data_7HGR
# 
_entry.id   7HGR 
# 
_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   7HGR         pdb_00007hgr 10.2210/pdb7hgr/pdb 
WWPDB D_1001407453 ?            ?                   
# 
_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                        7HGR 
_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           N 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    1   ? ?    ? ? 
4 non-polymer syn '2-[4-(propan-2-yl)piperazin-1-yl]pyrimidine'      206.287   2   ? ?    ? ? 
5 water       nat water                                              18.015    310 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                 SO4   
3 1,2-ETHANEDIOL                                EDO   
4 '2-[4-(propan-2-yl)piperazin-1-yl]pyrimidine' A1AM6 
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 
A1AM6 non-polymer         . '2-[4-(propan-2-yl)piperazin-1-yl]pyrimidine' ?                 'C11 H18 N4'     206.287 
ALA   'L-peptide linking' y ALANINE                                       ?                 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                      ?                 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                    ?                 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                               ?                 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                      ?                 'C3 H7 N O2 S'   121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                                'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN   'L-peptide linking' y GLUTAMINE                                     ?                 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                               ?                 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                       ?                 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                     ?                 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                         ?                 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                    ?                 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                       ?                 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                        ?                 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                    ?                 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                 ?                 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                       ?                 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                        ?                 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                 ?                 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                     ?                 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                    ?                 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                      ?                 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                        ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 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 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AM6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AM6 
_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 A1AM6 1   103 101 A1AM6 LIG B . 
K 2 SO4   1   101 5   SO4   SO4 C . 
L 4 A1AM6 1   102 101 A1AM6 LIG C . 
M 5 HOH   1   201 307 HOH   HOH A . 
M 5 HOH   2   202 202 HOH   HOH A . 
M 5 HOH   3   203 84  HOH   HOH A . 
M 5 HOH   4   204 259 HOH   HOH A . 
M 5 HOH   5   205 370 HOH   HOH A . 
M 5 HOH   6   206 304 HOH   HOH A . 
M 5 HOH   7   207 400 HOH   HOH A . 
M 5 HOH   8   208 358 HOH   HOH A . 
M 5 HOH   9   209 66  HOH   HOH A . 
M 5 HOH   10  210 334 HOH   HOH A . 
M 5 HOH   11  211 71  HOH   HOH A . 
M 5 HOH   12  212 278 HOH   HOH A . 
M 5 HOH   13  213 55  HOH   HOH A . 
M 5 HOH   14  214 86  HOH   HOH A . 
M 5 HOH   15  215 289 HOH   HOH A . 
M 5 HOH   16  216 8   HOH   HOH A . 
M 5 HOH   17  217 26  HOH   HOH A . 
M 5 HOH   18  218 199 HOH   HOH A . 
M 5 HOH   19  219 37  HOH   HOH A . 
M 5 HOH   20  220 28  HOH   HOH A . 
M 5 HOH   21  221 167 HOH   HOH A . 
M 5 HOH   22  222 85  HOH   HOH A . 
M 5 HOH   23  223 91  HOH   HOH A . 
M 5 HOH   24  224 208 HOH   HOH A . 
M 5 HOH   25  225 95  HOH   HOH A . 
M 5 HOH   26  226 293 HOH   HOH A . 
M 5 HOH   27  227 34  HOH   HOH A . 
M 5 HOH   28  228 87  HOH   HOH A . 
M 5 HOH   29  229 139 HOH   HOH A . 
M 5 HOH   30  230 406 HOH   HOH A . 
M 5 HOH   31  231 188 HOH   HOH A . 
M 5 HOH   32  232 73  HOH   HOH A . 
M 5 HOH   33  233 357 HOH   HOH A . 
M 5 HOH   34  234 21  HOH   HOH A . 
M 5 HOH   35  235 152 HOH   HOH A . 
M 5 HOH   36  236 260 HOH   HOH A . 
M 5 HOH   37  237 267 HOH   HOH A . 
M 5 HOH   38  238 41  HOH   HOH A . 
M 5 HOH   39  239 369 HOH   HOH A . 
M 5 HOH   40  240 1   HOH   HOH A . 
M 5 HOH   41  241 12  HOH   HOH A . 
M 5 HOH   42  242 190 HOH   HOH A . 
M 5 HOH   43  243 27  HOH   HOH A . 
M 5 HOH   44  244 346 HOH   HOH A . 
M 5 HOH   45  245 179 HOH   HOH A . 
M 5 HOH   46  246 2   HOH   HOH A . 
M 5 HOH   47  247 23  HOH   HOH A . 
M 5 HOH   48  248 274 HOH   HOH A . 
M 5 HOH   49  249 32  HOH   HOH A . 
M 5 HOH   50  250 60  HOH   HOH A . 
M 5 HOH   51  251 7   HOH   HOH A . 
M 5 HOH   52  252 97  HOH   HOH A . 
M 5 HOH   53  253 211 HOH   HOH A . 
M 5 HOH   54  254 42  HOH   HOH A . 
M 5 HOH   55  255 78  HOH   HOH A . 
M 5 HOH   56  256 288 HOH   HOH A . 
M 5 HOH   57  257 111 HOH   HOH A . 
M 5 HOH   58  258 292 HOH   HOH A . 
M 5 HOH   59  259 383 HOH   HOH A . 
M 5 HOH   60  260 58  HOH   HOH A . 
M 5 HOH   61  261 99  HOH   HOH A . 
M 5 HOH   62  262 299 HOH   HOH A . 
M 5 HOH   63  263 18  HOH   HOH A . 
M 5 HOH   64  264 145 HOH   HOH A . 
M 5 HOH   65  265 300 HOH   HOH A . 
M 5 HOH   66  266 218 HOH   HOH A . 
M 5 HOH   67  267 47  HOH   HOH A . 
M 5 HOH   68  268 164 HOH   HOH A . 
M 5 HOH   69  269 297 HOH   HOH A . 
M 5 HOH   70  270 93  HOH   HOH A . 
M 5 HOH   71  271 115 HOH   HOH A . 
M 5 HOH   72  272 38  HOH   HOH A . 
M 5 HOH   73  273 222 HOH   HOH A . 
M 5 HOH   74  274 203 HOH   HOH A . 
M 5 HOH   75  275 20  HOH   HOH A . 
M 5 HOH   76  276 94  HOH   HOH A . 
M 5 HOH   77  277 77  HOH   HOH A . 
M 5 HOH   78  278 382 HOH   HOH A . 
M 5 HOH   79  279 116 HOH   HOH A . 
M 5 HOH   80  280 143 HOH   HOH A . 
M 5 HOH   81  281 131 HOH   HOH A . 
M 5 HOH   82  282 301 HOH   HOH A . 
M 5 HOH   83  283 109 HOH   HOH A . 
M 5 HOH   84  284 381 HOH   HOH A . 
M 5 HOH   85  285 373 HOH   HOH A . 
M 5 HOH   86  286 14  HOH   HOH A . 
M 5 HOH   87  287 318 HOH   HOH A . 
M 5 HOH   88  288 327 HOH   HOH A . 
M 5 HOH   89  289 16  HOH   HOH A . 
M 5 HOH   90  290 9   HOH   HOH A . 
M 5 HOH   91  291 281 HOH   HOH A . 
M 5 HOH   92  292 402 HOH   HOH A . 
M 5 HOH   93  293 165 HOH   HOH A . 
M 5 HOH   94  294 19  HOH   HOH A . 
M 5 HOH   95  295 64  HOH   HOH A . 
M 5 HOH   96  296 113 HOH   HOH A . 
M 5 HOH   97  297 75  HOH   HOH A . 
M 5 HOH   98  298 31  HOH   HOH A . 
M 5 HOH   99  299 296 HOH   HOH A . 
M 5 HOH   100 300 22  HOH   HOH A . 
M 5 HOH   101 301 376 HOH   HOH A . 
M 5 HOH   102 302 63  HOH   HOH A . 
M 5 HOH   103 303 210 HOH   HOH A . 
M 5 HOH   104 304 384 HOH   HOH A . 
M 5 HOH   105 305 108 HOH   HOH A . 
M 5 HOH   106 306 185 HOH   HOH A . 
M 5 HOH   107 307 83  HOH   HOH A . 
M 5 HOH   108 308 392 HOH   HOH A . 
M 5 HOH   109 309 219 HOH   HOH A . 
M 5 HOH   110 310 205 HOH   HOH A . 
M 5 HOH   111 311 386 HOH   HOH A . 
M 5 HOH   112 312 35  HOH   HOH A . 
M 5 HOH   113 313 283 HOH   HOH A . 
M 5 HOH   114 314 156 HOH   HOH A . 
M 5 HOH   115 315 57  HOH   HOH A . 
M 5 HOH   116 316 125 HOH   HOH A . 
M 5 HOH   117 317 394 HOH   HOH A . 
M 5 HOH   118 318 332 HOH   HOH A . 
N 5 HOH   1   201 258 HOH   HOH B . 
N 5 HOH   2   202 98  HOH   HOH B . 
N 5 HOH   3   203 247 HOH   HOH B . 
N 5 HOH   4   204 412 HOH   HOH B . 
N 5 HOH   5   205 272 HOH   HOH B . 
N 5 HOH   6   206 68  HOH   HOH B . 
N 5 HOH   7   207 123 HOH   HOH B . 
N 5 HOH   8   208 172 HOH   HOH B . 
N 5 HOH   9   209 17  HOH   HOH B . 
N 5 HOH   10  210 184 HOH   HOH B . 
N 5 HOH   11  211 315 HOH   HOH B . 
N 5 HOH   12  212 69  HOH   HOH B . 
N 5 HOH   13  213 59  HOH   HOH B . 
N 5 HOH   14  214 352 HOH   HOH B . 
N 5 HOH   15  215 390 HOH   HOH B . 
N 5 HOH   16  216 338 HOH   HOH B . 
N 5 HOH   17  217 215 HOH   HOH B . 
N 5 HOH   18  218 89  HOH   HOH B . 
N 5 HOH   19  219 280 HOH   HOH B . 
N 5 HOH   20  220 336 HOH   HOH B . 
N 5 HOH   21  221 249 HOH   HOH B . 
N 5 HOH   22  222 363 HOH   HOH B . 
N 5 HOH   23  223 385 HOH   HOH B . 
N 5 HOH   24  224 368 HOH   HOH B . 
N 5 HOH   25  225 54  HOH   HOH B . 
N 5 HOH   26  226 6   HOH   HOH B . 
N 5 HOH   27  227 137 HOH   HOH B . 
N 5 HOH   28  228 343 HOH   HOH B . 
N 5 HOH   29  229 404 HOH   HOH B . 
N 5 HOH   30  230 333 HOH   HOH B . 
N 5 HOH   31  231 329 HOH   HOH B . 
N 5 HOH   32  232 223 HOH   HOH B . 
N 5 HOH   33  233 13  HOH   HOH B . 
N 5 HOH   34  234 10  HOH   HOH B . 
N 5 HOH   35  235 365 HOH   HOH B . 
N 5 HOH   36  236 375 HOH   HOH B . 
N 5 HOH   37  237 242 HOH   HOH B . 
N 5 HOH   38  238 24  HOH   HOH B . 
N 5 HOH   39  239 79  HOH   HOH B . 
N 5 HOH   40  240 5   HOH   HOH B . 
N 5 HOH   41  241 224 HOH   HOH B . 
N 5 HOH   42  242 261 HOH   HOH B . 
N 5 HOH   43  243 320 HOH   HOH B . 
N 5 HOH   44  244 337 HOH   HOH B . 
N 5 HOH   45  245 119 HOH   HOH B . 
N 5 HOH   46  246 168 HOH   HOH B . 
N 5 HOH   47  247 360 HOH   HOH B . 
N 5 HOH   48  248 25  HOH   HOH B . 
N 5 HOH   49  249 157 HOH   HOH B . 
N 5 HOH   50  250 96  HOH   HOH B . 
N 5 HOH   51  251 182 HOH   HOH B . 
N 5 HOH   52  252 150 HOH   HOH B . 
N 5 HOH   53  253 120 HOH   HOH B . 
N 5 HOH   54  254 340 HOH   HOH B . 
N 5 HOH   55  255 169 HOH   HOH B . 
N 5 HOH   56  256 74  HOH   HOH B . 
N 5 HOH   57  257 61  HOH   HOH B . 
N 5 HOH   58  258 175 HOH   HOH B . 
N 5 HOH   59  259 367 HOH   HOH B . 
N 5 HOH   60  260 76  HOH   HOH B . 
N 5 HOH   61  261 341 HOH   HOH B . 
N 5 HOH   62  262 217 HOH   HOH B . 
N 5 HOH   63  263 405 HOH   HOH B . 
N 5 HOH   64  264 153 HOH   HOH B . 
N 5 HOH   65  265 101 HOH   HOH B . 
N 5 HOH   66  266 36  HOH   HOH B . 
N 5 HOH   67  267 117 HOH   HOH B . 
N 5 HOH   68  268 374 HOH   HOH B . 
N 5 HOH   69  269 44  HOH   HOH B . 
N 5 HOH   70  270 413 HOH   HOH B . 
N 5 HOH   71  271 197 HOH   HOH B . 
N 5 HOH   72  272 403 HOH   HOH B . 
N 5 HOH   73  273 214 HOH   HOH B . 
N 5 HOH   74  274 378 HOH   HOH B . 
N 5 HOH   75  275 104 HOH   HOH B . 
N 5 HOH   76  276 72  HOH   HOH B . 
N 5 HOH   77  277 170 HOH   HOH B . 
N 5 HOH   78  278 366 HOH   HOH B . 
N 5 HOH   79  279 279 HOH   HOH B . 
N 5 HOH   80  280 177 HOH   HOH B . 
N 5 HOH   81  281 344 HOH   HOH B . 
N 5 HOH   82  282 46  HOH   HOH B . 
N 5 HOH   83  283 322 HOH   HOH B . 
N 5 HOH   84  284 389 HOH   HOH B . 
N 5 HOH   85  285 303 HOH   HOH B . 
N 5 HOH   86  286 335 HOH   HOH B . 
N 5 HOH   87  287 201 HOH   HOH B . 
N 5 HOH   88  288 163 HOH   HOH B . 
N 5 HOH   89  289 377 HOH   HOH B . 
N 5 HOH   90  290 291 HOH   HOH B . 
N 5 HOH   91  291 316 HOH   HOH B . 
N 5 HOH   92  292 342 HOH   HOH B . 
N 5 HOH   93  293 160 HOH   HOH B . 
N 5 HOH   94  294 339 HOH   HOH B . 
N 5 HOH   95  295 345 HOH   HOH B . 
N 5 HOH   96  296 314 HOH   HOH B . 
N 5 HOH   97  297 107 HOH   HOH B . 
N 5 HOH   98  298 312 HOH   HOH B . 
N 5 HOH   99  299 411 HOH   HOH B . 
O 5 HOH   1   201 356 HOH   HOH C . 
O 5 HOH   2   202 380 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   205 226 HOH   HOH C . 
O 5 HOH   6   206 391 HOH   HOH C . 
O 5 HOH   7   207 321 HOH   HOH C . 
O 5 HOH   8   208 309 HOH   HOH C . 
O 5 HOH   9   209 330 HOH   HOH C . 
O 5 HOH   10  210 118 HOH   HOH C . 
O 5 HOH   11  211 254 HOH   HOH C . 
O 5 HOH   12  212 395 HOH   HOH C . 
O 5 HOH   13  213 173 HOH   HOH C . 
O 5 HOH   14  214 271 HOH   HOH C . 
O 5 HOH   15  215 56  HOH   HOH C . 
O 5 HOH   16  216 317 HOH   HOH C . 
O 5 HOH   17  217 372 HOH   HOH C . 
O 5 HOH   18  218 90  HOH   HOH C . 
O 5 HOH   19  219 134 HOH   HOH C . 
O 5 HOH   20  220 132 HOH   HOH C . 
O 5 HOH   21  221 350 HOH   HOH C . 
O 5 HOH   22  222 151 HOH   HOH C . 
O 5 HOH   23  223 387 HOH   HOH C . 
O 5 HOH   24  224 53  HOH   HOH C . 
O 5 HOH   25  225 284 HOH   HOH C . 
O 5 HOH   26  226 353 HOH   HOH C . 
O 5 HOH   27  227 49  HOH   HOH C . 
O 5 HOH   28  228 189 HOH   HOH C . 
O 5 HOH   29  229 126 HOH   HOH C . 
O 5 HOH   30  230 15  HOH   HOH C . 
O 5 HOH   31  231 142 HOH   HOH C . 
O 5 HOH   32  232 102 HOH   HOH C . 
O 5 HOH   33  233 269 HOH   HOH C . 
O 5 HOH   34  234 408 HOH   HOH C . 
O 5 HOH   35  235 4   HOH   HOH C . 
O 5 HOH   36  236 48  HOH   HOH C . 
O 5 HOH   37  237 349 HOH   HOH C . 
O 5 HOH   38  238 148 HOH   HOH C . 
O 5 HOH   39  239 275 HOH   HOH C . 
O 5 HOH   40  240 295 HOH   HOH C . 
O 5 HOH   41  241 149 HOH   HOH C . 
O 5 HOH   42  242 45  HOH   HOH C . 
O 5 HOH   43  243 82  HOH   HOH C . 
O 5 HOH   44  244 290 HOH   HOH C . 
O 5 HOH   45  245 371 HOH   HOH C . 
O 5 HOH   46  246 362 HOH   HOH C . 
O 5 HOH   47  247 325 HOH   HOH C . 
O 5 HOH   48  248 40  HOH   HOH C . 
O 5 HOH   49  249 355 HOH   HOH C . 
O 5 HOH   50  250 407 HOH   HOH C . 
O 5 HOH   51  251 43  HOH   HOH C . 
O 5 HOH   52  252 122 HOH   HOH C . 
O 5 HOH   53  253 135 HOH   HOH C . 
O 5 HOH   54  254 209 HOH   HOH C . 
O 5 HOH   55  255 198 HOH   HOH C . 
O 5 HOH   56  256 65  HOH   HOH C . 
O 5 HOH   57  257 130 HOH   HOH C . 
O 5 HOH   58  258 294 HOH   HOH C . 
O 5 HOH   59  259 354 HOH   HOH C . 
O 5 HOH   60  260 302 HOH   HOH C . 
O 5 HOH   61  261 298 HOH   HOH C . 
O 5 HOH   62  262 398 HOH   HOH C . 
O 5 HOH   63  263 287 HOH   HOH C . 
O 5 HOH   64  264 409 HOH   HOH C . 
O 5 HOH   65  265 62  HOH   HOH C . 
O 5 HOH   66  266 67  HOH   HOH C . 
O 5 HOH   67  267 328 HOH   HOH C . 
O 5 HOH   68  268 348 HOH   HOH C . 
O 5 HOH   69  269 410 HOH   HOH C . 
O 5 HOH   70  270 171 HOH   HOH C . 
O 5 HOH   71  271 399 HOH   HOH C . 
O 5 HOH   72  272 397 HOH   HOH C . 
O 5 HOH   73  273 146 HOH   HOH C . 
O 5 HOH   74  274 305 HOH   HOH C . 
O 5 HOH   75  275 319 HOH   HOH C . 
O 5 HOH   76  276 241 HOH   HOH C . 
O 5 HOH   77  277 270 HOH   HOH C . 
O 5 HOH   78  278 401 HOH   HOH C . 
O 5 HOH   79  279 70  HOH   HOH C . 
O 5 HOH   80  280 324 HOH   HOH C . 
O 5 HOH   81  281 351 HOH   HOH C . 
O 5 HOH   82  282 103 HOH   HOH C . 
O 5 HOH   83  283 388 HOH   HOH C . 
O 5 HOH   84  284 347 HOH   HOH C . 
O 5 HOH   85  285 393 HOH   HOH C . 
O 5 HOH   86  286 310 HOH   HOH C . 
O 5 HOH   87  287 92  HOH   HOH C . 
O 5 HOH   88  288 364 HOH   HOH C . 
O 5 HOH   89  289 206 HOH   HOH C . 
O 5 HOH   90  290 396 HOH   HOH C . 
O 5 HOH   91  291 246 HOH   HOH C . 
O 5 HOH   92  292 313 HOH   HOH C . 
O 5 HOH   93  293 361 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 ASP 62 ? CG  ? A ASP 63 CG  
2  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
3  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
4  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
5  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
6  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
7  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
8  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
9  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
10 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
11 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
12 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
13 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
14 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
15 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
16 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
17 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
18 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
19 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
20 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
21 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
22 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
23 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
24 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
25 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
26 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
27 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
28 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
29 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
30 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
31 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
32 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
33 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
34 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
35 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
36 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
37 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
38 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
39 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
40 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
41 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
42 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
43 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
44 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
45 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
46 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
47 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
48 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
49 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
50 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
51 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
52 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
53 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
54 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
55 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
56 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
57 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
58 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HGR 
_cell.length_a           41.650 
_cell.length_b           42.150 
_cell.length_c           158.680 
_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                         7HGR 
_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          7HGR 
_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                     7HGR 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             52.89 
_reflns.d_resolution_high            1.41 
_reflns.number_obs                   54709 
_reflns.percent_possible_obs         99.5 
_reflns.pdbx_Rmerge_I_obs            0.055 
_reflns.pdbx_netI_over_sigmaI        12.9 
_reflns.pdbx_redundancy              5.7 
_reflns.pdbx_Rrim_I_all              0.060 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     312999 
_reflns.pdbx_chi_squared             0.92 
_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                  1.41 
_reflns_shell.d_res_low                   1.45 
_reflns_shell.number_measured_all         16021 
_reflns_shell.number_unique_obs           3849 
_reflns_shell.Rmerge_I_obs                1.510 
_reflns_shell.pdbx_chi_squared            0.67 
_reflns_shell.pdbx_redundancy             4.2 
_reflns_shell.percent_possible_obs        96.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.730 
_reflns_shell.pdbx_Rpim_I_all             0.833 
_reflns_shell.pdbx_CC_half                0.333 
_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                                 7HGR 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     51749 
_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                             40.77 
_refine.ls_d_res_high                            1.41 
_refine.ls_percent_reflns_obs                    99.37 
_refine.ls_R_factor_obs                          0.20483 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20322 
_refine.ls_R_factor_R_free                       0.23392 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  2876 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.968 
_refine.correlation_coeff_Fo_to_Fc_free          0.962 
_refine.B_iso_mean                               31.200 
_refine.aniso_B[1][1]                            0.83 
_refine.aniso_B[2][2]                            0.01 
_refine.aniso_B[3][3]                            -0.83 
_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                       0.072 
_refine.pdbx_overall_ESU_R_Free                  0.074 
_refine.overall_SU_ML                            0.065 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.747 
_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        2142 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         64 
_refine_hist.number_atoms_solvent             310 
_refine_hist.number_atoms_total               2516 
_refine_hist.d_res_high                       1.41 
_refine_hist.d_res_low                        40.77 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.010  0.012  ? 2311 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.919  1.831  ? 3145 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.080  5.000  ? 267  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       8.702  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.555 10.000 ? 309  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.139  0.200  ? 291  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.011  0.020  ? 1926 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.873  2.840  ? 1077 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.188  5.081  ? 1343 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.960  3.106  ? 1234 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.524  41.77  ? 3606 '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                       1.410 
_refine_ls_shell.d_res_low                        1.447 
_refine_ls_shell.number_reflns_R_work             3650 
_refine_ls_shell.R_factor_R_work                  0.352 
_refine_ls_shell.percent_reflns_obs               95.88 
_refine_ls_shell.R_factor_R_free                  0.342 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             189 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGR 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z104924088' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGR 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 2 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HGR A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGR B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGR 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 7HGR GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGR SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGR GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGR SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGR GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGR SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HGR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 262 ? ? O   C HOH 221 ? ? 1.22 
2  1 O   B HOH 219 ? ? O   B HOH 283 ? ? 1.49 
3  1 O   C HOH 258 ? ? O   C HOH 275 ? ? 1.71 
4  1 O   C ILE 25  ? ? O   C HOH 201 ? ? 1.76 
5  1 O2  A SO4 104 ? ? O   A HOH 201 ? ? 1.94 
6  1 O   B HOH 262 ? ? O   B HOH 268 ? ? 2.02 
7  1 OD2 C ASP 26  ? ? O   C HOH 202 ? ? 2.09 
8  1 C   C ILE 25  ? ? O   C HOH 201 ? ? 2.11 
9  1 O4  A SO4 104 ? ? O   A HOH 202 ? ? 2.12 
10 1 OD1 C ASP 26  ? ? O   C HOH 201 ? ? 2.13 
11 1 O   C HOH 272 ? ? O   C HOH 283 ? ? 2.13 
12 1 O   C HOH 273 ? ? O   C HOH 280 ? ? 2.15 
13 1 O   A PRO 37  ? ? O   A HOH 203 ? ? 2.15 
14 1 O   A GLY 17  ? ? NH1 A ARG 74  ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     221 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     296 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_654 
_pdbx_validate_symm_contact.dist              2.08 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 24 ? ? CZ A ARG 24 ? ? NH2 A ARG 24 ? ? 116.94 120.30 -3.36 0.50 N 
2 1 NE C ARG 74 ? ? CZ C ARG 74 ? ? NH1 C ARG 74 ? ? 114.71 120.30 -5.59 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -157.29 68.48  
2 1 ASN B 38 ? ? 79.10   -4.26  
3 1 ASN B 87 ? ? -159.47 59.37  
4 1 ASN C 87 ? ? -161.59 51.34  
5 1 ALA C 90 ? ? -54.74  174.99 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 VAL A 11 ? ? PHE A 12 ? ? 149.21 
2 1 VAL B 11 ? ? PHE B 12 ? ? 149.63 
# 
_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            0.094 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 318 ? 6.47 . 
2 1 O ? C HOH 293 ? 6.14 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C ASP 30 ? C ASP 31 
11 1 Y 1 C GLY 31 ? C GLY 32 
12 1 Y 1 C ALA 32 ? C ALA 33 
13 1 Y 1 C VAL 33 ? C VAL 34 
14 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 
A1AM6 N1   N N N 1   
A1AM6 N3   N Y N 2   
A1AM6 C4   C N N 3   
A1AM6 C5   C N N 4   
A1AM6 C6   C N N 5   
A1AM6 C7   C Y N 6   
A1AM6 C8   C Y N 7   
A1AM6 C10  C Y N 8   
A1AM6 N    N N N 9   
A1AM6 C    C N N 10  
A1AM6 C1   C N N 11  
A1AM6 C2   C N N 12  
A1AM6 C3   C N N 13  
A1AM6 C9   C Y N 14  
A1AM6 N2   N Y N 15  
A1AM6 H9   H N N 16  
A1AM6 H10  H N N 17  
A1AM6 H11  H N N 18  
A1AM6 H12  H N N 19  
A1AM6 H13  H N N 20  
A1AM6 H14  H N N 21  
A1AM6 H15  H N N 22  
A1AM6 H17  H N N 23  
A1AM6 H1   H N N 24  
A1AM6 H    H N N 25  
A1AM6 H2   H N N 26  
A1AM6 H3   H N N 27  
A1AM6 H4   H N N 28  
A1AM6 H5   H N N 29  
A1AM6 H6   H N N 30  
A1AM6 H7   H N N 31  
A1AM6 H8   H N N 32  
A1AM6 H16  H N N 33  
ALA   N    N N N 34  
ALA   CA   C N S 35  
ALA   C    C N N 36  
ALA   O    O N N 37  
ALA   CB   C N N 38  
ALA   OXT  O N N 39  
ALA   H    H N N 40  
ALA   H2   H N N 41  
ALA   HA   H N N 42  
ALA   HB1  H N N 43  
ALA   HB2  H N N 44  
ALA   HB3  H N N 45  
ALA   HXT  H N N 46  
ARG   N    N N N 47  
ARG   CA   C N S 48  
ARG   C    C N N 49  
ARG   O    O N N 50  
ARG   CB   C N N 51  
ARG   CG   C N N 52  
ARG   CD   C N N 53  
ARG   NE   N N N 54  
ARG   CZ   C N N 55  
ARG   NH1  N N N 56  
ARG   NH2  N N N 57  
ARG   OXT  O N N 58  
ARG   H    H N N 59  
ARG   H2   H N N 60  
ARG   HA   H N N 61  
ARG   HB2  H N N 62  
ARG   HB3  H N N 63  
ARG   HG2  H N N 64  
ARG   HG3  H N N 65  
ARG   HD2  H N N 66  
ARG   HD3  H N N 67  
ARG   HE   H N N 68  
ARG   HH11 H N N 69  
ARG   HH12 H N N 70  
ARG   HH21 H N N 71  
ARG   HH22 H N N 72  
ARG   HXT  H N N 73  
ASN   N    N N N 74  
ASN   CA   C N S 75  
ASN   C    C N N 76  
ASN   O    O N N 77  
ASN   CB   C N N 78  
ASN   CG   C N N 79  
ASN   OD1  O N N 80  
ASN   ND2  N N N 81  
ASN   OXT  O N N 82  
ASN   H    H N N 83  
ASN   H2   H N N 84  
ASN   HA   H N N 85  
ASN   HB2  H N N 86  
ASN   HB3  H N N 87  
ASN   HD21 H N N 88  
ASN   HD22 H N N 89  
ASN   HXT  H N N 90  
ASP   N    N N N 91  
ASP   CA   C N S 92  
ASP   C    C N N 93  
ASP   O    O N N 94  
ASP   CB   C N N 95  
ASP   CG   C N N 96  
ASP   OD1  O N N 97  
ASP   OD2  O N N 98  
ASP   OXT  O N N 99  
ASP   H    H N N 100 
ASP   H2   H N N 101 
ASP   HA   H N N 102 
ASP   HB2  H N N 103 
ASP   HB3  H N N 104 
ASP   HD2  H N N 105 
ASP   HXT  H N N 106 
CYS   N    N N N 107 
CYS   CA   C N R 108 
CYS   C    C N N 109 
CYS   O    O N N 110 
CYS   CB   C N N 111 
CYS   SG   S N N 112 
CYS   OXT  O N N 113 
CYS   H    H N N 114 
CYS   H2   H N N 115 
CYS   HA   H N N 116 
CYS   HB2  H N N 117 
CYS   HB3  H N N 118 
CYS   HG   H N N 119 
CYS   HXT  H N N 120 
EDO   C1   C N N 121 
EDO   O1   O N N 122 
EDO   C2   C N N 123 
EDO   O2   O N N 124 
EDO   H11  H N N 125 
EDO   H12  H N N 126 
EDO   HO1  H N N 127 
EDO   H21  H N N 128 
EDO   H22  H N N 129 
EDO   HO2  H N N 130 
GLN   N    N N N 131 
GLN   CA   C N S 132 
GLN   C    C N N 133 
GLN   O    O N N 134 
GLN   CB   C N N 135 
GLN   CG   C N N 136 
GLN   CD   C N N 137 
GLN   OE1  O N N 138 
GLN   NE2  N N N 139 
GLN   OXT  O N N 140 
GLN   H    H N N 141 
GLN   H2   H N N 142 
GLN   HA   H N N 143 
GLN   HB2  H N N 144 
GLN   HB3  H N N 145 
GLN   HG2  H N N 146 
GLN   HG3  H N N 147 
GLN   HE21 H N N 148 
GLN   HE22 H N N 149 
GLN   HXT  H N N 150 
GLU   N    N N N 151 
GLU   CA   C N S 152 
GLU   C    C N N 153 
GLU   O    O N N 154 
GLU   CB   C N N 155 
GLU   CG   C N N 156 
GLU   CD   C N N 157 
GLU   OE1  O N N 158 
GLU   OE2  O N N 159 
GLU   OXT  O N N 160 
GLU   H    H N N 161 
GLU   H2   H N N 162 
GLU   HA   H N N 163 
GLU   HB2  H N N 164 
GLU   HB3  H N N 165 
GLU   HG2  H N N 166 
GLU   HG3  H N N 167 
GLU   HE2  H N N 168 
GLU   HXT  H N N 169 
GLY   N    N N N 170 
GLY   CA   C N N 171 
GLY   C    C N N 172 
GLY   O    O N N 173 
GLY   OXT  O N N 174 
GLY   H    H N N 175 
GLY   H2   H N N 176 
GLY   HA2  H N N 177 
GLY   HA3  H N N 178 
GLY   HXT  H N N 179 
HIS   N    N N N 180 
HIS   CA   C N S 181 
HIS   C    C N N 182 
HIS   O    O N N 183 
HIS   CB   C N N 184 
HIS   CG   C Y N 185 
HIS   ND1  N Y N 186 
HIS   CD2  C Y N 187 
HIS   CE1  C Y N 188 
HIS   NE2  N Y N 189 
HIS   OXT  O N N 190 
HIS   H    H N N 191 
HIS   H2   H N N 192 
HIS   HA   H N N 193 
HIS   HB2  H N N 194 
HIS   HB3  H N N 195 
HIS   HD1  H N N 196 
HIS   HD2  H N N 197 
HIS   HE1  H N N 198 
HIS   HE2  H N N 199 
HIS   HXT  H N N 200 
HOH   O    O N N 201 
HOH   H1   H N N 202 
HOH   H2   H N N 203 
ILE   N    N N N 204 
ILE   CA   C N S 205 
ILE   C    C N N 206 
ILE   O    O N N 207 
ILE   CB   C N S 208 
ILE   CG1  C N N 209 
ILE   CG2  C N N 210 
ILE   CD1  C N N 211 
ILE   OXT  O N N 212 
ILE   H    H N N 213 
ILE   H2   H N N 214 
ILE   HA   H N N 215 
ILE   HB   H N N 216 
ILE   HG12 H N N 217 
ILE   HG13 H N N 218 
ILE   HG21 H N N 219 
ILE   HG22 H N N 220 
ILE   HG23 H N N 221 
ILE   HD11 H N N 222 
ILE   HD12 H N N 223 
ILE   HD13 H N N 224 
ILE   HXT  H N N 225 
LEU   N    N N N 226 
LEU   CA   C N S 227 
LEU   C    C N N 228 
LEU   O    O N N 229 
LEU   CB   C N N 230 
LEU   CG   C N N 231 
LEU   CD1  C N N 232 
LEU   CD2  C N N 233 
LEU   OXT  O N N 234 
LEU   H    H N N 235 
LEU   H2   H N N 236 
LEU   HA   H N N 237 
LEU   HB2  H N N 238 
LEU   HB3  H N N 239 
LEU   HG   H N N 240 
LEU   HD11 H N N 241 
LEU   HD12 H N N 242 
LEU   HD13 H N N 243 
LEU   HD21 H N N 244 
LEU   HD22 H N N 245 
LEU   HD23 H N N 246 
LEU   HXT  H N N 247 
LYS   N    N N N 248 
LYS   CA   C N S 249 
LYS   C    C N N 250 
LYS   O    O N N 251 
LYS   CB   C N N 252 
LYS   CG   C N N 253 
LYS   CD   C N N 254 
LYS   CE   C N N 255 
LYS   NZ   N N N 256 
LYS   OXT  O N N 257 
LYS   H    H N N 258 
LYS   H2   H N N 259 
LYS   HA   H N N 260 
LYS   HB2  H N N 261 
LYS   HB3  H N N 262 
LYS   HG2  H N N 263 
LYS   HG3  H N N 264 
LYS   HD2  H N N 265 
LYS   HD3  H N N 266 
LYS   HE2  H N N 267 
LYS   HE3  H N N 268 
LYS   HZ1  H N N 269 
LYS   HZ2  H N N 270 
LYS   HZ3  H N N 271 
LYS   HXT  H N N 272 
MET   N    N N N 273 
MET   CA   C N S 274 
MET   C    C N N 275 
MET   O    O N N 276 
MET   CB   C N N 277 
MET   CG   C N N 278 
MET   SD   S N N 279 
MET   CE   C N N 280 
MET   OXT  O N N 281 
MET   H    H N N 282 
MET   H2   H N N 283 
MET   HA   H N N 284 
MET   HB2  H N N 285 
MET   HB3  H N N 286 
MET   HG2  H N N 287 
MET   HG3  H N N 288 
MET   HE1  H N N 289 
MET   HE2  H N N 290 
MET   HE3  H N N 291 
MET   HXT  H N N 292 
PHE   N    N N N 293 
PHE   CA   C N S 294 
PHE   C    C N N 295 
PHE   O    O N N 296 
PHE   CB   C N N 297 
PHE   CG   C Y N 298 
PHE   CD1  C Y N 299 
PHE   CD2  C Y N 300 
PHE   CE1  C Y N 301 
PHE   CE2  C Y N 302 
PHE   CZ   C Y N 303 
PHE   OXT  O N N 304 
PHE   H    H N N 305 
PHE   H2   H N N 306 
PHE   HA   H N N 307 
PHE   HB2  H N N 308 
PHE   HB3  H N N 309 
PHE   HD1  H N N 310 
PHE   HD2  H N N 311 
PHE   HE1  H N N 312 
PHE   HE2  H N N 313 
PHE   HZ   H N N 314 
PHE   HXT  H N N 315 
PRO   N    N N N 316 
PRO   CA   C N S 317 
PRO   C    C N N 318 
PRO   O    O N N 319 
PRO   CB   C N N 320 
PRO   CG   C N N 321 
PRO   CD   C N N 322 
PRO   OXT  O N N 323 
PRO   H    H N N 324 
PRO   HA   H N N 325 
PRO   HB2  H N N 326 
PRO   HB3  H N N 327 
PRO   HG2  H N N 328 
PRO   HG3  H N N 329 
PRO   HD2  H N N 330 
PRO   HD3  H N N 331 
PRO   HXT  H N N 332 
SER   N    N N N 333 
SER   CA   C N S 334 
SER   C    C N N 335 
SER   O    O N N 336 
SER   CB   C N N 337 
SER   OG   O N N 338 
SER   OXT  O N N 339 
SER   H    H N N 340 
SER   H2   H N N 341 
SER   HA   H N N 342 
SER   HB2  H N N 343 
SER   HB3  H N N 344 
SER   HG   H N N 345 
SER   HXT  H N N 346 
SO4   S    S N N 347 
SO4   O1   O N N 348 
SO4   O2   O N N 349 
SO4   O3   O N N 350 
SO4   O4   O N N 351 
THR   N    N N N 352 
THR   CA   C N S 353 
THR   C    C N N 354 
THR   O    O N N 355 
THR   CB   C N R 356 
THR   OG1  O N N 357 
THR   CG2  C N N 358 
THR   OXT  O N N 359 
THR   H    H N N 360 
THR   H2   H N N 361 
THR   HA   H N N 362 
THR   HB   H N N 363 
THR   HG1  H N N 364 
THR   HG21 H N N 365 
THR   HG22 H N N 366 
THR   HG23 H N N 367 
THR   HXT  H N N 368 
TRP   N    N N N 369 
TRP   CA   C N S 370 
TRP   C    C N N 371 
TRP   O    O N N 372 
TRP   CB   C N N 373 
TRP   CG   C Y N 374 
TRP   CD1  C Y N 375 
TRP   CD2  C Y N 376 
TRP   NE1  N Y N 377 
TRP   CE2  C Y N 378 
TRP   CE3  C Y N 379 
TRP   CZ2  C Y N 380 
TRP   CZ3  C Y N 381 
TRP   CH2  C Y N 382 
TRP   OXT  O N N 383 
TRP   H    H N N 384 
TRP   H2   H N N 385 
TRP   HA   H N N 386 
TRP   HB2  H N N 387 
TRP   HB3  H N N 388 
TRP   HD1  H N N 389 
TRP   HE1  H N N 390 
TRP   HE3  H N N 391 
TRP   HZ2  H N N 392 
TRP   HZ3  H N N 393 
TRP   HH2  H N N 394 
TRP   HXT  H N N 395 
TYR   N    N N N 396 
TYR   CA   C N S 397 
TYR   C    C N N 398 
TYR   O    O N N 399 
TYR   CB   C N N 400 
TYR   CG   C Y N 401 
TYR   CD1  C Y N 402 
TYR   CD2  C Y N 403 
TYR   CE1  C Y N 404 
TYR   CE2  C Y N 405 
TYR   CZ   C Y N 406 
TYR   OH   O N N 407 
TYR   OXT  O N N 408 
TYR   H    H N N 409 
TYR   H2   H N N 410 
TYR   HA   H N N 411 
TYR   HB2  H N N 412 
TYR   HB3  H N N 413 
TYR   HD1  H N N 414 
TYR   HD2  H N N 415 
TYR   HE1  H N N 416 
TYR   HE2  H N N 417 
TYR   HH   H N N 418 
TYR   HXT  H N N 419 
VAL   N    N N N 420 
VAL   CA   C N S 421 
VAL   C    C N N 422 
VAL   O    O N N 423 
VAL   CB   C N N 424 
VAL   CG1  C N N 425 
VAL   CG2  C N N 426 
VAL   OXT  O N N 427 
VAL   H    H N N 428 
VAL   H2   H N N 429 
VAL   HA   H N N 430 
VAL   HB   H N N 431 
VAL   HG11 H N N 432 
VAL   HG12 H N N 433 
VAL   HG13 H N N 434 
VAL   HG21 H N N 435 
VAL   HG22 H N N 436 
VAL   HG23 H N N 437 
VAL   HXT  H N N 438 
# 
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 
A1AM6 C   C1   sing N N 1   
