data_7HGL
# 
_entry.id   7HGL 
# 
_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   7HGL         pdb_00007hgl 10.2210/pdb7hgl/pdb 
WWPDB D_1001407447 ?            ?                   
# 
_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                        7HGL 
_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    1   ? ?    ? ? 
4 non-polymer syn '4-[(5-chloro-1,2,3-thiadiazol-4-yl)methyl]morpholine' 219.692   2   ? ?    ? ? 
5 water       nat water                                                  18.015    233 ? ?    ? ? 
# 
_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 '4-[(5-chloro-1,2,3-thiadiazol-4-yl)methyl]morpholine' WJ4 
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 
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 
WJ4 non-polymer         . '4-[(5-chloro-1,2,3-thiadiazol-4-yl)methyl]morpholine' ?                 'C7 H10 Cl N3 O S' 219.692 
# 
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 34 LYS LYS 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 ?  ?   ?   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        WJ4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WJ4 
_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 WJ4 1   103 102 WJ4 LIG B . 
K 2 SO4 1   101 5   SO4 SO4 C . 
L 4 WJ4 1   102 101 WJ4 LIG C . 
M 5 HOH 1   201 27  HOH HOH A . 
M 5 HOH 2   202 95  HOH HOH A . 
M 5 HOH 3   203 85  HOH HOH A . 
M 5 HOH 4   204 111 HOH HOH A . 
M 5 HOH 5   205 274 HOH HOH A . 
M 5 HOH 6   206 8   HOH HOH A . 
M 5 HOH 7   207 202 HOH HOH A . 
M 5 HOH 8   208 87  HOH HOH A . 
M 5 HOH 9   209 34  HOH HOH A . 
M 5 HOH 10  210 208 HOH HOH A . 
M 5 HOH 11  211 142 HOH HOH A . 
M 5 HOH 12  212 37  HOH HOH A . 
M 5 HOH 13  213 91  HOH HOH A . 
M 5 HOH 14  214 164 HOH HOH A . 
M 5 HOH 15  215 333 HOH HOH A . 
M 5 HOH 16  216 199 HOH HOH A . 
M 5 HOH 17  217 165 HOH HOH A . 
M 5 HOH 18  218 307 HOH HOH A . 
M 5 HOH 19  219 66  HOH HOH A . 
M 5 HOH 20  220 19  HOH HOH A . 
M 5 HOH 21  221 145 HOH HOH A . 
M 5 HOH 22  222 260 HOH HOH A . 
M 5 HOH 23  223 289 HOH HOH A . 
M 5 HOH 24  224 12  HOH HOH A . 
M 5 HOH 25  225 143 HOH HOH A . 
M 5 HOH 26  226 304 HOH HOH A . 
M 5 HOH 27  227 26  HOH HOH A . 
M 5 HOH 28  228 99  HOH HOH A . 
M 5 HOH 29  229 97  HOH HOH A . 
M 5 HOH 30  230 42  HOH HOH A . 
M 5 HOH 31  231 23  HOH HOH A . 
M 5 HOH 32  232 60  HOH HOH A . 
M 5 HOH 33  233 58  HOH HOH A . 
M 5 HOH 34  234 115 HOH HOH A . 
M 5 HOH 35  235 2   HOH HOH A . 
M 5 HOH 36  236 113 HOH HOH A . 
M 5 HOH 37  237 203 HOH HOH A . 
M 5 HOH 38  238 84  HOH HOH A . 
M 5 HOH 39  239 31  HOH HOH A . 
M 5 HOH 40  240 22  HOH HOH A . 
M 5 HOH 41  241 1   HOH HOH A . 
M 5 HOH 42  242 47  HOH HOH A . 
M 5 HOH 43  243 9   HOH HOH A . 
M 5 HOH 44  244 28  HOH HOH A . 
M 5 HOH 45  245 7   HOH HOH A . 
M 5 HOH 46  246 21  HOH HOH A . 
M 5 HOH 47  247 222 HOH HOH A . 
M 5 HOH 48  248 267 HOH HOH A . 
M 5 HOH 49  249 211 HOH HOH A . 
M 5 HOH 50  250 86  HOH HOH A . 
M 5 HOH 51  251 55  HOH HOH A . 
M 5 HOH 52  252 32  HOH HOH A . 
M 5 HOH 53  253 218 HOH HOH A . 
M 5 HOH 54  254 73  HOH HOH A . 
M 5 HOH 55  255 14  HOH HOH A . 
M 5 HOH 56  256 190 HOH HOH A . 
M 5 HOH 57  257 139 HOH HOH A . 
M 5 HOH 58  258 300 HOH HOH A . 
M 5 HOH 59  259 35  HOH HOH A . 
M 5 HOH 60  260 293 HOH HOH A . 
M 5 HOH 61  261 288 HOH HOH A . 
M 5 HOH 62  262 38  HOH HOH A . 
M 5 HOH 63  263 179 HOH HOH A . 
M 5 HOH 64  264 156 HOH HOH A . 
M 5 HOH 65  265 20  HOH HOH A . 
M 5 HOH 66  266 93  HOH HOH A . 
M 5 HOH 67  267 131 HOH HOH A . 
M 5 HOH 68  268 292 HOH HOH A . 
M 5 HOH 69  269 78  HOH HOH A . 
M 5 HOH 70  270 63  HOH HOH A . 
M 5 HOH 71  271 167 HOH HOH A . 
M 5 HOH 72  272 270 HOH HOH A . 
M 5 HOH 73  273 283 HOH HOH A . 
M 5 HOH 74  274 16  HOH HOH A . 
M 5 HOH 75  275 301 HOH HOH A . 
M 5 HOH 76  276 287 HOH HOH A . 
M 5 HOH 77  277 71  HOH HOH A . 
M 5 HOH 78  278 188 HOH HOH A . 
M 5 HOH 79  279 318 HOH HOH A . 
M 5 HOH 80  280 109 HOH HOH A . 
M 5 HOH 81  281 64  HOH HOH A . 
M 5 HOH 82  282 83  HOH HOH A . 
M 5 HOH 83  283 278 HOH HOH A . 
M 5 HOH 84  284 185 HOH HOH A . 
M 5 HOH 85  285 219 HOH HOH A . 
M 5 HOH 86  286 327 HOH HOH A . 
M 5 HOH 87  287 210 HOH HOH A . 
M 5 HOH 88  288 132 HOH HOH A . 
M 5 HOH 89  289 281 HOH HOH A . 
M 5 HOH 90  290 332 HOH HOH A . 
M 5 HOH 91  291 57  HOH HOH A . 
M 5 HOH 92  292 297 HOH HOH A . 
M 5 HOH 93  293 75  HOH HOH A . 
M 5 HOH 94  294 259 HOH HOH A . 
M 5 HOH 95  295 125 HOH HOH A . 
M 5 HOH 96  296 205 HOH HOH A . 
M 5 HOH 97  297 206 HOH HOH A . 
M 5 HOH 98  298 77  HOH HOH A . 
M 5 HOH 99  299 152 HOH HOH A . 
M 5 HOH 100 300 94  HOH HOH A . 
N 5 HOH 1   201 68  HOH HOH B . 
N 5 HOH 2   202 54  HOH HOH B . 
N 5 HOH 3   203 10  HOH HOH B . 
N 5 HOH 4   204 17  HOH HOH B . 
N 5 HOH 5   205 272 HOH HOH B . 
N 5 HOH 6   206 331 HOH HOH B . 
N 5 HOH 7   207 123 HOH HOH B . 
N 5 HOH 8   208 153 HOH HOH B . 
N 5 HOH 9   209 249 HOH HOH B . 
N 5 HOH 10  210 89  HOH HOH B . 
N 5 HOH 11  211 168 HOH HOH B . 
N 5 HOH 12  212 177 HOH HOH B . 
N 5 HOH 13  213 13  HOH HOH B . 
N 5 HOH 14  214 175 HOH HOH B . 
N 5 HOH 15  215 247 HOH HOH B . 
N 5 HOH 16  216 224 HOH HOH B . 
N 5 HOH 17  217 59  HOH HOH B . 
N 5 HOH 18  218 329 HOH HOH B . 
N 5 HOH 19  219 69  HOH HOH B . 
N 5 HOH 20  220 258 HOH HOH B . 
N 5 HOH 21  221 315 HOH HOH B . 
N 5 HOH 22  222 98  HOH HOH B . 
N 5 HOH 23  223 6   HOH HOH B . 
N 5 HOH 24  224 61  HOH HOH B . 
N 5 HOH 25  225 24  HOH HOH B . 
N 5 HOH 26  226 74  HOH HOH B . 
N 5 HOH 27  227 96  HOH HOH B . 
N 5 HOH 28  228 280 HOH HOH B . 
N 5 HOH 29  229 5   HOH HOH B . 
N 5 HOH 30  230 150 HOH HOH B . 
N 5 HOH 31  231 214 HOH HOH B . 
N 5 HOH 32  232 217 HOH HOH B . 
N 5 HOH 33  233 36  HOH HOH B . 
N 5 HOH 34  234 197 HOH HOH B . 
N 5 HOH 35  235 137 HOH HOH B . 
N 5 HOH 36  236 25  HOH HOH B . 
N 5 HOH 37  237 172 HOH HOH B . 
N 5 HOH 38  238 119 HOH HOH B . 
N 5 HOH 39  239 117 HOH HOH B . 
N 5 HOH 40  240 261 HOH HOH B . 
N 5 HOH 41  241 320 HOH HOH B . 
N 5 HOH 42  242 279 HOH HOH B . 
N 5 HOH 43  243 223 HOH HOH B . 
N 5 HOH 44  244 79  HOH HOH B . 
N 5 HOH 45  245 169 HOH HOH B . 
N 5 HOH 46  246 157 HOH HOH B . 
N 5 HOH 47  247 72  HOH HOH B . 
N 5 HOH 48  248 101 HOH HOH B . 
N 5 HOH 49  249 201 HOH HOH B . 
N 5 HOH 50  250 322 HOH HOH B . 
N 5 HOH 51  251 120 HOH HOH B . 
N 5 HOH 52  252 160 HOH HOH B . 
N 5 HOH 53  253 242 HOH HOH B . 
N 5 HOH 54  254 46  HOH HOH B . 
N 5 HOH 55  255 76  HOH HOH B . 
N 5 HOH 56  256 104 HOH HOH B . 
N 5 HOH 57  257 291 HOH HOH B . 
N 5 HOH 58  258 182 HOH HOH B . 
N 5 HOH 59  259 303 HOH HOH B . 
N 5 HOH 60  260 312 HOH HOH B . 
N 5 HOH 61  261 215 HOH HOH B . 
N 5 HOH 62  262 163 HOH HOH B . 
N 5 HOH 63  263 44  HOH HOH B . 
N 5 HOH 64  264 316 HOH HOH B . 
N 5 HOH 65  265 334 HOH HOH B . 
N 5 HOH 66  266 314 HOH HOH B . 
N 5 HOH 67  267 107 HOH HOH B . 
N 5 HOH 68  268 170 HOH HOH B . 
O 5 HOH 1   201 296 HOH HOH C . 
O 5 HOH 2   202 321 HOH HOH C . 
O 5 HOH 3   203 53  HOH HOH C . 
O 5 HOH 4   204 323 HOH HOH C . 
O 5 HOH 5   205 198 HOH HOH C . 
O 5 HOH 6   206 290 HOH HOH C . 
O 5 HOH 7   207 226 HOH HOH C . 
O 5 HOH 8   208 126 HOH HOH C . 
O 5 HOH 9   209 43  HOH HOH C . 
O 5 HOH 10  210 269 HOH HOH C . 
O 5 HOH 11  211 309 HOH HOH C . 
O 5 HOH 12  212 302 HOH HOH C . 
O 5 HOH 13  213 40  HOH HOH C . 
O 5 HOH 14  214 102 HOH HOH C . 
O 5 HOH 15  215 298 HOH HOH C . 
O 5 HOH 16  216 294 HOH HOH C . 
O 5 HOH 17  217 317 HOH HOH C . 
O 5 HOH 18  218 173 HOH HOH C . 
O 5 HOH 19  219 325 HOH HOH C . 
O 5 HOH 20  220 45  HOH HOH C . 
O 5 HOH 21  221 65  HOH HOH C . 
O 5 HOH 22  222 275 HOH HOH C . 
O 5 HOH 23  223 118 HOH HOH C . 
O 5 HOH 24  224 151 HOH HOH C . 
O 5 HOH 25  225 4   HOH HOH C . 
O 5 HOH 26  226 254 HOH HOH C . 
O 5 HOH 27  227 90  HOH HOH C . 
O 5 HOH 28  228 324 HOH HOH C . 
O 5 HOH 29  229 15  HOH HOH C . 
O 5 HOH 30  230 41  HOH HOH C . 
O 5 HOH 31  231 146 HOH HOH C . 
O 5 HOH 32  232 122 HOH HOH C . 
O 5 HOH 33  233 67  HOH HOH C . 
O 5 HOH 34  234 271 HOH HOH C . 
O 5 HOH 35  235 82  HOH HOH C . 
O 5 HOH 36  236 305 HOH HOH C . 
O 5 HOH 37  237 284 HOH HOH C . 
O 5 HOH 38  238 103 HOH HOH C . 
O 5 HOH 39  239 209 HOH HOH C . 
O 5 HOH 40  240 184 HOH HOH C . 
O 5 HOH 41  241 171 HOH HOH C . 
O 5 HOH 42  242 49  HOH HOH C . 
O 5 HOH 43  243 189 HOH HOH C . 
O 5 HOH 44  244 56  HOH HOH C . 
O 5 HOH 45  245 299 HOH HOH C . 
O 5 HOH 46  246 134 HOH HOH C . 
O 5 HOH 47  247 148 HOH HOH C . 
O 5 HOH 48  248 62  HOH HOH C . 
O 5 HOH 49  249 241 HOH HOH C . 
O 5 HOH 50  250 130 HOH HOH C . 
O 5 HOH 51  251 161 HOH HOH C . 
O 5 HOH 52  252 246 HOH HOH C . 
O 5 HOH 53  253 70  HOH HOH C . 
O 5 HOH 54  254 135 HOH HOH C . 
O 5 HOH 55  255 328 HOH HOH C . 
O 5 HOH 56  256 48  HOH HOH C . 
O 5 HOH 57  257 295 HOH HOH C . 
O 5 HOH 58  258 92  HOH HOH C . 
O 5 HOH 59  259 313 HOH HOH C . 
O 5 HOH 60  260 149 HOH HOH C . 
O 5 HOH 61  261 108 HOH HOH C . 
O 5 HOH 62  262 116 HOH HOH C . 
O 5 HOH 63  263 319 HOH HOH C . 
O 5 HOH 64  264 310 HOH HOH C . 
O 5 HOH 65  265 330 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 34 ? CG  ? B LYS 35 CG  
15 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
16 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
17 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
18 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
19 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
20 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
21 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
22 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
23 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
24 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
25 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
26 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
27 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
28 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
29 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
30 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
31 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
32 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
33 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
34 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
35 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
36 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
37 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
38 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
39 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
40 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
41 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
42 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
43 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
44 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
45 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
46 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
47 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
48 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
49 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
50 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
51 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
52 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
53 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
54 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
55 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
56 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
57 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
58 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' XDS     .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HGL 
_cell.length_a           41.728 
_cell.length_b           42.207 
_cell.length_c           160.690 
_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                         7HGL 
_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          7HGL 
_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                     7HGL 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             80.35 
_reflns.d_resolution_high            1.73 
_reflns.number_obs                   30673 
_reflns.percent_possible_obs         99.3 
_reflns.pdbx_Rmerge_I_obs            0.130 
_reflns.pdbx_netI_over_sigmaI        5.5 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.143 
_reflns.pdbx_Rpim_I_all              0.058 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     192093 
_reflns.pdbx_chi_squared             0.79 
_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                  1.73 
_reflns_shell.d_res_low                   1.82 
_reflns_shell.number_measured_all         29432 
_reflns_shell.number_unique_obs           4430 
_reflns_shell.Rmerge_I_obs                3.212 
_reflns_shell.pdbx_chi_squared            0.51 
_reflns_shell.pdbx_redundancy             6.6 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             3.487 
_reflns_shell.pdbx_Rpim_I_all             1.344 
_reflns_shell.pdbx_CC_half                0.400 
_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                                 7HGL 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     27874 
_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                             80.35 
_refine.ls_d_res_high                            1.73 
_refine.ls_percent_reflns_obs                    95.41 
_refine.ls_R_factor_obs                          0.26625 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.26183 
_refine.ls_R_factor_R_free                       0.34359 
_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                  1555 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.950 
_refine.correlation_coeff_Fo_to_Fc_free          0.911 
_refine.B_iso_mean                               51.440 
_refine.aniso_B[1][1]                            3.47 
_refine.aniso_B[2][2]                            -1.52 
_refine.aniso_B[3][3]                            -1.95 
_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                       0.172 
_refine.pdbx_overall_ESU_R_Free                  0.182 
_refine.overall_SU_ML                            0.252 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             8.861 
_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         60 
_refine_hist.number_atoms_solvent             233 
_refine_hist.number_atoms_total               2427 
_refine_hist.d_res_high                       1.73 
_refine_hist.d_res_low                        80.35 
# 
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             0.007  0.012  ? 2299 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.930  1.832  ? 3130 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       9.131  5.000  ? 266  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       7.449  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.196 10.000 ? 299  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.142  0.200  ? 288  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1926 '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                  5.355  5.047  ? 1073 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 6.917  9.057  ? 1338 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  5.723  5.283  ? 1226 '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       11.261 77.53  ? 3690 '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                       1.725 
_refine_ls_shell.d_res_low                        1.770 
_refine_ls_shell.number_reflns_R_work             1275 
_refine_ls_shell.R_factor_R_work                  0.495 
_refine_ls_shell.percent_reflns_obs               61.47 
_refine_ls_shell.R_factor_R_free                  0.489 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             102 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGL 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z137790394' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGL 
_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 2 ? 
L N N 4 ? 
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 7HGL A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGL B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGL 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 7HGL GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGL SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGL GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGL SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGL GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGL 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 ? LYS B 66 ? TYR B 61 LYS B 65 1 ? 5  
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 ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O LEU B 54 ? O LEU B 53 N TYR B 41 ? N TYR B 40 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
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                   7HGL 
_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   B HOH 202 ? ? O B HOH 207 ? ? 1.68 
2  1 NH2 C ARG 74  ? ? O C HOH 201 ? ? 1.86 
3  1 O   A HOH 264 ? ? O A HOH 278 ? ? 1.94 
4  1 O   B HOH 228 ? ? O B HOH 250 ? ? 1.96 
5  1 O   A HOH 214 ? ? O A HOH 223 ? ? 1.98 
6  1 O   C HOH 228 ? ? O C HOH 231 ? ? 2.03 
7  1 O   B ASP 62  ? ? O B HOH 201 ? ? 2.03 
8  1 O   A PHE 5   ? ? O A HOH 201 ? ? 2.07 
9  1 N   A LYS 56  ? ? O A HOH 202 ? ? 2.08 
10 1 O   B HOH 224 ? ? O B HOH 260 ? ? 2.10 
11 1 O   B HOH 209 ? ? O B HOH 236 ? ? 2.10 
12 1 O2  C SO4 101 ? ? O C HOH 202 ? ? 2.18 
13 1 O   B HOH 249 ? ? O B HOH 254 ? ? 2.18 
14 1 O   B HOH 254 ? ? O B HOH 260 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     220 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     292 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_545 
_pdbx_validate_symm_contact.dist              2.10 
# 
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 38 ? ? 78.00   -1.25  
2 1 ASN A 87 ? ? -151.85 65.79  
3 1 PRO B 55 ? ? -49.47  -18.66 
4 1 ASN B 87 ? ? -160.22 56.86  
5 1 ALA B 90 ? ? -42.88  151.01 
6 1 PRO C 36 ? ? -44.92  159.09 
7 1 SER C 64 ? ? -153.41 19.16  
8 1 HIS C 89 ? ? -144.52 12.85  
9 1 SER C 91 ? ? -75.71  -81.10 
# 
_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   B 
_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   B 
_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            141.98 
# 
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 C GLY 0  ? C GLY 1  
9  1 Y 1 C MET 1  ? C MET 2  
10 1 Y 1 C PRO 2  ? C PRO 3  
11 1 Y 1 C ILE 28 ? C ILE 29 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
SO4 S    S  N N 314 
SO4 O1   O  N N 315 
SO4 O2   O  N N 316 
SO4 O3   O  N N 317 
SO4 O4   O  N N 318 
THR N    N  N N 319 
THR CA   C  N S 320 
THR C    C  N N 321 
THR O    O  N N 322 
THR CB   C  N R 323 
THR OG1  O  N N 324 
THR CG2  C  N N 325 
THR OXT  O  N N 326 
THR H    H  N N 327 
THR H2   H  N N 328 
THR HA   H  N N 329 
THR HB   H  N N 330 
THR HG1  H  N N 331 
THR HG21 H  N N 332 
THR HG22 H  N N 333 
THR HG23 H  N N 334 
THR HXT  H  N N 335 
TRP N    N  N N 336 
TRP CA   C  N S 337 
TRP C    C  N N 338 
TRP O    O  N N 339 
TRP CB   C  N N 340 
TRP CG   C  Y N 341 
TRP CD1  C  Y N 342 
TRP CD2  C  Y N 343 
TRP NE1  N  Y N 344 
TRP CE2  C  Y N 345 
TRP CE3  C  Y N 346 
TRP CZ2  C  Y N 347 
TRP CZ3  C  Y N 348 
TRP CH2  C  Y N 349 
TRP OXT  O  N N 350 
TRP H    H  N N 351 
TRP H2   H  N N 352 
TRP HA   H  N N 353 
TRP HB2  H  N N 354 
TRP HB3  H  N N 355 
TRP HD1  H  N N 356 
TRP HE1  H  N N 357 
TRP HE3  H  N N 358 
TRP HZ2  H  N N 359 
TRP HZ3  H  N N 360 
TRP HH2  H  N N 361 
TRP HXT  H  N N 362 
TYR N    N  N N 363 
TYR CA   C  N S 364 
TYR C    C  N N 365 
TYR O    O  N N 366 
TYR CB   C  N N 367 
TYR CG   C  Y N 368 
TYR CD1  C  Y N 369 
TYR CD2  C  Y N 370 
TYR CE1  C  Y N 371 
TYR CE2  C  Y N 372 
TYR CZ   C  Y N 373 
TYR OH   O  N N 374 
TYR OXT  O  N N 375 
TYR H    H  N N 376 
TYR H2   H  N N 377 
TYR HA   H  N N 378 
TYR HB2  H  N N 379 
TYR HB3  H  N N 380 
TYR HD1  H  N N 381 
TYR HD2  H  N N 382 
TYR HE1  H  N N 383 
TYR HE2  H  N N 384 
TYR HH   H  N N 385 
TYR HXT  H  N N 386 
VAL N    N  N N 387 
VAL CA   C  N S 388 
VAL C    C  N N 389 
VAL O    O  N N 390 
VAL CB   C  N N 391 
VAL CG1  C  N N 392 
VAL CG2  C  N N 393 
VAL OXT  O  N N 394 
VAL H    H  N N 395 
VAL H2   H  N N 396 
VAL HA   H  N N 397 
VAL HB   H  N N 398 
VAL HG11 H  N N 399 
VAL HG12 H  N N 400 
VAL HG13 H  N N 401 
VAL HG21 H  N N 402 
VAL HG22 H  N N 403 
VAL HG23 H  N N 404 
VAL HXT  H  N N 405 
WJ4 N1   N  Y N 406 
WJ4 C4   C  N N 407 
WJ4 C5   C  N N 408 
WJ4 C6   C  N N 409 
WJ4 N    N  Y N 410 
WJ4 C    C  Y N 411 
WJ4 O    O  N N 412 
WJ4 C1   C  Y N 413 
WJ4 C2   C  N N 414 
WJ4 C3   C  N N 415 
WJ4 N2   N  N N 416 
WJ4 S    S  Y N 417 
WJ4 CL   CL N N 418 
WJ4 H5   H  N N 419 
WJ4 H4   H  N N 420 
WJ4 H6   H  N N 421 
WJ4 H7   H  N N 422 
WJ4 H8   H  N N 423 
WJ4 H9   H  N N 424 
WJ4 H1   H  N N 425 
WJ4 H    H  N N 426 
WJ4 H3   H  N N 427 
WJ4 H2   H  N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
WJ4 C   CL   sing N N 389 
WJ4 C   S    sing Y N 390 
WJ4 S   N    sing Y N 391 
WJ4 N   N1   doub Y N 392 
WJ4 N1  C1   sing Y N 393 
WJ4 C1  C    doub Y N 394 
WJ4 C2  C1   sing N N 395 
WJ4 N2  C2   sing N N 396 
WJ4 N2  C3   sing N N 397 
WJ4 C3  C4   sing N N 398 
WJ4 C4  O    sing N N 399 
WJ4 O   C5   sing N N 400 
WJ4 C5  C6   sing N N 401 
WJ4 C6  N2   sing N N 402 
WJ4 C4  H5   sing N N 403 
WJ4 C4  H4   sing N N 404 
WJ4 C5  H6   sing N N 405 
WJ4 C5  H7   sing N N 406 
WJ4 C6  H8   sing N N 407 
WJ4 C6  H9   sing N N 408 
WJ4 C2  H1   sing N N 409 
WJ4 C2  H    sing N N 410 
WJ4 C3  H3   sing N N 411 
WJ4 C3  H2   sing N N 412 
# 
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                    7HGL 
_atom_sites.fract_transf_matrix[1][1]   0.023965 
_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]   0.023693 
_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]   0.006223 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
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  ? 1.639   4.364   2.585   1.00 68.07  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 2  ? 0.485   3.601   2.042   1.00 68.31  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 2  ? 0.977   2.427   1.197   1.00 68.63  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 2  ? 2.171   2.314   0.931   1.00 74.32  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 2  ? -0.455  4.514   1.243   1.00 79.46  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 2  ? -1.517  5.198   2.097   1.00 91.24  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 2  ? -3.076  4.329   2.387   1.00 94.27  ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 2  ? -3.664  5.220   3.836   1.00 97.39  ? 1   MET A CE  1 
ATOM   9    N  N   . PRO A 1 3  ? 0.085   1.465   0.846   1.00 73.10  ? 2   PRO A N   1 
ATOM   10   C  CA  . PRO A 1 3  ? 0.383   0.433   -0.160  1.00 71.62  ? 2   PRO A CA  1 
ATOM   11   C  C   . PRO A 1 3  ? 0.633   0.827   -1.622  1.00 60.93  ? 2   PRO A C   1 
ATOM   12   O  O   . PRO A 1 3  ? 0.017   1.747   -2.142  1.00 57.21  ? 2   PRO A O   1 
ATOM   13   C  CB  . PRO A 1 3  ? -0.858  -0.493  -0.017  1.00 74.26  ? 2   PRO A CB  1 
ATOM   14   C  CG  . PRO A 1 3  ? -1.329  -0.266  1.400   1.00 72.89  ? 2   PRO A CG  1 
ATOM   15   C  CD  . PRO A 1 3  ? -1.207  1.236   1.521   1.00 69.48  ? 2   PRO A CD  1 
ATOM   16   N  N   . HIS A 1 4  ? 1.548   0.104   -2.280  1.00 64.01  ? 3   HIS A N   1 
ATOM   17   C  CA  . HIS A 1 4  ? 1.741   0.161   -3.725  1.00 67.61  ? 3   HIS A CA  1 
ATOM   18   C  C   . HIS A 1 4  ? 1.301   -1.172  -4.336  1.00 62.43  ? 3   HIS A C   1 
ATOM   19   O  O   . HIS A 1 4  ? 0.955   -2.099  -3.610  1.00 56.98  ? 3   HIS A O   1 
ATOM   20   C  CB  . HIS A 1 4  ? 3.219   0.417   -4.056  1.00 74.61  ? 3   HIS A CB  1 
ATOM   21   C  CG  . HIS A 1 4  ? 3.820   1.647   -3.449  1.00 84.12  ? 3   HIS A CG  1 
ATOM   22   N  ND1 . HIS A 1 4  ? 4.476   1.636   -2.238  1.00 83.84  ? 3   HIS A ND1 1 
ATOM   23   C  CD2 . HIS A 1 4  ? 3.893   2.910   -3.897  1.00 84.04  ? 3   HIS A CD2 1 
ATOM   24   C  CE1 . HIS A 1 4  ? 4.922   2.860   -1.973  1.00 91.47  ? 3   HIS A CE1 1 
ATOM   25   N  NE2 . HIS A 1 4  ? 4.578   3.648   -2.968  1.00 87.96  ? 3   HIS A NE2 1 
ATOM   26   N  N   . ALA A 1 5  ? 1.356   -1.284  -5.671  1.00 55.34  ? 4   ALA A N   1 
ATOM   27   C  CA  . ALA A 1 5  ? 1.155   -2.552  -6.363  1.00 55.03  ? 4   ALA A CA  1 
ATOM   28   C  C   . ALA A 1 5  ? 2.214   -3.581  -5.959  1.00 52.51  ? 4   ALA A C   1 
ATOM   29   O  O   . ALA A 1 5  ? 3.230   -3.203  -5.373  1.00 47.20  ? 4   ALA A O   1 
ATOM   30   C  CB  . ALA A 1 5  ? 1.188   -2.310  -7.850  1.00 55.88  ? 4   ALA A CB  1 
ATOM   31   N  N   . PHE A 1 6  ? 2.001   -4.867  -6.318  1.00 45.48  ? 5   PHE A N   1 
ATOM   32   C  CA  . PHE A 1 6  ? 3.003   -5.879  -6.013  1.00 40.79  ? 5   PHE A CA  1 
ATOM   33   C  C   . PHE A 1 6  ? 4.203   -5.707  -6.940  1.00 37.03  ? 5   PHE A C   1 
ATOM   34   O  O   . PHE A 1 6  ? 4.023   -5.330  -8.091  1.00 45.46  ? 5   PHE A O   1 
ATOM   35   C  CB  . PHE A 1 6  ? 2.401   -7.282  -6.010  1.00 50.62  ? 5   PHE A CB  1 
ATOM   36   C  CG  . PHE A 1 6  ? 1.662   -7.677  -4.736  1.00 47.00  ? 5   PHE A CG  1 
ATOM   37   C  CD1 . PHE A 1 6  ? 2.363   -8.052  -3.591  1.00 46.98  ? 5   PHE A CD1 1 
ATOM   38   C  CD2 . PHE A 1 6  ? 0.265   -7.675  -4.692  1.00 49.27  ? 5   PHE A CD2 1 
ATOM   39   C  CE1 . PHE A 1 6  ? 1.694   -8.440  -2.435  1.00 44.69  ? 5   PHE A CE1 1 
ATOM   40   C  CE2 . PHE A 1 6  ? -0.405  -8.049  -3.533  1.00 48.57  ? 5   PHE A CE2 1 
ATOM   41   C  CZ  . PHE A 1 6  ? 0.303   -8.425  -2.404  1.00 48.08  ? 5   PHE A CZ  1 
ATOM   42   N  N   . LYS A 1 7  ? 5.423   -5.997  -6.446  1.00 37.08  ? 6   LYS A N   1 
ATOM   43   C  CA  . LYS A 1 7  ? 6.620   -5.836  -7.273  1.00 38.16  ? 6   LYS A CA  1 
ATOM   44   C  C   . LYS A 1 7  ? 7.575   -7.004  -7.016  1.00 38.35  ? 6   LYS A C   1 
ATOM   45   O  O   . LYS A 1 7  ? 7.535   -7.588  -5.957  1.00 33.83  ? 6   LYS A O   1 
ATOM   46   C  CB  . LYS A 1 7  ? 7.399   -4.530  -7.062  1.00 38.48  ? 6   LYS A CB  1 
ATOM   47   C  CG  . LYS A 1 7  ? 8.027   -4.417  -5.674  1.00 49.90  ? 6   LYS A CG  1 
ATOM   48   C  CD  . LYS A 1 7  ? 8.479   -3.029  -5.216  1.00 53.57  ? 6   LYS A CD  1 
ATOM   49   C  CE  . LYS A 1 7  ? 8.932   -2.995  -3.776  1.00 50.50  ? 6   LYS A CE  1 
ATOM   50   N  NZ  . LYS A 1 7  ? 7.772   -3.118  -2.889  1.00 50.98  ? 6   LYS A NZ  1 
ATOM   51   N  N   . PRO A 1 8  ? 8.422   -7.424  -7.987  1.00 40.14  ? 7   PRO A N   1 
ATOM   52   C  CA  . PRO A 1 8  ? 9.414   -8.479  -7.742  1.00 43.83  ? 7   PRO A CA  1 
ATOM   53   C  C   . PRO A 1 8  ? 10.049  -8.189  -6.382  1.00 36.52  ? 7   PRO A C   1 
ATOM   54   O  O   . PRO A 1 8  ? 10.372  -7.030  -6.166  1.00 40.17  ? 7   PRO A O   1 
ATOM   55   C  CB  . PRO A 1 8  ? 10.408  -8.109  -8.880  1.00 41.03  ? 7   PRO A CB  1 
ATOM   56   C  CG  . PRO A 1 8  ? 9.509   -7.774  -10.046 1.00 46.93  ? 7   PRO A CG  1 
ATOM   57   C  CD  . PRO A 1 8  ? 8.497   -6.863  -9.348  1.00 43.05  ? 7   PRO A CD  1 
ATOM   58   N  N   . GLY A 1 9  ? 10.286  -9.226  -5.545  1.00 32.35  ? 8   GLY A N   1 
ATOM   59   C  CA  . GLY A 1 9  ? 10.911  -9.159  -4.222  1.00 28.89  ? 8   GLY A CA  1 
ATOM   60   C  C   . GLY A 1 9  ? 9.911   -9.082  -3.051  1.00 32.24  ? 8   GLY A C   1 
ATOM   61   O  O   . GLY A 1 9  ? 10.133  -9.591  -1.961  1.00 26.70  ? 8   GLY A O   1 
ATOM   62   N  N   . ASP A 1 10 ? 8.681   -8.634  -3.321  1.00 32.80  ? 9   ASP A N   1 
ATOM   63   C  CA  . ASP A 1 10 ? 7.719   -8.643  -2.236  1.00 26.03  ? 9   ASP A CA  1 
ATOM   64   C  C   . ASP A 1 10 ? 7.641   -10.004 -1.585  1.00 21.01  ? 9   ASP A C   1 
ATOM   65   O  O   . ASP A 1 10 ? 7.519   -10.983 -2.302  1.00 35.23  ? 9   ASP A O   1 
ATOM   66   C  CB  . ASP A 1 10 ? 6.385   -8.097  -2.738  1.00 32.12  ? 9   ASP A CB  1 
ATOM   67   C  CG  . ASP A 1 10 ? 6.369   -6.582  -2.882  1.00 44.62  ? 9   ASP A CG  1 
ATOM   68   O  OD1 . ASP A 1 10 ? 7.419   -5.958  -2.636  1.00 38.09  ? 9   ASP A OD1 1 
ATOM   69   O  OD2 . ASP A 1 10 ? 5.318   -6.030  -3.254  1.00 38.64  ? 9   ASP A OD2 1 
ATOM   70   N  N   . LEU A 1 11 ? 7.520   -10.063 -0.235  1.00 29.48  ? 10  LEU A N   1 
ATOM   71   C  CA  . LEU A 1 11 ? 7.374   -11.356 0.429   1.00 29.07  ? 10  LEU A CA  1 
ATOM   72   C  C   . LEU A 1 11 ? 5.902   -11.477 0.792   1.00 37.19  ? 10  LEU A C   1 
ATOM   73   O  O   . LEU A 1 11 ? 5.282   -10.444 1.006   1.00 35.73  ? 10  LEU A O   1 
ATOM   74   C  CB  . LEU A 1 11 ? 8.319   -11.419 1.607   1.00 33.24  ? 10  LEU A CB  1 
ATOM   75   C  CG  . LEU A 1 11 ? 9.764   -11.271 1.126   1.00 27.57  ? 10  LEU A CG  1 
ATOM   76   C  CD1 . LEU A 1 11 ? 10.676  -11.341 2.318   1.00 28.85  ? 10  LEU A CD1 1 
ATOM   77   C  CD2 . LEU A 1 11 ? 9.985   -12.395 0.188   1.00 26.74  ? 10  LEU A CD2 1 
ATOM   78   N  N   . VAL A 1 12 ? 5.357   -12.691 0.721   1.00 37.68  ? 11  VAL A N   1 
ATOM   79   C  CA  . VAL A 1 12 ? 3.913   -12.878 0.864   1.00 40.62  ? 11  VAL A CA  1 
ATOM   80   C  C   . VAL A 1 12 ? 3.660   -14.276 1.402   1.00 40.29  ? 11  VAL A C   1 
ATOM   81   O  O   . VAL A 1 12 ? 4.584   -15.051 1.529   1.00 28.54  ? 11  VAL A O   1 
ATOM   82   C  CB  . VAL A 1 12 ? 3.029   -12.692 -0.382  1.00 35.61  ? 11  VAL A CB  1 
ATOM   83   C  CG1 . VAL A 1 12 ? 3.189   -11.334 -1.053  1.00 32.45  ? 11  VAL A CG1 1 
ATOM   84   C  CG2 . VAL A 1 12 ? 3.261   -13.788 -1.418  1.00 33.34  ? 11  VAL A CG2 1 
ATOM   85   N  N   . PHE A 1 13 ? 2.389   -14.550 1.718   1.00 31.33  ? 12  PHE A N   1 
ATOM   86   C  CA  . PHE A 1 13 ? 1.851   -15.886 1.806   1.00 39.40  ? 12  PHE A CA  1 
ATOM   87   C  C   . PHE A 1 13 ? 0.789   -15.926 0.727   1.00 41.62  ? 12  PHE A C   1 
ATOM   88   O  O   . PHE A 1 13 ? -0.042  -15.026 0.681   1.00 48.68  ? 12  PHE A O   1 
