B O   1 
ATOM   1357 C  CB  . LYS A 1 172 ? -10.336 11.542  8.759   1.00 20.10 ? 172 LYS B CB  1 
ATOM   1358 C  CG  . LYS A 1 172 ? -9.721  11.245  10.102  1.00 17.85 ? 172 LYS B CG  1 
ATOM   1359 C  CD  . LYS A 1 172 ? -8.282  11.722  10.152  1.00 21.54 ? 172 LYS B CD  1 
ATOM   1360 C  CE  . LYS A 1 172 ? -7.858  11.410  11.563  1.00 24.57 ? 172 LYS B CE  1 
ATOM   1361 N  NZ  . LYS A 1 172 ? -6.428  11.324  11.702  1.00 28.92 ? 172 LYS B NZ  1 
ATOM   1362 N  N   . GLY A 1 173 ? -13.067 11.042  10.614  1.00 15.06 ? 173 GLY B N   1 
ATOM   1363 C  CA  . GLY A 1 173 ? -13.829 11.566  11.748  1.00 15.55 ? 173 GLY B CA  1 
ATOM   1364 C  C   . GLY A 1 173 ? -15.316 11.449  11.565  1.00 16.21 ? 173 GLY B C   1 
ATOM   1365 O  O   . GLY A 1 173 ? -16.079 11.602  12.559  1.00 20.39 ? 173 GLY B O   1 
ATOM   1366 N  N   . LYS A 1 174 ? -15.861 11.221  10.388  1.00 15.87 ? 174 LYS B N   1 
ATOM   1367 C  CA  . LYS A 1 174 ? -17.300 11.143  10.185  1.00 16.90 ? 174 LYS B CA  1 
ATOM   1368 C  C   . LYS A 1 174 ? -17.856 9.847   10.804  1.00 16.67 ? 174 LYS B C   1 
ATOM   1369 O  O   . LYS A 1 174 ? -17.130 8.814   10.803  1.00 15.62 ? 174 LYS B O   1 
ATOM   1370 C  CB  . LYS A 1 174 ? -17.611 11.193  8.724   1.00 19.86 ? 174 LYS B CB  1 
ATOM   1371 C  CG  . LYS A 1 174 ? -17.337 12.610  8.186   1.00 24.54 ? 174 LYS B CG  1 
ATOM   1372 C  CD  . LYS A 1 174 ? -18.579 13.423  8.131   1.00 33.69 ? 174 LYS B CD  1 
ATOM   1373 C  CE  . LYS A 1 174 ? -19.030 13.507  6.687   1.00 41.38 ? 174 LYS B CE  1 
ATOM   1374 N  NZ  . LYS A 1 174 ? -18.182 14.597  6.120   1.00 45.38 ? 174 LYS B NZ  1 
ATOM   1375 N  N   . GLN A 1 175 ? -19.079 9.883   11.244  1.00 17.46 ? 175 GLN B N   1 
ATOM   1376 C  CA  . GLN A 1 175 ? -19.797 8.735   11.848  1.00 17.99 ? 175 GLN B CA  1 
ATOM   1377 C  C   . GLN A 1 175 ? -21.194 8.728   11.404  1.00 18.49 ? 175 GLN B C   1 
ATOM   1378 O  O   . GLN A 1 175 ? -21.789 9.790   10.954  1.00 19.86 ? 175 GLN B O   1 
ATOM   1379 C  CB  . GLN A 1 175 ? -19.696 8.737   13.370  1.00 19.63 ? 175 GLN B CB  1 
ATOM   1380 C  CG  . GLN A 1 175 ? -20.529 9.700   14.168  1.00 24.56 ? 175 GLN B CG  1 
ATOM   1381 C  CD  . GLN A 1 175 ? -20.253 9.338   15.638  1.00 34.78 ? 175 GLN B CD  1 
ATOM   1382 O  OE1 . GLN A 1 175 ? -21.177 9.111   16.437  1.00 32.67 ? 175 GLN B OE1 1 
ATOM   1383 N  NE2 . GLN A 1 175 ? -18.959 9.141   15.951  1.00 39.06 ? 175 GLN B NE2 1 
ATOM   1384 N  N   . THR A 1 176 ? -21.805 7.558   11.468  1.00 15.75 ? 176 THR B N   1 
ATOM   1385 C  CA  . THR A 1 176 ? -23.166 7.454   11.236  1.00 16.16 ? 176 THR B CA  1 
ATOM   1386 C  C   . THR A 1 176 ? -23.753 6.237   11.949  1.00 18.76 ? 176 THR B C   1 
ATOM   1387 O  O   . THR A 1 176 ? -22.967 5.350   12.344  1.00 16.34 ? 176 THR B O   1 
ATOM   1388 C  CB  . THR A 1 176 ? -23.492 7.396   9.729   1.00 19.27 ? 176 THR B CB  1 
ATOM   1389 O  OG1 . THR A 1 176 ? -24.874 7.699   9.492   1.00 22.58 ? 176 THR B OG1 1 
ATOM   1390 C  CG2 . THR A 1 176 ? -23.159 6.077   9.123   1.00 20.31 ? 176 THR B CG2 1 
ATOM   1391 N  N   A ARG A 1 177 ? -25.061 6.239   12.258  0.50 15.84 ? 177 ARG B N   1 
ATOM   1392 N  N   B ARG A 1 177 ? -25.074 6.133   12.023  0.50 13.81 ? 177 ARG B N   1 
ATOM   1393 C  CA  A ARG A 1 177 ? -25.660 5.091   12.972  0.50 17.85 ? 177 ARG B CA  1 
ATOM   1394 C  CA  B ARG A 1 177 ? -25.678 5.095   12.821  0.50 15.20 ? 177 ARG B CA  1 
ATOM   1395 C  C   A ARG A 1 177 ? -25.611 3.855   12.065  0.50 17.15 ? 177 ARG B C   1 
ATOM   1396 C  C   B ARG A 1 177 ? -25.647 3.822   12.008  0.50 15.25 ? 177 ARG B C   1 
ATOM   1397 O  O   A ARG A 1 177 ? -25.709 3.905   10.862  0.50 18.09 ? 177 ARG B O   1 
ATOM   1398 O  O   B ARG A 1 177 ? -25.792 3.813   10.805  0.50 16.97 ? 177 ARG B O   1 
ATOM   1399 C  CB  A ARG A 1 177 ? -27.104 5.339   13.548  0.50 22.45 ? 177 ARG B CB  1 
ATOM   1400 C  CB  B ARG A 1 177 ? -27.087 5.565   13.162  0.50 14.29 ? 177 ARG B CB  1 
ATOM   1401 C  CG  A ARG A 1 177 ? -28.293 5.455   12.627  0.50 23.59 ? 177 ARG B CG  1 
ATOM   1402 C  CG  B ARG A 1 177 ? -26.872 6.645   14.214  0.50 14.95 ? 177 ARG B CG  1 
ATOM   1403 C  CD  A ARG A 1 177 ? -29.576 5.466   13.477  0.50 30.08 ? 177 ARG B CD  1 
ATOM   1404 C  CD  B ARG A 1 177 ? -28.226 7.055   14.705  0.50 17.39 ? 177 ARG B CD  1 
ATOM   1405 N  NE  A ARG A 1 177 ? -29.770 6.603   14.375  0.50 33.44 ? 177 ARG B NE  1 
ATOM   1406 N  NE  B ARG A 1 177 ? -28.830 5.982   15.475  0.50 17.37 ? 177 ARG B NE  1 
ATOM   1407 C  CZ  A ARG A 1 177 ? -30.605 6.610   15.422  0.50 38.10 ? 177 ARG B CZ  1 
ATOM   1408 C  CZ  B ARG A 1 177 ? -29.982 6.140   16.095  0.50 18.13 ? 177 ARG B CZ  1 
ATOM   1409 N  NH1 A ARG A 1 177 ? -31.362 5.547   15.710  0.50 41.64 ? 177 ARG B NH1 1 
ATOM   1410 N  NH1 B ARG A 1 177 ? -30.555 7.387   16.100  0.50 12.87 ? 177 ARG B NH1 1 
ATOM   1411 N  NH2 A ARG A 1 177 ? -30.701 7.692   16.177  0.50 36.25 ? 177 ARG B NH2 1 
ATOM   1412 N  NH2 B ARG A 1 177 ? -30.447 5.127   16.768  0.50 17.41 ? 177 ARG B NH2 1 
ATOM   1413 N  N   . PHE A 1 178 ? -25.464 2.713   12.748  1.00 15.65 ? 178 PHE B N   1 
ATOM   1414 C  CA  . PHE A 1 178 ? -25.293 1.396   12.105  1.00 15.01 ? 178 PHE B CA  1 
ATOM   1415 C  C   . PHE A 1 178 ? -25.614 0.328   13.148  1.00 13.82 ? 178 PHE B C   1 
ATOM   1416 O  O   . PHE A 1 178 ? -24.969 0.220   14.223  1.00 16.62 ? 178 PHE B O   1 
ATOM   1417 C  CB  . PHE A 1 178 ? -23.837 1.254   11.699  1.00 17.47 ? 178 PHE B CB  1 
ATOM   1418 C  CG  . PHE A 1 178 ? -23.545 -0.004  10.905  1.00 16.90 ? 178 PHE B CG  1 
ATOM   1419 C  CD1 . PHE A 1 178 ? -23.854 -0.103  9.572   1.00 15.90 ? 178 PHE B CD1 1 
ATOM   1420 C  CD2 . PHE A 1 178 ? -22.955 -1.122  11.548  1.00 16.40 ? 178 PHE B CD2 1 
ATOM   1421 C  CE1 . PHE A 1 178 ? -23.621 -1.261  8.843   1.00 22.27 ? 178 PHE B CE1 1 
ATOM   1422 C  CE2 . PHE A 1 178 ? -22.734 -2.281  10.830  1.00 17.85 ? 178 PHE B CE2 1 
ATOM   1423 C  CZ  . PHE A 1 178 ? -23.074 -2.341  9.489   1.00 20.23 ? 178 PHE B CZ  1 
ATOM   1424 N  N   . THR A 1 179 ? -26.683 -0.402  12.829  1.00 15.92 ? 179 THR B N   1 
ATOM   1425 C  CA  . THR A 1 179 ? -27.060 -1.458  13.833  1.00 18.62 ? 179 THR B CA  1 
ATOM   1426 C  C   . THR A 1 179 ? -27.644 -2.609  13.086  1.00 18.85 ? 179 THR B C   1 
ATOM   1427 O  O   . THR A 1 179 ? -27.582 -2.638  11.887  1.00 21.09 ? 179 THR B O   1 
ATOM   1428 C  CB  . THR A 1 179 ? -27.988 -0.882  14.942  1.00 20.27 ? 179 THR B CB  1 
ATOM   1429 O  OG1 . THR A 1 179 ? -28.125 -1.824  16.083  1.00 19.83 ? 179 THR B OG1 1 
ATOM   1430 C  CG2 . THR A 1 179 ? -29.367 -0.482  14.314  1.00 20.78 ? 179 THR B CG2 1 
ATOM   1431 N  N   A ASN A 1 180 ? -28.153 -3.637  13.765  0.50 19.16 ? 180 ASN B N   1 
ATOM   1432 N  N   B ASN A 1 180 ? -28.026 -3.589  13.931  0.50 18.54 ? 180 ASN B N   1 
ATOM   1433 C  CA  A ASN A 1 180 ? -28.635 -4.857  13.036  0.50 17.47 ? 180 ASN B CA  1 
ATOM   1434 C  CA  B ASN A 1 180 ? -28.670 -4.833  13.535  0.50 18.62 ? 180 ASN B CA  1 
ATOM   1435 C  C   A ASN A 1 180 ? -27.509 -5.494  12.215  0.50 17.57 ? 180 ASN B C   1 
ATOM   1436 C  C   B ASN A 1 180 ? -27.717 -5.555  12.553  0.50 18.98 ? 180 ASN B C   1 
ATOM   1437 O  O   A ASN A 1 180 ? -27.621 -5.768  10.993  0.50 18.03 ? 180 ASN B O   1 
ATOM   1438 O  O   B ASN A 1 180 ? -28.184 -5.910  11.501  0.50 18.45 ? 180 ASN B O   1 
ATOM   1439 C  CB  A ASN A 1 180 ? -29.902 -4.629  12.163  0.50 18.76 ? 180 ASN B CB  1 
ATOM   1440 C  CB  B ASN A 1 180 ? -30.072 -4.509  12.938  0.50 21.48 ? 180 ASN B CB  1 
ATOM   1441 C  CG  A ASN A 1 180 ? -30.680 -5.940  11.981  0.50 19.59 ? 180 ASN B CG  1 
ATOM   1442 C  CG  B ASN A 1 180 ? -31.085 -3.915  13.972  0.50 25.38 ? 180 ASN B CG  1 
ATOM   1443 O  OD1 A ASN A 1 180 ? -30.478 -6.881  12.769  0.50 21.90 ? 180 ASN B OD1 1 
ATOM   1444 O  OD1 B ASN A 1 180 ? -31.106 -4.244  15.172  0.50 24.47 ? 180 ASN B OD1 1 
ATOM   1445 N  ND2 A ASN A 1 180 ? -31.531 -6.019  10.966  0.50 23.58 ? 180 ASN B ND2 1 
ATOM   1446 N  ND2 B ASN A 1 180 ? -31.960 -3.034  13.464  0.50 29.43 ? 180 ASN B ND2 1 
ATOM   1447 N  N   . PHE A 1 181 ? -26.417 -5.757  12.918  1.00 15.52 ? 181 PHE B N   1 
ATOM   1448 C  CA  . PHE A 1 181 ? -25.336 -6.344  12.176  1.00 15.40 ? 181 PHE B CA  1 
ATOM   1449 C  C   . PHE A 1 181 ? -25.040 -7.739  12.747  1.00 12.72 ? 181 PHE B C   1 
ATOM   1450 O  O   . PHE A 1 181 ? -24.649 -7.901  13.909  1.00 14.73 ? 181 PHE B O   1 
ATOM   1451 C  CB  . PHE A 1 181 ? -24.084 -5.438  12.262  1.00 15.86 ? 181 PHE B CB  1 
ATOM   1452 C  CG  . PHE A 1 181 ? -22.818 -5.993  11.633  1.00 17.69 ? 181 PHE B CG  1 
ATOM   1453 C  CD1 . PHE A 1 181 ? -22.729 -6.222  10.268  1.00 21.50 ? 181 PHE B CD1 1 
ATOM   1454 C  CD2 . PHE A 1 181 ? -21.601 -5.987  12.407  1.00 17.77 ? 181 PHE B CD2 1 
ATOM   1455 C  CE1 . PHE A 1 181 ? -21.500 -6.650  9.708   1.00 22.65 ? 181 PHE B CE1 1 
ATOM   1456 C  CE2 . PHE A 1 181 ? -20.371 -6.352  11.866  1.00 21.36 ? 181 PHE B CE2 1 
ATOM   1457 C  CZ  . PHE A 1 181 ? -20.340 -6.724  10.516  1.00 21.61 ? 181 PHE B CZ  1 
ATOM   1458 N  N   . ASP A 1 182 ? -25.345 -8.748  11.874  1.00 15.89 ? 182 ASP B N   1 
ATOM   1459 C  CA  . ASP A 1 182 ? -25.287 -10.160 12.392  1.00 15.79 ? 182 ASP B CA  1 
ATOM   1460 C  C   . ASP A 1 182 ? -23.885 -10.754 12.163  1.00 13.23 ? 182 ASP B C   1 
ATOM   1461 O  O   . ASP A 1 182 ? -23.588 -11.447 11.230  1.00 15.78 ? 182 ASP B O   1 
ATOM   1462 C  CB  . ASP A 1 182 ? -26.356 -10.956 11.659  1.00 14.75 ? 182 ASP B CB  1 
ATOM   1463 C  CG  . ASP A 1 182 ? -26.545 -12.364 12.246  1.00 15.13 ? 182 ASP B CG  1 
ATOM   1464 O  OD1 . ASP A 1 182 ? -25.765 -12.832 13.085  1.00 14.87 ? 182 ASP B OD1 1 
ATOM   1465 O  OD2 . ASP A 1 182 ? -27.454 -13.057 11.732  1.00 16.25 ? 182 ASP B OD2 1 
ATOM   1466 N  N   . LEU A 1 183 ? -23.026 -10.301 13.089  1.00 13.53 ? 183 LEU B N   1 
ATOM   1467 C  CA  . LEU A 1 183 ? -21.630 -10.664 13.057  1.00 12.63 ? 183 LEU B CA  1 
ATOM   1468 C  C   . LEU A 1 183 ? -21.421 -12.165 13.148  1.00 12.06 ? 183 LEU B C   1 
ATOM   1469 O  O   . LEU A 1 183 ? -20.520 -12.732 12.520  1.00 12.56 ? 183 LEU B O   1 
ATOM   1470 C  CB  . LEU A 1 183 ? -20.927 -9.878  14.180  1.00 12.08 ? 183 LEU B CB  1 
ATOM   1471 C  CG  . LEU A 1 183 ? -19.449 -10.084 14.305  1.00 12.14 ? 183 LEU B CG  1 
ATOM   1472 C  CD1 . LEU A 1 183 ? -18.619 -9.773  13.036  1.00 14.13 ? 183 LEU B CD1 1 
ATOM   1473 C  CD2 . LEU A 1 183 ? -18.861 -9.310  15.460  1.00 12.05 ? 183 LEU B CD2 1 
ATOM   1474 N  N   . LEU A 1 184 ? -22.278 -12.824 13.968  1.00 11.32 ? 184 LEU B N   1 
ATOM   1475 C  CA  . LEU A 1 184 ? -22.147 -14.258 14.065  1.00 12.34 ? 184 LEU B CA  1 
ATOM   1476 C  C   . LEU A 1 184 ? -22.320 -14.935 12.734  1.00 10.56 ? 184 LEU B C   1 
ATOM   1477 O  O   . LEU A 1 184 ? -21.582 -15.880 12.439  1.00 11.94 ? 184 LEU B O   1 
ATOM   1478 C  CB  . LEU A 1 184 ? -23.174 -14.758 15.149  1.00 11.52 ? 184 LEU B CB  1 
ATOM   1479 C  CG  . LEU A 1 184 ? -22.950 -16.252 15.519  1.00 12.29 ? 184 LEU B CG  1 
ATOM   1480 C  CD1 . LEU A 1 184 ? -21.646 -16.496 16.217  1.00 15.90 ? 184 LEU B CD1 1 
ATOM   1481 C  CD2 . LEU A 1 184 ? -24.066 -16.793 16.384  1.00 14.00 ? 184 LEU B CD2 1 
ATOM   1482 N  N   A SER A 1 185 ? -23.308 -14.507 11.930  0.50 11.89 ? 185 SER B N   1 
ATOM   1483 N  N   B SER A 1 185 ? -23.315 -14.516 11.953  0.50 11.76 ? 185 SER B N   1 
ATOM   1484 C  CA  A SER A 1 185 ? -23.536 -15.116 10.614  0.50 12.15 ? 185 SER B CA  1 
ATOM   1485 C  CA  B SER A 1 185 ? -23.531 -15.139 10.672  0.50 11.87 ? 185 SER B CA  1 
ATOM   1486 C  C   A SER A 1 185 ? -22.503 -14.724 9.579   0.50 12.88 ? 185 SER B C   1 
ATOM   1487 C  C   B SER A 1 185 ? -22.444 -14.798 9.680   0.50 12.19 ? 185 SER B C   1 
ATOM   1488 O  O   A SER A 1 185 ? -22.449 -15.324 8.492   0.50 13.89 ? 185 SER B O   1 
ATOM   1489 O  O   B SER A 1 185 ? -22.294 -15.536 8.728   0.50 12.64 ? 185 SER B O   1 
ATOM   1490 C  CB  A SER A 1 185 ? -24.945 -14.694 10.106  0.50 13.15 ? 185 SER B CB  1 
ATOM   1491 C  CB  B SER A 1 185 ? -24.904 -14.675 10.134  0.50 13.02 ? 185 SER B CB  1 
ATOM   1492 O  OG  A SER A 1 185 ? -24.969 -13.354 9.609   0.50 15.40 ? 185 SER B OG  1 
ATOM   1493 O  OG  B SER A 1 185 ? -25.949 -15.140 10.968  0.50 16.07 ? 185 SER B OG  1 
ATOM   1494 N  N   . LEU A 1 186 ? -21.701 -13.715 9.844   1.00 12.10 ? 186 LEU B N   1 
ATOM   1495 C  CA  . LEU A 1 186 ? -20.640 -13.325 8.919   1.00 11.63 ? 186 LEU B CA  1 
ATOM   1496 C  C   . LEU A 1 186 ? -19.453 -14.310 9.017   1.00 11.01 ? 186 LEU B C   1 
ATOM   1497 O  O   . LEU A 1 186 ? -18.721 -14.483 8.079   1.00 11.20 ? 186 LEU B O   1 
ATOM   1498 C  CB  . LEU A 1 186 ? -20.205 -11.859 9.353   1.00 11.31 ? 186 LEU B CB  1 
ATOM   1499 C  CG  . LEU A 1 186 ? -19.139 -11.257 8.458   1.00 13.27 ? 186 LEU B CG  1 
ATOM   1500 C  CD1 . LEU A 1 186 ? -19.624 -10.924 7.024   1.00 14.86 ? 186 LEU B CD1 1 
ATOM   1501 C  CD2 . LEU A 1 186 ? -18.677 -10.012 9.117   1.00 14.31 ? 186 LEU B CD2 1 
ATOM   1502 N  N   . LEU A 1 187 ? -19.240 -14.954 10.191  1.00 10.69 ? 187 LEU B N   1 
ATOM   1503 C  CA  . LEU A 1 187 ? -18.110 -15.866 10.312  1.00 10.26 ? 187 LEU B CA  1 
ATOM   1504 C  C   . LEU A 1 187 ? -18.203 -17.084 9.397   1.00 9.59  ? 187 LEU B C   1 
ATOM   1505 O  O   . LEU A 1 187 ? -19.273 -17.462 8.934   1.00 10.15 ? 187 LEU B O   1 
ATOM   1506 C  CB  . LEU A 1 187 ? -18.063 -16.309 11.826  1.00 9.59  ? 187 LEU B CB  1 
ATOM   1507 C  CG  . LEU A 1 187 ? -17.988 -15.196 12.834  1.00 9.71  ? 187 LEU B CG  1 
ATOM   1508 C  CD1 . LEU A 1 187 ? -17.920 -15.844 14.203  1.00 10.74 ? 187 LEU B CD1 1 
ATOM   1509 C  CD2 . LEU A 1 187 ? -16.747 -14.299 12.608  1.00 11.95 ? 187 LEU B CD2 1 
ATOM   1510 N  N   . PRO A 1 188 ? -17.053 -17.644 8.992   1.00 9.13  ? 188 PRO B N   1 
ATOM   1511 C  CA  . PRO A 1 188 ? -17.029 -18.772 8.072   1.00 9.59  ? 188 PRO B CA  1 
ATOM   1512 C  C   . PRO A 1 188 ? -17.642 -20.030 8.695   1.00 10.05 ? 188 PRO B C   1 
ATOM   1513 O  O   . PRO A 1 188 ? -17.770 -20.082 9.914   1.00 10.80 ? 188 PRO B O   1 
ATOM   1514 C  CB  . PRO A 1 188 ? -15.525 -18.949 7.777   1.00 10.01 ? 188 PRO B CB  1 
ATOM   1515 C  CG  . PRO A 1 188 ? -14.830 -18.416 9.009   1.00 10.35 ? 188 PRO B CG  1 
ATOM   1516 C  CD  . PRO A 1 188 ? -15.688 -17.240 9.425   1.00 9.34  ? 188 PRO B CD  1 
ATOM   1517 N  N   . PRO A 1 189 ? -17.918 -21.032 7.898   1.00 10.14 ? 189 PRO B N   1 
ATOM   1518 C  CA  . PRO A 1 189 ? -18.492 -22.246 8.443   1.00 10.94 ? 189 PRO B CA  1 
ATOM   1519 C  C   . PRO A 1 189 ? -17.567 -22.907 9.443   1.00 11.47 ? 189 PRO B C   1 
ATOM   1520 O  O   . PRO A 1 189 ? -18.132 -23.363 10.514  1.00 12.52 ? 189 PRO B O   1 
ATOM   1521 C  CB  . PRO A 1 189 ? -18.624 -23.120 7.145   1.00 13.07 ? 189 PRO B CB  1 
ATOM   1522 C  CG  . PRO A 1 189 ? -18.853 -22.138 6.002   1.00 12.65 ? 189 PRO B CG  1 
ATOM   1523 C  CD  . PRO A 1 189 ? -17.949 -20.965 6.399   1.00 12.08 ? 189 PRO B CD  1 
ATOM   1524 N  N   . SER A 1 190 ? -16.233 -22.998 9.241   1.00 11.57 ? 190 SER B N   1 
ATOM   1525 C  CA  . SER A 1 190 ? -15.390 -23.650 10.212  1.00 11.02 ? 190 SER B CA  1 
ATOM   1526 C  C   . SER A 1 190 ? -14.778 -22.582 11.103  1.00 11.11 ? 190 SER B C   1 
ATOM   1527 O  O   . SER A 1 190 ? -14.328 -21.501 10.648  1.00 11.21 ? 190 SER B O   1 
ATOM   1528 C  CB  . SER A 1 190 ? -14.208 -24.290 9.430   1.00 12.00 ? 190 SER B CB  1 
ATOM   1529 O  OG  . SER A 1 190 ? -13.340 -24.850 10.451  1.00 12.74 ? 190 SER B OG  1 
ATOM   1530 N  N   . TRP A 1 191 ? -14.706 -22.866 12.399  1.00 11.79 ? 191 TRP B N   1 
ATOM   1531 C  CA  . TRP A 1 191 ? -14.060 -21.953 13.385  1.00 11.86 ? 191 TRP B CA  1 
ATOM   1532 C  C   . TRP A 1 191 ? -12.771 -22.573 13.888  1.00 12.01 ? 191 TRP B C   1 
ATOM   1533 O  O   . TRP A 1 191 ? -12.302 -22.162 14.976  1.00 12.90 ? 191 TRP B O   1 
ATOM   1534 C  CB  . TRP A 1 191 ? -14.986 -21.584 14.561  1.00 11.29 ? 191 TRP B CB  1 
ATOM   1535 C  CG  . TRP A 1 191 ? -16.205 -20.824 14.067  1.00 11.56 ? 191 TRP B CG  1 
ATOM   1536 C  CD1 . TRP A 1 191 ? -16.411 -20.216 12.850  1.00 11.00 ? 191 TRP B CD1 1 
ATOM   1537 C  CD2 . TRP A 1 191 ? -17.406 -20.601 14.833  1.00 11.02 ? 191 TRP B CD2 1 
ATOM   1538 N  NE1 . TRP A 1 191 ? -17.676 -19.659 12.809  1.00 11.33 ? 191 TRP B NE1 1 
ATOM   1539 C  CE2 . TRP A 1 191 ? -18.298 -19.823 14.032  1.00 11.02 ? 191 TRP B CE2 1 
ATOM   1540 C  CE3 . TRP A 1 191 ? -17.788 -20.959 16.147  1.00 12.31 ? 191 TRP B CE3 1 
ATOM   1541 C  CZ2 . TRP A 1 191 ? -19.572 -19.460 14.451  1.00 12.68 ? 191 TRP B CZ2 1 
ATOM   1542 C  CZ3 . TRP A 1 191 ? -19.047 -20.575 16.574  1.00 13.51 ? 191 TRP B CZ3 1 
ATOM   1543 C  CH2 . TRP A 1 191 ? -19.931 -19.860 15.781  1.00 12.27 ? 191 TRP B CH2 1 
ATOM   1544 N  N   . ASP A 1 192 ? -12.181 -23.409 13.066  1.00 11.34 ? 192 ASP B N   1 
ATOM   1545 C  CA  . ASP A 1 192 ? -10.836 -23.896 13.441  1.00 13.36 ? 192 ASP B CA  1 
ATOM   1546 C  C   . ASP A 1 192 ? -9.834  -22.688 13.353  1.00 10.82 ? 192 ASP B C   1 
ATOM   1547 O  O   . ASP A 1 192 ? -9.944  -21.801 12.450  1.00 10.36 ? 192 ASP B O   1 
ATOM   1548 C  CB  . ASP A 1 192 ? -10.442 -25.035 12.599  1.00 16.56 ? 192 ASP B CB  1 
ATOM   1549 C  CG  . ASP A 1 192 ? -11.290 -26.273 12.892  1.00 14.22 ? 192 ASP B CG  1 
ATOM   1550 O  OD1 . ASP A 1 192 ? -11.998 -26.301 13.927  1.00 17.06 ? 192 ASP B OD1 1 
ATOM   1551 O  OD2 . ASP A 1 192 ? -11.227 -27.229 12.102  1.00 20.23 ? 192 ASP B OD2 1 
ATOM   1552 N  N   . TYR A 1 193 ? -8.911  -22.634 14.317  1.00 10.17 ? 193 TYR B N   1 
ATOM   1553 C  CA  . TYR A 1 193 ? -8.065  -21.453 14.443  1.00 9.71  ? 193 TYR B CA  1 
ATOM   1554 C  C   . TYR A 1 193 ? -6.624  -21.684 14.856  1.00 10.40 ? 193 TYR B C   1 
ATOM   1555 O  O   . TYR A 1 193 ? -6.333  -22.764 15.363  1.00 10.91 ? 193 TYR B O   1 
ATOM   1556 C  CB  . TYR A 1 193 ? -8.746  -20.428 15.418  1.00 10.47 ? 193 TYR B CB  1 
ATOM   1557 C  CG  . TYR A 1 193 ? -8.809  -21.055 16.856  1.00 9.74  ? 193 TYR B CG  1 
ATOM   1558 C  CD1 . TYR A 1 193 ? -7.735  -20.885 17.742  1.00 10.99 ? 193 TYR B CD1 1 
ATOM   1559 C  CD2 . TYR A 1 193 ? -9.926  -21.694 17.304  1.00 10.77 ? 193 TYR B CD2 1 
ATOM   1560 C  CE1 . TYR A 1 193 ? -7.778  -21.445 19.020  1.00 11.06 ? 193 TYR B CE1 1 
ATOM   1561 C  CE2 . TYR A 1 193 ? -9.989  -22.266 18.589  1.00 9.79  ? 193 TYR B CE2 1 
ATOM   1562 C  CZ  . TYR A 1 193 ? -8.899  -22.112 19.435  1.00 10.05 ? 193 TYR B CZ  1 
ATOM   1563 O  OH  . TYR A 1 193 ? -8.888  -22.743 20.673  1.00 11.88 ? 193 TYR B OH  1 
ATOM   1564 N  N   . TRP A 1 194 ? -5.771  -20.722 14.629  1.00 10.07 ? 194 TRP B N   1 
ATOM   1565 C  CA  . TRP A 1 194 ? -4.474  -20.610 15.222  1.00 10.07 ? 194 TRP B CA  1 
ATOM   1566 C  C   . TRP A 1 194 ? -4.471  -19.587 16.260  1.00 9.95  ? 194 TRP B C   1 
ATOM   1567 O  O   . TRP A 1 194 ? -5.238  -18.591 16.208  1.00 10.71 ? 194 TRP B O   1 
ATOM   1568 C  CB  . TRP A 1 194 ? -3.402  -20.236 14.142  1.00 11.50 ? 194 TRP B CB  1 
ATOM   1569 C  CG  . TRP A 1 194 ? -3.339  -21.210 13.026  1.00 10.73 ? 194 TRP B CG  1 
ATOM   1570 C  CD1 . TRP A 1 194 ? -2.777  -22.483 13.031  1.00 11.53 ? 194 TRP B CD1 1 
ATOM   1571 C  CD2 . TRP A 1 194 ? -3.811  -21.044 11.678  1.00 10.46 ? 194 TRP B CD2 1 
ATOM   1572 N  NE1 . TRP A 1 194 ? -2.883  -23.049 11.807  1.00 11.95 ? 194 TRP B NE1 1 
ATOM   1573 C  CE2 . TRP A 1 194 ? -3.480  -22.218 10.933  1.00 11.39 ? 194 TRP B CE2 1 
ATOM   1574 C  CE3 . TRP A 1 194 ? -4.439  -19.991 11.009  1.00 11.08 ? 194 TRP B CE3 1 
ATOM   1575 C  CZ2 . TRP A 1 194 ? -3.790  -22.359 9.617   1.00 11.65 ? 194 TRP B CZ2 1 
ATOM   1576 C  CZ3 . TRP A 1 194 ? -4.689  -20.108 9.632   1.00 11.44 ? 194 TRP B CZ3 1 
ATOM   1577 C  CH2 . TRP A 1 194 ? -4.380  -21.274 8.980   1.00 11.15 ? 194 TRP B CH2 1 
ATOM   1578 N  N   . THR A 1 195 ? -3.600  -19.681 17.274  1.00 9.15  ? 195 THR B N   1 
ATOM   1579 C  CA  . THR A 1 195 ? -3.522  -18.689 18.295  1.00 9.31  ? 195 THR B CA  1 
ATOM   1580 C  C   . THR A 1 195 ? -2.144  -18.423 18.805  1.00 9.84  ? 195 THR B C   1 
ATOM   1581 O  O   . THR A 1 195 ? -1.309  -19.402 18.881  1.00 10.66 ? 195 THR B O   1 
ATOM   1582 C  CB  . THR A 1 195 ? -4.485  -19.031 19.521  1.00 10.22 ? 195 THR B CB  1 
ATOM   1583 O  OG1 . THR A 1 195 ? -4.420  -18.067 20.522  1.00 10.09 ? 195 THR B OG1 1 
ATOM   1584 C  CG2 . THR A 1 195 ? -4.107  -20.461 20.136  1.00 11.00 ? 195 THR B CG2 1 
ATOM   1585 N  N   . TYR A 1 196 ? -1.850  -17.222 19.158  1.00 10.37 ? 196 TYR B N   1 
ATOM   1586 C  CA  . TYR A 1 196 ? -0.514  -16.839 19.725  1.00 9.48  ? 196 TYR B CA  1 
ATOM   1587 C  C   . TYR A 1 196 ? -0.674  -15.568 20.476  1.00 10.31 ? 196 TYR B C   1 
ATOM   1588 O  O   . TYR A 1 196 ? -1.604  -14.819 20.250  1.00 10.61 ? 196 TYR B O   1 
ATOM   1589 C  CB  . TYR A 1 196 ? 0.536   -16.722 18.611  1.00 9.97  ? 196 TYR B CB  1 
ATOM   1590 C  CG  . TYR A 1 196 ? 0.366   -15.491 17.733  1.00 10.72 ? 196 TYR B CG  1 
ATOM   1591 C  CD1 . TYR A 1 196 ? -0.610  -15.486 16.731  1.00 10.16 ? 196 TYR B CD1 1 
ATOM   1592 C  CD2 . TYR A 1 196 ? 1.123   -14.359 17.962  1.00 11.48 ? 196 TYR B CD2 1 
ATOM   1593 C  CE1 . TYR A 1 196 ? -0.798  -14.319 15.951  1.00 10.06 ? 196 TYR B CE1 1 
ATOM   1594 C  CE2 . TYR A 1 196 ? 0.955   -13.228 17.174  1.00 10.85 ? 196 TYR B CE2 1 
ATOM   1595 C  CZ  . TYR A 1 196 ? -0.073  -13.218 16.244  1.00 10.48 ? 196 TYR B CZ  1 
ATOM   1596 O  OH  . TYR A 1 196 ? -0.178  -12.037 15.493  1.00 10.29 ? 196 TYR B OH  1 
ATOM   1597 N  N   . PRO A 1 197 ? 0.273   -15.246 21.395  1.00 11.13 ? 197 PRO B N   1 
ATOM   1598 C  CA  . PRO A 1 197 ? 0.247   -14.015 22.112  1.00 9.98  ? 197 PRO B CA  1 
ATOM   1599 C  C   . PRO A 1 197 ? 0.862   -12.870 21.247  1.00 10.49 ? 197 PRO B C   1 
ATOM   1600 O  O   . PRO A 1 197 ? 2.022   -13.082 20.761  1.00 10.93 ? 197 PRO B O   1 
ATOM   1601 C  CB  . PRO A 1 197 ? 1.134   -14.313 23.382  1.00 11.87 ? 197 PRO B CB  1 
ATOM   1602 C  CG  . PRO A 1 197 ? 2.139   -15.386 22.842  1.00 11.09 ? 197 PRO B CG  1 
ATOM   1603 C  CD  . PRO A 1 197 ? 1.298   -16.228 21.864  1.00 11.02 ? 197 PRO B CD  1 
ATOM   1604 N  N   . GLY A 1 198 ? 0.235   -11.740 21.185  1.00 9.66  ? 198 GLY B N   1 
ATOM   1605 C  CA  . GLY A 1 198 ? 0.809   -10.662 20.364  1.00 10.73 ? 198 GLY B CA  1 
ATOM   1606 C  C   . GLY A 1 198 ? 0.337   -9.335  20.746  1.00 9.70  ? 198 GLY B C   1 
ATOM   1607 O  O   . GLY A 1 198 ? 0.152   -9.010  21.962  1.00 10.81 ? 198 GLY B O   1 
ATOM   1608 N  N   . SER A 1 199 ? 0.125   -8.433  19.766  1.00 9.56  ? 199 SER B N   1 
ATOM   1609 C  CA  . SER A 1 199 ? -0.074  -7.036  20.000  1.00 10.32 ? 199 SER B CA  1 
ATOM   1610 C  C   . SER A 1 199 ? -1.147  -6.404  19.162  1.00 10.20 ? 199 SER B C   1 
ATOM   1611 O  O   . SER A 1 199 ? -1.591  -7.044  18.168  1.00 10.46 ? 199 SER B O   1 
ATOM   1612 C  CB  . SER A 1 199 ? 1.217   -6.181  19.721  1.00 11.05 ? 199 SER B CB  1 
ATOM   1613 O  OG  . SER A 1 199 ? 1.494   -6.232  18.254  1.00 11.75 ? 199 SER B OG  1 
ATOM   1614 N  N   . LEU A 1 200 ? -1.527  -5.206  19.482  1.00 10.23 ? 200 LEU B N   1 
ATOM   1615 C  CA  . LEU A 1 200 ? -2.213  -4.366  18.492  1.00 10.50 ? 200 LEU B CA  1 
ATOM   1616 C  C   . LEU A 1 200 ? -1.300  -4.261  17.261  1.00 12.07 ? 200 LEU B C   1 
ATOM   1617 O  O   . LEU A 1 200 ? -0.075  -4.216  17.363  1.00 10.81 ? 200 LEU B O   1 
ATOM   1618 C  CB  . LEU A 1 200 ? -2.353  -2.923  19.004  1.00 11.32 ? 200 LEU B CB  1 
ATOM   1619 C  CG  . LEU A 1 200 ? -3.564  -2.628  19.808  1.00 14.96 ? 200 LEU B CG  1 
ATOM   1620 C  CD1 . LEU A 1 200 ? -3.697  -3.472  21.043  1.00 16.80 ? 200 LEU B CD1 1 
ATOM   1621 C  CD2 . LEU A 1 200 ? -3.584  -1.136  20.223  1.00 15.89 ? 200 LEU B CD2 1 
ATOM   1622 N  N   . THR A 1 201 ? -1.973  -4.269  16.084  1.00 10.73 ? 201 THR B N   1 
ATOM   1623 C  CA  . THR A 1 201 ? -1.210  -4.072  14.807  1.00 11.63 ? 201 THR B CA  1 
ATOM   1624 C  C   . THR A 1 201 ? -1.174  -2.633  14.356  1.00 11.94 ? 201 THR B C   1 
ATOM   1625 O  O   . THR A 1 201 ? -0.640  -2.355  13.248  1.00 11.45 ? 201 THR B O   1 
ATOM   1626 C  CB  . THR A 1 201 ? -1.777  -4.943  13.690  1.00 10.77 ? 201 THR B CB  1 
ATOM   1627 O  OG1 . THR A 1 201 ? -3.018  -4.452  13.313  1.00 9.71  ? 201 THR B OG1 1 
ATOM   1628 C  CG2 . THR A 1 201 ? -1.803  -6.415  14.090  1.00 11.02 ? 201 THR B CG2 1 
ATOM   1629 N  N   . VAL A 1 202 ? -1.678  -1.700  15.176  1.00 11.42 ? 202 VAL B N   1 
ATOM   1630 C  CA  . VAL A 1 202 ? -1.574  -0.260  14.979  1.00 11.88 ? 202 VAL B CA  1 
ATOM   1631 C  C   . VAL A 1 202 ? -1.019  0.381   16.234  1.00 14.25 ? 202 VAL B C   1 
ATOM   1632 O  O   . VAL A 1 202 ? -1.171  -0.185  17.355  1.00 12.71 ? 202 VAL B O   1 
ATOM   1633 C  CB  . VAL A 1 202 ? -2.906  0.381   14.672  1.00 12.67 ? 202 VAL B CB  1 
ATOM   1634 C  CG1 . VAL A 1 202 ? -3.506  -0.130  13.315  1.00 15.33 ? 202 VAL B CG1 1 
ATOM   1635 C  CG2 . VAL A 1 202 ? -3.939  0.193   15.792  1.00 15.03 ? 202 VAL B CG2 1 
ATOM   1636 N  N   . PRO A 1 203 ? -0.363  1.540   16.119  1.00 13.35 ? 203 PRO B N   1 
ATOM   1637 C  CA  . PRO A 1 203 ? 0.000   2.313   17.325  1.00 15.56 ? 203 PRO B CA  1 
ATOM   1638 C  C   . PRO A 1 203 ? -1.258  2.448   18.209  1.00 14.61 ? 203 PRO B C   1 
ATOM   1639 O  O   . PRO A 1 203 ? -2.337  2.747   17.737  1.00 13.99 ? 203 PRO B O   1 
ATOM   1640 C  CB  . PRO A 1 203 ? 0.449   3.679   16.707  1.00 15.32 ? 203 PRO B CB  1 
ATOM   1641 C  CG  . PRO A 1 203 ? 1.061   3.196   15.387  1.00 15.06 ? 203 PRO B CG  1 
ATOM   1642 C  CD  . PRO A 1 203 ? 0.053   2.188   14.873  1.00 14.22 ? 203 PRO B CD  1 
ATOM   1643 N  N   . PRO A 1 204 ? -1.108  2.233   19.552  1.00 15.20 ? 204 PRO B N   1 
ATOM   1644 C  CA  . PRO A 1 204 ? 0.127   2.157   20.283  1.00 15.82 ? 204 PRO B CA  1 
ATOM   1645 C  C   . PRO A 1 204 ? 0.839   0.839   20.397  1.00 14.17 ? 204 PRO B C   1 
ATOM   1646 O  O   . PRO A 1 204 ? 1.837   0.703   21.089  1.00 15.89 ? 204 PRO B O   1 
ATOM   1647 C  CB  . PRO A 1 204 ? -0.297  2.660   21.685  1.00 15.42 ? 204 PRO B CB  1 
ATOM   1648 C  CG  . PRO A 1 204 ? -1.724  2.188   21.777  1.00 16.71 ? 204 PRO B CG  1 
ATOM   1649 C  CD  . PRO A 1 204 ? -2.288  2.475   20.409  1.00 17.05 ? 204 PRO B CD  1 
ATOM   1650 N  N   . LEU A 1 205 ? 0.396   -0.219  19.631  1.00 11.97 ? 205 LEU B N   1 
ATOM   1651 C  CA  . LEU A 1 205 ? 1.142   -1.384  19.462  1.00 12.23 ? 205 LEU B CA  1 
ATOM   1652 C  C   . LEU A 1 205 ? 1.392   -2.224  20.753  1.00 10.50 ? 205 LEU B C   1 
ATOM   1653 O  O   . LEU A 1 205 ? 2.283   -3.066  20.859  1.00 11.87 ? 205 LEU B O   1 
ATOM   1654 C  CB  . LEU A 1 205 ? 2.529   -1.152  18.757  1.00 14.60 ? 205 LEU B CB  1 
ATOM   1655 C  CG  . LEU A 1 205 ? 2.385   -0.636  17.311  1.00 14.27 ? 205 LEU B CG  1 
ATOM   1656 C  CD1 . LEU A 1 205 ? 3.746   -0.058  16.805  1.00 15.93 ? 205 LEU B CD1 1 
ATOM   1657 C  CD2 . LEU A 1 205 ? 1.768   -1.551  16.261  1.00 15.01 ? 205 LEU B CD2 1 
ATOM   1658 N  N   . LEU A 1 206 ? 0.408   -2.022  21.674  1.00 13.21 ? 206 LEU B N   1 
ATOM   1659 C  CA  . LEU A 1 206 ? 0.524   -2.651  23.024  1.00 12.91 ? 206 LEU B CA  1 
ATOM   1660 C  C   . LEU A 1 206 ? 0.484   -4.182  22.955  1.00 13.60 ? 206 LEU B C   1 
ATOM   1661 O  O   . LEU A 1 206 ? -0.336  -4.733  22.155  1.00 11.56 ? 206 LEU B O   1 
ATOM   1662 C  CB  . LEU A 1 206 ? -0.619  -2.170  23.910  1.00 13.96 ? 206 LEU B CB  1 
ATOM   1663 C  CG  . LEU A 1 206 ? -0.667  -0.669  24.121  1.00 16.02 ? 206 LEU B CG  1 
ATOM   1664 C  CD1 . LEU A 1 206 ? -1.905  -0.179  24.839  1.00 17.85 ? 206 LEU B CD1 1 
ATOM   1665 C  CD2 . LEU A 1 206 ? 0.640   -0.239  24.871  1.00 21.21 ? 206 LEU B CD2 1 
ATOM   1666 N  N   . GLU A 1 207 ? 1.277   -4.895  23.720  1.00 12.60 ? 207 GLU B N   1 
ATOM   1667 C  CA  . GLU A 1 207 ? 1.399   -6.315  23.712  1.00 13.31 ? 207 GLU B CA  1 
ATOM   1668 C  C   . GLU A 1 207 ? 0.413   -6.919  24.701  1.00 14.26 ? 207 GLU B C   1 
ATOM   1669 O  O   . GLU A 1 207 ? 0.776   -7.513  25.745  1.00 13.76 ? 207 GLU B O   1 
ATOM   1670 C  CB  . GLU A 1 207 ? 2.850   -6.701  24.028  1.00 14.20 ? 207 GLU B CB  1 
ATOM   1671 C  CG  . GLU A 1 207 ? 3.699   -6.209  22.868  1.00 14.51 ? 207 GLU B CG  1 
ATOM   1672 C  CD  . GLU A 1 207 ? 5.174   -6.509  22.957  1.00 19.69 ? 207 GLU B CD  1 
ATOM   1673 O  OE1 . GLU A 1 207 ? 5.696   -6.734  24.120  1.00 19.17 ? 207 GLU B OE1 1 
ATOM   1674 O  OE2 . GLU A 1 207 ? 5.876   -6.549  21.891  1.00 16.33 ? 207 GLU B OE2 1 
ATOM   1675 N  N   . SER A 1 208 ? -0.861  -6.822  24.319  1.00 12.23 ? 208 SER B N   1 
ATOM   1676 C  CA  . SER A 1 208 ? -2.011  -7.142  25.201  1.00 11.63 ? 208 SER B CA  1 
ATOM   1677 C  C   . SER A 1 208 ? -2.983  -8.046  24.513  1.00 10.32 ? 208 SER B C   1 
ATOM   1678 O  O   . SER A 1 208 ? -4.075  -8.316  25.071  1.00 11.78 ? 208 SER B O   1 
ATOM   1679 C  CB  . SER A 1 208 ? -2.729  -5.898  25.635  1.00 14.02 ? 208 SER B CB  1 
ATOM   1680 O  OG  . SER A 1 208 ? -3.112  -5.083  24.517  1.00 15.45 ? 208 SER B OG  1 
ATOM   1681 N  N   . VAL A 1 209 ? -2.607  -8.602  23.362  1.00 10.03 ? 209 VAL B N   1 
ATOM   1682 C  CA  . VAL A 1 209 ? -3.632  -9.341  22.610  1.00 10.44 ? 209 VAL B CA  1 
ATOM   1683 C  C   . VAL A 1 209 ? -3.400  -10.805 22.508  1.00 9.80  ? 209 VAL B C   1 
ATOM   1684 O  O   . VAL A 1 209 ? -2.340  -11.290 22.133  1.00 11.60 ? 209 VAL B O   1 
ATOM   1685 C  CB  . VAL A 1 209 ? -3.650  -8.766  21.132  1.00 9.29  ? 209 VAL B CB  1 
ATOM   1686 C  CG1 . VAL A 1 209 ? -4.687  -9.483  20.314  1.00 9.77  ? 209 VAL B CG1 1 
ATOM   1687 C  CG2 . VAL A 1 209 ? -4.015  -7.285  21.124  1.00 11.50 ? 209 VAL B CG2 1 
ATOM   1688 N  N   . THR A 1 210 ? -4.457  -11.612 22.836  1.00 9.53  ? 210 THR B N   1 
ATOM   1689 C  CA  . THR A 1 210 ? -4.468  -13.009 22.504  1.00 10.45 ? 210 THR B CA  1 
ATOM   1690 C  C   . THR A 1 210 ? -5.112  -13.076 21.094  1.00 10.43 ? 210 THR B C   1 
ATOM   1691 O  O   . THR A 1 210 ? -6.280  -12.747 20.937  1.00 10.66 ? 210 THR B O   1 
ATOM   1692 C  CB  . THR A 1 210 ? -5.326  -13.888 23.463  1.00 9.76  ? 210 THR B CB  1 
ATOM   1693 O  OG1 . THR A 1 210 ? -4.721  -13.714 24.788  1.00 10.78 ? 210 THR B OG1 1 
ATOM   1694 C  CG2 . THR A 1 210 ? -5.269  -15.330 23.119  1.00 10.90 ? 210 THR B CG2 1 
ATOM   1695 N  N   . TRP A 1 211 ? -4.277  -13.423 20.127  1.00 9.05  ? 211 TRP B N   1 
ATOM   1696 C  CA  . TRP A 1 211 ? -4.772  -13.512 18.727  1.00 8.67  ? 211 TRP B CA  1 
ATOM   1697 C  C   . TRP A 1 211 ? -5.415  -14.861 18.496  1.00 8.31  ? 211 TRP B C   1 
ATOM   1698 O  O   . TRP A 1 211 ? -4.841  -15.898 18.845  1.00 8.98  ? 211 TRP B O   1 
ATOM   1699 C  CB  . TRP A 1 211 ? -3.600  -13.347 17.781  1.00 9.55  ? 211 TRP B CB  1 
ATOM   1700 C  CG  . TRP A 1 211 ? -3.346  -11.884 17.512  1.00 9.65  ? 211 TRP B CG  1 
ATOM   1701 C  CD1 . TRP A 1 211 ? -2.411  -11.046 18.138  1.00 10.59 ? 211 TRP B CD1 1 
ATOM   1702 C  CD2 . TRP A 1 211 ? -4.094  -11.045 16.622  1.00 8.48  ? 211 TRP B CD2 1 
ATOM   1703 N  NE1 . TRP A 1 211 ? -2.610  -9.753  17.742  1.00 9.32  ? 211 TRP B NE1 1 
ATOM   1704 C  CE2 . TRP A 1 211 ? -3.634  -9.714  16.799  1.00 9.35  ? 211 TRP B CE2 1 
ATOM   1705 C  CE3 . TRP A 1 211 ? -5.195  -11.296 15.768  1.00 9.00  ? 211 TRP B CE3 1 
ATOM   1706 C  CZ2 . TRP A 1 211 ? -4.197  -8.646  16.128  1.00 9.27  ? 211 TRP B CZ2 1 
ATOM   1707 C  CZ3 . TRP A 1 211 ? -5.725  -10.235 15.060  1.00 9.95  ? 211 TRP B CZ3 1 
ATOM   1708 C  CH2 . TRP A 1 211 ? -5.244  -8.920  15.261  1.00 8.98  ? 211 TRP B CH2 1 
ATOM   1709 N  N   . ILE A 1 212 ? -6.547  -14.859 17.794  1.00 8.64  ? 212 ILE B N   1 
ATOM   1710 C  CA  . ILE A 1 212 ? -7.295  -16.041 17.408  1.00 9.01  ? 212 ILE B CA  1 
ATOM   1711 C  C   . ILE A 1 212 ? -7.562  -15.855 15.894  1.00 8.06  ? 212 ILE B C   1 
ATOM   1712 O  O   . ILE A 1 212 ? -8.424  -15.017 15.565  1.00 9.23  ? 212 ILE B O   1 
ATOM   1713 C  CB  . ILE A 1 212 ? -8.612  -16.173 18.175  1.00 8.86  ? 212 ILE B CB  1 
ATOM   1714 C  CG1 . ILE A 1 212 ? -8.252  -16.319 19.682  1.00 9.91  ? 212 ILE B CG1 1 
ATOM   1715 C  CG2 . ILE A 1 212 ? -9.403  -17.441 17.727  1.00 10.19 ? 212 ILE B CG2 1 
ATOM   1716 C  CD1 . ILE A 1 212 ? -9.499  -16.175 20.632  1.00 11.00 ? 212 ILE B CD1 1 
ATOM   1717 N  N   . VAL A 1 213 ? -6.835  -16.586 15.046  1.00 8.50  ? 213 VAL B N   1 
ATOM   1718 C  CA  . VAL A 1 213 ? -6.948  -16.340 13.569  1.00 9.00  ? 213 VAL B CA  1 
ATOM   1719 C  C   . VAL A 1 213 ? -7.650  -17.493 12.948  1.00 8.47  ? 213 VAL B C   1 
ATOM   1720 O  O   . VAL A 1 213 ? -7.125  -18.661 13.049  1.00 8.88  ? 213 VAL B O   1 
ATOM   1721 C  CB  . VAL A 1 213 ? -5.525  -16.131 12.994  1.00 10.01 ? 213 VAL B CB  1 
ATOM   1722 C  CG1 . VAL A 1 213 ? -5.631  -15.994 11.458  1.00 11.43 ? 213 VAL B CG1 1 
ATOM   1723 C  CG2 . VAL A 1 213 ? -4.839  -14.866 13.573  1.00 9.85  ? 213 VAL B CG2 1 
ATOM   1724 N  N   . LEU A 1 214 ? -8.819  -17.350 12.371  1.00 8.68  ? 214 LEU B N   1 
ATOM   1725 C  CA  . LEU A 1 214 ? -9.495  -18.447 11.724  1.00 9.59  ? 214 LEU B CA  1 
ATOM   1726 C  C   . LEU A 1 214 ? -8.843  -18.843 10.450  1.00 9.55  ? 214 LEU B C   1 
ATOM   1727 O  O   . LEU A 1 214 ? -8.421  -18.014 9.657   1.00 10.12 ? 214 LEU B O   1 
ATOM   1728 C  CB  . LEU A 1 214 ? -10.990 -18.064 11.406  1.00 9.89  ? 214 LEU B CB  1 
ATOM   1729 C  CG  . LEU A 1 214 ? -11.775 -17.671 12.627  1.00 9.22  ? 214 LEU B CG  1 
ATOM   1730 C  CD1 . LEU A 1 214 ? -13.252 -17.484 12.209  1.00 11.39 ? 214 LEU B CD1 1 
ATOM   1731 C  CD2 . LEU A 1 214 ? -11.775 -18.710 13.725  1.00 12.06 ? 214 LEU B CD2 1 
ATOM   1732 N  N   . LYS A 1 215 ? -8.759  -20.192 10.252  1.00 9.30  ? 215 LYS B N   1 
ATOM   1733 C  CA  . LYS A 1 215 ? -8.142  -20.685 9.022   1.00 10.47 ? 215 LYS B CA  1 
ATOM   1734 C  C   . LYS A 1 215 ? -9.026  -20.370 7.765   1.00 9.28  ? 215 LYS B C   1 
ATOM   1735 O  O   . LYS A 1 215 ? -8.491  -20.103 6.662   1.00 11.77 ? 215 LYS B O   1 
ATOM   1736 C  CB  . LYS A 1 215 ? -7.876  -22.210 9.218   1.00 10.66 ? 215 LYS B CB  1 
ATOM   1737 C  CG  . LYS A 1 215 ? -7.426  -22.877 7.892   1.00 12.95 ? 215 LYS B CG  1 
ATOM   1738 C  CD  . LYS A 1 215 ? -7.157  -24.333 8.156   1.00 15.11 ? 215 LYS B CD  1 
ATOM   1739 C  CE  . LYS A 1 215 ? -6.819  -25.011 6.809   1.00 20.83 ? 215 LYS B CE  1 
ATOM   1740 N  NZ  . LYS A 1 215 ? -6.464  -26.463 6.974   1.00 26.18 ? 215 LYS B NZ  1 
ATOM   1741 N  N   . GLN A 1 216 ? -10.311 -20.531 7.871   1.00 9.50  ? 216 GLN B N   1 
ATOM   1742 C  CA  . GLN A 1 216 ? -11.170 -20.500 6.676   1.00 9.46  ? 216 GLN B CA  1 
ATOM   1743 C  C   . GLN A 1 216 ? -11.521 -19.049 6.318   1.00 10.35 ? 216 GLN B C   1 
ATOM   1744 O  O   . GLN A 1 216 ? -12.141 -18.345 7.187   1.00 10.12 ? 216 GLN B O   1 
ATOM   1745 C  CB  . GLN A 1 216 ? -12.439 -21.292 6.852   1.00 10.37 ? 216 GLN B CB  1 
ATOM   1746 C  CG  . GLN A 1 216 ? -13.281 -21.317 5.567   1.00 11.92 ? 216 GLN B CG  1 
ATOM   1747 C  CD  . GLN A 1 216 ? -14.495 -22.204 5.602   1.00 13.70 ? 216 GLN B CD  1 
ATOM   1748 O  OE1 . GLN A 1 216 ? -14.920 -22.685 6.651   1.00 13.28 ? 216 GLN B OE1 1 
ATOM   1749 N  NE2 . GLN A 1 216 ? -15.026 -22.468 4.459   1.00 17.02 ? 216 GLN B NE2 1 
ATOM   1750 N  N   . PRO A 1 217 ? -11.214 -18.566 5.103   1.00 10.63 ? 217 PRO B N   1 
ATOM   1751 C  CA  . PRO A 1 217 ? -11.640 -17.213 4.745   1.00 10.89 ? 217 PRO B CA  1 
ATOM   1752 C  C   . PRO A 1 217 ? -13.142 -17.123 4.449   1.00 11.51 ? 217 PRO B C   1 
ATOM   1753 O  O   . PRO A 1 217 ? -13.808 -18.112 4.170   1.00 12.81 ? 217 PRO B O   1 
ATOM   1754 C  CB  . PRO A 1 217 ? -10.899 -16.903 3.451   1.00 11.90 ? 217 PRO B CB  1 
ATOM   1755 C  CG  . PRO A 1 217 ? -9.890  -18.005 3.316   1.00 19.96 ? 217 PRO B CG  1 
ATOM   1756 C  CD  . PRO A 1 217 ? -10.475 -19.246 4.018   1.00 11.97 ? 217 PRO B CD  1 
ATOM   1757 N  N   . ILE A 1 218 ? -13.670 -15.898 4.506   1.00 9.60  ? 218 ILE B N   1 
ATOM   1758 C  CA  . ILE A 1 218 ? -14.987 -15.528 3.966   1.00 10.43 ? 218 ILE B CA  1 
ATOM   1759 C  C   . ILE A 1 218 ? -14.826 -14.820 2.673   1.00 10.14 ? 218 ILE B C   1 
ATOM   1760 O  O   . ILE A 1 218 ? -13.700 -14.438 2.285   1.00 10.80 ? 218 ILE B O   1 
ATOM   1761 C  CB  . ILE A 1 218 ? -15.842 -14.729 4.949   1.00 9.23  ? 218 ILE B CB  1 
ATOM   1762 C  CG1 . ILE A 1 218 ? -15.215 -13.366 5.232   1.00 9.73  ? 218 ILE B CG1 1 
ATOM   1763 C  CG2 . ILE A 1 218 ? -15.987 -15.517 6.261   1.00 11.85 ? 218 ILE B CG2 1 
ATOM   1764 C  CD1 . ILE A 1 218 ? -16.099 -12.433 6.032   1.00 12.64 ? 218 ILE B CD1 1 
ATOM   1765 N  N   A ASN A 1 219 ? -15.857 -14.700 1.818   0.50 9.36  ? 219 ASN B N   1 
ATOM   1766 N  N   B ASN A 1 219 ? -15.993 -14.567 2.038   0.50 9.71  ? 219 ASN B N   1 
ATOM   1767 C  CA  A ASN A 1 219 ? -15.704 -14.058 0.525   0.50 9.37  ? 219 ASN B CA  1 
ATOM   1768 C  CA  B ASN A 1 219 ? -16.025 -13.944 0.709   0.50 9.12  ? 219 ASN B CA  1 
ATOM   1769 C  C   A ASN A 1 219 ? -16.269 -12.651 0.555   0.50 9.76  ? 219 ASN B C   1 
ATOM   1770 C  C   B ASN A 1 219 ? -16.310 -12.466 0.687   0.50 9.75  ? 219 ASN B C   1 
ATOM   1771 O  O   A ASN A 1 219 ? -17.154 -12.346 1.331   0.50 9.55  ? 219 ASN B O   1 
ATOM   1772 O  O   B ASN A 1 219 ? -17.050 -11.920 1.551   0.50 9.14  ? 219 ASN B O   1 
ATOM   1773 C  CB  A ASN A 1 219 ? -16.520 -14.866 -0.501  0.50 11.11 ? 219 ASN B CB  1 
ATOM   1774 C  CB  B ASN A 1 219 ? -17.083 -14.643 -0.236  0.50 10.36 ? 219 ASN B CB  1 
ATOM   1775 C  CG  A ASN A 1 219 ? -16.070 -16.288 -0.582  0.50 13.74 ? 219 ASN B CG  1 
ATOM   1776 C  CG  B ASN A 1 219 ? -18.467 -14.681 0.362   0.50 12.13 ? 219 ASN B CG  1 
ATOM   1777 O  OD1 A ASN A 1 219 ? -16.677 -17.193 0.036   0.50 20.97 ? 219 ASN B OD1 1 
ATOM   1778 O  OD1 B ASN A 1 219 ? -19.475 -14.029 -0.102  0.50 14.04 ? 219 ASN B OD1 1 
ATOM   1779 N  ND2 A ASN A 1 219 ? -15.018 -16.521 -1.303  0.50 14.44 ? 219 ASN B ND2 1 
ATOM   1780 N  ND2 B ASN A 1 219 ? -18.583 -15.473 1.395   0.50 13.47 ? 219 ASN B ND2 1 
ATOM   1781 N  N   . ILE A 1 220 ? -15.727 -11.798 -0.320  1.00 8.74  ? 220 ILE B N   1 
ATOM   1782 C  CA  . ILE A 1 220 ? -16.148 -10.448 -0.598  1.00 10.24 ? 220 ILE B CA  1 
ATOM   1783 C  C   . ILE A 1 220 ? -15.980 -10.221 -2.131  1.00 10.42 ? 220 ILE B C   1 
ATOM   1784 O  O   . ILE A 1 220 ? -15.084 -10.848 -2.692  1.00 10.46 ? 220 ILE B O   1 
ATOM   1785 C  CB  . ILE A 1 220 ? -15.294 -9.397  0.220   1.00 8.80  ? 220 ILE B CB  1 
ATOM   1786 C  CG1 . ILE A 1 220 ? -15.901 -8.026  0.044   1.00 8.98  ? 220 ILE B CG1 1 
ATOM   1787 C  CG2 . ILE A 1 220 ? -13.799 -9.453  -0.150  1.00 10.76 ? 220 ILE B CG2 1 
ATOM   1788 C  CD1 . ILE A 1 220 ? -15.253 -6.932  0.990   1.00 11.05 ? 220 ILE B CD1 1 
ATOM   1789 N  N   . SER A 1 221 ? -16.838 -9.365  -2.717  1.00 9.21  ? 221 SER B N   1 
ATOM   1790 C  CA  . SER A 1 221 ? -16.536 -9.172  -4.163  1.00 9.38  ? 221 SER B CA  1 
ATOM   1791 C  C   . SER A 1 221 ? -15.424 -8.157  -4.326  1.00 10.06 ? 221 SER B C   1 
ATOM   1792 O  O   . SER A 1 221 ? -15.146 -7.354  -3.420  1.00 9.31  ? 221 SER B O   1 
ATOM   1793 C  CB  . SER A 1 221 ? -17.750 -8.625  -4.924  1.00 10.96 ? 221 SER B CB  1 
ATOM   1794 O  OG  . SER A 1 221 ? -18.121 -7.370  -4.518  1.00 10.51 ? 221 SER B OG  1 
ATOM   1795 N  N   A SER A 1 222 ? -14.818 -8.130  -5.513  0.50 11.05 ? 222 SER B N   1 
ATOM   1796 N  N   B SER A 1 222 ? -14.786 -8.147  -5.523  0.50 10.19 ? 222 SER B N   1 
ATOM   1797 C  CA  A SER A 1 222 ? -13.809 -7.138  -5.719  0.50 11.76 ? 222 SER B CA  1 
ATOM   1798 C  CA  B SER A 1 222 ? -13.780 -7.116  -5.774  0.50 10.45 ? 222 SER B CA  1 
ATOM   1799 C  C   A SER A 1 222 ? -14.372 -5.706  -5.679  0.50 9.85  ? 222 SER B C   1 
ATOM   1800 C  C   B SER A 1 222 ? -14.352 -5.722  -5.685  0.50 9.34  ? 222 SER B C   1 
ATOM   1801 O  O   A SER A 1 222 ? -13.721 -4.771  -5.201  0.50 10.10 ? 222 SER B O   1 
ATOM   1802 O  O   B SER A 1 222 ? -13.648 -4.833  -5.206  0.50 10.39 ? 222 SER B O   1 
ATOM   1803 C  CB  A SER A 1 222 ? -13.139 -7.430  -7.032  0.50 14.32 ? 222 SER B CB  1 
ATOM   1804 C  CB  B SER A 1 222 ? -13.097 -7.283  -7.130  0.50 11.16 ? 222 SER B CB  1 
ATOM   1805 O  OG  A SER A 1 222 ? -12.217 -6.444  -7.212  0.50 20.53 ? 222 SER B OG  1 
ATOM   1806 O  OG  B SER A 1 222 ? -14.036 -7.319  -8.209  0.50 11.48 ? 222 SER B OG  1 
ATOM   1807 N  N   . GLN A 1 223 ? -15.607 -5.523  -6.166  1.00 11.05 ? 223 GLN B N   1 
ATOM   1808 C  CA  . GLN A 1 223 ? -16.196 -4.187  -6.111  1.00 11.35 ? 223 GLN B CA  1 
ATOM   1809 C  C   . GLN A 1 223 ? -16.523 -3.741  -4.657  1.00 11.49 ? 223 GLN B C   1 
ATOM   1810 O  O   . GLN A 1 223 ? -16.359 -2.572  -4.346  1.00 13.78 ? 223 GLN B O   1 
ATOM   1811 C  CB  . GLN A 1 223 ? -17.447 -4.153  -6.962  1.00 13.47 ? 223 GLN B CB  1 
ATOM   1812 C  CG  . GLN A 1 223 ? -17.150 -4.407  -8.474  1.00 15.04 ? 223 GLN B CG  1 
ATOM   1813 C  CD  . GLN A 1 223 ? -17.122 -5.844  -8.837  1.00 16.70 ? 223 GLN B CD  1 
ATOM   1814 O  OE1 . GLN A 1 223 ? -17.306 -6.841  -8.048  1.00 15.86 ? 223 GLN B OE1 1 
ATOM   1815 N  NE2 . GLN A 1 223 ? -16.924 -6.052  -10.188 1.00 20.94 ? 223 GLN B NE2 1 
ATOM   1816 N  N   . GLN A 1 224 ? -16.980 -4.693  -3.829  1.00 10.71 ? 224 GLN B N   1 
ATOM   1817 C  CA  . GLN A 1 224 ? -17.184 -4.283  -2.443  1.00 11.74 ? 224 GLN B CA  1 
ATOM   1818 C  C   . GLN A 1 224 ? -15.869 -3.931  -1.776  1.00 10.12 ? 224 GLN B C   1 
ATOM   1819 O  O   . GLN A 1 224 ? -15.781 -2.926  -1.108  1.00 10.87 ? 224 GLN B O   1 
ATOM   1820 C  CB  . GLN A 1 224 ? -17.811 -5.480  -1.674  1.00 11.12 ? 224 GLN B CB  1 
ATOM   1821 C  CG  . GLN A 1 224 ? -19.298 -5.750  -2.027  1.00 11.80 ? 224 GLN B CG  1 
ATOM   1822 C  CD  . GLN A 1 224 ? -19.778 -6.985  -1.242  1.00 10.23 ? 224 GLN B CD  1 
ATOM   1823 O  OE1 . GLN A 1 224 ? -19.086 -8.001  -1.112  1.00 9.75  ? 224 GLN B OE1 1 
ATOM   1824 N  NE2 . GLN A 1 224 ? -21.002 -6.836  -0.677  1.00 11.99 ? 224 GLN B NE2 1 
ATOM   1825 N  N   . LEU A 1 225 ? -14.829 -4.740  -2.002  1.00 9.26  ? 225 LEU B N   1 
ATOM   1826 C  CA  . LEU A 1 225 ? -13.555 -4.418  -1.327  1.00 9.12  ? 225 LEU B CA  1 
ATOM   1827 C  C   . LEU A 1 225 ? -13.018 -3.061  -1.774  1.00 9.98  ? 225 LEU B C   1 
ATOM   1828 O  O   . LEU A 1 225 ? -12.473 -2.298  -1.010  1.00 9.56  ? 225 LEU B O   1 
ATOM   1829 C  CB  . LEU A 1 225 ? -12.567 -5.543  -1.558  1.00 10.09 ? 225 LEU B CB  1 
ATOM   1830 C  CG  . LEU A 1 225 ? -11.181 -5.315  -0.903  1.00 9.56  ? 225 LEU B CG  1 
ATOM   1831 C  CD1 . LEU A 1 225 ? -11.303 -5.177  0.643   1.00 12.60 ? 225 LEU B CD1 1 
ATOM   1832 C  CD2 . LEU A 1 225 ? -10.286 -6.545  -1.183  1.00 10.69 ? 225 LEU B CD2 1 
ATOM   1833 N  N   . ALA A 1 226 ? -13.182 -2.783  -3.097  1.00 10.22 ? 226 ALA B N   1 
ATOM   1834 C  CA  . ALA A 1 226 ? -12.628 -1.521  -3.588  1.00 10.36 ? 226 ALA B CA  1 
ATOM   1835 C  C   . ALA A 1 226 ? -13.283 -0.327  -2.967  1.00 10.52 ? 226 ALA B C   1 
ATOM   1836 O  O   . ALA A 1 226 ? -12.564 0.682   -2.878  1.00 11.28 ? 226 ALA B O   1 
ATOM   1837 C  CB  . ALA A 1 226 ? -12.802 -1.481  -5.154  1.00 10.75 ? 226 ALA B CB  1 
ATOM   1838 N  N   A LYS A 1 227 ? -14.544 -0.401  -2.495  0.50 10.69 ? 227 LYS B N   1 
ATOM   1839 N  N   B LYS A 1 227 ? -14.541 -0.397  -2.497  0.50 10.48 ? 227 LYS B N   1 
ATOM   1840 C  CA  A LYS A 1 227 ? -15.166 0.746   -1.886  0.50 11.38 ? 227 LYS B CA  1 
ATOM   1841 C  CA  B LYS A 1 227 ? -15.197 0.717   -1.855  0.50 10.95 ? 227 LYS B CA  1 
ATOM   1842 C  C   A LYS A 1 227 ? -14.395 1.210   -0.667  0.50 10.80 ? 227 LYS B C   1 
ATOM   1843 C  C   B LYS A 1 227 ? -14.392 1.206   -0.669  0.50 10.66 ? 227 LYS B C   1 
ATOM   1844 O  O   A LYS A 1 227 ? -14.379 2.385   -0.344  0.50 12.86 ? 227 LYS B O   1 
ATOM   1845 O  O   B LYS A 1 227 ? -14.358 2.384   -0.360  0.50 12.92 ? 227 LYS B O   1 
ATOM   1846 C  CB  A LYS A 1 227 ? -16.619 0.542   -1.602  0.50 13.40 ? 227 LYS B CB  1 
ATOM   1847 C  CB  B LYS A 1 227 ? -16.566 0.317   -1.451  0.50 12.59 ? 227 LYS B CB  1 
ATOM   1848 C  CG  A LYS A 1 227 ? -17.370 1.891   -1.497  0.50 16.59 ? 227 LYS B CG  1 
ATOM   1849 C  CG  B LYS A 1 227 ? -17.477 0.162   -2.649  0.50 14.32 ? 227 LYS B CG  1 
ATOM   1850 C  CD  A LYS A 1 227 ? -18.859 1.810   -1.748  0.50 17.07 ? 227 LYS B CD  1 
ATOM   1851 C  CD  B LYS A 1 227 ? -18.487 1.277   -2.873  0.50 19.07 ? 227 LYS B CD  1 
ATOM   1852 C  CE  A LYS A 1 227 ? -19.493 3.157   -2.074  0.50 18.57 ? 227 LYS B CE  1 
ATOM   1853 C  CE  B LYS A 1 227 ? -19.284 1.695   -1.641  0.50 17.41 ? 227 LYS B CE  1 
ATOM   1854 N  NZ  A LYS A 1 227 ? -20.957 2.882   -2.212  0.50 23.23 ? 227 LYS B NZ  1 
ATOM   1855 N  NZ  B LYS A 1 227 ? -20.777 1.723   -1.843  0.50 19.10 ? 227 LYS B NZ  1 
ATOM   1856 N  N   . PHE A 1 228 ? -13.761 0.277   0.070   1.00 9.91  ? 228 PHE B N   1 
ATOM   1857 C  CA  . PHE A 1 228 ? -13.046 0.681   1.284   1.00 10.00 ? 228 PHE B CA  1 
ATOM   1858 C  C   . PHE A 1 228 ? -11.900 1.614   0.975   1.00 11.21 ? 228 PHE B C   1 
ATOM   1859 O  O   . PHE A 1 228 ? -11.520 2.484   1.770   1.00 10.64 ? 228 PHE B O   1 
ATOM   1860 C  CB  . PHE A 1 228 ? -12.531 -0.528  2.076   1.00 10.14 ? 228 PHE B CB  1 
ATOM   1861 C  CG  . PHE A 1 228 ? -13.653 -1.320  2.661   1.00 10.39 ? 228 PHE B CG  1 
ATOM   1862 C  CD1 . PHE A 1 228 ? -14.072 -2.476  2.093   1.00 10.80 ? 228 PHE B CD1 1 
ATOM   1863 C  CD2 . PHE A 1 228 ? -14.361 -0.794  3.776   1.00 10.95 ? 228 PHE B CD2 1 
ATOM   1864 C  CE1 . PHE A 1 228 ? -15.156 -3.183  2.610   1.00 11.92 ? 228 PHE B CE1 1 
ATOM   1865 C  CE2 . PHE A 1 228 ? -15.484 -1.500  4.305   1.00 10.62 ? 228 PHE B CE2 1 
ATOM   1866 C  CZ  . PHE A 1 228 ? -15.927 -2.654  3.669   1.00 10.83 ? 228 PHE B CZ  1 
ATOM   1867 N  N   . ARG A 1 229 ? -11.274 1.466   -0.215  1.00 11.20 ? 229 ARG B N   1 
ATOM   1868 C  CA  . ARG A 1 229 ? -10.115 2.269   -0.567  1.00 11.54 ? 229 ARG B CA  1 
ATOM   1869 C  C   . ARG A 1 229 ? -10.434 3.695   -0.871  1.00 11.27 ? 229 ARG B C   1 
ATOM   1870 O  O   . ARG A 1 229 ? -9.515  4.511   -0.954  1.00 12.46 ? 229 ARG B O   1 
ATOM   1871 C  CB  . ARG A 1 229 ? -9.422  1.631   -1.844  1.00 11.63 ? 229 ARG B CB  1 
ATOM   1872 C  CG  . ARG A 1 229 ? -8.987  0.218   -1.638  1.00 10.84 ? 229 ARG B CG  1 
ATOM   1873 C  CD  . ARG A 1 229 ? -8.213  -0.324  -2.877  1.00 10.56 ? 229 ARG B CD  1 
ATOM   1874 N  NE  . ARG A 1 229 ? -7.792  -1.711  -2.716  1.00 9.65  ? 229 ARG B NE  1 
ATOM   1875 C  CZ  . ARG A 1 229 ? -8.415  -2.773  -3.253  1.00 11.27 ? 229 ARG B CZ  1 
ATOM   1876 N  NH1 . ARG A 1 229 ? -9.350  -2.579  -4.175  1.00 11.66 ? 229 ARG B NH1 1 
ATOM   1877 N  NH2 . ARG A 1 229 ? -8.067  -4.035  -2.906  1.00 11.14 ? 229 ARG B NH2 1 
ATOM   1878 N  N   A SER A 1 230 ? -11.724 3.977   -0.987  0.50 12.47 ? 230 SER B N   1 
ATOM   1879 N  N   B SER A 1 230 ? -11.713 3.992   -0.995  0.50 12.81 ? 230 SER B N   1 
ATOM   1880 C  CA  A SER A 1 230 ? -12.231 5.351   -1.223  0.50 14.05 ? 230 SER B CA  1 
ATOM   1881 C  CA  B SER A 1 230 ? -12.174 5.381   -1.239  0.50 14.43 ? 230 SER B CA  1 
ATOM   1882 C  C   A SER A 1 230 ? -12.516 6.105   0.054   0.50 13.60 ? 230 SER B C   1 
ATOM   1883 C  C   B SER A 1 230 ? -12.256 6.170   0.071   0.50 13.75 ? 230 SER B C   1 
ATOM   1884 O  O   A SER A 1 230 ? -12.907 7.280   -0.008  0.50 12.92 ? 230 SER B O   1 
ATOM   1885 O  O   B SER A 1 230 ? -12.298 7.409   0.086   0.50 11.23 ? 230 SER B O   1 
ATOM   1886 C  CB  A SER A 1 230 ? -13.496 5.304   -2.024  0.50 14.34 ? 230 SER B CB  1 
ATOM   1887 C  CB  B SER A 1 230 ? -13.505 5.339   -1.961  0.50 15.50 ? 230 SER B CB  1 
ATOM   1888 O  OG  A SER A 1 230 ? -14.598 4.921   -1.253  0.50 14.52 ? 230 SER B OG  1 
ATOM   1889 O  OG  B SER A 1 230 ? -13.290 5.134   -3.376  0.50 18.84 ? 230 SER B OG  1 
ATOM   1890 N  N   . LEU A 1 231 ? -12.236 5.512   1.244   1.00 12.75 ? 231 LEU B N   1 
ATOM   1891 C  CA  . LEU A 1 231 ? -12.195 6.325   2.467   1.00 12.92 ? 231 LEU B CA  1 
ATOM   1892 C  C   . LEU A 1 231 ? -10.972 7.200   2.448   1.00 15.21 ? 231 LEU B C   1 
ATOM   1893 O  O   . LEU A 1 231 ? -9.903  6.802   1.945   1.00 15.00 ? 231 LEU B O   1 
ATOM   1894 C  CB  . LEU A 1 231 ? -12.092 5.328   3.663   1.00 13.97 ? 231 LEU B CB  1 
ATOM   1895 C  CG  . LEU A 1 231 ? -13.340 4.527   3.882   1.00 12.42 ? 231 LEU B CG  1 
ATOM   1896 C  CD1 . LEU A 1 231 ? -13.009 3.442   4.993   1.00 13.18 ? 231 LEU B CD1 1 
ATOM   1897 C  CD2 . LEU A 1 231 ? -14.515 5.409   4.355   1.00 13.72 ? 231 LEU B CD2 1 
ATOM   1898 N  N   . LEU A 1 232 ? -11.076 8.370   3.071   1.00 14.76 ? 232 LEU B N   1 
ATOM   1899 C  CA  . LEU A 1 232 ? -9.895  9.266   3.169   1.00 15.85 ? 232 LEU B CA  1 
ATOM   1900 C  C   . LEU A 1 232 ? -9.189  9.055   4.475   1.00 14.49 ? 232 LEU B C   1 
ATOM   1901 O  O   . LEU A 1 232 ? -9.874  8.714   5.523   1.00 15.77 ? 232 LEU B O   1 
ATOM   1902 C  CB  . LEU A 1 232 ? -10.360 10.730  3.134   1.00 17.90 ? 232 LEU B CB  1 
ATOM   1903 C  CG  . LEU A 1 232 ? -11.142 11.073  1.874   1.00 17.57 ? 232 LEU B CG  1 
ATOM   1904 C  CD1 . LEU A 1 232 ? -11.662 12.477  1.983   1.00 23.62 ? 232 LEU B CD1 1 
ATOM   1905 C  CD2 . LEU A 1 232 ? -10.326 10.887  0.638   1.00 24.84 ? 232 LEU B CD2 1 
ATOM   1906 N  N   . CYS A 1 233 ? -7.885  9.264   4.503   1.00 15.01 ? 233 CYS B N   1 
ATOM   1907 C  CA  . CYS A 1 233 ? -7.063  9.264   5.720   1.00 16.86 ? 233 CYS B CA  1 
ATOM   1908 C  C   . CYS A 1 233 ? -6.876  10.702  6.210   1.00 18.96 ? 233 CYS B C   1 
ATOM   1909 O  O   . CYS A 1 233 ? -6.220  10.900  7.237   1.00 20.40 ? 233 CYS B O   1 
ATOM   1910 C  CB  . CYS A 1 233 ? -5.689  8.500   5.653   1.00 14.72 ? 233 CYS B CB  1 
ATOM   1911 S  SG  . CYS A 1 233 ? -4.664  9.225   4.324   1.00 22.48 ? 233 CYS B SG  1 
ATOM   1912 N  N   . THR A 1 234 ? -7.479  11.617  5.492   1.00 19.95 ? 234 THR B N   1 
ATOM   1913 C  CA  . THR A 1 234 ? -7.459  13.054  5.811   1.00 24.44 ? 234 THR B CA  1 
ATOM   1914 C  C   . THR A 1 234 ? -8.895  13.527  6.176   1.00 20.16 ? 234 THR B C   1 
ATOM   1915 O  O   . THR A 1 234 ? -10.013 12.968  5.773   1.00 22.23 ? 234 THR B O   1 
ATOM   1916 C  CB  . THR A 1 234 ? -6.887  13.790  4.562   1.00 21.03 ? 234 THR B CB  1 
