data_7HG6
# 
_entry.id   7HG6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   7HG6         pdb_00007hg6 10.2210/pdb7hg6/pdb 
WWPDB D_1001407432 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_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             ? 
# 
_pdbx_database_status.entry_id                        7HG6 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
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 'Hepatoma-derived growth factor-related protein 2'                   10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                                        96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                       62.068    2   ? ?    ? ? 
4 non-polymer syn '2-(4-bromanylpyrazol-1-yl)-~{N}-cyclopropyl-~{N}-methyl-ethanamide' 258.115   1   ? ?    ? ? 
5 water       nat water                                                                18.015    244 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_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       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                                        SO4 
3 1,2-ETHANEDIOL                                                       EDO 
4 '2-(4-bromanylpyrazol-1-yl)-~{N}-cyclopropyl-~{N}-methyl-ethanamide' 2NU 
5 water                                                                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_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               ? 
_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                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
2NU non-polymer         . '2-(4-bromanylpyrazol-1-yl)-~{N}-cyclopropyl-~{N}-methyl-ethanamide' ?                 'C9 H12 Br N3 O' 
258.115 
ALA 'L-peptide linking' y ALANINE                                                              ?                 'C3 H7 N O2'     
89.093  
ARG 'L-peptide linking' y ARGININE                                                             ?                 'C6 H15 N4 O2 1' 
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                           ?                 'C4 H8 N2 O3'    
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                      ?                 'C4 H7 N O4'     
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                             ?                 'C3 H7 N O2 S'   
121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                                       'ETHYLENE GLYCOL' 'C2 H6 O2'       
62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                            ?                 'C5 H10 N2 O3'   
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                      ?                 'C5 H9 N O4'     
147.129 
GLY 'peptide linking'   y GLYCINE                                                              ?                 'C2 H5 N O2'     
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                            ?                 'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                                                ?                 'H2 O'           
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                           ?                 'C6 H13 N O2'    
131.173 
LEU 'L-peptide linking' y LEUCINE                                                              ?                 'C6 H13 N O2'    
131.173 
LYS 'L-peptide linking' y LYSINE                                                               ?                 'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking' y METHIONINE                                                           ?                 'C5 H11 N O2 S'  
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                        ?                 'C9 H11 N O2'    
165.189 
PRO 'L-peptide linking' y PROLINE                                                              ?                 'C5 H9 N O2'     
115.130 
SER 'L-peptide linking' y SERINE                                                               ?                 'C3 H7 N O3'     
105.093 
SO4 non-polymer         . 'SULFATE ION'                                                        ?                 'O4 S -2'        
96.063  
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 
# 
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  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 ?  ?   ?   B . n 
B 1 35 LYS 35 34 ?  ?   ?   B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 32 ALA ALA C . n 
C 1 34 VAL 34 33 33 VAL VAL C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        2NU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   2NU 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
D 2 SO4 1   101 95  SO4 SO4 A . 
E 2 SO4 1   102 96  SO4 SO4 A . 
F 3 EDO 1   103 97  EDO EDO A . 
G 2 SO4 1   104 4   SO4 SO4 A . 
H 2 SO4 1   101 1   SO4 SO4 B . 
I 2 SO4 1   102 3   SO4 SO4 B . 
J 4 2NU 1   103 101 2NU LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 307 HOH HOH A . 
M 5 HOH 2   202 202 HOH HOH A . 
M 5 HOH 3   203 84  HOH HOH A . 
M 5 HOH 4   204 66  HOH HOH A . 
M 5 HOH 5   205 342 HOH HOH A . 
M 5 HOH 6   206 304 HOH HOH A . 
M 5 HOH 7   207 139 HOH HOH A . 
M 5 HOH 8   208 335 HOH HOH A . 
M 5 HOH 9   209 95  HOH HOH A . 
M 5 HOH 10  210 55  HOH HOH A . 
M 5 HOH 11  211 91  HOH HOH A . 
M 5 HOH 12  212 71  HOH HOH A . 
M 5 HOH 13  213 26  HOH HOH A . 
M 5 HOH 14  214 94  HOH HOH A . 
M 5 HOH 15  215 167 HOH HOH A . 
M 5 HOH 16  216 37  HOH HOH A . 
M 5 HOH 17  217 34  HOH HOH A . 
M 5 HOH 18  218 293 HOH HOH A . 
M 5 HOH 19  219 86  HOH HOH A . 
M 5 HOH 20  220 28  HOH HOH A . 
M 5 HOH 21  221 97  HOH HOH A . 
M 5 HOH 22  222 111 HOH HOH A . 
M 5 HOH 23  223 203 HOH HOH A . 
M 5 HOH 24  224 208 HOH HOH A . 
M 5 HOH 25  225 8   HOH HOH A . 
M 5 HOH 26  226 87  HOH HOH A . 
M 5 HOH 27  227 32  HOH HOH A . 
M 5 HOH 28  228 78  HOH HOH A . 
M 5 HOH 29  229 23  HOH HOH A . 
M 5 HOH 30  230 41  HOH HOH A . 
M 5 HOH 31  231 12  HOH HOH A . 
M 5 HOH 32  232 21  HOH HOH A . 
M 5 HOH 33  233 7   HOH HOH A . 
M 5 HOH 34  234 199 HOH HOH A . 
M 5 HOH 35  235 260 HOH HOH A . 
M 5 HOH 36  236 267 HOH HOH A . 
M 5 HOH 37  237 288 HOH HOH A . 
M 5 HOH 38  238 290 HOH HOH A . 
M 5 HOH 39  239 27  HOH HOH A . 
M 5 HOH 40  240 60  HOH HOH A . 
M 5 HOH 41  241 1   HOH HOH A . 
M 5 HOH 42  242 289 HOH HOH A . 
M 5 HOH 43  243 93  HOH HOH A . 
M 5 HOH 44  244 179 HOH HOH A . 
M 5 HOH 45  245 143 HOH HOH A . 
M 5 HOH 46  246 188 HOH HOH A . 
M 5 HOH 47  247 42  HOH HOH A . 
M 5 HOH 48  248 274 HOH HOH A . 
M 5 HOH 49  249 2   HOH HOH A . 
M 5 HOH 50  250 300 HOH HOH A . 
M 5 HOH 51  251 58  HOH HOH A . 
M 5 HOH 52  252 18  HOH HOH A . 
M 5 HOH 53  253 77  HOH HOH A . 
M 5 HOH 54  254 73  HOH HOH A . 
M 5 HOH 55  255 190 HOH HOH A . 
M 5 HOH 56  256 292 HOH HOH A . 
M 5 HOH 57  257 115 HOH HOH A . 
M 5 HOH 58  258 14  HOH HOH A . 
M 5 HOH 59  259 47  HOH HOH A . 
M 5 HOH 60  260 99  HOH HOH A . 
M 5 HOH 61  261 297 HOH HOH A . 
M 5 HOH 62  262 20  HOH HOH A . 
M 5 HOH 63  263 109 HOH HOH A . 
M 5 HOH 64  264 259 HOH HOH A . 
M 5 HOH 65  265 278 HOH HOH A . 
M 5 HOH 66  266 145 HOH HOH A . 
M 5 HOH 67  267 113 HOH HOH A . 
M 5 HOH 68  268 64  HOH HOH A . 
M 5 HOH 69  269 222 HOH HOH A . 
M 5 HOH 70  270 164 HOH HOH A . 
M 5 HOH 71  271 16  HOH HOH A . 
M 5 HOH 72  272 218 HOH HOH A . 
M 5 HOH 73  273 301 HOH HOH A . 
M 5 HOH 74  274 327 HOH HOH A . 
M 5 HOH 75  275 9   HOH HOH A . 
M 5 HOH 76  276 19  HOH HOH A . 
M 5 HOH 77  277 38  HOH HOH A . 
M 5 HOH 78  278 116 HOH HOH A . 
M 5 HOH 79  279 211 HOH HOH A . 
M 5 HOH 80  280 131 HOH HOH A . 
M 5 HOH 81  281 318 HOH HOH A . 
M 5 HOH 82  282 281 HOH HOH A . 
M 5 HOH 83  283 152 HOH HOH A . 
M 5 HOH 84  284 63  HOH HOH A . 
M 5 HOH 85  285 22  HOH HOH A . 
M 5 HOH 86  286 165 HOH HOH A . 
M 5 HOH 87  287 31  HOH HOH A . 
M 5 HOH 88  288 210 HOH HOH A . 
M 5 HOH 89  289 296 HOH HOH A . 
M 5 HOH 90  290 270 HOH HOH A . 
M 5 HOH 91  291 205 HOH HOH A . 
M 5 HOH 92  292 83  HOH HOH A . 
M 5 HOH 93  293 185 HOH HOH A . 
M 5 HOH 94  294 219 HOH HOH A . 
M 5 HOH 95  295 75  HOH HOH A . 
M 5 HOH 96  296 35  HOH HOH A . 
M 5 HOH 97  297 57  HOH HOH A . 
M 5 HOH 98  298 332 HOH HOH A . 
M 5 HOH 99  299 283 HOH HOH A . 
M 5 HOH 100 300 156 HOH HOH A . 
N 5 HOH 1   201 247 HOH HOH B . 
N 5 HOH 2   202 72  HOH HOH B . 
N 5 HOH 3   203 272 HOH HOH B . 
N 5 HOH 4   204 331 HOH HOH B . 
N 5 HOH 5   205 329 HOH HOH B . 
N 5 HOH 6   206 69  HOH HOH B . 
N 5 HOH 7   207 89  HOH HOH B . 
N 5 HOH 8   208 334 HOH HOH B . 
N 5 HOH 9   209 242 HOH HOH B . 
N 5 HOH 10  210 168 HOH HOH B . 
N 5 HOH 11  211 336 HOH HOH B . 
N 5 HOH 12  212 320 HOH HOH B . 
N 5 HOH 13  213 98  HOH HOH B . 
N 5 HOH 14  214 224 HOH HOH B . 
N 5 HOH 15  215 258 HOH HOH B . 
N 5 HOH 16  216 137 HOH HOH B . 
N 5 HOH 17  217 123 HOH HOH B . 
N 5 HOH 18  218 17  HOH HOH B . 
N 5 HOH 19  219 172 HOH HOH B . 
N 5 HOH 20  220 54  HOH HOH B . 
N 5 HOH 21  221 249 HOH HOH B . 
N 5 HOH 22  222 150 HOH HOH B . 
N 5 HOH 23  223 175 HOH HOH B . 
N 5 HOH 24  224 280 HOH HOH B . 
N 5 HOH 25  225 68  HOH HOH B . 
N 5 HOH 26  226 6   HOH HOH B . 
N 5 HOH 27  227 153 HOH HOH B . 
N 5 HOH 28  228 10  HOH HOH B . 
N 5 HOH 29  229 177 HOH HOH B . 
N 5 HOH 30  230 223 HOH HOH B . 
N 5 HOH 31  231 117 HOH HOH B . 
N 5 HOH 32  232 5   HOH HOH B . 
N 5 HOH 33  233 170 HOH HOH B . 
N 5 HOH 34  234 24  HOH HOH B . 
N 5 HOH 35  235 96  HOH HOH B . 
N 5 HOH 36  236 315 HOH HOH B . 
N 5 HOH 37  237 25  HOH HOH B . 
N 5 HOH 38  238 169 HOH HOH B . 
N 5 HOH 39  239 119 HOH HOH B . 
N 5 HOH 40  240 261 HOH HOH B . 
N 5 HOH 41  241 217 HOH HOH B . 
N 5 HOH 42  242 101 HOH HOH B . 
N 5 HOH 43  243 316 HOH HOH B . 
N 5 HOH 44  244 319 HOH HOH B . 
N 5 HOH 45  245 214 HOH HOH B . 
N 5 HOH 46  246 59  HOH HOH B . 
N 5 HOH 47  247 157 HOH HOH B . 
N 5 HOH 48  248 61  HOH HOH B . 
N 5 HOH 49  249 79  HOH HOH B . 
N 5 HOH 50  250 215 HOH HOH B . 
N 5 HOH 51  251 333 HOH HOH B . 
N 5 HOH 52  252 182 HOH HOH B . 
N 5 HOH 53  253 74  HOH HOH B . 
N 5 HOH 54  254 36  HOH HOH B . 
N 5 HOH 55  255 120 HOH HOH B . 
N 5 HOH 56  256 344 HOH HOH B . 
N 5 HOH 57  257 46  HOH HOH B . 
N 5 HOH 58  258 13  HOH HOH B . 
N 5 HOH 59  259 279 HOH HOH B . 
N 5 HOH 60  260 197 HOH HOH B . 
N 5 HOH 61  261 339 HOH HOH B . 
N 5 HOH 62  262 104 HOH HOH B . 
N 5 HOH 63  263 322 HOH HOH B . 
N 5 HOH 64  264 44  HOH HOH B . 
N 5 HOH 65  265 345 HOH HOH B . 
N 5 HOH 66  266 303 HOH HOH B . 
N 5 HOH 67  267 76  HOH HOH B . 
N 5 HOH 68  268 163 HOH HOH B . 
N 5 HOH 69  269 201 HOH HOH B . 
N 5 HOH 70  270 160 HOH HOH B . 
N 5 HOH 71  271 314 HOH HOH B . 
N 5 HOH 72  272 312 HOH HOH B . 
N 5 HOH 73  273 107 HOH HOH B . 
O 5 HOH 1   201 323 HOH HOH C . 
O 5 HOH 2   202 321 HOH HOH C . 
O 5 HOH 3   203 343 HOH HOH C . 
O 5 HOH 4   204 254 HOH HOH C . 
O 5 HOH 5   205 118 HOH HOH C . 
O 5 HOH 6   206 294 HOH HOH C . 
O 5 HOH 7   207 338 HOH HOH C . 
O 5 HOH 8   208 325 HOH HOH C . 
O 5 HOH 9   209 271 HOH HOH C . 
O 5 HOH 10  210 302 HOH HOH C . 
O 5 HOH 11  211 142 HOH HOH C . 
O 5 HOH 12  212 173 HOH HOH C . 
O 5 HOH 13  213 148 HOH HOH C . 
O 5 HOH 14  214 189 HOH HOH C . 
O 5 HOH 15  215 90  HOH HOH C . 
O 5 HOH 16  216 284 HOH HOH C . 
O 5 HOH 17  217 134 HOH HOH C . 
O 5 HOH 18  218 317 HOH HOH C . 
O 5 HOH 19  219 269 HOH HOH C . 
O 5 HOH 20  220 209 HOH HOH C . 
O 5 HOH 21  221 85  HOH HOH C . 
O 5 HOH 22  222 49  HOH HOH C . 
O 5 HOH 23  223 15  HOH HOH C . 
O 5 HOH 24  224 67  HOH HOH C . 
O 5 HOH 25  225 132 HOH HOH C . 
O 5 HOH 26  226 326 HOH HOH C . 
O 5 HOH 27  227 198 HOH HOH C . 
O 5 HOH 28  228 161 HOH HOH C . 
O 5 HOH 29  229 82  HOH HOH C . 
O 5 HOH 30  230 130 HOH HOH C . 
O 5 HOH 31  231 45  HOH HOH C . 
O 5 HOH 32  232 184 HOH HOH C . 
O 5 HOH 33  233 309 HOH HOH C . 
O 5 HOH 34  234 126 HOH HOH C . 
O 5 HOH 35  235 4   HOH HOH C . 
O 5 HOH 36  236 53  HOH HOH C . 
O 5 HOH 37  237 43  HOH HOH C . 
O 5 HOH 38  238 102 HOH HOH C . 
O 5 HOH 39  239 275 HOH HOH C . 
O 5 HOH 40  240 48  HOH HOH C . 
O 5 HOH 41  241 299 HOH HOH C . 
O 5 HOH 42  242 62  HOH HOH C . 
O 5 HOH 43  243 40  HOH HOH C . 
O 5 HOH 44  244 122 HOH HOH C . 
O 5 HOH 45  245 135 HOH HOH C . 
O 5 HOH 46  246 56  HOH HOH C . 
O 5 HOH 47  247 287 HOH HOH C . 
O 5 HOH 48  248 171 HOH HOH C . 
O 5 HOH 49  249 151 HOH HOH C . 
O 5 HOH 50  250 328 HOH HOH C . 
O 5 HOH 51  251 340 HOH HOH C . 
O 5 HOH 52  252 298 HOH HOH C . 
O 5 HOH 53  253 305 HOH HOH C . 
O 5 HOH 54  254 65  HOH HOH C . 
O 5 HOH 55  255 291 HOH HOH C . 
O 5 HOH 56  256 70  HOH HOH C . 
O 5 HOH 57  257 149 HOH HOH C . 
O 5 HOH 58  258 146 HOH HOH C . 
O 5 HOH 59  259 241 HOH HOH C . 
O 5 HOH 60  260 330 HOH HOH C . 
O 5 HOH 61  261 324 HOH HOH C . 
O 5 HOH 62  262 246 HOH HOH C . 
O 5 HOH 63  263 337 HOH HOH C . 
O 5 HOH 64  264 108 HOH HOH C . 
O 5 HOH 65  265 103 HOH HOH C . 
O 5 HOH 66  266 341 HOH HOH C . 
O 5 HOH 67  267 92  HOH HOH C . 
O 5 HOH 68  268 313 HOH HOH C . 
O 5 HOH 69  269 206 HOH HOH C . 
O 5 HOH 70  270 310 HOH HOH C . 
O 5 HOH 71  271 125 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
4  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
5  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
6  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
7  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
8  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
9  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
10 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
11 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
12 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
13 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
14 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
15 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
16 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
17 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
18 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
19 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
20 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
21 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
22 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
23 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
24 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
25 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
26 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
27 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
28 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
29 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
30 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
31 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
32 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
33 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
34 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
35 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
36 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
37 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
38 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
39 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
40 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
41 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
42 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
43 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
44 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
45 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
46 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
47 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
48 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
49 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
50 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
51 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
52 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
53 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
54 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
55 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
56 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
57 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HG6 
_cell.length_a           41.700 
_cell.length_b           42.280 
_cell.length_c           160.440 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HG6 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.entry_id          7HG6 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.76 
_exptl_crystal.density_percent_sol   55.0 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '28% PEG MME 2000; 0.15 M ammonium sulfate; 0.1 M sodium acetate pH 4.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2021-05-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.918076 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.918076 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HG6 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             80.22 
_reflns.d_resolution_high            1.52 
_reflns.number_obs                   44734 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.065 
_reflns.pdbx_netI_over_sigmaI        11.5 
_reflns.pdbx_redundancy              6.0 
_reflns.pdbx_Rrim_I_all              0.071 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     270412 
_reflns.pdbx_chi_squared             0.94 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.52 
_reflns_shell.d_res_low                   1.56 
_reflns_shell.number_measured_all         16561 
_reflns_shell.number_unique_obs           3254 
_reflns_shell.Rmerge_I_obs                1.607 
_reflns_shell.pdbx_chi_squared            0.68 
_reflns_shell.pdbx_redundancy             5.1 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.794 
_reflns_shell.pdbx_Rpim_I_all             0.784 
_reflns_shell.pdbx_CC_half                0.344 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HG6 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     42289 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             80.22 
_refine.ls_d_res_high                            1.52 
_refine.ls_percent_reflns_obs                    99.83 
_refine.ls_R_factor_obs                          0.21379 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.21179 
_refine.ls_R_factor_R_free                       0.24926 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  2373 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.955 
_refine.B_iso_mean                               39.348 
_refine.aniso_B[1][1]                            0.28 
_refine.aniso_B[2][2]                            -0.35 
_refine.aniso_B[3][3]                            0.07 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.090 
_refine.pdbx_overall_ESU_R_Free                  0.093 
_refine.overall_SU_ML                            0.085 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.448 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_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                         1 
_refine_hist.pdbx_number_atoms_protein        2134 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_refine_hist.number_atoms_solvent             244 
_refine_hist.number_atoms_total               2430 
_refine_hist.d_res_high                       1.52 
_refine_hist.d_res_low                        80.22 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.010  0.012  ? 2289 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.961  1.829  ? 3116 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.088  5.000  ? 266  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       12.091 5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.752 10.000 ? 299  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.140  0.200  ? 287  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1902 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.503  3.693  ? 1074 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.658  6.612  ? 1337 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.654  4.007  ? 1215 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.610  50.43  ? 3458 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.520 
_refine_ls_shell.d_res_low                        1.559 
_refine_ls_shell.number_reflns_R_work             3073 
_refine_ls_shell.R_factor_R_work                  0.349 
_refine_ls_shell.percent_reflns_obs               99.78 
_refine_ls_shell.R_factor_R_free                  0.372 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             174 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HG6 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z839706072' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HG6 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
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 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
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 7HG6 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HG6 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HG6 C 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
# 
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 7HG6 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HG6 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HG6 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HG6 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HG6 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HG6 SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
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_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? 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,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_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_
_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 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
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 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-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 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
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 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HG6 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 O   C HOH 207 ? ? O C HOH 219 ? ? 1.59 
2 1 O   B HOH 224 ? ? O B HOH 263 ? ? 1.76 
3 1 O   A HOH 290 ? ? O C HOH 203 ? ? 2.03 
4 1 OD1 C ASP 9   ? ? O C HOH 201 ? ? 2.04 
5 1 O   A HOH 246 ? ? O A HOH 291 ? ? 2.10 
6 1 O   A HOH 214 ? ? O A HOH 267 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 256 ? ? 1_555 O A HOH 269 ? ? 4_545 2.01 
2 1 O A HOH 239 ? ? 1_555 O C HOH 263 ? ? 4_445 2.07 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 24 ? ? CZ A ARG 24 ? ? NH2 A ARG 24 ? ? 117.28 120.30 -3.02  0.50 N 
2 1 CG C ARG 74 ? ? CD C ARG 74 ? ? NE  C ARG 74 ? ? 91.83  111.80 -19.97 2.10 N 
3 1 NE C ARG 74 ? ? CZ C ARG 74 ? ? NH1 C ARG 74 ? ? 113.07 120.30 -7.23  0.50 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 ASN A 87 ? ? -153.44 66.29  
2 1 PRO B 7  ? ? -38.87  125.60 
3 1 ASN B 38 ? ? 78.47   -2.31  
4 1 ASN B 87 ? ? -158.23 62.12  
5 1 ASN C 87 ? ? -145.98 53.48  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.39 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.153 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 B VAL 33 ? B VAL 34 
8  1 Y 1 B LYS 34 ? B LYS 35 
9  1 Y 1 C GLY 0  ? C GLY 1  
10 1 Y 1 C MET 1  ? C MET 2  
11 1 Y 1 C PRO 2  ? C PRO 3  
12 1 Y 1 C ALA 29 ? C ALA 30 
13 1 Y 1 C ASP 30 ? C ASP 31 
14 1 Y 1 C GLY 31 ? C GLY 32 
15 1 Y 1 C SER 93 ? C SER 94 
# 
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 
2NU C1   C  N N 1   
2NU C2   C  N N 2   
2NU C3   C  N N 3   
2NU C4   C  Y N 4   
2NU C5   C  Y N 5   
2NU C6   C  Y N 6   
2NU C7   C  N N 7   
2NU C8   C  N N 8   
2NU C9   C  N N 9   
2NU N1   N  N N 10  
2NU N2   N  Y N 11  
2NU N3   N  Y N 12  
2NU O1   O  N N 13  
2NU BR1  BR N N 14  
2NU H2   H  N N 15  
2NU H3   H  N N 16  
2NU H1   H  N N 17  
2NU H5   H  N N 18  
2NU H4   H  N N 19  
2NU H6   H  N N 20  
2NU H7   H  N N 21  
2NU H8   H  N N 22  
2NU H10  H  N N 23  
2NU H9   H  N N 24  
2NU H12  H  N N 25  
2NU H11  H  N N 26  
ALA N    N  N N 27  
ALA CA   C  N S 28  
ALA C    C  N N 29  
ALA O    O  N N 30  
ALA CB   C  N N 31  
ALA OXT  O  N N 32  
ALA H    H  N N 33  
ALA H2   H  N N 34  
ALA HA   H  N N 35  
ALA HB1  H  N N 36  
ALA HB2  H  N N 37  
ALA HB3  H  N N 38  
ALA HXT  H  N N 39  
ARG N    N  N N 40  
ARG CA   C  N S 41  
ARG C    C  N N 42  
ARG O    O  N N 43  
ARG CB   C  N N 44  
ARG CG   C  N N 45  
ARG CD   C  N N 46  
ARG NE   N  N N 47  
ARG CZ   C  N N 48  
ARG NH1  N  N N 49  
ARG NH2  N  N N 50  
ARG OXT  O  N N 51  
ARG H    H  N N 52  
ARG H2   H  N N 53  
ARG HA   H  N N 54  
ARG HB2  H  N N 55  
ARG HB3  H  N N 56  
ARG HG2  H  N N 57  
ARG HG3  H  N N 58  
ARG HD2  H  N N 59  
ARG HD3  H  N N 60  
ARG HE   H  N N 61  
ARG HH11 H  N N 62  
ARG HH12 H  N N 63  
ARG HH21 H  N N 64  
ARG HH22 H  N N 65  
ARG HXT  H  N N 66  
ASN N    N  N N 67  
ASN CA   C  N S 68  
ASN C    C  N N 69  
ASN O    O  N N 70  
ASN CB   C  N N 71  
ASN CG   C  N N 72  
ASN OD1  O  N N 73  
ASN ND2  N  N N 74  
ASN OXT  O  N N 75  
ASN H    H  N N 76  
ASN H2   H  N N 77  
ASN HA   H  N N 78  
ASN HB2  H  N N 79  
ASN HB3  H  N N 80  
ASN HD21 H  N N 81  
ASN HD22 H  N N 82  
ASN HXT  H  N N 83  
ASP N    N  N N 84  
ASP CA   C  N S 85  
ASP C    C  N N 86  
ASP O    O  N N 87  
ASP CB   C  N N 88  
ASP CG   C  N N 89  
ASP OD1  O  N N 90  
ASP OD2  O  N N 91  
ASP OXT  O  N N 92  
ASP H    H  N N 93  
ASP H2   H  N N 94  
ASP HA   H  N N 95  
ASP HB2  H  N N 96  
ASP HB3  H  N N 97  
ASP HD2  H  N N 98  
ASP HXT  H  N N 99  
CYS N    N  N N 100 
CYS CA   C  N R 101 
CYS C    C  N N 102 
CYS O    O  N N 103 
CYS CB   C  N N 104 
CYS SG   S  N N 105 
CYS OXT  O  N N 106 
CYS H    H  N N 107 
CYS H2   H  N N 108 
CYS HA   H  N N 109 
CYS HB2  H  N N 110 
CYS HB3  H  N N 111 
CYS HG   H  N N 112 
CYS HXT  H  N N 113 
EDO C1   C  N N 114 
EDO O1   O  N N 115 
EDO C2   C  N N 116 
EDO O2   O  N N 117 
EDO H11  H  N N 118 
EDO H12  H  N N 119 
EDO HO1  H  N N 120 
EDO H21  H  N N 121 
EDO H22  H  N N 122 
EDO HO2  H  N N 123 
GLN N    N  N N 124 
GLN CA   C  N S 125 
GLN C    C  N N 126 
GLN O    O  N N 127 
GLN CB   C  N N 128 
GLN CG   C  N N 129 
GLN CD   C  N N 130 
GLN OE1  O  N N 131 
GLN NE2  N  N N 132 
GLN OXT  O  N N 133 
GLN H    H  N N 134 
GLN H2   H  N N 135 
GLN HA   H  N N 136 
GLN HB2  H  N N 137 
GLN HB3  H  N N 138 
GLN HG2  H  N N 139 
GLN HG3  H  N N 140 
GLN HE21 H  N N 141 
GLN HE22 H  N N 142 
GLN HXT  H  N N 143 
GLU N    N  N N 144 
GLU CA   C  N S 145 
GLU C    C  N N 146 
GLU O    O  N N 147 
GLU CB   C  N N 148 
GLU CG   C  N N 149 
GLU CD   C  N N 150 
GLU OE1  O  N N 151 
GLU OE2  O  N N 152 
GLU OXT  O  N N 153 
GLU H    H  N N 154 
GLU H2   H  N N 155 
GLU HA   H  N N 156 
GLU HB2  H  N N 157 
GLU HB3  H  N N 158 
GLU HG2  H  N N 159 
GLU HG3  H  N N 160 
GLU HE2  H  N N 161 
GLU HXT  H  N N 162 
GLY N    N  N N 163 
GLY CA   C  N N 164 
GLY C    C  N N 165 
GLY O    O  N N 166 
GLY OXT  O  N N 167 
GLY H    H  N N 168 
GLY H2   H  N N 169 
GLY HA2  H  N N 170 
GLY HA3  H  N N 171 
GLY HXT  H  N N 172 
HIS N    N  N N 173 
HIS CA   C  N S 174 
HIS C    C  N N 175 
HIS O    O  N N 176 
HIS CB   C  N N 177 
HIS CG   C  Y N 178 
HIS ND1  N  Y N 179 
HIS CD2  C  Y N 180 
HIS CE1  C  Y N 181 
HIS NE2  N  Y N 182 
HIS OXT  O  N N 183 
HIS H    H  N N 184 
HIS H2   H  N N 185 
HIS HA   H  N N 186 
HIS HB2  H  N N 187 
HIS HB3  H  N N 188 
HIS HD1  H  N N 189 
HIS HD2  H  N N 190 
HIS HE1  H  N N 191 
HIS HE2  H  N N 192 
HIS HXT  H  N N 193 
HOH O    O  N N 194 
HOH H1   H  N N 195 
HOH H2   H  N N 196 
ILE N    N  N N 197 
ILE CA   C  N S 198 
ILE C    C  N N 199 
ILE O    O  N N 200 
ILE CB   C  N S 201 
ILE CG1  C  N N 202 
ILE CG2  C  N N 203 
ILE CD1  C  N N 204 
ILE OXT  O  N N 205 
ILE H    H  N N 206 
ILE H2   H  N N 207 
ILE HA   H  N N 208 
ILE HB   H  N N 209 
ILE HG12 H  N N 210 
ILE HG13 H  N N 211 
ILE HG21 H  N N 212 
ILE HG22 H  N N 213 
ILE HG23 H  N N 214 
ILE HD11 H  N N 215 
ILE HD12 H  N N 216 
ILE HD13 H  N N 217 
ILE HXT  H  N N 218 
LEU N    N  N N 219 
LEU CA   C  N S 220 
LEU C    C  N N 221 
LEU O    O  N N 222 
LEU CB   C  N N 223 
LEU CG   C  N N 224 
LEU CD1  C  N N 225 
LEU CD2  C  N N 226 
LEU OXT  O  N N 227 
LEU H    H  N N 228 
LEU H2   H  N N 229 
LEU HA   H  N N 230 
LEU HB2  H  N N 231 
LEU HB3  H  N N 232 
LEU HG   H  N N 233 
LEU HD11 H  N N 234 
LEU HD12 H  N N 235 
LEU HD13 H  N N 236 
LEU HD21 H  N N 237 
LEU HD22 H  N N 238 
LEU HD23 H  N N 239 
LEU HXT  H  N N 240 
LYS N    N  N N 241 
LYS CA   C  N S 242 
LYS C    C  N N 243 
LYS O    O  N N 244 
LYS CB   C  N N 245 
LYS CG   C  N N 246 
LYS CD   C  N N 247 
LYS CE   C  N N 248 
LYS NZ   N  N N 249 
LYS OXT  O  N N 250 
LYS H    H  N N 251 
LYS H2   H  N N 252 
LYS HA   H  N N 253 
LYS HB2  H  N N 254 
LYS HB3  H  N N 255 
LYS HG2  H  N N 256 
LYS HG3  H  N N 257 
LYS HD2  H  N N 258 
LYS HD3  H  N N 259 
LYS HE2  H  N N 260 
LYS HE3  H  N N 261 
LYS HZ1  H  N N 262 
LYS HZ2  H  N N 263 
LYS HZ3  H  N N 264 
LYS HXT  H  N N 265 
MET N    N  N N 266 
MET CA   C  N S 267 
MET C    C  N N 268 
MET O    O  N N 269 
MET CB   C  N N 270 
MET CG   C  N N 271 
MET SD   S  N N 272 
MET CE   C  N N 273 
MET OXT  O  N N 274 
MET H    H  N N 275 
MET H2   H  N N 276 
MET HA   H  N N 277 
MET HB2  H  N N 278 
MET HB3  H  N N 279 
MET HG2  H  N N 280 
MET HG3  H  N N 281 
MET HE1  H  N N 282 
MET HE2  H  N N 283 
MET HE3  H  N N 284 
MET HXT  H  N N 285 
PHE N    N  N N 286 
PHE CA   C  N S 287 
PHE C    C  N N 288 
PHE O    O  N N 289 
PHE CB   C  N N 290 
PHE CG   C  Y N 291 
PHE CD1  C  Y N 292 
PHE CD2  C  Y N 293 
PHE CE1  C  Y N 294 
PHE CE2  C  Y N 295 
PHE CZ   C  Y N 296 
PHE OXT  O  N N 297 
PHE H    H  N N 298 
PHE H2   H  N N 299 
PHE HA   H  N N 300 
PHE HB2  H  N N 301 
PHE HB3  H  N N 302 
PHE HD1  H  N N 303 
PHE HD2  H  N N 304 
PHE HE1  H  N N 305 
PHE HE2  H  N N 306 
PHE HZ   H  N N 307 
PHE HXT  H  N N 308 
PRO N    N  N N 309 
PRO CA   C  N S 310 
PRO C    C  N N 311 
PRO O    O  N N 312 
PRO CB   C  N N 313 
PRO CG   C  N N 314 
PRO CD   C  N N 315 
PRO OXT  O  N N 316 
PRO H    H  N N 317 
PRO HA   H  N N 318 
PRO HB2  H  N N 319 
PRO HB3  H  N N 320 
PRO HG2  H  N N 321 
PRO HG3  H  N N 322 
PRO HD2  H  N N 323 
PRO HD3  H  N N 324 
PRO HXT  H  N N 325 
SER N    N  N N 326 
SER CA   C  N S 327 
SER C    C  N N 328 
SER O    O  N N 329 
SER CB   C  N N 330 
SER OG   O  N N 331 
SER OXT  O  N N 332 
SER H    H  N N 333 
SER H2   H  N N 334 
SER HA   H  N N 335 
SER HB2  H  N N 336 
SER HB3  H  N N 337 
SER HG   H  N N 338 
SER HXT  H  N N 339 
SO4 S    S  N N 340 
SO4 O1   O  N N 341 
SO4 O2   O  N N 342 
SO4 O3   O  N N 343 
SO4 O4   O  N N 344 
THR N    N  N N 345 
THR CA   C  N S 346 
THR C    C  N N 347 
THR O    O  N N 348 
THR CB   C  N R 349 
THR OG1  O  N N 350 
THR CG2  C  N N 351 
THR OXT  O  N N 352 
THR H    H  N N 353 
THR H2   H  N N 354 
THR HA   H  N N 355 
THR HB   H  N N 356 
THR HG1  H  N N 357 
THR HG21 H  N N 358 
THR HG22 H  N N 359 
THR HG23 H  N N 360 
THR HXT  H  N N 361 
TRP N    N  N N 362 
TRP CA   C  N S 363 
TRP C    C  N N 364 
TRP O    O  N N 365 
TRP CB   C  N N 366 
TRP CG   C  Y N 367 
TRP CD1  C  Y N 368 
TRP CD2  C  Y N 369 
TRP NE1  N  Y N 370 
TRP CE2  C  Y N 371 
TRP CE3  C  Y N 372 
TRP CZ2  C  Y N 373 
TRP CZ3  C  Y N 374 
TRP CH2  C  Y N 375 
TRP OXT  O  N N 376 
TRP H    H  N N 377 
TRP H2   H  N N 378 
TRP HA   H  N N 379 
TRP HB2  H  N N 380 
TRP HB3  H  N N 381 
TRP HD1  H  N N 382 
TRP HE1  H  N N 383 
TRP HE3  H  N N 384 
TRP HZ2  H  N N 385 
TRP HZ3  H  N N 386 
TRP HH2  H  N N 387 
TRP HXT  H  N N 388 
TYR N    N  N N 389 
TYR CA   C  N S 390 
TYR C    C  N N 391 
TYR O    O  N N 392 
TYR CB   C  N N 393 
TYR CG   C  Y N 394 
TYR CD1  C  Y N 395 
TYR CD2  C  Y N 396 
TYR CE1  C  Y N 397 
TYR CE2  C  Y N 398 
TYR CZ   C  Y N 399 
TYR OH   O  N N 400 
TYR OXT  O  N N 401 
TYR H    H  N N 402 
TYR H2   H  N N 403 
TYR HA   H  N N 404 
TYR HB2  H  N N 405 
TYR HB3  H  N N 406 
TYR HD1  H  N N 407 
TYR HD2  H  N N 408 
TYR HE1  H  N N 409 
TYR HE2  H  N N 410 
TYR HH   H  N N 411 
TYR HXT  H  N N 412 
VAL N    N  N N 413 
VAL CA   C  N S 414 
VAL C    C  N N 415 
VAL O    O  N N 416 
VAL CB   C  N N 417 
VAL CG1  C  N N 418 
VAL CG2  C  N N 419 
VAL OXT  O  N N 420 
VAL H    H  N N 421 
VAL H2   H  N N 422 
VAL HA   H  N N 423 
VAL HB   H  N N 424 
VAL HG11 H  N N 425 
VAL HG12 H  N N 426 
VAL HG13 H  N N 427 
VAL HG21 H  N N 428 
VAL HG22 H  N N 429 
VAL HG23 H  N N 430 
VAL HXT  H  N N 431 
# 
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 
2NU BR1 C5   sing N N 1   
2NU C5  C6   sing Y N 2   
2NU C5  C4   doub Y N 3   
