data_7HGN
# 
_entry.id   7HGN 
# 
_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   7HGN         pdb_00007hgn 10.2210/pdb7hgn/pdb 
WWPDB D_1001407449 ?            ?                   
# 
_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                        7HGN 
_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 '(2,6-difluorophenyl)(pyrrolidin-1-yl)methanone'   211.208   2   ? ?    ? ? 
5 water       nat water                                              18.015    273 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                    SO4 
3 1,2-ETHANEDIOL                                   EDO 
4 '(2,6-difluorophenyl)(pyrrolidin-1-yl)methanone' NX7 
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 
NX7 non-polymer         . '(2,6-difluorophenyl)(pyrrolidin-1-yl)methanone' ?                 'C11 H11 F2 N O' 211.208 
PHE 'L-peptide linking' y PHENYLALANINE                                    ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                          ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                           ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                                    ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                                        ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                       ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                         ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                           ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 29 ALA ALA 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 33 VAL VAL 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 ?  ?   ?   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 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   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        NX7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NX7 
_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 NX7 1   103 101 NX7 LIG B . 
K 2 SO4 1   101 5   SO4 SO4 C . 
L 4 NX7 1   102 101 NX7 LIG C . 
M 5 HOH 1   201 202 HOH HOH A . 
M 5 HOH 2   202 304 HOH HOH A . 
M 5 HOH 3   203 307 HOH HOH A . 
M 5 HOH 4   204 259 HOH HOH A . 
M 5 HOH 5   205 335 HOH HOH A . 
M 5 HOH 6   206 343 HOH HOH A . 
M 5 HOH 7   207 334 HOH HOH A . 
M 5 HOH 8   208 341 HOH HOH A . 
M 5 HOH 9   209 218 HOH HOH A . 
M 5 HOH 10  210 260 HOH HOH A . 
M 5 HOH 11  211 66  HOH HOH A . 
M 5 HOH 12  212 208 HOH HOH A . 
M 5 HOH 13  213 139 HOH HOH A . 
M 5 HOH 14  214 293 HOH HOH A . 
M 5 HOH 15  215 86  HOH HOH A . 
M 5 HOH 16  216 55  HOH HOH A . 
M 5 HOH 17  217 301 HOH HOH A . 
M 5 HOH 18  218 351 HOH HOH A . 
M 5 HOH 19  219 71  HOH HOH A . 
M 5 HOH 20  220 42  HOH HOH A . 
M 5 HOH 21  221 34  HOH HOH A . 
M 5 HOH 22  222 142 HOH HOH A . 
M 5 HOH 23  223 26  HOH HOH A . 
M 5 HOH 24  224 289 HOH HOH A . 
M 5 HOH 25  225 91  HOH HOH A . 
M 5 HOH 26  226 199 HOH HOH A . 
M 5 HOH 27  227 292 HOH HOH A . 
M 5 HOH 28  228 23  HOH HOH A . 
M 5 HOH 29  229 8   HOH HOH A . 
M 5 HOH 30  230 32  HOH HOH A . 
M 5 HOH 31  231 28  HOH HOH A . 
M 5 HOH 32  232 290 HOH HOH A . 
M 5 HOH 33  233 37  HOH HOH A . 
M 5 HOH 34  234 97  HOH HOH A . 
M 5 HOH 35  235 85  HOH HOH A . 
M 5 HOH 36  236 188 HOH HOH A . 
M 5 HOH 37  237 27  HOH HOH A . 
M 5 HOH 38  238 87  HOH HOH A . 
M 5 HOH 39  239 7   HOH HOH A . 
M 5 HOH 40  240 84  HOH HOH A . 
M 5 HOH 41  241 1   HOH HOH A . 
M 5 HOH 42  242 278 HOH HOH A . 
M 5 HOH 43  243 12  HOH HOH A . 
M 5 HOH 44  244 60  HOH HOH A . 
M 5 HOH 45  245 78  HOH HOH A . 
M 5 HOH 46  246 203 HOH HOH A . 
M 5 HOH 47  247 167 HOH HOH A . 
M 5 HOH 48  248 300 HOH HOH A . 
M 5 HOH 49  249 2   HOH HOH A . 
M 5 HOH 50  250 99  HOH HOH A . 
M 5 HOH 51  251 38  HOH HOH A . 
M 5 HOH 52  252 288 HOH HOH A . 
M 5 HOH 53  253 370 HOH HOH A . 
M 5 HOH 54  254 94  HOH HOH A . 
M 5 HOH 55  255 115 HOH HOH A . 
M 5 HOH 56  256 336 HOH HOH A . 
M 5 HOH 57  257 35  HOH HOH A . 
M 5 HOH 58  258 179 HOH HOH A . 
M 5 HOH 59  259 267 HOH HOH A . 
M 5 HOH 60  260 111 HOH HOH A . 
M 5 HOH 61  261 131 HOH HOH A . 
M 5 HOH 62  262 58  HOH HOH A . 
M 5 HOH 63  263 145 HOH HOH A . 
M 5 HOH 64  264 274 HOH HOH A . 
M 5 HOH 65  265 363 HOH HOH A . 
M 5 HOH 66  266 93  HOH HOH A . 
M 5 HOH 67  267 164 HOH HOH A . 
M 5 HOH 68  268 95  HOH HOH A . 
M 5 HOH 69  269 299 HOH HOH A . 
M 5 HOH 70  270 20  HOH HOH A . 
M 5 HOH 71  271 18  HOH HOH A . 
M 5 HOH 72  272 190 HOH HOH A . 
M 5 HOH 73  273 116 HOH HOH A . 
M 5 HOH 74  274 109 HOH HOH A . 
M 5 HOH 75  275 318 HOH HOH A . 
M 5 HOH 76  276 297 HOH HOH A . 
M 5 HOH 77  277 211 HOH HOH A . 
M 5 HOH 78  278 21  HOH HOH A . 
M 5 HOH 79  279 14  HOH HOH A . 
M 5 HOH 80  280 222 HOH HOH A . 
M 5 HOH 81  281 327 HOH HOH A . 
M 5 HOH 82  282 165 HOH HOH A . 
M 5 HOH 83  283 143 HOH HOH A . 
M 5 HOH 84  284 47  HOH HOH A . 
M 5 HOH 85  285 296 HOH HOH A . 
M 5 HOH 86  286 9   HOH HOH A . 
M 5 HOH 87  287 19  HOH HOH A . 
M 5 HOH 88  288 77  HOH HOH A . 
M 5 HOH 89  289 73  HOH HOH A . 
M 5 HOH 90  290 16  HOH HOH A . 
M 5 HOH 91  291 364 HOH HOH A . 
M 5 HOH 92  292 113 HOH HOH A . 
M 5 HOH 93  293 281 HOH HOH A . 
M 5 HOH 94  294 31  HOH HOH A . 
M 5 HOH 95  295 210 HOH HOH A . 
M 5 HOH 96  296 22  HOH HOH A . 
M 5 HOH 97  297 372 HOH HOH A . 
M 5 HOH 98  298 362 HOH HOH A . 
M 5 HOH 99  299 374 HOH HOH A . 
M 5 HOH 100 300 63  HOH HOH A . 
M 5 HOH 101 301 83  HOH HOH A . 
M 5 HOH 102 302 219 HOH HOH A . 
M 5 HOH 103 303 156 HOH HOH A . 
M 5 HOH 104 304 108 HOH HOH A . 
M 5 HOH 105 305 64  HOH HOH A . 
M 5 HOH 106 306 185 HOH HOH A . 
M 5 HOH 107 307 152 HOH HOH A . 
M 5 HOH 108 308 57  HOH HOH A . 
M 5 HOH 109 309 375 HOH HOH A . 
M 5 HOH 110 310 283 HOH HOH A . 
M 5 HOH 111 311 205 HOH HOH A . 
M 5 HOH 112 312 75  HOH HOH A . 
M 5 HOH 113 313 313 HOH HOH A . 
M 5 HOH 114 314 332 HOH HOH A . 
M 5 HOH 115 315 358 HOH HOH A . 
N 5 HOH 1   201 247 HOH HOH B . 
N 5 HOH 2   202 258 HOH HOH B . 
N 5 HOH 3   203 329 HOH HOH B . 
N 5 HOH 4   204 123 HOH HOH B . 
N 5 HOH 5   205 215 HOH HOH B . 
N 5 HOH 6   206 371 HOH HOH B . 
N 5 HOH 7   207 366 HOH HOH B . 
N 5 HOH 8   208 249 HOH HOH B . 
N 5 HOH 9   209 68  HOH HOH B . 
N 5 HOH 10  210 69  HOH HOH B . 
N 5 HOH 11  211 272 HOH HOH B . 
N 5 HOH 12  212 172 HOH HOH B . 
N 5 HOH 13  213 72  HOH HOH B . 
N 5 HOH 14  214 242 HOH HOH B . 
N 5 HOH 15  215 357 HOH HOH B . 
N 5 HOH 16  216 98  HOH HOH B . 
N 5 HOH 17  217 89  HOH HOH B . 
N 5 HOH 18  218 333 HOH HOH B . 
N 5 HOH 19  219 46  HOH HOH B . 
N 5 HOH 20  220 169 HOH HOH B . 
N 5 HOH 21  221 224 HOH HOH B . 
N 5 HOH 22  222 17  HOH HOH B . 
N 5 HOH 23  223 345 HOH HOH B . 
N 5 HOH 24  224 119 HOH HOH B . 
N 5 HOH 25  225 261 HOH HOH B . 
N 5 HOH 26  226 316 HOH HOH B . 
N 5 HOH 27  227 10  HOH HOH B . 
N 5 HOH 28  228 54  HOH HOH B . 
N 5 HOH 29  229 315 HOH HOH B . 
N 5 HOH 30  230 353 HOH HOH B . 
N 5 HOH 31  231 153 HOH HOH B . 
N 5 HOH 32  232 137 HOH HOH B . 
N 5 HOH 33  233 5   HOH HOH B . 
N 5 HOH 34  234 331 HOH HOH B . 
N 5 HOH 35  235 359 HOH HOH B . 
N 5 HOH 36  236 6   HOH HOH B . 
N 5 HOH 37  237 320 HOH HOH B . 
N 5 HOH 38  238 117 HOH HOH B . 
N 5 HOH 39  239 168 HOH HOH B . 
N 5 HOH 40  240 25  HOH HOH B . 
N 5 HOH 41  241 61  HOH HOH B . 
N 5 HOH 42  242 24  HOH HOH B . 
N 5 HOH 43  243 59  HOH HOH B . 
N 5 HOH 44  244 101 HOH HOH B . 
N 5 HOH 45  245 175 HOH HOH B . 
N 5 HOH 46  246 36  HOH HOH B . 
N 5 HOH 47  247 120 HOH HOH B . 
N 5 HOH 48  248 76  HOH HOH B . 
N 5 HOH 49  249 96  HOH HOH B . 
N 5 HOH 50  250 150 HOH HOH B . 
N 5 HOH 51  251 79  HOH HOH B . 
N 5 HOH 52  252 13  HOH HOH B . 
N 5 HOH 53  253 214 HOH HOH B . 
N 5 HOH 54  254 280 HOH HOH B . 
N 5 HOH 55  255 74  HOH HOH B . 
N 5 HOH 56  256 197 HOH HOH B . 
N 5 HOH 57  257 303 HOH HOH B . 
N 5 HOH 58  258 346 HOH HOH B . 
N 5 HOH 59  259 170 HOH HOH B . 
N 5 HOH 60  260 157 HOH HOH B . 
N 5 HOH 61  261 279 HOH HOH B . 
N 5 HOH 62  262 217 HOH HOH B . 
N 5 HOH 63  263 44  HOH HOH B . 
N 5 HOH 64  264 104 HOH HOH B . 
N 5 HOH 65  265 223 HOH HOH B . 
N 5 HOH 66  266 367 HOH HOH B . 
N 5 HOH 67  267 201 HOH HOH B . 
N 5 HOH 68  268 182 HOH HOH B . 
N 5 HOH 69  269 177 HOH HOH B . 
N 5 HOH 70  270 319 HOH HOH B . 
N 5 HOH 71  271 163 HOH HOH B . 
N 5 HOH 72  272 291 HOH HOH B . 
N 5 HOH 73  273 349 HOH HOH B . 
N 5 HOH 74  274 356 HOH HOH B . 
N 5 HOH 75  275 339 HOH HOH B . 
N 5 HOH 76  276 322 HOH HOH B . 
N 5 HOH 77  277 352 HOH HOH B . 
N 5 HOH 78  278 160 HOH HOH B . 
N 5 HOH 79  279 314 HOH HOH B . 
N 5 HOH 80  280 107 HOH HOH B . 
N 5 HOH 81  281 369 HOH HOH B . 
N 5 HOH 82  282 312 HOH HOH B . 
N 5 HOH 83  283 310 HOH HOH B . 
O 5 HOH 1   201 361 HOH HOH C . 
O 5 HOH 2   202 254 HOH HOH C . 
O 5 HOH 3   203 161 HOH HOH C . 
O 5 HOH 4   204 321 HOH HOH C . 
O 5 HOH 5   205 323 HOH HOH C . 
O 5 HOH 6   206 317 HOH HOH C . 
O 5 HOH 7   207 350 HOH HOH C . 
O 5 HOH 8   208 269 HOH HOH C . 
O 5 HOH 9   209 173 HOH HOH C . 
O 5 HOH 10  210 49  HOH HOH C . 
O 5 HOH 11  211 295 HOH HOH C . 
O 5 HOH 12  212 118 HOH HOH C . 
O 5 HOH 13  213 337 HOH HOH C . 
O 5 HOH 14  214 338 HOH HOH C . 
O 5 HOH 15  215 90  HOH HOH C . 
O 5 HOH 16  216 226 HOH HOH C . 
O 5 HOH 17  217 15  HOH HOH C . 
O 5 HOH 18  218 284 HOH HOH C . 
O 5 HOH 19  219 45  HOH HOH C . 
O 5 HOH 20  220 56  HOH HOH C . 
O 5 HOH 21  221 134 HOH HOH C . 
O 5 HOH 22  222 189 HOH HOH C . 
O 5 HOH 23  223 271 HOH HOH C . 
O 5 HOH 24  224 305 HOH HOH C . 
O 5 HOH 25  225 149 HOH HOH C . 
O 5 HOH 26  226 135 HOH HOH C . 
O 5 HOH 27  227 41  HOH HOH C . 
O 5 HOH 28  228 82  HOH HOH C . 
O 5 HOH 29  229 344 HOH HOH C . 
O 5 HOH 30  230 126 HOH HOH C . 
O 5 HOH 31  231 102 HOH HOH C . 
O 5 HOH 32  232 132 HOH HOH C . 
O 5 HOH 33  233 122 HOH HOH C . 
O 5 HOH 34  234 4   HOH HOH C . 
O 5 HOH 35  235 302 HOH HOH C . 
O 5 HOH 36  236 40  HOH HOH C . 
O 5 HOH 37  237 48  HOH HOH C . 
O 5 HOH 38  238 294 HOH HOH C . 
O 5 HOH 39  239 43  HOH HOH C . 
O 5 HOH 40  240 53  HOH HOH C . 
O 5 HOH 41  241 62  HOH HOH C . 
O 5 HOH 42  242 67  HOH HOH C . 
O 5 HOH 43  243 342 HOH HOH C . 
O 5 HOH 44  244 246 HOH HOH C . 
O 5 HOH 45  245 148 HOH HOH C . 
O 5 HOH 46  246 298 HOH HOH C . 
O 5 HOH 47  247 275 HOH HOH C . 
O 5 HOH 48  248 365 HOH HOH C . 
O 5 HOH 49  249 209 HOH HOH C . 
O 5 HOH 50  250 198 HOH HOH C . 
O 5 HOH 51  251 373 HOH HOH C . 
O 5 HOH 52  252 130 HOH HOH C . 
O 5 HOH 53  253 330 HOH HOH C . 
O 5 HOH 54  254 287 HOH HOH C . 
O 5 HOH 55  255 328 HOH HOH C . 
O 5 HOH 56  256 354 HOH HOH C . 
O 5 HOH 57  257 309 HOH HOH C . 
O 5 HOH 58  258 355 HOH HOH C . 
O 5 HOH 59  259 65  HOH HOH C . 
O 5 HOH 60  260 146 HOH HOH C . 
O 5 HOH 61  261 171 HOH HOH C . 
O 5 HOH 62  262 241 HOH HOH C . 
O 5 HOH 63  263 70  HOH HOH C . 
O 5 HOH 64  264 270 HOH HOH C . 
O 5 HOH 65  265 348 HOH HOH C . 
O 5 HOH 66  266 103 HOH HOH C . 
O 5 HOH 67  267 340 HOH HOH C . 
O 5 HOH 68  268 324 HOH HOH C . 
O 5 HOH 69  269 368 HOH HOH C . 
O 5 HOH 70  270 347 HOH HOH C . 
O 5 HOH 71  271 151 HOH HOH C . 
O 5 HOH 72  272 92  HOH HOH C . 
O 5 HOH 73  273 360 HOH HOH C . 
O 5 HOH 74  274 206 HOH HOH C . 
O 5 HOH 75  275 125 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
4  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
5  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
6  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
7  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
8  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
9  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
10 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
11 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
12 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
13 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
14 1 Y 1 B LYS 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 73 ? CG  ? B LYS 74 CG  
19 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
20 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
21 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
22 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
23 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
24 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
25 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
26 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
27 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
28 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
29 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
30 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
31 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
32 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
33 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
34 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
35 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
36 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
37 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
38 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
39 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
40 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
41 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
42 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
43 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
44 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
45 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
46 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
47 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HGN 
_cell.length_a           41.310 
_cell.length_b           41.920 
_cell.length_c           158.030 
_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                         7HGN 
_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          7HGN 
_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                     7HGN 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             52.68 
_reflns.d_resolution_high            1.55 
_reflns.number_obs                   40913 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.064 
_reflns.pdbx_netI_over_sigmaI        12.0 
_reflns.pdbx_redundancy              6.1 
_reflns.pdbx_Rrim_I_all              0.070 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     251214 
_reflns.pdbx_chi_squared             0.97 
_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                  1.55 
_reflns_shell.d_res_low                   1.59 
_reflns_shell.number_measured_all         15560 
_reflns_shell.number_unique_obs           2986 
_reflns_shell.Rmerge_I_obs                2.155 
_reflns_shell.pdbx_chi_squared            0.82 
_reflns_shell.pdbx_redundancy             5.2 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.7 
_reflns_shell.pdbx_Rrim_I_all             2.397 
_reflns_shell.pdbx_Rpim_I_all             1.037 
_reflns_shell.pdbx_CC_half                0.355 
_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                                 7HGN 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     38673 
_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                             40.55 
_refine.ls_d_res_high                            1.55 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_R_factor_obs                          0.20249 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20023 
_refine.ls_R_factor_R_free                       0.24313 
_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                  2158 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.969 
_refine.correlation_coeff_Fo_to_Fc_free          0.958 
_refine.B_iso_mean                               35.588 
_refine.aniso_B[1][1]                            0.93 
_refine.aniso_B[2][2]                            0.24 
_refine.aniso_B[3][3]                            -1.16 
_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                       0.093 
_refine.pdbx_overall_ESU_R_Free                  0.097 
_refine.overall_SU_ML                            0.086 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.579 
_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        2137 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         64 
_refine_hist.number_atoms_solvent             273 
_refine_hist.number_atoms_total               2474 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        40.55 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.010  0.012  ? 2307 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.850  1.830  ? 3141 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.984  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       6.592  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.998 10.000 ? 302  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.134  0.200  ? 285  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1964 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.304  3.244  ? 1069 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.630  5.790  ? 1333 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.334  3.599  ? 1238 '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       9.053  48.80  ? 3604 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.550 
_refine_ls_shell.d_res_low                        1.590 
_refine_ls_shell.number_reflns_R_work             2788 
_refine_ls_shell.R_factor_R_work                  0.365 
_refine_ls_shell.percent_reflns_obs               99.63 
_refine_ls_shell.R_factor_R_free                  0.345 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             182 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGN 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z54226006' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGN 
_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 7HGN A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGN B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGN 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 7HGN GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGN SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGN GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGN SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGN GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGN SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O 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 ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HGN 
_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   A HOH 269 ? ? O C HOH 213 ? ? 1.51 
2  1 O   A HOH 268 ? ? O A HOH 290 ? ? 1.58 
3  1 O   B HOH 257 ? ? O B HOH 276 ? ? 1.74 
4  1 NE2 C HIS 89  ? ? O C HOH 201 ? ? 1.85 
5  1 O   B HOH 254 ? ? O B HOH 276 ? ? 1.97 
6  1 O   A HOH 302 ? ? O A HOH 307 ? ? 2.00 
7  1 O   C HOH 260 ? ? O C HOH 268 ? ? 2.02 
8  1 O4  A SO4 104 ? ? O A HOH 201 ? ? 2.03 
9  1 OH  A TYR 18  ? ? O A HOH 202 ? ? 2.07 
10 1 O   B HOH 250 ? ? O B HOH 275 ? ? 2.08 
11 1 O2  A SO4 104 ? ? O A HOH 203 ? ? 2.10 
12 1 O   B HOH 212 ? ? O B HOH 242 ? ? 2.15 
13 1 O2  C SO4 101 ? ? O C HOH 202 ? ? 2.15 
14 1 O   B ASP 27  ? B O B HOH 201 ? ? 2.16 
15 1 OD2 B ASP 26  ? ? O B HOH 202 ? ? 2.17 
16 1 O   A HOH 209 ? ? O A HOH 246 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 266 ? ? 1_555 O C HOH 229 ? ? 4_435 2.16 
2 1 O A HOH 257 ? ? 1_555 O A HOH 310 ? ? 4_545 2.18 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             C 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             C 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             C 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                110.49 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            10.29 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -159.15 65.72 
2 1 ASN B 38 ? ? 80.77   -2.69 
3 1 ASN B 87 ? ? -160.91 59.53 
4 1 ASN C 87 ? ? -160.19 55.01 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.089 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ASP 30 ? B ASP 31 
4  1 Y 1 B GLY 31 ? B GLY 32 
5  1 Y 1 B ALA 32 ? B ALA 33 
6  1 Y 1 C GLY 0  ? C GLY 1  
7  1 Y 1 C MET 1  ? C MET 2  
8  1 Y 1 C PRO 2  ? C PRO 3  
9  1 Y 1 C ASP 27 ? C ASP 28 
10 1 Y 1 C ILE 28 ? C ILE 29 
11 1 Y 1 C ALA 29 ? C ALA 30 
12 1 Y 1 C ASP 30 ? C ASP 31 
13 1 Y 1 C GLY 31 ? C GLY 32 
14 1 Y 1 C ALA 32 ? C ALA 33 
15 1 Y 1 C VAL 33 ? C VAL 34 
16 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 
NX7 C4   C Y N 260 
NX7 C5   C Y N 261 
NX7 C6   C N N 262 
NX7 C7   C N N 263 
NX7 C8   C N N 264 
NX7 C10  C N N 265 
NX7 N    N N N 266 
NX7 C    C Y N 267 
NX7 O    O N N 268 
NX7 C1   C Y N 269 
NX7 C2   C Y N 270 
NX7 C3   C Y N 271 
NX7 C9   C N N 272 
NX7 F    F N N 273 
NX7 F1   F N N 274 
NX7 H1   H N N 275 
NX7 H2   H N N 276 
NX7 H3   H N N 277 
NX7 H4   H N N 278 
NX7 H5   H N N 279 
NX7 H6   H N N 280 
NX7 H7   H N N 281 
NX7 H8   H N N 282 
NX7 H9   H N N 283 
NX7 H10  H N N 284 
NX7 H11  H N N 285 
PHE N    N N N 286 
PHE CA   C N S 287 
PHE C    C N N 288 
PHE O    O N N 289 
PHE CB   C N N 290 
PHE CG   C Y N 291 
PHE CD1  C Y N 292 
PHE CD2  C Y N 293 
PHE CE1  C Y N 294 
PHE CE2  C Y N 295 
PHE CZ   C Y N 296 
PHE OXT  O N N 297 
PHE H    H N N 298 
PHE H2   H N N 299 
PHE HA   H N N 300 
PHE HB2  H N N 301 
PHE HB3  H N N 302 
PHE HD1  H N N 303 
PHE HD2  H N N 304 
PHE HE1  H N N 305 
PHE HE2  H N N 306 
PHE HZ   H N N 307 
PHE HXT  H N N 308 
PRO N    N N N 309 
PRO CA   C N S 310 
PRO C    C N N 311 
PRO O    O N N 312 
PRO CB   C N N 313 
PRO CG   C N N 314 
PRO CD   C N N 315 
PRO OXT  O N N 316 
PRO H    H N N 317 
PRO HA   H N N 318 
PRO HB2  H N N 319 
PRO HB3  H N N 320 
PRO HG2  H N N 321 
PRO HG3  H N N 322 
PRO HD2  H N N 323 
PRO HD3  H N N 324 
PRO HXT  H N N 325 
SER N    N N N 326 
SER CA   C N S 327 
SER C    C N N 328 
SER O    O N N 329 
SER CB   C N N 330 
SER OG   O N N 331 
SER OXT  O N N 332 
SER H    H N N 333 
SER H2   H N N 334 
SER HA   H N N 335 
SER HB2  H N N 336 
SER HB3  H N N 337 
SER HG   H N N 338 
SER HXT  H N N 339 
SO4 S    S N N 340 
SO4 O1   O N N 341 
SO4 O2   O N N 342 
SO4 O3   O N N 343 
SO4 O4   O N N 344 
THR N    N N N 345 
THR CA   C N S 346 
THR C    C N N 347 
THR O    O N N 348 
THR CB   C N R 349 
THR OG1  O N N 350 
THR CG2  C N N 351 
THR OXT  O N N 352 
THR H    H N N 353 
THR H2   H N N 354 
THR HA   H N N 355 
THR HB   H N N 356 
THR HG1  H N N 357 
THR HG21 H N N 358 
THR HG22 H N N 359 
THR HG23 H N N 360 
THR HXT  H N N 361 
TRP N    N N N 362 
TRP CA   C N S 363 
TRP C    C N N 364 
TRP O    O N N 365 
TRP CB   C N N 366 
TRP CG   C Y N 367 
TRP CD1  C Y N 368 
TRP CD2  C Y N 369 
TRP NE1  N Y N 370 
TRP CE2  C Y N 371 
TRP CE3  C Y N 372 
TRP CZ2  C Y N 373 
TRP CZ3  C Y N 374 
TRP CH2  C Y N 375 
TRP OXT  O N N 376 
TRP H    H N N 377 
TRP H2   H N N 378 
TRP HA   H N N 379 
TRP HB2  H N N 380 
TRP HB3  H N N 381 
TRP HD1  H N N 382 
TRP HE1  H N N 383 
TRP HE3  H N N 384 
TRP HZ2  H N N 385 
TRP HZ3  H N N 386 
TRP HH2  H N N 387 
TRP HXT  H N N 388 
TYR N    N N N 389 
TYR CA   C N S 390 
TYR C    C N N 391 
TYR O    O N N 392 
TYR CB   C N N 393 
TYR CG   C Y N 394 
TYR CD1  C Y N 395 
TYR CD2  C Y N 396 
TYR CE1  C Y N 397 
TYR CE2  C Y N 398 
TYR CZ   C Y N 399 
TYR OH   O N N 400 
TYR OXT  O N N 401 
TYR H    H N N 402 
TYR H2   H N N 403 
TYR HA   H N N 404 
TYR HB2  H N N 405 
TYR HB3  H N N 406 
TYR HD1  H N N 407 
TYR HD2  H N N 408 
TYR HE1  H N N 409 
TYR HE2  H N N 410 
TYR HH   H N N 411 
TYR HXT  H N N 412 
VAL N    N N N 413 
VAL CA   C N S 414 
VAL C    C N N 415 
VAL O    O N N 416 
VAL CB   C N N 417 
VAL CG1  C N N 418 
VAL CG2  C N N 419 
VAL OXT  O N N 420 
VAL H    H N N 421 
VAL H2   H N N 422 
VAL HA   H N N 423 
VAL HB   H N N 424 
VAL HG11 H N N 425 
VAL HG12 H N N 426 
VAL HG13 H N N 427 
VAL HG21 H N N 428 
VAL HG22 H N N 429 
VAL HG23 H N N 430 
VAL HXT  H N N 431 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
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 
NX7 C9  C8   sing N N 246 
NX7 C9  C10  sing N N 247 
NX7 C8  C7   sing N N 248 
NX7 C10 N    sing N N 249 
NX7 C7  N    sing N N 250 
NX7 N   C6   sing N N 251 
NX7 F   C    sing N N 252 
NX7 C6  C5   sing N N 253 
NX7 C6  O    doub N N 254 
NX7 C5  C    doub Y N 255 
NX7 C5  C4   sing Y N 256 
NX7 C   C1   sing Y N 257 
NX7 F1  C4   sing N N 258 
NX7 C4  C3   doub Y N 259 
NX7 C1  C2   doub Y N 260 
NX7 C3  C2   sing Y N 261 
NX7 C7  H1   sing N N 262 
NX7 C7  H2   sing N N 263 
NX7 C8  H3   sing N N 264 
NX7 C8  H4   sing N N 265 
NX7 C10 H5   sing N N 266 
NX7 C10 H6   sing N N 267 
NX7 C1  H7   sing N N 268 
NX7 C2  H8   sing N N 269 
NX7 C3  H9   sing N N 270 
NX7 C9  H10  sing N N 271 
NX7 C9  H11  sing N N 272 
PHE N   CA   sing N N 273 
PHE N   H    sing N N 274 
PHE N   H2   sing N N 275 
PHE CA  C    sing N N 276 
PHE CA  CB   sing N N 277 
PHE CA  HA   sing N N 278 
PHE C   O    doub N N 279 
PHE C   OXT  sing N N 280 
PHE CB  CG   sing N N 281 
PHE CB  HB2  sing N N 282 
PHE CB  HB3  sing N N 283 
PHE CG  CD1  doub Y N 284 
PHE CG  CD2  sing Y N 285 
PHE CD1 CE1  sing Y N 286 
PHE CD1 HD1  sing N N 287 
PHE CD2 CE2  doub Y N 288 
PHE CD2 HD2  sing N N 289 
PHE CE1 CZ   doub Y N 290 
PHE CE1 HE1  sing N N 291 
PHE CE2 CZ   sing Y N 292 
PHE CE2 HE2  sing N N 293 
PHE CZ  HZ   sing N N 294 
PHE OXT HXT  sing N N 295 
PRO N   CA   sing N N 296 
PRO N   CD   sing N N 297 
PRO N   H    sing N N 298 
PRO CA  C    sing N N 299 
PRO CA  CB   sing N N 300 
PRO CA  HA   sing N N 301 
PRO C   O    doub N N 302 
PRO C   OXT  sing N N 303 
PRO CB  CG   sing N N 304 
PRO CB  HB2  sing N N 305 
PRO CB  HB3  sing N N 306 
PRO CG  CD   sing N N 307 
PRO CG  HG2  sing N N 308 
PRO CG  HG3  sing N N 309 
PRO CD  HD2  sing N N 310 
PRO CD  HD3  sing N N 311 
PRO OXT HXT  sing N N 312 
SER N   CA   sing N N 313 
SER N   H    sing N N 314 
SER N   H2   sing N N 315 
SER CA  C    sing N N 316 
SER CA  CB   sing N N 317 
SER CA  HA   sing N N 318 
SER C   O    doub N N 319 
SER C   OXT  sing N N 320 
SER CB  OG   sing N N 321 
SER CB  HB2  sing N N 322 
SER CB  HB3  sing N N 323 
SER OG  HG   sing N N 324 
SER OXT HXT  sing N N 325 
SO4 S   O1   doub N N 326 
SO4 S   O2   doub N N 327 
SO4 S   O3   sing N N 328 
SO4 S   O4   sing N N 329 
THR N   CA   sing N N 330 
THR N   H    sing N N 331 
THR N   H2   sing N N 332 
THR CA  C    sing N N 333 
THR CA  CB   sing N N 334 
THR CA  HA   sing N N 335 
THR C   O    doub N N 336 
THR C   OXT  sing N N 337 
THR CB  OG1  sing N N 338 
THR CB  CG2  sing N N 339 
THR CB  HB   sing N N 340 
THR OG1 HG1  sing N N 341 
THR CG2 HG21 sing N N 342 
THR CG2 HG22 sing N N 343 
THR CG2 HG23 sing N N 344 
THR OXT HXT  sing N N 345 
TRP N   CA   sing N N 346 
TRP N   H    sing N N 347 
TRP N   H2   sing N N 348 
TRP CA  C    sing N N 349 
TRP CA  CB   sing N N 350 
TRP CA  HA   sing N N 351 
TRP C   O    doub N N 352 
TRP C   OXT  sing N N 353 
TRP CB  CG   sing N N 354 
TRP CB  HB2  sing N N 355 
TRP CB  HB3  sing N N 356 
TRP CG  CD1  doub Y N 357 
TRP CG  CD2  sing Y N 358 
TRP CD1 NE1  sing Y N 359 
TRP CD1 HD1  sing N N 360 
TRP CD2 CE2  doub Y N 361 
TRP CD2 CE3  sing Y N 362 
TRP NE1 CE2  sing Y N 363 
TRP NE1 HE1  sing N N 364 
TRP CE2 CZ2  sing Y N 365 
TRP CE3 CZ3  doub Y N 366 
TRP CE3 HE3  sing N N 367 
TRP CZ2 CH2  doub Y N 368 
TRP CZ2 HZ2  sing N N 369 
TRP CZ3 CH2  sing Y N 370 
TRP CZ3 HZ3  sing N N 371 
TRP CH2 HH2  sing N N 372 
TRP OXT HXT  sing N N 373 
TYR N   CA   sing N N 374 
TYR N   H    sing N N 375 
TYR N   H2   sing N N 376 
TYR CA  C    sing N N 377 
TYR CA  CB   sing N N 378 
TYR CA  HA   sing N N 379 
TYR C   O    doub N N 380 
TYR C   OXT  sing N N 381 
TYR CB  CG   sing N N 382 
TYR CB  HB2  sing N N 383 
TYR CB  HB3  sing N N 384 
TYR CG  CD1  doub Y N 385 
TYR CG  CD2  sing Y N 386 
TYR CD1 CE1  sing Y N 387 
TYR CD1 HD1  sing N N 388 
TYR CD2 CE2  doub Y N 389 
TYR CD2 HD2  sing N N 390 
TYR CE1 CZ   doub Y N 391 
TYR CE1 HE1  sing N N 392 
TYR CE2 CZ   sing Y N 393 
TYR CE2 HE2  sing N N 394 
TYR CZ  OH   sing N N 395 
TYR OH  HH   sing N N 396 
TYR OXT HXT  sing N N 397 
VAL N   CA   sing N N 398 
VAL N   H    sing N N 399 
VAL N   H2   sing N N 400 
VAL CA  C    sing N N 401 
VAL CA  CB   sing N N 402 
VAL CA  HA   sing N N 403 
VAL C   O    doub N N 404 
VAL C   OXT  sing N N 405 
VAL CB  CG1  sing N N 406 
VAL CB  CG2  sing N N 407 
VAL CB  HB   sing N N 408 
VAL CG1 HG11 sing N N 409 
VAL CG1 HG12 sing N N 410 
VAL CG1 HG13 sing N N 411 
VAL CG2 HG21 sing N N 412 
VAL CG2 HG22 sing N N 413 
VAL CG2 HG23 sing N N 414 
VAL OXT HXT  sing N N 415 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium 1SC9822N 1 
'Research Foundation - Flanders (FWO)' Belgium 1SC9824N 2 
'Research Foundation - Flanders (FWO)' Belgium G053822N 3 
# 
_pdbx_deposit_group.group_id            G_1002305 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_description   
'Fragment screening against HRP-2 PWWP domain at the XChem facility of Diamond Light Source' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HGN 
_atom_sites.fract_transf_matrix[1][1]   0.024207 
_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]   0.023855 
_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]   0.006328 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
F 
N 
O 
S 