ATOM   1917 O  OG1 . THR A 1 234 ? -7.755  13.443  3.464   1.00 22.48 ? 234 THR B OG1 1 
ATOM   1918 C  CG2 . THR A 1 234 ? -5.430  13.472  4.305   1.00 24.29 ? 234 THR B CG2 1 
ATOM   1919 N  N   . ALA A 1 235 ? -8.926  14.581  7.017   1.00 28.76 ? 235 ALA B N   1 
ATOM   1920 C  CA  . ALA A 1 235 ? -10.159 15.181  7.545   1.00 26.44 ? 235 ALA B CA  1 
ATOM   1921 C  C   . ALA A 1 235 ? -10.758 16.192  6.590   1.00 34.00 ? 235 ALA B C   1 
ATOM   1922 O  O   . ALA A 1 235 ? -10.098 16.622  5.645   1.00 30.30 ? 235 ALA B O   1 
ATOM   1923 C  CB  . ALA A 1 235 ? -9.869  15.867  8.906   1.00 28.03 ? 235 ALA B CB  1 
ATOM   1924 N  N   . GLU A 1 236 ? -12.013 16.563  6.797   1.00 38.01 ? 236 GLU B N   1 
ATOM   1925 C  CA  . GLU A 1 236 ? -12.579 17.692  6.023   1.00 44.70 ? 236 GLU B CA  1 
ATOM   1926 C  C   . GLU A 1 236 ? -11.650 18.903  6.070   1.00 37.54 ? 236 GLU B C   1 
ATOM   1927 O  O   . GLU A 1 236 ? -11.130 19.254  7.113   1.00 38.14 ? 236 GLU B O   1 
ATOM   1928 C  CB  . GLU A 1 236 ? -13.943 18.099  6.556   1.00 49.25 ? 236 GLU B CB  1 
ATOM   1929 C  CG  . GLU A 1 236 ? -15.104 17.624  5.706   1.00 63.56 ? 236 GLU B CG  1 
ATOM   1930 C  CD  . GLU A 1 236 ? -16.352 17.405  6.538   1.00 77.94 ? 236 GLU B CD  1 
ATOM   1931 O  OE1 . GLU A 1 236 ? -17.462 17.784  6.081   1.00 76.30 ? 236 GLU B OE1 1 
ATOM   1932 O  OE2 . GLU A 1 236 ? -16.217 16.847  7.660   1.00 83.21 ? 236 GLU B OE2 1 
ATOM   1933 N  N   . GLY A 1 237 ? -11.403 19.498  4.909   1.00 42.57 ? 237 GLY B N   1 
ATOM   1934 C  CA  . GLY A 1 237 ? -10.646 20.752  4.848   1.00 43.83 ? 237 GLY B CA  1 
ATOM   1935 C  C   . GLY A 1 237 ? -9.149  20.606  4.637   1.00 42.29 ? 237 GLY B C   1 
ATOM   1936 O  O   . GLY A 1 237 ? -8.460  21.608  4.460   1.00 41.35 ? 237 GLY B O   1 
ATOM   1937 N  N   . GLU A 1 238 ? -8.650  19.363  4.637   1.00 39.97 ? 238 GLU B N   1 
ATOM   1938 C  CA  . GLU A 1 238 ? -7.201  19.045  4.551   1.00 42.14 ? 238 GLU B CA  1 
ATOM   1939 C  C   . GLU A 1 238 ? -7.000  18.501  3.106   1.00 42.76 ? 238 GLU B C   1 
ATOM   1940 O  O   . GLU A 1 238 ? -7.970  18.062  2.485   1.00 38.62 ? 238 GLU B O   1 
ATOM   1941 C  CB  . GLU A 1 238 ? -6.880  18.015  5.670   1.00 48.57 ? 238 GLU B CB  1 
ATOM   1942 C  CG  . GLU A 1 238 ? -5.472  17.445  5.826   1.00 50.36 ? 238 GLU B CG  1 
ATOM   1943 C  CD  . GLU A 1 238 ? -5.410  16.282  6.845   1.00 58.71 ? 238 GLU B CD  1 
ATOM   1944 O  OE1 . GLU A 1 238 ? -4.300  15.716  7.055   1.00 61.48 ? 238 GLU B OE1 1 
ATOM   1945 O  OE2 . GLU A 1 238 ? -6.457  15.897  7.449   1.00 53.45 ? 238 GLU B OE2 1 
ATOM   1946 N  N   . ALA A 1 239 ? -5.789  18.548  2.544   1.00 38.25 ? 239 ALA B N   1 
ATOM   1947 C  CA  . ALA A 1 239 ? -5.638  18.004  1.166   1.00 41.61 ? 239 ALA B CA  1 
ATOM   1948 C  C   . ALA A 1 239 ? -5.960  16.475  1.166   1.00 36.74 ? 239 ALA B C   1 
ATOM   1949 O  O   . ALA A 1 239 ? -5.387  15.746  1.982   1.00 37.88 ? 239 ALA B O   1 
ATOM   1950 C  CB  . ALA A 1 239 ? -4.231  18.251  0.611   1.00 39.77 ? 239 ALA B CB  1 
ATOM   1951 N  N   . ALA A 1 240 ? -6.837  16.038  0.262   1.00 31.63 ? 240 ALA B N   1 
ATOM   1952 C  CA  . ALA A 1 240 ? -7.338  14.613  0.280   1.00 26.88 ? 240 ALA B CA  1 
ATOM   1953 C  C   . ALA A 1 240 ? -6.238  13.601  0.009   1.00 27.53 ? 240 ALA B C   1 
ATOM   1954 O  O   . ALA A 1 240 ? -5.398  13.741  -0.901  1.00 25.79 ? 240 ALA B O   1 
ATOM   1955 C  CB  . ALA A 1 240 ? -8.493  14.398  -0.711  1.00 32.90 ? 240 ALA B CB  1 
ATOM   1956 N  N   . ALA A 1 241 ? -6.246  12.539  0.806   1.00 19.64 ? 241 ALA B N   1 
ATOM   1957 C  CA  . ALA A 1 241 ? -5.415  11.380  0.483   1.00 15.86 ? 241 ALA B CA  1 
ATOM   1958 C  C   . ALA A 1 241 ? -6.272  10.167  0.877   1.00 16.08 ? 241 ALA B C   1 
ATOM   1959 O  O   . ALA A 1 241 ? -7.101  10.261  1.806   1.00 17.09 ? 241 ALA B O   1 
ATOM   1960 C  CB  . ALA A 1 241 ? -4.129  11.378  1.226   1.00 17.10 ? 241 ALA B CB  1 
ATOM   1961 N  N   . PHE A 1 242 ? -6.175  9.127   0.084   1.00 13.49 ? 242 PHE B N   1 
ATOM   1962 C  CA  . PHE A 1 242 ? -7.035  7.954   0.172   1.00 12.69 ? 242 PHE B CA  1 
ATOM   1963 C  C   . PHE A 1 242 ? -6.343  6.853   0.910   1.00 11.47 ? 242 PHE B C   1 
ATOM   1964 O  O   . PHE A 1 242 ? -5.170  6.614   0.788   1.00 12.69 ? 242 PHE B O   1 
ATOM   1965 C  CB  . PHE A 1 242 ? -7.374  7.483   -1.278  1.00 13.83 ? 242 PHE B CB  1 
ATOM   1966 C  CG  . PHE A 1 242 ? -8.173  8.468   -2.030  1.00 15.48 ? 242 PHE B CG  1 
ATOM   1967 C  CD1 . PHE A 1 242 ? -7.514  9.411   -2.854  1.00 14.85 ? 242 PHE B CD1 1 
ATOM   1968 C  CD2 . PHE A 1 242 ? -9.561  8.504   -1.912  1.00 15.68 ? 242 PHE B CD2 1 
ATOM   1969 C  CE1 . PHE A 1 242 ? -8.300  10.332  -3.540  1.00 17.85 ? 242 PHE B CE1 1 
ATOM   1970 C  CE2 . PHE A 1 242 ? -10.347 9.395   -2.617  1.00 20.04 ? 242 PHE B CE2 1 
ATOM   1971 C  CZ  . PHE A 1 242 ? -9.675  10.308  -3.429  1.00 18.54 ? 242 PHE B CZ  1 
ATOM   1972 N  N   . LEU A 1 243 ? -7.208  6.131   1.697   1.00 12.16 ? 243 LEU B N   1 
ATOM   1973 C  CA  . LEU A 1 243 ? -6.707  4.964   2.464   1.00 12.49 ? 243 LEU B CA  1 
ATOM   1974 C  C   . LEU A 1 243 ? -6.703  3.729   1.580   1.00 10.68 ? 243 LEU B C   1 
ATOM   1975 O  O   . LEU A 1 243 ? -7.564  2.803   1.741   1.00 10.32 ? 243 LEU B O   1 
ATOM   1976 C  CB  . LEU A 1 243 ? -7.617  4.893   3.707   1.00 12.76 ? 243 LEU B CB  1 
ATOM   1977 C  CG  . LEU A 1 243 ? -7.178  3.853   4.704   1.00 12.09 ? 243 LEU B CG  1 
ATOM   1978 C  CD1 . LEU A 1 243 ? -5.881  4.251   5.354   1.00 12.34 ? 243 LEU B CD1 1 
ATOM   1979 C  CD2 . LEU A 1 243 ? -8.301  3.701   5.807   1.00 13.40 ? 243 LEU B CD2 1 
ATOM   1980 N  N   . VAL A 1 244 ? -5.795  3.707   0.636   1.00 10.66 ? 244 VAL B N   1 
ATOM   1981 C  CA  . VAL A 1 244 ? -5.817  2.591   -0.346  1.00 10.10 ? 244 VAL B CA  1 
ATOM   1982 C  C   . VAL A 1 244 ? -5.236  1.290   0.209   1.00 10.44 ? 244 VAL B C   1 
ATOM   1983 O  O   . VAL A 1 244 ? -5.432  0.191   -0.327  1.00 10.95 ? 244 VAL B O   1 
ATOM   1984 C  CB  . VAL A 1 244 ? -5.056  2.990   -1.669  1.00 11.99 ? 244 VAL B CB  1 
ATOM   1985 C  CG1 . VAL A 1 244 ? -5.780  4.134   -2.367  1.00 13.07 ? 244 VAL B CG1 1 
ATOM   1986 C  CG2 . VAL A 1 244 ? -3.564  3.189   -1.456  1.00 13.11 ? 244 VAL B CG2 1 
ATOM   1987 N  N   . SER A 1 245 ? -4.511  1.434   1.360   1.00 9.85  ? 245 SER B N   1 
ATOM   1988 C  CA  . SER A 1 245 ? -3.842  0.293   1.974   1.00 9.87  ? 245 SER B CA  1 
ATOM   1989 C  C   . SER A 1 245 ? -3.625  0.603   3.407   1.00 10.21 ? 245 SER B C   1 
ATOM   1990 O  O   . SER A 1 245 ? -3.225  1.672   3.797   1.00 11.46 ? 245 SER B O   1 
ATOM   1991 C  CB  . SER A 1 245 ? -2.490  0.010   1.309   1.00 11.77 ? 245 SER B CB  1 
ATOM   1992 O  OG  . SER A 1 245 ? -1.870  -1.172  1.795   1.00 12.70 ? 245 SER B OG  1 
ATOM   1993 N  N   . ASN A 1 246 ? -3.857  -0.409  4.272   1.00 9.64  ? 246 ASN B N   1 
ATOM   1994 C  CA  . ASN A 1 246 ? -3.806  -0.111  5.761   1.00 9.33  ? 246 ASN B CA  1 
ATOM   1995 C  C   . ASN A 1 246 ? -3.435  -1.415  6.445   1.00 10.07 ? 246 ASN B C   1 
ATOM   1996 O  O   . ASN A 1 246 ? -4.032  -1.728  7.491   1.00 10.31 ? 246 ASN B O   1 
ATOM   1997 C  CB  . ASN A 1 246 ? -5.095  0.471   6.279   1.00 9.34  ? 246 ASN B CB  1 
ATOM   1998 C  CG  . ASN A 1 246 ? -6.237  -0.467  6.179   1.00 8.16  ? 246 ASN B CG  1 
ATOM   1999 O  OD1 . ASN A 1 246 ? -6.175  -1.446  5.425   1.00 10.93 ? 246 ASN B OD1 1 
ATOM   2000 N  ND2 . ASN A 1 246 ? -7.325  -0.163  6.887   1.00 10.21 ? 246 ASN B ND2 1 
ATOM   2001 N  N   . HIS A 1 247 ? -2.449  -2.145  5.985   1.00 9.38  ? 247 HIS B N   1 
ATOM   2002 C  CA  . HIS A 1 247 ? -1.977  -3.379  6.680   1.00 9.51  ? 247 HIS B CA  1 
ATOM   2003 C  C   . HIS A 1 247 ? -0.561  -3.312  7.055   1.00 11.00 ? 247 HIS B C   1 
ATOM   2004 O  O   . HIS A 1 247 ? 0.314   -2.692  6.343   1.00 12.08 ? 247 HIS B O   1 
ATOM   2005 C  CB  . HIS A 1 247 ? -2.220  -4.636  5.810   1.00 12.27 ? 247 HIS B CB  1 
ATOM   2006 C  CG  . HIS A 1 247 ? -1.489  -4.635  4.464   1.00 12.12 ? 247 HIS B CG  1 
ATOM   2007 N  ND1 . HIS A 1 247 ? -2.003  -4.010  3.389   1.00 11.44 ? 247 HIS B ND1 1 
ATOM   2008 C  CD2 . HIS A 1 247 ? -0.229  -5.088  4.112   1.00 14.65 ? 247 HIS B CD2 1 
ATOM   2009 C  CE1 . HIS A 1 247 ? -1.137  -4.164  2.318   1.00 11.98 ? 247 HIS B CE1 1 
ATOM   2010 N  NE2 . HIS A 1 247 ? -0.065  -4.765  2.737   1.00 14.18 ? 247 HIS B NE2 1 
ATOM   2011 N  N   . ARG A 1 248 ? -0.218  -3.890  8.221   1.00 10.25 ? 248 ARG B N   1 
ATOM   2012 C  CA  . ARG A 1 248 ? 1.139   -3.808  8.733   1.00 11.71 ? 248 ARG B CA  1 
ATOM   2013 C  C   . ARG A 1 248 ? 1.817   -5.068  8.273   1.00 12.51 ? 248 ARG B C   1 
ATOM   2014 O  O   . ARG A 1 248 ? 1.201   -6.145  8.229   1.00 12.70 ? 248 ARG B O   1 
ATOM   2015 C  CB  . ARG A 1 248 ? 1.085   -3.858  10.297  1.00 11.24 ? 248 ARG B CB  1 
ATOM   2016 C  CG  . ARG A 1 248 ? 2.483   -3.672  10.945  1.00 11.99 ? 248 ARG B CG  1 
ATOM   2017 C  CD  . ARG A 1 248 ? 2.436   -3.842  12.472  1.00 11.51 ? 248 ARG B CD  1 
ATOM   2018 N  NE  . ARG A 1 248 ? 3.694   -3.340  13.023  1.00 13.63 ? 248 ARG B NE  1 
ATOM   2019 C  CZ  . ARG A 1 248 ? 4.199   -3.671  14.206  1.00 13.25 ? 248 ARG B CZ  1 
ATOM   2020 N  NH1 . ARG A 1 248 ? 3.554   -4.513  15.001  1.00 13.67 ? 248 ARG B NH1 1 
ATOM   2021 N  NH2 . ARG A 1 248 ? 5.356   -3.150  14.594  1.00 15.26 ? 248 ARG B NH2 1 
ATOM   2022 N  N   . PRO A 1 249 ? 3.139   -4.966  7.916   1.00 13.33 ? 249 PRO B N   1 
ATOM   2023 C  CA  . PRO A 1 249 ? 3.830   -6.191  7.571   1.00 13.34 ? 249 PRO B CA  1 
ATOM   2024 C  C   . PRO A 1 249 ? 3.973   -7.182  8.704   1.00 14.30 ? 249 PRO B C   1 
ATOM   2025 O  O   . PRO A 1 249 ? 3.896   -6.768  9.893   1.00 14.12 ? 249 PRO B O   1 
ATOM   2026 C  CB  . PRO A 1 249 ? 5.279   -5.682  7.137   1.00 16.92 ? 249 PRO B CB  1 
ATOM   2027 C  CG  . PRO A 1 249 ? 5.100   -4.217  6.872   1.00 20.52 ? 249 PRO B CG  1 
ATOM   2028 C  CD  . PRO A 1 249 ? 3.886   -3.708  7.710   1.00 15.71 ? 249 PRO B CD  1 
ATOM   2029 N  N   . PRO A 1 250 ? 4.247   -8.418  8.400   1.00 14.97 ? 250 PRO B N   1 
ATOM   2030 C  CA  . PRO A 1 250 ? 4.515   -9.436  9.498   1.00 14.75 ? 250 PRO B CA  1 
ATOM   2031 C  C   . PRO A 1 250 ? 5.759   -9.082  10.306  1.00 15.89 ? 250 PRO B C   1 
ATOM   2032 O  O   . PRO A 1 250 ? 6.716   -8.452  9.799   1.00 18.28 ? 250 PRO B O   1 
ATOM   2033 C  CB  . PRO A 1 250 ? 4.706   -10.763 8.763   1.00 15.79 ? 250 PRO B CB  1 
ATOM   2034 C  CG  . PRO A 1 250 ? 5.201   -10.265 7.424   1.00 22.99 ? 250 PRO B CG  1 
ATOM   2035 C  CD  . PRO A 1 250 ? 4.565   -8.939  7.046   1.00 19.03 ? 250 PRO B CD  1 
ATOM   2036 N  N   . GLN A 1 251 ? 5.740   -9.452  11.602  1.00 12.37 ? 251 GLN B N   1 
ATOM   2037 C  CA  . GLN A 1 251 ? 6.784   -9.077  12.561  1.00 13.56 ? 251 GLN B CA  1 
ATOM   2038 C  C   . GLN A 1 251 ? 7.434   -10.364 13.046  1.00 14.06 ? 251 GLN B C   1 
ATOM   2039 O  O   . GLN A 1 251 ? 6.918   -11.506 12.959  1.00 14.11 ? 251 GLN B O   1 
ATOM   2040 C  CB  . GLN A 1 251 ? 6.166   -8.349  13.747  1.00 13.54 ? 251 GLN B CB  1 
ATOM   2041 C  CG  . GLN A 1 251 ? 5.452   -7.120  13.262  1.00 13.34 ? 251 GLN B CG  1 
ATOM   2042 C  CD  . GLN A 1 251 ? 6.426   -6.167  12.530  1.00 19.55 ? 251 GLN B CD  1 
ATOM   2043 O  OE1 . GLN A 1 251 ? 7.528   -5.848  13.031  1.00 21.87 ? 251 GLN B OE1 1 
ATOM   2044 N  NE2 . GLN A 1 251 ? 6.004   -5.639  11.401  1.00 17.44 ? 251 GLN B NE2 1 
ATOM   2045 N  N   . PRO A 1 252 ? 8.675   -10.239 13.534  1.00 14.84 ? 252 PRO B N   1 
ATOM   2046 C  CA  . PRO A 1 252 ? 9.354   -11.441 13.955  1.00 15.72 ? 252 PRO B CA  1 
ATOM   2047 C  C   . PRO A 1 252 ? 8.679   -12.278 15.111  1.00 14.26 ? 252 PRO B C   1 
ATOM   2048 O  O   . PRO A 1 252 ? 8.236   -11.659 16.085  1.00 15.42 ? 252 PRO B O   1 
ATOM   2049 C  CB  . PRO A 1 252 ? 10.686  -10.873 14.510  1.00 16.67 ? 252 PRO B CB  1 
ATOM   2050 C  CG  . PRO A 1 252 ? 10.870  -9.558  13.833  1.00 18.01 ? 252 PRO B CG  1 
ATOM   2051 C  CD  . PRO A 1 252 ? 9.456   -9.021  13.714  1.00 16.59 ? 252 PRO B CD  1 
ATOM   2052 N  N   . LEU A 1 253 ? 8.711   -13.566 14.887  1.00 15.57 ? 253 LEU B N   1 
ATOM   2053 C  CA  . LEU A 1 253 ? 8.068   -14.485 15.856  1.00 15.64 ? 253 LEU B CA  1 
ATOM   2054 C  C   . LEU A 1 253 ? 8.727   -14.490 17.229  1.00 19.31 ? 253 LEU B C   1 
ATOM   2055 O  O   . LEU A 1 253 ? 8.063   -14.582 18.263  1.00 16.58 ? 253 LEU B O   1 
ATOM   2056 C  CB  . LEU A 1 253 ? 7.922   -15.859 15.283  1.00 19.12 ? 253 LEU B CB  1 
ATOM   2057 C  CG  . LEU A 1 253 ? 6.959   -16.767 16.112  1.00 17.91 ? 253 LEU B CG  1 
ATOM   2058 C  CD1 . LEU A 1 253 ? 5.492   -16.237 16.268  1.00 17.72 ? 253 LEU B CD1 1 
ATOM   2059 C  CD2 . LEU A 1 253 ? 6.881   -18.109 15.442  1.00 20.82 ? 253 LEU B CD2 1 
ATOM   2060 N  N   . LYS A 1 254 ? 10.053  -14.328 17.212  1.00 17.45 ? 254 LYS B N   1 
ATOM   2061 C  CA  . LYS A 1 254 ? 10.797  -14.184 18.440  1.00 20.11 ? 254 LYS B CA  1 
ATOM   2062 C  C   . LYS A 1 254 ? 10.527  -15.365 19.490  1.00 16.41 ? 254 LYS B C   1 
ATOM   2063 O  O   . LYS A 1 254 ? 10.453  -15.088 20.678  1.00 17.62 ? 254 LYS B O   1 
ATOM   2064 C  CB  . LYS A 1 254 ? 10.727  -12.808 18.959  1.00 21.23 ? 254 LYS B CB  1 
ATOM   2065 C  CG  . LYS A 1 254 ? 11.565  -11.945 18.039  1.00 23.93 ? 254 LYS B CG  1 
ATOM   2066 C  CD  . LYS A 1 254 ? 11.510  -10.591 18.578  1.00 25.57 ? 254 LYS B CD  1 
ATOM   2067 C  CE  . LYS A 1 254 ? 12.514  -9.689  17.789  1.00 28.48 ? 254 LYS B CE  1 
ATOM   2068 N  NZ  . LYS A 1 254 ? 12.368  -8.348  18.363  1.00 34.77 ? 254 LYS B NZ  1 
ATOM   2069 N  N   . GLY A 1 255 ? 10.374  -16.547 18.986  1.00 16.79 ? 255 GLY B N   1 
ATOM   2070 C  CA  . GLY A 1 255 ? 10.309  -17.704 19.937  1.00 18.66 ? 255 GLY B CA  1 
ATOM   2071 C  C   . GLY A 1 255 ? 8.942   -18.018 20.493  1.00 17.29 ? 255 GLY B C   1 
ATOM   2072 O  O   . GLY A 1 255 ? 8.802   -18.896 21.346  1.00 19.19 ? 255 GLY B O   1 
ATOM   2073 N  N   . ARG A 1 256 ? 7.932   -17.213 20.113  1.00 15.91 ? 256 ARG B N   1 
ATOM   2074 C  CA  . ARG A 1 256 ? 6.530   -17.541 20.514  1.00 15.68 ? 256 ARG B CA  1 
ATOM   2075 C  C   . ARG A 1 256 ? 6.068   -18.834 19.888  1.00 14.89 ? 256 ARG B C   1 
ATOM   2076 O  O   . ARG A 1 256 ? 6.473   -19.273 18.804  1.00 17.48 ? 256 ARG B O   1 
ATOM   2077 C  CB  . ARG A 1 256 ? 5.665   -16.329 20.101  1.00 15.28 ? 256 ARG B CB  1 
ATOM   2078 C  CG  . ARG A 1 256 ? 5.863   -15.180 20.880  1.00 13.06 ? 256 ARG B CG  1 
ATOM   2079 C  CD  . ARG A 1 256 ? 5.025   -13.970 20.426  1.00 13.56 ? 256 ARG B CD  1 
ATOM   2080 N  NE  . ARG A 1 256 ? 5.608   -13.444 19.173  1.00 13.86 ? 256 ARG B NE  1 
ATOM   2081 C  CZ  . ARG A 1 256 ? 5.075   -12.458 18.481  1.00 13.76 ? 256 ARG B CZ  1 
ATOM   2082 N  NH1 . ARG A 1 256 ? 3.823   -12.024 18.783  1.00 13.65 ? 256 ARG B NH1 1 
ATOM   2083 N  NH2 . ARG A 1 256 ? 5.694   -12.054 17.357  1.00 13.62 ? 256 ARG B NH2 1 
ATOM   2084 N  N   . LYS A 1 257 ? 5.126   -19.523 20.576  1.00 15.24 ? 257 LYS B N   1 
ATOM   2085 C  CA  . LYS A 1 257 ? 4.531   -20.735 20.104  1.00 17.96 ? 257 LYS B CA  1 
ATOM   2086 C  C   . LYS A 1 257 ? 3.183   -20.329 19.450  1.00 15.44 ? 257 LYS B C   1 
ATOM   2087 O  O   . LYS A 1 257 ? 2.340   -19.731 20.137  1.00 16.58 ? 257 LYS B O   1 
ATOM   2088 C  CB  . LYS A 1 257 ? 4.238   -21.665 21.353  1.00 18.89 ? 257 LYS B CB  1 
ATOM   2089 C  CG  . LYS A 1 257 ? 3.735   -23.016 20.986  1.00 20.34 ? 257 LYS B CG  1 
ATOM   2090 C  CD  . LYS A 1 257 ? 3.194   -23.861 22.146  1.00 20.73 ? 257 LYS B CD  1 
ATOM   2091 C  CE  . LYS A 1 257 ? 4.265   -24.193 23.205  1.00 24.04 ? 257 LYS B CE  1 
ATOM   2092 N  NZ  . LYS A 1 257 ? 3.614   -25.167 24.193  1.00 24.20 ? 257 LYS B NZ  1 
ATOM   2093 N  N   . VAL A 1 258 ? 3.051   -20.729 18.206  1.00 13.63 ? 258 VAL B N   1 
ATOM   2094 C  CA  . VAL A 1 258 ? 1.722   -20.602 17.546  1.00 13.82 ? 258 VAL B CA  1 
ATOM   2095 C  C   . VAL A 1 258 ? 1.107   -21.960 17.681  1.00 13.99 ? 258 VAL B C   1 
ATOM   2096 O  O   . VAL A 1 258 ? 1.697   -22.988 17.286  1.00 16.09 ? 258 VAL B O   1 
ATOM   2097 C  CB  . VAL A 1 258 ? 1.892   -20.282 16.054  1.00 14.48 ? 258 VAL B CB  1 
ATOM   2098 C  CG1 . VAL A 1 258 ? 0.476   -20.074 15.483  1.00 14.21 ? 258 VAL B CG1 1 
ATOM   2099 C  CG2 . VAL A 1 258 ? 2.772   -19.034 15.865  1.00 15.31 ? 258 VAL B CG2 1 
ATOM   2100 N  N   . ARG A 1 259 ? -0.132  -22.010 18.163  1.00 13.25 ? 259 ARG B N   1 
ATOM   2101 C  CA  . ARG A 1 259 ? -0.825  -23.291 18.425  1.00 13.95 ? 259 ARG B CA  1 
ATOM   2102 C  C   . ARG A 1 259 ? -2.019  -23.405 17.478  1.00 12.47 ? 259 ARG B C   1 
ATOM   2103 O  O   . ARG A 1 259 ? -2.599  -22.336 17.065  1.00 13.03 ? 259 ARG B O   1 
ATOM   2104 C  CB  . ARG A 1 259 ? -1.315  -23.304 19.855  1.00 13.48 ? 259 ARG B CB  1 
ATOM   2105 C  CG  . ARG A 1 259 ? -0.153  -23.397 20.883  1.00 13.92 ? 259 ARG B CG  1 
ATOM   2106 C  CD  . ARG A 1 259 ? -0.676  -23.433 22.301  1.00 15.26 ? 259 ARG B CD  1 
ATOM   2107 N  NE  . ARG A 1 259 ? -1.309  -22.190 22.710  1.00 14.42 ? 259 ARG B NE  1 
ATOM   2108 C  CZ  . ARG A 1 259 ? -2.253  -22.090 23.619  1.00 13.43 ? 259 ARG B CZ  1 
ATOM   2109 N  NH1 . ARG A 1 259 ? -2.644  -23.178 24.318  1.00 15.46 ? 259 ARG B NH1 1 
ATOM   2110 N  NH2 . ARG A 1 259 ? -2.680  -20.895 23.961  1.00 12.02 ? 259 ARG B NH2 1 
ATOM   2111 N  N   . ALA A 1 260 ? -2.410  -24.582 17.162  1.00 12.18 ? 260 ALA B N   1 
ATOM   2112 C  CA  . ALA A 1 260 ? -3.566  -24.905 16.323  1.00 12.54 ? 260 ALA B CA  1 
ATOM   2113 C  C   . ALA A 1 260 ? -4.599  -25.567 17.107  1.00 14.27 ? 260 ALA B C   1 
ATOM   2114 O  O   . ALA A 1 260 ? -4.313  -26.489 17.985  1.00 15.40 ? 260 ALA B O   1 
ATOM   2115 C  CB  . ALA A 1 260 ? -3.152  -25.702 15.108  1.00 16.16 ? 260 ALA B CB  1 
ATOM   2116 N  N   . SER A 1 261 ? -5.867  -25.241 16.911  1.00 12.49 ? 261 SER B N   1 
ATOM   2117 C  CA  . SER A 1 261 ? -7.031  -25.903 17.556  1.00 13.33 ? 261 SER B CA  1 
ATOM   2118 C  C   . SER A 1 261 ? -7.409  -27.232 16.884  1.00 12.51 ? 261 SER B C   1 
ATOM   2119 O  O   . SER A 1 261 ? -8.421  -27.794 17.283  1.00 14.57 ? 261 SER B O   1 
ATOM   2120 C  CB  . SER A 1 261 ? -8.221  -24.944 17.578  1.00 12.61 ? 261 SER B CB  1 
ATOM   2121 O  OG  . SER A 1 261 ? -8.824  -24.873 16.297  1.00 12.07 ? 261 SER B OG  1 
ATOM   2122 N  N   . PHE A 1 262 ? -6.777  -27.625 15.793  1.00 13.15 ? 262 PHE B N   1 
ATOM   2123 C  CA  . PHE A 1 262 ? -7.221  -28.662 14.904  1.00 14.59 ? 262 PHE B CA  1 
ATOM   2124 C  C   . PHE A 1 262 ? -5.938  -29.304 14.358  1.00 16.55 ? 262 PHE B C   1 
ATOM   2125 O  O   . PHE A 1 262 ? -4.855  -28.717 14.407  1.00 16.87 ? 262 PHE B O   1 
ATOM   2126 C  CB  . PHE A 1 262 ? -8.067  -28.022 13.778  1.00 14.88 ? 262 PHE B CB  1 
ATOM   2127 C  CG  . PHE A 1 262 ? -7.287  -27.088 12.900  1.00 14.45 ? 262 PHE B CG  1 
ATOM   2128 C  CD1 . PHE A 1 262 ? -6.707  -27.514 11.722  1.00 16.65 ? 262 PHE B CD1 1 
ATOM   2129 C  CD2 . PHE A 1 262 ? -7.022  -25.776 13.357  1.00 12.22 ? 262 PHE B CD2 1 
ATOM   2130 C  CE1 . PHE A 1 262 ? -5.875  -26.646 10.979  1.00 18.42 ? 262 PHE B CE1 1 
ATOM   2131 C  CE2 . PHE A 1 262 ? -6.237  -24.868 12.561  1.00 14.93 ? 262 PHE B CE2 1 
ATOM   2132 C  CZ  . PHE A 1 262 ? -5.627  -25.319 11.386  1.00 16.87 ? 262 PHE B CZ  1 
ATOM   2133 N  N   . HIS A 1 263 ? -6.101  -30.496 13.800  1.00 20.76 ? 263 HIS B N   1 
ATOM   2134 C  CA  . HIS A 1 263 ? -4.997  -31.180 13.037  1.00 22.90 ? 263 HIS B CA  1 
ATOM   2135 C  C   . HIS A 1 263 ? -5.621  -32.172 12.102  1.00 32.08 ? 263 HIS B C   1 
ATOM   2136 O  O   . HIS A 1 263 ? -4.854  -32.977 11.517  1.00 31.46 ? 263 HIS B O   1 
ATOM   2137 C  CB  . HIS A 1 263 ? -3.930  -31.800 13.921  1.00 26.35 ? 263 HIS B CB  1 
ATOM   2138 C  CG  . HIS A 1 263 ? -4.435  -32.818 14.920  1.00 29.12 ? 263 HIS B CG  1 
ATOM   2139 N  ND1 . HIS A 1 263 ? -5.770  -33.108 15.118  1.00 32.90 ? 263 HIS B ND1 1 
ATOM   2140 C  CD2 . HIS A 1 263 ? -3.754  -33.607 15.787  1.00 28.52 ? 263 HIS B CD2 1 
ATOM   2141 C  CE1 . HIS A 1 263 ? -5.887  -34.035 16.057  1.00 31.84 ? 263 HIS B CE1 1 
ATOM   2142 N  NE2 . HIS A 1 263 ? -4.678  -34.352 16.481  1.00 34.00 ? 263 HIS B NE2 1 
ATOM   2143 O  OXT . HIS A 1 263 ? -6.840  -32.203 11.933  1.00 31.82 ? 263 HIS B OXT 1 
ATOM   2144 N  N   . SER B 1 6   ? -50.772 -42.200 26.454  1.00 40.69 ? 6   SER A N   1 
ATOM   2145 C  CA  . SER B 1 6   ? -50.832 -42.349 27.949  1.00 40.73 ? 6   SER A CA  1 
ATOM   2146 C  C   . SER B 1 6   ? -49.517 -42.631 28.692  1.00 31.26 ? 6   SER A C   1 
ATOM   2147 O  O   . SER B 1 6   ? -49.555 -42.736 29.900  1.00 27.70 ? 6   SER A O   1 
ATOM   2148 C  CB  . SER B 1 6   ? -51.843 -43.443 28.364  1.00 40.35 ? 6   SER A CB  1 
ATOM   2149 O  OG  . SER B 1 6   ? -53.178 -42.998 28.176  1.00 58.77 ? 6   SER A OG  1 
ATOM   2150 N  N   . TRP B 1 7   ? -48.360 -42.721 28.018  1.00 25.92 ? 7   TRP A N   1 
ATOM   2151 C  CA  . TRP B 1 7   ? -47.086 -42.984 28.757  1.00 21.28 ? 7   TRP A CA  1 
ATOM   2152 C  C   . TRP B 1 7   ? -46.728 -41.840 29.693  1.00 16.71 ? 7   TRP A C   1 
ATOM   2153 O  O   . TRP B 1 7   ? -47.115 -40.704 29.491  1.00 17.66 ? 7   TRP A O   1 
ATOM   2154 C  CB  . TRP B 1 7   ? -45.931 -43.349 27.817  1.00 16.27 ? 7   TRP A CB  1 
ATOM   2155 C  CG  . TRP B 1 7   ? -45.488 -42.154 27.031  1.00 18.10 ? 7   TRP A CG  1 
ATOM   2156 C  CD1 . TRP B 1 7   ? -45.936 -41.738 25.762  1.00 19.06 ? 7   TRP A CD1 1 
ATOM   2157 C  CD2 . TRP B 1 7   ? -44.456 -41.218 27.413  1.00 16.27 ? 7   TRP A CD2 1 
ATOM   2158 N  NE1 . TRP B 1 7   ? -45.291 -40.577 25.382  1.00 18.30 ? 7   TRP A NE1 1 
ATOM   2159 C  CE2 . TRP B 1 7   ? -44.344 -40.225 26.333  1.00 16.57 ? 7   TRP A CE2 1 
ATOM   2160 C  CE3 . TRP B 1 7   ? -43.608 -41.087 28.568  1.00 14.45 ? 7   TRP A CE3 1 
ATOM   2161 C  CZ2 . TRP B 1 7   ? -43.424 -39.191 26.420  1.00 15.77 ? 7   TRP A CZ2 1 
ATOM   2162 C  CZ3 . TRP B 1 7   ? -42.655 -40.055 28.600  1.00 13.98 ? 7   TRP A CZ3 1 
ATOM   2163 C  CH2 . TRP B 1 7   ? -42.616 -39.084 27.592  1.00 15.66 ? 7   TRP A CH2 1 
ATOM   2164 N  N   . GLY B 1 8   ? -45.994 -42.157 30.766  1.00 15.50 ? 8   GLY A N   1 
ATOM   2165 C  CA  . GLY B 1 8   ? -45.471 -41.042 31.619  1.00 13.92 ? 8   GLY A CA  1 
ATOM   2166 C  C   . GLY B 1 8   ? -44.463 -41.627 32.535  1.00 11.42 ? 8   GLY A C   1 
ATOM   2167 O  O   . GLY B 1 8   ? -43.632 -42.500 32.226  1.00 12.82 ? 8   GLY A O   1 
ATOM   2168 N  N   . TYR B 1 9   ? -44.457 -41.094 33.796  1.00 13.51 ? 9   TYR A N   1 
ATOM   2169 C  CA  . TYR B 1 9   ? -43.450 -41.559 34.746  1.00 13.94 ? 9   TYR A CA  1 
ATOM   2170 C  C   . TYR B 1 9   ? -44.094 -41.918 36.080  1.00 15.03 ? 9   TYR A C   1 
ATOM   2171 O  O   . TYR B 1 9   ? -43.391 -41.996 37.076  1.00 17.60 ? 9   TYR A O   1 
ATOM   2172 C  CB  . TYR B 1 9   ? -42.403 -40.416 35.006  1.00 13.48 ? 9   TYR A CB  1 
ATOM   2173 C  CG  . TYR B 1 9   ? -41.613 -40.082 33.762  1.00 10.27 ? 9   TYR A CG  1 
ATOM   2174 C  CD1 . TYR B 1 9   ? -40.397 -40.689 33.524  1.00 10.77 ? 9   TYR A CD1 1 
ATOM   2175 C  CD2 . TYR B 1 9   ? -42.056 -39.053 32.919  1.00 11.10 ? 9   TYR A CD2 1 
ATOM   2176 C  CE1 . TYR B 1 9   ? -39.663 -40.394 32.371  1.00 9.51  ? 9   TYR A CE1 1 
ATOM   2177 C  CE2 . TYR B 1 9   ? -41.304 -38.743 31.780  1.00 10.10 ? 9   TYR A CE2 1 
ATOM   2178 C  CZ  . TYR B 1 9   ? -40.113 -39.398 31.568  1.00 10.26 ? 9   TYR A CZ  1 
ATOM   2179 O  OH  . TYR B 1 9   ? -39.378 -39.055 30.433  1.00 10.94 ? 9   TYR A OH  1 
ATOM   2180 N  N   . ARG B 1 10  ? -45.422 -42.095 36.044  1.00 15.86 ? 10  ARG A N   1 
ATOM   2181 C  CA  . ARG B 1 10  ? -46.133 -42.618 37.295  1.00 18.87 ? 10  ARG A CA  1 
ATOM   2182 C  C   . ARG B 1 10  ? -45.989 -44.156 37.391  1.00 20.67 ? 10  ARG A C   1 
ATOM   2183 O  O   . ARG B 1 10  ? -45.536 -44.839 36.486  1.00 18.78 ? 10  ARG A O   1 
ATOM   2184 C  CB  . ARG B 1 10  ? -47.532 -42.091 37.187  1.00 20.60 ? 10  ARG A CB  1 
ATOM   2185 C  CG  . ARG B 1 10  ? -47.625 -40.561 37.174  1.00 25.93 ? 10  ARG A CG  1 
ATOM   2186 C  CD  . ARG B 1 10  ? -48.972 -39.958 36.796  1.00 37.75 ? 10  ARG A CD  1 
ATOM   2187 N  NE  . ARG B 1 10  ? -49.953 -40.000 37.902  1.00 43.49 ? 10  ARG A NE  1 
ATOM   2188 C  CZ  . ARG B 1 10  ? -51.245 -39.590 37.838  1.00 53.59 ? 10  ARG A CZ  1 
ATOM   2189 N  NH1 . ARG B 1 10  ? -51.783 -39.047 36.711  1.00 44.02 ? 10  ARG A NH1 1 
ATOM   2190 N  NH2 . ARG B 1 10  ? -52.026 -39.716 38.928  1.00 49.37 ? 10  ARG A NH2 1 
ATOM   2191 N  N   . GLU B 1 11  ? -46.492 -44.751 38.504  1.00 24.20 ? 11  GLU A N   1 
ATOM   2192 C  CA  . GLU B 1 11  ? -46.395 -46.184 38.673  1.00 22.71 ? 11  GLU A CA  1 
ATOM   2193 C  C   . GLU B 1 11  ? -46.907 -47.027 37.490  1.00 22.80 ? 11  GLU A C   1 
ATOM   2194 O  O   . GLU B 1 11  ? -46.272 -48.004 37.106  1.00 25.95 ? 11  GLU A O   1 
ATOM   2195 C  CB  . GLU B 1 11  ? -47.212 -46.527 39.944  1.00 27.87 ? 11  GLU A CB  1 
ATOM   2196 C  CG  . GLU B 1 11  ? -47.268 -48.003 40.245  1.00 34.86 ? 11  GLU A CG  1 
ATOM   2197 C  CD  . GLU B 1 11  ? -45.920 -48.697 40.205  1.00 48.59 ? 11  GLU A CD  1 
ATOM   2198 O  OE1 . GLU B 1 11  ? -45.902 -49.874 39.758  1.00 59.56 ? 11  GLU A OE1 1 
ATOM   2199 O  OE2 . GLU B 1 11  ? -44.887 -48.079 40.587  1.00 51.31 ? 11  GLU A OE2 1 
ATOM   2200 N  N   A HIS B 1 12  ? -48.055 -46.583 36.998  0.50 24.82 ? 12  HIS A N   1 
ATOM   2201 N  N   B HIS B 1 12  ? -48.064 -46.682 36.990  0.50 24.12 ? 12  HIS A N   1 
ATOM   2202 C  CA  A HIS B 1 12  ? -48.931 -47.302 36.045  0.50 26.33 ? 12  HIS A CA  1 
ATOM   2203 C  CA  B HIS B 1 12  ? -48.713 -47.570 36.020  0.50 24.53 ? 12  HIS A CA  1 
ATOM   2204 C  C   A HIS B 1 12  ? -48.663 -47.016 34.595  0.50 24.63 ? 12  HIS A C   1 
ATOM   2205 C  C   B HIS B 1 12  ? -48.287 -47.304 34.599  0.50 22.41 ? 12  HIS A C   1 
ATOM   2206 O  O   A HIS B 1 12  ? -49.265 -47.587 33.699  0.50 22.13 ? 12  HIS A O   1 
ATOM   2207 O  O   B HIS B 1 12  ? -48.413 -48.198 33.737  0.50 19.77 ? 12  HIS A O   1 
ATOM   2208 C  CB  A HIS B 1 12  ? -50.381 -46.903 36.341  0.50 26.30 ? 12  HIS A CB  1 
ATOM   2209 C  CB  B HIS B 1 12  ? -50.252 -47.539 36.211  0.50 26.58 ? 12  HIS A CB  1 
ATOM   2210 C  CG  A HIS B 1 12  ? -50.572 -45.404 36.535  0.50 33.02 ? 12  HIS A CG  1 
ATOM   2211 C  CG  B HIS B 1 12  ? -50.700 -48.009 37.586  0.50 32.18 ? 12  HIS A CG  1 
ATOM   2212 N  ND1 A HIS B 1 12  ? -50.704 -44.555 35.501  0.50 34.22 ? 12  HIS A ND1 1 
ATOM   2213 N  ND1 B HIS B 1 12  ? -50.550 -49.283 37.996  0.50 31.67 ? 12  HIS A ND1 1 
ATOM   2214 C  CD2 A HIS B 1 12  ? -50.627 -44.619 37.699  0.50 31.58 ? 12  HIS A CD2 1 
ATOM   2215 C  CD2 B HIS B 1 12  ? -51.229 -47.306 38.667  0.50 34.30 ? 12  HIS A CD2 1 
ATOM   2216 C  CE1 A HIS B 1 12  ? -50.862 -43.301 35.966  0.50 31.69 ? 12  HIS A CE1 1 
ATOM   2217 C  CE1 B HIS B 1 12  ? -50.990 -49.401 39.260  0.50 32.05 ? 12  HIS A CE1 1 
ATOM   2218 N  NE2 A HIS B 1 12  ? -50.834 -43.344 37.310  0.50 33.38 ? 12  HIS A NE2 1 
ATOM   2219 N  NE2 B HIS B 1 12  ? -51.406 -48.195 39.673  0.50 37.16 ? 12  HIS A NE2 1 
ATOM   2220 N  N   . ASN B 1 13  ? -47.764 -46.077 34.350  1.00 21.27 ? 13  ASN A N   1 
ATOM   2221 C  CA  . ASN B 1 13  ? -47.447 -45.645 32.915  1.00 19.01 ? 13  ASN A CA  1 
ATOM   2222 C  C   . ASN B 1 13  ? -45.910 -45.373 32.768  1.00 19.08 ? 13  ASN A C   1 
ATOM   2223 O  O   . ASN B 1 13  ? -45.532 -44.903 31.665  1.00 16.83 ? 13  ASN A O   1 
ATOM   2224 C  CB  . ASN B 1 13  ? -48.292 -44.493 32.419  1.00 19.37 ? 13  ASN A CB  1 
ATOM   2225 C  CG  . ASN B 1 13  ? -48.030 -43.197 33.117  1.00 19.30 ? 13  ASN A CG  1 
ATOM   2226 O  OD1 . ASN B 1 13  ? -47.181 -43.170 33.988  1.00 18.84 ? 13  ASN A OD1 1 
ATOM   2227 N  ND2 . ASN B 1 13  ? -48.747 -42.174 32.790  1.00 17.79 ? 13  ASN A ND2 1 
ATOM   2228 N  N   . GLY B 1 14  ? -45.114 -45.690 33.768  1.00 17.73 ? 14  GLY A N   1 
ATOM   2229 C  CA  . GLY B 1 14  ? -43.692 -45.253 33.766  1.00 17.70 ? 14  GLY A CA  1 
ATOM   2230 C  C   . GLY B 1 14  ? -42.790 -46.130 32.976  1.00 18.02 ? 14  GLY A C   1 
ATOM   2231 O  O   . GLY B 1 14  ? -43.258 -47.119 32.355  1.00 18.31 ? 14  GLY A O   1 
ATOM   2232 N  N   . PRO B 1 15  ? -41.470 -45.885 32.999  1.00 17.20 ? 15  PRO A N   1 
ATOM   2233 C  CA  . PRO B 1 15  ? -40.457 -46.607 32.242  1.00 16.61 ? 15  PRO A CA  1 
ATOM   2234 C  C   . PRO B 1 15  ? -40.546 -48.129 32.114  1.00 19.48 ? 15  PRO A C   1 
ATOM   2235 O  O   . PRO B 1 15  ? -40.400 -48.643 31.031  1.00 17.88 ? 15  PRO A O   1 
ATOM   2236 C  CB  . PRO B 1 15  ? -39.125 -46.104 32.821  1.00 16.69 ? 15  PRO A CB  1 
ATOM   2237 C  CG  . PRO B 1 15  ? -39.513 -44.681 33.176  1.00 17.11 ? 15  PRO A CG  1 
ATOM   2238 C  CD  . PRO B 1 15  ? -40.900 -44.703 33.718  1.00 15.73 ? 15  PRO A CD  1 
ATOM   2239 N  N   . ILE B 1 16  ? -40.810 -48.813 33.254  1.00 19.83 ? 16  ILE A N   1 
ATOM   2240 C  CA  . ILE B 1 16  ? -40.900 -50.286 33.233  1.00 20.73 ? 16  ILE A CA  1 
ATOM   2241 C  C   . ILE B 1 16  ? -42.097 -50.746 32.412  1.00 19.57 ? 16  ILE A C   1 
ATOM   2242 O  O   . ILE B 1 16  ? -42.004 -51.872 31.903  1.00 23.87 ? 16  ILE A O   1 
ATOM   2243 C  CB  . ILE B 1 16  ? -40.926 -50.859 34.678  1.00 25.23 ? 16  ILE A CB  1 
ATOM   2244 C  CG1 . ILE B 1 16  ? -40.576 -52.350 34.675  1.00 33.56 ? 16  ILE A CG1 1 
ATOM   2245 C  CG2 . ILE B 1 16  ? -42.280 -50.680 35.301  1.00 25.82 ? 16  ILE A CG2 1 
ATOM   2246 C  CD1 . ILE B 1 16  ? -39.085 -52.642 34.527  1.00 37.64 ? 16  ILE A CD1 1 
ATOM   2247 N  N   . HIS B 1 17  ? -43.082 -49.895 32.132  1.00 19.61 ? 17  HIS A N   1 
ATOM   2248 C  CA  . HIS B 1 17  ? -44.209 -50.236 31.289  1.00 20.12 ? 17  HIS A CA  1 
ATOM   2249 C  C   . HIS B 1 17  ? -44.072 -49.871 29.832  1.00 19.87 ? 17  HIS A C   1 
ATOM   2250 O  O   . HIS B 1 17  ? -44.930 -50.218 29.036  1.00 19.21 ? 17  HIS A O   1 
ATOM   2251 C  CB  . HIS B 1 17  ? -45.475 -49.651 31.842  1.00 22.86 ? 17  HIS A CB  1 
ATOM   2252 C  CG  . HIS B 1 17  ? -45.815 -50.203 33.203  1.00 30.85 ? 17  HIS A CG  1 
ATOM   2253 N  ND1 . HIS B 1 17  ? -46.083 -51.532 33.394  1.00 31.81 ? 17  HIS A ND1 1 
ATOM   2254 C  CD2 . HIS B 1 17  ? -45.903 -49.593 34.466  1.00 29.86 ? 17  HIS A CD2 1 
ATOM   2255 C  CE1 . HIS B 1 17  ? -46.272 -51.761 34.723  1.00 30.08 ? 17  HIS A CE1 1 
ATOM   2256 N  NE2 . HIS B 1 17  ? -46.203 -50.581 35.373  1.00 28.85 ? 17  HIS A NE2 1 
ATOM   2257 N  N   . TRP B 1 18  ? -43.041 -49.069 29.450  1.00 16.93 ? 18  TRP A N   1 
ATOM   2258 C  CA  . TRP B 1 18  ? -43.092 -48.515 28.113  1.00 17.02 ? 18  TRP A CA  1 
ATOM   2259 C  C   . TRP B 1 18  ? -43.003 -49.630 27.006  1.00 16.67 ? 18  TRP A C   1 
ATOM   2260 O  O   . TRP B 1 18  ? -43.547 -49.410 25.924  1.00 18.84 ? 18  TRP A O   1 
ATOM   2261 C  CB  . TRP B 1 18  ? -41.874 -47.547 28.003  1.00 14.23 ? 18  TRP A CB  1 
ATOM   2262 C  CG  . TRP B 1 18  ? -42.072 -46.287 28.763  1.00 13.56 ? 18  TRP A CG  1 
ATOM   2263 C  CD1 . TRP B 1 18  ? -43.179 -45.804 29.496  1.00 14.84 ? 18  TRP A CD1 1 
ATOM   2264 C  CD2 . TRP B 1 18  ? -41.022 -45.265 28.957  1.00 12.99 ? 18  TRP A CD2 1 
ATOM   2265 N  NE1 . TRP B 1 18  ? -42.896 -44.602 30.062  1.00 13.85 ? 18  TRP A NE1 1 
ATOM   2266 C  CE2 . TRP B 1 18  ? -41.642 -44.227 29.740  1.00 11.56 ? 18  TRP A CE2 1 
ATOM   2267 C  CE3 . TRP B 1 18  ? -39.702 -45.116 28.527  1.00 11.81 ? 18  TRP A CE3 1 
ATOM   2268 C  CZ2 . TRP B 1 18  ? -40.971 -43.089 30.106  1.00 11.93 ? 18  TRP A CZ2 1 
ATOM   2269 C  CZ3 . TRP B 1 18  ? -39.073 -43.937 28.886  1.00 10.01 ? 18  TRP A CZ3 1 
ATOM   2270 C  CH2 . TRP B 1 18  ? -39.694 -42.986 29.616  1.00 11.00 ? 18  TRP A CH2 1 
ATOM   2271 N  N   . LYS B 1 19  ? -42.310 -50.711 27.373  1.00 19.04 ? 19  LYS A N   1 
ATOM   2272 C  CA  . LYS B 1 19  ? -42.117 -51.914 26.437  1.00 20.92 ? 19  LYS A CA  1 
ATOM   2273 C  C   . LYS B 1 19  ? -43.508 -52.448 25.981  1.00 23.68 ? 19  LYS A C   1 
ATOM   2274 O  O   . LYS B 1 19  ? -43.644 -53.075 24.957  1.00 24.89 ? 19  LYS A O   1 
ATOM   2275 C  CB  . LYS B 1 19  ? -41.230 -52.983 27.042  1.00 22.14 ? 19  LYS A CB  1 
ATOM   2276 C  CG  . LYS B 1 19  ? -41.843 -53.637 28.302  1.00 22.62 ? 19  LYS A CG  1 
ATOM   2277 C  CD  . LYS B 1 19  ? -41.024 -54.768 28.964  1.00 29.17 ? 19  LYS A CD  1 
ATOM   2278 C  CE  . LYS B 1 19  ? -39.752 -54.209 29.578  1.00 29.69 ? 19  LYS A CE  1 
ATOM   2279 N  NZ  . LYS B 1 19  ? -40.038 -53.640 30.924  1.00 31.01 ? 19  LYS A NZ  1 
ATOM   2280 N  N   . GLU B 1 20  ? -44.541 -52.200 26.748  1.00 20.18 ? 20  GLU A N   1 
ATOM   2281 C  CA  . GLU B 1 20  ? -45.924 -52.638 26.387  1.00 20.44 ? 20  GLU A CA  1 
ATOM   2282 C  C   . GLU B 1 20  ? -46.507 -51.915 25.197  1.00 25.18 ? 20  GLU A C   1 
ATOM   2283 O  O   . GLU B 1 20  ? -47.425 -52.411 24.468  1.00 26.01 ? 20  GLU A O   1 
ATOM   2284 C  CB  . GLU B 1 20  ? -46.907 -52.379 27.555  1.00 21.46 ? 20  GLU A CB  1 
ATOM   2285 C  CG  . GLU B 1 20  ? -46.553 -53.199 28.752  1.00 23.01 ? 20  GLU A CG  1 
ATOM   2286 C  CD  . GLU B 1 20  ? -47.213 -52.768 30.110  1.00 23.87 ? 20  GLU A CD  1 
ATOM   2287 O  OE1 . GLU B 1 20  ? -48.321 -52.180 30.120  1.00 35.17 ? 20  GLU A OE1 1 
ATOM   2288 O  OE2 . GLU B 1 20  ? -46.564 -53.063 31.167  1.00 24.50 ? 20  GLU A OE2 1 
ATOM   2289 N  N   . PHE B 1 21  ? -46.104 -50.704 24.986  1.00 23.27 ? 21  PHE A N   1 
ATOM   2290 C  CA  . PHE B 1 21  ? -46.593 -50.033 23.798  1.00 22.71 ? 21  PHE A CA  1 
ATOM   2291 C  C   . PHE B 1 21  ? -45.454 -49.758 22.796  1.00 21.51 ? 21  PHE A C   1 
ATOM   2292 O  O   . PHE B 1 21  ? -45.732 -49.410 21.681  1.00 21.71 ? 21  PHE A O   1 
ATOM   2293 C  CB  . PHE B 1 21  ? -47.314 -48.743 24.168  1.00 34.75 ? 21  PHE A CB  1 
ATOM   2294 C  CG  . PHE B 1 21  ? -48.646 -48.956 24.890  1.00 44.32 ? 21  PHE A CG  1 
ATOM   2295 C  CD1 . PHE B 1 21  ? -48.861 -50.055 25.729  1.00 44.10 ? 21  PHE A CD1 1 
ATOM   2296 C  CD2 . PHE B 1 21  ? -49.672 -47.996 24.770  1.00 53.21 ? 21  PHE A CD2 1 
ATOM   2297 C  CE1 . PHE B 1 21  ? -50.067 -50.189 26.425  1.00 49.18 ? 21  PHE A CE1 1 
ATOM   2298 C  CE2 . PHE B 1 21  ? -50.878 -48.143 25.451  1.00 58.76 ? 21  PHE A CE2 1 
ATOM   2299 C  CZ  . PHE B 1 21  ? -51.069 -49.248 26.278  1.00 52.34 ? 21  PHE A CZ  1 
ATOM   2300 N  N   . PHE B 1 22  ? -44.215 -49.823 23.269  1.00 20.84 ? 22  PHE A N   1 
ATOM   2301 C  CA  . PHE B 1 22  ? -43.041 -49.375 22.461  1.00 23.29 ? 22  PHE A CA  1 
ATOM   2302 C  C   . PHE B 1 22  ? -42.032 -50.450 22.653  1.00 23.76 ? 22  PHE A C   1 
ATOM   2303 O  O   . PHE B 1 22  ? -41.081 -50.429 23.463  1.00 21.95 ? 22  PHE A O   1 
ATOM   2304 C  CB  . PHE B 1 22  ? -42.527 -48.003 22.899  1.00 21.95 ? 22  PHE A CB  1 
ATOM   2305 C  CG  . PHE B 1 22  ? -43.565 -46.988 22.867  1.00 17.69 ? 22  PHE A CG  1 
ATOM   2306 C  CD1 . PHE B 1 22  ? -43.825 -46.332 21.705  1.00 22.44 ? 22  PHE A CD1 1 
ATOM   2307 C  CD2 . PHE B 1 22  ? -44.302 -46.660 23.985  1.00 23.21 ? 22  PHE A CD2 1 
ATOM   2308 C  CE1 . PHE B 1 22  ? -44.822 -45.420 21.584  1.00 20.72 ? 22  PHE A CE1 1 
ATOM   2309 C  CE2 . PHE B 1 22  ? -45.315 -45.710 23.920  1.00 22.42 ? 22  PHE A CE2 1 
ATOM   2310 C  CZ  . PHE B 1 22  ? -45.620 -45.102 22.704  1.00 20.97 ? 22  PHE A CZ  1 
ATOM   2311 N  N   . PRO B 1 23  ? -42.229 -51.512 21.871  1.00 28.71 ? 23  PRO A N   1 
ATOM   2312 C  CA  . PRO B 1 23  ? -41.373 -52.634 21.952  1.00 26.51 ? 23  PRO A CA  1 
ATOM   2313 C  C   . PRO B 1 23  ? -39.865 -52.355 21.777  1.00 24.23 ? 23  PRO A C   1 
ATOM   2314 O  O   . PRO B 1 23  ? -39.059 -53.040 22.377  1.00 23.61 ? 23  PRO A O   1 
ATOM   2315 C  CB  . PRO B 1 23  ? -41.957 -53.606 20.832  1.00 25.41 ? 23  PRO A CB  1 
ATOM   2316 C  CG  . PRO B 1 23  ? -42.869 -52.798 20.003  1.00 30.66 ? 23  PRO A CG  1 
ATOM   2317 C  CD  . PRO B 1 23  ? -43.315 -51.650 20.872  1.00 32.05 ? 23  PRO A CD  1 
ATOM   2318 N  N   . ILE B 1 24  ? -39.557 -51.337 20.953  1.00 19.19 ? 24  ILE A N   1 
ATOM   2319 C  CA  . ILE B 1 24  ? -38.088 -50.961 20.862  1.00 18.51 ? 24  ILE A CA  1 
ATOM   2320 C  C   . ILE B 1 24  ? -37.395 -50.596 22.279  1.00 16.05 ? 24  ILE A C   1 
ATOM   2321 O  O   . ILE B 1 24  ? -36.178 -50.590 22.411  1.00 17.04 ? 24  ILE A O   1 
ATOM   2322 C  CB  . ILE B 1 24  ? -37.913 -49.909 19.819  1.00 16.98 ? 24  ILE A CB  1 
ATOM   2323 C  CG1 . ILE B 1 24  ? -36.473 -49.951 19.330  1.00 17.29 ? 24  ILE A CG1 1 
ATOM   2324 C  CG2 . ILE B 1 24  ? -38.198 -48.544 20.435  1.00 16.63 ? 24  ILE A CG2 1 
ATOM   2325 C  CD1 . ILE B 1 24  ? -36.050 -51.217 18.539  1.00 18.74 ? 24  ILE A CD1 1 
ATOM   2326 N  N   . ALA B 1 25  ? -38.273 -50.456 23.300  1.00 18.33 ? 25  ALA A N   1 
ATOM   2327 C  CA  . ALA B 1 25  ? -37.727 -50.255 24.638  1.00 17.39 ? 25  ALA A CA  1 
ATOM   2328 C  C   . ALA B 1 25  ? -36.635 -51.184 25.085  1.00 16.28 ? 25  ALA A C   1 
ATOM   2329 O  O   . ALA B 1 25  ? -35.751 -50.870 25.861  1.00 16.38 ? 25  ALA A O   1 
ATOM   2330 C  CB  . ALA B 1 25  ? -38.830 -50.250 25.748  1.00 17.33 ? 25  ALA A CB  1 
ATOM   2331 N  N   . ASP B 1 26  ? -36.710 -52.512 24.625  1.00 17.94 ? 26  ASP A N   1 
ATOM   2332 C  CA  . ASP B 1 26  ? -35.687 -53.498 24.993  1.00 20.44 ? 26  ASP A CA  1 
ATOM   2333 C  C   . ASP B 1 26  ? -34.731 -53.773 23.834  1.00 20.93 ? 26  ASP A C   1 
ATOM   2334 O  O   . ASP B 1 26  ? -34.081 -54.848 23.757  1.00 22.84 ? 26  ASP A O   1 
ATOM   2335 C  CB  . ASP B 1 26  ? -36.468 -54.792 25.396  1.00 22.74 ? 26  ASP A CB  1 
ATOM   2336 C  CG  . ASP B 1 26  ? -37.361 -54.586 26.597  1.00 25.66 ? 26  ASP A CG  1 
ATOM   2337 O  OD1 . ASP B 1 26  ? -36.828 -54.050 27.574  1.00 28.78 ? 26  ASP A OD1 1 
ATOM   2338 O  OD2 . ASP B 1 26  ? -38.567 -54.955 26.506  1.00 31.02 ? 26  ASP A OD2 1 
ATOM   2339 N  N   . GLY B 1 27  ? -34.570 -52.776 22.938  1.00 18.81 ? 27  GLY A N   1 
ATOM   2340 C  CA  . GLY B 1 27  ? -33.662 -52.850 21.821  1.00 17.11 ? 27  GLY A CA  1 
ATOM   2341 C  C   . GLY B 1 27  ? -32.182 -52.864 22.116  1.00 16.28 ? 27  GLY A C   1 
ATOM   2342 O  O   . GLY B 1 27  ? -31.692 -52.852 23.273  1.00 17.50 ? 27  GLY A O   1 
ATOM   2343 N  N   . ASP B 1 28  ? -31.420 -52.909 21.054  1.00 16.50 ? 28  ASP A N   1 
ATOM   2344 C  CA  . ASP B 1 28  ? -29.991 -52.981 21.172  1.00 17.68 ? 28  ASP A CA  1 
ATOM   2345 C  C   . ASP B 1 28  ? -29.264 -51.674 21.189  1.00 13.55 ? 28  ASP A C   1 
ATOM   2346 O  O   . ASP B 1 28  ? -28.120 -51.602 21.445  1.00 14.13 ? 28  ASP A O   1 
ATOM   2347 C  CB  . ASP B 1 28  ? -29.414 -53.822 19.991  1.00 17.55 ? 28  ASP A CB  1 
ATOM   2348 C  CG  . ASP B 1 28  ? -29.690 -55.308 20.137  1.00 21.32 ? 28  ASP A CG  1 
ATOM   2349 O  OD1 . ASP B 1 28  ? -29.883 -55.792 21.275  1.00 25.71 ? 28  ASP A OD1 1 
ATOM   2350 O  OD2 . ASP B 1 28  ? -29.708 -55.995 19.105  1.00 26.09 ? 28  ASP A OD2 1 
ATOM   2351 N  N   . GLN B 1 29  ? -30.006 -50.548 20.920  1.00 13.31 ? 29  GLN A N   1 
ATOM   2352 C  CA  . GLN B 1 29  ? -29.308 -49.226 20.878  1.00 12.75 ? 29  GLN A CA  1 
ATOM   2353 C  C   . GLN B 1 29  ? -30.127 -48.244 21.707  1.00 12.25 ? 29  GLN A C   1 
ATOM   2354 O  O   . GLN B 1 29  ? -30.418 -47.111 21.232  1.00 11.69 ? 29  GLN A O   1 
ATOM   2355 C  CB  . GLN B 1 29  ? -29.046 -48.736 19.459  1.00 12.49 ? 29  GLN A CB  1 
ATOM   2356 C  CG  . GLN B 1 29  ? -28.106 -49.710 18.688  1.00 16.89 ? 29  GLN A CG  1 
ATOM   2357 C  CD  . GLN B 1 29  ? -27.254 -49.036 17.646  1.00 20.08 ? 29  GLN A CD  1 
ATOM   2358 O  OE1 . GLN B 1 29  ? -27.587 -47.924 17.124  1.00 15.13 ? 29  GLN A OE1 1 
ATOM   2359 N  NE2 . GLN B 1 29  ? -26.086 -49.710 17.293  1.00 25.91 ? 29  GLN A NE2 1 
ATOM   2360 N  N   . GLN B 1 30  ? -30.495 -48.598 22.923  1.00 12.61 ? 30  GLN A N   1 
ATOM   2361 C  CA  . GLN B 1 30  ? -31.373 -47.746 23.787  1.00 10.62 ? 30  GLN A CA  1 
ATOM   2362 C  C   . GLN B 1 30  ? -30.554 -46.828 24.628  1.00 11.19 ? 30  GLN A C   1 
ATOM   2363 O  O   . GLN B 1 30  ? -29.374 -47.126 24.960  1.00 11.00 ? 30  GLN A O   1 
ATOM   2364 C  CB  . GLN B 1 30  ? -32.277 -48.650 24.631  1.00 10.84 ? 30  GLN A CB  1 
ATOM   2365 C  CG  . GLN B 1 30  ? -33.336 -49.343 23.790  1.00 12.53 ? 30  GLN A CG  1 
ATOM   2366 C  CD  . GLN B 1 30  ? -34.355 -48.279 23.311  1.00 11.30 ? 30  GLN A CD  1 
ATOM   2367 O  OE1 . GLN B 1 30  ? -35.143 -47.722 24.085  1.00 10.74 ? 30  GLN A OE1 1 
ATOM   2368 N  NE2 . GLN B 1 30  ? -34.403 -47.977 21.989  1.00 10.98 ? 30  GLN A NE2 1 
ATOM   2369 N  N   . SER B 1 31  ? -31.186 -45.697 24.993  1.00 10.28 ? 31  SER A N   1 
ATOM   2370 C  CA  . SER B 1 31  ? -30.521 -44.715 25.843  1.00 9.77  ? 31  SER A CA  1 
ATOM   2371 C  C   . SER B 1 31  ? -31.470 -44.408 26.985  1.00 8.94  ? 31  SER A C   1 
ATOM   2372 O  O   . SER B 1 31  ? -32.691 -44.670 26.927  1.00 9.94  ? 31  SER A O   1 
ATOM   2373 C  CB  . SER B 1 31  ? -30.325 -43.352 25.011  1.00 9.15  ? 31  SER A CB  1 
ATOM   2374 O  OG  . SER B 1 31  ? -29.384 -43.648 24.009  1.00 9.35  ? 31  SER A OG  1 
ATOM   2375 N  N   . PRO B 1 32  ? -30.948 -43.848 28.074  1.00 9.35  ? 32  PRO A N   1 
ATOM   2376 C  CA  . PRO B 1 32  ? -29.563 -43.498 28.333  1.00 9.52  ? 32  PRO A CA  1 
ATOM   2377 C  C   . PRO B 1 32  ? -28.730 -44.756 28.708  1.00 11.50 ? 32  PRO A C   1 
ATOM   2378 O  O   . PRO B 1 32  ? -29.320 -45.871 28.645  1.00 10.10 ? 32  PRO A O   1 
ATOM   2379 C  CB  . PRO B 1 32  ? -29.704 -42.532 29.530  1.00 10.06 ? 32  PRO A CB  1 
ATOM   2380 C  CG  . PRO B 1 32  ? -30.838 -43.112 30.329  1.00 10.13 ? 32  PRO A CG  1 
ATOM   2381 C  CD  . PRO B 1 32  ? -31.824 -43.605 29.254  1.00 9.47  ? 32  PRO A CD  1 
ATOM   2382 N  N   . ILE B 1 33  ? -27.459 -44.559 29.017  1.00 9.79  ? 33  ILE A N   1 
ATOM   2383 C  CA  . ILE B 1 33  ? -26.546 -45.702 29.360  1.00 10.50 ? 33  ILE A CA  1 
ATOM   2384 C  C   . ILE B 1 33  ? -25.756 -45.243 30.552  1.00 11.94 ? 33  ILE A C   1 
ATOM   2385 O  O   . ILE B 1 33  ? -25.718 -44.094 30.977  1.00 11.50 ? 33  ILE A O   1 
ATOM   2386 C  CB  . ILE B 1 33  ? -25.591 -46.031 28.168  1.00 11.81 ? 33  ILE A CB  1 
ATOM   2387 C  CG1 . ILE B 1 33  ? -24.758 -44.792 27.810  1.00 12.39 ? 33  ILE A CG1 1 
ATOM   2388 C  CG2 . ILE B 1 33  ? -26.385 -46.584 26.973  1.00 13.54 ? 33  ILE A CG2 1 
ATOM   2389 C  CD1 . ILE B 1 33  ? -23.497 -45.178 27.028  1.00 13.40 ? 33  ILE A CD1 1 
ATOM   2390 N  N   . GLU B 1 34  ? -25.069 -46.287 31.105  1.00 12.67 ? 34  GLU A N   1 
ATOM   2391 C  CA  . GLU B 1 34  ? -23.946 -46.036 32.015  1.00 11.31 ? 34  GLU A CA  1 
ATOM   2392 C  C   . GLU B 1 34  ? -22.655 -45.953 31.227  1.00 10.31 ? 34  GLU A C   1 
ATOM   2393 O  O   . GLU B 1 34  ? -22.424 -46.779 30.328  1.00 12.78 ? 34  GLU A O   1 
ATOM   2394 C  CB  . GLU B 1 34  ? -23.869 -47.291 32.960  1.00 12.33 ? 34  GLU A CB  1 
ATOM   2395 C  CG  . GLU B 1 34  ? -25.012 -47.376 33.935  1.00 13.27 ? 34  GLU A CG  1 
ATOM   2396 C  CD  . GLU B 1 34  ? -24.691 -48.398 35.084  1.00 15.48 ? 34  GLU A CD  1 
ATOM   2397 O  OE1 . GLU B 1 34  ? -24.007 -48.002 36.062  1.00 18.29 ? 34  GLU A OE1 1 
ATOM   2398 O  OE2 . GLU B 1 34  ? -25.032 -49.551 34.866  1.00 14.91 ? 34  GLU A OE2 1 
ATOM   2399 N  N   . ILE B 1 35  ? -21.800 -44.987 31.558  1.00 11.56 ? 35  ILE A N   1 
ATOM   2400 C  CA  . ILE B 1 35  ? -20.484 -44.775 30.932  1.00 13.99 ? 35  ILE A CA  1 
ATOM   2401 C  C   . ILE B 1 35  ? -19.432 -45.267 31.967  1.00 13.96 ? 35  ILE A C   1 
ATOM   2402 O  O   . ILE B 1 35  ? -19.332 -44.656 32.981  1.00 14.94 ? 35  ILE A O   1 
ATOM   2403 C  CB  . ILE B 1 35  ? -20.294 -43.303 30.497  1.00 14.03 ? 35  ILE A CB  1 
ATOM   2404 C  CG1 . ILE B 1 35  ? -21.459 -42.893 29.532  1.00 16.16 ? 35  ILE A CG1 1 
ATOM   2405 C  CG2 . ILE B 1 35  ? -18.887 -43.085 29.933  1.00 16.73 ? 35  ILE A CG2 1 
ATOM   2406 C  CD1 . ILE B 1 35  ? -21.471 -41.447 29.116  1.00 16.52 ? 35  ILE A CD1 1 
ATOM   2407 N  N   . LYS B 1 36  ? -18.704 -46.316 31.569  1.00 16.00 ? 36  LYS A N   1 
ATOM   2408 C  CA  . LYS B 1 36  ? -17.570 -46.878 32.343  1.00 16.10 ? 36  LYS A CA  1 
ATOM   2409 C  C   . LYS B 1 36  ? -16.294 -46.267 31.726  1.00 14.01 ? 36  LYS A C   1 
ATOM   2410 O  O   . LYS B 1 36  ? -15.843 -46.723 30.695  1.00 18.56 ? 36  LYS A O   1 
ATOM   2411 C  CB  . LYS B 1 36  ? -17.665 -48.427 32.282  1.00 16.11 ? 36  LYS A CB  1 
ATOM   2412 C  CG  . LYS B 1 36  ? -16.507 -49.120 33.074  1.00 19.94 ? 36  LYS A CG  1 
ATOM   2413 C  CD  . LYS B 1 36  ? -16.789 -50.626 33.317  1.00 21.30 ? 36  LYS A CD  1 
ATOM   2414 C  CE  . LYS B 1 36  ? -17.906 -50.917 34.369  1.00 23.06 ? 36  LYS A CE  1 
ATOM   2415 N  NZ  . LYS B 1 36  ? -17.955 -52.439 34.657  1.00 19.57 ? 36  LYS A NZ  1 
ATOM   2416 N  N   . THR B 1 37  ? -15.742 -45.232 32.323  1.00 15.23 ? 37  THR A N   1 
ATOM   2417 C  CA  . THR B 1 37  ? -14.672 -44.466 31.696  1.00 18.45 ? 37  THR A CA  1 
ATOM   2418 C  C   . THR B 1 37  ? -13.444 -45.351 31.483  1.00 18.92 ? 37  THR A C   1 
ATOM   2419 O  O   . THR B 1 37  ? -12.733 -45.175 30.445  1.00 19.09 ? 37  THR A O   1 
ATOM   2420 C  CB  . THR B 1 37  ? -14.382 -43.148 32.403  1.00 17.79 ? 37  THR A CB  1 
ATOM   2421 O  OG1 . THR B 1 37  ? -13.868 -43.438 33.741  1.00 20.53 ? 37  THR A OG1 1 
ATOM   2422 C  CG2 . THR B 1 37  ? -15.728 -42.383 32.552  1.00 20.08 ? 37  THR A CG2 1 
ATOM   2423 N  N   . LYS B 1 38  ? -13.192 -46.354 32.342  1.00 21.17 ? 38  LYS A N   1 
ATOM   2424 C  CA  . LYS B 1 38  ? -11.966 -47.145 32.172  1.00 26.57 ? 38  LYS A CA  1 
ATOM   2425 C  C   . LYS B 1 38  ? -12.023 -47.870 30.838  1.00 25.20 ? 38  LYS A C   1 
ATOM   2426 O  O   . LYS B 1 38  ? -10.981 -48.172 30.262  1.00 30.40 ? 38  LYS A O   1 
ATOM   2427 C  CB  . LYS B 1 38  ? -11.738 -48.098 33.359  1.00 30.34 ? 38  LYS A CB  1 
ATOM   2428 C  CG  . LYS B 1 38  ? -12.664 -49.298 33.419  1.00 36.31 ? 38  LYS A CG  1 
ATOM   2429 C  CD  . LYS B 1 38  ? -11.899 -50.538 33.892  1.00 44.21 ? 38  LYS A CD  1 
ATOM   2430 C  CE  . LYS B 1 38  ? -12.846 -51.711 34.161  1.00 48.98 ? 38  LYS A CE  1 
ATOM   2431 N  NZ  . LYS B 1 38  ? -13.303 -52.398 32.911  1.00 52.07 ? 38  LYS A NZ  1 
ATOM   2432 N  N   . GLU B 1 39  ? -13.234 -48.082 30.336  1.00 23.09 ? 39  GLU A N   1 
ATOM   2433 C  CA  . GLU B 1 39  ? -13.445 -48.725 29.068  1.00 25.79 ? 39  GLU A CA  1 
ATOM   2434 C  C   . GLU B 1 39  ? -13.597 -47.887 27.818  1.00 26.27 ? 39  GLU A C   1 
ATOM   2435 O  O   . GLU B 1 39  ? -13.742 -48.425 26.720  1.00 33.85 ? 39  GLU A O   1 
ATOM   2436 C  CB  . GLU B 1 39  ? -14.640 -49.667 29.226  1.00 29.86 ? 39  GLU A CB  1 
ATOM   2437 C  CG  . GLU B 1 39  ? -14.233 -50.854 30.072  1.00 38.05 ? 39  GLU A CG  1 
ATOM   2438 C  CD  . GLU B 1 39  ? -15.259 -51.947 30.005  1.00 42.69 ? 39  GLU A CD  1 
ATOM   2439 O  OE1 . GLU B 1 39  ? -14.951 -53.072 30.443  1.00 47.99 ? 39  GLU A OE1 1 
ATOM   2440 O  OE2 . GLU B 1 39  ? -16.344 -51.663 29.476  1.00 44.36 ? 39  GLU A OE2 1 
ATOM   2441 N  N   . VAL B 1 40  ? -13.522 -46.570 27.963  1.00 22.53 ? 40  VAL A N   1 
ATOM   2442 C  CA  . VAL B 1 40  ? -13.800 -45.672 26.833  1.00 23.12 ? 40  VAL A CA  1 
ATOM   2443 C  C   . VAL B 1 40  ? -12.473 -45.359 26.150  1.00 23.62 ? 40  VAL A C   1 
ATOM   2444 O  O   . VAL B 1 40  ? -11.473 -45.061 26.846  1.00 26.96 ? 40  VAL A O   1 
ATOM   2445 C  CB  . VAL B 1 40  ? -14.406 -44.372 27.419  1.00 19.99 ? 40  VAL A CB  1 
ATOM   2446 C  CG1 . VAL B 1 40  ? -14.435 -43.203 26.428  1.00 21.27 ? 40  VAL A CG1 1 
ATOM   2447 C  CG2 . VAL B 1 40  ? -15.817 -44.580 27.922  1.00 19.48 ? 40  VAL A CG2 1 
ATOM   2448 N  N   . LYS B 1 41  ? -12.446 -45.331 24.820  1.00 22.84 ? 41  LYS A N   1 
ATOM   2449 C  CA  . LYS B 1 41  ? -11.224 -44.945 24.126  1.00 25.01 ? 41  LYS A CA  1 
ATOM   2450 C  C   . LYS B 1 41  ? -11.317 -43.556 23.572  1.00 20.89 ? 41  LYS A C   1 
ATOM   2451 O  O   . LYS B 1 41  ? -12.387 -43.233 22.958  1.00 19.21 ? 41  LYS A O   1 
ATOM   2452 C  CB  . LYS B 1 41  ? -11.065 -45.877 22.927  1.00 30.79 ? 41  LYS A CB  1 
ATOM   2453 C  CG  . LYS B 1 41  ? -10.557 -47.260 23.310  1.00 33.99 ? 41  LYS A CG  1 
ATOM   2454 C  CD  . LYS B 1 41  ? -9.784  -47.867 22.148  1.00 42.40 ? 41  LYS A CD  1 
ATOM   2455 C  CE  . LYS B 1 41  ? -8.451  -47.155 21.933  1.00 51.01 ? 41  LYS A CE  1 
ATOM   2456 N  NZ  . LYS B 1 41  ? -8.123  -47.022 20.474  1.00 50.51 ? 41  LYS A NZ  1 
ATOM   2457 N  N   . TYR B 1 42  ? -10.303 -42.728 23.825  1.00 19.41 ? 42  TYR A N   1 
ATOM   2458 C  CA  . TYR B 1 42  ? -10.141 -41.451 23.109  1.00 21.71 ? 42  TYR A CA  1 
ATOM   2459 C  C   . TYR B 1 42  ? -10.069 -41.802 21.609  1.00 21.59 ? 42  TYR A C   1 
ATOM   2460 O  O   . TYR B 1 42  ? -9.376  -42.699 21.157  1.00 20.98 ? 42  TYR A O   1 
ATOM   2461 C  CB  . TYR B 1 42  ? -8.840  -40.748 23.570  1.00 20.20 ? 42  TYR A CB  1 
ATOM   2462 C  CG  . TYR B 1 42  ? -8.372  -39.624 22.636  1.00 23.43 ? 42  TYR A CG  1 
ATOM   2463 C  CD1 . TYR B 1 42  ? -9.056  -38.431 22.577  1.00 21.08 ? 42  TYR A CD1 1 
ATOM   2464 C  CD2 . TYR B 1 42  ? -7.198  -39.759 21.794  1.00 23.83 ? 42  TYR A CD2 1 
ATOM   2465 C  CE1 . TYR B 1 42  ? -8.683  -37.399 21.710  1.00 23.08 ? 42  TYR A CE1 1 
ATOM   2466 C  CE2 . TYR B 1 42  ? -6.801  -38.742 20.933  1.00 27.85 ? 42  TYR A CE2 1 
ATOM   2467 C  CZ  . TYR B 1 42  ? -7.536  -37.544 20.905  1.00 23.87 ? 42  TYR A CZ  1 
ATOM   2468 O  OH  . TYR B 1 42  ? -7.179  -36.484 20.063  1.00 30.04 ? 42  TYR A OH  1 
ATOM   2469 N  N   . ASP B 1 43  ? -10.806 -41.053 20.812  1.00 18.63 ? 43  ASP A N   1 
ATOM   2470 C  CA  . ASP B 1 43  ? -10.797 -41.096 19.364  1.00 18.07 ? 43  ASP A CA  1 
ATOM   2471 C  C   . ASP B 1 43  ? -10.273 -39.809 18.737  1.00 20.94 ? 43  ASP A C   1 
ATOM   2472 O  O   . ASP B 1 43  ? -10.956 -38.749 18.706  1.00 18.19 ? 43  ASP A O   1 
ATOM   2473 C  CB  . ASP B 1 43  ? -12.234 -41.340 18.882  1.00 18.55 ? 43  ASP A CB  1 
ATOM   2474 C  CG  . ASP B 1 43  ? -12.281 -41.657 17.366  1.00 22.78 ? 43  ASP A CG  1 
ATOM   2475 O  OD1 . ASP B 1 43  ? -11.246 -41.398 16.658  1.00 23.09 ? 43  ASP A OD1 1 
ATOM   2476 O  OD2 . ASP B 1 43  ? -13.334 -42.093 16.885  1.00 25.75 ? 43  ASP A OD2 1 
ATOM   2477 N  N   . SER B 1 44  ? -9.028  -39.845 18.233  1.00 20.86 ? 44  SER A N   1 