ATOM   89   C  CB  . PHE A 1 13 ? 1.101   -16.184 3.113   1.00 37.89  ? 12  PHE A CB  1 
ATOM   90   C  CG  . PHE A 1 13 ? 1.975   -16.261 4.353   1.00 36.67  ? 12  PHE A CG  1 
ATOM   91   C  CD1 . PHE A 1 13 ? 2.219   -15.124 5.130   1.00 39.51  ? 12  PHE A CD1 1 
ATOM   92   C  CD2 . PHE A 1 13 ? 2.543   -17.468 4.751   1.00 39.91  ? 12  PHE A CD2 1 
ATOM   93   C  CE1 . PHE A 1 13 ? 3.059   -15.179 6.238   1.00 41.12  ? 12  PHE A CE1 1 
ATOM   94   C  CE2 . PHE A 1 13 ? 3.360   -17.525 5.891   1.00 46.44  ? 12  PHE A CE2 1 
ATOM   95   C  CZ  . PHE A 1 13 ? 3.607   -16.389 6.639   1.00 39.99  ? 12  PHE A CZ  1 
ATOM   96   N  N   . ALA A 1 14 ? 0.889   -16.961 -0.117  1.00 42.75  ? 13  ALA A N   1 
ATOM   97   C  CA  . ALA A 1 14 ? 0.109   -17.147 -1.318  1.00 38.59  ? 13  ALA A CA  1 
ATOM   98   C  C   . ALA A 1 14 ? -0.885  -18.266 -1.054  1.00 38.79  ? 13  ALA A C   1 
ATOM   99   O  O   . ALA A 1 14 ? -0.501  -19.361 -0.729  1.00 34.31  ? 13  ALA A O   1 
ATOM   100  C  CB  . ALA A 1 14 ? 1.040   -17.479 -2.449  1.00 41.91  ? 13  ALA A CB  1 
ATOM   101  N  N   . LYS A 1 15 ? -2.183  -17.998 -1.145  1.00 40.71  ? 14  LYS A N   1 
ATOM   102  C  CA  . LYS A 1 15 ? -3.135  -19.080 -0.982  1.00 32.19  ? 14  LYS A CA  1 
ATOM   103  C  C   . LYS A 1 15 ? -3.462  -19.740 -2.338  1.00 40.51  ? 14  LYS A C   1 
ATOM   104  O  O   . LYS A 1 15 ? -3.768  -19.051 -3.313  1.00 40.14  ? 14  LYS A O   1 
ATOM   105  C  CB  . LYS A 1 15 ? -4.432  -18.388 -0.567  1.00 32.78  ? 14  LYS A CB  1 
ATOM   106  C  CG  . LYS A 1 15 ? -5.463  -19.364 -0.022  1.00 43.26  ? 14  LYS A CG  1 
ATOM   107  C  CD  . LYS A 1 15 ? -4.831  -20.456 0.840   1.00 39.33  ? 14  LYS A CD  1 
ATOM   108  C  CE  . LYS A 1 15 ? -5.891  -21.231 1.570   1.00 48.04  ? 14  LYS A CE  1 
ATOM   109  N  NZ  . LYS A 1 15 ? -6.850  -21.753 0.593   1.00 48.84  ? 14  LYS A NZ  1 
ATOM   110  N  N   . MET A 1 16 ? -3.445  -21.082 -2.373  1.00 37.29  ? 15  MET A N   1 
ATOM   111  C  CA  . MET A 1 16 ? -3.935  -21.875 -3.496  1.00 42.32  ? 15  MET A CA  1 
ATOM   112  C  C   . MET A 1 16 ? -5.007  -22.857 -3.009  1.00 47.47  ? 15  MET A C   1 
ATOM   113  O  O   . MET A 1 16 ? -4.967  -23.291 -1.859  1.00 42.71  ? 15  MET A O   1 
ATOM   114  C  CB  . MET A 1 16 ? -2.826  -22.722 -4.112  1.00 43.09  ? 15  MET A CB  1 
ATOM   115  C  CG  . MET A 1 16 ? -1.594  -21.943 -4.493  1.00 45.74  ? 15  MET A CG  1 
ATOM   116  S  SD  . MET A 1 16 ? -1.209  -22.077 -6.243  1.00 53.68  ? 15  MET A SD  1 
ATOM   117  C  CE  . MET A 1 16 ? -2.807  -21.680 -6.960  1.00 62.45  ? 15  MET A CE  1 
ATOM   118  N  N   . LYS A 1 17 ? -5.954  -23.192 -3.898  1.00 52.83  ? 16  LYS A N   1 
ATOM   119  C  CA  . LYS A 1 17 ? -7.055  -24.102 -3.605  1.00 58.14  ? 16  LYS A CA  1 
ATOM   120  C  C   . LYS A 1 17 ? -6.492  -25.384 -3.011  1.00 52.45  ? 16  LYS A C   1 
ATOM   121  O  O   . LYS A 1 17 ? -5.545  -25.944 -3.545  1.00 50.99  ? 16  LYS A O   1 
ATOM   122  C  CB  . LYS A 1 17 ? -7.862  -24.460 -4.859  1.00 63.15  ? 16  LYS A CB  1 
ATOM   123  C  CG  . LYS A 1 17 ? -9.237  -25.080 -4.612  1.00 70.34  ? 16  LYS A CG  1 
ATOM   124  C  CD  . LYS A 1 17 ? -10.308 -24.063 -4.230  1.00 69.56  ? 16  LYS A CD  1 
ATOM   125  N  N   . GLY A 1 18 ? -7.057  -25.795 -1.874  1.00 60.52  ? 17  GLY A N   1 
ATOM   126  C  CA  . GLY A 1 18 ? -6.676  -27.039 -1.234  1.00 61.30  ? 17  GLY A CA  1 
ATOM   127  C  C   . GLY A 1 18 ? -5.237  -26.991 -0.735  1.00 66.46  ? 17  GLY A C   1 
ATOM   128  O  O   . GLY A 1 18 ? -4.534  -27.999 -0.778  1.00 75.53  ? 17  GLY A O   1 
ATOM   129  N  N   . TYR A 1 19 ? -4.806  -25.819 -0.259  1.00 48.98  ? 18  TYR A N   1 
ATOM   130  C  CA  . TYR A 1 19 ? -3.542  -25.758 0.449   1.00 51.69  ? 18  TYR A CA  1 
ATOM   131  C  C   . TYR A 1 19 ? -3.635  -24.666 1.508   1.00 46.20  ? 18  TYR A C   1 
ATOM   132  O  O   . TYR A 1 19 ? -4.418  -23.736 1.363   1.00 49.19  ? 18  TYR A O   1 
ATOM   133  C  CB  . TYR A 1 19 ? -2.309  -25.440 -0.403  1.00 47.27  ? 18  TYR A CB  1 
ATOM   134  C  CG  . TYR A 1 19 ? -1.756  -26.401 -1.439  1.00 57.90  ? 18  TYR A CG  1 
ATOM   135  C  CD1 . TYR A 1 19 ? -0.596  -27.121 -1.180  1.00 67.33  ? 18  TYR A CD1 1 
ATOM   136  C  CD2 . TYR A 1 19 ? -2.307  -26.495 -2.716  1.00 63.43  ? 18  TYR A CD2 1 
ATOM   137  C  CE1 . TYR A 1 19 ? -0.035  -27.956 -2.133  1.00 73.12  ? 18  TYR A CE1 1 
ATOM   138  C  CE2 . TYR A 1 19 ? -1.750  -27.323 -3.682  1.00 68.29  ? 18  TYR A CE2 1 
ATOM   139  C  CZ  . TYR A 1 19 ? -0.614  -28.066 -3.388  1.00 76.35  ? 18  TYR A CZ  1 
ATOM   140  O  OH  . TYR A 1 19 ? -0.043  -28.915 -4.308  1.00 64.09  ? 18  TYR A OH  1 
ATOM   141  N  N   . PRO A 1 20 ? -2.791  -24.695 2.566   1.00 51.68  ? 19  PRO A N   1 
ATOM   142  C  CA  . PRO A 1 20 ? -2.684  -23.558 3.489   1.00 51.25  ? 19  PRO A CA  1 
ATOM   143  C  C   . PRO A 1 20 ? -1.902  -22.394 2.871   1.00 47.10  ? 19  PRO A C   1 
ATOM   144  O  O   . PRO A 1 20 ? -1.135  -22.599 1.943   1.00 49.05  ? 19  PRO A O   1 
ATOM   145  C  CB  . PRO A 1 20 ? -1.932  -24.202 4.637   1.00 52.18  ? 19  PRO A CB  1 
ATOM   146  C  CG  . PRO A 1 20 ? -0.975  -25.135 3.935   1.00 54.71  ? 19  PRO A CG  1 
ATOM   147  C  CD  . PRO A 1 20 ? -1.827  -25.770 2.857   1.00 53.18  ? 19  PRO A CD  1 
ATOM   148  N  N   . HIS A 1 21 ? -2.105  -21.181 3.394   1.00 47.06  ? 20  HIS A N   1 
ATOM   149  C  CA  . HIS A 1 21 ? -1.357  -20.001 2.990   1.00 47.61  ? 20  HIS A CA  1 
ATOM   150  C  C   . HIS A 1 21 ? 0.134   -20.322 3.044   1.00 43.77  ? 20  HIS A C   1 
ATOM   151  O  O   . HIS A 1 21 ? 0.564   -20.736 4.088   1.00 39.51  ? 20  HIS A O   1 
ATOM   152  C  CB  . HIS A 1 21 ? -1.724  -18.841 3.921   1.00 36.42  ? 20  HIS A CB  1 
ATOM   153  C  CG  . HIS A 1 21 ? -3.158  -18.469 3.742   1.00 38.94  ? 20  HIS A CG  1 
ATOM   154  N  ND1 . HIS A 1 21 ? -4.202  -19.203 4.265   1.00 39.64  ? 20  HIS A ND1 1 
ATOM   155  C  CD2 . HIS A 1 21 ? -3.713  -17.479 3.053   1.00 41.07  ? 20  HIS A CD2 1 
ATOM   156  C  CE1 . HIS A 1 21 ? -5.346  -18.632 3.938   1.00 40.39  ? 20  HIS A CE1 1 
ATOM   157  N  NE2 . HIS A 1 21 ? -5.073  -17.575 3.206   1.00 43.14  ? 20  HIS A NE2 1 
ATOM   158  N  N   . TRP A 1 22 ? 0.892   -20.149 1.944   1.00 37.63  ? 21  TRP A N   1 
ATOM   159  C  CA  . TRP A 1 22 ? 2.219   -20.755 1.832   1.00 38.37  ? 21  TRP A CA  1 
ATOM   160  C  C   . TRP A 1 22 ? 3.254   -19.639 1.711   1.00 34.02  ? 21  TRP A C   1 
ATOM   161  O  O   . TRP A 1 22 ? 3.121   -18.778 0.850   1.00 37.39  ? 21  TRP A O   1 
ATOM   162  C  CB  . TRP A 1 22 ? 2.318   -21.666 0.580   1.00 31.11  ? 21  TRP A CB  1 
ATOM   163  C  CG  . TRP A 1 22 ? 3.536   -22.578 0.529   1.00 27.40  ? 21  TRP A CG  1 
ATOM   164  C  CD1 . TRP A 1 22 ? 4.870   -22.329 0.266   1.00 30.43  ? 21  TRP A CD1 1 
ATOM   165  C  CD2 . TRP A 1 22 ? 3.447   -23.979 0.837   1.00 30.07  ? 21  TRP A CD2 1 
ATOM   166  N  NE1 . TRP A 1 22 ? 5.624   -23.487 0.366   1.00 19.14  ? 21  TRP A NE1 1 
ATOM   167  C  CE2 . TRP A 1 22 ? 4.758   -24.513 0.766   1.00 33.08  ? 21  TRP A CE2 1 
ATOM   168  C  CE3 . TRP A 1 22 ? 2.366   -24.794 1.218   1.00 38.43  ? 21  TRP A CE3 1 
ATOM   169  C  CZ2 . TRP A 1 22 ? 4.971   -25.872 1.031   1.00 38.77  ? 21  TRP A CZ2 1 
ATOM   170  C  CZ3 . TRP A 1 22 ? 2.596   -26.132 1.472   1.00 42.74  ? 21  TRP A CZ3 1 
ATOM   171  C  CH2 . TRP A 1 22 ? 3.891   -26.659 1.383   1.00 40.32  ? 21  TRP A CH2 1 
ATOM   172  N  N   . PRO A 1 23 ? 4.391   -19.734 2.435   1.00 32.54  ? 22  PRO A N   1 
ATOM   173  C  CA  . PRO A 1 23 ? 5.524   -18.833 2.242   1.00 35.18  ? 22  PRO A CA  1 
ATOM   174  C  C   . PRO A 1 23 ? 5.880   -18.752 0.767   1.00 28.56  ? 22  PRO A C   1 
ATOM   175  O  O   . PRO A 1 23 ? 6.234   -19.780 0.193   1.00 41.48  ? 22  PRO A O   1 
ATOM   176  C  CB  . PRO A 1 23 ? 6.710   -19.469 3.021   1.00 36.48  ? 22  PRO A CB  1 
ATOM   177  C  CG  . PRO A 1 23 ? 6.230   -20.799 3.503   1.00 33.60  ? 22  PRO A CG  1 
ATOM   178  C  CD  . PRO A 1 23 ? 4.672   -20.775 3.438   1.00 33.73  ? 22  PRO A CD  1 
ATOM   179  N  N   . ALA A 1 24 ? 5.998   -17.514 0.252   1.00 27.73  ? 23  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 24 ? 6.152   -17.215 -1.170  1.00 34.01  ? 23  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 24 ? 6.745   -15.826 -1.448  1.00 27.53  ? 23  ALA A C   1 
ATOM   182  O  O   . ALA A 1 24 ? 6.720   -14.915 -0.614  1.00 28.35  ? 23  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 24 ? 4.810   -17.414 -1.874  1.00 39.71  ? 23  ALA A CB  1 
ATOM   184  N  N   . ARG A 1 25 ? 7.238   -15.651 -2.675  1.00 29.58  ? 24  ARG A N   1 
ATOM   185  C  CA  . ARG A 1 25 ? 7.760   -14.382 -3.141  1.00 28.41  ? 24  ARG A CA  1 
ATOM   186  C  C   . ARG A 1 25 ? 7.242   -14.144 -4.551  1.00 33.19  ? 24  ARG A C   1 
ATOM   187  O  O   . ARG A 1 25 ? 6.987   -15.106 -5.301  1.00 35.51  ? 24  ARG A O   1 
ATOM   188  C  CB  . ARG A 1 25 ? 9.289   -14.500 -3.021  1.00 27.67  ? 24  ARG A CB  1 
ATOM   189  C  CG  . ARG A 1 25 ? 10.097  -14.930 -4.223  1.00 39.55  ? 24  ARG A CG  1 
ATOM   190  C  CD  . ARG A 1 25 ? 11.547  -14.975 -3.686  1.00 32.49  ? 24  ARG A CD  1 
ATOM   191  N  NE  . ARG A 1 25 ? 12.230  -15.749 -4.727  1.00 38.33  ? 24  ARG A NE  1 
ATOM   192  C  CZ  . ARG A 1 25 ? 13.513  -16.154 -4.820  1.00 44.66  ? 24  ARG A CZ  1 
ATOM   193  N  NH1 . ARG A 1 25 ? 14.393  -15.872 -3.895  1.00 36.03  ? 24  ARG A NH1 1 
ATOM   194  N  NH2 . ARG A 1 25 ? 13.912  -16.849 -5.875  1.00 40.77  ? 24  ARG A NH2 1 
ATOM   195  N  N   . ILE A 1 26 ? 7.078   -12.856 -4.883  1.00 29.82  ? 25  ILE A N   1 
ATOM   196  C  CA  . ILE A 1 26 ? 6.931   -12.361 -6.240  1.00 26.22  ? 25  ILE A CA  1 
ATOM   197  C  C   . ILE A 1 26 ? 8.295   -12.469 -6.891  1.00 37.05  ? 25  ILE A C   1 
ATOM   198  O  O   . ILE A 1 26 ? 9.225   -11.830 -6.369  1.00 23.71  ? 25  ILE A O   1 
ATOM   199  C  CB  . ILE A 1 26 ? 6.502   -10.880 -6.278  1.00 31.17  ? 25  ILE A CB  1 
ATOM   200  C  CG1 . ILE A 1 26 ? 5.530   -10.447 -5.193  1.00 30.61  ? 25  ILE A CG1 1 
ATOM   201  C  CG2 . ILE A 1 26 ? 6.003   -10.502 -7.685  1.00 29.84  ? 25  ILE A CG2 1 
ATOM   202  C  CD1 . ILE A 1 26 ? 4.055   -10.655 -5.519  1.00 29.00  ? 25  ILE A CD1 1 
ATOM   203  N  N   . ASP A 1 27 ? 8.315   -13.152 -8.056  1.00 40.34  ? 26  ASP A N   1 
ATOM   204  C  CA  . ASP A 1 27 ? 9.503   -13.333 -8.885  1.00 37.62  ? 26  ASP A CA  1 
ATOM   205  C  C   . ASP A 1 27 ? 9.579   -12.233 -9.938  1.00 40.03  ? 26  ASP A C   1 
ATOM   206  O  O   . ASP A 1 27 ? 8.581   -11.575 -10.221 1.00 35.71  ? 26  ASP A O   1 
ATOM   207  C  CB  . ASP A 1 27 ? 9.602   -14.765 -9.392  1.00 39.73  ? 26  ASP A CB  1 
ATOM   208  C  CG  . ASP A 1 27 ? 10.529  -15.660 -8.580  1.00 39.73  ? 26  ASP A CG  1 
ATOM   209  O  OD1 . ASP A 1 27 ? 11.104  -15.152 -7.599  1.00 41.89  ? 26  ASP A OD1 1 
ATOM   210  O  OD2 . ASP A 1 27 ? 10.651  -16.836 -8.928  1.00 44.78  ? 26  ASP A OD2 1 
ATOM   211  N  N   . ASP A 1 28 ? 10.798  -11.950 -10.433 1.00 35.92  ? 27  ASP A N   1 
ATOM   212  C  CA  . ASP A 1 28 ? 10.941  -11.303 -11.733 1.00 47.58  ? 27  ASP A CA  1 
ATOM   213  C  C   . ASP A 1 28 ? 10.691  -12.297 -12.877 1.00 42.26  ? 27  ASP A C   1 
ATOM   214  O  O   . ASP A 1 28 ? 10.667  -13.523 -12.708 1.00 45.17  ? 27  ASP A O   1 
ATOM   215  C  CB  . ASP A 1 28 ? 12.365  -10.836 -11.997 1.00 55.39  ? 27  ASP A CB  1 
ATOM   216  C  CG  . ASP A 1 28 ? 12.822  -9.592  -11.256 1.00 61.11  ? 27  ASP A CG  1 
ATOM   217  O  OD1 . ASP A 1 28 ? 12.415  -8.482  -11.669 1.00 57.38  ? 27  ASP A OD1 1 
ATOM   218  O  OD2 . ASP A 1 28 ? 13.583  -9.757  -10.278 1.00 66.41  ? 27  ASP A OD2 1 
ATOM   219  N  N   . ILE A 1 29 ? 10.494  -11.741 -14.067 1.00 43.33  ? 28  ILE A N   1 
ATOM   220  C  CA  . ILE A 1 29 ? 10.502  -12.534 -15.282 1.00 44.35  ? 28  ILE A CA  1 
ATOM   221  C  C   . ILE A 1 29 ? 11.865  -12.365 -15.942 1.00 47.76  ? 28  ILE A C   1 
ATOM   222  O  O   . ILE A 1 29 ? 12.313  -11.242 -16.158 1.00 41.49  ? 28  ILE A O   1 
ATOM   223  C  CB  . ILE A 1 29 ? 9.331   -12.163 -16.206 1.00 41.57  ? 28  ILE A CB  1 
ATOM   224  C  CG1 . ILE A 1 29 ? 7.981   -12.311 -15.444 1.00 39.13  ? 28  ILE A CG1 1 
ATOM   225  C  CG2 . ILE A 1 29 ? 9.384   -13.064 -17.447 1.00 44.00  ? 28  ILE A CG2 1 
ATOM   226  C  CD1 . ILE A 1 29 ? 6.831   -11.539 -16.061 1.00 43.12  ? 28  ILE A CD1 1 
ATOM   227  N  N   . ALA A 1 30 ? 12.534  -13.500 -16.185 1.00 53.95  ? 29  ALA A N   1 
ATOM   228  C  CA  . ALA A 1 30 ? 13.833  -13.498 -16.843 1.00 48.55  ? 29  ALA A CA  1 
ATOM   229  C  C   . ALA A 1 30 ? 13.647  -13.226 -18.329 1.00 46.63  ? 29  ALA A C   1 
ATOM   230  O  O   . ALA A 1 30 ? 12.555  -13.426 -18.889 1.00 47.41  ? 29  ALA A O   1 
ATOM   231  C  CB  . ALA A 1 30 ? 14.595  -14.779 -16.589 1.00 50.07  ? 29  ALA A CB  1 
ATOM   232  N  N   . ASP A 1 31 ? 14.712  -12.697 -18.934 1.00 36.56  ? 30  ASP A N   1 
ATOM   233  C  CA  . ASP A 1 31 ? 14.735  -12.504 -20.374 1.00 43.97  ? 30  ASP A CA  1 
ATOM   234  C  C   . ASP A 1 31 ? 14.589  -13.863 -21.033 1.00 41.15  ? 30  ASP A C   1 
ATOM   235  O  O   . ASP A 1 31 ? 15.294  -14.806 -20.670 1.00 39.88  ? 30  ASP A O   1 
ATOM   236  C  CB  . ASP A 1 31 ? 16.033  -11.868 -20.843 1.00 42.56  ? 30  ASP A CB  1 
ATOM   237  C  CG  . ASP A 1 31 ? 16.091  -10.366 -20.648 1.00 48.36  ? 30  ASP A CG  1 
ATOM   238  O  OD1 . ASP A 1 31 ? 15.009  -9.783  -20.416 1.00 46.98  ? 30  ASP A OD1 1 
ATOM   239  O  OD2 . ASP A 1 31 ? 17.214  -9.814  -20.692 1.00 47.35  ? 30  ASP A OD2 1 
ATOM   240  N  N   . GLY A 1 32 ? 13.666  -13.918 -21.993 1.00 46.11  ? 31  GLY A N   1 
ATOM   241  C  CA  . GLY A 1 32 ? 13.365  -15.124 -22.747 1.00 39.16  ? 31  GLY A CA  1 
ATOM   242  C  C   . GLY A 1 32 ? 12.301  -16.009 -22.092 1.00 38.33  ? 31  GLY A C   1 
ATOM   243  O  O   . GLY A 1 32 ? 11.866  -16.948 -22.743 1.00 44.30  ? 31  GLY A O   1 
ATOM   244  N  N   . ALA A 1 33 ? 11.930  -15.741 -20.813 1.00 37.73  ? 32  ALA A N   1 
ATOM   245  C  CA  . ALA A 1 33 ? 11.126  -16.672 -20.033 1.00 41.16  ? 32  ALA A CA  1 
ATOM   246  C  C   . ALA A 1 33 ? 9.638   -16.309 -20.150 1.00 36.44  ? 32  ALA A C   1 
ATOM   247  O  O   . ALA A 1 33 ? 9.297   -15.176 -20.458 1.00 39.93  ? 32  ALA A O   1 
ATOM   248  C  CB  . ALA A 1 33 ? 11.611  -16.710 -18.592 1.00 47.60  ? 32  ALA A CB  1 
ATOM   249  N  N   . VAL A 1 34 ? 8.766   -17.294 -19.935 1.00 46.42  ? 33  VAL A N   1 
ATOM   250  C  CA  . VAL A 1 34 ? 7.313   -17.189 -20.103 1.00 48.08  ? 33  VAL A CA  1 
ATOM   251  C  C   . VAL A 1 34 ? 6.705   -16.057 -19.268 1.00 46.60  ? 33  VAL A C   1 
ATOM   252  O  O   . VAL A 1 34 ? 6.864   -15.969 -18.048 1.00 46.64  ? 33  VAL A O   1 
ATOM   253  C  CB  . VAL A 1 34 ? 6.674   -18.557 -19.764 1.00 56.50  ? 33  VAL A CB  1 
ATOM   254  C  CG1 . VAL A 1 34 ? 5.150   -18.528 -19.839 1.00 59.86  ? 33  VAL A CG1 1 
ATOM   255  C  CG2 . VAL A 1 34 ? 7.228   -19.686 -20.628 1.00 56.59  ? 33  VAL A CG2 1 
ATOM   256  N  N   . LYS A 1 35 ? 5.939   -15.194 -19.926 1.00 55.02  ? 34  LYS A N   1 
ATOM   257  C  CA  . LYS A 1 35 ? 5.222   -14.170 -19.178 1.00 54.59  ? 34  LYS A CA  1 
ATOM   258  C  C   . LYS A 1 35 ? 4.068   -14.813 -18.410 1.00 54.87  ? 34  LYS A C   1 
ATOM   259  O  O   . LYS A 1 35 ? 3.672   -15.943 -18.713 1.00 48.25  ? 34  LYS A O   1 
ATOM   260  C  CB  . LYS A 1 35 ? 4.822   -12.985 -20.060 1.00 52.99  ? 34  LYS A CB  1 
ATOM   261  C  CG  . LYS A 1 35 ? 5.996   -12.058 -20.398 1.00 52.03  ? 34  LYS A CG  1 
ATOM   262  C  CD  . LYS A 1 35 ? 5.682   -10.928 -21.372 1.00 52.27  ? 34  LYS A CD  1 
ATOM   263  C  CE  . LYS A 1 35 ? 5.560   -11.411 -22.780 1.00 46.77  ? 34  LYS A CE  1 
ATOM   264  N  NZ  . LYS A 1 35 ? 4.907   -10.426 -23.644 1.00 50.37  ? 34  LYS A NZ  1 
ATOM   265  N  N   . PRO A 1 36 ? 3.528   -14.130 -17.374 1.00 52.72  ? 35  PRO A N   1 
ATOM   266  C  CA  . PRO A 1 36 ? 2.377   -14.641 -16.630 1.00 50.69  ? 35  PRO A CA  1 
ATOM   267  C  C   . PRO A 1 36 ? 1.165   -14.130 -17.390 1.00 47.62  ? 35  PRO A C   1 
ATOM   268  O  O   . PRO A 1 36 ? 1.264   -13.104 -18.060 1.00 41.42  ? 35  PRO A O   1 
ATOM   269  C  CB  . PRO A 1 36 ? 2.520   -13.931 -15.272 1.00 55.95  ? 35  PRO A CB  1 
ATOM   270  C  CG  . PRO A 1 36 ? 3.161   -12.595 -15.607 1.00 55.68  ? 35  PRO A CG  1 
ATOM   271  C  CD  . PRO A 1 36 ? 3.995   -12.833 -16.859 1.00 59.07  ? 35  PRO A CD  1 
ATOM   272  N  N   . PRO A 1 37 ? -0.021  -14.775 -17.265 1.00 41.51  ? 36  PRO A N   1 
ATOM   273  C  CA  . PRO A 1 37 ? -1.229  -14.216 -17.859 1.00 46.45  ? 36  PRO A CA  1 
ATOM   274  C  C   . PRO A 1 37 ? -1.310  -12.763 -17.416 1.00 45.97  ? 36  PRO A C   1 
ATOM   275  O  O   . PRO A 1 37 ? -0.675  -12.376 -16.428 1.00 48.74  ? 36  PRO A O   1 
ATOM   276  C  CB  . PRO A 1 37 ? -2.414  -15.061 -17.336 1.00 38.89  ? 36  PRO A CB  1 
ATOM   277  C  CG  . PRO A 1 37 ? -1.788  -16.240 -16.615 1.00 44.03  ? 36  PRO A CG  1 
ATOM   278  C  CD  . PRO A 1 37 ? -0.271  -16.030 -16.547 1.00 42.72  ? 36  PRO A CD  1 
ATOM   279  N  N   . PRO A 1 38 ? -2.177  -11.948 -18.062 1.00 52.79  ? 37  PRO A N   1 
ATOM   280  C  CA  . PRO A 1 38 ? -2.388  -10.561 -17.633 1.00 54.58  ? 37  PRO A CA  1 
ATOM   281  C  C   . PRO A 1 38 ? -3.020  -10.531 -16.243 1.00 48.72  ? 37  PRO A C   1 
ATOM   282  O  O   . PRO A 1 38 ? -3.902  -11.336 -15.956 1.00 46.84  ? 37  PRO A O   1 
ATOM   283  C  CB  . PRO A 1 38 ? -3.314  -9.930  -18.709 1.00 58.13  ? 37  PRO A CB  1 
ATOM   284  C  CG  . PRO A 1 38 ? -3.850  -11.103 -19.518 1.00 58.69  ? 37  PRO A CG  1 
ATOM   285  C  CD  . PRO A 1 38 ? -3.030  -12.345 -19.197 1.00 51.09  ? 37  PRO A CD  1 
ATOM   286  N  N   . ASN A 1 39 ? -2.546  -9.615  -15.383 1.00 51.71  ? 38  ASN A N   1 
ATOM   287  C  CA  . ASN A 1 39 ? -3.124  -9.395  -14.067 1.00 43.76  ? 38  ASN A CA  1 
ATOM   288  C  C   . ASN A 1 39 ? -2.673  -10.479 -13.097 1.00 44.17  ? 38  ASN A C   1 
ATOM   289  O  O   . ASN A 1 39 ? -3.099  -10.478 -11.945 1.00 46.23  ? 38  ASN A O   1 
ATOM   290  C  CB  . ASN A 1 39 ? -4.654  -9.397  -14.106 1.00 50.99  ? 38  ASN A CB  1 
ATOM   291  C  CG  . ASN A 1 39 ? -5.172  -8.154  -14.784 1.00 53.05  ? 38  ASN A CG  1 
ATOM   292  O  OD1 . ASN A 1 39 ? -4.364  -7.316  -15.200 1.00 53.53  ? 38  ASN A OD1 1 
ATOM   293  N  ND2 . ASN A 1 39 ? -6.485  -8.001  -14.886 1.00 46.55  ? 38  ASN A ND2 1 
ATOM   294  N  N   . LYS A 1 40 ? -1.877  -11.440 -13.571 1.00 34.81  ? 39  LYS A N   1 
ATOM   295  C  CA  . LYS A 1 40 ? -1.272  -12.428 -12.696 1.00 39.95  ? 39  LYS A CA  1 
ATOM   296  C  C   . LYS A 1 40 ? 0.218   -12.108 -12.561 1.00 36.94  ? 39  LYS A C   1 
ATOM   297  O  O   . LYS A 1 40 ? 0.771   -11.344 -13.351 1.00 37.14  ? 39  LYS A O   1 
ATOM   298  C  CB  . LYS A 1 40 ? -1.467  -13.883 -13.136 1.00 42.48  ? 39  LYS A CB  1 
ATOM   299  C  CG  . LYS A 1 40 ? -2.912  -14.319 -13.386 1.00 45.12  ? 39  LYS A CG  1 
ATOM   300  C  CD  . LYS A 1 40 ? -3.804  -13.946 -12.222 1.00 35.38  ? 39  LYS A CD  1 
ATOM   301  C  CE  . LYS A 1 40 ? -5.194  -13.525 -12.636 1.00 42.20  ? 39  LYS A CE  1 
ATOM   302  N  NZ  . LYS A 1 40 ? -6.162  -14.558 -12.311 1.00 43.48  ? 39  LYS A NZ  1 
ATOM   303  N  N   . TYR A 1 41 ? 0.798   -12.639 -11.486 1.00 35.36  ? 40  TYR A N   1 
ATOM   304  C  CA  . TYR A 1 41 ? 2.214   -12.459 -11.182 1.00 31.64  ? 40  TYR A CA  1 
ATOM   305  C  C   . TYR A 1 41 ? 2.816   -13.837 -11.049 1.00 35.69  ? 40  TYR A C   1 
ATOM   306  O  O   . TYR A 1 41 ? 2.114   -14.810 -10.750 1.00 36.29  ? 40  TYR A O   1 
ATOM   307  C  CB  . TYR A 1 41 ? 2.260   -11.863 -9.769  1.00 30.76  ? 40  TYR A CB  1 
ATOM   308  C  CG  . TYR A 1 41 ? 1.819   -10.402 -9.680  1.00 32.46  ? 40  TYR A CG  1 
ATOM   309  C  CD1 . TYR A 1 41 ? 0.454   -10.083 -9.623  1.00 41.26  ? 40  TYR A CD1 1 
ATOM   310  C  CD2 . TYR A 1 41 ? 2.732   -9.342  -9.672  1.00 38.36  ? 40  TYR A CD2 1 
ATOM   311  C  CE1 . TYR A 1 41 ? 0.027   -8.761  -9.543  1.00 42.53  ? 40  TYR A CE1 1 
ATOM   312  C  CE2 . TYR A 1 41 ? 2.317   -8.010  -9.587  1.00 42.52  ? 40  TYR A CE2 1 
ATOM   313  C  CZ  . TYR A 1 41 ? 0.955   -7.731  -9.505  1.00 46.69  ? 40  TYR A CZ  1 
ATOM   314  O  OH  . TYR A 1 41 ? 0.445   -6.471  -9.424  1.00 51.03  ? 40  TYR A OH  1 
ATOM   315  N  N   . PRO A 1 42 ? 4.163   -13.931 -11.171 1.00 29.30  ? 41  PRO A N   1 
ATOM   316  C  CA  . PRO A 1 42 ? 4.877   -15.185 -10.947 1.00 35.50  ? 41  PRO A CA  1 
ATOM   317  C  C   . PRO A 1 42 ? 5.173   -15.308 -9.465  1.00 37.35  ? 41  PRO A C   1 
ATOM   318  O  O   . PRO A 1 42 ? 5.785   -14.386 -8.907  1.00 38.86  ? 41  PRO A O   1 
ATOM   319  C  CB  . PRO A 1 42 ? 6.184   -14.943 -11.731 1.00 31.62  ? 41  PRO A CB  1 
ATOM   320  C  CG  . PRO A 1 42 ? 6.394   -13.463 -11.554 1.00 30.39  ? 41  PRO A CG  1 
ATOM   321  C  CD  . PRO A 1 42 ? 5.013   -12.802 -11.524 1.00 36.92  ? 41  PRO A CD  1 
ATOM   322  N  N   . ILE A 1 43 ? 4.725   -16.427 -8.861  1.00 32.17  ? 42  ILE A N   1 
ATOM   323  C  CA  . ILE A 1 43 ? 4.809   -16.672 -7.425  1.00 33.08  ? 42  ILE A CA  1 
ATOM   324  C  C   . ILE A 1 43 ? 5.730   -17.861 -7.169  1.00 43.17  ? 42  ILE A C   1 
ATOM   325  O  O   . ILE A 1 43 ? 5.468   -18.980 -7.631  1.00 45.43  ? 42  ILE A O   1 
ATOM   326  C  CB  . ILE A 1 43 ? 3.414   -16.910 -6.812  1.00 36.54  ? 42  ILE A CB  1 
ATOM   327  C  CG1 . ILE A 1 43 ? 2.433   -15.777 -7.181  1.00 31.09  ? 42  ILE A CG1 1 
ATOM   328  C  CG2 . ILE A 1 43 ? 3.537   -17.112 -5.310  1.00 34.86  ? 42  ILE A CG2 1 
ATOM   329  C  CD1 . ILE A 1 43 ? 2.866   -14.370 -6.762  1.00 29.82  ? 42  ILE A CD1 1 
ATOM   330  N  N   . PHE A 1 44 ? 6.812   -17.608 -6.437  1.00 30.65  ? 43  PHE A N   1 
ATOM   331  C  CA  . PHE A 1 44 ? 7.775   -18.654 -6.188  1.00 37.35  ? 43  PHE A CA  1 
ATOM   332  C  C   . PHE A 1 44 ? 7.504   -19.188 -4.789  1.00 34.11  ? 43  PHE A C   1 
ATOM   333  O  O   . PHE A 1 44 ? 7.575   -18.415 -3.841  1.00 38.87  ? 43  PHE A O   1 
ATOM   334  C  CB  . PHE A 1 44 ? 9.183   -18.070 -6.399  1.00 27.54  ? 43  PHE A CB  1 
ATOM   335  C  CG  . PHE A 1 44 ? 10.208  -19.098 -5.931  1.00 37.81  ? 43  PHE A CG  1 
ATOM   336  C  CD1 . PHE A 1 44 ? 10.708  -20.072 -6.810  1.00 43.40  ? 43  PHE A CD1 1 
ATOM   337  C  CD2 . PHE A 1 44 ? 10.594  -19.158 -4.588  1.00 36.24  ? 43  PHE A CD2 1 
ATOM   338  C  CE1 . PHE A 1 44 ? 11.624  -21.026 -6.364  1.00 44.08  ? 43  PHE A CE1 1 
ATOM   339  C  CE2 . PHE A 1 44 ? 11.565  -20.062 -4.164  1.00 38.55  ? 43  PHE A CE2 1 
ATOM   340  C  CZ  . PHE A 1 44 ? 12.057  -21.023 -5.041  1.00 43.71  ? 43  PHE A CZ  1 
ATOM   341  N  N   . PHE A 1 45 ? 7.120   -20.467 -4.673  1.00 36.96  ? 44  PHE A N   1 
ATOM   342  C  CA  . PHE A 1 45 ? 6.754   -20.972 -3.354  1.00 33.61  ? 44  PHE A CA  1 
ATOM   343  C  C   . PHE A 1 45 ? 8.000   -21.458 -2.632  1.00 39.21  ? 44  PHE A C   1 
ATOM   344  O  O   . PHE A 1 45 ? 8.745   -22.251 -3.185  1.00 38.45  ? 44  PHE A O   1 
ATOM   345  C  CB  . PHE A 1 45 ? 5.695   -22.064 -3.305  1.00 36.90  ? 44  PHE A CB  1 
ATOM   346  C  CG  . PHE A 1 45 ? 4.361   -21.527 -3.805  1.00 33.32  ? 44  PHE A CG  1 
ATOM   347  C  CD1 . PHE A 1 45 ? 4.217   -21.166 -5.134  1.00 36.89  ? 44  PHE A CD1 1 
ATOM   348  C  CD2 . PHE A 1 45 ? 3.268   -21.369 -2.955  1.00 39.13  ? 44  PHE A CD2 1 
ATOM   349  C  CE1 . PHE A 1 45 ? 2.988   -20.698 -5.612  1.00 43.69  ? 44  PHE A CE1 1 
ATOM   350  C  CE2 . PHE A 1 45 ? 2.061   -20.850 -3.429  1.00 32.91  ? 44  PHE A CE2 1 
ATOM   351  C  CZ  . PHE A 1 45 ? 1.923   -20.536 -4.760  1.00 32.70  ? 44  PHE A CZ  1 
ATOM   352  N  N   . PHE A 1 46 ? 8.174   -20.969 -1.397  1.00 36.47  ? 45  PHE A N   1 
ATOM   353  C  CA  . PHE A 1 46 ? 9.243   -21.393 -0.513  1.00 33.05  ? 45  PHE A CA  1 
ATOM   354  C  C   . PHE A 1 46 ? 9.014   -22.829 -0.046  1.00 37.32  ? 45  PHE A C   1 
ATOM   355  O  O   . PHE A 1 46 ? 7.894   -23.357 0.221   1.00 17.84  ? 45  PHE A O   1 
ATOM   356  C  CB  . PHE A 1 46 ? 9.461   -20.415 0.653   1.00 34.97  ? 45  PHE A CB  1 
ATOM   357  C  CG  . PHE A 1 46 ? 9.960   -19.016 0.313   1.00 33.63  ? 45  PHE A CG  1 
ATOM   358  C  CD1 . PHE A 1 46 ? 11.311  -18.776 0.021   1.00 31.92  ? 45  PHE A CD1 1 
ATOM   359  C  CD2 . PHE A 1 46 ? 9.096   -17.942 0.364   1.00 31.45  ? 45  PHE A CD2 1 
ATOM   360  C  CE1 . PHE A 1 46 ? 11.749  -17.507 -0.293  1.00 39.49  ? 45  PHE A CE1 1 
ATOM   361  C  CE2 . PHE A 1 46 ? 9.545   -16.664 0.049   1.00 44.32  ? 45  PHE A CE2 1 
ATOM   362  C  CZ  . PHE A 1 46 ? 10.874  -16.445 -0.268  1.00 39.94  ? 45  PHE A CZ  1 
ATOM   363  N  N   . GLY A 1 47 ? 10.147  -23.490 0.122   1.00 20.54  ? 46  GLY A N   1 
ATOM   364  C  CA  . GLY A 1 47 ? 10.123  -24.882 0.524   1.00 33.58  ? 46  GLY A CA  1 
ATOM   365  C  C   . GLY A 1 47 ? 10.060  -25.804 -0.697  1.00 40.26  ? 46  GLY A C   1 
ATOM   366  O  O   . GLY A 1 47 ? 11.072  -26.363 -1.087  1.00 45.38  ? 46  GLY A O   1 
ATOM   367  N  N   . THR A 1 48 ? 8.870   -25.921 -1.305  1.00 41.27  ? 47  THR A N   1 
ATOM   368  C  CA  . THR A 1 48 ? 8.646   -26.767 -2.472  1.00 45.25  ? 47  THR A CA  1 
ATOM   369  C  C   . THR A 1 48 ? 9.430   -26.256 -3.676  1.00 49.24  ? 47  THR A C   1 
ATOM   370  O  O   . THR A 1 48 ? 9.765   -27.036 -4.570  1.00 52.11  ? 47  THR A O   1 
ATOM   371  C  CB  . THR A 1 48 ? 7.146   -26.815 -2.799  1.00 47.51  ? 47  THR A CB  1 
ATOM   372  O  OG1 . THR A 1 48 ? 6.733   -25.569 -3.365  1.00 46.85  ? 47  THR A OG1 1 
ATOM   373  C  CG2 . THR A 1 48 ? 6.293   -27.109 -1.587  1.00 37.08  ? 47  THR A CG2 1 
ATOM   374  N  N   . HIS A 1 49 ? 9.638   -24.933 -3.750  1.00 41.52  ? 48  HIS A N   1 
ATOM   375  C  CA  . HIS A 1 49 ? 10.321  -24.325 -4.881  1.00 42.41  ? 48  HIS A CA  1 
ATOM   376  C  C   . HIS A 1 49 ? 9.491   -24.349 -6.166  1.00 42.39  ? 48  HIS A C   1 
ATOM   377  O  O   . HIS A 1 49 ? 10.012  -24.129 -7.256  1.00 44.07  ? 48  HIS A O   1 
ATOM   378  C  CB  . HIS A 1 49 ? 11.724  -24.918 -5.055  1.00 45.79  ? 48  HIS A CB  1 
ATOM   379  C  CG  . HIS A 1 49 ? 12.536  -24.831 -3.812  1.00 41.47  ? 48  HIS A CG  1 
ATOM   380  N  ND1 . HIS A 1 49 ? 13.714  -25.533 -3.666  1.00 47.18  ? 48  HIS A ND1 1 
ATOM   381  C  CD2 . HIS A 1 49 ? 12.414  -24.090 -2.702  1.00 44.56  ? 48  HIS A CD2 1 
ATOM   382  C  CE1 . HIS A 1 49 ? 14.254  -25.252 -2.495  1.00 49.70  ? 48  HIS A CE1 1 
ATOM   383  N  NE2 . HIS A 1 49 ? 13.471  -24.402 -1.882  1.00 43.59  ? 48  HIS A NE2 1 
ATOM   384  N  N   . GLU A 1 50 ? 8.172   -24.512 -6.048  1.00 44.94  ? 49  GLU A N   1 
ATOM   385  C  CA  . GLU A 1 50 ? 7.320   -24.487 -7.227  1.00 42.34  ? 49  GLU A CA  1 
ATOM   386  C  C   . GLU A 1 50 ? 6.981   -23.046 -7.630  1.00 42.73  ? 49  GLU A C   1 
ATOM   387  O  O   . GLU A 1 50 ? 7.134   -22.119 -6.821  1.00 45.54  ? 49  GLU A O   1 
ATOM   388  C  CB  . GLU A 1 50 ? 6.064   -25.323 -6.954  1.00 48.08  ? 49  GLU A CB  1 
ATOM   389  C  CG  . GLU A 1 50 ? 6.398   -26.795 -6.707  1.00 50.10  ? 49  GLU A CG  1 
ATOM   390  C  CD  . GLU A 1 50 ? 5.281   -27.687 -6.188  1.00 63.12  ? 49  GLU A CD  1 
ATOM   391  O  OE1 . GLU A 1 50 ? 4.083   -27.309 -6.251  1.00 66.83  ? 49  GLU A OE1 1 
ATOM   392  O  OE2 . GLU A 1 50 ? 5.638   -28.775 -5.673  1.00 68.39  ? 49  GLU A OE2 1 
ATOM   393  N  N   . THR A 1 51 ? 6.542   -22.876 -8.889  1.00 39.23  ? 50  THR A N   1 
ATOM   394  C  CA  . THR A 1 51 ? 5.989   -21.624 -9.365  1.00 37.96  ? 50  THR A CA  1 
ATOM   395  C  C   . THR A 1 51 ? 4.506   -21.804 -9.669  1.00 43.61  ? 50  THR A C   1 
ATOM   396  O  O   . THR A 1 51 ? 3.998   -22.916 -9.766  1.00 46.69  ? 50  THR A O   1 
ATOM   397  C  CB  . THR A 1 51 ? 6.785   -20.996 -10.499 1.00 47.60  ? 50  THR A CB  1 
ATOM   398  O  OG1 . THR A 1 51 ? 8.109   -20.899 -9.980  1.00 41.26  ? 50  THR A OG1 1 
ATOM   399  C  CG2 . THR A 1 51 ? 6.257   -19.619 -10.875 1.00 53.43  ? 50  THR A CG2 1 
ATOM   400  N  N   . ALA A 1 52 ? 3.804   -20.672 -9.685  1.00 47.48  ? 51  ALA A N   1 
ATOM   401  C  CA  . ALA A 1 52 ? 2.398   -20.595 -10.038 1.00 43.49  ? 51  ALA A CA  1 
ATOM   402  C  C   . ALA A 1 52 ? 2.169   -19.158 -10.454 1.00 44.93  ? 51  ALA A C   1 
ATOM   403  O  O   . ALA A 1 52 ? 3.117   -18.373 -10.428 1.00 45.50  ? 51  ALA A O   1 
ATOM   404  C  CB  . ALA A 1 52 ? 1.505   -20.995 -8.883  1.00 46.20  ? 51  ALA A CB  1 
ATOM   405  N  N   . PHE A 1 53 ? 0.928   -18.859 -10.856 1.00 39.02  ? 52  PHE A N   1 
ATOM   406  C  CA  . PHE A 1 53 ? 0.568   -17.590 -11.453 1.00 39.69  ? 52  PHE A CA  1 
ATOM   407  C  C   . PHE A 1 53 ? -0.731  -17.169 -10.786 1.00 43.63  ? 52  PHE A C   1 
ATOM   408  O  O   . PHE A 1 53 ? -1.746  -17.841 -10.980 1.00 47.30  ? 52  PHE A O   1 
ATOM   409  C  CB  . PHE A 1 53 ? 0.373   -17.851 -12.954 1.00 47.33  ? 52  PHE A CB  1 
ATOM   410  C  CG  . PHE A 1 53 ? 1.609   -17.930 -13.845 1.00 51.70  ? 52  PHE A CG  1 
ATOM   411  C  CD1 . PHE A 1 53 ? 2.673   -17.038 -13.685 1.00 52.28  ? 52  PHE A CD1 1 
ATOM   412  C  CD2 . PHE A 1 53 ? 1.691   -18.879 -14.871 1.00 51.22  ? 52  PHE A CD2 1 
ATOM   413  C  CE1 . PHE A 1 53 ? 3.805   -17.115 -14.493 1.00 54.85  ? 52  PHE A CE1 1 
ATOM   414  C  CE2 . PHE A 1 53 ? 2.825   -18.952 -15.684 1.00 56.70  ? 52  PHE A CE2 1 
ATOM   415  C  CZ  . PHE A 1 53 ? 3.874   -18.063 -15.503 1.00 54.51  ? 52  PHE A CZ  1 
ATOM   416  N  N   . LEU A 1 54 ? -0.655  -16.095 -9.982  1.00 41.61  ? 53  LEU A N   1 
ATOM   417  C  CA  . LEU A 1 54 ? -1.646  -15.752 -8.971  1.00 40.29  ? 53  LEU A CA  1 
ATOM   418  C  C   . LEU A 1 54 ? -1.952  -14.260 -9.035  1.00 37.04  ? 53  LEU A C   1 
ATOM   419  O  O   . LEU A 1 54 ? -1.055  -13.421 -9.130  1.00 25.59  ? 53  LEU A O   1 
ATOM   420  C  CB  . LEU A 1 54 ? -1.241  -16.172 -7.557  1.00 36.66  ? 53  LEU A CB  1 
ATOM   421  C  CG  . LEU A 1 54 ? -1.080  -17.676 -7.307  1.00 42.66  ? 53  LEU A CG  1 
ATOM   422  C  CD1 . LEU A 1 54 ? -0.883  -17.895 -5.826  1.00 36.39  ? 53  LEU A CD1 1 
ATOM   423  C  CD2 . LEU A 1 54 ? -2.332  -18.389 -7.824  1.00 41.27  ? 53  LEU A CD2 1 
ATOM   424  N  N   . GLY A 1 55 ? -3.257  -13.928 -9.012  1.00 26.40  ? 54  GLY A N   1 
