data_7HG7
# 
_entry.id   7HG7 
# 
_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   7HG7         pdb_00007hg7 10.2210/pdb7hg7/pdb 
WWPDB D_1001407433 ?            ?                   
# 
_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                        7HG7 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2'   10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                        96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                       62.068    2   ? ?    ? ? 
4 non-polymer syn '~{N}-(4-fluorophenyl)-2-pyrrolidin-1-yl-ethanamide' 222.259   1   ? ?    ? ? 
5 water       nat water                                                18.015    247 ? ?    ? ? 
# 
_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 '~{N}-(4-fluorophenyl)-2-pyrrolidin-1-yl-ethanamide' EJQ 
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  
EJQ non-polymer         . '~{N}-(4-fluorophenyl)-2-pyrrolidin-1-yl-ethanamide' ?                 'C12 H15 F N2 O' 222.259 
GLN 'L-peptide linking' y GLUTAMINE                                            ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                      ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                              ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                            ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                           ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                              ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                               ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                           ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                        ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                              ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                               ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                                        ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                                            ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                           ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                             ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                               ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 ?  ?   ?   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 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 29 ALA ALA 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        EJQ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   EJQ 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4 1   101 95  SO4 SO4 A . 
E 2 SO4 1   102 96  SO4 SO4 A . 
F 3 EDO 1   103 97  EDO EDO A . 
G 2 SO4 1   104 4   SO4 SO4 A . 
H 2 SO4 1   101 1   SO4 SO4 B . 
I 2 SO4 1   102 3   SO4 SO4 B . 
J 4 EJQ 1   103 101 EJQ LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 307 HOH HOH A . 
M 5 HOH 2   202 84  HOH HOH A . 
M 5 HOH 3   203 202 HOH HOH A . 
M 5 HOH 4   204 304 HOH HOH A . 
M 5 HOH 5   205 259 HOH HOH A . 
M 5 HOH 6   206 339 HOH HOH A . 
M 5 HOH 7   207 342 HOH HOH A . 
M 5 HOH 8   208 289 HOH HOH A . 
M 5 HOH 9   209 139 HOH HOH A . 
M 5 HOH 10  210 38  HOH HOH A . 
M 5 HOH 11  211 66  HOH HOH A . 
M 5 HOH 12  212 338 HOH HOH A . 
M 5 HOH 13  213 55  HOH HOH A . 
M 5 HOH 14  214 94  HOH HOH A . 
M 5 HOH 15  215 37  HOH HOH A . 
M 5 HOH 16  216 179 HOH HOH A . 
M 5 HOH 17  217 91  HOH HOH A . 
M 5 HOH 18  218 208 HOH HOH A . 
M 5 HOH 19  219 293 HOH HOH A . 
M 5 HOH 20  220 85  HOH HOH A . 
M 5 HOH 21  221 346 HOH HOH A . 
M 5 HOH 22  222 8   HOH HOH A . 
M 5 HOH 23  223 345 HOH HOH A . 
M 5 HOH 24  224 71  HOH HOH A . 
M 5 HOH 25  225 86  HOH HOH A . 
M 5 HOH 26  226 93  HOH HOH A . 
M 5 HOH 27  227 26  HOH HOH A . 
M 5 HOH 28  228 28  HOH HOH A . 
M 5 HOH 29  229 116 HOH HOH A . 
M 5 HOH 30  230 290 HOH HOH A . 
M 5 HOH 31  231 34  HOH HOH A . 
M 5 HOH 32  232 87  HOH HOH A . 
M 5 HOH 33  233 167 HOH HOH A . 
M 5 HOH 34  234 23  HOH HOH A . 
M 5 HOH 35  235 32  HOH HOH A . 
M 5 HOH 36  236 97  HOH HOH A . 
M 5 HOH 37  237 78  HOH HOH A . 
M 5 HOH 38  238 111 HOH HOH A . 
M 5 HOH 39  239 7   HOH HOH A . 
M 5 HOH 40  240 260 HOH HOH A . 
M 5 HOH 41  241 292 HOH HOH A . 
M 5 HOH 42  242 274 HOH HOH A . 
M 5 HOH 43  243 41  HOH HOH A . 
M 5 HOH 44  244 188 HOH HOH A . 
M 5 HOH 45  245 99  HOH HOH A . 
M 5 HOH 46  246 60  HOH HOH A . 
M 5 HOH 47  247 190 HOH HOH A . 
M 5 HOH 48  248 21  HOH HOH A . 
M 5 HOH 49  249 2   HOH HOH A . 
M 5 HOH 50  250 287 HOH HOH A . 
M 5 HOH 51  251 12  HOH HOH A . 
M 5 HOH 52  252 1   HOH HOH A . 
M 5 HOH 53  253 95  HOH HOH A . 
M 5 HOH 54  254 222 HOH HOH A . 
M 5 HOH 55  255 267 HOH HOH A . 
M 5 HOH 56  256 165 HOH HOH A . 
M 5 HOH 57  257 18  HOH HOH A . 
M 5 HOH 58  258 199 HOH HOH A . 
M 5 HOH 59  259 300 HOH HOH A . 
M 5 HOH 60  260 27  HOH HOH A . 
M 5 HOH 61  261 288 HOH HOH A . 
M 5 HOH 62  262 299 HOH HOH A . 
M 5 HOH 63  263 203 HOH HOH A . 
M 5 HOH 64  264 109 HOH HOH A . 
M 5 HOH 65  265 58  HOH HOH A . 
M 5 HOH 66  266 145 HOH HOH A . 
M 5 HOH 67  267 341 HOH HOH A . 
M 5 HOH 68  268 77  HOH HOH A . 
M 5 HOH 69  269 143 HOH HOH A . 
M 5 HOH 70  270 164 HOH HOH A . 
M 5 HOH 71  271 20  HOH HOH A . 
M 5 HOH 72  272 31  HOH HOH A . 
M 5 HOH 73  273 42  HOH HOH A . 
M 5 HOH 74  274 14  HOH HOH A . 
M 5 HOH 75  275 278 HOH HOH A . 
M 5 HOH 76  276 297 HOH HOH A . 
M 5 HOH 77  277 9   HOH HOH A . 
M 5 HOH 78  278 115 HOH HOH A . 
M 5 HOH 79  279 16  HOH HOH A . 
M 5 HOH 80  280 47  HOH HOH A . 
M 5 HOH 81  281 73  HOH HOH A . 
M 5 HOH 82  282 19  HOH HOH A . 
M 5 HOH 83  283 301 HOH HOH A . 
M 5 HOH 84  284 152 HOH HOH A . 
M 5 HOH 85  285 281 HOH HOH A . 
M 5 HOH 86  286 218 HOH HOH A . 
M 5 HOH 87  287 327 HOH HOH A . 
M 5 HOH 88  288 64  HOH HOH A . 
M 5 HOH 89  289 131 HOH HOH A . 
M 5 HOH 90  290 113 HOH HOH A . 
M 5 HOH 91  291 318 HOH HOH A . 
M 5 HOH 92  292 22  HOH HOH A . 
M 5 HOH 93  293 210 HOH HOH A . 
M 5 HOH 94  294 270 HOH HOH A . 
M 5 HOH 95  295 296 HOH HOH A . 
M 5 HOH 96  296 83  HOH HOH A . 
M 5 HOH 97  297 347 HOH HOH A . 
M 5 HOH 98  298 211 HOH HOH A . 
M 5 HOH 99  299 63  HOH HOH A . 
M 5 HOH 100 300 185 HOH HOH A . 
M 5 HOH 101 301 205 HOH HOH A . 
M 5 HOH 102 302 219 HOH HOH A . 
M 5 HOH 103 303 283 HOH HOH A . 
M 5 HOH 104 304 57  HOH HOH A . 
M 5 HOH 105 305 156 HOH HOH A . 
M 5 HOH 106 306 35  HOH HOH A . 
M 5 HOH 107 307 75  HOH HOH A . 
M 5 HOH 108 308 125 HOH HOH A . 
M 5 HOH 109 309 332 HOH HOH A . 
N 5 HOH 1   201 331 HOH HOH B . 
N 5 HOH 2   202 272 HOH HOH B . 
N 5 HOH 3   203 343 HOH HOH B . 
N 5 HOH 4   204 340 HOH HOH B . 
N 5 HOH 5   205 123 HOH HOH B . 
N 5 HOH 6   206 89  HOH HOH B . 
N 5 HOH 7   207 258 HOH HOH B . 
N 5 HOH 8   208 279 HOH HOH B . 
N 5 HOH 9   209 247 HOH HOH B . 
N 5 HOH 10  210 98  HOH HOH B . 
N 5 HOH 11  211 249 HOH HOH B . 
N 5 HOH 12  212 150 HOH HOH B . 
N 5 HOH 13  213 334 HOH HOH B . 
N 5 HOH 14  214 172 HOH HOH B . 
N 5 HOH 15  215 69  HOH HOH B . 
N 5 HOH 16  216 59  HOH HOH B . 
N 5 HOH 17  217 329 HOH HOH B . 
N 5 HOH 18  218 54  HOH HOH B . 
N 5 HOH 19  219 137 HOH HOH B . 
N 5 HOH 20  220 242 HOH HOH B . 
N 5 HOH 21  221 215 HOH HOH B . 
N 5 HOH 22  222 61  HOH HOH B . 
N 5 HOH 23  223 169 HOH HOH B . 
N 5 HOH 24  224 223 HOH HOH B . 
N 5 HOH 25  225 280 HOH HOH B . 
N 5 HOH 26  226 157 HOH HOH B . 
N 5 HOH 27  227 6   HOH HOH B . 
N 5 HOH 28  228 117 HOH HOH B . 
N 5 HOH 29  229 17  HOH HOH B . 
N 5 HOH 30  230 24  HOH HOH B . 
N 5 HOH 31  231 10  HOH HOH B . 
N 5 HOH 32  232 96  HOH HOH B . 
N 5 HOH 33  233 68  HOH HOH B . 
N 5 HOH 34  234 74  HOH HOH B . 
N 5 HOH 35  235 261 HOH HOH B . 
N 5 HOH 36  236 175 HOH HOH B . 
N 5 HOH 37  237 5   HOH HOH B . 
N 5 HOH 38  238 119 HOH HOH B . 
N 5 HOH 39  239 320 HOH HOH B . 
N 5 HOH 40  240 344 HOH HOH B . 
N 5 HOH 41  241 25  HOH HOH B . 
N 5 HOH 42  242 168 HOH HOH B . 
N 5 HOH 43  243 101 HOH HOH B . 
N 5 HOH 44  244 333 HOH HOH B . 
N 5 HOH 45  245 315 HOH HOH B . 
N 5 HOH 46  246 76  HOH HOH B . 
N 5 HOH 47  247 79  HOH HOH B . 
N 5 HOH 48  248 336 HOH HOH B . 
N 5 HOH 49  249 170 HOH HOH B . 
N 5 HOH 50  250 197 HOH HOH B . 
N 5 HOH 51  251 153 HOH HOH B . 
N 5 HOH 52  252 36  HOH HOH B . 
N 5 HOH 53  253 217 HOH HOH B . 
N 5 HOH 54  254 13  HOH HOH B . 
N 5 HOH 55  255 120 HOH HOH B . 
N 5 HOH 56  256 182 HOH HOH B . 
N 5 HOH 57  257 224 HOH HOH B . 
N 5 HOH 58  258 46  HOH HOH B . 
N 5 HOH 59  259 44  HOH HOH B . 
N 5 HOH 60  260 214 HOH HOH B . 
N 5 HOH 61  261 72  HOH HOH B . 
N 5 HOH 62  262 104 HOH HOH B . 
N 5 HOH 63  263 303 HOH HOH B . 
N 5 HOH 64  264 322 HOH HOH B . 
N 5 HOH 65  265 177 HOH HOH B . 
N 5 HOH 66  266 319 HOH HOH B . 
N 5 HOH 67  267 163 HOH HOH B . 
N 5 HOH 68  268 160 HOH HOH B . 
N 5 HOH 69  269 291 HOH HOH B . 
N 5 HOH 70  270 316 HOH HOH B . 
N 5 HOH 71  271 201 HOH HOH B . 
N 5 HOH 72  272 70  HOH HOH B . 
N 5 HOH 73  273 107 HOH HOH B . 
N 5 HOH 74  274 314 HOH HOH B . 
N 5 HOH 75  275 335 HOH HOH B . 
N 5 HOH 76  276 313 HOH HOH B . 
N 5 HOH 77  277 312 HOH HOH B . 
O 5 HOH 1   201 254 HOH HOH C . 
O 5 HOH 2   202 321 HOH HOH C . 
O 5 HOH 3   203 323 HOH HOH C . 
O 5 HOH 4   204 161 HOH HOH C . 
O 5 HOH 5   205 173 HOH HOH C . 
O 5 HOH 6   206 226 HOH HOH C . 
O 5 HOH 7   207 271 HOH HOH C . 
O 5 HOH 8   208 269 HOH HOH C . 
O 5 HOH 9   209 118 HOH HOH C . 
O 5 HOH 10  210 184 HOH HOH C . 
O 5 HOH 11  211 15  HOH HOH C . 
O 5 HOH 12  212 90  HOH HOH C . 
O 5 HOH 13  213 189 HOH HOH C . 
O 5 HOH 14  214 45  HOH HOH C . 
O 5 HOH 15  215 337 HOH HOH C . 
O 5 HOH 16  216 302 HOH HOH C . 
O 5 HOH 17  217 142 HOH HOH C . 
O 5 HOH 18  218 134 HOH HOH C . 
O 5 HOH 19  219 209 HOH HOH C . 
O 5 HOH 20  220 317 HOH HOH C . 
O 5 HOH 21  221 49  HOH HOH C . 
O 5 HOH 22  222 126 HOH HOH C . 
O 5 HOH 23  223 102 HOH HOH C . 
O 5 HOH 24  224 82  HOH HOH C . 
O 5 HOH 25  225 309 HOH HOH C . 
O 5 HOH 26  226 43  HOH HOH C . 
O 5 HOH 27  227 4   HOH HOH C . 
O 5 HOH 28  228 325 HOH HOH C . 
O 5 HOH 29  229 132 HOH HOH C . 
O 5 HOH 30  230 40  HOH HOH C . 
O 5 HOH 31  231 56  HOH HOH C . 
O 5 HOH 32  232 149 HOH HOH C . 
O 5 HOH 33  233 328 HOH HOH C . 
O 5 HOH 34  234 284 HOH HOH C . 
O 5 HOH 35  235 53  HOH HOH C . 
O 5 HOH 36  236 48  HOH HOH C . 
O 5 HOH 37  237 148 HOH HOH C . 
O 5 HOH 38  238 62  HOH HOH C . 
O 5 HOH 39  239 198 HOH HOH C . 
O 5 HOH 40  240 122 HOH HOH C . 
O 5 HOH 41  241 298 HOH HOH C . 
O 5 HOH 42  242 326 HOH HOH C . 
O 5 HOH 43  243 151 HOH HOH C . 
O 5 HOH 44  244 135 HOH HOH C . 
O 5 HOH 45  245 130 HOH HOH C . 
O 5 HOH 46  246 275 HOH HOH C . 
O 5 HOH 47  247 65  HOH HOH C . 
O 5 HOH 48  248 67  HOH HOH C . 
O 5 HOH 49  249 294 HOH HOH C . 
O 5 HOH 50  250 146 HOH HOH C . 
O 5 HOH 51  251 330 HOH HOH C . 
O 5 HOH 52  252 305 HOH HOH C . 
O 5 HOH 53  253 241 HOH HOH C . 
O 5 HOH 54  254 246 HOH HOH C . 
O 5 HOH 55  255 108 HOH HOH C . 
O 5 HOH 56  256 324 HOH HOH C . 
O 5 HOH 57  257 171 HOH HOH C . 
O 5 HOH 58  258 103 HOH HOH C . 
O 5 HOH 59  259 92  HOH HOH C . 
O 5 HOH 60  260 206 HOH HOH C . 
O 5 HOH 61  261 310 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 ASP 62 ? CG  ? A ASP 63 CG  
4  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
5  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
6  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
7  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
8  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
9  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
10 1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
11 1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
12 1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
13 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
14 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
15 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
16 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
17 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
18 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
19 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
20 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
21 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
22 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
23 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
24 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
25 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
26 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
27 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
28 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
29 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
30 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
31 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
32 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
33 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
34 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
35 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
36 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
37 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
38 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
39 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
40 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
41 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
42 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
43 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
44 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
45 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
46 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
47 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
48 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
49 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
50 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
51 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
52 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
53 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
54 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
55 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
56 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
57 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
58 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HG7 
_cell.length_a           41.600 
_cell.length_b           42.170 
_cell.length_c           158.520 
_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                         7HG7 
_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          7HG7 
_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                     7HG7 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             52.84 
_reflns.d_resolution_high            1.76 
_reflns.number_obs                   28581 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.094 
_reflns.pdbx_netI_over_sigmaI        9.8 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.103 
_reflns.pdbx_Rpim_I_all              0.041 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     180840 
_reflns.pdbx_chi_squared             0.98 
_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                  1.76 
_reflns_shell.d_res_low                   1.81 
_reflns_shell.number_measured_all         14029 
_reflns_shell.number_unique_obs           2080 
_reflns_shell.Rmerge_I_obs                2.558 
_reflns_shell.pdbx_chi_squared            0.86 
_reflns_shell.pdbx_redundancy             6.7 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             2.770 
_reflns_shell.pdbx_Rpim_I_all             1.052 
_reflns_shell.pdbx_CC_half                0.370 
_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                                 7HG7 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     27053 
_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                             40.79 
_refine.ls_d_res_high                            1.76 
_refine.ls_percent_reflns_obs                    99.76 
_refine.ls_R_factor_obs                          0.20601 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20379 
_refine.ls_R_factor_R_free                       0.24505 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1466 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.952 
_refine.B_iso_mean                               39.332 
_refine.aniso_B[1][1]                            0.42 
_refine.aniso_B[2][2]                            0.11 
_refine.aniso_B[3][3]                            -0.53 
_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                       0.137 
_refine.pdbx_overall_ESU_R_Free                  0.132 
_refine.overall_SU_ML                            0.120 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.068 
_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        2125 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.number_atoms_solvent             247 
_refine_hist.number_atoms_total               2426 
_refine_hist.d_res_high                       1.76 
_refine_hist.d_res_low                        40.79 
# 
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  ? 2281 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.678  1.831  ? 3102 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.036  5.000  ? 264  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       6.625  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.753 10.000 ? 297  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.123  0.200  ? 286  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1890 '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                  3.529  3.712  ? 1068 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.878  6.628  ? 1329 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.462  4.000  ? 1213 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.339  55.29  ? 3528 '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                       1.760 
_refine_ls_shell.d_res_low                        1.806 
_refine_ls_shell.number_reflns_R_work             1966 
_refine_ls_shell.R_factor_R_work                  0.360 
_refine_ls_shell.percent_reflns_obs               99.76 
_refine_ls_shell.R_factor_R_free                  0.348 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             106 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HG7 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z46169164' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HG7 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HG7 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HG7 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HG7 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 7HG7 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HG7 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HG7 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HG7 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HG7 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HG7 SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O TRP C 22 ? O TRP C 21 N ALA C 14 ? N ALA C 13 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HG7 
_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 225 ? ? O B HOH 264 ? ? 1.70 
2  1 O   A HOH 262 ? ? O C HOH 215 ? ? 1.78 
3  1 O2  C SO4 102 ? ? O C HOH 201 ? ? 1.94 
4  1 O   C HOH 250 ? ? O C HOH 256 ? ? 2.00 
5  1 O   B HOH 203 ? ? O B HOH 259 ? ? 2.01 
6  1 O   A HOH 244 ? ? O A HOH 301 ? ? 2.07 
7  1 O2  C SO4 102 ? ? O C HOH 202 ? ? 2.07 
8  1 OD1 C ASP 9   ? ? O C HOH 203 ? ? 2.10 
9  1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.13 
10 1 O   A PRO 37  ? ? O A HOH 202 ? ? 2.15 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 253 ? ? 1_555 O A HOH 279 ? ? 4_545 2.04 
2 1 O A HOH 303 ? ? 1_555 O A HOH 306 ? ? 4_445 2.12 
3 1 O A HOH 241 ? ? 1_555 O A HOH 254 ? ? 4_545 2.16 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 38 ? ? 74.13   -0.75 
2 1 ASN A 87 ? ? -156.42 65.29 
3 1 ASN B 38 ? ? 75.50   -8.19 
4 1 ASN B 87 ? ? -158.49 58.25 
5 1 ASN C 87 ? ? -153.51 52.82 
# 
_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            0.088 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       309 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.25 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 ILE 28 ? B ILE 29 
4  1 Y 1 B ALA 29 ? B ALA 30 
5  1 Y 1 B ASP 30 ? B ASP 31 
6  1 Y 1 B GLY 31 ? B GLY 32 
7  1 Y 1 B ALA 32 ? B ALA 33 
8  1 Y 1 C GLY 0  ? C GLY 1  
9  1 Y 1 C MET 1  ? C MET 2  
10 1 Y 1 C PRO 2  ? C PRO 3  
11 1 Y 1 C ASP 30 ? C ASP 31 
12 1 Y 1 C GLY 31 ? C GLY 32 
13 1 Y 1 C ALA 32 ? C ALA 33 
14 1 Y 1 C VAL 33 ? C VAL 34 
15 1 Y 1 C LYS 34 ? C LYS 35 
16 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
EJQ C10  C N N 98  
EJQ C13  C N N 99  
EJQ C15  C N N 100 
EJQ C01  C Y N 101 
EJQ C02  C Y N 102 
EJQ C03  C Y N 103 
EJQ C04  C Y N 104 
EJQ C05  C Y N 105 
EJQ C06  C Y N 106 
EJQ C08  C N N 107 
EJQ C12  C N N 108 
EJQ C14  C N N 109 
EJQ F16  F N N 110 
EJQ N07  N N N 111 
EJQ N11  N N N 112 
EJQ O09  O N N 113 
EJQ H1   H N N 114 
EJQ H2   H N N 115 
EJQ H3   H N N 116 
EJQ H4   H N N 117 
EJQ H5   H N N 118 
EJQ H6   H N N 119 
EJQ H7   H N N 120 
EJQ H8   H N N 121 
EJQ H9   H N N 122 
EJQ H10  H N N 123 
EJQ H11  H N N 124 
EJQ H12  H N N 125 
EJQ H13  H N N 126 
EJQ H14  H N N 127 
EJQ H15  H N N 128 
GLN N    N N N 129 
GLN CA   C N S 130 
GLN C    C N N 131 
GLN O    O N N 132 
GLN CB   C N N 133 
GLN CG   C N N 134 
GLN CD   C N N 135 
GLN OE1  O N N 136 
GLN NE2  N N N 137 
GLN OXT  O N N 138 
GLN H    H N N 139 
GLN H2   H N N 140 
GLN HA   H N N 141 
GLN HB2  H N N 142 
GLN HB3  H N N 143 
GLN HG2  H N N 144 
GLN HG3  H N N 145 
GLN HE21 H N N 146 
GLN HE22 H N N 147 
GLN HXT  H N N 148 
GLU N    N N N 149 
GLU CA   C N S 150 
GLU C    C N N 151 
GLU O    O N N 152 
GLU CB   C N N 153 
GLU CG   C N N 154 
GLU CD   C N N 155 
GLU OE1  O N N 156 
GLU OE2  O N N 157 
GLU OXT  O N N 158 
GLU H    H N N 159 
GLU H2   H N N 160 
GLU HA   H N N 161 
GLU HB2  H N N 162 
GLU HB3  H N N 163 
GLU HG2  H N N 164 
GLU HG3  H N N 165 
GLU HE2  H N N 166 
GLU HXT  H N N 167 
GLY N    N N N 168 
GLY CA   C N N 169 
GLY C    C N N 170 
GLY O    O N N 171 
GLY OXT  O N N 172 
GLY H    H N N 173 
GLY H2   H N N 174 
GLY HA2  H N N 175 
GLY HA3  H N N 176 
GLY HXT  H N N 177 
HIS N    N N N 178 
HIS CA   C N S 179 
HIS C    C N N 180 
HIS O    O N N 181 
HIS CB   C N N 182 
HIS CG   C Y N 183 
HIS ND1  N Y N 184 
HIS CD2  C Y N 185 
HIS CE1  C Y N 186 
HIS NE2  N Y N 187 
HIS OXT  O N N 188 
HIS H    H N N 189 
HIS H2   H N N 190 
HIS HA   H N N 191 
HIS HB2  H N N 192 
HIS HB3  H N N 193 
HIS HD1  H N N 194 
HIS HD2  H N N 195 
HIS HE1  H N N 196 
HIS HE2  H N N 197 
HIS HXT  H N N 198 
HOH O    O N N 199 
HOH H1   H N N 200 
HOH H2   H N N 201 
ILE N    N N N 202 
ILE CA   C N S 203 
ILE C    C N N 204 
ILE O    O N N 205 
ILE CB   C N S 206 
ILE CG1  C N N 207 
ILE CG2  C N N 208 
ILE CD1  C N N 209 
ILE OXT  O N N 210 
ILE H    H N N 211 
ILE H2   H N N 212 
ILE HA   H N N 213 
ILE HB   H N N 214 
ILE HG12 H N N 215 
ILE HG13 H N N 216 
ILE HG21 H N N 217 
ILE HG22 H N N 218 
ILE HG23 H N N 219 
ILE HD11 H N N 220 
ILE HD12 H N N 221 
ILE HD13 H N N 222 
ILE HXT  H N N 223 
LEU N    N N N 224 
LEU CA   C N S 225 
LEU C    C N N 226 
LEU O    O N N 227 
LEU CB   C N N 228 
LEU CG   C N N 229 
LEU CD1  C N N 230 
LEU CD2  C N N 231 
LEU OXT  O N N 232 
LEU H    H N N 233 
LEU H2   H N N 234 
LEU HA   H N N 235 
LEU HB2  H N N 236 
LEU HB3  H N N 237 
LEU HG   H N N 238 
LEU HD11 H N N 239 
LEU HD12 H N N 240 
LEU HD13 H N N 241 
LEU HD21 H N N 242 
LEU HD22 H N N 243 
LEU HD23 H N N 244 
LEU HXT  H N N 245 
LYS N    N N N 246 
LYS CA   C N S 247 
LYS C    C N N 248 
LYS O    O N N 249 
LYS CB   C N N 250 
LYS CG   C N N 251 
LYS CD   C N N 252 
LYS CE   C N N 253 
LYS NZ   N N N 254 
LYS OXT  O N N 255 
LYS H    H N N 256 
LYS H2   H N N 257 
LYS HA   H N N 258 
LYS HB2  H N N 259 
LYS HB3  H N N 260 
LYS HG2  H N N 261 
LYS HG3  H N N 262 
LYS HD2  H N N 263 
LYS HD3  H N N 264 
LYS HE2  H N N 265 
LYS HE3  H N N 266 
LYS HZ1  H N N 267 
LYS HZ2  H N N 268 
LYS HZ3  H N N 269 
LYS HXT  H N N 270 
MET N    N N N 271 
MET CA   C N S 272 
MET C    C N N 273 
MET O    O N N 274 
MET CB   C N N 275 
MET CG   C N N 276 
MET SD   S N N 277 
MET CE   C N N 278 
MET OXT  O N N 279 
MET H    H N N 280 
MET H2   H N N 281 
MET HA   H N N 282 
MET HB2  H N N 283 
MET HB3  H N N 284 
MET HG2  H N N 285 
MET HG3  H N N 286 
MET HE1  H N N 287 
MET HE2  H N N 288 
MET HE3  H N N 289 
MET HXT  H N N 290 
PHE N    N N N 291 
PHE CA   C N S 292 
PHE C    C N N 293 
PHE O    O N N 294 
PHE CB   C N N 295 
PHE CG   C Y N 296 
PHE CD1  C Y N 297 
PHE CD2  C Y N 298 
PHE CE1  C Y N 299 
PHE CE2  C Y N 300 
PHE CZ   C Y N 301 
PHE OXT  O N N 302 
PHE H    H N N 303 
PHE H2   H N N 304 
PHE HA   H N N 305 
PHE HB2  H N N 306 
PHE HB3  H N N 307 
PHE HD1  H N N 308 
PHE HD2  H N N 309 
PHE HE1  H N N 310 
PHE HE2  H N N 311 
PHE HZ   H N N 312 
PHE HXT  H N N 313 
PRO N    N N N 314 
PRO CA   C N S 315 
PRO C    C N N 316 
PRO O    O N N 317 
PRO CB   C N N 318 
PRO CG   C N N 319 
PRO CD   C N N 320 
PRO OXT  O N N 321 
PRO H    H N N 322 
PRO HA   H N N 323 
PRO HB2  H N N 324 
PRO HB3  H N N 325 
PRO HG2  H N N 326 
PRO HG3  H N N 327 
PRO HD2  H N N 328 
PRO HD3  H N N 329 
PRO HXT  H N N 330 
SER N    N N N 331 
SER CA   C N S 332 
SER C    C N N 333 
SER O    O N N 334 
SER CB   C N N 335 
SER OG   O N N 336 
SER OXT  O N N 337 
SER H    H N N 338 
SER H2   H N N 339 
SER HA   H N N 340 
SER HB2  H N N 341 
SER HB3  H N N 342 
SER HG   H N N 343 
SER HXT  H N N 344 
SO4 S    S N N 345 
SO4 O1   O N N 346 
SO4 O2   O N N 347 
SO4 O3   O N N 348 
SO4 O4   O N N 349 
THR N    N N N 350 
THR CA   C N S 351 
THR C    C N N 352 
THR O    O N N 353 
THR CB   C N R 354 
THR OG1  O N N 355 
THR CG2  C N N 356 
THR OXT  O N N 357 
THR H    H N N 358 
THR H2   H N N 359 
THR HA   H N N 360 
THR HB   H N N 361 
THR HG1  H N N 362 
THR HG21 H N N 363 
THR HG22 H N N 364 
THR HG23 H N N 365 
THR HXT  H N N 366 
TRP N    N N N 367 
TRP CA   C N S 368 
TRP C    C N N 369 
TRP O    O N N 370 
TRP CB   C N N 371 
TRP CG   C Y N 372 
TRP CD1  C Y N 373 
TRP CD2  C Y N 374 
TRP NE1  N Y N 375 
TRP CE2  C Y N 376 
TRP CE3  C Y N 377 
TRP CZ2  C Y N 378 
TRP CZ3  C Y N 379 
TRP CH2  C Y N 380 
TRP OXT  O N N 381 
TRP H    H N N 382 
TRP H2   H N N 383 
TRP HA   H N N 384 
TRP HB2  H N N 385 
TRP HB3  H N N 386 
TRP HD1  H N N 387 
TRP HE1  H N N 388 
TRP HE3  H N N 389 
TRP HZ2  H N N 390 
TRP HZ3  H N N 391 
TRP HH2  H N N 392 
TRP HXT  H N N 393 
TYR N    N N N 394 
TYR CA   C N S 395 
TYR C    C N N 396 
TYR O    O N N 397 
TYR CB   C N N 398 
TYR CG   C Y N 399 
TYR CD1  C Y N 400 
TYR CD2  C Y N 401 
TYR CE1  C Y N 402 
TYR CE2  C Y N 403 
TYR CZ   C Y N 404 
TYR OH   O N N 405 
TYR OXT  O N N 406 
TYR H    H N N 407 
TYR H2   H N N 408 
TYR HA   H N N 409 
TYR HB2  H N N 410 
TYR HB3  H N N 411 
TYR HD1  H N N 412 
TYR HD2  H N N 413 
TYR HE1  H N N 414 
TYR HE2  H N N 415 
TYR HH   H N N 416 
TYR HXT  H N N 417 
VAL N    N N N 418 
VAL CA   C N S 419 
VAL C    C N N 420 
VAL O    O N N 421 
VAL CB   C N N 422 
VAL CG1  C N N 423 
VAL CG2  C N N 424 
VAL OXT  O N N 425 
VAL H    H N N 426 
VAL H2   H N N 427 
VAL HA   H N N 428 
VAL HB   H N N 429 
VAL HG11 H N N 430 
VAL HG12 H N N 431 
VAL HG13 H N N 432 
VAL HG21 H N N 433 
VAL HG22 H N N 434 
VAL HG23 H N N 435 
VAL HXT  H N N 436 
# 
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  
EJQ C15 C14  sing N N 92  
EJQ C15 N11  sing N N 93  
EJQ C10 C08  sing N N 94  
EJQ C10 N11  sing N N 95  
EJQ N07 C08  sing N N 96  
EJQ N07 C06  sing N N 97  
EJQ C14 C13  sing N N 98  
EJQ C08 O09  doub N N 99  
EJQ C06 C05  doub Y N 100 
EJQ C06 C01  sing Y N 101 
EJQ C05 C04  sing Y N 102 
EJQ N11 C12  sing N N 103 
EJQ C01 C02  doub Y N 104 
EJQ C04 C03  doub Y N 105 
EJQ C02 C03  sing Y N 106 
EJQ C03 F16  sing N N 107 
EJQ C12 C13  sing N N 108 
EJQ C10 H1   sing N N 109 
EJQ C10 H2   sing N N 110 
EJQ C13 H3   sing N N 111 
EJQ C13 H4   sing N N 112 
EJQ C15 H5   sing N N 113 
EJQ C15 H6   sing N N 114 
EJQ C01 H7   sing N N 115 
EJQ C02 H8   sing N N 116 
EJQ C04 H9   sing N N 117 
EJQ C05 H10  sing N N 118 
EJQ C12 H11  sing N N 119 
EJQ C12 H12  sing N N 120 
EJQ C14 H13  sing N N 121 
EJQ C14 H14  sing N N 122 
EJQ N07 H15  sing N N 123 
GLN N   CA   sing N N 124 
GLN N   H    sing N N 125 
GLN N   H2   sing N N 126 
GLN CA  C    sing N N 127 
GLN CA  CB   sing N N 128 
GLN CA  HA   sing N N 129 
GLN C   O    doub N N 130 
GLN C   OXT  sing N N 131 
GLN CB  CG   sing N N 132 
GLN CB  HB2  sing N N 133 
GLN CB  HB3  sing N N 134 
GLN CG  CD   sing N N 135 
GLN CG  HG2  sing N N 136 
GLN CG  HG3  sing N N 137 
GLN CD  OE1  doub N N 138 
GLN CD  NE2  sing N N 139 
GLN NE2 HE21 sing N N 140 
GLN NE2 HE22 sing N N 141 
GLN OXT HXT  sing N N 142 
GLU N   CA   sing N N 143 
GLU N   H    sing N N 144 
GLU N   H2   sing N N 145 
GLU CA  C    sing N N 146 
GLU CA  CB   sing N N 147 
GLU CA  HA   sing N N 148 
GLU C   O    doub N N 149 
GLU C   OXT  sing N N 150 
GLU CB  CG   sing N N 151 
GLU CB  HB2  sing N N 152 
GLU CB  HB3  sing N N 153 
GLU CG  CD   sing N N 154 
GLU CG  HG2  sing N N 155 
GLU CG  HG3  sing N N 156 
GLU CD  OE1  doub N N 157 
GLU CD  OE2  sing N N 158 
GLU OE2 HE2  sing N N 159 
GLU OXT HXT  sing N N 160 
GLY N   CA   sing N N 161 
GLY N   H    sing N N 162 
GLY N   H2   sing N N 163 
GLY CA  C    sing N N 164 
GLY CA  HA2  sing N N 165 
GLY CA  HA3  sing N N 166 
GLY C   O    doub N N 167 
GLY C   OXT  sing N N 168 
GLY OXT HXT  sing N N 169 
HIS N   CA   sing N N 170 
HIS N   H    sing N N 171 
HIS N   H2   sing N N 172 
HIS CA  C    sing N N 173 
HIS CA  CB   sing N N 174 
HIS CA  HA   sing N N 175 
HIS C   O    doub N N 176 
HIS C   OXT  sing N N 177 
HIS CB  CG   sing N N 178 
HIS CB  HB2  sing N N 179 
HIS CB  HB3  sing N N 180 
HIS CG  ND1  sing Y N 181 
HIS CG  CD2  doub Y N 182 
HIS ND1 CE1  doub Y N 183 
HIS ND1 HD1  sing N N 184 
HIS CD2 NE2  sing Y N 185 
HIS CD2 HD2  sing N N 186 
HIS CE1 NE2  sing Y N 187 
HIS CE1 HE1  sing N N 188 
HIS NE2 HE2  sing N N 189 
HIS OXT HXT  sing N N 190 
HOH O   H1   sing N N 191 
HOH O   H2   sing N N 192 
ILE N   CA   sing N N 193 
ILE N   H    sing N N 194 
ILE N   H2   sing N N 195 
ILE CA  C    sing N N 196 
ILE CA  CB   sing N N 197 
ILE CA  HA   sing N N 198 
ILE C   O    doub N N 199 
ILE C   OXT  sing N N 200 
ILE CB  CG1  sing N N 201 
ILE CB  CG2  sing N N 202 
ILE CB  HB   sing N N 203 
ILE CG1 CD1  sing N N 204 
ILE CG1 HG12 sing N N 205 
ILE CG1 HG13 sing N N 206 
ILE CG2 HG21 sing N N 207 
ILE CG2 HG22 sing N N 208 
ILE CG2 HG23 sing N N 209 
ILE CD1 HD11 sing N N 210 
ILE CD1 HD12 sing N N 211 
ILE CD1 HD13 sing N N 212 
ILE OXT HXT  sing N N 213 
LEU N   CA   sing N N 214 
LEU N   H    sing N N 215 
LEU N   H2   sing N N 216 
LEU CA  C    sing N N 217 
LEU CA  CB   sing N N 218 
LEU CA  HA   sing N N 219 
LEU C   O    doub N N 220 
LEU C   OXT  sing N N 221 
LEU CB  CG   sing N N 222 
LEU CB  HB2  sing N N 223 
LEU CB  HB3  sing N N 224 
LEU CG  CD1  sing N N 225 
LEU CG  CD2  sing N N 226 
LEU CG  HG   sing N N 227 
LEU CD1 HD11 sing N N 228 
LEU CD1 HD12 sing N N 229 
LEU CD1 HD13 sing N N 230 
LEU CD2 HD21 sing N N 231 
LEU CD2 HD22 sing N N 232 
LEU CD2 HD23 sing N N 233 
LEU OXT HXT  sing N N 234 
LYS N   CA   sing N N 235 
LYS N   H    sing N N 236 
LYS N   H2   sing N N 237 
LYS CA  C    sing N N 238 
LYS CA  CB   sing N N 239 
LYS CA  HA   sing N N 240 
LYS C   O    doub N N 241 
LYS C   OXT  sing N N 242 