2NU C6  N3   doub Y N 4   
2NU C4  N2   sing Y N 5   
2NU N3  N2   sing Y N 6   
2NU N2  C3   sing N N 7   
2NU C9  C8   sing N N 8   
2NU C9  C7   sing N N 9   
2NU C8  C7   sing N N 10  
2NU C1  N1   sing N N 11  
2NU C7  N1   sing N N 12  
2NU C3  C2   sing N N 13  
2NU N1  C2   sing N N 14  
2NU C2  O1   doub N N 15  
2NU C1  H2   sing N N 16  
2NU C1  H3   sing N N 17  
2NU C1  H1   sing N N 18  
2NU C3  H5   sing N N 19  
2NU C3  H4   sing N N 20  
2NU C4  H6   sing N N 21  
2NU C6  H7   sing N N 22  
2NU C7  H8   sing N N 23  
2NU C8  H10  sing N N 24  
2NU C8  H9   sing N N 25  
2NU C9  H12  sing N N 26  
2NU C9  H11  sing N N 27  
ALA N   CA   sing N N 28  
ALA N   H    sing N N 29  
ALA N   H2   sing N N 30  
ALA CA  C    sing N N 31  
ALA CA  CB   sing N N 32  
ALA CA  HA   sing N N 33  
ALA C   O    doub N N 34  
ALA C   OXT  sing N N 35  
ALA CB  HB1  sing N N 36  
ALA CB  HB2  sing N N 37  
ALA CB  HB3  sing N N 38  
ALA OXT HXT  sing N N 39  
ARG N   CA   sing N N 40  
ARG N   H    sing N N 41  
ARG N   H2   sing N N 42  
ARG CA  C    sing N N 43  
ARG CA  CB   sing N N 44  
ARG CA  HA   sing N N 45  
ARG C   O    doub N N 46  
ARG C   OXT  sing N N 47  
ARG CB  CG   sing N N 48  
ARG CB  HB2  sing N N 49  
ARG CB  HB3  sing N N 50  
ARG CG  CD   sing N N 51  
ARG CG  HG2  sing N N 52  
ARG CG  HG3  sing N N 53  
ARG CD  NE   sing N N 54  
ARG CD  HD2  sing N N 55  
ARG CD  HD3  sing N N 56  
ARG NE  CZ   sing N N 57  
ARG NE  HE   sing N N 58  
ARG CZ  NH1  sing N N 59  
ARG CZ  NH2  doub N N 60  
ARG NH1 HH11 sing N N 61  
ARG NH1 HH12 sing N N 62  
ARG NH2 HH21 sing N N 63  
ARG NH2 HH22 sing N N 64  
ARG OXT HXT  sing N N 65  
ASN N   CA   sing N N 66  
ASN N   H    sing N N 67  
ASN N   H2   sing N N 68  
ASN CA  C    sing N N 69  
ASN CA  CB   sing N N 70  
ASN CA  HA   sing N N 71  
ASN C   O    doub N N 72  
ASN C   OXT  sing N N 73  
ASN CB  CG   sing N N 74  
ASN CB  HB2  sing N N 75  
ASN CB  HB3  sing N N 76  
ASN CG  OD1  doub N N 77  
ASN CG  ND2  sing N N 78  
ASN ND2 HD21 sing N N 79  
ASN ND2 HD22 sing N N 80  
ASN OXT HXT  sing N N 81  
ASP N   CA   sing N N 82  
ASP N   H    sing N N 83  
ASP N   H2   sing N N 84  
ASP CA  C    sing N N 85  
ASP CA  CB   sing N N 86  
ASP CA  HA   sing N N 87  
ASP C   O    doub N N 88  
ASP C   OXT  sing N N 89  
ASP CB  CG   sing N N 90  
ASP CB  HB2  sing N N 91  
ASP CB  HB3  sing N N 92  
ASP CG  OD1  doub N N 93  
ASP CG  OD2  sing N N 94  
ASP OD2 HD2  sing N N 95  
ASP OXT HXT  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 
EDO C1  O1   sing N N 110 
EDO C1  C2   sing N N 111 
EDO C1  H11  sing N N 112 
EDO C1  H12  sing N N 113 
EDO O1  HO1  sing N N 114 
EDO C2  O2   sing N N 115 
EDO C2  H21  sing N N 116 
EDO C2  H22  sing N N 117 
EDO O2  HO2  sing N N 118 
GLN N   CA   sing N N 119 
GLN N   H    sing N N 120 
GLN N   H2   sing N N 121 
GLN CA  C    sing N N 122 
GLN CA  CB   sing N N 123 
GLN CA  HA   sing N N 124 
GLN C   O    doub N N 125 
GLN C   OXT  sing N N 126 
GLN CB  CG   sing N N 127 
GLN CB  HB2  sing N N 128 
GLN CB  HB3  sing N N 129 
GLN CG  CD   sing N N 130 
GLN CG  HG2  sing N N 131 
GLN CG  HG3  sing N N 132 
GLN CD  OE1  doub N N 133 
GLN CD  NE2  sing N N 134 
GLN NE2 HE21 sing N N 135 
GLN NE2 HE22 sing N N 136 
GLN OXT HXT  sing N N 137 
GLU N   CA   sing N N 138 
GLU N   H    sing N N 139 
GLU N   H2   sing N N 140 
GLU CA  C    sing N N 141 
GLU CA  CB   sing N N 142 
GLU CA  HA   sing N N 143 
GLU C   O    doub N N 144 
GLU C   OXT  sing N N 145 
GLU CB  CG   sing N N 146 
GLU CB  HB2  sing N N 147 
GLU CB  HB3  sing N N 148 
GLU CG  CD   sing N N 149 
GLU CG  HG2  sing N N 150 
GLU CG  HG3  sing N N 151 
GLU CD  OE1  doub N N 152 
GLU CD  OE2  sing N N 153 
GLU OE2 HE2  sing N N 154 
GLU OXT HXT  sing N N 155 
GLY N   CA   sing N N 156 
GLY N   H    sing N N 157 
GLY N   H2   sing N N 158 
GLY CA  C    sing N N 159 
GLY CA  HA2  sing N N 160 
GLY CA  HA3  sing N N 161 
GLY C   O    doub N N 162 
GLY C   OXT  sing N N 163 
GLY OXT HXT  sing N N 164 
HIS N   CA   sing N N 165 
HIS N   H    sing N N 166 
HIS N   H2   sing N N 167 
HIS CA  C    sing N N 168 
HIS CA  CB   sing N N 169 
HIS CA  HA   sing N N 170 
HIS C   O    doub N N 171 
HIS C   OXT  sing N N 172 
HIS CB  CG   sing N N 173 
HIS CB  HB2  sing N N 174 
HIS CB  HB3  sing N N 175 
HIS CG  ND1  sing Y N 176 
HIS CG  CD2  doub Y N 177 
HIS ND1 CE1  doub Y N 178 
HIS ND1 HD1  sing N N 179 
HIS CD2 NE2  sing Y N 180 
HIS CD2 HD2  sing N N 181 
HIS CE1 NE2  sing Y N 182 
HIS CE1 HE1  sing N N 183 
HIS NE2 HE2  sing N N 184 
HIS OXT HXT  sing N N 185 
HOH O   H1   sing N N 186 
HOH O   H2   sing N N 187 
ILE N   CA   sing N N 188 
ILE N   H    sing N N 189 
ILE N   H2   sing N N 190 
ILE CA  C    sing N N 191 
ILE CA  CB   sing N N 192 
ILE CA  HA   sing N N 193 
ILE C   O    doub N N 194 
ILE C   OXT  sing N N 195 
ILE CB  CG1  sing N N 196 
ILE CB  CG2  sing N N 197 
ILE CB  HB   sing N N 198 
ILE CG1 CD1  sing N N 199 
ILE CG1 HG12 sing N N 200 
ILE CG1 HG13 sing N N 201 
ILE CG2 HG21 sing N N 202 
ILE CG2 HG22 sing N N 203 
ILE CG2 HG23 sing N N 204 
ILE CD1 HD11 sing N N 205 
ILE CD1 HD12 sing N N 206 
ILE CD1 HD13 sing N N 207 
ILE OXT HXT  sing N N 208 
LEU N   CA   sing N N 209 
LEU N   H    sing N N 210 
LEU N   H2   sing N N 211 
LEU CA  C    sing N N 212 
LEU CA  CB   sing N N 213 
LEU CA  HA   sing N N 214 
LEU C   O    doub N N 215 
LEU C   OXT  sing N N 216 
LEU CB  CG   sing N N 217 
LEU CB  HB2  sing N N 218 
LEU CB  HB3  sing N N 219 
LEU CG  CD1  sing N N 220 
LEU CG  CD2  sing N N 221 
LEU CG  HG   sing N N 222 
LEU CD1 HD11 sing N N 223 
LEU CD1 HD12 sing N N 224 
LEU CD1 HD13 sing N N 225 
LEU CD2 HD21 sing N N 226 
LEU CD2 HD22 sing N N 227 
LEU CD2 HD23 sing N N 228 
LEU OXT HXT  sing N N 229 
LYS N   CA   sing N N 230 
LYS N   H    sing N N 231 
LYS N   H2   sing N N 232 
LYS CA  C    sing N N 233 
LYS CA  CB   sing N N 234 
LYS CA  HA   sing N N 235 
LYS C   O    doub N N 236 
LYS C   OXT  sing N N 237 
LYS CB  CG   sing N N 238 
LYS CB  HB2  sing N N 239 
LYS CB  HB3  sing N N 240 
LYS CG  CD   sing N N 241 
LYS CG  HG2  sing N N 242 
LYS CG  HG3  sing N N 243 
LYS CD  CE   sing N N 244 
LYS CD  HD2  sing N N 245 
LYS CD  HD3  sing N N 246 
LYS CE  NZ   sing N N 247 
LYS CE  HE2  sing N N 248 
LYS CE  HE3  sing N N 249 
LYS NZ  HZ1  sing N N 250 
LYS NZ  HZ2  sing N N 251 
LYS NZ  HZ3  sing N N 252 
LYS OXT HXT  sing N N 253 
MET N   CA   sing N N 254 
MET N   H    sing N N 255 
MET N   H2   sing N N 256 
MET CA  C    sing N N 257 
MET CA  CB   sing N N 258 
MET CA  HA   sing N N 259 
MET C   O    doub N N 260 
MET C   OXT  sing N N 261 
MET CB  CG   sing N N 262 
MET CB  HB2  sing N N 263 
MET CB  HB3  sing N N 264 
MET CG  SD   sing N N 265 
MET CG  HG2  sing N N 266 
MET CG  HG3  sing N N 267 
MET SD  CE   sing N N 268 
MET CE  HE1  sing N N 269 
MET CE  HE2  sing N N 270 
MET CE  HE3  sing N N 271 
MET OXT HXT  sing N N 272 
PHE N   CA   sing N N 273 
PHE N   H    sing N N 274 
PHE N   H2   sing N N 275 
PHE CA  C    sing N N 276 
PHE CA  CB   sing N N 277 
PHE CA  HA   sing N N 278 
PHE C   O    doub N N 279 
PHE C   OXT  sing N N 280 
PHE CB  CG   sing N N 281 
PHE CB  HB2  sing N N 282 
PHE CB  HB3  sing N N 283 
PHE CG  CD1  doub Y N 284 
PHE CG  CD2  sing Y N 285 
PHE CD1 CE1  sing Y N 286 
PHE CD1 HD1  sing N N 287 
PHE CD2 CE2  doub Y N 288 
PHE CD2 HD2  sing N N 289 
PHE CE1 CZ   doub Y N 290 
PHE CE1 HE1  sing N N 291 
PHE CE2 CZ   sing Y N 292 
PHE CE2 HE2  sing N N 293 
PHE CZ  HZ   sing N N 294 
PHE OXT HXT  sing N N 295 
PRO N   CA   sing N N 296 
PRO N   CD   sing N N 297 
PRO N   H    sing N N 298 
PRO CA  C    sing N N 299 
PRO CA  CB   sing N N 300 
PRO CA  HA   sing N N 301 
PRO C   O    doub N N 302 
PRO C   OXT  sing N N 303 
PRO CB  CG   sing N N 304 
PRO CB  HB2  sing N N 305 
PRO CB  HB3  sing N N 306 
PRO CG  CD   sing N N 307 
PRO CG  HG2  sing N N 308 
PRO CG  HG3  sing N N 309 
PRO CD  HD2  sing N N 310 
PRO CD  HD3  sing N N 311 
PRO OXT HXT  sing N N 312 
SER N   CA   sing N N 313 
SER N   H    sing N N 314 
SER N   H2   sing N N 315 
SER CA  C    sing N N 316 
SER CA  CB   sing N N 317 
SER CA  HA   sing N N 318 
SER C   O    doub N N 319 
SER C   OXT  sing N N 320 
SER CB  OG   sing N N 321 
SER CB  HB2  sing N N 322 
SER CB  HB3  sing N N 323 
SER OG  HG   sing N N 324 
SER OXT HXT  sing N N 325 
SO4 S   O1   doub N N 326 
SO4 S   O2   doub N N 327 
SO4 S   O3   sing N N 328 
SO4 S   O4   sing N N 329 
THR N   CA   sing N N 330 
THR N   H    sing N N 331 
THR N   H2   sing N N 332 
THR CA  C    sing N N 333 
THR CA  CB   sing N N 334 
THR CA  HA   sing N N 335 
THR C   O    doub N N 336 
THR C   OXT  sing N N 337 
THR CB  OG1  sing N N 338 
THR CB  CG2  sing N N 339 
THR CB  HB   sing N N 340 
THR OG1 HG1  sing N N 341 
THR CG2 HG21 sing N N 342 
THR CG2 HG22 sing N N 343 
THR CG2 HG23 sing N N 344 
THR OXT HXT  sing N N 345 
TRP N   CA   sing N N 346 
TRP N   H    sing N N 347 
TRP N   H2   sing N N 348 
TRP CA  C    sing N N 349 
TRP CA  CB   sing N N 350 
TRP CA  HA   sing N N 351 
TRP C   O    doub N N 352 
TRP C   OXT  sing N N 353 
TRP CB  CG   sing N N 354 
TRP CB  HB2  sing N N 355 
TRP CB  HB3  sing N N 356 
TRP CG  CD1  doub Y N 357 
TRP CG  CD2  sing Y N 358 
TRP CD1 NE1  sing Y N 359 
TRP CD1 HD1  sing N N 360 
TRP CD2 CE2  doub Y N 361 
TRP CD2 CE3  sing Y N 362 
TRP NE1 CE2  sing Y N 363 
TRP NE1 HE1  sing N N 364 
TRP CE2 CZ2  sing Y N 365 
TRP CE3 CZ3  doub Y N 366 
TRP CE3 HE3  sing N N 367 
TRP CZ2 CH2  doub Y N 368 
TRP CZ2 HZ2  sing N N 369 
TRP CZ3 CH2  sing Y N 370 
TRP CZ3 HZ3  sing N N 371 
TRP CH2 HH2  sing N N 372 
TRP OXT HXT  sing N N 373 
TYR N   CA   sing N N 374 
TYR N   H    sing N N 375 
TYR N   H2   sing N N 376 
TYR CA  C    sing N N 377 
TYR CA  CB   sing N N 378 
TYR CA  HA   sing N N 379 
TYR C   O    doub N N 380 
TYR C   OXT  sing N N 381 
TYR CB  CG   sing N N 382 
TYR CB  HB2  sing N N 383 
TYR CB  HB3  sing N N 384 
TYR CG  CD1  doub Y N 385 
TYR CG  CD2  sing Y N 386 
TYR CD1 CE1  sing Y N 387 
TYR CD1 HD1  sing N N 388 
TYR CD2 CE2  doub Y N 389 
TYR CD2 HD2  sing N N 390 
TYR CE1 CZ   doub Y N 391 
TYR CE1 HE1  sing N N 392 
TYR CE2 CZ   sing Y N 393 
TYR CE2 HE2  sing N N 394 
TYR CZ  OH   sing N N 395 
TYR OH  HH   sing N N 396 
TYR OXT HXT  sing N N 397 
VAL N   CA   sing N N 398 
VAL N   H    sing N N 399 
VAL N   H2   sing N N 400 
VAL CA  C    sing N N 401 
VAL CA  CB   sing N N 402 
VAL CA  HA   sing N N 403 
VAL C   O    doub N N 404 
VAL C   OXT  sing N N 405 
VAL CB  CG1  sing N N 406 
VAL CB  CG2  sing N N 407 
VAL CB  HB   sing N N 408 
VAL CG1 HG11 sing N N 409 
VAL CG1 HG12 sing N N 410 
VAL CG1 HG13 sing N N 411 
VAL CG2 HG21 sing N N 412 
VAL CG2 HG22 sing N N 413 
VAL CG2 HG23 sing N N 414 
VAL OXT HXT  sing N N 415 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium 1SC9822N 1 
'Research Foundation - Flanders (FWO)' Belgium 1SC9824N 2 
'Research Foundation - Flanders (FWO)' Belgium G053822N 3 
# 
_pdbx_deposit_group.group_id            G_1002305 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_description   
'Fragment screening against HRP-2 PWWP domain at the XChem facility of Diamond Light Source' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HG6 
_atom_sites.fract_transf_matrix[1][1]   0.023981 
_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]   0.023652 
_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]   0.006233 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
BR 
C  
N  
O  
S  
# 
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   . MET A 1 2  ? 1.337   4.278   2.354   1.00 50.12  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 2  ? 0.239   3.510   1.704   1.00 53.47  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 2  ? 0.806   2.435   0.775   1.00 50.93  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 2  ? 1.922   2.544   0.257   1.00 49.92  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 2  ? -0.740  4.429   0.961   1.00 60.56  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 2  ? -1.742  5.137   1.866   1.00 74.26  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 2  ? -3.118  4.214   2.597   1.00 82.83  ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 2  ? -3.519  5.308   3.969   1.00 70.90  ? 1   MET A CE  1 
ATOM   9    N  N   . PRO A 1 3  ? 0.073   1.318   0.580   1.00 39.14  ? 2   PRO A N   1 
ATOM   10   C  CA  . PRO A 1 3  ? 0.535   0.220   -0.272  1.00 38.79  ? 2   PRO A CA  1 
ATOM   11   C  C   . PRO A 1 3  ? 0.671   0.530   -1.758  1.00 39.49  ? 2   PRO A C   1 
ATOM   12   O  O   . PRO A 1 3  ? -0.058  1.315   -2.343  1.00 40.41  ? 2   PRO A O   1 
ATOM   13   C  CB  . PRO A 1 3  ? -0.595  -0.843  -0.009  1.00 40.49  ? 2   PRO A CB  1 
ATOM   14   C  CG  . PRO A 1 3  ? -1.100  -0.480  1.383   1.00 43.97  ? 2   PRO A CG  1 
ATOM   15   C  CD  . PRO A 1 3  ? -1.223  1.029   1.232   1.00 41.88  ? 2   PRO A CD  1 
ATOM   16   N  N   . HIS A 1 4  ? 1.637   -0.122  -2.389  1.00 37.55  ? 3   HIS A N   1 
ATOM   17   C  CA  . HIS A 1 4  ? 1.820   0.016   -3.821  1.00 38.76  ? 3   HIS A CA  1 
ATOM   18   C  C   . HIS A 1 4  ? 1.283   -1.276  -4.421  1.00 33.41  ? 3   HIS A C   1 
ATOM   19   O  O   . HIS A 1 4  ? 0.823   -2.145  -3.680  1.00 35.95  ? 3   HIS A O   1 
ATOM   20   C  CB  . HIS A 1 4  ? 3.317   0.201   -4.117  1.00 49.40  ? 3   HIS A CB  1 
ATOM   21   C  CG  . HIS A 1 4  ? 3.872   1.507   -3.627  1.00 58.65  ? 3   HIS A CG  1 
ATOM   22   N  ND1 . HIS A 1 4  ? 4.058   1.806   -2.292  1.00 63.24  ? 3   HIS A ND1 1 
ATOM   23   C  CD2 . HIS A 1 4  ? 4.235   2.610   -4.302  1.00 63.97  ? 3   HIS A CD2 1 
ATOM   24   C  CE1 . HIS A 1 4  ? 4.523   3.045   -2.180  1.00 65.87  ? 3   HIS A CE1 1 
ATOM   25   N  NE2 . HIS A 1 4  ? 4.643   3.551   -3.391  1.00 58.79  ? 3   HIS A NE2 1 
ATOM   26   N  N   . ALA A 1 5  ? 1.315   -1.431  -5.745  1.00 31.04  ? 4   ALA A N   1 
ATOM   27   C  CA  . ALA A 1 5  ? 1.068   -2.741  -6.344  1.00 31.13  ? 4   ALA A CA  1 
ATOM   28   C  C   . ALA A 1 5  ? 2.205   -3.692  -5.985  1.00 28.11  ? 4   ALA A C   1 
ATOM   29   O  O   . ALA A 1 5  ? 3.294   -3.223  -5.613  1.00 30.50  ? 4   ALA A O   1 
ATOM   30   C  CB  . ALA A 1 5  ? 0.975   -2.598  -7.853  1.00 39.03  ? 4   ALA A CB  1 
ATOM   31   N  N   . PHE A 1 6  ? 1.936   -4.989  -6.122  1.00 26.50  ? 5   PHE A N   1 
ATOM   32   C  CA  . PHE A 1 6  ? 2.957   -6.024  -5.935  1.00 27.07  ? 5   PHE A CA  1 
ATOM   33   C  C   . PHE A 1 6  ? 4.103   -5.792  -6.931  1.00 29.16  ? 5   PHE A C   1 
ATOM   34   O  O   . PHE A 1 6  ? 3.868   -5.356  -8.067  1.00 31.06  ? 5   PHE A O   1 
ATOM   35   C  CB  . PHE A 1 6  ? 2.412   -7.455  -6.001  1.00 28.27  ? 5   PHE A CB  1 
ATOM   36   C  CG  . PHE A 1 6  ? 1.590   -7.780  -4.753  1.00 27.59  ? 5   PHE A CG  1 
ATOM   37   C  CD1 . PHE A 1 6  ? 2.243   -8.006  -3.549  1.00 25.68  ? 5   PHE A CD1 1 
ATOM   38   C  CD2 . PHE A 1 6  ? 0.198   -7.920  -4.806  1.00 29.80  ? 5   PHE A CD2 1 
ATOM   39   C  CE1 . PHE A 1 6  ? 1.582   -8.319  -2.372  1.00 26.46  ? 5   PHE A CE1 1 
ATOM   40   C  CE2 . PHE A 1 6  ? -0.472  -8.298  -3.632  1.00 25.91  ? 5   PHE A CE2 1 
ATOM   41   C  CZ  . PHE A 1 6  ? 0.204   -8.452  -2.434  1.00 27.37  ? 5   PHE A CZ  1 
ATOM   42   N  N   . LYS A 1 7  ? 5.330   -6.090  -6.477  1.00 26.11  ? 6   LYS A N   1 
ATOM   43   C  CA  . LYS A 1 7  ? 6.510   -5.973  -7.347  1.00 27.17  ? 6   LYS A CA  1 
ATOM   44   C  C   . LYS A 1 7  ? 7.420   -7.178  -7.057  1.00 25.69  ? 6   LYS A C   1 
ATOM   45   O  O   . LYS A 1 7  ? 7.385   -7.763  -5.970  1.00 23.53  ? 6   LYS A O   1 
ATOM   46   C  CB  . LYS A 1 7  ? 7.193   -4.639  -7.005  1.00 27.10  ? 6   LYS A CB  1 
ATOM   47   C  CG  . LYS A 1 7  ? 7.810   -4.550  -5.641  1.00 30.70  ? 6   LYS A CG  1 
ATOM   48   C  CD  . LYS A 1 7  ? 8.566   -3.234  -5.399  1.00 40.51  ? 6   LYS A CD  1 
ATOM   49   C  CE  . LYS A 1 7  ? 9.175   -3.239  -4.018  1.00 38.33  ? 6   LYS A CE  1 
ATOM   50   N  NZ  . LYS A 1 7  ? 8.122   -3.173  -2.989  1.00 39.44  ? 6   LYS A NZ  1 
ATOM   51   N  N   . PRO A 1 8  ? 8.322   -7.573  -7.972  1.00 25.97  ? 7   PRO A N   1 
ATOM   52   C  CA  . PRO A 1 8  ? 9.251   -8.664  -7.694  1.00 24.15  ? 7   PRO A CA  1 
ATOM   53   C  C   . PRO A 1 8  ? 10.033  -8.373  -6.425  1.00 23.60  ? 7   PRO A C   1 
ATOM   54   O  O   . PRO A 1 8  ? 10.498  -7.239  -6.237  1.00 26.80  ? 7   PRO A O   1 
ATOM   55   C  CB  . PRO A 1 8  ? 10.150  -8.613  -8.995  1.00 28.32  ? 7   PRO A CB  1 
ATOM   56   C  CG  . PRO A 1 8  ? 9.186   -8.111  -10.049 1.00 28.89  ? 7   PRO A CG  1 
ATOM   57   C  CD  . PRO A 1 8  ? 8.452   -6.998  -9.339  1.00 27.00  ? 7   PRO A CD  1 
ATOM   58   N  N   . GLY A 1 9  ? 10.223  -9.433  -5.623  1.00 22.24  ? 8   GLY A N   1 
ATOM   59   C  CA  . GLY A 1 9  ? 10.945  -9.384  -4.363  1.00 23.40  ? 8   GLY A CA  1 
ATOM   60   C  C   . GLY A 1 9  ? 10.001  -9.245  -3.179  1.00 23.38  ? 8   GLY A C   1 
ATOM   61   O  O   . GLY A 1 9  ? 10.373  -9.513  -2.032  1.00 22.52  ? 8   GLY A O   1 
ATOM   62   N  N   . ASP A 1 10 ? 8.758   -8.819  -3.436  1.00 22.90  ? 9   ASP A N   1 
ATOM   63   C  CA  . ASP A 1 10 ? 7.844   -8.777  -2.296  1.00 20.68  ? 9   ASP A CA  1 
ATOM   64   C  C   . ASP A 1 10 ? 7.569   -10.163 -1.715  1.00 19.93  ? 9   ASP A C   1 
ATOM   65   O  O   . ASP A 1 10 ? 7.450   -11.166 -2.396  1.00 20.42  ? 9   ASP A O   1 
ATOM   66   C  CB  . ASP A 1 10 ? 6.506   -8.151  -2.704  1.00 19.84  ? 9   ASP A CB  1 
ATOM   67   C  CG  . ASP A 1 10 ? 6.503   -6.659  -2.916  1.00 23.79  ? 9   ASP A CG  1 
ATOM   68   O  OD1 . ASP A 1 10 ? 7.435   -5.953  -2.431  1.00 29.24  ? 9   ASP A OD1 1 
ATOM   69   O  OD2 . ASP A 1 10 ? 5.536   -6.199  -3.564  1.00 25.73  ? 9   ASP A OD2 1 
ATOM   70   N  N   . LEU A 1 11 ? 7.436   -10.216 -0.355  1.00 21.25  ? 10  LEU A N   1 
ATOM   71   C  CA  . LEU A 1 11 ? 7.278   -11.446 0.404   1.00 18.47  ? 10  LEU A CA  1 
ATOM   72   C  C   . LEU A 1 11 ? 5.814   -11.555 0.834   1.00 18.53  ? 10  LEU A C   1 
ATOM   73   O  O   . LEU A 1 11 ? 5.241   -10.518 1.236   1.00 23.70  ? 10  LEU A O   1 
ATOM   74   C  CB  . LEU A 1 11 ? 8.231   -11.447 1.613   1.00 21.52  ? 10  LEU A CB  1 
ATOM   75   C  CG  . LEU A 1 11 ? 9.708   -11.253 1.212   1.00 20.63  ? 10  LEU A CG  1 
ATOM   76   C  CD1 . LEU A 1 11 ? 10.538  -11.380 2.534   1.00 25.07  ? 10  LEU A CD1 1 
ATOM   77   C  CD2 . LEU A 1 11 ? 10.164  -12.268 0.215   1.00 22.33  ? 10  LEU A CD2 1 
ATOM   78   N  N   . VAL A 1 12 ? 5.271   -12.768 0.685   1.00 19.84  ? 11  VAL A N   1 
ATOM   79   C  CA  . VAL A 1 12 ? 3.812   -12.955 0.926   1.00 23.16  ? 11  VAL A CA  1 
ATOM   80   C  C   . VAL A 1 12 ? 3.578   -14.311 1.572   1.00 21.97  ? 11  VAL A C   1 
ATOM   81   O  O   . VAL A 1 12 ? 4.428   -15.189 1.604   1.00 21.44  ? 11  VAL A O   1 
ATOM   82   C  CB  . VAL A 1 12 ? 2.986   -12.862 -0.386  1.00 21.69  ? 11  VAL A CB  1 
ATOM   83   C  CG1 . VAL A 1 12 ? 3.145   -11.496 -1.038  1.00 23.73  ? 11  VAL A CG1 1 
ATOM   84   C  CG2 . VAL A 1 12 ? 3.410   -13.904 -1.425  1.00 23.02  ? 11  VAL A CG2 1 
ATOM   85   N  N   . PHE A 1 13 ? 2.320   -14.546 2.038   1.00 20.73  ? 12  PHE A N   1 
ATOM   86   C  CA  . PHE A 1 13 ? 1.767   -15.886 2.035   1.00 22.52  ? 12  PHE A CA  1 
ATOM   87   C  C   . PHE A 1 13 ? 0.807   -15.940 0.848   1.00 23.56  ? 12  PHE A C   1 
ATOM   88   O  O   . PHE A 1 13 ? 0.022   -14.996 0.663   1.00 23.18  ? 12  PHE A O   1 
ATOM   89   C  CB  . PHE A 1 13 ? 1.002   -16.227 3.336   1.00 23.04  ? 12  PHE A CB  1 
ATOM   90   C  CG  . PHE A 1 13 ? 1.941   -16.315 4.522   1.00 22.74  ? 12  PHE A CG  1 
ATOM   91   C  CD1 . PHE A 1 13 ? 2.294   -15.148 5.187   1.00 24.20  ? 12  PHE A CD1 1 
ATOM   92   C  CD2 . PHE A 1 13 ? 2.464   -17.552 4.917   1.00 25.88  ? 12  PHE A CD2 1 
ATOM   93   C  CE1 . PHE A 1 13 ? 3.207   -15.228 6.236   1.00 30.75  ? 12  PHE A CE1 1 
ATOM   94   C  CE2 . PHE A 1 13 ? 3.360   -17.630 6.005   1.00 24.73  ? 12  PHE A CE2 1 
ATOM   95   C  CZ  . PHE A 1 13 ? 3.714   -16.463 6.625   1.00 27.11  ? 12  PHE A CZ  1 
ATOM   96   N  N   . ALA A 1 14 ? 0.910   -17.031 0.090   1.00 23.31  ? 13  ALA A N   1 
ATOM   97   C  CA  . ALA A 1 14 ? 0.113   -17.181 -1.119  1.00 23.08  ? 13  ALA A CA  1 
ATOM   98   C  C   . ALA A 1 14 ? -0.854  -18.346 -0.901  1.00 27.09  ? 13  ALA A C   1 
ATOM   99   O  O   . ALA A 1 14 ? -0.464  -19.403 -0.391  1.00 25.07  ? 13  ALA A O   1 
ATOM   100  C  CB  . ALA A 1 14 ? 1.023   -17.378 -2.330  1.00 24.61  ? 13  ALA A CB  1 
ATOM   101  N  N   . LYS A 1 15 ? -2.138  -18.137 -1.300  1.00 24.56  ? 14  LYS A N   1 
ATOM   102  C  CA  . LYS A 1 15 ? -3.156  -19.162 -1.095  1.00 26.21  ? 14  LYS A CA  1 
ATOM   103  C  C   . LYS A 1 15 ? -3.508  -19.836 -2.413  1.00 27.60  ? 14  LYS A C   1 
ATOM   104  O  O   . LYS A 1 15 ? -3.833  -19.171 -3.387  1.00 29.58  ? 14  LYS A O   1 
ATOM   105  C  CB  . LYS A 1 15 ? -4.391  -18.466 -0.494  1.00 27.02  ? 14  LYS A CB  1 
ATOM   106  C  CG  . LYS A 1 15 ? -5.539  -19.437 -0.019  1.00 31.50  ? 14  LYS A CG  1 
ATOM   107  C  CD  . LYS A 1 15 ? -5.090  -20.376 1.106   1.00 32.95  ? 14  LYS A CD  1 
ATOM   108  C  CE  . LYS A 1 15 ? -6.181  -21.188 1.770   1.00 33.81  ? 14  LYS A CE  1 
ATOM   109  N  NZ  . LYS A 1 15 ? -6.496  -22.349 0.933   1.00 35.10  ? 14  LYS A NZ  1 
ATOM   110  N  N   . MET A 1 16 ? -3.500  -21.173 -2.352  1.00 30.43  ? 15  MET A N   1 
ATOM   111  C  CA  . MET A 1 16 ? -4.140  -21.952 -3.394  1.00 34.79  ? 15  MET A CA  1 
ATOM   112  C  C   . MET A 1 16 ? -5.072  -22.979 -2.771  1.00 37.23  ? 15  MET A C   1 
ATOM   113  O  O   . MET A 1 16 ? -4.886  -23.378 -1.638  1.00 31.69  ? 15  MET A O   1 
ATOM   114  C  CB  . MET A 1 16 ? -3.112  -22.743 -4.175  1.00 38.40  ? 15  MET A CB  1 
ATOM   115  C  CG  . MET A 1 16 ? -3.182  -22.258 -5.592  1.00 55.11  ? 15  MET A CG  1 
ATOM   116  S  SD  . MET A 1 16 ? -1.476  -21.813 -5.902  1.00 40.45  ? 15  MET A SD  1 
ATOM   117  C  CE  . MET A 1 16 ? -1.054  -23.382 -6.613  1.00 37.47  ? 15  MET A CE  1 
ATOM   118  N  N   . LYS A 1 17 ? -6.012  -23.429 -3.599  1.00 42.21  ? 16  LYS A N   1 
ATOM   119  C  CA  . LYS A 1 17 ? -7.016  -24.413 -3.219  1.00 45.49  ? 16  LYS A CA  1 
ATOM   120  C  C   . LYS A 1 17 ? -6.347  -25.653 -2.639  1.00 38.81  ? 16  LYS A C   1 
ATOM   121  O  O   . LYS A 1 17 ? -5.410  -26.193 -3.218  1.00 40.21  ? 16  LYS A O   1 
ATOM   122  C  CB  . LYS A 1 17 ? -7.704  -24.799 -4.533  1.00 47.68  ? 16  LYS A CB  1 
ATOM   123  C  CG  . LYS A 1 17 ? -8.996  -25.596 -4.339  1.00 52.85  ? 16  LYS A CG  1 
ATOM   124  C  CD  . LYS A 1 17 ? -10.035 -24.732 -3.625  1.00 55.58  ? 16  LYS A CD  1 
ATOM   125  N  N   . GLY A 1 18 ? -6.822  -26.088 -1.459  1.00 41.12  ? 17  GLY A N   1 
ATOM   126  C  CA  . GLY A 1 18 ? -6.413  -27.353 -0.891  1.00 41.46  ? 17  GLY A CA  1 
ATOM   127  C  C   . GLY A 1 18 ? -5.112  -27.205 -0.123  1.00 45.56  ? 17  GLY A C   1 
ATOM   128  O  O   . GLY A 1 18 ? -4.599  -28.175 0.423   1.00 45.29  ? 17  GLY A O   1 
ATOM   129  N  N   . TYR A 1 19 ? -4.577  -25.973 -0.090  1.00 39.88  ? 18  TYR A N   1 
ATOM   130  C  CA  . TYR A 1 19 ? -3.324  -25.788 0.607   1.00 36.79  ? 18  TYR A CA  1 
ATOM   131  C  C   . TYR A 1 19 ? -3.446  -24.676 1.630   1.00 31.56  ? 18  TYR A C   1 
ATOM   132  O  O   . TYR A 1 19 ? -4.205  -23.736 1.463   1.00 30.57  ? 18  TYR A O   1 
ATOM   133  C  CB  . TYR A 1 19 ? -2.250  -25.365 -0.397  1.00 42.20  ? 18  TYR A CB  1 
ATOM   134  C  CG  . TYR A 1 19 ? -1.685  -26.435 -1.317  1.00 42.74  ? 18  TYR A CG  1 
ATOM   135  C  CD1 . TYR A 1 19 ? -0.551  -27.149 -0.951  1.00 53.78  ? 18  TYR A CD1 1 
ATOM   136  C  CD2 . TYR A 1 19 ? -2.237  -26.666 -2.573  1.00 46.99  ? 18  TYR A CD2 1 
ATOM   137  C  CE1 . TYR A 1 19 ? -0.015  -28.113 -1.792  1.00 58.33  ? 18  TYR A CE1 1 
ATOM   138  C  CE2 . TYR A 1 19 ? -1.703  -27.621 -3.432  1.00 48.01  ? 18  TYR A CE2 1 
ATOM   139  C  CZ  . TYR A 1 19 ? -0.580  -28.338 -3.038  1.00 55.20  ? 18  TYR A CZ  1 
ATOM   140  O  OH  . TYR A 1 19 ? -0.025  -29.298 -3.852  1.00 57.84  ? 18  TYR A OH  1 
ATOM   141  N  N   . PRO A 1 20 ? -2.655  -24.739 2.720   1.00 32.98  ? 19  PRO A N   1 
ATOM   142  C  CA  . PRO A 1 20 ? -2.593  -23.657 3.700   1.00 31.95  ? 19  PRO A CA  1 
ATOM   143  C  C   . PRO A 1 20 ? -1.879  -22.454 3.056   1.00 27.94  ? 19  PRO A C   1 
ATOM   144  O  O   . PRO A 1 20 ? -1.120  -22.679 2.136   1.00 30.91  ? 19  PRO A O   1 
ATOM   145  C  CB  . PRO A 1 20 ? -1.775  -24.309 4.838   1.00 36.33  ? 19  PRO A CB  1 
ATOM   146  C  CG  . PRO A 1 20 ? -0.932  -25.377 4.166   1.00 35.23  ? 19  PRO A CG  1 
ATOM   147  C  CD  . PRO A 1 20 ? -1.773  -25.889 3.018   1.00 37.55  ? 19  PRO A CD  1 
ATOM   148  N  N   . HIS A 1 21 ? -2.207  -21.242 3.478   1.00 28.49  ? 20  HIS A N   1 
ATOM   149  C  CA  . HIS A 1 21 ? -1.487  -20.018 3.129   1.00 24.96  ? 20  HIS A CA  1 
ATOM   150  C  C   . HIS A 1 21 ? 0.018   -20.329 3.231   1.00 26.73  ? 20  HIS A C   1 
ATOM   151  O  O   . HIS A 1 21 ? 0.502   -20.726 4.288   1.00 27.89  ? 20  HIS A O   1 
ATOM   152  C  CB  . HIS A 1 21 ? -1.966  -18.878 4.048   1.00 26.58  ? 20  HIS A CB  1 
ATOM   153  C  CG  . HIS A 1 21 ? -3.394  -18.430 3.803   1.00 28.00  ? 20  HIS A CG  1 
ATOM   154  N  ND1 . HIS A 1 21 ? -4.436  -19.115 4.416   1.00 32.83  ? 20  HIS A ND1 1 
ATOM   155  C  CD2 . HIS A 1 21 ? -3.945  -17.437 3.075   1.00 29.32  ? 20  HIS A CD2 1 
ATOM   156  C  CE1 . HIS A 1 21 ? -5.588  -18.541 4.071   1.00 31.71  ? 20  HIS A CE1 1 
ATOM   157  N  NE2 . HIS A 1 21 ? -5.353  -17.523 3.262   1.00 30.39  ? 20  HIS A NE2 1 
ATOM   158  N  N   . TRP A 1 22 ? 0.769   -20.094 2.128   1.00 26.68  ? 21  TRP A N   1 
ATOM   159  C  CA  . TRP A 1 22 ? 2.097   -20.687 2.021   1.00 24.59  ? 21  TRP A CA  1 
ATOM   160  C  C   . TRP A 1 22 ? 3.172   -19.599 1.866   1.00 22.86  ? 21  TRP A C   1 
ATOM   161  O  O   . TRP A 1 22 ? 3.020   -18.693 1.069   1.00 24.11  ? 21  TRP A O   1 
ATOM   162  C  CB  . TRP A 1 22 ? 2.115   -21.599 0.795   1.00 27.01  ? 21  TRP A CB  1 
ATOM   163  C  CG  . TRP A 1 22 ? 3.251   -22.584 0.818   1.00 26.86  ? 21  TRP A CG  1 
ATOM   164  C  CD1 . TRP A 1 22 ? 4.596   -22.390 0.593   1.00 26.72  ? 21  TRP A CD1 1 
ATOM   165  C  CD2 . TRP A 1 22 ? 3.074   -23.978 1.120   1.00 29.56  ? 21  TRP A CD2 1 
ATOM   166  N  NE1 . TRP A 1 22 ? 5.257   -23.606 0.696   1.00 26.73  ? 21  TRP A NE1 1 
ATOM   167  C  CE2 . TRP A 1 22 ? 4.347   -24.583 1.040   1.00 27.29  ? 21  TRP A CE2 1 
ATOM   168  C  CE3 . TRP A 1 22 ? 1.960   -24.762 1.453   1.00 34.95  ? 21  TRP A CE3 1 
ATOM   169  C  CZ2 . TRP A 1 22 ? 4.538   -25.953 1.277   1.00 36.25  ? 21  TRP A CZ2 1 
ATOM   170  C  CZ3 . TRP A 1 22 ? 2.150   -26.118 1.674   1.00 37.14  ? 21  TRP A CZ3 1 
ATOM   171  C  CH2 . TRP A 1 22 ? 3.429   -26.705 1.603   1.00 35.71  ? 21  TRP A CH2 1 
ATOM   172  N  N   . PRO A 1 23 ? 4.328   -19.660 2.588   1.00 24.09  ? 22  PRO A N   1 
ATOM   173  C  CA  . PRO A 1 23 ? 5.371   -18.644 2.395   1.00 22.30  ? 22  PRO A CA  1 
ATOM   174  C  C   . PRO A 1 23 ? 5.884   -18.620 0.946   1.00 20.86  ? 22  PRO A C   1 
ATOM   175  O  O   . PRO A 1 23 ? 6.200   -19.662 0.377   1.00 23.66  ? 22  PRO A O   1 
ATOM   176  C  CB  . PRO A 1 23 ? 6.446   -19.121 3.399   1.00 21.70  ? 22  PRO A CB  1 
ATOM   177  C  CG  . PRO A 1 23 ? 6.240   -20.612 3.564   1.00 22.57  ? 22  PRO A CG  1 
ATOM   178  C  CD  . PRO A 1 23 ? 4.696   -20.722 3.541   1.00 24.44  ? 22  PRO A CD  1 
ATOM   179  N  N   . ALA A 1 24 ? 5.961   -17.401 0.400   1.00 19.62  ? 23  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 24 ? 6.303   -17.269 -1.021  1.00 19.61  ? 23  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 24 ? 6.843   -15.880 -1.316  1.00 19.54  ? 23  ALA A C   1 
ATOM   182  O  O   . ALA A 1 24 ? 6.824   -14.986 -0.481  1.00 21.35  ? 23  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 24 ? 5.057   -17.547 -1.884  1.00 22.08  ? 23  ALA A CB  1 
ATOM   184  N  N   . ARG A 1 25 ? 7.363   -15.702 -2.554  1.00 18.95  ? 24  ARG A N   1 
ATOM   185  C  CA  . ARG A 1 25 ? 7.720   -14.370 -3.006  1.00 18.26  ? 24  ARG A CA  1 
ATOM   186  C  C   . ARG A 1 25 ? 7.185   -14.108 -4.421  1.00 18.67  ? 24  ARG A C   1 
ATOM   187  O  O   . ARG A 1 25 ? 6.921   -15.072 -5.155  1.00 22.42  ? 24  ARG A O   1 
ATOM   188  C  CB  . ARG A 1 25 ? 9.255   -14.206 -2.944  1.00 21.44  ? 24  ARG A CB  1 
ATOM   189  C  CG  . ARG A 1 25 ? 9.988   -15.117 -3.927  1.00 23.72  ? 24  ARG A CG  1 
ATOM   190  C  CD  . ARG A 1 25 ? 11.526  -14.954 -3.770  1.00 22.47  ? 24  ARG A CD  1 
ATOM   191  N  NE  . ARG A 1 25 ? 12.209  -15.719 -4.858  1.00 23.56  ? 24  ARG A NE  1 
ATOM   192  C  CZ  . ARG A 1 25 ? 13.472  -16.120 -4.731  1.00 27.26  ? 24  ARG A CZ  1 
ATOM   193  N  NH1 . ARG A 1 25 ? 14.135  -15.991 -3.576  1.00 26.01  ? 24  ARG A NH1 1 
ATOM   194  N  NH2 . ARG A 1 25 ? 14.028  -16.708 -5.774  1.00 27.33  ? 24  ARG A NH2 1 
ATOM   195  N  N   . ILE A 1 26 ? 7.030   -12.843 -4.754  1.00 21.28  ? 25  ILE A N   1 
ATOM   196  C  CA  . ILE A 1 26 ? 6.840   -12.450 -6.157  1.00 19.99  ? 25  ILE A CA  1 
ATOM   197  C  C   . ILE A 1 26 ? 8.175   -12.592 -6.868  1.00 24.52  ? 25  ILE A C   1 
ATOM   198  O  O   . ILE A 1 26 ? 9.131   -11.929 -6.471  1.00 24.88  ? 25  ILE A O   1 
ATOM   199  C  CB  . ILE A 1 26 ? 6.369   -10.992 -6.212  1.00 22.07  ? 25  ILE A CB  1 
ATOM   200  C  CG1 . ILE A 1 26 ? 5.188   -10.709 -5.243  1.00 26.87  ? 25  ILE A CG1 1 
ATOM   201  C  CG2 . ILE A 1 26 ? 5.965   -10.642 -7.668  1.00 22.66  ? 25  ILE A CG2 1 
ATOM   202  C  CD1 . ILE A 1 26 ? 3.887   -11.376 -5.617  1.00 34.27  ? 25  ILE A CD1 1 
ATOM   203  N  N   . ASP A 1 27 ? 8.201   -13.395 -7.935  1.00 25.20  ? 26  ASP A N   1 
ATOM   204  C  CA  . ASP A 1 27 ? 9.462   -13.526 -8.686  1.00 24.28  ? 26  ASP A CA  1 
ATOM   205  C  C   . ASP A 1 27 ? 9.555   -12.515 -9.831  1.00 28.93  ? 26  ASP A C   1 
ATOM   206  O  O   . ASP A 1 27 ? 8.581   -11.906 -10.247 1.00 27.64  ? 26  ASP A O   1 
ATOM   207  C  CB  . ASP A 1 27 ? 9.571   -14.924 -9.247  1.00 26.04  ? 26  ASP A CB  1 
ATOM   208  C  CG  . ASP A 1 27 ? 10.534  -15.876 -8.562  1.00 29.13  ? 26  ASP A CG  1 
ATOM   209  O  OD1 . ASP A 1 27 ? 11.111  -15.511 -7.501  1.00 33.59  ? 26  ASP A OD1 1 
ATOM   210  O  OD2 . ASP A 1 27 ? 10.686  -16.986 -9.041  1.00 28.89  ? 26  ASP A OD2 1 
ATOM   211  N  N   . ASP A 1 28 ? 10.792  -12.323 -10.351 1.00 30.36  ? 27  ASP A N   1 
ATOM   212  C  CA  . ASP A 1 28 ? 10.998  -11.674 -11.629 1.00 36.78  ? 27  ASP A CA  1 
ATOM   213  C  C   . ASP A 1 28 ? 10.680  -12.683 -12.733 1.00 31.81  ? 27  ASP A C   1 
ATOM   214  O  O   . ASP A 1 28 ? 10.581  -13.877 -12.502 1.00 32.54  ? 27  ASP A O   1 
ATOM   215  C  CB  . ASP A 1 28 ? 12.470  -11.292 -11.764 1.00 41.67  ? 27  ASP A CB  1 
ATOM   216  C  CG  . ASP A 1 28 ? 12.963  -10.092 -10.954 1.00 50.65  ? 27  ASP A CG  1 
ATOM   217  O  OD1 . ASP A 1 28 ? 12.638  -8.943  -11.330 1.00 53.69  ? 27  ASP A OD1 1 
ATOM   218  O  OD2 . ASP A 1 28 ? 13.694  -10.314 -9.958  1.00 55.30  ? 27  ASP A OD2 1 
ATOM   219  N  N   . ILE A 1 29 ? 10.556  -12.192 -13.963 1.00 35.53  ? 28  ILE A N   1 
ATOM   220  C  CA  . ILE A 1 29 ? 10.541  -13.093 -15.117 1.00 32.50  ? 28  ILE A CA  1 
ATOM   221  C  C   . ILE A 1 29 ? 11.869  -12.825 -15.836 1.00 32.43  ? 28  ILE A C   1 
ATOM   222  O  O   . ILE A 1 29 ? 12.161  -11.675 -16.120 1.00 33.36  ? 28  ILE A O   1 
ATOM   223  C  CB  . ILE A 1 29 ? 9.346   -12.680 -15.988 1.00 36.68  ? 28  ILE A CB  1 
ATOM   224  C  CG1 . ILE A 1 29 ? 8.036   -12.823 -15.204 1.00 38.23  ? 28  ILE A CG1 1 
ATOM   225  C  CG2 . ILE A 1 29 ? 9.289   -13.468 -17.298 1.00 33.78  ? 28  ILE A CG2 1 
ATOM   226  C  CD1 . ILE A 1 29 ? 7.006   -11.829 -15.675 1.00 40.38  ? 28  ILE A CD1 1 
ATOM   227  N  N   . ALA A 1 30 ? 12.676  -13.877 -16.011 1.00 34.93  ? 29  ALA A N   1 
ATOM   228  C  CA  . ALA A 1 30 ? 13.958  -13.804 -16.706 1.00 32.55  ? 29  ALA A CA  1 
ATOM   229  C  C   . ALA A 1 30 ? 13.704  -13.413 -18.164 1.00 34.04  ? 29  ALA A C   1 
ATOM   230  O  O   . ALA A 1 30 ? 12.682  -13.767 -18.750 1.00 33.87  ? 29  ALA A O   1 
ATOM   231  C  CB  . ALA A 1 30 ? 14.615  -15.173 -16.626 1.00 34.87  ? 29  ALA A CB  1 
ATOM   232  N  N   . ASP A 1 31 ? 14.644  -12.658 -18.755 1.00 32.97  ? 30  ASP A N   1 
ATOM   233  C  CA  . ASP A 1 31 ? 14.664  -12.500 -20.217 1.00 32.07  ? 30  ASP A CA  1 
ATOM   234  C  C   . ASP A 1 31 ? 14.501  -13.860 -20.875 1.00 29.72  ? 30  ASP A C   1 
ATOM   235  O  O   . ASP A 1 31 ? 15.162  -14.813 -20.502 1.00 34.65  ? 30  ASP A O   1 
ATOM   236  C  CB  . ASP A 1 31 ? 15.943  -11.792 -20.652 1.00 31.32  ? 30  ASP A CB  1 
ATOM   237  C  CG  . ASP A 1 31 ? 15.984  -10.294 -20.425 1.00 38.09  ? 30  ASP A CG  1 