ATOM   425  C  CA  . GLY A 1 55 ? -3.674  -12.564 -8.849  1.00 31.06  ? 54  GLY A CA  1 
ATOM   426  C  C   . GLY A 1 55 ? -3.631  -12.129 -7.382  1.00 26.18  ? 54  GLY A C   1 
ATOM   427  O  O   . GLY A 1 55 ? -3.560  -12.966 -6.453  1.00 34.05  ? 54  GLY A O   1 
ATOM   428  N  N   . PRO A 1 56 ? -3.643  -10.808 -7.103  1.00 30.08  ? 55  PRO A N   1 
ATOM   429  C  CA  . PRO A 1 56 ? -3.598  -10.328 -5.705  1.00 27.50  ? 55  PRO A CA  1 
ATOM   430  C  C   . PRO A 1 56 ? -4.583  -10.861 -4.662  1.00 27.92  ? 55  PRO A C   1 
ATOM   431  O  O   . PRO A 1 56 ? -4.312  -10.889 -3.455  1.00 29.81  ? 55  PRO A O   1 
ATOM   432  C  CB  . PRO A 1 56 ? -3.738  -8.779  -5.855  1.00 30.93  ? 55  PRO A CB  1 
ATOM   433  C  CG  . PRO A 1 56 ? -3.367  -8.472  -7.305  1.00 33.85  ? 55  PRO A CG  1 
ATOM   434  C  CD  . PRO A 1 56 ? -3.623  -9.735  -8.115  1.00 31.10  ? 55  PRO A CD  1 
ATOM   435  N  N   . LYS A 1 57 ? -5.822  -11.198 -5.077  1.00 33.83  ? 56  LYS A N   1 
ATOM   436  C  CA  . LYS A 1 57 ? -6.765  -11.709 -4.091  1.00 31.66  ? 56  LYS A CA  1 
ATOM   437  C  C   . LYS A 1 57 ? -6.166  -12.941 -3.377  1.00 39.51  ? 56  LYS A C   1 
ATOM   438  O  O   . LYS A 1 57 ? -6.580  -13.326 -2.285  1.00 35.62  ? 56  LYS A O   1 
ATOM   439  C  CB  . LYS A 1 57 ? -8.111  -12.096 -4.745  1.00 30.35  ? 56  LYS A CB  1 
ATOM   440  C  CG  . LYS A 1 57 ? -8.031  -13.375 -5.616  1.00 39.34  ? 56  LYS A CG  1 
ATOM   441  C  CD  . LYS A 1 57 ? -9.311  -13.754 -6.355  1.00 41.70  ? 56  LYS A CD  1 
ATOM   442  C  CE  . LYS A 1 57 ? -9.263  -15.024 -7.131  1.00 45.79  ? 56  LYS A CE  1 
ATOM   443  N  NZ  . LYS A 1 57 ? -9.010  -16.176 -6.259  1.00 44.36  ? 56  LYS A NZ  1 
ATOM   444  N  N   . ASP A 1 58 ? -5.131  -13.550 -3.959  1.00 43.99  ? 57  ASP A N   1 
ATOM   445  C  CA  . ASP A 1 58 ? -4.548  -14.701 -3.293  1.00 43.80  ? 57  ASP A CA  1 
ATOM   446  C  C   . ASP A 1 58 ? -3.215  -14.376 -2.625  1.00 45.47  ? 57  ASP A C   1 
ATOM   447  O  O   . ASP A 1 58 ? -2.465  -15.313 -2.318  1.00 36.00  ? 57  ASP A O   1 
ATOM   448  C  CB  . ASP A 1 58 ? -4.431  -15.883 -4.229  1.00 36.46  ? 57  ASP A CB  1 
ATOM   449  C  CG  . ASP A 1 58 ? -5.786  -16.406 -4.692  1.00 49.11  ? 57  ASP A CG  1 
ATOM   450  O  OD1 . ASP A 1 58 ? -6.738  -16.309 -3.889  1.00 40.98  ? 57  ASP A OD1 1 
ATOM   451  O  OD2 . ASP A 1 58 ? -5.881  -16.905 -5.848  1.00 48.28  ? 57  ASP A OD2 1 
ATOM   452  N  N   . LEU A 1 59 ? -2.963  -13.080 -2.371  1.00 34.02  ? 58  LEU A N   1 
ATOM   453  C  CA  . LEU A 1 59 ? -1.620  -12.689 -1.938  1.00 32.03  ? 58  LEU A CA  1 
ATOM   454  C  C   . LEU A 1 59 ? -1.709  -11.844 -0.664  1.00 30.10  ? 58  LEU A C   1 
ATOM   455  O  O   . LEU A 1 59 ? -2.195  -10.713 -0.676  1.00 38.78  ? 58  LEU A O   1 
ATOM   456  C  CB  . LEU A 1 59 ? -0.781  -11.984 -3.014  1.00 28.37  ? 58  LEU A CB  1 
ATOM   457  C  CG  . LEU A 1 59 ? -0.593  -12.637 -4.381  1.00 24.14  ? 58  LEU A CG  1 
ATOM   458  C  CD1 . LEU A 1 59 ? 0.075   -11.723 -5.359  1.00 23.69  ? 58  LEU A CD1 1 
ATOM   459  C  CD2 . LEU A 1 59 ? 0.007   -14.063 -4.363  1.00 24.02  ? 58  LEU A CD2 1 
ATOM   460  N  N   . PHE A 1 60 ? -1.191  -12.389 0.425   1.00 35.31  ? 59  PHE A N   1 
ATOM   461  C  CA  . PHE A 1 60 ? -1.225  -11.731 1.719   1.00 34.31  ? 59  PHE A CA  1 
ATOM   462  C  C   . PHE A 1 60 ? 0.192   -11.274 2.044   1.00 36.59  ? 59  PHE A C   1 
ATOM   463  O  O   . PHE A 1 60 ? 1.024   -12.119 2.363   1.00 35.01  ? 59  PHE A O   1 
ATOM   464  C  CB  . PHE A 1 60 ? -1.643  -12.823 2.694   1.00 24.74  ? 59  PHE A CB  1 
ATOM   465  C  CG  . PHE A 1 60 ? -3.070  -13.291 2.376   1.00 25.40  ? 59  PHE A CG  1 
ATOM   466  C  CD1 . PHE A 1 60 ? -3.284  -14.169 1.331   1.00 29.48  ? 59  PHE A CD1 1 
ATOM   467  C  CD2 . PHE A 1 60 ? -4.148  -12.747 3.043   1.00 29.80  ? 59  PHE A CD2 1 
ATOM   468  C  CE1 . PHE A 1 60 ? -4.573  -14.551 0.977   1.00 35.19  ? 59  PHE A CE1 1 
ATOM   469  C  CE2 . PHE A 1 60 ? -5.449  -13.154 2.721   1.00 25.57  ? 59  PHE A CE2 1 
ATOM   470  C  CZ  . PHE A 1 60 ? -5.638  -14.070 1.709   1.00 28.17  ? 59  PHE A CZ  1 
ATOM   471  N  N   . PRO A 1 61 ? 0.458   -9.951  2.106   1.00 38.70  ? 60  PRO A N   1 
ATOM   472  C  CA  . PRO A 1 61 ? 1.821   -9.484  2.394   1.00 35.12  ? 60  PRO A CA  1 
ATOM   473  C  C   . PRO A 1 61 ? 2.327   -10.003 3.749   1.00 36.30  ? 60  PRO A C   1 
ATOM   474  O  O   . PRO A 1 61 ? 1.550   -10.216 4.659   1.00 39.10  ? 60  PRO A O   1 
ATOM   475  C  CB  . PRO A 1 61 ? 1.756   -7.968  2.261   1.00 31.19  ? 60  PRO A CB  1 
ATOM   476  C  CG  . PRO A 1 61 ? 0.359   -7.670  1.737   1.00 41.27  ? 60  PRO A CG  1 
ATOM   477  C  CD  . PRO A 1 61 ? -0.522  -8.857  2.048   1.00 28.34  ? 60  PRO A CD  1 
ATOM   478  N  N   . TYR A 1 62 ? 3.652   -10.242 3.868   1.00 35.10  ? 61  TYR A N   1 
ATOM   479  C  CA  . TYR A 1 62 ? 4.240   -11.144 4.846   1.00 36.48  ? 61  TYR A CA  1 
ATOM   480  C  C   . TYR A 1 62 ? 4.170   -10.564 6.271   1.00 32.52  ? 61  TYR A C   1 
ATOM   481  O  O   . TYR A 1 62 ? 3.734   -11.205 7.231   1.00 38.47  ? 61  TYR A O   1 
ATOM   482  C  CB  . TYR A 1 62 ? 5.694   -11.402 4.400   1.00 32.49  ? 61  TYR A CB  1 
ATOM   483  C  CG  . TYR A 1 62 ? 6.442   -12.290 5.386   1.00 46.75  ? 61  TYR A CG  1 
ATOM   484  C  CD1 . TYR A 1 62 ? 6.165   -13.656 5.485   1.00 46.61  ? 61  TYR A CD1 1 
ATOM   485  C  CD2 . TYR A 1 62 ? 7.407   -11.760 6.247   1.00 49.38  ? 61  TYR A CD2 1 
ATOM   486  C  CE1 . TYR A 1 62 ? 6.827   -14.478 6.386   1.00 43.07  ? 61  TYR A CE1 1 
ATOM   487  C  CE2 . TYR A 1 62 ? 8.072   -12.569 7.156   1.00 41.58  ? 61  TYR A CE2 1 
ATOM   488  C  CZ  . TYR A 1 62 ? 7.790   -13.927 7.219   1.00 48.97  ? 61  TYR A CZ  1 
ATOM   489  O  OH  . TYR A 1 62 ? 8.445   -14.724 8.110   1.00 53.28  ? 61  TYR A OH  1 
ATOM   490  N  N   . ASP A 1 63 ? 4.650   -9.341  6.420   1.00 42.63  ? 62  ASP A N   1 
ATOM   491  C  CA  . ASP A 1 63 ? 4.758   -8.725  7.736   1.00 42.09  ? 62  ASP A CA  1 
ATOM   492  C  C   . ASP A 1 63 ? 3.390   -8.751  8.415   1.00 40.52  ? 62  ASP A C   1 
ATOM   493  O  O   . ASP A 1 63 ? 3.231   -9.395  9.450   1.00 45.90  ? 62  ASP A O   1 
ATOM   494  C  CB  . ASP A 1 63 ? 5.526   -7.416  7.640   1.00 49.44  ? 62  ASP A CB  1 
ATOM   495  C  CG  . ASP A 1 63 ? 7.007   -7.574  7.304   1.00 61.49  ? 62  ASP A CG  1 
ATOM   496  O  OD1 . ASP A 1 63 ? 7.665   -8.435  7.927   1.00 60.11  ? 62  ASP A OD1 1 
ATOM   497  O  OD2 . ASP A 1 63 ? 7.514   -6.804  6.456   1.00 68.10  ? 62  ASP A OD2 1 
ATOM   498  N  N   . LYS A 1 64 ? 2.397   -8.101  7.793   1.00 45.54  ? 63  LYS A N   1 
ATOM   499  C  CA  . LYS A 1 64 ? 1.025   -8.119  8.300   1.00 40.60  ? 63  LYS A CA  1 
ATOM   500  C  C   . LYS A 1 64 ? 0.589   -9.534  8.705   1.00 43.23  ? 63  LYS A C   1 
ATOM   501  O  O   . LYS A 1 64 ? -0.043  -9.681  9.742   1.00 45.01  ? 63  LYS A O   1 
ATOM   502  C  CB  . LYS A 1 64 ? 0.068   -7.368  7.360   1.00 38.65  ? 63  LYS A CB  1 
ATOM   503  C  CG  . LYS A 1 64 ? -1.426  -7.695  7.575   1.00 41.46  ? 63  LYS A CG  1 
ATOM   504  C  CD  . LYS A 1 64 ? -2.371  -6.836  6.751   1.00 39.04  ? 63  LYS A CD  1 
ATOM   505  C  CE  . LYS A 1 64 ? -3.228  -5.932  7.572   1.00 45.06  ? 63  LYS A CE  1 
ATOM   506  N  NZ  . LYS A 1 64 ? -4.634  -6.329  7.442   1.00 40.76  ? 63  LYS A NZ  1 
ATOM   507  N  N   . SER A 1 65 ? 0.929   -10.570 7.907   1.00 48.12  ? 64  SER A N   1 
ATOM   508  C  CA  . SER A 1 65 ? 0.242   -11.858 7.953   1.00 41.57  ? 64  SER A CA  1 
ATOM   509  C  C   . SER A 1 65 ? 1.013   -12.951 8.698   1.00 45.78  ? 64  SER A C   1 
ATOM   510  O  O   . SER A 1 65 ? 0.423   -13.974 9.056   1.00 45.07  ? 64  SER A O   1 
ATOM   511  C  CB  . SER A 1 65 ? -0.090  -12.343 6.556   1.00 42.14  ? 64  SER A CB  1 
ATOM   512  O  OG  . SER A 1 65 ? -0.993  -11.467 5.897   1.00 56.32  ? 64  SER A OG  1 
ATOM   513  N  N   . LYS A 1 66 ? 2.335   -12.786 8.886   1.00 36.83  ? 65  LYS A N   1 
ATOM   514  C  CA  . LYS A 1 66 ? 3.136   -13.889 9.390   1.00 39.14  ? 65  LYS A CA  1 
ATOM   515  C  C   . LYS A 1 66 ? 2.666   -14.388 10.772  1.00 44.65  ? 65  LYS A C   1 
ATOM   516  O  O   . LYS A 1 66 ? 2.731   -15.583 11.073  1.00 52.99  ? 65  LYS A O   1 
ATOM   517  C  CB  . LYS A 1 66 ? 4.593   -13.437 9.206   1.00 34.47  ? 65  LYS A CB  1 
ATOM   518  C  CG  . LYS A 1 66 ? 5.202   -12.740 10.383  1.00 51.41  ? 65  LYS A CG  1 
ATOM   519  C  CD  . LYS A 1 66 ? 6.716   -12.907 10.303  1.00 61.82  ? 65  LYS A CD  1 
ATOM   520  C  CE  . LYS A 1 66 ? 7.412   -12.382 11.521  1.00 70.49  ? 65  LYS A CE  1 
ATOM   521  N  NZ  . LYS A 1 66 ? 7.106   -10.964 11.724  1.00 72.34  ? 65  LYS A NZ  1 
ATOM   522  N  N   A ASP A 1 67 ? 2.190   -13.488 11.639  0.50 45.39  ? 66  ASP A N   1 
ATOM   523  N  N   B ASP A 1 67 ? 2.167   -13.449 11.580  0.50 49.03  ? 66  ASP A N   1 
ATOM   524  C  CA  A ASP A 1 67 ? 1.665   -13.922 12.929  0.50 48.38  ? 66  ASP A CA  1 
ATOM   525  C  CA  B ASP A 1 67 ? 1.559   -13.677 12.883  0.50 54.94  ? 66  ASP A CA  1 
ATOM   526  C  C   A ASP A 1 67 ? 0.498   -14.895 12.736  0.50 50.25  ? 66  ASP A C   1 
ATOM   527  C  C   B ASP A 1 67 ? 0.437   -14.716 12.790  0.50 53.91  ? 66  ASP A C   1 
ATOM   528  O  O   A ASP A 1 67 ? 0.321   -15.811 13.536  0.50 54.89  ? 66  ASP A O   1 
ATOM   529  O  O   B ASP A 1 67 ? 0.242   -15.505 13.709  0.50 58.82  ? 66  ASP A O   1 
ATOM   530  C  CB  A ASP A 1 67 ? 1.295   -12.755 13.839  0.50 45.19  ? 66  ASP A CB  1 
ATOM   531  C  CB  B ASP A 1 67 ? 1.085   -12.338 13.432  0.50 57.86  ? 66  ASP A CB  1 
ATOM   532  C  CG  A ASP A 1 67 ? 2.437   -12.031 14.545  0.50 45.79  ? 66  ASP A CG  1 
ATOM   533  C  CG  B ASP A 1 67 ? 0.559   -12.312 14.856  0.50 59.59  ? 66  ASP A CG  1 
ATOM   534  O  OD1 A ASP A 1 67 ? 3.582   -12.529 14.502  0.50 45.57  ? 66  ASP A OD1 1 
ATOM   535  O  OD1 B ASP A 1 67 ? 1.340   -12.646 15.774  0.50 57.36  ? 66  ASP A OD1 1 
ATOM   536  O  OD2 A ASP A 1 67 ? 2.172   -10.962 15.132  0.50 40.98  ? 66  ASP A OD2 1 
ATOM   537  O  OD2 B ASP A 1 67 ? -0.620  -11.932 15.028  0.50 60.85  ? 66  ASP A OD2 1 
ATOM   538  N  N   . LYS A 1 68 ? -0.297  -14.712 11.670  1.00 52.86  ? 67  LYS A N   1 
ATOM   539  C  CA  . LYS A 1 68 ? -1.444  -15.588 11.469  1.00 47.95  ? 67  LYS A CA  1 
ATOM   540  C  C   . LYS A 1 68 ? -1.009  -16.903 10.832  1.00 46.19  ? 67  LYS A C   1 
ATOM   541  O  O   . LYS A 1 68 ? -1.422  -17.977 11.275  1.00 56.45  ? 67  LYS A O   1 
ATOM   542  C  CB  . LYS A 1 68 ? -2.580  -14.954 10.657  1.00 42.55  ? 67  LYS A CB  1 
ATOM   543  C  CG  . LYS A 1 68 ? -3.894  -15.706 10.701  1.00 39.00  ? 67  LYS A CG  1 
ATOM   544  C  CD  . LYS A 1 68 ? -4.928  -14.893 9.936   1.00 40.34  ? 67  LYS A CD  1 
ATOM   545  C  CE  . LYS A 1 68 ? -6.352  -15.276 10.246  1.00 43.83  ? 67  LYS A CE  1 
ATOM   546  N  NZ  . LYS A 1 68 ? -7.230  -14.511 9.360   1.00 50.25  ? 67  LYS A NZ  1 
ATOM   547  N  N   . TYR A 1 69 ? -0.183  -16.804 9.790   1.00 36.48  ? 68  TYR A N   1 
ATOM   548  C  CA  . TYR A 1 69 ? 0.044   -17.862 8.819   1.00 35.54  ? 68  TYR A CA  1 
ATOM   549  C  C   . TYR A 1 69 ? 1.489   -18.344 8.956   1.00 36.75  ? 68  TYR A C   1 
ATOM   550  O  O   . TYR A 1 69 ? 1.849   -19.345 8.376   1.00 45.64  ? 68  TYR A O   1 
ATOM   551  C  CB  . TYR A 1 69 ? -0.143  -17.426 7.354   1.00 30.99  ? 68  TYR A CB  1 
ATOM   552  C  CG  . TYR A 1 69 ? -1.553  -16.994 6.977   1.00 34.64  ? 68  TYR A CG  1 
ATOM   553  C  CD1 . TYR A 1 69 ? -2.678  -17.699 7.407   1.00 40.49  ? 68  TYR A CD1 1 
ATOM   554  C  CD2 . TYR A 1 69 ? -1.749  -15.897 6.155   1.00 33.29  ? 68  TYR A CD2 1 
ATOM   555  C  CE1 . TYR A 1 69 ? -3.961  -17.288 7.061   1.00 38.45  ? 68  TYR A CE1 1 
ATOM   556  C  CE2 . TYR A 1 69 ? -3.020  -15.478 5.806   1.00 37.31  ? 68  TYR A CE2 1 
ATOM   557  C  CZ  . TYR A 1 69 ? -4.126  -16.168 6.270   1.00 34.43  ? 68  TYR A CZ  1 
ATOM   558  O  OH  . TYR A 1 69 ? -5.384  -15.734 5.908   1.00 39.97  ? 68  TYR A OH  1 
ATOM   559  N  N   . GLY A 1 70 ? 2.318   -17.646 9.727   1.00 43.26  ? 69  GLY A N   1 
ATOM   560  C  CA  . GLY A 1 70 ? 3.696   -18.112 9.845   1.00 49.64  ? 69  GLY A CA  1 
ATOM   561  C  C   . GLY A 1 70 ? 3.873   -19.143 10.967  1.00 50.26  ? 69  GLY A C   1 
ATOM   562  O  O   . GLY A 1 70 ? 4.629   -18.920 11.895  1.00 51.95  ? 69  GLY A O   1 
ATOM   563  N  N   . LYS A 1 71 ? 3.185   -20.284 10.897  1.00 53.64  ? 70  LYS A N   1 
ATOM   564  C  CA  . LYS A 1 71 ? 3.314   -21.290 11.948  1.00 58.30  ? 70  LYS A CA  1 
ATOM   565  C  C   . LYS A 1 71 ? 3.546   -22.660 11.316  1.00 56.73  ? 70  LYS A C   1 
ATOM   566  O  O   . LYS A 1 71 ? 3.203   -22.866 10.149  1.00 57.83  ? 70  LYS A O   1 
ATOM   567  C  CB  . LYS A 1 71 ? 2.106   -21.283 12.894  1.00 61.35  ? 70  LYS A CB  1 
ATOM   568  C  CG  . LYS A 1 71 ? 2.081   -20.144 13.918  1.00 68.37  ? 70  LYS A CG  1 
ATOM   569  C  CD  . LYS A 1 71 ? 0.692   -19.853 14.476  1.00 73.08  ? 70  LYS A CD  1 
ATOM   570  N  N   . PRO A 1 72 ? 4.202   -23.615 12.022  1.00 55.09  ? 71  PRO A N   1 
ATOM   571  C  CA  . PRO A 1 72 ? 4.490   -24.928 11.440  1.00 50.81  ? 71  PRO A CA  1 
ATOM   572  C  C   . PRO A 1 72 ? 3.263   -25.717 11.009  1.00 50.58  ? 71  PRO A C   1 
ATOM   573  O  O   . PRO A 1 72 ? 2.212   -25.626 11.630  1.00 50.46  ? 71  PRO A O   1 
ATOM   574  C  CB  . PRO A 1 72 ? 5.341   -25.626 12.504  1.00 49.04  ? 71  PRO A CB  1 
ATOM   575  C  CG  . PRO A 1 72 ? 6.010   -24.438 13.173  1.00 58.26  ? 71  PRO A CG  1 
ATOM   576  C  CD  . PRO A 1 72 ? 4.850   -23.440 13.335  1.00 56.01  ? 71  PRO A CD  1 
ATOM   577  N  N   . ASN A 1 73 ? 3.445   -26.471 9.924   1.00 51.09  ? 72  ASN A N   1 
ATOM   578  C  CA  . ASN A 1 73 ? 2.397   -27.180 9.222   1.00 55.13  ? 72  ASN A CA  1 
ATOM   579  C  C   . ASN A 1 73 ? 3.088   -28.417 8.682   1.00 55.16  ? 72  ASN A C   1 
ATOM   580  O  O   . ASN A 1 73 ? 4.298   -28.385 8.463   1.00 48.13  ? 72  ASN A O   1 
ATOM   581  C  CB  . ASN A 1 73 ? 1.844   -26.301 8.100   1.00 68.32  ? 72  ASN A CB  1 
ATOM   582  C  CG  . ASN A 1 73 ? 0.656   -26.890 7.380   1.00 73.54  ? 72  ASN A CG  1 
ATOM   583  O  OD1 . ASN A 1 73 ? 0.763   -27.963 6.775   1.00 84.07  ? 72  ASN A OD1 1 
ATOM   584  N  ND2 . ASN A 1 73 ? -0.473  -26.196 7.414   1.00 60.27  ? 72  ASN A ND2 1 
ATOM   585  N  N   . LYS A 1 74 ? 2.315   -29.489 8.508   1.00 60.01  ? 73  LYS A N   1 
ATOM   586  C  CA  . LYS A 1 74 ? 2.861   -30.805 8.235   1.00 66.32  ? 73  LYS A CA  1 
ATOM   587  C  C   . LYS A 1 74 ? 3.142   -31.000 6.743   1.00 65.01  ? 73  LYS A C   1 
ATOM   588  O  O   . LYS A 1 74 ? 3.872   -31.924 6.384   1.00 59.86  ? 73  LYS A O   1 
ATOM   589  C  CB  . LYS A 1 74 ? 1.915   -31.885 8.780   1.00 81.97  ? 73  LYS A CB  1 
ATOM   590  C  CG  . LYS A 1 74 ? 0.627   -32.150 7.983   1.00 82.62  ? 73  LYS A CG  1 
ATOM   591  N  N   . ARG A 1 75 ? 2.573   -30.145 5.879   1.00 63.33  ? 74  ARG A N   1 
ATOM   592  C  CA  . ARG A 1 75 ? 2.654   -30.349 4.433   1.00 58.91  ? 74  ARG A CA  1 
ATOM   593  C  C   . ARG A 1 75 ? 4.110   -30.311 3.971   1.00 50.13  ? 74  ARG A C   1 
ATOM   594  O  O   . ARG A 1 75 ? 4.936   -29.624 4.563   1.00 53.04  ? 74  ARG A O   1 
ATOM   595  C  CB  . ARG A 1 75 ? 1.904   -29.323 3.573   1.00 55.57  ? 74  ARG A CB  1 
ATOM   596  C  CG  . ARG A 1 75 ? 0.417   -29.095 3.789   1.00 57.62  ? 74  ARG A CG  1 
ATOM   597  C  CD  . ARG A 1 75 ? -0.453  -30.100 3.069   1.00 59.18  ? 74  ARG A CD  1 
ATOM   598  N  NE  . ARG A 1 75 ? -1.811  -29.602 2.824   1.00 68.76  ? 74  ARG A NE  1 
ATOM   599  C  CZ  . ARG A 1 75 ? -2.661  -29.077 3.703   1.00 73.90  ? 74  ARG A CZ  1 
ATOM   600  N  NH1 . ARG A 1 75 ? -3.934  -28.965 3.365   1.00 78.82  ? 74  ARG A NH1 1 
ATOM   601  N  NH2 . ARG A 1 75 ? -2.275  -28.725 4.921   1.00 68.97  ? 74  ARG A NH2 1 
ATOM   602  N  N   . LYS A 1 76 ? 4.392   -31.056 2.896   1.00 48.66  ? 75  LYS A N   1 
ATOM   603  C  CA  . LYS A 1 76 ? 5.742   -31.251 2.391   1.00 51.68  ? 75  LYS A CA  1 
ATOM   604  C  C   . LYS A 1 76 ? 6.285   -29.903 1.940   1.00 51.36  ? 75  LYS A C   1 
ATOM   605  O  O   . LYS A 1 76 ? 5.640   -29.220 1.147   1.00 46.17  ? 75  LYS A O   1 
ATOM   606  C  CB  . LYS A 1 76 ? 5.716   -32.171 1.159   1.00 49.49  ? 75  LYS A CB  1 
ATOM   607  C  CG  . LYS A 1 76 ? 7.109   -32.613 0.718   1.00 50.69  ? 75  LYS A CG  1 
ATOM   608  C  CD  . LYS A 1 76 ? 7.202   -33.741 -0.300  1.00 59.16  ? 75  LYS A CD  1 
ATOM   609  C  CE  . LYS A 1 76 ? 8.656   -34.112 -0.507  1.00 60.21  ? 75  LYS A CE  1 
ATOM   610  N  N   . GLY A 1 77 ? 7.488   -29.549 2.398   1.00 52.90  ? 76  GLY A N   1 
ATOM   611  C  CA  . GLY A 1 77 ? 8.080   -28.287 1.985   1.00 44.87  ? 76  GLY A CA  1 
ATOM   612  C  C   . GLY A 1 77 ? 7.821   -27.140 2.972   1.00 44.39  ? 76  GLY A C   1 
ATOM   613  O  O   . GLY A 1 77 ? 8.712   -26.325 3.195   1.00 46.44  ? 76  GLY A O   1 
ATOM   614  N  N   . PHE A 1 78 ? 6.642   -27.119 3.617   1.00 46.70  ? 77  PHE A N   1 
ATOM   615  C  CA  . PHE A 1 78 ? 6.176   -26.002 4.435   1.00 50.23  ? 77  PHE A CA  1 
ATOM   616  C  C   . PHE A 1 78 ? 7.279   -25.398 5.306   1.00 48.69  ? 77  PHE A C   1 
ATOM   617  O  O   . PHE A 1 78 ? 7.673   -24.251 5.107   1.00 43.85  ? 77  PHE A O   1 
ATOM   618  C  CB  . PHE A 1 78 ? 4.920   -26.330 5.248   1.00 47.40  ? 77  PHE A CB  1 
ATOM   619  C  CG  . PHE A 1 78 ? 4.131   -25.062 5.533   1.00 42.71  ? 77  PHE A CG  1 
ATOM   620  C  CD1 . PHE A 1 78 ? 4.347   -24.342 6.703   1.00 42.98  ? 77  PHE A CD1 1 
ATOM   621  C  CD2 . PHE A 1 78 ? 3.163   -24.592 4.638   1.00 48.50  ? 77  PHE A CD2 1 
ATOM   622  C  CE1 . PHE A 1 78 ? 3.653   -23.163 6.957   1.00 50.50  ? 77  PHE A CE1 1 
ATOM   623  C  CE2 . PHE A 1 78 ? 2.452   -23.413 4.898   1.00 37.99  ? 77  PHE A CE2 1 
ATOM   624  C  CZ  . PHE A 1 78 ? 2.698   -22.703 6.073   1.00 39.15  ? 77  PHE A CZ  1 
ATOM   625  N  N   . ASN A 1 79 ? 7.769   -26.183 6.271   1.00 48.15  ? 78  ASN A N   1 
ATOM   626  C  CA  . ASN A 1 79 ? 8.623   -25.689 7.347   1.00 42.29  ? 78  ASN A CA  1 
ATOM   627  C  C   . ASN A 1 79 ? 10.019  -25.325 6.825   1.00 36.99  ? 78  ASN A C   1 
ATOM   628  O  O   . ASN A 1 79 ? 10.649  -24.411 7.358   1.00 47.08  ? 78  ASN A O   1 
ATOM   629  C  CB  . ASN A 1 79 ? 8.624   -26.640 8.544   1.00 38.35  ? 78  ASN A CB  1 
ATOM   630  C  CG  . ASN A 1 79 ? 7.214   -27.021 8.944   1.00 50.53  ? 78  ASN A CG  1 
ATOM   631  O  OD1 . ASN A 1 79 ? 6.375   -26.154 9.232   1.00 46.21  ? 78  ASN A OD1 1 
ATOM   632  N  ND2 . ASN A 1 79 ? 6.927   -28.315 8.952   1.00 49.85  ? 78  ASN A ND2 1 
ATOM   633  N  N   . GLU A 1 80 ? 10.499  -26.026 5.791   1.00 34.31  ? 79  GLU A N   1 
ATOM   634  C  CA  . GLU A 1 80 ? 11.631  -25.530 5.014   1.00 44.20  ? 79  GLU A CA  1 
ATOM   635  C  C   . GLU A 1 80 ? 11.286  -24.120 4.527   1.00 42.53  ? 79  GLU A C   1 
ATOM   636  O  O   . GLU A 1 80 ? 12.123  -23.225 4.517   1.00 42.61  ? 79  GLU A O   1 
ATOM   637  C  CB  . GLU A 1 80 ? 11.953  -26.368 3.770   1.00 42.09  ? 79  GLU A CB  1 
ATOM   638  C  CG  . GLU A 1 80 ? 13.396  -26.227 3.271   1.00 45.44  ? 79  GLU A CG  1 
ATOM   639  C  CD  . GLU A 1 80 ? 13.844  -27.011 2.020   1.00 58.61  ? 79  GLU A CD  1 
ATOM   640  O  OE1 . GLU A 1 80 ? 13.034  -27.804 1.505   1.00 49.33  ? 79  GLU A OE1 1 
ATOM   641  O  OE2 . GLU A 1 80 ? 15.002  -26.867 1.531   1.00 54.93  ? 79  GLU A OE2 1 
ATOM   642  N  N   . GLY A 1 81 ? 10.024  -23.928 4.135   1.00 41.76  ? 80  GLY A N   1 
ATOM   643  C  CA  . GLY A 1 81 ? 9.662   -22.730 3.397   1.00 43.30  ? 80  GLY A CA  1 
ATOM   644  C  C   . GLY A 1 81 ? 9.695   -21.524 4.329   1.00 35.50  ? 80  GLY A C   1 
ATOM   645  O  O   . GLY A 1 81 ? 10.145  -20.438 3.917   1.00 38.05  ? 80  GLY A O   1 
ATOM   646  N  N   . LEU A 1 82 ? 9.161   -21.741 5.543   1.00 35.01  ? 81  LEU A N   1 
ATOM   647  C  CA  . LEU A 1 82 ? 9.161   -20.767 6.625   1.00 37.93  ? 81  LEU A CA  1 
ATOM   648  C  C   . LEU A 1 82 ? 10.612  -20.400 6.919   1.00 39.11  ? 81  LEU A C   1 
ATOM   649  O  O   . LEU A 1 82 ? 10.923  -19.223 7.072   1.00 43.57  ? 81  LEU A O   1 
ATOM   650  C  CB  . LEU A 1 82 ? 8.447   -21.093 7.934   1.00 34.37  ? 81  LEU A CB  1 
ATOM   651  C  CG  . LEU A 1 82 ? 6.964   -21.497 7.915   1.00 44.01  ? 81  LEU A CG  1 
ATOM   652  C  CD1 . LEU A 1 82 ? 6.669   -22.310 9.211   1.00 41.51  ? 81  LEU A CD1 1 
ATOM   653  C  CD2 . LEU A 1 82 ? 6.002   -20.319 7.848   1.00 33.53  ? 81  LEU A CD2 1 
ATOM   654  N  N   . TRP A 1 83 ? 11.497  -21.394 6.936   1.00 39.73  ? 82  TRP A N   1 
ATOM   655  C  CA  . TRP A 1 83 ? 12.905  -21.073 7.146   1.00 38.71  ? 82  TRP A CA  1 
ATOM   656  C  C   . TRP A 1 83 ? 13.359  -20.055 6.115   1.00 36.89  ? 82  TRP A C   1 
ATOM   657  O  O   . TRP A 1 83 ? 13.943  -19.049 6.518   1.00 35.31  ? 82  TRP A O   1 
ATOM   658  C  CB  . TRP A 1 83 ? 13.827  -22.297 7.109   1.00 35.71  ? 82  TRP A CB  1 
ATOM   659  C  CG  . TRP A 1 83 ? 15.255  -21.977 7.484   1.00 35.68  ? 82  TRP A CG  1 
ATOM   660  C  CD1 . TRP A 1 83 ? 15.771  -22.019 8.749   1.00 48.03  ? 82  TRP A CD1 1 
ATOM   661  C  CD2 . TRP A 1 83 ? 16.352  -21.582 6.630   1.00 40.36  ? 82  TRP A CD2 1 
ATOM   662  N  NE1 . TRP A 1 83 ? 17.104  -21.684 8.743   1.00 43.35  ? 82  TRP A NE1 1 
ATOM   663  C  CE2 . TRP A 1 83 ? 17.485  -21.411 7.461   1.00 41.42  ? 82  TRP A CE2 1 
ATOM   664  C  CE3 . TRP A 1 83 ? 16.495  -21.361 5.255   1.00 40.91  ? 82  TRP A CE3 1 
ATOM   665  C  CZ2 . TRP A 1 83 ? 18.731  -21.034 6.963   1.00 38.64  ? 82  TRP A CZ2 1 
ATOM   666  C  CZ3 . TRP A 1 83 ? 17.729  -20.980 4.770   1.00 43.43  ? 82  TRP A CZ3 1 
ATOM   667  C  CH2 . TRP A 1 83 ? 18.831  -20.816 5.613   1.00 34.91  ? 82  TRP A CH2 1 
ATOM   668  N  N   . GLU A 1 84 ? 13.096  -20.353 4.810   1.00 41.65  ? 83  GLU A N   1 
ATOM   669  C  CA  . GLU A 1 84 ? 13.644  -19.618 3.682   1.00 38.60  ? 83  GLU A CA  1 
ATOM   670  C  C   . GLU A 1 84 ? 13.173  -18.154 3.773   1.00 39.51  ? 83  GLU A C   1 
ATOM   671  O  O   . GLU A 1 84 ? 13.954  -17.220 3.735   1.00 32.77  ? 83  GLU A O   1 
ATOM   672  C  CB  . GLU A 1 84 ? 13.330  -20.245 2.304   1.00 42.08  ? 83  GLU A CB  1 
ATOM   673  C  CG  . GLU A 1 84 ? 13.641  -21.729 2.061   1.00 35.93  ? 83  GLU A CG  1 
ATOM   674  C  CD  . GLU A 1 84 ? 13.352  -22.415 0.704   1.00 46.06  ? 83  GLU A CD  1 
ATOM   675  O  OE1 . GLU A 1 84 ? 12.242  -22.438 0.055   1.00 35.02  ? 83  GLU A OE1 1 
ATOM   676  O  OE2 . GLU A 1 84 ? 14.331  -23.059 0.293   1.00 38.17  ? 83  GLU A OE2 1 
ATOM   677  N  N   . ILE A 1 85 ? 11.863  -17.922 3.949   1.00 33.78  ? 84  ILE A N   1 
ATOM   678  C  CA  . ILE A 1 85 ? 11.317  -16.580 3.897   1.00 32.09  ? 84  ILE A CA  1 
ATOM   679  C  C   . ILE A 1 85 ? 11.823  -15.732 5.085   1.00 34.97  ? 84  ILE A C   1 
ATOM   680  O  O   . ILE A 1 85 ? 11.993  -14.510 4.980   1.00 33.80  ? 84  ILE A O   1 
ATOM   681  C  CB  . ILE A 1 85 ? 9.769   -16.688 3.776   1.00 31.39  ? 84  ILE A CB  1 
ATOM   682  C  CG1 . ILE A 1 85 ? 9.157   -15.414 3.243   1.00 34.03  ? 84  ILE A CG1 1 
ATOM   683  C  CG2 . ILE A 1 85 ? 9.137   -17.094 5.105   1.00 37.25  ? 84  ILE A CG2 1 
ATOM   684  C  CD1 . ILE A 1 85 ? 7.623   -15.448 3.126   1.00 34.05  ? 84  ILE A CD1 1 
ATOM   685  N  N   . GLN A 1 86 ? 12.142  -16.382 6.210   1.00 38.60  ? 85  GLN A N   1 
ATOM   686  C  CA  . GLN A 1 86 ? 12.656  -15.691 7.381   1.00 39.11  ? 85  GLN A CA  1 
ATOM   687  C  C   . GLN A 1 86 ? 14.176  -15.525 7.259   1.00 38.35  ? 85  GLN A C   1 
ATOM   688  O  O   . GLN A 1 86 ? 14.685  -14.521 7.729   1.00 40.64  ? 85  GLN A O   1 
ATOM   689  C  CB  . GLN A 1 86 ? 12.198  -16.414 8.650   1.00 45.83  ? 85  GLN A CB  1 
ATOM   690  C  CG  . GLN A 1 86 ? 12.570  -15.768 9.984   1.00 45.67  ? 85  GLN A CG  1 
ATOM   691  C  CD  . GLN A 1 86 ? 11.954  -16.491 11.176  1.00 52.43  ? 85  GLN A CD  1 
ATOM   692  O  OE1 . GLN A 1 86 ? 11.934  -17.735 11.256  1.00 51.14  ? 85  GLN A OE1 1 
ATOM   693  N  NE2 . GLN A 1 86 ? 11.413  -15.715 12.110  1.00 46.42  ? 85  GLN A NE2 1 
ATOM   694  N  N   . ASN A 1 87 ? 14.875  -16.410 6.531   1.00 38.55  ? 86  ASN A N   1 
ATOM   695  C  CA  . ASN A 1 87 ? 16.331  -16.422 6.683   1.00 39.38  ? 86  ASN A CA  1 
ATOM   696  C  C   . ASN A 1 87 ? 17.090  -16.050 5.409   1.00 49.25  ? 86  ASN A C   1 
ATOM   697  O  O   . ASN A 1 87 ? 18.182  -15.489 5.514   1.00 50.84  ? 86  ASN A O   1 
ATOM   698  C  CB  . ASN A 1 87 ? 16.839  -17.670 7.402   1.00 44.11  ? 86  ASN A CB  1 
ATOM   699  C  CG  . ASN A 1 87 ? 16.406  -17.705 8.856   1.00 39.67  ? 86  ASN A CG  1 
ATOM   700  O  OD1 . ASN A 1 87 ? 16.724  -16.806 9.651   1.00 40.32  ? 86  ASN A OD1 1 
ATOM   701  N  ND2 . ASN A 1 87 ? 15.624  -18.707 9.227   1.00 42.77  ? 86  ASN A ND2 1 
ATOM   702  N  N   . ASN A 1 88 ? 16.565  -16.375 4.220   1.00 41.73  ? 87  ASN A N   1 
ATOM   703  C  CA  . ASN A 1 88 ? 17.254  -15.946 3.011   1.00 49.00  ? 87  ASN A CA  1 
ATOM   704  C  C   . ASN A 1 88 ? 16.242  -15.774 1.880   1.00 40.36  ? 87  ASN A C   1 
ATOM   705  O  O   . ASN A 1 88 ? 16.192  -16.586 0.963   1.00 41.06  ? 87  ASN A O   1 
ATOM   706  C  CB  . ASN A 1 88 ? 18.383  -16.911 2.648   1.00 46.18  ? 87  ASN A CB  1 
ATOM   707  C  CG  . ASN A 1 88 ? 19.421  -16.271 1.771   1.00 42.24  ? 87  ASN A CG  1 
ATOM   708  O  OD1 . ASN A 1 88 ? 19.144  -15.239 1.160   1.00 37.99  ? 87  ASN A OD1 1 
ATOM   709  N  ND2 . ASN A 1 88 ? 20.634  -16.820 1.740   1.00 38.67  ? 87  ASN A ND2 1 
ATOM   710  N  N   . PRO A 1 89 ? 15.298  -14.811 1.953   1.00 35.20  ? 88  PRO A N   1 
ATOM   711  C  CA  . PRO A 1 89 ? 14.162  -14.891 1.052   1.00 32.91  ? 88  PRO A CA  1 
ATOM   712  C  C   . PRO A 1 89 ? 14.421  -14.315 -0.340  1.00 38.48  ? 88  PRO A C   1 
ATOM   713  O  O   . PRO A 1 89 ? 13.526  -14.398 -1.161  1.00 37.62  ? 88  PRO A O   1 
ATOM   714  C  CB  . PRO A 1 89 ? 13.138  -14.122 1.872   1.00 27.92  ? 88  PRO A CB  1 
ATOM   715  C  CG  . PRO A 1 89 ? 13.925  -12.991 2.520   1.00 34.46  ? 88  PRO A CG  1 
ATOM   716  C  CD  . PRO A 1 89 ? 15.239  -13.652 2.863   1.00 35.77  ? 88  PRO A CD  1 
ATOM   717  N  N   . HIS A 1 90 ? 15.650  -13.812 -0.612  1.00 31.36  ? 89  HIS A N   1 
ATOM   718  C  CA  . HIS A 1 90 ? 16.009  -13.150 -1.860  1.00 35.97  ? 89  HIS A CA  1 
ATOM   719  C  C   . HIS A 1 90 ? 17.030  -14.046 -2.543  1.00 40.62  ? 89  HIS A C   1 
ATOM   720  O  O   . HIS A 1 90 ? 17.543  -13.672 -3.595  1.00 40.69  ? 89  HIS A O   1 
ATOM   721  C  CB  . HIS A 1 90 ? 16.470  -11.679 -1.696  1.00 26.79  ? 89  HIS A CB  1 
ATOM   722  C  CG  . HIS A 1 90 ? 15.389  -10.822 -1.108  1.00 29.58  ? 89  HIS A CG  1 
ATOM   723  N  ND1 . HIS A 1 90 ? 14.118  -10.895 -1.664  1.00 30.80  ? 89  HIS A ND1 1 
ATOM   724  C  CD2 . HIS A 1 90 ? 15.277  -10.024 -0.012  1.00 31.29  ? 89  HIS A CD2 1 
ATOM   725  C  CE1 . HIS A 1 90 ? 13.292  -10.117 -0.997  1.00 29.54  ? 89  HIS A CE1 1 
ATOM   726  N  NE2 . HIS A 1 90 ? 13.955  -9.555  0.010   1.00 35.00  ? 89  HIS A NE2 1 
ATOM   727  N  N   . ALA A 1 91 ? 17.253  -15.240 -1.952  1.00 39.05  ? 90  ALA A N   1 
ATOM   728  C  CA  . ALA A 1 91 ? 18.291  -16.138 -2.454  1.00 40.18  ? 90  ALA A CA  1 
ATOM   729  C  C   . ALA A 1 91 ? 17.919  -16.751 -3.798  1.00 45.30  ? 90  ALA A C   1 
ATOM   730  O  O   . ALA A 1 91 ? 16.741  -16.779 -4.240  1.00 35.53  ? 90  ALA A O   1 
ATOM   731  C  CB  . ALA A 1 91 ? 18.678  -17.242 -1.487  1.00 34.76  ? 90  ALA A CB  1 
ATOM   732  N  N   . SER A 1 92 ? 18.978  -17.274 -4.430  1.00 33.62  ? 91  SER A N   1 
ATOM   733  C  CA  . SER A 1 92 ? 18.731  -18.121 -5.589  1.00 44.52  ? 91  SER A CA  1 
ATOM   734  C  C   . SER A 1 92 ? 18.573  -19.579 -5.180  1.00 49.83  ? 91  SER A C   1 
ATOM   735  O  O   . SER A 1 92 ? 19.530  -20.193 -4.705  1.00 49.37  ? 91  SER A O   1 
ATOM   736  C  CB  . SER A 1 92 ? 19.777  -18.002 -6.648  1.00 51.59  ? 91  SER A CB  1 
ATOM   737  O  OG  . SER A 1 92 ? 19.608  -19.115 -7.515  1.00 61.38  ? 91  SER A OG  1 
ATOM   738  N  N   . TYR A 1 93 ? 17.365  -20.116 -5.422  1.00 47.21  ? 92  TYR A N   1 
ATOM   739  C  CA  . TYR A 1 93 ? 17.012  -21.486 -5.074  1.00 49.17  ? 92  TYR A CA  1 
ATOM   740  C  C   . TYR A 1 93 ? 17.095  -22.386 -6.307  1.00 59.40  ? 92  TYR A C   1 
ATOM   741  O  O   . TYR A 1 93 ? 16.297  -23.309 -6.456  1.00 58.89  ? 92  TYR A O   1 
ATOM   742  C  CB  . TYR A 1 93 ? 15.686  -21.578 -4.309  1.00 46.83  ? 92  TYR A CB  1 
ATOM   743  C  CG  . TYR A 1 93 ? 15.784  -20.986 -2.909  1.00 46.98  ? 92  TYR A CG  1 
ATOM   744  C  CD1 . TYR A 1 93 ? 16.201  -21.767 -1.840  1.00 44.70  ? 92  TYR A CD1 1 
ATOM   745  C  CD2 . TYR A 1 93 ? 15.496  -19.638 -2.664  1.00 45.96  ? 92  TYR A CD2 1 
ATOM   746  C  CE1 . TYR A 1 93 ? 16.314  -21.244 -0.558  1.00 47.07  ? 92  TYR A CE1 1 
ATOM   747  C  CE2 . TYR A 1 93 ? 15.580  -19.111 -1.377  1.00 49.17  ? 92  TYR A CE2 1 
ATOM   748  C  CZ  . TYR A 1 93 ? 16.015  -19.909 -0.328  1.00 47.28  ? 92  TYR A CZ  1 
ATOM   749  O  OH  . TYR A 1 93 ? 16.140  -19.416 0.942   1.00 49.39  ? 92  TYR A OH  1 
ATOM   750  N  N   . SER A 1 94 ? 18.083  -22.107 -7.172  1.00 69.70  ? 93  SER A N   1 
ATOM   751  C  CA  . SER A 1 94 ? 18.622  -23.081 -8.111  1.00 83.20  ? 93  SER A CA  1 
ATOM   752  C  C   . SER A 1 94 ? 19.470  -24.106 -7.336  1.00 88.67  ? 93  SER A C   1 
ATOM   753  O  O   . SER A 1 94 ? 20.712  -23.923 -7.294  1.00 89.67  ? 93  SER A O   1 
ATOM   754  C  CB  . SER A 1 94 ? 19.419  -22.423 -9.221  1.00 81.18  ? 93  SER A CB  1 
ATOM   755  O  OG  . SER A 1 94 ? 18.573  -21.732 -10.133 1.00 76.92  ? 93  SER A OG  1 
ATOM   756  O  OXT . SER A 1 94 ? 18.853  -25.045 -6.777  1.00 89.19  ? 93  SER A OXT 1 
ATOM   757  N  N   . MET B 1 2  ? 38.812  -10.771 -42.793 1.00 73.66  ? 1   MET B N   1 
ATOM   758  C  CA  . MET B 1 2  ? 38.554  -11.826 -43.809 1.00 75.39  ? 1   MET B CA  1 
ATOM   759  C  C   . MET B 1 2  ? 37.066  -12.166 -43.788 1.00 68.10  ? 1   MET B C   1 
ATOM   760  O  O   . MET B 1 2  ? 36.572  -12.649 -42.774 1.00 70.10  ? 1   MET B O   1 
ATOM   761  C  CB  . MET B 1 2  ? 39.370  -13.087 -43.500 1.00 78.88  ? 1   MET B CB  1 
