data_7HGP
# 
_entry.id   7HGP 
# 
_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   7HGP         pdb_00007hgp 10.2210/pdb7hgp/pdb 
WWPDB D_1001407451 ?            ?                   
# 
_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                        7HGP 
_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    3   ? ?    ? ? 
4 non-polymer syn '2-(4-fluorophenoxy)-1-(pyrrolidin-1-yl)ethan-1-one' 223.243   1   ? ?    ? ? 
5 water       nat water                                                18.015    269 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                        SO4 
3 1,2-ETHANEDIOL                                       EDO 
4 '2-(4-fluorophenoxy)-1-(pyrrolidin-1-yl)ethan-1-one' I8G 
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  
I8G non-polymer         . '2-(4-fluorophenoxy)-1-(pyrrolidin-1-yl)ethan-1-one' ?                 'C12 H14 F N O2' 223.243 
ILE 'L-peptide linking' y ISOLEUCINE                                           ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                              ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                               ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                           ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                        ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                              ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                               ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                                        ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                                            ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                           ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                             ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                               ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 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 ?  ?   ?   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        I8G 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   I8G 
_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 4 I8G 1   104 101 I8G LIG A . 
H 2 SO4 1   105 4   SO4 SO4 A . 
I 3 EDO 1   101 101 EDO EDO B . 
J 2 SO4 1   102 1   SO4 SO4 B . 
K 2 SO4 1   103 3   SO4 SO4 B . 
L 3 EDO 1   101 101 EDO EDO C . 
M 2 SO4 1   102 5   SO4 SO4 C . 
N 5 HOH 1   201 307 HOH HOH A . 
N 5 HOH 2   202 304 HOH HOH A . 
N 5 HOH 3   203 369 HOH HOH A . 
N 5 HOH 4   204 202 HOH HOH A . 
N 5 HOH 5   205 71  HOH HOH A . 
N 5 HOH 6   206 84  HOH HOH A . 
N 5 HOH 7   207 343 HOH HOH A . 
N 5 HOH 8   208 66  HOH HOH A . 
N 5 HOH 9   209 86  HOH HOH A . 
N 5 HOH 10  210 55  HOH HOH A . 
N 5 HOH 11  211 334 HOH HOH A . 
N 5 HOH 12  212 293 HOH HOH A . 
N 5 HOH 13  213 259 HOH HOH A . 
N 5 HOH 14  214 139 HOH HOH A . 
N 5 HOH 15  215 350 HOH HOH A . 
N 5 HOH 16  216 91  HOH HOH A . 
N 5 HOH 17  217 87  HOH HOH A . 
N 5 HOH 18  218 188 HOH HOH A . 
N 5 HOH 19  219 208 HOH HOH A . 
N 5 HOH 20  220 199 HOH HOH A . 
N 5 HOH 21  221 26  HOH HOH A . 
N 5 HOH 22  222 289 HOH HOH A . 
N 5 HOH 23  223 7   HOH HOH A . 
N 5 HOH 24  224 260 HOH HOH A . 
N 5 HOH 25  225 37  HOH HOH A . 
N 5 HOH 26  226 28  HOH HOH A . 
N 5 HOH 27  227 8   HOH HOH A . 
N 5 HOH 28  228 116 HOH HOH A . 
N 5 HOH 29  229 190 HOH HOH A . 
N 5 HOH 30  230 142 HOH HOH A . 
N 5 HOH 31  231 42  HOH HOH A . 
N 5 HOH 32  232 211 HOH HOH A . 
N 5 HOH 33  233 77  HOH HOH A . 
N 5 HOH 34  234 111 HOH HOH A . 
N 5 HOH 35  235 179 HOH HOH A . 
N 5 HOH 36  236 152 HOH HOH A . 
N 5 HOH 37  237 336 HOH HOH A . 
N 5 HOH 38  238 1   HOH HOH A . 
N 5 HOH 39  239 27  HOH HOH A . 
N 5 HOH 40  240 34  HOH HOH A . 
N 5 HOH 41  241 97  HOH HOH A . 
N 5 HOH 42  242 95  HOH HOH A . 
N 5 HOH 43  243 292 HOH HOH A . 
N 5 HOH 44  244 32  HOH HOH A . 
N 5 HOH 45  245 12  HOH HOH A . 
N 5 HOH 46  246 2   HOH HOH A . 
N 5 HOH 47  247 145 HOH HOH A . 
N 5 HOH 48  248 99  HOH HOH A . 
N 5 HOH 49  249 131 HOH HOH A . 
N 5 HOH 50  250 64  HOH HOH A . 
N 5 HOH 51  251 338 HOH HOH A . 
N 5 HOH 52  252 357 HOH HOH A . 
N 5 HOH 53  253 23  HOH HOH A . 
N 5 HOH 54  254 267 HOH HOH A . 
N 5 HOH 55  255 21  HOH HOH A . 
N 5 HOH 56  256 109 HOH HOH A . 
N 5 HOH 57  257 274 HOH HOH A . 
N 5 HOH 58  258 344 HOH HOH A . 
N 5 HOH 59  259 58  HOH HOH A . 
N 5 HOH 60  260 60  HOH HOH A . 
N 5 HOH 61  261 38  HOH HOH A . 
N 5 HOH 62  262 300 HOH HOH A . 
N 5 HOH 63  263 218 HOH HOH A . 
N 5 HOH 64  264 287 HOH HOH A . 
N 5 HOH 65  265 203 HOH HOH A . 
N 5 HOH 66  266 93  HOH HOH A . 
N 5 HOH 67  267 31  HOH HOH A . 
N 5 HOH 68  268 297 HOH HOH A . 
N 5 HOH 69  269 288 HOH HOH A . 
N 5 HOH 70  270 35  HOH HOH A . 
N 5 HOH 71  271 18  HOH HOH A . 
N 5 HOH 72  272 20  HOH HOH A . 
N 5 HOH 73  273 94  HOH HOH A . 
N 5 HOH 74  274 78  HOH HOH A . 
N 5 HOH 75  275 370 HOH HOH A . 
N 5 HOH 76  276 143 HOH HOH A . 
N 5 HOH 77  277 222 HOH HOH A . 
N 5 HOH 78  278 14  HOH HOH A . 
N 5 HOH 79  279 164 HOH HOH A . 
N 5 HOH 80  280 299 HOH HOH A . 
N 5 HOH 81  281 9   HOH HOH A . 
N 5 HOH 82  282 165 HOH HOH A . 
N 5 HOH 83  283 281 HOH HOH A . 
N 5 HOH 84  284 167 HOH HOH A . 
N 5 HOH 85  285 113 HOH HOH A . 
N 5 HOH 86  286 318 HOH HOH A . 
N 5 HOH 87  287 19  HOH HOH A . 
N 5 HOH 88  288 16  HOH HOH A . 
N 5 HOH 89  289 210 HOH HOH A . 
N 5 HOH 90  290 115 HOH HOH A . 
N 5 HOH 91  291 301 HOH HOH A . 
N 5 HOH 92  292 47  HOH HOH A . 
N 5 HOH 93  293 346 HOH HOH A . 
N 5 HOH 94  294 63  HOH HOH A . 
N 5 HOH 95  295 22  HOH HOH A . 
N 5 HOH 96  296 73  HOH HOH A . 
N 5 HOH 97  297 327 HOH HOH A . 
N 5 HOH 98  298 361 HOH HOH A . 
N 5 HOH 99  299 108 HOH HOH A . 
N 5 HOH 100 300 83  HOH HOH A . 
N 5 HOH 101 301 185 HOH HOH A . 
N 5 HOH 102 302 219 HOH HOH A . 
N 5 HOH 103 303 354 HOH HOH A . 
N 5 HOH 104 304 332 HOH HOH A . 
N 5 HOH 105 305 283 HOH HOH A . 
N 5 HOH 106 306 57  HOH HOH A . 
N 5 HOH 107 307 156 HOH HOH A . 
N 5 HOH 108 308 75  HOH HOH A . 
N 5 HOH 109 309 205 HOH HOH A . 
N 5 HOH 110 310 125 HOH HOH A . 
O 5 HOH 1   201 331 HOH HOH B . 
O 5 HOH 2   202 89  HOH HOH B . 
O 5 HOH 3   203 272 HOH HOH B . 
O 5 HOH 4   204 184 HOH HOH B . 
O 5 HOH 5   205 17  HOH HOH B . 
O 5 HOH 6   206 258 HOH HOH B . 
O 5 HOH 7   207 247 HOH HOH B . 
O 5 HOH 8   208 69  HOH HOH B . 
O 5 HOH 9   209 363 HOH HOH B . 
O 5 HOH 10  210 68  HOH HOH B . 
O 5 HOH 11  211 177 HOH HOH B . 
O 5 HOH 12  212 249 HOH HOH B . 
O 5 HOH 13  213 168 HOH HOH B . 
O 5 HOH 14  214 333 HOH HOH B . 
O 5 HOH 15  215 59  HOH HOH B . 
O 5 HOH 16  216 172 HOH HOH B . 
O 5 HOH 17  217 242 HOH HOH B . 
O 5 HOH 18  218 137 HOH HOH B . 
O 5 HOH 19  219 223 HOH HOH B . 
O 5 HOH 20  220 54  HOH HOH B . 
O 5 HOH 21  221 98  HOH HOH B . 
O 5 HOH 22  222 6   HOH HOH B . 
O 5 HOH 23  223 352 HOH HOH B . 
O 5 HOH 24  224 101 HOH HOH B . 
O 5 HOH 25  225 320 HOH HOH B . 
O 5 HOH 26  226 175 HOH HOH B . 
O 5 HOH 27  227 10  HOH HOH B . 
O 5 HOH 28  228 5   HOH HOH B . 
O 5 HOH 29  229 261 HOH HOH B . 
O 5 HOH 30  230 123 HOH HOH B . 
O 5 HOH 31  231 315 HOH HOH B . 
O 5 HOH 32  232 170 HOH HOH B . 
O 5 HOH 33  233 74  HOH HOH B . 
O 5 HOH 34  234 117 HOH HOH B . 
O 5 HOH 35  235 150 HOH HOH B . 
O 5 HOH 36  236 24  HOH HOH B . 
O 5 HOH 37  237 157 HOH HOH B . 
O 5 HOH 38  238 197 HOH HOH B . 
O 5 HOH 39  239 153 HOH HOH B . 
O 5 HOH 40  240 280 HOH HOH B . 
O 5 HOH 41  241 61  HOH HOH B . 
O 5 HOH 42  242 169 HOH HOH B . 
O 5 HOH 43  243 96  HOH HOH B . 
O 5 HOH 44  244 329 HOH HOH B . 
O 5 HOH 45  245 119 HOH HOH B . 
O 5 HOH 46  246 72  HOH HOH B . 
O 5 HOH 47  247 79  HOH HOH B . 
O 5 HOH 48  248 120 HOH HOH B . 
O 5 HOH 49  249 345 HOH HOH B . 
O 5 HOH 50  250 355 HOH HOH B . 
O 5 HOH 51  251 319 HOH HOH B . 
O 5 HOH 52  252 215 HOH HOH B . 
O 5 HOH 53  253 13  HOH HOH B . 
O 5 HOH 54  254 182 HOH HOH B . 
O 5 HOH 55  255 217 HOH HOH B . 
O 5 HOH 56  256 25  HOH HOH B . 
O 5 HOH 57  257 36  HOH HOH B . 
O 5 HOH 58  258 76  HOH HOH B . 
O 5 HOH 59  259 303 HOH HOH B . 
O 5 HOH 60  260 104 HOH HOH B . 
O 5 HOH 61  261 214 HOH HOH B . 
O 5 HOH 62  262 46  HOH HOH B . 
O 5 HOH 63  263 44  HOH HOH B . 
O 5 HOH 64  264 351 HOH HOH B . 
O 5 HOH 65  265 364 HOH HOH B . 
O 5 HOH 66  266 279 HOH HOH B . 
O 5 HOH 67  267 362 HOH HOH B . 
O 5 HOH 68  268 322 HOH HOH B . 
O 5 HOH 69  269 201 HOH HOH B . 
O 5 HOH 70  270 291 HOH HOH B . 
O 5 HOH 71  271 224 HOH HOH B . 
O 5 HOH 72  272 353 HOH HOH B . 
O 5 HOH 73  273 160 HOH HOH B . 
O 5 HOH 74  274 163 HOH HOH B . 
O 5 HOH 75  275 103 HOH HOH B . 
O 5 HOH 76  276 337 HOH HOH B . 
O 5 HOH 77  277 316 HOH HOH B . 
O 5 HOH 78  278 314 HOH HOH B . 
O 5 HOH 79  279 107 HOH HOH B . 
O 5 HOH 80  280 335 HOH HOH B . 
O 5 HOH 81  281 312 HOH HOH B . 
O 5 HOH 82  282 313 HOH HOH B . 
P 5 HOH 1   201 347 HOH HOH C . 
P 5 HOH 2   202 254 HOH HOH C . 
P 5 HOH 3   203 321 HOH HOH C . 
P 5 HOH 4   204 365 HOH HOH C . 
P 5 HOH 5   205 358 HOH HOH C . 
P 5 HOH 6   206 323 HOH HOH C . 
P 5 HOH 7   207 341 HOH HOH C . 
P 5 HOH 8   208 317 HOH HOH C . 
P 5 HOH 9   209 326 HOH HOH C . 
P 5 HOH 10  210 148 HOH HOH C . 
P 5 HOH 11  211 161 HOH HOH C . 
P 5 HOH 12  212 342 HOH HOH C . 
P 5 HOH 13  213 309 HOH HOH C . 
P 5 HOH 14  214 226 HOH HOH C . 
P 5 HOH 15  215 271 HOH HOH C . 
P 5 HOH 16  216 118 HOH HOH C . 
P 5 HOH 17  217 49  HOH HOH C . 
P 5 HOH 18  218 173 HOH HOH C . 
P 5 HOH 19  219 126 HOH HOH C . 
P 5 HOH 20  220 269 HOH HOH C . 
P 5 HOH 21  221 339 HOH HOH C . 
P 5 HOH 22  222 189 HOH HOH C . 
P 5 HOH 23  223 85  HOH HOH C . 
P 5 HOH 24  224 134 HOH HOH C . 
P 5 HOH 25  225 151 HOH HOH C . 
P 5 HOH 26  226 82  HOH HOH C . 
P 5 HOH 27  227 325 HOH HOH C . 
P 5 HOH 28  228 90  HOH HOH C . 
P 5 HOH 29  229 294 HOH HOH C . 
P 5 HOH 30  230 15  HOH HOH C . 
P 5 HOH 31  231 40  HOH HOH C . 
P 5 HOH 32  232 102 HOH HOH C . 
P 5 HOH 33  233 4   HOH HOH C . 
P 5 HOH 34  234 330 HOH HOH C . 
P 5 HOH 35  235 284 HOH HOH C . 
P 5 HOH 36  236 43  HOH HOH C . 
P 5 HOH 37  237 171 HOH HOH C . 
P 5 HOH 38  238 56  HOH HOH C . 
P 5 HOH 39  239 48  HOH HOH C . 
P 5 HOH 40  240 45  HOH HOH C . 
P 5 HOH 41  241 132 HOH HOH C . 
P 5 HOH 42  242 53  HOH HOH C . 
P 5 HOH 43  243 41  HOH HOH C . 
P 5 HOH 44  244 302 HOH HOH C . 
P 5 HOH 45  245 122 HOH HOH C . 
P 5 HOH 46  246 298 HOH HOH C . 
P 5 HOH 47  247 349 HOH HOH C . 
P 5 HOH 48  248 328 HOH HOH C . 
P 5 HOH 49  249 135 HOH HOH C . 
P 5 HOH 50  250 130 HOH HOH C . 
P 5 HOH 51  251 275 HOH HOH C . 
P 5 HOH 52  252 62  HOH HOH C . 
P 5 HOH 53  253 356 HOH HOH C . 
P 5 HOH 54  254 198 HOH HOH C . 
P 5 HOH 55  255 149 HOH HOH C . 
P 5 HOH 56  256 209 HOH HOH C . 
P 5 HOH 57  257 65  HOH HOH C . 
P 5 HOH 58  258 67  HOH HOH C . 
P 5 HOH 59  259 146 HOH HOH C . 
P 5 HOH 60  260 246 HOH HOH C . 
P 5 HOH 61  261 241 HOH HOH C . 
P 5 HOH 62  262 366 HOH HOH C . 
P 5 HOH 63  263 305 HOH HOH C . 
P 5 HOH 64  264 70  HOH HOH C . 
P 5 HOH 65  265 296 HOH HOH C . 
P 5 HOH 66  266 270 HOH HOH C . 
P 5 HOH 67  267 324 HOH HOH C . 
P 5 HOH 68  268 340 HOH HOH C . 
P 5 HOH 69  269 359 HOH HOH C . 
P 5 HOH 70  270 92  HOH HOH C . 
P 5 HOH 71  271 310 HOH HOH C . 
P 5 HOH 72  272 206 HOH HOH C . 
P 5 HOH 73  273 368 HOH HOH C . 
P 5 HOH 74  274 367 HOH HOH C . 
P 5 HOH 75  275 360 HOH HOH C . 
P 5 HOH 76  276 348 HOH HOH C . 
P 5 HOH 77  277 295 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 ? CE  ? B LYS 74 CE  
19 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
20 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
21 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
22 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
23 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
24 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
25 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
26 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
27 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
28 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
29 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
30 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
31 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
32 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
33 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
34 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
35 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
36 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
37 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
38 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
39 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' XDS     .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HGP 
_cell.length_a           41.544 
_cell.length_b           42.085 
_cell.length_c           159.275 
_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                         7HGP 
_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          7HGP 
_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                     7HGP 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             40.69 
_reflns.d_resolution_high            1.62 
_reflns.number_obs                   34464 
_reflns.percent_possible_obs         95.4 
_reflns.pdbx_Rmerge_I_obs            0.069 
_reflns.pdbx_netI_over_sigmaI        8.6 
_reflns.pdbx_redundancy              3.5 
_reflns.pdbx_Rrim_I_all              0.081 
_reflns.pdbx_Rpim_I_all              0.042 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     119996 
_reflns.pdbx_chi_squared             0.89 
_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                  1.62 
_reflns_shell.d_res_low                   1.71 
_reflns_shell.number_measured_all         16737 
_reflns_shell.number_unique_obs           4996 
_reflns_shell.Rmerge_I_obs                1.035 
_reflns_shell.pdbx_chi_squared            0.64 
_reflns_shell.pdbx_redundancy             3.4 
_reflns_shell.percent_possible_obs        96.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.0 
_reflns_shell.pdbx_Rrim_I_all             1.222 
_reflns_shell.pdbx_Rpim_I_all             0.640 
_reflns_shell.pdbx_CC_half                0.417 
_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                                 7HGP 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     32566 
_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                             40.72 
_refine.ls_d_res_high                            1.62 
_refine.ls_percent_reflns_obs                    94.90 
_refine.ls_R_factor_obs                          0.21263 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.21041 
_refine.ls_R_factor_R_free                       0.25282 
_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                  1810 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.B_iso_mean                               45.652 
_refine.aniso_B[1][1]                            0.80 
_refine.aniso_B[2][2]                            -0.52 
_refine.aniso_B[3][3]                            -0.29 
_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                       0.117 
_refine.pdbx_overall_ESU_R_Free                  0.117 
_refine.overall_SU_ML                            0.101 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.063 
_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        2131 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_refine_hist.number_atoms_solvent             269 
_refine_hist.number_atoms_total               2458 
_refine_hist.d_res_high                       1.62 
_refine_hist.d_res_low                        40.72 
# 
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             0.008  0.012  ? 2292 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.759  1.837  ? 3113 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.883  5.000  ? 263  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       8.074  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.041 10.000 ? 304  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.127  0.200  ? 283  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1900 '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                  3.584  4.289  ? 1061 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.737  7.676  ? 1321 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.827  4.606  ? 1231 '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       10.288 63.60  ? 3646 '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                       1.625 
_refine_ls_shell.d_res_low                        1.667 
_refine_ls_shell.number_reflns_R_work             2372 
_refine_ls_shell.R_factor_R_work                  0.343 
_refine_ls_shell.percent_reflns_obs               94.11 
_refine_ls_shell.R_factor_R_free                  0.366 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             122 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGP 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z19735067' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGP 
_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 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 2 ? 
L N N 3 ? 
M N N 2 ? 
N N N 5 ? 
O N N 5 ? 
P 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 7HGP A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGP B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGP 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 7HGP GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGP SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGP GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGP SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGP GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGP 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,H,N 
2 1 B,I,J,K,O     
3 1 C,L,M,P       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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                   7HGP 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 240 ? ? O B HOH 268 ? ? 1.42 
2  1 O   C LYS 75  ? ? O C HOH 201 ? ? 1.78 
3  1 O2  A SO4 105 ? ? O A HOH 201 ? ? 1.99 
4  1 O4  C SO4 102 ? ? O C HOH 202 ? ? 2.01 
5  1 O   A HOH 251 ? ? O A HOH 274 ? ? 2.02 
6  1 OH  A TYR 18  ? ? O A HOH 202 ? ? 2.03 
7  1 O   B LYS 16  ? ? O B HOH 201 ? ? 2.05 
8  1 O2  C SO4 102 ? ? O C HOH 203 ? ? 2.06 
9  1 OD2 C ASP 66  ? ? O C HOH 204 ? ? 2.09 
10 1 O   C ILE 84  ? ? O C HOH 205 ? ? 2.10 
11 1 O   B HOH 247 ? ? O B HOH 271 ? ? 2.11 
12 1 O2  B SO4 102 ? ? O B HOH 202 ? ? 2.14 
13 1 OH  A TYR 18  ? ? O A HOH 203 ? ? 2.16 
14 1 O   B HOH 211 ? ? O B HOH 276 ? ? 2.17 
15 1 O   A HOH 270 ? ? O A HOH 305 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     242 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     288 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_545 
_pdbx_validate_symm_contact.dist              2.11 
# 
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 ? ? -152.03 65.14 
2 1 ASN B 38 ? ? 77.90   -0.42 
3 1 ASN B 87 ? ? -160.20 59.83 
4 1 ASN C 87 ? ? -148.66 55.08 
# 
_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            0.111 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C ASP 27 ? C ASP 28 
11 1 Y 1 C ILE 28 ? C ILE 29 
12 1 Y 1 C ALA 29 ? C ALA 30 
13 1 Y 1 C ASP 30 ? C ASP 31 
14 1 Y 1 C GLY 31 ? C GLY 32 
15 1 Y 1 C ALA 32 ? C ALA 33 
16 1 Y 1 C VAL 33 ? C VAL 34 
17 1 Y 1 C LYS 34 ? C LYS 35 
18 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 
I8G N1   N N N 171 
I8G C4   C Y N 172 
I8G C5   C N N 173 
I8G C6   C N N 174 
I8G C7   C N N 175 
I8G C8   C N N 176 
I8G C10  C N N 177 
I8G F1   F N N 178 
I8G C1   C Y N 179 
I8G C2   C Y N 180 
I8G C3   C Y N 181 
I8G O1   O N N 182 
I8G O2   O N N 183 
I8G C9   C N N 184 
I8G C11  C Y N 185 
I8G C12  C Y N 186 
I8G H3   H N N 187 
I8G H4   H N N 188 
I8G H5   H N N 189 
I8G H6   H N N 190 
I8G H7   H N N 191 
I8G H8   H N N 192 
I8G H11  H N N 193 
I8G H12  H N N 194 
I8G H1   H N N 195 
I8G H2   H N N 196 
I8G H9   H N N 197 
I8G H10  H N N 198 
I8G H13  H N N 199 
I8G H14  H N N 200 
ILE N    N N N 201 
ILE CA   C N S 202 
ILE C    C N N 203 
ILE O    O N N 204 
ILE CB   C N S 205 
ILE CG1  C N N 206 
ILE CG2  C N N 207 
ILE CD1  C N N 208 
ILE OXT  O N N 209 
ILE H    H N N 210 
ILE H2   H N N 211 
ILE HA   H N N 212 
ILE HB   H N N 213 
ILE HG12 H N N 214 
ILE HG13 H N N 215 
ILE HG21 H N N 216 
ILE HG22 H N N 217 
ILE HG23 H N N 218 
ILE HD11 H N N 219 
ILE HD12 H N N 220 
ILE HD13 H N N 221 
ILE HXT  H N N 222 
LEU N    N N N 223 
LEU CA   C N S 224 
LEU C    C N N 225 
LEU O    O N N 226 
LEU CB   C N N 227 
LEU CG   C N N 228 
LEU CD1  C N N 229 
LEU CD2  C N N 230 
LEU OXT  O N N 231 
LEU H    H N N 232 
LEU H2   H N N 233 
LEU HA   H N N 234 
LEU HB2  H N N 235 
LEU HB3  H N N 236 
LEU HG   H N N 237 
LEU HD11 H N N 238 
LEU HD12 H N N 239 
LEU HD13 H N N 240 
LEU HD21 H N N 241 
LEU HD22 H N N 242 
LEU HD23 H N N 243 
LEU HXT  H N N 244 
LYS N    N N N 245 
LYS CA   C N S 246 
LYS C    C N N 247 
LYS O    O N N 248 
LYS CB   C N N 249 
LYS CG   C N N 250 
LYS CD   C N N 251 
LYS CE   C N N 252 
LYS NZ   N N N 253 
LYS OXT  O N N 254 
LYS H    H N N 255 
LYS H2   H N N 256 
LYS HA   H N N 257 
LYS HB2  H N N 258 
LYS HB3  H N N 259 
LYS HG2  H N N 260 
LYS HG3  H N N 261 
LYS HD2  H N N 262 
LYS HD3  H N N 263 
LYS HE2  H N N 264 
LYS HE3  H N N 265 
LYS HZ1  H N N 266 
LYS HZ2  H N N 267 
LYS HZ3  H N N 268 
LYS HXT  H N N 269 
MET N    N N N 270 
MET CA   C N S 271 
MET C    C N N 272 
MET O    O N N 273 
MET CB   C N N 274 
MET CG   C N N 275 
MET SD   S N N 276 
MET CE   C N N 277 
MET OXT  O N N 278 
MET H    H N N 279 
MET H2   H N N 280 
MET HA   H N N 281 
MET HB2  H N N 282 
MET HB3  H N N 283 
MET HG2  H N N 284 
MET HG3  H N N 285 
MET HE1  H N N 286 
MET HE2  H N N 287 
MET HE3  H N N 288 
MET HXT  H N N 289 
PHE N    N N N 290 
PHE CA   C N S 291 
PHE C    C N N 292 
PHE O    O N N 293 
PHE CB   C N N 294 
PHE CG   C Y N 295 
PHE CD1  C Y N 296 
PHE CD2  C Y N 297 
PHE CE1  C Y N 298 
PHE CE2  C Y N 299 
PHE CZ   C Y N 300 
PHE OXT  O N N 301 
PHE H    H N N 302 
PHE H2   H N N 303 
PHE HA   H N N 304 
PHE HB2  H N N 305 
PHE HB3  H N N 306 
PHE HD1  H N N 307 
PHE HD2  H N N 308 
PHE HE1  H N N 309 
PHE HE2  H N N 310 
PHE HZ   H N N 311 
PHE HXT  H N N 312 
PRO N    N N N 313 
PRO CA   C N S 314 
PRO C    C N N 315 
PRO O    O N N 316 
PRO CB   C N N 317 
PRO CG   C N N 318 
PRO CD   C N N 319 
PRO OXT  O N N 320 
PRO H    H N N 321 
PRO HA   H N N 322 
PRO HB2  H N N 323 
PRO HB3  H N N 324 
PRO HG2  H N N 325 
PRO HG3  H N N 326 
PRO HD2  H N N 327 
PRO HD3  H N N 328 
PRO HXT  H N N 329 
SER N    N N N 330 
SER CA   C N S 331 
SER C    C N N 332 
SER O    O N N 333 
SER CB   C N N 334 
SER OG   O N N 335 
SER OXT  O N N 336 
SER H    H N N 337 
SER H2   H N N 338 
SER HA   H N N 339 
SER HB2  H N N 340 
SER HB3  H N N 341 
SER HG   H N N 342 
SER HXT  H N N 343 
SO4 S    S N N 344 
SO4 O1   O N N 345 
SO4 O2   O N N 346 
SO4 O3   O N N 347 
SO4 O4   O N N 348 
THR N    N N N 349 
THR CA   C N S 350 
THR C    C N N 351 
THR O    O N N 352 
THR CB   C N R 353 
THR OG1  O N N 354 
THR CG2  C N N 355 
THR OXT  O N N 356 
THR H    H N N 357 
THR H2   H N N 358 
THR HA   H N N 359 
THR HB   H N N 360 
THR HG1  H N N 361 
THR HG21 H N N 362 
THR HG22 H N N 363 
THR HG23 H N N 364 
THR HXT  H N N 365 
TRP N    N N N 366 
TRP CA   C N S 367 
TRP C    C N N 368 
TRP O    O N N 369 
TRP CB   C N N 370 
TRP CG   C Y N 371 
TRP CD1  C Y N 372 
TRP CD2  C Y N 373 
TRP NE1  N Y N 374 
TRP CE2  C Y N 375 
TRP CE3  C Y N 376 
TRP CZ2  C Y N 377 
TRP CZ3  C Y N 378 
TRP CH2  C Y N 379 
TRP OXT  O N N 380 
TRP H    H N N 381 
TRP H2   H N N 382 
TRP HA   H N N 383 
TRP HB2  H N N 384 
TRP HB3  H N N 385 
TRP HD1  H N N 386 
TRP HE1  H N N 387 
TRP HE3  H N N 388 
TRP HZ2  H N N 389 
TRP HZ3  H N N 390 
TRP HH2  H N N 391 
TRP HXT  H N N 392 
TYR N    N N N 393 
TYR CA   C N S 394 
TYR C    C N N 395 
TYR O    O N N 396 
TYR CB   C N N 397 
TYR CG   C Y N 398 
TYR CD1  C Y N 399 
TYR CD2  C Y N 400 
TYR CE1  C Y N 401 
TYR CE2  C Y N 402 
TYR CZ   C Y N 403 
TYR OH   O N N 404 
TYR OXT  O N N 405 
TYR H    H N N 406 
TYR H2   H N N 407 
TYR HA   H N N 408 
TYR HB2  H N N 409 
TYR HB3  H N N 410 
TYR HD1  H N N 411 
TYR HD2  H N N 412 
TYR HE1  H N N 413 
TYR HE2  H N N 414 
TYR HH   H N N 415 
TYR HXT  H N N 416 
VAL N    N N N 417 
VAL CA   C N S 418 
VAL C    C N N 419 
VAL O    O N N 420 
VAL CB   C N N 421 
VAL CG1  C N N 422 
VAL CG2  C N N 423 
VAL OXT  O N N 424 
VAL H    H N N 425 
VAL H2   H N N 426 
VAL HA   H N N 427 
VAL HB   H N N 428 
VAL HG11 H N N 429 
VAL HG12 H N N 430 
VAL HG13 H N N 431 
VAL HG21 H N N 432 
VAL HG22 H N N 433 
VAL HG23 H N N 434 
VAL HXT  H N N 435 
# 
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 
I8G F1  C1   sing N N 161 
I8G C1  C2   doub Y N 162 
I8G C2  C3   sing Y N 163 
I8G C3  C4   doub Y N 164 
I8G C4  O1   sing N N 165 
I8G O1  C5   sing N N 166 
I8G C5  C6   sing N N 167 
I8G C6  O2   doub N N 168 
I8G C6  N1   sing N N 169 
I8G N1  C7   sing N N 170 
I8G C7  C8   sing N N 171 
I8G C8  C9   sing N N 172 
I8G C9  C10  sing N N 173 
I8G C4  C11  sing Y N 174 
I8G C11 C12  doub Y N 175 
I8G C1  C12  sing Y N 176 
I8G N1  C10  sing N N 177 
I8G C5  H3   sing N N 178 
I8G C5  H4   sing N N 179 
I8G C7  H5   sing N N 180 
I8G C7  H6   sing N N 181 
I8G C8  H7   sing N N 182 
I8G C8  H8   sing N N 183 
I8G C10 H11  sing N N 184 
I8G C10 H12  sing N N 185 
I8G C2  H1   sing N N 186 
I8G C3  H2   sing N N 187 
I8G C9  H9   sing N N 188 
I8G C9  H10  sing N N 189 
I8G C11 H13  sing N N 190 
I8G C12 H14  sing N N 191 
ILE N   CA   sing N N 192 
ILE N   H    sing N N 193 
ILE N   H2   sing N N 194 
ILE CA  C    sing N N 195 
ILE CA  CB   sing N N 196 
ILE CA  HA   sing N N 197 
ILE C   O    doub N N 198 
ILE C   OXT  sing N N 199 
ILE CB  CG1  sing N N 200 
ILE CB  CG2  sing N N 201 
ILE CB  HB   sing N N 202 
ILE CG1 CD1  sing N N 203 
ILE CG1 HG12 sing N N 204 
ILE CG1 HG13 sing N N 205 
ILE CG2 HG21 sing N N 206 
ILE CG2 HG22 sing N N 207 
ILE CG2 HG23 sing N N 208 
ILE CD1 HD11 sing N N 209 
ILE CD1 HD12 sing N N 210 
ILE CD1 HD13 sing N N 211 
ILE OXT HXT  sing N N 212 
LEU N   CA   sing N N 213 
LEU N   H    sing N N 214 
LEU N   H2   sing N N 215 
LEU CA  C    sing N N 216 
LEU CA  CB   sing N N 217 
LEU CA  HA   sing N N 218 
LEU C   O    doub N N 219 
LEU C   OXT  sing N N 220 
LEU CB  CG   sing N N 221 
LEU CB  HB2  sing N N 222 
LEU CB  HB3  sing N N 223 
LEU CG  CD1  sing N N 224 
LEU CG  CD2  sing N N 225 
LEU CG  HG   sing N N 226 
LEU CD1 HD11 sing N N 227 
LEU CD1 HD12 sing N N 228 
LEU CD1 HD13 sing N N 229 
LEU CD2 HD21 sing N N 230 
LEU CD2 HD22 sing N N 231 
LEU CD2 HD23 sing N N 232 
LEU OXT HXT  sing N N 233 
LYS N   CA   sing N N 234 
LYS N   H    sing N N 235 
LYS N   H2   sing N N 236 
LYS CA  C    sing N N 237 
LYS CA  CB   sing N N 238 
LYS CA  HA   sing N N 239 
LYS C   O    doub N N 240 
LYS C   OXT  sing N N 241 
LYS CB  CG   sing N N 242 
LYS CB  HB2  sing N N 243 
LYS CB  HB3  sing N N 244 
LYS CG  CD   sing N N 245 
LYS CG  HG2  sing N N 246 
LYS CG  HG3  sing N N 247 
LYS CD  CE   sing N N 248 
LYS CD  HD2  sing N N 249 
LYS CD  HD3  sing N N 250 
LYS CE  NZ   sing N N 251 
LYS CE  HE2  sing N N 252 
LYS CE  HE3  sing N N 253 
LYS NZ  HZ1  sing N N 254 
LYS NZ  HZ2  sing N N 255 
LYS NZ  HZ3  sing N N 256 
LYS OXT HXT  sing N N 257 
MET N   CA   sing N N 258 
MET N   H    sing N N 259 
MET N   H2   sing N N 260 
MET CA  C    sing N N 261 
MET CA  CB   sing N N 262 
MET CA  HA   sing N N 263 
MET C   O    doub N N 264 
MET C   OXT  sing N N 265 
MET CB  CG   sing N N 266 
MET CB  HB2  sing N N 267 
MET CB  HB3  sing N N 268 
MET CG  SD   sing N N 269 
MET CG  HG2  sing N N 270 
MET CG  HG3  sing N N 271 
MET SD  CE   sing N N 272 
MET CE  HE1  sing N N 273 
MET CE  HE2  sing N N 274 
MET CE  HE3  sing N N 275 
MET OXT HXT  sing N N 276 
PHE N   CA   sing N N 277 
PHE N   H    sing N N 278 
PHE N   H2   sing N N 279 
PHE CA  C    sing N N 280 
PHE CA  CB   sing N N 281 
PHE CA  HA   sing N N 282 
PHE C   O    doub N N 283 
PHE C   OXT  sing N N 284 
PHE CB  CG   sing N N 285 
PHE CB  HB2  sing N N 286 
PHE CB  HB3  sing N N 287 
PHE CG  CD1  doub Y N 288 
PHE CG  CD2  sing Y N 289 
PHE CD1 CE1  sing Y N 290 
PHE CD1 HD1  sing N N 291 
PHE CD2 CE2  doub Y N 292 
PHE CD2 HD2  sing N N 293 
PHE CE1 CZ   doub Y N 294 
PHE CE1 HE1  sing N N 295 
PHE CE2 CZ   sing Y N 296 
PHE CE2 HE2  sing N N 297 
PHE CZ  HZ   sing N N 298 
PHE OXT HXT  sing N N 299 
PRO N   CA   sing N N 300 
PRO N   CD   sing N N 301 
PRO N   H    sing N N 302 
PRO CA  C    sing N N 303 
PRO CA  CB   sing N N 304 
PRO CA  HA   sing N N 305 
PRO C   O    doub N N 306 
PRO C   OXT  sing N N 307 
PRO CB  CG   sing N N 308 
PRO CB  HB2  sing N N 309 
PRO CB  HB3  sing N N 310 
PRO CG  CD   sing N N 311 
PRO CG  HG2  sing N N 312 
PRO CG  HG3  sing N N 313 
PRO CD  HD2  sing N N 314 
PRO CD  HD3  sing N N 315 
PRO OXT HXT  sing N N 316 
SER N   CA   sing N N 317 
SER N   H    sing N N 318 
SER N   H2   sing N N 319 
SER CA  C    sing N N 320 
SER CA  CB   sing N N 321 
SER CA  HA   sing N N 322 
SER C   O    doub N N 323 
SER C   OXT  sing N N 324 
SER CB  OG   sing N N 325 
SER CB  HB2  sing N N 326 
SER CB  HB3  sing N N 327 
SER OG  HG   sing N N 328 
SER OXT HXT  sing N N 329 
SO4 S   O1   doub N N 330 
SO4 S   O2   doub N N 331 
SO4 S   O3   sing N N 332 
SO4 S   O4   sing N N 333 
THR N   CA   sing N N 334 
THR N   H    sing N N 335 
THR N   H2   sing N N 336 
THR CA  C    sing N N 337 
THR CA  CB   sing N N 338 
THR CA  HA   sing N N 339 
THR C   O    doub N N 340 
THR C   OXT  sing N N 341 
THR CB  OG1  sing N N 342 
THR CB  CG2  sing N N 343 
THR CB  HB   sing N N 344 
THR OG1 HG1  sing N N 345 
THR CG2 HG21 sing N N 346 
THR CG2 HG22 sing N N 347 
THR CG2 HG23 sing N N 348 
THR OXT HXT  sing N N 349 
TRP N   CA   sing N N 350 
TRP N   H    sing N N 351 
TRP N   H2   sing N N 352 
TRP CA  C    sing N N 353 
TRP CA  CB   sing N N 354 
TRP CA  HA   sing N N 355 
TRP C   O    doub N N 356 
TRP C   OXT  sing N N 357 
TRP CB  CG   sing N N 358 
TRP CB  HB2  sing N N 359 
TRP CB  HB3  sing N N 360 
TRP CG  CD1  doub Y N 361 
TRP CG  CD2  sing Y N 362 
TRP CD1 NE1  sing Y N 363 
TRP CD1 HD1  sing N N 364 
TRP CD2 CE2  doub Y N 365 
TRP CD2 CE3  sing Y N 366 
TRP NE1 CE2  sing Y N 367 
TRP NE1 HE1  sing N N 368 
TRP CE2 CZ2  sing Y N 369 
TRP CE3 CZ3  doub Y N 370 
TRP CE3 HE3  sing N N 371 
TRP CZ2 CH2  doub Y N 372 
TRP CZ2 HZ2  sing N N 373 
TRP CZ3 CH2  sing Y N 374 
TRP CZ3 HZ3  sing N N 375 
TRP CH2 HH2  sing N N 376 
TRP OXT HXT  sing N N 377 
TYR N   CA   sing N N 378 
TYR N   H    sing N N 379 
TYR N   H2   sing N N 380 
TYR CA  C    sing N N 381 
TYR CA  CB   sing N N 382 
TYR CA  HA   sing N N 383 
TYR C   O    doub N N 384 
TYR C   OXT  sing N N 385 
TYR CB  CG   sing N N 386 
TYR CB  HB2  sing N N 387 
TYR CB  HB3  sing N N 388 
TYR CG  CD1  doub Y N 389 
TYR CG  CD2  sing Y N 390 
TYR CD1 CE1  sing Y N 391 
TYR CD1 HD1  sing N N 392 
TYR CD2 CE2  doub Y N 393 
TYR CD2 HD2  sing N N 394 
TYR CE1 CZ   doub Y N 395 
TYR CE1 HE1  sing N N 396 
TYR CE2 CZ   sing Y N 397 
TYR CE2 HE2  sing N N 398 