LYS CB  CG   sing N N 243 
LYS CB  HB2  sing N N 244 
LYS CB  HB3  sing N N 245 
LYS CG  CD   sing N N 246 
LYS CG  HG2  sing N N 247 
LYS CG  HG3  sing N N 248 
LYS CD  CE   sing N N 249 
LYS CD  HD2  sing N N 250 
LYS CD  HD3  sing N N 251 
LYS CE  NZ   sing N N 252 
LYS CE  HE2  sing N N 253 
LYS CE  HE3  sing N N 254 
LYS NZ  HZ1  sing N N 255 
LYS NZ  HZ2  sing N N 256 
LYS NZ  HZ3  sing N N 257 
LYS OXT HXT  sing N N 258 
MET N   CA   sing N N 259 
MET N   H    sing N N 260 
MET N   H2   sing N N 261 
MET CA  C    sing N N 262 
MET CA  CB   sing N N 263 
MET CA  HA   sing N N 264 
MET C   O    doub N N 265 
MET C   OXT  sing N N 266 
MET CB  CG   sing N N 267 
MET CB  HB2  sing N N 268 
MET CB  HB3  sing N N 269 
MET CG  SD   sing N N 270 
MET CG  HG2  sing N N 271 
MET CG  HG3  sing N N 272 
MET SD  CE   sing N N 273 
MET CE  HE1  sing N N 274 
MET CE  HE2  sing N N 275 
MET CE  HE3  sing N N 276 
MET OXT HXT  sing N N 277 
PHE N   CA   sing N N 278 
PHE N   H    sing N N 279 
PHE N   H2   sing N N 280 
PHE CA  C    sing N N 281 
PHE CA  CB   sing N N 282 
PHE CA  HA   sing N N 283 
PHE C   O    doub N N 284 
PHE C   OXT  sing N N 285 
PHE CB  CG   sing N N 286 
PHE CB  HB2  sing N N 287 
PHE CB  HB3  sing N N 288 
PHE CG  CD1  doub Y N 289 
PHE CG  CD2  sing Y N 290 
PHE CD1 CE1  sing Y N 291 
PHE CD1 HD1  sing N N 292 
PHE CD2 CE2  doub Y N 293 
PHE CD2 HD2  sing N N 294 
PHE CE1 CZ   doub Y N 295 
PHE CE1 HE1  sing N N 296 
PHE CE2 CZ   sing Y N 297 
PHE CE2 HE2  sing N N 298 
PHE CZ  HZ   sing N N 299 
PHE OXT HXT  sing N N 300 
PRO N   CA   sing N N 301 
PRO N   CD   sing N N 302 
PRO N   H    sing N N 303 
PRO CA  C    sing N N 304 
PRO CA  CB   sing N N 305 
PRO CA  HA   sing N N 306 
PRO C   O    doub N N 307 
PRO C   OXT  sing N N 308 
PRO CB  CG   sing N N 309 
PRO CB  HB2  sing N N 310 
PRO CB  HB3  sing N N 311 
PRO CG  CD   sing N N 312 
PRO CG  HG2  sing N N 313 
PRO CG  HG3  sing N N 314 
PRO CD  HD2  sing N N 315 
PRO CD  HD3  sing N N 316 
PRO OXT HXT  sing N N 317 
SER N   CA   sing N N 318 
SER N   H    sing N N 319 
SER N   H2   sing N N 320 
SER CA  C    sing N N 321 
SER CA  CB   sing N N 322 
SER CA  HA   sing N N 323 
SER C   O    doub N N 324 
SER C   OXT  sing N N 325 
SER CB  OG   sing N N 326 
SER CB  HB2  sing N N 327 
SER CB  HB3  sing N N 328 
SER OG  HG   sing N N 329 
SER OXT HXT  sing N N 330 
SO4 S   O1   doub N N 331 
SO4 S   O2   doub N N 332 
SO4 S   O3   sing N N 333 
SO4 S   O4   sing N N 334 
THR N   CA   sing N N 335 
THR N   H    sing N N 336 
THR N   H2   sing N N 337 
THR CA  C    sing N N 338 
THR CA  CB   sing N N 339 
THR CA  HA   sing N N 340 
THR C   O    doub N N 341 
THR C   OXT  sing N N 342 
THR CB  OG1  sing N N 343 
THR CB  CG2  sing N N 344 
THR CB  HB   sing N N 345 
THR OG1 HG1  sing N N 346 
THR CG2 HG21 sing N N 347 
THR CG2 HG22 sing N N 348 
THR CG2 HG23 sing N N 349 
THR OXT HXT  sing N N 350 
TRP N   CA   sing N N 351 
TRP N   H    sing N N 352 
TRP N   H2   sing N N 353 
TRP CA  C    sing N N 354 
TRP CA  CB   sing N N 355 
TRP CA  HA   sing N N 356 
TRP C   O    doub N N 357 
TRP C   OXT  sing N N 358 
TRP CB  CG   sing N N 359 
TRP CB  HB2  sing N N 360 
TRP CB  HB3  sing N N 361 
TRP CG  CD1  doub Y N 362 
TRP CG  CD2  sing Y N 363 
TRP CD1 NE1  sing Y N 364 
TRP CD1 HD1  sing N N 365 
TRP CD2 CE2  doub Y N 366 
TRP CD2 CE3  sing Y N 367 
TRP NE1 CE2  sing Y N 368 
TRP NE1 HE1  sing N N 369 
TRP CE2 CZ2  sing Y N 370 
TRP CE3 CZ3  doub Y N 371 
TRP CE3 HE3  sing N N 372 
TRP CZ2 CH2  doub Y N 373 
TRP CZ2 HZ2  sing N N 374 
TRP CZ3 CH2  sing Y N 375 
TRP CZ3 HZ3  sing N N 376 
TRP CH2 HH2  sing N N 377 
TRP OXT HXT  sing N N 378 
TYR N   CA   sing N N 379 
TYR N   H    sing N N 380 
TYR N   H2   sing N N 381 
TYR CA  C    sing N N 382 
TYR CA  CB   sing N N 383 
TYR CA  HA   sing N N 384 
TYR C   O    doub N N 385 
TYR C   OXT  sing N N 386 
TYR CB  CG   sing N N 387 
TYR CB  HB2  sing N N 388 
TYR CB  HB3  sing N N 389 
TYR CG  CD1  doub Y N 390 
TYR CG  CD2  sing Y N 391 
TYR CD1 CE1  sing Y N 392 
TYR CD1 HD1  sing N N 393 
TYR CD2 CE2  doub Y N 394 
TYR CD2 HD2  sing N N 395 
TYR CE1 CZ   doub Y N 396 
TYR CE1 HE1  sing N N 397 
TYR CE2 CZ   sing Y N 398 
TYR CE2 HE2  sing N N 399 
TYR CZ  OH   sing N N 400 
TYR OH  HH   sing N N 401 
TYR OXT HXT  sing N N 402 
VAL N   CA   sing N N 403 
VAL N   H    sing N N 404 
VAL N   H2   sing N N 405 
VAL CA  C    sing N N 406 
VAL CA  CB   sing N N 407 
VAL CA  HA   sing N N 408 
VAL C   O    doub N N 409 
VAL C   OXT  sing N N 410 
VAL CB  CG1  sing N N 411 
VAL CB  CG2  sing N N 412 
VAL CB  HB   sing N N 413 
VAL CG1 HG11 sing N N 414 
VAL CG1 HG12 sing N N 415 
VAL CG1 HG13 sing N N 416 
VAL CG2 HG21 sing N N 417 
VAL CG2 HG22 sing N N 418 
VAL CG2 HG23 sing N N 419 
VAL OXT HXT  sing N N 420 
# 
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                    7HG7 
_atom_sites.fract_transf_matrix[1][1]   0.024038 
_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]   0.023714 
_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]   0.006308 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
F 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 2  ? 0.795   4.380   2.229   1.00 58.04  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.299  3.564   1.640   1.00 63.15  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.266   2.471   0.729   1.00 55.48  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.387   2.588   0.232   1.00 51.87  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.326  4.452   0.925   1.00 73.38  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.293  5.164   1.872   1.00 79.68  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.579  4.153   2.644   1.00 75.37  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -4.303  5.299   3.827   1.00 82.11  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.458  1.330   0.576   1.00 49.69  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.071  0.243   -0.334  1.00 44.67  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.187   0.644   -1.789  1.00 44.38  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.542  1.444   -2.377  1.00 46.31  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.328  -0.715  -0.228  1.00 42.15  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.806  -0.510  1.202   1.00 46.12  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.670  0.996   1.353   1.00 43.22  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.230   0.048   -2.364  1.00 41.20  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.458   0.102   -3.793  1.00 40.38  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.887   -1.187  -4.384  1.00 40.79  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.357   -2.024  -3.654  1.00 39.44  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.965   0.249   -4.058  1.00 44.12  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.529   1.553   -3.570  1.00 55.86  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.702   1.849   -2.234  1.00 64.92  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 3.925   2.648   -4.234  1.00 68.27  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.189   3.077   -2.106  1.00 68.62  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.341   3.582   -3.308  1.00 67.50  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.991   -1.343  -5.710  1.00 32.97  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.744   -2.626  -6.347  1.00 31.12  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.823   -3.641  -5.973  1.00 31.55  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.911   -3.291  -5.503  1.00 30.11  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.645   -2.421  -7.855  1.00 35.98  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.504   -4.927  -6.151  1.00 30.21  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.494   -5.963  -5.927  1.00 30.23  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.676   -5.787  -6.892  1.00 32.55  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.464   -5.512  -8.066  1.00 32.73  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.900   -7.366  -6.059  1.00 25.05  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.160   -7.730  -4.781  1.00 28.08  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.868   -7.917  -3.582  1.00 25.18  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.219  -7.930  -4.780  1.00 24.22  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.210   -8.190  -2.378  1.00 27.06  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.864  -8.260  -3.575  1.00 21.25  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.157  -8.377  -2.390  1.00 25.42  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.910   -5.975  -6.388  1.00 26.64  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.086   -5.997  -7.262  1.00 28.69  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.967   -7.228  -6.984  1.00 26.87  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.943   -7.813  -5.904  1.00 23.82  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.879   -4.691  -7.099  1.00 30.13  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.421   -4.506  -5.687  1.00 34.34  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.229   -3.224  -5.471  1.00 40.44  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.866   -3.190  -4.108  1.00 41.23  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.864   -3.346  -3.053  1.00 39.65  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.812   -7.632  -7.955  1.00 26.79  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.763   -8.724  -7.765  1.00 27.21  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.542   -8.431  -6.483  1.00 23.04  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.936   -7.294  -6.203  1.00 26.42  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.670   -8.645  -9.026  1.00 29.47  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.770   -8.006  -10.080 1.00 33.79  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.891   -7.031  -9.305  1.00 33.22  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.682   -9.477  -5.678  1.00 23.20  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.428  -9.352  -4.438  1.00 20.35  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.498   -9.217  -3.229  1.00 22.69  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.914   -9.449  -2.081  1.00 25.06  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.248   -8.805  -3.446  1.00 21.06  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.315   -8.739  -2.311  1.00 22.65  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.118   -10.122 -1.675  1.00 21.25  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.972   -11.111 -2.379  1.00 21.67  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.960   -8.142  -2.683  1.00 23.71  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.993   -6.632  -2.883  1.00 27.99  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.983   -6.009  -2.452  1.00 27.80  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.085   -6.113  -3.539  1.00 29.10  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.036   -10.180 -0.326  1.00 20.91  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.806   -11.437 0.383   1.00 22.01  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.345   -11.485 0.835   1.00 21.25  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.795   -10.464 1.294   1.00 23.46  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.739   -11.543 1.609   1.00 19.07  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.230   -11.331 1.309   1.00 19.43  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.086  -11.429 2.590   1.00 20.92  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.695   -12.289 0.205   1.00 21.66  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.755   -12.692 0.745   1.00 21.18  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.325   -12.881 0.975   1.00 19.72  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.089   -14.258 1.581   1.00 24.81  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.959   -15.123 1.542   1.00 24.78  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.547   -12.778 -0.369  1.00 19.99  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.663   -11.365 -0.940  1.00 20.63  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.995   -13.840 -1.371  1.00 21.96  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.867   -14.469 2.088   1.00 21.61  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.343   -15.823 2.138   1.00 21.96  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.388   -15.914 0.957   1.00 25.82  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.385  -14.986 0.735   1.00 26.97  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.509   -16.094 3.409   1.00 20.76  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.448   -16.189 4.610   1.00 22.58  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.853   -15.042 5.287   1.00 24.86  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.967   -17.416 4.994   1.00 25.96  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.749   -15.129 6.359   1.00 29.75  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.891   -17.505 6.038   1.00 30.47  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.273   -16.368 6.724   1.00 32.23  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.480   -17.020 0.195   1.00 23.80  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.347  -17.145 -1.003  1.00 26.40  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.316  -18.310 -0.809  1.00 29.09  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.938  -19.389 -0.301  1.00 27.68  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.542   -17.333 -2.243  1.00 20.52  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.566  -18.094 -1.270  1.00 28.96  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.628  -19.047 -1.007  1.00 30.04  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.050  -19.739 -2.301  1.00 30.28  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.451  -19.087 -3.274  1.00 31.08  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.810  -18.379 -0.295  1.00 31.68  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.924  -19.367 0.093   1.00 36.86  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.528  -20.328 1.217   1.00 39.97  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.693  -21.132 1.759   1.00 37.82  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.080  -22.166 0.796   1.00 36.37  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.965  -21.075 -2.263  1.00 31.02  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.445  -21.961 -3.314  1.00 33.70  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.497  -22.875 -2.691  1.00 36.29  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.334  -23.291 -1.544  1.00 30.32  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.317  -22.921 -3.710  1.00 36.74  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -2.003  -22.255 -4.075  1.00 41.33  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -2.029  -21.828 -5.827  1.00 41.25  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.556  -23.384 -6.568  1.00 35.39  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.555  -23.168 -3.453  1.00 42.99  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.597  -24.122 -3.084  1.00 43.94  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.981  -25.381 -2.488  1.00 41.81  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -6.063  -25.966 -3.068  1.00 38.93  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.347  -24.529 -4.357  1.00 52.73  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.716  -25.170 -4.152  1.00 60.53  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.805 -24.221 -3.649  1.00 69.90  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.470  -25.775 -1.302  1.00 36.68  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -7.018  -27.026 -0.713  1.00 36.93  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.663  -26.961 -0.016  1.00 44.52  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.180  -27.988 0.456   1.00 43.15  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -5.037  -25.775 0.064   1.00 35.51  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.807  -25.724 0.818   1.00 35.70  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.870  -24.573 1.800   1.00 33.81  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.501  -23.564 1.517   1.00 33.05  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.620  -25.392 -0.087  1.00 40.89  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.243  -26.404 -1.158  1.00 42.37  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.299  -27.393 -0.913  1.00 54.50  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.783  -26.314 -2.435  1.00 45.19  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -0.921  -28.284 -1.906  1.00 58.40  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.425  -27.205 -3.435  1.00 51.68  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.488  -28.188 -3.168  1.00 64.07  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -1.135  -29.056 -4.165  1.00 80.18  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -3.130  -24.633 2.927   1.00 32.87  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -3.130  -23.510 3.868   1.00 35.87  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.400  -22.357 3.165   1.00 31.39  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.626  -22.598 2.240   1.00 29.89  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.350  -24.049 5.091   1.00 36.92  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.487  -25.160 4.520   1.00 36.76  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.186  -25.713 3.284   1.00 38.14  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.651  -21.130 3.622   1.00 29.17  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.923  -19.948 3.193   1.00 28.26  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.424  -20.225 3.329   1.00 28.44  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? 0.051   -20.559 4.429   1.00 28.27  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.373  -18.732 4.019   1.00 27.78  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.831  -18.389 3.871   1.00 31.49  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.839  -19.046 4.559   1.00 33.69  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.443  -17.394 3.174   1.00 31.50  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -6.019  -18.504 4.248   1.00 32.51  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.808  -17.490 3.420   1.00 32.97  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.309   -20.032 2.226   1.00 26.80  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.644   -20.617 2.082   1.00 27.18  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.703   -19.526 1.938   1.00 27.90  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.531   -18.648 1.125   1.00 27.38  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.671   -21.525 0.847   1.00 28.02  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.741   -22.585 0.902   1.00 29.16  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.080   -22.434 0.691   1.00 28.78  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.544   -23.979 1.227   1.00 30.84  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.720   -23.640 0.824   1.00 30.41  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.812   -24.605 1.164   1.00 32.74  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.427   -24.762 1.548   1.00 34.68  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 4.001   -25.970 1.424   1.00 32.28  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.616   -26.111 1.802   1.00 36.07  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.885   -26.703 1.764   1.00 33.84  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.855   -19.581 2.656   1.00 23.14  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.906   -18.574 2.479   1.00 25.30  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.424   -18.572 1.032   1.00 22.32  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.685   -19.631 0.453   1.00 24.14  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 5.975   -19.006 3.536   1.00 23.60  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.775   -20.536 3.737   1.00 22.65  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.227   -20.650 3.594   1.00 25.78  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.478   -17.382 0.437   1.00 20.06  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.765   -17.247 -0.993  1.00 21.93  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.358   -15.875 -1.304  1.00 21.81  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.380   -14.979 -0.467  1.00 22.94  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.502   -17.479 -1.838  1.00 23.85  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.857   -15.713 -2.546  1.00 22.28  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.258   -14.379 -2.949  1.00 22.52  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.718   -14.142 -4.355  1.00 23.13  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.433   -15.116 -5.054  1.00 22.50  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.780   -14.229 -2.898  1.00 20.85  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.467   -15.158 -3.884  1.00 21.84  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 11.013  -14.975 -3.842  1.00 22.13  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.737  -15.771 -4.845  1.00 25.73  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 12.988  -16.220 -4.723  1.00 25.71  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.657  -16.106 -3.582  1.00 23.11  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.527  -16.853 -5.758  1.00 27.99  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.585   -12.864 -4.729  1.00 22.27  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.331   -12.470 -6.121  1.00 24.51  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.666   -12.584 -6.850  1.00 23.45  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.643   -12.002 -6.399  1.00 24.87  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.853   -11.002 -6.211  1.00 28.91  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.682   -10.688 -5.251  1.00 33.74  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.504   -10.614 -7.662  1.00 23.01  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.382   -11.328 -5.643  1.00 36.69  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.717   -13.393 -7.901  1.00 25.11  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.962   -13.608 -8.638  1.00 30.62  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.130   -12.590 -9.763  1.00 30.96  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.189   -11.945 -10.223 1.00 29.50  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.063   -15.003 -9.244  1.00 32.04  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 10.033  -15.955 -8.565  1.00 34.06  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.643  -15.548 -7.558  1.00 35.01  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.162  -17.091 -9.037  1.00 36.43  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.385  -12.459 -10.212 1.00 32.32  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.666  -11.817 -11.478 1.00 36.62  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.361  -12.822 -12.597 1.00 33.32  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.298  -14.031 -12.377 1.00 33.44  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.133  -11.404 -11.527 1.00 41.44  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.512  -10.117 -10.793 1.00 54.85  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.069  -9.020  -11.234 1.00 52.18  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.279  -10.212 -9.799  1.00 59.81  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.173  -12.323 -13.811 1.00 35.13  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.142  -13.212 -14.972 1.00 31.78  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.503  -13.047 -15.657 1.00 31.30  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.866  -11.910 -15.956 1.00 33.21  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 8.998   -12.738 -15.877 1.00 35.07  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.638   -12.748 -15.111 1.00 38.28  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 8.944   -13.563 -17.165 1.00 30.04  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.697   -11.613 -15.469 1.00 34.06  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.255  -14.141 -15.837 1.00 32.10  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.572  -14.104 -16.482 1.00 32.14  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.394  -13.737 -17.963 1.00 30.19  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.360  -14.028 -18.573 1.00 31.82  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.232  -15.472 -16.365 1.00 32.09  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.403  -13.075 -18.538 1.00 33.11  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.445  -12.892 -19.986 1.00 30.61  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.228  -14.248 -20.658 1.00 26.26  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.871  -15.218 -20.291 1.00 31.20  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.779  -12.256 -20.372 1.00 31.80  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.860  -10.751 -20.119 1.00 34.96  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.821  -10.115 -20.047 1.00 40.35  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.964  -10.225 -19.990 1.00 39.39  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.306  -14.303 -21.628 1.00 28.44  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 13.028  -15.487 -22.421 1.00 30.11  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.071  -16.475 -21.754 1.00 33.66  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.737  -17.501 -22.342 1.00 34.16  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.694  -16.200 -20.502 1.00 32.71  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.832  -17.116 -19.768 1.00 35.68  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.351   -16.837 -20.065 1.00 32.87  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 8.939   -15.752 -20.489 1.00 33.54  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.140  -17.036 -18.262 1.00 33.49  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.529   -17.848 -19.791 1.00 36.98  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 7.085   -17.779 -19.983 1.00 37.02  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.470   -16.732 -19.058 1.00 35.50  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.711   -16.746 -17.856 1.00 38.55  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.587   -19.198 -19.652 1.00 40.95  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 5.076   -19.260 -19.459 1.00 42.82  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.065   -20.184 -20.714 1.00 39.99  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.679   -15.831 -19.644 1.00 38.42  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 5.006   -14.770 -18.910 1.00 40.68  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.723   -15.302 -18.265 1.00 40.41  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.165   -16.298 -18.720 1.00 34.75  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.690   -13.574 -19.814 1.00 40.85  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 5.922   -12.830 -20.338 1.00 38.44  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.598   -11.599 -21.185 1.00 42.00  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.194   -11.976 -22.584 1.00 42.15  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 4.960   -10.774 -23.384 1.00 42.47  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.202   -14.641 -17.201 1.00 39.38  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 1.943   -15.069 -16.582 1.00 37.35  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.784   -14.559 -17.437 1.00 39.08  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 0.952   -13.626 -18.210 1.00 37.19  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.943   -14.416 -15.186 1.00 33.63  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.085   -13.395 -15.194 1.00 37.21  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.737   -13.418 -16.586 1.00 35.90  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.448  -15.092 -17.274 1.00 41.87  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.624  -14.483 -17.900 1.00 42.78  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.779  -13.058 -17.395 1.00 44.17  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.256  -12.720 -16.319 1.00 37.15  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.832  -15.348 -17.501 1.00 38.93  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.245  -16.561 -16.838 1.00 37.79  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.764  -16.325 -16.533 1.00 39.89  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.508  -12.197 -18.148 1.00 41.85  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.860  -10.855 -17.684 1.00 45.79  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.463  -10.911 -16.284 1.00 39.65  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.147  -11.859 -15.938 1.00 45.06  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.904  -10.359 -18.719 1.00 43.72  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.318  -11.613 -19.445 1.00 39.31  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.065  -12.483 -19.489 1.00 46.93  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.135  -9.908  -15.477 1.00 43.43  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.712  -9.747  -14.156 1.00 46.40  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.146  -10.761 -13.158 1.00 39.05  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.517  -10.704 -11.997 1.00 36.01  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.235  -9.667  -14.226 1.00 51.13  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.677  -8.452  -15.007 1.00 49.98  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.531  -7.316  -14.536 1.00 53.22  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.182  -8.669  -16.209 1.00 55.41  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.238  -11.654 -13.587 1.00 34.95  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.675  -12.655 -12.677 1.00 28.20  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.206  -12.331 -12.399 1.00 27.29  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.471   -11.678 -13.213 1.00 33.12  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.840  -14.120 -13.122 1.00 29.77  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.264  -14.628 -13.440 1.00 39.51  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.260  -14.264 -12.343 1.00 41.14  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.731  -14.579 -12.561 1.00 50.55  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -5.961  -16.027 -12.636 1.00 47.42  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.263   -12.778 -11.236 1.00 