ATOM   762  C  CG  . MET B 1 2  ? 39.582  -13.990 -44.699 1.00 90.64  ? 1   MET B CG  1 
ATOM   763  S  SD  . MET B 1 2  ? 40.451  -13.171 -46.055 1.00 86.01  ? 1   MET B SD  1 
ATOM   764  C  CE  . MET B 1 2  ? 41.931  -12.484 -45.298 1.00 79.80  ? 1   MET B CE  1 
ATOM   765  N  N   . PRO B 1 3  ? 36.308  -11.921 -44.884 1.00 64.42  ? 2   PRO B N   1 
ATOM   766  C  CA  . PRO B 1 3  ? 34.852  -12.064 -44.855 1.00 59.58  ? 2   PRO B CA  1 
ATOM   767  C  C   . PRO B 1 3  ? 34.517  -13.506 -44.508 1.00 53.91  ? 2   PRO B C   1 
ATOM   768  O  O   . PRO B 1 3  ? 35.285  -14.414 -44.793 1.00 57.68  ? 2   PRO B O   1 
ATOM   769  C  CB  . PRO B 1 3  ? 34.389  -11.687 -46.279 1.00 53.98  ? 2   PRO B CB  1 
ATOM   770  C  CG  . PRO B 1 3  ? 35.555  -10.916 -46.851 1.00 60.32  ? 2   PRO B CG  1 
ATOM   771  C  CD  . PRO B 1 3  ? 36.800  -11.518 -46.212 1.00 64.03  ? 2   PRO B CD  1 
ATOM   772  N  N   . HIS B 1 4  ? 33.367  -13.695 -43.871 1.00 55.20  ? 3   HIS B N   1 
ATOM   773  C  CA  . HIS B 1 4  ? 32.919  -15.026 -43.529 1.00 58.23  ? 3   HIS B CA  1 
ATOM   774  C  C   . HIS B 1 4  ? 31.492  -15.137 -44.026 1.00 57.27  ? 3   HIS B C   1 
ATOM   775  O  O   . HIS B 1 4  ? 30.899  -14.123 -44.385 1.00 57.10  ? 3   HIS B O   1 
ATOM   776  C  CB  . HIS B 1 4  ? 33.105  -15.334 -42.038 1.00 61.96  ? 3   HIS B CB  1 
ATOM   777  C  CG  . HIS B 1 4  ? 34.524  -15.629 -41.676 1.00 81.52  ? 3   HIS B CG  1 
ATOM   778  N  ND1 . HIS B 1 4  ? 35.198  -16.734 -42.160 1.00 89.86  ? 3   HIS B ND1 1 
ATOM   779  C  CD2 . HIS B 1 4  ? 35.408  -14.957 -40.924 1.00 80.79  ? 3   HIS B CD2 1 
ATOM   780  C  CE1 . HIS B 1 4  ? 36.437  -16.733 -41.691 1.00 87.39  ? 3   HIS B CE1 1 
ATOM   781  N  NE2 . HIS B 1 4  ? 36.587  -15.663 -40.940 1.00 85.24  ? 3   HIS B NE2 1 
ATOM   782  N  N   . ALA B 1 5  ? 31.005  -16.379 -44.086 1.00 51.74  ? 4   ALA B N   1 
ATOM   783  C  CA  . ALA B 1 5  ? 29.631  -16.687 -44.448 1.00 55.20  ? 4   ALA B CA  1 
ATOM   784  C  C   . ALA B 1 5  ? 28.710  -15.595 -43.918 1.00 49.19  ? 4   ALA B C   1 
ATOM   785  O  O   . ALA B 1 5  ? 27.857  -15.096 -44.647 1.00 55.71  ? 4   ALA B O   1 
ATOM   786  C  CB  . ALA B 1 5  ? 29.262  -18.041 -43.869 1.00 48.35  ? 4   ALA B CB  1 
ATOM   787  N  N   . PHE B 1 6  ? 28.892  -15.272 -42.633 1.00 58.01  ? 5   PHE B N   1 
ATOM   788  C  CA  . PHE B 1 6  ? 28.132  -14.262 -41.903 1.00 64.00  ? 5   PHE B CA  1 
ATOM   789  C  C   . PHE B 1 6  ? 28.952  -12.978 -41.810 1.00 51.44  ? 5   PHE B C   1 
ATOM   790  O  O   . PHE B 1 6  ? 30.177  -13.006 -41.698 1.00 57.56  ? 5   PHE B O   1 
ATOM   791  C  CB  . PHE B 1 6  ? 27.669  -14.775 -40.527 1.00 53.03  ? 5   PHE B CB  1 
ATOM   792  C  CG  . PHE B 1 6  ? 26.603  -15.859 -40.627 1.00 48.40  ? 5   PHE B CG  1 
ATOM   793  C  CD1 . PHE B 1 6  ? 25.257  -15.525 -40.736 1.00 46.77  ? 5   PHE B CD1 1 
ATOM   794  C  CD2 . PHE B 1 6  ? 26.953  -17.206 -40.638 1.00 45.22  ? 5   PHE B CD2 1 
ATOM   795  C  CE1 . PHE B 1 6  ? 24.284  -16.496 -40.834 1.00 39.70  ? 5   PHE B CE1 1 
ATOM   796  C  CE2 . PHE B 1 6  ? 25.973  -18.182 -40.752 1.00 47.31  ? 5   PHE B CE2 1 
ATOM   797  C  CZ  . PHE B 1 6  ? 24.644  -17.825 -40.856 1.00 45.24  ? 5   PHE B CZ  1 
ATOM   798  N  N   . LYS B 1 7  ? 28.265  -11.844 -41.865 1.00 54.88  ? 6   LYS B N   1 
ATOM   799  C  CA  . LYS B 1 7  ? 28.972  -10.579 -41.793 1.00 59.84  ? 6   LYS B CA  1 
ATOM   800  C  C   . LYS B 1 7  ? 28.217  -9.634  -40.853 1.00 62.27  ? 6   LYS B C   1 
ATOM   801  O  O   . LYS B 1 7  ? 26.977  -9.597  -40.848 1.00 61.91  ? 6   LYS B O   1 
ATOM   802  C  CB  . LYS B 1 7  ? 29.251  -10.094 -43.225 1.00 63.77  ? 6   LYS B CB  1 
ATOM   803  C  CG  . LYS B 1 7  ? 28.074  -9.439  -43.929 1.00 63.49  ? 6   LYS B CG  1 
ATOM   804  C  CD  . LYS B 1 7  ? 27.908  -9.719  -45.414 1.00 63.47  ? 6   LYS B CD  1 
ATOM   805  C  CE  . LYS B 1 7  ? 26.801  -8.857  -45.932 1.00 62.94  ? 6   LYS B CE  1 
ATOM   806  N  NZ  . LYS B 1 7  ? 25.877  -9.606  -46.794 1.00 65.09  ? 6   LYS B NZ  1 
ATOM   807  N  N   . PRO B 1 8  ? 28.956  -8.850  -40.032 1.00 60.67  ? 7   PRO B N   1 
ATOM   808  C  CA  . PRO B 1 8  ? 28.348  -7.902  -39.097 1.00 55.75  ? 7   PRO B CA  1 
ATOM   809  C  C   . PRO B 1 8  ? 27.221  -7.145  -39.787 1.00 55.46  ? 7   PRO B C   1 
ATOM   810  O  O   . PRO B 1 8  ? 27.457  -6.388  -40.723 1.00 66.94  ? 7   PRO B O   1 
ATOM   811  C  CB  . PRO B 1 8  ? 29.560  -7.008  -38.807 1.00 60.85  ? 7   PRO B CB  1 
ATOM   812  C  CG  . PRO B 1 8  ? 30.710  -8.005  -38.744 1.00 64.17  ? 7   PRO B CG  1 
ATOM   813  C  CD  . PRO B 1 8  ? 30.432  -8.819  -39.994 1.00 57.42  ? 7   PRO B CD  1 
ATOM   814  N  N   . GLY B 1 9  ? 25.987  -7.395  -39.344 1.00 55.09  ? 8   GLY B N   1 
ATOM   815  C  CA  . GLY B 1 9  ? 24.839  -6.771  -39.976 1.00 40.27  ? 8   GLY B CA  1 
ATOM   816  C  C   . GLY B 1 9  ? 23.819  -7.813  -40.379 1.00 43.27  ? 8   GLY B C   1 
ATOM   817  O  O   . GLY B 1 9  ? 22.610  -7.541  -40.422 1.00 40.21  ? 8   GLY B O   1 
ATOM   818  N  N   . ASP B 1 10 ? 24.311  -9.029  -40.630 1.00 38.87  ? 9   ASP B N   1 
ATOM   819  C  CA  . ASP B 1 10 ? 23.367  -10.051 -41.045 1.00 47.73  ? 9   ASP B CA  1 
ATOM   820  C  C   . ASP B 1 10 ? 22.307  -10.206 -39.956 1.00 44.51  ? 9   ASP B C   1 
ATOM   821  O  O   . ASP B 1 10 ? 22.647  -10.231 -38.784 1.00 44.62  ? 9   ASP B O   1 
ATOM   822  C  CB  . ASP B 1 10 ? 24.074  -11.304 -41.532 1.00 50.39  ? 9   ASP B CB  1 
ATOM   823  C  CG  . ASP B 1 10 ? 24.828  -11.095 -42.837 1.00 55.06  ? 9   ASP B CG  1 
ATOM   824  O  OD1 . ASP B 1 10 ? 24.178  -10.623 -43.785 1.00 45.16  ? 9   ASP B OD1 1 
ATOM   825  O  OD2 . ASP B 1 10 ? 26.049  -11.367 -42.867 1.00 60.72  ? 9   ASP B OD2 1 
ATOM   826  N  N   . LEU B 1 11 ? 21.034  -10.202 -40.361 1.00 45.49  ? 10  LEU B N   1 
ATOM   827  C  CA  . LEU B 1 11 ? 19.923  -10.549 -39.490 1.00 40.55  ? 10  LEU B CA  1 
ATOM   828  C  C   . LEU B 1 11 ? 19.638  -12.047 -39.621 1.00 38.47  ? 10  LEU B C   1 
ATOM   829  O  O   . LEU B 1 11 ? 19.526  -12.556 -40.743 1.00 41.47  ? 10  LEU B O   1 
ATOM   830  C  CB  . LEU B 1 11 ? 18.677  -9.782  -39.925 1.00 35.43  ? 10  LEU B CB  1 
ATOM   831  C  CG  . LEU B 1 11 ? 18.901  -8.433  -40.616 1.00 34.01  ? 10  LEU B CG  1 
ATOM   832  C  CD1 . LEU B 1 11 ? 17.631  -7.584  -40.558 1.00 30.09  ? 10  LEU B CD1 1 
ATOM   833  C  CD2 . LEU B 1 11 ? 20.093  -7.653  -40.160 1.00 38.40  ? 10  LEU B CD2 1 
ATOM   834  N  N   . VAL B 1 12 ? 19.462  -12.703 -38.468 1.00 37.30  ? 11  VAL B N   1 
ATOM   835  C  CA  . VAL B 1 12 ? 19.132  -14.120 -38.373 1.00 39.41  ? 11  VAL B CA  1 
ATOM   836  C  C   . VAL B 1 12 ? 17.982  -14.327 -37.391 1.00 41.93  ? 11  VAL B C   1 
ATOM   837  O  O   . VAL B 1 12 ? 17.616  -13.442 -36.609 1.00 43.66  ? 11  VAL B O   1 
ATOM   838  C  CB  . VAL B 1 12 ? 20.394  -14.830 -37.843 1.00 37.31  ? 11  VAL B CB  1 
ATOM   839  C  CG1 . VAL B 1 12 ? 21.525  -14.753 -38.868 1.00 39.28  ? 11  VAL B CG1 1 
ATOM   840  C  CG2 . VAL B 1 12 ? 20.833  -14.284 -36.494 1.00 38.14  ? 11  VAL B CG2 1 
ATOM   841  N  N   . PHE B 1 13 ? 17.439  -15.544 -37.395 1.00 38.47  ? 12  PHE B N   1 
ATOM   842  C  CA  . PHE B 1 13 ? 17.028  -16.111 -36.121 1.00 34.11  ? 12  PHE B CA  1 
ATOM   843  C  C   . PHE B 1 13 ? 18.151  -16.961 -35.536 1.00 36.74  ? 12  PHE B C   1 
ATOM   844  O  O   . PHE B 1 13 ? 18.748  -17.765 -36.241 1.00 37.53  ? 12  PHE B O   1 
ATOM   845  C  CB  . PHE B 1 13 ? 15.761  -16.948 -36.207 1.00 34.06  ? 12  PHE B CB  1 
ATOM   846  C  CG  . PHE B 1 13 ? 14.549  -16.122 -36.584 1.00 38.34  ? 12  PHE B CG  1 
ATOM   847  C  CD1 . PHE B 1 13 ? 14.445  -15.560 -37.854 1.00 49.72  ? 12  PHE B CD1 1 
ATOM   848  C  CD2 . PHE B 1 13 ? 13.495  -15.987 -35.711 1.00 42.36  ? 12  PHE B CD2 1 
ATOM   849  C  CE1 . PHE B 1 13 ? 13.321  -14.844 -38.231 1.00 51.08  ? 12  PHE B CE1 1 
ATOM   850  C  CE2 . PHE B 1 13 ? 12.369  -15.271 -36.092 1.00 58.00  ? 12  PHE B CE2 1 
ATOM   851  C  CZ  . PHE B 1 13 ? 12.283  -14.700 -37.346 1.00 56.67  ? 12  PHE B CZ  1 
ATOM   852  N  N   . ALA B 1 14 ? 18.413  -16.779 -34.235 1.00 40.63  ? 13  ALA B N   1 
ATOM   853  C  CA  . ALA B 1 14 ? 19.374  -17.568 -33.481 1.00 42.08  ? 13  ALA B CA  1 
ATOM   854  C  C   . ALA B 1 14 ? 18.616  -18.465 -32.508 1.00 41.68  ? 13  ALA B C   1 
ATOM   855  O  O   . ALA B 1 14 ? 17.518  -18.090 -32.079 1.00 39.58  ? 13  ALA B O   1 
ATOM   856  C  CB  . ALA B 1 14 ? 20.363  -16.668 -32.771 1.00 39.78  ? 13  ALA B CB  1 
ATOM   857  N  N   . LYS B 1 15 ? 19.139  -19.687 -32.329 1.00 39.59  ? 14  LYS B N   1 
ATOM   858  C  CA  . LYS B 1 15 ? 18.560  -20.764 -31.533 1.00 41.12  ? 14  LYS B CA  1 
ATOM   859  C  C   . LYS B 1 15 ? 19.502  -21.127 -30.390 1.00 42.82  ? 14  LYS B C   1 
ATOM   860  O  O   . LYS B 1 15 ? 20.677  -21.411 -30.625 1.00 49.62  ? 14  LYS B O   1 
ATOM   861  C  CB  . LYS B 1 15 ? 18.407  -22.045 -32.364 1.00 37.45  ? 14  LYS B CB  1 
ATOM   862  C  CG  . LYS B 1 15 ? 17.612  -23.165 -31.720 1.00 36.73  ? 14  LYS B CG  1 
ATOM   863  C  CD  . LYS B 1 15 ? 16.131  -22.788 -31.602 1.00 39.46  ? 14  LYS B CD  1 
ATOM   864  C  CE  . LYS B 1 15 ? 15.266  -23.856 -30.966 1.00 43.48  ? 14  LYS B CE  1 
ATOM   865  N  NZ  . LYS B 1 15 ? 15.638  -24.128 -29.566 1.00 37.52  ? 14  LYS B NZ  1 
ATOM   866  N  N   . MET B 1 16 ? 18.947  -21.122 -29.171 1.00 48.53  ? 15  MET B N   1 
ATOM   867  C  CA  . MET B 1 16 ? 19.540  -21.628 -27.939 1.00 46.86  ? 15  MET B CA  1 
ATOM   868  C  C   . MET B 1 16 ? 18.550  -22.607 -27.313 1.00 51.72  ? 15  MET B C   1 
ATOM   869  O  O   . MET B 1 16 ? 17.332  -22.383 -27.396 1.00 49.80  ? 15  MET B O   1 
ATOM   870  C  CB  . MET B 1 16 ? 19.701  -20.503 -26.904 1.00 46.89  ? 15  MET B CB  1 
ATOM   871  C  CG  . MET B 1 16 ? 20.299  -19.195 -27.402 1.00 49.47  ? 15  MET B CG  1 
ATOM   872  S  SD  . MET B 1 16 ? 22.042  -18.954 -27.000 1.00 59.30  ? 15  MET B SD  1 
ATOM   873  C  CE  . MET B 1 16 ? 22.028  -18.489 -25.267 1.00 62.63  ? 15  MET B CE  1 
ATOM   874  N  N   . LYS B 1 17 ? 19.081  -23.669 -26.675 1.00 55.09  ? 16  LYS B N   1 
ATOM   875  C  CA  . LYS B 1 17 ? 18.298  -24.627 -25.893 1.00 50.97  ? 16  LYS B CA  1 
ATOM   876  C  C   . LYS B 1 17 ? 17.405  -23.865 -24.913 1.00 48.02  ? 16  LYS B C   1 
ATOM   877  O  O   . LYS B 1 17 ? 17.881  -22.973 -24.208 1.00 45.11  ? 16  LYS B O   1 
ATOM   878  C  CB  . LYS B 1 17 ? 19.240  -25.594 -25.157 1.00 54.03  ? 16  LYS B CB  1 
ATOM   879  C  CG  . LYS B 1 17 ? 18.803  -27.064 -25.060 1.00 57.85  ? 16  LYS B CG  1 
ATOM   880  C  CD  . LYS B 1 17 ? 19.039  -27.742 -23.710 1.00 65.22  ? 16  LYS B CD  1 
ATOM   881  N  N   . GLY B 1 18 ? 16.096  -24.161 -24.929 1.00 53.19  ? 17  GLY B N   1 
ATOM   882  C  CA  . GLY B 1 18 ? 15.151  -23.628 -23.946 1.00 47.82  ? 17  GLY B CA  1 
ATOM   883  C  C   . GLY B 1 18 ? 14.293  -22.499 -24.504 1.00 47.26  ? 17  GLY B C   1 
ATOM   884  O  O   . GLY B 1 18 ? 13.370  -21.984 -23.860 1.00 45.38  ? 17  GLY B O   1 
ATOM   885  N  N   . TYR B 1 19 ? 14.595  -22.120 -25.743 1.00 48.23  ? 18  TYR B N   1 
ATOM   886  C  CA  . TYR B 1 19 ? 14.096  -20.864 -26.268 1.00 48.92  ? 18  TYR B CA  1 
ATOM   887  C  C   . TYR B 1 19 ? 13.692  -21.072 -27.719 1.00 46.03  ? 18  TYR B C   1 
ATOM   888  O  O   . TYR B 1 19 ? 14.344  -21.827 -28.436 1.00 49.54  ? 18  TYR B O   1 
ATOM   889  C  CB  . TYR B 1 19 ? 15.235  -19.854 -26.106 1.00 41.12  ? 18  TYR B CB  1 
ATOM   890  C  CG  . TYR B 1 19 ? 15.673  -19.542 -24.690 1.00 46.58  ? 18  TYR B CG  1 
ATOM   891  C  CD1 . TYR B 1 19 ? 14.918  -18.696 -23.872 1.00 42.35  ? 18  TYR B CD1 1 
ATOM   892  C  CD2 . TYR B 1 19 ? 16.849  -20.082 -24.170 1.00 49.63  ? 18  TYR B CD2 1 
ATOM   893  C  CE1 . TYR B 1 19 ? 15.305  -18.416 -22.573 1.00 39.47  ? 18  TYR B CE1 1 
ATOM   894  C  CE2 . TYR B 1 19 ? 17.256  -19.786 -22.876 1.00 54.05  ? 18  TYR B CE2 1 
ATOM   895  C  CZ  . TYR B 1 19 ? 16.489  -18.945 -22.081 1.00 43.70  ? 18  TYR B CZ  1 
ATOM   896  O  OH  . TYR B 1 19 ? 16.882  -18.664 -20.800 1.00 52.82  ? 18  TYR B OH  1 
ATOM   897  N  N   . PRO B 1 20 ? 12.619  -20.405 -28.195 1.00 41.20  ? 19  PRO B N   1 
ATOM   898  C  CA  . PRO B 1 20 ? 12.318  -20.392 -29.622 1.00 38.86  ? 19  PRO B CA  1 
ATOM   899  C  C   . PRO B 1 20 ? 13.469  -19.715 -30.366 1.00 36.94  ? 19  PRO B C   1 
ATOM   900  O  O   . PRO B 1 20 ? 14.206  -18.925 -29.766 1.00 24.06  ? 19  PRO B O   1 
ATOM   901  C  CB  . PRO B 1 20 ? 11.020  -19.585 -29.707 1.00 36.80  ? 19  PRO B CB  1 
ATOM   902  C  CG  . PRO B 1 20 ? 11.079  -18.681 -28.486 1.00 48.41  ? 19  PRO B CG  1 
ATOM   903  C  CD  . PRO B 1 20 ? 11.703  -19.560 -27.411 1.00 49.46  ? 19  PRO B CD  1 
ATOM   904  N  N   . HIS B 1 21 ? 13.548  -20.030 -31.668 1.00 38.46  ? 20  HIS B N   1 
ATOM   905  C  CA  . HIS B 1 21 ? 14.333  -19.316 -32.664 1.00 44.04  ? 20  HIS B CA  1 
ATOM   906  C  C   . HIS B 1 21 ? 14.148  -17.817 -32.438 1.00 43.95  ? 20  HIS B C   1 
ATOM   907  O  O   . HIS B 1 21 ? 13.025  -17.287 -32.361 1.00 34.71  ? 20  HIS B O   1 
ATOM   908  C  CB  . HIS B 1 21 ? 13.990  -19.793 -34.084 1.00 38.54  ? 20  HIS B CB  1 
ATOM   909  C  CG  . HIS B 1 21 ? 14.225  -21.275 -34.268 1.00 42.14  ? 20  HIS B CG  1 
ATOM   910  N  ND1 . HIS B 1 21 ? 13.311  -22.252 -33.919 1.00 43.41  ? 20  HIS B ND1 1 
ATOM   911  C  CD2 . HIS B 1 21 ? 15.300  -21.934 -34.732 1.00 39.46  ? 20  HIS B CD2 1 
ATOM   912  C  CE1 . HIS B 1 21 ? 13.804  -23.450 -34.209 1.00 43.54  ? 20  HIS B CE1 1 
ATOM   913  N  NE2 . HIS B 1 21 ? 15.020  -23.279 -34.707 1.00 42.14  ? 20  HIS B NE2 1 
ATOM   914  N  N   . TRP B 1 22 ? 15.265  -17.122 -32.254 1.00 27.51  ? 21  TRP B N   1 
ATOM   915  C  CA  . TRP B 1 22 ? 15.061  -15.787 -31.715 1.00 37.56  ? 21  TRP B CA  1 
ATOM   916  C  C   . TRP B 1 22 ? 15.591  -14.667 -32.628 1.00 42.71  ? 21  TRP B C   1 
ATOM   917  O  O   . TRP B 1 22 ? 16.750  -14.711 -33.054 1.00 43.07  ? 21  TRP B O   1 
ATOM   918  C  CB  . TRP B 1 22 ? 15.647  -15.723 -30.295 1.00 38.15  ? 21  TRP B CB  1 
ATOM   919  C  CG  . TRP B 1 22 ? 15.190  -14.523 -29.500 1.00 42.78  ? 21  TRP B CG  1 
ATOM   920  C  CD1 . TRP B 1 22 ? 15.566  -13.222 -29.686 1.00 39.75  ? 21  TRP B CD1 1 
ATOM   921  C  CD2 . TRP B 1 22 ? 14.285  -14.523 -28.371 1.00 44.46  ? 21  TRP B CD2 1 
ATOM   922  N  NE1 . TRP B 1 22 ? 14.956  -12.418 -28.756 1.00 41.68  ? 21  TRP B NE1 1 
ATOM   923  C  CE2 . TRP B 1 22 ? 14.178  -13.180 -27.928 1.00 41.44  ? 21  TRP B CE2 1 
ATOM   924  C  CE3 . TRP B 1 22 ? 13.592  -15.525 -27.673 1.00 39.76  ? 21  TRP B CE3 1 
ATOM   925  C  CZ2 . TRP B 1 22 ? 13.394  -12.812 -26.836 1.00 42.32  ? 21  TRP B CZ2 1 
ATOM   926  C  CZ3 . TRP B 1 22 ? 12.826  -15.157 -26.581 1.00 40.44  ? 21  TRP B CZ3 1 
ATOM   927  C  CH2 . TRP B 1 22 ? 12.747  -13.822 -26.161 1.00 41.66  ? 21  TRP B CH2 1 
ATOM   928  N  N   . PRO B 1 23 ? 14.801  -13.597 -32.910 1.00 36.81  ? 22  PRO B N   1 
ATOM   929  C  CA  . PRO B 1 23 ? 15.252  -12.493 -33.785 1.00 37.32  ? 22  PRO B CA  1 
ATOM   930  C  C   . PRO B 1 23 ? 16.562  -11.951 -33.237 1.00 30.55  ? 22  PRO B C   1 
ATOM   931  O  O   . PRO B 1 23 ? 16.656  -11.692 -32.049 1.00 44.76  ? 22  PRO B O   1 
ATOM   932  C  CB  . PRO B 1 23 ? 14.139  -11.454 -33.689 1.00 39.26  ? 22  PRO B CB  1 
ATOM   933  C  CG  . PRO B 1 23 ? 13.387  -11.852 -32.440 1.00 39.92  ? 22  PRO B CG  1 
ATOM   934  C  CD  . PRO B 1 23 ? 13.433  -13.366 -32.400 1.00 36.49  ? 22  PRO B CD  1 
ATOM   935  N  N   . ALA B 1 24 ? 17.586  -11.839 -34.073 1.00 33.48  ? 23  ALA B N   1 
ATOM   936  C  CA  . ALA B 1 24 ? 18.933  -11.637 -33.550 1.00 30.43  ? 23  ALA B CA  1 
ATOM   937  C  C   . ALA B 1 24 ? 19.825  -11.034 -34.626 1.00 36.39  ? 23  ALA B C   1 
ATOM   938  O  O   . ALA B 1 24 ? 19.434  -11.034 -35.800 1.00 42.40  ? 23  ALA B O   1 
ATOM   939  C  CB  . ALA B 1 24 ? 19.451  -12.955 -33.049 1.00 37.93  ? 23  ALA B CB  1 
ATOM   940  N  N   . ARG B 1 25 ? 21.062  -10.590 -34.298 1.00 29.13  ? 24  ARG B N   1 
ATOM   941  C  CA  . ARG B 1 25 ? 21.801  -10.055 -35.445 1.00 33.84  ? 24  ARG B CA  1 
ATOM   942  C  C   . ARG B 1 25 ? 23.263  -10.345 -35.162 1.00 36.28  ? 24  ARG B C   1 
ATOM   943  O  O   . ARG B 1 25 ? 23.526  -10.657 -34.032 1.00 31.59  ? 24  ARG B O   1 
ATOM   944  C  CB  . ARG B 1 25 ? 21.652  -8.554  -35.699 1.00 42.32  ? 24  ARG B CB  1 
ATOM   945  C  CG  . ARG B 1 25 ? 22.378  -7.629  -34.729 1.00 44.66  ? 24  ARG B CG  1 
ATOM   946  C  CD  . ARG B 1 25 ? 22.064  -6.132  -34.883 1.00 44.11  ? 24  ARG B CD  1 
ATOM   947  N  NE  . ARG B 1 25 ? 22.728  -5.390  -33.814 1.00 44.53  ? 24  ARG B NE  1 
ATOM   948  C  CZ  . ARG B 1 25 ? 22.429  -4.185  -33.331 1.00 46.74  ? 24  ARG B CZ  1 
ATOM   949  N  NH1 . ARG B 1 25 ? 21.456  -3.484  -33.883 1.00 47.09  ? 24  ARG B NH1 1 
ATOM   950  N  NH2 . ARG B 1 25 ? 23.084  -3.715  -32.274 1.00 36.54  ? 24  ARG B NH2 1 
ATOM   951  N  N   . ILE B 1 26 ? 24.130  -10.358 -36.180 1.00 47.00  ? 25  ILE B N   1 
ATOM   952  C  CA  . ILE B 1 26 ? 25.567  -10.561 -36.015 1.00 41.06  ? 25  ILE B CA  1 
ATOM   953  C  C   . ILE B 1 26 ? 26.151  -9.190  -35.694 1.00 49.40  ? 25  ILE B C   1 
ATOM   954  O  O   . ILE B 1 26 ? 25.953  -8.264  -36.483 1.00 48.51  ? 25  ILE B O   1 
ATOM   955  C  CB  . ILE B 1 26 ? 26.203  -11.081 -37.322 1.00 42.43  ? 25  ILE B CB  1 
ATOM   956  C  CG1 . ILE B 1 26 ? 25.471  -12.259 -37.909 1.00 38.54  ? 25  ILE B CG1 1 
ATOM   957  C  CG2 . ILE B 1 26 ? 27.707  -11.355 -37.169 1.00 43.36  ? 25  ILE B CG2 1 
ATOM   958  C  CD1 . ILE B 1 26 ? 25.470  -13.482 -37.016 1.00 37.09  ? 25  ILE B CD1 1 
ATOM   959  N  N   . ASP B 1 27 ? 26.903  -9.101  -34.589 1.00 47.41  ? 26  ASP B N   1 
ATOM   960  C  CA  . ASP B 1 27 ? 27.528  -7.869  -34.125 1.00 53.97  ? 26  ASP B CA  1 
ATOM   961  C  C   . ASP B 1 27 ? 28.998  -7.822  -34.539 1.00 55.79  ? 26  ASP B C   1 
ATOM   962  O  O   . ASP B 1 27 ? 29.513  -8.793  -35.098 1.00 46.98  ? 26  ASP B O   1 
ATOM   963  C  CB  . ASP B 1 27 ? 27.475  -7.758  -32.611 1.00 49.77  ? 26  ASP B CB  1 
ATOM   964  C  CG  . ASP B 1 27 ? 26.231  -7.117  -32.013 1.00 52.93  ? 26  ASP B CG  1 
ATOM   965  O  OD1 . ASP B 1 27 ? 25.350  -6.706  -32.787 1.00 57.18  ? 26  ASP B OD1 1 
ATOM   966  O  OD2 . ASP B 1 27 ? 26.177  -6.997  -30.769 1.00 52.02  ? 26  ASP B OD2 1 
ATOM   967  N  N   A ASP B 1 28 ? 29.639  -6.703  -34.173 0.50 57.25  ? 27  ASP B N   1 
ATOM   968  N  N   B ASP B 1 28 ? 29.644  -6.675  -34.264 0.50 60.39  ? 27  ASP B N   1 
ATOM   969  C  CA  A ASP B 1 28 ? 31.018  -6.355  -34.473 0.50 56.52  ? 27  ASP B CA  1 
ATOM   970  C  CA  B ASP B 1 28 ? 31.057  -6.429  -34.525 0.50 62.64  ? 27  ASP B CA  1 
ATOM   971  C  C   A ASP B 1 28 ? 31.886  -6.773  -33.288 0.50 62.54  ? 27  ASP B C   1 
ATOM   972  C  C   B ASP B 1 28 ? 31.896  -6.813  -33.309 0.50 66.48  ? 27  ASP B C   1 
ATOM   973  O  O   A ASP B 1 28 ? 31.393  -7.417  -32.365 0.50 64.92  ? 27  ASP B O   1 
ATOM   974  O  O   B ASP B 1 28 ? 31.395  -7.455  -32.388 0.50 68.38  ? 27  ASP B O   1 
ATOM   975  C  CB  A ASP B 1 28 ? 31.080  -4.866  -34.776 0.50 50.22  ? 27  ASP B CB  1 
ATOM   976  C  CB  B ASP B 1 28 ? 31.307  -4.984  -34.932 0.50 62.86  ? 27  ASP B CB  1 
ATOM   977  C  CG  A ASP B 1 28 ? 29.763  -4.305  -35.298 0.50 44.74  ? 27  ASP B CG  1 
ATOM   978  C  CG  B ASP B 1 28 ? 31.546  -4.754  -36.417 0.50 60.78  ? 27  ASP B CG  1 
ATOM   979  O  OD1 A ASP B 1 28 ? 29.748  -3.714  -36.406 0.50 47.02  ? 27  ASP B OD1 1 
ATOM   980  O  OD1 B ASP B 1 28 ? 32.702  -4.932  -36.856 0.50 57.23  ? 27  ASP B OD1 1 
ATOM   981  O  OD2 A ASP B 1 28 ? 28.753  -4.494  -34.602 0.50 33.58  ? 27  ASP B OD2 1 
ATOM   982  O  OD2 B ASP B 1 28 ? 30.572  -4.421  -37.126 0.50 60.62  ? 27  ASP B OD2 1 
ATOM   983  N  N   . ILE B 1 29 ? 33.177  -6.417  -33.337 1.00 68.60  ? 28  ILE B N   1 
ATOM   984  C  CA  . ILE B 1 29 ? 34.138  -6.722  -32.285 1.00 66.38  ? 28  ILE B CA  1 
ATOM   985  C  C   . ILE B 1 29 ? 35.265  -5.674  -32.337 1.00 71.51  ? 28  ILE B C   1 
ATOM   986  O  O   . ILE B 1 29 ? 35.231  -4.742  -31.498 1.00 81.15  ? 28  ILE B O   1 
ATOM   987  C  CB  . ILE B 1 29 ? 34.701  -8.146  -32.446 1.00 64.59  ? 28  ILE B CB  1 
ATOM   988  N  N   . LYS B 1 35 ? 36.607  -11.234 -28.223 1.00 82.53  ? 34  LYS B N   1 
ATOM   989  C  CA  . LYS B 1 35 ? 36.706  -12.141 -29.403 1.00 76.98  ? 34  LYS B CA  1 
ATOM   990  C  C   . LYS B 1 35 ? 35.891  -13.414 -29.151 1.00 79.73  ? 34  LYS B C   1 
ATOM   991  O  O   . LYS B 1 35 ? 35.907  -13.948 -28.039 1.00 83.39  ? 34  LYS B O   1 
ATOM   992  C  CB  . LYS B 1 35 ? 38.174  -12.420 -29.753 1.00 62.51  ? 34  LYS B CB  1 
ATOM   993  N  N   . PRO B 1 36 ? 35.129  -13.921 -30.158 1.00 80.65  ? 35  PRO B N   1 
ATOM   994  C  CA  . PRO B 1 36 ? 34.450  -15.216 -30.041 1.00 74.33  ? 35  PRO B CA  1 
ATOM   995  C  C   . PRO B 1 36 ? 35.407  -16.407 -30.044 1.00 72.01  ? 35  PRO B C   1 
ATOM   996  O  O   . PRO B 1 36 ? 36.544  -16.293 -30.506 1.00 74.62  ? 35  PRO B O   1 
ATOM   997  C  CB  . PRO B 1 36 ? 33.525  -15.224 -31.269 1.00 75.38  ? 35  PRO B CB  1 
ATOM   998  C  CG  . PRO B 1 36 ? 34.246  -14.368 -32.279 1.00 81.30  ? 35  PRO B CG  1 
ATOM   999  C  CD  . PRO B 1 36 ? 34.849  -13.256 -31.444 1.00 79.35  ? 35  PRO B CD  1 
ATOM   1000 N  N   . PRO B 1 37 ? 34.976  -17.586 -29.535 1.00 66.05  ? 36  PRO B N   1 
ATOM   1001 C  CA  . PRO B 1 37 ? 35.778  -18.803 -29.637 1.00 70.26  ? 36  PRO B CA  1 
ATOM   1002 C  C   . PRO B 1 37 ? 35.738  -19.165 -31.119 1.00 76.13  ? 36  PRO B C   1 
ATOM   1003 O  O   . PRO B 1 37 ? 34.857  -18.690 -31.838 1.00 78.61  ? 36  PRO B O   1 
ATOM   1004 C  CB  . PRO B 1 37 ? 35.070  -19.847 -28.748 1.00 70.25  ? 36  PRO B CB  1 
ATOM   1005 C  CG  . PRO B 1 37 ? 33.957  -19.081 -28.051 1.00 72.83  ? 36  PRO B CG  1 
ATOM   1006 C  CD  . PRO B 1 37 ? 33.689  -17.815 -28.857 1.00 75.82  ? 36  PRO B CD  1 
ATOM   1007 N  N   . PRO B 1 38 ? 36.697  -19.974 -31.633 1.00 77.46  ? 37  PRO B N   1 
ATOM   1008 C  CA  . PRO B 1 38 ? 36.727  -20.295 -33.064 1.00 70.86  ? 37  PRO B CA  1 
ATOM   1009 C  C   . PRO B 1 38 ? 35.380  -20.780 -33.602 1.00 64.52  ? 37  PRO B C   1 
ATOM   1010 O  O   . PRO B 1 38 ? 34.627  -21.456 -32.895 1.00 59.21  ? 37  PRO B O   1 
ATOM   1011 C  CB  . PRO B 1 38 ? 37.854  -21.347 -33.155 1.00 66.53  ? 37  PRO B CB  1 
ATOM   1012 C  CG  . PRO B 1 38 ? 38.778  -20.983 -32.015 1.00 70.00  ? 37  PRO B CG  1 
ATOM   1013 C  CD  . PRO B 1 38 ? 37.827  -20.566 -30.891 1.00 72.03  ? 37  PRO B CD  1 
ATOM   1014 N  N   . ASN B 1 39 ? 35.079  -20.376 -34.845 1.00 60.96  ? 38  ASN B N   1 
ATOM   1015 C  CA  . ASN B 1 39 ? 33.905  -20.809 -35.600 1.00 69.64  ? 38  ASN B CA  1 
ATOM   1016 C  C   . ASN B 1 39 ? 32.578  -20.257 -35.056 1.00 65.76  ? 38  ASN B C   1 
ATOM   1017 O  O   . ASN B 1 39 ? 31.514  -20.720 -35.455 1.00 62.87  ? 38  ASN B O   1 
ATOM   1018 C  CB  . ASN B 1 39 ? 33.859  -22.325 -35.780 1.00 75.83  ? 38  ASN B CB  1 
ATOM   1019 C  CG  . ASN B 1 39 ? 34.923  -22.841 -36.722 1.00 80.16  ? 38  ASN B CG  1 
ATOM   1020 O  OD1 . ASN B 1 39 ? 35.398  -23.970 -36.560 1.00 81.21  ? 38  ASN B OD1 1 
ATOM   1021 N  ND2 . ASN B 1 39 ? 35.263  -22.067 -37.744 1.00 76.67  ? 38  ASN B ND2 1 
ATOM   1022 N  N   . LYS B 1 40 ? 32.623  -19.259 -34.163 1.00 66.15  ? 39  LYS B N   1 
ATOM   1023 C  CA  . LYS B 1 40 ? 31.411  -18.727 -33.559 1.00 57.23  ? 39  LYS B CA  1 
ATOM   1024 C  C   . LYS B 1 40 ? 31.351  -17.221 -33.805 1.00 60.37  ? 39  LYS B C   1 
ATOM   1025 O  O   . LYS B 1 40 ? 32.373  -16.583 -34.057 1.00 60.21  ? 39  LYS B O   1 
ATOM   1026 C  CB  . LYS B 1 40 ? 31.294  -19.222 -32.112 1.00 60.59  ? 39  LYS B CB  1 
ATOM   1027 C  CG  . LYS B 1 40 ? 31.417  -20.748 -32.056 1.00 62.49  ? 39  LYS B CG  1 
ATOM   1028 C  CD  . LYS B 1 40 ? 31.511  -21.431 -30.700 1.00 58.05  ? 39  LYS B CD  1 
ATOM   1029 C  CE  . LYS B 1 40 ? 30.168  -21.763 -30.167 1.00 61.69  ? 39  LYS B CE  1 
ATOM   1030 N  NZ  . LYS B 1 40 ? 30.239  -22.414 -28.857 1.00 61.56  ? 39  LYS B NZ  1 
ATOM   1031 N  N   . TYR B 1 41 ? 30.131  -16.675 -33.779 1.00 48.12  ? 40  TYR B N   1 
ATOM   1032 C  CA  . TYR B 1 41 ? 29.906  -15.271 -34.068 1.00 54.53  ? 40  TYR B CA  1 
ATOM   1033 C  C   . TYR B 1 41 ? 29.261  -14.579 -32.868 1.00 54.03  ? 40  TYR B C   1 
ATOM   1034 O  O   . TYR B 1 41 ? 28.471  -15.208 -32.156 1.00 53.02  ? 40  TYR B O   1 
ATOM   1035 C  CB  . TYR B 1 41 ? 28.944  -15.171 -35.255 1.00 60.02  ? 40  TYR B CB  1 
ATOM   1036 C  CG  . TYR B 1 41 ? 29.486  -15.610 -36.609 1.00 64.53  ? 40  TYR B CG  1 
ATOM   1037 C  CD1 . TYR B 1 41 ? 30.118  -14.706 -37.458 1.00 66.04  ? 40  TYR B CD1 1 
ATOM   1038 C  CD2 . TYR B 1 41 ? 29.348  -16.927 -37.044 1.00 70.42  ? 40  TYR B CD2 1 
ATOM   1039 C  CE1 . TYR B 1 41 ? 30.612  -15.102 -38.693 1.00 72.43  ? 40  TYR B CE1 1 
ATOM   1040 C  CE2 . TYR B 1 41 ? 29.834  -17.333 -38.278 1.00 64.61  ? 40  TYR B CE2 1 
ATOM   1041 C  CZ  . TYR B 1 41 ? 30.468  -16.418 -39.104 1.00 71.40  ? 40  TYR B CZ  1 
ATOM   1042 O  OH  . TYR B 1 41 ? 30.916  -16.807 -40.335 1.00 60.71  ? 40  TYR B OH  1 
ATOM   1043 N  N   . PRO B 1 42 ? 29.598  -13.287 -32.596 1.00 52.42  ? 41  PRO B N   1 
ATOM   1044 C  CA  . PRO B 1 42 ? 28.850  -12.457 -31.651 1.00 44.58  ? 41  PRO B CA  1 
ATOM   1045 C  C   . PRO B 1 42 ? 27.445  -12.107 -32.129 1.00 44.74  ? 41  PRO B C   1 
ATOM   1046 O  O   . PRO B 1 42 ? 27.266  -11.475 -33.168 1.00 50.31  ? 41  PRO B O   1 
ATOM   1047 C  CB  . PRO B 1 42 ? 29.733  -11.217 -31.499 1.00 49.20  ? 41  PRO B CB  1 
ATOM   1048 C  CG  . PRO B 1 42 ? 30.473  -11.150 -32.799 1.00 50.11  ? 41  PRO B CG  1 
ATOM   1049 C  CD  . PRO B 1 42 ? 30.794  -12.592 -33.101 1.00 52.41  ? 41  PRO B CD  1 
ATOM   1050 N  N   . ILE B 1 43 ? 26.463  -12.550 -31.344 1.00 48.50  ? 42  ILE B N   1 
ATOM   1051 C  CA  . ILE B 1 43 ? 25.037  -12.422 -31.615 1.00 42.41  ? 42  ILE B CA  1 
ATOM   1052 C  C   . ILE B 1 43 ? 24.470  -11.403 -30.638 1.00 43.48  ? 42  ILE B C   1 
ATOM   1053 O  O   . ILE B 1 43 ? 24.738  -11.515 -29.437 1.00 40.29  ? 42  ILE B O   1 
ATOM   1054 C  CB  . ILE B 1 43 ? 24.381  -13.788 -31.347 1.00 41.35  ? 42  ILE B CB  1 
ATOM   1055 C  CG1 . ILE B 1 43 ? 25.143  -14.972 -32.016 1.00 40.51  ? 42  ILE B CG1 1 
ATOM   1056 C  CG2 . ILE B 1 43 ? 22.873  -13.768 -31.650 1.00 41.15  ? 42  ILE B CG2 1 
ATOM   1057 C  CD1 . ILE B 1 43 ? 25.471  -14.798 -33.484 1.00 44.07  ? 42  ILE B CD1 1 
ATOM   1058 N  N   . PHE B 1 44 ? 23.665  -10.449 -31.144 1.00 43.28  ? 43  PHE B N   1 
ATOM   1059 C  CA  . PHE B 1 44 ? 22.852  -9.635  -30.254 1.00 43.61  ? 43  PHE B CA  1 
ATOM   1060 C  C   . PHE B 1 44 ? 21.420  -10.146 -30.396 1.00 43.49  ? 43  PHE B C   1 
ATOM   1061 O  O   . PHE B 1 44 ? 21.033  -10.468 -31.509 1.00 38.50  ? 43  PHE B O   1 
ATOM   1062 C  CB  . PHE B 1 44 ? 23.012  -8.184  -30.733 1.00 44.28  ? 43  PHE B CB  1 
ATOM   1063 C  CG  . PHE B 1 44 ? 22.107  -7.147  -30.078 1.00 46.20  ? 43  PHE B CG  1 
ATOM   1064 C  CD1 . PHE B 1 44 ? 20.873  -6.818  -30.644 1.00 48.34  ? 43  PHE B CD1 1 
ATOM   1065 C  CD2 . PHE B 1 44 ? 22.469  -6.523  -28.884 1.00 53.85  ? 43  PHE B CD2 1 
ATOM   1066 C  CE1 . PHE B 1 44 ? 20.025  -5.893  -30.046 1.00 43.85  ? 43  PHE B CE1 1 
ATOM   1067 C  CE2 . PHE B 1 44 ? 21.620  -5.600  -28.283 1.00 53.32  ? 43  PHE B CE2 1 
ATOM   1068 C  CZ  . PHE B 1 44 ? 20.401  -5.287  -28.868 1.00 53.67  ? 43  PHE B CZ  1 
ATOM   1069 N  N   . PHE B 1 45 ? 20.658  -10.212 -29.293 1.00 47.46  ? 44  PHE B N   1 
ATOM   1070 C  CA  . PHE B 1 45 ? 19.261  -10.657 -29.285 1.00 42.44  ? 44  PHE B CA  1 
ATOM   1071 C  C   . PHE B 1 45 ? 18.334  -9.441  -29.238 1.00 41.46  ? 44  PHE B C   1 
ATOM   1072 O  O   . PHE B 1 45 ? 18.449  -8.583  -28.375 1.00 42.60  ? 44  PHE B O   1 
ATOM   1073 C  CB  . PHE B 1 45 ? 18.958  -11.682 -28.176 1.00 36.79  ? 44  PHE B CB  1 
ATOM   1074 C  CG  . PHE B 1 45 ? 19.676  -13.007 -28.385 1.00 43.22  ? 44  PHE B CG  1 
ATOM   1075 C  CD1 . PHE B 1 45 ? 21.027  -13.135 -28.083 1.00 43.10  ? 44  PHE B CD1 1 
ATOM   1076 C  CD2 . PHE B 1 45 ? 19.012  -14.110 -28.921 1.00 42.09  ? 44  PHE B CD2 1 
ATOM   1077 C  CE1 . PHE B 1 45 ? 21.706  -14.316 -28.330 1.00 42.95  ? 44  PHE B CE1 1 
ATOM   1078 C  CE2 . PHE B 1 45 ? 19.684  -15.300 -29.132 1.00 42.17  ? 44  PHE B CE2 1 
ATOM   1079 C  CZ  . PHE B 1 45 ? 21.036  -15.398 -28.841 1.00 43.94  ? 44  PHE B CZ  1 
ATOM   1080 N  N   . PHE B 1 46 ? 17.430  -9.348  -30.212 1.00 47.04  ? 45  PHE B N   1 
ATOM   1081 C  CA  . PHE B 1 46 ? 16.519  -8.217  -30.280 1.00 50.92  ? 45  PHE B CA  1 
ATOM   1082 C  C   . PHE B 1 46 ? 15.534  -8.375  -29.127 1.00 50.08  ? 45  PHE B C   1 
ATOM   1083 O  O   . PHE B 1 46 ? 15.318  -9.493  -28.671 1.00 43.76  ? 45  PHE B O   1 
ATOM   1084 C  CB  . PHE B 1 46 ? 15.866  -8.052  -31.660 1.00 55.50  ? 45  PHE B CB  1 
ATOM   1085 C  CG  . PHE B 1 46 ? 16.776  -7.565  -32.784 1.00 54.75  ? 45  PHE B CG  1 
ATOM   1086 C  CD1 . PHE B 1 46 ? 17.198  -6.230  -32.841 1.00 53.90  ? 45  PHE B CD1 1 
ATOM   1087 C  CD2 . PHE B 1 46 ? 17.196  -8.433  -33.796 1.00 52.47  ? 45  PHE B CD2 1 
ATOM   1088 C  CE1 . PHE B 1 46 ? 18.031  -5.779  -33.867 1.00 46.89  ? 45  PHE B CE1 1 
ATOM   1089 C  CE2 . PHE B 1 46 ? 18.031  -7.976  -34.822 1.00 53.75  ? 45  PHE B CE2 1 
ATOM   1090 C  CZ  . PHE B 1 46 ? 18.436  -6.647  -34.855 1.00 46.11  ? 45  PHE B CZ  1 
ATOM   1091 N  N   . GLY B 1 47 ? 15.003  -7.252  -28.635 1.00 47.00  ? 46  GLY B N   1 
ATOM   1092 C  CA  . GLY B 1 47 ? 13.982  -7.263  -27.598 1.00 48.49  ? 46  GLY B CA  1 
ATOM   1093 C  C   . GLY B 1 47 ? 14.606  -7.305  -26.204 1.00 46.93  ? 46  GLY B C   1 
ATOM   1094 O  O   . GLY B 1 47 ? 14.428  -6.379  -25.419 1.00 49.10  ? 46  GLY B O   1 
ATOM   1095 N  N   . THR B 1 48 ? 15.363  -8.367  -25.921 1.00 44.94  ? 47  THR B N   1 
ATOM   1096 C  CA  . THR B 1 48 ? 15.990  -8.560  -24.623 1.00 46.43  ? 47  THR B CA  1 
ATOM   1097 C  C   . THR B 1 48 ? 17.396  -7.965  -24.608 1.00 43.98  ? 47  THR B C   1 