TYR CZ  OH   sing N N 399 
TYR OH  HH   sing N N 400 
TYR OXT HXT  sing N N 401 
VAL N   CA   sing N N 402 
VAL N   H    sing N N 403 
VAL N   H2   sing N N 404 
VAL CA  C    sing N N 405 
VAL CA  CB   sing N N 406 
VAL CA  HA   sing N N 407 
VAL C   O    doub N N 408 
VAL C   OXT  sing N N 409 
VAL CB  CG1  sing N N 410 
VAL CB  CG2  sing N N 411 
VAL CB  HB   sing N N 412 
VAL CG1 HG11 sing N N 413 
VAL CG1 HG12 sing N N 414 
VAL CG1 HG13 sing N N 415 
VAL CG2 HG21 sing N N 416 
VAL CG2 HG22 sing N N 417 
VAL CG2 HG23 sing N N 418 
VAL OXT HXT  sing N N 419 
# 
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                    7HGP 
_atom_sites.fract_transf_matrix[1][1]   0.024071 
_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]   0.023761 
_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]   0.006278 
_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  ? 1.089   4.218   2.197   1.00 65.55  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? 0.004   3.439   1.538   1.00 67.38  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.597   2.331   0.669   1.00 56.61  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.688   2.465   0.122   1.00 58.72  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -0.946  4.340   0.738   1.00 70.29  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -1.951  5.107   1.593   1.00 74.59  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.339  4.172   2.279   1.00 78.22  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -3.917  5.316   3.540   1.00 80.34  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.108  1.185   0.548   1.00 53.51  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? 0.328   0.072   -0.294  1.00 52.22  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.536   0.487   -1.748  1.00 46.76  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.145  1.362   -2.280  1.00 51.50  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -0.894  -0.876  -0.157  1.00 52.58  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.354  -0.626  1.264   1.00 56.87  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.364  0.887   1.263   1.00 52.50  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.483   -0.186  -2.390  1.00 46.03  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.657   -0.051  -3.819  1.00 42.09  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 1.018   -1.295  -4.425  1.00 40.09  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.452   -2.123  -3.711  1.00 45.08  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 3.156   0.106   -4.126  1.00 50.39  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.753   1.430   -3.744  1.00 61.85  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.330   2.213   -2.689  1.00 69.85  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.758   2.116   -4.319  1.00 69.52  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.051   3.327   -2.643  1.00 65.58  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.932   3.284   -3.618  1.00 64.64  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 1.091   -1.426  -5.744  1.00 36.10  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.851   -2.716  -6.358  1.00 36.32  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.996   -3.668  -6.000  1.00 32.61  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 3.082   -3.227  -5.595  1.00 35.86  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.740   -2.550  -7.862  1.00 40.86  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.721   -4.966  -6.111  1.00 31.67  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.736   -6.009  -5.975  1.00 33.26  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.880   -5.778  -6.959  1.00 36.17  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.682   -5.358  -8.099  1.00 37.24  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 2.161   -7.425  -6.090  1.00 32.87  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.379   -7.746  -4.825  1.00 33.59  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 2.063   -7.975  -3.625  1.00 31.75  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.022  -7.889  -4.851  1.00 33.03  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.409   -8.254  -2.439  1.00 34.24  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.668  -8.207  -3.654  1.00 30.87  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? 0.029   -8.388  -2.478  1.00 34.40  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 5.097   -6.066  -6.481  1.00 32.68  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.246   -5.988  -7.355  1.00 33.62  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 7.148   -7.184  -7.033  1.00 31.88  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 7.136   -7.685  -5.920  1.00 31.04  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 7.000   -4.684  -7.044  1.00 36.82  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.509   -4.552  -5.618  1.00 38.01  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.188   -3.193  -5.375  1.00 44.44  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.962   -3.150  -4.100  1.00 45.63  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 8.061   -3.211  -2.951  1.00 42.50  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 8.037   -7.586  -7.956  1.00 33.70  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.989   -8.665  -7.683  1.00 33.01  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.778   -8.376  -6.409  1.00 33.35  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.225  -7.258  -6.188  1.00 33.24  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.881   -8.652  -8.962  1.00 35.45  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.962   -8.071  -10.025 1.00 36.51  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 8.224   -6.959  -9.288  1.00 37.91  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.998   -9.425  -5.611  1.00 31.40  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.679  -9.291  -4.340  1.00 30.55  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.732   -9.185  -3.153  1.00 35.02  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 10.142  -9.438  -2.006  1.00 30.96  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.470   -8.768  -3.401  1.00 27.60  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.548   -8.740  -2.280  1.00 28.14  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.317   -10.125 -1.676  1.00 25.95  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 7.127   -11.073 -2.395  1.00 28.82  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.196   -8.167  -2.705  1.00 29.33  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 6.199   -6.661  -2.902  1.00 32.01  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 7.174   -5.993  -2.451  1.00 32.86  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.247   -6.150  -3.508  1.00 30.77  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.241   -10.183 -0.332  1.00 27.99  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 7.028   -11.428 0.406   1.00 28.23  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.558   -11.501 0.800   1.00 29.72  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.986   -10.507 1.262   1.00 32.13  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.929   -11.434 1.648   1.00 29.25  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.422   -11.265 1.313   1.00 31.43  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.265  -11.322 2.580   1.00 31.87  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.947   -12.225 0.224   1.00 31.27  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 5.015   -12.716 0.705   1.00 29.03  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.586   -12.901 0.938   1.00 29.04  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.352   -14.265 1.572   1.00 31.85  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 4.213   -15.137 1.612   1.00 29.14  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.806   -12.815 -0.389  1.00 31.15  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.960   -11.409 -1.001  1.00 31.96  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 3.224   -13.923 -1.378  1.00 30.29  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 2.113   -14.477 2.021   1.00 28.40  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.588   -15.809 2.039   1.00 29.44  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.612   -15.893 0.865   1.00 30.88  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.186  -14.966 0.650   1.00 29.27  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.818   -16.137 3.331   1.00 30.92  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.735   -16.256 4.533   1.00 34.39  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 2.086   -15.119 5.251   1.00 34.66  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 2.249   -17.491 4.919   1.00 32.49  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.955   -15.219 6.326   1.00 39.40  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 3.131   -17.589 6.003   1.00 36.49  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.483   -16.451 6.690   1.00 36.27  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.678   -17.008 0.133   1.00 31.03  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.121  -17.125 -1.082  1.00 30.43  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.087  -18.296 -0.901  1.00 33.80  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.710  -19.346 -0.378  1.00 33.28  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.745   -17.291 -2.328  1.00 29.02  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.342  -18.076 -1.332  1.00 31.37  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.353  -19.100 -1.097  1.00 34.86  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -3.668  -19.813 -2.411  1.00 35.03  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.038  -19.168 -3.379  1.00 39.80  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.578  -18.459 -0.432  1.00 33.21  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.667  -19.488 -0.033  1.00 41.47  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.222  -20.395 1.119   1.00 37.45  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.387  -21.102 1.774   1.00 45.58  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -6.809  -22.214 0.921   1.00 42.98  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.598  -21.151 -2.371  1.00 34.57  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.043  -22.021 -3.446  1.00 37.02  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.149  -22.895 -2.866  1.00 39.03  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.114  -23.208 -1.683  1.00 35.31  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -2.907  -22.993 -3.803  1.00 36.92  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -1.588  -22.300 -4.174  1.00 43.39  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.694  -21.806 -5.902  1.00 47.46  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.292  -23.281 -6.815  1.00 41.22  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.085  -23.293 -3.732  1.00 44.51  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.162  -24.207 -3.374  1.00 49.72  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.583  -25.452 -2.723  1.00 41.53  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -5.676  -26.067 -3.270  1.00 44.77  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -7.811  -24.658 -4.689  1.00 53.10  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.101  -25.466 -4.517  1.00 58.92  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.084 -24.783 -3.569  1.00 65.01  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.089  -25.809 -1.531  1.00 48.25  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -6.730  -27.084 -0.939  1.00 48.98  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.478  -27.001 -0.073  1.00 53.93  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.127  -27.976 0.580   1.00 57.88  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -4.811  -25.834 -0.060  1.00 43.17  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.583  -25.711 0.697   1.00 40.39  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.648  -24.583 1.716   1.00 39.33  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.331  -23.594 1.509   1.00 39.45  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.494  -25.336 -0.307  1.00 43.34  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.109  -26.432 -1.287  1.00 45.77  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.167  -27.384 -0.935  1.00 58.06  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.647  -26.470 -2.565  1.00 49.62  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -0.782  -28.368 -1.827  1.00 60.63  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.262  -27.444 -3.474  1.00 56.97  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.327  -28.395 -3.096  1.00 66.34  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -0.932  -29.383 -3.956  1.00 78.49  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -2.858  -24.649 2.810   1.00 37.09  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -2.806  -23.554 3.779   1.00 37.56  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.114  -22.369 3.068   1.00 36.76  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.437  -22.581 2.057   1.00 36.07  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -1.976  -24.161 4.937   1.00 41.20  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.122  -25.237 4.273   1.00 38.67  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -1.954  -25.773 3.133   1.00 41.20  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.403  -21.154 3.538   1.00 34.99  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.692  -19.933 3.153   1.00 30.51  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.188  -20.221 3.269   1.00 35.83  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? 0.272   -20.640 4.338   1.00 34.08  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.142  -18.765 4.033   1.00 33.06  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.595  -18.396 3.815   1.00 33.17  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.611  -19.062 4.480   1.00 39.38  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.205  -17.435 3.052   1.00 35.17  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -5.798  -18.530 4.139   1.00 40.31  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.577  -17.539 3.278   1.00 40.92  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.558   -20.032 2.163   1.00 34.48  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.884   -20.631 2.032   1.00 31.70  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.921   -19.515 1.912   1.00 30.36  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.770   -18.644 1.092   1.00 32.15  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.947   -21.479 0.766   1.00 31.87  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 3.020   -22.528 0.854   1.00 30.70  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.371   -22.367 0.686   1.00 31.94  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.792   -23.925 1.124   1.00 33.17  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 5.011   -23.586 0.843   1.00 32.97  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 4.063   -24.557 1.094   1.00 35.59  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.643   -24.698 1.373   1.00 37.30  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 4.226   -25.924 1.323   1.00 44.81  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.814   -26.060 1.576   1.00 41.38  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 3.084   -26.657 1.557   1.00 43.23  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 4.049   -19.560 2.643   1.00 29.69  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 5.094   -18.535 2.437   1.00 29.09  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.628   -18.543 0.990   1.00 31.44  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.900   -19.602 0.392   1.00 31.24  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 6.164   -19.059 3.456   1.00 30.58  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.955   -20.564 3.548   1.00 30.22  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.431   -20.606 3.602   1.00 31.08  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.739   -17.343 0.396   1.00 27.15  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 6.038   -17.229 -1.024  1.00 26.74  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.583   -15.824 -1.294  1.00 26.12  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.542   -14.942 -0.439  1.00 28.59  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.822   -17.553 -1.909  1.00 29.60  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 7.101   -15.636 -2.505  1.00 27.90  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.502   -14.321 -2.966  1.00 27.61  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.996   -14.061 -4.388  1.00 28.94  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.668   -15.013 -5.139  1.00 29.69  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 9.022   -14.185 -2.903  1.00 30.14  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.708   -15.084 -3.916  1.00 29.29  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 11.252  -14.883 -3.780  1.00 30.76  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.921  -15.675 -4.829  1.00 30.55  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 13.184  -16.103 -4.728  1.00 33.84  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.839  -15.969 -3.585  1.00 31.57  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.788  -16.699 -5.749  1.00 31.98  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.851   -12.777 -4.720  1.00 28.27  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.592   -12.400 -6.109  1.00 27.01  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.912   -12.508 -6.850  1.00 32.29  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.867   -11.885 -6.417  1.00 31.54  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 6.105   -10.951 -6.232  1.00 28.90  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.975   -10.618 -5.225  1.00 36.46  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.753   -10.638 -7.708  1.00 31.03  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.648   -11.275 -5.533  1.00 38.69  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.953   -13.334 -7.889  1.00 32.86  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 9.202   -13.520 -8.640  1.00 35.33  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.321   -12.508 -9.772  1.00 35.59  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.368   -11.865 -10.195 1.00 34.48  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.339   -14.924 -9.196  1.00 32.70  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 10.390  -15.816 -8.544  1.00 32.16  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.990  -15.401 -7.515  1.00 39.46  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.525  -16.949 -8.985  1.00 36.42  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.562  -12.325 -10.249 1.00 38.88  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.789  -11.681 -11.528 1.00 42.14  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.507  -12.723 -12.614 1.00 38.80  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.419  -13.923 -12.360 1.00 40.50  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.254  -11.262 -11.664 1.00 46.72  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.724  -10.045 -10.868 1.00 51.87  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.335  -8.918  -11.230 1.00 55.95  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.490  -10.230 -9.898  1.00 56.35  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.320  -12.254 -13.842 1.00 42.25  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.312  -13.159 -14.983 1.00 43.90  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.645  -12.943 -15.692 1.00 43.59  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.992  -11.803 -15.961 1.00 43.81  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 9.134   -12.760 -15.882 1.00 44.42  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.806   -12.856 -15.113 1.00 47.16  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 9.116   -13.569 -17.177 1.00 41.71  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.791   -11.831 -15.551 1.00 45.25  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.420  -14.011 -15.892 1.00 44.04  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.726  -13.888 -16.535 1.00 43.04  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.517  -13.546 -18.013 1.00 39.58  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.485  -13.882 -18.592 1.00 40.66  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.472  -15.201 -16.405 1.00 45.54  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.497  -12.866 -18.617 1.00 43.61  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.497  -12.702 -20.067 1.00 40.92  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.349  -14.076 -20.707 1.00 35.48  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 15.026  -15.013 -20.304 1.00 37.55  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.811  -12.060 -20.506 1.00 40.10  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.978  -10.578 -20.225 1.00 42.56  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.971  -9.907  -20.012 1.00 47.13  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 17.139  -10.107 -20.249 1.00 46.14  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.414  -14.179 -21.669 1.00 37.16  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 13.199  -15.352 -22.502 1.00 35.44  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.248  -16.369 -21.863 1.00 37.90  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.966  -17.374 -22.482 1.00 40.54  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.832  -16.137 -20.608 1.00 38.24  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.993  -17.101 -19.899 1.00 38.53  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.514   -16.824 -20.173 1.00 37.78  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 9.106   -15.720 -20.530 1.00 44.21  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.271  -16.979 -18.398 1.00 41.15  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.685   -17.839 -19.885 1.00 43.00  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 7.243   -17.780 -20.082 1.00 44.29  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.626   -16.741 -19.145 1.00 40.15  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.883   -16.775 -17.948 1.00 44.34  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.755   -19.212 -19.748 1.00 48.84  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 5.251   -19.291 -19.552 1.00 46.03  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.211   -20.230 -20.789 1.00 48.18  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.818   -15.820 -19.698 1.00 45.60  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 5.160   -14.766 -18.935 1.00 47.16  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.873   -15.283 -18.288 1.00 46.87  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.323   -16.293 -18.711 1.00 44.22  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.862   -13.498 -19.741 1.00 42.99  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 6.083   -12.733 -20.232 1.00 46.67  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.753   -11.472 -21.022 1.00 58.28  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.179   -11.767 -22.384 1.00 55.34  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 5.123   -10.529 -23.163 1.00 57.72  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.380   -14.641 -17.203 1.00 46.45  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 2.120   -15.070 -16.590 1.00 44.81  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.970   -14.572 -17.456 1.00 45.83  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 1.121   -13.661 -18.248 1.00 46.13  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 2.073   -14.369 -15.228 1.00 45.24  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.019   -13.188 -15.355 1.00 50.35  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.961   -13.462 -16.546 1.00 45.17  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.260  -15.066 -17.221 1.00 45.63  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.443  -14.481 -17.858 1.00 50.43  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.627  -13.039 -17.403 1.00 52.43  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.140  -12.651 -16.340 1.00 44.71  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.574  -15.385 -17.344 1.00 47.30  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -1.890  -16.680 -16.994 1.00 42.00  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.555  -16.249 -16.399 1.00 47.56  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.369  -12.201 -18.162 1.00 51.12  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.726  -10.863 -17.696 1.00 53.37  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.291  -10.949 -16.283 1.00 46.74  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -3.970  -11.919 -15.944 1.00 50.40  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.792  -10.381 -18.715 1.00 57.55  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.164  -11.626 -19.483 1.00 49.34  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -2.905  -12.484 -19.511 1.00 60.08  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -2.963  -9.920  -15.497 1.00 49.10  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.446  -9.682  -14.150 1.00 50.99  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -2.940  -10.751 -13.186 1.00 43.42  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.413  -10.775 -12.048 1.00 42.43  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -4.964  -9.544  -14.097 1.00 56.02  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.422  -8.369  -14.926 1.00 65.57  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.124  -7.214  -14.586 1.00 61.95  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.127  -8.650  -16.011 1.00 65.50  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -1.997  -11.605 -13.635 1.00 36.84  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.422  -12.604 -12.734 1.00 33.05  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? 0.047   -12.289 -12.452 1.00 33.45  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.706   -11.571 -13.221 1.00 37.71  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.548  -14.065 -13.158 1.00 37.55  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -2.975  -14.473 -13.604 1.00 40.62  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -3.833  -14.477 -12.347 1.00 46.10  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.323  -14.593 -12.590 1.00 53.46  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -5.650  -16.006 -12.779 1.00 55.59  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.517   -12.772 -11.289 1.00 30.64  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.921   -12.605 -10.912 1.00 31.74  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.579   -13.970 -10.843 1.00 29.95  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.969   -14.959 -10.460 1.00 32.00  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 2.008   -12.051 -9.471  1.00 29.92  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.507   -10.620 -9.465  1.00 34.55  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? 0.154   -10.326 -9.397  1.00 37.95  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.399   -9.565  -9.627  1.00 36.97  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.294  -9.012  -9.458  1.00 41.68  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.958   -8.246  -9.702  1.00 38.70  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.606   -7.974  -9.604  1.00 41.22  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? 