A1AM6 C1  C2   sing N N 2   
A1AM6 N   C1   sing N N 3   
A1AM6 N   C3   sing N N 4   
A1AM6 C3  C4   sing N N 5   
A1AM6 C4  N1   sing N N 6   
A1AM6 N1  C5   sing N N 7   
A1AM6 C5  C6   sing N N 8   
A1AM6 C6  N    sing N N 9   
A1AM6 C7  N1   sing N N 10  
A1AM6 C7  N2   doub Y N 11  
A1AM6 N2  C8   sing Y N 12  
A1AM6 C8  C9   doub Y N 13  
A1AM6 C9  C10  sing Y N 14  
A1AM6 C10 N3   doub Y N 15  
A1AM6 N3  C7   sing Y N 16  
A1AM6 C4  H9   sing N N 17  
A1AM6 C4  H10  sing N N 18  
A1AM6 C5  H11  sing N N 19  
A1AM6 C5  H12  sing N N 20  
A1AM6 C6  H13  sing N N 21  
A1AM6 C6  H14  sing N N 22  
A1AM6 C8  H15  sing N N 23  
A1AM6 C10 H17  sing N N 24  
A1AM6 C   H1   sing N N 25  
A1AM6 C   H    sing N N 26  
A1AM6 C   H2   sing N N 27  
A1AM6 C1  H3   sing N N 28  
A1AM6 C2  H4   sing N N 29  
A1AM6 C2  H5   sing N N 30  
A1AM6 C2  H6   sing N N 31  
A1AM6 C3  H7   sing N N 32  
A1AM6 C3  H8   sing N N 33  
A1AM6 C9  H16  sing N N 34  
ALA   N   CA   sing N N 35  
ALA   N   H    sing N N 36  
ALA   N   H2   sing N N 37  
ALA   CA  C    sing N N 38  
ALA   CA  CB   sing N N 39  
ALA   CA  HA   sing N N 40  
ALA   C   O    doub N N 41  
ALA   C   OXT  sing N N 42  
ALA   CB  HB1  sing N N 43  
ALA   CB  HB2  sing N N 44  
ALA   CB  HB3  sing N N 45  
ALA   OXT HXT  sing N N 46  
ARG   N   CA   sing N N 47  
ARG   N   H    sing N N 48  
ARG   N   H2   sing N N 49  
ARG   CA  C    sing N N 50  
ARG   CA  CB   sing N N 51  
ARG   CA  HA   sing N N 52  
ARG   C   O    doub N N 53  
ARG   C   OXT  sing N N 54  
ARG   CB  CG   sing N N 55  
ARG   CB  HB2  sing N N 56  
ARG   CB  HB3  sing N N 57  
ARG   CG  CD   sing N N 58  
ARG   CG  HG2  sing N N 59  
ARG   CG  HG3  sing N N 60  
ARG   CD  NE   sing N N 61  
ARG   CD  HD2  sing N N 62  
ARG   CD  HD3  sing N N 63  
ARG   NE  CZ   sing N N 64  
ARG   NE  HE   sing N N 65  
ARG   CZ  NH1  sing N N 66  
ARG   CZ  NH2  doub N N 67  
ARG   NH1 HH11 sing N N 68  
ARG   NH1 HH12 sing N N 69  
ARG   NH2 HH21 sing N N 70  
ARG   NH2 HH22 sing N N 71  
ARG   OXT HXT  sing N N 72  
ASN   N   CA   sing N N 73  
ASN   N   H    sing N N 74  
ASN   N   H2   sing N N 75  
ASN   CA  C    sing N N 76  
ASN   CA  CB   sing N N 77  
ASN   CA  HA   sing N N 78  
ASN   C   O    doub N N 79  
ASN   C   OXT  sing N N 80  
ASN   CB  CG   sing N N 81  
ASN   CB  HB2  sing N N 82  
ASN   CB  HB3  sing N N 83  
ASN   CG  OD1  doub N N 84  
ASN   CG  ND2  sing N N 85  
ASN   ND2 HD21 sing N N 86  
ASN   ND2 HD22 sing N N 87  
ASN   OXT HXT  sing N N 88  
ASP   N   CA   sing N N 89  
ASP   N   H    sing N N 90  
ASP   N   H2   sing N N 91  
ASP   CA  C    sing N N 92  
ASP   CA  CB   sing N N 93  
ASP   CA  HA   sing N N 94  
ASP   C   O    doub N N 95  
ASP   C   OXT  sing N N 96  
ASP   CB  CG   sing N N 97  
ASP   CB  HB2  sing N N 98  
ASP   CB  HB3  sing N N 99  
ASP   CG  OD1  doub N N 100 
ASP   CG  OD2  sing N N 101 
ASP   OD2 HD2  sing N N 102 
ASP   OXT HXT  sing N N 103 
CYS   N   CA   sing N N 104 
CYS   N   H    sing N N 105 
CYS   N   H2   sing N N 106 
CYS   CA  C    sing N N 107 
CYS   CA  CB   sing N N 108 
CYS   CA  HA   sing N N 109 
CYS   C   O    doub N N 110 
CYS   C   OXT  sing N N 111 
CYS   CB  SG   sing N N 112 
CYS   CB  HB2  sing N N 113 
CYS   CB  HB3  sing N N 114 
CYS   SG  HG   sing N N 115 
CYS   OXT HXT  sing N N 116 
EDO   C1  O1   sing N N 117 
EDO   C1  C2   sing N N 118 
EDO   C1  H11  sing N N 119 
EDO   C1  H12  sing N N 120 
EDO   O1  HO1  sing N N 121 
EDO   C2  O2   sing N N 122 
EDO   C2  H21  sing N N 123 
EDO   C2  H22  sing N N 124 
EDO   O2  HO2  sing N N 125 
GLN   N   CA   sing N N 126 
GLN   N   H    sing N N 127 
GLN   N   H2   sing N N 128 
GLN   CA  C    sing N N 129 
GLN   CA  CB   sing N N 130 
GLN   CA  HA   sing N N 131 
GLN   C   O    doub N N 132 
GLN   C   OXT  sing N N 133 
GLN   CB  CG   sing N N 134 
GLN   CB  HB2  sing N N 135 
GLN   CB  HB3  sing N N 136 
GLN   CG  CD   sing N N 137 
GLN   CG  HG2  sing N N 138 
GLN   CG  HG3  sing N N 139 
GLN   CD  OE1  doub N N 140 
GLN   CD  NE2  sing N N 141 
GLN   NE2 HE21 sing N N 142 
GLN   NE2 HE22 sing N N 143 
GLN   OXT HXT  sing N N 144 
GLU   N   CA   sing N N 145 
GLU   N   H    sing N N 146 
GLU   N   H2   sing N N 147 
GLU   CA  C    sing N N 148 
GLU   CA  CB   sing N N 149 
GLU   CA  HA   sing N N 150 
GLU   C   O    doub N N 151 
GLU   C   OXT  sing N N 152 
GLU   CB  CG   sing N N 153 
GLU   CB  HB2  sing N N 154 
GLU   CB  HB3  sing N N 155 
GLU   CG  CD   sing N N 156 
GLU   CG  HG2  sing N N 157 
GLU   CG  HG3  sing N N 158 
GLU   CD  OE1  doub N N 159 
GLU   CD  OE2  sing N N 160 
GLU   OE2 HE2  sing N N 161 
GLU   OXT HXT  sing N N 162 
GLY   N   CA   sing N N 163 
GLY   N   H    sing N N 164 
GLY   N   H2   sing N N 165 
GLY   CA  C    sing N N 166 
GLY   CA  HA2  sing N N 167 
GLY   CA  HA3  sing N N 168 
GLY   C   O    doub N N 169 
GLY   C   OXT  sing N N 170 
GLY   OXT HXT  sing N N 171 
HIS   N   CA   sing N N 172 
HIS   N   H    sing N N 173 
HIS   N   H2   sing N N 174 
HIS   CA  C    sing N N 175 
HIS   CA  CB   sing N N 176 
HIS   CA  HA   sing N N 177 
HIS   C   O    doub N N 178 
HIS   C   OXT  sing N N 179 
HIS   CB  CG   sing N N 180 
HIS   CB  HB2  sing N N 181 
HIS   CB  HB3  sing N N 182 
HIS   CG  ND1  sing Y N 183 
HIS   CG  CD2  doub Y N 184 
HIS   ND1 CE1  doub Y N 185 
HIS   ND1 HD1  sing N N 186 
HIS   CD2 NE2  sing Y N 187 
HIS   CD2 HD2  sing N N 188 
HIS   CE1 NE2  sing Y N 189 
HIS   CE1 HE1  sing N N 190 
HIS   NE2 HE2  sing N N 191 
HIS   OXT HXT  sing N N 192 
HOH   O   H1   sing N N 193 
HOH   O   H2   sing N N 194 
ILE   N   CA   sing N N 195 
ILE   N   H    sing N N 196 
ILE   N   H2   sing N N 197 
ILE   CA  C    sing N N 198 
ILE   CA  CB   sing N N 199 
ILE   CA  HA   sing N N 200 
ILE   C   O    doub N N 201 
ILE   C   OXT  sing N N 202 
ILE   CB  CG1  sing N N 203 
ILE   CB  CG2  sing N N 204 
ILE   CB  HB   sing N N 205 
ILE   CG1 CD1  sing N N 206 
ILE   CG1 HG12 sing N N 207 
ILE   CG1 HG13 sing N N 208 
ILE   CG2 HG21 sing N N 209 
ILE   CG2 HG22 sing N N 210 
ILE   CG2 HG23 sing N N 211 
ILE   CD1 HD11 sing N N 212 
ILE   CD1 HD12 sing N N 213 
ILE   CD1 HD13 sing N N 214 
ILE   OXT HXT  sing N N 215 
LEU   N   CA   sing N N 216 
LEU   N   H    sing N N 217 
LEU   N   H2   sing N N 218 
LEU   CA  C    sing N N 219 
LEU   CA  CB   sing N N 220 
LEU   CA  HA   sing N N 221 
LEU   C   O    doub N N 222 
LEU   C   OXT  sing N N 223 
LEU   CB  CG   sing N N 224 
LEU   CB  HB2  sing N N 225 
LEU   CB  HB3  sing N N 226 
LEU   CG  CD1  sing N N 227 
LEU   CG  CD2  sing N N 228 
LEU   CG  HG   sing N N 229 
LEU   CD1 HD11 sing N N 230 
LEU   CD1 HD12 sing N N 231 
LEU   CD1 HD13 sing N N 232 
LEU   CD2 HD21 sing N N 233 
LEU   CD2 HD22 sing N N 234 
LEU   CD2 HD23 sing N N 235 
LEU   OXT HXT  sing N N 236 
LYS   N   CA   sing N N 237 
LYS   N   H    sing N N 238 
LYS   N   H2   sing N N 239 
LYS   CA  C    sing N N 240 
LYS   CA  CB   sing N N 241 
LYS   CA  HA   sing N N 242 
LYS   C   O    doub N N 243 
LYS   C   OXT  sing N N 244 
LYS   CB  CG   sing N N 245 
LYS   CB  HB2  sing N N 246 
LYS   CB  HB3  sing N N 247 
LYS   CG  CD   sing N N 248 
LYS   CG  HG2  sing N N 249 
LYS   CG  HG3  sing N N 250 
LYS   CD  CE   sing N N 251 
LYS   CD  HD2  sing N N 252 
LYS   CD  HD3  sing N N 253 
LYS   CE  NZ   sing N N 254 
LYS   CE  HE2  sing N N 255 
LYS   CE  HE3  sing N N 256 
LYS   NZ  HZ1  sing N N 257 
LYS   NZ  HZ2  sing N N 258 
LYS   NZ  HZ3  sing N N 259 
LYS   OXT HXT  sing N N 260 
MET   N   CA   sing N N 261 
MET   N   H    sing N N 262 
MET   N   H2   sing N N 263 
MET   CA  C    sing N N 264 
MET   CA  CB   sing N N 265 
MET   CA  HA   sing N N 266 
MET   C   O    doub N N 267 
MET   C   OXT  sing N N 268 
MET   CB  CG   sing N N 269 
MET   CB  HB2  sing N N 270 
MET   CB  HB3  sing N N 271 
MET   CG  SD   sing N N 272 
MET   CG  HG2  sing N N 273 
MET   CG  HG3  sing N N 274 
MET   SD  CE   sing N N 275 
MET   CE  HE1  sing N N 276 
MET   CE  HE2  sing N N 277 
MET   CE  HE3  sing N N 278 
MET   OXT HXT  sing N N 279 
PHE   N   CA   sing N N 280 
PHE   N   H    sing N N 281 
PHE   N   H2   sing N N 282 
PHE   CA  C    sing N N 283 
PHE   CA  CB   sing N N 284 
PHE   CA  HA   sing N N 285 
PHE   C   O    doub N N 286 
PHE   C   OXT  sing N N 287 
PHE   CB  CG   sing N N 288 
PHE   CB  HB2  sing N N 289 
PHE   CB  HB3  sing N N 290 
PHE   CG  CD1  doub Y N 291 
PHE   CG  CD2  sing Y N 292 
PHE   CD1 CE1  sing Y N 293 
PHE   CD1 HD1  sing N N 294 
PHE   CD2 CE2  doub Y N 295 
PHE   CD2 HD2  sing N N 296 
PHE   CE1 CZ   doub Y N 297 
PHE   CE1 HE1  sing N N 298 
PHE   CE2 CZ   sing Y N 299 
PHE   CE2 HE2  sing N N 300 
PHE   CZ  HZ   sing N N 301 
PHE   OXT HXT  sing N N 302 
PRO   N   CA   sing N N 303 
PRO   N   CD   sing N N 304 
PRO   N   H    sing N N 305 
PRO   CA  C    sing N N 306 
PRO   CA  CB   sing N N 307 
PRO   CA  HA   sing N N 308 
PRO   C   O    doub N N 309 
PRO   C   OXT  sing N N 310 
PRO   CB  CG   sing N N 311 
PRO   CB  HB2  sing N N 312 
PRO   CB  HB3  sing N N 313 
PRO   CG  CD   sing N N 314 
PRO   CG  HG2  sing N N 315 
PRO   CG  HG3  sing N N 316 
PRO   CD  HD2  sing N N 317 
PRO   CD  HD3  sing N N 318 
PRO   OXT HXT  sing N N 319 
SER   N   CA   sing N N 320 
SER   N   H    sing N N 321 
SER   N   H2   sing N N 322 
SER   CA  C    sing N N 323 
SER   CA  CB   sing N N 324 
SER   CA  HA   sing N N 325 
SER   C   O    doub N N 326 
SER   C   OXT  sing N N 327 
SER   CB  OG   sing N N 328 
SER   CB  HB2  sing N N 329 
SER   CB  HB3  sing N N 330 
SER   OG  HG   sing N N 331 
SER   OXT HXT  sing N N 332 
SO4   S   O1   doub N N 333 
SO4   S   O2   doub N N 334 
SO4   S   O3   sing N N 335 
SO4   S   O4   sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
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                    7HGR 
_atom_sites.fract_transf_matrix[1][1]   0.024010 
_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]   0.023725 
_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]   0.006302 
_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 
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  ? 0.607   4.401   2.231   1.00 43.86  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.470  3.552   1.659   1.00 46.12  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.125   2.495   0.730   1.00 42.25  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.263   2.624   0.268   1.00 42.52  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.553  4.397   0.975   1.00 47.36  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.453  5.159   1.931   1.00 50.48  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.795  4.218   2.701   1.00 50.26  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -4.857  5.534   3.323   1.00 52.32  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.571  1.341   0.579   1.00 35.95  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? -0.141  0.241   -0.295  1.00 35.16  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.122   0.608   -1.757  1.00 30.46  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.576  1.441   -2.345  1.00 30.40  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.399  -0.720  -0.172  1.00 33.44  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.852  -0.517  1.266   1.00 38.06  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.771  0.992   1.371   1.00 37.20  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.128   -0.044  -2.355  1.00 31.55  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.296   0.042   -3.789  1.00 31.60  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 0.772   -1.266  -4.374  1.00 30.12  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.312   -2.150  -3.637  1.00 27.84  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 2.779   0.242   -4.153  1.00 35.97  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.327   1.558   -3.671  1.00 46.59  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 2.539   2.567   -3.151  1.00 52.92  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.585   2.020   -3.601  1.00 52.39  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 3.297   3.600   -2.805  1.00 48.82  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.548   3.292   -3.083  1.00 49.67  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 0.828   -1.413  -5.701  1.00 24.85  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.614   -2.717  -6.296  1.00 22.63  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.774   -3.644  -5.927  1.00 24.32  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 2.853   -3.203  -5.484  1.00 24.54  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.489   -2.582  -7.809  1.00 27.31  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.484   -4.930  -6.001  1.00 22.06  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.511   -5.935  -5.809  1.00 21.17  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.620   -5.753  -6.840  1.00 22.82  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.378   -5.388  -8.000  1.00 25.61  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 1.955   -7.354  -5.944  1.00 20.60  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.146   -7.703  -4.695  1.00 22.26  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 1.786   -7.939  -3.476  1.00 20.63  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? -0.231  -7.908  -4.786  1.00 21.59  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.056   -8.272  -2.318  1.00 20.15  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.930  -8.257  -3.635  1.00 20.25  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? -0.310  -8.443  -2.442  1.00 21.05  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 4.856   -6.007  -6.376  1.00 18.86  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 5.972   -6.000  -7.317  1.00 19.13  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 6.891   -7.185  -7.007  1.00 18.80  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 6.856   -7.766  -5.923  1.00 19.25  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.775   -4.703  -7.106  1.00 22.67  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.392   -4.553  -5.730  1.00 23.93  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 8.015   -3.181  -5.377  1.00 27.48  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.575   -3.178  -3.959  1.00 28.48  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.612   -3.303  -2.863  1.00 29.71  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 7.803   -7.566  -7.923  1.00 19.74  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.718   -8.677  -7.691  1.00 20.21  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.519   -8.407  -6.419  1.00 17.93  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 9.977   -7.296  -6.154  1.00 19.73  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.622   -8.696  -8.941  1.00 21.00  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.675   -8.132  -9.982  1.00 24.39  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 7.905   -7.000  -9.293  1.00 23.10  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 9.677   -9.472  -5.625  1.00 17.72  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.417  -9.397  -4.367  1.00 17.35  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.482   -9.247  -3.161  1.00 17.82  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 9.864   -9.526  -2.032  1.00 18.78  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.222   -8.821  -3.369  1.00 16.42  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.318   -8.754  -2.229  1.00 16.70  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.067   -10.149 -1.634  1.00 15.80  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 6.913   -11.134 -2.343  1.00 16.48  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 5.990   -8.127  -2.654  1.00 16.09  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 6.010   -6.629  -2.890  1.00 19.61  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 6.962   -5.956  -2.444  1.00 21.98  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.009   -6.156  -3.482  1.00 21.49  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 6.942   -10.184 -0.300  1.00 16.28  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 6.772   -11.432 0.436   1.00 14.91  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.299   -11.514 0.863   1.00 15.63  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 4.700   -10.513 1.283   1.00 17.92  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 7.739   -11.465 1.636   1.00 16.47  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.213   -11.227 1.269   1.00 17.50  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.058  -11.328 2.535   1.00 18.76  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.612   -12.258 0.223   1.00 17.55  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.735   -12.705 0.737   1.00 15.41  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.310   -12.919 0.968   1.00 16.36  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.086   -14.282 1.588   1.00 17.36  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 3.960   -15.152 1.631   1.00 17.29  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.512   -12.852 -0.344  1.00 14.53  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.679   -11.476 -0.981  1.00 16.82  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 2.899   -13.933 -1.341  1.00 17.15  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 1.852   -14.491 2.102   1.00 15.99  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.293   -15.826 2.099   1.00 16.33  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.320   -15.889 0.941   1.00 18.50  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.490  -14.947 0.762   1.00 18.22  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.522   -16.154 3.398   1.00 18.03  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.439   -16.196 4.604   1.00 17.70  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 1.769   -15.039 5.278   1.00 19.66  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 1.962   -17.409 5.031   1.00 20.67  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.658   -15.096 6.368   1.00 23.70  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 2.891   -17.471 6.079   1.00 21.19  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.244   -16.306 6.710   1.00 23.94  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.442   -16.966 0.160   1.00 17.66  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.344  -17.127 -1.049  1.00 17.46  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.342  -18.275 -0.839  1.00 18.41  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.972  -19.347 -0.315  1.00 20.66  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.553   -17.387 -2.251  1.00 18.50  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.602  -18.065 -1.254  1.00 18.35  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.600  -19.108 -1.028  1.00 20.22  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.949  -19.839 -2.322  1.00 21.44  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.331  -19.219 -3.300  1.00 24.04  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.848  -18.433 -0.434  1.00 20.92  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.965  -19.492 -0.070  1.00 24.03  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.534  -20.404 1.086   1.00 27.75  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.627  -21.186 1.772   1.00 29.16  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.986  -22.355 0.957   1.00 29.38  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.896  -21.189 -2.240  1.00 21.56  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.321  -22.094 -3.288  1.00 25.95  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.402  -22.973 -2.663  1.00 24.67  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.328  -23.297 -1.485  1.00 22.77  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -3.154  -23.039 -3.621  1.00 25.86  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -1.901  -22.296 -4.077  1.00 28.41  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -2.034  -21.705 -5.774  1.00 29.99  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -1.642  -23.259 -6.516  1.00 26.76  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.361  -23.358 -3.516  1.00 30.58  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.421  -24.289 -3.155  1.00 31.95  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.824  -25.535 -2.518  1.00 29.69  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.845  -26.128 -3.002  1.00 27.73  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.154  -24.639 -4.450  1.00 35.19  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.173  -25.767 -4.281  1.00 39.84  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.387 -25.536 -5.174  1.00 53.47  ? 16  LYS   A CD  1 
ATOM   125  C CE  . LYS   A 1 17 ? -11.521 -24.742 -4.548  1.00 62.06  ? 16  LYS   A CE  1 
ATOM   126  N NZ  . LYS   A 1 17 ? -11.196 -23.599 -3.678  1.00 56.09  ? 16  LYS   A NZ  1 
ATOM   127  N N   . GLY   A 1 18 ? -7.358  -25.915 -1.345  1.00 29.65  ? 17  GLY   A N   1 
ATOM   128  C CA  . GLY   A 1 18 ? -6.918  -27.163 -0.741  1.00 29.52  ? 17  GLY   A CA  1 
ATOM   129  C C   . GLY   A 1 18 ? -5.593  -27.085 0.013   1.00 31.58  ? 17  GLY   A C   1 
ATOM   130  O O   . GLY   A 1 18 ? -5.113  -28.081 0.549   1.00 35.95  ? 17  GLY   A O   1 
ATOM   131  N N   . TYR   A 1 19 ? -4.977  -25.891 0.058   1.00 27.51  ? 18  TYR   A N   1 
ATOM   132  C CA  . TYR   A 1 19 ? -3.756  -25.771 0.819   1.00 26.42  ? 18  TYR   A CA  1 
ATOM   133  C C   . TYR   A 1 19 ? -3.861  -24.621 1.799   1.00 24.47  ? 18  TYR   A C   1 
ATOM   134  O O   . TYR   A 1 19 ? -4.575  -23.661 1.529   1.00 24.70  ? 18  TYR   A O   1 
ATOM   135  C CB  . TYR   A 1 19 ? -2.594  -25.375 -0.098  1.00 28.31  ? 18  TYR   A CB  1 
ATOM   136  C CG  . TYR   A 1 19 ? -2.060  -26.437 -1.047  1.00 32.17  ? 18  TYR   A CG  1 
ATOM   137  C CD1 . TYR   A 1 19 ? -0.910  -27.146 -0.735  1.00 38.05  ? 18  TYR   A CD1 1 
ATOM   138  C CD2 . TYR   A 1 19 ? -2.679  -26.672 -2.261  1.00 31.50  ? 18  TYR   A CD2 1 
ATOM   139  C CE1 . TYR   A 1 19 ? -0.378  -28.070 -1.617  1.00 39.88  ? 18  TYR   A CE1 1 
ATOM   140  C CE2 . TYR   A 1 19 ? -2.170  -27.601 -3.158  1.00 37.32  ? 18  TYR   A CE2 1 
ATOM   141  C CZ  . TYR   A 1 19 ? -1.011  -28.295 -2.827  1.00 43.03  ? 18  TYR   A CZ  1 
ATOM   142  O OH  . TYR   A 1 19 ? -0.451  -29.228 -3.654  1.00 48.25  ? 18  TYR   A OH  1 
ATOM   143  N N   . PRO   A 1 20 ? -3.100  -24.667 2.910   1.00 26.15  ? 19  PRO   A N   1 
ATOM   144  C CA  . PRO   A 1 20 ? -3.073  -23.549 3.860   1.00 23.42  ? 19  PRO   A CA  1 
ATOM   145  C C   . PRO   A 1 20 ? -2.377  -22.350 3.168   1.00 22.01  ? 19  PRO   A C   1 
ATOM   146  O O   . PRO   A 1 20 ? -1.607  -22.551 2.225   1.00 22.07  ? 19  PRO   A O   1 
ATOM   147  C CB  . PRO   A 1 20 ? -2.273  -24.127 5.059   1.00 28.05  ? 19  PRO   A CB  1 
ATOM   148  C CG  . PRO   A 1 20 ? -1.402  -25.199 4.443   1.00 28.74  ? 19  PRO   A CG  1 
ATOM   149  C CD  . PRO   A 1 20 ? -2.199  -25.787 3.287   1.00 27.05  ? 19  PRO   A CD  1 
ATOM   150  N N   . HIS   A 1 21 ? -2.679  -21.165 3.667   1.00 21.72  ? 20  HIS   A N   1 
ATOM   151  C CA  . HIS   A 1 21 ? -1.968  -19.943 3.258   1.00 20.31  ? 20  HIS   A CA  1 
ATOM   152  C C   . HIS   A 1 21 ? -0.466  -20.203 3.369   1.00 22.85  ? 20  HIS   A C   1 
ATOM   153  O O   . HIS   A 1 21 ? 0.006   -20.631 4.417   1.00 21.11  ? 20  HIS   A O   1 
ATOM   154  C CB  . HIS   A 1 21 ? -2.392  -18.736 4.094   1.00 20.99  ? 20  HIS   A CB  1 
ATOM   155  C CG  . HIS   A 1 21 ? -3.835  -18.345 3.926   1.00 22.07  ? 20  HIS   A CG  1 
ATOM   156  N ND1 . HIS   A 1 21 ? -4.880  -19.003 4.577   1.00 27.03  ? 20  HIS   A ND1 1 
ATOM   157  C CD2 . HIS   A 1 21 ? -4.385  -17.364 3.205   1.00 23.57  ? 20  HIS   A CD2 1 
ATOM   158  C CE1 . HIS   A 1 21 ? -6.033  -18.413 4.225   1.00 24.94  ? 20  HIS   A CE1 1 
ATOM   159  N NE2 . HIS   A 1 21 ? -5.770  -17.419 3.393   1.00 26.97  ? 20  HIS   A NE2 1 
ATOM   160  N N   . TRP   A 1 22 ? 0.285   -19.964 2.257   1.00 19.97  ? 21  TRP   A N   1 
ATOM   161  C CA  . TRP   A 1 22 ? 1.595   -20.613 2.132   1.00 18.72  ? 21  TRP   A CA  1 
ATOM   162  C C   . TRP   A 1 22 ? 2.670   -19.538 1.957   1.00 18.55  ? 21  TRP   A C   1 
ATOM   163  O O   . TRP   A 1 22 ? 2.503   -18.623 1.152   1.00 18.63  ? 21  TRP   A O   1 
ATOM   164  C CB  . TRP   A 1 22 ? 1.605   -21.541 0.913   1.00 20.18  ? 21  TRP   A CB  1 
ATOM   165  C CG  . TRP   A 1 22 ? 2.702   -22.569 0.950   1.00 21.40  ? 21  TRP   A CG  1 
ATOM   166  C CD1 . TRP   A 1 22 ? 4.034   -22.349 0.767   1.00 20.77  ? 21  TRP   A CD1 1 
ATOM   167  C CD2 . TRP   A 1 22 ? 2.530   -23.952 1.287   1.00 23.16  ? 21  TRP   A CD2 1 
ATOM   168  N NE1 . TRP   A 1 22 ? 4.713   -23.549 0.867   1.00 19.87  ? 21  TRP   A NE1 1 
ATOM   169  C CE2 . TRP   A 1 22 ? 3.818   -24.532 1.233   1.00 23.03  ? 21  TRP   A CE2 1 
ATOM   170  C CE3 . TRP   A 1 22 ? 1.435   -24.768 1.600   1.00 24.52  ? 21  TRP   A CE3 1 
ATOM   171  C CZ2 . TRP   A 1 22 ? 4.042   -25.892 1.491   1.00 26.70  ? 21  TRP   A CZ2 1 
ATOM   172  C CZ3 . TRP   A 1 22 ? 1.664   -26.111 1.886   1.00 25.85  ? 21  TRP   A CZ3 1 
ATOM   173  C CH2 . TRP   A 1 22 ? 2.953   -26.667 1.828   1.00 30.31  ? 21  TRP   A CH2 1 
ATOM   174  N N   . PRO   A 1 23 ? 3.792   -19.591 2.697   1.00 17.14  ? 22  PRO   A N   1 
ATOM   175  C CA  . PRO   A 1 23 ? 4.852   -18.585 2.528   1.00 16.71  ? 22  PRO   A CA  1 
ATOM   176  C C   . PRO   A 1 23 ? 5.353   -18.563 1.072   1.00 16.07  ? 22  PRO   A C   1 
ATOM   177  O O   . PRO   A 1 23 ? 5.702   -19.588 0.494   1.00 18.34  ? 22  PRO   A O   1 
ATOM   178  C CB  . PRO   A 1 23 ? 5.940   -19.002 3.508   1.00 17.42  ? 22  PRO   A CB  1 
ATOM   179  C CG  . PRO   A 1 23 ? 5.750   -20.522 3.644   1.00 17.38  ? 22  PRO   A CG  1 
ATOM   180  C CD  . PRO   A 1 23 ? 4.173   -20.678 3.626   1.00 19.14  ? 22  PRO   A CD  1 
ATOM   181  N N   . ALA   A 1 24 ? 5.421   -17.368 0.484   1.00 14.77  ? 23  ALA   A N   1 
ATOM   182  C CA  . ALA   A 1 24 ? 5.755   -17.220 -0.924  1.00 15.27  ? 23  ALA   A CA  1 
ATOM   183  C C   . ALA   A 1 24 ? 6.281   -15.821 -1.247  1.00 15.66  ? 23  ALA   A C   1 
ATOM   184  O O   . ALA   A 1 24 ? 6.306   -14.935 -0.417  1.00 15.26  ? 23  ALA   A O   1 
ATOM   185  C CB  . ALA   A 1 24 ? 4.477   -17.522 -1.785  1.00 17.14  ? 23  ALA   A CB  1 
ATOM   186  N N   . ARG   A 1 25 ? 6.789   -15.661 -2.482  1.00 15.33  ? 24  ARG   A N   1 
ATOM   187  C CA  . ARG   A 1 25 ? 7.226   -14.358 -2.960  1.00 15.13  ? 24  ARG   A CA  1 
ATOM   188  C C   . ARG   A 1 25 ? 6.663   -14.105 -4.350  1.00 14.97  ? 24  ARG   A C   1 
ATOM   189  O O   . ARG   A 1 25 ? 6.388   -15.065 -5.085  1.00 16.66  ? 24  ARG   A O   1 
ATOM   190  C CB  . ARG   A 1 25 ? 8.754   -14.217 -2.886  1.00 15.99  ? 24  ARG   A CB  1 
ATOM   191  C CG  . ARG   A 1 25 ? 9.456   -15.117 -3.878  1.00 16.51  ? 24  ARG   A CG  1 
ATOM   192  C CD  . ARG   A 1 25 ? 10.992  -14.904 -3.783  1.00 16.70  ? 24  ARG   A CD  1 
ATOM   193  N NE  . ARG   A 1 25 ? 11.659  -15.722 -4.823  1.00 18.31  ? 24  ARG   A NE  1 
ATOM   194  C CZ  . ARG   A 1 25 ? 12.928  -16.140 -4.694  1.00 19.41  ? 24  ARG   A CZ  1 
ATOM   195  N NH1 . ARG   A 1 25 ? 13.601  -15.996 -3.580  1.00 18.92  ? 24  ARG   A NH1 1 
ATOM   196  N NH2 . ARG   A 1 25 ? 13.472  -16.733 -5.741  1.00 22.93  ? 24  ARG   A NH2 1 
ATOM   197  N N   . ILE   A 1 26 ? 6.529   -12.816 -4.696  1.00 17.24  ? 25  ILE   A N   1 
ATOM   198  C CA  . ILE   A 1 26 ? 6.326   -12.443 -6.096  1.00 17.45  ? 25  ILE   A CA  1 
ATOM   199  C C   . ILE   A 1 26 ? 7.661   -12.577 -6.803  1.00 17.95  ? 25  ILE   A C   1 
ATOM   200  O O   . ILE   A 1 26 ? 8.631   -11.928 -6.414  1.00 18.31  ? 25  ILE   A O   1 
ATOM   201  C CB  . ILE   A 1 26 ? 5.835   -10.988 -6.222  1.00 18.35  ? 25  ILE   A CB  1 
ATOM   202  C CG1 . ILE   A 1 26 ? 4.679   -10.633 -5.252  1.00 24.35  ? 25  ILE   A CG1 1 
ATOM   203  C CG2 . ILE   A 1 26 ? 5.496   -10.674 -7.684  1.00 20.12  ? 25  ILE   A CG2 1 
ATOM   204  C CD1 . ILE   A 1 26 ? 3.364   -11.306 -5.512  1.00 27.83  ? 25  ILE   A CD1 1 
ATOM   205  N N   . ASP   A 1 27 ? 7.692   -13.412 -7.839  1.00 18.28  ? 26  ASP   A N   1 
ATOM   206  C CA  . ASP   A 1 27 ? 8.932   -13.651 -8.573  1.00 20.00  ? 26  ASP   A CA  1 
ATOM   207  C C   . ASP   A 1 27 ? 9.101   -12.623 -9.681  1.00 22.84  ? 26  ASP   A C   1 
ATOM   208  O O   . ASP   A 1 27 ? 8.153   -12.009 -10.156 1.00 21.59  ? 26  ASP   A O   1 
ATOM   209  C CB  . ASP   A 1 27 ? 8.988   -15.053 -9.138  1.00 20.34  ? 26  ASP   A CB  1 
ATOM   210  C CG  . ASP   A 1 27 ? 10.021  -15.945 -8.498  1.00 19.56  ? 26  ASP   A CG  1 
ATOM   211  O OD1 . ASP   A 1 27 ? 10.632  -15.496 -7.494  1.00 25.02  ? 26  ASP   A OD1 1 
ATOM   212  O OD2 . ASP   A 1 27 ? 10.176  -17.062 -8.989  1.00 23.54  ? 26  ASP   A OD2 1 
ATOM   213  N N   . ASP   A 1 28 ? 10.361  -12.495 -10.138 1.00 25.26  ? 27  ASP   A N   1 
ATOM   214  C CA  . ASP   A 1 28 ? 10.609  -11.857 -11.412 1.00 29.32  ? 27  ASP   A CA  1 
ATOM   215  C C   . ASP   A 1 28 ? 10.307  -12.862 -12.533 1.00 27.12  ? 27  ASP   A C   1 
ATOM   216  O O   . ASP   A 1 28 ? 10.155  -14.046 -12.309 1.00 28.45  ? 27  ASP   A O   1 
ATOM   217  C CB  . ASP   A 1 28 ? 12.091  -11.508 -11.537 1.00 34.66  ? 27  ASP   A CB  1 
ATOM   218  C CG  . ASP   A 1 28 ? 12.635  -10.384 -10.658 1.00 47.26  ? 27  ASP   A CG  1 
ATOM   219  O OD1 . ASP   A 1 28 ? 12.302  -9.193  -10.909 1.00 43.45  ? 27  ASP   A OD1 1 
ATOM   220  O OD2 . ASP   A 1 28 ? 13.438  -10.704 -9.749  1.00 49.67  ? 27  ASP   A OD2 1 
ATOM   221  N N   . ILE   A 1 29 ? 10.204  -12.370 -13.759 1.00 30.96  ? 28  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 29 ? 10.113  -13.247 -14.930 1.00 25.20  ? 28  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 29 ? 11.456  -13.076 -15.631 1.00 25.50  ? 28  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 29 ? 11.830  -11.934 -15.879 1.00 27.53  ? 28  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 29 ? 9.004   -12.717 -15.827 1.00 26.06  ? 28  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 29 ? 7.642   -12.724 -15.096 1.00 29.37  ? 28  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 29 ? 8.962   -13.513 -17.141 1.00 26.38  ? 28  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 29 ? 6.689   -11.670 -15.618 1.00 31.09  ? 28  ILE   A CD1 1 
ATOM   229  N N   . ALA   A 1 30 ? 12.199  -14.177 -15.820 1.00 25.67  ? 29  ALA   A N   1 
ATOM   230  C CA  . ALA   A 1 30 ? 13.521  -14.082 -16.454 1.00 25.32  ? 29  ALA   A CA  1 
ATOM   231  C C   . ALA   A 1 30 ? 13.328  -13.730 -17.939 1.00 25.99  ? 29  ALA   A C   1 
ATOM   232  O O   . ALA   A 1 30 ? 12.302  -14.032 -18.553 1.00 26.15  ? 29  ALA   A O   1 
ATOM   233  C CB  . ALA   A 1 30 ? 14.251  -15.407 -16.307 1.00 26.68  ? 29  ALA   A CB  1 
ATOM   234  N N   . ASP   A 1 31 ? 14.288  -12.978 -18.474 1.00 23.84  ? 30  ASP   A N   1 
ATOM   235  C CA  . ASP   A 1 31 ? 14.303  -12.806 -19.922 1.00 24.03  ? 30  ASP   A CA  1 
ATOM   236  C C   . ASP   A 1 31 ? 14.179  -14.176 -20.588 1.00 22.04  ? 30  ASP   A C   1 
ATOM   237  O O   . ASP   A 1 31 ? 14.872  -15.120 -20.249 1.00 25.77  ? 30  ASP   A O   1 
ATOM   238  C CB  . ASP   A 1 31 ? 15.636  -12.164 -20.303 1.00 24.60  ? 30  ASP   A CB  1 
ATOM   239  C CG  . ASP   A 1 31 ? 15.722  -10.669 -20.075 1.00 28.51  ? 30  ASP   A CG  1 
ATOM   240  O OD1 . ASP   A 1 31 ? 14.665  -10.037 -20.036 1.00 32.86  ? 30  ASP   A OD1 1 
ATOM   241  O OD2 . ASP   A 1 31 ? 16.868  -10.166 -19.992 1.00 32.30  ? 30  ASP   A OD2 1 
ATOM   242  N N   . GLY   A 1 32 ? 13.310  -14.244 -21.601 1.00 21.83  ? 31  GLY   A N   1 
ATOM   243  C CA  . GLY   A 1 32 ? 13.109  -15.486 -22.341 1.00 21.60  ? 31  GLY   A CA  1 
ATOM   244  C C   . GLY   A 1 32 ? 12.137  -16.472 -21.704 1.00 25.55  ? 31  GLY   A C   1 
ATOM   245  O O   . GLY   A 1 32 ? 11.788  -17.457 -22.343 1.00 27.01  ? 31  GLY   A O   1 
ATOM   246  N N   . ALA   A 1 33 ? 11.738  -16.215 -20.447 1.00 25.00  ? 32  ALA   A N   1 
ATOM   247  C CA  . ALA   A 1 33 ? 10.904  -17.180 -19.734 1.00 26.94  ? 32  ALA   A CA  1 
ATOM   248  C C   . ALA   A 1 33 ? 9.421   -16.939 -20.007 1.00 26.46  ? 32  ALA   A C   1 
ATOM   249  O O   . ALA   A 1 33 ? 8.963   -15.878 -20.422 1.00 25.30  ? 32  ALA   A O   1 
ATOM   250  C CB  . ALA   A 1 33 ? 11.182  -17.055 -18.241 1.00 28.82  ? 32  ALA   A CB  1 
ATOM   251  N N   . VAL   A 1 34 ? 8.607   -17.965 -19.714 1.00 27.42  ? 33  VAL   A N   1 
ATOM   252  C CA  . VAL   A 1 34 ? 7.171   -17.814 -19.932 1.00 28.52  ? 33  VAL   A CA  1 
ATOM   253  C C   . VAL   A 1 34 ? 6.534   -16.772 -18.996 1.00 28.03  ? 33  VAL   A C   1 
ATOM   254  O O   . VAL   A 1 34 ? 6.715   -16.805 -17.779 1.00 29.71  ? 33  VAL   A O   1 
ATOM   255  C CB  . VAL   A 1 34 ? 6.587   -19.221 -19.662 1.00 29.38  ? 33  VAL   A CB  1 
ATOM   256  C CG1 . VAL   A 1 34 ? 5.060   -19.172 -19.541 1.00 33.72  ? 33  VAL   A CG1 1 
ATOM   257  C CG2 . VAL   A 1 34 ? 7.076   -20.263 -20.679 1.00 31.25  ? 33  VAL   A CG2 1 
ATOM   258  N N   . LYS   A 1 35 ? 5.779   -15.845 -19.579 1.00 28.95  ? 34  LYS   A N   1 
ATOM   259  C CA  . LYS   A 1 35 ? 5.070   -14.792 -18.845 1.00 30.55  ? 34  LYS   A CA  1 
ATOM   260  C C   . LYS   A 1 35 ? 3.745   -15.312 -18.282 1.00 33.44  ? 34  LYS   A C   1 
ATOM   261  O O   . LYS   A 1 35 ? 3.117   -16.216 -18.830 1.00 31.41  ? 34  LYS   A O   1 
ATOM   262  C CB  . LYS   A 1 35 ? 4.785   -13.535 -19.670 1.00 30.55  ? 34  LYS   A CB  1 
ATOM   263  C CG  . LYS   A 1 35 ? 6.067   -12.887 -20.233 1.00 29.27  ? 34  LYS   A CG  1 
ATOM   264  C CD  . LYS   A 1 35 ? 5.779   -11.712 -21.157 1.00 34.68  ? 34  LYS   A CD  1 
ATOM   265  C CE  . LYS   A 1 35 ? 5.265   -12.054 -22.532 1.00 34.34  ? 34  LYS   A CE  1 
ATOM   266  N NZ  . LYS   A 1 35 ? 5.121   -10.810 -23.285 1.00 37.81  ? 34  LYS   A NZ  1 
ATOM   267  N N   . PRO   A 1 36 ? 3.257   -14.731 -17.166 1.00 28.58  ? 35  PRO   A N   1 
ATOM   268  C CA  . PRO   A 1 36 ? 1.985   -15.162 -16.592 1.00 28.29  ? 35  PRO   A CA  1 
ATOM   269  C C   . PRO   A 1 36 ? 0.846   -14.675 -17.479 1.00 26.68  ? 35  PRO   A C   1 
ATOM   270  O O   . PRO   A 1 36 ? 1.002   -13.731 -18.251 1.00 30.42  ? 35  PRO   A O   1 
ATOM   271  C CB  . PRO   A 1 36 ? 1.907   -14.466 -15.212 1.00 29.11  ? 35  PRO   A CB  1 
ATOM   272  C CG  . PRO   A 1 36 ? 2.838   -13.254 -15.318 1.00 31.50  ? 35  PRO   A CG  1 