ATOM   2478 C  CA  . SER B 1 44  ? -8.440  -38.660 17.596  1.00 22.72 ? 44  SER A CA  1 
ATOM   2479 C  C   . SER B 1 44  ? -9.059  -38.250 16.285  1.00 24.40 ? 44  SER A C   1 
ATOM   2480 O  O   . SER B 1 44  ? -8.846  -37.097 15.824  1.00 23.51 ? 44  SER A O   1 
ATOM   2481 C  CB  . SER B 1 44  ? -6.888  -38.879 17.464  1.00 26.09 ? 44  SER A CB  1 
ATOM   2482 O  OG  . SER B 1 44  ? -6.743  -40.018 16.666  1.00 27.81 ? 44  SER A OG  1 
ATOM   2483 N  N   . SER B 1 45  ? -9.901  -39.111 15.685  1.00 20.94 ? 45  SER A N   1 
ATOM   2484 C  CA  . SER B 1 45  ? -10.578 -38.760 14.455  1.00 22.84 ? 45  SER A CA  1 
ATOM   2485 C  C   . SER B 1 45  ? -11.771 -37.808 14.675  1.00 20.57 ? 45  SER A C   1 
ATOM   2486 O  O   . SER B 1 45  ? -12.315 -37.221 13.704  1.00 22.11 ? 45  SER A O   1 
ATOM   2487 C  CB  . SER B 1 45  ? -11.032 -40.015 13.638  1.00 24.19 ? 45  SER A CB  1 
ATOM   2488 O  OG  . SER B 1 45  ? -12.143 -40.589 14.203  1.00 25.99 ? 45  SER A OG  1 
ATOM   2489 N  N   . LEU B 1 46  ? -12.216 -37.656 15.905  1.00 19.63 ? 46  LEU A N   1 
ATOM   2490 C  CA  . LEU B 1 46  ? -13.351 -36.770 16.149  1.00 18.15 ? 46  LEU A CA  1 
ATOM   2491 C  C   . LEU B 1 46  ? -12.955 -35.323 15.825  1.00 17.95 ? 46  LEU A C   1 
ATOM   2492 O  O   . LEU B 1 46  ? -11.862 -34.909 16.266  1.00 18.92 ? 46  LEU A O   1 
ATOM   2493 C  CB  . LEU B 1 46  ? -13.779 -36.872 17.642  1.00 16.64 ? 46  LEU A CB  1 
ATOM   2494 C  CG  . LEU B 1 46  ? -14.484 -38.180 17.997  1.00 15.30 ? 46  LEU A CG  1 
ATOM   2495 C  CD1 . LEU B 1 46  ? -14.584 -38.236 19.496  1.00 15.96 ? 46  LEU A CD1 1 
ATOM   2496 C  CD2 . LEU B 1 46  ? -15.915 -38.212 17.420  1.00 14.87 ? 46  LEU A CD2 1 
ATOM   2497 N  N   . ARG B 1 47  ? -13.761 -34.560 15.093  1.00 18.07 ? 47  ARG A N   1 
ATOM   2498 C  CA  . ARG B 1 47  ? -13.366 -33.194 14.768  1.00 17.92 ? 47  ARG A CA  1 
ATOM   2499 C  C   . ARG B 1 47  ? -13.763 -32.214 15.842  1.00 15.92 ? 47  ARG A C   1 
ATOM   2500 O  O   . ARG B 1 47  ? -14.629 -32.517 16.698  1.00 16.42 ? 47  ARG A O   1 
ATOM   2501 C  CB  . ARG B 1 47  ? -14.116 -32.755 13.472  1.00 23.90 ? 47  ARG A CB  1 
ATOM   2502 C  CG  . ARG B 1 47  ? -13.885 -33.610 12.179  1.00 29.03 ? 47  ARG A CG  1 
ATOM   2503 C  CD  . ARG B 1 47  ? -12.431 -33.748 11.695  1.00 41.84 ? 47  ARG A CD  1 
ATOM   2504 N  NE  . ARG B 1 47  ? -11.555 -33.969 12.852  1.00 51.89 ? 47  ARG A NE  1 
ATOM   2505 C  CZ  . ARG B 1 47  ? -10.273 -34.319 12.786  1.00 48.79 ? 47  ARG A CZ  1 
ATOM   2506 N  NH1 . ARG B 1 47  ? -9.694  -34.490 11.607  1.00 54.97 ? 47  ARG A NH1 1 
ATOM   2507 N  NH2 . ARG B 1 47  ? -9.568  -34.495 13.899  1.00 40.56 ? 47  ARG A NH2 1 
ATOM   2508 N  N   . PRO B 1 48  ? -13.200 -31.014 15.882  1.00 15.99 ? 48  PRO A N   1 
ATOM   2509 C  CA  . PRO B 1 48  ? -13.678 -30.115 16.893  1.00 15.03 ? 48  PRO A CA  1 
ATOM   2510 C  C   . PRO B 1 48  ? -15.200 -29.981 16.824  1.00 15.64 ? 48  PRO A C   1 
ATOM   2511 O  O   . PRO B 1 48  ? -15.795 -29.904 15.700  1.00 16.01 ? 48  PRO A O   1 
ATOM   2512 C  CB  . PRO B 1 48  ? -12.976 -28.763 16.500  1.00 18.50 ? 48  PRO A CB  1 
ATOM   2513 C  CG  . PRO B 1 48  ? -11.678 -29.239 15.935  1.00 18.87 ? 48  PRO A CG  1 
ATOM   2514 C  CD  . PRO B 1 48  ? -12.077 -30.410 15.086  1.00 17.40 ? 48  PRO A CD  1 
ATOM   2515 N  N   . LEU B 1 49  ? -15.825 -29.820 17.999  1.00 16.23 ? 49  LEU A N   1 
ATOM   2516 C  CA  . LEU B 1 49  ? -17.279 -29.445 17.990  1.00 15.34 ? 49  LEU A CA  1 
ATOM   2517 C  C   . LEU B 1 49  ? -17.503 -28.026 17.653  1.00 15.77 ? 49  LEU A C   1 
ATOM   2518 O  O   . LEU B 1 49  ? -16.644 -27.182 17.920  1.00 18.18 ? 49  LEU A O   1 
ATOM   2519 C  CB  . LEU B 1 49  ? -17.805 -29.683 19.363  1.00 18.31 ? 49  LEU A CB  1 
ATOM   2520 C  CG  . LEU B 1 49  ? -19.136 -30.122 19.741  1.00 21.86 ? 49  LEU A CG  1 
ATOM   2521 C  CD1 . LEU B 1 49  ? -19.521 -31.333 18.949  1.00 19.43 ? 49  LEU A CD1 1 
ATOM   2522 C  CD2 . LEU B 1 49  ? -19.171 -30.434 21.235  1.00 24.65 ? 49  LEU A CD2 1 
ATOM   2523 N  N   . SER B 1 50  ? -18.552 -27.741 16.918  1.00 13.23 ? 50  SER A N   1 
ATOM   2524 C  CA  . SER B 1 50  ? -18.843 -26.423 16.458  1.00 13.51 ? 50  SER A CA  1 
ATOM   2525 C  C   . SER B 1 50  ? -20.275 -26.151 16.884  1.00 11.92 ? 50  SER A C   1 
ATOM   2526 O  O   . SER B 1 50  ? -21.186 -26.812 16.454  1.00 13.32 ? 50  SER A O   1 
ATOM   2527 C  CB  . SER B 1 50  ? -18.749 -26.265 14.869  1.00 14.44 ? 50  SER A CB  1 
ATOM   2528 O  OG  . SER B 1 50  ? -19.513 -25.152 14.412  1.00 16.34 ? 50  SER A OG  1 
ATOM   2529 N  N   . ILE B 1 51  ? -20.450 -25.125 17.724  1.00 10.02 ? 51  ILE A N   1 
ATOM   2530 C  CA  . ILE B 1 51  ? -21.802 -24.806 18.134  1.00 10.50 ? 51  ILE A CA  1 
ATOM   2531 C  C   . ILE B 1 51  ? -22.120 -23.332 17.791  1.00 12.31 ? 51  ILE A C   1 
ATOM   2532 O  O   . ILE B 1 51  ? -21.503 -22.348 18.335  1.00 12.45 ? 51  ILE A O   1 
ATOM   2533 C  CB  . ILE B 1 51  ? -21.941 -24.979 19.635  1.00 10.45 ? 51  ILE A CB  1 
ATOM   2534 C  CG1 . ILE B 1 51  ? -21.552 -26.401 20.076  1.00 12.51 ? 51  ILE A CG1 1 
ATOM   2535 C  CG2 . ILE B 1 51  ? -23.355 -24.573 20.059  1.00 13.84 ? 51  ILE A CG2 1 
ATOM   2536 C  CD1 . ILE B 1 51  ? -21.654 -26.810 21.574  1.00 13.10 ? 51  ILE A CD1 1 
ATOM   2537 N  N   . LYS B 1 52  ? -22.988 -23.130 16.804  1.00 10.04 ? 52  LYS A N   1 
ATOM   2538 C  CA  . LYS B 1 52  ? -23.401 -21.805 16.402  1.00 10.44 ? 52  LYS A CA  1 
ATOM   2539 C  C   . LYS B 1 52  ? -24.816 -21.677 16.789  1.00 10.40 ? 52  LYS A C   1 
ATOM   2540 O  O   . LYS B 1 52  ? -25.682 -22.259 16.191  1.00 11.37 ? 52  LYS A O   1 
ATOM   2541 C  CB  . LYS B 1 52  ? -23.249 -21.597 14.871  1.00 10.54 ? 52  LYS A CB  1 
ATOM   2542 C  CG  . LYS B 1 52  ? -23.693 -20.224 14.422  1.00 11.56 ? 52  LYS A CG  1 
ATOM   2543 C  CD  . LYS B 1 52  ? -23.356 -19.890 12.966  1.00 12.94 ? 52  LYS A CD  1 
ATOM   2544 C  CE  . LYS B 1 52  ? -23.983 -20.756 11.975  1.00 13.05 ? 52  LYS A CE  1 
ATOM   2545 N  NZ  . LYS B 1 52  ? -23.685 -20.289 10.533  1.00 18.34 ? 52  LYS A NZ  1 
ATOM   2546 N  N   A TYR B 1 53  ? -25.105 -20.840 17.785  0.50 9.81  ? 53  TYR A N   1 
ATOM   2547 N  N   B TYR B 1 53  ? -25.044 -20.701 17.660  0.50 10.86 ? 53  TYR A N   1 
ATOM   2548 C  CA  A TYR B 1 53  ? -26.495 -20.633 18.257  0.50 9.40  ? 53  TYR A CA  1 
ATOM   2549 C  CA  B TYR B 1 53  ? -26.326 -20.546 18.299  0.50 11.26 ? 53  TYR A CA  1 
ATOM   2550 C  C   A TYR B 1 53  ? -26.861 -19.172 18.334  0.50 9.66  ? 53  TYR A C   1 
ATOM   2551 C  C   B TYR B 1 53  ? -26.786 -19.102 18.221  0.50 11.11 ? 53  TYR A C   1 
ATOM   2552 O  O   A TYR B 1 53  ? -26.122 -18.320 18.854  0.50 9.57  ? 53  TYR A O   1 
ATOM   2553 O  O   B TYR B 1 53  ? -26.035 -18.187 18.484  0.50 11.74 ? 53  TYR A O   1 
ATOM   2554 C  CB  A TYR B 1 53  ? -26.720 -21.231 19.676  0.50 8.35  ? 53  TYR A CB  1 
ATOM   2555 C  CB  B TYR B 1 53  ? -26.237 -21.036 19.775  0.50 10.90 ? 53  TYR A CB  1 
ATOM   2556 C  CG  A TYR B 1 53  ? -26.642 -22.715 19.872  0.50 7.19  ? 53  TYR A CG  1 
ATOM   2557 C  CG  B TYR B 1 53  ? -27.573 -20.724 20.394  0.50 10.97 ? 53  TYR A CG  1 
ATOM   2558 C  CD1 A TYR B 1 53  ? -26.873 -23.624 18.816  0.50 7.38  ? 53  TYR A CD1 1 
ATOM   2559 C  CD1 B TYR B 1 53  ? -28.701 -21.476 20.061  0.50 12.19 ? 53  TYR A CD1 1 
ATOM   2560 C  CD2 A TYR B 1 53  ? -26.455 -23.234 21.142  0.50 7.08  ? 53  TYR A CD2 1 
ATOM   2561 C  CD2 B TYR B 1 53  ? -27.724 -19.610 21.225  0.50 13.17 ? 53  TYR A CD2 1 
ATOM   2562 C  CE1 A TYR B 1 53  ? -26.825 -24.990 19.026  0.50 7.21  ? 53  TYR A CE1 1 
ATOM   2563 C  CE1 B TYR B 1 53  ? -29.933 -21.164 20.572  0.50 14.01 ? 53  TYR A CE1 1 
ATOM   2564 C  CE2 A TYR B 1 53  ? -26.469 -24.600 21.349  0.50 6.55  ? 53  TYR A CE2 1 
ATOM   2565 C  CE2 B TYR B 1 53  ? -28.944 -19.293 21.752  0.50 9.80  ? 53  TYR A CE2 1 
ATOM   2566 C  CZ  A TYR B 1 53  ? -26.618 -25.470 20.305  0.50 7.11  ? 53  TYR A CZ  1 
ATOM   2567 C  CZ  B TYR B 1 53  ? -30.077 -20.028 21.328  0.50 9.95  ? 53  TYR A CZ  1 
ATOM   2568 O  OH  A TYR B 1 53  ? -26.582 -26.800 20.574  0.50 7.23  ? 53  TYR A OH  1 
ATOM   2569 O  OH  B TYR B 1 53  ? -31.261 -19.741 21.899  0.50 15.95 ? 53  TYR A OH  1 
ATOM   2570 N  N   . ASP B 1 54  ? -28.014 -18.911 17.758  1.00 11.01 ? 54  ASP A N   1 
ATOM   2571 C  CA  . ASP B 1 54  ? -28.618 -17.570 17.668  1.00 10.03 ? 54  ASP A CA  1 
ATOM   2572 C  C   . ASP B 1 54  ? -29.787 -17.461 18.628  1.00 10.45 ? 54  ASP A C   1 
ATOM   2573 O  O   . ASP B 1 54  ? -30.751 -18.200 18.494  1.00 10.87 ? 54  ASP A O   1 
ATOM   2574 C  CB  . ASP B 1 54  ? -29.146 -17.416 16.217  1.00 11.70 ? 54  ASP A CB  1 
ATOM   2575 C  CG  . ASP B 1 54  ? -29.594 -16.023 15.911  1.00 12.39 ? 54  ASP A CG  1 
ATOM   2576 O  OD1 . ASP B 1 54  ? -30.194 -15.352 16.779  1.00 13.04 ? 54  ASP A OD1 1 
ATOM   2577 O  OD2 . ASP B 1 54  ? -29.447 -15.626 14.719  1.00 16.76 ? 54  ASP A OD2 1 
ATOM   2578 N  N   . PRO B 1 55  ? -29.701 -16.617 19.618  1.00 9.54  ? 55  PRO A N   1 
ATOM   2579 C  CA  . PRO B 1 55  ? -30.803 -16.494 20.576  1.00 10.72 ? 55  PRO A CA  1 
ATOM   2580 C  C   . PRO B 1 55  ? -32.182 -16.198 19.992  1.00 11.26 ? 55  PRO A C   1 
ATOM   2581 O  O   . PRO B 1 55  ? -33.197 -16.521 20.619  1.00 13.19 ? 55  PRO A O   1 
ATOM   2582 C  CB  . PRO B 1 55  ? -30.341 -15.307 21.492  1.00 12.06 ? 55  PRO A CB  1 
ATOM   2583 C  CG  . PRO B 1 55  ? -28.816 -15.367 21.415  1.00 12.31 ? 55  PRO A CG  1 
ATOM   2584 C  CD  . PRO B 1 55  ? -28.501 -15.773 20.007  1.00 10.64 ? 55  PRO A CD  1 
ATOM   2585 N  N   A SER B 1 56  ? -32.280 -15.537 18.839  0.50 10.63 ? 56  SER A N   1 
ATOM   2586 N  N   B SER B 1 56  ? -32.189 -15.568 18.833  0.50 12.20 ? 56  SER A N   1 
ATOM   2587 C  CA  A SER B 1 56  ? -33.574 -15.344 18.174  0.50 11.05 ? 56  SER A CA  1 
ATOM   2588 C  CA  B SER B 1 56  ? -33.418 -15.270 18.193  0.50 13.55 ? 56  SER A CA  1 
ATOM   2589 C  C   A SER B 1 56  ? -34.123 -16.600 17.516  0.50 11.53 ? 56  SER A C   1 
ATOM   2590 C  C   B SER B 1 56  ? -34.204 -16.452 17.734  0.50 12.52 ? 56  SER A C   1 
ATOM   2591 O  O   A SER B 1 56  ? -35.284 -16.619 16.985  0.50 12.03 ? 56  SER A O   1 
ATOM   2592 O  O   B SER B 1 56  ? -35.417 -16.324 17.533  0.50 12.43 ? 56  SER A O   1 
ATOM   2593 C  CB  A SER B 1 56  ? -33.419 -14.214 17.102  0.50 10.69 ? 56  SER A CB  1 
ATOM   2594 C  CB  B SER B 1 56  ? -33.139 -14.286 17.028  0.50 13.28 ? 56  SER A CB  1 
ATOM   2595 O  OG  A SER B 1 56  ? -32.728 -14.673 15.962  0.50 9.44  ? 56  SER A OG  1 
ATOM   2596 O  OG  B SER B 1 56  ? -32.868 -13.104 17.700  0.50 19.37 ? 56  SER A OG  1 
ATOM   2597 N  N   A SER B 1 57  ? -33.336 -17.679 17.542  0.50 9.36  ? 57  SER A N   1 
ATOM   2598 N  N   B SER B 1 57  ? -33.552 -17.611 17.544  0.50 10.87 ? 57  SER A N   1 
ATOM   2599 C  CA  A SER B 1 57  ? -33.844 -18.940 17.007  0.50 9.76  ? 57  SER A CA  1 
ATOM   2600 C  CA  B SER B 1 57  ? -34.219 -18.792 17.010  0.50 11.85 ? 57  SER A CA  1 
ATOM   2601 C  C   A SER B 1 57  ? -34.943 -19.546 17.918  0.50 9.68  ? 57  SER A C   1 
ATOM   2602 C  C   B SER B 1 57  ? -35.180 -19.452 17.973  0.50 10.89 ? 57  SER A C   1 
ATOM   2603 O  O   A SER B 1 57  ? -35.747 -20.329 17.381  0.50 9.40  ? 57  SER A O   1 
ATOM   2604 O  O   B SER B 1 57  ? -36.114 -20.161 17.614  0.50 11.18 ? 57  SER A O   1 
ATOM   2605 C  CB  A SER B 1 57  ? -32.776 -19.984 16.761  0.50 9.79  ? 57  SER A CB  1 
ATOM   2606 C  CB  B SER B 1 57  ? -33.228 -19.879 16.657  0.50 11.81 ? 57  SER A CB  1 
ATOM   2607 O  OG  A SER B 1 57  ? -31.909 -19.596 15.765  0.50 8.37  ? 57  SER A OG  1 
ATOM   2608 O  OG  B SER B 1 57  ? -32.271 -20.128 17.689  0.50 14.98 ? 57  SER A OG  1 
ATOM   2609 N  N   . ALA B 1 58  ? -34.958 -19.195 19.217  1.00 11.30 ? 58  ALA A N   1 
ATOM   2610 C  CA  . ALA B 1 58  ? -35.932 -19.729 20.201  1.00 11.46 ? 58  ALA A CA  1 
ATOM   2611 C  C   . ALA B 1 58  ? -37.285 -19.051 19.919  1.00 12.74 ? 58  ALA A C   1 
ATOM   2612 O  O   . ALA B 1 58  ? -37.346 -17.809 19.651  1.00 15.76 ? 58  ALA A O   1 
ATOM   2613 C  CB  . ALA B 1 58  ? -35.460 -19.402 21.618  1.00 12.81 ? 58  ALA A CB  1 
ATOM   2614 N  N   . LYS B 1 59  ? -38.344 -19.806 19.996  1.00 11.20 ? 59  LYS A N   1 
ATOM   2615 C  CA  . LYS B 1 59  ? -39.695 -19.263 19.764  1.00 12.11 ? 59  LYS A CA  1 
ATOM   2616 C  C   . LYS B 1 59  ? -40.662 -19.389 20.924  1.00 12.06 ? 59  LYS A C   1 
ATOM   2617 O  O   . LYS B 1 59  ? -41.357 -18.410 21.233  1.00 12.34 ? 59  LYS A O   1 
ATOM   2618 C  CB  . LYS B 1 59  ? -40.281 -19.988 18.590  1.00 15.36 ? 59  LYS A CB  1 
ATOM   2619 C  CG  . LYS B 1 59  ? -39.542 -19.666 17.233  1.00 21.45 ? 59  LYS A CG  1 
ATOM   2620 C  CD  . LYS B 1 59  ? -39.223 -18.149 17.083  1.00 23.24 ? 59  LYS A CD  1 
ATOM   2621 C  CE  . LYS B 1 59  ? -37.971 -17.988 16.210  1.00 27.18 ? 59  LYS A CE  1 
ATOM   2622 N  NZ  . LYS B 1 59  ? -37.657 -16.761 15.485  1.00 28.46 ? 59  LYS A NZ  1 
ATOM   2623 N  N   A ILE B 1 60  ? -40.872 -20.599 21.469  0.50 11.94 ? 60  ILE A N   1 
ATOM   2624 N  N   B ILE B 1 60  ? -40.719 -20.551 21.553  0.50 11.73 ? 60  ILE A N   1 
ATOM   2625 C  CA  A ILE B 1 60  ? -41.902 -20.821 22.499  0.50 11.42 ? 60  ILE A CA  1 
ATOM   2626 C  CA  B ILE B 1 60  ? -41.862 -20.915 22.372  0.50 11.04 ? 60  ILE A CA  1 
ATOM   2627 C  C   A ILE B 1 60  ? -41.381 -21.807 23.542  0.50 10.05 ? 60  ILE A C   1 
ATOM   2628 C  C   B ILE B 1 60  ? -41.251 -21.710 23.557  0.50 9.96  ? 60  ILE A C   1 
ATOM   2629 O  O   A ILE B 1 60  ? -40.621 -22.727 23.253  0.50 9.50  ? 60  ILE A O   1 
ATOM   2630 O  O   B ILE B 1 60  ? -40.202 -22.355 23.356  0.50 9.74  ? 60  ILE A O   1 
ATOM   2631 C  CB  A ILE B 1 60  ? -43.245 -21.429 22.024  0.50 10.44 ? 60  ILE A CB  1 
ATOM   2632 C  CB  B ILE B 1 60  ? -42.916 -21.692 21.555  0.50 11.28 ? 60  ILE A CB  1 
ATOM   2633 C  CG1 A ILE B 1 60  ? -43.037 -22.657 21.172  0.50 11.38 ? 60  ILE A CG1 1 
ATOM   2634 C  CG1 B ILE B 1 60  ? -43.451 -20.786 20.453  0.50 10.57 ? 60  ILE A CG1 1 
ATOM   2635 C  CG2 A ILE B 1 60  ? -44.081 -20.411 21.290  0.50 12.63 ? 60  ILE A CG2 1 
ATOM   2636 C  CG2 B ILE B 1 60  ? -44.064 -22.092 22.450  0.50 11.60 ? 60  ILE A CG2 1 
ATOM   2637 C  CD1 A ILE B 1 60  ? -44.368 -23.330 21.034  0.50 10.94 ? 60  ILE A CD1 1 
ATOM   2638 C  CD1 B ILE B 1 60  ? -44.134 -19.675 21.195  0.50 16.57 ? 60  ILE A CD1 1 
ATOM   2639 N  N   . ILE B 1 61  ? -41.878 -21.668 24.757  1.00 10.64 ? 61  ILE A N   1 
ATOM   2640 C  CA  . ILE B 1 61  ? -41.663 -22.711 25.804  1.00 10.41 ? 61  ILE A CA  1 
ATOM   2641 C  C   . ILE B 1 61  ? -43.029 -23.303 26.127  1.00 10.98 ? 61  ILE A C   1 
ATOM   2642 O  O   . ILE B 1 61  ? -44.030 -22.545 26.223  1.00 12.02 ? 61  ILE A O   1 
ATOM   2643 C  CB  . ILE B 1 61  ? -40.940 -22.136 27.011  1.00 11.38 ? 61  ILE A CB  1 
ATOM   2644 C  CG1 . ILE B 1 61  ? -40.471 -23.260 27.923  1.00 11.23 ? 61  ILE A CG1 1 
ATOM   2645 C  CG2 . ILE B 1 61  ? -41.776 -21.106 27.785  1.00 11.98 ? 61  ILE A CG2 1 
ATOM   2646 C  CD1 . ILE B 1 61  ? -39.558 -22.775 29.053  1.00 13.61 ? 61  ILE A CD1 1 
ATOM   2647 N  N   . SER B 1 62  ? -43.105 -24.586 26.309  1.00 11.25 ? 62  SER A N   1 
ATOM   2648 C  CA  . SER B 1 62  ? -44.340 -25.208 26.651  1.00 12.09 ? 62  SER A CA  1 
ATOM   2649 C  C   . SER B 1 62  ? -44.192 -26.313 27.624  1.00 11.95 ? 62  SER A C   1 
ATOM   2650 O  O   . SER B 1 62  ? -43.038 -26.812 27.809  1.00 11.93 ? 62  SER A O   1 
ATOM   2651 C  CB  . SER B 1 62  ? -45.047 -25.647 25.397  1.00 14.09 ? 62  SER A CB  1 
ATOM   2652 O  OG  . SER B 1 62  ? -44.247 -26.625 24.790  1.00 17.23 ? 62  SER A OG  1 
ATOM   2653 N  N   . ASN B 1 63  ? -45.299 -26.733 28.262  1.00 10.53 ? 63  ASN A N   1 
ATOM   2654 C  CA  . ASN B 1 63  ? -45.299 -27.906 29.119  1.00 11.19 ? 63  ASN A CA  1 
ATOM   2655 C  C   . ASN B 1 63  ? -45.885 -29.076 28.304  1.00 11.11 ? 63  ASN A C   1 
ATOM   2656 O  O   . ASN B 1 63  ? -47.092 -29.116 27.963  1.00 13.61 ? 63  ASN A O   1 
ATOM   2657 C  CB  . ASN B 1 63  ? -46.130 -27.635 30.387  1.00 12.25 ? 63  ASN A CB  1 
ATOM   2658 C  CG  . ASN B 1 63  ? -46.191 -28.809 31.270  1.00 12.23 ? 63  ASN A CG  1 
ATOM   2659 O  OD1 . ASN B 1 63  ? -45.823 -29.918 30.946  1.00 13.43 ? 63  ASN A OD1 1 
ATOM   2660 N  ND2 . ASN B 1 63  ? -46.719 -28.605 32.494  1.00 12.35 ? 63  ASN A ND2 1 
ATOM   2661 N  N   . SER B 1 64  ? -45.112 -30.044 27.931  1.00 10.84 ? 64  SER A N   1 
ATOM   2662 C  CA  . SER B 1 64  ? -45.602 -31.186 27.126  1.00 12.11 ? 64  SER A CA  1 
ATOM   2663 C  C   . SER B 1 64  ? -46.227 -32.228 28.024  1.00 12.40 ? 64  SER A C   1 
ATOM   2664 O  O   . SER B 1 64  ? -46.815 -33.178 27.492  1.00 13.79 ? 64  SER A O   1 
ATOM   2665 C  CB  . SER B 1 64  ? -44.390 -31.887 26.500  1.00 12.46 ? 64  SER A CB  1 
ATOM   2666 O  OG  . SER B 1 64  ? -43.554 -32.459 27.554  1.00 11.68 ? 64  SER A OG  1 
ATOM   2667 N  N   . GLY B 1 65  ? -46.198 -32.004 29.346  1.00 11.68 ? 65  GLY A N   1 
ATOM   2668 C  CA  . GLY B 1 65  ? -46.646 -33.079 30.286  1.00 13.38 ? 65  GLY A CA  1 
ATOM   2669 C  C   . GLY B 1 65  ? -45.519 -33.985 30.760  1.00 11.23 ? 65  GLY A C   1 
ATOM   2670 O  O   . GLY B 1 65  ? -45.659 -34.668 31.767  1.00 12.22 ? 65  GLY A O   1 
ATOM   2671 N  N   . HIS B 1 66  ? -44.374 -33.941 30.057  1.00 10.77 ? 66  HIS A N   1 
ATOM   2672 C  CA  . HIS B 1 66  ? -43.251 -34.809 30.337  1.00 11.06 ? 66  HIS A CA  1 
ATOM   2673 C  C   . HIS B 1 66  ? -42.003 -34.039 30.636  1.00 10.60 ? 66  HIS A C   1 
ATOM   2674 O  O   . HIS B 1 66  ? -41.061 -34.653 31.147  1.00 10.07 ? 66  HIS A O   1 
ATOM   2675 C  CB  . HIS B 1 66  ? -42.983 -35.643 29.057  1.00 13.47 ? 66  HIS A CB  1 
ATOM   2676 C  CG  . HIS B 1 66  ? -44.213 -36.275 28.522  1.00 14.45 ? 66  HIS A CG  1 
ATOM   2677 N  ND1 . HIS B 1 66  ? -44.646 -36.040 27.256  1.00 18.34 ? 66  HIS A ND1 1 
ATOM   2678 C  CD2 . HIS B 1 66  ? -45.022 -37.231 29.091  1.00 16.15 ? 66  HIS A CD2 1 
ATOM   2679 C  CE1 . HIS B 1 66  ? -45.776 -36.815 27.058  1.00 16.65 ? 66  HIS A CE1 1 
ATOM   2680 N  NE2 . HIS B 1 66  ? -45.992 -37.536 28.148  1.00 19.61 ? 66  HIS A NE2 1 
ATOM   2681 N  N   . SER B 1 67  ? -41.980 -32.738 30.348  1.00 8.52  ? 67  SER A N   1 
ATOM   2682 C  CA  . SER B 1 67  ? -40.921 -31.812 30.674  1.00 8.79  ? 67  SER A CA  1 
ATOM   2683 C  C   . SER B 1 67  ? -41.383 -30.414 30.197  1.00 9.41  ? 67  SER A C   1 
ATOM   2684 O  O   . SER B 1 67  ? -42.555 -30.296 29.705  1.00 10.51 ? 67  SER A O   1 
ATOM   2685 C  CB  . SER B 1 67  ? -39.531 -32.133 29.951  1.00 9.95  ? 67  SER A CB  1 
ATOM   2686 O  OG  . SER B 1 67  ? -38.498 -31.323 30.453  1.00 10.07 ? 67  SER A OG  1 
ATOM   2687 N  N   . PHE B 1 68  ? -40.553 -29.402 30.319  1.00 8.44  ? 68  PHE A N   1 
ATOM   2688 C  CA  . PHE B 1 68  ? -40.770 -28.179 29.528  1.00 9.13  ? 68  PHE A CA  1 
ATOM   2689 C  C   . PHE B 1 68  ? -40.024 -28.463 28.264  1.00 9.69  ? 68  PHE A C   1 
ATOM   2690 O  O   . PHE B 1 68  ? -38.986 -29.146 28.174  1.00 10.53 ? 68  PHE A O   1 
ATOM   2691 C  CB  . PHE B 1 68  ? -40.264 -26.908 30.243  1.00 9.93  ? 68  PHE A CB  1 
ATOM   2692 C  CG  . PHE B 1 68  ? -38.787 -26.790 30.297  1.00 10.25 ? 68  PHE A CG  1 
ATOM   2693 C  CD1 . PHE B 1 68  ? -38.111 -27.240 31.459  1.00 10.83 ? 68  PHE A CD1 1 
ATOM   2694 C  CD2 . PHE B 1 68  ? -38.040 -26.349 29.248  1.00 11.39 ? 68  PHE A CD2 1 
ATOM   2695 C  CE1 . PHE B 1 68  ? -36.726 -27.185 31.521  1.00 10.79 ? 68  PHE A CE1 1 
ATOM   2696 C  CE2 . PHE B 1 68  ? -36.627 -26.262 29.303  1.00 10.90 ? 68  PHE A CE2 1 
ATOM   2697 C  CZ  . PHE B 1 68  ? -35.978 -26.723 30.481  1.00 11.37 ? 68  PHE A CZ  1 
ATOM   2698 N  N   . ASN B 1 69  ? -40.512 -27.792 27.218  1.00 11.02 ? 69  ASN A N   1 
ATOM   2699 C  CA  . ASN B 1 69  ? -39.789 -27.819 25.895  1.00 11.47 ? 69  ASN A CA  1 
ATOM   2700 C  C   . ASN B 1 69  ? -39.654 -26.416 25.357  1.00 9.98  ? 69  ASN A C   1 
ATOM   2701 O  O   . ASN B 1 69  ? -40.670 -25.687 25.222  1.00 11.05 ? 69  ASN A O   1 
ATOM   2702 C  CB  . ASN B 1 69  ? -40.626 -28.519 24.813  1.00 13.50 ? 69  ASN A CB  1 
ATOM   2703 C  CG  . ASN B 1 69  ? -40.810 -29.950 25.053  1.00 18.06 ? 69  ASN A CG  1 
ATOM   2704 O  OD1 . ASN B 1 69  ? -39.922 -30.611 25.611  1.00 20.47 ? 69  ASN A OD1 1 
ATOM   2705 N  ND2 . ASN B 1 69  ? -41.829 -30.522 24.389  1.00 18.36 ? 69  ASN A ND2 1 
ATOM   2706 N  N   . VAL B 1 70  ? -38.426 -25.974 25.146  1.00 9.57  ? 70  VAL A N   1 
ATOM   2707 C  CA  . VAL B 1 70  ? -38.120 -24.746 24.340  1.00 9.54  ? 70  VAL A CA  1 
ATOM   2708 C  C   . VAL B 1 70  ? -37.976 -25.131 22.906  1.00 9.37  ? 70  VAL A C   1 
ATOM   2709 O  O   . VAL B 1 70  ? -37.142 -25.996 22.565  1.00 10.47 ? 70  VAL A O   1 
ATOM   2710 C  CB  . VAL B 1 70  ? -36.868 -24.034 24.795  1.00 9.86  ? 70  VAL A CB  1 
ATOM   2711 C  CG1 . VAL B 1 70  ? -36.664 -22.796 23.947  1.00 12.04 ? 70  VAL A CG1 1 
ATOM   2712 C  CG2 . VAL B 1 70  ? -36.926 -23.641 26.272  1.00 12.06 ? 70  VAL A CG2 1 
ATOM   2713 N  N   . ASP B 1 71  ? -38.810 -24.572 22.046  1.00 9.83  ? 71  ASP A N   1 
ATOM   2714 C  CA  . ASP B 1 71  ? -38.787 -25.003 20.587  1.00 10.03 ? 71  ASP A CA  1 
ATOM   2715 C  C   . ASP B 1 71  ? -38.185 -23.864 19.784  1.00 10.23 ? 71  ASP A C   1 
ATOM   2716 O  O   . ASP B 1 71  ? -38.440 -22.676 20.118  1.00 11.32 ? 71  ASP A O   1 
ATOM   2717 C  CB  . ASP B 1 71  ? -40.244 -25.246 20.095  1.00 13.67 ? 71  ASP A CB  1 
ATOM   2718 C  CG  . ASP B 1 71  ? -40.853 -26.505 20.691  1.00 16.39 ? 71  ASP A CG  1 
ATOM   2719 O  OD1 . ASP B 1 71  ? -40.091 -27.463 20.930  1.00 19.76 ? 71  ASP A OD1 1 
ATOM   2720 O  OD2 . ASP B 1 71  ? -42.081 -26.538 20.922  1.00 22.41 ? 71  ASP A OD2 1 
ATOM   2721 N  N   . PHE B 1 72  ? -37.416 -24.297 18.795  1.00 10.46 ? 72  PHE A N   1 
ATOM   2722 C  CA  . PHE B 1 72  ? -36.656 -23.338 17.924  1.00 11.36 ? 72  PHE A CA  1 
ATOM   2723 C  C   . PHE B 1 72  ? -37.120 -23.473 16.509  1.00 11.89 ? 72  PHE A C   1 
ATOM   2724 O  O   . PHE B 1 72  ? -37.675 -24.417 16.097  1.00 13.78 ? 72  PHE A O   1 
ATOM   2725 C  CB  . PHE B 1 72  ? -35.162 -23.676 18.017  1.00 11.81 ? 72  PHE A CB  1 
ATOM   2726 C  CG  . PHE B 1 72  ? -34.602 -23.558 19.428  1.00 10.18 ? 72  PHE A CG  1 
ATOM   2727 C  CD1 . PHE B 1 72  ? -34.799 -24.577 20.396  1.00 10.61 ? 72  PHE A CD1 1 
ATOM   2728 C  CD2 . PHE B 1 72  ? -33.867 -22.450 19.796  1.00 11.25 ? 72  PHE A CD2 1 
ATOM   2729 C  CE1 . PHE B 1 72  ? -34.219 -24.382 21.686  1.00 10.65 ? 72  PHE A CE1 1 
ATOM   2730 C  CE2 . PHE B 1 72  ? -33.290 -22.309 21.076  1.00 11.34 ? 72  PHE A CE2 1 
ATOM   2731 C  CZ  . PHE B 1 72  ? -33.540 -23.277 22.012  1.00 10.19 ? 72  PHE A CZ  1 
ATOM   2732 N  N   A ASP B 1 73  ? -37.009 -22.358 15.804  0.50 11.32 ? 73  ASP A N   1 
ATOM   2733 N  N   B ASP B 1 73  ? -36.556 -22.561 15.646  0.50 12.52 ? 73  ASP A N   1 
ATOM   2734 C  CA  A ASP B 1 73  ? -37.282 -22.378 14.368  0.50 10.56 ? 73  ASP A CA  1 
ATOM   2735 C  CA  B ASP B 1 73  ? -36.767 -22.543 14.168  0.50 13.06 ? 73  ASP A CA  1 
ATOM   2736 C  C   A ASP B 1 73  ? -36.800 -23.698 13.575  0.50 9.65  ? 73  ASP A C   1 
ATOM   2737 C  C   B ASP B 1 73  ? -36.616 -23.867 13.395  0.50 11.84 ? 73  ASP A C   1 
ATOM   2738 O  O   A ASP B 1 73  ? -35.673 -24.147 13.717  0.50 11.49 ? 73  ASP A O   1 
ATOM   2739 O  O   B ASP B 1 73  ? -35.539 -24.508 13.274  0.50 13.76 ? 73  ASP A O   1 
ATOM   2740 C  CB  A ASP B 1 73  ? -36.606 -21.151 13.789  0.50 10.96 ? 73  ASP A CB  1 
ATOM   2741 C  CB  B ASP B 1 73  ? -35.983 -21.429 13.455  0.50 15.82 ? 73  ASP A CB  1 
ATOM   2742 C  CG  A ASP B 1 73  ? -37.065 -20.868 12.383  0.50 12.71 ? 73  ASP A CG  1 
ATOM   2743 C  CG  B ASP B 1 73  ? -36.352 -20.076 13.942  0.50 15.06 ? 73  ASP A CG  1 
ATOM   2744 O  OD1 A ASP B 1 73  ? -36.602 -21.539 11.469  0.50 14.56 ? 73  ASP A OD1 1 
ATOM   2745 O  OD1 B ASP B 1 73  ? -37.517 -19.959 14.307  0.50 18.67 ? 73  ASP A OD1 1 
ATOM   2746 O  OD2 A ASP B 1 73  ? -38.025 -20.072 12.300  0.50 16.47 ? 73  ASP A OD2 1 
ATOM   2747 O  OD2 B ASP B 1 73  ? -35.457 -19.147 13.880  0.50 16.70 ? 73  ASP A OD2 1 
ATOM   2748 N  N   . ASP B 1 74  ? -37.675 -24.277 12.739  1.00 12.78 ? 74  ASP A N   1 
ATOM   2749 C  CA  . ASP B 1 74  ? -37.592 -25.552 12.047  1.00 14.46 ? 74  ASP A CA  1 
ATOM   2750 C  C   . ASP B 1 74  ? -36.907 -25.470 10.674  1.00 15.89 ? 74  ASP A C   1 
ATOM   2751 O  O   . ASP B 1 74  ? -36.517 -26.486 10.165  1.00 16.86 ? 74  ASP A O   1 
ATOM   2752 C  CB  . ASP B 1 74  ? -38.976 -26.097 11.791  1.00 19.20 ? 74  ASP A CB  1 
ATOM   2753 C  CG  . ASP B 1 74  ? -39.529 -26.839 12.921  1.00 28.20 ? 74  ASP A CG  1 
ATOM   2754 O  OD1 . ASP B 1 74  ? -38.806 -27.605 13.535  1.00 35.39 ? 74  ASP A OD1 1 
ATOM   2755 O  OD2 . ASP B 1 74  ? -40.733 -26.710 13.146  1.00 24.93 ? 74  ASP A OD2 1 
ATOM   2756 N  N   . THR B 1 75  ? -36.783 -24.291 10.067  1.00 14.93 ? 75  THR A N   1 
ATOM   2757 C  CA  . THR B 1 75  ? -36.316 -24.154 8.655   1.00 14.34 ? 75  THR A CA  1 
ATOM   2758 C  C   . THR B 1 75  ? -35.131 -23.232 8.371   1.00 14.63 ? 75  THR A C   1 
ATOM   2759 O  O   . THR B 1 75  ? -34.776 -23.002 7.174   1.00 13.44 ? 75  THR A O   1 
ATOM   2760 C  CB  . THR B 1 75  ? -37.547 -23.826 7.747   1.00 15.33 ? 75  THR A CB  1 
ATOM   2761 O  OG1 . THR B 1 75  ? -38.010 -22.523 8.122   1.00 16.65 ? 75  THR A OG1 1 
ATOM   2762 C  CG2 . THR B 1 75  ? -38.696 -24.952 7.856   1.00 19.65 ? 75  THR A CG2 1 
ATOM   2763 N  N   . GLU B 1 76  ? -34.349 -22.765 9.322   1.00 13.96 ? 76  GLU A N   1 
ATOM   2764 C  CA  . GLU B 1 76  ? -33.247 -21.985 9.140   1.00 12.49 ? 76  GLU A CA  1 
ATOM   2765 C  C   . GLU B 1 76  ? -31.951 -22.600 9.695   1.00 13.05 ? 76  GLU A C   1 
ATOM   2766 O  O   . GLU B 1 76  ? -32.107 -23.422 10.634  1.00 12.51 ? 76  GLU A O   1 
ATOM   2767 C  CB  . GLU B 1 76  ? -33.475 -20.639 9.905   1.00 14.21 ? 76  GLU A CB  1 
ATOM   2768 C  CG  . GLU B 1 76  ? -34.699 -19.822 9.347   1.00 16.64 ? 76  GLU A CG  1 
ATOM   2769 C  CD  . GLU B 1 76  ? -35.143 -18.697 10.282  1.00 24.04 ? 76  GLU A CD  1 
ATOM   2770 O  OE1 . GLU B 1 76  ? -34.632 -18.604 11.485  1.00 23.52 ? 76  GLU A OE1 1 
ATOM   2771 O  OE2 . GLU B 1 76  ? -36.012 -17.837 9.884   1.00 23.89 ? 76  GLU A OE2 1 
ATOM   2772 N  N   . ASN B 1 77  ? -30.791 -22.263 9.194   1.00 11.97 ? 77  ASN A N   1 
ATOM   2773 C  CA  . ASN B 1 77  ? -29.503 -22.713 9.738   1.00 13.18 ? 77  ASN A CA  1 
ATOM   2774 C  C   . ASN B 1 77  ? -28.749 -21.693 10.589  1.00 10.75 ? 77  ASN A C   1 
ATOM   2775 O  O   . ASN B 1 77  ? -27.547 -21.719 10.653  1.00 12.50 ? 77  ASN A O   1 
ATOM   2776 C  CB  . ASN B 1 77  ? -28.567 -23.346 8.652   1.00 15.14 ? 77  ASN A CB  1 
ATOM   2777 C  CG  . ASN B 1 77  ? -28.963 -24.766 8.248   1.00 13.80 ? 77  ASN A CG  1 
ATOM   2778 O  OD1 . ASN B 1 77  ? -29.728 -25.423 8.947   1.00 13.00 ? 77  ASN A OD1 1 
ATOM   2779 N  ND2 . ASN B 1 77  ? -28.393 -25.267 7.107   1.00 14.80 ? 77  ASN A ND2 1 
ATOM   2780 N  N   A LYS B 1 78  ? -29.538 -20.854 11.279  0.50 10.61 ? 78  LYS A N   1 
ATOM   2781 N  N   B LYS B 1 78  ? -29.488 -20.822 11.282  0.50 11.49 ? 78  LYS A N   1 
ATOM   2782 C  CA  A LYS B 1 78  ? -28.975 -19.870 12.218  0.50 10.06 ? 78  LYS A CA  1 
ATOM   2783 C  CA  B LYS B 1 78  ? -28.809 -19.877 12.188  0.50 11.14 ? 78  LYS A CA  1 
ATOM   2784 C  C   A LYS B 1 78  ? -28.380 -20.518 13.502  0.50 10.22 ? 78  LYS A C   1 
ATOM   2785 C  C   B LYS B 1 78  ? -28.262 -20.609 13.452  0.50 10.93 ? 78  LYS A C   1 
ATOM   2786 O  O   A LYS B 1 78  ? -27.449 -19.977 14.129  0.50 10.97 ? 78  LYS A O   1 
ATOM   2787 O  O   B LYS B 1 78  ? -27.226 -20.241 13.997  0.50 11.75 ? 78  LYS A O   1 
ATOM   2788 C  CB  A LYS B 1 78  ? -30.048 -18.859 12.593  0.50 10.09 ? 78  LYS A CB  1 
ATOM   2789 C  CB  B LYS B 1 78  ? -29.724 -18.684 12.536  0.50 11.82 ? 78  LYS A CB  1 
ATOM   2790 C  CG  A LYS B 1 78  ? -30.612 -18.074 11.443  0.50 11.02 ? 78  LYS A CG  1 
ATOM   2791 C  CG  B LYS B 1 78  ? -30.032 -17.724 11.356  0.50 14.45 ? 78  LYS A CG  1 
ATOM   2792 C  CD  A LYS B 1 78  ? -30.865 -16.686 11.967  0.50 16.53 ? 78  LYS A CD  1 
ATOM   2793 C  CD  B LYS B 1 78  ? -31.328 -16.931 11.580  0.50 21.91 ? 78  LYS A CD  1 
ATOM   2794 C  CE  A LYS B 1 78  ? -32.101 -16.663 12.875  0.50 16.08 ? 78  LYS A CE  1 
ATOM   2795 C  CE  B LYS B 1 78  ? -31.383 -15.650 10.692  0.50 21.87 ? 78  LYS A CE  1 
ATOM   2796 N  NZ  A LYS B 1 78  ? -32.818 -15.348 13.053  0.50 18.92 ? 78  LYS A NZ  1 
ATOM   2797 N  NZ  B LYS B 1 78  ? -32.277 -14.607 11.250  0.50 27.71 ? 78  LYS A NZ  1 
ATOM   2798 N  N   . SER B 1 79  ? -28.980 -21.681 13.889  1.00 10.32 ? 79  SER A N   1 
ATOM   2799 C  CA  . SER B 1 79  ? -28.539 -22.414 15.110  1.00 9.96  ? 79  SER A CA  1 
ATOM   2800 C  C   . SER B 1 79  ? -28.291 -23.831 14.707  1.00 8.22  ? 79  SER A C   1 
ATOM   2801 O  O   . SER B 1 79  ? -29.279 -24.599 14.492  1.00 9.59  ? 79  SER A O   1 
ATOM   2802 C  CB  . SER B 1 79  ? -29.641 -22.270 16.146  1.00 9.08  ? 79  SER A CB  1 
ATOM   2803 O  OG  . SER B 1 79  ? -29.722 -20.932 16.633  1.00 10.18 ? 79  SER A OG  1 
ATOM   2804 N  N   . VAL B 1 80  ? -27.038 -24.229 14.674  1.00 10.33 ? 80  VAL A N   1 
ATOM   2805 C  CA  . VAL B 1 80  ? -26.629 -25.573 14.159  1.00 9.22  ? 80  VAL A CA  1 
ATOM   2806 C  C   . VAL B 1 80  ? -25.426 -26.110 14.962  1.00 10.30 ? 80  VAL A C   1 
ATOM   2807 O  O   . VAL B 1 80  ? -24.622 -25.325 15.507  1.00 10.80 ? 80  VAL A O   1 
ATOM   2808 C  CB  . VAL B 1 80  ? -26.274 -25.511 12.649  1.00 10.34 ? 80  VAL A CB  1 
ATOM   2809 C  CG1 . VAL B 1 80  ? -27.472 -25.121 11.793  1.00 11.89 ? 80  VAL A CG1 1 
ATOM   2810 C  CG2 . VAL B 1 80  ? -25.076 -24.541 12.428  1.00 14.13 ? 80  VAL A CG2 1 
ATOM   2811 N  N   . LEU B 1 81  ? -25.413 -27.457 15.004  1.00 9.60  ? 81  LEU A N   1 
ATOM   2812 C  CA  . LEU B 1 81  ? -24.341 -28.230 15.640  1.00 10.75 ? 81  LEU A CA  1 
ATOM   2813 C  C   . LEU B 1 81  ? -23.638 -28.977 14.531  1.00 9.65  ? 81  LEU A C   1 
ATOM   2814 O  O   . LEU B 1 81  ? -24.265 -29.657 13.689  1.00 10.64 ? 81  LEU A O   1 
ATOM   2815 C  CB  . LEU B 1 81  ? -25.016 -29.226 16.673  1.00 10.18 ? 81  LEU A CB  1 
ATOM   2816 C  CG  . LEU B 1 81  ? -23.995 -30.154 17.333  1.00 10.95 ? 81  LEU A CG  1 
ATOM   2817 C  CD1 . LEU B 1 81  ? -23.114 -29.332 18.276  1.00 12.59 ? 81  LEU A CD1 1 
ATOM   2818 C  CD2 . LEU B 1 81  ? -24.824 -31.207 18.109  1.00 11.05 ? 81  LEU A CD2 1 
ATOM   2819 N  N   . ARG B 1 82  ? -22.295 -28.806 14.533  1.00 11.68 ? 82  ARG A N   1 
ATOM   2820 C  CA  . ARG B 1 82  ? -21.448 -29.502 13.549  1.00 11.77 ? 82  ARG A CA  1 
ATOM   2821 C  C   . ARG B 1 82  ? -20.234 -30.033 14.201  1.00 12.30 ? 82  ARG A C   1 
ATOM   2822 O  O   . ARG B 1 82  ? -19.969 -29.717 15.388  1.00 12.07 ? 82  ARG A O   1 
ATOM   2823 C  CB  . ARG B 1 82  ? -21.041 -28.455 12.383  1.00 11.66 ? 82  ARG A CB  1 
ATOM   2824 C  CG  . ARG B 1 82  ? -22.263 -28.099 11.506  1.00 12.22 ? 82  ARG A CG  1 
ATOM   2825 C  CD  . ARG B 1 82  ? -21.932 -26.863 10.573  1.00 12.66 ? 82  ARG A CD  1 
ATOM   2826 N  NE  . ARG B 1 82  ? -21.769 -25.640 11.349  1.00 14.39 ? 82  ARG A NE  1 
ATOM   2827 C  CZ  . ARG B 1 82  ? -21.545 -24.388 10.881  1.00 14.24 ? 82  ARG A CZ  1 
ATOM   2828 N  NH1 . ARG B 1 82  ? -21.395 -24.183 9.577   1.00 15.23 ? 82  ARG A NH1 1 
ATOM   2829 N  NH2 . ARG B 1 82  ? -21.495 -23.365 11.712  1.00 14.04 ? 82  ARG A NH2 1 
ATOM   2830 N  N   . GLY B 1 83  ? -19.476 -30.863 13.486  1.00 11.06 ? 83  GLY A N   1 
ATOM   2831 C  CA  . GLY B 1 83  ? -18.255 -31.319 14.049  1.00 11.05 ? 83  GLY A CA  1 
ATOM   2832 C  C   . GLY B 1 83  ? -18.455 -32.446 14.993  1.00 11.78 ? 83  GLY A C   1 
ATOM   2833 O  O   . GLY B 1 83  ? -19.427 -33.260 14.978  1.00 12.09 ? 83  GLY A O   1 
ATOM   2834 N  N   . GLY B 1 84  ? -17.449 -32.627 15.863  1.00 13.89 ? 84  GLY A N   1 
ATOM   2835 C  CA  . GLY B 1 84  ? -17.470 -33.861 16.680  1.00 14.89 ? 84  GLY A CA  1 
ATOM   2836 C  C   . GLY B 1 84  ? -17.560 -35.162 15.868  1.00 13.60 ? 84  GLY A C   1 
ATOM   2837 O  O   . GLY B 1 84  ? -16.823 -35.376 14.865  1.00 16.13 ? 84  GLY A O   1 
ATOM   2838 N  N   . PRO B 1 85  ? -18.513 -36.025 16.222  1.00 11.86 ? 85  PRO A N   1 
ATOM   2839 C  CA  . PRO B 1 85  ? -18.767 -37.280 15.514  1.00 12.63 ? 85  PRO A CA  1 
ATOM   2840 C  C   . PRO B 1 85  ? -19.664 -37.075 14.262  1.00 13.80 ? 85  PRO A C   1 
ATOM   2841 O  O   . PRO B 1 85  ? -19.874 -38.059 13.551  1.00 14.37 ? 85  PRO A O   1 
ATOM   2842 C  CB  . PRO B 1 85  ? -19.530 -38.127 16.557  1.00 14.24 ? 85  PRO A CB  1 
ATOM   2843 C  CG  . PRO B 1 85  ? -20.334 -37.084 17.300  1.00 12.83 ? 85  PRO A CG  1 
ATOM   2844 C  CD  . PRO B 1 85  ? -19.385 -35.872 17.419  1.00 12.39 ? 85  PRO A CD  1 
ATOM   2845 N  N   . LEU B 1 86  ? -20.182 -35.855 14.021  1.00 12.74 ? 86  LEU A N   1 
ATOM   2846 C  CA  . LEU B 1 86  ? -21.261 -35.719 13.075  1.00 12.16 ? 86  LEU A CA  1 
ATOM   2847 C  C   . LEU B 1 86  ? -20.769 -35.478 11.625  1.00 13.78 ? 86  LEU A C   1 
ATOM   2848 O  O   . LEU B 1 86  ? -19.769 -34.737 11.421  1.00 13.51 ? 86  LEU A O   1 
ATOM   2849 C  CB  . LEU B 1 86  ? -22.037 -34.445 13.476  1.00 13.26 ? 86  LEU A CB  1 
ATOM   2850 C  CG  . LEU B 1 86  ? -22.660 -34.552 14.914  1.00 10.57 ? 86  LEU A CG  1 
ATOM   2851 C  CD1 . LEU B 1 86  ? -23.256 -33.210 15.294  1.00 12.54 ? 86  LEU A CD1 1 
ATOM   2852 C  CD2 . LEU B 1 86  ? -23.675 -35.749 15.083  1.00 11.74 ? 86  LEU A CD2 1 
ATOM   2853 N  N   . THR B 1 87  ? -21.534 -36.051 10.729  1.00 13.63 ? 87  THR A N   1 
ATOM   2854 C  CA  . THR B 1 87  ? -21.351 -35.651 9.306   1.00 15.52 ? 87  THR A CA  1 
ATOM   2855 C  C   . THR B 1 87  ? -22.443 -34.631 8.864   1.00 12.64 ? 87  THR A C   1 
ATOM   2856 O  O   . THR B 1 87  ? -23.625 -34.959 9.043   1.00 14.54 ? 87  THR A O   1 
ATOM   2857 C  CB  . THR B 1 87  ? -21.475 -36.909 8.398   1.00 14.27 ? 87  THR A CB  1 
ATOM   2858 O  OG1 . THR B 1 87  ? -20.363 -37.734 8.766   1.00 19.72 ? 87  THR A OG1 1 
ATOM   2859 C  CG2 . THR B 1 87  ? -21.244 -36.541 6.920   1.00 16.60 ? 87  THR A CG2 1 
ATOM   2860 N  N   . GLY B 1 88  ? -22.066 -33.426 8.459   1.00 13.15 ? 88  GLY A N   1 
ATOM   2861 C  CA  . GLY B 1 88  ? -23.046 -32.420 8.034   1.00 13.02 ? 88  GLY A CA  1 
ATOM   2862 C  C   . GLY B 1 88  ? -23.601 -31.577 9.175   1.00 13.25 ? 88  GLY A C   1 
ATOM   2863 O  O   . GLY B 1 88  ? -23.019 -31.612 10.283  1.00 14.56 ? 88  GLY A O   1 
ATOM   2864 N  N   . SER B 1 89  ? -24.691 -30.928 8.927   1.00 12.13 ? 89  SER A N   1 
ATOM   2865 C  CA  . SER B 1 89  ? -25.129 -29.861 9.809   1.00 11.58 ? 89  SER A CA  1 
ATOM   2866 C  C   . SER B 1 89  ? -26.475 -30.338 10.429  1.00 11.47 ? 89  SER A C   1 
ATOM   2867 O  O   . SER B 1 89  ? -27.407 -30.745 9.758   1.00 12.06 ? 89  SER A O   1 
ATOM   2868 C  CB  . SER B 1 89  ? -25.379 -28.617 8.979   1.00 10.57 ? 89  SER A CB  1 
ATOM   2869 O  OG  . SER B 1 89  ? -25.809 -27.499 9.800   1.00 12.07 ? 89  SER A OG  1 
ATOM   2870 N  N   . TYR B 1 90  ? -26.482 -30.245 11.780  1.00 10.75 ? 90  TYR A N   1 
ATOM   2871 C  CA  . TYR B 1 90  ? -27.696 -30.665 12.539  1.00 8.88  ? 90  TYR A CA  1 
ATOM   2872 C  C   . TYR B 1 90  ? -28.315 -29.464 13.147  1.00 8.86  ? 90  TYR A C   1 
ATOM   2873 O  O   . TYR B 1 90  ? -27.665 -28.676 13.930  1.00 10.69 ? 90  TYR A O   1 
ATOM   2874 C  CB  . TYR B 1 90  ? -27.191 -31.677 13.634  1.00 9.41  ? 90  TYR A CB  1 
ATOM   2875 C  CG  . TYR B 1 90  ? -26.955 -33.067 13.085  1.00 8.97  ? 90  TYR A CG  1 
ATOM   2876 C  CD1 . TYR B 1 90  ? -25.868 -33.317 12.241  1.00 10.15 ? 90  TYR A CD1 1 
ATOM   2877 C  CD2 . TYR B 1 90  ? -27.822 -34.134 13.368  1.00 9.60  ? 90  TYR A CD2 1 
ATOM   2878 C  CE1 . TYR B 1 90  ? -25.619 -34.607 11.747  1.00 9.85  ? 90  TYR A CE1 1 
ATOM   2879 C  CE2 . TYR B 1 90  ? -27.615 -35.414 12.886  1.00 10.40 ? 90  TYR A CE2 1 
ATOM   2880 C  CZ  . TYR B 1 90  ? -26.487 -35.619 12.059  1.00 10.33 ? 90  TYR A CZ  1 
ATOM   2881 O  OH  . TYR B 1 90  ? -26.286 -36.890 11.583  1.00 11.08 ? 90  TYR A OH  1 
ATOM   2882 N  N   . ARG B 1 91  ? -29.565 -29.232 12.791  1.00 8.20  ? 91  ARG A N   1 
ATOM   2883 C  CA  . ARG B 1 91  ? -30.281 -28.036 13.128  1.00 9.44  ? 91  ARG A CA  1 
ATOM   2884 C  C   . ARG B 1 91  ? -30.868 -28.106 14.525  1.00 8.05  ? 91  ARG A C   1 
ATOM   2885 O  O   . ARG B 1 91  ? -31.532 -29.142 14.828  1.00 9.06  ? 91  ARG A O   1 
ATOM   2886 C  CB  . ARG B 1 91  ? -31.398 -27.791 12.071  1.00 9.56  ? 91  ARG A CB  1 
ATOM   2887 C  CG  . ARG B 1 91  ? -32.116 -26.441 12.212  1.00 11.63 ? 91  ARG A CG  1 
ATOM   2888 C  CD  . ARG B 1 91  ? -33.102 -26.253 11.073  1.00 13.05 ? 91  ARG A CD  1 
ATOM   2889 N  NE  . ARG B 1 91  ? -32.392 -26.182 9.808   1.00 12.61 ? 91  ARG A NE  1 
ATOM   2890 C  CZ  . ARG B 1 91  ? -32.894 -26.514 8.625   1.00 11.89 ? 91  ARG A CZ  1 
ATOM   2891 N  NH1 . ARG B 1 91  ? -34.140 -26.960 8.512   1.00 11.04 ? 91  ARG A NH1 1 
ATOM   2892 N  NH2 . ARG B 1 91  ? -32.128 -26.397 7.550   1.00 11.54 ? 91  ARG A NH2 1 
ATOM   2893 N  N   . LEU B 1 92  ? -30.705 -27.061 15.324  1.00 7.72  ? 92  LEU A N   1 
ATOM   2894 C  CA  . LEU B 1 92  ? -31.295 -27.072 16.680  1.00 8.05  ? 92  LEU A CA  1 
ATOM   2895 C  C   . LEU B 1 92  ? -32.788 -27.077 16.629  1.00 8.35  ? 92  LEU A C   1 
ATOM   2896 O  O   . LEU B 1 92  ? -33.415 -26.295 15.849  1.00 10.19 ? 92  LEU A O   1 
ATOM   2897 C  CB  . LEU B 1 92  ? -30.790 -25.818 17.352  1.00 8.90  ? 92  LEU A CB  1 
ATOM   2898 C  CG  . LEU B 1 92  ? -31.384 -25.495 18.752  1.00 8.95  ? 92  LEU A CG  1 
ATOM   2899 C  CD1 . LEU B 1 92  ? -31.015 -26.649 19.758  1.00 8.63  ? 92  LEU A CD1 1 
ATOM   2900 C  CD2 . LEU B 1 92  ? -30.890 -24.151 19.280  1.00 10.75 ? 92  LEU A CD2 1 
ATOM   2901 N  N   A ARG B 1 93  ? -33.424 -27.874 17.463  0.50 8.88  ? 93  ARG A N   1 
ATOM   2902 N  N   B ARG B 1 93  ? -33.428 -28.071 17.266  0.50 8.68  ? 93  ARG A N   1 
ATOM   2903 C  CA  A ARG B 1 93  ? -34.867 -27.968 17.412  0.50 9.22  ? 93  ARG A CA  1 
ATOM   2904 C  CA  B ARG B 1 93  ? -34.872 -28.258 17.355  0.50 9.13  ? 93  ARG A CA  1 
ATOM   2905 C  C   A ARG B 1 93  ? -35.556 -27.822 18.760  0.50 9.97  ? 93  ARG A C   1 
ATOM   2906 C  C   B ARG B 1 93  ? -35.477 -27.802 18.726  0.50 10.26 ? 93  ARG A C   1 
ATOM   2907 O  O   A ARG B 1 93  ? -36.652 -27.292 18.810  0.50 8.98  ? 93  ARG A O   1 
ATOM   2908 O  O   B ARG B 1 93  ? -36.411 -26.954 18.775  0.50 9.51  ? 93  ARG A O   1 
ATOM   2909 C  CB  A ARG B 1 93  ? -35.269 -29.262 16.696  0.50 11.33 ? 93  ARG A CB  1 
ATOM   2910 C  CB  B ARG B 1 93  ? -35.168 -29.794 17.110  0.50 9.23  ? 93  ARG A CB  1 
ATOM   2911 C  CG  A ARG B 1 93  ? -36.783 -29.504 16.726  0.50 13.03 ? 93  ARG A CG  1 
ATOM   2912 C  CG  B ARG B 1 93  ? -36.640 -30.168 17.430  0.50 12.20 ? 93  ARG A CG  1 
ATOM   2913 C  CD  A ARG B 1 93  ? -37.593 -28.509 15.941  0.50 18.88 ? 93  ARG A CD  1 
ATOM   2914 C  CD  B ARG B 1 93  ? -37.455 -29.802 16.224  0.50 13.79 ? 93  ARG A CD  1 
ATOM   2915 N  NE  A ARG B 1 93  ? -38.987 -28.813 16.232  0.50 24.08 ? 93  ARG A NE  1 
ATOM   2916 N  NE  B ARG B 1 93  ? -38.782 -30.386 16.338  0.50 15.84 ? 93  ARG A NE  1 
ATOM   2917 C  CZ  A ARG B 1 93  ? -39.784 -27.936 16.836  0.50 26.22 ? 93  ARG A CZ  1 
ATOM   2918 C  CZ  B ARG B 1 93  ? -39.776 -30.206 15.512  0.50 16.29 ? 93  ARG A CZ  1 
ATOM   2919 N  NH1 A ARG B 1 93  ? -39.323 -26.700 17.047  0.50 20.36 ? 93  ARG A NH1 1 
ATOM   2920 N  NH1 B ARG B 1 93  ? -39.609 -29.461 14.422  0.50 17.65 ? 93  ARG A NH1 1 
ATOM   2921 N  NH2 A ARG B 1 93  ? -41.058 -28.242 17.093  0.50 30.68 ? 93  ARG A NH2 1 
ATOM   2922 N  NH2 B ARG B 1 93  ? -40.916 -30.828 15.773  0.50 18.75 ? 93  ARG A NH2 1 
ATOM   2923 N  N   A GLN B 1 94  ? -34.945 -28.305 19.856  0.50 8.35  ? 94  GLN A N   1 
ATOM   2924 N  N   B GLN B 1 94  ? -34.954 -28.384 19.838  0.50 9.43  ? 94  GLN A N   1 
ATOM   2925 C  CA  A GLN B 1 94  ? -35.604 -28.153 21.147  0.50 7.65  ? 94  GLN A CA  1 
ATOM   2926 C  CA  B GLN B 1 94  ? -35.716 -28.533 21.102  0.50 9.53  ? 94  GLN A CA  1 
ATOM   2927 C  C   A GLN B 1 94  ? -34.583 -28.354 22.253  0.50 8.02  ? 94  GLN A C   1 
ATOM   2928 C  C   B GLN B 1 94  ? -34.710 -28.553 22.255  0.50 9.29  ? 94  GLN A C   1 
ATOM   2929 O  O   A GLN B 1 94  ? -33.527 -28.991 22.096  0.50 8.04  ? 94  GLN A O   1 
ATOM   2930 O  O   B GLN B 1 94  ? -33.685 -29.245 22.069  0.50 8.29  ? 94  GLN A O   1 
ATOM   2931 C  CB  A GLN B 1 94  ? -36.820 -29.152 21.250  0.50 8.16  ? 94  GLN A CB  1 
ATOM   2932 C  CB  B GLN B 1 94  ? -36.433 -29.918 20.999  0.50 11.57 ? 94  GLN A CB  1 
ATOM   2933 C  CG  A GLN B 1 94  ? -37.483 -29.441 22.610  0.50 10.17 ? 94  GLN A CG  1 
ATOM   2934 C  CG  B GLN B 1 94  ? -37.638 -30.126 21.724  0.50 16.64 ? 94  GLN A CG  1 
ATOM   2935 C  CD  A GLN B 1 94  ? -38.232 -30.785 22.573  0.50 10.16 ? 94  GLN A CD  1 
ATOM   2936 C  CD  B GLN B 1 94  ? -37.362 -30.889 22.906  0.50 16.50 ? 94  GLN A CD  1 
ATOM   2937 O  OE1 A GLN B 1 94  ? -37.646 -31.851 22.870  0.50 14.43 ? 94  GLN A OE1 1 
ATOM   2938 O  OE1 B GLN B 1 94  ? -38.189 -31.604 23.441  0.50 17.51 ? 94  GLN A OE1 1 
ATOM   2939 N  NE2 A GLN B 1 94  ? -39.426 -30.764 22.007  0.50 13.23 ? 94  GLN A NE2 1 
ATOM   2940 N  NE2 B GLN B 1 94  ? -36.189 -30.792 23.311  0.50 12.51 ? 94  GLN A NE2 1 
ATOM   2941 N  N   . VAL B 1 95  ? -34.988 -27.831 23.351  1.00 8.65  ? 95  VAL A N   1 
ATOM   2942 C  CA  . VAL B 1 95  ? -34.244 -28.058 24.656  1.00 8.10  ? 95  VAL A CA  1 
ATOM   2943 C  C   . VAL B 1 95  ? -35.255 -28.481 25.711  1.00 9.01  ? 95  VAL A C   1 
ATOM   2944 O  O   . VAL B 1 95  ? -36.370 -27.900 25.780  1.00 9.14  ? 95  VAL A O   1 
ATOM   2945 C  CB  . VAL B 1 95  ? -33.567 -26.705 25.087  1.00 8.92  ? 95  VAL A CB  1 
ATOM   2946 C  CG1 . VAL B 1 95  ? -32.991 -26.799 26.552  1.00 10.77 ? 95  VAL A CG1 1 
ATOM   2947 C  CG2 . VAL B 1 95  ? -32.442 -26.354 24.171  1.00 11.18 ? 95  VAL A CG2 1 
ATOM   2948 N  N   . HIS B 1 96  ? -34.888 -29.492 26.536  1.00 8.65  ? 96  HIS A N   1 
ATOM   2949 C  CA  . HIS B 1 96  ? -35.760 -29.885 27.665  1.00 7.63  ? 96  HIS A CA  1 
ATOM   2950 C  C   . HIS B 1 96  ? -34.816 -30.404 28.718  1.00 7.21  ? 96  HIS A C   1 
ATOM   2951 O  O   . HIS B 1 96  ? -33.610 -30.492 28.603  1.00 8.28  ? 96  HIS A O   1 
ATOM   2952 C  CB  . HIS B 1 96  ? -36.820 -30.900 27.215  1.00 7.52  ? 96  HIS A CB  1 
ATOM   2953 C  CG  . HIS B 1 96  ? -36.211 -32.162 26.708  1.00 7.73  ? 96  HIS A CG  1 
ATOM   2954 N  ND1 . HIS B 1 96  ? -36.072 -32.449 25.341  1.00 9.16  ? 96  HIS A ND1 1 
ATOM   2955 C  CD2 . HIS B 1 96  ? -35.717 -33.224 27.360  1.00 7.60  ? 96  HIS A CD2 1 
ATOM   2956 C  CE1 . HIS B 1 96  ? -35.471 -33.676 25.231  1.00 9.33  ? 96  HIS A CE1 1 
ATOM   2957 N  NE2 . HIS B 1 96  ? -35.222 -34.135 26.454  1.00 8.41  ? 96  HIS A NE2 1 
ATOM   2958 N  N   . LEU B 1 97  ? -35.476 -30.831 29.844  1.00 7.61  ? 97  LEU A N   1 
ATOM   2959 C  CA  . LEU B 1 97  ? -34.717 -31.215 31.053  1.00 7.97  ? 97  LEU A CA  1 
ATOM   2960 C  C   . LEU B 1 97  ? -35.371 -32.442 31.721  1.00 7.61  ? 97  LEU A C   1 
ATOM   2961 O  O   . LEU B 1 97  ? -36.592 -32.604 31.741  1.00 8.42  ? 97  LEU A O   1 
ATOM   2962 C  CB  . LEU B 1 97  ? -34.737 -30.031 32.035  1.00 8.40  ? 97  LEU A CB  1 
ATOM   2963 C  CG  . LEU B 1 97  ? -33.910 -30.186 33.366  1.00 8.61  ? 97  LEU A CG  1 
ATOM   2964 C  CD1 . LEU B 1 97  ? -32.454 -30.005 33.016  1.00 10.68 ? 97  LEU A CD1 1 
ATOM   2965 C  CD2 . LEU B 1 97  ? -34.294 -29.022 34.294  1.00 10.78 ? 97  LEU A CD2 1 
ATOM   2966 N  N   . HIS B 1 98  ? -34.484 -33.240 32.334  1.00 7.11  ? 98  HIS A N   1 
ATOM   2967 C  CA  . HIS B 1 98  ? -34.910 -34.427 33.105  1.00 7.30  ? 98  HIS A CA  1 
ATOM   2968 C  C   . HIS B 1 98  ? -34.401 -34.237 34.556  1.00 7.78  ? 98  HIS A C   1 
ATOM   2969 O  O   . HIS B 1 98  ? -33.285 -33.771 34.740  1.00 8.93  ? 98  HIS A O   1 
ATOM   2970 C  CB  . HIS B 1 98  ? -34.383 -35.686 32.577  1.00 8.25  ? 98  HIS A CB  1 
ATOM   2971 C  CG  . HIS B 1 98  ? -34.772 -35.967 31.146  1.00 8.41  ? 98  HIS A CG  1 
ATOM   2972 N  ND1 . HIS B 1 98  ? -35.902 -36.612 30.796  1.00 8.48  ? 98  HIS A ND1 1 
ATOM   2973 C  CD2 . HIS B 1 98  ? -34.118 -35.632 30.008  1.00 8.49  ? 98  HIS A CD2 1 
ATOM   2974 C  CE1 . HIS B 1 98  ? -35.982 -36.710 29.389  1.00 9.76  ? 98  HIS A CE1 1 
ATOM   2975 N  NE2 . HIS B 1 98  ? -34.867 -36.140 28.885  1.00 7.83  ? 98  HIS A NE2 1 
ATOM   2976 N  N   . TRP B 1 99  ? -35.217 -34.681 35.516  1.00 9.02  ? 99  TRP A N   1 
ATOM   2977 C  CA  . TRP B 1 99  ? -34.849 -34.565 36.970  1.00 9.67  ? 99  TRP A CA  1 
ATOM   2978 C  C   . TRP B 1 99  ? -35.506 -35.729 37.610  1.00 9.37  ? 99  TRP A C   1 
ATOM   2979 O  O   . TRP B 1 99  ? -36.265 -36.540 37.078  1.00 9.13  ? 99  TRP A O   1 
ATOM   2980 C  CB  . TRP B 1 99  ? -35.272 -33.205 37.508  1.00 10.28 ? 99  TRP A CB  1 
ATOM   2981 C  CG  . TRP B 1 99  ? -36.753 -32.985 37.371  1.00 8.82  ? 99  TRP A CG  1 
ATOM   2982 C  CD1 . TRP B 1 99  ? -37.783 -33.497 38.172  1.00 9.27  ? 99  TRP A CD1 1 
ATOM   2983 C  CD2 . TRP B 1 99  ? -37.437 -32.263 36.286  1.00 9.50  ? 99  TRP A CD2 1 
ATOM   2984 N  NE1 . TRP B 1 99  ? -39.028 -33.068 37.714  1.00 8.98  ? 99  TRP A NE1 1 
ATOM   2985 C  CE2 . TRP B 1 99  ? -38.853 -32.305 36.539  1.00 9.67  ? 99  TRP A CE2 1 
ATOM   2986 C  CE3 . TRP B 1 99  ? -37.001 -31.514 35.173  1.00 10.08 ? 99  TRP A CE3 1 
ATOM   2987 C  CZ2 . TRP B 1 99  ? -39.761 -31.690 35.754  1.00 9.95  ? 99  TRP A CZ2 1 
ATOM   2988 C  CZ3 . TRP B 1 99  ? -37.925 -30.871 34.378  1.00 9.96  ? 99  TRP A CZ3 1 
ATOM   2989 C  CH2 . TRP B 1 99  ? -39.283 -31.005 34.593  1.00 10.10 ? 99  TRP A CH2 1 
ATOM   2990 N  N   . GLY B 1 100 ? -35.182 -35.872 38.909  1.00 10.25 ? 100 GLY A N   1 
ATOM   2991 C  CA  . GLY B 1 100 ? -35.775 -36.919 39.778  1.00 11.37 ? 100 GLY A CA  1 
ATOM   2992 C  C   . GLY B 1 100 ? -36.513 -36.256 40.901  1.00 11.28 ? 100 GLY A C   1 
ATOM   2993 O  O   . GLY B 1 100 ? -36.558 -35.054 41.033  1.00 11.51 ? 100 GLY A O   1 
ATOM   2994 N  N   . SER B 1 101 ? -37.160 -37.093 41.771  1.00 13.16 ? 101 SER A N   1 
ATOM   2995 C  CA  . SER B 1 101 ? -37.977 -36.555 42.885  1.00 13.15 ? 101 SER A CA  1 
ATOM   2996 C  C   . SER B 1 101 ? -37.111 -36.064 44.023  1.00 12.00 ? 101 SER A C   1 
ATOM   2997 O  O   . SER B 1 101 ? -37.703 -35.348 44.861  1.00 15.80 ? 101 SER A O   1 
ATOM   2998 C  CB  . SER B 1 101 ? -39.011 -37.574 43.409  1.00 15.66 ? 101 SER A CB  1 
ATOM   2999 O  OG  . SER B 1 101 ? -38.301 -38.617 43.992  1.00 16.94 ? 101 SER A OG  1 
ATOM   3000 N  N   . ALA B 1 102 ? -35.863 -36.350 44.056  1.00 10.54 ? 102 ALA A N   1 
ATOM   3001 C  CA  . ALA B 1 102 ? -34.930 -35.730 45.021  1.00 10.90 ? 102 ALA A CA  1 
ATOM   3002 C  C   . ALA B 1 102 ? -33.621 -35.381 44.368  1.00 12.14 ? 102 ALA A C   1 
ATOM   3003 O  O   . ALA B 1 102 ? -33.253 -35.959 43.282  1.00 13.32 ? 102 ALA A O   1 
ATOM   3004 C  CB  . ALA B 1 102 ? -34.728 -36.695 46.177  1.00 12.84 ? 102 ALA A CB  1 
ATOM   3005 N  N   . ASP B 1 103 ? -32.862 -34.503 45.027  1.00 12.90 ? 103 ASP A N   1 
ATOM   3006 C  CA  . ASP B 1 103 ? -31.618 -33.997 44.371  1.00 12.71 ? 103 ASP A CA  1 
ATOM   3007 C  C   . ASP B 1 103 ? -30.519 -34.957 44.140  1.00 15.77 ? 103 ASP A C   1 
ATOM   3008 O  O   . ASP B 1 103 ? -29.573 -34.774 43.329  1.00 18.24 ? 103 ASP A O   1 
ATOM   3009 C  CB  . ASP B 1 103 ? -31.059 -32.826 45.186  1.00 16.11 ? 103 ASP A CB  1 
ATOM   3010 C  CG  . ASP B 1 103 ? -31.987 -31.637 45.297  1.00 14.35 ? 103 ASP A CG  1 
ATOM   3011 O  OD1 . ASP B 1 103 ? -32.897 -31.462 44.476  1.00 16.83 ? 103 ASP A OD1 1 
ATOM   3012 O  OD2 . ASP B 1 103 ? -31.756 -30.847 46.229  1.00 17.50 ? 103 ASP A OD2 1 
ATOM   3013 N  N   . ASP B 1 104 ? -30.541 -36.099 44.816  1.00 13.88 ? 104 ASP A N   1 
ATOM   3014 C  CA  . ASP B 1 104 ? -29.422 -37.026 44.740  1.00 15.88 ? 104 ASP A CA  1 
ATOM   3015 C  C   . ASP B 1 104 ? -29.348 -37.861 43.485  1.00 17.10 ? 104 ASP A C   1 
ATOM   3016 O  O   . ASP B 1 104 ? -28.287 -38.449 43.236  1.00 18.93 ? 104 ASP A O   1 
ATOM   3017 C  CB  . ASP B 1 104 ? -29.411 -38.036 45.965  1.00 17.52 ? 104 ASP A CB  1 
ATOM   3018 C  CG  . ASP B 1 104 ? -30.601 -38.870 45.982  1.00 17.37 ? 104 ASP A CG  1 
ATOM   3019 O  OD1 . ASP B 1 104 ? -31.677 -38.367 46.385  1.00 23.20 ? 104 ASP A OD1 1 
ATOM   3020 O  OD2 . ASP B 1 104 ? -30.476 -40.071 45.537  1.00 24.31 ? 104 ASP A OD2 1 
ATOM   3021 N  N   . HIS B 1 105 ? -30.413 -37.876 42.690  1.00 15.62 ? 105 HIS A N   1 
ATOM   3022 C  CA  . HIS B 1 105 ? -30.313 -38.620 41.426  1.00 16.47 ? 105 HIS A CA  1 
ATOM   3023 C  C   . HIS B 1 105 ? -31.443 -38.044 40.566  1.00 15.49 ? 105 HIS A C   1 
ATOM   3024 O  O   . HIS B 1 105 ? -32.386 -37.468 40.992  1.00 19.98 ? 105 HIS A O   1 
ATOM   3025 C  CB  . HIS B 1 105 ? -30.277 -40.139 41.552  1.00 20.23 ? 105 HIS A CB  1 
ATOM   3026 C  CG  . HIS B 1 105 ? -31.554 -40.775 42.009  1.00 24.34 ? 105 HIS A CG  1 
ATOM   3027 N  ND1 . HIS B 1 105 ? -31.867 -40.970 43.341  1.00 30.60 ? 105 HIS A ND1 1 
ATOM   3028 C  CD2 . HIS B 1 105 ? -32.550 -41.364 41.304  1.00 25.98 ? 105 HIS A CD2 1 
ATOM   3029 C  CE1 . HIS B 1 105 ? -33.024 -41.597 43.435  1.00 31.20 ? 105 HIS A CE1 1 
ATOM   3030 N  NE2 . HIS B 1 105 ? -33.460 -41.847 42.211  1.00 30.22 ? 105 HIS A NE2 1 
ATOM   3031 N  N   . GLY B 1 106 ? -31.273 -38.197 39.267  1.00 15.84 ? 106 GLY A N   1 
ATOM   3032 C  CA  . GLY B 1 106 ? -32.225 -37.614 38.354  1.00 14.91 ? 106 GLY A CA  1 
ATOM   3033 C  C   . GLY B 1 106 ? -31.654 -37.595 36.965  1.00 12.77 ? 106 GLY A C   1 
ATOM   3034 O  O   . GLY B 1 106 ? -32.400 -37.685 35.990  1.00 13.92 ? 106 GLY A O   1 
ATOM   3035 N  N   . SER B 1 107 ? -30.334 -37.488 36.850  1.00 9.86  ? 107 SER A N   1 
ATOM   3036 C  CA  . SER B 1 107 ? -29.792 -37.558 35.488  1.00 10.47 ? 107 SER A CA  1 
ATOM   3037 C  C   . SER B 1 107 ? -30.177 -38.879 34.819  1.00 11.35 ? 107 SER A C   1 