ATOM   238  O  OD1 . ASP A 1 31 ? 14.905  -9.705  -20.284 1.00 42.99  ? 30  ASP A OD1 1 
ATOM   239  O  OD2 . ASP A 1 31 ? 17.124  -9.735  -20.389 1.00 40.55  ? 30  ASP A OD2 1 
ATOM   240  N  N   . GLY A 1 32 ? 13.577  -13.948 -21.836 1.00 31.48  ? 31  GLY A N   1 
ATOM   241  C  CA  . GLY A 1 32 ? 13.381  -15.156 -22.616 1.00 31.47  ? 31  GLY A CA  1 
ATOM   242  C  C   . GLY A 1 32 ? 12.450  -16.196 -22.002 1.00 35.38  ? 31  GLY A C   1 
ATOM   243  O  O   . GLY A 1 32 ? 12.191  -17.216 -22.626 1.00 38.43  ? 31  GLY A O   1 
ATOM   244  N  N   . ALA A 1 33 ? 12.063  -16.011 -20.732 1.00 35.69  ? 32  ALA A N   1 
ATOM   245  C  CA  . ALA A 1 33 ? 11.241  -17.026 -20.089 1.00 34.35  ? 32  ALA A CA  1 
ATOM   246  C  C   . ALA A 1 33 ? 9.749   -16.724 -20.265 1.00 30.56  ? 32  ALA A C   1 
ATOM   247  O  O   . ALA A 1 33 ? 9.320   -15.624 -20.619 1.00 32.37  ? 32  ALA A O   1 
ATOM   248  C  CB  . ALA A 1 33 ? 11.618  -17.110 -18.625 1.00 34.44  ? 32  ALA A CB  1 
ATOM   249  N  N   . VAL A 1 34 ? 8.945   -17.774 -19.992 1.00 34.01  ? 33  VAL A N   1 
ATOM   250  C  CA  . VAL A 1 34 ? 7.494   -17.716 -20.146 1.00 37.99  ? 33  VAL A CA  1 
ATOM   251  C  C   . VAL A 1 34 ? 6.887   -16.701 -19.175 1.00 36.90  ? 33  VAL A C   1 
ATOM   252  O  O   . VAL A 1 34 ? 7.168   -16.768 -17.983 1.00 38.59  ? 33  VAL A O   1 
ATOM   253  C  CB  . VAL A 1 34 ? 7.001   -19.140 -19.811 1.00 39.52  ? 33  VAL A CB  1 
ATOM   254  C  CG1 . VAL A 1 34 ? 5.485   -19.193 -19.657 1.00 40.01  ? 33  VAL A CG1 1 
ATOM   255  C  CG2 . VAL A 1 34 ? 7.471   -20.147 -20.871 1.00 37.01  ? 33  VAL A CG2 1 
ATOM   256  N  N   . LYS A 1 35 ? 6.022   -15.818 -19.694 1.00 38.87  ? 34  LYS A N   1 
ATOM   257  C  CA  . LYS A 1 35 ? 5.401   -14.755 -18.910 1.00 35.78  ? 34  LYS A CA  1 
ATOM   258  C  C   . LYS A 1 35 ? 4.099   -15.277 -18.304 1.00 40.95  ? 34  LYS A C   1 
ATOM   259  O  O   . LYS A 1 35 ? 3.529   -16.238 -18.800 1.00 38.35  ? 34  LYS A O   1 
ATOM   260  C  CB  . LYS A 1 35 ? 5.092   -13.510 -19.743 1.00 39.26  ? 34  LYS A CB  1 
ATOM   261  C  CG  . LYS A 1 35 ? 6.318   -12.832 -20.367 1.00 42.33  ? 34  LYS A CG  1 
ATOM   262  C  CD  . LYS A 1 35 ? 6.080   -11.571 -21.191 1.00 49.32  ? 34  LYS A CD  1 
ATOM   263  C  CE  . LYS A 1 35 ? 5.565   -11.930 -22.559 1.00 46.80  ? 34  LYS A CE  1 
ATOM   264  N  NZ  . LYS A 1 35 ? 5.426   -10.738 -23.387 1.00 47.40  ? 34  LYS A NZ  1 
ATOM   265  N  N   . PRO A 1 36 ? 3.573   -14.654 -17.225 1.00 43.40  ? 35  PRO A N   1 
ATOM   266  C  CA  . PRO A 1 36 ? 2.323   -15.131 -16.627 1.00 38.90  ? 35  PRO A CA  1 
ATOM   267  C  C   . PRO A 1 36 ? 1.162   -14.688 -17.507 1.00 36.15  ? 35  PRO A C   1 
ATOM   268  O  O   . PRO A 1 36 ? 1.274   -13.752 -18.284 1.00 37.87  ? 35  PRO A O   1 
ATOM   269  C  CB  . PRO A 1 36 ? 2.218   -14.415 -15.268 1.00 38.26  ? 35  PRO A CB  1 
ATOM   270  C  CG  . PRO A 1 36 ? 3.475   -13.552 -15.165 1.00 45.40  ? 35  PRO A CG  1 
ATOM   271  C  CD  . PRO A 1 36 ? 4.077   -13.433 -16.580 1.00 40.58  ? 35  PRO A CD  1 
ATOM   272  N  N   . PRO A 1 37 ? -0.037  -15.248 -17.286 1.00 40.07  ? 36  PRO A N   1 
ATOM   273  C  CA  . PRO A 1 37 ? -1.250  -14.608 -17.789 1.00 41.18  ? 36  PRO A CA  1 
ATOM   274  C  C   . PRO A 1 37 ? -1.403  -13.146 -17.378 1.00 43.29  ? 36  PRO A C   1 
ATOM   275  O  O   . PRO A 1 37 ? -0.893  -12.718 -16.343 1.00 36.09  ? 36  PRO A O   1 
ATOM   276  C  CB  . PRO A 1 37 ? -2.374  -15.462 -17.198 1.00 41.45  ? 36  PRO A CB  1 
ATOM   277  C  CG  . PRO A 1 37 ? -1.747  -16.798 -16.874 1.00 37.38  ? 36  PRO A CG  1 
ATOM   278  C  CD  . PRO A 1 37 ? -0.267  -16.523 -16.595 1.00 39.45  ? 36  PRO A CD  1 
ATOM   279  N  N   . PRO A 1 38 ? -2.188  -12.326 -18.119 1.00 41.12  ? 37  PRO A N   1 
ATOM   280  C  CA  . PRO A 1 38 ? -2.584  -10.996 -17.647 1.00 42.90  ? 37  PRO A CA  1 
ATOM   281  C  C   . PRO A 1 38 ? -3.194  -10.966 -16.244 1.00 40.23  ? 37  PRO A C   1 
ATOM   282  O  O   . PRO A 1 38 ? -3.930  -11.876 -15.869 1.00 42.30  ? 37  PRO A O   1 
ATOM   283  C  CB  . PRO A 1 38 ? -3.540  -10.465 -18.747 1.00 50.18  ? 37  PRO A CB  1 
ATOM   284  C  CG  . PRO A 1 38 ? -3.838  -11.666 -19.594 1.00 41.94  ? 37  PRO A CG  1 
ATOM   285  C  CD  . PRO A 1 38 ? -2.675  -12.617 -19.487 1.00 52.30  ? 37  PRO A CD  1 
ATOM   286  N  N   . ASN A 1 39 ? -2.823  -9.922  -15.486 1.00 40.99  ? 38  ASN A N   1 
ATOM   287  C  CA  . ASN A 1 39 ? -3.265  -9.664  -14.136 1.00 42.32  ? 38  ASN A CA  1 
ATOM   288  C  C   . ASN A 1 39 ? -2.777  -10.752 -13.177 1.00 36.34  ? 38  ASN A C   1 
ATOM   289  O  O   . ASN A 1 39 ? -3.274  -10.781 -12.050 1.00 35.99  ? 38  ASN A O   1 
ATOM   290  C  CB  . ASN A 1 39 ? -4.786  -9.570  -14.056 1.00 49.73  ? 38  ASN A CB  1 
ATOM   291  C  CG  . ASN A 1 39 ? -5.303  -8.435  -14.912 1.00 54.95  ? 38  ASN A CG  1 
ATOM   292  O  OD1 . ASN A 1 39 ? -5.132  -7.261  -14.562 1.00 50.44  ? 38  ASN A OD1 1 
ATOM   293  N  ND2 . ASN A 1 39 ? -5.898  -8.767  -16.043 1.00 54.48  ? 38  ASN A ND2 1 
ATOM   294  N  N   . LYS A 1 40 ? -1.836  -11.631 -13.602 1.00 32.35  ? 39  LYS A N   1 
ATOM   295  C  CA  . LYS A 1 40 ? -1.282  -12.633 -12.676 1.00 24.73  ? 39  LYS A CA  1 
ATOM   296  C  C   . LYS A 1 40 ? 0.216   -12.380 -12.462 1.00 26.13  ? 39  LYS A C   1 
ATOM   297  O  O   . LYS A 1 40 ? 0.855   -11.654 -13.231 1.00 29.82  ? 39  LYS A O   1 
ATOM   298  C  CB  . LYS A 1 40 ? -1.405  -14.088 -13.130 1.00 31.00  ? 39  LYS A CB  1 
ATOM   299  C  CG  . LYS A 1 40 ? -2.824  -14.567 -13.542 1.00 31.14  ? 39  LYS A CG  1 
ATOM   300  C  CD  . LYS A 1 40 ? -3.695  -14.467 -12.300 1.00 33.92  ? 39  LYS A CD  1 
ATOM   301  C  CE  . LYS A 1 40 ? -5.160  -14.808 -12.603 1.00 42.81  ? 39  LYS A CE  1 
ATOM   302  N  NZ  . LYS A 1 40 ? -5.253  -16.196 -13.039 1.00 43.35  ? 39  LYS A NZ  1 
ATOM   303  N  N   . TYR A 1 41 ? 0.700   -12.812 -11.285 1.00 23.06  ? 40  TYR A N   1 
ATOM   304  C  CA  . TYR A 1 41 ? 2.112   -12.670 -10.935 1.00 25.40  ? 40  TYR A CA  1 
ATOM   305  C  C   . TYR A 1 41 ? 2.755   -14.047 -10.835 1.00 24.23  ? 40  TYR A C   1 
ATOM   306  O  O   . TYR A 1 41 ? 2.158   -15.044 -10.451 1.00 24.55  ? 40  TYR A O   1 
ATOM   307  C  CB  . TYR A 1 41 ? 2.188   -12.080 -9.486  1.00 25.02  ? 40  TYR A CB  1 
ATOM   308  C  CG  . TYR A 1 41 ? 1.716   -10.638 -9.478  1.00 25.87  ? 40  TYR A CG  1 
ATOM   309  C  CD1 . TYR A 1 41 ? 0.351   -10.356 -9.372  1.00 28.04  ? 40  TYR A CD1 1 
ATOM   310  C  CD2 . TYR A 1 41 ? 2.568   -9.563  -9.670  1.00 27.09  ? 40  TYR A CD2 1 
ATOM   311  C  CE1 . TYR A 1 41 ? -0.122  -9.056  -9.475  1.00 32.70  ? 40  TYR A CE1 1 
ATOM   312  C  CE2 . TYR A 1 41 ? 2.097   -8.249  -9.772  1.00 29.98  ? 40  TYR A CE2 1 
ATOM   313  C  CZ  . TYR A 1 41 ? 0.739   -7.997  -9.630  1.00 34.20  ? 40  TYR A CZ  1 
ATOM   314  O  OH  . TYR A 1 41 ? 0.141   -6.753  -9.776  1.00 33.97  ? 40  TYR A OH  1 
ATOM   315  N  N   . PRO A 1 42 ? 4.083   -14.169 -11.107 1.00 24.24  ? 41  PRO A N   1 
ATOM   316  C  CA  . PRO A 1 42 ? 4.739   -15.459 -10.888 1.00 23.81  ? 41  PRO A CA  1 
ATOM   317  C  C   . PRO A 1 42 ? 5.084   -15.592 -9.416  1.00 23.88  ? 41  PRO A C   1 
ATOM   318  O  O   . PRO A 1 42 ? 5.759   -14.689 -8.921  1.00 25.20  ? 41  PRO A O   1 
ATOM   319  C  CB  . PRO A 1 42 ? 6.088   -15.326 -11.680 1.00 25.62  ? 41  PRO A CB  1 
ATOM   320  C  CG  . PRO A 1 42 ? 6.209   -13.908 -12.004 1.00 25.76  ? 41  PRO A CG  1 
ATOM   321  C  CD  . PRO A 1 42 ? 4.909   -13.103 -11.698 1.00 26.07  ? 41  PRO A CD  1 
ATOM   322  N  N   . ILE A 1 43 ? 4.541   -16.631 -8.767  1.00 24.89  ? 42  ILE A N   1 
ATOM   323  C  CA  . ILE A 1 43 ? 4.783   -16.789 -7.330  1.00 23.51  ? 42  ILE A CA  1 
ATOM   324  C  C   . ILE A 1 43 ? 5.737   -17.959 -7.160  1.00 23.45  ? 42  ILE A C   1 
ATOM   325  O  O   . ILE A 1 43 ? 5.436   -19.108 -7.584  1.00 26.00  ? 42  ILE A O   1 
ATOM   326  C  CB  . ILE A 1 43 ? 3.437   -17.043 -6.636  1.00 22.63  ? 42  ILE A CB  1 
ATOM   327  C  CG1 . ILE A 1 43 ? 2.453   -15.941 -6.915  1.00 22.39  ? 42  ILE A CG1 1 
ATOM   328  C  CG2 . ILE A 1 43 ? 3.721   -17.154 -5.131  1.00 21.77  ? 42  ILE A CG2 1 
ATOM   329  C  CD1 . ILE A 1 43 ? 2.955   -14.530 -6.598  1.00 22.68  ? 42  ILE A CD1 1 
ATOM   330  N  N   . PHE A 1 44 ? 6.847   -17.720 -6.415  1.00 23.09  ? 43  PHE A N   1 
ATOM   331  C  CA  . PHE A 1 44 ? 7.743   -18.782 -6.061  1.00 24.20  ? 43  PHE A CA  1 
ATOM   332  C  C   . PHE A 1 44 ? 7.451   -19.173 -4.623  1.00 23.39  ? 43  PHE A C   1 
ATOM   333  O  O   . PHE A 1 44 ? 7.526   -18.342 -3.706  1.00 24.38  ? 43  PHE A O   1 
ATOM   334  C  CB  . PHE A 1 44 ? 9.192   -18.248 -6.208  1.00 24.37  ? 43  PHE A CB  1 
ATOM   335  C  CG  . PHE A 1 44 ? 10.205  -19.286 -5.771  1.00 25.20  ? 43  PHE A CG  1 
ATOM   336  C  CD1 . PHE A 1 44 ? 10.598  -20.302 -6.661  1.00 29.23  ? 43  PHE A CD1 1 
ATOM   337  C  CD2 . PHE A 1 44 ? 10.758  -19.256 -4.484  1.00 28.16  ? 43  PHE A CD2 1 
ATOM   338  C  CE1 . PHE A 1 44 ? 11.552  -21.247 -6.265  1.00 29.29  ? 43  PHE A CE1 1 
ATOM   339  C  CE2 . PHE A 1 44 ? 11.702  -20.219 -4.084  1.00 29.25  ? 43  PHE A CE2 1 
ATOM   340  C  CZ  . PHE A 1 44 ? 12.116  -21.195 -4.990  1.00 28.02  ? 43  PHE A CZ  1 
ATOM   341  N  N   . PHE A 1 45 ? 7.132   -20.460 -4.448  1.00 22.29  ? 44  PHE A N   1 
ATOM   342  C  CA  . PHE A 1 45 ? 6.801   -20.982 -3.130  1.00 22.85  ? 44  PHE A CA  1 
ATOM   343  C  C   . PHE A 1 45 ? 8.050   -21.476 -2.424  1.00 25.97  ? 44  PHE A C   1 
ATOM   344  O  O   . PHE A 1 45 ? 8.776   -22.347 -2.963  1.00 27.14  ? 44  PHE A O   1 
ATOM   345  C  CB  . PHE A 1 45 ? 5.814   -22.143 -3.339  1.00 26.14  ? 44  PHE A CB  1 
ATOM   346  C  CG  . PHE A 1 45 ? 4.437   -21.637 -3.766  1.00 24.11  ? 44  PHE A CG  1 
ATOM   347  C  CD1 . PHE A 1 45 ? 4.100   -21.488 -5.102  1.00 27.94  ? 44  PHE A CD1 1 
ATOM   348  C  CD2 . PHE A 1 45 ? 3.443   -21.399 -2.813  1.00 27.45  ? 44  PHE A CD2 1 
ATOM   349  C  CE1 . PHE A 1 45 ? 2.840   -20.974 -5.469  1.00 28.72  ? 44  PHE A CE1 1 
ATOM   350  C  CE2 . PHE A 1 45 ? 2.186   -20.896 -3.183  1.00 27.23  ? 44  PHE A CE2 1 
ATOM   351  C  CZ  . PHE A 1 45 ? 1.896   -20.688 -4.495  1.00 26.74  ? 44  PHE A CZ  1 
ATOM   352  N  N   . PHE A 1 46 ? 8.313   -20.911 -1.246  1.00 24.14  ? 45  PHE A N   1 
ATOM   353  C  CA  . PHE A 1 46 ? 9.460   -21.403 -0.473  1.00 24.14  ? 45  PHE A CA  1 
ATOM   354  C  C   . PHE A 1 46 ? 9.245   -22.861 -0.055  1.00 27.41  ? 45  PHE A C   1 
ATOM   355  O  O   . PHE A 1 46 ? 8.112   -23.342 0.075   1.00 26.62  ? 45  PHE A O   1 
ATOM   356  C  CB  . PHE A 1 46 ? 9.734   -20.492 0.732   1.00 24.93  ? 45  PHE A CB  1 
ATOM   357  C  CG  . PHE A 1 46 ? 10.197  -19.111 0.288   1.00 23.05  ? 45  PHE A CG  1 
ATOM   358  C  CD1 . PHE A 1 46 ? 11.466  -18.902 -0.253  1.00 23.83  ? 45  PHE A CD1 1 
ATOM   359  C  CD2 . PHE A 1 46 ? 9.452   -17.967 0.532   1.00 22.38  ? 45  PHE A CD2 1 
ATOM   360  C  CE1 . PHE A 1 46 ? 11.847  -17.626 -0.604  1.00 22.31  ? 45  PHE A CE1 1 
ATOM   361  C  CE2 . PHE A 1 46 ? 9.848   -16.688 0.225   1.00 20.55  ? 45  PHE A CE2 1 
ATOM   362  C  CZ  . PHE A 1 46 ? 11.071  -16.518 -0.389  1.00 22.80  ? 45  PHE A CZ  1 
ATOM   363  N  N   . GLY A 1 47 ? 10.356  -23.556 0.160   1.00 25.62  ? 46  GLY A N   1 
ATOM   364  C  CA  . GLY A 1 47 ? 10.288  -24.933 0.639   1.00 26.64  ? 46  GLY A CA  1 
ATOM   365  C  C   . GLY A 1 47 ? 10.076  -25.916 -0.517  1.00 33.61  ? 46  GLY A C   1 
ATOM   366  O  O   . GLY A 1 47 ? 10.942  -26.737 -0.808  1.00 34.75  ? 46  GLY A O   1 
ATOM   367  N  N   . THR A 1 48 ? 8.919   -25.846 -1.190  1.00 32.69  ? 47  THR A N   1 
ATOM   368  C  CA  . THR A 1 48 ? 8.698   -26.682 -2.371  1.00 32.40  ? 47  THR A CA  1 
ATOM   369  C  C   . THR A 1 48 ? 9.487   -26.199 -3.595  1.00 34.24  ? 47  THR A C   1 
ATOM   370  O  O   . THR A 1 48 ? 9.750   -26.968 -4.525  1.00 31.90  ? 47  THR A O   1 
ATOM   371  C  CB  . THR A 1 48 ? 7.208   -26.737 -2.713  1.00 33.97  ? 47  THR A CB  1 
ATOM   372  O  OG1 . THR A 1 48 ? 6.846   -25.441 -3.196  1.00 31.31  ? 47  THR A OG1 1 
ATOM   373  C  CG2 . THR A 1 48 ? 6.318   -27.199 -1.581  1.00 34.34  ? 47  THR A CG2 1 
ATOM   374  N  N   . HIS A 1 49 ? 9.806   -24.894 -3.656  1.00 28.44  ? 48  HIS A N   1 
ATOM   375  C  CA  . HIS A 1 49 ? 10.476  -24.287 -4.786  1.00 27.46  ? 48  HIS A CA  1 
ATOM   376  C  C   . HIS A 1 49 ? 9.630   -24.436 -6.049  1.00 28.67  ? 48  HIS A C   1 
ATOM   377  O  O   . HIS A 1 49 ? 10.193  -24.374 -7.134  1.00 33.61  ? 48  HIS A O   1 
ATOM   378  C  CB  . HIS A 1 49 ? 11.931  -24.781 -4.979  1.00 27.58  ? 48  HIS A CB  1 
ATOM   379  C  CG  . HIS A 1 49 ? 12.644  -24.841 -3.663  1.00 34.24  ? 48  HIS A CG  1 
ATOM   380  N  ND1 . HIS A 1 49 ? 13.390  -25.905 -3.204  1.00 33.59  ? 48  HIS A ND1 1 
ATOM   381  C  CD2 . HIS A 1 49 ? 12.706  -23.909 -2.704  1.00 30.97  ? 48  HIS A CD2 1 
ATOM   382  C  CE1 . HIS A 1 49 ? 13.860  -25.619 -1.994  1.00 40.29  ? 48  HIS A CE1 1 
ATOM   383  N  NE2 . HIS A 1 49 ? 13.460  -24.412 -1.667  1.00 34.63  ? 48  HIS A NE2 1 
ATOM   384  N  N   . GLU A 1 50 ? 8.302   -24.505 -5.905  1.00 29.44  ? 49  GLU A N   1 
ATOM   385  C  CA  . GLU A 1 50 ? 7.431   -24.539 -7.084  1.00 29.93  ? 49  GLU A CA  1 
ATOM   386  C  C   . GLU A 1 50 ? 6.977   -23.127 -7.477  1.00 30.02  ? 49  GLU A C   1 
ATOM   387  O  O   . GLU A 1 50 ? 7.185   -22.158 -6.729  1.00 28.56  ? 49  GLU A O   1 
ATOM   388  C  CB  . GLU A 1 50 ? 6.193   -25.400 -6.822  1.00 34.57  ? 49  GLU A CB  1 
ATOM   389  C  CG  . GLU A 1 50 ? 6.534   -26.878 -6.630  1.00 38.38  ? 49  GLU A CG  1 
ATOM   390  C  CD  . GLU A 1 50 ? 5.404   -27.729 -6.081  1.00 49.10  ? 49  GLU A CD  1 
ATOM   391  O  OE1 . GLU A 1 50 ? 4.277   -27.223 -5.897  1.00 52.71  ? 49  GLU A OE1 1 
ATOM   392  O  OE2 . GLU A 1 50 ? 5.698   -28.910 -5.771  1.00 59.35  ? 49  GLU A OE2 1 
ATOM   393  N  N   . THR A 1 51 ? 6.495   -22.960 -8.725  1.00 28.33  ? 50  THR A N   1 
ATOM   394  C  CA  . THR A 1 51 ? 6.040   -21.663 -9.203  1.00 27.58  ? 50  THR A CA  1 
ATOM   395  C  C   . THR A 1 51 ? 4.599   -21.837 -9.673  1.00 29.15  ? 50  THR A C   1 
ATOM   396  O  O   . THR A 1 51 ? 4.257   -22.832 -10.316 1.00 31.95  ? 50  THR A O   1 
ATOM   397  C  CB  . THR A 1 51 ? 6.892   -21.111 -10.348 1.00 30.34  ? 50  THR A CB  1 
ATOM   398  O  OG1 . THR A 1 51 ? 8.216   -20.754 -9.948  1.00 32.69  ? 50  THR A OG1 1 
ATOM   399  C  CG2 . THR A 1 51 ? 6.282   -19.895 -11.035 1.00 34.71  ? 50  THR A CG2 1 
ATOM   400  N  N   . ALA A 1 52 ? 3.735   -20.925 -9.276  1.00 30.71  ? 51  ALA A N   1 
ATOM   401  C  CA  . ALA A 1 52 ? 2.400   -20.857 -9.847  1.00 27.22  ? 51  ALA A CA  1 
ATOM   402  C  C   . ALA A 1 52 ? 2.057   -19.402 -10.136 1.00 29.51  ? 51  ALA A C   1 
ATOM   403  O  O   . ALA A 1 52 ? 2.769   -18.471 -9.745  1.00 29.12  ? 51  ALA A O   1 
ATOM   404  C  CB  . ALA A 1 52 ? 1.411   -21.464 -8.879  1.00 28.70  ? 51  ALA A CB  1 
ATOM   405  N  N   . PHE A 1 53 ? 0.999   -19.180 -10.927 1.00 25.45  ? 52  PHE A N   1 
ATOM   406  C  CA  . PHE A 1 53 ? 0.582   -17.854 -11.317 1.00 26.37  ? 52  PHE A CA  1 
ATOM   407  C  C   . PHE A 1 53 ? -0.665  -17.473 -10.550 1.00 31.22  ? 52  PHE A C   1 
ATOM   408  O  O   . PHE A 1 53 ? -1.677  -18.186 -10.623 1.00 33.98  ? 52  PHE A O   1 
ATOM   409  C  CB  . PHE A 1 53 ? 0.273   -17.838 -12.824 1.00 29.89  ? 52  PHE A CB  1 
ATOM   410  C  CG  . PHE A 1 53 ? 1.491   -18.139 -13.683 1.00 34.40  ? 52  PHE A CG  1 
ATOM   411  C  CD1 . PHE A 1 53 ? 2.667   -17.386 -13.566 1.00 39.62  ? 52  PHE A CD1 1 
ATOM   412  C  CD2 . PHE A 1 53 ? 1.454   -19.179 -14.616 1.00 38.26  ? 52  PHE A CD2 1 
ATOM   413  C  CE1 . PHE A 1 53 ? 3.791   -17.667 -14.354 1.00 44.40  ? 52  PHE A CE1 1 
ATOM   414  C  CE2 . PHE A 1 53 ? 2.575   -19.453 -15.389 1.00 39.16  ? 52  PHE A CE2 1 
ATOM   415  C  CZ  . PHE A 1 53 ? 3.734   -18.705 -15.266 1.00 40.42  ? 52  PHE A CZ  1 
ATOM   416  N  N   . LEU A 1 54 ? -0.570  -16.385 -9.760  1.00 24.78  ? 53  LEU A N   1 
ATOM   417  C  CA  . LEU A 1 54 ? -1.700  -16.029 -8.896  1.00 23.99  ? 53  LEU A CA  1 
ATOM   418  C  C   . LEU A 1 54 ? -1.988  -14.530 -8.991  1.00 24.94  ? 53  LEU A C   1 
ATOM   419  O  O   . LEU A 1 54 ? -1.131  -13.697 -9.343  1.00 25.46  ? 53  LEU A O   1 
ATOM   420  C  CB  . LEU A 1 54 ? -1.323  -16.308 -7.434  1.00 25.09  ? 53  LEU A CB  1 
ATOM   421  C  CG  . LEU A 1 54 ? -1.366  -17.774 -7.037  1.00 26.75  ? 53  LEU A CG  1 
ATOM   422  C  CD1 . LEU A 1 54 ? -0.995  -17.908 -5.562  1.00 27.77  ? 53  LEU A CD1 1 
ATOM   423  C  CD2 . LEU A 1 54 ? -2.797  -18.346 -7.294  1.00 32.03  ? 53  LEU A CD2 1 
ATOM   424  N  N   . GLY A 1 55 ? -3.270  -14.153 -8.735  1.00 23.80  ? 54  GLY A N   1 
ATOM   425  C  CA  . GLY A 1 55 ? -3.607  -12.737 -8.649  1.00 24.66  ? 54  GLY A CA  1 
ATOM   426  C  C   . GLY A 1 55 ? -3.640  -12.235 -7.185  1.00 21.30  ? 54  GLY A C   1 
ATOM   427  O  O   . GLY A 1 55 ? -3.589  -13.066 -6.257  1.00 21.75  ? 54  GLY A O   1 
ATOM   428  N  N   . PRO A 1 56 ? -3.759  -10.909 -7.008  1.00 23.42  ? 55  PRO A N   1 
ATOM   429  C  CA  . PRO A 1 56 ? -3.651  -10.276 -5.679  1.00 22.90  ? 55  PRO A CA  1 
ATOM   430  C  C   . PRO A 1 56 ? -4.633  -10.816 -4.658  1.00 24.04  ? 55  PRO A C   1 
ATOM   431  O  O   . PRO A 1 56 ? -4.364  -10.777 -3.461  1.00 21.98  ? 55  PRO A O   1 
ATOM   432  C  CB  . PRO A 1 56 ? -3.945  -8.808  -5.984  1.00 24.11  ? 55  PRO A CB  1 
ATOM   433  C  CG  . PRO A 1 56 ? -3.368  -8.578  -7.386  1.00 26.83  ? 55  PRO A CG  1 
ATOM   434  C  CD  . PRO A 1 56 ? -3.725  -9.888  -8.080  1.00 24.90  ? 55  PRO A CD  1 
ATOM   435  N  N   . LYS A 1 57 ? -5.784  -11.339 -5.128  1.00 25.48  ? 56  LYS A N   1 
ATOM   436  C  CA  . LYS A 1 57 ? -6.742  -11.913 -4.170  1.00 24.71  ? 56  LYS A CA  1 
ATOM   437  C  C   . LYS A 1 57 ? -6.187  -13.050 -3.303  1.00 25.84  ? 56  LYS A C   1 
ATOM   438  O  O   . LYS A 1 57 ? -6.630  -13.288 -2.192  1.00 23.94  ? 56  LYS A O   1 
ATOM   439  C  CB  . LYS A 1 57 ? -8.033  -12.416 -4.860  1.00 28.46  ? 56  LYS A CB  1 
ATOM   440  C  CG  . LYS A 1 57 ? -7.833  -13.711 -5.638  1.00 28.86  ? 56  LYS A CG  1 
ATOM   441  C  CD  . LYS A 1 57 ? -9.160  -14.149 -6.278  1.00 35.47  ? 56  LYS A CD  1 
ATOM   442  C  CE  . LYS A 1 57 ? -9.182  -15.539 -6.869  1.00 38.79  ? 56  LYS A CE  1 
ATOM   443  N  NZ  . LYS A 1 57 ? -8.879  -16.624 -5.930  1.00 45.10  ? 56  LYS A NZ  1 
ATOM   444  N  N   . ASP A 1 58 ? -5.134  -13.743 -3.781  1.00 22.49  ? 57  ASP A N   1 
ATOM   445  C  CA  . ASP A 1 58 ? -4.545  -14.872 -3.111  1.00 23.15  ? 57  ASP A CA  1 
ATOM   446  C  C   . ASP A 1 58 ? -3.169  -14.496 -2.519  1.00 20.89  ? 57  ASP A C   1 
ATOM   447  O  O   . ASP A 1 58 ? -2.495  -15.446 -2.109  1.00 24.09  ? 57  ASP A O   1 
ATOM   448  C  CB  . ASP A 1 58 ? -4.456  -16.048 -4.080  1.00 25.57  ? 57  ASP A CB  1 
ATOM   449  C  CG  . ASP A 1 58 ? -5.845  -16.603 -4.410  1.00 27.99  ? 57  ASP A CG  1 
ATOM   450  O  OD1 . ASP A 1 58 ? -6.652  -16.718 -3.441  1.00 31.35  ? 57  ASP A OD1 1 
ATOM   451  O  OD2 . ASP A 1 58 ? -6.083  -16.952 -5.571  1.00 30.50  ? 57  ASP A OD2 1 
ATOM   452  N  N   . LEU A 1 59 ? -2.857  -13.196 -2.476  1.00 20.99  ? 58  LEU A N   1 
ATOM   453  C  CA  . LEU A 1 59 ? -1.525  -12.772 -1.981  1.00 20.65  ? 58  LEU A CA  1 
ATOM   454  C  C   . LEU A 1 59 ? -1.690  -11.938 -0.720  1.00 18.92  ? 58  LEU A C   1 
ATOM   455  O  O   . LEU A 1 59 ? -2.243  -10.838 -0.749  1.00 21.84  ? 58  LEU A O   1 
ATOM   456  C  CB  . LEU A 1 59 ? -0.794  -12.044 -3.114  1.00 21.30  ? 58  LEU A CB  1 
ATOM   457  C  CG  . LEU A 1 59 ? -0.637  -12.853 -4.395  1.00 23.09  ? 58  LEU A CG  1 
ATOM   458  C  CD1 . LEU A 1 59 ? 0.013   -11.962 -5.458  1.00 25.38  ? 58  LEU A CD1 1 
ATOM   459  C  CD2 . LEU A 1 59 ? 0.200   -14.128 -4.244  1.00 21.72  ? 58  LEU A CD2 1 
ATOM   460  N  N   . PHE A 1 60 ? -1.088  -12.383 0.391   1.00 21.55  ? 59  PHE A N   1 
ATOM   461  C  CA  . PHE A 1 60 ? -1.188  -11.683 1.679   1.00 20.82  ? 59  PHE A CA  1 
ATOM   462  C  C   . PHE A 1 60 ? 0.213   -11.207 2.069   1.00 22.93  ? 59  PHE A C   1 
ATOM   463  O  O   . PHE A 1 60 ? 1.084   -12.059 2.288   1.00 25.84  ? 59  PHE A O   1 
ATOM   464  C  CB  . PHE A 1 60 ? -1.669  -12.738 2.679   1.00 23.90  ? 59  PHE A CB  1 
ATOM   465  C  CG  . PHE A 1 60 ? -3.111  -13.186 2.446   1.00 23.34  ? 59  PHE A CG  1 
ATOM   466  C  CD1 . PHE A 1 60 ? -3.388  -14.087 1.431   1.00 24.90  ? 59  PHE A CD1 1 
ATOM   467  C  CD2 . PHE A 1 60 ? -4.145  -12.641 3.228   1.00 25.07  ? 59  PHE A CD2 1 
ATOM   468  C  CE1 . PHE A 1 60 ? -4.709  -14.468 1.150   1.00 29.81  ? 59  PHE A CE1 1 
ATOM   469  C  CE2 . PHE A 1 60 ? -5.442  -13.013 2.923   1.00 27.15  ? 59  PHE A CE2 1 
ATOM   470  C  CZ  . PHE A 1 60 ? -5.694  -13.932 1.937   1.00 24.47  ? 59  PHE A CZ  1 
ATOM   471  N  N   . PRO A 1 61 ? 0.463   -9.901  2.169   1.00 25.01  ? 60  PRO A N   1 
ATOM   472  C  CA  . PRO A 1 61 ? 1.811   -9.399  2.520   1.00 24.17  ? 60  PRO A CA  1 
ATOM   473  C  C   . PRO A 1 61 ? 2.330   -10.039 3.800   1.00 25.17  ? 60  PRO A C   1 
ATOM   474  O  O   . PRO A 1 61 ? 1.623   -10.258 4.797   1.00 26.06  ? 60  PRO A O   1 
ATOM   475  C  CB  . PRO A 1 61 ? 1.615   -7.902  2.614   1.00 26.09  ? 60  PRO A CB  1 
ATOM   476  C  CG  . PRO A 1 61 ? 0.518   -7.621  1.555   1.00 28.64  ? 60  PRO A CG  1 
ATOM   477  C  CD  . PRO A 1 61 ? -0.443  -8.779  1.835   1.00 28.42  ? 60  PRO A CD  1 
ATOM   478  N  N   . TYR A 1 62 ? 3.634   -10.439 3.763   1.00 24.19  ? 61  TYR A N   1 
ATOM   479  C  CA  . TYR A 1 62 ? 4.173   -11.313 4.794   1.00 23.86  ? 61  TYR A CA  1 
ATOM   480  C  C   . TYR A 1 62 ? 4.198   -10.655 6.188   1.00 23.34  ? 61  TYR A C   1 
ATOM   481  O  O   . TYR A 1 62 ? 3.830   -11.343 7.154   1.00 25.93  ? 61  TYR A O   1 
ATOM   482  C  CB  . TYR A 1 62 ? 5.589   -11.758 4.325   1.00 24.33  ? 61  TYR A CB  1 
ATOM   483  C  CG  . TYR A 1 62 ? 6.384   -12.558 5.351   1.00 25.27  ? 61  TYR A CG  1 
ATOM   484  C  CD1 . TYR A 1 62 ? 6.098   -13.901 5.625   1.00 26.80  ? 61  TYR A CD1 1 
ATOM   485  C  CD2 . TYR A 1 62 ? 7.405   -11.938 6.063   1.00 31.20  ? 61  TYR A CD2 1 
ATOM   486  C  CE1 . TYR A 1 62 ? 6.785   -14.635 6.596   1.00 29.51  ? 61  TYR A CE1 1 
ATOM   487  C  CE2 . TYR A 1 62 ? 8.100   -12.685 7.005   1.00 26.61  ? 61  TYR A CE2 1 
ATOM   488  C  CZ  . TYR A 1 62 ? 7.801   -13.999 7.280   1.00 29.61  ? 61  TYR A CZ  1 
ATOM   489  O  OH  . TYR A 1 62 ? 8.528   -14.717 8.235   1.00 30.70  ? 61  TYR A OH  1 
ATOM   490  N  N   . ASP A 1 63 ? 4.580   -9.375  6.215   1.00 28.69  ? 62  ASP A N   1 
ATOM   491  C  CA  . ASP A 1 63 ? 4.727   -8.713  7.510   1.00 33.22  ? 62  ASP A CA  1 
ATOM   492  C  C   . ASP A 1 63 ? 3.389   -8.709  8.258   1.00 28.56  ? 62  ASP A C   1 
ATOM   493  O  O   . ASP A 1 63 ? 3.367   -9.159  9.402   1.00 36.21  ? 62  ASP A O   1 
ATOM   494  C  CB  . ASP A 1 63 ? 5.459   -7.386  7.426   1.00 35.24  ? 62  ASP A CB  1 
ATOM   495  C  CG  . ASP A 1 63 ? 5.801   -6.818  8.793   1.00 58.63  ? 62  ASP A CG  1 
ATOM   496  O  OD1 . ASP A 1 63 ? 6.540   -7.508  9.546   1.00 55.14  ? 62  ASP A OD1 1 
ATOM   497  O  OD2 . ASP A 1 63 ? 5.297   -5.708  9.102   1.00 66.23  ? 62  ASP A OD2 1 
ATOM   498  N  N   . LYS A 1 64 ? 2.314   -8.304  7.548   1.00 30.17  ? 63  LYS A N   1 
ATOM   499  C  CA  . LYS A 1 64 ? 0.988   -8.233  8.179   1.00 32.01  ? 63  LYS A CA  1 
ATOM   500  C  C   . LYS A 1 64 ? 0.496   -9.612  8.626   1.00 33.87  ? 63  LYS A C   1 
ATOM   501  O  O   . LYS A 1 64 ? -0.185  -9.732  9.644   1.00 31.63  ? 63  LYS A O   1 
ATOM   502  C  CB  . LYS A 1 64 ? 0.075   -7.557  7.150   1.00 29.30  ? 63  LYS A CB  1 
ATOM   503  C  CG  . LYS A 1 64 ? -1.393  -7.494  7.571   1.00 38.58  ? 63  LYS A CG  1 
ATOM   504  C  CD  . LYS A 1 64 ? -2.164  -6.692  6.534   1.00 32.69  ? 63  LYS A CD  1 
ATOM   505  C  CE  . LYS A 1 64 ? -3.348  -6.028  7.186   1.00 42.90  ? 63  LYS A CE  1 
ATOM   506  N  NZ  . LYS A 1 64 ? -4.387  -6.991  7.535   1.00 46.15  ? 63  LYS A NZ  1 
ATOM   507  N  N   . SER A 1 65 ? 0.794   -10.681 7.867   1.00 28.53  ? 64  SER A N   1 
ATOM   508  C  CA  . SER A 1 65 ? 0.127   -11.968 7.972   1.00 28.45  ? 64  SER A CA  1 
ATOM   509  C  C   . SER A 1 65 ? 0.893   -13.051 8.759   1.00 28.70  ? 64  SER A C   1 
ATOM   510  O  O   . SER A 1 65 ? 0.373   -14.156 8.923   1.00 30.83  ? 64  SER A O   1 
ATOM   511  C  CB  . SER A 1 65 ? -0.157  -12.507 6.573   1.00 31.74  ? 64  SER A CB  1 
ATOM   512  O  OG  . SER A 1 65 ? -1.041  -11.615 5.889   1.00 38.66  ? 64  SER A OG  1 
ATOM   513  N  N   . LYS A 1 66 ? 2.182   -12.809 9.082   1.00 29.15  ? 65  LYS A N   1 
ATOM   514  C  CA  . LYS A 1 66 ? 3.013   -13.883 9.605   1.00 31.89  ? 65  LYS A CA  1 
ATOM   515  C  C   . LYS A 1 66 ? 2.536   -14.392 10.965  1.00 32.26  ? 65  LYS A C   1 
ATOM   516  O  O   . LYS A 1 66 ? 2.651   -15.574 11.256  1.00 34.66  ? 65  LYS A O   1 
ATOM   517  C  CB  . LYS A 1 66 ? 4.488   -13.488 9.639   1.00 31.77  ? 65  LYS A CB  1 
ATOM   518  C  CG  . LYS A 1 66 ? 4.846   -12.315 10.500  1.00 33.11  ? 65  LYS A CG  1 
ATOM   519  C  CD  . LYS A 1 66 ? 6.325   -12.026 10.269  1.00 42.09  ? 65  LYS A CD  1 
ATOM   520  C  CE  . LYS A 1 66 ? 6.922   -11.142 11.329  1.00 50.04  ? 65  LYS A CE  1 
ATOM   521  N  NZ  . LYS A 1 66 ? 6.191   -9.876  11.439  1.00 56.97  ? 65  LYS A NZ  1 
ATOM   522  N  N   A ASP A 1 67 ? 1.967   -13.498 11.779  0.50 35.31  ? 66  ASP A N   1 
ATOM   523  N  N   B ASP A 1 67 ? 2.043   -13.474 11.800  0.50 33.32  ? 66  ASP A N   1 
ATOM   524  C  CA  A ASP A 1 67 ? 1.464   -13.901 13.089  0.50 37.92  ? 66  ASP A CA  1 
ATOM   525  C  CA  B ASP A 1 67 ? 1.446   -13.891 13.061  0.50 35.91  ? 66  ASP A CA  1 
ATOM   526  C  C   A ASP A 1 67 ? 0.314   -14.907 12.973  0.50 35.75  ? 66  ASP A C   1 
ATOM   527  C  C   B ASP A 1 67 ? 0.493   -15.058 12.814  0.50 33.02  ? 66  ASP A C   1 
ATOM   528  O  O   A ASP A 1 67 ? 0.065   -15.696 13.878  0.50 35.82  ? 66  ASP A O   1 
ATOM   529  O  O   B ASP A 1 67 ? 0.607   -16.120 13.431  0.50 34.91  ? 66  ASP A O   1 
ATOM   530  C  CB  A ASP A 1 67 ? 1.098   -12.689 13.931  0.50 40.75  ? 66  ASP A CB  1 
ATOM   531  C  CB  B ASP A 1 67 ? 0.722   -12.728 13.719  0.50 37.70  ? 66  ASP A CB  1 
ATOM   532  C  CG  A ASP A 1 67 ? 2.255   -11.889 14.518  0.50 46.18  ? 66  ASP A CG  1 
ATOM   533  C  CG  B ASP A 1 67 ? 0.160   -12.990 15.109  0.50 44.05  ? 66  ASP A CG  1 
ATOM   534  O  OD1 A ASP A 1 67 ? 3.422   -12.314 14.352  0.50 46.11  ? 66  ASP A OD1 1 
ATOM   535  O  OD1 B ASP A 1 67 ? 0.966   -13.068 16.064  0.50 48.44  ? 66  ASP A OD1 1 
ATOM   536  O  OD2 A ASP A 1 67 ? 1.980   -10.841 15.148  0.50 46.50  ? 66  ASP A OD2 1 
ATOM   537  O  OD2 B ASP A 1 67 ? -1.079  -13.109 15.223  0.50 50.18  ? 66  ASP A OD2 1 
ATOM   538  N  N   . LYS A 1 68 ? -0.436  -14.857 11.870  1.00 32.62  ? 67  LYS A N   1 
ATOM   539  C  CA  . LYS A 1 68 ? -1.516  -15.787 11.655  1.00 31.70  ? 67  LYS A CA  1 
ATOM   540  C  C   . LYS A 1 68 ? -1.033  -17.014 10.890  1.00 34.11  ? 67  LYS A C   1 
ATOM   541  O  O   . LYS A 1 68 ? -1.498  -18.115 11.151  1.00 37.33  ? 67  LYS A O   1 
ATOM   542  C  CB  . LYS A 1 68 ? -2.573  -15.055 10.824  1.00 31.74  ? 67  LYS A CB  1 
ATOM   543  C  CG  . LYS A 1 68 ? -3.864  -15.787 10.613  1.00 36.90  ? 67  LYS A CG  1 
ATOM   544  C  CD  . LYS A 1 68 ? -4.875  -14.853 9.936   1.00 38.31  ? 67  LYS A CD  1 
ATOM   545  C  CE  . LYS A 1 68 ? -6.261  -15.411 9.921   1.00 45.27  ? 67  LYS A CE  1 
ATOM   546  N  NZ  . LYS A 1 68 ? -7.168  -14.408 9.350   1.00 47.41  ? 67  LYS A NZ  1 
ATOM   547  N  N   . TYR A 1 69 ? -0.181  -16.831 9.855   1.00 30.33  ? 68  TYR A N   1 
ATOM   548  C  CA  . TYR A 1 69 ? 0.043   -17.934 8.935   1.00 28.04  ? 68  TYR A CA  1 
ATOM   549  C  C   . TYR A 1 69 ? 1.432   -18.562 9.075   1.00 28.48  ? 68  TYR A C   1 
ATOM   550  O  O   . TYR A 1 69 ? 1.640   -19.659 8.565   1.00 32.02  ? 68  TYR A O   1 
ATOM   551  C  CB  . TYR A 1 69 ? -0.149  -17.420 7.496   1.00 26.70  ? 68  TYR A CB  1 
ATOM   552  C  CG  . TYR A 1 69 ? -1.545  -16.982 7.107   1.00 29.31  ? 68  TYR A CG  1 
ATOM   553  C  CD1 . TYR A 1 69 ? -2.668  -17.729 7.481   1.00 30.18  ? 68  TYR A CD1 1 
ATOM   554  C  CD2 . TYR A 1 69 ? -1.733  -15.794 6.402   1.00 31.53  ? 68  TYR A CD2 1 
ATOM   555  C  CE1 . TYR A 1 69 ? -3.937  -17.321 7.095   1.00 34.44  ? 68  TYR A CE1 1 
ATOM   556  C  CE2 . TYR A 1 69 ? -3.003  -15.363 6.045   1.00 32.65  ? 68  TYR A CE2 1 
ATOM   557  C  CZ  . TYR A 1 69 ? -4.103  -16.124 6.404   1.00 33.84  ? 68  TYR A CZ  1 
ATOM   558  O  OH  . TYR A 1 69 ? -5.344  -15.699 6.013   1.00 33.51  ? 68  TYR A OH  1 
ATOM   559  N  N   . GLY A 1 70 ? 2.324   -17.926 9.843   1.00 29.08  ? 69  GLY A N   1 
ATOM   560  C  CA  . GLY A 1 70 ? 3.722   -18.361 9.944   1.00 31.41  ? 69  GLY A CA  1 
ATOM   561  C  C   . GLY A 1 70 ? 3.961   -19.293 11.133  1.00 33.10  ? 69  GLY A C   1 
ATOM   562  O  O   . GLY A 1 70 ? 4.703   -18.963 12.042  1.00 44.05  ? 69  GLY A O   1 
ATOM   563  N  N   . LYS A 1 71 ? 3.237   -20.405 11.132  1.00 37.42  ? 70  LYS A N   1 
ATOM   564  C  CA  . LYS A 1 71 ? 3.372   -21.450 12.134  1.00 40.39  ? 70  LYS A CA  1 
ATOM   565  C  C   . LYS A 1 71 ? 3.639   -22.777 11.425  1.00 33.87  ? 70  LYS A C   1 
ATOM   566  O  O   . LYS A 1 71 ? 3.254   -23.007 10.275  1.00 37.93  ? 70  LYS A O   1 
ATOM   567  C  CB  . LYS A 1 71 ? 2.111   -21.405 13.009  1.00 45.64  ? 70  LYS A CB  1 
ATOM   568  C  CG  . LYS A 1 71 ? 1.992   -20.193 13.935  1.00 44.35  ? 70  LYS A CG  1 
ATOM   569  C  CD  . LYS A 1 71 ? 0.551   -19.860 14.331  1.00 48.46  ? 70  LYS A CD  1 
ATOM   570  N  N   . PRO A 1 72 ? 4.323   -23.752 12.068  1.00 33.73  ? 71  PRO A N   1 
ATOM   571  C  CA  . PRO A 1 72 ? 4.579   -25.037 11.416  1.00 36.07  ? 71  PRO A CA  1 
ATOM   572  C  C   . PRO A 1 72 ? 3.368   -25.787 10.891  1.00 34.87  ? 71  PRO A C   1 
ATOM   573  O  O   . PRO A 1 72 ? 2.301   -25.717 11.494  1.00 41.77  ? 71  PRO A O   1 
ATOM   574  C  CB  . PRO A 1 72 ? 5.350   -25.827 12.494  1.00 41.24  ? 71  PRO A CB  1 
ATOM   575  C  CG  . PRO A 1 72 ? 5.971   -24.743 13.342  1.00 43.95  ? 71  PRO A CG  1 
ATOM   576  C  CD  . PRO A 1 72 ? 4.927   -23.616 13.404  1.00 41.07  ? 71  PRO A CD  1 
ATOM   577  N  N   . ASN A 1 73 ? 3.564   -26.517 9.791   1.00 40.24  ? 72  ASN A N   1 
ATOM   578  C  CA  . ASN A 1 73 ? 2.516   -27.258 9.122   1.00 45.16  ? 72  ASN A CA  1 
ATOM   579  C  C   . ASN A 1 73 ? 3.088   -28.607 8.717   1.00 45.86  ? 72  ASN A C   1 
ATOM   580  O  O   . ASN A 1 73 ? 4.266   -28.729 8.378   1.00 49.85  ? 72  ASN A O   1 
ATOM   581  C  CB  . ASN A 1 73 ? 2.029   -26.481 7.903   1.00 43.78  ? 72  ASN A CB  1 
ATOM   582  C  CG  . ASN A 1 73 ? 0.638   -26.858 7.444   1.00 55.54  ? 72  ASN A CG  1 
ATOM   583  O  OD1 . ASN A 1 73 ? 0.473   -27.765 6.621   1.00 51.80  ? 72  ASN A OD1 1 
ATOM   584  N  ND2 . ASN A 1 73 ? -0.369  -26.115 7.883   1.00 55.17  ? 72  ASN A ND2 1 
ATOM   585  N  N   . LYS A 1 74 ? 2.223   -29.615 8.717   1.00 50.33  ? 73  LYS A N   1 
ATOM   586  C  CA  . LYS A 1 74 ? 2.635   -30.972 8.433   1.00 50.76  ? 73  LYS A CA  1 
ATOM   587  C  C   . LYS A 1 74 ? 2.934   -31.139 6.945   1.00 50.23  ? 73  LYS A C   1 
ATOM   588  O  O   . LYS A 1 74 ? 3.536   -32.129 6.536   1.00 49.48  ? 73  LYS A O   1 
ATOM   589  C  CB  . LYS A 1 74 ? 1.541   -31.921 8.951   1.00 59.21  ? 73  LYS A CB  1 
ATOM   590  C  CG  . LYS A 1 74 ? 0.262   -32.042 8.114   1.00 61.00  ? 73  LYS A CG  1 
ATOM   591  N  N   . ARG A 1 75 ? 2.511   -30.174 6.126   1.00 42.94  ? 74  ARG A N   1 
ATOM   592  C  CA  . ARG A 1 75 ? 2.533   -30.387 4.689   1.00 45.59  ? 74  ARG A CA  1 
ATOM   593  C  C   . ARG A 1 75 ? 3.970   -30.334 4.176   1.00 39.08  ? 74  ARG A C   1 
ATOM   594  O  O   . ARG A 1 75 ? 4.779   -29.571 4.699   1.00 39.39  ? 74  ARG A O   1 
ATOM   595  C  CB  . ARG A 1 75 ? 1.607   -29.396 3.969   1.00 45.61  ? 74  ARG A CB  1 
ATOM   596  C  CG  . ARG A 1 75 ? 0.150   -29.623 4.343   1.00 54.30  ? 74  ARG A CG  1 
ATOM   597  C  CD  . ARG A 1 75 ? -0.437  -30.785 3.574   1.00 47.91  ? 74  ARG A CD  1 
ATOM   598  N  NE  . ARG A 1 75 ? -0.997  -30.408 2.273   1.00 57.82  ? 74  ARG A NE  1 
ATOM   599  C  CZ  . ARG A 1 75 ? -2.128  -29.717 2.124   1.00 58.08  ? 74  ARG A CZ  1 
ATOM   600  N  NH1 . ARG A 1 75 ? -2.583  -29.477 0.908   1.00 59.37  ? 74  ARG A NH1 1 
ATOM   601  N  NH2 . ARG A 1 75 ? -2.812  -29.306 3.184   1.00 60.86  ? 74  ARG A NH2 1 
ATOM   602  N  N   . LYS A 1 76 ? 4.247   -31.138 3.142   1.00 36.29  ? 75  LYS A N   1 
ATOM   603  C  CA  . LYS A 1 76 ? 5.598   -31.302 2.622   1.00 38.61  ? 75  LYS A CA  1 
ATOM   604  C  C   . LYS A 1 76 ? 6.192   -29.957 2.186   1.00 38.26  ? 75  LYS A C   1 
ATOM   605  O  O   . LYS A 1 76 ? 5.610   -29.282 1.338   1.00 37.57  ? 75  LYS A O   1 