0.133   -6.684  -9.697  1.00 40.02  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.902   -14.077 -11.095 1.00 29.88  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.581   -15.348 -10.847 1.00 27.91  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.885   -15.484 -9.356  1.00 29.90  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.546   -14.603 -8.796  1.00 33.25  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.844   -15.243 -11.709 1.00 31.99  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 6.083   -13.788 -11.881 1.00 31.58  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.776   -13.005 -11.607 1.00 35.21  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.359   -16.549 -8.732  1.00 30.37  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.549   -16.724 -7.292  1.00 29.52  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.532   -17.881 -7.083  1.00 30.31  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 5.285   -19.020 -7.513  1.00 33.77  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 3.197   -16.999 -6.598  1.00 28.98  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 2.175   -15.878 -6.938  1.00 30.97  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.420   -17.142 -5.075  1.00 28.03  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.709   -14.481 -6.585  1.00 32.23  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.619   -17.616 -6.336  1.00 27.03  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.538   -18.689 -6.014  1.00 27.41  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 7.262   -19.128 -4.581  1.00 30.06  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 7.259   -18.305 -3.668  1.00 32.25  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.960   -18.097 -6.154  1.00 29.62  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.977   -19.150 -5.747  1.00 29.98  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.341  -20.163 -6.651  1.00 35.72  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.576  -19.098 -4.484  1.00 36.19  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.288  -21.113 -6.285  1.00 36.32  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.511  -20.072 -4.116  1.00 37.22  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.885  -21.049 -5.025  1.00 38.75  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.901   -20.406 -4.400  1.00 30.68  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.535   -20.928 -3.089  1.00 28.83  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.801   -21.419 -2.400  1.00 32.09  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.507   -22.325 -2.913  1.00 31.78  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.573   -22.126 -3.295  1.00 34.06  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 4.212   -21.613 -3.739  1.00 32.35  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.929   -21.370 -5.082  1.00 37.13  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 3.211   -21.347 -2.784  1.00 34.54  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.668   -20.882 -5.447  1.00 37.12  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.971   -20.831 -3.158  1.00 30.95  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.708   -20.602 -4.491  1.00 35.98  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 8.065   -20.827 -1.227  1.00 31.23  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 9.216   -21.307 -0.454  1.00 33.37  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.992   -22.760 -0.038  1.00 35.00  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.853   -23.248 0.070   1.00 34.28  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.440   -20.384 0.754   1.00 34.29  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.914   -18.996 0.358   1.00 29.56  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 11.189  -18.804 -0.207  1.00 29.61  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 9.141   -17.854 0.598   1.00 31.92  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.608  -17.535 -0.561  1.00 28.80  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.614   -16.578 0.278   1.00 30.46  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.828  -16.424 -0.327  1.00 31.21  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 10.110  -23.475 0.156   1.00 33.39  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 10.025  -24.836 0.672   1.00 33.79  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.816   -25.834 -0.482  1.00 41.62  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.661  -26.678 -0.735  1.00 39.43  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.698   -25.722 -1.218  1.00 41.74  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.478   -26.569 -2.389  1.00 41.66  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 9.304   -26.121 -3.588  1.00 42.09  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.614   -26.936 -4.459  1.00 39.12  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 7.003   -26.634 -2.774  1.00 40.84  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.622   -25.359 -3.291  1.00 39.80  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 6.114   -27.089 -1.635  1.00 40.90  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.582   -24.812 -3.659  1.00 34.85  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 10.286  -24.194 -4.773  1.00 35.95  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.492   -24.315 -6.071  1.00 35.31  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 10.073  -24.330 -7.150  1.00 40.86  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.712  -24.747 -4.910  1.00 33.94  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.411  -24.766 -3.581  1.00 37.29  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 13.201  -25.805 -3.127  1.00 35.85  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.407  -23.842 -2.598  1.00 34.93  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.642  -25.515 -1.908  1.00 42.70  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 13.230  -24.303 -1.583  1.00 41.59  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 8.157   -24.358 -5.969  1.00 39.68  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 7.328   -24.428 -7.160  1.00 38.17  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.854   -23.020 -7.524  1.00 39.64  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.873   -22.121 -6.674  1.00 35.38  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 6.135   -25.346 -6.878  1.00 38.73  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.529   -26.802 -6.612  1.00 46.45  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 5.494   -27.727 -5.998  1.00 55.51  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 4.389   -27.279 -5.625  1.00 57.67  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.815   -28.926 -5.883  1.00 54.18  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 6.451   -22.822 -8.791  1.00 36.84  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.898   -21.539 -9.203  1.00 37.34  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.460   -21.755 -9.668  1.00 39.00  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 4.170   -22.749 -10.343 1.00 43.34  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.761   -20.895 -10.294 1.00 39.55  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 8.091   -20.565 -9.889  1.00 41.35  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 6.184   -19.591 -10.832 1.00 46.16  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.550   -20.850 -9.272  1.00 34.68  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 2.218   -20.787 -9.845  1.00 33.91  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.891   -19.332 -10.159 1.00 34.99  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.587   -18.424 -9.713  1.00 34.78  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 1.216   -21.383 -8.886  1.00 36.13  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.835   -19.097 -10.958 1.00 32.61  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.445   -17.739 -11.304 1.00 34.83  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -0.832  -17.417 -10.550 1.00 36.89  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -1.782  -18.199 -10.587 1.00 40.10  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? 0.065   -17.734 -12.791 1.00 37.87  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.258   -18.056 -13.663 1.00 39.26  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.436   -17.326 -13.523 1.00 43.75  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 1.197   -19.084 -14.605 1.00 42.33  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.549   -17.640 -14.300 1.00 57.40  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.311   -19.395 -15.357 1.00 44.82  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.472   -18.657 -15.223 1.00 43.99  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -0.782  -16.336 -9.771  1.00 31.67  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -1.881  -15.957 -8.902  1.00 31.60  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.167  -14.473 -9.050  1.00 34.81  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.315  -13.622 -9.367  1.00 32.61  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.564  -16.288 -7.445  1.00 34.02  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.481  -17.776 -7.109  1.00 34.89  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.119  -17.811 -5.623  1.00 35.01  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -2.877  -18.404 -7.306  1.00 37.59  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.413  -14.144 -8.731  1.00 29.62  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -3.726  -12.731 -8.687  1.00 30.96  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -3.804  -12.245 -7.225  1.00 30.12  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -3.773  -13.067 -6.307  1.00 28.21  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -3.879  -10.903 -7.009  1.00 30.26  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -3.826  -10.273 -5.676  1.00 30.64  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -4.834  -10.775 -4.650  1.00 30.39  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.562  -10.749 -3.462  1.00 29.56  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.079  -8.766  -5.989  1.00 33.20  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.551  -8.588  -7.433  1.00 32.65  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -3.920  -9.907  -8.086  1.00 31.93  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -5.965  -11.312 -5.136  1.00 33.62  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -6.949  -11.853 -4.197  1.00 35.29  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.401  -12.985 -3.330  1.00 32.38  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -6.880  -13.208 -2.212  1.00 30.99  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.212  -12.402 -4.878  1.00 37.35  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.056  -13.711 -5.614  1.00 39.84  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.383  -14.070 -6.294  1.00 41.49  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.320  -15.328 -7.095  1.00 45.97  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -8.785  -16.485 -6.370  1.00 56.32  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.356  -13.677 -3.833  1.00 31.34  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -4.784  -14.810 -3.164  1.00 31.23  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.431  -14.453 -2.530  1.00 31.89  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -2.736  -15.354 -2.091  1.00 29.74  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -4.702  -15.953 -4.166  1.00 35.84  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.089  -16.511 -4.471  1.00 34.58  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -6.903  -16.519 -3.515  1.00 36.83  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.324  -16.928 -5.626  1.00 36.72  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.085  -13.154 -2.477  1.00 29.11  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -1.746  -12.733 -1.999  1.00 26.22  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -1.880  -11.882 -0.733  1.00 24.67  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.496  -10.795 -0.758  1.00 28.63  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.021  -11.985 -3.131  1.00 27.43  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -0.853  -12.783 -4.430  1.00 30.23  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.136  -11.859 -5.392  1.00 30.44  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.015  -14.084 -4.276  1.00 27.95  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.321  -12.363 0.391   1.00 27.88  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.434  -11.668 1.677   1.00 26.64  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.049  -11.172 2.081   1.00 30.34  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.844   -12.001 2.280   1.00 33.04  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -1.884  -12.699 2.701   1.00 29.63  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.322  -13.129 2.419   1.00 30.97  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.617  -13.988 1.369   1.00 33.89  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.357  -12.614 3.207   1.00 34.32  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -4.935  -14.345 1.092   1.00 37.20  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.671  -12.969 2.919   1.00 32.77  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -5.934  -13.869 1.915   1.00 32.31  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? 0.196   -9.854  2.166   1.00 33.33  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.552   -9.380  2.493   1.00 30.75  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 2.103   -10.014 3.774   1.00 32.85  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.413   -10.176 4.780   1.00 32.92  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.364   -7.856  2.599   1.00 35.23  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? 0.240   -7.581  1.588   1.00 38.27  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -0.746  -8.745  1.873   1.00 34.79  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.400   -10.407 3.748   1.00 33.67  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.920   -11.267 4.790   1.00 33.63  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.965   -10.597 6.170   1.00 32.46  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.604   -11.252 7.148   1.00 35.54  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.326   -11.703 4.344   1.00 33.28  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 6.092   -12.460 5.415   1.00 32.45  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.844   -13.803 5.664   1.00 34.18  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 7.110   -11.837 6.131   1.00 37.47  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.548   -14.522 6.630   1.00 39.50  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.834   -12.552 7.072   1.00 36.35  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.559   -13.880 7.324   1.00 39.48  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 8.303   -14.547 8.276   1.00 37.19  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.409   -9.333  6.222   1.00 33.65  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.546   -8.645  7.509   1.00 39.31  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 3.216   -8.632  8.263   1.00 39.24  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 3.154   -9.100  9.403   1.00 45.36  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 5.233   -7.293  7.389   1.00 38.48  ? 62  ASP A CB  1 
ATOM   495  C CG  . ASP A 1 63 ? 6.734   -7.365  7.131   1.00 58.81  ? 62  ASP A CG  1 
ATOM   496  O OD1 . ASP A 1 63 ? 7.320   -8.417  7.468   1.00 65.55  ? 62  ASP A OD1 1 
ATOM   497  O OD2 . ASP A 1 63 ? 7.307   -6.376  6.584   1.00 66.43  ? 62  ASP A OD2 1 
ATOM   498  N N   . LYS A 1 64 ? 2.156   -8.187  7.573   1.00 40.95  ? 63  LYS A N   1 
ATOM   499  C CA  . LYS A 1 64 ? 0.825   -8.114  8.163   1.00 40.14  ? 63  LYS A CA  1 
ATOM   500  C C   . LYS A 1 64 ? 0.292   -9.492  8.566   1.00 43.20  ? 63  LYS A C   1 
ATOM   501  O O   . LYS A 1 64 ? -0.452  -9.569  9.547   1.00 40.87  ? 63  LYS A O   1 
ATOM   502  C CB  . LYS A 1 64 ? -0.110  -7.452  7.149   1.00 38.12  ? 63  LYS A CB  1 
ATOM   503  C CG  . LYS A 1 64 ? -1.565  -7.327  7.611   1.00 45.04  ? 63  LYS A CG  1 
ATOM   504  C CD  . LYS A 1 64 ? -2.342  -6.643  6.492   1.00 45.45  ? 63  LYS A CD  1 
ATOM   505  C CE  . LYS A 1 64 ? -3.524  -5.921  7.044   1.00 47.03  ? 63  LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 64 ? -4.492  -6.809  7.676   1.00 58.09  ? 63  LYS A NZ  1 
ATOM   507  N N   . SER A 1 65 ? 0.661   -10.579 7.847   1.00 35.90  ? 64  SER A N   1 
ATOM   508  C CA  . SER A 1 65 ? -0.058  -11.850 7.918   1.00 35.50  ? 64  SER A CA  1 
ATOM   509  C C   . SER A 1 65 ? 0.646   -12.943 8.723   1.00 35.53  ? 64  SER A C   1 
ATOM   510  O O   . SER A 1 65 ? 0.084   -14.020 8.933   1.00 36.19  ? 64  SER A O   1 
ATOM   511  C CB  . SER A 1 65 ? -0.343  -12.380 6.527   1.00 37.57  ? 64  SER A CB  1 
ATOM   512  O OG  . SER A 1 65 ? -1.317  -11.538 5.931   1.00 48.80  ? 64  SER A OG  1 
ATOM   513  N N   . LYS A 1 66 ? 1.913   -12.716 9.082   1.00 38.45  ? 65  LYS A N   1 
ATOM   514  C CA  . LYS A 1 66 ? 2.729   -13.827 9.560   1.00 38.63  ? 65  LYS A CA  1 
ATOM   515  C C   . LYS A 1 66 ? 2.278   -14.310 10.941  1.00 36.89  ? 65  LYS A C   1 
ATOM   516  O O   . LYS A 1 66 ? 2.448   -15.486 11.269  1.00 40.56  ? 65  LYS A O   1 
ATOM   517  C CB  . LYS A 1 66 ? 4.208   -13.417 9.547   1.00 39.02  ? 65  LYS A CB  1 
ATOM   518  C CG  . LYS A 1 66 ? 4.606   -12.225 10.391  1.00 40.92  ? 65  LYS A CG  1 
ATOM   519  C CD  . LYS A 1 66 ? 6.127   -12.165 10.461  1.00 54.89  ? 65  LYS A CD  1 
ATOM   520  C CE  . LYS A 1 66 ? 6.578   -11.184 11.497  1.00 54.18  ? 65  LYS A CE  1 
ATOM   521  N NZ  . LYS A 1 66 ? 6.080   -9.834  11.216  1.00 64.72  ? 65  LYS A NZ  1 
ATOM   522  N N   A ASP A 1 67 ? 1.712   -13.402 11.746  0.50 43.16  ? 66  ASP A N   1 
ATOM   523  N N   B ASP A 1 67 ? 1.735   -13.400 11.757  0.50 41.52  ? 66  ASP A N   1 
ATOM   524  C CA  A ASP A 1 67 ? 1.247   -13.771 13.079  0.50 44.79  ? 66  ASP A CA  1 
ATOM   525  C CA  B ASP A 1 67 ? 1.241   -13.801 13.067  0.50 41.27  ? 66  ASP A CA  1 
ATOM   526  C C   A ASP A 1 67 ? 0.141   -14.815 12.949  0.50 44.60  ? 66  ASP A C   1 
ATOM   527  C C   B ASP A 1 67 ? 0.235   -14.928 12.857  0.50 40.72  ? 66  ASP A C   1 
ATOM   528  O O   A ASP A 1 67 ? 0.005   -15.685 13.797  0.50 46.18  ? 66  ASP A O   1 
ATOM   529  O O   B ASP A 1 67 ? 0.275   -15.955 13.523  0.50 38.41  ? 66  ASP A O   1 
ATOM   530  C CB  A ASP A 1 67 ? 0.848   -12.558 13.910  0.50 46.65  ? 66  ASP A CB  1 
ATOM   531  C CB  B ASP A 1 67 ? 0.587   -12.645 13.811  0.50 40.98  ? 66  ASP A CB  1 
ATOM   532  C CG  A ASP A 1 67 ? 1.996   -11.769 14.528  0.50 52.58  ? 66  ASP A CG  1 
ATOM   533  C CG  B ASP A 1 67 ? 0.022   -13.002 15.178  0.50 46.13  ? 66  ASP A CG  1 
ATOM   534  O OD1 A ASP A 1 67 ? 3.118   -12.310 14.584  0.50 55.94  ? 66  ASP A OD1 1 
ATOM   535  O OD1 B ASP A 1 67 ? 0.828   -13.277 16.091  0.50 49.03  ? 66  ASP A OD1 1 
ATOM   536  O OD2 A ASP A 1 67 ? 1.773   -10.607 14.934  0.50 51.67  ? 66  ASP A OD2 1 
ATOM   537  O OD2 B ASP A 1 67 ? -1.227  -13.058 15.304  0.50 46.63  ? 66  ASP A OD2 1 
ATOM   538  N N   . LYS A 1 68 ? -0.632  -14.741 11.857  1.00 41.56  ? 67  LYS A N   1 
ATOM   539  C CA  . LYS A 1 68 ? -1.752  -15.639 11.657  1.00 40.96  ? 67  LYS A CA  1 
ATOM   540  C C   . LYS A 1 68 ? -1.343  -16.878 10.870  1.00 42.70  ? 67  LYS A C   1 
ATOM   541  O O   . LYS A 1 68 ? -1.918  -17.953 11.068  1.00 44.76  ? 67  LYS A O   1 
ATOM   542  C CB  . LYS A 1 68 ? -2.849  -14.882 10.901  1.00 41.93  ? 67  LYS A CB  1 
ATOM   543  C CG  . LYS A 1 68 ? -4.085  -15.709 10.686  1.00 43.72  ? 67  LYS A CG  1 
ATOM   544  C CD  . LYS A 1 68 ? -5.169  -14.793 10.106  1.00 42.69  ? 67  LYS A CD  1 
ATOM   545  C CE  . LYS A 1 68 ? -6.385  -15.517 9.612   1.00 55.33  ? 67  LYS A CE  1 
ATOM   546  N NZ  . LYS A 1 68 ? -7.328  -14.497 9.150   1.00 53.48  ? 67  LYS A NZ  1 
ATOM   547  N N   . TYR A 1 69 ? -0.452  -16.707 9.875   1.00 37.60  ? 68  TYR A N   1 
ATOM   548  C CA  . TYR A 1 69 ? -0.229  -17.797 8.945   1.00 33.21  ? 68  TYR A CA  1 
ATOM   549  C C   . TYR A 1 69 ? 1.167   -18.421 9.090   1.00 34.67  ? 68  TYR A C   1 
ATOM   550  O O   . TYR A 1 69 ? 1.419   -19.476 8.527   1.00 36.83  ? 68  TYR A O   1 
ATOM   551  C CB  . TYR A 1 69 ? -0.383  -17.312 7.487   1.00 34.76  ? 68  TYR A CB  1 
ATOM   552  C CG  . TYR A 1 69 ? -1.789  -16.886 7.071   1.00 37.63  ? 68  TYR A CG  1 
ATOM   553  C CD1 . TYR A 1 69 ? -2.912  -17.652 7.400   1.00 39.77  ? 68  TYR A CD1 1 
ATOM   554  C CD2 . TYR A 1 69 ? -1.981  -15.692 6.377   1.00 36.88  ? 68  TYR A CD2 1 
ATOM   555  C CE1 . TYR A 1 69 ? -4.185  -17.236 7.029   1.00 41.40  ? 68  TYR A CE1 1 
ATOM   556  C CE2 . TYR A 1 69 ? -3.248  -15.259 6.015   1.00 37.90  ? 68  TYR A CE2 1 
ATOM   557  C CZ  . TYR A 1 69 ? -4.344  -16.041 6.339   1.00 37.80  ? 68  TYR A CZ  1 
ATOM   558  O OH  . TYR A 1 69 ? -5.568  -15.571 5.948   1.00 38.81  ? 68  TYR A OH  1 
ATOM   559  N N   . GLY A 1 70 ? 2.063   -17.793 9.836   1.00 37.90  ? 69  GLY A N   1 
ATOM   560  C CA  . GLY A 1 70 ? 3.436   -18.286 9.845   1.00 35.51  ? 69  GLY A CA  1 
ATOM   561  C C   . GLY A 1 70 ? 3.657   -19.246 11.018  1.00 39.43  ? 69  GLY A C   1 
ATOM   562  O O   . GLY A 1 70 ? 4.430   -18.961 11.913  1.00 48.25  ? 69  GLY A O   1 
ATOM   563  N N   . LYS A 1 71 ? 2.919   -20.350 10.998  1.00 43.95  ? 70  LYS A N   1 
ATOM   564  C CA  . LYS A 1 71 ? 3.018   -21.377 12.017  1.00 46.93  ? 70  LYS A CA  1 
ATOM   565  C C   . LYS A 1 71 ? 3.326   -22.699 11.329  1.00 41.43  ? 70  LYS A C   1 
ATOM   566  O O   . LYS A 1 71 ? 2.937   -22.944 10.183  1.00 40.49  ? 70  LYS A O   1 
ATOM   567  C CB  . LYS A 1 71 ? 1.764   -21.386 12.905  1.00 50.98  ? 70  LYS A CB  1 
ATOM   568  C CG  . LYS A 1 71 ? 1.741   -20.214 13.873  1.00 51.76  ? 70  LYS A CG  1 
ATOM   569  C CD  . LYS A 1 71 ? 0.517   -20.206 14.780  1.00 63.93  ? 70  LYS A CD  1 
ATOM   570  N N   . PRO A 1 72 ? 4.041   -23.620 12.009  1.00 44.38  ? 71  PRO A N   1 
ATOM   571  C CA  . PRO A 1 72 ? 4.363   -24.900 11.391  1.00 42.46  ? 71  PRO A CA  1 
ATOM   572  C C   . PRO A 1 72 ? 3.119   -25.623 10.900  1.00 43.84  ? 71  PRO A C   1 
ATOM   573  O O   . PRO A 1 72 ? 2.055   -25.516 11.515  1.00 46.93  ? 71  PRO A O   1 
ATOM   574  C CB  . PRO A 1 72 ? 5.097   -25.684 12.496  1.00 45.24  ? 71  PRO A CB  1 
ATOM   575  C CG  . PRO A 1 72 ? 5.633   -24.604 13.407  1.00 46.09  ? 71  PRO A CG  1 
ATOM   576  C CD  . PRO A 1 72 ? 4.621   -23.448 13.353  1.00 47.90  ? 71  PRO A CD  1 
ATOM   577  N N   . ASN A 1 73 ? 3.299   -26.381 9.818   1.00 44.81  ? 72  ASN A N   1 
ATOM   578  C CA  . ASN A 1 73 ? 2.267   -27.156 9.152   1.00 51.64  ? 72  ASN A CA  1 
ATOM   579  C C   . ASN A 1 73 ? 2.902   -28.493 8.809   1.00 56.99  ? 72  ASN A C   1 
ATOM   580  O O   . ASN A 1 73 ? 4.120   -28.584 8.675   1.00 62.11  ? 72  ASN A O   1 
ATOM   581  C CB  . ASN A 1 73 ? 1.810   -26.470 7.858   1.00 49.34  ? 72  ASN A CB  1 
ATOM   582  C CG  . ASN A 1 73 ? 0.409   -26.846 7.417   1.00 56.63  ? 72  ASN A CG  1 
ATOM   583  O OD1 . ASN A 1 73 ? 0.242   -27.633 6.483   1.00 49.53  ? 72  ASN A OD1 1 
ATOM   584  N ND2 . ASN A 1 73 ? -0.614  -26.280 8.040   1.00 62.15  ? 72  ASN A ND2 1 
ATOM   585  N N   . LYS A 1 74 ? 2.068   -29.520 8.643   1.00 57.26  ? 73  LYS A N   1 
ATOM   586  C CA  . LYS A 1 74 ? 2.565   -30.859 8.403   1.00 55.14  ? 73  LYS A CA  1 
ATOM   587  C C   . LYS A 1 74 ? 2.815   -31.072 6.912   1.00 52.33  ? 73  LYS A C   1 
ATOM   588  O O   . LYS A 1 74 ? 3.495   -32.021 6.533   1.00 52.09  ? 73  LYS A O   1 
ATOM   589  C CB  . LYS A 1 74 ? 1.541   -31.838 9.000   1.00 67.19  ? 73  LYS A CB  1 
ATOM   590  C CG  . LYS A 1 74 ? 0.415   -32.282 8.064   1.00 68.75  ? 73  LYS A CG  1 
ATOM   591  N N   . ARG A 1 75 ? 2.284   -30.175 6.067   1.00 46.57  ? 74  ARG A N   1 
ATOM   592  C CA  . ARG A 1 75 ? 2.400   -30.334 4.625   1.00 45.75  ? 74  ARG A CA  1 
ATOM   593  C C   . ARG A 1 75 ? 3.857   -30.236 4.190   1.00 47.70  ? 74  ARG A C   1 
ATOM   594  O O   . ARG A 1 75 ? 4.595   -29.381 4.684   1.00 41.12  ? 74  ARG A O   1 
ATOM   595  C CB  . ARG A 1 75 ? 1.541   -29.302 3.883   1.00 52.80  ? 74  ARG A CB  1 
ATOM   596  C CG  . ARG A 1 75 ? 0.063   -29.511 4.190   1.00 59.79  ? 74  ARG A CG  1 
ATOM   597  C CD  . ARG A 1 75 ? -0.621  -30.601 3.384   1.00 51.27  ? 74  ARG A CD  1 
ATOM   598  N NE  . ARG A 1 75 ? -1.534  -30.074 2.365   1.00 67.25  ? 74  ARG A NE  1 
ATOM   599  C CZ  . ARG A 1 75 ? -2.642  -29.378 2.631   1.00 56.91  ? 74  ARG A CZ  1 
ATOM   600  N NH1 . ARG A 1 75 ? -3.433  -29.014 1.646   1.00 64.82  ? 74  ARG A NH1 1 
ATOM   601  N NH2 . ARG A 1 75 ? -2.978  -29.075 3.876   1.00 67.44  ? 74  ARG A NH2 1 
ATOM   602  N N   . LYS A 1 76 ? 4.187   -31.070 3.198   1.00 46.47  ? 75  LYS A N   1 
ATOM   603  C CA  . LYS A 1 76 ? 5.518   -31.214 2.646   1.00 48.40  ? 75  LYS A CA  1 
ATOM   604  C C   . LYS A 1 76 ? 6.045   -29.846 2.217   1.00 46.11  ? 75  LYS A C   1 
ATOM   605  O O   . LYS A 1 76 ? 5.450   -29.176 1.374   1.00 39.60  ? 75  LYS A O   1 
ATOM   606  C CB  . LYS A 1 76 ? 5.445   -32.132 1.426   1.00 47.13  ? 75  LYS A CB  1 
ATOM   607  C CG  . LYS A 1 76 ? 6.807   -32.563 0.908   1.00 54.50  ? 75  LYS A CG  1 
ATOM   608  C CD  . LYS A 1 76 ? 6.757   -33.571 -0.234  1.00 56.50  ? 75  LYS A CD  1 
ATOM   609  C CE  . LYS A 1 76 ? 8.146   -33.948 -0.652  1.00 60.36  ? 75  LYS A CE  1 
ATOM   610  N N   . GLY A 1 77 ? 7.192   -29.460 2.772   1.00 43.41  ? 76  GLY A N   1 
ATOM   611  C CA  . GLY A 1 77 ? 7.860   -28.271 2.271   1.00 42.02  ? 76  GLY A CA  1 
ATOM   612  C C   . GLY A 1 77 ? 7.532   -27.030 3.096   1.00 39.87  ? 76  GLY A C   1 
ATOM   613  O O   . GLY A 1 77 ? 8.277   -26.061 3.047   1.00 39.19  ? 76  GLY A O   1 
ATOM   614  N N   . PHE A 1 78 ? 6.449   -27.072 3.875   1.00 37.60  ? 77  PHE A N   1 
ATOM   615  C CA  . PHE A 1 78 ? 5.964   -25.866 4.529   1.00 38.73  ? 77  PHE A CA  1 
ATOM   616  C C   . PHE A 1 78 ? 7.005   -25.287 5.504   1.00 44.51  ? 77  PHE A C   1 
ATOM   617  O O   . PHE A 1 78 ? 7.311   -24.094 5.471   1.00 40.23  ? 77  PHE A O   1 
ATOM   618  C CB  . PHE A 1 78 ? 4.591   -26.163 5.142   1.00 37.01  ? 77  PHE A CB  1 
ATOM   619  C CG  . PHE A 1 78 ? 3.858   -24.890 5.519   1.00 37.78  ? 77  PHE A CG  1 
ATOM   620  C CD1 . PHE A 1 78 ? 4.156   -24.222 6.699   1.00 38.75  ? 77  PHE A CD1 1 
ATOM   621  C CD2 . PHE A 1 78 ? 2.895   -24.358 4.667   1.00 39.09  ? 77  PHE A CD2 1 
ATOM   622  C CE1 . PHE A 1 78 ? 3.517   -23.038 7.029   1.00 38.73  ? 77  PHE A CE1 1 
ATOM   623  C CE2 . PHE A 1 78 ? 2.253   -23.178 5.004   1.00 33.17  ? 77  PHE A CE2 1 
ATOM   624  C CZ  . PHE A 1 78 ? 2.565   -22.527 6.178   1.00 34.48  ? 77  PHE A CZ  1 
ATOM   625  N N   . ASN A 1 79 ? 7.524   -26.120 6.416   1.00 38.21  ? 78  ASN A N   1 
ATOM   626  C CA  . ASN A 1 79 ? 8.367   -25.611 7.489   1.00 40.46  ? 78  ASN A CA  1 
ATOM   627  C C   . ASN A 1 79 ? 9.726   -25.163 6.933   1.00 37.18  ? 78  ASN A C   1 
ATOM   628  O O   . ASN A 1 79 ? 10.300  -24.194 7.453   1.00 38.55  ? 78  ASN A O   1 
ATOM   629  C CB  . ASN A 1 79 ? 8.467   -26.632 8.620   1.00 38.93  ? 78  ASN A CB  1 
ATOM   630  C CG  . ASN A 1 79 ? 7.111   -26.969 9.202   1.00 47.42  ? 78  ASN A CG  1 
ATOM   631  O OD1 . ASN A 1 79 ? 6.174   -26.160 9.123   1.00 39.28  ? 78  ASN A OD1 1 
ATOM   632  N ND2 . ASN A 1 79 ? 6.988   -28.147 9.810   1.00 41.11  ? 78  ASN A ND2 1 
ATOM   633  N N   . GLU A 1 80 ? 10.237  -25.879 5.918   1.00 36.40  ? 79  GLU A N   1 
ATOM   634  C CA  . GLU A 1 80 ? 11.395  -25.384 5.167   1.00 37.17  ? 79  GLU A CA  1 
ATOM   635  C C   . GLU A 1 80 ? 11.082  -23.992 4.616   1.00 35.88  ? 79  GLU A C   1 
ATOM   636  O O   . GLU A 1 80 ? 11.906  -23.058 4.649   1.00 32.40  ? 79  GLU A O   1 
ATOM   637  C CB  . GLU A 1 80 ? 11.839  -26.288 4.013   1.00 37.77  ? 79  GLU A CB  1 
ATOM   638  C CG  . GLU A 1 80 ? 13.131  -25.829 3.322   1.00 39.41  ? 79  GLU A CG  1 
ATOM   639  C CD  . GLU A 1 80 ? 13.740  -26.872 2.369   1.00 45.61  ? 79  GLU A CD  1 
ATOM   640  O OE1 . GLU A 1 80 ? 13.106  -27.922 2.158   1.00 53.22  ? 79  GLU A OE1 1 
ATOM   641  O OE2 . GLU A 1 80 ? 14.849  -26.671 1.841   1.00 46.75  ? 79  GLU A OE2 1 
ATOM   642  N N   . GLY A 1 81 ? 9.865   -23.862 4.072   1.00 34.23  ? 80  GLY A N   1 
ATOM   643  C CA  . GLY A 1 81 ? 9.524   -22.568 3.499   1.00 35.60  ? 80  GLY A CA  1 
ATOM   644  C C   . GLY A 1 81 ? 9.405   -21.445 4.529   1.00 32.25  ? 80  GLY A C   1 
ATOM   645  O O   . GLY A 1 81 ? 9.710   -20.289 4.216   1.00 34.70  ? 80  GLY A O   1 
ATOM   646  N N   . LEU A 1 82 ? 8.891   -21.748 5.739   1.00 31.88  ? 81  LEU A N   1 
ATOM   647  C CA  . LEU A 1 82 ? 8.907   -20.750 6.800   1.00 33.60  ? 81  LEU A CA  1 
ATOM   648  C C   . LEU A 1 82 ? 10.336  -20.303 7.096   1.00 34.49  ? 81  LEU A C   1 
ATOM   649  O O   . LEU A 1 82 ? 10.562  -19.120 7.378   1.00 33.08  ? 81  LEU A O   1 
ATOM   650  C CB  . LEU A 1 82 ? 8.259   -21.252 8.089   1.00 36.37  ? 81  LEU A CB  1 
ATOM   651  C CG  . LEU A 1 82 ? 6.767   -21.568 7.987   1.00 36.87  ? 81  LEU A CG  1 
ATOM   652  C CD1 . LEU A 1 82 ? 6.396   -22.164 9.329   1.00 37.26  ? 81  LEU A CD1 1 
ATOM   653  C CD2 . LEU A 1 82 ? 5.866   -20.346 7.685   1.00 35.69  ? 81  LEU A CD2 1 
ATOM   654  N N   . TRP A 1 83 ? 11.289  -21.259 7.047   1.00 33.96  ? 82  TRP A N   1 
ATOM   655  C CA  . TRP A 1 83 ? 12.657  -20.861 7.330   1.00 34.70  ? 82  TRP A CA  1 
ATOM   656  C C   . TRP A 1 83 ? 13.162  -19.927 6.233   1.00 31.79  ? 82  TRP A C   1 
ATOM   657  O O   . TRP A 1 83 ? 13.897  -18.976 6.498   1.00 34.10  ? 82  TRP A O   1 
ATOM   658  C CB  . TRP A 1 83 ? 13.605  -22.077 7.465   1.00 34.63  ? 82  TRP A CB  1 
ATOM   659  C CG  . TRP A 1 83 ? 15.042  -21.698 7.744   1.00 34.09  ? 82  TRP A CG  1 
ATOM   660  C CD1 . TRP A 1 83 ? 15.624  -21.554 8.971   1.00 36.59  ? 82  TRP A CD1 1 
ATOM   661  C CD2 . TRP A 1 83 ? 16.054  -21.372 6.764   1.00 32.51  ? 82  TRP A CD2 1 
ATOM   662  N NE1 . TRP A 1 83 ? 16.940  -21.198 8.821   1.00 37.75  ? 82  TRP A NE1 1 
ATOM   663  C CE2 . TRP A 1 83 ? 17.223  -21.070 7.482   1.00 35.44  ? 82  TRP A CE2 1 
ATOM   664  C CE3 . TRP A 1 83 ? 16.076  -21.332 5.356   1.00 36.78  ? 82  TRP A CE3 1 
ATOM   665  C CZ2 . TRP A 1 83 ? 18.400  -20.708 6.831   1.00 34.00  ? 82  TRP A CZ2 1 
ATOM   666  C CZ3 . TRP A 1 83 ? 17.231  -20.943 4.717   1.00 38.14  ? 82  TRP A CZ3 1 
ATOM   667  C CH2 . TRP A 1 83 ? 18.388  -20.660 5.460   1.00 36.33  ? 82  TRP A CH2 1 
ATOM   668  N N   . GLU A 1 84 ? 12.847  -20.260 4.977   1.00 29.34  ? 83  GLU A N   1 
ATOM   669  C CA  . GLU A 1 84 ? 13.379  -19.516 3.862   1.00 29.29  ? 83  GLU A CA  1 
ATOM   670  C C   . GLU A 1 84 ? 12.840  -18.086 3.875   1.00 33.49  ? 83  GLU A C   1 
ATOM   671  O O   . GLU A 1 84 ? 13.576  -17.136 3.727   1.00 30.43  ? 83  GLU A O   1 
ATOM   672  C CB  . GLU A 1 84 ? 12.954  -20.201 2.563   1.00 30.00  ? 83  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 84 ? 13.692  -21.538 2.416   1.00 32.05  ? 83  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 84 ? 13.330  -22.269 1.115   1.00 37.62  ? 83  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 84 ? 12.407  -21.833 0.409   1.00 34.40  ? 83  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 84 ? 13.930  -23.334 0.797   1.00 35.65  ? 83  GLU A OE2 1 
ATOM   677  N N   . ILE A 1 85 ? 11.552  -17.924 4.153   1.00 30.45  ? 84  ILE A N   1 
ATOM   678  C CA  . ILE A 1 85 ? 10.992  -16.587 4.009   1.00 31.88  ? 84  ILE A CA  1 
ATOM   679  C C   . ILE A 1 85 ? 11.553  -15.675 5.108   1.00 31.57  ? 84  ILE A C   1 
ATOM   680  O O   . ILE A 1 85 ? 11.690  -14.457 4.914   1.00 32.16  ? 84  ILE A O   1 
ATOM   681  C CB  . ILE A 1 85 ? 9.444   -16.624 4.014   1.00 29.05  ? 84  ILE A CB  1 
ATOM   682  C CG1 . ILE A 1 85 ? 8.901   -15.248 3.592   1.00 31.16  ? 84  ILE A CG1 1 
ATOM   683  C CG2 . ILE A 1 85 ? 8.911   -17.015 5.413   1.00 31.10  ? 84  ILE A CG2 1 
ATOM   684  C CD1 . ILE A 1 85 ? 7.465   -15.362 3.073   1.00 28.75  ? 84  ILE A CD1 1 
ATOM   685  N N   . GLN A 1 86 ? 11.880  -16.269 6.267   1.00 30.38  ? 85  GLN A N   1 
ATOM   686  C CA  . GLN A 1 86 ? 12.339  -15.477 7.414   1.00 32.84  ? 85  GLN A CA  1 
ATOM   687  C C   . GLN A 1 86 ? 13.849  -15.225 7.323   1.00 36.07  ? 85  GLN A C   1 
ATOM   688  O O   . GLN A 1 86 ? 14.317  -14.137 7.722   1.00 37.77  ? 85  GLN A O   1 
ATOM   689  C CB  . GLN A 1 86 ? 11.927  -16.206 8.710   1.00 35.67  ? 85  GLN A CB  1 
ATOM   690  C CG  . GLN A 1 86 ? 12.643  -15.732 9.971   1.00 41.80  ? 85  GLN A CG  1 
ATOM   691  C CD  . GLN A 1 86 ? 11.929  -16.151 11.251  1.00 48.97  ? 85  GLN A CD  1 
ATOM   692  O OE1 . GLN A 1 86 ? 11.525  -17.311 11.429  1.00 48.45  ? 85  GLN A OE1 1 
ATOM   693  N NE2 . GLN A 1 86 ? 11.734  -15.188 12.145  1.00 50.74  ? 85  GLN A NE2 1 
ATOM   694  N N   . ASN A 1 87 ? 14.599  -16.207 6.775   1.00 30.08  ? 86  ASN A N   1 
ATOM   695  C CA  . ASN A 1 87 ? 16.053  -16.202 6.871   1.00 31.80  ? 86  ASN A CA  1 
ATOM   696  C C   . ASN A 1 87 ? 16.786  -15.836 5.578   1.00 34.13  ? 86  ASN A C   1 
ATOM   697  O O   . ASN A 1 87 ? 17.879  -15.257 5.643   1.00 33.03  ? 86  ASN A O   1 
ATOM   698  C CB  . ASN A 1 87 ? 16.591  -17.482 7.502   1.00 31.11  ? 86  ASN A CB  1 