ATOM   3038 O  O   . SER B 1 107 ? -30.513 -39.903 35.442  1.00 12.54 ? 107 SER A O   1 
ATOM   3039 C  CB  . SER B 1 107 ? -28.298 -37.341 35.461  1.00 10.07 ? 107 SER A CB  1 
ATOM   3040 O  OG  . SER B 1 107 ? -27.558 -38.435 36.142  1.00 10.45 ? 107 SER A OG  1 
ATOM   3041 N  N   . GLU B 1 108 ? -30.131 -38.854 33.462  1.00 10.17 ? 108 GLU A N   1 
ATOM   3042 C  CA  . GLU B 1 108 ? -30.407 -40.077 32.655  1.00 9.53  ? 108 GLU A CA  1 
ATOM   3043 C  C   . GLU B 1 108 ? -29.170 -40.862 32.493  1.00 9.46  ? 108 GLU A C   1 
ATOM   3044 O  O   . GLU B 1 108 ? -29.111 -42.082 32.809  1.00 11.05 ? 108 GLU A O   1 
ATOM   3045 C  CB  . GLU B 1 108 ? -31.083 -39.642 31.329  1.00 9.57  ? 108 GLU A CB  1 
ATOM   3046 C  CG  . GLU B 1 108 ? -32.451 -39.064 31.638  1.00 12.22 ? 108 GLU A CG  1 
ATOM   3047 C  CD  . GLU B 1 108 ? -33.532 -39.240 30.565  1.00 10.28 ? 108 GLU A CD  1 
ATOM   3048 O  OE1 . GLU B 1 108 ? -33.113 -39.051 29.378  1.00 10.58 ? 108 GLU A OE1 1 
ATOM   3049 O  OE2 . GLU B 1 108 ? -34.623 -39.598 30.879  1.00 10.64 ? 108 GLU A OE2 1 
ATOM   3050 N  N   . HIS B 1 109 ? -28.121 -40.280 31.926  1.00 8.74  ? 109 HIS A N   1 
ATOM   3051 C  CA  . HIS B 1 109 ? -26.805 -40.951 31.873  1.00 9.80  ? 109 HIS A CA  1 
ATOM   3052 C  C   . HIS B 1 109 ? -26.184 -40.938 33.273  1.00 11.06 ? 109 HIS A C   1 
ATOM   3053 O  O   . HIS B 1 109 ? -26.422 -40.023 34.069  1.00 10.14 ? 109 HIS A O   1 
ATOM   3054 C  CB  . HIS B 1 109 ? -25.891 -40.214 30.828  1.00 9.99  ? 109 HIS A CB  1 
ATOM   3055 C  CG  . HIS B 1 109 ? -26.384 -40.378 29.415  1.00 8.60  ? 109 HIS A CG  1 
ATOM   3056 N  ND1 . HIS B 1 109 ? -27.300 -39.509 28.862  1.00 8.56  ? 109 HIS A ND1 1 
ATOM   3057 C  CD2 . HIS B 1 109 ? -26.140 -41.374 28.538  1.00 9.57  ? 109 HIS A CD2 1 
ATOM   3058 C  CE1 . HIS B 1 109 ? -27.583 -39.985 27.578  1.00 8.60  ? 109 HIS A CE1 1 
ATOM   3059 N  NE2 . HIS B 1 109 ? -26.888 -41.110 27.379  1.00 9.47  ? 109 HIS A NE2 1 
ATOM   3060 N  N   . ILE B 1 110 ? -25.393 -42.004 33.503  1.00 11.36 ? 110 ILE A N   1 
ATOM   3061 C  CA  . ILE B 1 110 ? -24.712 -42.150 34.840  1.00 11.81 ? 110 ILE A CA  1 
ATOM   3062 C  C   . ILE B 1 110 ? -23.287 -42.529 34.506  1.00 12.66 ? 110 ILE A C   1 
ATOM   3063 O  O   . ILE B 1 110 ? -23.041 -43.522 33.756  1.00 14.87 ? 110 ILE A O   1 
ATOM   3064 C  CB  . ILE B 1 110 ? -25.447 -43.256 35.656  1.00 11.83 ? 110 ILE A CB  1 
ATOM   3065 C  CG1 . ILE B 1 110 ? -26.902 -42.829 35.889  1.00 12.53 ? 110 ILE A CG1 1 
ATOM   3066 C  CG2 . ILE B 1 110 ? -24.684 -43.592 36.993  1.00 14.05 ? 110 ILE A CG2 1 
ATOM   3067 C  CD1 . ILE B 1 110 ? -27.689 -43.894 36.722  1.00 14.18 ? 110 ILE A CD1 1 
ATOM   3068 N  N   A VAL B 1 111 ? -22.360 -41.797 35.119  0.50 13.90 ? 111 VAL A N   1 
ATOM   3069 N  N   B VAL B 1 111 ? -22.320 -41.822 35.053  0.50 15.10 ? 111 VAL A N   1 
ATOM   3070 C  CA  A VAL B 1 111 ? -20.909 -41.912 34.795  0.50 14.52 ? 111 VAL A CA  1 
ATOM   3071 C  CA  B VAL B 1 111 ? -20.921 -42.098 34.635  0.50 16.08 ? 111 VAL A CA  1 
ATOM   3072 C  C   A VAL B 1 111 ? -20.113 -42.561 35.917  0.50 14.23 ? 111 VAL A C   1 
ATOM   3073 C  C   B VAL B 1 111 ? -20.158 -42.596 35.860  0.50 15.56 ? 111 VAL A C   1 
ATOM   3074 O  O   A VAL B 1 111 ? -20.048 -41.993 36.960  0.50 15.43 ? 111 VAL A O   1 
ATOM   3075 O  O   B VAL B 1 111 ? -20.182 -42.003 36.905  0.50 15.78 ? 111 VAL A O   1 
ATOM   3076 C  CB  A VAL B 1 111 ? -20.327 -40.523 34.557  0.50 12.60 ? 111 VAL A CB  1 
ATOM   3077 C  CB  B VAL B 1 111 ? -20.264 -40.828 34.201  0.50 16.21 ? 111 VAL A CB  1 
ATOM   3078 C  CG1 A VAL B 1 111 ? -18.824 -40.541 34.212  0.50 15.68 ? 111 VAL A CG1 1 
ATOM   3079 C  CG1 B VAL B 1 111 ? -20.558 -39.843 35.322  0.50 18.74 ? 111 VAL A CG1 1 
ATOM   3080 C  CG2 A VAL B 1 111 ? -21.101 -39.835 33.413  0.50 10.94 ? 111 VAL A CG2 1 
ATOM   3081 C  CG2 B VAL B 1 111 ? -18.771 -41.066 33.897  0.50 18.16 ? 111 VAL A CG2 1 
ATOM   3082 N  N   . ASP B 1 112 ? -19.631 -43.782 35.690  1.00 14.02 ? 112 ASP A N   1 
ATOM   3083 C  CA  . ASP B 1 112 ? -18.862 -44.538 36.779  1.00 16.02 ? 112 ASP A CA  1 
ATOM   3084 C  C   . ASP B 1 112 ? -19.747 -44.507 38.054  1.00 18.98 ? 112 ASP A C   1 
ATOM   3085 O  O   . ASP B 1 112 ? -19.210 -44.351 39.176  1.00 20.12 ? 112 ASP A O   1 
ATOM   3086 C  CB  . ASP B 1 112 ? -17.504 -43.927 36.962  1.00 17.96 ? 112 ASP A CB  1 
ATOM   3087 C  CG  . ASP B 1 112 ? -16.580 -44.175 35.814  1.00 17.55 ? 112 ASP A CG  1 
ATOM   3088 O  OD1 . ASP B 1 112 ? -16.667 -45.265 35.227  1.00 19.19 ? 112 ASP A OD1 1 
ATOM   3089 O  OD2 . ASP B 1 112 ? -15.703 -43.289 35.607  1.00 20.33 ? 112 ASP A OD2 1 
ATOM   3090 N  N   . GLY B 1 113 ? -21.062 -44.733 37.902  1.00 14.96 ? 113 GLY A N   1 
ATOM   3091 C  CA  . GLY B 1 113 ? -21.958 -44.894 39.009  1.00 16.05 ? 113 GLY A CA  1 
ATOM   3092 C  C   . GLY B 1 113 ? -22.396 -43.577 39.622  1.00 16.68 ? 113 GLY A C   1 
ATOM   3093 O  O   . GLY B 1 113 ? -23.229 -43.614 40.524  1.00 17.60 ? 113 GLY A O   1 
ATOM   3094 N  N   . VAL B 1 114 ? -21.916 -42.413 39.116  1.00 15.45 ? 114 VAL A N   1 
ATOM   3095 C  CA  . VAL B 1 114 ? -22.304 -41.089 39.631  1.00 16.46 ? 114 VAL A CA  1 
ATOM   3096 C  C   . VAL B 1 114 ? -23.570 -40.512 38.929  1.00 15.81 ? 114 VAL A C   1 
ATOM   3097 O  O   . VAL B 1 114 ? -23.547 -40.435 37.662  1.00 16.71 ? 114 VAL A O   1 
ATOM   3098 C  CB  . VAL B 1 114 ? -21.158 -40.066 39.493  1.00 20.46 ? 114 VAL A CB  1 
ATOM   3099 C  CG1 . VAL B 1 114 ? -21.563 -38.656 39.956  1.00 21.10 ? 114 VAL A CG1 1 
ATOM   3100 C  CG2 . VAL B 1 114 ? -19.928 -40.561 40.280  1.00 23.43 ? 114 VAL A CG2 1 
ATOM   3101 N  N   . SER B 1 115 ? -24.653 -40.255 39.661  1.00 14.91 ? 115 SER A N   1 
ATOM   3102 C  CA  . SER B 1 115 ? -25.836 -39.561 39.110  1.00 15.26 ? 115 SER A CA  1 
ATOM   3103 C  C   . SER B 1 115 ? -25.700 -38.109 39.507  1.00 20.68 ? 115 SER A C   1 
ATOM   3104 O  O   . SER B 1 115 ? -25.055 -37.685 40.484  1.00 22.95 ? 115 SER A O   1 
ATOM   3105 C  CB  . SER B 1 115 ? -27.143 -40.067 39.669  1.00 19.61 ? 115 SER A CB  1 
ATOM   3106 O  OG  . SER B 1 115 ? -27.435 -41.349 39.215  1.00 19.59 ? 115 SER A OG  1 
ATOM   3107 N  N   . TYR B 1 116 ? -26.260 -37.325 38.640  1.00 15.10 ? 116 TYR A N   1 
ATOM   3108 C  CA  . TYR B 1 116 ? -26.350 -35.848 38.887  1.00 13.41 ? 116 TYR A CA  1 
ATOM   3109 C  C   . TYR B 1 116 ? -27.784 -35.526 39.178  1.00 11.77 ? 116 TYR A C   1 
ATOM   3110 O  O   . TYR B 1 116 ? -28.671 -36.415 39.107  1.00 11.82 ? 116 TYR A O   1 
ATOM   3111 C  CB  . TYR B 1 116 ? -25.843 -35.148 37.628  1.00 13.90 ? 116 TYR A CB  1 
ATOM   3112 C  CG  . TYR B 1 116 ? -24.341 -35.296 37.459  1.00 13.02 ? 116 TYR A CG  1 
ATOM   3113 C  CD1 . TYR B 1 116 ? -23.445 -34.466 38.202  1.00 14.25 ? 116 TYR A CD1 1 
ATOM   3114 C  CD2 . TYR B 1 116 ? -23.827 -36.270 36.616  1.00 14.33 ? 116 TYR A CD2 1 
ATOM   3115 C  CE1 . TYR B 1 116 ? -22.071 -34.667 37.992  1.00 17.50 ? 116 TYR A CE1 1 
ATOM   3116 C  CE2 . TYR B 1 116 ? -22.495 -36.487 36.423  1.00 18.13 ? 116 TYR A CE2 1 
ATOM   3117 C  CZ  . TYR B 1 116 ? -21.641 -35.663 37.118  1.00 20.42 ? 116 TYR A CZ  1 
ATOM   3118 O  OH  . TYR B 1 116 ? -20.326 -36.066 36.885  1.00 27.69 ? 116 TYR A OH  1 
ATOM   3119 N  N   . ALA B 1 117 ? -28.132 -34.348 39.642  1.00 10.78 ? 117 ALA A N   1 
ATOM   3120 C  CA  . ALA B 1 117 ? -29.473 -33.998 39.968  1.00 11.13 ? 117 ALA A CA  1 
ATOM   3121 C  C   . ALA B 1 117 ? -30.401 -33.933 38.766  1.00 10.65 ? 117 ALA A C   1 
ATOM   3122 O  O   . ALA B 1 117 ? -31.561 -34.103 38.901  1.00 11.53 ? 117 ALA A O   1 
ATOM   3123 C  CB  . ALA B 1 117 ? -29.466 -32.636 40.728  1.00 11.42 ? 117 ALA A CB  1 
ATOM   3124 N  N   . ALA B 1 118 ? -29.847 -33.540 37.630  1.00 10.59 ? 118 ALA A N   1 
ATOM   3125 C  CA  . ALA B 1 118 ? -30.748 -33.321 36.404  1.00 9.36  ? 118 ALA A CA  1 
ATOM   3126 C  C   . ALA B 1 118 ? -29.808 -33.421 35.201  1.00 8.75  ? 118 ALA A C   1 
ATOM   3127 O  O   . ALA B 1 118 ? -28.607 -33.487 35.266  1.00 8.94  ? 118 ALA A O   1 
ATOM   3128 C  CB  . ALA B 1 118 ? -31.420 -31.995 36.520  1.00 9.62  ? 118 ALA A CB  1 
ATOM   3129 N  N   . GLU B 1 119 ? -30.507 -33.415 34.047  1.00 7.85  ? 119 GLU A N   1 
ATOM   3130 C  CA  . GLU B 1 119 ? -29.756 -33.536 32.749  1.00 8.40  ? 119 GLU A CA  1 
ATOM   3131 C  C   . GLU B 1 119 ? -30.553 -32.717 31.693  1.00 7.27  ? 119 GLU A C   1 
ATOM   3132 O  O   . GLU B 1 119 ? -31.727 -33.032 31.460  1.00 8.34  ? 119 GLU A O   1 
ATOM   3133 C  CB  . GLU B 1 119 ? -29.582 -35.035 32.390  1.00 9.42  ? 119 GLU A CB  1 
ATOM   3134 C  CG  . GLU B 1 119 ? -28.742 -35.226 31.129  1.00 8.99  ? 119 GLU A CG  1 
ATOM   3135 C  CD  . GLU B 1 119 ? -28.449 -36.671 30.853  1.00 10.17 ? 119 GLU A CD  1 
ATOM   3136 O  OE1 . GLU B 1 119 ? -28.250 -37.449 31.851  1.00 9.45  ? 119 GLU A OE1 1 
ATOM   3137 O  OE2 . GLU B 1 119 ? -28.346 -37.108 29.690  1.00 9.51  ? 119 GLU A OE2 1 
ATOM   3138 N  N   . LEU B 1 120 ? -29.851 -31.779 31.049  1.00 7.80  ? 120 LEU A N   1 
ATOM   3139 C  CA  . LEU B 1 120 ? -30.434 -30.990 29.930  1.00 8.01  ? 120 LEU A CA  1 
ATOM   3140 C  C   . LEU B 1 120 ? -30.099 -31.705 28.628  1.00 7.62  ? 120 LEU A C   1 
ATOM   3141 O  O   . LEU B 1 120 ? -28.981 -32.175 28.425  1.00 7.78  ? 120 LEU A O   1 
ATOM   3142 C  CB  . LEU B 1 120 ? -29.719 -29.642 29.992  1.00 10.40 ? 120 LEU A CB  1 
ATOM   3143 C  CG  . LEU B 1 120 ? -30.359 -28.560 29.069  1.00 10.11 ? 120 LEU A CG  1 
ATOM   3144 C  CD1 . LEU B 1 120 ? -31.568 -27.931 29.710  1.00 11.31 ? 120 LEU A CD1 1 
ATOM   3145 C  CD2 . LEU B 1 120 ? -29.275 -27.525 28.798  1.00 13.12 ? 120 LEU A CD2 1 
ATOM   3146 N  N   . HIS B 1 121 ? -31.120 -31.735 27.773  1.00 7.89  ? 121 HIS A N   1 
ATOM   3147 C  CA  . HIS B 1 121 ? -30.955 -32.256 26.406  1.00 7.13  ? 121 HIS A CA  1 
ATOM   3148 C  C   . HIS B 1 121 ? -31.212 -31.219 25.343  1.00 7.57  ? 121 HIS A C   1 
ATOM   3149 O  O   . HIS B 1 121 ? -32.214 -30.509 25.430  1.00 8.21  ? 121 HIS A O   1 
ATOM   3150 C  CB  . HIS B 1 121 ? -31.910 -33.432 26.184  1.00 7.14  ? 121 HIS A CB  1 
ATOM   3151 C  CG  . HIS B 1 121 ? -31.500 -34.669 26.973  1.00 7.57  ? 121 HIS A CG  1 
ATOM   3152 N  ND1 . HIS B 1 121 ? -32.360 -35.707 27.278  1.00 9.34  ? 121 HIS A ND1 1 
ATOM   3153 C  CD2 . HIS B 1 121 ? -30.295 -34.981 27.531  1.00 8.53  ? 121 HIS A CD2 1 
ATOM   3154 C  CE1 . HIS B 1 121 ? -31.705 -36.648 27.996  1.00 8.62  ? 121 HIS A CE1 1 
ATOM   3155 N  NE2 . HIS B 1 121 ? -30.440 -36.237 28.147  1.00 7.43  ? 121 HIS A NE2 1 
ATOM   3156 N  N   . VAL B 1 122 ? -30.275 -31.158 24.414  1.00 8.56  ? 122 VAL A N   1 
ATOM   3157 C  CA  . VAL B 1 122 ? -30.349 -30.167 23.302  1.00 7.42  ? 122 VAL A CA  1 
ATOM   3158 C  C   . VAL B 1 122 ? -30.450 -31.000 22.034  1.00 7.04  ? 122 VAL A C   1 
ATOM   3159 O  O   . VAL B 1 122 ? -29.499 -31.671 21.635  1.00 7.29  ? 122 VAL A O   1 
ATOM   3160 C  CB  . VAL B 1 122 ? -29.128 -29.265 23.325  1.00 7.72  ? 122 VAL A CB  1 
ATOM   3161 C  CG1 . VAL B 1 122 ? -29.384 -28.119 22.307  1.00 7.78  ? 122 VAL A CG1 1 
ATOM   3162 C  CG2 . VAL B 1 122 ? -28.889 -28.617 24.736  1.00 9.68  ? 122 VAL A CG2 1 
ATOM   3163 N  N   . VAL B 1 123 ? -31.658 -30.993 21.454  1.00 7.68  ? 123 VAL A N   1 
ATOM   3164 C  CA  . VAL B 1 123 ? -32.020 -31.907 20.346  1.00 7.31  ? 123 VAL A CA  1 
ATOM   3165 C  C   . VAL B 1 123 ? -31.830 -31.211 18.989  1.00 7.32  ? 123 VAL A C   1 
ATOM   3166 O  O   . VAL B 1 123 ? -32.358 -30.081 18.807  1.00 7.49  ? 123 VAL A O   1 
ATOM   3167 C  CB  . VAL B 1 123 ? -33.482 -32.356 20.487  1.00 7.92  ? 123 VAL A CB  1 
ATOM   3168 C  CG1 . VAL B 1 123 ? -33.901 -33.325 19.386  1.00 9.82  ? 123 VAL A CG1 1 
ATOM   3169 C  CG2 . VAL B 1 123 ? -33.698 -33.060 21.854  1.00 9.33  ? 123 VAL A CG2 1 
ATOM   3170 N  N   . HIS B 1 124 ? -31.104 -31.886 18.098  1.00 7.47  ? 124 HIS A N   1 
ATOM   3171 C  CA  . HIS B 1 124 ? -30.837 -31.346 16.772  1.00 7.47  ? 124 HIS A CA  1 
ATOM   3172 C  C   . HIS B 1 124 ? -31.178 -32.438 15.796  1.00 8.10  ? 124 HIS A C   1 
ATOM   3173 O  O   . HIS B 1 124 ? -31.131 -33.621 16.050  1.00 8.35  ? 124 HIS A O   1 
ATOM   3174 C  CB  . HIS B 1 124 ? -29.323 -31.059 16.585  1.00 8.43  ? 124 HIS A CB  1 
ATOM   3175 C  CG  . HIS B 1 124 ? -28.705 -30.171 17.627  1.00 8.70  ? 124 HIS A CG  1 
ATOM   3176 N  ND1 . HIS B 1 124 ? -28.486 -30.698 18.933  1.00 8.44  ? 124 HIS A ND1 1 
ATOM   3177 C  CD2 . HIS B 1 124 ? -28.288 -28.878 17.643  1.00 9.41  ? 124 HIS A CD2 1 
ATOM   3178 C  CE1 . HIS B 1 124 ? -27.947 -29.727 19.692  1.00 8.24  ? 124 HIS A CE1 1 
ATOM   3179 N  NE2 . HIS B 1 124 ? -27.782 -28.588 18.935  1.00 9.02  ? 124 HIS A NE2 1 
ATOM   3180 N  N   . TRP B 1 125 ? -31.377 -32.034 14.505  1.00 8.57  ? 125 TRP A N   1 
ATOM   3181 C  CA  . TRP B 1 125 ? -31.691 -33.032 13.468  1.00 8.72  ? 125 TRP A CA  1 
ATOM   3182 C  C   . TRP B 1 125 ? -30.994 -32.722 12.111  1.00 8.61  ? 125 TRP A C   1 
ATOM   3183 O  O   . TRP B 1 125 ? -30.697 -31.581 11.776  1.00 8.72  ? 125 TRP A O   1 
ATOM   3184 C  CB  . TRP B 1 125 ? -33.221 -33.162 13.197  1.00 9.38  ? 125 TRP A CB  1 
ATOM   3185 C  CG  . TRP B 1 125 ? -33.888 -31.873 12.769  1.00 9.82  ? 125 TRP A CG  1 
ATOM   3186 C  CD1 . TRP B 1 125 ? -34.220 -30.810 13.584  1.00 11.21 ? 125 TRP A CD1 1 
ATOM   3187 C  CD2 . TRP B 1 125 ? -34.298 -31.520 11.414  1.00 10.50 ? 125 TRP A CD2 1 
ATOM   3188 N  NE1 . TRP B 1 125 ? -34.857 -29.806 12.803  1.00 10.94 ? 125 TRP A NE1 1 
ATOM   3189 C  CE2 . TRP B 1 125 ? -34.905 -30.215 11.500  1.00 10.01 ? 125 TRP A CE2 1 
ATOM   3190 C  CE3 . TRP B 1 125 ? -34.252 -32.219 10.166  1.00 11.97 ? 125 TRP A CE3 1 
ATOM   3191 C  CZ2 . TRP B 1 125 ? -35.490 -29.600 10.407  1.00 11.82 ? 125 TRP A CZ2 1 
ATOM   3192 C  CZ3 . TRP B 1 125 ? -34.776 -31.501 9.047   1.00 13.04 ? 125 TRP A CZ3 1 
ATOM   3193 C  CH2 . TRP B 1 125 ? -35.374 -30.252 9.167   1.00 14.29 ? 125 TRP A CH2 1 
ATOM   3194 N  N   . ASN B 1 126 ? -30.789 -33.805 11.344  1.00 9.04  ? 126 ASN A N   1 
ATOM   3195 C  CA  . ASN B 1 126 ? -29.962 -33.695 10.140  1.00 9.23  ? 126 ASN A CA  1 
ATOM   3196 C  C   . ASN B 1 126 ? -30.784 -33.150 8.926   1.00 9.93  ? 126 ASN A C   1 
ATOM   3197 O  O   . ASN B 1 126 ? -31.440 -33.896 8.243   1.00 9.72  ? 126 ASN A O   1 
ATOM   3198 C  CB  . ASN B 1 126 ? -29.465 -35.115 9.837   1.00 10.47 ? 126 ASN A CB  1 
ATOM   3199 C  CG  . ASN B 1 126 ? -28.492 -35.137 8.713   1.00 14.02 ? 126 ASN A CG  1 
ATOM   3200 O  OD1 . ASN B 1 126 ? -28.426 -34.194 7.884   1.00 11.52 ? 126 ASN A OD1 1 
ATOM   3201 N  ND2 . ASN B 1 126 ? -27.750 -36.213 8.642   1.00 14.15 ? 126 ASN A ND2 1 
ATOM   3202 N  N   . SER B 1 127 ? -30.701 -31.860 8.781   1.00 9.31  ? 127 SER A N   1 
ATOM   3203 C  CA  . SER B 1 127 ? -31.457 -31.131 7.692   1.00 10.16 ? 127 SER A CA  1 
ATOM   3204 C  C   . SER B 1 127 ? -30.604 -31.213 6.435   1.00 12.03 ? 127 SER A C   1 
ATOM   3205 O  O   . SER B 1 127 ? -31.177 -30.790 5.400   1.00 12.57 ? 127 SER A O   1 
ATOM   3206 C  CB  . SER B 1 127 ? -31.714 -29.725 8.176   1.00 11.41 ? 127 SER A CB  1 
ATOM   3207 O  OG  . SER B 1 127 ? -30.542 -29.007 8.483   1.00 12.19 ? 127 SER A OG  1 
ATOM   3208 N  N   . ASP B 1 128 ? -29.390 -31.724 6.441   1.00 10.87 ? 128 ASP A N   1 
ATOM   3209 C  CA  . ASP B 1 128 ? -28.640 -31.870 5.165   1.00 11.16 ? 128 ASP A CA  1 
ATOM   3210 C  C   . ASP B 1 128 ? -29.226 -33.078 4.484   1.00 12.26 ? 128 ASP A C   1 
ATOM   3211 O  O   . ASP B 1 128 ? -29.045 -33.155 3.239   1.00 14.42 ? 128 ASP A O   1 
ATOM   3212 C  CB  . ASP B 1 128 ? -27.165 -32.098 5.439   1.00 13.14 ? 128 ASP A CB  1 
ATOM   3213 C  CG  . ASP B 1 128 ? -26.409 -30.808 5.734   1.00 13.48 ? 128 ASP A CG  1 
ATOM   3214 O  OD1 . ASP B 1 128 ? -25.211 -30.896 6.078   1.00 14.07 ? 128 ASP A OD1 1 
ATOM   3215 O  OD2 . ASP B 1 128 ? -27.001 -29.712 5.623   1.00 14.93 ? 128 ASP A OD2 1 
ATOM   3216 N  N   . LYS B 1 129 ? -29.910 -33.987 5.129   1.00 11.90 ? 129 LYS A N   1 
ATOM   3217 C  CA  . LYS B 1 129 ? -30.429 -35.233 4.510   1.00 10.95 ? 129 LYS A CA  1 
ATOM   3218 C  C   . LYS B 1 129 ? -31.896 -35.367 4.536   1.00 12.49 ? 129 LYS A C   1 
ATOM   3219 O  O   . LYS B 1 129 ? -32.499 -36.066 3.708   1.00 12.69 ? 129 LYS A O   1 
ATOM   3220 C  CB  . LYS B 1 129 ? -29.783 -36.514 5.117   1.00 13.70 ? 129 LYS A CB  1 
ATOM   3221 C  CG  . LYS B 1 129 ? -28.333 -36.670 4.780   1.00 18.08 ? 129 LYS A CG  1 
ATOM   3222 C  CD  . LYS B 1 129 ? -27.706 -37.975 5.334   1.00 17.97 ? 129 LYS A CD  1 
ATOM   3223 C  CE  . LYS B 1 129 ? -28.458 -39.165 4.769   1.00 19.44 ? 129 LYS A CE  1 
ATOM   3224 N  NZ  . LYS B 1 129 ? -27.784 -40.480 5.138   1.00 19.23 ? 129 LYS A NZ  1 
ATOM   3225 N  N   . TYR B 1 130 ? -32.578 -34.864 5.571   1.00 12.03 ? 130 TYR A N   1 
ATOM   3226 C  CA  . TYR B 1 130 ? -33.958 -35.198 5.804   1.00 12.52 ? 130 TYR A CA  1 
ATOM   3227 C  C   . TYR B 1 130 ? -34.832 -33.950 5.741   1.00 10.91 ? 130 TYR A C   1 
ATOM   3228 O  O   . TYR B 1 130 ? -34.318 -32.902 6.060   1.00 12.49 ? 130 TYR A O   1 
ATOM   3229 C  CB  . TYR B 1 130 ? -34.092 -35.989 7.230   1.00 11.81 ? 130 TYR A CB  1 
ATOM   3230 C  CG  . TYR B 1 130 ? -33.216 -37.207 7.171   1.00 13.44 ? 130 TYR A CG  1 
ATOM   3231 C  CD1 . TYR B 1 130 ? -33.419 -38.188 6.191   1.00 13.97 ? 130 TYR A CD1 1 
ATOM   3232 C  CD2 . TYR B 1 130 ? -32.138 -37.387 8.039   1.00 12.62 ? 130 TYR A CD2 1 
ATOM   3233 C  CE1 . TYR B 1 130 ? -32.582 -39.325 6.068   1.00 16.33 ? 130 TYR A CE1 1 
ATOM   3234 C  CE2 . TYR B 1 130 ? -31.296 -38.505 7.985   1.00 12.53 ? 130 TYR A CE2 1 
ATOM   3235 C  CZ  . TYR B 1 130 ? -31.551 -39.465 6.996   1.00 13.16 ? 130 TYR A CZ  1 
ATOM   3236 O  OH  . TYR B 1 130 ? -30.709 -40.550 6.908   1.00 17.08 ? 130 TYR A OH  1 
ATOM   3237 N  N   . PRO B 1 131 ? -36.099 -34.122 5.424   1.00 12.95 ? 131 PRO A N   1 
ATOM   3238 C  CA  . PRO B 1 131 ? -36.955 -32.966 5.172   1.00 12.96 ? 131 PRO A CA  1 
ATOM   3239 C  C   . PRO B 1 131 ? -37.531 -32.338 6.381   1.00 14.03 ? 131 PRO A C   1 
ATOM   3240 O  O   . PRO B 1 131 ? -38.056 -31.186 6.321   1.00 15.10 ? 131 PRO A O   1 
ATOM   3241 C  CB  . PRO B 1 131 ? -38.076 -33.505 4.285   1.00 14.66 ? 131 PRO A CB  1 
ATOM   3242 C  CG  . PRO B 1 131 ? -38.195 -34.961 4.749   1.00 15.25 ? 131 PRO A CG  1 
ATOM   3243 C  CD  . PRO B 1 131 ? -36.708 -35.377 4.974   1.00 13.34 ? 131 PRO A CD  1 
ATOM   3244 N  N   . SER B 1 132 ? -37.547 -33.048 7.545   1.00 11.73 ? 132 SER A N   1 
ATOM   3245 C  CA  . SER B 1 132 ? -38.178 -32.494 8.715   1.00 13.74 ? 132 SER A CA  1 
ATOM   3246 C  C   . SER B 1 132 ? -37.589 -33.289 9.893   1.00 12.50 ? 132 SER A C   1 
ATOM   3247 O  O   . SER B 1 132 ? -37.048 -34.387 9.751   1.00 12.88 ? 132 SER A O   1 
ATOM   3248 C  CB  . SER B 1 132 ? -39.685 -32.831 8.738   1.00 15.38 ? 132 SER A CB  1 
ATOM   3249 O  OG  . SER B 1 132 ? -39.891 -34.195 8.714   1.00 16.90 ? 132 SER A OG  1 
ATOM   3250 N  N   . PHE B 1 133 ? -37.806 -32.675 11.055  1.00 14.36 ? 133 PHE A N   1 
ATOM   3251 C  CA  . PHE B 1 133 ? -37.411 -33.349 12.304  1.00 13.70 ? 133 PHE A CA  1 
ATOM   3252 C  C   . PHE B 1 133 ? -38.097 -34.698 12.423  1.00 14.20 ? 133 PHE A C   1 
ATOM   3253 O  O   . PHE B 1 133 ? -37.526 -35.729 12.756  1.00 13.93 ? 133 PHE A O   1 
ATOM   3254 C  CB  . PHE B 1 133 ? -37.745 -32.444 13.510  1.00 15.59 ? 133 PHE A CB  1 
ATOM   3255 C  CG  . PHE B 1 133 ? -37.621 -33.190 14.795  1.00 17.19 ? 133 PHE A CG  1 
ATOM   3256 C  CD1 . PHE B 1 133 ? -36.395 -33.301 15.420  1.00 17.29 ? 133 PHE A CD1 1 
ATOM   3257 C  CD2 . PHE B 1 133 ? -38.705 -33.928 15.297  1.00 18.54 ? 133 PHE A CD2 1 
ATOM   3258 C  CE1 . PHE B 1 133 ? -36.294 -34.070 16.603  1.00 18.77 ? 133 PHE A CE1 1 
ATOM   3259 C  CE2 . PHE B 1 133 ? -38.615 -34.729 16.491  1.00 19.11 ? 133 PHE A CE2 1 
ATOM   3260 C  CZ  . PHE B 1 133 ? -37.352 -34.810 17.058  1.00 20.80 ? 133 PHE A CZ  1 
ATOM   3261 N  N   . VAL B 1 134 ? -39.399 -34.730 12.130  1.00 16.69 ? 134 VAL A N   1 
ATOM   3262 C  CA  . VAL B 1 134 ? -40.112 -35.893 12.323  1.00 17.97 ? 134 VAL A CA  1 
ATOM   3263 C  C   . VAL B 1 134 ? -39.638 -37.054 11.448  1.00 17.04 ? 134 VAL A C   1 
ATOM   3264 O  O   . VAL B 1 134 ? -39.488 -38.213 11.835  1.00 20.76 ? 134 VAL A O   1 
ATOM   3265 C  CB  . VAL B 1 134 ? -41.644 -35.586 12.067  1.00 23.54 ? 134 VAL A CB  1 
ATOM   3266 C  CG1 . VAL B 1 134 ? -42.367 -36.865 11.723  1.00 28.66 ? 134 VAL A CG1 1 
ATOM   3267 C  CG2 . VAL B 1 134 ? -42.250 -34.807 13.231  1.00 26.48 ? 134 VAL A CG2 1 
ATOM   3268 N  N   A GLU B 1 135 ? -39.279 -36.677 10.209  0.50 15.80 ? 135 GLU A N   1 
ATOM   3269 N  N   B GLU B 1 135 ? -39.205 -36.775 10.223  0.50 14.05 ? 135 GLU A N   1 
ATOM   3270 C  CA  A GLU B 1 135 ? -38.691 -37.682 9.365   0.50 15.01 ? 135 GLU A CA  1 
ATOM   3271 C  CA  B GLU B 1 135 ? -38.623 -37.828 9.412   0.50 12.64 ? 135 GLU A CA  1 
ATOM   3272 C  C   A GLU B 1 135 ? -37.342 -38.163 9.887   0.50 14.48 ? 135 GLU A C   1 
ATOM   3273 C  C   B GLU B 1 135 ? -37.122 -38.290 9.767   0.50 12.39 ? 135 GLU A C   1 
ATOM   3274 O  O   A GLU B 1 135 ? -37.242 -39.277 10.061  0.50 12.36 ? 135 GLU A O   1 
ATOM   3275 O  O   B GLU B 1 135 ? -36.641 -39.485 9.659   0.50 12.31 ? 135 GLU A O   1 
ATOM   3276 C  CB  A GLU B 1 135 ? -38.556 -37.257 7.858   0.50 18.95 ? 135 GLU A CB  1 
ATOM   3277 C  CB  B GLU B 1 135 ? -38.735 -37.261 7.976   0.50 14.27 ? 135 GLU A CB  1 
ATOM   3278 C  CG  A GLU B 1 135 ? -39.805 -37.371 6.986   0.50 19.50 ? 135 GLU A CG  1 
ATOM   3279 C  CG  B GLU B 1 135 ? -38.606 -38.337 6.972   0.50 13.69 ? 135 GLU A CG  1 
ATOM   3280 C  CD  A GLU B 1 135 ? -40.176 -38.767 6.512   0.50 21.52 ? 135 GLU A CD  1 
ATOM   3281 C  CD  B GLU B 1 135 ? -37.286 -39.093 7.015   0.50 11.80 ? 135 GLU A CD  1 
ATOM   3282 O  OE1 A GLU B 1 135 ? -41.306 -38.893 5.895   0.50 22.32 ? 135 GLU A OE1 1 
ATOM   3283 O  OE1 B GLU B 1 135 ? -36.282 -38.349 7.147   0.50 12.27 ? 135 GLU A OE1 1 
ATOM   3284 O  OE2 A GLU B 1 135 ? -39.361 -39.724 6.694   0.50 21.57 ? 135 GLU A OE2 1 
ATOM   3285 O  OE2 B GLU B 1 135 ? -37.227 -40.407 6.875   0.50 12.67 ? 135 GLU A OE2 1 
ATOM   3286 N  N   . ALA B 1 136 ? -36.412 -37.262 10.242  1.00 12.90 ? 136 ALA A N   1 
ATOM   3287 C  CA  . ALA B 1 136 ? -35.060 -37.522 10.726  1.00 11.77 ? 136 ALA A CA  1 
ATOM   3288 C  C   . ALA B 1 136 ? -35.079 -38.415 12.026  1.00 11.59 ? 136 ALA A C   1 
ATOM   3289 O  O   . ALA B 1 136 ? -34.169 -39.235 12.150  1.00 11.65 ? 136 ALA A O   1 
ATOM   3290 C  CB  . ALA B 1 136 ? -34.387 -36.194 11.027  1.00 12.63 ? 136 ALA A CB  1 
ATOM   3291 N  N   . ALA B 1 137 ? -36.116 -38.290 12.804  1.00 13.28 ? 137 ALA A N   1 
ATOM   3292 C  CA  . ALA B 1 137 ? -36.184 -39.111 14.023  1.00 12.45 ? 137 ALA A CA  1 
ATOM   3293 C  C   . ALA B 1 137 ? -36.341 -40.567 13.731  1.00 13.69 ? 137 ALA A C   1 
ATOM   3294 O  O   . ALA B 1 137 ? -36.142 -41.378 14.685  1.00 13.68 ? 137 ALA A O   1 
ATOM   3295 C  CB  . ALA B 1 137 ? -37.347 -38.659 14.802  1.00 13.10 ? 137 ALA A CB  1 
ATOM   3296 N  N   . HIS B 1 138 ? -36.578 -41.017 12.472  1.00 14.35 ? 138 HIS A N   1 
ATOM   3297 C  CA  . HIS B 1 138 ? -36.731 -42.412 12.141  1.00 15.71 ? 138 HIS A CA  1 
ATOM   3298 C  C   . HIS B 1 138 ? -35.539 -42.863 11.354  1.00 16.25 ? 138 HIS A C   1 
ATOM   3299 O  O   . HIS B 1 138 ? -35.628 -43.924 10.697  1.00 21.15 ? 138 HIS A O   1 
ATOM   3300 C  CB  . HIS B 1 138 ? -38.012 -42.570 11.288  1.00 16.96 ? 138 HIS A CB  1 
ATOM   3301 C  CG  . HIS B 1 138 ? -39.255 -42.336 12.089  1.00 17.35 ? 138 HIS A CG  1 
ATOM   3302 N  ND1 . HIS B 1 138 ? -39.979 -43.382 12.706  1.00 21.61 ? 138 HIS A ND1 1 
ATOM   3303 C  CD2 . HIS B 1 138 ? -39.903 -41.171 12.393  1.00 20.70 ? 138 HIS A CD2 1 
ATOM   3304 C  CE1 . HIS B 1 138 ? -41.002 -42.862 13.344  1.00 20.89 ? 138 HIS A CE1 1 
ATOM   3305 N  NE2 . HIS B 1 138 ? -40.997 -41.530 13.173  1.00 22.86 ? 138 HIS A NE2 1 
ATOM   3306 N  N   . GLU B 1 139 ? -34.402 -42.131 11.393  1.00 14.66 ? 139 GLU A N   1 
ATOM   3307 C  CA  . GLU B 1 139 ? -33.233 -42.552 10.624  1.00 16.97 ? 139 GLU A CA  1 
ATOM   3308 C  C   . GLU B 1 139 ? -31.997 -42.703 11.530  1.00 15.48 ? 139 GLU A C   1 
ATOM   3309 O  O   . GLU B 1 139 ? -31.842 -41.868 12.455  1.00 13.37 ? 139 GLU A O   1 
ATOM   3310 C  CB  . GLU B 1 139 ? -32.933 -41.403 9.593   1.00 19.64 ? 139 GLU A CB  1 
ATOM   3311 C  CG  . GLU B 1 139 ? -34.056 -40.962 8.608   1.00 21.91 ? 139 GLU A CG  1 
ATOM   3312 C  CD  . GLU B 1 139 ? -34.245 -41.925 7.502   1.00 26.39 ? 139 GLU A CD  1 
ATOM   3313 O  OE1 . GLU B 1 139 ? -33.458 -42.887 7.469   1.00 27.33 ? 139 GLU A OE1 1 
ATOM   3314 O  OE2 . GLU B 1 139 ? -35.172 -41.618 6.625   1.00 25.41 ? 139 GLU A OE2 1 
ATOM   3315 N  N   . PRO B 1 140 ? -31.114 -43.652 11.343  1.00 15.60 ? 140 PRO A N   1 
ATOM   3316 C  CA  . PRO B 1 140 ? -30.007 -43.781 12.308  1.00 14.83 ? 140 PRO A CA  1 
ATOM   3317 C  C   . PRO B 1 140 ? -29.142 -42.578 12.482  1.00 14.51 ? 140 PRO A C   1 
ATOM   3318 O  O   . PRO B 1 140 ? -28.566 -42.367 13.603  1.00 13.97 ? 140 PRO A O   1 
ATOM   3319 C  CB  . PRO B 1 140 ? -29.146 -45.019 11.801  1.00 17.17 ? 140 PRO A CB  1 
ATOM   3320 C  CG  . PRO B 1 140 ? -30.208 -45.850 11.194  1.00 24.19 ? 140 PRO A CG  1 
ATOM   3321 C  CD  . PRO B 1 140 ? -31.096 -44.832 10.435  1.00 20.62 ? 140 PRO A CD  1 
ATOM   3322 N  N   . ASP B 1 141 ? -28.876 -41.845 11.404  1.00 11.35 ? 141 ASP A N   1 
ATOM   3323 C  CA  . ASP B 1 141 ? -28.045 -40.655 11.445  1.00 12.49 ? 141 ASP A CA  1 
ATOM   3324 C  C   . ASP B 1 141 ? -28.996 -39.414 11.546  1.00 9.90  ? 141 ASP A C   1 
ATOM   3325 O  O   . ASP B 1 141 ? -28.506 -38.296 11.205  1.00 10.83 ? 141 ASP A O   1 
ATOM   3326 C  CB  . ASP B 1 141 ? -27.163 -40.588 10.186  1.00 13.40 ? 141 ASP A CB  1 
ATOM   3327 C  CG  . ASP B 1 141 ? -27.964 -40.533 8.927   1.00 12.82 ? 141 ASP A CG  1 
ATOM   3328 O  OD1 . ASP B 1 141 ? -29.113 -40.863 8.917   1.00 13.07 ? 141 ASP A OD1 1 
ATOM   3329 O  OD2 . ASP B 1 141 ? -27.361 -40.166 7.864   1.00 16.49 ? 141 ASP A OD2 1 
ATOM   3330 N  N   . GLY B 1 142 ? -30.235 -39.590 11.985  1.00 10.95 ? 142 GLY A N   1 
ATOM   3331 C  CA  . GLY B 1 142 ? -31.150 -38.471 11.895  1.00 10.84 ? 142 GLY A CA  1 
ATOM   3332 C  C   . GLY B 1 142 ? -30.956 -37.361 12.949  1.00 9.25  ? 142 GLY A C   1 
ATOM   3333 O  O   . GLY B 1 142 ? -31.171 -36.195 12.693  1.00 9.59  ? 142 GLY A O   1 
ATOM   3334 N  N   . LEU B 1 143 ? -30.681 -37.779 14.228  1.00 8.93  ? 143 LEU A N   1 
ATOM   3335 C  CA  . LEU B 1 143 ? -30.761 -36.870 15.395  1.00 9.47  ? 143 LEU A CA  1 
ATOM   3336 C  C   . LEU B 1 143 ? -29.384 -36.782 16.060  1.00 8.70  ? 143 LEU A C   1 
ATOM   3337 O  O   . LEU B 1 143 ? -28.590 -37.737 16.052  1.00 9.93  ? 143 LEU A O   1 
ATOM   3338 C  CB  . LEU B 1 143 ? -31.780 -37.251 16.441  1.00 9.66  ? 143 LEU A CB  1 
ATOM   3339 C  CG  . LEU B 1 143 ? -33.196 -37.393 15.911  1.00 9.68  ? 143 LEU A CG  1 
ATOM   3340 C  CD1 . LEU B 1 143 ? -34.149 -37.797 17.040  1.00 10.27 ? 143 LEU A CD1 1 
ATOM   3341 C  CD2 . LEU B 1 143 ? -33.730 -36.124 15.106  1.00 11.60 ? 143 LEU A CD2 1 
ATOM   3342 N  N   . ALA B 1 144 ? -29.108 -35.665 16.675  1.00 8.95  ? 144 ALA A N   1 
ATOM   3343 C  CA  . ALA B 1 144 ? -27.883 -35.467 17.522  1.00 9.59  ? 144 ALA A CA  1 
ATOM   3344 C  C   . ALA B 1 144 ? -28.298 -34.765 18.746  1.00 8.70  ? 144 ALA A C   1 
ATOM   3345 O  O   . ALA B 1 144 ? -28.946 -33.707 18.671  1.00 9.94  ? 144 ALA A O   1 
ATOM   3346 C  CB  . ALA B 1 144 ? -26.802 -34.684 16.809  1.00 10.04 ? 144 ALA A CB  1 
ATOM   3347 N  N   . VAL B 1 145 ? -27.995 -35.319 19.934  1.00 9.04  ? 145 VAL A N   1 
ATOM   3348 C  CA  . VAL B 1 145 ? -28.469 -34.707 21.233  1.00 9.17  ? 145 VAL A CA  1 
ATOM   3349 C  C   . VAL B 1 145 ? -27.239 -34.397 22.039  1.00 8.17  ? 145 VAL A C   1 
ATOM   3350 O  O   . VAL B 1 145 ? -26.440 -35.320 22.291  1.00 9.05  ? 145 VAL A O   1 
ATOM   3351 C  CB  . VAL B 1 145 ? -29.510 -35.603 21.952  1.00 9.28  ? 145 VAL A CB  1 
ATOM   3352 C  CG1 . VAL B 1 145 ? -29.922 -34.850 23.234  1.00 9.68  ? 145 VAL A CG1 1 
ATOM   3353 C  CG2 . VAL B 1 145 ? -30.712 -35.920 21.049  1.00 10.44 ? 145 VAL A CG2 1 
ATOM   3354 N  N   . LEU B 1 146 ? -27.112 -33.177 22.519  1.00 8.27  ? 146 LEU A N   1 
ATOM   3355 C  CA  . LEU B 1 146 ? -26.147 -32.819 23.542  1.00 8.88  ? 146 LEU A CA  1 
ATOM   3356 C  C   . LEU B 1 146 ? -26.779 -33.063 24.879  1.00 10.21 ? 146 LEU A C   1 
ATOM   3357 O  O   . LEU B 1 146 ? -27.905 -32.599 25.140  1.00 11.50 ? 146 LEU A O   1 
ATOM   3358 C  CB  . LEU B 1 146 ? -25.770 -31.351 23.539  1.00 11.16 ? 146 LEU A CB  1 
ATOM   3359 C  CG  . LEU B 1 146 ? -25.190 -30.875 22.287  1.00 12.35 ? 146 LEU A CG  1 
ATOM   3360 C  CD1 . LEU B 1 146 ? -24.998 -29.319 22.415  1.00 15.39 ? 146 LEU A CD1 1 
ATOM   3361 C  CD2 . LEU B 1 146 ? -23.797 -31.500 21.969  1.00 13.54 ? 146 LEU A CD2 1 
ATOM   3362 N  N   . GLY B 1 147 ? -26.084 -33.766 25.754  1.00 10.09 ? 147 GLY A N   1 
ATOM   3363 C  CA  . GLY B 1 147 ? -26.474 -33.961 27.161  1.00 9.69  ? 147 GLY A CA  1 
ATOM   3364 C  C   . GLY B 1 147 ? -25.594 -33.149 28.075  1.00 9.93  ? 147 GLY A C   1 
ATOM   3365 O  O   . GLY B 1 147 ? -24.373 -33.276 27.938  1.00 10.38 ? 147 GLY A O   1 
ATOM   3366 N  N   . VAL B 1 148 ? -26.168 -32.416 28.996  1.00 8.67  ? 148 VAL A N   1 
ATOM   3367 C  CA  . VAL B 1 148 ? -25.373 -31.621 29.982  1.00 9.84  ? 148 VAL A CA  1 
ATOM   3368 C  C   . VAL B 1 148 ? -25.922 -31.994 31.327  1.00 8.72  ? 148 VAL A C   1 
ATOM   3369 O  O   . VAL B 1 148 ? -27.144 -31.913 31.619  1.00 9.09  ? 148 VAL A O   1 
ATOM   3370 C  CB  . VAL B 1 148 ? -25.561 -30.110 29.726  1.00 10.29 ? 148 VAL A CB  1 
ATOM   3371 C  CG1 . VAL B 1 148 ? -24.809 -29.250 30.790  1.00 12.93 ? 148 VAL A CG1 1 
ATOM   3372 C  CG2 . VAL B 1 148 ? -25.108 -29.711 28.300  1.00 13.40 ? 148 VAL A CG2 1 
ATOM   3373 N  N   . PHE B 1 149 ? -24.982 -32.417 32.210  1.00 8.82  ? 149 PHE A N   1 
ATOM   3374 C  CA  . PHE B 1 149 ? -25.350 -32.696 33.591  1.00 9.01  ? 149 PHE A CA  1 
ATOM   3375 C  C   . PHE B 1 149 ? -25.537 -31.475 34.427  1.00 8.74  ? 149 PHE A C   1 
ATOM   3376 O  O   . PHE B 1 149 ? -24.778 -30.523 34.232  1.00 9.73  ? 149 PHE A O   1 
ATOM   3377 C  CB  . PHE B 1 149 ? -24.265 -33.582 34.225  1.00 9.88  ? 149 PHE A CB  1 
ATOM   3378 C  CG  . PHE B 1 149 ? -24.117 -34.899 33.544  1.00 8.38  ? 149 PHE A CG  1 
ATOM   3379 C  CD1 . PHE B 1 149 ? -25.214 -35.817 33.498  1.00 9.06  ? 149 PHE A CD1 1 
ATOM   3380 C  CD2 . PHE B 1 149 ? -22.881 -35.283 32.974  1.00 9.05  ? 149 PHE A CD2 1 
ATOM   3381 C  CE1 . PHE B 1 149 ? -25.038 -37.083 32.958  1.00 9.85  ? 149 PHE A CE1 1 
ATOM   3382 C  CE2 . PHE B 1 149 ? -22.719 -36.534 32.379  1.00 9.09  ? 149 PHE A CE2 1 
ATOM   3383 C  CZ  . PHE B 1 149 ? -23.797 -37.428 32.379  1.00 9.08  ? 149 PHE A CZ  1 
ATOM   3384 N  N   . LEU B 1 150 ? -26.489 -31.535 35.334  1.00 9.26  ? 150 LEU A N   1 
ATOM   3385 C  CA  . LEU B 1 150 ? -26.631 -30.456 36.342  1.00 10.32 ? 150 LEU A CA  1 
ATOM   3386 C  C   . LEU B 1 150 ? -26.387 -31.060 37.725  1.00 10.80 ? 150 LEU A C   1 
ATOM   3387 O  O   . LEU B 1 150 ? -27.069 -31.984 38.137  1.00 12.20 ? 150 LEU A O   1 
ATOM   3388 C  CB  . LEU B 1 150 ? -28.032 -29.799 36.324  1.00 11.28 ? 150 LEU A CB  1 
ATOM   3389 C  CG  . LEU B 1 150 ? -28.378 -28.944 35.114  1.00 10.87 ? 150 LEU A CG  1 
ATOM   3390 C  CD1 . LEU B 1 150 ? -28.709 -29.858 33.902  1.00 13.03 ? 150 LEU A CD1 1 
ATOM   3391 C  CD2 . LEU B 1 150 ? -29.625 -28.071 35.341  1.00 16.24 ? 150 LEU A CD2 1 
ATOM   3392 N  N   . GLN B 1 151 ? -25.447 -30.431 38.431  1.00 11.60 ? 151 GLN A N   1 
ATOM   3393 C  CA  . GLN B 1 151 ? -25.108 -30.818 39.808  1.00 11.72 ? 151 GLN A CA  1 
ATOM   3394 C  C   . GLN B 1 151 ? -25.611 -29.787 40.790  1.00 12.73 ? 151 GLN A C   1 
ATOM   3395 O  O   . GLN B 1 151 ? -25.674 -28.589 40.489  1.00 13.72 ? 151 GLN A O   1 
ATOM   3396 C  CB  . GLN B 1 151 ? -23.586 -30.943 39.912  1.00 13.46 ? 151 GLN A CB  1 
ATOM   3397 C  CG  . GLN B 1 151 ? -22.819 -29.662 39.823  1.00 16.09 ? 151 GLN A CG  1 
ATOM   3398 C  CD  . GLN B 1 151 ? -21.333 -29.862 39.881  1.00 20.03 ? 151 GLN A CD  1 
ATOM   3399 O  OE1 . GLN B 1 151 ? -20.802 -30.964 40.100  1.00 21.04 ? 151 GLN A OE1 1 
ATOM   3400 N  NE2 . GLN B 1 151 ? -20.651 -28.749 39.717  1.00 24.75 ? 151 GLN A NE2 1 
ATOM   3401 N  N   . ILE B 1 152 ? -26.050 -30.248 41.956  1.00 11.71 ? 152 ILE A N   1 
ATOM   3402 C  CA  . ILE B 1 152 ? -26.447 -29.228 42.982  1.00 13.58 ? 152 ILE A CA  1 
ATOM   3403 C  C   . ILE B 1 152 ? -25.274 -28.361 43.356  1.00 18.24 ? 152 ILE A C   1 
ATOM   3404 O  O   . ILE B 1 152 ? -24.126 -28.865 43.616  1.00 18.00 ? 152 ILE A O   1 
ATOM   3405 C  CB  . ILE B 1 152 ? -26.945 -29.902 44.229  1.00 15.74 ? 152 ILE A CB  1 
ATOM   3406 C  CG1 . ILE B 1 152 ? -28.182 -30.714 43.906  1.00 15.42 ? 152 ILE A CG1 1 
ATOM   3407 C  CG2 . ILE B 1 152 ? -27.245 -28.795 45.300  1.00 16.14 ? 152 ILE A CG2 1 
ATOM   3408 C  CD1 . ILE B 1 152 ? -29.338 -29.953 43.277  1.00 18.25 ? 152 ILE A CD1 1 
ATOM   3409 N  N   . GLY B 1 153 ? -25.474 -27.057 43.252  1.00 16.45 ? 153 GLY A N   1 
ATOM   3410 C  CA  . GLY B 1 153 ? -24.319 -26.085 43.500  1.00 17.91 ? 153 GLY A CA  1 
ATOM   3411 C  C   . GLY B 1 153 ? -24.989 -24.717 43.705  1.00 18.50 ? 153 GLY A C   1 
ATOM   3412 O  O   . GLY B 1 153 ? -26.183 -24.616 43.963  1.00 21.14 ? 153 GLY A O   1 
ATOM   3413 N  N   A GLU B 1 154 ? -24.208 -23.698 43.716  0.50 19.55 ? 154 GLU A N   1 
ATOM   3414 N  N   B GLU B 1 154 ? -24.170 -23.712 43.424  0.50 20.98 ? 154 GLU A N   1 
ATOM   3415 C  CA  A GLU B 1 154 ? -24.876 -22.398 43.944  0.50 16.57 ? 154 GLU A CA  1 
ATOM   3416 C  CA  B GLU B 1 154 ? -24.628 -22.295 43.568  0.50 20.43 ? 154 GLU A CA  1 
ATOM   3417 C  C   A GLU B 1 154 ? -25.716 -22.075 42.686  0.50 16.99 ? 154 GLU A C   1 
ATOM   3418 C  C   B GLU B 1 154 ? -25.741 -22.054 42.516  0.50 19.20 ? 154 GLU A C   1 
ATOM   3419 O  O   A GLU B 1 154 ? -25.484 -22.656 41.587  0.50 19.00 ? 154 GLU A O   1 
ATOM   3420 O  O   B GLU B 1 154 ? -25.756 -22.687 41.424  0.50 18.42 ? 154 GLU A O   1 
ATOM   3421 C  CB  A GLU B 1 154 ? -23.828 -21.390 44.239  0.50 16.67 ? 154 GLU A CB  1 
ATOM   3422 C  CB  B GLU B 1 154 ? -23.431 -21.344 43.465  0.50 24.35 ? 154 GLU A CB  1 
ATOM   3423 C  CG  A GLU B 1 154 ? -23.109 -21.652 45.564  0.50 13.56 ? 154 GLU A CG  1 
ATOM   3424 C  CG  B GLU B 1 154 ? -22.693 -21.384 42.161  0.50 25.48 ? 154 GLU A CG  1 
ATOM   3425 C  CD  A GLU B 1 154 ? -21.689 -21.270 45.521  0.50 16.05 ? 154 GLU A CD  1 
ATOM   3426 C  CD  B GLU B 1 154 ? -21.707 -20.230 41.979  0.50 23.91 ? 154 GLU A CD  1 
ATOM   3427 O  OE1 A GLU B 1 154 ? -21.100 -21.162 44.464  0.50 15.47 ? 154 GLU A OE1 1 
ATOM   3428 O  OE1 B GLU B 1 154 ? -20.542 -20.328 42.365  0.50 30.70 ? 154 GLU A OE1 1 
ATOM   3429 O  OE2 A GLU B 1 154 ? -21.169 -20.960 46.605  0.50 14.56 ? 154 GLU A OE2 1 
ATOM   3430 O  OE2 B GLU B 1 154 ? -22.088 -19.276 41.375  0.50 24.24 ? 154 GLU A OE2 1 
ATOM   3431 N  N   . PRO B 1 155 ? -26.755 -21.232 42.821  1.00 16.05 ? 155 PRO A N   1 
ATOM   3432 C  CA  . PRO B 1 155 ? -27.765 -21.027 41.751  1.00 15.20 ? 155 PRO A CA  1 
ATOM   3433 C  C   . PRO B 1 155 ? -27.119 -20.565 40.475  1.00 15.68 ? 155 PRO A C   1 
ATOM   3434 O  O   . PRO B 1 155 ? -26.135 -19.828 40.451  1.00 16.12 ? 155 PRO A O   1 
ATOM   3435 C  CB  . PRO B 1 155 ? -28.724 -19.975 42.323  1.00 18.56 ? 155 PRO A CB  1 
ATOM   3436 C  CG  . PRO B 1 155 ? -27.990 -19.433 43.517  1.00 16.96 ? 155 PRO A CG  1 
ATOM   3437 C  CD  . PRO B 1 155 ? -27.078 -20.475 44.044  1.00 14.75 ? 155 PRO A CD  1 
ATOM   3438 N  N   . ASN B 1 156 ? -27.772 -20.984 39.419  1.00 16.23 ? 156 ASN A N   1 
ATOM   3439 C  CA  . ASN B 1 156 ? -27.294 -20.720 38.082  1.00 14.09 ? 156 ASN A CA  1 
ATOM   3440 C  C   . ASN B 1 156 ? -28.187 -19.613 37.447  1.00 13.26 ? 156 ASN A C   1 
ATOM   3441 O  O   . ASN B 1 156 ? -29.398 -19.873 37.097  1.00 14.44 ? 156 ASN A O   1 
ATOM   3442 C  CB  . ASN B 1 156 ? -27.412 -21.974 37.286  1.00 15.32 ? 156 ASN A CB  1 
ATOM   3443 C  CG  . ASN B 1 156 ? -26.681 -21.886 35.948  1.00 16.05 ? 156 ASN A CG  1 
ATOM   3444 O  OD1 . ASN B 1 156 ? -26.514 -20.795 35.327  1.00 15.96 ? 156 ASN A OD1 1 
ATOM   3445 N  ND2 . ASN B 1 156 ? -26.303 -23.040 35.435  1.00 14.61 ? 156 ASN A ND2 1 
ATOM   3446 N  N   . SER B 1 157 ? -27.588 -18.411 37.304  1.00 18.00 ? 157 SER A N   1 
ATOM   3447 C  CA  . SER B 1 157 ? -28.367 -17.302 36.713  1.00 16.26 ? 157 SER A CA  1 
ATOM   3448 C  C   . SER B 1 157 ? -28.814 -17.531 35.303  1.00 17.25 ? 157 SER A C   1 
ATOM   3449 O  O   . SER B 1 157 ? -29.780 -16.891 34.828  1.00 17.98 ? 157 SER A O   1 
ATOM   3450 C  CB  . SER B 1 157 ? -27.495 -16.005 36.733  1.00 21.40 ? 157 SER A CB  1 
ATOM   3451 O  OG  . SER B 1 157 ? -26.345 -16.254 35.905  1.00 25.27 ? 157 SER A OG  1 
ATOM   3452 N  N   . GLN B 1 158 ? -28.186 -18.496 34.608  1.00 15.40 ? 158 GLN A N   1 
ATOM   3453 C  CA  . GLN B 1 158 ? -28.655 -18.790 33.226  1.00 17.07 ? 158 GLN A CA  1 
ATOM   3454 C  C   . GLN B 1 158 ? -29.902 -19.585 33.109  1.00 17.65 ? 158 GLN A C   1 
ATOM   3455 O  O   . GLN B 1 158 ? -30.402 -19.891 32.027  1.00 17.41 ? 158 GLN A O   1 
ATOM   3456 C  CB  . GLN B 1 158 ? -27.529 -19.413 32.435  1.00 20.62 ? 158 GLN A CB  1 
ATOM   3457 C  CG  . GLN B 1 158 ? -26.222 -18.628 32.417  1.00 20.42 ? 158 GLN A CG  1 
ATOM   3458 C  CD  . GLN B 1 158 ? -26.387 -17.221 31.918  1.00 28.33 ? 158 GLN A CD  1 
ATOM   3459 O  OE1 . GLN B 1 158 ? -25.937 -16.283 32.578  1.00 37.76 ? 158 GLN A OE1 1 
ATOM   3460 N  NE2 . GLN B 1 158 ? -27.066 -17.050 30.772  1.00 24.87 ? 158 GLN A NE2 1 
ATOM   3461 N  N   . LEU B 1 159 ? -30.414 -20.095 34.220  1.00 17.00 ? 159 LEU A N   1 
ATOM   3462 C  CA  . LEU B 1 159 ? -31.724 -20.697 34.226  1.00 16.87 ? 159 LEU A CA  1 
ATOM   3463 C  C   . LEU B 1 159 ? -32.862 -19.714 34.462  1.00 14.13 ? 159 LEU A C   1 
ATOM   3464 O  O   . LEU B 1 159 ? -34.023 -20.166 34.404  1.00 14.81 ? 159 LEU A O   1 
ATOM   3465 C  CB  . LEU B 1 159 ? -31.788 -21.831 35.280  1.00 16.51 ? 159 LEU A CB  1 
ATOM   3466 C  CG  . LEU B 1 159 ? -30.867 -23.029 35.014  1.00 14.61 ? 159 LEU A CG  1 
ATOM   3467 C  CD1 . LEU B 1 159 ? -30.782 -23.897 36.250  1.00 18.65 ? 159 LEU A CD1 1 
ATOM   3468 C  CD2 . LEU B 1 159 ? -31.316 -23.910 33.867  1.00 17.69 ? 159 LEU A CD2 1 
ATOM   3469 N  N   . GLN B 1 160 ? -32.594 -18.427 34.771  1.00 14.21 ? 160 GLN A N   1 
ATOM   3470 C  CA  . GLN B 1 160 ? -33.696 -17.519 35.109  1.00 15.47 ? 160 GLN A CA  1 
ATOM   3471 C  C   . GLN B 1 160 ? -34.767 -17.382 34.022  1.00 14.19 ? 160 GLN A C   1 
ATOM   3472 O  O   . GLN B 1 160 ? -35.959 -17.311 34.352  1.00 15.10 ? 160 GLN A O   1 
ATOM   3473 C  CB  . GLN B 1 160 ? -33.165 -16.101 35.553  1.00 17.69 ? 160 GLN A CB  1 
ATOM   3474 C  CG  . GLN B 1 160 ? -34.252 -15.153 36.006  1.00 16.64 ? 160 GLN A CG  1 
ATOM   3475 C  CD  . GLN B 1 160 ? -33.903 -13.696 35.967  1.00 20.14 ? 160 GLN A CD  1 
ATOM   3476 O  OE1 . GLN B 1 160 ? -32.745 -13.283 35.876  1.00 24.16 ? 160 GLN A OE1 1 
ATOM   3477 N  NE2 . GLN B 1 160 ? -34.934 -12.894 35.934  1.00 23.28 ? 160 GLN A NE2 1 
ATOM   3478 N  N   . LYS B 1 161 ? -34.324 -17.275 32.796  1.00 14.64 ? 161 LYS A N   1 
ATOM   3479 C  CA  . LYS B 1 161 ? -35.400 -17.063 31.758  1.00 15.78 ? 161 LYS A CA  1 
ATOM   3480 C  C   . LYS B 1 161 ? -36.377 -18.244 31.689  1.00 15.15 ? 161 LYS A C   1 
ATOM   3481 O  O   . LYS B 1 161 ? -37.593 -18.032 31.665  1.00 16.29 ? 161 LYS A O   1 
ATOM   3482 C  CB  . LYS B 1 161 ? -34.756 -16.805 30.426  1.00 17.20 ? 161 LYS A CB  1 
ATOM   3483 C  CG  . LYS B 1 161 ? -35.798 -16.248 29.388  1.00 16.76 ? 161 LYS A CG  1 
ATOM   3484 C  CD  . LYS B 1 161 ? -35.101 -16.270 27.985  1.00 17.81 ? 161 LYS A CD  1 
ATOM   3485 C  CE  . LYS B 1 161 ? -36.089 -16.091 26.840  1.00 16.53 ? 161 LYS A CE  1 
ATOM   3486 N  NZ  . LYS B 1 161 ? -36.698 -14.647 26.919  1.00 18.82 ? 161 LYS A NZ  1 
ATOM   3487 N  N   . ILE B 1 162 ? -35.837 -19.448 31.874  1.00 13.59 ? 162 ILE A N   1 
ATOM   3488 C  CA  . ILE B 1 162 ? -36.705 -20.595 32.002  1.00 12.49 ? 162 ILE A CA  1 
ATOM   3489 C  C   . ILE B 1 162 ? -37.595 -20.590 33.260  1.00 12.43 ? 162 ILE A C   1 
ATOM   3490 O  O   . ILE B 1 162 ? -38.805 -20.760 33.178  1.00 13.33 ? 162 ILE A O   1 
ATOM   3491 C  CB  . ILE B 1 162 ? -35.870 -21.946 31.938  1.00 10.81 ? 162 ILE A CB  1 
ATOM   3492 C  CG1 . ILE B 1 162 ? -35.222 -22.055 30.514  1.00 11.97 ? 162 ILE A CG1 1 
ATOM   3493 C  CG2 . ILE B 1 162 ? -36.840 -23.085 32.171  1.00 13.38 ? 162 ILE A CG2 1 
ATOM   3494 C  CD1 . ILE B 1 162 ? -34.096 -23.098 30.430  1.00 14.10 ? 162 ILE A CD1 1 
ATOM   3495 N  N   . THR B 1 163 ? -36.940 -20.492 34.423  1.00 14.06 ? 163 THR A N   1 
ATOM   3496 C  CA  . THR B 1 163 ? -37.691 -20.614 35.680  1.00 15.49 ? 163 THR A CA  1 
ATOM   3497 C  C   . THR B 1 163 ? -38.747 -19.536 35.818  1.00 13.35 ? 163 THR A C   1 
ATOM   3498 O  O   . THR B 1 163 ? -39.804 -19.823 36.360  1.00 15.53 ? 163 THR A O   1 
ATOM   3499 C  CB  . THR B 1 163 ? -36.768 -20.598 36.897  1.00 16.56 ? 163 THR A CB  1 
ATOM   3500 O  OG1 . THR B 1 163 ? -35.962 -19.445 36.939  1.00 18.32 ? 163 THR A OG1 1 
ATOM   3501 C  CG2 . THR B 1 163 ? -35.900 -21.882 36.887  1.00 15.32 ? 163 THR A CG2 1 
ATOM   3502 N  N   . ASP B 1 164 ? -38.516 -18.317 35.264  1.00 15.83 ? 164 ASP A N   1 
ATOM   3503 C  CA  . ASP B 1 164 ? -39.547 -17.194 35.319  1.00 15.41 ? 164 ASP A CA  1 
ATOM   3504 C  C   . ASP B 1 164 ? -40.835 -17.600 34.593  1.00 17.34 ? 164 ASP A C   1 
ATOM   3505 O  O   . ASP B 1 164 ? -41.863 -17.008 34.803  1.00 19.27 ? 164 ASP A O   1 
ATOM   3506 C  CB  . ASP B 1 164 ? -39.035 -15.919 34.676  1.00 18.84 ? 164 ASP A CB  1 
ATOM   3507 C  CG  . ASP B 1 164 ? -38.105 -15.106 35.570  1.00 21.27 ? 164 ASP A CG  1 
ATOM   3508 O  OD1 . ASP B 1 164 ? -38.002 -15.437 36.792  1.00 23.24 ? 164 ASP A OD1 1 
ATOM   3509 O  OD2 . ASP B 1 164 ? -37.465 -14.144 35.073  1.00 21.82 ? 164 ASP A OD2 1 
ATOM   3510 N  N   . THR B 1 165 ? -40.772 -18.578 33.660  1.00 16.52 ? 165 THR A N   1 
ATOM   3511 C  CA  . THR B 1 165 ? -41.920 -18.899 32.878  1.00 15.68 ? 165 THR A CA  1 
ATOM   3512 C  C   . THR B 1 165 ? -42.745 -20.022 33.409  1.00 13.62 ? 165 THR A C   1 
ATOM   3513 O  O   . THR B 1 165 ? -43.844 -20.402 32.951  1.00 14.97 ? 165 THR A O   1 
ATOM   3514 C  CB  . THR B 1 165 ? -41.562 -19.317 31.416  1.00 14.89 ? 165 THR A CB  1 
ATOM   3515 O  OG1 . THR B 1 165 ? -40.924 -20.618 31.435  1.00 15.98 ? 165 THR A OG1 1 
ATOM   3516 C  CG2 . THR B 1 165 ? -40.771 -18.326 30.694  1.00 18.15 ? 165 THR A CG2 1 
ATOM   3517 N  N   . LEU B 1 166 ? -42.243 -20.745 34.437  1.00 14.39 ? 166 LEU A N   1 
ATOM   3518 C  CA  . LEU B 1 166 ? -42.853 -22.010 34.852  1.00 15.60 ? 166 LEU A CA  1 
ATOM   3519 C  C   . LEU B 1 166 ? -44.282 -21.878 35.372  1.00 15.49 ? 166 LEU A C   1 
ATOM   3520 O  O   . LEU B 1 166 ? -45.094 -22.733 35.087  1.00 16.39 ? 166 LEU A O   1 
ATOM   3521 C  CB  . LEU B 1 166 ? -41.927 -22.772 35.809  1.00 17.57 ? 166 LEU A CB  1 
ATOM   3522 C  CG  . LEU B 1 166 ? -40.520 -23.220 35.282  1.00 15.86 ? 166 LEU A CG  1 
ATOM   3523 C  CD1 . LEU B 1 166 ? -39.662 -23.757 36.532  1.00 15.50 ? 166 LEU A CD1 1 
ATOM   3524 C  CD2 . LEU B 1 166 ? -40.660 -24.216 34.111  1.00 18.70 ? 166 LEU A CD2 1 
ATOM   3525 N  N   . ASP B 1 167 ? -44.557 -20.794 36.111  1.00 17.18 ? 167 ASP A N   1 
ATOM   3526 C  CA  . ASP B 1 167 ? -45.969 -20.589 36.542  1.00 19.43 ? 167 ASP A CA  1 
ATOM   3527 C  C   . ASP B 1 167 ? -46.922 -20.490 35.351  1.00 18.26 ? 167 ASP A C   1 
ATOM   3528 O  O   . ASP B 1 167 ? -48.006 -21.141 35.408  1.00 21.09 ? 167 ASP A O   1 
ATOM   3529 C  CB  . ASP B 1 167 ? -46.046 -19.346 37.411  1.00 21.96 ? 167 ASP A CB  1 
ATOM   3530 C  CG  . ASP B 1 167 ? -45.427 -19.553 38.800  1.00 25.65 ? 167 ASP A CG  1 
ATOM   3531 O  OD1 . ASP B 1 167 ? -45.286 -20.710 39.260  1.00 29.73 ? 167 ASP A OD1 1 
ATOM   3532 O  OD2 . ASP B 1 167 ? -45.089 -18.509 39.440  1.00 32.78 ? 167 ASP A OD2 1 
ATOM   3533 N  N   . SER B 1 168 ? -46.493 -19.806 34.276  1.00 15.24 ? 168 SER A N   1 
ATOM   3534 C  CA  . SER B 1 168 ? -47.323 -19.682 33.101  1.00 17.50 ? 168 SER A CA  1 
ATOM   3535 C  C   . SER B 1 168 ? -47.554 -20.962 32.351  1.00 16.94 ? 168 SER A C   1 
ATOM   3536 O  O   . SER B 1 168 ? -48.486 -21.059 31.572  1.00 19.23 ? 168 SER A O   1 
ATOM   3537 C  CB  . SER B 1 168 ? -46.821 -18.608 32.217  1.00 19.36 ? 168 SER A CB  1 
ATOM   3538 O  OG  . SER B 1 168 ? -45.622 -19.020 31.582  1.00 21.63 ? 168 SER A OG  1 
ATOM   3539 N  N   . ILE B 1 169 ? -46.704 -21.977 32.547  1.00 14.53 ? 169 ILE A N   1 
ATOM   3540 C  CA  . ILE B 1 169 ? -46.875 -23.242 31.848  1.00 13.90 ? 169 ILE A CA  1 
ATOM   3541 C  C   . ILE B 1 169 ? -47.097 -24.361 32.828  1.00 13.38 ? 169 ILE A C   1 
ATOM   3542 O  O   . ILE B 1 169 ? -46.762 -25.504 32.590  1.00 13.17 ? 169 ILE A O   1 
ATOM   3543 C  CB  . ILE B 1 169 ? -45.763 -23.555 30.808  1.00 13.96 ? 169 ILE A CB  1 
ATOM   3544 C  CG1 . ILE B 1 169 ? -44.407 -23.596 31.518  1.00 14.49 ? 169 ILE A CG1 1 
ATOM   3545 C  CG2 . ILE B 1 169 ? -45.654 -22.476 29.706  1.00 13.33 ? 169 ILE A CG2 1 
ATOM   3546 C  CD1 . ILE B 1 169 ? -43.377 -24.391 30.647  1.00 15.16 ? 169 ILE A CD1 1 
ATOM   3547 N  N   . LYS B 1 170 ? -47.718 -24.037 34.023  1.00 14.50 ? 170 LYS A N   1 
ATOM   3548 C  CA  . LYS B 1 170 ? -47.946 -25.091 34.965  1.00 16.55 ? 170 LYS A CA  1 
ATOM   3549 C  C   . LYS B 1 170 ? -48.688 -26.309 34.445  1.00 13.61 ? 170 LYS A C   1 
ATOM   3550 O  O   . LYS B 1 170 ? -48.322 -27.471 34.753  1.00 16.49 ? 170 LYS A O   1 
ATOM   3551 C  CB  . LYS B 1 170 ? -48.728 -24.514 36.221  1.00 17.50 ? 170 LYS A CB  1 
ATOM   3552 C  CG  . LYS B 1 170 ? -48.923 -25.596 37.327  1.00 20.42 ? 170 LYS A CG  1 
ATOM   3553 C  CD  . LYS B 1 170 ? -49.663 -25.084 38.598  1.00 26.99 ? 170 LYS A CD  1 
ATOM   3554 C  CE  . LYS B 1 170 ? -49.386 -25.983 39.791  1.00 32.81 ? 170 LYS A CE  1 
ATOM   3555 N  NZ  . LYS B 1 170 ? -47.971 -25.868 40.238  1.00 27.49 ? 170 LYS A NZ  1 
ATOM   3556 N  N   . GLU B 1 171 ? -49.757 -26.110 33.651  1.00 15.12 ? 171 GLU A N   1 
ATOM   3557 C  CA  . GLU B 1 171 ? -50.584 -27.238 33.193  1.00 16.10 ? 171 GLU A CA  1 
ATOM   3558 C  C   . GLU B 1 171 ? -50.076 -27.758 31.859  1.00 13.54 ? 171 GLU A C   1 
ATOM   3559 O  O   . GLU B 1 171 ? -49.544 -26.922 31.041  1.00 14.98 ? 171 GLU A O   1 
ATOM   3560 C  CB  . GLU B 1 171 ? -52.077 -26.834 33.031  1.00 18.09 ? 171 GLU A CB  1 
ATOM   3561 C  CG  . GLU B 1 171 ? -52.766 -26.347 34.328  1.00 22.47 ? 171 GLU A CG  1 
ATOM   3562 C  CD  . GLU B 1 171 ? -52.263 -24.962 34.779  1.00 25.49 ? 171 GLU A CD  1 
ATOM   3563 O  OE1 . GLU B 1 171 ? -52.352 -24.711 36.015  1.00 39.38 ? 171 GLU A OE1 1 
ATOM   3564 O  OE2 . GLU B 1 171 ? -51.740 -24.068 33.998  1.00 26.88 ? 171 GLU A OE2 1 
ATOM   3565 N  N   . LYS B 1 172 ? -50.177 -29.060 31.679  1.00 15.42 ? 172 LYS A N   1 
ATOM   3566 C  CA  . LYS B 1 172 ? -49.898 -29.640 30.363  1.00 14.09 ? 172 LYS A CA  1 
ATOM   3567 C  C   . LYS B 1 172 ? -50.626 -28.917 29.254  1.00 15.48 ? 172 LYS A C   1 
ATOM   3568 O  O   . LYS B 1 172 ? -51.827 -28.667 29.382  1.00 15.62 ? 172 LYS A O   1 
ATOM   3569 C  CB  . LYS B 1 172 ? -50.268 -31.103 30.403  1.00 15.29 ? 172 LYS A CB  1 
ATOM   3570 C  CG  . LYS B 1 172 ? -50.033 -31.887 29.150  1.00 15.15 ? 172 LYS A CG  1 
ATOM   3571 C  CD  . LYS B 1 172 ? -50.480 -33.311 29.258  1.00 20.62 ? 172 LYS A CD  1 
ATOM   3572 C  CE  . LYS B 1 172 ? -50.121 -34.027 27.959  1.00 20.51 ? 172 LYS A CE  1 
ATOM   3573 N  NZ  . LYS B 1 172 ? -50.287 -35.494 28.113  1.00 29.16 ? 172 LYS A NZ  1 
ATOM   3574 N  N   . GLY B 1 173 ? -49.905 -28.674 28.172  1.00 13.40 ? 173 GLY A N   1 
ATOM   3575 C  CA  . GLY B 1 173 ? -50.417 -27.971 26.979  1.00 14.54 ? 173 GLY A CA  1 
ATOM   3576 C  C   . GLY B 1 173 ? -50.245 -26.508 26.978  1.00 14.65 ? 173 GLY A C   1 
ATOM   3577 O  O   . GLY B 1 173 ? -50.391 -25.910 25.902  1.00 17.39 ? 173 GLY A O   1 
ATOM   3578 N  N   A LYS B 1 174 ? -49.922 -25.876 28.080  0.50 13.81 ? 174 LYS A N   1 
ATOM   3579 N  N   B LYS B 1 174 ? -49.938 -25.866 28.102  0.50 13.81 ? 174 LYS A N   1 
ATOM   3580 C  CA  A LYS B 1 174 ? -49.731 -24.455 28.061  0.50 13.68 ? 174 LYS A CA  1 
ATOM   3581 C  CA  B LYS B 1 174 ? -49.708 -24.422 28.133  0.50 13.64 ? 174 LYS A CA  1 
ATOM   3582 C  C   A LYS B 1 174 ? -48.429 -24.074 27.399  0.50 13.33 ? 174 LYS A C   1 
ATOM   3583 C  C   B LYS B 1 174 ? -48.432 -24.075 27.401  0.50 13.26 ? 174 LYS A C   1 
ATOM   3584 O  O   A LYS B 1 174 ? -47.422 -24.844 27.483  0.50 13.82 ? 174 LYS A O   1 
ATOM   3585 O  O   B LYS B 1 174 ? -47.439 -24.870 27.456  0.50 13.83 ? 174 LYS A O   1 
ATOM   3586 C  CB  A LYS B 1 174 ? -49.787 -23.896 29.472  0.50 16.42 ? 174 LYS A CB  1 
ATOM   3587 C  CB  B LYS B 1 174 ? -49.614 -23.842 29.566  0.50 15.75 ? 174 LYS A CB  1 
ATOM   3588 C  CG  A LYS B 1 174 ? -51.138 -24.245 30.155  0.50 18.08 ? 174 LYS A CG  1 
ATOM   3589 C  CG  B LYS B 1 174 ? -50.935 -23.832 30.360  0.50 18.21 ? 174 LYS A CG  1 
ATOM   3590 C  CD  A LYS B 1 174 ? -51.323 -23.268 31.307  0.50 21.18 ? 174 LYS A CD  1 
ATOM   3591 C  CD  B LYS B 1 174 ? -51.907 -22.780 29.884  0.50 18.23 ? 174 LYS A CD  1 
ATOM   3592 C  CE  A LYS B 1 174 ? -52.751 -22.749 31.240  0.50 24.01 ? 174 LYS A CE  1 
ATOM   3593 C  CE  B LYS B 1 174 ? -53.280 -23.021 30.503  0.50 22.34 ? 174 LYS A CE  1 
ATOM   3594 N  NZ  A LYS B 1 174 ? -53.612 -23.828 30.658  0.50 23.71 ? 174 LYS A NZ  1 
ATOM   3595 N  NZ  B LYS B 1 174 ? -53.201 -23.156 31.992  0.50 27.02 ? 174 LYS A NZ  1 
ATOM   3596 N  N   . GLN B 1 175 ? -48.425 -22.952 26.720  1.00 13.11 ? 175 GLN A N   1 
ATOM   3597 C  CA  . GLN B 1 175 ? -47.219 -22.404 26.090  1.00 13.61 ? 175 GLN A CA  1 