ATOM   273  C CD  . PRO   A 1 36 ? 3.861   -13.613 -16.435 1.00 30.24  ? 35  PRO   A CD  1 
ATOM   274  N N   . PRO   A 1 37 ? -0.384  -15.173 -17.256 1.00 31.35  ? 36  PRO   A N   1 
ATOM   275  C CA  . PRO   A 1 37 ? -1.574  -14.586 -17.884 1.00 34.30  ? 36  PRO   A CA  1 
ATOM   276  C C   . PRO   A 1 37 ? -1.818  -13.160 -17.411 1.00 36.98  ? 36  PRO   A C   1 
ATOM   277  O O   . PRO   A 1 37 ? -1.362  -12.797 -16.330 1.00 28.94  ? 36  PRO   A O   1 
ATOM   278  C CB  . PRO   A 1 37 ? -2.709  -15.517 -17.394 1.00 32.38  ? 36  PRO   A CB  1 
ATOM   279  C CG  . PRO   A 1 37 ? -2.027  -16.769 -16.929 1.00 35.13  ? 36  PRO   A CG  1 
ATOM   280  C CD  . PRO   A 1 37 ? -0.682  -16.328 -16.395 1.00 31.42  ? 36  PRO   A CD  1 
ATOM   281  N N   . PRO   A 1 38 ? -2.586  -12.311 -18.138 1.00 34.83  ? 37  PRO   A N   1 
ATOM   282  C CA  . PRO   A 1 38 ? -2.926  -10.965 -17.662 1.00 37.76  ? 37  PRO   A CA  1 
ATOM   283  C C   . PRO   A 1 38 ? -3.553  -10.951 -16.267 1.00 29.92  ? 37  PRO   A C   1 
ATOM   284  O O   . PRO   A 1 38 ? -4.296  -11.863 -15.923 1.00 34.04  ? 37  PRO   A O   1 
ATOM   285  C CB  . PRO   A 1 38 ? -3.921  -10.424 -18.724 1.00 39.62  ? 37  PRO   A CB  1 
ATOM   286  C CG  . PRO   A 1 38 ? -4.366  -11.653 -19.420 1.00 35.31  ? 37  PRO   A CG  1 
ATOM   287  C CD  . PRO   A 1 38 ? -3.164  -12.583 -19.471 1.00 38.97  ? 37  PRO   A CD  1 
ATOM   288  N N   . ASN   A 1 39 ? -3.192  -9.932  -15.487 1.00 35.61  ? 38  ASN   A N   1 
ATOM   289  C CA  . ASN   A 1 39 ? -3.685  -9.718  -14.143 1.00 35.71  ? 38  ASN   A CA  1 
ATOM   290  C C   . ASN   A 1 39 ? -3.203  -10.795 -13.168 1.00 30.84  ? 38  ASN   A C   1 
ATOM   291  O O   . ASN   A 1 39 ? -3.679  -10.792 -12.035 1.00 32.25  ? 38  ASN   A O   1 
ATOM   292  C CB  . ASN   A 1 39 ? -5.201  -9.543  -14.136 1.00 39.58  ? 38  ASN   A CB  1 
ATOM   293  C CG  . ASN   A 1 39 ? -5.573  -8.339  -14.970 1.00 41.69  ? 38  ASN   A CG  1 
ATOM   294  O OD1 . ASN   A 1 39 ? -5.405  -7.194  -14.518 1.00 43.77  ? 38  ASN   A OD1 1 
ATOM   295  N ND2 . ASN   A 1 39 ? -5.987  -8.584  -16.201 1.00 46.45  ? 38  ASN   A ND2 1 
ATOM   296  N N   . LYS   A 1 40 ? -2.243  -11.662 -13.572 1.00 26.92  ? 39  LYS   A N   1 
ATOM   297  C CA  . LYS   A 1 40 ? -1.719  -12.672 -12.656 1.00 21.48  ? 39  LYS   A CA  1 
ATOM   298  C C   . LYS   A 1 40 ? -0.235  -12.390 -12.433 1.00 20.74  ? 39  LYS   A C   1 
ATOM   299  O O   . LYS   A 1 40 ? 0.435   -11.762 -13.256 1.00 23.23  ? 39  LYS   A O   1 
ATOM   300  C CB  . LYS   A 1 40 ? -1.828  -14.123 -13.128 1.00 23.18  ? 39  LYS   A CB  1 
ATOM   301  C CG  . LYS   A 1 40 ? -3.237  -14.634 -13.554 1.00 27.57  ? 39  LYS   A CG  1 
ATOM   302  C CD  . LYS   A 1 40 ? -4.139  -14.297 -12.378 1.00 32.14  ? 39  LYS   A CD  1 
ATOM   303  C CE  . LYS   A 1 40 ? -5.620  -14.548 -12.566 1.00 43.96  ? 39  LYS   A CE  1 
ATOM   304  N NZ  . LYS   A 1 40 ? -5.927  -15.975 -12.501 1.00 44.99  ? 39  LYS   A NZ  1 
ATOM   305  N N   . TYR   A 1 41 ? 0.247   -12.788 -11.253 1.00 18.30  ? 40  TYR   A N   1 
ATOM   306  C CA  . TYR   A 1 41 ? 1.655   -12.668 -10.864 1.00 18.52  ? 40  TYR   A CA  1 
ATOM   307  C C   . TYR   A 1 41 ? 2.259   -14.051 -10.781 1.00 17.19  ? 40  TYR   A C   1 
ATOM   308  O O   . TYR   A 1 41 ? 1.609   -15.021 -10.415 1.00 18.66  ? 40  TYR   A O   1 
ATOM   309  C CB  . TYR   A 1 41 ? 1.778   -12.010 -9.458  1.00 18.55  ? 40  TYR   A CB  1 
ATOM   310  C CG  . TYR   A 1 41 ? 1.270   -10.580 -9.428  1.00 20.39  ? 40  TYR   A CG  1 
ATOM   311  C CD1 . TYR   A 1 41 ? -0.099  -10.339 -9.307  1.00 22.70  ? 40  TYR   A CD1 1 
ATOM   312  C CD2 . TYR   A 1 41 ? 2.116   -9.518  -9.643  1.00 22.82  ? 40  TYR   A CD2 1 
ATOM   313  C CE1 . TYR   A 1 41 ? -0.594  -9.047  -9.404  1.00 23.99  ? 40  TYR   A CE1 1 
ATOM   314  C CE2 . TYR   A 1 41 ? 1.639   -8.203  -9.657  1.00 23.42  ? 40  TYR   A CE2 1 
ATOM   315  C CZ  . TYR   A 1 41 ? 0.277   -7.989  -9.529  1.00 26.99  ? 40  TYR   A CZ  1 
ATOM   316  O OH  . TYR   A 1 41 ? -0.264  -6.737  -9.682  1.00 28.29  ? 40  TYR   A OH  1 
ATOM   317  N N   . PRO   A 1 42 ? 3.580   -14.192 -11.037 1.00 17.34  ? 41  PRO   A N   1 
ATOM   318  C CA  . PRO   A 1 42 ? 4.254   -15.473 -10.819 1.00 18.19  ? 41  PRO   A CA  1 
ATOM   319  C C   . PRO   A 1 42 ? 4.619   -15.574 -9.346  1.00 18.14  ? 41  PRO   A C   1 
ATOM   320  O O   . PRO   A 1 42 ? 5.295   -14.694 -8.821  1.00 19.30  ? 41  PRO   A O   1 
ATOM   321  C CB  . PRO   A 1 42 ? 5.527   -15.362 -11.692 1.00 18.83  ? 41  PRO   A CB  1 
ATOM   322  C CG  . PRO   A 1 42 ? 5.743   -13.902 -11.870 1.00 19.35  ? 41  PRO   A CG  1 
ATOM   323  C CD  . PRO   A 1 42 ? 4.443   -13.133 -11.562 1.00 18.93  ? 41  PRO   A CD  1 
ATOM   324  N N   . ILE   A 1 43 ? 4.075   -16.587 -8.686  1.00 17.69  ? 42  ILE   A N   1 
ATOM   325  C CA  . ILE   A 1 43 ? 4.281   -16.760 -7.254  1.00 16.67  ? 42  ILE   A CA  1 
ATOM   326  C C   . ILE   A 1 43 ? 5.230   -17.929 -7.029  1.00 18.03  ? 42  ILE   A C   1 
ATOM   327  O O   . ILE   A 1 43 ? 4.930   -19.068 -7.476  1.00 20.05  ? 42  ILE   A O   1 
ATOM   328  C CB  . ILE   A 1 43 ? 2.946   -17.048 -6.568  1.00 16.92  ? 42  ILE   A CB  1 
ATOM   329  C CG1 . ILE   A 1 43 ? 1.955   -15.913 -6.874  1.00 17.48  ? 42  ILE   A CG1 1 
ATOM   330  C CG2 . ILE   A 1 43 ? 3.195   -17.235 -5.049  1.00 17.18  ? 42  ILE   A CG2 1 
ATOM   331  C CD1 . ILE   A 1 43 ? 2.429   -14.506 -6.511  1.00 17.62  ? 42  ILE   A CD1 1 
ATOM   332  N N   . PHE   A 1 44 ? 6.355   -17.655 -6.352  1.00 17.43  ? 43  PHE   A N   1 
ATOM   333  C CA  . PHE   A 1 44 ? 7.214   -18.758 -5.983  1.00 18.03  ? 43  PHE   A CA  1 
ATOM   334  C C   . PHE   A 1 44 ? 6.931   -19.137 -4.539  1.00 17.02  ? 43  PHE   A C   1 
ATOM   335  O O   . PHE   A 1 44 ? 6.997   -18.319 -3.636  1.00 17.71  ? 43  PHE   A O   1 
ATOM   336  C CB  . PHE   A 1 44 ? 8.669   -18.294 -6.133  1.00 18.81  ? 43  PHE   A CB  1 
ATOM   337  C CG  . PHE   A 1 44 ? 9.679   -19.333 -5.683  1.00 19.48  ? 43  PHE   A CG  1 
ATOM   338  C CD1 . PHE   A 1 44 ? 10.073  -20.340 -6.557  1.00 22.08  ? 43  PHE   A CD1 1 
ATOM   339  C CD2 . PHE   A 1 44 ? 10.244  -19.253 -4.411  1.00 21.02  ? 43  PHE   A CD2 1 
ATOM   340  C CE1 . PHE   A 1 44 ? 11.026  -21.277 -6.140  1.00 24.61  ? 43  PHE   A CE1 1 
ATOM   341  C CE2 . PHE   A 1 44 ? 11.219  -20.190 -4.009  1.00 22.62  ? 43  PHE   A CE2 1 
ATOM   342  C CZ  . PHE   A 1 44 ? 11.615  -21.181 -4.893  1.00 22.63  ? 43  PHE   A CZ  1 
ATOM   343  N N   . PHE   A 1 45 ? 6.627   -20.417 -4.330  1.00 16.81  ? 44  PHE   A N   1 
ATOM   344  C CA  . PHE   A 1 45 ? 6.254   -20.946 -3.037  1.00 17.32  ? 44  PHE   A CA  1 
ATOM   345  C C   . PHE   A 1 45 ? 7.476   -21.493 -2.320  1.00 19.38  ? 44  PHE   A C   1 
ATOM   346  O O   . PHE   A 1 45 ? 8.229   -22.331 -2.882  1.00 19.75  ? 44  PHE   A O   1 
ATOM   347  C CB  . PHE   A 1 45 ? 5.209   -22.074 -3.183  1.00 18.64  ? 44  PHE   A CB  1 
ATOM   348  C CG  . PHE   A 1 45 ? 3.848   -21.596 -3.629  1.00 18.58  ? 44  PHE   A CG  1 
ATOM   349  C CD1 . PHE   A 1 45 ? 3.551   -21.398 -4.955  1.00 22.02  ? 44  PHE   A CD1 1 
ATOM   350  C CD2 . PHE   A 1 45 ? 2.877   -21.309 -2.684  1.00 20.47  ? 44  PHE   A CD2 1 
ATOM   351  C CE1 . PHE   A 1 45 ? 2.287   -20.918 -5.359  1.00 23.10  ? 44  PHE   A CE1 1 
ATOM   352  C CE2 . PHE   A 1 45 ? 1.613   -20.826 -3.077  1.00 22.42  ? 44  PHE   A CE2 1 
ATOM   353  C CZ  . PHE   A 1 45 ? 1.319   -20.641 -4.420  1.00 23.35  ? 44  PHE   A CZ  1 
ATOM   354  N N   . PHE   A 1 46 ? 7.788   -20.901 -1.165  1.00 18.17  ? 45  PHE   A N   1 
ATOM   355  C CA  . PHE   A 1 46 ? 8.961   -21.367 -0.407  1.00 18.76  ? 45  PHE   A CA  1 
ATOM   356  C C   . PHE   A 1 46 ? 8.719   -22.792 0.067   1.00 21.68  ? 45  PHE   A C   1 
ATOM   357  O O   . PHE   A 1 46 ? 7.567   -23.239 0.228   1.00 20.48  ? 45  PHE   A O   1 
ATOM   358  C CB  . PHE   A 1 46 ? 9.203   -20.421 0.777   1.00 18.17  ? 45  PHE   A CB  1 
ATOM   359  C CG  . PHE   A 1 46 ? 9.667   -19.042 0.366   1.00 16.86  ? 45  PHE   A CG  1 
ATOM   360  C CD1 . PHE   A 1 46 ? 10.930  -18.862 -0.190  1.00 16.89  ? 45  PHE   A CD1 1 
ATOM   361  C CD2 . PHE   A 1 46 ? 8.895   -17.907 0.626   1.00 17.49  ? 45  PHE   A CD2 1 
ATOM   362  C CE1 . PHE   A 1 46 ? 11.356  -17.591 -0.552  1.00 17.14  ? 45  PHE   A CE1 1 
ATOM   363  C CE2 . PHE   A 1 46 ? 9.354   -16.635 0.303   1.00 16.70  ? 45  PHE   A CE2 1 
ATOM   364  C CZ  . PHE   A 1 46 ? 10.596  -16.470 -0.307  1.00 17.23  ? 45  PHE   A CZ  1 
ATOM   365  N N   . GLY   A 1 47 ? 9.827   -23.515 0.261   1.00 21.04  ? 46  GLY   A N   1 
ATOM   366  C CA  . GLY   A 1 47 ? 9.718   -24.894 0.759   1.00 21.35  ? 46  GLY   A CA  1 
ATOM   367  C C   . GLY   A 1 47 ? 9.517   -25.908 -0.378  1.00 25.45  ? 46  GLY   A C   1 
ATOM   368  O O   . GLY   A 1 47 ? 10.395  -26.728 -0.681  1.00 27.41  ? 46  GLY   A O   1 
ATOM   369  N N   . THR   A 1 48 ? 8.388   -25.805 -1.094  1.00 21.87  ? 47  THR   A N   1 
ATOM   370  C CA  . THR   A 1 48 ? 8.085   -26.651 -2.234  1.00 23.50  ? 47  THR   A CA  1 
ATOM   371  C C   . THR   A 1 48 ? 8.852   -26.184 -3.469  1.00 24.53  ? 47  THR   A C   1 
ATOM   372  O O   . THR   A 1 48 ? 9.154   -26.985 -4.356  1.00 25.88  ? 47  THR   A O   1 
ATOM   373  C CB  . THR   A 1 48 ? 6.588   -26.754 -2.523  1.00 24.27  ? 47  THR   A CB  1 
ATOM   374  O OG1 . THR   A 1 48 ? 6.262   -25.418 -2.958  1.00 23.61  ? 47  THR   A OG1 1 
ATOM   375  C CG2 . THR   A 1 48 ? 5.789   -27.240 -1.342  1.00 26.67  ? 47  THR   A CG2 1 
ATOM   376  N N   . HIS   A 1 49 ? 9.175   -24.871 -3.538  1.00 21.51  ? 48  HIS   A N   1 
ATOM   377  C CA  . HIS   A 1 49 ? 9.888   -24.282 -4.659  1.00 22.05  ? 48  HIS   A CA  1 
ATOM   378  C C   . HIS   A 1 49 ? 9.081   -24.417 -5.957  1.00 23.07  ? 48  HIS   A C   1 
ATOM   379  O O   . HIS   A 1 49 ? 9.646   -24.373 -7.049  1.00 25.78  ? 48  HIS   A O   1 
ATOM   380  C CB  . HIS   A 1 49 ? 11.334  -24.805 -4.792  1.00 21.92  ? 48  HIS   A CB  1 
ATOM   381  C CG  . HIS   A 1 49 ? 12.063  -24.800 -3.486  1.00 24.09  ? 48  HIS   A CG  1 
ATOM   382  N ND1 . HIS   A 1 49 ? 12.877  -25.840 -3.098  1.00 28.13  ? 48  HIS   A ND1 1 
ATOM   383  C CD2 . HIS   A 1 49 ? 12.103  -23.898 -2.471  1.00 22.39  ? 48  HIS   A CD2 1 
ATOM   384  C CE1 . HIS   A 1 49 ? 13.356  -25.594 -1.883  1.00 29.97  ? 48  HIS   A CE1 1 
ATOM   385  N NE2 . HIS   A 1 49 ? 12.929  -24.383 -1.491  1.00 23.52  ? 48  HIS   A NE2 1 
ATOM   386  N N   . GLU   A 1 50 ? 7.753   -24.530 -5.817  1.00 24.54  ? 49  GLU   A N   1 
ATOM   387  C CA  . GLU   A 1 50 ? 6.825   -24.550 -6.953  1.00 25.76  ? 49  GLU   A CA  1 
ATOM   388  C C   . GLU   A 1 50 ? 6.432   -23.123 -7.384  1.00 22.67  ? 49  GLU   A C   1 
ATOM   389  O O   . GLU   A 1 50 ? 6.597   -22.160 -6.613  1.00 22.52  ? 49  GLU   A O   1 
ATOM   390  C CB  . GLU   A 1 50 ? 5.540   -25.311 -6.637  1.00 28.22  ? 49  GLU   A CB  1 
ATOM   391  C CG  . GLU   A 1 50 ? 5.787   -26.787 -6.321  1.00 37.12  ? 49  GLU   A CG  1 
ATOM   392  C CD  . GLU   A 1 50 ? 4.566   -27.581 -5.914  1.00 44.38  ? 49  GLU   A CD  1 
ATOM   393  O OE1 . GLU   A 1 50 ? 3.426   -27.123 -6.076  1.00 48.06  ? 49  GLU   A OE1 1 
ATOM   394  O OE2 . GLU   A 1 50 ? 4.803   -28.685 -5.394  1.00 53.13  ? 49  GLU   A OE2 1 
ATOM   395  N N   . THR   A 1 51 ? 6.009   -22.956 -8.648  1.00 22.73  ? 50  THR   A N   1 
ATOM   396  C CA  . THR   A 1 51 ? 5.530   -21.672 -9.133  1.00 20.55  ? 50  THR   A CA  1 
ATOM   397  C C   . THR   A 1 51 ? 4.068   -21.854 -9.535  1.00 22.56  ? 50  THR   A C   1 
ATOM   398  O O   . THR   A 1 51 ? 3.786   -22.827 -10.257 1.00 26.28  ? 50  THR   A O   1 
ATOM   399  C CB  . THR   A 1 51 ? 6.329   -21.146 -10.328 1.00 25.63  ? 50  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 51 ? 7.645   -20.788 -9.882  1.00 26.82  ? 50  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 51 ? 5.732   -19.885 -10.940 1.00 27.45  ? 50  THR   A CG2 1 
ATOM   402  N N   . ALA   A 1 52 ? 3.173   -20.924 -9.172  1.00 20.09  ? 51  ALA   A N   1 
ATOM   403  C CA  . ALA   A 1 52 ? 1.838   -20.869 -9.752  1.00 19.64  ? 51  ALA   A CA  1 
ATOM   404  C C   . ALA   A 1 52 ? 1.517   -19.407 -10.044 1.00 19.65  ? 51  ALA   A C   1 
ATOM   405  O O   . ALA   A 1 52 ? 2.221   -18.485 -9.596  1.00 22.27  ? 51  ALA   A O   1 
ATOM   406  C CB  . ALA   A 1 52 ? 0.784   -21.431 -8.797  1.00 21.27  ? 51  ALA   A CB  1 
ATOM   407  N N   . PHE   A 1 53 ? 0.457   -19.157 -10.828 1.00 20.22  ? 52  PHE   A N   1 
ATOM   408  C CA  . PHE   A 1 53 ? 0.095   -17.809 -11.187 1.00 20.08  ? 52  PHE   A CA  1 
ATOM   409  C C   . PHE   A 1 53 ? -1.161  -17.460 -10.414 1.00 23.05  ? 52  PHE   A C   1 
ATOM   410  O O   . PHE   A 1 53 ? -2.161  -18.186 -10.460 1.00 26.56  ? 52  PHE   A O   1 
ATOM   411  C CB  . PHE   A 1 53 ? -0.172  -17.691 -12.689 1.00 22.92  ? 52  PHE   A CB  1 
ATOM   412  C CG  . PHE   A 1 53 ? 0.978   -18.165 -13.539 1.00 21.84  ? 52  PHE   A CG  1 
ATOM   413  C CD1 . PHE   A 1 53 ? 2.170   -17.444 -13.539 1.00 26.78  ? 52  PHE   A CD1 1 
ATOM   414  C CD2 . PHE   A 1 53 ? 0.806   -19.184 -14.463 1.00 28.51  ? 52  PHE   A CD2 1 
ATOM   415  C CE1 . PHE   A 1 53 ? 3.243   -17.836 -14.335 1.00 32.55  ? 52  PHE   A CE1 1 
ATOM   416  C CE2 . PHE   A 1 53 ? 1.870   -19.539 -15.286 1.00 30.03  ? 52  PHE   A CE2 1 
ATOM   417  C CZ  . PHE   A 1 53 ? 3.082   -18.874 -15.229 1.00 28.33  ? 52  PHE   A CZ  1 
ATOM   418  N N   . LEU   A 1 54 ? -1.078  -16.345 -9.698  1.00 18.85  ? 53  LEU   A N   1 
ATOM   419  C CA  . LEU   A 1 54 ? -2.203  -15.970 -8.850  1.00 19.27  ? 53  LEU   A CA  1 
ATOM   420  C C   . LEU   A 1 54 ? -2.487  -14.490 -8.984  1.00 19.34  ? 53  LEU   A C   1 
ATOM   421  O O   . LEU   A 1 54 ? -1.620  -13.674 -9.314  1.00 19.36  ? 53  LEU   A O   1 
ATOM   422  C CB  . LEU   A 1 54 ? -1.863  -16.276 -7.381  1.00 21.18  ? 53  LEU   A CB  1 
ATOM   423  C CG  . LEU   A 1 54 ? -1.812  -17.739 -6.981  1.00 21.98  ? 53  LEU   A CG  1 
ATOM   424  C CD1 . LEU   A 1 54 ? -1.435  -17.808 -5.489  1.00 21.87  ? 53  LEU   A CD1 1 
ATOM   425  C CD2 . LEU   A 1 54 ? -3.243  -18.278 -7.126  1.00 26.16  ? 53  LEU   A CD2 1 
ATOM   426  N N   . GLY   A 1 55 ? -3.761  -14.131 -8.712  1.00 18.54  ? 54  GLY   A N   1 
ATOM   427  C CA  . GLY   A 1 55 ? -4.087  -12.720 -8.641  1.00 20.06  ? 54  GLY   A CA  1 
ATOM   428  C C   . GLY   A 1 55 ? -4.107  -12.234 -7.181  1.00 18.04  ? 54  GLY   A C   1 
ATOM   429  O O   . GLY   A 1 55 ? -4.055  -13.025 -6.243  1.00 17.10  ? 54  GLY   A O   1 
ATOM   430  N N   . PRO   A 1 56 ? -4.195  -10.909 -6.970  1.00 18.30  ? 55  PRO   A N   1 
ATOM   431  C CA  . PRO   A 1 56 ? -4.145  -10.306 -5.639  1.00 17.38  ? 55  PRO   A CA  1 
ATOM   432  C C   . PRO   A 1 56 ? -5.129  -10.823 -4.593  1.00 18.26  ? 55  PRO   A C   1 
ATOM   433  O O   . PRO   A 1 56 ? -4.849  -10.742 -3.407  1.00 17.76  ? 55  PRO   A O   1 
ATOM   434  C CB  . PRO   A 1 56 ? -4.360  -8.798  -5.885  1.00 18.17  ? 55  PRO   A CB  1 
ATOM   435  C CG  . PRO   A 1 56 ? -3.765  -8.617  -7.267  1.00 20.37  ? 55  PRO   A CG  1 
ATOM   436  C CD  . PRO   A 1 56 ? -4.218  -9.871  -8.025  1.00 19.26  ? 55  PRO   A CD  1 
ATOM   437  N N   . LYS   A 1 57 ? -6.283  -11.348 -5.070  1.00 19.90  ? 56  LYS   A N   1 
ATOM   438  C CA  . LYS   A 1 57 ? -7.249  -11.882 -4.108  1.00 20.05  ? 56  LYS   A CA  1 
ATOM   439  C C   . LYS   A 1 57 ? -6.685  -13.017 -3.236  1.00 18.87  ? 56  LYS   A C   1 
ATOM   440  O O   . LYS   A 1 57 ? -7.123  -13.267 -2.113  1.00 18.87  ? 56  LYS   A O   1 
ATOM   441  C CB  . LYS   A 1 57 ? -8.532  -12.422 -4.796  1.00 22.00  ? 56  LYS   A CB  1 
ATOM   442  C CG  . LYS   A 1 57 ? -8.354  -13.732 -5.545  1.00 24.47  ? 56  LYS   A CG  1 
ATOM   443  C CD  . LYS   A 1 57 ? -9.582  -14.260 -6.305  1.00 31.27  ? 56  LYS   A CD  1 
ATOM   444  C CE  . LYS   A 1 57 ? -9.468  -15.722 -6.721  1.00 29.64  ? 56  LYS   A CE  1 
ATOM   445  N NZ  . LYS   A 1 57 ? -9.568  -16.693 -5.624  1.00 36.56  ? 56  LYS   A NZ  1 
ATOM   446  N N   . ASP   A 1 58 ? -5.599  -13.670 -3.723  1.00 17.87  ? 57  ASP   A N   1 
ATOM   447  C CA  . ASP   A 1 58 ? -5.030  -14.824 -3.075  1.00 18.92  ? 57  ASP   A CA  1 
ATOM   448  C C   . ASP   A 1 58 ? -3.672  -14.460 -2.435  1.00 16.07  ? 57  ASP   A C   1 
ATOM   449  O O   . ASP   A 1 58 ? -3.006  -15.360 -1.971  1.00 19.18  ? 57  ASP   A O   1 
ATOM   450  C CB  . ASP   A 1 58 ? -4.960  -15.979 -4.075  1.00 19.25  ? 57  ASP   A CB  1 
ATOM   451  C CG  . ASP   A 1 58 ? -6.344  -16.562 -4.344  1.00 23.00  ? 57  ASP   A CG  1 
ATOM   452  O OD1 . ASP   A 1 58 ? -7.102  -16.601 -3.378  1.00 24.53  ? 57  ASP   A OD1 1 
ATOM   453  O OD2 . ASP   A 1 58 ? -6.637  -16.922 -5.501  1.00 25.63  ? 57  ASP   A OD2 1 
ATOM   454  N N   . LEU   A 1 59 ? -3.325  -13.168 -2.397  1.00 16.69  ? 58  LEU   A N   1 
ATOM   455  C CA  . LEU   A 1 59 ? -1.992  -12.740 -1.924  1.00 16.20  ? 58  LEU   A CA  1 
ATOM   456  C C   . LEU   A 1 59 ? -2.144  -11.862 -0.669  1.00 15.57  ? 58  LEU   A C   1 
ATOM   457  O O   . LEU   A 1 59 ? -2.780  -10.787 -0.706  1.00 16.96  ? 58  LEU   A O   1 
ATOM   458  C CB  . LEU   A 1 59 ? -1.270  -11.977 -3.039  1.00 16.32  ? 58  LEU   A CB  1 
ATOM   459  C CG  . LEU   A 1 59 ? -1.132  -12.732 -4.343  1.00 17.72  ? 58  LEU   A CG  1 
ATOM   460  C CD1 . LEU   A 1 59 ? -0.449  -11.915 -5.445  1.00 19.48  ? 58  LEU   A CD1 1 
ATOM   461  C CD2 . LEU   A 1 59 ? -0.407  -14.067 -4.180  1.00 18.41  ? 58  LEU   A CD2 1 
ATOM   462  N N   . PHE   A 1 60 ? -1.574  -12.326 0.451   1.00 16.13  ? 59  PHE   A N   1 
ATOM   463  C CA  . PHE   A 1 60 ? -1.662  -11.649 1.756   1.00 17.00  ? 59  PHE   A CA  1 
ATOM   464  C C   . PHE   A 1 60 ? -0.272  -11.144 2.145   1.00 17.26  ? 59  PHE   A C   1 
ATOM   465  O O   . PHE   A 1 60 ? 0.647   -11.956 2.308   1.00 18.93  ? 59  PHE   A O   1 
ATOM   466  C CB  . PHE   A 1 60 ? -2.123  -12.692 2.779   1.00 18.14  ? 59  PHE   A CB  1 
ATOM   467  C CG  . PHE   A 1 60 ? -3.561  -13.110 2.509   1.00 18.43  ? 59  PHE   A CG  1 
ATOM   468  C CD1 . PHE   A 1 60 ? -3.866  -14.015 1.518   1.00 18.99  ? 59  PHE   A CD1 1 
ATOM   469  C CD2 . PHE   A 1 60 ? -4.572  -12.595 3.303   1.00 19.97  ? 59  PHE   A CD2 1 
ATOM   470  C CE1 . PHE   A 1 60 ? -5.178  -14.399 1.240   1.00 21.12  ? 59  PHE   A CE1 1 
ATOM   471  C CE2 . PHE   A 1 60 ? -5.879  -12.987 3.011   1.00 19.77  ? 59  PHE   A CE2 1 
ATOM   472  C CZ  . PHE   A 1 60 ? -6.175  -13.875 2.023   1.00 21.77  ? 59  PHE   A CZ  1 
ATOM   473  N N   . PRO   A 1 61 ? -0.052  -9.835  2.262   1.00 17.95  ? 60  PRO   A N   1 
ATOM   474  C CA  . PRO   A 1 61 ? 1.301   -9.321  2.557   1.00 18.41  ? 60  PRO   A CA  1 
ATOM   475  C C   . PRO   A 1 61 ? 1.849   -9.957  3.841   1.00 18.79  ? 60  PRO   A C   1 
ATOM   476  O O   . PRO   A 1 61 ? 1.163   -10.153 4.851   1.00 21.23  ? 60  PRO   A O   1 
ATOM   477  C CB  . PRO   A 1 61 ? 1.106   -7.810  2.671   1.00 20.24  ? 60  PRO   A CB  1 
ATOM   478  C CG  . PRO   A 1 61 ? -0.036  -7.506  1.699   1.00 23.90  ? 60  PRO   A CG  1 
ATOM   479  C CD  . PRO   A 1 61 ? -0.971  -8.726  1.913   1.00 21.28  ? 60  PRO   A CD  1 
ATOM   480  N N   . TYR   A 1 62 ? 3.124   -10.447 3.808   1.00 20.03  ? 61  TYR   A N   1 
ATOM   481  C CA  . TYR   A 1 62 ? 3.683   -11.278 4.861   1.00 20.03  ? 61  TYR   A CA  1 
ATOM   482  C C   . TYR   A 1 62 ? 3.733   -10.617 6.252   1.00 20.05  ? 61  TYR   A C   1 
ATOM   483  O O   . TYR   A 1 62 ? 3.377   -11.292 7.207   1.00 23.52  ? 61  TYR   A O   1 
ATOM   484  C CB  . TYR   A 1 62 ? 5.094   -11.683 4.378   1.00 20.89  ? 61  TYR   A CB  1 
ATOM   485  C CG  . TYR   A 1 62 ? 5.903   -12.440 5.425   1.00 19.76  ? 61  TYR   A CG  1 
ATOM   486  C CD1 . TYR   A 1 62 ? 5.652   -13.769 5.699   1.00 20.46  ? 61  TYR   A CD1 1 
ATOM   487  C CD2 . TYR   A 1 62 ? 6.939   -11.804 6.102   1.00 23.96  ? 61  TYR   A CD2 1 
ATOM   488  C CE1 . TYR   A 1 62 ? 6.334   -14.517 6.665   1.00 22.43  ? 61  TYR   A CE1 1 
ATOM   489  C CE2 . TYR   A 1 62 ? 7.633   -12.550 7.059   1.00 23.77  ? 61  TYR   A CE2 1 
ATOM   490  C CZ  . TYR   A 1 62 ? 7.361   -13.882 7.318   1.00 22.84  ? 61  TYR   A CZ  1 
ATOM   491  O OH  . TYR   A 1 62 ? 8.053   -14.656 8.243   1.00 25.61  ? 61  TYR   A OH  1 
ATOM   492  N N   . ASP   A 1 63 ? 4.170   -9.356  6.300   1.00 22.36  ? 62  ASP   A N   1 
ATOM   493  C CA  . ASP   A 1 63 ? 4.326   -8.656  7.586   1.00 24.94  ? 62  ASP   A CA  1 
ATOM   494  C C   . ASP   A 1 63 ? 2.984   -8.617  8.343   1.00 24.05  ? 62  ASP   A C   1 
ATOM   495  O O   . ASP   A 1 63 ? 2.918   -9.090  9.484   1.00 32.96  ? 62  ASP   A O   1 
ATOM   496  C CB  . ASP   A 1 63 ? 5.015   -7.314  7.418   1.00 27.48  ? 62  ASP   A CB  1 
ATOM   497  N N   . LYS   A 1 64 ? 1.936   -8.183  7.648   1.00 26.78  ? 63  LYS   A N   1 
ATOM   498  C CA  . LYS   A 1 64 ? 0.582   -8.085  8.202   1.00 28.03  ? 63  LYS   A CA  1 
ATOM   499  C C   . LYS   A 1 64 ? 0.062   -9.448  8.654   1.00 28.00  ? 63  LYS   A C   1 
ATOM   500  O O   . LYS   A 1 64 ? -0.634  -9.526  9.669   1.00 26.98  ? 63  LYS   A O   1 
ATOM   501  C CB  . LYS   A 1 64 ? -0.368  -7.525  7.129   1.00 27.30  ? 63  LYS   A CB  1 
ATOM   502  C CG  . LYS   A 1 64 ? -1.804  -7.252  7.679   1.00 28.33  ? 63  LYS   A CG  1 
ATOM   503  C CD  . LYS   A 1 64 ? -2.718  -6.614  6.645   1.00 30.02  ? 63  LYS   A CD  1 
ATOM   504  C CE  . LYS   A 1 64 ? -3.827  -5.776  7.136   1.00 37.39  ? 63  LYS   A CE  1 
ATOM   505  N NZ  . LYS   A 1 64 ? -4.798  -6.510  7.929   1.00 39.88  ? 63  LYS   A NZ  1 
ATOM   506  N N   . SER   A 1 65 ? 0.376   -10.542 7.916   1.00 25.05  ? 64  SER   A N   1 
ATOM   507  C CA  . SER   A 1 65 ? -0.293  -11.835 8.009   1.00 24.40  ? 64  SER   A CA  1 
ATOM   508  C C   . SER   A 1 65 ? 0.469   -12.905 8.795   1.00 23.09  ? 64  SER   A C   1 
ATOM   509  O O   . SER   A 1 65 ? -0.061  -14.004 9.014   1.00 24.37  ? 64  SER   A O   1 
ATOM   510  C CB  . SER   A 1 65 ? -0.586  -12.382 6.629   1.00 25.69  ? 64  SER   A CB  1 
ATOM   511  O OG  . SER   A 1 65 ? -1.396  -11.437 5.947   1.00 31.31  ? 64  SER   A OG  1 
ATOM   512  N N   . LYS   A 1 66 ? 1.714   -12.606 9.178   1.00 23.62  ? 65  LYS   A N   1 
ATOM   513  C CA  . LYS   A 1 66 ? 2.559   -13.685 9.688   1.00 26.79  ? 65  LYS   A CA  1 
ATOM   514  C C   . LYS   A 1 66 ? 2.092   -14.215 11.045  1.00 25.76  ? 65  LYS   A C   1 
ATOM   515  O O   . LYS   A 1 66 ? 2.243   -15.395 11.350  1.00 28.99  ? 65  LYS   A O   1 
ATOM   516  C CB  . LYS   A 1 66 ? 4.049   -13.343 9.645   1.00 27.77  ? 65  LYS   A CB  1 
ATOM   517  C CG  . LYS   A 1 66 ? 4.429   -12.116 10.433  1.00 30.24  ? 65  LYS   A CG  1 
ATOM   518  C CD  . LYS   A 1 66 ? 5.938   -11.938 10.275  1.00 37.76  ? 65  LYS   A CD  1 
ATOM   519  C CE  . LYS   A 1 66 ? 6.453   -10.921 11.260  1.00 41.92  ? 65  LYS   A CE  1 
ATOM   520  N NZ  . LYS   A 1 66 ? 5.795   -9.626  11.054  1.00 50.47  ? 65  LYS   A NZ  1 
ATOM   521  N N   A ASP   A 1 67 ? 1.494   -13.331 11.850  0.50 28.33  ? 66  ASP   A N   1 
ATOM   522  N N   B ASP   A 1 67 ? 1.502   -13.333 11.855  0.50 28.02  ? 66  ASP   A N   1 
ATOM   523  C CA  A ASP   A 1 67 ? 1.029   -13.761 13.165  0.50 30.34  ? 66  ASP   A CA  1 
ATOM   524  C CA  B ASP   A 1 67 ? 1.023   -13.787 13.156  0.50 29.52  ? 66  ASP   A CA  1 
ATOM   525  C C   A ASP   A 1 67 ? -0.063  -14.824 13.021  0.50 30.45  ? 66  ASP   A C   1 
ATOM   526  C C   B ASP   A 1 67 ? -0.007  -14.898 12.963  0.50 29.76  ? 66  ASP   A C   1 
ATOM   527  O O   A ASP   A 1 67 ? -0.120  -15.769 13.796  0.50 34.18  ? 66  ASP   A O   1 
ATOM   528  O O   B ASP   A 1 67 ? 0.036   -15.927 13.632  0.50 32.40  ? 66  ASP   A O   1 
ATOM   529  C CB  A ASP   A 1 67 ? 0.688   -12.574 14.055  0.50 32.84  ? 66  ASP   A CB  1 
ATOM   530  C CB  B ASP   A 1 67 ? 0.446   -12.638 13.963  0.50 31.87  ? 66  ASP   A CB  1 
ATOM   531  C CG  A ASP   A 1 67 ? 1.877   -11.831 14.652  0.50 36.10  ? 66  ASP   A CG  1 
ATOM   532  C CG  B ASP   A 1 67 ? 0.044   -12.987 15.389  0.50 34.58  ? 66  ASP   A CG  1 
ATOM   533  O OD1 A ASP   A 1 67 ? 3.021   -12.315 14.494  0.50 38.12  ? 66  ASP   A OD1 1 
ATOM   534  O OD1 B ASP   A 1 67 ? 0.947   -13.302 16.197  0.50 41.03  ? 66  ASP   A OD1 1 
ATOM   535  O OD2 A ASP   A 1 67 ? 1.664   -10.765 15.265  0.50 39.28  ? 66  ASP   A OD2 1 
ATOM   536  O OD2 B ASP   A 1 67 ? -1.171  -12.937 15.684  0.50 41.95  ? 66  ASP   A OD2 1 
ATOM   537  N N   . LYS   A 1 68 ? -0.892  -14.704 11.977  1.00 26.98  ? 67  LYS   A N   1 
ATOM   538  C CA  . LYS   A 1 68 ? -1.975  -15.627 11.726  1.00 26.78  ? 67  LYS   A CA  1 
ATOM   539  C C   . LYS   A 1 68 ? -1.529  -16.886 11.002  1.00 25.83  ? 67  LYS   A C   1 
ATOM   540  O O   . LYS   A 1 68 ? -2.016  -17.987 11.285  1.00 29.82  ? 67  LYS   A O   1 
ATOM   541  C CB  . LYS   A 1 68 ? -3.059  -14.860 10.960  1.00 28.74  ? 67  LYS   A CB  1 
ATOM   542  C CG  . LYS   A 1 68 ? -4.333  -15.647 10.773  1.00 28.21  ? 67  LYS   A CG  1 
ATOM   543  C CD  . LYS   A 1 68 ? -5.355  -14.695 10.151  1.00 34.96  ? 67  LYS   A CD  1 
ATOM   544  C CE  . LYS   A 1 68 ? -6.636  -15.367 9.748   1.00 42.81  ? 67  LYS   A CE  1 
ATOM   545  N NZ  . LYS   A 1 68 ? -7.572  -14.323 9.286   1.00 41.36  ? 67  LYS   A NZ  1 
ATOM   546  N N   . TYR   A 1 69 ? -0.686  -16.722 9.964   1.00 25.66  ? 68  TYR   A N   1 
ATOM   547  C CA  . TYR   A 1 69 ? -0.444  -17.828 9.046   1.00 23.85  ? 68  TYR   A CA  1 
ATOM   548  C C   . TYR   A 1 69 ? 0.951   -18.457 9.205   1.00 22.32  ? 68  TYR   A C   1 
ATOM   549  O O   . TYR   A 1 69 ? 1.186   -19.498 8.595   1.00 25.22  ? 68  TYR   A O   1 
ATOM   550  C CB  . TYR   A 1 69 ? -0.580  -17.273 7.613   1.00 22.29  ? 68  TYR   A CB  1 
ATOM   551  C CG  . TYR   A 1 69 ? -1.979  -16.853 7.181   1.00 24.90  ? 68  TYR   A CG  1 
ATOM   552  C CD1 . TYR   A 1 69 ? -3.092  -17.601 7.542   1.00 25.16  ? 68  TYR   A CD1 1 
ATOM   553  C CD2 . TYR   A 1 69 ? -2.164  -15.665 6.456   1.00 24.09  ? 68  TYR   A CD2 1 
ATOM   554  C CE1 . TYR   A 1 69 ? -4.373  -17.183 7.168   1.00 25.10  ? 68  TYR   A CE1 1 
ATOM   555  C CE2 . TYR   A 1 69 ? -3.428  -15.251 6.062   1.00 26.34  ? 68  TYR   A CE2 1 
ATOM   556  C CZ  . TYR   A 1 69 ? -4.533  -16.015 6.430   1.00 27.62  ? 68  TYR   A CZ  1 
ATOM   557  O OH  . TYR   A 1 69 ? -5.781  -15.618 6.023   1.00 27.40  ? 68  TYR   A OH  1 
ATOM   558  N N   . GLY   A 1 70 ? 1.818   -17.831 9.989   1.00 25.04  ? 69  GLY   A N   1 
ATOM   559  C CA  . GLY   A 1 70 ? 3.230   -18.221 10.061  1.00 23.93  ? 69  GLY   A CA  1 
ATOM   560  C C   . GLY   A 1 70 ? 3.490   -19.220 11.199  1.00 26.93  ? 69  GLY   A C   1 
ATOM   561  O O   . GLY   A 1 70 ? 4.314   -18.969 12.046  1.00 36.27  ? 69  GLY   A O   1 
ATOM   562  N N   . LYS   A 1 71 ? 2.718   -20.291 11.233  1.00 29.94  ? 70  LYS   A N   1 
ATOM   563  C CA  . LYS   A 1 71 ? 2.859   -21.293 12.281  1.00 32.51  ? 70  LYS   A CA  1 
ATOM   564  C C   . LYS   A 1 71 ? 3.160   -22.617 11.600  1.00 30.41  ? 70  LYS   A C   1 
ATOM   565  O O   . LYS   A 1 71 ? 2.761   -22.836 10.474  1.00 30.98  ? 70  LYS   A O   1 
ATOM   566  C CB  . LYS   A 1 71 ? 1.541   -21.485 13.042  1.00 36.72  ? 70  LYS   A CB  1 
ATOM   567  C CG  . LYS   A 1 71 ? 0.971   -20.234 13.693  1.00 42.82  ? 70  LYS   A CG  1 
ATOM   568  C CD  . LYS   A 1 71 ? 1.767   -19.749 14.899  1.00 47.68  ? 70  LYS   A CD  1 
ATOM   569  N N   . PRO   A 1 72 ? 3.883   -23.564 12.246  1.00 31.00  ? 71  PRO   A N   1 
ATOM   570  C CA  . PRO   A 1 72 ? 4.096   -24.869 11.616  1.00 30.26  ? 71  PRO   A CA  1 
ATOM   571  C C   . PRO   A 1 72 ? 2.843   -25.582 11.135  1.00 31.49  ? 71  PRO   A C   1 
ATOM   572  O O   . PRO   A 1 72 ? 1.782   -25.471 11.741  1.00 36.77  ? 71  PRO   A O   1 
ATOM   573  C CB  . PRO   A 1 72 ? 4.853   -25.655 12.710  1.00 34.75  ? 71  PRO   A CB  1 
ATOM   574  C CG  . PRO   A 1 72 ? 5.587   -24.580 13.455  1.00 35.68  ? 71  PRO   A CG  1 
ATOM   575  C CD  . PRO   A 1 72 ? 4.614   -23.387 13.509  1.00 35.61  ? 71  PRO   A CD  1 
ATOM   576  N N   . ASN   A 1 73 ? 3.006   -26.330 10.059  1.00 32.24  ? 72  ASN   A N   1 
ATOM   577  C CA  . ASN   A 1 73 ? 1.946   -27.066 9.400   1.00 34.15  ? 72  ASN   A CA  1 
ATOM   578  C C   . ASN   A 1 73 ? 2.561   -28.391 8.987   1.00 40.37  ? 72  ASN   A C   1 
ATOM   579  O O   . ASN   A 1 73 ? 3.748   -28.457 8.663   1.00 41.82  ? 72  ASN   A O   1 
ATOM   580  C CB  . ASN   A 1 73 ? 1.435   -26.264 8.202   1.00 36.77  ? 72  ASN   A CB  1 
ATOM   581  C CG  . ASN   A 1 73 ? 0.116   -26.742 7.650   1.00 42.62  ? 72  ASN   A CG  1 
ATOM   582  O OD1 . ASN   A 1 73 ? 0.081   -27.652 6.815   1.00 43.74  ? 72  ASN   A OD1 1 
ATOM   583  N ND2 . ASN   A 1 73 ? -0.971  -26.098 8.050   1.00 47.64  ? 72  ASN   A ND2 1 
ATOM   584  N N   . LYS   A 1 74 ? 1.750   -29.444 9.032   1.00 42.12  ? 73  LYS   A N   1 
ATOM   585  C CA  . LYS   A 1 74 ? 2.195   -30.785 8.711   1.00 40.46  ? 73  LYS   A CA  1 
ATOM   586  C C   . LYS   A 1 74 ? 2.443   -30.954 7.215   1.00 37.48  ? 73  LYS   A C   1 
ATOM   587  O O   . LYS   A 1 74 ? 3.114   -31.905 6.800   1.00 37.73  ? 73  LYS   A O   1 
ATOM   588  C CB  . LYS   A 1 74 ? 1.178   -31.806 9.247   1.00 46.91  ? 73  LYS   A CB  1 
ATOM   589  C CG  . LYS   A 1 74 ? -0.197  -31.831 8.572   1.00 47.20  ? 73  LYS   A CG  1 
ATOM   590  N N   . ARG   A 1 75 ? 1.951   -30.024 6.383   1.00 34.14  ? 74  ARG   A N   1 
ATOM   591  C CA  . ARG   A 1 75 ? 2.049   -30.223 4.951   1.00 33.81  ? 74  ARG   A CA  1 
ATOM   592  C C   . ARG   A 1 75 ? 3.495   -30.201 4.456   1.00 32.03  ? 74  ARG   A C   1 
ATOM   593  O O   . ARG   A 1 75 ? 4.318   -29.431 4.952   1.00 31.47  ? 74  ARG   A O   1 
ATOM   594  C CB  . ARG   A 1 75 ? 1.172   -29.189 4.235   1.00 35.80  ? 74  ARG   A CB  1 
ATOM   595  C CG  . ARG   A 1 75 ? -0.300  -29.481 4.486   1.00 44.11  ? 74  ARG   A CG  1 
ATOM   596  C CD  . ARG   A 1 75 ? -0.821  -30.581 3.571   1.00 42.02  ? 74  ARG   A CD  1 
ATOM   597  N NE  . ARG   A 1 75 ? -1.743  -30.039 2.571   1.00 54.67  ? 74  ARG   A NE  1 
ATOM   598  C CZ  . ARG   A 1 75 ? -2.921  -29.484 2.858   1.00 49.77  ? 74  ARG   A CZ  1 
ATOM   599  N NH1 . ARG   A 1 75 ? -3.679  -29.036 1.882   1.00 57.07  ? 74  ARG   A NH1 1 
ATOM   600  N NH2 . ARG   A 1 75 ? -3.354  -29.401 4.111   1.00 56.95  ? 74  ARG   A NH2 1 
ATOM   601  N N   . LYS   A 1 76 ? 3.754   -31.026 3.439   1.00 31.58  ? 75  LYS   A N   1 
ATOM   602  C CA  . LYS   A 1 76 ? 5.077   -31.204 2.863   1.00 32.14  ? 75  LYS   A CA  1 
ATOM   603  C C   . LYS   A 1 76 ? 5.669   -29.859 2.421   1.00 29.69  ? 75  LYS   A C   1 
ATOM   604  O O   . LYS   A 1 76 ? 5.091   -29.177 1.575   1.00 29.22  ? 75  LYS   A O   1 
ATOM   605  C CB  . LYS   A 1 76 ? 4.994   -32.096 1.622   1.00 35.14  ? 75  LYS   A CB  1 
ATOM   606  C CG  . LYS   A 1 76 ? 6.329   -32.551 1.081   1.00 38.05  ? 75  LYS   A CG  1 
ATOM   607  C CD  . LYS   A 1 76 ? 6.309   -33.436 -0.163  1.00 40.29  ? 75  LYS   A CD  1 
ATOM   608  C CE  . LYS   A 1 76 ? 7.708   -33.809 -0.534  1.00 43.42  ? 75  LYS   A CE  1 
ATOM   609  N N   . GLY   A 1 77 ? 6.851   -29.522 2.961   1.00 28.31  ? 76  GLY   A N   1 
ATOM   610  C CA  . GLY   A 1 77 ? 7.596   -28.364 2.479   1.00 25.69  ? 76  GLY   A CA  1 
ATOM   611  C C   . GLY   A 1 77 ? 7.236   -27.114 3.268   1.00 25.46  ? 76  GLY   A C   1 
ATOM   612  O O   . GLY   A 1 77 ? 7.908   -26.103 3.143   1.00 24.96  ? 76  GLY   A O   1 
ATOM   613  N N   . PHE   A 1 78 ? 6.185   -27.147 4.086   1.00 25.49  ? 77  PHE   A N   1 
ATOM   614  C CA  . PHE   A 1 78 ? 5.729   -25.920 4.704   1.00 24.35  ? 77  PHE   A CA  1 
ATOM   615  C C   . PHE   A 1 78 ? 6.734   -25.320 5.683   1.00 25.81  ? 77  PHE   A C   1 
ATOM   616  O O   . PHE   A 1 78 ? 6.974   -24.107 5.709   1.00 25.03  ? 77  PHE   A O   1 
ATOM   617  C CB  . PHE   A 1 78 ? 4.375   -26.133 5.394   1.00 24.48  ? 77  PHE   A CB  1 
ATOM   618  C CG  . PHE   A 1 78 ? 3.667   -24.839 5.796   1.00 23.27  ? 77  PHE   A CG  1 
ATOM   619  C CD1 . PHE   A 1 78 ? 3.915   -24.167 6.990   1.00 24.92  ? 77  PHE   A CD1 1 
ATOM   620  C CD2 . PHE   A 1 78 ? 2.686   -24.316 4.931   1.00 26.50  ? 77  PHE   A CD2 1 
ATOM   621  C CE1 . PHE   A 1 78 ? 3.259   -22.985 7.322   1.00 24.42  ? 77  PHE   A CE1 1 
ATOM   622  C CE2 . PHE   A 1 78 ? 2.002   -23.151 5.273   1.00 25.13  ? 77  PHE   A CE2 1 
ATOM   623  C CZ  . PHE   A 1 78 ? 2.301   -22.476 6.433   1.00 24.88  ? 77  PHE   A CZ  1 
ATOM   624  N N   . ASN   A 1 79 ? 7.293   -26.147 6.576   1.00 22.87  ? 78  ASN   A N   1 
ATOM   625  C CA  . ASN   A 1 79 ? 8.144   -25.634 7.627   1.00 21.26  ? 78  ASN   A CA  1 
ATOM   626  C C   . ASN   A 1 79 ? 9.502   -25.201 7.030   1.00 21.20  ? 78  ASN   A C   1 
ATOM   627  O O   . ASN   A 1 79 ? 10.081  -24.206 7.485   1.00 21.67  ? 78  ASN   A O   1 
ATOM   628  C CB  . ASN   A 1 79 ? 8.294   -26.668 8.756   1.00 24.21  ? 78  ASN   A CB  1 
ATOM   629  C CG  . ASN   A 1 79 ? 6.951   -26.968 9.393   1.00 32.83  ? 78  ASN   A CG  1 
ATOM   630  O OD1 . ASN   A 1 79 ? 6.036   -26.125 9.383   1.00 28.00  ? 78  ASN   A OD1 1 
ATOM   631  N ND2 . ASN   A 1 79 ? 6.829   -28.142 10.018  1.00 29.52  ? 78  ASN   A ND2 1 
ATOM   632  N N   . GLU   A 1 80 ? 9.966   -25.900 5.983   1.00 22.35  ? 79  GLU   A N   1 
ATOM   633  C CA  . GLU   A 1 80 ? 11.104  -25.413 5.211   1.00 21.88  ? 79  GLU   A CA  1 
ATOM   634  C C   . GLU   A 1 80 ? 10.765  -24.035 4.652   1.00 18.81  ? 79  GLU   A C   1 
ATOM   635  O O   . GLU   A 1 80 ? 11.593  -23.096 4.697   1.00 20.08  ? 79  GLU   A O   1 
ATOM   636  C CB  . GLU   A 1 80 ? 11.513  -26.394 4.112   1.00 22.71  ? 79  GLU   A CB  1 
ATOM   637  C CG  . GLU   A 1 80 ? 12.767  -25.965 3.351   1.00 24.65  ? 79  GLU   A CG  1 
ATOM   638  C CD  . GLU   A 1 80 ? 13.261  -26.993 2.339   1.00 34.56  ? 79  GLU   A CD  1 
ATOM   639  O OE1 . GLU   A 1 80 ? 12.573  -28.024 2.160   1.00 40.53  ? 79  GLU   A OE1 1 
ATOM   640  O OE2 . GLU   A 1 80 ? 14.338  -26.785 1.772   1.00 33.79  ? 79  GLU   A OE2 1 
ATOM   641  N N   . GLY   A 1 81 ? 9.507   -23.912 4.183   1.00 21.64  ? 80  GLY   A N   1 
ATOM   642  C CA  . GLY   A 1 81 ? 9.113   -22.631 3.590   1.00 22.23  ? 80  GLY   A CA  1 
ATOM   643  C C   . GLY   A 1 81 ? 9.143   -21.498 4.622   1.00 19.94  ? 80  GLY   A C   1 
ATOM   644  O O   . GLY   A 1 81 ? 9.488   -20.328 4.319   1.00 18.39  ? 80  GLY   A O   1 
ATOM   645  N N   . LEU   A 1 82 ? 8.686   -21.766 5.860   1.00 18.73  ? 81  LEU   A N   1 
ATOM   646  C CA  . LEU   A 1 82 ? 8.716   -20.777 6.910   1.00 20.00  ? 81  LEU   A CA  1 
ATOM   647  C C   . LEU   A 1 82 ? 10.149  -20.319 7.181   1.00 19.09  ? 81  LEU   A C   1 
ATOM   648  O O   . LEU   A 1 82 ? 10.385  -19.132 7.408   1.00 20.33  ? 81  LEU   A O   1 
ATOM   649  C CB  . LEU   A 1 82 ? 8.066   -21.253 8.210   1.00 22.35  ? 81  LEU   A CB  1 
ATOM   650  C CG  . LEU   A 1 82 ? 6.571   -21.577 8.122   1.00 23.08  ? 81  LEU   A CG  1 