ATOM   1098 O  O   . THR B 1 48 ? 17.974  -7.779  -23.547 1.00 52.04  ? 47  THR B O   1 
ATOM   1099 C  CB  . THR B 1 48 ? 16.050  -10.040 -24.228 1.00 44.86  ? 47  THR B CB  1 
ATOM   1100 O  OG1 . THR B 1 48 ? 17.237  -10.592 -24.794 1.00 43.17  ? 47  THR B OG1 1 
ATOM   1101 C  CG2 . THR B 1 48 ? 14.772  -10.802 -24.518 1.00 43.72  ? 47  THR B CG2 1 
ATOM   1102 N  N   . HIS B 1 49 ? 17.952  -7.710  -25.778 1.00 45.52  ? 48  HIS B N   1 
ATOM   1103 C  CA  . HIS B 1 49 ? 19.279  -7.115  -25.907 1.00 48.72  ? 48  HIS B CA  1 
ATOM   1104 C  C   . HIS B 1 49 ? 20.363  -7.912  -25.183 1.00 55.35  ? 48  HIS B C   1 
ATOM   1105 O  O   . HIS B 1 49 ? 21.434  -7.355  -24.928 1.00 61.74  ? 48  HIS B O   1 
ATOM   1106 C  CB  . HIS B 1 49 ? 19.299  -5.631  -25.511 1.00 49.65  ? 48  HIS B CB  1 
ATOM   1107 C  CG  . HIS B 1 49 ? 18.108  -4.847  -25.934 1.00 54.08  ? 48  HIS B CG  1 
ATOM   1108 N  ND1 . HIS B 1 49 ? 17.648  -3.774  -25.200 1.00 59.14  ? 48  HIS B ND1 1 
ATOM   1109 C  CD2 . HIS B 1 49 ? 17.297  -4.941  -27.001 1.00 62.39  ? 48  HIS B CD2 1 
ATOM   1110 C  CE1 . HIS B 1 49 ? 16.581  -3.257  -25.799 1.00 68.00  ? 48  HIS B CE1 1 
ATOM   1111 N  NE2 . HIS B 1 49 ? 16.351  -3.951  -26.899 1.00 69.77  ? 48  HIS B NE2 1 
ATOM   1112 N  N   . GLU B 1 50 ? 20.111  -9.205  -24.908 1.00 45.99  ? 49  GLU B N   1 
ATOM   1113 C  CA  . GLU B 1 50 ? 21.138  -10.116 -24.412 1.00 51.70  ? 49  GLU B CA  1 
ATOM   1114 C  C   . GLU B 1 50 ? 22.202  -10.357 -25.482 1.00 50.04  ? 49  GLU B C   1 
ATOM   1115 O  O   . GLU B 1 50 ? 22.029  -9.993  -26.646 1.00 47.25  ? 49  GLU B O   1 
ATOM   1116 C  CB  . GLU B 1 50 ? 20.508  -11.483 -24.142 1.00 52.89  ? 49  GLU B CB  1 
ATOM   1117 C  CG  . GLU B 1 50 ? 19.577  -11.507 -22.937 1.00 52.84  ? 49  GLU B CG  1 
ATOM   1118 C  CD  . GLU B 1 50 ? 20.332  -11.699 -21.641 1.00 74.53  ? 49  GLU B CD  1 
ATOM   1119 O  OE1 . GLU B 1 50 ? 20.231  -12.826 -21.098 1.00 77.58  ? 49  GLU B OE1 1 
ATOM   1120 O  OE2 . GLU B 1 50 ? 21.014  -10.748 -21.190 1.00 75.67  ? 49  GLU B OE2 1 
ATOM   1121 N  N   . THR B 1 51 ? 23.290  -11.039 -25.111 1.00 53.74  ? 50  THR B N   1 
ATOM   1122 C  CA  . THR B 1 51 ? 24.230  -11.463 -26.141 1.00 52.96  ? 50  THR B CA  1 
ATOM   1123 C  C   . THR B 1 51 ? 24.688  -12.903 -25.893 1.00 53.10  ? 50  THR B C   1 
ATOM   1124 O  O   . THR B 1 51 ? 24.439  -13.477 -24.833 1.00 50.65  ? 50  THR B O   1 
ATOM   1125 C  CB  . THR B 1 51 ? 25.396  -10.481 -26.277 1.00 53.40  ? 50  THR B CB  1 
ATOM   1126 O  OG1 . THR B 1 51 ? 26.425  -11.048 -25.479 1.00 50.09  ? 50  THR B OG1 1 
ATOM   1127 C  CG2 . THR B 1 51 ? 25.042  -9.060  -25.870 1.00 50.50  ? 50  THR B CG2 1 
ATOM   1128 N  N   . ALA B 1 52 ? 25.332  -13.497 -26.906 1.00 54.41  ? 51  ALA B N   1 
ATOM   1129 C  CA  . ALA B 1 52 ? 26.045  -14.755 -26.749 1.00 51.11  ? 51  ALA B CA  1 
ATOM   1130 C  C   . ALA B 1 52 ? 26.954  -15.019 -27.957 1.00 53.70  ? 51  ALA B C   1 
ATOM   1131 O  O   . ALA B 1 52 ? 26.979  -14.234 -28.911 1.00 56.18  ? 51  ALA B O   1 
ATOM   1132 C  CB  . ALA B 1 52 ? 25.079  -15.895 -26.460 1.00 51.57  ? 51  ALA B CB  1 
ATOM   1133 N  N   . PHE B 1 53 ? 27.748  -16.096 -27.885 1.00 47.87  ? 52  PHE B N   1 
ATOM   1134 C  CA  . PHE B 1 53 ? 28.463  -16.586 -29.055 1.00 48.91  ? 52  PHE B CA  1 
ATOM   1135 C  C   . PHE B 1 53 ? 27.753  -17.815 -29.615 1.00 54.87  ? 52  PHE B C   1 
ATOM   1136 O  O   . PHE B 1 53 ? 27.404  -18.725 -28.858 1.00 63.70  ? 52  PHE B O   1 
ATOM   1137 C  CB  . PHE B 1 53 ? 29.944  -16.891 -28.804 1.00 46.71  ? 52  PHE B CB  1 
ATOM   1138 C  CG  . PHE B 1 53 ? 30.718  -15.681 -28.308 1.00 49.56  ? 52  PHE B CG  1 
ATOM   1139 C  CD1 . PHE B 1 53 ? 30.934  -14.583 -29.134 1.00 53.41  ? 52  PHE B CD1 1 
ATOM   1140 C  CD2 . PHE B 1 53 ? 31.232  -15.645 -27.015 1.00 53.43  ? 52  PHE B CD2 1 
ATOM   1141 C  CE1 . PHE B 1 53 ? 31.641  -13.473 -28.684 1.00 47.80  ? 52  PHE B CE1 1 
ATOM   1142 C  CE2 . PHE B 1 53 ? 31.934  -14.532 -26.569 1.00 58.00  ? 52  PHE B CE2 1 
ATOM   1143 C  CZ  . PHE B 1 53 ? 32.141  -13.454 -27.405 1.00 50.27  ? 52  PHE B CZ  1 
ATOM   1144 N  N   . LEU B 1 54 ? 27.572  -17.848 -30.949 1.00 45.91  ? 53  LEU B N   1 
ATOM   1145 C  CA  . LEU B 1 54 ? 26.887  -18.967 -31.570 1.00 48.67  ? 53  LEU B CA  1 
ATOM   1146 C  C   . LEU B 1 54 ? 27.649  -19.425 -32.813 1.00 43.68  ? 53  LEU B C   1 
ATOM   1147 O  O   . LEU B 1 54 ? 28.198  -18.600 -33.542 1.00 50.28  ? 53  LEU B O   1 
ATOM   1148 C  CB  . LEU B 1 54 ? 25.430  -18.606 -31.896 1.00 48.30  ? 53  LEU B CB  1 
ATOM   1149 C  CG  . LEU B 1 54 ? 24.430  -18.562 -30.737 1.00 46.46  ? 53  LEU B CG  1 
ATOM   1150 C  CD1 . LEU B 1 54 ? 23.007  -18.393 -31.233 1.00 43.34  ? 53  LEU B CD1 1 
ATOM   1151 C  CD2 . LEU B 1 54 ? 24.510  -19.832 -29.897 1.00 53.11  ? 53  LEU B CD2 1 
ATOM   1152 N  N   . GLY B 1 55 ? 27.643  -20.745 -33.053 1.00 44.64  ? 54  GLY B N   1 
ATOM   1153 C  CA  . GLY B 1 55 ? 28.138  -21.341 -34.291 1.00 42.92  ? 54  GLY B CA  1 
ATOM   1154 C  C   . GLY B 1 55 ? 27.028  -21.525 -35.331 1.00 50.37  ? 54  GLY B C   1 
ATOM   1155 O  O   . GLY B 1 55 ? 25.845  -21.622 -34.990 1.00 49.03  ? 54  GLY B O   1 
ATOM   1156 N  N   . PRO B 1 56 ? 27.389  -21.555 -36.636 1.00 46.42  ? 55  PRO B N   1 
ATOM   1157 C  CA  . PRO B 1 56 ? 26.416  -21.434 -37.714 1.00 43.73  ? 55  PRO B CA  1 
ATOM   1158 C  C   . PRO B 1 56 ? 25.191  -22.328 -37.644 1.00 45.24  ? 55  PRO B C   1 
ATOM   1159 O  O   . PRO B 1 56 ? 24.244  -22.093 -38.386 1.00 45.81  ? 55  PRO B O   1 
ATOM   1160 C  CB  . PRO B 1 56 ? 27.261  -21.792 -38.943 1.00 43.88  ? 55  PRO B CB  1 
ATOM   1161 C  CG  . PRO B 1 56 ? 28.636  -21.288 -38.590 1.00 45.98  ? 55  PRO B CG  1 
ATOM   1162 C  CD  . PRO B 1 56 ? 28.777  -21.617 -37.132 1.00 43.49  ? 55  PRO B CD  1 
ATOM   1163 N  N   . LYS B 1 57 ? 25.276  -23.400 -36.844 1.00 40.84  ? 56  LYS B N   1 
ATOM   1164 C  CA  . LYS B 1 57 ? 24.259  -24.431 -36.875 1.00 46.57  ? 56  LYS B CA  1 
ATOM   1165 C  C   . LYS B 1 57 ? 23.011  -23.828 -36.248 1.00 39.46  ? 56  LYS B C   1 
ATOM   1166 O  O   . LYS B 1 57 ? 21.884  -24.230 -36.555 1.00 46.66  ? 56  LYS B O   1 
ATOM   1167 C  CB  . LYS B 1 57 ? 24.738  -25.697 -36.152 1.00 51.05  ? 56  LYS B CB  1 
ATOM   1168 C  CG  . LYS B 1 57 ? 24.881  -25.599 -34.654 1.00 50.66  ? 56  LYS B CG  1 
ATOM   1169 C  CD  . LYS B 1 57 ? 24.966  -26.987 -34.016 1.00 65.68  ? 56  LYS B CD  1 
ATOM   1170 C  CE  . LYS B 1 57 ? 25.276  -27.005 -32.533 1.00 60.77  ? 56  LYS B CE  1 
ATOM   1171 N  NZ  . LYS B 1 57 ? 24.165  -26.550 -31.693 1.00 65.79  ? 56  LYS B NZ  1 
ATOM   1172 N  N   . ASP B 1 58 ? 23.260  -22.873 -35.350 1.00 44.51  ? 57  ASP B N   1 
ATOM   1173 C  CA  . ASP B 1 58 ? 22.208  -22.260 -34.566 1.00 39.71  ? 57  ASP B CA  1 
ATOM   1174 C  C   . ASP B 1 58 ? 21.733  -20.979 -35.236 1.00 36.53  ? 57  ASP B C   1 
ATOM   1175 O  O   . ASP B 1 58 ? 20.871  -20.317 -34.681 1.00 43.14  ? 57  ASP B O   1 
ATOM   1176 C  CB  . ASP B 1 58 ? 22.592  -22.126 -33.095 1.00 45.54  ? 57  ASP B CB  1 
ATOM   1177 C  CG  . ASP B 1 58 ? 22.851  -23.419 -32.324 1.00 58.47  ? 57  ASP B CG  1 
ATOM   1178 O  OD1 . ASP B 1 58 ? 21.915  -24.257 -32.220 1.00 55.42  ? 57  ASP B OD1 1 
ATOM   1179 O  OD2 . ASP B 1 58 ? 23.981  -23.563 -31.812 1.00 47.56  ? 57  ASP B OD2 1 
ATOM   1180 N  N   . LEU B 1 59 ? 22.220  -20.681 -36.451 1.00 46.21  ? 58  LEU B N   1 
ATOM   1181 C  CA  . LEU B 1 59 ? 21.990  -19.383 -37.090 1.00 42.22  ? 58  LEU B CA  1 
ATOM   1182 C  C   . LEU B 1 59 ? 21.172  -19.544 -38.362 1.00 41.96  ? 58  LEU B C   1 
ATOM   1183 O  O   . LEU B 1 59 ? 21.546  -20.299 -39.256 1.00 42.72  ? 58  LEU B O   1 
ATOM   1184 C  CB  . LEU B 1 59 ? 23.349  -18.768 -37.397 1.00 43.10  ? 58  LEU B CB  1 
ATOM   1185 C  CG  . LEU B 1 59 ? 24.149  -18.385 -36.154 1.00 43.36  ? 58  LEU B CG  1 
ATOM   1186 C  CD1 . LEU B 1 59 ? 25.551  -17.851 -36.383 1.00 40.05  ? 58  LEU B CD1 1 
ATOM   1187 C  CD2 . LEU B 1 59 ? 23.330  -17.356 -35.404 1.00 47.86  ? 58  LEU B CD2 1 
ATOM   1188 N  N   . PHE B 1 60 ? 20.034  -18.843 -38.414 1.00 42.92  ? 59  PHE B N   1 
ATOM   1189 C  CA  . PHE B 1 60 ? 19.069  -18.995 -39.486 1.00 43.46  ? 59  PHE B CA  1 
ATOM   1190 C  C   . PHE B 1 60 ? 18.894  -17.668 -40.241 1.00 46.76  ? 59  PHE B C   1 
ATOM   1191 O  O   . PHE B 1 60 ? 18.294  -16.745 -39.703 1.00 52.01  ? 59  PHE B O   1 
ATOM   1192 C  CB  . PHE B 1 60 ? 17.786  -19.499 -38.811 1.00 42.20  ? 59  PHE B CB  1 
ATOM   1193 C  CG  . PHE B 1 60 ? 17.829  -20.966 -38.388 1.00 45.45  ? 59  PHE B CG  1 
ATOM   1194 C  CD1 . PHE B 1 60 ? 18.288  -21.348 -37.126 1.00 35.63  ? 59  PHE B CD1 1 
ATOM   1195 C  CD2 . PHE B 1 60 ? 17.415  -21.968 -39.257 1.00 39.97  ? 59  PHE B CD2 1 
ATOM   1196 C  CE1 . PHE B 1 60 ? 18.318  -22.688 -36.745 1.00 38.35  ? 59  PHE B CE1 1 
ATOM   1197 C  CE2 . PHE B 1 60 ? 17.459  -23.310 -38.875 1.00 44.05  ? 59  PHE B CE2 1 
ATOM   1198 C  CZ  . PHE B 1 60 ? 17.911  -23.667 -37.628 1.00 38.29  ? 59  PHE B CZ  1 
ATOM   1199 N  N   . PRO B 1 61 ? 19.404  -17.504 -41.493 1.00 50.15  ? 60  PRO B N   1 
ATOM   1200 C  CA  . PRO B 1 61 ? 19.263  -16.235 -42.224 1.00 46.89  ? 60  PRO B CA  1 
ATOM   1201 C  C   . PRO B 1 61 ? 17.824  -15.725 -42.306 1.00 49.05  ? 60  PRO B C   1 
ATOM   1202 O  O   . PRO B 1 61 ? 16.888  -16.498 -42.509 1.00 53.80  ? 60  PRO B O   1 
ATOM   1203 C  CB  . PRO B 1 61 ? 19.915  -16.494 -43.593 1.00 47.25  ? 60  PRO B CB  1 
ATOM   1204 C  CG  . PRO B 1 61 ? 20.908  -17.621 -43.312 1.00 54.94  ? 60  PRO B CG  1 
ATOM   1205 C  CD  . PRO B 1 61 ? 20.222  -18.481 -42.248 1.00 56.47  ? 60  PRO B CD  1 
ATOM   1206 N  N   . TYR B 1 62 ? 17.672  -14.404 -42.131 1.00 47.48  ? 61  TYR B N   1 
ATOM   1207 C  CA  . TYR B 1 62 ? 16.438  -13.860 -41.591 1.00 48.49  ? 61  TYR B CA  1 
ATOM   1208 C  C   . TYR B 1 62 ? 15.335  -13.981 -42.622 1.00 47.65  ? 61  TYR B C   1 
ATOM   1209 O  O   . TYR B 1 62 ? 14.258  -14.470 -42.283 1.00 43.12  ? 61  TYR B O   1 
ATOM   1210 C  CB  . TYR B 1 62 ? 16.573  -12.455 -40.988 1.00 52.35  ? 61  TYR B CB  1 
ATOM   1211 C  CG  . TYR B 1 62 ? 15.260  -11.719 -40.754 1.00 55.88  ? 61  TYR B CG  1 
ATOM   1212 C  CD1 . TYR B 1 62 ? 14.498  -11.963 -39.619 1.00 64.00  ? 61  TYR B CD1 1 
ATOM   1213 C  CD2 . TYR B 1 62 ? 14.789  -10.762 -41.649 1.00 64.33  ? 61  TYR B CD2 1 
ATOM   1214 C  CE1 . TYR B 1 62 ? 13.307  -11.292 -39.385 1.00 63.06  ? 61  TYR B CE1 1 
ATOM   1215 C  CE2 . TYR B 1 62 ? 13.592  -10.088 -41.433 1.00 64.25  ? 61  TYR B CE2 1 
ATOM   1216 C  CZ  . TYR B 1 62 ? 12.853  -10.349 -40.288 1.00 66.97  ? 61  TYR B CZ  1 
ATOM   1217 O  OH  . TYR B 1 62 ? 11.676  -9.718  -40.008 1.00 64.52  ? 61  TYR B OH  1 
ATOM   1218 N  N   . ASP B 1 63 ? 15.654  -13.533 -43.856 1.00 61.17  ? 62  ASP B N   1 
ATOM   1219 C  CA  . ASP B 1 63 ? 14.710  -13.347 -44.950 1.00 54.91  ? 62  ASP B CA  1 
ATOM   1220 C  C   . ASP B 1 63 ? 14.066  -14.683 -45.260 1.00 49.41  ? 62  ASP B C   1 
ATOM   1221 O  O   . ASP B 1 63 ? 12.838  -14.785 -45.314 1.00 45.17  ? 62  ASP B O   1 
ATOM   1222 C  CB  . ASP B 1 63 ? 15.342  -12.683 -46.168 1.00 59.23  ? 62  ASP B CB  1 
ATOM   1223 C  CG  . ASP B 1 63 ? 15.247  -11.161 -46.195 1.00 74.17  ? 62  ASP B CG  1 
ATOM   1224 O  OD1 . ASP B 1 63 ? 14.161  -10.630 -45.847 1.00 67.54  ? 62  ASP B OD1 1 
ATOM   1225 O  OD2 . ASP B 1 63 ? 16.245  -10.513 -46.594 1.00 84.54  ? 62  ASP B OD2 1 
ATOM   1226 N  N   . LYS B 1 64 ? 14.943  -15.686 -45.353 1.00 48.36  ? 63  LYS B N   1 
ATOM   1227 C  CA  . LYS B 1 64 ? 14.640  -17.076 -45.659 1.00 60.99  ? 63  LYS B CA  1 
ATOM   1228 C  C   . LYS B 1 64 ? 13.667  -17.691 -44.648 1.00 57.16  ? 63  LYS B C   1 
ATOM   1229 O  O   . LYS B 1 64 ? 12.894  -18.567 -45.026 1.00 61.09  ? 63  LYS B O   1 
ATOM   1230 C  CB  . LYS B 1 64 ? 15.944  -17.889 -45.708 1.00 56.74  ? 63  LYS B CB  1 
ATOM   1231 C  CG  . LYS B 1 64 ? 15.800  -19.333 -46.180 1.00 60.28  ? 63  LYS B CG  1 
ATOM   1232 C  CD  . LYS B 1 64 ? 17.054  -20.178 -46.000 1.00 68.16  ? 63  LYS B CD  1 
ATOM   1233 C  CE  . LYS B 1 64 ? 17.021  -21.477 -46.752 1.00 75.08  ? 63  LYS B CE  1 
ATOM   1234 N  NZ  . LYS B 1 64 ? 15.747  -22.197 -46.664 1.00 68.96  ? 63  LYS B NZ  1 
ATOM   1235 N  N   . SER B 1 65 ? 13.676  -17.214 -43.393 1.00 58.41  ? 64  SER B N   1 
ATOM   1236 C  CA  . SER B 1 65 ? 13.210  -18.013 -42.260 1.00 58.74  ? 64  SER B CA  1 
ATOM   1237 C  C   . SER B 1 65 ? 12.055  -17.354 -41.506 1.00 50.55  ? 64  SER B C   1 
ATOM   1238 O  O   . SER B 1 65 ? 11.467  -17.969 -40.615 1.00 53.52  ? 64  SER B O   1 
ATOM   1239 C  CB  . SER B 1 65 ? 14.356  -18.317 -41.327 1.00 54.67  ? 64  SER B CB  1 
ATOM   1240 O  OG  . SER B 1 65 ? 14.974  -17.104 -40.917 1.00 66.81  ? 64  SER B OG  1 
ATOM   1241 N  N   . LYS B 1 66 ? 11.702  -16.134 -41.919 1.00 47.85  ? 65  LYS B N   1 
ATOM   1242 C  CA  . LYS B 1 66 ? 10.977  -15.198 -41.080 1.00 50.89  ? 65  LYS B CA  1 
ATOM   1243 C  C   . LYS B 1 66 ? 9.478   -15.494 -41.080 1.00 54.26  ? 65  LYS B C   1 
ATOM   1244 O  O   . LYS B 1 66 ? 8.724   -14.933 -40.291 1.00 64.33  ? 65  LYS B O   1 
ATOM   1245 C  CB  . LYS B 1 66 ? 11.254  -13.776 -41.583 1.00 50.75  ? 65  LYS B CB  1 
ATOM   1246 C  CG  . LYS B 1 66 ? 10.498  -13.394 -42.851 1.00 40.61  ? 65  LYS B CG  1 
ATOM   1247 N  N   . ASP B 1 67 ? 8.999   -16.333 -41.981 1.00 53.00  ? 66  ASP B N   1 
ATOM   1248 C  CA  . ASP B 1 67 ? 7.573   -16.601 -41.872 1.00 71.93  ? 66  ASP B CA  1 
ATOM   1249 C  C   . ASP B 1 67 ? 7.336   -17.885 -41.073 1.00 69.96  ? 66  ASP B C   1 
ATOM   1250 O  O   . ASP B 1 67 ? 6.206   -18.182 -40.682 1.00 67.15  ? 66  ASP B O   1 
ATOM   1251 C  CB  . ASP B 1 67 ? 6.837   -16.388 -43.189 1.00 80.81  ? 66  ASP B CB  1 
ATOM   1252 C  CG  . ASP B 1 67 ? 7.306   -17.232 -44.364 1.00 82.30  ? 66  ASP B CG  1 
ATOM   1253 O  OD1 . ASP B 1 67 ? 7.006   -16.852 -45.522 1.00 97.33  ? 66  ASP B OD1 1 
ATOM   1254 O  OD2 . ASP B 1 67 ? 7.947   -18.267 -44.111 1.00 74.63  ? 66  ASP B OD2 1 
ATOM   1255 N  N   . LYS B 1 68 ? 8.424   -18.625 -40.817 1.00 63.50  ? 67  LYS B N   1 
ATOM   1256 C  CA  . LYS B 1 68 ? 8.373   -19.879 -40.075 1.00 57.58  ? 67  LYS B CA  1 
ATOM   1257 C  C   . LYS B 1 68 ? 8.607   -19.582 -38.595 1.00 50.85  ? 67  LYS B C   1 
ATOM   1258 O  O   . LYS B 1 68 ? 7.743   -19.854 -37.768 1.00 56.75  ? 67  LYS B O   1 
ATOM   1259 C  CB  . LYS B 1 68 ? 9.352   -20.855 -40.741 1.00 54.91  ? 67  LYS B CB  1 
ATOM   1260 C  CG  . LYS B 1 68 ? 9.609   -22.185 -40.077 1.00 63.24  ? 67  LYS B CG  1 
ATOM   1261 C  CD  . LYS B 1 68 ? 10.603  -22.985 -40.918 1.00 66.85  ? 67  LYS B CD  1 
ATOM   1262 C  CE  . LYS B 1 68 ? 11.028  -24.251 -40.247 1.00 61.60  ? 67  LYS B CE  1 
ATOM   1263 N  NZ  . LYS B 1 68 ? 9.833   -25.060 -39.982 1.00 60.10  ? 67  LYS B NZ  1 
ATOM   1264 N  N   . TYR B 1 69 ? 9.744   -18.938 -38.298 1.00 42.90  ? 68  TYR B N   1 
ATOM   1265 C  CA  . TYR B 1 69 ? 10.160  -18.566 -36.954 1.00 41.96  ? 68  TYR B CA  1 
ATOM   1266 C  C   . TYR B 1 69 ? 9.638   -17.197 -36.501 1.00 46.10  ? 68  TYR B C   1 
ATOM   1267 O  O   . TYR B 1 69 ? 9.777   -16.850 -35.333 1.00 45.84  ? 68  TYR B O   1 
ATOM   1268 C  CB  . TYR B 1 69 ? 11.693  -18.604 -37.009 1.00 47.66  ? 68  TYR B CB  1 
ATOM   1269 C  CG  . TYR B 1 69 ? 12.279  -19.989 -37.273 1.00 56.11  ? 68  TYR B CG  1 
ATOM   1270 C  CD1 . TYR B 1 69 ? 11.663  -21.140 -36.773 1.00 55.75  ? 68  TYR B CD1 1 
ATOM   1271 C  CD2 . TYR B 1 69 ? 13.463  -20.145 -37.995 1.00 49.70  ? 68  TYR B CD2 1 
ATOM   1272 C  CE1 . TYR B 1 69 ? 12.196  -22.404 -36.993 1.00 55.01  ? 68  TYR B CE1 1 
ATOM   1273 C  CE2 . TYR B 1 69 ? 14.018  -21.399 -38.195 1.00 59.74  ? 68  TYR B CE2 1 
ATOM   1274 C  CZ  . TYR B 1 69 ? 13.382  -22.529 -37.698 1.00 56.65  ? 68  TYR B CZ  1 
ATOM   1275 O  OH  . TYR B 1 69 ? 13.918  -23.762 -37.923 1.00 60.43  ? 68  TYR B OH  1 
ATOM   1276 N  N   . GLY B 1 70 ? 9.033   -16.396 -37.382 1.00 47.66  ? 69  GLY B N   1 
ATOM   1277 C  CA  . GLY B 1 70 ? 8.750   -15.032 -36.962 1.00 57.91  ? 69  GLY B CA  1 
ATOM   1278 C  C   . GLY B 1 70 ? 7.342   -14.859 -36.383 1.00 68.64  ? 69  GLY B C   1 
ATOM   1279 O  O   . GLY B 1 70 ? 6.691   -13.837 -36.624 1.00 60.82  ? 69  GLY B O   1 
ATOM   1280 N  N   . LYS B 1 71 ? 6.870   -15.855 -35.623 1.00 64.49  ? 70  LYS B N   1 
ATOM   1281 C  CA  . LYS B 1 71 ? 5.531   -15.785 -35.060 1.00 62.38  ? 70  LYS B CA  1 
ATOM   1282 C  C   . LYS B 1 71 ? 5.611   -15.164 -33.671 1.00 68.57  ? 70  LYS B C   1 
ATOM   1283 O  O   . LYS B 1 71 ? 6.562   -15.436 -32.937 1.00 74.08  ? 70  LYS B O   1 
ATOM   1284 C  CB  . LYS B 1 71 ? 4.881   -17.170 -34.977 1.00 65.76  ? 70  LYS B CB  1 
ATOM   1285 C  CG  . LYS B 1 71 ? 3.957   -17.574 -36.124 1.00 83.12  ? 70  LYS B CG  1 
ATOM   1286 C  CD  . LYS B 1 71 ? 4.570   -17.772 -37.508 1.00 82.24  ? 70  LYS B CD  1 
ATOM   1287 C  CE  . LYS B 1 71 ? 3.674   -18.643 -38.324 1.00 84.50  ? 70  LYS B CE  1 
ATOM   1288 N  NZ  . LYS B 1 71 ? 4.032   -18.616 -39.743 1.00 103.52 ? 70  LYS B NZ  1 
ATOM   1289 N  N   . PRO B 1 72 ? 4.622   -14.331 -33.255 1.00 63.65  ? 71  PRO B N   1 
ATOM   1290 C  CA  . PRO B 1 72 ? 4.620   -13.778 -31.898 1.00 61.92  ? 71  PRO B CA  1 
ATOM   1291 C  C   . PRO B 1 72 ? 4.406   -14.950 -30.943 1.00 60.61  ? 71  PRO B C   1 
ATOM   1292 O  O   . PRO B 1 72 ? 3.699   -15.903 -31.283 1.00 60.71  ? 71  PRO B O   1 
ATOM   1293 C  CB  . PRO B 1 72 ? 3.441   -12.794 -31.911 1.00 55.19  ? 71  PRO B CB  1 
ATOM   1294 C  CG  . PRO B 1 72 ? 2.515   -13.380 -32.966 1.00 62.19  ? 71  PRO B CG  1 
ATOM   1295 C  CD  . PRO B 1 72 ? 3.457   -13.899 -34.049 1.00 65.55  ? 71  PRO B CD  1 
ATOM   1296 N  N   . ASN B 1 73 ? 5.092   -14.901 -29.793 1.00 56.82  ? 72  ASN B N   1 
ATOM   1297 C  CA  . ASN B 1 73 ? 4.827   -15.807 -28.688 1.00 52.75  ? 72  ASN B CA  1 
ATOM   1298 C  C   . ASN B 1 73 ? 4.750   -14.979 -27.404 1.00 54.57  ? 72  ASN B C   1 
ATOM   1299 O  O   . ASN B 1 73 ? 4.812   -13.746 -27.469 1.00 46.73  ? 72  ASN B O   1 
ATOM   1300 C  CB  . ASN B 1 73 ? 5.808   -16.974 -28.635 1.00 52.22  ? 72  ASN B CB  1 
ATOM   1301 C  CG  . ASN B 1 73 ? 7.184   -16.563 -28.162 1.00 52.52  ? 72  ASN B CG  1 
ATOM   1302 O  OD1 . ASN B 1 73 ? 7.320   -15.988 -27.077 1.00 57.66  ? 72  ASN B OD1 1 
ATOM   1303 N  ND2 . ASN B 1 73 ? 8.217   -16.867 -28.935 1.00 57.26  ? 72  ASN B ND2 1 
ATOM   1304 N  N   . LYS B 1 74 ? 4.636   -15.670 -26.257 1.00 49.59  ? 73  LYS B N   1 
ATOM   1305 C  CA  . LYS B 1 74 ? 4.457   -15.002 -24.972 1.00 50.68  ? 73  LYS B CA  1 
ATOM   1306 C  C   . LYS B 1 74 ? 5.771   -14.926 -24.178 1.00 45.53  ? 73  LYS B C   1 
ATOM   1307 O  O   . LYS B 1 74 ? 5.756   -14.463 -23.047 1.00 52.75  ? 73  LYS B O   1 
ATOM   1308 C  CB  . LYS B 1 74 ? 3.225   -15.538 -24.224 1.00 50.23  ? 73  LYS B CB  1 
ATOM   1309 N  N   . ARG B 1 75 ? 6.907   -15.369 -24.753 1.00 46.65  ? 74  ARG B N   1 
ATOM   1310 C  CA  . ARG B 1 75 ? 8.209   -15.232 -24.100 1.00 41.65  ? 74  ARG B CA  1 
ATOM   1311 C  C   . ARG B 1 75 ? 8.643   -13.764 -24.033 1.00 36.39  ? 74  ARG B C   1 
ATOM   1312 O  O   . ARG B 1 75 ? 8.575   -13.063 -25.029 1.00 40.49  ? 74  ARG B O   1 
ATOM   1313 C  CB  . ARG B 1 75 ? 9.301   -16.031 -24.822 1.00 39.93  ? 74  ARG B CB  1 
ATOM   1314 C  CG  . ARG B 1 75 ? 9.133   -17.535 -24.992 1.00 43.75  ? 74  ARG B CG  1 
ATOM   1315 C  CD  . ARG B 1 75 ? 9.071   -18.308 -23.698 1.00 36.52  ? 74  ARG B CD  1 
ATOM   1316 N  NE  . ARG B 1 75 ? 9.259   -19.755 -23.856 1.00 35.41  ? 74  ARG B NE  1 
ATOM   1317 C  CZ  . ARG B 1 75 ? 10.423  -20.385 -23.812 1.00 40.57  ? 74  ARG B CZ  1 
ATOM   1318 N  NH1 . ARG B 1 75 ? 11.534  -19.706 -23.505 1.00 40.91  ? 74  ARG B NH1 1 
ATOM   1319 N  NH2 . ARG B 1 75 ? 10.475  -21.659 -24.174 1.00 35.58  ? 74  ARG B NH2 1 
ATOM   1320 N  N   . LYS B 1 76 ? 9.139   -13.323 -22.862 1.00 44.75  ? 75  LYS B N   1 
ATOM   1321 C  CA  . LYS B 1 76 ? 9.468   -11.940 -22.520 1.00 38.18  ? 75  LYS B CA  1 
ATOM   1322 C  C   . LYS B 1 76 ? 10.610  -11.387 -23.369 1.00 45.48  ? 75  LYS B C   1 
ATOM   1323 O  O   . LYS B 1 76 ? 11.716  -11.929 -23.326 1.00 46.12  ? 75  LYS B O   1 
ATOM   1324 C  CB  . LYS B 1 76 ? 9.971   -11.908 -21.071 1.00 40.93  ? 75  LYS B CB  1 
ATOM   1325 C  CG  . LYS B 1 76 ? 10.445  -10.528 -20.570 1.00 36.50  ? 75  LYS B CG  1 
ATOM   1326 C  CD  . LYS B 1 76 ? 10.870  -10.304 -19.114 1.00 43.74  ? 75  LYS B CD  1 
ATOM   1327 C  CE  . LYS B 1 76 ? 11.270  -8.868  -18.809 1.00 46.75  ? 75  LYS B CE  1 
ATOM   1328 N  NZ  . LYS B 1 76 ? 11.709  -8.549  -17.435 1.00 46.97  ? 75  LYS B NZ  1 
ATOM   1329 N  N   . GLY B 1 77 ? 10.337  -10.269 -24.067 1.00 45.26  ? 76  GLY B N   1 
ATOM   1330 C  CA  . GLY B 1 77 ? 11.276  -9.589  -24.952 1.00 40.61  ? 76  GLY B CA  1 
ATOM   1331 C  C   . GLY B 1 77 ? 11.079  -9.970  -26.422 1.00 43.70  ? 76  GLY B C   1 
ATOM   1332 O  O   . GLY B 1 77 ? 11.543  -9.259  -27.303 1.00 55.84  ? 76  GLY B O   1 
ATOM   1333 N  N   . PHE B 1 78 ? 10.330  -11.059 -26.686 1.00 48.83  ? 77  PHE B N   1 
ATOM   1334 C  CA  . PHE B 1 78 ? 10.182  -11.647 -28.010 1.00 42.40  ? 77  PHE B CA  1 
ATOM   1335 C  C   . PHE B 1 78 ? 9.492   -10.723 -29.017 1.00 50.59  ? 77  PHE B C   1 
ATOM   1336 O  O   . PHE B 1 78 ? 10.063  -10.400 -30.058 1.00 46.60  ? 77  PHE B O   1 
ATOM   1337 C  CB  . PHE B 1 78 ? 9.428   -12.972 -28.025 1.00 49.40  ? 77  PHE B CB  1 
ATOM   1338 C  CG  . PHE B 1 78 ? 9.720   -13.758 -29.291 1.00 44.08  ? 77  PHE B CG  1 
ATOM   1339 C  CD1 . PHE B 1 78 ? 10.957  -14.372 -29.479 1.00 46.25  ? 77  PHE B CD1 1 
ATOM   1340 C  CD2 . PHE B 1 78 ? 8.772   -13.867 -30.289 1.00 46.83  ? 77  PHE B CD2 1 
ATOM   1341 C  CE1 . PHE B 1 78 ? 11.224  -15.097 -30.627 1.00 46.11  ? 77  PHE B CE1 1 
ATOM   1342 C  CE2 . PHE B 1 78 ? 9.054   -14.577 -31.449 1.00 49.34  ? 77  PHE B CE2 1 
ATOM   1343 C  CZ  . PHE B 1 78 ? 10.276  -15.204 -31.610 1.00 48.16  ? 77  PHE B CZ  1 
ATOM   1344 N  N   . ASN B 1 79 ? 8.229   -10.376 -28.759 1.00 45.47  ? 78  ASN B N   1 
ATOM   1345 C  CA  . ASN B 1 79 ? 7.517   -9.461  -29.624 1.00 42.75  ? 78  ASN B CA  1 
ATOM   1346 C  C   . ASN B 1 79 ? 8.278   -8.142  -29.749 1.00 42.50  ? 78  ASN B C   1 
ATOM   1347 O  O   . ASN B 1 79 ? 8.253   -7.505  -30.805 1.00 50.04  ? 78  ASN B O   1 
ATOM   1348 C  CB  . ASN B 1 79 ? 6.063   -9.265  -29.204 1.00 42.84  ? 78  ASN B CB  1 
ATOM   1349 C  CG  . ASN B 1 79 ? 5.271   -10.548 -29.281 1.00 51.87  ? 78  ASN B CG  1 
ATOM   1350 O  OD1 . ASN B 1 79 ? 5.725   -11.546 -29.853 1.00 50.32  ? 78  ASN B OD1 1 
ATOM   1351 N  ND2 . ASN B 1 79 ? 4.064   -10.542 -28.740 1.00 50.99  ? 78  ASN B ND2 1 
ATOM   1352 N  N   . GLU B 1 80 ? 8.954   -7.720  -28.685 1.00 48.80  ? 79  GLU B N   1 
ATOM   1353 C  CA  . GLU B 1 80 ? 9.747   -6.512  -28.819 1.00 51.25  ? 79  GLU B CA  1 
ATOM   1354 C  C   . GLU B 1 80 ? 10.825  -6.790  -29.863 1.00 52.18  ? 79  GLU B C   1 
ATOM   1355 O  O   . GLU B 1 80 ? 11.022  -5.986  -30.763 1.00 46.59  ? 79  GLU B O   1 
ATOM   1356 C  CB  . GLU B 1 80 ? 10.296  -5.959  -27.504 1.00 47.06  ? 79  GLU B CB  1 
ATOM   1357 C  CG  . GLU B 1 80 ? 9.295   -5.075  -26.768 1.00 52.11  ? 79  GLU B CG  1 
ATOM   1358 N  N   . GLY B 1 81 ? 11.462  -7.963  -29.768 1.00 51.41  ? 80  GLY B N   1 
ATOM   1359 C  CA  . GLY B 1 81 ? 12.543  -8.315  -30.673 1.00 52.91  ? 80  GLY B CA  1 
ATOM   1360 C  C   . GLY B 1 81 ? 12.078  -8.335  -32.124 1.00 51.27  ? 80  GLY B C   1 
ATOM   1361 O  O   . GLY B 1 81 ? 12.858  -8.048  -33.023 1.00 54.52  ? 80  GLY B O   1 
ATOM   1362 N  N   . LEU B 1 82 ? 10.799  -8.688  -32.328 1.00 49.85  ? 81  LEU B N   1 
ATOM   1363 C  CA  . LEU B 1 82 ? 10.184  -8.753  -33.642 1.00 42.03  ? 81  LEU B CA  1 
ATOM   1364 C  C   . LEU B 1 82 ? 10.061  -7.338  -34.206 1.00 39.36  ? 81  LEU B C   1 
ATOM   1365 O  O   . LEU B 1 82 ? 10.337  -7.108  -35.390 1.00 41.63  ? 81  LEU B O   1 
ATOM   1366 C  CB  . LEU B 1 82 ? 8.819   -9.453  -33.668 1.00 40.71  ? 81  LEU B CB  1 
ATOM   1367 C  CG  . LEU B 1 82 ? 8.837   -10.971 -33.473 1.00 44.23  ? 81  LEU B CG  1 
ATOM   1368 C  CD1 . LEU B 1 82 ? 7.483   -11.682 -33.671 1.00 40.93  ? 81  LEU B CD1 1 
ATOM   1369 C  CD2 . LEU B 1 82 ? 9.917   -11.569 -34.348 1.00 42.07  ? 81  LEU B CD2 1 
ATOM   1370 N  N   . TRP B 1 83 ? 9.589   -6.406  -33.381 1.00 42.22  ? 82  TRP B N   1 
ATOM   1371 C  CA  . TRP B 1 83 ? 9.495   -5.019  -33.822 1.00 41.39  ? 82  TRP B CA  1 
ATOM   1372 C  C   . TRP B 1 83 ? 10.881  -4.502  -34.246 1.00 41.30  ? 82  TRP B C   1 
ATOM   1373 O  O   . TRP B 1 83 ? 11.031  -3.960  -35.341 1.00 43.34  ? 82  TRP B O   1 
ATOM   1374 C  CB  . TRP B 1 83 ? 8.829   -4.165  -32.740 1.00 41.54  ? 82  TRP B CB  1 
ATOM   1375 C  CG  . TRP B 1 83 ? 8.616   -2.720  -33.125 1.00 47.22  ? 82  TRP B CG  1 
ATOM   1376 C  CD1 . TRP B 1 83 ? 7.445   -2.150  -33.535 1.00 50.69  ? 82  TRP B CD1 1 
ATOM   1377 C  CD2 . TRP B 1 83 ? 9.615   -1.674  -33.168 1.00 45.35  ? 82  TRP B CD2 1 
ATOM   1378 N  NE1 . TRP B 1 83 ? 7.641   -0.822  -33.796 1.00 55.63  ? 82  TRP B NE1 1 
ATOM   1379 C  CE2 . TRP B 1 83 ? 8.963   -0.504  -33.594 1.00 46.39  ? 82  TRP B CE2 1 
ATOM   1380 C  CE3 . TRP B 1 83 ? 10.989  -1.612  -32.886 1.00 47.78  ? 82  TRP B CE3 1 
ATOM   1381 C  CZ2 . TRP B 1 83 ? 9.636   0.710   -33.744 1.00 45.92  ? 82  TRP B CZ2 1 
ATOM   1382 C  CZ3 . TRP B 1 83 ? 11.661  -0.418  -33.060 1.00 48.98  ? 82  TRP B CZ3 1 
ATOM   1383 C  CH2 . TRP B 1 83 ? 10.991  0.729   -33.486 1.00 46.77  ? 82  TRP B CH2 1 
ATOM   1384 N  N   . GLU B 1 84 ? 11.899  -4.716  -33.398 1.00 39.87  ? 83  GLU B N   1 
ATOM   1385 C  CA  . GLU B 1 84 ? 13.251  -4.228  -33.657 1.00 44.94  ? 83  GLU B CA  1 
ATOM   1386 C  C   . GLU B 1 84 ? 13.835  -4.734  -34.980 1.00 42.46  ? 83  GLU B C   1 
ATOM   1387 O  O   . GLU B 1 84 ? 14.276  -3.952  -35.815 1.00 41.10  ? 83  GLU B O   1 
ATOM   1388 C  CB  . GLU B 1 84 ? 14.148  -4.545  -32.471 1.00 46.21  ? 83  GLU B CB  1 
ATOM   1389 C  CG  . GLU B 1 84 ? 13.673  -3.847  -31.194 1.00 52.07  ? 83  GLU B CG  1 
ATOM   1390 C  CD  . GLU B 1 84 ? 14.596  -4.085  -30.025 1.00 44.27  ? 83  GLU B CD  1 
ATOM   1391 O  OE1 . GLU B 1 84 ? 15.479  -4.960  -30.200 1.00 44.26  ? 83  GLU B OE1 1 
ATOM   1392 O  OE2 . GLU B 1 84 ? 14.476  -3.394  -28.979 1.00 46.85  ? 83  GLU B OE2 1 
ATOM   1393 N  N   . ILE B 1 85 ? 13.822  -6.052  -35.184 1.00 48.39  ? 84  ILE B N   1 
ATOM   1394 C  CA  . ILE B 1 85 ? 14.418  -6.634  -36.378 1.00 44.62  ? 84  ILE B CA  1 
ATOM   1395 C  C   . ILE B 1 85 ? 13.728  -6.096  -37.633 1.00 45.16  ? 84  ILE B C   1 
ATOM   1396 O  O   . ILE B 1 85 ? 14.364  -5.924  -38.658 1.00 46.15  ? 84  ILE B O   1 
ATOM   1397 C  CB  . ILE B 1 85 ? 14.440  -8.175  -36.279 1.00 41.98  ? 84  ILE B CB  1 
ATOM   1398 C  CG1 . ILE B 1 85 ? 15.454  -8.780  -37.233 1.00 42.06  ? 84  ILE B CG1 1 
ATOM   1399 C  CG2 . ILE B 1 85 ? 13.042  -8.781  -36.454 1.00 36.73  ? 84  ILE B CG2 1 
ATOM   1400 C  CD1 . ILE B 1 85 ? 15.869  -10.210 -36.917 1.00 53.77  ? 84  ILE B CD1 1 
ATOM   1401 N  N   . GLN B 1 86 ? 12.428  -5.801  -37.531 1.00 40.97  ? 85  GLN B N   1 
ATOM   1402 C  CA  . GLN B 1 86 ? 11.620  -5.256  -38.600 1.00 40.78  ? 85  GLN B CA  1 
ATOM   1403 C  C   . GLN B 1 86 ? 11.873  -3.759  -38.831 1.00 35.95  ? 85  GLN B C   1 
ATOM   1404 O  O   . GLN B 1 86 ? 11.835  -3.286  -39.958 1.00 49.30  ? 85  GLN B O   1 
ATOM   1405 C  CB  . GLN B 1 86 ? 10.164  -5.529  -38.195 1.00 43.78  ? 85  GLN B CB  1 
ATOM   1406 C  CG  . GLN B 1 86 ? 9.832   -7.021  -38.155 1.00 52.73  ? 85  GLN B CG  1 
ATOM   1407 C  CD  . GLN B 1 86 ? 8.358   -7.375  -38.062 1.00 60.98  ? 85  GLN B CD  1 
ATOM   1408 O  OE1 . GLN B 1 86 ? 7.462   -6.523  -37.993 1.00 62.83  ? 85  GLN B OE1 1 
ATOM   1409 N  NE2 . GLN B 1 86 ? 8.094   -8.673  -38.085 1.00 62.93  ? 85  GLN B NE2 1 
ATOM   1410 N  N   . ASN B 1 87 ? 12.075  -2.975  -37.775 1.00 48.00  ? 86  ASN B N   1 
ATOM   1411 C  CA  . ASN B 1 87 ? 11.939  -1.538  -37.953 1.00 43.27  ? 86  ASN B CA  1 
ATOM   1412 C  C   . ASN B 1 87 ? 13.272  -0.837  -37.856 1.00 45.59  ? 86  ASN B C   1 
ATOM   1413 O  O   . ASN B 1 87 ? 13.446  0.224   -38.464 1.00 49.96  ? 86  ASN B O   1 
ATOM   1414 C  CB  . ASN B 1 87 ? 10.952  -0.893  -37.001 1.00 38.86  ? 86  ASN B CB  1 
ATOM   1415 C  CG  . ASN B 1 87 ? 9.578   -1.481  -37.214 1.00 46.17  ? 86  ASN B CG  1 
ATOM   1416 O  OD1 . ASN B 1 87 ? 8.756   -0.860  -37.883 1.00 48.34  ? 86  ASN B OD1 1 
ATOM   1417 N  ND2 . ASN B 1 87 ? 9.315   -2.670  -36.691 1.00 51.06  ? 86  ASN B ND2 1 
ATOM   1418 N  N   . ASN B 1 88 ? 14.214  -1.437  -37.140 1.00 41.27  ? 87  ASN B N   1 
ATOM   1419 C  CA  . ASN B 1 88 ? 15.456  -0.707  -36.982 1.00 43.08  ? 87  ASN B CA  1 
ATOM   1420 C  C   . ASN B 1 88 ? 16.550  -1.683  -36.592 1.00 44.83  ? 87  ASN B C   1 
ATOM   1421 O  O   . ASN B 1 88 ? 17.206  -1.528  -35.556 1.00 52.46  ? 87  ASN B O   1 
ATOM   1422 C  CB  . ASN B 1 88 ? 15.285  0.541   -36.114 1.00 41.97  ? 87  ASN B CB  1 
ATOM   1423 C  CG  . ASN B 1 88 ? 16.504  1.442   -36.144 1.00 40.61  ? 87  ASN B CG  1 
ATOM   1424 O  OD1 . ASN B 1 88 ? 17.627  0.996   -36.403 1.00 44.25  ? 87  ASN B OD1 1 
ATOM   1425 N  ND2 . ASN B 1 88 ? 16.328  2.715   -35.831 1.00 48.70  ? 87  ASN B ND2 1 
ATOM   1426 N  N   . PRO B 1 89 ? 16.776  -2.718  -37.414 1.00 41.19  ? 88  PRO B N   1 
ATOM   1427 C  CA  . PRO B 1 89 ? 17.723  -3.764  -37.034 1.00 44.80  ? 88  PRO B CA  1 
ATOM   1428 C  C   . PRO B 1 89 ? 19.144  -3.291  -36.730 1.00 41.49  ? 88  PRO B C   1 
ATOM   1429 O  O   . PRO B 1 89 ? 19.900  -4.038  -36.124 1.00 50.05  ? 88  PRO B O   1 
ATOM   1430 C  CB  . PRO B 1 89 ? 17.691  -4.658  -38.300 1.00 33.90  ? 88  PRO B CB  1 
ATOM   1431 C  CG  . PRO B 1 89 ? 17.295  -3.680  -39.396 1.00 37.63  ? 88  PRO B CG  1 
ATOM   1432 C  CD  . PRO B 1 89 ? 16.129  -2.969  -38.722 1.00 38.95  ? 88  PRO B CD  1 
ATOM   1433 N  N   . HIS B 1 90 ? 19.511  -2.079  -37.163 1.00 36.03  ? 89  HIS B N   1 
ATOM   1434 C  CA  . HIS B 1 90 ? 20.920  -1.678  -37.180 1.00 33.22  ? 89  HIS B CA  1 