# 
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  ? 0.409   4.276   2.546   1.00 48.99  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.655  3.563   1.793   1.00 50.78  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? -0.050  2.524   0.845   1.00 47.35  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.049   2.687   0.324   1.00 43.54  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.582  4.529   1.042   1.00 49.88  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.574  5.245   1.945   1.00 61.32  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.797  4.271   2.858   1.00 56.61  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -4.585  5.649   3.703   1.00 58.37  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.753  1.388   0.632   1.00 43.45  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.274  0.303   -0.227  1.00 38.95  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? -0.074  0.688   -1.694  1.00 37.47  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.817  1.485   -2.257  1.00 38.44  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.455  -0.714  -0.066  1.00 39.50  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.967  -0.437  1.341   1.00 43.07  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -2.042  1.072   1.278   1.00 42.86  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 0.932   0.076   -2.306  1.00 33.79  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.121   0.200   -3.730  1.00 33.19  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.590   -1.094  -4.324  1.00 31.95  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.153   -1.981  -3.588  1.00 32.09  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.630   0.304   -4.021  1.00 40.56  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.289   1.529   -3.455  1.00 53.53  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.139   1.995   -2.164  1.00 64.22  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.141   2.382   -4.047  1.00 59.85  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 3.859   3.101   -2.003  1.00 64.41  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.480   3.349   -3.137  1.00 58.26  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.654   -1.208  -5.649  1.00 25.03  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.421   -2.467  -6.324  1.00 25.98  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.532   -3.446  -5.928  1.00 25.68  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.619   -3.053  -5.453  1.00 25.85  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.420   -2.187  -7.821  1.00 29.59  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.227   -4.739  -6.070  1.00 27.24  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.241   -5.764  -5.894  1.00 25.23  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.379   -5.599  -6.905  1.00 25.30  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.169   -5.207  -8.062  1.00 26.84  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.641   -7.174  -6.006  1.00 24.03  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 0.888   -7.594  -4.757  1.00 26.80  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.579   -7.810  -3.564  1.00 24.73  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.502  -7.790  -4.787  1.00 23.51  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 0.918   -8.177  -2.381  1.00 23.30  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -1.154  -8.219  -3.629  1.00 23.22  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.475  -8.369  -2.427  1.00 22.59  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.603   -5.949  -6.454  1.00 21.33  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 5.763   -5.881  -7.330  1.00 24.55  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.668   -7.080  -7.032  1.00 21.07  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.647   -7.655  -5.936  1.00 22.51  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.539   -4.577  -7.101  1.00 28.05  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.157   -4.484  -5.719  1.00 29.30  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 7.836   -3.144  -5.447  1.00 36.69  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.471   -3.102  -4.097  1.00 38.87  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.559   -3.380  -2.988  1.00 37.91  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.520   -7.505  -7.981  1.00 22.50  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.440   -8.622  -7.733  1.00 21.62  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.256   -8.349  -6.463  1.00 22.27  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.684   -7.222  -6.222  1.00 23.26  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.341   -8.616  -9.015  1.00 24.79  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.424   -7.974  -10.056 1.00 26.31  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.623   -6.915  -9.332  1.00 25.76  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.442   -9.404  -5.643  1.00 20.67  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.167  -9.300  -4.392  1.00 19.23  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.228   -9.165  -3.193  1.00 21.32  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.565   -9.490  -2.038  1.00 21.49  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 7.973   -8.757  -3.436  1.00 18.87  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.084   -8.691  -2.286  1.00 17.27  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 6.806   -10.076 -1.678  1.00 17.49  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.600   -11.050 -2.389  1.00 19.55  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.739   -8.093  -2.694  1.00 21.90  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.756   -6.587  -2.908  1.00 24.11  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.755   -5.929  -2.511  1.00 25.81  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 4.802   -6.078  -3.519  1.00 24.74  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.699   -10.136 -0.328  1.00 18.98  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.502   -11.408 0.372   1.00 17.44  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.038   -11.491 0.806   1.00 15.77  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.455   -10.465 1.259   1.00 19.50  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.444   -11.466 1.591   1.00 18.44  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 8.929   -11.303 1.221   1.00 19.78  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 9.774   -11.439 2.493   1.00 21.47  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.375   -12.287 0.137   1.00 20.40  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.481   -12.695 0.655   1.00 17.83  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.053   -12.865 0.905   1.00 18.02  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 2.792   -14.227 1.518   1.00 20.49  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.633   -15.114 1.532   1.00 18.56  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.274   -12.767 -0.421  1.00 17.32  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.379   -11.361 -1.033  1.00 19.65  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.654   -13.877 -1.399  1.00 17.97  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.565   -14.403 2.037   1.00 18.63  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 0.996   -15.735 2.055   1.00 19.81  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? -0.010  -15.809 0.903   1.00 22.24  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.767  -14.864 0.674   1.00 21.31  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.222   -16.046 3.361   1.00 21.72  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.164   -16.149 4.543   1.00 20.25  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.507   -15.014 5.279   1.00 22.57  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.664   -17.396 4.908   1.00 22.46  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.414   -15.141 6.316   1.00 26.33  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.543   -17.524 5.973   1.00 26.56  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 2.926   -16.384 6.648   1.00 24.71  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.082   -16.897 0.122   1.00 21.83  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.673  -17.025 -1.110  1.00 20.15  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.674  -18.160 -0.888  1.00 22.29  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -1.329  -19.230 -0.355  1.00 22.75  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.226   -17.298 -2.331  1.00 19.03  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.919  -17.917 -1.320  1.00 20.86  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.953  -18.922 -1.078  1.00 23.90  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.338  -19.611 -2.384  1.00 24.18  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.748  -18.921 -3.327  1.00 27.95  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -5.187  -18.266 -0.440  1.00 25.55  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -6.365  -19.273 -0.147  1.00 30.06  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.913  -20.196 0.994   1.00 33.39  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -7.004  -20.995 1.689   1.00 38.14  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.506  -22.030 0.778   1.00 34.42  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -4.289  -20.958 -2.345  1.00 25.64  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.825  -21.828 -3.380  1.00 28.62  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.897  -22.725 -2.754  1.00 31.14  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.750  -23.174 -1.617  1.00 27.53  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.743  -22.796 -3.862  1.00 29.95  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -2.400  -22.126 -4.115  1.00 35.83  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -2.327  -21.714 -5.869  1.00 36.70  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.669  -23.269 -6.431  1.00 31.95  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.929  -22.998 -3.556  1.00 37.24  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.995  -23.931 -3.229  1.00 42.48  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -7.390  -25.191 -2.638  1.00 35.28  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -6.480  -25.797 -3.209  1.00 40.24  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.768  -24.317 -4.497  1.00 49.70  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -10.267 -24.052 -4.417  1.00 61.91  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.832 -23.194 -5.550  1.00 60.09  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.862  -25.544 -1.441  1.00 35.57  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -7.473  -26.819 -0.885  1.00 32.50  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -6.130  -26.805 -0.170  1.00 39.93  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.709  -27.856 0.313   1.00 38.92  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -5.457  -25.637 -0.099  1.00 31.96  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -4.209  -25.582 0.638   1.00 32.76  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -4.290  -24.461 1.662   1.00 29.73  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.997  -23.492 1.440   1.00 30.54  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.959  -25.266 -0.194  1.00 37.47  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.679  -26.276 -1.293  1.00 38.50  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.804  -27.331 -1.098  1.00 47.68  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -3.309  -26.160 -2.521  1.00 40.25  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -1.578  -28.260 -2.104  1.00 57.78  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -3.092  -27.076 -3.536  1.00 48.20  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -2.222  -28.128 -3.324  1.00 56.21  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -2.037  -29.005 -4.356  1.00 67.13  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -3.528  -24.552 2.779   1.00 29.07  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -3.433  -23.469 3.762   1.00 28.03  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.736  -22.278 3.091   1.00 28.02  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -2.042  -22.458 2.087   1.00 26.91  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.574  -24.047 4.902   1.00 30.18  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.796  -25.151 4.247   1.00 32.34  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.647  -25.693 3.095   1.00 31.79  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.971  -21.082 3.634   1.00 25.47  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -2.269  -19.876 3.193   1.00 23.74  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.766  -20.152 3.288   1.00 23.96  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? -0.292  -20.588 4.347   1.00 26.20  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.713  -18.662 4.014   1.00 22.49  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -4.153  -18.273 3.822   1.00 25.46  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -5.151  -18.951 4.497   1.00 27.90  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.730  -17.272 3.156   1.00 24.30  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -6.330  -18.421 4.177   1.00 26.06  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -6.126  -17.396 3.332   1.00 26.86  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? -0.038  -19.928 2.163   1.00 22.96  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.266   -20.568 1.997   1.00 22.58  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.340   -19.483 1.847   1.00 22.06  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.160   -18.565 1.062   1.00 23.24  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.254   -21.491 0.763   1.00 21.58  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.369   -22.499 0.819   1.00 22.45  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 3.707   -22.305 0.605   1.00 24.94  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.216   -23.905 1.138   1.00 25.27  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.382   -23.502 0.752   1.00 25.05  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.506   -24.494 1.101   1.00 28.14  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.123   -24.720 1.449   1.00 29.41  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 3.743   -25.854 1.340   1.00 28.84  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.359   -26.078 1.653   1.00 31.86  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.647   -26.629 1.660   1.00 32.26  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.488   -19.555 2.576   1.00 21.72  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.546   -18.537 2.450   1.00 20.16  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.062   -18.489 1.009   1.00 18.32  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.304   -19.529 0.377   1.00 21.27  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 5.594   -19.000 3.481   1.00 20.00  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.393   -20.505 3.601   1.00 18.53  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 3.827   -20.604 3.537   1.00 18.42  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.143   -17.276 0.450   1.00 17.11  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.422   -17.179 -0.983  1.00 17.97  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 5.990   -15.794 -1.315  1.00 17.93  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.014   -14.890 -0.483  1.00 18.57  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.116   -17.452 -1.800  1.00 18.90  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.499   -15.637 -2.557  1.00 19.13  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 6.945   -14.332 -3.013  1.00 18.27  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.397   -14.045 -4.402  1.00 17.54  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.153   -15.010 -5.144  1.00 20.03  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.476   -14.128 -2.945  1.00 19.23  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.173   -15.080 -3.912  1.00 18.51  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 10.735  -14.872 -3.772  1.00 19.43  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.361  -15.678 -4.839  1.00 21.17  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 12.613  -16.133 -4.760  1.00 20.92  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.309  -15.981 -3.639  1.00 20.62  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.145  -16.756 -5.819  1.00 23.49  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.279   -12.756 -4.729  1.00 17.35  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.054   -12.426 -6.135  1.00 17.89  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.396   -12.526 -6.848  1.00 21.72  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.348   -11.857 -6.465  1.00 21.16  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.540   -10.978 -6.251  1.00 20.09  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.353   -10.570 -5.330  1.00 28.64  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.304   -10.677 -7.738  1.00 21.01  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.005   -11.134 -5.670  1.00 33.20  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.446   -13.378 -7.870  1.00 22.66  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.676   -13.569 -8.619  1.00 25.39  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 8.818   -12.553 -9.742  1.00 25.88  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 7.865   -11.951 -10.215 1.00 24.60  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 8.773   -14.962 -9.219  1.00 25.22  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 9.783   -15.902 -8.574  1.00 23.26  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.374  -15.534 -7.533  1.00 29.31  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 9.902   -17.025 -9.053  1.00 27.20  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.086  -12.362 -10.151 1.00 28.00  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.386  -11.744 -11.425 1.00 31.28  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.124  -12.759 -12.531 1.00 27.15  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 9.980   -13.942 -12.307 1.00 30.95  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 11.877  -11.437 -11.503 1.00 35.89  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.388  -10.359 -10.554 1.00 45.65  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.049  -9.172  -10.791 1.00 45.97  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.123  -10.718 -9.596  1.00 49.30  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.038  -12.275 -13.755 1.00 30.63  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 9.979   -13.164 -14.909 1.00 28.17  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.331  -12.984 -15.592 1.00 27.55  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.676  -11.848 -15.868 1.00 30.34  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 8.846   -12.659 -15.803 1.00 32.92  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.507   -12.619 -15.072 1.00 35.83  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 8.772   -13.455 -17.108 1.00 30.88  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.593   -11.510 -15.558 1.00 33.95  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.073  -14.084 -15.783 1.00 28.99  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.384  -13.963 -16.425 1.00 30.30  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.182  -13.632 -17.906 1.00 29.19  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.137  -13.910 -18.509 1.00 29.49  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.200  -15.233 -16.245 1.00 30.85  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.155  -12.896 -18.448 1.00 28.71  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.208  -12.770 -19.901 1.00 28.32  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 13.977  -14.137 -20.532 1.00 22.50  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.597  -15.121 -20.148 1.00 29.65  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.586  -12.227 -20.237 1.00 29.98  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.685  -10.718 -20.103 1.00 31.40  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.632  -10.077 -20.089 1.00 34.06  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.817  -10.188 -20.096 1.00 35.70  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.114  -14.158 -21.554 1.00 25.23  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 12.899  -15.344 -22.353 1.00 27.12  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 11.964  -16.352 -21.690 1.00 34.49  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.673  -17.376 -22.298 1.00 32.77  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.577  -16.087 -20.428 1.00 28.58  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.685  -16.966 -19.673 1.00 30.79  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.203   -16.730 -19.989 1.00 26.43  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 8.766   -15.663 -20.401 1.00 28.84  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 10.944  -16.797 -18.175 1.00 33.64  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.388   -17.750 -19.677 1.00 32.02  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 6.944   -17.677 -19.870 1.00 28.03  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.334   -16.645 -18.915 1.00 31.33  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.581   -16.689 -17.704 1.00 34.31  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.413   -19.103 -19.577 1.00 34.50  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 4.887   -19.141 -19.604 1.00 34.89  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 6.989   -20.139 -20.551 1.00 34.26  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.574   -15.700 -19.478 1.00 32.63  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 4.870   -14.656 -18.744 1.00 32.17  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.553   -15.209 -18.201 1.00 33.36  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 2.996   -16.154 -18.739 1.00 32.89  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.531   -13.457 -19.628 1.00 34.74  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 5.796   -12.767 -20.194 1.00 30.72  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.428   -11.594 -21.089 1.00 39.93  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.168   -12.011 -22.497 1.00 40.62  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 4.908   -10.797 -23.262 1.00 41.65  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.036   -14.609 -17.109 1.00 34.65  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 1.732   -14.990 -16.559 1.00 30.09  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.646   -14.444 -17.468 1.00 33.52  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 0.847   -13.502 -18.238 1.00 36.42  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.639   -14.286 -15.168 1.00 31.70  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 2.933   -13.498 -15.019 1.00 36.40  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.667   -13.506 -16.375 1.00 31.40  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.590  -14.953 -17.324 1.00 35.12  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.748  -14.293 -17.932 1.00 34.49  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.951  -12.868 -17.445 1.00 41.77  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.468  -12.506 -16.370 1.00 31.59  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.937  -15.169 -17.502 1.00 38.27  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.339  -16.442 -16.988 1.00 34.05  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.918  -16.167 -16.563 1.00 37.62  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.727  -12.032 -18.178 1.00 40.38  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -3.151  -10.721 -17.676 1.00 43.39  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.814  -10.777 -16.304 1.00 36.30  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.504  -11.741 -15.972 1.00 41.28  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -4.128  -10.238 -18.772 1.00 46.96  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.537  -11.509 -19.460 1.00 44.49  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.246  -12.307 -19.538 1.00 49.73  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.529  -9.744  -15.516 1.00 36.55  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.968  -9.537  -14.150 1.00 37.42  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.469  -10.614 -13.182 1.00 35.22  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.941  -10.622 -12.032 1.00 36.07  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.464  -9.247  -14.095 1.00 45.36  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.756  -7.996  -14.885 1.00 46.30  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.618  -6.885  -14.360 1.00 42.72  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.113  -8.159  -16.151 1.00 52.16  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.502  -11.468 -13.608 1.00 31.64  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.944  -12.496 -12.715 1.00 25.03  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.429  -12.274 -12.501 1.00 24.22  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.236   -11.632 -13.311 1.00 28.66  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -2.168  -13.951 -13.114 1.00 29.11  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.600  -14.349 -13.529 1.00 34.24  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.575  -13.921 -12.438 1.00 37.61  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.998  -14.333 -12.755 1.00 41.95  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -6.056  -15.796 -12.731 1.00 42.97  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.030   -12.671 -11.307 1.00 20.30  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.436   -12.518 -10.926 1.00 20.40  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.042   -13.903 -10.825 1.00 19.64  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.392   -14.878 -10.423 1.00 21.48  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.527   -11.940 -9.486  1.00 20.27  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.062   -10.499 -9.459  1.00 24.53  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.298  -10.214 -9.317  1.00 26.50  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 1.942   -9.445  -9.679  1.00 26.29  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.761  -8.907  -9.334  1.00 28.97  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.483   -8.133  -9.701  1.00 27.36  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.125   -7.880  -9.534  1.00 27.67  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.383  -6.618  -9.639  1.00 33.38  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.370   -14.060 -11.076 1.00 20.82  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.000   -15.362 -10.886 1.00 18.52  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.314   -15.521 -9.403  1.00 20.59  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.049   -14.707 -8.846  1.00 23.14  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.272   -15.256 -11.750 1.00 21.87  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.530   -13.792 -11.923 1.00 22.56  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.277   -12.978 -11.519 1.00 23.30  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 3.696   -16.517 -8.765  1.00 18.77  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 3.935   -16.672 -7.320  1.00 18.48  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 4.885   -17.833 -7.134  1.00 19.59  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.564   -18.964 -7.529  1.00 21.83  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.594   -16.931 -6.624  1.00 18.25  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.630   -15.756 -6.939  1.00 20.18  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 2.858   -17.089 -5.109  1.00 19.09  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.170   -14.367 -6.604  1.00 20.60  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.021   -17.589 -6.420  1.00 19.72  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 6.911   -18.678 -6.041  1.00 20.02  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 6.633   -19.111 -4.599  1.00 19.72  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 6.723   -18.293 -3.685  1.00 20.75  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.361   -18.174 -6.177  1.00 20.86  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.400   -19.218 -5.775  1.00 22.17  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 9.784   -20.224 -6.657  1.00 25.92  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 9.951   -19.228 -4.484  1.00 25.86  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 10.692  -21.191 -6.262  1.00 28.18  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 10.871  -20.200 -4.091  1.00 29.91  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.252  -21.177 -4.995  1.00 28.18  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.236   -20.387 -4.436  1.00 20.17  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 5.851   -20.896 -3.125  1.00 18.70  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.129   -21.378 -2.445  1.00 21.43  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 7.830   -22.255 -2.984  1.00 23.00  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 4.849   -22.050 -3.307  1.00 22.36  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.479   -21.536 -3.737  1.00 22.00  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.178   -21.330 -5.089  1.00 25.83  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.507   -21.259 -2.780  1.00 24.01  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 1.930   -20.814 -5.467  1.00 25.95  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.263   -20.754 -3.154  1.00 24.31  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 0.983   -20.541 -4.495  1.00 24.74  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.416   -20.847 -1.257  1.00 19.88  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 8.599   -21.323 -0.552  1.00 21.75  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.371   -22.766 -0.076  1.00 23.43  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.234   -23.221 0.109   1.00 23.80  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 8.907   -20.466 0.687   1.00 22.97  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.338   -19.062 0.317   1.00 19.64  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 10.596  -18.828 -0.276  1.00 20.48  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 8.577   -17.936 0.616   1.00 21.04  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 10.977  -17.539 -0.640  1.00 19.90  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 8.987   -16.649 0.246   1.00 20.30  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.229  -16.433 -0.358  1.00 22.90  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 9.470   -23.489 0.128   1.00 22.89  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.344   -24.853 0.630   1.00 22.74  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.121   -25.863 -0.502  1.00 30.54  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.009  -26.686 -0.768  1.00 30.49  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 7.974   -25.767 -1.200  1.00 27.82  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 7.727   -26.596 -2.379  1.00 29.13  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 8.549   -26.142 -3.584  1.00 30.15  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 8.886   -26.936 -4.483  1.00 29.57  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.238   -26.631 -2.719  1.00 30.00  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 5.871   -25.301 -3.081  1.00 29.13  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.360   -27.151 -1.602  1.00 34.29  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 8.849   -24.836 -3.636  1.00 25.20  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 9.525   -24.213 -4.754  1.00 25.52  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 8.736   -24.339 -6.061  1.00 27.60  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.342   -24.290 -7.132  1.00 31.16  