24.20  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.669   -12.645 -10.865 1.00 24.12  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.297   -14.026 -10.787 1.00 25.06  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.640   -14.981 -10.376 1.00 25.84  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.741   -12.043 -9.451  1.00 25.08  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.303   -10.589 -9.435  1.00 26.80  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.054  -10.268 -9.347  1.00 33.97  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.198   -9.546  -9.563  1.00 29.93  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.502  -8.961  -9.433  1.00 34.76  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.762   -8.221  -9.582  1.00 30.37  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.410   -7.930  -9.509  1.00 35.66  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.077  -6.645  -9.573  1.00 37.27  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.613   -14.183 -11.093 1.00 23.68  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.286   -15.456 -10.849 1.00 24.62  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.636   -15.578 -9.364  1.00 25.33  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.291   -14.705 -8.792  1.00 27.08  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.551   -15.380 -11.721 1.00 25.18  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.820   -13.898 -11.885 1.00 23.11  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.491   -13.137 -11.649 1.00 26.99  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.147   -16.634 -8.730  1.00 24.52  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.318   -16.769 -7.296  1.00 21.68  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.260   -17.937 -7.067  1.00 26.74  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.957   -19.068 -7.469  1.00 25.01  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.973   -17.021 -6.588  1.00 22.82  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.930   -15.947 -6.894  1.00 22.96  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.218   -17.216 -5.075  1.00 21.16  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.301   -14.492 -6.607  1.00 23.20  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.357   -17.670 -6.339  1.00 22.64  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.251   -18.751 -5.988  1.00 27.36  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 6.962   -19.152 -4.547  1.00 24.45  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 6.992   -18.326 -3.639  1.00 27.24  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.695   -18.256 -6.124  1.00 25.81  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.740   -19.266 -5.674  1.00 29.27  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.171  -20.286 -6.547  1.00 29.75  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.280  -19.209 -4.386  1.00 29.52  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.148  -21.197 -6.151  1.00 31.25  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.246  -20.150 -3.982  1.00 32.09  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.696  -21.114 -4.878  1.00 31.63  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.671   -20.438 -4.347  1.00 23.29  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.242   -20.899 -3.030  1.00 23.47  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.503   -21.431 -2.367  1.00 26.68  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.221   -22.285 -2.948  1.00 26.61  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.268   -22.085 -3.214  1.00 28.52  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.908   -21.581 -3.663  1.00 26.26  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.631   -21.356 -5.011  1.00 28.87  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.897   -21.328 -2.728  1.00 27.08  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.391   -20.880 -5.422  1.00 29.52  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.657   -20.854 -3.150  1.00 24.33  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.403   -20.629 -4.489  1.00 28.58  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.788   -20.888 -1.184  1.00 24.91  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 8.954   -21.366 -0.457  1.00 27.16  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.700   -22.815 -0.005  1.00 27.60  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.551   -23.242 0.147   1.00 26.97  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.237   -20.449 0.742   1.00 24.31  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.674   -19.034 0.376   1.00 23.27  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 10.891  -18.808 -0.292  1.00 21.72  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 8.893   -17.930 0.688   1.00 20.90  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.306  -17.515 -0.619  1.00 21.18  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.319   -16.617 0.354   1.00 19.46  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.552  -16.424 -0.301  1.00 19.89  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 9.791   -23.542 0.257   1.00 28.47  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.717   -24.914 0.729   1.00 29.73  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.483   -25.908 -0.404  1.00 36.29  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.315  -26.782 -0.589  1.00 36.83  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.398   -25.745 -1.191  1.00 31.81  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.118   -26.659 -2.287  1.00 35.20  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 8.857   -26.211 -3.531  1.00 34.28  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.118   -27.019 -4.417  1.00 33.37  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.617   -26.752 -2.575  1.00 35.84  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.224   -25.425 -2.917  1.00 37.90  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.838   -27.263 -1.385  1.00 36.94  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.122   -24.897 -3.606  1.00 29.57  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 9.840   -24.287 -4.708  1.00 31.52  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.030   -24.386 -5.992  1.00 30.01  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.621   -24.384 -7.071  1.00 31.47  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.282  -24.814 -4.874  1.00 28.50  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.036  -24.808 -3.596  1.00 34.00  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 12.863  -25.844 -3.237  1.00 35.25  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.082  -23.898 -2.584  1.00 30.35  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.387  -25.578 -2.038  1.00 39.30  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 12.927  -24.399 -1.630  1.00 36.38  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.707   -24.551 -5.877  1.00 33.36  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.829   -24.511 -7.051  1.00 33.59  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.420   -23.076 -7.410  1.00 33.75  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.575   -22.173 -6.595  1.00 30.16  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.616   -25.408 -6.855  1.00 37.50  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.039   -26.854 -6.635  1.00 48.51  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 4.933   -27.737 -6.109  1.00 55.14  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 3.784   -27.270 -5.941  1.00 56.29  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.263   -28.909 -5.838  1.00 66.14  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 5.999   -22.868 -8.672  1.00 27.14  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.516   -21.576 -9.134  1.00 29.38  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.071   -21.788 -9.582  1.00 32.37  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.773   -22.809 -10.211 1.00 35.43  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.362   -21.062 -10.307 1.00 34.70  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.661   -20.664 -9.872  1.00 33.50  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.745   -19.846 -10.988 1.00 38.56  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.172   -20.875 -9.195  1.00 28.97  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.849   -20.786 -9.797  1.00 27.35  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.540   -19.331 -10.118 1.00 29.91  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.213   -18.421 -9.634  1.00 29.00  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.773   -21.398 -8.901  1.00 30.60  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.494   -19.121 -10.934 1.00 27.47  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.108   -17.776 -11.299 1.00 29.03  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.136  -17.405 -10.508 1.00 32.83  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.150  -18.095 -10.587 1.00 33.23  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.204  -17.800 -12.793 1.00 31.88  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.016   -18.105 -13.638 1.00 32.43  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.154   -17.314 -13.531 1.00 35.32  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.988   -19.124 -14.588 1.00 38.38  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.277   -17.572 -14.322 1.00 46.52  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.107   -19.365 -15.381 1.00 42.06  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.244   -18.596 -15.252 1.00 40.63  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.050  -16.293 -9.764  1.00 26.43  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.150  -15.954 -8.890  1.00 25.18  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.445  -14.465 -9.025  1.00 26.31  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.553  -13.671 -9.324  1.00 27.36  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.819  -16.286 -7.430  1.00 26.55  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.757  -17.770 -7.054  1.00 26.85  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.399  -17.783 -5.564  1.00 27.00  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.118  -18.405 -7.259  1.00 30.76  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.694  -14.105 -8.709  1.00 25.60  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -4.097  -12.705 -8.629  1.00 25.85  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.122  -12.209 -7.179  1.00 21.71  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.066  -13.009 -6.252  1.00 23.86  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.147  -10.873 -6.987  1.00 22.65  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.093  -10.225 -5.675  1.00 25.76  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.060  -10.771 -4.634  1.00 25.07  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.759  -10.754 -3.460  1.00 23.40  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.400  -8.751  -6.003  1.00 25.38  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.830  -8.602  -7.393  1.00 27.49  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.202  -9.898  -8.093  1.00 26.63  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.208  -11.273 -5.088  1.00 24.79  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.165  -11.809 -4.130  1.00 28.12  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.590  -12.944 -3.281  1.00 28.10  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.083  -13.168 -2.174  1.00 26.26  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.480  -12.281 -4.767  1.00 29.70  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.442  -13.589 -5.559  1.00 34.31  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.802  -13.874 -6.212  1.00 41.66  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.728  -15.007 -7.176  1.00 40.65  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.416  -16.225 -6.411  1.00 46.52  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.541  -13.619 -3.777  1.00 27.46  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.005  -14.778 -3.103  1.00 26.81  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.672  -14.433 -2.428  1.00 24.33  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -2.990  -15.350 -1.965  1.00 26.91  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -4.947  -15.980 -4.048  1.00 29.77  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.322  -16.555 -4.359  1.00 32.28  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.125  -16.605 -3.394  1.00 34.27  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.577  -16.935 -5.540  1.00 33.10  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.315  -13.130 -2.384  1.00 22.90  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -1.988  -12.700 -1.934  1.00 22.94  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.132  -11.864 -0.663  1.00 21.52  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.697  -10.779 -0.729  1.00 24.89  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.213  -11.949 -3.035  1.00 21.51  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.104  -12.699 -4.357  1.00 24.28  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.391  -11.956 -5.445  1.00 25.58  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.437  -14.053 -4.165  1.00 24.39  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.528  -12.333 0.457   1.00 23.09  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.623  -11.646 1.743   1.00 23.93  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.226  -11.184 2.158   1.00 22.49  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.660   -12.011 2.319   1.00 27.03  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -2.094  -12.682 2.763   1.00 24.20  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.530  -13.125 2.497   1.00 27.53  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.841  -14.035 1.478   1.00 24.68  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.560  -12.611 3.265   1.00 26.57  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.162  -14.388 1.216   1.00 28.68  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.875  -12.999 3.015   1.00 28.01  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.169  -13.899 2.017   1.00 29.24  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? 0.008   -9.862  2.241   1.00 26.04  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.308   -9.325  2.659   1.00 27.23  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.868   -9.977  3.921   1.00 26.19  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.183   -10.160 4.916   1.00 28.24  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.054   -7.801  2.785   1.00 27.29  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? -0.030  -7.556  1.687   1.00 30.73  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -0.899  -8.811  1.769   1.00 29.69  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.154   -10.345 3.837   1.00 25.39  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.740   -11.241 4.818   1.00 28.05  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.813   -10.564 6.195   1.00 26.83  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.524   -11.217 7.182   1.00 31.58  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.156   -11.605 4.358   1.00 28.24  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.927   -12.379 5.412   1.00 26.62  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.662   -13.731 5.649   1.00 27.58  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.948   -11.769 6.137   1.00 30.70  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.379   -14.462 6.591   1.00 30.08  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.669   -12.491 7.078   1.00 31.82  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.380   -13.821 7.307   1.00 32.14  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 8.082   -14.482 8.282   1.00 37.15  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.202   -9.284  6.248   1.00 26.76  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.366   -8.628  7.548   1.00 31.45  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 3.031   -8.598  8.304   1.00 33.79  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.973   -9.027  9.460   1.00 38.40  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 5.050   -7.267  7.442   1.00 30.05  ? 62  ASP A CB  1 
ATOM   495  N N   . LYS A 1 64 ? 1.961   -8.159  7.620   1.00 36.07  ? 63  LYS A N   1 
ATOM   496  C CA  . LYS A 1 64 ? 0.606   -8.094  8.175   1.00 33.89  ? 63  LYS A CA  1 
ATOM   497  C C   . LYS A 1 64 ? 0.077   -9.458  8.624   1.00 31.03  ? 63  LYS A C   1 
ATOM   498  O O   . LYS A 1 64 ? -0.650  -9.523  9.614   1.00 31.63  ? 63  LYS A O   1 
ATOM   499  C CB  . LYS A 1 64 ? -0.375  -7.501  7.151   1.00 36.04  ? 63  LYS A CB  1 
ATOM   500  C CG  . LYS A 1 64 ? -1.820  -7.260  7.679   1.00 38.56  ? 63  LYS A CG  1 
ATOM   501  C CD  . LYS A 1 64 ? -2.676  -6.476  6.696   1.00 37.64  ? 63  LYS A CD  1 
ATOM   502  C CE  . LYS A 1 64 ? -3.777  -5.722  7.356   1.00 43.95  ? 63  LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 64 ? -4.906  -6.585  7.675   1.00 50.76  ? 63  LYS A NZ  1 
ATOM   504  N N   . SER A 1 65 ? 0.447   -10.545 7.926   1.00 28.47  ? 64  SER A N   1 
ATOM   505  C CA  . SER A 1 65 ? -0.229  -11.836 8.019   1.00 31.56  ? 64  SER A CA  1 
ATOM   506  C C   . SER A 1 65 ? 0.534   -12.893 8.818   1.00 33.07  ? 64  SER A C   1 
ATOM   507  O O   . SER A 1 65 ? -0.025  -13.958 9.054   1.00 30.80  ? 64  SER A O   1 
ATOM   508  C CB  . SER A 1 65 ? -0.519  -12.406 6.637   1.00 33.15  ? 64  SER A CB  1 
ATOM   509  O OG  . SER A 1 65 ? -1.325  -11.483 5.924   1.00 39.97  ? 64  SER A OG  1 
ATOM   510  N N   . LYS A 1 66 ? 1.806   -12.641 9.166   1.00 34.50  ? 65  LYS A N   1 
ATOM   511  C CA  . LYS A 1 66 ? 2.652   -13.706 9.709   1.00 35.13  ? 65  LYS A CA  1 
ATOM   512  C C   . LYS A 1 66 ? 2.157   -14.229 11.059  1.00 31.84  ? 65  LYS A C   1 
ATOM   513  O O   . LYS A 1 66 ? 2.250   -15.429 11.332  1.00 33.22  ? 65  LYS A O   1 
ATOM   514  C CB  . LYS A 1 66 ? 4.151   -13.387 9.699   1.00 40.82  ? 65  LYS A CB  1 
ATOM   515  C CG  . LYS A 1 66 ? 4.591   -12.126 10.416  1.00 44.73  ? 65  LYS A CG  1 
ATOM   516  C CD  . LYS A 1 66 ? 6.113   -12.092 10.456  1.00 56.56  ? 65  LYS A CD  1 
ATOM   517  C CE  . LYS A 1 66 ? 6.671   -10.782 10.935  1.00 63.61  ? 65  LYS A CE  1 
ATOM   518  N NZ  . LYS A 1 66 ? 6.548   -9.691  9.957   1.00 71.55  ? 65  LYS A NZ  1 
ATOM   519  N N   A ASP A 1 67 ? 1.592   -13.337 11.877  0.50 35.41  ? 66  ASP A N   1 
ATOM   520  N N   B ASP A 1 67 ? 1.618   -13.336 11.895  0.50 35.49  ? 66  ASP A N   1 
ATOM   521  C CA  A ASP A 1 67 ? 1.058   -13.745 13.173  0.50 36.27  ? 66  ASP A CA  1 
ATOM   522  C CA  B ASP A 1 67 ? 1.063   -13.772 13.172  0.50 36.23  ? 66  ASP A CA  1 
ATOM   523  C C   A ASP A 1 67 ? -0.070  -14.766 13.011  0.50 39.20  ? 66  ASP A C   1 
ATOM   524  C C   B ASP A 1 67 ? 0.007   -14.854 12.943  0.50 39.12  ? 66  ASP A C   1 
ATOM   525  O O   A ASP A 1 67 ? -0.211  -15.668 13.832  0.50 39.40  ? 66  ASP A O   1 
ATOM   526  O O   B ASP A 1 67 ? -0.013  -15.868 13.640  0.50 37.00  ? 66  ASP A O   1 
ATOM   527  C CB  A ASP A 1 67 ? 0.775   -12.545 14.065  0.50 37.61  ? 66  ASP A CB  1 
ATOM   528  C CB  B ASP A 1 67 ? 0.548   -12.606 14.003  0.50 38.90  ? 66  ASP A CB  1 
ATOM   529  C CG  A ASP A 1 67 ? 2.023   -11.893 14.640  0.50 40.61  ? 66  ASP A CG  1 
ATOM   530  C CG  B ASP A 1 67 ? 0.143   -12.948 15.431  0.50 40.56  ? 66  ASP A CG  1 
ATOM   531  O OD1 A ASP A 1 67 ? 3.094   -12.543 14.577  0.50 42.71  ? 66  ASP A OD1 1 
ATOM   532  O OD1 B ASP A 1 67 ? 1.044   -13.072 16.290  0.50 42.83  ? 66  ASP A OD1 1 
ATOM   533  O OD2 A ASP A 1 67 ? 1.932   -10.732 15.112  0.50 37.76  ? 66  ASP A OD2 1 
ATOM   534  O OD2 B ASP A 1 67 ? -1.072  -13.124 15.673  0.50 50.59  ? 66  ASP A OD2 1 
ATOM   535  N N   . LYS A 1 68 ? -0.837  -14.670 11.919  1.00 36.76  ? 67  LYS A N   1 
ATOM   536  C CA  . LYS A 1 68 ? -1.926  -15.604 11.686  1.00 35.02  ? 67  LYS A CA  1 
ATOM   537  C C   . LYS A 1 68 ? -1.466  -16.877 10.986  1.00 36.68  ? 67  LYS A C   1 
ATOM   538  O O   . LYS A 1 68 ? -1.960  -17.979 11.273  1.00 36.04  ? 67  LYS A O   1 
ATOM   539  C CB  . LYS A 1 68 ? -3.003  -14.899 10.864  1.00 37.14  ? 67  LYS A CB  1 
ATOM   540  C CG  . LYS A 1 68 ? -4.288  -15.686 10.682  1.00 40.31  ? 67  LYS A CG  1 
ATOM   541  C CD  . LYS A 1 68 ? -5.327  -14.731 10.079  1.00 45.02  ? 67  LYS A CD  1 
ATOM   542  C CE  . LYS A 1 68 ? -6.706  -15.328 9.927   1.00 50.00  ? 67  LYS A CE  1 
ATOM   543  N NZ  . LYS A 1 68 ? -7.621  -14.501 9.123   1.00 43.76  ? 67  LYS A NZ  1 
ATOM   544  N N   . TYR A 1 69 ? -0.575  -16.730 10.001  1.00 33.72  ? 68  TYR A N   1 
ATOM   545  C CA  . TYR A 1 69 ? -0.390  -17.825 9.062   1.00 33.03  ? 68  TYR A CA  1 
ATOM   546  C C   . TYR A 1 69 ? 1.001   -18.443 9.198   1.00 33.82  ? 68  TYR A C   1 
ATOM   547  O O   . TYR A 1 69 ? 1.262   -19.495 8.619   1.00 32.89  ? 68  TYR A O   1 
ATOM   548  C CB  . TYR A 1 69 ? -0.552  -17.344 7.609   1.00 30.29  ? 68  TYR A CB  1 
ATOM   549  C CG  . TYR A 1 69 ? -1.954  -16.904 7.217   1.00 33.88  ? 68  TYR A CG  1 
ATOM   550  C CD1 . TYR A 1 69 ? -3.095  -17.636 7.575   1.00 34.78  ? 68  TYR A CD1 1 
ATOM   551  C CD2 . TYR A 1 69 ? -2.135  -15.723 6.487   1.00 31.54  ? 68  TYR A CD2 1 
ATOM   552  C CE1 . TYR A 1 69 ? -4.376  -17.218 7.201   1.00 31.53  ? 68  TYR A CE1 1 
ATOM   553  C CE2 . TYR A 1 69 ? -3.398  -15.304 6.105   1.00 35.47  ? 68  TYR A CE2 1 
ATOM   554  C CZ  . TYR A 1 69 ? -4.517  -16.031 6.486   1.00 35.31  ? 68  TYR A CZ  1 
ATOM   555  O OH  . TYR A 1 69 ? -5.726  -15.551 6.063   1.00 39.37  ? 68  TYR A OH  1 
ATOM   556  N N   . GLY A 1 70 ? 1.871   -17.796 9.963   1.00 32.37  ? 69  GLY A N   1 
ATOM   557  C CA  . GLY A 1 70 ? 3.258   -18.216 10.034  1.00 32.87  ? 69  GLY A CA  1 
ATOM   558  C C   . GLY A 1 70 ? 3.476   -19.209 11.179  1.00 34.51  ? 69  GLY A C   1 
ATOM   559  O O   . GLY A 1 70 ? 4.328   -18.983 12.018  1.00 42.70  ? 69  GLY A O   1 
ATOM   560  N N   . LYS A 1 71 ? 2.749   -20.322 11.140  1.00 38.32  ? 70  LYS A N   1 
ATOM   561  C CA  . LYS A 1 71 ? 2.800   -21.333 12.176  1.00 43.76  ? 70  LYS A CA  1 
ATOM   562  C C   . LYS A 1 71 ? 3.106   -22.664 11.506  1.00 39.77  ? 70  LYS A C   1 
ATOM   563  O O   . LYS A 1 71 ? 2.721   -22.890 10.366  1.00 36.49  ? 70  LYS A O   1 
ATOM   564  C CB  . LYS A 1 71 ? 1.487   -21.374 12.973  1.00 43.31  ? 70  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 71 ? 1.416   -20.235 13.991  1.00 50.88  ? 70  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 71 ? 0.021   -19.716 14.333  1.00 55.39  ? 70  LYS A CD  1 
ATOM   567  N N   . PRO A 1 72 ? 3.851   -23.573 12.170  1.00 40.52  ? 71  PRO A N   1 
ATOM   568  C CA  . PRO A 1 72 ? 4.104   -24.904 11.602  1.00 39.42  ? 71  PRO A CA  1 
ATOM   569  C C   . PRO A 1 72 ? 2.869   -25.632 11.092  1.00 41.01  ? 71  PRO A C   1 
ATOM   570  O O   . PRO A 1 72 ? 1.801   -25.535 11.671  1.00 47.52  ? 71  PRO A O   1 
ATOM   571  C CB  . PRO A 1 72 ? 4.789   -25.659 12.759  1.00 44.63  ? 71  PRO A CB  1 
ATOM   572  C CG  . PRO A 1 72 ? 5.466   -24.547 13.551  1.00 47.95  ? 71  PRO A CG  1 
ATOM   573  C CD  . PRO A 1 72 ? 4.531   -23.337 13.453  1.00 41.83  ? 71  PRO A CD  1 
ATOM   574  N N   . ASN A 1 73 ? 3.053   -26.406 10.027  1.00 43.44  ? 72  ASN A N   1 
ATOM   575  C CA  . ASN A 1 73 ? 1.973   -27.120 9.382   1.00 50.25  ? 72  ASN A CA  1 
ATOM   576  C C   . ASN A 1 73 ? 2.526   -28.473 8.963   1.00 59.35  ? 72  ASN A C   1 
ATOM   577  O O   . ASN A 1 73 ? 3.732   -28.620 8.761   1.00 62.34  ? 72  ASN A O   1 
ATOM   578  C CB  . ASN A 1 73 ? 1.519   -26.346 8.149   1.00 51.08  ? 72  ASN A CB  1 
ATOM   579  C CG  . ASN A 1 73 ? 0.161   -26.761 7.648   1.00 58.71  ? 72  ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 73 ? 0.067   -27.519 6.678   1.00 56.33  ? 72  ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 73 ? -0.894  -26.266 8.278   1.00 63.19  ? 72  ASN A ND2 1 
ATOM   582  N N   . LYS A 1 74 ? 1.632   -29.449 8.811   1.00 58.00  ? 73  LYS A N   1 
ATOM   583  C CA  . LYS A 1 74 ? 2.032   -30.820 8.555   1.00 52.94  ? 73  LYS A CA  1 
ATOM   584  C C   . LYS A 1 74 ? 2.461   -30.972 7.098   1.00 51.70  ? 73  LYS A C   1 
ATOM   585  O O   . LYS A 1 74 ? 3.237   -31.869 6.768   1.00 51.56  ? 73  LYS A O   1 
ATOM   586  C CB  . LYS A 1 74 ? 0.862   -31.737 8.948   1.00 57.97  ? 73  LYS A CB  1 
ATOM   587  C CG  . LYS A 1 74 ? -0.279  -31.830 7.931   1.00 55.35  ? 73  LYS A CG  1 
ATOM   588  N N   . ARG A 1 75 ? 1.967   -30.080 6.226   1.00 46.75  ? 74  ARG A N   1 
ATOM   589  C CA  . ARG A 1 75 ? 2.081   -30.282 4.790   1.00 46.42  ? 74  ARG A CA  1 
ATOM   590  C C   . ARG A 1 75 ? 3.539   -30.288 4.335   1.00 45.04  ? 74  ARG A C   1 
ATOM   591  O O   . ARG A 1 75 ? 4.366   -29.556 4.891   1.00 43.05  ? 74  ARG A O   1 
ATOM   592  C CB  . ARG A 1 75 ? 1.300   -29.179 4.069   1.00 50.50  ? 74  ARG A CB  1 
ATOM   593  C CG  . ARG A 1 75 ? -0.206  -29.369 4.159   1.00 51.66  ? 74  ARG A CG  1 
ATOM   594  C CD  . ARG A 1 75 ? -0.686  -30.620 3.428   1.00 51.38  ? 74  ARG A CD  1 
ATOM   595  N NE  . ARG A 1 75 ? -1.812  -30.238 2.570   1.00 67.25  ? 74  ARG A NE  1 
ATOM   596  C CZ  . ARG A 1 75 ? -2.889  -29.550 2.952   1.00 66.71  ? 74  ARG A CZ  1 
ATOM   597  N NH1 . ARG A 1 75 ? -3.734  -29.120 2.032   1.00 64.05  ? 74  ARG A NH1 1 
ATOM   598  N NH2 . ARG A 1 75 ? -3.097  -29.258 4.231   1.00 66.56  ? 74  ARG A NH2 1 
ATOM   599  N N   . LYS A 1 76 ? 3.805   -31.075 3.276   1.00 39.22  ? 75  LYS A N   1 
ATOM   600  C CA  . LYS A 1 76 ? 5.133   -31.253 2.714   1.00 42.79  ? 75  LYS A CA  1 
ATOM   601  C C   . LYS A 1 76 ? 5.687   -29.888 2.320   1.00 40.74  ? 75  LYS A C   1 
ATOM   602  O O   . LYS A 1 76 ? 5.110   -29.207 1.473   1.00 34.50  ? 75  LYS A O   1 
ATOM   603  C CB  . LYS A 1 76 ? 5.113   -32.130 1.459   1.00 42.81  ? 75  LYS A CB  1 
ATOM   604  C CG  . LYS A 1 76 ? 6.475   -32.479 0.863   1.00 46.86  ? 75  LYS A CG  1 
ATOM   605  C CD  . LYS A 1 76 ? 6.472   -33.577 -0.199  1.00 48.98  ? 75  LYS A CD  1 
ATOM   606  C CE  . LYS A 1 76 ? 7.874   -33.990 -0.573  1.00 51.05  ? 75  LYS A CE  1 
ATOM   607  N N   . GLY A 1 77 ? 6.804   -29.513 2.956   1.00 39.18  ? 76  GLY A N   1 
ATOM   608  C CA  . GLY A 1 77 ? 7.616   -28.398 2.502   1.00 34.69  ? 76  GLY A CA  1 
ATOM   609  C C   . GLY A 1 77 ? 7.244   -27.103 3.226   1.00 34.44  ? 76  GLY A C   1 
ATOM   610  O O   . GLY A 1 77 ? 7.936   -26.103 3.083   1.00 37.64  ? 76  GLY A O   1 
ATOM   611  N N   . PHE A 1 78 ? 6.162   -27.124 4.008   1.00 31.13  ? 77  PHE A N   1 
ATOM   612  C CA  . PHE A 1 78 ? 5.695   -25.903 4.629   1.00 32.18  ? 77  PHE A CA  1 
ATOM   613  C C   . PHE A 1 78 ? 6.711   -25.332 5.626   1.00 33.15  ? 77  PHE A C   1 
ATOM   614  O O   . PHE A 1 78 ? 6.958   -24.126 5.658   1.00 31.54  ? 77  PHE A O   1 
ATOM   615  C CB  . PHE A 1 78 ? 4.336   -26.170 5.281   1.00 34.47  ? 77  PHE A CB  1 
ATOM   616  C CG  . PHE A 1 78 ? 3.606   -24.887 5.646   1.00 33.01  ? 77  PHE A CG  1 
ATOM   617  C CD1 . PHE A 1 78 ? 3.861   -24.227 6.846   1.00 35.43  ? 77  PHE A CD1 1 
ATOM   618  C CD2 . PHE A 1 78 ? 2.632   -24.361 4.794   1.00 31.29  ? 77  PHE A CD2 1 
ATOM   619  C CE1 . PHE A 1 78 ? 3.195   -23.047 7.167   1.00 37.35  ? 77  PHE A CE1 1 
ATOM   620  C CE2 . PHE A 1 78 ? 1.961   -23.193 5.128   1.00 29.19  ? 77  PHE A CE2 1 
ATOM   621  C CZ  . PHE A 1 78 ? 2.242   -22.544 6.316   1.00 30.09  ? 77  PHE A CZ  1 
ATOM   622  N N   . ASN A 1 79 ? 7.240   -26.178 6.509   1.00 31.15  ? 78  ASN A N   1 
ATOM   623  C CA  . ASN A 1 79 ? 8.117   -25.682 7.561   1.00 34.23  ? 78  ASN A CA  1 
ATOM   624  C C   . ASN A 1 79 ? 9.458   -25.213 6.974   1.00 31.23  ? 78  ASN A C   1 
ATOM   625  O O   . ASN A 1 79 ? 10.043  -24.228 7.459   1.00 32.74  ? 78  ASN A O   1 
ATOM   626  C CB  . ASN A 1 79 ? 8.260   -26.739 8.650   1.00 37.49  ? 78  ASN A CB  1 
ATOM   627  C CG  . ASN A 1 79 ? 6.933   -27.014 9.327   1.00 45.17  ? 78  ASN A CG  1 
ATOM   628  O OD1 . ASN A 1 79 ? 6.017   -26.190 9.231   1.00 35.61  ? 78  ASN A OD1 1 
ATOM   629  N ND2 . ASN A 1 79 ? 6.812   -28.145 10.018  1.00 35.49  ? 78  ASN A ND2 1 
ATOM   630  N N   . GLU A 1 80 ? 9.924   -25.918 5.931   1.00 28.52  ? 79  GLU A N   1 
ATOM   631  C CA  . GLU A 1 80 ? 11.092  -25.465 5.180   1.00 29.50  ? 79  GLU A CA  1 
ATOM   632  C C   . GLU A 1 80 ? 10.800  -24.059 4.652   1.00 28.02  ? 79  GLU A C   1 
ATOM   633  O O   . GLU A 1 80 ? 11.640  -23.159 4.755   1.00 27.23  ? 79  GLU A O   1 
ATOM   634  C CB  . GLU A 1 80 ? 11.505  -26.387 4.033   1.00 32.11  ? 79  GLU A CB  1 
ATOM   635  C CG  . GLU A 1 80 ? 12.747  -25.921 3.264   1.00 31.94  ? 79  GLU A CG  1 
ATOM   636  C CD  . GLU A 1 80 ? 13.314  -26.975 2.305   1.00 42.54  ? 79  GLU A CD  1 
ATOM   637  O OE1 . GLU A 1 80 ? 12.728  -28.058 2.225   1.00 50.33  ? 79  GLU A OE1 1 
ATOM   638  O OE2 . GLU A 1 80 ? 14.332  -26.760 1.631   1.00 46.52  ? 79  GLU A OE2 1 
ATOM   639  N N   . GLY A 1 81 ? 9.578   -23.891 4.119   1.00 30.51  ? 80  GLY A N   1 
ATOM   640  C CA  . GLY A 1 81 ? 9.140   -22.615 3.555   1.00 28.15  ? 80  GLY A CA  1 
ATOM   641  C C   . GLY A 1 81 ? 9.128   -21.476 4.567   1.00 25.95  ? 80  GLY A C   1 
ATOM   642  O O   . GLY A 1 81 ? 9.439   -20.317 4.234   1.00 24.94  ? 80  GLY A O   1 
ATOM   643  N N   . LEU A 1 82 ? 8.678   -21.780 5.798   1.00 24.08  ? 81  LEU A N   1 
ATOM   644  C CA  . LEU A 1 82 ? 8.744   -20.808 6.874   1.00 26.98  ? 81  LEU A CA  1 
ATOM   645  C C   . LEU A 1 82 ? 10.184  -20.359 7.136   1.00 28.64  ? 81  LEU A C   1 
ATOM   646  O O   . LEU A 1 82 ? 10.427  -19.167 7.351   1.00 24.85  ? 81  LEU A O   1 
ATOM   647  C CB  . LEU A 1 82 ? 8.099   -21.309 8.166   1.00 27.45  ? 81  LEU A CB  1 
ATOM   648  C CG  . LEU A 1 82 ? 6.596   -21.609 8.108   1.00 31.59  ? 81  LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 82 ? 6.248   -22.174 9.466   1.00 34.83  ? 81  LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 82 ? 5.673   -20.424 7.819   1.00 30.27  ? 81  LEU A CD2 1 
ATOM   651  N N   . TRP A 1 83 ? 11.131  -21.302 7.098   1.00 26.71  ? 82  TRP A N   1 
ATOM   652  C CA  . TRP A 1 83 ? 12.517  -20.921 7.377   1.00 28.44  ? 82  TRP A CA  1 
ATOM   653  C C   . TRP A 1 83 ? 12.995  -19.993 6.260   1.00 25.49  ? 82  TRP A C   1 
ATOM   654  O O   . TRP A 1 83 ? 13.597  -18.957 6.515   1.00 27.68  ? 82  TRP A O   1 
ATOM   655  C CB  . TRP A 1 83 ? 13.434  -22.151 7.561   1.00 30.09  ? 82  TRP A CB  1 
ATOM   656  C CG  . TRP A 1 83 ? 14.896  -21.805 7.769   1.00 28.18  ? 82  TRP A CG  1 
ATOM   657  C CD1 . TRP A 1 83 ? 15.560  -21.668 8.955   1.00 29.60  ? 82  TRP A CD1 1 
ATOM   658  C CD2 . TRP A 1 83 ? 15.856  -21.498 6.738   1.00 26.84  ? 82  TRP A CD2 1 
ATOM   659  N NE1 . TRP A 1 83 ? 16.860  -21.324 8.735   1.00 28.47  ? 82  TRP A NE1 1 
ATOM   660  C CE2 . TRP A 1 83 ? 17.070  -21.201 7.385   1.00 29.83  ? 82  TRP A CE2 1 
ATOM   661  C CE3 . TRP A 1 83 ? 15.791  -21.454 5.336   1.00 27.26  ? 82  TRP A CE3 1 
ATOM   662  C CZ2 . TRP A 1 83 ? 18.221  -20.856 6.681   1.00 28.83  ? 82  TRP A CZ2 1 