ATOM   606  C  CB  . LYS A 1 76 ? 5.598   -32.239 1.411   1.00 43.90  ? 75  LYS A CB  1 
ATOM   607  C  CG  . LYS A 1 76 ? 6.971   -32.538 0.838   1.00 47.12  ? 75  LYS A CG  1 
ATOM   608  C  CD  . LYS A 1 76 ? 7.027   -33.709 -0.139  1.00 48.69  ? 75  LYS A CD  1 
ATOM   609  C  CE  . LYS A 1 76 ? 8.396   -33.877 -0.740  1.00 52.23  ? 75  LYS A CE  1 
ATOM   610  N  N   . GLY A 1 77 ? 7.386   -29.631 2.708   1.00 38.56  ? 76  GLY A N   1 
ATOM   611  C  CA  . GLY A 1 77 ? 8.134   -28.446 2.293   1.00 33.45  ? 76  GLY A CA  1 
ATOM   612  C  C   . GLY A 1 77 ? 7.794   -27.197 3.104   1.00 32.94  ? 76  GLY A C   1 
ATOM   613  O  O   . GLY A 1 77 ? 8.521   -26.202 3.027   1.00 31.37  ? 76  GLY A O   1 
ATOM   614  N  N   . PHE A 1 78 ? 6.704   -27.224 3.879   1.00 30.10  ? 77  PHE A N   1 
ATOM   615  C  CA  . PHE A 1 78 ? 6.215   -26.007 4.514   1.00 31.34  ? 77  PHE A CA  1 
ATOM   616  C  C   . PHE A 1 78 ? 7.222   -25.436 5.527   1.00 34.79  ? 77  PHE A C   1 
ATOM   617  O  O   . PHE A 1 78 ? 7.481   -24.230 5.548   1.00 31.95  ? 77  PHE A O   1 
ATOM   618  C  CB  . PHE A 1 78 ? 4.826   -26.290 5.088   1.00 32.61  ? 77  PHE A CB  1 
ATOM   619  C  CG  . PHE A 1 78 ? 4.119   -25.014 5.512   1.00 35.33  ? 77  PHE A CG  1 
ATOM   620  C  CD1 . PHE A 1 78 ? 4.417   -24.383 6.710   1.00 34.76  ? 77  PHE A CD1 1 
ATOM   621  C  CD2 . PHE A 1 78 ? 3.136   -24.446 4.693   1.00 35.92  ? 77  PHE A CD2 1 
ATOM   622  C  CE1 . PHE A 1 78 ? 3.761   -23.214 7.080   1.00 33.90  ? 77  PHE A CE1 1 
ATOM   623  C  CE2 . PHE A 1 78 ? 2.482   -23.264 5.074   1.00 29.57  ? 77  PHE A CE2 1 
ATOM   624  C  CZ  . PHE A 1 78 ? 2.782   -22.657 6.263   1.00 32.11  ? 77  PHE A CZ  1 
ATOM   625  N  N   . ASN A 1 79 ? 7.788   -26.293 6.398   1.00 33.04  ? 78  ASN A N   1 
ATOM   626  C  CA  . ASN A 1 79 ? 8.678   -25.793 7.446   1.00 32.31  ? 78  ASN A CA  1 
ATOM   627  C  C   . ASN A 1 79 ? 10.032  -25.325 6.881   1.00 27.34  ? 78  ASN A C   1 
ATOM   628  O  O   . ASN A 1 79 ? 10.624  -24.351 7.398   1.00 31.37  ? 78  ASN A O   1 
ATOM   629  C  CB  . ASN A 1 79 ? 8.798   -26.806 8.594   1.00 32.10  ? 78  ASN A CB  1 
ATOM   630  C  CG  . ASN A 1 79 ? 7.454   -27.092 9.226   1.00 39.33  ? 78  ASN A CG  1 
ATOM   631  O  OD1 . ASN A 1 79 ? 6.543   -26.265 9.141   1.00 35.11  ? 78  ASN A OD1 1 
ATOM   632  N  ND2 . ASN A 1 79 ? 7.318   -28.254 9.863   1.00 35.17  ? 78  ASN A ND2 1 
ATOM   633  N  N   . GLU A 1 80 ? 10.531  -25.989 5.825   1.00 28.11  ? 79  GLU A N   1 
ATOM   634  C  CA  . GLU A 1 80 ? 11.686  -25.480 5.105   1.00 29.19  ? 79  GLU A CA  1 
ATOM   635  C  C   . GLU A 1 80 ? 11.326  -24.100 4.545   1.00 27.18  ? 79  GLU A C   1 
ATOM   636  O  O   . GLU A 1 80 ? 12.136  -23.175 4.563   1.00 26.30  ? 79  GLU A O   1 
ATOM   637  C  CB  . GLU A 1 80 ? 12.121  -26.433 3.993   1.00 30.16  ? 79  GLU A CB  1 
ATOM   638  C  CG  . GLU A 1 80 ? 13.372  -25.968 3.263   1.00 31.28  ? 79  GLU A CG  1 
ATOM   639  C  CD  . GLU A 1 80 ? 13.854  -26.989 2.229   1.00 43.68  ? 79  GLU A CD  1 
ATOM   640  O  OE1 . GLU A 1 80 ? 13.147  -27.953 1.877   1.00 46.85  ? 79  GLU A OE1 1 
ATOM   641  O  OE2 . GLU A 1 80 ? 14.984  -26.799 1.761   1.00 40.21  ? 79  GLU A OE2 1 
ATOM   642  N  N   . GLY A 1 81 ? 10.121  -23.995 3.971   1.00 26.61  ? 80  GLY A N   1 
ATOM   643  C  CA  . GLY A 1 81 ? 9.710   -22.702 3.443   1.00 27.38  ? 80  GLY A CA  1 
ATOM   644  C  C   . GLY A 1 81 ? 9.667   -21.603 4.500   1.00 23.81  ? 80  GLY A C   1 
ATOM   645  O  O   . GLY A 1 81 ? 10.021  -20.464 4.180   1.00 24.91  ? 80  GLY A O   1 
ATOM   646  N  N   . LEU A 1 82 ? 9.212   -21.887 5.742   1.00 23.93  ? 81  LEU A N   1 
ATOM   647  C  CA  . LEU A 1 82 ? 9.203   -20.873 6.764   1.00 25.72  ? 81  LEU A CA  1 
ATOM   648  C  C   . LEU A 1 82 ? 10.641  -20.427 7.059   1.00 25.91  ? 81  LEU A C   1 
ATOM   649  O  O   . LEU A 1 82 ? 10.855  -19.240 7.331   1.00 25.45  ? 81  LEU A O   1 
ATOM   650  C  CB  . LEU A 1 82 ? 8.517   -21.356 8.048   1.00 29.24  ? 81  LEU A CB  1 
ATOM   651  C  CG  . LEU A 1 82 ? 7.027   -21.698 7.911   1.00 28.14  ? 81  LEU A CG  1 
ATOM   652  C  CD1 . LEU A 1 82 ? 6.707   -22.247 9.300   1.00 33.07  ? 81  LEU A CD1 1 
ATOM   653  C  CD2 . LEU A 1 82 ? 6.188   -20.441 7.701   1.00 30.68  ? 81  LEU A CD2 1 
ATOM   654  N  N   . TRP A 1 83 ? 11.604  -21.363 6.944   1.00 26.67  ? 82  TRP A N   1 
ATOM   655  C  CA  . TRP A 1 83 ? 12.972  -20.986 7.273   1.00 27.90  ? 82  TRP A CA  1 
ATOM   656  C  C   . TRP A 1 83 ? 13.477  -20.049 6.183   1.00 24.20  ? 82  TRP A C   1 
ATOM   657  O  O   . TRP A 1 83 ? 14.138  -19.058 6.454   1.00 24.80  ? 82  TRP A O   1 
ATOM   658  C  CB  . TRP A 1 83 ? 13.885  -22.229 7.437   1.00 29.23  ? 82  TRP A CB  1 
ATOM   659  C  CG  . TRP A 1 83 ? 15.326  -21.861 7.710   1.00 26.35  ? 82  TRP A CG  1 
ATOM   660  C  CD1 . TRP A 1 83 ? 15.946  -21.799 8.924   1.00 30.24  ? 82  TRP A CD1 1 
ATOM   661  C  CD2 . TRP A 1 83 ? 16.319  -21.508 6.728   1.00 26.98  ? 82  TRP A CD2 1 
ATOM   662  N  NE1 . TRP A 1 83 ? 17.251  -21.409 8.766   1.00 29.07  ? 82  TRP A NE1 1 
ATOM   663  C  CE2 . TRP A 1 83 ? 17.507  -21.239 7.433   1.00 27.13  ? 82  TRP A CE2 1 
ATOM   664  C  CE3 . TRP A 1 83 ? 16.336  -21.410 5.331   1.00 26.32  ? 82  TRP A CE3 1 
ATOM   665  C  CZ2 . TRP A 1 83 ? 18.681  -20.861 6.788   1.00 29.11  ? 82  TRP A CZ2 1 
ATOM   666  C  CZ3 . TRP A 1 83 ? 17.489  -21.010 4.691   1.00 28.94  ? 82  TRP A CZ3 1 
ATOM   667  C  CH2 . TRP A 1 83 ? 18.658  -20.761 5.417   1.00 30.61  ? 82  TRP A CH2 1 
ATOM   668  N  N   . GLU A 1 84 ? 13.135  -20.386 4.946   1.00 23.75  ? 83  GLU A N   1 
ATOM   669  C  CA  . GLU A 1 84 ? 13.674  -19.634 3.837   1.00 23.39  ? 83  GLU A CA  1 
ATOM   670  C  C   . GLU A 1 84 ? 13.152  -18.198 3.854   1.00 24.37  ? 83  GLU A C   1 
ATOM   671  O  O   . GLU A 1 84 ? 13.887  -17.254 3.669   1.00 22.59  ? 83  GLU A O   1 
ATOM   672  C  CB  . GLU A 1 84 ? 13.279  -20.314 2.535   1.00 24.06  ? 83  GLU A CB  1 
ATOM   673  C  CG  . GLU A 1 84 ? 14.042  -21.641 2.373   1.00 23.31  ? 83  GLU A CG  1 
ATOM   674  C  CD  . GLU A 1 84 ? 13.643  -22.327 1.063   1.00 27.48  ? 83  GLU A CD  1 
ATOM   675  O  OE1 . GLU A 1 84 ? 12.716  -21.902 0.328   1.00 27.51  ? 83  GLU A OE1 1 
ATOM   676  O  OE2 . GLU A 1 84 ? 14.202  -23.429 0.797   1.00 28.43  ? 83  GLU A OE2 1 
ATOM   677  N  N   . ILE A 1 85 ? 11.828  -18.017 4.040   1.00 23.03  ? 84  ILE A N   1 
ATOM   678  C  CA  . ILE A 1 85 ? 11.277  -16.656 3.976   1.00 21.84  ? 84  ILE A CA  1 
ATOM   679  C  C   . ILE A 1 85 ? 11.820  -15.766 5.116   1.00 20.99  ? 84  ILE A C   1 
ATOM   680  O  O   . ILE A 1 85 ? 11.975  -14.560 4.951   1.00 23.70  ? 84  ILE A O   1 
ATOM   681  C  CB  . ILE A 1 85 ? 9.720   -16.706 3.937   1.00 21.26  ? 84  ILE A CB  1 
ATOM   682  C  CG1 . ILE A 1 85 ? 9.171   -15.361 3.492   1.00 23.20  ? 84  ILE A CG1 1 
ATOM   683  C  CG2 . ILE A 1 85 ? 9.167   -17.090 5.326   1.00 22.97  ? 84  ILE A CG2 1 
ATOM   684  C  CD1 . ILE A 1 85 ? 7.707   -15.469 3.074   1.00 21.78  ? 84  ILE A CD1 1 
ATOM   685  N  N   . GLN A 1 86 ? 12.095  -16.386 6.276   1.00 22.95  ? 85  GLN A N   1 
ATOM   686  C  CA  . GLN A 1 86 ? 12.649  -15.657 7.426   1.00 26.02  ? 85  GLN A CA  1 
ATOM   687  C  C   . GLN A 1 86 ? 14.145  -15.370 7.304   1.00 25.89  ? 85  GLN A C   1 
ATOM   688  O  O   . GLN A 1 86 ? 14.592  -14.268 7.722   1.00 28.47  ? 85  GLN A O   1 
ATOM   689  C  CB  . GLN A 1 86 ? 12.250  -16.402 8.710   1.00 27.13  ? 85  GLN A CB  1 
ATOM   690  C  CG  . GLN A 1 86 ? 12.670  -15.711 10.001  1.00 32.26  ? 85  GLN A CG  1 
ATOM   691  C  CD  . GLN A 1 86 ? 12.042  -16.356 11.239  1.00 36.50  ? 85  GLN A CD  1 
ATOM   692  O  OE1 . GLN A 1 86 ? 11.885  -17.586 11.343  1.00 37.13  ? 85  GLN A OE1 1 
ATOM   693  N  NE2 . GLN A 1 86 ? 11.642  -15.522 12.191  1.00 46.74  ? 85  GLN A NE2 1 
ATOM   694  N  N   . ASN A 1 87 ? 14.897  -16.294 6.703   1.00 23.42  ? 86  ASN A N   1 
ATOM   695  C  CA  . ASN A 1 87 ? 16.350  -16.290 6.804   1.00 24.67  ? 86  ASN A CA  1 
ATOM   696  C  C   . ASN A 1 87 ? 17.097  -15.920 5.529   1.00 25.69  ? 86  ASN A C   1 
ATOM   697  O  O   . ASN A 1 87 ? 18.181  -15.316 5.606   1.00 26.73  ? 86  ASN A O   1 
ATOM   698  C  CB  . ASN A 1 87 ? 16.867  -17.575 7.431   1.00 24.87  ? 86  ASN A CB  1 
ATOM   699  C  CG  . ASN A 1 87 ? 16.395  -17.660 8.860   1.00 29.68  ? 86  ASN A CG  1 
ATOM   700  O  OD1 . ASN A 1 87 ? 16.752  -16.809 9.699   1.00 33.08  ? 86  ASN A OD1 1 
ATOM   701  N  ND2 . ASN A 1 87 ? 15.492  -18.591 9.143   1.00 29.60  ? 86  ASN A ND2 1 
ATOM   702  N  N   . ASN A 1 88 ? 16.575  -16.286 4.349   1.00 23.50  ? 87  ASN A N   1 
ATOM   703  C  CA  . ASN A 1 88 ? 17.237  -15.904 3.123   1.00 23.52  ? 87  ASN A CA  1 
ATOM   704  C  C   . ASN A 1 88 ? 16.188  -15.832 2.008   1.00 23.81  ? 87  ASN A C   1 
ATOM   705  O  O   . ASN A 1 88 ? 16.193  -16.623 1.051   1.00 24.11  ? 87  ASN A O   1 
ATOM   706  C  CB  . ASN A 1 88 ? 18.364  -16.887 2.790   1.00 24.77  ? 87  ASN A CB  1 
ATOM   707  C  CG  . ASN A 1 88 ? 19.388  -16.261 1.877   1.00 27.65  ? 87  ASN A CG  1 
ATOM   708  O  OD1 . ASN A 1 88 ? 19.146  -15.248 1.209   1.00 25.29  ? 87  ASN A OD1 1 
ATOM   709  N  ND2 . ASN A 1 88 ? 20.595  -16.834 1.887   1.00 30.02  ? 87  ASN A ND2 1 
ATOM   710  N  N   . PRO A 1 89 ? 15.247  -14.874 2.106   1.00 22.92  ? 88  PRO A N   1 
ATOM   711  C  CA  . PRO A 1 89 ? 14.113  -14.873 1.176   1.00 21.16  ? 88  PRO A CA  1 
ATOM   712  C  C   . PRO A 1 89 ? 14.467  -14.420 -0.224  1.00 25.71  ? 88  PRO A C   1 
ATOM   713  O  O   . PRO A 1 89 ? 13.670  -14.657 -1.130  1.00 23.42  ? 88  PRO A O   1 
ATOM   714  C  CB  . PRO A 1 89 ? 13.199  -13.873 1.853   1.00 23.01  ? 88  PRO A CB  1 
ATOM   715  C  CG  . PRO A 1 89 ? 14.081  -12.874 2.560   1.00 23.33  ? 88  PRO A CG  1 
ATOM   716  C  CD  . PRO A 1 89 ? 15.066  -13.874 3.157   1.00 22.42  ? 88  PRO A CD  1 
ATOM   717  N  N   . HIS A 1 90 ? 15.691  -13.865 -0.422  1.00 21.58  ? 89  HIS A N   1 
ATOM   718  C  CA  . HIS A 1 90 ? 15.995  -13.345 -1.764  1.00 21.48  ? 89  HIS A CA  1 
ATOM   719  C  C   . HIS A 1 90 ? 17.094  -14.156 -2.474  1.00 22.53  ? 89  HIS A C   1 
ATOM   720  O  O   . HIS A 1 90 ? 17.542  -13.721 -3.551  1.00 24.81  ? 89  HIS A O   1 
ATOM   721  C  CB  . HIS A 1 90 ? 16.360  -11.847 -1.696  1.00 21.36  ? 89  HIS A CB  1 
ATOM   722  C  CG  . HIS A 1 90 ? 15.297  -11.003 -1.108  1.00 23.86  ? 89  HIS A CG  1 
ATOM   723  N  ND1 . HIS A 1 90 ? 14.033  -10.902 -1.691  1.00 22.78  ? 89  HIS A ND1 1 
ATOM   724  C  CD2 . HIS A 1 90 ? 15.282  -10.294 0.005   1.00 22.29  ? 89  HIS A CD2 1 
ATOM   725  C  CE1 . HIS A 1 90 ? 13.290  -10.064 -0.952  1.00 21.34  ? 89  HIS A CE1 1 
ATOM   726  N  NE2 . HIS A 1 90 ? 14.026  -9.721  0.125   1.00 22.97  ? 89  HIS A NE2 1 
ATOM   727  N  N   . ALA A 1 91 ? 17.375  -15.336 -1.953  1.00 24.37  ? 90  ALA A N   1 
ATOM   728  C  CA  . ALA A 1 91 ? 18.440  -16.198 -2.500  1.00 24.86  ? 90  ALA A CA  1 
ATOM   729  C  C   . ALA A 1 91 ? 17.975  -16.910 -3.767  1.00 28.85  ? 90  ALA A C   1 
ATOM   730  O  O   . ALA A 1 91 ? 16.784  -17.002 -4.080  1.00 27.67  ? 90  ALA A O   1 
ATOM   731  C  CB  . ALA A 1 91 ? 18.910  -17.181 -1.453  1.00 25.22  ? 90  ALA A CB  1 
ATOM   732  N  N   . SER A 1 92 ? 18.961  -17.434 -4.529  1.00 27.11  ? 91  SER A N   1 
ATOM   733  C  CA  . SER A 1 92 ? 18.679  -18.333 -5.617  1.00 31.21  ? 91  SER A CA  1 
ATOM   734  C  C   . SER A 1 92 ? 18.423  -19.712 -5.032  1.00 34.38  ? 91  SER A C   1 
ATOM   735  O  O   . SER A 1 92 ? 19.256  -20.262 -4.309  1.00 34.87  ? 91  SER A O   1 
ATOM   736  C  CB  . SER A 1 92 ? 19.873  -18.363 -6.564  1.00 34.39  ? 91  SER A CB  1 
ATOM   737  O  OG  . SER A 1 92 ? 19.662  -19.480 -7.410  1.00 36.83  ? 91  SER A OG  1 
ATOM   738  N  N   . TYR A 1 93 ? 17.264  -20.279 -5.378  1.00 30.34  ? 92  TYR A N   1 
ATOM   739  C  CA  . TYR A 1 93 ? 16.867  -21.597 -4.941  1.00 31.73  ? 92  TYR A CA  1 
ATOM   740  C  C   . TYR A 1 93 ? 16.876  -22.529 -6.145  1.00 40.71  ? 92  TYR A C   1 
ATOM   741  O  O   . TYR A 1 93 ? 16.318  -23.612 -6.068  1.00 45.27  ? 92  TYR A O   1 
ATOM   742  C  CB  . TYR A 1 93 ? 15.522  -21.570 -4.187  1.00 29.58  ? 92  TYR A CB  1 
ATOM   743  C  CG  . TYR A 1 93 ? 15.680  -20.997 -2.788  1.00 27.13  ? 92  TYR A CG  1 
ATOM   744  C  CD1 . TYR A 1 93 ? 16.141  -21.777 -1.726  1.00 28.92  ? 92  TYR A CD1 1 
ATOM   745  C  CD2 . TYR A 1 93 ? 15.319  -19.669 -2.531  1.00 26.72  ? 92  TYR A CD2 1 
ATOM   746  C  CE1 . TYR A 1 93 ? 16.303  -21.220 -0.458  1.00 33.41  ? 92  TYR A CE1 1 
ATOM   747  C  CE2 . TYR A 1 93 ? 15.470  -19.111 -1.274  1.00 27.16  ? 92  TYR A CE2 1 
ATOM   748  C  CZ  . TYR A 1 93 ? 15.957  -19.888 -0.242  1.00 27.68  ? 92  TYR A CZ  1 
ATOM   749  O  OH  . TYR A 1 93 ? 16.183  -19.410 1.014   1.00 29.66  ? 92  TYR A OH  1 
ATOM   750  N  N   . SER A 1 94 ? 17.600  -22.119 -7.196  1.00 45.99  ? 93  SER A N   1 
ATOM   751  C  CA  . SER A 1 94 ? 17.687  -22.875 -8.438  1.00 60.23  ? 93  SER A CA  1 
ATOM   752  C  C   . SER A 1 94 ? 18.786  -23.948 -8.367  1.00 70.46  ? 93  SER A C   1 
ATOM   753  O  O   . SER A 1 94 ? 19.435  -24.051 -7.302  1.00 74.27  ? 93  SER A O   1 
ATOM   754  C  CB  . SER A 1 94 ? 17.883  -21.959 -9.617  1.00 60.25  ? 93  SER A CB  1 
ATOM   755  O  OG  . SER A 1 94 ? 16.619  -21.652 -10.193 1.00 58.58  ? 93  SER A OG  1 
ATOM   756  O  OXT . SER A 1 94 ? 18.943  -24.668 -9.384  1.00 80.25  ? 93  SER A OXT 1 
ATOM   757  N  N   . MET B 1 2  ? 38.923  -11.408 -42.718 1.00 70.74  ? 1   MET B N   1 
ATOM   758  C  CA  . MET B 1 2  ? 38.474  -12.287 -43.829 1.00 68.61  ? 1   MET B CA  1 
ATOM   759  C  C   . MET B 1 2  ? 36.948  -12.350 -43.804 1.00 60.24  ? 1   MET B C   1 
ATOM   760  O  O   . MET B 1 2  ? 36.376  -12.633 -42.755 1.00 71.42  ? 1   MET B O   1 
ATOM   761  C  CB  . MET B 1 2  ? 39.073  -13.692 -43.662 1.00 80.56  ? 1   MET B CB  1 
ATOM   762  C  CG  . MET B 1 2  ? 39.157  -14.544 -44.933 1.00 91.13  ? 1   MET B CG  1 
ATOM   763  S  SD  . MET B 1 2  ? 40.157  -13.921 -46.306 1.00 89.18  ? 1   MET B SD  1 
ATOM   764  C  CE  . MET B 1 2  ? 41.603  -13.175 -45.536 1.00 82.94  ? 1   MET B CE  1 
ATOM   765  N  N   . PRO B 1 3  ? 36.235  -12.055 -44.923 1.00 53.03  ? 2   PRO B N   1 
ATOM   766  C  CA  . PRO B 1 3  ? 34.782  -12.247 -44.975 1.00 54.44  ? 2   PRO B CA  1 
ATOM   767  C  C   . PRO B 1 3  ? 34.483  -13.691 -44.583 1.00 53.58  ? 2   PRO B C   1 
ATOM   768  O  O   . PRO B 1 3  ? 35.292  -14.565 -44.872 1.00 48.82  ? 2   PRO B O   1 
ATOM   769  C  CB  . PRO B 1 3  ? 34.415  -11.942 -46.431 1.00 54.43  ? 2   PRO B CB  1 
ATOM   770  C  CG  . PRO B 1 3  ? 35.516  -11.001 -46.883 1.00 48.43  ? 2   PRO B CG  1 
ATOM   771  C  CD  . PRO B 1 3  ? 36.772  -11.471 -46.166 1.00 46.73  ? 2   PRO B CD  1 
ATOM   772  N  N   . HIS B 1 4  ? 33.377  -13.901 -43.852 1.00 49.94  ? 3   HIS B N   1 
ATOM   773  C  CA  . HIS B 1 4  ? 32.910  -15.236 -43.498 1.00 47.62  ? 3   HIS B CA  1 
ATOM   774  C  C   . HIS B 1 4  ? 31.518  -15.453 -44.090 1.00 44.00  ? 3   HIS B C   1 
ATOM   775  O  O   . HIS B 1 4  ? 30.969  -14.561 -44.732 1.00 45.66  ? 3   HIS B O   1 
ATOM   776  C  CB  . HIS B 1 4  ? 33.021  -15.468 -41.986 1.00 55.60  ? 3   HIS B CB  1 
ATOM   777  C  CG  . HIS B 1 4  ? 34.429  -15.472 -41.483 1.00 67.37  ? 3   HIS B CG  1 
ATOM   778  N  ND1 . HIS B 1 4  ? 35.422  -16.260 -42.033 1.00 68.04  ? 3   HIS B ND1 1 
ATOM   779  C  CD2 . HIS B 1 4  ? 35.007  -14.803 -40.463 1.00 64.06  ? 3   HIS B CD2 1 
ATOM   780  C  CE1 . HIS B 1 4  ? 36.558  -16.053 -41.375 1.00 64.63  ? 3   HIS B CE1 1 
ATOM   781  N  NE2 . HIS B 1 4  ? 36.330  -15.171 -40.419 1.00 69.56  ? 3   HIS B NE2 1 
ATOM   782  N  N   . ALA B 1 5  ? 30.951  -16.654 -43.890 1.00 39.72  ? 4   ALA B N   1 
ATOM   783  C  CA  . ALA B 1 5  ? 29.643  -16.988 -44.431 1.00 41.06  ? 4   ALA B CA  1 
ATOM   784  C  C   . ALA B 1 5  ? 28.630  -15.954 -43.955 1.00 38.28  ? 4   ALA B C   1 
ATOM   785  O  O   . ALA B 1 5  ? 27.760  -15.523 -44.710 1.00 47.25  ? 4   ALA B O   1 
ATOM   786  C  CB  . ALA B 1 5  ? 29.254  -18.357 -43.945 1.00 45.08  ? 4   ALA B CB  1 
ATOM   787  N  N   . PHE B 1 6  ? 28.746  -15.609 -42.676 1.00 44.86  ? 5   PHE B N   1 
ATOM   788  C  CA  . PHE B 1 6  ? 27.940  -14.572 -42.059 1.00 42.73  ? 5   PHE B CA  1 
ATOM   789  C  C   . PHE B 1 6  ? 28.809  -13.346 -41.819 1.00 44.07  ? 5   PHE B C   1 
ATOM   790  O  O   . PHE B 1 6  ? 29.971  -13.474 -41.424 1.00 43.85  ? 5   PHE B O   1 
ATOM   791  C  CB  . PHE B 1 6  ? 27.541  -15.034 -40.653 1.00 43.28  ? 5   PHE B CB  1 
ATOM   792  C  CG  . PHE B 1 6  ? 26.483  -16.122 -40.708 1.00 39.30  ? 5   PHE B CG  1 
ATOM   793  C  CD1 . PHE B 1 6  ? 25.148  -15.772 -40.873 1.00 36.10  ? 5   PHE B CD1 1 
ATOM   794  C  CD2 . PHE B 1 6  ? 26.816  -17.472 -40.627 1.00 36.04  ? 5   PHE B CD2 1 
ATOM   795  C  CE1 . PHE B 1 6  ? 24.157  -16.730 -40.954 1.00 39.25  ? 5   PHE B CE1 1 
ATOM   796  C  CE2 . PHE B 1 6  ? 25.809  -18.429 -40.699 1.00 35.01  ? 5   PHE B CE2 1 
ATOM   797  C  CZ  . PHE B 1 6  ? 24.489  -18.067 -40.840 1.00 35.44  ? 5   PHE B CZ  1 
ATOM   798  N  N   . LYS B 1 7  ? 28.215  -12.175 -42.057 1.00 45.51  ? 6   LYS B N   1 
ATOM   799  C  CA  . LYS B 1 7  ? 28.943  -10.939 -41.825 1.00 43.15  ? 6   LYS B CA  1 
ATOM   800  C  C   . LYS B 1 7  ? 28.178  -10.097 -40.802 1.00 44.70  ? 6   LYS B C   1 
ATOM   801  O  O   . LYS B 1 7  ? 26.938  -10.171 -40.732 1.00 40.92  ? 6   LYS B O   1 
ATOM   802  C  CB  . LYS B 1 7  ? 29.099  -10.233 -43.171 1.00 45.49  ? 6   LYS B CB  1 
ATOM   803  C  CG  . LYS B 1 7  ? 27.791  -9.819  -43.828 1.00 44.96  ? 6   LYS B CG  1 
ATOM   804  C  CD  . LYS B 1 7  ? 27.959  -9.156  -45.194 1.00 53.24  ? 6   LYS B CD  1 
ATOM   805  C  CE  . LYS B 1 7  ? 26.641  -8.763  -45.797 1.00 50.56  ? 6   LYS B CE  1 
ATOM   806  N  NZ  . LYS B 1 7  ? 25.845  -9.947  -46.134 1.00 57.26  ? 6   LYS B NZ  1 
ATOM   807  N  N   . PRO B 1 8  ? 28.890  -9.229  -40.037 1.00 49.36  ? 7   PRO B N   1 
ATOM   808  C  CA  . PRO B 1 8  ? 28.273  -8.177  -39.217 1.00 39.90  ? 7   PRO B CA  1 
ATOM   809  C  C   . PRO B 1 8  ? 27.088  -7.517  -39.898 1.00 38.50  ? 7   PRO B C   1 
ATOM   810  O  O   . PRO B 1 8  ? 27.164  -7.082  -41.062 1.00 41.52  ? 7   PRO B O   1 
ATOM   811  C  CB  . PRO B 1 8  ? 29.497  -7.262  -39.152 1.00 42.60  ? 7   PRO B CB  1 
ATOM   812  C  CG  . PRO B 1 8  ? 30.602  -8.240  -38.821 1.00 45.02  ? 7   PRO B CG  1 
ATOM   813  C  CD  . PRO B 1 8  ? 30.363  -9.192  -39.954 1.00 46.93  ? 7   PRO B CD  1 
ATOM   814  N  N   . GLY B 1 9  ? 25.964  -7.528  -39.177 1.00 35.29  ? 8   GLY B N   1 
ATOM   815  C  CA  . GLY B 1 9  ? 24.740  -6.875  -39.599 1.00 34.63  ? 8   GLY B CA  1 
ATOM   816  C  C   . GLY B 1 9  ? 23.774  -7.842  -40.267 1.00 31.04  ? 8   GLY B C   1 
ATOM   817  O  O   . GLY B 1 9  ? 22.641  -7.468  -40.561 1.00 33.14  ? 8   GLY B O   1 
ATOM   818  N  N   . ASP B 1 10 ? 24.243  -9.081  -40.555 1.00 31.13  ? 9   ASP B N   1 
ATOM   819  C  CA  . ASP B 1 10 ? 23.331  -10.073 -41.114 1.00 32.11  ? 9   ASP B CA  1 
ATOM   820  C  C   . ASP B 1 10 ? 22.258  -10.406 -40.063 1.00 27.02  ? 9   ASP B C   1 
ATOM   821  O  O   . ASP B 1 10 ? 22.576  -10.454 -38.873 1.00 32.51  ? 9   ASP B O   1 
ATOM   822  C  CB  . ASP B 1 10 ? 23.998  -11.393 -41.467 1.00 32.12  ? 9   ASP B CB  1 
ATOM   823  C  CG  . ASP B 1 10 ? 24.778  -11.421 -42.777 1.00 41.79  ? 9   ASP B CG  1 
ATOM   824  O  OD1 . ASP B 1 10 ? 24.520  -10.523 -43.610 1.00 42.28  ? 9   ASP B OD1 1 
ATOM   825  O  OD2 . ASP B 1 10 ? 25.615  -12.354 -42.932 1.00 39.43  ? 9   ASP B OD2 1 
ATOM   826  N  N   . LEU B 1 11 ? 21.039  -10.543 -40.531 1.00 28.19  ? 10  LEU B N   1 
ATOM   827  C  CA  . LEU B 1 11 ? 19.891  -10.772 -39.644 1.00 28.06  ? 10  LEU B CA  1 
ATOM   828  C  C   . LEU B 1 11 ? 19.607  -12.268 -39.663 1.00 30.30  ? 10  LEU B C   1 
ATOM   829  O  O   . LEU B 1 11 ? 19.615  -12.859 -40.743 1.00 30.90  ? 10  LEU B O   1 
ATOM   830  C  CB  . LEU B 1 11 ? 18.673  -9.968  -40.088 1.00 29.26  ? 10  LEU B CB  1 
ATOM   831  C  CG  . LEU B 1 11 ? 18.944  -8.464  -40.233 1.00 29.07  ? 10  LEU B CG  1 
ATOM   832  C  CD1 . LEU B 1 11 ? 17.677  -7.763  -40.611 1.00 29.94  ? 10  LEU B CD1 1 
ATOM   833  C  CD2 . LEU B 1 11 ? 19.619  -7.912  -38.991 1.00 29.27  ? 10  LEU B CD2 1 
ATOM   834  N  N   . VAL B 1 12 ? 19.209  -12.839 -38.492 1.00 28.03  ? 11  VAL B N   1 
ATOM   835  C  CA  . VAL B 1 12 ? 19.022  -14.291 -38.384 1.00 26.80  ? 11  VAL B CA  1 
ATOM   836  C  C   . VAL B 1 12 ? 17.980  -14.544 -37.307 1.00 31.25  ? 11  VAL B C   1 
ATOM   837  O  O   . VAL B 1 12 ? 17.639  -13.626 -36.567 1.00 29.11  ? 11  VAL B O   1 
ATOM   838  C  CB  . VAL B 1 12 ? 20.308  -14.997 -37.923 1.00 26.55  ? 11  VAL B CB  1 
ATOM   839  C  CG1 . VAL B 1 12 ? 21.442  -14.871 -38.959 1.00 28.59  ? 11  VAL B CG1 1 
ATOM   840  C  CG2 . VAL B 1 12 ? 20.825  -14.569 -36.541 1.00 29.30  ? 11  VAL B CG2 1 
ATOM   841  N  N   . PHE B 1 13 ? 17.497  -15.794 -37.251 1.00 29.37  ? 12  PHE B N   1 
ATOM   842  C  CA  . PHE B 1 13 ? 16.980  -16.328 -35.993 1.00 28.76  ? 12  PHE B CA  1 
ATOM   843  C  C   . PHE B 1 13 ? 18.073  -17.209 -35.416 1.00 26.99  ? 12  PHE B C   1 
ATOM   844  O  O   . PHE B 1 13 ? 18.679  -17.990 -36.172 1.00 27.99  ? 12  PHE B O   1 
ATOM   845  C  CB  . PHE B 1 13 ? 15.756  -17.182 -36.257 1.00 29.34  ? 12  PHE B CB  1 
ATOM   846  C  CG  . PHE B 1 13 ? 14.547  -16.337 -36.636 1.00 28.60  ? 12  PHE B CG  1 
ATOM   847  C  CD1 . PHE B 1 13 ? 14.281  -16.019 -37.972 1.00 33.41  ? 12  PHE B CD1 1 
ATOM   848  C  CD2 . PHE B 1 13 ? 13.661  -15.905 -35.655 1.00 30.59  ? 12  PHE B CD2 1 
ATOM   849  C  CE1 . PHE B 1 13 ? 13.176  -15.255 -38.290 1.00 36.48  ? 12  PHE B CE1 1 
ATOM   850  C  CE2 . PHE B 1 13 ? 12.544  -15.149 -35.977 1.00 34.95  ? 12  PHE B CE2 1 
ATOM   851  C  CZ  . PHE B 1 13 ? 12.303  -14.831 -37.300 1.00 38.01  ? 12  PHE B CZ  1 
ATOM   852  N  N   . ALA B 1 14 ? 18.353  -17.058 -34.096 1.00 25.58  ? 13  ALA B N   1 
ATOM   853  C  CA  . ALA B 1 14 ? 19.401  -17.786 -33.407 1.00 27.07  ? 13  ALA B CA  1 
ATOM   854  C  C   . ALA B 1 14 ? 18.780  -18.739 -32.386 1.00 29.21  ? 13  ALA B C   1 
ATOM   855  O  O   . ALA B 1 14 ? 17.824  -18.365 -31.700 1.00 31.89  ? 13  ALA B O   1 
ATOM   856  C  CB  . ALA B 1 14 ? 20.373  -16.840 -32.726 1.00 29.51  ? 13  ALA B CB  1 
ATOM   857  N  N   . LYS B 1 15 ? 19.300  -19.971 -32.357 1.00 27.78  ? 14  LYS B N   1 
ATOM   858  C  CA  . LYS B 1 15 ? 18.676  -20.999 -31.519 1.00 28.96  ? 14  LYS B CA  1 
ATOM   859  C  C   . LYS B 1 15 ? 19.581  -21.306 -30.334 1.00 30.51  ? 14  LYS B C   1 
ATOM   860  O  O   . LYS B 1 15 ? 20.780  -21.599 -30.456 1.00 33.45  ? 14  LYS B O   1 
ATOM   861  C  CB  . LYS B 1 15 ? 18.353  -22.237 -32.376 1.00 29.51  ? 14  LYS B CB  1 
ATOM   862  C  CG  . LYS B 1 15 ? 17.756  -23.413 -31.497 1.00 30.85  ? 14  LYS B CG  1 
ATOM   863  C  CD  . LYS B 1 15 ? 16.295  -23.083 -31.250 1.00 31.92  ? 14  LYS B CD  1 
ATOM   864  C  CE  . LYS B 1 15 ? 15.442  -24.155 -30.522 1.00 33.41  ? 14  LYS B CE  1 
ATOM   865  N  NZ  . LYS B 1 15 ? 15.932  -24.382 -29.169 1.00 32.46  ? 14  LYS B NZ  1 
ATOM   866  N  N   . MET B 1 16 ? 18.995  -21.164 -29.143 1.00 29.54  ? 15  MET B N   1 
ATOM   867  C  CA  . MET B 1 16 ? 19.625  -21.593 -27.900 1.00 33.74  ? 15  MET B CA  1 
ATOM   868  C  C   . MET B 1 16 ? 18.745  -22.642 -27.221 1.00 34.40  ? 15  MET B C   1 
ATOM   869  O  O   . MET B 1 16 ? 17.516  -22.553 -27.236 1.00 33.25  ? 15  MET B O   1 
ATOM   870  C  CB  . MET B 1 16 ? 19.753  -20.417 -26.924 1.00 35.77  ? 15  MET B CB  1 
ATOM   871  C  CG  . MET B 1 16 ? 20.443  -19.200 -27.494 1.00 41.01  ? 15  MET B CG  1 
ATOM   872  S  SD  . MET B 1 16 ? 22.214  -19.158 -27.167 1.00 44.57  ? 15  MET B SD  1 
ATOM   873  C  CE  . MET B 1 16 ? 22.229  -19.099 -25.369 1.00 43.83  ? 15  MET B CE  1 
ATOM   874  N  N   . LYS B 1 17 ? 19.407  -23.561 -26.506 1.00 36.69  ? 16  LYS B N   1 
ATOM   875  C  CA  . LYS B 1 17 ? 18.668  -24.621 -25.841 1.00 36.42  ? 16  LYS B CA  1 
ATOM   876  C  C   . LYS B 1 17 ? 17.724  -23.986 -24.818 1.00 32.75  ? 16  LYS B C   1 
ATOM   877  O  O   . LYS B 1 17 ? 18.126  -23.117 -24.060 1.00 36.52  ? 16  LYS B O   1 
ATOM   878  C  CB  . LYS B 1 17 ? 19.684  -25.533 -25.143 1.00 42.27  ? 16  LYS B CB  1 
ATOM   879  C  CG  . LYS B 1 17 ? 19.041  -26.613 -24.249 1.00 42.76  ? 16  LYS B CG  1 
ATOM   880  C  CD  . LYS B 1 17 ? 19.980  -27.650 -23.645 1.00 52.35  ? 16  LYS B CD  1 
ATOM   881  N  N   . GLY B 1 18 ? 16.477  -24.433 -24.796 1.00 38.08  ? 17  GLY B N   1 
ATOM   882  C  CA  . GLY B 1 18 ? 15.511  -23.900 -23.845 1.00 40.53  ? 17  GLY B CA  1 
ATOM   883  C  C   . GLY B 1 18 ? 14.658  -22.775 -24.438 1.00 39.91  ? 17  GLY B C   1 
ATOM   884  O  O   . GLY B 1 18 ? 13.715  -22.298 -23.803 1.00 36.13  ? 17  GLY B O   1 
ATOM   885  N  N   . TYR B 1 19 ? 14.980  -22.313 -25.663 1.00 31.03  ? 18  TYR B N   1 
ATOM   886  C  CA  . TYR B 1 19 ? 14.296  -21.116 -26.124 1.00 28.62  ? 18  TYR B CA  1 
ATOM   887  C  C   . TYR B 1 19 ? 13.851  -21.303 -27.570 1.00 29.66  ? 18  TYR B C   1 
ATOM   888  O  O   . TYR B 1 19 ? 14.500  -22.074 -28.264 1.00 32.83  ? 18  TYR B O   1 
ATOM   889  C  CB  . TYR B 1 19 ? 15.241  -19.908 -26.138 1.00 30.50  ? 18  TYR B CB  1 
ATOM   890  C  CG  . TYR B 1 19 ? 15.721  -19.527 -24.746 1.00 36.30  ? 18  TYR B CG  1 
ATOM   891  C  CD1 . TYR B 1 19 ? 14.967  -18.674 -23.933 1.00 34.95  ? 18  TYR B CD1 1 
ATOM   892  C  CD2 . TYR B 1 19 ? 16.852  -20.129 -24.205 1.00 34.11  ? 18  TYR B CD2 1 
ATOM   893  C  CE1 . TYR B 1 19 ? 15.387  -18.370 -22.641 1.00 35.90  ? 18  TYR B CE1 1 
ATOM   894  C  CE2 . TYR B 1 19 ? 17.276  -19.824 -22.918 1.00 39.74  ? 18  TYR B CE2 1 
ATOM   895  C  CZ  . TYR B 1 19 ? 16.531  -18.961 -22.130 1.00 36.13  ? 18  TYR B CZ  1 
ATOM   896  O  OH  . TYR B 1 19 ? 17.023  -18.679 -20.872 1.00 40.71  ? 18  TYR B OH  1 
ATOM   897  N  N   . PRO B 1 20 ? 12.797  -20.629 -28.081 1.00 30.38  ? 19  PRO B N   1 
ATOM   898  C  CA  . PRO B 1 20 ? 12.445  -20.723 -29.499 1.00 28.65  ? 19  PRO B CA  1 
ATOM   899  C  C   . PRO B 1 20 ? 13.500  -19.965 -30.315 1.00 27.67  ? 19  PRO B C   1 
ATOM   900  O  O   . PRO B 1 20 ? 14.183  -19.101 -29.794 1.00 29.06  ? 19  PRO B O   1 
ATOM   901  C  CB  . PRO B 1 20 ? 11.050  -20.095 -29.598 1.00 33.15  ? 19  PRO B CB  1 
ATOM   902  C  CG  . PRO B 1 20 ? 11.046  -19.064 -28.498 1.00 33.67  ? 19  PRO B CG  1 
ATOM   903  C  CD  . PRO B 1 20 ? 11.844  -19.754 -27.372 1.00 31.57  ? 19  PRO B CD  1 
ATOM   904  N  N   . HIS B 1 21 ? 13.617  -20.348 -31.581 1.00 29.42  ? 20  HIS B N   1 
ATOM   905  C  CA  . HIS B 1 21 ? 14.449  -19.596 -32.516 1.00 28.97  ? 20  HIS B CA  1 
ATOM   906  C  C   . HIS B 1 21 ? 14.172  -18.094 -32.376 1.00 27.76  ? 20  HIS B C   1 
ATOM   907  O  O   . HIS B 1 21 ? 13.020  -17.667 -32.441 1.00 27.68  ? 20  HIS B O   1 
ATOM   908  C  CB  . HIS B 1 21 ? 14.108  -20.084 -33.929 1.00 28.11  ? 20  HIS B CB  1 
ATOM   909  C  CG  . HIS B 1 21 ? 14.384  -21.548 -34.149 1.00 31.19  ? 20  HIS B CG  1 
ATOM   910  N  ND1 . HIS B 1 21 ? 13.567  -22.590 -33.713 1.00 33.34  ? 20  HIS B ND1 1 
ATOM   911  C  CD2 . HIS B 1 21 ? 15.428  -22.136 -34.774 1.00 32.90  ? 20  HIS B CD2 1 
ATOM   912  C  CE1 . HIS B 1 21 ? 14.125  -23.752 -34.047 1.00 33.06  ? 20  HIS B CE1 1 
ATOM   913  N  NE2 . HIS B 1 21 ? 15.241  -23.514 -34.707 1.00 31.53  ? 20  HIS B NE2 1 
ATOM   914  N  N   . TRP B 1 22 ? 15.236  -17.299 -32.195 1.00 26.40  ? 21  TRP B N   1 
ATOM   915  C  CA  . TRP B 1 22 ? 15.043  -15.968 -31.620 1.00 26.32  ? 21  TRP B CA  1 
ATOM   916  C  C   . TRP B 1 22 ? 15.540  -14.910 -32.605 1.00 28.82  ? 21  TRP B C   1 
ATOM   917  O  O   . TRP B 1 22 ? 16.702  -15.044 -33.019 1.00 27.12  ? 21  TRP B O   1 
ATOM   918  C  CB  . TRP B 1 22 ? 15.822  -15.850 -30.299 1.00 28.99  ? 21  TRP B CB  1 
ATOM   919  C  CG  . TRP B 1 22 ? 15.320  -14.706 -29.443 1.00 27.62  ? 21  TRP B CG  1 
ATOM   920  C  CD1 . TRP B 1 22 ? 15.599  -13.371 -29.582 1.00 28.76  ? 21  TRP B CD1 1 
ATOM   921  C  CD2 . TRP B 1 22 ? 14.362  -14.785 -28.338 1.00 28.26  ? 21  TRP B CD2 1 
ATOM   922  N  NE1 . TRP B 1 22 ? 14.922  -12.630 -28.634 1.00 31.19  ? 21  TRP B NE1 1 
ATOM   923  C  CE2 . TRP B 1 22 ? 14.176  -13.476 -27.854 1.00 26.92  ? 21  TRP B CE2 1 
ATOM   924  C  CE3 . TRP B 1 22 ? 13.694  -15.856 -27.715 1.00 33.42  ? 21  TRP B CE3 1 
ATOM   925  C  CZ2 . TRP B 1 22 ? 13.318  -13.172 -26.785 1.00 30.48  ? 21  TRP B CZ2 1 
ATOM   926  C  CZ3 . TRP B 1 22 ? 12.867  -15.566 -26.650 1.00 32.04  ? 21  TRP B CZ3 1 
ATOM   927  C  CH2 . TRP B 1 22 ? 12.663  -14.250 -26.224 1.00 32.35  ? 21  TRP B CH2 1 
ATOM   928  N  N   . PRO B 1 23 ? 14.791  -13.805 -32.893 1.00 26.83  ? 22  PRO B N   1 
ATOM   929  C  CA  . PRO B 1 23 ? 15.275  -12.775 -33.839 1.00 25.61  ? 22  PRO B CA  1 
ATOM   930  C  C   . PRO B 1 23 ? 16.588  -12.162 -33.348 1.00 25.98  ? 22  PRO B C   1 
ATOM   931  O  O   . PRO B 1 23 ? 16.700  -11.765 -32.180 1.00 27.54  ? 22  PRO B O   1 
ATOM   932  C  CB  . PRO B 1 23 ? 14.139  -11.735 -33.927 1.00 26.06  ? 22  PRO B CB  1 
ATOM   933  C  CG  . PRO B 1 23 ? 13.416  -11.927 -32.564 1.00 27.20  ? 22  PRO B CG  1 
ATOM   934  C  CD  . PRO B 1 23 ? 13.455  -13.479 -32.352 1.00 26.53  ? 22  PRO B CD  1 
ATOM   935  N  N   . ALA B 1 24 ? 17.626  -12.063 -34.199 1.00 26.38  ? 23  ALA B N   1 
ATOM   936  C  CA  . ALA B 1 24 ? 18.961  -11.730 -33.714 1.00 24.71  ? 23  ALA B CA  1 
ATOM   937  C  C   . ALA B 1 24 ? 19.799  -11.170 -34.880 1.00 27.29  ? 23  ALA B C   1 
ATOM   938  O  O   . ALA B 1 24 ? 19.345  -11.194 -36.027 1.00 29.82  ? 23  ALA B O   1 
ATOM   939  C  CB  . ALA B 1 24 ? 19.673  -12.906 -33.022 1.00 28.56  ? 23  ALA B CB  1 
ATOM   940  N  N   . ARG B 1 25 ? 20.951  -10.595 -34.523 1.00 29.54  ? 24  ARG B N   1 
ATOM   941  C  CA  . ARG B 1 25 ? 21.844  -10.123 -35.581 1.00 29.69  ? 24  ARG B CA  1 
ATOM   942  C  C   . ARG B 1 25 ? 23.254  -10.582 -35.276 1.00 29.94  ? 24  ARG B C   1 
ATOM   943  O  O   . ARG B 1 25 ? 23.638  -10.820 -34.155 1.00 29.30  ? 24  ARG B O   1 
ATOM   944  C  CB  . ARG B 1 25 ? 21.804  -8.609  -35.767 1.00 28.95  ? 24  ARG B CB  1 
ATOM   945  C  CG  . ARG B 1 25 ? 22.406  -7.866  -34.588 1.00 28.92  ? 24  ARG B CG  1 
ATOM   946  C  CD  . ARG B 1 25 ? 22.176  -6.340  -34.742 1.00 28.43  ? 24  ARG B CD  1 
ATOM   947  N  NE  . ARG B 1 25 ? 22.758  -5.654  -33.590 1.00 30.75  ? 24  ARG B NE  1 
ATOM   948  C  CZ  . ARG B 1 25 ? 22.475  -4.386  -33.206 1.00 32.86  ? 24  ARG B CZ  1 
ATOM   949  N  NH1 . ARG B 1 25 ? 21.535  -3.708  -33.837 1.00 32.60  ? 24  ARG B NH1 1 
ATOM   950  N  NH2 . ARG B 1 25 ? 23.105  -3.847  -32.171 1.00 34.35  ? 24  ARG B NH2 1 
ATOM   951  N  N   . ILE B 1 26 ? 24.071  -10.683 -36.332 1.00 29.26  ? 25  ILE B N   1 
ATOM   952  C  CA  . ILE B 1 26 ? 25.493  -10.863 -36.118 1.00 31.00  ? 25  ILE B CA  1 
ATOM   953  C  C   . ILE B 1 26 ? 26.057  -9.484  -35.786 1.00 34.70  ? 25  ILE B C   1 
ATOM   954  O  O   . ILE B 1 26 ? 25.780  -8.538  -36.530 1.00 38.91  ? 25  ILE B O   1 
ATOM   955  C  CB  . ILE B 1 26 ? 26.169  -11.337 -37.410 1.00 33.86  ? 25  ILE B CB  1 
ATOM   956  C  CG1 . ILE B 1 26 ? 25.475  -12.543 -38.033 1.00 35.28  ? 25  ILE B CG1 1 
ATOM   957  C  CG2 . ILE B 1 26 ? 27.652  -11.601 -37.138 1.00 39.87  ? 25  ILE B CG2 1 
ATOM   958  C  CD1 . ILE B 1 26 ? 25.423  -13.751 -37.113 1.00 36.76  ? 25  ILE B CD1 1 
ATOM   959  N  N   . ASP B 1 27 ? 26.858  -9.434  -34.721 1.00 33.02  ? 26  ASP B N   1 
ATOM   960  C  CA  . ASP B 1 27 ? 27.523  -8.204  -34.294 1.00 42.66  ? 26  ASP B CA  1 
ATOM   961  C  C   . ASP B 1 27 ? 28.967  -8.123  -34.785 1.00 49.24  ? 26  ASP B C   1 
ATOM   962  O  O   . ASP B 1 27 ? 29.519  -9.109  -35.257 1.00 45.64  ? 26  ASP B O   1 
ATOM   963  C  CB  . ASP B 1 27 ? 27.481  -8.091  -32.786 1.00 39.50  ? 26  ASP B CB  1 
ATOM   964  C  CG  . ASP B 1 27 ? 26.289  -7.338  -32.216 1.00 42.21  ? 26  ASP B CG  1 
ATOM   965  O  OD1 . ASP B 1 27 ? 25.502  -6.779  -33.017 1.00 44.60  ? 26  ASP B OD1 1 
ATOM   966  O  OD2 . ASP B 1 27 ? 26.208  -7.287  -30.968 1.00 40.66  ? 26  ASP B OD2 1 
ATOM   967  N  N   A ASP B 1 28 ? 29.551  -6.920  -34.660 0.50 54.67  ? 27  ASP B N   1 
ATOM   968  N  N   B ASP B 1 28 ? 29.569  -6.933  -34.666 0.50 54.99  ? 27  ASP B N   1 
ATOM   969  C  CA  A ASP B 1 28 ? 30.968  -6.650  -34.853 0.50 59.43  ? 27  ASP B CA  1 
ATOM   970  C  CA  B ASP B 1 28 ? 30.990  -6.775  -34.926 0.50 60.25  ? 27  ASP B CA  1 
ATOM   971  C  C   A ASP B 1 28 ? 31.748  -7.110  -33.620 0.50 60.73  ? 27  ASP B C   1 
ATOM   972  C  C   B ASP B 1 28 ? 31.749  -6.953  -33.611 0.50 62.22  ? 27  ASP B C   1 
ATOM   973  O  O   A ASP B 1 28 ? 31.155  -7.527  -32.628 0.50 60.54  ? 27  ASP B O   1 