ATOM   651  C CD1 . LEU   A 1 82 ? 6.248   -22.122 9.504   1.00 24.27  ? 81  LEU   A CD1 1 
ATOM   652  C CD2 . LEU   A 1 82 ? 5.793   -20.301 7.917   1.00 24.27  ? 81  LEU   A CD2 1 
ATOM   653  N N   . TRP   A 1 83 ? 11.114  -21.257 7.162   1.00 20.12  ? 82  TRP   A N   1 
ATOM   654  C CA  . TRP   A 1 83 ? 12.507  -20.870 7.379   1.00 19.99  ? 82  TRP   A CA  1 
ATOM   655  C C   . TRP   A 1 83 ? 12.963  -19.944 6.255   1.00 18.18  ? 82  TRP   A C   1 
ATOM   656  O O   . TRP   A 1 83 ? 13.633  -18.962 6.523   1.00 19.15  ? 82  TRP   A O   1 
ATOM   657  C CB  . TRP   A 1 83 ? 13.440  -22.106 7.526   1.00 20.11  ? 82  TRP   A CB  1 
ATOM   658  C CG  . TRP   A 1 83 ? 14.895  -21.725 7.749   1.00 20.82  ? 82  TRP   A CG  1 
ATOM   659  C CD1 . TRP   A 1 83 ? 15.534  -21.581 8.947   1.00 22.05  ? 82  TRP   A CD1 1 
ATOM   660  C CD2 . TRP   A 1 83 ? 15.865  -21.433 6.716   1.00 19.18  ? 82  TRP   A CD2 1 
ATOM   661  N NE1 . TRP   A 1 83 ? 16.831  -21.232 8.725   1.00 22.51  ? 82  TRP   A NE1 1 
ATOM   662  C CE2 . TRP   A 1 83 ? 17.063  -21.114 7.381   1.00 21.61  ? 82  TRP   A CE2 1 
ATOM   663  C CE3 . TRP   A 1 83 ? 15.805  -21.400 5.311   1.00 20.14  ? 82  TRP   A CE3 1 
ATOM   664  C CZ2 . TRP   A 1 83 ? 18.220  -20.778 6.671   1.00 23.42  ? 82  TRP   A CZ2 1 
ATOM   665  C CZ3 . TRP   A 1 83 ? 16.949  -21.061 4.601   1.00 23.02  ? 82  TRP   A CZ3 1 
ATOM   666  C CH2 . TRP   A 1 83 ? 18.152  -20.782 5.293   1.00 23.39  ? 82  TRP   A CH2 1 
ATOM   667  N N   . GLU   A 1 84 ? 12.665  -20.304 5.016   1.00 18.17  ? 83  GLU   A N   1 
ATOM   668  C CA  . GLU   A 1 84 ? 13.160  -19.556 3.882   1.00 16.78  ? 83  GLU   A CA  1 
ATOM   669  C C   . GLU   A 1 84 ? 12.637  -18.121 3.886   1.00 19.44  ? 83  GLU   A C   1 
ATOM   670  O O   . GLU   A 1 84 ? 13.387  -17.176 3.675   1.00 18.45  ? 83  GLU   A O   1 
ATOM   671  C CB  . GLU   A 1 84 ? 12.756  -20.208 2.581   1.00 16.74  ? 83  GLU   A CB  1 
ATOM   672  C CG  . GLU   A 1 84 ? 13.432  -21.568 2.403   1.00 18.98  ? 83  GLU   A CG  1 
ATOM   673  C CD  . GLU   A 1 84 ? 13.034  -22.305 1.134   1.00 20.96  ? 83  GLU   A CD  1 
ATOM   674  O OE1 . GLU   A 1 84 ? 12.080  -21.920 0.431   1.00 21.22  ? 83  GLU   A OE1 1 
ATOM   675  O OE2 . GLU   A 1 84 ? 13.629  -23.425 0.868   1.00 22.76  ? 83  GLU   A OE2 1 
ATOM   676  N N   . ILE   A 1 85 ? 11.312  -17.948 4.126   1.00 16.66  ? 84  ILE   A N   1 
ATOM   677  C CA  . ILE   A 1 85 ? 10.744  -16.607 4.025   1.00 16.89  ? 84  ILE   A CA  1 
ATOM   678  C C   . ILE   A 1 85 ? 11.297  -15.703 5.134   1.00 17.80  ? 84  ILE   A C   1 
ATOM   679  O O   . ILE   A 1 85 ? 11.453  -14.505 4.922   1.00 18.98  ? 84  ILE   A O   1 
ATOM   680  C CB  . ILE   A 1 85 ? 9.193   -16.650 4.038   1.00 16.94  ? 84  ILE   A CB  1 
ATOM   681  C CG1 . ILE   A 1 85 ? 8.613   -15.279 3.608   1.00 16.65  ? 84  ILE   A CG1 1 
ATOM   682  C CG2 . ILE   A 1 85 ? 8.669   -17.048 5.433   1.00 18.84  ? 84  ILE   A CG2 1 
ATOM   683  C CD1 . ILE   A 1 85 ? 7.184   -15.435 3.105   1.00 17.04  ? 84  ILE   A CD1 1 
ATOM   684  N N   . GLN   A 1 86 ? 11.624  -16.263 6.313   1.00 18.09  ? 85  GLN   A N   1 
ATOM   685  C CA  . GLN   A 1 86 ? 12.155  -15.503 7.442   1.00 19.40  ? 85  GLN   A CA  1 
ATOM   686  C C   . GLN   A 1 86 ? 13.651  -15.260 7.288   1.00 19.42  ? 85  GLN   A C   1 
ATOM   687  O O   . GLN   A 1 86 ? 14.122  -14.157 7.666   1.00 23.56  ? 85  GLN   A O   1 
ATOM   688  C CB  . GLN   A 1 86 ? 11.790  -16.238 8.736   1.00 22.29  ? 85  GLN   A CB  1 
ATOM   689  C CG  . GLN   A 1 86 ? 12.243  -15.569 10.030  1.00 28.73  ? 85  GLN   A CG  1 
ATOM   690  C CD  . GLN   A 1 86 ? 11.586  -16.146 11.283  1.00 30.33  ? 85  GLN   A CD  1 
ATOM   691  O OE1 . GLN   A 1 86 ? 11.341  -17.358 11.387  1.00 32.54  ? 85  GLN   A OE1 1 
ATOM   692  N NE2 . GLN   A 1 86 ? 11.273  -15.274 12.238  1.00 37.72  ? 85  GLN   A NE2 1 
ATOM   693  N N   . ASN   A 1 87 ? 14.391  -16.232 6.735   1.00 18.26  ? 86  ASN   A N   1 
ATOM   694  C CA  . ASN   A 1 87 ? 15.855  -16.223 6.847   1.00 18.66  ? 86  ASN   A CA  1 
ATOM   695  C C   . ASN   A 1 87 ? 16.604  -15.952 5.537   1.00 18.20  ? 86  ASN   A C   1 
ATOM   696  O O   . ASN   A 1 87 ? 17.706  -15.345 5.568   1.00 21.27  ? 86  ASN   A O   1 
ATOM   697  C CB  . ASN   A 1 87 ? 16.327  -17.535 7.475   1.00 20.72  ? 86  ASN   A CB  1 
ATOM   698  C CG  . ASN   A 1 87 ? 15.885  -17.593 8.918   1.00 23.71  ? 86  ASN   A CG  1 
ATOM   699  O OD1 . ASN   A 1 87 ? 16.261  -16.701 9.706   1.00 27.37  ? 86  ASN   A OD1 1 
ATOM   700  N ND2 . ASN   A 1 87 ? 14.944  -18.460 9.250   1.00 23.09  ? 86  ASN   A ND2 1 
ATOM   701  N N   . ASN   A 1 88 ? 16.027  -16.278 4.360   1.00 17.78  ? 87  ASN   A N   1 
ATOM   702  C CA  . ASN   A 1 88 ? 16.680  -15.897 3.117   1.00 17.03  ? 87  ASN   A CA  1 
ATOM   703  C C   . ASN   A 1 88 ? 15.619  -15.854 2.015   1.00 18.39  ? 87  ASN   A C   1 
ATOM   704  O O   . ASN   A 1 88 ? 15.681  -16.575 1.012   1.00 18.83  ? 87  ASN   A O   1 
ATOM   705  C CB  . ASN   A 1 88 ? 17.859  -16.822 2.795   1.00 21.63  ? 87  ASN   A CB  1 
ATOM   706  C CG  . ASN   A 1 88 ? 18.903  -16.200 1.902   1.00 22.35  ? 87  ASN   A CG  1 
ATOM   707  O OD1 . ASN   A 1 88 ? 18.649  -15.209 1.214   1.00 19.80  ? 87  ASN   A OD1 1 
ATOM   708  N ND2 . ASN   A 1 88 ? 20.122  -16.749 1.887   1.00 26.51  ? 87  ASN   A ND2 1 
ATOM   709  N N   . PRO   A 1 89 ? 14.705  -14.873 2.113   1.00 17.69  ? 88  PRO   A N   1 
ATOM   710  C CA  . PRO   A 1 89 ? 13.573  -14.870 1.186   1.00 16.82  ? 88  PRO   A CA  1 
ATOM   711  C C   . PRO   A 1 89 ? 13.924  -14.432 -0.230  1.00 19.16  ? 88  PRO   A C   1 
ATOM   712  O O   . PRO   A 1 89 ? 13.133  -14.665 -1.136  1.00 17.39  ? 88  PRO   A O   1 
ATOM   713  C CB  . PRO   A 1 89 ? 12.651  -13.860 1.830   1.00 18.12  ? 88  PRO   A CB  1 
ATOM   714  C CG  . PRO   A 1 89 ? 13.563  -12.886 2.543   1.00 18.22  ? 88  PRO   A CG  1 
ATOM   715  C CD  . PRO   A 1 89 ? 14.640  -13.810 3.129   1.00 17.71  ? 88  PRO   A CD  1 
ATOM   716  N N   . HIS   A 1 90 ? 15.130  -13.832 -0.445  1.00 16.09  ? 89  HIS   A N   1 
ATOM   717  C CA  . HIS   A 1 90 ? 15.474  -13.340 -1.767  1.00 17.15  ? 89  HIS   A CA  1 
ATOM   718  C C   . HIS   A 1 90 ? 16.587  -14.146 -2.469  1.00 17.05  ? 89  HIS   A C   1 
ATOM   719  O O   . HIS   A 1 90 ? 17.019  -13.751 -3.547  1.00 18.92  ? 89  HIS   A O   1 
ATOM   720  C CB  . HIS   A 1 90 ? 15.845  -11.846 -1.676  1.00 16.48  ? 89  HIS   A CB  1 
ATOM   721  C CG  . HIS   A 1 90 ? 14.796  -10.968 -1.074  1.00 15.01  ? 89  HIS   A CG  1 
ATOM   722  N ND1 . HIS   A 1 90 ? 13.560  -10.898 -1.722  1.00 16.54  ? 89  HIS   A ND1 1 
ATOM   723  C CD2 . HIS   A 1 90 ? 14.736  -10.240 0.026   1.00 16.28  ? 89  HIS   A CD2 1 
ATOM   724  C CE1 . HIS   A 1 90 ? 12.768  -10.116 -0.998  1.00 16.22  ? 89  HIS   A CE1 1 
ATOM   725  N NE2 . HIS   A 1 90 ? 13.450  -9.693  0.060   1.00 18.41  ? 89  HIS   A NE2 1 
ATOM   726  N N   . ALA   A 1 91 ? 16.861  -15.338 -1.929  1.00 17.65  ? 90  ALA   A N   1 
ATOM   727  C CA  . ALA   A 1 91 ? 17.882  -16.225 -2.501  1.00 19.27  ? 90  ALA   A CA  1 
ATOM   728  C C   . ALA   A 1 91 ? 17.404  -16.890 -3.786  1.00 22.23  ? 90  ALA   A C   1 
ATOM   729  O O   . ALA   A 1 91 ? 16.220  -17.026 -4.042  1.00 22.34  ? 90  ALA   A O   1 
ATOM   730  C CB  . ALA   A 1 91 ? 18.302  -17.249 -1.482  1.00 20.61  ? 90  ALA   A CB  1 
ATOM   731  N N   . SER   A 1 92 ? 18.395  -17.413 -4.535  1.00 21.76  ? 91  SER   A N   1 
ATOM   732  C CA  . SER   A 1 92 ? 18.135  -18.391 -5.571  1.00 25.51  ? 91  SER   A CA  1 
ATOM   733  C C   . SER   A 1 92 ? 17.856  -19.769 -4.964  1.00 25.72  ? 91  SER   A C   1 
ATOM   734  O O   . SER   A 1 92 ? 18.658  -20.311 -4.181  1.00 29.34  ? 91  SER   A O   1 
ATOM   735  C CB  . SER   A 1 92 ? 19.337  -18.402 -6.475  1.00 29.23  ? 91  SER   A CB  1 
ATOM   736  O OG  . SER   A 1 92 ? 19.190  -19.438 -7.416  1.00 37.96  ? 91  SER   A OG  1 
ATOM   737  N N   . TYR   A 1 93 ? 16.707  -20.346 -5.327  1.00 23.86  ? 92  TYR   A N   1 
ATOM   738  C CA  . TYR   A 1 93 ? 16.322  -21.671 -4.874  1.00 26.15  ? 92  TYR   A CA  1 
ATOM   739  C C   . TYR   A 1 93 ? 16.145  -22.633 -6.045  1.00 31.39  ? 92  TYR   A C   1 
ATOM   740  O O   . TYR   A 1 93 ? 15.623  -23.731 -5.869  1.00 36.27  ? 92  TYR   A O   1 
ATOM   741  C CB  . TYR   A 1 93 ? 14.979  -21.592 -4.125  1.00 23.85  ? 92  TYR   A CB  1 
ATOM   742  C CG  . TYR   A 1 93 ? 15.124  -20.997 -2.741  1.00 22.91  ? 92  TYR   A CG  1 
ATOM   743  C CD1 . TYR   A 1 93 ? 15.567  -21.752 -1.640  1.00 24.61  ? 92  TYR   A CD1 1 
ATOM   744  C CD2 . TYR   A 1 93 ? 14.843  -19.636 -2.542  1.00 22.17  ? 92  TYR   A CD2 1 
ATOM   745  C CE1 . TYR   A 1 93 ? 15.736  -21.166 -0.388  1.00 25.51  ? 92  TYR   A CE1 1 
ATOM   746  C CE2 . TYR   A 1 93 ? 14.972  -19.072 -1.290  1.00 23.13  ? 92  TYR   A CE2 1 
ATOM   747  C CZ  . TYR   A 1 93 ? 15.431  -19.814 -0.218  1.00 21.76  ? 92  TYR   A CZ  1 
ATOM   748  O OH  . TYR   A 1 93 ? 15.653  -19.330 1.036   1.00 23.28  ? 92  TYR   A OH  1 
ATOM   749  N N   . SER   A 1 94 ? 16.547  -22.192 -7.232  1.00 36.26  ? 93  SER   A N   1 
ATOM   750  C CA  . SER   A 1 94 ? 16.814  -23.097 -8.337  1.00 46.30  ? 93  SER   A CA  1 
ATOM   751  C C   . SER   A 1 94 ? 17.889  -24.103 -7.896  1.00 55.20  ? 93  SER   A C   1 
ATOM   752  O O   . SER   A 1 94 ? 19.067  -23.681 -7.827  1.00 64.64  ? 93  SER   A O   1 
ATOM   753  C CB  . SER   A 1 94 ? 17.259  -22.298 -9.526  1.00 41.92  ? 93  SER   A CB  1 
ATOM   754  O OG  . SER   A 1 94 ? 16.245  -21.365 -9.872  1.00 53.57  ? 93  SER   A OG  1 
ATOM   755  O OXT . SER   A 1 94 ? 17.508  -25.262 -7.596  1.00 70.64  ? 93  SER   A OXT 1 
ATOM   756  N N   . MET   B 1 2  ? 38.699  -11.255 -41.843 1.00 47.35  ? 1   MET   B N   1 
ATOM   757  C CA  . MET   B 1 2  ? 38.415  -12.015 -43.091 1.00 49.00  ? 1   MET   B CA  1 
ATOM   758  C C   . MET   B 1 2  ? 36.901  -12.190 -43.180 1.00 43.40  ? 1   MET   B C   1 
ATOM   759  O O   . MET   B 1 2  ? 36.267  -12.449 -42.151 1.00 43.54  ? 1   MET   B O   1 
ATOM   760  C CB  . MET   B 1 2  ? 39.122  -13.380 -43.042 1.00 49.48  ? 1   MET   B CB  1 
ATOM   761  C CG  . MET   B 1 2  ? 39.120  -14.216 -44.329 1.00 63.98  ? 1   MET   B CG  1 
ATOM   762  S SD  . MET   B 1 2  ? 40.243  -13.734 -45.664 1.00 65.68  ? 1   MET   B SD  1 
ATOM   763  C CE  . MET   B 1 2  ? 41.297  -12.611 -44.734 1.00 41.78  ? 1   MET   B CE  1 
ATOM   764  N N   . PRO   B 1 3  ? 36.258  -12.039 -44.370 1.00 36.56  ? 2   PRO   B N   1 
ATOM   765  C CA  . PRO   B 1 3  ? 34.820  -12.305 -44.474 1.00 36.27  ? 2   PRO   B CA  1 
ATOM   766  C C   . PRO   B 1 3  ? 34.518  -13.741 -44.037 1.00 39.43  ? 2   PRO   B C   1 
ATOM   767  O O   . PRO   B 1 3  ? 35.314  -14.648 -44.263 1.00 37.17  ? 2   PRO   B O   1 
ATOM   768  C CB  . PRO   B 1 3  ? 34.469  -12.022 -45.936 1.00 37.48  ? 2   PRO   B CB  1 
ATOM   769  C CG  . PRO   B 1 3  ? 35.600  -11.090 -46.384 1.00 31.21  ? 2   PRO   B CG  1 
ATOM   770  C CD  . PRO   B 1 3  ? 36.840  -11.581 -45.644 1.00 33.26  ? 2   PRO   B CD  1 
ATOM   771  N N   . HIS   B 1 4  ? 33.377  -13.911 -43.355 1.00 36.45  ? 3   HIS   B N   1 
ATOM   772  C CA  . HIS   B 1 4  ? 32.907  -15.220 -42.928 1.00 35.89  ? 3   HIS   B CA  1 
ATOM   773  C C   . HIS   B 1 4  ? 31.544  -15.496 -43.565 1.00 33.58  ? 3   HIS   B C   1 
ATOM   774  O O   . HIS   B 1 4  ? 30.956  -14.647 -44.252 1.00 33.15  ? 3   HIS   B O   1 
ATOM   775  C CB  . HIS   B 1 4  ? 32.956  -15.323 -41.399 1.00 40.33  ? 3   HIS   B CB  1 
ATOM   776  C CG  . HIS   B 1 4  ? 34.361  -15.406 -40.887 1.00 47.12  ? 3   HIS   B CG  1 
ATOM   777  N ND1 . HIS   B 1 4  ? 35.268  -16.352 -41.333 1.00 48.28  ? 3   HIS   B ND1 1 
ATOM   778  C CD2 . HIS   B 1 4  ? 35.012  -14.665 -39.969 1.00 49.50  ? 3   HIS   B CD2 1 
ATOM   779  C CE1 . HIS   B 1 4  ? 36.425  -16.182 -40.699 1.00 46.82  ? 3   HIS   B CE1 1 
ATOM   780  N NE2 . HIS   B 1 4  ? 36.291  -15.162 -39.867 1.00 52.03  ? 3   HIS   B NE2 1 
ATOM   781  N N   . ALA   B 1 5  ? 31.029  -16.712 -43.350 1.00 31.90  ? 4   ALA   B N   1 
ATOM   782  C CA  . ALA   B 1 5  ? 29.743  -17.045 -43.931 1.00 33.42  ? 4   ALA   B CA  1 
ATOM   783  C C   . ALA   B 1 5  ? 28.699  -16.054 -43.430 1.00 31.34  ? 4   ALA   B C   1 
ATOM   784  O O   . ALA   B 1 5  ? 27.825  -15.630 -44.185 1.00 34.64  ? 4   ALA   B O   1 
ATOM   785  C CB  . ALA   B 1 5  ? 29.365  -18.460 -43.547 1.00 33.71  ? 4   ALA   B CB  1 
ATOM   786  N N   . PHE   B 1 6  ? 28.785  -15.732 -42.134 1.00 32.66  ? 5   PHE   B N   1 
ATOM   787  C CA  . PHE   B 1 6  ? 27.973  -14.679 -41.539 1.00 33.66  ? 5   PHE   B CA  1 
ATOM   788  C C   . PHE   B 1 6  ? 28.805  -13.413 -41.338 1.00 29.06  ? 5   PHE   B C   1 
ATOM   789  O O   . PHE   B 1 6  ? 29.933  -13.466 -40.858 1.00 33.75  ? 5   PHE   B O   1 
ATOM   790  C CB  . PHE   B 1 6  ? 27.378  -15.088 -40.187 1.00 31.12  ? 5   PHE   B CB  1 
ATOM   791  C CG  . PHE   B 1 6  ? 26.302  -16.163 -40.257 1.00 27.49  ? 5   PHE   B CG  1 
ATOM   792  C CD1 . PHE   B 1 6  ? 24.963  -15.817 -40.421 1.00 27.76  ? 5   PHE   B CD1 1 
ATOM   793  C CD2 . PHE   B 1 6  ? 26.639  -17.515 -40.212 1.00 31.05  ? 5   PHE   B CD2 1 
ATOM   794  C CE1 . PHE   B 1 6  ? 23.990  -16.804 -40.501 1.00 27.58  ? 5   PHE   B CE1 1 
ATOM   795  C CE2 . PHE   B 1 6  ? 25.649  -18.492 -40.273 1.00 25.47  ? 5   PHE   B CE2 1 
ATOM   796  C CZ  . PHE   B 1 6  ? 24.344  -18.143 -40.409 1.00 24.82  ? 5   PHE   B CZ  1 
ATOM   797  N N   . LYS   B 1 7  ? 28.197  -12.274 -41.667 1.00 33.07  ? 6   LYS   B N   1 
ATOM   798  C CA  . LYS   B 1 7  ? 28.884  -11.002 -41.501 1.00 31.74  ? 6   LYS   B CA  1 
ATOM   799  C C   . LYS   B 1 7  ? 28.154  -10.157 -40.460 1.00 29.80  ? 6   LYS   B C   1 
ATOM   800  O O   . LYS   B 1 7  ? 26.937  -10.295 -40.250 1.00 26.50  ? 6   LYS   B O   1 
ATOM   801  C CB  . LYS   B 1 7  ? 28.947  -10.246 -42.828 1.00 34.21  ? 6   LYS   B CB  1 
ATOM   802  C CG  . LYS   B 1 7  ? 27.659  -9.980  -43.557 1.00 39.12  ? 6   LYS   B CG  1 
ATOM   803  C CD  . LYS   B 1 7  ? 27.974  -9.559  -44.995 1.00 38.18  ? 6   LYS   B CD  1 
ATOM   804  C CE  . LYS   B 1 7  ? 26.761  -9.125  -45.749 1.00 40.35  ? 6   LYS   B CE  1 
ATOM   805  N NZ  . LYS   B 1 7  ? 25.787  -10.219 -45.863 1.00 42.87  ? 6   LYS   B NZ  1 
ATOM   806  N N   . PRO   B 1 8  ? 28.859  -9.199  -39.820 1.00 31.38  ? 7   PRO   B N   1 
ATOM   807  C CA  . PRO   B 1 8  ? 28.216  -8.263  -38.897 1.00 26.66  ? 7   PRO   B CA  1 
ATOM   808  C C   . PRO   B 1 8  ? 27.044  -7.561  -39.550 1.00 29.12  ? 7   PRO   B C   1 
ATOM   809  O O   . PRO   B 1 8  ? 27.138  -7.053  -40.685 1.00 31.52  ? 7   PRO   B O   1 
ATOM   810  C CB  . PRO   B 1 8  ? 29.382  -7.312  -38.629 1.00 30.44  ? 7   PRO   B CB  1 
ATOM   811  C CG  . PRO   B 1 8  ? 30.600  -8.202  -38.668 1.00 34.96  ? 7   PRO   B CG  1 
ATOM   812  C CD  . PRO   B 1 8  ? 30.311  -8.953  -39.943 1.00 35.10  ? 7   PRO   B CD  1 
ATOM   813  N N   . GLY   B 1 9  ? 25.940  -7.530  -38.810 1.00 23.28  ? 8   GLY   B N   1 
ATOM   814  C CA  . GLY   B 1 9  ? 24.693  -6.954  -39.254 1.00 24.78  ? 8   GLY   B CA  1 
ATOM   815  C C   . GLY   B 1 9  ? 23.719  -7.951  -39.872 1.00 22.54  ? 8   GLY   B C   1 
ATOM   816  O O   . GLY   B 1 9  ? 22.595  -7.592  -40.168 1.00 25.99  ? 8   GLY   B O   1 
ATOM   817  N N   . ASP   B 1 10 ? 24.170  -9.188  -40.168 1.00 23.73  ? 9   ASP   B N   1 
ATOM   818  C CA  . ASP   B 1 10 ? 23.243  -10.155 -40.720 1.00 26.47  ? 9   ASP   B CA  1 
ATOM   819  C C   . ASP   B 1 10 ? 22.222  -10.522 -39.639 1.00 19.87  ? 9   ASP   B C   1 
ATOM   820  O O   . ASP   B 1 10 ? 22.564  -10.572 -38.448 1.00 22.96  ? 9   ASP   B O   1 
ATOM   821  C CB  . ASP   B 1 10 ? 23.907  -11.460 -41.125 1.00 27.40  ? 9   ASP   B CB  1 
ATOM   822  C CG  . ASP   B 1 10 ? 24.716  -11.524 -42.421 1.00 30.82  ? 9   ASP   B CG  1 
ATOM   823  O OD1 . ASP   B 1 10 ? 24.502  -10.663 -43.265 1.00 33.42  ? 9   ASP   B OD1 1 
ATOM   824  O OD2 . ASP   B 1 10 ? 25.552  -12.468 -42.529 1.00 31.55  ? 9   ASP   B OD2 1 
ATOM   825  N N   . LEU   B 1 11 ? 21.012  -10.678 -40.113 1.00 20.86  ? 10  LEU   B N   1 
ATOM   826  C CA  . LEU   B 1 11 ? 19.854  -10.898 -39.246 1.00 21.45  ? 10  LEU   B CA  1 
ATOM   827  C C   . LEU   B 1 11 ? 19.613  -12.405 -39.225 1.00 20.86  ? 10  LEU   B C   1 
ATOM   828  O O   . LEU   B 1 11 ? 19.607  -13.043 -40.287 1.00 24.30  ? 10  LEU   B O   1 
ATOM   829  C CB  . LEU   B 1 11 ? 18.642  -10.075 -39.691 1.00 21.25  ? 10  LEU   B CB  1 
ATOM   830  C CG  . LEU   B 1 11 ? 18.935  -8.565  -39.795 1.00 21.37  ? 10  LEU   B CG  1 
ATOM   831  C CD1 . LEU   B 1 11 ? 17.684  -7.855  -40.199 1.00 22.49  ? 10  LEU   B CD1 1 
ATOM   832  C CD2 . LEU   B 1 11 ? 19.608  -8.064  -38.497 1.00 24.96  ? 10  LEU   B CD2 1 
ATOM   833  N N   . VAL   B 1 12 ? 19.277  -12.944 -38.037 1.00 19.80  ? 11  VAL   B N   1 
ATOM   834  C CA  . VAL   B 1 12 ? 19.088  -14.396 -37.910 1.00 20.06  ? 11  VAL   B CA  1 
ATOM   835  C C   . VAL   B 1 12 ? 17.978  -14.660 -36.906 1.00 18.98  ? 11  VAL   B C   1 
ATOM   836  O O   . VAL   B 1 12 ? 17.560  -13.780 -36.152 1.00 20.06  ? 11  VAL   B O   1 
ATOM   837  C CB  . VAL   B 1 12 ? 20.372  -15.101 -37.453 1.00 19.80  ? 11  VAL   B CB  1 
ATOM   838  C CG1 . VAL   B 1 12 ? 21.527  -14.931 -38.483 1.00 23.80  ? 11  VAL   B CG1 1 
ATOM   839  C CG2 . VAL   B 1 12 ? 20.841  -14.699 -36.040 1.00 20.55  ? 11  VAL   B CG2 1 
ATOM   840  N N   . PHE   B 1 13 ? 17.537  -15.938 -36.839 1.00 18.89  ? 12  PHE   B N   1 
ATOM   841  C CA  . PHE   B 1 13 ? 17.024  -16.476 -35.595 1.00 19.78  ? 12  PHE   B CA  1 
ATOM   842  C C   . PHE   B 1 13 ? 18.107  -17.343 -35.006 1.00 19.70  ? 12  PHE   B C   1 
ATOM   843  O O   . PHE   B 1 13 ? 18.724  -18.144 -35.744 1.00 22.29  ? 12  PHE   B O   1 
ATOM   844  C CB  . PHE   B 1 13 ? 15.770  -17.300 -35.847 1.00 18.40  ? 12  PHE   B CB  1 
ATOM   845  C CG  . PHE   B 1 13 ? 14.577  -16.470 -36.283 1.00 19.10  ? 12  PHE   B CG  1 
ATOM   846  C CD1 . PHE   B 1 13 ? 14.386  -16.188 -37.629 1.00 21.54  ? 12  PHE   B CD1 1 
ATOM   847  C CD2 . PHE   B 1 13 ? 13.669  -15.982 -35.350 1.00 21.29  ? 12  PHE   B CD2 1 
ATOM   848  C CE1 . PHE   B 1 13 ? 13.278  -15.459 -38.045 1.00 24.84  ? 12  PHE   B CE1 1 
ATOM   849  C CE2 . PHE   B 1 13 ? 12.563  -15.245 -35.764 1.00 22.83  ? 12  PHE   B CE2 1 
ATOM   850  C CZ  . PHE   B 1 13 ? 12.389  -14.963 -37.114 1.00 28.93  ? 12  PHE   B CZ  1 
ATOM   851  N N   . ALA   B 1 14 ? 18.357  -17.176 -33.691 1.00 20.16  ? 13  ALA   B N   1 
ATOM   852  C CA  . ALA   B 1 14 ? 19.370  -17.940 -33.003 1.00 19.08  ? 13  ALA   B CA  1 
ATOM   853  C C   . ALA   B 1 14 ? 18.701  -18.890 -32.000 1.00 19.25  ? 13  ALA   B C   1 
ATOM   854  O O   . ALA   B 1 14 ? 17.844  -18.470 -31.223 1.00 19.38  ? 13  ALA   B O   1 
ATOM   855  C CB  . ALA   B 1 14 ? 20.266  -16.999 -32.254 1.00 21.55  ? 13  ALA   B CB  1 
ATOM   856  N N   . LYS   B 1 15 ? 19.088  -20.166 -32.039 1.00 19.77  ? 14  LYS   B N   1 
ATOM   857  C CA  . LYS   B 1 15 ? 18.474  -21.215 -31.227 1.00 22.03  ? 14  LYS   B CA  1 
ATOM   858  C C   . LYS   B 1 15 ? 19.353  -21.596 -30.045 1.00 23.83  ? 14  LYS   B C   1 
ATOM   859  O O   . LYS   B 1 15 ? 20.542  -21.895 -30.202 1.00 24.07  ? 14  LYS   B O   1 
ATOM   860  C CB  . LYS   B 1 15 ? 18.205  -22.415 -32.132 1.00 22.84  ? 14  LYS   B CB  1 
ATOM   861  C CG  . LYS   B 1 15 ? 17.536  -23.554 -31.309 1.00 20.69  ? 14  LYS   B CG  1 
ATOM   862  C CD  . LYS   B 1 15 ? 16.100  -23.137 -31.007 1.00 22.97  ? 14  LYS   B CD  1 
ATOM   863  C CE  . LYS   B 1 15 ? 15.228  -24.235 -30.287 1.00 22.58  ? 14  LYS   B CE  1 
ATOM   864  N NZ  . LYS   B 1 15 ? 15.786  -24.545 -28.977 1.00 25.12  ? 14  LYS   B NZ  1 
ATOM   865  N N   . MET   B 1 16 ? 18.753  -21.587 -28.848 1.00 22.93  ? 15  MET   B N   1 
ATOM   866  C CA  . MET   B 1 16 ? 19.417  -22.016 -27.620 1.00 26.38  ? 15  MET   B CA  1 
ATOM   867  C C   . MET   B 1 16 ? 18.505  -22.997 -26.879 1.00 23.93  ? 15  MET   B C   1 
ATOM   868  O O   . MET   B 1 16 ? 17.279  -22.901 -26.962 1.00 22.58  ? 15  MET   B O   1 
ATOM   869  C CB  . MET   B 1 16 ? 19.803  -20.828 -26.735 1.00 27.89  ? 15  MET   B CB  1 
ATOM   870  C CG  . MET   B 1 16 ? 20.989  -20.066 -27.344 1.00 28.71  ? 15  MET   B CG  1 
ATOM   871  S SD  . MET   B 1 16 ? 21.606  -18.717 -26.327 1.00 28.26  ? 15  MET   B SD  1 
ATOM   872  C CE  . MET   B 1 16 ? 22.601  -19.733 -25.236 1.00 28.89  ? 15  MET   B CE  1 
ATOM   873  N N   . LYS   B 1 17 ? 19.146  -23.950 -26.183 1.00 24.97  ? 16  LYS   B N   1 
ATOM   874  C CA  . LYS   B 1 17 ? 18.379  -24.969 -25.465 1.00 25.84  ? 16  LYS   B CA  1 
ATOM   875  C C   . LYS   B 1 17 ? 17.458  -24.276 -24.455 1.00 24.59  ? 16  LYS   B C   1 
ATOM   876  O O   . LYS   B 1 17 ? 17.879  -23.366 -23.728 1.00 25.97  ? 16  LYS   B O   1 
ATOM   877  C CB  . LYS   B 1 17 ? 19.395  -25.870 -24.749 1.00 33.01  ? 16  LYS   B CB  1 
ATOM   878  C CG  . LYS   B 1 17 ? 18.787  -27.084 -24.055 1.00 40.94  ? 16  LYS   B CG  1 
ATOM   879  C CD  . LYS   B 1 17 ? 19.899  -27.901 -23.401 1.00 48.46  ? 16  LYS   B CD  1 
ATOM   880  C CE  . LYS   B 1 17 ? 19.573  -29.349 -23.134 1.00 60.91  ? 16  LYS   B CE  1 
ATOM   881  N NZ  . LYS   B 1 17 ? 18.373  -29.560 -22.318 1.00 65.56  ? 16  LYS   B NZ  1 
ATOM   882  N N   . GLY   B 1 18 ? 16.179  -24.657 -24.518 1.00 24.95  ? 17  GLY   B N   1 
ATOM   883  C CA  . GLY   B 1 18 ? 15.150  -24.163 -23.620 1.00 26.33  ? 17  GLY   B CA  1 
ATOM   884  C C   . GLY   B 1 18 ? 14.398  -22.934 -24.139 1.00 25.32  ? 17  GLY   B C   1 
ATOM   885  O O   . GLY   B 1 18 ? 13.469  -22.447 -23.491 1.00 25.77  ? 17  GLY   B O   1 
ATOM   886  N N   . TYR   B 1 19 ? 14.773  -22.443 -25.341 1.00 24.38  ? 18  TYR   B N   1 
ATOM   887  C CA  . TYR   B 1 19 ? 14.144  -21.251 -25.893 1.00 23.59  ? 18  TYR   B CA  1 
ATOM   888  C C   . TYR   B 1 19 ? 13.767  -21.481 -27.358 1.00 22.77  ? 18  TYR   B C   1 
ATOM   889  O O   . TYR   B 1 19 ? 14.447  -22.204 -28.091 1.00 23.69  ? 18  TYR   B O   1 
ATOM   890  C CB  . TYR   B 1 19 ? 15.123  -20.066 -25.837 1.00 21.78  ? 18  TYR   B CB  1 
ATOM   891  C CG  . TYR   B 1 19 ? 15.542  -19.740 -24.413 1.00 20.76  ? 18  TYR   B CG  1 
ATOM   892  C CD1 . TYR   B 1 19 ? 14.699  -19.015 -23.568 1.00 24.82  ? 18  TYR   B CD1 1 
ATOM   893  C CD2 . TYR   B 1 19 ? 16.702  -20.309 -23.895 1.00 22.16  ? 18  TYR   B CD2 1 
ATOM   894  C CE1 . TYR   B 1 19 ? 15.050  -18.820 -22.231 1.00 23.98  ? 18  TYR   B CE1 1 
ATOM   895  C CE2 . TYR   B 1 19 ? 17.074  -20.092 -22.569 1.00 27.02  ? 18  TYR   B CE2 1 
ATOM   896  C CZ  . TYR   B 1 19 ? 16.235  -19.347 -21.748 1.00 25.60  ? 18  TYR   B CZ  1 
ATOM   897  O OH  . TYR   B 1 19 ? 16.679  -19.167 -20.448 1.00 29.50  ? 18  TYR   B OH  1 
ATOM   898  N N   . PRO   B 1 20 ? 12.708  -20.805 -27.842 1.00 22.43  ? 19  PRO   B N   1 
ATOM   899  C CA  . PRO   B 1 20 ? 12.358  -20.823 -29.257 1.00 21.68  ? 19  PRO   B CA  1 
ATOM   900  C C   . PRO   B 1 20 ? 13.419  -20.089 -30.067 1.00 20.94  ? 19  PRO   B C   1 
ATOM   901  O O   . PRO   B 1 20 ? 14.087  -19.239 -29.532 1.00 21.60  ? 19  PRO   B O   1 
ATOM   902  C CB  . PRO   B 1 20 ? 11.058  -20.117 -29.341 1.00 23.52  ? 19  PRO   B CB  1 
ATOM   903  C CG  . PRO   B 1 20 ? 11.062  -19.180 -28.134 1.00 23.87  ? 19  PRO   B CG  1 
ATOM   904  C CD  . PRO   B 1 20 ? 11.814  -19.950 -27.040 1.00 22.08  ? 19  PRO   B CD  1 
ATOM   905  N N   . HIS   B 1 21 ? 13.556  -20.464 -31.348 1.00 20.32  ? 20  HIS   B N   1 
ATOM   906  C CA  . HIS   B 1 21 ? 14.424  -19.698 -32.265 1.00 19.01  ? 20  HIS   B CA  1 
ATOM   907  C C   . HIS   B 1 21 ? 14.172  -18.195 -32.091 1.00 19.97  ? 20  HIS   B C   1 
ATOM   908  O O   . HIS   B 1 21 ? 13.060  -17.734 -32.222 1.00 19.84  ? 20  HIS   B O   1 
ATOM   909  C CB  . HIS   B 1 21 ? 14.131  -20.158 -33.707 1.00 20.37  ? 20  HIS   B CB  1 
ATOM   910  C CG  . HIS   B 1 21 ? 14.266  -21.639 -33.936 1.00 21.18  ? 20  HIS   B CG  1 
ATOM   911  N ND1 . HIS   B 1 21 ? 13.332  -22.561 -33.469 1.00 22.62  ? 20  HIS   B ND1 1 
ATOM   912  C CD2 . HIS   B 1 21 ? 15.281  -22.385 -34.459 1.00 23.05  ? 20  HIS   B CD2 1 
ATOM   913  C CE1 . HIS   B 1 21 ? 13.735  -23.782 -33.806 1.00 23.18  ? 20  HIS   B CE1 1 
ATOM   914  N NE2 . HIS   B 1 21 ? 14.888  -23.727 -34.419 1.00 23.05  ? 20  HIS   B NE2 1 
ATOM   915  N N   . TRP   B 1 22 ? 15.238  -17.453 -31.852 1.00 19.44  ? 21  TRP   B N   1 
ATOM   916  C CA  . TRP   B 1 22 ? 15.037  -16.124 -31.263 1.00 18.99  ? 21  TRP   B CA  1 
ATOM   917  C C   . TRP   B 1 22 ? 15.539  -15.043 -32.221 1.00 18.41  ? 21  TRP   B C   1 
ATOM   918  O O   . TRP   B 1 22 ? 16.670  -15.160 -32.717 1.00 18.80  ? 21  TRP   B O   1 
ATOM   919  C CB  . TRP   B 1 22 ? 15.782  -16.051 -29.922 1.00 19.66  ? 21  TRP   B CB  1 
ATOM   920  C CG  . TRP   B 1 22 ? 15.293  -14.908 -29.050 1.00 18.92  ? 21  TRP   B CG  1 
ATOM   921  C CD1 . TRP   B 1 22 ? 15.567  -13.567 -29.157 1.00 18.98  ? 21  TRP   B CD1 1 
ATOM   922  C CD2 . TRP   B 1 22 ? 14.330  -15.017 -27.965 1.00 20.26  ? 21  TRP   B CD2 1 
ATOM   923  N NE1 . TRP   B 1 22 ? 14.815  -12.848 -28.241 1.00 20.45  ? 21  TRP   B NE1 1 
ATOM   924  C CE2 . TRP   B 1 22 ? 14.061  -13.716 -27.480 1.00 20.90  ? 21  TRP   B CE2 1 
ATOM   925  C CE3 . TRP   B 1 22 ? 13.691  -16.126 -27.382 1.00 21.83  ? 21  TRP   B CE3 1 
ATOM   926  C CZ2 . TRP   B 1 22 ? 13.164  -13.463 -26.429 1.00 22.19  ? 21  TRP   B CZ2 1 
ATOM   927  C CZ3 . TRP   B 1 22 ? 12.790  -15.886 -26.356 1.00 21.69  ? 21  TRP   B CZ3 1 
ATOM   928  C CH2 . TRP   B 1 22 ? 12.528  -14.573 -25.900 1.00 22.02  ? 21  TRP   B CH2 1 
ATOM   929  N N   . PRO   B 1 23 ? 14.791  -13.941 -32.483 1.00 20.48  ? 22  PRO   B N   1 
ATOM   930  C CA  . PRO   B 1 23 ? 15.276  -12.901 -33.423 1.00 17.82  ? 22  PRO   B CA  1 
ATOM   931  C C   . PRO   B 1 23 ? 16.591  -12.311 -32.911 1.00 19.55  ? 22  PRO   B C   1 
ATOM   932  O O   . PRO   B 1 23 ? 16.728  -11.926 -31.744 1.00 19.34  ? 22  PRO   B O   1 
ATOM   933  C CB  . PRO   B 1 23 ? 14.115  -11.860 -33.451 1.00 19.38  ? 22  PRO   B CB  1 
ATOM   934  C CG  . PRO   B 1 23 ? 13.406  -12.067 -32.106 1.00 20.22  ? 22  PRO   B CG  1 
ATOM   935  C CD  . PRO   B 1 23 ? 13.448  -13.602 -31.973 1.00 19.71  ? 22  PRO   B CD  1 
ATOM   936  N N   . ALA   B 1 24 ? 17.601  -12.190 -33.795 1.00 19.49  ? 23  ALA   B N   1 
ATOM   937  C CA  . ALA   B 1 24 ? 18.932  -11.843 -33.323 1.00 19.45  ? 23  ALA   B CA  1 
ATOM   938  C C   . ALA   B 1 24 ? 19.721  -11.262 -34.515 1.00 17.93  ? 23  ALA   B C   1 
ATOM   939  O O   . ALA   B 1 24 ? 19.228  -11.308 -35.631 1.00 20.19  ? 23  ALA   B O   1 
ATOM   940  C CB  . ALA   B 1 24 ? 19.614  -13.051 -32.673 1.00 20.25  ? 23  ALA   B CB  1 
ATOM   941  N N   . ARG   B 1 25 ? 20.895  -10.727 -34.190 1.00 20.11  ? 24  ARG   B N   1 
ATOM   942  C CA  . ARG   B 1 25 ? 21.829  -10.238 -35.206 1.00 19.39  ? 24  ARG   B CA  1 
ATOM   943  C C   . ARG   B 1 25 ? 23.220  -10.731 -34.865 1.00 20.55  ? 24  ARG   B C   1 
ATOM   944  O O   . ARG   B 1 25 ? 23.551  -10.996 -33.722 1.00 21.26  ? 24  ARG   B O   1 
ATOM   945  C CB  . ARG   B 1 25 ? 21.827  -8.709  -35.362 1.00 20.91  ? 24  ARG   B CB  1 
ATOM   946  C CG  . ARG   B 1 25 ? 22.406  -7.969  -34.172 1.00 21.50  ? 24  ARG   B CG  1 
ATOM   947  C CD  . ARG   B 1 25 ? 22.252  -6.444  -34.322 1.00 21.36  ? 24  ARG   B CD  1 
ATOM   948  N NE  . ARG   B 1 25 ? 22.839  -5.842  -33.139 1.00 23.72  ? 24  ARG   B NE  1 
ATOM   949  C CZ  . ARG   B 1 25 ? 22.570  -4.574  -32.768 1.00 23.44  ? 24  ARG   B CZ  1 
ATOM   950  N NH1 . ARG   B 1 25 ? 21.574  -3.944  -33.396 1.00 23.40  ? 24  ARG   B NH1 1 
ATOM   951  N NH2 . ARG   B 1 25 ? 23.253  -4.066  -31.753 1.00 23.99  ? 24  ARG   B NH2 1 
ATOM   952  N N   . ILE   B 1 26 ? 24.055  -10.805 -35.931 1.00 21.24  ? 25  ILE   B N   1 
ATOM   953  C CA  . ILE   B 1 26 ? 25.473  -11.002 -35.736 1.00 22.64  ? 25  ILE   B CA  1 
ATOM   954  C C   . ILE   B 1 26 ? 26.056  -9.636  -35.404 1.00 24.28  ? 25  ILE   B C   1 
ATOM   955  O O   . ILE   B 1 26 ? 25.808  -8.689  -36.125 1.00 26.33  ? 25  ILE   B O   1 
ATOM   956  C CB  . ILE   B 1 26 ? 26.080  -11.478 -37.073 1.00 26.64  ? 25  ILE   B CB  1 
ATOM   957  C CG1 . ILE   B 1 26 ? 25.325  -12.670 -37.650 1.00 26.61  ? 25  ILE   B CG1 1 
ATOM   958  C CG2 . ILE   B 1 26 ? 27.576  -11.765 -36.902 1.00 27.51  ? 25  ILE   B CG2 1 
ATOM   959  C CD1 . ILE   B 1 26 ? 25.432  -13.946 -36.829 1.00 26.59  ? 25  ILE   B CD1 1 
ATOM   960  N N   . ASP   B 1 27 ? 26.824  -9.593  -34.340 1.00 24.53  ? 26  ASP   B N   1 
ATOM   961  C CA  . ASP   B 1 27 ? 27.480  -8.350  -33.940 1.00 29.21  ? 26  ASP   B CA  1 
ATOM   962  C C   . ASP   B 1 27 ? 28.943  -8.375  -34.403 1.00 34.61  ? 26  ASP   B C   1 
ATOM   963  O O   . ASP   B 1 27 ? 29.494  -9.445  -34.682 1.00 38.22  ? 26  ASP   B O   1 
ATOM   964  C CB  . ASP   B 1 27 ? 27.457  -8.237  -32.426 1.00 26.94  ? 26  ASP   B CB  1 
ATOM   965  C CG  . ASP   B 1 27 ? 26.301  -7.460  -31.816 1.00 29.53  ? 26  ASP   B CG  1 
ATOM   966  O OD1 . ASP   B 1 27 ? 25.499  -6.886  -32.597 1.00 32.45  ? 26  ASP   B OD1 1 
ATOM   967  O OD2 . ASP   B 1 27 ? 26.244  -7.433  -30.549 1.00 30.42  ? 26  ASP   B OD2 1 
ATOM   968  N N   A ASP   B 1 28 ? 29.574  -7.191  -34.401 0.50 43.70  ? 27  ASP   B N   1 
ATOM   969  N N   B ASP   B 1 28 ? 29.583  -7.197  -34.445 0.50 41.53  ? 27  ASP   B N   1 
ATOM   970  C CA  A ASP   B 1 28 ? 30.991  -7.023  -34.691 0.50 50.82  ? 27  ASP   B CA  1 
ATOM   971  C CA  B ASP   B 1 28 ? 30.999  -7.108  -34.775 0.50 46.31  ? 27  ASP   B CA  1 
ATOM   972  C C   A ASP   B 1 28 ? 31.814  -7.515  -33.503 0.50 52.43  ? 27  ASP   B C   1 
ATOM   973  C C   B ASP   B 1 28 ? 31.822  -7.479  -33.541 0.50 49.46  ? 27  ASP   B C   1 
ATOM   974  O O   A ASP   B 1 28 ? 31.357  -7.447  -32.366 0.50 55.13  ? 27  ASP   B O   1 
ATOM   975  O O   B ASP   B 1 28 ? 31.373  -7.295  -32.414 0.50 52.18  ? 27  ASP   B O   1 
ATOM   976  C CB  A ASP   B 1 28 ? 31.315  -5.561  -34.958 0.50 51.04  ? 27  ASP   B CB  1 
ATOM   977  C CB  B ASP   B 1 28 ? 31.374  -5.736  -35.314 0.50 42.52  ? 27  ASP   B CB  1 
ATOM   978  C CG  A ASP   B 1 28 ? 30.170  -4.751  -35.548 0.50 50.95  ? 27  ASP   B CG  1 
ATOM   979  C CG  B ASP   B 1 28 ? 32.336  -5.732  -36.495 0.50 38.07  ? 27  ASP   B CG  1 
ATOM   980  O OD1 A ASP   B 1 28 ? 30.236  -4.433  -36.755 0.50 53.03  ? 27  ASP   B OD1 1 
ATOM   981  O OD1 B ASP   B 1 28 ? 33.312  -6.515  -36.475 0.50 43.53  ? 27  ASP   B OD1 1 
ATOM   982  O OD2 A ASP   B 1 28 ? 29.218  -4.453  -34.795 0.50 53.59  ? 27  ASP   B OD2 1 
ATOM   983  O OD2 B ASP   B 1 28 ? 32.108  -4.935  -37.423 0.50 39.16  ? 27  ASP   B OD2 1 
ATOM   984  N N   . ILE   B 1 29 ? 33.030  -8.001  -33.776 1.00 60.47  ? 28  ILE   B N   1 
ATOM   985  C CA  . ILE   B 1 29 ? 33.887  -8.551  -32.734 1.00 67.63  ? 28  ILE   B CA  1 
ATOM   986  C C   . ILE   B 1 29 ? 34.986  -7.534  -32.378 1.00 72.93  ? 28  ILE   B C   1 
ATOM   987  O O   . ILE   B 1 29 ? 34.631  -6.349  -32.161 1.00 80.26  ? 28  ILE   B O   1 
ATOM   988  C CB  . ILE   B 1 29 ? 34.476  -9.904  -33.176 1.00 61.97  ? 28  ILE   B CB  1 
ATOM   989  N N   . VAL   B 1 34 ? 36.957  -9.829  -24.962 1.00 67.57  ? 33  VAL   B N   1 
ATOM   990  C CA  . VAL   B 1 34 ? 36.763  -11.265 -25.325 1.00 68.28  ? 33  VAL   B CA  1 
ATOM   991  C C   . VAL   B 1 34 ? 36.648  -11.346 -26.845 1.00 74.84  ? 33  VAL   B C   1 
ATOM   992  O O   . VAL   B 1 34 ? 36.092  -10.443 -27.468 1.00 85.98  ? 33  VAL   B O   1 
ATOM   993  C CB  . VAL   B 1 34 ? 35.505  -11.792 -24.600 1.00 66.55  ? 33  VAL   B CB  1 
ATOM   994  C CG1 . VAL   B 1 34 ? 34.210  -11.179 -25.133 1.00 67.64  ? 33  VAL   B CG1 1 
ATOM   995  C CG2 . VAL   B 1 34 ? 35.417  -13.314 -24.589 1.00 61.41  ? 33  VAL   B CG2 1 
ATOM   996  N N   . LYS   B 1 35 ? 37.234  -12.395 -27.438 1.00 73.85  ? 34  LYS   B N   1 
ATOM   997  C CA  . LYS   B 1 35 ? 36.952  -12.755 -28.824 1.00 65.47  ? 34  LYS   B CA  1 
ATOM   998  C C   . LYS   B 1 35 ? 36.104  -14.028 -28.811 1.00 58.91  ? 34  LYS   B C   1 
ATOM   999  O O   . LYS   B 1 35 ? 36.192  -14.811 -27.860 1.00 57.90  ? 34  LYS   B O   1 
ATOM   1000 C CB  . LYS   B 1 35 ? 38.242  -12.848 -29.652 1.00 62.78  ? 34  LYS   B CB  1 
ATOM   1001 N N   . PRO   B 1 36 ? 35.238  -14.292 -29.826 1.00 54.27  ? 35  PRO   B N   1 
ATOM   1002 C CA  . PRO   B 1 36 ? 34.372  -15.474 -29.780 1.00 48.50  ? 35  PRO   B CA  1 
ATOM   1003 C C   . PRO   B 1 36 ? 35.229  -16.732 -29.761 1.00 40.03  ? 35  PRO   B C   1 
ATOM   1004 O O   . PRO   B 1 36 ? 36.316  -16.725 -30.327 1.00 47.35  ? 35  PRO   B O   1 
ATOM   1005 C CB  . PRO   B 1 36 ? 33.517  -15.365 -31.062 1.00 48.94  ? 35  PRO   B CB  1 
ATOM   1006 C CG  . PRO   B 1 36 ? 34.291  -14.426 -31.971 1.00 53.89  ? 35  PRO   B CG  1 
ATOM   1007 C CD  . PRO   B 1 36 ? 35.047  -13.491 -31.046 1.00 52.20  ? 35  PRO   B CD  1 
ATOM   1008 N N   . PRO   B 1 37 ? 34.784  -17.845 -29.135 1.00 39.84  ? 36  PRO   B N   1 
ATOM   1009 C CA  . PRO   B 1 37 ? 35.506  -19.111 -29.235 1.00 36.66  ? 36  PRO   B CA  1 
ATOM   1010 C C   . PRO   B 1 37 ? 35.587  -19.513 -30.703 1.00 41.88  ? 36  PRO   B C   1 
ATOM   1011 O O   . PRO   B 1 37 ? 34.818  -19.010 -31.544 1.00 38.97  ? 36  PRO   B O   1 
ATOM   1012 C CB  . PRO   B 1 37 ? 34.646  -20.100 -28.421 1.00 40.81  ? 36  PRO   B CB  1 
ATOM   1013 C CG  . PRO   B 1 37 ? 33.829  -19.219 -27.501 1.00 40.17  ? 36  PRO   B CG  1 
ATOM   1014 C CD  . PRO   B 1 37 ? 33.572  -17.954 -28.306 1.00 38.99  ? 36  PRO   B CD  1 
ATOM   1015 N N   . PRO   B 1 38 ? 36.502  -20.448 -31.058 1.00 39.77  ? 37  PRO   B N   1 
ATOM   1016 C CA  . PRO   B 1 38 ? 36.606  -20.942 -32.439 1.00 39.89  ? 37  PRO   B CA  1 
ATOM   1017 C C   . PRO   B 1 38 ? 35.243  -21.340 -33.005 1.00 36.03  ? 37  PRO   B C   1 
ATOM   1018 O O   . PRO   B 1 38 ? 34.440  -21.971 -32.311 1.00 38.62  ? 37  PRO   B O   1 
ATOM   1019 C CB  . PRO   B 1 38 ? 37.577  -22.150 -32.319 1.00 41.11  ? 37  PRO   B CB  1 
ATOM   1020 C CG  . PRO   B 1 38 ? 38.434  -21.802 -31.103 1.00 41.61  ? 37  PRO   B CG  1 
ATOM   1021 C CD  . PRO   B 1 38 ? 37.482  -21.074 -30.146 1.00 45.18  ? 37  PRO   B CD  1 
ATOM   1022 N N   . ASN   B 1 39 ? 34.998  -20.940 -34.259 1.00 34.67  ? 38  ASN   B N   1 
ATOM   1023 C CA  . ASN   B 1 39 ? 33.818  -21.363 -35.013 1.00 39.62  ? 38  ASN   B CA  1 
ATOM   1024 C C   . ASN   B 1 39 ? 32.549  -20.595 -34.634 1.00 36.73  ? 38  ASN   B C   1 
ATOM   1025 O O   . ASN   B 1 39 ? 31.518  -20.799 -35.269 1.00 35.88  ? 38  ASN   B O   1 
ATOM   1026 C CB  . ASN   B 1 39 ? 33.514  -22.857 -34.890 1.00 36.62  ? 38  ASN   B CB  1 
ATOM   1027 C CG  . ASN   B 1 39 ? 34.665  -23.747 -35.308 1.00 47.49  ? 38  ASN   B CG  1 
ATOM   1028 O OD1 . ASN   B 1 39 ? 35.023  -24.675 -34.573 1.00 52.48  ? 38  ASN   B OD1 1 