ATOM   699  C CG  . ASN A 1 87 ? 16.076  -17.570 8.924   1.00 34.66  ? 86  ASN A CG  1 
ATOM   700  O OD1 . ASN A 1 87 ? 16.394  -16.702 9.746   1.00 37.97  ? 86  ASN A OD1 1 
ATOM   701  N ND2 . ASN A 1 87 ? 15.111  -18.443 9.170   1.00 32.59  ? 86  ASN A ND2 1 
ATOM   702  N N   . ASN A 1 88 ? 16.267  -16.228 4.410   1.00 33.04  ? 87  ASN A N   1 
ATOM   703  C CA  . ASN A 1 88 ? 16.913  -15.812 3.182   1.00 29.29  ? 87  ASN A CA  1 
ATOM   704  C C   . ASN A 1 88 ? 15.886  -15.734 2.047   1.00 29.32  ? 87  ASN A C   1 
ATOM   705  O O   . ASN A 1 88 ? 15.946  -16.480 1.056   1.00 32.11  ? 87  ASN A O   1 
ATOM   706  C CB  . ASN A 1 88 ? 18.066  -16.747 2.782   1.00 30.16  ? 87  ASN A CB  1 
ATOM   707  C CG  . ASN A 1 88 ? 19.127  -16.094 1.919   1.00 36.16  ? 87  ASN A CG  1 
ATOM   708  O OD1 . ASN A 1 88 ? 18.890  -15.098 1.222   1.00 31.74  ? 87  ASN A OD1 1 
ATOM   709  N ND2 . ASN A 1 88 ? 20.313  -16.707 1.869   1.00 36.10  ? 87  ASN A ND2 1 
ATOM   710  N N   . PRO A 1 89 ? 14.904  -14.802 2.153   1.00 29.24  ? 88  PRO A N   1 
ATOM   711  C CA  . PRO A 1 89 ? 13.780  -14.815 1.206   1.00 26.68  ? 88  PRO A CA  1 
ATOM   712  C C   . PRO A 1 89 ? 14.135  -14.370 -0.210  1.00 31.46  ? 88  PRO A C   1 
ATOM   713  O O   . PRO A 1 89 ? 13.355  -14.578 -1.123  1.00 31.73  ? 88  PRO A O   1 
ATOM   714  C CB  . PRO A 1 89 ? 12.830  -13.832 1.901   1.00 30.06  ? 88  PRO A CB  1 
ATOM   715  C CG  . PRO A 1 89 ? 13.749  -12.834 2.569   1.00 28.69  ? 88  PRO A CG  1 
ATOM   716  C CD  . PRO A 1 89 ? 14.806  -13.769 3.191   1.00 28.44  ? 88  PRO A CD  1 
ATOM   717  N N   . HIS A 1 90 ? 15.321  -13.750 -0.400  1.00 28.44  ? 89  HIS A N   1 
ATOM   718  C CA  . HIS A 1 90 ? 15.703  -13.247 -1.721  1.00 29.35  ? 89  HIS A CA  1 
ATOM   719  C C   . HIS A 1 90 ? 16.815  -14.058 -2.391  1.00 31.34  ? 89  HIS A C   1 
ATOM   720  O O   . HIS A 1 90 ? 17.288  -13.683 -3.478  1.00 32.85  ? 89  HIS A O   1 
ATOM   721  C CB  . HIS A 1 90 ? 16.113  -11.763 -1.604  1.00 26.00  ? 89  HIS A CB  1 
ATOM   722  C CG  . HIS A 1 90 ? 15.014  -10.915 -1.048  1.00 30.20  ? 89  HIS A CG  1 
ATOM   723  N ND1 . HIS A 1 90 ? 13.772  -10.830 -1.642  1.00 29.56  ? 89  HIS A ND1 1 
ATOM   724  C CD2 . HIS A 1 90 ? 14.935  -10.226 0.102   1.00 28.96  ? 89  HIS A CD2 1 
ATOM   725  C CE1 . HIS A 1 90 ? 13.010  -10.006 -0.920  1.00 29.93  ? 89  HIS A CE1 1 
ATOM   726  N NE2 . HIS A 1 90 ? 13.676  -9.657  0.151   1.00 32.40  ? 89  HIS A NE2 1 
ATOM   727  N N   . ALA A 1 91 ? 17.106  -15.228 -1.820  1.00 30.47  ? 90  ALA A N   1 
ATOM   728  C CA  . ALA A 1 91 ? 18.129  -16.095 -2.388  1.00 29.41  ? 90  ALA A CA  1 
ATOM   729  C C   . ALA A 1 91 ? 17.674  -16.816 -3.653  1.00 36.51  ? 90  ALA A C   1 
ATOM   730  O O   . ALA A 1 91 ? 16.483  -16.976 -3.924  1.00 34.09  ? 90  ALA A O   1 
ATOM   731  C CB  . ALA A 1 91 ? 18.595  -17.071 -1.360  1.00 31.75  ? 90  ALA A CB  1 
ATOM   732  N N   . SER A 1 92 ? 18.670  -17.299 -4.406  1.00 33.95  ? 91  SER A N   1 
ATOM   733  C CA  . SER A 1 92 ? 18.426  -18.213 -5.505  1.00 39.38  ? 91  SER A CA  1 
ATOM   734  C C   . SER A 1 92 ? 18.170  -19.607 -4.941  1.00 42.52  ? 91  SER A C   1 
ATOM   735  O O   . SER A 1 92 ? 19.003  -20.139 -4.205  1.00 41.32  ? 91  SER A O   1 
ATOM   736  C CB  . SER A 1 92 ? 19.605  -18.199 -6.441  1.00 44.52  ? 91  SER A CB  1 
ATOM   737  O OG  . SER A 1 92 ? 19.476  -19.304 -7.310  1.00 45.36  ? 91  SER A OG  1 
ATOM   738  N N   . TYR A 1 93 ? 16.998  -20.176 -5.260  1.00 36.40  ? 92  TYR A N   1 
ATOM   739  C CA  . TYR A 1 93 ? 16.636  -21.511 -4.832  1.00 38.82  ? 92  TYR A CA  1 
ATOM   740  C C   . TYR A 1 93 ? 16.501  -22.430 -6.042  1.00 44.72  ? 92  TYR A C   1 
ATOM   741  O O   . TYR A 1 93 ? 15.843  -23.457 -5.951  1.00 51.01  ? 92  TYR A O   1 
ATOM   742  C CB  . TYR A 1 93 ? 15.300  -21.508 -4.082  1.00 35.15  ? 92  TYR A CB  1 
ATOM   743  C CG  . TYR A 1 93 ? 15.461  -20.929 -2.693  1.00 33.98  ? 92  TYR A CG  1 
ATOM   744  C CD1 . TYR A 1 93 ? 15.898  -21.709 -1.626  1.00 33.11  ? 92  TYR A CD1 1 
ATOM   745  C CD2 . TYR A 1 93 ? 15.176  -19.583 -2.453  1.00 33.57  ? 92  TYR A CD2 1 
ATOM   746  C CE1 . TYR A 1 93 ? 16.079  -21.154 -0.358  1.00 39.44  ? 92  TYR A CE1 1 
ATOM   747  C CE2 . TYR A 1 93 ? 15.302  -19.041 -1.190  1.00 32.73  ? 92  TYR A CE2 1 
ATOM   748  C CZ  . TYR A 1 93 ? 15.753  -19.819 -0.145  1.00 36.60  ? 92  TYR A CZ  1 
ATOM   749  O OH  . TYR A 1 93 ? 15.931  -19.247 1.075   1.00 34.89  ? 92  TYR A OH  1 
ATOM   750  N N   . SER A 1 94 ? 17.104  -22.040 -7.166  1.00 54.94  ? 93  SER A N   1 
ATOM   751  C CA  . SER A 1 94 ? 17.171  -22.925 -8.319  1.00 67.31  ? 93  SER A CA  1 
ATOM   752  C C   . SER A 1 94 ? 18.141  -24.074 -8.011  1.00 76.09  ? 93  SER A C   1 
ATOM   753  O O   . SER A 1 94 ? 19.316  -23.763 -7.712  1.00 72.26  ? 93  SER A O   1 
ATOM   754  C CB  . SER A 1 94 ? 17.563  -22.185 -9.573  1.00 67.91  ? 93  SER A CB  1 
ATOM   755  O OG  . SER A 1 94 ? 16.442  -21.485 -10.097 1.00 73.30  ? 93  SER A OG  1 
ATOM   756  O OXT . SER A 1 94 ? 17.679  -25.239 -8.061  1.00 90.86  ? 93  SER A OXT 1 
ATOM   757  N N   . MET B 1 2  ? 38.886  -11.367 -42.440 1.00 72.13  ? 1   MET B N   1 
ATOM   758  C CA  . MET B 1 2  ? 38.399  -12.248 -43.532 1.00 67.42  ? 1   MET B CA  1 
ATOM   759  C C   . MET B 1 2  ? 36.873  -12.301 -43.452 1.00 62.62  ? 1   MET B C   1 
ATOM   760  O O   . MET B 1 2  ? 36.316  -12.483 -42.369 1.00 68.97  ? 1   MET B O   1 
ATOM   761  C CB  . MET B 1 2  ? 39.035  -13.641 -43.415 1.00 73.75  ? 1   MET B CB  1 
ATOM   762  C CG  . MET B 1 2  ? 38.975  -14.525 -44.668 1.00 82.03  ? 1   MET B CG  1 
ATOM   763  S SD  . MET B 1 2  ? 39.994  -14.150 -46.115 1.00 81.63  ? 1   MET B SD  1 
ATOM   764  C CE  . MET B 1 2  ? 41.558  -13.579 -45.440 1.00 72.93  ? 1   MET B CE  1 
ATOM   765  N N   . PRO B 1 3  ? 36.145  -12.086 -44.576 1.00 53.81  ? 2   PRO B N   1 
ATOM   766  C CA  . PRO B 1 3  ? 34.685  -12.229 -44.586 1.00 59.36  ? 2   PRO B CA  1 
ATOM   767  C C   . PRO B 1 3  ? 34.350  -13.665 -44.189 1.00 61.49  ? 2   PRO B C   1 
ATOM   768  O O   . PRO B 1 3  ? 35.143  -14.556 -44.450 1.00 55.78  ? 2   PRO B O   1 
ATOM   769  C CB  . PRO B 1 3  ? 34.349  -11.936 -46.054 1.00 58.87  ? 2   PRO B CB  1 
ATOM   770  C CG  . PRO B 1 3  ? 35.453  -11.008 -46.492 1.00 53.95  ? 2   PRO B CG  1 
ATOM   771  C CD  . PRO B 1 3  ? 36.688  -11.629 -45.866 1.00 54.70  ? 2   PRO B CD  1 
ATOM   772  N N   . HIS B 1 4  ? 33.212  -13.873 -43.513 1.00 57.55  ? 3   HIS B N   1 
ATOM   773  C CA  . HIS B 1 4  ? 32.805  -15.224 -43.151 1.00 55.28  ? 3   HIS B CA  1 
ATOM   774  C C   . HIS B 1 4  ? 31.447  -15.536 -43.764 1.00 52.32  ? 3   HIS B C   1 
ATOM   775  O O   . HIS B 1 4  ? 30.859  -14.699 -44.448 1.00 47.25  ? 3   HIS B O   1 
ATOM   776  C CB  . HIS B 1 4  ? 32.896  -15.452 -41.638 1.00 59.02  ? 3   HIS B CB  1 
ATOM   777  C CG  . HIS B 1 4  ? 34.314  -15.526 -41.182 1.00 66.08  ? 3   HIS B CG  1 
ATOM   778  N ND1 . HIS B 1 4  ? 35.182  -16.490 -41.656 1.00 63.33  ? 3   HIS B ND1 1 
ATOM   779  C CD2 . HIS B 1 4  ? 35.037  -14.737 -40.370 1.00 62.59  ? 3   HIS B CD2 1 
ATOM   780  C CE1 . HIS B 1 4  ? 36.376  -16.301 -41.112 1.00 52.88  ? 3   HIS B CE1 1 
ATOM   781  N NE2 . HIS B 1 4  ? 36.309  -15.247 -40.330 1.00 65.35  ? 3   HIS B NE2 1 
ATOM   782  N N   . ALA B 1 5  ? 30.956  -16.758 -43.534 1.00 47.22  ? 4   ALA B N   1 
ATOM   783  C CA  . ALA B 1 5  ? 29.652  -17.102 -44.066 1.00 52.03  ? 4   ALA B CA  1 
ATOM   784  C C   . ALA B 1 5  ? 28.654  -16.058 -43.572 1.00 52.43  ? 4   ALA B C   1 
ATOM   785  O O   . ALA B 1 5  ? 27.822  -15.570 -44.336 1.00 51.71  ? 4   ALA B O   1 
ATOM   786  C CB  . ALA B 1 5  ? 29.268  -18.487 -43.608 1.00 49.83  ? 4   ALA B CB  1 
ATOM   787  N N   . PHE B 1 6  ? 28.758  -15.749 -42.275 1.00 54.47  ? 5   PHE B N   1 
ATOM   788  C CA  . PHE B 1 6  ? 27.966  -14.704 -41.643 1.00 53.21  ? 5   PHE B CA  1 
ATOM   789  C C   . PHE B 1 6  ? 28.856  -13.485 -41.388 1.00 45.54  ? 5   PHE B C   1 
ATOM   790  O O   . PHE B 1 6  ? 29.983  -13.600 -40.917 1.00 50.22  ? 5   PHE B O   1 
ATOM   791  C CB  . PHE B 1 6  ? 27.352  -15.139 -40.308 1.00 48.41  ? 5   PHE B CB  1 
ATOM   792  C CG  . PHE B 1 6  ? 26.297  -16.230 -40.415 1.00 48.43  ? 5   PHE B CG  1 
ATOM   793  C CD1 . PHE B 1 6  ? 24.963  -15.894 -40.604 1.00 39.68  ? 5   PHE B CD1 1 
ATOM   794  C CD2 . PHE B 1 6  ? 26.636  -17.577 -40.326 1.00 47.59  ? 5   PHE B CD2 1 
ATOM   795  C CE1 . PHE B 1 6  ? 23.985  -16.877 -40.716 1.00 43.46  ? 5   PHE B CE1 1 
ATOM   796  C CE2 . PHE B 1 6  ? 25.655  -18.561 -40.428 1.00 42.28  ? 5   PHE B CE2 1 
ATOM   797  C CZ  . PHE B 1 6  ? 24.329  -18.211 -40.598 1.00 40.86  ? 5   PHE B CZ  1 
ATOM   798  N N   . LYS B 1 7  ? 28.301  -12.312 -41.670 1.00 50.56  ? 6   LYS B N   1 
ATOM   799  C CA  . LYS B 1 7  ? 29.021  -11.064 -41.480 1.00 45.41  ? 6   LYS B CA  1 
ATOM   800  C C   . LYS B 1 7  ? 28.229  -10.191 -40.505 1.00 44.48  ? 6   LYS B C   1 
ATOM   801  O O   . LYS B 1 7  ? 26.993  -10.285 -40.456 1.00 43.26  ? 6   LYS B O   1 
ATOM   802  C CB  . LYS B 1 7  ? 29.131  -10.364 -42.836 1.00 53.63  ? 6   LYS B CB  1 
ATOM   803  C CG  . LYS B 1 7  ? 27.825  -9.925  -43.464 1.00 53.27  ? 6   LYS B CG  1 
ATOM   804  C CD  . LYS B 1 7  ? 28.024  -9.377  -44.877 1.00 63.79  ? 6   LYS B CD  1 
ATOM   805  C CE  . LYS B 1 7  ? 26.742  -9.167  -45.614 1.00 62.66  ? 6   LYS B CE  1 
ATOM   806  N NZ  . LYS B 1 7  ? 26.050  -10.448 -45.798 1.00 64.43  ? 6   LYS B NZ  1 
ATOM   807  N N   . PRO B 1 8  ? 28.906  -9.241  -39.818 1.00 50.79  ? 7   PRO B N   1 
ATOM   808  C CA  . PRO B 1 8  ? 28.254  -8.312  -38.885 1.00 43.93  ? 7   PRO B CA  1 
ATOM   809  C C   . PRO B 1 8  ? 27.097  -7.652  -39.595 1.00 43.75  ? 7   PRO B C   1 
ATOM   810  O O   . PRO B 1 8  ? 27.237  -7.264  -40.757 1.00 48.65  ? 7   PRO B O   1 
ATOM   811  C CB  . PRO B 1 8  ? 29.380  -7.313  -38.636 1.00 50.56  ? 7   PRO B CB  1 
ATOM   812  C CG  . PRO B 1 8  ? 30.623  -8.178  -38.683 1.00 56.03  ? 7   PRO B CG  1 
ATOM   813  C CD  . PRO B 1 8  ? 30.352  -8.970  -39.948 1.00 58.51  ? 7   PRO B CD  1 
ATOM   814  N N   . GLY B 1 9  ? 25.947  -7.604  -38.907 1.00 40.91  ? 8   GLY B N   1 
ATOM   815  C CA  . GLY B 1 9  ? 24.732  -6.977  -39.409 1.00 41.99  ? 8   GLY B CA  1 
ATOM   816  C C   . GLY B 1 9  ? 23.751  -7.958  -40.056 1.00 36.86  ? 8   GLY B C   1 
ATOM   817  O O   . GLY B 1 9  ? 22.622  -7.595  -40.339 1.00 37.86  ? 8   GLY B O   1 
ATOM   818  N N   . ASP B 1 10 ? 24.192  -9.195  -40.352 1.00 39.19  ? 9   ASP B N   1 
ATOM   819  C CA  . ASP B 1 10 ? 23.266  -10.190 -40.872 1.00 39.31  ? 9   ASP B CA  1 
ATOM   820  C C   . ASP B 1 10 ? 22.197  -10.516 -39.815 1.00 32.52  ? 9   ASP B C   1 
ATOM   821  O O   . ASP B 1 10 ? 22.485  -10.552 -38.620 1.00 36.98  ? 9   ASP B O   1 
ATOM   822  C CB  . ASP B 1 10 ? 23.972  -11.495 -41.193 1.00 40.37  ? 9   ASP B CB  1 
ATOM   823  C CG  . ASP B 1 10 ? 24.803  -11.556 -42.476 1.00 53.42  ? 9   ASP B CG  1 
ATOM   824  O OD1 . ASP B 1 10 ? 24.546  -10.727 -43.374 1.00 51.44  ? 9   ASP B OD1 1 
ATOM   825  O OD2 . ASP B 1 10 ? 25.713  -12.439 -42.555 1.00 47.23  ? 9   ASP B OD2 1 
ATOM   826  N N   . LEU B 1 11 ? 20.974  -10.715 -40.279 1.00 34.43  ? 10  LEU B N   1 
ATOM   827  C CA  . LEU B 1 11 ? 19.854  -10.926 -39.378 1.00 36.07  ? 10  LEU B CA  1 
ATOM   828  C C   . LEU B 1 11 ? 19.529  -12.409 -39.406 1.00 38.73  ? 10  LEU B C   1 
ATOM   829  O O   . LEU B 1 11 ? 19.588  -13.014 -40.476 1.00 40.03  ? 10  LEU B O   1 
ATOM   830  C CB  . LEU B 1 11 ? 18.641  -10.079 -39.754 1.00 36.97  ? 10  LEU B CB  1 
ATOM   831  C CG  . LEU B 1 11 ? 18.953  -8.574  -39.848 1.00 35.32  ? 10  LEU B CG  1 
ATOM   832  C CD1 . LEU B 1 11 ? 17.622  -7.904  -40.175 1.00 36.59  ? 10  LEU B CD1 1 
ATOM   833  C CD2 . LEU B 1 11 ? 19.605  -8.049  -38.568 1.00 34.79  ? 10  LEU B CD2 1 
ATOM   834  N N   . VAL B 1 12 ? 19.132  -12.944 -38.247 1.00 36.47  ? 11  VAL B N   1 
ATOM   835  C CA  . VAL B 1 12 ? 18.969  -14.390 -38.097 1.00 33.83  ? 11  VAL B CA  1 
ATOM   836  C C   . VAL B 1 12 ? 17.893  -14.644 -37.054 1.00 39.30  ? 11  VAL B C   1 
ATOM   837  O O   . VAL B 1 12 ? 17.494  -13.716 -36.332 1.00 35.76  ? 11  VAL B O   1 
ATOM   838  C CB  . VAL B 1 12 ? 20.257  -15.144 -37.684 1.00 36.40  ? 11  VAL B CB  1 
ATOM   839  C CG1 . VAL B 1 12 ? 21.388  -15.018 -38.718 1.00 36.12  ? 11  VAL B CG1 1 
ATOM   840  C CG2 . VAL B 1 12 ? 20.763  -14.789 -36.275 1.00 38.57  ? 11  VAL B CG2 1 
ATOM   841  N N   . PHE B 1 13 ? 17.441  -15.912 -37.015 1.00 35.13  ? 12  PHE B N   1 
ATOM   842  C CA  . PHE B 1 13 ? 16.936  -16.472 -35.768 1.00 32.82  ? 12  PHE B CA  1 
ATOM   843  C C   . PHE B 1 13 ? 18.033  -17.328 -35.167 1.00 34.96  ? 12  PHE B C   1 
ATOM   844  O O   . PHE B 1 13 ? 18.669  -18.094 -35.900 1.00 37.24  ? 12  PHE B O   1 
ATOM   845  C CB  . PHE B 1 13 ? 15.712  -17.321 -36.108 1.00 33.76  ? 12  PHE B CB  1 
ATOM   846  C CG  . PHE B 1 13 ? 14.515  -16.450 -36.433 1.00 38.39  ? 12  PHE B CG  1 
ATOM   847  C CD1 . PHE B 1 13 ? 14.218  -16.129 -37.760 1.00 34.65  ? 12  PHE B CD1 1 
ATOM   848  C CD2 . PHE B 1 13 ? 13.674  -16.010 -35.418 1.00 37.62  ? 12  PHE B CD2 1 
ATOM   849  C CE1 . PHE B 1 13 ? 13.114  -15.350 -38.048 1.00 41.83  ? 12  PHE B CE1 1 
ATOM   850  C CE2 . PHE B 1 13 ? 12.565  -15.230 -35.719 1.00 40.86  ? 12  PHE B CE2 1 
ATOM   851  C CZ  . PHE B 1 13 ? 12.291  -14.913 -37.040 1.00 44.22  ? 12  PHE B CZ  1 
ATOM   852  N N   . ALA B 1 14 ? 18.259  -17.176 -33.850 1.00 32.25  ? 13  ALA B N   1 
ATOM   853  C CA  . ALA B 1 14 ? 19.305  -17.894 -33.152 1.00 33.21  ? 13  ALA B CA  1 
ATOM   854  C C   . ALA B 1 14 ? 18.699  -18.844 -32.112 1.00 35.04  ? 13  ALA B C   1 
ATOM   855  O O   . ALA B 1 14 ? 17.768  -18.474 -31.399 1.00 36.24  ? 13  ALA B O   1 
ATOM   856  C CB  . ALA B 1 14 ? 20.264  -16.920 -32.499 1.00 33.45  ? 13  ALA B CB  1 
ATOM   857  N N   . LYS B 1 15 ? 19.251  -20.058 -32.042 1.00 34.20  ? 14  LYS B N   1 
ATOM   858  C CA  . LYS B 1 15 ? 18.643  -21.120 -31.242 1.00 36.37  ? 14  LYS B CA  1 
ATOM   859  C C   . LYS B 1 15 ? 19.523  -21.413 -30.034 1.00 36.66  ? 14  LYS B C   1 
ATOM   860  O O   . LYS B 1 15 ? 20.718  -21.690 -30.163 1.00 39.05  ? 14  LYS B O   1 
ATOM   861  C CB  . LYS B 1 15 ? 18.372  -22.384 -32.073 1.00 41.86  ? 14  LYS B CB  1 
ATOM   862  C CG  . LYS B 1 15 ? 17.683  -23.517 -31.272 1.00 37.26  ? 14  LYS B CG  1 
ATOM   863  C CD  . LYS B 1 15 ? 16.225  -23.174 -30.966 1.00 40.41  ? 14  LYS B CD  1 
ATOM   864  C CE  . LYS B 1 15 ? 15.386  -24.278 -30.286 1.00 37.47  ? 14  LYS B CE  1 
ATOM   865  N NZ  . LYS B 1 15 ? 15.890  -24.507 -28.933 1.00 38.49  ? 14  LYS B NZ  1 
ATOM   866  N N   . MET B 1 16 ? 18.914  -21.274 -28.852 1.00 37.14  ? 15  MET B N   1 
ATOM   867  C CA  . MET B 1 16 ? 19.515  -21.615 -27.570 1.00 41.30  ? 15  MET B CA  1 
ATOM   868  C C   . MET B 1 16 ? 18.673  -22.715 -26.918 1.00 43.49  ? 15  MET B C   1 
ATOM   869  O O   . MET B 1 16 ? 17.449  -22.690 -27.005 1.00 37.42  ? 15  MET B O   1 
ATOM   870  C CB  . MET B 1 16 ? 19.505  -20.405 -26.635 1.00 42.44  ? 15  MET B CB  1 
ATOM   871  C CG  . MET B 1 16 ? 20.289  -19.189 -27.120 1.00 47.16  ? 15  MET B CG  1 
ATOM   872  S SD  . MET B 1 16 ? 22.080  -19.200 -26.889 1.00 55.71  ? 15  MET B SD  1 
ATOM   873  C CE  . MET B 1 16 ? 22.195  -19.200 -25.093 1.00 52.77  ? 15  MET B CE  1 
ATOM   874  N N   . LYS B 1 17 ? 19.331  -23.681 -26.266 1.00 44.20  ? 16  LYS B N   1 
ATOM   875  C CA  . LYS B 1 17 ? 18.619  -24.718 -25.526 1.00 44.34  ? 16  LYS B CA  1 
ATOM   876  C C   . LYS B 1 17 ? 17.614  -24.060 -24.573 1.00 40.55  ? 16  LYS B C   1 
ATOM   877  O O   . LYS B 1 17 ? 17.947  -23.113 -23.872 1.00 42.56  ? 16  LYS B O   1 
ATOM   878  C CB  . LYS B 1 17 ? 19.670  -25.497 -24.720 1.00 51.96  ? 16  LYS B CB  1 
ATOM   879  C CG  . LYS B 1 17 ? 19.176  -26.758 -24.007 1.00 57.45  ? 16  LYS B CG  1 
ATOM   880  C CD  . LYS B 1 17 ? 20.097  -27.178 -22.863 1.00 54.65  ? 16  LYS B CD  1 
ATOM   881  N N   . GLY B 1 18 ? 16.371  -24.537 -24.613 1.00 44.11  ? 17  GLY B N   1 
ATOM   882  C CA  . GLY B 1 18 ? 15.325  -24.090 -23.705 1.00 47.06  ? 17  GLY B CA  1 
ATOM   883  C C   . GLY B 1 18 ? 14.529  -22.896 -24.240 1.00 45.61  ? 17  GLY B C   1 
ATOM   884  O O   . GLY B 1 18 ? 13.608  -22.447 -23.565 1.00 44.38  ? 17  GLY B O   1 
ATOM   885  N N   . TYR B 1 19 ? 14.871  -22.353 -25.432 1.00 40.33  ? 18  TYR B N   1 
ATOM   886  C CA  . TYR B 1 19 ? 14.116  -21.190 -25.913 1.00 35.17  ? 18  TYR B CA  1 
ATOM   887  C C   . TYR B 1 19 ? 13.690  -21.380 -27.373 1.00 34.07  ? 18  TYR B C   1 
ATOM   888  O O   . TYR B 1 19 ? 14.327  -22.138 -28.100 1.00 38.67  ? 18  TYR B O   1 
ATOM   889  C CB  . TYR B 1 19 ? 15.083  -19.996 -25.874 1.00 38.20  ? 18  TYR B CB  1 
ATOM   890  C CG  . TYR B 1 19 ? 15.576  -19.685 -24.463 1.00 43.34  ? 18  TYR B CG  1 
ATOM   891  C CD1 . TYR B 1 19 ? 14.828  -18.860 -23.626 1.00 39.91  ? 18  TYR B CD1 1 
ATOM   892  C CD2 . TYR B 1 19 ? 16.724  -20.281 -23.944 1.00 41.40  ? 18  TYR B CD2 1 
ATOM   893  C CE1 . TYR B 1 19 ? 15.243  -18.594 -22.327 1.00 41.26  ? 18  TYR B CE1 1 
ATOM   894  C CE2 . TYR B 1 19 ? 17.155  -20.008 -22.652 1.00 45.25  ? 18  TYR B CE2 1 
ATOM   895  C CZ  . TYR B 1 19 ? 16.403  -19.170 -21.846 1.00 43.44  ? 18  TYR B CZ  1 
ATOM   896  O OH  . TYR B 1 19 ? 16.806  -18.896 -20.573 1.00 48.69  ? 18  TYR B OH  1 
ATOM   897  N N   . PRO B 1 20 ? 12.677  -20.638 -27.885 1.00 36.97  ? 19  PRO B N   1 
ATOM   898  C CA  . PRO B 1 20 ? 12.300  -20.735 -29.301 1.00 35.31  ? 19  PRO B CA  1 
ATOM   899  C C   . PRO B 1 20 ? 13.368  -20.050 -30.147 1.00 33.01  ? 19  PRO B C   1 
ATOM   900  O O   . PRO B 1 20 ? 14.096  -19.236 -29.610 1.00 33.28  ? 19  PRO B O   1 
ATOM   901  C CB  . PRO B 1 20 ? 10.984  -20.002 -29.393 1.00 37.11  ? 19  PRO B CB  1 
ATOM   902  C CG  . PRO B 1 20 ? 11.004  -19.044 -28.201 1.00 38.51  ? 19  PRO B CG  1 
ATOM   903  C CD  . PRO B 1 20 ? 11.852  -19.691 -27.119 1.00 38.37  ? 19  PRO B CD  1 
ATOM   904  N N   . HIS B 1 21 ? 13.507  -20.441 -31.429 1.00 34.74  ? 20  HIS B N   1 
ATOM   905  C CA  . HIS B 1 21 ? 14.365  -19.697 -32.361 1.00 38.32  ? 20  HIS B CA  1 
ATOM   906  C C   . HIS B 1 21 ? 14.116  -18.194 -32.211 1.00 34.41  ? 20  HIS B C   1 
ATOM   907  O O   . HIS B 1 21 ? 12.977  -17.759 -32.229 1.00 34.33  ? 20  HIS B O   1 
ATOM   908  C CB  . HIS B 1 21 ? 14.048  -20.158 -33.797 1.00 33.43  ? 20  HIS B CB  1 
ATOM   909  C CG  . HIS B 1 21 ? 14.307  -21.625 -33.973 1.00 35.60  ? 20  HIS B CG  1 
ATOM   910  N ND1 . HIS B 1 21 ? 13.462  -22.640 -33.539 1.00 36.56  ? 20  HIS B ND1 1 
ATOM   911  C CD2 . HIS B 1 21 ? 15.355  -22.243 -34.530 1.00 35.05  ? 20  HIS B CD2 1 
ATOM   912  C CE1 . HIS B 1 21 ? 13.970  -23.815 -33.874 1.00 37.05  ? 20  HIS B CE1 1 
ATOM   913  N NE2 . HIS B 1 21 ? 15.126  -23.597 -34.460 1.00 35.72  ? 20  HIS B NE2 1 
ATOM   914  N N   . TRP B 1 22 ? 15.178  -17.397 -32.017 1.00 35.59  ? 21  TRP B N   1 
ATOM   915  C CA  . TRP B 1 22 ? 14.952  -16.077 -31.431 1.00 35.78  ? 21  TRP B CA  1 
ATOM   916  C C   . TRP B 1 22 ? 15.465  -14.996 -32.378 1.00 37.02  ? 21  TRP B C   1 
ATOM   917  O O   . TRP B 1 22 ? 16.575  -15.135 -32.844 1.00 33.56  ? 21  TRP B O   1 
ATOM   918  C CB  . TRP B 1 22 ? 15.720  -15.955 -30.105 1.00 36.07  ? 21  TRP B CB  1 
ATOM   919  C CG  . TRP B 1 22 ? 15.219  -14.808 -29.253 1.00 37.92  ? 21  TRP B CG  1 
ATOM   920  C CD1 . TRP B 1 22 ? 15.505  -13.468 -29.364 1.00 35.08  ? 21  TRP B CD1 1 
ATOM   921  C CD2 . TRP B 1 22 ? 14.297  -14.934 -28.142 1.00 37.45  ? 21  TRP B CD2 1 
ATOM   922  N NE1 . TRP B 1 22 ? 14.783  -12.753 -28.424 1.00 36.85  ? 21  TRP B NE1 1 
ATOM   923  C CE2 . TRP B 1 22 ? 14.046  -13.629 -27.656 1.00 34.40  ? 21  TRP B CE2 1 
ATOM   924  C CE3 . TRP B 1 22 ? 13.672  -16.033 -27.516 1.00 37.64  ? 21  TRP B CE3 1 
ATOM   925  C CZ2 . TRP B 1 22 ? 13.206  -13.378 -26.560 1.00 34.94  ? 21  TRP B CZ2 1 
ATOM   926  C CZ3 . TRP B 1 22 ? 12.873  -15.791 -26.417 1.00 35.69  ? 21  TRP B CZ3 1 
ATOM   927  C CH2 . TRP B 1 22 ? 12.588  -14.481 -25.990 1.00 34.41  ? 21  TRP B CH2 1 
ATOM   928  N N   . PRO B 1 23 ? 14.735  -13.886 -32.666 1.00 35.58  ? 22  PRO B N   1 
ATOM   929  C CA  . PRO B 1 23 ? 15.228  -12.882 -33.627 1.00 30.78  ? 22  PRO B CA  1 
ATOM   930  C C   . PRO B 1 23 ? 16.530  -12.290 -33.105 1.00 34.37  ? 22  PRO B C   1 
ATOM   931  O O   . PRO B 1 23 ? 16.628  -11.954 -31.928 1.00 35.81  ? 22  PRO B O   1 
ATOM   932  C CB  . PRO B 1 23 ? 14.061  -11.824 -33.686 1.00 32.36  ? 22  PRO B CB  1 
ATOM   933  C CG  . PRO B 1 23 ? 13.334  -12.015 -32.335 1.00 32.00  ? 22  PRO B CG  1 
ATOM   934  C CD  . PRO B 1 23 ? 13.429  -13.527 -32.093 1.00 33.13  ? 22  PRO B CD  1 
ATOM   935  N N   . ALA B 1 24 ? 17.557  -12.202 -33.959 1.00 32.17  ? 23  ALA B N   1 
ATOM   936  C CA  . ALA B 1 24 ? 18.876  -11.798 -33.504 1.00 32.53  ? 23  ALA B CA  1 
ATOM   937  C C   . ALA B 1 24 ? 19.704  -11.252 -34.662 1.00 31.87  ? 23  ALA B C   1 
ATOM   938  O O   . ALA B 1 24 ? 19.307  -11.319 -35.831 1.00 34.26  ? 23  ALA B O   1 
ATOM   939  C CB  . ALA B 1 24 ? 19.606  -12.936 -32.783 1.00 33.21  ? 23  ALA B CB  1 
ATOM   940  N N   . ARG B 1 25 ? 20.871  -10.712 -34.304 1.00 37.39  ? 24  ARG B N   1 
ATOM   941  C CA  . ARG B 1 25 ? 21.776  -10.252 -35.346 1.00 39.75  ? 24  ARG B CA  1 
ATOM   942  C C   . ARG B 1 25 ? 23.182  -10.745 -35.044 1.00 35.11  ? 24  ARG B C   1 
ATOM   943  O O   . ARG B 1 25 ? 23.522  -11.023 -33.902 1.00 36.18  ? 24  ARG B O   1 
ATOM   944  C CB  . ARG B 1 25 ? 21.784  -8.723  -35.446 1.00 38.21  ? 24  ARG B CB  1 
ATOM   945  C CG  . ARG B 1 25 ? 22.349  -8.036  -34.217 1.00 37.60  ? 24  ARG B CG  1 
ATOM   946  C CD  . ARG B 1 25 ? 22.198  -6.514  -34.392 1.00 34.33  ? 24  ARG B CD  1 
ATOM   947  N NE  . ARG B 1 25 ? 22.826  -5.827  -33.259 1.00 39.20  ? 24  ARG B NE  1 
ATOM   948  C CZ  . ARG B 1 25 ? 22.540  -4.566  -32.897 1.00 40.20  ? 24  ARG B CZ  1 
ATOM   949  N NH1 . ARG B 1 25 ? 21.555  -3.891  -33.503 1.00 38.58  ? 24  ARG B NH1 1 
ATOM   950  N NH2 . ARG B 1 25 ? 23.221  -4.019  -31.909 1.00 36.89  ? 24  ARG B NH2 1 
ATOM   951  N N   . ILE B 1 26 ? 24.002  -10.832 -36.097 1.00 36.83  ? 25  ILE B N   1 
ATOM   952  C CA  . ILE B 1 26 ? 25.425  -11.005 -35.906 1.00 35.49  ? 25  ILE B CA  1 
ATOM   953  C C   . ILE B 1 26 ? 25.997  -9.624  -35.580 1.00 44.04  ? 25  ILE B C   1 
ATOM   954  O O   . ILE B 1 26 ? 25.702  -8.666  -36.293 1.00 45.44  ? 25  ILE B O   1 
ATOM   955  C CB  . ILE B 1 26 ? 26.045  -11.476 -37.241 1.00 44.61  ? 25  ILE B CB  1 
ATOM   956  C CG1 . ILE B 1 26 ? 25.307  -12.662 -37.828 1.00 41.37  ? 25  ILE B CG1 1 
ATOM   957  C CG2 . ILE B 1 26 ? 27.558  -11.691 -37.145 1.00 43.50  ? 25  ILE B CG2 1 
ATOM   958  C CD1 . ILE B 1 26 ? 25.282  -13.874 -36.912 1.00 42.73  ? 25  ILE B CD1 1 
ATOM   959  N N   . ASP B 1 27 ? 26.856  -9.574  -34.559 1.00 39.04  ? 26  ASP B N   1 
ATOM   960  C CA  . ASP B 1 27 ? 27.483  -8.336  -34.102 1.00 51.80  ? 26  ASP B CA  1 
ATOM   961  C C   . ASP B 1 27 ? 28.959  -8.306  -34.511 1.00 53.27  ? 26  ASP B C   1 
ATOM   962  O O   . ASP B 1 27 ? 29.513  -9.344  -34.836 1.00 55.31  ? 26  ASP B O   1 
ATOM   963  C CB  . ASP B 1 27 ? 27.435  -8.256  -32.582 1.00 46.37  ? 26  ASP B CB  1 
ATOM   964  C CG  . ASP B 1 27 ? 26.264  -7.512  -31.960 1.00 50.76  ? 26  ASP B CG  1 
ATOM   965  O OD1 . ASP B 1 27 ? 25.426  -6.984  -32.721 1.00 46.53  ? 26  ASP B OD1 1 
ATOM   966  O OD2 . ASP B 1 27 ? 26.215  -7.445  -30.708 1.00 45.74  ? 26  ASP B OD2 1 
ATOM   967  N N   A ASP B 1 28 ? 29.578  -7.114  -34.477 0.50 59.83  ? 27  ASP B N   1 
ATOM   968  N N   B ASP B 1 28 ? 29.577  -7.114  -34.478 0.50 58.87  ? 27  ASP B N   1 
ATOM   969  C CA  A ASP B 1 28 ? 31.025  -6.973  -34.584 0.50 67.64  ? 27  ASP B CA  1 
ATOM   970  C CA  B ASP B 1 28 ? 31.024  -6.967  -34.580 0.50 65.77  ? 27  ASP B CA  1 
ATOM   971  C C   A ASP B 1 28 ? 31.659  -7.287  -33.228 0.50 68.70  ? 27  ASP B C   1 
ATOM   972  C C   B ASP B 1 28 ? 31.660  -7.273  -33.223 0.50 67.49  ? 27  ASP B C   1 
ATOM   973  O O   A ASP B 1 28 ? 30.957  -7.392  -32.223 0.50 72.45  ? 27  ASP B O   1 
ATOM   974  O O   B ASP B 1 28 ? 30.961  -7.361  -32.214 0.50 71.34  ? 27  ASP B O   1 
ATOM   975  C CB  A ASP B 1 28 ? 31.447  -5.577  -35.028 0.50 66.93  ? 27  ASP B CB  1 
ATOM   976  C CB  B ASP B 1 28 ? 31.437  -5.577  -35.048 0.50 62.63  ? 27  ASP B CB  1 
ATOM   977  C CG  A ASP B 1 28 ? 31.020  -5.140  -36.422 0.50 72.62  ? 27  ASP B CG  1 
ATOM   978  C CG  B ASP B 1 28 ? 31.352  -5.309  -36.544 0.50 66.52  ? 27  ASP B CG  1 
ATOM   979  O OD1 A ASP B 1 28 ? 31.857  -5.225  -37.351 0.50 69.81  ? 27  ASP B OD1 1 
ATOM   980  O OD1 B ASP B 1 28 ? 32.371  -5.529  -37.237 0.50 62.11  ? 27  ASP B OD1 1 
ATOM   981  O OD2 A ASP B 1 28 ? 29.872  -4.668  -36.560 0.50 78.31  ? 27  ASP B OD2 1 
ATOM   982  O OD2 B ASP B 1 28 ? 30.291  -4.830  -36.999 0.50 68.81  ? 27  ASP B OD2 1 
ATOM   983  N N   . ILE B 1 29 ? 32.992  -7.410  -33.203 1.00 71.90  ? 28  ILE B N   1 
ATOM   984  C CA  . ILE B 1 29 ? 33.716  -7.743  -31.979 1.00 77.92  ? 28  ILE B CA  1 
ATOM   985  C C   . ILE B 1 29 ? 33.890  -6.487  -31.102 1.00 82.30  ? 28  ILE B C   1 
ATOM   986  O O   . ILE B 1 29 ? 33.759  -5.367  -31.654 1.00 86.22  ? 28  ILE B O   1 
ATOM   987  C CB  . ILE B 1 29 ? 35.061  -8.433  -32.277 1.00 70.39  ? 28  ILE B CB  1 
ATOM   988  N N   . VAL B 1 34 ? 37.186  -9.915  -25.681 1.00 86.14  ? 33  VAL B N   1 
ATOM   989  C CA  . VAL B 1 34 ? 36.731  -11.335 -25.554 1.00 85.39  ? 33  VAL B CA  1 
ATOM   990  C C   . VAL B 1 34 ? 36.166  -11.785 -26.899 1.00 81.98  ? 33  VAL B C   1 
ATOM   991  O O   . VAL B 1 34 ? 34.973  -11.633 -27.170 1.00 77.79  ? 33  VAL B O   1 
ATOM   992  C CB  . VAL B 1 34 ? 35.739  -11.558 -24.392 1.00 88.07  ? 33  VAL B CB  1 
ATOM   993  C CG1 . VAL B 1 34 ? 34.585  -10.559 -24.411 1.00 92.84  ? 33  VAL B CG1 1 
ATOM   994  C CG2 . VAL B 1 34 ? 35.229  -12.998 -24.332 1.00 87.14  ? 33  VAL B CG2 1 
ATOM   995  N N   . LYS B 1 35 ? 37.054  -12.340 -27.733 1.00 79.30  ? 34  LYS B N   1 
ATOM   996  C CA  . LYS B 1 35 ? 36.707  -12.746 -29.086 1.00 74.47  ? 34  LYS B CA  1 
ATOM   997  C C   . LYS B 1 35 ? 35.851  -14.009 -29.022 1.00 69.21  ? 34  LYS B C   1 
ATOM   998  O O   . LYS B 1 35 ? 35.910  -14.754 -28.044 1.00 66.48  ? 34  LYS B O   1 
ATOM   999  C CB  . LYS B 1 35 ? 37.973  -12.900 -29.938 1.00 78.17  ? 34  LYS B CB  1 
ATOM   1000 N N   . PRO B 1 36 ? 34.996  -14.274 -30.037 1.00 62.86  ? 35  PRO B N   1 
ATOM   1001 C CA  . PRO B 1 36 ? 34.229  -15.521 -30.067 1.00 66.17  ? 35  PRO B CA  1 
ATOM   1002 C C   . PRO B 1 36 ? 35.155  -16.729 -29.960 1.00 60.97  ? 35  PRO B C   1 
ATOM   1003 O O   . PRO B 1 36 ? 36.298  -16.669 -30.405 1.00 65.69  ? 35  PRO B O   1 
ATOM   1004 C CB  . PRO B 1 36 ? 33.455  -15.514 -31.395 1.00 64.78  ? 35  PRO B CB  1 
ATOM   1005 C CG  . PRO B 1 36 ? 33.870  -14.239 -32.113 1.00 63.41  ? 35  PRO B CG  1 
ATOM   1006 C CD  . PRO B 1 36 ? 34.705  -13.383 -31.172 1.00 65.49  ? 35  PRO B CD  1 
ATOM   1007 N N   . PRO B 1 37 ? 34.714  -17.852 -29.351 1.00 59.97  ? 36  PRO B N   1 
ATOM   1008 C CA  . PRO B 1 37 ? 35.428  -19.115 -29.515 1.00 57.80  ? 36  PRO B CA  1 
ATOM   1009 C C   . PRO B 1 37 ? 35.528  -19.477 -30.999 1.00 63.89  ? 36  PRO B C   1 
ATOM   1010 O O   . PRO B 1 37 ? 34.742  -18.996 -31.820 1.00 57.64  ? 36  PRO B O   1 
ATOM   1011 C CB  . PRO B 1 37 ? 34.596  -20.133 -28.707 1.00 61.09  ? 36  PRO B CB  1 
ATOM   1012 C CG  . PRO B 1 37 ? 33.751  -19.290 -27.770 1.00 63.14  ? 36  PRO B CG  1 
ATOM   1013 C CD  . PRO B 1 37 ? 33.548  -17.957 -28.459 1.00 59.88  ? 36  PRO B CD  1 
ATOM   1014 N N   . PRO B 1 38 ? 36.502  -20.329 -31.402 1.00 65.43  ? 37  PRO B N   1 
ATOM   1015 C CA  . PRO B 1 38 ? 36.563  -20.843 -32.779 1.00 64.19  ? 37  PRO B CA  1 
ATOM   1016 C C   . PRO B 1 38 ? 35.220  -21.295 -33.357 1.00 55.14  ? 37  PRO B C   1 
ATOM   1017 O O   . PRO B 1 38 ? 34.492  -22.045 -32.716 1.00 58.46  ? 37  PRO B O   1 
ATOM   1018 C CB  . PRO B 1 38 ? 37.550  -22.032 -32.646 1.00 62.58  ? 37  PRO B CB  1 
ATOM   1019 C CG  . PRO B 1 38 ? 38.464  -21.645 -31.498 1.00 60.13  ? 37  PRO B CG  1 
ATOM   1020 C CD  . PRO B 1 38 ? 37.612  -20.809 -30.559 1.00 68.43  ? 37  PRO B CD  1 
ATOM   1021 N N   . ASN B 1 39 ? 34.910  -20.861 -34.585 1.00 55.01  ? 38  ASN B N   1 
ATOM   1022 C CA  . ASN B 1 39 ? 33.723  -21.314 -35.314 1.00 57.45  ? 38  ASN B CA  1 
ATOM   1023 C C   . ASN B 1 39 ? 32.437  -20.635 -34.828 1.00 50.47  ? 38  ASN B C   1 
ATOM   1024 O O   . ASN B 1 39 ? 31.356  -20.935 -35.323 1.00 48.01  ? 38  ASN B O   1 
ATOM   1025 C CB  . ASN B 1 39 ? 33.486  -22.821 -35.209 1.00 56.82  ? 38  ASN B CB  1 
ATOM   1026 C CG  . ASN B 1 39 ? 34.668  -23.665 -35.637 1.00 63.24  ? 38  ASN B CG  1 
ATOM   1027 O OD1 . ASN B 1 39 ? 34.988  -24.656 -34.973 1.00 62.50  ? 38  ASN B OD1 1 
ATOM   1028 N ND2 . ASN B 1 39 ? 35.302  -23.322 -36.752 1.00 62.54  ? 38  ASN B ND2 1 
ATOM   1029 N N   . LYS B 1 40 ? 32.537  -19.750 -33.830 1.00 55.50  ? 39  LYS B N   1 
ATOM   1030 C CA  . LYS B 1 40 ? 31.333  -19.146 -33.276 1.00 51.31  ? 39  LYS B CA  1 
ATOM   1031 C C   . LYS B 1 40 ? 31.305  -17.660 -33.587 1.00 46.77  ? 39  LYS B C   1 
ATOM   1032 O O   . LYS B 1 40 ? 32.347  -17.071 -33.870 1.00 49.60  ? 39  LYS B O   1 
ATOM   1033 C CB  . LYS B 1 40 ? 31.285  -19.410 -31.768 1.00 50.10  ? 39  LYS B CB  1 
ATOM   1034 C CG  . LYS B 1 40 ? 31.128  -20.884 -31.480 1.00 52.95  ? 39  LYS B CG  1 
ATOM   1035 C CD  . LYS B 1 40 ? 30.764  -21.193 -30.033 1.00 56.37  ? 39  LYS B CD  1 
ATOM   1036 C CE  . LYS B 1 40 ? 30.422  -22.636 -29.921 1.00 63.12  ? 39  LYS B CE  1 
ATOM   1037 N NZ  . LYS B 1 40 ? 31.379  -23.415 -30.708 1.00 72.54  ? 39  LYS B NZ  1 
ATOM   1038 N N   . TYR B 1 41 ? 30.104  -17.076 -33.501 1.00 46.12  ? 40  TYR B N   1 
ATOM   1039 C CA  . TYR B 1 41 ? 29.867  -15.663 -33.781 1.00 44.79  ? 40  TYR B CA  1 
ATOM   1040 C C   . TYR B 1 41 ? 29.257  -14.963 -32.570 1.00 45.76  ? 40  TYR B C   1 
ATOM   1041 O O   . TYR B 1 41 ? 28.475  -15.567 -31.836 1.00 42.12  ? 40  TYR B O   1 
ATOM   1042 C CB  . TYR B 1 41 ? 28.833  -15.517 -34.897 1.00 40.94  ? 40  TYR B CB  1 
ATOM   1043 C CG  . TYR B 1 41 ? 29.299  -15.970 -36.273 1.00 43.34  ? 40  TYR B CG  1 
ATOM   1044 C CD1 . TYR B 1 41 ? 30.083  -15.145 -37.088 1.00 42.64  ? 40  TYR B CD1 1 
ATOM   1045 C CD2 . TYR B 1 41 ? 28.952  -17.229 -36.747 1.00 41.97  ? 40  TYR B CD2 1 
ATOM   1046 C CE1 . TYR B 1 41 ? 30.508  -15.568 -38.343 1.00 46.97  ? 40  TYR B CE1 1 
ATOM   1047 C CE2 . TYR B 1 41 ? 29.366  -17.652 -38.002 1.00 46.63  ? 40  TYR B CE2 1 
ATOM   1048 C CZ  . TYR B 1 41 ? 30.144  -16.827 -38.801 1.00 48.62  ? 40  TYR B CZ  1 
ATOM   1049 O OH  . TYR B 1 41 ? 30.522  -17.291 -40.039 1.00 46.82  ? 40  TYR B OH  1 
ATOM   1050 N N   . PRO B 1 42 ? 29.551  -13.650 -32.370 1.00 47.32  ? 41  PRO B N   1 
ATOM   1051 C CA  . PRO B 1 42 ? 28.860  -12.841 -31.362 1.00 41.69  ? 41  PRO B CA  1 
ATOM   1052 C C   . PRO B 1 42 ? 27.436  -12.585 -31.842 1.00 39.87  ? 41  PRO B C   1 
ATOM   1053 O O   . PRO B 1 42 ? 27.227  -12.019 -32.919 1.00 39.85  ? 41  PRO B O   1 