ATOM   663  C CZ3 . TRP A 1 83 ? 16.933  -21.121 4.634   1.00 30.66  ? 82  TRP A CZ3 1 
ATOM   664  C CH2 . TRP A 1 83 ? 18.125  -20.794 5.310   1.00 30.27  ? 82  TRP A CH2 1 
ATOM   665  N N   . GLU A 1 84 ? 12.648  -20.341 5.016   1.00 27.34  ? 83  GLU A N   1 
ATOM   666  C CA  . GLU A 1 84 ? 13.171  -19.616 3.864   1.00 25.28  ? 83  GLU A CA  1 
ATOM   667  C C   . GLU A 1 84 ? 12.656  -18.181 3.879   1.00 25.44  ? 83  GLU A C   1 
ATOM   668  O O   . GLU A 1 84 ? 13.421  -17.254 3.653   1.00 21.98  ? 83  GLU A O   1 
ATOM   669  C CB  . GLU A 1 84 ? 12.812  -20.286 2.544   1.00 23.91  ? 83  GLU A CB  1 
ATOM   670  C CG  . GLU A 1 84 ? 13.443  -21.675 2.408   1.00 24.58  ? 83  GLU A CG  1 
ATOM   671  C CD  . GLU A 1 84 ? 13.068  -22.390 1.112   1.00 29.47  ? 83  GLU A CD  1 
ATOM   672  O OE1 . GLU A 1 84 ? 12.139  -21.899 0.448   1.00 31.12  ? 83  GLU A OE1 1 
ATOM   673  O OE2 . GLU A 1 84 ? 13.696  -23.424 0.730   1.00 33.78  ? 83  GLU A OE2 1 
ATOM   674  N N   . ILE A 1 85 ? 11.360  -18.002 4.174   1.00 24.55  ? 84  ILE A N   1 
ATOM   675  C CA  . ILE A 1 85 ? 10.774  -16.684 4.042   1.00 21.88  ? 84  ILE A CA  1 
ATOM   676  C C   . ILE A 1 85 ? 11.344  -15.749 5.113   1.00 24.20  ? 84  ILE A C   1 
ATOM   677  O O   . ILE A 1 85 ? 11.422  -14.518 4.926   1.00 23.08  ? 84  ILE A O   1 
ATOM   678  C CB  . ILE A 1 85 ? 9.225   -16.705 4.041   1.00 22.63  ? 84  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 85 ? 8.686   -15.314 3.555   1.00 23.98  ? 84  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 85 ? 8.662   -17.047 5.428   1.00 22.67  ? 84  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 85 ? 7.226   -15.325 3.058   1.00 21.74  ? 84  ILE A CD1 1 
ATOM   682  N N   . GLN A 1 86 ? 11.700  -16.341 6.264   1.00 26.05  ? 85  GLN A N   1 
ATOM   683  C CA  . GLN A 1 86 ? 12.203  -15.593 7.403   1.00 27.83  ? 85  GLN A CA  1 
ATOM   684  C C   . GLN A 1 86 ? 13.711  -15.341 7.294   1.00 27.88  ? 85  GLN A C   1 
ATOM   685  O O   . GLN A 1 86 ? 14.137  -14.242 7.662   1.00 31.29  ? 85  GLN A O   1 
ATOM   686  C CB  . GLN A 1 86 ? 11.735  -16.251 8.706   1.00 29.10  ? 85  GLN A CB  1 
ATOM   687  C CG  . GLN A 1 86 ? 12.354  -15.680 9.975   1.00 36.86  ? 85  GLN A CG  1 
ATOM   688  C CD  . GLN A 1 86 ? 11.673  -16.221 11.226  1.00 47.64  ? 85  GLN A CD  1 
ATOM   689  O OE1 . GLN A 1 86 ? 11.471  -17.439 11.389  1.00 37.64  ? 85  GLN A OE1 1 
ATOM   690  N NE2 . GLN A 1 86 ? 11.292  -15.310 12.114  1.00 43.63  ? 85  GLN A NE2 1 
ATOM   691  N N   . ASN A 1 87 ? 14.481  -16.275 6.701   1.00 25.09  ? 86  ASN A N   1 
ATOM   692  C CA  . ASN A 1 87 ? 15.938  -16.311 6.818   1.00 22.65  ? 86  ASN A CA  1 
ATOM   693  C C   . ASN A 1 87 ? 16.659  -15.971 5.511   1.00 25.32  ? 86  ASN A C   1 
ATOM   694  O O   . ASN A 1 87 ? 17.766  -15.402 5.549   1.00 24.94  ? 86  ASN A O   1 
ATOM   695  C CB  . ASN A 1 87 ? 16.414  -17.615 7.461   1.00 25.14  ? 86  ASN A CB  1 
ATOM   696  C CG  . ASN A 1 87 ? 15.936  -17.666 8.904   1.00 29.51  ? 86  ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 87 ? 16.432  -16.895 9.734   1.00 35.83  ? 86  ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 87 ? 14.921  -18.461 9.218   1.00 26.49  ? 86  ASN A ND2 1 
ATOM   699  N N   . ASN A 1 88 ? 16.066  -16.308 4.347   1.00 22.82  ? 87  ASN A N   1 
ATOM   700  C CA  . ASN A 1 88 ? 16.725  -15.932 3.097   1.00 24.13  ? 87  ASN A CA  1 
ATOM   701  C C   . ASN A 1 88 ? 15.680  -15.859 1.973   1.00 26.18  ? 87  ASN A C   1 
ATOM   702  O O   . ASN A 1 88 ? 15.731  -16.639 1.006   1.00 26.77  ? 87  ASN A O   1 
ATOM   703  C CB  . ASN A 1 88 ? 17.862  -16.898 2.758   1.00 29.67  ? 87  ASN A CB  1 
ATOM   704  C CG  . ASN A 1 88 ? 18.926  -16.268 1.885   1.00 30.61  ? 87  ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 88 ? 18.676  -15.259 1.220   1.00 27.21  ? 87  ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 88 ? 20.141  -16.810 1.899   1.00 35.17  ? 87  ASN A ND2 1 
ATOM   707  N N   . PRO A 1 89 ? 14.725  -14.906 2.067   1.00 25.16  ? 88  PRO A N   1 
ATOM   708  C CA  . PRO A 1 89 ? 13.572  -14.895 1.156   1.00 25.20  ? 88  PRO A CA  1 
ATOM   709  C C   . PRO A 1 89 ? 13.941  -14.490 -0.274  1.00 26.88  ? 88  PRO A C   1 
ATOM   710  O O   . PRO A 1 89 ? 13.143  -14.706 -1.172  1.00 24.26  ? 88  PRO A O   1 
ATOM   711  C CB  . PRO A 1 89 ? 12.623  -13.919 1.843   1.00 23.43  ? 88  PRO A CB  1 
ATOM   712  C CG  . PRO A 1 89 ? 13.569  -12.940 2.553   1.00 24.18  ? 88  PRO A CG  1 
ATOM   713  C CD  . PRO A 1 89 ? 14.663  -13.836 3.100   1.00 24.35  ? 88  PRO A CD  1 
ATOM   714  N N   . HIS A 1 90 ? 15.134  -13.911 -0.492  1.00 24.75  ? 89  HIS A N   1 
ATOM   715  C CA  . HIS A 1 90 ? 15.505  -13.369 -1.806  1.00 23.92  ? 89  HIS A CA  1 
ATOM   716  C C   . HIS A 1 90 ? 16.597  -14.199 -2.488  1.00 26.86  ? 89  HIS A C   1 
ATOM   717  O O   . HIS A 1 90 ? 17.080  -13.803 -3.551  1.00 26.26  ? 89  HIS A O   1 
ATOM   718  C CB  . HIS A 1 90 ? 15.916  -11.885 -1.679  1.00 26.53  ? 89  HIS A CB  1 
ATOM   719  C CG  . HIS A 1 90 ? 14.823  -11.041 -1.119  1.00 25.30  ? 89  HIS A CG  1 
ATOM   720  N ND1 . HIS A 1 90 ? 13.576  -10.935 -1.715  1.00 27.80  ? 89  HIS A ND1 1 
ATOM   721  C CD2 . HIS A 1 90 ? 14.777  -10.265 -0.030  1.00 24.83  ? 89  HIS A CD2 1 
ATOM   722  C CE1 . HIS A 1 90 ? 12.816  -10.119 -1.002  1.00 24.61  ? 89  HIS A CE1 1 
ATOM   723  N NE2 . HIS A 1 90 ? 13.526  -9.729  0.052   1.00 28.26  ? 89  HIS A NE2 1 
ATOM   724  N N   . ALA A 1 91 ? 16.898  -15.389 -1.935  1.00 26.44  ? 90  ALA A N   1 
ATOM   725  C CA  . ALA A 1 91 ? 17.978  -16.209 -2.449  1.00 29.65  ? 90  ALA A CA  1 
ATOM   726  C C   . ALA A 1 91 ? 17.514  -16.900 -3.724  1.00 31.15  ? 90  ALA A C   1 
ATOM   727  O O   . ALA A 1 91 ? 16.325  -17.035 -3.963  1.00 27.87  ? 90  ALA A O   1 
ATOM   728  C CB  . ALA A 1 91 ? 18.388  -17.245 -1.437  1.00 29.93  ? 90  ALA A CB  1 
ATOM   729  N N   . SER A 1 92 ? 18.482  -17.388 -4.504  1.00 30.26  ? 91  SER A N   1 
ATOM   730  C CA  . SER A 1 92 ? 18.153  -18.266 -5.612  1.00 33.15  ? 91  SER A CA  1 
ATOM   731  C C   . SER A 1 92 ? 17.869  -19.658 -5.066  1.00 36.38  ? 91  SER A C   1 
ATOM   732  O O   . SER A 1 92 ? 18.663  -20.173 -4.273  1.00 40.44  ? 91  SER A O   1 
ATOM   733  C CB  . SER A 1 92 ? 19.277  -18.284 -6.606  1.00 37.36  ? 91  SER A CB  1 
ATOM   734  O OG  . SER A 1 92 ? 19.119  -19.433 -7.411  1.00 43.52  ? 91  SER A OG  1 
ATOM   735  N N   . TYR A 1 93 ? 16.713  -20.233 -5.433  1.00 29.91  ? 92  TYR A N   1 
ATOM   736  C CA  . TYR A 1 93 ? 16.349  -21.548 -4.925  1.00 31.51  ? 92  TYR A CA  1 
ATOM   737  C C   . TYR A 1 93 ? 16.252  -22.543 -6.081  1.00 37.64  ? 92  TYR A C   1 
ATOM   738  O O   . TYR A 1 93 ? 15.677  -23.618 -5.926  1.00 47.00  ? 92  TYR A O   1 
ATOM   739  C CB  . TYR A 1 93 ? 15.029  -21.561 -4.136  1.00 29.06  ? 92  TYR A CB  1 
ATOM   740  C CG  . TYR A 1 93 ? 15.150  -20.963 -2.747  1.00 27.86  ? 92  TYR A CG  1 
ATOM   741  C CD1 . TYR A 1 93 ? 15.582  -21.735 -1.666  1.00 30.51  ? 92  TYR A CD1 1 
ATOM   742  C CD2 . TYR A 1 93 ? 14.834  -19.621 -2.526  1.00 27.11  ? 92  TYR A CD2 1 
ATOM   743  C CE1 . TYR A 1 93 ? 15.745  -21.168 -0.408  1.00 32.46  ? 92  TYR A CE1 1 
ATOM   744  C CE2 . TYR A 1 93 ? 14.981  -19.062 -1.273  1.00 28.08  ? 92  TYR A CE2 1 
ATOM   745  C CZ  . TYR A 1 93 ? 15.406  -19.837 -0.212  1.00 27.46  ? 92  TYR A CZ  1 
ATOM   746  O OH  . TYR A 1 93 ? 15.597  -19.284 1.019   1.00 30.36  ? 92  TYR A OH  1 
ATOM   747  N N   . SER A 1 94 ? 16.833  -22.185 -7.228  1.00 45.95  ? 93  SER A N   1 
ATOM   748  C CA  . SER A 1 94 ? 16.985  -23.134 -8.319  1.00 63.48  ? 93  SER A CA  1 
ATOM   749  C C   . SER A 1 94 ? 17.861  -24.315 -7.857  1.00 73.98  ? 93  SER A C   1 
ATOM   750  O O   . SER A 1 94 ? 19.077  -24.084 -7.604  1.00 72.42  ? 93  SER A O   1 
ATOM   751  C CB  . SER A 1 94 ? 17.544  -22.459 -9.547  1.00 65.11  ? 93  SER A CB  1 
ATOM   752  O OG  . SER A 1 94 ? 16.697  -21.390 -9.945  1.00 74.04  ? 93  SER A OG  1 
ATOM   753  O OXT . SER A 1 94 ? 17.294  -25.430 -7.735  1.00 81.27  ? 93  SER A OXT 1 
ATOM   754  N N   . MET B 1 2  ? 38.773  -10.950 -41.966 1.00 63.56  ? 1   MET B N   1 
ATOM   755  C CA  . MET B 1 2  ? 38.426  -11.964 -42.997 1.00 65.95  ? 1   MET B CA  1 
ATOM   756  C C   . MET B 1 2  ? 36.903  -12.132 -43.046 1.00 58.35  ? 1   MET B C   1 
ATOM   757  O O   . MET B 1 2  ? 36.278  -12.391 -42.014 1.00 52.24  ? 1   MET B O   1 
ATOM   758  C CB  . MET B 1 2  ? 39.144  -13.289 -42.706 1.00 77.82  ? 1   MET B CB  1 
ATOM   759  C CG  . MET B 1 2  ? 39.328  -14.206 -43.912 1.00 93.54  ? 1   MET B CG  1 
ATOM   760  S SD  . MET B 1 2  ? 40.362  -13.567 -45.250 1.00 97.18  ? 1   MET B SD  1 
ATOM   761  C CE  . MET B 1 2  ? 41.776  -12.891 -44.367 1.00 90.05  ? 1   MET B CE  1 
ATOM   762  N N   . PRO B 1 3  ? 36.257  -11.983 -44.236 1.00 52.05  ? 2   PRO B N   1 
ATOM   763  C CA  . PRO B 1 3  ? 34.806  -12.171 -44.352 1.00 49.98  ? 2   PRO B CA  1 
ATOM   764  C C   . PRO B 1 3  ? 34.458  -13.592 -43.902 1.00 50.58  ? 2   PRO B C   1 
ATOM   765  O O   . PRO B 1 3  ? 35.260  -14.504 -44.075 1.00 46.99  ? 2   PRO B O   1 
ATOM   766  C CB  . PRO B 1 3  ? 34.513  -11.916 -45.832 1.00 50.12  ? 2   PRO B CB  1 
ATOM   767  C CG  . PRO B 1 3  ? 35.692  -11.081 -46.302 1.00 51.18  ? 2   PRO B CG  1 
ATOM   768  C CD  . PRO B 1 3  ? 36.885  -11.626 -45.521 1.00 48.81  ? 2   PRO B CD  1 
ATOM   769  N N   . HIS B 1 4  ? 33.297  -13.761 -43.255 1.00 48.19  ? 3   HIS B N   1 
ATOM   770  C CA  . HIS B 1 4  ? 32.864  -15.089 -42.838 1.00 49.64  ? 3   HIS B CA  1 
ATOM   771  C C   . HIS B 1 4  ? 31.525  -15.402 -43.499 1.00 46.76  ? 3   HIS B C   1 
ATOM   772  O O   . HIS B 1 4  ? 30.971  -14.545 -44.202 1.00 41.10  ? 3   HIS B O   1 
ATOM   773  C CB  . HIS B 1 4  ? 32.954  -15.231 -41.318 1.00 54.18  ? 3   HIS B CB  1 
ATOM   774  C CG  . HIS B 1 4  ? 34.369  -15.336 -40.828 1.00 69.72  ? 3   HIS B CG  1 
ATOM   775  N ND1 . HIS B 1 4  ? 35.288  -16.220 -41.363 1.00 69.01  ? 3   HIS B ND1 1 
ATOM   776  C CD2 . HIS B 1 4  ? 35.009  -14.688 -39.830 1.00 63.03  ? 3   HIS B CD2 1 
ATOM   777  C CE1 . HIS B 1 4  ? 36.437  -16.097 -40.712 1.00 62.47  ? 3   HIS B CE1 1 
ATOM   778  N NE2 . HIS B 1 4  ? 36.290  -15.170 -39.780 1.00 65.24  ? 3   HIS B NE2 1 
ATOM   779  N N   . ALA B 1 5  ? 31.012  -16.630 -43.293 1.00 41.02  ? 4   ALA B N   1 
ATOM   780  C CA  . ALA B 1 5  ? 29.713  -16.954 -43.870 1.00 43.44  ? 4   ALA B CA  1 
ATOM   781  C C   . ALA B 1 5  ? 28.702  -15.921 -43.388 1.00 45.19  ? 4   ALA B C   1 
ATOM   782  O O   . ALA B 1 5  ? 27.886  -15.436 -44.176 1.00 44.40  ? 4   ALA B O   1 
ATOM   783  C CB  . ALA B 1 5  ? 29.273  -18.353 -43.495 1.00 42.45  ? 4   ALA B CB  1 
ATOM   784  N N   . PHE B 1 6  ? 28.764  -15.635 -42.077 1.00 43.24  ? 5   PHE B N   1 
ATOM   785  C CA  . PHE B 1 6  ? 27.948  -14.607 -41.444 1.00 48.51  ? 5   PHE B CA  1 
ATOM   786  C C   . PHE B 1 6  ? 28.801  -13.360 -41.205 1.00 42.97  ? 5   PHE B C   1 
ATOM   787  O O   . PHE B 1 6  ? 29.911  -13.449 -40.683 1.00 42.35  ? 5   PHE B O   1 
ATOM   788  C CB  . PHE B 1 6  ? 27.350  -15.097 -40.119 1.00 40.69  ? 5   PHE B CB  1 
ATOM   789  C CG  . PHE B 1 6  ? 26.281  -16.180 -40.242 1.00 39.41  ? 5   PHE B CG  1 
ATOM   790  C CD1 . PHE B 1 6  ? 24.941  -15.844 -40.422 1.00 34.52  ? 5   PHE B CD1 1 
ATOM   791  C CD2 . PHE B 1 6  ? 26.618  -17.533 -40.191 1.00 40.45  ? 5   PHE B CD2 1 
ATOM   792  C CE1 . PHE B 1 6  ? 23.968  -16.823 -40.546 1.00 36.29  ? 5   PHE B CE1 1 
ATOM   793  C CE2 . PHE B 1 6  ? 25.637  -18.520 -40.298 1.00 33.36  ? 5   PHE B CE2 1 
ATOM   794  C CZ  . PHE B 1 6  ? 24.312  -18.160 -40.438 1.00 34.50  ? 5   PHE B CZ  1 
ATOM   795  N N   . LYS B 1 7  ? 28.260  -12.195 -41.571 1.00 47.29  ? 6   LYS B N   1 
ATOM   796  C CA  . LYS B 1 7  ? 28.972  -10.948 -41.335 1.00 43.56  ? 6   LYS B CA  1 
ATOM   797  C C   . LYS B 1 7  ? 28.213  -10.081 -40.328 1.00 42.58  ? 6   LYS B C   1 
ATOM   798  O O   . LYS B 1 7  ? 26.994  -10.212 -40.170 1.00 35.94  ? 6   LYS B O   1 
ATOM   799  C CB  . LYS B 1 7  ? 29.126  -10.242 -42.680 1.00 44.99  ? 6   LYS B CB  1 
ATOM   800  C CG  . LYS B 1 7  ? 27.830  -9.954  -43.396 1.00 44.23  ? 6   LYS B CG  1 
ATOM   801  C CD  . LYS B 1 7  ? 28.131  -9.572  -44.844 1.00 50.93  ? 6   LYS B CD  1 
ATOM   802  C CE  . LYS B 1 7  ? 26.929  -9.153  -45.629 1.00 49.77  ? 6   LYS B CE  1 
ATOM   803  N NZ  . LYS B 1 7  ? 25.971  -10.252 -45.843 1.00 51.59  ? 6   LYS B NZ  1 
ATOM   804  N N   . PRO B 1 8  ? 28.897  -9.107  -39.672 1.00 43.40  ? 7   PRO B N   1 
ATOM   805  C CA  . PRO B 1 8  ? 28.239  -8.226  -38.705 1.00 38.81  ? 7   PRO B CA  1 
ATOM   806  C C   . PRO B 1 8  ? 27.090  -7.500  -39.384 1.00 38.66  ? 7   PRO B C   1 
ATOM   807  O O   . PRO B 1 8  ? 27.228  -7.022  -40.512 1.00 40.69  ? 7   PRO B O   1 
ATOM   808  C CB  . PRO B 1 8  ? 29.405  -7.309  -38.313 1.00 43.85  ? 7   PRO B CB  1 
ATOM   809  C CG  . PRO B 1 8  ? 30.632  -8.207  -38.474 1.00 45.18  ? 7   PRO B CG  1 
ATOM   810  C CD  . PRO B 1 8  ? 30.332  -8.792  -39.837 1.00 45.22  ? 7   PRO B CD  1 
ATOM   811  N N   . GLY B 1 9  ? 25.927  -7.502  -38.716 1.00 32.11  ? 8   GLY B N   1 
ATOM   812  C CA  . GLY B 1 9  ? 24.711  -6.883  -39.216 1.00 32.20  ? 8   GLY B CA  1 
ATOM   813  C C   . GLY B 1 9  ? 23.745  -7.867  -39.870 1.00 30.17  ? 8   GLY B C   1 
ATOM   814  O O   . GLY B 1 9  ? 22.623  -7.493  -40.195 1.00 32.73  ? 8   GLY B O   1 
ATOM   815  N N   . ASP B 1 10 ? 24.185  -9.118  -40.102 1.00 32.19  ? 9   ASP B N   1 
ATOM   816  C CA  . ASP B 1 10 ? 23.299  -10.125 -40.671 1.00 30.95  ? 9   ASP B CA  1 
ATOM   817  C C   . ASP B 1 10 ? 22.192  -10.456 -39.664 1.00 26.58  ? 9   ASP B C   1 
ATOM   818  O O   . ASP B 1 10 ? 22.452  -10.520 -38.465 1.00 29.08  ? 9   ASP B O   1 
ATOM   819  C CB  . ASP B 1 10 ? 24.032  -11.430 -40.933 1.00 30.74  ? 9   ASP B CB  1 
ATOM   820  C CG  . ASP B 1 10 ? 24.774  -11.507 -42.269 1.00 41.53  ? 9   ASP B CG  1 
ATOM   821  O OD1 . ASP B 1 10 ? 24.426  -10.730 -43.174 1.00 38.96  ? 9   ASP B OD1 1 
ATOM   822  O OD2 . ASP B 1 10 ? 25.682  -12.361 -42.401 1.00 40.16  ? 9   ASP B OD2 1 
ATOM   823  N N   . LEU B 1 11 ? 20.968  -10.578 -40.151 1.00 26.32  ? 10  LEU B N   1 
ATOM   824  C CA  . LEU B 1 11 ? 19.864  -10.833 -39.232 1.00 27.22  ? 10  LEU B CA  1 
ATOM   825  C C   . LEU B 1 11 ? 19.588  -12.329 -39.221 1.00 28.11  ? 10  LEU B C   1 
ATOM   826  O O   . LEU B 1 11 ? 19.737  -12.964 -40.256 1.00 31.46  ? 10  LEU B O   1 
ATOM   827  C CB  . LEU B 1 11 ? 18.664  -10.031 -39.711 1.00 26.78  ? 10  LEU B CB  1 
ATOM   828  C CG  . LEU B 1 11 ? 18.967  -8.523  -39.787 1.00 27.34  ? 10  LEU B CG  1 
ATOM   829  C CD1 . LEU B 1 11 ? 17.683  -7.793  -40.110 1.00 29.09  ? 10  LEU B CD1 1 
ATOM   830  C CD2 . LEU B 1 11 ? 19.641  -8.078  -38.474 1.00 28.10  ? 10  LEU B CD2 1 
ATOM   831  N N   . VAL B 1 12 ? 19.176  -12.874 -38.066 1.00 24.87  ? 11  VAL B N   1 
ATOM   832  C CA  . VAL B 1 12 ? 19.033  -14.322 -37.954 1.00 21.92  ? 11  VAL B CA  1 
ATOM   833  C C   . VAL B 1 12 ? 17.938  -14.602 -36.929 1.00 28.39  ? 11  VAL B C   1 
ATOM   834  O O   . VAL B 1 12 ? 17.523  -13.695 -36.209 1.00 26.04  ? 11  VAL B O   1 
ATOM   835  C CB  . VAL B 1 12 ? 20.342  -15.025 -37.516 1.00 24.40  ? 11  VAL B CB  1 
ATOM   836  C CG1 . VAL B 1 12 ? 21.481  -14.920 -38.555 1.00 26.97  ? 11  VAL B CG1 1 
ATOM   837  C CG2 . VAL B 1 12 ? 20.793  -14.685 -36.070 1.00 25.70  ? 11  VAL B CG2 1 
ATOM   838  N N   . PHE B 1 13 ? 17.515  -15.873 -36.876 1.00 26.79  ? 12  PHE B N   1 
ATOM   839  C CA  . PHE B 1 13 ? 16.977  -16.403 -35.639 1.00 26.45  ? 12  PHE B CA  1 
ATOM   840  C C   . PHE B 1 13 ? 18.059  -17.286 -35.059 1.00 29.23  ? 12  PHE B C   1 
ATOM   841  O O   . PHE B 1 13 ? 18.667  -18.071 -35.818 1.00 28.31  ? 12  PHE B O   1 
ATOM   842  C CB  . PHE B 1 13 ? 15.692  -17.196 -35.846 1.00 25.60  ? 12  PHE B CB  1 
ATOM   843  C CG  . PHE B 1 13 ? 14.502  -16.359 -36.265 1.00 27.90  ? 12  PHE B CG  1 
ATOM   844  C CD1 . PHE B 1 13 ? 14.252  -16.124 -37.616 1.00 30.27  ? 12  PHE B CD1 1 
ATOM   845  C CD2 . PHE B 1 13 ? 13.595  -15.885 -35.319 1.00 29.69  ? 12  PHE B CD2 1 
ATOM   846  C CE1 . PHE B 1 13 ? 13.135  -15.398 -38.004 1.00 32.80  ? 12  PHE B CE1 1 
ATOM   847  C CE2 . PHE B 1 13 ? 12.478  -15.142 -35.699 1.00 29.67  ? 12  PHE B CE2 1 
ATOM   848  C CZ  . PHE B 1 13 ? 12.246  -14.910 -37.053 1.00 35.12  ? 12  PHE B CZ  1 
ATOM   849  N N   . ALA B 1 14 ? 18.273  -17.122 -33.732 1.00 24.63  ? 13  ALA B N   1 
ATOM   850  C CA  . ALA B 1 14 ? 19.299  -17.829 -32.991 1.00 26.46  ? 13  ALA B CA  1 
ATOM   851  C C   . ALA B 1 14 ? 18.682  -18.761 -31.949 1.00 25.62  ? 13  ALA B C   1 
ATOM   852  O O   . ALA B 1 14 ? 17.787  -18.361 -31.201 1.00 25.15  ? 13  ALA B O   1 
ATOM   853  C CB  . ALA B 1 14 ? 20.263  -16.858 -32.339 1.00 26.11  ? 13  ALA B CB  1 
ATOM   854  N N   . LYS B 1 15 ? 19.175  -19.993 -31.923 1.00 25.79  ? 14  LYS B N   1 
ATOM   855  C CA  . LYS B 1 15 ? 18.560  -21.065 -31.150 1.00 28.43  ? 14  LYS B CA  1 
ATOM   856  C C   . LYS B 1 15 ? 19.445  -21.373 -29.947 1.00 29.06  ? 14  LYS B C   1 
ATOM   857  O O   . LYS B 1 15 ? 20.647  -21.608 -30.096 1.00 32.08  ? 14  LYS B O   1 
ATOM   858  C CB  . LYS B 1 15 ? 18.395  -22.366 -31.953 1.00 29.56  ? 14  LYS B CB  1 
ATOM   859  C CG  . LYS B 1 15 ? 17.656  -23.486 -31.155 1.00 27.18  ? 14  LYS B CG  1 
ATOM   860  C CD  . LYS B 1 15 ? 16.190  -23.110 -30.897 1.00 33.00  ? 14  LYS B CD  1 
ATOM   861  C CE  . LYS B 1 15 ? 15.314  -24.214 -30.232 1.00 31.85  ? 14  LYS B CE  1 
ATOM   862  N NZ  . LYS B 1 15 ? 15.806  -24.441 -28.862 1.00 29.83  ? 14  LYS B NZ  1 
ATOM   863  N N   . MET B 1 16 ? 18.820  -21.337 -28.771 1.00 30.59  ? 15  MET B N   1 
ATOM   864  C CA  . MET B 1 16 ? 19.443  -21.712 -27.513 1.00 36.97  ? 15  MET B CA  1 
ATOM   865  C C   . MET B 1 16 ? 18.570  -22.761 -26.820 1.00 33.68  ? 15  MET B C   1 
ATOM   866  O O   . MET B 1 16 ? 17.336  -22.725 -26.911 1.00 29.58  ? 15  MET B O   1 
ATOM   867  C CB  . MET B 1 16 ? 19.707  -20.482 -26.629 1.00 35.80  ? 15  MET B CB  1 
ATOM   868  C CG  . MET B 1 16 ? 20.902  -19.658 -27.125 1.00 44.84  ? 15  MET B CG  1 
ATOM   869  S SD  . MET B 1 16 ? 21.647  -18.441 -26.018 1.00 46.46  ? 15  MET B SD  1 
ATOM   870  C CE  . MET B 1 16 ? 22.260  -19.462 -24.675 1.00 44.00  ? 15  MET B CE  1 
ATOM   871  N N   . LYS B 1 17 ? 19.222  -23.715 -26.145 1.00 34.04  ? 16  LYS B N   1 
ATOM   872  C CA  . LYS B 1 17 ? 18.477  -24.751 -25.439 1.00 37.18  ? 16  LYS B CA  1 
ATOM   873  C C   . LYS B 1 17 ? 17.523  -24.071 -24.448 1.00 33.97  ? 16  LYS B C   1 
ATOM   874  O O   . LYS B 1 17 ? 17.907  -23.120 -23.765 1.00 32.39  ? 16  LYS B O   1 
ATOM   875  C CB  . LYS B 1 17 ? 19.436  -25.736 -24.749 1.00 45.57  ? 16  LYS B CB  1 
ATOM   876  C CG  . LYS B 1 17 ? 18.736  -26.926 -24.051 1.00 48.40  ? 16  LYS B CG  1 
ATOM   877  C CD  . LYS B 1 17 ? 19.596  -27.637 -23.009 1.00 51.11  ? 16  LYS B CD  1 
ATOM   878  N N   . GLY B 1 18 ? 16.258  -24.505 -24.449 1.00 36.08  ? 17  GLY B N   1 
ATOM   879  C CA  . GLY B 1 18 ? 15.264  -23.971 -23.527 1.00 36.22  ? 17  GLY B CA  1 
ATOM   880  C C   . GLY B 1 18 ? 14.425  -22.822 -24.098 1.00 35.27  ? 17  GLY B C   1 
ATOM   881  O O   . GLY B 1 18 ? 13.528  -22.350 -23.408 1.00 37.83  ? 17  GLY B O   1 
ATOM   882  N N   . TYR B 1 19 ? 14.707  -22.364 -25.337 1.00 31.77  ? 18  TYR B N   1 
ATOM   883  C CA  . TYR B 1 19 ? 14.039  -21.175 -25.862 1.00 29.00  ? 18  TYR B CA  1 
ATOM   884  C C   . TYR B 1 19 ? 13.679  -21.378 -27.333 1.00 30.56  ? 18  TYR B C   1 
ATOM   885  O O   . TYR B 1 19 ? 14.362  -22.112 -28.030 1.00 32.67  ? 18  TYR B O   1 
ATOM   886  C CB  . TYR B 1 19 ? 14.875  -19.888 -25.788 1.00 27.08  ? 18  TYR B CB  1 
ATOM   887  C CG  . TYR B 1 19 ? 15.343  -19.614 -24.372 1.00 29.18  ? 18  TYR B CG  1 
ATOM   888  C CD1 . TYR B 1 19 ? 14.491  -19.016 -23.444 1.00 30.25  ? 18  TYR B CD1 1 
ATOM   889  C CD2 . TYR B 1 19 ? 16.585  -20.056 -23.938 1.00 30.87  ? 18  TYR B CD2 1 
ATOM   890  C CE1 . TYR B 1 19 ? 14.895  -18.847 -22.124 1.00 33.21  ? 18  TYR B CE1 1 
ATOM   891  C CE2 . TYR B 1 19 ? 17.003  -19.871 -22.626 1.00 35.23  ? 18  TYR B CE2 1 
ATOM   892  C CZ  . TYR B 1 19 ? 16.149  -19.268 -21.718 1.00 35.42  ? 18  TYR B CZ  1 
ATOM   893  O OH  . TYR B 1 19 ? 16.585  -19.101 -20.432 1.00 36.93  ? 18  TYR B OH  1 
ATOM   894  N N   . PRO B 1 20 ? 12.618  -20.718 -27.844 1.00 29.25  ? 19  PRO B N   1 
ATOM   895  C CA  . PRO B 1 20 ? 12.286  -20.797 -29.272 1.00 27.76  ? 19  PRO B CA  1 
ATOM   896  C C   . PRO B 1 20 ? 13.377  -20.089 -30.080 1.00 29.71  ? 19  PRO B C   1 
ATOM   897  O O   . PRO B 1 20 ? 14.056  -19.223 -29.544 1.00 29.47  ? 19  PRO B O   1 
ATOM   898  C CB  . PRO B 1 20 ? 10.947  -20.074 -29.348 1.00 29.01  ? 19  PRO B CB  1 
ATOM   899  C CG  . PRO B 1 20 ? 11.005  -19.060 -28.202 1.00 32.14  ? 19  PRO B CG  1 
ATOM   900  C CD  . PRO B 1 20 ? 11.740  -19.824 -27.084 1.00 30.35  ? 19  PRO B CD  1 
ATOM   901  N N   . HIS B 1 21 ? 13.546  -20.455 -31.360 1.00 26.92  ? 20  HIS B N   1 
ATOM   902  C CA  . HIS B 1 21 ? 14.402  -19.686 -32.272 1.00 28.37  ? 20  HIS B CA  1 
ATOM   903  C C   . HIS B 1 21 ? 14.144  -18.184 -32.105 1.00 25.80  ? 20  HIS B C   1 
ATOM   904  O O   . HIS B 1 21 ? 13.008  -17.728 -32.183 1.00 25.28  ? 20  HIS B O   1 
ATOM   905  C CB  . HIS B 1 21 ? 14.144  -20.132 -33.724 1.00 25.76  ? 20  HIS B CB  1 
ATOM   906  C CG  . HIS B 1 21 ? 14.354  -21.620 -33.898 1.00 26.66  ? 20  HIS B CG  1 
ATOM   907  N ND1 . HIS B 1 21 ? 13.410  -22.553 -33.498 1.00 30.48  ? 20  HIS B ND1 1 
ATOM   908  C CD2 . HIS B 1 21 ? 15.371  -22.330 -34.399 1.00 28.45  ? 20  HIS B CD2 1 
ATOM   909  C CE1 . HIS B 1 21 ? 13.864  -23.791 -33.743 1.00 27.12  ? 20  HIS B CE1 1 
ATOM   910  N NE2 . HIS B 1 21 ? 15.051  -23.679 -34.301 1.00 28.17  ? 20  HIS B NE2 1 
ATOM   911  N N   . TRP B 1 22 ? 15.202  -17.409 -31.895 1.00 25.14  ? 21  TRP B N   1 
ATOM   912  C CA  . TRP B 1 22 ? 14.982  -16.087 -31.309 1.00 24.17  ? 21  TRP B CA  1 
ATOM   913  C C   . TRP B 1 22 ? 15.504  -14.974 -32.219 1.00 25.64  ? 21  TRP B C   1 
ATOM   914  O O   . TRP B 1 22 ? 16.619  -15.096 -32.730 1.00 24.70  ? 21  TRP B O   1 
ATOM   915  C CB  . TRP B 1 22 ? 15.662  -16.029 -29.928 1.00 22.51  ? 21  TRP B CB  1 
ATOM   916  C CG  . TRP B 1 22 ? 15.143  -14.878 -29.097 1.00 26.41  ? 21  TRP B CG  1 
ATOM   917  C CD1 . TRP B 1 22 ? 15.445  -13.540 -29.197 1.00 25.43  ? 21  TRP B CD1 1 
ATOM   918  C CD2 . TRP B 1 22 ? 14.210  -14.990 -27.993 1.00 26.35  ? 21  TRP B CD2 1 
ATOM   919  N NE1 . TRP B 1 22 ? 14.710  -12.812 -28.280 1.00 28.61  ? 21  TRP B NE1 1 
ATOM   920  C CE2 . TRP B 1 22 ? 13.959  -13.677 -27.521 1.00 25.02  ? 21  TRP B CE2 1 
ATOM   921  C CE3 . TRP B 1 22 ? 13.562  -16.080 -27.400 1.00 26.63  ? 21  TRP B CE3 1 
ATOM   922  C CZ2 . TRP B 1 22 ? 13.094  -13.432 -26.452 1.00 23.97  ? 21  TRP B CZ2 1 
ATOM   923  C CZ3 . TRP B 1 22 ? 12.711  -15.848 -26.337 1.00 26.26  ? 21  TRP B CZ3 1 
ATOM   924  C CH2 . TRP B 1 22 ? 12.455  -14.534 -25.916 1.00 25.05  ? 21  TRP B CH2 1 
ATOM   925  N N   . PRO B 1 23 ? 14.737  -13.884 -32.491 1.00 27.76  ? 22  PRO B N   1 
ATOM   926  C CA  . PRO B 1 23 ? 15.220  -12.806 -33.374 1.00 26.66  ? 22  PRO B CA  1 
ATOM   927  C C   . PRO B 1 23 ? 16.528  -12.217 -32.861 1.00 27.68  ? 22  PRO B C   1 
ATOM   928  O O   . PRO B 1 23 ? 16.672  -11.891 -31.692 1.00 26.51  ? 22  PRO B O   1 
ATOM   929  C CB  . PRO B 1 23 ? 14.083  -11.766 -33.432 1.00 26.54  ? 22  PRO B CB  1 
ATOM   930  C CG  . PRO B 1 23 ? 13.232  -12.119 -32.203 1.00 26.98  ? 22  PRO B CG  1 
ATOM   931  C CD  . PRO B 1 23 ? 13.353  -13.648 -32.062 1.00 24.71  ? 22  PRO B CD  1 
ATOM   932  N N   . ALA B 1 24 ? 17.520  -12.114 -33.742 1.00 24.92  ? 23  ALA B N   1 
ATOM   933  C CA  . ALA B 1 24 ? 18.851  -11.755 -33.294 1.00 26.56  ? 23  ALA B CA  1 
ATOM   934  C C   . ALA B 1 24 ? 19.661  -11.208 -34.475 1.00 23.35  ? 23  ALA B C   1 
ATOM   935  O O   . ALA B 1 24 ? 19.186  -11.201 -35.612 1.00 26.53  ? 23  ALA B O   1 
ATOM   936  C CB  . ALA B 1 24 ? 19.513  -12.972 -32.672 1.00 26.06  ? 23  ALA B CB  1 
ATOM   937  N N   . ARG B 1 25 ? 20.879  -10.744 -34.169 1.00 26.19  ? 24  ARG B N   1 
ATOM   938  C CA  . ARG B 1 25 ? 21.804  -10.268 -35.191 1.00 26.84  ? 24  ARG B CA  1 
ATOM   939  C C   . ARG B 1 25 ? 23.208  -10.725 -34.838 1.00 26.21  ? 24  ARG B C   1 
ATOM   940  O O   . ARG B 1 25 ? 23.480  -11.054 -33.690 1.00 27.88  ? 24  ARG B O   1 
ATOM   941  C CB  . ARG B 1 25 ? 21.810  -8.732  -35.230 1.00 25.01  ? 24  ARG B CB  1 
ATOM   942  C CG  . ARG B 1 25 ? 22.465  -8.054  -34.034 1.00 29.88  ? 24  ARG B CG  1 
ATOM   943  C CD  . ARG B 1 25 ? 22.175  -6.541  -34.210 1.00 27.75  ? 24  ARG B CD  1 
ATOM   944  N NE  . ARG B 1 25 ? 22.760  -5.820  -33.083 1.00 30.46  ? 24  ARG B NE  1 
ATOM   945  C CZ  . ARG B 1 25 ? 22.492  -4.561  -32.699 1.00 33.07  ? 24  ARG B CZ  1 
ATOM   946  N NH1 . ARG B 1 25 ? 21.545  -3.875  -33.311 1.00 29.06  ? 24  ARG B NH1 1 
ATOM   947  N NH2 . ARG B 1 25 ? 23.174  -4.019  -31.701 1.00 28.43  ? 24  ARG B NH2 1 
ATOM   948  N N   . ILE B 1 26 ? 24.087  -10.775 -35.864 1.00 26.54  ? 25  ILE B N   1 
ATOM   949  C CA  . ILE B 1 26 ? 25.506  -10.927 -35.626 1.00 29.71  ? 25  ILE B CA  1 
ATOM   950  C C   . ILE B 1 26 ? 26.031  -9.527  -35.314 1.00 32.72  ? 25  ILE B C   1 
ATOM   951  O O   . ILE B 1 26 ? 25.742  -8.589  -36.064 1.00 33.01  ? 25  ILE B O   1 
ATOM   952  C CB  . ILE B 1 26 ? 26.154  -11.422 -36.933 1.00 34.72  ? 25  ILE B CB  1 
ATOM   953  C CG1 . ILE B 1 26 ? 25.384  -12.581 -37.541 1.00 33.02  ? 25  ILE B CG1 1 
ATOM   954  C CG2 . ILE B 1 26 ? 27.642  -11.710 -36.751 1.00 35.33  ? 25  ILE B CG2 1 
ATOM   955  C CD1 . ILE B 1 26 ? 25.326  -13.802 -36.638 1.00 29.00  ? 25  ILE B CD1 1 
ATOM   956  N N   . ASP B 1 27 ? 26.819  -9.432  -34.238 1.00 33.68  ? 26  ASP B N   1 
ATOM   957  C CA  . ASP B 1 27 ? 27.519  -8.221  -33.823 1.00 43.38  ? 26  ASP B CA  1 
ATOM   958  C C   . ASP B 1 27 ? 28.977  -8.249  -34.310 1.00 45.26  ? 26  ASP B C   1 
ATOM   959  O O   . ASP B 1 27 ? 29.496  -9.316  -34.621 1.00 45.83  ? 26  ASP B O   1 
ATOM   960  C CB  . ASP B 1 27 ? 27.463  -8.136  -32.306 1.00 36.83  ? 26  ASP B CB  1 
ATOM   961  C CG  . ASP B 1 27 ? 26.287  -7.357  -31.731 1.00 42.42  ? 26  ASP B CG  1 
ATOM   962  O OD1 . ASP B 1 27 ? 25.545  -6.735  -32.529 1.00 40.37  ? 26  ASP B OD1 1 
ATOM   963  O OD2 . ASP B 1 27 ? 26.142  -7.346  -30.481 1.00 41.12  ? 26  ASP B OD2 1 
ATOM   964  N N   A ASP B 1 28 ? 29.634  -7.079  -34.248 0.50 51.02  ? 27  ASP B N   1 
ATOM   965  N N   B ASP B 1 28 ? 29.635  -7.080  -34.385 0.50 47.79  ? 27  ASP B N   1 
ATOM   966  C CA  A ASP B 1 28 ? 31.016  -6.859  -34.659 0.50 53.57  ? 27  ASP B CA  1 
ATOM   967  C CA  B ASP B 1 28 ? 31.008  -7.009  -34.878 0.50 48.08  ? 27  ASP B CA  1 
ATOM   968  C C   A ASP B 1 28 ? 31.991  -7.526  -33.679 0.50 52.56  ? 27  ASP B C   1 
ATOM   969  C C   B ASP B 1 28 ? 31.998  -7.362  -33.760 0.50 47.38  ? 27  ASP B C   1 
ATOM   970  O O   A ASP B 1 28 ? 31.546  -7.871  -32.561 0.50 55.88  ? 27  ASP B O   1 
ATOM   971  O O   B ASP B 1 28 ? 31.791  -6.862  -32.635 0.50 52.57  ? 27  ASP B O   1 
ATOM   972  C CB  A ASP B 1 28 ? 31.308  -5.371  -34.773 0.50 49.68  ? 27  ASP B CB  1 
ATOM   973  C CB  B ASP B 1 28 ? 31.350  -5.648  -35.467 0.50 44.18  ? 27  ASP B CB  1 
ATOM   974  C CG  A ASP B 1 28 ? 30.184  -4.551  -35.392 0.50 50.37  ? 27  ASP B CG  1 
ATOM   975  C CG  B ASP B 1 28 ? 32.378  -5.673  -36.588 0.50 41.13  ? 27  ASP B CG  1 
ATOM   976  O OD1 A ASP B 1 28 ? 30.303  -4.197  -36.582 0.50 54.56  ? 27  ASP B OD1 1 
ATOM   977  O OD1 B ASP B 1 28 ? 33.393  -6.386  -36.443 0.50 42.68  ? 27  ASP B OD1 1 
ATOM   978  O OD2 A ASP B 1 28 ? 29.196  -4.267  -34.678 0.50 50.45  ? 27  ASP B OD2 1 
ATOM   979  O OD2 B ASP B 1 28 ? 32.157  -4.983  -37.605 0.50 40.10  ? 27  ASP B OD2 1 
ATOM   980  N N   . VAL B 1 34 ? 37.078  -9.780  -25.320 1.00 69.98  ? 33  VAL B N   1 
ATOM   981  C CA  . VAL B 1 34 ? 36.791  -11.247 -25.311 1.00 72.34  ? 33  VAL B CA  1 
ATOM   982  C C   . VAL B 1 34 ? 36.320  -11.626 -26.709 1.00 76.98  ? 33  VAL B C   1 
ATOM   983  O O   . VAL B 1 34 ? 35.201  -11.294 -27.088 1.00 87.28  ? 33  VAL B O   1 
ATOM   984  C CB  . VAL B 1 34 ? 35.734  -11.602 -24.243 1.00 71.30  ? 33  VAL B CB  1 
ATOM   985  C CG1 . VAL B 1 34 ? 34.545  -10.646 -24.268 1.00 70.25  ? 33  VAL B CG1 1 
ATOM   986  C CG2 . VAL B 1 34 ? 35.264  -13.051 -24.339 1.00 65.89  ? 33  VAL B CG2 1 
ATOM   987  N N   . LYS B 1 35 ? 37.185  -12.304 -27.471 1.00 76.25  ? 34  LYS B N   1 
ATOM   988  C CA  . LYS B 1 35 ? 36.826  -12.755 -28.809 1.00 66.80  ? 34  LYS B CA  1 
ATOM   989  C C   . LYS B 1 35 ? 35.983  -14.032 -28.712 1.00 65.40  ? 34  LYS B C   1 
ATOM   990  O O   . LYS B 1 35 ? 36.071  -14.774 -27.728 1.00 61.56  ? 34  LYS B O   1 
ATOM   991  C CB  . LYS B 1 35 ? 38.075  -12.879 -29.693 1.00 61.49  ? 34  LYS B CB  1 
ATOM   992  N N   . PRO B 1 36 ? 35.110  -14.322 -29.710 1.00 60.24  ? 35  PRO B N   1 
ATOM   993  C CA  . PRO B 1 36 ? 34.352  -15.578 -29.716 1.00 56.06  ? 35  PRO B CA  1 
ATOM   994  C C   . PRO B 1 36 ? 35.257  -16.805 -29.666 1.00 47.02  ? 35  PRO B C   1 
ATOM   995  O O   . PRO B 1 36 ? 36.374  -16.759 -30.160 1.00 57.64  ? 35  PRO B O   1 
ATOM   996  C CB  . PRO B 1 36 ? 33.550  -15.505 -31.032 1.00 55.10  ? 35  PRO B CB  1 
ATOM   997  C CG  . PRO B 1 36 ? 34.254  -14.443 -31.860 1.00 61.89  ? 35  PRO B CG  1 
ATOM   998  C CD  . PRO B 1 36 ? 34.779  -13.444 -30.846 1.00 58.09  ? 35  PRO B CD  1 
ATOM   999  N N   . PRO B 1 37 ? 34.828  -17.927 -29.051 1.00 50.25  ? 36  PRO B N   1 
ATOM   1000 C CA  . PRO B 1 37 ? 35.542  -19.193 -29.205 1.00 50.10  ? 36  PRO B CA  1 
ATOM   1001 C C   . PRO B 1 37 ? 35.632  -19.492 -30.700 1.00 54.51  ? 36  PRO B C   1 
ATOM   1002 O O   . PRO B 1 37 ? 34.881  -18.925 -31.506 1.00 51.37  ? 36  PRO B O   1 
ATOM   1003 C CB  . PRO B 1 37 ? 34.636  -20.201 -28.480 1.00 53.13  ? 36  PRO B CB  1 
ATOM   1004 C CG  . PRO B 1 37 ? 33.868  -19.368 -27.473 1.00 52.92  ? 36  PRO B CG  1 
ATOM   1005 C CD  . PRO B 1 37 ? 33.657  -18.033 -28.166 1.00 52.51  ? 36  PRO B CD  1 
ATOM   1006 N N   . PRO B 1 38 ? 36.527  -20.418 -31.120 1.00 56.88  ? 37  PRO B N   1 
ATOM   1007 C CA  . PRO B 1 38 ? 36.592  -20.832 -32.529 1.00 55.81  ? 37  PRO B CA  1 
ATOM   1008 C C   . PRO B 1 38 ? 35.240  -21.300 -33.093 1.00 49.95  ? 37  PRO B C   1 
ATOM   1009 O O   . PRO B 1 38 ? 34.479  -21.974 -32.398 1.00 50.70  ? 37  PRO B O   1 
ATOM   1010 C CB  . PRO B 1 38 ? 37.661  -21.959 -32.557 1.00 54.14  ? 37  PRO B CB  1 
ATOM   1011 C CG  . PRO B 1 38 ? 38.406  -21.845 -31.230 1.00 52.18  ? 37  PRO B CG  1 
ATOM   1012 C CD  . PRO B 1 38 ? 37.502  -21.105 -30.250 1.00 57.01  ? 37  PRO B CD  1 
ATOM   1013 N N   . ASN B 1 39 ? 34.953  -20.931 -34.353 1.00 46.35  ? 38  ASN B N   1 
ATOM   1014 C CA  . ASN B 1 39 ? 33.751  -21.328 -35.095 1.00 48.59  ? 38  ASN B CA  1 
ATOM   1015 C C   . ASN B 1 39 ? 32.483  -20.578 -34.654 1.00 44.82  ? 38  ASN B C   1 
ATOM   1016 O O   . ASN B 1 39 ? 31.446  -20.708 -35.300 1.00 39.87  ? 38  ASN B O   1 
ATOM   1017 C CB  . ASN B 1 39 ? 33.442  -22.822 -35.005 1.00 49.32  ? 38  ASN B CB  1 
ATOM   1018 C CG  . ASN B 1 39 ? 34.677  -23.695 -35.041 1.00 61.48  ? 38  ASN B CG  1 
ATOM   1019 O OD1 . ASN B 1 39 ? 34.939  -24.425 -34.076 1.00 67.88  ? 38  ASN B OD1 1 
ATOM   1020 N ND2 . ASN B 1 39 ? 35.456  -23.619 -36.113 1.00 52.72  ? 38  ASN B ND2 1 
ATOM   1021 N N   . LYS B 1 40 ? 32.550  -19.793 -33.566 1.00 44.26  ? 39  LYS B N   1 