ATOM   1029 N ND2 . ASN   B 1 39 ? 35.251  -23.487 -36.469 1.00 42.47  ? 38  ASN   B ND2 1 
ATOM   1030 N N   . LYS   B 1 40 ? 32.597  -19.703 -33.628 1.00 33.71  ? 39  LYS   B N   1 
ATOM   1031 C CA  . LYS   B 1 40 ? 31.374  -19.065 -33.154 1.00 30.96  ? 39  LYS   B CA  1 
ATOM   1032 C C   . LYS   B 1 40 ? 31.357  -17.585 -33.502 1.00 28.99  ? 39  LYS   B C   1 
ATOM   1033 O O   . LYS   B 1 40 ? 32.399  -17.024 -33.802 1.00 33.03  ? 39  LYS   B O   1 
ATOM   1034 C CB  . LYS   B 1 40 ? 31.325  -19.291 -31.641 1.00 33.79  ? 39  LYS   B CB  1 
ATOM   1035 C CG  . LYS   B 1 40 ? 31.143  -20.765 -31.309 1.00 33.93  ? 39  LYS   B CG  1 
ATOM   1036 C CD  . LYS   B 1 40 ? 30.811  -20.912 -29.830 1.00 41.78  ? 39  LYS   B CD  1 
ATOM   1037 C CE  . LYS   B 1 40 ? 29.979  -22.105 -29.457 1.00 50.70  ? 39  LYS   B CE  1 
ATOM   1038 N NZ  . LYS   B 1 40 ? 30.481  -23.306 -30.116 1.00 48.81  ? 39  LYS   B NZ  1 
ATOM   1039 N N   . TYR   B 1 41 ? 30.173  -16.964 -33.402 1.00 27.80  ? 40  TYR   B N   1 
ATOM   1040 C CA  . TYR   B 1 41 ? 29.952  -15.551 -33.688 1.00 26.16  ? 40  TYR   B CA  1 
ATOM   1041 C C   . TYR   B 1 41 ? 29.398  -14.877 -32.446 1.00 27.49  ? 40  TYR   B C   1 
ATOM   1042 O O   . TYR   B 1 41 ? 28.648  -15.481 -31.678 1.00 26.61  ? 40  TYR   B O   1 
ATOM   1043 C CB  . TYR   B 1 41 ? 28.865  -15.465 -34.763 1.00 25.87  ? 40  TYR   B CB  1 
ATOM   1044 C CG  . TYR   B 1 41 ? 29.313  -15.935 -36.146 1.00 26.93  ? 40  TYR   B CG  1 
ATOM   1045 C CD1 . TYR   B 1 41 ? 29.936  -15.060 -37.041 1.00 26.50  ? 40  TYR   B CD1 1 
ATOM   1046 C CD2 . TYR   B 1 41 ? 29.131  -17.263 -36.534 1.00 27.64  ? 40  TYR   B CD2 1 
ATOM   1047 C CE1 . TYR   B 1 41 ? 30.373  -15.498 -38.279 1.00 30.78  ? 40  TYR   B CE1 1 
ATOM   1048 C CE2 . TYR   B 1 41 ? 29.563  -17.712 -37.772 1.00 31.10  ? 40  TYR   B CE2 1 
ATOM   1049 C CZ  . TYR   B 1 41 ? 30.204  -16.825 -38.635 1.00 30.57  ? 40  TYR   B CZ  1 
ATOM   1050 O OH  . TYR   B 1 41 ? 30.609  -17.212 -39.896 1.00 30.21  ? 40  TYR   B OH  1 
ATOM   1051 N N   . PRO   B 1 42 ? 29.645  -13.555 -32.268 1.00 28.33  ? 41  PRO   B N   1 
ATOM   1052 C CA  . PRO   B 1 42 ? 28.902  -12.795 -31.255 1.00 26.00  ? 41  PRO   B CA  1 
ATOM   1053 C C   . PRO   B 1 42 ? 27.477  -12.510 -31.715 1.00 23.46  ? 41  PRO   B C   1 
ATOM   1054 O O   . PRO   B 1 42 ? 27.269  -11.895 -32.769 1.00 24.78  ? 41  PRO   B O   1 
ATOM   1055 C CB  . PRO   B 1 42 ? 29.735  -11.482 -31.124 1.00 27.34  ? 41  PRO   B CB  1 
ATOM   1056 C CG  . PRO   B 1 42 ? 30.507  -11.364 -32.422 1.00 30.42  ? 41  PRO   B CG  1 
ATOM   1057 C CD  . PRO   B 1 42 ? 30.576  -12.752 -33.079 1.00 29.74  ? 41  PRO   B CD  1 
ATOM   1058 N N   . ILE   B 1 43 ? 26.487  -12.963 -30.920 1.00 23.61  ? 42  ILE   B N   1 
ATOM   1059 C CA  . ILE   B 1 43 ? 25.062  -12.777 -31.192 1.00 22.48  ? 42  ILE   B CA  1 
ATOM   1060 C C   . ILE   B 1 43 ? 24.489  -11.752 -30.228 1.00 22.52  ? 42  ILE   B C   1 
ATOM   1061 O O   . ILE   B 1 43 ? 24.823  -11.799 -29.051 1.00 26.45  ? 42  ILE   B O   1 
ATOM   1062 C CB  . ILE   B 1 43 ? 24.324  -14.111 -30.983 1.00 21.65  ? 42  ILE   B CB  1 
ATOM   1063 C CG1 . ILE   B 1 43 ? 25.067  -15.220 -31.761 1.00 24.44  ? 42  ILE   B CG1 1 
ATOM   1064 C CG2 . ILE   B 1 43 ? 22.866  -13.958 -31.416 1.00 24.44  ? 42  ILE   B CG2 1 
ATOM   1065 C CD1 . ILE   B 1 43 ? 25.224  -14.944 -33.244 1.00 24.66  ? 42  ILE   B CD1 1 
ATOM   1066 N N   . PHE   B 1 44 ? 23.638  -10.891 -30.757 1.00 21.03  ? 43  PHE   B N   1 
ATOM   1067 C CA  . PHE   B 1 44 ? 22.834  -9.991  -29.939 1.00 21.96  ? 43  PHE   B CA  1 
ATOM   1068 C C   . PHE   B 1 44 ? 21.397  -10.412 -30.166 1.00 20.84  ? 43  PHE   B C   1 
ATOM   1069 O O   . PHE   B 1 44 ? 20.935  -10.514 -31.313 1.00 21.57  ? 43  PHE   B O   1 
ATOM   1070 C CB  . PHE   B 1 44 ? 23.076  -8.535  -30.376 1.00 21.93  ? 43  PHE   B CB  1 
ATOM   1071 C CG  . PHE   B 1 44 ? 22.088  -7.531  -29.769 1.00 21.14  ? 43  PHE   B CG  1 
ATOM   1072 C CD1 . PHE   B 1 44 ? 20.893  -7.176  -30.416 1.00 20.33  ? 43  PHE   B CD1 1 
ATOM   1073 C CD2 . PHE   B 1 44 ? 22.346  -6.964  -28.529 1.00 25.89  ? 43  PHE   B CD2 1 
ATOM   1074 C CE1 . PHE   B 1 44 ? 20.039  -6.222  -29.850 1.00 23.18  ? 43  PHE   B CE1 1 
ATOM   1075 C CE2 . PHE   B 1 44 ? 21.458  -6.046  -27.945 1.00 22.28  ? 43  PHE   B CE2 1 
ATOM   1076 C CZ  . PHE   B 1 44 ? 20.301  -5.705  -28.607 1.00 23.40  ? 43  PHE   B CZ  1 
ATOM   1077 N N   . PHE   B 1 45 ? 20.686  -10.656 -29.045 1.00 20.48  ? 44  PHE   B N   1 
ATOM   1078 C CA  . PHE   B 1 45 ? 19.288  -11.060 -29.090 1.00 20.43  ? 44  PHE   B CA  1 
ATOM   1079 C C   . PHE   B 1 45 ? 18.401  -9.847  -28.954 1.00 20.77  ? 44  PHE   B C   1 
ATOM   1080 O O   . PHE   B 1 45 ? 18.446  -9.098  -27.958 1.00 22.19  ? 44  PHE   B O   1 
ATOM   1081 C CB  . PHE   B 1 45 ? 18.987  -12.062 -27.966 1.00 18.96  ? 44  PHE   B CB  1 
ATOM   1082 C CG  . PHE   B 1 45 ? 19.743  -13.377 -28.068 1.00 19.96  ? 44  PHE   B CG  1 
ATOM   1083 C CD1 . PHE   B 1 45 ? 21.085  -13.451 -27.714 1.00 21.12  ? 44  PHE   B CD1 1 
ATOM   1084 C CD2 . PHE   B 1 45 ? 19.141  -14.507 -28.630 1.00 19.78  ? 44  PHE   B CD2 1 
ATOM   1085 C CE1 . PHE   B 1 45 ? 21.822  -14.621 -27.877 1.00 22.97  ? 44  PHE   B CE1 1 
ATOM   1086 C CE2 . PHE   B 1 45 ? 19.883  -15.683 -28.755 1.00 21.83  ? 44  PHE   B CE2 1 
ATOM   1087 C CZ  . PHE   B 1 45 ? 21.217  -15.750 -28.420 1.00 21.38  ? 44  PHE   B CZ  1 
ATOM   1088 N N   . PHE   B 1 46 ? 17.532  -9.687  -29.931 1.00 19.53  ? 45  PHE   B N   1 
ATOM   1089 C CA  . PHE   B 1 46 ? 16.573  -8.609  -29.904 1.00 19.21  ? 45  PHE   B CA  1 
ATOM   1090 C C   . PHE   B 1 46 ? 15.588  -8.843  -28.749 1.00 21.80  ? 45  PHE   B C   1 
ATOM   1091 O O   . PHE   B 1 46 ? 15.319  -9.974  -28.351 1.00 20.71  ? 45  PHE   B O   1 
ATOM   1092 C CB  . PHE   B 1 46 ? 15.857  -8.410  -31.233 1.00 20.38  ? 45  PHE   B CB  1 
ATOM   1093 C CG  . PHE   B 1 46 ? 16.812  -7.953  -32.327 1.00 21.40  ? 45  PHE   B CG  1 
ATOM   1094 C CD1 . PHE   B 1 46 ? 17.261  -6.619  -32.300 1.00 22.68  ? 45  PHE   B CD1 1 
ATOM   1095 C CD2 . PHE   B 1 46 ? 17.174  -8.807  -33.391 1.00 21.90  ? 45  PHE   B CD2 1 
ATOM   1096 C CE1 . PHE   B 1 46 ? 18.095  -6.171  -33.343 1.00 23.61  ? 45  PHE   B CE1 1 
ATOM   1097 C CE2 . PHE   B 1 46 ? 18.013  -8.361  -34.408 1.00 20.73  ? 45  PHE   B CE2 1 
ATOM   1098 C CZ  . PHE   B 1 46 ? 18.437  -7.019  -34.378 1.00 20.35  ? 45  PHE   B CZ  1 
ATOM   1099 N N   . GLY   B 1 47 ? 15.046  -7.746  -28.239 1.00 21.93  ? 46  GLY   B N   1 
ATOM   1100 C CA  . GLY   B 1 47 ? 14.022  -7.809  -27.195 1.00 23.07  ? 46  GLY   B CA  1 
ATOM   1101 C C   . GLY   B 1 47 ? 14.640  -7.923  -25.807 1.00 24.16  ? 46  GLY   B C   1 
ATOM   1102 O O   . GLY   B 1 47 ? 14.440  -7.025  -24.964 1.00 27.11  ? 46  GLY   B O   1 
ATOM   1103 N N   . THR   B 1 48 ? 15.373  -9.012  -25.543 1.00 22.99  ? 47  THR   B N   1 
ATOM   1104 C CA  . THR   B 1 48 ? 16.085  -9.190  -24.284 1.00 23.95  ? 47  THR   B CA  1 
ATOM   1105 C C   . THR   B 1 48 ? 17.346  -8.334  -24.243 1.00 25.36  ? 47  THR   B C   1 
ATOM   1106 O O   . THR   B 1 48 ? 17.861  -8.040  -23.158 1.00 25.97  ? 47  THR   B O   1 
ATOM   1107 C CB  . THR   B 1 48 ? 16.388  -10.659 -23.955 1.00 23.90  ? 47  THR   B CB  1 
ATOM   1108 O OG1 . THR   B 1 48 ? 17.398  -11.156 -24.854 1.00 23.00  ? 47  THR   B OG1 1 
ATOM   1109 C CG2 . THR   B 1 48 ? 15.134  -11.526 -24.004 1.00 23.30  ? 47  THR   B CG2 1 
ATOM   1110 N N   . HIS   B 1 49 ? 17.924  -8.050  -25.418 1.00 22.26  ? 48  HIS   B N   1 
ATOM   1111 C CA  . HIS   B 1 49 ? 19.202  -7.345  -25.502 1.00 24.44  ? 48  HIS   B CA  1 
ATOM   1112 C C   . HIS   B 1 49 ? 20.341  -8.110  -24.845 1.00 25.46  ? 48  HIS   B C   1 
ATOM   1113 O O   . HIS   B 1 49 ? 21.354  -7.508  -24.501 1.00 30.90  ? 48  HIS   B O   1 
ATOM   1114 C CB  . HIS   B 1 49 ? 19.074  -5.875  -25.072 1.00 23.26  ? 48  HIS   B CB  1 
ATOM   1115 C CG  . HIS   B 1 49 ? 17.866  -5.220  -25.638 1.00 24.05  ? 48  HIS   B CG  1 
ATOM   1116 N ND1 . HIS   B 1 49 ? 17.105  -4.401  -24.830 1.00 30.27  ? 48  HIS   B ND1 1 
ATOM   1117 C CD2 . HIS   B 1 49 ? 17.234  -5.225  -26.834 1.00 22.01  ? 48  HIS   B CD2 1 
ATOM   1118 C CE1 . HIS   B 1 49 ? 16.042  -3.970  -25.519 1.00 31.83  ? 48  HIS   B CE1 1 
ATOM   1119 N NE2 . HIS   B 1 49 ? 16.112  -4.441  -26.776 1.00 26.58  ? 48  HIS   B NE2 1 
ATOM   1120 N N   . GLU   B 1 50 ? 20.232  -9.438  -24.737 1.00 24.26  ? 49  GLU   B N   1 
ATOM   1121 C CA  . GLU   B 1 50 ? 21.323  -10.264 -24.273 1.00 23.88  ? 49  GLU   B CA  1 
ATOM   1122 C C   . GLU   B 1 50 ? 22.324  -10.529 -25.407 1.00 22.26  ? 49  GLU   B C   1 
ATOM   1123 O O   . GLU   B 1 50 ? 22.011  -10.343 -26.582 1.00 23.91  ? 49  GLU   B O   1 
ATOM   1124 C CB  . GLU   B 1 50 ? 20.797  -11.637 -23.829 1.00 26.50  ? 49  GLU   B CB  1 
ATOM   1125 C CG  . GLU   B 1 50 ? 19.804  -11.515 -22.665 1.00 26.79  ? 49  GLU   B CG  1 
ATOM   1126 C CD  . GLU   B 1 50 ? 19.001  -12.784 -22.435 1.00 25.92  ? 49  GLU   B CD  1 
ATOM   1127 O OE1 . GLU   B 1 50 ? 18.253  -13.215 -23.345 1.00 24.87  ? 49  GLU   B OE1 1 
ATOM   1128 O OE2 . GLU   B 1 50 ? 19.109  -13.355 -21.310 1.00 27.11  ? 49  GLU   B OE2 1 
ATOM   1129 N N   . THR   B 1 51 ? 23.455  -11.082 -25.000 1.00 23.08  ? 50  THR   B N   1 
ATOM   1130 C CA  . THR   B 1 51 ? 24.512  -11.489 -25.919 1.00 25.90  ? 50  THR   B CA  1 
ATOM   1131 C C   . THR   B 1 51 ? 24.923  -12.916 -25.579 1.00 27.63  ? 50  THR   B C   1 
ATOM   1132 O O   . THR   B 1 51 ? 24.773  -13.396 -24.441 1.00 30.15  ? 50  THR   B O   1 
ATOM   1133 C CB  . THR   B 1 51 ? 25.685  -10.496 -25.962 1.00 30.60  ? 50  THR   B CB  1 
ATOM   1134 O OG1 . THR   B 1 51 ? 26.266  -10.504 -24.663 1.00 34.16  ? 50  THR   B OG1 1 
ATOM   1135 C CG2 . THR   B 1 51 ? 25.241  -9.088  -26.313 1.00 28.38  ? 50  THR   B CG2 1 
ATOM   1136 N N   . ALA   B 1 52 ? 25.396  -13.638 -26.602 1.00 26.30  ? 51  ALA   B N   1 
ATOM   1137 C CA  . ALA   B 1 52 ? 26.049  -14.913 -26.409 1.00 26.35  ? 51  ALA   B CA  1 
ATOM   1138 C C   . ALA   B 1 52 ? 26.916  -15.205 -27.630 1.00 25.89  ? 51  ALA   B C   1 
ATOM   1139 O O   . ALA   B 1 52 ? 26.834  -14.500 -28.650 1.00 28.28  ? 51  ALA   B O   1 
ATOM   1140 C CB  . ALA   B 1 52 ? 25.051  -16.038 -26.190 1.00 25.18  ? 51  ALA   B CB  1 
ATOM   1141 N N   . PHE   B 1 53 ? 27.693  -16.273 -27.512 1.00 27.05  ? 52  PHE   B N   1 
ATOM   1142 C CA  . PHE   B 1 53 ? 28.462  -16.801 -28.618 1.00 27.40  ? 52  PHE   B CA  1 
ATOM   1143 C C   . PHE   B 1 53 ? 27.794  -18.079 -29.108 1.00 28.12  ? 52  PHE   B C   1 
ATOM   1144 O O   . PHE   B 1 53 ? 27.681  -19.048 -28.343 1.00 27.91  ? 52  PHE   B O   1 
ATOM   1145 C CB  . PHE   B 1 53 ? 29.929  -17.046 -28.263 1.00 25.49  ? 52  PHE   B CB  1 
ATOM   1146 C CG  . PHE   B 1 53 ? 30.721  -15.821 -27.832 1.00 30.09  ? 52  PHE   B CG  1 
ATOM   1147 C CD1 . PHE   B 1 53 ? 31.007  -14.802 -28.730 1.00 31.46  ? 52  PHE   B CD1 1 
ATOM   1148 C CD2 . PHE   B 1 53 ? 31.195  -15.717 -26.531 1.00 34.56  ? 52  PHE   B CD2 1 
ATOM   1149 C CE1 . PHE   B 1 53 ? 31.710  -13.681 -28.328 1.00 33.61  ? 52  PHE   B CE1 1 
ATOM   1150 C CE2 . PHE   B 1 53 ? 31.922  -14.606 -26.132 1.00 34.98  ? 52  PHE   B CE2 1 
ATOM   1151 C CZ  . PHE   B 1 53 ? 32.180  -13.605 -27.031 1.00 34.53  ? 52  PHE   B CZ  1 
ATOM   1152 N N   . LEU   B 1 54 ? 27.468  -18.110 -30.410 1.00 24.74  ? 53  LEU   B N   1 
ATOM   1153 C CA  . LEU   B 1 54 ? 26.870  -19.309 -30.995 1.00 23.99  ? 53  LEU   B CA  1 
ATOM   1154 C C   . LEU   B 1 54 ? 27.568  -19.666 -32.312 1.00 24.18  ? 53  LEU   B C   1 
ATOM   1155 O O   . LEU   B 1 54 ? 28.028  -18.788 -33.044 1.00 25.12  ? 53  LEU   B O   1 
ATOM   1156 C CB  . LEU   B 1 54 ? 25.378  -19.139 -31.259 1.00 24.76  ? 53  LEU   B CB  1 
ATOM   1157 C CG  . LEU   B 1 54 ? 24.465  -18.945 -30.038 1.00 24.54  ? 53  LEU   B CG  1 
ATOM   1158 C CD1 . LEU   B 1 54 ? 23.062  -18.701 -30.528 1.00 24.33  ? 53  LEU   B CD1 1 
ATOM   1159 C CD2 . LEU   B 1 54 ? 24.546  -20.237 -29.187 1.00 27.11  ? 53  LEU   B CD2 1 
ATOM   1160 N N   . GLY   B 1 55 ? 27.496  -20.947 -32.655 1.00 24.91  ? 54  GLY   B N   1 
ATOM   1161 C CA  . GLY   B 1 55 ? 28.026  -21.459 -33.915 1.00 24.10  ? 54  GLY   B CA  1 
ATOM   1162 C C   . GLY   B 1 55 ? 26.929  -21.568 -34.977 1.00 25.55  ? 54  GLY   B C   1 
ATOM   1163 O O   . GLY   B 1 55 ? 25.735  -21.531 -34.656 1.00 24.75  ? 54  GLY   B O   1 
ATOM   1164 N N   . PRO   B 1 56 ? 27.283  -21.773 -36.269 1.00 23.10  ? 55  PRO   B N   1 
ATOM   1165 C CA  . PRO   B 1 56 ? 26.294  -21.812 -37.344 1.00 24.70  ? 55  PRO   B CA  1 
ATOM   1166 C C   . PRO   B 1 56 ? 25.137  -22.794 -37.262 1.00 20.36  ? 55  PRO   B C   1 
ATOM   1167 O O   . PRO   B 1 56 ? 24.081  -22.576 -37.847 1.00 23.03  ? 55  PRO   B O   1 
ATOM   1168 C CB  . PRO   B 1 56 ? 27.136  -22.075 -38.623 1.00 26.21  ? 55  PRO   B CB  1 
ATOM   1169 C CG  . PRO   B 1 56 ? 28.570  -21.871 -38.226 1.00 26.85  ? 55  PRO   B CG  1 
ATOM   1170 C CD  . PRO   B 1 56 ? 28.672  -21.924 -36.743 1.00 25.86  ? 55  PRO   B CD  1 
ATOM   1171 N N   . LYS   B 1 57 ? 25.359  -23.921 -36.568 1.00 24.96  ? 56  LYS   B N   1 
ATOM   1172 C CA  . LYS   B 1 57 ? 24.321  -24.940 -36.450 1.00 23.32  ? 56  LYS   B CA  1 
ATOM   1173 C C   . LYS   B 1 57 ? 23.074  -24.363 -35.778 1.00 23.86  ? 56  LYS   B C   1 
ATOM   1174 O O   . LYS   B 1 57 ? 21.943  -24.801 -36.037 1.00 23.13  ? 56  LYS   B O   1 
ATOM   1175 C CB  . LYS   B 1 57 ? 24.755  -26.209 -35.690 1.00 26.34  ? 56  LYS   B CB  1 
ATOM   1176 C CG  . LYS   B 1 57 ? 24.777  -26.014 -34.180 1.00 29.59  ? 56  LYS   B CG  1 
ATOM   1177 C CD  . LYS   B 1 57 ? 25.037  -27.383 -33.554 1.00 34.71  ? 56  LYS   B CD  1 
ATOM   1178 C CE  . LYS   B 1 57 ? 25.259  -27.378 -32.070 1.00 41.91  ? 56  LYS   B CE  1 
ATOM   1179 N NZ  . LYS   B 1 57 ? 24.110  -26.874 -31.321 1.00 36.49  ? 56  LYS   B NZ  1 
ATOM   1180 N N   . ASP   B 1 58 ? 23.287  -23.273 -35.003 1.00 22.54  ? 57  ASP   B N   1 
ATOM   1181 C CA  . ASP   B 1 58 ? 22.221  -22.644 -34.226 1.00 23.79  ? 57  ASP   B CA  1 
ATOM   1182 C C   . ASP   B 1 58 ? 21.780  -21.299 -34.815 1.00 21.69  ? 57  ASP   B C   1 
ATOM   1183 O O   . ASP   B 1 58 ? 20.975  -20.584 -34.181 1.00 21.69  ? 57  ASP   B O   1 
ATOM   1184 C CB  . ASP   B 1 58 ? 22.663  -22.473 -32.780 1.00 23.71  ? 57  ASP   B CB  1 
ATOM   1185 C CG  . ASP   B 1 58 ? 22.807  -23.798 -32.035 1.00 27.51  ? 57  ASP   B CG  1 
ATOM   1186 O OD1 . ASP   B 1 58 ? 21.910  -24.640 -32.223 1.00 27.82  ? 57  ASP   B OD1 1 
ATOM   1187 O OD2 . ASP   B 1 58 ? 23.788  -23.937 -31.270 1.00 32.38  ? 57  ASP   B OD2 1 
ATOM   1188 N N   . LEU   B 1 59 ? 22.235  -20.959 -36.040 1.00 20.84  ? 58  LEU   B N   1 
ATOM   1189 C CA  . LEU   B 1 59 ? 21.931  -19.664 -36.634 1.00 19.75  ? 58  LEU   B CA  1 
ATOM   1190 C C   . LEU   B 1 59 ? 21.209  -19.866 -37.954 1.00 20.68  ? 58  LEU   B C   1 
ATOM   1191 O O   . LEU   B 1 59 ? 21.735  -20.514 -38.867 1.00 22.24  ? 58  LEU   B O   1 
ATOM   1192 C CB  . LEU   B 1 59 ? 23.223  -18.881 -36.856 1.00 22.03  ? 58  LEU   B CB  1 
ATOM   1193 C CG  . LEU   B 1 59 ? 24.102  -18.658 -35.622 1.00 20.89  ? 58  LEU   B CG  1 
ATOM   1194 C CD1 . LEU   B 1 59 ? 25.419  -17.986 -35.962 1.00 23.30  ? 58  LEU   B CD1 1 
ATOM   1195 C CD2 . LEU   B 1 59 ? 23.318  -17.782 -34.632 1.00 23.72  ? 58  LEU   B CD2 1 
ATOM   1196 N N   . PHE   B 1 60 ? 20.037  -19.286 -38.060 1.00 18.95  ? 59  PHE   B N   1 
ATOM   1197 C CA  . PHE   B 1 60 ? 19.098  -19.464 -39.153 1.00 20.49  ? 59  PHE   B CA  1 
ATOM   1198 C C   . PHE   B 1 60 ? 18.918  -18.118 -39.842 1.00 22.74  ? 59  PHE   B C   1 
ATOM   1199 O O   . PHE   B 1 60 ? 18.361  -17.181 -39.261 1.00 21.22  ? 59  PHE   B O   1 
ATOM   1200 C CB  . PHE   B 1 60 ? 17.763  -20.021 -38.624 1.00 20.72  ? 59  PHE   B CB  1 
ATOM   1201 C CG  . PHE   B 1 60 ? 17.858  -21.413 -38.003 1.00 19.57  ? 59  PHE   B CG  1 
ATOM   1202 C CD1 . PHE   B 1 60 ? 18.365  -21.591 -36.716 1.00 21.25  ? 59  PHE   B CD1 1 
ATOM   1203 C CD2 . PHE   B 1 60 ? 17.474  -22.519 -38.748 1.00 23.17  ? 59  PHE   B CD2 1 
ATOM   1204 C CE1 . PHE   B 1 60 ? 18.504  -22.872 -36.172 1.00 21.10  ? 59  PHE   B CE1 1 
ATOM   1205 C CE2 . PHE   B 1 60 ? 17.556  -23.789 -38.188 1.00 22.21  ? 59  PHE   B CE2 1 
ATOM   1206 C CZ  . PHE   B 1 60 ? 18.125  -23.977 -36.944 1.00 24.48  ? 59  PHE   B CZ  1 
ATOM   1207 N N   . PRO   B 1 61 ? 19.404  -17.909 -41.078 1.00 22.74  ? 60  PRO   B N   1 
ATOM   1208 C CA  . PRO   B 1 61 ? 19.192  -16.614 -41.753 1.00 22.12  ? 60  PRO   B CA  1 
ATOM   1209 C C   . PRO   B 1 61 ? 17.739  -16.158 -41.690 1.00 22.28  ? 60  PRO   B C   1 
ATOM   1210 O O   . PRO   B 1 61 ? 16.790  -16.914 -41.959 1.00 25.61  ? 60  PRO   B O   1 
ATOM   1211 C CB  . PRO   B 1 61 ? 19.674  -16.885 -43.193 1.00 23.44  ? 60  PRO   B CB  1 
ATOM   1212 C CG  . PRO   B 1 61 ? 20.678  -17.987 -43.044 1.00 29.95  ? 60  PRO   B CG  1 
ATOM   1213 C CD  . PRO   B 1 61 ? 20.215  -18.867 -41.853 1.00 26.55  ? 60  PRO   B CD  1 
ATOM   1214 N N   . TYR   B 1 62 ? 17.539  -14.848 -41.373 1.00 23.42  ? 61  TYR   B N   1 
ATOM   1215 C CA  . TYR   B 1 62 ? 16.217  -14.345 -41.046 1.00 25.94  ? 61  TYR   B CA  1 
ATOM   1216 C C   . TYR   B 1 62 ? 15.231  -14.371 -42.203 1.00 25.96  ? 61  TYR   B C   1 
ATOM   1217 O O   . TYR   B 1 62 ? 14.085  -14.792 -42.024 1.00 29.90  ? 61  TYR   B O   1 
ATOM   1218 C CB  . TYR   B 1 62 ? 16.378  -12.889 -40.569 1.00 25.92  ? 61  TYR   B CB  1 
ATOM   1219 C CG  . TYR   B 1 62 ? 15.061  -12.173 -40.317 1.00 27.53  ? 61  TYR   B CG  1 
ATOM   1220 C CD1 . TYR   B 1 62 ? 14.303  -12.452 -39.189 1.00 28.74  ? 61  TYR   B CD1 1 
ATOM   1221 C CD2 . TYR   B 1 62 ? 14.615  -11.178 -41.186 1.00 31.98  ? 61  TYR   B CD2 1 
ATOM   1222 C CE1 . TYR   B 1 62 ? 13.122  -11.767 -38.949 1.00 29.26  ? 61  TYR   B CE1 1 
ATOM   1223 C CE2 . TYR   B 1 62 ? 13.428  -10.491 -40.965 1.00 33.61  ? 61  TYR   B CE2 1 
ATOM   1224 C CZ  . TYR   B 1 62 ? 12.681  -10.805 -39.844 1.00 33.37  ? 61  TYR   B CZ  1 
ATOM   1225 O OH  . TYR   B 1 62 ? 11.521  -10.151 -39.610 1.00 36.43  ? 61  TYR   B OH  1 
ATOM   1226 N N   . ASP   B 1 63 ? 15.677  -13.916 -43.394 1.00 33.06  ? 62  ASP   B N   1 
ATOM   1227 C CA  . ASP   B 1 63 ? 14.806  -13.898 -44.570 1.00 34.70  ? 62  ASP   B CA  1 
ATOM   1228 C C   . ASP   B 1 63 ? 14.248  -15.278 -44.899 1.00 30.38  ? 62  ASP   B C   1 
ATOM   1229 O O   . ASP   B 1 63 ? 13.040  -15.429 -45.038 1.00 36.19  ? 62  ASP   B O   1 
ATOM   1230 C CB  . ASP   B 1 63 ? 15.499  -13.274 -45.766 1.00 40.91  ? 62  ASP   B CB  1 
ATOM   1231 C CG  . ASP   B 1 63 ? 15.439  -11.758 -45.791 1.00 55.76  ? 62  ASP   B CG  1 
ATOM   1232 O OD1 . ASP   B 1 63 ? 14.600  -11.189 -45.039 1.00 56.41  ? 62  ASP   B OD1 1 
ATOM   1233 O OD2 . ASP   B 1 63 ? 16.238  -11.170 -46.551 1.00 67.38  ? 62  ASP   B OD2 1 
ATOM   1234 N N   . LYS   B 1 64 ? 15.137  -16.266 -44.971 1.00 33.59  ? 63  LYS   B N   1 
ATOM   1235 C CA  . LYS   B 1 64 ? 14.741  -17.633 -45.252 1.00 31.94  ? 63  LYS   B CA  1 
ATOM   1236 C C   . LYS   B 1 64 ? 13.762  -18.162 -44.202 1.00 30.84  ? 63  LYS   B C   1 
ATOM   1237 O O   . LYS   B 1 64 ? 12.826  -18.883 -44.550 1.00 32.16  ? 63  LYS   B O   1 
ATOM   1238 C CB  . LYS   B 1 64 ? 15.971  -18.534 -45.337 1.00 33.67  ? 63  LYS   B CB  1 
ATOM   1239 C CG  . LYS   B 1 64 ? 15.599  -19.958 -45.713 1.00 37.34  ? 63  LYS   B CG  1 
ATOM   1240 C CD  . LYS   B 1 64 ? 16.849  -20.815 -45.721 1.00 41.39  ? 63  LYS   B CD  1 
ATOM   1241 C CE  . LYS   B 1 64 ? 16.713  -22.202 -46.292 1.00 42.46  ? 63  LYS   B CE  1 
ATOM   1242 N NZ  . LYS   B 1 64 ? 15.458  -22.886 -46.012 1.00 43.79  ? 63  LYS   B NZ  1 
ATOM   1243 N N   . SER   B 1 65 ? 13.969  -17.799 -42.928 1.00 29.57  ? 64  SER   B N   1 
ATOM   1244 C CA  . SER   B 1 65 ? 13.295  -18.565 -41.872 1.00 27.53  ? 64  SER   B CA  1 
ATOM   1245 C C   . SER   B 1 65 ? 12.192  -17.790 -41.146 1.00 28.37  ? 64  SER   B C   1 
ATOM   1246 O O   . SER   B 1 65 ? 11.562  -18.333 -40.251 1.00 29.95  ? 64  SER   B O   1 
ATOM   1247 C CB  . SER   B 1 65 ? 14.361  -19.096 -40.942 1.00 30.71  ? 64  SER   B CB  1 
ATOM   1248 O OG  . SER   B 1 65 ? 14.989  -18.009 -40.291 1.00 38.66  ? 64  SER   B OG  1 
ATOM   1249 N N   . LYS   B 1 66 ? 11.894  -16.544 -41.539 1.00 28.53  ? 65  LYS   B N   1 
ATOM   1250 C CA  . LYS   B 1 66 ? 10.971  -15.713 -40.761 1.00 31.50  ? 65  LYS   B CA  1 
ATOM   1251 C C   . LYS   B 1 66 ? 9.524   -16.206 -40.764 1.00 31.38  ? 65  LYS   B C   1 
ATOM   1252 O O   . LYS   B 1 66 ? 8.806   -16.002 -39.787 1.00 32.55  ? 65  LYS   B O   1 
ATOM   1253 C CB  . LYS   B 1 66 ? 11.016  -14.218 -41.106 1.00 34.51  ? 65  LYS   B CB  1 
ATOM   1254 C CG  . LYS   B 1 66 ? 10.649  -13.896 -42.552 1.00 35.42  ? 65  LYS   B CG  1 
ATOM   1255 C CD  . LYS   B 1 66 ? 10.577  -12.398 -42.853 1.00 45.79  ? 65  LYS   B CD  1 
ATOM   1256 C CE  . LYS   B 1 66 ? 10.493  -12.125 -44.338 1.00 52.06  ? 65  LYS   B CE  1 
ATOM   1257 N NZ  . LYS   B 1 66 ? 9.481   -12.924 -45.058 1.00 53.90  ? 65  LYS   B NZ  1 
ATOM   1258 N N   . ASP   B 1 67 ? 9.054   -16.847 -41.831 1.00 32.95  ? 66  ASP   B N   1 
ATOM   1259 C CA  . ASP   B 1 67 ? 7.661   -17.257 -41.736 1.00 38.79  ? 66  ASP   B CA  1 
ATOM   1260 C C   . ASP   B 1 67 ? 7.493   -18.460 -40.803 1.00 38.18  ? 66  ASP   B C   1 
ATOM   1261 O O   . ASP   B 1 67 ? 6.420   -18.622 -40.220 1.00 43.00  ? 66  ASP   B O   1 
ATOM   1262 C CB  . ASP   B 1 67 ? 6.896   -17.253 -43.049 1.00 52.36  ? 66  ASP   B CB  1 
ATOM   1263 C CG  . ASP   B 1 67 ? 7.738   -17.210 -44.309 1.00 66.50  ? 66  ASP   B CG  1 
ATOM   1264 O OD1 . ASP   B 1 67 ? 7.784   -16.128 -44.936 1.00 76.27  ? 66  ASP   B OD1 1 
ATOM   1265 O OD2 . ASP   B 1 67 ? 8.329   -18.255 -44.647 1.00 82.10  ? 66  ASP   B OD2 1 
ATOM   1266 N N   . LYS   B 1 68 ? 8.556   -19.260 -40.631 1.00 34.44  ? 67  LYS   B N   1 
ATOM   1267 C CA  . LYS   B 1 68 ? 8.500   -20.383 -39.707 1.00 30.56  ? 67  LYS   B CA  1 
ATOM   1268 C C   . LYS   B 1 68 ? 8.669   -19.919 -38.252 1.00 29.93  ? 67  LYS   B C   1 
ATOM   1269 O O   . LYS   B 1 68 ? 7.923   -20.350 -37.360 1.00 30.95  ? 67  LYS   B O   1 
ATOM   1270 C CB  . LYS   B 1 68 ? 9.564   -21.413 -40.089 1.00 32.48  ? 67  LYS   B CB  1 
ATOM   1271 C CG  . LYS   B 1 68 ? 9.490   -22.722 -39.341 1.00 38.99  ? 67  LYS   B CG  1 
ATOM   1272 C CD  . LYS   B 1 68 ? 10.671  -23.586 -39.788 1.00 43.41  ? 67  LYS   B CD  1 
ATOM   1273 C CE  . LYS   B 1 68 ? 10.720  -24.934 -39.132 1.00 48.85  ? 67  LYS   B CE  1 
ATOM   1274 N NZ  . LYS   B 1 68 ? 9.549   -25.739 -39.474 1.00 51.78  ? 67  LYS   B NZ  1 
ATOM   1275 N N   . TYR   B 1 69 ? 9.646   -19.034 -38.001 1.00 27.09  ? 68  TYR   B N   1 
ATOM   1276 C CA  . TYR   B 1 69 ? 10.110  -18.776 -36.640 1.00 23.41  ? 68  TYR   B CA  1 
ATOM   1277 C C   . TYR   B 1 69 ? 9.636   -17.417 -36.122 1.00 26.76  ? 68  TYR   B C   1 
ATOM   1278 O O   . TYR   B 1 69 ? 9.820   -17.114 -34.930 1.00 26.03  ? 68  TYR   B O   1 
ATOM   1279 C CB  . TYR   B 1 69 ? 11.637  -18.858 -36.573 1.00 22.09  ? 68  TYR   B CB  1 
ATOM   1280 C CG  . TYR   B 1 69 ? 12.254  -20.211 -36.874 1.00 24.81  ? 68  TYR   B CG  1 
ATOM   1281 C CD1 . TYR   B 1 69 ? 11.698  -21.373 -36.360 1.00 25.60  ? 68  TYR   B CD1 1 
ATOM   1282 C CD2 . TYR   B 1 69 ? 13.401  -20.324 -37.659 1.00 24.02  ? 68  TYR   B CD2 1 
ATOM   1283 C CE1 . TYR   B 1 69 ? 12.250  -22.616 -36.643 1.00 25.86  ? 68  TYR   B CE1 1 
ATOM   1284 C CE2 . TYR   B 1 69 ? 13.960  -21.556 -37.961 1.00 28.30  ? 68  TYR   B CE2 1 
ATOM   1285 C CZ  . TYR   B 1 69 ? 13.379  -22.705 -37.447 1.00 30.05  ? 68  TYR   B CZ  1 
ATOM   1286 O OH  . TYR   B 1 69 ? 13.964  -23.899 -37.762 1.00 28.77  ? 68  TYR   B OH  1 
ATOM   1287 N N   . GLY   B 1 70 ? 9.080   -16.590 -37.019 1.00 28.07  ? 69  GLY   B N   1 
ATOM   1288 C CA  . GLY   B 1 70 ? 8.781   -15.197 -36.705 1.00 28.25  ? 69  GLY   B CA  1 
ATOM   1289 C C   . GLY   B 1 70 ? 7.371   -14.977 -36.157 1.00 28.91  ? 69  GLY   B C   1 
ATOM   1290 O O   . GLY   B 1 70 ? 6.843   -13.895 -36.317 1.00 32.57  ? 69  GLY   B O   1 
ATOM   1291 N N   . LYS   B 1 71 ? 6.764   -15.988 -35.526 1.00 32.34  ? 70  LYS   B N   1 
ATOM   1292 C CA  . LYS   B 1 71 ? 5.440   -15.828 -34.941 1.00 33.44  ? 70  LYS   B CA  1 
ATOM   1293 C C   . LYS   B 1 71 ? 5.564   -15.406 -33.482 1.00 34.13  ? 70  LYS   B C   1 
ATOM   1294 O O   . LYS   B 1 71 ? 6.447   -15.883 -32.750 1.00 32.86  ? 70  LYS   B O   1 
ATOM   1295 C CB  . LYS   B 1 71 ? 4.663   -17.150 -34.881 1.00 37.16  ? 70  LYS   B CB  1 
ATOM   1296 C CG  . LYS   B 1 71 ? 3.805   -17.510 -36.087 1.00 50.32  ? 70  LYS   B CG  1 
ATOM   1297 C CD  . LYS   B 1 71 ? 4.547   -17.781 -37.383 1.00 50.70  ? 70  LYS   B CD  1 
ATOM   1298 C CE  . LYS   B 1 71 ? 3.576   -18.269 -38.418 1.00 58.80  ? 70  LYS   B CE  1 
ATOM   1299 N NZ  . LYS   B 1 71 ? 3.974   -17.814 -39.753 1.00 62.64  ? 70  LYS   B NZ  1 
ATOM   1300 N N   . PRO   B 1 72 ? 4.641   -14.534 -33.003 1.00 33.00  ? 71  PRO   B N   1 
ATOM   1301 C CA  . PRO   B 1 72 ? 4.621   -14.140 -31.593 1.00 31.33  ? 71  PRO   B CA  1 
ATOM   1302 C C   . PRO   B 1 72 ? 4.418   -15.299 -30.616 1.00 31.01  ? 71  PRO   B C   1 
ATOM   1303 O O   . PRO   B 1 72 ? 3.810   -16.327 -30.946 1.00 32.61  ? 71  PRO   B O   1 
ATOM   1304 C CB  . PRO   B 1 72 ? 3.493   -13.116 -31.484 1.00 33.83  ? 71  PRO   B CB  1 
ATOM   1305 C CG  . PRO   B 1 72 ? 3.156   -12.736 -32.899 1.00 38.41  ? 71  PRO   B CG  1 
ATOM   1306 C CD  . PRO   B 1 72 ? 3.612   -13.865 -33.807 1.00 31.72  ? 71  PRO   B CD  1 
ATOM   1307 N N   . ASN   B 1 73 ? 4.976   -15.142 -29.412 1.00 30.28  ? 72  ASN   B N   1 
ATOM   1308 C CA  . ASN   B 1 73 ? 4.778   -16.128 -28.361 1.00 28.73  ? 72  ASN   B CA  1 
ATOM   1309 C C   . ASN   B 1 73 ? 4.715   -15.410 -27.003 1.00 29.97  ? 72  ASN   B C   1 
ATOM   1310 O O   . ASN   B 1 73 ? 4.757   -14.168 -26.927 1.00 35.05  ? 72  ASN   B O   1 
ATOM   1311 C CB  . ASN   B 1 73 ? 5.782   -17.290 -28.432 1.00 30.00  ? 72  ASN   B CB  1 
ATOM   1312 C CG  . ASN   B 1 73 ? 7.205   -16.849 -28.206 1.00 28.81  ? 72  ASN   B CG  1 
ATOM   1313 O OD1 . ASN   B 1 73 ? 7.474   -16.106 -27.247 1.00 28.90  ? 72  ASN   B OD1 1 
ATOM   1314 N ND2 . ASN   B 1 73 ? 8.119   -17.266 -29.085 1.00 25.98  ? 72  ASN   B ND2 1 
ATOM   1315 N N   . LYS   B 1 74 ? 4.658   -16.198 -25.931 1.00 31.84  ? 73  LYS   B N   1 
ATOM   1316 C CA  . LYS   B 1 74 ? 4.531   -15.605 -24.601 1.00 36.38  ? 73  LYS   B CA  1 
ATOM   1317 C C   . LYS   B 1 74 ? 5.859   -15.590 -23.817 1.00 36.73  ? 73  LYS   B C   1 
ATOM   1318 O O   . LYS   B 1 74 ? 5.850   -15.369 -22.599 1.00 33.05  ? 73  LYS   B O   1 
ATOM   1319 C CB  . LYS   B 1 74 ? 3.346   -16.269 -23.874 1.00 34.77  ? 73  LYS   B CB  1 
ATOM   1320 N N   . ARG   B 1 75 ? 7.012   -15.800 -24.483 1.00 26.00  ? 74  ARG   B N   1 
ATOM   1321 C CA  . ARG   B 1 75 ? 8.304   -15.652 -23.833 1.00 24.74  ? 74  ARG   B CA  1 
ATOM   1322 C C   . ARG   B 1 75 ? 8.644   -14.171 -23.675 1.00 26.23  ? 74  ARG   B C   1 
ATOM   1323 O O   . ARG   B 1 75 ? 8.523   -13.366 -24.600 1.00 26.09  ? 74  ARG   B O   1 
ATOM   1324 C CB  . ARG   B 1 75 ? 9.472   -16.378 -24.536 1.00 25.90  ? 74  ARG   B CB  1 
ATOM   1325 C CG  . ARG   B 1 75 ? 9.251   -17.870 -24.764 1.00 25.71  ? 74  ARG   B CG  1 
ATOM   1326 C CD  . ARG   B 1 75 ? 9.114   -18.632 -23.455 1.00 24.84  ? 74  ARG   B CD  1 
ATOM   1327 N NE  . ARG   B 1 75 ? 9.301   -20.077 -23.692 1.00 25.83  ? 74  ARG   B NE  1 
ATOM   1328 C CZ  . ARG   B 1 75 ? 10.411  -20.755 -23.520 1.00 23.64  ? 74  ARG   B CZ  1 
ATOM   1329 N NH1 . ARG   B 1 75 ? 11.546  -20.193 -23.109 1.00 28.18  ? 74  ARG   B NH1 1 
ATOM   1330 N NH2 . ARG   B 1 75 ? 10.394  -22.056 -23.831 1.00 29.30  ? 74  ARG   B NH2 1 
ATOM   1331 N N   . LYS   B 1 76 ? 9.059   -13.786 -22.464 1.00 25.58  ? 75  LYS   B N   1 
ATOM   1332 C CA  . LYS   B 1 76 ? 9.428   -12.415 -22.170 1.00 23.04  ? 75  LYS   B CA  1 
ATOM   1333 C C   . LYS   B 1 76 ? 10.528  -11.924 -23.135 1.00 22.55  ? 75  LYS   B C   1 
ATOM   1334 O O   . LYS   B 1 76 ? 11.616  -12.511 -23.170 1.00 24.67  ? 75  LYS   B O   1 
ATOM   1335 C CB  . LYS   B 1 76 ? 9.947   -12.362 -20.713 1.00 26.27  ? 75  LYS   B CB  1 
ATOM   1336 C CG  . LYS   B 1 76 ? 10.303  -10.931 -20.271 1.00 26.74  ? 75  LYS   B CG  1 
ATOM   1337 C CD  . LYS   B 1 76 ? 10.669  -10.820 -18.797 1.00 26.40  ? 75  LYS   B CD  1 
ATOM   1338 C CE  . LYS   B 1 76 ? 11.264  -9.469  -18.487 1.00 27.16  ? 75  LYS   B CE  1 
ATOM   1339 N NZ  . LYS   B 1 76 ? 11.319  -9.240  -17.035 1.00 33.01  ? 75  LYS   B NZ  1 
ATOM   1340 N N   . GLY   B 1 77 ? 10.199  -10.816 -23.803 1.00 22.34  ? 76  GLY   B N   1 
ATOM   1341 C CA  . GLY   B 1 77 ? 11.132  -10.126 -24.706 1.00 22.67  ? 76  GLY   B CA  1 
ATOM   1342 C C   . GLY   B 1 77 ? 10.973  -10.575 -26.158 1.00 24.60  ? 76  GLY   B C   1 
ATOM   1343 O O   . GLY   B 1 77 ? 11.506  -9.953  -27.073 1.00 22.31  ? 76  GLY   B O   1 
ATOM   1344 N N   . PHE   B 1 78 ? 10.272  -11.681 -26.393 1.00 22.43  ? 77  PHE   B N   1 
ATOM   1345 C CA  . PHE   B 1 78 ? 10.192  -12.196 -27.765 1.00 21.79  ? 77  PHE   B CA  1 
ATOM   1346 C C   . PHE   B 1 78 ? 9.451   -11.240 -28.714 1.00 23.68  ? 77  PHE   B C   1 
ATOM   1347 O O   . PHE   B 1 78 ? 9.903   -10.932 -29.828 1.00 22.42  ? 77  PHE   B O   1 
ATOM   1348 C CB  . PHE   B 1 78 ? 9.488   -13.550 -27.818 1.00 21.23  ? 77  PHE   B CB  1 
ATOM   1349 C CG  . PHE   B 1 78 ? 9.750   -14.252 -29.142 1.00 19.42  ? 77  PHE   B CG  1 
ATOM   1350 C CD1 . PHE   B 1 78 ? 10.830  -15.111 -29.252 1.00 20.75  ? 77  PHE   B CD1 1 
ATOM   1351 C CD2 . PHE   B 1 78 ? 8.815   -14.170 -30.176 1.00 23.13  ? 77  PHE   B CD2 1 
ATOM   1352 C CE1 . PHE   B 1 78 ? 11.075  -15.773 -30.469 1.00 20.76  ? 77  PHE   B CE1 1 
ATOM   1353 C CE2 . PHE   B 1 78 ? 9.057   -14.839 -31.380 1.00 24.63  ? 77  PHE   B CE2 1 
ATOM   1354 C CZ  . PHE   B 1 78 ? 10.160  -15.674 -31.482 1.00 21.62  ? 77  PHE   B CZ  1 
ATOM   1355 N N   . ASN   B 1 79 ? 8.252   -10.761 -28.366 1.00 23.07  ? 78  ASN   B N   1 
ATOM   1356 C CA  . ASN   B 1 79 ? 7.499   -9.930  -29.294 1.00 26.00  ? 78  ASN   B CA  1 
ATOM   1357 C C   . ASN   B 1 79 ? 8.191   -8.572  -29.466 1.00 27.52  ? 78  ASN   B C   1 
ATOM   1358 O O   . ASN   B 1 79 ? 8.199   -8.023  -30.580 1.00 25.98  ? 78  ASN   B O   1 
ATOM   1359 C CB  . ASN   B 1 79 ? 6.010   -9.810  -28.957 1.00 27.76  ? 78  ASN   B CB  1 
ATOM   1360 C CG  . ASN   B 1 79 ? 5.313   -11.156 -28.912 1.00 32.69  ? 78  ASN   B CG  1 
ATOM   1361 O OD1 . ASN   B 1 79 ? 5.850   -12.154 -29.412 1.00 29.03  ? 78  ASN   B OD1 1 
ATOM   1362 N ND2 . ASN   B 1 79 ? 4.173   -11.229 -28.231 1.00 33.38  ? 78  ASN   B ND2 1 
ATOM   1363 N N   . GLU   B 1 80 ? 8.831   -8.077  -28.406 1.00 24.36  ? 79  GLU   B N   1 
ATOM   1364 C CA  . GLU   B 1 80 ? 9.638   -6.867  -28.533 1.00 26.32  ? 79  GLU   B CA  1 
ATOM   1365 C C   . GLU   B 1 80 ? 10.759  -7.108  -29.548 1.00 23.87  ? 79  GLU   B C   1 
ATOM   1366 O O   . GLU   B 1 80 ? 10.994  -6.234  -30.403 1.00 24.28  ? 79  GLU   B O   1 
ATOM   1367 C CB  . GLU   B 1 80 ? 10.260  -6.458  -27.209 1.00 26.91  ? 79  GLU   B CB  1 
ATOM   1368 C CG  . GLU   B 1 80 ? 9.227   -5.952  -26.207 1.00 32.02  ? 79  GLU   B CG  1 
ATOM   1369 N N   . GLY   B 1 81 ? 11.395  -8.291  -29.440 1.00 22.57  ? 80  GLY   B N   1 
ATOM   1370 C CA  . GLY   B 1 81 ? 12.471  -8.746  -30.339 1.00 22.14  ? 80  GLY   B CA  1 
ATOM   1371 C C   . GLY   B 1 81 ? 11.989  -8.785  -31.787 1.00 21.47  ? 80  GLY   B C   1 
ATOM   1372 O O   . GLY   B 1 81 ? 12.705  -8.329  -32.698 1.00 21.46  ? 80  GLY   B O   1 
ATOM   1373 N N   . LEU   B 1 82 ? 10.771  -9.270  -32.033 1.00 21.89  ? 81  LEU   B N   1 
ATOM   1374 C CA  . LEU   B 1 82 ? 10.202  -9.260  -33.373 1.00 24.26  ? 81  LEU   B CA  1 
ATOM   1375 C C   . LEU   B 1 82 ? 10.072  -7.827  -33.889 1.00 23.90  ? 81  LEU   B C   1 
ATOM   1376 O O   . LEU   B 1 82 ? 10.284  -7.579  -35.081 1.00 23.61  ? 81  LEU   B O   1 
ATOM   1377 C CB  . LEU   B 1 82 ? 8.861   -10.006 -33.399 1.00 24.58  ? 81  LEU   B CB  1 
ATOM   1378 C CG  . LEU   B 1 82 ? 8.953   -11.527 -33.208 1.00 24.58  ? 81  LEU   B CG  1 
ATOM   1379 C CD1 . LEU   B 1 82 ? 7.540   -12.136 -33.235 1.00 24.85  ? 81  LEU   B CD1 1 
ATOM   1380 C CD2 . LEU   B 1 82 ? 9.861   -12.231 -34.232 1.00 24.90  ? 81  LEU   B CD2 1 
ATOM   1381 N N   . TRP   B 1 83 ? 9.624   -6.927  -33.012 1.00 23.19  ? 82  TRP   B N   1 
ATOM   1382 C CA  . TRP   B 1 83 ? 9.480   -5.518  -33.382 1.00 24.02  ? 82  TRP   B CA  1 
ATOM   1383 C C   . TRP   B 1 83 ? 10.832  -4.932  -33.787 1.00 24.11  ? 82  TRP   B C   1 
ATOM   1384 O O   . TRP   B 1 83 ? 10.924  -4.299  -34.843 1.00 24.50  ? 82  TRP   B O   1 
ATOM   1385 C CB  . TRP   B 1 83 ? 8.859   -4.686  -32.250 1.00 26.21  ? 82  TRP   B CB  1 
ATOM   1386 C CG  . TRP   B 1 83 ? 8.573   -3.285  -32.728 1.00 27.06  ? 82  TRP   B CG  1 
ATOM   1387 C CD1 . TRP   B 1 83 ? 7.437   -2.849  -33.337 1.00 31.27  ? 82  TRP   B CD1 1 
ATOM   1388 C CD2 . TRP   B 1 83 ? 9.508   -2.182  -32.746 1.00 30.34  ? 82  TRP   B CD2 1 
ATOM   1389 N NE1 . TRP   B 1 83 ? 7.592   -1.531  -33.713 1.00 33.90  ? 82  TRP   B NE1 1 
ATOM   1390 C CE2 . TRP   B 1 83 ? 8.845   -1.100  -33.368 1.00 31.28  ? 82  TRP   B CE2 1 
ATOM   1391 C CE3 . TRP   B 1 83 ? 10.820  -2.000  -32.281 1.00 29.28  ? 82  TRP   B CE3 1 
ATOM   1392 C CZ2 . TRP   B 1 83 ? 9.466   0.143   -33.540 1.00 29.19  ? 82  TRP   B CZ2 1 
ATOM   1393 C CZ3 . TRP   B 1 83 ? 11.424  -0.763  -32.436 1.00 31.24  ? 82  TRP   B CZ3 1 
ATOM   1394 C CH2 . TRP   B 1 83 ? 10.754  0.286   -33.066 1.00 29.46  ? 82  TRP   B CH2 1 
ATOM   1395 N N   . GLU   B 1 84 ? 11.876  -5.225  -33.017 1.00 21.81  ? 83  GLU   B N   1 
ATOM   1396 C CA  . GLU   B 1 84 ? 13.205  -4.681  -33.225 1.00 22.01  ? 83  GLU   B CA  1 
ATOM   1397 C C   . GLU   B 1 84 ? 13.809  -5.189  -34.538 1.00 23.30  ? 83  GLU   B C   1 
ATOM   1398 O O   . GLU   B 1 84 ? 14.415  -4.410  -35.281 1.00 21.93  ? 83  GLU   B O   1 
ATOM   1399 C CB  . GLU   B 1 84 ? 14.167  -4.861  -32.059 1.00 21.63  ? 83  GLU   B CB  1 
ATOM   1400 C CG  . GLU   B 1 84 ? 13.653  -4.176  -30.787 1.00 21.31  ? 83  GLU   B CG  1 
ATOM   1401 C CD  . GLU   B 1 84 ? 14.547  -4.546  -29.629 1.00 23.20  ? 83  GLU   B CD  1 
ATOM   1402 O OE1 . GLU   B 1 84 ? 15.496  -5.375  -29.690 1.00 22.64  ? 83  GLU   B OE1 1 
ATOM   1403 O OE2 . GLU   B 1 84 ? 14.298  -3.939  -28.522 1.00 25.37  ? 83  GLU   B OE2 1 
ATOM   1404 N N   . ILE   B 1 85 ? 13.692  -6.488  -34.825 1.00 22.19  ? 84  ILE   B N   1 
ATOM   1405 C CA  . ILE   B 1 85 ? 14.407  -7.018  -35.981 1.00 20.59  ? 84  ILE   B CA  1 
ATOM   1406 C C   . ILE   B 1 85 ? 13.754  -6.457  -37.254 1.00 21.64  ? 84  ILE   B C   1 