ATOM   1435 C  C   . HIS B 1 90 ? 21.168  -0.561  -36.148 1.00 40.05  ? 89  HIS B C   1 
ATOM   1436 O  O   . HIS B 1 90 ? 22.318  -0.135  -35.909 1.00 35.47  ? 89  HIS B O   1 
ATOM   1437 C  CB  . HIS B 1 90 ? 21.293  -1.284  -38.619 1.00 34.71  ? 89  HIS B CB  1 
ATOM   1438 C  CG  . HIS B 1 90 ? 21.246  -2.389  -39.640 1.00 34.15  ? 89  HIS B CG  1 
ATOM   1439 N  ND1 . HIS B 1 90 ? 21.642  -3.691  -39.417 1.00 33.98  ? 89  HIS B ND1 1 
ATOM   1440 C  CD2 . HIS B 1 90 ? 20.805  -2.363  -40.896 1.00 35.47  ? 89  HIS B CD2 1 
ATOM   1441 C  CE1 . HIS B 1 90 ? 21.459  -4.406  -40.505 1.00 29.09  ? 89  HIS B CE1 1 
ATOM   1442 N  NE2 . HIS B 1 90 ? 20.927  -3.612  -41.402 1.00 37.14  ? 89  HIS B NE2 1 
ATOM   1443 N  N   . ALA B 1 91 ? 20.087  -0.111  -35.498 1.00 38.15  ? 90  ALA B N   1 
ATOM   1444 C  CA  . ALA B 1 91 ? 20.129  0.765   -34.314 1.00 43.16  ? 90  ALA B CA  1 
ATOM   1445 C  C   . ALA B 1 91 ? 21.189  0.363   -33.301 1.00 42.59  ? 90  ALA B C   1 
ATOM   1446 O  O   . ALA B 1 91 ? 21.452  -0.828  -33.120 1.00 46.83  ? 90  ALA B O   1 
ATOM   1447 C  CB  . ALA B 1 91 ? 18.811  0.730   -33.589 1.00 34.95  ? 90  ALA B CB  1 
ATOM   1448 N  N   . SER B 1 92 ? 21.699  1.364   -32.559 1.00 54.37  ? 91  SER B N   1 
ATOM   1449 C  CA  . SER B 1 92 ? 22.334  1.144   -31.263 1.00 55.96  ? 91  SER B CA  1 
ATOM   1450 C  C   . SER B 1 92 ? 21.283  0.783   -30.212 1.00 63.53  ? 91  SER B C   1 
ATOM   1451 O  O   . SER B 1 92 ? 20.252  1.444   -30.098 1.00 59.87  ? 91  SER B O   1 
ATOM   1452 C  CB  . SER B 1 92 ? 23.128  2.336   -30.805 1.00 53.63  ? 91  SER B CB  1 
ATOM   1453 O  OG  . SER B 1 92 ? 24.002  1.920   -29.771 1.00 59.87  ? 91  SER B OG  1 
ATOM   1454 N  N   . TYR B 1 93 ? 21.562  -0.269  -29.438 1.00 64.90  ? 92  TYR B N   1 
ATOM   1455 C  CA  . TYR B 1 93 ? 20.704  -0.629  -28.317 1.00 69.18  ? 92  TYR B CA  1 
ATOM   1456 C  C   . TYR B 1 93 ? 21.456  -0.448  -26.997 1.00 68.50  ? 92  TYR B C   1 
ATOM   1457 O  O   . TYR B 1 93 ? 20.976  -0.859  -25.949 1.00 68.05  ? 92  TYR B O   1 
ATOM   1458 C  CB  . TYR B 1 93 ? 20.005  -1.972  -28.568 1.00 60.48  ? 92  TYR B CB  1 
ATOM   1459 C  CG  . TYR B 1 93 ? 18.926  -1.877  -29.641 1.00 57.56  ? 92  TYR B CG  1 
ATOM   1460 C  CD1 . TYR B 1 93 ? 17.663  -1.373  -29.347 1.00 58.20  ? 92  TYR B CD1 1 
ATOM   1461 C  CD2 . TYR B 1 93 ? 19.174  -2.261  -30.958 1.00 56.76  ? 92  TYR B CD2 1 
ATOM   1462 C  CE1 . TYR B 1 93 ? 16.682  -1.270  -30.322 1.00 47.29  ? 92  TYR B CE1 1 
ATOM   1463 C  CE2 . TYR B 1 93 ? 18.199  -2.163  -31.941 1.00 44.05  ? 92  TYR B CE2 1 
ATOM   1464 C  CZ  . TYR B 1 93 ? 16.946  -1.678  -31.618 1.00 43.69  ? 92  TYR B CZ  1 
ATOM   1465 O  OH  . TYR B 1 93 ? 16.001  -1.574  -32.603 1.00 45.63  ? 92  TYR B OH  1 
ATOM   1466 N  N   . SER B 1 94 ? 22.625  0.200   -27.068 1.00 75.67  ? 93  SER B N   1 
ATOM   1467 C  CA  . SER B 1 94 ? 23.445  0.543   -25.916 1.00 83.08  ? 93  SER B CA  1 
ATOM   1468 C  C   . SER B 1 94 ? 22.935  1.819   -25.224 1.00 88.45  ? 93  SER B C   1 
ATOM   1469 O  O   . SER B 1 94 ? 21.945  2.411   -25.727 1.00 82.15  ? 93  SER B O   1 
ATOM   1470 C  CB  . SER B 1 94 ? 24.895  0.704   -26.309 1.00 84.17  ? 93  SER B CB  1 
ATOM   1471 O  OG  . SER B 1 94 ? 25.515  -0.560  -26.486 1.00 78.34  ? 93  SER B OG  1 
ATOM   1472 O  OXT . SER B 1 94 ? 23.568  2.195   -24.207 1.00 103.85 ? 93  SER B OXT 1 
ATOM   1473 N  N   . HIS C 1 4  ? 33.212  -24.327 27.111  1.00 72.53  ? 3   HIS C N   1 
ATOM   1474 C  CA  . HIS C 1 4  ? 31.968  -23.513 27.223  1.00 75.25  ? 3   HIS C CA  1 
ATOM   1475 C  C   . HIS C 1 4  ? 31.350  -23.741 28.601  1.00 73.76  ? 3   HIS C C   1 
ATOM   1476 O  O   . HIS C 1 4  ? 32.039  -24.209 29.505  1.00 77.58  ? 3   HIS C O   1 
ATOM   1477 C  CB  . HIS C 1 4  ? 31.035  -23.779 26.035  1.00 69.56  ? 3   HIS C CB  1 
ATOM   1478 N  N   . ALA C 1 5  ? 30.059  -23.403 28.748  1.00 72.49  ? 4   ALA C N   1 
ATOM   1479 C  CA  . ALA C 1 5  ? 29.365  -23.486 30.024  1.00 71.15  ? 4   ALA C CA  1 
ATOM   1480 C  C   . ALA C 1 5  ? 27.855  -23.386 29.820  1.00 74.33  ? 4   ALA C C   1 
ATOM   1481 O  O   . ALA C 1 5  ? 27.364  -22.442 29.202  1.00 66.07  ? 4   ALA C O   1 
ATOM   1482 C  CB  . ALA C 1 5  ? 29.845  -22.372 30.908  1.00 74.20  ? 4   ALA C CB  1 
ATOM   1483 N  N   . PHE C 1 6  ? 27.119  -24.345 30.392  1.00 67.91  ? 5   PHE C N   1 
ATOM   1484 C  CA  . PHE C 1 6  ? 25.725  -24.506 30.021  1.00 66.37  ? 5   PHE C CA  1 
ATOM   1485 C  C   . PHE C 1 6  ? 24.862  -24.546 31.273  1.00 68.79  ? 5   PHE C C   1 
ATOM   1486 O  O   . PHE C 1 6  ? 25.156  -25.285 32.211  1.00 87.05  ? 5   PHE C O   1 
ATOM   1487 C  CB  . PHE C 1 6  ? 25.529  -25.698 29.071  1.00 63.26  ? 5   PHE C CB  1 
ATOM   1488 C  CG  . PHE C 1 6  ? 26.356  -25.621 27.790  1.00 62.22  ? 5   PHE C CG  1 
ATOM   1489 C  CD1 . PHE C 1 6  ? 27.565  -26.301 27.671  1.00 66.27  ? 5   PHE C CD1 1 
ATOM   1490 C  CD2 . PHE C 1 6  ? 25.945  -24.831 26.720  1.00 62.74  ? 5   PHE C CD2 1 
ATOM   1491 C  CE1 . PHE C 1 6  ? 28.335  -26.205 26.518  1.00 66.52  ? 5   PHE C CE1 1 
ATOM   1492 C  CE2 . PHE C 1 6  ? 26.713  -24.739 25.566  1.00 61.36  ? 5   PHE C CE2 1 
ATOM   1493 C  CZ  . PHE C 1 6  ? 27.902  -25.428 25.464  1.00 66.73  ? 5   PHE C CZ  1 
ATOM   1494 N  N   . LYS C 1 7  ? 23.791  -23.747 31.254  1.00 69.33  ? 6   LYS C N   1 
ATOM   1495 C  CA  . LYS C 1 7  ? 22.794  -23.702 32.314  1.00 68.95  ? 6   LYS C CA  1 
ATOM   1496 C  C   . LYS C 1 7  ? 21.420  -23.809 31.662  1.00 71.44  ? 6   LYS C C   1 
ATOM   1497 O  O   . LYS C 1 7  ? 21.234  -23.303 30.561  1.00 79.76  ? 6   LYS C O   1 
ATOM   1498 C  CB  . LYS C 1 7  ? 22.882  -22.385 33.096  1.00 55.66  ? 6   LYS C CB  1 
ATOM   1499 N  N   . PRO C 1 8  ? 20.419  -24.460 32.300  1.00 78.65  ? 7   PRO C N   1 
ATOM   1500 C  CA  . PRO C 1 8  ? 19.114  -24.675 31.665  1.00 78.76  ? 7   PRO C CA  1 
ATOM   1501 C  C   . PRO C 1 8  ? 18.571  -23.410 31.004  1.00 79.11  ? 7   PRO C C   1 
ATOM   1502 O  O   . PRO C 1 8  ? 18.636  -22.327 31.584  1.00 89.92  ? 7   PRO C O   1 
ATOM   1503 C  CB  . PRO C 1 8  ? 18.183  -25.197 32.780  1.00 76.89  ? 7   PRO C CB  1 
ATOM   1504 C  CG  . PRO C 1 8  ? 19.122  -25.673 33.868  1.00 76.83  ? 7   PRO C CG  1 
ATOM   1505 C  CD  . PRO C 1 8  ? 20.489  -25.022 33.659  1.00 79.51  ? 7   PRO C CD  1 
ATOM   1506 N  N   . GLY C 1 9  ? 18.042  -23.565 29.784  1.00 73.86  ? 8   GLY C N   1 
ATOM   1507 C  CA  . GLY C 1 9  ? 17.534  -22.454 28.992  1.00 58.26  ? 8   GLY C CA  1 
ATOM   1508 C  C   . GLY C 1 9  ? 18.523  -22.060 27.900  1.00 57.38  ? 8   GLY C C   1 
ATOM   1509 O  O   . GLY C 1 9  ? 18.121  -21.438 26.922  1.00 65.74  ? 8   GLY C O   1 
ATOM   1510 N  N   . ASP C 1 10 ? 19.805  -22.424 28.079  1.00 53.40  ? 9   ASP C N   1 
ATOM   1511 C  CA  . ASP C 1 10 ? 20.841  -22.226 27.071  1.00 62.86  ? 9   ASP C CA  1 
ATOM   1512 C  C   . ASP C 1 10 ? 20.435  -22.937 25.764  1.00 62.42  ? 9   ASP C C   1 
ATOM   1513 O  O   . ASP C 1 10 ? 19.990  -24.082 25.796  1.00 58.34  ? 9   ASP C O   1 
ATOM   1514 C  CB  . ASP C 1 10 ? 22.223  -22.551 27.642  1.00 61.58  ? 9   ASP C CB  1 
ATOM   1515 C  CG  . ASP C 1 10 ? 22.737  -21.687 28.800  1.00 69.82  ? 9   ASP C CG  1 
ATOM   1516 O  OD1 . ASP C 1 10 ? 22.032  -20.735 29.189  1.00 66.64  ? 9   ASP C OD1 1 
ATOM   1517 O  OD2 . ASP C 1 10 ? 23.853  -21.956 29.325  1.00 60.94  ? 9   ASP C OD2 1 
ATOM   1518 N  N   . LEU C 1 11 ? 20.592  -22.249 24.614  1.00 68.31  ? 10  LEU C N   1 
ATOM   1519 C  CA  . LEU C 1 11 ? 20.189  -22.718 23.285  1.00 63.66  ? 10  LEU C CA  1 
ATOM   1520 C  C   . LEU C 1 11 ? 21.400  -23.239 22.509  1.00 60.44  ? 10  LEU C C   1 
ATOM   1521 O  O   . LEU C 1 11 ? 22.430  -22.567 22.463  1.00 63.45  ? 10  LEU C O   1 
ATOM   1522 C  CB  . LEU C 1 11 ? 19.458  -21.647 22.467  1.00 52.21  ? 10  LEU C CB  1 
ATOM   1523 C  CG  . LEU C 1 11 ? 18.124  -21.148 23.033  1.00 51.07  ? 10  LEU C CG  1 
ATOM   1524 C  CD1 . LEU C 1 11 ? 17.459  -20.186 22.070  1.00 48.75  ? 10  LEU C CD1 1 
ATOM   1525 C  CD2 . LEU C 1 11 ? 17.203  -22.304 23.345  1.00 48.02  ? 10  LEU C CD2 1 
ATOM   1526 N  N   . VAL C 1 12 ? 21.233  -24.403 21.848  1.00 50.75  ? 11  VAL C N   1 
ATOM   1527 C  CA  . VAL C 1 12 ? 22.345  -25.181 21.316  1.00 50.07  ? 11  VAL C CA  1 
ATOM   1528 C  C   . VAL C 1 12 ? 21.947  -25.953 20.050  1.00 57.31  ? 11  VAL C C   1 
ATOM   1529 O  O   . VAL C 1 12 ? 20.781  -26.319 19.844  1.00 52.95  ? 11  VAL C O   1 
ATOM   1530 C  CB  . VAL C 1 12 ? 22.922  -26.142 22.382  1.00 51.59  ? 11  VAL C CB  1 
ATOM   1531 C  CG1 . VAL C 1 12 ? 23.593  -25.405 23.541  1.00 44.72  ? 11  VAL C CG1 1 
ATOM   1532 C  CG2 . VAL C 1 12 ? 21.878  -27.123 22.911  1.00 44.45  ? 11  VAL C CG2 1 
ATOM   1533 N  N   . PHE C 1 13 ? 22.948  -26.193 19.190  1.00 45.19  ? 12  PHE C N   1 
ATOM   1534 C  CA  . PHE C 1 13 ? 22.946  -27.367 18.333  1.00 55.02  ? 12  PHE C CA  1 
ATOM   1535 C  C   . PHE C 1 13 ? 23.679  -28.478 19.078  1.00 60.15  ? 12  PHE C C   1 
ATOM   1536 O  O   . PHE C 1 13 ? 24.710  -28.239 19.711  1.00 63.21  ? 12  PHE C O   1 
ATOM   1537 C  CB  . PHE C 1 13 ? 23.522  -27.163 16.927  1.00 60.28  ? 12  PHE C CB  1 
ATOM   1538 C  CG  . PHE C 1 13 ? 22.817  -26.086 16.111  1.00 58.74  ? 12  PHE C CG  1 
ATOM   1539 C  CD1 . PHE C 1 13 ? 21.863  -26.423 15.155  1.00 53.53  ? 12  PHE C CD1 1 
ATOM   1540 C  CD2 . PHE C 1 13 ? 23.111  -24.734 16.308  1.00 59.56  ? 12  PHE C CD2 1 
ATOM   1541 C  CE1 . PHE C 1 13 ? 21.230  -25.431 14.417  1.00 50.80  ? 12  PHE C CE1 1 
ATOM   1542 C  CE2 . PHE C 1 13 ? 22.464  -23.744 15.582  1.00 54.54  ? 12  PHE C CE2 1 
ATOM   1543 C  CZ  . PHE C 1 13 ? 21.522  -24.098 14.637  1.00 55.54  ? 12  PHE C CZ  1 
ATOM   1544 N  N   . ALA C 1 14 ? 23.110  -29.685 19.016  1.00 55.57  ? 13  ALA C N   1 
ATOM   1545 C  CA  . ALA C 1 14 ? 23.629  -30.829 19.746  1.00 54.18  ? 13  ALA C CA  1 
ATOM   1546 C  C   . ALA C 1 14 ? 23.828  -31.997 18.787  1.00 57.26  ? 13  ALA C C   1 
ATOM   1547 O  O   . ALA C 1 14 ? 22.873  -32.405 18.127  1.00 40.16  ? 13  ALA C O   1 
ATOM   1548 C  CB  . ALA C 1 14 ? 22.667  -31.190 20.847  1.00 48.87  ? 13  ALA C CB  1 
ATOM   1549 N  N   . LYS C 1 15 ? 25.074  -32.502 18.713  1.00 52.50  ? 14  LYS C N   1 
ATOM   1550 C  CA  . LYS C 1 15 ? 25.429  -33.579 17.803  1.00 53.22  ? 14  LYS C CA  1 
ATOM   1551 C  C   . LYS C 1 15 ? 25.356  -34.918 18.522  1.00 54.35  ? 14  LYS C C   1 
ATOM   1552 O  O   . LYS C 1 15 ? 26.032  -35.121 19.522  1.00 56.50  ? 14  LYS C O   1 
ATOM   1553 C  CB  . LYS C 1 15 ? 26.867  -33.427 17.292  1.00 54.87  ? 14  LYS C CB  1 
ATOM   1554 C  CG  . LYS C 1 15 ? 27.257  -34.333 16.125  1.00 56.50  ? 14  LYS C CG  1 
ATOM   1555 C  CD  . LYS C 1 15 ? 26.604  -34.118 14.761  1.00 59.48  ? 14  LYS C CD  1 
ATOM   1556 C  CE  . LYS C 1 15 ? 26.964  -35.125 13.703  1.00 51.20  ? 14  LYS C CE  1 
ATOM   1557 N  NZ  . LYS C 1 15 ? 26.770  -36.507 14.156  1.00 42.87  ? 14  LYS C NZ  1 
ATOM   1558 N  N   . MET C 1 16 ? 24.571  -35.839 17.962  1.00 51.15  ? 15  MET C N   1 
ATOM   1559 C  CA  . MET C 1 16 ? 24.656  -37.246 18.312  1.00 49.28  ? 15  MET C CA  1 
ATOM   1560 C  C   . MET C 1 16 ? 25.020  -38.043 17.061  1.00 57.38  ? 15  MET C C   1 
ATOM   1561 O  O   . MET C 1 16 ? 24.619  -37.683 15.951  1.00 63.57  ? 15  MET C O   1 
ATOM   1562 C  CB  . MET C 1 16 ? 23.306  -37.749 18.834  1.00 49.81  ? 15  MET C CB  1 
ATOM   1563 C  CG  . MET C 1 16 ? 23.054  -37.364 20.272  1.00 48.22  ? 15  MET C CG  1 
ATOM   1564 S  SD  . MET C 1 16 ? 21.426  -37.868 20.865  1.00 50.90  ? 15  MET C SD  1 
ATOM   1565 C  CE  . MET C 1 16 ? 21.828  -39.555 21.347  1.00 50.52  ? 15  MET C CE  1 
ATOM   1566 N  N   . LYS C 1 17 ? 25.742  -39.151 17.260  1.00 59.84  ? 16  LYS C N   1 
ATOM   1567 C  CA  . LYS C 1 17 ? 26.154  -40.054 16.190  1.00 64.45  ? 16  LYS C CA  1 
ATOM   1568 C  C   . LYS C 1 17 ? 24.965  -40.398 15.285  1.00 53.74  ? 16  LYS C C   1 
ATOM   1569 O  O   . LYS C 1 17 ? 23.896  -40.760 15.758  1.00 57.38  ? 16  LYS C O   1 
ATOM   1570 C  CB  . LYS C 1 17 ? 26.783  -41.294 16.848  1.00 63.53  ? 16  LYS C CB  1 
ATOM   1571 C  CG  . LYS C 1 17 ? 27.481  -42.342 15.975  1.00 59.65  ? 16  LYS C CG  1 
ATOM   1572 C  CD  . LYS C 1 17 ? 28.807  -41.861 15.390  1.00 65.72  ? 16  LYS C CD  1 
ATOM   1573 C  CE  . LYS C 1 17 ? 29.289  -42.811 14.326  1.00 68.31  ? 16  LYS C CE  1 
ATOM   1574 N  NZ  . LYS C 1 17 ? 30.565  -42.411 13.725  1.00 54.10  ? 16  LYS C NZ  1 
ATOM   1575 N  N   . GLY C 1 18 ? 25.164  -40.278 13.970  1.00 62.57  ? 17  GLY C N   1 
ATOM   1576 C  CA  . GLY C 1 18 ? 24.151  -40.657 12.994  1.00 63.96  ? 17  GLY C CA  1 
ATOM   1577 C  C   . GLY C 1 18 ? 23.087  -39.577 12.811  1.00 56.71  ? 17  GLY C C   1 
ATOM   1578 O  O   . GLY C 1 18 ? 22.103  -39.751 12.091  1.00 47.17  ? 17  GLY C O   1 
ATOM   1579 N  N   . TYR C 1 19 ? 23.307  -38.443 13.475  1.00 63.22  ? 18  TYR C N   1 
ATOM   1580 C  CA  . TYR C 1 19 ? 22.343  -37.362 13.430  1.00 64.00  ? 18  TYR C CA  1 
ATOM   1581 C  C   . TYR C 1 19 ? 23.055  -36.068 13.062  1.00 56.13  ? 18  TYR C C   1 
ATOM   1582 O  O   . TYR C 1 19 ? 24.198  -35.869 13.477  1.00 55.53  ? 18  TYR C O   1 
ATOM   1583 C  CB  . TYR C 1 19 ? 21.700  -37.314 14.815  1.00 56.96  ? 18  TYR C CB  1 
ATOM   1584 C  CG  . TYR C 1 19 ? 20.659  -38.394 15.048  1.00 53.87  ? 18  TYR C CG  1 
ATOM   1585 C  CD1 . TYR C 1 19 ? 20.985  -39.619 15.637  1.00 56.50  ? 18  TYR C CD1 1 
ATOM   1586 C  CD2 . TYR C 1 19 ? 19.339  -38.169 14.684  1.00 52.68  ? 18  TYR C CD2 1 
ATOM   1587 C  CE1 . TYR C 1 19 ? 20.021  -40.595 15.856  1.00 51.25  ? 18  TYR C CE1 1 
ATOM   1588 C  CE2 . TYR C 1 19 ? 18.370  -39.133 14.901  1.00 57.26  ? 18  TYR C CE2 1 
ATOM   1589 C  CZ  . TYR C 1 19 ? 18.710  -40.344 15.483  1.00 59.89  ? 18  TYR C CZ  1 
ATOM   1590 O  OH  . TYR C 1 19 ? 17.704  -41.254 15.666  1.00 71.05  ? 18  TYR C OH  1 
ATOM   1591 N  N   . PRO C 1 20 ? 22.386  -35.174 12.293  1.00 46.97  ? 19  PRO C N   1 
ATOM   1592 C  CA  . PRO C 1 20 ? 22.911  -33.833 12.000  1.00 46.51  ? 19  PRO C CA  1 
ATOM   1593 C  C   . PRO C 1 20 ? 22.835  -32.969 13.264  1.00 47.29  ? 19  PRO C C   1 
ATOM   1594 O  O   . PRO C 1 20 ? 21.917  -33.139 14.059  1.00 41.40  ? 19  PRO C O   1 
ATOM   1595 C  CB  . PRO C 1 20 ? 21.942  -33.330 10.883  1.00 49.97  ? 19  PRO C CB  1 
ATOM   1596 C  CG  . PRO C 1 20 ? 20.624  -34.019 11.180  1.00 43.18  ? 19  PRO C CG  1 
ATOM   1597 C  CD  . PRO C 1 20 ? 21.048  -35.407 11.699  1.00 44.22  ? 19  PRO C CD  1 
ATOM   1598 N  N   . HIS C 1 21 ? 23.807  -32.071 13.473  1.00 48.64  ? 20  HIS C N   1 
ATOM   1599 C  CA  . HIS C 1 21 ? 23.782  -31.149 14.610  1.00 47.47  ? 20  HIS C CA  1 
ATOM   1600 C  C   . HIS C 1 21 ? 22.409  -30.477 14.690  1.00 46.62  ? 20  HIS C C   1 
ATOM   1601 O  O   . HIS C 1 21 ? 21.965  -29.842 13.722  1.00 45.38  ? 20  HIS C O   1 
ATOM   1602 C  CB  . HIS C 1 21 ? 24.881  -30.085 14.504  1.00 48.33  ? 20  HIS C CB  1 
ATOM   1603 C  CG  . HIS C 1 21 ? 26.257  -30.618 14.283  1.00 49.53  ? 20  HIS C CG  1 
ATOM   1604 N  ND1 . HIS C 1 21 ? 26.588  -31.408 13.200  1.00 49.68  ? 20  HIS C ND1 1 
ATOM   1605 C  CD2 . HIS C 1 21 ? 27.393  -30.432 14.976  1.00 49.89  ? 20  HIS C CD2 1 
ATOM   1606 C  CE1 . HIS C 1 21 ? 27.878  -31.716 13.268  1.00 53.33  ? 20  HIS C CE1 1 
ATOM   1607 N  NE2 . HIS C 1 21 ? 28.384  -31.145 14.345  1.00 54.57  ? 20  HIS C NE2 1 
ATOM   1608 N  N   . TRP C 1 22 ? 21.746  -30.637 15.845  1.00 42.58  ? 21  TRP C N   1 
ATOM   1609 C  CA  . TRP C 1 22 ? 20.294  -30.462 15.898  1.00 43.08  ? 21  TRP C CA  1 
ATOM   1610 C  C   . TRP C 1 22 ? 19.895  -29.343 16.869  1.00 46.37  ? 21  TRP C C   1 
ATOM   1611 O  O   . TRP C 1 22 ? 20.439  -29.211 17.963  1.00 44.95  ? 21  TRP C O   1 
ATOM   1612 C  CB  . TRP C 1 22 ? 19.666  -31.808 16.265  1.00 32.18  ? 21  TRP C CB  1 
ATOM   1613 C  CG  . TRP C 1 22 ? 18.198  -31.974 15.959  1.00 30.94  ? 21  TRP C CG  1 
ATOM   1614 C  CD1 . TRP C 1 22 ? 17.130  -31.407 16.585  1.00 36.61  ? 21  TRP C CD1 1 
ATOM   1615 C  CD2 . TRP C 1 22 ? 17.660  -32.899 14.989  1.00 38.69  ? 21  TRP C CD2 1 
ATOM   1616 N  NE1 . TRP C 1 22 ? 15.964  -31.844 16.006  1.00 30.84  ? 21  TRP C NE1 1 
ATOM   1617 C  CE2 . TRP C 1 22 ? 16.251  -32.770 15.038  1.00 37.31  ? 21  TRP C CE2 1 
ATOM   1618 C  CE3 . TRP C 1 22 ? 18.226  -33.794 14.072  1.00 36.04  ? 21  TRP C CE3 1 
ATOM   1619 C  CZ2 . TRP C 1 22 ? 15.422  -33.527 14.218  1.00 35.29  ? 21  TRP C CZ2 1 
ATOM   1620 C  CZ3 . TRP C 1 22 ? 17.403  -34.543 13.263  1.00 37.91  ? 21  TRP C CZ3 1 
ATOM   1621 C  CH2 . TRP C 1 22 ? 16.013  -34.419 13.356  1.00 35.92  ? 21  TRP C CH2 1 
ATOM   1622 N  N   . PRO C 1 23 ? 18.919  -28.476 16.501  1.00 51.19  ? 22  PRO C N   1 
ATOM   1623 C  CA  . PRO C 1 23 ? 18.480  -27.394 17.387  1.00 51.04  ? 22  PRO C CA  1 
ATOM   1624 C  C   . PRO C 1 23 ? 17.919  -27.911 18.713  1.00 49.69  ? 22  PRO C C   1 
ATOM   1625 O  O   . PRO C 1 23 ? 17.031  -28.760 18.719  1.00 50.62  ? 22  PRO C O   1 
ATOM   1626 C  CB  . PRO C 1 23 ? 17.410  -26.700 16.508  1.00 47.73  ? 22  PRO C CB  1 
ATOM   1627 C  CG  . PRO C 1 23 ? 16.893  -27.802 15.597  1.00 44.74  ? 22  PRO C CG  1 
ATOM   1628 C  CD  . PRO C 1 23 ? 18.183  -28.500 15.224  1.00 47.72  ? 22  PRO C CD  1 
ATOM   1629 N  N   . ALA C 1 24 ? 18.415  -27.354 19.831  1.00 49.50  ? 23  ALA C N   1 
ATOM   1630 C  CA  . ALA C 1 24 ? 18.172  -27.923 21.154  1.00 53.59  ? 23  ALA C CA  1 
ATOM   1631 C  C   . ALA C 1 24 ? 18.367  -26.872 22.255  1.00 52.46  ? 23  ALA C C   1 
ATOM   1632 O  O   . ALA C 1 24 ? 18.743  -25.740 21.962  1.00 55.33  ? 23  ALA C O   1 
ATOM   1633 C  CB  . ALA C 1 24 ? 19.029  -29.169 21.357  1.00 47.52  ? 23  ALA C CB  1 
ATOM   1634 N  N   . ARG C 1 25 ? 18.036  -27.245 23.503  1.00 61.43  ? 24  ARG C N   1 
ATOM   1635 C  CA  . ARG C 1 25 ? 18.227  -26.430 24.702  1.00 54.61  ? 24  ARG C CA  1 
ATOM   1636 C  C   . ARG C 1 25 ? 18.600  -27.323 25.893  1.00 56.59  ? 24  ARG C C   1 
ATOM   1637 O  O   . ARG C 1 25 ? 18.152  -28.472 25.965  1.00 62.71  ? 24  ARG C O   1 
ATOM   1638 C  CB  . ARG C 1 25 ? 17.000  -25.565 25.049  1.00 53.97  ? 24  ARG C CB  1 
ATOM   1639 C  CG  . ARG C 1 25 ? 15.724  -26.335 25.349  1.00 48.28  ? 24  ARG C CG  1 
ATOM   1640 C  CD  . ARG C 1 25 ? 14.497  -25.536 25.794  1.00 46.80  ? 24  ARG C CD  1 
ATOM   1641 N  NE  . ARG C 1 25 ? 13.340  -26.443 25.924  1.00 47.97  ? 24  ARG C NE  1 
ATOM   1642 C  CZ  . ARG C 1 25 ? 12.047  -26.074 25.942  1.00 52.20  ? 24  ARG C CZ  1 
ATOM   1643 N  NH1 . ARG C 1 25 ? 11.705  -24.802 25.795  1.00 50.41  ? 24  ARG C NH1 1 
ATOM   1644 N  NH2 . ARG C 1 25 ? 11.088  -26.978 26.072  1.00 47.13  ? 24  ARG C NH2 1 
ATOM   1645 N  N   . ILE C 1 26 ? 19.405  -26.784 26.832  1.00 52.79  ? 25  ILE C N   1 
ATOM   1646 C  CA  . ILE C 1 26 ? 19.683  -27.431 28.115  1.00 54.69  ? 25  ILE C CA  1 
ATOM   1647 C  C   . ILE C 1 26 ? 18.423  -27.414 28.983  1.00 54.31  ? 25  ILE C C   1 
ATOM   1648 O  O   . ILE C 1 26 ? 17.815  -26.369 29.174  1.00 56.32  ? 25  ILE C O   1 
ATOM   1649 C  CB  . ILE C 1 26 ? 20.884  -26.795 28.860  1.00 50.61  ? 25  ILE C CB  1 
ATOM   1650 C  CG1 . ILE C 1 26 ? 22.058  -26.409 27.939  1.00 48.21  ? 25  ILE C CG1 1 
ATOM   1651 C  CG2 . ILE C 1 26 ? 21.340  -27.668 30.027  1.00 51.67  ? 25  ILE C CG2 1 
ATOM   1652 C  CD1 . ILE C 1 26 ? 22.518  -27.502 26.990  1.00 45.55  ? 25  ILE C CD1 1 
ATOM   1653 N  N   . ASP C 1 27 ? 18.028  -28.594 29.476  1.00 63.53  ? 26  ASP C N   1 
ATOM   1654 C  CA  . ASP C 1 27 ? 16.999  -28.750 30.498  1.00 71.65  ? 26  ASP C CA  1 
ATOM   1655 C  C   . ASP C 1 27 ? 17.634  -28.736 31.892  1.00 71.91  ? 26  ASP C C   1 
ATOM   1656 O  O   . ASP C 1 27 ? 18.860  -28.732 32.014  1.00 68.71  ? 26  ASP C O   1 
ATOM   1657 C  CB  . ASP C 1 27 ? 16.176  -30.008 30.261  1.00 71.55  ? 26  ASP C CB  1 
ATOM   1658 C  CG  . ASP C 1 27 ? 14.853  -29.812 29.535  1.00 75.03  ? 26  ASP C CG  1 
ATOM   1659 O  OD1 . ASP C 1 27 ? 14.858  -29.170 28.455  1.00 63.29  ? 26  ASP C OD1 1 
ATOM   1660 O  OD2 . ASP C 1 27 ? 13.826  -30.310 30.059  1.00 71.69  ? 26  ASP C OD2 1 
ATOM   1661 N  N   . ASP C 1 28 ? 16.788  -28.756 32.936  1.00 73.82  ? 27  ASP C N   1 
ATOM   1662 C  CA  . ASP C 1 28 ? 17.232  -28.670 34.321  1.00 77.97  ? 27  ASP C CA  1 
ATOM   1663 C  C   . ASP C 1 28 ? 17.200  -30.056 34.979  1.00 83.23  ? 27  ASP C C   1 
ATOM   1664 O  O   . ASP C 1 28 ? 16.248  -30.810 34.680  1.00 80.09  ? 27  ASP C O   1 
ATOM   1665 C  CB  . ASP C 1 28 ? 16.447  -27.621 35.093  1.00 74.72  ? 27  ASP C CB  1 
ATOM   1666 N  N   . ALA C 1 33 ? 14.448  -37.663 41.345  1.00 64.74  ? 32  ALA C N   1 
ATOM   1667 C  CA  . ALA C 1 33 ? 14.728  -37.815 39.895  1.00 69.95  ? 32  ALA C CA  1 
ATOM   1668 C  C   . ALA C 1 33 ? 16.176  -38.258 39.692  1.00 67.18  ? 32  ALA C C   1 
ATOM   1669 O  O   . ALA C 1 33 ? 16.978  -38.226 40.622  1.00 58.60  ? 32  ALA C O   1 
ATOM   1670 C  CB  . ALA C 1 33 ? 14.385  -36.552 39.123  1.00 59.78  ? 32  ALA C CB  1 
ATOM   1671 N  N   . VAL C 1 34 ? 16.492  -38.701 38.468  1.00 82.68  ? 33  VAL C N   1 
ATOM   1672 C  CA  . VAL C 1 34 ? 17.700  -39.467 38.191  1.00 82.87  ? 33  VAL C CA  1 
ATOM   1673 C  C   . VAL C 1 34 ? 18.864  -38.525 37.900  1.00 79.92  ? 33  VAL C C   1 
ATOM   1674 O  O   . VAL C 1 34 ? 18.683  -37.490 37.257  1.00 77.04  ? 33  VAL C O   1 
ATOM   1675 C  CB  . VAL C 1 34 ? 17.526  -40.527 37.081  1.00 84.82  ? 33  VAL C CB  1 
ATOM   1676 C  CG1 . VAL C 1 34 ? 18.787  -40.744 36.248  1.00 92.32  ? 33  VAL C CG1 1 
ATOM   1677 C  CG2 . VAL C 1 34 ? 17.024  -41.852 37.637  1.00 88.14  ? 33  VAL C CG2 1 
ATOM   1678 N  N   . LYS C 1 35 ? 20.048  -38.926 38.392  1.00 75.70  ? 34  LYS C N   1 
ATOM   1679 C  CA  . LYS C 1 35 ? 21.326  -38.292 38.112  1.00 75.14  ? 34  LYS C CA  1 
ATOM   1680 C  C   . LYS C 1 35 ? 21.617  -38.338 36.615  1.00 71.99  ? 34  LYS C C   1 
ATOM   1681 O  O   . LYS C 1 35 ? 21.559  -39.407 35.995  1.00 72.59  ? 34  LYS C O   1 
ATOM   1682 C  CB  . LYS C 1 35 ? 22.480  -39.033 38.804  1.00 71.99  ? 34  LYS C CB  1 
ATOM   1683 N  N   . PRO C 1 36 ? 21.952  -37.180 35.999  1.00 71.78  ? 35  PRO C N   1 
ATOM   1684 C  CA  . PRO C 1 36 ? 22.632  -37.173 34.702  1.00 74.91  ? 35  PRO C CA  1 
ATOM   1685 C  C   . PRO C 1 36 ? 23.960  -37.890 34.940  1.00 79.06  ? 35  PRO C C   1 
ATOM   1686 O  O   . PRO C 1 36 ? 24.602  -37.668 35.974  1.00 67.86  ? 35  PRO C O   1 
ATOM   1687 C  CB  . PRO C 1 36 ? 22.835  -35.677 34.373  1.00 82.07  ? 35  PRO C CB  1 
ATOM   1688 C  CG  . PRO C 1 36 ? 21.879  -34.943 35.300  1.00 88.48  ? 35  PRO C CG  1 
ATOM   1689 C  CD  . PRO C 1 36 ? 21.714  -35.826 36.530  1.00 82.90  ? 35  PRO C CD  1 
ATOM   1690 N  N   . PRO C 1 37 ? 24.390  -38.799 34.033  1.00 71.34  ? 36  PRO C N   1 
ATOM   1691 C  CA  . PRO C 1 37 ? 25.701  -39.439 34.160  1.00 72.01  ? 36  PRO C CA  1 
ATOM   1692 C  C   . PRO C 1 37 ? 26.764  -38.402 34.507  1.00 66.15  ? 36  PRO C C   1 
ATOM   1693 O  O   . PRO C 1 37 ? 26.537  -37.208 34.342  1.00 64.99  ? 36  PRO C O   1 
ATOM   1694 C  CB  . PRO C 1 37 ? 25.894  -40.079 32.779  1.00 72.51  ? 36  PRO C CB  1 
ATOM   1695 C  CG  . PRO C 1 37 ? 24.479  -40.456 32.383  1.00 73.93  ? 36  PRO C CG  1 
ATOM   1696 C  CD  . PRO C 1 37 ? 23.632  -39.283 32.867  1.00 74.32  ? 36  PRO C CD  1 
ATOM   1697 N  N   . PRO C 1 38 ? 27.920  -38.816 35.077  1.00 68.60  ? 37  PRO C N   1 
ATOM   1698 C  CA  . PRO C 1 38 ? 29.023  -37.891 35.340  1.00 61.15  ? 37  PRO C CA  1 
ATOM   1699 C  C   . PRO C 1 38 ? 29.252  -37.013 34.121  1.00 47.59  ? 37  PRO C C   1 
ATOM   1700 O  O   . PRO C 1 38 ? 29.442  -37.530 33.028  1.00 59.67  ? 37  PRO C O   1 
ATOM   1701 C  CB  . PRO C 1 38 ? 30.222  -38.833 35.595  1.00 61.13  ? 37  PRO C CB  1 
ATOM   1702 C  CG  . PRO C 1 38 ? 29.582  -40.072 36.186  1.00 67.43  ? 37  PRO C CG  1 
ATOM   1703 C  CD  . PRO C 1 38 ? 28.211  -40.191 35.524  1.00 69.05  ? 37  PRO C CD  1 
ATOM   1704 N  N   . ASN C 1 39 ? 29.184  -35.691 34.323  1.00 51.12  ? 38  ASN C N   1 
ATOM   1705 C  CA  . ASN C 1 39 ? 29.607  -34.691 33.352  1.00 47.05  ? 38  ASN C CA  1 
ATOM   1706 C  C   . ASN C 1 39 ? 28.665  -34.593 32.149  1.00 47.96  ? 38  ASN C C   1 
ATOM   1707 O  O   . ASN C 1 39 ? 29.090  -34.163 31.083  1.00 45.30  ? 38  ASN C O   1 
ATOM   1708 C  CB  . ASN C 1 39 ? 31.037  -34.925 32.874  1.00 55.36  ? 38  ASN C CB  1 
ATOM   1709 C  CG  . ASN C 1 39 ? 31.555  -33.792 32.018  1.00 65.25  ? 38  ASN C CG  1 
ATOM   1710 O  OD1 . ASN C 1 39 ? 31.338  -32.617 32.337  1.00 67.11  ? 38  ASN C OD1 1 
ATOM   1711 N  ND2 . ASN C 1 39 ? 32.252  -34.119 30.939  1.00 67.08  ? 38  ASN C ND2 1 
ATOM   1712 N  N   . LYS C 1 40 ? 27.385  -34.935 32.325  1.00 51.18  ? 39  LYS C N   1 
ATOM   1713 C  CA  . LYS C 1 40 ? 26.459  -34.950 31.198  1.00 56.78  ? 39  LYS C CA  1 
ATOM   1714 C  C   . LYS C 1 40 ? 25.391  -33.879 31.370  1.00 54.45  ? 39  LYS C C   1 
ATOM   1715 O  O   . LYS C 1 40 ? 24.993  -33.589 32.496  1.00 64.61  ? 39  LYS C O   1 
ATOM   1716 C  CB  . LYS C 1 40 ? 25.715  -36.293 31.109  1.00 62.19  ? 39  LYS C CB  1 
ATOM   1717 C  CG  . LYS C 1 40 ? 26.553  -37.485 30.684  1.00 54.97  ? 39  LYS C CG  1 
ATOM   1718 C  CD  . LYS C 1 40 ? 27.304  -37.284 29.377  1.00 58.55  ? 39  LYS C CD  1 
ATOM   1719 C  CE  . LYS C 1 40 ? 28.402  -38.299 29.215  1.00 71.27  ? 39  LYS C CE  1 
ATOM   1720 N  NZ  . LYS C 1 40 ? 29.010  -38.336 27.877  1.00 66.53  ? 39  LYS C NZ  1 
ATOM   1721 N  N   . TYR C 1 41 ? 24.883  -33.347 30.248  1.00 53.45  ? 40  TYR C N   1 
ATOM   1722 C  CA  . TYR C 1 41 ? 23.824  -32.350 30.321  1.00 54.97  ? 40  TYR C CA  1 
ATOM   1723 C  C   . TYR C 1 41 ? 22.529  -32.921 29.754  1.00 51.24  ? 40  TYR C C   1 
ATOM   1724 O  O   . TYR C 1 41 ? 22.546  -33.529 28.691  1.00 56.32  ? 40  TYR C O   1 
ATOM   1725 C  CB  . TYR C 1 41 ? 24.170  -31.122 29.474  1.00 49.84  ? 40  TYR C CB  1 
ATOM   1726 C  CG  . TYR C 1 41 ? 25.377  -30.340 29.967  1.00 59.74  ? 40  TYR C CG  1 
ATOM   1727 C  CD1 . TYR C 1 41 ? 26.668  -30.709 29.596  1.00 47.40  ? 40  TYR C CD1 1 
ATOM   1728 C  CD2 . TYR C 1 41 ? 25.220  -29.218 30.796  1.00 59.07  ? 40  TYR C CD2 1 
ATOM   1729 C  CE1 . TYR C 1 41 ? 27.769  -29.987 30.047  1.00 58.86  ? 40  TYR C CE1 1 
ATOM   1730 C  CE2 . TYR C 1 41 ? 26.315  -28.490 31.245  1.00 55.87  ? 40  TYR C CE2 1 
ATOM   1731 C  CZ  . TYR C 1 41 ? 27.592  -28.880 30.873  1.00 56.96  ? 40  TYR C CZ  1 
ATOM   1732 O  OH  . TYR C 1 41 ? 28.663  -28.161 31.318  1.00 63.93  ? 40  TYR C OH  1 
ATOM   1733 N  N   . PRO C 1 42 ? 21.359  -32.661 30.382  1.00 53.36  ? 41  PRO C N   1 
ATOM   1734 C  CA  . PRO C 1 42 ? 20.077  -33.047 29.782  1.00 54.69  ? 41  PRO C CA  1 
ATOM   1735 C  C   . PRO C 1 42 ? 19.716  -32.106 28.629  1.00 50.87  ? 41  PRO C C   1 
ATOM   1736 O  O   . PRO C 1 42 ? 19.782  -30.881 28.750  1.00 45.16  ? 41  PRO C O   1 
ATOM   1737 C  CB  . PRO C 1 42 ? 19.070  -33.001 30.957  1.00 55.09  ? 41  PRO C CB  1 
ATOM   1738 C  CG  . PRO C 1 42 ? 19.703  -32.049 31.972  1.00 57.58  ? 41  PRO C CG  1 
ATOM   1739 C  CD  . PRO C 1 42 ? 21.202  -31.923 31.654  1.00 51.56  ? 41  PRO C CD  1 
ATOM   1740 N  N   . ILE C 1 43 ? 19.338  -32.700 27.496  1.00 50.40  ? 42  ILE C N   1 
ATOM   1741 C  CA  . ILE C 1 43 ? 19.087  -31.952 26.276  1.00 45.03  ? 42  ILE C CA  1 
ATOM   1742 C  C   . ILE C 1 43 ? 17.630  -32.157 25.873  1.00 44.23  ? 42  ILE C C   1 
ATOM   1743 O  O   . ILE C 1 43 ? 17.082  -33.243 26.057  1.00 46.20  ? 42  ILE C O   1 
ATOM   1744 C  CB  . ILE C 1 43 ? 20.063  -32.417 25.188  1.00 43.01  ? 42  ILE C CB  1 
ATOM   1745 C  CG1 . ILE C 1 43 ? 21.537  -32.349 25.652  1.00 39.74  ? 42  ILE C CG1 1 
ATOM   1746 C  CG2 . ILE C 1 43 ? 19.818  -31.721 23.847  1.00 49.06  ? 42  ILE C CG2 1 
ATOM   1747 C  CD1 . ILE C 1 43 ? 22.039  -30.998 26.132  1.00 40.88  ? 42  ILE C CD1 1 
ATOM   1748 N  N   . PHE C 1 44 ? 17.020  -31.104 25.315  1.00 48.06  ? 43  PHE C N   1 
ATOM   1749 C  CA  . PHE C 1 44 ? 15.706  -31.213 24.696  1.00 43.92  ? 43  PHE C CA  1 
ATOM   1750 C  C   . PHE C 1 44 ? 15.799  -30.810 23.234  1.00 46.33  ? 43  PHE C C   1 
ATOM   1751 O  O   . PHE C 1 44 ? 16.164  -29.674 22.952  1.00 56.06  ? 43  PHE C O   1 
ATOM   1752 C  CB  . PHE C 1 44 ? 14.740  -30.235 25.339  1.00 42.49  ? 43  PHE C CB  1 
ATOM   1753 C  CG  . PHE C 1 44 ? 13.363  -30.137 24.703  1.00 43.87  ? 43  PHE C CG  1 
ATOM   1754 C  CD1 . PHE C 1 44 ? 12.337  -30.978 25.111  1.00 44.15  ? 43  PHE C CD1 1 
ATOM   1755 C  CD2 . PHE C 1 44 ? 13.093  -29.159 23.744  1.00 46.95  ? 43  PHE C CD2 1 
ATOM   1756 C  CE1 . PHE C 1 44 ? 11.070  -30.848 24.560  1.00 51.37  ? 43  PHE C CE1 1 
ATOM   1757 C  CE2 . PHE C 1 44 ? 11.832  -29.043 23.182  1.00 49.53  ? 43  PHE C CE2 1 
ATOM   1758 C  CZ  . PHE C 1 44 ? 10.825  -29.890 23.588  1.00 49.49  ? 43  PHE C CZ  1 
ATOM   1759 N  N   . PHE C 1 45 ? 15.465  -31.757 22.336  1.00 50.33  ? 44  PHE C N   1 
ATOM   1760 C  CA  . PHE C 1 45 ? 15.551  -31.585 20.888  1.00 42.25  ? 44  PHE C CA  1 
ATOM   1761 C  C   . PHE C 1 45 ? 14.271  -30.909 20.402  1.00 44.48  ? 44  PHE C C   1 
ATOM   1762 O  O   . PHE C 1 45 ? 13.163  -31.424 20.608  1.00 44.72  ? 44  PHE C O   1 
ATOM   1763 C  CB  . PHE C 1 45 ? 15.884  -32.864 20.097  1.00 35.08  ? 44  PHE C CB  1 
ATOM   1764 C  CG  . PHE C 1 45 ? 17.227  -33.497 20.460  1.00 36.03  ? 44  PHE C CG  1 
ATOM   1765 C  CD1 . PHE C 1 45 ? 18.393  -33.128 19.793  1.00 33.10  ? 44  PHE C CD1 1 
ATOM   1766 C  CD2 . PHE C 1 45 ? 17.329  -34.392 21.531  1.00 37.08  ? 44  PHE C CD2 1 
ATOM   1767 C  CE1 . PHE C 1 45 ? 19.636  -33.664 20.148  1.00 32.35  ? 44  PHE C CE1 1 
ATOM   1768 C  CE2 . PHE C 1 45 ? 18.571  -34.921 21.897  1.00 43.55  ? 44  PHE C CE2 1 
ATOM   1769 C  CZ  . PHE C 1 45 ? 19.714  -34.563 21.210  1.00 35.11  ? 44  PHE C CZ  1 
ATOM   1770 N  N   . PHE C 1 46 ? 14.463  -29.755 19.744  1.00 51.31  ? 45  PHE C N   1 