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 10.969  -24.731 -4.893  1.00 27.77  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 11.669  -24.765 -3.569  1.00 30.94  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 12.479  -25.812 -3.209  1.00 28.50  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 11.713  -23.880 -2.529  1.00 28.08  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 12.966  -25.603 -1.982  1.00 36.94  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 12.561  -24.408 -1.565  1.00 28.69  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.399   -24.444 -5.963  1.00 29.14  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.509   -24.462 -7.121  1.00 29.57  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.088   -23.035 -7.493  1.00 25.80  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.205   -22.134 -6.669  1.00 24.98  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.265   -25.264 -6.736  1.00 34.12  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 5.516   -26.766 -6.605  1.00 46.76  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 4.329   -27.525 -6.044  1.00 53.86  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 3.187   -26.997 -5.999  1.00 59.39  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 4.587   -28.668 -5.605  1.00 63.48  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 5.716   -22.812 -8.762  1.00 24.63  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.185   -21.537 -9.214  1.00 24.41  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 3.732   -21.734 -9.637  1.00 26.03  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.422   -22.725 -10.298 1.00 30.51  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 5.995   -20.950 -10.376 1.00 29.36  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.308   -20.627 -9.921  1.00 27.05  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.338   -19.741 -11.026 1.00 29.61  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 2.857   -20.796 -9.258  1.00 23.20  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.535   -20.682 -9.862  1.00 23.91  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.215   -19.219 -10.161 1.00 26.24  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 1.894   -18.308 -9.683  1.00 24.60  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.489   -21.260 -8.945  1.00 25.00  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.148   -19.001 -10.948 1.00 22.34  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? -0.196  -17.657 -11.331 1.00 24.66  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.435  -17.282 -10.546 1.00 26.97  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.472  -17.958 -10.641 1.00 30.82  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.481  -17.607 -12.834 1.00 26.83  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 0.718   -17.980 -13.687 1.00 28.58  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 1.938   -17.326 -13.546 1.00 30.74  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.586   -18.919 -14.713 1.00 35.27  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.027   -17.660 -14.338 1.00 42.69  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 1.681   -19.229 -15.511 1.00 35.39  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 2.894   -18.628 -15.310 1.00 36.11  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.314  -16.192 -9.785  1.00 22.40  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.423  -15.813 -8.925  1.00 22.67  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.713  -14.324 -9.045  1.00 23.25  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.833  -13.512 -9.329  1.00 22.78  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -2.131  -16.137 -7.454  1.00 23.98  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -2.028  -17.616 -7.113  1.00 23.50  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.720  -17.643 -5.624  1.00 25.15  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.453  -18.187 -7.380  1.00 28.73  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.985  -13.974 -8.762  1.00 20.30  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -4.333  -12.565 -8.651  1.00 21.75  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.353  -12.082 -7.187  1.00 18.27  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.297  -12.892 -6.257  1.00 19.64  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.415  -10.755 -7.000  1.00 18.67  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.334  -10.111 -5.689  1.00 19.35  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.327  -10.633 -4.665  1.00 20.63  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -5.066  -10.646 -3.475  1.00 20.79  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.513  -8.651  -5.991  1.00 23.81  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.927  -8.516  -7.393  1.00 22.03  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.449  -9.760  -8.083  1.00 21.76  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.485  -11.100 -5.151  1.00 21.41  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.435  -11.645 -4.176  1.00 21.62  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.926  -12.835 -3.353  1.00 21.33  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.382  -13.062 -2.222  1.00 21.17  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.729  -12.076 -4.884  1.00 26.40  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.605  -13.390 -5.642  1.00 26.15  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.945  -13.669 -6.351  1.00 36.16  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.788  -14.833 -7.267  1.00 34.86  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.722  -16.057 -6.463  1.00 39.57  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.832  -13.510 -3.809  1.00 19.83  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.305  -14.650 -3.120  1.00 20.50  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.936  -14.308 -2.516  1.00 18.56  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -3.285  -15.238 -2.084  1.00 21.23  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -5.225  -15.820 -4.098  1.00 22.99  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.612  -16.373 -4.419  1.00 26.94  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.398  -16.476 -3.461  1.00 29.85  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.877  -16.681 -5.599  1.00 29.22  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.585  -13.009 -2.425  1.00 18.05  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -2.230  -12.598 -1.983  1.00 17.94  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.369  -11.747 -0.724  1.00 16.98  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.966  -10.663 -0.747  1.00 20.28  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.477  -11.844 -3.085  1.00 18.27  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.343  -12.607 -4.400  1.00 20.10  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.634  -11.736 -5.437  1.00 19.54  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.591  -13.945 -4.209  1.00 19.14  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.857  -12.274 0.386   1.00 17.26  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.920  -11.585 1.683   1.00 17.13  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.543  -11.111 2.127   1.00 19.39  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.365   -11.914 2.315   1.00 23.22  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -2.402  -12.603 2.712   1.00 19.88  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.841  -13.032 2.441   1.00 19.46  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -4.139  -13.937 1.416   1.00 21.34  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.889  -12.502 3.200   1.00 23.43  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.464  -14.333 1.143   1.00 25.43  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -6.194  -12.883 2.888   1.00 20.73  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.489  -13.807 1.914   1.00 22.53  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? -0.285  -9.799  2.165   1.00 22.38  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.049   -9.312  2.523   1.00 19.98  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.588   -9.925  3.800   1.00 19.69  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 0.892   -10.046 4.806   1.00 21.85  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 0.846   -7.781  2.610   1.00 22.99  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? -0.227  -7.507  1.511   1.00 25.55  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -1.180  -8.708  1.731   1.00 26.11  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 2.880   -10.337 3.756   1.00 21.35  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.484   -11.182 4.787   1.00 20.26  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.515   -10.485 6.148   1.00 21.90  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.104   -11.125 7.114   1.00 25.58  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 4.930   -11.531 4.340   1.00 20.96  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.678   -12.335 5.409   1.00 22.21  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.345   -13.653 5.645   1.00 24.73  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.719   -11.759 6.130   1.00 28.97  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 5.993   -14.420 6.601   1.00 28.50  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.401   -12.521 7.074   1.00 26.12  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.033   -13.834 7.302   1.00 29.20  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 7.646   -14.628 8.236   1.00 31.72  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 3.922   -9.207  6.191   1.00 23.52  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.069   -8.523  7.485   1.00 28.01  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 2.731   -8.442  8.236   1.00 27.46  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.658   -8.802  9.410   1.00 32.33  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 4.810   -7.211  7.322   1.00 31.58  ? 62  ASP A CB  1 
ATOM   495  C CG  . ASP A 1 63 ? 6.326   -7.320  7.163   1.00 47.69  ? 62  ASP A CG  1 
ATOM   496  O OD1 . ASP A 1 63 ? 6.921   -8.294  7.691   1.00 56.92  ? 62  ASP A OD1 1 
ATOM   497  O OD2 . ASP A 1 63 ? 6.913   -6.414  6.521   1.00 63.45  ? 62  ASP A OD2 1 
ATOM   498  N N   . LYS A 1 64 ? 1.657   -8.065  7.526   1.00 28.28  ? 63  LYS A N   1 
ATOM   499  C CA  . LYS A 1 64 ? 0.328   -7.997  8.140   1.00 29.88  ? 63  LYS A CA  1 
ATOM   500  C C   . LYS A 1 64 ? -0.208  -9.372  8.546   1.00 28.76  ? 63  LYS A C   1 
ATOM   501  O O   . LYS A 1 64 ? -0.953  -9.503  9.547   1.00 29.29  ? 63  LYS A O   1 
ATOM   502  C CB  . LYS A 1 64 ? -0.605  -7.329  7.118   1.00 27.98  ? 63  LYS A CB  1 
ATOM   503  C CG  . LYS A 1 64 ? -2.059  -7.202  7.590   1.00 30.78  ? 63  LYS A CG  1 
ATOM   504  C CD  . LYS A 1 64 ? -2.893  -6.473  6.548   1.00 32.70  ? 63  LYS A CD  1 
ATOM   505  C CE  . LYS A 1 64 ? -4.136  -5.793  7.036   1.00 33.50  ? 63  LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 64 ? -4.955  -6.533  7.987   1.00 40.38  ? 63  LYS A NZ  1 
ATOM   507  N N   . SER A 1 65 ? 0.116   -10.421 7.769   1.00 25.06  ? 64  SER A N   1 
ATOM   508  C CA  . SER A 1 65 ? -0.527  -11.726 7.877   1.00 25.25  ? 64  SER A CA  1 
ATOM   509  C C   . SER A 1 65 ? 0.218   -12.779 8.701   1.00 25.01  ? 64  SER A C   1 
ATOM   510  O O   . SER A 1 65 ? -0.339  -13.849 8.942   1.00 26.19  ? 64  SER A O   1 
ATOM   511  C CB  . SER A 1 65 ? -0.771  -12.287 6.486   1.00 27.09  ? 64  SER A CB  1 
ATOM   512  O OG  . SER A 1 65 ? -1.826  -11.497 5.982   1.00 39.15  ? 64  SER A OG  1 
ATOM   513  N N   . LYS A 1 66 ? 1.475   -12.510 9.088   1.00 27.05  ? 65  LYS A N   1 
ATOM   514  C CA  . LYS A 1 66 ? 2.304   -13.606 9.585   1.00 30.73  ? 65  LYS A CA  1 
ATOM   515  C C   . LYS A 1 66 ? 1.863   -14.112 10.963  1.00 29.20  ? 65  LYS A C   1 
ATOM   516  O O   . LYS A 1 66 ? 2.032   -15.285 11.270  1.00 29.74  ? 65  LYS A O   1 
ATOM   517  C CB  . LYS A 1 66 ? 3.796   -13.261 9.603   1.00 30.31  ? 65  LYS A CB  1 
ATOM   518  C CG  . LYS A 1 66 ? 4.170   -12.000 10.352  1.00 34.42  ? 65  LYS A CG  1 
ATOM   519  C CD  . LYS A 1 66 ? 5.694   -11.993 10.418  1.00 47.61  ? 65  LYS A CD  1 
ATOM   520  C CE  . LYS A 1 66 ? 6.237   -10.724 11.030  1.00 59.94  ? 65  LYS A CE  1 
ATOM   521  N NZ  . LYS A 1 66 ? 6.109   -9.546  10.162  1.00 62.01  ? 65  LYS A NZ  1 
ATOM   522  N N   A ASP A 1 67 ? 1.273   -13.235 11.785  0.50 32.64  ? 66  ASP A N   1 
ATOM   523  N N   B ASP A 1 67 ? 1.316   -13.229 11.804  0.50 31.79  ? 66  ASP A N   1 
ATOM   524  C CA  A ASP A 1 67 ? 0.822   -13.648 13.110  0.50 34.30  ? 66  ASP A CA  1 
ATOM   525  C CA  B ASP A 1 67 ? 0.826   -13.701 13.092  0.50 32.45  ? 66  ASP A CA  1 
ATOM   526  C C   A ASP A 1 67 ? -0.351  -14.630 12.995  0.50 34.04  ? 66  ASP A C   1 
ATOM   527  C C   B ASP A 1 67 ? -0.191  -14.815 12.858  0.50 32.88  ? 66  ASP A C   1 
ATOM   528  O O   A ASP A 1 67 ? -0.595  -15.433 13.883  0.50 34.89  ? 66  ASP A O   1 
ATOM   529  O O   B ASP A 1 67 ? -0.135  -15.867 13.493  0.50 29.78  ? 66  ASP A O   1 
ATOM   530  C CB  A ASP A 1 67 ? 0.594   -12.447 14.022  0.50 35.36  ? 66  ASP A CB  1 
ATOM   531  C CB  B ASP A 1 67 ? 0.203   -12.581 13.909  0.50 33.08  ? 66  ASP A CB  1 
ATOM   532  C CG  A ASP A 1 67 ? 1.851   -11.745 14.534  0.50 40.95  ? 66  ASP A CG  1 
ATOM   533  C CG  B ASP A 1 67 ? -0.142  -12.949 15.344  0.50 38.32  ? 66  ASP A CG  1 
ATOM   534  O OD1 A ASP A 1 67 ? 2.945   -12.344 14.457  0.50 38.77  ? 66  ASP A OD1 1 
ATOM   535  O OD1 B ASP A 1 67 ? 0.792   -13.014 16.174  0.50 41.54  ? 66  ASP A OD1 1 
ATOM   536  O OD2 A ASP A 1 67 ? 1.737   -10.589 15.001  0.50 43.15  ? 66  ASP A OD2 1 
ATOM   537  O OD2 B ASP A 1 67 ? -1.339  -13.188 15.612  0.50 43.31  ? 66  ASP A OD2 1 
ATOM   538  N N   . LYS A 1 68 ? -1.069  -14.599 11.870  1.00 29.70  ? 67  LYS A N   1 
ATOM   539  C CA  . LYS A 1 68 ? -2.183  -15.500 11.649  1.00 29.89  ? 67  LYS A CA  1 
ATOM   540  C C   . LYS A 1 68 ? -1.744  -16.765 10.927  1.00 32.59  ? 67  LYS A C   1 
ATOM   541  O O   . LYS A 1 68 ? -2.193  -17.856 11.250  1.00 30.31  ? 67  LYS A O   1 
ATOM   542  C CB  . LYS A 1 68 ? -3.243  -14.759 10.832  1.00 31.69  ? 67  LYS A CB  1 
ATOM   543  C CG  . LYS A 1 68 ? -4.504  -15.527 10.633  1.00 35.65  ? 67  LYS A CG  1 
ATOM   544  C CD  . LYS A 1 68 ? -5.497  -14.520 10.042  1.00 42.81  ? 67  LYS A CD  1 
ATOM   545  C CE  . LYS A 1 68 ? -6.795  -15.169 9.717   1.00 52.62  ? 67  LYS A CE  1 
ATOM   546  N NZ  . LYS A 1 68 ? -7.768  -14.172 9.258   1.00 55.44  ? 67  LYS A NZ  1 
ATOM   547  N N   . TYR A 1 69 ? -0.876  -16.625 9.913   1.00 28.14  ? 68  TYR A N   1 
ATOM   548  C CA  . TYR A 1 69 ? -0.720  -17.740 8.992   1.00 26.18  ? 68  TYR A CA  1 
ATOM   549  C C   . TYR A 1 69 ? 0.670   -18.373 9.122   1.00 25.90  ? 68  TYR A C   1 
ATOM   550  O O   . TYR A 1 69 ? 0.864   -19.464 8.580   1.00 27.17  ? 68  TYR A O   1 
ATOM   551  C CB  . TYR A 1 69 ? -0.908  -17.306 7.526   1.00 23.33  ? 68  TYR A CB  1 
ATOM   552  C CG  . TYR A 1 69 ? -2.312  -16.849 7.145   1.00 26.72  ? 68  TYR A CG  1 
ATOM   553  C CD1 . TYR A 1 69 ? -3.448  -17.602 7.464   1.00 28.62  ? 68  TYR A CD1 1 
ATOM   554  C CD2 . TYR A 1 69 ? -2.487  -15.667 6.424   1.00 25.82  ? 68  TYR A CD2 1 
ATOM   555  C CE1 . TYR A 1 69 ? -4.722  -17.166 7.115   1.00 29.24  ? 68  TYR A CE1 1 
ATOM   556  C CE2 . TYR A 1 69 ? -3.757  -15.236 6.038   1.00 28.26  ? 68  TYR A CE2 1 
ATOM   557  C CZ  . TYR A 1 69 ? -4.869  -15.979 6.403   1.00 28.42  ? 68  TYR A CZ  1 
ATOM   558  O OH  . TYR A 1 69 ? -6.087  -15.526 5.986   1.00 30.74  ? 68  TYR A OH  1 
ATOM   559  N N   . GLY A 1 70 ? 1.565   -17.732 9.878   1.00 25.06  ? 69  GLY A N   1 
ATOM   560  C CA  . GLY A 1 70 ? 2.972   -18.137 9.970   1.00 26.35  ? 69  GLY A CA  1 
ATOM   561  C C   . GLY A 1 70 ? 3.164   -19.086 11.155  1.00 27.06  ? 69  GLY A C   1 
ATOM   562  O O   . GLY A 1 70 ? 3.746   -18.710 12.150  1.00 33.31  ? 69  GLY A O   1 
ATOM   563  N N   . LYS A 1 71 ? 2.589   -20.270 11.033  1.00 32.34  ? 70  LYS A N   1 
ATOM   564  C CA  . LYS A 1 71 ? 2.548   -21.256 12.105  1.00 34.41  ? 70  LYS A CA  1 
ATOM   565  C C   . LYS A 1 71 ? 2.774   -22.604 11.441  1.00 30.89  ? 70  LYS A C   1 
ATOM   566  O O   . LYS A 1 71 ? 2.355   -22.830 10.318  1.00 30.25  ? 70  LYS A O   1 
ATOM   567  C CB  . LYS A 1 71 ? 1.205   -21.296 12.851  1.00 33.38  ? 70  LYS A CB  1 
ATOM   568  C CG  . LYS A 1 71 ? 0.946   -20.074 13.734  1.00 38.63  ? 70  LYS A CG  1 
ATOM   569  C CD  . LYS A 1 71 ? 0.264   -20.361 15.069  1.00 50.38  ? 70  LYS A CD  1 
ATOM   570  N N   . PRO A 1 72 ? 3.468   -23.569 12.094  1.00 31.37  ? 71  PRO A N   1 
ATOM   571  C CA  . PRO A 1 72 ? 3.747   -24.845 11.430  1.00 30.71  ? 71  PRO A CA  1 
ATOM   572  C C   . PRO A 1 72 ? 2.527   -25.592 10.911  1.00 32.48  ? 71  PRO A C   1 
ATOM   573  O O   . PRO A 1 72 ? 1.452   -25.496 11.513  1.00 36.23  ? 71  PRO A O   1 
ATOM   574  C CB  . PRO A 1 72 ? 4.513   -25.607 12.536  1.00 32.24  ? 71  PRO A CB  1 
ATOM   575  C CG  . PRO A 1 72 ? 5.114   -24.518 13.348  1.00 35.26  ? 71  PRO A CG  1 
ATOM   576  C CD  . PRO A 1 72 ? 4.023   -23.458 13.446  1.00 34.59  ? 71  PRO A CD  1 
ATOM   577  N N   . ASN A 1 73 ? 2.712   -26.312 9.808   1.00 32.79  ? 72  ASN A N   1 
ATOM   578  C CA  . ASN A 1 73 ? 1.657   -27.051 9.144   1.00 41.72  ? 72  ASN A CA  1 
ATOM   579  C C   . ASN A 1 73 ? 2.211   -28.398 8.691   1.00 43.71  ? 72  ASN A C   1 
ATOM   580  O O   . ASN A 1 73 ? 3.389   -28.530 8.372   1.00 45.49  ? 72  ASN A O   1 
ATOM   581  C CB  . ASN A 1 73 ? 1.020   -26.179 8.057   1.00 44.25  ? 72  ASN A CB  1 
ATOM   582  C CG  . ASN A 1 73 ? -0.313  -26.684 7.567   1.00 45.23  ? 72  ASN A CG  1 
ATOM   583  O OD1 . ASN A 1 73 ? -0.354  -27.615 6.760   1.00 47.63  ? 72  ASN A OD1 1 
ATOM   584  N ND2 . ASN A 1 73 ? -1.400  -26.026 7.952   1.00 46.60  ? 72  ASN A ND2 1 
ATOM   585  N N   . LYS A 1 74 ? 1.332   -29.407 8.676   1.00 50.31  ? 73  LYS A N   1 
ATOM   586  C CA  . LYS A 1 74 ? 1.710   -30.780 8.400   1.00 44.99  ? 73  LYS A CA  1 
ATOM   587  C C   . LYS A 1 74 ? 2.094   -30.950 6.933   1.00 47.67  ? 73  LYS A C   1 
ATOM   588  O O   . LYS A 1 74 ? 2.860   -31.858 6.597   1.00 45.67  ? 73  LYS A O   1 
ATOM   589  C CB  . LYS A 1 74 ? 0.545   -31.693 8.812   1.00 52.30  ? 73  LYS A CB  1 
ATOM   590  C CG  . LYS A 1 74 ? -0.650  -31.725 7.854   1.00 48.56  ? 73  LYS A CG  1 
ATOM   591  N N   . ARG A 1 75 ? 1.579   -30.060 6.065   1.00 39.71  ? 74  ARG A N   1 
ATOM   592  C CA  . ARG A 1 75 ? 1.682   -30.230 4.621   1.00 40.03  ? 74  ARG A CA  1 
ATOM   593  C C   . ARG A 1 75 ? 3.146   -30.201 4.173   1.00 37.32  ? 74  ARG A C   1 
ATOM   594  O O   . ARG A 1 75 ? 3.959   -29.439 4.720   1.00 36.18  ? 74  ARG A O   1 
ATOM   595  C CB  . ARG A 1 75 ? 0.822   -29.174 3.910   1.00 41.44  ? 74  ARG A CB  1 
ATOM   596  C CG  . ARG A 1 75 ? -0.648  -29.334 4.258   1.00 46.33  ? 74  ARG A CG  1 
ATOM   597  C CD  . ARG A 1 75 ? -1.232  -30.475 3.448   1.00 46.97  ? 74  ARG A CD  1 
ATOM   598  N NE  . ARG A 1 75 ? -2.126  -30.036 2.369   1.00 60.99  ? 74  ARG A NE  1 
ATOM   599  C CZ  . ARG A 1 75 ? -3.321  -29.447 2.530   1.00 59.84  ? 74  ARG A CZ  1 
ATOM   600  N NH1 . ARG A 1 75 ? -4.087  -29.246 1.474   1.00 55.96  ? 74  ARG A NH1 1 
ATOM   601  N NH2 . ARG A 1 75 ? -3.774  -29.120 3.736   1.00 63.81  ? 74  ARG A NH2 1 
ATOM   602  N N   . LYS A 1 76 ? 3.454   -31.040 3.176   1.00 36.40  ? 75  LYS A N   1 
ATOM   603  C CA  . LYS A 1 76 ? 4.813   -31.220 2.677   1.00 38.34  ? 75  LYS A CA  1 
ATOM   604  C C   . LYS A 1 76 ? 5.389   -29.868 2.260   1.00 32.42  ? 75  LYS A C   1 
ATOM   605  O O   . LYS A 1 76 ? 4.802   -29.172 1.433   1.00 31.83  ? 75  LYS A O   1 
ATOM   606  C CB  . LYS A 1 76 ? 4.851   -32.131 1.442   1.00 39.88  ? 75  LYS A CB  1 
ATOM   607  C CG  . LYS A 1 76 ? 6.205   -32.458 0.817   1.00 43.93  ? 75  LYS A CG  1 
ATOM   608  C CD  . LYS A 1 76 ? 6.166   -33.662 -0.125  1.00 47.95  ? 75  LYS A CD  1 
ATOM   609  C CE  . LYS A 1 76 ? 7.474   -33.990 -0.782  1.00 52.26  ? 75  LYS A CE  1 
ATOM   610  N N   . GLY A 1 77 ? 6.557   -29.515 2.813   1.00 33.61  ? 76  GLY A N   1 
ATOM   611  C CA  . GLY A 1 77 ? 7.217   -28.323 2.318   1.00 29.10  ? 76  GLY A CA  1 
ATOM   612  C C   . GLY A 1 77 ? 6.851   -27.064 3.101   1.00 28.56  ? 76  GLY A C   1 
ATOM   613  O O   . GLY A 1 77 ? 7.588   -26.077 3.023   1.00 26.66  ? 76  GLY A O   1 
ATOM   614  N N   . PHE A 1 78 ? 5.746   -27.094 3.852   1.00 24.61  ? 77  PHE A N   1 
ATOM   615  C CA  . PHE A 1 78 ? 5.296   -25.883 4.528   1.00 27.80  ? 77  PHE A CA  1 
ATOM   616  C C   . PHE A 1 78 ? 6.339   -25.303 5.491   1.00 29.35  ? 77  PHE A C   1 
ATOM   617  O O   . PHE A 1 78 ? 6.536   -24.087 5.564   1.00 25.29  ? 77  PHE A O   1 
ATOM   618  C CB  . PHE A 1 78 ? 3.977   -26.157 5.249   1.00 28.33  ? 77  PHE A CB  1 
ATOM   619  C CG  . PHE A 1 78 ? 3.215   -24.881 5.580   1.00 27.35  ? 77  PHE A CG  1 
ATOM   620  C CD1 . PHE A 1 78 ? 3.470   -24.185 6.757   1.00 25.83  ? 77  PHE A CD1 1 
ATOM   621  C CD2 . PHE A 1 78 ? 2.280   -24.373 4.674   1.00 26.52  ? 77  PHE A CD2 1 
ATOM   622  C CE1 . PHE A 1 78 ? 2.801   -23.003 7.055   1.00 30.84  ? 77  PHE A CE1 1 
ATOM   623  C CE2 . PHE A 1 78 ? 1.624   -23.193 4.967   1.00 23.27  ? 77  PHE A CE2 1 
ATOM   624  C CZ  . PHE A 1 78 ? 1.879   -22.511 6.149   1.00 25.20  ? 77  PHE A CZ  1 
ATOM   625  N N   . ASN A 1 79 ? 6.907   -26.134 6.367   1.00 26.43  ? 78  ASN A N   1 
ATOM   626  C CA  . ASN A 1 79 ? 7.709   -25.587 7.453   1.00 24.10  ? 78  ASN A CA  1 
ATOM   627  C C   . ASN A 1 79 ? 9.080   -25.160 6.901   1.00 25.43  ? 78  ASN A C   1 
ATOM   628  O O   . ASN A 1 79 ? 9.685   -24.183 7.387   1.00 24.90  ? 78  ASN A O   1 
ATOM   629  C CB  . ASN A 1 79 ? 7.860   -26.630 8.559   1.00 28.38  ? 78  ASN A CB  1 
ATOM   630  C CG  . ASN A 1 79 ? 6.527   -26.966 9.193   1.00 35.23  ? 78  ASN A CG  1 
ATOM   631  O OD1 . ASN A 1 79 ? 5.602   -26.145 9.196   1.00 31.29  ? 78  ASN A OD1 1 
ATOM   632  N ND2 . ASN A 1 79 ? 6.423   -28.155 9.782   1.00 31.55  ? 78  ASN A ND2 1 
ATOM   633  N N   . GLU A 1 80 ? 9.550   -25.875 5.871   1.00 25.53  ? 79  GLU A N   1 
ATOM   634  C CA  . GLU A 1 80 ? 10.702  -25.404 5.115   1.00 26.42  ? 79  GLU A CA  1 
ATOM   635  C C   . GLU A 1 80 ? 10.400  -24.025 4.542   1.00 23.70  ? 79  GLU A C   1 
ATOM   636  O O   . GLU A 1 80 ? 11.253  -23.116 4.576   1.00 22.78  ? 79  GLU A O   1 
ATOM   637  C CB  . GLU A 1 80 ? 11.058  -26.311 3.939   1.00 26.17  ? 79  GLU A CB  1 
ATOM   638  C CG  . GLU A 1 80 ? 12.382  -25.936 3.258   1.00 26.74  ? 79  GLU A CG  1 
ATOM   639  C CD  . GLU A 1 80 ? 12.874  -26.917 2.199   1.00 40.26  ? 79  GLU A CD  1 
ATOM   640  O OE1 . GLU A 1 80 ? 12.209  -27.950 1.971   1.00 47.46  ? 79  GLU A OE1 1 
ATOM   641  O OE2 . GLU A 1 80 ? 13.944  -26.658 1.625   1.00 40.98  ? 79  GLU A OE2 1 
ATOM   642  N N   . GLY A 1 81 ? 9.168   -23.888 4.032   1.00 24.32  ? 80  GLY A N   1 
ATOM   643  C CA  . GLY A 1 81 ? 8.756   -22.599 3.472   1.00 22.47  ? 80  GLY A CA  1 
ATOM   644  C C   . GLY A 1 81 ? 8.737   -21.478 4.524   1.00 21.19  ? 80  GLY A C   1 
ATOM   645  O O   . GLY A 1 81 ? 9.115   -20.331 4.239   1.00 20.95  ? 80  GLY A O   1 
ATOM   646  N N   . LEU A 1 82 ? 8.312   -21.778 5.759   1.00 20.18  ? 81  LEU A N   1 
ATOM   647  C CA  . LEU A 1 82 ? 8.354   -20.748 6.784   1.00 23.51  ? 81  LEU A CA  1 
ATOM   648  C C   . LEU A 1 82 ? 9.801   -20.310 7.059   1.00 22.80  ? 81  LEU A C   1 
ATOM   649  O O   . LEU A 1 82 ? 10.066  -19.143 7.340   1.00 23.30  ? 81  LEU A O   1 
ATOM   650  C CB  . LEU A 1 82 ? 7.713   -21.246 8.078   1.00 22.94  ? 81  LEU A CB  1 
ATOM   651  C CG  . LEU A 1 82 ? 6.199   -21.505 8.001   1.00 24.25  ? 81  LEU A CG  1 
ATOM   652  C CD1 . LEU A 1 82 ? 5.788   -22.118 9.335   1.00 27.18  ? 81  LEU A CD1 1 
ATOM   653  C CD2 . LEU A 1 82 ? 5.398   -20.246 7.780   1.00 25.77  ? 81  LEU A CD2 1 
ATOM   654  N N   . TRP A 1 83 ? 10.739  -21.263 7.036   1.00 22.74  ? 82  TRP A N   1 
ATOM   655  C CA  . TRP A 1 83 ? 12.123  -20.899 7.281   1.00 22.77  ? 82  TRP A CA  1 
ATOM   656  C C   . TRP A 1 83 ? 12.613  -19.960 6.186   1.00 22.12  ? 82  TRP A C   1 
ATOM   657  O O   . TRP A 1 83 ? 13.209  -18.921 6.457   1.00 22.87  ? 82  TRP A O   1 
ATOM   658  C CB  . TRP A 1 83 ? 13.034  -22.137 7.417   1.00 22.86  ? 82  TRP A CB  1 
ATOM   659  C CG  . TRP A 1 83 ? 14.473  -21.736 7.651   1.00 23.54  ? 82  TRP A CG  1 
ATOM   660  C CD1 . TRP A 1 83 ? 15.078  -21.573 8.867   1.00 25.03  ? 82  TRP A CD1 1 
ATOM   661  C CD2 . TRP A 1 83 ? 15.462  -21.430 6.653   1.00 24.46  ? 82  TRP A CD2 1 
ATOM   662  N NE1 . TRP A 1 83 ? 16.370  -21.182 8.693   1.00 24.54  ? 82  TRP A NE1 1 
ATOM   663  C CE2 . TRP A 1 83 ? 16.624  -21.048 7.344   1.00 24.12  ? 82  TRP A CE2 1 
ATOM   664  C CE3 . TRP A 1 83 ? 15.454  -21.376 5.254   1.00 24.83  ? 82  TRP A CE3 1 
ATOM   665  C CZ2 . TRP A 1 83 ? 17.796  -20.658 6.679   1.00 24.60  ? 82  TRP A CZ2 1 
ATOM   666  C CZ3 . TRP A 1 83 ? 16.591  -20.968 4.593   1.00 26.20  ? 82  TRP A CZ3 1 
ATOM   667  C CH2 . TRP A 1 83 ? 17.757  -20.620 5.299   1.00 28.12  ? 82  TRP A CH2 1 
ATOM   668  N N   . GLU A 1 84 ? 12.259  -20.294 4.952   1.00 20.69  ? 83  GLU A N   1 
ATOM   669  C CA  . GLU A 1 84 ? 12.775  -19.547 3.813   1.00 18.67  ? 83  GLU A CA  1 
ATOM   670  C C   . GLU A 1 84 ? 12.272  -18.107 3.830   1.00 21.36  ? 83  GLU A C   1 
ATOM   671  O O   . GLU A 1 84 ? 13.019  -17.157 3.611   1.00 20.92  ? 83  GLU A O   1 
ATOM   672  C CB  . GLU A 1 84 ? 12.402  -20.176 2.478   1.00 20.25  ? 83  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 84 ? 13.074  -21.546 2.333   1.00 20.87  ? 83  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 84 ? 12.702  -22.294 1.076   1.00 23.89  ? 83  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 84 ? 11.768  -21.878 0.343   1.00 24.83  ? 83  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 84 ? 13.310  -23.380 0.823   1.00 24.69  ? 83  GLU A OE2 1 
ATOM   677  N N   . ILE A 1 85 ? 10.974  -17.933 4.082   1.00 18.95  ? 84  ILE A N   1 
ATOM   678  C CA  . ILE A 1 85 ? 10.430  -16.596 3.974   1.00 19.41  ? 84  ILE A CA  1 
ATOM   679  C C   . ILE A 1 85 ? 10.983  -15.712 5.098   1.00 21.78  ? 84  ILE A C   1 
ATOM   680  O O   . ILE A 1 85 ? 11.158  -14.513 4.903   1.00 20.84  ? 84  ILE A O   1 
ATOM   681  C CB  . ILE A 1 85 ? 8.884   -16.652 3.976   1.00 19.15  ? 84  ILE A CB  1 
ATOM   682  C CG1 . ILE A 1 85 ? 8.306   -15.271 3.500   1.00 18.76  ? 84  ILE A CG1 1 
ATOM   683  C CG2 . ILE A 1 85 ? 8.331   -17.045 5.368   1.00 20.78  ? 84  ILE A CG2 1 
ATOM   684  C CD1 . ILE A 1 85 ? 6.847   -15.342 3.041   1.00 18.22  ? 84  ILE A CD1 1 
ATOM   685  N N   . GLN A 1 86 ? 11.259  -16.317 6.276   1.00 20.68  ? 85  GLN A N   1 
ATOM   686  C CA  . GLN A 1 86 ? 11.778  -15.550 7.405   1.00 22.84  ? 85  GLN A CA  1 
ATOM   687  C C   . GLN A 1 86 ? 13.275  -15.258 7.256   1.00 23.43  ? 85  GLN A C   1 
ATOM   688  O O   . GLN A 1 86 ? 13.726  -14.178 7.673   1.00 25.53  ? 85  GLN A O   1 
ATOM   689  C CB  . GLN A 1 86 ? 11.433  -16.291 8.702   1.00 24.72  ? 85  GLN A CB  1 
ATOM   690  C CG  . GLN A 1 86 ? 11.788  -15.493 9.951   1.00 31.87  ? 85  GLN A CG  1 
ATOM   691  C CD  . GLN A 1 86 ? 11.181  -16.048 11.227  1.00 37.99  ? 85  GLN A CD  1 
ATOM   692  O OE1 . GLN A 1 86 ? 10.819  -17.239 11.328  1.00 34.66  ? 85  GLN A OE1 1 
ATOM   693  N NE2 . GLN A 1 86 ? 11.079  -15.161 12.210  1.00 36.53  ? 85  GLN A NE2 1 
ATOM   694  N N   . ASN A 1 87 ? 14.015  -16.238 6.728   1.00 20.85  ? 86  ASN A N   1 
ATOM   695  C CA  . ASN A 1 87 ? 15.480  -16.259 6.825   1.00 21.80  ? 86  ASN A CA  1 
ATOM   696  C C   . ASN A 1 87 ? 16.211  -15.928 5.527   1.00 22.71  ? 86  ASN A C   1 
ATOM   697  O O   . ASN A 1 87 ? 17.328  -15.396 5.586   1.00 23.16  ? 86  ASN A O   1 
ATOM   698  C CB  . ASN A 1 87 ? 15.987  -17.516 7.525   1.00 23.02  ? 86  ASN A CB  1 
ATOM   699  C CG  . ASN A 1 87 ? 15.455  -17.566 8.941   1.00 26.11  ? 86  ASN A CG  1 
ATOM   700  O OD1 . ASN A 1 87 ? 15.802  -16.689 9.747   1.00 28.34  ? 86  ASN A OD1 1 
ATOM   701  N ND2 . ASN A 1 87 ? 14.495  -18.436 9.220   1.00 26.22  ? 86  ASN A ND2 1 
ATOM   702  N N   . ASN A 1 88 ? 15.644  -16.231 4.350   1.00 20.53  ? 87  ASN A N   1 
ATOM   703  C CA  . ASN A 1 88 ? 16.339  -15.864 3.124   1.00 18.70  ? 87  ASN A CA  1 
ATOM   704  C C   . ASN A 1 88 ? 15.316  -15.822 1.980   1.00 20.30  ? 87  ASN A C   1 
ATOM   705  O O   . ASN A 1 88 ? 15.359  -16.599 1.008   1.00 21.51  ? 87  ASN A O   1 
ATOM   706  C CB  . ASN A 1 88 ? 17.482  -16.831 2.798   1.00 22.42  ? 87  ASN A CB  1 
ATOM   707  C CG  . ASN A 1 88 ? 18.539  -16.204 1.907   1.00 22.91  ? 87  ASN A CG  1 
ATOM   708  O OD1 . ASN A 1 88 ? 18.315  -15.187 1.225   1.00 22.01  ? 87  ASN A OD1 1 
ATOM   709  N ND2 . ASN A 1 88 ? 19.738  -16.806 1.898   1.00 24.87  ? 87  ASN A ND2 1 
ATOM   710  N N   . PRO A 1 89 ? 14.378  -14.869 2.076   1.00 21.01  ? 88  PRO A N   1 
ATOM   711  C CA  . PRO A 1 89 ? 13.235  -14.856 1.156   1.00 18.76  ? 88  PRO A CA  1 
ATOM   712  C C   . PRO A 1 89 ? 13.593  -14.378 -0.243  1.00 21.35  ? 88  PRO A C   1 
ATOM   713  O O   . PRO A 1 89 ? 12.812  -14.622 -1.136  1.00 20.74  ? 88  PRO A O   1 
ATOM   714  C CB  . PRO A 1 89 ? 12.290  -13.917 1.874   1.00 19.75  ? 88  PRO A CB  1 
ATOM   715  C CG  . PRO A 1 89 ? 13.231  -12.900 2.540   1.00 20.20  ? 88  PRO A CG  1 
ATOM   716  C CD  . PRO A 1 89 ? 14.292  -13.849 3.133   1.00 20.41  ? 88  PRO A CD  1 
ATOM   717  N N   . HIS A 1 90 ? 14.823  -13.828 -0.467  1.00 17.72  ? 89  HIS A N   1 
ATOM   718  C CA  . HIS A 1 90 ? 15.114  -13.318 -1.811  1.00 18.81  ? 89  HIS A CA  1 
ATOM   719  C C   . HIS A 1 90 ? 16.246  -14.113 -2.472  1.00 20.82  ? 89  HIS A C   1 
ATOM   720  O O   . HIS A 1 90 ? 16.750  -13.702 -3.523  1.00 21.80  ? 89  HIS A O   1 
ATOM   721  C CB  . HIS A 1 90 ? 15.508  -11.831 -1.694  1.00 18.71  ? 89  HIS A CB  1 
ATOM   722  C CG  . HIS A 1 90 ? 14.442  -10.998 -1.077  1.00 18.93  ? 89  HIS A CG  1 
ATOM   723  N ND1 . HIS A 1 90 ? 13.171  -10.911 -1.652  1.00 18.62  ? 89  HIS A ND1 1 
ATOM   724  C CD2 . HIS A 1 90 ? 14.401  -10.324 0.070   1.00 19.14  ? 89  HIS A CD2 1 
ATOM   725  C CE1 . HIS A 1 90 ? 12.433  -10.090 -0.912  1.00 21.30  ? 89  HIS A CE1 1 
ATOM   726  N NE2 . HIS A 1 90 ? 13.148  -9.749  0.163   1.00 21.63  ? 89  HIS A NE2 1 
ATOM   727  N N   . ALA A 1 91 ? 16.522  -15.304 -1.926  1.00 20.19  ? 90  ALA A N   1 
ATOM   728  C CA  . ALA A 1 91 ? 17.592  -16.145 -2.479  1.00 21.75  ? 90  ALA A CA  1 
ATOM   729  C C   . ALA A 1 91 ? 17.149  -16.857 -3.754  1.00 23.88  ? 90  ALA A C   1 
ATOM   730  O O   . ALA A 1 91 ? 15.974  -16.964 -4.076  1.00 23.32  ? 90  ALA A O   1 
ATOM   731  C CB  . ALA A 1 91 ? 18.086  -17.168 -1.463  1.00 22.70  ? 90  ALA A CB  1 