ATOM   1407 O O   . ILE   B 1 85 ? 14.434  -6.276  -38.269 1.00 22.66  ? 84  ILE   B O   1 
ATOM   1408 C CB  . ILE   B 1 85 ? 14.447  -8.564  -35.935 1.00 20.08  ? 84  ILE   B CB  1 
ATOM   1409 C CG1 . ILE   B 1 85 ? 15.500  -9.112  -36.900 1.00 20.18  ? 84  ILE   B CG1 1 
ATOM   1410 C CG2 . ILE   B 1 85 ? 13.081  -9.184  -36.224 1.00 21.82  ? 84  ILE   B CG2 1 
ATOM   1411 C CD1 . ILE   B 1 85 ? 15.897  -10.550 -36.620 1.00 22.22  ? 84  ILE   B CD1 1 
ATOM   1412 N N   . GLN   B 1 86 ? 12.449  -6.170  -37.196 1.00 22.41  ? 85  GLN   B N   1 
ATOM   1413 C CA  . GLN   B 1 86 ? 11.675  -5.621  -38.293 1.00 25.39  ? 85  GLN   B CA  1 
ATOM   1414 C C   . GLN   B 1 86 ? 11.939  -4.125  -38.457 1.00 28.92  ? 85  GLN   B C   1 
ATOM   1415 O O   . GLN   B 1 86 ? 12.140  -3.661  -39.592 1.00 29.48  ? 85  GLN   B O   1 
ATOM   1416 C CB  . GLN   B 1 86 ? 10.193  -5.936  -38.072 1.00 28.09  ? 85  GLN   B CB  1 
ATOM   1417 N N   . ASN   B 1 87 ? 11.974  -3.376  -37.340 1.00 22.22  ? 86  ASN   B N   1 
ATOM   1418 C CA  . ASN   B 1 87 ? 11.862  -1.911  -37.478 1.00 25.52  ? 86  ASN   B CA  1 
ATOM   1419 C C   . ASN   B 1 87 ? 13.184  -1.183  -37.284 1.00 23.34  ? 86  ASN   B C   1 
ATOM   1420 O O   . ASN   B 1 87 ? 13.308  -0.022  -37.729 1.00 25.61  ? 86  ASN   B O   1 
ATOM   1421 C CB  . ASN   B 1 87 ? 10.843  -1.373  -36.477 1.00 27.74  ? 86  ASN   B CB  1 
ATOM   1422 C CG  . ASN   B 1 87 ? 9.462   -1.796  -36.921 1.00 33.15  ? 86  ASN   B CG  1 
ATOM   1423 O OD1 . ASN   B 1 87 ? 8.919   -1.205  -37.855 1.00 38.37  ? 86  ASN   B OD1 1 
ATOM   1424 N ND2 . ASN   B 1 87 ? 8.896   -2.851  -36.351 1.00 34.39  ? 86  ASN   B ND2 1 
ATOM   1425 N N   . ASN   B 1 88 ? 14.129  -1.750  -36.551 1.00 23.11  ? 87  ASN   B N   1 
ATOM   1426 C CA  . ASN   B 1 88 ? 15.389  -1.062  -36.286 1.00 24.36  ? 87  ASN   B CA  1 
ATOM   1427 C C   . ASN   B 1 88 ? 16.470  -2.062  -35.883 1.00 22.21  ? 87  ASN   B C   1 
ATOM   1428 O O   . ASN   B 1 88 ? 17.074  -2.006  -34.805 1.00 22.13  ? 87  ASN   B O   1 
ATOM   1429 C CB  . ASN   B 1 88 ? 15.224  0.140   -35.359 1.00 26.62  ? 87  ASN   B CB  1 
ATOM   1430 C CG  . ASN   B 1 88 ? 16.311  1.165   -35.554 1.00 26.99  ? 87  ASN   B CG  1 
ATOM   1431 O OD1 . ASN   B 1 88 ? 17.343  0.931   -36.201 1.00 26.67  ? 87  ASN   B OD1 1 
ATOM   1432 N ND2 . ASN   B 1 88 ? 16.092  2.347   -34.987 1.00 29.65  ? 87  ASN   B ND2 1 
ATOM   1433 N N   . PRO   B 1 89 ? 16.740  -3.015  -36.801 1.00 22.18  ? 88  PRO   B N   1 
ATOM   1434 C CA  . PRO   B 1 89 ? 17.671  -4.097  -36.484 1.00 21.17  ? 88  PRO   B CA  1 
ATOM   1435 C C   . PRO   B 1 89 ? 19.117  -3.701  -36.236 1.00 20.41  ? 88  PRO   B C   1 
ATOM   1436 O O   . PRO   B 1 89 ? 19.857  -4.412  -35.610 1.00 22.87  ? 88  PRO   B O   1 
ATOM   1437 C CB  . PRO   B 1 89 ? 17.571  -5.049  -37.717 1.00 21.86  ? 88  PRO   B CB  1 
ATOM   1438 C CG  . PRO   B 1 89 ? 17.144  -4.125  -38.883 1.00 22.26  ? 88  PRO   B CG  1 
ATOM   1439 C CD  . PRO   B 1 89 ? 16.212  -3.118  -38.176 1.00 21.63  ? 88  PRO   B CD  1 
ATOM   1440 N N   . HIS   B 1 90 ? 19.527  -2.499  -36.753 1.00 21.90  ? 89  HIS   B N   1 
ATOM   1441 C CA  . HIS   B 1 90 ? 20.921  -2.091  -36.676 1.00 21.93  ? 89  HIS   B CA  1 
ATOM   1442 C C   . HIS   B 1 90 ? 21.181  -0.989  -35.636 1.00 22.27  ? 89  HIS   B C   1 
ATOM   1443 O O   . HIS   B 1 90 ? 22.316  -0.505  -35.544 1.00 23.77  ? 89  HIS   B O   1 
ATOM   1444 C CB  . HIS   B 1 90 ? 21.433  -1.642  -38.066 1.00 20.39  ? 89  HIS   B CB  1 
ATOM   1445 C CG  . HIS   B 1 90 ? 21.251  -2.752  -39.053 1.00 23.51  ? 89  HIS   B CG  1 
ATOM   1446 N ND1 . HIS   B 1 90 ? 21.893  -3.976  -38.938 1.00 23.39  ? 89  HIS   B ND1 1 
ATOM   1447 C CD2 . HIS   B 1 90 ? 20.561  -2.779  -40.216 1.00 21.88  ? 89  HIS   B CD2 1 
ATOM   1448 C CE1 . HIS   B 1 90 ? 21.558  -4.726  -39.997 1.00 21.20  ? 89  HIS   B CE1 1 
ATOM   1449 N NE2 . HIS   B 1 90 ? 20.786  -4.017  -40.786 1.00 22.48  ? 89  HIS   B NE2 1 
ATOM   1450 N N   . ALA   B 1 91 ? 20.209  -0.752  -34.763 1.00 22.50  ? 90  ALA   B N   1 
ATOM   1451 C CA  . ALA   B 1 91 ? 20.331  0.286   -33.742 1.00 24.06  ? 90  ALA   B CA  1 
ATOM   1452 C C   . ALA   B 1 91 ? 21.291  -0.108  -32.612 1.00 26.14  ? 90  ALA   B C   1 
ATOM   1453 O O   . ALA   B 1 91 ? 21.590  -1.275  -32.356 1.00 25.64  ? 90  ALA   B O   1 
ATOM   1454 C CB  . ALA   B 1 91 ? 18.952  0.658   -33.240 1.00 24.34  ? 90  ALA   B CB  1 
ATOM   1455 N N   . SER   B 1 92 ? 21.757  0.907   -31.850 1.00 27.03  ? 91  SER   B N   1 
ATOM   1456 C CA  . SER   B 1 92 ? 22.407  0.687   -30.571 1.00 29.48  ? 91  SER   B CA  1 
ATOM   1457 C C   . SER   B 1 92 ? 21.303  0.507   -29.523 1.00 30.57  ? 91  SER   B C   1 
ATOM   1458 O O   . SER   B 1 92 ? 20.411  1.363   -29.446 1.00 32.04  ? 91  SER   B O   1 
ATOM   1459 C CB  . SER   B 1 92 ? 23.230  1.958   -30.219 1.00 28.97  ? 91  SER   B CB  1 
ATOM   1460 O OG  . SER   B 1 92 ? 23.764  1.809   -28.916 1.00 40.43  ? 91  SER   B OG  1 
ATOM   1461 N N   . TYR   B 1 93 ? 21.365  -0.626  -28.795 1.00 31.18  ? 92  TYR   B N   1 
ATOM   1462 C CA  . TYR   B 1 93 ? 20.456  -1.040  -27.739 1.00 34.04  ? 92  TYR   B CA  1 
ATOM   1463 C C   . TYR   B 1 93 ? 21.161  -0.963  -26.385 1.00 44.02  ? 92  TYR   B C   1 
ATOM   1464 O O   . TYR   B 1 93 ? 20.565  -1.298  -25.361 1.00 45.70  ? 92  TYR   B O   1 
ATOM   1465 C CB  . TYR   B 1 93 ? 19.911  -2.443  -28.031 1.00 27.73  ? 92  TYR   B CB  1 
ATOM   1466 C CG  . TYR   B 1 93 ? 18.922  -2.376  -29.180 1.00 25.45  ? 92  TYR   B CG  1 
ATOM   1467 C CD1 . TYR   B 1 93 ? 17.610  -1.974  -28.936 1.00 25.66  ? 92  TYR   B CD1 1 
ATOM   1468 C CD2 . TYR   B 1 93 ? 19.277  -2.695  -30.496 1.00 26.21  ? 92  TYR   B CD2 1 
ATOM   1469 C CE1 . TYR   B 1 93 ? 16.680  -1.822  -29.944 1.00 25.01  ? 92  TYR   B CE1 1 
ATOM   1470 C CE2 . TYR   B 1 93 ? 18.345  -2.562  -31.519 1.00 25.98  ? 92  TYR   B CE2 1 
ATOM   1471 C CZ  . TYR   B 1 93 ? 17.046  -2.159  -31.242 1.00 26.58  ? 92  TYR   B CZ  1 
ATOM   1472 O OH  . TYR   B 1 93 ? 16.092  -2.042  -32.201 1.00 28.12  ? 92  TYR   B OH  1 
ATOM   1473 N N   . SER   B 1 94 ? 22.423  -0.504  -26.403 1.00 53.64  ? 93  SER   B N   1 
ATOM   1474 C CA  . SER   B 1 94 ? 23.085  0.086   -25.246 1.00 63.36  ? 93  SER   B CA  1 
ATOM   1475 C C   . SER   B 1 94 ? 22.220  1.236   -24.701 1.00 69.32  ? 93  SER   B C   1 
ATOM   1476 O O   . SER   B 1 94 ? 22.369  2.368   -25.220 1.00 76.72  ? 93  SER   B O   1 
ATOM   1477 C CB  . SER   B 1 94 ? 24.463  0.598   -25.609 1.00 64.45  ? 93  SER   B CB  1 
ATOM   1478 O OG  . SER   B 1 94 ? 25.324  -0.463  -25.997 1.00 63.73  ? 93  SER   B OG  1 
ATOM   1479 O OXT . SER   B 1 94 ? 21.408  0.965   -23.791 1.00 68.87  ? 93  SER   B OXT 1 
ATOM   1480 N N   . HIS   C 1 4  ? 33.635  -23.533 27.481  1.00 76.66  ? 3   HIS   C N   1 
ATOM   1481 C CA  . HIS   C 1 4  ? 32.254  -22.983 27.390  1.00 72.02  ? 3   HIS   C CA  1 
ATOM   1482 C C   . HIS   C 1 4  ? 31.488  -23.351 28.660  1.00 76.88  ? 3   HIS   C C   1 
ATOM   1483 O O   . HIS   C 1 4  ? 32.009  -24.079 29.504  1.00 75.44  ? 3   HIS   C O   1 
ATOM   1484 C CB  . HIS   C 1 4  ? 31.583  -23.486 26.108  1.00 63.71  ? 3   HIS   C CB  1 
ATOM   1485 N N   . ALA   C 1 5  ? 30.254  -22.840 28.791  1.00 73.71  ? 4   ALA   C N   1 
ATOM   1486 C CA  . ALA   C 1 5  ? 29.382  -23.217 29.894  1.00 71.37  ? 4   ALA   C CA  1 
ATOM   1487 C C   . ALA   C 1 5  ? 27.912  -23.029 29.529  1.00 76.52  ? 4   ALA   C C   1 
ATOM   1488 O O   . ALA   C 1 5  ? 27.533  -22.007 28.957  1.00 81.88  ? 4   ALA   C O   1 
ATOM   1489 C CB  . ALA   C 1 5  ? 29.711  -22.399 31.101  1.00 79.12  ? 4   ALA   C CB  1 
ATOM   1490 N N   . PHE   C 1 6  ? 27.091  -24.009 29.927  1.00 63.83  ? 5   PHE   C N   1 
ATOM   1491 C CA  . PHE   C 1 6  ? 25.689  -24.033 29.552  1.00 54.73  ? 5   PHE   C CA  1 
ATOM   1492 C C   . PHE   C 1 6  ? 24.830  -24.102 30.805  1.00 57.06  ? 5   PHE   C C   1 
ATOM   1493 O O   . PHE   C 1 6  ? 25.056  -24.944 31.672  1.00 67.16  ? 5   PHE   C O   1 
ATOM   1494 C CB  . PHE   C 1 6  ? 25.388  -25.222 28.626  1.00 48.26  ? 5   PHE   C CB  1 
ATOM   1495 C CG  . PHE   C 1 6  ? 26.218  -25.257 27.346  1.00 42.95  ? 5   PHE   C CG  1 
ATOM   1496 C CD1 . PHE   C 1 6  ? 27.393  -25.999 27.270  1.00 41.70  ? 5   PHE   C CD1 1 
ATOM   1497 C CD2 . PHE   C 1 6  ? 25.864  -24.481 26.244  1.00 42.01  ? 5   PHE   C CD2 1 
ATOM   1498 C CE1 . PHE   C 1 6  ? 28.156  -26.029 26.101  1.00 46.90  ? 5   PHE   C CE1 1 
ATOM   1499 C CE2 . PHE   C 1 6  ? 26.617  -24.515 25.082  1.00 39.63  ? 5   PHE   C CE2 1 
ATOM   1500 C CZ  . PHE   C 1 6  ? 27.769  -25.278 25.006  1.00 41.95  ? 5   PHE   C CZ  1 
ATOM   1501 N N   . LYS   C 1 7  ? 23.840  -23.213 30.880  1.00 48.97  ? 6   LYS   C N   1 
ATOM   1502 C CA  . LYS   C 1 7  ? 22.900  -23.202 31.989  1.00 48.89  ? 6   LYS   C CA  1 
ATOM   1503 C C   . LYS   C 1 7  ? 21.564  -23.674 31.437  1.00 38.58  ? 6   LYS   C C   1 
ATOM   1504 O O   . LYS   C 1 7  ? 21.367  -23.652 30.220  1.00 39.61  ? 6   LYS   C O   1 
ATOM   1505 C CB  . LYS   C 1 7  ? 22.770  -21.814 32.641  1.00 49.09  ? 6   LYS   C CB  1 
ATOM   1506 N N   . PRO   C 1 8  ? 20.604  -24.104 32.278  1.00 41.83  ? 7   PRO   C N   1 
ATOM   1507 C CA  . PRO   C 1 8  ? 19.264  -24.415 31.786  1.00 42.94  ? 7   PRO   C CA  1 
ATOM   1508 C C   . PRO   C 1 8  ? 18.753  -23.238 30.956  1.00 49.16  ? 7   PRO   C C   1 
ATOM   1509 O O   . PRO   C 1 8  ? 19.004  -22.073 31.299  1.00 49.57  ? 7   PRO   C O   1 
ATOM   1510 C CB  . PRO   C 1 8  ? 18.465  -24.665 33.073  1.00 48.71  ? 7   PRO   C CB  1 
ATOM   1511 C CG  . PRO   C 1 8  ? 19.514  -25.218 34.023  1.00 45.56  ? 7   PRO   C CG  1 
ATOM   1512 C CD  . PRO   C 1 8  ? 20.775  -24.410 33.712  1.00 40.95  ? 7   PRO   C CD  1 
ATOM   1513 N N   . GLY   C 1 9  ? 18.108  -23.574 29.828  1.00 41.34  ? 8   GLY   C N   1 
ATOM   1514 C CA  . GLY   C 1 9  ? 17.371  -22.619 29.009  1.00 42.32  ? 8   GLY   C CA  1 
ATOM   1515 C C   . GLY   C 1 9  ? 18.176  -22.106 27.815  1.00 39.81  ? 8   GLY   C C   1 
ATOM   1516 O O   . GLY   C 1 9  ? 17.574  -21.569 26.878  1.00 42.66  ? 8   GLY   C O   1 
ATOM   1517 N N   . ASP   C 1 10 ? 19.513  -22.263 27.870  1.00 39.22  ? 9   ASP   C N   1 
ATOM   1518 C CA  . ASP   C 1 10 ? 20.430  -21.949 26.793  1.00 36.22  ? 9   ASP   C CA  1 
ATOM   1519 C C   . ASP   C 1 10 ? 20.070  -22.691 25.507  1.00 38.18  ? 9   ASP   C C   1 
ATOM   1520 O O   . ASP   C 1 10 ? 19.768  -23.884 25.511  1.00 33.83  ? 9   ASP   C O   1 
ATOM   1521 C CB  . ASP   C 1 10 ? 21.888  -22.214 27.128  1.00 40.31  ? 9   ASP   C CB  1 
ATOM   1522 C CG  . ASP   C 1 10 ? 22.516  -21.325 28.195  1.00 51.26  ? 9   ASP   C CG  1 
ATOM   1523 O OD1 . ASP   C 1 10 ? 21.868  -20.342 28.587  1.00 54.01  ? 9   ASP   C OD1 1 
ATOM   1524 O OD2 . ASP   C 1 10 ? 23.644  -21.637 28.632  1.00 52.43  ? 9   ASP   C OD2 1 
ATOM   1525 N N   . LEU   C 1 11 ? 20.133  -21.953 24.396  1.00 34.02  ? 10  LEU   C N   1 
ATOM   1526 C CA  . LEU   C 1 11 ? 19.736  -22.487 23.110  1.00 30.29  ? 10  LEU   C CA  1 
ATOM   1527 C C   . LEU   C 1 11 ? 20.989  -22.964 22.418  1.00 27.68  ? 10  LEU   C C   1 
ATOM   1528 O O   . LEU   C 1 11 ? 22.021  -22.292 22.436  1.00 29.60  ? 10  LEU   C O   1 
ATOM   1529 C CB  . LEU   C 1 11 ? 19.094  -21.326 22.350  1.00 29.32  ? 10  LEU   C CB  1 
ATOM   1530 C CG  . LEU   C 1 11 ? 17.806  -20.815 22.983  1.00 28.75  ? 10  LEU   C CG  1 
ATOM   1531 C CD1 . LEU   C 1 11 ? 17.265  -19.822 21.956  1.00 31.05  ? 10  LEU   C CD1 1 
ATOM   1532 C CD2 . LEU   C 1 11 ? 16.847  -21.944 23.286  1.00 29.95  ? 10  LEU   C CD2 1 
ATOM   1533 N N   . VAL   C 1 12 ? 20.903  -24.152 21.776  1.00 25.53  ? 11  VAL   C N   1 
ATOM   1534 C CA  . VAL   C 1 12 ? 22.097  -24.764 21.212  1.00 26.45  ? 11  VAL   C CA  1 
ATOM   1535 C C   . VAL   C 1 12 ? 21.710  -25.517 19.911  1.00 24.69  ? 11  VAL   C C   1 
ATOM   1536 O O   . VAL   C 1 12 ? 20.512  -25.733 19.667  1.00 24.55  ? 11  VAL   C O   1 
ATOM   1537 C CB  . VAL   C 1 12 ? 22.807  -25.733 22.197  1.00 26.94  ? 11  VAL   C CB  1 
ATOM   1538 C CG1 . VAL   C 1 12 ? 23.184  -25.066 23.524  1.00 30.69  ? 11  VAL   C CG1 1 
ATOM   1539 C CG2 . VAL   C 1 12 ? 21.972  -26.973 22.494  1.00 27.80  ? 11  VAL   C CG2 1 
ATOM   1540 N N   . PHE   C 1 13 ? 22.748  -25.909 19.155  1.00 25.92  ? 12  PHE   C N   1 
ATOM   1541 C CA  . PHE   C 1 13 ? 22.666  -27.096 18.309  1.00 22.95  ? 12  PHE   C CA  1 
ATOM   1542 C C   . PHE   C 1 13 ? 23.383  -28.260 18.990  1.00 24.55  ? 12  PHE   C C   1 
ATOM   1543 O O   . PHE   C 1 13 ? 24.482  -28.146 19.567  1.00 25.44  ? 12  PHE   C O   1 
ATOM   1544 C CB  . PHE   C 1 13 ? 23.293  -26.900 16.913  1.00 27.74  ? 12  PHE   C CB  1 
ATOM   1545 C CG  . PHE   C 1 13 ? 22.539  -25.872 16.079  1.00 27.90  ? 12  PHE   C CG  1 
ATOM   1546 C CD1 . PHE   C 1 13 ? 21.501  -26.269 15.235  1.00 25.48  ? 12  PHE   C CD1 1 
ATOM   1547 C CD2 . PHE   C 1 13 ? 22.851  -24.515 16.167  1.00 28.13  ? 12  PHE   C CD2 1 
ATOM   1548 C CE1 . PHE   C 1 13 ? 20.787  -25.315 14.522  1.00 30.09  ? 12  PHE   C CE1 1 
ATOM   1549 C CE2 . PHE   C 1 13 ? 22.133  -23.580 15.456  1.00 31.24  ? 12  PHE   C CE2 1 
ATOM   1550 C CZ  . PHE   C 1 13 ? 21.106  -23.988 14.635  1.00 30.82  ? 12  PHE   C CZ  1 
ATOM   1551 N N   . ALA   C 1 14 ? 22.709  -29.423 18.972  1.00 22.80  ? 13  ALA   C N   1 
ATOM   1552 C CA  . ALA   C 1 14 ? 23.157  -30.607 19.692  1.00 21.38  ? 13  ALA   C CA  1 
ATOM   1553 C C   . ALA   C 1 14 ? 23.440  -31.724 18.697  1.00 21.95  ? 13  ALA   C C   1 
ATOM   1554 O O   . ALA   C 1 14 ? 22.596  -32.045 17.869  1.00 21.74  ? 13  ALA   C O   1 
ATOM   1555 C CB  . ALA   C 1 14 ? 22.087  -31.041 20.656  1.00 20.68  ? 13  ALA   C CB  1 
ATOM   1556 N N   . LYS   C 1 15 ? 24.635  -32.276 18.784  1.00 22.31  ? 14  LYS   C N   1 
ATOM   1557 C CA  . LYS   C 1 15 ? 25.024  -33.287 17.805  1.00 21.60  ? 14  LYS   C CA  1 
ATOM   1558 C C   . LYS   C 1 15 ? 25.054  -34.669 18.434  1.00 21.45  ? 14  LYS   C C   1 
ATOM   1559 O O   . LYS   C 1 15 ? 25.831  -34.925 19.365  1.00 25.58  ? 14  LYS   C O   1 
ATOM   1560 C CB  . LYS   C 1 15 ? 26.434  -32.991 17.272  1.00 23.55  ? 14  LYS   C CB  1 
ATOM   1561 C CG  . LYS   C 1 15 ? 26.941  -33.929 16.163  1.00 26.16  ? 14  LYS   C CG  1 
ATOM   1562 C CD  . LYS   C 1 15 ? 26.056  -33.884 14.899  1.00 24.03  ? 14  LYS   C CD  1 
ATOM   1563 C CE  . LYS   C 1 15 ? 26.563  -34.728 13.716  1.00 27.99  ? 14  LYS   C CE  1 
ATOM   1564 N NZ  . LYS   C 1 15 ? 26.341  -36.156 13.929  1.00 27.15  ? 14  LYS   C NZ  1 
ATOM   1565 N N   . MET   C 1 16 ? 24.285  -35.591 17.860  1.00 20.91  ? 15  MET   C N   1 
ATOM   1566 C CA  . MET   C 1 16 ? 24.315  -37.024 18.190  1.00 20.66  ? 15  MET   C CA  1 
ATOM   1567 C C   . MET   C 1 16 ? 24.754  -37.813 16.965  1.00 25.09  ? 15  MET   C C   1 
ATOM   1568 O O   . MET   C 1 16 ? 24.399  -37.461 15.834  1.00 23.22  ? 15  MET   C O   1 
ATOM   1569 C CB  . MET   C 1 16 ? 22.931  -37.518 18.634  1.00 24.86  ? 15  MET   C CB  1 
ATOM   1570 C CG  . MET   C 1 16 ? 22.517  -36.801 19.894  1.00 27.83  ? 15  MET   C CG  1 
ATOM   1571 S SD  . MET   C 1 16 ? 21.000  -37.498 20.559  1.00 32.42  ? 15  MET   C SD  1 
ATOM   1572 C CE  . MET   C 1 16 ? 21.436  -39.176 21.042  1.00 31.62  ? 15  MET   C CE  1 
ATOM   1573 N N   . LYS   C 1 17 ? 25.501  -38.913 17.190  1.00 24.52  ? 16  LYS   C N   1 
ATOM   1574 C CA  . LYS   C 1 17 ? 25.809  -39.849 16.111  1.00 27.50  ? 16  LYS   C CA  1 
ATOM   1575 C C   . LYS   C 1 17 ? 24.525  -40.292 15.404  1.00 21.98  ? 16  LYS   C C   1 
ATOM   1576 O O   . LYS   C 1 17 ? 23.578  -40.739 16.051  1.00 26.04  ? 16  LYS   C O   1 
ATOM   1577 C CB  . LYS   C 1 17 ? 26.573  -41.040 16.708  1.00 25.39  ? 16  LYS   C CB  1 
ATOM   1578 C CG  . LYS   C 1 17 ? 27.135  -42.019 15.681  1.00 31.30  ? 16  LYS   C CG  1 
ATOM   1579 C CD  . LYS   C 1 17 ? 28.299  -41.272 15.044  1.00 32.79  ? 16  LYS   C CD  1 
ATOM   1580 C CE  . LYS   C 1 17 ? 29.083  -42.204 14.162  1.00 44.40  ? 16  LYS   C CE  1 
ATOM   1581 N NZ  . LYS   C 1 17 ? 30.301  -41.578 13.655  1.00 40.51  ? 16  LYS   C NZ  1 
ATOM   1582 N N   . GLY   C 1 18 ? 24.564  -40.171 14.060  1.00 24.29  ? 17  GLY   C N   1 
ATOM   1583 C CA  . GLY   C 1 18 ? 23.472  -40.619 13.212  1.00 25.85  ? 17  GLY   C CA  1 
ATOM   1584 C C   . GLY   C 1 18 ? 22.496  -39.491 12.858  1.00 24.56  ? 17  GLY   C C   1 
ATOM   1585 O O   . GLY   C 1 18 ? 21.508  -39.766 12.166  1.00 25.47  ? 17  GLY   C O   1 
ATOM   1586 N N   . TYR   C 1 19 ? 22.791  -38.261 13.314  1.00 23.50  ? 18  TYR   C N   1 
ATOM   1587 C CA  . TYR   C 1 19 ? 21.829  -37.155 13.152  1.00 22.48  ? 18  TYR   C CA  1 
ATOM   1588 C C   . TYR   C 1 19 ? 22.574  -35.869 12.866  1.00 21.92  ? 18  TYR   C C   1 
ATOM   1589 O O   . TYR   C 1 19 ? 23.688  -35.665 13.355  1.00 23.05  ? 18  TYR   C O   1 
ATOM   1590 C CB  . TYR   C 1 19 ? 20.955  -36.856 14.391  1.00 22.27  ? 18  TYR   C CB  1 
ATOM   1591 C CG  . TYR   C 1 19 ? 20.249  -38.141 14.806  1.00 22.82  ? 18  TYR   C CG  1 
ATOM   1592 C CD1 . TYR   C 1 19 ? 20.870  -39.034 15.672  1.00 23.34  ? 18  TYR   C CD1 1 
ATOM   1593 C CD2 . TYR   C 1 19 ? 18.993  -38.458 14.294  1.00 23.86  ? 18  TYR   C CD2 1 
ATOM   1594 C CE1 . TYR   C 1 19 ? 20.275  -40.214 16.050  1.00 25.82  ? 18  TYR   C CE1 1 
ATOM   1595 C CE2 . TYR   C 1 19 ? 18.408  -39.670 14.644  1.00 28.26  ? 18  TYR   C CE2 1 
ATOM   1596 C CZ  . TYR   C 1 19 ? 19.042  -40.519 15.537  1.00 28.46  ? 18  TYR   C CZ  1 
ATOM   1597 O OH  . TYR   C 1 19 ? 18.561  -41.744 15.959  1.00 34.03  ? 18  TYR   C OH  1 
ATOM   1598 N N   . PRO   C 1 20 ? 21.997  -34.944 12.067  1.00 21.50  ? 19  PRO   C N   1 
ATOM   1599 C CA  . PRO   C 1 20 ? 22.633  -33.643 11.879  1.00 21.71  ? 19  PRO   C CA  1 
ATOM   1600 C C   . PRO   C 1 20 ? 22.605  -32.818 13.166  1.00 22.15  ? 19  PRO   C C   1 
ATOM   1601 O O   . PRO   C 1 20 ? 21.827  -33.080 14.070  1.00 21.52  ? 19  PRO   C O   1 
ATOM   1602 C CB  . PRO   C 1 20 ? 21.774  -33.012 10.766  1.00 24.46  ? 19  PRO   C CB  1 
ATOM   1603 C CG  . PRO   C 1 20 ? 20.437  -33.585 10.996  1.00 23.43  ? 19  PRO   C CG  1 
ATOM   1604 C CD  . PRO   C 1 20 ? 20.689  -35.041 11.391  1.00 20.97  ? 19  PRO   C CD  1 
ATOM   1605 N N   . HIS   C 1 21 ? 23.461  -31.798 13.213  1.00 22.03  ? 20  HIS   C N   1 
ATOM   1606 C CA  . HIS   C 1 21 ? 23.419  -30.859 14.332  1.00 22.22  ? 20  HIS   C CA  1 
ATOM   1607 C C   . HIS   C 1 21 ? 22.000  -30.307 14.482  1.00 22.87  ? 20  HIS   C C   1 
ATOM   1608 O O   . HIS   C 1 21 ? 21.460  -29.754 13.526  1.00 22.92  ? 20  HIS   C O   1 
ATOM   1609 C CB  . HIS   C 1 21 ? 24.402  -29.716 14.081  1.00 25.99  ? 20  HIS   C CB  1 
ATOM   1610 C CG  . HIS   C 1 21 ? 25.825  -30.183 14.053  1.00 26.49  ? 20  HIS   C CG  1 
ATOM   1611 N ND1 . HIS   C 1 21 ? 26.481  -30.854 13.044  1.00 30.90  ? 20  HIS   C ND1 1 
ATOM   1612 C CD2 . HIS   C 1 21 ? 26.743  -29.993 15.037  1.00 28.59  ? 20  HIS   C CD2 1 
ATOM   1613 C CE1 . HIS   C 1 21 ? 27.742  -31.073 13.415  1.00 31.86  ? 20  HIS   C CE1 1 
ATOM   1614 N NE2 . HIS   C 1 21 ? 27.924  -30.559 14.613  1.00 30.86  ? 20  HIS   C NE2 1 
ATOM   1615 N N   . TRP   C 1 22 ? 21.418  -30.447 15.689  1.00 19.78  ? 21  TRP   C N   1 
ATOM   1616 C CA  . TRP   C 1 22 ? 19.968  -30.326 15.804  1.00 19.07  ? 21  TRP   C CA  1 
ATOM   1617 C C   . TRP   C 1 22 ? 19.593  -29.162 16.716  1.00 21.24  ? 21  TRP   C C   1 
ATOM   1618 O O   . TRP   C 1 22 ? 20.194  -28.992 17.794  1.00 21.37  ? 21  TRP   C O   1 
ATOM   1619 C CB  . TRP   C 1 22 ? 19.417  -31.644 16.372  1.00 19.08  ? 21  TRP   C CB  1 
ATOM   1620 C CG  . TRP   C 1 22 ? 17.963  -31.848 16.048  1.00 20.70  ? 21  TRP   C CG  1 
ATOM   1621 C CD1 . TRP   C 1 22 ? 16.894  -31.241 16.646  1.00 22.89  ? 21  TRP   C CD1 1 
ATOM   1622 C CD2 . TRP   C 1 22 ? 17.426  -32.732 15.039  1.00 20.70  ? 21  TRP   C CD2 1 
ATOM   1623 N NE1 . TRP   C 1 22 ? 15.723  -31.656 16.048  1.00 22.26  ? 21  TRP   C NE1 1 
ATOM   1624 C CE2 . TRP   C 1 22 ? 16.016  -32.577 15.073  1.00 21.41  ? 21  TRP   C CE2 1 
ATOM   1625 C CE3 . TRP   C 1 22 ? 18.013  -33.619 14.136  1.00 20.70  ? 21  TRP   C CE3 1 
ATOM   1626 C CZ2 . TRP   C 1 22 ? 15.204  -33.299 14.186  1.00 21.14  ? 21  TRP   C CZ2 1 
ATOM   1627 C CZ3 . TRP   C 1 22 ? 17.216  -34.327 13.250  1.00 21.43  ? 21  TRP   C CZ3 1 
ATOM   1628 C CH2 . TRP   C 1 22 ? 15.822  -34.148 13.299  1.00 22.88  ? 21  TRP   C CH2 1 
ATOM   1629 N N   . PRO   C 1 23 ? 18.573  -28.335 16.363  1.00 21.42  ? 22  PRO   C N   1 
ATOM   1630 C CA  . PRO   C 1 23 ? 18.202  -27.254 17.271  1.00 21.15  ? 22  PRO   C CA  1 
ATOM   1631 C C   . PRO   C 1 23 ? 17.656  -27.818 18.579  1.00 20.21  ? 22  PRO   C C   1 
ATOM   1632 O O   . PRO   C 1 23 ? 16.786  -28.689 18.591  1.00 21.87  ? 22  PRO   C O   1 
ATOM   1633 C CB  . PRO   C 1 23 ? 17.115  -26.516 16.434  1.00 24.33  ? 22  PRO   C CB  1 
ATOM   1634 C CG  . PRO   C 1 23 ? 16.568  -27.549 15.472  1.00 22.90  ? 22  PRO   C CG  1 
ATOM   1635 C CD  . PRO   C 1 23 ? 17.818  -28.321 15.078  1.00 21.31  ? 22  PRO   C CD  1 
ATOM   1636 N N   . ALA   C 1 24 ? 18.157  -27.271 19.689  1.00 22.62  ? 23  ALA   C N   1 
ATOM   1637 C CA  . ALA   C 1 24 ? 17.844  -27.820 21.008  1.00 24.25  ? 23  ALA   C CA  1 
ATOM   1638 C C   . ALA   C 1 24 ? 18.006  -26.739 22.076  1.00 28.17  ? 23  ALA   C C   1 
ATOM   1639 O O   . ALA   C 1 24 ? 18.479  -25.625 21.810  1.00 27.88  ? 23  ALA   C O   1 
ATOM   1640 C CB  . ALA   C 1 24 ? 18.763  -29.034 21.301  1.00 24.75  ? 23  ALA   C CB  1 
ATOM   1641 N N   . ARG   C 1 25 ? 17.717  -27.126 23.326  1.00 28.00  ? 24  ARG   C N   1 
ATOM   1642 C CA  . ARG   C 1 25 ? 18.077  -26.285 24.461  1.00 26.87  ? 24  ARG   C CA  1 
ATOM   1643 C C   . ARG   C 1 25 ? 18.515  -27.156 25.643  1.00 25.35  ? 24  ARG   C C   1 
ATOM   1644 O O   . ARG   C 1 25 ? 18.169  -28.346 25.707  1.00 28.10  ? 24  ARG   C O   1 
ATOM   1645 C CB  . ARG   C 1 25 ? 16.865  -25.482 24.935  1.00 30.34  ? 24  ARG   C CB  1 
ATOM   1646 C CG  . ARG   C 1 25 ? 15.598  -26.249 25.274  1.00 34.93  ? 24  ARG   C CG  1 
ATOM   1647 C CD  . ARG   C 1 25 ? 14.596  -25.279 25.939  1.00 36.30  ? 24  ARG   C CD  1 
ATOM   1648 N NE  . ARG   C 1 25 ? 13.424  -26.051 26.364  1.00 40.99  ? 24  ARG   C NE  1 
ATOM   1649 C CZ  . ARG   C 1 25 ? 12.144  -25.932 26.014  1.00 45.59  ? 24  ARG   C CZ  1 
ATOM   1650 N NH1 . ARG   C 1 25 ? 11.712  -24.868 25.363  1.00 41.47  ? 24  ARG   C NH1 1 
ATOM   1651 N NH2 . ARG   C 1 25 ? 11.283  -26.871 26.370  1.00 51.02  ? 24  ARG   C NH2 1 
ATOM   1652 N N   . ILE   C 1 26 ? 19.254  -26.520 26.546  1.00 29.60  ? 25  ILE   C N   1 
ATOM   1653 C CA  . ILE   C 1 26 ? 19.675  -27.136 27.791  1.00 29.69  ? 25  ILE   C CA  1 
ATOM   1654 C C   . ILE   C 1 26 ? 18.485  -27.057 28.724  1.00 36.44  ? 25  ILE   C C   1 
ATOM   1655 O O   . ILE   C 1 26 ? 17.981  -25.952 28.953  1.00 34.97  ? 25  ILE   C O   1 
ATOM   1656 C CB  . ILE   C 1 26 ? 20.867  -26.366 28.385  1.00 30.08  ? 25  ILE   C CB  1 
ATOM   1657 C CG1 . ILE   C 1 26 ? 21.994  -26.116 27.385  1.00 35.19  ? 25  ILE   C CG1 1 
ATOM   1658 C CG2 . ILE   C 1 26 ? 21.364  -27.058 29.664  1.00 34.43  ? 25  ILE   C CG2 1 
ATOM   1659 C CD1 . ILE   C 1 26 ? 22.760  -27.337 26.937  1.00 36.94  ? 25  ILE   C CD1 1 
ATOM   1660 N N   . ASP   C 1 27 ? 18.030  -28.206 29.219  1.00 36.33  ? 26  ASP   C N   1 
ATOM   1661 C CA  . ASP   C 1 27 ? 16.999  -28.256 30.242  1.00 41.73  ? 26  ASP   C CA  1 
ATOM   1662 C C   . ASP   C 1 27 ? 17.618  -28.287 31.637  1.00 46.54  ? 26  ASP   C C   1 
ATOM   1663 O O   . ASP   C 1 27 ? 18.834  -28.421 31.783  1.00 43.57  ? 26  ASP   C O   1 
ATOM   1664 C CB  . ASP   C 1 27 ? 16.097  -29.458 30.036  1.00 42.36  ? 26  ASP   C CB  1 
ATOM   1665 C CG  . ASP   C 1 27 ? 14.876  -29.194 29.176  1.00 47.93  ? 26  ASP   C CG  1 
ATOM   1666 O OD1 . ASP   C 1 27 ? 14.758  -28.054 28.669  1.00 44.52  ? 26  ASP   C OD1 1 
ATOM   1667 O OD2 . ASP   C 1 27 ? 14.037  -30.114 29.083  1.00 56.90  ? 26  ASP   C OD2 1 
ATOM   1668 N N   . ASP   C 1 28 ? 16.767  -28.146 32.661  1.00 56.98  ? 27  ASP   C N   1 
ATOM   1669 C CA  . ASP   C 1 28 ? 17.178  -28.406 34.034  1.00 63.40  ? 27  ASP   C CA  1 
ATOM   1670 C C   . ASP   C 1 28 ? 16.684  -29.800 34.413  1.00 60.33  ? 27  ASP   C C   1 
ATOM   1671 O O   . ASP   C 1 28 ? 15.812  -30.338 33.736  1.00 60.38  ? 27  ASP   C O   1 
ATOM   1672 C CB  . ASP   C 1 28 ? 16.752  -27.289 34.980  1.00 68.46  ? 27  ASP   C CB  1 
ATOM   1673 C CG  . ASP   C 1 28 ? 17.561  -27.127 36.265  1.00 67.08  ? 27  ASP   C CG  1 
ATOM   1674 O OD1 . ASP   C 1 28 ? 18.331  -28.048 36.627  1.00 56.92  ? 27  ASP   C OD1 1 
ATOM   1675 O OD2 . ASP   C 1 28 ? 17.438  -26.058 36.893  1.00 68.19  ? 27  ASP   C OD2 1 
ATOM   1676 N N   . ILE   C 1 29 ? 17.277  -30.384 35.466  1.00 55.73  ? 28  ILE   C N   1 
ATOM   1677 C CA  . ILE   C 1 29 ? 16.856  -31.674 35.994  1.00 57.30  ? 28  ILE   C CA  1 
ATOM   1678 C C   . ILE   C 1 29 ? 16.039  -31.421 37.257  1.00 52.15  ? 28  ILE   C C   1 
ATOM   1679 O O   . ILE   C 1 29 ? 16.416  -30.570 38.062  1.00 48.71  ? 28  ILE   C O   1 
ATOM   1680 C CB  . ILE   C 1 29 ? 18.082  -32.556 36.299  1.00 55.21  ? 28  ILE   C CB  1 
ATOM   1681 N N   . ALA   C 1 30 ? 14.925  -32.152 37.422  1.00 51.35  ? 29  ALA   C N   1 
ATOM   1682 C CA  . ALA   C 1 30 ? 14.167  -32.117 38.669  1.00 49.29  ? 29  ALA   C CA  1 
ATOM   1683 C C   . ALA   C 1 30 ? 15.016  -32.673 39.821  1.00 48.81  ? 29  ALA   C C   1 
ATOM   1684 O O   . ALA   C 1 30 ? 15.649  -33.765 39.633  1.00 42.34  ? 29  ALA   C O   1 
ATOM   1685 C CB  . ALA   C 1 30 ? 12.861  -32.883 38.523  1.00 49.96  ? 29  ALA   C CB  1 
ATOM   1686 N N   . LYS   C 1 35 ? 19.726  -38.769 37.767  1.00 53.83  ? 34  LYS   C N   1 
ATOM   1687 C CA  . LYS   C 1 35 ? 20.972  -37.974 37.589  1.00 50.39  ? 34  LYS   C CA  1 
ATOM   1688 C C   . LYS   C 1 35 ? 21.503  -38.203 36.175  1.00 46.67  ? 34  LYS   C C   1 
ATOM   1689 O O   . LYS   C 1 35 ? 21.486  -39.329 35.674  1.00 51.08  ? 34  LYS   C O   1 
ATOM   1690 C CB  . LYS   C 1 35 ? 22.036  -38.368 38.625  1.00 54.46  ? 34  LYS   C CB  1 
ATOM   1691 N N   . PRO   C 1 36 ? 22.007  -37.151 35.491  1.00 41.38  ? 35  PRO   C N   1 
ATOM   1692 C CA  . PRO   C 1 36 ? 22.694  -37.348 34.216  1.00 38.85  ? 35  PRO   C CA  1 
ATOM   1693 C C   . PRO   C 1 36 ? 23.870  -38.290 34.477  1.00 45.12  ? 35  PRO   C C   1 
ATOM   1694 O O   . PRO   C 1 36 ? 24.327  -38.444 35.618  1.00 44.11  ? 35  PRO   C O   1 
ATOM   1695 C CB  . PRO   C 1 36 ? 23.160  -35.930 33.828  1.00 45.43  ? 35  PRO   C CB  1 
ATOM   1696 C CG  . PRO   C 1 36 ? 22.276  -35.002 34.640  1.00 45.51  ? 35  PRO   C CG  1 
ATOM   1697 C CD  . PRO   C 1 36 ? 21.973  -35.746 35.932  1.00 43.15  ? 35  PRO   C CD  1 
ATOM   1698 N N   . PRO   C 1 37 ? 24.415  -38.955 33.438  1.00 37.41  ? 36  PRO   C N   1 
ATOM   1699 C CA  . PRO   C 1 37 ? 25.731  -39.561 33.566  1.00 37.60  ? 36  PRO   C CA  1 
ATOM   1700 C C   . PRO   C 1 37 ? 26.665  -38.410 33.898  1.00 35.31  ? 36  PRO   C C   1 
ATOM   1701 O O   . PRO   C 1 37 ? 26.358  -37.232 33.665  1.00 33.20  ? 36  PRO   C O   1 
ATOM   1702 C CB  . PRO   C 1 37 ? 26.004  -40.145 32.166  1.00 35.70  ? 36  PRO   C CB  1 
ATOM   1703 C CG  . PRO   C 1 37 ? 24.610  -40.400 31.643  1.00 38.21  ? 36  PRO   C CG  1 
ATOM   1704 C CD  . PRO   C 1 37 ? 23.796  -39.217 32.130  1.00 37.05  ? 36  PRO   C CD  1 
ATOM   1705 N N   . PRO   C 1 38 ? 27.845  -38.739 34.457  1.00 33.00  ? 37  PRO   C N   1 
ATOM   1706 C CA  . PRO   C 1 38 ? 28.897  -37.751 34.663  1.00 30.78  ? 37  PRO   C CA  1 
ATOM   1707 C C   . PRO   C 1 38 ? 29.165  -36.823 33.485  1.00 29.14  ? 37  PRO   C C   1 
ATOM   1708 O O   . PRO   C 1 38 ? 29.472  -37.267 32.377  1.00 28.35  ? 37  PRO   C O   1 
ATOM   1709 C CB  . PRO   C 1 38 ? 30.102  -38.688 34.993  1.00 32.37  ? 37  PRO   C CB  1 
ATOM   1710 C CG  . PRO   C 1 38 ? 29.443  -39.834 35.707  1.00 33.45  ? 37  PRO   C CG  1 
ATOM   1711 C CD  . PRO   C 1 38 ? 28.193  -40.099 34.916  1.00 35.43  ? 37  PRO   C CD  1 
ATOM   1712 N N   . ASN   C 1 39 ? 29.026  -35.511 33.765  1.00 29.76  ? 38  ASN   C N   1 
ATOM   1713 C CA  . ASN   C 1 39 ? 29.436  -34.425 32.898  1.00 31.14  ? 38  ASN   C CA  1 
ATOM   1714 C C   . ASN   C 1 39 ? 28.534  -34.353 31.669  1.00 31.45  ? 38  ASN   C C   1 
ATOM   1715 O O   . ASN   C 1 39 ? 29.015  -33.971 30.606  1.00 37.09  ? 38  ASN   C O   1 
ATOM   1716 C CB  . ASN   C 1 39 ? 30.901  -34.510 32.487  1.00 34.88  ? 38  ASN   C CB  1 
ATOM   1717 C CG  . ASN   C 1 39 ? 31.413  -33.222 31.885  1.00 42.27  ? 38  ASN   C CG  1 
ATOM   1718 O OD1 . ASN   C 1 39 ? 30.958  -32.131 32.255  1.00 55.20  ? 38  ASN   C OD1 1 
ATOM   1719 N ND2 . ASN   C 1 39 ? 32.323  -33.316 30.925  1.00 44.63  ? 38  ASN   C ND2 1 
ATOM   1720 N N   . LYS   C 1 40 ? 27.269  -34.769 31.816  1.00 27.49  ? 39  LYS   C N   1 
ATOM   1721 C CA  . LYS   C 1 40 ? 26.338  -34.657 30.707  1.00 27.09  ? 39  LYS   C CA  1 
ATOM   1722 C C   . LYS   C 1 40 ? 25.195  -33.719 31.068  1.00 29.00  ? 39  LYS   C C   1 
ATOM   1723 O O   . LYS   C 1 40 ? 24.770  -33.604 32.203  1.00 31.19  ? 39  LYS   C O   1 
ATOM   1724 C CB  . LYS   C 1 40 ? 25.704  -36.004 30.346  1.00 26.57  ? 39  LYS   C CB  1 
ATOM   1725 C CG  . LYS   C 1 40 ? 26.670  -37.092 29.919  1.00 30.29  ? 39  LYS   C CG  1 
ATOM   1726 C CD  . LYS   C 1 40 ? 27.674  -36.837 28.816  1.00 33.78  ? 39  LYS   C CD  1 
ATOM   1727 C CE  . LYS   C 1 40 ? 28.324  -38.167 28.502  1.00 35.78  ? 39  LYS   C CE  1 
ATOM   1728 N NZ  . LYS   C 1 40 ? 29.382  -37.952 27.503  1.00 42.51  ? 39  LYS   C NZ  1 
ATOM   1729 N N   . TYR   C 1 41 ? 24.671  -33.063 30.033  1.00 26.07  ? 40  TYR   C N   1 
ATOM   1730 C CA  . TYR   C 1 41 ? 23.577  -32.107 30.188  1.00 26.88  ? 40  TYR   C CA  1 
ATOM   1731 C C   . TYR   C 1 41 ? 22.297  -32.759 29.700  1.00 26.48  ? 40  TYR   C C   1 
ATOM   1732 O O   . TYR   C 1 41 ? 22.326  -33.530 28.729  1.00 27.71  ? 40  TYR   C O   1 
ATOM   1733 C CB  . TYR   C 1 41 ? 23.756  -30.884 29.280  1.00 25.78  ? 40  TYR   C CB  1 
ATOM   1734 C CG  . TYR   C 1 41 ? 24.926  -30.000 29.674  1.00 27.45  ? 40  TYR   C CG  1 
ATOM   1735 C CD1 . TYR   C 1 41 ? 26.207  -30.267 29.198  1.00 28.49  ? 40  TYR   C CD1 1 
ATOM   1736 C CD2 . TYR   C 1 41 ? 24.754  -28.911 30.527  1.00 30.76  ? 40  TYR   C CD2 1 
ATOM   1737 C CE1 . TYR   C 1 41 ? 27.293  -29.489 29.563  1.00 36.59  ? 40  TYR   C CE1 1 
ATOM   1738 C CE2 . TYR   C 1 41 ? 25.828  -28.097 30.849  1.00 30.21  ? 40  TYR   C CE2 1 
ATOM   1739 C CZ  . TYR   C 1 41 ? 27.096  -28.404 30.402  1.00 34.21  ? 40  TYR   C CZ  1 
ATOM   1740 O OH  . TYR   C 1 41 ? 28.166  -27.617 30.728  1.00 46.17  ? 40  TYR   C OH  1 
ATOM   1741 N N   . PRO   C 1 42 ? 21.142  -32.428 30.322  1.00 28.81  ? 41  PRO   C N   1 
ATOM   1742 C CA  . PRO   C 1 42 ? 19.832  -32.801 29.782  1.00 25.99  ? 41  PRO   C CA  1 
ATOM   1743 C C   . PRO   C 1 42 ? 19.517  -31.845 28.642  1.00 25.95  ? 41  PRO   C C   1 
ATOM   1744 O O   . PRO   C 1 42 ? 19.582  -30.618 28.808  1.00 27.13  ? 41  PRO   C O   1 
ATOM   1745 C CB  . PRO   C 1 42 ? 18.835  -32.622 30.929  1.00 30.57  ? 41  PRO   C CB  1 
ATOM   1746 C CG  . PRO   C 1 42 ? 19.643  -31.960 32.012  1.00 33.06  ? 41  PRO   C CG  1 
ATOM   1747 C CD  . PRO   C 1 42 ? 21.042  -31.608 31.552  1.00 30.15  ? 41  PRO   C CD  1 
ATOM   1748 N N   . ILE   C 1 43 ? 19.233  -32.461 27.496  1.00 24.96  ? 42  ILE   C N   1 
ATOM   1749 C CA  . ILE   C 1 43 ? 18.946  -31.707 26.280  1.00 22.67  ? 42  ILE   C CA  1 
ATOM   1750 C C   . ILE   C 1 43 ? 17.516  -31.962 25.884  1.00 23.73  ? 42  ILE   C C   1 
ATOM   1751 O O   . ILE   C 1 43 ? 17.013  -33.084 25.922  1.00 26.36  ? 42  ILE   C O   1 
ATOM   1752 C CB  . ILE   C 1 43 ? 19.868  -32.175 25.153  1.00 23.91  ? 42  ILE   C CB  1 
ATOM   1753 C CG1 . ILE   C 1 43 ? 21.341  -31.990 25.534  1.00 25.35  ? 42  ILE   C CG1 1 
ATOM   1754 C CG2 . ILE   C 1 43 ? 19.482  -31.444 23.851  1.00 23.08  ? 42  ILE   C CG2 1 
ATOM   1755 C CD1 . ILE   C 1 43 ? 21.735  -30.578 25.941  1.00 27.20  ? 42  ILE   C CD1 1 
ATOM   1756 N N   . PHE   C 1 44 ? 16.865  -30.864 25.430  1.00 26.40  ? 43  PHE   C N   1 
ATOM   1757 C CA  . PHE   C 1 44 ? 15.566  -31.015 24.798  1.00 27.09  ? 43  PHE   C CA  1 
ATOM   1758 C C   . PHE   C 1 44 ? 15.699  -30.623 23.324  1.00 23.43  ? 43  PHE   C C   1 
ATOM   1759 O O   . PHE   C 1 44 ? 16.283  -29.565 23.041  1.00 25.54  ? 43  PHE   C O   1 
ATOM   1760 C CB  . PHE   C 1 44 ? 14.565  -30.035 25.433  1.00 27.91  ? 43  PHE   C CB  1 
ATOM   1761 C CG  . PHE   C 1 44 ? 13.179  -30.015 24.797  1.00 28.52  ? 43  PHE   C CG  1 
ATOM   1762 C CD1 . PHE   C 1 44 ? 12.229  -31.013 25.076  1.00 29.84  ? 43  PHE   C CD1 1 
ATOM   1763 C CD2 . PHE   C 1 44 ? 12.826  -28.987 23.900  1.00 31.09  ? 43  PHE   C CD2 1 
ATOM   1764 C CE1 . PHE   C 1 44 ? 10.955  -30.992 24.493  1.00 33.49  ? 43  PHE   C CE1 1 
ATOM   1765 C CE2 . PHE   C 1 44 ? 11.555  -28.973 23.313  1.00 29.11  ? 43  PHE   C CE2 1 
ATOM   1766 C CZ  . PHE   C 1 44 ? 10.624  -29.959 23.617  1.00 31.15  ? 43  PHE   C CZ  1 
ATOM   1767 N N   . PHE   C 1 45 ? 15.217  -31.501 22.439  1.00 22.64  ? 44  PHE   C N   1 
ATOM   1768 C CA  . PHE   C 1 45 ? 15.372  -31.286 20.998  1.00 24.86  ? 44  PHE   C CA  1 
ATOM   1769 C C   . PHE   C 1 45 ? 14.103  -30.659 20.451  1.00 24.54  ? 44  PHE   C C   1 
ATOM   1770 O O   . PHE   C 1 45 ? 13.004  -31.227 20.594  1.00 25.02  ? 44  PHE   C O   1 
ATOM   1771 C CB  . PHE   C 1 45 ? 15.614  -32.632 20.302  1.00 22.77  ? 44  PHE   C CB  1 
ATOM   1772 C CG  . PHE   C 1 45 ? 16.970  -33.232 20.642  1.00 24.09  ? 44  PHE   C CG  1 
ATOM   1773 C CD1 . PHE   C 1 45 ? 18.098  -32.970 19.854  1.00 23.54  ? 44  PHE   C CD1 1 
ATOM   1774 C CD2 . PHE   C 1 45 ? 17.100  -34.083 21.741  1.00 22.73  ? 44  PHE   C CD2 1 
ATOM   1775 C CE1 . PHE   C 1 45 ? 19.338  -33.514 20.175  1.00 24.35  ? 44  PHE   C CE1 1 
ATOM   1776 C CE2 . PHE   C 1 45 ? 18.356  -34.598 22.058  1.00 26.99  ? 44  PHE   C CE2 1 
ATOM   1777 C CZ  . PHE   C 1 45 ? 19.449  -34.363 21.246  1.00 22.69  ? 44  PHE   C CZ  1 
ATOM   1778 N N   . PHE   C 1 46 ? 14.280  -29.491 19.800  1.00 24.00  ? 45  PHE   C N   1 
ATOM   1779 C CA  . PHE   C 1 46 ? 13.125  -28.908 19.129  1.00 23.44  ? 45  PHE   C CA  1 
ATOM   1780 C C   . PHE   C 1 46 ? 12.631  -29.772 17.965  1.00 25.26  ? 45  PHE   C C   1 
ATOM   1781 O O   . PHE   C 1 46 ? 13.370  -30.538 17.336  1.00 24.04  ? 45  PHE   C O   1 
ATOM   1782 C CB  . PHE   C 1 46 ? 13.372  -27.452 18.717  1.00 23.69  ? 45  PHE   C CB  1 
ATOM   1783 C CG  . PHE   C 1 46 ? 13.687  -26.474 19.843  1.00 23.77  ? 45  PHE   C CG  1 
ATOM   1784 C CD1 . PHE   C 1 46 ? 12.658  -26.009 20.664  1.00 27.27  ? 45  PHE   C CD1 1 