ATOM   1022 C CA  . LYS B 1 40 ? 31.365  -19.139 -33.026 1.00 46.04  ? 39  LYS B CA  1 
ATOM   1023 C C   . LYS B 1 40 ? 31.335  -17.658 -33.400 1.00 40.72  ? 39  LYS B C   1 
ATOM   1024 O O   . LYS B 1 40 ? 32.322  -17.103 -33.840 1.00 47.50  ? 39  LYS B O   1 
ATOM   1025 C CB  . LYS B 1 40 ? 31.315  -19.380 -31.516 1.00 42.76  ? 39  LYS B CB  1 
ATOM   1026 C CG  . LYS B 1 40 ? 30.984  -20.812 -31.109 1.00 43.79  ? 39  LYS B CG  1 
ATOM   1027 C CD  . LYS B 1 40 ? 30.905  -20.910 -29.587 1.00 58.83  ? 39  LYS B CD  1 
ATOM   1028 C CE  . LYS B 1 40 ? 29.796  -21.750 -29.016 1.00 68.14  ? 39  LYS B CE  1 
ATOM   1029 N NZ  . LYS B 1 40 ? 30.085  -23.184 -28.965 1.00 66.74  ? 39  LYS B NZ  1 
ATOM   1030 N N   . TYR B 1 41 ? 30.170  -17.039 -33.228 1.00 37.07  ? 40  TYR B N   1 
ATOM   1031 C CA  . TYR B 1 41 ? 29.908  -15.645 -33.557 1.00 34.28  ? 40  TYR B CA  1 
ATOM   1032 C C   . TYR B 1 41 ? 29.347  -14.929 -32.334 1.00 36.88  ? 40  TYR B C   1 
ATOM   1033 O O   . TYR B 1 41 ? 28.589  -15.519 -31.562 1.00 35.91  ? 40  TYR B O   1 
ATOM   1034 C CB  . TYR B 1 41 ? 28.838  -15.522 -34.642 1.00 33.10  ? 40  TYR B CB  1 
ATOM   1035 C CG  . TYR B 1 41 ? 29.303  -15.966 -36.023 1.00 34.79  ? 40  TYR B CG  1 
ATOM   1036 C CD1 . TYR B 1 41 ? 29.964  -15.087 -36.871 1.00 34.12  ? 40  TYR B CD1 1 
ATOM   1037 C CD2 . TYR B 1 41 ? 29.113  -17.268 -36.457 1.00 34.51  ? 40  TYR B CD2 1 
ATOM   1038 C CE1 . TYR B 1 41 ? 30.426  -15.500 -38.114 1.00 40.31  ? 40  TYR B CE1 1 
ATOM   1039 C CE2 . TYR B 1 41 ? 29.552  -17.693 -37.705 1.00 37.20  ? 40  TYR B CE2 1 
ATOM   1040 C CZ  . TYR B 1 41 ? 30.232  -16.808 -38.532 1.00 41.70  ? 40  TYR B CZ  1 
ATOM   1041 O OH  . TYR B 1 41 ? 30.657  -17.188 -39.786 1.00 38.76  ? 40  TYR B OH  1 
ATOM   1042 N N   . PRO B 1 42 ? 29.621  -13.606 -32.198 1.00 38.84  ? 41  PRO B N   1 
ATOM   1043 C CA  . PRO B 1 42 ? 28.935  -12.780 -31.202 1.00 35.29  ? 41  PRO B CA  1 
ATOM   1044 C C   . PRO B 1 42 ? 27.487  -12.550 -31.639 1.00 32.47  ? 41  PRO B C   1 
ATOM   1045 O O   . PRO B 1 42 ? 27.236  -11.953 -32.698 1.00 33.66  ? 41  PRO B O   1 
ATOM   1046 C CB  . PRO B 1 42 ? 29.740  -11.436 -31.181 1.00 37.67  ? 41  PRO B CB  1 
ATOM   1047 C CG  . PRO B 1 42 ? 30.721  -11.500 -32.350 1.00 39.57  ? 41  PRO B CG  1 
ATOM   1048 C CD  . PRO B 1 42 ? 30.543  -12.838 -33.061 1.00 35.85  ? 41  PRO B CD  1 
ATOM   1049 N N   . ILE B 1 43 ? 26.537  -13.008 -30.803 1.00 30.61  ? 42  ILE B N   1 
ATOM   1050 C CA  . ILE B 1 43 ? 25.110  -12.863 -31.080 1.00 30.59  ? 42  ILE B CA  1 
ATOM   1051 C C   . ILE B 1 43 ? 24.485  -11.817 -30.150 1.00 30.27  ? 42  ILE B C   1 
ATOM   1052 O O   . ILE B 1 43 ? 24.800  -11.792 -28.972 1.00 31.83  ? 42  ILE B O   1 
ATOM   1053 C CB  . ILE B 1 43 ? 24.383  -14.214 -30.935 1.00 27.81  ? 42  ILE B CB  1 
ATOM   1054 C CG1 . ILE B 1 43 ? 25.088  -15.299 -31.773 1.00 30.98  ? 42  ILE B CG1 1 
ATOM   1055 C CG2 . ILE B 1 43 ? 22.911  -14.077 -31.336 1.00 29.98  ? 42  ILE B CG2 1 
ATOM   1056 C CD1 . ILE B 1 43 ? 25.244  -14.927 -33.236 1.00 27.43  ? 42  ILE B CD1 1 
ATOM   1057 N N   . PHE B 1 44 ? 23.601  -10.974 -30.707 1.00 29.67  ? 43  PHE B N   1 
ATOM   1058 C CA  . PHE B 1 44 ? 22.792  -10.028 -29.949 1.00 29.90  ? 43  PHE B CA  1 
ATOM   1059 C C   . PHE B 1 44 ? 21.332  -10.429 -30.123 1.00 27.36  ? 43  PHE B C   1 
ATOM   1060 O O   . PHE B 1 44 ? 20.835  -10.486 -31.246 1.00 27.41  ? 43  PHE B O   1 
ATOM   1061 C CB  . PHE B 1 44 ? 23.023  -8.550  -30.319 1.00 28.19  ? 43  PHE B CB  1 
ATOM   1062 C CG  . PHE B 1 44 ? 22.054  -7.543  -29.689 1.00 30.50  ? 43  PHE B CG  1 
ATOM   1063 C CD1 . PHE B 1 44 ? 20.894  -7.133  -30.363 1.00 28.35  ? 43  PHE B CD1 1 
ATOM   1064 C CD2 . PHE B 1 44 ? 22.310  -6.960  -28.452 1.00 34.23  ? 43  PHE B CD2 1 
ATOM   1065 C CE1 . PHE B 1 44 ? 20.020  -6.201  -29.801 1.00 31.25  ? 43  PHE B CE1 1 
ATOM   1066 C CE2 . PHE B 1 44 ? 21.437  -6.016  -27.885 1.00 28.02  ? 43  PHE B CE2 1 
ATOM   1067 C CZ  . PHE B 1 44 ? 20.286  -5.659  -28.557 1.00 33.01  ? 43  PHE B CZ  1 
ATOM   1068 N N   . PHE B 1 45 ? 20.648  -10.698 -28.993 1.00 27.50  ? 44  PHE B N   1 
ATOM   1069 C CA  . PHE B 1 45 ? 19.244  -11.072 -29.019 1.00 26.91  ? 44  PHE B CA  1 
ATOM   1070 C C   . PHE B 1 45 ? 18.378  -9.834  -28.897 1.00 27.52  ? 44  PHE B C   1 
ATOM   1071 O O   . PHE B 1 45 ? 18.465  -9.117  -27.905 1.00 29.32  ? 44  PHE B O   1 
ATOM   1072 C CB  . PHE B 1 45 ? 18.918  -12.028 -27.865 1.00 26.60  ? 44  PHE B CB  1 
ATOM   1073 C CG  . PHE B 1 45 ? 19.635  -13.366 -28.000 1.00 25.80  ? 44  PHE B CG  1 
ATOM   1074 C CD1 . PHE B 1 45 ? 20.873  -13.594 -27.401 1.00 29.05  ? 44  PHE B CD1 1 
ATOM   1075 C CD2 . PHE B 1 45 ? 19.053  -14.414 -28.719 1.00 29.41  ? 44  PHE B CD2 1 
ATOM   1076 C CE1 . PHE B 1 45 ? 21.540  -14.809 -27.575 1.00 31.98  ? 44  PHE B CE1 1 
ATOM   1077 C CE2 . PHE B 1 45 ? 19.708  -15.636 -28.866 1.00 30.44  ? 44  PHE B CE2 1 
ATOM   1078 C CZ  . PHE B 1 45 ? 20.958  -15.826 -28.322 1.00 28.55  ? 44  PHE B CZ  1 
ATOM   1079 N N   . PHE B 1 46 ? 17.486  -9.644  -29.882 1.00 25.48  ? 45  PHE B N   1 
ATOM   1080 C CA  . PHE B 1 46 ? 16.539  -8.557  -29.850 1.00 27.75  ? 45  PHE B CA  1 
ATOM   1081 C C   . PHE B 1 46 ? 15.537  -8.822  -28.720 1.00 31.07  ? 45  PHE B C   1 
ATOM   1082 O O   . PHE B 1 46 ? 15.285  -9.973  -28.343 1.00 25.49  ? 45  PHE B O   1 
ATOM   1083 C CB  . PHE B 1 46 ? 15.816  -8.421  -31.189 1.00 25.21  ? 45  PHE B CB  1 
ATOM   1084 C CG  . PHE B 1 46 ? 16.762  -7.928  -32.280 1.00 28.67  ? 45  PHE B CG  1 
ATOM   1085 C CD1 . PHE B 1 46 ? 17.147  -6.577  -32.333 1.00 28.84  ? 45  PHE B CD1 1 
ATOM   1086 C CD2 . PHE B 1 46 ? 17.176  -8.780  -33.305 1.00 25.92  ? 45  PHE B CD2 1 
ATOM   1087 C CE1 . PHE B 1 46 ? 17.989  -6.109  -33.355 1.00 31.09  ? 45  PHE B CE1 1 
ATOM   1088 C CE2 . PHE B 1 46 ? 18.026  -8.299  -34.312 1.00 27.88  ? 45  PHE B CE2 1 
ATOM   1089 C CZ  . PHE B 1 46 ? 18.413  -6.957  -34.331 1.00 27.40  ? 45  PHE B CZ  1 
ATOM   1090 N N   . GLY B 1 47 ? 14.983  -7.733  -28.189 1.00 30.08  ? 46  GLY B N   1 
ATOM   1091 C CA  . GLY B 1 47 ? 13.965  -7.833  -27.150 1.00 31.26  ? 46  GLY B CA  1 
ATOM   1092 C C   . GLY B 1 47 ? 14.627  -7.919  -25.776 1.00 33.37  ? 46  GLY B C   1 
ATOM   1093 O O   . GLY B 1 47 ? 14.496  -7.015  -24.970 1.00 34.56  ? 46  GLY B O   1 
ATOM   1094 N N   . THR B 1 48 ? 15.347  -9.008  -25.511 1.00 29.94  ? 47  THR B N   1 
ATOM   1095 C CA  . THR B 1 48 ? 16.031  -9.178  -24.240 1.00 30.68  ? 47  THR B CA  1 
ATOM   1096 C C   . THR B 1 48 ? 17.314  -8.359  -24.181 1.00 31.85  ? 47  THR B C   1 
ATOM   1097 O O   . THR B 1 48 ? 17.800  -8.065  -23.091 1.00 31.43  ? 47  THR B O   1 
ATOM   1098 C CB  . THR B 1 48 ? 16.351  -10.646 -23.947 1.00 31.34  ? 47  THR B CB  1 
ATOM   1099 O OG1 . THR B 1 48 ? 17.356  -11.099 -24.860 1.00 28.48  ? 47  THR B OG1 1 
ATOM   1100 C CG2 . THR B 1 48 ? 15.105  -11.514 -23.932 1.00 28.56  ? 47  THR B CG2 1 
ATOM   1101 N N   . HIS B 1 49 ? 17.908  -8.100  -25.349 1.00 30.16  ? 48  HIS B N   1 
ATOM   1102 C CA  . HIS B 1 49 ? 19.190  -7.424  -25.478 1.00 32.06  ? 48  HIS B CA  1 
ATOM   1103 C C   . HIS B 1 49 ? 20.299  -8.206  -24.797 1.00 33.54  ? 48  HIS B C   1 
ATOM   1104 O O   . HIS B 1 49 ? 21.286  -7.596  -24.407 1.00 38.07  ? 48  HIS B O   1 
ATOM   1105 C CB  . HIS B 1 49 ? 19.155  -5.946  -25.043 1.00 30.96  ? 48  HIS B CB  1 
ATOM   1106 C CG  . HIS B 1 49 ? 17.975  -5.245  -25.607 1.00 36.23  ? 48  HIS B CG  1 
ATOM   1107 N ND1 . HIS B 1 49 ? 17.216  -4.400  -24.836 1.00 40.44  ? 48  HIS B ND1 1 
ATOM   1108 C CD2 . HIS B 1 49 ? 17.373  -5.293  -26.827 1.00 33.06  ? 48  HIS B CD2 1 
ATOM   1109 C CE1 . HIS B 1 49 ? 16.191  -3.955  -25.563 1.00 44.40  ? 48  HIS B CE1 1 
ATOM   1110 N NE2 . HIS B 1 49 ? 16.267  -4.480  -26.773 1.00 36.75  ? 48  HIS B NE2 1 
ATOM   1111 N N   . GLU B 1 50 ? 20.170  -9.535  -24.719 1.00 29.65  ? 49  GLU B N   1 
ATOM   1112 C CA  . GLU B 1 50 ? 21.250  -10.378 -24.221 1.00 33.31  ? 49  GLU B CA  1 
ATOM   1113 C C   . GLU B 1 50 ? 22.257  -10.622 -25.347 1.00 33.67  ? 49  GLU B C   1 
ATOM   1114 O O   . GLU B 1 50 ? 21.943  -10.385 -26.516 1.00 31.14  ? 49  GLU B O   1 
ATOM   1115 C CB  . GLU B 1 50 ? 20.693  -11.735 -23.795 1.00 34.25  ? 49  GLU B CB  1 
ATOM   1116 C CG  . GLU B 1 50 ? 19.772  -11.584 -22.580 1.00 32.07  ? 49  GLU B CG  1 
ATOM   1117 C CD  . GLU B 1 50 ? 18.953  -12.826 -22.293 1.00 34.59  ? 49  GLU B CD  1 
ATOM   1118 O OE1 . GLU B 1 50 ? 18.150  -13.205 -23.173 1.00 34.36  ? 49  GLU B OE1 1 
ATOM   1119 O OE2 . GLU B 1 50 ? 19.130  -13.413 -21.197 1.00 35.86  ? 49  GLU B OE2 1 
ATOM   1120 N N   . THR B 1 51 ? 23.443  -11.114 -24.974 1.00 29.12  ? 50  THR B N   1 
ATOM   1121 C CA  . THR B 1 51 ? 24.481  -11.512 -25.920 1.00 32.14  ? 50  THR B CA  1 
ATOM   1122 C C   . THR B 1 51 ? 24.929  -12.932 -25.569 1.00 37.41  ? 50  THR B C   1 
ATOM   1123 O O   . THR B 1 51 ? 24.834  -13.369 -24.413 1.00 36.50  ? 50  THR B O   1 
ATOM   1124 C CB  . THR B 1 51 ? 25.638  -10.501 -25.985 1.00 33.55  ? 50  THR B CB  1 
ATOM   1125 O OG1 . THR B 1 51 ? 26.235  -10.481 -24.696 1.00 40.02  ? 50  THR B OG1 1 
ATOM   1126 C CG2 . THR B 1 51 ? 25.195  -9.062  -26.197 1.00 32.82  ? 50  THR B CG2 1 
ATOM   1127 N N   . ALA B 1 52 ? 25.369  -13.677 -26.592 1.00 34.62  ? 51  ALA B N   1 
ATOM   1128 C CA  . ALA B 1 52 ? 25.944  -14.996 -26.394 1.00 35.68  ? 51  ALA B CA  1 
ATOM   1129 C C   . ALA B 1 52 ? 26.899  -15.291 -27.544 1.00 31.33  ? 51  ALA B C   1 
ATOM   1130 O O   . ALA B 1 52 ? 26.950  -14.535 -28.505 1.00 33.52  ? 51  ALA B O   1 
ATOM   1131 C CB  . ALA B 1 52 ? 24.876  -16.068 -26.266 1.00 33.77  ? 51  ALA B CB  1 
ATOM   1132 N N   . PHE B 1 53 ? 27.629  -16.407 -27.430 1.00 31.70  ? 52  PHE B N   1 
ATOM   1133 C CA  . PHE B 1 53 ? 28.413  -16.904 -28.550 1.00 38.78  ? 52  PHE B CA  1 
ATOM   1134 C C   . PHE B 1 53 ? 27.730  -18.165 -29.077 1.00 38.77  ? 52  PHE B C   1 
ATOM   1135 O O   . PHE B 1 53 ? 27.483  -19.100 -28.310 1.00 39.82  ? 52  PHE B O   1 
ATOM   1136 C CB  . PHE B 1 53 ? 29.864  -17.175 -28.131 1.00 39.85  ? 52  PHE B CB  1 
ATOM   1137 C CG  . PHE B 1 53 ? 30.659  -15.925 -27.784 1.00 43.42  ? 52  PHE B CG  1 
ATOM   1138 C CD1 . PHE B 1 53 ? 30.844  -14.917 -28.723 1.00 44.81  ? 52  PHE B CD1 1 
ATOM   1139 C CD2 . PHE B 1 53 ? 31.192  -15.753 -26.511 1.00 47.31  ? 52  PHE B CD2 1 
ATOM   1140 C CE1 . PHE B 1 53 ? 31.545  -13.766 -28.396 1.00 41.80  ? 52  PHE B CE1 1 
ATOM   1141 C CE2 . PHE B 1 53 ? 31.904  -14.609 -26.182 1.00 47.58  ? 52  PHE B CE2 1 
ATOM   1142 C CZ  . PHE B 1 53 ? 32.073  -13.619 -27.120 1.00 45.24  ? 52  PHE B CZ  1 
ATOM   1143 N N   . LEU B 1 54 ? 27.392  -18.170 -30.381 1.00 35.51  ? 53  LEU B N   1 
ATOM   1144 C CA  . LEU B 1 54 ? 26.766  -19.340 -30.985 1.00 33.44  ? 53  LEU B CA  1 
ATOM   1145 C C   . LEU B 1 54 ? 27.489  -19.709 -32.285 1.00 35.29  ? 53  LEU B C   1 
ATOM   1146 O O   . LEU B 1 54 ? 28.025  -18.831 -32.969 1.00 34.03  ? 53  LEU B O   1 
ATOM   1147 C CB  . LEU B 1 54 ? 25.285  -19.082 -31.261 1.00 31.19  ? 53  LEU B CB  1 
ATOM   1148 C CG  . LEU B 1 54 ? 24.399  -18.854 -30.029 1.00 33.85  ? 53  LEU B CG  1 
ATOM   1149 C CD1 . LEU B 1 54 ? 22.995  -18.645 -30.558 1.00 29.79  ? 53  LEU B CD1 1 
ATOM   1150 C CD2 . LEU B 1 54 ? 24.493  -20.106 -29.135 1.00 32.38  ? 53  LEU B CD2 1 
ATOM   1151 N N   . GLY B 1 55 ? 27.477  -21.011 -32.606 1.00 32.51  ? 54  GLY B N   1 
ATOM   1152 C CA  . GLY B 1 55 ? 28.009  -21.525 -33.861 1.00 29.99  ? 54  GLY B CA  1 
ATOM   1153 C C   . GLY B 1 55 ? 26.912  -21.548 -34.933 1.00 31.50  ? 54  GLY B C   1 
ATOM   1154 O O   . GLY B 1 55 ? 25.717  -21.389 -34.624 1.00 31.87  ? 54  GLY B O   1 
ATOM   1155 N N   . PRO B 1 56 ? 27.275  -21.748 -36.219 1.00 30.35  ? 55  PRO B N   1 
ATOM   1156 C CA  . PRO B 1 56 ? 26.305  -21.780 -37.319 1.00 32.77  ? 55  PRO B CA  1 
ATOM   1157 C C   . PRO B 1 56 ? 25.108  -22.720 -37.219 1.00 30.74  ? 55  PRO B C   1 
ATOM   1158 O O   . PRO B 1 56 ? 24.060  -22.435 -37.781 1.00 29.16  ? 55  PRO B O   1 
ATOM   1159 C CB  . PRO B 1 56 ? 27.151  -22.055 -38.587 1.00 33.34  ? 55  PRO B CB  1 
ATOM   1160 C CG  . PRO B 1 56 ? 28.576  -21.856 -38.179 1.00 34.80  ? 55  PRO B CG  1 
ATOM   1161 C CD  . PRO B 1 56 ? 28.656  -21.942 -36.680 1.00 32.34  ? 55  PRO B CD  1 
ATOM   1162 N N   . LYS B 1 57 ? 25.274  -23.857 -36.528 1.00 35.61  ? 56  LYS B N   1 
ATOM   1163 C CA  . LYS B 1 57 ? 24.235  -24.869 -36.472 1.00 33.71  ? 56  LYS B CA  1 
ATOM   1164 C C   . LYS B 1 57 ? 22.994  -24.258 -35.821 1.00 31.98  ? 56  LYS B C   1 
ATOM   1165 O O   . LYS B 1 57 ? 21.881  -24.720 -36.055 1.00 29.79  ? 56  LYS B O   1 
ATOM   1166 C CB  . LYS B 1 57 ? 24.719  -26.125 -35.734 1.00 36.80  ? 56  LYS B CB  1 
ATOM   1167 C CG  . LYS B 1 57 ? 24.766  -26.035 -34.215 1.00 39.20  ? 56  LYS B CG  1 
ATOM   1168 C CD  . LYS B 1 57 ? 24.790  -27.436 -33.602 1.00 45.05  ? 56  LYS B CD  1 
ATOM   1169 C CE  . LYS B 1 57 ? 25.126  -27.507 -32.135 1.00 48.13  ? 56  LYS B CE  1 
ATOM   1170 N NZ  . LYS B 1 57 ? 24.195  -26.802 -31.251 1.00 50.42  ? 56  LYS B NZ  1 
ATOM   1171 N N   . ASP B 1 58 ? 23.200  -23.155 -35.088 1.00 31.47  ? 57  ASP B N   1 
ATOM   1172 C CA  . ASP B 1 58 ? 22.145  -22.556 -34.286 1.00 30.99  ? 57  ASP B CA  1 
ATOM   1173 C C   . ASP B 1 58 ? 21.706  -21.204 -34.850 1.00 30.12  ? 57  ASP B C   1 
ATOM   1174 O O   . ASP B 1 58 ? 20.936  -20.485 -34.189 1.00 30.06  ? 57  ASP B O   1 
ATOM   1175 C CB  . ASP B 1 58 ? 22.553  -22.464 -32.823 1.00 30.37  ? 57  ASP B CB  1 
ATOM   1176 C CG  . ASP B 1 58 ? 22.696  -23.787 -32.080 1.00 35.78  ? 57  ASP B CG  1 
ATOM   1177 O OD1 . ASP B 1 58 ? 21.765  -24.625 -32.179 1.00 36.88  ? 57  ASP B OD1 1 
ATOM   1178 O OD2 . ASP B 1 58 ? 23.706  -23.928 -31.357 1.00 40.68  ? 57  ASP B OD2 1 
ATOM   1179 N N   . LEU B 1 59 ? 22.169  -20.882 -36.068 1.00 27.61  ? 58  LEU B N   1 
ATOM   1180 C CA  . LEU B 1 59 ? 21.863  -19.589 -36.670 1.00 27.27  ? 58  LEU B CA  1 
ATOM   1181 C C   . LEU B 1 59 ? 21.108  -19.773 -37.975 1.00 26.93  ? 58  LEU B C   1 
ATOM   1182 O O   . LEU B 1 59 ? 21.614  -20.392 -38.907 1.00 29.02  ? 58  LEU B O   1 
ATOM   1183 C CB  . LEU B 1 59 ? 23.147  -18.790 -36.883 1.00 28.98  ? 58  LEU B CB  1 
ATOM   1184 C CG  . LEU B 1 59 ? 23.991  -18.599 -35.617 1.00 27.57  ? 58  LEU B CG  1 
ATOM   1185 C CD1 . LEU B 1 59 ? 25.275  -17.897 -35.978 1.00 32.98  ? 58  LEU B CD1 1 
ATOM   1186 C CD2 . LEU B 1 59 ? 23.221  -17.750 -34.606 1.00 29.61  ? 58  LEU B CD2 1 
ATOM   1187 N N   . PHE B 1 60 ? 19.915  -19.188 -38.030 1.00 26.56  ? 59  PHE B N   1 
ATOM   1188 C CA  . PHE B 1 60 ? 19.011  -19.363 -39.157 1.00 25.48  ? 59  PHE B CA  1 
ATOM   1189 C C   . PHE B 1 60 ? 18.889  -17.995 -39.823 1.00 29.46  ? 59  PHE B C   1 
ATOM   1190 O O   . PHE B 1 60 ? 18.283  -17.095 -39.259 1.00 28.73  ? 59  PHE B O   1 
ATOM   1191 C CB  . PHE B 1 60 ? 17.679  -19.901 -38.597 1.00 26.28  ? 59  PHE B CB  1 
ATOM   1192 C CG  . PHE B 1 60 ? 17.795  -21.314 -38.022 1.00 25.97  ? 59  PHE B CG  1 
ATOM   1193 C CD1 . PHE B 1 60 ? 18.318  -21.515 -36.747 1.00 30.35  ? 59  PHE B CD1 1 
ATOM   1194 C CD2 . PHE B 1 60 ? 17.446  -22.423 -38.781 1.00 29.31  ? 59  PHE B CD2 1 
ATOM   1195 C CE1 . PHE B 1 60 ? 18.477  -22.795 -36.223 1.00 32.28  ? 59  PHE B CE1 1 
ATOM   1196 C CE2 . PHE B 1 60 ? 17.603  -23.701 -38.269 1.00 31.48  ? 59  PHE B CE2 1 
ATOM   1197 C CZ  . PHE B 1 60 ? 18.134  -23.885 -36.995 1.00 32.53  ? 59  PHE B CZ  1 
ATOM   1198 N N   . PRO B 1 61 ? 19.425  -17.780 -41.055 1.00 34.83  ? 60  PRO B N   1 
ATOM   1199 C CA  . PRO B 1 61 ? 19.168  -16.519 -41.769 1.00 33.60  ? 60  PRO B CA  1 
ATOM   1200 C C   . PRO B 1 61 ? 17.714  -16.045 -41.699 1.00 32.54  ? 60  PRO B C   1 
ATOM   1201 O O   . PRO B 1 61 ? 16.795  -16.814 -41.936 1.00 31.58  ? 60  PRO B O   1 
ATOM   1202 C CB  . PRO B 1 61 ? 19.668  -16.776 -43.213 1.00 32.63  ? 60  PRO B CB  1 
ATOM   1203 C CG  . PRO B 1 61 ? 20.719  -17.852 -43.048 1.00 38.77  ? 60  PRO B CG  1 
ATOM   1204 C CD  . PRO B 1 61 ? 20.282  -18.714 -41.814 1.00 36.27  ? 60  PRO B CD  1 
ATOM   1205 N N   . TYR B 1 62 ? 17.496  -14.737 -41.422 1.00 29.00  ? 61  TYR B N   1 
ATOM   1206 C CA  . TYR B 1 62 ? 16.190  -14.244 -41.027 1.00 33.19  ? 61  TYR B CA  1 
ATOM   1207 C C   . TYR B 1 62 ? 15.181  -14.297 -42.166 1.00 34.80  ? 61  TYR B C   1 
ATOM   1208 O O   . TYR B 1 62 ? 14.037  -14.687 -41.951 1.00 32.20  ? 61  TYR B O   1 
ATOM   1209 C CB  . TYR B 1 62 ? 16.341  -12.784 -40.579 1.00 33.47  ? 61  TYR B CB  1 
ATOM   1210 C CG  . TYR B 1 62 ? 15.022  -12.090 -40.297 1.00 36.70  ? 61  TYR B CG  1 
ATOM   1211 C CD1 . TYR B 1 62 ? 14.284  -12.391 -39.159 1.00 36.23  ? 61  TYR B CD1 1 
ATOM   1212 C CD2 . TYR B 1 62 ? 14.558  -11.080 -41.137 1.00 44.59  ? 61  TYR B CD2 1 
ATOM   1213 C CE1 . TYR B 1 62 ? 13.095  -11.729 -38.887 1.00 39.46  ? 61  TYR B CE1 1 
ATOM   1214 C CE2 . TYR B 1 62 ? 13.370  -10.418 -40.881 1.00 43.46  ? 61  TYR B CE2 1 
ATOM   1215 C CZ  . TYR B 1 62 ? 12.635  -10.751 -39.755 1.00 43.49  ? 61  TYR B CZ  1 
ATOM   1216 O OH  . TYR B 1 62 ? 11.460  -10.097 -39.523 1.00 47.97  ? 61  TYR B OH  1 
ATOM   1217 N N   . ASP B 1 63 ? 15.614  -13.891 -43.368 1.00 42.66  ? 62  ASP B N   1 
ATOM   1218 C CA  . ASP B 1 63 ? 14.719  -13.802 -44.518 1.00 47.23  ? 62  ASP B CA  1 
ATOM   1219 C C   . ASP B 1 63 ? 14.124  -15.163 -44.860 1.00 38.93  ? 62  ASP B C   1 
ATOM   1220 O O   . ASP B 1 63 ? 12.912  -15.274 -45.018 1.00 44.95  ? 62  ASP B O   1 
ATOM   1221 C CB  . ASP B 1 63 ? 15.408  -13.223 -45.740 1.00 52.05  ? 62  ASP B CB  1 
ATOM   1222 C CG  . ASP B 1 63 ? 15.072  -11.766 -46.012 1.00 69.32  ? 62  ASP B CG  1 
ATOM   1223 O OD1 . ASP B 1 63 ? 14.517  -11.105 -45.095 1.00 70.09  ? 62  ASP B OD1 1 
ATOM   1224 O OD2 . ASP B 1 63 ? 15.325  -11.322 -47.154 1.00 73.96  ? 62  ASP B OD2 1 
ATOM   1225 N N   . LYS B 1 64 ? 14.988  -16.173 -44.957 1.00 43.01  ? 63  LYS B N   1 
ATOM   1226 C CA  . LYS B 1 64 ? 14.594  -17.542 -45.248 1.00 43.05  ? 63  LYS B CA  1 
ATOM   1227 C C   . LYS B 1 64 ? 13.635  -18.077 -44.186 1.00 41.67  ? 63  LYS B C   1 
ATOM   1228 O O   . LYS B 1 64 ? 12.730  -18.848 -44.493 1.00 44.08  ? 63  LYS B O   1 
ATOM   1229 C CB  . LYS B 1 64 ? 15.826  -18.447 -45.219 1.00 45.33  ? 63  LYS B CB  1 
ATOM   1230 C CG  . LYS B 1 64 ? 15.553  -19.881 -45.638 1.00 43.11  ? 63  LYS B CG  1 
ATOM   1231 C CD  . LYS B 1 64 ? 16.828  -20.703 -45.769 1.00 49.31  ? 63  LYS B CD  1 
ATOM   1232 C CE  . LYS B 1 64 ? 16.651  -22.020 -46.496 1.00 48.15  ? 63  LYS B CE  1 
ATOM   1233 N NZ  . LYS B 1 64 ? 15.527  -22.848 -46.064 1.00 42.62  ? 63  LYS B NZ  1 
ATOM   1234 N N   . SER B 1 65 ? 13.846  -17.706 -42.924 1.00 40.55  ? 64  SER B N   1 
ATOM   1235 C CA  . SER B 1 65 ? 13.205  -18.489 -41.869 1.00 37.94  ? 64  SER B CA  1 
ATOM   1236 C C   . SER B 1 65 ? 12.103  -17.723 -41.135 1.00 36.85  ? 64  SER B C   1 
ATOM   1237 O O   . SER B 1 65 ? 11.436  -18.303 -40.281 1.00 37.84  ? 64  SER B O   1 
ATOM   1238 C CB  . SER B 1 65 ? 14.252  -19.017 -40.934 1.00 37.91  ? 64  SER B CB  1 
ATOM   1239 O OG  . SER B 1 65 ? 14.929  -17.911 -40.360 1.00 48.30  ? 64  SER B OG  1 
ATOM   1240 N N   . LYS B 1 66 ? 11.862  -16.447 -41.498 1.00 39.41  ? 65  LYS B N   1 
ATOM   1241 C CA  . LYS B 1 66 ? 10.943  -15.588 -40.757 1.00 39.60  ? 65  LYS B CA  1 
ATOM   1242 C C   . LYS B 1 66 ? 9.504   -16.112 -40.726 1.00 42.62  ? 65  LYS B C   1 
ATOM   1243 O O   . LYS B 1 66 ? 8.797   -15.933 -39.740 1.00 43.76  ? 65  LYS B O   1 
ATOM   1244 C CB  . LYS B 1 66 ? 10.966  -14.097 -41.133 1.00 37.85  ? 65  LYS B CB  1 
ATOM   1245 C CG  . LYS B 1 66 ? 10.481  -13.709 -42.531 1.00 42.94  ? 65  LYS B CG  1 
ATOM   1246 N N   . ASP B 1 67 ? 9.025   -16.750 -41.788 1.00 43.45  ? 66  ASP B N   1 
ATOM   1247 C CA  . ASP B 1 67 ? 7.623   -17.114 -41.716 1.00 47.89  ? 66  ASP B CA  1 
ATOM   1248 C C   . ASP B 1 67 ? 7.460   -18.345 -40.821 1.00 50.77  ? 66  ASP B C   1 
ATOM   1249 O O   . ASP B 1 67 ? 6.387   -18.576 -40.251 1.00 52.54  ? 66  ASP B O   1 
ATOM   1250 C CB  . ASP B 1 67 ? 6.945   -17.064 -43.075 1.00 60.37  ? 66  ASP B CB  1 
ATOM   1251 C CG  . ASP B 1 67 ? 7.567   -17.944 -44.143 1.00 68.41  ? 66  ASP B CG  1 
ATOM   1252 O OD1 . ASP B 1 67 ? 7.840   -17.417 -45.249 1.00 76.20  ? 66  ASP B OD1 1 
ATOM   1253 O OD2 . ASP B 1 67 ? 7.767   -19.145 -43.852 1.00 76.24  ? 66  ASP B OD2 1 
ATOM   1254 N N   . LYS B 1 68 ? 8.553   -19.098 -40.647 1.00 42.54  ? 67  LYS B N   1 
ATOM   1255 C CA  . LYS B 1 68 ? 8.503   -20.261 -39.773 1.00 37.67  ? 67  LYS B CA  1 
ATOM   1256 C C   . LYS B 1 68 ? 8.696   -19.846 -38.314 1.00 35.40  ? 67  LYS B C   1 
ATOM   1257 O O   . LYS B 1 68 ? 7.944   -20.277 -37.431 1.00 37.00  ? 67  LYS B O   1 
ATOM   1258 C CB  . LYS B 1 68 ? 9.537   -21.275 -40.250 1.00 40.65  ? 67  LYS B CB  1 
ATOM   1259 C CG  . LYS B 1 68 ? 9.551   -22.546 -39.434 1.00 47.63  ? 67  LYS B CG  1 
ATOM   1260 C CD  . LYS B 1 68 ? 10.487  -23.483 -40.186 1.00 57.75  ? 67  LYS B CD  1 
ATOM   1261 C CE  . LYS B 1 68 ? 10.988  -24.619 -39.355 1.00 64.30  ? 67  LYS B CE  1 
ATOM   1262 N NZ  . LYS B 1 68 ? 9.983   -25.655 -39.125 1.00 60.56  ? 67  LYS B NZ  1 
ATOM   1263 N N   . TYR B 1 69 ? 9.692   -18.987 -38.057 1.00 33.24  ? 68  TYR B N   1 
ATOM   1264 C CA  . TYR B 1 69 ? 10.103  -18.750 -36.671 1.00 29.22  ? 68  TYR B CA  1 
ATOM   1265 C C   . TYR B 1 69 ? 9.566   -17.430 -36.121 1.00 34.28  ? 68  TYR B C   1 
ATOM   1266 O O   . TYR B 1 69 ? 9.715   -17.157 -34.924 1.00 32.74  ? 68  TYR B O   1 
ATOM   1267 C CB  . TYR B 1 69 ? 11.625  -18.808 -36.524 1.00 29.35  ? 68  TYR B CB  1 
ATOM   1268 C CG  . TYR B 1 69 ? 12.211  -20.181 -36.829 1.00 31.65  ? 68  TYR B CG  1 
ATOM   1269 C CD1 . TYR B 1 69 ? 11.682  -21.337 -36.263 1.00 32.49  ? 68  TYR B CD1 1 
ATOM   1270 C CD2 . TYR B 1 69 ? 13.322  -20.308 -37.668 1.00 34.13  ? 68  TYR B CD2 1 
ATOM   1271 C CE1 . TYR B 1 69 ? 12.225  -22.588 -36.528 1.00 33.76  ? 68  TYR B CE1 1 
ATOM   1272 C CE2 . TYR B 1 69 ? 13.858  -21.547 -37.961 1.00 34.40  ? 68  TYR B CE2 1 
ATOM   1273 C CZ  . TYR B 1 69 ? 13.311  -22.683 -37.384 1.00 35.38  ? 68  TYR B CZ  1 
ATOM   1274 O OH  . TYR B 1 69 ? 13.865  -23.882 -37.672 1.00 32.26  ? 68  TYR B OH  1 
ATOM   1275 N N   . GLY B 1 70 ? 8.979   -16.605 -36.994 1.00 33.19  ? 69  GLY B N   1 
ATOM   1276 C CA  . GLY B 1 70 ? 8.705   -15.227 -36.617 1.00 35.55  ? 69  GLY B CA  1 
ATOM   1277 C C   . GLY B 1 70 ? 7.267   -14.998 -36.145 1.00 39.99  ? 69  GLY B C   1 
ATOM   1278 O O   . GLY B 1 70 ? 6.712   -13.934 -36.412 1.00 41.57  ? 69  GLY B O   1 
ATOM   1279 N N   . LYS B 1 71 ? 6.673   -15.978 -35.452 1.00 41.34  ? 70  LYS B N   1 
ATOM   1280 C CA  . LYS B 1 71 ? 5.333   -15.821 -34.904 1.00 46.60  ? 70  LYS B CA  1 
ATOM   1281 C C   . LYS B 1 71 ? 5.436   -15.373 -33.454 1.00 47.92  ? 70  LYS B C   1 
ATOM   1282 O O   . LYS B 1 71 ? 6.299   -15.875 -32.735 1.00 46.50  ? 70  LYS B O   1 
ATOM   1283 C CB  . LYS B 1 71 ? 4.593   -17.158 -34.783 1.00 51.21  ? 70  LYS B CB  1 
ATOM   1284 C CG  . LYS B 1 71 ? 3.672   -17.552 -35.942 1.00 66.32  ? 70  LYS B CG  1 
ATOM   1285 C CD  . LYS B 1 71 ? 4.374   -17.878 -37.254 1.00 65.91  ? 70  LYS B CD  1 
ATOM   1286 C CE  . LYS B 1 71 ? 3.435   -18.236 -38.364 1.00 68.99  ? 70  LYS B CE  1 
ATOM   1287 N NZ  . LYS B 1 71 ? 4.017   -17.824 -39.647 1.00 70.16  ? 70  LYS B NZ  1 
ATOM   1288 N N   . PRO B 1 72 ? 4.551   -14.468 -32.964 1.00 44.44  ? 71  PRO B N   1 
ATOM   1289 C CA  . PRO B 1 72 ? 4.576   -14.073 -31.551 1.00 44.00  ? 71  PRO B CA  1 
ATOM   1290 C C   . PRO B 1 72 ? 4.352   -15.256 -30.616 1.00 46.06  ? 71  PRO B C   1 
ATOM   1291 O O   . PRO B 1 72 ? 3.696   -16.229 -30.995 1.00 38.65  ? 71  PRO B O   1 
ATOM   1292 C CB  . PRO B 1 72 ? 3.494   -12.995 -31.398 1.00 43.90  ? 71  PRO B CB  1 
ATOM   1293 C CG  . PRO B 1 72 ? 3.193   -12.578 -32.819 1.00 47.09  ? 71  PRO B CG  1 
ATOM   1294 C CD  . PRO B 1 72 ? 3.508   -13.766 -33.732 1.00 45.72  ? 71  PRO B CD  1 
ATOM   1295 N N   . ASN B 1 73 ? 4.931   -15.179 -29.406 1.00 38.51  ? 72  ASN B N   1 
ATOM   1296 C CA  . ASN B 1 73 ? 4.610   -16.162 -28.380 1.00 37.73  ? 72  ASN B CA  1 
ATOM   1297 C C   . ASN B 1 73 ? 4.586   -15.460 -27.012 1.00 40.13  ? 72  ASN B C   1 
ATOM   1298 O O   . ASN B 1 73 ? 4.670   -14.236 -26.943 1.00 39.54  ? 72  ASN B O   1 
ATOM   1299 C CB  . ASN B 1 73 ? 5.568   -17.348 -28.437 1.00 40.21  ? 72  ASN B CB  1 
ATOM   1300 C CG  . ASN B 1 73 ? 6.997   -16.912 -28.226 1.00 37.01  ? 72  ASN B CG  1 
ATOM   1301 O OD1 . ASN B 1 73 ? 7.265   -16.171 -27.276 1.00 36.23  ? 72  ASN B OD1 1 
ATOM   1302 N ND2 . ASN B 1 73 ? 7.919   -17.314 -29.100 1.00 35.42  ? 72  ASN B ND2 1 
ATOM   1303 N N   . LYS B 1 74 ? 4.535   -16.240 -25.929 1.00 38.36  ? 73  LYS B N   1 
ATOM   1304 C CA  . LYS B 1 74 ? 4.400   -15.705 -24.572 1.00 43.86  ? 73  LYS B CA  1 
ATOM   1305 C C   . LYS B 1 74 ? 5.742   -15.647 -23.816 1.00 43.50  ? 73  LYS B C   1 
ATOM   1306 O O   . LYS B 1 74 ? 5.764   -15.554 -22.578 1.00 38.17  ? 73  LYS B O   1 
ATOM   1307 C CB  . LYS B 1 74 ? 3.393   -16.591 -23.819 1.00 45.04  ? 73  LYS B CB  1 
ATOM   1308 N N   . ARG B 1 75 ? 6.874   -15.685 -24.536 1.00 33.07  ? 74  ARG B N   1 
ATOM   1309 C CA  . ARG B 1 75 ? 8.170   -15.577 -23.865 1.00 31.94  ? 74  ARG B CA  1 
ATOM   1310 C C   . ARG B 1 75 ? 8.536   -14.098 -23.717 1.00 33.22  ? 74  ARG B C   1 
ATOM   1311 O O   . ARG B 1 75 ? 8.399   -13.323 -24.661 1.00 37.02  ? 74  ARG B O   1 
ATOM   1312 C CB  . ARG B 1 75 ? 9.323   -16.305 -24.569 1.00 33.78  ? 74  ARG B CB  1 
ATOM   1313 C CG  . ARG B 1 75 ? 9.281   -17.809 -24.798 1.00 31.36  ? 74  ARG B CG  1 
ATOM   1314 C CD  . ARG B 1 75 ? 9.064   -18.561 -23.503 1.00 37.05  ? 74  ARG B CD  1 
ATOM   1315 N NE  . ARG B 1 75 ? 9.153   -19.998 -23.762 1.00 34.38  ? 74  ARG B NE  1 
ATOM   1316 C CZ  . ARG B 1 75 ? 10.195  -20.742 -23.505 1.00 34.07  ? 74  ARG B CZ  1 
ATOM   1317 N NH1 . ARG B 1 75 ? 11.303  -20.209 -23.008 1.00 40.11  ? 74  ARG B NH1 1 
ATOM   1318 N NH2 . ARG B 1 75 ? 10.162  -22.020 -23.813 1.00 36.13  ? 74  ARG B NH2 1 
ATOM   1319 N N   . LYS B 1 76 ? 9.032   -13.711 -22.526 1.00 32.46  ? 75  LYS B N   1 
ATOM   1320 C CA  . LYS B 1 76 ? 9.329   -12.319 -22.220 1.00 31.04  ? 75  LYS B CA  1 
ATOM   1321 C C   . LYS B 1 76 ? 10.441  -11.794 -23.140 1.00 27.13  ? 75  LYS B C   1 
ATOM   1322 O O   . LYS B 1 76 ? 11.528  -12.391 -23.208 1.00 29.80  ? 75  LYS B O   1 
ATOM   1323 C CB  . LYS B 1 76 ? 9.808   -12.203 -20.762 1.00 34.89  ? 75  LYS B CB  1 
ATOM   1324 C CG  . LYS B 1 76 ? 10.212  -10.767 -20.363 1.00 35.17  ? 75  LYS B CG  1 
ATOM   1325 C CD  . LYS B 1 76 ? 10.745  -10.696 -18.936 1.00 38.01  ? 75  LYS B CD  1 
ATOM   1326 C CE  . LYS B 1 76 ? 10.820  -9.307  -18.345 1.00 40.65  ? 75  LYS B CE  1 
ATOM   1327 N NZ  . LYS B 1 76 ? 11.258  -9.379  -16.939 1.00 49.38  ? 75  LYS B NZ  1 
ATOM   1328 N N   . GLY B 1 77 ? 10.146  -10.675 -23.811 1.00 28.91  ? 76  GLY B N   1 
ATOM   1329 C CA  . GLY B 1 77 ? 11.089  -10.037 -24.717 1.00 33.45  ? 76  GLY B CA  1 
ATOM   1330 C C   . GLY B 1 77 ? 10.914  -10.501 -26.170 1.00 32.66  ? 76  GLY B C   1 
ATOM   1331 O O   . GLY B 1 77 ? 11.409  -9.860  -27.076 1.00 31.18  ? 76  GLY B O   1 
ATOM   1332 N N   . PHE B 1 78 ? 10.247  -11.631 -26.406 1.00 29.88  ? 77  PHE B N   1 
ATOM   1333 C CA  . PHE B 1 78 ? 10.088  -12.122 -27.780 1.00 30.29  ? 77  PHE B CA  1 
ATOM   1334 C C   . PHE B 1 78 ? 9.329   -11.166 -28.704 1.00 30.56  ? 77  PHE B C   1 
ATOM   1335 O O   . PHE B 1 78 ? 9.754   -10.899 -29.830 1.00 27.18  ? 77  PHE B O   1 
ATOM   1336 C CB  . PHE B 1 78 ? 9.457   -13.516 -27.807 1.00 28.57  ? 77  PHE B CB  1 
ATOM   1337 C CG  . PHE B 1 78 ? 9.649   -14.211 -29.143 1.00 28.18  ? 77  PHE B CG  1 
ATOM   1338 C CD1 . PHE B 1 78 ? 10.755  -15.029 -29.352 1.00 28.25  ? 77  PHE B CD1 1 
ATOM   1339 C CD2 . PHE B 1 78 ? 8.701   -14.080 -30.162 1.00 30.81  ? 77  PHE B CD2 1 
ATOM   1340 C CE1 . PHE B 1 78 ? 10.945  -15.670 -30.570 1.00 28.99  ? 77  PHE B CE1 1 
ATOM   1341 C CE2 . PHE B 1 78 ? 8.895   -14.718 -31.385 1.00 33.50  ? 77  PHE B CE2 1 
ATOM   1342 C CZ  . PHE B 1 78 ? 10.017  -15.515 -31.577 1.00 31.77  ? 77  PHE B CZ  1 
ATOM   1343 N N   . ASN B 1 79 ? 8.160   -10.676 -28.306 1.00 30.52  ? 78  ASN B N   1 
ATOM   1344 C CA  . ASN B 1 79 ? 7.403   -9.858  -29.249 1.00 31.59  ? 78  ASN B CA  1 
ATOM   1345 C C   . ASN B 1 79 ? 8.092   -8.500  -29.427 1.00 33.21  ? 78  ASN B C   1 
ATOM   1346 O O   . ASN B 1 79 ? 8.082   -7.927  -30.522 1.00 34.74  ? 78  ASN B O   1 
ATOM   1347 C CB  . ASN B 1 79 ? 5.921   -9.724  -28.890 1.00 33.36  ? 78  ASN B CB  1 
ATOM   1348 C CG  . ASN B 1 79 ? 5.183   -11.046 -28.882 1.00 40.26  ? 78  ASN B CG  1 
ATOM   1349 O OD1 . ASN B 1 79 ? 5.673   -12.054 -29.412 1.00 37.92  ? 78  ASN B OD1 1 
ATOM   1350 N ND2 . ASN B 1 79 ? 4.013   -11.078 -28.253 1.00 40.50  ? 78  ASN B ND2 1 
ATOM   1351 N N   . GLU B 1 80 ? 8.756   -8.035  -28.376 1.00 30.59  ? 79  GLU B N   1 
ATOM   1352 C CA  . GLU B 1 80 ? 9.592   -6.844  -28.495 1.00 34.12  ? 79  GLU B CA  1 
ATOM   1353 C C   . GLU B 1 80 ? 10.733  -7.094  -29.486 1.00 29.59  ? 79  GLU B C   1 
ATOM   1354 O O   . GLU B 1 80 ? 11.066  -6.194  -30.244 1.00 30.76  ? 79  GLU B O   1 
ATOM   1355 C CB  . GLU B 1 80 ? 10.234  -6.298  -27.226 1.00 31.79  ? 79  GLU B CB  1 
ATOM   1356 C CG  . GLU B 1 80 ? 9.202   -5.816  -26.212 1.00 43.21  ? 79  GLU B CG  1 
ATOM   1357 N N   . GLY B 1 81 ? 11.296  -8.316  -29.469 1.00 30.67  ? 80  GLY B N   1 
ATOM   1358 C CA  . GLY B 1 81 ? 12.385  -8.708  -30.359 1.00 28.11  ? 80  GLY B CA  1 
ATOM   1359 C C   . GLY B 1 81 ? 11.903  -8.732  -31.804 1.00 29.21  ? 80  GLY B C   1 
ATOM   1360 O O   . GLY B 1 81 ? 12.642  -8.331  -32.714 1.00 30.31  ? 80  GLY B O   1 
ATOM   1361 N N   . LEU B 1 82 ? 10.656  -9.159  -32.006 1.00 27.22  ? 81  LEU B N   1 
ATOM   1362 C CA  . LEU B 1 82 ? 10.095  -9.217  -33.347 1.00 30.82  ? 81  LEU B CA  1 
ATOM   1363 C C   . LEU B 1 82 ? 9.967   -7.792  -33.877 1.00 31.46  ? 81  LEU B C   1 
ATOM   1364 O O   . LEU B 1 82 ? 10.224  -7.538  -35.049 1.00 31.09  ? 81  LEU B O   1 
ATOM   1365 C CB  . LEU B 1 82 ? 8.748   -9.955  -33.358 1.00 29.80  ? 81  LEU B CB  1 
ATOM   1366 C CG  . LEU B 1 82 ? 8.833   -11.480 -33.192 1.00 29.49  ? 81  LEU B CG  1 
ATOM   1367 C CD1 . LEU B 1 82 ? 7.449   -12.155 -33.274 1.00 30.26  ? 81  LEU B CD1 1 
ATOM   1368 C CD2 . LEU B 1 82 ? 9.831   -12.080 -34.188 1.00 27.60  ? 81  LEU B CD2 1 
ATOM   1369 N N   . TRP B 1 83 ? 9.564   -6.868  -33.006 1.00 29.27  ? 82  TRP B N   1 
ATOM   1370 C CA  . TRP B 1 83 ? 9.487   -5.459  -33.368 1.00 30.89  ? 82  TRP B CA  1 
ATOM   1371 C C   . TRP B 1 83 ? 10.844  -4.888  -33.785 1.00 30.50  ? 82  TRP B C   1 
ATOM   1372 O O   . TRP B 1 83 ? 10.926  -4.164  -34.792 1.00 33.50  ? 82  TRP B O   1 
ATOM   1373 C CB  . TRP B 1 83 ? 8.872   -4.626  -32.237 1.00 30.67  ? 82  TRP B CB  1 
ATOM   1374 C CG  . TRP B 1 83 ? 8.559   -3.229  -32.705 1.00 33.60  ? 82  TRP B CG  1 
ATOM   1375 C CD1 . TRP B 1 83 ? 7.403   -2.789  -33.278 1.00 36.67  ? 82  TRP B CD1 1 
ATOM   1376 C CD2 . TRP B 1 83 ? 9.471   -2.114  -32.724 1.00 34.53  ? 82  TRP B CD2 1 
ATOM   1377 N NE1 . TRP B 1 83 ? 7.527   -1.461  -33.626 1.00 41.61  ? 82  TRP B NE1 1 
ATOM   1378 C CE2 . TRP B 1 83 ? 8.785   -1.025  -33.304 1.00 36.45  ? 82  TRP B CE2 1 
ATOM   1379 C CE3 . TRP B 1 83 ? 10.796  -1.930  -32.297 1.00 37.22  ? 82  TRP B CE3 1 
ATOM   1380 C CZ2 . TRP B 1 83 ? 9.378   0.226   -33.457 1.00 40.24  ? 82  TRP B CZ2 1 
ATOM   1381 C CZ3 . TRP B 1 83 ? 11.379  -0.688  -32.450 1.00 37.92  ? 82  TRP B CZ3 1 
ATOM   1382 C CH2 . TRP B 1 83 ? 10.684  0.365   -33.038 1.00 41.57  ? 82  TRP B CH2 1 