ATOM   732  N N   . SER A 1 92 ? 18.132  -17.358 -4.502  1.00 23.85  ? 91  SER A N   1 
ATOM   733  C CA  . SER A 1 92 ? 17.890  -18.294 -5.587  1.00 26.22  ? 91  SER A CA  1 
ATOM   734  C C   . SER A 1 92 ? 17.620  -19.689 -5.017  1.00 27.00  ? 91  SER A C   1 
ATOM   735  O O   . SER A 1 92 ? 18.408  -20.248 -4.239  1.00 29.84  ? 91  SER A O   1 
ATOM   736  C CB  . SER A 1 92 ? 19.112  -18.286 -6.504  1.00 30.72  ? 91  SER A CB  1 
ATOM   737  O OG  . SER A 1 92 ? 18.988  -19.389 -7.370  1.00 38.35  ? 91  SER A OG  1 
ATOM   738  N N   . TYR A 1 93 ? 16.455  -20.254 -5.352  1.00 24.16  ? 92  TYR A N   1 
ATOM   739  C CA  . TYR A 1 93 ? 16.070  -21.580 -4.923  1.00 28.26  ? 92  TYR A CA  1 
ATOM   740  C C   . TYR A 1 93 ? 15.980  -22.480 -6.155  1.00 35.59  ? 92  TYR A C   1 
ATOM   741  O O   . TYR A 1 93 ? 15.400  -23.558 -6.087  1.00 42.22  ? 92  TYR A O   1 
ATOM   742  C CB  . TYR A 1 93 ? 14.687  -21.513 -4.245  1.00 26.89  ? 92  TYR A CB  1 
ATOM   743  C CG  . TYR A 1 93 ? 14.808  -20.929 -2.844  1.00 26.16  ? 92  TYR A CG  1 
ATOM   744  C CD1 . TYR A 1 93 ? 15.230  -21.711 -1.776  1.00 26.75  ? 92  TYR A CD1 1 
ATOM   745  C CD2 . TYR A 1 93 ? 14.516  -19.586 -2.612  1.00 26.63  ? 92  TYR A CD2 1 
ATOM   746  C CE1 . TYR A 1 93 ? 15.416  -21.152 -0.516  1.00 27.32  ? 92  TYR A CE1 1 
ATOM   747  C CE2 . TYR A 1 93 ? 14.630  -19.042 -1.344  1.00 24.61  ? 92  TYR A CE2 1 
ATOM   748  C CZ  . TYR A 1 93 ? 15.080  -19.822 -0.290  1.00 24.65  ? 92  TYR A CZ  1 
ATOM   749  O OH  . TYR A 1 93 ? 15.293  -19.299 0.968   1.00 27.09  ? 92  TYR A OH  1 
ATOM   750  N N   . SER A 1 94 ? 16.532  -21.994 -7.265  1.00 36.82  ? 93  SER A N   1 
ATOM   751  C CA  . SER A 1 94 ? 16.748  -22.770 -8.479  1.00 53.50  ? 93  SER A CA  1 
ATOM   752  C C   . SER A 1 94 ? 17.526  -24.045 -8.118  1.00 65.56  ? 93  SER A C   1 
ATOM   753  O O   . SER A 1 94 ? 18.755  -23.928 -7.887  1.00 70.61  ? 93  SER A O   1 
ATOM   754  C CB  . SER A 1 94 ? 17.492  -21.941 -9.520  1.00 49.90  ? 93  SER A CB  1 
ATOM   755  O OG  . SER A 1 94 ? 16.868  -20.678 -9.715  1.00 67.30  ? 93  SER A OG  1 
ATOM   756  O OXT . SER A 1 94 ? 16.870  -25.109 -8.042  1.00 80.12  ? 93  SER A OXT 1 
ATOM   757  N N   . MET B 1 2  ? 38.880  -11.246 -41.675 1.00 78.98  ? 1   MET B N   1 
ATOM   758  C CA  . MET B 1 2  ? 38.449  -12.040 -42.856 1.00 77.19  ? 1   MET B CA  1 
ATOM   759  C C   . MET B 1 2  ? 36.920  -12.123 -42.864 1.00 68.32  ? 1   MET B C   1 
ATOM   760  O O   . MET B 1 2  ? 36.305  -12.336 -41.816 1.00 65.68  ? 1   MET B O   1 
ATOM   761  C CB  . MET B 1 2  ? 39.061  -13.447 -42.806 1.00 85.90  ? 1   MET B CB  1 
ATOM   762  C CG  . MET B 1 2  ? 39.315  -14.089 -44.168 1.00 97.48  ? 1   MET B CG  1 
ATOM   763  S SD  . MET B 1 2  ? 40.652  -13.381 -45.158 1.00 92.23  ? 1   MET B SD  1 
ATOM   764  C CE  . MET B 1 2  ? 42.107  -13.557 -44.114 1.00 92.59  ? 1   MET B CE  1 
ATOM   765  N N   . PRO B 1 3  ? 36.251  -11.939 -44.031 1.00 52.38  ? 2   PRO B N   1 
ATOM   766  C CA  . PRO B 1 3  ? 34.809  -12.181 -44.120 1.00 51.83  ? 2   PRO B CA  1 
ATOM   767  C C   . PRO B 1 3  ? 34.517  -13.612 -43.663 1.00 56.47  ? 2   PRO B C   1 
ATOM   768  O O   . PRO B 1 3  ? 35.347  -14.507 -43.841 1.00 45.58  ? 2   PRO B O   1 
ATOM   769  C CB  . PRO B 1 3  ? 34.479  -11.917 -45.605 1.00 53.06  ? 2   PRO B CB  1 
ATOM   770  C CG  . PRO B 1 3  ? 35.608  -11.001 -46.081 1.00 46.67  ? 2   PRO B CG  1 
ATOM   771  C CD  . PRO B 1 3  ? 36.833  -11.462 -45.299 1.00 44.04  ? 2   PRO B CD  1 
ATOM   772  N N   . HIS B 1 4  ? 33.373  -13.788 -42.983 1.00 54.50  ? 3   HIS B N   1 
ATOM   773  C CA  . HIS B 1 4  ? 32.898  -15.103 -42.569 1.00 56.96  ? 3   HIS B CA  1 
ATOM   774  C C   . HIS B 1 4  ? 31.534  -15.358 -43.205 1.00 53.10  ? 3   HIS B C   1 
ATOM   775  O O   . HIS B 1 4  ? 30.977  -14.459 -43.843 1.00 53.13  ? 3   HIS B O   1 
ATOM   776  C CB  . HIS B 1 4  ? 32.933  -15.241 -41.045 1.00 64.65  ? 3   HIS B CB  1 
ATOM   777  C CG  . HIS B 1 4  ? 34.320  -15.450 -40.536 1.00 74.86  ? 3   HIS B CG  1 
ATOM   778  N ND1 . HIS B 1 4  ? 35.207  -16.309 -41.154 1.00 74.35  ? 3   HIS B ND1 1 
ATOM   779  C CD2 . HIS B 1 4  ? 34.968  -14.928 -39.483 1.00 71.73  ? 3   HIS B CD2 1 
ATOM   780  C CE1 . HIS B 1 4  ? 36.353  -16.298 -40.489 1.00 73.32  ? 3   HIS B CE1 1 
ATOM   781  N NE2 . HIS B 1 4  ? 36.227  -15.468 -39.472 1.00 77.71  ? 3   HIS B NE2 1 
ATOM   782  N N   . ALA B 1 5  ? 31.013  -16.588 -43.054 1.00 44.67  ? 4   ALA B N   1 
ATOM   783  C CA  . ALA B 1 5  ? 29.729  -16.909 -43.652 1.00 39.93  ? 4   ALA B CA  1 
ATOM   784  C C   . ALA B 1 5  ? 28.696  -15.898 -43.166 1.00 41.19  ? 4   ALA B C   1 
ATOM   785  O O   . ALA B 1 5  ? 27.916  -15.359 -43.952 1.00 42.55  ? 4   ALA B O   1 
ATOM   786  C CB  . ALA B 1 5  ? 29.314  -18.304 -43.269 1.00 45.43  ? 4   ALA B CB  1 
ATOM   787  N N   . PHE B 1 6  ? 28.675  -15.721 -41.845 1.00 40.81  ? 5   PHE B N   1 
ATOM   788  C CA  . PHE B 1 6  ? 27.893  -14.669 -41.215 1.00 43.13  ? 5   PHE B CA  1 
ATOM   789  C C   . PHE B 1 6  ? 28.780  -13.463 -40.905 1.00 38.63  ? 5   PHE B C   1 
ATOM   790  O O   . PHE B 1 6  ? 29.905  -13.618 -40.431 1.00 44.05  ? 5   PHE B O   1 
ATOM   791  C CB  . PHE B 1 6  ? 27.272  -15.159 -39.904 1.00 41.11  ? 5   PHE B CB  1 
ATOM   792  C CG  . PHE B 1 6  ? 26.155  -16.181 -40.055 1.00 33.88  ? 5   PHE B CG  1 
ATOM   793  C CD1 . PHE B 1 6  ? 24.840  -15.773 -40.230 1.00 34.44  ? 5   PHE B CD1 1 
ATOM   794  C CD2 . PHE B 1 6  ? 26.422  -17.550 -39.957 1.00 36.30  ? 5   PHE B CD2 1 
ATOM   795  C CE1 . PHE B 1 6  ? 23.821  -16.703 -40.325 1.00 34.54  ? 5   PHE B CE1 1 
ATOM   796  C CE2 . PHE B 1 6  ? 25.392  -18.480 -40.059 1.00 32.37  ? 5   PHE B CE2 1 
ATOM   797  C CZ  . PHE B 1 6  ? 24.100  -18.055 -40.212 1.00 32.93  ? 5   PHE B CZ  1 
ATOM   798  N N   . LYS B 1 7  ? 28.240  -12.269 -41.148 1.00 40.22  ? 6   LYS B N   1 
ATOM   799  C CA  . LYS B 1 7  ? 28.977  -11.037 -40.912 1.00 41.23  ? 6   LYS B CA  1 
ATOM   800  C C   . LYS B 1 7  ? 28.173  -10.104 -40.003 1.00 44.99  ? 6   LYS B C   1 
ATOM   801  O O   . LYS B 1 7  ? 26.932  -10.166 -39.956 1.00 39.27  ? 6   LYS B O   1 
ATOM   802  C CB  . LYS B 1 7  ? 29.229  -10.384 -42.265 1.00 44.12  ? 6   LYS B CB  1 
ATOM   803  C CG  . LYS B 1 7  ? 27.987  -9.976  -43.006 1.00 41.46  ? 6   LYS B CG  1 
ATOM   804  C CD  . LYS B 1 7  ? 28.368  -9.686  -44.454 1.00 51.73  ? 6   LYS B CD  1 
ATOM   805  C CE  . LYS B 1 7  ? 27.326  -8.903  -45.183 1.00 50.62  ? 6   LYS B CE  1 
ATOM   806  N NZ  . LYS B 1 7  ? 26.066  -9.647  -45.279 1.00 56.66  ? 6   LYS B NZ  1 
ATOM   807  N N   . PRO B 1 8  ? 28.842  -9.170  -39.288 1.00 47.50  ? 7   PRO B N   1 
ATOM   808  C CA  . PRO B 1 8  ? 28.137  -8.288  -38.363 1.00 40.16  ? 7   PRO B CA  1 
ATOM   809  C C   . PRO B 1 8  ? 27.010  -7.538  -39.051 1.00 37.50  ? 7   PRO B C   1 
ATOM   810  O O   . PRO B 1 8  ? 27.149  -7.066  -40.189 1.00 40.39  ? 7   PRO B O   1 
ATOM   811  C CB  . PRO B 1 8  ? 29.261  -7.414  -37.803 1.00 45.69  ? 7   PRO B CB  1 
ATOM   812  C CG  . PRO B 1 8  ? 30.486  -8.306  -37.909 1.00 48.31  ? 7   PRO B CG  1 
ATOM   813  C CD  . PRO B 1 8  ? 30.297  -8.920  -39.294 1.00 49.25  ? 7   PRO B CD  1 
ATOM   814  N N   . GLY B 1 9  ? 25.851  -7.530  -38.371 1.00 33.53  ? 8   GLY B N   1 
ATOM   815  C CA  . GLY B 1 9  ? 24.632  -6.928  -38.864 1.00 30.37  ? 8   GLY B CA  1 
ATOM   816  C C   . GLY B 1 9  ? 23.692  -7.932  -39.510 1.00 27.57  ? 8   GLY B C   1 
ATOM   817  O O   . GLY B 1 9  ? 22.574  -7.597  -39.874 1.00 30.24  ? 8   GLY B O   1 
ATOM   818  N N   . ASP B 1 10 ? 24.170  -9.166  -39.755 1.00 31.29  ? 9   ASP B N   1 
ATOM   819  C CA  . ASP B 1 10 ? 23.320  -10.197 -40.330 1.00 30.81  ? 9   ASP B CA  1 
ATOM   820  C C   . ASP B 1 10 ? 22.190  -10.527 -39.346 1.00 24.09  ? 9   ASP B C   1 
ATOM   821  O O   . ASP B 1 10 ? 22.453  -10.564 -38.142 1.00 28.70  ? 9   ASP B O   1 
ATOM   822  C CB  . ASP B 1 10 ? 24.136  -11.450 -40.606 1.00 32.79  ? 9   ASP B CB  1 
ATOM   823  C CG  . ASP B 1 10 ? 24.855  -11.489 -41.951 1.00 40.60  ? 9   ASP B CG  1 
ATOM   824  O OD1 . ASP B 1 10 ? 24.537  -10.655 -42.818 1.00 40.03  ? 9   ASP B OD1 1 
ATOM   825  O OD2 . ASP B 1 10 ? 25.714  -12.378 -42.114 1.00 38.06  ? 9   ASP B OD2 1 
ATOM   826  N N   . LEU B 1 11 ? 20.981  -10.638 -39.868 1.00 25.76  ? 10  LEU B N   1 
ATOM   827  C CA  . LEU B 1 11 ? 19.838  -10.842 -38.982 1.00 24.24  ? 10  LEU B CA  1 
ATOM   828  C C   . LEU B 1 11 ? 19.541  -12.335 -38.981 1.00 24.96  ? 10  LEU B C   1 
ATOM   829  O O   . LEU B 1 11 ? 19.592  -12.958 -40.053 1.00 27.83  ? 10  LEU B O   1 
ATOM   830  C CB  . LEU B 1 11 ? 18.645  -10.030 -39.472 1.00 26.52  ? 10  LEU B CB  1 
ATOM   831  C CG  . LEU B 1 11 ? 18.925  -8.506  -39.522 1.00 23.97  ? 10  LEU B CG  1 
ATOM   832  C CD1 . LEU B 1 11 ? 17.653  -7.798  -39.904 1.00 28.11  ? 10  LEU B CD1 1 
ATOM   833  C CD2 . LEU B 1 11 ? 19.558  -8.075  -38.186 1.00 26.37  ? 10  LEU B CD2 1 
ATOM   834  N N   . VAL B 1 12 ? 19.119  -12.871 -37.819 1.00 23.89  ? 11  VAL B N   1 
ATOM   835  C CA  . VAL B 1 12 ? 18.907  -14.318 -37.750 1.00 22.65  ? 11  VAL B CA  1 
ATOM   836  C C   . VAL B 1 12 ? 17.792  -14.566 -36.736 1.00 26.61  ? 11  VAL B C   1 
ATOM   837  O O   . VAL B 1 12 ? 17.371  -13.644 -36.010 1.00 24.32  ? 11  VAL B O   1 
ATOM   838  C CB  . VAL B 1 12 ? 20.195  -15.041 -37.320 1.00 23.39  ? 11  VAL B CB  1 
ATOM   839  C CG1 . VAL B 1 12 ? 21.321  -14.843 -38.356 1.00 26.77  ? 11  VAL B CG1 1 
ATOM   840  C CG2 . VAL B 1 12 ? 20.644  -14.704 -35.877 1.00 25.76  ? 11  VAL B CG2 1 
ATOM   841  N N   . PHE B 1 13 ? 17.316  -15.818 -36.715 1.00 24.75  ? 12  PHE B N   1 
ATOM   842  C CA  . PHE B 1 13 ? 16.774  -16.357 -35.483 1.00 24.23  ? 12  PHE B CA  1 
ATOM   843  C C   . PHE B 1 13 ? 17.851  -17.244 -34.893 1.00 27.75  ? 12  PHE B C   1 
ATOM   844  O O   . PHE B 1 13 ? 18.466  -18.018 -35.647 1.00 25.29  ? 12  PHE B O   1 
ATOM   845  C CB  . PHE B 1 13 ? 15.528  -17.197 -35.744 1.00 23.76  ? 12  PHE B CB  1 
ATOM   846  C CG  . PHE B 1 13 ? 14.317  -16.374 -36.131 1.00 26.61  ? 12  PHE B CG  1 
ATOM   847  C CD1 . PHE B 1 13 ? 14.090  -15.990 -37.457 1.00 27.92  ? 12  PHE B CD1 1 
ATOM   848  C CD2 . PHE B 1 13 ? 13.414  -15.962 -35.153 1.00 25.60  ? 12  PHE B CD2 1 
ATOM   849  C CE1 . PHE B 1 13 ? 12.963  -15.257 -37.790 1.00 30.22  ? 12  PHE B CE1 1 
ATOM   850  C CE2 . PHE B 1 13 ? 12.293  -15.222 -35.494 1.00 27.77  ? 12  PHE B CE2 1 
ATOM   851  C CZ  . PHE B 1 13 ? 12.074  -14.859 -36.814 1.00 33.51  ? 12  PHE B CZ  1 
ATOM   852  N N   . ALA B 1 14 ? 18.032  -17.159 -33.557 1.00 24.05  ? 13  ALA B N   1 
ATOM   853  C CA  . ALA B 1 14 ? 19.086  -17.914 -32.926 1.00 23.27  ? 13  ALA B CA  1 
ATOM   854  C C   . ALA B 1 14 ? 18.507  -18.823 -31.842 1.00 24.01  ? 13  ALA B C   1 
ATOM   855  O O   . ALA B 1 14 ? 17.567  -18.414 -31.162 1.00 25.18  ? 13  ALA B O   1 
ATOM   856  C CB  . ALA B 1 14 ? 20.068  -16.934 -32.332 1.00 25.34  ? 13  ALA B CB  1 
ATOM   857  N N   . LYS B 1 15 ? 18.981  -20.072 -31.811 1.00 23.39  ? 14  LYS B N   1 
ATOM   858  C CA  . LYS B 1 15 ? 18.355  -21.090 -30.954 1.00 24.09  ? 14  LYS B CA  1 
ATOM   859  C C   . LYS B 1 15 ? 19.246  -21.424 -29.775 1.00 27.41  ? 14  LYS B C   1 
ATOM   860  O O   . LYS B 1 15 ? 20.424  -21.740 -29.941 1.00 30.59  ? 14  LYS B O   1 
ATOM   861  C CB  . LYS B 1 15 ? 18.047  -22.343 -31.806 1.00 29.23  ? 14  LYS B CB  1 
ATOM   862  C CG  . LYS B 1 15 ? 17.315  -23.473 -31.055 1.00 24.96  ? 14  LYS B CG  1 
ATOM   863  C CD  . LYS B 1 15 ? 15.870  -23.057 -30.750 1.00 26.52  ? 14  LYS B CD  1 
ATOM   864  C CE  . LYS B 1 15 ? 15.018  -24.143 -30.049 1.00 28.51  ? 14  LYS B CE  1 
ATOM   865  N NZ  . LYS B 1 15 ? 15.595  -24.414 -28.727 1.00 29.12  ? 14  LYS B NZ  1 
ATOM   866  N N   . MET B 1 16 ? 18.666  -21.351 -28.569 1.00 27.20  ? 15  MET B N   1 
ATOM   867  C CA  . MET B 1 16 ? 19.339  -21.841 -27.374 1.00 32.35  ? 15  MET B CA  1 
ATOM   868  C C   . MET B 1 16 ? 18.428  -22.848 -26.683 1.00 30.39  ? 15  MET B C   1 
ATOM   869  O O   . MET B 1 16 ? 17.201  -22.725 -26.772 1.00 27.46  ? 15  MET B O   1 
ATOM   870  C CB  . MET B 1 16 ? 19.648  -20.692 -26.413 1.00 35.61  ? 15  MET B CB  1 
ATOM   871  C CG  . MET B 1 16 ? 20.473  -19.598 -27.061 1.00 38.09  ? 15  MET B CG  1 
ATOM   872  S SD  . MET B 1 16 ? 21.545  -18.647 -25.966 1.00 40.76  ? 15  MET B SD  1 
ATOM   873  C CE  . MET B 1 16 ? 21.038  -18.969 -24.274 1.00 50.96  ? 15  MET B CE  1 
ATOM   874  N N   . LYS B 1 17 ? 19.041  -23.833 -26.007 1.00 29.65  ? 16  LYS B N   1 
ATOM   875  C CA  . LYS B 1 17 ? 18.252  -24.811 -25.264 1.00 34.62  ? 16  LYS B CA  1 
ATOM   876  C C   . LYS B 1 17 ? 17.329  -24.090 -24.276 1.00 30.17  ? 16  LYS B C   1 
ATOM   877  O O   . LYS B 1 17 ? 17.754  -23.180 -23.570 1.00 33.88  ? 16  LYS B O   1 
ATOM   878  C CB  . LYS B 1 17 ? 19.163  -25.809 -24.536 1.00 43.22  ? 16  LYS B CB  1 
ATOM   879  C CG  . LYS B 1 17 ? 18.412  -26.900 -23.748 1.00 44.51  ? 16  LYS B CG  1 
ATOM   880  C CD  . LYS B 1 17 ? 19.265  -28.076 -23.267 1.00 49.87  ? 16  LYS B CD  1 
ATOM   881  N N   . GLY B 1 18 ? 16.047  -24.457 -24.308 1.00 32.69  ? 17  GLY B N   1 
ATOM   882  C CA  . GLY B 1 18 ? 15.071  -23.932 -23.371 1.00 33.39  ? 17  GLY B CA  1 
ATOM   883  C C   . GLY B 1 18 ? 14.263  -22.768 -23.929 1.00 33.90  ? 17  GLY B C   1 
ATOM   884  O O   . GLY B 1 18 ? 13.353  -22.286 -23.253 1.00 32.48  ? 17  GLY B O   1 
ATOM   885  N N   . TYR B 1 19 ? 14.590  -22.311 -25.157 1.00 28.66  ? 18  TYR B N   1 
ATOM   886  C CA  . TYR B 1 19 ? 13.935  -21.109 -25.638 1.00 28.34  ? 18  TYR B CA  1 
ATOM   887  C C   . TYR B 1 19 ? 13.533  -21.367 -27.086 1.00 28.27  ? 18  TYR B C   1 
ATOM   888  O O   . TYR B 1 19 ? 14.217  -22.112 -27.784 1.00 30.00  ? 18  TYR B O   1 
ATOM   889  C CB  . TYR B 1 19 ? 14.960  -19.970 -25.630 1.00 25.64  ? 18  TYR B CB  1 
ATOM   890  C CG  . TYR B 1 19 ? 15.481  -19.643 -24.234 1.00 28.30  ? 18  TYR B CG  1 
ATOM   891  C CD1 . TYR B 1 19 ? 14.820  -18.704 -23.431 1.00 31.82  ? 18  TYR B CD1 1 
ATOM   892  C CD2 . TYR B 1 19 ? 16.593  -20.304 -23.721 1.00 30.55  ? 18  TYR B CD2 1 
ATOM   893  C CE1 . TYR B 1 19 ? 15.279  -18.430 -22.144 1.00 35.10  ? 18  TYR B CE1 1 
ATOM   894  C CE2 . TYR B 1 19 ? 17.082  -19.997 -22.458 1.00 36.43  ? 18  TYR B CE2 1 
ATOM   895  C CZ  . TYR B 1 19 ? 16.423  -19.057 -21.678 1.00 34.90  ? 18  TYR B CZ  1 
ATOM   896  O OH  . TYR B 1 19 ? 16.948  -18.790 -20.442 1.00 34.38  ? 18  TYR B OH  1 
ATOM   897  N N   . PRO B 1 20 ? 12.478  -20.697 -27.586 1.00 25.97  ? 19  PRO B N   1 
ATOM   898  C CA  . PRO B 1 20 ? 12.147  -20.756 -29.019 1.00 23.98  ? 19  PRO B CA  1 
ATOM   899  C C   . PRO B 1 20 ? 13.216  -20.013 -29.832 1.00 25.28  ? 19  PRO B C   1 
ATOM   900  O O   . PRO B 1 20 ? 13.949  -19.174 -29.315 1.00 25.46  ? 19  PRO B O   1 
ATOM   901  C CB  . PRO B 1 20 ? 10.815  -20.084 -29.094 1.00 24.24  ? 19  PRO B CB  1 
ATOM   902  C CG  . PRO B 1 20 ? 10.878  -19.032 -27.977 1.00 27.43  ? 19  PRO B CG  1 
ATOM   903  C CD  . PRO B 1 20 ? 11.648  -19.735 -26.856 1.00 27.72  ? 19  PRO B CD  1 
ATOM   904  N N   . HIS B 1 21 ? 13.294  -20.352 -31.127 1.00 24.14  ? 20  HIS B N   1 
ATOM   905  C CA  . HIS B 1 21 ? 14.156  -19.626 -32.057 1.00 24.48  ? 20  HIS B CA  1 
ATOM   906  C C   . HIS B 1 21 ? 13.888  -18.125 -31.935 1.00 22.03  ? 20  HIS B C   1 
ATOM   907  O O   . HIS B 1 21 ? 12.734  -17.692 -32.013 1.00 24.44  ? 20  HIS B O   1 
ATOM   908  C CB  . HIS B 1 21 ? 13.823  -20.112 -33.478 1.00 25.42  ? 20  HIS B CB  1 
ATOM   909  C CG  . HIS B 1 21 ? 14.086  -21.580 -33.692 1.00 27.33  ? 20  HIS B CG  1 
ATOM   910  N ND1 . HIS B 1 21 ? 13.222  -22.579 -33.268 1.00 26.39  ? 20  HIS B ND1 1 
ATOM   911  C CD2 . HIS B 1 21 ? 15.127  -22.225 -34.277 1.00 28.42  ? 20  HIS B CD2 1 
ATOM   912  C CE1 . HIS B 1 21 ? 13.724  -23.770 -33.586 1.00 27.67  ? 20  HIS B CE1 1 
ATOM   913  N NE2 . HIS B 1 21 ? 14.884  -23.595 -34.208 1.00 26.89  ? 20  HIS B NE2 1 
ATOM   914  N N   . TRP B 1 22 ? 14.954  -17.344 -31.758 1.00 22.13  ? 21  TRP B N   1 
ATOM   915  C CA  . TRP B 1 22 ? 14.749  -16.021 -31.159 1.00 21.63  ? 21  TRP B CA  1 
ATOM   916  C C   . TRP B 1 22 ? 15.292  -14.947 -32.100 1.00 23.15  ? 21  TRP B C   1 
ATOM   917  O O   . TRP B 1 22 ? 16.430  -15.107 -32.545 1.00 22.87  ? 21  TRP B O   1 
ATOM   918  C CB  . TRP B 1 22 ? 15.440  -15.961 -29.800 1.00 22.53  ? 21  TRP B CB  1 
ATOM   919  C CG  . TRP B 1 22 ? 14.965  -14.819 -28.941 1.00 22.71  ? 21  TRP B CG  1 
ATOM   920  C CD1 . TRP B 1 22 ? 15.277  -13.491 -29.081 1.00 21.63  ? 21  TRP B CD1 1 
ATOM   921  C CD2 . TRP B 1 22 ? 14.009  -14.895 -27.846 1.00 25.38  ? 21  TRP B CD2 1 
ATOM   922  N NE1 . TRP B 1 22 ? 14.604  -12.735 -28.154 1.00 24.01  ? 21  TRP B NE1 1 
ATOM   923  C CE2 . TRP B 1 22 ? 13.826  -13.574 -27.377 1.00 26.10  ? 21  TRP B CE2 1 
ATOM   924  C CE3 . TRP B 1 22 ? 13.333  -15.957 -27.227 1.00 25.84  ? 21  TRP B CE3 1 
ATOM   925  C CZ2 . TRP B 1 22 ? 12.962  -13.260 -26.319 1.00 27.09  ? 21  TRP B CZ2 1 
ATOM   926  C CZ3 . TRP B 1 22 ? 12.477  -15.647 -26.182 1.00 26.70  ? 21  TRP B CZ3 1 
ATOM   927  C CH2 . TRP B 1 22 ? 12.254  -14.312 -25.777 1.00 25.82  ? 21  TRP B CH2 1 
ATOM   928  N N   . PRO B 1 23 ? 14.553  -13.851 -32.406 1.00 23.02  ? 22  PRO B N   1 
ATOM   929  C CA  . PRO B 1 23 ? 15.090  -12.821 -33.325 1.00 23.80  ? 22  PRO B CA  1 
ATOM   930  C C   . PRO B 1 23 ? 16.391  -12.263 -32.770 1.00 23.37  ? 22  PRO B C   1 
ATOM   931  O O   . PRO B 1 23 ? 16.514  -11.946 -31.576 1.00 22.46  ? 22  PRO B O   1 
ATOM   932  C CB  . PRO B 1 23 ? 13.930  -11.773 -33.390 1.00 23.12  ? 22  PRO B CB  1 
ATOM   933  C CG  . PRO B 1 23 ? 13.195  -11.942 -32.057 1.00 24.56  ? 22  PRO B CG  1 
ATOM   934  C CD  . PRO B 1 23 ? 13.224  -13.478 -31.892 1.00 22.28  ? 22  PRO B CD  1 
ATOM   935  N N   . ALA B 1 24 ? 17.428  -12.156 -33.608 1.00 23.04  ? 23  ALA B N   1 
ATOM   936  C CA  . ALA B 1 24 ? 18.742  -11.794 -33.098 1.00 21.74  ? 23  ALA B CA  1 
ATOM   937  C C   . ALA B 1 24 ? 19.594  -11.235 -34.244 1.00 22.33  ? 23  ALA B C   1 
ATOM   938  O O   . ALA B 1 24 ? 19.167  -11.270 -35.392 1.00 24.01  ? 23  ALA B O   1 
ATOM   939  C CB  . ALA B 1 24 ? 19.444  -12.962 -32.443 1.00 23.60  ? 23  ALA B CB  1 
ATOM   940  N N   . ARG B 1 25 ? 20.769  -10.734 -33.882 1.00 25.67  ? 24  ARG B N   1 
ATOM   941  C CA  . ARG B 1 25 ? 21.730  -10.254 -34.874 1.00 24.70  ? 24  ARG B CA  1 
ATOM   942  C C   . ARG B 1 25 ? 23.121  -10.729 -34.500 1.00 23.42  ? 24  ARG B C   1 
ATOM   943  O O   . ARG B 1 25 ? 23.451  -10.953 -33.350 1.00 24.04  ? 24  ARG B O   1 
ATOM   944  C CB  . ARG B 1 25 ? 21.685  -8.730  -35.001 1.00 24.12  ? 24  ARG B CB  1 
ATOM   945  C CG  . ARG B 1 25 ? 22.314  -7.988  -33.845 1.00 23.50  ? 24  ARG B CG  1 
ATOM   946  C CD  . ARG B 1 25 ? 22.095  -6.473  -34.028 1.00 24.66  ? 24  ARG B CD  1 
ATOM   947  N NE  . ARG B 1 25 ? 22.601  -5.756  -32.859 1.00 25.09  ? 24  ARG B NE  1 
ATOM   948  C CZ  . ARG B 1 25 ? 22.325  -4.480  -32.528 1.00 24.74  ? 24  ARG B CZ  1 
ATOM   949  N NH1 . ARG B 1 25 ? 21.367  -3.811  -33.157 1.00 24.60  ? 24  ARG B NH1 1 
ATOM   950  N NH2 . ARG B 1 25 ? 22.986  -3.904  -31.528 1.00 26.98  ? 24  ARG B NH2 1 
ATOM   951  N N   . ILE B 1 26 ? 23.979  -10.814 -35.531 1.00 26.18  ? 25  ILE B N   1 
ATOM   952  C CA  . ILE B 1 26 ? 25.411  -11.011 -35.347 1.00 29.72  ? 25  ILE B CA  1 
ATOM   953  C C   . ILE B 1 26 ? 25.978  -9.635  -35.012 1.00 30.78  ? 25  ILE B C   1 
ATOM   954  O O   . ILE B 1 26 ? 25.752  -8.677  -35.751 1.00 31.68  ? 25  ILE B O   1 
ATOM   955  C CB  . ILE B 1 26 ? 26.035  -11.505 -36.662 1.00 32.84  ? 25  ILE B CB  1 
ATOM   956  C CG1 . ILE B 1 26 ? 25.254  -12.677 -37.237 1.00 32.52  ? 25  ILE B CG1 1 
ATOM   957  C CG2 . ILE B 1 26 ? 27.533  -11.803 -36.475 1.00 33.73  ? 25  ILE B CG2 1 
ATOM   958  C CD1 . ILE B 1 26 ? 25.360  -13.945 -36.416 1.00 33.38  ? 25  ILE B CD1 1 
ATOM   959  N N   . ASP B 1 27 ? 26.709  -9.571  -33.916 1.00 32.00  ? 26  ASP B N   1 
ATOM   960  C CA  . ASP B 1 27 ? 27.393  -8.353  -33.522 1.00 37.77  ? 26  ASP B CA  1 
ATOM   961  C C   . ASP B 1 27 ? 28.870  -8.461  -33.914 1.00 46.59  ? 26  ASP B C   1 
ATOM   962  O O   . ASP B 1 27 ? 29.357  -9.547  -34.217 1.00 42.94  ? 26  ASP B O   1 
ATOM   963  C CB  . ASP B 1 27 ? 27.314  -8.222  -32.015 1.00 34.64  ? 26  ASP B CB  1 
ATOM   964  C CG  . ASP B 1 27 ? 26.118  -7.474  -31.444 1.00 39.33  ? 26  ASP B CG  1 
ATOM   965  O OD1 . ASP B 1 27 ? 25.329  -6.896  -32.228 1.00 40.98  ? 26  ASP B OD1 1 
ATOM   966  O OD2 . ASP B 1 27 ? 26.017  -7.433  -30.193 1.00 37.20  ? 26  ASP B OD2 1 
ATOM   967  N N   A ASP B 1 28 ? 29.578  -7.326  -33.874 0.50 50.42  ? 27  ASP B N   1 
ATOM   968  N N   B ASP B 1 28 ? 29.570  -7.318  -33.867 0.50 50.56  ? 27  ASP B N   1 
ATOM   969  C CA  A ASP B 1 28 ? 31.007  -7.258  -34.143 0.50 55.07  ? 27  ASP B CA  1 
ATOM   970  C CA  B ASP B 1 28 ? 30.999  -7.242  -34.134 0.50 55.51  ? 27  ASP B CA  1 
ATOM   971  C C   A ASP B 1 28 ? 31.748  -7.404  -32.819 0.50 59.10  ? 27  ASP B C   1 
ATOM   972  C C   B ASP B 1 28 ? 31.732  -7.442  -32.811 0.50 59.36  ? 27  ASP B C   1 
ATOM   973  O O   A ASP B 1 28 ? 31.208  -7.044  -31.774 0.50 62.51  ? 27  ASP B O   1 
ATOM   974  O O   B ASP B 1 28 ? 31.170  -7.155  -31.757 0.50 62.86  ? 27  ASP B O   1 
ATOM   975  C CB  A ASP B 1 28 ? 31.316  -5.945  -34.839 0.50 53.60  ? 27  ASP B CB  1 
ATOM   976  C CB  B ASP B 1 28 ? 31.356  -5.905  -34.763 0.50 53.97  ? 27  ASP B CB  1 
ATOM   977  C CG  A ASP B 1 28 ? 30.268  -4.883  -34.549 0.50 52.15  ? 27  ASP B CG  1 
ATOM   978  C CG  B ASP B 1 28 ? 32.428  -5.957  -35.839 0.50 53.64  ? 27  ASP B CG  1 
ATOM   979  O OD1 A ASP B 1 28 ? 29.612  -4.435  -35.507 0.50 50.82  ? 27  ASP B OD1 1 
ATOM   980  O OD1 B ASP B 1 28 ? 33.550  -6.409  -35.528 0.50 53.80  ? 27  ASP B OD1 1 
ATOM   981  O OD2 A ASP B 1 28 ? 30.066  -4.577  -33.351 0.50 54.84  ? 27  ASP B OD2 1 
ATOM   982  O OD2 B ASP B 1 28 ? 32.124  -5.549  -36.978 0.50 53.63  ? 27  ASP B OD2 1 
ATOM   983  N N   . ILE B 1 29 ? 32.977  -7.935  -32.878 1.00 66.75  ? 28  ILE B N   1 
ATOM   984  C CA  . ILE B 1 29 ? 33.777  -8.181  -31.684 1.00 68.33  ? 28  ILE B CA  1 
ATOM   985  C C   . ILE B 1 29 ? 34.134  -6.844  -31.029 1.00 78.93  ? 28  ILE B C   1 
ATOM   986  O O   . ILE B 1 29 ? 34.453  -5.866  -31.710 1.00 81.80  ? 28  ILE B O   1 
ATOM   987  C CB  . ILE B 1 29 ? 35.012  -9.048  -31.998 1.00 67.27  ? 28  ILE B CB  1 
ATOM   988  N N   . ALA B 1 30 ? 34.035  -6.819  -29.694 1.00 80.52  ? 29  ALA B N   1 
ATOM   989  C CA  . ALA B 1 30 ? 34.217  -5.625  -28.885 1.00 71.18  ? 29  ALA B CA  1 
ATOM   990  C C   . ALA B 1 30 ? 35.075  -5.969  -27.666 1.00 68.62  ? 29  ALA B C   1 
ATOM   991  O O   . ALA B 1 30 ? 36.293  -5.711  -27.749 1.00 76.10  ? 29  ALA B O   1 
ATOM   992  C CB  . ALA B 1 30 ? 32.865  -5.079  -28.468 1.00 72.93  ? 29  ALA B CB  1 
ATOM   993  N N   . VAL B 1 34 ? 35.468  -10.473 -24.047 1.00 66.68  ? 33  VAL B N   1 
ATOM   994  C CA  . VAL B 1 34 ? 36.376  -11.561 -24.531 1.00 75.44  ? 33  VAL B CA  1 
ATOM   995  C C   . VAL B 1 34 ? 36.401  -11.523 -26.060 1.00 75.78  ? 33  VAL B C   1 
ATOM   996  O O   . VAL B 1 34 ? 36.197  -10.461 -26.643 1.00 80.66  ? 33  VAL B O   1 
ATOM   997  C CB  . VAL B 1 34 ? 35.894  -12.910 -23.952 1.00 78.60  ? 33  VAL B CB  1 
ATOM   998  C CG1 . VAL B 1 34 ? 34.495  -13.285 -24.425 1.00 70.76  ? 33  VAL B CG1 1 
ATOM   999  C CG2 . VAL B 1 34 ? 36.884  -14.051 -24.179 1.00 84.03  ? 33  VAL B CG2 1 
ATOM   1000 N N   . LYS B 1 35 ? 36.720  -12.660 -26.696 1.00 73.43  ? 34  LYS B N   1 
ATOM   1001 C CA  . LYS B 1 35 ? 36.401  -12.916 -28.098 1.00 73.02  ? 34  LYS B CA  1 
ATOM   1002 C C   . LYS B 1 35 ? 35.537  -14.179 -28.173 1.00 69.43  ? 34  LYS B C   1 
ATOM   1003 O O   . LYS B 1 35 ? 35.566  -14.999 -27.246 1.00 67.41  ? 34  LYS B O   1 
ATOM   1004 C CB  . LYS B 1 35 ? 37.661  -13.027 -28.970 1.00 67.82  ? 34  LYS B CB  1 
ATOM   1005 N N   . PRO B 1 36 ? 34.721  -14.391 -29.241 1.00 65.72  ? 35  PRO B N   1 
ATOM   1006 C CA  . PRO B 1 36 ? 33.959  -15.638 -29.363 1.00 55.10  ? 35  PRO B CA  1 
ATOM   1007 C C   . PRO B 1 36 ? 34.937  -16.805 -29.380 1.00 48.21  ? 35  PRO B C   1 
ATOM   1008 O O   . PRO B 1 36 ? 36.009  -16.699 -29.968 1.00 52.58  ? 35  PRO B O   1 
ATOM   1009 C CB  . PRO B 1 36 ? 33.166  -15.532 -30.683 1.00 51.89  ? 35  PRO B CB  1 
ATOM   1010 C CG  . PRO B 1 36 ? 33.791  -14.347 -31.412 1.00 57.45  ? 35  PRO B CG  1 
ATOM   1011 C CD  . PRO B 1 36 ? 34.475  -13.469 -30.366 1.00 57.29  ? 35  PRO B CD  1 
ATOM   1012 N N   . PRO B 1 37 ? 34.595  -17.957 -28.760 1.00 50.47  ? 36  PRO B N   1 
ATOM   1013 C CA  . PRO B 1 37 ? 35.365  -19.176 -28.979 1.00 49.72  ? 36  PRO B CA  1 
ATOM   1014 C C   . PRO B 1 37 ? 35.420  -19.425 -30.491 1.00 58.37  ? 36  PRO B C   1 
ATOM   1015 O O   . PRO B 1 37 ? 34.617  -18.875 -31.260 1.00 53.89  ? 36  PRO B O   1 
ATOM   1016 C CB  . PRO B 1 37 ? 34.573  -20.283 -28.242 1.00 47.82  ? 36  PRO B CB  1 
ATOM   1017 C CG  . PRO B 1 37 ? 33.561  -19.563 -27.374 1.00 50.93  ? 36  PRO B CG  1 
ATOM   1018 C CD  . PRO B 1 37 ? 33.419  -18.149 -27.893 1.00 50.86  ? 36  PRO B CD  1 
ATOM   1019 N N   . PRO B 1 38 ? 36.344  -20.289 -30.975 1.00 55.44  ? 37  PRO B N   1 
ATOM   1020 C CA  . PRO B 1 38 ? 36.409  -20.621 -32.406 1.00 59.66  ? 37  PRO B CA  1 
ATOM   1021 C C   . PRO B 1 38 ? 35.111  -21.225 -32.947 1.00 54.43  ? 37  PRO B C   1 
ATOM   1022 O O   . PRO B 1 38 ? 34.455  -22.011 -32.268 1.00 58.63  ? 37  PRO B O   1 
ATOM   1023 C CB  . PRO B 1 38 ? 37.601  -21.594 -32.537 1.00 63.65  ? 37  PRO B CB  1 
ATOM   1024 C CG  . PRO B 1 38 ? 38.335  -21.506 -31.198 1.00 57.79  ? 37  PRO B CG  1 
ATOM   1025 C CD  . PRO B 1 38 ? 37.349  -20.999 -30.162 1.00 57.53  ? 37  PRO B CD  1 
ATOM   1026 N N   . ASN B 1 39 ? 34.737  -20.820 -34.166 1.00 51.46  ? 38  ASN B N   1 
ATOM   1027 C CA  . ASN B 1 39 ? 33.544  -21.306 -34.853 1.00 52.86  ? 38  ASN B CA  1 
ATOM   1028 C C   . ASN B 1 39 ? 32.264  -20.607 -34.383 1.00 46.73  ? 38  ASN B C   1 
ATOM   1029 O O   . ASN B 1 39 ? 31.205  -20.868 -34.938 1.00 41.85  ? 38  ASN B O   1 
ATOM   1030 C CB  . ASN B 1 39 ? 33.346  -22.815 -34.733 1.00 51.40  ? 38  ASN B CB  1 
ATOM   1031 C CG  . ASN B 1 39 ? 34.594  -23.624 -34.998 1.00 65.54  ? 38  ASN B CG  1 
ATOM   1032 O OD1 . ASN B 1 39 ? 34.863  -24.581 -34.261 1.00 69.51  ? 38  ASN B OD1 1 
ATOM   1033 N ND2 . ASN B 1 39 ? 35.359  -23.278 -36.026 1.00 58.26  ? 38  ASN B ND2 1 
ATOM   1034 N N   . LYS B 1 40 ? 32.344  -19.701 -33.395 1.00 45.53  ? 39  LYS B N   1 
ATOM   1035 C CA  . LYS B 1 40 ? 31.132  -19.099 -32.854 1.00 44.18  ? 39  LYS B CA  1 
ATOM   1036 C C   . LYS B 1 40 ? 31.090  -17.594 -33.098 1.00 44.73  ? 39  LYS B C   1 
ATOM   1037 O O   . LYS B 1 40 ? 32.107  -16.954 -33.354 1.00 45.31  ? 39  LYS B O   1 
ATOM   1038 C CB  . LYS B 1 40 ? 31.037  -19.450 -31.370 1.00 45.04  ? 39  LYS B CB  1 
ATOM   1039 C CG  . LYS B 1 40 ? 31.020  -20.941 -31.107 1.00 46.35  ? 39  LYS B CG  1 
ATOM   1040 C CD  . LYS B 1 40 ? 30.994  -21.224 -29.610 1.00 54.84  ? 39  LYS B CD  1 
ATOM   1041 C CE  . LYS B 1 40 ? 29.658  -21.459 -28.992 1.00 58.20  ? 39  LYS B CE  1 
ATOM   1042 N NZ  . LYS B 1 40 ? 29.215  -22.820 -29.299 1.00 63.52  ? 39  LYS B NZ  1 
ATOM   1043 N N   . TYR B 1 41 ? 29.887  -17.023 -32.994 1.00 38.02  ? 40  TYR B N   1 
ATOM   1044 C CA  . TYR B 1 41 ? 29.723  -15.605 -33.259 1.00 36.08  ? 40  TYR B CA  1 
ATOM   1045 C C   . TYR B 1 41 ? 29.126  -14.955 -32.025 1.00 36.49  ? 40  TYR B C   1 
ATOM   1046 O O   . TYR B 1 41 ? 28.384  -15.607 -31.305 1.00 32.90  ? 40  TYR B O   1 
ATOM   1047 C CB  . TYR B 1 41 ? 28.693  -15.456 -34.378 1.00 32.93  ? 40  TYR B CB  1 
ATOM   1048 C CG  . TYR B 1 41 ? 29.191  -15.944 -35.732 1.00 38.69  ? 40  TYR B CG  1 
ATOM   1049 C CD1 . TYR B 1 41 ? 29.865  -15.077 -36.587 1.00 36.46  ? 40  TYR B CD1 1 
ATOM   1050 C CD2 . TYR B 1 41 ? 28.977  -17.250 -36.153 1.00 37.26  ? 40  TYR B CD2 1 
ATOM   1051 C CE1 . TYR B 1 41 ? 30.344  -15.509 -37.815 1.00 41.65  ? 40  TYR B CE1 1 
ATOM   1052 C CE2 . TYR B 1 41 ? 29.432  -17.689 -37.388 1.00 37.58  ? 40  TYR B CE2 1 
ATOM   1053 C CZ  . TYR B 1 41 ? 30.129  -16.817 -38.211 1.00 39.32  ? 40  TYR B CZ  1 
ATOM   1054 O OH  . TYR B 1 41 ? 30.582  -17.213 -39.438 1.00 38.61  ? 40  TYR B OH  1 
ATOM   1055 N N   . PRO B 1 42 ? 29.380  -13.647 -31.798 1.00 38.02  ? 41  PRO B N   1 
ATOM   1056 C CA  . PRO B 1 42 ? 28.648  -12.914 -30.773 1.00 33.44  ? 41  PRO B CA  1 
ATOM   1057 C C   . PRO B 1 42 ? 27.227  -12.679 -31.284 1.00 32.42  ? 41  PRO B C   1 
ATOM   1058 O O   . PRO B 1 42 ? 27.025  -12.053 -32.330 1.00 34.74  ? 41  PRO B O   1 
ATOM   1059 C CB  . PRO B 1 42 ? 29.465  -11.603 -30.609 1.00 37.33  ? 41  PRO B CB  1 
ATOM   1060 C CG  . PRO B 1 42 ? 30.208  -11.419 -31.919 1.00 38.11  ? 41  PRO B CG  1 
ATOM   1061 C CD  . PRO B 1 42 ? 30.310  -12.800 -32.562 1.00 39.00  ? 41  PRO B CD  1 
ATOM   1062 N N   . ILE B 1 43 ? 26.236  -13.149 -30.510 1.00 28.47  ? 42  ILE B N   1 
ATOM   1063 C CA  . ILE B 1 43 ? 24.843  -12.923 -30.842 1.00 25.61  ? 42  ILE B CA  1 
ATOM   1064 C C   . ILE B 1 43 ? 24.223  -11.895 -29.887 1.00 28.13  ? 42  ILE B C   1 
ATOM   1065 O O   . ILE B 1 43 ? 24.438  -11.966 -28.690 1.00 33.97  ? 42  ILE B O   1 
ATOM   1066 C CB  . ILE B 1 43 ? 24.106  -14.257 -30.685 1.00 28.00  ? 42  ILE B CB  1 
ATOM   1067 C CG1 . ILE B 1 43 ? 24.858  -15.402 -31.418 1.00 28.67  ? 42  ILE B CG1 1 
ATOM   1068 C CG2 . ILE B 1 43 ? 22.658  -14.116 -31.168 1.00 28.27  ? 42  ILE B CG2 1 
ATOM   1069 C CD1 . ILE B 1 43 ? 25.105  -15.147 -32.890 1.00 28.71  ? 42  ILE B CD1 1 
ATOM   1070 N N   . PHE B 1 44 ? 23.438  -10.987 -30.453 1.00 26.68  ? 43  PHE B N   1 
ATOM   1071 C CA  . PHE B 1 44 ? 22.630  -10.046 -29.688 1.00 28.21  ? 43  PHE B CA  1 
ATOM   1072 C C   . PHE B 1 44 ? 21.170  -10.434 -29.872 1.00 24.53  ? 43  PHE B C   1 
ATOM   1073 O O   . PHE B 1 44 ? 20.650  -10.467 -30.998 1.00 24.94  ? 43  PHE B O   1 
ATOM   1074 C CB  . PHE B 1 44 ? 22.901  -8.581  -30.075 1.00 26.84  ? 43  PHE B CB  1 
ATOM   1075 C CG  . PHE B 1 44 ? 21.928  -7.570  -29.464 1.00 26.81  ? 43  PHE B CG  1 
ATOM   1076 C CD1 . PHE B 1 44 ? 20.752  -7.178  -30.127 1.00 26.59  ? 43  PHE B CD1 1 
ATOM   1077 C CD2 . PHE B 1 44 ? 22.175  -7.064  -28.193 1.00 33.16  ? 43  PHE B CD2 1 
ATOM   1078 C CE1 . PHE B 1 44 ? 19.880  -6.257  -29.525 1.00 30.81  ? 43  PHE B CE1 1 
ATOM   1079 C CE2 . PHE B 1 44 ? 21.320  -6.133  -27.599 1.00 29.66  ? 43  PHE B CE2 1 
ATOM   1080 C CZ  . PHE B 1 44 ? 20.186  -5.734  -28.282 1.00 33.32  ? 43  PHE B CZ  1 
ATOM   1081 N N   . PHE B 1 45 ? 20.494  -10.730 -28.740 1.00 25.04  ? 44  PHE B N   1 
ATOM   1082 C CA  . PHE B 1 45 ? 19.092  -11.092 -28.840 1.00 22.25  ? 44  PHE B CA  1 
ATOM   1083 C C   . PHE B 1 45 ? 18.197  -9.877  -28.710 1.00 23.63  ? 44  PHE B C   1 
ATOM   1084 O O   . PHE B 1 45 ? 18.237  -9.138  -27.705 1.00 26.71  ? 44  PHE B O   1 
ATOM   1085 C CB  . PHE B 1 45 ? 18.682  -12.119 -27.778 1.00 22.23  ? 44  PHE B CB  1 
ATOM   1086 C CG  . PHE B 1 45 ? 19.392  -13.456 -27.911 1.00 22.45  ? 44  PHE B CG  1 