ATOM   1785 C CD2 . PHE   C 1 46 ? 14.985  -25.977 20.043  1.00 24.37  ? 45  PHE   C CD2 1 
ATOM   1786 C CE1 . PHE   C 1 46 ? 12.958  -25.086 21.672  1.00 26.69  ? 45  PHE   C CE1 1 
ATOM   1787 C CE2 . PHE   C 1 46 ? 15.282  -25.080 21.068  1.00 28.04  ? 45  PHE   C CE2 1 
ATOM   1788 C CZ  . PHE   C 1 46 ? 14.259  -24.629 21.883  1.00 25.63  ? 45  PHE   C CZ  1 
ATOM   1789 N N   . GLY   C 1 47 ? 11.328  -29.661 17.683  1.00 23.12  ? 46  GLY   C N   1 
ATOM   1790 C CA  . GLY   C 1 47 ? 10.738  -30.350 16.547  1.00 28.03  ? 46  GLY   C CA  1 
ATOM   1791 C C   . GLY   C 1 47 ? 10.289  -31.766 16.902  1.00 30.24  ? 46  GLY   C C   1 
ATOM   1792 O O   . GLY   C 1 47 ? 9.111   -32.110 16.823  1.00 35.52  ? 46  GLY   C O   1 
ATOM   1793 N N   . THR   C 1 48 ? 11.241  -32.600 17.331  1.00 27.76  ? 47  THR   C N   1 
ATOM   1794 C CA  . THR   C 1 48 ? 10.869  -33.931 17.789  1.00 29.81  ? 47  THR   C CA  1 
ATOM   1795 C C   . THR   C 1 48 ? 10.401  -33.886 19.253  1.00 28.83  ? 47  THR   C C   1 
ATOM   1796 O O   . THR   C 1 48 ? 9.706   -34.805 19.707  1.00 31.69  ? 47  THR   C O   1 
ATOM   1797 C CB  . THR   C 1 48 ? 12.032  -34.915 17.606  1.00 25.89  ? 47  THR   C CB  1 
ATOM   1798 O OG1 . THR   C 1 48 ? 12.966  -34.450 18.585  1.00 28.98  ? 47  THR   C OG1 1 
ATOM   1799 C CG2 . THR   C 1 48 ? 12.573  -35.039 16.187  1.00 26.28  ? 47  THR   C CG2 1 
ATOM   1800 N N   . HIS   C 1 49 ? 10.809  -32.876 20.015  1.00 29.55  ? 48  HIS   C N   1 
ATOM   1801 C CA  . HIS   C 1 49 ? 10.484  -32.771 21.437  1.00 30.95  ? 48  HIS   C CA  1 
ATOM   1802 C C   . HIS   C 1 49 ? 10.976  -33.979 22.242  1.00 30.68  ? 48  HIS   C C   1 
ATOM   1803 O O   . HIS   C 1 49 ? 10.383  -34.307 23.276  1.00 35.00  ? 48  HIS   C O   1 
ATOM   1804 C CB  . HIS   C 1 49 ? 8.982   -32.518 21.650  1.00 33.21  ? 48  HIS   C CB  1 
ATOM   1805 C CG  . HIS   C 1 49 ? 8.452   -31.457 20.737  1.00 35.53  ? 48  HIS   C CG  1 
ATOM   1806 N ND1 . HIS   C 1 49 ? 7.383   -31.690 19.894  1.00 40.66  ? 48  HIS   C ND1 1 
ATOM   1807 C CD2 . HIS   C 1 49 ? 8.894   -30.221 20.457  1.00 34.50  ? 48  HIS   C CD2 1 
ATOM   1808 C CE1 . HIS   C 1 49 ? 7.162   -30.602 19.160  1.00 37.89  ? 48  HIS   C CE1 1 
ATOM   1809 N NE2 . HIS   C 1 49 ? 8.070   -29.699 19.485  1.00 37.89  ? 48  HIS   C NE2 1 
ATOM   1810 N N   . GLU   C 1 50 ? 12.062  -34.609 21.794  1.00 29.84  ? 49  GLU   C N   1 
ATOM   1811 C CA  . GLU   C 1 50 ? 12.729  -35.655 22.560  1.00 29.09  ? 49  GLU   C CA  1 
ATOM   1812 C C   . GLU   C 1 50 ? 13.738  -35.080 23.554  1.00 28.35  ? 49  GLU   C C   1 
ATOM   1813 O O   . GLU   C 1 50 ? 14.127  -33.918 23.505  1.00 29.34  ? 49  GLU   C O   1 
ATOM   1814 C CB  . GLU   C 1 50 ? 13.464  -36.597 21.614  1.00 28.31  ? 49  GLU   C CB  1 
ATOM   1815 C CG  . GLU   C 1 50 ? 12.542  -37.309 20.626  1.00 30.92  ? 49  GLU   C CG  1 
ATOM   1816 C CD  . GLU   C 1 50 ? 13.349  -37.842 19.458  1.00 38.41  ? 49  GLU   C CD  1 
ATOM   1817 O OE1 . GLU   C 1 50 ? 14.145  -37.055 18.925  1.00 38.09  ? 49  GLU   C OE1 1 
ATOM   1818 O OE2 . GLU   C 1 50 ? 13.214  -39.006 19.079  1.00 43.76  ? 49  GLU   C OE2 1 
ATOM   1819 N N   . THR   C 1 51 ? 14.146  -35.947 24.499  1.00 29.97  ? 50  THR   C N   1 
ATOM   1820 C CA  . THR   C 1 51 ? 15.216  -35.648 25.448  1.00 30.71  ? 50  THR   C CA  1 
ATOM   1821 C C   . THR   C 1 51 ? 16.337  -36.689 25.348  1.00 27.73  ? 50  THR   C C   1 
ATOM   1822 O O   . THR   C 1 51 ? 16.161  -37.830 24.923  1.00 30.27  ? 50  THR   C O   1 
ATOM   1823 C CB  . THR   C 1 51 ? 14.669  -35.513 26.873  1.00 38.04  ? 50  THR   C CB  1 
ATOM   1824 O OG1 . THR   C 1 51 ? 13.987  -36.744 27.134  1.00 36.42  ? 50  THR   C OG1 1 
ATOM   1825 C CG2 . THR   C 1 51 ? 13.766  -34.305 27.072  1.00 33.67  ? 50  THR   C CG2 1 
ATOM   1826 N N   . ALA   C 1 52 ? 17.533  -36.228 25.714  1.00 27.24  ? 51  ALA   C N   1 
ATOM   1827 C CA  . ALA   C 1 52 ? 18.690  -37.096 25.845  1.00 27.51  ? 51  ALA   C CA  1 
ATOM   1828 C C   . ALA   C 1 52 ? 19.713  -36.397 26.733  1.00 29.22  ? 51  ALA   C C   1 
ATOM   1829 O O   . ALA   C 1 52 ? 19.557  -35.225 27.084  1.00 30.66  ? 51  ALA   C O   1 
ATOM   1830 C CB  . ALA   C 1 52 ? 19.290  -37.353 24.490  1.00 26.66  ? 51  ALA   C CB  1 
ATOM   1831 N N   . PHE   C 1 53 ? 20.770  -37.130 27.125  1.00 28.79  ? 52  PHE   C N   1 
ATOM   1832 C CA  . PHE   C 1 53 ? 21.894  -36.536 27.841  1.00 28.14  ? 52  PHE   C CA  1 
ATOM   1833 C C   . PHE   C 1 53 ? 23.095  -36.452 26.902  1.00 28.12  ? 52  PHE   C C   1 
ATOM   1834 O O   . PHE   C 1 53 ? 23.472  -37.434 26.267  1.00 28.90  ? 52  PHE   C O   1 
ATOM   1835 C CB  . PHE   C 1 53 ? 22.285  -37.440 29.023  1.00 26.24  ? 52  PHE   C CB  1 
ATOM   1836 C CG  . PHE   C 1 53 ? 21.279  -37.403 30.153  1.00 28.94  ? 52  PHE   C CG  1 
ATOM   1837 C CD1 . PHE   C 1 53 ? 20.903  -36.213 30.757  1.00 30.54  ? 52  PHE   C CD1 1 
ATOM   1838 C CD2 . PHE   C 1 53 ? 20.689  -38.588 30.601  1.00 37.27  ? 52  PHE   C CD2 1 
ATOM   1839 C CE1 . PHE   C 1 53 ? 19.985  -36.196 31.807  1.00 34.80  ? 52  PHE   C CE1 1 
ATOM   1840 C CE2 . PHE   C 1 53 ? 19.756  -38.560 31.646  1.00 37.84  ? 52  PHE   C CE2 1 
ATOM   1841 C CZ  . PHE   C 1 53 ? 19.410  -37.368 32.243  1.00 36.13  ? 52  PHE   C CZ  1 
ATOM   1842 N N   . LEU   C 1 54 ? 23.747  -35.294 26.850  1.00 24.46  ? 53  LEU   C N   1 
ATOM   1843 C CA  . LEU   C 1 54 ? 24.890  -35.110 25.964  1.00 23.73  ? 53  LEU   C CA  1 
ATOM   1844 C C   . LEU   C 1 54 ? 25.997  -34.319 26.656  1.00 26.83  ? 53  LEU   C C   1 
ATOM   1845 O O   . LEU   C 1 54 ? 25.721  -33.479 27.506  1.00 27.36  ? 53  LEU   C O   1 
ATOM   1846 C CB  . LEU   C 1 54 ? 24.489  -34.381 24.679  1.00 25.15  ? 53  LEU   C CB  1 
ATOM   1847 C CG  . LEU   C 1 54 ? 23.549  -35.134 23.734  1.00 27.04  ? 53  LEU   C CG  1 
ATOM   1848 C CD1 . LEU   C 1 54 ? 23.240  -34.222 22.558  1.00 26.46  ? 53  LEU   C CD1 1 
ATOM   1849 C CD2 . LEU   C 1 54 ? 24.237  -36.419 23.231  1.00 33.38  ? 53  LEU   C CD2 1 
ATOM   1850 N N   . GLY   C 1 55 ? 27.237  -34.608 26.272  1.00 28.60  ? 54  GLY   C N   1 
ATOM   1851 C CA  . GLY   C 1 55 ? 28.387  -33.895 26.802  1.00 28.41  ? 54  GLY   C CA  1 
ATOM   1852 C C   . GLY   C 1 55 ? 28.642  -32.592 26.058  1.00 33.63  ? 54  GLY   C C   1 
ATOM   1853 O O   . GLY   C 1 55 ? 28.130  -32.351 24.957  1.00 31.23  ? 54  GLY   C O   1 
ATOM   1854 N N   . PRO   C 1 56 ? 29.468  -31.702 26.645  1.00 32.48  ? 55  PRO   C N   1 
ATOM   1855 C CA  . PRO   C 1 56 ? 29.697  -30.372 26.095  1.00 33.29  ? 55  PRO   C CA  1 
ATOM   1856 C C   . PRO   C 1 56 ? 30.313  -30.395 24.703  1.00 32.35  ? 55  PRO   C C   1 
ATOM   1857 O O   . PRO   C 1 56 ? 30.099  -29.456 23.934  1.00 42.94  ? 55  PRO   C O   1 
ATOM   1858 C CB  . PRO   C 1 56 ? 30.611  -29.692 27.156  1.00 37.29  ? 55  PRO   C CB  1 
ATOM   1859 C CG  . PRO   C 1 56 ? 31.279  -30.862 27.824  1.00 37.66  ? 55  PRO   C CG  1 
ATOM   1860 C CD  . PRO   C 1 56 ? 30.236  -31.955 27.883  1.00 33.28  ? 55  PRO   C CD  1 
ATOM   1861 N N   . LYS   C 1 57 ? 31.019  -31.481 24.376  1.00 36.72  ? 56  LYS   C N   1 
ATOM   1862 C CA  . LYS   C 1 57 ? 31.680  -31.599 23.085  1.00 38.71  ? 56  LYS   C CA  1 
ATOM   1863 C C   . LYS   C 1 57 ? 30.609  -31.629 21.994  1.00 38.26  ? 56  LYS   C C   1 
ATOM   1864 O O   . LYS   C 1 57 ? 30.893  -31.296 20.837  1.00 38.17  ? 56  LYS   C O   1 
ATOM   1865 C CB  . LYS   C 1 57 ? 32.549  -32.861 22.997  1.00 41.28  ? 56  LYS   C CB  1 
ATOM   1866 N N   . ASP   C 1 58 ? 29.377  -31.980 22.393  1.00 34.49  ? 57  ASP   C N   1 
ATOM   1867 C CA  . ASP   C 1 58 ? 28.307  -32.201 21.425  1.00 33.29  ? 57  ASP   C CA  1 
ATOM   1868 C C   . ASP   C 1 58 ? 27.415  -30.969 21.240  1.00 31.22  ? 57  ASP   C C   1 
ATOM   1869 O O   . ASP   C 1 58 ? 26.435  -31.039 20.510  1.00 29.15  ? 57  ASP   C O   1 
ATOM   1870 C CB  . ASP   C 1 58 ? 27.422  -33.361 21.847  1.00 32.80  ? 57  ASP   C CB  1 
ATOM   1871 C CG  . ASP   C 1 58 ? 28.105  -34.704 22.009  1.00 36.90  ? 57  ASP   C CG  1 
ATOM   1872 O OD1 . ASP   C 1 58 ? 29.135  -34.902 21.360  1.00 35.62  ? 57  ASP   C OD1 1 
ATOM   1873 O OD2 . ASP   C 1 58 ? 27.553  -35.553 22.746  1.00 40.94  ? 57  ASP   C OD2 1 
ATOM   1874 N N   . LEU   C 1 59 ? 27.709  -29.837 21.884  1.00 26.69  ? 58  LEU   C N   1 
ATOM   1875 C CA  . LEU   C 1 59 ? 26.781  -28.726 22.034  1.00 29.68  ? 58  LEU   C CA  1 
ATOM   1876 C C   . LEU   C 1 59 ? 27.405  -27.458 21.464  1.00 32.00  ? 58  LEU   C C   1 
ATOM   1877 O O   . LEU   C 1 59 ? 28.597  -27.242 21.678  1.00 36.45  ? 58  LEU   C O   1 
ATOM   1878 C CB  . LEU   C 1 59 ? 26.395  -28.536 23.510  1.00 27.86  ? 58  LEU   C CB  1 
ATOM   1879 C CG  . LEU   C 1 59 ? 25.874  -29.806 24.196  1.00 26.55  ? 58  LEU   C CG  1 
ATOM   1880 C CD1 . LEU   C 1 59 ? 25.634  -29.564 25.675  1.00 30.18  ? 58  LEU   C CD1 1 
ATOM   1881 C CD2 . LEU   C 1 59 ? 24.536  -30.218 23.527  1.00 23.69  ? 58  LEU   C CD2 1 
ATOM   1882 N N   . PHE   C 1 60 ? 26.598  -26.671 20.724  1.00 29.65  ? 59  PHE   C N   1 
ATOM   1883 C CA  . PHE   C 1 60 ? 27.065  -25.437 20.086  1.00 33.31  ? 59  PHE   C CA  1 
ATOM   1884 C C   . PHE   C 1 60 ? 26.090  -24.312 20.390  1.00 33.74  ? 59  PHE   C C   1 
ATOM   1885 O O   . PHE   C 1 60 ? 24.903  -24.441 20.156  1.00 32.36  ? 59  PHE   C O   1 
ATOM   1886 C CB  . PHE   C 1 60 ? 27.167  -25.669 18.575  1.00 29.19  ? 59  PHE   C CB  1 
ATOM   1887 C CG  . PHE   C 1 60 ? 28.121  -26.813 18.288  1.00 28.00  ? 59  PHE   C CG  1 
ATOM   1888 C CD1 . PHE   C 1 60 ? 27.680  -28.127 18.372  1.00 27.37  ? 59  PHE   C CD1 1 
ATOM   1889 C CD2 . PHE   C 1 60 ? 29.472  -26.591 18.013  1.00 35.63  ? 59  PHE   C CD2 1 
ATOM   1890 C CE1 . PHE   C 1 60 ? 28.537  -29.195 18.130  1.00 30.33  ? 59  PHE   C CE1 1 
ATOM   1891 C CE2 . PHE   C 1 60 ? 30.327  -27.655 17.761  1.00 33.04  ? 59  PHE   C CE2 1 
ATOM   1892 C CZ  . PHE   C 1 60 ? 29.863  -28.954 17.823  1.00 37.68  ? 59  PHE   C CZ  1 
ATOM   1893 N N   . PRO   C 1 61 ? 26.516  -23.161 20.967  1.00 34.86  ? 60  PRO   C N   1 
ATOM   1894 C CA  . PRO   C 1 61 ? 25.541  -22.113 21.290  1.00 34.27  ? 60  PRO   C CA  1 
ATOM   1895 C C   . PRO   C 1 61 ? 24.833  -21.600 20.045  1.00 30.52  ? 60  PRO   C C   1 
ATOM   1896 O O   . PRO   C 1 61 ? 25.465  -21.428 19.010  1.00 35.87  ? 60  PRO   C O   1 
ATOM   1897 C CB  . PRO   C 1 61 ? 26.328  -21.004 22.024  1.00 38.14  ? 60  PRO   C CB  1 
ATOM   1898 C CG  . PRO   C 1 61 ? 27.773  -21.392 21.825  1.00 37.36  ? 60  PRO   C CG  1 
ATOM   1899 C CD  . PRO   C 1 61 ? 27.892  -22.847 21.388  1.00 42.34  ? 60  PRO   C CD  1 
ATOM   1900 N N   . TYR   C 1 62 ? 23.510  -21.430 20.163  1.00 34.09  ? 61  TYR   C N   1 
ATOM   1901 C CA  . TYR   C 1 62 ? 22.613  -21.149 19.050  1.00 34.59  ? 61  TYR   C CA  1 
ATOM   1902 C C   . TYR   C 1 62 ? 23.055  -19.908 18.270  1.00 42.22  ? 61  TYR   C C   1 
ATOM   1903 O O   . TYR   C 1 62 ? 23.147  -19.951 17.044  1.00 42.33  ? 61  TYR   C O   1 
ATOM   1904 C CB  . TYR   C 1 62 ? 21.166  -21.044 19.532  1.00 37.82  ? 61  TYR   C CB  1 
ATOM   1905 C CG  . TYR   C 1 62 ? 20.216  -20.671 18.409  1.00 37.03  ? 61  TYR   C CG  1 
ATOM   1906 C CD1 . TYR   C 1 62 ? 20.034  -21.525 17.318  1.00 37.62  ? 61  TYR   C CD1 1 
ATOM   1907 C CD2 . TYR   C 1 62 ? 19.517  -19.469 18.442  1.00 39.82  ? 61  TYR   C CD2 1 
ATOM   1908 C CE1 . TYR   C 1 62 ? 19.172  -21.178 16.282  1.00 35.61  ? 61  TYR   C CE1 1 
ATOM   1909 C CE2 . TYR   C 1 62 ? 18.641  -19.122 17.422  1.00 37.71  ? 61  TYR   C CE2 1 
ATOM   1910 C CZ  . TYR   C 1 62 ? 18.482  -19.972 16.337  1.00 39.94  ? 61  TYR   C CZ  1 
ATOM   1911 O OH  . TYR   C 1 62 ? 17.632  -19.599 15.337  1.00 38.55  ? 61  TYR   C OH  1 
ATOM   1912 N N   . ASP   C 1 63 ? 23.374  -18.819 18.975  1.00 44.16  ? 62  ASP   C N   1 
ATOM   1913 C CA  . ASP   C 1 63 ? 23.595  -17.565 18.268  1.00 46.19  ? 62  ASP   C CA  1 
ATOM   1914 C C   . ASP   C 1 63 ? 24.932  -17.584 17.540  1.00 43.52  ? 62  ASP   C C   1 
ATOM   1915 O O   . ASP   C 1 63 ? 25.048  -17.038 16.439  1.00 50.21  ? 62  ASP   C O   1 
ATOM   1916 C CB  . ASP   C 1 63 ? 23.235  -16.360 19.123  1.00 52.67  ? 62  ASP   C CB  1 
ATOM   1917 C CG  . ASP   C 1 63 ? 21.737  -16.085 19.168  1.00 63.09  ? 62  ASP   C CG  1 
ATOM   1918 O OD1 . ASP   C 1 63 ? 21.174  -16.049 20.282  1.00 64.36  ? 62  ASP   C OD1 1 
ATOM   1919 O OD2 . ASP   C 1 63 ? 21.134  -15.935 18.078  1.00 65.08  ? 62  ASP   C OD2 1 
ATOM   1920 N N   . LYS   C 1 64 ? 25.920  -18.243 18.143  1.00 36.54  ? 63  LYS   C N   1 
ATOM   1921 C CA  . LYS   C 1 64 ? 27.246  -18.356 17.571  1.00 38.34  ? 63  LYS   C CA  1 
ATOM   1922 C C   . LYS   C 1 64 ? 27.231  -19.271 16.356  1.00 39.31  ? 63  LYS   C C   1 
ATOM   1923 O O   . LYS   C 1 64 ? 28.013  -19.054 15.445  1.00 37.10  ? 63  LYS   C O   1 
ATOM   1924 C CB  . LYS   C 1 64 ? 28.313  -18.838 18.568  1.00 43.71  ? 63  LYS   C CB  1 
ATOM   1925 N N   . SER   C 1 65 ? 26.336  -20.281 16.325  1.00 32.69  ? 64  SER   C N   1 
ATOM   1926 C CA  . SER   C 1 65 ? 26.545  -21.307 15.315  1.00 32.12  ? 64  SER   C CA  1 
ATOM   1927 C C   . SER   C 1 65 ? 25.396  -21.394 14.303  1.00 28.29  ? 64  SER   C C   1 
ATOM   1928 O O   . SER   C 1 65 ? 25.487  -22.225 13.396  1.00 29.56  ? 64  SER   C O   1 
ATOM   1929 C CB  . SER   C 1 65 ? 26.859  -22.673 15.927  1.00 35.45  ? 64  SER   C CB  1 
ATOM   1930 O OG  . SER   C 1 65 ? 25.710  -23.142 16.624  1.00 36.18  ? 64  SER   C OG  1 
ATOM   1931 N N   . LYS   C 1 66 ? 24.344  -20.578 14.471  1.00 29.23  ? 65  LYS   C N   1 
ATOM   1932 C CA  . LYS   C 1 66 ? 23.183  -20.727 13.596  1.00 30.73  ? 65  LYS   C CA  1 
ATOM   1933 C C   . LYS   C 1 66 ? 23.531  -20.486 12.119  1.00 31.84  ? 65  LYS   C C   1 
ATOM   1934 O O   . LYS   C 1 66 ? 22.925  -21.097 11.247  1.00 30.44  ? 65  LYS   C O   1 
ATOM   1935 C CB  . LYS   C 1 66 ? 21.945  -19.938 14.020  1.00 32.71  ? 65  LYS   C CB  1 
ATOM   1936 C CG  . LYS   C 1 66 ? 22.232  -18.446 14.134  1.00 30.19  ? 65  LYS   C CG  1 
ATOM   1937 C CD  . LYS   C 1 66 ? 21.020  -17.757 14.735  1.00 34.95  ? 65  LYS   C CD  1 
ATOM   1938 C CE  . LYS   C 1 66 ? 21.142  -16.284 14.652  1.00 39.14  ? 65  LYS   C CE  1 
ATOM   1939 N NZ  . LYS   C 1 66 ? 19.905  -15.809 15.260  1.00 41.30  ? 65  LYS   C NZ  1 
ATOM   1940 N N   . ASP   C 1 67 ? 24.494  -19.601 11.821  1.00 34.18  ? 66  ASP   C N   1 
ATOM   1941 C CA  . ASP   C 1 67 ? 24.859  -19.359 10.423  1.00 35.99  ? 66  ASP   C CA  1 
ATOM   1942 C C   . ASP   C 1 67 ? 25.318  -20.654 9.736   1.00 37.23  ? 66  ASP   C C   1 
ATOM   1943 O O   . ASP   C 1 67 ? 25.061  -20.871 8.556   1.00 35.58  ? 66  ASP   C O   1 
ATOM   1944 C CB  . ASP   C 1 67 ? 25.747  -18.117 10.286  1.00 37.54  ? 66  ASP   C CB  1 
ATOM   1945 C CG  . ASP   C 1 67 ? 27.175  -18.228 10.811  1.00 44.89  ? 66  ASP   C CG  1 
ATOM   1946 O OD1 . ASP   C 1 67 ? 27.534  -19.303 11.359  1.00 51.50  ? 66  ASP   C OD1 1 
ATOM   1947 O OD2 . ASP   C 1 67 ? 27.914  -17.214 10.721  1.00 46.29  ? 66  ASP   C OD2 1 
ATOM   1948 N N   . LYS   C 1 68 ? 25.925  -21.567 10.505  1.00 31.20  ? 67  LYS   C N   1 
ATOM   1949 C CA  . LYS   C 1 68 ? 26.449  -22.829 10.010  1.00 29.83  ? 67  LYS   C CA  1 
ATOM   1950 C C   . LYS   C 1 68 ? 25.405  -23.962 10.078  1.00 29.53  ? 67  LYS   C C   1 
ATOM   1951 O O   . LYS   C 1 68 ? 25.242  -24.742 9.129   1.00 32.20  ? 67  LYS   C O   1 
ATOM   1952 C CB  . LYS   C 1 68 ? 27.724  -23.136 10.801  1.00 36.07  ? 67  LYS   C CB  1 
ATOM   1953 C CG  . LYS   C 1 68 ? 28.427  -24.380 10.354  1.00 38.80  ? 67  LYS   C CG  1 
ATOM   1954 C CD  . LYS   C 1 68 ? 29.749  -24.565 11.109  1.00 42.95  ? 67  LYS   C CD  1 
ATOM   1955 C CE  . LYS   C 1 68 ? 30.428  -25.892 10.904  1.00 53.98  ? 67  LYS   C CE  1 
ATOM   1956 N NZ  . LYS   C 1 68 ? 30.589  -26.273 9.495   1.00 62.27  ? 67  LYS   C NZ  1 
ATOM   1957 N N   . TYR   C 1 69 ? 24.682  -24.058 11.204  1.00 28.77  ? 68  TYR   C N   1 
ATOM   1958 C CA  . TYR   C 1 69 ? 23.832  -25.233 11.362  1.00 24.08  ? 68  TYR   C CA  1 
ATOM   1959 C C   . TYR   C 1 69 ? 22.347  -24.902 11.215  1.00 25.54  ? 68  TYR   C C   1 
ATOM   1960 O O   . TYR   C 1 69 ? 21.552  -25.812 11.062  1.00 24.89  ? 68  TYR   C O   1 
ATOM   1961 C CB  . TYR   C 1 69 ? 23.954  -25.904 12.736  1.00 25.79  ? 68  TYR   C CB  1 
ATOM   1962 C CG  . TYR   C 1 69 ? 25.388  -26.331 13.033  1.00 24.78  ? 68  TYR   C CG  1 
ATOM   1963 C CD1 . TYR   C 1 69 ? 26.111  -27.091 12.121  1.00 25.17  ? 68  TYR   C CD1 1 
ATOM   1964 C CD2 . TYR   C 1 69 ? 26.011  -25.873 14.189  1.00 27.86  ? 68  TYR   C CD2 1 
ATOM   1965 C CE1 . TYR   C 1 69 ? 27.408  -27.509 12.404  1.00 27.89  ? 68  TYR   C CE1 1 
ATOM   1966 C CE2 . TYR   C 1 69 ? 27.296  -26.306 14.487  1.00 26.55  ? 68  TYR   C CE2 1 
ATOM   1967 C CZ  . TYR   C 1 69 ? 27.994  -27.088 13.583  1.00 28.36  ? 68  TYR   C CZ  1 
ATOM   1968 O OH  . TYR   C 1 69 ? 29.291  -27.434 13.904  1.00 35.35  ? 68  TYR   C OH  1 
ATOM   1969 N N   . GLY   C 1 70 ? 21.978  -23.622 11.228  1.00 24.90  ? 69  GLY   C N   1 
ATOM   1970 C CA  . GLY   C 1 70 ? 20.560  -23.268 11.168  1.00 26.81  ? 69  GLY   C CA  1 
ATOM   1971 C C   . GLY   C 1 70 ? 20.122  -23.139 9.710   1.00 26.34  ? 69  GLY   C C   1 
ATOM   1972 O O   . GLY   C 1 70 ? 20.045  -22.052 9.153   1.00 27.85  ? 69  GLY   C O   1 
ATOM   1973 N N   . LYS   C 1 71 ? 20.001  -24.276 9.051   1.00 24.92  ? 70  LYS   C N   1 
ATOM   1974 C CA  . LYS   C 1 71 ? 19.615  -24.328 7.645   1.00 28.08  ? 70  LYS   C CA  1 
ATOM   1975 C C   . LYS   C 1 71 ? 18.738  -25.562 7.534   1.00 27.02  ? 70  LYS   C C   1 
ATOM   1976 O O   . LYS   C 1 71 ? 18.877  -26.512 8.300   1.00 27.05  ? 70  LYS   C O   1 
ATOM   1977 C CB  . LYS   C 1 71 ? 20.783  -24.516 6.672   1.00 30.28  ? 70  LYS   C CB  1 
ATOM   1978 C CG  . LYS   C 1 71 ? 21.792  -25.553 7.123   1.00 35.96  ? 70  LYS   C CG  1 
ATOM   1979 C CD  . LYS   C 1 71 ? 23.038  -25.833 6.294   1.00 38.55  ? 70  LYS   C CD  1 
ATOM   1980 C CE  . LYS   C 1 71 ? 23.567  -27.125 6.814   1.00 41.92  ? 70  LYS   C CE  1 
ATOM   1981 N N   . PRO   C 1 72 ? 17.762  -25.598 6.611   1.00 22.41  ? 71  PRO   C N   1 
ATOM   1982 C CA  . PRO   C 1 72 ? 16.834  -26.726 6.567   1.00 21.55  ? 71  PRO   C CA  1 
ATOM   1983 C C   . PRO   C 1 72 ? 17.499  -28.056 6.263   1.00 24.95  ? 71  PRO   C C   1 
ATOM   1984 O O   . PRO   C 1 72 ? 18.516  -28.122 5.575   1.00 27.91  ? 71  PRO   C O   1 
ATOM   1985 C CB  . PRO   C 1 72 ? 15.958  -26.296 5.406   1.00 24.13  ? 71  PRO   C CB  1 
ATOM   1986 C CG  . PRO   C 1 72 ? 15.906  -24.800 5.595   1.00 23.59  ? 71  PRO   C CG  1 
ATOM   1987 C CD  . PRO   C 1 72 ? 17.383  -24.468 5.740   1.00 22.44  ? 71  PRO   C CD  1 
ATOM   1988 N N   . ASN   C 1 73 ? 16.798  -29.085 6.692   1.00 27.81  ? 72  ASN   C N   1 
ATOM   1989 C CA  . ASN   C 1 73 ? 17.122  -30.389 6.145   1.00 32.20  ? 72  ASN   C CA  1 
ATOM   1990 C C   . ASN   C 1 73 ? 15.880  -31.247 6.244   1.00 25.75  ? 72  ASN   C C   1 
ATOM   1991 O O   . ASN   C 1 73 ? 14.924  -30.924 6.941   1.00 27.58  ? 72  ASN   C O   1 
ATOM   1992 C CB  . ASN   C 1 73 ? 18.482  -30.935 6.567   1.00 43.00  ? 72  ASN   C CB  1 
ATOM   1993 C CG  . ASN   C 1 73 ? 18.374  -31.720 7.843   1.00 41.72  ? 72  ASN   C CG  1 
ATOM   1994 O OD1 . ASN   C 1 73 ? 18.028  -32.913 7.826   1.00 38.58  ? 72  ASN   C OD1 1 
ATOM   1995 N ND2 . ASN   C 1 73 ? 18.677  -31.058 8.939   1.00 49.69  ? 72  ASN   C ND2 1 
ATOM   1996 N N   . LYS   C 1 74 ? 15.959  -32.409 5.594   1.00 26.69  ? 73  LYS   C N   1 
ATOM   1997 C CA  . LYS   C 1 74 ? 14.759  -33.191 5.350   1.00 25.66  ? 73  LYS   C CA  1 
ATOM   1998 C C   . LYS   C 1 74 ? 14.468  -34.154 6.494   1.00 27.79  ? 73  LYS   C C   1 
ATOM   1999 O O   . LYS   C 1 74 ? 13.410  -34.779 6.508   1.00 30.48  ? 73  LYS   C O   1 
ATOM   2000 C CB  . LYS   C 1 74 ? 14.930  -33.942 4.017   1.00 30.10  ? 73  LYS   C CB  1 
ATOM   2001 N N   . ARG   C 1 75 ? 15.362  -34.243 7.503   1.00 23.33  ? 74  ARG   C N   1 
ATOM   2002 C CA  . ARG   C 1 75 ? 15.104  -35.196 8.581   1.00 22.93  ? 74  ARG   C CA  1 
ATOM   2003 C C   . ARG   C 1 75 ? 13.809  -34.847 9.326   1.00 25.72  ? 74  ARG   C C   1 
ATOM   2004 O O   . ARG   C 1 75 ? 13.482  -33.666 9.570   1.00 25.65  ? 74  ARG   C O   1 
ATOM   2005 C CB  . ARG   C 1 75 ? 16.303  -35.294 9.548   1.00 25.03  ? 74  ARG   C CB  1 
ATOM   2006 C CG  . ARG   C 1 75 ? 17.679  -35.452 8.900   1.00 32.56  ? 74  ARG   C CG  1 
ATOM   2007 C CD  . ARG   C 1 75 ? 17.994  -36.776 8.151   1.00 36.62  ? 74  ARG   C CD  1 
ATOM   2008 N NE  . ARG   C 1 75 ? 18.115  -37.794 9.187   1.00 31.69  ? 74  ARG   C NE  1 
ATOM   2009 C CZ  . ARG   C 1 75 ? 19.242  -38.239 9.789   1.00 27.71  ? 74  ARG   C CZ  1 
ATOM   2010 N NH1 . ARG   C 1 75 ? 19.053  -38.811 10.942  1.00 32.48  ? 74  ARG   C NH1 1 
ATOM   2011 N NH2 . ARG   C 1 75 ? 20.463  -38.006 9.291   1.00 27.97  ? 74  ARG   C NH2 1 
ATOM   2012 N N   . LYS   C 1 76 ? 13.055  -35.895 9.700   1.00 29.96  ? 75  LYS   C N   1 
ATOM   2013 C CA  . LYS   C 1 76 ? 11.766  -35.753 10.369  1.00 32.76  ? 75  LYS   C CA  1 
ATOM   2014 C C   . LYS   C 1 76 ? 11.872  -34.823 11.573  1.00 29.10  ? 75  LYS   C C   1 
ATOM   2015 O O   . LYS   C 1 76 ? 12.695  -35.016 12.476  1.00 29.05  ? 75  LYS   C O   1 
ATOM   2016 C CB  . LYS   C 1 76 ? 11.148  -37.095 10.789  1.00 33.99  ? 75  LYS   C CB  1 
ATOM   2017 C CG  . LYS   C 1 76 ? 9.667   -36.961 11.179  1.00 39.32  ? 75  LYS   C CG  1 
ATOM   2018 C CD  . LYS   C 1 76 ? 8.991   -38.173 11.829  1.00 42.10  ? 75  LYS   C CD  1 
ATOM   2019 N N   . GLY   C 1 77 ? 11.036  -33.775 11.562  1.00 30.04  ? 76  GLY   C N   1 
ATOM   2020 C CA  . GLY   C 1 77 ? 10.915  -32.888 12.699  1.00 26.07  ? 76  GLY   C CA  1 
ATOM   2021 C C   . GLY   C 1 77 ? 11.897  -31.708 12.655  1.00 24.10  ? 76  GLY   C C   1 
ATOM   2022 O O   . GLY   C 1 77 ? 11.764  -30.782 13.453  1.00 26.46  ? 76  GLY   C O   1 
ATOM   2023 N N   . PHE   C 1 78 ? 12.874  -31.727 11.743  1.00 23.28  ? 77  PHE   C N   1 
ATOM   2024 C CA  . PHE   C 1 78 ? 13.974  -30.773 11.850  1.00 22.21  ? 77  PHE   C CA  1 
ATOM   2025 C C   . PHE   C 1 78 ? 13.483  -29.340 11.608  1.00 22.59  ? 77  PHE   C C   1 
ATOM   2026 O O   . PHE   C 1 78 ? 13.869  -28.394 12.302  1.00 22.86  ? 77  PHE   C O   1 
ATOM   2027 C CB  . PHE   C 1 78 ? 15.072  -31.166 10.864  1.00 25.06  ? 77  PHE   C CB  1 
ATOM   2028 C CG  . PHE   C 1 78 ? 16.373  -30.411 11.084  1.00 21.50  ? 77  PHE   C CG  1 
ATOM   2029 C CD1 . PHE   C 1 78 ? 16.552  -29.130 10.565  1.00 21.44  ? 77  PHE   C CD1 1 
ATOM   2030 C CD2 . PHE   C 1 78 ? 17.392  -30.956 11.856  1.00 22.06  ? 77  PHE   C CD2 1 
ATOM   2031 C CE1 . PHE   C 1 78 ? 17.740  -28.438 10.793  1.00 21.59  ? 77  PHE   C CE1 1 
ATOM   2032 C CE2 . PHE   C 1 78 ? 18.563  -30.247 12.077  1.00 21.28  ? 77  PHE   C CE2 1 
ATOM   2033 C CZ  . PHE   C 1 78 ? 18.737  -28.998 11.549  1.00 20.97  ? 77  PHE   C CZ  1 
ATOM   2034 N N   . ASN   C 1 79 ? 12.717  -29.176 10.516  1.00 23.85  ? 78  ASN   C N   1 
ATOM   2035 C CA  . ASN   C 1 79 ? 12.377  -27.814 10.120  1.00 24.91  ? 78  ASN   C CA  1 
ATOM   2036 C C   . ASN   C 1 79 ? 11.375  -27.197 11.079  1.00 25.02  ? 78  ASN   C C   1 
ATOM   2037 O O   . ASN   C 1 79 ? 11.420  -26.000 11.378  1.00 24.38  ? 78  ASN   C O   1 
ATOM   2038 C CB  . ASN   C 1 79 ? 11.907  -27.809 8.675   1.00 23.97  ? 78  ASN   C CB  1 
ATOM   2039 C CG  . ASN   C 1 79 ? 13.013  -28.218 7.734   1.00 23.21  ? 78  ASN   C CG  1 
ATOM   2040 O OD1 . ASN   C 1 79 ? 14.199  -27.917 7.958   1.00 24.22  ? 78  ASN   C OD1 1 
ATOM   2041 N ND2 . ASN   C 1 79 ? 12.643  -28.765 6.588   1.00 23.23  ? 78  ASN   C ND2 1 
ATOM   2042 N N   . GLU   C 1 80 ? 10.510  -28.027 11.633  1.00 25.56  ? 79  GLU   C N   1 
ATOM   2043 C CA  . GLU   C 1 80 ? 9.669   -27.514 12.700  1.00 25.67  ? 79  GLU   C CA  1 
ATOM   2044 C C   . GLU   C 1 80 ? 10.525  -27.075 13.881  1.00 28.12  ? 79  GLU   C C   1 
ATOM   2045 O O   . GLU   C 1 80 ? 10.242  -26.073 14.534  1.00 27.27  ? 79  GLU   C O   1 
ATOM   2046 C CB  . GLU   C 1 80 ? 8.678   -28.585 13.131  1.00 33.19  ? 79  GLU   C CB  1 
ATOM   2047 C CG  . GLU   C 1 80 ? 7.757   -28.092 14.237  1.00 33.48  ? 79  GLU   C CG  1 
ATOM   2048 C CD  . GLU   C 1 80 ? 6.525   -28.948 14.355  1.00 44.10  ? 79  GLU   C CD  1 
ATOM   2049 O OE1 . GLU   C 1 80 ? 6.507   -30.083 13.817  1.00 46.81  ? 79  GLU   C OE1 1 
ATOM   2050 O OE2 . GLU   C 1 80 ? 5.572   -28.441 14.966  1.00 43.80  ? 79  GLU   C OE2 1 
ATOM   2051 N N   . GLY   C 1 81 ? 11.597  -27.870 14.158  1.00 25.01  ? 80  GLY   C N   1 
ATOM   2052 C CA  . GLY   C 1 81 ? 12.524  -27.510 15.217  1.00 23.46  ? 80  GLY   C CA  1 
ATOM   2053 C C   . GLY   C 1 81 ? 13.165  -26.148 14.985  1.00 23.72  ? 80  GLY   C C   1 
ATOM   2054 O O   . GLY   C 1 81 ? 13.338  -25.395 15.938  1.00 25.78  ? 80  GLY   C O   1 
ATOM   2055 N N   . LEU   C 1 82 ? 13.596  -25.873 13.731  1.00 25.50  ? 81  LEU   C N   1 
ATOM   2056 C CA  . LEU   C 1 82 ? 14.179  -24.584 13.385  1.00 23.99  ? 81  LEU   C CA  1 
ATOM   2057 C C   . LEU   C 1 82 ? 13.140  -23.487 13.630  1.00 22.43  ? 81  LEU   C C   1 
ATOM   2058 O O   . LEU   C 1 82 ? 13.532  -22.412 14.086  1.00 25.37  ? 81  LEU   C O   1 
ATOM   2059 C CB  . LEU   C 1 82 ? 14.668  -24.571 11.933  1.00 23.55  ? 81  LEU   C CB  1 
ATOM   2060 C CG  . LEU   C 1 82 ? 15.900  -25.395 11.545  1.00 25.13  ? 81  LEU   C CG  1 
ATOM   2061 C CD1 . LEU   C 1 82 ? 16.212  -25.281 10.039  1.00 24.68  ? 81  LEU   C CD1 1 
ATOM   2062 C CD2 . LEU   C 1 82 ? 17.119  -24.963 12.307  1.00 24.61  ? 81  LEU   C CD2 1 
ATOM   2063 N N   . TRP   C 1 83 ? 11.863  -23.774 13.332  1.00 24.00  ? 82  TRP   C N   1 
ATOM   2064 C CA  . TRP   C 1 83 ? 10.845  -22.748 13.587  1.00 28.55  ? 82  TRP   C CA  1 
ATOM   2065 C C   . TRP   C 1 83 ? 10.765  -22.460 15.096  1.00 31.84  ? 82  TRP   C C   1 
ATOM   2066 O O   . TRP   C 1 83 ? 10.808  -21.298 15.531  1.00 30.46  ? 82  TRP   C O   1 
ATOM   2067 C CB  . TRP   C 1 83 ? 9.484   -23.106 12.974  1.00 25.32  ? 82  TRP   C CB  1 
ATOM   2068 C CG  . TRP   C 1 83 ? 8.531   -21.952 13.122  1.00 31.82  ? 82  TRP   C CG  1 
ATOM   2069 C CD1 . TRP   C 1 83 ? 8.379   -20.905 12.259  1.00 31.96  ? 82  TRP   C CD1 1 
ATOM   2070 C CD2 . TRP   C 1 83 ? 7.643   -21.700 14.234  1.00 35.84  ? 82  TRP   C CD2 1 
ATOM   2071 N NE1 . TRP   C 1 83 ? 7.443   -20.033 12.740  1.00 30.65  ? 82  TRP   C NE1 1 
ATOM   2072 C CE2 . TRP   C 1 83 ? 6.975   -20.484 13.948  1.00 34.35  ? 82  TRP   C CE2 1 
ATOM   2073 C CE3 . TRP   C 1 83 ? 7.350   -22.387 15.422  1.00 35.72  ? 82  TRP   C CE3 1 
ATOM   2074 C CZ2 . TRP   C 1 83 ? 6.038   -19.946 14.823  1.00 39.87  ? 82  TRP   C CZ2 1 
ATOM   2075 C CZ3 . TRP   C 1 83 ? 6.429   -21.846 16.298  1.00 41.27  ? 82  TRP   C CZ3 1 
ATOM   2076 C CH2 . TRP   C 1 83 ? 5.794   -20.638 15.998  1.00 36.11  ? 82  TRP   C CH2 1 
ATOM   2077 N N   . GLU   C 1 84 ? 10.816  -23.539 15.899  1.00 27.36  ? 83  GLU   C N   1 
ATOM   2078 C CA  . GLU   C 1 84 ? 10.661  -23.383 17.348  1.00 29.15  ? 83  GLU   C CA  1 
ATOM   2079 C C   . GLU   C 1 84 ? 11.813  -22.621 17.996  1.00 30.62  ? 83  GLU   C C   1 
ATOM   2080 O O   . GLU   C 1 84 ? 11.590  -21.731 18.842  1.00 30.39  ? 83  GLU   C O   1 
ATOM   2081 C CB  . GLU   C 1 84 ? 10.508  -24.749 18.014  1.00 26.55  ? 83  GLU   C CB  1 
ATOM   2082 C CG  . GLU   C 1 84 ? 9.163   -25.394 17.712  1.00 31.58  ? 83  GLU   C CG  1 
ATOM   2083 C CD  . GLU   C 1 84 ? 9.075   -26.818 18.192  1.00 33.06  ? 83  GLU   C CD  1 
ATOM   2084 O OE1 . GLU   C 1 84 ? 10.082  -27.273 18.775  1.00 28.87  ? 83  GLU   C OE1 1 
ATOM   2085 O OE2 . GLU   C 1 84 ? 8.047   -27.470 17.942  1.00 33.09  ? 83  GLU   C OE2 1 
ATOM   2086 N N   . ILE   C 1 85 ? 13.055  -22.917 17.583  1.00 26.73  ? 84  ILE   C N   1 
ATOM   2087 C CA  . ILE   C 1 85 ? 14.232  -22.298 18.187  1.00 27.78  ? 84  ILE   C CA  1 
ATOM   2088 C C   . ILE   C 1 85 ? 14.311  -20.779 17.936  1.00 28.58  ? 84  ILE   C C   1 
ATOM   2089 O O   . ILE   C 1 85 ? 14.790  -20.031 18.784  1.00 29.82  ? 84  ILE   C O   1 
ATOM   2090 C CB  . ILE   C 1 85 ? 15.542  -23.033 17.843  1.00 28.46  ? 84  ILE   C CB  1 
ATOM   2091 C CG1 . ILE   C 1 85 ? 16.638  -22.665 18.855  1.00 27.49  ? 84  ILE   C CG1 1 
ATOM   2092 C CG2 . ILE   C 1 85 ? 16.003  -22.803 16.389  1.00 26.57  ? 84  ILE   C CG2 1 
ATOM   2093 C CD1 . ILE   C 1 85 ? 17.795  -23.653 18.952  1.00 26.62  ? 84  ILE   C CD1 1 
ATOM   2094 N N   . GLN   C 1 86 ? 13.847  -20.346 16.757  1.00 28.80  ? 85  GLN   C N   1 
ATOM   2095 C CA  . GLN   C 1 86 ? 13.901  -18.941 16.399  1.00 29.87  ? 85  GLN   C CA  1 
ATOM   2096 C C   . GLN   C 1 86 ? 12.675  -18.188 16.910  1.00 32.02  ? 85  GLN   C C   1 
ATOM   2097 O O   . GLN   C 1 86 ? 12.782  -17.009 17.258  1.00 35.31  ? 85  GLN   C O   1 
ATOM   2098 C CB  . GLN   C 1 86 ? 14.038  -18.886 14.872  1.00 29.65  ? 85  GLN   C CB  1 
ATOM   2099 C CG  . GLN   C 1 86 ? 14.116  -17.458 14.337  1.00 32.47  ? 85  GLN   C CG  1 
ATOM   2100 C CD  . GLN   C 1 86 ? 14.457  -17.418 12.862  1.00 31.83  ? 85  GLN   C CD  1 
ATOM   2101 O OE1 . GLN   C 1 86 ? 14.308  -18.406 12.121  1.00 30.41  ? 85  GLN   C OE1 1 
ATOM   2102 N NE2 . GLN   C 1 86 ? 14.950  -16.269 12.423  1.00 34.98  ? 85  GLN   C NE2 1 
ATOM   2103 N N   . ASN   C 1 87 ? 11.535  -18.853 16.975  1.00 28.03  ? 86  ASN   C N   1 
ATOM   2104 C CA  . ASN   C 1 87 ? 10.259  -18.158 17.151  1.00 36.28  ? 86  ASN   C CA  1 
ATOM   2105 C C   . ASN   C 1 87 ? 9.583   -18.485 18.486  1.00 39.70  ? 86  ASN   C C   1 
ATOM   2106 O O   . ASN   C 1 87 ? 8.621   -17.805 18.842  1.00 39.91  ? 86  ASN   C O   1 
ATOM   2107 C CB  . ASN   C 1 87 ? 9.283   -18.399 16.001  1.00 34.71  ? 86  ASN   C CB  1 
ATOM   2108 C CG  . ASN   C 1 87 ? 9.821   -17.827 14.711  1.00 35.30  ? 86  ASN   C CG  1 
ATOM   2109 O OD1 . ASN   C 1 87 ? 9.787   -16.607 14.534  1.00 36.74  ? 86  ASN   C OD1 1 
ATOM   2110 N ND2 . ASN   C 1 87 ? 10.367  -18.654 13.829  1.00 30.81  ? 86  ASN   C ND2 1 
ATOM   2111 N N   . ASN   C 1 88 ? 10.030  -19.528 19.211  1.00 34.27  ? 87  ASN   C N   1 
ATOM   2112 C CA  . ASN   C 1 88 ? 9.296   -19.912 20.420  1.00 36.68  ? 87  ASN   C CA  1 
ATOM   2113 C C   . ASN   C 1 88 ? 10.187  -20.775 21.312  1.00 33.80  ? 87  ASN   C C   1 
ATOM   2114 O O   . ASN   C 1 88 ? 9.789   -21.892 21.663  1.00 38.79  ? 87  ASN   C O   1 
ATOM   2115 C CB  . ASN   C 1 88 ? 7.997   -20.649 20.109  1.00 42.91  ? 87  ASN   C CB  1 
ATOM   2116 C CG  . ASN   C 1 88 ? 7.007   -20.599 21.254  1.00 52.64  ? 87  ASN   C CG  1 
ATOM   2117 O OD1 . ASN   C 1 88 ? 7.220   -19.857 22.221  1.00 58.30  ? 87  ASN   C OD1 1 
ATOM   2118 N ND2 . ASN   C 1 88 ? 5.913   -21.345 21.157  1.00 47.52  ? 87  ASN   C ND2 1 
ATOM   2119 N N   . PRO   C 1 89 ? 11.423  -20.336 21.632  1.00 34.47  ? 88  PRO   C N   1 
ATOM   2120 C CA  . PRO   C 1 89 ? 12.424  -21.248 22.181  1.00 32.36  ? 88  PRO   C CA  1 
ATOM   2121 C C   . PRO   C 1 89 ? 12.115  -21.748 23.589  1.00 39.37  ? 88  PRO   C C   1 
ATOM   2122 O O   . PRO   C 1 89 ? 12.754  -22.701 24.051  1.00 37.11  ? 88  PRO   C O   1 
ATOM   2123 C CB  . PRO   C 1 89 ? 13.734  -20.466 22.105  1.00 34.85  ? 88  PRO   C CB  1 
ATOM   2124 C CG  . PRO   C 1 89 ? 13.277  -19.003 22.188  1.00 39.06  ? 88  PRO   C CG  1 
ATOM   2125 C CD  . PRO   C 1 89 ? 11.935  -18.971 21.471  1.00 38.82  ? 88  PRO   C CD  1 
ATOM   2126 N N   . HIS   C 1 90 ? 11.136  -21.109 24.254  1.00 43.27  ? 89  HIS   C N   1 
ATOM   2127 C CA  . HIS   C 1 90 ? 10.875  -21.426 25.655  1.00 45.44  ? 89  HIS   C CA  1 
ATOM   2128 C C   . HIS   C 1 90 ? 9.435   -21.853 25.931  1.00 46.56  ? 89  HIS   C C   1 
ATOM   2129 O O   . HIS   C 1 90 ? 9.067   -21.987 27.090  1.00 57.59  ? 89  HIS   C O   1 
ATOM   2130 C CB  . HIS   C 1 90 ? 11.319  -20.293 26.572  1.00 38.77  ? 89  HIS   C CB  1 
ATOM   2131 C CG  . HIS   C 1 90 ? 12.703  -19.796 26.322  1.00 38.80  ? 89  HIS   C CG  1 
ATOM   2132 N ND1 . HIS   C 1 90 ? 13.839  -20.541 26.582  1.00 42.05  ? 89  HIS   C ND1 1 
ATOM   2133 C CD2 . HIS   C 1 90 ? 13.121  -18.630 25.842  1.00 38.31  ? 89  HIS   C CD2 1 
ATOM   2134 C CE1 . HIS   C 1 90 ? 14.918  -19.815 26.290  1.00 36.91  ? 89  HIS   C CE1 1 
ATOM   2135 N NE2 . HIS   C 1 90 ? 14.492  -18.642 25.828  1.00 35.86  ? 89  HIS   C NE2 1 
ATOM   2136 N N   . ALA   C 1 91 ? 8.627   -22.100 24.894  1.00 49.82  ? 90  ALA   C N   1 
ATOM   2137 C CA  . ALA   C 1 91 ? 7.344   -22.759 25.090  1.00 54.75  ? 90  ALA   C CA  1 
ATOM   2138 C C   . ALA   C 1 91 ? 7.575   -24.080 25.825  1.00 68.02  ? 90  ALA   C C   1 
ATOM   2139 O O   . ALA   C 1 91 ? 8.724   -24.457 26.063  1.00 65.63  ? 90  ALA   C O   1 
ATOM   2140 C CB  . ALA   C 1 91 ? 6.619   -22.949 23.771  1.00 58.87  ? 90  ALA   C CB  1 
ATOM   2141 N N   . SER   C 1 92 ? 6.484   -24.775 26.183  1.00 71.31  ? 91  SER   C N   1 
ATOM   2142 C CA  . SER   C 1 92 ? 6.567   -25.890 27.119  1.00 73.54  ? 91  SER   C CA  1 
ATOM   2143 C C   . SER   C 1 92 ? 6.545   -27.252 26.416  1.00 75.09  ? 91  SER   C C   1 
ATOM   2144 O O   . SER   C 1 92 ? 7.019   -28.245 26.970  1.00 82.26  ? 91  SER   C O   1 
ATOM   2145 C CB  . SER   C 1 92 ? 5.520   -25.773 28.208  1.00 75.32  ? 91  SER   C CB  1 
ATOM   2146 O OG  . SER   C 1 92 ? 4.247   -25.441 27.670  1.00 82.06  ? 91  SER   C OG  1 
ATOM   2147 N N   . TYR   C 1 93 ? 5.983   -27.296 25.202  1.00 69.83  ? 92  TYR   C N   1 
ATOM   2148 C CA  . TYR   C 1 93 ? 5.943   -28.498 24.380  1.00 73.98  ? 92  TYR   C CA  1 
ATOM   2149 C C   . TYR   C 1 93 ? 5.597   -29.719 25.244  1.00 75.03  ? 92  TYR   C C   1 
ATOM   2150 O O   . TYR   C 1 93 ? 5.876   -30.847 24.774  1.00 81.01  ? 92  TYR   C O   1 
ATOM   2151 C CB  . TYR   C 1 93 ? 7.255   -28.640 23.594  1.00 68.06  ? 92  TYR   C CB  1 
ATOM   2152 C CG  . TYR   C 1 93 ? 7.618   -27.389 22.804  1.00 60.45  ? 92  TYR   C CG  1 
ATOM   2153 C CD1 . TYR   C 1 93 ? 6.980   -27.097 21.601  1.00 56.26  ? 92  TYR   C CD1 1 
ATOM   2154 C CD2 . TYR   C 1 93 ? 8.573   -26.490 23.274  1.00 54.58  ? 92  TYR   C CD2 1 
ATOM   2155 C CE1 . TYR   C 1 93 ? 7.280   -25.949 20.887  1.00 59.42  ? 92  TYR   C CE1 1 
ATOM   2156 C CE2 . TYR   C 1 93 ? 8.887   -25.344 22.560  1.00 61.32  ? 92  TYR   C CE2 1 
ATOM   2157 C CZ  . TYR   C 1 93 ? 8.244   -25.077 21.363  1.00 61.61  ? 92  TYR   C CZ  1 
ATOM   2158 O OH  . TYR   C 1 93 ? 8.534   -23.940 20.658  1.00 63.32  ? 92  TYR   C OH  1 
HETATM 2159 S S   . SO4   D 2 .  ? 1.119   -33.863 2.012   1.00 85.67  ? 101 SO4   A S   1 
HETATM 2160 O O1  . SO4   D 2 .  ? 1.384   -34.493 0.740   1.00 71.52  ? 101 SO4   A O1  1 
HETATM 2161 O O2  . SO4   D 2 .  ? 1.263   -32.434 1.892   1.00 75.96  ? 101 SO4   A O2  1 
HETATM 2162 O O3  . SO4   D 2 .  ? -0.225  -34.177 2.435   1.00 89.02  ? 101 SO4   A O3  1 