ATOM   3598 C  C   . GLN B 1 175 ? -47.129 -20.912 26.247  1.00 15.10 ? 175 GLN A C   1 
ATOM   3599 O  O   . GLN B 1 175 ? -48.160 -20.197 26.526  1.00 17.04 ? 175 GLN A O   1 
ATOM   3600 C  CB  . GLN B 1 175 ? -47.160 -22.786 24.622  1.00 14.31 ? 175 GLN A CB  1 
ATOM   3601 C  CG  . GLN B 1 175 ? -48.186 -22.010 23.735  1.00 18.52 ? 175 GLN A CG  1 
ATOM   3602 C  CD  . GLN B 1 175 ? -48.139 -22.554 22.352  1.00 17.62 ? 175 GLN A CD  1 
ATOM   3603 O  OE1 . GLN B 1 175 ? -48.326 -23.718 22.146  1.00 21.11 ? 175 GLN A OE1 1 
ATOM   3604 N  NE2 . GLN B 1 175 ? -47.934 -21.628 21.368  1.00 18.71 ? 175 GLN A NE2 1 
ATOM   3605 N  N   A THR B 1 176 ? -45.947 -20.378 26.087  0.50 13.72 ? 176 THR A N   1 
ATOM   3606 N  N   B THR B 1 176 ? -45.917 -20.367 26.232  0.50 13.34 ? 176 THR A N   1 
ATOM   3607 C  CA  A THR B 1 176 ? -45.773 -18.963 26.134  0.50 14.90 ? 176 THR A CA  1 
ATOM   3608 C  CA  B THR B 1 176 ? -45.676 -18.921 26.274  0.50 14.09 ? 176 THR A CA  1 
ATOM   3609 C  C   A THR B 1 176 ? -44.645 -18.615 25.185  0.50 13.55 ? 176 THR A C   1 
ATOM   3610 C  C   B THR B 1 176 ? -44.520 -18.494 25.378  0.50 14.01 ? 176 THR A C   1 
ATOM   3611 O  O   A THR B 1 176 ? -43.789 -19.481 24.830  0.50 12.14 ? 176 THR A O   1 
ATOM   3612 O  O   B THR B 1 176 ? -43.518 -19.220 25.211  0.50 13.15 ? 176 THR A O   1 
ATOM   3613 C  CB  A THR B 1 176 ? -45.547 -18.475 27.557  0.50 17.40 ? 176 THR A CB  1 
ATOM   3614 C  CB  B THR B 1 176 ? -45.566 -18.330 27.682  0.50 17.72 ? 176 THR A CB  1 
ATOM   3615 O  OG1 A THR B 1 176 ? -45.674 -17.007 27.604  0.50 17.02 ? 176 THR A OG1 1 
ATOM   3616 O  OG1 B THR B 1 176 ? -44.256 -17.853 27.996  0.50 18.64 ? 176 THR A OG1 1 
ATOM   3617 C  CG2 A THR B 1 176 ? -44.328 -19.049 28.097  0.50 15.97 ? 176 THR A CG2 1 
ATOM   3618 C  CG2 B THR B 1 176 ? -46.245 -19.130 28.683  0.50 12.24 ? 176 THR A CG2 1 
ATOM   3619 N  N   A ARG B 1 177 ? -44.612 -17.365 24.791  0.50 13.16 ? 177 ARG A N   1 
ATOM   3620 N  N   B ARG B 1 177 ? -44.622 -17.325 24.788  0.50 13.82 ? 177 ARG A N   1 
ATOM   3621 C  CA  A ARG B 1 177 ? -43.595 -16.817 23.971  0.50 13.14 ? 177 ARG A CA  1 
ATOM   3622 C  CA  B ARG B 1 177 ? -43.600 -16.856 23.901  0.50 13.53 ? 177 ARG A CA  1 
ATOM   3623 C  C   A ARG B 1 177 ? -42.279 -16.991 24.696  0.50 13.45 ? 177 ARG A C   1 
ATOM   3624 C  C   B ARG B 1 177 ? -42.254 -16.862 24.649  0.50 13.90 ? 177 ARG A C   1 
ATOM   3625 O  O   A ARG B 1 177 ? -42.180 -16.807 25.924  0.50 14.50 ? 177 ARG A O   1 
ATOM   3626 O  O   B ARG B 1 177 ? -42.108 -16.439 25.817  0.50 14.06 ? 177 ARG A O   1 
ATOM   3627 C  CB  A ARG B 1 177 ? -43.810 -15.279 23.875  0.50 14.22 ? 177 ARG A CB  1 
ATOM   3628 C  CB  B ARG B 1 177 ? -43.857 -15.392 23.427  0.50 15.20 ? 177 ARG A CB  1 
ATOM   3629 C  CG  A ARG B 1 177 ? -42.791 -14.611 23.017  0.50 13.23 ? 177 ARG A CG  1 
ATOM   3630 C  CG  B ARG B 1 177 ? -42.788 -14.952 22.434  0.50 15.66 ? 177 ARG A CG  1 
ATOM   3631 C  CD  A ARG B 1 177 ? -43.030 -13.124 22.667  0.50 17.60 ? 177 ARG A CD  1 
ATOM   3632 C  CD  B ARG B 1 177 ? -43.107 -13.611 21.803  0.50 20.19 ? 177 ARG A CD  1 
ATOM   3633 N  NE  A ARG B 1 177 ? -42.310 -12.821 21.423  0.50 21.27 ? 177 ARG A NE  1 
ATOM   3634 N  NE  B ARG B 1 177 ? -42.018 -12.944 21.076  0.50 21.69 ? 177 ARG A NE  1 
ATOM   3635 C  CZ  A ARG B 1 177 ? -41.613 -11.715 21.095  0.50 23.57 ? 177 ARG A CZ  1 
ATOM   3636 C  CZ  B ARG B 1 177 ? -41.512 -13.242 19.878  0.50 21.97 ? 177 ARG A CZ  1 
ATOM   3637 N  NH1 A ARG B 1 177 ? -41.470 -10.712 21.926  0.50 27.00 ? 177 ARG A NH1 1 
ATOM   3638 N  NH1 B ARG B 1 177 ? -41.851 -14.273 19.161  0.50 17.60 ? 177 ARG A NH1 1 
ATOM   3639 N  NH2 A ARG B 1 177 ? -41.041 -11.625 19.899  0.50 24.35 ? 177 ARG A NH2 1 
ATOM   3640 N  NH2 B ARG B 1 177 ? -40.598 -12.435 19.348  0.50 28.42 ? 177 ARG A NH2 1 
ATOM   3641 N  N   . PHE B 1 178 ? -41.220 -17.294 23.916  1.00 12.22 ? 178 PHE A N   1 
ATOM   3642 C  CA  . PHE B 1 178 ? -39.863 -17.490 24.515  1.00 12.25 ? 178 PHE A CA  1 
ATOM   3643 C  C   . PHE B 1 178 ? -38.816 -17.320 23.464  1.00 11.90 ? 178 PHE A C   1 
ATOM   3644 O  O   . PHE B 1 178 ? -38.543 -18.211 22.667  1.00 13.42 ? 178 PHE A O   1 
ATOM   3645 C  CB  . PHE B 1 178 ? -39.792 -18.889 25.131  1.00 12.77 ? 178 PHE A CB  1 
ATOM   3646 C  CG  . PHE B 1 178 ? -38.660 -19.111 26.074  1.00 12.70 ? 178 PHE A CG  1 
ATOM   3647 C  CD1 . PHE B 1 178 ? -38.810 -18.799 27.396  1.00 13.56 ? 178 PHE A CD1 1 
ATOM   3648 C  CD2 . PHE B 1 178 ? -37.442 -19.674 25.637  1.00 11.81 ? 178 PHE A CD2 1 
ATOM   3649 C  CE1 . PHE B 1 178 ? -37.825 -19.054 28.310  1.00 14.27 ? 178 PHE A CE1 1 
ATOM   3650 C  CE2 . PHE B 1 178 ? -36.425 -19.916 26.583  1.00 13.29 ? 178 PHE A CE2 1 
ATOM   3651 C  CZ  . PHE B 1 178 ? -36.643 -19.600 27.895  1.00 12.75 ? 178 PHE A CZ  1 
ATOM   3652 N  N   . THR B 1 179 ? -38.311 -16.110 23.353  1.00 13.28 ? 179 THR A N   1 
ATOM   3653 C  CA  . THR B 1 179 ? -37.267 -15.838 22.366  1.00 14.20 ? 179 THR A CA  1 
ATOM   3654 C  C   . THR B 1 179 ? -36.123 -15.083 23.017  1.00 13.00 ? 179 THR A C   1 
ATOM   3655 O  O   . THR B 1 179 ? -36.164 -14.699 24.212  1.00 15.20 ? 179 THR A O   1 
ATOM   3656 C  CB  . THR B 1 179 ? -37.760 -15.128 21.074  1.00 16.53 ? 179 THR A CB  1 
ATOM   3657 O  OG1 . THR B 1 179 ? -36.745 -15.240 20.034  1.00 16.92 ? 179 THR A OG1 1 
ATOM   3658 C  CG2 . THR B 1 179 ? -38.123 -13.667 21.391  1.00 17.08 ? 179 THR A CG2 1 
ATOM   3659 N  N   A ASN B 1 180 ? -35.096 -14.839 22.202  0.50 13.25 ? 180 ASN A N   1 
ATOM   3660 N  N   B ASN B 1 180 ? -35.035 -14.809 22.277  0.50 14.31 ? 180 ASN A N   1 
ATOM   3661 C  CA  A ASN B 1 180 ? -33.914 -14.193 22.729  0.50 13.28 ? 180 ASN A CA  1 
ATOM   3662 C  CA  B ASN B 1 180 ? -33.840 -14.139 22.877  0.50 15.03 ? 180 ASN A CA  1 
ATOM   3663 C  C   A ASN B 1 180 ? -33.387 -14.955 23.941  0.50 14.19 ? 180 ASN A C   1 
ATOM   3664 C  C   B ASN B 1 180 ? -33.182 -14.956 23.974  0.50 14.79 ? 180 ASN A C   1 
ATOM   3665 O  O   A ASN B 1 180 ? -33.260 -14.450 25.045  0.50 14.70 ? 180 ASN A O   1 
ATOM   3666 O  O   B ASN B 1 180 ? -32.739 -14.475 25.048  0.50 13.64 ? 180 ASN A O   1 
ATOM   3667 C  CB  A ASN B 1 180 ? -34.175 -12.687 22.994  0.50 15.15 ? 180 ASN A CB  1 
ATOM   3668 C  CB  B ASN B 1 180 ? -34.141 -12.709 23.412  0.50 18.56 ? 180 ASN A CB  1 
ATOM   3669 C  CG  A ASN B 1 180 ? -34.529 -11.958 21.725  0.50 17.05 ? 180 ASN A CG  1 
ATOM   3670 C  CG  B ASN B 1 180 ? -32.898 -11.929 23.762  0.50 24.77 ? 180 ASN A CG  1 
ATOM   3671 O  OD1 A ASN B 1 180 ? -33.895 -12.146 20.677  0.50 18.65 ? 180 ASN A OD1 1 
ATOM   3672 O  OD1 B ASN B 1 180 ? -31.753 -12.266 23.369  0.50 30.49 ? 180 ASN A OD1 1 
ATOM   3673 N  ND2 A ASN B 1 180 ? -35.597 -11.194 21.783  0.50 18.17 ? 180 ASN A ND2 1 
ATOM   3674 N  ND2 B ASN B 1 180 ? -33.119 -10.831 24.516  0.50 27.95 ? 180 ASN A ND2 1 
ATOM   3675 N  N   . PHE B 1 181 ? -33.164 -16.259 23.729  1.00 13.33 ? 181 PHE A N   1 
ATOM   3676 C  CA  . PHE B 1 181 ? -32.696 -17.180 24.785  1.00 12.81 ? 181 PHE A CA  1 
ATOM   3677 C  C   . PHE B 1 181 ? -31.208 -17.489 24.549  1.00 12.18 ? 181 PHE A C   1 
ATOM   3678 O  O   . PHE B 1 181 ? -30.870 -18.063 23.504  1.00 13.14 ? 181 PHE A O   1 
ATOM   3679 C  CB  . PHE B 1 181 ? -33.512 -18.468 24.636  1.00 13.27 ? 181 PHE A CB  1 
ATOM   3680 C  CG  . PHE B 1 181 ? -33.049 -19.641 25.488  1.00 12.56 ? 181 PHE A CG  1 
ATOM   3681 C  CD1 . PHE B 1 181 ? -32.657 -19.484 26.820  1.00 12.61 ? 181 PHE A CD1 1 
ATOM   3682 C  CD2 . PHE B 1 181 ? -33.062 -20.921 24.963  1.00 13.64 ? 181 PHE A CD2 1 
ATOM   3683 C  CE1 . PHE B 1 181 ? -32.290 -20.575 27.578  1.00 12.81 ? 181 PHE A CE1 1 
ATOM   3684 C  CE2 . PHE B 1 181 ? -32.717 -22.031 25.753  1.00 15.25 ? 181 PHE A CE2 1 
ATOM   3685 C  CZ  . PHE B 1 181 ? -32.313 -21.832 27.045  1.00 12.41 ? 181 PHE A CZ  1 
ATOM   3686 N  N   . ASP B 1 182 ? -30.391 -17.217 25.548  1.00 12.79 ? 182 ASP A N   1 
ATOM   3687 C  CA  . ASP B 1 182 ? -28.946 -17.547 25.429  1.00 12.40 ? 182 ASP A CA  1 
ATOM   3688 C  C   . ASP B 1 182 ? -28.652 -18.995 25.886  1.00 12.76 ? 182 ASP A C   1 
ATOM   3689 O  O   . ASP B 1 182 ? -28.271 -19.230 27.020  1.00 14.82 ? 182 ASP A O   1 
ATOM   3690 C  CB  . ASP B 1 182 ? -28.214 -16.561 26.308  1.00 13.14 ? 182 ASP A CB  1 
ATOM   3691 C  CG  . ASP B 1 182 ? -26.713 -16.732 26.275  1.00 13.58 ? 182 ASP A CG  1 
ATOM   3692 O  OD1 . ASP B 1 182 ? -26.211 -17.570 25.500  1.00 15.39 ? 182 ASP A OD1 1 
ATOM   3693 O  OD2 . ASP B 1 182 ? -26.031 -16.011 27.033  1.00 18.84 ? 182 ASP A OD2 1 
ATOM   3694 N  N   . LEU B 1 183 ? -28.859 -19.918 24.952  1.00 12.25 ? 183 LEU A N   1 
ATOM   3695 C  CA  . LEU B 1 183 ? -28.576 -21.353 25.227  1.00 11.63 ? 183 LEU A CA  1 
ATOM   3696 C  C   . LEU B 1 183 ? -27.108 -21.612 25.387  1.00 11.99 ? 183 LEU A C   1 
ATOM   3697 O  O   . LEU B 1 183 ? -26.639 -22.439 26.229  1.00 12.77 ? 183 LEU A O   1 
ATOM   3698 C  CB  . LEU B 1 183 ? -29.170 -22.146 24.057  1.00 12.94 ? 183 LEU A CB  1 
ATOM   3699 C  CG  . LEU B 1 183 ? -28.897 -23.684 24.158  1.00 13.49 ? 183 LEU A CG  1 
ATOM   3700 C  CD1 . LEU B 1 183 ? -29.450 -24.293 25.424  1.00 15.57 ? 183 LEU A CD1 1 
ATOM   3701 C  CD2 . LEU B 1 183 ? -29.567 -24.327 22.928  1.00 14.55 ? 183 LEU A CD2 1 
ATOM   3702 N  N   . LEU B 1 184 ? -26.247 -20.897 24.664  1.00 13.56 ? 184 LEU A N   1 
ATOM   3703 C  CA  . LEU B 1 184 ? -24.863 -21.195 24.638  1.00 13.98 ? 184 LEU A CA  1 
ATOM   3704 C  C   . LEU B 1 184 ? -24.312 -21.028 26.018  1.00 12.71 ? 184 LEU A C   1 
ATOM   3705 O  O   . LEU B 1 184 ? -23.530 -21.821 26.445  1.00 16.27 ? 184 LEU A O   1 
ATOM   3706 C  CB  . LEU B 1 184 ? -24.239 -20.200 23.639  1.00 15.83 ? 184 LEU A CB  1 
ATOM   3707 C  CG  . LEU B 1 184 ? -22.805 -20.549 23.413  1.00 18.01 ? 184 LEU A CG  1 
ATOM   3708 C  CD1 . LEU B 1 184 ? -22.541 -21.841 22.636  1.00 20.90 ? 184 LEU A CD1 1 
ATOM   3709 C  CD2 . LEU B 1 184 ? -22.202 -19.361 22.608  1.00 18.31 ? 184 LEU A CD2 1 
ATOM   3710 N  N   A SER B 1 185 ? -24.787 -20.018 26.808  0.50 13.33 ? 185 SER A N   1 
ATOM   3711 N  N   B SER B 1 185 ? -24.807 -20.024 26.784  0.50 14.54 ? 185 SER A N   1 
ATOM   3712 C  CA  A SER B 1 185 ? -24.282 -19.790 28.180  0.50 14.29 ? 185 SER A CA  1 
ATOM   3713 C  CA  B SER B 1 185 ? -24.305 -19.780 28.120  0.50 16.22 ? 185 SER A CA  1 
ATOM   3714 C  C   A SER B 1 185 ? -24.822 -20.775 29.232  0.50 14.73 ? 185 SER A C   1 
ATOM   3715 C  C   B SER B 1 185 ? -24.724 -20.822 29.142  0.50 15.63 ? 185 SER A C   1 
ATOM   3716 O  O   A SER B 1 185 ? -24.417 -20.719 30.412  0.50 17.56 ? 185 SER A O   1 
ATOM   3717 O  O   B SER B 1 185 ? -24.144 -20.825 30.230  0.50 16.79 ? 185 SER A O   1 
ATOM   3718 C  CB  A SER B 1 185 ? -24.522 -18.341 28.686  0.50 14.05 ? 185 SER A CB  1 
ATOM   3719 C  CB  B SER B 1 185 ? -24.797 -18.451 28.681  0.50 17.74 ? 185 SER A CB  1 
ATOM   3720 O  OG  A SER B 1 185 ? -23.979 -17.383 27.714  0.50 12.20 ? 185 SER A OG  1 
ATOM   3721 O  OG  B SER B 1 185 ? -26.116 -18.589 29.157  0.50 24.72 ? 185 SER A OG  1 
ATOM   3722 N  N   . LEU B 1 186 ? -25.701 -21.692 28.824  1.00 14.46 ? 186 LEU A N   1 
ATOM   3723 C  CA  . LEU B 1 186 ? -26.106 -22.756 29.713  1.00 14.63 ? 186 LEU A CA  1 
ATOM   3724 C  C   . LEU B 1 186 ? -25.139 -23.862 29.642  1.00 17.47 ? 186 LEU A C   1 
ATOM   3725 O  O   . LEU B 1 186 ? -24.998 -24.488 30.678  1.00 21.82 ? 186 LEU A O   1 
ATOM   3726 C  CB  . LEU B 1 186 ? -27.495 -23.276 29.393  1.00 17.50 ? 186 LEU A CB  1 
ATOM   3727 C  CG  . LEU B 1 186 ? -28.581 -22.632 30.212  1.00 21.58 ? 186 LEU A CG  1 
ATOM   3728 C  CD1 . LEU B 1 186 ? -29.844 -23.271 29.595  1.00 21.24 ? 186 LEU A CD1 1 
ATOM   3729 C  CD2 . LEU B 1 186 ? -28.473 -22.999 31.729  1.00 20.01 ? 186 LEU A CD2 1 
ATOM   3730 N  N   . LEU B 1 187 ? -24.288 -24.043 28.615  1.00 13.52 ? 187 LEU A N   1 
ATOM   3731 C  CA  . LEU B 1 187 ? -23.268 -25.009 28.481  1.00 13.33 ? 187 LEU A CA  1 
ATOM   3732 C  C   . LEU B 1 187 ? -22.066 -24.737 29.375  1.00 13.83 ? 187 LEU A C   1 
ATOM   3733 O  O   . LEU B 1 187 ? -21.708 -23.620 29.678  1.00 14.11 ? 187 LEU A O   1 
ATOM   3734 C  CB  . LEU B 1 187 ? -22.748 -25.160 27.014  1.00 14.09 ? 187 LEU A CB  1 
ATOM   3735 C  CG  . LEU B 1 187 ? -23.935 -25.331 26.054  1.00 17.54 ? 187 LEU A CG  1 
ATOM   3736 C  CD1 . LEU B 1 187 ? -23.281 -25.333 24.668  1.00 18.36 ? 187 LEU A CD1 1 
ATOM   3737 C  CD2 . LEU B 1 187 ? -24.722 -26.601 26.249  1.00 20.02 ? 187 LEU A CD2 1 
ATOM   3738 N  N   . PRO B 1 188 ? -21.434 -25.827 29.901  1.00 14.01 ? 188 PRO A N   1 
ATOM   3739 C  CA  . PRO B 1 188 ? -20.252 -25.640 30.731  1.00 13.14 ? 188 PRO A CA  1 
ATOM   3740 C  C   . PRO B 1 188 ? -19.084 -25.059 29.945  1.00 13.10 ? 188 PRO A C   1 
ATOM   3741 O  O   . PRO B 1 188 ? -19.070 -25.132 28.694  1.00 13.14 ? 188 PRO A O   1 
ATOM   3742 C  CB  . PRO B 1 188 ? -19.913 -27.076 31.211  1.00 13.94 ? 188 PRO A CB  1 
ATOM   3743 C  CG  . PRO B 1 188 ? -20.365 -27.933 30.092  1.00 12.78 ? 188 PRO A CG  1 
ATOM   3744 C  CD  . PRO B 1 188 ? -21.668 -27.296 29.656  1.00 13.05 ? 188 PRO A CD  1 
ATOM   3745 N  N   . PRO B 1 189 ? -18.031 -24.615 30.650  1.00 13.57 ? 189 PRO A N   1 
ATOM   3746 C  CA  . PRO B 1 189 ? -16.838 -24.011 29.921  1.00 13.16 ? 189 PRO A CA  1 
ATOM   3747 C  C   . PRO B 1 189 ? -16.145 -25.081 29.093  1.00 13.57 ? 189 PRO A C   1 
ATOM   3748 O  O   . PRO B 1 189 ? -15.789 -24.787 27.956  1.00 14.55 ? 189 PRO A O   1 
ATOM   3749 C  CB  . PRO B 1 189 ? -15.913 -23.480 31.036  1.00 15.43 ? 189 PRO A CB  1 
ATOM   3750 C  CG  . PRO B 1 189 ? -16.897 -23.294 32.188  1.00 16.95 ? 189 PRO A CG  1 
ATOM   3751 C  CD  . PRO B 1 189 ? -18.028 -24.297 32.103  1.00 14.93 ? 189 PRO A CD  1 
ATOM   3752 N  N   . SER B 1 190 ? -15.927 -26.311 29.609  1.00 12.31 ? 190 SER A N   1 
ATOM   3753 C  CA  . SER B 1 190 ? -15.330 -27.332 28.751  1.00 11.35 ? 190 SER A CA  1 
ATOM   3754 C  C   . SER B 1 190 ? -16.421 -28.150 28.018  1.00 11.98 ? 190 SER A C   1 
ATOM   3755 O  O   . SER B 1 190 ? -17.437 -28.518 28.642  1.00 12.06 ? 190 SER A O   1 
ATOM   3756 C  CB  . SER B 1 190 ? -14.622 -28.339 29.675  1.00 13.10 ? 190 SER A CB  1 
ATOM   3757 O  OG  . SER B 1 190 ? -14.151 -29.409 28.893  1.00 13.72 ? 190 SER A OG  1 
ATOM   3758 N  N   . TRP B 1 191 ? -16.190 -28.401 26.746  1.00 11.76 ? 191 TRP A N   1 
ATOM   3759 C  CA  . TRP B 1 191 ? -17.116 -29.172 25.926  1.00 12.35 ? 191 TRP A CA  1 
ATOM   3760 C  C   . TRP B 1 191 ? -16.566 -30.564 25.658  1.00 12.98 ? 191 TRP A C   1 
ATOM   3761 O  O   . TRP B 1 191 ? -17.013 -31.266 24.755  1.00 13.95 ? 191 TRP A O   1 
ATOM   3762 C  CB  . TRP B 1 191 ? -17.439 -28.447 24.606  1.00 14.00 ? 191 TRP A CB  1 
ATOM   3763 C  CG  . TRP B 1 191 ? -18.164 -27.174 24.827  1.00 10.70 ? 191 TRP A CG  1 
ATOM   3764 C  CD1 . TRP B 1 191 ? -18.638 -26.623 25.973  1.00 12.42 ? 191 TRP A CD1 1 
ATOM   3765 C  CD2 . TRP B 1 191 ? -18.413 -26.181 23.804  1.00 10.68 ? 191 TRP A CD2 1 
ATOM   3766 N  NE1 . TRP B 1 191 ? -19.175 -25.380 25.757  1.00 12.36 ? 191 TRP A NE1 1 
ATOM   3767 C  CE2 . TRP B 1 191 ? -19.018 -25.081 24.431  1.00 11.65 ? 191 TRP A CE2 1 
ATOM   3768 C  CE3 . TRP B 1 191 ? -18.178 -26.145 22.445  1.00 11.37 ? 191 TRP A CE3 1 
ATOM   3769 C  CZ2 . TRP B 1 191 ? -19.413 -23.941 23.711  1.00 11.33 ? 191 TRP A CZ2 1 
ATOM   3770 C  CZ3 . TRP B 1 191 ? -18.515 -24.948 21.724  1.00 11.75 ? 191 TRP A CZ3 1 
ATOM   3771 C  CH2 . TRP B 1 191 ? -19.163 -23.928 22.340  1.00 13.01 ? 191 TRP A CH2 1 
ATOM   3772 N  N   . ASP B 1 192 ? -15.612 -31.019 26.489  1.00 11.19 ? 192 ASP A N   1 
ATOM   3773 C  CA  . ASP B 1 192 ? -15.199 -32.436 26.334  1.00 13.08 ? 192 ASP A CA  1 
ATOM   3774 C  C   . ASP B 1 192 ? -16.407 -33.384 26.520  1.00 11.21 ? 192 ASP A C   1 
ATOM   3775 O  O   . ASP B 1 192 ? -17.279 -33.107 27.374  1.00 10.89 ? 192 ASP A O   1 
ATOM   3776 C  CB  . ASP B 1 192 ? -14.211 -32.786 27.489  1.00 14.34 ? 192 ASP A CB  1 
ATOM   3777 C  CG  . ASP B 1 192 ? -12.768 -32.191 27.274  1.00 17.84 ? 192 ASP A CG  1 
ATOM   3778 O  OD1 . ASP B 1 192 ? -12.520 -31.725 26.192  1.00 18.02 ? 192 ASP A OD1 1 
ATOM   3779 O  OD2 . ASP B 1 192 ? -12.041 -32.187 28.279  1.00 20.46 ? 192 ASP A OD2 1 
ATOM   3780 N  N   . TYR B 1 193 ? -16.440 -34.436 25.719  1.00 9.66  ? 193 TYR A N   1 
ATOM   3781 C  CA  . TYR B 1 193 ? -17.620 -35.314 25.717  1.00 10.23 ? 193 TYR A CA  1 
ATOM   3782 C  C   . TYR B 1 193 ? -17.362 -36.763 25.417  1.00 10.86 ? 193 TYR A C   1 
ATOM   3783 O  O   . TYR B 1 193 ? -16.278 -37.139 24.984  1.00 11.10 ? 193 TYR A O   1 
ATOM   3784 C  CB  . TYR B 1 193 ? -18.625 -34.730 24.652  1.00 11.48 ? 193 TYR A CB  1 
ATOM   3785 C  CG  . TYR B 1 193 ? -18.086 -34.828 23.254  1.00 10.52 ? 193 TYR A CG  1 
ATOM   3786 C  CD1 . TYR B 1 193 ? -18.215 -35.991 22.498  1.00 10.76 ? 193 TYR A CD1 1 
ATOM   3787 C  CD2 . TYR B 1 193 ? -17.399 -33.761 22.710  1.00 11.20 ? 193 TYR A CD2 1 
ATOM   3788 C  CE1 . TYR B 1 193 ? -17.677 -36.065 21.221  1.00 12.16 ? 193 TYR A CE1 1 
ATOM   3789 C  CE2 . TYR B 1 193 ? -16.865 -33.826 21.453  1.00 11.68 ? 193 TYR A CE2 1 
ATOM   3790 C  CZ  . TYR B 1 193 ? -17.005 -34.978 20.708  1.00 10.66 ? 193 TYR A CZ  1 
ATOM   3791 O  OH  . TYR B 1 193 ? -16.471 -35.052 19.442  1.00 13.70 ? 193 TYR A OH  1 
ATOM   3792 N  N   . TRP B 1 194 ? -18.389 -37.566 25.733  1.00 10.03 ? 194 TRP A N   1 
ATOM   3793 C  CA  . TRP B 1 194 ? -18.456 -38.903 25.276  1.00 10.12 ? 194 TRP A CA  1 
ATOM   3794 C  C   . TRP B 1 194 ? -19.495 -39.060 24.162  1.00 9.92  ? 194 TRP A C   1 
ATOM   3795 O  O   . TRP B 1 194 ? -20.521 -38.316 24.201  1.00 10.42 ? 194 TRP A O   1 
ATOM   3796 C  CB  . TRP B 1 194 ? -18.893 -39.875 26.427  1.00 11.58 ? 194 TRP A CB  1 
ATOM   3797 C  CG  . TRP B 1 194 ? -17.907 -39.896 27.575  1.00 11.34 ? 194 TRP A CG  1 
ATOM   3798 C  CD1 . TRP B 1 194 ? -16.667 -40.563 27.611  1.00 12.94 ? 194 TRP A CD1 1 
ATOM   3799 C  CD2 . TRP B 1 194 ? -18.069 -39.222 28.836  1.00 11.29 ? 194 TRP A CD2 1 
ATOM   3800 N  NE1 . TRP B 1 194 ? -16.067 -40.294 28.813  1.00 13.03 ? 194 TRP A NE1 1 
ATOM   3801 C  CE2 . TRP B 1 194 ? -16.868 -39.500 29.596  1.00 12.21 ? 194 TRP A CE2 1 
ATOM   3802 C  CE3 . TRP B 1 194 ? -19.089 -38.438 29.427  1.00 11.05 ? 194 TRP A CE3 1 
ATOM   3803 C  CZ2 . TRP B 1 194 ? -16.719 -39.009 30.901  1.00 13.36 ? 194 TRP A CZ2 1 
ATOM   3804 C  CZ3 . TRP B 1 194 ? -18.940 -37.981 30.702  1.00 12.42 ? 194 TRP A CZ3 1 
ATOM   3805 C  CH2 . TRP B 1 194 ? -17.742 -38.262 31.435  1.00 14.49 ? 194 TRP A CH2 1 
ATOM   3806 N  N   . THR B 1 195 ? -19.347 -40.018 23.264  1.00 10.77 ? 195 THR A N   1 
ATOM   3807 C  CA  . THR B 1 195 ? -20.327 -40.143 22.219  1.00 11.57 ? 195 THR A CA  1 
ATOM   3808 C  C   . THR B 1 195 ? -20.598 -41.550 21.905  1.00 10.84 ? 195 THR A C   1 
ATOM   3809 O  O   . THR B 1 195 ? -19.674 -42.436 22.023  1.00 11.59 ? 195 THR A O   1 
ATOM   3810 C  CB  . THR B 1 195 ? -19.920 -39.329 20.953  1.00 13.24 ? 195 THR A CB  1 
ATOM   3811 O  OG1 . THR B 1 195 ? -20.973 -39.459 19.962  1.00 11.59 ? 195 THR A OG1 1 
ATOM   3812 C  CG2 . THR B 1 195 ? -18.546 -39.819 20.289  1.00 13.11 ? 195 THR A CG2 1 
ATOM   3813 N  N   . TYR B 1 196 ? -21.817 -41.951 21.580  1.00 11.24 ? 196 TYR A N   1 
ATOM   3814 C  CA  . TYR B 1 196 ? -22.218 -43.307 21.312  1.00 10.49 ? 196 TYR A CA  1 
ATOM   3815 C  C   . TYR B 1 196 ? -23.525 -43.282 20.558  1.00 12.07 ? 196 TYR A C   1 
ATOM   3816 O  O   . TYR B 1 196 ? -24.247 -42.268 20.622  1.00 10.58 ? 196 TYR A O   1 
ATOM   3817 C  CB  . TYR B 1 196 ? -22.317 -44.147 22.594  1.00 12.03 ? 196 TYR A CB  1 
ATOM   3818 C  CG  . TYR B 1 196 ? -23.579 -43.801 23.415  1.00 9.72  ? 196 TYR A CG  1 
ATOM   3819 C  CD1 . TYR B 1 196 ? -23.580 -42.753 24.301  1.00 9.12  ? 196 TYR A CD1 1 
ATOM   3820 C  CD2 . TYR B 1 196 ? -24.774 -44.553 23.256  1.00 10.01 ? 196 TYR A CD2 1 
ATOM   3821 C  CE1 . TYR B 1 196 ? -24.752 -42.361 24.975  1.00 9.63  ? 196 TYR A CE1 1 
ATOM   3822 C  CE2 . TYR B 1 196 ? -25.954 -44.252 23.951  1.00 9.58  ? 196 TYR A CE2 1 
ATOM   3823 C  CZ  . TYR B 1 196 ? -25.917 -43.119 24.845  1.00 8.87  ? 196 TYR A CZ  1 
ATOM   3824 O  OH  . TYR B 1 196 ? -27.108 -42.872 25.468  1.00 10.20 ? 196 TYR A OH  1 
ATOM   3825 N  N   . PRO B 1 197 ? -23.912 -44.335 19.855  1.00 11.14 ? 197 PRO A N   1 
ATOM   3826 C  CA  . PRO B 1 197 ? -25.206 -44.389 19.079  1.00 11.13 ? 197 PRO A CA  1 
ATOM   3827 C  C   . PRO B 1 197 ? -26.272 -44.868 19.991  1.00 10.44 ? 197 PRO A C   1 
ATOM   3828 O  O   . PRO B 1 197 ? -26.093 -45.903 20.726  1.00 10.96 ? 197 PRO A O   1 
ATOM   3829 C  CB  . PRO B 1 197 ? -24.854 -45.429 17.977  1.00 11.90 ? 197 PRO A CB  1 
ATOM   3830 C  CG  . PRO B 1 197 ? -23.861 -46.399 18.648  1.00 12.71 ? 197 PRO A CG  1 
ATOM   3831 C  CD  . PRO B 1 197 ? -23.037 -45.501 19.539  1.00 12.10 ? 197 PRO A CD  1 
ATOM   3832 N  N   . GLY B 1 198 ? -27.404 -44.147 20.050  1.00 10.18 ? 198 GLY A N   1 
ATOM   3833 C  CA  . GLY B 1 198 ? -28.466 -44.565 20.895  1.00 10.19 ? 198 GLY A CA  1 
ATOM   3834 C  C   . GLY B 1 198 ? -29.809 -44.093 20.433  1.00 9.85  ? 198 GLY A C   1 
ATOM   3835 O  O   . GLY B 1 198 ? -30.139 -44.094 19.228  1.00 10.98 ? 198 GLY A O   1 
ATOM   3836 N  N   . SER B 1 199 ? -30.665 -43.730 21.391  1.00 9.57  ? 199 SER A N   1 
ATOM   3837 C  CA  . SER B 1 199 ? -32.095 -43.616 21.084  1.00 9.56  ? 199 SER A CA  1 
ATOM   3838 C  C   . SER B 1 199 ? -32.682 -42.369 21.776  1.00 8.09  ? 199 SER A C   1 
ATOM   3839 O  O   . SER B 1 199 ? -32.082 -41.744 22.680  1.00 9.36  ? 199 SER A O   1 
ATOM   3840 C  CB  . SER B 1 199 ? -32.939 -44.801 21.574  1.00 9.92  ? 199 SER A CB  1 
ATOM   3841 O  OG  . SER B 1 199 ? -33.063 -44.820 23.024  1.00 9.66  ? 199 SER A OG  1 
ATOM   3842 N  N   . LEU B 1 200 ? -33.926 -42.020 21.434  1.00 8.55  ? 200 LEU A N   1 
ATOM   3843 C  CA  . LEU B 1 200 ? -34.730 -41.146 22.306  1.00 8.99  ? 200 LEU A CA  1 
ATOM   3844 C  C   . LEU B 1 200 ? -34.832 -41.851 23.651  1.00 8.39  ? 200 LEU A C   1 
ATOM   3845 O  O   . LEU B 1 200 ? -34.977 -43.065 23.752  1.00 9.62  ? 200 LEU A O   1 
ATOM   3846 C  CB  . LEU B 1 200 ? -36.150 -41.049 21.774  1.00 11.23 ? 200 LEU A CB  1 
ATOM   3847 C  CG  . LEU B 1 200 ? -36.493 -39.907 20.823  1.00 15.12 ? 200 LEU A CG  1 
ATOM   3848 C  CD1 . LEU B 1 200 ? -35.684 -40.003 19.611  1.00 16.05 ? 200 LEU A CD1 1 
ATOM   3849 C  CD2 . LEU B 1 200 ? -37.929 -39.989 20.317  1.00 16.07 ? 200 LEU A CD2 1 
ATOM   3850 N  N   . THR B 1 201 ? -34.879 -41.028 24.703  1.00 8.43  ? 201 THR A N   1 
ATOM   3851 C  CA  . THR B 1 201 ? -35.079 -41.601 26.066  1.00 8.71  ? 201 THR A CA  1 
ATOM   3852 C  C   . THR B 1 201 ? -36.518 -41.555 26.471  1.00 8.74  ? 201 THR A C   1 
ATOM   3853 O  O   . THR B 1 201 ? -36.777 -41.928 27.664  1.00 9.83  ? 201 THR A O   1 
ATOM   3854 C  CB  . THR B 1 201 ? -34.153 -40.930 27.091  1.00 8.88  ? 201 THR A CB  1 
ATOM   3855 O  OG1 . THR B 1 201 ? -34.634 -39.609 27.348  1.00 8.86  ? 201 THR A OG1 1 
ATOM   3856 C  CG2 . THR B 1 201 ? -32.729 -40.931 26.631  1.00 9.56  ? 201 THR A CG2 1 
ATOM   3857 N  N   . VAL B 1 202 ? -37.443 -41.148 25.595  1.00 9.54  ? 202 VAL A N   1 
ATOM   3858 C  CA  . VAL B 1 202 ? -38.864 -41.182 25.839  1.00 11.18 ? 202 VAL A CA  1 
ATOM   3859 C  C   . VAL B 1 202 ? -39.514 -41.916 24.715  1.00 11.57 ? 202 VAL A C   1 
ATOM   3860 O  O   . VAL B 1 202 ? -38.952 -41.864 23.584  1.00 10.79 ? 202 VAL A O   1 
ATOM   3861 C  CB  . VAL B 1 202 ? -39.495 -39.778 25.906  1.00 9.64  ? 202 VAL A CB  1 
ATOM   3862 C  CG1 . VAL B 1 202 ? -38.903 -39.020 27.095  1.00 12.55 ? 202 VAL A CG1 1 
ATOM   3863 C  CG2 . VAL B 1 202 ? -39.232 -38.957 24.692  1.00 10.71 ? 202 VAL A CG2 1 
ATOM   3864 N  N   . PRO B 1 203 ? -40.674 -42.502 24.929  1.00 11.24 ? 203 PRO A N   1 
ATOM   3865 C  CA  . PRO B 1 203 ? -41.485 -42.990 23.759  1.00 11.66 ? 203 PRO A CA  1 
ATOM   3866 C  C   . PRO B 1 203 ? -41.550 -41.902 22.690  1.00 11.41 ? 203 PRO A C   1 
ATOM   3867 O  O   . PRO B 1 203 ? -41.816 -40.764 22.951  1.00 12.01 ? 203 PRO A O   1 
ATOM   3868 C  CB  . PRO B 1 203 ? -42.831 -43.258 24.403  1.00 12.15 ? 203 PRO A CB  1 
ATOM   3869 C  CG  . PRO B 1 203 ? -42.457 -43.694 25.828  1.00 12.48 ? 203 PRO A CG  1 
ATOM   3870 C  CD  . PRO B 1 203 ? -41.364 -42.698 26.229  1.00 11.40 ? 203 PRO A CD  1 
ATOM   3871 N  N   . PRO B 1 204 ? -41.306 -42.294 21.401  1.00 12.31 ? 204 PRO A N   1 
ATOM   3872 C  CA  . PRO B 1 204 ? -41.242 -43.655 20.885  1.00 12.98 ? 204 PRO A CA  1 
ATOM   3873 C  C   . PRO B 1 204 ? -39.894 -44.350 20.928  1.00 13.29 ? 204 PRO A C   1 
ATOM   3874 O  O   . PRO B 1 204 ? -39.804 -45.485 20.386  1.00 14.08 ? 204 PRO A O   1 
ATOM   3875 C  CB  . PRO B 1 204 ? -41.804 -43.397 19.402  1.00 13.24 ? 204 PRO A CB  1 
ATOM   3876 C  CG  . PRO B 1 204 ? -41.238 -42.038 19.025  1.00 15.03 ? 204 PRO A CG  1 
ATOM   3877 C  CD  . PRO B 1 204 ? -41.506 -41.270 20.372  1.00 12.44 ? 204 PRO A CD  1 
ATOM   3878 N  N   . LEU B 1 205 ? -38.900 -43.796 21.636  1.00 11.63 ? 205 LEU A N   1 
ATOM   3879 C  CA  . LEU B 1 205 ? -37.697 -44.509 21.861  1.00 11.74 ? 205 LEU A CA  1 
ATOM   3880 C  C   . LEU B 1 205 ? -36.911 -44.940 20.611  1.00 10.96 ? 205 LEU A C   1 
ATOM   3881 O  O   . LEU B 1 205 ? -36.080 -45.893 20.611  1.00 10.75 ? 205 LEU A O   1 
ATOM   3882 C  CB  . LEU B 1 205 ? -37.979 -45.792 22.690  1.00 12.02 ? 205 LEU A CB  1 
ATOM   3883 C  CG  . LEU B 1 205 ? -38.596 -45.475 24.128  1.00 12.33 ? 205 LEU A CG  1 
ATOM   3884 C  CD1 . LEU B 1 205 ? -39.110 -46.766 24.841  1.00 14.39 ? 205 LEU A CD1 1 
ATOM   3885 C  CD2 . LEU B 1 205 ? -37.598 -44.793 25.056  1.00 12.34 ? 205 LEU A CD2 1 
ATOM   3886 N  N   . LEU B 1 206 ? -37.098 -44.108 19.588  1.00 10.68 ? 206 LEU A N   1 
ATOM   3887 C  CA  . LEU B 1 206 ? -36.441 -44.446 18.263  1.00 10.67 ? 206 LEU A CA  1 
ATOM   3888 C  C   . LEU B 1 206 ? -34.953 -44.429 18.383  1.00 10.48 ? 206 LEU A C   1 
ATOM   3889 O  O   . LEU B 1 206 ? -34.334 -43.512 18.952  1.00 10.59 ? 206 LEU A O   1 
ATOM   3890 C  CB  . LEU B 1 206 ? -36.937 -43.426 17.219  1.00 11.75 ? 206 LEU A CB  1 
ATOM   3891 C  CG  . LEU B 1 206 ? -38.487 -43.514 17.015  1.00 11.79 ? 206 LEU A CG  1 
ATOM   3892 C  CD1 . LEU B 1 206 ? -38.980 -42.271 16.219  1.00 13.71 ? 206 LEU A CD1 1 
ATOM   3893 C  CD2 . LEU B 1 206 ? -38.838 -44.781 16.243  1.00 16.44 ? 206 LEU A CD2 1 
ATOM   3894 N  N   . GLU B 1 207 ? -34.310 -45.383 17.689  1.00 11.52 ? 207 GLU A N   1 
ATOM   3895 C  CA  . GLU B 1 207 ? -32.858 -45.561 17.657  1.00 10.67 ? 207 GLU A CA  1 
ATOM   3896 C  C   . GLU B 1 207 ? -32.259 -44.725 16.543  1.00 11.27 ? 207 GLU A C   1 
ATOM   3897 O  O   . GLU B 1 207 ? -31.704 -45.212 15.531  1.00 12.70 ? 207 GLU A O   1 
ATOM   3898 C  CB  . GLU B 1 207 ? -32.497 -47.052 17.629  1.00 10.64 ? 207 GLU A CB  1 
ATOM   3899 C  CG  . GLU B 1 207 ? -33.050 -47.724 18.892  1.00 12.11 ? 207 GLU A CG  1 
ATOM   3900 C  CD  . GLU B 1 207 ? -32.810 -49.193 19.034  1.00 11.80 ? 207 GLU A CD  1 
ATOM   3901 O  OE1 . GLU B 1 207 ? -32.658 -49.824 17.944  1.00 14.84 ? 207 GLU A OE1 1 
ATOM   3902 O  OE2 . GLU B 1 207 ? -32.682 -49.700 20.151  1.00 11.63 ? 207 GLU A OE2 1 
ATOM   3903 N  N   . SER B 1 208 ? -32.308 -43.425 16.711  1.00 10.44 ? 208 SER A N   1 
ATOM   3904 C  CA  . SER B 1 208 ? -31.914 -42.440 15.685  1.00 10.19 ? 208 SER A CA  1 
ATOM   3905 C  C   . SER B 1 208 ? -30.983 -41.353 16.197  1.00 10.39 ? 208 SER A C   1 
ATOM   3906 O  O   . SER B 1 208 ? -30.679 -40.341 15.508  1.00 11.50 ? 208 SER A O   1 
ATOM   3907 C  CB  . SER B 1 208 ? -33.179 -41.724 15.185  1.00 12.34 ? 208 SER A CB  1 
ATOM   3908 O  OG  . SER B 1 208 ? -33.872 -41.225 16.300  1.00 12.86 ? 208 SER A OG  1 
ATOM   3909 N  N   . VAL B 1 209 ? -30.412 -41.583 17.436  1.00 9.84  ? 209 VAL A N   1 
ATOM   3910 C  CA  . VAL B 1 209 ? -29.616 -40.501 18.069  1.00 10.24 ? 209 VAL A CA  1 
ATOM   3911 C  C   . VAL B 1 209 ? -28.153 -40.735 18.142  1.00 9.54  ? 209 VAL A C   1 
ATOM   3912 O  O   . VAL B 1 209 ? -27.709 -41.783 18.743  1.00 11.69 ? 209 VAL A O   1 
ATOM   3913 C  CB  . VAL B 1 209 ? -30.135 -40.235 19.542  1.00 9.71  ? 209 VAL A CB  1 
ATOM   3914 C  CG1 . VAL B 1 209 ? -29.432 -39.112 20.185  1.00 9.42  ? 209 VAL A CG1 1 
ATOM   3915 C  CG2 . VAL B 1 209 ? -31.628 -39.858 19.434  1.00 9.62  ? 209 VAL A CG2 1 
ATOM   3916 N  N   . THR B 1 210 ? -27.386 -39.783 17.703  1.00 9.12  ? 210 THR A N   1 
ATOM   3917 C  CA  . THR B 1 210 ? -25.942 -39.741 18.063  1.00 8.58  ? 210 THR A CA  1 
ATOM   3918 C  C   . THR B 1 210 ? -25.847 -38.894 19.293  1.00 10.60 ? 210 THR A C   1 
ATOM   3919 O  O   . THR B 1 210 ? -26.123 -37.644 19.282  1.00 9.85  ? 210 THR A O   1 
ATOM   3920 C  CB  . THR B 1 210 ? -25.118 -39.044 16.918  1.00 9.91  ? 210 THR A CB  1 
ATOM   3921 O  OG1 . THR B 1 210 ? -25.263 -39.844 15.749  1.00 10.45 ? 210 THR A OG1 1 
ATOM   3922 C  CG2 . THR B 1 210 ? -23.661 -38.952 17.301  1.00 9.84  ? 210 THR A CG2 1 
ATOM   3923 N  N   . TRP B 1 211 ? -25.511 -39.533 20.431  1.00 8.78  ? 211 TRP A N   1 
ATOM   3924 C  CA  . TRP B 1 211 ? -25.426 -38.835 21.739  1.00 8.69  ? 211 TRP A CA  1 
ATOM   3925 C  C   . TRP B 1 211 ? -24.105 -38.213 21.925  1.00 8.50  ? 211 TRP A C   1 
ATOM   3926 O  O   . TRP B 1 211 ? -23.038 -38.863 21.623  1.00 10.58 ? 211 TRP A O   1 
ATOM   3927 C  CB  . TRP B 1 211 ? -25.665 -39.856 22.870  1.00 8.23  ? 211 TRP A CB  1 
ATOM   3928 C  CG  . TRP B 1 211 ? -27.131 -40.026 23.124  1.00 7.98  ? 211 TRP A CG  1 
ATOM   3929 C  CD1 . TRP B 1 211 ? -27.999 -41.012 22.651  1.00 7.96  ? 211 TRP A CD1 1 
ATOM   3930 C  CD2 . TRP B 1 211 ? -27.948 -39.130 23.877  1.00 7.99  ? 211 TRP A CD2 1 
ATOM   3931 N  NE1 . TRP B 1 211 ? -29.325 -40.738 23.005  1.00 8.81  ? 211 TRP A NE1 1 
ATOM   3932 C  CE2 . TRP B 1 211 ? -29.312 -39.607 23.773  1.00 7.78  ? 211 TRP A CE2 1 
ATOM   3933 C  CE3 . TRP B 1 211 ? -27.713 -37.977 24.593  1.00 8.97  ? 211 TRP A CE3 1 
ATOM   3934 C  CZ2 . TRP B 1 211 ? -30.366 -38.946 24.361  1.00 7.98  ? 211 TRP A CZ2 1 
ATOM   3935 C  CZ3 . TRP B 1 211 ? -28.799 -37.299 25.161  1.00 8.12  ? 211 TRP A CZ3 1 
ATOM   3936 C  CH2 . TRP B 1 211 ? -30.112 -37.803 25.061  1.00 7.64  ? 211 TRP A CH2 1 
ATOM   3937 N  N   . ILE B 1 212 ? -24.078 -37.015 22.423  1.00 8.88  ? 212 ILE A N   1 
ATOM   3938 C  CA  . ILE B 1 212 ? -22.882 -36.262 22.805  1.00 9.10  ? 212 ILE A CA  1 
ATOM   3939 C  C   . ILE B 1 212 ? -23.024 -35.746 24.180  1.00 9.07  ? 212 ILE A C   1 
ATOM   3940 O  O   . ILE B 1 212 ? -23.777 -34.803 24.420  1.00 9.74  ? 212 ILE A O   1 
ATOM   3941 C  CB  . ILE B 1 212 ? -22.626 -35.081 21.786  1.00 8.99  ? 212 ILE A CB  1 
ATOM   3942 C  CG1 . ILE B 1 212 ? -22.549 -35.644 20.363  1.00 9.83  ? 212 ILE A CG1 1 
ATOM   3943 C  CG2 . ILE B 1 212 ? -21.452 -34.164 22.215  1.00 10.40 ? 212 ILE A CG2 1 
ATOM   3944 C  CD1 . ILE B 1 212 ? -22.694 -34.567 19.244  1.00 12.40 ? 212 ILE A CD1 1 
ATOM   3945 N  N   . VAL B 1 213 ? -22.459 -36.544 25.141  1.00 9.36  ? 213 VAL A N   1 
ATOM   3946 C  CA  . VAL B 1 213 ? -22.697 -36.272 26.553  1.00 9.70  ? 213 VAL A CA  1 
ATOM   3947 C  C   . VAL B 1 213 ? -21.482 -35.535 27.080  1.00 9.66  ? 213 VAL A C   1 
ATOM   3948 O  O   . VAL B 1 213 ? -20.382 -36.095 27.124  1.00 9.90  ? 213 VAL A O   1 
ATOM   3949 C  CB  . VAL B 1 213 ? -22.954 -37.606 27.298  1.00 10.02 ? 213 VAL A CB  1 
ATOM   3950 C  CG1 . VAL B 1 213 ? -23.154 -37.368 28.767  1.00 10.97 ? 213 VAL A CG1 1 
ATOM   3951 C  CG2 . VAL B 1 213 ? -24.227 -38.337 26.713  1.00 9.41  ? 213 VAL A CG2 1 
ATOM   3952 N  N   . LEU B 1 214 ? -21.708 -34.300 27.561  1.00 9.39  ? 214 LEU A N   1 
ATOM   3953 C  CA  . LEU B 1 214 ? -20.562 -33.486 28.074  1.00 10.16 ? 214 LEU A CA  1 
ATOM   3954 C  C   . LEU B 1 214 ? -20.128 -33.960 29.459  1.00 9.33  ? 214 LEU A C   1 
ATOM   3955 O  O   . LEU B 1 214 ? -20.978 -34.260 30.313  1.00 9.66  ? 214 LEU A O   1 
ATOM   3956 C  CB  . LEU B 1 214 ? -20.914 -32.003 28.090  1.00 10.78 ? 214 LEU A CB  1 
ATOM   3957 C  CG  . LEU B 1 214 ? -20.744 -31.316 26.707  1.00 13.69 ? 214 LEU A CG  1 
ATOM   3958 C  CD1 . LEU B 1 214 ? -21.440 -32.000 25.570  1.00 17.50 ? 214 LEU A CD1 1 
ATOM   3959 C  CD2 . LEU B 1 214 ? -21.028 -29.794 26.851  1.00 14.30 ? 214 LEU A CD2 1 
ATOM   3960 N  N   . LYS B 1 215 ? -18.820 -33.988 29.655  1.00 9.19  ? 215 LYS A N   1 
ATOM   3961 C  CA  . LYS B 1 215 ? -18.285 -34.448 30.963  1.00 9.79  ? 215 LYS A CA  1 
ATOM   3962 C  C   . LYS B 1 215 ? -18.520 -33.474 32.108  1.00 10.61 ? 215 LYS A C   1 
ATOM   3963 O  O   . LYS B 1 215 ? -18.818 -33.843 33.264  1.00 12.65 ? 215 LYS A O   1 
ATOM   3964 C  CB  . LYS B 1 215 ? -16.802 -34.700 30.762  1.00 11.83 ? 215 LYS A CB  1 
ATOM   3965 C  CG  . LYS B 1 215 ? -16.037 -35.004 32.094  1.00 14.70 ? 215 LYS A CG  1 
ATOM   3966 C  CD  . LYS B 1 215 ? -14.600 -35.419 31.813  1.00 17.92 ? 215 LYS A CD  1 
ATOM   3967 C  CE  . LYS B 1 215 ? -13.819 -35.527 33.109  1.00 24.68 ? 215 LYS A CE  1 
ATOM   3968 N  NZ  . LYS B 1 215 ? -12.436 -35.942 32.678  1.00 30.17 ? 215 LYS A NZ  1 
ATOM   3969 N  N   . GLN B 1 216 ? -18.366 -32.146 31.835  1.00 10.56 ? 216 GLN A N   1 
ATOM   3970 C  CA  . GLN B 1 216 ? -18.395 -31.178 32.902  1.00 10.22 ? 216 GLN A CA  1 
ATOM   3971 C  C   . GLN B 1 216 ? -19.819 -30.773 33.245  1.00 11.18 ? 216 GLN A C   1 
ATOM   3972 O  O   . GLN B 1 216 ? -20.517 -30.267 32.336  1.00 10.88 ? 216 GLN A O   1 
ATOM   3973 C  CB  . GLN B 1 216 ? -17.574 -29.917 32.527  1.00 11.61 ? 216 GLN A CB  1 
ATOM   3974 C  CG  . GLN B 1 216 ? -17.650 -28.848 33.667  1.00 13.20 ? 216 GLN A CG  1 
ATOM   3975 C  CD  . GLN B 1 216 ? -16.755 -27.672 33.476  1.00 16.43 ? 216 GLN A CD  1 
ATOM   3976 O  OE1 . GLN B 1 216 ? -16.235 -27.400 32.389  1.00 15.97 ? 216 GLN A OE1 1 
ATOM   3977 N  NE2 . GLN B 1 216 ? -16.614 -26.893 34.525  1.00 18.82 ? 216 GLN A NE2 1 
ATOM   3978 N  N   . PRO B 1 217 ? -20.304 -30.921 34.450  1.00 11.09 ? 217 PRO A N   1 
ATOM   3979 C  CA  . PRO B 1 217 ? -21.630 -30.463 34.812  1.00 11.38 ? 217 PRO A CA  1 
ATOM   3980 C  C   . PRO B 1 217 ? -21.730 -28.958 34.920  1.00 11.83 ? 217 PRO A C   1 
ATOM   3981 O  O   . PRO B 1 217 ? -20.679 -28.270 35.139  1.00 13.31 ? 217 PRO A O   1 
ATOM   3982 C  CB  . PRO B 1 217 ? -21.869 -31.081 36.213  1.00 11.81 ? 217 PRO A CB  1 
ATOM   3983 C  CG  . PRO B 1 217 ? -20.467 -31.273 36.724  1.00 17.35 ? 217 PRO A CG  1 
ATOM   3984 C  CD  . PRO B 1 217 ? -19.576 -31.583 35.557  1.00 11.70 ? 217 PRO A CD  1 
ATOM   3985 N  N   . ILE B 1 218 ? -22.942 -28.445 34.880  1.00 11.12 ? 218 ILE A N   1 
ATOM   3986 C  CA  . ILE B 1 218 ? -23.228 -27.065 35.266  1.00 11.92 ? 218 ILE A CA  1 
ATOM   3987 C  C   . ILE B 1 218 ? -23.935 -27.105 36.622  1.00 12.06 ? 218 ILE A C   1 
ATOM   3988 O  O   . ILE B 1 218 ? -24.413 -28.196 37.063  1.00 13.24 ? 218 ILE A O   1 
ATOM   3989 C  CB  . ILE B 1 218 ? -24.096 -26.296 34.220  1.00 11.69 ? 218 ILE A CB  1 
ATOM   3990 C  CG1 . ILE B 1 218 ? -25.472 -26.958 34.093  1.00 11.16 ? 218 ILE A CG1 1 
ATOM   3991 C  CG2 . ILE B 1 218 ? -23.358 -26.291 32.908  1.00 11.68 ? 218 ILE A CG2 1 
ATOM   3992 C  CD1 . ILE B 1 218 ? -26.415 -26.152 33.137  1.00 11.66 ? 218 ILE A CD1 1 
ATOM   3993 N  N   . ASN B 1 219 ? -24.108 -26.002 37.316  1.00 12.38 ? 219 ASN A N   1 
ATOM   3994 C  CA  . ASN B 1 219 ? -24.737 -25.954 38.624  1.00 11.35 ? 219 ASN A CA  1 
ATOM   3995 C  C   . ASN B 1 219 ? -26.190 -25.729 38.530  1.00 10.47 ? 219 ASN A C   1 
ATOM   3996 O  O   . ASN B 1 219 ? -26.690 -25.028 37.579  1.00 12.58 ? 219 ASN A O   1 
ATOM   3997 C  CB  . ASN B 1 219 ? -24.096 -24.826 39.443  1.00 14.98 ? 219 ASN A CB  1 
ATOM   3998 C  CG  . ASN B 1 219 ? -22.774 -25.186 39.977  1.00 22.68 ? 219 ASN A CG  1 
ATOM   3999 O  OD1 . ASN B 1 219 ? -22.395 -26.345 40.093  1.00 22.14 ? 219 ASN A OD1 1 
ATOM   4000 N  ND2 . ASN B 1 219 ? -22.114 -24.137 40.472  1.00 29.20 ? 219 ASN A ND2 1 
ATOM   4001 N  N   . ILE B 1 220 ? -26.950 -26.137 39.495  1.00 11.00 ? 220 ILE A N   1 
ATOM   4002 C  CA  . ILE B 1 220 ? -28.321 -25.694 39.769  1.00 11.79 ? 220 ILE A CA  1 
ATOM   4003 C  C   . ILE B 1 220 ? -28.506 -25.720 41.309  1.00 11.41 ? 220 ILE A C   1 
ATOM   4004 O  O   . ILE B 1 220 ? -28.010 -26.628 41.964  1.00 11.50 ? 220 ILE A O   1 
ATOM   4005 C  CB  . ILE B 1 220 ? -29.383 -26.614 39.038  1.00 10.68 ? 220 ILE A CB  1 
ATOM   4006 C  CG1 . ILE B 1 220 ? -30.762 -26.021 39.181  1.00 11.05 ? 220 ILE A CG1 1 
ATOM   4007 C  CG2 . ILE B 1 220 ? -29.286 -28.061 39.521  1.00 11.55 ? 220 ILE A CG2 1 
ATOM   4008 C  CD1 . ILE B 1 220 ? -31.802 -26.678 38.247  1.00 12.78 ? 220 ILE A CD1 1 
ATOM   4009 N  N   . SER B 1 221 ? -29.232 -24.755 41.842  1.00 11.66 ? 221 SER A N   1 
ATOM   4010 C  CA  . SER B 1 221 ? -29.504 -24.917 43.286  1.00 11.69 ? 221 SER A CA  1 
ATOM   4011 C  C   . SER B 1 221 ? -30.676 -25.817 43.561  1.00 13.16 ? 221 SER A C   1 
ATOM   4012 O  O   . SER B 1 221 ? -31.558 -26.046 42.693  1.00 12.20 ? 221 SER A O   1 
ATOM   4013 C  CB  . SER B 1 221 ? -29.817 -23.501 43.892  1.00 11.83 ? 221 SER A CB  1 
ATOM   4014 O  OG  . SER B 1 221 ? -31.088 -23.035 43.520  1.00 12.41 ? 221 SER A OG  1 
ATOM   4015 N  N   A SER B 1 222 ? -30.689 -26.315 44.789  0.50 12.94 ? 222 SER A N   1 
ATOM   4016 N  N   B SER B 1 222 ? -30.944 -26.301 44.786  0.50 11.46 ? 222 SER A N   1 
ATOM   4017 C  CA  A SER B 1 222 ? -31.810 -27.037 45.180  0.50 11.65 ? 222 SER A CA  1 
ATOM   4018 C  CA  B SER B 1 222 ? -32.154 -27.051 45.111  0.50 10.90 ? 222 SER A CA  1 
ATOM   4019 C  C   A SER B 1 222 ? -33.126 -26.333 44.972  0.50 12.28 ? 222 SER A C   1 
ATOM   4020 C  C   B SER B 1 222 ? -33.410 -26.283 44.947  0.50 12.17 ? 222 SER A C   1 
ATOM   4021 O  O   A SER B 1 222 ? -34.015 -26.949 44.480  0.50 12.03 ? 222 SER A O   1 
ATOM   4022 O  O   B SER B 1 222 ? -34.518 -26.748 44.547  0.50 8.95  ? 222 SER A O   1 
ATOM   4023 C  CB  A SER B 1 222 ? -31.714 -27.581 46.622  0.50 11.84 ? 222 SER A CB  1 
ATOM   4024 C  CB  B SER B 1 222 ? -32.058 -27.541 46.587  0.50 11.14 ? 222 SER A CB  1 
ATOM   4025 O  OG  A SER B 1 222 ? -32.973 -28.157 46.937  0.50 14.57 ? 222 SER A OG  1 
ATOM   4026 O  OG  B SER B 1 222 ? -30.931 -28.392 46.736  0.50 12.84 ? 222 SER A OG  1 
ATOM   4027 N  N   . GLN B 1 223 ? -33.293 -25.010 45.357  1.00 11.41 ? 223 GLN A N   1 
ATOM   4028 C  CA  . GLN B 1 223 ? -34.461 -24.239 45.194  1.00 11.73 ? 223 GLN A CA  1 
ATOM   4029 C  C   . GLN B 1 223 ? -34.869 -24.096 43.701  1.00 12.04 ? 223 GLN A C   1 
ATOM   4030 O  O   . GLN B 1 223 ? -36.051 -24.124 43.407  1.00 12.91 ? 223 GLN A O   1 
ATOM   4031 C  CB  . GLN B 1 223 ? -34.292 -22.776 45.773  1.00 13.17 ? 223 GLN A CB  1 
ATOM   4032 C  CG  . GLN B 1 223 ? -34.314 -22.776 47.295  1.00 16.34 ? 223 GLN A CG  1 
ATOM   4033 C  CD  . GLN B 1 223 ? -34.413 -21.335 47.838  1.00 17.04 ? 223 GLN A CD  1 
ATOM   4034 O  OE1 . GLN B 1 223 ? -35.157 -20.526 47.327  1.00 16.52 ? 223 GLN A OE1 1 
ATOM   4035 N  NE2 . GLN B 1 223 ? -33.640 -21.061 48.889  1.00 17.26 ? 223 GLN A NE2 1 
ATOM   4036 N  N   . GLN B 1 224 ? -33.847 -23.903 42.852  1.00 11.52 ? 224 GLN A N   1 
ATOM   4037 C  CA  . GLN B 1 224 ? -34.228 -23.810 41.383  1.00 12.92 ? 224 GLN A CA  1 
ATOM   4038 C  C   . GLN B 1 224 ? -34.786 -25.128 40.889  1.00 12.40 ? 224 GLN A C   1 
ATOM   4039 O  O   . GLN B 1 224 ? -35.818 -25.129 40.194  1.00 12.79 ? 224 GLN A O   1 
ATOM   4040 C  CB  . GLN B 1 224 ? -32.983 -23.457 40.574  1.00 11.78 ? 224 GLN A CB  1 
ATOM   4041 C  CG  . GLN B 1 224 ? -32.465 -22.064 40.710  1.00 13.24 ? 224 GLN A CG  1 
ATOM   4042 C  CD  . GLN B 1 224 ? -31.257 -21.812 39.882  1.00 11.54 ? 224 GLN A CD  1 
ATOM   4043 O  OE1 . GLN B 1 224 ? -30.252 -22.500 40.016  1.00 13.18 ? 224 GLN A OE1 1 
ATOM   4044 N  NE2 . GLN B 1 224 ? -31.336 -20.833 38.994  1.00 13.57 ? 224 GLN A NE2 1 
ATOM   4045 N  N   . LEU B 1 225 ? -34.126 -26.213 41.281  1.00 11.15 ? 225 LEU A N   1 
ATOM   4046 C  CA  . LEU B 1 225 ? -34.554 -27.515 40.731  1.00 12.80 ? 225 LEU A CA  1 
ATOM   4047 C  C   . LEU B 1 225 ? -35.960 -27.851 41.189  1.00 12.97 ? 225 LEU A C   1 
ATOM   4048 O  O   . LEU B 1 225 ? -36.812 -28.361 40.467  1.00 14.73 ? 225 LEU A O   1 
ATOM   4049 C  CB  . LEU B 1 225 ? -33.488 -28.620 41.077  1.00 13.88 ? 225 LEU A CB  1 
ATOM   4050 C  CG  . LEU B 1 225 ? -33.859 -30.000 40.495  1.00 14.34 ? 225 LEU A CG  1 
ATOM   4051 C  CD1 . LEU B 1 225 ? -34.048 -29.919 38.975  1.00 15.69 ? 225 LEU A CD1 1 
ATOM   4052 C  CD2 . LEU B 1 225 ? -32.711 -30.854 40.863  1.00 15.16 ? 225 LEU A CD2 1 
ATOM   4053 N  N   . ALA B 1 226 ? -36.323 -27.544 42.453  1.00 12.92 ? 226 ALA A N   1 
ATOM   4054 C  CA  . ALA B 1 226 ? -37.615 -27.807 42.967  1.00 12.80 ? 226 ALA A CA  1 
ATOM   4055 C  C   . ALA B 1 226 ? -38.757 -27.145 42.182  1.00 12.86 ? 226 ALA A C   1 
ATOM   4056 O  O   . ALA B 1 226 ? -39.841 -27.638 42.164  1.00 13.98 ? 226 ALA A O   1 
ATOM   4057 C  CB  . ALA B 1 226 ? -37.750 -27.384 44.502  1.00 14.75 ? 226 ALA A CB  1 
ATOM   4058 N  N   . LYS B 1 227 ? -38.528 -25.998 41.557  1.00 12.52 ? 227 LYS A N   1 
ATOM   4059 C  CA  . LYS B 1 227 ? -39.539 -25.345 40.755  1.00 12.10 ? 227 LYS A CA  1 
ATOM   4060 C  C   . LYS B 1 227 ? -39.963 -26.193 39.598  1.00 11.73 ? 227 LYS A C   1 
ATOM   4061 O  O   . LYS B 1 227 ? -41.115 -26.140 39.211  1.00 13.79 ? 227 LYS A O   1 
ATOM   4062 C  CB  . LYS B 1 227 ? -38.967 -24.050 40.250  1.00 14.64 ? 227 LYS A CB  1 
ATOM   4063 C  CG  . LYS B 1 227 ? -38.652 -23.048 41.404  1.00 17.66 ? 227 LYS A CG  1 
ATOM   4064 C  CD  . LYS B 1 227 ? -38.013 -21.748 40.962  1.00 23.33 ? 227 LYS A CD  1 
ATOM   4065 C  CE  . LYS B 1 227 ? -39.015 -20.660 40.552  1.00 29.33 ? 227 LYS A CE  1 
ATOM   4066 N  NZ  . LYS B 1 227 ? -38.303 -19.321 40.739  1.00 29.46 ? 227 LYS A NZ  1 
ATOM   4067 N  N   . PHE B 1 228 ? -39.039 -26.996 39.037  1.00 11.49 ? 228 PHE A N   1 
ATOM   4068 C  CA  . PHE B 1 228 ? -39.439 -27.846 37.863  1.00 11.51 ? 228 PHE A CA  1 
ATOM   4069 C  C   . PHE B 1 228 ? -40.437 -28.906 38.298  1.00 11.27 ? 228 PHE A C   1 
ATOM   4070 O  O   . PHE B 1 228 ? -41.343 -29.307 37.549  1.00 12.08 ? 228 PHE A O   1 
ATOM   4071 C  CB  . PHE B 1 228 ? -38.227 -28.460 37.204  1.00 11.20 ? 228 PHE A CB  1 
ATOM   4072 C  CG  . PHE B 1 228 ? -37.370 -27.433 36.551  1.00 10.75 ? 228 PHE A CG  1 
ATOM   4073 C  CD1 . PHE B 1 228 ? -36.249 -26.903 37.148  1.00 12.75 ? 228 PHE A CD1 1 
ATOM   4074 C  CD2 . PHE B 1 228 ? -37.777 -26.884 35.273  1.00 12.45 ? 228 PHE A CD2 1 
ATOM   4075 C  CE1 . PHE B 1 228 ? -35.495 -25.867 36.534  1.00 13.96 ? 228 PHE A CE1 1 
ATOM   4076 C  CE2 . PHE B 1 228 ? -37.001 -25.877 34.707  1.00 12.07 ? 228 PHE A CE2 1 
ATOM   4077 C  CZ  . PHE B 1 228 ? -35.882 -25.385 35.284  1.00 12.20 ? 228 PHE A CZ  1 
ATOM   4078 N  N   . ARG B 1 229 ? -40.288 -29.401 39.581  1.00 11.62 ? 229 ARG A N   1 
ATOM   4079 C  CA  . ARG B 1 229 ? -41.193 -30.447 40.109  1.00 12.68 ? 229 ARG A CA  1 
ATOM   4080 C  C   . ARG B 1 229 ? -42.576 -29.939 40.375  1.00 12.01 ? 229 ARG A C   1 
ATOM   4081 O  O   . ARG B 1 229 ? -43.449 -30.726 40.598  1.00 13.27 ? 229 ARG A O   1 
ATOM   4082 C  CB  . ARG B 1 229 ? -40.622 -31.092 41.379  1.00 12.78 ? 229 ARG A CB  1 
ATOM   4083 C  CG  . ARG B 1 229 ? -39.244 -31.557 41.209  1.00 11.92 ? 229 ARG A CG  1 
ATOM   4084 C  CD  . ARG B 1 229 ? -38.826 -32.464 42.432  1.00 12.73 ? 229 ARG A CD  1 
ATOM   4085 N  NE  . ARG B 1 229 ? -37.415 -32.833 42.341  1.00 12.07 ? 229 ARG A NE  1 
ATOM   4086 C  CZ  . ARG B 1 229 ? -36.439 -32.225 43.008  1.00 11.31 ? 229 ARG A CZ  1 
ATOM   4087 N  NH1 . ARG B 1 229 ? -36.721 -31.223 43.827  1.00 12.04 ? 229 ARG A NH1 1 
ATOM   4088 N  NH2 . ARG B 1 229 ? -35.182 -32.623 42.861  1.00 12.61 ? 229 ARG A NH2 1 
ATOM   4089 N  N   . SER B 1 230 ? -42.802 -28.618 40.326  1.00 13.79 ? 230 SER A N   1 
ATOM   4090 C  CA  . SER B 1 230 ? -44.117 -28.010 40.424  1.00 16.94 ? 230 SER A CA  1 
ATOM   4091 C  C   . SER B 1 230 ? -44.930 -28.005 39.131  1.00 15.85 ? 230 SER A C   1 
ATOM   4092 O  O   . SER B 1 230 ? -46.158 -27.684 39.088  1.00 16.79 ? 230 SER A O   1 
ATOM   4093 C  CB  . SER B 1 230 ? -44.079 -26.580 40.974  1.00 18.75 ? 230 SER A CB  1 
ATOM   4094 O  OG  . SER B 1 230 ? -43.732 -26.816 42.324  1.00 34.10 ? 230 SER A OG  1 
ATOM   4095 N  N   . LEU B 1 231 ? -44.274 -28.306 37.996  1.00 13.18 ? 231 LEU A N   1 
ATOM   4096 C  CA  . LEU B 1 231 ? -45.042 -28.514 36.799  1.00 13.26 ? 231 LEU A CA  1 
ATOM   4097 C  C   . LEU B 1 231 ? -45.973 -29.679 36.924  1.00 13.36 ? 231 LEU A C   1 
ATOM   4098 O  O   . LEU B 1 231 ? -45.638 -30.670 37.625  1.00 13.95 ? 231 LEU A O   1 
ATOM   4099 C  CB  . LEU B 1 231 ? -44.034 -28.784 35.592  1.00 13.66 ? 231 LEU A CB  1 
ATOM   4100 C  CG  . LEU B 1 231 ? -43.164 -27.640 35.178  1.00 11.16 ? 231 LEU A CG  1 
ATOM   4101 C  CD1 . LEU B 1 231 ? -42.082 -28.153 34.207  1.00 13.87 ? 231 LEU A CD1 1 
ATOM   4102 C  CD2 . LEU B 1 231 ? -44.045 -26.504 34.524  1.00 12.53 ? 231 LEU A CD2 1 
ATOM   4103 N  N   . LEU B 1 232 ? -47.130 -29.660 36.226  1.00 13.50 ? 232 LEU A N   1 
ATOM   4104 C  CA  . LEU B 1 232 ? -48.053 -30.783 36.174  1.00 13.42 ? 232 LEU A CA  1 
ATOM   4105 C  C   . LEU B 1 232 ? -47.854 -31.677 34.984  1.00 12.78 ? 232 LEU A C   1 
ATOM   4106 O  O   . LEU B 1 232 ? -47.466 -31.172 33.865  1.00 14.80 ? 232 LEU A O   1 
ATOM   4107 C  CB  . LEU B 1 232 ? -49.515 -30.340 36.230  1.00 15.09 ? 232 LEU A CB  1 
ATOM   4108 C  CG  . LEU B 1 232 ? -49.827 -29.419 37.389  1.00 14.80 ? 232 LEU A CG  1 
ATOM   4109 C  CD1 . LEU B 1 232 ? -51.349 -29.029 37.279  1.00 18.07 ? 232 LEU A CD1 1 
ATOM   4110 C  CD2 . LEU B 1 232 ? -49.549 -30.042 38.739  1.00 15.75 ? 232 LEU A CD2 1 
ATOM   4111 N  N   . CYS B 1 233 ? -48.156 -32.934 35.096  1.00 13.10 ? 233 CYS A N   1 
ATOM   4112 C  CA  . CYS B 1 233 ? -48.215 -33.869 33.943  1.00 13.95 ? 233 CYS A CA  1 
ATOM   4113 C  C   . CYS B 1 233 ? -49.682 -33.944 33.478  1.00 16.57 ? 233 CYS A C   1 
ATOM   4114 O  O   . CYS B 1 233 ? -49.949 -34.659 32.529  1.00 18.04 ? 233 CYS A O   1 
ATOM   4115 C  CB  . CYS B 1 233 ? -47.565 -35.190 34.263  1.00 14.53 ? 233 CYS A CB  1 
ATOM   4116 S  SG  . CYS B 1 233 ? -48.489 -36.143 35.558  1.00 18.52 ? 233 CYS A SG  1 
ATOM   4117 N  N   . THR B 1 234 ? -50.552 -33.147 34.061  1.00 16.50 ? 234 THR A N   1 
ATOM   4118 C  CA  . THR B 1 234 ? -51.975 -33.149 33.719  1.00 16.91 ? 234 THR A CA  1 
ATOM   4119 C  C   . THR B 1 234 ? -52.360 -31.755 33.145  1.00 18.58 ? 234 THR A C   1 
ATOM   4120 O  O   . THR B 1 234 ? -51.846 -30.726 33.470  1.00 16.54 ? 234 THR A O   1 
ATOM   4121 C  CB  . THR B 1 234 ? -52.786 -33.462 34.992  1.00 18.23 ? 234 THR A CB  1 
ATOM   4122 O  OG1 . THR B 1 234 ? -52.305 -32.638 36.036  1.00 17.03 ? 234 THR A OG1 1 
ATOM   4123 C  CG2 . THR B 1 234 ? -52.685 -34.994 35.333  1.00 20.52 ? 234 THR A CG2 1 
ATOM   4124 N  N   . ALA B 1 235 ? -53.457 -31.780 32.350  1.00 19.90 ? 235 ALA A N   1 
ATOM   4125 C  CA  . ALA B 1 235 ? -53.996 -30.604 31.701  1.00 23.62 ? 235 ALA A CA  1 
ATOM   4126 C  C   . ALA B 1 235 ? -54.978 -29.840 32.596  1.00 26.41 ? 235 ALA A C   1 
ATOM   4127 O  O   . ALA B 1 235 ? -55.456 -30.394 33.596  1.00 26.92 ? 235 ALA A O   1 
ATOM   4128 C  CB  . ALA B 1 235 ? -54.648 -31.017 30.338  1.00 22.84 ? 235 ALA A CB  1 
ATOM   4129 N  N   . GLU B 1 236 ? -55.260 -28.587 32.267  1.00 31.32 ? 236 GLU A N   1 
ATOM   4130 C  CA  . GLU B 1 236 ? -56.282 -27.803 32.992  1.00 33.38 ? 236 GLU A CA  1 
ATOM   4131 C  C   . GLU B 1 236 ? -57.623 -28.592 33.110  1.00 32.66 ? 236 GLU A C   1 
ATOM   4132 O  O   . GLU B 1 236 ? -58.013 -29.313 32.178  1.00 35.99 ? 236 GLU A O   1 
ATOM   4133 C  CB  . GLU B 1 236 ? -56.521 -26.493 32.246  1.00 34.47 ? 236 GLU A CB  1 
ATOM   4134 C  CG  . GLU B 1 236 ? -56.852 -25.334 33.163  1.00 43.52 ? 236 GLU A CG  1 
ATOM   4135 C  CD  . GLU B 1 236 ? -56.721 -24.019 32.433  1.00 56.90 ? 236 GLU A CD  1 
ATOM   4136 O  OE1 . GLU B 1 236 ? -56.340 -23.009 33.089  1.00 60.24 ? 236 GLU A OE1 1 
ATOM   4137 O  OE2 . GLU B 1 236 ? -56.981 -24.022 31.201  1.00 47.42 ? 236 GLU A OE2 1 
ATOM   4138 N  N   . GLY B 1 237 ? -58.244 -28.517 34.294  1.00 33.39 ? 237 GLY A N   1 
ATOM   4139 C  CA  . GLY B 1 237 ? -59.564 -29.113 34.548  1.00 41.22 ? 237 GLY A CA  1 
ATOM   4140 C  C   . GLY B 1 237 ? -59.513 -30.608 34.839  1.00 44.34 ? 237 GLY A C   1 
ATOM   4141 O  O   . GLY B 1 237 ? -60.564 -31.245 34.984  1.00 46.44 ? 237 GLY A O   1 
ATOM   4142 N  N   . GLU B 1 238 ? -58.297 -31.159 34.911  1.00 40.54 ? 238 GLU A N   1 
ATOM   4143 C  CA  . GLU B 1 238 ? -58.012 -32.606 35.069  1.00 39.21 ? 238 GLU A CA  1 
ATOM   4144 C  C   . GLU B 1 238 ? -57.439 -32.671 36.510  1.00 38.32 ? 238 GLU A C   1 
ATOM   4145 O  O   . GLU B 1 238 ? -56.864 -31.683 36.974  1.00 35.33 ? 238 GLU A O   1 
ATOM   4146 C  CB  . GLU B 1 238 ? -57.017 -33.069 33.967  1.00 45.40 ? 238 GLU A CB  1 
ATOM   4147 C  CG  . GLU B 1 238 ? -56.687 -34.566 33.903  1.00 47.36 ? 238 GLU A CG  1 
ATOM   4148 C  CD  . GLU B 1 238 ? -55.522 -35.006 32.963  1.00 51.38 ? 238 GLU A CD  1 
ATOM   4149 O  OE1 . GLU B 1 238 ? -54.996 -34.253 32.070  1.00 39.07 ? 238 GLU A OE1 1 
ATOM   4150 O  OE2 . GLU B 1 238 ? -55.107 -36.192 33.117  1.00 45.87 ? 238 GLU A OE2 1 
ATOM   4151 N  N   . ALA B 1 239 ? -57.641 -33.773 37.252  1.00 40.36 ? 239 ALA A N   1 
ATOM   4152 C  CA  . ALA B 1 239 ? -57.183 -33.796 38.675  1.00 32.17 ? 239 ALA A CA  1 
ATOM   4153 C  C   . ALA B 1 239 ? -55.639 -33.732 38.566  1.00 27.87 ? 239 ALA A C   1 
ATOM   4154 O  O   . ALA B 1 239 ? -55.059 -34.479 37.737  1.00 28.03 ? 239 ALA A O   1 
ATOM   4155 C  CB  . ALA B 1 239 ? -57.617 -35.079 39.395  1.00 31.92 ? 239 ALA A CB  1 
ATOM   4156 N  N   . ALA B 1 240 ? -55.061 -32.844 39.366  1.00 27.94 ? 240 ALA A N   1 
ATOM   4157 C  CA  . ALA B 1 240 ? -53.661 -32.530 39.207  1.00 22.01 ? 240 ALA A CA  1 
ATOM   4158 C  C   . ALA B 1 240 ? -52.749 -33.684 39.633  1.00 21.92 ? 240 ALA A C   1 