ATOM   1383 N N   . GLU B 1 84 ? 11.887  -5.178  -32.994 1.00 27.94  ? 83  GLU B N   1 
ATOM   1384 C CA  . GLU B 1 84 ? 13.210  -4.613  -33.199 1.00 29.88  ? 83  GLU B CA  1 
ATOM   1385 C C   . GLU B 1 84 ? 13.813  -5.076  -34.524 1.00 29.31  ? 83  GLU B C   1 
ATOM   1386 O O   . GLU B 1 84 ? 14.349  -4.249  -35.275 1.00 31.23  ? 83  GLU B O   1 
ATOM   1387 C CB  . GLU B 1 84 ? 14.157  -4.868  -32.029 1.00 28.54  ? 83  GLU B CB  1 
ATOM   1388 C CG  . GLU B 1 84 ? 13.711  -4.147  -30.753 1.00 32.88  ? 83  GLU B CG  1 
ATOM   1389 C CD  . GLU B 1 84 ? 14.543  -4.530  -29.546 1.00 35.21  ? 83  GLU B CD  1 
ATOM   1390 O OE1 . GLU B 1 84 ? 15.415  -5.402  -29.712 1.00 34.06  ? 83  GLU B OE1 1 
ATOM   1391 O OE2 . GLU B 1 84 ? 14.352  -3.958  -28.438 1.00 34.85  ? 83  GLU B OE2 1 
ATOM   1392 N N   . ILE B 1 85 ? 13.758  -6.391  -34.786 1.00 28.87  ? 84  ILE B N   1 
ATOM   1393 C CA  . ILE B 1 85 ? 14.447  -6.942  -35.954 1.00 28.85  ? 84  ILE B CA  1 
ATOM   1394 C C   . ILE B 1 85 ? 13.789  -6.388  -37.223 1.00 28.08  ? 84  ILE B C   1 
ATOM   1395 O O   . ILE B 1 85 ? 14.432  -6.211  -38.260 1.00 25.51  ? 84  ILE B O   1 
ATOM   1396 C CB  . ILE B 1 85 ? 14.448  -8.482  -35.928 1.00 28.47  ? 84  ILE B CB  1 
ATOM   1397 C CG1 . ILE B 1 85 ? 15.487  -9.064  -36.926 1.00 30.86  ? 84  ILE B CG1 1 
ATOM   1398 C CG2 . ILE B 1 85 ? 13.041  -9.034  -36.169 1.00 29.14  ? 84  ILE B CG2 1 
ATOM   1399 C CD1 . ILE B 1 85 ? 15.917  -10.504 -36.657 1.00 28.53  ? 84  ILE B CD1 1 
ATOM   1400 N N   . GLN B 1 86 ? 12.495  -6.123  -37.121 1.00 27.74  ? 85  GLN B N   1 
ATOM   1401 C CA  . GLN B 1 86 ? 11.705  -5.590  -38.217 1.00 32.88  ? 85  GLN B CA  1 
ATOM   1402 C C   . GLN B 1 86 ? 11.881  -4.074  -38.363 1.00 36.11  ? 85  GLN B C   1 
ATOM   1403 O O   . GLN B 1 86 ? 11.962  -3.586  -39.487 1.00 35.06  ? 85  GLN B O   1 
ATOM   1404 C CB  . GLN B 1 86 ? 10.241  -5.974  -38.014 1.00 33.20  ? 85  GLN B CB  1 
ATOM   1405 N N   . ASN B 1 87 ? 11.963  -3.324  -37.254 1.00 30.54  ? 86  ASN B N   1 
ATOM   1406 C CA  . ASN B 1 87 ? 11.836  -1.865  -37.390 1.00 33.37  ? 86  ASN B CA  1 
ATOM   1407 C C   . ASN B 1 87 ? 13.149  -1.101  -37.219 1.00 33.33  ? 86  ASN B C   1 
ATOM   1408 O O   . ASN B 1 87 ? 13.268  0.040   -37.687 1.00 35.34  ? 86  ASN B O   1 
ATOM   1409 C CB  . ASN B 1 87 ? 10.739  -1.328  -36.462 1.00 37.05  ? 86  ASN B CB  1 
ATOM   1410 C CG  . ASN B 1 87 ? 9.388   -1.833  -36.913 1.00 40.13  ? 86  ASN B CG  1 
ATOM   1411 O OD1 . ASN B 1 87 ? 8.849   -1.313  -37.892 1.00 47.09  ? 86  ASN B OD1 1 
ATOM   1412 N ND2 . ASN B 1 87 ? 8.872   -2.901  -36.311 1.00 38.00  ? 86  ASN B ND2 1 
ATOM   1413 N N   . ASN B 1 88 ? 14.114  -1.673  -36.484 1.00 30.34  ? 87  ASN B N   1 
ATOM   1414 C CA  . ASN B 1 88 ? 15.368  -0.984  -36.217 1.00 35.08  ? 87  ASN B CA  1 
ATOM   1415 C C   . ASN B 1 88 ? 16.464  -1.977  -35.848 1.00 30.93  ? 87  ASN B C   1 
ATOM   1416 O O   . ASN B 1 88 ? 17.072  -1.884  -34.774 1.00 28.86  ? 87  ASN B O   1 
ATOM   1417 C CB  . ASN B 1 88 ? 15.231  0.125   -35.174 1.00 37.86  ? 87  ASN B CB  1 
ATOM   1418 C CG  . ASN B 1 88 ? 16.253  1.212   -35.404 1.00 36.76  ? 87  ASN B CG  1 
ATOM   1419 O OD1 . ASN B 1 88 ? 17.268  1.018   -36.096 1.00 34.35  ? 87  ASN B OD1 1 
ATOM   1420 N ND2 . ASN B 1 88 ? 15.985  2.389   -34.866 1.00 39.00  ? 87  ASN B ND2 1 
ATOM   1421 N N   . PRO B 1 89 ? 16.758  -2.946  -36.752 1.00 32.86  ? 88  PRO B N   1 
ATOM   1422 C CA  . PRO B 1 89 ? 17.686  -4.034  -36.448 1.00 29.64  ? 88  PRO B CA  1 
ATOM   1423 C C   . PRO B 1 89 ? 19.115  -3.603  -36.141 1.00 30.97  ? 88  PRO B C   1 
ATOM   1424 O O   . PRO B 1 89 ? 19.868  -4.382  -35.559 1.00 28.72  ? 88  PRO B O   1 
ATOM   1425 C CB  . PRO B 1 89 ? 17.649  -4.944  -37.702 1.00 27.12  ? 88  PRO B CB  1 
ATOM   1426 C CG  . PRO B 1 89 ? 17.127  -4.059  -38.831 1.00 29.38  ? 88  PRO B CG  1 
ATOM   1427 C CD  . PRO B 1 89 ? 16.226  -3.016  -38.132 1.00 29.39  ? 88  PRO B CD  1 
ATOM   1428 N N   . HIS B 1 90 ? 19.514  -2.386  -36.594 1.00 31.69  ? 89  HIS B N   1 
ATOM   1429 C CA  . HIS B 1 90 ? 20.917  -2.004  -36.533 1.00 28.27  ? 89  HIS B CA  1 
ATOM   1430 C C   . HIS B 1 90 ? 21.175  -0.907  -35.499 1.00 30.78  ? 89  HIS B C   1 
ATOM   1431 O O   . HIS B 1 90 ? 22.299  -0.389  -35.412 1.00 27.57  ? 89  HIS B O   1 
ATOM   1432 C CB  . HIS B 1 90 ? 21.452  -1.573  -37.917 1.00 26.87  ? 89  HIS B CB  1 
ATOM   1433 C CG  . HIS B 1 90 ? 21.254  -2.648  -38.932 1.00 30.51  ? 89  HIS B CG  1 
ATOM   1434 N ND1 . HIS B 1 90 ? 21.816  -3.902  -38.821 1.00 30.22  ? 89  HIS B ND1 1 
ATOM   1435 C CD2 . HIS B 1 90 ? 20.513  -2.666  -40.054 1.00 29.58  ? 89  HIS B CD2 1 
ATOM   1436 C CE1 . HIS B 1 90 ? 21.469  -4.629  -39.871 1.00 27.19  ? 89  HIS B CE1 1 
ATOM   1437 N NE2 . HIS B 1 90 ? 20.686  -3.891  -40.626 1.00 29.31  ? 89  HIS B NE2 1 
ATOM   1438 N N   . ALA B 1 91 ? 20.174  -0.654  -34.652 1.00 29.91  ? 90  ALA B N   1 
ATOM   1439 C CA  . ALA B 1 91 ? 20.264  0.379   -33.637 1.00 32.19  ? 90  ALA B CA  1 
ATOM   1440 C C   . ALA B 1 91 ? 21.231  -0.028  -32.526 1.00 34.91  ? 90  ALA B C   1 
ATOM   1441 O O   . ALA B 1 91 ? 21.491  -1.208  -32.301 1.00 29.34  ? 90  ALA B O   1 
ATOM   1442 C CB  . ALA B 1 91 ? 18.873  0.698   -33.092 1.00 29.47  ? 90  ALA B CB  1 
ATOM   1443 N N   . SER B 1 92 ? 21.724  0.974   -31.789 1.00 31.02  ? 91  SER B N   1 
ATOM   1444 C CA  . SER B 1 92 ? 22.367  0.766   -30.502 1.00 39.76  ? 91  SER B CA  1 
ATOM   1445 C C   . SER B 1 92 ? 21.302  0.512   -29.436 1.00 42.03  ? 91  SER B C   1 
ATOM   1446 O O   . SER B 1 92 ? 20.406  1.329   -29.262 1.00 43.48  ? 91  SER B O   1 
ATOM   1447 C CB  . SER B 1 92 ? 23.181  1.988   -30.116 1.00 41.60  ? 91  SER B CB  1 
ATOM   1448 O OG  . SER B 1 92 ? 23.721  1.780   -28.819 1.00 51.18  ? 91  SER B OG  1 
ATOM   1449 N N   . TYR B 1 93 ? 21.423  -0.619  -28.731 1.00 37.94  ? 92  TYR B N   1 
ATOM   1450 C CA  . TYR B 1 93 ? 20.534  -1.013  -27.650 1.00 44.64  ? 92  TYR B CA  1 
ATOM   1451 C C   . TYR B 1 93 ? 21.323  -0.971  -26.336 1.00 51.18  ? 92  TYR B C   1 
ATOM   1452 O O   . TYR B 1 93 ? 20.856  -1.464  -25.312 1.00 53.30  ? 92  TYR B O   1 
ATOM   1453 C CB  . TYR B 1 93 ? 19.853  -2.358  -27.955 1.00 39.44  ? 92  TYR B CB  1 
ATOM   1454 C CG  . TYR B 1 93 ? 18.833  -2.273  -29.083 1.00 32.82  ? 92  TYR B CG  1 
ATOM   1455 C CD1 . TYR B 1 93 ? 17.538  -1.839  -28.847 1.00 31.17  ? 92  TYR B CD1 1 
ATOM   1456 C CD2 . TYR B 1 93 ? 19.164  -2.617  -30.390 1.00 31.86  ? 92  TYR B CD2 1 
ATOM   1457 C CE1 . TYR B 1 93 ? 16.605  -1.716  -29.863 1.00 30.97  ? 92  TYR B CE1 1 
ATOM   1458 C CE2 . TYR B 1 93 ? 18.240  -2.485  -31.417 1.00 28.96  ? 92  TYR B CE2 1 
ATOM   1459 C CZ  . TYR B 1 93 ? 16.954  -2.055  -31.159 1.00 30.88  ? 92  TYR B CZ  1 
ATOM   1460 O OH  . TYR B 1 93 ? 16.019  -1.974  -32.170 1.00 29.77  ? 92  TYR B OH  1 
ATOM   1461 N N   . SER B 1 94 ? 22.494  -0.313  -26.391 1.00 66.76  ? 93  SER B N   1 
ATOM   1462 C CA  . SER B 1 94 ? 23.484  -0.202  -25.324 1.00 76.71  ? 93  SER B CA  1 
ATOM   1463 C C   . SER B 1 94 ? 22.848  0.311   -24.022 1.00 90.95  ? 93  SER B C   1 
ATOM   1464 O O   . SER B 1 94 ? 23.438  0.011   -22.952 1.00 94.85  ? 93  SER B O   1 
ATOM   1465 C CB  . SER B 1 94 ? 24.616  0.721   -25.723 1.00 75.94  ? 93  SER B CB  1 
ATOM   1466 O OG  . SER B 1 94 ? 25.302  0.288   -26.890 1.00 83.09  ? 93  SER B OG  1 
ATOM   1467 O OXT . SER B 1 94 ? 21.815  1.029   -24.119 1.00 87.48  ? 93  SER B OXT 1 
ATOM   1468 N N   . HIS C 1 4  ? 33.000  -23.341 26.549  1.00 87.90  ? 3   HIS C N   1 
ATOM   1469 C CA  . HIS C 1 4  ? 31.847  -22.514 27.003  1.00 89.04  ? 3   HIS C CA  1 
ATOM   1470 C C   . HIS C 1 4  ? 31.367  -23.035 28.358  1.00 88.07  ? 3   HIS C C   1 
ATOM   1471 O O   . HIS C 1 4  ? 32.131  -23.667 29.089  1.00 84.25  ? 3   HIS C O   1 
ATOM   1472 C CB  . HIS C 1 4  ? 30.749  -22.495 25.928  1.00 82.73  ? 3   HIS C CB  1 
ATOM   1473 N N   . ALA C 1 5  ? 30.106  -22.720 28.685  1.00 88.03  ? 4   ALA C N   1 
ATOM   1474 C CA  . ALA C 1 5  ? 29.339  -23.376 29.734  1.00 78.13  ? 4   ALA C CA  1 
ATOM   1475 C C   . ALA C 1 5  ? 27.850  -23.141 29.496  1.00 82.57  ? 4   ALA C C   1 
ATOM   1476 O O   . ALA C 1 5  ? 27.466  -22.172 28.836  1.00 80.16  ? 4   ALA C O   1 
ATOM   1477 C CB  . ALA C 1 5  ? 29.752  -22.865 31.080  1.00 85.38  ? 4   ALA C CB  1 
ATOM   1478 N N   . PHE C 1 6  ? 27.020  -24.032 30.053  1.00 70.69  ? 5   PHE C N   1 
ATOM   1479 C CA  . PHE C 1 6  ? 25.628  -24.106 29.652  1.00 61.08  ? 5   PHE C CA  1 
ATOM   1480 C C   . PHE C 1 6  ? 24.755  -24.233 30.895  1.00 70.20  ? 5   PHE C C   1 
ATOM   1481 O O   . PHE C 1 6  ? 24.802  -25.248 31.585  1.00 81.82  ? 5   PHE C O   1 
ATOM   1482 C CB  . PHE C 1 6  ? 25.433  -25.298 28.699  1.00 52.88  ? 5   PHE C CB  1 
ATOM   1483 C CG  . PHE C 1 6  ? 26.213  -25.281 27.385  1.00 48.61  ? 5   PHE C CG  1 
ATOM   1484 C CD1 . PHE C 1 6  ? 27.352  -26.061 27.207  1.00 51.89  ? 5   PHE C CD1 1 
ATOM   1485 C CD2 . PHE C 1 6  ? 25.809  -24.477 26.321  1.00 49.44  ? 5   PHE C CD2 1 
ATOM   1486 C CE1 . PHE C 1 6  ? 28.052  -26.054 25.997  1.00 57.36  ? 5   PHE C CE1 1 
ATOM   1487 C CE2 . PHE C 1 6  ? 26.505  -24.474 25.113  1.00 45.38  ? 5   PHE C CE2 1 
ATOM   1488 C CZ  . PHE C 1 6  ? 27.626  -25.255 24.948  1.00 51.22  ? 5   PHE C CZ  1 
ATOM   1489 N N   . LYS C 1 7  ? 23.964  -23.190 31.169  1.00 69.90  ? 6   LYS C N   1 
ATOM   1490 C CA  . LYS C 1 7  ? 22.947  -23.250 32.209  1.00 67.78  ? 6   LYS C CA  1 
ATOM   1491 C C   . LYS C 1 7  ? 21.669  -23.743 31.544  1.00 58.24  ? 6   LYS C C   1 
ATOM   1492 O O   . LYS C 1 7  ? 21.594  -23.756 30.316  1.00 64.00  ? 6   LYS C O   1 
ATOM   1493 C CB  . LYS C 1 7  ? 22.722  -21.891 32.889  1.00 66.86  ? 6   LYS C CB  1 
ATOM   1494 N N   . PRO C 1 8  ? 20.639  -24.188 32.301  1.00 60.27  ? 7   PRO C N   1 
ATOM   1495 C CA  . PRO C 1 8  ? 19.347  -24.512 31.690  1.00 59.60  ? 7   PRO C CA  1 
ATOM   1496 C C   . PRO C 1 8  ? 18.836  -23.319 30.884  1.00 65.37  ? 7   PRO C C   1 
ATOM   1497 O O   . PRO C 1 8  ? 19.231  -22.177 31.140  1.00 63.56  ? 7   PRO C O   1 
ATOM   1498 C CB  . PRO C 1 8  ? 18.471  -24.852 32.897  1.00 61.40  ? 7   PRO C CB  1 
ATOM   1499 C CG  . PRO C 1 8  ? 19.465  -25.382 33.911  1.00 59.55  ? 7   PRO C CG  1 
ATOM   1500 C CD  . PRO C 1 8  ? 20.672  -24.466 33.751  1.00 60.16  ? 7   PRO C CD  1 
ATOM   1501 N N   . GLY C 1 9  ? 18.007  -23.612 29.871  1.00 59.32  ? 8   GLY C N   1 
ATOM   1502 C CA  . GLY C 1 9  ? 17.352  -22.591 29.071  1.00 58.80  ? 8   GLY C CA  1 
ATOM   1503 C C   . GLY C 1 9  ? 18.143  -22.219 27.819  1.00 53.91  ? 8   GLY C C   1 
ATOM   1504 O O   . GLY C 1 9  ? 17.542  -21.860 26.810  1.00 60.13  ? 8   GLY C O   1 
ATOM   1505 N N   . ASP C 1 10 ? 19.479  -22.329 27.899  1.00 50.75  ? 9   ASP C N   1 
ATOM   1506 C CA  . ASP C 1 10 ? 20.401  -21.982 26.836  1.00 47.10  ? 9   ASP C CA  1 
ATOM   1507 C C   . ASP C 1 10 ? 20.033  -22.703 25.541  1.00 50.28  ? 9   ASP C C   1 
ATOM   1508 O O   . ASP C 1 10 ? 19.581  -23.843 25.564  1.00 45.43  ? 9   ASP C O   1 
ATOM   1509 C CB  . ASP C 1 10 ? 21.849  -22.260 27.210  1.00 54.44  ? 9   ASP C CB  1 
ATOM   1510 C CG  . ASP C 1 10 ? 22.461  -21.373 28.290  1.00 62.77  ? 9   ASP C CG  1 
ATOM   1511 O OD1 . ASP C 1 10 ? 21.709  -20.600 28.912  1.00 63.17  ? 9   ASP C OD1 1 
ATOM   1512 O OD2 . ASP C 1 10 ? 23.692  -21.461 28.503  1.00 65.35  ? 9   ASP C OD2 1 
ATOM   1513 N N   . LEU C 1 11 ? 20.241  -22.013 24.415  1.00 48.90  ? 10  LEU C N   1 
ATOM   1514 C CA  . LEU C 1 11 ? 19.857  -22.528 23.111  1.00 45.29  ? 10  LEU C CA  1 
ATOM   1515 C C   . LEU C 1 11 ? 21.091  -23.015 22.371  1.00 39.00  ? 10  LEU C C   1 
ATOM   1516 O O   . LEU C 1 11 ? 22.116  -22.340 22.347  1.00 41.68  ? 10  LEU C O   1 
ATOM   1517 C CB  . LEU C 1 11 ? 19.113  -21.461 22.312  1.00 45.69  ? 10  LEU C CB  1 
ATOM   1518 C CG  . LEU C 1 11 ? 17.830  -20.928 22.952  1.00 42.03  ? 10  LEU C CG  1 
ATOM   1519 C CD1 . LEU C 1 11 ? 17.173  -19.982 21.960  1.00 48.01  ? 10  LEU C CD1 1 
ATOM   1520 C CD2 . LEU C 1 11 ? 16.929  -22.081 23.315  1.00 41.75  ? 10  LEU C CD2 1 
ATOM   1521 N N   . VAL C 1 12 ? 20.982  -24.204 21.758  1.00 37.14  ? 11  VAL C N   1 
ATOM   1522 C CA  . VAL C 1 12 ? 22.148  -24.832 21.171  1.00 34.90  ? 11  VAL C CA  1 
ATOM   1523 C C   . VAL C 1 12 ? 21.741  -25.585 19.890  1.00 34.01  ? 11  VAL C C   1 
ATOM   1524 O O   . VAL C 1 12 ? 20.548  -25.736 19.613  1.00 33.95  ? 11  VAL C O   1 
ATOM   1525 C CB  . VAL C 1 12 ? 22.711  -25.797 22.235  1.00 40.33  ? 11  VAL C CB  1 
ATOM   1526 C CG1 . VAL C 1 12 ? 22.925  -25.117 23.591  1.00 36.94  ? 11  VAL C CG1 1 
ATOM   1527 C CG2 . VAL C 1 12 ? 21.827  -27.026 22.403  1.00 32.60  ? 11  VAL C CG2 1 
ATOM   1528 N N   . PHE C 1 13 ? 22.754  -25.989 19.107  1.00 30.81  ? 12  PHE C N   1 
ATOM   1529 C CA  . PHE C 1 13 ? 22.697  -27.170 18.257  1.00 32.21  ? 12  PHE C CA  1 
ATOM   1530 C C   . PHE C 1 13 ? 23.358  -28.335 18.992  1.00 33.94  ? 12  PHE C C   1 
ATOM   1531 O O   . PHE C 1 13 ? 24.447  -28.201 19.573  1.00 35.40  ? 12  PHE C O   1 
ATOM   1532 C CB  . PHE C 1 13 ? 23.336  -26.970 16.870  1.00 34.97  ? 12  PHE C CB  1 
ATOM   1533 C CG  . PHE C 1 13 ? 22.548  -25.958 16.053  1.00 37.93  ? 12  PHE C CG  1 
ATOM   1534 C CD1 . PHE C 1 13 ? 21.495  -26.365 15.236  1.00 35.21  ? 12  PHE C CD1 1 
ATOM   1535 C CD2 . PHE C 1 13 ? 22.838  -24.594 16.132  1.00 37.09  ? 12  PHE C CD2 1 
ATOM   1536 C CE1 . PHE C 1 13 ? 20.755  -25.437 14.510  1.00 36.96  ? 12  PHE C CE1 1 
ATOM   1537 C CE2 . PHE C 1 13 ? 22.090  -23.668 15.416  1.00 39.60  ? 12  PHE C CE2 1 
ATOM   1538 C CZ  . PHE C 1 13 ? 21.055  -24.092 14.599  1.00 39.19  ? 12  PHE C CZ  1 
ATOM   1539 N N   . ALA C 1 14 ? 22.667  -29.482 18.972  1.00 29.66  ? 13  ALA C N   1 
ATOM   1540 C CA  . ALA C 1 14 ? 23.124  -30.646 19.700  1.00 28.65  ? 13  ALA C CA  1 
ATOM   1541 C C   . ALA C 1 14 ? 23.378  -31.770 18.701  1.00 32.13  ? 13  ALA C C   1 
ATOM   1542 O O   . ALA C 1 14 ? 22.527  -32.039 17.855  1.00 26.85  ? 13  ALA C O   1 
ATOM   1543 C CB  . ALA C 1 14 ? 22.056  -31.028 20.691  1.00 24.78  ? 13  ALA C CB  1 
ATOM   1544 N N   . LYS C 1 15 ? 24.566  -32.380 18.780  1.00 32.73  ? 14  LYS C N   1 
ATOM   1545 C CA  . LYS C 1 15 ? 24.997  -33.363 17.797  1.00 33.19  ? 14  LYS C CA  1 
ATOM   1546 C C   . LYS C 1 15 ? 24.982  -34.743 18.435  1.00 31.73  ? 14  LYS C C   1 
ATOM   1547 O O   . LYS C 1 15 ? 25.719  -34.996 19.383  1.00 32.22  ? 14  LYS C O   1 
ATOM   1548 C CB  . LYS C 1 15 ? 26.411  -33.106 17.246  1.00 38.23  ? 14  LYS C CB  1 
ATOM   1549 C CG  . LYS C 1 15 ? 26.821  -34.094 16.129  1.00 38.24  ? 14  LYS C CG  1 
ATOM   1550 C CD  . LYS C 1 15 ? 25.931  -34.026 14.874  1.00 30.05  ? 14  LYS C CD  1 
ATOM   1551 C CE  . LYS C 1 15 ? 26.455  -34.927 13.747  1.00 31.15  ? 14  LYS C CE  1 
ATOM   1552 N NZ  . LYS C 1 15 ? 26.287  -36.349 14.106  1.00 29.04  ? 14  LYS C NZ  1 
ATOM   1553 N N   . MET C 1 16 ? 24.163  -35.636 17.874  1.00 29.37  ? 15  MET C N   1 
ATOM   1554 C CA  . MET C 1 16 ? 24.156  -37.052 18.223  1.00 30.50  ? 15  MET C CA  1 
ATOM   1555 C C   . MET C 1 16 ? 24.665  -37.862 17.035  1.00 35.03  ? 15  MET C C   1 
ATOM   1556 O O   . MET C 1 16 ? 24.473  -37.470 15.885  1.00 31.45  ? 15  MET C O   1 
ATOM   1557 C CB  . MET C 1 16 ? 22.741  -37.530 18.563  1.00 31.80  ? 15  MET C CB  1 
ATOM   1558 C CG  . MET C 1 16 ? 22.191  -36.950 19.846  1.00 37.13  ? 15  MET C CG  1 
ATOM   1559 S SD  . MET C 1 16 ? 20.563  -37.637 20.221  1.00 45.18  ? 15  MET C SD  1 
ATOM   1560 C CE  . MET C 1 16 ? 19.623  -37.028 18.812  1.00 41.82  ? 15  MET C CE  1 
ATOM   1561 N N   . LYS C 1 17 ? 25.322  -38.995 17.321  1.00 36.89  ? 16  LYS C N   1 
ATOM   1562 C CA  . LYS C 1 17 ? 25.726  -39.904 16.251  1.00 39.22  ? 16  LYS C CA  1 
ATOM   1563 C C   . LYS C 1 17 ? 24.464  -40.327 15.493  1.00 31.02  ? 16  LYS C C   1 
ATOM   1564 O O   . LYS C 1 17 ? 23.486  -40.780 16.087  1.00 33.61  ? 16  LYS C O   1 
ATOM   1565 C CB  . LYS C 1 17 ? 26.460  -41.122 16.846  1.00 37.64  ? 16  LYS C CB  1 
ATOM   1566 C CG  . LYS C 1 17 ? 27.109  -42.099 15.847  1.00 40.22  ? 16  LYS C CG  1 
ATOM   1567 C CD  . LYS C 1 17 ? 28.257  -41.402 15.131  1.00 43.00  ? 16  LYS C CD  1 
ATOM   1568 C CE  . LYS C 1 17 ? 29.097  -42.331 14.297  1.00 53.76  ? 16  LYS C CE  1 
ATOM   1569 N NZ  . LYS C 1 17 ? 30.270  -41.617 13.791  1.00 49.13  ? 16  LYS C NZ  1 
ATOM   1570 N N   . GLY C 1 18 ? 24.497  -40.203 14.169  1.00 35.10  ? 17  GLY C N   1 
ATOM   1571 C CA  . GLY C 1 18 ? 23.359  -40.665 13.389  1.00 31.78  ? 17  GLY C CA  1 
ATOM   1572 C C   . GLY C 1 18 ? 22.415  -39.537 12.964  1.00 35.55  ? 17  GLY C C   1 
ATOM   1573 O O   . GLY C 1 18 ? 21.398  -39.812 12.329  1.00 35.29  ? 17  GLY C O   1 
ATOM   1574 N N   . TYR C 1 19 ? 22.739  -38.285 13.332  1.00 35.75  ? 18  TYR C N   1 
ATOM   1575 C CA  . TYR C 1 19 ? 21.801  -37.174 13.181  1.00 33.23  ? 18  TYR C CA  1 
ATOM   1576 C C   . TYR C 1 19 ? 22.554  -35.890 12.871  1.00 30.61  ? 18  TYR C C   1 
ATOM   1577 O O   . TYR C 1 19 ? 23.666  -35.676 13.343  1.00 31.99  ? 18  TYR C O   1 
ATOM   1578 C CB  . TYR C 1 19 ? 20.976  -36.924 14.452  1.00 32.42  ? 18  TYR C CB  1 
ATOM   1579 C CG  . TYR C 1 19 ? 20.116  -38.111 14.832  1.00 34.46  ? 18  TYR C CG  1 
ATOM   1580 C CD1 . TYR C 1 19 ? 20.594  -39.129 15.660  1.00 33.53  ? 18  TYR C CD1 1 
ATOM   1581 C CD2 . TYR C 1 19 ? 18.822  -38.208 14.347  1.00 34.03  ? 18  TYR C CD2 1 
ATOM   1582 C CE1 . TYR C 1 19 ? 19.794  -40.213 15.978  1.00 34.17  ? 18  TYR C CE1 1 
ATOM   1583 C CE2 . TYR C 1 19 ? 18.009  -39.281 14.677  1.00 40.60  ? 18  TYR C CE2 1 
ATOM   1584 C CZ  . TYR C 1 19 ? 18.503  -40.291 15.481  1.00 42.98  ? 18  TYR C CZ  1 
ATOM   1585 O OH  . TYR C 1 19 ? 17.660  -41.327 15.775  1.00 44.51  ? 18  TYR C OH  1 
ATOM   1586 N N   . PRO C 1 20 ? 21.984  -34.982 12.057  1.00 30.96  ? 19  PRO C N   1 
ATOM   1587 C CA  . PRO C 1 20 ? 22.603  -33.668 11.856  1.00 30.96  ? 19  PRO C CA  1 
ATOM   1588 C C   . PRO C 1 20 ? 22.623  -32.838 13.147  1.00 32.06  ? 19  PRO C C   1 
ATOM   1589 O O   . PRO C 1 20 ? 21.872  -33.126 14.075  1.00 29.38  ? 19  PRO C O   1 
ATOM   1590 C CB  . PRO C 1 20 ? 21.686  -33.072 10.772  1.00 35.27  ? 19  PRO C CB  1 
ATOM   1591 C CG  . PRO C 1 20 ? 20.349  -33.677 11.068  1.00 32.54  ? 19  PRO C CG  1 
ATOM   1592 C CD  . PRO C 1 20 ? 20.672  -35.143 11.386  1.00 30.95  ? 19  PRO C CD  1 
ATOM   1593 N N   . HIS C 1 21 ? 23.469  -31.798 13.206  1.00 34.87  ? 20  HIS C N   1 
ATOM   1594 C CA  . HIS C 1 21 ? 23.394  -30.876 14.331  1.00 32.79  ? 20  HIS C CA  1 
ATOM   1595 C C   . HIS C 1 21 ? 21.950  -30.376 14.448  1.00 31.99  ? 20  HIS C C   1 
ATOM   1596 O O   . HIS C 1 21 ? 21.356  -29.979 13.445  1.00 32.64  ? 20  HIS C O   1 
ATOM   1597 C CB  . HIS C 1 21 ? 24.360  -29.704 14.156  1.00 33.28  ? 20  HIS C CB  1 
ATOM   1598 C CG  . HIS C 1 21 ? 25.792  -30.126 14.177  1.00 36.33  ? 20  HIS C CG  1 
ATOM   1599 N ND1 . HIS C 1 21 ? 26.436  -30.742 13.123  1.00 35.83  ? 20  HIS C ND1 1 
ATOM   1600 C CD2 . HIS C 1 21 ? 26.704  -30.024 15.175  1.00 41.39  ? 20  HIS C CD2 1 
ATOM   1601 C CE1 . HIS C 1 21 ? 27.699  -30.994 13.475  1.00 43.36  ? 20  HIS C CE1 1 
ATOM   1602 N NE2 . HIS C 1 21 ? 27.888  -30.551 14.717  1.00 39.63  ? 20  HIS C NE2 1 
ATOM   1603 N N   . TRP C 1 22 ? 21.381  -30.455 15.665  1.00 29.05  ? 21  TRP C N   1 
ATOM   1604 C CA  . TRP C 1 22 ? 19.933  -30.374 15.806  1.00 26.01  ? 21  TRP C CA  1 
ATOM   1605 C C   . TRP C 1 22 ? 19.604  -29.219 16.746  1.00 27.35  ? 21  TRP C C   1 
ATOM   1606 O O   . TRP C 1 22 ? 20.178  -29.134 17.841  1.00 26.82  ? 21  TRP C O   1 
ATOM   1607 C CB  . TRP C 1 22 ? 19.343  -31.693 16.345  1.00 29.99  ? 21  TRP C CB  1 
ATOM   1608 C CG  . TRP C 1 22 ? 17.884  -31.896 15.991  1.00 34.15  ? 21  TRP C CG  1 
ATOM   1609 C CD1 . TRP C 1 22 ? 16.778  -31.343 16.580  1.00 30.77  ? 21  TRP C CD1 1 
ATOM   1610 C CD2 . TRP C 1 22 ? 17.380  -32.774 14.956  1.00 31.93  ? 21  TRP C CD2 1 
ATOM   1611 N NE1 . TRP C 1 22 ? 15.630  -31.776 15.959  1.00 30.86  ? 21  TRP C NE1 1 
ATOM   1612 C CE2 . TRP C 1 22 ? 15.966  -32.671 14.976  1.00 31.63  ? 21  TRP C CE2 1 
ATOM   1613 C CE3 . TRP C 1 22 ? 17.985  -33.644 14.035  1.00 28.62  ? 21  TRP C CE3 1 
ATOM   1614 C CZ2 . TRP C 1 22 ? 15.166  -33.399 14.087  1.00 29.64  ? 21  TRP C CZ2 1 
ATOM   1615 C CZ3 . TRP C 1 22 ? 17.195  -34.340 13.139  1.00 31.79  ? 21  TRP C CZ3 1 
ATOM   1616 C CH2 . TRP C 1 22 ? 15.805  -34.250 13.202  1.00 28.18  ? 21  TRP C CH2 1 
ATOM   1617 N N   . PRO C 1 23 ? 18.631  -28.347 16.389  1.00 28.28  ? 22  PRO C N   1 
ATOM   1618 C CA  . PRO C 1 23 ? 18.213  -27.270 17.280  1.00 30.20  ? 22  PRO C CA  1 
ATOM   1619 C C   . PRO C 1 23 ? 17.582  -27.805 18.570  1.00 28.30  ? 22  PRO C C   1 
ATOM   1620 O O   . PRO C 1 23 ? 16.724  -28.680 18.554  1.00 31.06  ? 22  PRO C O   1 
ATOM   1621 C CB  . PRO C 1 23 ? 17.214  -26.491 16.390  1.00 32.05  ? 22  PRO C CB  1 
ATOM   1622 C CG  . PRO C 1 23 ? 16.649  -27.547 15.465  1.00 28.87  ? 22  PRO C CG  1 
ATOM   1623 C CD  . PRO C 1 23 ? 17.911  -28.327 15.091  1.00 27.36  ? 22  PRO C CD  1 
ATOM   1624 N N   . ALA C 1 24 ? 18.058  -27.277 19.699  1.00 32.52  ? 23  ALA C N   1 
ATOM   1625 C CA  . ALA C 1 24 ? 17.745  -27.841 21.003  1.00 34.17  ? 23  ALA C CA  1 
ATOM   1626 C C   . ALA C 1 24 ? 17.971  -26.793 22.093  1.00 35.04  ? 23  ALA C C   1 
ATOM   1627 O O   . ALA C 1 24 ? 18.510  -25.711 21.840  1.00 37.26  ? 23  ALA C O   1 
ATOM   1628 C CB  . ALA C 1 24 ? 18.610  -29.074 21.258  1.00 30.86  ? 23  ALA C CB  1 
ATOM   1629 N N   . ARG C 1 25 ? 17.559  -27.123 23.321  1.00 37.88  ? 24  ARG C N   1 
ATOM   1630 C CA  . ARG C 1 25 ? 17.972  -26.316 24.457  1.00 37.42  ? 24  ARG C CA  1 
ATOM   1631 C C   . ARG C 1 25 ? 18.419  -27.219 25.610  1.00 37.42  ? 24  ARG C C   1 
ATOM   1632 O O   . ARG C 1 25 ? 18.002  -28.379 25.694  1.00 36.73  ? 24  ARG C O   1 
ATOM   1633 C CB  . ARG C 1 25 ? 16.801  -25.448 24.920  1.00 39.31  ? 24  ARG C CB  1 
ATOM   1634 C CG  . ARG C 1 25 ? 15.516  -26.162 25.313  1.00 44.90  ? 24  ARG C CG  1 
ATOM   1635 C CD  . ARG C 1 25 ? 14.465  -25.227 25.938  1.00 46.48  ? 24  ARG C CD  1 
ATOM   1636 N NE  . ARG C 1 25 ? 13.301  -26.040 26.303  1.00 54.48  ? 24  ARG C NE  1 
ATOM   1637 C CZ  . ARG C 1 25 ? 12.021  -25.909 25.955  1.00 62.42  ? 24  ARG C CZ  1 
ATOM   1638 N NH1 . ARG C 1 25 ? 11.610  -24.864 25.257  1.00 60.84  ? 24  ARG C NH1 1 
ATOM   1639 N NH2 . ARG C 1 25 ? 11.144  -26.827 26.340  1.00 58.93  ? 24  ARG C NH2 1 
ATOM   1640 N N   . ILE C 1 26 ? 19.221  -26.631 26.504  1.00 38.30  ? 25  ILE C N   1 
ATOM   1641 C CA  . ILE C 1 26 ? 19.580  -27.217 27.789  1.00 42.35  ? 25  ILE C CA  1 
ATOM   1642 C C   . ILE C 1 26 ? 18.354  -27.223 28.696  1.00 48.74  ? 25  ILE C C   1 
ATOM   1643 O O   . ILE C 1 26 ? 17.766  -26.186 28.982  1.00 50.55  ? 25  ILE C O   1 
ATOM   1644 C CB  . ILE C 1 26 ? 20.751  -26.456 28.444  1.00 45.65  ? 25  ILE C CB  1 
ATOM   1645 C CG1 . ILE C 1 26 ? 21.866  -26.116 27.467  1.00 49.66  ? 25  ILE C CG1 1 
ATOM   1646 C CG2 . ILE C 1 26 ? 21.272  -27.178 29.692  1.00 45.32  ? 25  ILE C CG2 1 
ATOM   1647 C CD1 . ILE C 1 26 ? 22.708  -27.280 26.993  1.00 47.80  ? 25  ILE C CD1 1 
ATOM   1648 N N   . ASP C 1 27 ? 17.970  -28.413 29.144  1.00 51.12  ? 26  ASP C N   1 
ATOM   1649 C CA  . ASP C 1 27 ? 16.893  -28.558 30.105  1.00 57.22  ? 26  ASP C CA  1 
ATOM   1650 C C   . ASP C 1 27 ? 17.430  -28.395 31.522  1.00 60.27  ? 26  ASP C C   1 
ATOM   1651 O O   . ASP C 1 27 ? 18.633  -28.234 31.719  1.00 55.74  ? 26  ASP C O   1 
ATOM   1652 C CB  . ASP C 1 27 ? 16.226  -29.914 29.968  1.00 59.32  ? 26  ASP C CB  1 
ATOM   1653 C CG  . ASP C 1 27 ? 14.856  -29.872 29.323  1.00 66.11  ? 26  ASP C CG  1 
ATOM   1654 O OD1 . ASP C 1 27 ? 14.518  -28.796 28.771  1.00 68.82  ? 26  ASP C OD1 1 
ATOM   1655 O OD2 . ASP C 1 27 ? 14.125  -30.885 29.450  1.00 60.34  ? 26  ASP C OD2 1 
ATOM   1656 N N   . ASP C 1 28 ? 16.516  -28.422 32.499  1.00 71.25  ? 27  ASP C N   1 
ATOM   1657 C CA  . ASP C 1 28 ? 16.898  -28.539 33.896  1.00 77.78  ? 27  ASP C CA  1 
ATOM   1658 C C   . ASP C 1 28 ? 16.320  -29.843 34.427  1.00 77.94  ? 27  ASP C C   1 
ATOM   1659 O O   . ASP C 1 28 ? 15.149  -30.128 34.188  1.00 86.26  ? 27  ASP C O   1 
ATOM   1660 C CB  . ASP C 1 28 ? 16.479  -27.332 34.724  1.00 85.08  ? 27  ASP C CB  1 
ATOM   1661 C CG  . ASP C 1 28 ? 17.209  -27.148 36.051  1.00 86.24  ? 27  ASP C CG  1 
ATOM   1662 O OD1 . ASP C 1 28 ? 17.917  -28.088 36.485  1.00 80.47  ? 27  ASP C OD1 1 
ATOM   1663 O OD2 . ASP C 1 28 ? 17.094  -26.049 36.634  1.00 84.97  ? 27  ASP C OD2 1 
ATOM   1664 N N   . ILE C 1 29 ? 17.169  -30.610 35.129  1.00 81.56  ? 28  ILE C N   1 
ATOM   1665 C CA  . ILE C 1 29 ? 16.798  -31.858 35.778  1.00 74.89  ? 28  ILE C CA  1 
ATOM   1666 C C   . ILE C 1 29 ? 16.156  -31.534 37.123  1.00 73.89  ? 28  ILE C C   1 
ATOM   1667 O O   . ILE C 1 29 ? 16.657  -30.681 37.855  1.00 78.25  ? 28  ILE C O   1 
ATOM   1668 C CB  . ILE C 1 29 ? 18.026  -32.774 35.945  1.00 75.32  ? 28  ILE C CB  1 
ATOM   1669 N N   . ALA C 1 30 ? 15.039  -32.216 37.419  1.00 71.59  ? 29  ALA C N   1 
ATOM   1670 C CA  . ALA C 1 30 ? 14.330  -32.122 38.689  1.00 66.36  ? 29  ALA C CA  1 
ATOM   1671 C C   . ALA C 1 30 ? 15.183  -32.726 39.810  1.00 64.78  ? 29  ALA C C   1 
ATOM   1672 O O   . ALA C 1 30 ? 15.721  -33.845 39.580  1.00 52.13  ? 29  ALA C O   1 
ATOM   1673 C CB  . ALA C 1 30 ? 12.991  -32.826 38.576  1.00 61.29  ? 29  ALA C CB  1 
ATOM   1674 N N   . PRO C 1 36 ? 21.713  -37.495 35.669  1.00 46.74  ? 35  PRO C N   1 
ATOM   1675 C CA  . PRO C 1 36 ? 22.477  -37.498 34.428  1.00 51.02  ? 35  PRO C CA  1 
ATOM   1676 C C   . PRO C 1 36 ? 23.742  -38.339 34.596  1.00 58.94  ? 35  PRO C C   1 
ATOM   1677 O O   . PRO C 1 36 ? 24.288  -38.450 35.695  1.00 52.58  ? 35  PRO C O   1 
ATOM   1678 C CB  . PRO C 1 36 ? 22.797  -36.022 34.105  1.00 52.92  ? 35  PRO C CB  1 
ATOM   1679 C CG  . PRO C 1 36 ? 22.077  -35.214 35.157  1.00 51.23  ? 35  PRO C CG  1 
ATOM   1680 C CD  . PRO C 1 36 ? 21.672  -36.165 36.271  1.00 48.12  ? 35  PRO C CD  1 
ATOM   1681 N N   . PRO C 1 37 ? 24.263  -38.971 33.520  1.00 54.74  ? 36  PRO C N   1 
ATOM   1682 C CA  . PRO C 1 37 ? 25.595  -39.569 33.576  1.00 51.63  ? 36  PRO C CA  1 
ATOM   1683 C C   . PRO C 1 37 ? 26.578  -38.427 33.827  1.00 50.45  ? 36  PRO C C   1 
ATOM   1684 O O   . PRO C 1 37 ? 26.261  -37.254 33.582  1.00 44.21  ? 36  PRO C O   1 
ATOM   1685 C CB  . PRO C 1 37 ? 25.756  -40.225 32.191  1.00 47.86  ? 36  PRO C CB  1 
ATOM   1686 C CG  . PRO C 1 37 ? 24.321  -40.427 31.745  1.00 46.98  ? 36  PRO C CG  1 
ATOM   1687 C CD  . PRO C 1 37 ? 23.614  -39.162 32.215  1.00 51.69  ? 36  PRO C CD  1 
ATOM   1688 N N   . PRO C 1 38 ? 27.766  -38.738 34.395  1.00 45.70  ? 37  PRO C N   1 
ATOM   1689 C CA  . PRO C 1 38 ? 28.756  -37.718 34.728  1.00 45.67  ? 37  PRO C CA  1 
ATOM   1690 C C   . PRO C 1 38 ? 29.088  -36.812 33.553  1.00 41.58  ? 37  PRO C C   1 
ATOM   1691 O O   . PRO C 1 38 ? 29.387  -37.301 32.463  1.00 38.42  ? 37  PRO C O   1 
ATOM   1692 C CB  . PRO C 1 38 ? 29.970  -38.576 35.164  1.00 48.58  ? 37  PRO C CB  1 
ATOM   1693 C CG  . PRO C 1 38 ? 29.325  -39.815 35.746  1.00 44.02  ? 37  PRO C CG  1 
ATOM   1694 C CD  . PRO C 1 38 ? 28.181  -40.093 34.800  1.00 46.51  ? 37  PRO C CD  1 
ATOM   1695 N N   . ASN C 1 39 ? 29.020  -35.497 33.809  1.00 39.17  ? 38  ASN C N   1 
ATOM   1696 C CA  . ASN C 1 39 ? 29.433  -34.466 32.875  1.00 35.83  ? 38  ASN C CA  1 
ATOM   1697 C C   . ASN C 1 39 ? 28.528  -34.468 31.641  1.00 37.70  ? 38  ASN C C   1 
ATOM   1698 O O   . ASN C 1 39 ? 29.004  -34.136 30.556  1.00 43.49  ? 38  ASN C O   1 
ATOM   1699 C CB  . ASN C 1 39 ? 30.866  -34.681 32.379  1.00 36.97  ? 38  ASN C CB  1 
ATOM   1700 C CG  . ASN C 1 39 ? 31.488  -33.456 31.734  1.00 51.98  ? 38  ASN C CG  1 
ATOM   1701 O OD1 . ASN C 1 39 ? 31.014  -32.326 31.913  1.00 57.84  ? 38  ASN C OD1 1 
ATOM   1702 N ND2 . ASN C 1 39 ? 32.570  -33.644 30.984  1.00 54.60  ? 38  ASN C ND2 1 
ATOM   1703 N N   . LYS C 1 40 ? 27.249  -34.842 31.794  1.00 37.78  ? 39  LYS C N   1 
ATOM   1704 C CA  . LYS C 1 40 ? 26.313  -34.756 30.674  1.00 36.46  ? 39  LYS C CA  1 
ATOM   1705 C C   . LYS C 1 40 ? 25.189  -33.778 30.981  1.00 39.11  ? 39  LYS C C   1 
ATOM   1706 O O   . LYS C 1 40 ? 24.753  -33.679 32.120  1.00 38.62  ? 39  LYS C O   1 
ATOM   1707 C CB  . LYS C 1 40 ? 25.598  -36.085 30.411  1.00 34.49  ? 39  LYS C CB  1 
ATOM   1708 C CG  . LYS C 1 40 ? 26.489  -37.226 30.054  1.00 39.05  ? 39  LYS C CG  1 
ATOM   1709 C CD  . LYS C 1 40 ? 27.477  -36.926 28.940  1.00 45.68  ? 39  LYS C CD  1 
ATOM   1710 C CE  . LYS C 1 40 ? 28.047  -38.231 28.463  1.00 48.92  ? 39  LYS C CE  1 
ATOM   1711 N NZ  . LYS C 1 40 ? 29.294  -37.974 27.739  1.00 53.30  ? 39  LYS C NZ  1 
ATOM   1712 N N   . TYR C 1 41 ? 24.672  -33.113 29.940  1.00 37.91  ? 40  TYR C N   1 
ATOM   1713 C CA  . TYR C 1 41 ? 23.560  -32.179 30.107  1.00 37.61  ? 40  TYR C CA  1 
ATOM   1714 C C   . TYR C 1 41 ? 22.288  -32.824 29.588  1.00 37.84  ? 40  TYR C C   1 
ATOM   1715 O O   . TYR C 1 41 ? 22.338  -33.636 28.652  1.00 34.99  ? 40  TYR C O   1 
ATOM   1716 C CB  . TYR C 1 41 ? 23.648  -30.895 29.272  1.00 36.75  ? 40  TYR C CB  1 
ATOM   1717 C CG  . TYR C 1 41 ? 24.849  -30.048 29.643  1.00 39.13  ? 40  TYR C CG  1 
ATOM   1718 C CD1 . TYR C 1 41 ? 26.109  -30.338 29.132  1.00 38.38  ? 40  TYR C CD1 1 
ATOM   1719 C CD2 . TYR C 1 41 ? 24.713  -28.944 30.489  1.00 41.28  ? 40  TYR C CD2 1 
ATOM   1720 C CE1 . TYR C 1 41 ? 27.214  -29.577 29.473  1.00 46.49  ? 40  TYR C CE1 1 
ATOM   1721 C CE2 . TYR C 1 41 ? 25.814  -28.160 30.807  1.00 38.65  ? 40  TYR C CE2 1 
ATOM   1722 C CZ  . TYR C 1 41 ? 27.063  -28.488 30.317  1.00 46.31  ? 40  TYR C CZ  1 
ATOM   1723 O OH  . TYR C 1 41 ? 28.152  -27.734 30.645  1.00 60.57  ? 40  TYR C OH  1 
ATOM   1724 N N   . PRO C 1 42 ? 21.134  -32.482 30.207  1.00 36.12  ? 41  PRO C N   1 
ATOM   1725 C CA  . PRO C 1 42 ? 19.831  -32.956 29.735  1.00 36.24  ? 41  PRO C CA  1 
ATOM   1726 C C   . PRO C 1 42 ? 19.463  -32.022 28.593  1.00 35.65  ? 41  PRO C C   1 
ATOM   1727 O O   . PRO C 1 42 ? 19.477  -30.794 28.751  1.00 37.26  ? 41  PRO C O   1 
ATOM   1728 C CB  . PRO C 1 42 ? 18.911  -32.801 30.975  1.00 36.36  ? 41  PRO C CB  1 
ATOM   1729 C CG  . PRO C 1 42 ? 19.565  -31.729 31.800  1.00 41.57  ? 41  PRO C CG  1 
ATOM   1730 C CD  . PRO C 1 42 ? 21.040  -31.630 31.411  1.00 38.26  ? 41  PRO C CD  1 
ATOM   1731 N N   . ILE C 1 43 ? 19.179  -32.628 27.437  1.00 35.32  ? 42  ILE C N   1 
ATOM   1732 C CA  . ILE C 1 43 ? 18.927  -31.853 26.231  1.00 36.86  ? 42  ILE C CA  1 
ATOM   1733 C C   . ILE C 1 43 ? 17.494  -32.112 25.794  1.00 34.41  ? 42  ILE C C   1 
ATOM   1734 O O   . ILE C 1 43 ? 17.056  -33.268 25.769  1.00 34.43  ? 42  ILE C O   1 
ATOM   1735 C CB  . ILE C 1 43 ? 19.901  -32.268 25.110  1.00 37.39  ? 42  ILE C CB  1 
ATOM   1736 C CG1 . ILE C 1 43 ? 21.376  -32.019 25.507  1.00 33.40  ? 42  ILE C CG1 1 
ATOM   1737 C CG2 . ILE C 1 43 ? 19.520  -31.593 23.777  1.00 34.24  ? 42  ILE C CG2 1 
ATOM   1738 C CD1 . ILE C 1 43 ? 21.676  -30.571 25.880  1.00 36.96  ? 42  ILE C CD1 1 
ATOM   1739 N N   . PHE C 1 44 ? 16.801  -31.032 25.404  1.00 36.33  ? 43  PHE C N   1 
ATOM   1740 C CA  . PHE C 1 44 ? 15.508  -31.149 24.745  1.00 34.32  ? 43  PHE C CA  1 
ATOM   1741 C C   . PHE C 1 44 ? 15.682  -30.743 23.282  1.00 31.05  ? 43  PHE C C   1 
ATOM   1742 O O   . PHE C 1 44 ? 16.237  -29.677 23.008  1.00 34.63  ? 43  PHE C O   1 