ATOM   1087 C CD1 . PHE B 1 45 ? 20.648  -13.661 -27.351 1.00 26.31  ? 44  PHE B CD1 1 
ATOM   1088 C CD2 . PHE B 1 45 ? 18.841  -14.494 -28.661 1.00 22.65  ? 44  PHE B CD2 1 
ATOM   1089 C CE1 . PHE B 1 45 ? 21.307  -14.880 -27.498 1.00 33.54  ? 44  PHE B CE1 1 
ATOM   1090 C CE2 . PHE B 1 45 ? 19.488  -15.722 -28.768 1.00 29.06  ? 44  PHE B CE2 1 
ATOM   1091 C CZ  . PHE B 1 45 ? 20.740  -15.904 -28.236 1.00 28.48  ? 44  PHE B CZ  1 
ATOM   1092 N N   . PHE B 1 46 ? 17.338  -9.688  -29.720 1.00 23.50  ? 45  PHE B N   1 
ATOM   1093 C CA  . PHE B 1 46 ? 16.419  -8.571  -29.686 1.00 22.43  ? 45  PHE B CA  1 
ATOM   1094 C C   . PHE B 1 46 ? 15.399  -8.771  -28.551 1.00 26.54  ? 45  PHE B C   1 
ATOM   1095 O O   . PHE B 1 46 ? 15.182  -9.888  -28.088 1.00 24.42  ? 45  PHE B O   1 
ATOM   1096 C CB  . PHE B 1 46 ? 15.701  -8.337  -31.010 1.00 22.39  ? 45  PHE B CB  1 
ATOM   1097 C CG  . PHE B 1 46 ? 16.636  -7.889  -32.125 1.00 27.63  ? 45  PHE B CG  1 
ATOM   1098 C CD1 . PHE B 1 46 ? 17.123  -6.579  -32.137 1.00 27.90  ? 45  PHE B CD1 1 
ATOM   1099 C CD2 . PHE B 1 46 ? 17.003  -8.753  -33.164 1.00 23.77  ? 45  PHE B CD2 1 
ATOM   1100 C CE1 . PHE B 1 46 ? 17.982  -6.159  -33.164 1.00 29.27  ? 45  PHE B CE1 1 
ATOM   1101 C CE2 . PHE B 1 46 ? 17.828  -8.307  -34.217 1.00 25.26  ? 45  PHE B CE2 1 
ATOM   1102 C CZ  . PHE B 1 46 ? 18.304  -7.001  -34.209 1.00 26.38  ? 45  PHE B CZ  1 
ATOM   1103 N N   . GLY B 1 47 ? 14.805  -7.659  -28.113 1.00 26.41  ? 46  GLY B N   1 
ATOM   1104 C CA  . GLY B 1 47 ? 13.779  -7.681  -27.055 1.00 28.04  ? 46  GLY B CA  1 
ATOM   1105 C C   . GLY B 1 47 ? 14.428  -7.784  -25.670 1.00 30.62  ? 46  GLY B C   1 
ATOM   1106 O O   . GLY B 1 47 ? 14.230  -6.910  -24.825 1.00 30.90  ? 46  GLY B O   1 
ATOM   1107 N N   . THR B 1 48 ? 15.133  -8.886  -25.404 1.00 28.70  ? 47  THR B N   1 
ATOM   1108 C CA  . THR B 1 48 ? 15.773  -9.104  -24.119 1.00 28.42  ? 47  THR B CA  1 
ATOM   1109 C C   . THR B 1 48 ? 17.045  -8.269  -24.025 1.00 29.62  ? 47  THR B C   1 
ATOM   1110 O O   . THR B 1 48 ? 17.480  -7.911  -22.924 1.00 29.15  ? 47  THR B O   1 
ATOM   1111 C CB  . THR B 1 48 ? 16.120  -10.572 -23.860 1.00 27.80  ? 47  THR B CB  1 
ATOM   1112 O OG1 . THR B 1 48 ? 17.062  -11.017 -24.844 1.00 25.62  ? 47  THR B OG1 1 
ATOM   1113 C CG2 . THR B 1 48 ? 14.884  -11.454 -23.798 1.00 26.02  ? 47  THR B CG2 1 
ATOM   1114 N N   . HIS B 1 49 ? 17.670  -8.048  -25.188 1.00 28.77  ? 48  HIS B N   1 
ATOM   1115 C CA  . HIS B 1 49 ? 18.950  -7.358  -25.296 1.00 29.03  ? 48  HIS B CA  1 
ATOM   1116 C C   . HIS B 1 49 ? 20.097  -8.100  -24.620 1.00 30.00  ? 48  HIS B C   1 
ATOM   1117 O O   . HIS B 1 49 ? 21.071  -7.459  -24.240 1.00 35.64  ? 48  HIS B O   1 
ATOM   1118 C CB  . HIS B 1 49 ? 18.836  -5.869  -24.901 1.00 27.63  ? 48  HIS B CB  1 
ATOM   1119 C CG  . HIS B 1 49 ? 17.666  -5.160  -25.480 1.00 29.88  ? 48  HIS B CG  1 
ATOM   1120 N ND1 . HIS B 1 49 ? 16.889  -4.313  -24.718 1.00 34.04  ? 48  HIS B ND1 1 
ATOM   1121 C CD2 . HIS B 1 49 ? 17.071  -5.206  -26.690 1.00 27.01  ? 48  HIS B CD2 1 
ATOM   1122 C CE1 . HIS B 1 49 ? 15.870  -3.868  -25.445 1.00 36.05  ? 48  HIS B CE1 1 
ATOM   1123 N NE2 . HIS B 1 49 ? 15.978  -4.373  -26.674 1.00 32.20  ? 48  HIS B NE2 1 
ATOM   1124 N N   . GLU B 1 50 ? 19.994  -9.418  -24.435 1.00 27.70  ? 49  GLU B N   1 
ATOM   1125 C CA  . GLU B 1 50 ? 21.060  -10.240 -23.891 1.00 32.91  ? 49  GLU B CA  1 
ATOM   1126 C C   . GLU B 1 50 ? 21.970  -10.710 -25.026 1.00 32.87  ? 49  GLU B C   1 
ATOM   1127 O O   . GLU B 1 50 ? 21.644  -10.520 -26.195 1.00 32.17  ? 49  GLU B O   1 
ATOM   1128 C CB  . GLU B 1 50 ? 20.471  -11.526 -23.316 1.00 39.47  ? 49  GLU B CB  1 
ATOM   1129 C CG  . GLU B 1 50 ? 19.522  -11.266 -22.153 1.00 41.90  ? 49  GLU B CG  1 
ATOM   1130 C CD  . GLU B 1 50 ? 20.089  -11.557 -20.779 1.00 46.41  ? 49  GLU B CD  1 
ATOM   1131 O OE1 . GLU B 1 50 ? 21.288  -11.863 -20.644 1.00 50.35  ? 49  GLU B OE1 1 
ATOM   1132 O OE2 . GLU B 1 50 ? 19.273  -11.540 -19.839 1.00 45.37  ? 49  GLU B OE2 1 
ATOM   1133 N N   . THR B 1 51 ? 23.119  -11.274 -24.656 1.00 31.89  ? 50  THR B N   1 
ATOM   1134 C CA  . THR B 1 51 ? 24.128  -11.740 -25.603 1.00 33.31  ? 50  THR B CA  1 
ATOM   1135 C C   . THR B 1 51 ? 24.575  -13.145 -25.218 1.00 34.82  ? 50  THR B C   1 
ATOM   1136 O O   . THR B 1 51 ? 24.537  -13.561 -24.061 1.00 33.78  ? 50  THR B O   1 
ATOM   1137 C CB  . THR B 1 51 ? 25.326  -10.784 -25.653 1.00 36.61  ? 50  THR B CB  1 
ATOM   1138 O OG1 . THR B 1 51 ? 25.869  -10.927 -24.339 1.00 41.15  ? 50  THR B OG1 1 
ATOM   1139 C CG2 . THR B 1 51 ? 24.946  -9.345  -25.969 1.00 36.33  ? 50  THR B CG2 1 
ATOM   1140 N N   . ALA B 1 52 ? 25.021  -13.894 -26.223 1.00 33.05  ? 51  ALA B N   1 
ATOM   1141 C CA  . ALA B 1 52 ? 25.629  -15.192 -26.008 1.00 34.56  ? 51  ALA B CA  1 
ATOM   1142 C C   . ALA B 1 52 ? 26.493  -15.474 -27.233 1.00 33.98  ? 51  ALA B C   1 
ATOM   1143 O O   . ALA B 1 52 ? 26.429  -14.724 -28.209 1.00 35.80  ? 51  ALA B O   1 
ATOM   1144 C CB  . ALA B 1 52 ? 24.576  -16.245 -25.823 1.00 34.11  ? 51  ALA B CB  1 
ATOM   1145 N N   . PHE B 1 53 ? 27.306  -16.526 -27.146 1.00 35.79  ? 52  PHE B N   1 
ATOM   1146 C CA  . PHE B 1 53 ? 28.078  -16.985 -28.291 1.00 35.67  ? 52  PHE B CA  1 
ATOM   1147 C C   . PHE B 1 53 ? 27.434  -18.265 -28.835 1.00 35.47  ? 52  PHE B C   1 
ATOM   1148 O O   . PHE B 1 53 ? 27.231  -19.219 -28.093 1.00 37.71  ? 52  PHE B O   1 
ATOM   1149 C CB  . PHE B 1 53 ? 29.553  -17.263 -27.957 1.00 38.06  ? 52  PHE B CB  1 
ATOM   1150 C CG  . PHE B 1 53 ? 30.310  -16.050 -27.454 1.00 40.39  ? 52  PHE B CG  1 
ATOM   1151 C CD1 . PHE B 1 53 ? 30.532  -14.965 -28.291 1.00 46.88  ? 52  PHE B CD1 1 
ATOM   1152 C CD2 . PHE B 1 53 ? 30.790  -15.998 -26.152 1.00 48.80  ? 52  PHE B CD2 1 
ATOM   1153 C CE1 . PHE B 1 53 ? 31.213  -13.848 -27.835 1.00 50.01  ? 52  PHE B CE1 1 
ATOM   1154 C CE2 . PHE B 1 53 ? 31.476  -14.879 -25.700 1.00 49.14  ? 52  PHE B CE2 1 
ATOM   1155 C CZ  . PHE B 1 53 ? 31.675  -13.809 -26.534 1.00 47.04  ? 52  PHE B CZ  1 
ATOM   1156 N N   . LEU B 1 54 ? 27.123  -18.287 -30.141 1.00 33.01  ? 53  LEU B N   1 
ATOM   1157 C CA  . LEU B 1 54 ? 26.490  -19.445 -30.755 1.00 33.70  ? 53  LEU B CA  1 
ATOM   1158 C C   . LEU B 1 54 ? 27.204  -19.772 -32.066 1.00 31.81  ? 53  LEU B C   1 
ATOM   1159 O O   . LEU B 1 54 ? 27.742  -18.880 -32.732 1.00 32.52  ? 53  LEU B O   1 
ATOM   1160 C CB  . LEU B 1 54 ? 25.016  -19.229 -31.095 1.00 30.84  ? 53  LEU B CB  1 
ATOM   1161 C CG  . LEU B 1 54 ? 24.039  -19.043 -29.928 1.00 32.37  ? 53  LEU B CG  1 
ATOM   1162 C CD1 . LEU B 1 54 ? 22.727  -18.628 -30.575 1.00 32.94  ? 53  LEU B CD1 1 
ATOM   1163 C CD2 . LEU B 1 54 ? 23.913  -20.381 -29.214 1.00 33.26  ? 53  LEU B CD2 1 
ATOM   1164 N N   . GLY B 1 55 ? 27.083  -21.045 -32.449 1.00 32.51  ? 54  GLY B N   1 
ATOM   1165 C CA  . GLY B 1 55 ? 27.677  -21.549 -33.673 1.00 31.64  ? 54  GLY B CA  1 
ATOM   1166 C C   . GLY B 1 55 ? 26.619  -21.638 -34.765 1.00 31.08  ? 54  GLY B C   1 
ATOM   1167 O O   . GLY B 1 55 ? 25.422  -21.614 -34.488 1.00 29.67  ? 54  GLY B O   1 
ATOM   1168 N N   . PRO B 1 56 ? 27.016  -21.784 -36.047 1.00 28.66  ? 55  PRO B N   1 
ATOM   1169 C CA  . PRO B 1 56 ? 26.039  -21.790 -37.134 1.00 28.85  ? 55  PRO B CA  1 
ATOM   1170 C C   . PRO B 1 56 ? 24.874  -22.769 -37.063 1.00 25.74  ? 55  PRO B C   1 
ATOM   1171 O O   . PRO B 1 56 ? 23.833  -22.490 -37.629 1.00 27.85  ? 55  PRO B O   1 
ATOM   1172 C CB  . PRO B 1 56 ? 26.871  -21.969 -38.416 1.00 32.61  ? 55  PRO B CB  1 
ATOM   1173 C CG  . PRO B 1 56 ? 28.320  -21.785 -38.005 1.00 32.15  ? 55  PRO B CG  1 
ATOM   1174 C CD  . PRO B 1 56 ? 28.414  -21.888 -36.498 1.00 33.44  ? 55  PRO B CD  1 
ATOM   1175 N N   . LYS B 1 57 ? 25.035  -23.918 -36.372 1.00 30.02  ? 56  LYS B N   1 
ATOM   1176 C CA  . LYS B 1 57 ? 23.970  -24.918 -36.354 1.00 29.37  ? 56  LYS B CA  1 
ATOM   1177 C C   . LYS B 1 57 ? 22.742  -24.324 -35.673 1.00 28.62  ? 56  LYS B C   1 
ATOM   1178 O O   . LYS B 1 57 ? 21.627  -24.789 -35.892 1.00 26.39  ? 56  LYS B O   1 
ATOM   1179 C CB  . LYS B 1 57 ? 24.369  -26.213 -35.627 1.00 32.14  ? 56  LYS B CB  1 
ATOM   1180 C CG  . LYS B 1 57 ? 24.664  -26.055 -34.160 1.00 34.94  ? 56  LYS B CG  1 
ATOM   1181 C CD  . LYS B 1 57 ? 24.729  -27.413 -33.468 1.00 37.32  ? 56  LYS B CD  1 
ATOM   1182 C CE  . LYS B 1 57 ? 24.846  -27.289 -31.978 1.00 43.25  ? 56  LYS B CE  1 
ATOM   1183 N NZ  . LYS B 1 57 ? 23.577  -26.925 -31.337 1.00 49.37  ? 56  LYS B NZ  1 
ATOM   1184 N N   . ASP B 1 58 ? 22.977  -23.261 -34.876 1.00 28.86  ? 57  ASP B N   1 
ATOM   1185 C CA  . ASP B 1 58 ? 21.913  -22.633 -34.112 1.00 29.70  ? 57  ASP B CA  1 
ATOM   1186 C C   . ASP B 1 58 ? 21.506  -21.280 -34.688 1.00 27.69  ? 57  ASP B C   1 
ATOM   1187 O O   . ASP B 1 58 ? 20.721  -20.552 -34.053 1.00 27.04  ? 57  ASP B O   1 
ATOM   1188 C CB  . ASP B 1 58 ? 22.299  -22.474 -32.649 1.00 27.49  ? 57  ASP B CB  1 
ATOM   1189 C CG  . ASP B 1 58 ? 22.398  -23.792 -31.897 1.00 38.02  ? 57  ASP B CG  1 
ATOM   1190 O OD1 . ASP B 1 58 ? 21.478  -24.597 -32.053 1.00 33.86  ? 57  ASP B OD1 1 
ATOM   1191 O OD2 . ASP B 1 58 ? 23.387  -23.983 -31.169 1.00 38.74  ? 57  ASP B OD2 1 
ATOM   1192 N N   . LEU B 1 59 ? 21.956  -20.988 -35.923 1.00 25.17  ? 58  LEU B N   1 
ATOM   1193 C CA  . LEU B 1 59 ? 21.735  -19.661 -36.493 1.00 24.67  ? 58  LEU B CA  1 
ATOM   1194 C C   . LEU B 1 59 ? 21.020  -19.794 -37.823 1.00 26.38  ? 58  LEU B C   1 
ATOM   1195 O O   . LEU B 1 59 ? 21.512  -20.459 -38.739 1.00 28.68  ? 58  LEU B O   1 
ATOM   1196 C CB  . LEU B 1 59 ? 23.047  -18.908 -36.685 1.00 28.38  ? 58  LEU B CB  1 
ATOM   1197 C CG  . LEU B 1 59 ? 23.826  -18.672 -35.397 1.00 29.29  ? 58  LEU B CG  1 
ATOM   1198 C CD1 . LEU B 1 59 ? 25.190  -18.060 -35.674 1.00 28.90  ? 58  LEU B CD1 1 
ATOM   1199 C CD2 . LEU B 1 59 ? 22.988  -17.792 -34.453 1.00 27.13  ? 58  LEU B CD2 1 
ATOM   1200 N N   . PHE B 1 60 ? 19.843  -19.199 -37.881 1.00 23.48  ? 59  PHE B N   1 
ATOM   1201 C CA  . PHE B 1 60 ? 18.938  -19.356 -39.004 1.00 23.73  ? 59  PHE B CA  1 
ATOM   1202 C C   . PHE B 1 60 ? 18.763  -17.997 -39.672 1.00 26.59  ? 59  PHE B C   1 
ATOM   1203 O O   . PHE B 1 60 ? 18.155  -17.084 -39.116 1.00 25.27  ? 59  PHE B O   1 
ATOM   1204 C CB  . PHE B 1 60 ? 17.602  -19.852 -38.439 1.00 23.21  ? 59  PHE B CB  1 
ATOM   1205 C CG  . PHE B 1 60 ? 17.668  -21.275 -37.885 1.00 23.88  ? 59  PHE B CG  1 
ATOM   1206 C CD1 . PHE B 1 60 ? 18.117  -21.498 -36.574 1.00 26.86  ? 59  PHE B CD1 1 
ATOM   1207 C CD2 . PHE B 1 60 ? 17.227  -22.358 -38.650 1.00 25.81  ? 59  PHE B CD2 1 
ATOM   1208 C CE1 . PHE B 1 60 ? 18.207  -22.792 -36.055 1.00 26.33  ? 59  PHE B CE1 1 
ATOM   1209 C CE2 . PHE B 1 60 ? 17.252  -23.657 -38.090 1.00 25.14  ? 59  PHE B CE2 1 
ATOM   1210 C CZ  . PHE B 1 60 ? 17.781  -23.864 -36.828 1.00 27.07  ? 59  PHE B CZ  1 
ATOM   1211 N N   . PRO B 1 61 ? 19.307  -17.804 -40.902 1.00 29.02  ? 60  PRO B N   1 
ATOM   1212 C CA  . PRO B 1 61 ? 19.049  -16.561 -41.639 1.00 29.63  ? 60  PRO B CA  1 
ATOM   1213 C C   . PRO B 1 61 ? 17.611  -16.041 -41.604 1.00 26.77  ? 60  PRO B C   1 
ATOM   1214 O O   . PRO B 1 61 ? 16.619  -16.735 -41.868 1.00 28.10  ? 60  PRO B O   1 
ATOM   1215 C CB  . PRO B 1 61 ? 19.678  -16.839 -43.045 1.00 25.94  ? 60  PRO B CB  1 
ATOM   1216 C CG  . PRO B 1 61 ? 20.828  -17.803 -42.741 1.00 32.45  ? 60  PRO B CG  1 
ATOM   1217 C CD  . PRO B 1 61 ? 20.315  -18.675 -41.547 1.00 32.46  ? 60  PRO B CD  1 
ATOM   1218 N N   . TYR B 1 62 ? 17.463  -14.748 -41.222 1.00 26.89  ? 61  TYR B N   1 
ATOM   1219 C CA  . TYR B 1 62 ? 16.156  -14.224 -40.884 1.00 25.73  ? 61  TYR B CA  1 
ATOM   1220 C C   . TYR B 1 62 ? 15.155  -14.214 -42.037 1.00 28.87  ? 61  TYR B C   1 
ATOM   1221 O O   . TYR B 1 62 ? 14.007  -14.605 -41.853 1.00 29.93  ? 61  TYR B O   1 
ATOM   1222 C CB  . TYR B 1 62 ? 16.310  -12.797 -40.338 1.00 30.62  ? 61  TYR B CB  1 
ATOM   1223 C CG  . TYR B 1 62 ? 14.993  -12.069 -40.139 1.00 32.41  ? 61  TYR B CG  1 
ATOM   1224 C CD1 . TYR B 1 62 ? 14.230  -12.291 -39.005 1.00 31.26  ? 61  TYR B CD1 1 
ATOM   1225 C CD2 . TYR B 1 62 ? 14.599  -11.052 -40.999 1.00 36.05  ? 61  TYR B CD2 1 
ATOM   1226 C CE1 . TYR B 1 62 ? 13.045  -11.611 -38.790 1.00 32.74  ? 61  TYR B CE1 1 
ATOM   1227 C CE2 . TYR B 1 62 ? 13.419  -10.354 -40.793 1.00 37.79  ? 61  TYR B CE2 1 
ATOM   1228 C CZ  . TYR B 1 62 ? 12.664  -10.614 -39.668 1.00 35.65  ? 61  TYR B CZ  1 
ATOM   1229 O OH  . TYR B 1 62 ? 11.533  -9.904  -39.461 1.00 38.72  ? 61  TYR B OH  1 
ATOM   1230 N N   . ASP B 1 63 ? 15.601  -13.800 -43.238 1.00 37.92  ? 62  ASP B N   1 
ATOM   1231 C CA  . ASP B 1 63 ? 14.698  -13.741 -44.382 1.00 41.56  ? 62  ASP B CA  1 
ATOM   1232 C C   . ASP B 1 63 ? 14.170  -15.134 -44.743 1.00 36.65  ? 62  ASP B C   1 
ATOM   1233 O O   . ASP B 1 63 ? 12.975  -15.288 -44.971 1.00 39.55  ? 62  ASP B O   1 
ATOM   1234 C CB  . ASP B 1 63 ? 15.253  -12.927 -45.543 1.00 46.56  ? 62  ASP B CB  1 
ATOM   1235 C CG  . ASP B 1 63 ? 15.254  -11.414 -45.353 1.00 64.95  ? 62  ASP B CG  1 
ATOM   1236 O OD1 . ASP B 1 63 ? 14.305  -10.880 -44.713 1.00 61.22  ? 62  ASP B OD1 1 
ATOM   1237 O OD2 . ASP B 1 63 ? 16.197  -10.765 -45.873 1.00 75.98  ? 62  ASP B OD2 1 
ATOM   1238 N N   . LYS B 1 64 ? 15.055  -16.139 -44.747 1.00 37.90  ? 63  LYS B N   1 
ATOM   1239 C CA  . LYS B 1 64 ? 14.658  -17.510 -45.044 1.00 36.62  ? 63  LYS B CA  1 
ATOM   1240 C C   . LYS B 1 64 ? 13.614  -18.020 -44.035 1.00 37.64  ? 63  LYS B C   1 
ATOM   1241 O O   . LYS B 1 64 ? 12.660  -18.698 -44.398 1.00 40.29  ? 63  LYS B O   1 
ATOM   1242 C CB  . LYS B 1 64 ? 15.905  -18.396 -45.131 1.00 39.16  ? 63  LYS B CB  1 
ATOM   1243 C CG  . LYS B 1 64 ? 15.591  -19.853 -45.530 1.00 36.37  ? 63  LYS B CG  1 
ATOM   1244 C CD  . LYS B 1 64 ? 16.798  -20.728 -45.849 1.00 40.84  ? 63  LYS B CD  1 
ATOM   1245 C CE  . LYS B 1 64 ? 16.502  -22.229 -45.733 1.00 38.62  ? 63  LYS B CE  1 
ATOM   1246 N NZ  . LYS B 1 64 ? 15.359  -22.643 -46.549 1.00 43.90  ? 63  LYS B NZ  1 
ATOM   1247 N N   . SER B 1 65 ? 13.789  -17.709 -42.749 1.00 35.18  ? 64  SER B N   1 
ATOM   1248 C CA  . SER B 1 65 ? 13.095  -18.487 -41.721 1.00 33.27  ? 64  SER B CA  1 
ATOM   1249 C C   . SER B 1 65 ? 12.007  -17.693 -40.974 1.00 31.31  ? 64  SER B C   1 
ATOM   1250 O O   . SER B 1 65 ? 11.358  -18.222 -40.069 1.00 31.35  ? 64  SER B O   1 
ATOM   1251 C CB  . SER B 1 65 ? 14.133  -19.018 -40.792 1.00 36.58  ? 64  SER B CB  1 
ATOM   1252 O OG  . SER B 1 65 ? 14.825  -17.919 -40.228 1.00 43.07  ? 64  SER B OG  1 
ATOM   1253 N N   . LYS B 1 66 ? 11.746  -16.441 -41.387 1.00 34.46  ? 65  LYS B N   1 
ATOM   1254 C CA  . LYS B 1 66 ? 10.847  -15.553 -40.655 1.00 37.62  ? 65  LYS B CA  1 
ATOM   1255 C C   . LYS B 1 66 ? 9.411   -16.051 -40.652 1.00 39.11  ? 65  LYS B C   1 
ATOM   1256 O O   . LYS B 1 66 ? 8.698   -15.828 -39.684 1.00 38.83  ? 65  LYS B O   1 
ATOM   1257 C CB  . LYS B 1 66 ? 10.826  -14.071 -41.061 1.00 38.06  ? 65  LYS B CB  1 
ATOM   1258 C CG  . LYS B 1 66 ? 10.771  -13.869 -42.574 1.00 37.99  ? 65  LYS B CG  1 
ATOM   1259 C CD  . LYS B 1 66 ? 10.580  -12.448 -43.099 1.00 52.65  ? 65  LYS B CD  1 
ATOM   1260 C CE  . LYS B 1 66 ? 10.524  -12.412 -44.602 1.00 54.95  ? 65  LYS B CE  1 
ATOM   1261 N NZ  . LYS B 1 66 ? 9.420   -13.210 -45.155 1.00 58.47  ? 65  LYS B NZ  1 
ATOM   1262 N N   . ASP B 1 67 ? 8.951   -16.722 -41.711 1.00 40.81  ? 66  ASP B N   1 
ATOM   1263 C CA  . ASP B 1 67 ? 7.554   -17.131 -41.598 1.00 46.41  ? 66  ASP B CA  1 
ATOM   1264 C C   . ASP B 1 67 ? 7.405   -18.362 -40.703 1.00 44.30  ? 66  ASP B C   1 
ATOM   1265 O O   . ASP B 1 67 ? 6.337   -18.590 -40.132 1.00 43.57  ? 66  ASP B O   1 
ATOM   1266 C CB  . ASP B 1 67 ? 6.756   -17.051 -42.892 1.00 63.13  ? 66  ASP B CB  1 
ATOM   1267 C CG  . ASP B 1 67 ? 7.451   -17.559 -44.145 1.00 75.54  ? 66  ASP B CG  1 
ATOM   1268 O OD1 . ASP B 1 67 ? 6.885   -17.367 -45.250 1.00 76.83  ? 66  ASP B OD1 1 
ATOM   1269 O OD2 . ASP B 1 67 ? 8.550   -18.134 -44.001 1.00 81.12  ? 66  ASP B OD2 1 
ATOM   1270 N N   . LYS B 1 68 ? 8.495   -19.115 -40.529 1.00 38.55  ? 67  LYS B N   1 
ATOM   1271 C CA  . LYS B 1 68 ? 8.487   -20.270 -39.642 1.00 33.17  ? 67  LYS B CA  1 
ATOM   1272 C C   . LYS B 1 68 ? 8.618   -19.831 -38.183 1.00 34.27  ? 67  LYS B C   1 
ATOM   1273 O O   . LYS B 1 68 ? 7.854   -20.288 -37.310 1.00 34.38  ? 67  LYS B O   1 
ATOM   1274 C CB  . LYS B 1 68 ? 9.582   -21.228 -40.125 1.00 38.02  ? 67  LYS B CB  1 
ATOM   1275 C CG  . LYS B 1 68 ? 9.678   -22.561 -39.421 1.00 47.68  ? 67  LYS B CG  1 
ATOM   1276 C CD  . LYS B 1 68 ? 10.190  -23.570 -40.452 1.00 58.52  ? 67  LYS B CD  1 
ATOM   1277 C CE  . LYS B 1 68 ? 10.764  -24.826 -39.868 1.00 64.42  ? 67  LYS B CE  1 
ATOM   1278 N NZ  . LYS B 1 68 ? 9.853   -25.534 -38.962 1.00 62.22  ? 67  LYS B NZ  1 
ATOM   1279 N N   . TYR B 1 69 ? 9.589   -18.943 -37.904 1.00 31.37  ? 68  TYR B N   1 
ATOM   1280 C CA  . TYR B 1 69 ? 9.929   -18.712 -36.502 1.00 25.97  ? 68  TYR B CA  1 
ATOM   1281 C C   . TYR B 1 69 ? 9.371   -17.391 -35.991 1.00 32.88  ? 68  TYR B C   1 
ATOM   1282 O O   . TYR B 1 69 ? 9.458   -17.131 -34.785 1.00 31.24  ? 68  TYR B O   1 
ATOM   1283 C CB  . TYR B 1 69 ? 11.445  -18.702 -36.341 1.00 26.29  ? 68  TYR B CB  1 
ATOM   1284 C CG  . TYR B 1 69 ? 12.026  -20.077 -36.670 1.00 29.60  ? 68  TYR B CG  1 
ATOM   1285 C CD1 . TYR B 1 69 ? 11.522  -21.249 -36.105 1.00 29.07  ? 68  TYR B CD1 1 
ATOM   1286 C CD2 . TYR B 1 69 ? 13.110  -20.196 -37.529 1.00 30.58  ? 68  TYR B CD2 1 
ATOM   1287 C CE1 . TYR B 1 69 ? 12.075  -22.497 -36.385 1.00 32.37  ? 68  TYR B CE1 1 
ATOM   1288 C CE2 . TYR B 1 69 ? 13.669  -21.432 -37.815 1.00 33.33  ? 68  TYR B CE2 1 
ATOM   1289 C CZ  . TYR B 1 69 ? 13.140  -22.590 -37.264 1.00 34.74  ? 68  TYR B CZ  1 
ATOM   1290 O OH  . TYR B 1 69 ? 13.711  -23.795 -37.569 1.00 34.84  ? 68  TYR B OH  1 
ATOM   1291 N N   . GLY B 1 70 ? 8.857   -16.561 -36.906 1.00 32.87  ? 69  GLY B N   1 
ATOM   1292 C CA  . GLY B 1 70 ? 8.554   -15.164 -36.625 1.00 36.55  ? 69  GLY B CA  1 
ATOM   1293 C C   . GLY B 1 70 ? 7.162   -14.918 -36.037 1.00 38.33  ? 69  GLY B C   1 
ATOM   1294 O O   . GLY B 1 70 ? 6.594   -13.850 -36.259 1.00 42.76  ? 69  GLY B O   1 
ATOM   1295 N N   . LYS B 1 71 ? 6.643   -15.857 -35.245 1.00 38.02  ? 70  LYS B N   1 
ATOM   1296 C CA  . LYS B 1 71 ? 5.286   -15.739 -34.749 1.00 44.73  ? 70  LYS B CA  1 
ATOM   1297 C C   . LYS B 1 71 ? 5.341   -15.382 -33.273 1.00 45.09  ? 70  LYS B C   1 
ATOM   1298 O O   . LYS B 1 71 ? 6.180   -15.926 -32.557 1.00 39.01  ? 70  LYS B O   1 
ATOM   1299 C CB  . LYS B 1 71 ? 4.525   -17.061 -34.896 1.00 44.89  ? 70  LYS B CB  1 
ATOM   1300 C CG  . LYS B 1 71 ? 4.290   -17.400 -36.376 1.00 50.25  ? 70  LYS B CG  1 
ATOM   1301 C CD  . LYS B 1 71 ? 3.814   -18.826 -36.617 1.00 52.92  ? 70  LYS B CD  1 
ATOM   1302 C CE  . LYS B 1 71 ? 3.260   -19.010 -37.997 1.00 62.63  ? 70  LYS B CE  1 
ATOM   1303 N NZ  . LYS B 1 71 ? 4.163   -18.478 -39.020 1.00 70.89  ? 70  LYS B NZ  1 
ATOM   1304 N N   . PRO B 1 72 ? 4.443   -14.486 -32.788 1.00 41.01  ? 71  PRO B N   1 
ATOM   1305 C CA  . PRO B 1 72 ? 4.458   -14.064 -31.386 1.00 40.68  ? 71  PRO B CA  1 
ATOM   1306 C C   . PRO B 1 72 ? 4.250   -15.241 -30.435 1.00 41.29  ? 71  PRO B C   1 
ATOM   1307 O O   . PRO B 1 72 ? 3.658   -16.254 -30.800 1.00 36.26  ? 71  PRO B O   1 
ATOM   1308 C CB  . PRO B 1 72 ? 3.337   -12.995 -31.271 1.00 41.76  ? 71  PRO B CB  1 
ATOM   1309 C CG  . PRO B 1 72 ? 3.013   -12.631 -32.703 1.00 46.87  ? 71  PRO B CG  1 
ATOM   1310 C CD  . PRO B 1 72 ? 3.381   -13.829 -33.572 1.00 44.68  ? 71  PRO B CD  1 
ATOM   1311 N N   . ASN B 1 73 ? 4.775   -15.115 -29.208 1.00 39.10  ? 72  ASN B N   1 
ATOM   1312 C CA  . ASN B 1 73 ? 4.539   -16.139 -28.202 1.00 35.83  ? 72  ASN B CA  1 
ATOM   1313 C C   . ASN B 1 73 ? 4.502   -15.460 -26.823 1.00 38.87  ? 72  ASN B C   1 
ATOM   1314 O O   . ASN B 1 73 ? 4.596   -14.232 -26.718 1.00 44.07  ? 72  ASN B O   1 
ATOM   1315 C CB  . ASN B 1 73 ? 5.563   -17.272 -28.272 1.00 36.12  ? 72  ASN B CB  1 
ATOM   1316 C CG  . ASN B 1 73 ? 6.985   -16.811 -28.042 1.00 34.11  ? 72  ASN B CG  1 
ATOM   1317 O OD1 . ASN B 1 73 ? 7.235   -16.058 -27.089 1.00 34.09  ? 72  ASN B OD1 1 
ATOM   1318 N ND2 . ASN B 1 73 ? 7.920   -17.210 -28.911 1.00 27.88  ? 72  ASN B ND2 1 
ATOM   1319 N N   . LYS B 1 74 ? 4.474   -16.275 -25.768 1.00 39.48  ? 73  LYS B N   1 
ATOM   1320 C CA  . LYS B 1 74 ? 4.302   -15.715 -24.428 1.00 42.76  ? 73  LYS B CA  1 
ATOM   1321 C C   . LYS B 1 74 ? 5.628   -15.579 -23.662 1.00 42.20  ? 73  LYS B C   1 
ATOM   1322 O O   . LYS B 1 74 ? 5.612   -15.357 -22.446 1.00 35.74  ? 73  LYS B O   1 
ATOM   1323 C CB  . LYS B 1 74 ? 3.248   -16.553 -23.687 1.00 43.39  ? 73  LYS B CB  1 
ATOM   1324 N N   . ARG B 1 75 ? 6.776   -15.690 -24.356 1.00 29.85  ? 74  ARG B N   1 
ATOM   1325 C CA  . ARG B 1 75 ? 8.074   -15.517 -23.711 1.00 28.69  ? 74  ARG B CA  1 
ATOM   1326 C C   . ARG B 1 75 ? 8.375   -14.018 -23.566 1.00 28.19  ? 74  ARG B C   1 
ATOM   1327 O O   . ARG B 1 75 ? 8.195   -13.245 -24.510 1.00 31.60  ? 74  ARG B O   1 
ATOM   1328 C CB  . ARG B 1 75 ? 9.255   -16.251 -24.369 1.00 30.58  ? 74  ARG B CB  1 
ATOM   1329 C CG  . ARG B 1 75 ? 9.095   -17.757 -24.600 1.00 28.07  ? 74  ARG B CG  1 
ATOM   1330 C CD  . ARG B 1 75 ? 8.976   -18.546 -23.305 1.00 30.55  ? 74  ARG B CD  1 
ATOM   1331 N NE  . ARG B 1 75 ? 9.103   -19.987 -23.565 1.00 31.52  ? 74  ARG B NE  1 
ATOM   1332 C CZ  . ARG B 1 75 ? 10.251  -20.620 -23.400 1.00 29.18  ? 74  ARG B CZ  1 
ATOM   1333 N NH1 . ARG B 1 75 ? 11.321  -19.974 -22.959 1.00 36.03  ? 74  ARG B NH1 1 
ATOM   1334 N NH2 . ARG B 1 75 ? 10.346  -21.910 -23.697 1.00 31.41  ? 74  ARG B NH2 1 
ATOM   1335 N N   . LYS B 1 76 ? 8.831   -13.615 -22.358 1.00 26.64  ? 75  LYS B N   1 
ATOM   1336 C CA  . LYS B 1 76 ? 9.217   -12.244 -22.074 1.00 25.46  ? 75  LYS B CA  1 
ATOM   1337 C C   . LYS B 1 76 ? 10.282  -11.765 -23.073 1.00 23.42  ? 75  LYS B C   1 
ATOM   1338 O O   . LYS B 1 76 ? 11.364  -12.347 -23.119 1.00 26.12  ? 75  LYS B O   1 
ATOM   1339 C CB  . LYS B 1 76 ? 9.843   -12.243 -20.658 1.00 26.40  ? 75  LYS B CB  1 
ATOM   1340 C CG  . LYS B 1 76 ? 10.166  -10.819 -20.146 1.00 28.32  ? 75  LYS B CG  1 
ATOM   1341 C CD  . LYS B 1 76 ? 10.743  -10.735 -18.746 1.00 29.92  ? 75  LYS B CD  1 
ATOM   1342 C CE  . LYS B 1 76 ? 10.992  -9.294  -18.368 1.00 34.52  ? 75  LYS B CE  1 
ATOM   1343 N NZ  . LYS B 1 76 ? 11.320  -9.204  -16.936 1.00 38.85  ? 75  LYS B NZ  1 
ATOM   1344 N N   . GLY B 1 77 ? 9.993   -10.660 -23.753 1.00 25.27  ? 76  GLY B N   1 
ATOM   1345 C CA  . GLY B 1 77 ? 10.973  -10.028 -24.636 1.00 24.97  ? 76  GLY B CA  1 
ATOM   1346 C C   . GLY B 1 77 ? 10.700  -10.401 -26.092 1.00 27.48  ? 76  GLY B C   1 
ATOM   1347 O O   . GLY B 1 77 ? 11.256  -9.772  -27.004 1.00 26.56  ? 76  GLY B O   1 
ATOM   1348 N N   . PHE B 1 78 ? 9.894   -11.461 -26.331 1.00 25.52  ? 77  PHE B N   1 
ATOM   1349 C CA  . PHE B 1 78 ? 9.822   -12.003 -27.701 1.00 25.81  ? 77  PHE B CA  1 
ATOM   1350 C C   . PHE B 1 78 ? 9.124   -11.047 -28.661 1.00 29.17  ? 77  PHE B C   1 
ATOM   1351 O O   . PHE B 1 78 ? 9.626   -10.766 -29.763 1.00 27.66  ? 77  PHE B O   1 
ATOM   1352 C CB  . PHE B 1 78 ? 9.096   -13.348 -27.758 1.00 27.72  ? 77  PHE B CB  1 
ATOM   1353 C CG  . PHE B 1 78 ? 9.357   -14.069 -29.066 1.00 28.07  ? 77  PHE B CG  1 
ATOM   1354 C CD1 . PHE B 1 78 ? 10.495  -14.870 -29.187 1.00 24.65  ? 77  PHE B CD1 1 
ATOM   1355 C CD2 . PHE B 1 78 ? 8.420   -13.994 -30.091 1.00 31.60  ? 77  PHE B CD2 1 
ATOM   1356 C CE1 . PHE B 1 78 ? 10.746  -15.542 -30.383 1.00 25.68  ? 77  PHE B CE1 1 
ATOM   1357 C CE2 . PHE B 1 78 ? 8.666   -14.691 -31.275 1.00 32.37  ? 77  PHE B CE2 1 
ATOM   1358 C CZ  . PHE B 1 78 ? 9.820   -15.466 -31.385 1.00 27.62  ? 77  PHE B CZ  1 
ATOM   1359 N N   . ASN B 1 79 ? 7.934   -10.566 -28.290 1.00 26.99  ? 78  ASN B N   1 
ATOM   1360 C CA  . ASN B 1 79 ? 7.204   -9.694  -29.193 1.00 29.88  ? 78  ASN B CA  1 
ATOM   1361 C C   . ASN B 1 79 ? 7.940   -8.372  -29.391 1.00 29.17  ? 78  ASN B C   1 
ATOM   1362 O O   . ASN B 1 79 ? 7.917   -7.817  -30.505 1.00 28.70  ? 78  ASN B O   1 
ATOM   1363 C CB  . ASN B 1 79 ? 5.735   -9.572  -28.822 1.00 32.88  ? 78  ASN B CB  1 
ATOM   1364 C CG  . ASN B 1 79 ? 5.050   -10.920 -28.831 1.00 39.26  ? 78  ASN B CG  1 
ATOM   1365 O OD1 . ASN B 1 79 ? 5.598   -11.909 -29.345 1.00 41.08  ? 78  ASN B OD1 1 
ATOM   1366 N ND2 . ASN B 1 79 ? 3.890   -11.000 -28.198 1.00 38.03  ? 78  ASN B ND2 1 
ATOM   1367 N N   . GLU B 1 80 ? 8.654   -7.928  -28.357 1.00 27.87  ? 79  GLU B N   1 
ATOM   1368 C CA  . GLU B 1 80 ? 9.437   -6.704  -28.505 1.00 31.33  ? 79  GLU B CA  1 
ATOM   1369 C C   . GLU B 1 80 ? 10.606  -6.980  -29.460 1.00 26.21  ? 79  GLU B C   1 
ATOM   1370 O O   . GLU B 1 80 ? 10.904  -6.120  -30.283 1.00 26.32  ? 79  GLU B O   1 
ATOM   1371 C CB  . GLU B 1 80 ? 10.026  -6.165  -27.206 1.00 29.40  ? 79  GLU B CB  1 
ATOM   1372 C CG  . GLU B 1 80 ? 8.951   -5.597  -26.289 1.00 43.21  ? 79  GLU B CG  1 
ATOM   1373 N N   . GLY B 1 81 ? 11.214  -8.178  -29.346 1.00 25.15  ? 80  GLY B N   1 
ATOM   1374 C CA  . GLY B 1 81 ? 12.309  -8.615  -30.214 1.00 23.96  ? 80  GLY B CA  1 
ATOM   1375 C C   . GLY B 1 81 ? 11.852  -8.663  -31.662 1.00 26.45  ? 80  GLY B C   1 
ATOM   1376 O O   . GLY B 1 81 ? 12.604  -8.225  -32.548 1.00 23.81  ? 80  GLY B O   1 
ATOM   1377 N N   . LEU B 1 82 ? 10.614  -9.149  -31.883 1.00 23.39  ? 81  LEU B N   1 
ATOM   1378 C CA  . LEU B 1 82 ? 10.052  -9.138  -33.232 1.00 28.06  ? 81  LEU B CA  1 
ATOM   1379 C C   . LEU B 1 82 ? 9.929   -7.714  -33.765 1.00 29.38  ? 81  LEU B C   1 
ATOM   1380 O O   . LEU B 1 82 ? 10.213  -7.459  -34.942 1.00 27.72  ? 81  LEU B O   1 
ATOM   1381 C CB  . LEU B 1 82 ? 8.719   -9.885  -33.303 1.00 24.57  ? 81  LEU B CB  1 
ATOM   1382 C CG  . LEU B 1 82 ? 8.840   -11.404 -33.105 1.00 26.61  ? 81  LEU B CG  1 
ATOM   1383 C CD1 . LEU B 1 82 ? 7.444   -12.026 -33.123 1.00 26.87  ? 81  LEU B CD1 1 
ATOM   1384 C CD2 . LEU B 1 82 ? 9.755   -12.083 -34.134 1.00 23.81  ? 81  LEU B CD2 1 
ATOM   1385 N N   . TRP B 1 83 ? 9.489   -6.775  -32.922 1.00 25.99  ? 82  TRP B N   1 
ATOM   1386 C CA  . TRP B 1 83 ? 9.377   -5.384  -33.355 1.00 26.93  ? 82  TRP B CA  1 
ATOM   1387 C C   . TRP B 1 83 ? 10.756  -4.844  -33.722 1.00 27.32  ? 82  TRP B C   1 
ATOM   1388 O O   . TRP B 1 83 ? 10.877  -4.202  -34.764 1.00 28.46  ? 82  TRP B O   1 
ATOM   1389 C CB  . TRP B 1 83 ? 8.731   -4.503  -32.267 1.00 30.27  ? 82  TRP B CB  1 
ATOM   1390 C CG  . TRP B 1 83 ? 8.445   -3.100  -32.748 1.00 30.26  ? 82  TRP B CG  1 
ATOM   1391 C CD1 . TRP B 1 83 ? 7.298   -2.626  -33.321 1.00 33.37  ? 82  TRP B CD1 1 
ATOM   1392 C CD2 . TRP B 1 83 ? 9.385   -2.007  -32.739 1.00 34.43  ? 82  TRP B CD2 1 
ATOM   1393 N NE1 . TRP B 1 83 ? 7.455   -1.302  -33.647 1.00 35.66  ? 82  TRP B NE1 1 
ATOM   1394 C CE2 . TRP B 1 83 ? 8.722   -0.896  -33.305 1.00 35.19  ? 82  TRP B CE2 1 
ATOM   1395 C CE3 . TRP B 1 83 ? 10.715  -1.871  -32.299 1.00 32.12  ? 82  TRP B CE3 1 
ATOM   1396 C CZ2 . TRP B 1 83 ? 9.350   0.348   -33.426 1.00 35.48  ? 82  TRP B CZ2 1 
ATOM   1397 C CZ3 . TRP B 1 83 ? 11.335  -0.638  -32.414 1.00 33.45  ? 82  TRP B CZ3 1 
ATOM   1398 C CH2 . TRP B 1 83 ? 10.658  0.446   -32.982 1.00 34.09  ? 82  TRP B CH2 1 
ATOM   1399 N N   . GLU B 1 84 ? 11.760  -5.130  -32.888 1.00 25.62  ? 83  GLU B N   1 
ATOM   1400 C CA  . GLU B 1 84 ? 13.098  -4.596  -33.064 1.00 26.31  ? 83  GLU B CA  1 
ATOM   1401 C C   . GLU B 1 84 ? 13.731  -5.074  -34.375 1.00 28.74  ? 83  GLU B C   1 
ATOM   1402 O O   . GLU B 1 84 ? 14.322  -4.263  -35.105 1.00 26.50  ? 83  GLU B O   1 
ATOM   1403 C CB  . GLU B 1 84 ? 14.016  -4.943  -31.901 1.00 25.85  ? 83  GLU B CB  1 
ATOM   1404 C CG  . GLU B 1 84 ? 13.555  -4.187  -30.653 1.00 29.09  ? 83  GLU B CG  1 
ATOM   1405 C CD  . GLU B 1 84 ? 14.419  -4.492  -29.465 1.00 28.30  ? 83  GLU B CD  1 
ATOM   1406 O OE1 . GLU B 1 84 ? 15.380  -5.296  -29.540 1.00 26.73  ? 83  GLU B OE1 1 
ATOM   1407 O OE2 . GLU B 1 84 ? 14.064  -3.914  -28.384 1.00 30.30  ? 83  GLU B OE2 1 
ATOM   1408 N N   . ILE B 1 85 ? 13.613  -6.377  -34.670 1.00 27.54  ? 84  ILE B N   1 
ATOM   1409 C CA  . ILE B 1 85 ? 14.332  -6.929  -35.825 1.00 23.72  ? 84  ILE B CA  1 
ATOM   1410 C C   . ILE B 1 85 ? 13.701  -6.403  -37.119 1.00 25.19  ? 84  ILE B C   1 
ATOM   1411 O O   . ILE B 1 85 ? 14.416  -6.234  -38.121 1.00 26.28  ? 84  ILE B O   1 
ATOM   1412 C CB  . ILE B 1 85 ? 14.396  -8.473  -35.782 1.00 23.04  ? 84  ILE B CB  1 
ATOM   1413 C CG1 . ILE B 1 85 ? 15.395  -9.063  -36.805 1.00 24.30  ? 84  ILE B CG1 1 
ATOM   1414 C CG2 . ILE B 1 85 ? 13.004  -9.080  -35.961 1.00 25.10  ? 84  ILE B CG2 1 
ATOM   1415 C CD1 . ILE B 1 85 ? 15.791  -10.498 -36.450 1.00 24.22  ? 84  ILE B CD1 1 
ATOM   1416 N N   . GLN B 1 86 ? 12.385  -6.137  -37.087 1.00 26.23  ? 85  GLN B N   1 
ATOM   1417 C CA  . GLN B 1 86 ? 11.623  -5.624  -38.215 1.00 27.37  ? 85  GLN B CA  1 
ATOM   1418 C C   . GLN B 1 86 ? 11.797  -4.103  -38.354 1.00 29.30  ? 85  GLN B C   1 
ATOM   1419 O O   . GLN B 1 86 ? 11.852  -3.611  -39.473 1.00 33.17  ? 85  GLN B O   1 
ATOM   1420 C CB  . GLN B 1 86 ? 10.130  -5.943  -38.044 1.00 33.11  ? 85  GLN B CB  1 
ATOM   1421 N N   . ASN B 1 87 ? 11.911  -3.353  -37.244 1.00 28.27  ? 86  ASN B N   1 
ATOM   1422 C CA  . ASN B 1 87 ? 11.762  -1.891  -37.350 1.00 27.67  ? 86  ASN B CA  1 
ATOM   1423 C C   . ASN B 1 87 ? 13.071  -1.124  -37.168 1.00 28.26  ? 86  ASN B C   1 
ATOM   1424 O O   . ASN B 1 87 ? 13.184  0.015   -37.644 1.00 28.54  ? 86  ASN B O   1 
ATOM   1425 C CB  . ASN B 1 87 ? 10.651  -1.370  -36.430 1.00 29.94  ? 86  ASN B CB  1 
ATOM   1426 C CG  . ASN B 1 87 ? 9.313   -1.868  -36.910 1.00 33.94  ? 86  ASN B CG  1 
ATOM   1427 O OD1 . ASN B 1 87 ? 8.821   -1.386  -37.929 1.00 38.08  ? 86  ASN B OD1 1 
ATOM   1428 N ND2 . ASN B 1 87 ? 8.759   -2.887  -36.275 1.00 35.86  ? 86  ASN B ND2 1 
ATOM   1429 N N   . ASN B 1 88 ? 14.038  -1.694  -36.442 1.00 25.65  ? 87  ASN B N   1 
ATOM   1430 C CA  . ASN B 1 88 ? 15.277  -0.993  -36.159 1.00 30.66  ? 87  ASN B CA  1 
ATOM   1431 C C   . ASN B 1 88 ? 16.351  -1.988  -35.750 1.00 25.89  ? 87  ASN B C   1 
ATOM   1432 O O   . ASN B 1 88 ? 16.899  -1.929  -34.657 1.00 26.13  ? 87  ASN B O   1 
ATOM   1433 C CB  . ASN B 1 88 ? 15.114  0.191   -35.201 1.00 30.04  ? 87  ASN B CB  1 
ATOM   1434 C CG  . ASN B 1 88 ? 16.204  1.219   -35.420 1.00 30.58  ? 87  ASN B CG  1 
ATOM   1435 O OD1 . ASN B 1 88 ? 17.240  0.956   -36.039 1.00 30.95  ? 87  ASN B OD1 1 
ATOM   1436 N ND2 . ASN B 1 88 ? 16.038  2.410   -34.862 1.00 32.56  ? 87  ASN B ND2 1 
ATOM   1437 N N   . PRO B 1 89 ? 16.672  -2.952  -36.647 1.00 24.54  ? 88  PRO B N   1 
ATOM   1438 C CA  . PRO B 1 89 ? 17.558  -4.055  -36.303 1.00 22.20  ? 88  PRO B CA  1 
ATOM   1439 C C   . PRO B 1 89 ? 18.989  -3.641  -36.032 1.00 22.96  ? 88  PRO B C   1 
ATOM   1440 O O   . PRO B 1 89 ? 19.724  -4.386  -35.412 1.00 26.09  ? 88  PRO B O   1 
ATOM   1441 C CB  . PRO B 1 89 ? 17.439  -5.008  -37.507 1.00 21.71  ? 88  PRO B CB  1 