ATOM   1771 C  CA  . PHE C 1 46 ? 13.405  -29.024 19.057  1.00 42.55  ? 45  PHE C CA  1 
ATOM   1772 C  C   . PHE C 1 46 ? 12.874  -29.857 17.901  1.00 45.56  ? 45  PHE C C   1 
ATOM   1773 O  O   . PHE C 1 46 ? 13.630  -30.528 17.201  1.00 44.00  ? 45  PHE C O   1 
ATOM   1774 C  CB  . PHE C 1 46 ? 13.765  -27.609 18.584  1.00 38.86  ? 45  PHE C CB  1 
ATOM   1775 C  CG  . PHE C 1 46 ? 13.988  -26.635 19.738  1.00 44.46  ? 45  PHE C CG  1 
ATOM   1776 C  CD1 . PHE C 1 46 ? 12.913  -26.151 20.475  1.00 41.08  ? 45  PHE C CD1 1 
ATOM   1777 C  CD2 . PHE C 1 46 ? 15.276  -26.219 20.087  1.00 41.31  ? 45  PHE C CD2 1 
ATOM   1778 C  CE1 . PHE C 1 46 ? 13.116  -25.237 21.508  1.00 45.81  ? 45  PHE C CE1 1 
ATOM   1779 C  CE2 . PHE C 1 46 ? 15.474  -25.303 21.118  1.00 45.73  ? 45  PHE C CE2 1 
ATOM   1780 C  CZ  . PHE C 1 46 ? 14.399  -24.824 21.828  1.00 46.44  ? 45  PHE C CZ  1 
ATOM   1781 N  N   . GLY C 1 47 ? 11.550  -29.783 17.721  1.00 48.62  ? 46  GLY C N   1 
ATOM   1782 C  CA  . GLY C 1 47 ? 10.891  -30.476 16.636  1.00 44.04  ? 46  GLY C CA  1 
ATOM   1783 C  C   . GLY C 1 47 ? 10.479  -31.881 17.061  1.00 51.92  ? 46  GLY C C   1 
ATOM   1784 O  O   . GLY C 1 47 ? 9.285   -32.173 17.150  1.00 47.83  ? 46  GLY C O   1 
ATOM   1785 N  N   . THR C 1 48 ? 11.480  -32.746 17.284  1.00 47.69  ? 47  THR C N   1 
ATOM   1786 C  CA  . THR C 1 48 ? 11.224  -34.113 17.712  1.00 51.70  ? 47  THR C CA  1 
ATOM   1787 C  C   . THR C 1 48 ? 10.630  -34.093 19.114  1.00 46.89  ? 47  THR C C   1 
ATOM   1788 O  O   . THR C 1 48 ? 9.782   -34.936 19.406  1.00 47.57  ? 47  THR C O   1 
ATOM   1789 C  CB  . THR C 1 48 ? 12.489  -34.972 17.662  1.00 52.84  ? 47  THR C CB  1 
ATOM   1790 O  OG1 . THR C 1 48 ? 13.393  -34.386 18.591  1.00 51.95  ? 47  THR C OG1 1 
ATOM   1791 C  CG2 . THR C 1 48 ? 13.071  -35.063 16.265  1.00 50.29  ? 47  THR C CG2 1 
ATOM   1792 N  N   . HIS C 1 49 ? 11.098  -33.132 19.943  1.00 50.59  ? 48  HIS C N   1 
ATOM   1793 C  CA  . HIS C 1 49 ? 10.745  -32.965 21.348  1.00 57.29  ? 48  HIS C CA  1 
ATOM   1794 C  C   . HIS C 1 49 ? 11.310  -34.110 22.194  1.00 63.55  ? 48  HIS C C   1 
ATOM   1795 O  O   . HIS C 1 49 ? 10.850  -34.370 23.304  1.00 59.28  ? 48  HIS C O   1 
ATOM   1796 C  CB  . HIS C 1 49 ? 9.233   -32.764 21.514  1.00 59.36  ? 48  HIS C CB  1 
ATOM   1797 C  CG  . HIS C 1 49 ? 8.712   -31.626 20.714  1.00 63.60  ? 48  HIS C CG  1 
ATOM   1798 N  ND1 . HIS C 1 49 ? 7.429   -31.597 20.212  1.00 60.34  ? 48  HIS C ND1 1 
ATOM   1799 C  CD2 . HIS C 1 49 ? 9.300   -30.480 20.321  1.00 65.08  ? 48  HIS C CD2 1 
ATOM   1800 C  CE1 . HIS C 1 49 ? 7.253   -30.467 19.540  1.00 61.91  ? 48  HIS C CE1 1 
ATOM   1801 N  NE2 . HIS C 1 49 ? 8.376   -29.774 19.590  1.00 66.19  ? 48  HIS C NE2 1 
ATOM   1802 N  N   . GLU C 1 50 ? 12.331  -34.796 21.671  1.00 64.41  ? 49  GLU C N   1 
ATOM   1803 C  CA  . GLU C 1 50 ? 12.986  -35.844 22.429  1.00 55.07  ? 49  GLU C CA  1 
ATOM   1804 C  C   . GLU C 1 50 ? 13.932  -35.223 23.454  1.00 54.95  ? 49  GLU C C   1 
ATOM   1805 O  O   . GLU C 1 50 ? 14.116  -34.004 23.476  1.00 49.27  ? 49  GLU C O   1 
ATOM   1806 C  CB  . GLU C 1 50 ? 13.609  -36.824 21.441  1.00 58.84  ? 49  GLU C CB  1 
ATOM   1807 C  CG  . GLU C 1 50 ? 12.543  -37.607 20.682  1.00 64.79  ? 49  GLU C CG  1 
ATOM   1808 C  CD  . GLU C 1 50 ? 13.061  -38.726 19.800  1.00 73.94  ? 49  GLU C CD  1 
ATOM   1809 O  OE1 . GLU C 1 50 ? 14.283  -38.996 19.791  1.00 80.27  ? 49  GLU C OE1 1 
ATOM   1810 O  OE2 . GLU C 1 50 ? 12.214  -39.336 19.117  1.00 81.08  ? 49  GLU C OE2 1 
ATOM   1811 N  N   . THR C 1 51 ? 14.469  -36.071 24.345  1.00 57.64  ? 50  THR C N   1 
ATOM   1812 C  CA  . THR C 1 51 ? 15.484  -35.676 25.311  1.00 51.95  ? 50  THR C CA  1 
ATOM   1813 C  C   . THR C 1 51 ? 16.666  -36.638 25.211  1.00 50.98  ? 50  THR C C   1 
ATOM   1814 O  O   . THR C 1 51 ? 16.553  -37.721 24.636  1.00 45.83  ? 50  THR C O   1 
ATOM   1815 C  CB  . THR C 1 51 ? 14.887  -35.659 26.715  1.00 64.47  ? 50  THR C CB  1 
ATOM   1816 O  OG1 . THR C 1 51 ? 14.479  -37.003 26.958  1.00 73.62  ? 50  THR C OG1 1 
ATOM   1817 C  CG2 . THR C 1 51 ? 13.692  -34.730 26.835  1.00 74.65  ? 50  THR C CG2 1 
ATOM   1818 N  N   . ALA C 1 52 ? 17.808  -36.218 25.764  1.00 52.20  ? 51  ALA C N   1 
ATOM   1819 C  CA  . ALA C 1 52 ? 18.980  -37.077 25.845  1.00 52.29  ? 51  ALA C CA  1 
ATOM   1820 C  C   . ALA C 1 52 ? 20.042  -36.398 26.697  1.00 48.82  ? 51  ALA C C   1 
ATOM   1821 O  O   . ALA C 1 52 ? 19.992  -35.190 26.890  1.00 54.80  ? 51  ALA C O   1 
ATOM   1822 C  CB  . ALA C 1 52 ? 19.502  -37.427 24.467  1.00 45.48  ? 51  ALA C CB  1 
ATOM   1823 N  N   . PHE C 1 53 ? 20.996  -37.184 27.197  1.00 50.55  ? 52  PHE C N   1 
ATOM   1824 C  CA  . PHE C 1 53 ? 22.054  -36.645 28.045  1.00 52.93  ? 52  PHE C CA  1 
ATOM   1825 C  C   . PHE C 1 53 ? 23.307  -36.527 27.196  1.00 46.63  ? 52  PHE C C   1 
ATOM   1826 O  O   . PHE C 1 53 ? 23.775  -37.553 26.724  1.00 41.84  ? 52  PHE C O   1 
ATOM   1827 C  CB  . PHE C 1 53 ? 22.390  -37.537 29.248  1.00 50.97  ? 52  PHE C CB  1 
ATOM   1828 C  CG  . PHE C 1 53 ? 21.362  -37.431 30.358  1.00 61.30  ? 52  PHE C CG  1 
ATOM   1829 C  CD1 . PHE C 1 53 ? 21.386  -36.360 31.246  1.00 59.60  ? 52  PHE C CD1 1 
ATOM   1830 C  CD2 . PHE C 1 53 ? 20.344  -38.369 30.476  1.00 70.38  ? 52  PHE C CD2 1 
ATOM   1831 C  CE1 . PHE C 1 53 ? 20.427  -36.242 32.234  1.00 54.44  ? 52  PHE C CE1 1 
ATOM   1832 C  CE2 . PHE C 1 53 ? 19.390  -38.250 31.476  1.00 67.95  ? 52  PHE C CE2 1 
ATOM   1833 C  CZ  . PHE C 1 53 ? 19.436  -37.186 32.350  1.00 61.33  ? 52  PHE C CZ  1 
ATOM   1834 N  N   . LEU C 1 54 ? 23.813  -35.292 27.031  1.00 48.25  ? 53  LEU C N   1 
ATOM   1835 C  CA  . LEU C 1 54 ? 24.966  -35.024 26.180  1.00 50.82  ? 53  LEU C CA  1 
ATOM   1836 C  C   . LEU C 1 54 ? 26.127  -34.413 26.963  1.00 51.24  ? 53  LEU C C   1 
ATOM   1837 O  O   . LEU C 1 54 ? 25.952  -33.578 27.855  1.00 55.35  ? 53  LEU C O   1 
ATOM   1838 C  CB  . LEU C 1 54 ? 24.652  -34.274 24.884  1.00 45.42  ? 53  LEU C CB  1 
ATOM   1839 C  CG  . LEU C 1 54 ? 23.841  -35.069 23.851  1.00 53.23  ? 53  LEU C CG  1 
ATOM   1840 C  CD1 . LEU C 1 54 ? 23.578  -34.240 22.613  1.00 60.75  ? 53  LEU C CD1 1 
ATOM   1841 C  CD2 . LEU C 1 54 ? 24.505  -36.402 23.487  1.00 46.83  ? 53  LEU C CD2 1 
ATOM   1842 N  N   . GLY C 1 55 ? 27.323  -34.892 26.617  1.00 54.30  ? 54  GLY C N   1 
ATOM   1843 C  CA  . GLY C 1 55 ? 28.573  -34.384 27.146  1.00 53.72  ? 54  GLY C CA  1 
ATOM   1844 C  C   . GLY C 1 55 ? 28.926  -33.066 26.471  1.00 63.12  ? 54  GLY C C   1 
ATOM   1845 O  O   . GLY C 1 55 ? 28.464  -32.798 25.358  1.00 70.05  ? 54  GLY C O   1 
ATOM   1846 N  N   . PRO C 1 56 ? 29.756  -32.220 27.129  1.00 70.14  ? 55  PRO C N   1 
ATOM   1847 C  CA  . PRO C 1 56 ? 30.086  -30.883 26.627  1.00 67.79  ? 55  PRO C CA  1 
ATOM   1848 C  C   . PRO C 1 56 ? 30.746  -30.766 25.253  1.00 64.61  ? 55  PRO C C   1 
ATOM   1849 O  O   . PRO C 1 56 ? 30.642  -29.719 24.621  1.00 74.41  ? 55  PRO C O   1 
ATOM   1850 C  CB  . PRO C 1 56 ? 30.970  -30.320 27.763  1.00 66.49  ? 55  PRO C CB  1 
ATOM   1851 C  CG  . PRO C 1 56 ? 31.589  -31.551 28.392  1.00 59.81  ? 55  PRO C CG  1 
ATOM   1852 C  CD  . PRO C 1 56 ? 30.418  -32.509 28.414  1.00 67.99  ? 55  PRO C CD  1 
ATOM   1853 N  N   . LYS C 1 57 ? 31.389  -31.842 24.781  1.00 60.14  ? 56  LYS C N   1 
ATOM   1854 C  CA  . LYS C 1 57 ? 31.993  -31.849 23.453  1.00 65.26  ? 56  LYS C CA  1 
ATOM   1855 C  C   . LYS C 1 57 ? 30.928  -31.814 22.350  1.00 65.41  ? 56  LYS C C   1 
ATOM   1856 O  O   . LYS C 1 57 ? 31.197  -31.315 21.260  1.00 61.31  ? 56  LYS C O   1 
ATOM   1857 C  CB  . LYS C 1 57 ? 32.986  -33.004 23.277  1.00 58.49  ? 56  LYS C CB  1 
ATOM   1858 N  N   . ASP C 1 58 ? 29.719  -32.317 22.648  1.00 69.18  ? 57  ASP C N   1 
ATOM   1859 C  CA  . ASP C 1 58 ? 28.673  -32.528 21.654  1.00 62.09  ? 57  ASP C CA  1 
ATOM   1860 C  C   . ASP C 1 58 ? 27.865  -31.254 21.408  1.00 58.45  ? 57  ASP C C   1 
ATOM   1861 O  O   . ASP C 1 58 ? 27.032  -31.226 20.505  1.00 63.89  ? 57  ASP C O   1 
ATOM   1862 C  CB  . ASP C 1 58 ? 27.684  -33.600 22.091  1.00 67.11  ? 57  ASP C CB  1 
ATOM   1863 C  CG  . ASP C 1 58 ? 28.259  -34.982 22.380  1.00 73.34  ? 57  ASP C CG  1 
ATOM   1864 O  OD1 . ASP C 1 58 ? 28.851  -35.570 21.454  1.00 74.69  ? 57  ASP C OD1 1 
ATOM   1865 O  OD2 . ASP C 1 58 ? 28.087  -35.469 23.523  1.00 65.64  ? 57  ASP C OD2 1 
ATOM   1866 N  N   . LEU C 1 59 ? 28.097  -30.214 22.219  1.00 58.58  ? 58  LEU C N   1 
ATOM   1867 C  CA  . LEU C 1 59 ? 27.151  -29.116 22.337  1.00 55.66  ? 58  LEU C CA  1 
ATOM   1868 C  C   . LEU C 1 59 ? 27.771  -27.843 21.773  1.00 63.79  ? 58  LEU C C   1 
ATOM   1869 O  O   . LEU C 1 59 ? 28.945  -27.566 22.017  1.00 66.38  ? 58  LEU C O   1 
ATOM   1870 C  CB  . LEU C 1 59 ? 26.714  -28.950 23.793  1.00 60.61  ? 58  LEU C CB  1 
ATOM   1871 C  CG  . LEU C 1 59 ? 26.091  -30.177 24.478  1.00 60.64  ? 58  LEU C CG  1 
ATOM   1872 C  CD1 . LEU C 1 59 ? 25.742  -29.885 25.933  1.00 57.47  ? 58  LEU C CD1 1 
ATOM   1873 C  CD2 . LEU C 1 59 ? 24.871  -30.751 23.762  1.00 51.04  ? 58  LEU C CD2 1 
ATOM   1874 N  N   . PHE C 1 60 ? 26.976  -27.090 21.002  1.00 60.41  ? 59  PHE C N   1 
ATOM   1875 C  CA  . PHE C 1 60 ? 27.446  -25.858 20.380  1.00 63.99  ? 59  PHE C CA  1 
ATOM   1876 C  C   . PHE C 1 60 ? 26.422  -24.753 20.614  1.00 67.12  ? 59  PHE C C   1 
ATOM   1877 O  O   . PHE C 1 60 ? 25.217  -24.957 20.451  1.00 65.15  ? 59  PHE C O   1 
ATOM   1878 C  CB  . PHE C 1 60 ? 27.757  -26.016 18.890  1.00 59.48  ? 59  PHE C CB  1 
ATOM   1879 C  CG  . PHE C 1 60 ? 28.677  -27.189 18.580  1.00 71.67  ? 59  PHE C CG  1 
ATOM   1880 C  CD1 . PHE C 1 60 ? 28.165  -28.475 18.408  1.00 64.05  ? 59  PHE C CD1 1 
ATOM   1881 C  CD2 . PHE C 1 60 ? 30.057  -27.007 18.473  1.00 78.30  ? 59  PHE C CD2 1 
ATOM   1882 C  CE1 . PHE C 1 60 ? 29.010  -29.539 18.134  1.00 65.15  ? 59  PHE C CE1 1 
ATOM   1883 C  CE2 . PHE C 1 60 ? 30.899  -28.079 18.193  1.00 73.96  ? 59  PHE C CE2 1 
ATOM   1884 C  CZ  . PHE C 1 60 ? 30.374  -29.341 18.024  1.00 66.64  ? 59  PHE C CZ  1 
ATOM   1885 N  N   . PRO C 1 61 ? 26.879  -23.547 21.012  1.00 69.24  ? 60  PRO C N   1 
ATOM   1886 C  CA  . PRO C 1 61 ? 25.963  -22.438 21.265  1.00 67.95  ? 60  PRO C CA  1 
ATOM   1887 C  C   . PRO C 1 61 ? 25.413  -21.952 19.920  1.00 63.81  ? 60  PRO C C   1 
ATOM   1888 O  O   . PRO C 1 61 ? 26.152  -21.804 18.949  1.00 59.52  ? 60  PRO C O   1 
ATOM   1889 C  CB  . PRO C 1 61 ? 26.850  -21.401 22.001  1.00 75.22  ? 60  PRO C CB  1 
ATOM   1890 C  CG  . PRO C 1 61 ? 28.151  -22.138 22.305  1.00 70.15  ? 60  PRO C CG  1 
ATOM   1891 C  CD  . PRO C 1 61 ? 28.294  -23.186 21.212  1.00 73.15  ? 60  PRO C CD  1 
ATOM   1892 N  N   . TYR C 1 62 ? 24.090  -21.765 19.889  1.00 64.88  ? 61  TYR C N   1 
ATOM   1893 C  CA  . TYR C 1 62 ? 23.284  -21.415 18.733  1.00 63.17  ? 61  TYR C CA  1 
ATOM   1894 C  C   . TYR C 1 62 ? 23.875  -20.220 17.994  1.00 80.12  ? 61  TYR C C   1 
ATOM   1895 O  O   . TYR C 1 62 ? 24.290  -20.356 16.842  1.00 81.50  ? 61  TYR C O   1 
ATOM   1896 C  CB  . TYR C 1 62 ? 21.933  -21.061 19.357  1.00 63.48  ? 61  TYR C CB  1 
ATOM   1897 C  CG  . TYR C 1 62 ? 20.809  -20.719 18.395  1.00 65.70  ? 61  TYR C CG  1 
ATOM   1898 C  CD1 . TYR C 1 62 ? 20.741  -21.300 17.134  1.00 70.60  ? 61  TYR C CD1 1 
ATOM   1899 C  CD2 . TYR C 1 62 ? 19.813  -19.819 18.751  1.00 69.36  ? 61  TYR C CD2 1 
ATOM   1900 C  CE1 . TYR C 1 62 ? 19.719  -20.996 16.250  1.00 64.75  ? 61  TYR C CE1 1 
ATOM   1901 C  CE2 . TYR C 1 62 ? 18.785  -19.504 17.876  1.00 72.32  ? 61  TYR C CE2 1 
ATOM   1902 C  CZ  . TYR C 1 62 ? 18.742  -20.093 16.622  1.00 63.39  ? 61  TYR C CZ  1 
ATOM   1903 O  OH  . TYR C 1 62 ? 17.730  -19.820 15.752  1.00 61.06  ? 61  TYR C OH  1 
ATOM   1904 N  N   . ASP C 1 63 ? 23.901  -19.060 18.672  1.00 83.15  ? 62  ASP C N   1 
ATOM   1905 C  CA  . ASP C 1 63 ? 24.383  -17.800 18.117  1.00 73.58  ? 62  ASP C CA  1 
ATOM   1906 C  C   . ASP C 1 63 ? 25.791  -17.953 17.560  1.00 72.06  ? 62  ASP C C   1 
ATOM   1907 O  O   . ASP C 1 63 ? 26.097  -17.358 16.531  1.00 92.84  ? 62  ASP C O   1 
ATOM   1908 C  CB  . ASP C 1 63 ? 24.400  -16.653 19.118  1.00 79.01  ? 62  ASP C CB  1 
ATOM   1909 C  CG  . ASP C 1 63 ? 23.074  -15.958 19.391  1.00 84.77  ? 62  ASP C CG  1 
ATOM   1910 O  OD1 . ASP C 1 63 ? 23.116  -14.842 19.952  1.00 95.30  ? 62  ASP C OD1 1 
ATOM   1911 O  OD2 . ASP C 1 63 ? 22.014  -16.532 19.052  1.00 79.19  ? 62  ASP C OD2 1 
ATOM   1912 N  N   . LYS C 1 64 ? 26.648  -18.734 18.230  1.00 62.38  ? 63  LYS C N   1 
ATOM   1913 C  CA  . LYS C 1 64 ? 28.028  -18.814 17.768  1.00 61.51  ? 63  LYS C CA  1 
ATOM   1914 C  C   . LYS C 1 64 ? 28.173  -19.752 16.571  1.00 60.96  ? 63  LYS C C   1 
ATOM   1915 O  O   . LYS C 1 64 ? 29.264  -19.834 16.010  1.00 70.77  ? 63  LYS C O   1 
ATOM   1916 C  CB  . LYS C 1 64 ? 29.073  -19.127 18.845  1.00 57.16  ? 63  LYS C CB  1 
ATOM   1917 N  N   . SER C 1 65 ? 27.099  -20.453 16.174  1.00 63.74  ? 64  SER C N   1 
ATOM   1918 C  CA  . SER C 1 65 ? 27.228  -21.355 15.034  1.00 63.22  ? 64  SER C CA  1 
ATOM   1919 C  C   . SER C 1 65 ? 25.921  -21.598 14.273  1.00 56.22  ? 64  SER C C   1 
ATOM   1920 O  O   . SER C 1 65 ? 25.834  -22.570 13.536  1.00 53.59  ? 64  SER C O   1 
ATOM   1921 C  CB  . SER C 1 65 ? 27.800  -22.671 15.471  1.00 66.39  ? 64  SER C CB  1 
ATOM   1922 O  OG  . SER C 1 65 ? 26.835  -23.345 16.266  1.00 58.97  ? 64  SER C OG  1 
ATOM   1923 N  N   . LYS C 1 66 ? 24.912  -20.737 14.418  1.00 53.93  ? 65  LYS C N   1 
ATOM   1924 C  CA  . LYS C 1 66 ? 23.675  -20.974 13.682  1.00 64.59  ? 65  LYS C CA  1 
ATOM   1925 C  C   . LYS C 1 66 ? 23.940  -20.806 12.190  1.00 74.55  ? 65  LYS C C   1 
ATOM   1926 O  O   . LYS C 1 66 ? 23.259  -21.430 11.381  1.00 71.88  ? 65  LYS C O   1 
ATOM   1927 C  CB  . LYS C 1 66 ? 22.452  -20.153 14.119  1.00 56.18  ? 65  LYS C CB  1 
ATOM   1928 C  CG  . LYS C 1 66 ? 22.679  -18.655 14.006  1.00 60.10  ? 65  LYS C CG  1 
ATOM   1929 C  CD  . LYS C 1 66 ? 21.500  -17.744 14.318  1.00 75.95  ? 65  LYS C CD  1 
ATOM   1930 C  CE  . LYS C 1 66 ? 21.938  -16.328 14.071  1.00 81.35  ? 65  LYS C CE  1 
ATOM   1931 N  NZ  . LYS C 1 66 ? 20.919  -15.362 14.472  1.00 80.94  ? 65  LYS C NZ  1 
ATOM   1932 N  N   . ASP C 1 67 ? 24.930  -19.963 11.848  1.00 79.82  ? 66  ASP C N   1 
ATOM   1933 C  CA  . ASP C 1 67 ? 25.303  -19.717 10.462  1.00 72.79  ? 66  ASP C CA  1 
ATOM   1934 C  C   . ASP C 1 67 ? 25.754  -21.019 9.794   1.00 77.53  ? 66  ASP C C   1 
ATOM   1935 O  O   . ASP C 1 67 ? 25.556  -21.195 8.587   1.00 68.75  ? 66  ASP C O   1 
ATOM   1936 C  CB  . ASP C 1 67 ? 26.254  -18.535 10.303  1.00 76.00  ? 66  ASP C CB  1 
ATOM   1937 C  CG  . ASP C 1 67 ? 27.665  -18.657 10.871  1.00 75.32  ? 66  ASP C CG  1 
ATOM   1938 O  OD1 . ASP C 1 67 ? 28.312  -19.706 10.652  1.00 72.79  ? 66  ASP C OD1 1 
ATOM   1939 O  OD2 . ASP C 1 67 ? 28.141  -17.660 11.461  1.00 67.95  ? 66  ASP C OD2 1 
ATOM   1940 N  N   . LYS C 1 68 ? 26.328  -21.929 10.597  1.00 74.40  ? 67  LYS C N   1 
ATOM   1941 C  CA  . LYS C 1 68 ? 26.852  -23.205 10.120  1.00 77.40  ? 67  LYS C CA  1 
ATOM   1942 C  C   . LYS C 1 68 ? 25.777  -24.302 10.108  1.00 62.56  ? 67  LYS C C   1 
ATOM   1943 O  O   . LYS C 1 68 ? 25.690  -25.074 9.155   1.00 62.20  ? 67  LYS C O   1 
ATOM   1944 C  CB  . LYS C 1 68 ? 28.090  -23.559 10.957  1.00 72.17  ? 67  LYS C CB  1 
ATOM   1945 C  CG  . LYS C 1 68 ? 28.963  -24.696 10.457  1.00 78.88  ? 67  LYS C CG  1 
ATOM   1946 C  CD  . LYS C 1 68 ? 30.344  -24.680 11.108  1.00 89.31  ? 67  LYS C CD  1 
ATOM   1947 C  CE  . LYS C 1 68 ? 31.108  -25.978 11.076  1.00 91.90  ? 67  LYS C CE  1 
ATOM   1948 N  NZ  . LYS C 1 68 ? 31.498  -26.420 9.734   1.00 94.54  ? 67  LYS C NZ  1 
ATOM   1949 N  N   . TYR C 1 69 ? 24.958  -24.379 11.163  1.00 56.08  ? 68  TYR C N   1 
ATOM   1950 C  CA  . TYR C 1 69 ? 24.122  -25.559 11.364  1.00 56.77  ? 68  TYR C CA  1 
ATOM   1951 C  C   . TYR C 1 69 ? 22.636  -25.222 11.247  1.00 55.45  ? 68  TYR C C   1 
ATOM   1952 O  O   . TYR C 1 69 ? 21.814  -26.136 11.183  1.00 48.65  ? 68  TYR C O   1 
ATOM   1953 C  CB  . TYR C 1 69 ? 24.349  -26.140 12.764  1.00 56.03  ? 68  TYR C CB  1 
ATOM   1954 C  CG  . TYR C 1 69 ? 25.753  -26.658 13.052  1.00 60.18  ? 68  TYR C CG  1 
ATOM   1955 C  CD1 . TYR C 1 69 ? 26.511  -27.291 12.070  1.00 65.79  ? 68  TYR C CD1 1 
ATOM   1956 C  CD2 . TYR C 1 69 ? 26.309  -26.522 14.316  1.00 69.15  ? 68  TYR C CD2 1 
ATOM   1957 C  CE1 . TYR C 1 69 ? 27.782  -27.772 12.342  1.00 68.14  ? 68  TYR C CE1 1 
ATOM   1958 C  CE2 . TYR C 1 69 ? 27.584  -26.986 14.595  1.00 69.31  ? 68  TYR C CE2 1 
ATOM   1959 C  CZ  . TYR C 1 69 ? 28.323  -27.604 13.604  1.00 61.20  ? 68  TYR C CZ  1 
ATOM   1960 O  OH  . TYR C 1 69 ? 29.567  -28.060 13.903  1.00 71.18  ? 68  TYR C OH  1 
ATOM   1961 N  N   . GLY C 1 70 ? 22.295  -23.923 11.298  1.00 53.89  ? 69  GLY C N   1 
ATOM   1962 C  CA  . GLY C 1 70 ? 20.924  -23.464 11.104  1.00 56.12  ? 69  GLY C CA  1 
ATOM   1963 C  C   . GLY C 1 70 ? 20.550  -23.421 9.623   1.00 53.94  ? 69  GLY C C   1 
ATOM   1964 O  O   . GLY C 1 70 ? 20.172  -22.373 9.103   1.00 61.35  ? 69  GLY C O   1 
ATOM   1965 N  N   . LYS C 1 71 ? 20.685  -24.567 8.947   1.00 56.33  ? 70  LYS C N   1 
ATOM   1966 C  CA  . LYS C 1 71 ? 20.257  -24.757 7.566   1.00 65.83  ? 70  LYS C CA  1 
ATOM   1967 C  C   . LYS C 1 71 ? 19.215  -25.873 7.519   1.00 63.51  ? 70  LYS C C   1 
ATOM   1968 O  O   . LYS C 1 71 ? 19.276  -26.825 8.292   1.00 58.11  ? 70  LYS C O   1 
ATOM   1969 C  CB  . LYS C 1 71 ? 21.414  -25.045 6.594   1.00 64.66  ? 70  LYS C CB  1 
ATOM   1970 C  CG  . LYS C 1 71 ? 22.475  -26.054 7.027   1.00 68.55  ? 70  LYS C CG  1 
ATOM   1971 C  CD  . LYS C 1 71 ? 23.329  -26.622 5.898   1.00 72.91  ? 70  LYS C CD  1 
ATOM   1972 C  CE  . LYS C 1 71 ? 24.272  -27.686 6.367   1.00 77.65  ? 70  LYS C CE  1 
ATOM   1973 N  N   . PRO C 1 72 ? 18.203  -25.819 6.629   1.00 56.19  ? 71  PRO C N   1 
ATOM   1974 C  CA  . PRO C 1 72 ? 17.212  -26.897 6.621   1.00 50.64  ? 71  PRO C CA  1 
ATOM   1975 C  C   . PRO C 1 72 ? 17.881  -28.195 6.165   1.00 54.42  ? 71  PRO C C   1 
ATOM   1976 O  O   . PRO C 1 72 ? 19.012  -28.202 5.688   1.00 56.75  ? 71  PRO C O   1 
ATOM   1977 C  CB  . PRO C 1 72 ? 16.074  -26.433 5.713   1.00 43.45  ? 71  PRO C CB  1 
ATOM   1978 C  CG  . PRO C 1 72 ? 16.522  -25.071 5.175   1.00 45.08  ? 71  PRO C CG  1 
ATOM   1979 C  CD  . PRO C 1 72 ? 17.945  -24.753 5.648   1.00 42.81  ? 71  PRO C CD  1 
ATOM   1980 N  N   . ASN C 1 73 ? 17.207  -29.306 6.438   1.00 54.51  ? 72  ASN C N   1 
ATOM   1981 C  CA  . ASN C 1 73 ? 17.558  -30.610 5.912   1.00 52.55  ? 72  ASN C CA  1 
ATOM   1982 C  C   . ASN C 1 73 ? 16.327  -31.492 6.100   1.00 45.97  ? 72  ASN C C   1 
ATOM   1983 O  O   . ASN C 1 73 ? 15.299  -31.014 6.578   1.00 53.20  ? 72  ASN C O   1 
ATOM   1984 C  CB  . ASN C 1 73 ? 18.964  -31.086 6.302   1.00 52.93  ? 72  ASN C CB  1 
ATOM   1985 C  CG  . ASN C 1 73 ? 19.075  -31.595 7.724   1.00 52.47  ? 72  ASN C CG  1 
ATOM   1986 O  OD1 . ASN C 1 73 ? 18.063  -31.883 8.366   1.00 49.45  ? 72  ASN C OD1 1 
ATOM   1987 N  ND2 . ASN C 1 73 ? 20.294  -31.723 8.230   1.00 48.85  ? 72  ASN C ND2 1 
ATOM   1988 N  N   . LYS C 1 74 ? 16.441  -32.761 5.700   1.00 53.86  ? 73  LYS C N   1 
ATOM   1989 C  CA  . LYS C 1 74 ? 15.287  -33.567 5.340   1.00 58.68  ? 73  LYS C CA  1 
ATOM   1990 C  C   . LYS C 1 74 ? 14.801  -34.410 6.518   1.00 53.80  ? 73  LYS C C   1 
ATOM   1991 O  O   . LYS C 1 74 ? 13.639  -34.814 6.551   1.00 59.63  ? 73  LYS C O   1 
ATOM   1992 C  CB  . LYS C 1 74 ? 15.739  -34.383 4.125   1.00 59.59  ? 73  LYS C CB  1 
ATOM   1993 N  N   . ARG C 1 75 ? 15.697  -34.648 7.488   1.00 56.37  ? 74  ARG C N   1 
ATOM   1994 C  CA  . ARG C 1 75 ? 15.484  -35.550 8.615   1.00 41.94  ? 74  ARG C CA  1 
ATOM   1995 C  C   . ARG C 1 75 ? 14.239  -35.130 9.395   1.00 46.73  ? 74  ARG C C   1 
ATOM   1996 O  O   . ARG C 1 75 ? 13.956  -33.936 9.562   1.00 51.11  ? 74  ARG C O   1 
ATOM   1997 C  CB  . ARG C 1 75 ? 16.729  -35.492 9.506   1.00 41.96  ? 74  ARG C CB  1 
ATOM   1998 C  CG  . ARG C 1 75 ? 18.081  -35.605 8.804   1.00 39.29  ? 74  ARG C CG  1 
ATOM   1999 C  CD  . ARG C 1 75 ? 18.547  -37.000 8.433   1.00 41.12  ? 74  ARG C CD  1 
ATOM   2000 N  NE  . ARG C 1 75 ? 18.473  -37.966 9.537   1.00 35.70  ? 74  ARG C NE  1 
ATOM   2001 C  CZ  . ARG C 1 75 ? 19.559  -38.448 10.124  1.00 39.74  ? 74  ARG C CZ  1 
ATOM   2002 N  NH1 . ARG C 1 75 ? 19.427  -39.111 11.252  1.00 41.65  ? 74  ARG C NH1 1 
ATOM   2003 N  NH2 . ARG C 1 75 ? 20.765  -38.154 9.609   1.00 27.34  ? 74  ARG C NH2 1 
ATOM   2004 N  N   . LYS C 1 76 ? 13.517  -36.129 9.908   1.00 53.42  ? 75  LYS C N   1 
ATOM   2005 C  CA  . LYS C 1 76 ? 12.170  -35.920 10.420  1.00 56.28  ? 75  LYS C CA  1 
ATOM   2006 C  C   . LYS C 1 76 ? 12.208  -34.941 11.592  1.00 59.44  ? 75  LYS C C   1 
ATOM   2007 O  O   . LYS C 1 76 ? 12.851  -35.209 12.610  1.00 50.15  ? 75  LYS C O   1 
ATOM   2008 C  CB  . LYS C 1 76 ? 11.429  -37.223 10.772  1.00 57.09  ? 75  LYS C CB  1 
ATOM   2009 C  CG  . LYS C 1 76 ? 9.889   -37.124 10.763  1.00 51.80  ? 75  LYS C CG  1 
ATOM   2010 C  CD  . LYS C 1 76 ? 9.183   -37.596 12.030  1.00 56.00  ? 75  LYS C CD  1 
ATOM   2011 N  N   . GLY C 1 77 ? 11.519  -33.805 11.399  1.00 60.14  ? 76  GLY C N   1 
ATOM   2012 C  CA  . GLY C 1 77 ? 11.216  -32.840 12.446  1.00 52.10  ? 76  GLY C CA  1 
ATOM   2013 C  C   . GLY C 1 77 ? 12.324  -31.802 12.627  1.00 47.17  ? 76  GLY C C   1 
ATOM   2014 O  O   . GLY C 1 77 ? 12.296  -31.027 13.577  1.00 47.01  ? 76  GLY C O   1 
ATOM   2015 N  N   . PHE C 1 78 ? 13.308  -31.792 11.722  1.00 46.01  ? 77  PHE C N   1 
ATOM   2016 C  CA  . PHE C 1 78 ? 14.424  -30.871 11.850  1.00 47.46  ? 77  PHE C CA  1 
ATOM   2017 C  C   . PHE C 1 78 ? 13.955  -29.459 11.513  1.00 53.87  ? 77  PHE C C   1 
ATOM   2018 O  O   . PHE C 1 78 ? 14.255  -28.521 12.264  1.00 53.45  ? 77  PHE C O   1 
ATOM   2019 C  CB  . PHE C 1 78 ? 15.642  -31.339 11.060  1.00 40.67  ? 77  PHE C CB  1 
ATOM   2020 C  CG  . PHE C 1 78 ? 16.941  -30.549 11.189  1.00 38.20  ? 77  PHE C CG  1 
ATOM   2021 C  CD1 . PHE C 1 78 ? 17.047  -29.256 10.694  1.00 42.03  ? 77  PHE C CD1 1 
ATOM   2022 C  CD2 . PHE C 1 78 ? 18.086  -31.153 11.704  1.00 39.72  ? 77  PHE C CD2 1 
ATOM   2023 C  CE1 . PHE C 1 78 ? 18.254  -28.563 10.746  1.00 48.23  ? 77  PHE C CE1 1 
ATOM   2024 C  CE2 . PHE C 1 78 ? 19.302  -30.467 11.743  1.00 48.04  ? 77  PHE C CE2 1 
ATOM   2025 C  CZ  . PHE C 1 78 ? 19.389  -29.173 11.252  1.00 46.75  ? 77  PHE C CZ  1 
ATOM   2026 N  N   . ASN C 1 79 ? 13.159  -29.341 10.436  1.00 48.56  ? 78  ASN C N   1 
ATOM   2027 C  CA  . ASN C 1 79 ? 12.737  -28.028 9.961   1.00 50.80  ? 78  ASN C CA  1 
ATOM   2028 C  C   . ASN C 1 79 ? 11.850  -27.369 11.015  1.00 50.05  ? 78  ASN C C   1 
ATOM   2029 O  O   . ASN C 1 79 ? 12.010  -26.178 11.295  1.00 44.95  ? 78  ASN C O   1 
ATOM   2030 C  CB  . ASN C 1 79 ? 12.278  -28.042 8.502   1.00 44.91  ? 78  ASN C CB  1 
ATOM   2031 C  CG  . ASN C 1 79 ? 13.449  -28.311 7.588   1.00 50.95  ? 78  ASN C CG  1 
ATOM   2032 O  OD1 . ASN C 1 79 ? 14.592  -28.036 7.975   1.00 48.65  ? 78  ASN C OD1 1 
ATOM   2033 N  ND2 . ASN C 1 79 ? 13.206  -28.861 6.404   1.00 48.09  ? 78  ASN C ND2 1 
ATOM   2034 N  N   . GLU C 1 80 ? 10.977  -28.174 11.636  1.00 46.37  ? 79  GLU C N   1 
ATOM   2035 C  CA  . GLU C 1 80 ? 10.102  -27.701 12.697  1.00 48.41  ? 79  GLU C CA  1 
ATOM   2036 C  C   . GLU C 1 80 ? 10.989  -27.285 13.861  1.00 49.69  ? 79  GLU C C   1 
ATOM   2037 O  O   . GLU C 1 80 ? 10.749  -26.263 14.496  1.00 55.46  ? 79  GLU C O   1 
ATOM   2038 C  CB  . GLU C 1 80 ? 9.137   -28.796 13.148  1.00 48.27  ? 79  GLU C CB  1 
ATOM   2039 C  CG  . GLU C 1 80 ? 8.172   -28.316 14.220  1.00 44.70  ? 79  GLU C CG  1 
ATOM   2040 C  CD  . GLU C 1 80 ? 6.834   -29.028 14.120  1.00 50.78  ? 79  GLU C CD  1 
ATOM   2041 O  OE1 . GLU C 1 80 ? 6.812   -30.077 13.453  1.00 61.89  ? 79  GLU C OE1 1 
ATOM   2042 O  OE2 . GLU C 1 80 ? 5.809   -28.531 14.639  1.00 44.97  ? 79  GLU C OE2 1 
ATOM   2043 N  N   . GLY C 1 81 ? 12.064  -28.054 14.066  1.00 50.23  ? 80  GLY C N   1 
ATOM   2044 C  CA  . GLY C 1 81 ? 13.064  -27.717 15.070  1.00 49.60  ? 80  GLY C CA  1 
ATOM   2045 C  C   . GLY C 1 81 ? 13.651  -26.323 14.857  1.00 44.32  ? 80  GLY C C   1 
ATOM   2046 O  O   . GLY C 1 81 ? 13.813  -25.576 15.813  1.00 48.01  ? 80  GLY C O   1 
ATOM   2047 N  N   . LEU C 1 82 ? 13.988  -25.994 13.603  1.00 44.83  ? 81  LEU C N   1 
ATOM   2048 C  CA  . LEU C 1 82 ? 14.600  -24.718 13.218  1.00 48.07  ? 81  LEU C CA  1 
ATOM   2049 C  C   . LEU C 1 82 ? 13.659  -23.542 13.514  1.00 47.19  ? 81  LEU C C   1 
ATOM   2050 O  O   . LEU C 1 82 ? 14.098  -22.512 14.009  1.00 51.32  ? 81  LEU C O   1 
ATOM   2051 C  CB  . LEU C 1 82 ? 14.996  -24.768 11.743  1.00 43.17  ? 81  LEU C CB  1 
ATOM   2052 C  CG  . LEU C 1 82 ? 16.309  -25.466 11.353  1.00 35.84  ? 81  LEU C CG  1 
ATOM   2053 C  CD1 . LEU C 1 82 ? 16.414  -25.421 9.837   1.00 38.21  ? 81  LEU C CD1 1 
ATOM   2054 C  CD2 . LEU C 1 82 ? 17.558  -24.822 11.958  1.00 36.30  ? 81  LEU C CD2 1 
ATOM   2055 N  N   . TRP C 1 83 ? 12.356  -23.714 13.251  1.00 42.49  ? 82  TRP C N   1 
ATOM   2056 C  CA  . TRP C 1 83 ? 11.372  -22.670 13.488  1.00 49.34  ? 82  TRP C CA  1 
ATOM   2057 C  C   . TRP C 1 83 ? 11.229  -22.383 14.987  1.00 52.62  ? 82  TRP C C   1 
ATOM   2058 O  O   . TRP C 1 83 ? 11.198  -21.222 15.410  1.00 49.73  ? 82  TRP C O   1 
ATOM   2059 C  CB  . TRP C 1 83 ? 10.016  -23.085 12.901  1.00 54.66  ? 82  TRP C CB  1 
ATOM   2060 C  CG  . TRP C 1 83 ? 8.999   -21.986 13.012  1.00 53.67  ? 82  TRP C CG  1 
ATOM   2061 C  CD1 . TRP C 1 83 ? 8.780   -21.005 12.089  1.00 57.35  ? 82  TRP C CD1 1 
ATOM   2062 C  CD2 . TRP C 1 83 ? 8.114   -21.706 14.120  1.00 59.93  ? 82  TRP C CD2 1 
ATOM   2063 N  NE1 . TRP C 1 83 ? 7.786   -20.165 12.516  1.00 53.56  ? 82  TRP C NE1 1 
ATOM   2064 C  CE2 . TRP C 1 83 ? 7.366   -20.553 13.762  1.00 59.87  ? 82  TRP C CE2 1 
ATOM   2065 C  CE3 . TRP C 1 83 ? 7.877   -22.306 15.368  1.00 52.82  ? 82  TRP C CE3 1 
ATOM   2066 C  CZ2 . TRP C 1 83 ? 6.402   -19.993 14.604  1.00 55.68  ? 82  TRP C CZ2 1 
ATOM   2067 C  CZ3 . TRP C 1 83 ? 6.937   -21.742 16.205  1.00 59.51  ? 82  TRP C CZ3 1 
ATOM   2068 C  CH2 . TRP C 1 83 ? 6.214   -20.602 15.828  1.00 66.93  ? 82  TRP C CH2 1 
ATOM   2069 N  N   . GLU C 1 84 ? 11.107  -23.462 15.776  1.00 45.43  ? 83  GLU C N   1 
ATOM   2070 C  CA  . GLU C 1 84 ? 11.055  -23.414 17.228  1.00 41.77  ? 83  GLU C CA  1 
ATOM   2071 C  C   . GLU C 1 84 ? 12.263  -22.659 17.805  1.00 44.52  ? 83  GLU C C   1 
ATOM   2072 O  O   . GLU C 1 84 ? 12.096  -21.682 18.543  1.00 41.63  ? 83  GLU C O   1 
ATOM   2073 C  CB  . GLU C 1 84 ? 10.871  -24.805 17.837  1.00 47.14  ? 83  GLU C CB  1 
ATOM   2074 C  CG  . GLU C 1 84 ? 9.466   -25.384 17.687  1.00 53.34  ? 83  GLU C CG  1 
ATOM   2075 C  CD  . GLU C 1 84 ? 9.400   -26.881 17.992  1.00 53.89  ? 83  GLU C CD  1 
ATOM   2076 O  OE1 . GLU C 1 84 ? 10.436  -27.520 18.322  1.00 48.78  ? 83  GLU C OE1 1 
ATOM   2077 O  OE2 . GLU C 1 84 ? 8.285   -27.426 17.899  1.00 49.74  ? 83  GLU C OE2 1 
ATOM   2078 N  N   . ILE C 1 85 ? 13.491  -23.081 17.483  1.00 36.16  ? 84  ILE C N   1 
ATOM   2079 C  CA  . ILE C 1 85 ? 14.627  -22.427 18.130  1.00 37.86  ? 84  ILE C CA  1 
ATOM   2080 C  C   . ILE C 1 85 ? 14.642  -20.917 17.886  1.00 46.29  ? 84  ILE C C   1 
ATOM   2081 O  O   . ILE C 1 85 ? 15.170  -20.197 18.716  1.00 56.58  ? 84  ILE C O   1 
ATOM   2082 C  CB  . ILE C 1 85 ? 15.961  -23.078 17.722  1.00 34.16  ? 84  ILE C CB  1 
ATOM   2083 C  CG1 . ILE C 1 85 ? 17.096  -22.687 18.632  1.00 44.89  ? 84  ILE C CG1 1 
ATOM   2084 C  CG2 . ILE C 1 85 ? 16.327  -22.782 16.279  1.00 37.62  ? 84  ILE C CG2 1 
ATOM   2085 C  CD1 . ILE C 1 85 ? 18.334  -23.566 18.474  1.00 48.64  ? 84  ILE C CD1 1 
ATOM   2086 N  N   . GLN C 1 86 ? 14.120  -20.435 16.741  1.00 58.75  ? 85  GLN C N   1 
ATOM   2087 C  CA  . GLN C 1 86 ? 14.280  -19.040 16.335  1.00 51.24  ? 85  GLN C CA  1 
ATOM   2088 C  C   . GLN C 1 86 ? 13.133  -18.170 16.845  1.00 49.26  ? 85  GLN C C   1 
ATOM   2089 O  O   . GLN C 1 86 ? 13.354  -16.997 17.115  1.00 63.82  ? 85  GLN C O   1 
ATOM   2090 C  CB  . GLN C 1 86 ? 14.371  -18.929 14.809  1.00 58.79  ? 85  GLN C CB  1 
ATOM   2091 C  CG  . GLN C 1 86 ? 14.724  -17.545 14.271  1.00 52.39  ? 85  GLN C CG  1 
ATOM   2092 C  CD  . GLN C 1 86 ? 15.008  -17.543 12.781  1.00 69.14  ? 85  GLN C CD  1 
ATOM   2093 O  OE1 . GLN C 1 86 ? 14.707  -18.505 12.062  1.00 69.83  ? 85  GLN C OE1 1 
ATOM   2094 N  NE2 . GLN C 1 86 ? 15.591  -16.454 12.292  1.00 63.73  ? 85  GLN C NE2 1 
ATOM   2095 N  N   . ASN C 1 87 ? 11.928  -18.736 16.990  1.00 50.60  ? 86  ASN C N   1 
ATOM   2096 C  CA  . ASN C 1 87 ? 10.724  -17.963 17.294  1.00 59.09  ? 86  ASN C CA  1 
ATOM   2097 C  C   . ASN C 1 87 ? 10.097  -18.292 18.660  1.00 65.90  ? 86  ASN C C   1 
ATOM   2098 O  O   . ASN C 1 87 ? 9.492   -17.423 19.295  1.00 67.17  ? 86  ASN C O   1 
ATOM   2099 C  CB  . ASN C 1 87 ? 9.639   -18.172 16.239  1.00 63.13  ? 86  ASN C CB  1 
ATOM   2100 C  CG  . ASN C 1 87 ? 10.055  -17.711 14.860  1.00 67.83  ? 86  ASN C CG  1 
ATOM   2101 O  OD1 . ASN C 1 87 ? 10.024  -16.511 14.565  1.00 78.33  ? 86  ASN C OD1 1 
ATOM   2102 N  ND2 . ASN C 1 87 ? 10.435  -18.645 14.005  1.00 45.73  ? 86  ASN C ND2 1 
ATOM   2103 N  N   . ASN C 1 88 ? 10.179  -19.557 19.098  1.00 65.82  ? 87  ASN C N   1 
ATOM   2104 C  CA  . ASN C 1 88 ? 9.421   -20.015 20.256  1.00 66.06  ? 87  ASN C CA  1 
ATOM   2105 C  C   . ASN C 1 88 ? 10.304  -20.923 21.108  1.00 60.81  ? 87  ASN C C   1 
ATOM   2106 O  O   . ASN C 1 88 ? 9.868   -22.025 21.440  1.00 63.08  ? 87  ASN C O   1 
ATOM   2107 C  CB  . ASN C 1 88 ? 8.170   -20.785 19.829  1.00 66.92  ? 87  ASN C CB  1 