ATOM   1054 C CB  . PRO B 1 42 ? 29.664  -11.531 -31.233 1.00 44.00  ? 41  PRO B CB  1 
ATOM   1055 C CG  . PRO B 1 42 ? 30.573  -11.503 -32.467 1.00 42.70  ? 41  PRO B CG  1 
ATOM   1056 C CD  . PRO B 1 42 ? 30.547  -12.873 -33.133 1.00 48.67  ? 41  PRO B CD  1 
ATOM   1057 N N   . ILE B 1 43 ? 26.468  -13.054 -31.039 1.00 39.53  ? 42  ILE B N   1 
ATOM   1058 C CA  . ILE B 1 43 ? 25.048  -12.888 -31.326 1.00 36.85  ? 42  ILE B CA  1 
ATOM   1059 C C   . ILE B 1 43 ? 24.453  -11.836 -30.389 1.00 35.76  ? 42  ILE B C   1 
ATOM   1060 O O   . ILE B 1 43 ? 24.781  -11.807 -29.218 1.00 41.17  ? 42  ILE B O   1 
ATOM   1061 C CB  . ILE B 1 43 ? 24.315  -14.232 -31.178 1.00 37.29  ? 42  ILE B CB  1 
ATOM   1062 C CG1 . ILE B 1 43 ? 25.070  -15.327 -31.952 1.00 40.00  ? 42  ILE B CG1 1 
ATOM   1063 C CG2 . ILE B 1 43 ? 22.848  -14.102 -31.623 1.00 38.31  ? 42  ILE B CG2 1 
ATOM   1064 C CD1 . ILE B 1 43 ? 25.239  -15.035 -33.428 1.00 40.31  ? 42  ILE B CD1 1 
ATOM   1065 N N   . PHE B 1 44 ? 23.608  -10.969 -30.941 1.00 37.86  ? 43  PHE B N   1 
ATOM   1066 C CA  . PHE B 1 44 ? 22.783  -10.094 -30.113 1.00 37.76  ? 43  PHE B CA  1 
ATOM   1067 C C   . PHE B 1 44 ? 21.326  -10.476 -30.311 1.00 35.03  ? 43  PHE B C   1 
ATOM   1068 O O   . PHE B 1 44 ? 20.830  -10.495 -31.435 1.00 36.53  ? 43  PHE B O   1 
ATOM   1069 C CB  . PHE B 1 44 ? 23.021  -8.633  -30.511 1.00 36.90  ? 43  PHE B CB  1 
ATOM   1070 C CG  . PHE B 1 44 ? 22.049  -7.626  -29.899 1.00 39.96  ? 43  PHE B CG  1 
ATOM   1071 C CD1 . PHE B 1 44 ? 20.868  -7.273  -30.550 1.00 40.36  ? 43  PHE B CD1 1 
ATOM   1072 C CD2 . PHE B 1 44 ? 22.333  -7.024  -28.678 1.00 42.99  ? 43  PHE B CD2 1 
ATOM   1073 C CE1 . PHE B 1 44 ? 19.997  -6.349  -29.995 1.00 42.35  ? 43  PHE B CE1 1 
ATOM   1074 C CE2 . PHE B 1 44 ? 21.459  -6.092  -28.128 1.00 39.87  ? 43  PHE B CE2 1 
ATOM   1075 C CZ  . PHE B 1 44 ? 20.293  -5.767  -28.778 1.00 46.64  ? 43  PHE B CZ  1 
ATOM   1076 N N   . PHE B 1 45 ? 20.622  -10.741 -29.201 1.00 34.62  ? 44  PHE B N   1 
ATOM   1077 C CA  . PHE B 1 45 ? 19.243  -11.163 -29.275 1.00 36.36  ? 44  PHE B CA  1 
ATOM   1078 C C   . PHE B 1 45 ? 18.365  -9.943  -29.087 1.00 34.29  ? 44  PHE B C   1 
ATOM   1079 O O   . PHE B 1 45 ? 18.478  -9.233  -28.088 1.00 38.57  ? 44  PHE B O   1 
ATOM   1080 C CB  . PHE B 1 45 ? 19.013  -12.108 -28.085 1.00 36.26  ? 44  PHE B CB  1 
ATOM   1081 C CG  . PHE B 1 45 ? 19.745  -13.440 -28.224 1.00 33.56  ? 44  PHE B CG  1 
ATOM   1082 C CD1 . PHE B 1 45 ? 21.049  -13.606 -27.790 1.00 39.75  ? 44  PHE B CD1 1 
ATOM   1083 C CD2 . PHE B 1 45 ? 19.127  -14.503 -28.893 1.00 34.94  ? 44  PHE B CD2 1 
ATOM   1084 C CE1 . PHE B 1 45 ? 21.703  -14.820 -27.962 1.00 44.41  ? 44  PHE B CE1 1 
ATOM   1085 C CE2 . PHE B 1 45 ? 19.774  -15.722 -29.029 1.00 36.67  ? 44  PHE B CE2 1 
ATOM   1086 C CZ  . PHE B 1 45 ? 21.057  -15.877 -28.587 1.00 36.98  ? 44  PHE B CZ  1 
ATOM   1087 N N   . PHE B 1 46 ? 17.497  -9.715  -30.065 1.00 32.10  ? 45  PHE B N   1 
ATOM   1088 C CA  . PHE B 1 46 ? 16.612  -8.573  -30.009 1.00 33.02  ? 45  PHE B CA  1 
ATOM   1089 C C   . PHE B 1 46 ? 15.626  -8.775  -28.851 1.00 35.94  ? 45  PHE B C   1 
ATOM   1090 O O   . PHE B 1 46 ? 15.299  -9.908  -28.455 1.00 36.83  ? 45  PHE B O   1 
ATOM   1091 C CB  . PHE B 1 46 ? 15.864  -8.359  -31.320 1.00 31.46  ? 45  PHE B CB  1 
ATOM   1092 C CG  . PHE B 1 46 ? 16.751  -7.909  -32.470 1.00 37.08  ? 45  PHE B CG  1 
ATOM   1093 C CD1 . PHE B 1 46 ? 17.294  -6.612  -32.484 1.00 39.32  ? 45  PHE B CD1 1 
ATOM   1094 C CD2 . PHE B 1 46 ? 17.040  -8.779  -33.519 1.00 35.11  ? 45  PHE B CD2 1 
ATOM   1095 C CE1 . PHE B 1 46 ? 18.132  -6.207  -33.532 1.00 34.94  ? 45  PHE B CE1 1 
ATOM   1096 C CE2 . PHE B 1 46 ? 17.851  -8.369  -34.580 1.00 34.84  ? 45  PHE B CE2 1 
ATOM   1097 C CZ  . PHE B 1 46 ? 18.365  -7.074  -34.586 1.00 35.76  ? 45  PHE B CZ  1 
ATOM   1098 N N   . GLY B 1 47 ? 15.129  -7.655  -28.339 1.00 36.71  ? 46  GLY B N   1 
ATOM   1099 C CA  . GLY B 1 47 ? 14.078  -7.712  -27.332 1.00 38.06  ? 46  GLY B CA  1 
ATOM   1100 C C   . GLY B 1 47 ? 14.694  -7.836  -25.943 1.00 37.65  ? 46  GLY B C   1 
ATOM   1101 O O   . GLY B 1 47 ? 14.536  -6.948  -25.102 1.00 41.23  ? 46  GLY B O   1 
ATOM   1102 N N   . THR B 1 48 ? 15.452  -8.913  -25.718 1.00 39.20  ? 47  THR B N   1 
ATOM   1103 C CA  . THR B 1 48 ? 16.098  -9.131  -24.434 1.00 43.18  ? 47  THR B CA  1 
ATOM   1104 C C   . THR B 1 48 ? 17.384  -8.320  -24.360 1.00 42.39  ? 47  THR B C   1 
ATOM   1105 O O   . THR B 1 48 ? 17.850  -7.988  -23.268 1.00 41.98  ? 47  THR B O   1 
ATOM   1106 C CB  . THR B 1 48 ? 16.353  -10.619 -24.134 1.00 42.86  ? 47  THR B CB  1 
ATOM   1107 O OG1 . THR B 1 48 ? 17.405  -11.158 -24.946 1.00 39.01  ? 47  THR B OG1 1 
ATOM   1108 C CG2 . THR B 1 48 ? 15.060  -11.431 -24.107 1.00 39.09  ? 47  THR B CG2 1 
ATOM   1109 N N   . HIS B 1 49 ? 17.983  -8.103  -25.535 1.00 40.22  ? 48  HIS B N   1 
ATOM   1110 C CA  . HIS B 1 49 ? 19.262  -7.428  -25.680 1.00 43.60  ? 48  HIS B CA  1 
ATOM   1111 C C   . HIS B 1 49 ? 20.359  -8.229  -24.991 1.00 42.42  ? 48  HIS B C   1 
ATOM   1112 O O   . HIS B 1 49 ? 21.378  -7.673  -24.582 1.00 47.71  ? 48  HIS B O   1 
ATOM   1113 C CB  . HIS B 1 49 ? 19.182  -5.956  -25.252 1.00 39.26  ? 48  HIS B CB  1 
ATOM   1114 C CG  . HIS B 1 49 ? 17.989  -5.248  -25.805 1.00 42.51  ? 48  HIS B CG  1 
ATOM   1115 N ND1 . HIS B 1 49 ? 17.298  -4.326  -25.056 1.00 44.81  ? 48  HIS B ND1 1 
ATOM   1116 C CD2 . HIS B 1 49 ? 17.347  -5.312  -26.985 1.00 38.94  ? 48  HIS B CD2 1 
ATOM   1117 C CE1 . HIS B 1 49 ? 16.269  -3.868  -25.762 1.00 50.49  ? 48  HIS B CE1 1 
ATOM   1118 N NE2 . HIS B 1 49 ? 16.282  -4.458  -26.943 1.00 47.76  ? 48  HIS B NE2 1 
ATOM   1119 N N   . GLU B 1 50 ? 20.163  -9.543  -24.858 1.00 40.71  ? 49  GLU B N   1 
ATOM   1120 C CA  . GLU B 1 50 ? 21.229  -10.367 -24.316 1.00 40.57  ? 49  GLU B CA  1 
ATOM   1121 C C   . GLU B 1 50 ? 22.191  -10.718 -25.462 1.00 41.44  ? 49  GLU B C   1 
ATOM   1122 O O   . GLU B 1 50 ? 21.881  -10.496 -26.648 1.00 39.68  ? 49  GLU B O   1 
ATOM   1123 C CB  . GLU B 1 50 ? 20.658  -11.664 -23.738 1.00 50.04  ? 49  GLU B CB  1 
ATOM   1124 C CG  . GLU B 1 50 ? 19.676  -11.442 -22.586 1.00 44.55  ? 49  GLU B CG  1 
ATOM   1125 C CD  . GLU B 1 50 ? 19.041  -12.765 -22.168 1.00 57.82  ? 49  GLU B CD  1 
ATOM   1126 O OE1 . GLU B 1 50 ? 18.226  -13.316 -22.947 1.00 61.14  ? 49  GLU B OE1 1 
ATOM   1127 O OE2 . GLU B 1 50 ? 19.367  -13.264 -21.067 1.00 62.70  ? 49  GLU B OE2 1 
ATOM   1128 N N   . THR B 1 51 ? 23.337  -11.286 -25.081 1.00 40.58  ? 50  THR B N   1 
ATOM   1129 C CA  . THR B 1 51 ? 24.360  -11.718 -26.029 1.00 41.61  ? 50  THR B CA  1 
ATOM   1130 C C   . THR B 1 51 ? 24.769  -13.155 -25.708 1.00 45.15  ? 50  THR B C   1 
ATOM   1131 O O   . THR B 1 51 ? 24.596  -13.632 -24.588 1.00 46.62  ? 50  THR B O   1 
ATOM   1132 C CB  . THR B 1 51 ? 25.555  -10.752 -26.059 1.00 46.93  ? 50  THR B CB  1 
ATOM   1133 O OG1 . THR B 1 51 ? 26.025  -10.647 -24.723 1.00 45.62  ? 50  THR B OG1 1 
ATOM   1134 C CG2 . THR B 1 51 ? 25.171  -9.331  -26.435 1.00 43.06  ? 50  THR B CG2 1 
ATOM   1135 N N   . ALA B 1 52 ? 25.282  -13.858 -26.731 1.00 44.33  ? 51  ALA B N   1 
ATOM   1136 C CA  . ALA B 1 52 ? 25.971  -15.126 -26.563 1.00 43.22  ? 51  ALA B CA  1 
ATOM   1137 C C   . ALA B 1 52 ? 26.842  -15.383 -27.788 1.00 43.54  ? 51  ALA B C   1 
ATOM   1138 O O   . ALA B 1 52 ? 26.809  -14.610 -28.754 1.00 41.74  ? 51  ALA B O   1 
ATOM   1139 C CB  . ALA B 1 52 ? 24.998  -16.271 -26.295 1.00 42.42  ? 51  ALA B CB  1 
ATOM   1140 N N   . PHE B 1 53 ? 27.641  -16.455 -27.714 1.00 45.02  ? 52  PHE B N   1 
ATOM   1141 C CA  . PHE B 1 53 ? 28.380  -16.939 -28.868 1.00 44.23  ? 52  PHE B CA  1 
ATOM   1142 C C   . PHE B 1 53 ? 27.728  -18.225 -29.385 1.00 40.16  ? 52  PHE B C   1 
ATOM   1143 O O   . PHE B 1 53 ? 27.559  -19.177 -28.628 1.00 42.46  ? 52  PHE B O   1 
ATOM   1144 C CB  . PHE B 1 53 ? 29.817  -17.186 -28.404 1.00 46.52  ? 52  PHE B CB  1 
ATOM   1145 C CG  . PHE B 1 53 ? 30.613  -15.953 -27.991 1.00 47.45  ? 52  PHE B CG  1 
ATOM   1146 C CD1 . PHE B 1 53 ? 30.912  -14.958 -28.916 1.00 51.49  ? 52  PHE B CD1 1 
ATOM   1147 C CD2 . PHE B 1 53 ? 31.099  -15.818 -26.694 1.00 52.76  ? 52  PHE B CD2 1 
ATOM   1148 C CE1 . PHE B 1 53 ? 31.652  -13.840 -28.557 1.00 48.80  ? 52  PHE B CE1 1 
ATOM   1149 C CE2 . PHE B 1 53 ? 31.846  -14.701 -26.335 1.00 53.46  ? 52  PHE B CE2 1 
ATOM   1150 C CZ  . PHE B 1 53 ? 32.118  -13.724 -27.264 1.00 49.56  ? 52  PHE B CZ  1 
ATOM   1151 N N   . LEU B 1 54 ? 27.354  -18.249 -30.675 1.00 42.03  ? 53  LEU B N   1 
ATOM   1152 C CA  . LEU B 1 54 ? 26.719  -19.419 -31.272 1.00 38.67  ? 53  LEU B CA  1 
ATOM   1153 C C   . LEU B 1 54 ? 27.476  -19.810 -32.544 1.00 39.99  ? 53  LEU B C   1 
ATOM   1154 O O   . LEU B 1 54 ? 28.044  -18.947 -33.233 1.00 39.64  ? 53  LEU B O   1 
ATOM   1155 C CB  . LEU B 1 54 ? 25.241  -19.207 -31.617 1.00 38.71  ? 53  LEU B CB  1 
ATOM   1156 C CG  . LEU B 1 54 ? 24.278  -19.044 -30.438 1.00 39.97  ? 53  LEU B CG  1 
ATOM   1157 C CD1 . LEU B 1 54 ? 22.900  -18.625 -30.923 1.00 40.22  ? 53  LEU B CD1 1 
ATOM   1158 C CD2 . LEU B 1 54 ? 24.201  -20.389 -29.710 1.00 44.66  ? 53  LEU B CD2 1 
ATOM   1159 N N   . GLY B 1 55 ? 27.422  -21.114 -32.842 1.00 40.34  ? 54  GLY B N   1 
ATOM   1160 C CA  . GLY B 1 55 ? 27.938  -21.694 -34.069 1.00 38.51  ? 54  GLY B CA  1 
ATOM   1161 C C   . GLY B 1 55 ? 26.863  -21.697 -35.148 1.00 40.91  ? 54  GLY B C   1 
ATOM   1162 O O   . GLY B 1 55 ? 25.668  -21.551 -34.858 1.00 38.29  ? 54  GLY B O   1 
ATOM   1163 N N   . PRO B 1 56 ? 27.241  -21.872 -36.436 1.00 40.40  ? 55  PRO B N   1 
ATOM   1164 C CA  . PRO B 1 56 ? 26.267  -21.899 -37.515 1.00 38.31  ? 55  PRO B CA  1 
ATOM   1165 C C   . PRO B 1 56 ? 25.091  -22.849 -37.378 1.00 36.86  ? 55  PRO B C   1 
ATOM   1166 O O   . PRO B 1 56 ? 24.041  -22.575 -37.923 1.00 36.18  ? 55  PRO B O   1 
ATOM   1167 C CB  . PRO B 1 56 ? 27.091  -22.207 -38.787 1.00 43.99  ? 55  PRO B CB  1 
ATOM   1168 C CG  . PRO B 1 56 ? 28.527  -21.955 -38.406 1.00 44.61  ? 55  PRO B CG  1 
ATOM   1169 C CD  . PRO B 1 56 ? 28.627  -22.060 -36.911 1.00 45.21  ? 55  PRO B CD  1 
ATOM   1170 N N   . LYS B 1 57 ? 25.263  -23.985 -36.701 1.00 38.46  ? 56  LYS B N   1 
ATOM   1171 C CA  . LYS B 1 57 ? 24.150  -24.930 -36.615 1.00 39.42  ? 56  LYS B CA  1 
ATOM   1172 C C   . LYS B 1 57 ? 22.929  -24.288 -35.951 1.00 39.28  ? 56  LYS B C   1 
ATOM   1173 O O   . LYS B 1 57 ? 21.795  -24.752 -36.149 1.00 36.58  ? 56  LYS B O   1 
ATOM   1174 C CB  . LYS B 1 57 ? 24.595  -26.200 -35.868 1.00 44.63  ? 56  LYS B CB  1 
ATOM   1175 C CG  . LYS B 1 57 ? 24.833  -26.045 -34.364 1.00 46.94  ? 56  LYS B CG  1 
ATOM   1176 C CD  . LYS B 1 57 ? 25.034  -27.391 -33.667 1.00 55.36  ? 56  LYS B CD  1 
ATOM   1177 C CE  . LYS B 1 57 ? 25.176  -27.337 -32.160 1.00 53.16  ? 56  LYS B CE  1 
ATOM   1178 N NZ  . LYS B 1 57 ? 23.966  -26.899 -31.453 1.00 52.11  ? 56  LYS B NZ  1 
ATOM   1179 N N   . ASP B 1 58 ? 23.170  -23.205 -35.197 1.00 34.45  ? 57  ASP B N   1 
ATOM   1180 C CA  . ASP B 1 58 ? 22.144  -22.597 -34.369 1.00 35.80  ? 57  ASP B CA  1 
ATOM   1181 C C   . ASP B 1 58 ? 21.708  -21.271 -34.971 1.00 34.48  ? 57  ASP B C   1 
ATOM   1182 O O   . ASP B 1 58 ? 20.934  -20.549 -34.330 1.00 36.55  ? 57  ASP B O   1 
ATOM   1183 C CB  . ASP B 1 58 ? 22.581  -22.505 -32.908 1.00 38.91  ? 57  ASP B CB  1 
ATOM   1184 C CG  . ASP B 1 58 ? 22.763  -23.848 -32.205 1.00 47.45  ? 57  ASP B CG  1 
ATOM   1185 O OD1 . ASP B 1 58 ? 21.853  -24.697 -32.348 1.00 39.86  ? 57  ASP B OD1 1 
ATOM   1186 O OD2 . ASP B 1 58 ? 23.783  -24.011 -31.490 1.00 47.68  ? 57  ASP B OD2 1 
ATOM   1187 N N   . LEU B 1 59 ? 22.209  -20.976 -36.188 1.00 37.63  ? 58  LEU B N   1 
ATOM   1188 C CA  . LEU B 1 59 ? 21.982  -19.680 -36.809 1.00 35.63  ? 58  LEU B CA  1 
ATOM   1189 C C   . LEU B 1 59 ? 21.182  -19.845 -38.099 1.00 33.21  ? 58  LEU B C   1 
ATOM   1190 O O   . LEU B 1 59 ? 21.615  -20.555 -39.009 1.00 37.15  ? 58  LEU B O   1 
ATOM   1191 C CB  . LEU B 1 59 ? 23.308  -18.957 -37.013 1.00 36.42  ? 58  LEU B CB  1 
ATOM   1192 C CG  . LEU B 1 59 ? 24.105  -18.659 -35.740 1.00 32.25  ? 58  LEU B CG  1 
ATOM   1193 C CD1 . LEU B 1 59 ? 25.319  -17.891 -36.155 1.00 36.66  ? 58  LEU B CD1 1 
ATOM   1194 C CD2 . LEU B 1 59 ? 23.305  -17.843 -34.674 1.00 34.34  ? 58  LEU B CD2 1 
ATOM   1195 N N   . PHE B 1 60 ? 20.002  -19.214 -38.148 1.00 32.43  ? 59  PHE B N   1 
ATOM   1196 C CA  . PHE B 1 60 ? 19.032  -19.396 -39.220 1.00 34.99  ? 59  PHE B CA  1 
ATOM   1197 C C   . PHE B 1 60 ? 18.842  -18.047 -39.931 1.00 37.30  ? 59  PHE B C   1 
ATOM   1198 O O   . PHE B 1 60 ? 18.203  -17.128 -39.397 1.00 34.28  ? 59  PHE B O   1 
ATOM   1199 C CB  . PHE B 1 60 ? 17.688  -19.978 -38.746 1.00 32.53  ? 59  PHE B CB  1 
ATOM   1200 C CG  . PHE B 1 60 ? 17.769  -21.386 -38.139 1.00 33.36  ? 59  PHE B CG  1 
ATOM   1201 C CD1 . PHE B 1 60 ? 18.353  -21.576 -36.884 1.00 33.58  ? 59  PHE B CD1 1 
ATOM   1202 C CD2 . PHE B 1 60 ? 17.299  -22.490 -38.845 1.00 39.31  ? 59  PHE B CD2 1 
ATOM   1203 C CE1 . PHE B 1 60 ? 18.478  -22.859 -36.338 1.00 37.41  ? 59  PHE B CE1 1 
ATOM   1204 C CE2 . PHE B 1 60 ? 17.416  -23.771 -38.299 1.00 38.59  ? 59  PHE B CE2 1 
ATOM   1205 C CZ  . PHE B 1 60 ? 18.008  -23.950 -37.063 1.00 40.37  ? 59  PHE B CZ  1 
ATOM   1206 N N   . PRO B 1 61 ? 19.384  -17.869 -41.160 1.00 41.81  ? 60  PRO B N   1 
ATOM   1207 C CA  . PRO B 1 61 ? 19.174  -16.616 -41.905 1.00 39.24  ? 60  PRO B CA  1 
ATOM   1208 C C   . PRO B 1 61 ? 17.727  -16.114 -41.878 1.00 40.61  ? 60  PRO B C   1 
ATOM   1209 O O   . PRO B 1 61 ? 16.781  -16.861 -42.114 1.00 37.89  ? 60  PRO B O   1 
ATOM   1210 C CB  . PRO B 1 61 ? 19.722  -16.945 -43.332 1.00 37.38  ? 60  PRO B CB  1 
ATOM   1211 C CG  . PRO B 1 61 ? 20.798  -17.992 -43.065 1.00 46.38  ? 60  PRO B CG  1 
ATOM   1212 C CD  . PRO B 1 61 ? 20.265  -18.826 -41.868 1.00 40.81  ? 60  PRO B CD  1 
ATOM   1213 N N   . TYR B 1 62 ? 17.544  -14.818 -41.572 1.00 40.94  ? 61  TYR B N   1 
ATOM   1214 C CA  . TYR B 1 62 ? 16.242  -14.305 -41.185 1.00 42.24  ? 61  TYR B CA  1 
ATOM   1215 C C   . TYR B 1 62 ? 15.214  -14.333 -42.308 1.00 40.19  ? 61  TYR B C   1 
ATOM   1216 O O   . TYR B 1 62 ? 14.063  -14.720 -42.072 1.00 41.85  ? 61  TYR B O   1 
ATOM   1217 C CB  . TYR B 1 62 ? 16.421  -12.840 -40.773 1.00 43.03  ? 61  TYR B CB  1 
ATOM   1218 C CG  . TYR B 1 62 ? 15.097  -12.153 -40.491 1.00 43.91  ? 61  TYR B CG  1 
ATOM   1219 C CD1 . TYR B 1 62 ? 14.393  -12.392 -39.319 1.00 43.32  ? 61  TYR B CD1 1 
ATOM   1220 C CD2 . TYR B 1 62 ? 14.624  -11.182 -41.358 1.00 49.23  ? 61  TYR B CD2 1 
ATOM   1221 C CE1 . TYR B 1 62 ? 13.198  -11.739 -39.058 1.00 44.46  ? 61  TYR B CE1 1 
ATOM   1222 C CE2 . TYR B 1 62 ? 13.447  -10.503 -41.100 1.00 53.11  ? 61  TYR B CE2 1 
ATOM   1223 C CZ  . TYR B 1 62 ? 12.737  -10.785 -39.949 1.00 47.80  ? 61  TYR B CZ  1 
ATOM   1224 O OH  . TYR B 1 62 ? 11.584  -10.105 -39.731 1.00 47.73  ? 61  TYR B OH  1 
ATOM   1225 N N   . ASP B 1 63 ? 15.642  -13.920 -43.515 1.00 44.93  ? 62  ASP B N   1 
ATOM   1226 C CA  . ASP B 1 63 ? 14.812  -13.926 -44.719 1.00 45.92  ? 62  ASP B CA  1 
ATOM   1227 C C   . ASP B 1 63 ? 14.282  -15.325 -45.036 1.00 40.51  ? 62  ASP B C   1 
ATOM   1228 O O   . ASP B 1 63 ? 13.081  -15.508 -45.229 1.00 47.88  ? 62  ASP B O   1 
ATOM   1229 C CB  . ASP B 1 63 ? 15.541  -13.294 -45.893 1.00 52.31  ? 62  ASP B CB  1 
ATOM   1230 C CG  . ASP B 1 63 ? 15.375  -11.785 -46.030 1.00 67.68  ? 62  ASP B CG  1 
ATOM   1231 O OD1 . ASP B 1 63 ? 14.684  -11.181 -45.170 1.00 65.11  ? 62  ASP B OD1 1 
ATOM   1232 O OD2 . ASP B 1 63 ? 15.916  -11.221 -47.012 1.00 72.82  ? 62  ASP B OD2 1 
ATOM   1233 N N   . LYS B 1 64 ? 15.169  -16.320 -45.045 1.00 48.20  ? 63  LYS B N   1 
ATOM   1234 C CA  . LYS B 1 64 ? 14.738  -17.683 -45.292 1.00 50.08  ? 63  LYS B CA  1 
ATOM   1235 C C   . LYS B 1 64 ? 13.752  -18.171 -44.227 1.00 50.01  ? 63  LYS B C   1 
ATOM   1236 O O   . LYS B 1 64 ? 12.834  -18.924 -44.543 1.00 49.29  ? 63  LYS B O   1 
ATOM   1237 C CB  . LYS B 1 64 ? 15.926  -18.644 -45.310 1.00 51.04  ? 63  LYS B CB  1 
ATOM   1238 C CG  . LYS B 1 64 ? 15.542  -20.044 -45.733 1.00 51.06  ? 63  LYS B CG  1 
ATOM   1239 C CD  . LYS B 1 64 ? 16.725  -21.002 -45.660 1.00 57.50  ? 63  LYS B CD  1 
ATOM   1240 C CE  . LYS B 1 64 ? 16.609  -22.314 -46.421 1.00 51.94  ? 63  LYS B CE  1 
ATOM   1241 N NZ  . LYS B 1 64 ? 15.288  -22.939 -46.466 1.00 51.93  ? 63  LYS B NZ  1 
ATOM   1242 N N   . SER B 1 65 ? 13.927  -17.755 -42.968 1.00 44.96  ? 64  SER B N   1 
ATOM   1243 C CA  . SER B 1 65 ? 13.258  -18.499 -41.894 1.00 43.87  ? 64  SER B CA  1 
ATOM   1244 C C   . SER B 1 65 ? 12.145  -17.724 -41.182 1.00 46.30  ? 64  SER B C   1 
ATOM   1245 O O   . SER B 1 65 ? 11.516  -18.280 -40.286 1.00 46.16  ? 64  SER B O   1 
ATOM   1246 C CB  . SER B 1 65 ? 14.268  -19.013 -40.910 1.00 50.69  ? 64  SER B CB  1 
ATOM   1247 O OG  . SER B 1 65 ? 15.062  -17.946 -40.403 1.00 60.89  ? 64  SER B OG  1 
ATOM   1248 N N   . LYS B 1 66 ? 11.839  -16.485 -41.604 1.00 46.39  ? 65  LYS B N   1 
ATOM   1249 C CA  . LYS B 1 66 ? 10.953  -15.610 -40.831 1.00 45.14  ? 65  LYS B CA  1 
ATOM   1250 C C   . LYS B 1 66 ? 9.500   -16.084 -40.786 1.00 50.13  ? 65  LYS B C   1 
ATOM   1251 O O   . LYS B 1 66 ? 8.784   -15.833 -39.812 1.00 51.52  ? 65  LYS B O   1 
ATOM   1252 C CB  . LYS B 1 66 ? 11.028  -14.152 -41.304 1.00 48.44  ? 65  LYS B CB  1 
ATOM   1253 C CG  . LYS B 1 66 ? 10.590  -13.908 -42.747 1.00 49.71  ? 65  LYS B CG  1 
ATOM   1254 C CD  . LYS B 1 66 ? 10.728  -12.436 -43.136 1.00 62.17  ? 65  LYS B CD  1 
ATOM   1255 C CE  . LYS B 1 66 ? 10.620  -12.202 -44.614 1.00 63.34  ? 65  LYS B CE  1 
ATOM   1256 N NZ  . LYS B 1 66 ? 9.502   -12.928 -45.236 1.00 70.40  ? 65  LYS B NZ  1 
ATOM   1257 N N   . ASP B 1 67 ? 9.031   -16.750 -41.840 1.00 46.67  ? 66  ASP B N   1 
ATOM   1258 C CA  . ASP B 1 67 ? 7.639   -17.167 -41.840 1.00 50.26  ? 66  ASP B CA  1 
ATOM   1259 C C   . ASP B 1 67 ? 7.438   -18.327 -40.858 1.00 51.63  ? 66  ASP B C   1 
ATOM   1260 O O   . ASP B 1 67 ? 6.366   -18.486 -40.278 1.00 55.50  ? 66  ASP B O   1 
ATOM   1261 C CB  . ASP B 1 67 ? 7.143   -17.431 -43.254 1.00 64.12  ? 66  ASP B CB  1 
ATOM   1262 C CG  . ASP B 1 67 ? 7.734   -18.653 -43.941 1.00 79.73  ? 66  ASP B CG  1 
ATOM   1263 O OD1 . ASP B 1 67 ? 8.428   -18.468 -44.965 1.00 94.16  ? 66  ASP B OD1 1 
ATOM   1264 O OD2 . ASP B 1 67 ? 7.477   -19.782 -43.462 1.00 86.84  ? 66  ASP B OD2 1 
ATOM   1265 N N   . LYS B 1 68 ? 8.484   -19.131 -40.673 1.00 49.50  ? 67  LYS B N   1 
ATOM   1266 C CA  . LYS B 1 68 ? 8.436   -20.277 -39.788 1.00 43.62  ? 67  LYS B CA  1 
ATOM   1267 C C   . LYS B 1 68 ? 8.662   -19.864 -38.335 1.00 44.24  ? 67  LYS B C   1 
ATOM   1268 O O   . LYS B 1 68 ? 7.937   -20.341 -37.468 1.00 45.34  ? 67  LYS B O   1 
ATOM   1269 C CB  . LYS B 1 68 ? 9.467   -21.311 -40.243 1.00 44.42  ? 67  LYS B CB  1 
ATOM   1270 C CG  . LYS B 1 68 ? 9.529   -22.588 -39.416 1.00 48.00  ? 67  LYS B CG  1 
ATOM   1271 C CD  . LYS B 1 68 ? 10.543  -23.548 -40.027 1.00 58.29  ? 67  LYS B CD  1 
ATOM   1272 C CE  . LYS B 1 68 ? 10.701  -24.816 -39.234 1.00 65.76  ? 67  LYS B CE  1 
ATOM   1273 N NZ  . LYS B 1 68 ? 9.452   -25.583 -39.186 1.00 70.17  ? 67  LYS B NZ  1 
ATOM   1274 N N   . TYR B 1 69 ? 9.668   -19.006 -38.069 1.00 38.34  ? 68  TYR B N   1 
ATOM   1275 C CA  . TYR B 1 69 ? 10.072  -18.725 -36.688 1.00 35.62  ? 68  TYR B CA  1 
ATOM   1276 C C   . TYR B 1 69 ? 9.570   -17.354 -36.219 1.00 43.99  ? 68  TYR B C   1 
ATOM   1277 O O   . TYR B 1 69 ? 9.609   -17.071 -35.019 1.00 45.48  ? 68  TYR B O   1 
ATOM   1278 C CB  . TYR B 1 69 ? 11.585  -18.833 -36.491 1.00 39.45  ? 68  TYR B CB  1 
ATOM   1279 C CG  . TYR B 1 69 ? 12.202  -20.193 -36.800 1.00 41.69  ? 68  TYR B CG  1 
ATOM   1280 C CD1 . TYR B 1 69 ? 11.689  -21.358 -36.241 1.00 42.66  ? 68  TYR B CD1 1 
ATOM   1281 C CD2 . TYR B 1 69 ? 13.259  -20.313 -37.696 1.00 40.09  ? 68  TYR B CD2 1 
ATOM   1282 C CE1 . TYR B 1 69 ? 12.252  -22.595 -36.527 1.00 44.52  ? 68  TYR B CE1 1 
ATOM   1283 C CE2 . TYR B 1 69 ? 13.831  -21.544 -37.996 1.00 43.86  ? 68  TYR B CE2 1 
ATOM   1284 C CZ  . TYR B 1 69 ? 13.317  -22.686 -37.408 1.00 44.91  ? 68  TYR B CZ  1 
ATOM   1285 O OH  . TYR B 1 69 ? 13.840  -23.902 -37.707 1.00 45.63  ? 68  TYR B OH  1 
ATOM   1286 N N   . GLY B 1 70 ? 9.141   -16.489 -37.155 1.00 45.66  ? 69  GLY B N   1 
ATOM   1287 C CA  . GLY B 1 70 ? 8.855   -15.095 -36.822 1.00 50.54  ? 69  GLY B CA  1 
ATOM   1288 C C   . GLY B 1 70 ? 7.446   -14.875 -36.263 1.00 52.86  ? 69  GLY B C   1 
ATOM   1289 O O   . GLY B 1 70 ? 6.798   -13.875 -36.585 1.00 49.71  ? 69  GLY B O   1 
ATOM   1290 N N   . LYS B 1 71 ? 6.974   -15.809 -35.423 1.00 54.67  ? 70  LYS B N   1 
ATOM   1291 C CA  . LYS B 1 71 ? 5.610   -15.753 -34.916 1.00 54.64  ? 70  LYS B CA  1 
ATOM   1292 C C   . LYS B 1 71 ? 5.623   -15.354 -33.446 1.00 53.06  ? 70  LYS B C   1 
ATOM   1293 O O   . LYS B 1 71 ? 6.420   -15.870 -32.669 1.00 49.16  ? 70  LYS B O   1 
ATOM   1294 C CB  . LYS B 1 71 ? 4.873   -17.099 -34.941 1.00 58.42  ? 70  LYS B CB  1 
ATOM   1295 C CG  . LYS B 1 71 ? 3.907   -17.353 -36.098 1.00 70.63  ? 70  LYS B CG  1 
ATOM   1296 C CD  . LYS B 1 71 ? 4.583   -17.574 -37.445 1.00 68.66  ? 70  LYS B CD  1 
ATOM   1297 C CE  . LYS B 1 71 ? 3.663   -18.095 -38.507 1.00 76.02  ? 70  LYS B CE  1 
ATOM   1298 N NZ  . LYS B 1 71 ? 4.148   -17.710 -39.838 1.00 74.28  ? 70  LYS B NZ  1 
ATOM   1299 N N   . PRO B 1 72 ? 4.736   -14.426 -33.021 1.00 54.37  ? 71  PRO B N   1 
ATOM   1300 C CA  . PRO B 1 72 ? 4.661   -14.043 -31.614 1.00 50.42  ? 71  PRO B CA  1 
ATOM   1301 C C   . PRO B 1 72 ? 4.465   -15.241 -30.694 1.00 47.20  ? 71  PRO B C   1 
ATOM   1302 O O   . PRO B 1 72 ? 3.855   -16.243 -31.075 1.00 43.33  ? 71  PRO B O   1 
ATOM   1303 C CB  . PRO B 1 72 ? 3.483   -13.056 -31.591 1.00 53.40  ? 71  PRO B CB  1 
ATOM   1304 C CG  . PRO B 1 72 ? 3.534   -12.444 -32.971 1.00 51.40  ? 71  PRO B CG  1 
ATOM   1305 C CD  . PRO B 1 72 ? 3.826   -13.644 -33.875 1.00 49.35  ? 71  PRO B CD  1 
ATOM   1306 N N   . ASN B 1 73 ? 5.030   -15.119 -29.483 1.00 49.83  ? 72  ASN B N   1 
ATOM   1307 C CA  . ASN B 1 73 ? 4.821   -16.089 -28.422 1.00 49.19  ? 72  ASN B CA  1 
ATOM   1308 C C   . ASN B 1 73 ? 4.748   -15.328 -27.091 1.00 54.03  ? 72  ASN B C   1 
ATOM   1309 O O   . ASN B 1 73 ? 4.842   -14.096 -27.056 1.00 52.37  ? 72  ASN B O   1 
ATOM   1310 C CB  . ASN B 1 73 ? 5.823   -17.241 -28.494 1.00 46.41  ? 72  ASN B CB  1 
ATOM   1311 C CG  . ASN B 1 73 ? 7.244   -16.789 -28.247 1.00 47.15  ? 72  ASN B CG  1 
ATOM   1312 O OD1 . ASN B 1 73 ? 7.490   -16.074 -27.267 1.00 45.74  ? 72  ASN B OD1 1 
ATOM   1313 N ND2 . ASN B 1 73 ? 8.183   -17.186 -29.109 1.00 41.78  ? 72  ASN B ND2 1 
ATOM   1314 N N   . LYS B 1 74 ? 4.592   -16.071 -25.995 1.00 50.17  ? 73  LYS B N   1 
ATOM   1315 C CA  . LYS B 1 74 ? 4.491   -15.471 -24.669 1.00 54.94  ? 73  LYS B CA  1 
ATOM   1316 C C   . LYS B 1 74 ? 5.824   -15.506 -23.904 1.00 53.40  ? 73  LYS B C   1 
ATOM   1317 O O   . LYS B 1 74 ? 5.815   -15.393 -22.676 1.00 51.07  ? 73  LYS B O   1 
ATOM   1318 C CB  . LYS B 1 74 ? 3.331   -16.115 -23.889 1.00 51.48  ? 73  LYS B CB  1 
ATOM   1319 C CG  . LYS B 1 74 ? 3.459   -17.622 -23.715 1.00 64.35  ? 73  LYS B CG  1 
ATOM   1320 C CD  . LYS B 1 74 ? 2.138   -18.387 -23.681 1.00 67.69  ? 73  LYS B CD  1 
ATOM   1321 N N   . ARG B 1 75 ? 6.962   -15.674 -24.609 1.00 41.18  ? 74  ARG B N   1 
ATOM   1322 C CA  . ARG B 1 75 ? 8.274   -15.553 -23.976 1.00 42.52  ? 74  ARG B CA  1 
ATOM   1323 C C   . ARG B 1 75 ? 8.612   -14.065 -23.823 1.00 42.00  ? 74  ARG B C   1 
ATOM   1324 O O   . ARG B 1 75 ? 8.354   -13.246 -24.717 1.00 43.21  ? 74  ARG B O   1 
ATOM   1325 C CB  . ARG B 1 75 ? 9.412   -16.339 -24.650 1.00 44.42  ? 74  ARG B CB  1 
ATOM   1326 C CG  . ARG B 1 75 ? 9.351   -17.849 -24.869 1.00 40.98  ? 74  ARG B CG  1 
ATOM   1327 C CD  . ARG B 1 75 ? 9.155   -18.614 -23.552 1.00 43.50  ? 74  ARG B CD  1 
ATOM   1328 N NE  . ARG B 1 75 ? 9.372   -20.058 -23.695 1.00 40.73  ? 74  ARG B NE  1 
ATOM   1329 C CZ  . ARG B 1 75 ? 10.511  -20.674 -23.495 1.00 39.74  ? 74  ARG B CZ  1 
ATOM   1330 N NH1 . ARG B 1 75 ? 11.567  -20.004 -23.029 1.00 45.42  ? 74  ARG B NH1 1 
ATOM   1331 N NH2 . ARG B 1 75 ? 10.605  -21.956 -23.813 1.00 44.59  ? 74  ARG B NH2 1 
ATOM   1332 N N   . LYS B 1 76 ? 9.126   -13.709 -22.636 1.00 41.18  ? 75  LYS B N   1 
ATOM   1333 C CA  . LYS B 1 76 ? 9.409   -12.330 -22.293 1.00 36.79  ? 75  LYS B CA  1 
ATOM   1334 C C   . LYS B 1 76 ? 10.544  -11.805 -23.181 1.00 35.94  ? 75  LYS B C   1 
ATOM   1335 O O   . LYS B 1 76 ? 11.608  -12.440 -23.273 1.00 37.10  ? 75  LYS B O   1 
ATOM   1336 C CB  . LYS B 1 76 ? 9.957   -12.200 -20.860 1.00 41.03  ? 75  LYS B CB  1 
ATOM   1337 C CG  . LYS B 1 76 ? 10.355  -10.756 -20.472 1.00 43.47  ? 75  LYS B CG  1 
ATOM   1338 C CD  . LYS B 1 76 ? 10.797  -10.587 -19.021 1.00 45.89  ? 75  LYS B CD  1 
ATOM   1339 C CE  . LYS B 1 76 ? 10.936  -9.143  -18.582 1.00 46.98  ? 75  LYS B CE  1 
ATOM   1340 N NZ  . LYS B 1 76 ? 11.270  -9.074  -17.149 1.00 56.34  ? 75  LYS B NZ  1 
ATOM   1341 N N   . GLY B 1 77 ? 10.240  -10.702 -23.850 1.00 38.97  ? 76  GLY B N   1 
ATOM   1342 C CA  . GLY B 1 77 ? 11.181  -10.049 -24.764 1.00 42.42  ? 76  GLY B CA  1 
ATOM   1343 C C   . GLY B 1 77 ? 11.009  -10.501 -26.217 1.00 39.88  ? 76  GLY B C   1 
ATOM   1344 O O   . GLY B 1 77 ? 11.592  -9.911  -27.128 1.00 41.43  ? 76  GLY B O   1 
ATOM   1345 N N   . PHE B 1 78 ? 10.235  -11.563 -26.463 1.00 36.78  ? 77  PHE B N   1 
ATOM   1346 C CA  . PHE B 1 78 ? 10.158  -12.108 -27.824 1.00 35.36  ? 77  PHE B CA  1 
ATOM   1347 C C   . PHE B 1 78 ? 9.434   -11.175 -28.802 1.00 39.43  ? 77  PHE B C   1 
ATOM   1348 O O   . PHE B 1 78 ? 9.953   -10.894 -29.873 1.00 35.76  ? 77  PHE B O   1 
ATOM   1349 C CB  . PHE B 1 78 ? 9.412   -13.447 -27.859 1.00 35.77  ? 77  PHE B CB  1 
ATOM   1350 C CG  . PHE B 1 78 ? 9.647   -14.188 -29.169 1.00 37.90  ? 77  PHE B CG  1 
ATOM   1351 C CD1 . PHE B 1 78 ? 10.762  -15.006 -29.330 1.00 34.66  ? 77  PHE B CD1 1 
ATOM   1352 C CD2 . PHE B 1 78 ? 8.729   -14.082 -30.221 1.00 40.11  ? 77  PHE B CD2 1 
ATOM   1353 C CE1 . PHE B 1 78 ? 10.977  -15.680 -30.542 1.00 35.75  ? 77  PHE B CE1 1 
ATOM   1354 C CE2 . PHE B 1 78 ? 8.936   -14.773 -31.416 1.00 37.71  ? 77  PHE B CE2 1 
ATOM   1355 C CZ  . PHE B 1 78 ? 10.065  -15.584 -31.564 1.00 36.80  ? 77  PHE B CZ  1 
ATOM   1356 N N   . ASN B 1 79 ? 8.199   -10.756 -28.499 1.00 36.71  ? 78  ASN B N   1 
ATOM   1357 C CA  . ASN B 1 79 ? 7.473   -9.841  -29.372 1.00 41.18  ? 78  ASN B CA  1 
ATOM   1358 C C   . ASN B 1 79 ? 8.232   -8.506  -29.522 1.00 43.05  ? 78  ASN B C   1 
ATOM   1359 O O   . ASN B 1 79 ? 8.210   -7.903  -30.594 1.00 41.52  ? 78  ASN B O   1 
ATOM   1360 C CB  . ASN B 1 79 ? 5.998   -9.721  -28.999 1.00 42.49  ? 78  ASN B CB  1 
ATOM   1361 C CG  . ASN B 1 79 ? 5.281   -11.055 -29.027 1.00 49.02  ? 78  ASN B CG  1 
ATOM   1362 O OD1 . ASN B 1 79 ? 5.792   -12.030 -29.598 1.00 47.01  ? 78  ASN B OD1 1 
ATOM   1363 N ND2 . ASN B 1 79 ? 4.120   -11.136 -28.390 1.00 48.39  ? 78  ASN B ND2 1 
ATOM   1364 N N   . GLU B 1 80 ? 8.936   -8.061  -28.482 1.00 41.84  ? 79  GLU B N   1 
ATOM   1365 C CA  . GLU B 1 80 ? 9.699   -6.830  -28.628 1.00 42.92  ? 79  GLU B CA  1 
ATOM   1366 C C   . GLU B 1 80 ? 10.825  -7.070  -29.640 1.00 40.18  ? 79  GLU B C   1 
ATOM   1367 O O   . GLU B 1 80 ? 11.124  -6.179  -30.446 1.00 40.15  ? 79  GLU B O   1 
ATOM   1368 C CB  . GLU B 1 80 ? 10.289  -6.311  -27.322 1.00 43.23  ? 79  GLU B CB  1 
ATOM   1369 C CG  . GLU B 1 80 ? 9.252   -5.560  -26.494 1.00 50.61  ? 79  GLU B CG  1 
ATOM   1370 N N   . GLY B 1 81 ? 11.415  -8.279  -29.555 1.00 37.66  ? 80  GLY B N   1 
ATOM   1371 C CA  . GLY B 1 81 ? 12.463  -8.724  -30.467 1.00 38.67  ? 80  GLY B CA  1 
ATOM   1372 C C   . GLY B 1 81 ? 11.965  -8.713  -31.903 1.00 37.42  ? 80  GLY B C   1 
ATOM   1373 O O   . GLY B 1 81 ? 12.708  -8.330  -32.820 1.00 38.95  ? 80  GLY B O   1 
ATOM   1374 N N   . LEU B 1 82 ? 10.713  -9.119  -32.092 1.00 34.35  ? 81  LEU B N   1 
ATOM   1375 C CA  . LEU B 1 82 ? 10.167  -9.212  -33.431 1.00 40.34  ? 81  LEU B CA  1 
ATOM   1376 C C   . LEU B 1 82 ? 10.011  -7.793  -33.966 1.00 40.67  ? 81  LEU B C   1 
ATOM   1377 O O   . LEU B 1 82 ? 10.231  -7.560  -35.143 1.00 40.40  ? 81  LEU B O   1 
ATOM   1378 C CB  . LEU B 1 82 ? 8.854   -9.994  -33.542 1.00 36.85  ? 81  LEU B CB  1 
ATOM   1379 C CG  . LEU B 1 82 ? 8.940   -11.497 -33.249 1.00 37.68  ? 81  LEU B CG  1 
ATOM   1380 C CD1 . LEU B 1 82 ? 7.546   -12.132 -33.271 1.00 37.25  ? 81  LEU B CD1 1 
ATOM   1381 C CD2 . LEU B 1 82 ? 9.856   -12.149 -34.261 1.00 35.80  ? 81  LEU B CD2 1 
ATOM   1382 N N   . TRP B 1 83 ? 9.644   -6.866  -33.077 1.00 38.15  ? 82  TRP B N   1 
ATOM   1383 C CA  . TRP B 1 83 ? 9.488   -5.479  -33.462 1.00 37.46  ? 82  TRP B CA  1 
ATOM   1384 C C   . TRP B 1 83 ? 10.835  -4.919  -33.910 1.00 38.62  ? 82  TRP B C   1 
ATOM   1385 O O   . TRP B 1 83 ? 10.896  -4.294  -34.972 1.00 38.07  ? 82  TRP B O   1 
ATOM   1386 C CB  . TRP B 1 83 ? 8.817   -4.632  -32.366 1.00 41.73  ? 82  TRP B CB  1 
ATOM   1387 C CG  . TRP B 1 83 ? 8.524   -3.234  -32.849 1.00 41.12  ? 82  TRP B CG  1 
ATOM   1388 C CD1 . TRP B 1 83 ? 7.380   -2.777  -33.439 1.00 51.44  ? 82  TRP B CD1 1 
ATOM   1389 C CD2 . TRP B 1 83 ? 9.451   -2.127  -32.860 1.00 42.96  ? 82  TRP B CD2 1 
ATOM   1390 N NE1 . TRP B 1 83 ? 7.527   -1.461  -33.804 1.00 50.14  ? 82  TRP B NE1 1 
ATOM   1391 C CE2 . TRP B 1 83 ? 8.785   -1.037  -33.459 1.00 46.45  ? 82  TRP B CE2 1 
ATOM   1392 C CE3 . TRP B 1 83 ? 10.773  -1.960  -32.421 1.00 41.98  ? 82  TRP B CE3 1 
ATOM   1393 C CZ2 . TRP B 1 83 ? 9.395   0.211   -33.620 1.00 47.54  ? 82  TRP B CZ2 1 
ATOM   1394 C CZ3 . TRP B 1 83 ? 11.363  -0.718  -32.562 1.00 47.99  ? 82  TRP B CZ3 1 
ATOM   1395 C CH2 . TRP B 1 83 ? 10.685  0.346   -33.159 1.00 42.24  ? 82  TRP B CH2 1 
ATOM   1396 N N   . GLU B 1 84 ? 11.901  -5.236  -33.153 1.00 35.64  ? 83  GLU B N   1 
ATOM   1397 C CA  . GLU B 1 84 ? 13.225  -4.672  -33.371 1.00 39.82  ? 83  GLU B CA  1 
ATOM   1398 C C   . GLU B 1 84 ? 13.796  -5.178  -34.696 1.00 40.66  ? 83  GLU B C   1 
ATOM   1399 O O   . GLU B 1 84 ? 14.331  -4.381  -35.463 1.00 37.71  ? 83  GLU B O   1 
ATOM   1400 C CB  . GLU B 1 84 ? 14.198  -4.921  -32.227 1.00 36.05  ? 83  GLU B CB  1 
ATOM   1401 C CG  . GLU B 1 84 ? 13.733  -4.275  -30.912 1.00 42.23  ? 83  GLU B CG  1 
ATOM   1402 C CD  . GLU B 1 84 ? 14.608  -4.593  -29.731 1.00 42.43  ? 83  GLU B CD  1 
ATOM   1403 O OE1 . GLU B 1 84 ? 15.501  -5.455  -29.909 1.00 38.38  ? 83  GLU B OE1 1 
ATOM   1404 O OE2 . GLU B 1 84 ? 14.458  -3.957  -28.648 1.00 44.15  ? 83  GLU B OE2 1 
ATOM   1405 N N   . ILE B 1 85 ? 13.686  -6.490  -34.966 1.00 38.63  ? 84  ILE B N   1 
ATOM   1406 C CA  . ILE B 1 85 ? 14.370  -7.048  -36.135 1.00 36.83  ? 84  ILE B CA  1 
ATOM   1407 C C   . ILE B 1 85 ? 13.743  -6.514  -37.425 1.00 37.00  ? 84  ILE B C   1 
ATOM   1408 O O   . ILE B 1 85 ? 14.427  -6.316  -38.444 1.00 36.05  ? 84  ILE B O   1 
ATOM   1409 C CB  . ILE B 1 85 ? 14.454  -8.591  -36.087 1.00 36.93  ? 84  ILE B CB  1 