ATOM   1442 C CG  . PRO B 1 89 ? 17.093  -4.082  -38.659 1.00 22.52  ? 88  PRO B CG  1 
ATOM   1443 C CD  . PRO B 1 89 ? 16.151  -3.039  -38.032 1.00 22.44  ? 88  PRO B CD  1 
ATOM   1444 N N   . HIS B 1 90 ? 19.392  -2.442  -36.528 1.00 24.18  ? 89  HIS B N   1 
ATOM   1445 C CA  . HIS B 1 90 ? 20.803  -2.080  -36.399 1.00 24.60  ? 89  HIS B CA  1 
ATOM   1446 C C   . HIS B 1 90 ? 21.037  -0.942  -35.386 1.00 28.15  ? 89  HIS B C   1 
ATOM   1447 O O   . HIS B 1 90 ? 22.137  -0.404  -35.268 1.00 26.77  ? 89  HIS B O   1 
ATOM   1448 C CB  . HIS B 1 90 ? 21.372  -1.665  -37.771 1.00 26.53  ? 89  HIS B CB  1 
ATOM   1449 C CG  . HIS B 1 90 ? 21.170  -2.723  -38.809 1.00 28.36  ? 89  HIS B CG  1 
ATOM   1450 N ND1 . HIS B 1 90 ? 21.779  -3.956  -38.687 1.00 29.07  ? 89  HIS B ND1 1 
ATOM   1451 C CD2 . HIS B 1 90 ? 20.434  -2.778  -39.953 1.00 26.95  ? 89  HIS B CD2 1 
ATOM   1452 C CE1 . HIS B 1 90 ? 21.432  -4.718  -39.730 1.00 28.00  ? 89  HIS B CE1 1 
ATOM   1453 N NE2 . HIS B 1 90 ? 20.669  -4.011  -40.514 1.00 26.38  ? 89  HIS B NE2 1 
ATOM   1454 N N   . ALA B 1 91 ? 20.043  -0.699  -34.545 1.00 26.61  ? 90  ALA B N   1 
ATOM   1455 C CA  . ALA B 1 91 ? 20.148  0.356   -33.545 1.00 28.03  ? 90  ALA B CA  1 
ATOM   1456 C C   . ALA B 1 91 ? 21.038  -0.063  -32.377 1.00 31.01  ? 90  ALA B C   1 
ATOM   1457 O O   . ALA B 1 91 ? 21.342  -1.245  -32.165 1.00 29.95  ? 90  ALA B O   1 
ATOM   1458 C CB  . ALA B 1 91 ? 18.750  0.737   -33.070 1.00 28.94  ? 90  ALA B CB  1 
ATOM   1459 N N   . SER B 1 92 ? 21.450  0.954   -31.590 1.00 31.62  ? 91  SER B N   1 
ATOM   1460 C CA  . SER B 1 92 ? 22.076  0.756   -30.296 1.00 35.17  ? 91  SER B CA  1 
ATOM   1461 C C   . SER B 1 92 ? 20.968  0.550   -29.255 1.00 35.41  ? 91  SER B C   1 
ATOM   1462 O O   . SER B 1 92 ? 20.008  1.328   -29.219 1.00 36.32  ? 91  SER B O   1 
ATOM   1463 C CB  . SER B 1 92 ? 22.925  1.962   -29.946 1.00 35.19  ? 91  SER B CB  1 
ATOM   1464 O OG  . SER B 1 92 ? 23.499  1.727   -28.669 1.00 44.53  ? 91  SER B OG  1 
ATOM   1465 N N   . TYR B 1 93 ? 21.064  -0.571  -28.513 1.00 32.53  ? 92  TYR B N   1 
ATOM   1466 C CA  . TYR B 1 93 ? 20.114  -1.031  -27.507 1.00 35.19  ? 92  TYR B CA  1 
ATOM   1467 C C   . TYR B 1 93 ? 20.825  -1.129  -26.156 1.00 45.57  ? 92  TYR B C   1 
ATOM   1468 O O   . TYR B 1 93 ? 20.231  -1.503  -25.151 1.00 49.50  ? 92  TYR B O   1 
ATOM   1469 C CB  . TYR B 1 93 ? 19.535  -2.395  -27.910 1.00 30.75  ? 92  TYR B CB  1 
ATOM   1470 C CG  . TYR B 1 93 ? 18.532  -2.244  -29.037 1.00 29.02  ? 92  TYR B CG  1 
ATOM   1471 C CD1 . TYR B 1 93 ? 17.229  -1.799  -28.824 1.00 28.41  ? 92  TYR B CD1 1 
ATOM   1472 C CD2 . TYR B 1 93 ? 18.873  -2.602  -30.342 1.00 30.83  ? 92  TYR B CD2 1 
ATOM   1473 C CE1 . TYR B 1 93 ? 16.325  -1.640  -29.863 1.00 30.33  ? 92  TYR B CE1 1 
ATOM   1474 C CE2 . TYR B 1 93 ? 17.970  -2.468  -31.384 1.00 27.05  ? 92  TYR B CE2 1 
ATOM   1475 C CZ  . TYR B 1 93 ? 16.701  -1.987  -31.156 1.00 28.55  ? 92  TYR B CZ  1 
ATOM   1476 O OH  . TYR B 1 93 ? 15.843  -1.882  -32.196 1.00 29.37  ? 92  TYR B OH  1 
ATOM   1477 N N   . SER B 1 94 ? 22.102  -0.746  -26.159 1.00 48.85  ? 93  SER B N   1 
ATOM   1478 C CA  . SER B 1 94 ? 22.978  -0.722  -24.998 1.00 59.49  ? 93  SER B CA  1 
ATOM   1479 C C   . SER B 1 94 ? 22.542  0.376   -24.009 1.00 70.31  ? 93  SER B C   1 
ATOM   1480 O O   . SER B 1 94 ? 21.725  1.233   -24.413 1.00 78.41  ? 93  SER B O   1 
ATOM   1481 C CB  . SER B 1 94 ? 24.387  -0.484  -25.462 1.00 54.80  ? 93  SER B CB  1 
ATOM   1482 O OG  . SER B 1 94 ? 24.427  0.722   -26.217 1.00 59.23  ? 93  SER B OG  1 
ATOM   1483 O OXT . SER B 1 94 ? 23.052  0.354   -22.862 1.00 75.45  ? 93  SER B OXT 1 
ATOM   1484 N N   . HIS C 1 4  ? 32.246  -23.630 28.500  1.00 82.18  ? 3   HIS C N   1 
ATOM   1485 C CA  . HIS C 1 4  ? 31.098  -22.759 28.119  1.00 81.96  ? 3   HIS C CA  1 
ATOM   1486 C C   . HIS C 1 4  ? 30.016  -22.840 29.201  1.00 77.29  ? 3   HIS C C   1 
ATOM   1487 O O   . HIS C 1 4  ? 30.151  -23.588 30.167  1.00 68.61  ? 3   HIS C O   1 
ATOM   1488 C CB  . HIS C 1 4  ? 30.619  -23.094 26.697  1.00 86.03  ? 3   HIS C CB  1 
ATOM   1489 C CG  . HIS C 1 4  ? 29.891  -21.960 26.046  1.00 91.96  ? 3   HIS C CG  1 
ATOM   1490 N ND1 . HIS C 1 4  ? 30.500  -21.082 25.175  1.00 95.93  ? 3   HIS C ND1 1 
ATOM   1491 C CD2 . HIS C 1 4  ? 28.622  -21.544 26.158  1.00 89.88  ? 3   HIS C CD2 1 
ATOM   1492 C CE1 . HIS C 1 4  ? 29.620  -20.170 24.784  1.00 88.53  ? 3   HIS C CE1 1 
ATOM   1493 N NE2 . HIS C 1 4  ? 28.474  -20.432 25.371  1.00 86.62  ? 3   HIS C NE2 1 
ATOM   1494 N N   . ALA C 1 5  ? 28.933  -22.075 29.016  1.00 80.15  ? 4   ALA C N   1 
ATOM   1495 C CA  . ALA C 1 5  ? 27.924  -21.845 30.038  1.00 81.78  ? 4   ALA C CA  1 
ATOM   1496 C C   . ALA C 1 5  ? 26.543  -22.247 29.527  1.00 75.05  ? 4   ALA C C   1 
ATOM   1497 O O   . ALA C 1 5  ? 26.009  -21.583 28.640  1.00 78.52  ? 4   ALA C O   1 
ATOM   1498 C CB  . ALA C 1 5  ? 27.929  -20.370 30.387  1.00 83.75  ? 4   ALA C CB  1 
ATOM   1499 N N   . PHE C 1 6  ? 25.952  -23.295 30.124  1.00 61.39  ? 5   PHE C N   1 
ATOM   1500 C CA  . PHE C 1 6  ? 24.620  -23.729 29.723  1.00 51.46  ? 5   PHE C CA  1 
ATOM   1501 C C   . PHE C 1 6  ? 23.703  -23.853 30.943  1.00 56.31  ? 5   PHE C C   1 
ATOM   1502 O O   . PHE C 1 6  ? 23.897  -24.724 31.789  1.00 66.15  ? 5   PHE C O   1 
ATOM   1503 C CB  . PHE C 1 6  ? 24.704  -25.025 28.896  1.00 45.61  ? 5   PHE C CB  1 
ATOM   1504 C CG  . PHE C 1 6  ? 25.501  -24.991 27.590  1.00 42.85  ? 5   PHE C CG  1 
ATOM   1505 C CD1 . PHE C 1 6  ? 26.683  -25.708 27.447  1.00 43.38  ? 5   PHE C CD1 1 
ATOM   1506 C CD2 . PHE C 1 6  ? 25.081  -24.214 26.511  1.00 47.84  ? 5   PHE C CD2 1 
ATOM   1507 C CE1 . PHE C 1 6  ? 27.404  -25.667 26.257  1.00 45.98  ? 5   PHE C CE1 1 
ATOM   1508 C CE2 . PHE C 1 6  ? 25.818  -24.164 25.328  1.00 44.77  ? 5   PHE C CE2 1 
ATOM   1509 C CZ  . PHE C 1 6  ? 26.962  -24.905 25.198  1.00 42.31  ? 5   PHE C CZ  1 
ATOM   1510 N N   . LYS C 1 7  ? 22.676  -23.000 31.019  1.00 48.69  ? 6   LYS C N   1 
ATOM   1511 C CA  . LYS C 1 7  ? 21.660  -23.132 32.055  1.00 49.94  ? 6   LYS C CA  1 
ATOM   1512 C C   . LYS C 1 7  ? 20.373  -23.617 31.398  1.00 44.44  ? 6   LYS C C   1 
ATOM   1513 O O   . LYS C 1 7  ? 20.224  -23.488 30.167  1.00 43.76  ? 6   LYS C O   1 
ATOM   1514 C CB  . LYS C 1 7  ? 21.430  -21.827 32.839  1.00 57.29  ? 6   LYS C CB  1 
ATOM   1515 C CG  . LYS C 1 7  ? 22.278  -20.602 32.487  1.00 59.46  ? 6   LYS C CG  1 
ATOM   1516 C CD  . LYS C 1 7  ? 21.486  -19.305 32.363  1.00 55.73  ? 6   LYS C CD  1 
ATOM   1517 N N   . PRO C 1 8  ? 19.400  -24.173 32.172  1.00 43.45  ? 7   PRO C N   1 
ATOM   1518 C CA  . PRO C 1 8  ? 18.119  -24.611 31.608  1.00 41.14  ? 7   PRO C CA  1 
ATOM   1519 C C   . PRO C 1 8  ? 17.468  -23.458 30.848  1.00 49.76  ? 7   PRO C C   1 
ATOM   1520 O O   . PRO C 1 8  ? 17.417  -22.338 31.359  1.00 52.52  ? 7   PRO C O   1 
ATOM   1521 C CB  . PRO C 1 8  ? 17.299  -25.046 32.845  1.00 49.76  ? 7   PRO C CB  1 
ATOM   1522 C CG  . PRO C 1 8  ? 18.362  -25.448 33.840  1.00 44.69  ? 7   PRO C CG  1 
ATOM   1523 C CD  . PRO C 1 8  ? 19.487  -24.436 33.627  1.00 44.55  ? 7   PRO C CD  1 
ATOM   1524 N N   . GLY C 1 9  ? 16.993  -23.743 29.626  1.00 52.74  ? 8   GLY C N   1 
ATOM   1525 C CA  . GLY C 1 9  ? 16.318  -22.751 28.801  1.00 46.34  ? 8   GLY C CA  1 
ATOM   1526 C C   . GLY C 1 9  ? 17.220  -22.129 27.730  1.00 44.24  ? 8   GLY C C   1 
ATOM   1527 O O   . GLY C 1 9  ? 16.711  -21.472 26.825  1.00 43.79  ? 8   GLY C O   1 
ATOM   1528 N N   . ASP C 1 10 ? 18.546  -22.317 27.833  1.00 40.90  ? 9   ASP C N   1 
ATOM   1529 C CA  . ASP C 1 10 ? 19.494  -21.858 26.828  1.00 34.73  ? 9   ASP C CA  1 
ATOM   1530 C C   . ASP C 1 10 ? 19.280  -22.590 25.495  1.00 38.82  ? 9   ASP C C   1 
ATOM   1531 O O   . ASP C 1 10 ? 19.158  -23.803 25.465  1.00 38.11  ? 9   ASP C O   1 
ATOM   1532 C CB  . ASP C 1 10 ? 20.941  -22.089 27.246  1.00 36.77  ? 9   ASP C CB  1 
ATOM   1533 C CG  . ASP C 1 10 ? 21.530  -21.121 28.273  1.00 51.40  ? 9   ASP C CG  1 
ATOM   1534 O OD1 . ASP C 1 10 ? 20.762  -20.285 28.815  1.00 58.68  ? 9   ASP C OD1 1 
ATOM   1535 O OD2 . ASP C 1 10 ? 22.764  -21.189 28.511  1.00 54.82  ? 9   ASP C OD2 1 
ATOM   1536 N N   . LEU C 1 11 ? 19.288  -21.844 24.378  1.00 35.19  ? 10  LEU C N   1 
ATOM   1537 C CA  . LEU C 1 11 ? 19.051  -22.410 23.060  1.00 34.56  ? 10  LEU C CA  1 
ATOM   1538 C C   . LEU C 1 11 ? 20.363  -22.847 22.403  1.00 34.14  ? 10  LEU C C   1 
ATOM   1539 O O   . LEU C 1 11 ? 21.340  -22.101 22.386  1.00 32.52  ? 10  LEU C O   1 
ATOM   1540 C CB  . LEU C 1 11 ? 18.337  -21.335 22.235  1.00 32.68  ? 10  LEU C CB  1 
ATOM   1541 C CG  . LEU C 1 11 ? 17.033  -20.812 22.839  1.00 31.59  ? 10  LEU C CG  1 
ATOM   1542 C CD1 . LEU C 1 11 ? 16.401  -19.747 21.920  1.00 32.68  ? 10  LEU C CD1 1 
ATOM   1543 C CD2 . LEU C 1 11 ? 15.991  -21.885 23.183  1.00 31.57  ? 10  LEU C CD2 1 
ATOM   1544 N N   . VAL C 1 12 ? 20.355  -24.045 21.768  1.00 30.08  ? 11  VAL C N   1 
ATOM   1545 C CA  . VAL C 1 12 ? 21.566  -24.588 21.193  1.00 28.02  ? 11  VAL C CA  1 
ATOM   1546 C C   . VAL C 1 12 ? 21.228  -25.352 19.900  1.00 27.38  ? 11  VAL C C   1 
ATOM   1547 O O   . VAL C 1 12 ? 20.067  -25.601 19.615  1.00 27.24  ? 11  VAL C O   1 
ATOM   1548 C CB  . VAL C 1 12 ? 22.269  -25.555 22.175  1.00 29.80  ? 11  VAL C CB  1 
ATOM   1549 C CG1 . VAL C 1 12 ? 22.634  -24.849 23.475  1.00 30.04  ? 11  VAL C CG1 1 
ATOM   1550 C CG2 . VAL C 1 12 ? 21.439  -26.803 22.464  1.00 31.01  ? 11  VAL C CG2 1 
ATOM   1551 N N   . PHE C 1 13 ? 22.277  -25.689 19.142  1.00 29.12  ? 12  PHE C N   1 
ATOM   1552 C CA  . PHE C 1 13 ? 22.217  -26.851 18.261  1.00 26.02  ? 12  PHE C CA  1 
ATOM   1553 C C   . PHE C 1 13 ? 22.932  -28.009 18.953  1.00 27.64  ? 12  PHE C C   1 
ATOM   1554 O O   . PHE C 1 13 ? 24.021  -27.839 19.508  1.00 30.67  ? 12  PHE C O   1 
ATOM   1555 C CB  . PHE C 1 13 ? 22.804  -26.649 16.858  1.00 30.01  ? 12  PHE C CB  1 
ATOM   1556 C CG  . PHE C 1 13 ? 21.992  -25.687 16.012  1.00 30.73  ? 12  PHE C CG  1 
ATOM   1557 C CD1 . PHE C 1 13 ? 20.939  -26.156 15.226  1.00 30.95  ? 12  PHE C CD1 1 
ATOM   1558 C CD2 . PHE C 1 13 ? 22.264  -24.322 16.029  1.00 32.03  ? 12  PHE C CD2 1 
ATOM   1559 C CE1 . PHE C 1 13 ? 20.182  -25.273 14.470  1.00 33.57  ? 12  PHE C CE1 1 
ATOM   1560 C CE2 . PHE C 1 13 ? 21.486  -23.441 15.283  1.00 35.80  ? 12  PHE C CE2 1 
ATOM   1561 C CZ  . PHE C 1 13 ? 20.451  -23.925 14.519  1.00 33.67  ? 12  PHE C CZ  1 
ATOM   1562 N N   . ALA C 1 14 ? 22.312  -29.195 18.913  1.00 26.77  ? 13  ALA C N   1 
ATOM   1563 C CA  . ALA C 1 14 ? 22.739  -30.369 19.665  1.00 25.04  ? 13  ALA C CA  1 
ATOM   1564 C C   . ALA C 1 14 ? 23.002  -31.498 18.682  1.00 27.79  ? 13  ALA C C   1 
ATOM   1565 O O   . ALA C 1 14 ? 22.150  -31.799 17.846  1.00 24.28  ? 13  ALA C O   1 
ATOM   1566 C CB  . ALA C 1 14 ? 21.660  -30.813 20.644  1.00 27.51  ? 13  ALA C CB  1 
ATOM   1567 N N   . LYS C 1 15 ? 24.185  -32.106 18.787  1.00 25.04  ? 14  LYS C N   1 
ATOM   1568 C CA  . LYS C 1 15 ? 24.577  -33.104 17.805  1.00 27.65  ? 14  LYS C CA  1 
ATOM   1569 C C   . LYS C 1 15 ? 24.602  -34.473 18.467  1.00 27.30  ? 14  LYS C C   1 
ATOM   1570 O O   . LYS C 1 15 ? 25.347  -34.682 19.420  1.00 29.60  ? 14  LYS C O   1 
ATOM   1571 C CB  . LYS C 1 15 ? 25.980  -32.851 17.235  1.00 29.27  ? 14  LYS C CB  1 
ATOM   1572 C CG  . LYS C 1 15 ? 26.408  -33.881 16.177  1.00 28.73  ? 14  LYS C CG  1 
ATOM   1573 C CD  . LYS C 1 15 ? 25.629  -33.786 14.870  1.00 27.56  ? 14  LYS C CD  1 
ATOM   1574 C CE  . LYS C 1 15 ? 26.216  -34.680 13.748  1.00 27.19  ? 14  LYS C CE  1 
ATOM   1575 N NZ  . LYS C 1 15 ? 25.974  -36.066 14.114  1.00 27.30  ? 14  LYS C NZ  1 
ATOM   1576 N N   . MET C 1 16 ? 23.817  -35.407 17.920  1.00 25.22  ? 15  MET C N   1 
ATOM   1577 C CA  . MET C 1 16 ? 23.763  -36.819 18.290  1.00 26.75  ? 15  MET C CA  1 
ATOM   1578 C C   . MET C 1 16 ? 24.237  -37.627 17.086  1.00 28.09  ? 15  MET C C   1 
ATOM   1579 O O   . MET C 1 16 ? 23.984  -37.237 15.947  1.00 25.62  ? 15  MET C O   1 
ATOM   1580 C CB  . MET C 1 16 ? 22.337  -37.273 18.631  1.00 26.97  ? 15  MET C CB  1 
ATOM   1581 C CG  . MET C 1 16 ? 21.888  -36.809 20.018  1.00 34.59  ? 15  MET C CG  1 
ATOM   1582 S SD  . MET C 1 16 ? 20.315  -37.504 20.558  1.00 43.47  ? 15  MET C SD  1 
ATOM   1583 C CE  . MET C 1 16 ? 20.108  -39.172 19.912  1.00 46.36  ? 15  MET C CE  1 
ATOM   1584 N N   . LYS C 1 17 ? 24.950  -38.737 17.342  1.00 29.53  ? 16  LYS C N   1 
ATOM   1585 C CA  . LYS C 1 17 ? 25.324  -39.630 16.245  1.00 31.73  ? 16  LYS C CA  1 
ATOM   1586 C C   . LYS C 1 17 ? 24.046  -40.079 15.530  1.00 27.94  ? 16  LYS C C   1 
ATOM   1587 O O   . LYS C 1 17 ? 23.096  -40.566 16.149  1.00 28.50  ? 16  LYS C O   1 
ATOM   1588 C CB  . LYS C 1 17 ? 26.016  -40.880 16.819  1.00 30.99  ? 16  LYS C CB  1 
ATOM   1589 C CG  . LYS C 1 17 ? 26.629  -41.845 15.789  1.00 35.06  ? 16  LYS C CG  1 
ATOM   1590 C CD  . LYS C 1 17 ? 27.851  -41.185 15.166  1.00 40.08  ? 16  LYS C CD  1 
ATOM   1591 C CE  . LYS C 1 17 ? 28.556  -42.134 14.240  1.00 54.33  ? 16  LYS C CE  1 
ATOM   1592 N NZ  . LYS C 1 17 ? 29.790  -41.524 13.740  1.00 49.01  ? 16  LYS C NZ  1 
ATOM   1593 N N   . GLY C 1 18 ? 24.085  -39.966 14.197  1.00 27.96  ? 17  GLY C N   1 
ATOM   1594 C CA  . GLY C 1 18 ? 22.988  -40.450 13.380  1.00 28.67  ? 17  GLY C CA  1 
ATOM   1595 C C   . GLY C 1 18 ? 22.033  -39.330 12.954  1.00 31.23  ? 17  GLY C C   1 
ATOM   1596 O O   . GLY C 1 18 ? 21.064  -39.614 12.289  1.00 30.09  ? 17  GLY C O   1 
ATOM   1597 N N   . TYR C 1 19 ? 22.287  -38.087 13.382  1.00 28.16  ? 18  TYR C N   1 
ATOM   1598 C CA  . TYR C 1 19 ? 21.350  -36.979 13.196  1.00 26.23  ? 18  TYR C CA  1 
ATOM   1599 C C   . TYR C 1 19 ? 22.142  -35.722 12.873  1.00 26.51  ? 18  TYR C C   1 
ATOM   1600 O O   . TYR C 1 19 ? 23.248  -35.504 13.370  1.00 25.06  ? 18  TYR C O   1 
ATOM   1601 C CB  . TYR C 1 19 ? 20.606  -36.708 14.516  1.00 23.49  ? 18  TYR C CB  1 
ATOM   1602 C CG  . TYR C 1 19 ? 19.757  -37.893 14.930  1.00 25.41  ? 18  TYR C CG  1 
ATOM   1603 C CD1 . TYR C 1 19 ? 20.288  -38.916 15.724  1.00 25.74  ? 18  TYR C CD1 1 
ATOM   1604 C CD2 . TYR C 1 19 ? 18.463  -38.033 14.452  1.00 25.75  ? 18  TYR C CD2 1 
ATOM   1605 C CE1 . TYR C 1 19 ? 19.527  -40.018 16.067  1.00 29.99  ? 18  TYR C CE1 1 
ATOM   1606 C CE2 . TYR C 1 19 ? 17.691  -39.123 14.818  1.00 33.88  ? 18  TYR C CE2 1 
ATOM   1607 C CZ  . TYR C 1 19 ? 18.229  -40.122 15.606  1.00 32.92  ? 18  TYR C CZ  1 
ATOM   1608 O OH  . TYR C 1 19 ? 17.457  -41.193 15.962  1.00 43.59  ? 18  TYR C OH  1 
ATOM   1609 N N   . PRO C 1 20 ? 21.593  -34.806 12.066  1.00 27.10  ? 19  PRO C N   1 
ATOM   1610 C CA  . PRO C 1 20 ? 22.244  -33.510 11.858  1.00 24.60  ? 19  PRO C CA  1 
ATOM   1611 C C   . PRO C 1 20 ? 22.183  -32.668 13.140  1.00 23.35  ? 19  PRO C C   1 
ATOM   1612 O O   . PRO C 1 20 ? 21.418  -32.979 14.059  1.00 24.36  ? 19  PRO C O   1 
ATOM   1613 C CB  . PRO C 1 20 ? 21.381  -32.931 10.714  1.00 27.09  ? 19  PRO C CB  1 
ATOM   1614 C CG  . PRO C 1 20 ? 20.012  -33.505 10.932  1.00 27.25  ? 19  PRO C CG  1 
ATOM   1615 C CD  . PRO C 1 20 ? 20.263  -34.913 11.423  1.00 25.53  ? 19  PRO C CD  1 
ATOM   1616 N N   . HIS C 1 21 ? 23.028  -31.635 13.199  1.00 24.81  ? 20  HIS C N   1 
ATOM   1617 C CA  . HIS C 1 21 ? 22.993  -30.683 14.303  1.00 25.21  ? 20  HIS C CA  1 
ATOM   1618 C C   . HIS C 1 21 ? 21.564  -30.168 14.436  1.00 24.93  ? 20  HIS C C   1 
ATOM   1619 O O   . HIS C 1 21 ? 20.990  -29.688 13.455  1.00 26.83  ? 20  HIS C O   1 
ATOM   1620 C CB  . HIS C 1 21 ? 23.987  -29.537 14.096  1.00 27.27  ? 20  HIS C CB  1 
ATOM   1621 C CG  . HIS C 1 21 ? 25.416  -29.968 14.164  1.00 27.41  ? 20  HIS C CG  1 
ATOM   1622 N ND1 . HIS C 1 21 ? 26.053  -30.660 13.157  1.00 32.72  ? 20  HIS C ND1 1 
ATOM   1623 C CD2 . HIS C 1 21 ? 26.319  -29.788 15.153  1.00 33.28  ? 20  HIS C CD2 1 
ATOM   1624 C CE1 . HIS C 1 21 ? 27.317  -30.897 13.530  1.00 34.97  ? 20  HIS C CE1 1 
ATOM   1625 N NE2 . HIS C 1 21 ? 27.523  -30.351 14.724  1.00 33.57  ? 20  HIS C NE2 1 
ATOM   1626 N N   . TRP C 1 22 ? 20.984  -30.290 15.643  1.00 21.70  ? 21  TRP C N   1 
ATOM   1627 C CA  . TRP C 1 22 ? 19.531  -30.184 15.734  1.00 21.98  ? 21  TRP C CA  1 
ATOM   1628 C C   . TRP C 1 22 ? 19.124  -29.020 16.638  1.00 22.25  ? 21  TRP C C   1 
ATOM   1629 O O   . TRP C 1 22 ? 19.670  -28.885 17.746  1.00 23.68  ? 21  TRP C O   1 
ATOM   1630 C CB  . TRP C 1 22 ? 18.978  -31.493 16.345  1.00 24.31  ? 21  TRP C CB  1 
ATOM   1631 C CG  . TRP C 1 22 ? 17.515  -31.729 16.013  1.00 26.79  ? 21  TRP C CG  1 
ATOM   1632 C CD1 . TRP C 1 22 ? 16.403  -31.166 16.583  1.00 25.61  ? 21  TRP C CD1 1 
ATOM   1633 C CD2 . TRP C 1 22 ? 17.020  -32.627 14.989  1.00 25.87  ? 21  TRP C CD2 1 
ATOM   1634 N NE1 . TRP C 1 22 ? 15.265  -31.623 15.967  1.00 26.27  ? 21  TRP C NE1 1 
ATOM   1635 C CE2 . TRP C 1 22 ? 15.604  -32.541 15.006  1.00 24.07  ? 21  TRP C CE2 1 
ATOM   1636 C CE3 . TRP C 1 22 ? 17.633  -33.504 14.088  1.00 24.28  ? 21  TRP C CE3 1 
ATOM   1637 C CZ2 . TRP C 1 22 ? 14.823  -33.273 14.098  1.00 24.75  ? 21  TRP C CZ2 1 
ATOM   1638 C CZ3 . TRP C 1 22 ? 16.864  -34.245 13.208  1.00 25.18  ? 21  TRP C CZ3 1 
ATOM   1639 C CH2 . TRP C 1 22 ? 15.468  -34.141 13.248  1.00 22.97  ? 21  TRP C CH2 1 
ATOM   1640 N N   . PRO C 1 23 ? 18.077  -28.218 16.307  1.00 24.15  ? 22  PRO C N   1 
ATOM   1641 C CA  . PRO C 1 23 ? 17.653  -27.140 17.207  1.00 24.59  ? 22  PRO C CA  1 
ATOM   1642 C C   . PRO C 1 23 ? 17.122  -27.697 18.526  1.00 22.67  ? 22  PRO C C   1 
ATOM   1643 O O   . PRO C 1 23 ? 16.299  -28.608 18.523  1.00 23.76  ? 22  PRO C O   1 
ATOM   1644 C CB  . PRO C 1 23 ? 16.551  -26.410 16.363  1.00 27.32  ? 22  PRO C CB  1 
ATOM   1645 C CG  . PRO C 1 23 ? 16.052  -27.460 15.413  1.00 25.43  ? 22  PRO C CG  1 
ATOM   1646 C CD  . PRO C 1 23 ? 17.345  -28.203 15.030  1.00 21.04  ? 22  PRO C CD  1 
ATOM   1647 N N   . ALA C 1 24 ? 17.630  -27.156 19.641  1.00 23.99  ? 23  ALA C N   1 
ATOM   1648 C CA  . ALA C 1 24 ? 17.320  -27.714 20.951  1.00 26.44  ? 23  ALA C CA  1 
ATOM   1649 C C   . ALA C 1 24 ? 17.447  -26.643 22.027  1.00 28.72  ? 23  ALA C C   1 
ATOM   1650 O O   . ALA C 1 24 ? 17.980  -25.542 21.795  1.00 29.03  ? 23  ALA C O   1 
ATOM   1651 C CB  . ALA C 1 24 ? 18.275  -28.872 21.277  1.00 25.70  ? 23  ALA C CB  1 
ATOM   1652 N N   . ARG C 1 25 ? 17.044  -27.023 23.261  1.00 28.67  ? 24  ARG C N   1 
ATOM   1653 C CA  . ARG C 1 25 ? 17.400  -26.203 24.405  1.00 30.11  ? 24  ARG C CA  1 
ATOM   1654 C C   . ARG C 1 25 ? 17.835  -27.103 25.562  1.00 32.22  ? 24  ARG C C   1 
ATOM   1655 O O   . ARG C 1 25 ? 17.492  -28.285 25.596  1.00 33.50  ? 24  ARG C O   1 
ATOM   1656 C CB  . ARG C 1 25 ? 16.172  -25.459 24.916  1.00 30.13  ? 24  ARG C CB  1 
ATOM   1657 C CG  . ARG C 1 25 ? 14.904  -26.247 25.193  1.00 36.04  ? 24  ARG C CG  1 
ATOM   1658 C CD  . ARG C 1 25 ? 13.941  -25.335 25.990  1.00 38.69  ? 24  ARG C CD  1 
ATOM   1659 N NE  . ARG C 1 25 ? 12.717  -26.127 26.188  1.00 44.15  ? 24  ARG C NE  1 
ATOM   1660 C CZ  . ARG C 1 25 ? 11.446  -25.844 25.906  1.00 52.93  ? 24  ARG C CZ  1 
ATOM   1661 N NH1 . ARG C 1 25 ? 11.111  -24.705 25.319  1.00 46.93  ? 24  ARG C NH1 1 
ATOM   1662 N NH2 . ARG C 1 25 ? 10.498  -26.719 26.215  1.00 51.27  ? 24  ARG C NH2 1 
ATOM   1663 N N   . ILE C 1 26 ? 18.508  -26.492 26.527  1.00 33.53  ? 25  ILE C N   1 
ATOM   1664 C CA  . ILE C 1 26 ? 18.807  -27.154 27.795  1.00 36.34  ? 25  ILE C CA  1 
ATOM   1665 C C   . ILE C 1 26 ? 17.527  -27.297 28.630  1.00 42.33  ? 25  ILE C C   1 
ATOM   1666 O O   . ILE C 1 26 ? 16.700  -26.387 28.715  1.00 42.92  ? 25  ILE C O   1 
ATOM   1667 C CB  . ILE C 1 26 ? 19.914  -26.396 28.541  1.00 37.00  ? 25  ILE C CB  1 
ATOM   1668 C CG1 . ILE C 1 26 ? 21.032  -25.888 27.634  1.00 35.80  ? 25  ILE C CG1 1 
ATOM   1669 C CG2 . ILE C 1 26 ? 20.457  -27.166 29.744  1.00 37.36  ? 25  ILE C CG2 1 
ATOM   1670 C CD1 . ILE C 1 26 ? 22.030  -26.906 27.116  1.00 40.85  ? 25  ILE C CD1 1 
ATOM   1671 N N   . ASP C 1 27 ? 17.358  -28.477 29.228  1.00 42.29  ? 26  ASP C N   1 
ATOM   1672 C CA  . ASP C 1 27 ? 16.301  -28.718 30.200  1.00 54.27  ? 26  ASP C CA  1 
ATOM   1673 C C   . ASP C 1 27 ? 16.809  -28.527 31.632  1.00 52.60  ? 26  ASP C C   1 
ATOM   1674 O O   . ASP C 1 27 ? 17.956  -28.064 31.770  1.00 54.78  ? 26  ASP C O   1 
ATOM   1675 C CB  . ASP C 1 27 ? 15.720  -30.111 30.062  1.00 59.05  ? 26  ASP C CB  1 
ATOM   1676 C CG  . ASP C 1 27 ? 14.347  -30.142 29.424  1.00 65.64  ? 26  ASP C CG  1 
ATOM   1677 O OD1 . ASP C 1 27 ? 13.959  -29.090 28.867  1.00 66.95  ? 26  ASP C OD1 1 
ATOM   1678 O OD2 . ASP C 1 27 ? 13.681  -31.192 29.539  1.00 58.93  ? 26  ASP C OD2 1 
ATOM   1679 N N   . LYS C 1 35 ? 19.607  -38.770 37.822  1.00 65.44  ? 34  LYS C N   1 
ATOM   1680 C CA  . LYS C 1 35 ? 20.515  -37.628 37.532  1.00 61.41  ? 34  LYS C CA  1 
ATOM   1681 C C   . LYS C 1 35 ? 21.195  -37.885 36.187  1.00 57.33  ? 34  LYS C C   1 
ATOM   1682 O O   . LYS C 1 35 ? 21.233  -39.024 35.724  1.00 60.60  ? 34  LYS C O   1 
ATOM   1683 C CB  . LYS C 1 35 ? 21.488  -37.435 38.706  1.00 64.66  ? 34  LYS C CB  1 
ATOM   1684 N N   . PRO C 1 36 ? 21.739  -36.847 35.508  1.00 53.89  ? 35  PRO C N   1 
ATOM   1685 C CA  . PRO C 1 36 ? 22.437  -37.050 34.236  1.00 56.84  ? 35  PRO C CA  1 
ATOM   1686 C C   . PRO C 1 36 ? 23.653  -37.950 34.453  1.00 57.45  ? 35  PRO C C   1 
ATOM   1687 O O   . PRO C 1 36 ? 24.206  -38.008 35.554  1.00 49.49  ? 35  PRO C O   1 
ATOM   1688 C CB  . PRO C 1 36 ? 22.868  -35.620 33.809  1.00 59.53  ? 35  PRO C CB  1 
ATOM   1689 C CG  . PRO C 1 36 ? 22.054  -34.672 34.670  1.00 60.41  ? 35  PRO C CG  1 
ATOM   1690 C CD  . PRO C 1 36 ? 21.739  -35.438 35.944  1.00 61.85  ? 35  PRO C CD  1 
ATOM   1691 N N   . PRO C 1 37 ? 24.138  -38.674 33.421  1.00 49.76  ? 36  PRO C N   1 
ATOM   1692 C CA  . PRO C 1 37 ? 25.471  -39.273 33.508  1.00 49.39  ? 36  PRO C CA  1 
ATOM   1693 C C   . PRO C 1 37 ? 26.455  -38.140 33.785  1.00 48.48  ? 36  PRO C C   1 
ATOM   1694 O O   . PRO C 1 37 ? 26.171  -36.983 33.462  1.00 37.97  ? 36  PRO C O   1 
ATOM   1695 C CB  . PRO C 1 37 ? 25.661  -39.911 32.115  1.00 46.72  ? 36  PRO C CB  1 
ATOM   1696 C CG  . PRO C 1 37 ? 24.248  -40.185 31.667  1.00 46.33  ? 36  PRO C CG  1 
ATOM   1697 C CD  . PRO C 1 37 ? 23.452  -38.981 32.156  1.00 50.46  ? 36  PRO C CD  1 
ATOM   1698 N N   . PRO C 1 38 ? 27.631  -38.435 34.393  1.00 43.36  ? 37  PRO C N   1 
ATOM   1699 C CA  . PRO C 1 38 ? 28.638  -37.418 34.695  1.00 48.33  ? 37  PRO C CA  1 
ATOM   1700 C C   . PRO C 1 38 ? 28.869  -36.542 33.476  1.00 38.59  ? 37  PRO C C   1 
ATOM   1701 O O   . PRO C 1 38 ? 29.049  -37.072 32.377  1.00 33.17  ? 37  PRO C O   1 
ATOM   1702 C CB  . PRO C 1 38 ? 29.897  -38.267 35.014  1.00 48.89  ? 37  PRO C CB  1 
ATOM   1703 C CG  . PRO C 1 38 ? 29.325  -39.555 35.561  1.00 46.16  ? 37  PRO C CG  1 
ATOM   1704 C CD  . PRO C 1 38 ? 28.062  -39.793 34.765  1.00 49.63  ? 37  PRO C CD  1 
ATOM   1705 N N   . ASN C 1 39 ? 28.782  -35.221 33.705  1.00 35.27  ? 38  ASN C N   1 
ATOM   1706 C CA  . ASN C 1 39 ? 29.131  -34.181 32.759  1.00 36.74  ? 38  ASN C CA  1 
ATOM   1707 C C   . ASN C 1 39 ? 28.175  -34.195 31.559  1.00 37.58  ? 38  ASN C C   1 
ATOM   1708 O O   . ASN C 1 39 ? 28.619  -33.878 30.459  1.00 42.22  ? 38  ASN C O   1 
ATOM   1709 C CB  . ASN C 1 39 ? 30.563  -34.330 32.253  1.00 39.62  ? 38  ASN C CB  1 
ATOM   1710 C CG  . ASN C 1 39 ? 31.116  -33.043 31.674  1.00 51.33  ? 38  ASN C CG  1 
ATOM   1711 O OD1 . ASN C 1 39 ? 30.644  -31.947 31.994  1.00 56.22  ? 38  ASN C OD1 1 
ATOM   1712 N ND2 . ASN C 1 39 ? 32.127  -33.148 30.824  1.00 51.06  ? 38  ASN C ND2 1 
ATOM   1713 N N   . LYS C 1 40 ? 26.908  -34.599 31.749  1.00 33.83  ? 39  LYS C N   1 
ATOM   1714 C CA  . LYS C 1 40 ? 25.938  -34.509 30.656  1.00 33.86  ? 39  LYS C CA  1 
ATOM   1715 C C   . LYS C 1 40 ? 24.798  -33.546 30.990  1.00 32.61  ? 39  LYS C C   1 
ATOM   1716 O O   . LYS C 1 40 ? 24.352  -33.425 32.124  1.00 34.07  ? 39  LYS C O   1 
ATOM   1717 C CB  . LYS C 1 40 ? 25.245  -35.824 30.277  1.00 31.84  ? 39  LYS C CB  1 
ATOM   1718 C CG  . LYS C 1 40 ? 26.164  -36.989 29.925  1.00 36.48  ? 39  LYS C CG  1 
ATOM   1719 C CD  . LYS C 1 40 ? 26.993  -36.867 28.664  1.00 40.15  ? 39  LYS C CD  1 
ATOM   1720 C CE  . LYS C 1 40 ? 27.832  -38.098 28.427  1.00 45.93  ? 39  LYS C CE  1 
ATOM   1721 N NZ  . LYS C 1 40 ? 28.801  -37.817 27.355  1.00 53.07  ? 39  LYS C NZ  1 
ATOM   1722 N N   . TYR C 1 41 ? 24.292  -32.861 29.955  1.00 30.78  ? 40  TYR C N   1 
ATOM   1723 C CA  . TYR C 1 41 ? 23.136  -31.986 30.102  1.00 28.95  ? 40  TYR C CA  1 
ATOM   1724 C C   . TYR C 1 41 ? 21.890  -32.674 29.555  1.00 32.83  ? 40  TYR C C   1 
ATOM   1725 O O   . TYR C 1 41 ? 21.967  -33.414 28.561  1.00 34.78  ? 40  TYR C O   1 
ATOM   1726 C CB  . TYR C 1 41 ? 23.279  -30.769 29.172  1.00 29.77  ? 40  TYR C CB  1 
ATOM   1727 C CG  . TYR C 1 41 ? 24.377  -29.810 29.593  1.00 33.77  ? 40  TYR C CG  1 
ATOM   1728 C CD1 . TYR C 1 41 ? 25.702  -29.988 29.201  1.00 37.48  ? 40  TYR C CD1 1 
ATOM   1729 C CD2 . TYR C 1 41 ? 24.073  -28.740 30.425  1.00 38.04  ? 40  TYR C CD2 1 
ATOM   1730 C CE1 . TYR C 1 41 ? 26.700  -29.120 29.618  1.00 43.44  ? 40  TYR C CE1 1 
ATOM   1731 C CE2 . TYR C 1 41 ? 25.049  -27.844 30.803  1.00 38.31  ? 40  TYR C CE2 1 
ATOM   1732 C CZ  . TYR C 1 41 ? 26.360  -28.040 30.418  1.00 44.28  ? 40  TYR C CZ  1 
ATOM   1733 O OH  . TYR C 1 41 ? 27.272  -27.116 30.826  1.00 51.61  ? 40  TYR C OH  1 
ATOM   1734 N N   . PRO C 1 42 ? 20.712  -32.396 30.162  1.00 32.82  ? 41  PRO C N   1 
ATOM   1735 C CA  . PRO C 1 42 ? 19.420  -32.806 29.616  1.00 29.80  ? 41  PRO C CA  1 
ATOM   1736 C C   . PRO C 1 42 ? 19.072  -31.835 28.495  1.00 30.81  ? 41  PRO C C   1 
ATOM   1737 O O   . PRO C 1 42 ? 19.144  -30.619 28.683  1.00 33.45  ? 41  PRO C O   1 
ATOM   1738 C CB  . PRO C 1 42 ? 18.470  -32.675 30.825  1.00 31.90  ? 41  PRO C CB  1 
ATOM   1739 C CG  . PRO C 1 42 ? 19.069  -31.576 31.628  1.00 36.83  ? 41  PRO C CG  1 
ATOM   1740 C CD  . PRO C 1 42 ? 20.577  -31.648 31.431  1.00 36.88  ? 41  PRO C CD  1 
ATOM   1741 N N   . ILE C 1 43 ? 18.799  -32.417 27.325  1.00 32.00  ? 42  ILE C N   1 
ATOM   1742 C CA  . ILE C 1 43 ? 18.488  -31.622 26.137  1.00 28.05  ? 42  ILE C CA  1 
ATOM   1743 C C   . ILE C 1 43 ? 17.053  -31.910 25.724  1.00 30.77  ? 42  ILE C C   1 
ATOM   1744 O O   . ILE C 1 43 ? 16.633  -33.069 25.705  1.00 33.17  ? 42  ILE C O   1 
ATOM   1745 C CB  . ILE C 1 43 ? 19.491  -31.979 25.019  1.00 28.76  ? 42  ILE C CB  1 
ATOM   1746 C CG1 . ILE C 1 43 ? 20.964  -31.695 25.437  1.00 29.38  ? 42  ILE C CG1 1 
ATOM   1747 C CG2 . ILE C 1 43 ? 19.088  -31.285 23.700  1.00 25.23  ? 42  ILE C CG2 1 
ATOM   1748 C CD1 . ILE C 1 43 ? 21.260  -30.309 25.972  1.00 30.58  ? 42  ILE C CD1 1 
ATOM   1749 N N   . PHE C 1 44 ? 16.301  -30.849 25.339  1.00 28.92  ? 43  PHE C N   1 
ATOM   1750 C CA  . PHE C 1 44 ? 15.012  -31.036 24.699  1.00 29.44  ? 43  PHE C CA  1 
ATOM   1751 C C   . PHE C 1 44 ? 15.195  -30.644 23.228  1.00 26.01  ? 43  PHE C C   1 
ATOM   1752 O O   . PHE C 1 44 ? 15.636  -29.528 22.974  1.00 29.53  ? 43  PHE C O   1 
ATOM   1753 C CB  . PHE C 1 44 ? 14.055  -30.036 25.355  1.00 31.84  ? 43  PHE C CB  1 
ATOM   1754 C CG  . PHE C 1 44 ? 12.664  -29.975 24.739  1.00 35.60  ? 43  PHE C CG  1 
ATOM   1755 C CD1 . PHE C 1 44 ? 11.697  -30.950 25.001  1.00 36.56  ? 43  PHE C CD1 1 
ATOM   1756 C CD2 . PHE C 1 44 ? 12.334  -28.936 23.863  1.00 38.17  ? 43  PHE C CD2 1 
ATOM   1757 C CE1 . PHE C 1 44 ? 10.423  -30.864 24.436  1.00 40.56  ? 43  PHE C CE1 1 
ATOM   1758 C CE2 . PHE C 1 44 ? 11.069  -28.871 23.283  1.00 34.32  ? 43  PHE C CE2 1 
ATOM   1759 C CZ  . PHE C 1 44 ? 10.119  -29.830 23.568  1.00 38.66  ? 43  PHE C CZ  1 
ATOM   1760 N N   . PHE C 1 45 ? 14.829  -31.543 22.322  1.00 25.18  ? 44  PHE C N   1 
ATOM   1761 C CA  . PHE C 1 45 ? 14.912  -31.277 20.891  1.00 25.14  ? 44  PHE C CA  1 
ATOM   1762 C C   . PHE C 1 45 ? 13.634  -30.602 20.402  1.00 31.02  ? 44  PHE C C   1 
ATOM   1763 O O   . PHE C 1 45 ? 12.536  -31.169 20.508  1.00 28.93  ? 44  PHE C O   1 
ATOM   1764 C CB  . PHE C 1 45 ? 15.203  -32.551 20.103  1.00 25.99  ? 44  PHE C CB  1 
ATOM   1765 C CG  . PHE C 1 45 ? 16.596  -33.070 20.427  1.00 27.58  ? 44  PHE C CG  1 
ATOM   1766 C CD1 . PHE C 1 45 ? 17.714  -32.611 19.726  1.00 25.05  ? 44  PHE C CD1 1 
ATOM   1767 C CD2 . PHE C 1 45 ? 16.782  -33.997 21.458  1.00 28.10  ? 44  PHE C CD2 1 
ATOM   1768 C CE1 . PHE C 1 45 ? 18.993  -33.111 20.014  1.00 27.68  ? 44  PHE C CE1 1 
ATOM   1769 C CE2 . PHE C 1 45 ? 18.054  -34.477 21.746  1.00 30.08  ? 44  PHE C CE2 1 
ATOM   1770 C CZ  . PHE C 1 45 ? 19.153  -34.024 21.053  1.00 30.94  ? 44  PHE C CZ  1 
ATOM   1771 N N   . PHE C 1 46 ? 13.814  -29.461 19.713  1.00 25.40  ? 45  PHE C N   1 
ATOM   1772 C CA  . PHE C 1 46 ? 12.660  -28.844 19.059  1.00 26.56  ? 45  PHE C CA  1 
ATOM   1773 C C   . PHE C 1 46 ? 12.139  -29.717 17.914  1.00 28.30  ? 45  PHE C C   1 
ATOM   1774 O O   . PHE C 1 46 ? 12.876  -30.458 17.275  1.00 26.53  ? 45  PHE C O   1 
ATOM   1775 C CB  . PHE C 1 46 ? 12.952  -27.395 18.634  1.00 24.35  ? 45  PHE C CB  1 
ATOM   1776 C CG  . PHE C 1 46 ? 13.207  -26.421 19.768  1.00 25.77  ? 45  PHE C CG  1 
ATOM   1777 C CD1 . PHE C 1 46 ? 12.147  -25.982 20.570  1.00 30.01  ? 45  PHE C CD1 1 
ATOM   1778 C CD2 . PHE C 1 46 ? 14.487  -25.931 20.033  1.00 25.77  ? 45  PHE C CD2 1 
ATOM   1779 C CE1 . PHE C 1 46 ? 12.425  -25.094 21.609  1.00 27.70  ? 45  PHE C CE1 1 
ATOM   1780 C CE2 . PHE C 1 46 ? 14.752  -25.029 21.057  1.00 29.40  ? 45  PHE C CE2 1 
ATOM   1781 C CZ  . PHE C 1 46 ? 13.707  -24.594 21.839  1.00 29.68  ? 45  PHE C CZ  1 
ATOM   1782 N N   . GLY C 1 47 ? 10.841  -29.577 17.605  1.00 25.88  ? 46  GLY C N   1 
ATOM   1783 C CA  . GLY C 1 47 ? 10.241  -30.282 16.480  1.00 30.15  ? 46  GLY C CA  1 
ATOM   1784 C C   . GLY C 1 47 ? 9.802   -31.706 16.835  1.00 38.72  ? 46  GLY C C   1 
ATOM   1785 O O   . GLY C 1 47 ? 8.607   -32.022 16.765  1.00 36.07  ? 46  GLY C O   1 
ATOM   1786 N N   . THR C 1 48 ? 10.765  -32.554 17.228  1.00 34.55  ? 47  THR C N   1 
ATOM   1787 C CA  . THR C 1 48 ? 10.473  -33.917 17.691  1.00 33.76  ? 47  THR C CA  1 
ATOM   1788 C C   . THR C 1 48 ? 9.961   -33.875 19.135  1.00 34.57  ? 47  THR C C   1 
ATOM   1789 O O   . THR C 1 48 ? 9.171   -34.741 19.520  1.00 38.63  ? 47  THR C O   1 
ATOM   1790 C CB  . THR C 1 48 ? 11.703  -34.831 17.588  1.00 28.61  ? 47  THR C CB  1 
ATOM   1791 O OG1 . THR C 1 48 ? 12.553  -34.265 18.586  1.00 30.21  ? 47  THR C OG1 1 
ATOM   1792 C CG2 . THR C 1 48 ? 12.289  -34.935 16.189  1.00 32.74  ? 47  THR C CG2 1 
ATOM   1793 N N   . HIS C 1 49 ? 10.385  -32.880 19.928  1.00 29.43  ? 48  HIS C N   1 
ATOM   1794 C CA  . HIS C 1 49 ? 10.010  -32.756 21.341  1.00 32.85  ? 48  HIS C CA  1 
ATOM   1795 C C   . HIS C 1 49 ? 10.497  -33.940 22.185  1.00 36.17  ? 48  HIS C C   1 
ATOM   1796 O O   . HIS C 1 49 ? 9.906   -34.262 23.216  1.00 38.07  ? 48  HIS C O   1 