ATOM   1743 C CB  . PHE C 1 44 ? 14.502  -30.199 25.415  1.00 34.79  ? 43  PHE C CB  1 
ATOM   1744 C CG  . PHE C 1 44 ? 13.126  -30.139 24.759  1.00 39.53  ? 43  PHE C CG  1 
ATOM   1745 C CD1 . PHE C 1 44 ? 12.182  -31.141 24.995  1.00 42.66  ? 43  PHE C CD1 1 
ATOM   1746 C CD2 . PHE C 1 44 ? 12.780  -29.082 23.907  1.00 39.55  ? 43  PHE C CD2 1 
ATOM   1747 C CE1 . PHE C 1 44 ? 10.923  -31.095 24.400  1.00 49.44  ? 43  PHE C CE1 1 
ATOM   1748 C CE2 . PHE C 1 44 ? 11.524  -29.041 23.307  1.00 43.20  ? 43  PHE C CE2 1 
ATOM   1749 C CZ  . PHE C 1 44 ? 10.598  -30.042 23.558  1.00 49.77  ? 43  PHE C CZ  1 
ATOM   1750 N N   . PHE C 1 45 ? 15.173  -31.588 22.381  1.00 31.64  ? 44  PHE C N   1 
ATOM   1751 C CA  . PHE C 1 45 ? 15.320  -31.385 20.947  1.00 35.65  ? 44  PHE C CA  1 
ATOM   1752 C C   . PHE C 1 45 ? 14.046  -30.736 20.415  1.00 34.65  ? 44  PHE C C   1 
ATOM   1753 O O   . PHE C 1 45 ? 12.965  -31.296 20.572  1.00 35.90  ? 44  PHE C O   1 
ATOM   1754 C CB  . PHE C 1 45 ? 15.623  -32.680 20.182  1.00 31.95  ? 44  PHE C CB  1 
ATOM   1755 C CG  . PHE C 1 45 ? 16.996  -33.270 20.480  1.00 34.12  ? 44  PHE C CG  1 
ATOM   1756 C CD1 . PHE C 1 45 ? 18.123  -32.861 19.776  1.00 31.32  ? 44  PHE C CD1 1 
ATOM   1757 C CD2 . PHE C 1 45 ? 17.160  -34.202 21.501  1.00 31.45  ? 44  PHE C CD2 1 
ATOM   1758 C CE1 . PHE C 1 45 ? 19.369  -33.409 20.061  1.00 32.70  ? 44  PHE C CE1 1 
ATOM   1759 C CE2 . PHE C 1 45 ? 18.406  -34.751 21.784  1.00 36.41  ? 44  PHE C CE2 1 
ATOM   1760 C CZ  . PHE C 1 45 ? 19.500  -34.358 21.065  1.00 33.11  ? 44  PHE C CZ  1 
ATOM   1761 N N   . PHE C 1 46 ? 14.190  -29.571 19.761  1.00 34.01  ? 45  PHE C N   1 
ATOM   1762 C CA  . PHE C 1 46 ? 13.049  -28.936 19.105  1.00 31.97  ? 45  PHE C CA  1 
ATOM   1763 C C   . PHE C 1 46 ? 12.593  -29.769 17.914  1.00 31.91  ? 45  PHE C C   1 
ATOM   1764 O O   . PHE C 1 46 ? 13.393  -30.482 17.301  1.00 35.24  ? 45  PHE C O   1 
ATOM   1765 C CB  . PHE C 1 46 ? 13.296  -27.472 18.692  1.00 29.58  ? 45  PHE C CB  1 
ATOM   1766 C CG  . PHE C 1 46 ? 13.644  -26.500 19.807  1.00 33.86  ? 45  PHE C CG  1 
ATOM   1767 C CD1 . PHE C 1 46 ? 12.655  -26.013 20.662  1.00 36.67  ? 45  PHE C CD1 1 
ATOM   1768 C CD2 . PHE C 1 46 ? 14.957  -26.057 19.983  1.00 30.52  ? 45  PHE C CD2 1 
ATOM   1769 C CE1 . PHE C 1 46 ? 12.991  -25.134 21.688  1.00 33.41  ? 45  PHE C CE1 1 
ATOM   1770 C CE2 . PHE C 1 46 ? 15.276  -25.165 20.998  1.00 32.41  ? 45  PHE C CE2 1 
ATOM   1771 C CZ  . PHE C 1 46 ? 14.297  -24.713 21.858  1.00 34.14  ? 45  PHE C CZ  1 
ATOM   1772 N N   . GLY C 1 47 ? 11.310  -29.626 17.548  1.00 31.65  ? 46  GLY C N   1 
ATOM   1773 C CA  . GLY C 1 47 ? 10.781  -30.350 16.409  1.00 37.09  ? 46  GLY C CA  1 
ATOM   1774 C C   . GLY C 1 47 ? 10.309  -31.740 16.823  1.00 44.50  ? 46  GLY C C   1 
ATOM   1775 O O   . GLY C 1 47 ? 9.114   -32.037 16.747  1.00 42.97  ? 46  GLY C O   1 
ATOM   1776 N N   . THR C 1 48 ? 11.254  -32.577 17.280  1.00 39.57  ? 47  THR C N   1 
ATOM   1777 C CA  . THR C 1 48 ? 10.914  -33.943 17.663  1.00 40.67  ? 47  THR C CA  1 
ATOM   1778 C C   . THR C 1 48 ? 10.399  -33.941 19.100  1.00 37.40  ? 47  THR C C   1 
ATOM   1779 O O   . THR C 1 48 ? 9.649   -34.832 19.492  1.00 41.87  ? 47  THR C O   1 
ATOM   1780 C CB  . THR C 1 48 ? 12.106  -34.886 17.553  1.00 36.26  ? 47  THR C CB  1 
ATOM   1781 O OG1 . THR C 1 48 ? 13.005  -34.404 18.561  1.00 35.92  ? 47  THR C OG1 1 
ATOM   1782 C CG2 . THR C 1 48 ? 12.694  -35.005 16.155  1.00 34.55  ? 47  THR C CG2 1 
ATOM   1783 N N   . HIS C 1 49 ? 10.832  -32.962 19.896  1.00 38.96  ? 48  HIS C N   1 
ATOM   1784 C CA  . HIS C 1 49 ? 10.417  -32.855 21.290  1.00 44.89  ? 48  HIS C CA  1 
ATOM   1785 C C   . HIS C 1 49 ? 10.944  -34.009 22.149  1.00 42.27  ? 48  HIS C C   1 
ATOM   1786 O O   . HIS C 1 49 ? 10.383  -34.269 23.209  1.00 45.98  ? 48  HIS C O   1 
ATOM   1787 C CB  . HIS C 1 49 ? 8.894   -32.689 21.421  1.00 47.17  ? 48  HIS C CB  1 
ATOM   1788 C CG  . HIS C 1 49 ? 8.358   -31.566 20.590  1.00 49.85  ? 48  HIS C CG  1 
ATOM   1789 N ND1 . HIS C 1 49 ? 7.335   -31.749 19.683  1.00 50.09  ? 48  HIS C ND1 1 
ATOM   1790 C CD2 . HIS C 1 49 ? 8.740   -30.284 20.473  1.00 46.25  ? 48  HIS C CD2 1 
ATOM   1791 C CE1 . HIS C 1 49 ? 7.095   -30.599 19.061  1.00 53.71  ? 48  HIS C CE1 1 
ATOM   1792 N NE2 . HIS C 1 49 ? 7.940   -29.698 19.527  1.00 52.48  ? 48  HIS C NE2 1 
ATOM   1793 N N   . GLU C 1 50 ? 12.058  -34.631 21.745  1.00 39.06  ? 49  GLU C N   1 
ATOM   1794 C CA  . GLU C 1 50 ? 12.623  -35.744 22.495  1.00 39.96  ? 49  GLU C CA  1 
ATOM   1795 C C   . GLU C 1 50 ? 13.756  -35.254 23.393  1.00 39.34  ? 49  GLU C C   1 
ATOM   1796 O O   . GLU C 1 50 ? 14.149  -34.100 23.311  1.00 39.13  ? 49  GLU C O   1 
ATOM   1797 C CB  . GLU C 1 50 ? 13.026  -36.842 21.525  1.00 42.97  ? 49  GLU C CB  1 
ATOM   1798 C CG  . GLU C 1 50 ? 11.839  -37.467 20.798  1.00 52.77  ? 49  GLU C CG  1 
ATOM   1799 C CD  . GLU C 1 50 ? 12.399  -38.365 19.713  1.00 60.42  ? 49  GLU C CD  1 
ATOM   1800 O OE1 . GLU C 1 50 ? 13.647  -38.543 19.648  1.00 57.80  ? 49  GLU C OE1 1 
ATOM   1801 O OE2 . GLU C 1 50 ? 11.576  -38.852 18.910  1.00 72.63  ? 49  GLU C OE2 1 
ATOM   1802 N N   . THR C 1 51 ? 14.210  -36.115 24.317  1.00 43.91  ? 50  THR C N   1 
ATOM   1803 C CA  . THR C 1 51 ? 15.254  -35.759 25.278  1.00 43.05  ? 50  THR C CA  1 
ATOM   1804 C C   . THR C 1 51 ? 16.409  -36.756 25.186  1.00 38.84  ? 50  THR C C   1 
ATOM   1805 O O   . THR C 1 51 ? 16.254  -37.870 24.686  1.00 37.22  ? 50  THR C O   1 
ATOM   1806 C CB  . THR C 1 51 ? 14.696  -35.737 26.701  1.00 43.55  ? 50  THR C CB  1 
ATOM   1807 O OG1 . THR C 1 51 ? 14.160  -37.057 26.805  1.00 43.86  ? 50  THR C OG1 1 
ATOM   1808 C CG2 . THR C 1 51 ? 13.709  -34.609 26.963  1.00 44.83  ? 50  THR C CG2 1 
ATOM   1809 N N   . ALA C 1 52 ? 17.574  -36.332 25.685  1.00 37.80  ? 51  ALA C N   1 
ATOM   1810 C CA  . ALA C 1 52 ? 18.773  -37.151 25.719  1.00 38.44  ? 51  ALA C CA  1 
ATOM   1811 C C   . ALA C 1 52 ? 19.790  -36.482 26.634  1.00 41.37  ? 51  ALA C C   1 
ATOM   1812 O O   . ALA C 1 52 ? 19.592  -35.341 27.038  1.00 43.10  ? 51  ALA C O   1 
ATOM   1813 C CB  . ALA C 1 52 ? 19.322  -37.352 24.318  1.00 37.04  ? 51  ALA C CB  1 
ATOM   1814 N N   . PHE C 1 53 ? 20.869  -37.208 26.967  1.00 38.64  ? 52  PHE C N   1 
ATOM   1815 C CA  . PHE C 1 53 ? 21.986  -36.640 27.709  1.00 40.63  ? 52  PHE C CA  1 
ATOM   1816 C C   . PHE C 1 53 ? 23.157  -36.528 26.752  1.00 36.95  ? 52  PHE C C   1 
ATOM   1817 O O   . PHE C 1 53 ? 23.485  -37.489 26.063  1.00 38.69  ? 52  PHE C O   1 
ATOM   1818 C CB  . PHE C 1 53 ? 22.418  -37.550 28.866  1.00 38.32  ? 52  PHE C CB  1 
ATOM   1819 C CG  . PHE C 1 53 ? 21.401  -37.554 29.995  1.00 41.08  ? 52  PHE C CG  1 
ATOM   1820 C CD1 . PHE C 1 53 ? 20.993  -36.360 30.582  1.00 39.98  ? 52  PHE C CD1 1 
ATOM   1821 C CD2 . PHE C 1 53 ? 20.824  -38.743 30.430  1.00 47.65  ? 52  PHE C CD2 1 
ATOM   1822 C CE1 . PHE C 1 53 ? 20.059  -36.351 31.614  1.00 44.72  ? 52  PHE C CE1 1 
ATOM   1823 C CE2 . PHE C 1 53 ? 19.891  -38.726 31.469  1.00 52.75  ? 52  PHE C CE2 1 
ATOM   1824 C CZ  . PHE C 1 53 ? 19.497  -37.527 32.045  1.00 44.66  ? 52  PHE C CZ  1 
ATOM   1825 N N   . LEU C 1 54 ? 23.785  -35.353 26.715  1.00 36.40  ? 53  LEU C N   1 
ATOM   1826 C CA  . LEU C 1 54 ? 24.922  -35.146 25.827  1.00 34.14  ? 53  LEU C CA  1 
ATOM   1827 C C   . LEU C 1 54 ? 26.005  -34.387 26.585  1.00 34.15  ? 53  LEU C C   1 
ATOM   1828 O O   . LEU C 1 54 ? 25.681  -33.609 27.464  1.00 33.63  ? 53  LEU C O   1 
ATOM   1829 C CB  . LEU C 1 54 ? 24.478  -34.352 24.598  1.00 36.78  ? 53  LEU C CB  1 
ATOM   1830 C CG  . LEU C 1 54 ? 23.538  -35.065 23.620  1.00 43.25  ? 53  LEU C CG  1 
ATOM   1831 C CD1 . LEU C 1 54 ? 23.195  -34.123 22.480  1.00 37.06  ? 53  LEU C CD1 1 
ATOM   1832 C CD2 . LEU C 1 54 ? 24.182  -36.332 23.062  1.00 47.98  ? 53  LEU C CD2 1 
ATOM   1833 N N   . GLY C 1 55 ? 27.269  -34.603 26.208  1.00 36.39  ? 54  GLY C N   1 
ATOM   1834 C CA  . GLY C 1 55 ? 28.403  -33.882 26.754  1.00 36.38  ? 54  GLY C CA  1 
ATOM   1835 C C   . GLY C 1 55 ? 28.639  -32.564 26.016  1.00 40.91  ? 54  GLY C C   1 
ATOM   1836 O O   . GLY C 1 55 ? 28.121  -32.336 24.904  1.00 35.98  ? 54  GLY C O   1 
ATOM   1837 N N   . PRO C 1 56 ? 29.434  -31.648 26.618  1.00 41.46  ? 55  PRO C N   1 
ATOM   1838 C CA  . PRO C 1 56 ? 29.617  -30.309 26.066  1.00 46.14  ? 55  PRO C CA  1 
ATOM   1839 C C   . PRO C 1 56 ? 30.271  -30.329 24.688  1.00 43.69  ? 55  PRO C C   1 
ATOM   1840 O O   . PRO C 1 56 ? 30.042  -29.426 23.887  1.00 52.55  ? 55  PRO C O   1 
ATOM   1841 C CB  . PRO C 1 56 ? 30.442  -29.542 27.132  1.00 52.48  ? 55  PRO C CB  1 
ATOM   1842 C CG  . PRO C 1 56 ? 31.087  -30.628 27.967  1.00 43.25  ? 55  PRO C CG  1 
ATOM   1843 C CD  . PRO C 1 56 ? 30.201  -31.859 27.859  1.00 45.63  ? 55  PRO C CD  1 
ATOM   1844 N N   . LYS C 1 57 ? 31.021  -31.401 24.405  1.00 43.38  ? 56  LYS C N   1 
ATOM   1845 C CA  . LYS C 1 57 ? 31.668  -31.605 23.117  1.00 46.14  ? 56  LYS C CA  1 
ATOM   1846 C C   . LYS C 1 57 ? 30.623  -31.607 21.997  1.00 50.46  ? 56  LYS C C   1 
ATOM   1847 O O   . LYS C 1 57 ? 30.950  -31.342 20.834  1.00 48.15  ? 56  LYS C O   1 
ATOM   1848 C CB  . LYS C 1 57 ? 32.333  -32.985 23.035  1.00 46.45  ? 56  LYS C CB  1 
ATOM   1849 N N   . ASP C 1 58 ? 29.374  -31.909 22.370  1.00 44.38  ? 57  ASP C N   1 
ATOM   1850 C CA  . ASP C 1 58 ? 28.318  -32.209 21.411  1.00 42.88  ? 57  ASP C CA  1 
ATOM   1851 C C   . ASP C 1 58 ? 27.380  -31.025 21.220  1.00 38.21  ? 57  ASP C C   1 
ATOM   1852 O O   . ASP C 1 58 ? 26.365  -31.150 20.527  1.00 37.05  ? 57  ASP C O   1 
ATOM   1853 C CB  . ASP C 1 58 ? 27.507  -33.414 21.857  1.00 45.16  ? 57  ASP C CB  1 
ATOM   1854 C CG  . ASP C 1 58 ? 28.276  -34.720 21.839  1.00 45.09  ? 57  ASP C CG  1 
ATOM   1855 O OD1 . ASP C 1 58 ? 29.268  -34.787 21.100  1.00 52.75  ? 57  ASP C OD1 1 
ATOM   1856 O OD2 . ASP C 1 58 ? 27.882  -35.648 22.566  1.00 50.54  ? 57  ASP C OD2 1 
ATOM   1857 N N   . LEU C 1 59 ? 27.700  -29.890 21.845  1.00 31.68  ? 58  LEU C N   1 
ATOM   1858 C CA  . LEU C 1 59 ? 26.750  -28.788 21.955  1.00 36.07  ? 58  LEU C CA  1 
ATOM   1859 C C   . LEU C 1 59 ? 27.395  -27.502 21.455  1.00 42.62  ? 58  LEU C C   1 
ATOM   1860 O O   . LEU C 1 59 ? 28.579  -27.276 21.744  1.00 41.37  ? 58  LEU C O   1 
ATOM   1861 C CB  . LEU C 1 59 ? 26.327  -28.613 23.418  1.00 34.96  ? 58  LEU C CB  1 
ATOM   1862 C CG  . LEU C 1 59 ? 25.804  -29.865 24.131  1.00 36.00  ? 58  LEU C CG  1 
ATOM   1863 C CD1 . LEU C 1 59 ? 25.609  -29.566 25.616  1.00 35.50  ? 58  LEU C CD1 1 
ATOM   1864 C CD2 . LEU C 1 59 ? 24.482  -30.294 23.482  1.00 28.09  ? 58  LEU C CD2 1 
ATOM   1865 N N   . PHE C 1 60 ? 26.592  -26.677 20.753  1.00 42.57  ? 59  PHE C N   1 
ATOM   1866 C CA  . PHE C 1 60 ? 27.014  -25.419 20.140  1.00 40.99  ? 59  PHE C CA  1 
ATOM   1867 C C   . PHE C 1 60 ? 26.014  -24.312 20.467  1.00 42.86  ? 59  PHE C C   1 
ATOM   1868 O O   . PHE C 1 60 ? 24.834  -24.431 20.146  1.00 43.23  ? 59  PHE C O   1 
ATOM   1869 C CB  . PHE C 1 60 ? 27.220  -25.577 18.627  1.00 40.50  ? 59  PHE C CB  1 
ATOM   1870 C CG  . PHE C 1 60 ? 28.154  -26.737 18.316  1.00 38.36  ? 59  PHE C CG  1 
ATOM   1871 C CD1 . PHE C 1 60 ? 27.687  -28.047 18.315  1.00 37.35  ? 59  PHE C CD1 1 
ATOM   1872 C CD2 . PHE C 1 60 ? 29.509  -26.521 18.065  1.00 44.62  ? 59  PHE C CD2 1 
ATOM   1873 C CE1 . PHE C 1 60 ? 28.538  -29.109 18.100  1.00 36.55  ? 59  PHE C CE1 1 
ATOM   1874 C CE2 . PHE C 1 60 ? 30.366  -27.591 17.817  1.00 43.36  ? 59  PHE C CE2 1 
ATOM   1875 C CZ  . PHE C 1 60 ? 29.882  -28.878 17.834  1.00 42.42  ? 59  PHE C CZ  1 
ATOM   1876 N N   . PRO C 1 61 ? 26.429  -23.182 21.100  1.00 42.17  ? 60  PRO C N   1 
ATOM   1877 C CA  . PRO C 1 61 ? 25.501  -22.079 21.356  1.00 43.42  ? 60  PRO C CA  1 
ATOM   1878 C C   . PRO C 1 61 ? 24.846  -21.647 20.051  1.00 40.06  ? 60  PRO C C   1 
ATOM   1879 O O   . PRO C 1 61 ? 25.496  -21.580 19.008  1.00 43.45  ? 60  PRO C O   1 
ATOM   1880 C CB  . PRO C 1 61 ? 26.303  -20.943 22.052  1.00 44.39  ? 60  PRO C CB  1 
ATOM   1881 C CG  . PRO C 1 61 ? 27.743  -21.441 22.047  1.00 44.84  ? 60  PRO C CG  1 
ATOM   1882 C CD  . PRO C 1 61 ? 27.787  -22.904 21.603  1.00 48.17  ? 60  PRO C CD  1 
ATOM   1883 N N   . TYR C 1 62 ? 23.528  -21.443 20.146  1.00 45.56  ? 61  TYR C N   1 
ATOM   1884 C CA  . TYR C 1 62 ? 22.629  -21.225 19.031  1.00 47.19  ? 61  TYR C CA  1 
ATOM   1885 C C   . TYR C 1 62 ? 23.034  -19.983 18.238  1.00 57.12  ? 61  TYR C C   1 
ATOM   1886 O O   . TYR C 1 62 ? 23.008  -20.018 17.009  1.00 57.05  ? 61  TYR C O   1 
ATOM   1887 C CB  . TYR C 1 62 ? 21.212  -21.035 19.568  1.00 45.21  ? 61  TYR C CB  1 
ATOM   1888 C CG  . TYR C 1 62 ? 20.227  -20.681 18.467  1.00 50.93  ? 61  TYR C CG  1 
ATOM   1889 C CD1 . TYR C 1 62 ? 20.091  -21.493 17.341  1.00 50.31  ? 61  TYR C CD1 1 
ATOM   1890 C CD2 . TYR C 1 62 ? 19.479  -19.508 18.531  1.00 50.19  ? 61  TYR C CD2 1 
ATOM   1891 C CE1 . TYR C 1 62 ? 19.195  -21.166 16.332  1.00 50.61  ? 61  TYR C CE1 1 
ATOM   1892 C CE2 . TYR C 1 62 ? 18.583  -19.172 17.528  1.00 50.76  ? 61  TYR C CE2 1 
ATOM   1893 C CZ  . TYR C 1 62 ? 18.454  -19.996 16.421  1.00 45.29  ? 61  TYR C CZ  1 
ATOM   1894 O OH  . TYR C 1 62 ? 17.584  -19.665 15.427  1.00 47.85  ? 61  TYR C OH  1 
ATOM   1895 N N   . ASP C 1 63 ? 23.420  -18.905 18.941  1.00 50.34  ? 62  ASP C N   1 
ATOM   1896 C CA  . ASP C 1 63 ? 23.680  -17.636 18.272  1.00 60.10  ? 62  ASP C CA  1 
ATOM   1897 C C   . ASP C 1 63 ? 25.005  -17.670 17.526  1.00 54.52  ? 62  ASP C C   1 
ATOM   1898 O O   . ASP C 1 63 ? 25.105  -17.133 16.424  1.00 67.31  ? 62  ASP C O   1 
ATOM   1899 C CB  . ASP C 1 63 ? 23.434  -16.428 19.159  1.00 62.21  ? 62  ASP C CB  1 
ATOM   1900 C CG  . ASP C 1 63 ? 21.965  -16.033 19.213  1.00 70.58  ? 62  ASP C CG  1 
ATOM   1901 O OD1 . ASP C 1 63 ? 21.424  -15.931 20.333  1.00 63.29  ? 62  ASP C OD1 1 
ATOM   1902 O OD2 . ASP C 1 63 ? 21.365  -15.870 18.122  1.00 78.74  ? 62  ASP C OD2 1 
ATOM   1903 N N   . LYS C 1 64 ? 25.995  -18.327 18.123  1.00 47.44  ? 63  LYS C N   1 
ATOM   1904 C CA  . LYS C 1 64 ? 27.319  -18.425 17.538  1.00 51.90  ? 63  LYS C CA  1 
ATOM   1905 C C   . LYS C 1 64 ? 27.293  -19.327 16.308  1.00 48.81  ? 63  LYS C C   1 
ATOM   1906 O O   . LYS C 1 64 ? 28.104  -19.127 15.412  1.00 48.58  ? 63  LYS C O   1 
ATOM   1907 C CB  . LYS C 1 64 ? 28.360  -18.954 18.536  1.00 53.80  ? 63  LYS C CB  1 
ATOM   1908 N N   . SER C 1 65 ? 26.388  -20.324 16.269  1.00 46.15  ? 64  SER C N   1 
ATOM   1909 C CA  . SER C 1 65 ? 26.571  -21.394 15.293  1.00 39.63  ? 64  SER C CA  1 
ATOM   1910 C C   . SER C 1 65 ? 25.409  -21.486 14.299  1.00 41.03  ? 64  SER C C   1 
ATOM   1911 O O   . SER C 1 65 ? 25.446  -22.303 13.380  1.00 39.60  ? 64  SER C O   1 
ATOM   1912 C CB  . SER C 1 65 ? 26.872  -22.737 15.965  1.00 43.75  ? 64  SER C CB  1 
ATOM   1913 O OG  . SER C 1 65 ? 25.705  -23.248 16.604  1.00 39.52  ? 64  SER C OG  1 
ATOM   1914 N N   . LYS C 1 66 ? 24.379  -20.649 14.466  1.00 40.33  ? 65  LYS C N   1 
ATOM   1915 C CA  . LYS C 1 66 ? 23.205  -20.806 13.609  1.00 43.26  ? 65  LYS C CA  1 
ATOM   1916 C C   . LYS C 1 66 ? 23.545  -20.534 12.143  1.00 45.82  ? 65  LYS C C   1 
ATOM   1917 O O   . LYS C 1 66 ? 22.920  -21.120 11.267  1.00 42.20  ? 65  LYS C O   1 
ATOM   1918 C CB  . LYS C 1 66 ? 21.967  -20.010 14.025  1.00 42.27  ? 65  LYS C CB  1 
ATOM   1919 C CG  . LYS C 1 66 ? 22.170  -18.504 13.987  1.00 42.25  ? 65  LYS C CG  1 
ATOM   1920 C CD  . LYS C 1 66 ? 20.891  -17.785 14.389  1.00 49.09  ? 65  LYS C CD  1 
ATOM   1921 C CE  . LYS C 1 66 ? 21.090  -16.319 14.570  1.00 46.01  ? 65  LYS C CE  1 
ATOM   1922 N NZ  . LYS C 1 66 ? 19.898  -15.805 15.231  1.00 54.73  ? 65  LYS C NZ  1 
ATOM   1923 N N   . ASP C 1 67 ? 24.538  -19.672 11.876  1.00 47.30  ? 66  ASP C N   1 
ATOM   1924 C CA  . ASP C 1 67 ? 24.904  -19.341 10.500  1.00 47.69  ? 66  ASP C CA  1 
ATOM   1925 C C   . ASP C 1 67 ? 25.323  -20.625 9.780   1.00 42.80  ? 66  ASP C C   1 
ATOM   1926 O O   . ASP C 1 67 ? 24.999  -20.810 8.613   1.00 43.78  ? 66  ASP C O   1 
ATOM   1927 C CB  . ASP C 1 67 ? 25.745  -18.064 10.391  1.00 46.62  ? 66  ASP C CB  1 
ATOM   1928 C CG  . ASP C 1 67 ? 27.231  -18.133 10.735  1.00 59.44  ? 66  ASP C CG  1 
ATOM   1929 O OD1 . ASP C 1 67 ? 27.789  -19.253 10.802  1.00 64.40  ? 66  ASP C OD1 1 
ATOM   1930 O OD2 . ASP C 1 67 ? 27.841  -17.050 10.942  1.00 66.10  ? 66  ASP C OD2 1 
ATOM   1931 N N   . LYS C 1 68 ? 25.909  -21.572 10.530  1.00 40.26  ? 67  LYS C N   1 
ATOM   1932 C CA  . LYS C 1 68 ? 26.428  -22.828 9.990   1.00 43.61  ? 67  LYS C CA  1 
ATOM   1933 C C   . LYS C 1 68 ? 25.419  -23.990 10.078  1.00 41.18  ? 67  LYS C C   1 
ATOM   1934 O O   . LYS C 1 68 ? 25.296  -24.781 9.141   1.00 40.88  ? 67  LYS C O   1 
ATOM   1935 C CB  . LYS C 1 68 ? 27.755  -23.108 10.711  1.00 42.44  ? 67  LYS C CB  1 
ATOM   1936 C CG  . LYS C 1 68 ? 28.513  -24.374 10.350  1.00 51.22  ? 67  LYS C CG  1 
ATOM   1937 C CD  . LYS C 1 68 ? 29.745  -24.472 11.253  1.00 56.81  ? 67  LYS C CD  1 
ATOM   1938 C CE  . LYS C 1 68 ? 30.320  -25.846 11.471  1.00 68.64  ? 67  LYS C CE  1 
ATOM   1939 N NZ  . LYS C 1 68 ? 31.206  -26.337 10.413  1.00 78.57  ? 67  LYS C NZ  1 
ATOM   1940 N N   . TYR C 1 69 ? 24.693  -24.119 11.198  1.00 36.90  ? 68  TYR C N   1 
ATOM   1941 C CA  . TYR C 1 69 ? 23.860  -25.303 11.376  1.00 35.63  ? 68  TYR C CA  1 
ATOM   1942 C C   . TYR C 1 69 ? 22.382  -24.984 11.170  1.00 33.30  ? 68  TYR C C   1 
ATOM   1943 O O   . TYR C 1 69 ? 21.600  -25.911 11.025  1.00 32.50  ? 68  TYR C O   1 
ATOM   1944 C CB  . TYR C 1 69 ? 23.941  -25.905 12.783  1.00 33.86  ? 68  TYR C CB  1 
ATOM   1945 C CG  . TYR C 1 69 ? 25.346  -26.368 13.118  1.00 35.16  ? 68  TYR C CG  1 
ATOM   1946 C CD1 . TYR C 1 69 ? 26.084  -27.136 12.225  1.00 35.56  ? 68  TYR C CD1 1 
ATOM   1947 C CD2 . TYR C 1 69 ? 25.954  -25.949 14.293  1.00 39.82  ? 68  TYR C CD2 1 
ATOM   1948 C CE1 . TYR C 1 69 ? 27.370  -27.564 12.522  1.00 37.13  ? 68  TYR C CE1 1 
ATOM   1949 C CE2 . TYR C 1 69 ? 27.236  -26.372 14.603  1.00 42.19  ? 68  TYR C CE2 1 
ATOM   1950 C CZ  . TYR C 1 69 ? 27.946  -27.161 13.714  1.00 38.27  ? 68  TYR C CZ  1 
ATOM   1951 O OH  . TYR C 1 69 ? 29.221  -27.519 14.053  1.00 46.69  ? 68  TYR C OH  1 
ATOM   1952 N N   . GLY C 1 70 ? 22.017  -23.688 11.209  1.00 30.34  ? 69  GLY C N   1 
ATOM   1953 C CA  . GLY C 1 70 ? 20.610  -23.304 11.162  1.00 33.11  ? 69  GLY C CA  1 
ATOM   1954 C C   . GLY C 1 70 ? 20.175  -23.174 9.707   1.00 34.95  ? 69  GLY C C   1 
ATOM   1955 O O   . GLY C 1 70 ? 20.136  -22.073 9.158   1.00 38.57  ? 69  GLY C O   1 
ATOM   1956 N N   . LYS C 1 71 ? 20.028  -24.322 9.057   1.00 35.52  ? 70  LYS C N   1 
ATOM   1957 C CA  . LYS C 1 71 ? 19.655  -24.377 7.651   1.00 38.75  ? 70  LYS C CA  1 
ATOM   1958 C C   . LYS C 1 71 ? 18.805  -25.627 7.491   1.00 38.72  ? 70  LYS C C   1 
ATOM   1959 O O   . LYS C 1 71 ? 19.012  -26.612 8.201   1.00 38.78  ? 70  LYS C O   1 
ATOM   1960 C CB  . LYS C 1 71 ? 20.863  -24.500 6.714   1.00 38.90  ? 70  LYS C CB  1 
ATOM   1961 C CG  . LYS C 1 71 ? 21.912  -25.512 7.184   1.00 49.48  ? 70  LYS C CG  1 
ATOM   1962 C CD  . LYS C 1 71 ? 23.045  -25.988 6.280   1.00 54.84  ? 70  LYS C CD  1 
ATOM   1963 C CE  . LYS C 1 71 ? 23.918  -27.022 6.948   1.00 51.63  ? 70  LYS C CE  1 
ATOM   1964 N N   . PRO C 1 72 ? 17.792  -25.627 6.597   1.00 33.38  ? 71  PRO C N   1 
ATOM   1965 C CA  . PRO C 1 72 ? 16.851  -26.733 6.589   1.00 26.55  ? 71  PRO C CA  1 
ATOM   1966 C C   . PRO C 1 72 ? 17.475  -28.077 6.239   1.00 29.95  ? 71  PRO C C   1 
ATOM   1967 O O   . PRO C 1 72 ? 18.452  -28.144 5.490   1.00 35.36  ? 71  PRO C O   1 
ATOM   1968 C CB  . PRO C 1 72 ? 15.912  -26.271 5.469   1.00 28.18  ? 71  PRO C CB  1 
ATOM   1969 C CG  . PRO C 1 72 ? 15.906  -24.772 5.650   1.00 32.73  ? 71  PRO C CG  1 
ATOM   1970 C CD  . PRO C 1 72 ? 17.408  -24.511 5.713   1.00 30.97  ? 71  PRO C CD  1 
ATOM   1971 N N   . ASN C 1 73 ? 16.795  -29.133 6.651   1.00 34.32  ? 72  ASN C N   1 
ATOM   1972 C CA  . ASN C 1 73 ? 17.078  -30.423 6.046   1.00 41.58  ? 72  ASN C CA  1 
ATOM   1973 C C   . ASN C 1 73 ? 15.852  -31.308 6.182   1.00 35.19  ? 72  ASN C C   1 
ATOM   1974 O O   . ASN C 1 73 ? 14.885  -30.928 6.829   1.00 34.23  ? 72  ASN C O   1 
ATOM   1975 C CB  . ASN C 1 73 ? 18.391  -31.054 6.507   1.00 49.73  ? 72  ASN C CB  1 
ATOM   1976 C CG  . ASN C 1 73 ? 18.293  -31.596 7.906   1.00 46.13  ? 72  ASN C CG  1 
ATOM   1977 O OD1 . ASN C 1 73 ? 17.571  -32.568 8.159   1.00 44.33  ? 72  ASN C OD1 1 
ATOM   1978 N ND2 . ASN C 1 73 ? 19.010  -30.973 8.818   1.00 52.12  ? 72  ASN C ND2 1 
ATOM   1979 N N   . LYS C 1 74 ? 15.950  -32.508 5.609   1.00 39.09  ? 73  LYS C N   1 
ATOM   1980 C CA  . LYS C 1 74 ? 14.764  -33.303 5.330   1.00 39.82  ? 73  LYS C CA  1 
ATOM   1981 C C   . LYS C 1 74 ? 14.479  -34.244 6.485   1.00 37.31  ? 73  LYS C C   1 
ATOM   1982 O O   . LYS C 1 74 ? 13.465  -34.936 6.456   1.00 38.76  ? 73  LYS C O   1 
ATOM   1983 C CB  . LYS C 1 74 ? 14.904  -34.065 4.006   1.00 41.98  ? 73  LYS C CB  1 
ATOM   1984 N N   . ARG C 1 75 ? 15.353  -34.271 7.509   1.00 33.51  ? 74  ARG C N   1 
ATOM   1985 C CA  . ARG C 1 75 ? 15.142  -35.235 8.576   1.00 34.07  ? 74  ARG C CA  1 
ATOM   1986 C C   . ARG C 1 75 ? 13.853  -34.906 9.324   1.00 35.85  ? 74  ARG C C   1 
ATOM   1987 O O   . ARG C 1 75 ? 13.506  -33.737 9.551   1.00 34.87  ? 74  ARG C O   1 
ATOM   1988 C CB  . ARG C 1 75 ? 16.287  -35.359 9.606   1.00 36.27  ? 74  ARG C CB  1 
ATOM   1989 C CG  . ARG C 1 75 ? 17.666  -35.509 8.973   1.00 45.67  ? 74  ARG C CG  1 
ATOM   1990 C CD  . ARG C 1 75 ? 17.940  -36.835 8.232   1.00 46.73  ? 74  ARG C CD  1 
ATOM   1991 N NE  . ARG C 1 75 ? 17.982  -37.894 9.243   1.00 43.70  ? 74  ARG C NE  1 
ATOM   1992 C CZ  . ARG C 1 75 ? 19.138  -38.334 9.757   1.00 40.09  ? 74  ARG C CZ  1 
ATOM   1993 N NH1 . ARG C 1 75 ? 19.122  -38.996 10.884  1.00 36.67  ? 74  ARG C NH1 1 
ATOM   1994 N NH2 . ARG C 1 75 ? 20.290  -38.005 9.205   1.00 39.88  ? 74  ARG C NH2 1 
ATOM   1995 N N   . LYS C 1 76 ? 13.180  -35.970 9.761   1.00 36.29  ? 75  LYS C N   1 
ATOM   1996 C CA  . LYS C 1 76 ? 11.897  -35.839 10.439  1.00 41.07  ? 75  LYS C CA  1 
ATOM   1997 C C   . LYS C 1 76 ? 11.976  -34.841 11.593  1.00 40.03  ? 75  LYS C C   1 
ATOM   1998 O O   . LYS C 1 76 ? 12.759  -35.010 12.542  1.00 36.80  ? 75  LYS C O   1 
ATOM   1999 C CB  . LYS C 1 76 ? 11.293  -37.192 10.848  1.00 43.28  ? 75  LYS C CB  1 
ATOM   2000 C CG  . LYS C 1 76 ? 9.760   -37.164 10.883  1.00 52.39  ? 75  LYS C CG  1 
ATOM   2001 C CD  . LYS C 1 76 ? 9.088   -38.094 11.892  1.00 56.65  ? 75  LYS C CD  1 
ATOM   2002 N N   . GLY C 1 77 ? 11.117  -33.815 11.515  1.00 39.36  ? 76  GLY C N   1 
ATOM   2003 C CA  . GLY C 1 77 ? 10.902  -32.908 12.633  1.00 38.22  ? 76  GLY C CA  1 
ATOM   2004 C C   . GLY C 1 77 ? 11.909  -31.755 12.631  1.00 34.21  ? 76  GLY C C   1 
ATOM   2005 O O   . GLY C 1 77 ? 11.801  -30.832 13.435  1.00 38.18  ? 76  GLY C O   1 
ATOM   2006 N N   . PHE C 1 78 ? 12.871  -31.771 11.692  1.00 31.78  ? 77  PHE C N   1 
ATOM   2007 C CA  . PHE C 1 78 ? 13.962  -30.810 11.757  1.00 28.93  ? 77  PHE C CA  1 
ATOM   2008 C C   . PHE C 1 78 ? 13.461  -29.374 11.530  1.00 33.11  ? 77  PHE C C   1 
ATOM   2009 O O   . PHE C 1 78 ? 13.883  -28.412 12.200  1.00 31.75  ? 77  PHE C O   1 
ATOM   2010 C CB  . PHE C 1 78 ? 15.092  -31.136 10.758  1.00 35.22  ? 77  PHE C CB  1 
ATOM   2011 C CG  . PHE C 1 78 ? 16.401  -30.390 11.029  1.00 31.67  ? 77  PHE C CG  1 
ATOM   2012 C CD1 . PHE C 1 78 ? 16.625  -29.106 10.537  1.00 32.80  ? 77  PHE C CD1 1 
ATOM   2013 C CD2 . PHE C 1 78 ? 17.405  -30.961 11.805  1.00 29.31  ? 77  PHE C CD2 1 
ATOM   2014 C CE1 . PHE C 1 78 ? 17.803  -28.417 10.804  1.00 32.90  ? 77  PHE C CE1 1 
ATOM   2015 C CE2 . PHE C 1 78 ? 18.581  -30.264 12.082  1.00 27.04  ? 77  PHE C CE2 1 
ATOM   2016 C CZ  . PHE C 1 78 ? 18.772  -28.987 11.602  1.00 32.89  ? 77  PHE C CZ  1 
ATOM   2017 N N   . ASN C 1 79 ? 12.641  -29.214 10.488  1.00 27.61  ? 78  ASN C N   1 
ATOM   2018 C CA  . ASN C 1 79 ? 12.340  -27.876 10.014  1.00 29.41  ? 78  ASN C CA  1 
ATOM   2019 C C   . ASN C 1 79 ? 11.391  -27.209 11.002  1.00 30.19  ? 78  ASN C C   1 
ATOM   2020 O O   . ASN C 1 79 ? 11.487  -26.011 11.271  1.00 31.01  ? 78  ASN C O   1 
ATOM   2021 C CB  . ASN C 1 79 ? 11.889  -27.898 8.563   1.00 32.39  ? 78  ASN C CB  1 
ATOM   2022 C CG  . ASN C 1 79 ? 13.024  -28.277 7.639   1.00 32.48  ? 78  ASN C CG  1 
ATOM   2023 O OD1 . ASN C 1 79 ? 14.192  -28.036 7.955   1.00 32.89  ? 78  ASN C OD1 1 
ATOM   2024 N ND2 . ASN C 1 79 ? 12.714  -28.849 6.488   1.00 31.95  ? 78  ASN C ND2 1 
ATOM   2025 N N   . GLU C 1 80 ? 10.520  -27.996 11.606  1.00 34.49  ? 79  GLU C N   1 
ATOM   2026 C CA  . GLU C 1 80 ? 9.689   -27.455 12.673  1.00 33.10  ? 79  GLU C CA  1 
ATOM   2027 C C   . GLU C 1 80 ? 10.558  -27.079 13.871  1.00 39.46  ? 79  GLU C C   1 
ATOM   2028 O O   . GLU C 1 80 ? 10.292  -26.078 14.545  1.00 37.40  ? 79  GLU C O   1 
ATOM   2029 C CB  . GLU C 1 80 ? 8.676   -28.521 13.066  1.00 37.83  ? 79  GLU C CB  1 
ATOM   2030 C CG  . GLU C 1 80 ? 7.756   -28.031 14.175  1.00 43.05  ? 79  GLU C CG  1 
ATOM   2031 C CD  . GLU C 1 80 ? 6.497   -28.846 14.334  1.00 50.41  ? 79  GLU C CD  1 
ATOM   2032 O OE1 . GLU C 1 80 ? 6.330   -29.913 13.703  1.00 53.49  ? 79  GLU C OE1 1 
ATOM   2033 O OE2 . GLU C 1 80 ? 5.662   -28.366 15.115  1.00 51.33  ? 79  GLU C OE2 1 
ATOM   2034 N N   . GLY C 1 81 ? 11.636  -27.861 14.095  1.00 35.75  ? 80  GLY C N   1 
ATOM   2035 C CA  . GLY C 1 81 ? 12.568  -27.553 15.175  1.00 31.38  ? 80  GLY C CA  1 
ATOM   2036 C C   . GLY C 1 81 ? 13.187  -26.172 14.966  1.00 32.17  ? 80  GLY C C   1 
ATOM   2037 O O   . GLY C 1 81 ? 13.390  -25.419 15.912  1.00 31.61  ? 80  GLY C O   1 
ATOM   2038 N N   . LEU C 1 82 ? 13.599  -25.903 13.720  1.00 31.38  ? 81  LEU C N   1 
ATOM   2039 C CA  . LEU C 1 82 ? 14.214  -24.633 13.363  1.00 34.43  ? 81  LEU C CA  1 
ATOM   2040 C C   . LEU C 1 82 ? 13.240  -23.478 13.615  1.00 31.47  ? 81  LEU C C   1 
ATOM   2041 O O   . LEU C 1 82 ? 13.650  -22.399 14.062  1.00 33.94  ? 81  LEU C O   1 
ATOM   2042 C CB  . LEU C 1 82 ? 14.611  -24.697 11.888  1.00 35.21  ? 81  LEU C CB  1 
ATOM   2043 C CG  . LEU C 1 82 ? 15.897  -25.454 11.525  1.00 33.37  ? 81  LEU C CG  1 
ATOM   2044 C CD1 . LEU C 1 82 ? 16.192  -25.301 10.037  1.00 29.56  ? 81  LEU C CD1 1 
ATOM   2045 C CD2 . LEU C 1 82 ? 17.048  -24.878 12.279  1.00 28.57  ? 81  LEU C CD2 1 
ATOM   2046 N N   . TRP C 1 83 ? 11.964  -23.695 13.294  1.00 31.35  ? 82  TRP C N   1 
ATOM   2047 C CA  . TRP C 1 83 ? 10.931  -22.700 13.581  1.00 41.65  ? 82  TRP C CA  1 
ATOM   2048 C C   . TRP C 1 83 ? 10.827  -22.420 15.090  1.00 41.63  ? 82  TRP C C   1 
ATOM   2049 O O   . TRP C 1 83 ? 10.873  -21.264 15.517  1.00 39.01  ? 82  TRP C O   1 
ATOM   2050 C CB  . TRP C 1 83 ? 9.571   -23.113 13.001  1.00 42.16  ? 82  TRP C CB  1 
ATOM   2051 C CG  . TRP C 1 83 ? 8.577   -21.983 13.080  1.00 50.23  ? 82  TRP C CG  1 
ATOM   2052 C CD1 . TRP C 1 83 ? 8.375   -20.999 12.155  1.00 48.66  ? 82  TRP C CD1 1 
ATOM   2053 C CD2 . TRP C 1 83 ? 7.688   -21.686 14.182  1.00 51.66  ? 82  TRP C CD2 1 
ATOM   2054 N NE1 . TRP C 1 83 ? 7.409   -20.131 12.582  1.00 42.36  ? 82  TRP C NE1 1 
ATOM   2055 C CE2 . TRP C 1 83 ? 6.972   -20.520 13.821  1.00 46.62  ? 82  TRP C CE2 1 
ATOM   2056 C CE3 . TRP C 1 83 ? 7.431   -22.287 15.424  1.00 50.55  ? 82  TRP C CE3 1 
ATOM   2057 C CZ2 . TRP C 1 83 ? 6.027   -19.948 14.666  1.00 51.23  ? 82  TRP C CZ2 1 
ATOM   2058 C CZ3 . TRP C 1 83 ? 6.497   -21.718 16.264  1.00 47.87  ? 82  TRP C CZ3 1 
ATOM   2059 C CH2 . TRP C 1 83 ? 5.817   -20.556 15.889  1.00 54.34  ? 82  TRP C CH2 1 
ATOM   2060 N N   . GLU C 1 84 ? 10.745  -23.480 15.897  1.00 37.35  ? 83  GLU C N   1 
ATOM   2061 C CA  . GLU C 1 84 ? 10.659  -23.357 17.352  1.00 39.96  ? 83  GLU C CA  1 
ATOM   2062 C C   . GLU C 1 84 ? 11.829  -22.590 17.960  1.00 38.77  ? 83  GLU C C   1 
ATOM   2063 O O   . GLU C 1 84 ? 11.605  -21.692 18.779  1.00 40.38  ? 83  GLU C O   1 
ATOM   2064 C CB  . GLU C 1 84 ? 10.515  -24.705 18.060  1.00 36.27  ? 83  GLU C CB  1 
ATOM   2065 C CG  . GLU C 1 84 ? 9.177   -25.358 17.747  1.00 38.41  ? 83  GLU C CG  1 
ATOM   2066 C CD  . GLU C 1 84 ? 9.095   -26.806 18.163  1.00 44.85  ? 83  GLU C CD  1 
ATOM   2067 O OE1 . GLU C 1 84 ? 10.080  -27.322 18.736  1.00 41.71  ? 83  GLU C OE1 1 
ATOM   2068 O OE2 . GLU C 1 84 ? 8.052   -27.422 17.875  1.00 45.27  ? 83  GLU C OE2 1 
ATOM   2069 N N   . ILE C 1 85 ? 13.067  -22.927 17.569  1.00 35.87  ? 84  ILE C N   1 
ATOM   2070 C CA  . ILE C 1 85 ? 14.252  -22.356 18.199  1.00 36.00  ? 84  ILE C CA  1 
ATOM   2071 C C   . ILE C 1 85 ? 14.368  -20.852 17.905  1.00 40.06  ? 84  ILE C C   1 
ATOM   2072 O O   . ILE C 1 85 ? 14.923  -20.104 18.702  1.00 34.75  ? 84  ILE C O   1 
ATOM   2073 C CB  . ILE C 1 85 ? 15.545  -23.102 17.838  1.00 33.92  ? 84  ILE C CB  1 
ATOM   2074 C CG1 . ILE C 1 85 ? 16.668  -22.761 18.866  1.00 31.74  ? 84  ILE C CG1 1 
ATOM   2075 C CG2 . ILE C 1 85 ? 15.993  -22.854 16.383  1.00 33.89  ? 84  ILE C CG2 1 
ATOM   2076 C CD1 . ILE C 1 85 ? 17.907  -23.645 18.804  1.00 33.13  ? 84  ILE C CD1 1 
ATOM   2077 N N   . GLN C 1 86 ? 13.887  -20.430 16.729  1.00 38.65  ? 85  GLN C N   1 
ATOM   2078 C CA  . GLN C 1 86 ? 13.880  -19.027 16.328  1.00 41.76  ? 85  GLN C CA  1 
ATOM   2079 C C   . GLN C 1 86 ? 12.667  -18.263 16.882  1.00 39.50  ? 85  GLN C C   1 
ATOM   2080 O O   . GLN C 1 86 ? 12.795  -17.095 17.244  1.00 46.17  ? 85  GLN C O   1 
ATOM   2081 C CB  . GLN C 1 86 ? 13.950  -18.944 14.796  1.00 40.25  ? 85  GLN C CB  1 
ATOM   2082 C CG  . GLN C 1 86 ? 14.135  -17.522 14.261  1.00 43.36  ? 85  GLN C CG  1 
ATOM   2083 C CD  . GLN C 1 86 ? 14.514  -17.498 12.790  1.00 44.09  ? 85  GLN C CD  1 
ATOM   2084 O OE1 . GLN C 1 86 ? 14.439  -18.511 12.084  1.00 43.07  ? 85  GLN C OE1 1 
ATOM   2085 N NE2 . GLN C 1 86 ? 14.980  -16.348 12.325  1.00 40.59  ? 85  GLN C NE2 1 
ATOM   2086 N N   . ASN C 1 87 ? 11.498  -18.904 16.933  1.00 38.64  ? 86  ASN C N   1 
ATOM   2087 C CA  . ASN C 1 87 ? 10.232  -18.209 17.107  1.00 49.06  ? 86  ASN C CA  1 
ATOM   2088 C C   . ASN C 1 87 ? 9.543   -18.546 18.435  1.00 54.82  ? 86  ASN C C   1 
ATOM   2089 O O   . ASN C 1 87 ? 8.639   -17.823 18.827  1.00 51.95  ? 86  ASN C O   1 
ATOM   2090 C CB  . ASN C 1 87 ? 9.247   -18.494 15.977  1.00 45.13  ? 86  ASN C CB  1 
ATOM   2091 C CG  . ASN C 1 87 ? 9.754   -17.957 14.661  1.00 47.82  ? 86  ASN C CG  1 
ATOM   2092 O OD1 . ASN C 1 87 ? 9.862   -16.739 14.494  1.00 48.12  ? 86  ASN C OD1 1 
ATOM   2093 N ND2 . ASN C 1 87 ? 10.124  -18.836 13.744  1.00 40.80  ? 86  ASN C ND2 1 
ATOM   2094 N N   . ASN C 1 88 ? 9.915   -19.651 19.107  1.00 53.75  ? 87  ASN C N   1 
ATOM   2095 C CA  . ASN C 1 88 ? 9.215   -20.023 20.338  1.00 47.32  ? 87  ASN C CA  1 
ATOM   2096 C C   . ASN C 1 88 ? 10.140  -20.837 21.241  1.00 42.88  ? 87  ASN C C   1 
ATOM   2097 O O   . ASN C 1 88 ? 9.782   -21.936 21.662  1.00 49.95  ? 87  ASN C O   1 
ATOM   2098 C CB  . ASN C 1 88 ? 7.939   -20.809 20.043  1.00 53.04  ? 87  ASN C CB  1 
ATOM   2099 C CG  . ASN C 1 88 ? 6.904   -20.678 21.137  1.00 58.75  ? 87  ASN C CG  1 
ATOM   2100 O OD1 . ASN C 1 88 ? 7.081   -19.875 22.060  1.00 63.94  ? 87  ASN C OD1 1 
ATOM   2101 N ND2 . ASN C 1 88 ? 5.827   -21.443 21.049  1.00 54.39  ? 87  ASN C ND2 1 
ATOM   2102 N N   . PRO C 1 89 ? 11.358  -20.343 21.556  1.00 42.36  ? 88  PRO C N   1 