ATOM   1410 C CG1 . ILE B 1 85 ? 15.473  -9.092  -37.116 1.00 36.46  ? 84  ILE B CG1 1 
ATOM   1411 C CG2 . ILE B 1 85 ? 13.068  -9.205  -36.321 1.00 34.86  ? 84  ILE B CG2 1 
ATOM   1412 C CD1 . ILE B 1 85 ? 16.020  -10.493 -36.850 1.00 42.58  ? 84  ILE B CD1 1 
ATOM   1413 N N   . GLN B 1 86 ? 12.450  -6.216  -37.316 1.00 35.34  ? 85  GLN B N   1 
ATOM   1414 C CA  . GLN B 1 86 ? 11.593  -5.693  -38.361 1.00 41.84  ? 85  GLN B CA  1 
ATOM   1415 C C   . GLN B 1 86 ? 11.839  -4.197  -38.582 1.00 45.08  ? 85  GLN B C   1 
ATOM   1416 O O   . GLN B 1 86 ? 11.891  -3.756  -39.737 1.00 44.08  ? 85  GLN B O   1 
ATOM   1417 C CB  . GLN B 1 86 ? 10.150  -6.017  -37.964 1.00 46.41  ? 85  GLN B CB  1 
ATOM   1418 C CG  . GLN B 1 86 ? 9.742   -7.446  -38.334 1.00 60.76  ? 85  GLN B CG  1 
ATOM   1419 C CD  . GLN B 1 86 ? 8.554   -8.022  -37.584 1.00 62.55  ? 85  GLN B CD  1 
ATOM   1420 O OE1 . GLN B 1 86 ? 7.439   -7.485  -37.584 1.00 70.52  ? 85  GLN B OE1 1 
ATOM   1421 N NE2 . GLN B 1 86 ? 8.780   -9.165  -36.958 1.00 54.00  ? 85  GLN B NE2 1 
ATOM   1422 N N   . ASN B 1 87 ? 11.975  -3.414  -37.492 1.00 37.42  ? 86  ASN B N   1 
ATOM   1423 C CA  . ASN B 1 87 ? 11.803  -1.967  -37.641 1.00 38.18  ? 86  ASN B CA  1 
ATOM   1424 C C   . ASN B 1 87 ? 13.105  -1.203  -37.446 1.00 40.02  ? 86  ASN B C   1 
ATOM   1425 O O   . ASN B 1 87 ? 13.224  -0.075  -37.925 1.00 42.47  ? 86  ASN B O   1 
ATOM   1426 C CB  . ASN B 1 87 ? 10.791  -1.410  -36.634 1.00 41.37  ? 86  ASN B CB  1 
ATOM   1427 C CG  . ASN B 1 87 ? 9.417   -1.926  -36.945 1.00 49.36  ? 86  ASN B CG  1 
ATOM   1428 O OD1 . ASN B 1 87 ? 8.825   -1.531  -37.957 1.00 51.24  ? 86  ASN B OD1 1 
ATOM   1429 N ND2 . ASN B 1 87 ? 8.933   -2.858  -36.140 1.00 51.55  ? 86  ASN B ND2 1 
ATOM   1430 N N   . ASN B 1 88 ? 14.067  -1.782  -36.719 1.00 38.97  ? 87  ASN B N   1 
ATOM   1431 C CA  . ASN B 1 88 ? 15.334  -1.100  -36.473 1.00 38.97  ? 87  ASN B CA  1 
ATOM   1432 C C   . ASN B 1 88 ? 16.419  -2.097  -36.067 1.00 39.99  ? 87  ASN B C   1 
ATOM   1433 O O   . ASN B 1 88 ? 17.021  -1.990  -34.977 1.00 35.24  ? 87  ASN B O   1 
ATOM   1434 C CB  . ASN B 1 88 ? 15.211  0.079   -35.498 1.00 42.88  ? 87  ASN B CB  1 
ATOM   1435 C CG  . ASN B 1 88 ? 16.295  1.125   -35.701 1.00 45.15  ? 87  ASN B CG  1 
ATOM   1436 O OD1 . ASN B 1 88 ? 17.340  0.858   -36.313 1.00 40.16  ? 87  ASN B OD1 1 
ATOM   1437 N ND2 . ASN B 1 88 ? 16.073  2.332   -35.194 1.00 41.91  ? 87  ASN B ND2 1 
ATOM   1438 N N   . PRO B 1 89 ? 16.712  -3.075  -36.962 1.00 39.84  ? 88  PRO B N   1 
ATOM   1439 C CA  . PRO B 1 89 ? 17.695  -4.122  -36.665 1.00 35.27  ? 88  PRO B CA  1 
ATOM   1440 C C   . PRO B 1 89 ? 19.125  -3.695  -36.379 1.00 34.09  ? 88  PRO B C   1 
ATOM   1441 O O   . PRO B 1 89 ? 19.893  -4.471  -35.819 1.00 35.27  ? 88  PRO B O   1 
ATOM   1442 C CB  . PRO B 1 89 ? 17.599  -5.046  -37.933 1.00 35.78  ? 88  PRO B CB  1 
ATOM   1443 C CG  . PRO B 1 89 ? 17.120  -4.119  -39.053 1.00 36.97  ? 88  PRO B CG  1 
ATOM   1444 C CD  . PRO B 1 89 ? 16.097  -3.242  -38.302 1.00 36.78  ? 88  PRO B CD  1 
ATOM   1445 N N   . HIS B 1 90 ? 19.518  -2.496  -36.859 1.00 33.87  ? 89  HIS B N   1 
ATOM   1446 C CA  . HIS B 1 90 ? 20.922  -2.126  -36.813 1.00 33.42  ? 89  HIS B CA  1 
ATOM   1447 C C   . HIS B 1 90 ? 21.207  -1.082  -35.726 1.00 40.21  ? 89  HIS B C   1 
ATOM   1448 O O   . HIS B 1 90 ? 22.327  -0.566  -35.640 1.00 38.05  ? 89  HIS B O   1 
ATOM   1449 C CB  . HIS B 1 90 ? 21.373  -1.689  -38.218 1.00 36.02  ? 89  HIS B CB  1 
ATOM   1450 C CG  . HIS B 1 90 ? 21.212  -2.790  -39.221 1.00 37.31  ? 89  HIS B CG  1 
ATOM   1451 N ND1 . HIS B 1 90 ? 21.810  -4.019  -39.087 1.00 38.09  ? 89  HIS B ND1 1 
ATOM   1452 C CD2 . HIS B 1 90 ? 20.579  -2.818  -40.389 1.00 34.27  ? 89  HIS B CD2 1 
ATOM   1453 C CE1 . HIS B 1 90 ? 21.483  -4.768  -40.133 1.00 35.22  ? 89  HIS B CE1 1 
ATOM   1454 N NE2 . HIS B 1 90 ? 20.728  -4.054  -40.914 1.00 37.23  ? 89  HIS B NE2 1 
ATOM   1455 N N   . ALA B 1 91 ? 20.188  -0.782  -34.910 1.00 40.52  ? 90  ALA B N   1 
ATOM   1456 C CA  . ALA B 1 91 ? 20.293  0.253   -33.886 1.00 40.38  ? 90  ALA B CA  1 
ATOM   1457 C C   . ALA B 1 91 ? 21.213  -0.163  -32.746 1.00 42.17  ? 90  ALA B C   1 
ATOM   1458 O O   . ALA B 1 91 ? 21.536  -1.338  -32.546 1.00 40.23  ? 90  ALA B O   1 
ATOM   1459 C CB  . ALA B 1 91 ? 18.932  0.672   -33.369 1.00 35.84  ? 90  ALA B CB  1 
ATOM   1460 N N   . SER B 1 92 ? 21.661  0.866   -32.006 1.00 44.00  ? 91  SER B N   1 
ATOM   1461 C CA  . SER B 1 92 ? 22.323  0.693   -30.732 1.00 44.53  ? 91  SER B CA  1 
ATOM   1462 C C   . SER B 1 92 ? 21.250  0.488   -29.668 1.00 47.43  ? 91  SER B C   1 
ATOM   1463 O O   . SER B 1 92 ? 20.334  1.308   -29.536 1.00 48.54  ? 91  SER B O   1 
ATOM   1464 C CB  . SER B 1 92 ? 23.203  1.906   -30.430 1.00 51.49  ? 91  SER B CB  1 
ATOM   1465 O OG  . SER B 1 92 ? 23.708  1.830   -29.109 1.00 56.10  ? 91  SER B OG  1 
ATOM   1466 N N   . TYR B 1 93 ? 21.347  -0.666  -28.999 1.00 49.06  ? 92  TYR B N   1 
ATOM   1467 C CA  . TYR B 1 93 ? 20.472  -1.095  -27.925 1.00 50.81  ? 92  TYR B CA  1 
ATOM   1468 C C   . TYR B 1 93 ? 21.261  -1.003  -26.619 1.00 56.30  ? 92  TYR B C   1 
ATOM   1469 O O   . TYR B 1 93 ? 20.850  -1.544  -25.592 1.00 59.11  ? 92  TYR B O   1 
ATOM   1470 C CB  . TYR B 1 93 ? 19.808  -2.449  -28.230 1.00 45.06  ? 92  TYR B CB  1 
ATOM   1471 C CG  . TYR B 1 93 ? 18.833  -2.360  -29.393 1.00 39.65  ? 92  TYR B CG  1 
ATOM   1472 C CD1 . TYR B 1 93 ? 17.541  -1.898  -29.185 1.00 37.91  ? 92  TYR B CD1 1 
ATOM   1473 C CD2 . TYR B 1 93 ? 19.198  -2.702  -30.697 1.00 40.95  ? 92  TYR B CD2 1 
ATOM   1474 C CE1 . TYR B 1 93 ? 16.642  -1.731  -30.223 1.00 39.42  ? 92  TYR B CE1 1 
ATOM   1475 C CE2 . TYR B 1 93 ? 18.296  -2.541  -31.745 1.00 39.85  ? 92  TYR B CE2 1 
ATOM   1476 C CZ  . TYR B 1 93 ? 17.005  -2.098  -31.506 1.00 38.67  ? 92  TYR B CZ  1 
ATOM   1477 O OH  . TYR B 1 93 ? 16.058  -1.938  -32.477 1.00 40.29  ? 92  TYR B OH  1 
ATOM   1478 N N   . SER B 1 94 ? 22.379  -0.262  -26.681 1.00 65.71  ? 93  SER B N   1 
ATOM   1479 C CA  . SER B 1 94 ? 23.138  0.154   -25.510 1.00 66.99  ? 93  SER B CA  1 
ATOM   1480 C C   . SER B 1 94 ? 22.153  0.567   -24.404 1.00 78.75  ? 93  SER B C   1 
ATOM   1481 O O   . SER B 1 94 ? 21.550  1.650   -24.562 1.00 74.53  ? 93  SER B O   1 
ATOM   1482 C CB  . SER B 1 94 ? 24.056  1.312   -25.846 1.00 71.77  ? 93  SER B CB  1 
ATOM   1483 O OG  . SER B 1 94 ? 25.007  0.976   -26.849 1.00 70.75  ? 93  SER B OG  1 
ATOM   1484 O OXT . SER B 1 94 ? 21.990  -0.220  -23.445 1.00 86.25  ? 93  SER B OXT 1 
ATOM   1485 N N   . HIS C 1 4  ? 32.750  -24.092 27.262  1.00 71.37  ? 3   HIS C N   1 
ATOM   1486 C CA  . HIS C 1 4  ? 31.755  -22.994 27.397  1.00 81.83  ? 3   HIS C CA  1 
ATOM   1487 C C   . HIS C 1 4  ? 31.061  -23.145 28.754  1.00 86.78  ? 3   HIS C C   1 
ATOM   1488 O O   . HIS C 1 4  ? 31.689  -23.532 29.741  1.00 79.48  ? 3   HIS C O   1 
ATOM   1489 C CB  . HIS C 1 4  ? 30.861  -22.964 26.148  1.00 81.74  ? 3   HIS C CB  1 
ATOM   1490 C CG  . HIS C 1 4  ? 30.067  -21.714 25.926  1.00 85.59  ? 3   HIS C CG  1 
ATOM   1491 N ND1 . HIS C 1 4  ? 30.637  -20.513 25.557  1.00 84.23  ? 3   HIS C ND1 1 
ATOM   1492 C CD2 . HIS C 1 4  ? 28.748  -21.482 26.013  1.00 81.79  ? 3   HIS C CD2 1 
ATOM   1493 C CE1 . HIS C 1 4  ? 29.686  -19.597 25.424  1.00 79.93  ? 3   HIS C CE1 1 
ATOM   1494 N NE2 . HIS C 1 4  ? 28.531  -20.165 25.694  1.00 84.81  ? 3   HIS C NE2 1 
ATOM   1495 N N   . ALA C 1 5  ? 29.759  -22.842 28.783  1.00 90.47  ? 4   ALA C N   1 
ATOM   1496 C CA  . ALA C 1 5  ? 28.929  -22.908 29.974  1.00 87.35  ? 4   ALA C CA  1 
ATOM   1497 C C   . ALA C 1 5  ? 27.476  -23.025 29.530  1.00 87.12  ? 4   ALA C C   1 
ATOM   1498 O O   . ALA C 1 5  ? 27.104  -22.447 28.509  1.00 86.39  ? 4   ALA C O   1 
ATOM   1499 C CB  . ALA C 1 5  ? 29.118  -21.639 30.762  1.00 88.88  ? 4   ALA C CB  1 
ATOM   1500 N N   . PHE C 1 6  ? 26.663  -23.756 30.302  1.00 71.47  ? 5   PHE C N   1 
ATOM   1501 C CA  . PHE C 1 6  ? 25.261  -23.900 29.953  1.00 63.92  ? 5   PHE C CA  1 
ATOM   1502 C C   . PHE C 1 6  ? 24.418  -24.055 31.214  1.00 65.39  ? 5   PHE C C   1 
ATOM   1503 O O   . PHE C 1 6  ? 24.725  -24.867 32.080  1.00 78.19  ? 5   PHE C O   1 
ATOM   1504 C CB  . PHE C 1 6  ? 25.056  -25.085 28.996  1.00 64.69  ? 5   PHE C CB  1 
ATOM   1505 C CG  . PHE C 1 6  ? 25.771  -24.995 27.654  1.00 56.65  ? 5   PHE C CG  1 
ATOM   1506 C CD1 . PHE C 1 6  ? 26.868  -25.801 27.380  1.00 51.18  ? 5   PHE C CD1 1 
ATOM   1507 C CD2 . PHE C 1 6  ? 25.358  -24.091 26.677  1.00 54.35  ? 5   PHE C CD2 1 
ATOM   1508 C CE1 . PHE C 1 6  ? 27.526  -25.726 26.154  1.00 60.71  ? 5   PHE C CE1 1 
ATOM   1509 C CE2 . PHE C 1 6  ? 26.019  -24.017 25.453  1.00 58.13  ? 5   PHE C CE2 1 
ATOM   1510 C CZ  . PHE C 1 6  ? 27.096  -24.839 25.183  1.00 51.37  ? 5   PHE C CZ  1 
ATOM   1511 N N   . LYS C 1 7  ? 23.341  -23.277 31.297  1.00 59.55  ? 6   LYS C N   1 
ATOM   1512 C CA  . LYS C 1 7  ? 22.335  -23.473 32.326  1.00 62.19  ? 6   LYS C CA  1 
ATOM   1513 C C   . LYS C 1 7  ? 21.020  -23.796 31.626  1.00 56.95  ? 6   LYS C C   1 
ATOM   1514 O O   . LYS C 1 7  ? 20.963  -23.739 30.399  1.00 57.95  ? 6   LYS C O   1 
ATOM   1515 C CB  . LYS C 1 7  ? 22.270  -22.251 33.253  1.00 65.24  ? 6   LYS C CB  1 
ATOM   1516 N N   . PRO C 1 8  ? 19.934  -24.128 32.366  1.00 59.22  ? 7   PRO C N   1 
ATOM   1517 C CA  . PRO C 1 8  ? 18.646  -24.455 31.757  1.00 64.81  ? 7   PRO C CA  1 
ATOM   1518 C C   . PRO C 1 8  ? 18.080  -23.265 30.986  1.00 70.32  ? 7   PRO C C   1 
ATOM   1519 O O   . PRO C 1 8  ? 18.021  -22.149 31.502  1.00 66.80  ? 7   PRO C O   1 
ATOM   1520 C CB  . PRO C 1 8  ? 17.776  -24.821 32.976  1.00 68.82  ? 7   PRO C CB  1 
ATOM   1521 C CG  . PRO C 1 8  ? 18.776  -25.216 34.034  1.00 60.03  ? 7   PRO C CG  1 
ATOM   1522 C CD  . PRO C 1 8  ? 19.900  -24.212 33.837  1.00 58.63  ? 7   PRO C CD  1 
ATOM   1523 N N   . GLY C 1 9  ? 17.679  -23.518 29.736  1.00 73.75  ? 8   GLY C N   1 
ATOM   1524 C CA  . GLY C 1 9  ? 17.068  -22.493 28.907  1.00 63.94  ? 8   GLY C CA  1 
ATOM   1525 C C   . GLY C 1 9  ? 17.990  -22.029 27.782  1.00 60.96  ? 8   GLY C C   1 
ATOM   1526 O O   . GLY C 1 9  ? 17.510  -21.488 26.790  1.00 69.74  ? 8   GLY C O   1 
ATOM   1527 N N   . ASP C 1 10 ? 19.303  -22.257 27.938  1.00 53.62  ? 9   ASP C N   1 
ATOM   1528 C CA  . ASP C 1 10 ? 20.292  -21.947 26.920  1.00 48.23  ? 9   ASP C CA  1 
ATOM   1529 C C   . ASP C 1 10 ? 19.954  -22.653 25.604  1.00 51.87  ? 9   ASP C C   1 
ATOM   1530 O O   . ASP C 1 10 ? 19.687  -23.850 25.578  1.00 48.23  ? 9   ASP C O   1 
ATOM   1531 C CB  . ASP C 1 10 ? 21.710  -22.246 27.379  1.00 53.38  ? 9   ASP C CB  1 
ATOM   1532 C CG  . ASP C 1 10 ? 22.365  -21.215 28.296  1.00 61.89  ? 9   ASP C CG  1 
ATOM   1533 O OD1 . ASP C 1 10 ? 21.814  -20.101 28.431  1.00 66.37  ? 9   ASP C OD1 1 
ATOM   1534 O OD2 . ASP C 1 10 ? 23.425  -21.534 28.871  1.00 64.36  ? 9   ASP C OD2 1 
ATOM   1535 N N   . LEU C 1 11 ? 19.951  -21.886 24.511  1.00 52.48  ? 10  LEU C N   1 
ATOM   1536 C CA  . LEU C 1 11 ? 19.615  -22.420 23.202  1.00 48.96  ? 10  LEU C CA  1 
ATOM   1537 C C   . LEU C 1 11 ? 20.895  -22.884 22.532  1.00 42.39  ? 10  LEU C C   1 
ATOM   1538 O O   . LEU C 1 11 ? 21.895  -22.183 22.588  1.00 44.80  ? 10  LEU C O   1 
ATOM   1539 C CB  . LEU C 1 11 ? 18.900  -21.343 22.378  1.00 50.78  ? 10  LEU C CB  1 
ATOM   1540 C CG  . LEU C 1 11 ? 17.617  -20.800 23.007  1.00 48.15  ? 10  LEU C CG  1 
ATOM   1541 C CD1 . LEU C 1 11 ? 16.912  -19.762 22.150  1.00 55.05  ? 10  LEU C CD1 1 
ATOM   1542 C CD2 . LEU C 1 11 ? 16.711  -21.973 23.280  1.00 49.19  ? 10  LEU C CD2 1 
ATOM   1543 N N   . VAL C 1 12 ? 20.863  -24.068 21.892  1.00 41.73  ? 11  VAL C N   1 
ATOM   1544 C CA  . VAL C 1 12 ? 22.071  -24.661 21.331  1.00 40.60  ? 11  VAL C CA  1 
ATOM   1545 C C   . VAL C 1 12 ? 21.691  -25.421 20.054  1.00 40.75  ? 11  VAL C C   1 
ATOM   1546 O O   . VAL C 1 12 ? 20.510  -25.612 19.820  1.00 37.83  ? 11  VAL C O   1 
ATOM   1547 C CB  . VAL C 1 12 ? 22.668  -25.673 22.332  1.00 42.61  ? 11  VAL C CB  1 
ATOM   1548 C CG1 . VAL C 1 12 ? 22.996  -25.043 23.691  1.00 45.31  ? 11  VAL C CG1 1 
ATOM   1549 C CG2 . VAL C 1 12 ? 21.776  -26.912 22.490  1.00 41.11  ? 11  VAL C CG2 1 
ATOM   1550 N N   . PHE C 1 13 ? 22.706  -25.826 19.268  1.00 41.14  ? 12  PHE C N   1 
ATOM   1551 C CA  . PHE C 1 13 ? 22.643  -26.980 18.379  1.00 38.03  ? 12  PHE C CA  1 
ATOM   1552 C C   . PHE C 1 13 ? 23.359  -28.152 19.061  1.00 37.84  ? 12  PHE C C   1 
ATOM   1553 O O   . PHE C 1 13 ? 24.419  -27.988 19.668  1.00 40.55  ? 12  PHE C O   1 
ATOM   1554 C CB  . PHE C 1 13 ? 23.344  -26.719 17.041  1.00 42.76  ? 12  PHE C CB  1 
ATOM   1555 C CG  . PHE C 1 13 ? 22.599  -25.722 16.174  1.00 46.36  ? 12  PHE C CG  1 
ATOM   1556 C CD1 . PHE C 1 13 ? 21.589  -26.142 15.300  1.00 39.97  ? 12  PHE C CD1 1 
ATOM   1557 C CD2 . PHE C 1 13 ? 22.937  -24.375 16.216  1.00 45.51  ? 12  PHE C CD2 1 
ATOM   1558 C CE1 . PHE C 1 13 ? 20.928  -25.221 14.507  1.00 46.14  ? 12  PHE C CE1 1 
ATOM   1559 C CE2 . PHE C 1 13 ? 22.262  -23.463 15.432  1.00 50.65  ? 12  PHE C CE2 1 
ATOM   1560 C CZ  . PHE C 1 13 ? 21.279  -23.889 14.572  1.00 48.89  ? 12  PHE C CZ  1 
ATOM   1561 N N   . ALA C 1 14 ? 22.728  -29.332 19.018  1.00 36.94  ? 13  ALA C N   1 
ATOM   1562 C CA  . ALA C 1 14 ? 23.211  -30.468 19.788  1.00 34.26  ? 13  ALA C CA  1 
ATOM   1563 C C   . ALA C 1 14 ? 23.530  -31.576 18.803  1.00 40.61  ? 13  ALA C C   1 
ATOM   1564 O O   . ALA C 1 14 ? 22.670  -31.899 17.988  1.00 37.38  ? 13  ALA C O   1 
ATOM   1565 C CB  . ALA C 1 14 ? 22.112  -30.935 20.718  1.00 36.89  ? 13  ALA C CB  1 
ATOM   1566 N N   . LYS C 1 15 ? 24.736  -32.153 18.909  1.00 38.47  ? 14  LYS C N   1 
ATOM   1567 C CA  . LYS C 1 15 ? 25.184  -33.145 17.942  1.00 40.16  ? 14  LYS C CA  1 
ATOM   1568 C C   . LYS C 1 15 ? 25.168  -34.543 18.551  1.00 38.81  ? 14  LYS C C   1 
ATOM   1569 O O   . LYS C 1 15 ? 25.863  -34.810 19.533  1.00 43.22  ? 14  LYS C O   1 
ATOM   1570 C CB  . LYS C 1 15 ? 26.587  -32.831 17.391  1.00 41.67  ? 14  LYS C CB  1 
ATOM   1571 C CG  . LYS C 1 15 ? 27.052  -33.838 16.299  1.00 45.96  ? 14  LYS C CG  1 
ATOM   1572 C CD  . LYS C 1 15 ? 26.210  -33.780 15.017  1.00 42.55  ? 14  LYS C CD  1 
ATOM   1573 C CE  . LYS C 1 15 ? 26.686  -34.589 13.819  1.00 40.90  ? 14  LYS C CE  1 
ATOM   1574 N NZ  . LYS C 1 15 ? 26.610  -36.029 14.052  1.00 39.90  ? 14  LYS C NZ  1 
ATOM   1575 N N   . MET C 1 16 ? 24.358  -35.437 17.969  1.00 36.65  ? 15  MET C N   1 
ATOM   1576 C CA  . MET C 1 16 ? 24.410  -36.862 18.301  1.00 37.07  ? 15  MET C CA  1 
ATOM   1577 C C   . MET C 1 16 ? 24.906  -37.651 17.100  1.00 40.35  ? 15  MET C C   1 
ATOM   1578 O O   . MET C 1 16 ? 24.623  -37.303 15.961  1.00 35.03  ? 15  MET C O   1 
ATOM   1579 C CB  . MET C 1 16 ? 23.008  -37.398 18.611  1.00 37.42  ? 15  MET C CB  1 
ATOM   1580 C CG  . MET C 1 16 ? 22.346  -36.716 19.813  1.00 41.07  ? 15  MET C CG  1 
ATOM   1581 S SD  . MET C 1 16 ? 20.789  -37.505 20.242  1.00 47.68  ? 15  MET C SD  1 
ATOM   1582 C CE  . MET C 1 16 ? 19.736  -36.861 18.928  1.00 47.69  ? 15  MET C CE  1 
ATOM   1583 N N   . LYS C 1 17 ? 25.589  -38.774 17.352  1.00 38.81  ? 16  LYS C N   1 
ATOM   1584 C CA  . LYS C 1 17 ? 25.986  -39.611 16.232  1.00 40.71  ? 16  LYS C CA  1 
ATOM   1585 C C   . LYS C 1 17 ? 24.736  -40.048 15.458  1.00 34.14  ? 16  LYS C C   1 
ATOM   1586 O O   . LYS C 1 17 ? 23.764  -40.519 16.036  1.00 39.41  ? 16  LYS C O   1 
ATOM   1587 C CB  . LYS C 1 17 ? 26.716  -40.841 16.793  1.00 39.67  ? 16  LYS C CB  1 
ATOM   1588 C CG  . LYS C 1 17 ? 27.250  -41.809 15.749  1.00 48.89  ? 16  LYS C CG  1 
ATOM   1589 C CD  . LYS C 1 17 ? 28.438  -41.162 15.053  1.00 56.14  ? 16  LYS C CD  1 
ATOM   1590 C CE  . LYS C 1 17 ? 29.364  -42.119 14.363  1.00 64.68  ? 16  LYS C CE  1 
ATOM   1591 N NZ  . LYS C 1 17 ? 30.558  -41.408 13.893  1.00 53.46  ? 16  LYS C NZ  1 
ATOM   1592 N N   . GLY C 1 18 ? 24.805  -39.927 14.138  1.00 39.70  ? 17  GLY C N   1 
ATOM   1593 C CA  . GLY C 1 18 ? 23.714  -40.419 13.303  1.00 39.21  ? 17  GLY C CA  1 
ATOM   1594 C C   . GLY C 1 18 ? 22.756  -39.289 12.920  1.00 39.03  ? 17  GLY C C   1 
ATOM   1595 O O   . GLY C 1 18 ? 21.759  -39.535 12.244  1.00 39.73  ? 17  GLY C O   1 
ATOM   1596 N N   . TYR C 1 19 ? 23.032  -38.070 13.405  1.00 36.61  ? 18  TYR C N   1 
ATOM   1597 C CA  . TYR C 1 19 ? 22.090  -36.960 13.230  1.00 38.68  ? 18  TYR C CA  1 
ATOM   1598 C C   . TYR C 1 19 ? 22.839  -35.669 12.934  1.00 38.12  ? 18  TYR C C   1 
ATOM   1599 O O   . TYR C 1 19 ? 23.953  -35.457 13.400  1.00 37.14  ? 18  TYR C O   1 
ATOM   1600 C CB  . TYR C 1 19 ? 21.257  -36.677 14.488  1.00 35.71  ? 18  TYR C CB  1 
ATOM   1601 C CG  . TYR C 1 19 ? 20.400  -37.867 14.875  1.00 38.69  ? 18  TYR C CG  1 
ATOM   1602 C CD1 . TYR C 1 19 ? 20.921  -38.915 15.630  1.00 38.71  ? 18  TYR C CD1 1 
ATOM   1603 C CD2 . TYR C 1 19 ? 19.085  -37.954 14.445  1.00 38.69  ? 18  TYR C CD2 1 
ATOM   1604 C CE1 . TYR C 1 19 ? 20.136  -40.005 15.956  1.00 38.01  ? 18  TYR C CE1 1 
ATOM   1605 C CE2 . TYR C 1 19 ? 18.298  -39.043 14.767  1.00 43.15  ? 18  TYR C CE2 1 
ATOM   1606 C CZ  . TYR C 1 19 ? 18.836  -40.080 15.503  1.00 38.83  ? 18  TYR C CZ  1 
ATOM   1607 O OH  . TYR C 1 19 ? 18.031  -41.138 15.821  1.00 50.42  ? 18  TYR C OH  1 
ATOM   1608 N N   . PRO C 1 20 ? 22.229  -34.760 12.144  1.00 36.65  ? 19  PRO C N   1 
ATOM   1609 C CA  . PRO C 1 20 ? 22.812  -33.441 11.900  1.00 37.09  ? 19  PRO C CA  1 
ATOM   1610 C C   . PRO C 1 20 ? 22.736  -32.638 13.194  1.00 36.82  ? 19  PRO C C   1 
ATOM   1611 O O   . PRO C 1 20 ? 21.938  -32.949 14.082  1.00 34.25  ? 19  PRO C O   1 
ATOM   1612 C CB  . PRO C 1 20 ? 21.859  -32.867 10.817  1.00 39.26  ? 19  PRO C CB  1 
ATOM   1613 C CG  . PRO C 1 20 ? 20.528  -33.529 11.127  1.00 38.05  ? 19  PRO C CG  1 
ATOM   1614 C CD  . PRO C 1 20 ? 20.935  -34.960 11.454  1.00 34.57  ? 19  PRO C CD  1 
ATOM   1615 N N   . HIS C 1 21 ? 23.574  -31.603 13.289  1.00 38.04  ? 20  HIS C N   1 
ATOM   1616 C CA  . HIS C 1 21 ? 23.516  -30.715 14.432  1.00 38.61  ? 20  HIS C CA  1 
ATOM   1617 C C   . HIS C 1 21 ? 22.087  -30.191 14.544  1.00 36.30  ? 20  HIS C C   1 
ATOM   1618 O O   . HIS C 1 21 ? 21.545  -29.699 13.564  1.00 39.49  ? 20  HIS C O   1 
ATOM   1619 C CB  . HIS C 1 21 ? 24.468  -29.524 14.265  1.00 38.68  ? 20  HIS C CB  1 
ATOM   1620 C CG  . HIS C 1 21 ? 25.918  -29.936 14.291  1.00 41.14  ? 20  HIS C CG  1 
ATOM   1621 N ND1 . HIS C 1 21 ? 26.571  -30.581 13.270  1.00 42.86  ? 20  HIS C ND1 1 
ATOM   1622 C CD2 . HIS C 1 21 ? 26.820  -29.791 15.268  1.00 47.06  ? 20  HIS C CD2 1 
ATOM   1623 C CE1 . HIS C 1 21 ? 27.835  -30.788 13.612  1.00 46.29  ? 20  HIS C CE1 1 
ATOM   1624 N NE2 . HIS C 1 21 ? 28.013  -30.294 14.815  1.00 41.16  ? 20  HIS C NE2 1 
ATOM   1625 N N   . TRP C 1 22 ? 21.501  -30.331 15.735  1.00 34.28  ? 21  TRP C N   1 
ATOM   1626 C CA  . TRP C 1 22 ? 20.052  -30.250 15.858  1.00 35.07  ? 21  TRP C CA  1 
ATOM   1627 C C   . TRP C 1 22 ? 19.674  -29.079 16.755  1.00 36.47  ? 21  TRP C C   1 
ATOM   1628 O O   . TRP C 1 22 ? 20.210  -28.926 17.849  1.00 35.05  ? 21  TRP C O   1 
ATOM   1629 C CB  . TRP C 1 22 ? 19.492  -31.551 16.453  1.00 37.05  ? 21  TRP C CB  1 
ATOM   1630 C CG  . TRP C 1 22 ? 18.034  -31.760 16.121  1.00 34.89  ? 21  TRP C CG  1 
ATOM   1631 C CD1 . TRP C 1 22 ? 16.926  -31.196 16.689  1.00 37.97  ? 21  TRP C CD1 1 
ATOM   1632 C CD2 . TRP C 1 22 ? 17.550  -32.626 15.069  1.00 36.79  ? 21  TRP C CD2 1 
ATOM   1633 N NE1 . TRP C 1 22 ? 15.787  -31.650 16.051  1.00 39.68  ? 21  TRP C NE1 1 
ATOM   1634 C CE2 . TRP C 1 22 ? 16.138  -32.521 15.054  1.00 35.66  ? 21  TRP C CE2 1 
ATOM   1635 C CE3 . TRP C 1 22 ? 18.176  -33.473 14.154  1.00 34.87  ? 21  TRP C CE3 1 
ATOM   1636 C CZ2 . TRP C 1 22 ? 15.353  -33.251 14.151  1.00 38.12  ? 21  TRP C CZ2 1 
ATOM   1637 C CZ3 . TRP C 1 22 ? 17.403  -34.196 13.264  1.00 41.25  ? 21  TRP C CZ3 1 
ATOM   1638 C CH2 . TRP C 1 22 ? 16.011  -34.099 13.280  1.00 35.14  ? 21  TRP C CH2 1 
ATOM   1639 N N   . PRO C 1 23 ? 18.662  -28.258 16.394  1.00 39.66  ? 22  PRO C N   1 
ATOM   1640 C CA  . PRO C 1 23 ? 18.262  -27.166 17.283  1.00 35.98  ? 22  PRO C CA  1 
ATOM   1641 C C   . PRO C 1 23 ? 17.687  -27.683 18.597  1.00 35.08  ? 22  PRO C C   1 
ATOM   1642 O O   . PRO C 1 23 ? 16.826  -28.557 18.597  1.00 36.51  ? 22  PRO C O   1 
ATOM   1643 C CB  . PRO C 1 23 ? 17.225  -26.434 16.413  1.00 38.59  ? 22  PRO C CB  1 
ATOM   1644 C CG  . PRO C 1 23 ? 16.679  -27.506 15.492  1.00 36.83  ? 22  PRO C CG  1 
ATOM   1645 C CD  . PRO C 1 23 ? 17.939  -28.270 15.103  1.00 39.09  ? 22  PRO C CD  1 
ATOM   1646 N N   . ALA C 1 24 ? 18.188  -27.138 19.719  1.00 39.46  ? 23  ALA C N   1 
ATOM   1647 C CA  . ALA C 1 24 ? 17.878  -27.719 21.022  1.00 42.37  ? 23  ALA C CA  1 
ATOM   1648 C C   . ALA C 1 24 ? 17.972  -26.668 22.136  1.00 44.25  ? 23  ALA C C   1 
ATOM   1649 O O   . ALA C 1 24 ? 18.411  -25.543 21.911  1.00 44.95  ? 23  ALA C O   1 
ATOM   1650 C CB  . ALA C 1 24 ? 18.842  -28.887 21.265  1.00 38.20  ? 23  ALA C CB  1 
ATOM   1651 N N   . ARG C 1 25 ? 17.570  -27.054 23.350  1.00 42.84  ? 24  ARG C N   1 
ATOM   1652 C CA  . ARG C 1 25 ? 17.871  -26.261 24.534  1.00 41.32  ? 24  ARG C CA  1 
ATOM   1653 C C   . ARG C 1 25 ? 18.391  -27.175 25.653  1.00 47.24  ? 24  ARG C C   1 
ATOM   1654 O O   . ARG C 1 25 ? 18.191  -28.390 25.621  1.00 46.57  ? 24  ARG C O   1 
ATOM   1655 C CB  . ARG C 1 25 ? 16.609  -25.497 24.946  1.00 42.83  ? 24  ARG C CB  1 
ATOM   1656 C CG  . ARG C 1 25 ? 15.394  -26.279 25.411  1.00 47.76  ? 24  ARG C CG  1 
ATOM   1657 C CD  . ARG C 1 25 ? 14.342  -25.375 26.084  1.00 50.70  ? 24  ARG C CD  1 
ATOM   1658 N NE  . ARG C 1 25 ? 13.171  -26.198 26.414  1.00 55.15  ? 24  ARG C NE  1 
ATOM   1659 C CZ  . ARG C 1 25 ? 11.909  -26.003 26.062  1.00 57.23  ? 24  ARG C CZ  1 
ATOM   1660 N NH1 . ARG C 1 25 ? 11.559  -24.906 25.414  1.00 57.55  ? 24  ARG C NH1 1 
ATOM   1661 N NH2 . ARG C 1 25 ? 10.992  -26.910 26.384  1.00 52.87  ? 24  ARG C NH2 1 
ATOM   1662 N N   . ILE C 1 26 ? 19.057  -26.558 26.632  1.00 46.88  ? 25  ILE C N   1 
ATOM   1663 C CA  . ILE C 1 26 ? 19.423  -27.207 27.885  1.00 47.48  ? 25  ILE C CA  1 
ATOM   1664 C C   . ILE C 1 26 ? 18.183  -27.238 28.769  1.00 54.91  ? 25  ILE C C   1 
ATOM   1665 O O   . ILE C 1 26 ? 17.579  -26.194 28.992  1.00 59.43  ? 25  ILE C O   1 
ATOM   1666 C CB  . ILE C 1 26 ? 20.559  -26.427 28.577  1.00 51.25  ? 25  ILE C CB  1 
ATOM   1667 C CG1 . ILE C 1 26 ? 21.697  -26.059 27.637  1.00 51.81  ? 25  ILE C CG1 1 
ATOM   1668 C CG2 . ILE C 1 26 ? 21.062  -27.168 29.822  1.00 53.48  ? 25  ILE C CG2 1 
ATOM   1669 C CD1 . ILE C 1 26 ? 22.551  -27.216 27.159  1.00 51.27  ? 25  ILE C CD1 1 
ATOM   1670 N N   . ASP C 1 27 ? 17.798  -28.441 29.216  1.00 50.33  ? 26  ASP C N   1 
ATOM   1671 C CA  . ASP C 1 27 ? 16.694  -28.650 30.146  1.00 57.78  ? 26  ASP C CA  1 
ATOM   1672 C C   . ASP C 1 27 ? 17.156  -28.498 31.599  1.00 54.44  ? 26  ASP C C   1 
ATOM   1673 O O   . ASP C 1 27 ? 18.261  -27.959 31.794  1.00 62.15  ? 26  ASP C O   1 
ATOM   1674 C CB  . ASP C 1 27 ? 16.076  -30.029 30.003  1.00 57.59  ? 26  ASP C CB  1 
ATOM   1675 C CG  . ASP C 1 27 ? 14.767  -30.089 29.235  1.00 66.38  ? 26  ASP C CG  1 
ATOM   1676 O OD1 . ASP C 1 27 ? 14.433  -29.066 28.600  1.00 65.96  ? 26  ASP C OD1 1 
ATOM   1677 O OD2 . ASP C 1 27 ? 14.085  -31.142 29.321  1.00 60.49  ? 26  ASP C OD2 1 
ATOM   1678 N N   . PRO C 1 36 ? 21.474  -38.113 35.684  1.00 60.29  ? 35  PRO C N   1 
ATOM   1679 C CA  . PRO C 1 36 ? 22.377  -37.621 34.650  1.00 58.61  ? 35  PRO C CA  1 
ATOM   1680 C C   . PRO C 1 36 ? 23.727  -38.332 34.775  1.00 61.91  ? 35  PRO C C   1 
ATOM   1681 O O   . PRO C 1 36 ? 24.247  -38.506 35.875  1.00 56.78  ? 35  PRO C O   1 
ATOM   1682 C CB  . PRO C 1 36 ? 22.465  -36.105 34.856  1.00 56.67  ? 35  PRO C CB  1 
ATOM   1683 C CG  . PRO C 1 36 ? 21.807  -35.844 36.205  1.00 62.54  ? 35  PRO C CG  1 
ATOM   1684 C CD  . PRO C 1 36 ? 21.376  -37.171 36.798  1.00 65.76  ? 35  PRO C CD  1 
ATOM   1685 N N   . PRO C 1 37 ? 24.311  -38.838 33.667  1.00 57.89  ? 36  PRO C N   1 
ATOM   1686 C CA  . PRO C 1 37 ? 25.658  -39.403 33.714  1.00 52.38  ? 36  PRO C CA  1 
ATOM   1687 C C   . PRO C 1 37 ? 26.619  -38.255 33.985  1.00 54.12  ? 36  PRO C C   1 
ATOM   1688 O O   . PRO C 1 37 ? 26.305  -37.103 33.687  1.00 45.69  ? 36  PRO C O   1 
ATOM   1689 C CB  . PRO C 1 37 ? 25.829  -40.006 32.306  1.00 52.14  ? 36  PRO C CB  1 
ATOM   1690 C CG  . PRO C 1 37 ? 24.403  -40.220 31.854  1.00 50.29  ? 36  PRO C CG  1 
ATOM   1691 C CD  . PRO C 1 37 ? 23.691  -38.967 32.336  1.00 59.03  ? 36  PRO C CD  1 
ATOM   1692 N N   . PRO C 1 38 ? 27.816  -38.543 34.547  1.00 50.41  ? 37  PRO C N   1 
ATOM   1693 C CA  . PRO C 1 38 ? 28.795  -37.503 34.860  1.00 51.47  ? 37  PRO C CA  1 
ATOM   1694 C C   . PRO C 1 38 ? 29.116  -36.644 33.641  1.00 50.96  ? 37  PRO C C   1 
ATOM   1695 O O   . PRO C 1 38 ? 29.406  -37.173 32.570  1.00 52.69  ? 37  PRO C O   1 
ATOM   1696 C CB  . PRO C 1 38 ? 30.033  -38.320 35.313  1.00 52.51  ? 37  PRO C CB  1 
ATOM   1697 C CG  . PRO C 1 38 ? 29.461  -39.639 35.763  1.00 51.71  ? 37  PRO C CG  1 
ATOM   1698 C CD  . PRO C 1 38 ? 28.307  -39.903 34.827  1.00 51.19  ? 37  PRO C CD  1 
ATOM   1699 N N   . ASN C 1 39 ? 29.006  -35.317 33.825  1.00 48.16  ? 38  ASN C N   1 
ATOM   1700 C CA  . ASN C 1 39 ? 29.437  -34.299 32.883  1.00 45.22  ? 38  ASN C CA  1 
ATOM   1701 C C   . ASN C 1 39 ? 28.529  -34.303 31.654  1.00 46.09  ? 38  ASN C C   1 
ATOM   1702 O O   . ASN C 1 39 ? 28.992  -33.966 30.566  1.00 53.31  ? 38  ASN C O   1 
ATOM   1703 C CB  . ASN C 1 39 ? 30.917  -34.419 32.525  1.00 47.47  ? 38  ASN C CB  1 
ATOM   1704 C CG  . ASN C 1 39 ? 31.511  -33.192 31.868  1.00 59.35  ? 38  ASN C CG  1 
ATOM   1705 O OD1 . ASN C 1 39 ? 31.200  -32.059 32.250  1.00 69.01  ? 38  ASN C OD1 1 
ATOM   1706 N ND2 . ASN C 1 39 ? 32.370  -33.379 30.874  1.00 60.53  ? 38  ASN C ND2 1 
ATOM   1707 N N   . LYS C 1 40 ? 27.261  -34.703 31.844  1.00 44.70  ? 39  LYS C N   1 
ATOM   1708 C CA  . LYS C 1 40 ? 26.270  -34.619 30.779  1.00 40.54  ? 39  LYS C CA  1 
ATOM   1709 C C   . LYS C 1 40 ? 25.164  -33.631 31.142  1.00 44.54  ? 39  LYS C C   1 
ATOM   1710 O O   . LYS C 1 40 ? 24.772  -33.516 32.296  1.00 45.52  ? 39  LYS C O   1 
ATOM   1711 C CB  . LYS C 1 40 ? 25.571  -35.967 30.541  1.00 40.16  ? 39  LYS C CB  1 
ATOM   1712 C CG  . LYS C 1 40 ? 26.526  -37.076 30.167  1.00 44.36  ? 39  LYS C CG  1 
ATOM   1713 C CD  . LYS C 1 40 ? 27.310  -36.890 28.877  1.00 49.04  ? 39  LYS C CD  1 
ATOM   1714 C CE  . LYS C 1 40 ? 28.060  -38.146 28.532  1.00 54.85  ? 39  LYS C CE  1 
ATOM   1715 N NZ  . LYS C 1 40 ? 28.987  -37.943 27.415  1.00 60.45  ? 39  LYS C NZ  1 
ATOM   1716 N N   . TYR C 1 41 ? 24.649  -32.943 30.119  1.00 41.20  ? 40  TYR C N   1 
ATOM   1717 C CA  . TYR C 1 41 ? 23.554  -32.003 30.271  1.00 43.94  ? 40  TYR C CA  1 
ATOM   1718 C C   . TYR C 1 41 ? 22.295  -32.664 29.751  1.00 44.04  ? 40  TYR C C   1 
ATOM   1719 O O   . TYR C 1 41 ? 22.365  -33.416 28.782  1.00 43.61  ? 40  TYR C O   1 
ATOM   1720 C CB  . TYR C 1 41 ? 23.687  -30.805 29.326  1.00 38.93  ? 40  TYR C CB  1 
ATOM   1721 C CG  . TYR C 1 41 ? 24.859  -29.931 29.725  1.00 39.65  ? 40  TYR C CG  1 
ATOM   1722 C CD1 . TYR C 1 41 ? 26.148  -30.185 29.257  1.00 42.95  ? 40  TYR C CD1 1 
ATOM   1723 C CD2 . TYR C 1 41 ? 24.676  -28.869 30.609  1.00 45.72  ? 40  TYR C CD2 1 
ATOM   1724 C CE1 . TYR C 1 41 ? 27.219  -29.398 29.631  1.00 49.02  ? 40  TYR C CE1 1 
ATOM   1725 C CE2 . TYR C 1 41 ? 25.749  -28.078 30.987  1.00 42.45  ? 40  TYR C CE2 1 
ATOM   1726 C CZ  . TYR C 1 41 ? 27.015  -28.343 30.506  1.00 53.60  ? 40  TYR C CZ  1 
ATOM   1727 O OH  . TYR C 1 41 ? 28.052  -27.548 30.897  1.00 65.73  ? 40  TYR C OH  1 
ATOM   1728 N N   . PRO C 1 42 ? 21.115  -32.315 30.310  1.00 46.02  ? 41  PRO C N   1 
ATOM   1729 C CA  . PRO C 1 42 ? 19.849  -32.820 29.783  1.00 43.62  ? 41  PRO C CA  1 
ATOM   1730 C C   . PRO C 1 42 ? 19.441  -31.908 28.634  1.00 46.18  ? 41  PRO C C   1 
ATOM   1731 O O   . PRO C 1 42 ? 19.362  -30.678 28.812  1.00 45.92  ? 41  PRO C O   1 
ATOM   1732 C CB  . PRO C 1 42 ? 18.871  -32.739 30.969  1.00 46.28  ? 41  PRO C CB  1 
ATOM   1733 C CG  . PRO C 1 42 ? 19.574  -31.846 31.977  1.00 42.40  ? 41  PRO C CG  1 
ATOM   1734 C CD  . PRO C 1 42 ? 20.947  -31.424 31.475  1.00 46.15  ? 41  PRO C CD  1 
ATOM   1735 N N   . ILE C 1 43 ? 19.192  -32.540 27.479  1.00 41.48  ? 42  ILE C N   1 
ATOM   1736 C CA  . ILE C 1 43 ? 18.921  -31.797 26.248  1.00 44.57  ? 42  ILE C CA  1 
ATOM   1737 C C   . ILE C 1 43 ? 17.480  -32.023 25.808  1.00 41.04  ? 42  ILE C C   1 
ATOM   1738 O O   . ILE C 1 43 ? 16.985  -33.153 25.795  1.00 45.06  ? 42  ILE C O   1 
ATOM   1739 C CB  . ILE C 1 43 ? 19.904  -32.204 25.130  1.00 41.33  ? 42  ILE C CB  1 
ATOM   1740 C CG1 . ILE C 1 43 ? 21.371  -31.970 25.534  1.00 44.69  ? 42  ILE C CG1 1 
ATOM   1741 C CG2 . ILE C 1 43 ? 19.546  -31.524 23.794  1.00 42.92  ? 42  ILE C CG2 1 
ATOM   1742 C CD1 . ILE C 1 43 ? 21.742  -30.539 25.885  1.00 43.80  ? 42  ILE C CD1 1 
ATOM   1743 N N   . PHE C 1 44 ? 16.823  -30.931 25.387  1.00 42.48  ? 43  PHE C N   1 
ATOM   1744 C CA  . PHE C 1 44 ? 15.532  -31.040 24.730  1.00 43.61  ? 43  PHE C CA  1 
ATOM   1745 C C   . PHE C 1 44 ? 15.720  -30.623 23.274  1.00 38.70  ? 43  PHE C C   1 
ATOM   1746 O O   . PHE C 1 44 ? 16.356  -29.594 23.014  1.00 40.10  ? 43  PHE C O   1 
ATOM   1747 C CB  . PHE C 1 44 ? 14.583  -30.029 25.382  1.00 49.31  ? 43  PHE C CB  1 
ATOM   1748 C CG  . PHE C 1 44 ? 13.197  -29.980 24.754  1.00 46.50  ? 43  PHE C CG  1 
ATOM   1749 C CD1 . PHE C 1 44 ? 12.252  -30.958 25.037  1.00 46.81  ? 43  PHE C CD1 1 
ATOM   1750 C CD2 . PHE C 1 44 ? 12.849  -28.950 23.877  1.00 50.19  ? 43  PHE C CD2 1 
ATOM   1751 C CE1 . PHE C 1 44 ? 10.990  -30.918 24.445  1.00 53.71  ? 43  PHE C CE1 1 
ATOM   1752 C CE2 . PHE C 1 44 ? 11.589  -28.911 23.292  1.00 46.40  ? 43  PHE C CE2 1 
ATOM   1753 C CZ  . PHE C 1 44 ? 10.662  -29.887 23.586  1.00 50.14  ? 43  PHE C CZ  1 
ATOM   1754 N N   . PHE C 1 45 ? 15.208  -31.460 22.375  1.00 39.95  ? 44  PHE C N   1 
ATOM   1755 C CA  . PHE C 1 45 ? 15.365  -31.279 20.938  1.00 44.48  ? 44  PHE C CA  1 
ATOM   1756 C C   . PHE C 1 45 ? 14.102  -30.639 20.373  1.00 41.38  ? 44  PHE C C   1 
ATOM   1757 O O   . PHE C 1 45 ? 13.008  -31.194 20.482  1.00 42.85  ? 44  PHE C O   1 
ATOM   1758 C CB  . PHE C 1 45 ? 15.715  -32.595 20.242  1.00 37.98  ? 44  PHE C CB  1 
ATOM   1759 C CG  . PHE C 1 45 ? 17.105  -33.137 20.547  1.00 38.67  ? 44  PHE C CG  1 
ATOM   1760 C CD1 . PHE C 1 45 ? 18.216  -32.714 19.822  1.00 37.06  ? 44  PHE C CD1 1 
ATOM   1761 C CD2 . PHE C 1 45 ? 17.301  -34.083 21.552  1.00 41.06  ? 44  PHE C CD2 1 
ATOM   1762 C CE1 . PHE C 1 45 ? 19.490  -33.230 20.081  1.00 44.41  ? 44  PHE C CE1 1 
ATOM   1763 C CE2 . PHE C 1 45 ? 18.575  -34.589 21.807  1.00 39.86  ? 44  PHE C CE2 1 
ATOM   1764 C CZ  . PHE C 1 45 ? 19.670  -34.151 21.093  1.00 42.98  ? 44  PHE C CZ  1 