ATOM   974  O  O   B ASP B 1 28 ? 31.132  -7.029  -32.550 0.50 63.84  ? 27  ASP B O   1 
ATOM   975  C  CB  A ASP B 1 28 ? 31.209  -5.168  -35.112 0.50 57.41  ? 27  ASP B CB  1 
ATOM   976  C  CB  B ASP B 1 28 ? 31.284  -5.481  -35.671 0.50 58.11  ? 27  ASP B CB  1 
ATOM   977  C  CG  A ASP B 1 28 ? 30.680  -4.624  -36.433 0.50 58.02  ? 27  ASP B CG  1 
ATOM   978  C  CG  B ASP B 1 28 ? 32.257  -5.638  -36.830 0.50 57.91  ? 27  ASP B CG  1 
ATOM   979  O  OD1 A ASP B 1 28 ? 31.277  -4.944  -37.485 0.50 55.47  ? 27  ASP B OD1 1 
ATOM   980  O  OD1 B ASP B 1 28 ? 33.214  -6.424  -36.679 0.50 58.78  ? 27  ASP B OD1 1 
ATOM   981  O  OD2 A ASP B 1 28 ? 29.675  -3.883  -36.404 0.50 53.41  ? 27  ASP B OD2 1 
ATOM   982  O  OD2 B ASP B 1 28 ? 32.051  -4.972  -37.872 0.50 53.01  ? 27  ASP B OD2 1 
ATOM   983  N  N   . ILE B 1 29 ? 33.085  -7.036  -33.696 1.00 66.12  ? 28  ILE B N   1 
ATOM   984  C  CA  . ILE B 1 29 ? 33.935  -7.252  -32.531 1.00 66.97  ? 28  ILE B CA  1 
ATOM   985  C  C   . ILE B 1 29 ? 34.661  -5.935  -32.201 1.00 70.13  ? 28  ILE B C   1 
ATOM   986  O  O   . ILE B 1 29 ? 33.993  -5.060  -31.604 1.00 64.32  ? 28  ILE B O   1 
ATOM   987  C  CB  . ILE B 1 29 ? 34.920  -8.421  -32.727 1.00 67.95  ? 28  ILE B CB  1 
ATOM   988  N  N   . PRO B 1 36 ? 35.174  -14.260 -30.039 1.00 63.88  ? 35  PRO B N   1 
ATOM   989  C  CA  . PRO B 1 36 ? 34.447  -15.521 -30.132 1.00 59.69  ? 35  PRO B CA  1 
ATOM   990  C  C   . PRO B 1 36 ? 35.396  -16.705 -30.003 1.00 54.29  ? 35  PRO B C   1 
ATOM   991  O  O   . PRO B 1 36 ? 36.548  -16.603 -30.401 1.00 59.02  ? 35  PRO B O   1 
ATOM   992  C  CB  . PRO B 1 36 ? 33.805  -15.482 -31.527 1.00 59.65  ? 35  PRO B CB  1 
ATOM   993  C  CG  . PRO B 1 36 ? 33.726  -14.009 -31.871 1.00 63.42  ? 35  PRO B CG  1 
ATOM   994  C  CD  . PRO B 1 36 ? 34.906  -13.367 -31.158 1.00 60.31  ? 35  PRO B CD  1 
ATOM   995  N  N   . PRO B 1 37 ? 34.960  -17.856 -29.441 1.00 55.94  ? 36  PRO B N   1 
ATOM   996  C  CA  . PRO B 1 37 ? 35.669  -19.115 -29.665 1.00 52.51  ? 36  PRO B CA  1 
ATOM   997  C  C   . PRO B 1 37 ? 35.689  -19.341 -31.176 1.00 64.37  ? 36  PRO B C   1 
ATOM   998  O  O   . PRO B 1 37 ? 34.822  -18.834 -31.889 1.00 63.96  ? 36  PRO B O   1 
ATOM   999  C  CB  . PRO B 1 37 ? 34.805  -20.160 -28.941 1.00 56.84  ? 36  PRO B CB  1 
ATOM   1000 C  CG  . PRO B 1 37 ? 34.002  -19.363 -27.929 1.00 57.35  ? 36  PRO B CG  1 
ATOM   1001 C  CD  . PRO B 1 37 ? 33.802  -17.993 -28.542 1.00 52.99  ? 36  PRO B CD  1 
ATOM   1002 N  N   . PRO B 1 38 ? 36.662  -20.104 -31.727 1.00 66.86  ? 37  PRO B N   1 
ATOM   1003 C  CA  . PRO B 1 38 ? 36.694  -20.370 -33.175 1.00 66.71  ? 37  PRO B CA  1 
ATOM   1004 C  C   . PRO B 1 38 ? 35.368  -20.932 -33.708 1.00 58.99  ? 37  PRO B C   1 
ATOM   1005 O  O   . PRO B 1 38 ? 34.663  -21.650 -32.998 1.00 59.28  ? 37  PRO B O   1 
ATOM   1006 C  CB  . PRO B 1 38 ? 37.859  -21.381 -33.346 1.00 71.45  ? 37  PRO B CB  1 
ATOM   1007 C  CG  . PRO B 1 38 ? 38.675  -21.269 -32.064 1.00 68.33  ? 37  PRO B CG  1 
ATOM   1008 C  CD  . PRO B 1 38 ? 37.739  -20.776 -30.978 1.00 69.77  ? 37  PRO B CD  1 
ATOM   1009 N  N   . ASN B 1 39 ? 35.033  -20.598 -34.961 1.00 57.21  ? 38  ASN B N   1 
ATOM   1010 C  CA  . ASN B 1 39 ? 33.860  -21.143 -35.645 1.00 60.96  ? 38  ASN B CA  1 
ATOM   1011 C  C   . ASN B 1 39 ? 32.546  -20.474 -35.213 1.00 53.94  ? 38  ASN B C   1 
ATOM   1012 O  O   . ASN B 1 39 ? 31.487  -20.806 -35.732 1.00 45.60  ? 38  ASN B O   1 
ATOM   1013 C  CB  . ASN B 1 39 ? 33.724  -22.655 -35.459 1.00 65.57  ? 38  ASN B CB  1 
ATOM   1014 C  CG  . ASN B 1 39 ? 34.923  -23.432 -35.957 1.00 73.39  ? 38  ASN B CG  1 
ATOM   1015 O  OD1 . ASN B 1 39 ? 35.280  -24.456 -35.364 1.00 74.60  ? 38  ASN B OD1 1 
ATOM   1016 N  ND2 . ASN B 1 39 ? 35.533  -22.992 -37.052 1.00 66.81  ? 38  ASN B ND2 1 
ATOM   1017 N  N   . LYS B 1 40 ? 32.595  -19.534 -34.260 1.00 53.54  ? 39  LYS B N   1 
ATOM   1018 C  CA  . LYS B 1 40 ? 31.370  -18.990 -33.696 1.00 44.24  ? 39  LYS B CA  1 
ATOM   1019 C  C   . LYS B 1 40 ? 31.372  -17.487 -33.902 1.00 42.97  ? 39  LYS B C   1 
ATOM   1020 O  O   . LYS B 1 40 ? 32.407  -16.912 -34.234 1.00 48.29  ? 39  LYS B O   1 
ATOM   1021 C  CB  . LYS B 1 40 ? 31.242  -19.360 -32.216 1.00 47.43  ? 39  LYS B CB  1 
ATOM   1022 C  CG  . LYS B 1 40 ? 31.644  -20.803 -31.982 1.00 46.28  ? 39  LYS B CG  1 
ATOM   1023 C  CD  . LYS B 1 40 ? 31.462  -21.408 -30.598 1.00 59.20  ? 39  LYS B CD  1 
ATOM   1024 C  CE  . LYS B 1 40 ? 30.192  -22.168 -30.467 1.00 62.96  ? 39  LYS B CE  1 
ATOM   1025 N  NZ  . LYS B 1 40 ? 30.149  -22.935 -29.216 1.00 63.43  ? 39  LYS B NZ  1 
ATOM   1026 N  N   . TYR B 1 41 ? 30.185  -16.883 -33.757 1.00 38.08  ? 40  TYR B N   1 
ATOM   1027 C  CA  . TYR B 1 41 ? 29.964  -15.488 -34.085 1.00 35.59  ? 40  TYR B CA  1 
ATOM   1028 C  C   . TYR B 1 41 ? 29.341  -14.777 -32.882 1.00 39.61  ? 40  TYR B C   1 
ATOM   1029 O  O   . TYR B 1 41 ? 28.595  -15.379 -32.094 1.00 33.97  ? 40  TYR B O   1 
ATOM   1030 C  CB  . TYR B 1 41 ? 28.973  -15.336 -35.242 1.00 37.72  ? 40  TYR B CB  1 
ATOM   1031 C  CG  . TYR B 1 41 ? 29.409  -15.829 -36.617 1.00 38.55  ? 40  TYR B CG  1 
ATOM   1032 C  CD1 . TYR B 1 41 ? 30.000  -14.977 -37.541 1.00 41.85  ? 40  TYR B CD1 1 
ATOM   1033 C  CD2 . TYR B 1 41 ? 29.162  -17.143 -37.005 1.00 36.17  ? 40  TYR B CD2 1 
ATOM   1034 C  CE1 . TYR B 1 41 ? 30.386  -15.432 -38.797 1.00 44.85  ? 40  TYR B CE1 1 
ATOM   1035 C  CE2 . TYR B 1 41 ? 29.553  -17.609 -38.249 1.00 39.58  ? 40  TYR B CE2 1 
ATOM   1036 C  CZ  . TYR B 1 41 ? 30.157  -16.751 -39.153 1.00 43.63  ? 40  TYR B CZ  1 
ATOM   1037 O  OH  . TYR B 1 41 ? 30.465  -17.214 -40.415 1.00 40.24  ? 40  TYR B OH  1 
ATOM   1038 N  N   . PRO B 1 42 ? 29.573  -13.455 -32.720 1.00 42.63  ? 41  PRO B N   1 
ATOM   1039 C  CA  . PRO B 1 42 ? 28.888  -12.710 -31.666 1.00 34.58  ? 41  PRO B CA  1 
ATOM   1040 C  C   . PRO B 1 42 ? 27.456  -12.451 -32.109 1.00 34.83  ? 41  PRO B C   1 
ATOM   1041 O  O   . PRO B 1 42 ? 27.214  -11.833 -33.159 1.00 37.33  ? 41  PRO B O   1 
ATOM   1042 C  CB  . PRO B 1 42 ? 29.703  -11.403 -31.489 1.00 36.83  ? 41  PRO B CB  1 
ATOM   1043 C  CG  . PRO B 1 42 ? 30.619  -11.331 -32.703 1.00 40.90  ? 41  PRO B CG  1 
ATOM   1044 C  CD  . PRO B 1 42 ? 30.500  -12.618 -33.511 1.00 38.77  ? 41  PRO B CD  1 
ATOM   1045 N  N   . ILE B 1 43 ? 26.507  -12.917 -31.272 1.00 33.70  ? 42  ILE B N   1 
ATOM   1046 C  CA  . ILE B 1 43 ? 25.083  -12.724 -31.530 1.00 32.60  ? 42  ILE B CA  1 
ATOM   1047 C  C   . ILE B 1 43 ? 24.508  -11.703 -30.546 1.00 29.53  ? 42  ILE B C   1 
ATOM   1048 O  O   . ILE B 1 43 ? 24.772  -11.805 -29.371 1.00 34.57  ? 42  ILE B O   1 
ATOM   1049 C  CB  . ILE B 1 43 ? 24.358  -14.074 -31.395 1.00 29.80  ? 42  ILE B CB  1 
ATOM   1050 C  CG1 . ILE B 1 43 ? 25.090  -15.189 -32.201 1.00 34.44  ? 42  ILE B CG1 1 
ATOM   1051 C  CG2 . ILE B 1 43 ? 22.868  -13.942 -31.769 1.00 29.31  ? 42  ILE B CG2 1 
ATOM   1052 C  CD1 . ILE B 1 43 ? 25.241  -14.931 -33.689 1.00 33.32  ? 42  ILE B CD1 1 
ATOM   1053 N  N   . PHE B 1 44 ? 23.703  -10.785 -31.065 1.00 32.24  ? 43  PHE B N   1 
ATOM   1054 C  CA  . PHE B 1 44 ? 22.849  -9.883  -30.303 1.00 32.20  ? 43  PHE B CA  1 
ATOM   1055 C  C   . PHE B 1 44 ? 21.403  -10.326 -30.503 1.00 28.77  ? 43  PHE B C   1 
ATOM   1056 O  O   . PHE B 1 44 ? 20.883  -10.333 -31.614 1.00 28.58  ? 43  PHE B O   1 
ATOM   1057 C  CB  . PHE B 1 44 ? 23.063  -8.470  -30.846 1.00 31.44  ? 43  PHE B CB  1 
ATOM   1058 C  CG  . PHE B 1 44 ? 22.163  -7.436  -30.166 1.00 31.64  ? 43  PHE B CG  1 
ATOM   1059 C  CD1 . PHE B 1 44 ? 20.970  -7.036  -30.750 1.00 33.96  ? 43  PHE B CD1 1 
ATOM   1060 C  CD2 . PHE B 1 44 ? 22.519  -6.894  -28.933 1.00 38.98  ? 43  PHE B CD2 1 
ATOM   1061 C  CE1 . PHE B 1 44 ? 20.140  -6.107  -30.128 1.00 35.01  ? 43  PHE B CE1 1 
ATOM   1062 C  CE2 . PHE B 1 44 ? 21.688  -5.948  -28.319 1.00 33.69  ? 43  PHE B CE2 1 
ATOM   1063 C  CZ  . PHE B 1 44 ? 20.521  -5.567  -28.923 1.00 35.38  ? 43  PHE B CZ  1 
ATOM   1064 N  N   . PHE B 1 45 ? 20.697  -10.590 -29.388 1.00 29.18  ? 44  PHE B N   1 
ATOM   1065 C  CA  . PHE B 1 45 ? 19.312  -10.986 -29.431 1.00 29.84  ? 44  PHE B CA  1 
ATOM   1066 C  C   . PHE B 1 45 ? 18.434  -9.768  -29.253 1.00 28.70  ? 44  PHE B C   1 
ATOM   1067 O  O   . PHE B 1 45 ? 18.582  -9.013  -28.265 1.00 31.24  ? 44  PHE B O   1 
ATOM   1068 C  CB  . PHE B 1 45 ? 19.025  -11.996 -28.296 1.00 29.67  ? 44  PHE B CB  1 
ATOM   1069 C  CG  . PHE B 1 45 ? 19.777  -13.320 -28.411 1.00 28.19  ? 44  PHE B CG  1 
ATOM   1070 C  CD1 . PHE B 1 45 ? 20.992  -13.524 -27.784 1.00 33.43  ? 44  PHE B CD1 1 
ATOM   1071 C  CD2 . PHE B 1 45 ? 19.228  -14.377 -29.135 1.00 27.21  ? 44  PHE B CD2 1 
ATOM   1072 C  CE1 . PHE B 1 45 ? 21.685  -14.716 -27.946 1.00 39.89  ? 44  PHE B CE1 1 
ATOM   1073 C  CE2 . PHE B 1 45 ? 19.890  -15.575 -29.238 1.00 30.78  ? 44  PHE B CE2 1 
ATOM   1074 C  CZ  . PHE B 1 45 ? 21.122  -15.733 -28.689 1.00 31.47  ? 44  PHE B CZ  1 
ATOM   1075 N  N   . PHE B 1 46 ? 17.587  -9.565  -30.267 1.00 27.46  ? 45  PHE B N   1 
ATOM   1076 C  CA  . PHE B 1 46 ? 16.609  -8.472  -30.293 1.00 26.30  ? 45  PHE B CA  1 
ATOM   1077 C  C   . PHE B 1 46 ? 15.608  -8.639  -29.137 1.00 28.24  ? 45  PHE B C   1 
ATOM   1078 O  O   . PHE B 1 46 ? 15.292  -9.760  -28.739 1.00 29.97  ? 45  PHE B O   1 
ATOM   1079 C  CB  . PHE B 1 46 ? 15.858  -8.240  -31.595 1.00 26.99  ? 45  PHE B CB  1 
ATOM   1080 C  CG  . PHE B 1 46 ? 16.796  -7.801  -32.715 1.00 30.82  ? 45  PHE B CG  1 
ATOM   1081 C  CD1 . PHE B 1 46 ? 17.340  -6.495  -32.716 1.00 30.58  ? 45  PHE B CD1 1 
ATOM   1082 C  CD2 . PHE B 1 46 ? 17.043  -8.660  -33.794 1.00 29.22  ? 45  PHE B CD2 1 
ATOM   1083 C  CE1 . PHE B 1 46 ? 18.207  -6.111  -33.742 1.00 28.92  ? 45  PHE B CE1 1 
ATOM   1084 C  CE2 . PHE B 1 46 ? 17.871  -8.247  -34.843 1.00 29.99  ? 45  PHE B CE2 1 
ATOM   1085 C  CZ  . PHE B 1 46 ? 18.405  -6.957  -34.821 1.00 31.15  ? 45  PHE B CZ  1 
ATOM   1086 N  N   . GLY B 1 47 ? 15.123  -7.510  -28.614 1.00 29.01  ? 46  GLY B N   1 
ATOM   1087 C  CA  . GLY B 1 47 ? 14.089  -7.555  -27.561 1.00 29.76  ? 46  GLY B CA  1 
ATOM   1088 C  C   . GLY B 1 47 ? 14.731  -7.678  -26.178 1.00 32.07  ? 46  GLY B C   1 
ATOM   1089 O  O   . GLY B 1 47 ? 14.608  -6.786  -25.335 1.00 37.97  ? 46  GLY B O   1 
ATOM   1090 N  N   . THR B 1 48 ? 15.500  -8.737  -25.942 1.00 32.97  ? 47  THR B N   1 
ATOM   1091 C  CA  . THR B 1 48 ? 16.152  -8.933  -24.655 1.00 34.92  ? 47  THR B CA  1 
ATOM   1092 C  C   . THR B 1 48 ? 17.442  -8.135  -24.603 1.00 35.58  ? 47  THR B C   1 
ATOM   1093 O  O   . THR B 1 48 ? 17.893  -7.736  -23.526 1.00 36.26  ? 47  THR B O   1 
ATOM   1094 C  CB  . THR B 1 48 ? 16.428  -10.403 -24.316 1.00 39.30  ? 47  THR B CB  1 
ATOM   1095 O  OG1 . THR B 1 48 ? 17.531  -10.914 -25.077 1.00 36.42  ? 47  THR B OG1 1 
ATOM   1096 C  CG2 . THR B 1 48 ? 15.169  -11.260 -24.341 1.00 34.62  ? 47  THR B CG2 1 
ATOM   1097 N  N   . HIS B 1 49 ? 18.025  -7.910  -25.781 1.00 33.02  ? 48  HIS B N   1 
ATOM   1098 C  CA  . HIS B 1 49 ? 19.309  -7.243  -25.899 1.00 35.01  ? 48  HIS B CA  1 
ATOM   1099 C  C   . HIS B 1 49 ? 20.410  -8.029  -25.212 1.00 33.78  ? 48  HIS B C   1 
ATOM   1100 O  O   . HIS B 1 49 ? 21.419  -7.429  -24.850 1.00 39.78  ? 48  HIS B O   1 
ATOM   1101 C  CB  . HIS B 1 49 ? 19.259  -5.766  -25.474 1.00 32.77  ? 48  HIS B CB  1 
ATOM   1102 C  CG  . HIS B 1 49 ? 18.057  -5.075  -26.002 1.00 34.65  ? 48  HIS B CG  1 
ATOM   1103 N  ND1 . HIS B 1 49 ? 17.251  -4.318  -25.177 1.00 38.91  ? 48  HIS B ND1 1 
ATOM   1104 C  CD2 . HIS B 1 49 ? 17.476  -5.048  -27.215 1.00 31.87  ? 48  HIS B CD2 1 
ATOM   1105 C  CE1 . HIS B 1 49 ? 16.243  -3.821  -25.887 1.00 41.57  ? 48  HIS B CE1 1 
ATOM   1106 N  NE2 . HIS B 1 49 ? 16.367  -4.256  -27.140 1.00 39.24  ? 48  HIS B NE2 1 
ATOM   1107 N  N   . GLU B 1 50 ? 20.247  -9.353  -25.047 1.00 33.50  ? 49  GLU B N   1 
ATOM   1108 C  CA  . GLU B 1 50 ? 21.319  -10.178 -24.489 1.00 33.27  ? 49  GLU B CA  1 
ATOM   1109 C  C   . GLU B 1 50 ? 22.251  -10.629 -25.621 1.00 33.99  ? 49  GLU B C   1 
ATOM   1110 O  O   . GLU B 1 50 ? 21.939  -10.385 -26.802 1.00 34.38  ? 49  GLU B O   1 
ATOM   1111 C  CB  . GLU B 1 50 ? 20.755  -11.423 -23.800 1.00 36.34  ? 49  GLU B CB  1 
ATOM   1112 C  CG  . GLU B 1 50 ? 19.889  -11.110 -22.584 1.00 41.45  ? 49  GLU B CG  1 
ATOM   1113 C  CD  . GLU B 1 50 ? 20.516  -10.641 -21.265 1.00 52.70  ? 49  GLU B CD  1 
ATOM   1114 O  OE1 . GLU B 1 50 ? 21.753  -10.609 -21.091 1.00 44.08  ? 49  GLU B OE1 1 
ATOM   1115 O  OE2 . GLU B 1 50 ? 19.725  -10.304 -20.351 1.00 54.57  ? 49  GLU B OE2 1 
ATOM   1116 N  N   . THR B 1 51 ? 23.387  -11.238 -25.234 1.00 37.36  ? 50  THR B N   1 
ATOM   1117 C  CA  . THR B 1 51 ? 24.399  -11.697 -26.188 1.00 40.90  ? 50  THR B CA  1 
ATOM   1118 C  C   . THR B 1 51 ? 24.832  -13.133 -25.874 1.00 43.49  ? 50  THR B C   1 
ATOM   1119 O  O   . THR B 1 51 ? 24.648  -13.643 -24.771 1.00 41.41  ? 50  THR B O   1 
ATOM   1120 C  CB  . THR B 1 51 ? 25.582  -10.724 -26.304 1.00 45.88  ? 50  THR B CB  1 
ATOM   1121 O  OG1 . THR B 1 51 ? 26.178  -10.558 -25.026 1.00 46.04  ? 50  THR B OG1 1 
ATOM   1122 C  CG2 . THR B 1 51 ? 25.187  -9.332  -26.758 1.00 47.92  ? 50  THR B CG2 1 
ATOM   1123 N  N   . ALA B 1 52 ? 25.358  -13.823 -26.893 1.00 39.25  ? 51  ALA B N   1 
ATOM   1124 C  CA  . ALA B 1 52 ? 25.982  -15.124 -26.762 1.00 39.86  ? 51  ALA B CA  1 
ATOM   1125 C  C   . ALA B 1 52 ? 26.879  -15.328 -27.977 1.00 37.77  ? 51  ALA B C   1 
ATOM   1126 O  O   . ALA B 1 52 ? 26.773  -14.573 -28.957 1.00 36.28  ? 51  ALA B O   1 
ATOM   1127 C  CB  . ALA B 1 52 ? 24.942  -16.225 -26.682 1.00 40.25  ? 51  ALA B CB  1 
ATOM   1128 N  N   . PHE B 1 53 ? 27.734  -16.355 -27.891 1.00 38.22  ? 52  PHE B N   1 
ATOM   1129 C  CA  . PHE B 1 53 ? 28.437  -16.833 -29.070 1.00 39.68  ? 52  PHE B CA  1 
ATOM   1130 C  C   . PHE B 1 53 ? 27.753  -18.104 -29.585 1.00 39.07  ? 52  PHE B C   1 
ATOM   1131 O  O   . PHE B 1 53 ? 27.506  -19.053 -28.843 1.00 40.78  ? 52  PHE B O   1 
ATOM   1132 C  CB  . PHE B 1 53 ? 29.919  -17.077 -28.762 1.00 39.83  ? 52  PHE B CB  1 
ATOM   1133 C  CG  . PHE B 1 53 ? 30.721  -15.884 -28.262 1.00 42.08  ? 52  PHE B CG  1 
ATOM   1134 C  CD1 . PHE B 1 53 ? 31.018  -14.826 -29.111 1.00 46.24  ? 52  PHE B CD1 1 
ATOM   1135 C  CD2 . PHE B 1 53 ? 31.214  -15.852 -26.963 1.00 47.14  ? 52  PHE B CD2 1 
ATOM   1136 C  CE1 . PHE B 1 53 ? 31.770  -13.742 -28.678 1.00 47.89  ? 52  PHE B CE1 1 
ATOM   1137 C  CE2 . PHE B 1 53 ? 31.931  -14.748 -26.517 1.00 48.88  ? 52  PHE B CE2 1 
ATOM   1138 C  CZ  . PHE B 1 53 ? 32.215  -13.705 -27.371 1.00 47.32  ? 52  PHE B CZ  1 
ATOM   1139 N  N   . LEU B 1 54 ? 27.447  -18.127 -30.889 1.00 38.44  ? 53  LEU B N   1 
ATOM   1140 C  CA  . LEU B 1 54 ? 26.843  -19.287 -31.518 1.00 32.32  ? 53  LEU B CA  1 
ATOM   1141 C  C   . LEU B 1 54 ? 27.629  -19.632 -32.790 1.00 34.48  ? 53  LEU B C   1 
ATOM   1142 O  O   . LEU B 1 54 ? 28.153  -18.732 -33.468 1.00 38.03  ? 53  LEU B O   1 
ATOM   1143 C  CB  . LEU B 1 54 ? 25.369  -19.064 -31.864 1.00 33.46  ? 53  LEU B CB  1 
ATOM   1144 C  CG  . LEU B 1 54 ? 24.404  -18.996 -30.679 1.00 32.79  ? 53  LEU B CG  1 
ATOM   1145 C  CD1 . LEU B 1 54 ? 23.020  -18.628 -31.147 1.00 31.52  ? 53  LEU B CD1 1 
ATOM   1146 C  CD2 . LEU B 1 54 ? 24.435  -20.377 -30.042 1.00 40.22  ? 53  LEU B CD2 1 
ATOM   1147 N  N   . GLY B 1 55 ? 27.622  -20.939 -33.108 1.00 34.87  ? 54  GLY B N   1 
ATOM   1148 C  CA  . GLY B 1 55 ? 28.097  -21.516 -34.363 1.00 35.51  ? 54  GLY B CA  1 
ATOM   1149 C  C   . GLY B 1 55 ? 27.009  -21.523 -35.437 1.00 32.57  ? 54  GLY B C   1 
ATOM   1150 O  O   . GLY B 1 55 ? 25.829  -21.371 -35.146 1.00 33.96  ? 54  GLY B O   1 
ATOM   1151 N  N   . PRO B 1 56 ? 27.354  -21.688 -36.741 1.00 33.31  ? 55  PRO B N   1 
ATOM   1152 C  CA  . PRO B 1 56 ? 26.337  -21.737 -37.801 1.00 32.87  ? 55  PRO B CA  1 
ATOM   1153 C  C   . PRO B 1 56 ? 25.176  -22.719 -37.713 1.00 31.72  ? 55  PRO B C   1 
ATOM   1154 O  O   . PRO B 1 56 ? 24.124  -22.451 -38.284 1.00 31.46  ? 55  PRO B O   1 
ATOM   1155 C  CB  . PRO B 1 56 ? 27.132  -21.961 -39.119 1.00 36.25  ? 55  PRO B CB  1 
ATOM   1156 C  CG  . PRO B 1 56 ? 28.561  -22.161 -38.685 1.00 38.10  ? 55  PRO B CG  1 
ATOM   1157 C  CD  . PRO B 1 56 ? 28.743  -21.779 -37.230 1.00 37.08  ? 55  PRO B CD  1 
ATOM   1158 N  N   . LYS B 1 57 ? 25.360  -23.849 -37.008 1.00 30.87  ? 56  LYS B N   1 
ATOM   1159 C  CA  . LYS B 1 57 ? 24.287  -24.830 -36.921 1.00 30.63  ? 56  LYS B CA  1 
ATOM   1160 C  C   . LYS B 1 57 ? 23.079  -24.226 -36.209 1.00 30.82  ? 56  LYS B C   1 
ATOM   1161 O  O   . LYS B 1 57 ? 21.956  -24.678 -36.399 1.00 30.63  ? 56  LYS B O   1 
ATOM   1162 C  CB  . LYS B 1 57 ? 24.691  -26.134 -36.213 1.00 39.38  ? 56  LYS B CB  1 
ATOM   1163 C  CG  . LYS B 1 57 ? 24.922  -26.074 -34.710 1.00 47.62  ? 56  LYS B CG  1 
ATOM   1164 C  CD  . LYS B 1 57 ? 24.843  -27.468 -34.090 1.00 49.28  ? 56  LYS B CD  1 
ATOM   1165 C  CE  . LYS B 1 57 ? 25.266  -27.524 -32.653 1.00 51.74  ? 56  LYS B CE  1 
ATOM   1166 N  NZ  . LYS B 1 57 ? 24.264  -26.978 -31.735 1.00 48.20  ? 56  LYS B NZ  1 
ATOM   1167 N  N   . ASP B 1 58 ? 23.332  -23.144 -35.439 1.00 29.26  ? 57  ASP B N   1 
ATOM   1168 C  CA  . ASP B 1 58 ? 22.265  -22.524 -34.670 1.00 28.76  ? 57  ASP B CA  1 
ATOM   1169 C  C   . ASP B 1 58 ? 21.826  -21.194 -35.273 1.00 31.48  ? 57  ASP B C   1 
ATOM   1170 O  O   . ASP B 1 58 ? 21.069  -20.454 -34.633 1.00 31.28  ? 57  ASP B O   1 
ATOM   1171 C  CB  . ASP B 1 58 ? 22.734  -22.373 -33.240 1.00 28.44  ? 57  ASP B CB  1 
ATOM   1172 C  CG  . ASP B 1 58 ? 22.887  -23.699 -32.504 1.00 36.94  ? 57  ASP B CG  1 
ATOM   1173 O  OD1 . ASP B 1 58 ? 21.931  -24.533 -32.594 1.00 34.16  ? 57  ASP B OD1 1 
ATOM   1174 O  OD2 . ASP B 1 58 ? 23.897  -23.831 -31.789 1.00 37.83  ? 57  ASP B OD2 1 
ATOM   1175 N  N   . LEU B 1 59 ? 22.292  -20.878 -36.502 1.00 28.59  ? 58  LEU B N   1 
ATOM   1176 C  CA  . LEU B 1 59 ? 22.023  -19.568 -37.119 1.00 29.80  ? 58  LEU B CA  1 
ATOM   1177 C  C   . LEU B 1 59 ? 21.238  -19.745 -38.418 1.00 27.98  ? 58  LEU B C   1 
ATOM   1178 O  O   . LEU B 1 59 ? 21.655  -20.464 -39.337 1.00 31.75  ? 58  LEU B O   1 
ATOM   1179 C  CB  . LEU B 1 59 ? 23.337  -18.809 -37.336 1.00 28.38  ? 58  LEU B CB  1 
ATOM   1180 C  CG  . LEU B 1 59 ? 24.206  -18.550 -36.102 1.00 28.87  ? 58  LEU B CG  1 
ATOM   1181 C  CD1 . LEU B 1 59 ? 25.474  -17.769 -36.484 1.00 31.75  ? 58  LEU B CD1 1 
ATOM   1182 C  CD2 . LEU B 1 59 ? 23.420  -17.716 -35.037 1.00 32.21  ? 58  LEU B CD2 1 
ATOM   1183 N  N   . PHE B 1 60 ? 20.046  -19.155 -38.487 1.00 25.93  ? 59  PHE B N   1 
ATOM   1184 C  CA  . PHE B 1 60 ? 19.102  -19.341 -39.573 1.00 27.99  ? 59  PHE B CA  1 
ATOM   1185 C  C   . PHE B 1 60 ? 18.885  -18.000 -40.271 1.00 29.85  ? 59  PHE B C   1 
ATOM   1186 O  O   . PHE B 1 60 ? 18.291  -17.093 -39.707 1.00 28.29  ? 59  PHE B O   1 
ATOM   1187 C  CB  . PHE B 1 60 ? 17.765  -19.876 -39.003 1.00 27.45  ? 59  PHE B CB  1 
ATOM   1188 C  CG  . PHE B 1 60 ? 17.882  -21.278 -38.414 1.00 28.50  ? 59  PHE B CG  1 
ATOM   1189 C  CD1 . PHE B 1 60 ? 18.414  -21.450 -37.132 1.00 27.91  ? 59  PHE B CD1 1 
ATOM   1190 C  CD2 . PHE B 1 60 ? 17.448  -22.388 -39.143 1.00 28.93  ? 59  PHE B CD2 1 
ATOM   1191 C  CE1 . PHE B 1 60 ? 18.545  -22.731 -36.606 1.00 32.99  ? 59  PHE B CE1 1 
ATOM   1192 C  CE2 . PHE B 1 60 ? 17.596  -23.667 -38.610 1.00 30.34  ? 59  PHE B CE2 1 
ATOM   1193 C  CZ  . PHE B 1 60 ? 18.143  -23.831 -37.354 1.00 31.96  ? 59  PHE B CZ  1 
ATOM   1194 N  N   . PRO B 1 61 ? 19.380  -17.789 -41.514 1.00 32.08  ? 60  PRO B N   1 
ATOM   1195 C  CA  . PRO B 1 61 ? 19.148  -16.508 -42.191 1.00 31.37  ? 60  PRO B CA  1 
ATOM   1196 C  C   . PRO B 1 61 ? 17.688  -16.038 -42.142 1.00 26.02  ? 60  PRO B C   1 
ATOM   1197 O  O   . PRO B 1 61 ? 16.728  -16.773 -42.407 1.00 32.71  ? 60  PRO B O   1 
ATOM   1198 C  CB  . PRO B 1 61 ? 19.611  -16.813 -43.636 1.00 34.37  ? 60  PRO B CB  1 
ATOM   1199 C  CG  . PRO B 1 61 ? 20.709  -17.820 -43.447 1.00 43.32  ? 60  PRO B CG  1 
ATOM   1200 C  CD  . PRO B 1 61 ? 20.208  -18.731 -42.292 1.00 36.36  ? 60  PRO B CD  1 
ATOM   1201 N  N   . TYR B 1 62 ? 17.522  -14.728 -41.788 1.00 29.95  ? 61  TYR B N   1 
ATOM   1202 C  CA  . TYR B 1 62 ? 16.235  -14.151 -41.493 1.00 31.16  ? 61  TYR B CA  1 
ATOM   1203 C  C   . TYR B 1 62 ? 15.233  -14.202 -42.639 1.00 34.19  ? 61  TYR B C   1 
ATOM   1204 O  O   . TYR B 1 62 ? 14.101  -14.602 -42.405 1.00 33.95  ? 61  TYR B O   1 
ATOM   1205 C  CB  . TYR B 1 62 ? 16.421  -12.732 -40.923 1.00 32.55  ? 61  TYR B CB  1 
ATOM   1206 C  CG  . TYR B 1 62 ? 15.119  -11.986 -40.671 1.00 37.49  ? 61  TYR B CG  1 
ATOM   1207 C  CD1 . TYR B 1 62 ? 14.359  -12.232 -39.541 1.00 39.20  ? 61  TYR B CD1 1 
ATOM   1208 C  CD2 . TYR B 1 62 ? 14.687  -10.982 -41.542 1.00 42.43  ? 61  TYR B CD2 1 
ATOM   1209 C  CE1 . TYR B 1 62 ? 13.178  -11.551 -39.309 1.00 38.61  ? 61  TYR B CE1 1 
ATOM   1210 C  CE2 . TYR B 1 62 ? 13.521  -10.263 -41.308 1.00 41.03  ? 61  TYR B CE2 1 
ATOM   1211 C  CZ  . TYR B 1 62 ? 12.765  -10.555 -40.182 1.00 42.97  ? 61  TYR B CZ  1 
ATOM   1212 O  OH  . TYR B 1 62 ? 11.601  -9.892  -39.964 1.00 42.92  ? 61  TYR B OH  1 
ATOM   1213 N  N   . ASP B 1 63 ? 15.625  -13.767 -43.853 1.00 35.98  ? 62  ASP B N   1 
ATOM   1214 C  CA  . ASP B 1 63 ? 14.694  -13.775 -44.980 1.00 48.06  ? 62  ASP B CA  1 
ATOM   1215 C  C   . ASP B 1 63 ? 14.160  -15.182 -45.237 1.00 37.45  ? 62  ASP B C   1 
ATOM   1216 O  O   . ASP B 1 63 ? 12.946  -15.385 -45.304 1.00 47.62  ? 62  ASP B O   1 
ATOM   1217 C  CB  . ASP B 1 63 ? 15.280  -13.126 -46.223 1.00 51.54  ? 62  ASP B CB  1 
ATOM   1218 C  CG  . ASP B 1 63 ? 15.145  -11.612 -46.303 1.00 70.32  ? 62  ASP B CG  1 
ATOM   1219 O  OD1 . ASP B 1 63 ? 14.396  -11.031 -45.474 1.00 73.03  ? 62  ASP B OD1 1 
ATOM   1220 O  OD2 . ASP B 1 63 ? 15.803  -11.017 -47.188 1.00 75.91  ? 62  ASP B OD2 1 
ATOM   1221 N  N   . LYS B 1 64 ? 15.071  -16.141 -45.371 1.00 41.86  ? 63  LYS B N   1 
ATOM   1222 C  CA  . LYS B 1 64 ? 14.708  -17.527 -45.604 1.00 42.25  ? 63  LYS B CA  1 
ATOM   1223 C  C   . LYS B 1 64 ? 13.738  -18.016 -44.528 1.00 38.28  ? 63  LYS B C   1 
ATOM   1224 O  O   . LYS B 1 64 ? 12.801  -18.743 -44.839 1.00 41.34  ? 63  LYS B O   1 
ATOM   1225 C  CB  . LYS B 1 64 ? 15.958  -18.417 -45.642 1.00 45.59  ? 63  LYS B CB  1 
ATOM   1226 C  CG  . LYS B 1 64 ? 15.639  -19.879 -45.931 1.00 44.39  ? 63  LYS B CG  1 
ATOM   1227 C  CD  . LYS B 1 64 ? 16.864  -20.774 -46.015 1.00 46.91  ? 63  LYS B CD  1 
ATOM   1228 C  CE  . LYS B 1 64 ? 16.649  -22.061 -46.797 1.00 48.34  ? 63  LYS B CE  1 
ATOM   1229 N  NZ  . LYS B 1 64 ? 15.437  -22.827 -46.501 1.00 52.17  ? 63  LYS B NZ  1 
ATOM   1230 N  N   . SER B 1 65 ? 13.927  -17.573 -43.279 1.00 36.08  ? 64  SER B N   1 
ATOM   1231 C  CA  . SER B 1 65 ? 13.335  -18.303 -42.148 1.00 41.00  ? 64  SER B CA  1 
ATOM   1232 C  C   . SER B 1 65 ? 12.213  -17.554 -41.419 1.00 41.28  ? 64  SER B C   1 
ATOM   1233 O  O   . SER B 1 65 ? 11.536  -18.119 -40.557 1.00 38.84  ? 64  SER B O   1 
ATOM   1234 C  CB  . SER B 1 65 ? 14.390  -18.843 -41.229 1.00 41.91  ? 64  SER B CB  1 
ATOM   1235 O  OG  . SER B 1 65 ? 15.180  -17.795 -40.692 1.00 58.77  ? 64  SER B OG  1 
ATOM   1236 N  N   . LYS B 1 66 ? 11.902  -16.323 -41.841 1.00 40.53  ? 65  LYS B N   1 
ATOM   1237 C  CA  . LYS B 1 66 ? 10.988  -15.497 -41.060 1.00 40.67  ? 65  LYS B CA  1 
ATOM   1238 C  C   . LYS B 1 66 ? 9.550   -16.010 -41.076 1.00 42.24  ? 65  LYS B C   1 
ATOM   1239 O  O   . LYS B 1 66 ? 8.818   -15.849 -40.100 1.00 44.48  ? 65  LYS B O   1 
ATOM   1240 C  CB  . LYS B 1 66 ? 11.070  -14.023 -41.475 1.00 40.02  ? 65  LYS B CB  1 
ATOM   1241 C  CG  . LYS B 1 66 ? 10.441  -13.693 -42.822 1.00 43.60  ? 65  LYS B CG  1 
ATOM   1242 N  N   . ASP B 1 67 ? 9.077   -16.602 -42.172 1.00 41.43  ? 66  ASP B N   1 
ATOM   1243 C  CA  . ASP B 1 67 ? 7.674   -16.984 -42.077 1.00 47.07  ? 66  ASP B CA  1 
ATOM   1244 C  C   . ASP B 1 67 ? 7.492   -18.172 -41.125 1.00 46.84  ? 66  ASP B C   1 
ATOM   1245 O  O   . ASP B 1 67 ? 6.445   -18.300 -40.491 1.00 53.08  ? 66  ASP B O   1 
ATOM   1246 C  CB  . ASP B 1 67 ? 6.949   -16.960 -43.416 1.00 58.59  ? 66  ASP B CB  1 
ATOM   1247 C  CG  . ASP B 1 67 ? 7.337   -18.041 -44.409 1.00 71.87  ? 66  ASP B CG  1 
ATOM   1248 O  OD1 . ASP B 1 67 ? 6.871   -17.965 -45.570 1.00 86.92  ? 66  ASP B OD1 1 
ATOM   1249 O  OD2 . ASP B 1 67 ? 8.090   -18.953 -44.016 1.00 78.35  ? 66  ASP B OD2 1 
ATOM   1250 N  N   . LYS B 1 68 ? 8.533   -19.012 -41.004 1.00 48.68  ? 67  LYS B N   1 
ATOM   1251 C  CA  . LYS B 1 68 ? 8.506   -20.172 -40.129 1.00 45.60  ? 67  LYS B CA  1 
ATOM   1252 C  C   . LYS B 1 68 ? 8.692   -19.787 -38.660 1.00 40.39  ? 67  LYS B C   1 
ATOM   1253 O  O   . LYS B 1 68 ? 7.920   -20.247 -37.822 1.00 43.73  ? 67  LYS B O   1 
ATOM   1254 C  CB  . LYS B 1 68 ? 9.574   -21.189 -40.541 1.00 42.02  ? 67  LYS B CB  1 
ATOM   1255 C  CG  . LYS B 1 68 ? 9.693   -22.428 -39.670 1.00 49.01  ? 67  LYS B CG  1 
ATOM   1256 C  CD  . LYS B 1 68 ? 10.731  -23.348 -40.299 1.00 60.91  ? 67  LYS B CD  1 
ATOM   1257 C  CE  . LYS B 1 68 ? 10.969  -24.602 -39.533 1.00 60.71  ? 67  LYS B CE  1 
ATOM   1258 N  NZ  . LYS B 1 68 ? 9.795   -25.473 -39.620 1.00 68.27  ? 67  LYS B NZ  1 
ATOM   1259 N  N   . TYR B 1 69 ? 9.699   -18.959 -38.353 1.00 36.42  ? 68  TYR B N   1 
ATOM   1260 C  CA  . TYR B 1 69 ? 10.053  -18.679 -36.967 1.00 32.03  ? 68  TYR B CA  1 
ATOM   1261 C  C   . TYR B 1 69 ? 9.559   -17.311 -36.502 1.00 34.61  ? 68  TYR B C   1 
ATOM   1262 O  O   . TYR B 1 69 ? 9.656   -17.013 -35.317 1.00 40.73  ? 68  TYR B O   1 
ATOM   1263 C  CB  . TYR B 1 69 ? 11.565  -18.725 -36.782 1.00 32.16  ? 68  TYR B CB  1 
ATOM   1264 C  CG  . TYR B 1 69 ? 12.220  -20.087 -37.021 1.00 33.21  ? 68  TYR B CG  1 
ATOM   1265 C  CD1 . TYR B 1 69 ? 11.736  -21.252 -36.438 1.00 34.03  ? 68  TYR B CD1 1 
ATOM   1266 C  CD2 . TYR B 1 69 ? 13.306  -20.200 -37.887 1.00 39.04  ? 68  TYR B CD2 1 
ATOM   1267 C  CE1 . TYR B 1 69 ? 12.342  -22.484 -36.663 1.00 37.26  ? 68  TYR B CE1 1 
ATOM   1268 C  CE2 . TYR B 1 69 ? 13.891  -21.429 -38.158 1.00 37.31  ? 68  TYR B CE2 1 
ATOM   1269 C  CZ  . TYR B 1 69 ? 13.421  -22.568 -37.524 1.00 39.64  ? 68  TYR B CZ  1 
ATOM   1270 O  OH  . TYR B 1 69 ? 14.005  -23.760 -37.802 1.00 38.66  ? 68  TYR B OH  1 
ATOM   1271 N  N   . GLY B 1 70 ? 9.154   -16.440 -37.431 1.00 37.87  ? 69  GLY B N   1 
ATOM   1272 C  CA  . GLY B 1 70 ? 8.888   -15.047 -37.097 1.00 42.42  ? 69  GLY B CA  1 
ATOM   1273 C  C   . GLY B 1 70 ? 7.485   -14.820 -36.526 1.00 47.50  ? 69  GLY B C   1 
ATOM   1274 O  O   . GLY B 1 70 ? 6.828   -13.833 -36.873 1.00 47.15  ? 69  GLY B O   1 
ATOM   1275 N  N   . LYS B 1 71 ? 7.031   -15.732 -35.653 1.00 48.77  ? 70  LYS B N   1 
ATOM   1276 C  CA  . LYS B 1 71 ? 5.668   -15.670 -35.148 1.00 48.46  ? 70  LYS B CA  1 
ATOM   1277 C  C   . LYS B 1 71 ? 5.692   -15.230 -33.695 1.00 53.98  ? 70  LYS B C   1 
ATOM   1278 O  O   . LYS B 1 71 ? 6.555   -15.667 -32.940 1.00 48.21  ? 70  LYS B O   1 
ATOM   1279 C  CB  . LYS B 1 71 ? 4.978   -17.034 -35.046 1.00 52.75  ? 70  LYS B CB  1 
ATOM   1280 C  CG  . LYS B 1 71 ? 3.952   -17.351 -36.123 1.00 63.12  ? 70  LYS B CG  1 
ATOM   1281 C  CD  . LYS B 1 71 ? 4.552   -17.798 -37.450 1.00 66.90  ? 70  LYS B CD  1 
ATOM   1282 C  CE  . LYS B 1 71 ? 3.500   -18.307 -38.385 1.00 76.41  ? 70  LYS B CE  1 
ATOM   1283 N  NZ  . LYS B 1 71 ? 4.084   -19.097 -39.472 1.00 81.25  ? 70  LYS B NZ  1 
ATOM   1284 N  N   . PRO B 1 72 ? 4.750   -14.369 -33.254 1.00 50.78  ? 71  PRO B N   1 
ATOM   1285 C  CA  . PRO B 1 72 ? 4.654   -14.043 -31.829 1.00 48.13  ? 71  PRO B CA  1 
ATOM   1286 C  C   . PRO B 1 72 ? 4.502   -15.254 -30.910 1.00 40.58  ? 71  PRO B C   1 
ATOM   1287 O  O   . PRO B 1 72 ? 3.951   -16.284 -31.301 1.00 47.59  ? 71  PRO B O   1 
ATOM   1288 C  CB  . PRO B 1 72 ? 3.474   -13.055 -31.758 1.00 47.76  ? 71  PRO B CB  1 
ATOM   1289 C  CG  . PRO B 1 72 ? 3.469   -12.434 -33.140 1.00 50.30  ? 71  PRO B CG  1 
ATOM   1290 C  CD  . PRO B 1 72 ? 3.846   -13.566 -34.092 1.00 44.55  ? 71  PRO B CD  1 
ATOM   1291 N  N   . ASN B 1 73 ? 5.036   -15.106 -29.693 1.00 47.48  ? 72  ASN B N   1 
ATOM   1292 C  CA  . ASN B 1 73 ? 4.870   -16.091 -28.634 1.00 40.73  ? 72  ASN B CA  1 
ATOM   1293 C  C   . ASN B 1 73 ? 4.839   -15.359 -27.282 1.00 50.97  ? 72  ASN B C   1 
ATOM   1294 O  O   . ASN B 1 73 ? 4.831   -14.119 -27.223 1.00 51.46  ? 72  ASN B O   1 
ATOM   1295 C  CB  . ASN B 1 73 ? 5.919   -17.203 -28.688 1.00 41.95  ? 72  ASN B CB  1 
ATOM   1296 C  CG  . ASN B 1 73 ? 7.329   -16.757 -28.360 1.00 40.71  ? 72  ASN B CG  1 
ATOM   1297 O  OD1 . ASN B 1 73 ? 7.547   -16.025 -27.383 1.00 38.97  ? 72  ASN B OD1 1 
ATOM   1298 N  ND2 . ASN B 1 73 ? 8.310   -17.148 -29.179 1.00 34.47  ? 72  ASN B ND2 1 
ATOM   1299 N  N   . LYS B 1 74 ? 4.885   -16.139 -26.195 1.00 45.69  ? 73  LYS B N   1 
ATOM   1300 C  CA  . LYS B 1 74 ? 4.726   -15.591 -24.853 1.00 47.54  ? 73  LYS B CA  1 
ATOM   1301 C  C   . LYS B 1 74 ? 6.043   -15.527 -24.057 1.00 50.04  ? 73  LYS B C   1 
ATOM   1302 O  O   . LYS B 1 74 ? 6.003   -15.347 -22.838 1.00 48.05  ? 73  LYS B O   1 
ATOM   1303 C  CB  . LYS B 1 74 ? 3.590   -16.344 -24.128 1.00 43.81  ? 73  LYS B CB  1 
ATOM   1304 N  N   . ARG B 1 75 ? 7.215   -15.673 -24.706 1.00 38.67  ? 74  ARG B N   1 
ATOM   1305 C  CA  . ARG B 1 75 ? 8.479   -15.488 -24.002 1.00 35.47  ? 74  ARG B CA  1 
ATOM   1306 C  C   . ARG B 1 75 ? 8.743   -13.983 -23.852 1.00 32.19  ? 74  ARG B C   1 
ATOM   1307 O  O   . ARG B 1 75 ? 8.474   -13.189 -24.765 1.00 34.03  ? 74  ARG B O   1 
ATOM   1308 C  CB  . ARG B 1 75 ? 9.635   -16.234 -24.689 1.00 36.36  ? 74  ARG B CB  1 
ATOM   1309 C  CG  . ARG B 1 75 ? 9.508   -17.729 -24.981 1.00 35.11  ? 74  ARG B CG  1 
ATOM   1310 C  CD  . ARG B 1 75 ? 9.259   -18.522 -23.698 1.00 38.34  ? 74  ARG B CD  1 
ATOM   1311 N  NE  . ARG B 1 75 ? 9.515   -19.950 -23.899 1.00 34.33  ? 74  ARG B NE  1 
ATOM   1312 C  CZ  . ARG B 1 75 ? 10.648  -20.573 -23.661 1.00 35.16  ? 74  ARG B CZ  1 
ATOM   1313 N  NH1 . ARG B 1 75 ? 11.704  -19.920 -23.160 1.00 39.55  ? 74  ARG B NH1 1 
ATOM   1314 N  NH2 . ARG B 1 75 ? 10.737  -21.859 -23.978 1.00 39.13  ? 74  ARG B NH2 1 
ATOM   1315 N  N   . LYS B 1 76 ? 9.229   -13.573 -22.668 1.00 33.04  ? 75  LYS B N   1 
ATOM   1316 C  CA  . LYS B 1 76 ? 9.622   -12.211 -22.360 1.00 30.31  ? 75  LYS B CA  1 
ATOM   1317 C  C   . LYS B 1 76 ? 10.674  -11.701 -23.357 1.00 30.18  ? 75  LYS B C   1 
ATOM   1318 O  O   . LYS B 1 76 ? 11.760  -12.290 -23.427 1.00 31.59  ? 75  LYS B O   1 
ATOM   1319 C  CB  . LYS B 1 76 ? 10.246  -12.163 -20.957 1.00 31.64  ? 75  LYS B CB  1 
ATOM   1320 C  CG  . LYS B 1 76 ? 10.605  -10.746 -20.550 1.00 33.32  ? 75  LYS B CG  1 
ATOM   1321 C  CD  . LYS B 1 76 ? 11.029  -10.605 -19.096 1.00 36.21  ? 75  LYS B CD  1 
ATOM   1322 C  CE  . LYS B 1 76 ? 11.310  -9.159  -18.741 1.00 38.77  ? 75  LYS B CE  1 
ATOM   1323 N  NZ  . LYS B 1 76 ? 11.746  -9.038  -17.337 1.00 48.84  ? 75  LYS B NZ  1 
ATOM   1324 N  N   . GLY B 1 77 ? 10.264  -10.651 -24.089 1.00 30.57  ? 76  GLY B N   1 
ATOM   1325 C  CA  . GLY B 1 77 ? 11.170  -9.916  -24.987 1.00 31.33  ? 76  GLY B CA  1 
ATOM   1326 C  C   . GLY B 1 77 ? 11.042  -10.369 -26.430 1.00 34.09  ? 76  GLY B C   1 
ATOM   1327 O  O   . GLY B 1 77 ? 11.650  -9.776  -27.321 1.00 33.62  ? 76  GLY B O   1 
ATOM   1328 N  N   . PHE B 1 78 ? 10.270  -11.427 -26.680 1.00 31.77  ? 77  PHE B N   1 
ATOM   1329 C  CA  . PHE B 1 78 ? 10.186  -11.977 -28.034 1.00 30.40  ? 77  PHE B CA  1 
ATOM   1330 C  C   . PHE B 1 78 ? 9.452   -11.026 -28.987 1.00 33.89  ? 77  PHE B C   1 
ATOM   1331 O  O   . PHE B 1 78 ? 9.934   -10.750 -30.101 1.00 31.79  ? 77  PHE B O   1 
ATOM   1332 C  CB  . PHE B 1 78 ? 9.501   -13.347 -28.021 1.00 30.29  ? 77  PHE B CB  1 
ATOM   1333 C  CG  . PHE B 1 78 ? 9.711   -14.070 -29.338 1.00 30.28  ? 77  PHE B CG  1 
ATOM   1334 C  CD1 . PHE B 1 78 ? 10.814  -14.905 -29.499 1.00 29.57  ? 77  PHE B CD1 1 
ATOM   1335 C  CD2 . PHE B 1 78 ? 8.806   -13.928 -30.383 1.00 33.16  ? 77  PHE B CD2 1 
ATOM   1336 C  CE1 . PHE B 1 78 ? 11.040  -15.555 -30.728 1.00 28.07  ? 77  PHE B CE1 1 
ATOM   1337 C  CE2 . PHE B 1 78 ? 9.022   -14.595 -31.589 1.00 32.90  ? 77  PHE B CE2 1 
ATOM   1338 C  CZ  . PHE B 1 78 ? 10.120  -15.431 -31.724 1.00 30.47  ? 77  PHE B CZ  1 
ATOM   1339 N  N   . ASN B 1 79 ? 8.280   -10.518 -28.595 1.00 32.98  ? 78  ASN B N   1 
ATOM   1340 C  CA  . ASN B 1 79 ? 7.499   -9.677  -29.496 1.00 34.83  ? 78  ASN B CA  1 
ATOM   1341 C  C   . ASN B 1 79 ? 8.207   -8.328  -29.722 1.00 34.16  ? 78  ASN B C   1 
ATOM   1342 O  O   . ASN B 1 79 ? 8.128   -7.775  -30.828 1.00 34.85  ? 78  ASN B O   1 