ATOM   2103 C CA  . PRO C 1 89 ? 12.372  -21.180 22.198  1.00 47.78  ? 88  PRO C CA  1 
ATOM   2104 C C   . PRO C 1 89 ? 12.085  -21.725 23.599  1.00 54.28  ? 88  PRO C C   1 
ATOM   2105 O O   . PRO C 1 89 ? 12.769  -22.655 24.037  1.00 49.49  ? 88  PRO C O   1 
ATOM   2106 C CB  . PRO C 1 89 ? 13.646  -20.327 22.131  1.00 49.60  ? 88  PRO C CB  1 
ATOM   2107 C CG  . PRO C 1 89 ? 13.120  -18.903 22.093  1.00 48.33  ? 88  PRO C CG  1 
ATOM   2108 C CD  . PRO C 1 89 ? 11.827  -18.975 21.290  1.00 45.48  ? 88  PRO C CD  1 
ATOM   2109 N N   . HIS C 1 90 ? 11.044  -21.191 24.265  1.00 59.29  ? 89  HIS C N   1 
ATOM   2110 C CA  . HIS C 1 90 ? 10.770  -21.545 25.653  1.00 55.63  ? 89  HIS C CA  1 
ATOM   2111 C C   . HIS C 1 90 ? 9.311   -21.946 25.892  1.00 56.84  ? 89  HIS C C   1 
ATOM   2112 O O   . HIS C 1 90 ? 8.837   -21.894 27.020  1.00 66.30  ? 89  HIS C O   1 
ATOM   2113 C CB  . HIS C 1 90 ? 11.290  -20.473 26.613  1.00 46.23  ? 89  HIS C CB  1 
ATOM   2114 C CG  . HIS C 1 90 ? 12.672  -19.983 26.327  1.00 46.87  ? 89  HIS C CG  1 
ATOM   2115 N ND1 . HIS C 1 90 ? 12.928  -18.716 25.847  1.00 51.81  ? 89  HIS C ND1 1 
ATOM   2116 C CD2 . HIS C 1 90 ? 13.881  -20.546 26.497  1.00 47.44  ? 89  HIS C CD2 1 
ATOM   2117 C CE1 . HIS C 1 90 ? 14.241  -18.539 25.706  1.00 43.86  ? 89  HIS C CE1 1 
ATOM   2118 N NE2 . HIS C 1 90 ? 14.837  -19.634 26.101  1.00 46.64  ? 89  HIS C NE2 1 
ATOM   2119 N N   . ALA C 1 91 ? 8.602   -22.387 24.848  1.00 63.14  ? 90  ALA C N   1 
ATOM   2120 C CA  . ALA C 1 91 ? 7.295   -23.004 25.035  1.00 64.92  ? 90  ALA C CA  1 
ATOM   2121 C C   . ALA C 1 91 ? 7.454   -24.386 25.680  1.00 75.94  ? 90  ALA C C   1 
ATOM   2122 O O   . ALA C 1 91 ? 8.579   -24.852 25.868  1.00 76.74  ? 90  ALA C O   1 
ATOM   2123 C CB  . ALA C 1 91 ? 6.542   -23.061 23.719  1.00 63.07  ? 90  ALA C CB  1 
ATOM   2124 N N   . SER C 1 92 ? 6.321   -25.046 25.983  1.00 77.78  ? 91  SER C N   1 
ATOM   2125 C CA  . SER C 1 92 ? 6.270   -26.218 26.854  1.00 76.99  ? 91  SER C CA  1 
ATOM   2126 C C   . SER C 1 92 ? 6.302   -27.545 26.091  1.00 75.76  ? 91  SER C C   1 
ATOM   2127 O O   . SER C 1 92 ? 6.879   -28.518 26.574  1.00 71.80  ? 91  SER C O   1 
ATOM   2128 C CB  . SER C 1 92 ? 5.069   -26.158 27.777  1.00 72.15  ? 91  SER C CB  1 
ATOM   2129 O OG  . SER C 1 92 ? 5.267   -25.173 28.780  1.00 75.34  ? 91  SER C OG  1 
ATOM   2130 N N   . TYR C 1 93 ? 5.617   -27.600 24.942  1.00 81.96  ? 92  TYR C N   1 
ATOM   2131 C CA  . TYR C 1 93 ? 5.497   -28.807 24.130  1.00 86.84  ? 92  TYR C CA  1 
ATOM   2132 C C   . TYR C 1 93 ? 5.328   -30.039 25.041  1.00 91.89  ? 92  TYR C C   1 
ATOM   2133 O O   . TYR C 1 93 ? 4.238   -30.664 25.075  1.00 96.74  ? 92  TYR C O   1 
ATOM   2134 C CB  . TYR C 1 93 ? 6.707   -28.966 23.199  1.00 86.03  ? 92  TYR C CB  1 
ATOM   2135 C CG  . TYR C 1 93 ? 7.209   -27.677 22.557  1.00 77.28  ? 92  TYR C CG  1 
ATOM   2136 C CD1 . TYR C 1 93 ? 6.686   -27.216 21.350  1.00 65.23  ? 92  TYR C CD1 1 
ATOM   2137 C CD2 . TYR C 1 93 ? 8.207   -26.919 23.164  1.00 70.15  ? 92  TYR C CD2 1 
ATOM   2138 C CE1 . TYR C 1 93 ? 7.141   -26.043 20.769  1.00 67.39  ? 92  TYR C CE1 1 
ATOM   2139 C CE2 . TYR C 1 93 ? 8.674   -25.749 22.586  1.00 70.16  ? 92  TYR C CE2 1 
ATOM   2140 C CZ  . TYR C 1 93 ? 8.143   -25.310 21.386  1.00 68.68  ? 92  TYR C CZ  1 
ATOM   2141 O OH  . TYR C 1 93 ? 8.601   -24.140 20.835  1.00 70.52  ? 92  TYR C OH  1 
HETATM 2142 S S   . SO4 D 2 .  ? 1.052   -33.728 1.992   1.00 90.77  ? 101 SO4 A S   1 
HETATM 2143 O O1  . SO4 D 2 .  ? 1.464   -34.450 0.807   1.00 70.35  ? 101 SO4 A O1  1 
HETATM 2144 O O2  . SO4 D 2 .  ? 1.070   -32.309 1.733   1.00 79.00  ? 101 SO4 A O2  1 
HETATM 2145 O O3  . SO4 D 2 .  ? -0.283  -34.133 2.365   1.00 97.45  ? 101 SO4 A O3  1 
HETATM 2146 O O4  . SO4 D 2 .  ? 1.952   -34.018 3.076   1.00 84.75  ? 101 SO4 A O4  1 
HETATM 2147 S S   . SO4 E 2 .  ? -9.329  -24.564 1.312   1.00 95.39  ? 102 SO4 A S   1 
HETATM 2148 O O1  . SO4 E 2 .  ? -9.418  -24.219 -0.083  1.00 91.74  ? 102 SO4 A O1  1 
HETATM 2149 O O2  . SO4 E 2 .  ? -9.715  -23.437 2.122   1.00 89.11  ? 102 SO4 A O2  1 
HETATM 2150 O O3  . SO4 E 2 .  ? -10.199 -25.682 1.581   1.00 99.07  ? 102 SO4 A O3  1 
HETATM 2151 O O4  . SO4 E 2 .  ? -7.977  -24.927 1.632   1.00 102.23 ? 102 SO4 A O4  1 
HETATM 2152 C C1  . EDO F 3 .  ? 13.963  -19.638 -7.586  1.00 43.95  ? 103 EDO A C1  1 
HETATM 2153 O O1  . EDO F 3 .  ? 15.073  -18.835 -7.215  1.00 36.75  ? 103 EDO A O1  1 
HETATM 2154 C C2  . EDO F 3 .  ? 12.998  -19.006 -8.540  1.00 38.94  ? 103 EDO A C2  1 
HETATM 2155 O O2  . EDO F 3 .  ? 12.704  -17.647 -8.276  1.00 39.74  ? 103 EDO A O2  1 
HETATM 2156 S S   . SO4 G 2 .  ? 9.018   -29.387 5.812   1.00 67.23  ? 104 SO4 A S   1 
HETATM 2157 O O1  . SO4 G 2 .  ? 9.637   -28.463 4.923   1.00 62.36  ? 104 SO4 A O1  1 
HETATM 2158 O O2  . SO4 G 2 .  ? 8.728   -30.605 5.085   1.00 68.96  ? 104 SO4 A O2  1 
HETATM 2159 O O3  . SO4 G 2 .  ? 9.906   -29.667 6.910   1.00 69.17  ? 104 SO4 A O3  1 
HETATM 2160 O O4  . SO4 G 2 .  ? 7.789   -28.828 6.314   1.00 73.58  ? 104 SO4 A O4  1 
HETATM 2161 S S   . SO4 H 2 .  ? 7.397   -8.613  -24.735 1.00 76.53  ? 101 SO4 B S   1 
HETATM 2162 O O1  . SO4 H 2 .  ? 8.524   -8.592  -25.628 1.00 44.69  ? 101 SO4 B O1  1 
HETATM 2163 O O2  . SO4 H 2 .  ? 6.260   -9.203  -25.406 1.00 57.92  ? 101 SO4 B O2  1 
HETATM 2164 O O3  . SO4 H 2 .  ? 7.663   -9.390  -23.525 1.00 49.42  ? 101 SO4 B O3  1 
HETATM 2165 O O4  . SO4 H 2 .  ? 7.134   -7.239  -24.380 1.00 70.51  ? 101 SO4 B O4  1 
HETATM 2166 S S   . SO4 I 2 .  ? 14.409  -26.965 -26.459 1.00 55.99  ? 102 SO4 B S   1 
HETATM 2167 O O1  . SO4 I 2 .  ? 15.826  -26.813 -26.293 1.00 52.53  ? 102 SO4 B O1  1 
HETATM 2168 O O2  . SO4 I 2 .  ? 14.139  -28.217 -27.120 1.00 66.98  ? 102 SO4 B O2  1 
HETATM 2169 O O3  . SO4 I 2 .  ? 13.786  -26.977 -25.160 1.00 67.77  ? 102 SO4 B O3  1 
HETATM 2170 O O4  . SO4 I 2 .  ? 13.872  -25.881 -27.236 1.00 54.28  ? 102 SO4 B O4  1 
HETATM 2171 C C10 . EJQ J 4 .  ? 19.086  -16.749 -23.047 0.80 29.21  ? 103 EJQ B C10 1 
HETATM 2172 C C13 . EJQ J 4 .  ? 16.139  -15.578 -24.869 0.80 28.07  ? 103 EJQ B C13 1 
HETATM 2173 C C15 . EJQ J 4 .  ? 18.461  -16.086 -25.318 0.80 27.47  ? 103 EJQ B C15 1 
HETATM 2174 C C01 . EJQ J 4 .  ? 23.502  -16.032 -22.827 0.80 35.85  ? 103 EJQ B C01 1 
HETATM 2175 C C02 . EJQ J 4 .  ? 24.867  -15.917 -22.611 0.80 40.26  ? 103 EJQ B C02 1 
HETATM 2176 C C03 . EJQ J 4 .  ? 25.464  -16.790 -21.739 0.80 44.81  ? 103 EJQ B C03 1 
HETATM 2177 C C04 . EJQ J 4 .  ? 24.782  -17.794 -21.108 0.80 43.87  ? 103 EJQ B C04 1 
HETATM 2178 C C05 . EJQ J 4 .  ? 23.418  -17.905 -21.332 0.80 38.56  ? 103 EJQ B C05 1 
HETATM 2179 C C06 . EJQ J 4 .  ? 22.763  -16.999 -22.163 0.80 34.99  ? 103 EJQ B C06 1 
HETATM 2180 C C08 . EJQ J 4 .  ? 20.510  -16.226 -22.942 0.80 33.04  ? 103 EJQ B C08 1 
HETATM 2181 C C12 . EJQ J 4 .  ? 16.795  -16.237 -23.698 0.80 27.45  ? 103 EJQ B C12 1 
HETATM 2182 C C14 . EJQ J 4 .  ? 17.084  -15.917 -25.972 0.80 29.24  ? 103 EJQ B C14 1 
HETATM 2183 F F16 . EJQ J 4 .  ? 26.781  -16.619 -21.453 0.80 43.38  ? 103 EJQ B F16 1 
HETATM 2184 N N07 . EJQ J 4 .  ? 21.336  -17.027 -22.233 0.80 33.91  ? 103 EJQ B N07 1 
HETATM 2185 N N11 . EJQ J 4 .  ? 18.212  -15.917 -23.871 0.80 28.42  ? 103 EJQ B N11 1 
HETATM 2186 O O09 . EJQ J 4 .  ? 20.843  -15.147 -23.453 0.80 30.76  ? 103 EJQ B O09 1 
HETATM 2187 C C1  . EDO K 3 .  ? 16.812  -36.369 16.520  1.00 38.17  ? 101 EDO C C1  1 
HETATM 2188 O O1  . EDO K 3 .  ? 15.779  -36.874 15.693  1.00 41.69  ? 101 EDO C O1  1 
HETATM 2189 C C2  . EDO K 3 .  ? 16.381  -35.353 17.509  1.00 40.60  ? 101 EDO C C2  1 
HETATM 2190 O O2  . EDO K 3 .  ? 15.308  -35.838 18.245  1.00 35.16  ? 101 EDO C O2  1 
HETATM 2191 S S   . SO4 L 2 .  ? 29.015  -38.510 12.244  1.00 85.92  ? 102 SO4 C S   1 
HETATM 2192 O O1  . SO4 L 2 .  ? 29.926  -37.638 11.546  1.00 89.74  ? 102 SO4 C O1  1 
HETATM 2193 O O2  . SO4 L 2 .  ? 27.663  -38.121 11.950  1.00 72.75  ? 102 SO4 C O2  1 
HETATM 2194 O O3  . SO4 L 2 .  ? 29.227  -39.868 11.822  1.00 82.94  ? 102 SO4 C O3  1 
HETATM 2195 O O4  . SO4 L 2 .  ? 29.247  -38.413 13.663  1.00 91.30  ? 102 SO4 C O4  1 
HETATM 2196 O O   . HOH M 5 .  ? 8.445   -32.562 4.306   1.00 60.96  ? 201 HOH A O   1 
HETATM 2197 O O   . HOH M 5 .  ? -5.522  -13.405 -16.520 1.00 51.92  ? 202 HOH A O   1 
HETATM 2198 O O   . HOH M 5 .  ? 5.677   -28.995 7.044   1.00 54.92  ? 203 HOH A O   1 
HETATM 2199 O O   . HOH M 5 .  ? -2.309  -30.948 -3.852  1.00 54.38  ? 204 HOH A O   1 
HETATM 2200 O O   . HOH M 5 .  ? 3.876   -34.562 4.287   1.00 59.61  ? 205 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? 9.872   -18.671 10.080  1.00 64.61  ? 206 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? 4.152   -10.570 13.552  1.00 62.59  ? 207 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? 13.974  -15.731 -9.191  1.00 36.03  ? 208 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? 0.576   -10.644 -15.486 1.00 46.10  ? 209 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? -8.436  -21.217 -1.089  1.00 41.81  ? 210 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? 10.967  -29.713 2.946   1.00 43.55  ? 211 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 10.797  -9.670  -13.319 1.00 54.44  ? 212 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? 9.091   -18.261 -11.014 1.00 35.85  ? 213 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? -7.003  -21.986 -5.651  1.00 76.72  ? 214 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? 4.478   -7.960  0.982   1.00 38.15  ? 215 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? 12.637  -28.284 -3.982  1.00 58.20  ? 216 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? -2.407  3.152   -1.933  1.00 47.17  ? 217 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 1.401   -24.513 13.994  1.00 77.47  ? 218 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? -3.658  -10.828 6.782   1.00 40.25  ? 219 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 9.315   -22.613 -9.480  1.00 41.36  ? 220 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? -2.425  -11.527 14.145  1.00 58.10  ? 221 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 19.737  -15.476 7.250   1.00 33.94  ? 222 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 14.883  -17.555 -19.126 1.00 38.75  ? 223 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? 0.209   -33.759 5.009   1.00 51.64  ? 224 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 15.781  -24.435 1.946   1.00 48.73  ? 225 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? -5.059  -25.552 -5.456  1.00 66.11  ? 226 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 10.952  -23.602 9.860   1.00 44.94  ? 227 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? 4.445   -3.535  -3.355  1.00 36.24  ? 228 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 2.638   -10.142 -13.237 1.00 51.35  ? 229 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 2.418   -25.094 -10.123 1.00 43.18  ? 230 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 9.492   -6.072  -1.514  1.00 48.06  ? 231 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 6.922   -10.576 -12.153 1.00 42.95  ? 232 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? -0.640  -29.288 10.239  1.00 59.70  ? 233 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? 11.492  -12.027 5.955   1.00 37.37  ? 234 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? -8.048  -15.792 -0.985  1.00 40.12  ? 235 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 10.648  -5.248  -7.823  1.00 31.68  ? 236 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? -7.905  -16.663 1.920   1.00 44.48  ? 237 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 3.234   -29.532 -0.474  1.00 41.00  ? 238 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? -0.690  -20.908 7.036   1.00 35.23  ? 239 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? -7.803  -17.232 6.684   1.00 51.52  ? 240 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 12.882  -9.280  -7.242  1.00 45.99  ? 241 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 11.348  -12.415 -6.112  1.00 30.55  ? 242 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 1.698   0.491   -7.636  1.00 49.14  ? 243 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? -4.463  -21.243 6.173   1.00 45.10  ? 244 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 1.510   -18.497 -18.663 1.00 48.78  ? 245 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? -5.784  -19.572 -5.647  1.00 47.76  ? 246 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? 10.060  -13.193 9.712   1.00 47.27  ? 247 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 8.794   -16.222 -13.133 1.00 35.34  ? 248 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? -1.783  -22.003 -0.600  1.00 28.93  ? 249 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 14.365  -29.428 4.005   1.00 52.23  ? 250 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? -5.802  -15.786 -8.015  1.00 31.47  ? 251 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? 17.186  -12.899 1.359   1.00 23.11  ? 252 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 13.178  -11.619 7.906   1.00 57.77  ? 253 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? -6.084  -12.838 6.755   1.00 41.14  ? 254 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? 13.198  -12.084 -4.266  1.00 24.12  ? 255 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 12.653  -15.579 -12.080 1.00 54.30  ? 256 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 1.706   -10.332 11.634  1.00 36.73  ? 257 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? 8.323   -18.092 -15.939 1.00 48.19  ? 258 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? -1.291  -11.744 11.303  1.00 42.06  ? 259 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 1.836   -4.662  -10.352 1.00 48.84  ? 260 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? 15.702  -12.083 -5.380  1.00 39.18  ? 261 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 9.624   -30.406 9.702   1.00 33.72  ? 262 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 0.072   -23.435 9.297   1.00 54.09  ? 263 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 11.315  -5.933  -4.030  1.00 54.08  ? 264 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 8.071   -17.375 8.660   1.00 50.53  ? 265 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? -1.459  -7.504  11.562  1.00 47.46  ? 266 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? 11.473  -16.741 -14.748 1.00 46.50  ? 267 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? 16.763  -12.507 -16.901 1.00 42.71  ? 268 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? 6.457   -6.029  0.431   1.00 55.16  ? 269 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 12.592  -13.565 -8.631  1.00 43.33  ? 270 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 7.839   -7.818  1.217   1.00 32.63  ? 271 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? -6.364  -26.667 3.430   1.00 48.55  ? 272 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? -6.319  -11.450 -11.285 1.00 42.02  ? 273 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? 5.023   -7.547  3.895   1.00 38.32  ? 274 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 1.855   -24.972 -6.462  1.00 54.55  ? 275 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? 2.361   -6.122  5.378   1.00 45.28  ? 276 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 10.920  -7.965  0.414   1.00 30.28  ? 277 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? 6.463   -16.310 -14.808 1.00 57.84  ? 278 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? -7.278  -11.475 -7.997  1.00 31.23  ? 279 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 9.575   -20.441 -18.436 1.00 43.56  ? 280 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? -11.240 -16.073 -3.896  1.00 59.18  ? 281 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? 21.345  -16.760 -3.417  1.00 34.48  ? 282 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 17.048  -18.280 -9.611  1.00 51.71  ? 283 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 8.955   -1.747  -0.547  1.00 77.27  ? 284 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? 22.330  -16.609 -0.417  1.00 44.49  ? 285 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? -0.630  -20.956 10.862  1.00 70.61  ? 286 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? -4.019  -26.784 7.369   1.00 62.34  ? 287 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? 9.212   -27.617 -7.724  1.00 66.81  ? 288 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? -4.302  -7.623  -10.930 1.00 62.73  ? 289 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? -8.217  -19.808 -3.444  1.00 50.07  ? 290 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? -3.861  -7.881  10.625  1.00 50.80  ? 291 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 8.731   -9.149  -13.855 1.00 39.11  ? 292 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 16.781  -9.991  -9.690  1.00 51.22  ? 293 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? 11.772  -20.977 10.779  1.00 49.25  ? 294 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? 1.124   -29.352 -7.252  1.00 53.58  ? 295 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? -7.312  -14.084 -9.177  1.00 51.01  ? 296 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? -1.135  -9.091  13.966  1.00 54.00  ? 297 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? 15.316  -28.251 -1.655  1.00 66.35  ? 298 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? -5.757  -23.525 -7.095  1.00 52.13  ? 299 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? -10.413 -28.037 -1.877  1.00 58.57  ? 300 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? -6.212  -22.349 6.048   1.00 55.73  ? 301 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? 11.266  -1.924  -1.740  1.00 49.25  ? 302 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? -11.311 -13.449 -2.886  1.00 51.47  ? 303 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? 4.568   -9.841  -11.306 1.00 42.73  ? 304 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? -7.138  -19.106 8.378   1.00 61.53  ? 305 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? 8.164   -8.215  4.438   1.00 39.69  ? 306 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? 7.931   -30.682 -1.998  1.00 60.87  ? 307 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? -5.295  -20.835 -8.432  1.00 55.03  ? 308 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? 4.139   -3.036  2.250   1.00 71.97  ? 309 HOH A O   1 
HETATM 2305 O O   . HOH N 5 .  ? 19.827  -22.012 -23.241 1.00 58.64  ? 201 HOH B O   1 
HETATM 2306 O O   . HOH N 5 .  ? 9.935   -11.044 -38.079 1.00 70.33  ? 202 HOH B O   1 
HETATM 2307 O O   . HOH N 5 .  ? 24.768  -8.443  -42.993 1.00 68.60  ? 203 HOH B O   1 
HETATM 2308 O O   . HOH N 5 .  ? 12.900  -25.961 -37.175 1.00 48.85  ? 204 HOH B O   1 
HETATM 2309 O O   . HOH N 5 .  ? 25.971  -4.612  -33.502 1.00 50.96  ? 205 HOH B O   1 
HETATM 2310 O O   . HOH N 5 .  ? 6.626   -12.440 -25.979 1.00 40.52  ? 206 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 27.720  -8.126  -28.858 1.00 47.46  ? 207 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 26.233  -0.320  -29.125 1.00 52.85  ? 208 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 30.851  -8.100  -30.154 1.00 56.61  ? 209 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 25.141  -5.099  -29.776 1.00 43.23  ? 210 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 24.400  -1.538  -36.332 1.00 55.19  ? 211 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 23.375  -2.279  -29.001 1.00 47.93  ? 212 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 17.621  -15.296 -20.254 1.00 42.71  ? 213 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 12.862  -4.597  -41.713 1.00 66.56  ? 214 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 30.470  -19.765 -40.223 1.00 36.11  ? 215 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 8.724   -8.840  -16.511 1.00 42.01  ? 216 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 10.240  -19.737 -43.186 1.00 57.27  ? 217 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 25.502  -5.964  -35.858 1.00 43.05  ? 218 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 20.887  -13.577 -42.557 1.00 41.61  ? 219 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 6.182   -7.472  -32.313 1.00 63.88  ? 220 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 34.745  -23.291 -30.111 1.00 61.83  ? 221 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 20.608  -10.166 -42.783 1.00 37.79  ? 222 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 12.992  -22.433 -20.761 1.00 54.23  ? 223 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 3.186   -8.837  -26.990 1.00 56.76  ? 224 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 21.864  3.635   -32.244 1.00 45.02  ? 225 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 7.571   -12.506 -38.572 1.00 56.65  ? 226 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 10.600  -18.913 -33.017 1.00 30.36  ? 227 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 27.753  -17.454 -24.899 1.00 39.91  ? 228 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 26.264  -23.003 -30.997 1.00 36.28  ? 229 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 14.390  -6.177  -41.009 1.00 45.70  ? 230 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 16.769  -19.239 -28.801 1.00 25.51  ? 231 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 19.928  -25.524 -34.033 1.00 48.19  ? 232 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 10.352  -16.690 -44.230 1.00 57.36  ? 233 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 14.517  -24.429 -40.337 1.00 47.31  ? 234 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 22.648  -23.065 -28.791 1.00 45.86  ? 235 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 27.274  -10.495 -29.154 1.00 48.81  ? 236 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 18.201  -0.426  -38.312 1.00 31.70  ? 237 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 32.580  -18.701 -42.218 1.00 46.94  ? 238 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 17.356  -19.572 -42.002 1.00 61.63  ? 239 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 4.812   -19.051 -25.730 1.00 58.26  ? 240 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 23.798  -4.200  -36.817 1.00 32.44  ? 241 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 8.505   -27.818 -38.018 1.00 62.66  ? 242 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 7.915   -18.718 -31.574 1.00 55.70  ? 243 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 20.649  -19.789 -21.869 1.00 55.99  ? 244 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 7.087   -19.055 -34.955 1.00 51.30  ? 245 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 7.280   -8.194  -20.920 1.00 50.16  ? 246 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 17.574  -3.730  -22.010 1.00 54.68  ? 247 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 20.097  -7.881  -21.282 1.00 49.57  ? 248 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 31.616  -12.160 -38.671 1.00 59.82  ? 249 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 1.643   -12.858 -28.412 1.00 55.76  ? 250 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 20.867  -25.010 -29.369 1.00 58.55  ? 251 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 21.076  -6.448  -42.513 1.00 44.66  ? 252 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 31.985  -21.465 -38.137 1.00 45.77  ? 253 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 10.563  -21.765 -32.802 1.00 36.60  ? 254 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 18.505  -25.876 -28.831 1.00 47.32  ? 255 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 6.490   -20.801 -25.054 1.00 51.94  ? 256 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 19.736  -2.947  -22.856 1.00 67.72  ? 257 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 16.872  -9.521  -43.842 1.00 54.64  ? 258 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 24.915  -6.489  -42.555 1.00 52.64  ? 259 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 18.073  -15.940 -45.807 1.00 51.54  ? 260 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 23.711  -11.657 -21.791 1.00 49.96  ? 261 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 27.980  -24.660 -34.901 1.00 36.61  ? 262 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 18.429  4.519   -34.120 1.00 44.53  ? 263 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 20.344  3.857   -32.967 1.00 36.15  ? 264 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 17.592  -0.234  -25.535 1.00 61.93  ? 265 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 6.965   -23.579 -24.191 1.00 56.91  ? 266 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 12.778  -20.329 -19.749 1.00 62.25  ? 267 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 16.075  -26.093 -21.193 1.00 72.09  ? 268 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 9.800   -6.171  -40.937 1.00 46.82  ? 269 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 39.621  -13.636 -39.078 1.00 66.53  ? 270 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 15.065  -8.030  -43.015 1.00 49.96  ? 271 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 8.268   -21.424 -27.186 1.00 39.27  ? 272 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 7.396   -9.987  -18.562 1.00 45.92  ? 273 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 15.160  -21.931 -41.848 1.00 57.49  ? 274 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 28.688  -15.011 -23.236 1.00 49.77  ? 275 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 8.716   -22.535 -19.377 1.00 57.81  ? 276 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 22.384  -29.354 -35.390 1.00 58.59  ? 277 HOH B O   1 
HETATM 2382 O O   . HOH O 5 .  ? 26.360  -39.332 12.717  1.00 43.99  ? 201 HOH C O   1 
HETATM 2383 O O   . HOH O 5 .  ? 26.849  -37.917 10.054  1.00 47.75  ? 202 HOH C O   1 
HETATM 2384 O O   . HOH O 5 .  ? 19.819  -19.961 29.571  1.00 52.51  ? 203 HOH C O   1 
HETATM 2385 O O   . HOH O 5 .  ? 8.817   -36.705 18.674  1.00 60.52  ? 204 HOH C O   1 
HETATM 2386 O O   . HOH O 5 .  ? 5.780   -26.542 16.552  1.00 56.19  ? 205 HOH C O   1 
HETATM 2387 O O   . HOH O 5 .  ? 7.278   -31.493 12.273  1.00 49.98  ? 206 HOH C O   1 
HETATM 2388 O O   . HOH O 5 .  ? 19.117  -20.380 10.526  1.00 46.38  ? 207 HOH C O   1 
HETATM 2389 O O   . HOH O 5 .  ? 15.155  -21.199 12.451  1.00 46.23  ? 208 HOH C O   1 
HETATM 2390 O O   . HOH O 5 .  ? 17.618  -17.135 14.956  1.00 48.09  ? 209 HOH C O   1 
HETATM 2391 O O   . HOH O 5 .  ? 31.235  -29.755 32.070  1.00 66.88  ? 210 HOH C O   1 
HETATM 2392 O O   . HOH O 5 .  ? 19.830  -41.868 12.192  1.00 34.93  ? 211 HOH C O   1 
HETATM 2393 O O   . HOH O 5 .  ? 12.708  -31.628 8.075   1.00 38.20  ? 212 HOH C O   1 
HETATM 2394 O O   . HOH O 5 .  ? 13.854  -37.157 13.550  1.00 46.92  ? 213 HOH C O   1 
HETATM 2395 O O   . HOH O 5 .  ? 22.169  -28.461 11.010  1.00 32.08  ? 214 HOH C O   1 
HETATM 2396 O O   . HOH O 5 .  ? 9.156   -30.226 11.412  1.00 52.44  ? 215 HOH C O   1 
HETATM 2397 O O   . HOH O 5 .  ? 31.676  -33.535 25.785  1.00 47.74  ? 216 HOH C O   1 
HETATM 2398 O O   . HOH O 5 .  ? 25.591  -19.607 6.333   1.00 40.88  ? 217 HOH C O   1 
HETATM 2399 O O   . HOH O 5 .  ? 22.958  -41.708 18.508  1.00 45.38  ? 218 HOH C O   1 
HETATM 2400 O O   . HOH O 5 .  ? 27.708  -15.195 12.841  1.00 55.45  ? 219 HOH C O   1 
HETATM 2401 O O   . HOH O 5 .  ? 12.010  -28.972 27.710  1.00 68.96  ? 220 HOH C O   1 
HETATM 2402 O O   . HOH O 5 .  ? 28.002  -37.369 15.910  1.00 44.53  ? 221 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 15.538  -17.548 19.320  1.00 47.48  ? 222 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 25.151  -31.314 10.816  1.00 36.57  ? 223 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 25.571  -33.795 34.703  1.00 60.45  ? 224 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 33.280  -24.345 31.463  1.00 57.93  ? 225 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 20.739  -39.893 26.351  1.00 40.55  ? 226 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 22.010  -34.412 16.513  1.00 29.15  ? 227 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 15.343  -39.244 17.057  1.00 59.25  ? 228 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 19.068  -26.723 3.192   1.00 61.47  ? 229 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 6.955   -18.011 10.840  1.00 46.73  ? 230 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 31.301  -39.880 27.297  1.00 49.32  ? 231 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 31.698  -43.207 11.964  1.00 53.77  ? 232 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 14.105  -38.604 9.414   1.00 61.64  ? 233 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 30.194  -31.933 15.546  1.00 59.30  ? 234 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 22.950  -18.497 21.686  1.00 49.72  ? 235 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 29.694  -39.941 31.457  1.00 40.40  ? 236 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 9.127   -18.861 23.755  1.00 52.91  ? 237 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 25.568  -39.568 20.100  1.00 40.10  ? 238 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 20.075  -19.172 24.724  1.00 49.89  ? 239 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 20.906  -28.791 8.516   1.00 40.59  ? 240 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 30.772  -35.549 28.397  1.00 52.90  ? 241 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 16.422  -37.797 20.211  1.00 58.42  ? 242 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 30.496  -17.167 9.683   1.00 50.95  ? 243 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 31.379  -43.391 15.877  1.00 58.25  ? 244 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 20.913  -29.617 4.759   1.00 56.17  ? 245 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 26.092  -17.770 13.703  1.00 56.63  ? 246 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 30.203  -32.768 18.255  1.00 52.68  ? 247 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 25.646  -17.909 21.141  1.00 60.55  ? 248 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 27.577  -37.608 25.062  1.00 54.77  ? 249 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 20.322  -13.049 13.380  1.00 50.55  ? 250 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 14.562  -22.277 28.333  1.00 64.54  ? 251 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 29.978  -25.424 32.408  1.00 55.27  ? 252 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 16.637  -36.929 29.403  1.00 62.14  ? 253 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 4.740   -23.821 18.542  1.00 60.53  ? 254 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 26.013  -13.876 11.045  1.00 51.14  ? 255 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 22.172  -13.775 13.176  1.00 49.28  ? 256 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 2.383   -28.986 13.567  1.00 61.98  ? 257 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 32.152  -39.267 29.858  1.00 52.20  ? 258 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 28.521  -41.632 29.771  1.00 45.75  ? 259 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 33.499  -44.490 15.220  1.00 39.85  ? 260 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 37.383  -25.315 26.343  1.00 71.54  ? 261 HOH C O   1 
# 