HETATM 2163 O O4  . SO4   D 2 .  ? 2.050   -34.348 2.993   1.00 79.93  ? 101 SO4   A O4  1 
HETATM 2164 S S   . SO4   E 2 .  ? -9.655  -24.787 0.974   1.00 82.48  ? 102 SO4   A S   1 
HETATM 2165 O O1  . SO4   E 2 .  ? -9.236  -24.852 -0.397  1.00 77.62  ? 102 SO4   A O1  1 
HETATM 2166 O O2  . SO4   E 2 .  ? -10.594 -23.704 1.127   1.00 91.54  ? 102 SO4   A O2  1 
HETATM 2167 O O3  . SO4   E 2 .  ? -10.289 -26.031 1.336   1.00 88.88  ? 102 SO4   A O3  1 
HETATM 2168 O O4  . SO4   E 2 .  ? -8.514  -24.558 1.827   1.00 73.94  ? 102 SO4   A O4  1 
HETATM 2169 C C1  . EDO   F 3 .  ? 13.791  -19.542 -7.321  1.00 32.35  ? 103 EDO   A C1  1 
HETATM 2170 O O1  . EDO   F 3 .  ? 15.074  -18.881 -7.198  1.00 28.54  ? 103 EDO   A O1  1 
HETATM 2171 C C2  . EDO   F 3 .  ? 12.931  -19.028 -8.441  1.00 29.97  ? 103 EDO   A C2  1 
HETATM 2172 O O2  . EDO   F 3 .  ? 12.492  -17.714 -8.202  1.00 28.24  ? 103 EDO   A O2  1 
HETATM 2173 S S   . SO4   G 2 .  ? 8.981   -29.370 5.924   1.00 49.33  ? 104 SO4   A S   1 
HETATM 2174 O O1  . SO4   G 2 .  ? 9.589   -28.387 5.104   1.00 51.12  ? 104 SO4   A O1  1 
HETATM 2175 O O2  . SO4   G 2 .  ? 8.580   -30.497 5.098   1.00 55.69  ? 104 SO4   A O2  1 
HETATM 2176 O O3  . SO4   G 2 .  ? 9.925   -29.819 6.928   1.00 55.01  ? 104 SO4   A O3  1 
HETATM 2177 O O4  . SO4   G 2 .  ? 7.797   -28.830 6.546   1.00 55.51  ? 104 SO4   A O4  1 
HETATM 2178 S S   . SO4   H 2 .  ? 7.545   -8.470  -24.707 1.00 68.24  ? 101 SO4   B S   1 
HETATM 2179 O O1  . SO4   H 2 .  ? 8.616   -8.545  -25.672 1.00 35.18  ? 101 SO4   B O1  1 
HETATM 2180 O O2  . SO4   H 2 .  ? 6.312   -8.892  -25.331 1.00 55.74  ? 101 SO4   B O2  1 
HETATM 2181 O O3  . SO4   H 2 .  ? 7.782   -9.337  -23.532 1.00 43.62  ? 101 SO4   B O3  1 
HETATM 2182 O O4  . SO4   H 2 .  ? 7.475   -7.071  -24.322 1.00 53.84  ? 101 SO4   B O4  1 
HETATM 2183 S S   . SO4   I 2 .  ? 14.311  -27.073 -26.554 1.00 42.84  ? 102 SO4   B S   1 
HETATM 2184 O O1  . SO4   I 2 .  ? 15.721  -26.969 -26.327 1.00 41.49  ? 102 SO4   B O1  1 
HETATM 2185 O O2  . SO4   I 2 .  ? 14.013  -28.405 -27.035 1.00 56.72  ? 102 SO4   B O2  1 
HETATM 2186 O O3  . SO4   I 2 .  ? 13.601  -26.854 -25.318 1.00 54.99  ? 102 SO4   B O3  1 
HETATM 2187 O O4  . SO4   I 2 .  ? 13.849  -26.117 -27.533 1.00 44.87  ? 102 SO4   B O4  1 
HETATM 2188 N N1  . A1AM6 J 4 .  ? 21.081  -16.724 -23.232 0.94 25.87  ? 103 A1AM6 B N1  1 
HETATM 2189 N N3  . A1AM6 J 4 .  ? 22.295  -18.229 -21.943 0.94 34.77  ? 103 A1AM6 B N3  1 
HETATM 2190 C C4  . A1AM6 J 4 .  ? 20.963  -15.435 -23.931 0.94 24.99  ? 103 A1AM6 B C4  1 
HETATM 2191 C C5  . A1AM6 J 4 .  ? 19.831  -17.063 -22.546 0.94 25.14  ? 103 A1AM6 B C5  1 
HETATM 2192 C C6  . A1AM6 J 4 .  ? 18.675  -17.087 -23.520 0.94 21.96  ? 103 A1AM6 B C6  1 
HETATM 2193 C C7  . A1AM6 J 4 .  ? 22.302  -17.171 -22.789 0.94 29.27  ? 103 A1AM6 B C7  1 
HETATM 2194 C C8  . A1AM6 J 4 .  ? 24.553  -17.001 -22.814 0.94 35.85  ? 103 A1AM6 B C8  1 
HETATM 2195 C C10 . A1AM6 J 4 .  ? 23.508  -18.658 -21.549 0.94 35.50  ? 103 A1AM6 B C10 1 
HETATM 2196 N N   . A1AM6 J 4 .  ? 18.576  -15.815 -24.286 0.94 22.23  ? 103 A1AM6 B N   1 
HETATM 2197 C C   . A1AM6 J 4 .  ? 16.113  -15.581 -24.475 0.94 25.21  ? 103 A1AM6 B C   1 
HETATM 2198 C C1  . A1AM6 J 4 .  ? 17.438  -15.752 -25.224 0.94 21.05  ? 103 A1AM6 B C1  1 
HETATM 2199 C C2  . A1AM6 J 4 .  ? 17.426  -16.904 -26.262 0.94 20.65  ? 103 A1AM6 B C2  1 
HETATM 2200 C C3  . A1AM6 J 4 .  ? 19.852  -15.519 -24.967 0.94 22.30  ? 103 A1AM6 B C3  1 
HETATM 2201 C C9  . A1AM6 J 4 .  ? 24.680  -18.079 -21.961 0.94 39.39  ? 103 A1AM6 B C9  1 
HETATM 2202 N N2  . A1AM6 J 4 .  ? 23.373  -16.522 -23.238 0.94 29.00  ? 103 A1AM6 B N2  1 
HETATM 2203 S S   . SO4   K 2 .  ? 29.182  -38.147 12.325  1.00 96.68  ? 101 SO4   C S   1 
HETATM 2204 O O1  . SO4   K 2 .  ? 30.412  -37.695 11.725  1.00 100.49 ? 101 SO4   C O1  1 
HETATM 2205 O O2  . SO4   K 2 .  ? 28.148  -37.177 12.083  1.00 91.20  ? 101 SO4   C O2  1 
HETATM 2206 O O3  . SO4   K 2 .  ? 28.800  -39.410 11.754  1.00 89.68  ? 101 SO4   C O3  1 
HETATM 2207 O O4  . SO4   K 2 .  ? 29.372  -38.303 13.745  1.00 98.74  ? 101 SO4   C O4  1 
HETATM 2208 N N1  . A1AM6 L 4 .  ? 17.650  -39.309 20.281  0.74 29.16  ? 102 A1AM6 C N1  1 
HETATM 2209 N N3  . A1AM6 L 4 .  ? 18.676  -41.307 20.755  0.74 32.12  ? 102 A1AM6 C N3  1 
HETATM 2210 C C4  . A1AM6 L 4 .  ? 17.036  -38.049 20.698  0.74 28.57  ? 102 A1AM6 C C4  1 
HETATM 2211 C C5  . A1AM6 L 4 .  ? 17.233  -39.723 18.938  0.74 32.04  ? 102 A1AM6 C C5  1 
HETATM 2212 C C6  . A1AM6 L 4 .  ? 16.500  -38.603 18.255  0.74 38.12  ? 102 A1AM6 C C6  1 
HETATM 2213 C C7  . A1AM6 L 4 .  ? 18.002  -40.234 21.206  0.74 31.86  ? 102 A1AM6 C C7  1 
HETATM 2214 C C8  . A1AM6 L 4 .  ? 18.152  -40.838 23.385  0.74 39.62  ? 102 A1AM6 C C8  1 
HETATM 2215 C C10 . A1AM6 L 4 .  ? 19.117  -42.150 21.705  0.74 37.42  ? 102 A1AM6 C C10 1 
HETATM 2216 N N   . A1AM6 L 4 .  ? 17.299  -37.386 18.371  0.74 28.16  ? 102 A1AM6 C N   1 
HETATM 2217 C C   . A1AM6 L 4 .  ? 18.789  -35.794 17.292  0.74 27.01  ? 102 A1AM6 C C   1 
HETATM 2218 C C1  . A1AM6 L 4 .  ? 17.350  -36.306 17.367  0.74 29.41  ? 102 A1AM6 C C1  1 
HETATM 2219 C C2  . A1AM6 L 4 .  ? 16.295  -35.216 17.538  0.74 30.78  ? 102 A1AM6 C C2  1 
HETATM 2220 C C3  . A1AM6 L 4 .  ? 17.452  -36.944 19.770  0.74 26.21  ? 102 A1AM6 C C3  1 
HETATM 2221 C C9  . A1AM6 L 4 .  ? 18.883  -41.961 23.049  0.74 37.45  ? 102 A1AM6 C C9  1 
HETATM 2222 N N2  . A1AM6 L 4 .  ? 17.703  -39.950 22.481  0.74 31.06  ? 102 A1AM6 C N2  1 
HETATM 2223 O O   . HOH   M 5 .  ? 8.543   -32.248 4.254   1.00 47.61  ? 201 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 5.774   -28.917 7.167   1.00 38.40  ? 202 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? -5.507  -13.513 -16.567 1.00 48.54  ? 203 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? 3.802   -34.518 4.481   1.00 52.82  ? 204 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? 3.859   -10.253 13.757  1.00 48.52  ? 205 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? -2.077  -30.975 -4.118  1.00 36.49  ? 206 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? -1.518  -34.059 0.317   1.00 43.77  ? 207 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? 11.126  -9.470  -13.122 1.00 50.99  ? 208 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? 10.911  -29.695 3.095   1.00 36.28  ? 209 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 17.379  -15.507 -20.753 1.00 32.33  ? 210 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 0.164   -33.847 4.971   1.00 52.48  ? 211 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 1.793   -25.141 -6.561  1.00 46.09  ? 212 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? 8.946   -18.333 -10.942 1.00 30.00  ? 213 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? 15.779  -24.578 1.946   1.00 33.99  ? 214 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? -6.803  -5.366  9.226   1.00 30.00  ? 215 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 19.765  -15.500 7.230   1.00 26.07  ? 216 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? 11.056  -23.633 9.892   1.00 35.43  ? 217 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 8.238   -18.035 -15.960 1.00 40.70  ? 218 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? 4.489   -7.849  1.218   1.00 30.76  ? 219 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 4.333   -3.578  -3.275  1.00 27.86  ? 220 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? -0.674  -29.225 10.138  1.00 49.87  ? 221 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 9.353   -22.800 -9.436  1.00 29.71  ? 222 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? -2.473  3.323   -2.190  1.00 38.50  ? 223 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? 1.720   -24.888 14.359  1.00 58.12  ? 224 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? 12.753  -11.927 8.279   1.00 49.71  ? 225 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? -3.873  -10.803 6.782   1.00 36.91  ? 226 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? 9.549   -6.043  -1.703  1.00 29.29  ? 227 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? 6.962   -10.573 -12.098 1.00 32.42  ? 228 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? 0.421   -10.523 -15.651 1.00 39.86  ? 229 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? 13.109  -8.751  -21.859 1.00 47.13  ? 230 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? -4.408  -21.194 6.122   1.00 37.93  ? 231 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? -11.307 -16.041 -3.617  1.00 44.84  ? 232 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? 18.869  -11.627 -18.826 1.00 42.27  ? 233 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? 8.837   -16.349 -13.054 1.00 31.34  ? 234 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? 8.872   -2.520  -0.536  1.00 57.98  ? 235 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? -7.994  -17.161 6.621   1.00 36.66  ? 236 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? 13.236  -12.004 -4.241  1.00 20.12  ? 237 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? 1.684   0.548   -7.462  1.00 31.69  ? 238 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? -2.793  -11.726 13.787  1.00 45.62  ? 239 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 17.100  -12.911 1.354   1.00 18.15  ? 240 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? -5.819  -15.856 -8.001  1.00 26.84  ? 241 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? 9.969   -13.159 9.587   1.00 37.57  ? 242 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? 1.818   -4.619  -10.174 1.00 33.17  ? 243 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 11.326  -16.614 -14.792 1.00 34.59  ? 244 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 12.939  -28.224 -4.539  1.00 44.10  ? 245 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? -1.842  -22.053 -0.512  1.00 23.10  ? 246 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? 11.483  -11.893 5.925   1.00 32.16  ? 247 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? 11.377  -12.394 -6.120  1.00 23.35  ? 248 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? -8.201  -15.738 -0.947  1.00 31.47  ? 249 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? -5.920  -19.759 -5.547  1.00 30.99  ? 250 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? -0.754  -20.880 7.112   1.00 30.44  ? 251 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? 10.821  -5.177  -7.800  1.00 30.44  ? 252 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? 15.251  -28.031 -0.580  1.00 51.10  ? 253 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? -6.281  -11.640 -11.305 1.00 37.45  ? 254 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? -8.033  -16.697 1.838   1.00 36.03  ? 255 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 15.568  -12.150 -5.390  1.00 28.67  ? 256 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? 3.153   -29.559 -0.471  1.00 36.33  ? 257 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? 12.920  -9.557  -7.197  1.00 41.19  ? 258 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? -1.639  -7.878  -16.718 1.00 52.34  ? 259 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? 8.079   -17.490 8.661   1.00 37.89  ? 260 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? 0.755   -17.829 -19.026 1.00 49.88  ? 261 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 9.680   -30.563 9.691   1.00 28.28  ? 262 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? 1.643   -10.450 11.811  1.00 33.52  ? 263 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? -1.497  -7.571  11.638  1.00 43.57  ? 264 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? -1.386  -11.795 11.325  1.00 33.62  ? 265 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? -0.629  -20.547 11.217  1.00 50.84  ? 266 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? 9.606   -20.397 -18.459 1.00 40.07  ? 267 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 12.557  -13.427 -8.461  1.00 34.65  ? 268 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? 2.462   -6.393  5.378   1.00 36.88  ? 269 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? -4.538  -25.847 -5.627  1.00 32.99  ? 270 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? 6.214   -15.970 -14.994 1.00 41.86  ? 271 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? -8.567  -21.124 -1.209  1.00 36.40  ? 272 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? -6.071  -12.798 6.848   1.00 33.40  ? 273 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? 0.081   -23.214 9.290   1.00 44.09  ? 274 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? 7.862   -7.840  1.256   1.00 27.00  ? 275 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? -7.262  -21.768 -5.873  1.00 44.83  ? 276 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 16.757  -12.312 -16.934 1.00 41.18  ? 277 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? -5.866  -17.500 -9.934  1.00 47.58  ? 278 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? 2.818   -9.954  -13.324 1.00 39.87  ? 279 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? 6.129   -5.831  0.428   1.00 38.13  ? 280 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? 14.887  -13.151 10.384  1.00 43.84  ? 281 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? 16.960  -18.400 -9.504  1.00 42.91  ? 282 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? 11.222  -6.182  -3.632  1.00 40.39  ? 283 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? 6.076   -0.830  -3.728  1.00 44.81  ? 284 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? -2.979  -21.034 -9.667  1.00 37.72  ? 285 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? 4.978   -7.523  3.974   1.00 32.57  ? 286 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? -4.139  -7.929  10.572  1.00 40.24  ? 287 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? -3.960  -26.581 7.533   1.00 54.51  ? 288 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? -7.333  -11.516 -7.955  1.00 27.80  ? 289 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? 10.981  -7.864  0.355   1.00 22.11  ? 290 HOH   A O   1 
HETATM 2313 O O   . HOH   M 5 .  ? 22.125  -16.653 -0.464  1.00 39.43  ? 291 HOH   A O   1 
HETATM 2314 O O   . HOH   M 5 .  ? -13.734 -25.407 -3.570  1.00 67.73  ? 292 HOH   A O   1 
HETATM 2315 O O   . HOH   M 5 .  ? 13.007  -15.326 -12.257 1.00 42.98  ? 293 HOH   A O   1 
HETATM 2316 O O   . HOH   M 5 .  ? 21.286  -16.723 -3.471  1.00 27.62  ? 294 HOH   A O   1 
HETATM 2317 O O   . HOH   M 5 .  ? 10.792  -27.736 -7.042  1.00 51.34  ? 295 HOH   A O   1 
HETATM 2318 O O   . HOH   M 5 .  ? -8.318  -19.600 -3.406  1.00 42.79  ? 296 HOH   A O   1 
HETATM 2319 O O   . HOH   M 5 .  ? 7.584   -29.809 -3.876  1.00 57.01  ? 297 HOH   A O   1 
HETATM 2320 O O   . HOH   M 5 .  ? -6.025  -26.772 3.439   1.00 43.46  ? 298 HOH   A O   1 
HETATM 2321 O O   . HOH   M 5 .  ? 1.201   -29.454 -7.062  1.00 45.37  ? 299 HOH   A O   1 
HETATM 2322 O O   . HOH   M 5 .  ? 8.982   -9.219  -13.760 1.00 33.86  ? 300 HOH   A O   1 
HETATM 2323 O O   . HOH   M 5 .  ? 17.219  -13.619 10.735  1.00 46.23  ? 301 HOH   A O   1 
HETATM 2324 O O   . HOH   M 5 .  ? -5.725  -23.586 -6.845  1.00 32.68  ? 302 HOH   A O   1 
HETATM 2325 O O   . HOH   M 5 .  ? 16.872  -10.107 -9.783  1.00 42.99  ? 303 HOH   A O   1 
HETATM 2326 O O   . HOH   M 5 .  ? 8.626   -12.850 12.520  1.00 46.06  ? 304 HOH   A O   1 
HETATM 2327 O O   . HOH   M 5 .  ? 4.893   -6.955  -10.989 1.00 43.56  ? 305 HOH   A O   1 
HETATM 2328 O O   . HOH   M 5 .  ? -10.161 -28.327 -1.689  1.00 55.98  ? 306 HOH   A O   1 
HETATM 2329 O O   . HOH   M 5 .  ? -7.421  -14.037 -9.341  1.00 33.82  ? 307 HOH   A O   1 
HETATM 2330 O O   . HOH   M 5 .  ? 7.004   -18.102 -14.075 1.00 71.13  ? 308 HOH   A O   1 
HETATM 2331 O O   . HOH   M 5 .  ? 11.059  -2.234  -0.976  1.00 43.31  ? 309 HOH   A O   1 
HETATM 2332 O O   . HOH   M 5 .  ? -6.235  -22.926 5.806   1.00 49.83  ? 310 HOH   A O   1 
HETATM 2333 O O   . HOH   M 5 .  ? -3.203  -21.540 7.962   1.00 39.13  ? 311 HOH   A O   1 
HETATM 2334 O O   . HOH   M 5 .  ? 7.989   -8.238  4.551   1.00 32.82  ? 312 HOH   A O   1 
HETATM 2335 O O   . HOH   M 5 .  ? -11.402 -13.467 -2.863  1.00 35.90  ? 313 HOH   A O   1 
HETATM 2336 O O   . HOH   M 5 .  ? -7.043  -19.108 8.408   1.00 49.12  ? 314 HOH   A O   1 
HETATM 2337 O O   . HOH   M 5 .  ? 4.586   -9.650  -11.402 1.00 38.61  ? 315 HOH   A O   1 
HETATM 2338 O O   . HOH   M 5 .  ? -5.183  -21.106 -7.914  1.00 44.52  ? 316 HOH   A O   1 
HETATM 2339 O O   . HOH   M 5 .  ? 4.910   -10.129 -17.803 1.00 53.20  ? 317 HOH   A O   1 
HETATM 2340 O O   . HOH   M 5 .  ? 4.653   -3.545  3.094   1.00 64.74  ? 318 HOH   A O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 27.966  -8.235  -29.083 1.00 39.05  ? 201 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 25.233  -5.226  -29.986 1.00 33.57  ? 202 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 30.732  -8.107  -30.014 1.00 44.08  ? 203 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 20.127  -22.251 -23.438 1.00 40.93  ? 204 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 9.965   -11.363 -38.008 1.00 42.11  ? 205 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 10.409  -16.806 -44.360 1.00 44.70  ? 206 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 26.172  -4.596  -33.501 1.00 44.24  ? 207 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 13.009  -4.578  -41.884 1.00 41.57  ? 208 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 26.236  -23.027 -31.046 1.00 31.90  ? 209 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 30.209  -12.753 -45.922 1.00 61.48  ? 210 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 7.133   -19.227 -35.107 1.00 41.77  ? 211 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 30.473  -19.818 -40.311 1.00 28.78  ? 212 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 8.805   -8.678  -16.446 1.00 33.91  ? 213 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 12.839  -26.278 -37.414 1.00 41.74  ? 214 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 1.691   -16.630 -32.526 1.00 45.52  ? 215 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 14.973  -17.689 -19.035 1.00 31.46  ? 216 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 34.740  -23.342 -30.037 1.00 46.27  ? 217 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 6.663   -12.199 -26.133 1.00 29.61  ? 218 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 22.118  3.441   -32.640 1.00 41.66  ? 219 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 19.037  -19.693 -19.231 1.00 45.73  ? 220 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 24.520  -1.730  -36.524 1.00 43.90  ? 221 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 4.587   -18.881 -25.511 1.00 48.64  ? 222 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 34.385  -17.466 -35.615 1.00 51.01  ? 223 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 11.240  -8.172  -41.471 1.00 41.82  ? 224 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 25.485  -5.979  -35.827 1.00 37.19  ? 225 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 10.616  -18.936 -33.033 1.00 24.73  ? 226 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 20.820  -13.338 -42.736 1.00 33.44  ? 227 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 17.996  -28.188 -27.287 1.00 48.12  ? 228 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 23.117  -5.416  -24.815 1.00 42.63  ? 229 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 23.329  -13.629 -22.098 1.00 45.12  ? 230 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 10.181  -19.789 -43.243 1.00 40.80  ? 231 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 3.125   -8.885  -27.153 1.00 46.93  ? 232 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 10.690  -21.885 -32.900 1.00 30.93  ? 233 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 16.773  -19.468 -28.826 1.00 20.03  ? 234 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 19.793  -7.942  -21.141 1.00 43.29  ? 235 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 32.282  -11.970 -41.658 1.00 43.42  ? 236 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 6.260   -7.527  -32.545 1.00 46.76  ? 237 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 14.377  -6.371  -41.078 1.00 37.70  ? 238 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 18.093  -3.637  -22.307 1.00 49.80  ? 239 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 18.176  -0.591  -38.421 1.00 24.59  ? 240 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 21.125  -3.329  -23.465 1.00 59.64  ? 241 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 22.669  -23.251 -28.749 1.00 37.80  ? 242 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 17.619  -19.847 -42.157 1.00 43.19  ? 243 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 20.687  -20.464 -21.210 1.00 37.95  ? 244 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 32.517  -18.933 -42.362 1.00 38.29  ? 245 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 8.377   -28.066 -38.317 1.00 45.99  ? 246 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 15.926  -26.363 -34.752 1.00 38.30  ? 247 HOH   B O   1 
HETATM 2388 O O   . HOH   N 5 .  ? 23.811  -4.291  -36.847 1.00 25.25  ? 248 HOH   B O   1 
HETATM 2389 O O   . HOH   N 5 .  ? 7.667   -12.510 -38.687 1.00 43.86  ? 249 HOH   B O   1 
HETATM 2390 O O   . HOH   N 5 .  ? 19.855  -25.586 -33.996 1.00 36.34  ? 250 HOH   B O   1 
HETATM 2391 O O   . HOH   N 5 .  ? 6.859   -21.019 -24.888 1.00 38.66  ? 251 HOH   B O   1 
HETATM 2392 O O   . HOH   N 5 .  ? 23.617  -2.382  -29.181 1.00 33.23  ? 252 HOH   B O   1 
HETATM 2393 O O   . HOH   N 5 .  ? 18.303  -25.952 -28.928 1.00 34.35  ? 253 HOH   B O   1 
HETATM 2394 O O   . HOH   N 5 .  ? 22.021  -24.175 -26.519 1.00 34.96  ? 254 HOH   B O   1 
HETATM 2395 O O   . HOH   N 5 .  ? 13.659  -22.218 -20.597 1.00 45.89  ? 255 HOH   B O   1 
HETATM 2396 O O   . HOH   N 5 .  ? 14.684  -24.535 -40.524 1.00 36.48  ? 256 HOH   B O   1 
HETATM 2397 O O   . HOH   N 5 .  ? 20.551  -10.138 -42.950 1.00 33.51  ? 257 HOH   B O   1 
HETATM 2398 O O   . HOH   N 5 .  ? 27.425  -10.452 -28.960 1.00 42.63  ? 258 HOH   B O   1 
HETATM 2399 O O   . HOH   N 5 .  ? 4.262   -19.253 -31.152 1.00 44.63  ? 259 HOH   B O   1 
HETATM 2400 O O   . HOH   N 5 .  ? 7.512   -8.131  -20.819 1.00 41.00  ? 260 HOH   B O   1 
HETATM 2401 O O   . HOH   N 5 .  ? 25.374  -27.094 -28.629 1.00 50.98  ? 261 HOH   B O   1 
HETATM 2402 O O   . HOH   N 5 .  ? 31.956  -21.190 -38.193 1.00 37.33  ? 262 HOH   B O   1 
HETATM 2403 O O   . HOH   N 5 .  ? 12.317  -4.932  -24.804 1.00 48.75  ? 263 HOH   B O   1 
HETATM 2404 O O   . HOH   N 5 .  ? 20.806  -25.283 -29.521 1.00 57.31  ? 264 HOH   B O   1 
HETATM 2405 O O   . HOH   N 5 .  ? 7.841   -18.388 -31.900 1.00 44.49  ? 265 HOH   B O   1 
HETATM 2406 O O   . HOH   N 5 .  ? 21.128  -6.514  -42.551 1.00 33.85  ? 266 HOH   B O   1 
HETATM 2407 O O   . HOH   N 5 .  ? 28.002  -17.502 -24.791 1.00 34.76  ? 267 HOH   B O   1 
HETATM 2408 O O   . HOH   N 5 .  ? 32.742  -23.047 -38.059 1.00 53.13  ? 268 HOH   B O   1 
HETATM 2409 O O   . HOH   N 5 .  ? 24.898  -6.679  -42.687 1.00 41.34  ? 269 HOH   B O   1 
HETATM 2410 O O   . HOH   N 5 .  ? 16.118  -29.610 -24.893 1.00 49.36  ? 270 HOH   B O   1 
HETATM 2411 O O   . HOH   N 5 .  ? 1.866   -13.207 -28.269 1.00 44.41  ? 271 HOH   B O   1 
HETATM 2412 O O   . HOH   N 5 .  ? 25.222  -8.427  -22.649 1.00 47.32  ? 272 HOH   B O   1 
HETATM 2413 O O   . HOH   N 5 .  ? 18.090  -15.853 -45.749 1.00 35.04  ? 273 HOH   B O   1 
HETATM 2414 O O   . HOH   N 5 .  ? 27.893  -2.141  -26.302 1.00 53.53  ? 274 HOH   B O   1 
HETATM 2415 O O   . HOH   N 5 .  ? 27.904  -24.808 -35.069 1.00 31.29  ? 275 HOH   B O   1 
HETATM 2416 O O   . HOH   N 5 .  ? 23.716  -10.946 -21.893 1.00 36.70  ? 276 HOH   B O   1 
HETATM 2417 O O   . HOH   N 5 .  ? 31.625  -12.007 -38.651 1.00 55.54  ? 277 HOH   B O   1 
HETATM 2418 O O   . HOH   N 5 .  ? 18.583  -13.325 -44.509 1.00 37.94  ? 278 HOH   B O   1 
HETATM 2419 O O   . HOH   N 5 .  ? 26.197  -0.290  -29.054 1.00 40.49  ? 279 HOH   B O   1 
HETATM 2420 O O   . HOH   N 5 .  ? 17.456  -0.604  -25.454 1.00 49.65  ? 280 HOH   B O   1 
HETATM 2421 O O   . HOH   N 5 .  ? 18.227  -23.301 -20.550 1.00 55.53  ? 281 HOH   B O   1 
HETATM 2422 O O   . HOH   N 5 .  ? 17.195  -9.731  -43.860 1.00 42.62  ? 282 HOH   B O   1 
HETATM 2423 O O   . HOH   N 5 .  ? 20.681  3.732   -32.906 1.00 28.12  ? 283 HOH   B O   1 
HETATM 2424 O O   . HOH   N 5 .  ? 23.141  -14.520 -43.117 1.00 42.43  ? 284 HOH   B O   1 
HETATM 2425 O O   . HOH   N 5 .  ? 18.458  4.408   -34.163 1.00 37.26  ? 285 HOH   B O   1 
HETATM 2426 O O   . HOH   N 5 .  ? 18.580  -16.996 -18.872 1.00 43.37  ? 286 HOH   B O   1 
HETATM 2427 O O   . HOH   N 5 .  ? 15.212  -8.062  -43.158 1.00 40.59  ? 287 HOH   B O   1 
HETATM 2428 O O   . HOH   N 5 .  ? 12.786  -20.190 -19.545 1.00 45.16  ? 288 HOH   B O   1 
HETATM 2429 O O   . HOH   N 5 .  ? 24.289  -4.262  -28.111 1.00 58.17  ? 289 HOH   B O   1 
HETATM 2430 O O   . HOH   N 5 .  ? 9.821   -6.307  -41.071 1.00 38.78  ? 290 HOH   B O   1 
HETATM 2431 O O   . HOH   N 5 .  ? 39.925  -13.957 -39.101 1.00 63.69  ? 291 HOH   B O   1 
HETATM 2432 O O   . HOH   N 5 .  ? 26.988  -22.949 -28.369 1.00 52.76  ? 292 HOH   B O   1 
HETATM 2433 O O   . HOH   N 5 .  ? 16.817  -25.681 -20.716 1.00 61.96  ? 293 HOH   B O   1 
HETATM 2434 O O   . HOH   N 5 .  ? 22.422  -23.490 -24.010 1.00 42.39  ? 294 HOH   B O   1 
HETATM 2435 O O   . HOH   N 5 .  ? 15.287  -18.665 -16.538 1.00 41.39  ? 295 HOH   B O   1 
HETATM 2436 O O   . HOH   N 5 .  ? 15.468  -21.966 -41.881 1.00 43.71  ? 296 HOH   B O   1 
HETATM 2437 O O   . HOH   N 5 .  ? 7.348   -9.941  -18.639 1.00 39.02  ? 297 HOH   B O   1 
HETATM 2438 O O   . HOH   N 5 .  ? 22.450  -29.335 -35.532 1.00 42.61  ? 298 HOH   B O   1 
HETATM 2439 O O   . HOH   N 5 .  ? 39.306  -19.597 -26.972 1.00 52.07  ? 299 HOH   B O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 16.408  -26.713 28.705  1.00 45.66  ? 201 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 14.133  -32.059 29.841  1.00 51.84  ? 202 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 20.096  -19.780 29.891  1.00 51.64  ? 203 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 8.745   -36.525 18.522  1.00 57.34  ? 204 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 7.445   -31.462 12.208  1.00 41.40  ? 205 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 16.495  -17.744 25.031  1.00 59.51  ? 206 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 26.974  -37.784 10.147  1.00 34.36  ? 207 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 33.277  -24.394 31.579  1.00 48.26  ? 208 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 14.743  -21.688 28.580  1.00 61.47  ? 209 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 17.628  -17.186 14.686  1.00 43.52  ? 210 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 26.491  -39.071 12.658  1.00 34.06  ? 211 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 21.692  -13.720 17.037  1.00 67.73  ? 212 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 5.620   -26.591 16.680  1.00 46.51  ? 213 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 19.119  -20.123 10.537  1.00 34.01  ? 214 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 31.156  -39.799 27.240  1.00 39.85  ? 215 HOH   C O   1 
HETATM 2455 O O   . HOH   O 5 .  ? 12.090  -28.703 28.160  1.00 52.69  ? 216 HOH   C O   1 
HETATM 2456 O O   . HOH   O 5 .  ? 17.362  -40.721 11.410  1.00 49.06  ? 217 HOH   C O   1 
HETATM 2457 O O   . HOH   O 5 .  ? 12.750  -31.524 8.276   1.00 30.07  ? 218 HOH   C O   1 
HETATM 2458 O O   . HOH   O 5 .  ? 23.155  -41.510 18.525  1.00 36.32  ? 219 HOH   C O   1 
HETATM 2459 O O   . HOH   O 5 .  ? 19.428  -26.729 3.529   1.00 46.35  ? 220 HOH   C O   1 
HETATM 2460 O O   . HOH   O 5 .  ? 9.458   -30.331 10.872  1.00 42.00  ? 221 HOH   C O   1 
HETATM 2461 O O   . HOH   O 5 .  ? 30.314  -17.421 9.619   1.00 43.42  ? 222 HOH   C O   1 
HETATM 2462 O O   . HOH   O 5 .  ? 25.876  -24.108 6.617   1.00 60.14  ? 223 HOH   C O   1 
HETATM 2463 O O   . HOH   O 5 .  ? 23.026  -18.499 21.604  1.00 42.80  ? 224 HOH   C O   1 
HETATM 2464 O O   . HOH   O 5 .  ? 30.215  -31.478 15.637  1.00 51.39  ? 225 HOH   C O   1 
HETATM 2465 O O   . HOH   O 5 .  ? 30.359  -29.221 12.215  1.00 49.73  ? 226 HOH   C O   1 
HETATM 2466 O O   . HOH   O 5 .  ? 28.118  -37.324 15.908  1.00 33.35  ? 227 HOH   C O   1 
HETATM 2467 O O   . HOH   O 5 .  ? 13.625  -37.363 13.395  1.00 44.26  ? 228 HOH   C O   1 
HETATM 2468 O O   . HOH   O 5 .  ? 15.807  -17.592 19.399  1.00 41.65  ? 229 HOH   C O   1 
HETATM 2469 O O   . HOH   O 5 .  ? 19.799  -41.898 12.071  1.00 25.28  ? 230 HOH   C O   1 
HETATM 2470 O O   . HOH   O 5 .  ? 25.720  -19.539 6.259   1.00 31.42  ? 231 HOH   C O   1 
HETATM 2471 O O   . HOH   O 5 .  ? 25.117  -31.436 10.732  1.00 32.55  ? 232 HOH   C O   1 
HETATM 2472 O O   . HOH   O 5 .  ? 15.153  -21.026 12.353  1.00 33.42  ? 233 HOH   C O   1 
HETATM 2473 O O   . HOH   O 5 .  ? 19.217  -42.943 18.345  1.00 47.58  ? 234 HOH   C O   1 
HETATM 2474 O O   . HOH   O 5 .  ? 22.067  -34.397 16.502  1.00 21.90  ? 235 HOH   C O   1 
HETATM 2475 O O   . HOH   O 5 .  ? 29.830  -39.823 31.355  1.00 30.21  ? 236 HOH   C O   1 
HETATM 2476 O O   . HOH   O 5 .  ? 5.790   -33.331 23.534  1.00 56.15  ? 237 HOH   C O   1 
HETATM 2477 O O   . HOH   O 5 .  ? 9.148   -18.787 23.912  1.00 40.11  ? 238 HOH   C O   1 
HETATM 2478 O O   . HOH   O 5 .  ? 25.720  -17.514 13.783  1.00 37.88  ? 239 HOH   C O   1 
HETATM 2479 O O   . HOH   O 5 .  ? 20.164  -40.864 39.564  1.00 61.04  ? 240 HOH   C O   1 
HETATM 2480 O O   . HOH   O 5 .  ? 31.813  -43.227 11.975  1.00 44.48  ? 241 HOH   C O   1 
HETATM 2481 O O   . HOH   O 5 .  ? 22.153  -28.552 11.068  1.00 27.11  ? 242 HOH   C O   1 
HETATM 2482 O O   . HOH   O 5 .  ? 25.601  -33.798 34.897  1.00 44.69  ? 243 HOH   C O   1 
HETATM 2483 O O   . HOH   O 5 .  ? 23.167  -37.952 10.122  1.00 32.36  ? 244 HOH   C O   1 
HETATM 2484 O O   . HOH   O 5 .  ? 16.400  -38.412 11.955  1.00 51.43  ? 245 HOH   C O   1 
HETATM 2485 O O   . HOH   O 5 .  ? 17.922  -21.205 12.971  1.00 40.79  ? 246 HOH   C O   1 
HETATM 2486 O O   . HOH   O 5 .  ? 14.917  -39.322 16.784  1.00 45.76  ? 247 HOH   C O   1 
HETATM 2487 O O   . HOH   O 5 .  ? 6.845   -17.934 10.861  1.00 37.15  ? 248 HOH   C O   1 
HETATM 2488 O O   . HOH   O 5 .  ? 28.107  -36.596 18.694  1.00 37.43  ? 249 HOH   C O   1 
HETATM 2489 O O   . HOH   O 5 .  ? 14.541  -39.567 23.237  1.00 49.78  ? 250 HOH   C O   1 
HETATM 2490 O O   . HOH   O 5 .  ? 20.802  -39.978 26.449  1.00 31.51  ? 251 HOH   C O   1 
HETATM 2491 O O   . HOH   O 5 .  ? 20.727  -28.791 8.505   1.00 29.19  ? 252 HOH   C O   1 
HETATM 2492 O O   . HOH   O 5 .  ? 31.491  -43.241 15.771  1.00 49.70  ? 253 HOH   C O   1 
HETATM 2493 O O   . HOH   O 5 .  ? 27.864  -15.077 12.780  1.00 52.17  ? 254 HOH   C O   1 
HETATM 2494 O O   . HOH   O 5 .  ? 19.858  -19.034 24.927  1.00 44.22  ? 255 HOH   C O   1 
HETATM 2495 O O   . HOH   O 5 .  ? 30.173  -32.514 18.212  1.00 35.85  ? 256 HOH   C O   1 
HETATM 2496 O O   . HOH   O 5 .  ? 20.880  -29.724 4.714   1.00 48.22  ? 257 HOH   C O   1 
HETATM 2497 O O   . HOH   O 5 .  ? 27.569  -37.402 25.187  1.00 37.74  ? 258 HOH   C O   1 
HETATM 2498 O O   . HOH   O 5 .  ? 30.548  -35.805 14.920  1.00 51.17  ? 259 HOH   C O   1 
HETATM 2499 O O   . HOH   O 5 .  ? 31.764  -34.044 25.753  1.00 43.86  ? 260 HOH   C O   1 
HETATM 2500 O O   . HOH   O 5 .  ? 30.688  -35.433 28.516  1.00 49.18  ? 261 HOH   C O   1 
HETATM 2501 O O   . HOH   O 5 .  ? 16.437  -33.467 28.858  1.00 48.83  ? 262 HOH   C O   1 
HETATM 2502 O O   . HOH   O 5 .  ? 14.330  -29.491 4.194   1.00 37.26  ? 263 HOH   C O   1 
HETATM 2503 O O   . HOH   O 5 .  ? 22.548  -39.495 24.209  1.00 58.25  ? 264 HOH   C O   1 
HETATM 2504 O O   . HOH   O 5 .  ? 25.489  -39.755 20.178  1.00 32.19  ? 265 HOH   C O   1 
HETATM 2505 O O   . HOH   O 5 .  ? 25.287  -18.060 21.301  1.00 50.30  ? 266 HOH   C O   1 
HETATM 2506 O O   . HOH   O 5 .  ? 14.401  -38.721 10.015  1.00 47.33  ? 267 HOH   C O   1 
HETATM 2507 O O   . HOH   O 5 .  ? 12.391  -38.561 24.129  1.00 42.16  ? 268 HOH   C O   1 
HETATM 2508 O O   . HOH   O 5 .  ? 23.749  -40.441 27.639  1.00 60.45  ? 269 HOH   C O   1 
HETATM 2509 O O   . HOH   O 5 .  ? 2.460   -28.831 13.556  1.00 48.12  ? 270 HOH   C O   1 
HETATM 2510 O O   . HOH   O 5 .  ? 16.684  -29.359 2.919   1.00 51.38  ? 271 HOH   C O   1 
HETATM 2511 O O   . HOH   O 5 .  ? 29.149  -22.056 25.543  1.00 64.13  ? 272 HOH   C O   1 
HETATM 2512 O O   . HOH   O 5 .  ? 20.425  -12.859 13.408  1.00 45.12  ? 273 HOH   C O   1 
HETATM 2513 O O   . HOH   O 5 .  ? 30.238  -25.267 32.377  1.00 47.53  ? 274 HOH   C O   1 
HETATM 2514 O O   . HOH   O 5 .  ? 28.010  -38.824 24.340  1.00 39.12  ? 275 HOH   C O   1 
HETATM 2515 O O   . HOH   O 5 .  ? 17.346  -36.368 29.712  1.00 53.75  ? 276 HOH   C O   1 
HETATM 2516 O O   . HOH   O 5 .  ? 12.001  -21.196 10.747  1.00 36.60  ? 277 HOH   C O   1 
HETATM 2517 O O   . HOH   O 5 .  ? 18.368  -34.820 41.961  1.00 60.87  ? 278 HOH   C O   1 
HETATM 2518 O O   . HOH   O 5 .  ? 29.237  -41.695 27.197  1.00 35.79  ? 279 HOH   C O   1 
HETATM 2519 O O   . HOH   O 5 .  ? 22.297  -13.851 13.071  1.00 47.86  ? 280 HOH   C O   1 
HETATM 2520 O O   . HOH   O 5 .  ? 23.772  -15.837 11.959  1.00 40.71  ? 281 HOH   C O   1 
HETATM 2521 O O   . HOH   O 5 .  ? 32.180  -39.225 29.945  1.00 40.01  ? 282 HOH   C O   1 
HETATM 2522 O O   . HOH   O 5 .  ? 30.679  -20.571 25.543  1.00 56.26  ? 283 HOH   C O   1 
HETATM 2523 O O   . HOH   O 5 .  ? 32.445  -39.727 16.543  1.00 59.00  ? 284 HOH   C O   1 
HETATM 2524 O O   . HOH   O 5 .  ? 25.794  -33.476 10.011  1.00 48.66  ? 285 HOH   C O   1 
HETATM 2525 O O   . HOH   O 5 .  ? 37.538  -24.304 26.551  1.00 58.97  ? 286 HOH   C O   1 
HETATM 2526 O O   . HOH   O 5 .  ? 28.419  -41.517 29.871  1.00 34.80  ? 287 HOH   C O   1 
HETATM 2527 O O   . HOH   O 5 .  ? 24.268  -29.194 9.430   1.00 39.04  ? 288 HOH   C O   1 
HETATM 2528 O O   . HOH   O 5 .  ? 33.503  -44.439 15.197  1.00 32.03  ? 289 HOH   C O   1 
HETATM 2529 O O   . HOH   O 5 .  ? 28.651  -17.589 28.502  1.00 58.96  ? 290 HOH   C O   1 
HETATM 2530 O O   . HOH   O 5 .  ? 4.523   -24.543 18.062  1.00 54.21  ? 291 HOH   C O   1 
HETATM 2531 O O   . HOH   O 5 .  ? 29.817  -40.344 19.021  1.00 51.18  ? 292 HOH   C O   1 
HETATM 2532 O O   . HOH   O 5 .  ? 0.850   -21.140 17.684  1.00 59.22  ? 293 HOH   C O   1 
# 