ATOM   1343 C  CB  . ASN B 1 79 ? 6.025   -9.572  -29.082 1.00 41.09  ? 78  ASN B CB  1 
ATOM   1344 C  CG  . ASN B 1 79 ? 5.264   -10.889 -29.076 1.00 42.54  ? 78  ASN B CG  1 
ATOM   1345 O  OD1 . ASN B 1 79 ? 5.625   -11.858 -29.750 1.00 39.14  ? 78  ASN B OD1 1 
ATOM   1346 N  ND2 . ASN B 1 79 ? 4.186   -10.976 -28.307 1.00 48.12  ? 78  ASN B ND2 1 
ATOM   1347 N  N   . GLU B 1 80 ? 8.949   -7.843  -28.716 1.00 33.11  ? 79  GLU B N   1 
ATOM   1348 C  CA  . GLU B 1 80 ? 9.690   -6.600  -28.867 1.00 34.40  ? 79  GLU B CA  1 
ATOM   1349 C  C   . GLU B 1 80 ? 10.847  -6.865  -29.841 1.00 35.46  ? 79  GLU B C   1 
ATOM   1350 O  O   . GLU B 1 80 ? 11.182  -5.990  -30.657 1.00 32.43  ? 79  GLU B O   1 
ATOM   1351 C  CB  . GLU B 1 80 ? 10.259  -6.126  -27.530 1.00 38.57  ? 79  GLU B CB  1 
ATOM   1352 C  CG  . GLU B 1 80 ? 9.221   -5.545  -26.572 1.00 46.07  ? 79  GLU B CG  1 
ATOM   1353 N  N   . GLY B 1 81 ? 11.423  -8.083  -29.757 1.00 30.89  ? 80  GLY B N   1 
ATOM   1354 C  CA  . GLY B 1 81 ? 12.523  -8.496  -30.637 1.00 33.19  ? 80  GLY B CA  1 
ATOM   1355 C  C   . GLY B 1 81 ? 12.078  -8.574  -32.094 1.00 34.36  ? 80  GLY B C   1 
ATOM   1356 O  O   . GLY B 1 81 ? 12.836  -8.231  -33.017 1.00 31.98  ? 80  GLY B O   1 
ATOM   1357 N  N   . LEU B 1 82 ? 10.864  -9.052  -32.298 1.00 29.27  ? 81  LEU B N   1 
ATOM   1358 C  CA  . LEU B 1 82 ? 10.256  -9.094  -33.621 1.00 32.14  ? 81  LEU B CA  1 
ATOM   1359 C  C   . LEU B 1 82 ? 10.148  -7.669  -34.162 1.00 31.96  ? 81  LEU B C   1 
ATOM   1360 O  O   . LEU B 1 82 ? 10.448  -7.425  -35.329 1.00 31.71  ? 81  LEU B O   1 
ATOM   1361 C  CB  . LEU B 1 82 ? 8.891   -9.797  -33.648 1.00 34.36  ? 81  LEU B CB  1 
ATOM   1362 C  CG  . LEU B 1 82 ? 8.913   -11.320 -33.472 1.00 32.30  ? 81  LEU B CG  1 
ATOM   1363 C  CD1 . LEU B 1 82 ? 7.523   -11.934 -33.572 1.00 34.96  ? 81  LEU B CD1 1 
ATOM   1364 C  CD2 . LEU B 1 82 ? 9.909   -11.970 -34.443 1.00 31.37  ? 81  LEU B CD2 1 
ATOM   1365 N  N   . TRP B 1 83 ? 9.657   -6.752  -33.324 1.00 31.86  ? 82  TRP B N   1 
ATOM   1366 C  CA  . TRP B 1 83 ? 9.511   -5.354  -33.707 1.00 34.86  ? 82  TRP B CA  1 
ATOM   1367 C  C   . TRP B 1 83 ? 10.855  -4.783  -34.181 1.00 34.49  ? 82  TRP B C   1 
ATOM   1368 O  O   . TRP B 1 83 ? 10.920  -4.215  -35.283 1.00 33.17  ? 82  TRP B O   1 
ATOM   1369 C  CB  . TRP B 1 83 ? 8.937   -4.519  -32.552 1.00 36.09  ? 82  TRP B CB  1 
ATOM   1370 C  CG  . TRP B 1 83 ? 8.587   -3.139  -33.048 1.00 33.44  ? 82  TRP B CG  1 
ATOM   1371 C  CD1 . TRP B 1 83 ? 7.413   -2.753  -33.619 1.00 44.16  ? 82  TRP B CD1 1 
ATOM   1372 C  CD2 . TRP B 1 83 ? 9.478   -2.009  -33.134 1.00 37.32  ? 82  TRP B CD2 1 
ATOM   1373 N  NE1 . TRP B 1 83 ? 7.488   -1.444  -34.020 1.00 46.27  ? 82  TRP B NE1 1 
ATOM   1374 C  CE2 . TRP B 1 83 ? 8.743   -0.968  -33.741 1.00 41.14  ? 82  TRP B CE2 1 
ATOM   1375 C  CE3 . TRP B 1 83 ? 10.806  -1.775  -32.753 1.00 37.33  ? 82  TRP B CE3 1 
ATOM   1376 C  CZ2 . TRP B 1 83 ? 9.302   0.290   -33.969 1.00 39.74  ? 82  TRP B CZ2 1 
ATOM   1377 C  CZ3 . TRP B 1 83 ? 11.355  -0.531  -32.975 1.00 41.40  ? 82  TRP B CZ3 1 
ATOM   1378 C  CH2 . TRP B 1 83 ? 10.608  0.478   -33.586 1.00 33.28  ? 82  TRP B CH2 1 
ATOM   1379 N  N   . GLU B 1 84 ? 11.914  -5.016  -33.387 1.00 29.45  ? 83  GLU B N   1 
ATOM   1380 C  CA  . GLU B 1 84 ? 13.234  -4.468  -33.632 1.00 32.55  ? 83  GLU B CA  1 
ATOM   1381 C  C   . GLU B 1 84 ? 13.805  -4.984  -34.953 1.00 31.15  ? 83  GLU B C   1 
ATOM   1382 O  O   . GLU B 1 84 ? 14.416  -4.218  -35.704 1.00 31.94  ? 83  GLU B O   1 
ATOM   1383 C  CB  . GLU B 1 84 ? 14.185  -4.760  -32.481 1.00 29.86  ? 83  GLU B CB  1 
ATOM   1384 C  CG  . GLU B 1 84 ? 13.736  -4.022  -31.215 1.00 33.95  ? 83  GLU B CG  1 
ATOM   1385 C  CD  . GLU B 1 84 ? 14.577  -4.349  -30.017 1.00 34.22  ? 83  GLU B CD  1 
ATOM   1386 O  OE1 . GLU B 1 84 ? 15.524  -5.179  -30.123 1.00 31.27  ? 83  GLU B OE1 1 
ATOM   1387 O  OE2 . GLU B 1 84 ? 14.306  -3.742  -28.928 1.00 35.83  ? 83  GLU B OE2 1 
ATOM   1388 N  N   . ILE B 1 85 ? 13.674  -6.297  -35.190 1.00 29.94  ? 84  ILE B N   1 
ATOM   1389 C  CA  . ILE B 1 85 ? 14.317  -6.882  -36.374 1.00 29.00  ? 84  ILE B CA  1 
ATOM   1390 C  C   . ILE B 1 85 ? 13.667  -6.322  -37.640 1.00 28.20  ? 84  ILE B C   1 
ATOM   1391 O  O   . ILE B 1 85 ? 14.369  -6.154  -38.656 1.00 31.56  ? 84  ILE B O   1 
ATOM   1392 C  CB  . ILE B 1 85 ? 14.376  -8.424  -36.341 1.00 28.07  ? 84  ILE B CB  1 
ATOM   1393 C  CG1 . ILE B 1 85 ? 15.383  -8.974  -37.400 1.00 29.41  ? 84  ILE B CG1 1 
ATOM   1394 C  CG2 . ILE B 1 85 ? 12.980  -9.024  -36.544 1.00 27.74  ? 84  ILE B CG2 1 
ATOM   1395 C  CD1 . ILE B 1 85 ? 15.947  -10.348 -37.028 1.00 27.76  ? 84  ILE B CD1 1 
ATOM   1396 N  N   . GLN B 1 86 ? 12.343  -6.116  -37.588 1.00 31.84  ? 85  GLN B N   1 
ATOM   1397 C  CA  . GLN B 1 86 ? 11.531  -5.573  -38.676 1.00 31.80  ? 85  GLN B CA  1 
ATOM   1398 C  C   . GLN B 1 86 ? 11.801  -4.076  -38.870 1.00 37.17  ? 85  GLN B C   1 
ATOM   1399 O  O   . GLN B 1 86 ? 11.905  -3.592  -39.999 1.00 39.74  ? 85  GLN B O   1 
ATOM   1400 C  CB  . GLN B 1 86 ? 10.050  -5.835  -38.391 1.00 38.34  ? 85  GLN B CB  1 
ATOM   1401 C  CG  . GLN B 1 86 ? 9.571   -7.235  -38.790 1.00 48.36  ? 85  GLN B CG  1 
ATOM   1402 C  CD  . GLN B 1 86 ? 8.482   -7.846  -37.924 1.00 50.75  ? 85  GLN B CD  1 
ATOM   1403 O  OE1 . GLN B 1 86 ? 7.351   -7.344  -37.804 1.00 60.29  ? 85  GLN B OE1 1 
ATOM   1404 N  NE2 . GLN B 1 86 ? 8.813   -8.999  -37.350 1.00 49.93  ? 85  GLN B NE2 1 
ATOM   1405 N  N   . ASN B 1 87 ? 11.961  -3.325  -37.786 1.00 32.50  ? 86  ASN B N   1 
ATOM   1406 C  CA  . ASN B 1 87 ? 11.839  -1.874  -37.936 1.00 31.04  ? 86  ASN B CA  1 
ATOM   1407 C  C   . ASN B 1 87 ? 13.136  -1.099  -37.739 1.00 31.82  ? 86  ASN B C   1 
ATOM   1408 O  O   . ASN B 1 87 ? 13.252  0.026   -38.249 1.00 33.16  ? 86  ASN B O   1 
ATOM   1409 C  CB  . ASN B 1 87 ? 10.893  -1.280  -36.889 1.00 33.01  ? 86  ASN B CB  1 
ATOM   1410 C  CG  . ASN B 1 87 ? 9.475   -1.701  -37.188 1.00 40.55  ? 86  ASN B CG  1 
ATOM   1411 O  OD1 . ASN B 1 87 ? 8.884   -1.233  -38.163 1.00 51.21  ? 86  ASN B OD1 1 
ATOM   1412 N  ND2 . ASN B 1 87 ? 8.941   -2.642  -36.429 1.00 45.81  ? 86  ASN B ND2 1 
ATOM   1413 N  N   . ASN B 1 88 ? 14.100  -1.617  -36.984 1.00 32.47  ? 87  ASN B N   1 
ATOM   1414 C  CA  . ASN B 1 88 ? 15.360  -0.907  -36.805 1.00 32.34  ? 87  ASN B CA  1 
ATOM   1415 C  C   . ASN B 1 88 ? 16.446  -1.899  -36.385 1.00 33.89  ? 87  ASN B C   1 
ATOM   1416 O  O   . ASN B 1 88 ? 17.057  -1.837  -35.300 1.00 31.05  ? 87  ASN B O   1 
ATOM   1417 C  CB  . ASN B 1 88 ? 15.182  0.339   -35.931 1.00 37.58  ? 87  ASN B CB  1 
ATOM   1418 C  CG  . ASN B 1 88 ? 16.332  1.321   -36.031 1.00 34.51  ? 87  ASN B CG  1 
ATOM   1419 O  OD1 . ASN B 1 88 ? 17.361  1.071   -36.667 1.00 38.14  ? 87  ASN B OD1 1 
ATOM   1420 N  ND2 . ASN B 1 88 ? 16.185  2.465   -35.374 1.00 40.55  ? 87  ASN B ND2 1 
ATOM   1421 N  N   . PRO B 1 89 ? 16.737  -2.882  -37.270 1.00 31.94  ? 88  PRO B N   1 
ATOM   1422 C  CA  . PRO B 1 89 ? 17.677  -3.952  -36.925 1.00 29.80  ? 88  PRO B CA  1 
ATOM   1423 C  C   . PRO B 1 89 ? 19.113  -3.529  -36.668 1.00 26.99  ? 88  PRO B C   1 
ATOM   1424 O  O   . PRO B 1 89 ? 19.887  -4.271  -36.072 1.00 29.63  ? 88  PRO B O   1 
ATOM   1425 C  CB  . PRO B 1 89 ? 17.602  -4.884  -38.156 1.00 30.49  ? 88  PRO B CB  1 
ATOM   1426 C  CG  . PRO B 1 89 ? 17.112  -3.973  -39.282 1.00 28.25  ? 88  PRO B CG  1 
ATOM   1427 C  CD  . PRO B 1 89 ? 16.123  -3.040  -38.604 1.00 32.16  ? 88  PRO B CD  1 
ATOM   1428 N  N   . HIS B 1 90 ? 19.501  -2.337  -37.201 1.00 28.17  ? 89  HIS B N   1 
ATOM   1429 C  CA  . HIS B 1 90 ? 20.884  -1.916  -37.110 1.00 28.98  ? 89  HIS B CA  1 
ATOM   1430 C  C   . HIS B 1 90 ? 21.150  -0.844  -36.049 1.00 34.17  ? 89  HIS B C   1 
ATOM   1431 O  O   . HIS B 1 90 ? 22.286  -0.382  -35.963 1.00 32.53  ? 89  HIS B O   1 
ATOM   1432 C  CB  . HIS B 1 90 ? 21.391  -1.457  -38.492 1.00 27.91  ? 89  HIS B CB  1 
ATOM   1433 C  CG  . HIS B 1 90 ? 21.251  -2.576  -39.474 1.00 30.58  ? 89  HIS B CG  1 
ATOM   1434 N  ND1 . HIS B 1 90 ? 21.844  -3.811  -39.369 1.00 27.75  ? 89  HIS B ND1 1 
ATOM   1435 C  CD2 . HIS B 1 90 ? 20.568  -2.590  -40.614 1.00 29.25  ? 89  HIS B CD2 1 
ATOM   1436 C  CE1 . HIS B 1 90 ? 21.517  -4.537  -40.415 1.00 28.60  ? 89  HIS B CE1 1 
ATOM   1437 N  NE2 . HIS B 1 90 ? 20.704  -3.837  -41.170 1.00 31.17  ? 89  HIS B NE2 1 
ATOM   1438 N  N   . ALA B 1 91 ? 20.140  -0.531  -35.215 1.00 32.84  ? 90  ALA B N   1 
ATOM   1439 C  CA  . ALA B 1 91 ? 20.300  0.506   -34.193 1.00 32.57  ? 90  ALA B CA  1 
ATOM   1440 C  C   . ALA B 1 91 ? 21.279  0.119   -33.085 1.00 41.14  ? 90  ALA B C   1 
ATOM   1441 O  O   . ALA B 1 91 ? 21.563  -1.056  -32.840 1.00 35.35  ? 90  ALA B O   1 
ATOM   1442 C  CB  . ALA B 1 91 ? 18.943  0.863   -33.627 1.00 30.78  ? 90  ALA B CB  1 
ATOM   1443 N  N   . SER B 1 92 ? 21.803  1.142   -32.379 1.00 38.41  ? 91  SER B N   1 
ATOM   1444 C  CA  . SER B 1 92 ? 22.457  0.957   -31.101 1.00 40.11  ? 91  SER B CA  1 
ATOM   1445 C  C   . SER B 1 92 ? 21.384  0.682   -30.046 1.00 41.59  ? 91  SER B C   1 
ATOM   1446 O  O   . SER B 1 92 ? 20.425  1.451   -29.934 1.00 47.23  ? 91  SER B O   1 
ATOM   1447 C  CB  . SER B 1 92 ? 23.225  2.227   -30.707 1.00 41.76  ? 91  SER B CB  1 
ATOM   1448 O  OG  . SER B 1 92 ? 23.741  2.064   -29.399 1.00 46.52  ? 91  SER B OG  1 
ATOM   1449 N  N   . TYR B 1 93 ? 21.567  -0.410  -29.296 1.00 41.79  ? 92  TYR B N   1 
ATOM   1450 C  CA  . TYR B 1 93 ? 20.676  -0.829  -28.222 1.00 44.32  ? 92  TYR B CA  1 
ATOM   1451 C  C   . TYR B 1 93 ? 21.431  -0.710  -26.903 1.00 54.94  ? 92  TYR B C   1 
ATOM   1452 O  O   . TYR B 1 93 ? 21.082  -1.363  -25.924 1.00 57.29  ? 92  TYR B O   1 
ATOM   1453 C  CB  . TYR B 1 93 ? 20.041  -2.207  -28.475 1.00 36.70  ? 92  TYR B CB  1 
ATOM   1454 C  CG  . TYR B 1 93 ? 19.027  -2.162  -29.602 1.00 32.95  ? 92  TYR B CG  1 
ATOM   1455 C  CD1 . TYR B 1 93 ? 17.728  -1.725  -29.385 1.00 36.39  ? 92  TYR B CD1 1 
ATOM   1456 C  CD2 . TYR B 1 93 ? 19.366  -2.529  -30.910 1.00 37.13  ? 92  TYR B CD2 1 
ATOM   1457 C  CE1 . TYR B 1 93 ? 16.805  -1.619  -30.405 1.00 35.40  ? 92  TYR B CE1 1 
ATOM   1458 C  CE2 . TYR B 1 93 ? 18.447  -2.385  -31.937 1.00 31.98  ? 92  TYR B CE2 1 
ATOM   1459 C  CZ  . TYR B 1 93 ? 17.151  -1.982  -31.688 1.00 34.58  ? 92  TYR B CZ  1 
ATOM   1460 O  OH  . TYR B 1 93 ? 16.177  -1.850  -32.627 1.00 34.49  ? 92  TYR B OH  1 
ATOM   1461 N  N   . SER B 1 94 ? 22.467  0.140   -26.914 1.00 57.58  ? 93  SER B N   1 
ATOM   1462 C  CA  . SER B 1 94 ? 23.304  0.425   -25.759 1.00 65.71  ? 93  SER B CA  1 
ATOM   1463 C  C   . SER B 1 94 ? 22.451  1.093   -24.672 1.00 75.65  ? 93  SER B C   1 
ATOM   1464 O  O   . SER B 1 94 ? 21.666  1.995   -25.038 1.00 75.83  ? 93  SER B O   1 
ATOM   1465 C  CB  . SER B 1 94 ? 24.469  1.311   -26.140 1.00 69.02  ? 93  SER B CB  1 
ATOM   1466 O  OG  . SER B 1 94 ? 25.422  0.603   -26.918 1.00 72.66  ? 93  SER B OG  1 
ATOM   1467 O  OXT . SER B 1 94 ? 22.596  0.685   -23.497 1.00 88.49  ? 93  SER B OXT 1 
ATOM   1468 N  N   . HIS C 1 4  ? 32.500  -23.878 26.937  1.00 69.48  ? 3   HIS C N   1 
ATOM   1469 C  CA  . HIS C 1 4  ? 31.806  -22.733 27.587  1.00 78.56  ? 3   HIS C CA  1 
ATOM   1470 C  C   . HIS C 1 4  ? 31.188  -23.210 28.902  1.00 80.43  ? 3   HIS C C   1 
ATOM   1471 O  O   . HIS C 1 4  ? 31.882  -23.778 29.750  1.00 76.56  ? 3   HIS C O   1 
ATOM   1472 C  CB  . HIS C 1 4  ? 30.832  -22.066 26.603  1.00 76.98  ? 3   HIS C CB  1 
ATOM   1473 N  N   . ALA C 1 5  ? 29.876  -22.979 29.047  1.00 80.99  ? 4   ALA C N   1 
ATOM   1474 C  CA  . ALA C 1 5  ? 29.102  -23.350 30.222  1.00 72.85  ? 4   ALA C CA  1 
ATOM   1475 C  C   . ALA C 1 5  ? 27.618  -23.222 29.902  1.00 74.59  ? 4   ALA C C   1 
ATOM   1476 O  O   . ALA C 1 5  ? 27.205  -22.303 29.195  1.00 71.70  ? 4   ALA C O   1 
ATOM   1477 C  CB  . ALA C 1 5  ? 29.452  -22.438 31.360  1.00 71.63  ? 4   ALA C CB  1 
ATOM   1478 N  N   . PHE C 1 6  ? 26.821  -24.138 30.455  1.00 60.80  ? 5   PHE C N   1 
ATOM   1479 C  CA  . PHE C 1 6  ? 25.452  -24.277 30.008  1.00 56.26  ? 5   PHE C CA  1 
ATOM   1480 C  C   . PHE C 1 6  ? 24.541  -24.333 31.228  1.00 56.33  ? 5   PHE C C   1 
ATOM   1481 O  O   . PHE C 1 6  ? 24.819  -25.074 32.164  1.00 74.43  ? 5   PHE C O   1 
ATOM   1482 C  CB  . PHE C 1 6  ? 25.366  -25.491 29.064  1.00 53.19  ? 5   PHE C CB  1 
ATOM   1483 C  CG  . PHE C 1 6  ? 26.144  -25.383 27.753  1.00 49.87  ? 5   PHE C CG  1 
ATOM   1484 C  CD1 . PHE C 1 6  ? 27.327  -26.088 27.554  1.00 52.74  ? 5   PHE C CD1 1 
ATOM   1485 C  CD2 . PHE C 1 6  ? 25.705  -24.560 26.716  1.00 55.66  ? 5   PHE C CD2 1 
ATOM   1486 C  CE1 . PHE C 1 6  ? 28.037  -25.987 26.363  1.00 52.24  ? 5   PHE C CE1 1 
ATOM   1487 C  CE2 . PHE C 1 6  ? 26.410  -24.479 25.518  1.00 52.58  ? 5   PHE C CE2 1 
ATOM   1488 C  CZ  . PHE C 1 6  ? 27.572  -25.188 25.339  1.00 45.32  ? 5   PHE C CZ  1 
ATOM   1489 N  N   . LYS C 1 7  ? 23.464  -23.542 31.210  1.00 55.27  ? 6   LYS C N   1 
ATOM   1490 C  CA  . LYS C 1 7  ? 22.469  -23.568 32.274  1.00 57.55  ? 6   LYS C CA  1 
ATOM   1491 C  C   . LYS C 1 7  ? 21.134  -23.946 31.644  1.00 54.76  ? 6   LYS C C   1 
ATOM   1492 O  O   . LYS C 1 7  ? 20.992  -23.829 30.432  1.00 61.07  ? 6   LYS C O   1 
ATOM   1493 C  CB  . LYS C 1 7  ? 22.421  -22.216 33.001  1.00 62.44  ? 6   LYS C CB  1 
ATOM   1494 N  N   . PRO C 1 8  ? 20.121  -24.429 32.403  1.00 53.56  ? 7   PRO C N   1 
ATOM   1495 C  CA  . PRO C 1 8  ? 18.831  -24.768 31.803  1.00 59.65  ? 7   PRO C CA  1 
ATOM   1496 C  C   . PRO C 1 8  ? 18.364  -23.569 30.979  1.00 61.48  ? 7   PRO C C   1 
ATOM   1497 O  O   . PRO C 1 8  ? 18.609  -22.424 31.361  1.00 65.29  ? 7   PRO C O   1 
ATOM   1498 C  CB  . PRO C 1 8  ? 17.944  -25.054 33.021  1.00 64.61  ? 7   PRO C CB  1 
ATOM   1499 C  CG  . PRO C 1 8  ? 18.921  -25.556 34.065  1.00 57.60  ? 7   PRO C CG  1 
ATOM   1500 C  CD  . PRO C 1 8  ? 20.176  -24.710 33.851  1.00 54.55  ? 7   PRO C CD  1 
ATOM   1501 N  N   . GLY C 1 9  ? 17.764  -23.848 29.813  1.00 61.50  ? 8   GLY C N   1 
ATOM   1502 C  CA  . GLY C 1 9  ? 17.163  -22.817 28.981  1.00 56.30  ? 8   GLY C CA  1 
ATOM   1503 C  C   . GLY C 1 9  ? 18.077  -22.320 27.860  1.00 57.89  ? 8   GLY C C   1 
ATOM   1504 O  O   . GLY C 1 9  ? 17.577  -21.781 26.877  1.00 66.17  ? 8   GLY C O   1 
ATOM   1505 N  N   . ASP C 1 10 ? 19.399  -22.486 28.015  1.00 47.37  ? 9   ASP C N   1 
ATOM   1506 C  CA  . ASP C 1 10 ? 20.379  -22.173 26.985  1.00 43.37  ? 9   ASP C CA  1 
ATOM   1507 C  C   . ASP C 1 10 ? 20.085  -22.917 25.666  1.00 44.69  ? 9   ASP C C   1 
ATOM   1508 O  O   . ASP C 1 10 ? 19.865  -24.139 25.647  1.00 40.20  ? 9   ASP C O   1 
ATOM   1509 C  CB  . ASP C 1 10 ? 21.806  -22.420 27.454  1.00 46.38  ? 9   ASP C CB  1 
ATOM   1510 C  CG  . ASP C 1 10 ? 22.377  -21.497 28.531  1.00 56.96  ? 9   ASP C CG  1 
ATOM   1511 O  OD1 . ASP C 1 10 ? 21.719  -20.504 28.869  1.00 61.51  ? 9   ASP C OD1 1 
ATOM   1512 O  OD2 . ASP C 1 10 ? 23.489  -21.776 29.032  1.00 59.17  ? 9   ASP C OD2 1 
ATOM   1513 N  N   . LEU C 1 11 ? 20.147  -22.174 24.552  1.00 45.53  ? 10  LEU C N   1 
ATOM   1514 C  CA  . LEU C 1 11 ? 19.870  -22.721 23.225  1.00 43.25  ? 10  LEU C CA  1 
ATOM   1515 C  C   . LEU C 1 11 ? 21.163  -23.174 22.535  1.00 39.84  ? 10  LEU C C   1 
ATOM   1516 O  O   . LEU C 1 11 ? 22.158  -22.448 22.526  1.00 43.02  ? 10  LEU C O   1 
ATOM   1517 C  CB  . LEU C 1 11 ? 19.070  -21.694 22.414  1.00 37.33  ? 10  LEU C CB  1 
ATOM   1518 C  CG  . LEU C 1 11 ? 17.824  -21.133 23.108  1.00 36.86  ? 10  LEU C CG  1 
ATOM   1519 C  CD1 . LEU C 1 11 ? 17.160  -20.166 22.141  1.00 40.25  ? 10  LEU C CD1 1 
ATOM   1520 C  CD2 . LEU C 1 11 ? 16.868  -22.275 23.454  1.00 40.08  ? 10  LEU C CD2 1 
ATOM   1521 N  N   . VAL C 1 12 ? 21.155  -24.382 21.906  1.00 34.43  ? 11  VAL C N   1 
ATOM   1522 C  CA  . VAL C 1 12 ? 22.387  -24.993 21.416  1.00 36.21  ? 11  VAL C CA  1 
ATOM   1523 C  C   . VAL C 1 12 ? 22.102  -25.712 20.082  1.00 35.48  ? 11  VAL C C   1 
ATOM   1524 O  O   . VAL C 1 12 ? 20.935  -25.905 19.766  1.00 36.60  ? 11  VAL C O   1 
ATOM   1525 C  CB  . VAL C 1 12 ? 23.011  -26.002 22.414  1.00 36.80  ? 11  VAL C CB  1 
ATOM   1526 C  CG1 . VAL C 1 12 ? 23.329  -25.346 23.764  1.00 39.33  ? 11  VAL C CG1 1 
ATOM   1527 C  CG2 . VAL C 1 12 ? 22.141  -27.248 22.595  1.00 38.05  ? 11  VAL C CG2 1 
ATOM   1528 N  N   . PHE C 1 13 ? 23.159  -26.041 19.322  1.00 34.19  ? 12  PHE C N   1 
ATOM   1529 C  CA  . PHE C 1 13 ? 23.109  -27.196 18.412  1.00 32.19  ? 12  PHE C CA  1 
ATOM   1530 C  C   . PHE C 1 13 ? 23.730  -28.396 19.131  1.00 33.46  ? 12  PHE C C   1 
ATOM   1531 O  O   . PHE C 1 13 ? 24.841  -28.309 19.702  1.00 34.06  ? 12  PHE C O   1 
ATOM   1532 C  CB  . PHE C 1 13 ? 23.751  -26.990 17.027  1.00 37.02  ? 12  PHE C CB  1 
ATOM   1533 C  CG  . PHE C 1 13 ? 22.983  -25.989 16.191  1.00 39.67  ? 12  PHE C CG  1 
ATOM   1534 C  CD1 . PHE C 1 13 ? 21.957  -26.422 15.342  1.00 40.06  ? 12  PHE C CD1 1 
ATOM   1535 C  CD2 . PHE C 1 13 ? 23.259  -24.620 16.270  1.00 37.56  ? 12  PHE C CD2 1 
ATOM   1536 C  CE1 . PHE C 1 13 ? 21.223  -25.501 14.605  1.00 38.16  ? 12  PHE C CE1 1 
ATOM   1537 C  CE2 . PHE C 1 13 ? 22.502  -23.715 15.545  1.00 39.81  ? 12  PHE C CE2 1 
ATOM   1538 C  CZ  . PHE C 1 13 ? 21.490  -24.161 14.711  1.00 35.33  ? 12  PHE C CZ  1 
ATOM   1539 N  N   . ALA C 1 14 ? 23.034  -29.550 19.098  1.00 31.14  ? 13  ALA C N   1 
ATOM   1540 C  CA  . ALA C 1 14 ? 23.481  -30.735 19.827  1.00 31.01  ? 13  ALA C CA  1 
ATOM   1541 C  C   . ALA C 1 14 ? 23.823  -31.845 18.831  1.00 33.39  ? 13  ALA C C   1 
ATOM   1542 O  O   . ALA C 1 14 ? 22.987  -32.128 17.961  1.00 30.15  ? 13  ALA C O   1 
ATOM   1543 C  CB  . ALA C 1 14 ? 22.437  -31.178 20.804  1.00 32.06  ? 13  ALA C CB  1 
ATOM   1544 N  N   . LYS C 1 15 ? 25.021  -32.451 18.980  1.00 32.54  ? 14  LYS C N   1 
ATOM   1545 C  CA  . LYS C 1 15 ? 25.483  -33.451 18.020  1.00 32.37  ? 14  LYS C CA  1 
ATOM   1546 C  C   . LYS C 1 15 ? 25.486  -34.856 18.615  1.00 33.75  ? 14  LYS C C   1 
ATOM   1547 O  O   . LYS C 1 15 ? 26.233  -35.147 19.555  1.00 33.71  ? 14  LYS C O   1 
ATOM   1548 C  CB  . LYS C 1 15 ? 26.887  -33.113 17.481  1.00 34.09  ? 14  LYS C CB  1 
ATOM   1549 C  CG  . LYS C 1 15 ? 27.375  -34.095 16.414  1.00 33.91  ? 14  LYS C CG  1 
ATOM   1550 C  CD  . LYS C 1 15 ? 26.552  -33.963 15.132  1.00 35.04  ? 14  LYS C CD  1 
ATOM   1551 C  CE  . LYS C 1 15 ? 27.120  -34.710 13.955  1.00 39.02  ? 14  LYS C CE  1 
ATOM   1552 N  NZ  . LYS C 1 15 ? 26.907  -36.144 14.095  1.00 33.68  ? 14  LYS C NZ  1 
ATOM   1553 N  N   . MET C 1 16 ? 24.665  -35.760 18.051  1.00 28.54  ? 15  MET C N   1 
ATOM   1554 C  CA  . MET C 1 16 ? 24.702  -37.179 18.392  1.00 29.65  ? 15  MET C CA  1 
ATOM   1555 C  C   . MET C 1 16 ? 25.184  -37.988 17.184  1.00 35.06  ? 15  MET C C   1 
ATOM   1556 O  O   . MET C 1 16 ? 24.997  -37.578 16.038  1.00 29.98  ? 15  MET C O   1 
ATOM   1557 C  CB  . MET C 1 16 ? 23.303  -37.682 18.742  1.00 32.10  ? 15  MET C CB  1 
ATOM   1558 C  CG  . MET C 1 16 ? 22.594  -36.911 19.861  1.00 34.41  ? 15  MET C CG  1 
ATOM   1559 S  SD  . MET C 1 16 ? 21.034  -37.721 20.262  1.00 40.05  ? 15  MET C SD  1 
ATOM   1560 C  CE  . MET C 1 16 ? 19.989  -37.177 18.898  1.00 38.99  ? 15  MET C CE  1 
ATOM   1561 N  N   . LYS C 1 17 ? 25.772  -39.165 17.456  1.00 33.66  ? 16  LYS C N   1 
ATOM   1562 C  CA  . LYS C 1 17 ? 26.196  -40.029 16.358  1.00 37.21  ? 16  LYS C CA  1 
ATOM   1563 C  C   . LYS C 1 17 ? 24.976  -40.376 15.502  1.00 31.07  ? 16  LYS C C   1 
ATOM   1564 O  O   . LYS C 1 17 ? 23.953  -40.821 16.028  1.00 33.09  ? 16  LYS C O   1 
ATOM   1565 C  CB  . LYS C 1 17 ? 26.777  -41.338 16.908  1.00 38.55  ? 16  LYS C CB  1 
ATOM   1566 C  CG  . LYS C 1 17 ? 27.435  -42.283 15.875  1.00 42.37  ? 16  LYS C CG  1 
ATOM   1567 C  CD  . LYS C 1 17 ? 28.769  -41.725 15.380  1.00 44.37  ? 16  LYS C CD  1 
ATOM   1568 C  CE  . LYS C 1 17 ? 29.443  -42.557 14.311  1.00 50.86  ? 16  LYS C CE  1 
ATOM   1569 N  NZ  . LYS C 1 17 ? 30.671  -41.861 13.902  1.00 48.00  ? 16  LYS C NZ  1 
ATOM   1570 N  N   . GLY C 1 18 ? 25.135  -40.177 14.184  1.00 35.94  ? 17  GLY C N   1 
ATOM   1571 C  CA  . GLY C 1 18 ? 24.133  -40.614 13.220  1.00 36.89  ? 17  GLY C CA  1 
ATOM   1572 C  C   . GLY C 1 18 ? 23.060  -39.565 12.956  1.00 35.81  ? 17  GLY C C   1 
ATOM   1573 O  O   . GLY C 1 18 ? 22.067  -39.875 12.315  1.00 32.38  ? 17  GLY C O   1 
ATOM   1574 N  N   . TYR C 1 19 ? 23.250  -38.353 13.499  1.00 32.24  ? 18  TYR C N   1 
ATOM   1575 C  CA  . TYR C 1 19 ? 22.347  -37.227 13.229  1.00 32.11  ? 18  TYR C CA  1 
ATOM   1576 C  C   . TYR C 1 19 ? 23.123  -35.941 12.979  1.00 31.19  ? 18  TYR C C   1 
ATOM   1577 O  O   . TYR C 1 19 ? 24.231  -35.749 13.498  1.00 31.45  ? 18  TYR C O   1 
ATOM   1578 C  CB  . TYR C 1 19 ? 21.474  -36.926 14.458  1.00 26.55  ? 18  TYR C CB  1 
ATOM   1579 C  CG  . TYR C 1 19 ? 20.662  -38.133 14.869  1.00 30.92  ? 18  TYR C CG  1 
ATOM   1580 C  CD1 . TYR C 1 19 ? 21.211  -39.155 15.647  1.00 31.95  ? 18  TYR C CD1 1 
ATOM   1581 C  CD2 . TYR C 1 19 ? 19.335  -38.237 14.465  1.00 31.13  ? 18  TYR C CD2 1 
ATOM   1582 C  CE1 . TYR C 1 19 ? 20.462  -40.259 16.022  1.00 33.40  ? 18  TYR C CE1 1 
ATOM   1583 C  CE2 . TYR C 1 19 ? 18.581  -39.339 14.837  1.00 36.50  ? 18  TYR C CE2 1 
ATOM   1584 C  CZ  . TYR C 1 19 ? 19.139  -40.332 15.622  1.00 36.11  ? 18  TYR C CZ  1 
ATOM   1585 O  OH  . TYR C 1 19 ? 18.373  -41.430 15.927  1.00 44.77  ? 18  TYR C OH  1 
ATOM   1586 N  N   . PRO C 1 20 ? 22.548  -34.998 12.193  1.00 31.57  ? 19  PRO C N   1 
ATOM   1587 C  CA  . PRO C 1 20 ? 23.180  -33.708 11.934  1.00 29.93  ? 19  PRO C CA  1 
ATOM   1588 C  C   . PRO C 1 20 ? 23.119  -32.894 13.224  1.00 32.38  ? 19  PRO C C   1 
ATOM   1589 O  O   . PRO C 1 20 ? 22.350  -33.215 14.144  1.00 29.22  ? 19  PRO C O   1 
ATOM   1590 C  CB  . PRO C 1 20 ? 22.291  -33.090 10.834  1.00 34.78  ? 19  PRO C CB  1 
ATOM   1591 C  CG  . PRO C 1 20 ? 20.928  -33.713 11.064  1.00 31.24  ? 19  PRO C CG  1 
ATOM   1592 C  CD  . PRO C 1 20 ? 21.210  -35.124 11.555  1.00 30.51  ? 19  PRO C CD  1 
ATOM   1593 N  N   . HIS C 1 21 ? 23.948  -31.859 13.284  1.00 31.88  ? 20  HIS C N   1 
ATOM   1594 C  CA  . HIS C 1 21 ? 23.886  -30.970 14.441  1.00 31.19  ? 20  HIS C CA  1 
ATOM   1595 C  C   . HIS C 1 21 ? 22.460  -30.453 14.560  1.00 35.19  ? 20  HIS C C   1 
ATOM   1596 O  O   . HIS C 1 21 ? 21.917  -29.936 13.590  1.00 32.28  ? 20  HIS C O   1 
ATOM   1597 C  CB  . HIS C 1 21 ? 24.836  -29.782 14.258  1.00 35.50  ? 20  HIS C CB  1 
ATOM   1598 C  CG  . HIS C 1 21 ? 26.267  -30.176 14.350  1.00 35.07  ? 20  HIS C CG  1 
ATOM   1599 N  ND1 . HIS C 1 21 ? 26.968  -30.772 13.323  1.00 37.86  ? 20  HIS C ND1 1 
ATOM   1600 C  CD2 . HIS C 1 21 ? 27.123  -30.077 15.384  1.00 40.13  ? 20  HIS C CD2 1 
ATOM   1601 C  CE1 . HIS C 1 21 ? 28.203  -31.039 13.735  1.00 45.80  ? 20  HIS C CE1 1 
ATOM   1602 N  NE2 . HIS C 1 21 ? 28.322  -30.600 14.974  1.00 40.25  ? 20  HIS C NE2 1 
ATOM   1603 N  N   . TRP C 1 22 ? 21.868  -30.535 15.763  1.00 30.28  ? 21  TRP C N   1 
ATOM   1604 C  CA  . TRP C 1 22 ? 20.418  -30.457 15.868  1.00 27.96  ? 21  TRP C CA  1 
ATOM   1605 C  C   . TRP C 1 22 ? 19.990  -29.297 16.770  1.00 29.84  ? 21  TRP C C   1 
ATOM   1606 O  O   . TRP C 1 22 ? 20.507  -29.149 17.890  1.00 30.33  ? 21  TRP C O   1 
ATOM   1607 C  CB  . TRP C 1 22 ? 19.865  -31.785 16.428  1.00 25.70  ? 21  TRP C CB  1 
ATOM   1608 C  CG  . TRP C 1 22 ? 18.413  -31.980 16.065  1.00 27.27  ? 21  TRP C CG  1 
ATOM   1609 C  CD1 . TRP C 1 22 ? 17.324  -31.406 16.653  1.00 28.12  ? 21  TRP C CD1 1 
ATOM   1610 C  CD2 . TRP C 1 22 ? 17.929  -32.861 15.021  1.00 29.12  ? 21  TRP C CD2 1 
ATOM   1611 N  NE1 . TRP C 1 22 ? 16.187  -31.823 15.991  1.00 30.79  ? 21  TRP C NE1 1 
ATOM   1612 C  CE2 . TRP C 1 22 ? 16.526  -32.719 15.007  1.00 29.82  ? 21  TRP C CE2 1 
ATOM   1613 C  CE3 . TRP C 1 22 ? 18.534  -33.753 14.122  1.00 27.64  ? 21  TRP C CE3 1 
ATOM   1614 C  CZ2 . TRP C 1 22 ? 15.717  -33.440 14.122  1.00 30.64  ? 21  TRP C CZ2 1 
ATOM   1615 C  CZ3 . TRP C 1 22 ? 17.739  -34.442 13.214  1.00 31.34  ? 21  TRP C CZ3 1 
ATOM   1616 C  CH2 . TRP C 1 22 ? 16.339  -34.299 13.243  1.00 29.39  ? 21  TRP C CH2 1 
ATOM   1617 N  N   . PRO C 1 23 ? 18.986  -28.462 16.403  1.00 33.47  ? 22  PRO C N   1 
ATOM   1618 C  CA  . PRO C 1 23 ? 18.571  -27.369 17.297  1.00 30.59  ? 22  PRO C CA  1 
ATOM   1619 C  C   . PRO C 1 23 ? 18.029  -27.918 18.611  1.00 29.35  ? 22  PRO C C   1 
ATOM   1620 O  O   . PRO C 1 23 ? 17.176  -28.804 18.617  1.00 29.02  ? 22  PRO C O   1 
ATOM   1621 C  CB  . PRO C 1 23 ? 17.487  -26.643 16.431  1.00 30.48  ? 22  PRO C CB  1 
ATOM   1622 C  CG  . PRO C 1 23 ? 16.961  -27.705 15.505  1.00 30.46  ? 22  PRO C CG  1 
ATOM   1623 C  CD  . PRO C 1 23 ? 18.243  -28.456 15.116  1.00 30.73  ? 22  PRO C CD  1 
ATOM   1624 N  N   . ALA C 1 24 ? 18.539  -27.387 19.736  1.00 29.54  ? 23  ALA C N   1 
ATOM   1625 C  CA  . ALA C 1 24 ? 18.214  -27.984 21.032  1.00 32.76  ? 23  ALA C CA  1 
ATOM   1626 C  C   . ALA C 1 24 ? 18.270  -26.934 22.145  1.00 35.19  ? 23  ALA C C   1 
ATOM   1627 O  O   . ALA C 1 24 ? 18.733  -25.801 21.920  1.00 38.15  ? 23  ALA C O   1 
ATOM   1628 C  CB  . ALA C 1 24 ? 19.232  -29.118 21.308  1.00 33.27  ? 23  ALA C CB  1 
ATOM   1629 N  N   . ARG C 1 25 ? 17.869  -27.339 23.359  1.00 37.28  ? 24  ARG C N   1 
ATOM   1630 C  CA  . ARG C 1 25 ? 18.132  -26.537 24.547  1.00 36.97  ? 24  ARG C CA  1 
ATOM   1631 C  C   . ARG C 1 25 ? 18.621  -27.424 25.704  1.00 40.23  ? 24  ARG C C   1 
ATOM   1632 O  O   . ARG C 1 25 ? 18.251  -28.601 25.778  1.00 41.04  ? 24  ARG C O   1 
ATOM   1633 C  CB  . ARG C 1 25 ? 16.882  -25.777 24.992  1.00 37.91  ? 24  ARG C CB  1 
ATOM   1634 C  CG  . ARG C 1 25 ? 15.675  -26.577 25.449  1.00 46.83  ? 24  ARG C CG  1 
ATOM   1635 C  CD  . ARG C 1 25 ? 14.519  -25.672 25.868  1.00 49.41  ? 24  ARG C CD  1 
ATOM   1636 N  NE  . ARG C 1 25 ? 13.320  -26.504 26.066  1.00 52.70  ? 24  ARG C NE  1 
ATOM   1637 C  CZ  . ARG C 1 25 ? 12.041  -26.137 26.026  1.00 56.29  ? 24  ARG C CZ  1 
ATOM   1638 N  NH1 . ARG C 1 25 ? 11.682  -24.926 25.623  1.00 47.78  ? 24  ARG C NH1 1 
ATOM   1639 N  NH2 . ARG C 1 25 ? 11.109  -27.020 26.348  1.00 54.59  ? 24  ARG C NH2 1 
ATOM   1640 N  N   . ILE C 1 26 ? 19.359  -26.809 26.637  1.00 37.62  ? 25  ILE C N   1 
ATOM   1641 C  CA  . ILE C 1 26 ? 19.663  -27.398 27.944  1.00 40.91  ? 25  ILE C CA  1 
ATOM   1642 C  C   . ILE C 1 26 ? 18.410  -27.397 28.815  1.00 49.00  ? 25  ILE C C   1 
ATOM   1643 O  O   . ILE C 1 26 ? 17.786  -26.353 28.975  1.00 54.06  ? 25  ILE C O   1 
ATOM   1644 C  CB  . ILE C 1 26 ? 20.795  -26.624 28.646  1.00 40.58  ? 25  ILE C CB  1 
ATOM   1645 C  CG1 . ILE C 1 26 ? 21.994  -26.318 27.755  1.00 40.35  ? 25  ILE C CG1 1 
ATOM   1646 C  CG2 . ILE C 1 26 ? 21.217  -27.325 29.947  1.00 43.98  ? 25  ILE C CG2 1 
ATOM   1647 C  CD1 . ILE C 1 26 ? 22.824  -27.515 27.317  1.00 42.07  ? 25  ILE C CD1 1 
ATOM   1648 N  N   . ASP C 1 27 ? 18.065  -28.555 29.394  1.00 50.58  ? 26  ASP C N   1 
ATOM   1649 C  CA  . ASP C 1 27 ? 16.997  -28.664 30.381  1.00 60.80  ? 26  ASP C CA  1 
ATOM   1650 C  C   . ASP C 1 27 ? 17.555  -28.616 31.805  1.00 63.93  ? 26  ASP C C   1 
ATOM   1651 O  O   . ASP C 1 27 ? 18.748  -28.842 32.014  1.00 65.04  ? 26  ASP C O   1 
ATOM   1652 C  CB  . ASP C 1 27 ? 16.266  -29.992 30.271  1.00 60.68  ? 26  ASP C CB  1 
ATOM   1653 C  CG  . ASP C 1 27 ? 15.082  -30.041 29.322  1.00 69.10  ? 26  ASP C CG  1 
ATOM   1654 O  OD1 . ASP C 1 27 ? 14.893  -29.052 28.570  1.00 65.80  ? 26  ASP C OD1 1 
ATOM   1655 O  OD2 . ASP C 1 27 ? 14.345  -31.058 29.377  1.00 68.54  ? 26  ASP C OD2 1 
ATOM   1656 N  N   . ASP C 1 28 ? 16.667  -28.339 32.777  1.00 73.16  ? 27  ASP C N   1 
ATOM   1657 C  CA  . ASP C 1 28 ? 16.933  -28.562 34.192  1.00 72.08  ? 27  ASP C CA  1 
ATOM   1658 C  C   . ASP C 1 28 ? 16.681  -30.037 34.478  1.00 75.68  ? 27  ASP C C   1 
ATOM   1659 O  O   . ASP C 1 28 ? 15.939  -30.672 33.734  1.00 70.86  ? 27  ASP C O   1 
ATOM   1660 C  CB  . ASP C 1 28 ? 16.057  -27.708 35.095  1.00 66.76  ? 27  ASP C CB  1 
ATOM   1661 N  N   . ILE C 1 29 ? 17.309  -30.563 35.541  1.00 79.50  ? 28  ILE C N   1 
ATOM   1662 C  CA  . ILE C 1 29 ? 17.163  -31.961 35.914  1.00 73.89  ? 28  ILE C CA  1 
ATOM   1663 C  C   . ILE C 1 29 ? 16.067  -32.077 36.985  1.00 71.36  ? 28  ILE C C   1 
ATOM   1664 O  O   . ILE C 1 29 ? 16.088  -31.233 37.901  1.00 78.64  ? 28  ILE C O   1 
ATOM   1665 C  CB  . ILE C 1 29 ? 18.503  -32.554 36.390  1.00 72.06  ? 28  ILE C CB  1 
ATOM   1666 N  N   . ALA C 1 33 ? 14.843  -36.660 40.577  1.00 68.51  ? 32  ALA C N   1 
ATOM   1667 C  CA  . ALA C 1 33 ? 15.133  -37.319 39.279  1.00 67.12  ? 32  ALA C CA  1 
ATOM   1668 C  C   . ALA C 1 33 ? 16.384  -38.191 39.392  1.00 69.50  ? 32  ALA C C   1 
ATOM   1669 O  O   . ALA C 1 33 ? 17.102  -38.140 40.393  1.00 62.98  ? 32  ALA C O   1 
ATOM   1670 C  CB  . ALA C 1 33 ? 15.274  -36.273 38.188  1.00 58.03  ? 32  ALA C CB  1 
ATOM   1671 N  N   . VAL C 1 34 ? 16.630  -39.022 38.369  1.00 74.43  ? 33  VAL C N   1 
ATOM   1672 C  CA  . VAL C 1 34 ? 17.914  -39.705 38.290  1.00 73.81  ? 33  VAL C CA  1 
ATOM   1673 C  C   . VAL C 1 34 ? 18.905  -38.804 37.555  1.00 74.24  ? 33  VAL C C   1 
ATOM   1674 O  O   . VAL C 1 34 ? 18.554  -38.124 36.582  1.00 61.59  ? 33  VAL C O   1 
ATOM   1675 C  CB  . VAL C 1 34 ? 18.041  -41.202 37.928  1.00 72.03  ? 33  VAL C CB  1 
ATOM   1676 C  CG1 . VAL C 1 34 ? 19.155  -41.482 36.923  1.00 78.81  ? 33  VAL C CG1 1 
ATOM   1677 C  CG2 . VAL C 1 34 ? 18.242  -42.045 39.182  1.00 69.97  ? 33  VAL C CG2 1 
ATOM   1678 N  N   . LYS C 1 35 ? 20.131  -38.790 38.100  1.00 65.38  ? 34  LYS C N   1 
ATOM   1679 C  CA  . LYS C 1 35 ? 21.171  -37.846 37.729  1.00 62.39  ? 34  LYS C CA  1 
ATOM   1680 C  C   . LYS C 1 35 ? 21.674  -38.202 36.336  1.00 58.11  ? 34  LYS C C   1 
ATOM   1681 O  O   . LYS C 1 35 ? 21.616  -39.365 35.927  1.00 59.53  ? 34  LYS C O   1 
ATOM   1682 C  CB  . LYS C 1 35 ? 22.306  -37.864 38.761  1.00 56.68  ? 34  LYS C CB  1 
ATOM   1683 N  N   . PRO C 1 36 ? 22.144  -37.190 35.570  1.00 57.36  ? 35  PRO C N   1 
ATOM   1684 C  CA  . PRO C 1 36 ? 22.849  -37.438 34.314  1.00 59.55  ? 35  PRO C CA  1 
ATOM   1685 C  C   . PRO C 1 36 ? 23.974  -38.435 34.584  1.00 55.92  ? 35  PRO C C   1 
ATOM   1686 O  O   . PRO C 1 36 ? 24.377  -38.636 35.736  1.00 56.66  ? 35  PRO C O   1 
ATOM   1687 C  CB  . PRO C 1 36 ? 23.380  -36.027 33.940  1.00 58.69  ? 35  PRO C CB  1 
ATOM   1688 C  CG  . PRO C 1 36 ? 22.389  -35.069 34.577  1.00 59.47  ? 35  PRO C CG  1 
ATOM   1689 C  CD  . PRO C 1 36 ? 21.983  -35.754 35.873  1.00 57.41  ? 35  PRO C CD  1 
ATOM   1690 N  N   . PRO C 1 37 ? 24.508  -39.124 33.555  1.00 54.68  ? 36  PRO C N   1 
ATOM   1691 C  CA  . PRO C 1 37 ? 25.797  -39.786 33.724  1.00 49.05  ? 36  PRO C CA  1 
ATOM   1692 C  C   . PRO C 1 37 ? 26.756  -38.645 34.066  1.00 48.96  ? 36  PRO C C   1 
ATOM   1693 O  O   . PRO C 1 37 ? 26.434  -37.462 33.876  1.00 44.51  ? 36  PRO C O   1 
ATOM   1694 C  CB  . PRO C 1 37 ? 26.027  -40.401 32.343  1.00 47.59  ? 36  PRO C CB  1 
ATOM   1695 C  CG  . PRO C 1 37 ? 24.612  -40.636 31.875  1.00 51.69  ? 36  PRO C CG  1 
ATOM   1696 C  CD  . PRO C 1 37 ? 23.910  -39.342 32.223  1.00 48.44  ? 36  PRO C CD  1 
ATOM   1697 N  N   . PRO C 1 38 ? 27.940  -38.960 34.645  1.00 44.12  ? 37  PRO C N   1 
ATOM   1698 C  CA  . PRO C 1 38 ? 28.911  -37.930 35.014  1.00 43.89  ? 37  PRO C CA  1 
ATOM   1699 C  C   . PRO C 1 38 ? 29.246  -37.034 33.831  1.00 39.03  ? 37  PRO C C   1 
ATOM   1700 O  O   . PRO C 1 38 ? 29.526  -37.509 32.721  1.00 43.62  ? 37  PRO C O   1 
ATOM   1701 C  CB  . PRO C 1 38 ? 30.121  -38.782 35.450  1.00 44.04  ? 37  PRO C CB  1 
ATOM   1702 C  CG  . PRO C 1 38 ? 29.464  -40.035 35.997  1.00 44.65  ? 37  PRO C CG  1 
ATOM   1703 C  CD  . PRO C 1 38 ? 28.398  -40.325 34.956  1.00 46.27  ? 37  PRO C CD  1 
ATOM   1704 N  N   . ASN C 1 39 ? 29.161  -35.726 34.106  1.00 42.12  ? 38  ASN C N   1 
ATOM   1705 C  CA  . ASN C 1 39 ? 29.608  -34.656 33.236  1.00 41.56  ? 38  ASN C CA  1 
ATOM   1706 C  C   . ASN C 1 39 ? 28.740  -34.586 31.978  1.00 44.91  ? 38  ASN C C   1 
ATOM   1707 O  O   . ASN C 1 39 ? 29.219  -34.105 30.950  1.00 49.67  ? 38  ASN C O   1 
ATOM   1708 C  CB  . ASN C 1 39 ? 31.086  -34.786 32.893  1.00 49.72  ? 38  ASN C CB  1 
ATOM   1709 C  CG  . ASN C 1 39 ? 31.660  -33.535 32.270  1.00 61.76  ? 38  ASN C CG  1 
ATOM   1710 O  OD1 . ASN C 1 39 ? 31.337  -32.421 32.701  1.00 73.13  ? 38  ASN C OD1 1 