ATOM   4159 O  O   . ALA B 1 240 ? -52.974 -34.382 40.650  1.00 20.53 ? 240 ALA A O   1 
ATOM   4160 C  CB  . ALA B 1 240 ? -53.317 -31.258 39.963  1.00 22.72 ? 240 ALA A CB  1 
ATOM   4161 N  N   . ALA B 1 241 ? -51.636 -33.857 38.914  1.00 17.26 ? 241 ALA A N   1 
ATOM   4162 C  CA  . ALA B 1 241 ? -50.600 -34.771 39.285  1.00 16.02 ? 241 ALA A CA  1 
ATOM   4163 C  C   . ALA B 1 241 ? -49.337 -34.004 38.890  1.00 15.12 ? 241 ALA A C   1 
ATOM   4164 O  O   . ALA B 1 241 ? -49.301 -33.363 37.813  1.00 16.86 ? 241 ALA A O   1 
ATOM   4165 C  CB  . ALA B 1 241 ? -50.691 -36.064 38.566  1.00 17.36 ? 241 ALA A CB  1 
ATOM   4166 N  N   . PHE B 1 242 ? -48.323 -34.035 39.708  1.00 12.81 ? 242 PHE A N   1 
ATOM   4167 C  CA  . PHE B 1 242 ? -47.089 -33.311 39.554  1.00 12.23 ? 242 PHE A CA  1 
ATOM   4168 C  C   . PHE B 1 242 ? -46.010 -34.113 38.864  1.00 11.09 ? 242 PHE A C   1 
ATOM   4169 O  O   . PHE B 1 242 ? -45.843 -35.321 39.113  1.00 12.94 ? 242 PHE A O   1 
ATOM   4170 C  CB  . PHE B 1 242 ? -46.562 -32.917 40.974  1.00 13.41 ? 242 PHE A CB  1 
ATOM   4171 C  CG  . PHE B 1 242 ? -47.387 -31.893 41.621  1.00 15.13 ? 242 PHE A CG  1 
ATOM   4172 C  CD1 . PHE B 1 242 ? -48.443 -32.250 42.438  1.00 18.13 ? 242 PHE A CD1 1 
ATOM   4173 C  CD2 . PHE B 1 242 ? -47.120 -30.538 41.359  1.00 17.83 ? 242 PHE A CD2 1 
ATOM   4174 C  CE1 . PHE B 1 242 ? -49.209 -31.222 43.029  1.00 17.06 ? 242 PHE A CE1 1 
ATOM   4175 C  CE2 . PHE B 1 242 ? -47.878 -29.529 41.938  1.00 21.97 ? 242 PHE A CE2 1 
ATOM   4176 C  CZ  . PHE B 1 242 ? -48.952 -29.910 42.772  1.00 17.12 ? 242 PHE A CZ  1 
ATOM   4177 N  N   . LEU B 1 243 ? -45.229 -33.414 38.010  1.00 11.84 ? 243 LEU A N   1 
ATOM   4178 C  CA  . LEU B 1 243 ? -44.090 -34.049 37.296  1.00 11.18 ? 243 LEU A CA  1 
ATOM   4179 C  C   . LEU B 1 243 ? -42.858 -33.971 38.216  1.00 10.23 ? 243 LEU A C   1 
ATOM   4180 O  O   . LEU B 1 243 ? -41.883 -33.255 38.002  1.00 10.82 ? 243 LEU A O   1 
ATOM   4181 C  CB  . LEU B 1 243 ? -43.900 -33.231 35.960  1.00 13.14 ? 243 LEU A CB  1 
ATOM   4182 C  CG  . LEU B 1 243 ? -42.890 -33.848 35.033  1.00 11.98 ? 243 LEU A CG  1 
ATOM   4183 C  CD1 . LEU B 1 243 ? -43.384 -35.192 34.623  1.00 12.79 ? 243 LEU A CD1 1 
ATOM   4184 C  CD2 . LEU B 1 243 ? -42.816 -32.817 33.843  1.00 15.16 ? 243 LEU A CD2 1 
ATOM   4185 N  N   . VAL B 1 244 ? -42.904 -34.792 39.272  1.00 11.07 ? 244 VAL A N   1 
ATOM   4186 C  CA  . VAL B 1 244 ? -41.800 -34.720 40.253  1.00 10.94 ? 244 VAL A CA  1 
ATOM   4187 C  C   . VAL B 1 244 ? -40.557 -35.435 39.802  1.00 10.09 ? 244 VAL A C   1 
ATOM   4188 O  O   . VAL B 1 244 ? -39.484 -35.212 40.305  1.00 10.50 ? 244 VAL A O   1 
ATOM   4189 C  CB  . VAL B 1 244 ? -42.258 -35.241 41.676  1.00 11.65 ? 244 VAL A CB  1 
ATOM   4190 C  CG1 . VAL B 1 244 ? -43.294 -34.281 42.304  1.00 14.30 ? 244 VAL A CG1 1 
ATOM   4191 C  CG2 . VAL B 1 244 ? -42.740 -36.648 41.649  1.00 16.13 ? 244 VAL A CG2 1 
ATOM   4192 N  N   . SER B 1 245 ? -40.721 -36.384 38.828  1.00 10.07 ? 245 SER A N   1 
ATOM   4193 C  CA  . SER B 1 245 ? -39.646 -37.107 38.311  1.00 9.31  ? 245 SER A CA  1 
ATOM   4194 C  C   . SER B 1 245 ? -39.920 -37.421 36.820  1.00 9.84  ? 245 SER A C   1 
ATOM   4195 O  O   . SER B 1 245 ? -41.020 -37.825 36.475  1.00 10.65 ? 245 SER A O   1 
ATOM   4196 C  CB  . SER B 1 245 ? -39.424 -38.425 39.079  1.00 11.19 ? 245 SER A CB  1 
ATOM   4197 O  OG  . SER B 1 245 ? -38.241 -39.167 38.722  1.00 11.92 ? 245 SER A OG  1 
ATOM   4198 N  N   . ASN B 1 246 ? -38.843 -37.365 36.015  1.00 8.88  ? 246 ASN A N   1 
ATOM   4199 C  CA  . ASN B 1 246 ? -39.084 -37.637 34.520  1.00 8.84  ? 246 ASN A CA  1 
ATOM   4200 C  C   . ASN B 1 246 ? -37.821 -38.124 33.897  1.00 8.00  ? 246 ASN A C   1 
ATOM   4201 O  O   . ASN B 1 246 ? -37.523 -37.679 32.741  1.00 10.69 ? 246 ASN A O   1 
ATOM   4202 C  CB  . ASN B 1 246 ? -39.635 -36.367 33.845  1.00 8.58  ? 246 ASN A CB  1 
ATOM   4203 C  CG  . ASN B 1 246 ? -38.653 -35.208 33.845  1.00 8.51  ? 246 ASN A CG  1 
ATOM   4204 O  OD1 . ASN B 1 246 ? -37.694 -35.233 34.596  1.00 9.95  ? 246 ASN A OD1 1 
ATOM   4205 N  ND2 . ASN B 1 246 ? -38.900 -34.177 33.043  1.00 10.14 ? 246 ASN A ND2 1 
ATOM   4206 N  N   . HIS B 1 247 ? -37.149 -39.044 34.480  1.00 8.83  ? 247 HIS A N   1 
ATOM   4207 C  CA  . HIS B 1 247 ? -35.945 -39.628 33.953  1.00 9.44  ? 247 HIS A CA  1 
ATOM   4208 C  C   . HIS B 1 247 ? -36.051 -41.070 33.747  1.00 11.63 ? 247 HIS A C   1 
ATOM   4209 O  O   . HIS B 1 247 ? -36.639 -41.869 34.593  1.00 12.63 ? 247 HIS A O   1 
ATOM   4210 C  CB  . HIS B 1 247 ? -34.654 -39.320 34.808  1.00 9.25  ? 247 HIS A CB  1 
ATOM   4211 C  CG  . HIS B 1 247 ? -34.720 -39.893 36.220  1.00 9.92  ? 247 HIS A CG  1 
ATOM   4212 N  ND1 . HIS B 1 247 ? -34.053 -40.994 36.589  1.00 14.53 ? 247 HIS A ND1 1 
ATOM   4213 C  CD2 . HIS B 1 247 ? -35.443 -39.433 37.279  1.00 9.94  ? 247 HIS A CD2 1 
ATOM   4214 C  CE1 . HIS B 1 247 ? -34.366 -41.202 37.933  1.00 12.64 ? 247 HIS A CE1 1 
ATOM   4215 N  NE2 . HIS B 1 247 ? -35.157 -40.302 38.334  1.00 13.18 ? 247 HIS A NE2 1 
ATOM   4216 N  N   . ARG B 1 248 ? -35.508 -41.571 32.650  1.00 9.43  ? 248 ARG A N   1 
ATOM   4217 C  CA  . ARG B 1 248 ? -35.485 -43.073 32.344  1.00 9.37  ? 248 ARG A CA  1 
ATOM   4218 C  C   . ARG B 1 248 ? -34.125 -43.618 32.869  1.00 9.85  ? 248 ARG A C   1 
ATOM   4219 O  O   . ARG B 1 248 ? -33.087 -42.989 32.714  1.00 10.42 ? 248 ARG A O   1 
ATOM   4220 C  CB  . ARG B 1 248 ? -35.483 -43.216 30.812  1.00 9.75  ? 248 ARG A CB  1 
ATOM   4221 C  CG  . ARG B 1 248 ? -35.620 -44.711 30.429  1.00 10.07 ? 248 ARG A CG  1 
ATOM   4222 C  CD  . ARG B 1 248 ? -35.379 -45.007 28.953  1.00 10.77 ? 248 ARG A CD  1 
ATOM   4223 N  NE  . ARG B 1 248 ? -35.906 -46.336 28.646  1.00 11.52 ? 248 ARG A NE  1 
ATOM   4224 C  CZ  . ARG B 1 248 ? -35.643 -47.038 27.548  1.00 13.46 ? 248 ARG A CZ  1 
ATOM   4225 N  NH1 . ARG B 1 248 ? -34.844 -46.556 26.607  1.00 12.20 ? 248 ARG A NH1 1 
ATOM   4226 N  NH2 . ARG B 1 248 ? -36.193 -48.234 27.396  1.00 14.64 ? 248 ARG A NH2 1 
ATOM   4227 N  N   . PRO B 1 249 ? -34.146 -44.835 33.512  1.00 10.84 ? 249 PRO A N   1 
ATOM   4228 C  CA  . PRO B 1 249 ? -32.897 -45.441 33.951  1.00 11.01 ? 249 PRO A CA  1 
ATOM   4229 C  C   . PRO B 1 249 ? -32.029 -45.828 32.766  1.00 11.00 ? 249 PRO A C   1 
ATOM   4230 O  O   . PRO B 1 249 ? -32.547 -46.099 31.656  1.00 10.66 ? 249 PRO A O   1 
ATOM   4231 C  CB  . PRO B 1 249 ? -33.372 -46.742 34.592  1.00 14.84 ? 249 PRO A CB  1 
ATOM   4232 C  CG  . PRO B 1 249 ? -34.819 -46.508 34.947  1.00 14.31 ? 249 PRO A CG  1 
ATOM   4233 C  CD  . PRO B 1 249 ? -35.367 -45.510 33.873  1.00 12.66 ? 249 PRO A CD  1 
ATOM   4234 N  N   . PRO B 1 250 ? -30.738 -45.930 32.958  1.00 10.61 ? 250 PRO A N   1 
ATOM   4235 C  CA  . PRO B 1 250 ? -29.850 -46.467 31.911  1.00 12.27 ? 250 PRO A CA  1 
ATOM   4236 C  C   . PRO B 1 250 ? -30.255 -47.835 31.453  1.00 12.97 ? 250 PRO A C   1 
ATOM   4237 O  O   . PRO B 1 250 ? -30.684 -48.699 32.302  1.00 12.81 ? 250 PRO A O   1 
ATOM   4238 C  CB  . PRO B 1 250 ? -28.469 -46.538 32.599  1.00 13.85 ? 250 PRO A CB  1 
ATOM   4239 C  CG  . PRO B 1 250 ? -28.497 -45.399 33.670  1.00 12.89 ? 250 PRO A CG  1 
ATOM   4240 C  CD  . PRO B 1 250 ? -29.933 -45.434 34.137  1.00 12.51 ? 250 PRO A CD  1 
ATOM   4241 N  N   . GLN B 1 251 ? -29.977 -48.097 30.221  1.00 11.42 ? 251 GLN A N   1 
ATOM   4242 C  CA  . GLN B 1 251 ? -30.318 -49.370 29.562  1.00 12.01 ? 251 GLN A CA  1 
ATOM   4243 C  C   . GLN B 1 251 ? -28.930 -49.956 29.216  1.00 11.52 ? 251 GLN A C   1 
ATOM   4244 O  O   . GLN B 1 251 ? -27.912 -49.284 29.051  1.00 12.42 ? 251 GLN A O   1 
ATOM   4245 C  CB  . GLN B 1 251 ? -31.084 -49.064 28.257  1.00 11.52 ? 251 GLN A CB  1 
ATOM   4246 C  CG  . GLN B 1 251 ? -32.425 -48.411 28.636  1.00 12.56 ? 251 GLN A CG  1 
ATOM   4247 C  CD  . GLN B 1 251 ? -33.230 -49.208 29.694  1.00 15.28 ? 251 GLN A CD  1 
ATOM   4248 O  OE1 . GLN B 1 251 ? -33.490 -50.418 29.470  1.00 17.30 ? 251 GLN A OE1 1 
ATOM   4249 N  NE2 . GLN B 1 251 ? -33.661 -48.606 30.749  1.00 15.18 ? 251 GLN A NE2 1 
ATOM   4250 N  N   . PRO B 1 252 ? -28.902 -51.310 28.961  1.00 12.68 ? 252 PRO A N   1 
ATOM   4251 C  CA  . PRO B 1 252 ? -27.590 -51.948 28.708  1.00 14.44 ? 252 PRO A CA  1 
ATOM   4252 C  C   . PRO B 1 252 ? -26.945 -51.602 27.376  1.00 12.63 ? 252 PRO A C   1 
ATOM   4253 O  O   . PRO B 1 252 ? -27.702 -51.341 26.367  1.00 12.62 ? 252 PRO A O   1 
ATOM   4254 C  CB  . PRO B 1 252 ? -27.929 -53.434 28.680  1.00 16.65 ? 252 PRO A CB  1 
ATOM   4255 C  CG  . PRO B 1 252 ? -29.213 -53.562 29.405  1.00 18.32 ? 252 PRO A CG  1 
ATOM   4256 C  CD  . PRO B 1 252 ? -29.999 -52.261 29.132  1.00 13.83 ? 252 PRO A CD  1 
ATOM   4257 N  N   . LEU B 1 253 ? -25.623 -51.588 27.330  1.00 14.26 ? 253 LEU A N   1 
ATOM   4258 C  CA  . LEU B 1 253 ? -24.928 -51.208 26.169  1.00 15.74 ? 253 LEU A CA  1 
ATOM   4259 C  C   . LEU B 1 253 ? -25.075 -52.178 24.992  1.00 17.94 ? 253 LEU A C   1 
ATOM   4260 O  O   . LEU B 1 253 ? -25.016 -51.786 23.835  1.00 16.00 ? 253 LEU A O   1 
ATOM   4261 C  CB  . LEU B 1 253 ? -23.433 -51.074 26.446  1.00 20.29 ? 253 LEU A CB  1 
ATOM   4262 C  CG  . LEU B 1 253 ? -22.950 -49.721 26.899  1.00 25.71 ? 253 LEU A CG  1 
ATOM   4263 C  CD1 . LEU B 1 253 ? -21.451 -49.775 27.162  1.00 26.05 ? 253 LEU A CD1 1 
ATOM   4264 C  CD2 . LEU B 1 253 ? -23.206 -48.659 25.834  1.00 23.75 ? 253 LEU A CD2 1 
ATOM   4265 N  N   A LYS B 1 254 ? -25.130 -53.457 25.400  0.50 16.70 ? 254 LYS A N   1 
ATOM   4266 N  N   B LYS B 1 254 ? -25.281 -53.482 25.211  0.50 14.97 ? 254 LYS A N   1 
ATOM   4267 C  CA  A LYS B 1 254 ? -25.350 -54.607 24.543  0.50 19.74 ? 254 LYS A CA  1 
ATOM   4268 C  CA  B LYS B 1 254 ? -25.540 -54.383 24.034  0.50 14.59 ? 254 LYS A CA  1 
ATOM   4269 C  C   A LYS B 1 254 ? -24.458 -54.619 23.330  0.50 18.37 ? 254 LYS A C   1 
ATOM   4270 C  C   B LYS B 1 254 ? -24.360 -54.396 23.014  0.50 14.65 ? 254 LYS A C   1 
ATOM   4271 O  O   A LYS B 1 254 ? -24.991 -54.843 22.240  0.50 21.57 ? 254 LYS A O   1 
ATOM   4272 O  O   B LYS B 1 254 ? -24.534 -54.383 21.763  0.50 14.78 ? 254 LYS A O   1 
ATOM   4273 C  CB  A LYS B 1 254 ? -26.815 -54.689 24.101  0.50 17.28 ? 254 LYS A CB  1 
ATOM   4274 C  CB  B LYS B 1 254 ? -26.946 -54.153 23.407  0.50 14.94 ? 254 LYS A CB  1 
ATOM   4275 C  CG  A LYS B 1 254 ? -27.880 -54.778 25.163  0.50 19.79 ? 254 LYS A CG  1 
ATOM   4276 C  CG  B LYS B 1 254 ? -28.109 -54.414 24.361  0.50 14.56 ? 254 LYS A CG  1 
ATOM   4277 C  CD  A LYS B 1 254 ? -29.195 -54.726 24.402  0.50 20.26 ? 254 LYS A CD  1 
ATOM   4278 C  CD  B LYS B 1 254 ? -28.202 -55.877 24.746  0.50 15.72 ? 254 LYS A CD  1 
ATOM   4279 C  CE  A LYS B 1 254 ? -30.132 -55.853 24.817  0.50 27.42 ? 254 LYS A CE  1 
ATOM   4280 C  CE  B LYS B 1 254 ? -29.148 -56.067 25.892  0.50 16.42 ? 254 LYS A CE  1 
ATOM   4281 N  NZ  A LYS B 1 254 ? -31.498 -55.270 25.079  0.50 23.27 ? 254 LYS A NZ  1 
ATOM   4282 N  NZ  B LYS B 1 254 ? -30.552 -55.624 25.717  0.50 22.41 ? 254 LYS A NZ  1 
ATOM   4283 N  N   . GLY B 1 255 ? -23.178 -54.325 23.560  1.00 17.56 ? 255 GLY A N   1 
ATOM   4284 C  CA  . GLY B 1 255 ? -22.055 -54.419 22.633  1.00 18.07 ? 255 GLY A CA  1 
ATOM   4285 C  C   . GLY B 1 255 ? -21.595 -53.134 22.001  1.00 17.88 ? 255 GLY A C   1 
ATOM   4286 O  O   . GLY B 1 255 ? -20.553 -53.063 21.410  1.00 17.82 ? 255 GLY A O   1 
ATOM   4287 N  N   . ARG B 1 256 ? -22.374 -52.017 22.194  1.00 16.39 ? 256 ARG A N   1 
ATOM   4288 C  CA  . ARG B 1 256 ? -21.841 -50.721 21.757  1.00 15.27 ? 256 ARG A CA  1 
ATOM   4289 C  C   . ARG B 1 256 ? -20.651 -50.206 22.543  1.00 15.55 ? 256 ARG A C   1 
ATOM   4290 O  O   . ARG B 1 256 ? -20.513 -50.572 23.749  1.00 20.34 ? 256 ARG A O   1 
ATOM   4291 C  CB  . ARG B 1 256 ? -22.939 -49.596 21.854  1.00 15.18 ? 256 ARG A CB  1 
ATOM   4292 C  CG  . ARG B 1 256 ? -24.172 -49.869 20.995  1.00 13.95 ? 256 ARG A CG  1 
ATOM   4293 C  CD  . ARG B 1 256 ? -25.358 -48.939 21.458  1.00 14.09 ? 256 ARG A CD  1 
ATOM   4294 N  NE  . ARG B 1 256 ? -25.904 -49.330 22.733  1.00 14.83 ? 256 ARG A NE  1 
ATOM   4295 C  CZ  . ARG B 1 256 ? -26.816 -48.642 23.376  1.00 14.50 ? 256 ARG A CZ  1 
ATOM   4296 N  NH1 . ARG B 1 256 ? -27.238 -47.421 22.909  1.00 11.72 ? 256 ARG A NH1 1 
ATOM   4297 N  NH2 . ARG B 1 256 ? -27.382 -49.085 24.415  1.00 13.23 ? 256 ARG A NH2 1 
ATOM   4298 N  N   . LYS B 1 257 ? -19.815 -49.432 21.908  1.00 18.22 ? 257 LYS A N   1 
ATOM   4299 C  CA  . LYS B 1 257 ? -18.717 -48.869 22.662  1.00 19.08 ? 257 LYS A CA  1 
ATOM   4300 C  C   . LYS B 1 257 ? -18.970 -47.351 22.648  1.00 19.04 ? 257 LYS A C   1 
ATOM   4301 O  O   . LYS B 1 257 ? -19.654 -46.767 21.793  1.00 19.78 ? 257 LYS A O   1 
ATOM   4302 C  CB  . LYS B 1 257 ? -17.417 -49.183 21.964  1.00 22.74 ? 257 LYS A CB  1 
ATOM   4303 C  CG  . LYS B 1 257 ? -16.925 -50.667 22.089  1.00 25.84 ? 257 LYS A CG  1 
ATOM   4304 C  CD  . LYS B 1 257 ? -16.103 -50.924 20.829  1.00 31.57 ? 257 LYS A CD  1 
ATOM   4305 C  CE  . LYS B 1 257 ? -15.363 -52.242 20.713  1.00 31.51 ? 257 LYS A CE  1 
ATOM   4306 N  NZ  . LYS B 1 257 ? -15.894 -53.240 21.631  1.00 35.32 ? 257 LYS A NZ  1 
ATOM   4307 N  N   . VAL B 1 258 ? -18.458 -46.758 23.691  1.00 16.54 ? 258 VAL A N   1 
ATOM   4308 C  CA  . VAL B 1 258 ? -18.528 -45.317 23.899  1.00 14.70 ? 258 VAL A CA  1 
ATOM   4309 C  C   . VAL B 1 258 ? -17.177 -44.696 23.595  1.00 15.30 ? 258 VAL A C   1 
ATOM   4310 O  O   . VAL B 1 258 ? -16.120 -45.287 24.042  1.00 19.07 ? 258 VAL A O   1 
ATOM   4311 C  CB  . VAL B 1 258 ? -18.868 -45.035 25.344  1.00 14.72 ? 258 VAL A CB  1 
ATOM   4312 C  CG1 . VAL B 1 258 ? -18.945 -43.512 25.609  1.00 15.61 ? 258 VAL A CG1 1 
ATOM   4313 C  CG2 . VAL B 1 258 ? -20.163 -45.722 25.765  1.00 15.54 ? 258 VAL A CG2 1 
ATOM   4314 N  N   . ARG B 1 259 ? -17.089 -43.598 22.875  1.00 15.33 ? 259 ARG A N   1 
ATOM   4315 C  CA  . ARG B 1 259 ? -15.781 -42.953 22.503  1.00 16.91 ? 259 ARG A CA  1 
ATOM   4316 C  C   . ARG B 1 259 ? -15.649 -41.660 23.242  1.00 15.50 ? 259 ARG A C   1 
ATOM   4317 O  O   . ARG B 1 259 ? -16.667 -40.993 23.579  1.00 14.79 ? 259 ARG A O   1 
ATOM   4318 C  CB  . ARG B 1 259 ? -15.749 -42.596 21.006  1.00 17.91 ? 259 ARG A CB  1 
ATOM   4319 C  CG  . ARG B 1 259 ? -15.825 -43.866 20.164  1.00 18.55 ? 259 ARG A CG  1 
ATOM   4320 C  CD  . ARG B 1 259 ? -15.642 -43.406 18.737  1.00 23.14 ? 259 ARG A CD  1 
ATOM   4321 N  NE  . ARG B 1 259 ? -16.905 -42.868 18.229  1.00 21.33 ? 259 ARG A NE  1 
ATOM   4322 C  CZ  . ARG B 1 259 ? -17.022 -42.046 17.191  1.00 21.17 ? 259 ARG A CZ  1 
ATOM   4323 N  NH1 . ARG B 1 259 ? -15.948 -41.653 16.521  1.00 22.84 ? 259 ARG A NH1 1 
ATOM   4324 N  NH2 . ARG B 1 259 ? -18.222 -41.617 16.820  1.00 20.93 ? 259 ARG A NH2 1 
ATOM   4325 N  N   . ALA B 1 260 ? -14.456 -41.183 23.558  1.00 14.40 ? 260 ALA A N   1 
ATOM   4326 C  CA  . ALA B 1 260 ? -14.174 -39.916 24.284  1.00 14.95 ? 260 ALA A CA  1 
ATOM   4327 C  C   . ALA B 1 260 ? -13.546 -38.897 23.325  1.00 14.66 ? 260 ALA A C   1 
ATOM   4328 O  O   . ALA B 1 260 ? -12.678 -39.305 22.507  1.00 16.33 ? 260 ALA A O   1 
ATOM   4329 C  CB  . ALA B 1 260 ? -13.247 -40.179 25.500  1.00 16.69 ? 260 ALA A CB  1 
ATOM   4330 N  N   . SER B 1 261 ? -13.873 -37.611 23.465  1.00 12.88 ? 261 SER A N   1 
ATOM   4331 C  CA  . SER B 1 261 ? -13.264 -36.569 22.650  1.00 14.30 ? 261 SER A CA  1 
ATOM   4332 C  C   . SER B 1 261 ? -11.900 -36.093 23.228  1.00 16.42 ? 261 SER A C   1 
ATOM   4333 O  O   . SER B 1 261 ? -11.283 -35.152 22.662  1.00 16.26 ? 261 SER A O   1 
ATOM   4334 C  CB  . SER B 1 261 ? -14.202 -35.359 22.642  1.00 14.17 ? 261 SER A CB  1 
ATOM   4335 O  OG  . SER B 1 261 ? -14.208 -34.707 23.861  1.00 12.53 ? 261 SER A OG  1 
ATOM   4336 N  N   . PHE B 1 262 ? -11.513 -36.614 24.402  1.00 14.81 ? 262 PHE A N   1 
ATOM   4337 C  CA  . PHE B 1 262 ? -10.462 -36.035 25.194  1.00 16.46 ? 262 PHE A CA  1 
ATOM   4338 C  C   . PHE B 1 262 ? -9.610  -37.184 25.750  1.00 19.75 ? 262 PHE A C   1 
ATOM   4339 O  O   . PHE B 1 262 ? -10.057 -38.288 25.841  1.00 19.40 ? 262 PHE A O   1 
ATOM   4340 C  CB  . PHE B 1 262 ? -11.071 -35.172 26.336  1.00 15.97 ? 262 PHE A CB  1 
ATOM   4341 C  CG  . PHE B 1 262 ? -11.956 -36.001 27.243  1.00 16.33 ? 262 PHE A CG  1 
ATOM   4342 C  CD1 . PHE B 1 262 ? -11.423 -36.593 28.387  1.00 18.88 ? 262 PHE A CD1 1 
ATOM   4343 C  CD2 . PHE B 1 262 ? -13.328 -36.221 26.955  1.00 15.56 ? 262 PHE A CD2 1 
ATOM   4344 C  CE1 . PHE B 1 262 ? -12.158 -37.399 29.183  1.00 18.62 ? 262 PHE A CE1 1 
ATOM   4345 C  CE2 . PHE B 1 262 ? -14.103 -36.997 27.785  1.00 16.11 ? 262 PHE A CE2 1 
ATOM   4346 C  CZ  . PHE B 1 262 ? -13.537 -37.581 28.933  1.00 18.40 ? 262 PHE A CZ  1 
ATOM   4347 N  N   . HIS B 1 263 ? -8.349  -36.845 26.096  1.00 24.79 ? 263 HIS A N   1 
ATOM   4348 C  CA  . HIS B 1 263 ? -7.332  -37.802 26.622  1.00 34.31 ? 263 HIS A CA  1 
ATOM   4349 C  C   . HIS B 1 263 ? -7.378  -37.950 28.096  1.00 42.48 ? 263 HIS A C   1 
ATOM   4350 O  O   . HIS B 1 263 ? -6.404  -38.467 28.685  1.00 49.62 ? 263 HIS A O   1 
ATOM   4351 C  CB  . HIS B 1 263 ? -5.933  -37.251 26.406  1.00 38.29 ? 263 HIS A CB  1 
ATOM   4352 C  CG  . HIS B 1 263 ? -5.515  -37.066 24.979  1.00 45.00 ? 263 HIS A CG  1 
ATOM   4353 N  ND1 . HIS B 1 263 ? -4.958  -38.078 24.229  1.00 48.27 ? 263 HIS A ND1 1 
ATOM   4354 C  CD2 . HIS B 1 263 ? -5.473  -35.957 24.203  1.00 49.82 ? 263 HIS A CD2 1 
ATOM   4355 C  CE1 . HIS B 1 263 ? -4.640  -37.614 23.033  1.00 49.06 ? 263 HIS A CE1 1 
ATOM   4356 N  NE2 . HIS B 1 263 ? -4.942  -36.330 22.992  1.00 50.87 ? 263 HIS A NE2 1 
ATOM   4357 O  OXT . HIS B 1 263 ? -8.359  -37.569 28.735  1.00 49.20 ? 263 HIS A OXT 1 
HETATM 4358 ZN ZN  . ZN  C 2 .   ? -6.793  -4.591  13.155  1.00 9.25  ? 301 ZN  B ZN  1 
HETATM 4359 O  O18 A E1F D 3 .   ? -4.531  -5.395  16.749  0.50 13.52 ? 302 E1F B O18 1 
HETATM 4360 O  O18 B E1F D 3 .   ? -4.806  -4.987  16.575  0.50 10.30 ? 302 E1F B O18 1 
HETATM 4361 C  C13 A E1F D 3 .   ? -12.881 2.250   20.677  0.50 29.23 ? 302 E1F B C13 1 
HETATM 4362 C  C13 B E1F D 3 .   ? -5.126  1.028   23.095  0.50 17.29 ? 302 E1F B C13 1 
HETATM 4363 C  C1  A E1F D 3 .   ? -7.410  -1.002  18.471  0.50 14.17 ? 302 E1F B C1  1 
HETATM 4364 C  C1  B E1F D 3 .   ? -7.027  -0.858  18.650  0.50 16.09 ? 302 E1F B C1  1 
HETATM 4365 C  C2  A E1F D 3 .   ? -6.718  -3.465  18.370  0.50 11.58 ? 302 E1F B C2  1 
HETATM 4366 C  C2  B E1F D 3 .   ? -6.870  -3.169  18.391  0.50 17.32 ? 302 E1F B C2  1 
HETATM 4367 CL CL1 A E1F D 3 .   ? -6.511  -5.032  19.215  0.50 10.22 ? 302 E1F B CL1 1 
HETATM 4368 CL CL1 B E1F D 3 .   ? -7.046  -4.670  19.188  0.50 13.72 ? 302 E1F B CL1 1 
HETATM 4369 C  C21 A E1F D 3 .   ? -7.222  -2.282  19.069  0.50 13.33 ? 302 E1F B C21 1 
HETATM 4370 C  C21 B E1F D 3 .   ? -7.138  -2.094  19.194  0.50 17.16 ? 302 E1F B C21 1 
HETATM 4371 C  C5  A E1F D 3 .   ? -7.100  -0.942  17.087  0.50 12.61 ? 302 E1F B C5  1 
HETATM 4372 C  C5  B E1F D 3 .   ? -6.687  -0.698  17.300  0.50 17.25 ? 302 E1F B C5  1 
HETATM 4373 C  C4  A E1F D 3 .   ? -6.615  -2.080  16.388  0.50 12.06 ? 302 E1F B C4  1 
HETATM 4374 C  C4  B E1F D 3 .   ? -6.435  -1.791  16.492  0.50 18.35 ? 302 E1F B C4  1 
HETATM 4375 C  C3  A E1F D 3 .   ? -6.426  -3.329  16.989  0.50 11.36 ? 302 E1F B C3  1 
HETATM 4376 C  C3  B E1F D 3 .   ? -6.539  -3.022  17.053  0.50 16.61 ? 302 E1F B C3  1 
HETATM 4377 S  S16 A E1F D 3 .   ? -5.811  -4.735  16.058  0.50 8.95  ? 302 E1F B S16 1 
HETATM 4378 S  S16 B E1F D 3 .   ? -6.242  -4.443  16.034  0.50 16.22 ? 302 E1F B S16 1 
HETATM 4379 N  N19 A E1F D 3 .   ? -5.304  -4.132  14.563  0.50 8.99  ? 302 E1F B N19 1 
HETATM 4380 N  N19 B E1F D 3 .   ? -5.974  -3.818  14.465  0.50 11.43 ? 302 E1F B N19 1 
HETATM 4381 O  O17 A E1F D 3 .   ? -6.980  -5.601  15.916  0.50 9.23  ? 302 E1F B O17 1 
HETATM 4382 O  O17 B E1F D 3 .   ? -7.447  -5.322  16.099  0.50 14.33 ? 302 E1F B O17 1 
HETATM 4383 C  C6  A E1F D 3 .   ? -7.922  0.236   19.131  0.50 19.29 ? 302 E1F B C6  1 
HETATM 4384 C  C6  B E1F D 3 .   ? -7.269  0.263   19.516  0.50 17.67 ? 302 E1F B C6  1 
HETATM 4385 O  O12 A E1F D 3 .   ? -7.418  1.385   18.865  0.50 18.38 ? 302 E1F B O12 1 
HETATM 4386 O  O12 B E1F D 3 .   ? -8.149  0.163   20.379  0.50 16.77 ? 302 E1F B O12 1 
HETATM 4387 C  C7  A E1F D 3 .   ? -9.002  0.071   20.189  0.50 19.21 ? 302 E1F B C7  1 
HETATM 4388 C  C7  B E1F D 3 .   ? -6.442  1.470   19.199  0.50 17.11 ? 302 E1F B C7  1 
HETATM 4389 S  S8  A E1F D 3 .   ? -10.545 -0.960  20.074  0.50 23.69 ? 302 E1F B S8  1 
HETATM 4390 S  S8  B E1F D 3 .   ? -7.148  2.855   20.140  0.50 19.62 ? 302 E1F B S8  1 
HETATM 4391 C  C9  A E1F D 3 .   ? -11.274 0.671   20.005  0.50 26.96 ? 302 E1F B C9  1 
HETATM 4392 C  C9  B E1F D 3 .   ? -6.489  2.306   21.715  0.50 17.99 ? 302 E1F B C9  1 
HETATM 4393 N  N11 A E1F D 3 .   ? -10.738 1.644   19.163  0.50 28.84 ? 302 E1F B N11 1 
HETATM 4394 N  N11 B E1F D 3 .   ? -6.859  3.054   22.787  0.50 19.27 ? 302 E1F B N11 1 
HETATM 4395 C  C14 A E1F D 3 .   ? -11.230 2.885   19.032  0.50 26.51 ? 302 E1F B C14 1 
HETATM 4396 C  C14 B E1F D 3 .   ? -6.380  2.824   24.031  0.50 18.61 ? 302 E1F B C14 1 
HETATM 4397 C  C15 A E1F D 3 .   ? -12.334 3.224   19.828  0.50 32.04 ? 302 E1F B C15 1 
HETATM 4398 C  C15 B E1F D 3 .   ? -5.461  1.804   24.189  0.50 16.27 ? 302 E1F B C15 1 
HETATM 4399 N  N10 A E1F D 3 .   ? -12.362 0.980   20.767  0.50 22.61 ? 302 E1F B N10 1 
HETATM 4400 N  N10 B E1F D 3 .   ? -5.604  1.320   21.861  0.50 16.19 ? 302 E1F B N10 1 
HETATM 4401 C  C1  . CIT E 4 .   ? 3.151   -5.307  -1.697  1.00 43.75 ? 303 CIT B C1  1 
HETATM 4402 O  O1  . CIT E 4 .   ? 4.080   -5.511  -0.875  1.00 49.79 ? 303 CIT B O1  1 
HETATM 4403 O  O2  . CIT E 4 .   ? 2.758   -6.161  -2.515  1.00 51.17 ? 303 CIT B O2  1 
HETATM 4404 C  C2  . CIT E 4 .   ? 2.531   -3.918  -1.738  1.00 33.98 ? 303 CIT B C2  1 
HETATM 4405 C  C3  . CIT E 4 .   ? 1.597   -3.635  -0.581  1.00 29.58 ? 303 CIT B C3  1 
HETATM 4406 O  O7  . CIT E 4 .   ? 0.669   -4.642  -0.221  1.00 21.61 ? 303 CIT B O7  1 
HETATM 4407 C  C4  . CIT E 4 .   ? 1.246   -2.220  -0.245  1.00 26.82 ? 303 CIT B C4  1 
HETATM 4408 C  C5  . CIT E 4 .   ? 0.085   -2.070  -1.236  1.00 25.63 ? 303 CIT B C5  1 
HETATM 4409 O  O3  . CIT E 4 .   ? 0.167   -2.018  -2.512  1.00 27.97 ? 303 CIT B O3  1 
HETATM 4410 O  O4  . CIT E 4 .   ? -0.992  -2.286  -0.733  1.00 19.21 ? 303 CIT B O4  1 
HETATM 4411 C  C6  . CIT E 4 .   ? 2.623   -3.911  0.539   1.00 31.97 ? 303 CIT B C6  1 
HETATM 4412 O  O5  . CIT E 4 .   ? 3.813   -3.451  0.523   1.00 32.65 ? 303 CIT B O5  1 
HETATM 4413 O  O6  . CIT E 4 .   ? 2.375   -4.668  1.479   1.00 27.13 ? 303 CIT B O6  1 
HETATM 4414 C  C1  . EDO F 5 .   ? -18.087 -26.621 9.793   1.00 25.34 ? 304 EDO B C1  1 
HETATM 4415 O  O1  . EDO F 5 .   ? -16.871 -26.633 9.007   1.00 29.52 ? 304 EDO B O1  1 
HETATM 4416 C  C2  . EDO F 5 .   ? -17.852 -26.815 11.267  1.00 21.61 ? 304 EDO B C2  1 
HETATM 4417 O  O2  . EDO F 5 .   ? -17.669 -28.267 11.610  1.00 23.68 ? 304 EDO B O2  1 
HETATM 4418 C  C1  . EDO G 5 .   ? -3.711  -35.798 19.150  1.00 47.60 ? 305 EDO B C1  1 
HETATM 4419 O  O1  . EDO G 5 .   ? -4.724  -36.701 18.723  1.00 46.10 ? 305 EDO B O1  1 
HETATM 4420 C  C2  . EDO G 5 .   ? -3.692  -35.245 20.578  1.00 54.71 ? 305 EDO B C2  1 
HETATM 4421 O  O2  . EDO G 5 .   ? -2.416  -34.598 20.878  1.00 45.87 ? 305 EDO B O2  1 
HETATM 4422 C  C   . ACY H 6 .   ? 1.663   -27.448 22.852  1.00 42.28 ? 306 ACY B C   1 
HETATM 4423 O  O   . ACY H 6 .   ? 0.965   -28.462 22.548  1.00 43.85 ? 306 ACY B O   1 
HETATM 4424 O  OXT . ACY H 6 .   ? 2.910   -27.354 22.682  1.00 41.50 ? 306 ACY B OXT 1 
HETATM 4425 C  CH3 . ACY H 6 .   ? 0.989   -26.293 23.464  1.00 27.23 ? 306 ACY B CH3 1 
HETATM 4426 C  C   . ACY I 6 .   ? 1.495   -22.565 25.600  1.00 44.17 ? 307 ACY B C   1 
HETATM 4427 O  O   . ACY I 6 .   ? 0.464   -21.947 26.003  1.00 40.64 ? 307 ACY B O   1 
HETATM 4428 O  OXT . ACY I 6 .   ? 1.592   -23.851 25.560  1.00 36.58 ? 307 ACY B OXT 1 
HETATM 4429 C  CH3 . ACY I 6 .   ? 2.645   -21.684 25.176  1.00 38.61 ? 307 ACY B CH3 1 
HETATM 4430 C  C   . ACY J 6 .   ? -29.064 -4.900  33.252  1.00 43.75 ? 308 ACY B C   1 
HETATM 4431 O  O   . ACY J 6 .   ? -28.741 -3.828  32.640  1.00 42.38 ? 308 ACY B O   1 
HETATM 4432 O  OXT . ACY J 6 .   ? -28.453 -6.008  33.088  1.00 35.23 ? 308 ACY B OXT 1 
HETATM 4433 C  CH3 . ACY J 6 .   ? -30.234 -4.872  34.190  1.00 43.72 ? 308 ACY B CH3 1 
HETATM 4434 ZN ZN  . ZN  K 2 .   ? -34.356 -35.898 26.962  1.00 8.22  ? 301 ZN  A ZN  1 
HETATM 4435 O  O18 . E1F L 3 .   ? -33.855 -38.530 23.834  1.00 12.51 ? 302 E1F A O18 1 
HETATM 4436 C  C13 . E1F L 3 .   ? -40.275 -38.541 17.659  1.00 37.86 ? 302 E1F A C13 1 
HETATM 4437 C  C1  . E1F L 3 .   ? -37.953 -35.925 21.642  1.00 23.01 ? 302 E1F A C1  1 
HETATM 4438 C  C2  . E1F L 3 .   ? -35.617 -36.558 21.809  1.00 15.52 ? 302 E1F A C2  1 
HETATM 4439 CL CL1 . E1F L 3 .   ? -34.091 -36.838 21.027  1.00 14.56 ? 302 E1F A CL1 1 
HETATM 4440 C  C21 . E1F L 3 .   ? -36.722 -36.148 21.019  1.00 22.16 ? 302 E1F A C21 1 
HETATM 4441 C  C5  . E1F L 3 .   ? -38.052 -36.096 23.041  1.00 19.62 ? 302 E1F A C5  1 
HETATM 4442 C  C4  . E1F L 3 .   ? -36.964 -36.523 23.825  1.00 16.02 ? 302 E1F A C4  1 
HETATM 4443 C  C3  . E1F L 3 .   ? -35.709 -36.659 23.206  1.00 13.56 ? 302 E1F A C3  1 
HETATM 4444 S  S16 . E1F L 3 .   ? -34.358 -37.181 24.255  1.00 11.58 ? 302 E1F A S16 1 
HETATM 4445 N  N19 . E1F L 3 .   ? -34.965 -37.250 25.837  1.00 11.95 ? 302 E1F A N19 1 
HETATM 4446 O  O17 . E1F L 3 .   ? -33.463 -36.064 24.173  1.00 11.15 ? 302 E1F A O17 1 
HETATM 4447 C  C6  . E1F L 3 .   ? -39.151 -35.471 20.910  1.00 30.89 ? 302 E1F A C6  1 
HETATM 4448 O  O12 . E1F L 3 .   ? -39.097 -34.412 20.219  1.00 36.70 ? 302 E1F A O12 1 
HETATM 4449 C  C7  . E1F L 3 .   ? -40.431 -36.162 21.070  1.00 31.67 ? 302 E1F A C7  1 
HETATM 4450 S  S8  . E1F L 3 .   ? -41.484 -35.266 19.820  1.00 36.22 ? 302 E1F A S8  1 
HETATM 4451 C  C9  . E1F L 3 .   ? -41.261 -36.534 18.519  1.00 39.30 ? 302 E1F A C9  1 
HETATM 4452 N  N11 . E1F L 3 .   ? -41.958 -36.475 17.315  1.00 48.05 ? 302 E1F A N11 1 
HETATM 4453 C  C14 . E1F L 3 .   ? -41.830 -37.408 16.295  1.00 41.67 ? 302 E1F A C14 1 
HETATM 4454 C  C15 . E1F L 3 .   ? -40.961 -38.471 16.453  1.00 39.09 ? 302 E1F A C15 1 
HETATM 4455 N  N10 . E1F L 3 .   ? -40.406 -37.602 18.662  1.00 41.69 ? 302 E1F A N10 1 
HETATM 4456 C  C1  . CIT M 4 .   ? -36.396 -45.681 39.524  1.00 50.97 ? 303 CIT A C1  1 
HETATM 4457 O  O1  . CIT M 4 .   ? -35.429 -45.943 40.308  1.00 56.05 ? 303 CIT A O1  1 
HETATM 4458 O  O2  . CIT M 4 .   ? -36.749 -46.495 38.598  1.00 44.36 ? 303 CIT A O2  1 
HETATM 4459 C  C2  . CIT M 4 .   ? -37.179 -44.362 39.679  1.00 34.34 ? 303 CIT A C2  1 
HETATM 4460 C  C3  . CIT M 4 .   ? -36.578 -43.166 40.507  1.00 33.46 ? 303 CIT A C3  1 
HETATM 4461 O  O7  . CIT M 4 .   ? -35.179 -42.887 40.208  1.00 30.57 ? 303 CIT A O7  1 
HETATM 4462 C  C4  . CIT M 4 .   ? -37.510 -41.916 40.311  1.00 27.97 ? 303 CIT A C4  1 
HETATM 4463 C  C5  . CIT M 4 .   ? -37.151 -40.741 41.242  1.00 28.80 ? 303 CIT A C5  1 
HETATM 4464 O  O3  . CIT M 4 .   ? -36.234 -39.991 40.942  1.00 23.47 ? 303 CIT A O3  1 
HETATM 4465 O  O4  . CIT M 4 .   ? -37.710 -40.570 42.334  1.00 41.98 ? 303 CIT A O4  1 
HETATM 4466 C  C6  . CIT M 4 .   ? -36.644 -43.598 41.979  1.00 41.00 ? 303 CIT A C6  1 
HETATM 4467 O  O5  . CIT M 4 .   ? -35.597 -43.658 42.694  1.00 39.84 ? 303 CIT A O5  1 
HETATM 4468 O  O6  . CIT M 4 .   ? -37.777 -43.907 42.458  1.00 48.41 ? 303 CIT A O6  1 
HETATM 4469 C  C1  . PEG N 7 .   ? -25.742 -52.431 19.848  1.00 18.12 ? 304 PEG A C1  1 
HETATM 4470 O  O1  . PEG N 7 .   ? -26.344 -53.317 20.649  1.00 25.99 ? 304 PEG A O1  1 
HETATM 4471 C  C2  . PEG N 7 .   ? -25.751 -52.232 18.309  1.00 23.06 ? 304 PEG A C2  1 
HETATM 4472 O  O2  . PEG N 7 .   ? -26.666 -52.765 17.361  1.00 22.48 ? 304 PEG A O2  1 
HETATM 4473 C  C3  . PEG N 7 .   ? -27.131 -54.101 17.419  1.00 35.74 ? 304 PEG A C3  1 
HETATM 4474 C  C4  . PEG N 7 .   ? -28.014 -54.621 16.270  1.00 30.62 ? 304 PEG A C4  1 
HETATM 4475 O  O4  . PEG N 7 .   ? -29.162 -55.210 16.901  1.00 32.39 ? 304 PEG A O4  1 
HETATM 4476 C  C1  . EDO O 5 .   ? -40.074 -14.872 27.778  1.00 29.41 ? 305 EDO A C1  1 
HETATM 4477 O  O1  . EDO O 5 .   ? -38.934 -14.627 28.643  1.00 23.26 ? 305 EDO A O1  1 
HETATM 4478 C  C2  . EDO O 5 .   ? -40.147 -14.118 26.404  1.00 29.70 ? 305 EDO A C2  1 
HETATM 4479 O  O2  . EDO O 5 .   ? -39.103 -14.002 25.345  1.00 20.09 ? 305 EDO A O2  1 
HETATM 4480 O  O   . HOH P 8 .   ? -13.180 -18.555 28.176  1.00 14.82 ? 401 HOH B O   1 
HETATM 4481 O  O   . HOH P 8 .   ? -4.925  -11.364 26.037  1.00 13.52 ? 402 HOH B O   1 
HETATM 4482 O  O   . HOH P 8 .   ? -2.045  -2.106  10.846  1.00 11.67 ? 403 HOH B O   1 
HETATM 4483 O  O   . HOH P 8 .   ? -19.623 -16.762 24.356  1.00 16.09 ? 404 HOH B O   1 
HETATM 4484 O  O   . HOH P 8 .   ? -6.590  -5.731  -0.739  1.00 10.06 ? 405 HOH B O   1 
HETATM 4485 O  O   . HOH P 8 .   ? -11.575 -21.727 10.220  1.00 12.27 ? 406 HOH B O   1 
HETATM 4486 O  O   . HOH P 8 .   ? -5.456  -15.720 26.589  1.00 16.22 ? 407 HOH B O   1 
HETATM 4487 O  O   . HOH P 8 .   ? -0.992  -0.673  -6.329  1.00 13.12 ? 408 HOH B O   1 
HETATM 4488 O  O   . HOH P 8 .   ? -10.304 -16.545 8.279   1.00 9.94  ? 409 HOH B O   1 
HETATM 4489 O  O   . HOH P 8 .   ? -25.198 -14.796 19.315  1.00 13.23 ? 410 HOH B O   1 
HETATM 4490 O  O   . HOH P 8 .   ? -20.348 -20.744 11.051  1.00 15.02 ? 411 HOH B O   1 
HETATM 4491 O  O   . HOH P 8 .   ? -17.828 -23.766 18.385  1.00 12.19 ? 412 HOH B O   1 
HETATM 4492 O  O   . HOH P 8 .   ? 4.141   -19.606 12.300  1.00 22.18 ? 413 HOH B O   1 
HETATM 4493 O  O   . HOH P 8 .   ? -22.509 -19.597 18.704  1.00 12.86 ? 414 HOH B O   1 
HETATM 4494 O  O   . HOH P 8 .   ? -7.161  -15.463 28.622  1.00 14.35 ? 415 HOH B O   1 
HETATM 4495 O  O   . HOH P 8 .   ? 0.115   -19.899 21.784  1.00 13.42 ? 416 HOH B O   1 
HETATM 4496 O  O   . HOH P 8 .   ? -17.308 -10.437 28.781  1.00 13.74 ? 417 HOH B O   1 
HETATM 4497 O  O   . HOH P 8 .   ? -20.772 -5.531  22.869  1.00 13.30 ? 418 HOH B O   1 
HETATM 4498 O  O   . HOH P 8 .   ? 6.335   -13.582 11.350  1.00 19.16 ? 419 HOH B O   1 
HETATM 4499 O  O   . HOH P 8 .   ? -0.508  -11.965 25.601  1.00 14.36 ? 420 HOH B O   1 
HETATM 4500 O  O   . HOH P 8 .   ? -15.894 -5.383  34.680  1.00 15.96 ? 421 HOH B O   1 
HETATM 4501 O  O   . HOH P 8 .   ? -24.532 -11.660 15.395  1.00 14.35 ? 422 HOH B O   1 
HETATM 4502 O  O   . HOH P 8 .   ? -10.596 -21.660 26.889  1.00 19.09 ? 423 HOH B O   1 
HETATM 4503 O  O   . HOH P 8 .   ? -1.979  -14.070 24.692  1.00 13.11 ? 424 HOH B O   1 
HETATM 4504 O  O   . HOH P 8 .   ? -26.496 -12.832 20.951  1.00 13.90 ? 425 HOH B O   1 
HETATM 4505 O  O   . HOH P 8 .   ? -4.275  -20.589 26.358  1.00 18.57 ? 426 HOH B O   1 
HETATM 4506 O  O   . HOH P 8 .   ? -10.919 -4.842  -4.701  1.00 14.42 ? 427 HOH B O   1 
HETATM 4507 O  O   . HOH P 8 .   ? -4.127  6.078   8.108   1.00 19.72 ? 428 HOH B O   1 
HETATM 4508 O  O   . HOH P 8 .   ? -9.593  2.462   12.883  1.00 21.34 ? 429 HOH B O   1 
HETATM 4509 O  O   . HOH P 8 .   ? -5.806  0.394   10.649  1.00 13.88 ? 430 HOH B O   1 
HETATM 4510 O  O   . HOH P 8 .   ? -21.266 -18.115 10.807  1.00 13.74 ? 431 HOH B O   1 
HETATM 4511 O  O   . HOH P 8 .   ? -0.400  -0.858  4.166   1.00 15.77 ? 432 HOH B O   1 
HETATM 4512 O  O   . HOH P 8 .   ? 1.401   -8.279  6.789   1.00 19.56 ? 433 HOH B O   1 
HETATM 4513 O  O   . HOH P 8 .   ? -14.837 -0.171  28.156  1.00 20.84 ? 434 HOH B O   1 
HETATM 4514 O  O   . HOH P 8 .   ? -5.837  -19.907 6.015   1.00 14.50 ? 435 HOH B O   1 
HETATM 4515 O  O   . HOH P 8 .   ? -13.406 -23.354 17.313  1.00 13.75 ? 436 HOH B O   1 
HETATM 4516 O  O   . HOH P 8 .   ? 3.495   -17.052 5.920   1.00 17.25 ? 437 HOH B O   1 
HETATM 4517 O  O   . HOH P 8 .   ? -11.536 -25.553 16.730  1.00 17.05 ? 438 HOH B O   1 
HETATM 4518 O  O   . HOH P 8 .   ? -2.190  -18.439 22.297  1.00 12.47 ? 439 HOH B O   1 
HETATM 4519 O  O   . HOH P 8 .   ? 4.567   -24.543 6.882   1.00 17.50 ? 440 HOH B O   1 
HETATM 4520 O  O   . HOH P 8 .   ? -3.632  -25.876 8.145   1.00 19.37 ? 441 HOH B O   1 
HETATM 4521 O  O   . HOH P 8 .   ? 5.572   -22.269 4.170   1.00 17.27 ? 442 HOH B O   1 
HETATM 4522 O  O   . HOH P 8 .   ? -0.737  -13.885 -1.610  1.00 25.64 ? 443 HOH B O   1 
HETATM 4523 O  O   . HOH P 8 .   ? -0.444  -8.480  2.926   1.00 20.33 ? 444 HOH B O   1 
HETATM 4524 O  O   . HOH P 8 .   ? 5.875   -1.898  11.783  1.00 17.51 ? 445 HOH B O   1 
HETATM 4525 O  O   . HOH P 8 .   ? 13.624  -16.821 19.396  1.00 19.29 ? 446 HOH B O   1 
HETATM 4526 O  O   . HOH P 8 .   ? -21.441 3.938   0.063   1.00 22.03 ? 447 HOH B O   1 
HETATM 4527 O  O   . HOH P 8 .   ? -28.861 -12.051 19.789  1.00 16.69 ? 448 HOH B O   1 
HETATM 4528 O  O   . HOH P 8 .   ? -7.564  -7.282  37.760  1.00 18.99 ? 449 HOH B O   1 
HETATM 4529 O  O   . HOH P 8 .   ? -17.016 -2.784  34.097  1.00 19.02 ? 450 HOH B O   1 
HETATM 4530 O  O   . HOH P 8 .   ? -10.697 -27.115 18.947  1.00 20.71 ? 451 HOH B O   1 
HETATM 4531 O  O   . HOH P 8 .   ? 1.261   -10.416 24.175  1.00 14.16 ? 452 HOH B O   1 
HETATM 4532 O  O   . HOH P 8 .   ? -5.590  9.551   9.568   1.00 20.36 ? 453 HOH B O   1 
HETATM 4533 O  O   . HOH P 8 .   ? -26.717 -14.357 17.018  1.00 14.52 ? 454 HOH B O   1 
HETATM 4534 O  O   . HOH P 8 .   ? -24.002 8.842   15.312  1.00 30.50 ? 455 HOH B O   1 
HETATM 4535 O  O   . HOH P 8 .   ? -1.780  -4.808  -2.203  1.00 18.58 ? 456 HOH B O   1 
HETATM 4536 O  O   . HOH P 8 .   ? -9.139  -13.977 32.664  1.00 18.17 ? 457 HOH B O   1 
HETATM 4537 O  O   . HOH P 8 .   ? -20.351 -6.629  -5.716  1.00 14.26 ? 458 HOH B O   1 
HETATM 4538 O  O   . HOH P 8 .   ? -10.769 -24.154 8.655   1.00 16.28 ? 459 HOH B O   1 
HETATM 4539 O  O   . HOH P 8 .   ? -17.595 -9.893  32.865  1.00 21.89 ? 460 HOH B O   1 
HETATM 4540 O  O   . HOH P 8 .   ? -15.023 -25.402 13.922  1.00 18.27 ? 461 HOH B O   1 
HETATM 4541 O  O   . HOH P 8 .   ? -2.085  -25.772 10.872  1.00 21.20 ? 462 HOH B O   1 
HETATM 4542 O  O   . HOH P 8 .   ? -3.929  9.364   -1.968  1.00 17.94 ? 463 HOH B O   1 
HETATM 4543 O  O   . HOH P 8 .   ? -19.482 -14.270 5.470   1.00 16.14 ? 464 HOH B O   1 
HETATM 4544 O  O   . HOH P 8 .   ? 2.911   -3.351  25.587  1.00 19.71 ? 465 HOH B O   1 
HETATM 4545 O  O   . HOH P 8 .   ? -20.792 -4.440  -7.552  1.00 17.85 ? 466 HOH B O   1 
HETATM 4546 O  O   . HOH P 8 .   ? -15.341 1.304   20.277  1.00 26.84 ? 467 HOH B O   1 
HETATM 4547 O  O   . HOH P 8 .   ? -5.020  -12.384 -2.017  1.00 18.10 ? 468 HOH B O   1 
HETATM 4548 O  O   . HOH P 8 .   ? 5.401   -9.048  25.549  1.00 26.74 ? 469 HOH B O   1 
HETATM 4549 O  O   . HOH P 8 .   ? -6.344  -14.139 32.685  1.00 22.42 ? 470 HOH B O   1 
HETATM 4550 O  O   . HOH P 8 .   ? 12.481  -18.577 7.488   1.00 20.42 ? 471 HOH B O   1 
HETATM 4551 O  O   . HOH P 8 .   ? -5.309  -15.594 30.706  1.00 20.36 ? 472 HOH B O   1 
HETATM 4552 O  O   . HOH P 8 .   ? -7.331  -13.786 -1.220  1.00 19.52 ? 473 HOH B O   1 
HETATM 4553 O  O   . HOH P 8 .   ? -21.960 -6.713  25.014  1.00 17.11 ? 474 HOH B O   1 
HETATM 4554 O  O   . HOH P 8 .   ? 10.041  -14.842 12.490  1.00 29.63 ? 475 HOH B O   1 
HETATM 4555 O  O   . HOH P 8 .   ? 2.138   -7.952  4.268   1.00 18.43 ? 476 HOH B O   1 
HETATM 4556 O  O   . HOH P 8 .   ? 8.326   -6.744  24.266  1.00 25.51 ? 477 HOH B O   1 
HETATM 4557 O  O   . HOH P 8 .   ? -9.435  -0.009  15.081  1.00 20.09 ? 478 HOH B O   1 
HETATM 4558 O  O   . HOH P 8 .   ? -10.576 -26.803 9.738   1.00 24.39 ? 479 HOH B O   1 
HETATM 4559 O  O   . HOH P 8 .   ? -17.691 3.893   15.062  1.00 26.39 ? 480 HOH B O   1 
HETATM 4560 O  O   . HOH P 8 .   ? -2.704  3.868   2.291   1.00 18.62 ? 481 HOH B O   1 
HETATM 4561 O  O   . HOH P 8 .   ? -23.394 6.138   2.465   1.00 24.74 ? 482 HOH B O   1 
HETATM 4562 O  O   . HOH P 8 .   ? -4.710  -1.940  33.624  1.00 25.36 ? 483 HOH B O   1 
HETATM 4563 O  O   . HOH P 8 .   ? -23.336 -18.097 8.078   1.00 21.49 ? 484 HOH B O   1 
HETATM 4564 O  O   . HOH P 8 .   ? -25.835 -15.976 -0.771  1.00 23.51 ? 485 HOH B O   1 
HETATM 4565 O  O   . HOH P 8 .   ? -12.834 1.975   28.061  1.00 23.50 ? 486 HOH B O   1 
HETATM 4566 O  O   . HOH P 8 .   ? -7.889  -28.479 20.671  1.00 24.67 ? 487 HOH B O   1 
HETATM 4567 O  O   . HOH P 8 .   ? 4.126   -15.610 -1.132  1.00 18.75 ? 488 HOH B O   1 
HETATM 4568 O  O   . HOH P 8 .   ? -22.151 -0.671  -1.343  1.00 23.56 ? 489 HOH B O   1 
HETATM 4569 O  O   . HOH P 8 .   ? 3.401   1.871   23.061  1.00 25.28 ? 490 HOH B O   1 
HETATM 4570 O  O   . HOH P 8 .   ? -17.498 -17.037 -3.258  1.00 23.58 ? 491 HOH B O   1 
HETATM 4571 O  O   . HOH P 8 .   ? -16.311 6.834   0.623   1.00 28.26 ? 492 HOH B O   1 
HETATM 4572 O  O   . HOH P 8 .   ? 1.199   -21.641 0.647   1.00 22.71 ? 493 HOH B O   1 
HETATM 4573 O  O   . HOH P 8 .   ? -3.687  -17.836 26.262  1.00 19.17 ? 494 HOH B O   1 
HETATM 4574 O  O   . HOH P 8 .   ? -7.412  0.801   13.091  1.00 26.03 ? 495 HOH B O   1 
HETATM 4575 O  O   . HOH P 8 .   ? -5.909  -18.579 29.090  1.00 23.35 ? 496 HOH B O   1 
HETATM 4576 O  O   . HOH P 8 .   ? 8.550   0.211   12.778  1.00 25.03 ? 497 HOH B O   1 
HETATM 4577 O  O   . HOH P 8 .   ? 1.870   -19.317 23.879  1.00 18.98 ? 498 HOH B O   1 
HETATM 4578 O  O   . HOH P 8 .   ? 7.744   -9.427  17.760  1.00 17.78 ? 499 HOH B O   1 
HETATM 4579 O  O   . HOH P 8 .   ? 2.804   -9.117  26.783  1.00 20.69 ? 500 HOH B O   1 
HETATM 4580 O  O   . HOH P 8 .   ? 8.857   -5.910  15.242  1.00 21.04 ? 501 HOH B O   1 
HETATM 4581 O  O   . HOH P 8 .   ? -21.790 -4.395  32.735  1.00 20.99 ? 502 HOH B O   1 
HETATM 4582 O  O   . HOH P 8 .   ? -2.764  -27.988 12.573  1.00 23.12 ? 503 HOH B O   1 
HETATM 4583 O  O   . HOH P 8 .   ? -17.117 -0.004  29.938  1.00 36.30 ? 504 HOH B O   1 
HETATM 4584 O  O   . HOH P 8 .   ? 7.075   -20.316 12.750  1.00 31.48 ? 505 HOH B O   1 
HETATM 4585 O  O   . HOH P 8 .   ? -15.983 -23.715 23.961  1.00 15.93 ? 506 HOH B O   1 
HETATM 4586 O  O   . HOH P 8 .   ? -19.882 -13.708 30.148  1.00 25.71 ? 507 HOH B O   1 
HETATM 4587 O  O   . HOH P 8 .   ? 5.004   -5.035  26.365  1.00 24.32 ? 508 HOH B O   1 
HETATM 4588 O  O   . HOH P 8 .   ? -13.941 8.831   -1.728  1.00 27.39 ? 509 HOH B O   1 
HETATM 4589 O  O   . HOH P 8 .   ? -16.486 -18.915 4.107   1.00 24.86 ? 510 HOH B O   1 
HETATM 4590 O  O   . HOH P 8 .   ? -24.471 -4.622  23.374  1.00 21.12 ? 511 HOH B O   1 
HETATM 4591 O  O   . HOH P 8 .   ? -28.665 -12.548 9.443   1.00 27.83 ? 512 HOH B O   1 
HETATM 4592 O  O   . HOH P 8 .   ? -13.273 -28.943 11.981  1.00 30.78 ? 513 HOH B O   1 
HETATM 4593 O  O   . HOH P 8 .   ? 8.977   -13.306 22.051  1.00 28.50 ? 514 HOH B O   1 
HETATM 4594 O  O   . HOH P 8 .   ? -18.664 -20.976 26.805  1.00 19.52 ? 515 HOH B O   1 
HETATM 4595 O  O   . HOH P 8 .   ? 10.257  -7.380  16.888  1.00 29.61 ? 516 HOH B O   1 
HETATM 4596 O  O   . HOH P 8 .   ? 1.698   -28.369 12.163  1.00 33.98 ? 517 HOH B O   1 
HETATM 4597 O  O   . HOH P 8 .   ? -2.437  6.613   5.970   1.00 22.42 ? 518 HOH B O   1 
HETATM 4598 O  O   . HOH P 8 .   ? -19.065 5.269   19.104  1.00 25.81 ? 519 HOH B O   1 
HETATM 4599 O  O   . HOH P 8 .   ? -10.958 2.962   32.837  1.00 33.46 ? 520 HOH B O   1 
HETATM 4600 O  O   . HOH P 8 .   ? -4.594  -24.034 26.127  1.00 24.87 ? 521 HOH B O   1 
HETATM 4601 O  O   . HOH P 8 .   ? -16.872 -15.740 32.957  1.00 32.72 ? 522 HOH B O   1 
HETATM 4602 O  O   . HOH P 8 .   ? 0.433   -5.823  28.205  1.00 22.23 ? 523 HOH B O   1 
HETATM 4603 O  O   . HOH P 8 .   ? -8.881  -13.541 -3.339  1.00 19.37 ? 524 HOH B O   1 
HETATM 4604 O  O   . HOH P 8 .   ? -12.789 2.593   -4.844  1.00 25.10 ? 525 HOH B O   1 
HETATM 4605 O  O   . HOH P 8 .   ? -19.181 -4.379  33.161  1.00 24.17 ? 526 HOH B O   1 
HETATM 4606 O  O   . HOH P 8 .   ? -13.698 -20.404 2.342   1.00 21.50 ? 527 HOH B O   1 
HETATM 4607 O  O   . HOH P 8 .   ? 7.097   -3.702  27.513  1.00 40.10 ? 528 HOH B O   1 
HETATM 4608 O  O   . HOH P 8 .   ? 3.404   -5.547  3.919   1.00 22.07 ? 529 HOH B O   1 
HETATM 4609 O  O   . HOH P 8 .   ? -17.421 0.587   21.610  1.00 22.95 ? 530 HOH B O   1 
HETATM 4610 O  O   . HOH P 8 .   ? -12.679 -23.656 32.707  1.00 38.31 ? 531 HOH B O   1 
HETATM 4611 O  O   . HOH P 8 .   ? 6.106   2.111   22.431  1.00 24.36 ? 532 HOH B O   1 
HETATM 4612 O  O   . HOH P 8 .   ? -28.477 -9.830  8.946   1.00 35.40 ? 533 HOH B O   1 
HETATM 4613 O  O   . HOH P 8 .   ? -12.654 -19.442 31.940  1.00 28.34 ? 534 HOH B O   1 
HETATM 4614 O  O   . HOH P 8 .   ? -20.891 -0.820  32.091  1.00 20.75 ? 535 HOH B O   1 
HETATM 4615 O  O   . HOH P 8 .   ? -16.410 -0.498  -6.057  1.00 20.97 ? 536 HOH B O   1 
HETATM 4616 O  O   . HOH P 8 .   ? 8.699   -19.981 17.531  1.00 25.55 ? 537 HOH B O   1 
HETATM 4617 O  O   . HOH P 8 .   ? -22.554 -11.451 32.677  1.00 22.60 ? 538 HOH B O   1 
HETATM 4618 O  O   . HOH P 8 .   ? -22.887 -12.904 4.746   1.00 39.72 ? 539 HOH B O   1 
HETATM 4619 O  O   . HOH P 8 .   ? -15.667 -25.358 6.383   1.00 31.44 ? 540 HOH B O   1 
HETATM 4620 O  O   . HOH P 8 .   ? -14.287 -27.401 10.190  1.00 24.75 ? 541 HOH B O   1 
HETATM 4621 O  O   . HOH P 8 .   ? -28.713 -10.612 23.912  1.00 29.72 ? 542 HOH B O   1 
HETATM 4622 O  O   . HOH P 8 .   ? -27.446 -6.844  2.054   1.00 25.35 ? 543 HOH B O   1 
HETATM 4623 O  O   . HOH P 8 .   ? -5.122  -22.261 4.998   1.00 23.21 ? 544 HOH B O   1 
HETATM 4624 O  O   . HOH P 8 .   ? -27.688 -1.408  3.232   1.00 40.50 ? 545 HOH B O   1 
HETATM 4625 O  O   . HOH P 8 .   ? -10.917 -24.699 5.942   1.00 26.36 ? 546 HOH B O   1 
HETATM 4626 O  O   . HOH P 8 .   ? -19.484 -16.629 31.152  1.00 30.38 ? 547 HOH B O   1 
HETATM 4627 O  O   . HOH P 8 .   ? -26.496 -1.978  31.871  1.00 30.30 ? 548 HOH B O   1 
HETATM 4628 O  O   . HOH P 8 .   ? -23.979 -6.355  16.322  1.00 21.09 ? 549 HOH B O   1 
HETATM 4629 O  O   . HOH P 8 .   ? -19.969 12.675  11.635  1.00 23.74 ? 550 HOH B O   1 
HETATM 4630 O  O   . HOH P 8 .   ? -18.187 -20.450 29.468  1.00 29.22 ? 551 HOH B O   1 
HETATM 4631 O  O   . HOH P 8 .   ? -10.288 -22.943 4.193   1.00 24.16 ? 552 HOH B O   1 
HETATM 4632 O  O   . HOH P 8 .   ? -0.926  -23.513 4.439   1.00 30.15 ? 553 HOH B O   1 
HETATM 4633 O  O   . HOH P 8 .   ? -8.468  3.913   33.261  1.00 38.49 ? 554 HOH B O   1 
HETATM 4634 O  O   . HOH P 8 .   ? 5.183   -21.921 16.781  1.00 30.38 ? 555 HOH B O   1 
HETATM 4635 O  O   . HOH P 8 .   ? -20.877 -19.205 7.418   1.00 18.65 ? 556 HOH B O   1 
HETATM 4636 O  O   . HOH P 8 .   ? 7.482   -3.382  10.001  1.00 25.04 ? 557 HOH B O   1 
HETATM 4637 O  O   . HOH P 8 .   ? -2.088  -21.108 28.024  1.00 30.21 ? 558 HOH B O   1 
HETATM 4638 O  O   . HOH P 8 .   ? 12.865  2.569   17.829  1.00 29.06 ? 559 HOH B O   1 
HETATM 4639 O  O   . HOH P 8 .   ? -14.933 -11.339 37.687  1.00 27.39 ? 560 HOH B O   1 
HETATM 4640 O  O   . HOH P 8 .   ? -22.132 -14.849 0.418   1.00 22.82 ? 561 HOH B O   1 
HETATM 4641 O  O   . HOH P 8 .   ? 0.815   -3.157  27.388  1.00 26.10 ? 562 HOH B O   1 
HETATM 4642 O  O   . HOH P 8 .   ? -10.703 -14.612 34.914  1.00 29.43 ? 563 HOH B O   1 
HETATM 4643 O  O   . HOH P 8 .   ? -5.129  -31.554 26.932  1.00 36.82 ? 564 HOH B O   1 
HETATM 4644 O  O   . HOH P 8 .   ? -16.624 -17.056 31.096  1.00 31.13 ? 565 HOH B O   1 
HETATM 4645 O  O   . HOH P 8 .   ? -0.231  3.777   1.117   1.00 31.47 ? 566 HOH B O   1 
HETATM 4646 O  O   . HOH P 8 .   ? -28.356 0.604   10.751  1.00 24.81 ? 567 HOH B O   1 
HETATM 4647 O  O   . HOH P 8 .   ? 9.825   -17.185 7.153   1.00 29.63 ? 568 HOH B O   1 
HETATM 4648 O  O   . HOH P 8 .   ? -13.170 -15.392 34.551  1.00 28.64 ? 569 HOH B O   1 
HETATM 4649 O  O   . HOH P 8 .   ? -4.369  -10.878 -8.347  1.00 34.69 ? 570 HOH B O   1 
HETATM 4650 O  O   . HOH P 8 .   ? -19.836 1.325   24.686  1.00 25.60 ? 571 HOH B O   1 
HETATM 4651 O  O   . HOH P 8 .   ? -0.122  -28.592 8.024   1.00 45.83 ? 572 HOH B O   1 
HETATM 4652 O  O   . HOH P 8 .   ? -9.414  15.549  3.084   1.00 29.40 ? 573 HOH B O   1 
HETATM 4653 O  O   . HOH P 8 .   ? -26.384 -0.029  5.350   1.00 28.99 ? 574 HOH B O   1 
HETATM 4654 O  O   . HOH P 8 .   ? -8.422  -27.827 8.329   1.00 27.36 ? 575 HOH B O   1 
HETATM 4655 O  O   . HOH P 8 .   ? 6.030   1.550   6.010   1.00 28.85 ? 576 HOH B O   1 
HETATM 4656 O  O   . HOH P 8 .   ? -23.960 -4.452  26.330  1.00 28.63 ? 577 HOH B O   1 
HETATM 4657 O  O   . HOH P 8 .   ? -18.474 -2.024  31.545  1.00 29.27 ? 578 HOH B O   1 
HETATM 4658 O  O   . HOH P 8 .   ? 4.185   -18.276 23.057  1.00 19.66 ? 579 HOH B O   1 
HETATM 4659 O  O   . HOH P 8 .   ? -3.154  6.289   3.440   1.00 25.53 ? 580 HOH B O   1 
HETATM 4660 O  O   . HOH P 8 .   ? -3.101  8.635   9.090   1.00 31.89 ? 581 HOH B O   1 
HETATM 4661 O  O   . HOH P 8 .   ? -17.194 -24.588 4.040   1.00 28.69 ? 582 HOH B O   1 
HETATM 4662 O  O   . HOH P 8 .   ? -27.157 -2.515  -1.416  1.00 29.81 ? 583 HOH B O   1 
HETATM 4663 O  O   . HOH P 8 .   ? -27.790 -1.230  23.553  1.00 33.17 ? 584 HOH B O   1 
HETATM 4664 O  O   . HOH P 8 .   ? -7.873  -12.326 -5.758  1.00 27.45 ? 585 HOH B O   1 
HETATM 4665 O  O   . HOH P 8 .   ? -2.574  7.814   0.231   1.00 36.66 ? 586 HOH B O   1 
HETATM 4666 O  O   . HOH P 8 .   ? -13.747 7.852   -4.311  1.00 35.26 ? 587 HOH B O   1 
HETATM 4667 O  O   . HOH P 8 .   ? 8.254   -7.272  7.876   1.00 34.38 ? 588 HOH B O   1 
HETATM 4668 O  O   . HOH P 8 .   ? -1.674  -16.760 24.477  1.00 15.64 ? 589 HOH B O   1 
HETATM 4669 O  O   . HOH P 8 .   ? -21.539 -0.886  34.788  1.00 15.65 ? 590 HOH B O   1 
HETATM 4670 O  O   . HOH P 8 .   ? 0.596   -17.733 25.656  1.00 18.71 ? 591 HOH B O   1 
HETATM 4671 O  O   . HOH P 8 .   ? 2.144   -15.791 26.844  1.00 21.07 ? 592 HOH B O   1 
HETATM 4672 O  O   . HOH P 8 .   ? 2.480   -2.895  4.723   1.00 23.78 ? 593 HOH B O   1 
HETATM 4673 O  O   . HOH P 8 .   ? -1.786  -31.251 22.891  1.00 29.47 ? 594 HOH B O   1 
HETATM 4674 O  O   . HOH P 8 .   ? -12.808 -27.557 7.985   1.00 32.29 ? 595 HOH B O   1 
HETATM 4675 O  O   . HOH P 8 .   ? -3.352  -24.203 5.832   1.00 29.64 ? 596 HOH B O   1 
HETATM 4676 O  O   . HOH P 8 .   ? -18.628 -17.312 4.331   1.00 27.71 ? 597 HOH B O   1 
HETATM 4677 O  O   . HOH P 8 .   ? -26.690 8.859   11.929  1.00 24.56 ? 598 HOH B O   1 
HETATM 4678 O  O   . HOH P 8 .   ? 8.481   -22.646 18.642  1.00 35.75 ? 599 HOH B O   1 
HETATM 4679 O  O   . HOH P 8 .   ? 8.774   -15.573 8.386   1.00 31.18 ? 600 HOH B O   1 
HETATM 4680 O  O   . HOH P 8 .   ? -9.198  2.642   16.762  1.00 38.45 ? 601 HOH B O   1 
HETATM 4681 O  O   . HOH P 8 .   ? -11.871 -28.119 27.946  1.00 26.86 ? 602 HOH B O   1 
HETATM 4682 O  O   . HOH P 8 .   ? -22.059 10.779  8.363   1.00 28.58 ? 603 HOH B O   1 
HETATM 4683 O  O   . HOH P 8 .   ? -16.891 7.920   -1.411  1.00 34.27 ? 604 HOH B O   1 
HETATM 4684 O  O   . HOH P 8 .   ? -14.412 -21.779 27.989  1.00 24.33 ? 605 HOH B O   1 
HETATM 4685 O  O   . HOH P 8 .   ? -22.021 2.888   26.071  1.00 27.52 ? 606 HOH B O   1 
HETATM 4686 O  O   . HOH P 8 .   ? -0.820  -25.532 26.431  1.00 29.82 ? 607 HOH B O   1 
HETATM 4687 O  O   . HOH P 8 .   ? 8.707   -4.605  7.655   1.00 37.52 ? 608 HOH B O   1 
HETATM 4688 O  O   . HOH P 8 .   ? 6.285   -16.042 12.268  1.00 29.50 ? 609 HOH B O   1 
HETATM 4689 O  O   . HOH P 8 .   ? -18.305 -30.224 10.018  1.00 34.57 ? 610 HOH B O   1 
HETATM 4690 O  O   . HOH P 8 .   ? -13.688 -4.600  -9.501  1.00 28.21 ? 611 HOH B O   1 
HETATM 4691 O  O   . HOH P 8 .   ? -1.710  9.209   6.706   1.00 32.22 ? 612 HOH B O   1 
HETATM 4692 O  O   . HOH P 8 .   ? -30.854 -7.745  22.810  1.00 35.76 ? 613 HOH B O   1 
HETATM 4693 O  O   . HOH P 8 .   ? 12.052  -14.253 15.283  1.00 29.62 ? 614 HOH B O   1 
HETATM 4694 O  O   . HOH P 8 .   ? -0.650  -29.339 13.053  1.00 31.66 ? 615 HOH B O   1 
HETATM 4695 O  O   . HOH P 8 .   ? -1.997  -14.145 28.902  1.00 43.53 ? 616 HOH B O   1 
HETATM 4696 O  O   . HOH P 8 .   ? 11.434  -24.916 12.044  1.00 32.47 ? 617 HOH B O   1 
HETATM 4697 O  O   . HOH P 8 .   ? -1.373  -21.190 2.579   1.00 34.27 ? 618 HOH B O   1 
HETATM 4698 O  O   . HOH P 8 .   ? 1.936   -13.106 26.744  1.00 25.90 ? 619 HOH B O   1 
HETATM 4699 O  O   . HOH P 8 .   ? -0.521  -19.411 27.832  1.00 37.53 ? 620 HOH B O   1 
HETATM 4700 O  O   . HOH P 8 .   ? -7.285  -16.585 -1.317  1.00 29.08 ? 621 HOH B O   1 
HETATM 4701 O  O   . HOH P 8 .   ? -7.751  -22.595 3.899   1.00 40.07 ? 622 HOH B O   1 
HETATM 4702 O  O   . HOH P 8 .   ? -4.926  3.220   17.256  1.00 35.47 ? 623 HOH B O   1 
HETATM 4703 O  O   . HOH P 8 .   ? -12.784 -18.017 34.459  1.00 32.79 ? 624 HOH B O   1 
HETATM 4704 O  O   . HOH P 8 .   ? -23.791 -19.098 -3.323  1.00 29.25 ? 625 HOH B O   1 
HETATM 4705 O  O   . HOH P 8 .   ? -8.889  -23.044 28.800  1.00 30.91 ? 626 HOH B O   1 
HETATM 4706 O  O   . HOH P 8 .   ? 1.141   -0.849  28.768  1.00 30.33 ? 627 HOH B O   1 
HETATM 4707 O  O   . HOH P 8 .   ? -20.034 8.199   18.986  1.00 35.66 ? 628 HOH B O   1 
HETATM 4708 O  O   . HOH P 8 .   ? -10.225 -15.579 -4.423  1.00 27.25 ? 629 HOH B O   1 
HETATM 4709 O  O   . HOH P 8 .   ? -0.663  -16.384 -2.577  1.00 38.75 ? 630 HOH B O   1 
HETATM 4710 O  O   . HOH P 8 .   ? -31.064 -8.827  19.680  1.00 30.67 ? 631 HOH B O   1 
HETATM 4711 O  O   . HOH P 8 .   ? -16.296 5.895   16.630  1.00 35.42 ? 632 HOH B O   1 
HETATM 4712 O  O   . HOH P 8 .   ? 10.409  -18.281 16.389  1.00 25.28 ? 633 HOH B O   1 
HETATM 4713 O  O   . HOH P 8 .   ? -15.853 -8.961  -10.484 1.00 40.92 ? 634 HOH B O   1 
HETATM 4714 O  O   . HOH P 8 .   ? -10.677 14.388  11.875  1.00 31.84 ? 635 HOH B O   1 
HETATM 4715 O  O   . HOH P 8 .   ? -10.998 -11.085 38.505  1.00 33.15 ? 636 HOH B O   1 
HETATM 4716 O  O   . HOH P 8 .   ? 8.404   -13.557 24.304  1.00 27.82 ? 637 HOH B O   1 
HETATM 4717 O  O   . HOH P 8 .   ? -29.977 -0.959  19.039  1.00 29.60 ? 638 HOH B O   1 
HETATM 4718 O  O   . HOH P 8 .   ? -13.647 15.363  8.798   1.00 29.30 ? 639 HOH B O   1 