ATOM   1765 N N   . PHE C 1 46 ? 14.282  -29.490 19.706  1.00 40.05  ? 45  PHE C N   1 
ATOM   1766 C CA  . PHE C 1 46 ? 13.145  -28.865 19.039  1.00 38.45  ? 45  PHE C CA  1 
ATOM   1767 C C   . PHE C 1 46 ? 12.677  -29.739 17.879  1.00 40.09  ? 45  PHE C C   1 
ATOM   1768 O O   . PHE C 1 46 ? 13.447  -30.510 17.278  1.00 38.56  ? 45  PHE C O   1 
ATOM   1769 C CB  . PHE C 1 46 ? 13.494  -27.423 18.634  1.00 37.12  ? 45  PHE C CB  1 
ATOM   1770 C CG  . PHE C 1 46 ? 13.708  -26.473 19.802  1.00 39.41  ? 45  PHE C CG  1 
ATOM   1771 C CD1 . PHE C 1 46 ? 12.645  -26.078 20.618  1.00 42.17  ? 45  PHE C CD1 1 
ATOM   1772 C CD2 . PHE C 1 46 ? 14.969  -25.954 20.075  1.00 40.67  ? 45  PHE C CD2 1 
ATOM   1773 C CE1 . PHE C 1 46 ? 12.854  -25.217 21.688  1.00 41.50  ? 45  PHE C CE1 1 
ATOM   1774 C CE2 . PHE C 1 46 ? 15.164  -25.088 21.151  1.00 42.07  ? 45  PHE C CE2 1 
ATOM   1775 C CZ  . PHE C 1 46 ? 14.111  -24.713 21.943  1.00 39.26  ? 45  PHE C CZ  1 
ATOM   1776 N N   . GLY C 1 47 ? 11.391  -29.584 17.534  1.00 35.67  ? 46  GLY C N   1 
ATOM   1777 C CA  . GLY C 1 47 ? 10.828  -30.302 16.407  1.00 41.82  ? 46  GLY C CA  1 
ATOM   1778 C C   . GLY C 1 47 ? 10.411  -31.715 16.800  1.00 49.89  ? 46  GLY C C   1 
ATOM   1779 O O   . GLY C 1 47 ? 9.235   -32.058 16.730  1.00 46.69  ? 46  GLY C O   1 
ATOM   1780 N N   . THR C 1 48 ? 11.385  -32.547 17.199  1.00 41.96  ? 47  THR C N   1 
ATOM   1781 C CA  . THR C 1 48 ? 11.029  -33.901 17.624  1.00 44.56  ? 47  THR C CA  1 
ATOM   1782 C C   . THR C 1 48 ? 10.479  -33.868 19.047  1.00 41.70  ? 47  THR C C   1 
ATOM   1783 O O   . THR C 1 48 ? 9.698   -34.741 19.412  1.00 44.28  ? 47  THR C O   1 
ATOM   1784 C CB  . THR C 1 48 ? 12.237  -34.829 17.573  1.00 42.42  ? 47  THR C CB  1 
ATOM   1785 O OG1 . THR C 1 48 ? 13.138  -34.264 18.532  1.00 41.51  ? 47  THR C OG1 1 
ATOM   1786 C CG2 . THR C 1 48 ? 12.807  -34.979 16.175  1.00 40.99  ? 47  THR C CG2 1 
ATOM   1787 N N   . HIS C 1 49 ? 10.919  -32.891 19.833  1.00 42.40  ? 48  HIS C N   1 
ATOM   1788 C CA  . HIS C 1 49 ? 10.607  -32.790 21.254  1.00 50.08  ? 48  HIS C CA  1 
ATOM   1789 C C   . HIS C 1 49 ? 11.058  -34.038 22.023  1.00 46.22  ? 48  HIS C C   1 
ATOM   1790 O O   . HIS C 1 49 ? 10.436  -34.392 23.023  1.00 50.79  ? 48  HIS C O   1 
ATOM   1791 C CB  . HIS C 1 49 ? 9.112   -32.530 21.487  1.00 44.47  ? 48  HIS C CB  1 
ATOM   1792 C CG  . HIS C 1 49 ? 8.512   -31.438 20.653  1.00 51.70  ? 48  HIS C CG  1 
ATOM   1793 N ND1 . HIS C 1 49 ? 7.245   -31.558 20.119  1.00 56.39  ? 48  HIS C ND1 1 
ATOM   1794 C CD2 . HIS C 1 49 ? 8.967   -30.240 20.256  1.00 47.91  ? 48  HIS C CD2 1 
ATOM   1795 C CE1 . HIS C 1 49 ? 6.950   -30.466 19.431  1.00 54.17  ? 48  HIS C CE1 1 
ATOM   1796 N NE2 . HIS C 1 49 ? 7.978   -29.651 19.500  1.00 51.35  ? 48  HIS C NE2 1 
ATOM   1797 N N   . GLU C 1 50 ? 12.182  -34.636 21.611  1.00 42.54  ? 49  GLU C N   1 
ATOM   1798 C CA  . GLU C 1 50 ? 12.782  -35.741 22.343  1.00 44.61  ? 49  GLU C CA  1 
ATOM   1799 C C   . GLU C 1 50 ? 13.849  -35.209 23.303  1.00 47.44  ? 49  GLU C C   1 
ATOM   1800 O O   . GLU C 1 50 ? 14.179  -34.024 23.276  1.00 41.68  ? 49  GLU C O   1 
ATOM   1801 C CB  . GLU C 1 50 ? 13.248  -36.800 21.356  1.00 45.14  ? 49  GLU C CB  1 
ATOM   1802 C CG  . GLU C 1 50 ? 12.117  -37.431 20.542  1.00 52.82  ? 49  GLU C CG  1 
ATOM   1803 C CD  . GLU C 1 50 ? 12.772  -38.295 19.491  1.00 56.83  ? 49  GLU C CD  1 
ATOM   1804 O OE1 . GLU C 1 50 ? 14.013  -38.408 19.558  1.00 56.85  ? 49  GLU C OE1 1 
ATOM   1805 O OE2 . GLU C 1 50 ? 12.084  -38.824 18.606  1.00 63.76  ? 49  GLU C OE2 1 
ATOM   1806 N N   . THR C 1 51 ? 14.319  -36.074 24.219  1.00 51.96  ? 50  THR C N   1 
ATOM   1807 C CA  . THR C 1 51 ? 15.333  -35.691 25.197  1.00 44.73  ? 50  THR C CA  1 
ATOM   1808 C C   . THR C 1 51 ? 16.476  -36.707 25.125  1.00 41.72  ? 50  THR C C   1 
ATOM   1809 O O   . THR C 1 51 ? 16.306  -37.834 24.664  1.00 41.83  ? 50  THR C O   1 
ATOM   1810 C CB  . THR C 1 51 ? 14.771  -35.596 26.625  1.00 52.00  ? 50  THR C CB  1 
ATOM   1811 O OG1 . THR C 1 51 ? 14.189  -36.862 26.929  1.00 50.86  ? 50  THR C OG1 1 
ATOM   1812 C CG2 . THR C 1 51 ? 13.766  -34.477 26.838  1.00 52.13  ? 50  THR C CG2 1 
ATOM   1813 N N   . ALA C 1 52 ? 17.670  -36.256 25.515  1.00 41.97  ? 51  ALA C N   1 
ATOM   1814 C CA  . ALA C 1 52 ? 18.836  -37.113 25.669  1.00 44.95  ? 51  ALA C CA  1 
ATOM   1815 C C   . ALA C 1 52 ? 19.813  -36.426 26.619  1.00 49.29  ? 51  ALA C C   1 
ATOM   1816 O O   . ALA C 1 52 ? 19.607  -35.279 27.009  1.00 48.38  ? 51  ALA C O   1 
ATOM   1817 C CB  . ALA C 1 52 ? 19.483  -37.392 24.333  1.00 44.34  ? 51  ALA C CB  1 
ATOM   1818 N N   . PHE C 1 53 ? 20.902  -37.121 26.960  1.00 46.80  ? 52  PHE C N   1 
ATOM   1819 C CA  . PHE C 1 53 ? 21.975  -36.530 27.747  1.00 47.05  ? 52  PHE C CA  1 
ATOM   1820 C C   . PHE C 1 53 ? 23.177  -36.357 26.835  1.00 44.89  ? 52  PHE C C   1 
ATOM   1821 O O   . PHE C 1 53 ? 23.546  -37.304 26.146  1.00 46.24  ? 52  PHE C O   1 
ATOM   1822 C CB  . PHE C 1 53 ? 22.301  -37.480 28.913  1.00 47.98  ? 52  PHE C CB  1 
ATOM   1823 C CG  . PHE C 1 53 ? 21.295  -37.364 30.047  1.00 50.25  ? 52  PHE C CG  1 
ATOM   1824 C CD1 . PHE C 1 53 ? 21.193  -36.189 30.785  1.00 52.69  ? 52  PHE C CD1 1 
ATOM   1825 C CD2 . PHE C 1 53 ? 20.428  -38.411 30.355  1.00 66.09  ? 52  PHE C CD2 1 
ATOM   1826 C CE1 . PHE C 1 53 ? 20.258  -36.073 31.806  1.00 57.87  ? 52  PHE C CE1 1 
ATOM   1827 C CE2 . PHE C 1 53 ? 19.501  -38.292 31.383  1.00 64.30  ? 52  PHE C CE2 1 
ATOM   1828 C CZ  . PHE C 1 53 ? 19.412  -37.119 32.101  1.00 61.25  ? 52  PHE C CZ  1 
ATOM   1829 N N   . LEU C 1 54 ? 23.813  -35.173 26.857  1.00 38.29  ? 53  LEU C N   1 
ATOM   1830 C CA  . LEU C 1 54 ? 24.982  -34.966 26.004  1.00 37.65  ? 53  LEU C CA  1 
ATOM   1831 C C   . LEU C 1 54 ? 26.024  -34.173 26.781  1.00 39.91  ? 53  LEU C C   1 
ATOM   1832 O O   . LEU C 1 54 ? 25.685  -33.329 27.611  1.00 45.06  ? 53  LEU C O   1 
ATOM   1833 C CB  . LEU C 1 54 ? 24.632  -34.213 24.716  1.00 40.21  ? 53  LEU C CB  1 
ATOM   1834 C CG  . LEU C 1 54 ? 23.783  -34.956 23.676  1.00 50.41  ? 53  LEU C CG  1 
ATOM   1835 C CD1 . LEU C 1 54 ? 23.471  -33.971 22.560  1.00 47.60  ? 53  LEU C CD1 1 
ATOM   1836 C CD2 . LEU C 1 54 ? 24.529  -36.174 23.104  1.00 54.99  ? 53  LEU C CD2 1 
ATOM   1837 N N   . GLY C 1 55 ? 27.292  -34.403 26.443  1.00 42.87  ? 54  GLY C N   1 
ATOM   1838 C CA  . GLY C 1 55 ? 28.411  -33.642 26.976  1.00 44.83  ? 54  GLY C CA  1 
ATOM   1839 C C   . GLY C 1 55 ? 28.666  -32.323 26.245  1.00 50.61  ? 54  GLY C C   1 
ATOM   1840 O O   . GLY C 1 55 ? 28.136  -32.053 25.149  1.00 42.95  ? 54  GLY C O   1 
ATOM   1841 N N   . PRO C 1 56 ? 29.499  -31.452 26.858  1.00 48.55  ? 55  PRO C N   1 
ATOM   1842 C CA  . PRO C 1 56 ? 29.725  -30.097 26.368  1.00 51.47  ? 55  PRO C CA  1 
ATOM   1843 C C   . PRO C 1 56 ? 30.303  -29.995 24.962  1.00 49.32  ? 55  PRO C C   1 
ATOM   1844 O O   . PRO C 1 56 ? 30.023  -29.029 24.253  1.00 57.81  ? 55  PRO C O   1 
ATOM   1845 C CB  . PRO C 1 56 ? 30.637  -29.447 27.467  1.00 44.90  ? 55  PRO C CB  1 
ATOM   1846 C CG  . PRO C 1 56 ? 31.282  -30.616 28.155  1.00 44.07  ? 55  PRO C CG  1 
ATOM   1847 C CD  . PRO C 1 56 ? 30.228  -31.713 28.118  1.00 49.10  ? 55  PRO C CD  1 
ATOM   1848 N N   . LYS C 1 57 ? 31.059  -31.018 24.559  1.00 45.48  ? 56  LYS C N   1 
ATOM   1849 C CA  . LYS C 1 57 ? 31.709  -31.024 23.257  1.00 50.07  ? 56  LYS C CA  1 
ATOM   1850 C C   . LYS C 1 57 ? 30.670  -31.177 22.144  1.00 51.59  ? 56  LYS C C   1 
ATOM   1851 O O   . LYS C 1 57 ? 30.979  -30.944 20.978  1.00 46.22  ? 56  LYS C O   1 
ATOM   1852 C CB  . LYS C 1 57 ? 32.625  -32.247 23.136  1.00 58.88  ? 56  LYS C CB  1 
ATOM   1853 N N   . ASP C 1 58 ? 29.462  -31.622 22.512  1.00 46.24  ? 57  ASP C N   1 
ATOM   1854 C CA  . ASP C 1 58 ? 28.424  -31.920 21.529  1.00 48.04  ? 57  ASP C CA  1 
ATOM   1855 C C   . ASP C 1 58 ? 27.421  -30.778 21.404  1.00 46.57  ? 57  ASP C C   1 
ATOM   1856 O O   . ASP C 1 58 ? 26.412  -30.918 20.715  1.00 44.68  ? 57  ASP C O   1 
ATOM   1857 C CB  . ASP C 1 58 ? 27.704  -33.219 21.859  1.00 48.30  ? 57  ASP C CB  1 
ATOM   1858 C CG  . ASP C 1 58 ? 28.571  -34.469 21.892  1.00 51.02  ? 57  ASP C CG  1 
ATOM   1859 O OD1 . ASP C 1 58 ? 29.474  -34.555 21.065  1.00 51.96  ? 57  ASP C OD1 1 
ATOM   1860 O OD2 . ASP C 1 58 ? 28.279  -35.374 22.694  1.00 54.69  ? 57  ASP C OD2 1 
ATOM   1861 N N   . LEU C 1 59 ? 27.686  -29.650 22.079  1.00 40.33  ? 58  LEU C N   1 
ATOM   1862 C CA  . LEU C 1 59 ? 26.743  -28.550 22.182  1.00 47.60  ? 58  LEU C CA  1 
ATOM   1863 C C   . LEU C 1 59 ? 27.360  -27.269 21.636  1.00 49.07  ? 58  LEU C C   1 
ATOM   1864 O O   . LEU C 1 59 ? 28.553  -27.036 21.822  1.00 59.13  ? 58  LEU C O   1 
ATOM   1865 C CB  . LEU C 1 59 ? 26.390  -28.379 23.655  1.00 44.91  ? 58  LEU C CB  1 
ATOM   1866 C CG  . LEU C 1 59 ? 25.847  -29.646 24.318  1.00 45.51  ? 58  LEU C CG  1 
ATOM   1867 C CD1 . LEU C 1 59 ? 25.628  -29.478 25.802  1.00 42.71  ? 58  LEU C CD1 1 
ATOM   1868 C CD2 . LEU C 1 59 ? 24.558  -30.107 23.620  1.00 37.81  ? 58  LEU C CD2 1 
ATOM   1869 N N   . PHE C 1 60 ? 26.519  -26.450 20.990  1.00 51.07  ? 59  PHE C N   1 
ATOM   1870 C CA  . PHE C 1 60 ? 26.962  -25.240 20.300  1.00 46.94  ? 59  PHE C CA  1 
ATOM   1871 C C   . PHE C 1 60 ? 25.974  -24.119 20.623  1.00 50.24  ? 59  PHE C C   1 
ATOM   1872 O O   . PHE C 1 60 ? 24.764  -24.252 20.417  1.00 44.56  ? 59  PHE C O   1 
ATOM   1873 C CB  . PHE C 1 60 ? 27.239  -25.525 18.812  1.00 44.79  ? 59  PHE C CB  1 
ATOM   1874 C CG  . PHE C 1 60 ? 28.227  -26.661 18.540  1.00 48.89  ? 59  PHE C CG  1 
ATOM   1875 C CD1 . PHE C 1 60 ? 27.806  -27.989 18.489  1.00 46.33  ? 59  PHE C CD1 1 
ATOM   1876 C CD2 . PHE C 1 60 ? 29.583  -26.406 18.323  1.00 53.20  ? 59  PHE C CD2 1 
ATOM   1877 C CE1 . PHE C 1 60 ? 28.700  -29.029 18.282  1.00 46.30  ? 59  PHE C CE1 1 
ATOM   1878 C CE2 . PHE C 1 60 ? 30.482  -27.445 18.096  1.00 48.65  ? 59  PHE C CE2 1 
ATOM   1879 C CZ  . PHE C 1 60 ? 30.045  -28.753 18.069  1.00 55.13  ? 59  PHE C CZ  1 
ATOM   1880 N N   . PRO C 1 61 ? 26.417  -22.982 21.219  1.00 52.64  ? 60  PRO C N   1 
ATOM   1881 C CA  . PRO C 1 61 ? 25.482  -21.923 21.601  1.00 51.17  ? 60  PRO C CA  1 
ATOM   1882 C C   . PRO C 1 61 ? 24.768  -21.499 20.329  1.00 44.27  ? 60  PRO C C   1 
ATOM   1883 O O   . PRO C 1 61 ? 25.388  -21.391 19.278  1.00 51.08  ? 60  PRO C O   1 
ATOM   1884 C CB  . PRO C 1 61 ? 26.374  -20.809 22.177  1.00 51.71  ? 60  PRO C CB  1 
ATOM   1885 C CG  . PRO C 1 61 ? 27.614  -21.552 22.594  1.00 52.15  ? 60  PRO C CG  1 
ATOM   1886 C CD  . PRO C 1 61 ? 27.815  -22.634 21.534  1.00 61.18  ? 60  PRO C CD  1 
ATOM   1887 N N   . TYR C 1 62 ? 23.445  -21.334 20.441  1.00 49.75  ? 61  TYR C N   1 
ATOM   1888 C CA  . TYR C 1 62 ? 22.609  -21.122 19.273  1.00 51.44  ? 61  TYR C CA  1 
ATOM   1889 C C   . TYR C 1 62 ? 23.020  -19.855 18.519  1.00 59.57  ? 61  TYR C C   1 
ATOM   1890 O O   . TYR C 1 62 ? 23.141  -19.875 17.294  1.00 60.95  ? 61  TYR C O   1 
ATOM   1891 C CB  . TYR C 1 62 ? 21.141  -21.020 19.675  1.00 52.15  ? 61  TYR C CB  1 
ATOM   1892 C CG  . TYR C 1 62 ? 20.221  -20.623 18.529  1.00 52.30  ? 61  TYR C CG  1 
ATOM   1893 C CD1 . TYR C 1 62 ? 19.929  -21.509 17.493  1.00 48.73  ? 61  TYR C CD1 1 
ATOM   1894 C CD2 . TYR C 1 62 ? 19.627  -19.365 18.500  1.00 51.93  ? 61  TYR C CD2 1 
ATOM   1895 C CE1 . TYR C 1 62 ? 19.082  -21.150 16.454  1.00 49.97  ? 61  TYR C CE1 1 
ATOM   1896 C CE2 . TYR C 1 62 ? 18.775  -19.001 17.469  1.00 56.99  ? 61  TYR C CE2 1 
ATOM   1897 C CZ  . TYR C 1 62 ? 18.495  -19.895 16.451  1.00 51.43  ? 61  TYR C CZ  1 
ATOM   1898 O OH  . TYR C 1 62 ? 17.655  -19.513 15.439  1.00 51.53  ? 61  TYR C OH  1 
ATOM   1899 N N   . ASP C 1 63 ? 23.229  -18.752 19.243  1.00 58.33  ? 62  ASP C N   1 
ATOM   1900 C CA  . ASP C 1 63 ? 23.436  -17.484 18.554  1.00 62.05  ? 62  ASP C CA  1 
ATOM   1901 C C   . ASP C 1 63 ? 24.724  -17.529 17.737  1.00 55.12  ? 62  ASP C C   1 
ATOM   1902 O O   . ASP C 1 63 ? 24.767  -17.011 16.618  1.00 59.51  ? 62  ASP C O   1 
ATOM   1903 C CB  . ASP C 1 63 ? 23.198  -16.278 19.455  1.00 59.67  ? 62  ASP C CB  1 
ATOM   1904 C CG  . ASP C 1 63 ? 21.733  -15.917 19.668  1.00 69.34  ? 62  ASP C CG  1 
ATOM   1905 O OD1 . ASP C 1 63 ? 21.370  -15.565 20.806  1.00 64.39  ? 62  ASP C OD1 1 
ATOM   1906 O OD2 . ASP C 1 63 ? 20.955  -16.006 18.688  1.00 76.83  ? 62  ASP C OD2 1 
ATOM   1907 N N   . LYS C 1 64 ? 25.739  -18.224 18.264  1.00 53.10  ? 63  LYS C N   1 
ATOM   1908 C CA  . LYS C 1 64 ? 27.078  -18.207 17.697  1.00 53.43  ? 63  LYS C CA  1 
ATOM   1909 C C   . LYS C 1 64 ? 27.189  -19.161 16.509  1.00 52.53  ? 63  LYS C C   1 
ATOM   1910 O O   . LYS C 1 64 ? 27.986  -18.931 15.611  1.00 47.88  ? 63  LYS C O   1 
ATOM   1911 C CB  . LYS C 1 64 ? 28.147  -18.518 18.750  1.00 60.15  ? 63  LYS C CB  1 
ATOM   1912 N N   . SER C 1 65 ? 26.367  -20.221 16.470  1.00 50.60  ? 64  SER C N   1 
ATOM   1913 C CA  . SER C 1 65 ? 26.583  -21.204 15.423  1.00 45.37  ? 64  SER C CA  1 
ATOM   1914 C C   . SER C 1 65 ? 25.400  -21.304 14.457  1.00 45.96  ? 64  SER C C   1 
ATOM   1915 O O   . SER C 1 65 ? 25.477  -22.065 13.503  1.00 44.79  ? 64  SER C O   1 
ATOM   1916 C CB  . SER C 1 65 ? 26.964  -22.542 15.996  1.00 50.84  ? 64  SER C CB  1 
ATOM   1917 O OG  . SER C 1 65 ? 25.855  -23.095 16.694  1.00 47.65  ? 64  SER C OG  1 
ATOM   1918 N N   . LYS C 1 66 ? 24.334  -20.518 14.655  1.00 44.20  ? 65  LYS C N   1 
ATOM   1919 C CA  . LYS C 1 66 ? 23.191  -20.616 13.743  1.00 46.75  ? 65  LYS C CA  1 
ATOM   1920 C C   . LYS C 1 66 ? 23.555  -20.362 12.279  1.00 51.38  ? 65  LYS C C   1 
ATOM   1921 O O   . LYS C 1 66 ? 22.932  -20.915 11.379  1.00 47.60  ? 65  LYS C O   1 
ATOM   1922 C CB  . LYS C 1 66 ? 22.011  -19.748 14.168  1.00 49.61  ? 65  LYS C CB  1 
ATOM   1923 C CG  . LYS C 1 66 ? 22.320  -18.275 14.302  1.00 44.28  ? 65  LYS C CG  1 
ATOM   1924 C CD  . LYS C 1 66 ? 21.057  -17.636 14.870  1.00 56.13  ? 65  LYS C CD  1 
ATOM   1925 C CE  . LYS C 1 66 ? 21.113  -16.153 14.935  1.00 56.54  ? 65  LYS C CE  1 
ATOM   1926 N NZ  . LYS C 1 66 ? 19.713  -15.756 15.051  1.00 62.96  ? 65  LYS C NZ  1 
ATOM   1927 N N   . ASP C 1 67 ? 24.558  -19.520 12.022  1.00 49.50  ? 66  ASP C N   1 
ATOM   1928 C CA  . ASP C 1 67 ? 24.946  -19.216 10.654  1.00 48.00  ? 66  ASP C CA  1 
ATOM   1929 C C   . ASP C 1 67 ? 25.409  -20.490 9.945   1.00 50.61  ? 66  ASP C C   1 
ATOM   1930 O O   . ASP C 1 67 ? 25.136  -20.674 8.757   1.00 46.06  ? 66  ASP C O   1 
ATOM   1931 C CB  . ASP C 1 67 ? 25.864  -17.992 10.598  1.00 49.87  ? 66  ASP C CB  1 
ATOM   1932 C CG  . ASP C 1 67 ? 27.313  -18.192 11.032  1.00 65.74  ? 66  ASP C CG  1 
ATOM   1933 O OD1 . ASP C 1 67 ? 27.629  -19.278 11.581  1.00 63.30  ? 66  ASP C OD1 1 
ATOM   1934 O OD2 . ASP C 1 67 ? 28.125  -17.257 10.812  1.00 59.75  ? 66  ASP C OD2 1 
ATOM   1935 N N   . LYS C 1 68 ? 26.072  -21.391 10.696  1.00 45.87  ? 67  LYS C N   1 
ATOM   1936 C CA  . LYS C 1 68 ? 26.563  -22.652 10.166  1.00 42.02  ? 67  LYS C CA  1 
ATOM   1937 C C   . LYS C 1 68 ? 25.515  -23.780 10.248  1.00 43.02  ? 67  LYS C C   1 
ATOM   1938 O O   . LYS C 1 68 ? 25.349  -24.515 9.276   1.00 44.30  ? 67  LYS C O   1 
ATOM   1939 C CB  . LYS C 1 68 ? 27.868  -22.985 10.890  1.00 45.66  ? 67  LYS C CB  1 
ATOM   1940 C CG  . LYS C 1 68 ? 28.529  -24.309 10.533  1.00 53.60  ? 67  LYS C CG  1 
ATOM   1941 C CD  . LYS C 1 68 ? 29.849  -24.469 11.291  1.00 63.49  ? 67  LYS C CD  1 
ATOM   1942 C CE  . LYS C 1 68 ? 30.541  -25.774 11.043  1.00 75.21  ? 67  LYS C CE  1 
ATOM   1943 N NZ  . LYS C 1 68 ? 30.828  -26.029 9.629   1.00 74.88  ? 67  LYS C NZ  1 
ATOM   1944 N N   . TYR C 1 69 ? 24.794  -23.918 11.382  1.00 39.70  ? 68  TYR C N   1 
ATOM   1945 C CA  . TYR C 1 69 ? 23.962  -25.111 11.528  1.00 39.88  ? 68  TYR C CA  1 
ATOM   1946 C C   . TYR C 1 69 ? 22.477  -24.819 11.316  1.00 39.43  ? 68  TYR C C   1 
ATOM   1947 O O   . TYR C 1 69 ? 21.663  -25.746 11.218  1.00 40.67  ? 68  TYR C O   1 
ATOM   1948 C CB  . TYR C 1 69 ? 24.124  -25.713 12.931  1.00 40.96  ? 68  TYR C CB  1 
ATOM   1949 C CG  . TYR C 1 69 ? 25.550  -26.163 13.233  1.00 37.62  ? 68  TYR C CG  1 
ATOM   1950 C CD1 . TYR C 1 69 ? 26.273  -26.956 12.348  1.00 41.69  ? 68  TYR C CD1 1 
ATOM   1951 C CD2 . TYR C 1 69 ? 26.173  -25.741 14.406  1.00 41.11  ? 68  TYR C CD2 1 
ATOM   1952 C CE1 . TYR C 1 69 ? 27.576  -27.349 12.639  1.00 44.08  ? 68  TYR C CE1 1 
ATOM   1953 C CE2 . TYR C 1 69 ? 27.460  -26.147 14.712  1.00 45.92  ? 68  TYR C CE2 1 
ATOM   1954 C CZ  . TYR C 1 69 ? 28.168  -26.930 13.821  1.00 44.74  ? 68  TYR C CZ  1 
ATOM   1955 O OH  . TYR C 1 69 ? 29.451  -27.288 14.164  1.00 48.71  ? 68  TYR C OH  1 
ATOM   1956 N N   . GLY C 1 70 ? 22.105  -23.543 11.337  1.00 38.23  ? 69  GLY C N   1 
ATOM   1957 C CA  . GLY C 1 70 ? 20.684  -23.248 11.253  1.00 40.78  ? 69  GLY C CA  1 
ATOM   1958 C C   . GLY C 1 70 ? 20.320  -23.096 9.780   1.00 40.91  ? 69  GLY C C   1 
ATOM   1959 O O   . GLY C 1 70 ? 20.306  -21.979 9.278   1.00 42.33  ? 69  GLY C O   1 
ATOM   1960 N N   . LYS C 1 71 ? 20.203  -24.237 9.096   1.00 40.60  ? 70  LYS C N   1 
ATOM   1961 C CA  . LYS C 1 71 ? 19.834  -24.312 7.691   1.00 39.43  ? 70  LYS C CA  1 
ATOM   1962 C C   . LYS C 1 71 ? 18.956  -25.536 7.569   1.00 41.00  ? 70  LYS C C   1 
ATOM   1963 O O   . LYS C 1 71 ? 19.166  -26.501 8.302   1.00 40.45  ? 70  LYS C O   1 
ATOM   1964 C CB  . LYS C 1 71 ? 21.063  -24.510 6.791   1.00 44.63  ? 70  LYS C CB  1 
ATOM   1965 C CG  . LYS C 1 71 ? 22.069  -25.477 7.343   1.00 43.83  ? 70  LYS C CG  1 
ATOM   1966 C CD  . LYS C 1 71 ? 23.179  -25.990 6.437   1.00 53.89  ? 70  LYS C CD  1 
ATOM   1967 C CE  . LYS C 1 71 ? 24.107  -26.760 7.310   1.00 53.61  ? 70  LYS C CE  1 
ATOM   1968 N N   . PRO C 1 72 ? 17.943  -25.526 6.670   1.00 37.00  ? 71  PRO C N   1 
ATOM   1969 C CA  . PRO C 1 72 ? 17.017  -26.652 6.579   1.00 33.61  ? 71  PRO C CA  1 
ATOM   1970 C C   . PRO C 1 72 ? 17.696  -27.975 6.243   1.00 40.16  ? 71  PRO C C   1 
ATOM   1971 O O   . PRO C 1 72 ? 18.760  -28.023 5.623   1.00 40.59  ? 71  PRO C O   1 
ATOM   1972 C CB  . PRO C 1 72 ? 16.020  -26.221 5.471   1.00 34.23  ? 71  PRO C CB  1 
ATOM   1973 C CG  . PRO C 1 72 ? 16.112  -24.710 5.498   1.00 37.60  ? 71  PRO C CG  1 
ATOM   1974 C CD  . PRO C 1 72 ? 17.593  -24.392 5.790   1.00 37.55  ? 71  PRO C CD  1 
ATOM   1975 N N   . ASN C 1 73 ? 17.056  -29.049 6.678   1.00 40.06  ? 72  ASN C N   1 
ATOM   1976 C CA  . ASN C 1 73 ? 17.336  -30.313 6.038   1.00 46.62  ? 72  ASN C CA  1 
ATOM   1977 C C   . ASN C 1 73 ? 16.104  -31.193 6.174   1.00 39.70  ? 72  ASN C C   1 
ATOM   1978 O O   . ASN C 1 73 ? 15.142  -30.840 6.855   1.00 40.08  ? 72  ASN C O   1 
ATOM   1979 C CB  . ASN C 1 73 ? 18.703  -30.893 6.391   1.00 48.78  ? 72  ASN C CB  1 
ATOM   1980 C CG  . ASN C 1 73 ? 18.715  -31.615 7.714   1.00 51.80  ? 72  ASN C CG  1 
ATOM   1981 O OD1 . ASN C 1 73 ? 18.368  -32.806 7.796   1.00 46.17  ? 72  ASN C OD1 1 
ATOM   1982 N ND2 . ASN C 1 73 ? 19.179  -30.914 8.730   1.00 52.69  ? 72  ASN C ND2 1 
ATOM   1983 N N   . LYS C 1 74 ? 16.192  -32.365 5.574   1.00 38.98  ? 73  LYS C N   1 
ATOM   1984 C CA  . LYS C 1 74 ? 14.999  -33.168 5.339   1.00 39.14  ? 73  LYS C CA  1 
ATOM   1985 C C   . LYS C 1 74 ? 14.690  -34.100 6.504   1.00 41.60  ? 73  LYS C C   1 
ATOM   1986 O O   . LYS C 1 74 ? 13.654  -34.780 6.497   1.00 41.70  ? 73  LYS C O   1 
ATOM   1987 C CB  . LYS C 1 74 ? 15.171  -33.940 4.025   1.00 43.67  ? 73  LYS C CB  1 
ATOM   1988 C CG  . LYS C 1 74 ? 15.478  -33.043 2.828   1.00 50.22  ? 73  LYS C CG  1 
ATOM   1989 C CD  . LYS C 1 74 ? 14.200  -32.305 2.460   1.00 52.76  ? 73  LYS C CD  1 
ATOM   1990 N N   . ARG C 1 75 ? 15.583  -34.176 7.507   1.00 40.05  ? 74  ARG C N   1 
ATOM   1991 C CA  . ARG C 1 75 ? 15.339  -35.146 8.574   1.00 37.96  ? 74  ARG C CA  1 
ATOM   1992 C C   . ARG C 1 75 ? 14.042  -34.808 9.309   1.00 40.65  ? 74  ARG C C   1 
ATOM   1993 O O   . ARG C 1 75 ? 13.721  -33.643 9.523   1.00 42.09  ? 74  ARG C O   1 
ATOM   1994 C CB  . ARG C 1 75 ? 16.513  -35.192 9.572   1.00 42.69  ? 74  ARG C CB  1 
ATOM   1995 C CG  . ARG C 1 75 ? 17.906  -35.387 8.985   1.00 49.16  ? 74  ARG C CG  1 
ATOM   1996 C CD  . ARG C 1 75 ? 18.328  -36.738 8.361   1.00 50.86  ? 74  ARG C CD  1 
ATOM   1997 N NE  . ARG C 1 75 ? 18.295  -37.756 9.411   1.00 45.47  ? 74  ARG C NE  1 
ATOM   1998 C CZ  . ARG C 1 75 ? 19.398  -38.211 10.010  1.00 37.11  ? 74  ARG C CZ  1 
ATOM   1999 N NH1 . ARG C 1 75 ? 19.277  -38.730 11.203  1.00 42.12  ? 74  ARG C NH1 1 
ATOM   2000 N NH2 . ARG C 1 75 ? 20.586  -37.992 9.478   1.00 41.81  ? 74  ARG C NH2 1 
ATOM   2001 N N   . LYS C 1 76 ? 13.343  -35.857 9.758   1.00 41.73  ? 75  LYS C N   1 
ATOM   2002 C CA  . LYS C 1 76 ? 12.041  -35.753 10.397  1.00 49.13  ? 75  LYS C CA  1 
ATOM   2003 C C   . LYS C 1 76 ? 12.102  -34.776 11.567  1.00 45.09  ? 75  LYS C C   1 
ATOM   2004 O O   . LYS C 1 76 ? 12.926  -34.921 12.478  1.00 40.16  ? 75  LYS C O   1 
ATOM   2005 C CB  . LYS C 1 76 ? 11.478  -37.139 10.754  1.00 42.84  ? 75  LYS C CB  1 
ATOM   2006 C CG  . LYS C 1 76 ? 9.972   -37.160 10.992  1.00 52.08  ? 75  LYS C CG  1 
ATOM   2007 C CD  . LYS C 1 76 ? 9.467   -38.485 11.558  1.00 63.03  ? 75  LYS C CD  1 
ATOM   2008 N N   . GLY C 1 77 ? 11.239  -33.753 11.510  1.00 43.72  ? 76  GLY C N   1 
ATOM   2009 C CA  . GLY C 1 77 ? 11.048  -32.828 12.617  1.00 38.97  ? 76  GLY C CA  1 
ATOM   2010 C C   . GLY C 1 77 ? 12.052  -31.671 12.644  1.00 37.06  ? 76  GLY C C   1 
ATOM   2011 O O   . GLY C 1 77 ? 11.879  -30.754 13.431  1.00 41.21  ? 76  GLY C O   1 
ATOM   2012 N N   . PHE C 1 78 ? 13.054  -31.676 11.752  1.00 34.88  ? 77  PHE C N   1 
ATOM   2013 C CA  . PHE C 1 78 ? 14.158  -30.727 11.836  1.00 33.05  ? 77  PHE C CA  1 
ATOM   2014 C C   . PHE C 1 78 ? 13.711  -29.282 11.552  1.00 39.74  ? 77  PHE C C   1 
ATOM   2015 O O   . PHE C 1 78 ? 14.135  -28.331 12.213  1.00 39.32  ? 77  PHE C O   1 
ATOM   2016 C CB  . PHE C 1 78 ? 15.265  -31.120 10.852  1.00 38.04  ? 77  PHE C CB  1 
ATOM   2017 C CG  . PHE C 1 78 ? 16.530  -30.318 11.107  1.00 38.74  ? 77  PHE C CG  1 
ATOM   2018 C CD1 . PHE C 1 78 ? 16.689  -29.039 10.589  1.00 38.53  ? 77  PHE C CD1 1 
ATOM   2019 C CD2 . PHE C 1 78 ? 17.573  -30.857 11.856  1.00 34.84  ? 77  PHE C CD2 1 
ATOM   2020 C CE1 . PHE C 1 78 ? 17.848  -28.309 10.818  1.00 37.29  ? 77  PHE C CE1 1 
ATOM   2021 C CE2 . PHE C 1 78 ? 18.730  -30.121 12.100  1.00 38.65  ? 77  PHE C CE2 1 
ATOM   2022 C CZ  . PHE C 1 78 ? 18.876  -28.854 11.582  1.00 42.34  ? 77  PHE C CZ  1 
ATOM   2023 N N   . ASN C 1 79 ? 12.932  -29.103 10.480  1.00 37.08  ? 78  ASN C N   1 
ATOM   2024 C CA  . ASN C 1 79 ? 12.568  -27.762 10.044  1.00 38.48  ? 78  ASN C CA  1 
ATOM   2025 C C   . ASN C 1 79 ? 11.553  -27.136 10.994  1.00 41.18  ? 78  ASN C C   1 
ATOM   2026 O O   . ASN C 1 79 ? 11.624  -25.948 11.275  1.00 38.45  ? 78  ASN C O   1 
ATOM   2027 C CB  . ASN C 1 79 ? 12.140  -27.733 8.587   1.00 36.12  ? 78  ASN C CB  1 
ATOM   2028 C CG  . ASN C 1 79 ? 13.269  -28.167 7.688   1.00 37.96  ? 78  ASN C CG  1 
ATOM   2029 O OD1 . ASN C 1 79 ? 14.428  -27.891 8.001   1.00 36.97  ? 78  ASN C OD1 1 
ATOM   2030 N ND2 . ASN C 1 79 ? 12.951  -28.838 6.594   1.00 39.12  ? 78  ASN C ND2 1 
ATOM   2031 N N   . GLU C 1 80 ? 10.632  -27.947 11.519  1.00 42.43  ? 79  GLU C N   1 
ATOM   2032 C CA  . GLU C 1 80 ? 9.761   -27.480 12.590  1.00 38.32  ? 79  GLU C CA  1 
ATOM   2033 C C   . GLU C 1 80 ? 10.637  -27.103 13.788  1.00 46.90  ? 79  GLU C C   1 
ATOM   2034 O O   . GLU C 1 80 ? 10.390  -26.091 14.438  1.00 45.03  ? 79  GLU C O   1 
ATOM   2035 C CB  . GLU C 1 80 ? 8.656   -28.516 12.843  1.00 39.76  ? 79  GLU C CB  1 
ATOM   2036 C CG  . GLU C 1 80 ? 7.673   -28.126 13.943  1.00 38.50  ? 79  GLU C CG  1 
ATOM   2037 C CD  . GLU C 1 80 ? 6.407   -28.951 14.110  1.00 50.69  ? 79  GLU C CD  1 
ATOM   2038 O OE1 . GLU C 1 80 ? 6.329   -30.107 13.641  1.00 56.39  ? 79  GLU C OE1 1 
ATOM   2039 O OE2 . GLU C 1 80 ? 5.465   -28.399 14.703  1.00 54.03  ? 79  GLU C OE2 1 
ATOM   2040 N N   . GLY C 1 81 ? 11.696  -27.899 14.072  1.00 37.93  ? 80  GLY C N   1 
ATOM   2041 C CA  . GLY C 1 81 ? 12.576  -27.505 15.170  1.00 37.19  ? 80  GLY C CA  1 
ATOM   2042 C C   . GLY C 1 81 ? 13.237  -26.145 14.931  1.00 39.67  ? 80  GLY C C   1 
ATOM   2043 O O   . GLY C 1 81 ? 13.463  -25.392 15.875  1.00 38.38  ? 80  GLY C O   1 
ATOM   2044 N N   . LEU C 1 82 ? 13.583  -25.854 13.665  1.00 39.52  ? 81  LEU C N   1 
ATOM   2045 C CA  . LEU C 1 82 ? 14.236  -24.589 13.329  1.00 40.41  ? 81  LEU C CA  1 
ATOM   2046 C C   . LEU C 1 82 ? 13.243  -23.451 13.576  1.00 38.36  ? 81  LEU C C   1 
ATOM   2047 O O   . LEU C 1 82 ? 13.627  -22.374 14.055  1.00 40.52  ? 81  LEU C O   1 
ATOM   2048 C CB  . LEU C 1 82 ? 14.665  -24.561 11.860  1.00 40.66  ? 81  LEU C CB  1 
ATOM   2049 C CG  . LEU C 1 82 ? 15.936  -25.331 11.484  1.00 38.74  ? 81  LEU C CG  1 
ATOM   2050 C CD1 . LEU C 1 82 ? 16.159  -25.147 9.993   1.00 39.36  ? 81  LEU C CD1 1 
ATOM   2051 C CD2 . LEU C 1 82 ? 17.180  -24.892 12.232  1.00 34.65  ? 81  LEU C CD2 1 
ATOM   2052 N N   . TRP C 1 83 ? 11.977  -23.716 13.246  1.00 38.66  ? 82  TRP C N   1 
ATOM   2053 C CA  . TRP C 1 83 ? 10.945  -22.719 13.500  1.00 48.45  ? 82  TRP C CA  1 
ATOM   2054 C C   . TRP C 1 83 ? 10.843  -22.435 15.009  1.00 50.50  ? 82  TRP C C   1 
ATOM   2055 O O   . TRP C 1 83 ? 10.846  -21.276 15.433  1.00 48.71  ? 82  TRP C O   1 
ATOM   2056 C CB  . TRP C 1 83 ? 9.593   -23.138 12.900  1.00 43.43  ? 82  TRP C CB  1 
ATOM   2057 C CG  . TRP C 1 83 ? 8.594   -22.014 12.996  1.00 52.20  ? 82  TRP C CG  1 
ATOM   2058 C CD1 . TRP C 1 83 ? 8.409   -21.013 12.086  1.00 56.72  ? 82  TRP C CD1 1 
ATOM   2059 C CD2 . TRP C 1 83 ? 7.700   -21.727 14.095  1.00 50.46  ? 82  TRP C CD2 1 
ATOM   2060 N NE1 . TRP C 1 83 ? 7.446   -20.142 12.524  1.00 50.72  ? 82  TRP C NE1 1 
ATOM   2061 C CE2 . TRP C 1 83 ? 6.988   -20.551 13.746  1.00 54.47  ? 82  TRP C CE2 1 
ATOM   2062 C CE3 . TRP C 1 83 ? 7.421   -22.351 15.321  1.00 45.26  ? 82  TRP C CE3 1 
ATOM   2063 C CZ2 . TRP C 1 83 ? 6.023   -19.987 14.582  1.00 49.90  ? 82  TRP C CZ2 1 
ATOM   2064 C CZ3 . TRP C 1 83 ? 6.456   -21.796 16.141  1.00 52.23  ? 82  TRP C CZ3 1 
ATOM   2065 C CH2 . TRP C 1 83 ? 5.790   -20.619 15.787  1.00 53.98  ? 82  TRP C CH2 1 
ATOM   2066 N N   . GLU C 1 84 ? 10.834  -23.503 15.818  1.00 46.60  ? 83  GLU C N   1 
ATOM   2067 C CA  . GLU C 1 84 ? 10.668  -23.400 17.267  1.00 45.74  ? 83  GLU C CA  1 
ATOM   2068 C C   . GLU C 1 84 ? 11.792  -22.593 17.926  1.00 44.00  ? 83  GLU C C   1 
ATOM   2069 O O   . GLU C 1 84 ? 11.518  -21.700 18.737  1.00 50.82  ? 83  GLU C O   1 
ATOM   2070 C CB  . GLU C 1 84 ? 10.514  -24.766 17.941  1.00 42.80  ? 83  GLU C CB  1 
ATOM   2071 C CG  . GLU C 1 84 ? 9.202   -25.455 17.579  1.00 41.40  ? 83  GLU C CG  1 
ATOM   2072 C CD  . GLU C 1 84 ? 9.122   -26.901 18.016  1.00 48.40  ? 83  GLU C CD  1 
ATOM   2073 O OE1 . GLU C 1 84 ? 10.133  -27.452 18.514  1.00 47.11  ? 83  GLU C OE1 1 
ATOM   2074 O OE2 . GLU C 1 84 ? 8.042   -27.479 17.860  1.00 48.36  ? 83  GLU C OE2 1 
ATOM   2075 N N   . ILE C 1 85 ? 13.050  -22.864 17.557  1.00 41.33  ? 84  ILE C N   1 
ATOM   2076 C CA  . ILE C 1 85 ? 14.207  -22.265 18.219  1.00 43.12  ? 84  ILE C CA  1 
ATOM   2077 C C   . ILE C 1 85 ? 14.322  -20.753 17.975  1.00 43.68  ? 84  ILE C C   1 
ATOM   2078 O O   . ILE C 1 85 ? 14.822  -20.032 18.831  1.00 42.08  ? 84  ILE C O   1 
ATOM   2079 C CB  . ILE C 1 85 ? 15.505  -22.997 17.857  1.00 39.97  ? 84  ILE C CB  1 
ATOM   2080 C CG1 . ILE C 1 85 ? 16.601  -22.665 18.863  1.00 41.02  ? 84  ILE C CG1 1 
ATOM   2081 C CG2 . ILE C 1 85 ? 15.930  -22.735 16.396  1.00 39.06  ? 84  ILE C CG2 1 
ATOM   2082 C CD1 . ILE C 1 85 ? 17.736  -23.672 18.966  1.00 42.52  ? 84  ILE C CD1 1 
ATOM   2083 N N   . GLN C 1 86 ? 13.915  -20.300 16.783  1.00 41.41  ? 85  GLN C N   1 
ATOM   2084 C CA  . GLN C 1 86 ? 13.940  -18.894 16.415  1.00 45.52  ? 85  GLN C CA  1 
ATOM   2085 C C   . GLN C 1 86 ? 12.666  -18.174 16.861  1.00 43.06  ? 85  GLN C C   1 
ATOM   2086 O O   . GLN C 1 86 ? 12.727  -16.985 17.188  1.00 49.44  ? 85  GLN C O   1 
ATOM   2087 C CB  . GLN C 1 86 ? 14.094  -18.791 14.895  1.00 41.42  ? 85  GLN C CB  1 
ATOM   2088 C CG  . GLN C 1 86 ? 14.212  -17.363 14.359  1.00 43.05  ? 85  GLN C CG  1 
ATOM   2089 C CD  . GLN C 1 86 ? 14.608  -17.337 12.898  1.00 48.62  ? 85  GLN C CD  1 
ATOM   2090 O OE1 . GLN C 1 86 ? 14.483  -18.335 12.174  1.00 45.77  ? 85  GLN C OE1 1 
ATOM   2091 N NE2 . GLN C 1 86 ? 15.178  -16.224 12.463  1.00 49.37  ? 85  GLN C NE2 1 
ATOM   2092 N N   . ASN C 1 87 ? 11.529  -18.876 16.888  1.00 46.01  ? 86  ASN C N   1 
ATOM   2093 C CA  . ASN C 1 87 ? 10.244  -18.198 17.009  1.00 49.31  ? 86  ASN C CA  1 
ATOM   2094 C C   . ASN C 1 87 ? 9.549   -18.485 18.342  1.00 58.27  ? 86  ASN C C   1 
ATOM   2095 O O   . ASN C 1 87 ? 8.769   -17.663 18.796  1.00 57.74  ? 86  ASN C O   1 
ATOM   2096 C CB  . ASN C 1 87 ? 9.311   -18.475 15.837  1.00 45.82  ? 86  ASN C CB  1 
ATOM   2097 C CG  . ASN C 1 87 ? 9.878   -17.853 14.589  1.00 52.46  ? 86  ASN C CG  1 
ATOM   2098 O OD1 . ASN C 1 87 ? 9.938   -16.622 14.497  1.00 53.50  ? 86  ASN C OD1 1 
ATOM   2099 N ND2 . ASN C 1 87 ? 10.349  -18.675 13.659  1.00 42.85  ? 86  ASN C ND2 1 
ATOM   2100 N N   . ASN C 1 88 ? 9.776   -19.655 18.946  1.00 54.38  ? 87  ASN C N   1 
ATOM   2101 C CA  . ASN C 1 88 ? 9.066   -19.979 20.178  1.00 53.65  ? 87  ASN C CA  1 
ATOM   2102 C C   . ASN C 1 88 ? 9.935   -20.864 21.073  1.00 49.01  ? 87  ASN C C   1 
ATOM   2103 O O   . ASN C 1 88 ? 9.514   -21.961 21.440  1.00 53.77  ? 87  ASN C O   1 
ATOM   2104 C CB  . ASN C 1 88 ? 7.734   -20.655 19.880  1.00 53.57  ? 87  ASN C CB  1 
ATOM   2105 C CG  . ASN C 1 88 ? 6.798   -20.654 21.066  1.00 61.12  ? 87  ASN C CG  1 
ATOM   2106 O OD1 . ASN C 1 88 ? 7.016   -19.924 22.042  1.00 60.92  ? 87  ASN C OD1 1 
ATOM   2107 N ND2 . ASN C 1 88 ? 5.754   -21.464 20.991  1.00 56.19  ? 87  ASN C ND2 1 
ATOM   2108 N N   . PRO C 1 89 ? 11.168  -20.435 21.412  1.00 46.71  ? 88  PRO C N   1 
ATOM   2109 C CA  . PRO C 1 89 ? 12.154  -21.332 22.014  1.00 54.90  ? 88  PRO C CA  1 
ATOM   2110 C C   . PRO C 1 89 ? 11.881  -21.783 23.449  1.00 58.66  ? 88  PRO C C   1 
ATOM   2111 O O   . PRO C 1 89 ? 12.392  -22.814 23.879  1.00 51.36  ? 88  PRO C O   1 
ATOM   2112 C CB  . PRO C 1 89 ? 13.456  -20.521 21.896  1.00 57.06  ? 88  PRO C CB  1 
ATOM   2113 C CG  . PRO C 1 89 ? 12.993  -19.075 21.981  1.00 54.53  ? 88  PRO C CG  1 
ATOM   2114 C CD  . PRO C 1 89 ? 11.724  -19.099 21.147  1.00 47.66  ? 88  PRO C CD  1 
ATOM   2115 N N   . HIS C 1 90 ? 11.066  -21.025 24.186  1.00 60.68  ? 89  HIS C N   1 
ATOM   2116 C CA  . HIS C 1 90 ? 10.885  -21.351 25.594  1.00 61.49  ? 89  HIS C CA  1 
ATOM   2117 C C   . HIS C 1 90 ? 9.421   -21.687 25.876  1.00 62.14  ? 89  HIS C C   1 
ATOM   2118 O O   . HIS C 1 90 ? 8.934   -21.439 26.974  1.00 70.10  ? 89  HIS C O   1 
ATOM   2119 C CB  . HIS C 1 90 ? 11.468  -20.274 26.517  1.00 48.37  ? 89  HIS C CB  1 