ATOM   1797 C CB  . HIS C 1 49 ? 8.491   -32.601 21.497  1.00 39.10  ? 48  HIS C CB  1 
ATOM   1798 C CG  . HIS C 1 49 ? 8.011   -31.468 20.660  1.00 39.19  ? 48  HIS C CG  1 
ATOM   1799 N ND1 . HIS C 1 49 ? 6.958   -31.601 19.786  1.00 46.44  ? 48  HIS C ND1 1 
ATOM   1800 C CD2 . HIS C 1 49 ? 8.507   -30.226 20.486  1.00 38.04  ? 48  HIS C CD2 1 
ATOM   1801 C CE1 . HIS C 1 49 ? 6.795   -30.451 19.135  1.00 45.69  ? 48  HIS C CE1 1 
ATOM   1802 N NE2 . HIS C 1 49 ? 7.719   -29.603 19.546  1.00 47.03  ? 48  HIS C NE2 1 
ATOM   1803 N N   . GLU C 1 50 ? 11.580  -34.575 21.752  1.00 33.46  ? 49  GLU C N   1 
ATOM   1804 C CA  . GLU C 1 50 ? 12.193  -35.657 22.516  1.00 38.02  ? 49  GLU C CA  1 
ATOM   1805 C C   . GLU C 1 50 ? 13.325  -35.127 23.397  1.00 40.11  ? 49  GLU C C   1 
ATOM   1806 O O   . GLU C 1 50 ? 13.754  -33.983 23.255  1.00 35.07  ? 49  GLU C O   1 
ATOM   1807 C CB  . GLU C 1 50 ? 12.664  -36.670 21.487  1.00 37.19  ? 49  GLU C CB  1 
ATOM   1808 C CG  . GLU C 1 50 ? 11.489  -37.343 20.780  1.00 48.62  ? 49  GLU C CG  1 
ATOM   1809 C CD  . GLU C 1 50 ? 11.931  -38.284 19.679  1.00 57.85  ? 49  GLU C CD  1 
ATOM   1810 O OE1 . GLU C 1 50 ? 13.002  -38.918 19.814  1.00 65.45  ? 49  GLU C OE1 1 
ATOM   1811 O OE2 . GLU C 1 50 ? 11.184  -38.395 18.689  1.00 65.67  ? 49  GLU C OE2 1 
ATOM   1812 N N   . THR C 1 51 ? 13.805  -35.971 24.334  1.00 34.43  ? 50  THR C N   1 
ATOM   1813 C CA  . THR C 1 51 ? 14.878  -35.562 25.227  1.00 36.08  ? 50  THR C CA  1 
ATOM   1814 C C   . THR C 1 51 ? 16.043  -36.562 25.171  1.00 31.59  ? 50  THR C C   1 
ATOM   1815 O O   . THR C 1 51 ? 15.907  -37.713 24.750  1.00 35.55  ? 50  THR C O   1 
ATOM   1816 C CB  . THR C 1 51 ? 14.370  -35.308 26.652  1.00 41.24  ? 50  THR C CB  1 
ATOM   1817 O OG1 . THR C 1 51 ? 13.830  -36.553 27.084  1.00 42.30  ? 50  THR C OG1 1 
ATOM   1818 C CG2 . THR C 1 51 ? 13.329  -34.204 26.759  1.00 37.19  ? 50  THR C CG2 1 
ATOM   1819 N N   . ALA C 1 52 ? 17.226  -36.090 25.538  1.00 33.91  ? 51  ALA C N   1 
ATOM   1820 C CA  . ALA C 1 52 ? 18.408  -36.942 25.611  1.00 32.07  ? 51  ALA C CA  1 
ATOM   1821 C C   . ALA C 1 52 ? 19.418  -36.258 26.515  1.00 34.72  ? 51  ALA C C   1 
ATOM   1822 O O   . ALA C 1 52 ? 19.269  -35.085 26.832  1.00 37.53  ? 51  ALA C O   1 
ATOM   1823 C CB  . ALA C 1 52 ? 18.981  -37.175 24.229  1.00 33.84  ? 51  ALA C CB  1 
ATOM   1824 N N   . PHE C 1 53 ? 20.455  -36.992 26.945  1.00 36.69  ? 52  PHE C N   1 
ATOM   1825 C CA  . PHE C 1 53 ? 21.568  -36.376 27.663  1.00 35.01  ? 52  PHE C CA  1 
ATOM   1826 C C   . PHE C 1 53 ? 22.736  -36.244 26.702  1.00 34.11  ? 52  PHE C C   1 
ATOM   1827 O O   . PHE C 1 53 ? 23.096  -37.213 26.026  1.00 34.21  ? 52  PHE C O   1 
ATOM   1828 C CB  . PHE C 1 53 ? 22.023  -37.316 28.793  1.00 32.78  ? 52  PHE C CB  1 
ATOM   1829 C CG  . PHE C 1 53 ? 21.068  -37.305 29.969  1.00 37.21  ? 52  PHE C CG  1 
ATOM   1830 C CD1 . PHE C 1 53 ? 20.794  -36.127 30.658  1.00 37.49  ? 52  PHE C CD1 1 
ATOM   1831 C CD2 . PHE C 1 53 ? 20.374  -38.458 30.324  1.00 47.63  ? 52  PHE C CD2 1 
ATOM   1832 C CE1 . PHE C 1 53 ? 19.907  -36.106 31.728  1.00 41.00  ? 52  PHE C CE1 1 
ATOM   1833 C CE2 . PHE C 1 53 ? 19.477  -38.430 31.385  1.00 47.32  ? 52  PHE C CE2 1 
ATOM   1834 C CZ  . PHE C 1 53 ? 19.238  -37.255 32.074  1.00 40.77  ? 52  PHE C CZ  1 
ATOM   1835 N N   . LEU C 1 54 ? 23.375  -35.065 26.682  1.00 29.50  ? 53  LEU C N   1 
ATOM   1836 C CA  . LEU C 1 54 ? 24.525  -34.876 25.813  1.00 30.58  ? 53  LEU C CA  1 
ATOM   1837 C C   . LEU C 1 54 ? 25.613  -34.108 26.559  1.00 30.59  ? 53  LEU C C   1 
ATOM   1838 O O   . LEU C 1 54 ? 25.319  -33.323 27.449  1.00 31.75  ? 53  LEU C O   1 
ATOM   1839 C CB  . LEU C 1 54 ? 24.145  -34.114 24.536  1.00 31.13  ? 53  LEU C CB  1 
ATOM   1840 C CG  . LEU C 1 54 ? 23.345  -34.853 23.463  1.00 32.04  ? 53  LEU C CG  1 
ATOM   1841 C CD1 . LEU C 1 54 ? 23.029  -33.867 22.369  1.00 30.30  ? 53  LEU C CD1 1 
ATOM   1842 C CD2 . LEU C 1 54 ? 24.171  -35.997 22.874  1.00 40.48  ? 53  LEU C CD2 1 
ATOM   1843 N N   . GLY C 1 55 ? 26.865  -34.328 26.158  1.00 33.09  ? 54  GLY C N   1 
ATOM   1844 C CA  . GLY C 1 55 ? 27.990  -33.609 26.723  1.00 31.12  ? 54  GLY C CA  1 
ATOM   1845 C C   . GLY C 1 55 ? 28.190  -32.261 26.034  1.00 39.16  ? 54  GLY C C   1 
ATOM   1846 O O   . GLY C 1 55 ? 27.687  -31.982 24.926  1.00 31.83  ? 54  GLY C O   1 
ATOM   1847 N N   . PRO C 1 56 ? 28.951  -31.359 26.685  1.00 37.68  ? 55  PRO C N   1 
ATOM   1848 C CA  . PRO C 1 56 ? 29.060  -29.986 26.199  1.00 37.74  ? 55  PRO C CA  1 
ATOM   1849 C C   . PRO C 1 56 ? 29.747  -29.918 24.832  1.00 36.99  ? 55  PRO C C   1 
ATOM   1850 O O   . PRO C 1 56 ? 29.530  -28.982 24.079  1.00 41.91  ? 55  PRO C O   1 
ATOM   1851 C CB  . PRO C 1 56 ? 29.812  -29.273 27.355  1.00 38.41  ? 55  PRO C CB  1 
ATOM   1852 C CG  . PRO C 1 56 ? 30.630  -30.391 27.977  1.00 37.58  ? 55  PRO C CG  1 
ATOM   1853 C CD  . PRO C 1 56 ? 29.741  -31.623 27.908  1.00 37.65  ? 55  PRO C CD  1 
ATOM   1854 N N   . LYS C 1 57 ? 30.504  -30.961 24.479  1.00 31.41  ? 56  LYS C N   1 
ATOM   1855 C CA  . LYS C 1 57 ? 31.194  -31.028 23.208  1.00 36.68  ? 56  LYS C CA  1 
ATOM   1856 C C   . LYS C 1 57 ? 30.174  -31.065 22.075  1.00 38.03  ? 56  LYS C C   1 
ATOM   1857 O O   . LYS C 1 57 ? 30.506  -30.713 20.946  1.00 35.76  ? 56  LYS C O   1 
ATOM   1858 C CB  . LYS C 1 57 ? 31.989  -32.328 23.022  1.00 38.40  ? 56  LYS C CB  1 
ATOM   1859 N N   . ASP C 1 58 ? 28.960  -31.537 22.396  1.00 33.33  ? 57  ASP C N   1 
ATOM   1860 C CA  . ASP C 1 58 ? 27.952  -31.845 21.387  1.00 34.13  ? 57  ASP C CA  1 
ATOM   1861 C C   . ASP C 1 58 ? 26.957  -30.705 21.252  1.00 32.78  ? 57  ASP C C   1 
ATOM   1862 O O   . ASP C 1 58 ? 25.957  -30.852 20.547  1.00 29.98  ? 57  ASP C O   1 
ATOM   1863 C CB  . ASP C 1 58 ? 27.206  -33.105 21.774  1.00 38.60  ? 57  ASP C CB  1 
ATOM   1864 C CG  . ASP C 1 58 ? 28.101  -34.331 21.729  1.00 43.86  ? 57  ASP C CG  1 
ATOM   1865 O OD1 . ASP C 1 58 ? 29.081  -34.279 20.984  1.00 47.46  ? 57  ASP C OD1 1 
ATOM   1866 O OD2 . ASP C 1 58 ? 27.822  -35.292 22.462  1.00 48.38  ? 57  ASP C OD2 1 
ATOM   1867 N N   . LEU C 1 59 ? 27.269  -29.576 21.892  1.00 27.89  ? 58  LEU C N   1 
ATOM   1868 C CA  . LEU C 1 59 ? 26.343  -28.457 22.027  1.00 31.70  ? 58  LEU C CA  1 
ATOM   1869 C C   . LEU C 1 59 ? 26.970  -27.166 21.516  1.00 34.92  ? 58  LEU C C   1 
ATOM   1870 O O   . LEU C 1 59 ? 28.128  -26.876 21.845  1.00 36.55  ? 58  LEU C O   1 
ATOM   1871 C CB  . LEU C 1 59 ? 25.973  -28.277 23.492  1.00 32.88  ? 58  LEU C CB  1 
ATOM   1872 C CG  . LEU C 1 59 ? 25.378  -29.508 24.171  1.00 30.76  ? 58  LEU C CG  1 
ATOM   1873 C CD1 . LEU C 1 59 ? 25.174  -29.096 25.623  1.00 32.90  ? 58  LEU C CD1 1 
ATOM   1874 C CD2 . LEU C 1 59 ? 24.056  -29.960 23.516  1.00 26.76  ? 58  LEU C CD2 1 
ATOM   1875 N N   . PHE C 1 60 ? 26.169  -26.382 20.775  1.00 37.24  ? 59  PHE C N   1 
ATOM   1876 C CA  . PHE C 1 60 ? 26.617  -25.145 20.134  1.00 33.25  ? 59  PHE C CA  1 
ATOM   1877 C C   . PHE C 1 60 ? 25.618  -24.030 20.423  1.00 36.83  ? 59  PHE C C   1 
ATOM   1878 O O   . PHE C 1 60 ? 24.440  -24.201 20.160  1.00 31.85  ? 59  PHE C O   1 
ATOM   1879 C CB  . PHE C 1 60 ? 26.775  -25.429 18.634  1.00 32.97  ? 59  PHE C CB  1 
ATOM   1880 C CG  . PHE C 1 60 ? 27.711  -26.589 18.326  1.00 31.76  ? 59  PHE C CG  1 
ATOM   1881 C CD1 . PHE C 1 60 ? 27.286  -27.915 18.410  1.00 30.12  ? 59  PHE C CD1 1 
ATOM   1882 C CD2 . PHE C 1 60 ? 29.052  -26.348 18.002  1.00 39.53  ? 59  PHE C CD2 1 
ATOM   1883 C CE1 . PHE C 1 60 ? 28.164  -28.969 18.170  1.00 29.55  ? 59  PHE C CE1 1 
ATOM   1884 C CE2 . PHE C 1 60 ? 29.923  -27.408 17.743  1.00 33.94  ? 59  PHE C CE2 1 
ATOM   1885 C CZ  . PHE C 1 60 ? 29.477  -28.708 17.832  1.00 36.13  ? 59  PHE C CZ  1 
ATOM   1886 N N   . PRO C 1 61 ? 25.997  -22.862 21.013  1.00 35.90  ? 60  PRO C N   1 
ATOM   1887 C CA  . PRO C 1 61 ? 24.991  -21.842 21.339  1.00 36.41  ? 60  PRO C CA  1 
ATOM   1888 C C   . PRO C 1 61 ? 24.268  -21.419 20.064  1.00 31.82  ? 60  PRO C C   1 
ATOM   1889 O O   . PRO C 1 61 ? 24.906  -21.282 19.017  1.00 39.58  ? 60  PRO C O   1 
ATOM   1890 C CB  . PRO C 1 61 ? 25.790  -20.671 21.981  1.00 38.88  ? 60  PRO C CB  1 
ATOM   1891 C CG  . PRO C 1 61 ? 27.150  -21.264 22.290  1.00 37.49  ? 60  PRO C CG  1 
ATOM   1892 C CD  . PRO C 1 61 ? 27.372  -22.481 21.389  1.00 42.76  ? 60  PRO C CD  1 
ATOM   1893 N N   . TYR C 1 62 ? 22.940  -21.259 20.172  1.00 35.36  ? 61  TYR C N   1 
ATOM   1894 C CA  . TYR C 1 62 ? 22.071  -21.001 19.029  1.00 36.10  ? 61  TYR C CA  1 
ATOM   1895 C C   . TYR C 1 62 ? 22.524  -19.751 18.272  1.00 40.87  ? 61  TYR C C   1 
ATOM   1896 O O   . TYR C 1 62 ? 22.686  -19.784 17.052  1.00 39.07  ? 61  TYR C O   1 
ATOM   1897 C CB  . TYR C 1 62 ? 20.608  -20.854 19.450  1.00 35.83  ? 61  TYR C CB  1 
ATOM   1898 C CG  . TYR C 1 62 ? 19.646  -20.485 18.331  1.00 38.30  ? 61  TYR C CG  1 
ATOM   1899 C CD1 . TYR C 1 62 ? 19.434  -21.355 17.257  1.00 37.64  ? 61  TYR C CD1 1 
ATOM   1900 C CD2 . TYR C 1 62 ? 18.933  -19.287 18.366  1.00 38.21  ? 61  TYR C CD2 1 
ATOM   1901 C CE1 . TYR C 1 62 ? 18.568  -21.019 16.224  1.00 37.95  ? 61  TYR C CE1 1 
ATOM   1902 C CE2 . TYR C 1 62 ? 18.064  -18.948 17.342  1.00 40.74  ? 61  TYR C CE2 1 
ATOM   1903 C CZ  . TYR C 1 62 ? 17.886  -19.812 16.269  1.00 40.14  ? 61  TYR C CZ  1 
ATOM   1904 O OH  . TYR C 1 62 ? 17.010  -19.472 15.271  1.00 41.26  ? 61  TYR C OH  1 
ATOM   1905 N N   . ASP C 1 63 ? 22.736  -18.647 18.996  1.00 44.48  ? 62  ASP C N   1 
ATOM   1906 C CA  . ASP C 1 63 ? 23.011  -17.387 18.315  1.00 49.96  ? 62  ASP C CA  1 
ATOM   1907 C C   . ASP C 1 63 ? 24.340  -17.436 17.565  1.00 44.86  ? 62  ASP C C   1 
ATOM   1908 O O   . ASP C 1 63 ? 24.431  -16.929 16.449  1.00 51.51  ? 62  ASP C O   1 
ATOM   1909 C CB  . ASP C 1 63 ? 22.811  -16.199 19.240  1.00 61.80  ? 62  ASP C CB  1 
ATOM   1910 C CG  . ASP C 1 63 ? 21.354  -15.793 19.412  1.00 76.65  ? 62  ASP C CG  1 
ATOM   1911 O OD1 . ASP C 1 63 ? 21.050  -15.132 20.424  1.00 78.77  ? 62  ASP C OD1 1 
ATOM   1912 O OD2 . ASP C 1 63 ? 20.537  -16.124 18.518  1.00 82.98  ? 62  ASP C OD2 1 
ATOM   1913 N N   . LYS C 1 64 ? 25.347  -18.075 18.162  1.00 40.57  ? 63  LYS C N   1 
ATOM   1914 C CA  . LYS C 1 64 ? 26.686  -18.158 17.590  1.00 37.28  ? 63  LYS C CA  1 
ATOM   1915 C C   . LYS C 1 64 ? 26.735  -19.083 16.376  1.00 38.74  ? 63  LYS C C   1 
ATOM   1916 O O   . LYS C 1 64 ? 27.594  -18.912 15.514  1.00 39.17  ? 63  LYS C O   1 
ATOM   1917 C CB  . LYS C 1 64 ? 27.741  -18.667 18.584  1.00 40.62  ? 63  LYS C CB  1 
ATOM   1918 N N   . SER C 1 65 ? 25.837  -20.085 16.300  1.00 35.25  ? 64  SER C N   1 
ATOM   1919 C CA  . SER C 1 65 ? 26.087  -21.158 15.338  1.00 31.90  ? 64  SER C CA  1 
ATOM   1920 C C   . SER C 1 65 ? 24.944  -21.282 14.315  1.00 34.23  ? 64  SER C C   1 
ATOM   1921 O O   . SER C 1 65 ? 25.021  -22.094 13.391  1.00 33.27  ? 64  SER C O   1 
ATOM   1922 C CB  . SER C 1 65 ? 26.373  -22.481 16.032  1.00 41.49  ? 64  SER C CB  1 
ATOM   1923 O OG  . SER C 1 65 ? 25.194  -23.013 16.619  1.00 37.90  ? 64  SER C OG  1 
ATOM   1924 N N   . LYS C 1 66 ? 23.884  -20.482 14.487  1.00 32.37  ? 65  LYS C N   1 
ATOM   1925 C CA  . LYS C 1 66 ? 22.725  -20.642 13.617  1.00 32.01  ? 65  LYS C CA  1 
ATOM   1926 C C   . LYS C 1 66 ? 23.065  -20.373 12.151  1.00 35.10  ? 65  LYS C C   1 
ATOM   1927 O O   . LYS C 1 66 ? 22.442  -20.956 11.284  1.00 32.53  ? 65  LYS C O   1 
ATOM   1928 C CB  . LYS C 1 66 ? 21.490  -19.824 13.986  1.00 34.97  ? 65  LYS C CB  1 
ATOM   1929 C CG  . LYS C 1 66 ? 21.754  -18.335 14.083  1.00 33.94  ? 65  LYS C CG  1 
ATOM   1930 C CD  . LYS C 1 66 ? 20.504  -17.628 14.588  1.00 41.29  ? 65  LYS C CD  1 
ATOM   1931 C CE  . LYS C 1 66 ? 20.696  -16.152 14.659  1.00 45.26  ? 65  LYS C CE  1 
ATOM   1932 N NZ  . LYS C 1 66 ? 19.558  -15.630 15.407  1.00 56.07  ? 65  LYS C NZ  1 
ATOM   1933 N N   . ASP C 1 67 ? 24.056  -19.518 11.866  1.00 37.70  ? 66  ASP C N   1 
ATOM   1934 C CA  . ASP C 1 67 ? 24.400  -19.232 10.475  1.00 38.61  ? 66  ASP C CA  1 
ATOM   1935 C C   . ASP C 1 67 ? 24.885  -20.519 9.802   1.00 37.93  ? 66  ASP C C   1 
ATOM   1936 O O   . ASP C 1 67 ? 24.624  -20.759 8.624   1.00 40.04  ? 66  ASP C O   1 
ATOM   1937 C CB  . ASP C 1 67 ? 25.278  -17.982 10.346  1.00 37.80  ? 66  ASP C CB  1 
ATOM   1938 C CG  . ASP C 1 67 ? 26.719  -18.112 10.843  1.00 51.34  ? 66  ASP C CG  1 
ATOM   1939 O OD1 . ASP C 1 67 ? 27.059  -19.176 11.417  1.00 54.43  ? 66  ASP C OD1 1 
ATOM   1940 O OD2 . ASP C 1 67 ? 27.501  -17.133 10.690  1.00 53.69  ? 66  ASP C OD2 1 
ATOM   1941 N N   . LYS C 1 68 ? 25.504  -21.410 10.581  1.00 32.77  ? 67  LYS C N   1 
ATOM   1942 C CA  . LYS C 1 68 ? 26.023  -22.667 10.070  1.00 31.26  ? 67  LYS C CA  1 
ATOM   1943 C C   . LYS C 1 68 ? 24.985  -23.805 10.092  1.00 33.84  ? 67  LYS C C   1 
ATOM   1944 O O   . LYS C 1 68 ? 24.880  -24.567 9.128   1.00 34.03  ? 67  LYS C O   1 
ATOM   1945 C CB  . LYS C 1 68 ? 27.246  -23.074 10.897  1.00 34.22  ? 67  LYS C CB  1 
ATOM   1946 C CG  . LYS C 1 68 ? 27.999  -24.315 10.425  1.00 40.46  ? 67  LYS C CG  1 
ATOM   1947 C CD  . LYS C 1 68 ? 29.278  -24.405 11.263  1.00 51.59  ? 67  LYS C CD  1 
ATOM   1948 C CE  . LYS C 1 68 ? 29.948  -25.742 11.365  1.00 58.54  ? 67  LYS C CE  1 
ATOM   1949 N NZ  . LYS C 1 68 ? 30.498  -26.241 10.103  1.00 65.21  ? 67  LYS C NZ  1 
ATOM   1950 N N   . TYR C 1 69 ? 24.253  -23.972 11.208  1.00 26.64  ? 68  TYR C N   1 
ATOM   1951 C CA  . TYR C 1 69 ? 23.427  -25.172 11.343  1.00 26.46  ? 68  TYR C CA  1 
ATOM   1952 C C   . TYR C 1 69 ? 21.942  -24.858 11.139  1.00 28.31  ? 68  TYR C C   1 
ATOM   1953 O O   . TYR C 1 69 ? 21.131  -25.776 11.031  1.00 28.34  ? 68  TYR C O   1 
ATOM   1954 C CB  . TYR C 1 69 ? 23.569  -25.804 12.737  1.00 26.16  ? 68  TYR C CB  1 
ATOM   1955 C CG  . TYR C 1 69 ? 24.991  -26.221 13.060  1.00 28.67  ? 68  TYR C CG  1 
ATOM   1956 C CD1 . TYR C 1 69 ? 25.735  -27.017 12.194  1.00 28.55  ? 68  TYR C CD1 1 
ATOM   1957 C CD2 . TYR C 1 69 ? 25.572  -25.787 14.248  1.00 30.66  ? 68  TYR C CD2 1 
ATOM   1958 C CE1 . TYR C 1 69 ? 27.028  -27.420 12.511  1.00 30.07  ? 68  TYR C CE1 1 
ATOM   1959 C CE2 . TYR C 1 69 ? 26.861  -26.182 14.566  1.00 33.49  ? 68  TYR C CE2 1 
ATOM   1960 C CZ  . TYR C 1 69 ? 27.578  -26.988 13.700  1.00 34.52  ? 68  TYR C CZ  1 
ATOM   1961 O OH  . TYR C 1 69 ? 28.860  -27.277 14.106  1.00 39.17  ? 68  TYR C OH  1 
ATOM   1962 N N   . GLY C 1 70 ? 21.573  -23.567 11.153  1.00 27.47  ? 69  GLY C N   1 
ATOM   1963 C CA  . GLY C 1 70 ? 20.158  -23.223 11.077  1.00 31.05  ? 69  GLY C CA  1 
ATOM   1964 C C   . GLY C 1 70 ? 19.763  -23.110 9.608   1.00 29.80  ? 69  GLY C C   1 
ATOM   1965 O O   . GLY C 1 70 ? 19.743  -22.026 9.033   1.00 32.62  ? 69  GLY C O   1 
ATOM   1966 N N   . LYS C 1 71 ? 19.624  -24.264 8.990   1.00 28.77  ? 70  LYS C N   1 
ATOM   1967 C CA  . LYS C 1 71 ? 19.230  -24.317 7.594   1.00 31.29  ? 70  LYS C CA  1 
ATOM   1968 C C   . LYS C 1 71 ? 18.353  -25.544 7.492   1.00 30.61  ? 70  LYS C C   1 
ATOM   1969 O O   . LYS C 1 71 ? 18.561  -26.519 8.218   1.00 30.48  ? 70  LYS C O   1 
ATOM   1970 C CB  . LYS C 1 71 ? 20.415  -24.464 6.634   1.00 32.90  ? 70  LYS C CB  1 
ATOM   1971 C CG  . LYS C 1 71 ? 21.418  -25.487 7.101   1.00 39.27  ? 70  LYS C CG  1 
ATOM   1972 C CD  . LYS C 1 71 ? 22.573  -25.918 6.207   1.00 45.75  ? 70  LYS C CD  1 
ATOM   1973 C CE  . LYS C 1 71 ? 23.473  -26.837 6.998   1.00 47.69  ? 70  LYS C CE  1 
ATOM   1974 N N   . PRO C 1 72 ? 17.359  -25.553 6.587   1.00 25.33  ? 71  PRO C N   1 
ATOM   1975 C CA  . PRO C 1 72 ? 16.424  -26.670 6.545   1.00 26.83  ? 71  PRO C CA  1 
ATOM   1976 C C   . PRO C 1 72 ? 17.068  -27.999 6.186   1.00 29.46  ? 71  PRO C C   1 
ATOM   1977 O O   . PRO C 1 72 ? 18.086  -28.063 5.480   1.00 30.65  ? 71  PRO C O   1 
ATOM   1978 C CB  . PRO C 1 72 ? 15.447  -26.240 5.457   1.00 29.63  ? 71  PRO C CB  1 
ATOM   1979 C CG  . PRO C 1 72 ? 15.536  -24.735 5.517   1.00 27.01  ? 71  PRO C CG  1 
ATOM   1980 C CD  . PRO C 1 72 ? 17.010  -24.431 5.702   1.00 27.81  ? 71  PRO C CD  1 
ATOM   1981 N N   . ASN C 1 73 ? 16.401  -29.045 6.622   1.00 29.10  ? 72  ASN C N   1 
ATOM   1982 C CA  . ASN C 1 73 ? 16.709  -30.332 6.027   1.00 35.71  ? 72  ASN C CA  1 
ATOM   1983 C C   . ASN C 1 73 ? 15.485  -31.213 6.175   1.00 32.15  ? 72  ASN C C   1 
ATOM   1984 O O   . ASN C 1 73 ? 14.522  -30.812 6.824   1.00 29.76  ? 72  ASN C O   1 
ATOM   1985 C CB  . ASN C 1 73 ? 18.048  -30.896 6.487   1.00 43.98  ? 72  ASN C CB  1 
ATOM   1986 C CG  . ASN C 1 73 ? 17.946  -31.530 7.847   1.00 38.66  ? 72  ASN C CG  1 
ATOM   1987 O OD1 . ASN C 1 73 ? 17.251  -32.545 8.015   1.00 37.92  ? 72  ASN C OD1 1 
ATOM   1988 N ND2 . ASN C 1 73 ? 18.679  -30.970 8.790   1.00 44.36  ? 72  ASN C ND2 1 
ATOM   1989 N N   . LYS C 1 74 ? 15.512  -32.377 5.524   1.00 32.33  ? 73  LYS C N   1 
ATOM   1990 C CA  . LYS C 1 74 ? 14.253  -33.085 5.359   1.00 30.12  ? 73  LYS C CA  1 
ATOM   1991 C C   . LYS C 1 74 ? 14.030  -34.092 6.473   1.00 32.41  ? 73  LYS C C   1 
ATOM   1992 O O   . LYS C 1 74 ? 13.042  -34.822 6.444   1.00 37.19  ? 73  LYS C O   1 
ATOM   1993 C CB  . LYS C 1 74 ? 14.154  -33.701 3.955   1.00 35.39  ? 73  LYS C CB  1 
ATOM   1994 C CG  . LYS C 1 74 ? 13.251  -32.862 3.008   1.00 42.68  ? 73  LYS C CG  1 
ATOM   1995 C CD  . LYS C 1 74 ? 13.997  -31.920 2.077   1.00 52.23  ? 73  LYS C CD  1 
ATOM   1996 N N   . ARG C 1 75 ? 14.901  -34.111 7.501   1.00 27.27  ? 74  ARG C N   1 
ATOM   1997 C CA  . ARG C 1 75 ? 14.697  -35.096 8.556   1.00 27.53  ? 74  ARG C CA  1 
ATOM   1998 C C   . ARG C 1 75 ? 13.410  -34.778 9.314   1.00 29.32  ? 74  ARG C C   1 
ATOM   1999 O O   . ARG C 1 75 ? 13.105  -33.615 9.597   1.00 29.41  ? 74  ARG C O   1 
ATOM   2000 C CB  . ARG C 1 75 ? 15.849  -35.190 9.584   1.00 31.09  ? 74  ARG C CB  1 
ATOM   2001 C CG  . ARG C 1 75 ? 17.218  -35.409 8.946   1.00 35.76  ? 74  ARG C CG  1 
ATOM   2002 C CD  . ARG C 1 75 ? 17.479  -36.788 8.279   1.00 38.69  ? 74  ARG C CD  1 
ATOM   2003 N NE  . ARG C 1 75 ? 17.488  -37.786 9.352   1.00 36.09  ? 74  ARG C NE  1 
ATOM   2004 C CZ  . ARG C 1 75 ? 18.630  -38.193 9.946   1.00 35.16  ? 74  ARG C CZ  1 
ATOM   2005 N NH1 . ARG C 1 75 ? 18.576  -38.781 11.116  1.00 38.69  ? 74  ARG C NH1 1 
ATOM   2006 N NH2 . ARG C 1 75 ? 19.797  -37.869 9.437   1.00 33.68  ? 74  ARG C NH2 1 
ATOM   2007 N N   . LYS C 1 76 ? 12.719  -35.854 9.712   1.00 31.07  ? 75  LYS C N   1 
ATOM   2008 C CA  . LYS C 1 76 ? 11.459  -35.788 10.435  1.00 34.43  ? 75  LYS C CA  1 
ATOM   2009 C C   . LYS C 1 76 ? 11.539  -34.789 11.585  1.00 31.84  ? 75  LYS C C   1 
ATOM   2010 O O   . LYS C 1 76 ? 12.313  -34.930 12.546  1.00 32.03  ? 75  LYS C O   1 
ATOM   2011 C CB  . LYS C 1 76 ? 10.887  -37.142 10.880  1.00 39.68  ? 75  LYS C CB  1 
ATOM   2012 C CG  . LYS C 1 76 ? 9.353   -37.167 10.868  1.00 48.73  ? 75  LYS C CG  1 
ATOM   2013 C CD  . LYS C 1 76 ? 8.657   -38.063 11.893  1.00 47.62  ? 75  LYS C CD  1 
ATOM   2014 N N   . GLY C 1 77 ? 10.715  -33.740 11.483  1.00 32.49  ? 76  GLY C N   1 
ATOM   2015 C CA  . GLY C 1 77 ? 10.583  -32.840 12.620  1.00 29.73  ? 76  GLY C CA  1 
ATOM   2016 C C   . GLY C 1 77 ? 11.537  -31.645 12.568  1.00 25.37  ? 76  GLY C C   1 
ATOM   2017 O O   . GLY C 1 77 ? 11.392  -30.710 13.356  1.00 28.19  ? 76  GLY C O   1 
ATOM   2018 N N   . PHE C 1 78 ? 12.517  -31.673 11.657  1.00 26.94  ? 77  PHE C N   1 
ATOM   2019 C CA  . PHE C 1 78 ? 13.611  -30.725 11.755  1.00 25.66  ? 77  PHE C CA  1 
ATOM   2020 C C   . PHE C 1 78 ? 13.082  -29.304 11.505  1.00 26.60  ? 77  PHE C C   1 
ATOM   2021 O O   . PHE C 1 78 ? 13.420  -28.362 12.198  1.00 26.34  ? 77  PHE C O   1 
ATOM   2022 C CB  . PHE C 1 78 ? 14.696  -31.053 10.731  1.00 27.79  ? 77  PHE C CB  1 
ATOM   2023 C CG  . PHE C 1 78 ? 15.975  -30.279 11.001  1.00 27.04  ? 77  PHE C CG  1 
ATOM   2024 C CD1 . PHE C 1 78 ? 16.158  -29.013 10.472  1.00 23.96  ? 77  PHE C CD1 1 
ATOM   2025 C CD2 . PHE C 1 78 ? 16.978  -30.804 11.820  1.00 27.13  ? 77  PHE C CD2 1 
ATOM   2026 C CE1 . PHE C 1 78 ? 17.342  -28.302 10.683  1.00 27.55  ? 77  PHE C CE1 1 
ATOM   2027 C CE2 . PHE C 1 78 ? 18.157  -30.085 12.056  1.00 27.25  ? 77  PHE C CE2 1 
ATOM   2028 C CZ  . PHE C 1 78 ? 18.320  -28.831 11.520  1.00 24.87  ? 77  PHE C CZ  1 
ATOM   2029 N N   . ASN C 1 79 ? 12.332  -29.136 10.417  1.00 26.44  ? 78  ASN C N   1 
ATOM   2030 C CA  . ASN C 1 79 ? 12.003  -27.780 10.004  1.00 27.24  ? 78  ASN C CA  1 
ATOM   2031 C C   . ASN C 1 79 ? 11.015  -27.146 10.975  1.00 27.42  ? 78  ASN C C   1 
ATOM   2032 O O   . ASN C 1 79 ? 11.098  -25.941 11.252  1.00 25.54  ? 78  ASN C O   1 
ATOM   2033 C CB  . ASN C 1 79 ? 11.506  -27.756 8.567   1.00 27.33  ? 78  ASN C CB  1 
ATOM   2034 C CG  . ASN C 1 79 ? 12.606  -28.177 7.625   1.00 27.75  ? 78  ASN C CG  1 
ATOM   2035 O OD1 . ASN C 1 79 ? 13.780  -27.923 7.916   1.00 27.76  ? 78  ASN C OD1 1 
ATOM   2036 N ND2 . ASN C 1 79 ? 12.257  -28.731 6.477   1.00 28.03  ? 78  ASN C ND2 1 
ATOM   2037 N N   . GLU C 1 80 ? 10.103  -27.959 11.509  1.00 31.06  ? 79  GLU C N   1 
ATOM   2038 C CA  . GLU C 1 80 ? 9.224   -27.495 12.574  1.00 28.33  ? 79  GLU C CA  1 
ATOM   2039 C C   . GLU C 1 80 ? 10.042  -27.091 13.793  1.00 29.52  ? 79  GLU C C   1 
ATOM   2040 O O   . GLU C 1 80 ? 9.757   -26.072 14.419  1.00 26.68  ? 79  GLU C O   1 
ATOM   2041 C CB  . GLU C 1 80 ? 8.177   -28.552 12.933  1.00 32.24  ? 79  GLU C CB  1 
ATOM   2042 C CG  . GLU C 1 80 ? 7.202   -28.066 13.999  1.00 30.97  ? 79  GLU C CG  1 
ATOM   2043 C CD  . GLU C 1 80 ? 5.935   -28.899 14.128  1.00 46.57  ? 79  GLU C CD  1 
ATOM   2044 O OE1 . GLU C 1 80 ? 5.840   -29.995 13.531  1.00 46.77  ? 79  GLU C OE1 1 
ATOM   2045 O OE2 . GLU C 1 80 ? 5.014   -28.420 14.820  1.00 45.07  ? 79  GLU C OE2 1 
ATOM   2046 N N   . GLY C 1 81 ? 11.144  -27.832 14.065  1.00 27.38  ? 80  GLY C N   1 
ATOM   2047 C CA  . GLY C 1 81 ? 12.038  -27.456 15.157  1.00 25.29  ? 80  GLY C CA  1 
ATOM   2048 C C   . GLY C 1 81 ? 12.731  -26.118 14.902  1.00 25.19  ? 80  GLY C C   1 
ATOM   2049 O O   . GLY C 1 81 ? 12.961  -25.334 15.817  1.00 25.36  ? 80  GLY C O   1 
ATOM   2050 N N   . LEU C 1 82 ? 13.098  -25.874 13.636  1.00 24.64  ? 81  LEU C N   1 
ATOM   2051 C CA  . LEU C 1 82 ? 13.701  -24.588 13.314  1.00 27.40  ? 81  LEU C CA  1 
ATOM   2052 C C   . LEU C 1 82 ? 12.695  -23.458 13.561  1.00 24.73  ? 81  LEU C C   1 
ATOM   2053 O O   . LEU C 1 82 ? 13.095  -22.354 13.966  1.00 27.41  ? 81  LEU C O   1 
ATOM   2054 C CB  . LEU C 1 82 ? 14.149  -24.604 11.843  1.00 27.74  ? 81  LEU C CB  1 
ATOM   2055 C CG  . LEU C 1 82 ? 15.443  -25.332 11.481  1.00 26.83  ? 81  LEU C CG  1 
ATOM   2056 C CD1 . LEU C 1 82 ? 15.714  -25.184 9.970   1.00 25.61  ? 81  LEU C CD1 1 
ATOM   2057 C CD2 . LEU C 1 82 ? 16.659  -24.809 12.222  1.00 24.80  ? 81  LEU C CD2 1 
ATOM   2058 N N   . TRP C 1 83 ? 11.423  -23.702 13.255  1.00 25.63  ? 82  TRP C N   1 
ATOM   2059 C CA  . TRP C 1 83 ? 10.404  -22.676 13.494  1.00 28.99  ? 82  TRP C CA  1 
ATOM   2060 C C   . TRP C 1 83 ? 10.230  -22.433 14.995  1.00 27.35  ? 82  TRP C C   1 
ATOM   2061 O O   . TRP C 1 83 ? 10.225  -21.294 15.447  1.00 29.60  ? 82  TRP C O   1 
ATOM   2062 C CB  . TRP C 1 83 ? 9.065   -23.013 12.841  1.00 31.12  ? 82  TRP C CB  1 
ATOM   2063 C CG  . TRP C 1 83 ? 8.037   -21.913 12.995  1.00 34.72  ? 82  TRP C CG  1 
ATOM   2064 C CD1 . TRP C 1 83 ? 7.769   -20.893 12.121  1.00 33.55  ? 82  TRP C CD1 1 
ATOM   2065 C CD2 . TRP C 1 83 ? 7.122   -21.740 14.106  1.00 31.12  ? 82  TRP C CD2 1 
ATOM   2066 N NE1 . TRP C 1 83 ? 6.777   -20.090 12.617  1.00 33.30  ? 82  TRP C NE1 1 
ATOM   2067 C CE2 . TRP C 1 83 ? 6.357   -20.578 13.826  1.00 33.99  ? 82  TRP C CE2 1 
ATOM   2068 C CE3 . TRP C 1 83 ? 6.907   -22.430 15.309  1.00 33.01  ? 82  TRP C CE3 1 
ATOM   2069 C CZ2 . TRP C 1 83 ? 5.370   -20.121 14.695  1.00 39.35  ? 82  TRP C CZ2 1 
ATOM   2070 C CZ3 . TRP C 1 83 ? 5.916   -21.984 16.161  1.00 37.71  ? 82  TRP C CZ3 1 
ATOM   2071 C CH2 . TRP C 1 83 ? 5.164   -20.847 15.854  1.00 40.88  ? 82  TRP C CH2 1 
ATOM   2072 N N   . GLU C 1 84 ? 10.214  -23.515 15.785  1.00 29.13  ? 83  GLU C N   1 
ATOM   2073 C CA  . GLU C 1 84 ? 10.057  -23.342 17.231  1.00 28.20  ? 83  GLU C CA  1 
ATOM   2074 C C   . GLU C 1 84 ? 11.200  -22.571 17.883  1.00 30.11  ? 83  GLU C C   1 
ATOM   2075 O O   . GLU C 1 84 ? 10.962  -21.699 18.728  1.00 30.71  ? 83  GLU C O   1 
ATOM   2076 C CB  . GLU C 1 84 ? 9.959   -24.681 17.955  1.00 27.93  ? 83  GLU C CB  1 
ATOM   2077 C CG  . GLU C 1 84 ? 8.712   -25.429 17.499  1.00 31.25  ? 83  GLU C CG  1 
ATOM   2078 C CD  . GLU C 1 84 ? 8.623   -26.841 18.024  1.00 36.43  ? 83  GLU C CD  1 
ATOM   2079 O OE1 . GLU C 1 84 ? 9.636   -27.224 18.644  1.00 32.90  ? 83  GLU C OE1 1 
ATOM   2080 O OE2 . GLU C 1 84 ? 7.571   -27.516 17.817  1.00 39.17  ? 83  GLU C OE2 1 
ATOM   2081 N N   . ILE C 1 85 ? 12.455  -22.879 17.510  1.00 29.44  ? 84  ILE C N   1 
ATOM   2082 C CA  . ILE C 1 85 ? 13.613  -22.273 18.140  1.00 29.12  ? 84  ILE C CA  1 
ATOM   2083 C C   . ILE C 1 85 ? 13.667  -20.760 17.911  1.00 30.05  ? 84  ILE C C   1 
ATOM   2084 O O   . ILE C 1 85 ? 14.170  -20.032 18.750  1.00 29.33  ? 84  ILE C O   1 
ATOM   2085 C CB  . ILE C 1 85 ? 14.939  -22.973 17.795  1.00 28.04  ? 84  ILE C CB  1 
ATOM   2086 C CG1 . ILE C 1 85 ? 16.063  -22.552 18.759  1.00 31.69  ? 84  ILE C CG1 1 
ATOM   2087 C CG2 . ILE C 1 85 ? 15.348  -22.816 16.324  1.00 28.47  ? 84  ILE C CG2 1 
ATOM   2088 C CD1 . ILE C 1 85 ? 17.248  -23.508 18.786  1.00 29.98  ? 84  ILE C CD1 1 
ATOM   2089 N N   . GLN C 1 86 ? 13.262  -20.320 16.718  1.00 28.40  ? 85  GLN C N   1 
ATOM   2090 C CA  . GLN C 1 86 ? 13.270  -18.914 16.346  1.00 28.26  ? 85  GLN C CA  1 
ATOM   2091 C C   . GLN C 1 86 ? 12.011  -18.188 16.841  1.00 30.80  ? 85  GLN C C   1 
ATOM   2092 O O   . GLN C 1 86 ? 12.099  -17.009 17.196  1.00 34.94  ? 85  GLN C O   1 
ATOM   2093 C CB  . GLN C 1 86 ? 13.227  -18.814 14.813  1.00 28.88  ? 85  GLN C CB  1 
ATOM   2094 C CG  . GLN C 1 86 ? 13.547  -17.407 14.282  1.00 32.44  ? 85  GLN C CG  1 
ATOM   2095 C CD  . GLN C 1 86 ? 14.079  -17.438 12.853  1.00 35.32  ? 85  GLN C CD  1 
ATOM   2096 O OE1 . GLN C 1 86 ? 13.983  -18.445 12.142  1.00 36.88  ? 85  GLN C OE1 1 
ATOM   2097 N NE2 . GLN C 1 86 ? 14.672  -16.338 12.421  1.00 38.01  ? 85  GLN C NE2 1 
ATOM   2098 N N   . ASN C 1 87 ? 10.865  -18.875 16.885  1.00 32.09  ? 86  ASN C N   1 
ATOM   2099 C CA  . ASN C 1 87 ? 9.558   -18.231 17.021  1.00 36.04  ? 86  ASN C CA  1 
ATOM   2100 C C   . ASN C 1 87 ? 8.816   -18.566 18.324  1.00 38.66  ? 86  ASN C C   1 
ATOM   2101 O O   . ASN C 1 87 ? 7.854   -17.871 18.653  1.00 39.01  ? 86  ASN C O   1 
ATOM   2102 C CB  . ASN C 1 87 ? 8.620   -18.525 15.855  1.00 33.91  ? 86  ASN C CB  1 
ATOM   2103 C CG  . ASN C 1 87 ? 9.199   -17.915 14.600  1.00 35.89  ? 86  ASN C CG  1 
ATOM   2104 O OD1 . ASN C 1 87 ? 9.321   -16.686 14.522  1.00 37.71  ? 86  ASN C OD1 1 
ATOM   2105 N ND2 . ASN C 1 87 ? 9.649   -18.744 13.674  1.00 32.61  ? 86  ASN C ND2 1 
ATOM   2106 N N   . ASN C 1 88 ? 9.178   -19.644 19.036  1.00 38.37  ? 87  ASN C N   1 
ATOM   2107 C CA  . ASN C 1 88 ? 8.421   -20.013 20.242  1.00 33.91  ? 87  ASN C CA  1 
ATOM   2108 C C   . ASN C 1 88 ? 9.279   -20.921 21.117  1.00 41.73  ? 87  ASN C C   1 
ATOM   2109 O O   . ASN C 1 88 ? 8.864   -22.047 21.429  1.00 45.09  ? 87  ASN C O   1 
ATOM   2110 C CB  . ASN C 1 88 ? 7.160   -20.817 19.901  1.00 37.79  ? 87  ASN C CB  1 
ATOM   2111 C CG  . ASN C 1 88 ? 6.080   -20.800 20.970  1.00 46.35  ? 87  ASN C CG  1 
ATOM   2112 O OD1 . ASN C 1 88 ? 6.111   -19.978 21.890  1.00 48.06  ? 87  ASN C OD1 1 
ATOM   2113 N ND2 . ASN C 1 88 ? 5.091   -21.678 20.854  1.00 46.28  ? 87  ASN C ND2 1 
ATOM   2114 N N   . PRO C 1 89 ? 10.502  -20.479 21.490  1.00 36.35  ? 88  PRO C N   1 
ATOM   2115 C CA  . PRO C 1 89 ? 11.512  -21.369 22.059  1.00 36.93  ? 88  PRO C CA  1 
ATOM   2116 C C   . PRO C 1 89 ? 11.273  -21.818 23.496  1.00 42.44  ? 88  PRO C C   1 
ATOM   2117 O O   . PRO C 1 89 ? 12.039  -22.645 24.006  1.00 39.98  ? 88  PRO C O   1 
ATOM   2118 C CB  . PRO C 1 89 ? 12.818  -20.575 21.941  1.00 31.63  ? 88  PRO C CB  1 
ATOM   2119 C CG  . PRO C 1 89 ? 12.390  -19.136 21.923  1.00 36.97  ? 88  PRO C CG  1 
ATOM   2120 C CD  . PRO C 1 89 ? 11.011  -19.118 21.287  1.00 37.73  ? 88  PRO C CD  1 
ATOM   2121 N N   . HIS C 1 90 ? 10.243  -21.249 24.140  1.00 43.98  ? 89  HIS C N   1 
ATOM   2122 C CA  . HIS C 1 90 ? 9.985   -21.547 25.545  1.00 42.01  ? 89  HIS C CA  1 
ATOM   2123 C C   . HIS C 1 90 ? 8.552   -22.009 25.808  1.00 44.87  ? 89  HIS C C   1 
ATOM   2124 O O   . HIS C 1 90 ? 8.171   -22.128 26.968  1.00 48.39  ? 89  HIS C O   1 
ATOM   2125 C CB  . HIS C 1 90 ? 10.439  -20.418 26.475  1.00 40.63  ? 89  HIS C CB  1 
ATOM   2126 C CG  . HIS C 1 90 ? 11.851  -19.963 26.291  1.00 42.92  ? 89  HIS C CG  1 
ATOM   2127 N ND1 . HIS C 1 90 ? 12.960  -20.749 26.534  1.00 43.92  ? 89  HIS C ND1 1 
ATOM   2128 C CD2 . HIS C 1 90 ? 12.326  -18.790 25.863  1.00 42.96  ? 89  HIS C CD2 1 
ATOM   2129 C CE1 . HIS C 1 90 ? 14.069  -20.053 26.284  1.00 41.80  ? 89  HIS C CE1 1 
ATOM   2130 N NE2 . HIS C 1 90 ? 13.705  -18.858 25.863  1.00 40.54  ? 89  HIS C NE2 1 
ATOM   2131 N N   . ALA C 1 91 ? 7.770   -22.311 24.760  1.00 45.21  ? 90  ALA C N   1 
ATOM   2132 C CA  . ALA C 1 91 ? 6.501   -23.014 24.929  1.00 52.47  ? 90  ALA C CA  1 
ATOM   2133 C C   . ALA C 1 91 ? 6.751   -24.396 25.545  1.00 58.45  ? 90  ALA C C   1 
ATOM   2134 O O   . ALA C 1 91 ? 7.904   -24.799 25.707  1.00 59.15  ? 90  ALA C O   1 
ATOM   2135 C CB  . ALA C 1 91 ? 5.745   -23.099 23.614  1.00 50.32  ? 90  ALA C CB  1 
ATOM   2136 N N   . SER C 1 92 ? 5.667   -25.119 25.871  1.00 67.95  ? 91  SER C N   1 
ATOM   2137 C CA  . SER C 1 92 ? 5.722   -26.321 26.698  1.00 66.01  ? 91  SER C CA  1 
ATOM   2138 C C   . SER C 1 92 ? 5.964   -27.584 25.873  1.00 67.56  ? 91  SER C C   1 
ATOM   2139 O O   . SER C 1 92 ? 6.811   -28.401 26.234  1.00 64.40  ? 91  SER C O   1 
ATOM   2140 C CB  . SER C 1 92 ? 4.468   -26.473 27.528  1.00 69.73  ? 91  SER C CB  1 
ATOM   2141 O OG  . SER C 1 92 ? 4.322   -25.395 28.440  1.00 70.21  ? 91  SER C OG  1 
ATOM   2142 N N   . TYR C 1 93 ? 5.161   -27.754 24.811  1.00 65.48  ? 92  TYR C N   1 
ATOM   2143 C CA  . TYR C 1 93 ? 5.174   -28.928 23.949  1.00 68.31  ? 92  TYR C CA  1 
ATOM   2144 C C   . TYR C 1 93 ? 5.026   -30.211 24.798  1.00 76.20  ? 92  TYR C C   1 
ATOM   2145 O O   . TYR C 1 93 ? 3.885   -30.621 25.149  1.00 79.22  ? 92  TYR C O   1 
ATOM   2146 C CB  . TYR C 1 93 ? 6.429   -28.944 23.067  1.00 68.07  ? 92  TYR C CB  1 
ATOM   2147 C CG  . TYR C 1 93 ? 6.711   -27.665 22.280  1.00 64.16  ? 92  TYR C CG  1 
ATOM   2148 C CD1 . TYR C 1 93 ? 6.033   -27.387 21.092  1.00 56.17  ? 92  TYR C CD1 1 
ATOM   2149 C CD2 . TYR C 1 93 ? 7.661   -26.743 22.716  1.00 57.50  ? 92  TYR C CD2 1 
ATOM   2150 C CE1 . TYR C 1 93 ? 6.285   -26.232 20.369  1.00 49.48  ? 92  TYR C CE1 1 
ATOM   2151 C CE2 . TYR C 1 93 ? 7.931   -25.588 21.993  1.00 50.86  ? 92  TYR C CE2 1 