ATOM   2108 C  CG  . ASN C 1 88 ? 7.130   -20.927 20.922  1.00 77.32  ? 87  ASN C CG  1 
ATOM   2109 O  OD1 . ASN C 1 88 ? 7.141   -20.191 21.917  1.00 82.04  ? 87  ASN C OD1 1 
ATOM   2110 N  ND2 . ASN C 1 88 ? 6.192   -21.844 20.741  1.00 70.11  ? 87  ASN C ND2 1 
ATOM   2111 N  N   . PRO C 1 89 ? 11.552  -20.511 21.462  1.00 53.38  ? 88  PRO C N   1 
ATOM   2112 C  CA  . PRO C 1 89 ? 12.521  -21.404 22.117  1.00 60.07  ? 88  PRO C CA  1 
ATOM   2113 C  C   . PRO C 1 89 ? 12.474  -21.728 23.618  1.00 65.03  ? 88  PRO C C   1 
ATOM   2114 O  O   . PRO C 1 89 ? 13.429  -22.314 24.133  1.00 70.06  ? 88  PRO C O   1 
ATOM   2115 C  CB  . PRO C 1 89 ? 13.878  -20.756 21.734  1.00 52.80  ? 88  PRO C CB  1 
ATOM   2116 C  CG  . PRO C 1 89 ? 13.564  -19.273 21.713  1.00 61.49  ? 88  PRO C CG  1 
ATOM   2117 C  CD  . PRO C 1 89 ? 12.119  -19.171 21.218  1.00 55.86  ? 88  PRO C CD  1 
ATOM   2118 N  N   . HIS C 1 90 ? 11.379  -21.363 24.308  1.00 64.16  ? 89  HIS C N   1 
ATOM   2119 C  CA  . HIS C 1 90 ? 11.249  -21.565 25.749  1.00 59.30  ? 89  HIS C CA  1 
ATOM   2120 C  C   . HIS C 1 90 ? 9.807   -21.909 26.130  1.00 66.75  ? 89  HIS C C   1 
ATOM   2121 O  O   . HIS C 1 90 ? 9.470   -21.901 27.314  1.00 71.95  ? 89  HIS C O   1 
ATOM   2122 C  CB  . HIS C 1 90 ? 11.781  -20.371 26.554  1.00 44.45  ? 89  HIS C CB  1 
ATOM   2123 C  CG  . HIS C 1 90 ? 13.240  -20.092 26.361  1.00 43.10  ? 89  HIS C CG  1 
ATOM   2124 N  ND1 . HIS C 1 90 ? 13.717  -18.980 25.692  1.00 48.85  ? 89  HIS C ND1 1 
ATOM   2125 C  CD2 . HIS C 1 90 ? 14.325  -20.771 26.754  1.00 46.23  ? 89  HIS C CD2 1 
ATOM   2126 C  CE1 . HIS C 1 90 ? 15.051  -19.008 25.660  1.00 46.53  ? 89  HIS C CE1 1 
ATOM   2127 N  NE2 . HIS C 1 90 ? 15.439  -20.095 26.302  1.00 47.09  ? 89  HIS C NE2 1 
ATOM   2128 N  N   . ALA C 1 91 ? 8.962   -22.235 25.138  1.00 67.74  ? 90  ALA C N   1 
ATOM   2129 C  CA  . ALA C 1 91 ? 7.641   -22.788 25.416  1.00 65.33  ? 90  ALA C CA  1 
ATOM   2130 C  C   . ALA C 1 91 ? 7.786   -24.179 26.038  1.00 68.44  ? 90  ALA C C   1 
ATOM   2131 O  O   . ALA C 1 91 ? 8.889   -24.721 26.128  1.00 60.85  ? 90  ALA C O   1 
ATOM   2132 C  CB  . ALA C 1 91 ? 6.797   -22.819 24.154  1.00 62.11  ? 90  ALA C CB  1 
ATOM   2133 N  N   . SER C 1 92 ? 6.665   -24.757 26.478  1.00 75.21  ? 91  SER C N   1 
ATOM   2134 C  CA  . SER C 1 92 ? 6.715   -26.060 27.122  1.00 82.76  ? 91  SER C CA  1 
ATOM   2135 C  C   . SER C 1 92 ? 6.918   -27.156 26.075  1.00 80.25  ? 91  SER C C   1 
ATOM   2136 O  O   . SER C 1 92 ? 8.053   -27.576 25.859  1.00 74.45  ? 91  SER C O   1 
ATOM   2137 C  CB  . SER C 1 92 ? 5.525   -26.307 28.035  1.00 85.59  ? 91  SER C CB  1 
ATOM   2138 O  OG  . SER C 1 92 ? 4.292   -26.025 27.386  1.00 81.69  ? 91  SER C OG  1 
ATOM   2139 N  N   . TYR C 1 93 ? 5.822   -27.562 25.410  1.00 78.03  ? 92  TYR C N   1 
ATOM   2140 C  CA  . TYR C 1 93 ? 5.770   -28.650 24.437  1.00 78.74  ? 92  TYR C CA  1 
ATOM   2141 C  C   . TYR C 1 93 ? 5.446   -29.970 25.163  1.00 76.16  ? 92  TYR C C   1 
ATOM   2142 O  O   . TYR C 1 93 ? 4.249   -30.252 25.421  1.00 74.18  ? 92  TYR C O   1 
ATOM   2143 C  CB  . TYR C 1 93 ? 7.009   -28.817 23.545  1.00 79.81  ? 92  TYR C CB  1 
ATOM   2144 C  CG  . TYR C 1 93 ? 7.485   -27.564 22.815  1.00 79.60  ? 92  TYR C CG  1 
ATOM   2145 C  CD1 . TYR C 1 93 ? 6.812   -27.075 21.696  1.00 78.63  ? 92  TYR C CD1 1 
ATOM   2146 C  CD2 . TYR C 1 93 ? 8.629   -26.890 23.229  1.00 72.40  ? 92  TYR C CD2 1 
ATOM   2147 C  CE1 . TYR C 1 93 ? 7.248   -25.941 21.028  1.00 75.94  ? 92  TYR C CE1 1 
ATOM   2148 C  CE2 . TYR C 1 93 ? 9.076   -25.759 22.568  1.00 72.83  ? 92  TYR C CE2 1 
ATOM   2149 C  CZ  . TYR C 1 93 ? 8.383   -25.279 21.470  1.00 69.95  ? 92  TYR C CZ  1 
ATOM   2150 O  OH  . TYR C 1 93 ? 8.833   -24.155 20.840  1.00 59.07  ? 92  TYR C OH  1 
HETATM 2151 S  S   . SO4 D 2 .  ? 0.722   -33.296 1.193   1.00 169.77 ? 101 SO4 A S   1 
HETATM 2152 O  O1  . SO4 D 2 .  ? 0.880   -33.211 -0.234  1.00 178.61 ? 101 SO4 A O1  1 
HETATM 2153 O  O2  . SO4 D 2 .  ? 1.501   -32.264 1.824   1.00 153.07 ? 101 SO4 A O2  1 
HETATM 2154 O  O3  . SO4 D 2 .  ? -0.665  -33.123 1.527   1.00 162.71 ? 101 SO4 A O3  1 
HETATM 2155 O  O4  . SO4 D 2 .  ? 1.170   -34.587 1.648   1.00 168.28 ? 101 SO4 A O4  1 
HETATM 2156 S  S   . SO4 E 2 .  ? -8.796  -24.816 1.179   1.00 115.82 ? 102 SO4 A S   1 
HETATM 2157 O  O1  . SO4 E 2 .  ? -9.254  -24.549 -0.167  1.00 95.12  ? 102 SO4 A O1  1 
HETATM 2158 O  O2  . SO4 E 2 .  ? -9.402  -23.871 2.086   1.00 99.96  ? 102 SO4 A O2  1 
HETATM 2159 O  O3  . SO4 E 2 .  ? -9.166  -26.153 1.565   1.00 111.28 ? 102 SO4 A O3  1 
HETATM 2160 O  O4  . SO4 E 2 .  ? -7.361  -24.694 1.237   1.00 108.36 ? 102 SO4 A O4  1 
HETATM 2161 C  C1  . EDO F 3 .  ? 14.498  -19.540 -7.350  1.00 59.58  ? 103 EDO A C1  1 
HETATM 2162 O  O1  . EDO F 3 .  ? 15.648  -18.726 -7.346  1.00 51.45  ? 103 EDO A O1  1 
HETATM 2163 C  C2  . EDO F 3 .  ? 13.607  -19.199 -8.489  1.00 66.06  ? 103 EDO A C2  1 
HETATM 2164 O  O2  . EDO F 3 .  ? 12.987  -17.932 -8.362  1.00 59.32  ? 103 EDO A O2  1 
HETATM 2165 S  S   . SO4 G 2 .  ? 9.506   -29.443 5.629   1.00 89.85  ? 104 SO4 A S   1 
HETATM 2166 O  O1  . SO4 G 2 .  ? 10.529  -28.918 4.770   1.00 81.00  ? 104 SO4 A O1  1 
HETATM 2167 O  O2  . SO4 G 2 .  ? 9.008   -30.678 5.082   1.00 94.44  ? 104 SO4 A O2  1 
HETATM 2168 O  O3  . SO4 G 2 .  ? 10.058  -29.692 6.934   1.00 97.12  ? 104 SO4 A O3  1 
HETATM 2169 O  O4  . SO4 G 2 .  ? 8.427   -28.499 5.732   1.00 80.87  ? 104 SO4 A O4  1 
HETATM 2170 S  S   . SO4 H 2 .  ? 7.421   -8.384  -25.211 1.00 98.66  ? 101 SO4 B S   1 
HETATM 2171 O  O1  . SO4 H 2 .  ? 8.677   -8.519  -25.905 1.00 81.89  ? 101 SO4 B O1  1 
HETATM 2172 O  O2  . SO4 H 2 .  ? 6.408   -9.150  -25.893 1.00 83.31  ? 101 SO4 B O2  1 
HETATM 2173 O  O3  . SO4 H 2 .  ? 7.531   -8.870  -23.849 1.00 65.05  ? 101 SO4 B O3  1 
HETATM 2174 O  O4  . SO4 H 2 .  ? 7.057   -6.988  -25.212 1.00 92.18  ? 101 SO4 B O4  1 
HETATM 2175 S  S   . SO4 I 2 .  ? 14.294  -26.839 -27.065 1.00 81.74  ? 102 SO4 B S   1 
HETATM 2176 O  O1  . SO4 I 2 .  ? 14.327  -25.650 -26.264 1.00 84.84  ? 102 SO4 B O1  1 
HETATM 2177 O  O2  . SO4 I 2 .  ? 15.639  -27.361 -27.190 1.00 82.29  ? 102 SO4 B O2  1 
HETATM 2178 O  O3  . SO4 I 2 .  ? 13.439  -27.829 -26.446 1.00 82.44  ? 102 SO4 B O3  1 
HETATM 2179 O  O4  . SO4 I 2 .  ? 13.772  -26.511 -28.365 1.00 79.46  ? 102 SO4 B O4  1 
HETATM 2180 N  N1  . WJ4 J 4 .  ? 17.563  -14.338 -24.012 0.90 72.70  ? 103 WJ4 B N1  1 
HETATM 2181 C  C4  . WJ4 J 4 .  ? 21.390  -16.034 -21.794 0.90 56.83  ? 103 WJ4 B C4  1 
HETATM 2182 C  C5  . WJ4 J 4 .  ? 21.761  -14.957 -23.835 0.90 55.69  ? 103 WJ4 B C5  1 
HETATM 2183 C  C6  . WJ4 J 4 .  ? 20.305  -15.152 -24.156 0.90 58.48  ? 103 WJ4 B C6  1 
HETATM 2184 N  N   . WJ4 J 4 .  ? 16.904  -13.456 -24.695 0.90 66.34  ? 103 WJ4 B N   1 
HETATM 2185 C  C   . WJ4 J 4 .  ? 17.147  -15.590 -25.918 0.90 65.15  ? 103 WJ4 B C   1 
HETATM 2186 O  O   . WJ4 J 4 .  ? 22.236  -15.957 -22.941 0.90 57.31  ? 103 WJ4 B O   1 
HETATM 2187 C  C1  . WJ4 J 4 .  ? 17.718  -15.534 -24.645 0.90 63.63  ? 103 WJ4 B C1  1 
HETATM 2188 C  C2  . WJ4 J 4 .  ? 18.436  -16.685 -23.991 0.90 62.18  ? 103 WJ4 B C2  1 
HETATM 2189 C  C3  . WJ4 J 4 .  ? 19.987  -16.448 -22.166 0.90 59.66  ? 103 WJ4 B C3  1 
HETATM 2190 N  N2  . WJ4 J 4 .  ? 19.830  -16.440 -23.621 0.90 61.13  ? 103 WJ4 B N2  1 
HETATM 2191 S  S   . WJ4 J 4 .  ? 16.424  -14.058 -26.184 0.90 58.67  ? 103 WJ4 B S   1 
HETATM 2192 CL CL  . WJ4 J 4 .  ? 17.240  -16.947 -26.982 0.90 51.82  ? 103 WJ4 B CL  1 
HETATM 2193 S  S   . SO4 K 2 .  ? 29.987  -38.443 12.159  1.00 111.57 ? 101 SO4 C S   1 
HETATM 2194 O  O1  . SO4 K 2 .  ? 31.378  -38.064 12.090  1.00 107.21 ? 101 SO4 C O1  1 
HETATM 2195 O  O2  . SO4 K 2 .  ? 29.374  -38.225 10.880  1.00 90.05  ? 101 SO4 C O2  1 
HETATM 2196 O  O3  . SO4 K 2 .  ? 29.875  -39.833 12.516  1.00 109.50 ? 101 SO4 C O3  1 
HETATM 2197 O  O4  . SO4 K 2 .  ? 29.317  -37.646 13.154  1.00 114.39 ? 101 SO4 C O4  1 
HETATM 2198 N  N1  . WJ4 L 4 .  ? 16.289  -37.200 18.315  0.72 47.07  ? 102 WJ4 C N1  1 
HETATM 2199 C  C4  . WJ4 L 4 .  ? 16.899  -39.371 21.653  0.72 49.85  ? 102 WJ4 C C4  1 
HETATM 2200 C  C5  . WJ4 L 4 .  ? 18.347  -41.025 20.896  0.72 54.86  ? 102 WJ4 C C5  1 
HETATM 2201 C  C6  . WJ4 L 4 .  ? 18.649  -40.388 19.565  0.72 52.77  ? 102 WJ4 C C6  1 
HETATM 2202 N  N   . WJ4 L 4 .  ? 15.639  -36.173 17.891  0.72 42.30  ? 102 WJ4 C N   1 
HETATM 2203 C  C   . WJ4 L 4 .  ? 17.990  -35.955 17.535  0.72 42.42  ? 102 WJ4 C C   1 
HETATM 2204 O  O   . WJ4 L 4 .  ? 17.011  -40.740 21.319  0.72 54.55  ? 102 WJ4 C O   1 
HETATM 2205 C  C1  . WJ4 L 4 .  ? 17.633  -37.106 18.123  0.72 43.94  ? 102 WJ4 C C1  1 
HETATM 2206 C  C2  . WJ4 L 4 .  ? 18.568  -38.217 18.514  0.72 49.58  ? 102 WJ4 C C2  1 
HETATM 2207 C  C3  . WJ4 L 4 .  ? 17.768  -38.514 20.771  0.72 51.89  ? 102 WJ4 C C3  1 
HETATM 2208 N  N2  . WJ4 L 4 .  ? 17.907  -39.131 19.442  0.72 53.72  ? 102 WJ4 C N2  1 
HETATM 2209 S  S   . WJ4 L 4 .  ? 16.670  -35.047 17.220  0.72 45.92  ? 102 WJ4 C S   1 
HETATM 2210 CL CL  . WJ4 L 4 .  ? 19.590  -35.459 17.230  0.72 40.68  ? 102 WJ4 C CL  1 
HETATM 2211 O  O   . HOH M 5 .  ? 2.974   -4.707  -9.766  1.00 70.82  ? 201 HOH A O   1 
HETATM 2212 O  O   . HOH M 5 .  ? -6.475  -9.369  -5.826  1.00 46.23  ? 202 HOH A O   1 
HETATM 2213 O  O   . HOH M 5 .  ? 9.561   -22.631 -8.928  1.00 63.51  ? 203 HOH A O   1 
HETATM 2214 O  O   . HOH M 5 .  ? 3.477   -29.735 0.513   1.00 61.19  ? 204 HOH A O   1 
HETATM 2215 O  O   . HOH M 5 .  ? 11.549  -11.853 -6.291  1.00 25.81  ? 205 HOH A O   1 
HETATM 2216 O  O   . HOH M 5 .  ? 20.160  -15.926 6.675   1.00 51.35  ? 206 HOH A O   1 
HETATM 2217 O  O   . HOH M 5 .  ? 5.767   -29.234 6.739   1.00 69.12  ? 207 HOH A O   1 
HETATM 2218 O  O   . HOH M 5 .  ? 7.467   -10.185 -11.775 1.00 37.44  ? 208 HOH A O   1 
HETATM 2219 O  O   . HOH M 5 .  ? 9.813   -6.137  -2.468  1.00 56.93  ? 209 HOH A O   1 
HETATM 2220 O  O   . HOH M 5 .  ? 0.993   -24.777 13.546  1.00 64.18  ? 210 HOH A O   1 
HETATM 2221 O  O   . HOH M 5 .  ? 4.857   -1.575  -6.201  1.00 60.02  ? 211 HOH A O   1 
HETATM 2222 O  O   . HOH M 5 .  ? 5.058   -8.101  1.780   1.00 44.38  ? 212 HOH A O   1 
HETATM 2223 O  O   . HOH M 5 .  ? -1.772  3.181   -1.187  1.00 45.19  ? 213 HOH A O   1 
HETATM 2224 O  O   . HOH M 5 .  ? -7.093  -6.476  7.774   1.00 44.73  ? 214 HOH A O   1 
HETATM 2225 O  O   . HOH M 5 .  ? 17.793  -14.429 -20.810 1.00 41.16  ? 215 HOH A O   1 
HETATM 2226 O  O   . HOH M 5 .  ? 8.611   -17.314 -16.749 1.00 58.62  ? 216 HOH A O   1 
HETATM 2227 O  O   . HOH M 5 .  ? 12.946  -13.157 -9.675  1.00 67.21  ? 217 HOH A O   1 
HETATM 2228 O  O   . HOH M 5 .  ? 9.674   -32.698 3.606   1.00 67.03  ? 218 HOH A O   1 
HETATM 2229 O  O   . HOH M 5 .  ? 10.436  -27.895 1.635   1.00 60.45  ? 219 HOH A O   1 
HETATM 2230 O  O   . HOH M 5 .  ? 21.542  -16.943 -4.125  1.00 38.30  ? 220 HOH A O   1 
HETATM 2231 O  O   . HOH M 5 .  ? -1.255  -7.810  11.098  1.00 57.61  ? 221 HOH A O   1 
HETATM 2232 O  O   . HOH M 5 .  ? -7.389  -17.161 6.777   1.00 49.32  ? 222 HOH A O   1 
HETATM 2233 O  O   . HOH M 5 .  ? -6.325  -5.339  9.204   1.00 57.12  ? 223 HOH A O   1 
HETATM 2234 O  O   . HOH M 5 .  ? -5.542  -15.729 -8.216  1.00 52.69  ? 224 HOH A O   1 
HETATM 2235 O  O   . HOH M 5 .  ? 6.930   -5.738  -0.024  1.00 67.16  ? 225 HOH A O   1 
HETATM 2236 O  O   . HOH M 5 .  ? -2.143  -30.456 -3.686  1.00 60.17  ? 226 HOH A O   1 
HETATM 2237 O  O   . HOH M 5 .  ? 11.675  -23.921 9.783   1.00 48.69  ? 227 HOH A O   1 
HETATM 2238 O  O   . HOH M 5 .  ? 1.197   -16.976 -18.771 1.00 54.95  ? 228 HOH A O   1 
HETATM 2239 O  O   . HOH M 5 .  ? 10.883  -4.550  -7.061  1.00 63.30  ? 229 HOH A O   1 
HETATM 2240 O  O   . HOH M 5 .  ? -5.715  -11.028 -11.598 1.00 44.95  ? 230 HOH A O   1 
HETATM 2241 O  O   . HOH M 5 .  ? 11.966  -11.975 5.946   1.00 36.10  ? 231 HOH A O   1 
HETATM 2242 O  O   . HOH M 5 .  ? -5.334  -19.564 -5.885  1.00 56.20  ? 232 HOH A O   1 
HETATM 2243 O  O   . HOH M 5 .  ? 8.313   -17.250 9.112   1.00 72.83  ? 233 HOH A O   1 
HETATM 2244 O  O   . HOH M 5 .  ? 6.316   -15.641 -15.399 1.00 109.01 ? 234 HOH A O   1 
HETATM 2245 O  O   . HOH M 5 .  ? -1.283  -22.055 -1.017  1.00 43.58  ? 235 HOH A O   1 
HETATM 2246 O  O   . HOH M 5 .  ? -6.840  -20.607 -3.885  1.00 64.97  ? 236 HOH A O   1 
HETATM 2247 O  O   . HOH M 5 .  ? 0.605   -23.368 9.466   1.00 53.70  ? 237 HOH A O   1 
HETATM 2248 O  O   . HOH M 5 .  ? -5.379  -13.586 -16.447 1.00 51.77  ? 238 HOH A O   1 
HETATM 2249 O  O   . HOH M 5 .  ? -5.847  -27.159 2.596   1.00 66.26  ? 239 HOH A O   1 
HETATM 2250 O  O   . HOH M 5 .  ? 9.251   -9.284  -14.006 1.00 65.71  ? 240 HOH A O   1 
HETATM 2251 O  O   . HOH M 5 .  ? 17.654  -12.956 1.566   1.00 45.49  ? 241 HOH A O   1 
HETATM 2252 O  O   . HOH M 5 .  ? 10.104  -19.699 -19.749 1.00 53.17  ? 242 HOH A O   1 
HETATM 2253 O  O   . HOH M 5 .  ? 11.381  -8.205  0.079   1.00 44.19  ? 243 HOH A O   1 
HETATM 2254 O  O   . HOH M 5 .  ? 5.034   -3.164  -3.266  1.00 47.87  ? 244 HOH A O   1 
HETATM 2255 O  O   . HOH M 5 .  ? -0.562  -21.020 6.600   1.00 32.75  ? 245 HOH A O   1 
HETATM 2256 O  O   . HOH M 5 .  ? 9.070   -15.532 -13.760 1.00 58.17  ? 246 HOH A O   1 
HETATM 2257 O  O   . HOH M 5 .  ? -6.003  -13.085 6.510   1.00 45.29  ? 247 HOH A O   1 
HETATM 2258 O  O   . HOH M 5 .  ? 13.333  -11.829 -4.189  1.00 30.72  ? 248 HOH A O   1 
HETATM 2259 O  O   . HOH M 5 .  ? 16.311  -28.461 -0.390  1.00 63.89  ? 249 HOH A O   1 
HETATM 2260 O  O   . HOH M 5 .  ? 16.746  -24.199 1.240   1.00 41.83  ? 250 HOH A O   1 
HETATM 2261 O  O   . HOH M 5 .  ? 8.960   -18.398 -11.022 1.00 51.70  ? 251 HOH A O   1 
HETATM 2262 O  O   . HOH M 5 .  ? -7.728  -15.705 -1.190  1.00 42.93  ? 252 HOH A O   1 
HETATM 2263 O  O   . HOH M 5 .  ? -0.281  -20.600 11.224  1.00 66.58  ? 253 HOH A O   1 
HETATM 2264 O  O   . HOH M 5 .  ? -10.393 -16.632 -3.796  1.00 54.80  ? 254 HOH A O   1 
HETATM 2265 O  O   . HOH M 5 .  ? 5.923   -8.042  4.205   1.00 50.62  ? 255 HOH A O   1 
HETATM 2266 O  O   . HOH M 5 .  ? 10.482  -13.767 9.924   1.00 58.31  ? 256 HOH A O   1 
HETATM 2267 O  O   . HOH M 5 .  ? 0.251   -9.638  -16.117 1.00 66.18  ? 257 HOH A O   1 
HETATM 2268 O  O   . HOH M 5 .  ? -1.279  -11.878 11.197  1.00 37.62  ? 258 HOH A O   1 
HETATM 2269 O  O   . HOH M 5 .  ? 8.892   -8.293  4.369   1.00 45.34  ? 259 HOH A O   1 
HETATM 2270 O  O   . HOH M 5 .  ? -3.756  -10.776 6.576   1.00 58.86  ? 260 HOH A O   1 
HETATM 2271 O  O   . HOH M 5 .  ? 15.780  -11.625 -4.751  1.00 50.67  ? 261 HOH A O   1 
HETATM 2272 O  O   . HOH M 5 .  ? -8.325  -21.585 -1.954  1.00 64.64  ? 262 HOH A O   1 
HETATM 2273 O  O   . HOH M 5 .  ? 13.546  -28.131 -5.058  1.00 55.34  ? 263 HOH A O   1 
HETATM 2274 O  O   . HOH M 5 .  ? -4.789  -21.420 6.200   1.00 45.58  ? 264 HOH A O   1 
HETATM 2275 O  O   . HOH M 5 .  ? 8.083   -7.578  1.413   1.00 48.60  ? 265 HOH A O   1 
HETATM 2276 O  O   . HOH M 5 .  ? -3.933  -25.588 -6.104  1.00 56.56  ? 266 HOH A O   1 
HETATM 2277 O  O   . HOH M 5 .  ? 14.475  -13.316 10.537  1.00 52.41  ? 267 HOH A O   1 
HETATM 2278 O  O   . HOH M 5 .  ? 13.509  -9.733  -7.206  1.00 73.92  ? 268 HOH A O   1 
HETATM 2279 O  O   . HOH M 5 .  ? -7.728  -16.568 2.017   1.00 61.24  ? 269 HOH A O   1 
HETATM 2280 O  O   . HOH M 5 .  ? -5.440  -23.159 -6.961  1.00 56.23  ? 270 HOH A O   1 
HETATM 2281 O  O   . HOH M 5 .  ? -0.277  -30.241 10.057  1.00 59.45  ? 271 HOH A O   1 
HETATM 2282 O  O   . HOH M 5 .  ? 12.068  -20.786 10.657  1.00 66.77  ? 272 HOH A O   1 
HETATM 2283 O  O   . HOH M 5 .  ? -9.680  -13.544 -2.589  1.00 73.01  ? 273 HOH A O   1 
HETATM 2284 O  O   . HOH M 5 .  ? -6.996  -11.363 -7.977  1.00 44.50  ? 274 HOH A O   1 
HETATM 2285 O  O   . HOH M 5 .  ? 18.347  -17.731 -10.057 1.00 55.99  ? 275 HOH A O   1 
HETATM 2286 O  O   . HOH M 5 .  ? 15.201  -29.443 3.389   1.00 56.27  ? 276 HOH A O   1 
HETATM 2287 O  O   . HOH M 5 .  ? 0.537   -33.739 4.678   1.00 59.88  ? 277 HOH A O   1 
HETATM 2288 O  O   . HOH M 5 .  ? -2.885  -21.266 6.516   1.00 36.25  ? 278 HOH A O   1 
HETATM 2289 O  O   . HOH M 5 .  ? -3.582  -7.805  10.177  1.00 47.12  ? 279 HOH A O   1 
HETATM 2290 O  O   . HOH M 5 .  ? 11.943  -6.160  -3.407  1.00 60.16  ? 280 HOH A O   1 
HETATM 2291 O  O   . HOH M 5 .  ? 11.022  -27.583 -7.578  1.00 67.42  ? 281 HOH A O   1 
HETATM 2292 O  O   . HOH M 5 .  ? -6.745  -13.839 -9.097  1.00 44.58  ? 282 HOH A O   1 
HETATM 2293 O  O   . HOH M 5 .  ? 2.367   -24.407 -6.104  1.00 64.47  ? 283 HOH A O   1 
HETATM 2294 O  O   . HOH M 5 .  ? -10.799 -27.165 -1.799  1.00 53.31  ? 284 HOH A O   1 
HETATM 2295 O  O   . HOH M 5 .  ? -8.880  -19.413 2.206   1.00 56.79  ? 285 HOH A O   1 
HETATM 2296 O  O   . HOH M 5 .  ? -4.064  -26.669 7.285   1.00 55.28  ? 286 HOH A O   1 
HETATM 2297 O  O   . HOH M 5 .  ? 17.156  -9.585  -11.334 1.00 51.74  ? 287 HOH A O   1 
HETATM 2298 O  O   . HOH M 5 .  ? 1.073   5.401   -2.605  1.00 62.38  ? 288 HOH A O   1 
HETATM 2299 O  O   . HOH M 5 .  ? 22.564  -18.343 -1.337  1.00 57.38  ? 289 HOH A O   1 
HETATM 2300 O  O   . HOH M 5 .  ? 6.999   -1.310  0.644   1.00 53.75  ? 290 HOH A O   1 
HETATM 2301 O  O   . HOH M 5 .  ? 5.315   -9.494  -11.575 1.00 46.50  ? 291 HOH A O   1 
HETATM 2302 O  O   . HOH M 5 .  ? 2.447   -5.203  4.548   1.00 59.54  ? 292 HOH A O   1 
HETATM 2303 O  O   . HOH M 5 .  ? 10.248  -30.641 -1.043  1.00 60.95  ? 293 HOH A O   1 
HETATM 2304 O  O   . HOH M 5 .  ? 5.043   4.982   5.279   1.00 71.74  ? 294 HOH A O   1 
HETATM 2305 O  O   . HOH M 5 .  ? -4.878  -20.763 -9.305  1.00 66.60  ? 295 HOH A O   1 
HETATM 2306 O  O   . HOH M 5 .  ? -6.252  -23.168 5.564   1.00 59.51  ? 296 HOH A O   1 
HETATM 2307 O  O   . HOH M 5 .  ? 13.096  -18.071 -15.714 1.00 48.28  ? 297 HOH A O   1 
HETATM 2308 O  O   . HOH M 5 .  ? 17.280  -14.067 -15.207 1.00 57.24  ? 298 HOH A O   1 
HETATM 2309 O  O   . HOH M 5 .  ? 9.323   -0.792  1.014   1.00 55.44  ? 299 HOH A O   1 
HETATM 2310 O  O   . HOH M 5 .  ? -9.674  -21.574 -6.760  1.00 64.28  ? 300 HOH A O   1 
HETATM 2311 O  O   . HOH N 5 .  ? 10.860  -14.320 -45.327 1.00 53.83  ? 201 HOH B O   1 
HETATM 2312 O  O   . HOH N 5 .  ? 24.940  -5.371  -34.566 1.00 69.62  ? 202 HOH B O   1 
HETATM 2313 O  O   . HOH N 5 .  ? 16.480  -18.948 -29.645 1.00 24.80  ? 203 HOH B O   1 
HETATM 2314 O  O   . HOH N 5 .  ? 26.191  -22.939 -31.670 1.00 43.26  ? 204 HOH B O   1 
HETATM 2315 O  O   . HOH N 5 .  ? 10.057  -10.309 -38.435 1.00 71.72  ? 205 HOH B O   1 
HETATM 2316 O  O   . HOH N 5 .  ? 20.232  -22.660 -24.400 1.00 44.68  ? 206 HOH B O   1 
HETATM 2317 O  O   . HOH N 5 .  ? 26.360  -4.490  -34.435 1.00 49.97  ? 207 HOH B O   1 
HETATM 2318 O  O   . HOH N 5 .  ? 21.027  -25.401 -30.259 1.00 68.61  ? 208 HOH B O   1 
HETATM 2319 O  O   . HOH N 5 .  ? 23.810  -1.648  -37.104 1.00 58.59  ? 209 HOH B O   1 
HETATM 2320 O  O   . HOH N 5 .  ? 6.864   -11.878 -26.368 1.00 47.25  ? 210 HOH B O   1 
HETATM 2321 O  O   . HOH N 5 .  ? 8.759   -26.974 -38.754 1.00 60.59  ? 211 HOH B O   1 
HETATM 2322 O  O   . HOH N 5 .  ? 18.636  0.086   -25.976 1.00 65.40  ? 212 HOH B O   1 
HETATM 2323 O  O   . HOH N 5 .  ? 10.843  -21.765 -33.385 1.00 59.39  ? 213 HOH B O   1 
HETATM 2324 O  O   . HOH N 5 .  ? 27.243  -10.902 -29.260 1.00 57.53  ? 214 HOH B O   1 
HETATM 2325 O  O   . HOH N 5 .  ? 30.570  -7.638  -29.916 1.00 66.18  ? 215 HOH B O   1 
HETATM 2326 O  O   . HOH N 5 .  ? 21.559  -3.350  -25.440 1.00 74.86  ? 216 HOH B O   1 
HETATM 2327 O  O   . HOH N 5 .  ? 9.162   -8.400  -16.873 1.00 46.49  ? 217 HOH B O   1 
HETATM 2328 O  O   . HOH N 5 .  ? 10.520  -17.728 -44.219 1.00 52.03  ? 218 HOH B O   1 
HETATM 2329 O  O   . HOH N 5 .  ? 11.512  1.639   -39.562 1.00 44.88  ? 219 HOH B O   1 
HETATM 2330 O  O   . HOH N 5 .  ? 27.929  -7.945  -29.041 1.00 52.30  ? 220 HOH B O   1 
HETATM 2331 O  O   . HOH N 5 .  ? 7.798   -18.382 -34.415 1.00 77.18  ? 221 HOH B O   1 
HETATM 2332 O  O   . HOH N 5 .  ? 25.215  -4.565  -30.232 1.00 64.04  ? 222 HOH B O   1 
HETATM 2333 O  O   . HOH N 5 .  ? 10.401  -18.689 -33.495 1.00 45.33  ? 223 HOH B O   1 
HETATM 2334 O  O   . HOH N 5 .  ? 21.569  -9.864  -43.724 1.00 30.12  ? 224 HOH B O   1 
HETATM 2335 O  O   . HOH N 5 .  ? 14.666  -7.057  -41.117 1.00 72.64  ? 225 HOH B O   1 
HETATM 2336 O  O   . HOH N 5 .  ? 14.543  -24.465 -40.490 1.00 52.60  ? 226 HOH B O   1 
HETATM 2337 O  O   . HOH N 5 .  ? 19.960  -24.816 -34.083 1.00 49.73  ? 227 HOH B O   1 
HETATM 2338 O  O   . HOH N 5 .  ? 22.189  3.964   -33.428 1.00 43.94  ? 228 HOH B O   1 
HETATM 2339 O  O   . HOH N 5 .  ? 18.185  -0.378  -38.933 1.00 44.17  ? 229 HOH B O   1 
HETATM 2340 O  O   . HOH N 5 .  ? 23.264  -2.481  -29.081 1.00 63.34  ? 230 HOH B O   1 
HETATM 2341 O  O   . HOH N 5 .  ? 18.213  -12.780 -44.779 1.00 60.72  ? 231 HOH B O   1 
HETATM 2342 O  O   . HOH N 5 .  ? 31.788  -21.090 -38.255 1.00 72.79  ? 232 HOH B O   1 
HETATM 2343 O  O   . HOH N 5 .  ? 21.234  -5.752  -43.298 1.00 53.55  ? 233 HOH B O   1 
HETATM 2344 O  O   . HOH N 5 .  ? 2.041   -13.263 -28.110 1.00 56.21  ? 234 HOH B O   1 
HETATM 2345 O  O   . HOH N 5 .  ? 20.491  -13.264 -43.380 1.00 69.91  ? 235 HOH B O   1 
HETATM 2346 O  O   . HOH N 5 .  ? 23.765  -3.726  -37.425 1.00 53.32  ? 236 HOH B O   1 
HETATM 2347 O  O   . HOH N 5 .  ? 13.696  -4.747  -41.714 1.00 62.41  ? 237 HOH B O   1 
HETATM 2348 O  O   . HOH N 5 .  ? 33.253  -18.731 -43.153 1.00 73.57  ? 238 HOH B O   1 
HETATM 2349 O  O   . HOH N 5 .  ? 27.303  -17.626 -25.389 1.00 73.40  ? 239 HOH B O   1 
HETATM 2350 O  O   . HOH N 5 .  ? 22.943  -22.872 -29.113 1.00 65.33  ? 240 HOH B O   1 
HETATM 2351 O  O   . HOH N 5 .  ? 17.374  -19.552 -42.268 1.00 69.75  ? 241 HOH B O   1 
HETATM 2352 O  O   . HOH N 5 .  ? 25.657  -0.569  -29.919 1.00 74.12  ? 242 HOH B O   1 
HETATM 2353 O  O   . HOH N 5 .  ? 3.513   -7.962  -27.308 1.00 79.26  ? 243 HOH B O   1 
HETATM 2354 O  O   . HOH N 5 .  ? 19.226  -3.199  -22.679 1.00 66.89  ? 244 HOH B O   1 
HETATM 2355 O  O   . HOH N 5 .  ? 13.598  -21.743 -20.843 1.00 56.44  ? 245 HOH B O   1 
HETATM 2356 O  O   . HOH N 5 .  ? 5.984   -9.496  -40.143 1.00 66.48  ? 246 HOH B O   1 
HETATM 2357 O  O   . HOH N 5 .  ? 24.258  -9.887  -22.391 1.00 65.78  ? 247 HOH B O   1 
HETATM 2358 O  O   . HOH N 5 .  ? 8.119   -18.397 -31.741 1.00 70.14  ? 248 HOH B O   1 
HETATM 2359 O  O   . HOH N 5 .  ? 15.292  -8.433  -43.774 1.00 35.51  ? 249 HOH B O   1 
HETATM 2360 O  O   . HOH N 5 .  ? 20.258  4.215   -33.250 1.00 37.72  ? 250 HOH B O   1 
HETATM 2361 O  O   . HOH N 5 .  ? 18.580  -25.661 -29.653 1.00 70.11  ? 251 HOH B O   1 
HETATM 2362 O  O   . HOH N 5 .  ? 17.360  -24.629 -21.361 1.00 57.06  ? 252 HOH B O   1 
HETATM 2363 O  O   . HOH N 5 .  ? 6.446   -5.816  -34.477 1.00 98.29  ? 253 HOH B O   1 
HETATM 2364 O  O   . HOH N 5 .  ? 17.361  -9.122  -43.706 1.00 23.72  ? 254 HOH B O   1 
HETATM 2365 O  O   . HOH N 5 .  ? 7.753   -7.093  -20.881 1.00 61.65  ? 255 HOH B O   1 
HETATM 2366 O  O   . HOH N 5 .  ? 27.879  -24.871 -35.069 1.00 50.22  ? 256 HOH B O   1 
HETATM 2367 O  O   . HOH N 5 .  ? 9.879   -5.871  -41.267 1.00 57.92  ? 257 HOH B O   1 
HETATM 2368 O  O   . HOH N 5 .  ? 5.519   -18.996 -25.574 1.00 59.32  ? 258 HOH B O   1 
HETATM 2369 O  O   . HOH N 5 .  ? 17.897  4.716   -33.233 1.00 60.77  ? 259 HOH B O   1 
HETATM 2370 O  O   . HOH N 5 .  ? 19.529  -9.375  -43.646 1.00 22.08  ? 260 HOH B O   1 
HETATM 2371 O  O   . HOH N 5 .  ? 34.695  -23.692 -29.740 1.00 56.54  ? 261 HOH B O   1 
HETATM 2372 O  O   . HOH N 5 .  ? 12.825  -19.677 -19.642 1.00 51.67  ? 262 HOH B O   1 
HETATM 2373 O  O   . HOH N 5 .  ? 24.543  -5.586  -43.459 1.00 57.38  ? 263 HOH B O   1 
HETATM 2374 O  O   . HOH N 5 .  ? 40.008  -13.990 -39.080 1.00 76.26  ? 264 HOH B O   1 
HETATM 2375 O  O   . HOH N 5 .  ? 22.807  -23.311 -24.581 1.00 46.49  ? 265 HOH B O   1 
HETATM 2376 O  O   . HOH N 5 .  ? 15.254  -21.131 -42.383 1.00 54.90  ? 266 HOH B O   1 
HETATM 2377 O  O   . HOH N 5 .  ? 7.564   -9.012  -18.541 1.00 44.42  ? 267 HOH B O   1 
HETATM 2378 O  O   . HOH N 5 .  ? 33.477  -13.020 -37.394 1.00 60.51  ? 268 HOH B O   1 
HETATM 2379 O  O   . HOH O 5 .  ? 21.234  -36.711 8.531   1.00 48.76  ? 201 HOH C O   1 
HETATM 2380 O  O   . HOH O 5 .  ? 27.351  -38.065 10.092  1.00 48.84  ? 202 HOH C O   1 
HETATM 2381 O  O   . HOH O 5 .  ? 23.446  -18.622 20.777  1.00 40.15  ? 203 HOH C O   1 
HETATM 2382 O  O   . HOH O 5 .  ? 20.078  -20.374 30.382  1.00 57.05  ? 204 HOH C O   1 
HETATM 2383 O  O   . HOH O 5 .  ? 21.265  -19.974 24.734  1.00 64.78  ? 205 HOH C O   1 
HETATM 2384 O  O   . HOH O 5 .  ? 23.156  -38.093 9.608   1.00 32.72  ? 206 HOH C O   1 
HETATM 2385 O  O   . HOH O 5 .  ? 8.187   -31.607 12.214  1.00 63.45  ? 207 HOH C O   1 
HETATM 2386 O  O   . HOH O 5 .  ? 15.918  -17.972 19.348  1.00 76.34  ? 208 HOH C O   1 
HETATM 2387 O  O   . HOH O 5 .  ? 20.844  -39.592 26.839  1.00 58.98  ? 209 HOH C O   1 
HETATM 2388 O  O   . HOH O 5 .  ? 15.351  -21.112 12.375  1.00 62.61  ? 210 HOH C O   1 
HETATM 2389 O  O   . HOH O 5 .  ? 33.676  -23.870 31.359  1.00 54.13  ? 211 HOH C O   1 
HETATM 2390 O  O   . HOH O 5 .  ? 32.006  -33.879 26.097  1.00 60.95  ? 212 HOH C O   1 
HETATM 2391 O  O   . HOH O 5 .  ? 7.087   -18.245 11.045  1.00 48.94  ? 213 HOH C O   1 
HETATM 2392 O  O   . HOH O 5 .  ? 25.822  -31.521 10.789  1.00 50.86  ? 214 HOH C O   1 
HETATM 2393 O  O   . HOH O 5 .  ? 30.433  -36.562 29.039  1.00 63.38  ? 215 HOH C O   1 
HETATM 2394 O  O   . HOH O 5 .  ? 26.284  -38.122 26.692  1.00 61.75  ? 216 HOH C O   1 
HETATM 2395 O  O   . HOH O 5 .  ? 12.304  -28.910 28.277  1.00 49.22  ? 217 HOH C O   1 
HETATM 2396 O  O   . HOH O 5 .  ? 6.361   -25.917 17.064  1.00 65.78  ? 218 HOH C O   1 
HETATM 2397 O  O   . HOH O 5 .  ? 15.927  -39.789 16.838  1.00 60.03  ? 219 HOH C O   1 
HETATM 2398 O  O   . HOH O 5 .  ? 22.452  -28.618 10.841  1.00 55.05  ? 220 HOH C O   1 
HETATM 2399 O  O   . HOH O 5 .  ? 30.530  -32.419 19.019  1.00 76.87  ? 221 HOH C O   1 
HETATM 2400 O  O   . HOH O 5 .  ? 26.185  -17.792 13.974  1.00 62.40  ? 222 HOH C O   1 
HETATM 2401 O  O   . HOH O 5 .  ? 17.905  -17.350 14.947  1.00 54.40  ? 223 HOH C O   1 
HETATM 2402 O  O   . HOH O 5 .  ? 30.667  -17.341 10.889  1.00 55.97  ? 224 HOH C O   1 
HETATM 2403 O  O   . HOH O 5 .  ? 22.198  -35.207 17.036  1.00 41.17  ? 225 HOH C O   1 
HETATM 2404 O  O   . HOH O 5 .  ? 26.991  -38.770 12.544  1.00 54.96  ? 226 HOH C O   1 
HETATM 2405 O  O   . HOH O 5 .  ? 13.251  -31.555 8.203   1.00 46.19  ? 227 HOH C O   1 
HETATM 2406 O  O   . HOH O 5 .  ? 22.047  -13.213 13.253  1.00 58.74  ? 228 HOH C O   1 
HETATM 2407 O  O   . HOH O 5 .  ? 20.533  -41.965 12.342  1.00 55.39  ? 229 HOH C O   1 
HETATM 2408 O  O   . HOH O 5 .  ? 23.036  -22.241 8.501   1.00 71.58  ? 230 HOH C O   1 
HETATM 2409 O  O   . HOH O 5 .  ? 20.138  -12.819 13.802  1.00 52.20  ? 231 HOH C O   1 
HETATM 2410 O  O   . HOH O 5 .  ? 21.380  -28.626 8.418   1.00 58.73  ? 232 HOH C O   1 
HETATM 2411 O  O   . HOH O 5 .  ? 26.051  -18.349 20.916  1.00 46.38  ? 233 HOH C O   1 
HETATM 2412 O  O   . HOH O 5 .  ? 20.179  -20.015 10.596  1.00 63.32  ? 234 HOH C O   1 
HETATM 2413 O  O   . HOH O 5 .  ? 25.071  -33.398 35.287  1.00 88.00  ? 235 HOH C O   1 
HETATM 2414 O  O   . HOH O 5 .  ? 29.730  -25.800 32.378  1.00 75.20  ? 236 HOH C O   1 
HETATM 2415 O  O   . HOH O 5 .  ? 30.044  -33.410 14.415  1.00 79.42  ? 237 HOH C O   1 
HETATM 2416 O  O   . HOH O 5 .  ? 31.627  -38.643 31.509  1.00 67.56  ? 238 HOH C O   1 
HETATM 2417 O  O   . HOH O 5 .  ? 29.248  -16.027 13.617  1.00 72.38  ? 239 HOH C O   1 
HETATM 2418 O  O   . HOH O 5 .  ? 30.606  -30.786 34.526  1.00 64.60  ? 240 HOH C O   1 
HETATM 2419 O  O   . HOH O 5 .  ? 2.868   -28.121 14.245  1.00 56.43  ? 241 HOH C O   1 
HETATM 2420 O  O   . HOH O 5 .  ? 28.683  -37.426 16.310  1.00 76.22  ? 242 HOH C O   1 
HETATM 2421 O  O   . HOH O 5 .  ? 13.424  -37.838 14.079  1.00 59.75  ? 243 HOH C O   1 
HETATM 2422 O  O   . HOH O 5 .  ? 31.718  -39.678 27.308  1.00 62.16  ? 244 HOH C O   1 
HETATM 2423 O  O   . HOH O 5 .  ? 9.764   -30.510 10.020  1.00 39.83  ? 245 HOH C O   1 
HETATM 2424 O  O   . HOH O 5 .  ? 23.058  -41.810 18.615  1.00 53.49  ? 246 HOH C O   1 
HETATM 2425 O  O   . HOH O 5 .  ? 9.484   -18.857 23.756  1.00 63.60  ? 247 HOH C O   1 
HETATM 2426 O  O   . HOH O 5 .  ? 26.013  -39.903 20.388  1.00 46.22  ? 248 HOH C O   1 
HETATM 2427 O  O   . HOH O 5 .  ? 17.135  -34.523 29.026  1.00 62.62  ? 249 HOH C O   1 
HETATM 2428 O  O   . HOH O 5 .  ? 21.615  -29.814 4.443   1.00 67.97  ? 250 HOH C O   1 
HETATM 2429 O  O   . HOH O 5 .  ? 8.987   -37.381 21.518  1.00 51.69  ? 251 HOH C O   1 
HETATM 2430 O  O   . HOH O 5 .  ? 4.898   -23.421 18.098  1.00 66.73  ? 252 HOH C O   1 
HETATM 2431 O  O   . HOH O 5 .  ? 29.582  -41.601 27.427  1.00 52.77  ? 253 HOH C O   1 
HETATM 2432 O  O   . HOH O 5 .  ? 31.313  -44.774 16.106  1.00 68.23  ? 254 HOH C O   1 
HETATM 2433 O  O   . HOH O 5 .  ? 13.769  -39.511 9.198   1.00 68.61  ? 255 HOH C O   1 
HETATM 2434 O  O   . HOH O 5 .  ? 29.552  -40.802 31.842  1.00 70.89  ? 256 HOH C O   1 
HETATM 2435 O  O   . HOH O 5 .  ? 19.507  -42.491 39.087  1.00 67.40  ? 257 HOH C O   1 
HETATM 2436 O  O   . HOH O 5 .  ? 28.583  -41.536 29.672  1.00 53.35  ? 258 HOH C O   1 
HETATM 2437 O  O   . HOH O 5 .  ? 28.278  -39.717 20.010  1.00 58.47  ? 259 HOH C O   1 
HETATM 2438 O  O   . HOH O 5 .  ? 33.632  -44.031 12.194  1.00 55.15  ? 260 HOH C O   1 
HETATM 2439 O  O   . HOH O 5 .  ? 26.334  -14.253 11.595  1.00 53.61  ? 261 HOH C O   1 
HETATM 2440 O  O   . HOH O 5 .  ? 24.311  -13.864 12.921  1.00 74.44  ? 262 HOH C O   1 
HETATM 2441 O  O   . HOH O 5 .  ? 26.844  -39.901 24.618  1.00 55.56  ? 263 HOH C O   1 
HETATM 2442 O  O   . HOH O 5 .  ? 37.096  -25.792 28.382  1.00 72.22  ? 264 HOH C O   1 
HETATM 2443 O  O   . HOH O 5 .  ? 18.177  -16.731 28.267  1.00 52.06  ? 265 HOH C O   1 
# 