ATOM   1711 N  ND2 . ASN C 1 39 ? 32.493  -33.688 31.249  1.00 55.99  ? 38  ASN C ND2 1 
ATOM   1712 N  N   . LYS C 1 40 ? 27.481  -35.047 32.067  1.00 38.14  ? 39  LYS C N   1 
ATOM   1713 C  CA  . LYS C 1 40 ? 26.569  -34.917 30.934  1.00 33.97  ? 39  LYS C CA  1 
ATOM   1714 C  C   . LYS C 1 40 ? 25.472  -33.904 31.261  1.00 37.74  ? 39  LYS C C   1 
ATOM   1715 O  O   . LYS C 1 40 ? 25.127  -33.725 32.418  1.00 38.56  ? 39  LYS C O   1 
ATOM   1716 C  CB  . LYS C 1 40 ? 25.802  -36.222 30.644  1.00 36.22  ? 39  LYS C CB  1 
ATOM   1717 C  CG  . LYS C 1 40 ? 26.664  -37.432 30.337  1.00 39.19  ? 39  LYS C CG  1 
ATOM   1718 C  CD  . LYS C 1 40 ? 27.341  -37.391 28.973  1.00 44.53  ? 39  LYS C CD  1 
ATOM   1719 C  CE  . LYS C 1 40 ? 28.236  -38.585 28.685  1.00 43.91  ? 39  LYS C CE  1 
ATOM   1720 N  NZ  . LYS C 1 40 ? 28.952  -38.427 27.416  1.00 52.93  ? 39  LYS C NZ  1 
ATOM   1721 N  N   . TYR C 1 41 ? 24.900  -33.260 30.224  1.00 33.91  ? 40  TYR C N   1 
ATOM   1722 C  CA  . TYR C 1 41 ? 23.807  -32.298 30.366  1.00 37.74  ? 40  TYR C CA  1 
ATOM   1723 C  C   . TYR C 1 41 ? 22.525  -32.924 29.833  1.00 39.65  ? 40  TYR C C   1 
ATOM   1724 O  O   . TYR C 1 41 ? 22.618  -33.649 28.841  1.00 35.18  ? 40  TYR C O   1 
ATOM   1725 C  CB  . TYR C 1 41 ? 24.023  -31.091 29.441  1.00 33.47  ? 40  TYR C CB  1 
ATOM   1726 C  CG  . TYR C 1 41 ? 25.168  -30.172 29.849  1.00 35.60  ? 40  TYR C CG  1 
ATOM   1727 C  CD1 . TYR C 1 41 ? 26.473  -30.422 29.426  1.00 36.99  ? 40  TYR C CD1 1 
ATOM   1728 C  CD2 . TYR C 1 41 ? 24.955  -29.105 30.726  1.00 41.38  ? 40  TYR C CD2 1 
ATOM   1729 C  CE1 . TYR C 1 41 ? 27.538  -29.643 29.845  1.00 48.28  ? 40  TYR C CE1 1 
ATOM   1730 C  CE2 . TYR C 1 41 ? 26.016  -28.305 31.128  1.00 40.60  ? 40  TYR C CE2 1 
ATOM   1731 C  CZ  . TYR C 1 41 ? 27.304  -28.581 30.706  1.00 47.29  ? 40  TYR C CZ  1 
ATOM   1732 O  OH  . TYR C 1 41 ? 28.340  -27.801 31.128  1.00 53.32  ? 40  TYR C OH  1 
ATOM   1733 N  N   . PRO C 1 42 ? 21.328  -32.602 30.409  1.00 38.42  ? 41  PRO C N   1 
ATOM   1734 C  CA  . PRO C 1 42 ? 20.020  -33.018 29.868  1.00 37.85  ? 41  PRO C CA  1 
ATOM   1735 C  C   . PRO C 1 42 ? 19.685  -32.119 28.676  1.00 39.02  ? 41  PRO C C   1 
ATOM   1736 O  O   . PRO C 1 42 ? 19.708  -30.891 28.801  1.00 41.26  ? 41  PRO C O   1 
ATOM   1737 C  CB  . PRO C 1 42 ? 19.016  -32.823 31.032  1.00 40.43  ? 41  PRO C CB  1 
ATOM   1738 C  CG  . PRO C 1 42 ? 19.749  -31.969 32.048  1.00 45.17  ? 41  PRO C CG  1 
ATOM   1739 C  CD  . PRO C 1 42 ? 21.170  -31.715 31.576  1.00 41.93  ? 41  PRO C CD  1 
ATOM   1740 N  N   . ILE C 1 43 ? 19.424  -32.755 27.524  1.00 37.20  ? 42  ILE C N   1 
ATOM   1741 C  CA  . ILE C 1 43 ? 19.189  -32.005 26.293  1.00 35.31  ? 42  ILE C CA  1 
ATOM   1742 C  C   . ILE C 1 43 ? 17.758  -32.274 25.852  1.00 33.17  ? 42  ILE C C   1 
ATOM   1743 O  O   . ILE C 1 43 ? 17.289  -33.409 25.905  1.00 36.30  ? 42  ILE C O   1 
ATOM   1744 C  CB  . ILE C 1 43 ? 20.198  -32.446 25.218  1.00 31.34  ? 42  ILE C CB  1 
ATOM   1745 C  CG1 . ILE C 1 43 ? 21.663  -32.192 25.633  1.00 35.56  ? 42  ILE C CG1 1 
ATOM   1746 C  CG2 . ILE C 1 43 ? 19.879  -31.782 23.866  1.00 37.21  ? 42  ILE C CG2 1 
ATOM   1747 C  CD1 . ILE C 1 43 ? 22.045  -30.748 25.903  1.00 34.37  ? 42  ILE C CD1 1 
ATOM   1748 N  N   . PHE C 1 44 ? 17.061  -31.227 25.364  1.00 35.49  ? 43  PHE C N   1 
ATOM   1749 C  CA  . PHE C 1 44 ? 15.754  -31.406 24.736  1.00 35.17  ? 43  PHE C CA  1 
ATOM   1750 C  C   . PHE C 1 44 ? 15.911  -30.929 23.285  1.00 31.53  ? 43  PHE C C   1 
ATOM   1751 O  O   . PHE C 1 44 ? 16.494  -29.854 23.064  1.00 33.72  ? 43  PHE C O   1 
ATOM   1752 C  CB  . PHE C 1 44 ? 14.728  -30.525 25.457  1.00 40.80  ? 43  PHE C CB  1 
ATOM   1753 C  CG  . PHE C 1 44 ? 13.375  -30.372 24.776  1.00 42.72  ? 43  PHE C CG  1 
ATOM   1754 C  CD1 . PHE C 1 44 ? 12.361  -31.301 24.998  1.00 42.53  ? 43  PHE C CD1 1 
ATOM   1755 C  CD2 . PHE C 1 44 ? 13.132  -29.299 23.911  1.00 47.26  ? 43  PHE C CD2 1 
ATOM   1756 C  CE1 . PHE C 1 44 ? 11.134  -31.173 24.351  1.00 44.23  ? 43  PHE C CE1 1 
ATOM   1757 C  CE2 . PHE C 1 44 ? 11.898  -29.162 23.281  1.00 44.77  ? 43  PHE C CE2 1 
ATOM   1758 C  CZ  . PHE C 1 44 ? 10.905  -30.099 23.510  1.00 48.72  ? 43  PHE C CZ  1 
ATOM   1759 N  N   . PHE C 1 45 ? 15.480  -31.784 22.339  1.00 34.47  ? 44  PHE C N   1 
ATOM   1760 C  CA  . PHE C 1 45 ? 15.691  -31.556 20.911  1.00 32.90  ? 44  PHE C CA  1 
ATOM   1761 C  C   . PHE C 1 45 ? 14.434  -30.900 20.338  1.00 31.48  ? 44  PHE C C   1 
ATOM   1762 O  O   . PHE C 1 45 ? 13.336  -31.426 20.500  1.00 35.73  ? 44  PHE C O   1 
ATOM   1763 C  CB  . PHE C 1 45 ? 16.062  -32.838 20.166  1.00 30.02  ? 44  PHE C CB  1 
ATOM   1764 C  CG  . PHE C 1 45 ? 17.417  -33.407 20.548  1.00 31.34  ? 44  PHE C CG  1 
ATOM   1765 C  CD1 . PHE C 1 45 ? 18.554  -33.001 19.853  1.00 30.00  ? 44  PHE C CD1 1 
ATOM   1766 C  CD2 . PHE C 1 45 ? 17.536  -34.386 21.545  1.00 31.96  ? 44  PHE C CD2 1 
ATOM   1767 C  CE1 . PHE C 1 45 ? 19.819  -33.527 20.160  1.00 34.32  ? 44  PHE C CE1 1 
ATOM   1768 C  CE2 . PHE C 1 45 ? 18.801  -34.895 21.862  1.00 36.00  ? 44  PHE C CE2 1 
ATOM   1769 C  CZ  . PHE C 1 45 ? 19.930  -34.458 21.170  1.00 33.07  ? 44  PHE C CZ  1 
ATOM   1770 N  N   . PHE C 1 46 ? 14.602  -29.712 19.715  1.00 31.09  ? 45  PHE C N   1 
ATOM   1771 C  CA  . PHE C 1 46 ? 13.438  -29.109 19.071  1.00 33.39  ? 45  PHE C CA  1 
ATOM   1772 C  C   . PHE C 1 46 ? 12.968  -29.947 17.888  1.00 33.79  ? 45  PHE C C   1 
ATOM   1773 O  O   . PHE C 1 46 ? 13.734  -30.704 17.263  1.00 31.57  ? 45  PHE C O   1 
ATOM   1774 C  CB  . PHE C 1 46 ? 13.710  -27.663 18.642  1.00 31.94  ? 45  PHE C CB  1 
ATOM   1775 C  CG  . PHE C 1 46 ? 13.985  -26.688 19.772  1.00 34.79  ? 45  PHE C CG  1 
ATOM   1776 C  CD1 . PHE C 1 46 ? 12.957  -26.193 20.574  1.00 38.76  ? 45  PHE C CD1 1 
ATOM   1777 C  CD2 . PHE C 1 46 ? 15.282  -26.225 19.970  1.00 32.21  ? 45  PHE C CD2 1 
ATOM   1778 C  CE1 . PHE C 1 46 ? 13.260  -25.281 21.589  1.00 36.44  ? 45  PHE C CE1 1 
ATOM   1779 C  CE2 . PHE C 1 46 ? 15.572  -25.334 20.989  1.00 38.43  ? 45  PHE C CE2 1 
ATOM   1780 C  CZ  . PHE C 1 46 ? 14.553  -24.859 21.781  1.00 34.61  ? 45  PHE C CZ  1 
ATOM   1781 N  N   . GLY C 1 47 ? 11.675  -29.808 17.570  1.00 30.52  ? 46  GLY C N   1 
ATOM   1782 C  CA  . GLY C 1 47 ? 11.130  -30.517 16.431  1.00 32.31  ? 46  GLY C CA  1 
ATOM   1783 C  C   . GLY C 1 47 ? 10.705  -31.937 16.802  1.00 36.75  ? 46  GLY C C   1 
ATOM   1784 O  O   . GLY C 1 47 ? 9.528   -32.260 16.724  1.00 41.13  ? 46  GLY C O   1 
ATOM   1785 N  N   . THR C 1 48 ? 11.660  -32.791 17.220  1.00 32.55  ? 47  THR C N   1 
ATOM   1786 C  CA  . THR C 1 48 ? 11.323  -34.155 17.620  1.00 34.47  ? 47  THR C CA  1 
ATOM   1787 C  C   . THR C 1 48 ? 10.754  -34.152 19.044  1.00 35.44  ? 47  THR C C   1 
ATOM   1788 O  O   . THR C 1 48 ? 9.984   -35.042 19.378  1.00 41.34  ? 47  THR C O   1 
ATOM   1789 C  CB  . THR C 1 48 ? 12.548  -35.069 17.520  1.00 34.33  ? 47  THR C CB  1 
ATOM   1790 O  OG1 . THR C 1 48 ? 13.430  -34.516 18.500  1.00 37.16  ? 47  THR C OG1 1 
ATOM   1791 C  CG2 . THR C 1 48 ? 13.120  -35.162 16.122  1.00 36.11  ? 47  THR C CG2 1 
ATOM   1792 N  N   . HIS C 1 49 ? 11.139  -33.167 19.855  1.00 36.85  ? 48  HIS C N   1 
ATOM   1793 C  CA  . HIS C 1 49 ? 10.780  -33.055 21.272  1.00 38.97  ? 48  HIS C CA  1 
ATOM   1794 C  C   . HIS C 1 49 ? 11.299  -34.234 22.108  1.00 41.00  ? 48  HIS C C   1 
ATOM   1795 O  O   . HIS C 1 49 ? 10.777  -34.509 23.190  1.00 44.44  ? 48  HIS C O   1 
ATOM   1796 C  CB  . HIS C 1 49 ? 9.279   -32.766 21.446  1.00 40.43  ? 48  HIS C CB  1 
ATOM   1797 C  CG  . HIS C 1 49 ? 8.750   -31.695 20.535  1.00 44.76  ? 48  HIS C CG  1 
ATOM   1798 N  ND1 . HIS C 1 49 ? 7.590   -31.892 19.813  1.00 53.36  ? 48  HIS C ND1 1 
ATOM   1799 C  CD2 . HIS C 1 49 ? 9.177   -30.462 20.218  1.00 48.49  ? 48  HIS C CD2 1 
ATOM   1800 C  CE1 . HIS C 1 49 ? 7.336   -30.820 19.073  1.00 54.78  ? 48  HIS C CE1 1 
ATOM   1801 N  NE2 . HIS C 1 49 ? 8.285   -29.930 19.296  1.00 40.67  ? 48  HIS C NE2 1 
ATOM   1802 N  N   . GLU C 1 50 ? 12.356  -34.907 21.643  1.00 37.58  ? 49  GLU C N   1 
ATOM   1803 C  CA  . GLU C 1 50 ? 12.971  -35.969 22.434  1.00 38.79  ? 49  GLU C CA  1 
ATOM   1804 C  C   . GLU C 1 50 ? 14.046  -35.424 23.387  1.00 38.95  ? 49  GLU C C   1 
ATOM   1805 O  O   . GLU C 1 50 ? 14.416  -34.247 23.376  1.00 38.57  ? 49  GLU C O   1 
ATOM   1806 C  CB  . GLU C 1 50 ? 13.468  -37.045 21.470  1.00 42.14  ? 49  GLU C CB  1 
ATOM   1807 C  CG  . GLU C 1 50 ? 12.357  -37.560 20.556  1.00 47.61  ? 49  GLU C CG  1 
ATOM   1808 C  CD  . GLU C 1 50 ? 12.820  -38.540 19.498  1.00 55.28  ? 49  GLU C CD  1 
ATOM   1809 O  OE1 . GLU C 1 50 ? 14.030  -38.862 19.450  1.00 63.86  ? 49  GLU C OE1 1 
ATOM   1810 O  OE2 . GLU C 1 50 ? 11.958  -39.001 18.716  1.00 62.97  ? 49  GLU C OE2 1 
ATOM   1811 N  N   . THR C 1 51 ? 14.528  -36.296 24.282  1.00 44.17  ? 50  THR C N   1 
ATOM   1812 C  CA  . THR C 1 51 ? 15.558  -35.928 25.246  1.00 42.21  ? 50  THR C CA  1 
ATOM   1813 C  C   . THR C 1 51 ? 16.678  -36.962 25.174  1.00 36.87  ? 50  THR C C   1 
ATOM   1814 O  O   . THR C 1 51 ? 16.445  -38.113 24.800  1.00 43.18  ? 50  THR C O   1 
ATOM   1815 C  CB  . THR C 1 51 ? 15.003  -35.863 26.673  1.00 46.90  ? 50  THR C CB  1 
ATOM   1816 O  OG1 . THR C 1 51 ? 14.510  -37.180 26.928  1.00 46.67  ? 50  THR C OG1 1 
ATOM   1817 C  CG2 . THR C 1 51 ? 13.967  -34.771 26.886  1.00 51.61  ? 50  THR C CG2 1 
ATOM   1818 N  N   . ALA C 1 52 ? 17.887  -36.523 25.540  1.00 37.36  ? 51  ALA C N   1 
ATOM   1819 C  CA  . ALA C 1 52 ? 19.097  -37.333 25.663  1.00 37.14  ? 51  ALA C CA  1 
ATOM   1820 C  C   . ALA C 1 52 ? 20.060  -36.642 26.635  1.00 40.52  ? 51  ALA C C   1 
ATOM   1821 O  O   . ALA C 1 52 ? 19.860  -35.488 27.022  1.00 41.10  ? 51  ALA C O   1 
ATOM   1822 C  CB  . ALA C 1 52 ? 19.761  -37.526 24.313  1.00 40.30  ? 51  ALA C CB  1 
ATOM   1823 N  N   . PHE C 1 53 ? 21.139  -37.343 27.013  1.00 39.48  ? 52  PHE C N   1 
ATOM   1824 C  CA  . PHE C 1 53 ? 22.215  -36.727 27.783  1.00 38.31  ? 52  PHE C CA  1 
ATOM   1825 C  C   . PHE C 1 53 ? 23.444  -36.618 26.900  1.00 39.07  ? 52  PHE C C   1 
ATOM   1826 O  O   . PHE C 1 53 ? 23.799  -37.597 26.232  1.00 42.86  ? 52  PHE C O   1 
ATOM   1827 C  CB  . PHE C 1 53 ? 22.587  -37.621 28.974  1.00 41.38  ? 52  PHE C CB  1 
ATOM   1828 C  CG  . PHE C 1 53 ? 21.548  -37.640 30.085  1.00 44.76  ? 52  PHE C CG  1 
ATOM   1829 C  CD1 . PHE C 1 53 ? 21.311  -36.511 30.865  1.00 41.10  ? 52  PHE C CD1 1 
ATOM   1830 C  CD2 . PHE C 1 53 ? 20.797  -38.786 30.334  1.00 54.97  ? 52  PHE C CD2 1 
ATOM   1831 C  CE1 . PHE C 1 53 ? 20.377  -36.536 31.889  1.00 47.22  ? 52  PHE C CE1 1 
ATOM   1832 C  CE2 . PHE C 1 53 ? 19.858  -38.796 31.353  1.00 51.79  ? 52  PHE C CE2 1 
ATOM   1833 C  CZ  . PHE C 1 53 ? 19.649  -37.670 32.120  1.00 48.78  ? 52  PHE C CZ  1 
ATOM   1834 N  N   . LEU C 1 54 ? 24.100  -35.437 26.902  1.00 33.49  ? 53  LEU C N   1 
ATOM   1835 C  CA  . LEU C 1 54 ? 25.248  -35.225 26.038  1.00 34.33  ? 53  LEU C CA  1 
ATOM   1836 C  C   . LEU C 1 54 ? 26.327  -34.464 26.806  1.00 34.98  ? 53  LEU C C   1 
ATOM   1837 O  O   . LEU C 1 54 ? 26.012  -33.725 27.732  1.00 36.80  ? 53  LEU C O   1 
ATOM   1838 C  CB  . LEU C 1 54 ? 24.835  -34.478 24.772  1.00 34.51  ? 53  LEU C CB  1 
ATOM   1839 C  CG  . LEU C 1 54 ? 24.017  -35.282 23.756  1.00 38.19  ? 53  LEU C CG  1 
ATOM   1840 C  CD1 . LEU C 1 54 ? 23.667  -34.345 22.628  1.00 39.56  ? 53  LEU C CD1 1 
ATOM   1841 C  CD2 . LEU C 1 54 ? 24.774  -36.524 23.214  1.00 44.76  ? 53  LEU C CD2 1 
ATOM   1842 N  N   . GLY C 1 55 ? 27.586  -34.631 26.395  1.00 36.34  ? 54  GLY C N   1 
ATOM   1843 C  CA  . GLY C 1 55 ? 28.689  -33.918 27.021  1.00 40.90  ? 54  GLY C CA  1 
ATOM   1844 C  C   . GLY C 1 55 ? 28.963  -32.587 26.327  1.00 47.80  ? 54  GLY C C   1 
ATOM   1845 O  O   . GLY C 1 55 ? 28.480  -32.325 25.209  1.00 38.91  ? 54  GLY C O   1 
ATOM   1846 N  N   . PRO C 1 56 ? 29.758  -31.696 26.967  1.00 45.85  ? 55  PRO C N   1 
ATOM   1847 C  CA  . PRO C 1 56 ? 30.010  -30.353 26.438  1.00 48.13  ? 55  PRO C CA  1 
ATOM   1848 C  C   . PRO C 1 56 ? 30.577  -30.277 25.025  1.00 41.03  ? 55  PRO C C   1 
ATOM   1849 O  O   . PRO C 1 56 ? 30.275  -29.328 24.302  1.00 55.69  ? 55  PRO C O   1 
ATOM   1850 C  CB  . PRO C 1 56 ? 30.969  -29.713 27.495  1.00 42.57  ? 55  PRO C CB  1 
ATOM   1851 C  CG  . PRO C 1 56 ? 31.553  -30.905 28.209  1.00 45.30  ? 55  PRO C CG  1 
ATOM   1852 C  CD  . PRO C 1 56 ? 30.411  -31.907 28.278  1.00 45.94  ? 55  PRO C CD  1 
ATOM   1853 N  N   . LYS C 1 57 ? 31.361  -31.289 24.633  1.00 42.48  ? 56  LYS C N   1 
ATOM   1854 C  CA  . LYS C 1 57 ? 32.019  -31.247 23.338  1.00 43.67  ? 56  LYS C CA  1 
ATOM   1855 C  C   . LYS C 1 57 ? 30.974  -31.468 22.245  1.00 48.16  ? 56  LYS C C   1 
ATOM   1856 O  O   . LYS C 1 57 ? 31.231  -31.178 21.077  1.00 45.48  ? 56  LYS C O   1 
ATOM   1857 C  CB  . LYS C 1 57 ? 33.059  -32.354 23.169  1.00 45.36  ? 56  LYS C CB  1 
ATOM   1858 N  N   . ASP C 1 58 ? 29.807  -31.997 22.634  1.00 45.99  ? 57  ASP C N   1 
ATOM   1859 C  CA  . ASP C 1 58 ? 28.764  -32.250 21.651  1.00 46.68  ? 57  ASP C CA  1 
ATOM   1860 C  C   . ASP C 1 58 ? 27.811  -31.068 21.510  1.00 45.29  ? 57  ASP C C   1 
ATOM   1861 O  O   . ASP C 1 58 ? 26.827  -31.186 20.784  1.00 39.35  ? 57  ASP C O   1 
ATOM   1862 C  CB  . ASP C 1 58 ? 27.980  -33.519 21.944  1.00 43.56  ? 57  ASP C CB  1 
ATOM   1863 C  CG  . ASP C 1 58 ? 28.821  -34.783 22.002  1.00 47.29  ? 57  ASP C CG  1 
ATOM   1864 O  OD1 . ASP C 1 58 ? 29.707  -34.928 21.154  1.00 51.05  ? 57  ASP C OD1 1 
ATOM   1865 O  OD2 . ASP C 1 58 ? 28.567  -35.605 22.881  1.00 48.58  ? 57  ASP C OD2 1 
ATOM   1866 N  N   . LEU C 1 59 ? 28.087  -29.946 22.192  1.00 38.56  ? 58  LEU C N   1 
ATOM   1867 C  CA  . LEU C 1 59 ? 27.159  -28.830 22.318  1.00 42.07  ? 58  LEU C CA  1 
ATOM   1868 C  C   . LEU C 1 59 ? 27.767  -27.532 21.779  1.00 47.08  ? 58  LEU C C   1 
ATOM   1869 O  O   . LEU C 1 59 ? 28.932  -27.238 22.054  1.00 53.05  ? 58  LEU C O   1 
ATOM   1870 C  CB  . LEU C 1 59 ? 26.754  -28.699 23.787  1.00 38.63  ? 58  LEU C CB  1 
ATOM   1871 C  CG  . LEU C 1 59 ? 26.186  -29.979 24.406  1.00 36.01  ? 58  LEU C CG  1 
ATOM   1872 C  CD1 . LEU C 1 59 ? 25.862  -29.848 25.879  1.00 36.45  ? 58  LEU C CD1 1 
ATOM   1873 C  CD2 . LEU C 1 59 ? 24.930  -30.448 23.656  1.00 32.77  ? 58  LEU C CD2 1 
ATOM   1874 N  N   . PHE C 1 60 ? 26.959  -26.763 21.031  1.00 43.99  ? 59  PHE C N   1 
ATOM   1875 C  CA  . PHE C 1 60 ? 27.403  -25.540 20.366  1.00 43.32  ? 59  PHE C CA  1 
ATOM   1876 C  C   . PHE C 1 60 ? 26.397  -24.427 20.642  1.00 45.38  ? 59  PHE C C   1 
ATOM   1877 O  O   . PHE C 1 60 ? 25.208  -24.558 20.361  1.00 42.53  ? 59  PHE C O   1 
ATOM   1878 C  CB  . PHE C 1 60 ? 27.649  -25.751 18.864  1.00 44.38  ? 59  PHE C CB  1 
ATOM   1879 C  CG  . PHE C 1 60 ? 28.592  -26.910 18.574  1.00 38.35  ? 59  PHE C CG  1 
ATOM   1880 C  CD1 . PHE C 1 60 ? 28.149  -28.228 18.626  1.00 40.31  ? 59  PHE C CD1 1 
ATOM   1881 C  CD2 . PHE C 1 60 ? 29.938  -26.690 18.295  1.00 46.77  ? 59  PHE C CD2 1 
ATOM   1882 C  CE1 . PHE C 1 60 ? 29.021  -29.286 18.429  1.00 40.17  ? 59  PHE C CE1 1 
ATOM   1883 C  CE2 . PHE C 1 60 ? 30.805  -27.753 18.061  1.00 44.76  ? 59  PHE C CE2 1 
ATOM   1884 C  CZ  . PHE C 1 60 ? 30.351  -29.052 18.118  1.00 45.57  ? 59  PHE C CZ  1 
ATOM   1885 N  N   . PRO C 1 61 ? 26.824  -23.270 21.201  1.00 44.43  ? 60  PRO C N   1 
ATOM   1886 C  CA  . PRO C 1 61 ? 25.862  -22.219 21.555  1.00 43.84  ? 60  PRO C CA  1 
ATOM   1887 C  C   . PRO C 1 61 ? 25.144  -21.750 20.285  1.00 38.64  ? 60  PRO C C   1 
ATOM   1888 O  O   . PRO C 1 61 ? 25.739  -21.676 19.209  1.00 42.01  ? 60  PRO C O   1 
ATOM   1889 C  CB  . PRO C 1 61 ? 26.701  -21.118 22.248  1.00 44.82  ? 60  PRO C CB  1 
ATOM   1890 C  CG  . PRO C 1 61 ? 28.071  -21.775 22.432  1.00 43.03  ? 60  PRO C CG  1 
ATOM   1891 C  CD  . PRO C 1 61 ? 28.231  -22.901 21.429  1.00 46.76  ? 60  PRO C CD  1 
ATOM   1892 N  N   . TYR C 1 62 ? 23.826  -21.536 20.404  1.00 44.25  ? 61  TYR C N   1 
ATOM   1893 C  CA  . TYR C 1 62 ? 22.955  -21.312 19.256  1.00 43.91  ? 61  TYR C CA  1 
ATOM   1894 C  C   . TYR C 1 62 ? 23.382  -20.070 18.478  1.00 52.69  ? 61  TYR C C   1 
ATOM   1895 O  O   . TYR C 1 62 ? 23.602  -20.147 17.266  1.00 55.30  ? 61  TYR C O   1 
ATOM   1896 C  CB  . TYR C 1 62 ? 21.515  -21.028 19.678  1.00 42.77  ? 61  TYR C CB  1 
ATOM   1897 C  CG  . TYR C 1 62 ? 20.573  -20.697 18.527  1.00 45.64  ? 61  TYR C CG  1 
ATOM   1898 C  CD1 . TYR C 1 62 ? 20.415  -21.565 17.446  1.00 50.98  ? 61  TYR C CD1 1 
ATOM   1899 C  CD2 . TYR C 1 62 ? 19.834  -19.520 18.530  1.00 50.87  ? 61  TYR C CD2 1 
ATOM   1900 C  CE1 . TYR C 1 62 ? 19.539  -21.270 16.410  1.00 47.99  ? 61  TYR C CE1 1 
ATOM   1901 C  CE2 . TYR C 1 62 ? 18.964  -19.210 17.496  1.00 53.48  ? 61  TYR C CE2 1 
ATOM   1902 C  CZ  . TYR C 1 62 ? 18.811  -20.087 16.436  1.00 47.30  ? 61  TYR C CZ  1 
ATOM   1903 O  OH  . TYR C 1 62 ? 17.947  -19.739 15.428  1.00 52.27  ? 61  TYR C OH  1 
ATOM   1904 N  N   . ASP C 1 63 ? 23.483  -18.934 19.190  1.00 54.52  ? 62  ASP C N   1 
ATOM   1905 C  CA  . ASP C 1 63 ? 23.802  -17.667 18.546  1.00 52.36  ? 62  ASP C CA  1 
ATOM   1906 C  C   . ASP C 1 63 ? 25.129  -17.750 17.807  1.00 50.98  ? 62  ASP C C   1 
ATOM   1907 O  O   . ASP C 1 63 ? 25.259  -17.214 16.705  1.00 53.99  ? 62  ASP C O   1 
ATOM   1908 C  CB  . ASP C 1 63 ? 23.637  -16.481 19.479  1.00 59.18  ? 62  ASP C CB  1 
ATOM   1909 C  CG  . ASP C 1 63 ? 22.268  -15.830 19.358  1.00 78.29  ? 62  ASP C CG  1 
ATOM   1910 O  OD1 . ASP C 1 63 ? 21.480  -15.938 20.325  1.00 74.90  ? 62  ASP C OD1 1 
ATOM   1911 O  OD2 . ASP C 1 63 ? 21.994  -15.253 18.275  1.00 87.44  ? 62  ASP C OD2 1 
ATOM   1912 N  N   . LYS C 1 64 ? 26.083  -18.458 18.406  1.00 43.29  ? 63  LYS C N   1 
ATOM   1913 C  CA  . LYS C 1 64 ? 27.439  -18.513 17.895  1.00 48.34  ? 63  LYS C CA  1 
ATOM   1914 C  C   . LYS C 1 64 ? 27.522  -19.424 16.672  1.00 49.60  ? 63  LYS C C   1 
ATOM   1915 O  O   . LYS C 1 64 ? 28.363  -19.187 15.805  1.00 42.44  ? 63  LYS C O   1 
ATOM   1916 C  CB  . LYS C 1 64 ? 28.468  -18.886 18.973  1.00 53.53  ? 63  LYS C CB  1 
ATOM   1917 N  N   . SER C 1 65 ? 26.651  -20.453 16.578  1.00 43.33  ? 64  SER C N   1 
ATOM   1918 C  CA  . SER C 1 65 ? 26.882  -21.444 15.529  1.00 38.77  ? 64  SER C CA  1 
ATOM   1919 C  C   . SER C 1 65 ? 25.731  -21.533 14.518  1.00 38.06  ? 64  SER C C   1 
ATOM   1920 O  O   . SER C 1 65 ? 25.845  -22.293 13.567  1.00 39.97  ? 64  SER C O   1 
ATOM   1921 C  CB  . SER C 1 65 ? 27.229  -22.815 16.067  1.00 38.97  ? 64  SER C CB  1 
ATOM   1922 O  OG  . SER C 1 65 ? 26.140  -23.275 16.848  1.00 46.61  ? 64  SER C OG  1 
ATOM   1923 N  N   . LYS C 1 66 ? 24.675  -20.737 14.672  1.00 40.42  ? 65  LYS C N   1 
ATOM   1924 C  CA  . LYS C 1 66 ? 23.541  -20.878 13.765  1.00 44.62  ? 65  LYS C CA  1 
ATOM   1925 C  C   . LYS C 1 66 ? 23.913  -20.555 12.320  1.00 51.15  ? 65  LYS C C   1 
ATOM   1926 O  O   . LYS C 1 66 ? 23.306  -21.107 11.397  1.00 43.64  ? 65  LYS C O   1 
ATOM   1927 C  CB  . LYS C 1 66 ? 22.309  -20.051 14.123  1.00 44.97  ? 65  LYS C CB  1 
ATOM   1928 C  CG  . LYS C 1 66 ? 22.571  -18.567 14.226  1.00 40.02  ? 65  LYS C CG  1 
ATOM   1929 C  CD  . LYS C 1 66 ? 21.242  -17.886 14.508  1.00 49.70  ? 65  LYS C CD  1 
ATOM   1930 C  CE  . LYS C 1 66 ? 21.497  -16.529 15.044  1.00 50.15  ? 65  LYS C CE  1 
ATOM   1931 N  NZ  . LYS C 1 66 ? 20.200  -15.885 15.195  1.00 52.66  ? 65  LYS C NZ  1 
ATOM   1932 N  N   . ASP C 1 67 ? 24.885  -19.652 12.111  1.00 43.00  ? 66  ASP C N   1 
ATOM   1933 C  CA  . ASP C 1 67 ? 25.257  -19.358 10.734  1.00 46.49  ? 66  ASP C CA  1 
ATOM   1934 C  C   . ASP C 1 67 ? 25.658  -20.654 10.019  1.00 47.49  ? 66  ASP C C   1 
ATOM   1935 O  O   . ASP C 1 67 ? 25.364  -20.822 8.847   1.00 42.40  ? 66  ASP C O   1 
ATOM   1936 C  CB  . ASP C 1 67 ? 26.137  -18.115 10.589  1.00 48.90  ? 66  ASP C CB  1 
ATOM   1937 C  CG  . ASP C 1 67 ? 27.652  -18.265 10.692  1.00 64.66  ? 66  ASP C CG  1 
ATOM   1938 O  OD1 . ASP C 1 67 ? 28.207  -19.246 10.129  1.00 64.58  ? 66  ASP C OD1 1 
ATOM   1939 O  OD2 . ASP C 1 67 ? 28.284  -17.343 11.261  1.00 67.66  ? 66  ASP C OD2 1 
ATOM   1940 N  N   . LYS C 1 68 ? 26.280  -21.597 10.744  1.00 44.34  ? 67  LYS C N   1 
ATOM   1941 C  CA  . LYS C 1 68 ? 26.802  -22.821 10.152  1.00 39.07  ? 67  LYS C CA  1 
ATOM   1942 C  C   . LYS C 1 68 ? 25.796  -23.983 10.208  1.00 40.91  ? 67  LYS C C   1 
ATOM   1943 O  O   . LYS C 1 68 ? 25.689  -24.748 9.255   1.00 42.42  ? 67  LYS C O   1 
ATOM   1944 C  CB  . LYS C 1 68 ? 27.999  -23.247 11.001  1.00 35.54  ? 67  LYS C CB  1 
ATOM   1945 C  CG  . LYS C 1 68 ? 28.823  -24.405 10.500  1.00 39.57  ? 67  LYS C CG  1 
ATOM   1946 C  CD  . LYS C 1 68 ? 30.066  -24.346 11.394  1.00 52.13  ? 67  LYS C CD  1 
ATOM   1947 C  CE  . LYS C 1 68 ? 30.930  -25.561 11.559  1.00 59.48  ? 67  LYS C CE  1 
ATOM   1948 N  NZ  . LYS C 1 68 ? 31.534  -26.074 10.327  1.00 69.30  ? 67  LYS C NZ  1 
ATOM   1949 N  N   . TYR C 1 69 ? 25.083  -24.145 11.338  1.00 37.93  ? 68  TYR C N   1 
ATOM   1950 C  CA  . TYR C 1 69 ? 24.243  -25.327 11.512  1.00 37.61  ? 68  TYR C CA  1 
ATOM   1951 C  C   . TYR C 1 69 ? 22.766  -25.009 11.288  1.00 35.15  ? 68  TYR C C   1 
ATOM   1952 O  O   . TYR C 1 69 ? 21.967  -25.934 11.108  1.00 31.75  ? 68  TYR C O   1 
ATOM   1953 C  CB  . TYR C 1 69 ? 24.413  -25.922 12.923  1.00 32.19  ? 68  TYR C CB  1 
ATOM   1954 C  CG  . TYR C 1 69 ? 25.839  -26.371 13.219  1.00 33.94  ? 68  TYR C CG  1 
ATOM   1955 C  CD1 . TYR C 1 69 ? 26.541  -27.206 12.359  1.00 38.96  ? 68  TYR C CD1 1 
ATOM   1956 C  CD2 . TYR C 1 69 ? 26.444  -25.985 14.411  1.00 40.08  ? 68  TYR C CD2 1 
ATOM   1957 C  CE1 . TYR C 1 69 ? 27.829  -27.632 12.658  1.00 38.62  ? 68  TYR C CE1 1 
ATOM   1958 C  CE2 . TYR C 1 69 ? 27.729  -26.402 14.719  1.00 39.77  ? 68  TYR C CE2 1 
ATOM   1959 C  CZ  . TYR C 1 69 ? 28.412  -27.216 13.842  1.00 40.39  ? 68  TYR C CZ  1 
ATOM   1960 O  OH  . TYR C 1 69 ? 29.679  -27.579 14.182  1.00 47.20  ? 68  TYR C OH  1 
ATOM   1961 N  N   . GLY C 1 70 ? 22.392  -23.717 11.287  1.00 35.57  ? 69  GLY C N   1 
ATOM   1962 C  CA  . GLY C 1 70 ? 20.969  -23.385 11.255  1.00 34.18  ? 69  GLY C CA  1 
ATOM   1963 C  C   . GLY C 1 70 ? 20.534  -23.227 9.804   1.00 35.22  ? 69  GLY C C   1 
ATOM   1964 O  O   . GLY C 1 70 ? 20.442  -22.117 9.301   1.00 36.52  ? 69  GLY C O   1 
ATOM   1965 N  N   . LYS C 1 71 ? 20.476  -24.364 9.125   1.00 33.92  ? 70  LYS C N   1 
ATOM   1966 C  CA  . LYS C 1 71 ? 20.118  -24.466 7.721   1.00 36.31  ? 70  LYS C CA  1 
ATOM   1967 C  C   . LYS C 1 71 ? 19.229  -25.688 7.593   1.00 37.15  ? 70  LYS C C   1 
ATOM   1968 O  O   . LYS C 1 71 ? 19.331  -26.642 8.368   1.00 37.54  ? 70  LYS C O   1 
ATOM   1969 C  CB  . LYS C 1 71 ? 21.382  -24.668 6.871   1.00 37.11  ? 70  LYS C CB  1 
ATOM   1970 C  CG  . LYS C 1 71 ? 22.355  -25.690 7.405   1.00 43.58  ? 70  LYS C CG  1 
ATOM   1971 C  CD  . LYS C 1 71 ? 23.561  -26.038 6.535   1.00 51.90  ? 70  LYS C CD  1 
ATOM   1972 C  CE  . LYS C 1 71 ? 24.483  -26.996 7.240   1.00 53.35  ? 70  LYS C CE  1 
ATOM   1973 N  N   . PRO C 1 72 ? 18.302  -25.699 6.627   1.00 34.05  ? 71  PRO C N   1 
ATOM   1974 C  CA  . PRO C 1 72 ? 17.374  -26.819 6.537   1.00 30.29  ? 71  PRO C CA  1 
ATOM   1975 C  C   . PRO C 1 72 ? 18.039  -28.143 6.203   1.00 32.38  ? 71  PRO C C   1 
ATOM   1976 O  O   . PRO C 1 72 ? 19.067  -28.217 5.503   1.00 35.74  ? 71  PRO C O   1 
ATOM   1977 C  CB  . PRO C 1 72 ? 16.389  -26.404 5.441   1.00 31.27  ? 71  PRO C CB  1 
ATOM   1978 C  CG  . PRO C 1 72 ? 16.498  -24.891 5.442   1.00 32.16  ? 71  PRO C CG  1 
ATOM   1979 C  CD  . PRO C 1 72 ? 17.962  -24.556 5.761   1.00 32.02  ? 71  PRO C CD  1 
ATOM   1980 N  N   . ASN C 1 73 ? 17.334  -29.178 6.621   1.00 31.90  ? 72  ASN C N   1 
ATOM   1981 C  CA  . ASN C 1 73 ? 17.619  -30.489 6.070   1.00 37.71  ? 72  ASN C CA  1 
ATOM   1982 C  C   . ASN C 1 73 ? 16.406  -31.382 6.244   1.00 35.62  ? 72  ASN C C   1 
ATOM   1983 O  O   . ASN C 1 73 ? 15.471  -31.059 6.955   1.00 36.77  ? 72  ASN C O   1 
ATOM   1984 C  CB  . ASN C 1 73 ? 18.952  -31.087 6.504   1.00 40.62  ? 72  ASN C CB  1 
ATOM   1985 C  CG  . ASN C 1 73 ? 18.831  -31.720 7.864   1.00 38.25  ? 72  ASN C CG  1 
ATOM   1986 O  OD1 . ASN C 1 73 ? 18.297  -32.827 7.984   1.00 40.74  ? 72  ASN C OD1 1 
ATOM   1987 N  ND2 . ASN C 1 73 ? 19.431  -31.100 8.857   1.00 51.76  ? 72  ASN C ND2 1 
ATOM   1988 N  N   . LYS C 1 74 ? 16.447  -32.517 5.555   1.00 36.60  ? 73  LYS C N   1 
ATOM   1989 C  CA  . LYS C 1 74 ? 15.228  -33.278 5.334   1.00 33.16  ? 73  LYS C CA  1 
ATOM   1990 C  C   . LYS C 1 74 ? 15.026  -34.275 6.457   1.00 34.81  ? 73  LYS C C   1 
ATOM   1991 O  O   . LYS C 1 74 ? 14.005  -34.963 6.507   1.00 37.51  ? 73  LYS C O   1 
ATOM   1992 C  CB  . LYS C 1 74 ? 15.361  -34.007 3.993   1.00 39.01  ? 73  LYS C CB  1 
ATOM   1993 N  N   . ARG C 1 75 ? 15.956  -34.307 7.423   1.00 30.67  ? 74  ARG C N   1 
ATOM   1994 C  CA  . ARG C 1 75 ? 15.732  -35.285 8.476   1.00 30.06  ? 74  ARG C CA  1 
ATOM   1995 C  C   . ARG C 1 75 ? 14.454  -34.976 9.265   1.00 31.80  ? 74  ARG C C   1 
ATOM   1996 O  O   . ARG C 1 75 ? 14.098  -33.810 9.487   1.00 34.32  ? 74  ARG C O   1 
ATOM   1997 C  CB  . ARG C 1 75 ? 16.933  -35.323 9.429   1.00 33.40  ? 74  ARG C CB  1 
ATOM   1998 C  CG  . ARG C 1 75 ? 17.169  -36.797 9.705   1.00 42.67  ? 74  ARG C CG  1 
ATOM   1999 C  CD  . ARG C 1 75 ? 18.128  -37.385 8.657   1.00 45.34  ? 74  ARG C CD  1 
ATOM   2000 N  NE  . ARG C 1 75 ? 18.594  -38.398 9.584   1.00 48.56  ? 74  ARG C NE  1 
ATOM   2001 C  CZ  . ARG C 1 75 ? 19.787  -38.552 10.127  1.00 34.17  ? 74  ARG C CZ  1 
ATOM   2002 N  NH1 . ARG C 1 75 ? 19.737  -38.981 11.355  1.00 40.72  ? 74  ARG C NH1 1 
ATOM   2003 N  NH2 . ARG C 1 75 ? 20.891  -38.137 9.517   1.00 35.82  ? 74  ARG C NH2 1 
ATOM   2004 N  N   . LYS C 1 76 ? 13.799  -36.046 9.736   1.00 34.04  ? 75  LYS C N   1 
ATOM   2005 C  CA  . LYS C 1 76 ? 12.514  -35.975 10.410  1.00 37.73  ? 75  LYS C CA  1 
ATOM   2006 C  C   . LYS C 1 76 ? 12.534  -35.019 11.597  1.00 36.07  ? 75  LYS C C   1 
ATOM   2007 O  O   . LYS C 1 76 ? 13.242  -35.222 12.594  1.00 34.81  ? 75  LYS C O   1 
ATOM   2008 C  CB  . LYS C 1 76 ? 11.935  -37.353 10.760  1.00 37.70  ? 75  LYS C CB  1 
ATOM   2009 C  CG  . LYS C 1 76 ? 10.499  -37.253 11.224  1.00 37.79  ? 75  LYS C CG  1 
ATOM   2010 C  CD  . LYS C 1 76 ? 9.900   -38.550 11.752  1.00 50.67  ? 75  LYS C CD  1 
ATOM   2011 N  N   . GLY C 1 77 ? 11.736  -33.943 11.465  1.00 37.14  ? 76  GLY C N   1 
ATOM   2012 C  CA  . GLY C 1 77 ? 11.443  -33.059 12.582  1.00 30.84  ? 76  GLY C CA  1 
ATOM   2013 C  C   . GLY C 1 77 ? 12.410  -31.870 12.633  1.00 29.31  ? 76  GLY C C   1 
ATOM   2014 O  O   . GLY C 1 77 ? 12.242  -30.962 13.435  1.00 35.69  ? 76  GLY C O   1 
ATOM   2015 N  N   . PHE C 1 78 ? 13.402  -31.864 11.748  1.00 30.23  ? 77  PHE C N   1 
ATOM   2016 C  CA  . PHE C 1 78 ? 14.503  -30.923 11.837  1.00 31.16  ? 77  PHE C CA  1 
ATOM   2017 C  C   . PHE C 1 78 ? 14.002  -29.508 11.533  1.00 31.16  ? 77  PHE C C   1 
ATOM   2018 O  O   . PHE C 1 78 ? 14.324  -28.559 12.221  1.00 28.41  ? 77  PHE C O   1 
ATOM   2019 C  CB  . PHE C 1 78 ? 15.615  -31.332 10.880  1.00 32.28  ? 77  PHE C CB  1 
ATOM   2020 C  CG  . PHE C 1 78 ? 16.890  -30.551 11.130  1.00 30.96  ? 77  PHE C CG  1 
ATOM   2021 C  CD1 . PHE C 1 78 ? 17.073  -29.269 10.598  1.00 33.99  ? 77  PHE C CD1 1 
ATOM   2022 C  CD2 . PHE C 1 78 ? 17.930  -31.106 11.873  1.00 29.02  ? 77  PHE C CD2 1 
ATOM   2023 C  CE1 . PHE C 1 78 ? 18.245  -28.551 10.835  1.00 33.07  ? 77  PHE C CE1 1 
ATOM   2024 C  CE2 . PHE C 1 78 ? 19.110  -30.388 12.093  1.00 30.33  ? 77  PHE C CE2 1 
ATOM   2025 C  CZ  . PHE C 1 78 ? 19.285  -29.122 11.560  1.00 31.68  ? 77  PHE C CZ  1 
ATOM   2026 N  N   . ASN C 1 79 ? 13.253  -29.374 10.437  1.00 31.93  ? 78  ASN C N   1 
ATOM   2027 C  CA  . ASN C 1 79 ? 12.924  -28.026 10.008  1.00 33.21  ? 78  ASN C CA  1 
ATOM   2028 C  C   . ASN C 1 79 ? 11.901  -27.402 10.957  1.00 31.71  ? 78  ASN C C   1 
ATOM   2029 O  O   . ASN C 1 79 ? 11.945  -26.193 11.244  1.00 31.53  ? 78  ASN C O   1 
ATOM   2030 C  CB  . ASN C 1 79 ? 12.473  -28.010 8.557   1.00 31.81  ? 78  ASN C CB  1 
ATOM   2031 C  CG  . ASN C 1 79 ? 13.609  -28.308 7.610   1.00 31.39  ? 78  ASN C CG  1 
ATOM   2032 O  OD1 . ASN C 1 79 ? 14.771  -28.026 7.917   1.00 31.25  ? 78  ASN C OD1 1 
ATOM   2033 N  ND2 . ASN C 1 79 ? 13.312  -28.955 6.488   1.00 32.54  ? 78  ASN C ND2 1 
ATOM   2034 N  N   . GLU C 1 80 ? 10.983  -28.215 11.471  1.00 32.71  ? 79  GLU C N   1 
ATOM   2035 C  CA  . GLU C 1 80 ? 10.140  -27.705 12.543  1.00 35.39  ? 79  GLU C CA  1 
ATOM   2036 C  C   . GLU C 1 80 ? 11.008  -27.285 13.737  1.00 41.62  ? 79  GLU C C   1 
ATOM   2037 O  O   . GLU C 1 80 ? 10.759  -26.258 14.381  1.00 34.74  ? 79  GLU C O   1 
ATOM   2038 C  CB  . GLU C 1 80 ? 9.004   -28.682 12.865  1.00 40.59  ? 79  GLU C CB  1 
ATOM   2039 C  CG  . GLU C 1 80 ? 8.129   -28.216 14.017  1.00 37.89  ? 79  GLU C CG  1 
ATOM   2040 C  CD  . GLU C 1 80 ? 6.926   -29.107 14.247  1.00 47.20  ? 79  GLU C CD  1 
ATOM   2041 O  OE1 . GLU C 1 80 ? 7.003   -30.312 13.932  1.00 55.84  ? 79  GLU C OE1 1 
ATOM   2042 O  OE2 . GLU C 1 80 ? 5.889   -28.582 14.684  1.00 46.87  ? 79  GLU C OE2 1 
ATOM   2043 N  N   . GLY C 1 81 ? 12.052  -28.076 14.046  1.00 34.67  ? 80  GLY C N   1 
ATOM   2044 C  CA  . GLY C 1 81 ? 12.929  -27.674 15.137  1.00 34.90  ? 80  GLY C CA  1 
ATOM   2045 C  C   . GLY C 1 81 ? 13.599  -26.311 14.902  1.00 33.71  ? 80  GLY C C   1 
ATOM   2046 O  O   . GLY C 1 81 ? 13.754  -25.540 15.842  1.00 35.09  ? 80  GLY C O   1 
ATOM   2047 N  N   . LEU C 1 82 ? 14.152  -26.057 13.684  1.00 29.48  ? 81  LEU C N   1 
ATOM   2048 C  CA  . LEU C 1 82 ? 14.643  -24.729 13.323  1.00 33.17  ? 81  LEU C CA  1 
ATOM   2049 C  C   . LEU C 1 82 ? 13.571  -23.663 13.574  1.00 31.97  ? 81  LEU C C   1 
ATOM   2050 O  O   . LEU C 1 82 ? 13.888  -22.576 14.065  1.00 33.42  ? 81  LEU C O   1 
ATOM   2051 C  CB  . LEU C 1 82 ? 15.086  -24.662 11.864  1.00 32.54  ? 81  LEU C CB  1 
ATOM   2052 C  CG  . LEU C 1 82 ? 16.299  -25.499 11.482  1.00 30.87  ? 81  LEU C CG  1 
ATOM   2053 C  CD1 . LEU C 1 82 ? 16.529  -25.312 10.009  1.00 30.30  ? 81  LEU C CD1 1 
ATOM   2054 C  CD2 . LEU C 1 82 ? 17.527  -25.113 12.240  1.00 27.20  ? 81  LEU C CD2 1 
ATOM   2055 N  N   . TRP C 1 83 ? 12.307  -23.961 13.262  1.00 31.54  ? 82  TRP C N   1 
ATOM   2056 C  CA  . TRP C 1 83 ? 11.297  -22.922 13.455  1.00 35.78  ? 82  TRP C CA  1 
ATOM   2057 C  C   . TRP C 1 83 ? 11.161  -22.622 14.955  1.00 36.84  ? 82  TRP C C   1 
ATOM   2058 O  O   . TRP C 1 83 ? 11.127  -21.460 15.374  1.00 37.45  ? 82  TRP C O   1 
ATOM   2059 C  CB  . TRP C 1 83 ? 9.937   -23.292 12.838  1.00 37.13  ? 82  TRP C CB  1 
ATOM   2060 C  CG  . TRP C 1 83 ? 8.960   -22.149 12.965  1.00 41.42  ? 82  TRP C CG  1 
ATOM   2061 C  CD1 . TRP C 1 83 ? 8.805   -21.101 12.095  1.00 40.15  ? 82  TRP C CD1 1 
ATOM   2062 C  CD2 . TRP C 1 83 ? 8.083   -21.879 14.083  1.00 45.45  ? 82  TRP C CD2 1 
ATOM   2063 N  NE1 . TRP C 1 83 ? 7.840   -20.241 12.556  1.00 40.90  ? 82  TRP C NE1 1 
ATOM   2064 C  CE2 . TRP C 1 83 ? 7.386   -20.683 13.774  1.00 42.96  ? 82  TRP C CE2 1 
ATOM   2065 C  CE3 . TRP C 1 83 ? 7.809   -22.538 15.296  1.00 44.09  ? 82  TRP C CE3 1 
ATOM   2066 C  CZ2 . TRP C 1 83 ? 6.433   -20.144 14.630  1.00 48.91  ? 82  TRP C CZ2 1 
ATOM   2067 C  CZ3 . TRP C 1 83 ? 6.863   -21.996 16.141  1.00 54.39  ? 82  TRP C CZ3 1 
ATOM   2068 C  CH2 . TRP C 1 83 ? 6.200   -20.813 15.814  1.00 44.93  ? 82  TRP C CH2 1 
ATOM   2069 N  N   . GLU C 1 84 ? 11.181  -23.689 15.766  1.00 34.80  ? 83  GLU C N   1 
ATOM   2070 C  CA  . GLU C 1 84 ? 11.055  -23.542 17.213  1.00 39.91  ? 83  GLU C CA  1 
ATOM   2071 C  C   . GLU C 1 84 ? 12.215  -22.773 17.852  1.00 37.39  ? 83  GLU C C   1 
ATOM   2072 O  O   . GLU C 1 84 ? 11.990  -21.878 18.676  1.00 41.99  ? 83  GLU C O   1 
ATOM   2073 C  CB  . GLU C 1 84 ? 10.858  -24.876 17.925  1.00 39.02  ? 83  GLU C CB  1 
ATOM   2074 C  CG  . GLU C 1 84 ? 9.538   -25.548 17.575  1.00 38.61  ? 83  GLU C CG  1 
ATOM   2075 C  CD  . GLU C 1 84 ? 9.425   -26.997 18.005  1.00 42.01  ? 83  GLU C CD  1 
ATOM   2076 O  OE1 . GLU C 1 84 ? 10.395  -27.586 18.571  1.00 41.28  ? 83  GLU C OE1 1 
ATOM   2077 O  OE2 . GLU C 1 84 ? 8.329   -27.537 17.787  1.00 45.47  ? 83  GLU C OE2 1 
ATOM   2078 N  N   . ILE C 1 85 ? 13.457  -23.129 17.520  1.00 39.34  ? 84  ILE C N   1 