ATOM   2120 C CG  . HIS C 1 90 ? 12.858  -19.761 26.239  1.00 50.20  ? 89  HIS C CG  1 
ATOM   2121 N ND1 . HIS C 1 90 ? 14.014  -20.464 26.515  1.00 50.87  ? 89  HIS C ND1 1 
ATOM   2122 C CD2 . HIS C 1 90 ? 13.270  -18.583 25.748  1.00 50.21  ? 89  HIS C CD2 1 
ATOM   2123 C CE1 . HIS C 1 90 ? 15.080  -19.727 26.193  1.00 48.43  ? 89  HIS C CE1 1 
ATOM   2124 N NE2 . HIS C 1 90 ? 14.653  -18.580 25.712  1.00 51.07  ? 89  HIS C NE2 1 
ATOM   2125 N N   . ALA C 1 91 ? 8.727   -22.250 24.878  1.00 66.56  ? 90  ALA C N   1 
ATOM   2126 C CA  . ALA C 1 91 ? 7.403   -22.823 25.073  1.00 61.35  ? 90  ALA C CA  1 
ATOM   2127 C C   . ALA C 1 91 ? 7.523   -24.256 25.597  1.00 65.24  ? 90  ALA C C   1 
ATOM   2128 O O   . ALA C 1 91 ? 8.614   -24.828 25.607  1.00 70.05  ? 90  ALA C O   1 
ATOM   2129 C CB  . ALA C 1 91 ? 6.595   -22.767 23.791  1.00 56.25  ? 90  ALA C CB  1 
ATOM   2130 N N   . SER C 1 92 ? 6.374   -24.835 25.979  1.00 69.47  ? 91  SER C N   1 
ATOM   2131 C CA  . SER C 1 92 ? 6.296   -26.068 26.757  1.00 67.60  ? 91  SER C CA  1 
ATOM   2132 C C   . SER C 1 92 ? 6.524   -27.307 25.898  1.00 69.09  ? 91  SER C C   1 
ATOM   2133 O O   . SER C 1 92 ? 7.272   -28.200 26.291  1.00 74.39  ? 91  SER C O   1 
ATOM   2134 C CB  . SER C 1 92 ? 4.971   -26.169 27.481  1.00 61.56  ? 91  SER C CB  1 
ATOM   2135 O OG  . SER C 1 92 ? 5.048   -25.459 28.706  1.00 67.01  ? 91  SER C OG  1 
ATOM   2136 N N   . TYR C 1 93 ? 5.828   -27.365 24.756  1.00 69.22  ? 92  TYR C N   1 
ATOM   2137 C CA  . TYR C 1 93 ? 5.834   -28.508 23.856  1.00 68.42  ? 92  TYR C CA  1 
ATOM   2138 C C   . TYR C 1 93 ? 5.557   -29.792 24.640  1.00 76.48  ? 92  TYR C C   1 
ATOM   2139 O O   . TYR C 1 93 ? 4.503   -29.823 25.313  1.00 88.25  ? 92  TYR C O   1 
ATOM   2140 C CB  . TYR C 1 93 ? 7.158   -28.545 23.089  1.00 70.59  ? 92  TYR C CB  1 
ATOM   2141 C CG  . TYR C 1 93 ? 7.453   -27.259 22.329  1.00 62.46  ? 92  TYR C CG  1 
ATOM   2142 C CD1 . TYR C 1 93 ? 6.688   -26.883 21.232  1.00 60.42  ? 92  TYR C CD1 1 
ATOM   2143 C CD2 . TYR C 1 93 ? 8.513   -26.438 22.695  1.00 62.63  ? 92  TYR C CD2 1 
ATOM   2144 C CE1 . TYR C 1 93 ? 6.953   -25.719 20.530  1.00 60.83  ? 92  TYR C CE1 1 
ATOM   2145 C CE2 . TYR C 1 93 ? 8.790   -25.274 22.001  1.00 62.29  ? 92  TYR C CE2 1 
ATOM   2146 C CZ  . TYR C 1 93 ? 8.009   -24.913 20.918  1.00 62.98  ? 92  TYR C CZ  1 
ATOM   2147 O OH  . TYR C 1 93 ? 8.290   -23.754 20.250  1.00 62.90  ? 92  TYR C OH  1 
HETATM 2148 S S   . SO4 D 2 .  ? 1.655   -33.857 2.043   1.00 90.65  ? 101 SO4 A S   1 
HETATM 2149 O O1  . SO4 D 2 .  ? 2.339   -34.445 0.924   1.00 66.30  ? 101 SO4 A O1  1 
HETATM 2150 O O2  . SO4 D 2 .  ? 1.624   -32.420 1.886   1.00 66.97  ? 101 SO4 A O2  1 
HETATM 2151 O O3  . SO4 D 2 .  ? 0.307   -34.364 2.095   1.00 87.86  ? 101 SO4 A O3  1 
HETATM 2152 O O4  . SO4 D 2 .  ? 2.344   -34.204 3.267   1.00 79.05  ? 101 SO4 A O4  1 
HETATM 2153 S S   . SO4 E 2 .  ? -8.957  -24.667 1.535   1.00 91.91  ? 102 SO4 A S   1 
HETATM 2154 O O1  . SO4 E 2 .  ? -9.216  -24.540 0.125   1.00 74.73  ? 102 SO4 A O1  1 
HETATM 2155 O O2  . SO4 E 2 .  ? -9.329  -23.445 2.198   1.00 86.44  ? 102 SO4 A O2  1 
HETATM 2156 O O3  . SO4 E 2 .  ? -9.717  -25.772 2.065   1.00 87.03  ? 102 SO4 A O3  1 
HETATM 2157 O O4  . SO4 E 2 .  ? -7.559  -24.914 1.759   1.00 92.54  ? 102 SO4 A O4  1 
HETATM 2158 C C1  . EDO F 3 .  ? 14.171  -19.504 -7.384  1.00 46.28  ? 103 EDO A C1  1 
HETATM 2159 O O1  . EDO F 3 .  ? 15.380  -18.776 -7.265  1.00 40.76  ? 103 EDO A O1  1 
HETATM 2160 C C2  . EDO F 3 .  ? 13.328  -18.954 -8.502  1.00 44.22  ? 103 EDO A C2  1 
HETATM 2161 O O2  . EDO F 3 .  ? 12.749  -17.691 -8.236  1.00 43.75  ? 103 EDO A O2  1 
HETATM 2162 N N1  . I8G G 4 .  ? 1.962   -25.088 -4.479  0.66 54.80  ? 104 I8G A N1  1 
HETATM 2163 C C4  . I8G G 4 .  ? 2.863   -25.728 -8.782  0.66 55.94  ? 104 I8G A C4  1 
HETATM 2164 C C5  . I8G G 4 .  ? 2.609   -24.434 -6.763  0.66 49.53  ? 104 I8G A C5  1 
HETATM 2165 C C6  . I8G G 4 .  ? 1.641   -25.086 -5.795  0.66 52.05  ? 104 I8G A C6  1 
HETATM 2166 C C7  . I8G G 4 .  ? 3.319   -24.980 -3.870  0.66 50.21  ? 104 I8G A C7  1 
HETATM 2167 C C8  . I8G G 4 .  ? 3.064   -25.086 -2.376  0.66 43.44  ? 104 I8G A C8  1 
HETATM 2168 C C10 . I8G G 4 .  ? 0.929   -25.234 -3.447  0.66 54.15  ? 104 I8G A C10 1 
HETATM 2169 F F1  . I8G G 4 .  ? 4.937   -28.817 -10.493 0.66 62.13  ? 104 I8G A F1  1 
HETATM 2170 C C1  . I8G G 4 .  ? 4.258   -27.781 -9.917  0.66 52.98  ? 104 I8G A C1  1 
HETATM 2171 C C2  . I8G G 4 .  ? 4.269   -26.562 -10.540 0.66 48.84  ? 104 I8G A C2  1 
HETATM 2172 C C3  . I8G G 4 .  ? 3.547   -25.523 -9.969  0.66 50.65  ? 104 I8G A C3  1 
HETATM 2173 O O1  . I8G G 4 .  ? 2.229   -24.702 -8.117  0.66 55.83  ? 104 I8G A O1  1 
HETATM 2174 O O2  . I8G G 4 .  ? 0.608   -25.590 -6.215  0.66 54.92  ? 104 I8G A O2  1 
HETATM 2175 C C9  . I8G G 4 .  ? 1.603   -24.673 -2.211  0.66 52.82  ? 104 I8G A C9  1 
HETATM 2176 C C11 . I8G G 4 .  ? 2.854   -26.983 -8.191  0.66 49.58  ? 104 I8G A C11 1 
HETATM 2177 C C12 . I8G G 4 .  ? 3.561   -28.023 -8.764  0.66 51.25  ? 104 I8G A C12 1 
HETATM 2178 S S   . SO4 H 2 .  ? 9.245   -29.458 5.768   1.00 63.79  ? 105 SO4 A S   1 
HETATM 2179 O O1  . SO4 H 2 .  ? 9.943   -28.662 4.847   1.00 52.33  ? 105 SO4 A O1  1 
HETATM 2180 O O2  . SO4 H 2 .  ? 8.697   -30.608 5.065   1.00 60.79  ? 105 SO4 A O2  1 
HETATM 2181 O O3  . SO4 H 2 .  ? 10.146  -29.896 6.803   1.00 66.83  ? 105 SO4 A O3  1 
HETATM 2182 O O4  . SO4 H 2 .  ? 8.170   -28.699 6.325   1.00 65.76  ? 105 SO4 A O4  1 
HETATM 2183 C C1  . EDO I 3 .  ? 17.462  -16.349 -25.680 1.00 64.06  ? 101 EDO B C1  1 
HETATM 2184 O O1  . EDO I 3 .  ? 17.899  -16.413 -24.324 1.00 52.68  ? 101 EDO B O1  1 
HETATM 2185 C C2  . EDO I 3 .  ? 16.894  -15.012 -26.005 1.00 64.80  ? 101 EDO B C2  1 
HETATM 2186 O O2  . EDO I 3 .  ? 17.514  -13.955 -25.304 1.00 62.88  ? 101 EDO B O2  1 
HETATM 2187 S S   . SO4 J 2 .  ? 7.161   -9.067  -25.032 1.00 67.26  ? 102 SO4 B S   1 
HETATM 2188 O O1  . SO4 J 2 .  ? 8.273   -8.553  -25.838 1.00 49.93  ? 102 SO4 B O1  1 
HETATM 2189 O O2  . SO4 J 2 .  ? 6.600   -10.233 -25.657 1.00 61.64  ? 102 SO4 B O2  1 
HETATM 2190 O O3  . SO4 J 2 .  ? 7.622   -9.388  -23.683 1.00 51.42  ? 102 SO4 B O3  1 
HETATM 2191 O O4  . SO4 J 2 .  ? 6.131   -8.068  -24.964 1.00 66.47  ? 102 SO4 B O4  1 
HETATM 2192 S S   . SO4 K 2 .  ? 14.604  -26.984 -26.513 1.00 61.38  ? 103 SO4 B S   1 
HETATM 2193 O O1  . SO4 K 2 .  ? 15.868  -26.441 -26.115 1.00 65.09  ? 103 SO4 B O1  1 
HETATM 2194 O O2  . SO4 K 2 .  ? 14.834  -28.229 -27.199 1.00 71.17  ? 103 SO4 B O2  1 
HETATM 2195 O O3  . SO4 K 2 .  ? 13.786  -27.212 -25.354 1.00 68.70  ? 103 SO4 B O3  1 
HETATM 2196 O O4  . SO4 K 2 .  ? 13.912  -26.076 -27.387 1.00 62.11  ? 103 SO4 B O4  1 
HETATM 2197 C C1  . EDO L 3 .  ? 16.797  -36.096 16.343  1.00 46.31  ? 101 EDO C C1  1 
HETATM 2198 O O1  . EDO L 3 .  ? 15.734  -36.873 15.812  1.00 49.78  ? 101 EDO C O1  1 
HETATM 2199 C C2  . EDO L 3 .  ? 16.426  -35.119 17.429  1.00 41.06  ? 101 EDO C C2  1 
HETATM 2200 O O2  . EDO L 3 .  ? 15.477  -35.606 18.339  1.00 38.62  ? 101 EDO C O2  1 
HETATM 2201 S S   . SO4 M 2 .  ? 29.508  -38.578 11.696  1.00 99.73  ? 102 SO4 C S   1 
HETATM 2202 O O1  . SO4 M 2 .  ? 30.767  -37.881 11.595  1.00 87.90  ? 102 SO4 C O1  1 
HETATM 2203 O O2  . SO4 M 2 .  ? 28.895  -38.643 10.398  1.00 85.42  ? 102 SO4 C O2  1 
HETATM 2204 O O3  . SO4 M 2 .  ? 29.739  -39.910 12.182  1.00 78.29  ? 102 SO4 C O3  1 
HETATM 2205 O O4  . SO4 M 2 .  ? 28.631  -37.875 12.599  1.00 81.41  ? 102 SO4 C O4  1 
HETATM 2206 O O   . HOH N 5 .  ? 9.597   -32.078 4.073   1.00 58.94  ? 201 HOH A O   1 
HETATM 2207 O O   . HOH N 5 .  ? -2.049  -31.076 -3.809  1.00 64.81  ? 202 HOH A O   1 
HETATM 2208 O O   . HOH N 5 .  ? 1.039   -29.105 -4.801  1.00 62.43  ? 203 HOH A O   1 
HETATM 2209 O O   . HOH N 5 .  ? 6.001   -29.105 6.810   1.00 56.45  ? 204 HOH A O   1 
HETATM 2210 O O   . HOH N 5 .  ? 0.146   -33.623 4.257   1.00 67.61  ? 205 HOH A O   1 
HETATM 2211 O O   . HOH N 5 .  ? -5.694  -13.393 -16.458 1.00 56.30  ? 206 HOH A O   1 
HETATM 2212 O O   . HOH N 5 .  ? 1.827   2.254   3.339   1.00 78.83  ? 207 HOH A O   1 
HETATM 2213 O O   . HOH N 5 .  ? 11.173  -29.575 2.962   1.00 48.98  ? 208 HOH A O   1 
HETATM 2214 O O   . HOH N 5 .  ? 16.099  -24.544 1.822   1.00 49.48  ? 209 HOH A O   1 
HETATM 2215 O O   . HOH N 5 .  ? 9.485   -18.178 -10.865 1.00 40.41  ? 210 HOH A O   1 
HETATM 2216 O O   . HOH N 5 .  ? 4.437   -10.408 13.698  1.00 63.21  ? 211 HOH A O   1 
HETATM 2217 O O   . HOH N 5 .  ? -3.566  -10.761 6.747   1.00 43.41  ? 212 HOH A O   1 
HETATM 2218 O O   . HOH N 5 .  ? 4.574   -34.586 4.394   1.00 68.98  ? 213 HOH A O   1 
HETATM 2219 O O   . HOH N 5 .  ? 0.600   -10.584 -15.546 1.00 53.99  ? 214 HOH A O   1 
HETATM 2220 O O   . HOH N 5 .  ? -1.152  -28.549 -6.342  1.00 83.29  ? 215 HOH A O   1 
HETATM 2221 O O   . HOH N 5 .  ? -1.946  3.151   -2.062  1.00 55.03  ? 216 HOH A O   1 
HETATM 2222 O O   . HOH N 5 .  ? 7.279   -10.613 -12.130 1.00 47.87  ? 217 HOH A O   1 
HETATM 2223 O O   . HOH N 5 .  ? -4.194  -21.117 5.985   1.00 47.72  ? 218 HOH A O   1 
HETATM 2224 O O   . HOH N 5 .  ? 1.170   -24.958 13.875  1.00 66.05  ? 219 HOH A O   1 
HETATM 2225 O O   . HOH N 5 .  ? 8.232   -17.776 -15.987 1.00 68.08  ? 220 HOH A O   1 
HETATM 2226 O O   . HOH N 5 .  ? 11.275  -23.583 9.771   1.00 44.91  ? 221 HOH A O   1 
HETATM 2227 O O   . HOH N 5 .  ? 14.095  -15.725 -9.292  1.00 42.79  ? 222 HOH A O   1 
HETATM 2228 O O   . HOH N 5 .  ? -0.583  -21.004 6.781   1.00 42.06  ? 223 HOH A O   1 
HETATM 2229 O O   . HOH N 5 .  ? -7.657  -16.997 6.637   1.00 54.13  ? 224 HOH A O   1 
HETATM 2230 O O   . HOH N 5 .  ? 4.704   -7.890  0.915   1.00 45.59  ? 225 HOH A O   1 
HETATM 2231 O O   . HOH N 5 .  ? 4.505   -3.598  -3.253  1.00 41.82  ? 226 HOH A O   1 
HETATM 2232 O O   . HOH N 5 .  ? 19.930  -15.495 7.356   1.00 39.91  ? 227 HOH A O   1 
HETATM 2233 O O   . HOH N 5 .  ? 2.889   -10.007 -13.139 1.00 52.88  ? 228 HOH A O   1 
HETATM 2234 O O   . HOH N 5 .  ? 10.130  -13.066 9.583   1.00 48.97  ? 229 HOH A O   1 
HETATM 2235 O O   . HOH N 5 .  ? 5.002   -1.509  -6.384  1.00 44.30  ? 230 HOH A O   1 
HETATM 2236 O O   . HOH N 5 .  ? -5.961  -11.440 -11.475 1.00 49.46  ? 231 HOH A O   1 
HETATM 2237 O O   . HOH N 5 .  ? 15.608  -28.046 -0.355  1.00 58.34  ? 232 HOH A O   1 
HETATM 2238 O O   . HOH N 5 .  ? 16.510  -11.982 -17.044 1.00 50.10  ? 233 HOH A O   1 
HETATM 2239 O O   . HOH N 5 .  ? 3.660   -29.633 -0.606  1.00 50.12  ? 234 HOH A O   1 
HETATM 2240 O O   . HOH N 5 .  ? 13.315  -27.964 -4.759  1.00 62.63  ? 235 HOH A O   1 
HETATM 2241 O O   . HOH N 5 .  ? 9.297   -2.459  -0.637  1.00 71.54  ? 236 HOH A O   1 
HETATM 2242 O O   . HOH N 5 .  ? -6.614  -29.917 1.813   1.00 56.74  ? 237 HOH A O   1 
HETATM 2243 O O   . HOH N 5 .  ? 17.338  -12.849 1.407   1.00 28.95  ? 238 HOH A O   1 
HETATM 2244 O O   . HOH N 5 .  ? 1.974   -4.767  -10.374 1.00 49.95  ? 239 HOH A O   1 
HETATM 2245 O O   . HOH N 5 .  ? 9.795   -6.033  -1.630  1.00 44.78  ? 240 HOH A O   1 
HETATM 2246 O O   . HOH N 5 .  ? 11.097  -5.199  -7.784  1.00 42.53  ? 241 HOH A O   1 
HETATM 2247 O O   . HOH N 5 .  ? 13.285  -11.618 8.098   1.00 62.37  ? 242 HOH A O   1 
HETATM 2248 O O   . HOH N 5 .  ? 12.865  -9.613  -7.287  1.00 50.42  ? 243 HOH A O   1 
HETATM 2249 O O   . HOH N 5 .  ? -7.904  -15.853 -1.023  1.00 45.55  ? 244 HOH A O   1 
HETATM 2250 O O   . HOH N 5 .  ? -5.511  -15.848 -8.041  1.00 37.22  ? 245 HOH A O   1 
HETATM 2251 O O   . HOH N 5 .  ? -1.492  -22.040 -0.662  1.00 36.10  ? 246 HOH A O   1 
HETATM 2252 O O   . HOH N 5 .  ? -1.238  -7.641  11.389  1.00 51.44  ? 247 HOH A O   1 
HETATM 2253 O O   . HOH N 5 .  ? 1.780   -18.611 -18.600 1.00 55.73  ? 248 HOH A O   1 
HETATM 2254 O O   . HOH N 5 .  ? 14.868  -13.184 10.294  1.00 53.76  ? 249 HOH A O   1 
HETATM 2255 O O   . HOH N 5 .  ? 10.846  -27.747 -6.838  1.00 55.33  ? 250 HOH A O   1 
HETATM 2256 O O   . HOH N 5 .  ? -8.361  -17.132 3.353   1.00 58.37  ? 251 HOH A O   1 
HETATM 2257 O O   . HOH N 5 .  ? 4.725   5.985   -4.384  1.00 66.10  ? 252 HOH A O   1 
HETATM 2258 O O   . HOH N 5 .  ? 11.635  -11.808 5.879   1.00 41.06  ? 253 HOH A O   1 
HETATM 2259 O O   . HOH N 5 .  ? 13.460  -11.934 -4.226  1.00 29.42  ? 254 HOH A O   1 
HETATM 2260 O O   . HOH N 5 .  ? 9.137   -16.362 -13.048 1.00 43.99  ? 255 HOH A O   1 
HETATM 2261 O O   . HOH N 5 .  ? 11.458  -5.914  -4.009  1.00 52.67  ? 256 HOH A O   1 
HETATM 2262 O O   . HOH N 5 .  ? 11.659  -12.338 -6.112  1.00 34.46  ? 257 HOH A O   1 
HETATM 2263 O O   . HOH N 5 .  ? -2.669  -11.531 13.373  1.00 58.59  ? 258 HOH A O   1 
HETATM 2264 O O   . HOH N 5 .  ? 7.920   -17.333 8.758   1.00 53.08  ? 259 HOH A O   1 
HETATM 2265 O O   . HOH N 5 .  ? -5.590  -19.703 -5.742  1.00 42.10  ? 260 HOH A O   1 
HETATM 2266 O O   . HOH N 5 .  ? -8.317  -21.261 -1.357  1.00 54.65  ? 261 HOH A O   1 
HETATM 2267 O O   . HOH N 5 .  ? -1.447  -11.776 11.140  1.00 42.18  ? 262 HOH A O   1 
HETATM 2268 O O   . HOH N 5 .  ? -0.615  -20.525 11.400  1.00 60.64  ? 263 HOH A O   1 
HETATM 2269 O O   . HOH N 5 .  ? 14.863  -29.463 3.879   1.00 48.01  ? 264 HOH A O   1 
HETATM 2270 O O   . HOH N 5 .  ? 0.328   -23.226 8.938   1.00 51.92  ? 265 HOH A O   1 
HETATM 2271 O O   . HOH N 5 .  ? -4.091  -25.840 -5.703  1.00 49.26  ? 266 HOH A O   1 
HETATM 2272 O O   . HOH N 5 .  ? -5.790  -26.850 3.190   1.00 61.40  ? 267 HOH A O   1 
HETATM 2273 O O   . HOH N 5 .  ? 2.592   -6.265  5.417   1.00 43.93  ? 268 HOH A O   1 
HETATM 2274 O O   . HOH N 5 .  ? 15.852  -11.835 -5.226  1.00 43.14  ? 269 HOH A O   1 
HETATM 2275 O O   . HOH N 5 .  ? 8.238   -8.188  4.471   1.00 47.46  ? 270 HOH A O   1 
HETATM 2276 O O   . HOH N 5 .  ? 1.794   -10.333 11.695  1.00 45.39  ? 271 HOH A O   1 
HETATM 2277 O O   . HOH N 5 .  ? 8.058   -7.811  1.213   1.00 38.77  ? 272 HOH A O   1 
HETATM 2278 O O   . HOH N 5 .  ? -6.842  -21.710 -6.105  1.00 55.80  ? 273 HOH A O   1 
HETATM 2279 O O   . HOH N 5 .  ? -7.804  -16.727 1.449   1.00 47.17  ? 274 HOH A O   1 
HETATM 2280 O O   . HOH N 5 .  ? 2.957   -28.338 -3.209  1.00 56.30  ? 275 HOH A O   1 
HETATM 2281 O O   . HOH N 5 .  ? 6.402   -5.842  0.458   1.00 65.83  ? 276 HOH A O   1 
HETATM 2282 O O   . HOH N 5 .  ? -6.030  -12.674 6.668   1.00 47.59  ? 277 HOH A O   1 
HETATM 2283 O O   . HOH N 5 .  ? 5.425   -7.542  3.998   1.00 43.01  ? 278 HOH A O   1 
HETATM 2284 O O   . HOH N 5 .  ? 12.969  -13.299 -8.494  1.00 53.18  ? 279 HOH A O   1 
HETATM 2285 O O   . HOH N 5 .  ? 9.686   -30.395 9.788   1.00 43.87  ? 280 HOH A O   1 
HETATM 2286 O O   . HOH N 5 .  ? 11.289  -7.751  0.414   1.00 35.77  ? 281 HOH A O   1 
HETATM 2287 O O   . HOH N 5 .  ? 12.970  -15.614 -11.945 1.00 62.95  ? 282 HOH A O   1 
HETATM 2288 O O   . HOH N 5 .  ? 22.421  -16.650 -0.415  1.00 49.24  ? 283 HOH A O   1 
HETATM 2289 O O   . HOH N 5 .  ? -0.663  -29.173 10.152  1.00 55.95  ? 284 HOH A O   1 
HETATM 2290 O O   . HOH N 5 .  ? -8.172  -19.388 -3.241  1.00 57.02  ? 285 HOH A O   1 
HETATM 2291 O O   . HOH N 5 .  ? -3.717  -7.866  10.551  1.00 55.26  ? 286 HOH A O   1 
HETATM 2292 O O   . HOH N 5 .  ? 21.583  -16.607 -3.390  1.00 39.08  ? 287 HOH A O   1 
HETATM 2293 O O   . HOH N 5 .  ? -7.091  -11.492 -8.086  1.00 35.38  ? 288 HOH A O   1 
HETATM 2294 O O   . HOH N 5 .  ? -3.450  -10.598 9.348   1.00 55.79  ? 289 HOH A O   1 
HETATM 2295 O O   . HOH N 5 .  ? 6.455   -16.148 -14.825 1.00 62.27  ? 290 HOH A O   1 
HETATM 2296 O O   . HOH N 5 .  ? 17.401  -18.202 -9.723  1.00 57.57  ? 291 HOH A O   1 
HETATM 2297 O O   . HOH N 5 .  ? 9.926   -20.497 -18.443 1.00 50.15  ? 292 HOH A O   1 
HETATM 2298 O O   . HOH N 5 .  ? -5.391  -17.158 -15.869 1.00 56.11  ? 293 HOH A O   1 
HETATM 2299 O O   . HOH N 5 .  ? -5.321  -23.561 -7.016  1.00 47.74  ? 294 HOH A O   1 
HETATM 2300 O O   . HOH N 5 .  ? 8.874   -9.117  -13.697 1.00 52.43  ? 295 HOH A O   1 
HETATM 2301 O O   . HOH N 5 .  ? -10.648 -15.816 -3.445  1.00 55.97  ? 296 HOH A O   1 
HETATM 2302 O O   . HOH N 5 .  ? -4.070  -26.589 6.931   1.00 70.97  ? 297 HOH A O   1 
HETATM 2303 O O   . HOH N 5 .  ? -9.127  -21.488 -4.736  1.00 166.78 ? 298 HOH A O   1 
HETATM 2304 O O   . HOH N 5 .  ? 5.077   -7.308  -10.995 1.00 56.46  ? 299 HOH A O   1 
HETATM 2305 O O   . HOH N 5 .  ? -7.225  -14.154 -9.325  1.00 45.35  ? 300 HOH A O   1 
HETATM 2306 O O   . HOH N 5 .  ? -10.239 -27.944 -2.222  1.00 75.32  ? 301 HOH A O   1 
HETATM 2307 O O   . HOH N 5 .  ? 11.613  -1.963  -1.676  1.00 53.09  ? 302 HOH A O   1 
HETATM 2308 O O   . HOH N 5 .  ? 6.688   -18.473 -13.877 1.00 114.72 ? 303 HOH A O   1 
HETATM 2309 O O   . HOH N 5 .  ? 5.692   -3.354  0.789   1.00 64.71  ? 304 HOH A O   1 
HETATM 2310 O O   . HOH N 5 .  ? 9.532   -7.421  2.899   1.00 48.39  ? 305 HOH A O   1 
HETATM 2311 O O   . HOH N 5 .  ? 4.648   -9.685  -11.294 1.00 51.45  ? 306 HOH A O   1 
HETATM 2312 O O   . HOH N 5 .  ? -6.979  -19.424 8.238   1.00 57.33  ? 307 HOH A O   1 
HETATM 2313 O O   . HOH N 5 .  ? 8.091   -30.638 -2.441  1.00 75.28  ? 308 HOH A O   1 
HETATM 2314 O O   . HOH N 5 .  ? -6.138  -23.139 5.691   1.00 62.43  ? 309 HOH A O   1 
HETATM 2315 O O   . HOH N 5 .  ? -4.942  -21.081 -7.882  1.00 57.09  ? 310 HOH A O   1 
HETATM 2316 O O   . HOH O 5 .  ? 19.755  -22.229 -23.500 1.00 58.80  ? 201 HOH B O   1 
HETATM 2317 O O   . HOH O 5 .  ? 6.600   -12.297 -26.230 1.00 50.94  ? 202 HOH B O   1 
HETATM 2318 O O   . HOH O 5 .  ? 10.084  -11.178 -38.254 1.00 61.04  ? 203 HOH B O   1 
HETATM 2319 O O   . HOH O 5 .  ? 30.297  -12.916 -46.053 1.00 82.08  ? 204 HOH B O   1 
HETATM 2320 O O   . HOH O 5 .  ? 26.134  -23.182 -31.408 1.00 47.72  ? 205 HOH B O   1 
HETATM 2321 O O   . HOH O 5 .  ? 27.777  -8.267  -28.935 1.00 54.92  ? 206 HOH B O   1 
HETATM 2322 O O   . HOH O 5 .  ? 30.722  -8.477  -29.946 1.00 69.96  ? 207 HOH B O   1 
HETATM 2323 O O   . HOH O 5 .  ? 30.379  -19.805 -40.439 1.00 46.76  ? 208 HOH B O   1 
HETATM 2324 O O   . HOH O 5 .  ? 26.403  -12.969 -44.962 1.00 69.76  ? 209 HOH B O   1 
HETATM 2325 O O   . HOH O 5 .  ? 10.395  -16.940 -44.364 1.00 47.09  ? 210 HOH B O   1 
HETATM 2326 O O   . HOH O 5 .  ? 18.473  -0.754  -24.959 1.00 86.54  ? 211 HOH B O   1 
HETATM 2327 O O   . HOH O 5 .  ? 24.477  -1.747  -36.479 1.00 62.60  ? 212 HOH B O   1 
HETATM 2328 O O   . HOH O 5 .  ? 8.312   -27.797 -38.428 1.00 64.75  ? 213 HOH B O   1 
HETATM 2329 O O   . HOH O 5 .  ? 17.618  -15.289 -21.351 1.00 57.23  ? 214 HOH B O   1 
HETATM 2330 O O   . HOH O 5 .  ? 8.733   -8.643  -16.711 1.00 53.52  ? 215 HOH B O   1 
HETATM 2331 O O   . HOH O 5 .  ? 12.761  -4.677  -42.035 1.00 56.69  ? 216 HOH B O   1 
HETATM 2332 O O   . HOH O 5 .  ? 6.082   -7.401  -32.079 1.00 56.38  ? 217 HOH B O   1 
HETATM 2333 O O   . HOH O 5 .  ? 20.852  -13.519 -42.745 1.00 48.82  ? 218 HOH B O   1 
HETATM 2334 O O   . HOH O 5 .  ? 3.264   -8.857  -27.326 1.00 59.18  ? 219 HOH B O   1 
HETATM 2335 O O   . HOH O 5 .  ? 25.498  -6.044  -35.908 1.00 46.99  ? 220 HOH B O   1 
HETATM 2336 O O   . HOH O 5 .  ? 25.046  -5.171  -29.938 1.00 51.87  ? 221 HOH B O   1 
HETATM 2337 O O   . HOH O 5 .  ? 10.662  -18.863 -32.977 1.00 38.77  ? 222 HOH B O   1 
HETATM 2338 O O   . HOH O 5 .  ? 32.118  -11.859 -42.081 1.00 57.04  ? 223 HOH B O   1 
HETATM 2339 O O   . HOH O 5 .  ? 7.459   -18.223 -31.781 1.00 52.46  ? 224 HOH B O   1 
HETATM 2340 O O   . HOH O 5 .  ? 17.585  -19.689 -42.118 1.00 56.18  ? 225 HOH B O   1 
HETATM 2341 O O   . HOH O 5 .  ? 27.272  -10.688 -29.074 1.00 56.33  ? 226 HOH B O   1 
HETATM 2342 O O   . HOH O 5 .  ? 16.795  -19.257 -28.952 1.00 34.71  ? 227 HOH B O   1 
HETATM 2343 O O   . HOH O 5 .  ? 18.073  -0.555  -38.575 1.00 38.83  ? 228 HOH B O   1 
HETATM 2344 O O   . HOH O 5 .  ? 22.671  -23.201 -28.904 1.00 45.26  ? 229 HOH B O   1 
HETATM 2345 O O   . HOH O 5 .  ? 15.606  -25.564 -45.572 1.00 56.72  ? 230 HOH B O   1 
HETATM 2346 O O   . HOH O 5 .  ? 7.154   -19.275 -35.009 1.00 60.48  ? 231 HOH B O   1 
HETATM 2347 O O   . HOH O 5 .  ? 31.716  -12.058 -39.324 1.00 65.58  ? 232 HOH B O   1 
HETATM 2348 O O   . HOH O 5 .  ? 14.712  -24.424 -40.349 1.00 55.99  ? 233 HOH B O   1 
HETATM 2349 O O   . HOH O 5 .  ? 27.944  -17.695 -25.178 1.00 53.23  ? 234 HOH B O   1 
HETATM 2350 O O   . HOH O 5 .  ? 23.635  -2.358  -29.213 1.00 49.28  ? 235 HOH B O   1 
HETATM 2351 O O   . HOH O 5 .  ? 14.094  -6.268  -41.279 1.00 50.15  ? 236 HOH B O   1 
HETATM 2352 O O   . HOH O 5 .  ? 7.378   -12.664 -39.111 1.00 70.68  ? 237 HOH B O   1 
HETATM 2353 O O   . HOH O 5 .  ? 1.905   -12.988 -28.289 1.00 59.84  ? 238 HOH B O   1 
HETATM 2354 O O   . HOH O 5 .  ? 21.114  -26.619 -30.310 1.00 71.40  ? 239 HOH B O   1 
HETATM 2355 O O   . HOH O 5 .  ? 21.370  3.615   -32.874 1.00 46.33  ? 240 HOH B O   1 
HETATM 2356 O O   . HOH O 5 .  ? 20.355  -10.025 -43.029 1.00 49.48  ? 241 HOH B O   1 
HETATM 2357 O O   . HOH O 5 .  ? 13.599  -22.198 -20.667 1.00 71.55  ? 242 HOH B O   1 
HETATM 2358 O O   . HOH O 5 .  ? 19.833  -25.686 -34.209 1.00 50.43  ? 243 HOH B O   1 
HETATM 2359 O O   . HOH O 5 .  ? 10.387  -19.825 -43.147 1.00 52.43  ? 244 HOH B O   1 
HETATM 2360 O O   . HOH O 5 .  ? 32.471  -19.082 -42.442 1.00 52.62  ? 245 HOH B O   1 
HETATM 2361 O O   . HOH O 5 .  ? 23.804  -11.400 -22.136 1.00 48.23  ? 246 HOH B O   1 
HETATM 2362 O O   . HOH O 5 .  ? 17.949  -3.471  -22.261 1.00 66.69  ? 247 HOH B O   1 
HETATM 2363 O O   . HOH O 5 .  ? 18.481  -26.013 -28.951 1.00 51.72  ? 248 HOH B O   1 
HETATM 2364 O O   . HOH O 5 .  ? 13.217  -12.452 -47.464 1.00 67.86  ? 249 HOH B O   1 
HETATM 2365 O O   . HOH O 5 .  ? 28.854  -12.428 -35.407 1.00 77.24  ? 250 HOH B O   1 
HETATM 2366 O O   . HOH O 5 .  ? 8.101   -23.529 -24.420 1.00 62.53  ? 251 HOH B O   1 
HETATM 2367 O O   . HOH O 5 .  ? 34.360  -23.550 -30.016 1.00 66.39  ? 252 HOH B O   1 
HETATM 2368 O O   . HOH O 5 .  ? 10.552  -21.870 -32.849 1.00 49.88  ? 253 HOH B O   1 
HETATM 2369 O O   . HOH O 5 .  ? 6.621   -20.656 -24.998 1.00 56.34  ? 254 HOH B O   1 
HETATM 2370 O O   . HOH O 5 .  ? 31.856  -21.171 -38.378 1.00 56.03  ? 255 HOH B O   1 
HETATM 2371 O O   . HOH O 5 .  ? 23.992  -4.249  -36.881 1.00 39.61  ? 256 HOH B O   1 
HETATM 2372 O O   . HOH O 5 .  ? 20.931  -6.559  -42.778 1.00 48.95  ? 257 HOH B O   1 
HETATM 2373 O O   . HOH O 5 .  ? 7.800   -7.909  -20.924 1.00 65.03  ? 258 HOH B O   1 
HETATM 2374 O O   . HOH O 5 .  ? 18.267  4.508   -34.530 1.00 48.61  ? 259 HOH B O   1 
HETATM 2375 O O   . HOH O 5 .  ? 27.908  -24.892 -35.174 1.00 48.07  ? 260 HOH B O   1 
HETATM 2376 O O   . HOH O 5 .  ? 18.203  -15.881 -45.922 1.00 50.55  ? 261 HOH B O   1 
HETATM 2377 O O   . HOH O 5 .  ? 17.291  -9.811  -43.790 1.00 56.17  ? 262 HOH B O   1 
HETATM 2378 O O   . HOH O 5 .  ? 24.650  -6.745  -42.749 1.00 66.91  ? 263 HOH B O   1 
HETATM 2379 O O   . HOH O 5 .  ? 18.651  -13.198 -44.632 1.00 60.32  ? 264 HOH B O   1 
HETATM 2380 O O   . HOH O 5 .  ? 12.128  -4.582  -25.057 1.00 63.67  ? 265 HOH B O   1 
HETATM 2381 O O   . HOH O 5 .  ? 26.500  -0.730  -29.364 1.00 62.16  ? 266 HOH B O   1 
HETATM 2382 O O   . HOH O 5 .  ? 2.880   -16.156 -42.877 1.00 66.70  ? 267 HOH B O   1 
HETATM 2383 O O   . HOH O 5 .  ? 20.094  3.844   -33.450 1.00 52.07  ? 268 HOH B O   1 
HETATM 2384 O O   . HOH O 5 .  ? 15.109  -8.083  -43.244 1.00 59.15  ? 269 HOH B O   1 
HETATM 2385 O O   . HOH O 5 .  ? 9.703   -6.453  -41.206 1.00 52.52  ? 270 HOH B O   1 
HETATM 2386 O O   . HOH O 5 .  ? 20.050  -3.605  -22.460 1.00 66.91  ? 271 HOH B O   1 
HETATM 2387 O O   . HOH O 5 .  ? 27.963  -24.880 -32.314 1.00 51.34  ? 272 HOH B O   1 
HETATM 2388 O O   . HOH O 5 .  ? 17.354  -26.098 -21.186 1.00 69.65  ? 273 HOH B O   1 
HETATM 2389 O O   . HOH O 5 .  ? 13.154  -20.114 -19.462 1.00 64.77  ? 274 HOH B O   1 
HETATM 2390 O O   . HOH O 5 .  ? 11.459  -24.140 -29.860 1.00 61.82  ? 275 HOH B O   1 
HETATM 2391 O O   . HOH O 5 .  ? 16.454  -0.526  -25.709 1.00 61.38  ? 276 HOH B O   1 
HETATM 2392 O O   . HOH O 5 .  ? 39.647  -13.493 -39.019 1.00 70.57  ? 277 HOH B O   1 
HETATM 2393 O O   . HOH O 5 .  ? 15.448  -21.766 -41.936 1.00 58.97  ? 278 HOH B O   1 
HETATM 2394 O O   . HOH O 5 .  ? 7.402   -10.053 -18.606 1.00 53.89  ? 279 HOH B O   1 
HETATM 2395 O O   . HOH O 5 .  ? 24.688  -4.157  -27.821 1.00 59.84  ? 280 HOH B O   1 
HETATM 2396 O O   . HOH O 5 .  ? 22.508  -29.171 -35.762 1.00 52.23  ? 281 HOH B O   1 
HETATM 2397 O O   . HOH O 5 .  ? 9.376   -22.626 -19.331 1.00 65.23  ? 282 HOH B O   1 
HETATM 2398 O O   . HOH P 5 .  ? 12.109  -35.134 14.047  1.00 60.05  ? 201 HOH C O   1 
HETATM 2399 O O   . HOH P 5 .  ? 26.872  -38.847 12.725  1.00 48.61  ? 202 HOH C O   1 
HETATM 2400 O O   . HOH P 5 .  ? 27.093  -37.662 10.238  1.00 55.43  ? 203 HOH C O   1 
HETATM 2401 O O   . HOH P 5 .  ? 29.670  -16.348 11.890  1.00 67.59  ? 204 HOH C O   1 
HETATM 2402 O O   . HOH P 5 .  ? 16.776  -19.276 18.931  1.00 80.00  ? 205 HOH C O   1 
HETATM 2403 O O   . HOH P 5 .  ? 20.001  -19.852 29.725  1.00 64.86  ? 206 HOH C O   1 
HETATM 2404 O O   . HOH P 5 .  ? 26.852  -25.717 32.254  1.00 103.92 ? 207 HOH C O   1 
HETATM 2405 O O   . HOH P 5 .  ? 12.308  -28.075 28.130  1.00 59.47  ? 208 HOH C O   1 
HETATM 2406 O O   . HOH P 5 .  ? 16.199  -37.572 20.154  1.00 53.97  ? 209 HOH C O   1 
HETATM 2407 O O   . HOH P 5 .  ? 8.827   -19.005 23.373  1.00 61.46  ? 210 HOH C O   1 
HETATM 2408 O O   . HOH P 5 .  ? 8.778   -36.677 18.251  1.00 59.79  ? 211 HOH C O   1 
HETATM 2409 O O   . HOH P 5 .  ? 14.417  -22.551 25.242  1.00 151.84 ? 212 HOH C O   1 
HETATM 2410 O O   . HOH P 5 .  ? 33.233  -24.226 31.532  1.00 61.38  ? 213 HOH C O   1 
HETATM 2411 O O   . HOH P 5 .  ? 7.866   -31.506 12.309  1.00 52.19  ? 214 HOH C O   1 
HETATM 2412 O O   . HOH P 5 .  ? 19.447  -20.068 10.602  1.00 49.21  ? 215 HOH C O   1 
HETATM 2413 O O   . HOH P 5 .  ? 17.464  -16.936 15.101  1.00 54.20  ? 216 HOH C O   1 
HETATM 2414 O O   . HOH P 5 .  ? 28.177  -36.974 15.845  1.00 48.51  ? 217 HOH C O   1 
HETATM 2415 O O   . HOH P 5 .  ? 5.503   -26.844 16.740  1.00 57.22  ? 218 HOH C O   1 
HETATM 2416 O O   . HOH P 5 .  ? 15.318  -17.587 19.491  1.00 52.34  ? 219 HOH C O   1 
HETATM 2417 O O   . HOH P 5 .  ? 15.470  -21.198 12.673  1.00 51.57  ? 220 HOH C O   1 
HETATM 2418 O O   . HOH P 5 .  ? 15.594  -16.586 24.351  1.00 81.20  ? 221 HOH C O   1 
HETATM 2419 O O   . HOH P 5 .  ? 14.276  -37.042 13.674  1.00 51.98  ? 222 HOH C O   1 
HETATM 2420 O O   . HOH P 5 .  ? 30.492  -40.476 9.486   1.00 50.99  ? 223 HOH C O   1 
HETATM 2421 O O   . HOH P 5 .  ? 23.084  -41.400 18.406  1.00 52.06  ? 224 HOH C O   1 
HETATM 2422 O O   . HOH P 5 .  ? 30.481  -17.590 9.641   1.00 50.23  ? 225 HOH C O   1 
HETATM 2423 O O   . HOH P 5 .  ? 25.476  -33.699 34.847  1.00 63.23  ? 226 HOH C O   1 
HETATM 2424 O O   . HOH P 5 .  ? 14.523  -39.023 16.832  1.00 60.68  ? 227 HOH C O   1 
HETATM 2425 O O   . HOH P 5 .  ? 12.919  -31.433 8.245   1.00 40.76  ? 228 HOH C O   1 
HETATM 2426 O O   . HOH P 5 .  ? 27.767  -37.427 25.082  1.00 69.86  ? 229 HOH C O   1 
HETATM 2427 O O   . HOH P 5 .  ? 20.251  -41.754 12.203  1.00 37.48  ? 230 HOH C O   1 
HETATM 2428 O O   . HOH P 5 .  ? 7.045   -18.146 10.713  1.00 46.05  ? 231 HOH C O   1 
HETATM 2429 O O   . HOH P 5 .  ? 25.384  -31.173 10.870  1.00 45.55  ? 232 HOH C O   1 
HETATM 2430 O O   . HOH P 5 .  ? 22.215  -34.239 16.619  1.00 34.08  ? 233 HOH C O   1 
HETATM 2431 O O   . HOH P 5 .  ? 13.224  -22.692 27.927  1.00 69.85  ? 234 HOH C O   1 
HETATM 2432 O O   . HOH P 5 .  ? 30.491  -31.153 15.675  1.00 50.79  ? 235 HOH C O   1 
HETATM 2433 O O   . HOH P 5 .  ? 20.728  -39.835 26.435  1.00 49.33  ? 236 HOH C O   1 
HETATM 2434 O O   . HOH P 5 .  ? 2.788   -28.475 13.977  1.00 65.48  ? 237 HOH C O   1 
HETATM 2435 O O   . HOH P 5 .  ? 31.185  -39.620 27.141  1.00 57.83  ? 238 HOH C O   1 
HETATM 2436 O O   . HOH P 5 .  ? 29.916  -39.631 31.375  1.00 50.44  ? 239 HOH C O   1 
HETATM 2437 O O   . HOH P 5 .  ? 22.301  -28.455 11.114  1.00 38.17  ? 240 HOH C O   1 
HETATM 2438 O O   . HOH P 5 .  ? 19.244  -26.857 3.125   1.00 53.40  ? 241 HOH C O   1 
HETATM 2439 O O   . HOH P 5 .  ? 21.699  -18.083 21.990  1.00 61.37  ? 242 HOH C O   1 
HETATM 2440 O O   . HOH P 5 .  ? 22.868  -21.772 7.521   1.00 48.38  ? 243 HOH C O   1 
HETATM 2441 O O   . HOH P 5 .  ? 31.848  -33.285 26.016  1.00 55.32  ? 244 HOH C O   1 
HETATM 2442 O O   . HOH P 5 .  ? 21.034  -28.583 8.625   1.00 44.60  ? 245 HOH C O   1 
HETATM 2443 O O   . HOH P 5 .  ? 30.266  -35.664 28.688  1.00 64.55  ? 246 HOH C O   1 
HETATM 2444 O O   . HOH P 5 .  ? 30.747  -28.922 12.244  1.00 60.33  ? 247 HOH C O   1 
HETATM 2445 O O   . HOH P 5 .  ? 13.781  -38.664 9.113   1.00 63.70  ? 248 HOH C O   1 
HETATM 2446 O O   . HOH P 5 .  ? 31.712  -43.205 15.883  1.00 59.75  ? 249 HOH C O   1 
HETATM 2447 O O   . HOH P 5 .  ? 21.096  -29.490 4.668   1.00 69.91  ? 250 HOH C O   1 
HETATM 2448 O O   . HOH P 5 .  ? 25.947  -17.375 13.964  1.00 53.21  ? 251 HOH C O   1 
HETATM 2449 O O   . HOH P 5 .  ? 25.696  -39.558 20.195  1.00 47.20  ? 252 HOH C O   1 
HETATM 2450 O O   . HOH P 5 .  ? 12.774  -38.671 24.022  1.00 60.19  ? 253 HOH C O   1 
HETATM 2451 O O   . HOH P 5 .  ? 20.156  -18.834 24.837  1.00 65.92  ? 254 HOH C O   1 
HETATM 2452 O O   . HOH P 5 .  ? 31.988  -43.401 11.969  1.00 64.62  ? 255 HOH C O   1 
HETATM 2453 O O   . HOH P 5 .  ? 28.294  -14.964 13.023  1.00 67.79  ? 256 HOH C O   1 
HETATM 2454 O O   . HOH P 5 .  ? 30.391  -32.656 18.305  1.00 56.89  ? 257 HOH C O   1 
HETATM 2455 O O   . HOH P 5 .  ? 25.267  -17.588 21.648  1.00 72.40  ? 258 HOH C O   1 
HETATM 2456 O O   . HOH P 5 .  ? 20.558  -12.876 13.431  1.00 59.47  ? 259 HOH C O   1 
HETATM 2457 O O   . HOH P 5 .  ? 4.627   -23.684 18.647  1.00 73.35  ? 260 HOH C O   1 
HETATM 2458 O O   . HOH P 5 .  ? 17.276  -37.770 28.572  1.00 72.03  ? 261 HOH C O   1 
HETATM 2459 O O   . HOH P 5 .  ? 16.970  -39.617 21.784  1.00 58.33  ? 262 HOH C O   1 
HETATM 2460 O O   . HOH P 5 .  ? 28.785  -25.043 33.173  1.00 65.26  ? 263 HOH C O   1 
HETATM 2461 O O   . HOH P 5 .  ? 29.234  -41.525 27.201  1.00 53.37  ? 264 HOH C O   1 
HETATM 2462 O O   . HOH P 5 .  ? 21.832  -33.656 7.228   1.00 64.93  ? 265 HOH C O   1 
HETATM 2463 O O   . HOH P 5 .  ? 11.974  -21.125 10.694  1.00 50.25  ? 266 HOH C O   1 
HETATM 2464 O O   . HOH P 5 .  ? 22.661  -13.873 13.534  1.00 61.34  ? 267 HOH C O   1 
HETATM 2465 O O   . HOH P 5 .  ? 23.923  -15.698 12.155  1.00 57.85  ? 268 HOH C O   1 
HETATM 2466 O O   . HOH P 5 .  ? 29.133  -29.770 10.000  1.00 71.99  ? 269 HOH C O   1 
HETATM 2467 O O   . HOH P 5 .  ? 28.511  -41.561 29.868  1.00 50.32  ? 270 HOH C O   1 
HETATM 2468 O O   . HOH P 5 .  ? 37.222  -23.742 27.177  1.00 81.60  ? 271 HOH C O   1 
HETATM 2469 O O   . HOH P 5 .  ? 33.589  -44.388 15.347  1.00 48.36  ? 272 HOH C O   1 
HETATM 2470 O O   . HOH P 5 .  ? 22.360  -39.731 22.482  1.00 66.23  ? 273 HOH C O   1 
HETATM 2471 O O   . HOH P 5 .  ? 20.902  -40.603 19.593  1.00 53.53  ? 274 HOH C O   1 
HETATM 2472 O O   . HOH P 5 .  ? 24.498  -29.065 9.322   1.00 48.68  ? 275 HOH C O   1 
HETATM 2473 O O   . HOH P 5 .  ? 20.153  -37.451 40.442  1.00 67.18  ? 276 HOH C O   1 
HETATM 2474 O O   . HOH P 5 .  ? 20.368  -41.030 39.603  1.00 69.72  ? 277 HOH C O   1 
# 