HETATM 4719 O  O   . HOH P 8 .   ? -13.120 8.783   14.093  1.00 43.29 ? 640 HOH B O   1 
HETATM 4720 O  O   . HOH P 8 .   ? 7.403   -21.472 15.175  1.00 34.27 ? 641 HOH B O   1 
HETATM 4721 O  O   . HOH P 8 .   ? -0.999  -29.573 25.541  1.00 38.80 ? 642 HOH B O   1 
HETATM 4722 O  O   . HOH P 8 .   ? -6.548  2.730   15.051  1.00 33.95 ? 643 HOH B O   1 
HETATM 4723 O  O   . HOH P 8 .   ? -13.620 2.658   17.628  1.00 45.78 ? 644 HOH B O   1 
HETATM 4724 O  O   . HOH P 8 .   ? -13.409 5.178   14.209  1.00 27.45 ? 645 HOH B O   1 
HETATM 4725 O  O   . HOH P 8 .   ? -2.736  9.260   13.269  1.00 35.84 ? 646 HOH B O   1 
HETATM 4726 O  O   . HOH P 8 .   ? -3.271  6.977   17.558  1.00 41.52 ? 647 HOH B O   1 
HETATM 4727 O  O   . HOH P 8 .   ? -8.600  8.855   14.393  1.00 33.62 ? 648 HOH B O   1 
HETATM 4728 O  O   . HOH P 8 .   ? -6.095  14.640  10.601  1.00 36.98 ? 649 HOH B O   1 
HETATM 4729 O  O   . HOH P 8 .   ? 4.548   -0.752  4.937   1.00 39.33 ? 650 HOH B O   1 
HETATM 4730 O  O   . HOH P 8 .   ? 6.220   -5.586  3.626   1.00 37.08 ? 651 HOH B O   1 
HETATM 4731 O  O   . HOH P 8 .   ? 11.278  -0.564  10.957  1.00 41.82 ? 652 HOH B O   1 
HETATM 4732 O  O   . HOH P 8 .   ? 12.102  0.543   18.779  1.00 38.97 ? 653 HOH B O   1 
HETATM 4733 O  O   . HOH P 8 .   ? 11.067  -2.833  22.342  1.00 42.71 ? 654 HOH B O   1 
HETATM 4734 O  O   . HOH P 8 .   ? 13.033  -6.120  16.725  1.00 41.66 ? 655 HOH B O   1 
HETATM 4735 O  O   . HOH P 8 .   ? 10.691  9.417   19.183  1.00 30.72 ? 656 HOH B O   1 
HETATM 4736 O  O   . HOH P 8 .   ? 14.922  2.952   17.016  1.00 37.07 ? 657 HOH B O   1 
HETATM 4737 O  O   . HOH P 8 .   ? 4.035   -0.646  25.315  1.00 31.45 ? 658 HOH B O   1 
HETATM 4738 O  O   . HOH P 8 .   ? 1.609   2.715   27.097  1.00 39.16 ? 659 HOH B O   1 
HETATM 4739 O  O   . HOH P 8 .   ? 2.857   0.659   27.693  1.00 36.51 ? 660 HOH B O   1 
HETATM 4740 O  O   . HOH P 8 .   ? -4.775  3.821   26.609  1.00 39.18 ? 661 HOH B O   1 
HETATM 4741 O  O   . HOH P 8 .   ? 8.184   -26.695 8.320   1.00 32.55 ? 662 HOH B O   1 
HETATM 4742 O  O   . HOH P 8 .   ? 5.289   -28.237 14.574  1.00 37.44 ? 663 HOH B O   1 
HETATM 4743 O  O   . HOH P 8 .   ? 1.375   -30.459 16.371  1.00 36.97 ? 664 HOH B O   1 
HETATM 4744 O  O   . HOH P 8 .   ? 1.200   -30.974 19.553  1.00 38.52 ? 665 HOH B O   1 
HETATM 4745 O  O   . HOH P 8 .   ? 5.310   -21.043 14.285  1.00 36.12 ? 666 HOH B O   1 
HETATM 4746 O  O   . HOH P 8 .   ? -10.948 -29.150 23.145  1.00 37.22 ? 667 HOH B O   1 
HETATM 4747 O  O   . HOH P 8 .   ? -22.696 -13.513 28.967  1.00 41.18 ? 668 HOH B O   1 
HETATM 4748 O  O   . HOH P 8 .   ? -20.705 -11.422 34.702  1.00 31.64 ? 669 HOH B O   1 
HETATM 4749 O  O   . HOH P 8 .   ? -30.044 -9.546  12.560  1.00 40.24 ? 670 HOH B O   1 
HETATM 4750 O  O   . HOH P 8 .   ? -30.655 -2.222  16.938  1.00 31.68 ? 671 HOH B O   1 
HETATM 4751 O  O   . HOH P 8 .   ? -26.814 -3.248  23.056  1.00 36.39 ? 672 HOH B O   1 
HETATM 4752 O  O   . HOH P 8 .   ? -21.701 3.979   29.477  1.00 36.51 ? 673 HOH B O   1 
HETATM 4753 O  O   . HOH P 8 .   ? -26.935 -1.171  26.924  1.00 34.72 ? 674 HOH B O   1 
HETATM 4754 O  O   . HOH P 8 .   ? -8.992  -21.557 31.388  1.00 39.73 ? 675 HOH B O   1 
HETATM 4755 O  O   . HOH P 8 .   ? -0.261  -6.215  -3.861  1.00 30.95 ? 676 HOH B O   1 
HETATM 4756 O  O   . HOH P 8 .   ? 1.511   -5.283  -5.755  1.00 30.09 ? 677 HOH B O   1 
HETATM 4757 O  O   . HOH P 8 .   ? -7.358  -20.452 1.974   1.00 34.34 ? 678 HOH B O   1 
HETATM 4758 O  O   . HOH P 8 .   ? -9.528  -26.771 5.256   1.00 41.04 ? 679 HOH B O   1 
HETATM 4759 O  O   . HOH P 8 .   ? -15.803 -28.236 13.530  1.00 30.89 ? 680 HOH B O   1 
HETATM 4760 O  O   . HOH P 8 .   ? -1.479  -5.183  36.862  1.00 35.39 ? 681 HOH B O   1 
HETATM 4761 O  O   . HOH P 8 .   ? -14.337 -12.599 -8.385  1.00 39.90 ? 682 HOH B O   1 
HETATM 4762 O  O   . HOH P 8 .   ? -15.494 -19.859 0.213   1.00 33.90 ? 683 HOH B O   1 
HETATM 4763 O  O   . HOH P 8 .   ? -20.634 -18.986 4.686   1.00 26.81 ? 684 HOH B O   1 
HETATM 4764 O  O   . HOH P 8 .   ? -21.755 -15.383 5.556   1.00 33.62 ? 685 HOH B O   1 
HETATM 4765 O  O   . HOH P 8 .   ? -27.609 -10.669 4.581   1.00 37.85 ? 686 HOH B O   1 
HETATM 4766 O  O   . HOH P 8 .   ? -24.100 4.133   -1.070  1.00 38.44 ? 687 HOH B O   1 
HETATM 4767 O  O   . HOH P 8 .   ? -14.303 5.951   -7.740  1.00 33.09 ? 688 HOH B O   1 
HETATM 4768 O  O   . HOH P 8 .   ? -16.950 5.294   -3.001  1.00 39.67 ? 689 HOH B O   1 
HETATM 4769 O  O   . HOH P 8 .   ? -13.871 -1.891  -8.573  1.00 37.91 ? 690 HOH B O   1 
HETATM 4770 O  O   . HOH P 8 .   ? 9.800   -10.756 10.067  1.00 36.44 ? 691 HOH B O   1 
HETATM 4771 O  O   . HOH P 8 .   ? 14.253  -12.472 15.385  1.00 45.60 ? 692 HOH B O   1 
HETATM 4772 O  O   . HOH P 8 .   ? -9.763  -20.416 0.369   1.00 36.54 ? 693 HOH B O   1 
HETATM 4773 O  O   . HOH P 8 .   ? -14.235 -22.221 34.278  1.00 34.40 ? 694 HOH B O   1 
HETATM 4774 O  O   . HOH P 8 .   ? -24.632 -8.113  31.188  1.00 32.89 ? 695 HOH B O   1 
HETATM 4775 O  O   . HOH P 8 .   ? -30.192 2.149   11.763  1.00 30.00 ? 696 HOH B O   1 
HETATM 4776 O  O   . HOH P 8 .   ? 6.748   -30.963 4.440   1.00 30.00 ? 697 HOH B O   1 
HETATM 4777 O  O   . HOH P 8 .   ? 9.063   -28.605 6.989   1.00 30.00 ? 698 HOH B O   1 
HETATM 4778 O  O   . HOH P 8 .   ? 8.946   11.235  2.698   1.00 30.00 ? 699 HOH B O   1 
HETATM 4779 O  O   . HOH Q 8 .   ? -22.382 -32.155 31.393  1.00 11.13 ? 401 HOH A O   1 
HETATM 4780 O  O   . HOH Q 8 .   ? -27.659 -39.802 14.510  1.00 13.42 ? 402 HOH A O   1 
HETATM 4781 O  O   . HOH Q 8 .   ? -37.283 -18.265 7.505   1.00 21.00 ? 403 HOH A O   1 
HETATM 4782 O  O   . HOH Q 8 .   ? -28.760 -45.534 17.176  1.00 17.06 ? 404 HOH A O   1 
HETATM 4783 O  O   . HOH Q 8 .   ? -17.225 -31.158 29.373  1.00 13.90 ? 405 HOH A O   1 
HETATM 4784 O  O   . HOH Q 8 .   ? -20.410 -31.963 10.987  1.00 13.86 ? 406 HOH A O   1 
HETATM 4785 O  O   . HOH Q 8 .   ? -22.152 -25.108 14.077  1.00 14.82 ? 407 HOH A O   1 
HETATM 4786 O  O   . HOH Q 8 .   ? -34.964 -28.215 6.087   1.00 11.73 ? 408 HOH A O   1 
HETATM 4787 O  O   . HOH Q 8 .   ? -28.478 -27.756 10.027  1.00 10.89 ? 409 HOH A O   1 
HETATM 4788 O  O   . HOH Q 8 .   ? -31.884 -42.338 35.103  1.00 16.32 ? 410 HOH A O   1 
HETATM 4789 O  O   . HOH Q 8 .   ? -30.090 -47.394 14.813  1.00 20.30 ? 411 HOH A O   1 
HETATM 4790 O  O   . HOH Q 8 .   ? -33.245 -23.622 15.043  1.00 11.50 ? 412 HOH A O   1 
HETATM 4791 O  O   . HOH Q 8 .   ? -16.374 -22.565 26.339  1.00 14.82 ? 413 HOH A O   1 
HETATM 4792 O  O   . HOH Q 8 .   ? -37.690 -28.449 6.191   1.00 13.98 ? 414 HOH A O   1 
HETATM 4793 O  O   . HOH Q 8 .   ? -31.747 -22.398 13.139  1.00 12.57 ? 415 HOH A O   1 
HETATM 4794 O  O   . HOH Q 8 .   ? -24.523 -17.340 20.622  1.00 12.64 ? 416 HOH A O   1 
HETATM 4795 O  O   . HOH Q 8 .   ? -19.836 -21.112 19.985  1.00 11.57 ? 417 HOH A O   1 
HETATM 4796 O  O   . HOH Q 8 .   ? -42.591 -25.287 23.138  1.00 14.84 ? 418 HOH A O   1 
HETATM 4797 O  O   . HOH Q 8 .   ? -25.417 -49.050 30.150  1.00 14.62 ? 419 HOH A O   1 
HETATM 4798 O  O   . HOH Q 8 .   ? -23.639 -37.837 11.512  1.00 12.80 ? 420 HOH A O   1 
HETATM 4799 O  O   . HOH Q 8 .   ? -28.901 -25.748 46.897  1.00 14.55 ? 421 HOH A O   1 
HETATM 4800 O  O   . HOH Q 8 .   ? -29.849 -51.055 24.474  1.00 16.24 ? 422 HOH A O   1 
HETATM 4801 O  O   . HOH Q 8 .   ? -27.423 -43.972 15.472  1.00 18.94 ? 423 HOH A O   1 
HETATM 4802 O  O   . HOH Q 8 .   ? -34.266 -49.597 15.711  1.00 17.49 ? 424 HOH A O   1 
HETATM 4803 O  O   . HOH Q 8 .   ? -22.043 -21.663 8.325   1.00 18.80 ? 425 HOH A O   1 
HETATM 4804 O  O   . HOH Q 8 .   ? -24.963 -54.848 28.085  1.00 24.86 ? 426 HOH A O   1 
HETATM 4805 O  O   . HOH Q 8 .   ? -35.951 -47.336 16.137  1.00 15.11 ? 427 HOH A O   1 
HETATM 4806 O  O   . HOH Q 8 .   ? -22.139 -45.837 35.487  1.00 17.71 ? 428 HOH A O   1 
HETATM 4807 O  O   . HOH Q 8 .   ? -32.525 -52.560 18.491  1.00 18.82 ? 429 HOH A O   1 
HETATM 4808 O  O   . HOH Q 8 .   ? -29.320 -12.864 17.132  1.00 17.99 ? 430 HOH A O   1 
HETATM 4809 O  O   . HOH Q 8 .   ? -24.511 -22.914 33.037  1.00 20.72 ? 431 HOH A O   1 
HETATM 4810 O  O   . HOH Q 8 .   ? -20.820 -41.838 18.418  1.00 20.89 ? 432 HOH A O   1 
HETATM 4811 O  O   . HOH Q 8 .   ? -42.365 -19.208 37.422  1.00 23.02 ? 433 HOH A O   1 
HETATM 4812 O  O   . HOH Q 8 .   ? -8.907  -31.604 14.350  1.00 24.10 ? 434 HOH A O   1 
HETATM 4813 O  O   . HOH Q 8 .   ? -23.277 -39.441 13.786  1.00 20.12 ? 435 HOH A O   1 
HETATM 4814 O  O   . HOH Q 8 .   ? -28.602 -28.052 48.553  1.00 18.70 ? 436 HOH A O   1 
HETATM 4815 O  O   . HOH Q 8 .   ? -33.734 -19.344 38.526  1.00 17.33 ? 437 HOH A O   1 
HETATM 4816 O  O   . HOH Q 8 .   ? -17.906 -23.516 13.240  1.00 18.06 ? 438 HOH A O   1 
HETATM 4817 O  O   . HOH Q 8 .   ? -14.388 -46.699 34.912  1.00 19.14 ? 439 HOH A O   1 
HETATM 4818 O  O   . HOH Q 8 .   ? -37.751 -48.051 30.103  1.00 17.93 ? 440 HOH A O   1 
HETATM 4819 O  O   . HOH Q 8 .   ? -25.925 -43.224 40.848  1.00 23.23 ? 441 HOH A O   1 
HETATM 4820 O  O   . HOH Q 8 .   ? -25.048 -25.161 8.580   1.00 20.17 ? 442 HOH A O   1 
HETATM 4821 O  O   . HOH Q 8 .   ? -15.636 -24.788 16.528  1.00 15.18 ? 443 HOH A O   1 
HETATM 4822 O  O   . HOH Q 8 .   ? -51.111 -21.794 26.289  1.00 23.60 ? 444 HOH A O   1 
HETATM 4823 O  O   . HOH Q 8 .   ? -14.803 -31.516 30.952  1.00 21.95 ? 445 HOH A O   1 
HETATM 4824 O  O   . HOH Q 8 .   ? -14.413 -33.263 19.246  1.00 16.20 ? 446 HOH A O   1 
HETATM 4825 O  O   . HOH Q 8 .   ? -21.608 -49.232 36.821  1.00 19.06 ? 447 HOH A O   1 
HETATM 4826 O  O   . HOH Q 8 .   ? -36.945 -13.284 18.044  1.00 28.69 ? 448 HOH A O   1 
HETATM 4827 O  O   . HOH Q 8 .   ? -11.934 -34.181 20.067  1.00 18.00 ? 449 HOH A O   1 
HETATM 4828 O  O   . HOH Q 8 .   ? -20.485 -39.185 11.155  1.00 23.46 ? 450 HOH A O   1 
HETATM 4829 O  O   . HOH Q 8 .   ? -19.076 -36.370 34.278  1.00 21.77 ? 451 HOH A O   1 
HETATM 4830 O  O   . HOH Q 8 .   ? -18.254 -24.042 35.767  1.00 27.51 ? 452 HOH A O   1 
HETATM 4831 O  O   . HOH Q 8 .   ? -40.173 -50.781 29.296  1.00 21.66 ? 453 HOH A O   1 
HETATM 4832 O  O   . HOH Q 8 .   ? -13.371 -40.991 29.755  1.00 24.96 ? 454 HOH A O   1 
HETATM 4833 O  O   . HOH Q 8 .   ? -35.369 -19.491 40.635  1.00 24.08 ? 455 HOH A O   1 
HETATM 4834 O  O   . HOH Q 8 .   ? -20.224 -47.882 34.756  1.00 19.73 ? 456 HOH A O   1 
HETATM 4835 O  O   . HOH Q 8 .   ? -33.355 -45.292 13.098  1.00 20.66 ? 457 HOH A O   1 
HETATM 4836 O  O   . HOH Q 8 .   ? -36.734 -54.807 20.964  1.00 35.48 ? 458 HOH A O   1 
HETATM 4837 O  O   . HOH Q 8 .   ? -10.517 -35.943 18.544  1.00 21.92 ? 459 HOH A O   1 
HETATM 4838 O  O   . HOH Q 8 .   ? -41.300 -49.783 19.586  1.00 25.81 ? 460 HOH A O   1 
HETATM 4839 O  O   . HOH Q 8 .   ? -37.330 -17.583 38.316  1.00 23.57 ? 461 HOH A O   1 
HETATM 4840 O  O   . HOH Q 8 .   ? -26.762 -15.244 14.284  1.00 16.05 ? 462 HOH A O   1 
HETATM 4841 O  O   . HOH Q 8 .   ? -25.628 -18.154 10.498  1.00 21.19 ? 463 HOH A O   1 
HETATM 4842 O  O   . HOH Q 8 .   ? -7.363  -42.099 18.841  1.00 34.75 ? 464 HOH A O   1 
HETATM 4843 O  O   . HOH Q 8 .   ? -40.511 -47.299 18.411  1.00 22.88 ? 465 HOH A O   1 
HETATM 4844 O  O   . HOH Q 8 .   ? -26.107 -27.538 4.312   1.00 31.95 ? 466 HOH A O   1 
HETATM 4845 O  O   . HOH Q 8 .   ? -31.507 -16.441 32.309  1.00 24.96 ? 467 HOH A O   1 
HETATM 4846 O  O   . HOH Q 8 .   ? -31.029 -24.078 47.279  1.00 14.26 ? 468 HOH A O   1 
HETATM 4847 O  O   . HOH Q 8 .   ? -17.283 -34.205 12.411  1.00 17.48 ? 469 HOH A O   1 
HETATM 4848 O  O   . HOH Q 8 .   ? -25.198 -36.449 7.151   1.00 19.04 ? 470 HOH A O   1 
HETATM 4849 O  O   . HOH Q 8 .   ? -41.148 -47.455 35.829  1.00 24.48 ? 471 HOH A O   1 
HETATM 4850 O  O   . HOH Q 8 .   ? -23.365 -39.974 9.702   1.00 23.02 ? 472 HOH A O   1 
HETATM 4851 O  O   . HOH Q 8 .   ? -35.344 -27.234 13.983  1.00 22.67 ? 473 HOH A O   1 
HETATM 4852 O  O   . HOH Q 8 .   ? -38.567 -48.270 16.561  1.00 19.88 ? 474 HOH A O   1 
HETATM 4853 O  O   . HOH Q 8 .   ? -26.191 -17.672 13.082  1.00 16.43 ? 475 HOH A O   1 
HETATM 4854 O  O   . HOH Q 8 .   ? -38.601 -15.453 31.251  1.00 19.06 ? 476 HOH A O   1 
HETATM 4855 O  O   . HOH Q 8 .   ? -23.845 -32.800 4.607   1.00 21.19 ? 477 HOH A O   1 
HETATM 4856 O  O   . HOH Q 8 .   ? -14.307 -47.105 23.238  1.00 28.39 ? 478 HOH A O   1 
HETATM 4857 O  O   . HOH Q 8 .   ? -33.335 -51.552 27.080  1.00 22.36 ? 479 HOH A O   1 
HETATM 4858 O  O   . HOH Q 8 .   ? -24.341 -46.059 41.490  1.00 18.83 ? 480 HOH A O   1 
HETATM 4859 O  O   . HOH Q 8 .   ? -26.623 -24.550 46.565  1.00 20.12 ? 481 HOH A O   1 
HETATM 4860 O  O   . HOH Q 8 .   ? -35.596 -16.768 13.443  1.00 33.39 ? 482 HOH A O   1 
HETATM 4861 O  O   . HOH Q 8 .   ? -24.333 -40.056 42.505  1.00 20.61 ? 483 HOH A O   1 
HETATM 4862 O  O   . HOH Q 8 .   ? -36.973 -13.570 32.557  1.00 27.66 ? 484 HOH A O   1 
HETATM 4863 O  O   . HOH Q 8 .   ? -43.294 -55.235 24.214  1.00 34.38 ? 485 HOH A O   1 
HETATM 4864 O  O   . HOH Q 8 .   ? -38.348 -46.047 12.515  1.00 28.45 ? 486 HOH A O   1 
HETATM 4865 O  O   . HOH Q 8 .   ? -25.799 -33.234 41.879  1.00 20.54 ? 487 HOH A O   1 
HETATM 4866 O  O   . HOH Q 8 .   ? -44.544 -17.558 34.760  1.00 25.12 ? 488 HOH A O   1 
HETATM 4867 O  O   . HOH Q 8 .   ? -25.131 -22.410 9.168   1.00 20.19 ? 489 HOH A O   1 
HETATM 4868 O  O   . HOH Q 8 .   ? -24.776 -46.812 38.564  1.00 25.37 ? 490 HOH A O   1 
HETATM 4869 O  O   . HOH Q 8 .   ? -14.426 -30.435 20.406  1.00 19.51 ? 491 HOH A O   1 
HETATM 4870 O  O   . HOH Q 8 .   ? -30.037 -21.506 47.101  1.00 16.44 ? 492 HOH A O   1 
HETATM 4871 O  O   . HOH Q 8 .   ? -31.412 -11.732 20.826  1.00 33.14 ? 493 HOH A O   1 
HETATM 4872 O  O   . HOH Q 8 .   ? -12.722 -32.306 23.673  1.00 22.81 ? 494 HOH A O   1 
HETATM 4873 O  O   . HOH Q 8 .   ? -22.052 -19.408 30.709  1.00 22.57 ? 495 HOH A O   1 
HETATM 4874 O  O   . HOH Q 8 .   ? -29.350 -18.388 29.503  1.00 29.52 ? 496 HOH A O   1 
HETATM 4875 O  O   . HOH Q 8 .   ? -18.490 -27.809 36.729  1.00 19.81 ? 497 HOH A O   1 
HETATM 4876 O  O   . HOH Q 8 .   ? -24.919 -39.141 7.559   1.00 21.42 ? 498 HOH A O   1 
HETATM 4877 O  O   . HOH Q 8 .   ? -39.148 -28.519 8.660   1.00 23.95 ? 499 HOH A O   1 
HETATM 4878 O  O   . HOH Q 8 .   ? -19.864 -25.589 34.476  1.00 21.72 ? 500 HOH A O   1 
HETATM 4879 O  O   . HOH Q 8 .   ? -38.866 -50.987 16.164  1.00 25.33 ? 501 HOH A O   1 
HETATM 4880 O  O   . HOH Q 8 .   ? -45.458 -24.417 37.493  1.00 30.61 ? 502 HOH A O   1 
HETATM 4881 O  O   . HOH Q 8 .   ? -26.437 -17.658 22.721  1.00 24.97 ? 503 HOH A O   1 
HETATM 4882 O  O   . HOH Q 8 .   ? -32.959 -19.680 31.091  1.00 22.43 ? 504 HOH A O   1 
HETATM 4883 O  O   . HOH Q 8 .   ? -31.378 -16.238 27.980  1.00 20.06 ? 505 HOH A O   1 
HETATM 4884 O  O   . HOH Q 8 .   ? -41.838 -26.766 43.579  1.00 26.71 ? 506 HOH A O   1 
HETATM 4885 O  O   . HOH Q 8 .   ? -19.645 -32.966 7.456   1.00 28.86 ? 507 HOH A O   1 
HETATM 4886 O  O   . HOH Q 8 .   ? -21.301 -41.115 14.346  1.00 29.54 ? 508 HOH A O   1 
HETATM 4887 O  O   . HOH Q 8 .   ? -49.171 -19.449 29.096  1.00 28.81 ? 509 HOH A O   1 
HETATM 4888 O  O   . HOH Q 8 .   ? -35.227 -26.610 47.990  1.00 23.59 ? 510 HOH A O   1 
HETATM 4889 O  O   . HOH Q 8 .   ? -13.727 -28.280 25.030  1.00 19.03 ? 511 HOH A O   1 
HETATM 4890 O  O   . HOH Q 8 .   ? -43.541 -15.156 27.808  1.00 31.38 ? 512 HOH A O   1 
HETATM 4891 O  O   . HOH Q 8 .   ? -20.856 -22.483 27.193  1.00 21.87 ? 513 HOH A O   1 
HETATM 4892 O  O   . HOH Q 8 .   ? -43.129 -25.334 18.503  1.00 36.96 ? 514 HOH A O   1 
HETATM 4893 O  O   . HOH Q 8 .   ? -28.851 -50.813 32.450  1.00 17.72 ? 515 HOH A O   1 
HETATM 4894 O  O   . HOH Q 8 .   ? -21.808 -38.402 43.904  1.00 36.74 ? 516 HOH A O   1 
HETATM 4895 O  O   . HOH Q 8 .   ? -48.663 -54.749 24.707  1.00 25.88 ? 517 HOH A O   1 
HETATM 4896 O  O   . HOH Q 8 .   ? -33.030 -19.972 13.450  1.00 20.26 ? 518 HOH A O   1 
HETATM 4897 O  O   . HOH Q 8 .   ? -27.639 -31.199 1.670   1.00 34.15 ? 519 HOH A O   1 
HETATM 4898 O  O   . HOH Q 8 .   ? -14.399 -24.977 34.745  1.00 34.49 ? 520 HOH A O   1 
HETATM 4899 O  O   . HOH Q 8 .   ? -15.492 -53.053 35.630  1.00 29.31 ? 521 HOH A O   1 
HETATM 4900 O  O   . HOH Q 8 .   ? -14.875 -30.321 22.857  1.00 26.06 ? 522 HOH A O   1 
HETATM 4901 O  O   . HOH Q 8 .   ? -21.687 -23.531 33.971  1.00 27.05 ? 523 HOH A O   1 
HETATM 4902 O  O   . HOH Q 8 .   ? -18.763 -40.665 14.078  1.00 26.76 ? 524 HOH A O   1 
HETATM 4903 O  O   . HOH Q 8 .   ? -14.968 -25.806 25.474  1.00 21.98 ? 525 HOH A O   1 
HETATM 4904 O  O   . HOH Q 8 .   ? -20.920 -26.118 7.407   1.00 22.04 ? 526 HOH A O   1 
HETATM 4905 O  O   . HOH Q 8 .   ? -27.011 -35.451 42.522  1.00 28.05 ? 527 HOH A O   1 
HETATM 4906 O  O   . HOH Q 8 .   ? -48.332 -18.072 24.044  1.00 30.77 ? 528 HOH A O   1 
HETATM 4907 O  O   . HOH Q 8 .   ? -38.943 -53.477 18.210  1.00 30.65 ? 529 HOH A O   1 
HETATM 4908 O  O   . HOH Q 8 .   ? -24.708 -35.471 4.642   1.00 26.93 ? 530 HOH A O   1 
HETATM 4909 O  O   . HOH Q 8 .   ? -21.388 -28.259 43.602  1.00 36.70 ? 531 HOH A O   1 
HETATM 4910 O  O   . HOH Q 8 .   ? -31.849 -53.519 26.004  1.00 25.98 ? 532 HOH A O   1 
HETATM 4911 O  O   . HOH Q 8 .   ? -37.470 -25.092 47.594  1.00 22.91 ? 533 HOH A O   1 
HETATM 4912 O  O   . HOH Q 8 .   ? -26.733 -45.810 39.823  1.00 24.20 ? 534 HOH A O   1 
HETATM 4913 O  O   . HOH Q 8 .   ? -34.502 -12.680 26.729  1.00 34.04 ? 535 HOH A O   1 
HETATM 4914 O  O   . HOH Q 8 .   ? -18.664 -20.538 47.101  1.00 24.53 ? 536 HOH A O   1 
HETATM 4915 O  O   . HOH Q 8 .   ? -19.661 -47.772 29.324  1.00 30.07 ? 537 HOH A O   1 
HETATM 4916 O  O   . HOH Q 8 .   ? -21.142 -32.908 4.876   1.00 29.53 ? 538 HOH A O   1 
HETATM 4917 O  O   . HOH Q 8 .   ? -40.208 -23.025 12.500  1.00 28.40 ? 539 HOH A O   1 
HETATM 4918 O  O   . HOH Q 8 .   ? -24.523 -18.200 42.259  1.00 29.56 ? 540 HOH A O   1 
HETATM 4919 O  O   . HOH Q 8 .   ? -25.025 -42.525 16.121  1.00 22.16 ? 541 HOH A O   1 
HETATM 4920 O  O   . HOH Q 8 .   ? -27.387 -47.030 14.585  1.00 24.46 ? 542 HOH A O   1 
HETATM 4921 O  O   . HOH Q 8 .   ? -43.079 -24.088 39.184  1.00 30.69 ? 543 HOH A O   1 
HETATM 4922 O  O   . HOH Q 8 .   ? -16.732 -29.919 37.448  1.00 26.81 ? 544 HOH A O   1 
HETATM 4923 O  O   . HOH Q 8 .   ? -13.140 -39.192 32.324  1.00 28.41 ? 545 HOH A O   1 
HETATM 4924 O  O   . HOH Q 8 .   ? -36.620 -43.634 36.628  1.00 27.80 ? 546 HOH A O   1 
HETATM 4925 O  O   . HOH Q 8 .   ? -23.222 -29.248 5.754   1.00 22.79 ? 547 HOH A O   1 
HETATM 4926 O  O   . HOH Q 8 .   ? -20.295 -21.794 31.126  1.00 31.50 ? 548 HOH A O   1 
HETATM 4927 O  O   . HOH Q 8 .   ? -54.056 -27.302 29.809  1.00 25.17 ? 549 HOH A O   1 
HETATM 4928 O  O   . HOH Q 8 .   ? -51.224 -19.842 32.331  1.00 48.50 ? 550 HOH A O   1 
HETATM 4929 O  O   . HOH Q 8 .   ? -23.502 -31.391 44.240  1.00 33.99 ? 551 HOH A O   1 
HETATM 4930 O  O   . HOH Q 8 .   ? -48.322 -48.490 20.811  1.00 34.79 ? 552 HOH A O   1 
HETATM 4931 O  O   . HOH Q 8 .   ? -29.978 -13.720 13.208  1.00 30.26 ? 553 HOH A O   1 
HETATM 4932 O  O   . HOH Q 8 .   ? -11.825 -29.326 20.385  1.00 24.77 ? 554 HOH A O   1 
HETATM 4933 O  O   . HOH Q 8 .   ? -47.097 -15.865 25.422  1.00 25.94 ? 555 HOH A O   1 
HETATM 4934 O  O   . HOH Q 8 .   ? -17.795 -47.688 36.058  1.00 24.43 ? 556 HOH A O   1 
HETATM 4935 O  O   . HOH Q 8 .   ? -11.268 -35.768 35.608  1.00 40.87 ? 557 HOH A O   1 
HETATM 4936 O  O   . HOH Q 8 .   ? -32.080 -23.884 49.993  1.00 20.59 ? 558 HOH A O   1 
HETATM 4937 O  O   . HOH Q 8 .   ? -21.623 -28.799 7.834   1.00 22.58 ? 559 HOH A O   1 
HETATM 4938 O  O   . HOH Q 8 .   ? -14.951 -39.005 34.039  1.00 34.93 ? 560 HOH A O   1 
HETATM 4939 O  O   . HOH Q 8 .   ? -15.845 -31.772 35.317  1.00 33.68 ? 561 HOH A O   1 
HETATM 4940 O  O   . HOH Q 8 .   ? -38.550 -40.898 36.653  1.00 13.12 ? 562 HOH A O   1 
HETATM 4941 O  O   . HOH Q 8 .   ? -33.877 -30.441 5.085   1.00 11.98 ? 563 HOH A O   1 
HETATM 4942 O  O   . HOH Q 8 .   ? -33.487 -34.334 40.864  1.00 12.18 ? 564 HOH A O   1 
HETATM 4943 O  O   . HOH Q 8 .   ? -37.060 -40.167 29.902  1.00 9.78  ? 565 HOH A O   1 
HETATM 4944 O  O   . HOH Q 8 .   ? -39.374 -36.356 29.574  1.00 13.81 ? 566 HOH A O   1 
HETATM 4945 O  O   . HOH Q 8 .   ? -30.032 -40.618 38.085  1.00 17.86 ? 567 HOH A O   1 
HETATM 4946 O  O   . HOH Q 8 .   ? -45.149 -37.379 32.095  1.00 16.97 ? 568 HOH A O   1 
HETATM 4947 O  O   . HOH Q 8 .   ? -38.990 -29.978 11.053  1.00 19.91 ? 569 HOH A O   1 
HETATM 4948 O  O   . HOH Q 8 .   ? -43.226 -37.956 37.943  1.00 17.83 ? 570 HOH A O   1 
HETATM 4949 O  O   . HOH Q 8 .   ? -45.882 -38.697 34.347  1.00 20.62 ? 571 HOH A O   1 
HETATM 4950 O  O   . HOH Q 8 .   ? -40.854 -31.726 11.951  1.00 24.28 ? 572 HOH A O   1 
HETATM 4951 O  O   . HOH Q 8 .   ? -54.353 -30.659 36.116  1.00 22.16 ? 573 HOH A O   1 
HETATM 4952 O  O   . HOH Q 8 .   ? -48.617 -36.078 30.381  1.00 21.52 ? 574 HOH A O   1 
HETATM 4953 O  O   . HOH Q 8 .   ? -34.452 -38.714 42.698  1.00 21.18 ? 575 HOH A O   1 
HETATM 4954 O  O   . HOH Q 8 .   ? -17.071 -48.411 25.647  1.00 23.17 ? 576 HOH A O   1 
HETATM 4955 O  O   . HOH Q 8 .   ? -41.103 -32.844 26.785  1.00 24.30 ? 577 HOH A O   1 
HETATM 4956 O  O   . HOH Q 8 .   ? -43.198 -40.242 39.413  1.00 25.06 ? 578 HOH A O   1 
HETATM 4957 O  O   . HOH Q 8 .   ? -27.411 -56.823 28.633  1.00 29.12 ? 579 HOH A O   1 
HETATM 4958 O  O   . HOH Q 8 .   ? -46.552 -26.119 43.526  1.00 29.30 ? 580 HOH A O   1 
HETATM 4959 O  O   . HOH Q 8 .   ? -48.538 -39.290 33.551  1.00 25.30 ? 581 HOH A O   1 
HETATM 4960 O  O   . HOH Q 8 .   ? -22.317 -42.791 16.401  1.00 26.47 ? 582 HOH A O   1 
HETATM 4961 O  O   . HOH Q 8 .   ? -43.117 -18.383 16.996  1.00 27.75 ? 583 HOH A O   1 
HETATM 4962 O  O   . HOH Q 8 .   ? -29.352 -13.558 24.675  1.00 30.29 ? 584 HOH A O   1 
HETATM 4963 O  O   . HOH Q 8 .   ? -48.200 -39.225 27.146  1.00 35.32 ? 585 HOH A O   1 
HETATM 4964 O  O   . HOH Q 8 .   ? -31.708 -40.696 2.762   1.00 29.91 ? 586 HOH A O   1 
HETATM 4965 O  O   . HOH Q 8 .   ? -19.155 -26.246 38.698  1.00 39.57 ? 587 HOH A O   1 
HETATM 4966 O  O   . HOH Q 8 .   ? -16.275 -54.984 31.696  1.00 26.50 ? 588 HOH A O   1 
HETATM 4967 O  O   . HOH Q 8 .   ? -42.127 -37.968 22.547  1.00 31.69 ? 589 HOH A O   1 
HETATM 4968 O  O   . HOH Q 8 .   ? -45.686 -37.610 36.934  1.00 25.48 ? 590 HOH A O   1 
HETATM 4969 O  O   . HOH Q 8 .   ? -44.236 -54.061 31.713  1.00 43.33 ? 591 HOH A O   1 
HETATM 4970 O  O   . HOH Q 8 .   ? -26.827 -16.908 40.353  1.00 26.39 ? 592 HOH A O   1 
HETATM 4971 O  O   . HOH Q 8 .   ? -16.844 -37.162 35.354  1.00 29.81 ? 593 HOH A O   1 
HETATM 4972 O  O   . HOH Q 8 .   ? -28.755 -34.844 0.880   1.00 28.11 ? 594 HOH A O   1 
HETATM 4973 O  O   . HOH Q 8 .   ? -42.906 -29.033 21.902  1.00 30.65 ? 595 HOH A O   1 
HETATM 4974 O  O   . HOH Q 8 .   ? -48.733 -25.982 23.762  1.00 23.77 ? 596 HOH A O   1 
HETATM 4975 O  O   . HOH Q 8 .   ? -37.773 -51.809 28.781  1.00 34.72 ? 597 HOH A O   1 
HETATM 4976 O  O   . HOH Q 8 .   ? -39.853 -35.269 26.781  1.00 25.90 ? 598 HOH A O   1 
HETATM 4977 O  O   . HOH Q 8 .   ? -36.067 -45.509 13.940  1.00 27.36 ? 599 HOH A O   1 
HETATM 4978 O  O   . HOH Q 8 .   ? -42.458 -46.085 16.764  1.00 31.26 ? 600 HOH A O   1 
HETATM 4979 O  O   . HOH Q 8 .   ? -27.625 -18.763 8.462   1.00 35.02 ? 601 HOH A O   1 
HETATM 4980 O  O   . HOH Q 8 .   ? -34.498 -54.056 17.171  1.00 34.53 ? 602 HOH A O   1 
HETATM 4981 O  O   . HOH Q 8 .   ? -7.865  -33.718 25.554  1.00 34.76 ? 603 HOH A O   1 
HETATM 4982 O  O   . HOH Q 8 .   ? -17.785 -47.304 28.218  1.00 34.74 ? 604 HOH A O   1 
HETATM 4983 O  O   . HOH Q 8 .   ? -24.650 -25.552 47.587  1.00 31.24 ? 605 HOH A O   1 
HETATM 4984 O  O   . HOH Q 8 .   ? -41.319 -14.701 32.025  1.00 30.90 ? 606 HOH A O   1 
HETATM 4985 O  O   . HOH Q 8 .   ? -40.297 -25.333 15.936  1.00 41.34 ? 607 HOH A O   1 
HETATM 4986 O  O   . HOH Q 8 .   ? -15.483 -40.857 36.302  1.00 30.71 ? 608 HOH A O   1 
HETATM 4987 O  O   . HOH Q 8 .   ? -48.792 -17.104 35.048  1.00 38.08 ? 609 HOH A O   1 
HETATM 4988 O  O   . HOH Q 8 .   ? -18.146 -54.464 22.221  1.00 33.43 ? 610 HOH A O   1 
HETATM 4989 O  O   . HOH Q 8 .   ? -22.641 -23.541 36.588  1.00 24.26 ? 611 HOH A O   1 
HETATM 4990 O  O   . HOH Q 8 .   ? -28.023 -41.295 44.002  1.00 41.65 ? 612 HOH A O   1 
HETATM 4991 O  O   . HOH Q 8 .   ? -51.787 -36.883 32.308  1.00 35.41 ? 613 HOH A O   1 
HETATM 4992 O  O   . HOH Q 8 .   ? -8.106  -41.788 12.222  1.00 37.10 ? 614 HOH A O   1 
HETATM 4993 O  O   . HOH Q 8 .   ? -23.884 -21.392 37.871  1.00 32.96 ? 615 HOH A O   1 
HETATM 4994 O  O   . HOH Q 8 .   ? -14.454 -49.302 24.358  1.00 35.71 ? 616 HOH A O   1 
HETATM 4995 O  O   . HOH Q 8 .   ? -58.569 -23.690 28.453  1.00 40.50 ? 617 HOH A O   1 
HETATM 4996 O  O   . HOH Q 8 .   ? -34.851 -11.545 18.641  1.00 42.55 ? 618 HOH A O   1 
HETATM 4997 O  O   . HOH Q 8 .   ? -32.984 -49.238 13.433  1.00 34.07 ? 619 HOH A O   1 
HETATM 4998 O  O   . HOH Q 8 .   ? -38.221 -45.976 36.368  1.00 32.30 ? 620 HOH A O   1 
HETATM 4999 O  O   . HOH Q 8 .   ? -41.319 -20.506 43.442  1.00 36.51 ? 621 HOH A O   1 
HETATM 5000 O  O   . HOH Q 8 .   ? -54.287 -25.321 27.662  1.00 40.31 ? 622 HOH A O   1 
HETATM 5001 O  O   . HOH Q 8 .   ? -24.918 -17.874 38.407  1.00 28.88 ? 623 HOH A O   1 
HETATM 5002 O  O   . HOH Q 8 .   ? -18.072 -31.541 39.091  1.00 33.39 ? 624 HOH A O   1 
HETATM 5003 O  O   . HOH Q 8 .   ? -11.243 -31.721 18.805  1.00 27.84 ? 625 HOH A O   1 
HETATM 5004 O  O   . HOH Q 8 .   ? -42.612 -11.330 25.222  1.00 37.77 ? 626 HOH A O   1 
HETATM 5005 O  O   . HOH Q 8 .   ? -40.679 -42.641 36.896  1.00 28.37 ? 627 HOH A O   1 
HETATM 5006 O  O   . HOH Q 8 .   ? -54.709 -27.994 37.382  1.00 30.21 ? 628 HOH A O   1 
HETATM 5007 O  O   . HOH Q 8 .   ? -11.393 -29.292 25.785  1.00 32.25 ? 629 HOH A O   1 
HETATM 5008 O  O   . HOH Q 8 .   ? -9.146  -33.583 22.856  1.00 33.29 ? 630 HOH A O   1 
HETATM 5009 O  O   . HOH Q 8 .   ? -4.924  -43.042 22.786  1.00 41.87 ? 631 HOH A O   1 
HETATM 5010 O  O   . HOH Q 8 .   ? -7.998  -43.815 25.210  1.00 34.44 ? 632 HOH A O   1 
HETATM 5011 O  O   . HOH Q 8 .   ? -7.177  -44.086 21.791  1.00 42.03 ? 633 HOH A O   1 
HETATM 5012 O  O   . HOH Q 8 .   ? -10.368 -44.799 18.745  1.00 36.90 ? 634 HOH A O   1 
HETATM 5013 O  O   . HOH Q 8 .   ? -13.456 -43.669 14.575  1.00 33.63 ? 635 HOH A O   1 
HETATM 5014 O  O   . HOH Q 8 .   ? -27.122 -14.446 28.810  1.00 29.64 ? 636 HOH A O   1 
HETATM 5015 O  O   . HOH Q 8 .   ? -14.091 -31.290 33.492  1.00 41.82 ? 637 HOH A O   1 
HETATM 5016 O  O   . HOH Q 8 .   ? -16.613 -34.050 35.511  1.00 35.14 ? 638 HOH A O   1 
HETATM 5017 O  O   . HOH Q 8 .   ? -17.954 -40.099 37.655  1.00 34.95 ? 639 HOH A O   1 
HETATM 5018 O  O   . HOH Q 8 .   ? -46.899 -46.575 29.398  1.00 39.51 ? 640 HOH A O   1 
HETATM 5019 O  O   . HOH Q 8 .   ? -46.183 -41.646 21.876  1.00 50.74 ? 641 HOH A O   1 
HETATM 5020 O  O   . HOH Q 8 .   ? -49.007 -36.439 25.499  1.00 37.77 ? 642 HOH A O   1 
HETATM 5021 O  O   . HOH Q 8 .   ? -42.713 -33.408 23.558  1.00 37.15 ? 643 HOH A O   1 
HETATM 5022 O  O   . HOH Q 8 .   ? -41.635 -36.016 24.853  1.00 38.33 ? 644 HOH A O   1 
HETATM 5023 O  O   . HOH Q 8 .   ? -45.108 -29.284 24.289  1.00 31.90 ? 645 HOH A O   1 
HETATM 5024 O  O   . HOH Q 8 .   ? -47.762 -38.437 31.110  1.00 33.37 ? 646 HOH A O   1 
HETATM 5025 O  O   . HOH Q 8 .   ? -47.219 -38.184 39.879  1.00 37.84 ? 647 HOH A O   1 
HETATM 5026 O  O   . HOH Q 8 .   ? -37.467 -52.051 31.568  1.00 38.23 ? 648 HOH A O   1 
HETATM 5027 O  O   . HOH Q 8 .   ? -21.285 -24.188 43.342  1.00 35.69 ? 649 HOH A O   1 
HETATM 5028 O  O   . HOH Q 8 .   ? -32.886 -55.763 27.206  1.00 33.36 ? 650 HOH A O   1 
HETATM 5029 O  O   . HOH Q 8 .   ? -22.476 -37.025 3.630   1.00 31.89 ? 651 HOH A O   1 
HETATM 5030 O  O   . HOH Q 8 .   ? -24.422 -40.145 4.949   1.00 41.75 ? 652 HOH A O   1 
HETATM 5031 O  O   . HOH Q 8 .   ? -32.335 -44.459 37.277  1.00 35.77 ? 653 HOH A O   1 
HETATM 5032 O  O   . HOH Q 8 .   ? -25.945 -43.065 43.383  1.00 29.11 ? 654 HOH A O   1 
HETATM 5033 O  O   . HOH Q 8 .   ? -20.887 -33.150 41.297  1.00 33.98 ? 655 HOH A O   1 
HETATM 5034 O  O   . HOH Q 8 .   ? -34.421 -13.362 31.741  1.00 41.03 ? 656 HOH A O   1 
HETATM 5035 O  O   . HOH Q 8 .   ? -46.470 -15.944 35.783  1.00 36.27 ? 657 HOH A O   1 
HETATM 5036 O  O   . HOH Q 8 .   ? -51.518 -19.390 27.910  1.00 36.98 ? 658 HOH A O   1 
HETATM 5037 O  O   . HOH Q 8 .   ? -40.120 -12.543 17.753  1.00 41.18 ? 659 HOH A O   1 
HETATM 5038 O  O   . HOH Q 8 .   ? -19.328 -45.982 19.310  1.00 34.45 ? 660 HOH A O   1 
HETATM 5039 O  O   . HOH Q 8 .   ? -19.359 -43.735 18.930  1.00 38.62 ? 661 HOH A O   1 
HETATM 5040 O  O   . HOH Q 8 .   ? -9.524  -39.599 30.182  1.00 34.58 ? 662 HOH A O   1 
HETATM 5041 O  O   . HOH Q 8 .   ? -41.521 -32.600 21.686  1.00 38.81 ? 663 HOH A O   1 
HETATM 5042 O  O   . HOH Q 8 .   ? -42.333 -30.596 14.007  1.00 38.48 ? 664 HOH A O   1 
HETATM 5043 O  O   . HOH Q 8 .   ? -18.506 -33.906 38.109  1.00 35.34 ? 665 HOH A O   1 
HETATM 5044 O  O   . HOH Q 8 .   ? -29.114 -41.702 1.866   1.00 36.34 ? 666 HOH A O   1 
HETATM 5045 O  O   . HOH Q 8 .   ? -17.007 -43.113 40.665  1.00 38.85 ? 667 HOH A O   1 
HETATM 5046 O  O   . HOH Q 8 .   ? -25.829 -38.234 43.988  1.00 39.92 ? 668 HOH A O   1 
HETATM 5047 O  O   . HOH Q 8 .   ? -47.393 -33.756 25.079  1.00 30.00 ? 669 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   B . n 
A 1 2   MET 2   2   ?   ?   ?   B . n 
A 1 3   SER 3   3   ?   ?   ?   B . n 
A 1 4   ARG 4   4   ?   ?   ?   B . n 
A 1 5   LEU 5   5   ?   ?   ?   B . n 
A 1 6   SER 6   6   6   SER SER B . n 
A 1 7   TRP 7   7   7   TRP TRP B . n 
A 1 8   GLY 8   8   8   GLY GLY B . n 
A 1 9   TYR 9   9   9   TYR TYR B . n 
A 1 10  ARG 10  10  10  ARG ARG B . n 
A 1 11  GLU 11  11  11  GLU GLU B . n 
A 1 12  HIS 12  12  12  HIS HIS B . n 
A 1 13  ASN 13  13  13  ASN ASN B . n 
A 1 14  GLY 14  14  14  GLY GLY B . n 
A 1 15  PRO 15  15  15  PRO PRO B . n 
A 1 16  ILE 16  16  16  ILE ILE B . n 
A 1 17  HIS 17  17  17  HIS HIS B . n 
A 1 18  TRP 18  18  18  TRP TRP B . n 
A 1 19  LYS 19  19  19  LYS LYS B . n 
A 1 20  GLU 20  20  20  GLU GLU B . n 
A 1 21  PHE 21  21  21  PHE PHE B . n 
A 1 22  PHE 22  22  22  PHE PHE B . n 
A 1 23  PRO 23  23  23  PRO PRO B . n 
A 1 24  ILE 24  24  24  ILE ILE B . n 
A 1 25  ALA 25  25  25  ALA ALA B . n 
A 1 26  ASP 26  26  26  ASP ASP B . n 
A 1 27  GLY 27  27  27  GLY GLY B . n 
A 1 28  ASP 28  28  28  ASP ASP B . n 
A 1 29  GLN 29  29  29  GLN GLN B . n 
A 1 30  GLN 30  30  30  GLN GLN B . n 
A 1 31  SER 31  31  31  SER SER B . n 
A 1 32  PRO 32  32  32  PRO PRO B . n 
A 1 33  ILE 33  33  33  ILE ILE B . n 
A 1 34  GLU 34  34  34  GLU GLU B . n 
A 1 35  ILE 35  35  35  ILE ILE B . n 
A 1 36  LYS 36  36  36  LYS LYS B . n 
A 1 37  THR 37  37  37  THR THR B . n 
A 1 38  LYS 38  38  38  LYS LYS B . n 
A 1 39  GLU 39  39  39  GLU GLU B . n 
A 1 40  VAL 40  40  40  VAL VAL B . n 
A 1 41  LYS 41  41  41  LYS LYS B . n 
A 1 42  TYR 42  42  42  TYR TYR B . n 
A 1 43  ASP 43  43  43  ASP ASP B . n 
A 1 44  SER 44  44  44  SER SER B . n 
A 1 45  SER 45  45  45  SER SER B . n 
A 1 46  LEU 46  46  46  LEU LEU B . n 
A 1 47  ARG 47  47  47  ARG ARG B . n 
A 1 48  PRO 48  48  48  PRO PRO B . n 
A 1 49  LEU 49  49  49  LEU LEU B . n 
A 1 50  SER 50  50  50  SER SER B . n 
A 1 51  ILE 51  51  51  ILE ILE B . n 
A 1 52  LYS 52  52  52  LYS LYS B . n 
A 1 53  TYR 53  53  53  TYR TYR B . n 
A 1 54  ASP 54  54  54  ASP ASP B . n 
A 1 55  PRO 55  55  55  PRO PRO B . n 
A 1 56  SER 56  56  56  SER SER B . n 
A 1 57  SER 57  57  57  SER SER B . n 
A 1 58  ALA 58  58  58  ALA ALA B . n 
A 1 59  LYS 59  59  59  LYS LYS B . n 
A 1 60  ILE 60  60  60  ILE ILE B . n 
A 1 61  ILE 61  61  61  ILE ILE B . n 
A 1 62  SER 62  62  62  SER SER B . n 
A 1 63  ASN 63  63  63  ASN ASN B . n 
A 1 64  SER 64  64  64  SER SER B . n 
A 1 65  GLY 65  65  65  GLY GLY B . n 
A 1 66  HIS 66  66  66  HIS HIS B . n 
A 1 67  SER 67  67  67  SER SER B . n 
A 1 68  PHE 68  68  68  PHE PHE B . n 
A 1 69  ASN 69  69  69  ASN ASN B . n 
A 1 70  VAL 70  70  70  VAL VAL B . n 
A 1 71  ASP 71  71  71  ASP ASP B . n 
A 1 72  PHE 72  72  72  PHE PHE B . n 
A 1 73  ASP 73  73  73  ASP ASP B . n 
A 1 74  ASP 74  74  74  ASP ASP B . n 
A 1 75  THR 75  75  75  THR THR B . n 
A 1 76  GLU 76  76  76  GLU GLU B . n 
A 1 77  ASN 77  77  77  ASN ASN B . n 
A 1 78  LYS 78  78  78  LYS LYS B . n 
A 1 79  SER 79  79  79  SER SER B . n 
A 1 80  VAL 80  80  80  VAL VAL B . n 
A 1 81  LEU 81  81  81  LEU LEU B . n 
A 1 82  ARG 82  82  82  ARG ARG B . n 
A 1 83  GLY 83  83  83  GLY GLY B . n 
A 1 84  GLY 84  84  84  GLY GLY B . n 
A 1 85  PRO 85  85  85  PRO PRO B . n 
A 1 86  LEU 86  86  86  LEU LEU B . n 
A 1 87  THR 87  87  87  THR THR B . n 
A 1 88  GLY 88  88  88  GLY GLY B . n 
A 1 89  SER 89  89  89  SER SER B . n 
A 1 90  TYR 90  90  90  TYR TYR B . n 
A 1 91  ARG 91  91  91  ARG ARG B . n 
A 1 92  LEU 92  92  92  LEU LEU B . n 
A 1 93  ARG 93  93  93  ARG ARG B . n 
A 1 94  GLN 94  94  94  GLN GLN B . n 
A 1 95  VAL 95  95  95  VAL VAL B . n 
A 1 96  HIS 96  96  96  HIS HIS B . n 
A 1 97  LEU 97  97  97  LEU LEU B . n 
A 1 98  HIS 98  98  98  HIS HIS B . n 
A 1 99  TRP 99  99  99  TRP TRP B . n 
A 1 100 GLY 100 100 100 GLY GLY B . n 
A 1 101 SER 101 101 101 SER SER B . n 
A 1 102 ALA 102 102 102 ALA ALA B . n 
A 1 103 ASP 103 103 103 ASP ASP B . n 
A 1 104 ASP 104 104 104 ASP ASP B . n 
A 1 105 HIS 105 105 105 HIS HIS B . n 
A 1 106 GLY 106 106 106 GLY GLY B . n 
A 1 107 SER 107 107 107 SER SER B . n 
A 1 108 GLU 108 108 108 GLU GLU B . n 
A 1 109 HIS 109 109 109 HIS HIS B . n 
A 1 110 ILE 110 110 110 ILE ILE B . n 
A 1 111 VAL 111 111 111 VAL VAL B . n 
A 1 112 ASP 112 112 112 ASP ASP B . n 
A 1 113 GLY 113 113 113 GLY GLY B . n 
A 1 114 VAL 114 114 114 VAL VAL B . n 
A 1 115 SER 115 115 115 SER SER B . n 
A 1 116 TYR 116 116 116 TYR TYR B . n 
A 1 117 ALA 117 117 117 ALA ALA B . n 
A 1 118 ALA 118 118 118 ALA ALA B . n 
A 1 119 GLU 119 119 119 GLU GLU B . n 
A 1 120 LEU 120 120 120 LEU LEU B . n 
A 1 121 HIS 121 121 121 HIS HIS B . n 
A 1 122 VAL 122 122 122 VAL VAL B . n 
A 1 123 VAL 123 123 123 VAL VAL B . n 
A 1 124 HIS 124 124 124 HIS HIS B . n 
A 1 125 TRP 125 125 125 TRP TRP B . n 
A 1 126 ASN 126 126 126 ASN ASN B . n 
A 1 127 SER 127 127 127 SER SER B . n 
A 1 128 ASP 128 128 128 ASP ASP B . n 
A 1 129 LYS 129 129 129 LYS LYS B . n 
A 1 130 TYR 130 130 130 TYR TYR B . n 
A 1 131 PRO 131 131 131 PRO PRO B . n 
A 1 132 SER 132 132 132 SER SER B . n 
A 1 133 PHE 133 133 133 PHE PHE B . n 
A 1 134 VAL 134 134 134 VAL VAL B . n 
A 1 135 GLU 135 135 135 GLU GLU B . n 
A 1 136 ALA 136 136 136 ALA ALA B . n 
A 1 137 ALA 137 137 137 ALA ALA B . n 
A 1 138 HIS 138 138 138 HIS HIS B . n 
A 1 139 GLU 139 139 139 GLU GLU B . n 
A 1 140 PRO 140 140 140 PRO PRO B . n 
A 1 141 ASP 141 141 141 ASP ASP B . n 
A 1 142 GLY 142 142 142 GLY GLY B . n 
A 1 143 LEU 143 143 143 LEU LEU B . n 
A 1 144 ALA 144 144 144 ALA ALA B . n 
A 1 145 VAL 145 145 145 VAL VAL B . n 
A 1 146 LEU 146 146 146 LEU LEU B . n 
A 1 147 GLY 147 147 147 GLY GLY B . n 
A 1 148 VAL 148 148 148 VAL VAL B . n 
A 1 149 PHE 149 149 149 PHE PHE B . n 
A 1 150 LEU 150 150 150 LEU LEU B . n 
A 1 151 GLN 151 151 151 GLN GLN B . n 
A 1 152 ILE 152 152 152 ILE ILE B . n 
A 1 153 GLY 153 153 153 GLY GLY B . n 
A 1 154 GLU 154 154 154 GLU GLU B . n 
A 1 155 PRO 155 155 155 PRO PRO B . n 
A 1 156 ASN 156 156 156 ASN ASN B . n 
A 1 157 SER 157 157 157 SER SER B . n 
A 1 158 GLN 158 158 158 GLN GLN B . n 
A 1 159 LEU 159 159 159 LEU LEU B . n 
A 1 160 GLN 160 160 160 GLN GLN B . n 
A 1 161 LYS 161 161 161 LYS LYS B . n 
A 1 162 ILE 162 162 162 ILE ILE B . n 
A 1 163 THR 163 163 163 THR THR B . n 
A 1 164 ASP 164 164 164 ASP ASP B . n 
A 1 165 THR 165 165 165 THR THR B . n 
A 1 166 LEU 166 166 166 LEU LEU B . n 
A 1 167 ASP 167 167 167 ASP ASP B . n 
A 1 168 SER 168 168 168 SER SER B . n 
A 1 169 ILE 169 169 169 ILE ILE B . n 
A 1 170 LYS 170 170 170 LYS LYS B . n 
A 1 171 GLU 171 171 171 GLU GLU B . n 
A 1 172 LYS 172 172 172 LYS LYS B . n 
A 1 173 GLY 173 173 173 GLY GLY B . n 
A 1 174 LYS 174 174 174 LYS LYS B . n 
A 1 175 GLN 175 175 175 GLN GLN B . n 
A 1 176 THR 176 176 176 THR THR B . n 
A 1 177 ARG 177 177 177 ARG ARG B . n 
A 1 178 PHE 178 178 178 PHE PHE B . n 
A 1 179 THR 179 179 179 THR THR B . n 
A 1 180 ASN 180 180 180 ASN ASN B . n 
A 1 181 PHE 181 181 181 PHE PHE B . n 
A 1 182 ASP 182 182 182 ASP ASP B . n 
A 1 183 LEU 183 183 183 LEU LEU B . n 
A 1 184 LEU 184 184 184 LEU LEU B . n 
A 1 185 SER 185 185 185 SER SER B . n 
A 1 186 LEU 186 186 186 LEU LEU B . n 
A 1 187 LEU 187 187 187 LEU LEU B . n 
A 1 188 PRO 188 188 188 PRO PRO B . n 
A 1 189 PRO 189 189 189 PRO PRO B . n 
A 1 190 SER 190 190 190 SER SER B . n 
A 1 191 TRP 191 191 191 TRP TRP B . n 
A 1 192 ASP 192 192 192 ASP ASP B . n 
A 1 193 TYR 193 193 193 TYR TYR B . n 
A 1 194 TRP 194 194 194 TRP TRP B . n 
A 1 195 THR 195 195 195 THR THR B . n 
A 1 196 TYR 196 196 196 TYR TYR B . n 
A 1 197 PRO 197 197 197 PRO PRO B . n 
A 1 198 GLY 198 198 198 GLY GLY B . n 
A 1 199 SER 199 199 199 SER SER B . n 
A 1 200 LEU 200 200 200 LEU LEU B . n 
A 1 201 THR 201 201 201 THR THR B . n 
A 1 202 VAL 202 202 202 VAL VAL B . n 
A 1 203 PRO 203 203 203 PRO PRO B . n 
A 1 204 PRO 204 204 204 PRO PRO B . n 
A 1 205 LEU 205 205 205 LEU LEU B . n 
A 1 206 LEU 206 206 206 LEU LEU B . n 
A 1 207 GLU 207 207 207 GLU GLU B . n 
A 1 208 SER 208 208 208 SER SER B . n 
A 1 209 VAL 209 209 209 VAL VAL B . n 
A 1 210 THR 210 210 210 THR THR B . n 
A 1 211 TRP 211 211 211 TRP TRP B . n 
A 1 212 ILE 212 212 212 ILE ILE B . n 
A 1 213 VAL 213 213 213 VAL VAL B . n 
A 1 214 LEU 214 214 214 LEU LEU B . n 
A 1 215 LYS 215 215 215 LYS LYS B . n 
A 1 216 GLN 216 216 216 GLN GLN B . n 
A 1 217 PRO 217 217 217 PRO PRO B . n 
A 1 218 ILE 218 218 218 ILE ILE B . n 
A 1 219 ASN 219 219 219 ASN ASN B . n 
A 1 220 ILE 220 220 220 ILE ILE B . n 
A 1 221 SER 221 221 221 SER SER B . n 
A 1 222 SER 222 222 222 SER SER B . n 
A 1 223 GLN 223 223 223 GLN GLN B . n 
A 1 224 GLN 224 224 224 GLN GLN B . n 
A 1 225 LEU 225 225 225 LEU LEU B . n 
A 1 226 ALA 226 226 226 ALA ALA B . n 
A 1 227 LYS 227 227 227 LYS LYS B . n 
A 1 228 PHE 228 228 228 PHE PHE B . n 
A 1 229 ARG 229 229 229 ARG ARG B . n 
A 1 230 SER 230 230 230 SER SER B . n 
A 1 231 LEU 231 231 231 LEU LEU B . n 
A 1 232 LEU 232 232 232 LEU LEU B . n 
A 1 233 CYS 233 233 233 CYS CYS B . n 
A 1 234 THR 234 234 234 THR THR B . n 
A 1 235 ALA 235 235 235 ALA ALA B . n 
A 1 236 GLU 236 236 236 GLU GLU B . n 
A 1 237 GLY 237 237 237 GLY GLY B . n 
A 1 238 GLU 238 238 238 GLU GLU B . n 
A 1 239 ALA 239 239 239 ALA ALA B . n 
A 1 240 ALA 240 240 240 ALA ALA B . n 
A 1 241 ALA 241 241 241 ALA ALA B . n 
A 1 242 PHE 242 242 242 PHE PHE B . n 
A 1 243 LEU 243 243 243 LEU LEU B . n 
A 1 244 VAL 244 244 244 VAL VAL B . n 
A 1 245 SER 245 245 245 SER SER B . n 
A 1 246 ASN 246 246 246 ASN ASN B . n 
A 1 247 HIS 247 247 247 HIS HIS B . n 
A 1 248 ARG 248 248 248 ARG ARG B . n 
A 1 249 PRO 249 249 249 PRO PRO B . n 
A 1 250 PRO 250 250 250 PRO PRO B . n 
A 1 251 GLN 251 251 251 GLN GLN B . n 
A 1 252 PRO 252 252 252 PRO PRO B . n 
A 1 253 LEU 253 253 253 LEU LEU B . n 
A 1 254 LYS 254 254 254 LYS LYS B . n 
A 1 255 GLY 255 255 255 GLY GLY B . n 
A 1 256 ARG 256 256 256 ARG ARG B . n 
A 1 257 LYS 257 257 257 LYS LYS B . n 
A 1 258 VAL 258 258 258 VAL VAL B . n 
A 1 259 ARG 259 259 259 ARG ARG B . n 
A 1 260 ALA 260 260 260 ALA ALA B . n 
A 1 261 SER 261 261 261 SER SER B . n 
A 1 262 PHE 262 262 262 PHE PHE B . n 
A 1 263 HIS 263 263 263 HIS HIS B . n 
B 1 1   MET 1   1   ?   ?   ?   A . n 
B 1 2   MET 2   2   ?   ?   ?   A . n 
B 1 3   SER 3   3   ?   ?   ?   A . n 
B 1 4   ARG 4   4   ?   ?   ?   A . n 
B 1 5   LEU 5   5   ?   ?   ?   A . n 
B 1 6   SER 6   6   6   SER SER A . n 
B 1 7   TRP 7   7   7   TRP TRP A . n 
B 1 8   GLY 8   8   8   GLY GLY A . n 
B 1 9   TYR 9   9   9   TYR TYR A . n 
B 1 10  ARG 10  10  10  ARG ARG A . n 
B 1 11  GLU 11  11  11  GLU GLU A . n 
B 1 12  HIS 12  12  12  HIS HIS A . n 
B 1 13  ASN 13  13  13  ASN ASN A . n 
B 1 14  GLY 14  14  14  GLY GLY A . n 
B 1 15  PRO 15  15  15  PRO PRO A . n 
B 1 16  ILE 16  16  16  ILE ILE A . n 
B 1 17  HIS 17  17  17  HIS HIS A . n 
B 1 18  TRP 18  18  18  TRP TRP A . n 
B 1 19  LYS 19  19  19  LYS LYS A . n 
B 1 20  GLU 20  20  20  GLU GLU A . n 
B 1 21  PHE 21  21  21  PHE PHE A . n 
B 1 22  PHE 22  22  22  PHE PHE A . n 
B 1 23  PRO 23  23  23  PRO PRO A . n 
B 1 24  ILE 24  24  24  ILE ILE A . n 
B 1 25  ALA 25  25  25  ALA ALA A . n 
B 1 26  ASP 26  26  26  ASP ASP A . n 
B 1 27  GLY 27  27  27  GLY GLY A . n 
B 1 28  ASP 28  28  28  ASP ASP A . n 
B 1 29  GLN 29  29  29  GLN GLN A . n 
B 1 30  GLN 30  30  30  GLN GLN A . n 
B 1 31  SER 31  31  31  SER SER A . n 
B 1 32  PRO 32  32  32  PRO PRO A . n 
B 1 33  ILE 33  33  33  ILE ILE A . n 
B 1 34  GLU 34  34  34  GLU GLU A . n 
B 1 35  ILE 35  35  35  ILE ILE A . n 
B 1 36  LYS 36  36  36  LYS LYS A . n 
B 1 37  THR 37  37  37  THR THR A . n 
B 1 38  LYS 38  38  38  LYS LYS A . n 
B 1 39  GLU 39  39  39  GLU GLU A . n 
B 1 40  VAL 40  40  40  VAL VAL A . n 
B 1 41  LYS 41  41  41  LYS LYS A . n 
B 1 42  TYR 42  42  42  TYR TYR A . n 
B 1 43  ASP 43  43  43  ASP ASP A . n 
B 1 44  SER 44  44  44  SER SER A . n 
B 1 45  SER 45  45  45  SER SER A . n 
B 1 46  LEU 46  46  46  LEU LEU A . n 
B 1 47  ARG 47  47  47  ARG ARG A . n 
B 1 48  PRO 48  48  48  PRO PRO A . n 
B 1 49  LEU 49  49  49  LEU LEU A . n 
B 1 50  SER 50  50  50  SER SER A . n 
B 1 51  ILE 51  51  51  ILE ILE A . n 
B 1 52  LYS 52  52  52  LYS LYS A . n 
B 1 53  TYR 53  53  53  TYR TYR A . n 
B 1 54  ASP 54  54  54  ASP ASP A . n 
B 1 55  PRO 55  55  55  PRO PRO A . n 
B 1 56  SER 56  56  56  SER SER A . n 
B 1 57  SER 57  57  57  SER SER A . n 
B 1 58  ALA 58  58  58  ALA ALA A . n 
B 1 59  LYS 59  59  59  LYS LYS A . n 
B 1 60  ILE 60  60  60  ILE ILE A . n 
B 1 61  ILE 61  61  61  ILE ILE A . n 
B 1 62  SER 62  62  62  SER SER A . n 
B 1 63  ASN 63  63  63  ASN ASN A . n 
B 1 64  SER 64  64  64  SER SER A . n 
B 1 65  GLY 65  65  65  GLY GLY A . n 
B 1 66  HIS 66  66  66  HIS HIS A . n 
B 1 67  SER 67  67  67  SER SER A . n 
B 1 68  PHE 68  68  68  PHE PHE A . n 
B 1 69  ASN 69  69  69  ASN ASN A . n 
B 1 70  VAL 70  70  70  VAL VAL A . n 
B 1 71  ASP 71  71  71  ASP ASP A . n 
B 1 72  PHE 72  72  72  PHE PHE A . n 
B 1 73  ASP 73  73  73  ASP ASP A . n 
B 1 74  ASP 74  74  74  ASP ASP A . n 
B 1 75  THR 75  75  75  THR THR A . n 
B 1 76  GLU 76  76  76  GLU GLU A . n 
B 1 77  ASN 77  77  77  ASN ASN A . n 
B 1 78  LYS 78  78  78  LYS LYS A . n 
B 1 79  SER 79  79  79  SER SER A . n 
B 1 80  VAL 80  80  80  VAL VAL A . n 
B 1 81  LEU 81  81  81  LEU LEU A . n 
B 1 82  ARG 82  82  82  ARG ARG A . n 
B 1 83  GLY 83  83  83  GLY GLY A . n 
B 1 84  GLY 84  84  84  GLY GLY A . n 
B 1 85  PRO 85  85  85  PRO PRO A . n 
B 1 86  LEU 86  86  86  LEU LEU A . n 
B 1 87  THR 87  87  87  THR THR A . n 
B 1 88  GLY 88  88  88  GLY GLY A . n 
B 1 89  SER 89  89  89  SER SER A . n 
B 1 90  TYR 90  90  90  TYR TYR A . n 
B 1 91  ARG 91  91  91  ARG ARG A . n 
B 1 92  LEU 92  92  92  LEU LEU A . n 
B 1 93  ARG 93  93  93  ARG ARG A . n 
B 1 94  GLN 94  94  94  GLN GLN A . n 
B 1 95  VAL 95  95  95  VAL VAL A . n 
B 1 96  HIS 96  96  96  HIS HIS A . n 
B 1 97  LEU 97  97  97  LEU LEU A . n 
B 1 98  HIS 98  98  98  HIS HIS A . n 
B 1 99  TRP 99  99  99  TRP TRP A . n 
B 1 100 GLY 100 100 100 GLY GLY A . n 
B 1 101 SER 101 101 101 SER SER A . n 
B 1 102 ALA 102 102 102 ALA ALA A . n 
B 1 103 ASP 103 103 103 ASP ASP A . n 
B 1 104 ASP 104 104 104 ASP ASP A . n 
B 1 105 HIS 105 105 105 HIS HIS A . n 
B 1 106 GLY 106 106 106 GLY GLY A . n 
B 1 107 SER 107 107 107 SER SER A . n 
B 1 108 GLU 108 108 108 GLU GLU A . n 
B 1 109 HIS 109 109 109 HIS HIS A . n 
B 1 110 ILE 110 110 110 ILE ILE A . n 
B 1 111 VAL 111 111 111 VAL VAL A . n 
B 1 112 ASP 112 112 112 ASP ASP A . n 
B 1 113 GLY 113 113 113 GLY GLY A . n 
B 1 114 VAL 114 114 114 VAL VAL A . n 
B 1 115 SER 115 115 115 SER SER A . n 
B 1 116 TYR 116 116 116 TYR TYR A . n 
B 1 117 ALA 117 117 117 ALA ALA A . n 
B 1 118 ALA 118 118 118 ALA ALA A . n 
B 1 119 GLU 119 119 119 GLU GLU A . n 
B 1 120 LEU 120 120 120 LEU LEU A . n 
B 1 121 HIS 121 121 121 HIS HIS A . n 
B 1 122 VAL 122 122 122 VAL VAL A . n 
B 1 123 VAL 123 123 123 VAL VAL A . n 
B 1 124 HIS 124 124 124 HIS HIS A . n 
B 1 125 TRP 125 125 125 TRP TRP A . n 
B 1 126 ASN 126 126 126 ASN ASN A . n 
B 1 127 SER 127 127 127 SER SER A . n 
B 1 128 ASP 128 128 128 ASP ASP A . n 
B 1 129 LYS 129 129 129 LYS LYS A . n 
B 1 130 TYR 130 130 130 TYR TYR A . n 
B 1 131 PRO 131 131 131 PRO PRO A . n 
B 1 132 SER 132 132 132 SER SER A . n 
B 1 133 PHE 133 133 133 PHE PHE A . n 
B 1 134 VAL 134 134 134 VAL VAL A . n 
B 1 135 GLU 135 135 135 GLU GLU A . n 
B 1 136 ALA 136 136 136 ALA ALA A . n 
B 1 137 ALA 137 137 137 ALA ALA A . n 
B 1 138 HIS 138 138 138 HIS HIS A . n 
B 1 139 GLU 139 139 139 GLU GLU A . n 
B 1 140 PRO 140 140 140 PRO PRO A . n 
B 1 141 ASP 141 141 141 ASP ASP A . n 
B 1 142 GLY 142 142 142 GLY GLY A . n 
B 1 143 LEU 143 143 143 LEU LEU A . n 
B 1 144 ALA 144 144 144 ALA ALA A . n 
B 1 145 VAL 145 145 145 VAL VAL A . n 
B 1 146 LEU 146 146 146 LEU LEU A . n 
B 1 147 GLY 147 147 147 GLY GLY A . n 
B 1 148 VAL 148 148 148 VAL VAL A . n 
B 1 149 PHE 149 149 149 PHE PHE A . n 
B 1 150 LEU 150 150 150 LEU LEU A . n 
B 1 151 GLN 151 151 151 GLN GLN A . n 
B 1 152 ILE 152 152 152 ILE ILE A . n 
B 1 153 GLY 153 153 153 GLY GLY A . n 
B 1 154 GLU 154 154 154 GLU GLU A . n 
B 1 155 PRO 155 155 155 PRO PRO A . n 
B 1 156 ASN 156 156 156 ASN ASN A . n 
B 1 157 SER 157 157 157 SER SER A . n 
B 1 158 GLN 158 158 158 GLN GLN A . n 
B 1 159 LEU 159 159 159 LEU LEU A . n 
B 1 160 GLN 160 160 160 GLN GLN A . n 
B 1 161 LYS 161 161 161 LYS LYS A . n 
B 1 162 ILE 162 162 162 ILE ILE A . n 
B 1 163 THR 163 163 163 THR THR A . n 
B 1 164 ASP 164 164 164 ASP ASP A . n 
B 1 165 THR 165 165 165 THR THR A . n 
B 1 166 LEU 166 166 166 LEU LEU A . n 
B 1 167 ASP 167 167 167 ASP ASP A . n 
B 1 168 SER 168 168 168 SER SER A . n 
B 1 169 ILE 169 169 169 ILE ILE A . n 
B 1 170 LYS 170 170 170 LYS LYS A . n 
B 1 171 GLU 171 171 171 GLU GLU A . n 
B 1 172 LYS 172 172 172 LYS LYS A . n 
B 1 173 GLY 173 173 173 GLY GLY A . n 
B 1 174 LYS 174 174 174 LYS LYS A . n 
B 1 175 GLN 175 175 175 GLN GLN A . n 
B 1 176 THR 176 176 176 THR THR A . n 
B 1 177 ARG 177 177 177 ARG ARG A . n 
B 1 178 PHE 178 178 178 PHE PHE A . n 
B 1 179 THR 179 179 179 THR THR A . n 
B 1 180 ASN 180 180 180 ASN ASN A . n 
B 1 181 PHE 181 181 181 PHE PHE A . n 
B 1 182 ASP 182 182 182 ASP ASP A . n 
B 1 183 LEU 183 183 183 LEU LEU A . n 
B 1 184 LEU 184 184 184 LEU LEU A . n 
B 1 185 SER 185 185 185 SER SER A . n 
B 1 186 LEU 186 186 186 LEU LEU A . n 
B 1 187 LEU 187 187 187 LEU LEU A . n 
B 1 188 PRO 188 188 188 PRO PRO A . n 
B 1 189 PRO 189 189 189 PRO PRO A . n 
B 1 190 SER 190 190 190 SER SER A . n 
B 1 191 TRP 191 191 191 TRP TRP A . n 
B 1 192 ASP 192 192 192 ASP ASP A . n 
B 1 193 TYR 193 193 193 TYR TYR A . n 
B 1 194 TRP 194 194 194 TRP TRP A . n 
B 1 195 THR 195 195 195 THR THR A . n 
B 1 196 TYR 196 196 196 TYR TYR A . n 
B 1 197 PRO 197 197 197 PRO PRO A . n 
B 1 198 GLY 198 198 198 GLY GLY A . n 
B 1 199 SER 199 199 199 SER SER A . n 
B 1 200 LEU 200 200 200 LEU LEU A . n 
B 1 201 THR 201 201 201 THR THR A . n 
B 1 202 VAL 202 202 202 VAL VAL A . n 
B 1 203 PRO 203 203 203 PRO PRO A . n 
B 1 204 PRO 204 204 204 PRO PRO A . n 
B 1 205 LEU 205 205 205 LEU LEU A . n 
B 1 206 LEU 206 206 206 LEU LEU A . n 
B 1 207 GLU 207 207 207 GLU GLU A . n 
B 1 208 SER 208 208 208 SER SER A . n 
B 1 209 VAL 209 209 209 VAL VAL A . n 
B 1 210 THR 210 210 210 THR THR A . n 
B 1 211 TRP 211 211 211 TRP TRP A . n 
B 1 212 ILE 212 212 212 ILE ILE A . n 
B 1 213 VAL 213 213 213 VAL VAL A . n 
B 1 214 LEU 214 214 214 LEU LEU A . n 
B 1 215 LYS 215 215 215 LYS LYS A . n 
B 1 216 GLN 216 216 216 GLN GLN A . n 
B 1 217 PRO 217 217 217 PRO PRO A . n 
B 1 218 ILE 218 218 218 ILE ILE A . n 
B 1 219 ASN 219 219 219 ASN ASN A . n 
B 1 220 ILE 220 220 220 ILE ILE A . n 
B 1 221 SER 221 221 221 SER SER A . n 
B 1 222 SER 222 222 222 SER SER A . n 
B 1 223 GLN 223 223 223 GLN GLN A . n 
B 1 224 GLN 224 224 224 GLN GLN A . n 
B 1 225 LEU 225 225 225 LEU LEU A . n 
B 1 226 ALA 226 226 226 ALA ALA A . n 
B 1 227 LYS 227 227 227 LYS LYS A . n 
B 1 228 PHE 228 228 228 PHE PHE A . n 
B 1 229 ARG 229 229 229 ARG ARG A . n 
B 1 230 SER 230 230 230 SER SER A . n 
B 1 231 LEU 231 231 231 LEU LEU A . n 
B 1 232 LEU 232 232 232 LEU LEU A . n 
B 1 233 CYS 233 233 233 CYS CYS A . n 
B 1 234 THR 234 234 234 THR THR A . n 
B 1 235 ALA 235 235 235 ALA ALA A . n 
B 1 236 GLU 236 236 236 GLU GLU A . n 
B 1 237 GLY 237 237 237 GLY GLY A . n 
B 1 238 GLU 238 238 238 GLU GLU A . n 
B 1 239 ALA 239 239 239 ALA ALA A . n 
B 1 240 ALA 240 240 240 ALA ALA A . n 
B 1 241 ALA 241 241 241 ALA ALA A . n 
B 1 242 PHE 242 242 242 PHE PHE A . n 
B 1 243 LEU 243 243 243 LEU LEU A . n 
B 1 244 VAL 244 244 244 VAL VAL A . n 
B 1 245 SER 245 245 245 SER SER A . n 
B 1 246 ASN 246 246 246 ASN ASN A . n 
B 1 247 HIS 247 247 247 HIS HIS A . n 
B 1 248 ARG 248 248 248 ARG ARG A . n 
B 1 249 PRO 249 249 249 PRO PRO A . n 
B 1 250 PRO 250 250 250 PRO PRO A . n 
B 1 251 GLN 251 251 251 GLN GLN A . n 
B 1 252 PRO 252 252 252 PRO PRO A . n 
B 1 253 LEU 253 253 253 LEU LEU A . n 
B 1 254 LYS 254 254 254 LYS LYS A . n 
B 1 255 GLY 255 255 255 GLY GLY A . n 
B 1 256 ARG 256 256 256 ARG ARG A . n 
B 1 257 LYS 257 257 257 LYS LYS A . n 
B 1 258 VAL 258 258 258 VAL VAL A . n 
B 1 259 ARG 259 259 259 ARG ARG A . n 
B 1 260 ALA 260 260 260 ALA ALA A . n 
B 1 261 SER 261 261 261 SER SER A . n 
B 1 262 PHE 262 262 262 PHE PHE A . n 
B 1 263 HIS 263 263 263 HIS HIS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN  1   301 1   ZN  ZN  B . 