ATOM   2152 C CZ  . TYR C 1 93 ? 7.237   -25.332 20.822  1.00 51.51  ? 92  TYR C CZ  1 
ATOM   2153 O OH  . TYR C 1 93 ? 7.485   -24.185 20.116  1.00 52.09  ? 92  TYR C OH  1 
HETATM 2154 S S   . SO4 D 2 .  ? 0.923   -33.676 1.824   1.00 82.44  ? 101 SO4 A S   1 
HETATM 2155 O O1  . SO4 D 2 .  ? 1.405   -34.361 0.649   1.00 68.41  ? 101 SO4 A O1  1 
HETATM 2156 O O2  . SO4 D 2 .  ? 1.069   -32.255 1.640   1.00 88.40  ? 101 SO4 A O2  1 
HETATM 2157 O O3  . SO4 D 2 .  ? -0.469  -33.988 2.046   1.00 91.40  ? 101 SO4 A O3  1 
HETATM 2158 O O4  . SO4 D 2 .  ? 1.684   -34.090 2.967   1.00 76.95  ? 101 SO4 A O4  1 
HETATM 2159 S S   . SO4 E 2 .  ? -10.120 -24.614 1.101   1.00 98.29  ? 102 SO4 A S   1 
HETATM 2160 O O1  . SO4 E 2 .  ? -9.965  -24.388 -0.312  1.00 93.52  ? 102 SO4 A O1  1 
HETATM 2161 O O2  . SO4 E 2 .  ? -10.157 -23.351 1.792   1.00 94.75  ? 102 SO4 A O2  1 
HETATM 2162 O O3  . SO4 E 2 .  ? -11.350 -25.330 1.330   1.00 105.08 ? 102 SO4 A O3  1 
HETATM 2163 O O4  . SO4 E 2 .  ? -9.012  -25.390 1.596   1.00 90.47  ? 102 SO4 A O4  1 
HETATM 2164 C C1  . EDO F 3 .  ? 13.571  -19.472 -7.415  1.00 38.00  ? 103 EDO A C1  1 
HETATM 2165 O O1  . EDO F 3 .  ? 14.802  -18.750 -7.267  1.00 29.96  ? 103 EDO A O1  1 
HETATM 2166 C C2  . EDO F 3 .  ? 12.690  -19.006 -8.535  1.00 32.41  ? 103 EDO A C2  1 
HETATM 2167 O O2  . EDO F 3 .  ? 12.163  -17.722 -8.322  1.00 31.17  ? 103 EDO A O2  1 
HETATM 2168 S S   . SO4 G 2 .  ? 8.563   -29.440 5.813   1.00 50.04  ? 104 SO4 A S   1 
HETATM 2169 O O1  . SO4 G 2 .  ? 9.199   -28.514 4.953   1.00 45.37  ? 104 SO4 A O1  1 
HETATM 2170 O O2  . SO4 G 2 .  ? 8.207   -30.628 5.046   1.00 60.21  ? 104 SO4 A O2  1 
HETATM 2171 O O3  . SO4 G 2 .  ? 9.450   -29.784 6.899   1.00 53.31  ? 104 SO4 A O3  1 
HETATM 2172 O O4  . SO4 G 2 .  ? 7.344   -28.874 6.347   1.00 58.84  ? 104 SO4 A O4  1 
HETATM 2173 S S   . SO4 H 2 .  ? 7.205   -8.514  -24.646 1.00 59.54  ? 101 SO4 B S   1 
HETATM 2174 O O1  . SO4 H 2 .  ? 8.345   -8.480  -25.565 1.00 33.94  ? 101 SO4 B O1  1 
HETATM 2175 O O2  . SO4 H 2 .  ? 6.088   -9.110  -25.282 1.00 43.01  ? 101 SO4 B O2  1 
HETATM 2176 O O3  . SO4 H 2 .  ? 7.436   -9.298  -23.433 1.00 41.17  ? 101 SO4 B O3  1 
HETATM 2177 O O4  . SO4 H 2 .  ? 6.939   -7.129  -24.305 1.00 55.28  ? 101 SO4 B O4  1 
HETATM 2178 S S   . SO4 I 2 .  ? 14.188  -27.032 -26.374 1.00 52.51  ? 102 SO4 B S   1 
HETATM 2179 O O1  . SO4 I 2 .  ? 15.571  -26.771 -26.120 1.00 47.07  ? 102 SO4 B O1  1 
HETATM 2180 O O2  . SO4 I 2 .  ? 14.056  -28.346 -26.940 1.00 61.33  ? 102 SO4 B O2  1 
HETATM 2181 O O3  . SO4 I 2 .  ? 13.464  -26.950 -25.130 1.00 59.42  ? 102 SO4 B O3  1 
HETATM 2182 O O4  . SO4 I 2 .  ? 13.642  -26.064 -27.298 1.00 49.75  ? 102 SO4 B O4  1 
HETATM 2183 C C4  . NX7 J 4 .  ? 18.802  -15.141 -21.355 0.84 37.58  ? 103 NX7 B C4  1 
HETATM 2184 C C5  . NX7 J 4 .  ? 19.138  -14.813 -22.660 0.84 30.96  ? 103 NX7 B C5  1 
HETATM 2185 C C6  . NX7 J 4 .  ? 18.094  -14.486 -23.682 0.84 28.86  ? 103 NX7 B C6  1 
HETATM 2186 C C7  . NX7 J 4 .  ? 16.732  -15.252 -25.583 0.84 28.73  ? 103 NX7 B C7  1 
HETATM 2187 C C8  . NX7 J 4 .  ? 16.678  -16.606 -26.315 0.84 25.29  ? 103 NX7 B C8  1 
HETATM 2188 C C10 . NX7 J 4 .  ? 18.162  -16.856 -24.490 0.84 27.79  ? 103 NX7 B C10 1 
HETATM 2189 N N   . NX7 J 4 .  ? 17.699  -15.479 -24.503 0.84 27.87  ? 103 NX7 B N   1 
HETATM 2190 C C   . NX7 J 4 .  ? 20.483  -14.890 -22.973 0.84 35.76  ? 103 NX7 B C   1 
HETATM 2191 O O   . NX7 J 4 .  ? 17.607  -13.369 -23.720 0.84 34.13  ? 103 NX7 B O   1 
HETATM 2192 C C1  . NX7 J 4 .  ? 21.453  -15.262 -22.071 0.84 40.30  ? 103 NX7 B C1  1 
HETATM 2193 C C2  . NX7 J 4 .  ? 21.063  -15.566 -20.770 0.84 39.08  ? 103 NX7 B C2  1 
HETATM 2194 C C3  . NX7 J 4 .  ? 19.724  -15.503 -20.404 0.84 37.12  ? 103 NX7 B C3  1 
HETATM 2195 C C9  . NX7 J 4 .  ? 17.907  -17.312 -25.936 0.84 26.97  ? 103 NX7 B C9  1 
HETATM 2196 F F   . NX7 J 4 .  ? 20.834  -14.612 -24.246 0.84 37.67  ? 103 NX7 B F   1 
HETATM 2197 F F1  . NX7 J 4 .  ? 17.484  -15.096 -21.023 0.84 37.14  ? 103 NX7 B F1  1 
HETATM 2198 S S   . SO4 K 2 .  ? 28.790  -38.279 12.406  1.00 85.15  ? 101 SO4 C S   1 
HETATM 2199 O O1  . SO4 K 2 .  ? 29.974  -37.583 11.962  1.00 87.88  ? 101 SO4 C O1  1 
HETATM 2200 O O2  . SO4 K 2 .  ? 27.636  -37.742 11.740  1.00 78.48  ? 101 SO4 C O2  1 
HETATM 2201 O O3  . SO4 K 2 .  ? 28.902  -39.676 12.094  1.00 72.85  ? 101 SO4 C O3  1 
HETATM 2202 O O4  . SO4 K 2 .  ? 28.649  -38.115 13.832  1.00 93.02  ? 101 SO4 C O4  1 
HETATM 2203 C C4  . NX7 L 4 .  ? 15.862  -38.124 20.707  0.54 41.99  ? 102 NX7 C C4  1 
HETATM 2204 C C5  . NX7 L 4 .  ? 15.569  -38.143 19.350  0.54 38.59  ? 102 NX7 C C5  1 
HETATM 2205 C C6  . NX7 L 4 .  ? 15.548  -36.837 18.588  0.54 38.37  ? 102 NX7 C C6  1 
HETATM 2206 C C7  . NX7 L 4 .  ? 17.865  -37.340 17.888  0.54 34.02  ? 102 NX7 C C7  1 
HETATM 2207 C C8  . NX7 L 4 .  ? 18.952  -36.310 17.952  0.54 32.21  ? 102 NX7 C C8  1 
HETATM 2208 C C10 . NX7 L 4 .  ? 16.814  -35.296 17.131  0.54 34.55  ? 102 NX7 C C10 1 
HETATM 2209 N N   . NX7 L 4 .  ? 16.649  -36.527 17.905  0.54 36.45  ? 102 NX7 C N   1 
HETATM 2210 C C   . NX7 L 4 .  ? 15.471  -39.411 18.783  0.54 39.40  ? 102 NX7 C C   1 
HETATM 2211 O O   . NX7 L 4 .  ? 14.612  -36.063 18.656  0.54 31.90  ? 102 NX7 C O   1 
HETATM 2212 C C1  . NX7 L 4 .  ? 15.670  -40.576 19.488  0.54 42.05  ? 102 NX7 C C1  1 
HETATM 2213 C C2  . NX7 L 4 .  ? 15.969  -40.489 20.840  0.54 39.77  ? 102 NX7 C C2  1 
HETATM 2214 C C3  . NX7 L 4 .  ? 16.060  -39.257 21.463  0.54 39.41  ? 102 NX7 C C3  1 
HETATM 2215 C C9  . NX7 L 4 .  ? 18.343  -35.108 17.112  0.54 36.06  ? 102 NX7 C C9  1 
HETATM 2216 F F   . NX7 L 4 .  ? 15.133  -39.504 17.466  0.54 42.23  ? 102 NX7 C F   1 
HETATM 2217 F F1  . NX7 L 4 .  ? 15.995  -36.924 21.307  0.54 46.62  ? 102 NX7 C F1  1 
HETATM 2218 O O   . HOH M 5 .  ? 5.371   -28.909 6.821   1.00 43.90  ? 201 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? -2.595  -30.920 -3.811  1.00 63.90  ? 202 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 8.665   -32.022 3.545   1.00 56.24  ? 203 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? 3.698   -34.166 4.028   1.00 58.50  ? 204 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 9.711   -18.887 10.095  1.00 63.47  ? 205 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? 3.693   -10.263 13.541  1.00 48.69  ? 206 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 10.754  -9.152  -12.807 1.00 52.54  ? 207 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? -2.356  -9.669  4.481   1.00 51.71  ? 208 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? -0.831  -21.051 9.357   1.00 55.17  ? 209 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? -8.071  -16.958 6.557   1.00 38.14  ? 210 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? 10.527  -29.644 3.123   1.00 38.72  ? 211 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? 0.501   -24.799 13.755  1.00 49.55  ? 212 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? 0.519   -10.605 -15.626 1.00 47.97  ? 213 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? -4.189  -11.093 6.854   1.00 46.20  ? 214 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? 15.282  -24.454 2.050   1.00 39.92  ? 215 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 8.663   -18.142 -11.026 1.00 28.59  ? 216 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 16.938  -18.080 -9.780  1.00 42.03  ? 217 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? -9.571  -15.498 10.611  1.00 58.53  ? 218 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? -0.145  -33.774 4.818   1.00 55.69  ? 219 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? -6.413  -11.246 -11.393 1.00 37.95  ? 220 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 9.274   -6.000  -1.743  1.00 35.03  ? 221 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? 4.532   -1.440  -6.280  1.00 32.21  ? 222 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 10.633  -23.616 9.785   1.00 32.92  ? 223 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? -6.902  -5.273  9.265   1.00 36.16  ? 224 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? -2.745  3.297   -2.084  1.00 38.72  ? 225 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 8.125   -17.741 -15.815 1.00 53.28  ? 226 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? 12.473  -9.648  -7.249  1.00 44.43  ? 227 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 11.075  -12.016 5.855   1.00 34.84  ? 228 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 19.401  -15.593 7.273   1.00 28.07  ? 229 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? -8.267  -15.702 -1.035  1.00 35.11  ? 230 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 4.094   -3.498  -3.231  1.00 32.21  ? 231 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 2.193   -25.115 -10.093 1.00 36.08  ? 232 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? 4.178   -7.784  1.097   1.00 32.57  ? 233 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 10.455  -5.170  -7.801  1.00 33.99  ? 234 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 9.012   -22.692 -9.511  1.00 33.15  ? 235 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? -4.748  -21.122 6.081   1.00 41.62  ? 236 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 1.492   -4.646  -10.131 1.00 32.97  ? 237 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 6.652   -10.442 -12.155 1.00 39.17  ? 238 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? -1.132  -20.906 6.940   1.00 32.02  ? 239 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? -5.975  -13.945 -16.693 1.00 57.06  ? 240 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 16.801  -12.881 1.356   1.00 19.33  ? 241 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 1.616   -24.752 -6.370  1.00 51.06  ? 242 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? -6.052  -15.719 -8.153  1.00 28.01  ? 243 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? -6.151  -19.515 -5.660  1.00 36.86  ? 244 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? -8.388  -16.558 1.925   1.00 41.69  ? 245 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? -0.188  -23.120 9.196   1.00 39.80  ? 246 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? -1.205  -29.079 9.803   1.00 53.55  ? 247 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? -1.503  -11.579 11.341  1.00 38.39  ? 248 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? -2.161  -21.929 -0.661  1.00 25.96  ? 249 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 1.396   -18.453 -18.640 1.00 44.90  ? 250 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? -9.003  -21.029 -1.373  1.00 44.85  ? 251 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? 15.365  -12.117 -5.380  1.00 30.17  ? 252 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? -2.866  -11.574 13.891  1.00 48.78  ? 253 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? -8.145  -21.128 -5.278  1.00 62.14  ? 254 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 6.016   -16.150 -14.985 1.00 48.30  ? 255 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? 11.303  -16.590 -14.716 1.00 39.84  ? 256 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? 7.691   -8.252  4.512   1.00 39.19  ? 257 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 12.922  -28.195 -4.676  1.00 50.30  ? 258 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? 12.870  -11.976 -4.264  1.00 21.66  ? 259 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? 2.802   -29.636 -0.526  1.00 36.75  ? 260 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 14.044  -13.143 10.302  1.00 45.47  ? 261 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 8.004   -17.911 8.871   1.00 43.84  ? 262 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? -1.607  -7.393  11.346  1.00 41.94  ? 263 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? 11.158  -12.288 -6.118  1.00 27.44  ? 264 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? -3.271  -18.675 13.782  1.00 53.15  ? 265 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? -4.818  -25.725 -5.563  1.00 46.51  ? 266 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? 12.334  -13.254 -8.449  1.00 36.67  ? 267 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? -7.388  -9.987  -7.668  1.00 47.94  ? 268 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? 9.157   -30.439 9.706   1.00 34.74  ? 269 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 7.678   -7.876  1.222   1.00 27.08  ? 270 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 1.375   -10.322 11.661  1.00 32.65  ? 271 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? 9.659   -13.059 9.651   1.00 40.65  ? 272 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? 2.653   -9.968  -13.229 1.00 50.30  ? 273 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? 10.836  -5.961  -3.827  1.00 48.73  ? 274 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? -4.333  -8.072  10.451  1.00 47.80  ? 275 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? 2.015   -6.102  5.321   1.00 31.91  ? 276 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? 14.907  -28.101 -0.791  1.00 58.94  ? 277 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? 8.501   -16.376 -13.171 1.00 33.74  ? 278 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? 4.660   -7.435  3.915   1.00 32.16  ? 279 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? -6.411  -12.665 6.747   1.00 39.67  ? 280 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? -3.953  -27.000 6.653   1.00 55.23  ? 281 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? 12.779  -15.104 -12.056 1.00 44.94  ? 282 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? 5.934   -5.825  0.444   1.00 44.06  ? 283 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? 9.510   -20.351 -18.431 1.00 39.88  ? 284 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? 0.900   -28.719 -7.194  1.00 55.50  ? 285 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? 10.678  -7.848  0.356   1.00 23.74  ? 286 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? 20.968  -16.601 -3.465  1.00 27.52  ? 287 HOH A O   1 
HETATM 2305 O O   . HOH M 5 .  ? 16.764  -12.621 -16.700 1.00 42.28  ? 288 HOH A O   1 
HETATM 2306 O O   . HOH M 5 .  ? -11.825 -15.816 -4.122  1.00 55.38  ? 289 HOH A O   1 
HETATM 2307 O O   . HOH M 5 .  ? -7.601  -11.500 -8.078  1.00 30.68  ? 290 HOH A O   1 
HETATM 2308 O O   . HOH M 5 .  ? -6.067  -17.269 -9.936  1.00 50.48  ? 291 HOH A O   1 
HETATM 2309 O O   . HOH M 5 .  ? -8.277  -19.570 -3.416  1.00 43.14  ? 292 HOH A O   1 
HETATM 2310 O O   . HOH M 5 .  ? 21.912  -16.552 -0.490  1.00 37.65  ? 293 HOH A O   1 
HETATM 2311 O O   . HOH M 5 .  ? -6.440  -26.386 3.507   1.00 48.85  ? 294 HOH A O   1 
HETATM 2312 O O   . HOH M 5 .  ? 16.483  -9.971  -9.696  1.00 48.03  ? 295 HOH A O   1 
HETATM 2313 O O   . HOH M 5 .  ? 8.662   -9.110  -13.727 1.00 39.14  ? 296 HOH A O   1 
HETATM 2314 O O   . HOH M 5 .  ? 7.483   -8.379  13.177  1.00 48.19  ? 297 HOH A O   1 
HETATM 2315 O O   . HOH M 5 .  ? -0.963  -3.302  -10.743 1.00 51.58  ? 298 HOH A O   1 
HETATM 2316 O O   . HOH M 5 .  ? 8.587   -12.616 12.154  1.00 58.71  ? 299 HOH A O   1 
HETATM 2317 O O   . HOH M 5 .  ? -6.264  -23.111 -7.095  1.00 48.97  ? 300 HOH A O   1 
HETATM 2318 O O   . HOH M 5 .  ? -7.617  -14.043 -9.252  1.00 44.86  ? 301 HOH A O   1 
HETATM 2319 O O   . HOH M 5 .  ? 10.767  -1.806  -1.961  1.00 60.04  ? 302 HOH A O   1 
HETATM 2320 O O   . HOH M 5 .  ? -7.376  -19.293 7.497   1.00 69.61  ? 303 HOH A O   1 
HETATM 2321 O O   . HOH M 5 .  ? 4.672   -7.020  -11.044 1.00 46.59  ? 304 HOH A O   1 
HETATM 2322 O O   . HOH M 5 .  ? 8.175   -27.926 -8.160  1.00 59.84  ? 305 HOH A O   1 
HETATM 2323 O O   . HOH M 5 .  ? -10.400 -28.466 -1.907  1.00 56.43  ? 306 HOH A O   1 
HETATM 2324 O O   . HOH M 5 .  ? 10.424  -2.876  -0.312  1.00 64.34  ? 307 HOH A O   1 
HETATM 2325 O O   . HOH M 5 .  ? 4.644   -9.819  -11.237 1.00 51.63  ? 308 HOH A O   1 
HETATM 2326 O O   . HOH M 5 .  ? 14.769  -13.688 -12.571 1.00 50.06  ? 309 HOH A O   1 
HETATM 2327 O O   . HOH M 5 .  ? -11.544 -13.146 -2.913  1.00 57.34  ? 310 HOH A O   1 
HETATM 2328 O O   . HOH M 5 .  ? -6.579  -23.140 5.529   1.00 48.43  ? 311 HOH A O   1 
HETATM 2329 O O   . HOH M 5 .  ? 7.647   -30.522 -1.777  1.00 54.19  ? 312 HOH A O   1 
HETATM 2330 O O   . HOH M 5 .  ? 8.553   -22.447 -19.101 1.00 54.14  ? 313 HOH A O   1 
HETATM 2331 O O   . HOH M 5 .  ? 4.519   -3.285  2.892   1.00 67.48  ? 314 HOH A O   1 
HETATM 2332 O O   . HOH M 5 .  ? -13.485 -25.092 -4.467  1.00 64.87  ? 315 HOH A O   1 
HETATM 2333 O O   . HOH N 5 .  ? 31.042  -8.379  -29.980 1.00 51.94  ? 201 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 27.520  -8.053  -28.758 1.00 48.77  ? 202 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 10.025  -19.626 -43.097 1.00 51.92  ? 203 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 25.799  -4.860  -33.289 1.00 46.17  ? 204 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 34.580  -22.978 -30.123 1.00 64.15  ? 205 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 3.598   -18.658 -30.386 1.00 51.82  ? 206 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 12.600  -25.927 -37.149 1.00 54.82  ? 207 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 24.160  -1.633  -35.882 1.00 61.46  ? 208 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 10.451  -16.558 -44.181 1.00 51.22  ? 209 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 30.134  -19.582 -40.095 1.00 40.79  ? 210 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 9.914   -11.213 -38.078 1.00 50.78  ? 211 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 13.194  -4.643  -41.360 1.00 73.29  ? 212 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 23.537  -11.192 -21.609 1.00 44.68  ? 213 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 6.047   -7.459  -32.190 1.00 48.50  ? 214 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 16.971  -7.558  -20.442 1.00 45.98  ? 215 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 24.885  -5.174  -29.694 1.00 36.59  ? 216 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 6.409   -12.039 -25.943 1.00 42.39  ? 217 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 15.892  -17.013 -18.822 1.00 38.22  ? 218 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 17.016  -9.609  -43.649 1.00 46.42  ? 219 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 12.865  -22.358 -20.658 1.00 50.87  ? 220 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 20.308  -2.959  -22.929 1.00 61.79  ? 221 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 25.912  -23.146 -30.954 1.00 33.85  ? 222 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 1.651   -16.514 -32.565 1.00 56.81  ? 223 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 32.504  -18.533 -41.935 1.00 57.58  ? 224 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 22.406  -23.438 -28.716 1.00 41.87  ? 225 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 38.930  -12.520 -39.294 1.00 76.19  ? 226 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 16.590  -19.277 -28.685 1.00 23.80  ? 227 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 25.416  -5.987  -35.549 1.00 50.06  ? 228 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 6.998   -19.417 -34.872 1.00 47.92  ? 229 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 26.696  -22.645 -28.235 1.00 57.22  ? 230 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 20.724  -25.950 -29.788 1.00 71.56  ? 231 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 20.873  -13.296 -42.456 1.00 36.97  ? 232 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 18.161  -0.517  -38.212 1.00 26.62  ? 233 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 20.380  -22.321 -23.172 1.00 62.15  ? 234 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 22.124  -28.827 -32.781 1.00 53.23  ? 235 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 10.293  -18.906 -32.785 1.00 26.77  ? 236 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 17.399  -19.587 -41.957 1.00 60.59  ? 237 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 27.345  -17.968 -24.704 1.00 47.66  ? 238 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 8.098   -27.678 -38.227 1.00 56.54  ? 239 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 23.671  -4.190  -36.545 1.00 29.40  ? 240 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 20.575  -10.021 -42.641 1.00 37.73  ? 241 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 14.501  -6.304  -40.989 1.00 40.47  ? 242 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 8.518   -8.670  -16.516 1.00 41.33  ? 243 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 7.477   -18.380 -31.515 1.00 47.50  ? 244 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 26.938  -10.507 -28.667 1.00 56.66  ? 245 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 21.238  -6.550  -42.219 1.00 38.37  ? 246 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 17.981  -26.038 -29.015 1.00 36.10  ? 247 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 7.362   -8.131  -20.765 1.00 44.93  ? 248 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 19.526  -25.600 -34.033 1.00 39.61  ? 249 HOH B O   1 
HETATM 2382 O O   . HOH N 5 .  ? 23.289  -2.456  -28.824 1.00 38.18  ? 250 HOH B O   1 
HETATM 2383 O O   . HOH N 5 .  ? 17.852  -3.470  -22.070 1.00 54.10  ? 251 HOH B O   1 
HETATM 2384 O O   . HOH N 5 .  ? 10.489  -21.690 -32.579 1.00 33.99  ? 252 HOH B O   1 
HETATM 2385 O O   . HOH N 5 .  ? 17.852  -15.585 -45.532 1.00 39.17  ? 253 HOH B O   1 
HETATM 2386 O O   . HOH N 5 .  ? 21.047  3.716   -32.582 1.00 33.31  ? 254 HOH B O   1 
HETATM 2387 O O   . HOH N 5 .  ? 14.384  -24.520 -40.382 1.00 46.79  ? 255 HOH B O   1 
HETATM 2388 O O   . HOH N 5 .  ? 1.483   -12.775 -28.150 1.00 52.23  ? 256 HOH B O   1 
HETATM 2389 O O   . HOH N 5 .  ? 17.939  4.691   -34.307 1.00 39.34  ? 257 HOH B O   1 
HETATM 2390 O O   . HOH N 5 .  ? 16.946  -25.807 -34.222 1.00 40.45  ? 258 HOH B O   1 
HETATM 2391 O O   . HOH N 5 .  ? 31.095  -11.914 -38.215 1.00 59.06  ? 259 HOH B O   1 
HETATM 2392 O O   . HOH N 5 .  ? 7.582   -12.644 -38.875 1.00 60.47  ? 260 HOH B O   1 
HETATM 2393 O O   . HOH N 5 .  ? 25.649  -0.482  -28.864 1.00 46.58  ? 261 HOH B O   1 
HETATM 2394 O O   . HOH N 5 .  ? 31.784  -21.345 -37.938 1.00 53.66  ? 262 HOH B O   1 
HETATM 2395 O O   . HOH N 5 .  ? 24.869  -6.576  -42.331 1.00 48.59  ? 263 HOH B O   1 
HETATM 2396 O O   . HOH N 5 .  ? 27.779  -24.952 -34.893 1.00 37.07  ? 264 HOH B O   1 
HETATM 2397 O O   . HOH N 5 .  ? 2.810   -8.047  -27.206 1.00 54.97  ? 265 HOH B O   1 
HETATM 2398 O O   . HOH N 5 .  ? 9.670   -2.686  -41.801 1.00 63.08  ? 266 HOH B O   1 
HETATM 2399 O O   . HOH N 5 .  ? 14.971  -8.174  -42.828 1.00 53.78  ? 267 HOH B O   1 
HETATM 2400 O O   . HOH N 5 .  ? 6.011   -20.329 -24.930 1.00 42.90  ? 268 HOH B O   1 
HETATM 2401 O O   . HOH N 5 .  ? 16.932  -0.450  -25.189 1.00 54.18  ? 269 HOH B O   1 
HETATM 2402 O O   . HOH N 5 .  ? 7.065   -22.986 -24.170 1.00 60.34  ? 270 HOH B O   1 
HETATM 2403 O O   . HOH N 5 .  ? 12.649  -20.312 -19.630 1.00 48.88  ? 271 HOH B O   1 
HETATM 2404 O O   . HOH N 5 .  ? 9.582   -6.197  -40.793 1.00 48.22  ? 272 HOH B O   1 
HETATM 2405 O O   . HOH N 5 .  ? 37.454  -4.549  -24.364 1.00 57.48  ? 273 HOH B O   1 
HETATM 2406 O O   . HOH N 5 .  ? 27.595  -24.857 -32.141 1.00 39.76  ? 274 HOH B O   1 
HETATM 2407 O O   . HOH N 5 .  ? 24.126  -4.083  -27.842 1.00 58.67  ? 275 HOH B O   1 
HETATM 2408 O O   . HOH N 5 .  ? 19.276  4.100   -33.361 1.00 49.80  ? 276 HOH B O   1 
HETATM 2409 O O   . HOH N 5 .  ? 20.701  -19.651 -21.828 1.00 62.46  ? 277 HOH B O   1 
HETATM 2410 O O   . HOH N 5 .  ? 15.065  -26.292 -20.748 1.00 58.74  ? 278 HOH B O   1 
HETATM 2411 O O   . HOH N 5 .  ? 15.187  -21.827 -41.775 1.00 52.61  ? 279 HOH B O   1 
HETATM 2412 O O   . HOH N 5 .  ? 7.146   -9.713  -18.429 1.00 43.44  ? 280 HOH B O   1 
HETATM 2413 O O   . HOH N 5 .  ? 11.019  -5.224  -18.976 1.00 57.41  ? 281 HOH B O   1 
HETATM 2414 O O   . HOH N 5 .  ? 19.267  -8.478  -43.529 1.00 50.36  ? 282 HOH B O   1 
HETATM 2415 O O   . HOH N 5 .  ? 16.228  2.957   -26.781 1.00 59.65  ? 283 HOH B O   1 
HETATM 2416 O O   . HOH O 5 .  ? 15.091  -17.762 25.321  1.00 53.14  ? 201 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 26.092  -38.892 12.706  1.00 36.10  ? 202 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 7.976   -36.130 18.254  1.00 55.87  ? 203 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 26.150  -37.415 10.064  1.00 44.72  ? 204 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 19.248  -20.741 30.455  1.00 86.88  ? 205 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 12.128  -27.984 28.050  1.00 51.42  ? 206 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 29.479  -27.687 31.700  1.00 48.95  ? 207 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 14.517  -20.894 12.168  1.00 35.59  ? 208 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 5.243   -26.600 16.570  1.00 38.91  ? 209 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 27.711  -37.160 16.003  1.00 38.33  ? 210 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 20.565  -40.884 38.914  1.00 64.27  ? 211 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 17.114  -16.961 14.680  1.00 49.84  ? 212 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 8.778   -30.167 11.138  1.00 52.36  ? 213 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 21.828  -20.150 24.045  1.00 46.52  ? 214 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 12.378  -31.411 8.223   1.00 34.23  ? 215 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 7.011   -31.786 11.986  1.00 44.01  ? 216 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 19.430  -41.705 12.261  1.00 29.40  ? 217 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 29.822  -31.208 15.742  1.00 43.55  ? 218 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 21.815  -28.347 11.087  1.00 28.33  ? 219 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 30.797  -39.578 26.990  1.00 42.04  ? 220 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 22.676  -41.471 18.648  1.00 43.14  ? 221 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 13.589  -37.109 13.503  1.00 42.96  ? 222 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 18.682  -20.074 10.574  1.00 37.03  ? 223 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 30.204  -25.281 32.284  1.00 56.20  ? 224 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 31.428  -43.004 12.164  1.00 49.31  ? 225 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 30.981  -43.097 15.630  1.00 58.13  ? 226 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 22.371  -21.670 7.364   1.00 39.67  ? 227 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 25.739  -33.555 34.481  1.00 57.43  ? 228 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 13.770  -37.449 6.121   1.00 64.81  ? 229 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 15.124  -17.495 19.230  1.00 38.27  ? 230 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 24.696  -31.158 10.805  1.00 36.78  ? 231 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 18.758  -26.698 3.162   1.00 42.69  ? 232 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 20.309  -28.670 8.444   1.00 35.01  ? 233 HOH C O   1 
HETATM 2449 O O   . HOH O 5 .  ? 21.623  -34.227 16.569  1.00 25.68  ? 234 HOH C O   1 
HETATM 2450 O O   . HOH O 5 .  ? 31.404  -33.265 25.801  1.00 40.06  ? 235 HOH C O   1 
HETATM 2451 O O   . HOH O 5 .  ? 6.535   -17.912 10.856  1.00 37.55  ? 236 HOH C O   1 
HETATM 2452 O O   . HOH O 5 .  ? 29.464  -39.632 31.280  1.00 35.11  ? 237 HOH C O   1 
HETATM 2453 O O   . HOH O 5 .  ? 27.284  -37.515 24.971  1.00 43.71  ? 238 HOH C O   1 
HETATM 2454 O O   . HOH O 5 .  ? 20.361  -39.732 26.188  1.00 42.65  ? 239 HOH C O   1 
HETATM 2455 O O   . HOH O 5 .  ? 22.566  -18.342 21.851  1.00 51.70  ? 240 HOH C O   1 
HETATM 2456 O O   . HOH O 5 .  ? 25.297  -39.316 20.150  1.00 35.61  ? 241 HOH C O   1 
HETATM 2457 O O   . HOH O 5 .  ? 25.127  -17.827 21.047  1.00 59.44  ? 242 HOH C O   1 
HETATM 2458 O O   . HOH O 5 .  ? 29.967  -29.087 12.103  1.00 50.93  ? 243 HOH C O   1 
HETATM 2459 O O   . HOH O 5 .  ? 3.371   -22.798 18.778  1.00 44.72  ? 244 HOH C O   1 
HETATM 2460 O O   . HOH O 5 .  ? 8.389   -19.027 23.735  1.00 46.87  ? 245 HOH C O   1 
HETATM 2461 O O   . HOH O 5 .  ? 30.273  -35.505 28.409  1.00 54.63  ? 246 HOH C O   1 
HETATM 2462 O O   . HOH O 5 .  ? 25.344  -17.403 13.688  1.00 38.90  ? 247 HOH C O   1 
HETATM 2463 O O   . HOH O 5 .  ? 27.661  -36.337 18.648  1.00 46.51  ? 248 HOH C O   1 
HETATM 2464 O O   . HOH O 5 .  ? 27.277  -15.176 12.914  1.00 57.18  ? 249 HOH C O   1 
HETATM 2465 O O   . HOH O 5 .  ? 19.587  -18.917 24.859  1.00 41.46  ? 250 HOH C O   1 
HETATM 2466 O O   . HOH O 5 .  ? 25.425  -24.042 6.242   1.00 59.69  ? 251 HOH C O   1 
HETATM 2467 O O   . HOH O 5 .  ? 20.666  -29.368 4.727   1.00 54.83  ? 252 HOH C O   1 
HETATM 2468 O O   . HOH O 5 .  ? 12.343  -23.486 27.880  1.00 64.12  ? 253 HOH C O   1 
HETATM 2469 O O   . HOH O 5 .  ? 14.103  -29.278 4.046   1.00 44.11  ? 254 HOH C O   1 
HETATM 2470 O O   . HOH O 5 .  ? 13.706  -38.788 9.380   1.00 59.52  ? 255 HOH C O   1 
HETATM 2471 O O   . HOH O 5 .  ? 12.034  -38.583 24.280  1.00 57.19  ? 256 HOH C O   1 
HETATM 2472 O O   . HOH O 5 .  ? 32.900  -24.424 31.624  1.00 52.39  ? 257 HOH C O   1 
HETATM 2473 O O   . HOH O 5 .  ? 33.612  -35.892 31.655  1.00 49.65  ? 258 HOH C O   1 
HETATM 2474 O O   . HOH O 5 .  ? 29.636  -32.431 18.187  1.00 43.81  ? 259 HOH C O   1 
HETATM 2475 O O   . HOH O 5 .  ? 19.886  -12.905 13.337  1.00 45.19  ? 260 HOH C O   1 
HETATM 2476 O O   . HOH O 5 .  ? 1.857   -28.679 13.291  1.00 66.19  ? 261 HOH C O   1 
HETATM 2477 O O   . HOH O 5 .  ? 17.095  -36.683 29.180  1.00 64.71  ? 262 HOH C O   1 
HETATM 2478 O O   . HOH O 5 .  ? 28.823  -41.410 27.111  1.00 41.75  ? 263 HOH C O   1 
HETATM 2479 O O   . HOH O 5 .  ? 11.590  -21.000 10.752  1.00 35.31  ? 264 HOH C O   1 
HETATM 2480 O O   . HOH O 5 .  ? 29.811  -33.148 13.923  1.00 51.36  ? 265 HOH C O   1 
HETATM 2481 O O   . HOH O 5 .  ? 31.699  -38.861 29.565  1.00 47.55  ? 266 HOH C O   1 
HETATM 2482 O O   . HOH O 5 .  ? 23.476  -15.751 12.074  1.00 39.94  ? 267 HOH C O   1 
HETATM 2483 O O   . HOH O 5 .  ? 21.840  -13.414 13.285  1.00 50.35  ? 268 HOH C O   1 
HETATM 2484 O O   . HOH O 5 .  ? 36.064  -22.750 29.193  1.00 53.65  ? 269 HOH C O   1 
HETATM 2485 O O   . HOH O 5 .  ? 29.098  -17.931 28.545  1.00 53.68  ? 270 HOH C O   1 
HETATM 2486 O O   . HOH O 5 .  ? 31.115  -20.479 11.206  1.00 64.27  ? 271 HOH C O   1 
HETATM 2487 O O   . HOH O 5 .  ? 28.116  -41.386 29.747  1.00 42.83  ? 272 HOH C O   1 
HETATM 2488 O O   . HOH O 5 .  ? 10.471  -16.260 24.134  1.00 64.13  ? 273 HOH C O   1 
HETATM 2489 O O   . HOH O 5 .  ? 33.292  -44.124 15.256  1.00 46.22  ? 274 HOH C O   1 
HETATM 2490 O O   . HOH O 5 .  ? 15.132  -41.955 8.008   1.00 53.49  ? 275 HOH C O   1 
# 