ATOM   2079 C  CA  . ILE C 1 85 ? 14.596  -22.512 18.176  1.00 38.35  ? 84  ILE C CA  1 
ATOM   2080 C  C   . ILE C 1 85 ? 14.600  -20.991 17.941  1.00 39.09  ? 84  ILE C C   1 
ATOM   2081 O  O   . ILE C 1 85 ? 14.980  -20.239 18.825  1.00 38.44  ? 84  ILE C O   1 
ATOM   2082 C  CB  . ILE C 1 85 ? 15.914  -23.216 17.806  1.00 37.70  ? 84  ILE C CB  1 
ATOM   2083 C  CG1 . ILE C 1 85 ? 17.024  -22.841 18.801  1.00 39.09  ? 84  ILE C CG1 1 
ATOM   2084 C  CG2 . ILE C 1 85 ? 16.323  -22.972 16.344  1.00 37.94  ? 84  ILE C CG2 1 
ATOM   2085 C  CD1 . ILE C 1 85 ? 18.174  -23.831 18.909  1.00 39.40  ? 84  ILE C CD1 1 
ATOM   2086 N  N   . GLN C 1 86 ? 14.149  -20.549 16.754  1.00 35.03  ? 85  GLN C N   1 
ATOM   2087 C  CA  . GLN C 1 86 ? 14.170  -19.131 16.392  1.00 39.77  ? 85  GLN C CA  1 
ATOM   2088 C  C   . GLN C 1 86 ? 12.899  -18.399 16.838  1.00 37.16  ? 85  GLN C C   1 
ATOM   2089 O  O   . GLN C 1 86 ? 12.943  -17.210 17.151  1.00 43.15  ? 85  GLN C O   1 
ATOM   2090 C  CB  . GLN C 1 86 ? 14.398  -19.027 14.877  1.00 38.41  ? 85  GLN C CB  1 
ATOM   2091 C  CG  . GLN C 1 86 ? 14.513  -17.599 14.345  1.00 37.34  ? 85  GLN C CG  1 
ATOM   2092 C  CD  . GLN C 1 86 ? 14.912  -17.548 12.881  1.00 40.52  ? 85  GLN C CD  1 
ATOM   2093 O  OE1 . GLN C 1 86 ? 14.830  -18.540 12.136  1.00 39.35  ? 85  GLN C OE1 1 
ATOM   2094 N  NE2 . GLN C 1 86 ? 15.468  -16.412 12.480  1.00 43.20  ? 85  GLN C NE2 1 
ATOM   2095 N  N   . ASN C 1 87 ? 11.757  -19.079 16.857  1.00 40.68  ? 86  ASN C N   1 
ATOM   2096 C  CA  . ASN C 1 87 ? 10.488  -18.381 17.013  1.00 42.02  ? 86  ASN C CA  1 
ATOM   2097 C  C   . ASN C 1 87 ? 9.883   -18.609 18.404  1.00 45.43  ? 86  ASN C C   1 
ATOM   2098 O  O   . ASN C 1 87 ? 9.287   -17.689 18.961  1.00 47.15  ? 86  ASN C O   1 
ATOM   2099 C  CB  . ASN C 1 87 ? 9.535   -18.660 15.860  1.00 40.03  ? 86  ASN C CB  1 
ATOM   2100 C  CG  . ASN C 1 87 ? 10.124  -18.079 14.606  1.00 45.02  ? 86  ASN C CG  1 
ATOM   2101 O  OD1 . ASN C 1 87 ? 10.195  -16.851 14.496  1.00 42.91  ? 86  ASN C OD1 1 
ATOM   2102 N  ND2 . ASN C 1 87 ? 10.632  -18.917 13.710  1.00 40.94  ? 86  ASN C ND2 1 
ATOM   2103 N  N   . ASN C 1 88 ? 10.059  -19.811 18.972  1.00 46.92  ? 87  ASN C N   1 
ATOM   2104 C  CA  . ASN C 1 88 ? 9.333   -20.177 20.186  1.00 43.55  ? 87  ASN C CA  1 
ATOM   2105 C  C   . ASN C 1 88 ? 10.182  -21.076 21.088  1.00 43.09  ? 87  ASN C C   1 
ATOM   2106 O  O   . ASN C 1 88 ? 9.738   -22.172 21.472  1.00 43.93  ? 87  ASN C O   1 
ATOM   2107 C  CB  . ASN C 1 88 ? 8.014   -20.854 19.841  1.00 49.97  ? 87  ASN C CB  1 
ATOM   2108 C  CG  . ASN C 1 88 ? 7.053   -20.846 21.010  1.00 58.01  ? 87  ASN C CG  1 
ATOM   2109 O  OD1 . ASN C 1 88 ? 7.266   -20.128 21.997  1.00 62.27  ? 87  ASN C OD1 1 
ATOM   2110 N  ND2 . ASN C 1 88 ? 5.984   -21.618 20.901  1.00 57.80  ? 87  ASN C ND2 1 
ATOM   2111 N  N   . PRO C 1 89 ? 11.418  -20.650 21.439  1.00 40.24  ? 88  PRO C N   1 
ATOM   2112 C  CA  . PRO C 1 89 ? 12.391  -21.537 22.088  1.00 45.57  ? 88  PRO C CA  1 
ATOM   2113 C  C   . PRO C 1 89 ? 12.193  -21.937 23.545  1.00 53.09  ? 88  PRO C C   1 
ATOM   2114 O  O   . PRO C 1 89 ? 12.909  -22.818 24.020  1.00 48.91  ? 88  PRO C O   1 
ATOM   2115 C  CB  . PRO C 1 89 ? 13.727  -20.824 21.940  1.00 39.09  ? 88  PRO C CB  1 
ATOM   2116 C  CG  . PRO C 1 89 ? 13.344  -19.363 21.796  1.00 46.24  ? 88  PRO C CG  1 
ATOM   2117 C  CD  . PRO C 1 89 ? 11.989  -19.334 21.129  1.00 41.02  ? 88  PRO C CD  1 
ATOM   2118 N  N   . HIS C 1 90 ? 11.247  -21.281 24.232  1.00 54.60  ? 89  HIS C N   1 
ATOM   2119 C  CA  . HIS C 1 90 ? 11.039  -21.546 25.648  1.00 51.73  ? 89  HIS C CA  1 
ATOM   2120 C  C   . HIS C 1 90 ? 9.583   -21.918 25.948  1.00 58.93  ? 89  HIS C C   1 
ATOM   2121 O  O   . HIS C 1 90 ? 9.160   -21.867 27.097  1.00 62.92  ? 89  HIS C O   1 
ATOM   2122 C  CB  . HIS C 1 90 ? 11.607  -20.414 26.510  1.00 43.22  ? 89  HIS C CB  1 
ATOM   2123 C  CG  . HIS C 1 90 ? 13.057  -20.073 26.323  1.00 37.44  ? 89  HIS C CG  1 
ATOM   2124 N  ND1 . HIS C 1 90 ? 13.496  -18.886 25.778  1.00 43.07  ? 89  HIS C ND1 1 
ATOM   2125 C  CD2 . HIS C 1 90 ? 14.183  -20.745 26.665  1.00 42.47  ? 89  HIS C CD2 1 
ATOM   2126 C  CE1 . HIS C 1 90 ? 14.825  -18.849 25.763  1.00 45.86  ? 89  HIS C CE1 1 
ATOM   2127 N  NE2 . HIS C 1 90 ? 15.271  -19.970 26.306  1.00 45.80  ? 89  HIS C NE2 1 
ATOM   2128 N  N   . ALA C 1 91 ? 8.823   -22.334 24.928  1.00 58.71  ? 90  ALA C N   1 
ATOM   2129 C  CA  . ALA C 1 91 ? 7.507   -22.928 25.126  1.00 59.12  ? 90  ALA C CA  1 
ATOM   2130 C  C   . ALA C 1 91 ? 7.627   -24.334 25.727  1.00 62.98  ? 90  ALA C C   1 
ATOM   2131 O  O   . ALA C 1 91 ? 8.712   -24.911 25.775  1.00 66.73  ? 90  ALA C O   1 
ATOM   2132 C  CB  . ALA C 1 91 ? 6.736   -22.951 23.818  1.00 58.77  ? 90  ALA C CB  1 
ATOM   2133 N  N   . SER C 1 92 ? 6.477   -24.893 26.128  1.00 70.91  ? 91  SER C N   1 
ATOM   2134 C  CA  . SER C 1 92 ? 6.379   -26.127 26.899  1.00 71.38  ? 91  SER C CA  1 
ATOM   2135 C  C   . SER C 1 92 ? 6.768   -27.355 26.082  1.00 70.10  ? 91  SER C C   1 
ATOM   2136 O  O   . SER C 1 92 ? 7.735   -28.031 26.420  1.00 71.15  ? 91  SER C O   1 
ATOM   2137 C  CB  . SER C 1 92 ? 4.997   -26.297 27.475  1.00 64.53  ? 91  SER C CB  1 
ATOM   2138 O  OG  . SER C 1 92 ? 4.874   -25.501 28.640  1.00 73.03  ? 91  SER C OG  1 
ATOM   2139 N  N   . TYR C 1 93 ? 5.952   -27.659 25.063  1.00 68.51  ? 92  TYR C N   1 
ATOM   2140 C  CA  . TYR C 1 93 ? 6.078   -28.837 24.215  1.00 71.79  ? 92  TYR C CA  1 
ATOM   2141 C  C   . TYR C 1 93 ? 5.924   -30.118 25.055  1.00 75.69  ? 92  TYR C C   1 
ATOM   2142 O  O   . TYR C 1 93 ? 4.885   -30.298 25.731  1.00 77.80  ? 92  TYR C O   1 
ATOM   2143 C  CB  . TYR C 1 93 ? 7.398   -28.828 23.436  1.00 72.25  ? 92  TYR C CB  1 
ATOM   2144 C  CG  . TYR C 1 93 ? 7.682   -27.574 22.616  1.00 65.77  ? 92  TYR C CG  1 
ATOM   2145 C  CD1 . TYR C 1 93 ? 6.937   -27.283 21.475  1.00 60.02  ? 92  TYR C CD1 1 
ATOM   2146 C  CD2 . TYR C 1 93 ? 8.721   -26.712 22.953  1.00 60.45  ? 92  TYR C CD2 1 
ATOM   2147 C  CE1 . TYR C 1 93 ? 7.192   -26.158 20.710  1.00 57.76  ? 92  TYR C CE1 1 
ATOM   2148 C  CE2 . TYR C 1 93 ? 8.989   -25.586 22.188  1.00 58.58  ? 92  TYR C CE2 1 
ATOM   2149 C  CZ  . TYR C 1 93 ? 8.224   -25.309 21.068  1.00 60.18  ? 92  TYR C CZ  1 
ATOM   2150 O  OH  . TYR C 1 93 ? 8.472   -24.198 20.307  1.00 60.52  ? 92  TYR C OH  1 
HETATM 2151 S  S   . SO4 D 2 .  ? 1.602   -33.751 1.779   1.00 115.07 ? 101 SO4 A S   1 
HETATM 2152 O  O1  . SO4 D 2 .  ? 2.357   -34.443 0.765   1.00 89.86  ? 101 SO4 A O1  1 
HETATM 2153 O  O2  . SO4 D 2 .  ? 1.474   -32.360 1.426   1.00 110.42 ? 101 SO4 A O2  1 
HETATM 2154 O  O3  . SO4 D 2 .  ? 0.292   -34.342 1.883   1.00 118.22 ? 101 SO4 A O3  1 
HETATM 2155 O  O4  . SO4 D 2 .  ? 2.285   -33.862 3.042   1.00 110.15 ? 101 SO4 A O4  1 
HETATM 2156 S  S   . SO4 E 2 .  ? -9.151  -24.687 1.045   1.00 107.53 ? 102 SO4 A S   1 
HETATM 2157 O  O1  . SO4 E 2 .  ? -9.918  -24.403 -0.139  1.00 101.14 ? 102 SO4 A O1  1 
HETATM 2158 O  O2  . SO4 E 2 .  ? -9.265  -23.587 1.966   1.00 103.59 ? 102 SO4 A O2  1 
HETATM 2159 O  O3  . SO4 E 2 .  ? -9.641  -25.892 1.667   1.00 105.76 ? 102 SO4 A O3  1 
HETATM 2160 O  O4  . SO4 E 2 .  ? -7.772  -24.863 0.686   1.00 119.58 ? 102 SO4 A O4  1 
HETATM 2161 C  C1  . EDO F 3 .  ? 14.350  -19.506 -7.266  1.00 36.09  ? 103 EDO A C1  1 
HETATM 2162 O  O1  . EDO F 3 .  ? 15.627  -18.857 -7.248  1.00 34.05  ? 103 EDO A O1  1 
HETATM 2163 C  C2  . EDO F 3 .  ? 13.477  -19.060 -8.404  1.00 36.26  ? 103 EDO A C2  1 
HETATM 2164 O  O2  . EDO F 3 .  ? 12.916  -17.772 -8.286  1.00 33.66  ? 103 EDO A O2  1 
HETATM 2165 S  S   . SO4 G 2 .  ? 9.492   -29.501 5.761   1.00 57.44  ? 104 SO4 A S   1 
HETATM 2166 O  O1  . SO4 G 2 .  ? 10.287  -28.951 4.723   1.00 50.30  ? 104 SO4 A O1  1 
HETATM 2167 O  O2  . SO4 G 2 .  ? 8.808   -30.668 5.228   1.00 66.93  ? 104 SO4 A O2  1 
HETATM 2168 O  O3  . SO4 G 2 .  ? 10.325  -29.905 6.873   1.00 64.45  ? 104 SO4 A O3  1 
HETATM 2169 O  O4  . SO4 G 2 .  ? 8.512   -28.532 6.178   1.00 71.25  ? 104 SO4 A O4  1 
HETATM 2170 S  S   . SO4 H 2 .  ? 7.462   -8.572  -25.145 1.00 72.70  ? 101 SO4 B S   1 
HETATM 2171 O  O1  . SO4 H 2 .  ? 8.635   -8.475  -26.002 1.00 47.77  ? 101 SO4 B O1  1 
HETATM 2172 O  O2  . SO4 H 2 .  ? 6.428   -9.373  -25.761 1.00 52.97  ? 101 SO4 B O2  1 
HETATM 2173 O  O3  . SO4 H 2 .  ? 7.811   -9.183  -23.879 1.00 55.51  ? 101 SO4 B O3  1 
HETATM 2174 O  O4  . SO4 H 2 .  ? 6.985   -7.226  -24.927 1.00 72.84  ? 101 SO4 B O4  1 
HETATM 2175 S  S   . SO4 I 2 .  ? 14.670  -27.008 -26.755 1.00 59.29  ? 102 SO4 B S   1 
HETATM 2176 O  O1  . SO4 I 2 .  ? 15.875  -26.473 -26.195 1.00 64.61  ? 102 SO4 B O1  1 
HETATM 2177 O  O2  . SO4 I 2 .  ? 14.998  -28.197 -27.514 1.00 70.22  ? 102 SO4 B O2  1 
HETATM 2178 O  O3  . SO4 I 2 .  ? 13.765  -27.367 -25.697 1.00 70.29  ? 102 SO4 B O3  1 
HETATM 2179 O  O4  . SO4 I 2 .  ? 14.037  -26.037 -27.613 1.00 55.50  ? 102 SO4 B O4  1 
HETATM 2180 C  C1  . 2NU J 4 .  ? 16.665  -14.093 -26.054 0.68 33.95  ? 103 2NU B C1  1 
HETATM 2181 C  C2  . 2NU J 4 .  ? 17.567  -14.479 -23.841 0.68 42.99  ? 103 2NU B C2  1 
HETATM 2182 C  C3  . 2NU J 4 .  ? 17.900  -15.485 -22.738 0.68 46.18  ? 103 2NU B C3  1 
HETATM 2183 C  C4  . 2NU J 4 .  ? 18.268  -14.611 -20.430 0.68 46.73  ? 103 2NU B C4  1 
HETATM 2184 C  C5  . 2NU J 4 .  ? 19.281  -13.934 -19.836 0.68 51.16  ? 103 2NU B C5  1 
HETATM 2185 C  C6  . 2NU J 4 .  ? 20.286  -13.823 -20.787 0.68 53.66  ? 103 2NU B C6  1 
HETATM 2186 C  C7  . 2NU J 4 .  ? 17.431  -16.435 -25.279 0.68 34.49  ? 103 2NU B C7  1 
HETATM 2187 C  C8  . 2NU J 4 .  ? 18.763  -16.875 -25.798 0.68 34.48  ? 103 2NU B C8  1 
HETATM 2188 C  C9  . 2NU J 4 .  ? 17.547  -16.937 -26.688 0.68 26.18  ? 103 2NU B C9  1 
HETATM 2189 N  N1  . 2NU J 4 .  ? 17.230  -14.976 -25.045 0.68 35.93  ? 103 2NU B N1  1 
HETATM 2190 N  N2  . 2NU J 4 .  ? 18.670  -14.858 -21.679 0.68 50.02  ? 103 2NU B N2  1 
HETATM 2191 N  N3  . 2NU J 4 .  ? 19.919  -14.387 -21.922 0.68 50.36  ? 103 2NU B N3  1 
HETATM 2192 O  O1  . 2NU J 4 .  ? 17.641  -13.276 -23.632 0.68 38.80  ? 103 2NU B O1  1 
HETATM 2193 BR BR1 . 2NU J 4 .  ? 19.271  -13.247 -18.086 0.68 54.30  ? 103 2NU B BR1 1 
HETATM 2194 C  C1  . EDO K 3 .  ? 17.094  -36.387 16.278  1.00 37.39  ? 101 EDO C C1  1 
HETATM 2195 O  O1  . EDO K 3 .  ? 15.965  -37.104 15.740  1.00 42.88  ? 101 EDO C O1  1 
HETATM 2196 C  C2  . EDO K 3 .  ? 16.746  -35.459 17.419  1.00 35.56  ? 101 EDO C C2  1 
HETATM 2197 O  O2  . EDO K 3 .  ? 15.809  -35.970 18.356  1.00 34.75  ? 101 EDO C O2  1 
HETATM 2198 S  S   . SO4 L 2 .  ? 29.599  -38.641 12.294  1.00 105.84 ? 102 SO4 C S   1 
HETATM 2199 O  O1  . SO4 L 2 .  ? 30.646  -37.657 12.186  1.00 109.98 ? 102 SO4 C O1  1 
HETATM 2200 O  O2  . SO4 L 2 .  ? 28.612  -38.406 11.272  1.00 93.25  ? 102 SO4 C O2  1 
HETATM 2201 O  O3  . SO4 L 2 .  ? 30.148  -39.959 12.129  1.00 89.15  ? 102 SO4 C O3  1 
HETATM 2202 O  O4  . SO4 L 2 .  ? 28.991  -38.543 13.594  1.00 114.32 ? 102 SO4 C O4  1 
HETATM 2203 O  O   . HOH M 5 .  ? 9.494   -32.307 3.847   1.00 54.91  ? 201 HOH A O   1 
HETATM 2204 O  O   . HOH M 5 .  ? 6.390   -29.137 6.755   1.00 53.69  ? 202 HOH A O   1 
HETATM 2205 O  O   . HOH M 5 .  ? -5.478  -13.411 -16.628 1.00 49.09  ? 203 HOH A O   1 
HETATM 2206 O  O   . HOH M 5 .  ? 11.622  -29.722 2.869   1.00 48.25  ? 204 HOH A O   1 
HETATM 2207 O  O   . HOH M 5 .  ? -2.373  -11.836 13.617  1.00 51.25  ? 205 HOH A O   1 
HETATM 2208 O  O   . HOH M 5 .  ? -1.831  -30.944 -3.792  1.00 53.34  ? 206 HOH A O   1 
HETATM 2209 O  O   . HOH M 5 .  ? 0.915   -10.724 -15.516 1.00 47.34  ? 207 HOH A O   1 
HETATM 2210 O  O   . HOH M 5 .  ? 9.729   -18.375 10.286  1.00 70.63  ? 208 HOH A O   1 
HETATM 2211 O  O   . HOH M 5 .  ? 13.118  -12.241 8.066   1.00 50.47  ? 209 HOH A O   1 
HETATM 2212 O  O   . HOH M 5 .  ? 9.541   -18.196 -10.950 1.00 37.35  ? 210 HOH A O   1 
HETATM 2213 O  O   . HOH M 5 .  ? -1.874  3.058   -1.988  1.00 47.60  ? 211 HOH A O   1 
HETATM 2214 O  O   . HOH M 5 .  ? 0.394   -33.759 4.739   1.00 60.09  ? 212 HOH A O   1 
HETATM 2215 O  O   . HOH M 5 .  ? 11.445  -23.830 9.772   1.00 37.45  ? 213 HOH A O   1 
HETATM 2216 O  O   . HOH M 5 .  ? -7.337  -21.295 -4.239  1.00 82.46  ? 214 HOH A O   1 
HETATM 2217 O  O   . HOH M 5 .  ? -0.030  -29.685 10.026  1.00 59.46  ? 215 HOH A O   1 
HETATM 2218 O  O   . HOH M 5 .  ? 5.086   -7.907  1.199   1.00 34.77  ? 216 HOH A O   1 
HETATM 2219 O  O   . HOH M 5 .  ? 9.953   -6.064  -1.654  1.00 36.39  ? 217 HOH A O   1 
HETATM 2220 O  O   . HOH M 5 .  ? -3.467  -11.063 6.794   1.00 41.28  ? 218 HOH A O   1 
HETATM 2221 O  O   . HOH M 5 .  ? 16.444  -24.562 1.699   1.00 40.08  ? 219 HOH A O   1 
HETATM 2222 O  O   . HOH M 5 .  ? 4.783   -3.639  -3.284  1.00 33.45  ? 220 HOH A O   1 
HETATM 2223 O  O   . HOH M 5 .  ? 11.300  -5.191  -7.826  1.00 36.71  ? 221 HOH A O   1 
HETATM 2224 O  O   . HOH M 5 .  ? 3.694   -29.690 -0.542  1.00 42.88  ? 222 HOH A O   1 
HETATM 2225 O  O   . HOH M 5 .  ? 0.735   -23.422 9.320   1.00 47.60  ? 223 HOH A O   1 
HETATM 2226 O  O   . HOH M 5 .  ? 1.494   -24.914 13.977  1.00 51.74  ? 224 HOH A O   1 
HETATM 2227 O  O   . HOH M 5 .  ? 20.299  -15.491 7.335   1.00 30.38  ? 225 HOH A O   1 
HETATM 2228 O  O   . HOH M 5 .  ? 7.150   -10.511 -12.122 1.00 42.24  ? 226 HOH A O   1 
HETATM 2229 O  O   . HOH M 5 .  ? -7.766  -15.810 -1.103  1.00 36.93  ? 227 HOH A O   1 
HETATM 2230 O  O   . HOH M 5 .  ? -7.442  -16.769 1.648   1.00 41.62  ? 228 HOH A O   1 
HETATM 2231 O  O   . HOH M 5 .  ? 11.888  -11.993 5.960   1.00 37.77  ? 229 HOH A O   1 
HETATM 2232 O  O   . HOH M 5 .  ? 2.096   0.488   -7.572  1.00 42.04  ? 230 HOH A O   1 
HETATM 2233 O  O   . HOH M 5 .  ? -5.349  -15.999 -8.061  1.00 30.17  ? 231 HOH A O   1 
HETATM 2234 O  O   . HOH M 5 .  ? 9.274   -16.214 -13.228 1.00 38.84  ? 232 HOH A O   1 
HETATM 2235 O  O   . HOH M 5 .  ? -0.250  -21.023 6.946   1.00 35.29  ? 233 HOH A O   1 
HETATM 2236 O  O   . HOH M 5 .  ? 8.755   -17.819 -15.955 1.00 62.59  ? 234 HOH A O   1 
HETATM 2237 O  O   . HOH M 5 .  ? -7.595  -17.232 6.593   1.00 43.03  ? 235 HOH A O   1 
HETATM 2238 O  O   . HOH M 5 .  ? 13.684  -12.024 -4.217  1.00 25.50  ? 236 HOH A O   1 
HETATM 2239 O  O   . HOH M 5 .  ? 16.075  -12.076 -5.267  1.00 35.95  ? 237 HOH A O   1 
HETATM 2240 O  O   . HOH M 5 .  ? 2.949   -25.285 -10.018 1.00 40.95  ? 238 HOH A O   1 
HETATM 2241 O  O   . HOH M 5 .  ? 2.218   -4.706  -10.242 1.00 38.95  ? 239 HOH A O   1 
HETATM 2242 O  O   . HOH M 5 .  ? -5.495  -19.896 -5.530  1.00 38.62  ? 240 HOH A O   1 
HETATM 2243 O  O   . HOH M 5 .  ? 17.617  -12.885 1.373   1.00 23.38  ? 241 HOH A O   1 
HETATM 2244 O  O   . HOH M 5 .  ? 14.432  -15.622 -9.277  1.00 40.57  ? 242 HOH A O   1 
HETATM 2245 O  O   . HOH M 5 .  ? -4.116  -25.913 -5.698  1.00 49.24  ? 243 HOH A O   1 
HETATM 2246 O  O   . HOH M 5 .  ? 14.099  -28.205 -4.668  1.00 55.35  ? 244 HOH A O   1 
HETATM 2247 O  O   . HOH M 5 .  ? 7.044   -5.939  0.369   1.00 50.48  ? 245 HOH A O   1 
HETATM 2248 O  O   . HOH M 5 .  ? -3.638  -21.252 6.096   1.00 43.76  ? 246 HOH A O   1 
HETATM 2249 O  O   . HOH M 5 .  ? -5.937  -11.587 -11.498 1.00 42.11  ? 247 HOH A O   1 
HETATM 2250 O  O   . HOH M 5 .  ? 11.921  -12.367 -6.180  1.00 29.62  ? 248 HOH A O   1 
HETATM 2251 O  O   . HOH M 5 .  ? -1.341  -22.095 -0.660  1.00 28.99  ? 249 HOH A O   1 
HETATM 2252 O  O   . HOH M 5 .  ? -1.160  -11.877 11.252  1.00 41.49  ? 250 HOH A O   1 
HETATM 2253 O  O   . HOH M 5 .  ? 8.300   -17.562 8.631   1.00 41.22  ? 251 HOH A O   1 
HETATM 2254 O  O   . HOH M 5 .  ? 1.951   -10.592 11.576  1.00 37.11  ? 252 HOH A O   1 
HETATM 2255 O  O   . HOH M 5 .  ? 16.774  -11.539 -17.131 1.00 45.34  ? 253 HOH A O   1 
HETATM 2256 O  O   . HOH M 5 .  ? -11.151 -16.350 -4.116  1.00 61.14  ? 254 HOH A O   1 
HETATM 2257 O  O   . HOH M 5 .  ? 10.500  -13.078 9.639   1.00 41.76  ? 255 HOH A O   1 
HETATM 2258 O  O   . HOH M 5 .  ? 13.365  -9.476  -7.172  1.00 48.62  ? 256 HOH A O   1 
HETATM 2259 O  O   . HOH M 5 .  ? 6.662   -16.274 -15.135 1.00 50.28  ? 257 HOH A O   1 
HETATM 2260 O  O   . HOH M 5 .  ? 5.449   -7.663  3.993   1.00 37.09  ? 258 HOH A O   1 
HETATM 2261 O  O   . HOH M 5 .  ? 10.060  -20.093 -18.558 1.00 54.95  ? 259 HOH A O   1 
HETATM 2262 O  O   . HOH M 5 .  ? 1.941   -18.719 -18.744 1.00 45.77  ? 260 HOH A O   1 
HETATM 2263 O  O   . HOH M 5 .  ? 2.809   -6.325  5.399   1.00 37.95  ? 261 HOH A O   1 
HETATM 2264 O  O   . HOH M 5 .  ? 8.396   -7.894  1.221   1.00 32.89  ? 262 HOH A O   1 
HETATM 2265 O  O   . HOH M 5 .  ? 11.734  -5.862  -3.887  1.00 58.00  ? 263 HOH A O   1 
HETATM 2266 O  O   . HOH M 5 .  ? 4.802   -34.773 4.379   1.00 63.41  ? 264 HOH A O   1 
HETATM 2267 O  O   . HOH M 5 .  ? 2.557   -24.835 -6.522  1.00 61.21  ? 265 HOH A O   1 
HETATM 2268 O  O   . HOH M 5 .  ? -1.263  -7.564  11.434  1.00 42.83  ? 266 HOH A O   1 
HETATM 2269 O  O   . HOH M 5 .  ? -8.026  -19.398 -3.387  1.00 53.47  ? 267 HOH A O   1 
HETATM 2270 O  O   . HOH M 5 .  ? 10.153  -27.730 -7.430  1.00 53.00  ? 268 HOH A O   1 
HETATM 2271 O  O   . HOH M 5 .  ? -5.871  -12.756 6.663   1.00 41.77  ? 269 HOH A O   1 
HETATM 2272 O  O   . HOH M 5 .  ? 13.144  -13.466 -8.592  1.00 47.19  ? 270 HOH A O   1 
HETATM 2273 O  O   . HOH M 5 .  ? -6.929  -11.523 -7.994  1.00 30.86  ? 271 HOH A O   1 
HETATM 2274 O  O   . HOH M 5 .  ? -0.131  -20.913 10.991  1.00 72.31  ? 272 HOH A O   1 
HETATM 2275 O  O   . HOH M 5 .  ? 17.549  -18.212 -9.621  1.00 51.83  ? 273 HOH A O   1 
HETATM 2276 O  O   . HOH M 5 .  ? -3.394  -26.726 7.374   1.00 55.62  ? 274 HOH A O   1 
HETATM 2277 O  O   . HOH M 5 .  ? 11.469  -7.881  0.414   1.00 27.78  ? 275 HOH A O   1 
HETATM 2278 O  O   . HOH M 5 .  ? 21.878  -16.769 -3.562  1.00 33.72  ? 276 HOH A O   1 
HETATM 2279 O  O   . HOH M 5 .  ? -8.284  -21.224 -1.414  1.00 45.42  ? 277 HOH A O   1 
HETATM 2280 O  O   . HOH M 5 .  ? 3.479   -9.872  -13.272 1.00 54.24  ? 278 HOH A O   1 
HETATM 2281 O  O   . HOH M 5 .  ? 16.059  -28.247 -0.867  1.00 53.34  ? 279 HOH A O   1 
HETATM 2282 O  O   . HOH M 5 .  ? 15.573  -13.385 10.625  1.00 56.81  ? 280 HOH A O   1 
HETATM 2283 O  O   . HOH M 5 .  ? -3.434  -7.823  10.552  1.00 49.72  ? 281 HOH A O   1 
HETATM 2284 O  O   . HOH M 5 .  ? 22.857  -16.688 -0.488  1.00 42.43  ? 282 HOH A O   1 
HETATM 2285 O  O   . HOH M 5 .  ? 9.384   -2.753  0.045   1.00 67.02  ? 283 HOH A O   1 
HETATM 2286 O  O   . HOH M 5 .  ? -5.137  -23.635 -6.799  1.00 42.39  ? 284 HOH A O   1 
HETATM 2287 O  O   . HOH M 5 .  ? 9.054   -9.159  -13.983 1.00 40.96  ? 285 HOH A O   1 
HETATM 2288 O  O   . HOH M 5 .  ? 13.679  -15.299 -12.246 1.00 60.11  ? 286 HOH A O   1 
HETATM 2289 O  O   . HOH M 5 .  ? -5.888  -26.647 3.264   1.00 51.70  ? 287 HOH A O   1 
HETATM 2290 O  O   . HOH M 5 .  ? 17.285  -10.026 -9.369  1.00 49.82  ? 288 HOH A O   1 
HETATM 2291 O  O   . HOH M 5 .  ? 1.487   -29.288 -7.205  1.00 58.41  ? 289 HOH A O   1 
HETATM 2292 O  O   . HOH M 5 .  ? 12.008  -21.399 10.610  1.00 51.92  ? 290 HOH A O   1 
HETATM 2293 O  O   . HOH M 5 .  ? -5.491  -22.250 6.131   1.00 57.54  ? 291 HOH A O   1 
HETATM 2294 O  O   . HOH M 5 .  ? -6.959  -14.153 -9.359  1.00 37.56  ? 292 HOH A O   1 
HETATM 2295 O  O   . HOH M 5 .  ? -9.978  -28.365 -1.899  1.00 48.49  ? 293 HOH A O   1 
HETATM 2296 O  O   . HOH M 5 .  ? 11.755  -1.990  -1.832  1.00 46.39  ? 294 HOH A O   1 
HETATM 2297 O  O   . HOH M 5 .  ? 8.300   -30.509 -2.700  1.00 58.59  ? 295 HOH A O   1 
HETATM 2298 O  O   . HOH M 5 .  ? 8.431   -8.310  4.579   1.00 42.00  ? 296 HOH A O   1 
HETATM 2299 O  O   . HOH M 5 .  ? 5.140   -9.537  -11.358 1.00 49.65  ? 297 HOH A O   1 
HETATM 2300 O  O   . HOH M 5 .  ? 6.142   -3.329  0.873   1.00 62.12  ? 298 HOH A O   1 
HETATM 2301 O  O   . HOH M 5 .  ? -10.912 -13.645 -2.922  1.00 47.62  ? 299 HOH A O   1 
HETATM 2302 O  O   . HOH M 5 .  ? -7.042  -19.299 8.048   1.00 57.45  ? 300 HOH A O   1 
HETATM 2303 O  O   . HOH N 5 .  ? 30.675  -8.034  -30.409 1.00 66.65  ? 201 HOH B O   1 
HETATM 2304 O  O   . HOH N 5 .  ? 23.785  -11.056 -22.264 1.00 43.01  ? 202 HOH B O   1 
HETATM 2305 O  O   . HOH N 5 .  ? 10.246  -11.112 -38.416 1.00 53.60  ? 203 HOH B O   1 
HETATM 2306 O  O   . HOH N 5 .  ? 20.267  -21.987 -23.635 1.00 52.87  ? 204 HOH B O   1 
HETATM 2307 O  O   . HOH N 5 .  ? 10.490  -19.395 -43.325 1.00 67.51  ? 205 HOH B O   1 
HETATM 2308 O  O   . HOH N 5 .  ? 30.442  -19.746 -40.625 1.00 41.77  ? 206 HOH B O   1 
HETATM 2309 O  O   . HOH N 5 .  ? 6.706   -12.215 -26.323 1.00 46.44  ? 207 HOH B O   1 
HETATM 2310 O  O   . HOH N 5 .  ? 15.701  -17.096 -19.329 1.00 41.76  ? 208 HOH B O   1 
HETATM 2311 O  O   . HOH N 5 .  ? 6.010   -7.447  -32.369 1.00 48.71  ? 209 HOH B O   1 
HETATM 2312 O  O   . HOH N 5 .  ? 8.688   -27.651 -38.589 1.00 59.75  ? 210 HOH B O   1 
HETATM 2313 O  O   . HOH N 5 .  ? 11.141  -7.893  -41.646 1.00 48.12  ? 211 HOH B O   1 
HETATM 2314 O  O   . HOH N 5 .  ? 17.714  -19.646 -42.416 1.00 52.00  ? 212 HOH B O   1 
HETATM 2315 O  O   . HOH N 5 .  ? 25.193  -4.932  -30.277 1.00 47.86  ? 213 HOH B O   1 
HETATM 2316 O  O   . HOH N 5 .  ? 20.179  -2.299  -23.597 1.00 70.13  ? 214 HOH B O   1 
HETATM 2317 O  O   . HOH N 5 .  ? 27.924  -8.128  -29.103 1.00 44.28  ? 215 HOH B O   1 
HETATM 2318 O  O   . HOH N 5 .  ? 20.771  -13.236 -43.126 1.00 43.88  ? 216 HOH B O   1 
HETATM 2319 O  O   . HOH N 5 .  ? 25.843  -4.376  -34.149 1.00 57.49  ? 217 HOH B O   1 
HETATM 2320 O  O   . HOH N 5 .  ? 26.438  -22.982 -31.658 1.00 41.40  ? 218 HOH B O   1 
HETATM 2321 O  O   . HOH N 5 .  ? 13.089  -4.557  -42.206 1.00 58.81  ? 219 HOH B O   1 
HETATM 2322 O  O   . HOH N 5 .  ? 25.388  -5.905  -36.103 1.00 48.67  ? 220 HOH B O   1 
HETATM 2323 O  O   . HOH N 5 .  ? 24.587  -1.606  -36.680 1.00 53.84  ? 221 HOH B O   1 
HETATM 2324 O  O   . HOH N 5 .  ? 23.597  -2.158  -29.696 1.00 48.73  ? 222 HOH B O   1 
HETATM 2325 O  O   . HOH N 5 .  ? 27.132  -10.479 -29.262 1.00 53.38  ? 223 HOH B O   1 
HETATM 2326 O  O   . HOH N 5 .  ? 22.312  3.763   -32.943 1.00 52.79  ? 224 HOH B O   1 
HETATM 2327 O  O   . HOH N 5 .  ? 10.159  -16.747 -44.676 1.00 44.52  ? 225 HOH B O   1 
HETATM 2328 O  O   . HOH N 5 .  ? 10.647  -18.767 -33.253 1.00 34.17  ? 226 HOH B O   1 
HETATM 2329 O  O   . HOH N 5 .  ? 20.898  -25.765 -30.361 1.00 60.79  ? 227 HOH B O   1 
HETATM 2330 O  O   . HOH N 5 .  ? 16.876  -19.210 -29.200 1.00 29.21  ? 228 HOH B O   1 
HETATM 2331 O  O   . HOH N 5 .  ? 18.529  -0.316  -25.752 1.00 57.67  ? 229 HOH B O   1 
HETATM 2332 O  O   . HOH N 5 .  ? 2.968   -8.583  -27.631 1.00 55.31  ? 230 HOH B O   1 
HETATM 2333 O  O   . HOH N 5 .  ? 28.030  -17.467 -25.356 1.00 51.87  ? 231 HOH B O   1 
HETATM 2334 O  O   . HOH N 5 .  ? 18.212  -0.425  -38.872 1.00 34.07  ? 232 HOH B O   1 
HETATM 2335 O  O   . HOH N 5 .  ? 31.559  -12.382 -39.386 1.00 60.31  ? 233 HOH B O   1 
HETATM 2336 O  O   . HOH N 5 .  ? 14.397  -6.274  -41.471 1.00 44.16  ? 234 HOH B O   1 
HETATM 2337 O  O   . HOH N 5 .  ? 19.952  -25.664 -34.631 1.00 42.68  ? 235 HOH B O   1 
HETATM 2338 O  O   . HOH N 5 .  ? 6.995   -19.364 -35.257 1.00 56.73  ? 236 HOH B O   1 
HETATM 2339 O  O   . HOH N 5 .  ? 23.772  -4.036  -37.255 1.00 36.24  ? 237 HOH B O   1 
HETATM 2340 O  O   . HOH N 5 .  ? 13.703  -22.372 -20.927 1.00 62.20  ? 238 HOH B O   1 
HETATM 2341 O  O   . HOH N 5 .  ? 32.544  -18.921 -43.101 1.00 53.56  ? 239 HOH B O   1 
HETATM 2342 O  O   . HOH N 5 .  ? 22.933  -23.055 -29.171 1.00 45.12  ? 240 HOH B O   1 
HETATM 2343 O  O   . HOH N 5 .  ? 32.087  -21.193 -38.543 1.00 43.87  ? 241 HOH B O   1 
HETATM 2344 O  O   . HOH N 5 .  ? 7.465   -18.212 -31.862 1.00 54.60  ? 242 HOH B O   1 
HETATM 2345 O  O   . HOH N 5 .  ? 38.974  -13.118 -40.344 1.00 95.52  ? 243 HOH B O   1 
HETATM 2346 O  O   . HOH N 5 .  ? 8.361   -23.536 -24.487 1.00 59.74  ? 244 HOH B O   1 
HETATM 2347 O  O   . HOH N 5 .  ? 17.872  -15.787 -46.237 1.00 50.96  ? 245 HOH B O   1 
HETATM 2348 O  O   . HOH N 5 .  ? 8.881   -8.648  -16.710 1.00 43.97  ? 246 HOH B O   1 
HETATM 2349 O  O   . HOH N 5 .  ? 7.741   -12.502 -39.364 1.00 60.31  ? 247 HOH B O   1 
HETATM 2350 O  O   . HOH N 5 .  ? 20.294  -10.203 -43.395 1.00 43.76  ? 248 HOH B O   1 
HETATM 2351 O  O   . HOH N 5 .  ? 17.964  -3.414  -22.406 1.00 63.65  ? 249 HOH B O   1 
HETATM 2352 O  O   . HOH N 5 .  ? 35.304  -22.968 -30.335 1.00 71.62  ? 250 HOH B O   1 
HETATM 2353 O  O   . HOH N 5 .  ? 22.125  -15.133 -23.941 1.00 48.90  ? 251 HOH B O   1 
HETATM 2354 O  O   . HOH N 5 .  ? 6.775   -20.567 -25.101 1.00 42.30  ? 252 HOH B O   1 
HETATM 2355 O  O   . HOH N 5 .  ? 14.648  -24.446 -40.710 1.00 44.64  ? 253 HOH B O   1 
HETATM 2356 O  O   . HOH N 5 .  ? 21.145  -6.376  -43.004 1.00 37.87  ? 254 HOH B O   1 
HETATM 2357 O  O   . HOH N 5 .  ? 18.585  -25.921 -29.180 1.00 41.11  ? 255 HOH B O   1 
HETATM 2358 O  O   . HOH N 5 .  ? 20.569  -7.478  -21.305 1.00 58.83  ? 256 HOH B O   1 
HETATM 2359 O  O   . HOH N 5 .  ? 16.962  -9.659  -44.363 1.00 52.32  ? 257 HOH B O   1 
HETATM 2360 O  O   . HOH N 5 .  ? 10.603  -21.833 -32.985 1.00 38.62  ? 258 HOH B O   1 
HETATM 2361 O  O   . HOH N 5 .  ? 26.156  -0.184  -29.878 1.00 51.03  ? 259 HOH B O   1 
HETATM 2362 O  O   . HOH N 5 .  ? 1.828   -12.978 -28.921 1.00 54.48  ? 260 HOH B O   1 
HETATM 2363 O  O   . HOH N 5 .  ? 18.551  -12.844 -44.590 1.00 53.15  ? 261 HOH B O   1 
HETATM 2364 O  O   . HOH N 5 .  ? 28.060  -24.751 -35.522 1.00 46.13  ? 262 HOH B O   1 
HETATM 2365 O  O   . HOH N 5 .  ? 20.613  3.963   -33.355 1.00 41.67  ? 263 HOH B O   1 
HETATM 2366 O  O   . HOH N 5 .  ? 24.777  -6.175  -43.106 1.00 47.56  ? 264 HOH B O   1 
HETATM 2367 O  O   . HOH N 5 .  ? 25.027  -8.012  -23.191 1.00 57.43  ? 265 HOH B O   1 
HETATM 2368 O  O   . HOH N 5 .  ? 18.637  4.651   -34.622 1.00 43.53  ? 266 HOH B O   1 
HETATM 2369 O  O   . HOH N 5 .  ? 7.840   -7.616  -20.770 1.00 58.50  ? 267 HOH B O   1 
HETATM 2370 O  O   . HOH N 5 .  ? 13.348  -20.050 -19.880 1.00 52.10  ? 268 HOH B O   1 
HETATM 2371 O  O   . HOH N 5 .  ? 15.199  -8.037  -43.409 1.00 44.39  ? 269 HOH B O   1 
HETATM 2372 O  O   . HOH N 5 .  ? 17.188  -25.688 -21.121 1.00 61.44  ? 270 HOH B O   1 
HETATM 2373 O  O   . HOH N 5 .  ? 14.996  -21.918 -42.286 1.00 48.57  ? 271 HOH B O   1 
HETATM 2374 O  O   . HOH N 5 .  ? 22.681  -29.239 -35.992 1.00 46.45  ? 272 HOH B O   1 
HETATM 2375 O  O   . HOH N 5 .  ? 7.397   -9.909  -18.727 1.00 49.55  ? 273 HOH B O   1 
HETATM 2376 O  O   . HOH O 5 .  ? 20.716  -20.505 30.648  1.00 69.53  ? 201 HOH C O   1 
HETATM 2377 O  O   . HOH O 5 .  ? 26.702  -37.692 10.422  1.00 50.86  ? 202 HOH C O   1 
HETATM 2378 O  O   . HOH O 5 .  ? 13.442  -19.981 10.854  1.00 59.17  ? 203 HOH C O   1 
HETATM 2379 O  O   . HOH O 5 .  ? 26.885  -39.358 12.746  1.00 42.29  ? 204 HOH C O   1 
HETATM 2380 O  O   . HOH O 5 .  ? 17.500  -17.320 15.353  1.00 47.54  ? 205 HOH C O   1 
HETATM 2381 O  O   . HOH O 5 .  ? 28.192  -37.533 25.249  1.00 55.08  ? 206 HOH C O   1 
HETATM 2382 O  O   . HOH O 5 .  ? 16.088  -21.530 13.602  1.00 48.64  ? 207 HOH C O   1 
HETATM 2383 O  O   . HOH O 5 .  ? 15.309  -39.172 16.948  1.00 56.58  ? 208 HOH C O   1 
HETATM 2384 O  O   . HOH O 5 .  ? 19.464  -20.206 10.554  1.00 44.48  ? 209 HOH C O   1 
HETATM 2385 O  O   . HOH O 5 .  ? 31.936  -33.334 26.011  1.00 50.24  ? 210 HOH C O   1 
HETATM 2386 O  O   . HOH O 5 .  ? 25.909  -19.560 6.700   1.00 45.04  ? 211 HOH C O   1 
HETATM 2387 O  O   . HOH O 5 .  ? 6.199   -26.502 16.817  1.00 55.95  ? 212 HOH C O   1 
HETATM 2388 O  O   . HOH O 5 .  ? 9.129   -19.092 23.447  1.00 52.51  ? 213 HOH C O   1 
HETATM 2389 O  O   . HOH O 5 .  ? 14.864  -37.292 13.408  1.00 41.78  ? 214 HOH C O   1 
HETATM 2390 O  O   . HOH O 5 .  ? 13.267  -31.577 8.212   1.00 33.76  ? 215 HOH C O   1 
HETATM 2391 O  O   . HOH O 5 .  ? 30.730  -31.211 15.780  1.00 50.67  ? 216 HOH C O   1 
HETATM 2392 O  O   . HOH O 5 .  ? 23.551  -41.658 18.488  1.00 42.82  ? 217 HOH C O   1 
HETATM 2393 O  O   . HOH O 5 .  ? 12.335  -28.470 28.237  1.00 55.87  ? 218 HOH C O   1 
HETATM 2394 O  O   . HOH O 5 .  ? 15.393  -21.142 12.221  1.00 39.38  ? 219 HOH C O   1 
HETATM 2395 O  O   . HOH O 5 .  ? 28.806  -15.317 12.927  1.00 52.34  ? 220 HOH C O   1 
HETATM 2396 O  O   . HOH O 5 .  ? 30.780  -40.541 9.590   1.00 46.98  ? 221 HOH C O   1 
HETATM 2397 O  O   . HOH O 5 .  ? 28.300  -37.412 16.006  1.00 49.33  ? 222 HOH C O   1 
HETATM 2398 O  O   . HOH O 5 .  ? 20.404  -41.997 12.206  1.00 31.07  ? 223 HOH C O   1 
HETATM 2399 O  O   . HOH O 5 .  ? 26.152  -18.196 21.096  1.00 59.75  ? 224 HOH C O   1 
HETATM 2400 O  O   . HOH O 5 .  ? 20.214  -26.776 3.515   1.00 56.89  ? 225 HOH C O   1 
HETATM 2401 O  O   . HOH O 5 .  ? 16.641  -38.014 19.945  1.00 52.33  ? 226 HOH C O   1 
HETATM 2402 O  O   . HOH O 5 .  ? 21.894  -20.078 24.439  1.00 78.55  ? 227 HOH C O   1 
HETATM 2403 O  O   . HOH O 5 .  ? 9.079   -37.268 18.080  1.00 51.89  ? 228 HOH C O   1 
HETATM 2404 O  O   . HOH O 5 .  ? 25.891  -33.827 35.056  1.00 59.13  ? 229 HOH C O   1 
HETATM 2405 O  O   . HOH O 5 .  ? 21.187  -29.861 4.906   1.00 62.10  ? 230 HOH C O   1 
HETATM 2406 O  O   . HOH O 5 .  ? 22.635  -28.601 11.151  1.00 34.34  ? 231 HOH C O   1 
HETATM 2407 O  O   . HOH O 5 .  ? 31.423  -29.673 32.506  1.00 76.25  ? 232 HOH C O   1 
HETATM 2408 O  O   . HOH O 5 .  ? 33.630  -24.488 31.765  1.00 57.65  ? 233 HOH C O   1 
HETATM 2409 O  O   . HOH O 5 .  ? 16.092  -17.755 19.425  1.00 43.25  ? 234 HOH C O   1 
HETATM 2410 O  O   . HOH O 5 .  ? 22.519  -34.577 16.648  1.00 29.83  ? 235 HOH C O   1 
HETATM 2411 O  O   . HOH O 5 .  ? 23.518  -18.645 22.014  1.00 59.47  ? 236 HOH C O   1 
HETATM 2412 O  O   . HOH O 5 .  ? 20.928  -40.152 26.587  1.00 44.31  ? 237 HOH C O   1 
HETATM 2413 O  O   . HOH O 5 .  ? 25.538  -31.373 10.932  1.00 37.83  ? 238 HOH C O   1 
HETATM 2414 O  O   . HOH O 5 .  ? 26.029  -17.590 13.977  1.00 50.92  ? 239 HOH C O   1 
HETATM 2415 O  O   . HOH O 5 .  ? 30.081  -40.087 31.533  1.00 47.34  ? 240 HOH C O   1 
HETATM 2416 O  O   . HOH O 5 .  ? 10.036  -30.497 9.960   1.00 36.97  ? 241 HOH C O   1 
HETATM 2417 O  O   . HOH O 5 .  ? 25.777  -39.922 20.277  1.00 37.83  ? 242 HOH C O   1 
HETATM 2418 O  O   . HOH O 5 .  ? 7.214   -17.987 10.800  1.00 41.34  ? 243 HOH C O   1 
HETATM 2419 O  O   . HOH O 5 .  ? 21.310  -28.816 8.619   1.00 36.54  ? 244 HOH C O   1 
HETATM 2420 O  O   . HOH O 5 .  ? 31.745  -43.612 16.060  1.00 60.49  ? 245 HOH C O   1 
HETATM 2421 O  O   . HOH O 5 .  ? 31.440  -40.084 27.470  1.00 43.80  ? 246 HOH C O   1 
HETATM 2422 O  O   . HOH O 5 .  ? 14.738  -29.545 3.921   1.00 41.25  ? 247 HOH C O   1 
HETATM 2423 O  O   . HOH O 5 .  ? 2.918   -28.100 14.432  1.00 50.71  ? 248 HOH C O   1 
HETATM 2424 O  O   . HOH O 5 .  ? 30.803  -17.486 9.594   1.00 48.38  ? 249 HOH C O   1 
HETATM 2425 O  O   . HOH O 5 .  ? 14.301  -39.050 9.177   1.00 59.60  ? 250 HOH C O   1 
HETATM 2426 O  O   . HOH O 5 .  ? 20.368  -36.935 40.583  1.00 61.90  ? 251 HOH C O   1 
HETATM 2427 O  O   . HOH O 5 .  ? 30.731  -36.011 28.980  1.00 51.98  ? 252 HOH C O   1 
HETATM 2428 O  O   . HOH O 5 .  ? 28.751  -25.264 32.923  1.00 48.66  ? 253 HOH C O   1 
HETATM 2429 O  O   . HOH O 5 .  ? 30.647  -32.775 18.360  1.00 50.82  ? 254 HOH C O   1 
HETATM 2430 O  O   . HOH O 5 .  ? 11.949  -36.583 39.007  1.00 68.72  ? 255 HOH C O   1 
HETATM 2431 O  O   . HOH O 5 .  ? 29.381  -41.777 27.402  1.00 42.88  ? 256 HOH C O   1 
HETATM 2432 O  O   . HOH O 5 .  ? 32.455  -43.814 11.776  1.00 58.29  ? 257 HOH C O   1 
HETATM 2433 O  O   . HOH O 5 .  ? 20.895  -13.020 13.413  1.00 51.61  ? 258 HOH C O   1 
HETATM 2434 O  O   . HOH O 5 .  ? 17.587  -37.251 29.072  1.00 55.64  ? 259 HOH C O   1 
HETATM 2435 O  O   . HOH O 5 .  ? 13.745  -23.194 28.016  1.00 53.93  ? 260 HOH C O   1 
HETATM 2436 O  O   . HOH O 5 .  ? 22.981  -14.038 13.610  1.00 53.79  ? 261 HOH C O   1 
HETATM 2437 O  O   . HOH O 5 .  ? 5.122   -24.173 18.265  1.00 73.82  ? 262 HOH C O   1 
HETATM 2438 O  O   . HOH O 5 .  ? 24.022  -15.930 12.006  1.00 50.24  ? 263 HOH C O   1 
HETATM 2439 O  O   . HOH O 5 .  ? 26.209  -14.077 11.318  1.00 50.40  ? 264 HOH C O   1 
HETATM 2440 O  O   . HOH O 5 .  ? 32.154  -39.300 30.103  1.00 54.77  ? 265 HOH C O   1 
HETATM 2441 O  O   . HOH O 5 .  ? 14.958  -34.518 35.569  1.00 56.57  ? 266 HOH C O   1 
HETATM 2442 O  O   . HOH O 5 .  ? 28.626  -41.820 29.950  1.00 45.04  ? 267 HOH C O   1 
HETATM 2443 O  O   . HOH O 5 .  ? 29.234  -40.902 19.702  1.00 67.46  ? 268 HOH C O   1 
HETATM 2444 O  O   . HOH O 5 .  ? 33.863  -44.779 15.520  1.00 43.69  ? 269 HOH C O   1 
HETATM 2445 O  O   . HOH O 5 .  ? 36.955  -24.517 28.094  1.00 74.58  ? 270 HOH C O   1 
HETATM 2446 O  O   . HOH O 5 .  ? 16.156  -42.328 8.234   1.00 48.18  ? 271 HOH C O   1 
# 