D 3 E1F 1   302 2   E1F E18 B . 
E 4 CIT 1   303 1   CIT CIT B . 
F 5 EDO 1   304 1   EDO EDO B . 
G 5 EDO 1   305 2   EDO EDO B . 
H 6 ACY 1   306 1   ACY ACY B . 
I 6 ACY 1   307 2   ACY ACY B . 
J 6 ACY 1   308 3   ACY ACY B . 
K 2 ZN  1   301 2   ZN  ZN  A . 
L 3 E1F 1   302 1   E1F E18 A . 
M 4 CIT 1   303 2   CIT CIT A . 
N 7 PEG 1   304 5   PEG PEG A . 
O 5 EDO 1   305 3   EDO EDO A . 
P 8 HOH 1   401 2   HOH HOH B . 
P 8 HOH 2   402 3   HOH HOH B . 
P 8 HOH 3   403 4   HOH HOH B . 
P 8 HOH 4   404 6   HOH HOH B . 
P 8 HOH 5   405 10  HOH HOH B . 
P 8 HOH 6   406 11  HOH HOH B . 
P 8 HOH 7   407 12  HOH HOH B . 
P 8 HOH 8   408 13  HOH HOH B . 
P 8 HOH 9   409 14  HOH HOH B . 
P 8 HOH 10  410 15  HOH HOH B . 
P 8 HOH 11  411 17  HOH HOH B . 
P 8 HOH 12  412 18  HOH HOH B . 
P 8 HOH 13  413 21  HOH HOH B . 
P 8 HOH 14  414 22  HOH HOH B . 
P 8 HOH 15  415 23  HOH HOH B . 
P 8 HOH 16  416 26  HOH HOH B . 
P 8 HOH 17  417 27  HOH HOH B . 
P 8 HOH 18  418 28  HOH HOH B . 
P 8 HOH 19  419 29  HOH HOH B . 
P 8 HOH 20  420 31  HOH HOH B . 
P 8 HOH 21  421 32  HOH HOH B . 
P 8 HOH 22  422 33  HOH HOH B . 
P 8 HOH 23  423 36  HOH HOH B . 
P 8 HOH 24  424 37  HOH HOH B . 
P 8 HOH 25  425 38  HOH HOH B . 
P 8 HOH 26  426 39  HOH HOH B . 
P 8 HOH 27  427 40  HOH HOH B . 
P 8 HOH 28  428 41  HOH HOH B . 
P 8 HOH 29  429 42  HOH HOH B . 
P 8 HOH 30  430 43  HOH HOH B . 
P 8 HOH 31  431 45  HOH HOH B . 
P 8 HOH 32  432 48  HOH HOH B . 
P 8 HOH 33  433 50  HOH HOH B . 
P 8 HOH 34  434 51  HOH HOH B . 
P 8 HOH 35  435 53  HOH HOH B . 
P 8 HOH 36  436 56  HOH HOH B . 
P 8 HOH 37  437 57  HOH HOH B . 
P 8 HOH 38  438 58  HOH HOH B . 
P 8 HOH 39  439 59  HOH HOH B . 
P 8 HOH 40  440 60  HOH HOH B . 
P 8 HOH 41  441 63  HOH HOH B . 
P 8 HOH 42  442 66  HOH HOH B . 
P 8 HOH 43  443 67  HOH HOH B . 
P 8 HOH 44  444 69  HOH HOH B . 
P 8 HOH 45  445 71  HOH HOH B . 
P 8 HOH 46  446 75  HOH HOH B . 
P 8 HOH 47  447 76  HOH HOH B . 
P 8 HOH 48  448 78  HOH HOH B . 
P 8 HOH 49  449 79  HOH HOH B . 
P 8 HOH 50  450 83  HOH HOH B . 
P 8 HOH 51  451 84  HOH HOH B . 
P 8 HOH 52  452 88  HOH HOH B . 
P 8 HOH 53  453 90  HOH HOH B . 
P 8 HOH 54  454 91  HOH HOH B . 
P 8 HOH 55  455 92  HOH HOH B . 
P 8 HOH 56  456 93  HOH HOH B . 
P 8 HOH 57  457 95  HOH HOH B . 
P 8 HOH 58  458 96  HOH HOH B . 
P 8 HOH 59  459 99  HOH HOH B . 
P 8 HOH 60  460 100 HOH HOH B . 
P 8 HOH 61  461 101 HOH HOH B . 
P 8 HOH 62  462 102 HOH HOH B . 
P 8 HOH 63  463 103 HOH HOH B . 
P 8 HOH 64  464 105 HOH HOH B . 
P 8 HOH 65  465 106 HOH HOH B . 
P 8 HOH 66  466 108 HOH HOH B . 
P 8 HOH 67  467 111 HOH HOH B . 
P 8 HOH 68  468 112 HOH HOH B . 
P 8 HOH 69  469 114 HOH HOH B . 
P 8 HOH 70  470 115 HOH HOH B . 
P 8 HOH 71  471 117 HOH HOH B . 
P 8 HOH 72  472 118 HOH HOH B . 
P 8 HOH 73  473 121 HOH HOH B . 
P 8 HOH 74  474 122 HOH HOH B . 
P 8 HOH 75  475 123 HOH HOH B . 
P 8 HOH 76  476 124 HOH HOH B . 
P 8 HOH 77  477 125 HOH HOH B . 
P 8 HOH 78  478 128 HOH HOH B . 
P 8 HOH 79  479 130 HOH HOH B . 
P 8 HOH 80  480 133 HOH HOH B . 
P 8 HOH 81  481 135 HOH HOH B . 
P 8 HOH 82  482 141 HOH HOH B . 
P 8 HOH 83  483 145 HOH HOH B . 
P 8 HOH 84  484 146 HOH HOH B . 
P 8 HOH 85  485 148 HOH HOH B . 
P 8 HOH 86  486 149 HOH HOH B . 
P 8 HOH 87  487 151 HOH HOH B . 
P 8 HOH 88  488 152 HOH HOH B . 
P 8 HOH 89  489 153 HOH HOH B . 
P 8 HOH 90  490 156 HOH HOH B . 
P 8 HOH 91  491 159 HOH HOH B . 
P 8 HOH 92  492 161 HOH HOH B . 
P 8 HOH 93  493 162 HOH HOH B . 
P 8 HOH 94  494 163 HOH HOH B . 
P 8 HOH 95  495 165 HOH HOH B . 
P 8 HOH 96  496 166 HOH HOH B . 
P 8 HOH 97  497 169 HOH HOH B . 
P 8 HOH 98  498 170 HOH HOH B . 
P 8 HOH 99  499 171 HOH HOH B . 
P 8 HOH 100 500 172 HOH HOH B . 
P 8 HOH 101 501 173 HOH HOH B . 
P 8 HOH 102 502 174 HOH HOH B . 
P 8 HOH 103 503 177 HOH HOH B . 
P 8 HOH 104 504 180 HOH HOH B . 
P 8 HOH 105 505 181 HOH HOH B . 
P 8 HOH 106 506 190 HOH HOH B . 
P 8 HOH 107 507 192 HOH HOH B . 
P 8 HOH 108 508 193 HOH HOH B . 
P 8 HOH 109 509 194 HOH HOH B . 
P 8 HOH 110 510 195 HOH HOH B . 
P 8 HOH 111 511 197 HOH HOH B . 
P 8 HOH 112 512 198 HOH HOH B . 
P 8 HOH 113 513 199 HOH HOH B . 
P 8 HOH 114 514 200 HOH HOH B . 
P 8 HOH 115 515 206 HOH HOH B . 
P 8 HOH 116 516 212 HOH HOH B . 
P 8 HOH 117 517 213 HOH HOH B . 
P 8 HOH 118 518 214 HOH HOH B . 
P 8 HOH 119 519 215 HOH HOH B . 
P 8 HOH 120 520 218 HOH HOH B . 
P 8 HOH 121 521 219 HOH HOH B . 
P 8 HOH 122 522 220 HOH HOH B . 
P 8 HOH 123 523 221 HOH HOH B . 
P 8 HOH 124 524 222 HOH HOH B . 
P 8 HOH 125 525 223 HOH HOH B . 
P 8 HOH 126 526 225 HOH HOH B . 
P 8 HOH 127 527 226 HOH HOH B . 
P 8 HOH 128 528 228 HOH HOH B . 
P 8 HOH 129 529 229 HOH HOH B . 
P 8 HOH 130 530 231 HOH HOH B . 
P 8 HOH 131 531 233 HOH HOH B . 
P 8 HOH 132 532 234 HOH HOH B . 
P 8 HOH 133 533 236 HOH HOH B . 
P 8 HOH 134 534 237 HOH HOH B . 
P 8 HOH 135 535 238 HOH HOH B . 
P 8 HOH 136 536 241 HOH HOH B . 
P 8 HOH 137 537 242 HOH HOH B . 
P 8 HOH 138 538 244 HOH HOH B . 
P 8 HOH 139 539 245 HOH HOH B . 
P 8 HOH 140 540 246 HOH HOH B . 
P 8 HOH 141 541 247 HOH HOH B . 
P 8 HOH 142 542 248 HOH HOH B . 
P 8 HOH 143 543 249 HOH HOH B . 
P 8 HOH 144 544 251 HOH HOH B . 
P 8 HOH 145 545 253 HOH HOH B . 
P 8 HOH 146 546 256 HOH HOH B . 
P 8 HOH 147 547 257 HOH HOH B . 
P 8 HOH 148 548 258 HOH HOH B . 
P 8 HOH 149 549 259 HOH HOH B . 
P 8 HOH 150 550 260 HOH HOH B . 
P 8 HOH 151 551 262 HOH HOH B . 
P 8 HOH 152 552 264 HOH HOH B . 
P 8 HOH 153 553 266 HOH HOH B . 
P 8 HOH 154 554 268 HOH HOH B . 
P 8 HOH 155 555 269 HOH HOH B . 
P 8 HOH 156 556 271 HOH HOH B . 
P 8 HOH 157 557 273 HOH HOH B . 
P 8 HOH 158 558 274 HOH HOH B . 
P 8 HOH 159 559 276 HOH HOH B . 
P 8 HOH 160 560 278 HOH HOH B . 
P 8 HOH 161 561 283 HOH HOH B . 
P 8 HOH 162 562 284 HOH HOH B . 
P 8 HOH 163 563 286 HOH HOH B . 
P 8 HOH 164 564 292 HOH HOH B . 
P 8 HOH 165 565 293 HOH HOH B . 
P 8 HOH 166 566 294 HOH HOH B . 
P 8 HOH 167 567 297 HOH HOH B . 
P 8 HOH 168 568 298 HOH HOH B . 
P 8 HOH 169 569 304 HOH HOH B . 
P 8 HOH 170 570 306 HOH HOH B . 
P 8 HOH 171 571 307 HOH HOH B . 
P 8 HOH 172 572 308 HOH HOH B . 
P 8 HOH 173 573 316 HOH HOH B . 
P 8 HOH 174 574 320 HOH HOH B . 
P 8 HOH 175 575 321 HOH HOH B . 
P 8 HOH 176 576 323 HOH HOH B . 
P 8 HOH 177 577 324 HOH HOH B . 
P 8 HOH 178 578 325 HOH HOH B . 
P 8 HOH 179 579 326 HOH HOH B . 
P 8 HOH 180 580 328 HOH HOH B . 
P 8 HOH 181 581 330 HOH HOH B . 
P 8 HOH 182 582 331 HOH HOH B . 
P 8 HOH 183 583 332 HOH HOH B . 
P 8 HOH 184 584 333 HOH HOH B . 
P 8 HOH 185 585 338 HOH HOH B . 
P 8 HOH 186 586 341 HOH HOH B . 
P 8 HOH 187 587 342 HOH HOH B . 
P 8 HOH 188 588 343 HOH HOH B . 
P 8 HOH 189 589 346 HOH HOH B . 
P 8 HOH 190 590 347 HOH HOH B . 
P 8 HOH 191 591 348 HOH HOH B . 
P 8 HOH 192 592 350 HOH HOH B . 
P 8 HOH 193 593 370 HOH HOH B . 
P 8 HOH 194 594 372 HOH HOH B . 
P 8 HOH 195 595 374 HOH HOH B . 
P 8 HOH 196 596 378 HOH HOH B . 
P 8 HOH 197 597 379 HOH HOH B . 
P 8 HOH 198 598 380 HOH HOH B . 
P 8 HOH 199 599 382 HOH HOH B . 
P 8 HOH 200 600 383 HOH HOH B . 
P 8 HOH 201 601 385 HOH HOH B . 
P 8 HOH 202 602 387 HOH HOH B . 
P 8 HOH 203 603 389 HOH HOH B . 
P 8 HOH 204 604 393 HOH HOH B . 
P 8 HOH 205 605 394 HOH HOH B . 
P 8 HOH 206 606 395 HOH HOH B . 
P 8 HOH 207 607 399 HOH HOH B . 
P 8 HOH 208 608 400 HOH HOH B . 
P 8 HOH 209 609 403 HOH HOH B . 
P 8 HOH 210 610 404 HOH HOH B . 
P 8 HOH 211 611 406 HOH HOH B . 
P 8 HOH 212 612 407 HOH HOH B . 
P 8 HOH 213 613 409 HOH HOH B . 
P 8 HOH 214 614 411 HOH HOH B . 
P 8 HOH 215 615 412 HOH HOH B . 
P 8 HOH 216 616 413 HOH HOH B . 
P 8 HOH 217 617 414 HOH HOH B . 
P 8 HOH 218 618 418 HOH HOH B . 
P 8 HOH 219 619 421 HOH HOH B . 
P 8 HOH 220 620 423 HOH HOH B . 
P 8 HOH 221 621 425 HOH HOH B . 
P 8 HOH 222 622 427 HOH HOH B . 
P 8 HOH 223 623 430 HOH HOH B . 
P 8 HOH 224 624 432 HOH HOH B . 
P 8 HOH 225 625 433 HOH HOH B . 
P 8 HOH 226 626 434 HOH HOH B . 
P 8 HOH 227 627 436 HOH HOH B . 
P 8 HOH 228 628 438 HOH HOH B . 
P 8 HOH 229 629 441 HOH HOH B . 
P 8 HOH 230 630 443 HOH HOH B . 
P 8 HOH 231 631 449 HOH HOH B . 
P 8 HOH 232 632 451 HOH HOH B . 
P 8 HOH 233 633 452 HOH HOH B . 
P 8 HOH 234 634 454 HOH HOH B . 
P 8 HOH 235 635 455 HOH HOH B . 
P 8 HOH 236 636 458 HOH HOH B . 
P 8 HOH 237 637 459 HOH HOH B . 
P 8 HOH 238 638 460 HOH HOH B . 
P 8 HOH 239 639 465 HOH HOH B . 
P 8 HOH 240 640 466 HOH HOH B . 
P 8 HOH 241 641 467 HOH HOH B . 
P 8 HOH 242 642 470 HOH HOH B . 
P 8 HOH 243 643 471 HOH HOH B . 
P 8 HOH 244 644 472 HOH HOH B . 
P 8 HOH 245 645 473 HOH HOH B . 
P 8 HOH 246 646 474 HOH HOH B . 
P 8 HOH 247 647 475 HOH HOH B . 
P 8 HOH 248 648 476 HOH HOH B . 
P 8 HOH 249 649 477 HOH HOH B . 
P 8 HOH 250 650 478 HOH HOH B . 
P 8 HOH 251 651 479 HOH HOH B . 
P 8 HOH 252 652 480 HOH HOH B . 
P 8 HOH 253 653 481 HOH HOH B . 
P 8 HOH 254 654 482 HOH HOH B . 
P 8 HOH 255 655 483 HOH HOH B . 
P 8 HOH 256 656 484 HOH HOH B . 
P 8 HOH 257 657 485 HOH HOH B . 
P 8 HOH 258 658 486 HOH HOH B . 
P 8 HOH 259 659 487 HOH HOH B . 
P 8 HOH 260 660 488 HOH HOH B . 
P 8 HOH 261 661 489 HOH HOH B . 
P 8 HOH 262 662 490 HOH HOH B . 
P 8 HOH 263 663 491 HOH HOH B . 
P 8 HOH 264 664 492 HOH HOH B . 
P 8 HOH 265 665 493 HOH HOH B . 
P 8 HOH 266 666 494 HOH HOH B . 
P 8 HOH 267 667 495 HOH HOH B . 
P 8 HOH 268 668 503 HOH HOH B . 
P 8 HOH 269 669 504 HOH HOH B . 
P 8 HOH 270 670 506 HOH HOH B . 
P 8 HOH 271 671 507 HOH HOH B . 
P 8 HOH 272 672 508 HOH HOH B . 
P 8 HOH 273 673 509 HOH HOH B . 
P 8 HOH 274 674 510 HOH HOH B . 
P 8 HOH 275 675 514 HOH HOH B . 
P 8 HOH 276 676 515 HOH HOH B . 
P 8 HOH 277 677 516 HOH HOH B . 
P 8 HOH 278 678 517 HOH HOH B . 
P 8 HOH 279 679 518 HOH HOH B . 
P 8 HOH 280 680 519 HOH HOH B . 
P 8 HOH 281 681 520 HOH HOH B . 
P 8 HOH 282 682 521 HOH HOH B . 
P 8 HOH 283 683 522 HOH HOH B . 
P 8 HOH 284 684 523 HOH HOH B . 
P 8 HOH 285 685 524 HOH HOH B . 
P 8 HOH 286 686 525 HOH HOH B . 
P 8 HOH 287 687 526 HOH HOH B . 
P 8 HOH 288 688 527 HOH HOH B . 
P 8 HOH 289 689 528 HOH HOH B . 
P 8 HOH 290 690 529 HOH HOH B . 
P 8 HOH 291 691 530 HOH HOH B . 
P 8 HOH 292 692 531 HOH HOH B . 
P 8 HOH 293 693 556 HOH HOH B . 
P 8 HOH 294 694 561 HOH HOH B . 
P 8 HOH 295 695 563 HOH HOH B . 
P 8 HOH 296 696 564 HOH HOH B . 
P 8 HOH 297 697 566 HOH HOH B . 
P 8 HOH 298 698 567 HOH HOH B . 
P 8 HOH 299 699 568 HOH HOH B . 
Q 8 HOH 1   401 1   HOH HOH A . 
Q 8 HOH 2   402 5   HOH HOH A . 
Q 8 HOH 3   403 7   HOH HOH A . 
Q 8 HOH 4   404 8   HOH HOH A . 
Q 8 HOH 5   405 9   HOH HOH A . 
Q 8 HOH 6   406 16  HOH HOH A . 
Q 8 HOH 7   407 19  HOH HOH A . 
Q 8 HOH 8   408 20  HOH HOH A . 
Q 8 HOH 9   409 24  HOH HOH A . 
Q 8 HOH 10  410 25  HOH HOH A . 
Q 8 HOH 11  411 30  HOH HOH A . 
Q 8 HOH 12  412 34  HOH HOH A . 
Q 8 HOH 13  413 35  HOH HOH A . 
Q 8 HOH 14  414 44  HOH HOH A . 
Q 8 HOH 15  415 46  HOH HOH A . 
Q 8 HOH 16  416 47  HOH HOH A . 
Q 8 HOH 17  417 49  HOH HOH A . 
Q 8 HOH 18  418 52  HOH HOH A . 
Q 8 HOH 19  419 54  HOH HOH A . 
Q 8 HOH 20  420 55  HOH HOH A . 
Q 8 HOH 21  421 61  HOH HOH A . 
Q 8 HOH 22  422 62  HOH HOH A . 
Q 8 HOH 23  423 64  HOH HOH A . 
Q 8 HOH 24  424 65  HOH HOH A . 
Q 8 HOH 25  425 68  HOH HOH A . 
Q 8 HOH 26  426 70  HOH HOH A . 
Q 8 HOH 27  427 72  HOH HOH A . 
Q 8 HOH 28  428 73  HOH HOH A . 
Q 8 HOH 29  429 74  HOH HOH A . 
Q 8 HOH 30  430 77  HOH HOH A . 
Q 8 HOH 31  431 80  HOH HOH A . 
Q 8 HOH 32  432 81  HOH HOH A . 
Q 8 HOH 33  433 82  HOH HOH A . 
Q 8 HOH 34  434 85  HOH HOH A . 
Q 8 HOH 35  435 86  HOH HOH A . 
Q 8 HOH 36  436 87  HOH HOH A . 
Q 8 HOH 37  437 89  HOH HOH A . 
Q 8 HOH 38  438 94  HOH HOH A . 
Q 8 HOH 39  439 97  HOH HOH A . 
Q 8 HOH 40  440 98  HOH HOH A . 
Q 8 HOH 41  441 104 HOH HOH A . 
Q 8 HOH 42  442 107 HOH HOH A . 
Q 8 HOH 43  443 109 HOH HOH A . 
Q 8 HOH 44  444 110 HOH HOH A . 
Q 8 HOH 45  445 113 HOH HOH A . 
Q 8 HOH 46  446 116 HOH HOH A . 
Q 8 HOH 47  447 119 HOH HOH A . 
Q 8 HOH 48  448 120 HOH HOH A . 
Q 8 HOH 49  449 126 HOH HOH A . 
Q 8 HOH 50  450 127 HOH HOH A . 
Q 8 HOH 51  451 129 HOH HOH A . 
Q 8 HOH 52  452 131 HOH HOH A . 
Q 8 HOH 53  453 132 HOH HOH A . 
Q 8 HOH 54  454 134 HOH HOH A . 
Q 8 HOH 55  455 136 HOH HOH A . 
Q 8 HOH 56  456 137 HOH HOH A . 
Q 8 HOH 57  457 138 HOH HOH A . 
Q 8 HOH 58  458 139 HOH HOH A . 
Q 8 HOH 59  459 140 HOH HOH A . 
Q 8 HOH 60  460 142 HOH HOH A . 
Q 8 HOH 61  461 143 HOH HOH A . 
Q 8 HOH 62  462 144 HOH HOH A . 
Q 8 HOH 63  463 147 HOH HOH A . 
Q 8 HOH 64  464 150 HOH HOH A . 
Q 8 HOH 65  465 154 HOH HOH A . 
Q 8 HOH 66  466 155 HOH HOH A . 
Q 8 HOH 67  467 157 HOH HOH A . 
Q 8 HOH 68  468 158 HOH HOH A . 
Q 8 HOH 69  469 160 HOH HOH A . 
Q 8 HOH 70  470 164 HOH HOH A . 
Q 8 HOH 71  471 167 HOH HOH A . 
Q 8 HOH 72  472 168 HOH HOH A . 
Q 8 HOH 73  473 175 HOH HOH A . 
Q 8 HOH 74  474 176 HOH HOH A . 
Q 8 HOH 75  475 178 HOH HOH A . 
Q 8 HOH 76  476 179 HOH HOH A . 
Q 8 HOH 77  477 182 HOH HOH A . 
Q 8 HOH 78  478 183 HOH HOH A . 
Q 8 HOH 79  479 184 HOH HOH A . 
Q 8 HOH 80  480 185 HOH HOH A . 
Q 8 HOH 81  481 186 HOH HOH A . 
Q 8 HOH 82  482 187 HOH HOH A . 
Q 8 HOH 83  483 188 HOH HOH A . 
Q 8 HOH 84  484 189 HOH HOH A . 
Q 8 HOH 85  485 191 HOH HOH A . 
Q 8 HOH 86  486 196 HOH HOH A . 
Q 8 HOH 87  487 201 HOH HOH A . 
Q 8 HOH 88  488 202 HOH HOH A . 
Q 8 HOH 89  489 203 HOH HOH A . 
Q 8 HOH 90  490 204 HOH HOH A . 
Q 8 HOH 91  491 205 HOH HOH A . 
Q 8 HOH 92  492 207 HOH HOH A . 
Q 8 HOH 93  493 208 HOH HOH A . 
Q 8 HOH 94  494 209 HOH HOH A . 
Q 8 HOH 95  495 210 HOH HOH A . 
Q 8 HOH 96  496 211 HOH HOH A . 
Q 8 HOH 97  497 216 HOH HOH A . 
Q 8 HOH 98  498 217 HOH HOH A . 
Q 8 HOH 99  499 224 HOH HOH A . 
Q 8 HOH 100 500 227 HOH HOH A . 
Q 8 HOH 101 501 230 HOH HOH A . 
Q 8 HOH 102 502 232 HOH HOH A . 
Q 8 HOH 103 503 235 HOH HOH A . 
Q 8 HOH 104 504 239 HOH HOH A . 
Q 8 HOH 105 505 240 HOH HOH A . 
Q 8 HOH 106 506 243 HOH HOH A . 
Q 8 HOH 107 507 250 HOH HOH A . 
Q 8 HOH 108 508 252 HOH HOH A . 
Q 8 HOH 109 509 254 HOH HOH A . 
Q 8 HOH 110 510 255 HOH HOH A . 
Q 8 HOH 111 511 261 HOH HOH A . 
Q 8 HOH 112 512 263 HOH HOH A . 
Q 8 HOH 113 513 265 HOH HOH A . 
Q 8 HOH 114 514 267 HOH HOH A . 
Q 8 HOH 115 515 270 HOH HOH A . 
Q 8 HOH 116 516 272 HOH HOH A . 
Q 8 HOH 117 517 275 HOH HOH A . 
Q 8 HOH 118 518 277 HOH HOH A . 
Q 8 HOH 119 519 279 HOH HOH A . 
Q 8 HOH 120 520 280 HOH HOH A . 
Q 8 HOH 121 521 281 HOH HOH A . 
Q 8 HOH 122 522 282 HOH HOH A . 
Q 8 HOH 123 523 285 HOH HOH A . 
Q 8 HOH 124 524 287 HOH HOH A . 
Q 8 HOH 125 525 288 HOH HOH A . 
Q 8 HOH 126 526 289 HOH HOH A . 
Q 8 HOH 127 527 290 HOH HOH A . 
Q 8 HOH 128 528 291 HOH HOH A . 
Q 8 HOH 129 529 295 HOH HOH A . 
Q 8 HOH 130 530 296 HOH HOH A . 
Q 8 HOH 131 531 299 HOH HOH A . 
Q 8 HOH 132 532 300 HOH HOH A . 
Q 8 HOH 133 533 301 HOH HOH A . 
Q 8 HOH 134 534 302 HOH HOH A . 
Q 8 HOH 135 535 303 HOH HOH A . 
Q 8 HOH 136 536 305 HOH HOH A . 
Q 8 HOH 137 537 309 HOH HOH A . 
Q 8 HOH 138 538 310 HOH HOH A . 
Q 8 HOH 139 539 311 HOH HOH A . 
Q 8 HOH 140 540 312 HOH HOH A . 
Q 8 HOH 141 541 313 HOH HOH A . 
Q 8 HOH 142 542 314 HOH HOH A . 
Q 8 HOH 143 543 315 HOH HOH A . 
Q 8 HOH 144 544 317 HOH HOH A . 
Q 8 HOH 145 545 318 HOH HOH A . 
Q 8 HOH 146 546 319 HOH HOH A . 
Q 8 HOH 147 547 322 HOH HOH A . 
Q 8 HOH 148 548 327 HOH HOH A . 
Q 8 HOH 149 549 329 HOH HOH A . 
Q 8 HOH 150 550 334 HOH HOH A . 
Q 8 HOH 151 551 335 HOH HOH A . 
Q 8 HOH 152 552 336 HOH HOH A . 
Q 8 HOH 153 553 337 HOH HOH A . 
Q 8 HOH 154 554 339 HOH HOH A . 
Q 8 HOH 155 555 340 HOH HOH A . 
Q 8 HOH 156 556 344 HOH HOH A . 
Q 8 HOH 157 557 345 HOH HOH A . 
Q 8 HOH 158 558 349 HOH HOH A . 
Q 8 HOH 159 559 351 HOH HOH A . 
Q 8 HOH 160 560 352 HOH HOH A . 
Q 8 HOH 161 561 353 HOH HOH A . 
Q 8 HOH 162 562 354 HOH HOH A . 
Q 8 HOH 163 563 355 HOH HOH A . 
Q 8 HOH 164 564 356 HOH HOH A . 
Q 8 HOH 165 565 357 HOH HOH A . 
Q 8 HOH 166 566 358 HOH HOH A . 
Q 8 HOH 167 567 359 HOH HOH A . 
Q 8 HOH 168 568 360 HOH HOH A . 
Q 8 HOH 169 569 361 HOH HOH A . 
Q 8 HOH 170 570 362 HOH HOH A . 
Q 8 HOH 171 571 363 HOH HOH A . 
Q 8 HOH 172 572 364 HOH HOH A . 
Q 8 HOH 173 573 365 HOH HOH A . 
Q 8 HOH 174 574 366 HOH HOH A . 
Q 8 HOH 175 575 367 HOH HOH A . 
Q 8 HOH 176 576 368 HOH HOH A . 
Q 8 HOH 177 577 369 HOH HOH A . 
Q 8 HOH 178 578 371 HOH HOH A . 
Q 8 HOH 179 579 373 HOH HOH A . 
Q 8 HOH 180 580 375 HOH HOH A . 
Q 8 HOH 181 581 376 HOH HOH A . 
Q 8 HOH 182 582 377 HOH HOH A . 
Q 8 HOH 183 583 381 HOH HOH A . 
Q 8 HOH 184 584 384 HOH HOH A . 
Q 8 HOH 185 585 386 HOH HOH A . 
Q 8 HOH 186 586 388 HOH HOH A . 
Q 8 HOH 187 587 390 HOH HOH A . 
Q 8 HOH 188 588 391 HOH HOH A . 
Q 8 HOH 189 589 392 HOH HOH A . 
Q 8 HOH 190 590 396 HOH HOH A . 
Q 8 HOH 191 591 397 HOH HOH A . 
Q 8 HOH 192 592 398 HOH HOH A . 
Q 8 HOH 193 593 401 HOH HOH A . 
Q 8 HOH 194 594 402 HOH HOH A . 
Q 8 HOH 195 595 405 HOH HOH A . 
Q 8 HOH 196 596 408 HOH HOH A . 
Q 8 HOH 197 597 410 HOH HOH A . 
Q 8 HOH 198 598 415 HOH HOH A . 
Q 8 HOH 199 599 416 HOH HOH A . 
Q 8 HOH 200 600 417 HOH HOH A . 
Q 8 HOH 201 601 419 HOH HOH A . 
Q 8 HOH 202 602 420 HOH HOH A . 
Q 8 HOH 203 603 422 HOH HOH A . 
Q 8 HOH 204 604 424 HOH HOH A . 
Q 8 HOH 205 605 426 HOH HOH A . 
Q 8 HOH 206 606 428 HOH HOH A . 
Q 8 HOH 207 607 429 HOH HOH A . 
Q 8 HOH 208 608 431 HOH HOH A . 
Q 8 HOH 209 609 435 HOH HOH A . 
Q 8 HOH 210 610 437 HOH HOH A . 
Q 8 HOH 211 611 439 HOH HOH A . 
Q 8 HOH 212 612 440 HOH HOH A . 
Q 8 HOH 213 613 442 HOH HOH A . 
Q 8 HOH 214 614 444 HOH HOH A . 
Q 8 HOH 215 615 445 HOH HOH A . 
Q 8 HOH 216 616 446 HOH HOH A . 
Q 8 HOH 217 617 447 HOH HOH A . 
Q 8 HOH 218 618 448 HOH HOH A . 
Q 8 HOH 219 619 450 HOH HOH A . 
Q 8 HOH 220 620 453 HOH HOH A . 
Q 8 HOH 221 621 456 HOH HOH A . 
Q 8 HOH 222 622 457 HOH HOH A . 
Q 8 HOH 223 623 461 HOH HOH A . 
Q 8 HOH 224 624 462 HOH HOH A . 
Q 8 HOH 225 625 463 HOH HOH A . 
Q 8 HOH 226 626 464 HOH HOH A . 
Q 8 HOH 227 627 468 HOH HOH A . 
Q 8 HOH 228 628 469 HOH HOH A . 
Q 8 HOH 229 629 496 HOH HOH A . 
Q 8 HOH 230 630 497 HOH HOH A . 
Q 8 HOH 231 631 498 HOH HOH A . 
Q 8 HOH 232 632 499 HOH HOH A . 
Q 8 HOH 233 633 500 HOH HOH A . 
Q 8 HOH 234 634 501 HOH HOH A . 
Q 8 HOH 235 635 502 HOH HOH A . 
Q 8 HOH 236 636 505 HOH HOH A . 
Q 8 HOH 237 637 511 HOH HOH A . 
Q 8 HOH 238 638 512 HOH HOH A . 
Q 8 HOH 239 639 513 HOH HOH A . 
Q 8 HOH 240 640 532 HOH HOH A . 
Q 8 HOH 241 641 533 HOH HOH A . 
Q 8 HOH 242 642 534 HOH HOH A . 
Q 8 HOH 243 643 535 HOH HOH A . 
Q 8 HOH 244 644 536 HOH HOH A . 
Q 8 HOH 245 645 537 HOH HOH A . 
Q 8 HOH 246 646 538 HOH HOH A . 
Q 8 HOH 247 647 539 HOH HOH A . 
Q 8 HOH 248 648 540 HOH HOH A . 
Q 8 HOH 249 649 541 HOH HOH A . 
Q 8 HOH 250 650 542 HOH HOH A . 
Q 8 HOH 251 651 543 HOH HOH A . 
Q 8 HOH 252 652 544 HOH HOH A . 
Q 8 HOH 253 653 545 HOH HOH A . 
Q 8 HOH 254 654 546 HOH HOH A . 
Q 8 HOH 255 655 547 HOH HOH A . 
Q 8 HOH 256 656 548 HOH HOH A . 
Q 8 HOH 257 657 549 HOH HOH A . 
Q 8 HOH 258 658 550 HOH HOH A . 
Q 8 HOH 259 659 551 HOH HOH A . 
Q 8 HOH 260 660 552 HOH HOH A . 
Q 8 HOH 261 661 553 HOH HOH A . 
Q 8 HOH 262 662 554 HOH HOH A . 
Q 8 HOH 263 663 555 HOH HOH A . 
Q 8 HOH 264 664 557 HOH HOH A . 
Q 8 HOH 265 665 558 HOH HOH A . 
Q 8 HOH 266 666 559 HOH HOH A . 
Q 8 HOH 267 667 560 HOH HOH A . 
Q 8 HOH 268 668 562 HOH HOH A . 
Q 8 HOH 269 669 565 HOH HOH A . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,P 
2 1 B,K,L,M,N,O,Q       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 NE2 ? A HIS 98  ? B HIS 98  ? 1_555 101.8 ? 
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_555 112.5 ? 
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 96.9  ? 
4  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N19 B D E1F .   ? B E1F 302 ? 1_555 96.4  ? 
5  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N19 B D E1F .   ? B E1F 302 ? 1_555 119.2 ? 
6  ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N19 B D E1F .   ? B E1F 302 ? 1_555 127.8 ? 
7  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N19 A D E1F .   ? B E1F 302 ? 1_555 115.8 ? 
8  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N19 A D E1F .   ? B E1F 302 ? 1_555 114.2 ? 
9  ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N19 A D E1F .   ? B E1F 302 ? 1_555 113.5 ? 
10 N19 B D E1F .   ? B E1F 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N19 A D E1F .   ? B E1F 302 ? 1_555 19.6  ? 
11 NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S16 B D E1F .   ? B E1F 302 ? 1_555 90.8  ? 
12 NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S16 B D E1F .   ? B E1F 302 ? 1_555 149.8 ? 
13 ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S16 B D E1F .   ? B E1F 302 ? 1_555 103.4 ? 
14 N19 B D E1F .   ? B E1F 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S16 B D E1F .   ? B E1F 302 ? 1_555 31.2  ? 
15 N19 A D E1F .   ? B E1F 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S16 B D E1F .   ? B E1F 302 ? 1_555 36.7  ? 
16 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? K ZN . ? A ZN 301 ? 1_555 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 103.7 ? 
17 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? K ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 112.1 ? 
18 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? K ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 96.5  ? 
19 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? K ZN . ? A ZN 301 ? 1_555 N19 ? L E1F .   ? A E1F 302 ? 1_555 109.9 ? 
20 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? K ZN . ? A ZN 301 ? 1_555 N19 ? L E1F .   ? A E1F 302 ? 1_555 114.1 ? 
21 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 ZN ? K ZN . ? A ZN 301 ? 1_555 N19 ? L E1F .   ? A E1F 302 ? 1_555 119.0 ? 
22 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? K ZN . ? A ZN 301 ? 1_555 S16 ? L E1F .   ? A E1F 302 ? 1_555 98.4  ? 
23 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? K ZN . ? A ZN 301 ? 1_555 S16 ? L E1F .   ? A E1F 302 ? 1_555 144.6 ? 
24 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 ZN ? K ZN . ? A ZN 301 ? 1_555 S16 ? L E1F .   ? A E1F 302 ? 1_555 100.5 ? 
25 N19 ? L E1F .   ? A E1F 302 ? 1_555 ZN ? K ZN . ? A ZN 301 ? 1_555 S16 ? L E1F .   ? A E1F 302 ? 1_555 31.0  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2013-11-06 
2 'Structure model' 1 1 2018-05-16 
3 'Structure model' 1 2 2023-11-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Refinement description' 
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Database references'    
5 3 'Structure model' 'Derived calculations'   
6 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  2 'Structure model' diffrn_source                 
2  2 'Structure model' software                      
3  3 'Structure model' chem_comp_atom                
4  3 'Structure model' chem_comp_bond                
5  3 'Structure model' database_2                    
6  3 'Structure model' pdbx_initial_refinement_model 
7  3 'Structure model' pdbx_struct_conn_angle        
8  3 'Structure model' struct_conn                   
9  3 'Structure model' struct_ref_seq_dif            
10 3 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
2  2 'Structure model' '_software.version'                           
3  3 'Structure model' '_database_2.pdbx_DOI'                        
4  3 'Structure model' '_database_2.pdbx_database_accession'         
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_alt_id'  
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_alt_id'  
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
17 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
18 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
19 3 'Structure model' '_pdbx_struct_conn_angle.value'               
20 3 'Structure model' '_struct_conn.pdbx_dist_value'                
21 3 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
22 3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
23 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
24 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
25 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
26 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
27 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
28 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
29 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
30 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
31 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
32 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
33 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
34 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
35 3 'Structure model' '_struct_ref_seq_dif.details'                 
36 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
37 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
38 3 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      5.2.0019 ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
SCALA       3.2.19   22/12/2005      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk 'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 2 
PDB_EXTRACT 3.006    'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 3 
DNA         .        ?               ?       ?                    ?                     'data collection' ? ?          ? 4 
XDS         .        ?               ?       ?                    ?                     'data reduction'  ? ?          ? 5 
MOLREP      .        ?               ?       ?                    ?                     phasing           ? ?          ? 6 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NH2 A ARG 177 ? B O A HOH 659 ? ? 1.67 
2 1 NZ  A LYS 254 ? A O A HOH 532 ? ? 2.01 
3 1 NH1 A ARG 93  ? A O A HOH 607 ? ? 2.01 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             135 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            B 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             135 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            B 
_pdbx_validate_rmsd_bond.bond_value                1.323 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            0.071 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              177 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              177 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              177 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                124.97 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            4.67 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER B 67  ? ? -174.58 -177.43 
2  1 ASN B 77  ? ? -94.77  46.72   
3  1 HIS B 105 ? ? -159.47 89.44   
4  1 PHE B 178 ? ? -161.81 115.83  
5  1 ASN B 246 ? ? -153.51 46.56   
6  1 LYS A 59  ? ? -120.12 -54.05  
7  1 SER A 67  ? ? -177.29 -176.44 
8  1 ASP A 73  ? A -37.46  132.36  
9  1 ARG A 93  ? A -130.77 -34.35  
10 1 ASN A 246 ? ? -155.31 47.11   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 B MET 1 ? A MET 1 
2  1 Y 1 B MET 2 ? A MET 2 
3  1 Y 1 B SER 3 ? A SER 3 
4  1 Y 1 B ARG 4 ? A ARG 4 
5  1 Y 1 B LEU 5 ? A LEU 5 
6  1 Y 1 A MET 1 ? B MET 1 
7  1 Y 1 A MET 2 ? B MET 2 
8  1 Y 1 A SER 3 ? B SER 3 
9  1 Y 1 A ARG 4 ? B ARG 4 
10 1 Y 1 A LEU 5 ? B LEU 5 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ACY C    C  N N 1   
ACY O    O  N N 2   
ACY OXT  O  N N 3   
ACY CH3  C  N N 4   
ACY HXT  H  N N 5   
ACY H1   H  N N 6   
ACY H2   H  N N 7   
ACY H3   H  N N 8   
ALA N    N  N N 9   
ALA CA   C  N S 10  
ALA C    C  N N 11  
ALA O    O  N N 12  
ALA CB   C  N N 13  
ALA OXT  O  N N 14  
ALA H    H  N N 15  
ALA H2   H  N N 16  
ALA HA   H  N N 17  
ALA HB1  H  N N 18  
ALA HB2  H  N N 19  
ALA HB3  H  N N 20  
ALA HXT  H  N N 21  
ARG N    N  N N 22  
ARG CA   C  N S 23  
ARG C    C  N N 24  
ARG O    O  N N 25  
ARG CB   C  N N 26  
ARG CG   C  N N 27  
ARG CD   C  N N 28  
ARG NE   N  N N 29  
ARG CZ   C  N N 30  
ARG NH1  N  N N 31  
ARG NH2  N  N N 32  
ARG OXT  O  N N 33  
ARG H    H  N N 34  
ARG H2   H  N N 35  
ARG HA   H  N N 36  
ARG HB2  H  N N 37  
ARG HB3  H  N N 38  
ARG HG2  H  N N 39  
ARG HG3  H  N N 40  
ARG HD2  H  N N 41  
ARG HD3  H  N N 42  
ARG HE   H  N N 43  
ARG HH11 H  N N 44  
ARG HH12 H  N N 45  
ARG HH21 H  N N 46  
ARG HH22 H  N N 47  
ARG HXT  H  N N 48  
ASN N    N  N N 49  
ASN CA   C  N S 50  
ASN C    C  N N 51  
ASN O    O  N N 52  
ASN CB   C  N N 53  
ASN CG   C  N N 54  
ASN OD1  O  N N 55  
ASN ND2  N  N N 56  
ASN OXT  O  N N 57  
ASN H    H  N N 58  
ASN H2   H  N N 59  
ASN HA   H  N N 60  
ASN HB2  H  N N 61  
ASN HB3  H  N N 62  
ASN HD21 H  N N 63  
ASN HD22 H  N N 64  
ASN HXT  H  N N 65  
ASP N    N  N N 66  
ASP CA   C  N S 67  
ASP C    C  N N 68  
ASP O    O  N N 69  
ASP CB   C  N N 70  
ASP CG   C  N N 71  
ASP OD1  O  N N 72  
ASP OD2  O  N N 73  
ASP OXT  O  N N 74  
ASP H    H  N N 75  
ASP H2   H  N N 76  
ASP HA   H  N N 77  
ASP HB2  H  N N 78  
ASP HB3  H  N N 79  
ASP HD2  H  N N 80  
ASP HXT  H  N N 81  
CIT C1   C  N N 82  
CIT O1   O  N N 83  
CIT O2   O  N N 84  
CIT C2   C  N N 85  
CIT C3   C  N N 86  
CIT O7   O  N N 87  
CIT C4   C  N N 88  
CIT C5   C  N N 89  
CIT O3   O  N N 90  
CIT O4   O  N N 91  
CIT C6   C  N N 92  
CIT O5   O  N N 93  
CIT O6   O  N N 94  
CIT HO2  H  N N 95  
CIT H21  H  N N 96  
CIT H22  H  N N 97  
CIT HO7  H  N N 98  
CIT H41  H  N N 99  
CIT H42  H  N N 100 
CIT HO4  H  N N 101 
CIT HO6  H  N N 102 
CYS N    N  N N 103 
CYS CA   C  N R 104 
CYS C    C  N N 105 
CYS O    O  N N 106 
CYS CB   C  N N 107 
CYS SG   S  N N 108 
CYS OXT  O  N N 109 
CYS H    H  N N 110 
CYS H2   H  N N 111 
CYS HA   H  N N 112 
CYS HB2  H  N N 113 
CYS HB3  H  N N 114 
CYS HG   H  N N 115 
CYS HXT  H  N N 116 
E1F O18  O  N N 117 
E1F C13  C  Y N 118 
E1F C1   C  Y N 119 
E1F C2   C  Y N 120 
E1F CL1  CL N N 121 
E1F C21  C  Y N 122 
E1F C5   C  Y N 123 
E1F C4   C  Y N 124 
E1F C3   C  Y N 125 
E1F S16  S  N N 126 
E1F N19  N  N N 127 
E1F O17  O  N N 128 
E1F C6   C  N N 129 
E1F O12  O  N N 130 
E1F C7   C  N N 131 
E1F S8   S  N N 132 
E1F C9   C  Y N 133 
E1F N11  N  Y N 134 
E1F C14  C  Y N 135 
E1F C15  C  Y N 136 
E1F N10  N  Y N 137 
E1F H1   H  N N 138 
E1F H2   H  N N 139 
E1F H3   H  N N 140 
E1F H4   H  N N 141 
E1F H5   H  N N 142 
E1F H6   H  N N 143 
E1F H7   H  N N 144 
E1F H8   H  N N 145 
E1F H9   H  N N 146 
E1F H10  H  N N 147 
EDO C1   C  N N 148 
EDO O1   O  N N 149 
EDO C2   C  N N 150 
EDO O2   O  N N 151 
EDO H11  H  N N 152 
EDO H12  H  N N 153 
EDO HO1  H  N N 154 
EDO H21  H  N N 155 
EDO H22  H  N N 156 
EDO HO2  H  N N 157 
GLN N    N  N N 158 
GLN CA   C  N S 159 
GLN C    C  N N 160 
GLN O    O  N N 161 
GLN CB   C  N N 162 
GLN CG   C  N N 163 
GLN CD   C  N N 164 
GLN OE1  O  N N 165 
GLN NE2  N  N N 166 
GLN OXT  O  N N 167 
GLN H    H  N N 168 
GLN H2   H  N N 169 
GLN HA   H  N N 170 
GLN HB2  H  N N 171 
GLN HB3  H  N N 172 
GLN HG2  H  N N 173 
GLN HG3  H  N N 174 
GLN HE21 H  N N 175 
GLN HE22 H  N N 176 
GLN HXT  H  N N 177 
GLU N    N  N N 178 
GLU CA   C  N S 179 
GLU C    C  N N 180 
GLU O    O  N N 181 
GLU CB   C  N N 182 
GLU CG   C  N N 183 
GLU CD   C  N N 184 
GLU OE1  O  N N 185 
GLU OE2  O  N N 186 
GLU OXT  O  N N 187 
GLU H    H  N N 188 
GLU H2   H  N N 189 
GLU HA   H  N N 190 
GLU HB2  H  N N 191 
GLU HB3  H  N N 192 
GLU HG2  H  N N 193 
GLU HG3  H  N N 194 
GLU HE2  H  N N 195 
GLU HXT  H  N N 196 
GLY N    N  N N 197 
GLY CA   C  N N 198 
GLY C    C  N N 199 
GLY O    O  N N 200 
GLY OXT  O  N N 201 
GLY H    H  N N 202 
GLY H2   H  N N 203 
GLY HA2  H  N N 204 
GLY HA3  H  N N 205 
GLY HXT  H  N N 206 
HIS N    N  N N 207 
HIS CA   C  N S 208 
HIS C    C  N N 209 
HIS O    O  N N 210 
HIS CB   C  N N 211 
HIS CG   C  Y N 212 
HIS ND1  N  Y N 213 
HIS CD2  C  Y N 214 
HIS CE1  C  Y N 215 
HIS NE2  N  Y N 216 
HIS OXT  O  N N 217 
HIS H    H  N N 218 
HIS H2   H  N N 219 
HIS HA   H  N N 220 
HIS HB2  H  N N 221 
HIS HB3  H  N N 222 
HIS HD1  H  N N 223 
HIS HD2  H  N N 224 
HIS HE1  H  N N 225 
HIS HE2  H  N N 226 
HIS HXT  H  N N 227 
HOH O    O  N N 228 
HOH H1   H  N N 229 
HOH H2   H  N N 230 
ILE N    N  N N 231 
ILE CA   C  N S 232 
ILE C    C  N N 233 
ILE O    O  N N 234 
ILE CB   C  N S 235 
ILE CG1  C  N N 236 
ILE CG2  C  N N 237 
ILE CD1  C  N N 238 
ILE OXT  O  N N 239 
ILE H    H  N N 240 
ILE H2   H  N N 241 
ILE HA   H  N N 242 
ILE HB   H  N N 243 
ILE HG12 H  N N 244 
ILE HG13 H  N N 245 
ILE HG21 H  N N 246 
ILE HG22 H  N N 247 
ILE HG23 H  N N 248 
ILE HD11 H  N N 249 
ILE HD12 H  N N 250 
ILE HD13 H  N N 251 
ILE HXT  H  N N 252 
LEU N    N  N N 253 
LEU CA   C  N S 254 
LEU C    C  N N 255 
LEU O    O  N N 256 
LEU CB   C  N N 257 
LEU CG   C  N N 258 
LEU CD1  C  N N 259 
LEU CD2  C  N N 260 
LEU OXT  O  N N 261 
LEU H    H  N N 262 
LEU H2   H  N N 263 
LEU HA   H  N N 264 
LEU HB2  H  N N 265 
LEU HB3  H  N N 266 
LEU HG   H  N N 267 
LEU HD11 H  N N 268 
LEU HD12 H  N N 269 
LEU HD13 H  N N 270 
LEU HD21 H  N N 271 
LEU HD22 H  N N 272 
LEU HD23 H  N N 273 
LEU HXT  H  N N 274 
LYS N    N  N N 275 
LYS CA   C  N S 276 
LYS C    C  N N 277 
LYS O    O  N N 278 
LYS CB   C  N N 279 
LYS CG   C  N N 280 
LYS CD   C  N N 281 
LYS CE   C  N N 282 
LYS NZ   N  N N 283 
LYS OXT  O  N N 284 
LYS H    H  N N 285 
LYS H2   H  N N 286 
LYS HA   H  N N 287 
LYS HB2  H  N N 288 
LYS HB3  H  N N 289 
LYS HG2  H  N N 290 
LYS HG3  H  N N 291 
LYS HD2  H  N N 292 
LYS HD3  H  N N 293 
LYS HE2  H  N N 294 
LYS HE3  H  N N 295 
LYS HZ1  H  N N 296 
LYS HZ2  H  N N 297 
LYS HZ3  H  N N 298 
LYS HXT  H  N N 299 
MET N    N  N N 300 
MET CA   C  N S 301 
MET C    C  N N 302 
MET O    O  N N 303 
MET CB   C  N N 304 
MET CG   C  N N 305 
MET SD   S  N N 306 
MET CE   C  N N 307 
MET OXT  O  N N 308 
MET H    H  N N 309 
MET H2   H  N N 310 
MET HA   H  N N 311 
MET HB2  H  N N 312 
MET HB3  H  N N 313 
MET HG2  H  N N 314 
MET HG3  H  N N 315 
MET HE1  H  N N 316 
MET HE2  H  N N 317 
MET HE3  H  N N 318 
MET HXT  H  N N 319 
PEG C1   C  N N 320 
PEG O1   O  N N 321 
PEG C2   C  N N 322 
PEG O2   O  N N 323 
PEG C3   C  N N 324 
PEG C4   C  N N 325 
PEG O4   O  N N 326 
PEG H11  H  N N 327 
PEG H12  H  N N 328 
PEG HO1  H  N N 329 
PEG H21  H  N N 330 
PEG H22  H  N N 331 
PEG H31  H  N N 332 
PEG H32  H  N N 333 
PEG H41  H  N N 334 
PEG H42  H  N N 335 
PEG HO4  H  N N 336 
PHE N    N  N N 337 
PHE CA   C  N S 338 
PHE C    C  N N 339 
PHE O    O  N N 340 
PHE CB   C  N N 341 
PHE CG   C  Y N 342 
PHE CD1  C  Y N 343 
PHE CD2  C  Y N 344 
PHE CE1  C  Y N 345 
PHE CE2  C  Y N 346 
PHE CZ   C  Y N 347 
PHE OXT  O  N N 348 
PHE H    H  N N 349 
PHE H2   H  N N 350 
PHE HA   H  N N 351 
PHE HB2  H  N N 352 
PHE HB3  H  N N 353 
PHE HD1  H  N N 354 
PHE HD2  H  N N 355 
PHE HE1  H  N N 356 
PHE HE2  H  N N 357 
PHE HZ   H  N N 358 
PHE HXT  H  N N 359 
PRO N    N  N N 360 
PRO CA   C  N S 361 
PRO C    C  N N 362 
PRO O    O  N N 363 
PRO CB   C  N N 364 
PRO CG   C  N N 365 
PRO CD   C  N N 366 
PRO OXT  O  N N 367 
PRO H    H  N N 368 
PRO HA   H  N N 369 
PRO HB2  H  N N 370 
PRO HB3  H  N N 371 
PRO HG2  H  N N 372 
PRO HG3  H  N N 373 
PRO HD2  H  N N 374 
PRO HD3  H  N N 375 
PRO HXT  H  N N 376 
SER N    N  N N 377 
SER CA   C  N S 378 
SER C    C  N N 379 
SER O    O  N N 380 
SER CB   C  N N 381 
SER OG   O  N N 382 
SER OXT  O  N N 383 
SER H    H  N N 384 
SER H2   H  N N 385 
SER HA   H  N N 386 
SER HB2  H  N N 387 
SER HB3  H  N N 388 
SER HG   H  N N 389 
SER HXT  H  N N 390 
THR N    N  N N 391 
THR CA   C  N S 392 
THR C    C  N N 393 
THR O    O  N N 394 
THR CB   C  N R 395 
THR OG1  O  N N 396 
THR CG2  C  N N 397 
THR OXT  O  N N 398 
THR H    H  N N 399 
THR H2   H  N N 400 
THR HA   H  N N 401 
THR HB   H  N N 402 
THR HG1  H  N N 403 
THR HG21 H  N N 404 
THR HG22 H  N N 405 
THR HG23 H  N N 406 
THR HXT  H  N N 407 
TRP N    N  N N 408 
TRP CA   C  N S 409 
TRP C    C  N N 410 
TRP O    O  N N 411 
TRP CB   C  N N 412 
TRP CG   C  Y N 413 
TRP CD1  C  Y N 414 
TRP CD2  C  Y N 415 
TRP NE1  N  Y N 416 
TRP CE2  C  Y N 417 
TRP CE3  C  Y N 418 
TRP CZ2  C  Y N 419 
TRP CZ3  C  Y N 420 
TRP CH2  C  Y N 421 
TRP OXT  O  N N 422 
TRP H    H  N N 423 
TRP H2   H  N N 424 
TRP HA   H  N N 425 
TRP HB2  H  N N 426 
TRP HB3  H  N N 427 
TRP HD1  H  N N 428 
TRP HE1  H  N N 429 
TRP HE3  H  N N 430 
TRP HZ2  H  N N 431 
TRP HZ3  H  N N 432 
TRP HH2  H  N N 433 
TRP HXT  H  N N 434 
TYR N    N  N N 435 
TYR CA   C  N S 436 
TYR C    C  N N 437 
TYR O    O  N N 438 
TYR CB   C  N N 439 
TYR CG   C  Y N 440 
TYR CD1  C  Y N 441 
TYR CD2  C  Y N 442 
TYR CE1  C  Y N 443 
TYR CE2  C  Y N 444 
TYR CZ   C  Y N 445 
TYR OH   O  N N 446 
TYR OXT  O  N N 447 
TYR H    H  N N 448 
TYR H2   H  N N 449 
TYR HA   H  N N 450 
TYR HB2  H  N N 451 
TYR HB3  H  N N 452 
TYR HD1  H  N N 453 
TYR HD2  H  N N 454 
TYR HE1  H  N N 455 
TYR HE2  H  N N 456 
TYR HH   H  N N 457 
TYR HXT  H  N N 458 
VAL N    N  N N 459 
VAL CA   C  N S 460 
VAL C    C  N N 461 
VAL O    O  N N 462 
VAL CB   C  N N 463 
VAL CG1  C  N N 464 
VAL CG2  C  N N 465 
VAL OXT  O  N N 466 
VAL H    H  N N 467 
VAL H2   H  N N 468 
VAL HA   H  N N 469 
VAL HB   H  N N 470 
VAL HG11 H  N N 471 
VAL HG12 H  N N 472 
VAL HG13 H  N N 473 
VAL HG21 H  N N 474 
VAL HG22 H  N N 475 
VAL HG23 H  N N 476 
VAL HXT  H  N N 477 
ZN  ZN   ZN N N 478 
# 
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 
ACY C   O    doub N N 1   
ACY C   OXT  sing N N 2   
ACY C   CH3  sing N N 3   
ACY OXT HXT  sing N N 4   
ACY CH3 H1   sing N N 5   
ACY CH3 H2   sing N N 6   
ACY CH3 H3   sing N N 7   
ALA N   CA   sing N N 8   
ALA N   H    sing N N 9   
ALA N   H2   sing N N 10  
ALA CA  C    sing N N 11  
ALA CA  CB   sing N N 12  
ALA CA  HA   sing N N 13  
ALA C   O    doub N N 14  
ALA C   OXT  sing N N 15  
ALA CB  HB1  sing N N 16  
ALA CB  HB2  sing N N 17  
ALA CB  HB3  sing N N 18  
ALA OXT HXT  sing N N 19  
ARG N   CA   sing N N 20  
ARG N   H    sing N N 21  
ARG N   H2   sing N N 22  
ARG CA  C    sing N N 23  
ARG CA  CB   sing N N 24  
ARG CA  HA   sing N N 25  
ARG C   O    doub N N 26  
ARG C   OXT  sing N N 27  
ARG CB  CG   sing N N 28  
ARG CB  HB2  sing N N 29  
ARG CB  HB3  sing N N 30  
ARG CG  CD   sing N N 31  
ARG CG  HG2  sing N N 32  
ARG CG  HG3  sing N N 33  
ARG CD  NE   sing N N 34  
ARG CD  HD2  sing N N 35  
ARG CD  HD3  sing N N 36  
ARG NE  CZ   sing N N 37  
ARG NE  HE   sing N N 38  
ARG CZ  NH1  sing N N 39  
ARG CZ  NH2  doub N N 40  
ARG NH1 HH11 sing N N 41  
ARG NH1 HH12 sing N N 42  
ARG NH2 HH21 sing N N 43  
ARG NH2 HH22 sing N N 44  
ARG OXT HXT  sing N N 45  
ASN N   CA   sing N N 46  
ASN N   H    sing N N 47  
ASN N   H2   sing N N 48  
ASN CA  C    sing N N 49  
ASN CA  CB   sing N N 50  
ASN CA  HA   sing N N 51  
ASN C   O    doub N N 52  
ASN C   OXT  sing N N 53  
ASN CB  CG   sing N N 54  
ASN CB  HB2  sing N N 55  
ASN CB  HB3  sing N N 56  
ASN CG  OD1  doub N N 57  
ASN CG  ND2  sing N N 58  
ASN ND2 HD21 sing N N 59  
ASN ND2 HD22 sing N N 60  
ASN OXT HXT  sing N N 61  
ASP N   CA   sing N N 62  
ASP N   H    sing N N 63  
ASP N   H2   sing N N 64  
ASP CA  C    sing N N 65  
ASP CA  CB   sing N N 66  
ASP CA  HA   sing N N 67  
ASP C   O    doub N N 68  
ASP C   OXT  sing N N 69  
ASP CB  CG   sing N N 70  
ASP CB  HB2  sing N N 71  
ASP CB  HB3  sing N N 72  
ASP CG  OD1  doub N N 73  
ASP CG  OD2  sing N N 74  
ASP OD2 HD2  sing N N 75  
ASP OXT HXT  sing N N 76  
CIT C1  O1   doub N N 77  
CIT C1  O2   sing N N 78  
CIT C1  C2   sing N N 79  
CIT O2  HO2  sing N N 80  
CIT C2  C3   sing N N 81  
CIT C2  H21  sing N N 82  
CIT C2  H22  sing N N 83  
CIT C3  O7   sing N N 84  
CIT C3  C4   sing N N 85  
CIT C3  C6   sing N N 86  
CIT O7  HO7  sing N N 87  
CIT C4  C5   sing N N 88  
CIT C4  H41  sing N N 89  
CIT C4  H42  sing N N 90  
CIT C5  O3   doub N N 91  
CIT C5  O4   sing N N 92  
CIT O4  HO4  sing N N 93  
CIT C6  O5   doub N N 94  
CIT C6  O6   sing N N 95  
CIT O6  HO6  sing N N 96  
CYS N   CA   sing N N 97  
CYS N   H    sing N N 98  
CYS N   H2   sing N N 99  
CYS CA  C    sing N N 100 
CYS CA  CB   sing N N 101 
CYS CA  HA   sing N N 102 
CYS C   O    doub N N 103 
CYS C   OXT  sing N N 104 
CYS CB  SG   sing N N 105 
CYS CB  HB2  sing N N 106 
CYS CB  HB3  sing N N 107 
CYS SG  HG   sing N N 108 
CYS OXT HXT  sing N N 109 
E1F S8  C9   sing N N 110 
E1F S8  C7   sing N N 111 
E1F N11 C9   doub Y N 112 
E1F N11 C14  sing Y N 113 
E1F C9  N10  sing Y N 114 
E1F C7  C6   sing N N 115 
E1F O12 C6   doub N N 116 
E1F C14 C15  doub Y N 117 
E1F C6  C1   sing N N 118 
E1F C5  C1   doub Y N 119 
E1F C5  C4   sing Y N 120 
E1F C1  C21  sing Y N 121 
E1F N10 C13  doub Y N 122 
E1F C15 C13  sing Y N 123 
E1F C4  C3   doub Y N 124 
E1F C21 C2   doub Y N 125 
E1F C3  C2   sing Y N 126 
E1F C3  S16  sing N N 127 
E1F C2  CL1  sing N N 128 
E1F N19 S16  sing N N 129 
E1F O17 S16  doub N N 130 
E1F S16 O18  doub N N 131 
E1F C13 H1   sing N N 132 
E1F C21 H2   sing N N 133 
E1F C5  H3   sing N N 134 
E1F C4  H4   sing N N 135 
E1F N19 H5   sing N N 136 
E1F N19 H6   sing N N 137 
E1F C7  H7   sing N N 138 
E1F C7  H8   sing N N 139 
E1F C14 H9   sing N N 140 
E1F C15 H10  sing N N 141 
EDO C1  O1   sing N N 142 
EDO C1  C2   sing N N 143 
EDO C1  H11  sing N N 144 
EDO C1  H12  sing N N 145 
EDO O1  HO1  sing N N 146 
EDO C2  O2   sing N N 147 
EDO C2  H21  sing N N 148 
EDO C2  H22  sing N N 149 
EDO O2  HO2  sing N N 150 
GLN N   CA   sing N N 151 
GLN N   H    sing N N 152 
GLN N   H2   sing N N 153 
GLN CA  C    sing N N 154 
GLN CA  CB   sing N N 155 
GLN CA  HA   sing N N 156 
GLN C   O    doub N N 157 
GLN C   OXT  sing N N 158 
GLN CB  CG   sing N N 159 
GLN CB  HB2  sing N N 160 
GLN CB  HB3  sing N N 161 
GLN CG  CD   sing N N 162 
GLN CG  HG2  sing N N 163 
GLN CG  HG3  sing N N 164 
GLN CD  OE1  doub N N 165 
GLN CD  NE2  sing N N 166 
GLN NE2 HE21 sing N N 167 
GLN NE2 HE22 sing N N 168 
GLN OXT HXT  sing N N 169 
GLU N   CA   sing N N 170 
GLU N   H    sing N N 171 
GLU N   H2   sing N N 172 
GLU CA  C    sing N N 173 
GLU CA  CB   sing N N 174 
GLU CA  HA   sing N N 175 
GLU C   O    doub N N 176 
GLU C   OXT  sing N N 177 
GLU CB  CG   sing N N 178 
GLU CB  HB2  sing N N 179 
GLU CB  HB3  sing N N 180 
GLU CG  CD   sing N N 181 
GLU CG  HG2  sing N N 182 
GLU CG  HG3  sing N N 183 
GLU CD  OE1  doub N N 184 
GLU CD  OE2  sing N N 185 
GLU OE2 HE2  sing N N 186 
GLU OXT HXT  sing N N 187 
GLY N   CA   sing N N 188 
GLY N   H    sing N N 189 
GLY N   H2   sing N N 190 
GLY CA  C    sing N N 191 
GLY CA  HA2  sing N N 192 
GLY CA  HA3  sing N N 193 
GLY C   O    doub N N 194 
GLY C   OXT  sing N N 195 
GLY OXT HXT  sing N N 196 
HIS N   CA   sing N N 197 
HIS N   H    sing N N 198 
HIS N   H2   sing N N 199 
HIS CA  C    sing N N 200 
HIS CA  CB   sing N N 201 
HIS CA  HA   sing N N 202 
HIS C   O    doub N N 203 
HIS C   OXT  sing N N 204 
HIS CB  CG   sing N N 205 
HIS CB  HB2  sing N N 206 
HIS CB  HB3  sing N N 207 
HIS CG  ND1  sing Y N 208 
HIS CG  CD2  doub Y N 209 
HIS ND1 CE1  doub Y N 210 
HIS ND1 HD1  sing N N 211 
HIS CD2 NE2  sing Y N 212 
HIS CD2 HD2  sing N N 213 
HIS CE1 NE2  sing Y N 214 
HIS CE1 HE1  sing N N 215 
HIS NE2 HE2  sing N N 216 
HIS OXT HXT  sing N N 217 
HOH O   H1   sing N N 218 
HOH O   H2   sing N N 219 
ILE N   CA   sing N N 220 
ILE N   H    sing N N 221 
ILE N   H2   sing N N 222 
ILE CA  C    sing N N 223 
ILE CA  CB   sing N N 224 
ILE CA  HA   sing N N 225 
ILE C   O    doub N N 226 
ILE C   OXT  sing N N 227 
ILE CB  CG1  sing N N 228 
ILE CB  CG2  sing N N 229 
ILE CB  HB   sing N N 230 
ILE CG1 CD1  sing N N 231 
ILE CG1 HG12 sing N N 232 
ILE CG1 HG13 sing N N 233 
ILE CG2 HG21 sing N N 234 
ILE CG2 HG22 sing N N 235 
ILE CG2 HG23 sing N N 236 
ILE CD1 HD11 sing N N 237 
ILE CD1 HD12 sing N N 238 
ILE CD1 HD13 sing N N 239 
ILE OXT HXT  sing N N 240 
LEU N   CA   sing N N 241 
LEU N   H    sing N N 242 
LEU N   H2   sing N N 243 
LEU CA  C    sing N N 244 
LEU CA  CB   sing N N 245 
LEU CA  HA   sing N N 246 
LEU C   O    doub N N 247 
LEU C   OXT  sing N N 248 
LEU CB  CG   sing N N 249 
LEU CB  HB2  sing N N 250 
LEU CB  HB3  sing N N 251 
LEU CG  CD1  sing N N 252 
LEU CG  CD2  sing N N 253 
LEU CG  HG   sing N N 254 
LEU CD1 HD11 sing N N 255 
LEU CD1 HD12 sing N N 256 
LEU CD1 HD13 sing N N 257 
LEU CD2 HD21 sing N N 258 
LEU CD2 HD22 sing N N 259 
LEU CD2 HD23 sing N N 260 
LEU OXT HXT  sing N N 261 
LYS N   CA   sing N N 262 
LYS N   H    sing N N 263 
LYS N   H2   sing N N 264 
LYS CA  C    sing N N 265 
LYS CA  CB   sing N N 266 
LYS CA  HA   sing N N 267 
LYS C   O    doub N N 268 
LYS C   OXT  sing N N 269 
LYS CB  CG   sing N N 270 
LYS CB  HB2  sing N N 271 
LYS CB  HB3  sing N N 272 
LYS CG  CD   sing N N 273 
LYS CG  HG2  sing N N 274 
LYS CG  HG3  sing N N 275 
LYS CD  CE   sing N N 276 
LYS CD  HD2  sing N N 277 
LYS CD  HD3  sing N N 278 
LYS CE  NZ   sing N N 279 
LYS CE  HE2  sing N N 280 
LYS CE  HE3  sing N N 281 
LYS NZ  HZ1  sing N N 282 
LYS NZ  HZ2  sing N N 283 
LYS NZ  HZ3  sing N N 284 
LYS OXT HXT  sing N N 285 
MET N   CA   sing N N 286 
MET N   H    sing N N 287 
MET N   H2   sing N N 288 
MET CA  C    sing N N 289 
MET CA  CB   sing N N 290 
MET CA  HA   sing N N 291 
MET C   O    doub N N 292 
MET C   OXT  sing N N 293 
MET CB  CG   sing N N 294 
MET CB  HB2  sing N N 295 
MET CB  HB3  sing N N 296 
MET CG  SD   sing N N 297 
MET CG  HG2  sing N N 298 
MET CG  HG3  sing N N 299 
MET SD  CE   sing N N 300 
MET CE  HE1  sing N N 301 
MET CE  HE2  sing N N 302 
MET CE  HE3  sing N N 303 
MET OXT HXT  sing N N 304 
PEG C1  O1   sing N N 305 
PEG C1  C2   sing N N 306 
PEG C1  H11  sing N N 307 
PEG C1  H12  sing N N 308 
PEG O1  HO1  sing N N 309 
PEG C2  O2   sing N N 310 
PEG C2  H21  sing N N 311 
PEG C2  H22  sing N N 312 
PEG O2  C3   sing N N 313 
PEG C3  C4   sing N N 314 
PEG C3  H31  sing N N 315 
PEG C3  H32  sing N N 316 
PEG C4  O4   sing N N 317 
PEG C4  H41  sing N N 318 
PEG C4  H42  sing N N 319 
PEG O4  HO4  sing N N 320 
PHE N   CA   sing N N 321 
PHE N   H    sing N N 322 
PHE N   H2   sing N N 323 
PHE CA  C    sing N N 324 
PHE CA  CB   sing N N 325 
PHE CA  HA   sing N N 326 
PHE C   O    doub N N 327 
PHE C   OXT  sing N N 328 
PHE CB  CG   sing N N 329 
PHE CB  HB2  sing N N 330 
PHE CB  HB3  sing N N 331 
PHE CG  CD1  doub Y N 332 
PHE CG  CD2  sing Y N 333 
PHE CD1 CE1  sing Y N 334 
PHE CD1 HD1  sing N N 335 
PHE CD2 CE2  doub Y N 336 
PHE CD2 HD2  sing N N 337 
PHE CE1 CZ   doub Y N 338 
PHE CE1 HE1  sing N N 339 
PHE CE2 CZ   sing Y N 340 
PHE CE2 HE2  sing N N 341 
PHE CZ  HZ   sing N N 342 
PHE OXT HXT  sing N N 343 
PRO N   CA   sing N N 344 
PRO N   CD   sing N N 345 
PRO N   H    sing N N 346 
PRO CA  C    sing N N 347 
PRO CA  CB   sing N N 348 
PRO CA  HA   sing N N 349 
PRO C   O    doub N N 350 
PRO C   OXT  sing N N 351 
PRO CB  CG   sing N N 352 
PRO CB  HB2  sing N N 353 
PRO CB  HB3  sing N N 354 
PRO CG  CD   sing N N 355 
PRO CG  HG2  sing N N 356 
PRO CG  HG3  sing N N 357 
PRO CD  HD2  sing N N 358 
PRO CD  HD3  sing N N 359 
PRO OXT HXT  sing N N 360 
SER N   CA   sing N N 361 
SER N   H    sing N N 362 
SER N   H2   sing N N 363 
SER CA  C    sing N N 364 
SER CA  CB   sing N N 365 
SER CA  HA   sing N N 366 
SER C   O    doub N N 367 
SER C   OXT  sing N N 368 
SER CB  OG   sing N N 369 
SER CB  HB2  sing N N 370 
SER CB  HB3  sing N N 371 
SER OG  HG   sing N N 372 
SER OXT HXT  sing N N 373 
THR N   CA   sing N N 374 
THR N   H    sing N N 375 
THR N   H2   sing N N 376 
THR CA  C    sing N N 377 
THR CA  CB   sing N N 378 
THR CA  HA   sing N N 379 
THR C   O    doub N N 380 
THR C   OXT  sing N N 381 
THR CB  OG1  sing N N 382 
THR CB  CG2  sing N N 383 
THR CB  HB   sing N N 384 
THR OG1 HG1  sing N N 385 
THR CG2 HG21 sing N N 386 
THR CG2 HG22 sing N N 387 
THR CG2 HG23 sing N N 388 
THR OXT HXT  sing N N 389 
TRP N   CA   sing N N 390 
TRP N   H    sing N N 391 
TRP N   H2   sing N N 392 
TRP CA  C    sing N N 393 
TRP CA  CB   sing N N 394 
TRP CA  HA   sing N N 395 
TRP C   O    doub N N 396 
TRP C   OXT  sing N N 397 
TRP CB  CG   sing N N 398 
TRP CB  HB2  sing N N 399 
TRP CB  HB3  sing N N 400 
TRP CG  CD1  doub Y N 401 
TRP CG  CD2  sing Y N 402 
TRP CD1 NE1  sing Y N 403 
TRP CD1 HD1  sing N N 404 
TRP CD2 CE2  doub Y N 405 
TRP CD2 CE3  sing Y N 406 
TRP NE1 CE2  sing Y N 407 
TRP NE1 HE1  sing N N 408 
TRP CE2 CZ2  sing Y N 409 
TRP CE3 CZ3  doub Y N 410 
TRP CE3 HE3  sing N N 411 
TRP CZ2 CH2  doub Y N 412 
TRP CZ2 HZ2  sing N N 413 
TRP CZ3 CH2  sing Y N 414 
TRP CZ3 HZ3  sing N N 415 
TRP CH2 HH2  sing N N 416 
TRP OXT HXT  sing N N 417 
TYR N   CA   sing N N 418 
TYR N   H    sing N N 419 
TYR N   H2   sing N N 420 
TYR CA  C    sing N N 421 
TYR CA  CB   sing N N 422 
TYR CA  HA   sing N N 423 
TYR C   O    doub N N 424 
TYR C   OXT  sing N N 425 
TYR CB  CG   sing N N 426 
TYR CB  HB2  sing N N 427 
TYR CB  HB3  sing N N 428 
TYR CG  CD1  doub Y N 429 
TYR CG  CD2  sing Y N 430 
TYR CD1 CE1  sing Y N 431 
TYR CD1 HD1  sing N N 432 
TYR CD2 CE2  doub Y N 433 
TYR CD2 HD2  sing N N 434 
TYR CE1 CZ   doub Y N 435 
TYR CE1 HE1  sing N N 436 
TYR CE2 CZ   sing Y N 437 
TYR CE2 HE2  sing N N 438 
TYR CZ  OH   sing N N 439 
TYR OH  HH   sing N N 440 
TYR OXT HXT  sing N N 441 
VAL N   CA   sing N N 442 
VAL N   H    sing N N 443 
VAL N   H2   sing N N 444 
VAL CA  C    sing N N 445 
VAL CA  CB   sing N N 446 
VAL CA  HA   sing N N 447 
VAL C   O    doub N N 448 
VAL C   OXT  sing N N 449 
VAL CB  CG1  sing N N 450 
VAL CB  CG2  sing N N 451 
VAL CB  HB   sing N N 452 
VAL CG1 HG11 sing N N 453 
VAL CG1 HG12 sing N N 454 
VAL CG1 HG13 sing N N 455 
VAL CG2 HG21 sing N N 456 
VAL CG2 HG22 sing N N 457 
VAL CG2 HG23 sing N N 458 
VAL OXT HXT  sing N N 459 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                      ZN  
3 '2-chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' E1F 
4 'CITRIC ACID'                                                   CIT 
5 1,2-ETHANEDIOL                                                  EDO 
6 'ACETIC ACID'                                                   ACY 
7 'DI(HYDROXYETHYL)ETHER'                                         PEG 
8 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          ? 
# 
